data_4N4N
# 
_entry.id   4N4N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.339 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4N4N         
RCSB  RCSB082746   
WWPDB D_1000082746 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4N4J . unspecified 
PDB 4N4K . unspecified 
PDB 4N4L . unspecified 
PDB 4N4M . unspecified 
PDB 4N4O . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4N4N 
_pdbx_database_status.recvd_initial_deposition_date   2013-10-08 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Maalcke, W.J.'     1 
'Dietl, A.'         2 
'Marritt, S.J.'     3 
'Butt, J.N.'        4 
'Jetten, M.S.M.'    5 
'Keltjens, J.T.'    6 
'Barends, T.R.M.B.' 7 
'Kartal, B.'        8 
# 
_citation.id                        primary 
_citation.title                     'Structural Basis of Biological NO Generation by Octaheme Oxidoreductases.' 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            289 
_citation.page_first                1228 
_citation.page_last                 1242 
_citation.year                      2014 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24302732 
_citation.pdbx_database_id_DOI      10.1074/jbc.M113.525147 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Maalcke, W.J.'  1 ? 
primary 'Dietl, A.'      2 ? 
primary 'Marritt, S.J.'  3 ? 
primary 'Butt, J.N.'     4 ? 
primary 'Jetten, M.S.'   5 ? 
primary 'Keltjens, J.T.' 6 ? 
primary 'Barends, T.R.'  7 ? 
primary 'Kartal, B.'     8 ? 
# 
_cell.entry_id           4N4N 
_cell.length_a           140.720 
_cell.length_b           141.970 
_cell.length_c           106.720 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4N4N 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'Hydroxylamine oxidoreductase' 61720.473 3    1.7.2.6 ? 'UNP residues 25-528' ? 
2 polymer     nat 'hydroxylamine oxidoreductase' 6182.173  3    1.7.2.6 ? 'UNP residues 28-84'  ? 
3 non-polymer syn 'HEME C'                       618.503   24   ?       ? ?                     ? 
4 non-polymer syn 'POTASSIUM ION'                39.098    1    ?       ? ?                     ? 
5 non-polymer syn 'PHOSPHATE ION'                94.971    1    ?       ? ?                     ? 
6 water       nat water                          18.015    1094 ?       ? ?                     ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        HAO 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;DISTVPDETYDALKLDRGKATPKETYEALVKRYKDPAHGAGKGTMGDYWEPIAISIYMDPNTFYKPPVSPKEVAERKDCV
ECHSDETPVWVRAWKRSTHANLDKIRNLKSDDPLYYKKGKLEEVENNLRSMGKLGEKETLKEVGCIDCHVDVNKKDKADH
TKDIRMPTADTCGTCHLREFAERESERDTMVWPNGQWPAGRPSHALDYTANIETTVWAAMPQREVAEGCTMCHTNQNKCD
NCHTRHEFSAAESRKPEACATCHSGVDHNNWEAYTMSKHGKLAEMNRDKWNWEVRLKDAFSKGGQNAPTCAACHMEYEGE
YTHNITRKTRWANYPFVPGIAENITSDWSEARLDSWVLTCTQCHSERFARSYLDLMDKGTLEGLAKYQEANAIVHKMYED
GTLTGQKTNRPNPPEPEKPGFGIFTQLFWSKGNNPASLELKVLEMAENNLAKMHVGLAHVNPGGWTYTEGWGPMNRAYVE
IQDEYTKMQELSALQARVNKLEGKQTSLLDLKGTGEKISLGGLGGGMLLAGALALIGWRKRKQTRA
;
;DISTVPDETYDALKLDRGKATPKETYEALVKRYKDPAHGAGKGTMGDYWEPIAISIYMDPNTFYKPPVSPKEVAERKDCV
ECHSDETPVWVRAWKRSTHANLDKIRNLKSDDPLYYKKGKLEEVENNLRSMGKLGEKETLKEVGCIDCHVDVNKKDKADH
TKDIRMPTADTCGTCHLREFAERESERDTMVWPNGQWPAGRPSHALDYTANIETTVWAAMPQREVAEGCTMCHTNQNKCD
NCHTRHEFSAAESRKPEACATCHSGVDHNNWEAYTMSKHGKLAEMNRDKWNWEVRLKDAFSKGGQNAPTCAACHMEYEGE
YTHNITRKTRWANYPFVPGIAENITSDWSEARLDSWVLTCTQCHSERFARSYLDLMDKGTLEGLAKYQEANAIVHKMYED
GTLTGQKTNRPNPPEPEKPGFGIFTQLFWSKGNNPASLELKVLEMAENNLAKMHVGLAHVNPGGWTYTEGWGPMNRAYVE
IQDEYTKMQELSALQARVNKLEGKQTSLLDLKGTGEKISLGGLGGGMLLAGALALIGWRKRKQTRA
;
A,C,E ? 
2 'polypeptide(L)' no no SSLAPISAKDMLDYLACKDKKPTDVVKSHTEVENGKIVRVKCGDIVALVQKAREQSG 
SSLAPISAKDMLDYLACKDKKPTDVVKSHTEVENGKIVRVKCGDIVALVQKAREQSG B,D,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   ILE n 
1 3   SER n 
1 4   THR n 
1 5   VAL n 
1 6   PRO n 
1 7   ASP n 
1 8   GLU n 
1 9   THR n 
1 10  TYR n 
1 11  ASP n 
1 12  ALA n 
1 13  LEU n 
1 14  LYS n 
1 15  LEU n 
1 16  ASP n 
1 17  ARG n 
1 18  GLY n 
1 19  LYS n 
1 20  ALA n 
1 21  THR n 
1 22  PRO n 
1 23  LYS n 
1 24  GLU n 
1 25  THR n 
1 26  TYR n 
1 27  GLU n 
1 28  ALA n 
1 29  LEU n 
1 30  VAL n 
1 31  LYS n 
1 32  ARG n 
1 33  TYR n 
1 34  LYS n 
1 35  ASP n 
1 36  PRO n 
1 37  ALA n 
1 38  HIS n 
1 39  GLY n 
1 40  ALA n 
1 41  GLY n 
1 42  LYS n 
1 43  GLY n 
1 44  THR n 
1 45  MET n 
1 46  GLY n 
1 47  ASP n 
1 48  TYR n 
1 49  TRP n 
1 50  GLU n 
1 51  PRO n 
1 52  ILE n 
1 53  ALA n 
1 54  ILE n 
1 55  SER n 
1 56  ILE n 
1 57  TYR n 
1 58  MET n 
1 59  ASP n 
1 60  PRO n 
1 61  ASN n 
1 62  THR n 
1 63  PHE n 
1 64  TYR n 
1 65  LYS n 
1 66  PRO n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PRO n 
1 71  LYS n 
1 72  GLU n 
1 73  VAL n 
1 74  ALA n 
1 75  GLU n 
1 76  ARG n 
1 77  LYS n 
1 78  ASP n 
1 79  CYS n 
1 80  VAL n 
1 81  GLU n 
1 82  CYS n 
1 83  HIS n 
1 84  SER n 
1 85  ASP n 
1 86  GLU n 
1 87  THR n 
1 88  PRO n 
1 89  VAL n 
1 90  TRP n 
1 91  VAL n 
1 92  ARG n 
1 93  ALA n 
1 94  TRP n 
1 95  LYS n 
1 96  ARG n 
1 97  SER n 
1 98  THR n 
1 99  HIS n 
1 100 ALA n 
1 101 ASN n 
1 102 LEU n 
1 103 ASP n 
1 104 LYS n 
1 105 ILE n 
1 106 ARG n 
1 107 ASN n 
1 108 LEU n 
1 109 LYS n 
1 110 SER n 
1 111 ASP n 
1 112 ASP n 
1 113 PRO n 
1 114 LEU n 
1 115 TYR n 
1 116 TYR n 
1 117 LYS n 
1 118 LYS n 
1 119 GLY n 
1 120 LYS n 
1 121 LEU n 
1 122 GLU n 
1 123 GLU n 
1 124 VAL n 
1 125 GLU n 
1 126 ASN n 
1 127 ASN n 
1 128 LEU n 
1 129 ARG n 
1 130 SER n 
1 131 MET n 
1 132 GLY n 
1 133 LYS n 
1 134 LEU n 
1 135 GLY n 
1 136 GLU n 
1 137 LYS n 
1 138 GLU n 
1 139 THR n 
1 140 LEU n 
1 141 LYS n 
1 142 GLU n 
1 143 VAL n 
1 144 GLY n 
1 145 CYS n 
1 146 ILE n 
1 147 ASP n 
1 148 CYS n 
1 149 HIS n 
1 150 VAL n 
1 151 ASP n 
1 152 VAL n 
1 153 ASN n 
1 154 LYS n 
1 155 LYS n 
1 156 ASP n 
1 157 LYS n 
1 158 ALA n 
1 159 ASP n 
1 160 HIS n 
1 161 THR n 
1 162 LYS n 
1 163 ASP n 
1 164 ILE n 
1 165 ARG n 
1 166 MET n 
1 167 PRO n 
1 168 THR n 
1 169 ALA n 
1 170 ASP n 
1 171 THR n 
1 172 CYS n 
1 173 GLY n 
1 174 THR n 
1 175 CYS n 
1 176 HIS n 
1 177 LEU n 
1 178 ARG n 
1 179 GLU n 
1 180 PHE n 
1 181 ALA n 
1 182 GLU n 
1 183 ARG n 
1 184 GLU n 
1 185 SER n 
1 186 GLU n 
1 187 ARG n 
1 188 ASP n 
1 189 THR n 
1 190 MET n 
1 191 VAL n 
1 192 TRP n 
1 193 PRO n 
1 194 ASN n 
1 195 GLY n 
1 196 GLN n 
1 197 TRP n 
1 198 PRO n 
1 199 ALA n 
1 200 GLY n 
1 201 ARG n 
1 202 PRO n 
1 203 SER n 
1 204 HIS n 
1 205 ALA n 
1 206 LEU n 
1 207 ASP n 
1 208 TYR n 
1 209 THR n 
1 210 ALA n 
1 211 ASN n 
1 212 ILE n 
1 213 GLU n 
1 214 THR n 
1 215 THR n 
1 216 VAL n 
1 217 TRP n 
1 218 ALA n 
1 219 ALA n 
1 220 MET n 
1 221 PRO n 
1 222 GLN n 
1 223 ARG n 
1 224 GLU n 
1 225 VAL n 
1 226 ALA n 
1 227 GLU n 
1 228 GLY n 
1 229 CYS n 
1 230 THR n 
1 231 MET n 
1 232 CYS n 
1 233 HIS n 
1 234 THR n 
1 235 ASN n 
1 236 GLN n 
1 237 ASN n 
1 238 LYS n 
1 239 CYS n 
1 240 ASP n 
1 241 ASN n 
1 242 CYS n 
1 243 HIS n 
1 244 THR n 
1 245 ARG n 
1 246 HIS n 
1 247 GLU n 
1 248 PHE n 
1 249 SER n 
1 250 ALA n 
1 251 ALA n 
1 252 GLU n 
1 253 SER n 
1 254 ARG n 
1 255 LYS n 
1 256 PRO n 
1 257 GLU n 
1 258 ALA n 
1 259 CYS n 
1 260 ALA n 
1 261 THR n 
1 262 CYS n 
1 263 HIS n 
1 264 SER n 
1 265 GLY n 
1 266 VAL n 
1 267 ASP n 
1 268 HIS n 
1 269 ASN n 
1 270 ASN n 
1 271 TRP n 
1 272 GLU n 
1 273 ALA n 
1 274 TYR n 
1 275 THR n 
1 276 MET n 
1 277 SER n 
1 278 LYS n 
1 279 HIS n 
1 280 GLY n 
1 281 LYS n 
1 282 LEU n 
1 283 ALA n 
1 284 GLU n 
1 285 MET n 
1 286 ASN n 
1 287 ARG n 
1 288 ASP n 
1 289 LYS n 
1 290 TRP n 
1 291 ASN n 
1 292 TRP n 
1 293 GLU n 
1 294 VAL n 
1 295 ARG n 
1 296 LEU n 
1 297 LYS n 
1 298 ASP n 
1 299 ALA n 
1 300 PHE n 
1 301 SER n 
1 302 LYS n 
1 303 GLY n 
1 304 GLY n 
1 305 GLN n 
1 306 ASN n 
1 307 ALA n 
1 308 PRO n 
1 309 THR n 
1 310 CYS n 
1 311 ALA n 
1 312 ALA n 
1 313 CYS n 
1 314 HIS n 
1 315 MET n 
1 316 GLU n 
1 317 TYR n 
1 318 GLU n 
1 319 GLY n 
1 320 GLU n 
1 321 TYR n 
1 322 THR n 
1 323 HIS n 
1 324 ASN n 
1 325 ILE n 
1 326 THR n 
1 327 ARG n 
1 328 LYS n 
1 329 THR n 
1 330 ARG n 
1 331 TRP n 
1 332 ALA n 
1 333 ASN n 
1 334 TYR n 
1 335 PRO n 
1 336 PHE n 
1 337 VAL n 
1 338 PRO n 
1 339 GLY n 
1 340 ILE n 
1 341 ALA n 
1 342 GLU n 
1 343 ASN n 
1 344 ILE n 
1 345 THR n 
1 346 SER n 
1 347 ASP n 
1 348 TRP n 
1 349 SER n 
1 350 GLU n 
1 351 ALA n 
1 352 ARG n 
1 353 LEU n 
1 354 ASP n 
1 355 SER n 
1 356 TRP n 
1 357 VAL n 
1 358 LEU n 
1 359 THR n 
1 360 CYS n 
1 361 THR n 
1 362 GLN n 
1 363 CYS n 
1 364 HIS n 
1 365 SER n 
1 366 GLU n 
1 367 ARG n 
1 368 PHE n 
1 369 ALA n 
1 370 ARG n 
1 371 SER n 
1 372 TYR n 
1 373 LEU n 
1 374 ASP n 
1 375 LEU n 
1 376 MET n 
1 377 ASP n 
1 378 LYS n 
1 379 GLY n 
1 380 THR n 
1 381 LEU n 
1 382 GLU n 
1 383 GLY n 
1 384 LEU n 
1 385 ALA n 
1 386 LYS n 
1 387 TYR n 
1 388 GLN n 
1 389 GLU n 
1 390 ALA n 
1 391 ASN n 
1 392 ALA n 
1 393 ILE n 
1 394 VAL n 
1 395 HIS n 
1 396 LYS n 
1 397 MET n 
1 398 TYR n 
1 399 GLU n 
1 400 ASP n 
1 401 GLY n 
1 402 THR n 
1 403 LEU n 
1 404 THR n 
1 405 GLY n 
1 406 GLN n 
1 407 LYS n 
1 408 THR n 
1 409 ASN n 
1 410 ARG n 
1 411 PRO n 
1 412 ASN n 
1 413 PRO n 
1 414 PRO n 
1 415 GLU n 
1 416 PRO n 
1 417 GLU n 
1 418 LYS n 
1 419 PRO n 
1 420 GLY n 
1 421 PHE n 
1 422 GLY n 
1 423 ILE n 
1 424 PHE n 
1 425 THR n 
1 426 GLN n 
1 427 LEU n 
1 428 PHE n 
1 429 TRP n 
1 430 SER n 
1 431 LYS n 
1 432 GLY n 
1 433 ASN n 
1 434 ASN n 
1 435 PRO n 
1 436 ALA n 
1 437 SER n 
1 438 LEU n 
1 439 GLU n 
1 440 LEU n 
1 441 LYS n 
1 442 VAL n 
1 443 LEU n 
1 444 GLU n 
1 445 MET n 
1 446 ALA n 
1 447 GLU n 
1 448 ASN n 
1 449 ASN n 
1 450 LEU n 
1 451 ALA n 
1 452 LYS n 
1 453 MET n 
1 454 HIS n 
1 455 VAL n 
1 456 GLY n 
1 457 LEU n 
1 458 ALA n 
1 459 HIS n 
1 460 VAL n 
1 461 ASN n 
1 462 PRO n 
1 463 GLY n 
1 464 GLY n 
1 465 TRP n 
1 466 THR n 
1 467 TYR n 
1 468 THR n 
1 469 GLU n 
1 470 GLY n 
1 471 TRP n 
1 472 GLY n 
1 473 PRO n 
1 474 MET n 
1 475 ASN n 
1 476 ARG n 
1 477 ALA n 
1 478 TYR n 
1 479 VAL n 
1 480 GLU n 
1 481 ILE n 
1 482 GLN n 
1 483 ASP n 
1 484 GLU n 
1 485 TYR n 
1 486 THR n 
1 487 LYS n 
1 488 MET n 
1 489 GLN n 
1 490 GLU n 
1 491 LEU n 
1 492 SER n 
1 493 ALA n 
1 494 LEU n 
1 495 GLN n 
1 496 ALA n 
1 497 ARG n 
1 498 VAL n 
1 499 ASN n 
1 500 LYS n 
1 501 LEU n 
1 502 GLU n 
1 503 GLY n 
1 504 LYS n 
1 505 GLN n 
1 506 THR n 
1 507 SER n 
1 508 LEU n 
1 509 LEU n 
1 510 ASP n 
1 511 LEU n 
1 512 LYS n 
1 513 GLY n 
1 514 THR n 
1 515 GLY n 
1 516 GLU n 
1 517 LYS n 
1 518 ILE n 
1 519 SER n 
1 520 LEU n 
1 521 GLY n 
1 522 GLY n 
1 523 LEU n 
1 524 GLY n 
1 525 GLY n 
1 526 GLY n 
1 527 MET n 
1 528 LEU n 
1 529 LEU n 
1 530 ALA n 
1 531 GLY n 
1 532 ALA n 
1 533 LEU n 
1 534 ALA n 
1 535 LEU n 
1 536 ILE n 
1 537 GLY n 
1 538 TRP n 
1 539 ARG n 
1 540 LYS n 
1 541 ARG n 
1 542 LYS n 
1 543 GLN n 
1 544 THR n 
1 545 ARG n 
1 546 ALA n 
2 1   SER n 
2 2   SER n 
2 3   LEU n 
2 4   ALA n 
2 5   PRO n 
2 6   ILE n 
2 7   SER n 
2 8   ALA n 
2 9   LYS n 
2 10  ASP n 
2 11  MET n 
2 12  LEU n 
2 13  ASP n 
2 14  TYR n 
2 15  LEU n 
2 16  ALA n 
2 17  CYS n 
2 18  LYS n 
2 19  ASP n 
2 20  LYS n 
2 21  LYS n 
2 22  PRO n 
2 23  THR n 
2 24  ASP n 
2 25  VAL n 
2 26  VAL n 
2 27  LYS n 
2 28  SER n 
2 29  HIS n 
2 30  THR n 
2 31  GLU n 
2 32  VAL n 
2 33  GLU n 
2 34  ASN n 
2 35  GLY n 
2 36  LYS n 
2 37  ILE n 
2 38  VAL n 
2 39  ARG n 
2 40  VAL n 
2 41  LYS n 
2 42  CYS n 
2 43  GLY n 
2 44  ASP n 
2 45  ILE n 
2 46  VAL n 
2 47  ALA n 
2 48  LEU n 
2 49  VAL n 
2 50  GLN n 
2 51  LYS n 
2 52  ALA n 
2 53  ARG n 
2 54  GLU n 
2 55  GLN n 
2 56  SER n 
2 57  GLY n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample ? ? ? 'Nitrosomonas europaea' 915 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample ? ? ? 'Nitrosomonas europaea' 915 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP HAO_NITEU    Q50925 1 
;DISTVPDETYDALKLDRGKATPKETYEALVKRYKDPAHGAGKGTMGDYWEPIAISIYMDPNTFYKPPVSPKEVAERKDCV
ECHSDETPVWVRAWKRSTHANLDKIRNLKSDDPLYYKKGKLEEVENNLRSMGKLGEKETLKEVGCIDCHVDVNKKDKADH
TKDIRMPTADTCGTCHLREFAERESERDTMVWPNGQWPAGRPSHALDYTANIETTVWAAMPQREVAEGCTMCHTNQNKCD
NCHTRHEFSAAESRKPEACATCHSGVDHNNWEAYTMSKHGKLAEMNRDKWNWEVRLKDAFSKGGQNAPTCAACHMEYEGE
YTHNITRKTRWANYPFVPGIAENITSDWSEARLDSWVLTCTQCHSERFARSYLDLMDKGTLEGLAKYQEANAIVHKMYED
GTLTGQKTNRPNPPEPEKPGFGIFTQLFWSKGNNPASLELKVLEMAENNLAKMHVGLAHVNPGGWTYTEGWGPMNRAYVE
IQDEYTKMQELSALQARVNKLEGKQTSLLDLKGTGEKISLGGLGGGMLLAGALALIGWRKRKQTRA
;
25 ? 
2 UNP Q82V11_NITEU Q82V11 2 SSLAPISAKDMLDYLACKDKKPTDVVKSHTEVENGKIVRVKCGDIVALVQKAREQSG 28 ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4N4N A 1 ? 546 ? Q50925 25 ? 570 ? 25 570 
2 2 4N4N B 1 ? 57  ? Q82V11 28 ? 84  ? 28 84  
3 1 4N4N C 1 ? 546 ? Q50925 25 ? 570 ? 25 570 
4 2 4N4N D 1 ? 57  ? Q82V11 28 ? 84  ? 28 84  
5 1 4N4N E 1 ? 546 ? Q50925 25 ? 570 ? 25 570 
6 2 4N4N F 1 ? 57  ? Q82V11 28 ? 84  ? 28 84  
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'       75.067  
HEC non-polymer         . 'HEME C'        ? 'C34 H34 Fe N4 O4' 618.503 
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER           ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'      131.173 
K   non-polymer         . 'POTASSIUM ION' ? 'K 1'              39.098  
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'      165.189 
PO4 non-polymer         . 'PHOSPHATE ION' ? 'O4 P -3'          94.971  
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'      117.146 
# 
_exptl.entry_id          4N4N 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.78 
_exptl_crystal.density_percent_sol   55.82 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'MICROBATCH UNDER OIL' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    
'42% v/v PEG400, 50 mM potassium nitrate, 100 mM MES/NaOH, pH 7.5, MICROBATCH UNDER OIL, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'PSI PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2012-12-01 
_diffrn_detector.details                'two horizontal deflecting and one vertical deflecting X-ray mirror' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'double crystal Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9786 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, DESY BEAMLINE P11' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
# 
_reflns.entry_id                     4N4N 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50.40 
_reflns.d_resolution_high            2.2 
_reflns.number_obs                   98124 
_reflns.number_all                   98124 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.102 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.6 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.6 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.2 
_reflns_shell.d_res_low              2.3 
_reflns_shell.percent_possible_all   99.3 
_reflns_shell.Rmerge_I_obs           0.588 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4N4N 
_refine.ls_number_reflns_obs                     98124 
_refine.ls_number_reflns_all                     98124 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             50.40 
_refine.ls_d_res_high                            2.20 
_refine.ls_percent_reflns_obs                    99.97 
_refine.ls_R_factor_obs                          0.18246 
_refine.ls_R_factor_all                          0.18246 
_refine.ls_R_factor_R_work                       0.17928 
_refine.ls_R_factor_R_free                       0.21273 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.5 
_refine.ls_number_reflns_R_free                  10263 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.931 
_refine.B_iso_mean                               29.017 
_refine.aniso_B[1][1]                            -2.15 
_refine.aniso_B[2][2]                            0.26 
_refine.aniso_B[3][3]                            1.89 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB ENTRY 1FGJ' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.266 
_refine.pdbx_overall_ESU_R_Free                  0.192 
_refine.overall_SU_ML                            0.093 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.594 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        13309 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1038 
_refine_hist.number_atoms_solvent             1094 
_refine_hist.number_atoms_total               15441 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        50.40 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d             0.007  0.022  ? 14947 ? 'X-RAY DIFFRACTION' 
r_bond_other_d               ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg          1.025  2.144  ? 20416 ? 'X-RAY DIFFRACTION' 
r_angle_other_deg            ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg       5.055  5.000  ? 1674  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg       33.164 24.587 ? 654   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg       14.630 15.000 ? 2389  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg       17.906 15.000 ? 81    ? 'X-RAY DIFFRACTION' 
r_chiral_restr               0.070  0.200  ? 1954  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined         0.006  0.032  ? 11568 ? 'X-RAY DIFFRACTION' 
r_gen_planes_other           ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbd_refined                ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbd_other                  ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbtor_refined              ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbtor_other                ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined        ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_other          ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined          ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_metal_ion_other            ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined       ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_other         ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined     ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_other       ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_refined ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_other   ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_mcbond_it                  0.283  1.500  ? 8374  ? 'X-RAY DIFFRACTION' 
r_mcbond_other               ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_mcangle_it                 0.536  2.000  ? 13489 ? 'X-RAY DIFFRACTION' 
r_mcangle_other              ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_scbond_it                  0.723  3.000  ? 6573  ? 'X-RAY DIFFRACTION' 
r_scbond_other               ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_scangle_it                 1.124  4.500  ? 6927  ? 'X-RAY DIFFRACTION' 
r_scangle_other              ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_long_range_B_refined       ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_long_range_B_other         ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr           ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_sphericity_free            ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded          ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.200 
_refine_ls_shell.d_res_low                        2.257 
_refine_ls_shell.number_reflns_R_work             7111 
_refine_ls_shell.R_factor_R_work                  0.224 
_refine_ls_shell.percent_reflns_obs               99.94 
_refine_ls_shell.R_factor_R_free                  0.264 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             751 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4N4N 
_struct.title                     'Nitrosomonas europea HAO' 
_struct.pdbx_descriptor           'Hydroxylamine oxidoreductase (E.C.1.7.2.6), hydroxylamine oxidoreductase (E.C.1.7.2.6)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4N4N 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'C-type cytochrome, OXIDOREDUCTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 5 ? 
GA N N 6 ? 
HA N N 6 ? 
IA N N 6 ? 
JA N N 6 ? 
KA N N 6 ? 
LA N N 6 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  PRO A 6   ? LEU A 13  ? PRO A 30  LEU A 37  1 ? 8  
HELX_P HELX_P2  2  THR A 21  ? LYS A 34  ? THR A 45  LYS A 58  1 ? 14 
HELX_P HELX_P3  3  ASP A 35  ? GLY A 39  ? ASP A 59  GLY A 63  5 ? 5  
HELX_P HELX_P4  4  ILE A 54  ? ASP A 59  ? ILE A 78  ASP A 83  1 ? 6  
HELX_P HELX_P5  5  ASP A 59  ? TYR A 64  ? ASP A 83  TYR A 88  1 ? 6  
HELX_P HELX_P6  6  GLU A 75  ? THR A 87  ? GLU A 99  THR A 111 1 ? 13 
HELX_P HELX_P7  7  THR A 87  ? ARG A 96  ? THR A 111 ARG A 120 1 ? 10 
HELX_P HELX_P8  8  SER A 97  ? ALA A 100 ? SER A 121 ALA A 124 5 ? 4  
HELX_P HELX_P9  9  ASN A 101 ? ASN A 107 ? ASN A 125 ASN A 131 1 ? 7  
HELX_P HELX_P10 10 TYR A 115 ? MET A 131 ? TYR A 139 MET A 155 1 ? 17 
HELX_P HELX_P11 11 GLY A 144 ? VAL A 150 ? GLY A 168 VAL A 174 1 ? 7  
HELX_P HELX_P12 12 THR A 168 ? HIS A 176 ? THR A 192 HIS A 200 1 ? 9  
HELX_P HELX_P13 13 HIS A 176 ? SER A 185 ? HIS A 200 SER A 209 1 ? 10 
HELX_P HELX_P14 14 SER A 185 ? MET A 190 ? SER A 209 MET A 214 1 ? 6  
HELX_P HELX_P15 15 LEU A 206 ? GLU A 213 ? LEU A 230 GLU A 237 1 ? 8  
HELX_P HELX_P16 16 THR A 214 ? MET A 220 ? THR A 238 MET A 244 1 ? 7  
HELX_P HELX_P17 17 GLN A 222 ? CYS A 232 ? GLN A 246 CYS A 256 1 ? 11 
HELX_P HELX_P18 18 SER A 249 ? LYS A 255 ? SER A 273 LYS A 279 1 ? 7  
HELX_P HELX_P19 19 PRO A 256 ? ALA A 260 ? PRO A 280 ALA A 284 5 ? 5  
HELX_P HELX_P20 20 ASN A 269 ? SER A 277 ? ASN A 293 SER A 301 1 ? 9  
HELX_P HELX_P21 21 SER A 277 ? ARG A 287 ? SER A 301 ARG A 311 1 ? 11 
HELX_P HELX_P22 22 ARG A 295 ? ALA A 299 ? ARG A 319 ALA A 323 5 ? 5  
HELX_P HELX_P23 23 THR A 309 ? MET A 315 ? THR A 333 MET A 339 1 ? 7  
HELX_P HELX_P24 24 SER A 346 ? THR A 361 ? SER A 370 THR A 385 1 ? 16 
HELX_P HELX_P25 25 SER A 365 ? GLY A 401 ? SER A 389 GLY A 425 1 ? 37 
HELX_P HELX_P26 26 PHE A 424 ? TRP A 429 ? PHE A 448 TRP A 453 1 ? 6  
HELX_P HELX_P27 27 ALA A 436 ? ASN A 448 ? ALA A 460 ASN A 472 1 ? 13 
HELX_P HELX_P28 28 ASN A 448 ? HIS A 459 ? ASN A 472 HIS A 483 1 ? 12 
HELX_P HELX_P29 29 ASN A 461 ? TRP A 465 ? ASN A 485 TRP A 489 5 ? 5  
HELX_P HELX_P30 30 GLY A 470 ? GLU A 502 ? GLY A 494 GLU A 526 1 ? 33 
HELX_P HELX_P31 31 SER B 7   ? CYS B 17  ? SER B 34  CYS B 44  1 ? 11 
HELX_P HELX_P32 32 CYS B 42  ? GLU B 54  ? CYS B 69  GLU B 81  1 ? 13 
HELX_P HELX_P33 33 PRO C 6   ? LEU C 13  ? PRO C 30  LEU C 37  1 ? 8  
HELX_P HELX_P34 34 THR C 21  ? LYS C 34  ? THR C 45  LYS C 58  1 ? 14 
HELX_P HELX_P35 35 ASP C 35  ? GLY C 39  ? ASP C 59  GLY C 63  5 ? 5  
HELX_P HELX_P36 36 ILE C 54  ? ASP C 59  ? ILE C 78  ASP C 83  1 ? 6  
HELX_P HELX_P37 37 ASP C 59  ? TYR C 64  ? ASP C 83  TYR C 88  1 ? 6  
HELX_P HELX_P38 38 GLU C 75  ? THR C 87  ? GLU C 99  THR C 111 1 ? 13 
HELX_P HELX_P39 39 THR C 87  ? ARG C 96  ? THR C 111 ARG C 120 1 ? 10 
HELX_P HELX_P40 40 SER C 97  ? ALA C 100 ? SER C 121 ALA C 124 5 ? 4  
HELX_P HELX_P41 41 ASN C 101 ? ASN C 107 ? ASN C 125 ASN C 131 1 ? 7  
HELX_P HELX_P42 42 TYR C 115 ? MET C 131 ? TYR C 139 MET C 155 1 ? 17 
HELX_P HELX_P43 43 GLY C 144 ? VAL C 150 ? GLY C 168 VAL C 174 1 ? 7  
HELX_P HELX_P44 44 THR C 168 ? THR C 174 ? THR C 192 THR C 198 1 ? 7  
HELX_P HELX_P45 45 HIS C 176 ? SER C 185 ? HIS C 200 SER C 209 1 ? 10 
HELX_P HELX_P46 46 SER C 185 ? MET C 190 ? SER C 209 MET C 214 1 ? 6  
HELX_P HELX_P47 47 LEU C 206 ? GLU C 213 ? LEU C 230 GLU C 237 1 ? 8  
HELX_P HELX_P48 48 THR C 214 ? MET C 220 ? THR C 238 MET C 244 1 ? 7  
HELX_P HELX_P49 49 GLN C 222 ? CYS C 232 ? GLN C 246 CYS C 256 1 ? 11 
HELX_P HELX_P50 50 SER C 249 ? LYS C 255 ? SER C 273 LYS C 279 1 ? 7  
HELX_P HELX_P51 51 PRO C 256 ? ALA C 260 ? PRO C 280 ALA C 284 5 ? 5  
HELX_P HELX_P52 52 ASN C 269 ? SER C 277 ? ASN C 293 SER C 301 1 ? 9  
HELX_P HELX_P53 53 SER C 277 ? ARG C 287 ? SER C 301 ARG C 311 1 ? 11 
HELX_P HELX_P54 54 ARG C 295 ? PHE C 300 ? ARG C 319 PHE C 324 1 ? 6  
HELX_P HELX_P55 55 THR C 309 ? MET C 315 ? THR C 333 MET C 339 1 ? 7  
HELX_P HELX_P56 56 ALA C 341 ? THR C 345 ? ALA C 365 THR C 369 5 ? 5  
HELX_P HELX_P57 57 SER C 346 ? THR C 361 ? SER C 370 THR C 385 1 ? 16 
HELX_P HELX_P58 58 SER C 365 ? GLY C 401 ? SER C 389 GLY C 425 1 ? 37 
HELX_P HELX_P59 59 ILE C 423 ? PHE C 428 ? ILE C 447 PHE C 452 5 ? 6  
HELX_P HELX_P60 60 ALA C 436 ? ASN C 448 ? ALA C 460 ASN C 472 1 ? 13 
HELX_P HELX_P61 61 ASN C 448 ? HIS C 459 ? ASN C 472 HIS C 483 1 ? 12 
HELX_P HELX_P62 62 ASN C 461 ? TRP C 465 ? ASN C 485 TRP C 489 5 ? 5  
HELX_P HELX_P63 63 GLY C 470 ? LYS C 500 ? GLY C 494 LYS C 524 1 ? 31 
HELX_P HELX_P64 64 SER D 7   ? CYS D 17  ? SER D 34  CYS D 44  1 ? 11 
HELX_P HELX_P65 65 CYS D 42  ? SER D 56  ? CYS D 69  SER D 83  1 ? 15 
HELX_P HELX_P66 66 PRO E 6   ? LEU E 13  ? PRO E 30  LEU E 37  1 ? 8  
HELX_P HELX_P67 67 THR E 21  ? LYS E 34  ? THR E 45  LYS E 58  1 ? 14 
HELX_P HELX_P68 68 ASP E 35  ? GLY E 39  ? ASP E 59  GLY E 63  5 ? 5  
HELX_P HELX_P69 69 MET E 45  ? TRP E 49  ? MET E 69  TRP E 73  5 ? 5  
HELX_P HELX_P70 70 ILE E 54  ? ASP E 59  ? ILE E 78  ASP E 83  1 ? 6  
HELX_P HELX_P71 71 ASP E 59  ? TYR E 64  ? ASP E 83  TYR E 88  1 ? 6  
HELX_P HELX_P72 72 GLU E 75  ? THR E 87  ? GLU E 99  THR E 111 1 ? 13 
HELX_P HELX_P73 73 THR E 87  ? SER E 97  ? THR E 111 SER E 121 1 ? 11 
HELX_P HELX_P74 74 THR E 98  ? ALA E 100 ? THR E 122 ALA E 124 5 ? 3  
HELX_P HELX_P75 75 ASN E 101 ? ASN E 107 ? ASN E 125 ASN E 131 1 ? 7  
HELX_P HELX_P76 76 TYR E 115 ? MET E 131 ? TYR E 139 MET E 155 1 ? 17 
HELX_P HELX_P77 77 GLY E 144 ? VAL E 150 ? GLY E 168 VAL E 174 1 ? 7  
HELX_P HELX_P78 78 THR E 168 ? THR E 174 ? THR E 192 THR E 198 1 ? 7  
HELX_P HELX_P79 79 HIS E 176 ? SER E 185 ? HIS E 200 SER E 209 1 ? 10 
HELX_P HELX_P80 80 SER E 185 ? MET E 190 ? SER E 209 MET E 214 1 ? 6  
HELX_P HELX_P81 81 LEU E 206 ? GLU E 213 ? LEU E 230 GLU E 237 1 ? 8  
HELX_P HELX_P82 82 THR E 214 ? MET E 220 ? THR E 238 MET E 244 1 ? 7  
HELX_P HELX_P83 83 GLN E 222 ? CYS E 232 ? GLN E 246 CYS E 256 1 ? 11 
HELX_P HELX_P84 84 SER E 249 ? LYS E 255 ? SER E 273 LYS E 279 1 ? 7  
HELX_P HELX_P85 85 PRO E 256 ? THR E 261 ? PRO E 280 THR E 285 1 ? 6  
HELX_P HELX_P86 86 ASN E 269 ? SER E 277 ? ASN E 293 SER E 301 1 ? 9  
HELX_P HELX_P87 87 SER E 277 ? ARG E 287 ? SER E 301 ARG E 311 1 ? 11 
HELX_P HELX_P88 88 ARG E 295 ? ALA E 299 ? ARG E 319 ALA E 323 5 ? 5  
HELX_P HELX_P89 89 THR E 309 ? MET E 315 ? THR E 333 MET E 339 1 ? 7  
HELX_P HELX_P90 90 SER E 346 ? THR E 361 ? SER E 370 THR E 385 1 ? 16 
HELX_P HELX_P91 91 SER E 365 ? GLY E 401 ? SER E 389 GLY E 425 1 ? 37 
HELX_P HELX_P92 92 PHE E 424 ? TRP E 429 ? PHE E 448 TRP E 453 1 ? 6  
HELX_P HELX_P93 93 ALA E 436 ? ASN E 448 ? ALA E 460 ASN E 472 1 ? 13 
HELX_P HELX_P94 94 ASN E 448 ? HIS E 459 ? ASN E 472 HIS E 483 1 ? 12 
HELX_P HELX_P95 95 ASN E 461 ? TRP E 465 ? ASN E 485 TRP E 489 5 ? 5  
HELX_P HELX_P96 96 GLY E 470 ? GLY E 503 ? GLY E 494 GLY E 527 1 ? 34 
HELX_P HELX_P97 97 SER F 7   ? CYS F 17  ? SER F 34  CYS F 44  1 ? 11 
HELX_P HELX_P98 98 CYS F 42  ? GLN F 55  ? CYS F 69  GLN F 82  1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? B CYS 17  SG  ? ? ? 1_555 B  CYS 42  SG  ? ? B CYS 44  B CYS 69  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf2  disulf ?    ? D CYS 17  SG  ? ? ? 1_555 D  CYS 42  SG  ? ? D CYS 44  D CYS 69  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf3  disulf ?    ? F CYS 17  SG  ? ? ? 1_555 F  CYS 42  SG  ? ? F CYS 44  F CYS 69  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
covale1  covale none ? A CYS 79  SG  ? ? ? 1_555 I  HEC .   CAB ? ? A CYS 103 A HEC 603 1_555 ? ? ? ? ? ? ? 1.798 ? ? 
covale2  covale none ? A CYS 82  SG  ? ? ? 1_555 I  HEC .   CAC ? ? A CYS 106 A HEC 603 1_555 ? ? ? ? ? ? ? 1.813 ? ? 
covale3  covale none ? A CYS 145 SG  ? ? ? 1_555 J  HEC .   CAB ? ? A CYS 169 A HEC 604 1_555 ? ? ? ? ? ? ? 1.799 ? ? 
covale4  covale none ? A CYS 148 SG  ? ? ? 1_555 J  HEC .   CAC ? ? A CYS 172 A HEC 604 1_555 ? ? ? ? ? ? ? 1.813 ? ? 
covale5  covale none ? A CYS 172 SG  ? ? ? 1_555 H  HEC .   CAB ? ? A CYS 196 A HEC 602 1_555 ? ? ? ? ? ? ? 1.798 ? ? 
covale6  covale none ? A CYS 175 SG  ? ? ? 1_555 H  HEC .   CAC ? ? A CYS 199 A HEC 602 1_555 ? ? ? ? ? ? ? 1.805 ? ? 
covale7  covale none ? A CYS 229 SG  ? ? ? 1_555 P  HEC .   CAB ? ? A CYS 253 C HEC 601 1_555 ? ? ? ? ? ? ? 1.806 ? ? 
covale8  covale none ? A CYS 232 SG  ? ? ? 1_555 P  HEC .   CAC ? ? A CYS 256 C HEC 601 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
covale9  covale none ? A CYS 239 SG  ? ? ? 1_555 G  HEC .   CAB ? ? A CYS 263 A HEC 601 1_555 ? ? ? ? ? ? ? 1.805 ? ? 
covale10 covale none ? A CYS 242 SG  ? ? ? 1_555 G  HEC .   CAC ? ? A CYS 266 A HEC 601 1_555 ? ? ? ? ? ? ? 1.804 ? ? 
covale11 covale none ? A CYS 259 SG  ? ? ? 1_555 L  HEC .   CAB ? ? A CYS 283 A HEC 606 1_555 ? ? ? ? ? ? ? 1.802 ? ? 
covale12 covale none ? A CYS 262 SG  ? ? ? 1_555 L  HEC .   CAC ? ? A CYS 286 A HEC 606 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
covale13 covale none ? A CYS 310 SG  ? ? ? 1_555 K  HEC .   CAB ? ? A CYS 334 A HEC 605 1_555 ? ? ? ? ? ? ? 1.796 ? ? 
covale14 covale none ? A CYS 313 SG  ? ? ? 1_555 K  HEC .   CAC ? ? A CYS 337 A HEC 605 1_555 ? ? ? ? ? ? ? 1.820 ? ? 
covale15 covale none ? A CYS 360 SG  ? ? ? 1_555 M  HEC .   CAB ? ? A CYS 384 A HEC 607 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
covale16 covale none ? A CYS 363 SG  ? ? ? 1_555 M  HEC .   CAC ? ? A CYS 387 A HEC 607 1_555 ? ? ? ? ? ? ? 1.615 ? ? 
covale17 covale none ? A TYR 467 OH  ? ? ? 1_555 N  HEC .   C4B ? ? A TYR 491 A HEC 608 1_555 ? ? ? ? ? ? ? 1.481 ? ? 
covale18 covale none ? A TYR 467 CE2 ? ? ? 1_555 N  HEC .   CHC ? ? A TYR 491 A HEC 608 1_555 ? ? ? ? ? ? ? 1.493 ? ? 
covale19 covale none ? N HEC .   CAB ? ? ? 1_555 E  CYS 229 SG  ? ? A HEC 608 E CYS 253 1_555 ? ? ? ? ? ? ? 1.809 ? ? 
covale20 covale none ? N HEC .   CAC ? ? ? 1_555 E  CYS 232 SG  ? ? A HEC 608 E CYS 256 1_555 ? ? ? ? ? ? ? 1.801 ? ? 
covale21 covale none ? C CYS 79  SG  ? ? ? 1_555 S  HEC .   CAB ? ? C CYS 103 C HEC 604 1_555 ? ? ? ? ? ? ? 1.798 ? ? 
covale22 covale none ? C CYS 82  SG  ? ? ? 1_555 S  HEC .   CAC ? ? C CYS 106 C HEC 604 1_555 ? ? ? ? ? ? ? 1.809 ? ? 
covale23 covale none ? C CYS 145 SG  ? ? ? 1_555 T  HEC .   CAB ? ? C CYS 169 C HEC 605 1_555 ? ? ? ? ? ? ? 1.795 ? ? 
covale24 covale none ? C CYS 148 SG  ? ? ? 1_555 T  HEC .   CAC ? ? C CYS 172 C HEC 605 1_555 ? ? ? ? ? ? ? 1.810 ? ? 
covale25 covale none ? C CYS 172 SG  ? ? ? 1_555 R  HEC .   CAB ? ? C CYS 196 C HEC 603 1_555 ? ? ? ? ? ? ? 1.798 ? ? 
covale26 covale none ? C CYS 175 SG  ? ? ? 1_555 R  HEC .   CAC ? ? C CYS 199 C HEC 603 1_555 ? ? ? ? ? ? ? 1.801 ? ? 
covale27 covale none ? C CYS 229 SG  ? ? ? 1_555 X  HEC .   CAB ? ? C CYS 253 E HEC 601 1_555 ? ? ? ? ? ? ? 1.807 ? ? 
covale28 covale none ? C CYS 232 SG  ? ? ? 1_555 X  HEC .   CAC ? ? C CYS 256 E HEC 601 1_555 ? ? ? ? ? ? ? 1.805 ? ? 
covale29 covale none ? C CYS 239 SG  ? ? ? 1_555 Q  HEC .   CAB ? ? C CYS 263 C HEC 602 1_555 ? ? ? ? ? ? ? 1.804 ? ? 
covale30 covale none ? C CYS 242 SG  ? ? ? 1_555 Q  HEC .   CAC ? ? C CYS 266 C HEC 602 1_555 ? ? ? ? ? ? ? 1.802 ? ? 
covale31 covale none ? C CYS 259 SG  ? ? ? 1_555 V  HEC .   CAB ? ? C CYS 283 C HEC 607 1_555 ? ? ? ? ? ? ? 1.799 ? ? 
covale32 covale none ? C CYS 262 SG  ? ? ? 1_555 V  HEC .   CAC ? ? C CYS 286 C HEC 607 1_555 ? ? ? ? ? ? ? 1.808 ? ? 
covale33 covale none ? C CYS 310 SG  ? ? ? 1_555 U  HEC .   CAB ? ? C CYS 334 C HEC 606 1_555 ? ? ? ? ? ? ? 1.792 ? ? 
covale34 covale none ? C CYS 313 SG  ? ? ? 1_555 U  HEC .   CAC ? ? C CYS 337 C HEC 606 1_555 ? ? ? ? ? ? ? 1.819 ? ? 
covale35 covale none ? C CYS 360 SG  ? ? ? 1_555 W  HEC .   CAB ? ? C CYS 384 C HEC 608 1_555 ? ? ? ? ? ? ? 1.799 ? ? 
covale36 covale none ? C CYS 363 SG  ? ? ? 1_555 W  HEC .   CAC ? ? C CYS 387 C HEC 608 1_555 ? ? ? ? ? ? ? 1.623 ? ? 
covale37 covale none ? C TYR 467 OH  ? ? ? 1_555 P  HEC .   C4B ? ? C TYR 491 C HEC 601 1_555 ? ? ? ? ? ? ? 1.480 ? ? 
covale38 covale none ? C TYR 467 CE2 ? ? ? 1_555 P  HEC .   CHC ? ? C TYR 491 C HEC 601 1_555 ? ? ? ? ? ? ? 1.496 ? ? 
covale39 covale none ? E CYS 79  SG  ? ? ? 1_555 AA HEC .   CAB ? ? E CYS 103 E HEC 604 1_555 ? ? ? ? ? ? ? 1.799 ? ? 
covale40 covale none ? E CYS 82  SG  ? ? ? 1_555 AA HEC .   CAC ? ? E CYS 106 E HEC 604 1_555 ? ? ? ? ? ? ? 1.806 ? ? 
covale41 covale none ? E CYS 145 SG  ? ? ? 1_555 BA HEC .   CAB ? ? E CYS 169 E HEC 605 1_555 ? ? ? ? ? ? ? 1.796 ? ? 
covale42 covale none ? E CYS 148 SG  ? ? ? 1_555 BA HEC .   CAC ? ? E CYS 172 E HEC 605 1_555 ? ? ? ? ? ? ? 1.819 ? ? 
covale43 covale none ? E CYS 172 SG  ? ? ? 1_555 Z  HEC .   CAB ? ? E CYS 196 E HEC 603 1_555 ? ? ? ? ? ? ? 1.801 ? ? 
covale44 covale none ? E CYS 175 SG  ? ? ? 1_555 Z  HEC .   CAC ? ? E CYS 199 E HEC 603 1_555 ? ? ? ? ? ? ? 1.808 ? ? 
covale45 covale none ? E CYS 239 SG  ? ? ? 1_555 Y  HEC .   CAB ? ? E CYS 263 E HEC 602 1_555 ? ? ? ? ? ? ? 1.801 ? ? 
covale46 covale none ? E CYS 242 SG  ? ? ? 1_555 Y  HEC .   CAC ? ? E CYS 266 E HEC 602 1_555 ? ? ? ? ? ? ? 1.801 ? ? 
covale47 covale none ? E CYS 259 SG  ? ? ? 1_555 DA HEC .   CAB ? ? E CYS 283 E HEC 607 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
covale48 covale none ? E CYS 262 SG  ? ? ? 1_555 DA HEC .   CAC ? ? E CYS 286 E HEC 607 1_555 ? ? ? ? ? ? ? 1.803 ? ? 
covale49 covale none ? E CYS 310 SG  ? ? ? 1_555 CA HEC .   CAB ? ? E CYS 334 E HEC 606 1_555 ? ? ? ? ? ? ? 1.794 ? ? 
covale50 covale none ? E CYS 313 SG  ? ? ? 1_555 CA HEC .   CAC ? ? E CYS 337 E HEC 606 1_555 ? ? ? ? ? ? ? 1.810 ? ? 
covale51 covale none ? E CYS 360 SG  ? ? ? 1_555 EA HEC .   CAB ? ? E CYS 384 E HEC 608 1_555 ? ? ? ? ? ? ? 1.802 ? ? 
covale52 covale none ? E CYS 363 SG  ? ? ? 1_555 EA HEC .   CAC ? ? E CYS 387 E HEC 608 1_555 ? ? ? ? ? ? ? 1.623 ? ? 
covale53 covale none ? E TYR 467 OH  ? ? ? 1_555 X  HEC .   C4B ? ? E TYR 491 E HEC 601 1_555 ? ? ? ? ? ? ? 1.483 ? ? 
covale54 covale none ? E TYR 467 CE2 ? ? ? 1_555 X  HEC .   CHC ? ? E TYR 491 E HEC 601 1_555 ? ? ? ? ? ? ? 1.493 ? ? 
metalc1  metalc ?    ? A HIS 83  NE2 ? ? ? 1_555 I  HEC .   FE  ? ? A HIS 107 A HEC 603 1_555 ? ? ? ? ? ? ? 1.869 ? ? 
metalc2  metalc ?    ? A HIS 99  NE2 ? ? ? 1_555 H  HEC .   FE  ? ? A HIS 123 A HEC 602 1_555 ? ? ? ? ? ? ? 1.873 ? ? 
metalc3  metalc ?    ? A HIS 149 NE2 ? ? ? 1_555 J  HEC .   FE  ? ? A HIS 173 A HEC 604 1_555 ? ? ? ? ? ? ? 1.875 ? ? 
metalc4  metalc ?    ? A HIS 160 NE2 ? ? ? 1_555 I  HEC .   FE  ? ? A HIS 184 A HEC 603 1_555 ? ? ? ? ? ? ? 1.891 ? ? 
metalc5  metalc ?    ? A HIS 176 NE2 ? ? ? 1_555 H  HEC .   FE  ? ? A HIS 200 A HEC 602 1_555 ? ? ? ? ? ? ? 1.869 ? ? 
metalc6  metalc ?    ? A HIS 204 NE2 ? ? ? 1_555 L  HEC .   FE  ? ? A HIS 228 A HEC 606 1_555 ? ? ? ? ? ? ? 1.879 ? ? 
metalc7  metalc ?    ? A HIS 233 NE2 ? ? ? 1_555 P  HEC .   FE  ? ? A HIS 257 C HEC 601 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc8  metalc ?    ? A HIS 243 NE2 ? ? ? 1_555 G  HEC .   FE  ? ? A HIS 267 A HEC 601 1_555 ? ? ? ? ? ? ? 1.879 ? ? 
metalc9  metalc ?    ? A HIS 246 NE2 ? ? ? 1_555 J  HEC .   FE  ? ? A HIS 270 A HEC 604 1_555 ? ? ? ? ? ? ? 1.872 ? ? 
metalc10 metalc ?    ? A HIS 263 NE2 ? ? ? 1_555 L  HEC .   FE  ? ? A HIS 287 A HEC 606 1_555 ? ? ? ? ? ? ? 1.859 ? ? 
metalc11 metalc ?    ? A HIS 279 NE2 ? ? ? 1_555 M  HEC .   FE  ? ? A HIS 303 A HEC 607 1_555 ? ? ? ? ? ? ? 1.873 ? ? 
metalc12 metalc ?    ? A ASP 288 OD1 ? ? ? 1_555 O  K   .   K   ? ? A ASP 312 A K   609 1_555 ? ? ? ? ? ? ? 2.628 ? ? 
metalc13 metalc ?    ? A ASP 288 OD2 ? ? ? 1_555 O  K   .   K   ? ? A ASP 312 A K   609 1_555 ? ? ? ? ? ? ? 2.827 ? ? 
metalc14 metalc ?    ? A HIS 314 NE2 ? ? ? 1_555 K  HEC .   FE  ? ? A HIS 338 A HEC 605 1_555 ? ? ? ? ? ? ? 1.870 ? ? 
metalc15 metalc ?    ? A HIS 323 NE2 ? ? ? 1_555 G  HEC .   FE  ? ? A HIS 347 A HEC 601 1_555 ? ? ? ? ? ? ? 1.878 ? ? 
metalc16 metalc ?    ? A HIS 364 NE2 ? ? ? 1_555 M  HEC .   FE  ? ? A HIS 388 A HEC 607 1_555 ? ? ? ? ? ? ? 1.869 ? ? 
metalc17 metalc ?    ? A HIS 459 NE2 ? ? ? 1_555 K  HEC .   FE  ? ? A HIS 483 A HEC 605 1_555 ? ? ? ? ? ? ? 1.881 ? ? 
metalc18 metalc ?    ? N HEC .   FE  ? ? ? 1_555 GA HOH .   O   ? ? A HEC 608 A HOH 971 1_555 ? ? ? ? ? ? ? 2.457 ? ? 
metalc19 metalc ?    ? N HEC .   FE  ? ? ? 1_555 E  HIS 233 NE2 ? ? A HEC 608 E HIS 257 1_555 ? ? ? ? ? ? ? 2.131 ? ? 
metalc20 metalc ?    ? O K   .   K   ? ? ? 1_555 GA HOH .   O   ? ? A K   609 A HOH 916 1_555 ? ? ? ? ? ? ? 2.875 ? ? 
metalc21 metalc ?    ? O K   .   K   ? ? ? 1_555 C  ASP 288 OD1 ? ? A K   609 C ASP 312 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc22 metalc ?    ? O K   .   K   ? ? ? 1_555 C  ASP 288 OD2 ? ? A K   609 C ASP 312 1_555 ? ? ? ? ? ? ? 2.635 ? ? 
metalc23 metalc ?    ? O K   .   K   ? ? ? 1_555 E  ASP 288 OD2 ? ? A K   609 E ASP 312 1_555 ? ? ? ? ? ? ? 2.630 ? ? 
metalc24 metalc ?    ? O K   .   K   ? ? ? 1_555 E  ASP 288 OD1 ? ? A K   609 E ASP 312 1_555 ? ? ? ? ? ? ? 2.921 ? ? 
metalc25 metalc ?    ? C HIS 83  NE2 ? ? ? 1_555 S  HEC .   FE  ? ? C HIS 107 C HEC 604 1_555 ? ? ? ? ? ? ? 1.876 ? ? 
metalc26 metalc ?    ? C HIS 99  NE2 ? ? ? 1_555 R  HEC .   FE  ? ? C HIS 123 C HEC 603 1_555 ? ? ? ? ? ? ? 1.869 ? ? 
metalc27 metalc ?    ? C HIS 149 NE2 ? ? ? 1_555 T  HEC .   FE  ? ? C HIS 173 C HEC 605 1_555 ? ? ? ? ? ? ? 1.870 ? ? 
metalc28 metalc ?    ? C HIS 160 NE2 ? ? ? 1_555 S  HEC .   FE  ? ? C HIS 184 C HEC 604 1_555 ? ? ? ? ? ? ? 1.881 ? ? 
metalc29 metalc ?    ? C HIS 176 NE2 ? ? ? 1_555 R  HEC .   FE  ? ? C HIS 200 C HEC 603 1_555 ? ? ? ? ? ? ? 1.875 ? ? 
metalc30 metalc ?    ? C HIS 204 NE2 ? ? ? 1_555 V  HEC .   FE  ? ? C HIS 228 C HEC 607 1_555 ? ? ? ? ? ? ? 1.874 ? ? 
metalc31 metalc ?    ? C HIS 233 NE2 ? ? ? 1_555 X  HEC .   FE  ? ? C HIS 257 E HEC 601 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
metalc32 metalc ?    ? C HIS 243 NE2 ? ? ? 1_555 Q  HEC .   FE  ? ? C HIS 267 C HEC 602 1_555 ? ? ? ? ? ? ? 1.881 ? ? 
metalc33 metalc ?    ? C HIS 246 NE2 ? ? ? 1_555 T  HEC .   FE  ? ? C HIS 270 C HEC 605 1_555 ? ? ? ? ? ? ? 1.869 ? ? 
metalc34 metalc ?    ? C HIS 263 NE2 ? ? ? 1_555 V  HEC .   FE  ? ? C HIS 287 C HEC 607 1_555 ? ? ? ? ? ? ? 1.868 ? ? 
metalc35 metalc ?    ? C HIS 279 NE2 ? ? ? 1_555 W  HEC .   FE  ? ? C HIS 303 C HEC 608 1_555 ? ? ? ? ? ? ? 1.870 ? ? 
metalc36 metalc ?    ? C HIS 314 NE2 ? ? ? 1_555 U  HEC .   FE  ? ? C HIS 338 C HEC 606 1_555 ? ? ? ? ? ? ? 1.866 ? ? 
metalc37 metalc ?    ? C HIS 323 NE2 ? ? ? 1_555 Q  HEC .   FE  ? ? C HIS 347 C HEC 602 1_555 ? ? ? ? ? ? ? 1.882 ? ? 
metalc38 metalc ?    ? C HIS 364 NE2 ? ? ? 1_555 W  HEC .   FE  ? ? C HIS 388 C HEC 608 1_555 ? ? ? ? ? ? ? 1.886 ? ? 
metalc39 metalc ?    ? C HIS 459 NE2 ? ? ? 1_555 U  HEC .   FE  ? ? C HIS 483 C HEC 606 1_555 ? ? ? ? ? ? ? 1.869 ? ? 
metalc40 metalc ?    ? E HIS 83  NE2 ? ? ? 1_555 AA HEC .   FE  ? ? E HIS 107 E HEC 604 1_555 ? ? ? ? ? ? ? 1.871 ? ? 
metalc41 metalc ?    ? E HIS 99  NE2 ? ? ? 1_555 Z  HEC .   FE  ? ? E HIS 123 E HEC 603 1_555 ? ? ? ? ? ? ? 1.871 ? ? 
metalc42 metalc ?    ? E HIS 149 NE2 ? ? ? 1_555 BA HEC .   FE  ? ? E HIS 173 E HEC 605 1_555 ? ? ? ? ? ? ? 1.872 ? ? 
metalc43 metalc ?    ? E HIS 160 NE2 ? ? ? 1_555 AA HEC .   FE  ? ? E HIS 184 E HEC 604 1_555 ? ? ? ? ? ? ? 1.883 ? ? 
metalc44 metalc ?    ? E HIS 176 NE2 ? ? ? 1_555 Z  HEC .   FE  ? ? E HIS 200 E HEC 603 1_555 ? ? ? ? ? ? ? 1.878 ? ? 
metalc45 metalc ?    ? E HIS 204 NE2 ? ? ? 1_555 DA HEC .   FE  ? ? E HIS 228 E HEC 607 1_555 ? ? ? ? ? ? ? 1.871 ? ? 
metalc46 metalc ?    ? E HIS 243 NE2 ? ? ? 1_555 Y  HEC .   FE  ? ? E HIS 267 E HEC 602 1_555 ? ? ? ? ? ? ? 1.879 ? ? 
metalc47 metalc ?    ? E HIS 246 NE2 ? ? ? 1_555 BA HEC .   FE  ? ? E HIS 270 E HEC 605 1_555 ? ? ? ? ? ? ? 1.878 ? ? 
metalc48 metalc ?    ? E HIS 263 NE2 ? ? ? 1_555 DA HEC .   FE  ? ? E HIS 287 E HEC 607 1_555 ? ? ? ? ? ? ? 1.866 ? ? 
metalc49 metalc ?    ? E HIS 279 NE2 ? ? ? 1_555 EA HEC .   FE  ? ? E HIS 303 E HEC 608 1_555 ? ? ? ? ? ? ? 1.876 ? ? 
metalc50 metalc ?    ? E HIS 314 NE2 ? ? ? 1_555 CA HEC .   FE  ? ? E HIS 338 E HEC 606 1_555 ? ? ? ? ? ? ? 1.872 ? ? 
metalc51 metalc ?    ? E HIS 323 NE2 ? ? ? 1_555 Y  HEC .   FE  ? ? E HIS 347 E HEC 602 1_555 ? ? ? ? ? ? ? 1.871 ? ? 
metalc52 metalc ?    ? E HIS 364 NE2 ? ? ? 1_555 EA HEC .   FE  ? ? E HIS 388 E HEC 608 1_555 ? ? ? ? ? ? ? 1.872 ? ? 
metalc53 metalc ?    ? E HIS 459 NE2 ? ? ? 1_555 CA HEC .   FE  ? ? E HIS 483 E HEC 606 1_555 ? ? ? ? ? ? ? 1.874 ? ? 
metalc54 metalc ?    ? X HEC .   FE  ? ? ? 1_555 KA HOH .   O   ? ? E HEC 601 E HOH 948 1_555 ? ? ? ? ? ? ? 2.681 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  SER 69  A . ? SER 93  A PRO 70  A ? PRO 94  A 1 3.84  
2  ARG 201 A . ? ARG 225 A PRO 202 A ? PRO 226 A 1 -1.28 
3  ARG 245 A . ? ARG 269 A HIS 246 A ? HIS 270 A 1 -1.35 
4  GLU 415 A . ? GLU 439 A PRO 416 A ? PRO 440 A 1 6.44  
5  ASN 434 A . ? ASN 458 A PRO 435 A ? PRO 459 A 1 1.22  
6  SER 69  C . ? SER 93  C PRO 70  C ? PRO 94  C 1 6.29  
7  ARG 201 C . ? ARG 225 C PRO 202 C ? PRO 226 C 1 -1.90 
8  ARG 245 C . ? ARG 269 C HIS 246 C ? HIS 270 C 1 -3.71 
9  GLU 415 C . ? GLU 439 C PRO 416 C ? PRO 440 C 1 3.41  
10 ASN 434 C . ? ASN 458 C PRO 435 C ? PRO 459 C 1 4.50  
11 SER 69  E . ? SER 93  E PRO 70  E ? PRO 94  E 1 5.25  
12 ARG 201 E . ? ARG 225 E PRO 202 E ? PRO 226 E 1 -4.07 
13 ARG 245 E . ? ARG 269 E HIS 246 E ? HIS 270 E 1 -1.79 
14 GLU 415 E . ? GLU 439 E PRO 416 E ? PRO 440 E 1 3.54  
15 ASN 434 E . ? ASN 458 E PRO 435 E ? PRO 459 E 1 0.51  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 2 ? 
C ? 2 ? 
D ? 2 ? 
E ? 2 ? 
F ? 2 ? 
G ? 2 ? 
H ? 2 ? 
I ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? anti-parallel 
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
G 1 2 ? anti-parallel 
H 1 2 ? anti-parallel 
I 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 VAL A 73  ? ALA A 74  ? VAL A 97  ALA A 98  
A 2 ALA A 158 ? ASP A 159 ? ALA A 182 ASP A 183 
B 1 GLU A 316 ? TYR A 317 ? GLU A 340 TYR A 341 
B 2 GLU A 320 ? TYR A 321 ? GLU A 344 TYR A 345 
C 1 VAL B 25  ? GLU B 33  ? VAL B 52  GLU B 60  
C 2 LYS B 36  ? LYS B 41  ? LYS B 63  LYS B 68  
D 1 VAL C 73  ? ALA C 74  ? VAL C 97  ALA C 98  
D 2 ALA C 158 ? ASP C 159 ? ALA C 182 ASP C 183 
E 1 GLU C 316 ? TYR C 317 ? GLU C 340 TYR C 341 
E 2 GLU C 320 ? TYR C 321 ? GLU C 344 TYR C 345 
F 1 VAL D 25  ? GLU D 33  ? VAL D 52  GLU D 60  
F 2 LYS D 36  ? LYS D 41  ? LYS D 63  LYS D 68  
G 1 VAL E 73  ? ALA E 74  ? VAL E 97  ALA E 98  
G 2 ALA E 158 ? ASP E 159 ? ALA E 182 ASP E 183 
H 1 GLU E 316 ? TYR E 317 ? GLU E 340 TYR E 341 
H 2 GLU E 320 ? TYR E 321 ? GLU E 344 TYR E 345 
I 1 VAL F 25  ? GLU F 33  ? VAL F 52  GLU F 60  
I 2 LYS F 36  ? LYS F 41  ? LYS F 63  LYS F 68  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N ALA A 74  ? N ALA A 98  O ALA A 158 ? O ALA A 182 
B 1 2 N TYR A 317 ? N TYR A 341 O GLU A 320 ? O GLU A 344 
C 1 2 N VAL B 26  ? N VAL B 53  O VAL B 40  ? O VAL B 67  
D 1 2 N ALA C 74  ? N ALA C 98  O ALA C 158 ? O ALA C 182 
E 1 2 N TYR C 317 ? N TYR C 341 O GLU C 320 ? O GLU C 344 
F 1 2 N VAL D 26  ? N VAL D 53  O VAL D 40  ? O VAL D 67  
G 1 2 N ALA E 74  ? N ALA E 98  O ALA E 158 ? O ALA E 182 
H 1 2 N TYR E 317 ? N TYR E 341 O GLU E 320 ? O GLU E 344 
I 1 2 N VAL F 26  ? N VAL F 53  O VAL F 40  ? O VAL F 67  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A HEC 601 ? 21 'BINDING SITE FOR RESIDUE HEC A 601' 
AC2 Software A HEC 602 ? 19 'BINDING SITE FOR RESIDUE HEC A 602' 
AC3 Software A HEC 603 ? 17 'BINDING SITE FOR RESIDUE HEC A 603' 
AC4 Software A HEC 604 ? 23 'BINDING SITE FOR RESIDUE HEC A 604' 
AC5 Software A HEC 605 ? 20 'BINDING SITE FOR RESIDUE HEC A 605' 
AC6 Software A HEC 606 ? 23 'BINDING SITE FOR RESIDUE HEC A 606' 
AC7 Software A HEC 607 ? 22 'BINDING SITE FOR RESIDUE HEC A 607' 
AC8 Software A HEC 608 ? 23 'BINDING SITE FOR RESIDUE HEC A 608' 
AC9 Software A K   609 ? 4  'BINDING SITE FOR RESIDUE K A 609'   
BC1 Software C HEC 601 ? 24 'BINDING SITE FOR RESIDUE HEC C 601' 
BC2 Software C HEC 602 ? 21 'BINDING SITE FOR RESIDUE HEC C 602' 
BC3 Software C HEC 603 ? 19 'BINDING SITE FOR RESIDUE HEC C 603' 
BC4 Software C HEC 604 ? 20 'BINDING SITE FOR RESIDUE HEC C 604' 
BC5 Software C HEC 605 ? 22 'BINDING SITE FOR RESIDUE HEC C 605' 
BC6 Software C HEC 606 ? 21 'BINDING SITE FOR RESIDUE HEC C 606' 
BC7 Software C HEC 607 ? 22 'BINDING SITE FOR RESIDUE HEC C 607' 
BC8 Software C HEC 608 ? 19 'BINDING SITE FOR RESIDUE HEC C 608' 
BC9 Software E HEC 601 ? 23 'BINDING SITE FOR RESIDUE HEC E 601' 
CC1 Software E HEC 602 ? 21 'BINDING SITE FOR RESIDUE HEC E 602' 
CC2 Software E HEC 603 ? 17 'BINDING SITE FOR RESIDUE HEC E 603' 
CC3 Software E HEC 604 ? 18 'BINDING SITE FOR RESIDUE HEC E 604' 
CC4 Software E HEC 605 ? 22 'BINDING SITE FOR RESIDUE HEC E 605' 
CC5 Software E HEC 606 ? 21 'BINDING SITE FOR RESIDUE HEC E 606' 
CC6 Software E HEC 607 ? 23 'BINDING SITE FOR RESIDUE HEC E 607' 
CC7 Software E HEC 608 ? 21 'BINDING SITE FOR RESIDUE HEC E 608' 
CC8 Software E PO4 609 ? 5  'BINDING SITE FOR RESIDUE PO4 E 609' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 21 TYR A  116 ? TYR A 140 . ? 1_555 ? 
2   AC1 21 LYS A  117 ? LYS A 141 . ? 1_555 ? 
3   AC1 21 CYS A  172 ? CYS A 196 . ? 1_555 ? 
4   AC1 21 HIS A  176 ? HIS A 200 . ? 1_555 ? 
5   AC1 21 GLU A  179 ? GLU A 203 . ? 1_555 ? 
6   AC1 21 HIS A  204 ? HIS A 228 . ? 1_555 ? 
7   AC1 21 ASN A  235 ? ASN A 259 . ? 1_555 ? 
8   AC1 21 CYS A  239 ? CYS A 263 . ? 1_555 ? 
9   AC1 21 CYS A  242 ? CYS A 266 . ? 1_555 ? 
10  AC1 21 HIS A  243 ? HIS A 267 . ? 1_555 ? 
11  AC1 21 SER A  253 ? SER A 277 . ? 1_555 ? 
12  AC1 21 ARG A  254 ? ARG A 278 . ? 1_555 ? 
13  AC1 21 ARG A  295 ? ARG A 319 . ? 1_555 ? 
14  AC1 21 LEU A  296 ? LEU A 320 . ? 1_555 ? 
15  AC1 21 MET A  315 ? MET A 339 . ? 1_555 ? 
16  AC1 21 HIS A  323 ? HIS A 347 . ? 1_555 ? 
17  AC1 21 HEC H  .   ? HEC A 602 . ? 1_555 ? 
18  AC1 21 HEC L  .   ? HEC A 606 . ? 1_555 ? 
19  AC1 21 HOH GA .   ? HOH A 767 . ? 1_555 ? 
20  AC1 21 HOH GA .   ? HOH A 785 . ? 1_555 ? 
21  AC1 21 HOH GA .   ? HOH A 979 . ? 1_555 ? 
22  AC2 19 THR A  98  ? THR A 122 . ? 1_555 ? 
23  AC2 19 HIS A  99  ? HIS A 123 . ? 1_555 ? 
24  AC2 19 LYS A  117 ? LYS A 141 . ? 1_555 ? 
25  AC2 19 LYS A  120 ? LYS A 144 . ? 1_555 ? 
26  AC2 19 LEU A  121 ? LEU A 145 . ? 1_555 ? 
27  AC2 19 VAL A  124 ? VAL A 148 . ? 1_555 ? 
28  AC2 19 VAL A  143 ? VAL A 167 . ? 1_555 ? 
29  AC2 19 CYS A  172 ? CYS A 196 . ? 1_555 ? 
30  AC2 19 CYS A  175 ? CYS A 199 . ? 1_555 ? 
31  AC2 19 HIS A  176 ? HIS A 200 . ? 1_555 ? 
32  AC2 19 CYS A  239 ? CYS A 263 . ? 1_555 ? 
33  AC2 19 HIS A  243 ? HIS A 267 . ? 1_555 ? 
34  AC2 19 PHE A  248 ? PHE A 272 . ? 1_555 ? 
35  AC2 19 SER A  249 ? SER A 273 . ? 1_555 ? 
36  AC2 19 ALA A  250 ? ALA A 274 . ? 1_555 ? 
37  AC2 19 HEC G  .   ? HEC A 601 . ? 1_555 ? 
38  AC2 19 HEC J  .   ? HEC A 604 . ? 1_555 ? 
39  AC2 19 HOH GA .   ? HOH A 825 . ? 1_555 ? 
40  AC2 19 HOH GA .   ? HOH A 903 . ? 1_555 ? 
41  AC3 17 TYR A  57  ? TYR A 81  . ? 1_555 ? 
42  AC3 17 TYR A  64  ? TYR A 88  . ? 1_555 ? 
43  AC3 17 ASP A  78  ? ASP A 102 . ? 1_555 ? 
44  AC3 17 CYS A  79  ? CYS A 103 . ? 1_555 ? 
45  AC3 17 CYS A  82  ? CYS A 106 . ? 1_555 ? 
46  AC3 17 HIS A  83  ? HIS A 107 . ? 1_555 ? 
47  AC3 17 GLU A  86  ? GLU A 110 . ? 1_555 ? 
48  AC3 17 CYS A  145 ? CYS A 169 . ? 1_555 ? 
49  AC3 17 HIS A  149 ? HIS A 173 . ? 1_555 ? 
50  AC3 17 HIS A  160 ? HIS A 184 . ? 1_555 ? 
51  AC3 17 ILE A  164 ? ILE A 188 . ? 1_555 ? 
52  AC3 17 MET A  166 ? MET A 190 . ? 1_555 ? 
53  AC3 17 HEC J  .   ? HEC A 604 . ? 1_555 ? 
54  AC3 17 HOH GA .   ? HOH A 838 . ? 1_555 ? 
55  AC3 17 SER C  365 ? SER C 389 . ? 1_555 ? 
56  AC3 17 GLU C  366 ? GLU C 390 . ? 1_555 ? 
57  AC3 17 ARG C  367 ? ARG C 391 . ? 1_555 ? 
58  AC4 23 TYR A  57  ? TYR A 81  . ? 1_555 ? 
59  AC4 23 PRO A  60  ? PRO A 84  . ? 1_555 ? 
60  AC4 23 HIS A  83  ? HIS A 107 . ? 1_555 ? 
61  AC4 23 TRP A  90  ? TRP A 114 . ? 1_555 ? 
62  AC4 23 TRP A  94  ? TRP A 118 . ? 1_555 ? 
63  AC4 23 HIS A  99  ? HIS A 123 . ? 1_555 ? 
64  AC4 23 VAL A  143 ? VAL A 167 . ? 1_555 ? 
65  AC4 23 GLY A  144 ? GLY A 168 . ? 1_555 ? 
66  AC4 23 CYS A  145 ? CYS A 169 . ? 1_555 ? 
67  AC4 23 CYS A  148 ? CYS A 172 . ? 1_555 ? 
68  AC4 23 HIS A  149 ? HIS A 173 . ? 1_555 ? 
69  AC4 23 MET A  166 ? MET A 190 . ? 1_555 ? 
70  AC4 23 PRO A  167 ? PRO A 191 . ? 1_555 ? 
71  AC4 23 LYS A  238 ? LYS A 262 . ? 1_555 ? 
72  AC4 23 ASP A  240 ? ASP A 264 . ? 1_555 ? 
73  AC4 23 ARG A  245 ? ARG A 269 . ? 1_555 ? 
74  AC4 23 HIS A  246 ? HIS A 270 . ? 1_555 ? 
75  AC4 23 PHE A  248 ? PHE A 272 . ? 1_555 ? 
76  AC4 23 HEC H  .   ? HEC A 602 . ? 1_555 ? 
77  AC4 23 HEC I  .   ? HEC A 603 . ? 1_555 ? 
78  AC4 23 HIS C  364 ? HIS C 388 . ? 1_555 ? 
79  AC4 23 SER C  365 ? SER C 389 . ? 1_555 ? 
80  AC4 23 HOH IA .   ? HOH C 776 . ? 1_555 ? 
81  AC5 20 HIS A  263 ? HIS A 287 . ? 1_555 ? 
82  AC5 20 ASN A  270 ? ASN A 294 . ? 1_555 ? 
83  AC5 20 TYR A  274 ? TYR A 298 . ? 1_555 ? 
84  AC5 20 PRO A  308 ? PRO A 332 . ? 1_555 ? 
85  AC5 20 THR A  309 ? THR A 333 . ? 1_555 ? 
86  AC5 20 CYS A  310 ? CYS A 334 . ? 1_555 ? 
87  AC5 20 CYS A  313 ? CYS A 337 . ? 1_555 ? 
88  AC5 20 HIS A  314 ? HIS A 338 . ? 1_555 ? 
89  AC5 20 THR A  329 ? THR A 353 . ? 1_555 ? 
90  AC5 20 ARG A  330 ? ARG A 354 . ? 1_555 ? 
91  AC5 20 TRP A  331 ? TRP A 355 . ? 1_555 ? 
92  AC5 20 ALA A  332 ? ALA A 356 . ? 1_555 ? 
93  AC5 20 TRP A  356 ? TRP A 380 . ? 1_555 ? 
94  AC5 20 MET A  376 ? MET A 400 . ? 1_555 ? 
95  AC5 20 HIS A  459 ? HIS A 483 . ? 1_555 ? 
96  AC5 20 HEC L  .   ? HEC A 606 . ? 1_555 ? 
97  AC5 20 HEC M  .   ? HEC A 607 . ? 1_555 ? 
98  AC5 20 HOH GA .   ? HOH A 711 . ? 1_555 ? 
99  AC5 20 HOH GA .   ? HOH A 858 . ? 1_555 ? 
100 AC5 20 HEC P  .   ? HEC C 601 . ? 1_555 ? 
101 AC6 23 PRO A  202 ? PRO A 226 . ? 1_555 ? 
102 AC6 23 SER A  203 ? SER A 227 . ? 1_555 ? 
103 AC6 23 HIS A  204 ? HIS A 228 . ? 1_555 ? 
104 AC6 23 ASP A  207 ? ASP A 231 . ? 1_555 ? 
105 AC6 23 ALA A  210 ? ALA A 234 . ? 1_555 ? 
106 AC6 23 CYS A  232 ? CYS A 256 . ? 1_555 ? 
107 AC6 23 HIS A  233 ? HIS A 257 . ? 1_555 ? 
108 AC6 23 ASN A  235 ? ASN A 259 . ? 1_555 ? 
109 AC6 23 ASN A  241 ? ASN A 265 . ? 1_555 ? 
110 AC6 23 CYS A  242 ? CYS A 266 . ? 1_555 ? 
111 AC6 23 ALA A  258 ? ALA A 282 . ? 1_555 ? 
112 AC6 23 CYS A  259 ? CYS A 283 . ? 1_555 ? 
113 AC6 23 CYS A  262 ? CYS A 286 . ? 1_555 ? 
114 AC6 23 HIS A  263 ? HIS A 287 . ? 1_555 ? 
115 AC6 23 CYS A  310 ? CYS A 334 . ? 1_555 ? 
116 AC6 23 HIS A  314 ? HIS A 338 . ? 1_555 ? 
117 AC6 23 ILE A  325 ? ILE A 349 . ? 1_555 ? 
118 AC6 23 THR A  329 ? THR A 353 . ? 1_555 ? 
119 AC6 23 ALA A  332 ? ALA A 356 . ? 1_555 ? 
120 AC6 23 HEC G  .   ? HEC A 601 . ? 1_555 ? 
121 AC6 23 HEC K  .   ? HEC A 605 . ? 1_555 ? 
122 AC6 23 HOH GA .   ? HOH A 749 . ? 1_555 ? 
123 AC6 23 HEC P  .   ? HEC C 601 . ? 1_555 ? 
124 AC7 22 HIS A  279 ? HIS A 303 . ? 1_555 ? 
125 AC7 22 LEU A  282 ? LEU A 306 . ? 1_555 ? 
126 AC7 22 PHE A  300 ? PHE A 324 . ? 1_555 ? 
127 AC7 22 ASN A  306 ? ASN A 330 . ? 1_555 ? 
128 AC7 22 ALA A  307 ? ALA A 331 . ? 1_555 ? 
129 AC7 22 PRO A  308 ? PRO A 332 . ? 1_555 ? 
130 AC7 22 THR A  359 ? THR A 383 . ? 1_555 ? 
131 AC7 22 CYS A  360 ? CYS A 384 . ? 1_555 ? 
132 AC7 22 CYS A  363 ? CYS A 387 . ? 1_555 ? 
133 AC7 22 HIS A  364 ? HIS A 388 . ? 1_555 ? 
134 AC7 22 PHE A  368 ? PHE A 392 . ? 1_555 ? 
135 AC7 22 TYR A  372 ? TYR A 396 . ? 1_555 ? 
136 AC7 22 VAL A  460 ? VAL A 484 . ? 1_555 ? 
137 AC7 22 HEC K  .   ? HEC A 605 . ? 1_555 ? 
138 AC7 22 HOH GA .   ? HOH A 709 . ? 1_555 ? 
139 AC7 22 HOH GA .   ? HOH A 908 . ? 1_555 ? 
140 AC7 22 LYS E  238 ? LYS E 262 . ? 1_555 ? 
141 AC7 22 ASP E  240 ? ASP E 264 . ? 1_555 ? 
142 AC7 22 THR E  244 ? THR E 268 . ? 1_555 ? 
143 AC7 22 ARG E  245 ? ARG E 269 . ? 1_555 ? 
144 AC7 22 HOH KA .   ? HOH E 719 . ? 1_555 ? 
145 AC7 22 HOH KA .   ? HOH E 818 . ? 1_555 ? 
146 AC8 23 THR A  466 ? THR A 490 . ? 1_555 ? 
147 AC8 23 TYR A  467 ? TYR A 491 . ? 1_555 ? 
148 AC8 23 HOH GA .   ? HOH A 788 . ? 1_555 ? 
149 AC8 23 HOH GA .   ? HOH A 971 . ? 1_555 ? 
150 AC8 23 TRP E  197 ? TRP E 221 . ? 1_555 ? 
151 AC8 23 ARG E  201 ? ARG E 225 . ? 1_555 ? 
152 AC8 23 ALA E  210 ? ALA E 234 . ? 1_555 ? 
153 AC8 23 ASN E  211 ? ASN E 235 . ? 1_555 ? 
154 AC8 23 THR E  214 ? THR E 238 . ? 1_555 ? 
155 AC8 23 TRP E  217 ? TRP E 241 . ? 1_555 ? 
156 AC8 23 CYS E  229 ? CYS E 253 . ? 1_555 ? 
157 AC8 23 CYS E  232 ? CYS E 256 . ? 1_555 ? 
158 AC8 23 HIS E  233 ? HIS E 257 . ? 1_555 ? 
159 AC8 23 THR E  261 ? THR E 285 . ? 1_555 ? 
160 AC8 23 CYS E  262 ? CYS E 286 . ? 1_555 ? 
161 AC8 23 HIS E  263 ? HIS E 287 . ? 1_555 ? 
162 AC8 23 HIS E  268 ? HIS E 292 . ? 1_555 ? 
163 AC8 23 ASN E  333 ? ASN E 357 . ? 1_555 ? 
164 AC8 23 PHE E  428 ? PHE E 452 . ? 1_555 ? 
165 AC8 23 HEC CA .   ? HEC E 606 . ? 1_555 ? 
166 AC8 23 HEC DA .   ? HEC E 607 . ? 1_555 ? 
167 AC8 23 HOH KA .   ? HOH E 713 . ? 1_555 ? 
168 AC8 23 HOH KA .   ? HOH E 779 . ? 1_555 ? 
169 AC9 4  ASP A  288 ? ASP A 312 . ? 1_555 ? 
170 AC9 4  HOH GA .   ? HOH A 916 . ? 1_555 ? 
171 AC9 4  ASP C  288 ? ASP C 312 . ? 1_555 ? 
172 AC9 4  ASP E  288 ? ASP E 312 . ? 1_555 ? 
173 BC1 24 TRP A  197 ? TRP A 221 . ? 1_555 ? 
174 BC1 24 ARG A  201 ? ARG A 225 . ? 1_555 ? 
175 BC1 24 ALA A  210 ? ALA A 234 . ? 1_555 ? 
176 BC1 24 ASN A  211 ? ASN A 235 . ? 1_555 ? 
177 BC1 24 THR A  214 ? THR A 238 . ? 1_555 ? 
178 BC1 24 TRP A  217 ? TRP A 241 . ? 1_555 ? 
179 BC1 24 GLY A  228 ? GLY A 252 . ? 1_555 ? 
180 BC1 24 CYS A  229 ? CYS A 253 . ? 1_555 ? 
181 BC1 24 CYS A  232 ? CYS A 256 . ? 1_555 ? 
182 BC1 24 HIS A  233 ? HIS A 257 . ? 1_555 ? 
183 BC1 24 THR A  261 ? THR A 285 . ? 1_555 ? 
184 BC1 24 CYS A  262 ? CYS A 286 . ? 1_555 ? 
185 BC1 24 HIS A  263 ? HIS A 287 . ? 1_555 ? 
186 BC1 24 HIS A  268 ? HIS A 292 . ? 1_555 ? 
187 BC1 24 ASN A  333 ? ASN A 357 . ? 1_555 ? 
188 BC1 24 PHE A  428 ? PHE A 452 . ? 1_555 ? 
189 BC1 24 HEC K  .   ? HEC A 605 . ? 1_555 ? 
190 BC1 24 HEC L  .   ? HEC A 606 . ? 1_555 ? 
191 BC1 24 HOH GA .   ? HOH A 775 . ? 1_555 ? 
192 BC1 24 HOH GA .   ? HOH A 968 . ? 1_555 ? 
193 BC1 24 THR C  466 ? THR C 490 . ? 1_555 ? 
194 BC1 24 TYR C  467 ? TYR C 491 . ? 1_555 ? 
195 BC1 24 HOH IA .   ? HOH C 704 . ? 1_555 ? 
196 BC1 24 HOH IA .   ? HOH C 851 . ? 1_555 ? 
197 BC2 21 TYR C  116 ? TYR C 140 . ? 1_555 ? 
198 BC2 21 LYS C  117 ? LYS C 141 . ? 1_555 ? 
199 BC2 21 CYS C  172 ? CYS C 196 . ? 1_555 ? 
200 BC2 21 HIS C  176 ? HIS C 200 . ? 1_555 ? 
201 BC2 21 GLU C  179 ? GLU C 203 . ? 1_555 ? 
202 BC2 21 HIS C  204 ? HIS C 228 . ? 1_555 ? 
203 BC2 21 ASN C  235 ? ASN C 259 . ? 1_555 ? 
204 BC2 21 CYS C  239 ? CYS C 263 . ? 1_555 ? 
205 BC2 21 CYS C  242 ? CYS C 266 . ? 1_555 ? 
206 BC2 21 HIS C  243 ? HIS C 267 . ? 1_555 ? 
207 BC2 21 SER C  253 ? SER C 277 . ? 1_555 ? 
208 BC2 21 ARG C  254 ? ARG C 278 . ? 1_555 ? 
209 BC2 21 ARG C  295 ? ARG C 319 . ? 1_555 ? 
210 BC2 21 LEU C  296 ? LEU C 320 . ? 1_555 ? 
211 BC2 21 MET C  315 ? MET C 339 . ? 1_555 ? 
212 BC2 21 HIS C  323 ? HIS C 347 . ? 1_555 ? 
213 BC2 21 HEC R  .   ? HEC C 603 . ? 1_555 ? 
214 BC2 21 HEC V  .   ? HEC C 607 . ? 1_555 ? 
215 BC2 21 HOH IA .   ? HOH C 710 . ? 1_555 ? 
216 BC2 21 HOH IA .   ? HOH C 770 . ? 1_555 ? 
217 BC2 21 HOH IA .   ? HOH C 873 . ? 1_555 ? 
218 BC3 19 THR C  98  ? THR C 122 . ? 1_555 ? 
219 BC3 19 HIS C  99  ? HIS C 123 . ? 1_555 ? 
220 BC3 19 LYS C  117 ? LYS C 141 . ? 1_555 ? 
221 BC3 19 LYS C  120 ? LYS C 144 . ? 1_555 ? 
222 BC3 19 LEU C  121 ? LEU C 145 . ? 1_555 ? 
223 BC3 19 VAL C  143 ? VAL C 167 . ? 1_555 ? 
224 BC3 19 VAL C  152 ? VAL C 176 . ? 1_555 ? 
225 BC3 19 CYS C  172 ? CYS C 196 . ? 1_555 ? 
226 BC3 19 CYS C  175 ? CYS C 199 . ? 1_555 ? 
227 BC3 19 HIS C  176 ? HIS C 200 . ? 1_555 ? 
228 BC3 19 CYS C  239 ? CYS C 263 . ? 1_555 ? 
229 BC3 19 HIS C  243 ? HIS C 267 . ? 1_555 ? 
230 BC3 19 PHE C  248 ? PHE C 272 . ? 1_555 ? 
231 BC3 19 SER C  249 ? SER C 273 . ? 1_555 ? 
232 BC3 19 ALA C  250 ? ALA C 274 . ? 1_555 ? 
233 BC3 19 HEC Q  .   ? HEC C 602 . ? 1_555 ? 
234 BC3 19 HEC T  .   ? HEC C 605 . ? 1_555 ? 
235 BC3 19 HOH IA .   ? HOH C 798 . ? 1_555 ? 
236 BC3 19 HOH IA .   ? HOH C 824 . ? 1_555 ? 
237 BC4 20 LYS A  137 ? LYS A 161 . ? 4_455 ? 
238 BC4 20 TYR C  57  ? TYR C 81  . ? 1_555 ? 
239 BC4 20 TYR C  64  ? TYR C 88  . ? 1_555 ? 
240 BC4 20 PRO C  70  ? PRO C 94  . ? 1_555 ? 
241 BC4 20 ASP C  78  ? ASP C 102 . ? 1_555 ? 
242 BC4 20 CYS C  79  ? CYS C 103 . ? 1_555 ? 
243 BC4 20 CYS C  82  ? CYS C 106 . ? 1_555 ? 
244 BC4 20 HIS C  83  ? HIS C 107 . ? 1_555 ? 
245 BC4 20 GLU C  86  ? GLU C 110 . ? 1_555 ? 
246 BC4 20 CYS C  145 ? CYS C 169 . ? 1_555 ? 
247 BC4 20 HIS C  149 ? HIS C 173 . ? 1_555 ? 
248 BC4 20 HIS C  160 ? HIS C 184 . ? 1_555 ? 
249 BC4 20 ILE C  164 ? ILE C 188 . ? 1_555 ? 
250 BC4 20 MET C  166 ? MET C 190 . ? 1_555 ? 
251 BC4 20 HEC T  .   ? HEC C 605 . ? 1_555 ? 
252 BC4 20 HOH IA .   ? HOH C 778 . ? 1_555 ? 
253 BC4 20 HOH IA .   ? HOH C 817 . ? 1_555 ? 
254 BC4 20 SER E  365 ? SER E 389 . ? 1_555 ? 
255 BC4 20 GLU E  366 ? GLU E 390 . ? 1_555 ? 
256 BC4 20 ARG E  367 ? ARG E 391 . ? 1_555 ? 
257 BC5 22 TYR C  57  ? TYR C 81  . ? 1_555 ? 
258 BC5 22 PRO C  60  ? PRO C 84  . ? 1_555 ? 
259 BC5 22 HIS C  83  ? HIS C 107 . ? 1_555 ? 
260 BC5 22 TRP C  90  ? TRP C 114 . ? 1_555 ? 
261 BC5 22 HIS C  99  ? HIS C 123 . ? 1_555 ? 
262 BC5 22 VAL C  143 ? VAL C 167 . ? 1_555 ? 
263 BC5 22 GLY C  144 ? GLY C 168 . ? 1_555 ? 
264 BC5 22 CYS C  145 ? CYS C 169 . ? 1_555 ? 
265 BC5 22 CYS C  148 ? CYS C 172 . ? 1_555 ? 
266 BC5 22 HIS C  149 ? HIS C 173 . ? 1_555 ? 
267 BC5 22 MET C  166 ? MET C 190 . ? 1_555 ? 
268 BC5 22 PRO C  167 ? PRO C 191 . ? 1_555 ? 
269 BC5 22 LYS C  238 ? LYS C 262 . ? 1_555 ? 
270 BC5 22 ASP C  240 ? ASP C 264 . ? 1_555 ? 
271 BC5 22 ARG C  245 ? ARG C 269 . ? 1_555 ? 
272 BC5 22 HIS C  246 ? HIS C 270 . ? 1_555 ? 
273 BC5 22 PHE C  248 ? PHE C 272 . ? 1_555 ? 
274 BC5 22 HEC R  .   ? HEC C 603 . ? 1_555 ? 
275 BC5 22 HEC S  .   ? HEC C 604 . ? 1_555 ? 
276 BC5 22 HIS E  364 ? HIS E 388 . ? 1_555 ? 
277 BC5 22 SER E  365 ? SER E 389 . ? 1_555 ? 
278 BC5 22 HOH KA .   ? HOH E 757 . ? 1_555 ? 
279 BC6 21 HIS C  263 ? HIS C 287 . ? 1_555 ? 
280 BC6 21 ASN C  270 ? ASN C 294 . ? 1_555 ? 
281 BC6 21 TYR C  274 ? TYR C 298 . ? 1_555 ? 
282 BC6 21 PRO C  308 ? PRO C 332 . ? 1_555 ? 
283 BC6 21 THR C  309 ? THR C 333 . ? 1_555 ? 
284 BC6 21 CYS C  310 ? CYS C 334 . ? 1_555 ? 
285 BC6 21 CYS C  313 ? CYS C 337 . ? 1_555 ? 
286 BC6 21 HIS C  314 ? HIS C 338 . ? 1_555 ? 
287 BC6 21 THR C  329 ? THR C 353 . ? 1_555 ? 
288 BC6 21 ARG C  330 ? ARG C 354 . ? 1_555 ? 
289 BC6 21 TRP C  331 ? TRP C 355 . ? 1_555 ? 
290 BC6 21 ALA C  332 ? ALA C 356 . ? 1_555 ? 
291 BC6 21 TRP C  356 ? TRP C 380 . ? 1_555 ? 
292 BC6 21 MET C  376 ? MET C 400 . ? 1_555 ? 
293 BC6 21 ALA C  458 ? ALA C 482 . ? 1_555 ? 
294 BC6 21 HIS C  459 ? HIS C 483 . ? 1_555 ? 
295 BC6 21 HEC V  .   ? HEC C 607 . ? 1_555 ? 
296 BC6 21 HEC W  .   ? HEC C 608 . ? 1_555 ? 
297 BC6 21 HOH IA .   ? HOH C 702 . ? 1_555 ? 
298 BC6 21 HOH IA .   ? HOH C 840 . ? 1_555 ? 
299 BC6 21 HEC X  .   ? HEC E 601 . ? 1_555 ? 
300 BC7 22 PRO C  202 ? PRO C 226 . ? 1_555 ? 
301 BC7 22 SER C  203 ? SER C 227 . ? 1_555 ? 
302 BC7 22 HIS C  204 ? HIS C 228 . ? 1_555 ? 
303 BC7 22 ASP C  207 ? ASP C 231 . ? 1_555 ? 
304 BC7 22 ALA C  210 ? ALA C 234 . ? 1_555 ? 
305 BC7 22 CYS C  232 ? CYS C 256 . ? 1_555 ? 
306 BC7 22 HIS C  233 ? HIS C 257 . ? 1_555 ? 
307 BC7 22 ASN C  235 ? ASN C 259 . ? 1_555 ? 
308 BC7 22 ASN C  241 ? ASN C 265 . ? 1_555 ? 
309 BC7 22 CYS C  242 ? CYS C 266 . ? 1_555 ? 
310 BC7 22 ALA C  258 ? ALA C 282 . ? 1_555 ? 
311 BC7 22 CYS C  259 ? CYS C 283 . ? 1_555 ? 
312 BC7 22 CYS C  262 ? CYS C 286 . ? 1_555 ? 
313 BC7 22 HIS C  263 ? HIS C 287 . ? 1_555 ? 
314 BC7 22 CYS C  310 ? CYS C 334 . ? 1_555 ? 
315 BC7 22 ILE C  325 ? ILE C 349 . ? 1_555 ? 
316 BC7 22 THR C  329 ? THR C 353 . ? 1_555 ? 
317 BC7 22 ALA C  332 ? ALA C 356 . ? 1_555 ? 
318 BC7 22 HEC Q  .   ? HEC C 602 . ? 1_555 ? 
319 BC7 22 HEC U  .   ? HEC C 606 . ? 1_555 ? 
320 BC7 22 HOH IA .   ? HOH C 857 . ? 1_555 ? 
321 BC7 22 HEC X  .   ? HEC E 601 . ? 1_555 ? 
322 BC8 19 LYS A  238 ? LYS A 262 . ? 1_555 ? 
323 BC8 19 ASP A  240 ? ASP A 264 . ? 1_555 ? 
324 BC8 19 THR A  244 ? THR A 268 . ? 1_555 ? 
325 BC8 19 ARG A  245 ? ARG A 269 . ? 1_555 ? 
326 BC8 19 HOH GA .   ? HOH A 808 . ? 1_555 ? 
327 BC8 19 HIS C  279 ? HIS C 303 . ? 1_555 ? 
328 BC8 19 PHE C  300 ? PHE C 324 . ? 1_555 ? 
329 BC8 19 ASN C  306 ? ASN C 330 . ? 1_555 ? 
330 BC8 19 PRO C  308 ? PRO C 332 . ? 1_555 ? 
331 BC8 19 THR C  359 ? THR C 383 . ? 1_555 ? 
332 BC8 19 CYS C  360 ? CYS C 384 . ? 1_555 ? 
333 BC8 19 CYS C  363 ? CYS C 387 . ? 1_555 ? 
334 BC8 19 HIS C  364 ? HIS C 388 . ? 1_555 ? 
335 BC8 19 PHE C  368 ? PHE C 392 . ? 1_555 ? 
336 BC8 19 TYR C  372 ? TYR C 396 . ? 1_555 ? 
337 BC8 19 VAL C  460 ? VAL C 484 . ? 1_555 ? 
338 BC8 19 HEC U  .   ? HEC C 606 . ? 1_555 ? 
339 BC8 19 HOH IA .   ? HOH C 776 . ? 1_555 ? 
340 BC8 19 HOH IA .   ? HOH C 812 . ? 1_555 ? 
341 BC9 23 TRP C  197 ? TRP C 221 . ? 1_555 ? 
342 BC9 23 ARG C  201 ? ARG C 225 . ? 1_555 ? 
343 BC9 23 ALA C  210 ? ALA C 234 . ? 1_555 ? 
344 BC9 23 ASN C  211 ? ASN C 235 . ? 1_555 ? 
345 BC9 23 THR C  214 ? THR C 238 . ? 1_555 ? 
346 BC9 23 GLY C  228 ? GLY C 252 . ? 1_555 ? 
347 BC9 23 CYS C  229 ? CYS C 253 . ? 1_555 ? 
348 BC9 23 CYS C  232 ? CYS C 256 . ? 1_555 ? 
349 BC9 23 HIS C  233 ? HIS C 257 . ? 1_555 ? 
350 BC9 23 THR C  261 ? THR C 285 . ? 1_555 ? 
351 BC9 23 CYS C  262 ? CYS C 286 . ? 1_555 ? 
352 BC9 23 HIS C  263 ? HIS C 287 . ? 1_555 ? 
353 BC9 23 HIS C  268 ? HIS C 292 . ? 1_555 ? 
354 BC9 23 ASN C  333 ? ASN C 357 . ? 1_555 ? 
355 BC9 23 PHE C  428 ? PHE C 452 . ? 1_555 ? 
356 BC9 23 HEC U  .   ? HEC C 606 . ? 1_555 ? 
357 BC9 23 HEC V  .   ? HEC C 607 . ? 1_555 ? 
358 BC9 23 HOH IA .   ? HOH C 729 . ? 1_555 ? 
359 BC9 23 THR E  466 ? THR E 490 . ? 1_555 ? 
360 BC9 23 TYR E  467 ? TYR E 491 . ? 1_555 ? 
361 BC9 23 HOH KA .   ? HOH E 704 . ? 1_555 ? 
362 BC9 23 HOH KA .   ? HOH E 753 . ? 1_555 ? 
363 BC9 23 HOH KA .   ? HOH E 948 . ? 1_555 ? 
364 CC1 21 TYR E  116 ? TYR E 140 . ? 1_555 ? 
365 CC1 21 LYS E  117 ? LYS E 141 . ? 1_555 ? 
366 CC1 21 CYS E  172 ? CYS E 196 . ? 1_555 ? 
367 CC1 21 HIS E  176 ? HIS E 200 . ? 1_555 ? 
368 CC1 21 GLU E  179 ? GLU E 203 . ? 1_555 ? 
369 CC1 21 HIS E  204 ? HIS E 228 . ? 1_555 ? 
370 CC1 21 ASN E  235 ? ASN E 259 . ? 1_555 ? 
371 CC1 21 CYS E  239 ? CYS E 263 . ? 1_555 ? 
372 CC1 21 CYS E  242 ? CYS E 266 . ? 1_555 ? 
373 CC1 21 HIS E  243 ? HIS E 267 . ? 1_555 ? 
374 CC1 21 SER E  253 ? SER E 277 . ? 1_555 ? 
375 CC1 21 ARG E  254 ? ARG E 278 . ? 1_555 ? 
376 CC1 21 ARG E  295 ? ARG E 319 . ? 1_555 ? 
377 CC1 21 LEU E  296 ? LEU E 320 . ? 1_555 ? 
378 CC1 21 MET E  315 ? MET E 339 . ? 1_555 ? 
379 CC1 21 HIS E  323 ? HIS E 347 . ? 1_555 ? 
380 CC1 21 HEC Z  .   ? HEC E 603 . ? 1_555 ? 
381 CC1 21 HEC DA .   ? HEC E 607 . ? 1_555 ? 
382 CC1 21 HOH KA .   ? HOH E 799 . ? 1_555 ? 
383 CC1 21 HOH KA .   ? HOH E 851 . ? 1_555 ? 
384 CC1 21 HOH KA .   ? HOH E 886 . ? 1_555 ? 
385 CC2 17 THR E  98  ? THR E 122 . ? 1_555 ? 
386 CC2 17 HIS E  99  ? HIS E 123 . ? 1_555 ? 
387 CC2 17 LYS E  117 ? LYS E 141 . ? 1_555 ? 
388 CC2 17 LYS E  120 ? LYS E 144 . ? 1_555 ? 
389 CC2 17 LEU E  121 ? LEU E 145 . ? 1_555 ? 
390 CC2 17 VAL E  143 ? VAL E 167 . ? 1_555 ? 
391 CC2 17 CYS E  172 ? CYS E 196 . ? 1_555 ? 
392 CC2 17 CYS E  175 ? CYS E 199 . ? 1_555 ? 
393 CC2 17 HIS E  176 ? HIS E 200 . ? 1_555 ? 
394 CC2 17 CYS E  239 ? CYS E 263 . ? 1_555 ? 
395 CC2 17 HIS E  243 ? HIS E 267 . ? 1_555 ? 
396 CC2 17 PHE E  248 ? PHE E 272 . ? 1_555 ? 
397 CC2 17 ALA E  250 ? ALA E 274 . ? 1_555 ? 
398 CC2 17 HEC Y  .   ? HEC E 602 . ? 1_555 ? 
399 CC2 17 HEC BA .   ? HEC E 605 . ? 1_555 ? 
400 CC2 17 HOH KA .   ? HOH E 765 . ? 1_555 ? 
401 CC2 17 HOH KA .   ? HOH E 891 . ? 1_555 ? 
402 CC3 18 SER A  365 ? SER A 389 . ? 1_555 ? 
403 CC3 18 GLU A  366 ? GLU A 390 . ? 1_555 ? 
404 CC3 18 ARG A  367 ? ARG A 391 . ? 1_555 ? 
405 CC3 18 TYR E  57  ? TYR E 81  . ? 1_555 ? 
406 CC3 18 TYR E  64  ? TYR E 88  . ? 1_555 ? 
407 CC3 18 PRO E  70  ? PRO E 94  . ? 1_555 ? 
408 CC3 18 GLU E  72  ? GLU E 96  . ? 1_555 ? 
409 CC3 18 ASP E  78  ? ASP E 102 . ? 1_555 ? 
410 CC3 18 CYS E  79  ? CYS E 103 . ? 1_555 ? 
411 CC3 18 CYS E  82  ? CYS E 106 . ? 1_555 ? 
412 CC3 18 HIS E  83  ? HIS E 107 . ? 1_555 ? 
413 CC3 18 GLU E  86  ? GLU E 110 . ? 1_555 ? 
414 CC3 18 HIS E  149 ? HIS E 173 . ? 1_555 ? 
415 CC3 18 HIS E  160 ? HIS E 184 . ? 1_555 ? 
416 CC3 18 ILE E  164 ? ILE E 188 . ? 1_555 ? 
417 CC3 18 HEC BA .   ? HEC E 605 . ? 1_555 ? 
418 CC3 18 HOH KA .   ? HOH E 792 . ? 1_555 ? 
419 CC3 18 HOH KA .   ? HOH E 993 . ? 1_555 ? 
420 CC4 22 HIS A  364 ? HIS A 388 . ? 1_555 ? 
421 CC4 22 SER A  365 ? SER A 389 . ? 1_555 ? 
422 CC4 22 HOH GA .   ? HOH A 709 . ? 1_555 ? 
423 CC4 22 TYR E  57  ? TYR E 81  . ? 1_555 ? 
424 CC4 22 PRO E  60  ? PRO E 84  . ? 1_555 ? 
425 CC4 22 HIS E  83  ? HIS E 107 . ? 1_555 ? 
426 CC4 22 TRP E  90  ? TRP E 114 . ? 1_555 ? 
427 CC4 22 HIS E  99  ? HIS E 123 . ? 1_555 ? 
428 CC4 22 VAL E  143 ? VAL E 167 . ? 1_555 ? 
429 CC4 22 GLY E  144 ? GLY E 168 . ? 1_555 ? 
430 CC4 22 CYS E  145 ? CYS E 169 . ? 1_555 ? 
431 CC4 22 CYS E  148 ? CYS E 172 . ? 1_555 ? 
432 CC4 22 HIS E  149 ? HIS E 173 . ? 1_555 ? 
433 CC4 22 MET E  166 ? MET E 190 . ? 1_555 ? 
434 CC4 22 PRO E  167 ? PRO E 191 . ? 1_555 ? 
435 CC4 22 LYS E  238 ? LYS E 262 . ? 1_555 ? 
436 CC4 22 ASP E  240 ? ASP E 264 . ? 1_555 ? 
437 CC4 22 ARG E  245 ? ARG E 269 . ? 1_555 ? 
438 CC4 22 HIS E  246 ? HIS E 270 . ? 1_555 ? 
439 CC4 22 PHE E  248 ? PHE E 272 . ? 1_555 ? 
440 CC4 22 HEC Z  .   ? HEC E 603 . ? 1_555 ? 
441 CC4 22 HEC AA .   ? HEC E 604 . ? 1_555 ? 
442 CC5 21 HEC N  .   ? HEC A 608 . ? 1_555 ? 
443 CC5 21 CYS E  259 ? CYS E 283 . ? 1_555 ? 
444 CC5 21 HIS E  263 ? HIS E 287 . ? 1_555 ? 
445 CC5 21 ASN E  270 ? ASN E 294 . ? 1_555 ? 
446 CC5 21 TYR E  274 ? TYR E 298 . ? 1_555 ? 
447 CC5 21 PRO E  308 ? PRO E 332 . ? 1_555 ? 
448 CC5 21 THR E  309 ? THR E 333 . ? 1_555 ? 
449 CC5 21 CYS E  310 ? CYS E 334 . ? 1_555 ? 
450 CC5 21 CYS E  313 ? CYS E 337 . ? 1_555 ? 
451 CC5 21 HIS E  314 ? HIS E 338 . ? 1_555 ? 
452 CC5 21 THR E  329 ? THR E 353 . ? 1_555 ? 
453 CC5 21 ARG E  330 ? ARG E 354 . ? 1_555 ? 
454 CC5 21 TRP E  331 ? TRP E 355 . ? 1_555 ? 
455 CC5 21 ALA E  332 ? ALA E 356 . ? 1_555 ? 
456 CC5 21 TRP E  356 ? TRP E 380 . ? 1_555 ? 
457 CC5 21 MET E  376 ? MET E 400 . ? 1_555 ? 
458 CC5 21 ALA E  458 ? ALA E 482 . ? 1_555 ? 
459 CC5 21 HIS E  459 ? HIS E 483 . ? 1_555 ? 
460 CC5 21 HEC DA .   ? HEC E 607 . ? 1_555 ? 
461 CC5 21 HEC EA .   ? HEC E 608 . ? 1_555 ? 
462 CC5 21 HOH KA .   ? HOH E 706 . ? 1_555 ? 
463 CC6 23 HEC N  .   ? HEC A 608 . ? 1_555 ? 
464 CC6 23 PRO E  202 ? PRO E 226 . ? 1_555 ? 
465 CC6 23 SER E  203 ? SER E 227 . ? 1_555 ? 
466 CC6 23 HIS E  204 ? HIS E 228 . ? 1_555 ? 
467 CC6 23 ASP E  207 ? ASP E 231 . ? 1_555 ? 
468 CC6 23 ALA E  210 ? ALA E 234 . ? 1_555 ? 
469 CC6 23 CYS E  232 ? CYS E 256 . ? 1_555 ? 
470 CC6 23 HIS E  233 ? HIS E 257 . ? 1_555 ? 
471 CC6 23 ASN E  235 ? ASN E 259 . ? 1_555 ? 
472 CC6 23 ASN E  241 ? ASN E 265 . ? 1_555 ? 
473 CC6 23 CYS E  242 ? CYS E 266 . ? 1_555 ? 
474 CC6 23 ALA E  258 ? ALA E 282 . ? 1_555 ? 
475 CC6 23 CYS E  259 ? CYS E 283 . ? 1_555 ? 
476 CC6 23 CYS E  262 ? CYS E 286 . ? 1_555 ? 
477 CC6 23 HIS E  263 ? HIS E 287 . ? 1_555 ? 
478 CC6 23 CYS E  310 ? CYS E 334 . ? 1_555 ? 
479 CC6 23 HIS E  314 ? HIS E 338 . ? 1_555 ? 
480 CC6 23 ILE E  325 ? ILE E 349 . ? 1_555 ? 
481 CC6 23 THR E  329 ? THR E 353 . ? 1_555 ? 
482 CC6 23 ALA E  332 ? ALA E 356 . ? 1_555 ? 
483 CC6 23 HEC Y  .   ? HEC E 602 . ? 1_555 ? 
484 CC6 23 HEC CA .   ? HEC E 606 . ? 1_555 ? 
485 CC6 23 HOH KA .   ? HOH E 717 . ? 1_555 ? 
486 CC7 21 TRP C  90  ? TRP C 114 . ? 1_555 ? 
487 CC7 21 LYS C  238 ? LYS C 262 . ? 1_555 ? 
488 CC7 21 ASP C  240 ? ASP C 264 . ? 1_555 ? 
489 CC7 21 THR C  244 ? THR C 268 . ? 1_555 ? 
490 CC7 21 ARG C  245 ? ARG C 269 . ? 1_555 ? 
491 CC7 21 HOH IA .   ? HOH C 735 . ? 1_555 ? 
492 CC7 21 HIS E  279 ? HIS E 303 . ? 1_555 ? 
493 CC7 21 LEU E  282 ? LEU E 306 . ? 1_555 ? 
494 CC7 21 ASN E  306 ? ASN E 330 . ? 1_555 ? 
495 CC7 21 PRO E  308 ? PRO E 332 . ? 1_555 ? 
496 CC7 21 THR E  359 ? THR E 383 . ? 1_555 ? 
497 CC7 21 CYS E  360 ? CYS E 384 . ? 1_555 ? 
498 CC7 21 CYS E  363 ? CYS E 387 . ? 1_555 ? 
499 CC7 21 HIS E  364 ? HIS E 388 . ? 1_555 ? 
500 CC7 21 PHE E  368 ? PHE E 392 . ? 1_555 ? 
501 CC7 21 TYR E  372 ? TYR E 396 . ? 1_555 ? 
502 CC7 21 VAL E  460 ? VAL E 484 . ? 1_555 ? 
503 CC7 21 HEC CA .   ? HEC E 606 . ? 1_555 ? 
504 CC7 21 HOH KA .   ? HOH E 757 . ? 1_555 ? 
505 CC7 21 HOH KA .   ? HOH E 776 . ? 1_555 ? 
506 CC7 21 HOH KA .   ? HOH E 782 . ? 1_555 ? 
507 CC8 5  LEU E  15  ? LEU E 39  . ? 1_555 ? 
508 CC8 5  ASP E  16  ? ASP E 40  . ? 1_555 ? 
509 CC8 5  LYS E  19  ? LYS E 43  . ? 1_555 ? 
510 CC8 5  GLU E  24  ? GLU E 48  . ? 1_555 ? 
511 CC8 5  HOH KA .   ? HOH E 989 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4N4N 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4N4N 
_atom_sites.fract_transf_matrix[1][1]   0.007106 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007044 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.009370 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
FE 
K  
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ASP A  1 1   ? 58.667  69.671  7.056   1.00 32.75 ?  25   ASP A N   1 
ATOM   2     C  CA  . ASP A  1 1   ? 57.486  69.767  7.961   1.00 32.80 ?  25   ASP A CA  1 
ATOM   3     C  C   . ASP A  1 1   ? 56.604  68.524  7.856   1.00 32.73 ?  25   ASP A C   1 
ATOM   4     O  O   . ASP A  1 1   ? 56.495  67.914  6.789   1.00 32.72 ?  25   ASP A O   1 
ATOM   5     C  CB  . ASP A  1 1   ? 56.664  71.019  7.629   1.00 32.88 ?  25   ASP A CB  1 
ATOM   6     C  CG  . ASP A  1 1   ? 55.738  71.448  8.768   1.00 33.49 ?  25   ASP A CG  1 
ATOM   7     O  OD1 . ASP A  1 1   ? 55.678  70.761  9.815   1.00 33.97 ?  25   ASP A OD1 1 
ATOM   8     O  OD2 . ASP A  1 1   ? 55.065  72.490  8.616   1.00 33.80 -1 25   ASP A OD2 1 
ATOM   9     N  N   . ILE A  1 2   ? 55.992  68.149  8.977   1.00 32.64 ?  26   ILE A N   1 
ATOM   10    C  CA  . ILE A  1 2   ? 54.968  67.107  8.996   1.00 32.39 ?  26   ILE A CA  1 
ATOM   11    C  C   . ILE A  1 2   ? 53.608  67.788  9.144   1.00 32.28 ?  26   ILE A C   1 
ATOM   12    O  O   . ILE A  1 2   ? 53.243  68.242  10.233  1.00 32.04 ?  26   ILE A O   1 
ATOM   13    C  CB  . ILE A  1 2   ? 55.203  66.073  10.126  1.00 32.41 ?  26   ILE A CB  1 
ATOM   14    C  CG1 . ILE A  1 2   ? 56.630  65.514  10.050  1.00 32.39 ?  26   ILE A CG1 1 
ATOM   15    C  CG2 . ILE A  1 2   ? 54.175  64.940  10.035  1.00 32.16 ?  26   ILE A CG2 1 
ATOM   16    C  CD1 . ILE A  1 2   ? 57.105  64.812  11.314  1.00 32.33 ?  26   ILE A CD1 1 
ATOM   17    N  N   . SER A  1 3   ? 52.877  67.855  8.032   1.00 32.07 ?  27   SER A N   1 
ATOM   18    C  CA  . SER A  1 3   ? 51.649  68.652  7.915   1.00 31.91 ?  27   SER A CA  1 
ATOM   19    C  C   . SER A  1 3   ? 50.535  68.289  8.901   1.00 31.68 ?  27   SER A C   1 
ATOM   20    O  O   . SER A  1 3   ? 49.674  69.115  9.203   1.00 31.61 ?  27   SER A O   1 
ATOM   21    C  CB  . SER A  1 3   ? 51.105  68.558  6.488   1.00 31.99 ?  27   SER A CB  1 
ATOM   22    O  OG  . SER A  1 3   ? 50.782  67.217  6.158   1.00 31.77 ?  27   SER A OG  1 
ATOM   23    N  N   . THR A  1 4   ? 50.559  67.056  9.393   1.00 31.36 ?  28   THR A N   1 
ATOM   24    C  CA  . THR A  1 4   ? 49.499  66.544  10.256  1.00 31.05 ?  28   THR A CA  1 
ATOM   25    C  C   . THR A  1 4   ? 49.836  66.632  11.750  1.00 31.01 ?  28   THR A C   1 
ATOM   26    O  O   . THR A  1 4   ? 49.046  66.206  12.598  1.00 31.08 ?  28   THR A O   1 
ATOM   27    C  CB  . THR A  1 4   ? 49.141  65.090  9.883   1.00 31.06 ?  28   THR A CB  1 
ATOM   28    O  OG1 . THR A  1 4   ? 50.338  64.304  9.818   1.00 30.50 ?  28   THR A OG1 1 
ATOM   29    C  CG2 . THR A  1 4   ? 48.428  65.040  8.533   1.00 30.87 ?  28   THR A CG2 1 
ATOM   30    N  N   . VAL A  1 5   ? 51.002  67.191  12.065  1.00 30.85 ?  29   VAL A N   1 
ATOM   31    C  CA  . VAL A  1 5   ? 51.424  67.383  13.456  1.00 30.93 ?  29   VAL A CA  1 
ATOM   32    C  C   . VAL A  1 5   ? 51.095  68.806  13.935  1.00 31.01 ?  29   VAL A C   1 
ATOM   33    O  O   . VAL A  1 5   ? 51.451  69.779  13.272  1.00 30.92 ?  29   VAL A O   1 
ATOM   34    C  CB  . VAL A  1 5   ? 52.933  67.044  13.651  1.00 30.83 ?  29   VAL A CB  1 
ATOM   35    C  CG1 . VAL A  1 5   ? 53.395  67.334  15.079  1.00 30.72 ?  29   VAL A CG1 1 
ATOM   36    C  CG2 . VAL A  1 5   ? 53.181  65.591  13.325  1.00 30.81 ?  29   VAL A CG2 1 
ATOM   37    N  N   . PRO A  1 6   ? 50.393  68.921  15.081  1.00 31.19 ?  30   PRO A N   1 
ATOM   38    C  CA  . PRO A  1 6   ? 49.985  70.196  15.689  1.00 31.39 ?  30   PRO A CA  1 
ATOM   39    C  C   . PRO A  1 6   ? 51.156  71.112  16.054  1.00 31.59 ?  30   PRO A C   1 
ATOM   40    O  O   . PRO A  1 6   ? 52.235  70.624  16.408  1.00 31.34 ?  30   PRO A O   1 
ATOM   41    C  CB  . PRO A  1 6   ? 49.269  69.756  16.971  1.00 31.32 ?  30   PRO A CB  1 
ATOM   42    C  CG  . PRO A  1 6   ? 48.813  68.376  16.696  1.00 31.25 ?  30   PRO A CG  1 
ATOM   43    C  CD  . PRO A  1 6   ? 49.869  67.769  15.836  1.00 31.20 ?  30   PRO A CD  1 
ATOM   44    N  N   . ASP A  1 7   ? 50.920  72.424  15.970  1.00 31.88 ?  31   ASP A N   1 
ATOM   45    C  CA  . ASP A  1 7   ? 51.889  73.457  16.364  1.00 32.38 ?  31   ASP A CA  1 
ATOM   46    C  C   . ASP A  1 7   ? 52.445  73.245  17.774  1.00 32.46 ?  31   ASP A C   1 
ATOM   47    O  O   . ASP A  1 7   ? 53.649  73.390  17.999  1.00 32.41 ?  31   ASP A O   1 
ATOM   48    C  CB  . ASP A  1 7   ? 51.251  74.855  16.300  1.00 32.51 ?  31   ASP A CB  1 
ATOM   49    C  CG  . ASP A  1 7   ? 51.061  75.365  14.877  1.00 33.01 ?  31   ASP A CG  1 
ATOM   50    O  OD1 . ASP A  1 7   ? 51.794  74.928  13.957  1.00 32.78 ?  31   ASP A OD1 1 
ATOM   51    O  OD2 . ASP A  1 7   ? 50.170  76.223  14.686  1.00 33.95 -1 31   ASP A OD2 1 
ATOM   52    N  N   . GLU A  1 8   ? 51.557  72.905  18.710  1.00 32.58 ?  32   GLU A N   1 
ATOM   53    C  CA  . GLU A  1 8   ? 51.913  72.730  20.125  1.00 32.90 ?  32   GLU A CA  1 
ATOM   54    C  C   . GLU A  1 8   ? 52.959  71.646  20.384  1.00 32.65 ?  32   GLU A C   1 
ATOM   55    O  O   . GLU A  1 8   ? 53.642  71.679  21.407  1.00 32.63 ?  32   GLU A O   1 
ATOM   56    C  CB  . GLU A  1 8   ? 50.670  72.501  21.004  1.00 33.10 ?  32   GLU A CB  1 
ATOM   57    C  CG  . GLU A  1 8   ? 49.572  71.660  20.375  1.00 34.47 ?  32   GLU A CG  1 
ATOM   58    C  CD  . GLU A  1 8   ? 48.539  72.504  19.645  1.00 35.78 ?  32   GLU A CD  1 
ATOM   59    O  OE1 . GLU A  1 8   ? 48.709  72.744  18.432  1.00 36.19 ?  32   GLU A OE1 1 
ATOM   60    O  OE2 . GLU A  1 8   ? 47.563  72.938  20.290  1.00 37.28 -1 32   GLU A OE2 1 
ATOM   61    N  N   . THR A  1 9   ? 53.089  70.699  19.456  1.00 32.47 ?  33   THR A N   1 
ATOM   62    C  CA  . THR A  1 9   ? 54.119  69.666  19.551  1.00 32.31 ?  33   THR A CA  1 
ATOM   63    C  C   . THR A  1 9   ? 55.506  70.241  19.263  1.00 32.41 ?  33   THR A C   1 
ATOM   64    O  O   . THR A  1 9   ? 56.448  70.003  20.018  1.00 32.32 ?  33   THR A O   1 
ATOM   65    C  CB  . THR A  1 9   ? 53.819  68.474  18.622  1.00 32.27 ?  33   THR A CB  1 
ATOM   66    O  OG1 . THR A  1 9   ? 52.581  67.875  19.019  1.00 31.94 ?  33   THR A OG1 1 
ATOM   67    C  CG2 . THR A  1 9   ? 54.931  67.424  18.693  1.00 32.00 ?  33   THR A CG2 1 
ATOM   68    N  N   . TYR A  1 10  ? 55.618  71.000  18.176  1.00 32.50 ?  34   TYR A N   1 
ATOM   69    C  CA  . TYR A  1 10  ? 56.868  71.678  17.833  1.00 32.61 ?  34   TYR A CA  1 
ATOM   70    C  C   . TYR A  1 10  ? 57.273  72.718  18.881  1.00 32.90 ?  34   TYR A C   1 
ATOM   71    O  O   . TYR A  1 10  ? 58.460  72.882  19.167  1.00 33.16 ?  34   TYR A O   1 
ATOM   72    C  CB  . TYR A  1 10  ? 56.780  72.295  16.436  1.00 32.18 ?  34   TYR A CB  1 
ATOM   73    C  CG  . TYR A  1 10  ? 56.744  71.255  15.332  1.00 31.77 ?  34   TYR A CG  1 
ATOM   74    C  CD1 . TYR A  1 10  ? 57.926  70.721  14.815  1.00 30.57 ?  34   TYR A CD1 1 
ATOM   75    C  CD2 . TYR A  1 10  ? 55.531  70.798  14.813  1.00 31.50 ?  34   TYR A CD2 1 
ATOM   76    C  CE1 . TYR A  1 10  ? 57.905  69.767  13.808  1.00 30.66 ?  34   TYR A CE1 1 
ATOM   77    C  CE2 . TYR A  1 10  ? 55.499  69.838  13.798  1.00 31.22 ?  34   TYR A CE2 1 
ATOM   78    C  CZ  . TYR A  1 10  ? 56.691  69.328  13.304  1.00 31.00 ?  34   TYR A CZ  1 
ATOM   79    O  OH  . TYR A  1 10  ? 56.674  68.380  12.307  1.00 30.93 ?  34   TYR A OH  1 
ATOM   80    N  N   . ASP A  1 11  ? 56.285  73.400  19.455  1.00 33.21 ?  35   ASP A N   1 
ATOM   81    C  CA  . ASP A  1 11  ? 56.524  74.375  20.525  1.00 33.82 ?  35   ASP A CA  1 
ATOM   82    C  C   . ASP A  1 11  ? 57.056  73.726  21.805  1.00 33.89 ?  35   ASP A C   1 
ATOM   83    O  O   . ASP A  1 11  ? 57.964  74.262  22.440  1.00 33.91 ?  35   ASP A O   1 
ATOM   84    C  CB  . ASP A  1 11  ? 55.252  75.183  20.821  1.00 33.90 ?  35   ASP A CB  1 
ATOM   85    C  CG  . ASP A  1 11  ? 54.865  76.112  19.676  1.00 34.76 ?  35   ASP A CG  1 
ATOM   86    O  OD1 . ASP A  1 11  ? 55.729  76.399  18.817  1.00 35.92 ?  35   ASP A OD1 1 
ATOM   87    O  OD2 . ASP A  1 11  ? 53.695  76.558  19.632  1.00 35.43 -1 35   ASP A OD2 1 
ATOM   88    N  N   . ALA A  1 12  ? 56.496  72.571  22.166  1.00 34.13 ?  36   ALA A N   1 
ATOM   89    C  CA  . ALA A  1 12  ? 56.910  71.834  23.364  1.00 34.26 ?  36   ALA A CA  1 
ATOM   90    C  C   . ALA A  1 12  ? 58.330  71.287  23.244  1.00 34.45 ?  36   ALA A C   1 
ATOM   91    O  O   . ALA A  1 12  ? 59.050  71.184  24.241  1.00 34.50 ?  36   ALA A O   1 
ATOM   92    C  CB  . ALA A  1 12  ? 55.930  70.705  23.661  1.00 34.14 ?  36   ALA A CB  1 
ATOM   93    N  N   . LEU A  1 13  ? 58.723  70.945  22.019  1.00 34.63 ?  37   LEU A N   1 
ATOM   94    C  CA  . LEU A  1 13  ? 60.050  70.393  21.740  1.00 34.98 ?  37   LEU A CA  1 
ATOM   95    C  C   . LEU A  1 13  ? 61.056  71.466  21.314  1.00 35.17 ?  37   LEU A C   1 
ATOM   96    O  O   . LEU A  1 13  ? 62.208  71.152  21.004  1.00 35.15 ?  37   LEU A O   1 
ATOM   97    C  CB  . LEU A  1 13  ? 59.955  69.317  20.652  1.00 34.90 ?  37   LEU A CB  1 
ATOM   98    C  CG  . LEU A  1 13  ? 59.020  68.121  20.868  1.00 35.13 ?  37   LEU A CG  1 
ATOM   99    C  CD1 . LEU A  1 13  ? 58.764  67.430  19.539  1.00 34.97 ?  37   LEU A CD1 1 
ATOM   100   C  CD2 . LEU A  1 13  ? 59.564  67.138  21.900  1.00 34.61 ?  37   LEU A CD2 1 
ATOM   101   N  N   . LYS A  1 14  ? 60.609  72.722  21.301  1.00 35.55 ?  38   LYS A N   1 
ATOM   102   C  CA  . LYS A  1 14  ? 61.410  73.872  20.847  1.00 35.93 ?  38   LYS A CA  1 
ATOM   103   C  C   . LYS A  1 14  ? 61.991  73.681  19.443  1.00 35.84 ?  38   LYS A C   1 
ATOM   104   O  O   . LYS A  1 14  ? 63.179  73.918  19.200  1.00 35.83 ?  38   LYS A O   1 
ATOM   105   C  CB  . LYS A  1 14  ? 62.503  74.250  21.861  1.00 36.11 ?  38   LYS A CB  1 
ATOM   106   C  CG  . LYS A  1 14  ? 61.986  75.023  23.073  1.00 37.28 ?  38   LYS A CG  1 
ATOM   107   C  CD  . LYS A  1 14  ? 61.949  74.164  24.332  1.00 39.35 ?  38   LYS A CD  1 
ATOM   108   C  CE  . LYS A  1 14  ? 63.286  74.195  25.071  1.00 40.49 ?  38   LYS A CE  1 
ATOM   109   N  NZ  . LYS A  1 14  ? 63.285  73.325  26.286  1.00 41.51 ?  38   LYS A NZ  1 
ATOM   110   N  N   . LEU A  1 15  ? 61.135  73.245  18.526  1.00 35.72 ?  39   LEU A N   1 
ATOM   111   C  CA  . LEU A  1 15  ? 61.518  73.087  17.133  1.00 35.59 ?  39   LEU A CA  1 
ATOM   112   C  C   . LEU A  1 15  ? 60.771  74.089  16.269  1.00 35.44 ?  39   LEU A C   1 
ATOM   113   O  O   . LEU A  1 15  ? 59.611  74.416  16.538  1.00 35.36 ?  39   LEU A O   1 
ATOM   114   C  CB  . LEU A  1 15  ? 61.219  71.666  16.643  1.00 35.53 ?  39   LEU A CB  1 
ATOM   115   C  CG  . LEU A  1 15  ? 61.968  70.469  17.236  1.00 35.66 ?  39   LEU A CG  1 
ATOM   116   C  CD1 . LEU A  1 15  ? 61.259  69.183  16.844  1.00 35.61 ?  39   LEU A CD1 1 
ATOM   117   C  CD2 . LEU A  1 15  ? 63.428  70.430  16.794  1.00 35.47 ?  39   LEU A CD2 1 
ATOM   118   N  N   . ASP A  1 16  ? 61.451  74.578  15.236  1.00 35.35 ?  40   ASP A N   1 
ATOM   119   C  CA  . ASP A  1 16  ? 60.802  75.345  14.187  1.00 35.20 ?  40   ASP A CA  1 
ATOM   120   C  C   . ASP A  1 16  ? 60.323  74.355  13.129  1.00 34.79 ?  40   ASP A C   1 
ATOM   121   O  O   . ASP A  1 16  ? 61.129  73.678  12.488  1.00 34.64 ?  40   ASP A O   1 
ATOM   122   C  CB  . ASP A  1 16  ? 61.766  76.376  13.587  1.00 35.48 ?  40   ASP A CB  1 
ATOM   123   C  CG  . ASP A  1 16  ? 61.080  77.340  12.624  1.00 36.22 ?  40   ASP A CG  1 
ATOM   124   O  OD1 . ASP A  1 16  ? 60.086  76.952  11.971  1.00 36.87 ?  40   ASP A OD1 1 
ATOM   125   O  OD2 . ASP A  1 16  ? 61.547  78.494  12.513  1.00 37.76 -1 40   ASP A OD2 1 
ATOM   126   N  N   . ARG A  1 17  ? 59.004  74.273  12.961  1.00 34.48 ?  41   ARG A N   1 
ATOM   127   C  CA  . ARG A  1 17  ? 58.398  73.299  12.051  1.00 34.03 ?  41   ARG A CA  1 
ATOM   128   C  C   . ARG A  1 17  ? 58.743  73.544  10.580  1.00 33.93 ?  41   ARG A C   1 
ATOM   129   O  O   . ARG A  1 17  ? 58.739  72.613  9.773   1.00 33.73 ?  41   ARG A O   1 
ATOM   130   C  CB  . ARG A  1 17  ? 56.882  73.212  12.265  1.00 33.95 ?  41   ARG A CB  1 
ATOM   131   C  CG  . ARG A  1 17  ? 56.062  74.416  11.799  1.00 32.96 ?  41   ARG A CG  1 
ATOM   132   C  CD  . ARG A  1 17  ? 54.579  74.152  12.027  1.00 31.95 ?  41   ARG A CD  1 
ATOM   133   N  NE  . ARG A  1 17  ? 54.155  72.903  11.391  1.00 31.43 ?  41   ARG A NE  1 
ATOM   134   C  CZ  . ARG A  1 17  ? 53.271  72.051  11.904  1.00 30.82 ?  41   ARG A CZ  1 
ATOM   135   N  NH1 . ARG A  1 17  ? 52.695  72.296  13.076  1.00 30.13 ?  41   ARG A NH1 1 
ATOM   136   N  NH2 . ARG A  1 17  ? 52.962  70.945  11.241  1.00 30.06 ?  41   ARG A NH2 1 
ATOM   137   N  N   . GLY A  1 18  ? 59.052  74.795  10.246  1.00 33.82 ?  42   GLY A N   1 
ATOM   138   C  CA  . GLY A  1 18  ? 59.480  75.149  8.896   1.00 33.67 ?  42   GLY A CA  1 
ATOM   139   C  C   . GLY A  1 18  ? 60.911  74.738  8.587   1.00 33.69 ?  42   GLY A C   1 
ATOM   140   O  O   . GLY A  1 18  ? 61.296  74.663  7.420   1.00 33.65 ?  42   GLY A O   1 
ATOM   141   N  N   . LYS A  1 19  ? 61.689  74.446  9.629   1.00 33.66 ?  43   LYS A N   1 
ATOM   142   C  CA  . LYS A  1 19  ? 63.131  74.236  9.492   1.00 33.87 ?  43   LYS A CA  1 
ATOM   143   C  C   . LYS A  1 19  ? 63.606  72.836  9.884   1.00 33.63 ?  43   LYS A C   1 
ATOM   144   O  O   . LYS A  1 19  ? 64.482  72.274  9.225   1.00 33.62 ?  43   LYS A O   1 
ATOM   145   C  CB  . LYS A  1 19  ? 63.902  75.289  10.300  1.00 34.03 ?  43   LYS A CB  1 
ATOM   146   C  CG  . LYS A  1 19  ? 63.748  76.716  9.786   1.00 35.28 ?  43   LYS A CG  1 
ATOM   147   C  CD  . LYS A  1 19  ? 64.427  77.714  10.723  1.00 37.36 ?  43   LYS A CD  1 
ATOM   148   C  CE  . LYS A  1 19  ? 64.213  79.152  10.257  1.00 38.71 ?  43   LYS A CE  1 
ATOM   149   N  NZ  . LYS A  1 19  ? 64.801  80.136  11.219  1.00 39.91 ?  43   LYS A NZ  1 
ATOM   150   N  N   . ALA A  1 20  ? 63.036  72.285  10.957  1.00 33.35 ?  44   ALA A N   1 
ATOM   151   C  CA  . ALA A  1 20  ? 63.476  70.994  11.496  1.00 33.12 ?  44   ALA A CA  1 
ATOM   152   C  C   . ALA A  1 20  ? 63.431  69.872  10.461  1.00 32.84 ?  44   ALA A C   1 
ATOM   153   O  O   . ALA A  1 20  ? 62.445  69.713  9.741   1.00 32.87 ?  44   ALA A O   1 
ATOM   154   C  CB  . ALA A  1 20  ? 62.662  70.618  12.735  1.00 33.10 ?  44   ALA A CB  1 
ATOM   155   N  N   . THR A  1 21  ? 64.518  69.111  10.392  1.00 32.53 ?  45   THR A N   1 
ATOM   156   C  CA  . THR A  1 21  ? 64.607  67.945  9.517   1.00 32.41 ?  45   THR A CA  1 
ATOM   157   C  C   . THR A  1 21  ? 63.888  66.754  10.166  1.00 32.14 ?  45   THR A C   1 
ATOM   158   O  O   . THR A  1 21  ? 63.588  66.796  11.366  1.00 31.99 ?  45   THR A O   1 
ATOM   159   C  CB  . THR A  1 21  ? 66.082  67.556  9.235   1.00 32.37 ?  45   THR A CB  1 
ATOM   160   O  OG1 . THR A  1 21  ? 66.721  67.163  10.458  1.00 32.68 ?  45   THR A OG1 1 
ATOM   161   C  CG2 . THR A  1 21  ? 66.845  68.722  8.606   1.00 32.52 ?  45   THR A CG2 1 
ATOM   162   N  N   . PRO A  1 22  ? 63.598  65.697  9.381   1.00 31.79 ?  46   PRO A N   1 
ATOM   163   C  CA  . PRO A  1 22  ? 63.075  64.471  9.980   1.00 31.68 ?  46   PRO A CA  1 
ATOM   164   C  C   . PRO A  1 22  ? 63.934  63.962  11.142  1.00 31.58 ?  46   PRO A C   1 
ATOM   165   O  O   . PRO A  1 22  ? 63.392  63.564  12.176  1.00 31.37 ?  46   PRO A O   1 
ATOM   166   C  CB  . PRO A  1 22  ? 63.099  63.482  8.815   1.00 31.50 ?  46   PRO A CB  1 
ATOM   167   C  CG  . PRO A  1 22  ? 62.871  64.330  7.616   1.00 31.68 ?  46   PRO A CG  1 
ATOM   168   C  CD  . PRO A  1 22  ? 63.547  65.648  7.905   1.00 31.94 ?  46   PRO A CD  1 
ATOM   169   N  N   . LYS A  1 23  ? 65.255  63.999  10.973  1.00 31.55 ?  47   LYS A N   1 
ATOM   170   C  CA  . LYS A  1 23  ? 66.196  63.558  12.003  1.00 31.61 ?  47   LYS A CA  1 
ATOM   171   C  C   . LYS A  1 23  ? 66.035  64.350  13.302  1.00 31.57 ?  47   LYS A C   1 
ATOM   172   O  O   . LYS A  1 23  ? 65.957  63.763  14.383  1.00 31.64 ?  47   LYS A O   1 
ATOM   173   C  CB  . LYS A  1 23  ? 67.638  63.642  11.485  1.00 31.80 ?  47   LYS A CB  1 
ATOM   174   C  CG  . LYS A  1 23  ? 68.694  63.068  12.428  1.00 32.14 ?  47   LYS A CG  1 
ATOM   175   C  CD  . LYS A  1 23  ? 70.089  63.178  11.817  1.00 33.26 ?  47   LYS A CD  1 
ATOM   176   C  CE  . LYS A  1 23  ? 71.168  63.325  12.885  1.00 33.54 ?  47   LYS A CE  1 
ATOM   177   N  NZ  . LYS A  1 23  ? 71.313  62.107  13.716  1.00 34.14 ?  47   LYS A NZ  1 
ATOM   178   N  N   . GLU A  1 24  ? 65.968  65.674  13.185  1.00 31.50 ?  48   GLU A N   1 
ATOM   179   C  CA  . GLU A  1 24  ? 65.827  66.557  14.347  1.00 31.53 ?  48   GLU A CA  1 
ATOM   180   C  C   . GLU A  1 24  ? 64.486  66.362  15.056  1.00 31.18 ?  48   GLU A C   1 
ATOM   181   O  O   . GLU A  1 24  ? 64.431  66.322  16.288  1.00 31.00 ?  48   GLU A O   1 
ATOM   182   C  CB  . GLU A  1 24  ? 66.005  68.027  13.942  1.00 31.58 ?  48   GLU A CB  1 
ATOM   183   C  CG  . GLU A  1 24  ? 67.435  68.399  13.549  1.00 32.58 ?  48   GLU A CG  1 
ATOM   184   C  CD  . GLU A  1 24  ? 67.570  69.839  13.083  1.00 33.23 ?  48   GLU A CD  1 
ATOM   185   O  OE1 . GLU A  1 24  ? 66.775  70.270  12.222  1.00 33.95 ?  48   GLU A OE1 1 
ATOM   186   O  OE2 . GLU A  1 24  ? 68.479  70.540  13.573  1.00 34.33 -1 48   GLU A OE2 1 
ATOM   187   N  N   . THR A  1 25  ? 63.418  66.247  14.268  1.00 30.93 ?  49   THR A N   1 
ATOM   188   C  CA  . THR A  1 25  ? 62.074  66.028  14.795  1.00 30.98 ?  49   THR A CA  1 
ATOM   189   C  C   . THR A  1 25  ? 62.024  64.699  15.552  1.00 30.87 ?  49   THR A C   1 
ATOM   190   O  O   . THR A  1 25  ? 61.554  64.644  16.692  1.00 30.64 ?  49   THR A O   1 
ATOM   191   C  CB  . THR A  1 25  ? 61.006  66.049  13.677  1.00 31.01 ?  49   THR A CB  1 
ATOM   192   O  OG1 . THR A  1 25  ? 61.165  67.230  12.877  1.00 31.53 ?  49   THR A OG1 1 
ATOM   193   C  CG2 . THR A  1 25  ? 59.600  66.030  14.274  1.00 30.91 ?  49   THR A CG2 1 
ATOM   194   N  N   . TYR A  1 26  ? 62.534  63.648  14.911  1.00 30.82 ?  50   TYR A N   1 
ATOM   195   C  CA  . TYR A  1 26  ? 62.623  62.320  15.514  1.00 30.92 ?  50   TYR A CA  1 
ATOM   196   C  C   . TYR A  1 26  ? 63.370  62.352  16.846  1.00 30.70 ?  50   TYR A C   1 
ATOM   197   O  O   . TYR A  1 26  ? 62.855  61.875  17.857  1.00 30.81 ?  50   TYR A O   1 
ATOM   198   C  CB  . TYR A  1 26  ? 63.283  61.328  14.543  1.00 30.86 ?  50   TYR A CB  1 
ATOM   199   C  CG  . TYR A  1 26  ? 63.482  59.938  15.114  1.00 31.42 ?  50   TYR A CG  1 
ATOM   200   C  CD1 . TYR A  1 26  ? 62.427  59.025  15.160  1.00 31.16 ?  50   TYR A CD1 1 
ATOM   201   C  CD2 . TYR A  1 26  ? 64.725  59.536  15.607  1.00 31.80 ?  50   TYR A CD2 1 
ATOM   202   C  CE1 . TYR A  1 26  ? 62.600  57.752  15.689  1.00 32.08 ?  50   TYR A CE1 1 
ATOM   203   C  CE2 . TYR A  1 26  ? 64.911  58.259  16.138  1.00 32.77 ?  50   TYR A CE2 1 
ATOM   204   C  CZ  . TYR A  1 26  ? 63.843  57.372  16.172  1.00 32.72 ?  50   TYR A CZ  1 
ATOM   205   O  OH  . TYR A  1 26  ? 64.014  56.111  16.691  1.00 33.83 ?  50   TYR A OH  1 
ATOM   206   N  N   . GLU A  1 27  ? 64.569  62.933  16.842  1.00 30.64 ?  51   GLU A N   1 
ATOM   207   C  CA  . GLU A  1 27  ? 65.432  62.965  18.031  1.00 30.67 ?  51   GLU A CA  1 
ATOM   208   C  C   . GLU A  1 27  ? 64.830  63.725  19.208  1.00 30.25 ?  51   GLU A C   1 
ATOM   209   O  O   . GLU A  1 27  ? 65.026  63.333  20.354  1.00 30.15 ?  51   GLU A O   1 
ATOM   210   C  CB  . GLU A  1 27  ? 66.812  63.535  17.694  1.00 30.74 ?  51   GLU A CB  1 
ATOM   211   C  CG  . GLU A  1 27  ? 67.731  62.550  16.987  1.00 32.33 ?  51   GLU A CG  1 
ATOM   212   C  CD  . GLU A  1 27  ? 69.030  63.184  16.505  1.00 34.21 ?  51   GLU A CD  1 
ATOM   213   O  OE1 . GLU A  1 27  ? 69.210  64.409  16.674  1.00 35.19 ?  51   GLU A OE1 1 
ATOM   214   O  OE2 . GLU A  1 27  ? 69.870  62.450  15.945  1.00 35.55 -1 51   GLU A OE2 1 
ATOM   215   N  N   . ALA A  1 28  ? 64.120  64.814  18.920  1.00 30.09 ?  52   ALA A N   1 
ATOM   216   C  CA  . ALA A  1 28  ? 63.441  65.593  19.955  1.00 29.91 ?  52   ALA A CA  1 
ATOM   217   C  C   . ALA A  1 28  ? 62.273  64.804  20.568  1.00 29.92 ?  52   ALA A C   1 
ATOM   218   O  O   . ALA A  1 28  ? 62.092  64.796  21.791  1.00 29.64 ?  52   ALA A O   1 
ATOM   219   C  CB  . ALA A  1 28  ? 62.964  66.930  19.395  1.00 29.76 ?  52   ALA A CB  1 
ATOM   220   N  N   . LEU A  1 29  ? 61.499  64.143  19.706  1.00 29.90 ?  53   LEU A N   1 
ATOM   221   C  CA  . LEU A  1 29  ? 60.407  63.258  20.117  1.00 30.11 ?  53   LEU A CA  1 
ATOM   222   C  C   . LEU A  1 29  ? 60.893  62.129  21.025  1.00 30.24 ?  53   LEU A C   1 
ATOM   223   O  O   . LEU A  1 29  ? 60.350  61.919  22.114  1.00 30.19 ?  53   LEU A O   1 
ATOM   224   C  CB  . LEU A  1 29  ? 59.725  62.665  18.877  1.00 30.19 ?  53   LEU A CB  1 
ATOM   225   C  CG  . LEU A  1 29  ? 58.344  63.097  18.360  1.00 30.09 ?  53   LEU A CG  1 
ATOM   226   C  CD1 . LEU A  1 29  ? 57.685  64.241  19.125  1.00 29.58 ?  53   LEU A CD1 1 
ATOM   227   C  CD2 . LEU A  1 29  ? 58.419  63.386  16.871  1.00 30.01 ?  53   LEU A CD2 1 
ATOM   228   N  N   . VAL A  1 30  ? 61.926  61.421  20.568  1.00 30.55 ?  54   VAL A N   1 
ATOM   229   C  CA  . VAL A  1 30  ? 62.498  60.276  21.285  1.00 30.76 ?  54   VAL A CA  1 
ATOM   230   C  C   . VAL A  1 30  ? 63.132  60.685  22.620  1.00 30.98 ?  54   VAL A C   1 
ATOM   231   O  O   . VAL A  1 30  ? 63.044  59.942  23.604  1.00 30.88 ?  54   VAL A O   1 
ATOM   232   C  CB  . VAL A  1 30  ? 63.501  59.490  20.385  1.00 30.83 ?  54   VAL A CB  1 
ATOM   233   C  CG1 . VAL A  1 30  ? 64.260  58.420  21.178  1.00 30.73 ?  54   VAL A CG1 1 
ATOM   234   C  CG2 . VAL A  1 30  ? 62.761  58.843  19.226  1.00 30.63 ?  54   VAL A CG2 1 
ATOM   235   N  N   . LYS A  1 31  ? 63.749  61.868  22.651  1.00 31.17 ?  55   LYS A N   1 
ATOM   236   C  CA  . LYS A  1 31  ? 64.326  62.413  23.888  1.00 31.59 ?  55   LYS A CA  1 
ATOM   237   C  C   . LYS A  1 31  ? 63.258  62.594  24.972  1.00 31.35 ?  55   LYS A C   1 
ATOM   238   O  O   . LYS A  1 31  ? 63.494  62.292  26.145  1.00 31.31 ?  55   LYS A O   1 
ATOM   239   C  CB  . LYS A  1 31  ? 65.067  63.733  23.620  1.00 31.86 ?  55   LYS A CB  1 
ATOM   240   C  CG  . LYS A  1 31  ? 65.680  64.364  24.866  1.00 33.21 ?  55   LYS A CG  1 
ATOM   241   C  CD  . LYS A  1 31  ? 67.053  64.961  24.584  1.00 35.52 ?  55   LYS A CD  1 
ATOM   242   C  CE  . LYS A  1 31  ? 67.904  64.999  25.851  1.00 36.64 ?  55   LYS A CE  1 
ATOM   243   N  NZ  . LYS A  1 31  ? 68.051  63.648  26.485  1.00 37.82 ?  55   LYS A NZ  1 
ATOM   244   N  N   . ARG A  1 32  ? 62.088  63.080  24.570  1.00 31.17 ?  56   ARG A N   1 
ATOM   245   C  CA  . ARG A  1 32  ? 60.955  63.197  25.483  1.00 31.05 ?  56   ARG A CA  1 
ATOM   246   C  C   . ARG A  1 32  ? 60.387  61.815  25.805  1.00 30.89 ?  56   ARG A C   1 
ATOM   247   O  O   . ARG A  1 32  ? 60.160  61.487  26.970  1.00 30.63 ?  56   ARG A O   1 
ATOM   248   C  CB  . ARG A  1 32  ? 59.874  64.105  24.892  1.00 30.95 ?  56   ARG A CB  1 
ATOM   249   C  CG  . ARG A  1 32  ? 58.622  64.200  25.747  1.00 30.99 ?  56   ARG A CG  1 
ATOM   250   C  CD  . ARG A  1 32  ? 57.731  65.342  25.323  1.00 31.01 ?  56   ARG A CD  1 
ATOM   251   N  NE  . ARG A  1 32  ? 57.067  65.083  24.049  1.00 30.86 ?  56   ARG A NE  1 
ATOM   252   C  CZ  . ARG A  1 32  ? 56.092  65.837  23.552  1.00 30.95 ?  56   ARG A CZ  1 
ATOM   253   N  NH1 . ARG A  1 32  ? 55.663  66.897  24.223  1.00 31.00 ?  56   ARG A NH1 1 
ATOM   254   N  NH2 . ARG A  1 32  ? 55.544  65.530  22.386  1.00 30.84 ?  56   ARG A NH2 1 
ATOM   255   N  N   . TYR A  1 33  ? 60.188  61.014  24.757  1.00 30.98 ?  57   TYR A N   1 
ATOM   256   C  CA  . TYR A  1 33  ? 59.624  59.665  24.851  1.00 31.06 ?  57   TYR A CA  1 
ATOM   257   C  C   . TYR A  1 33  ? 60.364  58.754  25.836  1.00 31.43 ?  57   TYR A C   1 
ATOM   258   O  O   . TYR A  1 33  ? 59.738  57.965  26.545  1.00 31.25 ?  57   TYR A O   1 
ATOM   259   C  CB  . TYR A  1 33  ? 59.582  59.031  23.453  1.00 30.94 ?  57   TYR A CB  1 
ATOM   260   C  CG  . TYR A  1 33  ? 59.044  57.615  23.389  1.00 30.30 ?  57   TYR A CG  1 
ATOM   261   C  CD1 . TYR A  1 33  ? 57.692  57.352  23.588  1.00 29.79 ?  57   TYR A CD1 1 
ATOM   262   C  CD2 . TYR A  1 33  ? 59.886  56.544  23.096  1.00 29.94 ?  57   TYR A CD2 1 
ATOM   263   C  CE1 . TYR A  1 33  ? 57.196  56.054  23.520  1.00 29.36 ?  57   TYR A CE1 1 
ATOM   264   C  CE2 . TYR A  1 33  ? 59.400  55.242  23.023  1.00 29.48 ?  57   TYR A CE2 1 
ATOM   265   C  CZ  . TYR A  1 33  ? 58.053  55.006  23.235  1.00 29.16 ?  57   TYR A CZ  1 
ATOM   266   O  OH  . TYR A  1 33  ? 57.568  53.722  23.165  1.00 28.46 ?  57   TYR A OH  1 
ATOM   267   N  N   . LYS A  1 34  ? 61.689  58.879  25.885  1.00 31.91 ?  58   LYS A N   1 
ATOM   268   C  CA  . LYS A  1 34  ? 62.524  58.015  26.727  1.00 32.32 ?  58   LYS A CA  1 
ATOM   269   C  C   . LYS A  1 34  ? 62.914  58.624  28.074  1.00 32.32 ?  58   LYS A C   1 
ATOM   270   O  O   . LYS A  1 34  ? 63.623  57.993  28.858  1.00 32.45 ?  58   LYS A O   1 
ATOM   271   C  CB  . LYS A  1 34  ? 63.776  57.571  25.964  1.00 32.45 ?  58   LYS A CB  1 
ATOM   272   C  CG  . LYS A  1 34  ? 63.554  56.371  25.065  1.00 33.14 ?  58   LYS A CG  1 
ATOM   273   C  CD  . LYS A  1 34  ? 64.841  55.978  24.370  1.00 34.66 ?  58   LYS A CD  1 
ATOM   274   C  CE  . LYS A  1 34  ? 64.765  54.566  23.829  1.00 35.51 ?  58   LYS A CE  1 
ATOM   275   N  NZ  . LYS A  1 34  ? 65.904  54.267  22.909  1.00 36.56 ?  58   LYS A NZ  1 
ATOM   276   N  N   . ASP A  1 35  ? 62.439  59.838  28.342  1.00 32.61 ?  59   ASP A N   1 
ATOM   277   C  CA  . ASP A  1 35  ? 62.767  60.551  29.575  1.00 32.85 ?  59   ASP A CA  1 
ATOM   278   C  C   . ASP A  1 35  ? 61.835  60.155  30.722  1.00 32.98 ?  59   ASP A C   1 
ATOM   279   O  O   . ASP A  1 35  ? 60.615  60.289  30.599  1.00 32.97 ?  59   ASP A O   1 
ATOM   280   C  CB  . ASP A  1 35  ? 62.714  62.067  29.340  1.00 33.11 ?  59   ASP A CB  1 
ATOM   281   C  CG  . ASP A  1 35  ? 63.131  62.876  30.563  1.00 33.56 ?  59   ASP A CG  1 
ATOM   282   O  OD1 . ASP A  1 35  ? 63.887  62.365  31.413  1.00 34.06 ?  59   ASP A OD1 1 
ATOM   283   O  OD2 . ASP A  1 35  ? 62.704  64.043  30.667  1.00 35.15 -1 59   ASP A OD2 1 
ATOM   284   N  N   . PRO A  1 36  ? 62.410  59.668  31.844  1.00 33.16 ?  60   PRO A N   1 
ATOM   285   C  CA  . PRO A  1 36  ? 61.641  59.290  33.037  1.00 33.23 ?  60   PRO A CA  1 
ATOM   286   C  C   . PRO A  1 36  ? 60.740  60.403  33.579  1.00 33.27 ?  60   PRO A C   1 
ATOM   287   O  O   . PRO A  1 36  ? 59.686  60.112  34.153  1.00 33.29 ?  60   PRO A O   1 
ATOM   288   C  CB  . PRO A  1 36  ? 62.732  58.951  34.060  1.00 33.21 ?  60   PRO A CB  1 
ATOM   289   C  CG  . PRO A  1 36  ? 63.871  58.482  33.235  1.00 33.25 ?  60   PRO A CG  1 
ATOM   290   C  CD  . PRO A  1 36  ? 63.838  59.318  31.987  1.00 33.07 ?  60   PRO A CD  1 
ATOM   291   N  N   . ALA A  1 37  ? 61.157  61.657  33.402  1.00 33.15 ?  61   ALA A N   1 
ATOM   292   C  CA  . ALA A  1 37  ? 60.365  62.807  33.835  1.00 33.07 ?  61   ALA A CA  1 
ATOM   293   C  C   . ALA A  1 37  ? 59.124  63.001  32.962  1.00 32.95 ?  61   ALA A C   1 
ATOM   294   O  O   . ALA A  1 37  ? 58.171  63.663  33.373  1.00 33.34 ?  61   ALA A O   1 
ATOM   295   C  CB  . ALA A  1 37  ? 61.216  64.073  33.849  1.00 33.12 ?  61   ALA A CB  1 
ATOM   296   N  N   . HIS A  1 38  ? 59.143  62.414  31.767  1.00 32.59 ?  62   HIS A N   1 
ATOM   297   C  CA  . HIS A  1 38  ? 58.014  62.487  30.838  1.00 32.19 ?  62   HIS A CA  1 
ATOM   298   C  C   . HIS A  1 38  ? 57.177  61.202  30.780  1.00 31.72 ?  62   HIS A C   1 
ATOM   299   O  O   . HIS A  1 38  ? 56.235  61.108  29.992  1.00 31.38 ?  62   HIS A O   1 
ATOM   300   C  CB  . HIS A  1 38  ? 58.493  62.890  29.439  1.00 32.34 ?  62   HIS A CB  1 
ATOM   301   C  CG  . HIS A  1 38  ? 58.757  64.357  29.293  1.00 32.76 ?  62   HIS A CG  1 
ATOM   302   N  ND1 . HIS A  1 38  ? 59.999  64.916  29.508  1.00 33.67 ?  62   HIS A ND1 1 
ATOM   303   C  CD2 . HIS A  1 38  ? 57.935  65.382  28.968  1.00 33.27 ?  62   HIS A CD2 1 
ATOM   304   C  CE1 . HIS A  1 38  ? 59.933  66.221  29.312  1.00 33.83 ?  62   HIS A CE1 1 
ATOM   305   N  NE2 . HIS A  1 38  ? 58.691  66.530  28.984  1.00 33.89 ?  62   HIS A NE2 1 
ATOM   306   N  N   . GLY A  1 39  ? 57.522  60.219  31.615  1.00 31.28 ?  63   GLY A N   1 
ATOM   307   C  CA  . GLY A  1 39  ? 56.707  59.011  31.752  1.00 30.82 ?  63   GLY A CA  1 
ATOM   308   C  C   . GLY A  1 39  ? 57.381  57.660  31.568  1.00 30.56 ?  63   GLY A C   1 
ATOM   309   O  O   . GLY A  1 39  ? 56.834  56.639  31.992  1.00 30.81 ?  63   GLY A O   1 
ATOM   310   N  N   . ALA A  1 40  ? 58.557  57.644  30.941  1.00 30.07 ?  64   ALA A N   1 
ATOM   311   C  CA  . ALA A  1 40  ? 59.293  56.398  30.680  1.00 29.71 ?  64   ALA A CA  1 
ATOM   312   C  C   . ALA A  1 40  ? 59.831  55.729  31.955  1.00 29.30 ?  64   ALA A C   1 
ATOM   313   O  O   . ALA A  1 40  ? 59.933  56.363  33.008  1.00 29.53 ?  64   ALA A O   1 
ATOM   314   C  CB  . ALA A  1 40  ? 60.426  56.648  29.686  1.00 29.64 ?  64   ALA A CB  1 
ATOM   315   N  N   . GLY A  1 41  ? 60.164  54.445  31.853  1.00 28.75 ?  65   GLY A N   1 
ATOM   316   C  CA  . GLY A  1 41  ? 60.734  53.698  32.976  1.00 28.26 ?  65   GLY A CA  1 
ATOM   317   C  C   . GLY A  1 41  ? 59.698  53.134  33.933  1.00 27.91 ?  65   GLY A C   1 
ATOM   318   O  O   . GLY A  1 41  ? 58.551  52.903  33.553  1.00 27.80 ?  65   GLY A O   1 
ATOM   319   N  N   . LYS A  1 42  ? 60.105  52.919  35.181  1.00 27.73 ?  66   LYS A N   1 
ATOM   320   C  CA  . LYS A  1 42  ? 59.250  52.259  36.175  1.00 27.72 ?  66   LYS A CA  1 
ATOM   321   C  C   . LYS A  1 42  ? 58.279  53.199  36.896  1.00 27.66 ?  66   LYS A C   1 
ATOM   322   O  O   . LYS A  1 42  ? 57.342  52.745  37.554  1.00 27.78 ?  66   LYS A O   1 
ATOM   323   C  CB  . LYS A  1 42  ? 60.097  51.479  37.190  1.00 27.64 ?  66   LYS A CB  1 
ATOM   324   C  CG  . LYS A  1 42  ? 60.780  50.239  36.609  1.00 27.36 ?  66   LYS A CG  1 
ATOM   325   C  CD  . LYS A  1 42  ? 61.500  49.427  37.680  1.00 26.74 ?  66   LYS A CD  1 
ATOM   326   C  CE  . LYS A  1 42  ? 60.523  48.649  38.549  1.00 26.21 ?  66   LYS A CE  1 
ATOM   327   N  NZ  . LYS A  1 42  ? 61.213  47.932  39.653  1.00 26.39 ?  66   LYS A NZ  1 
ATOM   328   N  N   . GLY A  1 43  ? 58.503  54.503  36.766  1.00 27.64 ?  67   GLY A N   1 
ATOM   329   C  CA  . GLY A  1 43  ? 57.627  55.503  37.369  1.00 27.65 ?  67   GLY A CA  1 
ATOM   330   C  C   . GLY A  1 43  ? 57.901  55.768  38.837  1.00 27.79 ?  67   GLY A C   1 
ATOM   331   O  O   . GLY A  1 43  ? 58.810  55.181  39.429  1.00 27.94 ?  67   GLY A O   1 
ATOM   332   N  N   . THR A  1 44  ? 57.088  56.641  39.429  1.00 27.79 ?  68   THR A N   1 
ATOM   333   C  CA  . THR A  1 44  ? 57.310  57.146  40.787  1.00 27.79 ?  68   THR A CA  1 
ATOM   334   C  C   . THR A  1 44  ? 57.248  56.077  41.873  1.00 27.73 ?  68   THR A C   1 
ATOM   335   O  O   . THR A  1 44  ? 57.829  56.244  42.947  1.00 27.39 ?  68   THR A O   1 
ATOM   336   C  CB  . THR A  1 44  ? 56.308  58.272  41.147  1.00 27.91 ?  68   THR A CB  1 
ATOM   337   O  OG1 . THR A  1 44  ? 54.982  57.730  41.229  1.00 28.10 ?  68   THR A OG1 1 
ATOM   338   C  CG2 . THR A  1 44  ? 56.346  59.393  40.104  1.00 28.08 ?  68   THR A CG2 1 
ATOM   339   N  N   . MET A  1 45  ? 56.544  54.983  41.590  1.00 27.72 ?  69   MET A N   1 
ATOM   340   C  CA  . MET A  1 45  ? 56.353  53.914  42.570  1.00 27.69 ?  69   MET A CA  1 
ATOM   341   C  C   . MET A  1 45  ? 57.145  52.657  42.206  1.00 27.61 ?  69   MET A C   1 
ATOM   342   O  O   . MET A  1 45  ? 56.792  51.547  42.608  1.00 27.61 ?  69   MET A O   1 
ATOM   343   C  CB  . MET A  1 45  ? 54.859  53.615  42.749  1.00 27.63 ?  69   MET A CB  1 
ATOM   344   C  CG  . MET A  1 45  ? 54.067  54.773  43.361  1.00 28.00 ?  69   MET A CG  1 
ATOM   345   S  SD  . MET A  1 45  ? 52.277  54.510  43.450  1.00 27.95 ?  69   MET A SD  1 
ATOM   346   C  CE  . MET A  1 45  ? 51.863  54.520  41.711  1.00 26.93 ?  69   MET A CE  1 
ATOM   347   N  N   . GLY A  1 46  ? 58.239  52.848  41.467  1.00 27.72 ?  70   GLY A N   1 
ATOM   348   C  CA  . GLY A  1 46  ? 59.076  51.750  40.982  1.00 27.56 ?  70   GLY A CA  1 
ATOM   349   C  C   . GLY A  1 46  ? 59.723  50.866  42.037  1.00 27.90 ?  70   GLY A C   1 
ATOM   350   O  O   . GLY A  1 46  ? 60.058  49.712  41.751  1.00 27.76 ?  70   GLY A O   1 
ATOM   351   N  N   . ASP A  1 47  ? 59.908  51.399  43.249  1.00 27.92 ?  71   ASP A N   1 
ATOM   352   C  CA  . ASP A  1 47  ? 60.489  50.629  44.363  1.00 28.29 ?  71   ASP A CA  1 
ATOM   353   C  C   . ASP A  1 47  ? 59.489  49.640  44.961  1.00 28.08 ?  71   ASP A C   1 
ATOM   354   O  O   . ASP A  1 47  ? 59.854  48.782  45.771  1.00 28.00 ?  71   ASP A O   1 
ATOM   355   C  CB  . ASP A  1 47  ? 60.997  51.562  45.475  1.00 28.69 ?  71   ASP A CB  1 
ATOM   356   C  CG  . ASP A  1 47  ? 62.088  52.512  45.004  1.00 29.80 ?  71   ASP A CG  1 
ATOM   357   O  OD1 . ASP A  1 47  ? 62.896  52.135  44.125  1.00 31.31 ?  71   ASP A OD1 1 
ATOM   358   O  OD2 . ASP A  1 47  ? 62.136  53.646  45.525  1.00 32.07 -1 71   ASP A OD2 1 
ATOM   359   N  N   . TYR A  1 48  ? 58.228  49.764  44.557  1.00 27.73 ?  72   TYR A N   1 
ATOM   360   C  CA  . TYR A  1 48  ? 57.154  48.959  45.129  1.00 27.39 ?  72   TYR A CA  1 
ATOM   361   C  C   . TYR A  1 48  ? 56.829  47.695  44.334  1.00 27.06 ?  72   TYR A C   1 
ATOM   362   O  O   . TYR A  1 48  ? 56.255  46.751  44.881  1.00 26.95 ?  72   TYR A O   1 
ATOM   363   C  CB  . TYR A  1 48  ? 55.908  49.824  45.342  1.00 27.54 ?  72   TYR A CB  1 
ATOM   364   C  CG  . TYR A  1 48  ? 56.103  50.870  46.422  1.00 27.76 ?  72   TYR A CG  1 
ATOM   365   C  CD1 . TYR A  1 48  ? 56.547  52.155  46.106  1.00 27.58 ?  72   TYR A CD1 1 
ATOM   366   C  CD2 . TYR A  1 48  ? 55.865  50.562  47.765  1.00 28.64 ?  72   TYR A CD2 1 
ATOM   367   C  CE1 . TYR A  1 48  ? 56.739  53.116  47.103  1.00 28.58 ?  72   TYR A CE1 1 
ATOM   368   C  CE2 . TYR A  1 48  ? 56.055  51.512  48.769  1.00 28.88 ?  72   TYR A CE2 1 
ATOM   369   C  CZ  . TYR A  1 48  ? 56.490  52.785  48.430  1.00 29.02 ?  72   TYR A CZ  1 
ATOM   370   O  OH  . TYR A  1 48  ? 56.674  53.725  49.416  1.00 29.86 ?  72   TYR A OH  1 
ATOM   371   N  N   . TRP A  1 49  ? 57.216  47.670  43.058  1.00 26.56 ?  73   TRP A N   1 
ATOM   372   C  CA  . TRP A  1 49  ? 56.918  46.537  42.180  1.00 25.91 ?  73   TRP A CA  1 
ATOM   373   C  C   . TRP A  1 49  ? 58.112  46.083  41.331  1.00 25.79 ?  73   TRP A C   1 
ATOM   374   O  O   . TRP A  1 49  ? 59.005  46.874  41.020  1.00 25.50 ?  73   TRP A O   1 
ATOM   375   C  CB  . TRP A  1 49  ? 55.721  46.860  41.277  1.00 25.77 ?  73   TRP A CB  1 
ATOM   376   C  CG  . TRP A  1 49  ? 55.972  47.983  40.317  1.00 24.95 ?  73   TRP A CG  1 
ATOM   377   C  CD1 . TRP A  1 49  ? 55.783  49.311  40.551  1.00 24.34 ?  73   TRP A CD1 1 
ATOM   378   C  CD2 . TRP A  1 49  ? 56.456  47.877  38.971  1.00 24.52 ?  73   TRP A CD2 1 
ATOM   379   N  NE1 . TRP A  1 49  ? 56.120  50.042  39.441  1.00 24.10 ?  73   TRP A NE1 1 
ATOM   380   C  CE2 . TRP A  1 49  ? 56.539  49.188  38.455  1.00 24.37 ?  73   TRP A CE2 1 
ATOM   381   C  CE3 . TRP A  1 49  ? 56.830  46.803  38.153  1.00 23.93 ?  73   TRP A CE3 1 
ATOM   382   C  CZ2 . TRP A  1 49  ? 56.974  49.456  37.152  1.00 24.16 ?  73   TRP A CZ2 1 
ATOM   383   C  CZ3 . TRP A  1 49  ? 57.267  47.071  36.857  1.00 24.12 ?  73   TRP A CZ3 1 
ATOM   384   C  CH2 . TRP A  1 49  ? 57.335  48.387  36.372  1.00 24.04 ?  73   TRP A CH2 1 
ATOM   385   N  N   . GLU A  1 50  ? 58.102  44.801  40.965  1.00 25.53 ?  74   GLU A N   1 
ATOM   386   C  CA  . GLU A  1 50  ? 59.121  44.200  40.107  1.00 25.48 ?  74   GLU A CA  1 
ATOM   387   C  C   . GLU A  1 50  ? 58.463  43.560  38.887  1.00 25.11 ?  74   GLU A C   1 
ATOM   388   O  O   . GLU A  1 50  ? 57.328  43.084  38.980  1.00 25.00 ?  74   GLU A O   1 
ATOM   389   C  CB  . GLU A  1 50  ? 59.920  43.134  40.867  1.00 25.79 ?  74   GLU A CB  1 
ATOM   390   C  CG  . GLU A  1 50  ? 60.855  43.678  41.949  1.00 26.75 ?  74   GLU A CG  1 
ATOM   391   C  CD  . GLU A  1 50  ? 60.105  44.203  43.154  1.00 28.47 ?  74   GLU A CD  1 
ATOM   392   O  OE1 . GLU A  1 50  ? 60.393  45.339  43.591  1.00 29.35 ?  74   GLU A OE1 1 
ATOM   393   O  OE2 . GLU A  1 50  ? 59.209  43.487  43.651  1.00 29.03 -1 74   GLU A OE2 1 
ATOM   394   N  N   . PRO A  1 51  ? 59.175  43.540  37.741  1.00 24.62 ?  75   PRO A N   1 
ATOM   395   C  CA  . PRO A  1 51  ? 58.637  42.958  36.513  1.00 24.28 ?  75   PRO A CA  1 
ATOM   396   C  C   . PRO A  1 51  ? 58.407  41.457  36.648  1.00 23.86 ?  75   PRO A C   1 
ATOM   397   O  O   . PRO A  1 51  ? 59.084  40.795  37.438  1.00 23.68 ?  75   PRO A O   1 
ATOM   398   C  CB  . PRO A  1 51  ? 59.756  43.207  35.495  1.00 24.42 ?  75   PRO A CB  1 
ATOM   399   C  CG  . PRO A  1 51  ? 61.004  43.286  36.328  1.00 24.59 ?  75   PRO A CG  1 
ATOM   400   C  CD  . PRO A  1 51  ? 60.554  44.028  37.546  1.00 24.51 ?  75   PRO A CD  1 
ATOM   401   N  N   . ILE A  1 52  ? 57.448  40.936  35.890  1.00 23.28 ?  76   ILE A N   1 
ATOM   402   C  CA  . ILE A  1 52  ? 57.279  39.494  35.759  1.00 22.76 ?  76   ILE A CA  1 
ATOM   403   C  C   . ILE A  1 52  ? 57.786  39.084  34.378  1.00 22.60 ?  76   ILE A C   1 
ATOM   404   O  O   . ILE A  1 52  ? 58.230  39.939  33.612  1.00 22.74 ?  76   ILE A O   1 
ATOM   405   C  CB  . ILE A  1 52  ? 55.820  39.032  36.036  1.00 22.72 ?  76   ILE A CB  1 
ATOM   406   C  CG1 . ILE A  1 52  ? 54.816  39.771  35.142  1.00 22.32 ?  76   ILE A CG1 1 
ATOM   407   C  CG2 . ILE A  1 52  ? 55.483  39.205  37.528  1.00 22.28 ?  76   ILE A CG2 1 
ATOM   408   C  CD1 . ILE A  1 52  ? 53.430  39.146  35.119  1.00 20.80 ?  76   ILE A CD1 1 
ATOM   409   N  N   . ALA A  1 53  ? 57.743  37.793  34.060  1.00 22.29 ?  77   ALA A N   1 
ATOM   410   C  CA  . ALA A  1 53  ? 58.354  37.303  32.821  1.00 22.23 ?  77   ALA A CA  1 
ATOM   411   C  C   . ALA A  1 53  ? 57.849  38.019  31.558  1.00 22.17 ?  77   ALA A C   1 
ATOM   412   O  O   . ALA A  1 53  ? 58.644  38.379  30.692  1.00 21.87 ?  77   ALA A O   1 
ATOM   413   C  CB  . ALA A  1 53  ? 58.202  35.787  32.696  1.00 22.20 ?  77   ALA A CB  1 
ATOM   414   N  N   . ILE A  1 54  ? 56.538  38.248  31.470  1.00 22.30 ?  78   ILE A N   1 
ATOM   415   C  CA  . ILE A  1 54  ? 55.951  38.885  30.283  1.00 22.24 ?  78   ILE A CA  1 
ATOM   416   C  C   . ILE A  1 54  ? 56.264  40.383  30.157  1.00 22.29 ?  78   ILE A C   1 
ATOM   417   O  O   . ILE A  1 54  ? 56.184  40.946  29.057  1.00 22.44 ?  78   ILE A O   1 
ATOM   418   C  CB  . ILE A  1 54  ? 54.424  38.621  30.167  1.00 22.31 ?  78   ILE A CB  1 
ATOM   419   C  CG1 . ILE A  1 54  ? 53.978  38.737  28.706  1.00 22.21 ?  78   ILE A CG1 1 
ATOM   420   C  CG2 . ILE A  1 54  ? 53.623  39.563  31.064  1.00 22.05 ?  78   ILE A CG2 1 
ATOM   421   C  CD1 . ILE A  1 54  ? 53.017  37.680  28.285  1.00 22.98 ?  78   ILE A CD1 1 
ATOM   422   N  N   . SER A  1 55  ? 56.652  41.007  31.270  1.00 22.07 ?  79   SER A N   1 
ATOM   423   C  CA  . SER A  1 55  ? 56.956  42.444  31.314  1.00 22.17 ?  79   SER A CA  1 
ATOM   424   C  C   . SER A  1 55  ? 58.070  42.866  30.352  1.00 22.19 ?  79   SER A C   1 
ATOM   425   O  O   . SER A  1 55  ? 58.132  44.028  29.945  1.00 22.24 ?  79   SER A O   1 
ATOM   426   C  CB  . SER A  1 55  ? 57.311  42.877  32.739  1.00 22.09 ?  79   SER A CB  1 
ATOM   427   O  OG  . SER A  1 55  ? 56.305  42.491  33.661  1.00 22.21 ?  79   SER A OG  1 
ATOM   428   N  N   . ILE A  1 56  ? 58.946  41.927  29.993  1.00 22.17 ?  80   ILE A N   1 
ATOM   429   C  CA  . ILE A  1 56  ? 59.995  42.202  29.001  1.00 22.40 ?  80   ILE A CA  1 
ATOM   430   C  C   . ILE A  1 56  ? 59.400  42.539  27.623  1.00 22.38 ?  80   ILE A C   1 
ATOM   431   O  O   . ILE A  1 56  ? 60.031  43.233  26.828  1.00 22.56 ?  80   ILE A O   1 
ATOM   432   C  CB  . ILE A  1 56  ? 61.048  41.058  28.889  1.00 22.31 ?  80   ILE A CB  1 
ATOM   433   C  CG1 . ILE A  1 56  ? 60.444  39.799  28.257  1.00 22.57 ?  80   ILE A CG1 1 
ATOM   434   C  CG2 . ILE A  1 56  ? 61.685  40.762  30.259  1.00 22.35 ?  80   ILE A CG2 1 
ATOM   435   C  CD1 . ILE A  1 56  ? 61.478  38.774  27.781  1.00 22.83 ?  80   ILE A CD1 1 
ATOM   436   N  N   . TYR A  1 57  ? 58.187  42.045  27.359  1.00 22.19 ?  81   TYR A N   1 
ATOM   437   C  CA  . TYR A  1 57  ? 57.461  42.358  26.124  1.00 21.82 ?  81   TYR A CA  1 
ATOM   438   C  C   . TYR A  1 57  ? 56.532  43.566  26.292  1.00 22.17 ?  81   TYR A C   1 
ATOM   439   O  O   . TYR A  1 57  ? 56.208  44.239  25.315  1.00 22.11 ?  81   TYR A O   1 
ATOM   440   C  CB  . TYR A  1 57  ? 56.665  41.140  25.634  1.00 21.54 ?  81   TYR A CB  1 
ATOM   441   C  CG  . TYR A  1 57  ? 57.507  39.895  25.461  1.00 20.23 ?  81   TYR A CG  1 
ATOM   442   C  CD1 . TYR A  1 57  ? 58.322  39.730  24.341  1.00 19.55 ?  81   TYR A CD1 1 
ATOM   443   C  CD2 . TYR A  1 57  ? 57.497  38.888  26.424  1.00 19.62 ?  81   TYR A CD2 1 
ATOM   444   C  CE1 . TYR A  1 57  ? 59.107  38.594  24.187  1.00 19.81 ?  81   TYR A CE1 1 
ATOM   445   C  CE2 . TYR A  1 57  ? 58.279  37.747  26.278  1.00 19.71 ?  81   TYR A CE2 1 
ATOM   446   C  CZ  . TYR A  1 57  ? 59.081  37.608  25.157  1.00 19.18 ?  81   TYR A CZ  1 
ATOM   447   O  OH  . TYR A  1 57  ? 59.855  36.482  25.009  1.00 19.42 ?  81   TYR A OH  1 
ATOM   448   N  N   . MET A  1 58  ? 56.109  43.830  27.528  1.00 22.49 ?  82   MET A N   1 
ATOM   449   C  CA  . MET A  1 58  ? 55.178  44.930  27.822  1.00 22.98 ?  82   MET A CA  1 
ATOM   450   C  C   . MET A  1 58  ? 55.879  46.285  27.888  1.00 23.26 ?  82   MET A C   1 
ATOM   451   O  O   . MET A  1 58  ? 55.347  47.286  27.401  1.00 23.03 ?  82   MET A O   1 
ATOM   452   C  CB  . MET A  1 58  ? 54.408  44.670  29.126  1.00 22.93 ?  82   MET A CB  1 
ATOM   453   C  CG  . MET A  1 58  ? 53.614  43.361  29.167  1.00 23.10 ?  82   MET A CG  1 
ATOM   454   S  SD  . MET A  1 58  ? 52.134  43.334  28.125  1.00 24.17 ?  82   MET A SD  1 
ATOM   455   C  CE  . MET A  1 58  ? 52.719  42.528  26.635  1.00 23.20 ?  82   MET A CE  1 
ATOM   456   N  N   . ASP A  1 59  ? 57.063  46.308  28.504  1.00 23.65 ?  83   ASP A N   1 
ATOM   457   C  CA  . ASP A  1 59  ? 57.915  47.496  28.528  1.00 24.29 ?  83   ASP A CA  1 
ATOM   458   C  C   . ASP A  1 59  ? 59.363  47.112  28.188  1.00 24.59 ?  83   ASP A C   1 
ATOM   459   O  O   . ASP A  1 59  ? 60.204  46.998  29.083  1.00 24.54 ?  83   ASP A O   1 
ATOM   460   C  CB  . ASP A  1 59  ? 57.829  48.189  29.896  1.00 24.34 ?  83   ASP A CB  1 
ATOM   461   C  CG  . ASP A  1 59  ? 58.610  49.499  29.954  1.00 24.98 ?  83   ASP A CG  1 
ATOM   462   O  OD1 . ASP A  1 59  ? 59.059  50.009  28.900  1.00 25.05 ?  83   ASP A OD1 1 
ATOM   463   O  OD2 . ASP A  1 59  ? 58.768  50.027  31.074  1.00 25.95 -1 83   ASP A OD2 1 
ATOM   464   N  N   . PRO A  1 60  ? 59.655  46.907  26.888  1.00 25.11 ?  84   PRO A N   1 
ATOM   465   C  CA  . PRO A  1 60  ? 60.982  46.448  26.454  1.00 25.50 ?  84   PRO A CA  1 
ATOM   466   C  C   . PRO A  1 60  ? 62.150  47.391  26.780  1.00 25.95 ?  84   PRO A C   1 
ATOM   467   O  O   . PRO A  1 60  ? 63.208  46.921  27.204  1.00 26.16 ?  84   PRO A O   1 
ATOM   468   C  CB  . PRO A  1 60  ? 60.819  46.291  24.936  1.00 25.52 ?  84   PRO A CB  1 
ATOM   469   C  CG  . PRO A  1 60  ? 59.353  46.093  24.737  1.00 25.20 ?  84   PRO A CG  1 
ATOM   470   C  CD  . PRO A  1 60  ? 58.710  46.972  25.756  1.00 24.94 ?  84   PRO A CD  1 
ATOM   471   N  N   . ASN A  1 61  ? 61.963  48.697  26.598  1.00 26.52 ?  85   ASN A N   1 
ATOM   472   C  CA  . ASN A  1 61  ? 63.041  49.673  26.835  1.00 27.12 ?  85   ASN A CA  1 
ATOM   473   C  C   . ASN A  1 61  ? 63.581  49.661  28.271  1.00 27.20 ?  85   ASN A C   1 
ATOM   474   O  O   . ASN A  1 61  ? 64.753  49.969  28.504  1.00 27.30 ?  85   ASN A O   1 
ATOM   475   C  CB  . ASN A  1 61  ? 62.613  51.092  26.424  1.00 26.98 ?  85   ASN A CB  1 
ATOM   476   C  CG  . ASN A  1 61  ? 62.565  51.283  24.907  1.00 28.32 ?  85   ASN A CG  1 
ATOM   477   O  OD1 . ASN A  1 61  ? 63.264  50.596  24.152  1.00 29.00 ?  85   ASN A OD1 1 
ATOM   478   N  ND2 . ASN A  1 61  ? 61.740  52.230  24.455  1.00 28.16 ?  85   ASN A ND2 1 
ATOM   479   N  N   . THR A  1 62  ? 62.724  49.290  29.219  1.00 27.35 ?  86   THR A N   1 
ATOM   480   C  CA  . THR A  1 62  ? 63.113  49.167  30.618  1.00 27.40 ?  86   THR A CA  1 
ATOM   481   C  C   . THR A  1 62  ? 63.613  47.759  30.962  1.00 27.47 ?  86   THR A C   1 
ATOM   482   O  O   . THR A  1 62  ? 64.578  47.606  31.719  1.00 27.47 ?  86   THR A O   1 
ATOM   483   C  CB  . THR A  1 62  ? 61.939  49.538  31.553  1.00 27.50 ?  86   THR A CB  1 
ATOM   484   O  OG1 . THR A  1 62  ? 61.430  50.827  31.193  1.00 27.71 ?  86   THR A OG1 1 
ATOM   485   C  CG2 . THR A  1 62  ? 62.377  49.563  33.018  1.00 27.76 ?  86   THR A CG2 1 
ATOM   486   N  N   . PHE A  1 63  ? 62.974  46.738  30.394  1.00 27.42 ?  87   PHE A N   1 
ATOM   487   C  CA  . PHE A  1 63  ? 63.147  45.375  30.898  1.00 27.39 ?  87   PHE A CA  1 
ATOM   488   C  C   . PHE A  1 63  ? 63.764  44.346  29.951  1.00 27.69 ?  87   PHE A C   1 
ATOM   489   O  O   . PHE A  1 63  ? 64.265  43.320  30.416  1.00 27.57 ?  87   PHE A O   1 
ATOM   490   C  CB  . PHE A  1 63  ? 61.815  44.839  31.440  1.00 27.36 ?  87   PHE A CB  1 
ATOM   491   C  CG  . PHE A  1 63  ? 61.292  45.594  32.631  1.00 26.89 ?  87   PHE A CG  1 
ATOM   492   C  CD1 . PHE A  1 63  ? 62.078  45.761  33.771  1.00 27.14 ?  87   PHE A CD1 1 
ATOM   493   C  CD2 . PHE A  1 63  ? 60.008  46.123  32.621  1.00 26.69 ?  87   PHE A CD2 1 
ATOM   494   C  CE1 . PHE A  1 63  ? 61.596  46.459  34.878  1.00 26.75 ?  87   PHE A CE1 1 
ATOM   495   C  CE2 . PHE A  1 63  ? 59.512  46.820  33.727  1.00 26.76 ?  87   PHE A CE2 1 
ATOM   496   C  CZ  . PHE A  1 63  ? 60.310  46.988  34.854  1.00 26.73 ?  87   PHE A CZ  1 
ATOM   497   N  N   . TYR A  1 64  ? 63.724  44.599  28.642  1.00 27.89 ?  88   TYR A N   1 
ATOM   498   C  CA  . TYR A  1 64  ? 64.133  43.576  27.676  1.00 28.32 ?  88   TYR A CA  1 
ATOM   499   C  C   . TYR A  1 64  ? 65.638  43.336  27.550  1.00 28.73 ?  88   TYR A C   1 
ATOM   500   O  O   . TYR A  1 64  ? 66.419  44.264  27.337  1.00 28.67 ?  88   TYR A O   1 
ATOM   501   C  CB  . TYR A  1 64  ? 63.534  43.811  26.282  1.00 28.18 ?  88   TYR A CB  1 
ATOM   502   C  CG  . TYR A  1 64  ? 63.769  42.631  25.368  1.00 28.02 ?  88   TYR A CG  1 
ATOM   503   C  CD1 . TYR A  1 64  ? 62.957  41.501  25.443  1.00 27.02 ?  88   TYR A CD1 1 
ATOM   504   C  CD2 . TYR A  1 64  ? 64.833  42.623  24.457  1.00 27.73 ?  88   TYR A CD2 1 
ATOM   505   C  CE1 . TYR A  1 64  ? 63.179  40.407  24.624  1.00 26.59 ?  88   TYR A CE1 1 
ATOM   506   C  CE2 . TYR A  1 64  ? 65.063  41.525  23.633  1.00 26.36 ?  88   TYR A CE2 1 
ATOM   507   C  CZ  . TYR A  1 64  ? 64.231  40.424  23.723  1.00 26.44 ?  88   TYR A CZ  1 
ATOM   508   O  OH  . TYR A  1 64  ? 64.444  39.331  22.915  1.00 26.22 ?  88   TYR A OH  1 
ATOM   509   N  N   . LYS A  1 65  ? 66.013  42.067  27.679  1.00 29.40 ?  89   LYS A N   1 
ATOM   510   C  CA  . LYS A  1 65  ? 67.334  41.570  27.305  1.00 29.86 ?  89   LYS A CA  1 
ATOM   511   C  C   . LYS A  1 65  ? 67.121  40.415  26.327  1.00 29.88 ?  89   LYS A C   1 
ATOM   512   O  O   . LYS A  1 65  ? 66.164  39.656  26.483  1.00 29.96 ?  89   LYS A O   1 
ATOM   513   C  CB  . LYS A  1 65  ? 68.093  41.068  28.538  1.00 30.15 ?  89   LYS A CB  1 
ATOM   514   C  CG  . LYS A  1 65  ? 68.482  42.149  29.548  1.00 31.12 ?  89   LYS A CG  1 
ATOM   515   C  CD  . LYS A  1 65  ? 69.671  42.958  29.061  1.00 33.45 ?  89   LYS A CD  1 
ATOM   516   C  CE  . LYS A  1 65  ? 70.353  43.695  30.202  1.00 34.43 ?  89   LYS A CE  1 
ATOM   517   N  NZ  . LYS A  1 65  ? 71.678  44.231  29.768  1.00 35.74 ?  89   LYS A NZ  1 
ATOM   518   N  N   . PRO A  1 66  ? 68.003  40.275  25.314  1.00 30.02 ?  90   PRO A N   1 
ATOM   519   C  CA  . PRO A  1 66  ? 67.897  39.157  24.370  1.00 30.09 ?  90   PRO A CA  1 
ATOM   520   C  C   . PRO A  1 66  ? 68.052  37.801  25.072  1.00 30.26 ?  90   PRO A C   1 
ATOM   521   O  O   . PRO A  1 66  ? 68.655  37.739  26.147  1.00 30.10 ?  90   PRO A O   1 
ATOM   522   C  CB  . PRO A  1 66  ? 69.075  39.387  23.414  1.00 30.18 ?  90   PRO A CB  1 
ATOM   523   C  CG  . PRO A  1 66  ? 69.444  40.811  23.577  1.00 30.03 ?  90   PRO A CG  1 
ATOM   524   C  CD  . PRO A  1 66  ? 69.138  41.159  24.989  1.00 30.03 ?  90   PRO A CD  1 
ATOM   525   N  N   . PRO A  1 67  ? 67.505  36.721  24.475  1.00 30.46 ?  91   PRO A N   1 
ATOM   526   C  CA  . PRO A  1 67  ? 67.640  35.401  25.095  1.00 30.76 ?  91   PRO A CA  1 
ATOM   527   C  C   . PRO A  1 67  ? 69.086  34.910  25.067  1.00 31.09 ?  91   PRO A C   1 
ATOM   528   O  O   . PRO A  1 67  ? 69.864  35.328  24.205  1.00 30.94 ?  91   PRO A O   1 
ATOM   529   C  CB  . PRO A  1 67  ? 66.749  34.504  24.227  1.00 30.67 ?  91   PRO A CB  1 
ATOM   530   C  CG  . PRO A  1 67  ? 66.604  35.217  22.940  1.00 30.59 ?  91   PRO A CG  1 
ATOM   531   C  CD  . PRO A  1 67  ? 66.698  36.675  23.240  1.00 30.45 ?  91   PRO A CD  1 
ATOM   532   N  N   . VAL A  1 68  ? 69.439  34.045  26.014  1.00 31.49 ?  92   VAL A N   1 
ATOM   533   C  CA  . VAL A  1 68  ? 70.796  33.495  26.084  1.00 32.11 ?  92   VAL A CA  1 
ATOM   534   C  C   . VAL A  1 68  ? 71.003  32.387  25.050  1.00 32.35 ?  92   VAL A C   1 
ATOM   535   O  O   . VAL A  1 68  ? 72.135  32.067  24.692  1.00 32.45 ?  92   VAL A O   1 
ATOM   536   C  CB  . VAL A  1 68  ? 71.177  33.008  27.517  1.00 32.18 ?  92   VAL A CB  1 
ATOM   537   C  CG1 . VAL A  1 68  ? 71.246  34.190  28.482  1.00 32.56 ?  92   VAL A CG1 1 
ATOM   538   C  CG2 . VAL A  1 68  ? 70.204  31.945  28.029  1.00 32.38 ?  92   VAL A CG2 1 
ATOM   539   N  N   . SER A  1 69  ? 69.897  31.823  24.569  1.00 32.59 ?  93   SER A N   1 
ATOM   540   C  CA  . SER A  1 69  ? 69.920  30.778  23.554  1.00 32.83 ?  93   SER A CA  1 
ATOM   541   C  C   . SER A  1 69  ? 68.923  31.134  22.451  1.00 32.97 ?  93   SER A C   1 
ATOM   542   O  O   . SER A  1 69  ? 67.810  31.565  22.755  1.00 32.97 ?  93   SER A O   1 
ATOM   543   C  CB  . SER A  1 69  ? 69.576  29.424  24.181  1.00 32.66 ?  93   SER A CB  1 
ATOM   544   O  OG  . SER A  1 69  ? 69.621  28.386  23.218  1.00 33.15 ?  93   SER A OG  1 
ATOM   545   N  N   . PRO A  1 70  ? 69.309  30.959  21.169  1.00 33.15 ?  94   PRO A N   1 
ATOM   546   C  CA  . PRO A  1 70  ? 70.560  30.389  20.647  1.00 33.37 ?  94   PRO A CA  1 
ATOM   547   C  C   . PRO A  1 70  ? 71.780  31.305  20.778  1.00 33.70 ?  94   PRO A C   1 
ATOM   548   O  O   . PRO A  1 70  ? 71.650  32.531  20.688  1.00 33.63 ?  94   PRO A O   1 
ATOM   549   C  CB  . PRO A  1 70  ? 70.245  30.168  19.165  1.00 33.35 ?  94   PRO A CB  1 
ATOM   550   C  CG  . PRO A  1 70  ? 69.252  31.238  18.837  1.00 33.08 ?  94   PRO A CG  1 
ATOM   551   C  CD  . PRO A  1 70  ? 68.406  31.379  20.077  1.00 33.15 ?  94   PRO A CD  1 
ATOM   552   N  N   . LYS A  1 71  ? 72.949  30.694  20.988  1.00 34.08 ?  95   LYS A N   1 
ATOM   553   C  CA  . LYS A  1 71  ? 74.229  31.406  21.025  1.00 34.42 ?  95   LYS A CA  1 
ATOM   554   C  C   . LYS A  1 71  ? 74.800  31.467  19.609  1.00 34.38 ?  95   LYS A C   1 
ATOM   555   O  O   . LYS A  1 71  ? 75.767  30.773  19.288  1.00 34.35 ?  95   LYS A O   1 
ATOM   556   C  CB  . LYS A  1 71  ? 75.235  30.716  21.965  1.00 34.65 ?  95   LYS A CB  1 
ATOM   557   C  CG  . LYS A  1 71  ? 74.786  30.529  23.417  1.00 35.66 ?  95   LYS A CG  1 
ATOM   558   C  CD  . LYS A  1 71  ? 74.180  29.141  23.646  1.00 37.56 ?  95   LYS A CD  1 
ATOM   559   C  CE  . LYS A  1 71  ? 73.673  28.959  25.073  1.00 38.01 ?  95   LYS A CE  1 
ATOM   560   N  NZ  . LYS A  1 71  ? 74.788  28.884  26.064  1.00 39.37 ?  95   LYS A NZ  1 
ATOM   561   N  N   . GLU A  1 72  ? 74.182  32.288  18.763  1.00 34.40 ?  96   GLU A N   1 
ATOM   562   C  CA  . GLU A  1 72  ? 74.570  32.389  17.358  1.00 34.36 ?  96   GLU A CA  1 
ATOM   563   C  C   . GLU A  1 72  ? 74.615  33.821  16.848  1.00 33.90 ?  96   GLU A C   1 
ATOM   564   O  O   . GLU A  1 72  ? 73.962  34.711  17.393  1.00 34.04 ?  96   GLU A O   1 
ATOM   565   C  CB  . GLU A  1 72  ? 73.620  31.573  16.472  1.00 34.55 ?  96   GLU A CB  1 
ATOM   566   C  CG  . GLU A  1 72  ? 74.054  30.129  16.223  1.00 36.03 ?  96   GLU A CG  1 
ATOM   567   C  CD  . GLU A  1 72  ? 75.239  29.997  15.264  1.00 37.01 ?  96   GLU A CD  1 
ATOM   568   O  OE1 . GLU A  1 72  ? 75.757  31.027  14.775  1.00 37.95 ?  96   GLU A OE1 1 
ATOM   569   O  OE2 . GLU A  1 72  ? 75.657  28.847  15.005  1.00 37.74 -1 96   GLU A OE2 1 
ATOM   570   N  N   . VAL A  1 73  ? 75.402  34.028  15.798  1.00 33.43 ?  97   VAL A N   1 
ATOM   571   C  CA  . VAL A  1 73  ? 75.392  35.276  15.047  1.00 32.76 ?  97   VAL A CA  1 
ATOM   572   C  C   . VAL A  1 73  ? 74.717  35.015  13.706  1.00 32.38 ?  97   VAL A C   1 
ATOM   573   O  O   . VAL A  1 73  ? 74.878  33.942  13.120  1.00 32.39 ?  97   VAL A O   1 
ATOM   574   C  CB  . VAL A  1 73  ? 76.810  35.884  14.862  1.00 32.89 ?  97   VAL A CB  1 
ATOM   575   C  CG1 . VAL A  1 73  ? 77.372  36.354  16.206  1.00 32.59 ?  97   VAL A CG1 1 
ATOM   576   C  CG2 . VAL A  1 73  ? 77.756  34.893  14.198  1.00 32.28 ?  97   VAL A CG2 1 
ATOM   577   N  N   . ALA A  1 74  ? 73.947  35.988  13.235  1.00 31.71 ?  98   ALA A N   1 
ATOM   578   C  CA  . ALA A  1 74  ? 73.082  35.771  12.086  1.00 31.11 ?  98   ALA A CA  1 
ATOM   579   C  C   . ALA A  1 74  ? 73.006  36.992  11.196  1.00 30.81 ?  98   ALA A C   1 
ATOM   580   O  O   . ALA A  1 74  ? 72.981  38.126  11.676  1.00 30.63 ?  98   ALA A O   1 
ATOM   581   C  CB  . ALA A  1 74  ? 71.677  35.366  12.551  1.00 31.07 ?  98   ALA A CB  1 
ATOM   582   N  N   . GLU A  1 75  ? 72.969  36.744  9.892   1.00 30.57 ?  99   GLU A N   1 
ATOM   583   C  CA  . GLU A  1 75  ? 72.719  37.797  8.918   1.00 30.43 ?  99   GLU A CA  1 
ATOM   584   C  C   . GLU A  1 75  ? 71.242  37.836  8.531   1.00 29.99 ?  99   GLU A C   1 
ATOM   585   O  O   . GLU A  1 75  ? 70.465  36.972  8.943   1.00 29.78 ?  99   GLU A O   1 
ATOM   586   C  CB  . GLU A  1 75  ? 73.611  37.617  7.690   1.00 30.65 ?  99   GLU A CB  1 
ATOM   587   C  CG  . GLU A  1 75  ? 75.007  38.183  7.899   1.00 31.71 ?  99   GLU A CG  1 
ATOM   588   C  CD  . GLU A  1 75  ? 76.056  37.567  6.991   1.00 33.39 ?  99   GLU A CD  1 
ATOM   589   O  OE1 . GLU A  1 75  ? 75.696  36.881  6.010   1.00 33.43 ?  99   GLU A OE1 1 
ATOM   590   O  OE2 . GLU A  1 75  ? 77.255  37.775  7.270   1.00 34.46 -1 99   GLU A OE2 1 
ATOM   591   N  N   . ARG A  1 76  ? 70.879  38.849  7.748   1.00 29.40 ?  100  ARG A N   1 
ATOM   592   C  CA  . ARG A  1 76  ? 69.510  39.091  7.296   1.00 29.15 ?  100  ARG A CA  1 
ATOM   593   C  C   . ARG A  1 76  ? 68.740  37.824  6.905   1.00 29.05 ?  100  ARG A C   1 
ATOM   594   O  O   . ARG A  1 76  ? 67.656  37.573  7.434   1.00 29.02 ?  100  ARG A O   1 
ATOM   595   C  CB  . ARG A  1 76  ? 69.517  40.101  6.138   1.00 28.92 ?  100  ARG A CB  1 
ATOM   596   C  CG  . ARG A  1 76  ? 68.150  40.554  5.664   1.00 28.32 ?  100  ARG A CG  1 
ATOM   597   C  CD  . ARG A  1 76  ? 68.262  41.678  4.629   1.00 27.80 ?  100  ARG A CD  1 
ATOM   598   N  NE  . ARG A  1 76  ? 68.693  42.940  5.235   1.00 26.96 ?  100  ARG A NE  1 
ATOM   599   C  CZ  . ARG A  1 76  ? 67.869  43.845  5.761   1.00 26.49 ?  100  ARG A CZ  1 
ATOM   600   N  NH1 . ARG A  1 76  ? 66.556  43.639  5.759   1.00 25.45 ?  100  ARG A NH1 1 
ATOM   601   N  NH2 . ARG A  1 76  ? 68.357  44.959  6.295   1.00 25.18 ?  100  ARG A NH2 1 
ATOM   602   N  N   . LYS A  1 77  ? 69.302  37.032  5.990   1.00 28.92 ?  101  LYS A N   1 
ATOM   603   C  CA  . LYS A  1 77  ? 68.627  35.835  5.483   1.00 28.87 ?  101  LYS A CA  1 
ATOM   604   C  C   . LYS A  1 77  ? 68.534  34.713  6.522   1.00 28.66 ?  101  LYS A C   1 
ATOM   605   O  O   . LYS A  1 77  ? 67.645  33.860  6.438   1.00 28.76 ?  101  LYS A O   1 
ATOM   606   C  CB  . LYS A  1 77  ? 69.267  35.342  4.172   1.00 28.99 ?  101  LYS A CB  1 
ATOM   607   C  CG  . LYS A  1 77  ? 70.664  34.711  4.287   1.00 30.02 ?  101  LYS A CG  1 
ATOM   608   C  CD  . LYS A  1 77  ? 70.600  33.198  4.184   1.00 31.05 ?  101  LYS A CD  1 
ATOM   609   C  CE  . LYS A  1 77  ? 71.911  32.595  3.696   1.00 31.11 ?  101  LYS A CE  1 
ATOM   610   N  NZ  . LYS A  1 77  ? 72.883  32.348  4.797   1.00 31.09 ?  101  LYS A NZ  1 
ATOM   611   N  N   . ASP A  1 78  ? 69.442  34.720  7.498   1.00 28.07 ?  102  ASP A N   1 
ATOM   612   C  CA  . ASP A  1 78  ? 69.450  33.690  8.538   1.00 27.64 ?  102  ASP A CA  1 
ATOM   613   C  C   . ASP A  1 78  ? 68.272  33.855  9.504   1.00 27.31 ?  102  ASP A C   1 
ATOM   614   O  O   . ASP A  1 78  ? 67.780  32.868  10.059  1.00 27.04 ?  102  ASP A O   1 
ATOM   615   C  CB  . ASP A  1 78  ? 70.782  33.674  9.297   1.00 27.71 ?  102  ASP A CB  1 
ATOM   616   C  CG  . ASP A  1 78  ? 71.989  33.581  8.371   1.00 27.35 ?  102  ASP A CG  1 
ATOM   617   O  OD1 . ASP A  1 78  ? 71.987  32.746  7.442   1.00 26.69 ?  102  ASP A OD1 1 
ATOM   618   O  OD2 . ASP A  1 78  ? 72.949  34.349  8.586   1.00 27.44 -1 102  ASP A OD2 1 
ATOM   619   N  N   . CYS A  1 79  ? 67.829  35.101  9.691   1.00 26.88 ?  103  CYS A N   1 
ATOM   620   C  CA  . CYS A  1 79  ? 66.622  35.395  10.469  1.00 26.60 ?  103  CYS A CA  1 
ATOM   621   C  C   . CYS A  1 79  ? 65.438  34.653  9.878   1.00 26.28 ?  103  CYS A C   1 
ATOM   622   O  O   . CYS A  1 79  ? 64.751  33.912  10.573  1.00 26.27 ?  103  CYS A O   1 
ATOM   623   C  CB  . CYS A  1 79  ? 66.315  36.895  10.473  1.00 26.51 ?  103  CYS A CB  1 
ATOM   624   S  SG  . CYS A  1 79  ? 67.693  37.962  10.904  1.00 26.32 ?  103  CYS A SG  1 
ATOM   625   N  N   . VAL A  1 80  ? 65.227  34.856  8.581   1.00 26.11 ?  104  VAL A N   1 
ATOM   626   C  CA  . VAL A  1 80  ? 64.100  34.286  7.857   1.00 26.02 ?  104  VAL A CA  1 
ATOM   627   C  C   . VAL A  1 80  ? 64.182  32.760  7.822   1.00 26.01 ?  104  VAL A C   1 
ATOM   628   O  O   . VAL A  1 80  ? 63.212  32.078  8.147   1.00 25.91 ?  104  VAL A O   1 
ATOM   629   C  CB  . VAL A  1 80  ? 64.017  34.862  6.419   1.00 25.93 ?  104  VAL A CB  1 
ATOM   630   C  CG1 . VAL A  1 80  ? 62.813  34.310  5.676   1.00 25.83 ?  104  VAL A CG1 1 
ATOM   631   C  CG2 . VAL A  1 80  ? 63.956  36.382  6.460   1.00 26.04 ?  104  VAL A CG2 1 
ATOM   632   N  N   . GLU A  1 81  ? 65.350  32.238  7.451   1.00 25.96 ?  105  GLU A N   1 
ATOM   633   C  CA  . GLU A  1 81  ? 65.535  30.801  7.272   1.00 26.02 ?  105  GLU A CA  1 
ATOM   634   C  C   . GLU A  1 81  ? 65.300  29.979  8.542   1.00 25.94 ?  105  GLU A C   1 
ATOM   635   O  O   . GLU A  1 81  ? 64.539  29.014  8.519   1.00 25.95 ?  105  GLU A O   1 
ATOM   636   C  CB  . GLU A  1 81  ? 66.913  30.499  6.668   1.00 25.98 ?  105  GLU A CB  1 
ATOM   637   C  CG  . GLU A  1 81  ? 67.015  30.860  5.184   1.00 26.53 ?  105  GLU A CG  1 
ATOM   638   C  CD  . GLU A  1 81  ? 68.353  30.503  4.556   1.00 27.52 ?  105  GLU A CD  1 
ATOM   639   O  OE1 . GLU A  1 81  ? 69.285  30.094  5.281   1.00 27.94 ?  105  GLU A OE1 1 
ATOM   640   O  OE2 . GLU A  1 81  ? 68.476  30.645  3.323   1.00 28.60 -1 105  GLU A OE2 1 
ATOM   641   N  N   . CYS A  1 82  ? 65.941  30.359  9.644   1.00 25.71 ?  106  CYS A N   1 
ATOM   642   C  CA  . CYS A  1 82  ? 65.824  29.584  10.876  1.00 25.73 ?  106  CYS A CA  1 
ATOM   643   C  C   . CYS A  1 82  ? 64.446  29.752  11.509  1.00 25.66 ?  106  CYS A C   1 
ATOM   644   O  O   . CYS A  1 82  ? 63.851  28.778  11.976  1.00 25.74 ?  106  CYS A O   1 
ATOM   645   C  CB  . CYS A  1 82  ? 66.921  29.958  11.866  1.00 25.50 ?  106  CYS A CB  1 
ATOM   646   S  SG  . CYS A  1 82  ? 66.933  28.991  13.395  1.00 26.39 ?  106  CYS A SG  1 
ATOM   647   N  N   . HIS A  1 83  ? 63.937  30.981  11.509  1.00 25.42 ?  107  HIS A N   1 
ATOM   648   C  CA  . HIS A  1 83  ? 62.623  31.250  12.079  1.00 25.55 ?  107  HIS A CA  1 
ATOM   649   C  C   . HIS A  1 83  ? 61.480  30.690  11.222  1.00 25.65 ?  107  HIS A C   1 
ATOM   650   O  O   . HIS A  1 83  ? 60.360  30.534  11.708  1.00 25.53 ?  107  HIS A O   1 
ATOM   651   C  CB  . HIS A  1 83  ? 62.446  32.742  12.363  1.00 25.31 ?  107  HIS A CB  1 
ATOM   652   C  CG  . HIS A  1 83  ? 63.103  33.193  13.634  1.00 24.99 ?  107  HIS A CG  1 
ATOM   653   N  ND1 . HIS A  1 83  ? 62.447  33.196  14.845  1.00 24.30 ?  107  HIS A ND1 1 
ATOM   654   C  CD2 . HIS A  1 83  ? 64.355  33.649  13.883  1.00 24.23 ?  107  HIS A CD2 1 
ATOM   655   C  CE1 . HIS A  1 83  ? 63.265  33.636  15.785  1.00 24.59 ?  107  HIS A CE1 1 
ATOM   656   N  NE2 . HIS A  1 83  ? 64.430  33.918  15.229  1.00 24.63 ?  107  HIS A NE2 1 
ATOM   657   N  N   . SER A  1 84  ? 61.779  30.366  9.962   1.00 25.68 ?  108  SER A N   1 
ATOM   658   C  CA  . SER A  1 84  ? 60.821  29.707  9.071   1.00 26.10 ?  108  SER A CA  1 
ATOM   659   C  C   . SER A  1 84  ? 60.435  28.325  9.597   1.00 26.14 ?  108  SER A C   1 
ATOM   660   O  O   . SER A  1 84  ? 59.375  27.799  9.255   1.00 26.08 ?  108  SER A O   1 
ATOM   661   C  CB  . SER A  1 84  ? 61.371  29.612  7.641   1.00 26.13 ?  108  SER A CB  1 
ATOM   662   O  OG  . SER A  1 84  ? 60.402  29.095  6.745   1.00 27.16 ?  108  SER A OG  1 
ATOM   663   N  N   . ASP A  1 85  ? 61.293  27.754  10.441  1.00 26.41 ?  109  ASP A N   1 
ATOM   664   C  CA  . ASP A  1 85  ? 60.993  26.497  11.128  1.00 26.55 ?  109  ASP A CA  1 
ATOM   665   C  C   . ASP A  1 85  ? 60.705  26.700  12.620  1.00 26.49 ?  109  ASP A C   1 
ATOM   666   O  O   . ASP A  1 85  ? 59.881  25.988  13.197  1.00 26.48 ?  109  ASP A O   1 
ATOM   667   C  CB  . ASP A  1 85  ? 62.145  25.501  10.959  1.00 26.71 ?  109  ASP A CB  1 
ATOM   668   C  CG  . ASP A  1 85  ? 62.460  25.212  9.507   1.00 27.37 ?  109  ASP A CG  1 
ATOM   669   O  OD1 . ASP A  1 85  ? 61.515  25.066  8.700   1.00 27.63 ?  109  ASP A OD1 1 
ATOM   670   O  OD2 . ASP A  1 85  ? 63.661  25.125  9.174   1.00 28.49 -1 109  ASP A OD2 1 
ATOM   671   N  N   . GLU A  1 86  ? 61.390  27.663  13.237  1.00 26.22 ?  110  GLU A N   1 
ATOM   672   C  CA  . GLU A  1 86  ? 61.294  27.877  14.684  1.00 26.20 ?  110  GLU A CA  1 
ATOM   673   C  C   . GLU A  1 86  ? 60.026  28.625  15.100  1.00 25.61 ?  110  GLU A C   1 
ATOM   674   O  O   . GLU A  1 86  ? 59.397  28.278  16.103  1.00 25.49 ?  110  GLU A O   1 
ATOM   675   C  CB  . GLU A  1 86  ? 62.537  28.603  15.218  1.00 26.51 ?  110  GLU A CB  1 
ATOM   676   C  CG  . GLU A  1 86  ? 63.828  27.793  15.146  1.00 27.96 ?  110  GLU A CG  1 
ATOM   677   C  CD  . GLU A  1 86  ? 63.928  26.710  16.210  1.00 29.89 ?  110  GLU A CD  1 
ATOM   678   O  OE1 . GLU A  1 86  ? 63.053  26.641  17.099  1.00 30.56 ?  110  GLU A OE1 1 
ATOM   679   O  OE2 . GLU A  1 86  ? 64.900  25.927  16.161  1.00 31.42 -1 110  GLU A OE2 1 
ATOM   680   N  N   . THR A  1 87  ? 59.673  29.660  14.342  1.00 24.90 ?  111  THR A N   1 
ATOM   681   C  CA  . THR A  1 87  ? 58.410  30.377  14.528  1.00 24.33 ?  111  THR A CA  1 
ATOM   682   C  C   . THR A  1 87  ? 57.735  30.533  13.160  1.00 24.29 ?  111  THR A C   1 
ATOM   683   O  O   . THR A  1 87  ? 57.613  31.653  12.651  1.00 24.06 ?  111  THR A O   1 
ATOM   684   C  CB  . THR A  1 87  ? 58.613  31.768  15.200  1.00 24.43 ?  111  THR A CB  1 
ATOM   685   O  OG1 . THR A  1 87  ? 59.436  32.601  14.373  1.00 23.66 ?  111  THR A OG1 1 
ATOM   686   C  CG2 . THR A  1 87  ? 59.243  31.638  16.589  1.00 23.70 ?  111  THR A CG2 1 
ATOM   687   N  N   . PRO A  1 88  ? 57.298  29.404  12.559  1.00 24.17 ?  112  PRO A N   1 
ATOM   688   C  CA  . PRO A  1 88  ? 56.940  29.358  11.130  1.00 24.18 ?  112  PRO A CA  1 
ATOM   689   C  C   . PRO A  1 88  ? 55.897  30.381  10.673  1.00 24.13 ?  112  PRO A C   1 
ATOM   690   O  O   . PRO A  1 88  ? 56.061  30.984  9.610   1.00 24.29 ?  112  PRO A O   1 
ATOM   691   C  CB  . PRO A  1 88  ? 56.420  27.923  10.924  1.00 24.16 ?  112  PRO A CB  1 
ATOM   692   C  CG  . PRO A  1 88  ? 56.153  27.386  12.293  1.00 24.24 ?  112  PRO A CG  1 
ATOM   693   C  CD  . PRO A  1 88  ? 57.094  28.099  13.218  1.00 24.18 ?  112  PRO A CD  1 
ATOM   694   N  N   . VAL A  1 89  ? 54.848  30.578  11.467  1.00 24.10 ?  113  VAL A N   1 
ATOM   695   C  CA  . VAL A  1 89  ? 53.741  31.458  11.080  1.00 23.93 ?  113  VAL A CA  1 
ATOM   696   C  C   . VAL A  1 89  ? 54.158  32.939  11.046  1.00 23.84 ?  113  VAL A C   1 
ATOM   697   O  O   . VAL A  1 89  ? 53.649  33.704  10.222  1.00 23.74 ?  113  VAL A O   1 
ATOM   698   C  CB  . VAL A  1 89  ? 52.469  31.211  11.952  1.00 23.99 ?  113  VAL A CB  1 
ATOM   699   C  CG1 . VAL A  1 89  ? 51.324  32.130  11.548  1.00 23.80 ?  113  VAL A CG1 1 
ATOM   700   C  CG2 . VAL A  1 89  ? 52.023  29.747  11.844  1.00 24.18 ?  113  VAL A CG2 1 
ATOM   701   N  N   . TRP A  1 90  ? 55.095  33.326  11.914  1.00 23.63 ?  114  TRP A N   1 
ATOM   702   C  CA  . TRP A  1 90  ? 55.652  34.688  11.905  1.00 23.64 ?  114  TRP A CA  1 
ATOM   703   C  C   . TRP A  1 90  ? 56.329  35.044  10.576  1.00 23.69 ?  114  TRP A C   1 
ATOM   704   O  O   . TRP A  1 90  ? 56.177  36.159  10.075  1.00 23.59 ?  114  TRP A O   1 
ATOM   705   C  CB  . TRP A  1 90  ? 56.650  34.894  13.049  1.00 23.44 ?  114  TRP A CB  1 
ATOM   706   C  CG  . TRP A  1 90  ? 56.076  35.232  14.420  1.00 23.63 ?  114  TRP A CG  1 
ATOM   707   C  CD1 . TRP A  1 90  ? 56.789  35.356  15.586  1.00 23.07 ?  114  TRP A CD1 1 
ATOM   708   C  CD2 . TRP A  1 90  ? 54.700  35.480  14.771  1.00 22.90 ?  114  TRP A CD2 1 
ATOM   709   N  NE1 . TRP A  1 90  ? 55.952  35.667  16.629  1.00 22.57 ?  114  TRP A NE1 1 
ATOM   710   C  CE2 . TRP A  1 90  ? 54.668  35.751  16.162  1.00 23.09 ?  114  TRP A CE2 1 
ATOM   711   C  CE3 . TRP A  1 90  ? 53.499  35.508  14.049  1.00 22.71 ?  114  TRP A CE3 1 
ATOM   712   C  CZ2 . TRP A  1 90  ? 53.478  36.037  16.846  1.00 22.49 ?  114  TRP A CZ2 1 
ATOM   713   C  CZ3 . TRP A  1 90  ? 52.316  35.792  14.731  1.00 23.11 ?  114  TRP A CZ3 1 
ATOM   714   C  CH2 . TRP A  1 90  ? 52.318  36.052  16.118  1.00 22.59 ?  114  TRP A CH2 1 
ATOM   715   N  N   . VAL A  1 91  ? 57.080  34.095  10.020  1.00 23.85 ?  115  VAL A N   1 
ATOM   716   C  CA  . VAL A  1 91  ? 57.741  34.279  8.725   1.00 23.83 ?  115  VAL A CA  1 
ATOM   717   C  C   . VAL A  1 91  ? 56.694  34.309  7.615   1.00 24.17 ?  115  VAL A C   1 
ATOM   718   O  O   . VAL A  1 91  ? 56.781  35.105  6.679   1.00 23.98 ?  115  VAL A O   1 
ATOM   719   C  CB  . VAL A  1 91  ? 58.776  33.156  8.454   1.00 23.74 ?  115  VAL A CB  1 
ATOM   720   C  CG1 . VAL A  1 91  ? 59.421  33.321  7.074   1.00 23.53 ?  115  VAL A CG1 1 
ATOM   721   C  CG2 . VAL A  1 91  ? 59.838  33.156  9.538   1.00 23.16 ?  115  VAL A CG2 1 
ATOM   722   N  N   . ARG A  1 92  ? 55.696  33.442  7.752   1.00 24.58 ?  116  ARG A N   1 
ATOM   723   C  CA  . ARG A  1 92  ? 54.595  33.336  6.807   1.00 25.07 ?  116  ARG A CA  1 
ATOM   724   C  C   . ARG A  1 92  ? 53.752  34.611  6.763   1.00 25.12 ?  116  ARG A C   1 
ATOM   725   O  O   . ARG A  1 92  ? 53.417  35.100  5.681   1.00 24.95 ?  116  ARG A O   1 
ATOM   726   C  CB  . ARG A  1 92  ? 53.730  32.134  7.178   1.00 25.33 ?  116  ARG A CB  1 
ATOM   727   C  CG  . ARG A  1 92  ? 52.932  31.594  6.036   1.00 26.80 ?  116  ARG A CG  1 
ATOM   728   C  CD  . ARG A  1 92  ? 52.634  30.118  6.213   1.00 27.99 ?  116  ARG A CD  1 
ATOM   729   N  NE  . ARG A  1 92  ? 52.106  29.603  4.957   1.00 29.53 ?  116  ARG A NE  1 
ATOM   730   C  CZ  . ARG A  1 92  ? 52.750  28.770  4.148   1.00 29.40 ?  116  ARG A CZ  1 
ATOM   731   N  NH1 . ARG A  1 92  ? 53.948  28.297  4.470   1.00 28.82 ?  116  ARG A NH1 1 
ATOM   732   N  NH2 . ARG A  1 92  ? 52.169  28.387  3.022   1.00 29.38 ?  116  ARG A NH2 1 
ATOM   733   N  N   . ALA A  1 93  ? 53.416  35.140  7.940   1.00 25.31 ?  117  ALA A N   1 
ATOM   734   C  CA  . ALA A  1 93  ? 52.673  36.395  8.057   1.00 25.58 ?  117  ALA A CA  1 
ATOM   735   C  C   . ALA A  1 93  ? 53.498  37.579  7.539   1.00 25.83 ?  117  ALA A C   1 
ATOM   736   O  O   . ALA A  1 93  ? 52.976  38.455  6.846   1.00 25.81 ?  117  ALA A O   1 
ATOM   737   C  CB  . ALA A  1 93  ? 52.247  36.632  9.511   1.00 25.29 ?  117  ALA A CB  1 
ATOM   738   N  N   . TRP A  1 94  ? 54.784  37.598  7.886   1.00 26.16 ?  118  TRP A N   1 
ATOM   739   C  CA  . TRP A  1 94  ? 55.704  38.628  7.403   1.00 26.55 ?  118  TRP A CA  1 
ATOM   740   C  C   . TRP A  1 94  ? 55.812  38.638  5.872   1.00 26.68 ?  118  TRP A C   1 
ATOM   741   O  O   . TRP A  1 94  ? 55.804  39.699  5.262   1.00 26.55 ?  118  TRP A O   1 
ATOM   742   C  CB  . TRP A  1 94  ? 57.089  38.469  8.043   1.00 26.50 ?  118  TRP A CB  1 
ATOM   743   C  CG  . TRP A  1 94  ? 58.128  39.371  7.441   1.00 26.94 ?  118  TRP A CG  1 
ATOM   744   C  CD1 . TRP A  1 94  ? 58.314  40.698  7.703   1.00 27.16 ?  118  TRP A CD1 1 
ATOM   745   C  CD2 . TRP A  1 94  ? 59.111  39.012  6.463   1.00 26.79 ?  118  TRP A CD2 1 
ATOM   746   N  NE1 . TRP A  1 94  ? 59.356  41.187  6.953   1.00 27.84 ?  118  TRP A NE1 1 
ATOM   747   C  CE2 . TRP A  1 94  ? 59.864  40.174  6.183   1.00 27.61 ?  118  TRP A CE2 1 
ATOM   748   C  CE3 . TRP A  1 94  ? 59.429  37.822  5.795   1.00 26.89 ?  118  TRP A CE3 1 
ATOM   749   C  CZ2 . TRP A  1 94  ? 60.917  40.181  5.261   1.00 27.51 ?  118  TRP A CZ2 1 
ATOM   750   C  CZ3 . TRP A  1 94  ? 60.479  37.828  4.881   1.00 27.08 ?  118  TRP A CZ3 1 
ATOM   751   C  CH2 . TRP A  1 94  ? 61.209  39.002  4.623   1.00 27.33 ?  118  TRP A CH2 1 
ATOM   752   N  N   . LYS A  1 95  ? 55.897  37.456  5.266   1.00 27.21 ?  119  LYS A N   1 
ATOM   753   C  CA  . LYS A  1 95  ? 56.008  37.329  3.807   1.00 27.86 ?  119  LYS A CA  1 
ATOM   754   C  C   . LYS A  1 95  ? 54.823  37.924  3.037   1.00 28.19 ?  119  LYS A C   1 
ATOM   755   O  O   . LYS A  1 95  ? 55.001  38.471  1.943   1.00 28.35 ?  119  LYS A O   1 
ATOM   756   C  CB  . LYS A  1 95  ? 56.240  35.869  3.404   1.00 27.90 ?  119  LYS A CB  1 
ATOM   757   C  CG  . LYS A  1 95  ? 57.693  35.412  3.568   1.00 28.13 ?  119  LYS A CG  1 
ATOM   758   C  CD  . LYS A  1 95  ? 57.880  33.928  3.258   1.00 27.91 ?  119  LYS A CD  1 
ATOM   759   C  CE  . LYS A  1 95  ? 57.776  33.630  1.757   1.00 28.44 ?  119  LYS A CE  1 
ATOM   760   N  NZ  . LYS A  1 95  ? 58.864  34.281  0.972   1.00 27.86 ?  119  LYS A NZ  1 
ATOM   761   N  N   . ARG A  1 96  ? 53.622  37.823  3.605   1.00 28.59 ?  120  ARG A N   1 
ATOM   762   C  CA  . ARG A  1 96  ? 52.426  38.381  2.961   1.00 29.04 ?  120  ARG A CA  1 
ATOM   763   C  C   . ARG A  1 96  ? 52.139  39.837  3.352   1.00 28.71 ?  120  ARG A C   1 
ATOM   764   O  O   . ARG A  1 96  ? 51.154  40.423  2.896   1.00 29.06 ?  120  ARG A O   1 
ATOM   765   C  CB  . ARG A  1 96  ? 51.192  37.483  3.170   1.00 29.36 ?  120  ARG A CB  1 
ATOM   766   C  CG  . ARG A  1 96  ? 50.786  37.249  4.615   1.00 30.67 ?  120  ARG A CG  1 
ATOM   767   C  CD  . ARG A  1 96  ? 49.516  36.391  4.710   1.00 33.65 ?  120  ARG A CD  1 
ATOM   768   N  NE  . ARG A  1 96  ? 49.382  35.775  6.032   1.00 34.99 ?  120  ARG A NE  1 
ATOM   769   C  CZ  . ARG A  1 96  ? 49.605  34.491  6.294   1.00 36.54 ?  120  ARG A CZ  1 
ATOM   770   N  NH1 . ARG A  1 96  ? 49.955  33.652  5.326   1.00 37.24 ?  120  ARG A NH1 1 
ATOM   771   N  NH2 . ARG A  1 96  ? 49.469  34.037  7.532   1.00 38.00 ?  120  ARG A NH2 1 
ATOM   772   N  N   . SER A  1 97  ? 53.014  40.419  4.171   1.00 28.29 ?  121  SER A N   1 
ATOM   773   C  CA  . SER A  1 97  ? 52.883  41.811  4.594   1.00 27.84 ?  121  SER A CA  1 
ATOM   774   C  C   . SER A  1 97  ? 53.503  42.789  3.591   1.00 27.67 ?  121  SER A C   1 
ATOM   775   O  O   . SER A  1 97  ? 54.407  42.435  2.831   1.00 27.48 ?  121  SER A O   1 
ATOM   776   C  CB  . SER A  1 97  ? 53.513  42.015  5.977   1.00 28.01 ?  121  SER A CB  1 
ATOM   777   O  OG  . SER A  1 97  ? 54.931  41.997  5.912   1.00 27.50 ?  121  SER A OG  1 
ATOM   778   N  N   . THR A  1 98  ? 53.002  44.022  3.603   1.00 27.37 ?  122  THR A N   1 
ATOM   779   C  CA  . THR A  1 98  ? 53.566  45.118  2.816   1.00 27.22 ?  122  THR A CA  1 
ATOM   780   C  C   . THR A  1 98  ? 55.065  45.298  3.090   1.00 27.09 ?  122  THR A C   1 
ATOM   781   O  O   . THR A  1 98  ? 55.847  45.528  2.162   1.00 26.92 ?  122  THR A O   1 
ATOM   782   C  CB  . THR A  1 98  ? 52.816  46.432  3.102   1.00 27.18 ?  122  THR A CB  1 
ATOM   783   O  OG1 . THR A  1 98  ? 51.478  46.331  2.601   1.00 27.72 ?  122  THR A OG1 1 
ATOM   784   C  CG2 . THR A  1 98  ? 53.506  47.622  2.449   1.00 27.26 ?  122  THR A CG2 1 
ATOM   785   N  N   . HIS A  1 99  ? 55.453  45.175  4.362   1.00 26.88 ?  123  HIS A N   1 
ATOM   786   C  CA  . HIS A  1 99  ? 56.847  45.311  4.783   1.00 26.72 ?  123  HIS A CA  1 
ATOM   787   C  C   . HIS A  1 99  ? 57.822  44.433  3.976   1.00 26.96 ?  123  HIS A C   1 
ATOM   788   O  O   . HIS A  1 99  ? 58.977  44.813  3.774   1.00 26.98 ?  123  HIS A O   1 
ATOM   789   C  CB  . HIS A  1 99  ? 56.994  45.047  6.292   1.00 26.52 ?  123  HIS A CB  1 
ATOM   790   C  CG  . HIS A  1 99  ? 56.570  46.196  7.164   1.00 25.78 ?  123  HIS A CG  1 
ATOM   791   N  ND1 . HIS A  1 99  ? 55.903  46.016  8.358   1.00 24.70 ?  123  HIS A ND1 1 
ATOM   792   C  CD2 . HIS A  1 99  ? 56.720  47.535  7.019   1.00 24.87 ?  123  HIS A CD2 1 
ATOM   793   C  CE1 . HIS A  1 99  ? 55.664  47.194  8.910   1.00 24.43 ?  123  HIS A CE1 1 
ATOM   794   N  NE2 . HIS A  1 99  ? 56.147  48.135  8.117   1.00 24.26 ?  123  HIS A NE2 1 
ATOM   795   N  N   . ALA A  1 100 ? 57.346  43.281  3.502   1.00 27.03 ?  124  ALA A N   1 
ATOM   796   C  CA  . ALA A  1 100 ? 58.184  42.324  2.776   1.00 27.45 ?  124  ALA A CA  1 
ATOM   797   C  C   . ALA A  1 100 ? 58.013  42.378  1.259   1.00 27.73 ?  124  ALA A C   1 
ATOM   798   O  O   . ALA A  1 100 ? 58.643  41.603  0.538   1.00 27.87 ?  124  ALA A O   1 
ATOM   799   C  CB  . ALA A  1 100 ? 57.922  40.909  3.278   1.00 27.40 ?  124  ALA A CB  1 
ATOM   800   N  N   . ASN A  1 101 ? 57.154  43.278  0.784   1.00 28.12 ?  125  ASN A N   1 
ATOM   801   C  CA  . ASN A  1 101 ? 56.870  43.419  -0.642  1.00 28.62 ?  125  ASN A CA  1 
ATOM   802   C  C   . ASN A  1 101 ? 56.833  44.886  -1.058  1.00 28.95 ?  125  ASN A C   1 
ATOM   803   O  O   . ASN A  1 101 ? 55.860  45.341  -1.659  1.00 28.99 ?  125  ASN A O   1 
ATOM   804   C  CB  . ASN A  1 101 ? 55.528  42.757  -1.010  1.00 28.82 ?  125  ASN A CB  1 
ATOM   805   C  CG  . ASN A  1 101 ? 55.453  41.295  -0.606  1.00 28.88 ?  125  ASN A CG  1 
ATOM   806   O  OD1 . ASN A  1 101 ? 55.702  40.406  -1.416  1.00 29.91 ?  125  ASN A OD1 1 
ATOM   807   N  ND2 . ASN A  1 101 ? 55.095  41.042  0.647   1.00 28.70 ?  125  ASN A ND2 1 
ATOM   808   N  N   . LEU A  1 102 ? 57.893  45.625  -0.743  1.00 29.54 ?  126  LEU A N   1 
ATOM   809   C  CA  . LEU A  1 102 ? 57.931  47.064  -1.009  1.00 30.16 ?  126  LEU A CA  1 
ATOM   810   C  C   . LEU A  1 102 ? 57.916  47.423  -2.501  1.00 30.93 ?  126  LEU A C   1 
ATOM   811   O  O   . LEU A  1 102 ? 57.465  48.508  -2.874  1.00 30.94 ?  126  LEU A O   1 
ATOM   812   C  CB  . LEU A  1 102 ? 59.122  47.722  -0.305  1.00 29.85 ?  126  LEU A CB  1 
ATOM   813   C  CG  . LEU A  1 102 ? 59.137  47.739  1.228   1.00 29.55 ?  126  LEU A CG  1 
ATOM   814   C  CD1 . LEU A  1 102 ? 60.326  48.541  1.722   1.00 28.93 ?  126  LEU A CD1 1 
ATOM   815   C  CD2 . LEU A  1 102 ? 57.837  48.292  1.816   1.00 28.43 ?  126  LEU A CD2 1 
ATOM   816   N  N   . ASP A  1 103 ? 58.398  46.513  -3.346  1.00 31.76 ?  127  ASP A N   1 
ATOM   817   C  CA  . ASP A  1 103 ? 58.382  46.731  -4.797  1.00 32.76 ?  127  ASP A CA  1 
ATOM   818   C  C   . ASP A  1 103 ? 56.968  46.744  -5.376  1.00 33.00 ?  127  ASP A C   1 
ATOM   819   O  O   . ASP A  1 103 ? 56.711  47.399  -6.385  1.00 33.26 ?  127  ASP A O   1 
ATOM   820   C  CB  . ASP A  1 103 ? 59.268  45.709  -5.515  1.00 33.11 ?  127  ASP A CB  1 
ATOM   821   C  CG  . ASP A  1 103 ? 60.748  46.029  -5.379  1.00 34.09 ?  127  ASP A CG  1 
ATOM   822   O  OD1 . ASP A  1 103 ? 61.128  47.197  -5.618  1.00 35.23 ?  127  ASP A OD1 1 
ATOM   823   O  OD2 . ASP A  1 103 ? 61.529  45.118  -5.031  1.00 36.14 -1 127  ASP A OD2 1 
ATOM   824   N  N   . LYS A  1 104 ? 56.067  46.020  -4.717  1.00 33.32 ?  128  LYS A N   1 
ATOM   825   C  CA  . LYS A  1 104 ? 54.643  45.997  -5.044  1.00 33.65 ?  128  LYS A CA  1 
ATOM   826   C  C   . LYS A  1 104 ? 54.045  47.391  -4.868  1.00 33.60 ?  128  LYS A C   1 
ATOM   827   O  O   . LYS A  1 104 ? 53.230  47.836  -5.677  1.00 33.51 ?  128  LYS A O   1 
ATOM   828   C  CB  . LYS A  1 104 ? 53.943  44.999  -4.121  1.00 33.80 ?  128  LYS A CB  1 
ATOM   829   C  CG  . LYS A  1 104 ? 52.675  44.360  -4.654  1.00 34.91 ?  128  LYS A CG  1 
ATOM   830   C  CD  . LYS A  1 104 ? 52.414  43.050  -3.901  1.00 35.64 ?  128  LYS A CD  1 
ATOM   831   C  CE  . LYS A  1 104 ? 50.940  42.672  -3.881  1.00 35.97 ?  128  LYS A CE  1 
ATOM   832   N  NZ  . LYS A  1 104 ? 50.729  41.376  -3.169  1.00 36.00 ?  128  LYS A NZ  1 
ATOM   833   N  N   . ILE A  1 105 ? 54.477  48.074  -3.809  1.00 33.71 ?  129  ILE A N   1 
ATOM   834   C  CA  . ILE A  1 105 ? 54.062  49.445  -3.508  1.00 33.86 ?  129  ILE A CA  1 
ATOM   835   C  C   . ILE A  1 105 ? 54.623  50.450  -4.522  1.00 34.19 ?  129  ILE A C   1 
ATOM   836   O  O   . ILE A  1 105 ? 53.942  51.409  -4.896  1.00 34.05 ?  129  ILE A O   1 
ATOM   837   C  CB  . ILE A  1 105 ? 54.462  49.849  -2.055  1.00 33.73 ?  129  ILE A CB  1 
ATOM   838   C  CG1 . ILE A  1 105 ? 53.896  48.854  -1.026  1.00 33.44 ?  129  ILE A CG1 1 
ATOM   839   C  CG2 . ILE A  1 105 ? 54.043  51.284  -1.734  1.00 33.36 ?  129  ILE A CG2 1 
ATOM   840   C  CD1 . ILE A  1 105 ? 52.365  48.698  -1.030  1.00 32.73 ?  129  ILE A CD1 1 
ATOM   841   N  N   . ARG A  1 106 ? 55.857  50.221  -4.968  1.00 34.70 ?  130  ARG A N   1 
ATOM   842   C  CA  . ARG A  1 106 ? 56.494  51.077  -5.976  1.00 35.26 ?  130  ARG A CA  1 
ATOM   843   C  C   . ARG A  1 106 ? 55.796  51.017  -7.329  1.00 35.76 ?  130  ARG A C   1 
ATOM   844   O  O   . ARG A  1 106 ? 55.802  51.994  -8.081  1.00 35.97 ?  130  ARG A O   1 
ATOM   845   C  CB  . ARG A  1 106 ? 57.974  50.723  -6.145  1.00 35.19 ?  130  ARG A CB  1 
ATOM   846   C  CG  . ARG A  1 106 ? 58.810  51.117  -4.959  1.00 34.69 ?  130  ARG A CG  1 
ATOM   847   C  CD  . ARG A  1 106 ? 60.296  51.180  -5.260  1.00 34.16 ?  130  ARG A CD  1 
ATOM   848   N  NE  . ARG A  1 106 ? 61.017  51.497  -4.029  1.00 33.23 ?  130  ARG A NE  1 
ATOM   849   C  CZ  . ARG A  1 106 ? 61.459  50.591  -3.161  1.00 32.32 ?  130  ARG A CZ  1 
ATOM   850   N  NH1 . ARG A  1 106 ? 61.289  49.295  -3.394  1.00 31.95 ?  130  ARG A NH1 1 
ATOM   851   N  NH2 . ARG A  1 106 ? 62.083  50.985  -2.062  1.00 32.17 ?  130  ARG A NH2 1 
ATOM   852   N  N   . ASN A  1 107 ? 55.197  49.868  -7.626  1.00 36.35 ?  131  ASN A N   1 
ATOM   853   C  CA  . ASN A  1 107 ? 54.535  49.641  -8.907  1.00 36.94 ?  131  ASN A CA  1 
ATOM   854   C  C   . ASN A  1 107 ? 53.041  49.975  -8.908  1.00 37.09 ?  131  ASN A C   1 
ATOM   855   O  O   . ASN A  1 107 ? 52.338  49.686  -9.881  1.00 37.05 ?  131  ASN A O   1 
ATOM   856   C  CB  . ASN A  1 107 ? 54.775  48.203  -9.374  1.00 37.14 ?  131  ASN A CB  1 
ATOM   857   C  CG  . ASN A  1 107 ? 56.215  47.958  -9.793  1.00 38.18 ?  131  ASN A CG  1 
ATOM   858   O  OD1 . ASN A  1 107 ? 56.927  48.886  -10.190 1.00 39.59 ?  131  ASN A OD1 1 
ATOM   859   N  ND2 . ASN A  1 107 ? 56.652  46.705  -9.709  1.00 38.71 ?  131  ASN A ND2 1 
ATOM   860   N  N   . LEU A  1 108 ? 52.565  50.582  -7.820  1.00 37.38 ?  132  LEU A N   1 
ATOM   861   C  CA  . LEU A  1 108 ? 51.175  51.033  -7.726  1.00 37.68 ?  132  LEU A CA  1 
ATOM   862   C  C   . LEU A  1 108 ? 50.902  52.146  -8.738  1.00 37.89 ?  132  LEU A C   1 
ATOM   863   O  O   . LEU A  1 108 ? 51.655  53.119  -8.821  1.00 37.77 ?  132  LEU A O   1 
ATOM   864   C  CB  . LEU A  1 108 ? 50.838  51.510  -6.306  1.00 37.51 ?  132  LEU A CB  1 
ATOM   865   C  CG  . LEU A  1 108 ? 50.711  50.480  -5.175  1.00 37.54 ?  132  LEU A CG  1 
ATOM   866   C  CD1 . LEU A  1 108 ? 50.692  51.177  -3.820  1.00 36.59 ?  132  LEU A CD1 1 
ATOM   867   C  CD2 . LEU A  1 108 ? 49.474  49.593  -5.337  1.00 37.46 ?  132  LEU A CD2 1 
ATOM   868   N  N   . LYS A  1 109 ? 49.831  51.979  -9.510  1.00 38.29 ?  133  LYS A N   1 
ATOM   869   C  CA  . LYS A  1 109 ? 49.442  52.949  -10.536 1.00 38.77 ?  133  LYS A CA  1 
ATOM   870   C  C   . LYS A  1 109 ? 48.484  53.990  -9.958  1.00 38.77 ?  133  LYS A C   1 
ATOM   871   O  O   . LYS A  1 109 ? 47.880  53.768  -8.905  1.00 38.73 ?  133  LYS A O   1 
ATOM   872   C  CB  . LYS A  1 109 ? 48.806  52.242  -11.742 1.00 38.96 ?  133  LYS A CB  1 
ATOM   873   C  CG  . LYS A  1 109 ? 49.587  51.044  -12.298 1.00 39.68 ?  133  LYS A CG  1 
ATOM   874   C  CD  . LYS A  1 109 ? 50.931  51.455  -12.898 1.00 41.37 ?  133  LYS A CD  1 
ATOM   875   C  CE  . LYS A  1 109 ? 51.636  50.271  -13.547 1.00 42.08 ?  133  LYS A CE  1 
ATOM   876   N  NZ  . LYS A  1 109 ? 53.053  50.587  -13.891 1.00 42.72 ?  133  LYS A NZ  1 
ATOM   877   N  N   . SER A  1 110 ? 48.346  55.119  -10.654 1.00 38.78 ?  134  SER A N   1 
ATOM   878   C  CA  . SER A  1 110 ? 47.539  56.250  -10.179 1.00 38.83 ?  134  SER A CA  1 
ATOM   879   C  C   . SER A  1 110 ? 46.022  56.002  -10.188 1.00 38.68 ?  134  SER A C   1 
ATOM   880   O  O   . SER A  1 110 ? 45.258  56.797  -9.633  1.00 38.66 ?  134  SER A O   1 
ATOM   881   C  CB  . SER A  1 110 ? 47.870  57.512  -10.978 1.00 38.81 ?  134  SER A CB  1 
ATOM   882   O  OG  . SER A  1 110 ? 47.515  57.347  -12.339 1.00 39.37 ?  134  SER A OG  1 
ATOM   883   N  N   . ASP A  1 111 ? 45.594  54.909  -10.815 1.00 38.49 ?  135  ASP A N   1 
ATOM   884   C  CA  . ASP A  1 111 ? 44.177  54.536  -10.836 1.00 38.40 ?  135  ASP A CA  1 
ATOM   885   C  C   . ASP A  1 111 ? 43.824  53.500  -9.754  1.00 37.98 ?  135  ASP A C   1 
ATOM   886   O  O   . ASP A  1 111 ? 42.669  53.088  -9.633  1.00 37.92 ?  135  ASP A O   1 
ATOM   887   C  CB  . ASP A  1 111 ? 43.765  54.050  -12.235 1.00 38.57 ?  135  ASP A CB  1 
ATOM   888   C  CG  . ASP A  1 111 ? 44.470  52.768  -12.650 1.00 39.56 ?  135  ASP A CG  1 
ATOM   889   O  OD1 . ASP A  1 111 ? 45.605  52.518  -12.191 1.00 40.80 ?  135  ASP A OD1 1 
ATOM   890   O  OD2 . ASP A  1 111 ? 43.886  52.004  -13.447 1.00 40.85 -1 135  ASP A OD2 1 
ATOM   891   N  N   . ASP A  1 112 ? 44.829  53.092  -8.977  1.00 37.48 ?  136  ASP A N   1 
ATOM   892   C  CA  . ASP A  1 112 ? 44.651  52.172  -7.853  1.00 36.99 ?  136  ASP A CA  1 
ATOM   893   C  C   . ASP A  1 112 ? 44.245  52.975  -6.618  1.00 36.42 ?  136  ASP A C   1 
ATOM   894   O  O   . ASP A  1 112 ? 44.902  53.957  -6.283  1.00 36.42 ?  136  ASP A O   1 
ATOM   895   C  CB  . ASP A  1 112 ? 45.956  51.408  -7.579  1.00 37.02 ?  136  ASP A CB  1 
ATOM   896   C  CG  . ASP A  1 112 ? 45.755  50.162  -6.712  1.00 37.59 ?  136  ASP A CG  1 
ATOM   897   O  OD1 . ASP A  1 112 ? 45.145  50.255  -5.622  1.00 37.93 ?  136  ASP A OD1 1 
ATOM   898   O  OD2 . ASP A  1 112 ? 46.236  49.083  -7.119  1.00 37.54 -1 136  ASP A OD2 1 
ATOM   899   N  N   . PRO A  1 113 ? 43.160  52.560  -5.934  1.00 35.97 ?  137  PRO A N   1 
ATOM   900   C  CA  . PRO A  1 113 ? 42.739  53.255  -4.710  1.00 35.47 ?  137  PRO A CA  1 
ATOM   901   C  C   . PRO A  1 113 ? 43.771  53.204  -3.569  1.00 35.02 ?  137  PRO A C   1 
ATOM   902   O  O   . PRO A  1 113 ? 43.665  53.977  -2.618  1.00 35.02 ?  137  PRO A O   1 
ATOM   903   C  CB  . PRO A  1 113 ? 41.445  52.527  -4.312  1.00 35.57 ?  137  PRO A CB  1 
ATOM   904   C  CG  . PRO A  1 113 ? 41.472  51.228  -5.047  1.00 35.64 ?  137  PRO A CG  1 
ATOM   905   C  CD  . PRO A  1 113 ? 42.207  51.503  -6.320  1.00 35.98 ?  137  PRO A CD  1 
ATOM   906   N  N   . LEU A  1 114 ? 44.761  52.316  -3.676  1.00 34.45 ?  138  LEU A N   1 
ATOM   907   C  CA  . LEU A  1 114 ? 45.804  52.177  -2.652  1.00 33.99 ?  138  LEU A CA  1 
ATOM   908   C  C   . LEU A  1 114 ? 47.090  52.936  -2.997  1.00 33.63 ?  138  LEU A C   1 
ATOM   909   O  O   . LEU A  1 114 ? 48.110  52.786  -2.317  1.00 33.54 ?  138  LEU A O   1 
ATOM   910   C  CB  . LEU A  1 114 ? 46.122  50.695  -2.390  1.00 33.97 ?  138  LEU A CB  1 
ATOM   911   C  CG  . LEU A  1 114 ? 44.995  49.691  -2.109  1.00 34.13 ?  138  LEU A CG  1 
ATOM   912   C  CD1 . LEU A  1 114 ? 45.561  48.429  -1.471  1.00 34.53 ?  138  LEU A CD1 1 
ATOM   913   C  CD2 . LEU A  1 114 ? 43.893  50.278  -1.232  1.00 34.05 ?  138  LEU A CD2 1 
ATOM   914   N  N   . TYR A  1 115 ? 47.021  53.763  -4.038  1.00 33.16 ?  139  TYR A N   1 
ATOM   915   C  CA  . TYR A  1 115 ? 48.169  54.518  -4.557  1.00 32.77 ?  139  TYR A CA  1 
ATOM   916   C  C   . TYR A  1 115 ? 48.868  55.381  -3.504  1.00 32.29 ?  139  TYR A C   1 
ATOM   917   O  O   . TYR A  1 115 ? 50.083  55.589  -3.579  1.00 32.08 ?  139  TYR A O   1 
ATOM   918   C  CB  . TYR A  1 115 ? 47.722  55.383  -5.739  1.00 32.89 ?  139  TYR A CB  1 
ATOM   919   C  CG  . TYR A  1 115 ? 48.819  56.147  -6.454  1.00 33.67 ?  139  TYR A CG  1 
ATOM   920   C  CD1 . TYR A  1 115 ? 49.834  55.479  -7.136  1.00 34.26 ?  139  TYR A CD1 1 
ATOM   921   C  CD2 . TYR A  1 115 ? 48.816  57.541  -6.481  1.00 34.67 ?  139  TYR A CD2 1 
ATOM   922   C  CE1 . TYR A  1 115 ? 50.829  56.173  -7.810  1.00 34.89 ?  139  TYR A CE1 1 
ATOM   923   C  CE2 . TYR A  1 115 ? 49.810  58.248  -7.156  1.00 35.59 ?  139  TYR A CE2 1 
ATOM   924   C  CZ  . TYR A  1 115 ? 50.813  57.554  -7.816  1.00 35.33 ?  139  TYR A CZ  1 
ATOM   925   O  OH  . TYR A  1 115 ? 51.801  58.237  -8.483  1.00 35.90 ?  139  TYR A OH  1 
ATOM   926   N  N   . TYR A  1 116 ? 48.104  55.863  -2.524  1.00 31.64 ?  140  TYR A N   1 
ATOM   927   C  CA  . TYR A  1 116 ? 48.636  56.701  -1.444  1.00 31.11 ?  140  TYR A CA  1 
ATOM   928   C  C   . TYR A  1 116 ? 49.854  56.082  -0.746  1.00 31.26 ?  140  TYR A C   1 
ATOM   929   O  O   . TYR A  1 116 ? 50.701  56.803  -0.207  1.00 31.21 ?  140  TYR A O   1 
ATOM   930   C  CB  . TYR A  1 116 ? 47.534  57.033  -0.421  1.00 30.86 ?  140  TYR A CB  1 
ATOM   931   C  CG  . TYR A  1 116 ? 47.265  55.936  0.589   1.00 29.36 ?  140  TYR A CG  1 
ATOM   932   C  CD1 . TYR A  1 116 ? 46.376  54.901  0.300   1.00 27.92 ?  140  TYR A CD1 1 
ATOM   933   C  CD2 . TYR A  1 116 ? 47.903  55.932  1.832   1.00 27.81 ?  140  TYR A CD2 1 
ATOM   934   C  CE1 . TYR A  1 116 ? 46.131  53.891  1.217   1.00 27.11 ?  140  TYR A CE1 1 
ATOM   935   C  CE2 . TYR A  1 116 ? 47.666  54.922  2.761   1.00 27.21 ?  140  TYR A CE2 1 
ATOM   936   C  CZ  . TYR A  1 116 ? 46.776  53.903  2.444   1.00 27.10 ?  140  TYR A CZ  1 
ATOM   937   O  OH  . TYR A  1 116 ? 46.528  52.898  3.350   1.00 26.62 ?  140  TYR A OH  1 
ATOM   938   N  N   . LYS A  1 117 ? 49.928  54.749  -0.767  1.00 31.37 ?  141  LYS A N   1 
ATOM   939   C  CA  . LYS A  1 117 ? 51.012  53.992  -0.133  1.00 31.56 ?  141  LYS A CA  1 
ATOM   940   C  C   . LYS A  1 117 ? 52.380  54.245  -0.769  1.00 31.62 ?  141  LYS A C   1 
ATOM   941   O  O   . LYS A  1 117 ? 53.398  54.219  -0.075  1.00 31.56 ?  141  LYS A O   1 
ATOM   942   C  CB  . LYS A  1 117 ? 50.696  52.491  -0.143  1.00 31.64 ?  141  LYS A CB  1 
ATOM   943   C  CG  . LYS A  1 117 ? 49.693  52.045  0.921   1.00 31.45 ?  141  LYS A CG  1 
ATOM   944   C  CD  . LYS A  1 117 ? 48.819  50.912  0.404   1.00 31.70 ?  141  LYS A CD  1 
ATOM   945   C  CE  . LYS A  1 117 ? 48.504  49.874  1.475   1.00 32.62 ?  141  LYS A CE  1 
ATOM   946   N  NZ  . LYS A  1 117 ? 47.894  50.414  2.721   1.00 31.81 ?  141  LYS A NZ  1 
ATOM   947   N  N   . LYS A  1 118 ? 52.397  54.481  -2.082  1.00 31.76 ?  142  LYS A N   1 
ATOM   948   C  CA  . LYS A  1 118 ? 53.625  54.832  -2.806  1.00 31.77 ?  142  LYS A CA  1 
ATOM   949   C  C   . LYS A  1 118 ? 54.253  56.107  -2.239  1.00 31.69 ?  142  LYS A C   1 
ATOM   950   O  O   . LYS A  1 118 ? 55.469  56.170  -2.042  1.00 31.81 ?  142  LYS A O   1 
ATOM   951   C  CB  . LYS A  1 118 ? 53.347  54.984  -4.308  1.00 32.00 ?  142  LYS A CB  1 
ATOM   952   C  CG  . LYS A  1 118 ? 54.580  55.267  -5.172  1.00 32.25 ?  142  LYS A CG  1 
ATOM   953   C  CD  . LYS A  1 118 ? 54.253  55.097  -6.653  1.00 33.25 ?  142  LYS A CD  1 
ATOM   954   C  CE  . LYS A  1 118 ? 55.474  55.312  -7.539  1.00 34.02 ?  142  LYS A CE  1 
ATOM   955   N  NZ  . LYS A  1 118 ? 55.743  56.757  -7.774  1.00 35.06 ?  142  LYS A NZ  1 
ATOM   956   N  N   . GLY A  1 119 ? 53.418  57.112  -1.975  1.00 31.46 ?  143  GLY A N   1 
ATOM   957   C  CA  . GLY A  1 119 ? 53.870  58.354  -1.343  1.00 31.44 ?  143  GLY A CA  1 
ATOM   958   C  C   . GLY A  1 119 ? 54.384  58.135  0.071   1.00 31.36 ?  143  GLY A C   1 
ATOM   959   O  O   . GLY A  1 119 ? 55.365  58.752  0.485   1.00 31.47 ?  143  GLY A O   1 
ATOM   960   N  N   . LYS A  1 120 ? 53.721  57.248  0.809   1.00 31.27 ?  144  LYS A N   1 
ATOM   961   C  CA  . LYS A  1 120 ? 54.125  56.916  2.178   1.00 31.07 ?  144  LYS A CA  1 
ATOM   962   C  C   . LYS A  1 120 ? 55.491  56.232  2.231   1.00 30.86 ?  144  LYS A C   1 
ATOM   963   O  O   . LYS A  1 120 ? 56.289  56.507  3.125   1.00 30.52 ?  144  LYS A O   1 
ATOM   964   C  CB  . LYS A  1 120 ? 53.062  56.055  2.871   1.00 30.99 ?  144  LYS A CB  1 
ATOM   965   C  CG  . LYS A  1 120 ? 51.829  56.828  3.307   1.00 31.38 ?  144  LYS A CG  1 
ATOM   966   C  CD  . LYS A  1 120 ? 51.013  56.044  4.326   1.00 31.83 ?  144  LYS A CD  1 
ATOM   967   C  CE  . LYS A  1 120 ? 49.928  56.905  4.956   1.00 32.25 ?  144  LYS A CE  1 
ATOM   968   N  NZ  . LYS A  1 120 ? 50.483  58.073  5.708   1.00 32.78 ?  144  LYS A NZ  1 
ATOM   969   N  N   . LEU A  1 121 ? 55.745  55.339  1.274   1.00 30.95 ?  145  LEU A N   1 
ATOM   970   C  CA  . LEU A  1 121 ? 57.047  54.683  1.135   1.00 31.13 ?  145  LEU A CA  1 
ATOM   971   C  C   . LEU A  1 121 ? 58.153  55.701  0.857   1.00 31.21 ?  145  LEU A C   1 
ATOM   972   O  O   . LEU A  1 121 ? 59.234  55.630  1.452   1.00 31.23 ?  145  LEU A O   1 
ATOM   973   C  CB  . LEU A  1 121 ? 57.001  53.628  0.021   1.00 31.22 ?  145  LEU A CB  1 
ATOM   974   C  CG  . LEU A  1 121 ? 58.275  53.102  -0.661  1.00 31.27 ?  145  LEU A CG  1 
ATOM   975   C  CD1 . LEU A  1 121 ? 59.220  52.376  0.298   1.00 31.59 ?  145  LEU A CD1 1 
ATOM   976   C  CD2 . LEU A  1 121 ? 57.876  52.177  -1.787  1.00 31.65 ?  145  LEU A CD2 1 
ATOM   977   N  N   . GLU A  1 122 ? 57.868  56.643  -0.040  1.00 31.22 ?  146  GLU A N   1 
ATOM   978   C  CA  . GLU A  1 122 ? 58.832  57.675  -0.424  1.00 31.48 ?  146  GLU A CA  1 
ATOM   979   C  C   . GLU A  1 122 ? 59.155  58.610  0.742   1.00 31.36 ?  146  GLU A C   1 
ATOM   980   O  O   . GLU A  1 122 ? 60.309  59.009  0.922   1.00 31.24 ?  146  GLU A O   1 
ATOM   981   C  CB  . GLU A  1 122 ? 58.338  58.440  -1.660  1.00 31.48 ?  146  GLU A CB  1 
ATOM   982   C  CG  . GLU A  1 122 ? 58.431  57.607  -2.946  1.00 32.37 ?  146  GLU A CG  1 
ATOM   983   C  CD  . GLU A  1 122 ? 57.644  58.181  -4.118  1.00 33.47 ?  146  GLU A CD  1 
ATOM   984   O  OE1 . GLU A  1 122 ? 57.051  59.274  -3.982  1.00 34.32 ?  146  GLU A OE1 1 
ATOM   985   O  OE2 . GLU A  1 122 ? 57.615  57.524  -5.184  1.00 33.54 -1 146  GLU A OE2 1 
ATOM   986   N  N   . GLU A  1 123 ? 58.138  58.932  1.540   1.00 31.40 ?  147  GLU A N   1 
ATOM   987   C  CA  . GLU A  1 123 ? 58.321  59.709  2.769   1.00 31.38 ?  147  GLU A CA  1 
ATOM   988   C  C   . GLU A  1 123 ? 59.178  58.951  3.787   1.00 31.30 ?  147  GLU A C   1 
ATOM   989   O  O   . GLU A  1 123 ? 60.068  59.533  4.412   1.00 31.18 ?  147  GLU A O   1 
ATOM   990   C  CB  . GLU A  1 123 ? 56.965  60.081  3.379   1.00 31.50 ?  147  GLU A CB  1 
ATOM   991   C  CG  . GLU A  1 123 ? 57.059  60.933  4.642   1.00 31.96 ?  147  GLU A CG  1 
ATOM   992   C  CD  . GLU A  1 123 ? 55.716  61.469  5.091   1.00 33.59 ?  147  GLU A CD  1 
ATOM   993   O  OE1 . GLU A  1 123 ? 55.238  61.049  6.164   1.00 34.05 ?  147  GLU A OE1 1 
ATOM   994   O  OE2 . GLU A  1 123 ? 55.135  62.309  4.371   1.00 34.52 -1 147  GLU A OE2 1 
ATOM   995   N  N   . VAL A  1 124 ? 58.907  57.655  3.940   1.00 31.23 ?  148  VAL A N   1 
ATOM   996   C  CA  . VAL A  1 124 ? 59.686  56.795  4.831   1.00 31.20 ?  148  VAL A CA  1 
ATOM   997   C  C   . VAL A  1 124 ? 61.166  56.795  4.429   1.00 31.33 ?  148  VAL A C   1 
ATOM   998   O  O   . VAL A  1 124 ? 62.052  56.898  5.287   1.00 31.24 ?  148  VAL A O   1 
ATOM   999   C  CB  . VAL A  1 124 ? 59.116  55.351  4.883   1.00 31.12 ?  148  VAL A CB  1 
ATOM   1000  C  CG1 . VAL A  1 124 ? 60.159  54.361  5.401   1.00 30.87 ?  148  VAL A CG1 1 
ATOM   1001  C  CG2 . VAL A  1 124 ? 57.866  55.307  5.750   1.00 30.61 ?  148  VAL A CG2 1 
ATOM   1002  N  N   . GLU A  1 125 ? 61.415  56.697  3.126   1.00 31.42 ?  149  GLU A N   1 
ATOM   1003  C  CA  . GLU A  1 125 ? 62.770  56.725  2.575   1.00 31.70 ?  149  GLU A CA  1 
ATOM   1004  C  C   . GLU A  1 125 ? 63.476  58.066  2.810   1.00 31.84 ?  149  GLU A C   1 
ATOM   1005  O  O   . GLU A  1 125 ? 64.656  58.093  3.165   1.00 31.79 ?  149  GLU A O   1 
ATOM   1006  C  CB  . GLU A  1 125 ? 62.748  56.360  1.089   1.00 31.74 ?  149  GLU A CB  1 
ATOM   1007  C  CG  . GLU A  1 125 ? 62.489  54.874  0.853   1.00 32.27 ?  149  GLU A CG  1 
ATOM   1008  C  CD  . GLU A  1 125 ? 62.326  54.505  -0.608  1.00 32.91 ?  149  GLU A CD  1 
ATOM   1009  O  OE1 . GLU A  1 125 ? 61.780  55.313  -1.389  1.00 33.23 ?  149  GLU A OE1 1 
ATOM   1010  O  OE2 . GLU A  1 125 ? 62.729  53.381  -0.969  1.00 33.58 -1 149  GLU A OE2 1 
ATOM   1011  N  N   . ASN A  1 126 ? 62.745  59.166  2.632   1.00 32.02 ?  150  ASN A N   1 
ATOM   1012  C  CA  . ASN A  1 126 ? 63.275  60.500  2.907   1.00 32.28 ?  150  ASN A CA  1 
ATOM   1013  C  C   . ASN A  1 126 ? 63.657  60.666  4.381   1.00 32.15 ?  150  ASN A C   1 
ATOM   1014  O  O   . ASN A  1 126 ? 64.703  61.239  4.690   1.00 32.16 ?  150  ASN A O   1 
ATOM   1015  C  CB  . ASN A  1 126 ? 62.287  61.589  2.467   1.00 32.38 ?  150  ASN A CB  1 
ATOM   1016  C  CG  . ASN A  1 126 ? 62.873  62.996  2.569   1.00 33.31 ?  150  ASN A CG  1 
ATOM   1017  O  OD1 . ASN A  1 126 ? 62.387  63.830  3.337   1.00 33.91 ?  150  ASN A OD1 1 
ATOM   1018  N  ND2 . ASN A  1 126 ? 63.921  63.263  1.794   1.00 33.93 ?  150  ASN A ND2 1 
ATOM   1019  N  N   . ASN A  1 127 ? 62.813  60.150  5.277   1.00 31.94 ?  151  ASN A N   1 
ATOM   1020  C  CA  . ASN A  1 127 ? 63.106  60.131  6.713   1.00 31.81 ?  151  ASN A CA  1 
ATOM   1021  C  C   . ASN A  1 127 ? 64.425  59.417  7.013   1.00 31.80 ?  151  ASN A C   1 
ATOM   1022  O  O   . ASN A  1 127 ? 65.256  59.927  7.768   1.00 31.50 ?  151  ASN A O   1 
ATOM   1023  C  CB  . ASN A  1 127 ? 61.971  59.460  7.501   1.00 31.73 ?  151  ASN A CB  1 
ATOM   1024  C  CG  . ASN A  1 127 ? 60.667  60.247  7.460   1.00 31.61 ?  151  ASN A CG  1 
ATOM   1025  O  OD1 . ASN A  1 127 ? 60.658  61.469  7.301   1.00 31.18 ?  151  ASN A OD1 1 
ATOM   1026  N  ND2 . ASN A  1 127 ? 59.553  59.539  7.619   1.00 31.53 ?  151  ASN A ND2 1 
ATOM   1027  N  N   . LEU A  1 128 ? 64.605  58.246  6.404   1.00 31.94 ?  152  LEU A N   1 
ATOM   1028  C  CA  . LEU A  1 128 ? 65.795  57.419  6.607   1.00 32.39 ?  152  LEU A CA  1 
ATOM   1029  C  C   . LEU A  1 128 ? 67.066  58.028  6.011   1.00 32.74 ?  152  LEU A C   1 
ATOM   1030  O  O   . LEU A  1 128 ? 68.164  57.793  6.518   1.00 32.89 ?  152  LEU A O   1 
ATOM   1031  C  CB  . LEU A  1 128 ? 65.577  56.004  6.057   1.00 32.28 ?  152  LEU A CB  1 
ATOM   1032  C  CG  . LEU A  1 128 ? 64.573  55.078  6.755   1.00 31.93 ?  152  LEU A CG  1 
ATOM   1033  C  CD1 . LEU A  1 128 ? 64.554  53.718  6.068   1.00 31.45 ?  152  LEU A CD1 1 
ATOM   1034  C  CD2 . LEU A  1 128 ? 64.874  54.926  8.241   1.00 31.64 ?  152  LEU A CD2 1 
ATOM   1035  N  N   . ARG A  1 129 ? 66.911  58.802  4.940   1.00 33.22 ?  153  ARG A N   1 
ATOM   1036  C  CA  . ARG A  1 129 ? 68.028  59.533  4.338   1.00 33.75 ?  153  ARG A CA  1 
ATOM   1037  C  C   . ARG A  1 129 ? 68.462  60.686  5.232   1.00 34.12 ?  153  ARG A C   1 
ATOM   1038  O  O   . ARG A  1 129 ? 69.658  60.924  5.416   1.00 34.38 ?  153  ARG A O   1 
ATOM   1039  C  CB  . ARG A  1 129 ? 67.662  60.036  2.940   1.00 33.53 ?  153  ARG A CB  1 
ATOM   1040  C  CG  . ARG A  1 129 ? 67.663  58.940  1.898   1.00 33.44 ?  153  ARG A CG  1 
ATOM   1041  C  CD  . ARG A  1 129 ? 66.814  59.298  0.698   1.00 33.17 ?  153  ARG A CD  1 
ATOM   1042  N  NE  . ARG A  1 129 ? 66.701  58.168  -0.219  1.00 33.27 ?  153  ARG A NE  1 
ATOM   1043  C  CZ  . ARG A  1 129 ? 65.700  57.990  -1.076  1.00 33.34 ?  153  ARG A CZ  1 
ATOM   1044  N  NH1 . ARG A  1 129 ? 64.706  58.869  -1.140  1.00 33.43 ?  153  ARG A NH1 1 
ATOM   1045  N  NH2 . ARG A  1 129 ? 65.690  56.927  -1.866  1.00 32.82 ?  153  ARG A NH2 1 
ATOM   1046  N  N   . SER A  1 130 ? 67.480  61.385  5.796   1.00 34.58 ?  154  SER A N   1 
ATOM   1047  C  CA  . SER A  1 130 ? 67.728  62.439  6.774   1.00 34.84 ?  154  SER A CA  1 
ATOM   1048  C  C   . SER A  1 130 ? 68.474  61.911  8.003   1.00 35.21 ?  154  SER A C   1 
ATOM   1049  O  O   . SER A  1 130 ? 69.318  62.606  8.571   1.00 35.24 ?  154  SER A O   1 
ATOM   1050  C  CB  . SER A  1 130 ? 66.407  63.081  7.191   1.00 34.77 ?  154  SER A CB  1 
ATOM   1051  O  OG  . SER A  1 130 ? 66.615  64.147  8.099   1.00 34.91 ?  154  SER A OG  1 
ATOM   1052  N  N   . MET A  1 131 ? 68.165  60.677  8.396   1.00 35.69 ?  155  MET A N   1 
ATOM   1053  C  CA  . MET A  1 131 ? 68.770  60.050  9.572   1.00 36.13 ?  155  MET A CA  1 
ATOM   1054  C  C   . MET A  1 131 ? 70.086  59.332  9.254   1.00 36.44 ?  155  MET A C   1 
ATOM   1055  O  O   . MET A  1 131 ? 70.774  58.854  10.161  1.00 36.49 ?  155  MET A O   1 
ATOM   1056  C  CB  . MET A  1 131 ? 67.775  59.081  10.224  1.00 36.17 ?  155  MET A CB  1 
ATOM   1057  C  CG  . MET A  1 131 ? 66.529  59.763  10.779  1.00 36.62 ?  155  MET A CG  1 
ATOM   1058  S  SD  . MET A  1 131 ? 65.155  58.629  11.047  1.00 37.50 ?  155  MET A SD  1 
ATOM   1059  C  CE  . MET A  1 131 ? 63.788  59.789  11.120  1.00 37.24 ?  155  MET A CE  1 
ATOM   1060  N  N   . GLY A  1 132 ? 70.425  59.260  7.967   1.00 36.76 ?  156  GLY A N   1 
ATOM   1061  C  CA  . GLY A  1 132 ? 71.649  58.600  7.516   1.00 37.28 ?  156  GLY A CA  1 
ATOM   1062  C  C   . GLY A  1 132 ? 71.597  57.083  7.557   1.00 37.70 ?  156  GLY A C   1 
ATOM   1063  O  O   . GLY A  1 132 ? 72.637  56.425  7.558   1.00 37.86 ?  156  GLY A O   1 
ATOM   1064  N  N   . LYS A  1 133 ? 70.386  56.527  7.589   1.00 37.94 ?  157  LYS A N   1 
ATOM   1065  C  CA  . LYS A  1 133 ? 70.194  55.076  7.605   1.00 38.17 ?  157  LYS A CA  1 
ATOM   1066  C  C   . LYS A  1 133 ? 69.926  54.551  6.195   1.00 38.15 ?  157  LYS A C   1 
ATOM   1067  O  O   . LYS A  1 133 ? 69.747  53.351  5.993   1.00 38.13 ?  157  LYS A O   1 
ATOM   1068  C  CB  . LYS A  1 133 ? 69.039  54.681  8.545   1.00 38.25 ?  157  LYS A CB  1 
ATOM   1069  C  CG  . LYS A  1 133 ? 69.111  55.252  9.968   1.00 38.44 ?  157  LYS A CG  1 
ATOM   1070  C  CD  . LYS A  1 133 ? 70.225  54.631  10.808  1.00 39.39 ?  157  LYS A CD  1 
ATOM   1071  C  CE  . LYS A  1 133 ? 69.835  53.267  11.360  1.00 39.92 ?  157  LYS A CE  1 
ATOM   1072  N  NZ  . LYS A  1 133 ? 70.998  52.590  12.006  1.00 40.18 ?  157  LYS A NZ  1 
ATOM   1073  N  N   . LEU A  1 134 ? 69.901  55.464  5.227   1.00 38.40 ?  158  LEU A N   1 
ATOM   1074  C  CA  . LEU A  1 134 ? 69.644  55.136  3.826   1.00 38.52 ?  158  LEU A CA  1 
ATOM   1075  C  C   . LEU A  1 134 ? 70.318  56.156  2.909   1.00 38.85 ?  158  LEU A C   1 
ATOM   1076  O  O   . LEU A  1 134 ? 70.302  57.356  3.190   1.00 38.84 ?  158  LEU A O   1 
ATOM   1077  C  CB  . LEU A  1 134 ? 68.135  55.113  3.561   1.00 38.35 ?  158  LEU A CB  1 
ATOM   1078  C  CG  . LEU A  1 134 ? 67.609  54.576  2.227   1.00 38.12 ?  158  LEU A CG  1 
ATOM   1079  C  CD1 . LEU A  1 134 ? 67.670  53.054  2.184   1.00 37.36 ?  158  LEU A CD1 1 
ATOM   1080  C  CD2 . LEU A  1 134 ? 66.186  55.057  2.002   1.00 37.64 ?  158  LEU A CD2 1 
ATOM   1081  N  N   . GLY A  1 135 ? 70.907  55.672  1.816   1.00 39.28 ?  159  GLY A N   1 
ATOM   1082  C  CA  . GLY A  1 135 ? 71.567  56.537  0.834   1.00 39.64 ?  159  GLY A CA  1 
ATOM   1083  C  C   . GLY A  1 135 ? 70.576  57.341  0.012   1.00 40.06 ?  159  GLY A C   1 
ATOM   1084  O  O   . GLY A  1 135 ? 69.421  56.938  -0.139  1.00 40.14 ?  159  GLY A O   1 
ATOM   1085  N  N   . GLU A  1 136 ? 71.030  58.474  -0.527  1.00 40.37 ?  160  GLU A N   1 
ATOM   1086  C  CA  . GLU A  1 136 ? 70.169  59.377  -1.307  1.00 40.70 ?  160  GLU A CA  1 
ATOM   1087  C  C   . GLU A  1 136 ? 69.643  58.745  -2.598  1.00 40.45 ?  160  GLU A C   1 
ATOM   1088  O  O   . GLU A  1 136 ? 68.564  59.103  -3.076  1.00 40.42 ?  160  GLU A O   1 
ATOM   1089  C  CB  . GLU A  1 136 ? 70.884  60.702  -1.619  1.00 41.02 ?  160  GLU A CB  1 
ATOM   1090  C  CG  . GLU A  1 136 ? 71.442  61.457  -0.396  1.00 42.36 ?  160  GLU A CG  1 
ATOM   1091  C  CD  . GLU A  1 136 ? 70.404  61.718  0.694   1.00 43.86 ?  160  GLU A CD  1 
ATOM   1092  O  OE1 . GLU A  1 136 ? 69.305  62.231  0.383   1.00 44.46 ?  160  GLU A OE1 1 
ATOM   1093  O  OE2 . GLU A  1 136 ? 70.699  61.417  1.872   1.00 44.74 -1 160  GLU A OE2 1 
ATOM   1094  N  N   . LYS A  1 137 ? 70.413  57.812  -3.154  1.00 40.30 ?  161  LYS A N   1 
ATOM   1095  C  CA  . LYS A  1 137 ? 69.996  57.041  -4.329  1.00 40.03 ?  161  LYS A CA  1 
ATOM   1096  C  C   . LYS A  1 137 ? 69.448  55.662  -3.953  1.00 39.56 ?  161  LYS A C   1 
ATOM   1097  O  O   . LYS A  1 137 ? 68.802  54.998  -4.768  1.00 39.62 ?  161  LYS A O   1 
ATOM   1098  C  CB  . LYS A  1 137 ? 71.169  56.857  -5.292  1.00 40.17 ?  161  LYS A CB  1 
ATOM   1099  C  CG  . LYS A  1 137 ? 71.312  57.928  -6.358  1.00 40.94 ?  161  LYS A CG  1 
ATOM   1100  C  CD  . LYS A  1 137 ? 71.834  57.339  -7.676  1.00 41.99 ?  161  LYS A CD  1 
ATOM   1101  C  CE  . LYS A  1 137 ? 73.021  56.405  -7.464  1.00 42.47 ?  161  LYS A CE  1 
ATOM   1102  N  NZ  . LYS A  1 137 ? 73.556  55.843  -8.737  1.00 44.01 ?  161  LYS A NZ  1 
ATOM   1103  N  N   . GLU A  1 138 ? 69.721  55.237  -2.722  1.00 38.92 ?  162  GLU A N   1 
ATOM   1104  C  CA  . GLU A  1 138 ? 69.363  53.899  -2.254  1.00 38.15 ?  162  GLU A CA  1 
ATOM   1105  C  C   . GLU A  1 138 ? 67.877  53.795  -1.912  1.00 37.52 ?  162  GLU A C   1 
ATOM   1106  O  O   . GLU A  1 138 ? 67.345  54.618  -1.162  1.00 37.42 ?  162  GLU A O   1 
ATOM   1107  C  CB  . GLU A  1 138 ? 70.221  53.525  -1.042  1.00 38.13 ?  162  GLU A CB  1 
ATOM   1108  C  CG  . GLU A  1 138 ? 70.082  52.080  -0.572  1.00 38.49 ?  162  GLU A CG  1 
ATOM   1109  C  CD  . GLU A  1 138 ? 70.716  51.843  0.790   1.00 39.16 ?  162  GLU A CD  1 
ATOM   1110  O  OE1 . GLU A  1 138 ? 71.028  52.832  1.491   1.00 39.59 ?  162  GLU A OE1 1 
ATOM   1111  O  OE2 . GLU A  1 138 ? 70.898  50.666  1.167   1.00 39.94 -1 162  GLU A OE2 1 
ATOM   1112  N  N   . THR A  1 139 ? 67.214  52.791  -2.481  1.00 36.68 ?  163  THR A N   1 
ATOM   1113  C  CA  . THR A  1 139 ? 65.831  52.478  -2.120  1.00 35.91 ?  163  THR A CA  1 
ATOM   1114  C  C   . THR A  1 139 ? 65.802  51.549  -0.906  1.00 35.13 ?  163  THR A C   1 
ATOM   1115  O  O   . THR A  1 139 ? 66.737  50.778  -0.682  1.00 35.11 ?  163  THR A O   1 
ATOM   1116  C  CB  . THR A  1 139 ? 65.043  51.818  -3.284  1.00 36.02 ?  163  THR A CB  1 
ATOM   1117  O  OG1 . THR A  1 139 ? 65.756  50.674  -3.775  1.00 36.01 ?  163  THR A OG1 1 
ATOM   1118  C  CG2 . THR A  1 139 ? 64.808  52.805  -4.423  1.00 36.05 ?  163  THR A CG2 1 
ATOM   1119  N  N   . LEU A  1 140 ? 64.734  51.640  -0.118  1.00 34.19 ?  164  LEU A N   1 
ATOM   1120  C  CA  . LEU A  1 140 ? 64.505  50.707  0.979   1.00 33.22 ?  164  LEU A CA  1 
ATOM   1121  C  C   . LEU A  1 140 ? 64.088  49.360  0.386   1.00 32.68 ?  164  LEU A C   1 
ATOM   1122  O  O   . LEU A  1 140 ? 63.032  49.247  -0.248  1.00 32.57 ?  164  LEU A O   1 
ATOM   1123  C  CB  . LEU A  1 140 ? 63.441  51.255  1.940   1.00 33.33 ?  164  LEU A CB  1 
ATOM   1124  C  CG  . LEU A  1 140 ? 63.130  50.522  3.251   1.00 33.02 ?  164  LEU A CG  1 
ATOM   1125  C  CD1 . LEU A  1 140 ? 64.363  50.363  4.135   1.00 32.44 ?  164  LEU A CD1 1 
ATOM   1126  C  CD2 . LEU A  1 140 ? 62.024  51.252  4.001   1.00 32.53 ?  164  LEU A CD2 1 
ATOM   1127  N  N   . LYS A  1 141 ? 64.936  48.350  0.567   1.00 31.83 ?  165  LYS A N   1 
ATOM   1128  C  CA  . LYS A  1 141 ? 64.723  47.049  -0.068  1.00 31.22 ?  165  LYS A CA  1 
ATOM   1129  C  C   . LYS A  1 141 ? 63.588  46.258  0.586   1.00 30.60 ?  165  LYS A C   1 
ATOM   1130  O  O   . LYS A  1 141 ? 62.780  45.629  -0.107  1.00 30.45 ?  165  LYS A O   1 
ATOM   1131  C  CB  . LYS A  1 141 ? 66.027  46.241  -0.110  1.00 31.37 ?  165  LYS A CB  1 
ATOM   1132  C  CG  . LYS A  1 141 ? 67.130  46.901  -0.952  1.00 31.74 ?  165  LYS A CG  1 
ATOM   1133  C  CD  . LYS A  1 141 ? 66.954  46.632  -2.452  1.00 32.68 ?  165  LYS A CD  1 
ATOM   1134  C  CE  . LYS A  1 141 ? 67.260  47.862  -3.317  1.00 33.36 ?  165  LYS A CE  1 
ATOM   1135  N  NZ  . LYS A  1 141 ? 68.416  48.701  -2.854  1.00 33.27 ?  165  LYS A NZ  1 
ATOM   1136  N  N   . GLU A  1 142 ? 63.532  46.301  1.916   1.00 29.57 ?  166  GLU A N   1 
ATOM   1137  C  CA  . GLU A  1 142 ? 62.495  45.610  2.681   1.00 28.87 ?  166  GLU A CA  1 
ATOM   1138  C  C   . GLU A  1 142 ? 62.467  46.098  4.122   1.00 28.20 ?  166  GLU A C   1 
ATOM   1139  O  O   . GLU A  1 142 ? 63.356  46.827  4.564   1.00 28.12 ?  166  GLU A O   1 
ATOM   1140  C  CB  . GLU A  1 142 ? 62.701  44.086  2.655   1.00 28.77 ?  166  GLU A CB  1 
ATOM   1141  C  CG  . GLU A  1 142 ? 63.985  43.609  3.331   1.00 29.35 ?  166  GLU A CG  1 
ATOM   1142  C  CD  . GLU A  1 142 ? 64.058  42.094  3.513   1.00 29.78 ?  166  GLU A CD  1 
ATOM   1143  O  OE1 . GLU A  1 142 ? 63.361  41.346  2.791   1.00 29.27 ?  166  GLU A OE1 1 
ATOM   1144  O  OE2 . GLU A  1 142 ? 64.834  41.652  4.385   1.00 29.66 -1 166  GLU A OE2 1 
ATOM   1145  N  N   . VAL A  1 143 ? 61.427  45.700  4.841   1.00 27.42 ?  167  VAL A N   1 
ATOM   1146  C  CA  . VAL A  1 143 ? 61.407  45.820  6.289   1.00 26.77 ?  167  VAL A CA  1 
ATOM   1147  C  C   . VAL A  1 143 ? 61.317  44.392  6.810   1.00 26.35 ?  167  VAL A C   1 
ATOM   1148  O  O   . VAL A  1 143 ? 60.232  43.809  6.855   1.00 26.29 ?  167  VAL A O   1 
ATOM   1149  C  CB  . VAL A  1 143 ? 60.220  46.670  6.789   1.00 26.72 ?  167  VAL A CB  1 
ATOM   1150  C  CG1 . VAL A  1 143 ? 60.409  47.049  8.248   1.00 26.53 ?  167  VAL A CG1 1 
ATOM   1151  C  CG2 . VAL A  1 143 ? 60.047  47.913  5.925   1.00 26.42 ?  167  VAL A CG2 1 
ATOM   1152  N  N   . GLY A  1 144 ? 62.473  43.835  7.170   1.00 25.87 ?  168  GLY A N   1 
ATOM   1153  C  CA  . GLY A  1 144 ? 62.582  42.445  7.612   1.00 25.42 ?  168  GLY A CA  1 
ATOM   1154  C  C   . GLY A  1 144 ? 62.900  42.289  9.086   1.00 25.02 ?  168  GLY A C   1 
ATOM   1155  O  O   . GLY A  1 144 ? 62.987  43.275  9.817   1.00 25.17 ?  168  GLY A O   1 
ATOM   1156  N  N   . CYS A  1 145 ? 63.082  41.043  9.517   1.00 24.77 ?  169  CYS A N   1 
ATOM   1157  C  CA  . CYS A  1 145 ? 63.300  40.721  10.933  1.00 24.59 ?  169  CYS A CA  1 
ATOM   1158  C  C   . CYS A  1 145 ? 64.443  41.530  11.536  1.00 24.59 ?  169  CYS A C   1 
ATOM   1159  O  O   . CYS A  1 145 ? 64.297  42.126  12.606  1.00 24.52 ?  169  CYS A O   1 
ATOM   1160  C  CB  . CYS A  1 145 ? 63.569  39.224  11.117  1.00 24.32 ?  169  CYS A CB  1 
ATOM   1161  S  SG  . CYS A  1 145 ? 62.702  38.133  9.952   1.00 24.06 ?  169  CYS A SG  1 
ATOM   1162  N  N   . ILE A  1 146 ? 65.571  41.559  10.829  1.00 24.67 ?  170  ILE A N   1 
ATOM   1163  C  CA  . ILE A  1 146 ? 66.772  42.262  11.278  1.00 24.67 ?  170  ILE A CA  1 
ATOM   1164  C  C   . ILE A  1 146 ? 66.545  43.777  11.447  1.00 24.82 ?  170  ILE A C   1 
ATOM   1165  O  O   . ILE A  1 146 ? 67.144  44.399  12.323  1.00 24.87 ?  170  ILE A O   1 
ATOM   1166  C  CB  . ILE A  1 146 ? 67.992  41.950  10.343  1.00 24.51 ?  170  ILE A CB  1 
ATOM   1167  C  CG1 . ILE A  1 146 ? 69.330  42.258  11.039  1.00 24.46 ?  170  ILE A CG1 1 
ATOM   1168  C  CG2 . ILE A  1 146 ? 67.859  42.650  8.985   1.00 24.48 ?  170  ILE A CG2 1 
ATOM   1169  C  CD1 . ILE A  1 146 ? 70.553  41.598  10.371  1.00 23.30 ?  170  ILE A CD1 1 
ATOM   1170  N  N   . ASP A  1 147 ? 65.664  44.350  10.627  1.00 24.94 ?  171  ASP A N   1 
ATOM   1171  C  CA  . ASP A  1 147 ? 65.411  45.797  10.634  1.00 25.02 ?  171  ASP A CA  1 
ATOM   1172  C  C   . ASP A  1 147 ? 64.688  46.281  11.892  1.00 25.02 ?  171  ASP A C   1 
ATOM   1173  O  O   . ASP A  1 147 ? 65.158  47.208  12.566  1.00 25.02 ?  171  ASP A O   1 
ATOM   1174  C  CB  . ASP A  1 147 ? 64.642  46.208  9.378   1.00 25.06 ?  171  ASP A CB  1 
ATOM   1175  C  CG  . ASP A  1 147 ? 65.415  45.916  8.108   1.00 25.48 ?  171  ASP A CG  1 
ATOM   1176  O  OD1 . ASP A  1 147 ? 66.539  46.442  7.962   1.00 24.93 ?  171  ASP A OD1 1 
ATOM   1177  O  OD2 . ASP A  1 147 ? 64.903  45.153  7.263   1.00 25.74 -1 171  ASP A OD2 1 
ATOM   1178  N  N   . CYS A  1 148 ? 63.555  45.655  12.204  1.00 24.69 ?  172  CYS A N   1 
ATOM   1179  C  CA  . CYS A  1 148 ? 62.799  45.996  13.406  1.00 24.74 ?  172  CYS A CA  1 
ATOM   1180  C  C   . CYS A  1 148 ? 63.468  45.454  14.663  1.00 24.90 ?  172  CYS A C   1 
ATOM   1181  O  O   . CYS A  1 148 ? 63.480  46.123  15.694  1.00 25.02 ?  172  CYS A O   1 
ATOM   1182  C  CB  . CYS A  1 148 ? 61.366  45.461  13.328  1.00 24.46 ?  172  CYS A CB  1 
ATOM   1183  S  SG  . CYS A  1 148 ? 60.279  46.292  12.143  1.00 23.37 ?  172  CYS A SG  1 
ATOM   1184  N  N   . HIS A  1 149 ? 64.018  44.243  14.570  1.00 25.23 ?  173  HIS A N   1 
ATOM   1185  C  CA  . HIS A  1 149 ? 64.513  43.524  15.745  1.00 25.49 ?  173  HIS A CA  1 
ATOM   1186  C  C   . HIS A  1 149 ? 65.998  43.744  16.082  1.00 25.91 ?  173  HIS A C   1 
ATOM   1187  O  O   . HIS A  1 149 ? 66.461  43.303  17.138  1.00 25.82 ?  173  HIS A O   1 
ATOM   1188  C  CB  . HIS A  1 149 ? 64.197  42.022  15.640  1.00 25.38 ?  173  HIS A CB  1 
ATOM   1189  C  CG  . HIS A  1 149 ? 62.739  41.691  15.768  1.00 24.82 ?  173  HIS A CG  1 
ATOM   1190  N  ND1 . HIS A  1 149 ? 62.071  41.740  16.972  1.00 23.93 ?  173  HIS A ND1 1 
ATOM   1191  C  CD2 . HIS A  1 149 ? 61.828  41.283  14.849  1.00 23.81 ?  173  HIS A CD2 1 
ATOM   1192  C  CE1 . HIS A  1 149 ? 60.810  41.387  16.788  1.00 24.37 ?  173  HIS A CE1 1 
ATOM   1193  N  NE2 . HIS A  1 149 ? 60.633  41.106  15.509  1.00 23.92 ?  173  HIS A NE2 1 
ATOM   1194  N  N   . VAL A  1 150 ? 66.740  44.419  15.202  1.00 26.37 ?  174  VAL A N   1 
ATOM   1195  C  CA  . VAL A  1 150 ? 68.134  44.789  15.505  1.00 26.83 ?  174  VAL A CA  1 
ATOM   1196  C  C   . VAL A  1 150 ? 68.448  46.262  15.198  1.00 27.21 ?  174  VAL A C   1 
ATOM   1197  O  O   . VAL A  1 150 ? 68.758  47.035  16.105  1.00 27.31 ?  174  VAL A O   1 
ATOM   1198  C  CB  . VAL A  1 150 ? 69.177  43.855  14.809  1.00 26.76 ?  174  VAL A CB  1 
ATOM   1199  C  CG1 . VAL A  1 150 ? 70.596  44.270  15.181  1.00 26.97 ?  174  VAL A CG1 1 
ATOM   1200  C  CG2 . VAL A  1 150 ? 68.950  42.397  15.184  1.00 26.09 ?  174  VAL A CG2 1 
ATOM   1201  N  N   . ASP A  1 151 ? 68.367  46.638  13.924  1.00 27.69 ?  175  ASP A N   1 
ATOM   1202  C  CA  . ASP A  1 151 ? 68.750  47.978  13.470  1.00 28.33 ?  175  ASP A CA  1 
ATOM   1203  C  C   . ASP A  1 151 ? 68.237  48.174  12.050  1.00 28.39 ?  175  ASP A C   1 
ATOM   1204  O  O   . ASP A  1 151 ? 68.422  47.302  11.198  1.00 28.33 ?  175  ASP A O   1 
ATOM   1205  C  CB  . ASP A  1 151 ? 70.284  48.146  13.517  1.00 28.49 ?  175  ASP A CB  1 
ATOM   1206  C  CG  . ASP A  1 151 ? 70.738  49.571  13.232  1.00 29.37 ?  175  ASP A CG  1 
ATOM   1207  O  OD1 . ASP A  1 151 ? 70.066  50.528  13.675  1.00 29.69 ?  175  ASP A OD1 1 
ATOM   1208  O  OD2 . ASP A  1 151 ? 71.789  49.735  12.571  1.00 30.95 -1 175  ASP A OD2 1 
ATOM   1209  N  N   . VAL A  1 152 ? 67.592  49.315  11.805  1.00 28.73 ?  176  VAL A N   1 
ATOM   1210  C  CA  . VAL A  1 152 ? 66.995  49.622  10.497  1.00 29.27 ?  176  VAL A CA  1 
ATOM   1211  C  C   . VAL A  1 152 ? 68.047  49.650  9.381   1.00 29.82 ?  176  VAL A C   1 
ATOM   1212  O  O   . VAL A  1 152 ? 69.037  50.380  9.469   1.00 29.73 ?  176  VAL A O   1 
ATOM   1213  C  CB  . VAL A  1 152 ? 66.182  50.948  10.526  1.00 29.10 ?  176  VAL A CB  1 
ATOM   1214  C  CG1 . VAL A  1 152 ? 65.779  51.381  9.119   1.00 29.54 ?  176  VAL A CG1 1 
ATOM   1215  C  CG2 . VAL A  1 152 ? 64.944  50.798  11.399  1.00 28.79 ?  176  VAL A CG2 1 
ATOM   1216  N  N   . ASN A  1 153 ? 67.815  48.840  8.346   1.00 30.51 ?  177  ASN A N   1 
ATOM   1217  C  CA  . ASN A  1 153 ? 68.698  48.727  7.176   1.00 31.25 ?  177  ASN A CA  1 
ATOM   1218  C  C   . ASN A  1 153 ? 70.103  48.206  7.519   1.00 31.44 ?  177  ASN A C   1 
ATOM   1219  O  O   . ASN A  1 153 ? 71.099  48.633  6.927   1.00 31.41 ?  177  ASN A O   1 
ATOM   1220  C  CB  . ASN A  1 153 ? 68.756  50.054  6.397   1.00 31.33 ?  177  ASN A CB  1 
ATOM   1221  C  CG  . ASN A  1 153 ? 69.084  49.861  4.922   1.00 32.52 ?  177  ASN A CG  1 
ATOM   1222  O  OD1 . ASN A  1 153 ? 68.729  48.844  4.315   1.00 33.57 ?  177  ASN A OD1 1 
ATOM   1223  N  ND2 . ASN A  1 153 ? 69.761  50.847  4.334   1.00 33.26 ?  177  ASN A ND2 1 
ATOM   1224  N  N   . LYS A  1 154 ? 70.170  47.280  8.478   1.00 31.85 ?  178  LYS A N   1 
ATOM   1225  C  CA  . LYS A  1 154 ? 71.438  46.675  8.883   1.00 32.21 ?  178  LYS A CA  1 
ATOM   1226  C  C   . LYS A  1 154 ? 72.051  45.883  7.728   1.00 32.51 ?  178  LYS A C   1 
ATOM   1227  O  O   . LYS A  1 154 ? 71.360  45.112  7.056   1.00 32.41 ?  178  LYS A O   1 
ATOM   1228  C  CB  . LYS A  1 154 ? 71.256  45.785  10.115  1.00 32.23 ?  178  LYS A CB  1 
ATOM   1229  C  CG  . LYS A  1 154 ? 72.562  45.294  10.719  1.00 32.24 ?  178  LYS A CG  1 
ATOM   1230  C  CD  . LYS A  1 154 ? 72.372  44.783  12.132  1.00 32.37 ?  178  LYS A CD  1 
ATOM   1231  C  CE  . LYS A  1 154 ? 73.690  44.352  12.761  1.00 32.57 ?  178  LYS A CE  1 
ATOM   1232  N  NZ  . LYS A  1 154 ? 74.685  45.466  12.830  1.00 33.43 ?  178  LYS A NZ  1 
ATOM   1233  N  N   . LYS A  1 155 ? 73.348  46.084  7.510   1.00 32.89 ?  179  LYS A N   1 
ATOM   1234  C  CA  . LYS A  1 155 ? 74.045  45.499  6.359   1.00 33.32 ?  179  LYS A CA  1 
ATOM   1235  C  C   . LYS A  1 155 ? 74.895  44.274  6.710   1.00 33.14 ?  179  LYS A C   1 
ATOM   1236  O  O   . LYS A  1 155 ? 75.382  43.577  5.819   1.00 33.37 ?  179  LYS A O   1 
ATOM   1237  C  CB  . LYS A  1 155 ? 74.901  46.565  5.660   1.00 33.37 ?  179  LYS A CB  1 
ATOM   1238  C  CG  . LYS A  1 155 ? 74.102  47.719  5.051   1.00 34.32 ?  179  LYS A CG  1 
ATOM   1239  C  CD  . LYS A  1 155 ? 73.512  47.349  3.688   1.00 36.25 ?  179  LYS A CD  1 
ATOM   1240  C  CE  . LYS A  1 155 ? 72.372  48.284  3.282   1.00 37.18 ?  179  LYS A CE  1 
ATOM   1241  N  NZ  . LYS A  1 155 ? 72.795  49.711  3.139   1.00 37.89 ?  179  LYS A NZ  1 
ATOM   1242  N  N   . ASP A  1 156 ? 75.059  44.011  8.004   1.00 33.13 ?  180  ASP A N   1 
ATOM   1243  C  CA  . ASP A  1 156 ? 75.930  42.929  8.473   1.00 33.01 ?  180  ASP A CA  1 
ATOM   1244  C  C   . ASP A  1 156 ? 75.260  42.021  9.511   1.00 32.88 ?  180  ASP A C   1 
ATOM   1245  O  O   . ASP A  1 156 ? 74.041  42.071  9.693   1.00 32.79 ?  180  ASP A O   1 
ATOM   1246  C  CB  . ASP A  1 156 ? 77.255  43.498  9.004   1.00 33.27 ?  180  ASP A CB  1 
ATOM   1247  C  CG  . ASP A  1 156 ? 77.063  44.528  10.111  1.00 33.70 ?  180  ASP A CG  1 
ATOM   1248  O  OD1 . ASP A  1 156 ? 75.923  44.991  10.334  1.00 35.02 ?  180  ASP A OD1 1 
ATOM   1249  O  OD2 . ASP A  1 156 ? 78.066  44.881  10.763  1.00 34.38 -1 180  ASP A OD2 1 
ATOM   1250  N  N   . LYS A  1 157 ? 76.065  41.196  10.183  1.00 32.66 ?  181  LYS A N   1 
ATOM   1251  C  CA  . LYS A  1 157 ? 75.556  40.195  11.118  1.00 32.55 ?  181  LYS A CA  1 
ATOM   1252  C  C   . LYS A  1 157 ? 75.187  40.747  12.496  1.00 32.23 ?  181  LYS A C   1 
ATOM   1253  O  O   . LYS A  1 157 ? 75.744  41.751  12.955  1.00 32.10 ?  181  LYS A O   1 
ATOM   1254  C  CB  . LYS A  1 157 ? 76.535  39.015  11.257  1.00 32.79 ?  181  LYS A CB  1 
ATOM   1255  C  CG  . LYS A  1 157 ? 77.833  39.324  12.007  1.00 33.49 ?  181  LYS A CG  1 
ATOM   1256  C  CD  . LYS A  1 157 ? 78.657  38.060  12.212  1.00 35.26 ?  181  LYS A CD  1 
ATOM   1257  C  CE  . LYS A  1 157 ? 79.974  38.351  12.922  1.00 36.19 ?  181  LYS A CE  1 
ATOM   1258  N  NZ  . LYS A  1 157 ? 79.800  38.628  14.381  1.00 37.19 ?  181  LYS A NZ  1 
ATOM   1259  N  N   . ALA A  1 158 ? 74.244  40.069  13.145  1.00 31.83 ?  182  ALA A N   1 
ATOM   1260  C  CA  . ALA A  1 158 ? 73.798  40.424  14.484  1.00 31.52 ?  182  ALA A CA  1 
ATOM   1261  C  C   . ALA A  1 158 ? 74.041  39.268  15.448  1.00 31.33 ?  182  ALA A C   1 
ATOM   1262  O  O   . ALA A  1 158 ? 73.956  38.102  15.067  1.00 31.42 ?  182  ALA A O   1 
ATOM   1263  C  CB  . ALA A  1 158 ? 72.320  40.798  14.463  1.00 31.46 ?  182  ALA A CB  1 
ATOM   1264  N  N   . ASP A  1 159 ? 74.348  39.606  16.694  1.00 31.16 ?  183  ASP A N   1 
ATOM   1265  C  CA  . ASP A  1 159 ? 74.512  38.626  17.762  1.00 31.13 ?  183  ASP A CA  1 
ATOM   1266  C  C   . ASP A  1 159 ? 73.151  38.418  18.435  1.00 30.82 ?  183  ASP A C   1 
ATOM   1267  O  O   . ASP A  1 159 ? 72.678  39.298  19.152  1.00 30.80 ?  183  ASP A O   1 
ATOM   1268  C  CB  . ASP A  1 159 ? 75.554  39.145  18.767  1.00 31.17 ?  183  ASP A CB  1 
ATOM   1269  C  CG  . ASP A  1 159 ? 75.915  38.128  19.849  1.00 32.04 ?  183  ASP A CG  1 
ATOM   1270  O  OD1 . ASP A  1 159 ? 75.134  37.186  20.117  1.00 32.51 ?  183  ASP A OD1 1 
ATOM   1271  O  OD2 . ASP A  1 159 ? 77.001  38.286  20.447  1.00 32.95 -1 183  ASP A OD2 1 
ATOM   1272  N  N   . HIS A  1 160 ? 72.531  37.256  18.195  1.00 30.56 ?  184  HIS A N   1 
ATOM   1273  C  CA  . HIS A  1 160 ? 71.203  36.908  18.750  1.00 30.10 ?  184  HIS A CA  1 
ATOM   1274  C  C   . HIS A  1 160 ? 71.134  37.132  20.271  1.00 30.07 ?  184  HIS A C   1 
ATOM   1275  O  O   . HIS A  1 160 ? 70.077  37.487  20.801  1.00 29.92 ?  184  HIS A O   1 
ATOM   1276  C  CB  . HIS A  1 160 ? 70.845  35.448  18.410  1.00 29.77 ?  184  HIS A CB  1 
ATOM   1277  C  CG  . HIS A  1 160 ? 69.375  35.190  18.198  1.00 29.24 ?  184  HIS A CG  1 
ATOM   1278  N  ND1 . HIS A  1 160 ? 68.491  34.989  19.236  1.00 28.31 ?  184  HIS A ND1 1 
ATOM   1279  C  CD2 . HIS A  1 160 ? 68.651  35.044  17.060  1.00 27.84 ?  184  HIS A CD2 1 
ATOM   1280  C  CE1 . HIS A  1 160 ? 67.283  34.757  18.747  1.00 28.61 ?  184  HIS A CE1 1 
ATOM   1281  N  NE2 . HIS A  1 160 ? 67.350  34.783  17.426  1.00 27.12 ?  184  HIS A NE2 1 
ATOM   1282  N  N   . THR A  1 161 ? 72.263  36.932  20.956  1.00 29.99 ?  185  THR A N   1 
ATOM   1283  C  CA  . THR A  1 161 ? 72.346  37.061  22.418  1.00 30.16 ?  185  THR A CA  1 
ATOM   1284  C  C   . THR A  1 161 ? 72.580  38.487  22.926  1.00 30.23 ?  185  THR A C   1 
ATOM   1285  O  O   . THR A  1 161 ? 72.513  38.731  24.133  1.00 30.29 ?  185  THR A O   1 
ATOM   1286  C  CB  . THR A  1 161 ? 73.447  36.146  23.031  1.00 30.28 ?  185  THR A CB  1 
ATOM   1287  O  OG1 . THR A  1 161 ? 74.750  36.641  22.685  1.00 30.08 ?  185  THR A OG1 1 
ATOM   1288  C  CG2 . THR A  1 161 ? 73.297  34.702  22.558  1.00 30.23 ?  185  THR A CG2 1 
ATOM   1289  N  N   . LYS A  1 162 ? 72.856  39.419  22.015  1.00 30.30 ?  186  LYS A N   1 
ATOM   1290  C  CA  . LYS A  1 162 ? 73.195  40.794  22.395  1.00 30.55 ?  186  LYS A CA  1 
ATOM   1291  C  C   . LYS A  1 162 ? 72.376  41.861  21.680  1.00 30.13 ?  186  LYS A C   1 
ATOM   1292  O  O   . LYS A  1 162 ? 71.997  42.859  22.286  1.00 30.14 ?  186  LYS A O   1 
ATOM   1293  C  CB  . LYS A  1 162 ? 74.679  41.078  22.130  1.00 30.83 ?  186  LYS A CB  1 
ATOM   1294  C  CG  . LYS A  1 162 ? 75.624  40.637  23.226  1.00 32.79 ?  186  LYS A CG  1 
ATOM   1295  C  CD  . LYS A  1 162 ? 76.967  41.353  23.083  1.00 35.40 ?  186  LYS A CD  1 
ATOM   1296  C  CE  . LYS A  1 162 ? 78.024  40.753  24.002  1.00 36.68 ?  186  LYS A CE  1 
ATOM   1297  N  NZ  . LYS A  1 162 ? 78.446  39.395  23.539  1.00 38.07 ?  186  LYS A NZ  1 
ATOM   1298  N  N   . ASP A  1 163 ? 72.119  41.645  20.392  1.00 29.71 ?  187  ASP A N   1 
ATOM   1299  C  CA  . ASP A  1 163 ? 71.630  42.701  19.506  1.00 29.32 ?  187  ASP A CA  1 
ATOM   1300  C  C   . ASP A  1 163 ? 70.118  42.693  19.281  1.00 28.80 ?  187  ASP A C   1 
ATOM   1301  O  O   . ASP A  1 163 ? 69.568  43.662  18.760  1.00 28.63 ?  187  ASP A O   1 
ATOM   1302  C  CB  . ASP A  1 163 ? 72.349  42.622  18.152  1.00 29.59 ?  187  ASP A CB  1 
ATOM   1303  C  CG  . ASP A  1 163 ? 73.864  42.724  18.278  1.00 30.21 ?  187  ASP A CG  1 
ATOM   1304  O  OD1 . ASP A  1 163 ? 74.356  43.308  19.266  1.00 30.35 ?  187  ASP A OD1 1 
ATOM   1305  O  OD2 . ASP A  1 163 ? 74.567  42.216  17.374  1.00 31.46 -1 187  ASP A OD2 1 
ATOM   1306  N  N   . ILE A  1 164 ? 69.458  41.600  19.661  1.00 28.24 ?  188  ILE A N   1 
ATOM   1307  C  CA  . ILE A  1 164 ? 68.012  41.462  19.476  1.00 27.70 ?  188  ILE A CA  1 
ATOM   1308  C  C   . ILE A  1 164 ? 67.236  42.376  20.427  1.00 27.40 ?  188  ILE A C   1 
ATOM   1309  O  O   . ILE A  1 164 ? 67.505  42.421  21.630  1.00 27.07 ?  188  ILE A O   1 
ATOM   1310  C  CB  . ILE A  1 164 ? 67.539  39.989  19.652  1.00 27.68 ?  188  ILE A CB  1 
ATOM   1311  C  CG1 . ILE A  1 164 ? 68.178  39.065  18.602  1.00 27.66 ?  188  ILE A CG1 1 
ATOM   1312  C  CG2 . ILE A  1 164 ? 66.011  39.885  19.628  1.00 27.76 ?  188  ILE A CG2 1 
ATOM   1313  C  CD1 . ILE A  1 164 ? 67.752  39.309  17.172  1.00 26.83 ?  188  ILE A CD1 1 
ATOM   1314  N  N   . ARG A  1 165 ? 66.272  43.098  19.869  1.00 27.06 ?  189  ARG A N   1 
ATOM   1315  C  CA  . ARG A  1 165 ? 65.400  43.966  20.643  1.00 27.02 ?  189  ARG A CA  1 
ATOM   1316  C  C   . ARG A  1 165 ? 63.936  43.657  20.333  1.00 26.83 ?  189  ARG A C   1 
ATOM   1317  O  O   . ARG A  1 165 ? 63.623  43.055  19.294  1.00 26.80 ?  189  ARG A O   1 
ATOM   1318  C  CB  . ARG A  1 165 ? 65.698  45.435  20.318  1.00 27.13 ?  189  ARG A CB  1 
ATOM   1319  C  CG  . ARG A  1 165 ? 65.278  45.846  18.913  1.00 27.34 ?  189  ARG A CG  1 
ATOM   1320  C  CD  . ARG A  1 165 ? 65.826  47.197  18.505  1.00 28.15 ?  189  ARG A CD  1 
ATOM   1321  N  NE  . ARG A  1 165 ? 65.557  47.459  17.091  1.00 27.48 ?  189  ARG A NE  1 
ATOM   1322  C  CZ  . ARG A  1 165 ? 65.945  48.552  16.442  1.00 27.50 ?  189  ARG A CZ  1 
ATOM   1323  N  NH1 . ARG A  1 165 ? 66.627  49.499  17.078  1.00 26.86 ?  189  ARG A NH1 1 
ATOM   1324  N  NH2 . ARG A  1 165 ? 65.655  48.694  15.155  1.00 26.53 ?  189  ARG A NH2 1 
ATOM   1325  N  N   . MET A  1 166 ? 63.049  44.062  21.238  1.00 26.44 ?  190  MET A N   1 
ATOM   1326  C  CA  . MET A  1 166 ? 61.627  44.125  20.932  1.00 26.09 ?  190  MET A CA  1 
ATOM   1327  C  C   . MET A  1 166 ? 61.351  45.514  20.385  1.00 25.98 ?  190  MET A C   1 
ATOM   1328  O  O   . MET A  1 166 ? 61.678  46.504  21.037  1.00 25.96 ?  190  MET A O   1 
ATOM   1329  C  CB  . MET A  1 166 ? 60.768  43.857  22.170  1.00 26.06 ?  190  MET A CB  1 
ATOM   1330  C  CG  . MET A  1 166 ? 60.761  42.417  22.657  1.00 25.53 ?  190  MET A CG  1 
ATOM   1331  S  SD  . MET A  1 166 ? 60.221  41.227  21.416  1.00 25.53 ?  190  MET A SD  1 
ATOM   1332  C  CE  . MET A  1 166 ? 61.755  40.392  21.034  1.00 24.57 ?  190  MET A CE  1 
ATOM   1333  N  N   . PRO A  1 167 ? 60.771  45.596  19.171  1.00 25.95 ?  191  PRO A N   1 
ATOM   1334  C  CA  . PRO A  1 167 ? 60.544  46.893  18.541  1.00 25.82 ?  191  PRO A CA  1 
ATOM   1335  C  C   . PRO A  1 167 ? 59.517  47.711  19.305  1.00 25.78 ?  191  PRO A C   1 
ATOM   1336  O  O   . PRO A  1 167 ? 58.391  47.252  19.531  1.00 26.01 ?  191  PRO A O   1 
ATOM   1337  C  CB  . PRO A  1 167 ? 60.027  46.525  17.141  1.00 25.74 ?  191  PRO A CB  1 
ATOM   1338  C  CG  . PRO A  1 167 ? 60.452  45.111  16.938  1.00 25.92 ?  191  PRO A CG  1 
ATOM   1339  C  CD  . PRO A  1 167 ? 60.349  44.493  18.293  1.00 25.73 ?  191  PRO A CD  1 
ATOM   1340  N  N   . THR A  1 168 ? 59.924  48.910  19.710  1.00 25.69 ?  192  THR A N   1 
ATOM   1341  C  CA  . THR A  1 168 ? 59.064  49.818  20.460  1.00 25.54 ?  192  THR A CA  1 
ATOM   1342  C  C   . THR A  1 168 ? 58.591  50.964  19.556  1.00 25.57 ?  192  THR A C   1 
ATOM   1343  O  O   . THR A  1 168 ? 58.899  50.973  18.362  1.00 25.49 ?  192  THR A O   1 
ATOM   1344  C  CB  . THR A  1 168 ? 59.774  50.344  21.734  1.00 25.41 ?  192  THR A CB  1 
ATOM   1345  O  OG1 . THR A  1 168 ? 61.095  50.783  21.405  1.00 25.51 ?  192  THR A OG1 1 
ATOM   1346  C  CG2 . THR A  1 168 ? 59.871  49.244  22.782  1.00 25.11 ?  192  THR A CG2 1 
ATOM   1347  N  N   . ALA A  1 169 ? 57.834  51.912  20.113  1.00 25.50 ?  193  ALA A N   1 
ATOM   1348  C  CA  . ALA A  1 169 ? 57.242  53.000  19.317  1.00 25.74 ?  193  ALA A CA  1 
ATOM   1349  C  C   . ALA A  1 169 ? 58.281  53.815  18.548  1.00 25.82 ?  193  ALA A C   1 
ATOM   1350  O  O   . ALA A  1 169 ? 58.046  54.200  17.401  1.00 25.85 ?  193  ALA A O   1 
ATOM   1351  C  CB  . ALA A  1 169 ? 56.381  53.910  20.182  1.00 25.53 ?  193  ALA A CB  1 
ATOM   1352  N  N   . ASP A  1 170 ? 59.425  54.065  19.182  1.00 25.88 ?  194  ASP A N   1 
ATOM   1353  C  CA  . ASP A  1 170 ? 60.528  54.797  18.553  1.00 25.95 ?  194  ASP A CA  1 
ATOM   1354  C  C   . ASP A  1 170 ? 61.177  54.004  17.419  1.00 25.66 ?  194  ASP A C   1 
ATOM   1355  O  O   . ASP A  1 170 ? 61.694  54.595  16.470  1.00 25.72 ?  194  ASP A O   1 
ATOM   1356  C  CB  . ASP A  1 170 ? 61.586  55.188  19.591  1.00 26.12 ?  194  ASP A CB  1 
ATOM   1357  C  CG  . ASP A  1 170 ? 62.050  54.008  20.427  1.00 26.77 ?  194  ASP A CG  1 
ATOM   1358  O  OD1 . ASP A  1 170 ? 61.199  53.361  21.072  1.00 27.35 ?  194  ASP A OD1 1 
ATOM   1359  O  OD2 . ASP A  1 170 ? 63.266  53.728  20.445  1.00 28.65 -1 194  ASP A OD2 1 
ATOM   1360  N  N   . THR A  1 171 ? 61.151  52.673  17.527  1.00 25.33 ?  195  THR A N   1 
ATOM   1361  C  CA  . THR A  1 171 ? 61.673  51.797  16.478  1.00 25.08 ?  195  THR A CA  1 
ATOM   1362  C  C   . THR A  1 171 ? 60.854  51.958  15.202  1.00 24.92 ?  195  THR A C   1 
ATOM   1363  O  O   . THR A  1 171 ? 61.406  52.252  14.142  1.00 25.03 ?  195  THR A O   1 
ATOM   1364  C  CB  . THR A  1 171 ? 61.670  50.308  16.898  1.00 25.23 ?  195  THR A CB  1 
ATOM   1365  O  OG1 . THR A  1 171 ? 62.283  50.160  18.187  1.00 25.36 ?  195  THR A OG1 1 
ATOM   1366  C  CG2 . THR A  1 171 ? 62.419  49.463  15.871  1.00 25.01 ?  195  THR A CG2 1 
ATOM   1367  N  N   . CYS A  1 172 ? 59.540  51.758  15.317  1.00 24.71 ?  196  CYS A N   1 
ATOM   1368  C  CA  . CYS A  1 172 ? 58.607  51.983  14.212  1.00 24.45 ?  196  CYS A CA  1 
ATOM   1369  C  C   . CYS A  1 172 ? 58.725  53.423  13.713  1.00 24.61 ?  196  CYS A C   1 
ATOM   1370  O  O   . CYS A  1 172 ? 58.708  53.674  12.506  1.00 24.32 ?  196  CYS A O   1 
ATOM   1371  C  CB  . CYS A  1 172 ? 57.164  51.715  14.657  1.00 24.18 ?  196  CYS A CB  1 
ATOM   1372  S  SG  . CYS A  1 172 ? 56.858  50.103  15.422  1.00 23.10 ?  196  CYS A SG  1 
ATOM   1373  N  N   . GLY A  1 173 ? 58.862  54.349  14.663  1.00 24.74 ?  197  GLY A N   1 
ATOM   1374  C  CA  . GLY A  1 173 ? 58.922  55.782  14.391  1.00 25.25 ?  197  GLY A CA  1 
ATOM   1375  C  C   . GLY A  1 173 ? 60.150  56.260  13.634  1.00 25.59 ?  197  GLY A C   1 
ATOM   1376  O  O   . GLY A  1 173 ? 60.151  57.371  13.100  1.00 25.49 ?  197  GLY A O   1 
ATOM   1377  N  N   . THR A  1 174 ? 61.191  55.427  13.592  1.00 25.78 ?  198  THR A N   1 
ATOM   1378  C  CA  . THR A  1 174 ? 62.388  55.704  12.793  1.00 26.14 ?  198  THR A CA  1 
ATOM   1379  C  C   . THR A  1 174 ? 61.984  55.885  11.331  1.00 26.28 ?  198  THR A C   1 
ATOM   1380  O  O   . THR A  1 174 ? 62.420  56.827  10.669  1.00 26.71 ?  198  THR A O   1 
ATOM   1381  C  CB  . THR A  1 174 ? 63.437  54.566  12.923  1.00 26.24 ?  198  THR A CB  1 
ATOM   1382  O  OG1 . THR A  1 174 ? 63.640  54.252  14.307  1.00 26.33 ?  198  THR A OG1 1 
ATOM   1383  C  CG2 . THR A  1 174 ? 64.764  54.969  12.311  1.00 26.37 ?  198  THR A CG2 1 
ATOM   1384  N  N   . CYS A  1 175 ? 61.132  54.987  10.847  1.00 26.06 ?  199  CYS A N   1 
ATOM   1385  C  CA  . CYS A  1 175 ? 60.590  55.066  9.498   1.00 25.73 ?  199  CYS A CA  1 
ATOM   1386  C  C   . CYS A  1 175 ? 59.283  55.851  9.455   1.00 25.71 ?  199  CYS A C   1 
ATOM   1387  O  O   . CYS A  1 175 ? 59.143  56.801  8.679   1.00 25.71 ?  199  CYS A O   1 
ATOM   1388  C  CB  . CYS A  1 175 ? 60.354  53.663  8.958   1.00 25.79 ?  199  CYS A CB  1 
ATOM   1389  S  SG  . CYS A  1 175 ? 61.865  52.725  8.704   1.00 25.05 ?  199  CYS A SG  1 
ATOM   1390  N  N   . HIS A  1 176 ? 58.336  55.446  10.300  1.00 25.41 ?  200  HIS A N   1 
ATOM   1391  C  CA  . HIS A  1 176 ? 56.999  56.029  10.323  1.00 25.03 ?  200  HIS A CA  1 
ATOM   1392  C  C   . HIS A  1 176 ? 56.946  57.253  11.245  1.00 25.04 ?  200  HIS A C   1 
ATOM   1393  O  O   . HIS A  1 176 ? 56.215  57.276  12.248  1.00 24.94 ?  200  HIS A O   1 
ATOM   1394  C  CB  . HIS A  1 176 ? 55.957  54.966  10.720  1.00 24.86 ?  200  HIS A CB  1 
ATOM   1395  C  CG  . HIS A  1 176 ? 55.917  53.775  9.805   1.00 24.19 ?  200  HIS A CG  1 
ATOM   1396  N  ND1 . HIS A  1 176 ? 55.739  53.885  8.441   1.00 23.85 ?  200  HIS A ND1 1 
ATOM   1397  C  CD2 . HIS A  1 176 ? 56.002  52.446  10.063  1.00 24.08 ?  200  HIS A CD2 1 
ATOM   1398  C  CE1 . HIS A  1 176 ? 55.726  52.679  7.899   1.00 23.31 ?  200  HIS A CE1 1 
ATOM   1399  N  NE2 . HIS A  1 176 ? 55.879  51.785  8.861   1.00 23.61 ?  200  HIS A NE2 1 
ATOM   1400  N  N   . LEU A  1 177 ? 57.725  58.274  10.886  1.00 24.83 ?  201  LEU A N   1 
ATOM   1401  C  CA  . LEU A  1 177 ? 57.873  59.477  11.704  1.00 24.67 ?  201  LEU A CA  1 
ATOM   1402  C  C   . LEU A  1 177 ? 56.542  60.209  11.881  1.00 24.45 ?  201  LEU A C   1 
ATOM   1403  O  O   . LEU A  1 177 ? 56.210  60.641  12.985  1.00 24.13 ?  201  LEU A O   1 
ATOM   1404  C  CB  . LEU A  1 177 ? 58.915  60.427  11.095  1.00 24.58 ?  201  LEU A CB  1 
ATOM   1405  C  CG  . LEU A  1 177 ? 59.837  61.247  12.020  1.00 25.11 ?  201  LEU A CG  1 
ATOM   1406  C  CD1 . LEU A  1 177 ? 60.256  62.554  11.344  1.00 24.04 ?  201  LEU A CD1 1 
ATOM   1407  C  CD2 . LEU A  1 177 ? 59.252  61.536  13.396  1.00 24.31 ?  201  LEU A CD2 1 
ATOM   1408  N  N   . ARG A  1 178 ? 55.793  60.338  10.788  1.00 24.37 ?  202  ARG A N   1 
ATOM   1409  C  CA  . ARG A  1 178 ? 54.497  61.016  10.799  1.00 24.44 ?  202  ARG A CA  1 
ATOM   1410  C  C   . ARG A  1 178 ? 53.553  60.419  11.847  1.00 24.20 ?  202  ARG A C   1 
ATOM   1411  O  O   . ARG A  1 178 ? 53.065  61.130  12.725  1.00 24.20 ?  202  ARG A O   1 
ATOM   1412  C  CB  . ARG A  1 178 ? 53.859  60.957  9.407   1.00 24.57 ?  202  ARG A CB  1 
ATOM   1413  C  CG  . ARG A  1 178 ? 52.485  61.614  9.317   1.00 25.25 ?  202  ARG A CG  1 
ATOM   1414  C  CD  . ARG A  1 178 ? 51.914  61.525  7.908   1.00 26.45 ?  202  ARG A CD  1 
ATOM   1415  N  NE  . ARG A  1 178 ? 52.745  62.219  6.924   1.00 27.31 ?  202  ARG A NE  1 
ATOM   1416  C  CZ  . ARG A  1 178 ? 52.649  63.513  6.627   1.00 27.55 ?  202  ARG A CZ  1 
ATOM   1417  N  NH1 . ARG A  1 178 ? 51.755  64.285  7.236   1.00 27.33 ?  202  ARG A NH1 1 
ATOM   1418  N  NH2 . ARG A  1 178 ? 53.452  64.034  5.711   1.00 28.08 ?  202  ARG A NH2 1 
ATOM   1419  N  N   . GLU A  1 179 ? 53.316  59.113  11.748  1.00 24.11 ?  203  GLU A N   1 
ATOM   1420  C  CA  . GLU A  1 179 ? 52.404  58.408  12.653  1.00 24.12 ?  203  GLU A CA  1 
ATOM   1421  C  C   . GLU A  1 179 ? 52.858  58.467  14.114  1.00 23.96 ?  203  GLU A C   1 
ATOM   1422  O  O   . GLU A  1 179 ? 52.046  58.694  15.008  1.00 23.85 ?  203  GLU A O   1 
ATOM   1423  C  CB  . GLU A  1 179 ? 52.216  56.958  12.200  1.00 24.07 ?  203  GLU A CB  1 
ATOM   1424  C  CG  . GLU A  1 179 ? 51.427  56.807  10.893  1.00 24.51 ?  203  GLU A CG  1 
ATOM   1425  C  CD  . GLU A  1 179 ? 52.270  56.992  9.625   1.00 25.58 ?  203  GLU A CD  1 
ATOM   1426  O  OE1 . GLU A  1 179 ? 53.506  57.179  9.714   1.00 24.65 ?  203  GLU A OE1 1 
ATOM   1427  O  OE2 . GLU A  1 179 ? 51.681  56.940  8.523   1.00 26.54 -1 203  GLU A OE2 1 
ATOM   1428  N  N   . PHE A  1 180 ? 54.160  58.282  14.334  1.00 23.91 ?  204  PHE A N   1 
ATOM   1429  C  CA  . PHE A  1 180 ? 54.769  58.365  15.663  1.00 23.89 ?  204  PHE A CA  1 
ATOM   1430  C  C   . PHE A  1 180 ? 54.612  59.768  16.259  1.00 23.79 ?  204  PHE A C   1 
ATOM   1431  O  O   . PHE A  1 180 ? 54.229  59.914  17.422  1.00 23.55 ?  204  PHE A O   1 
ATOM   1432  C  CB  . PHE A  1 180 ? 56.246  57.960  15.577  1.00 23.74 ?  204  PHE A CB  1 
ATOM   1433  C  CG  . PHE A  1 180 ? 57.006  58.082  16.871  1.00 24.32 ?  204  PHE A CG  1 
ATOM   1434  C  CD1 . PHE A  1 180 ? 56.569  57.436  18.030  1.00 24.34 ?  204  PHE A CD1 1 
ATOM   1435  C  CD2 . PHE A  1 180 ? 58.195  58.806  16.919  1.00 24.78 ?  204  PHE A CD2 1 
ATOM   1436  C  CE1 . PHE A  1 180 ? 57.289  57.538  19.224  1.00 25.21 ?  204  PHE A CE1 1 
ATOM   1437  C  CE2 . PHE A  1 180 ? 58.924  58.913  18.108  1.00 25.33 ?  204  PHE A CE2 1 
ATOM   1438  C  CZ  . PHE A  1 180 ? 58.467  58.280  19.265  1.00 24.93 ?  204  PHE A CZ  1 
ATOM   1439  N  N   . ALA A  1 181 ? 54.902  60.786  15.448  1.00 23.77 ?  205  ALA A N   1 
ATOM   1440  C  CA  . ALA A  1 181 ? 54.737  62.186  15.842  1.00 23.82 ?  205  ALA A CA  1 
ATOM   1441  C  C   . ALA A  1 181 ? 53.278  62.537  16.121  1.00 23.81 ?  205  ALA A C   1 
ATOM   1442  O  O   . ALA A  1 181 ? 52.992  63.255  17.075  1.00 23.95 ?  205  ALA A O   1 
ATOM   1443  C  CB  . ALA A  1 181 ? 55.312  63.113  14.778  1.00 23.79 ?  205  ALA A CB  1 
ATOM   1444  N  N   . GLU A  1 182 ? 52.367  62.039  15.285  1.00 23.87 ?  206  GLU A N   1 
ATOM   1445  C  CA  . GLU A  1 182 ? 50.929  62.243  15.490  1.00 24.05 ?  206  GLU A CA  1 
ATOM   1446  C  C   . GLU A  1 182 ? 50.509  61.650  16.826  1.00 24.03 ?  206  GLU A C   1 
ATOM   1447  O  O   . GLU A  1 182 ? 49.800  62.288  17.599  1.00 23.97 ?  206  GLU A O   1 
ATOM   1448  C  CB  . GLU A  1 182 ? 50.108  61.593  14.371  1.00 23.95 ?  206  GLU A CB  1 
ATOM   1449  C  CG  . GLU A  1 182 ? 50.103  62.346  13.055  1.00 24.05 ?  206  GLU A CG  1 
ATOM   1450  C  CD  . GLU A  1 182 ? 49.507  61.534  11.914  1.00 24.40 ?  206  GLU A CD  1 
ATOM   1451  O  OE1 . GLU A  1 182 ? 49.093  60.377  12.139  1.00 24.18 ?  206  GLU A OE1 1 
ATOM   1452  O  OE2 . GLU A  1 182 ? 49.453  62.054  10.781  1.00 25.43 -1 206  GLU A OE2 1 
ATOM   1453  N  N   . ARG A  1 183 ? 50.958  60.423  17.080  1.00 24.08 ?  207  ARG A N   1 
ATOM   1454  C  CA  . ARG A  1 183 ? 50.664  59.717  18.320  1.00 24.29 ?  207  ARG A CA  1 
ATOM   1455  C  C   . ARG A  1 183 ? 51.201  60.498  19.512  1.00 24.37 ?  207  ARG A C   1 
ATOM   1456  O  O   . ARG A  1 183 ? 50.471  60.749  20.473  1.00 24.63 ?  207  ARG A O   1 
ATOM   1457  C  CB  . ARG A  1 183 ? 51.266  58.305  18.285  1.00 24.26 ?  207  ARG A CB  1 
ATOM   1458  C  CG  . ARG A  1 183 ? 50.571  57.280  19.176  1.00 24.27 ?  207  ARG A CG  1 
ATOM   1459  C  CD  . ARG A  1 183 ? 50.822  57.488  20.673  1.00 24.47 ?  207  ARG A CD  1 
ATOM   1460  N  NE  . ARG A  1 183 ? 52.228  57.354  21.064  1.00 24.76 ?  207  ARG A NE  1 
ATOM   1461  C  CZ  . ARG A  1 183 ? 52.843  56.196  21.297  1.00 24.83 ?  207  ARG A CZ  1 
ATOM   1462  N  NH1 . ARG A  1 183 ? 52.190  55.048  21.167  1.00 25.32 ?  207  ARG A NH1 1 
ATOM   1463  N  NH2 . ARG A  1 183 ? 54.121  56.179  21.653  1.00 24.32 ?  207  ARG A NH2 1 
ATOM   1464  N  N   . GLU A  1 184 ? 52.470  60.895  19.439  1.00 24.22 ?  208  GLU A N   1 
ATOM   1465  C  CA  . GLU A  1 184 ? 53.114  61.618  20.535  1.00 24.13 ?  208  GLU A CA  1 
ATOM   1466  C  C   . GLU A  1 184 ? 52.495  62.987  20.794  1.00 24.12 ?  208  GLU A C   1 
ATOM   1467  O  O   . GLU A  1 184 ? 52.560  63.494  21.919  1.00 23.98 ?  208  GLU A O   1 
ATOM   1468  C  CB  . GLU A  1 184 ? 54.624  61.746  20.291  1.00 24.23 ?  208  GLU A CB  1 
ATOM   1469  C  CG  . GLU A  1 184 ? 55.406  60.467  20.558  1.00 24.03 ?  208  GLU A CG  1 
ATOM   1470  C  CD  . GLU A  1 184 ? 55.253  59.977  21.987  1.00 24.68 ?  208  GLU A CD  1 
ATOM   1471  O  OE1 . GLU A  1 184 ? 55.848  60.586  22.902  1.00 24.89 ?  208  GLU A OE1 1 
ATOM   1472  O  OE2 . GLU A  1 184 ? 54.540  58.977  22.197  1.00 25.26 -1 208  GLU A OE2 1 
ATOM   1473  N  N   . SER A  1 185 ? 51.877  63.569  19.762  1.00 23.89 ?  209  SER A N   1 
ATOM   1474  C  CA  . SER A  1 185 ? 51.248  64.892  19.865  1.00 23.98 ?  209  SER A CA  1 
ATOM   1475  C  C   . SER A  1 185 ? 50.072  64.932  20.845  1.00 24.17 ?  209  SER A C   1 
ATOM   1476  O  O   . SER A  1 185 ? 49.672  66.008  21.300  1.00 24.24 ?  209  SER A O   1 
ATOM   1477  C  CB  . SER A  1 185 ? 50.819  65.407  18.488  1.00 23.82 ?  209  SER A CB  1 
ATOM   1478  O  OG  . SER A  1 185 ? 49.658  64.756  18.012  1.00 23.66 ?  209  SER A OG  1 
ATOM   1479  N  N   . GLU A  1 186 ? 49.531  63.758  21.166  1.00 24.34 ?  210  GLU A N   1 
ATOM   1480  C  CA  . GLU A  1 186 ? 48.505  63.617  22.202  1.00 24.68 ?  210  GLU A CA  1 
ATOM   1481  C  C   . GLU A  1 186 ? 48.967  64.209  23.535  1.00 24.87 ?  210  GLU A C   1 
ATOM   1482  O  O   . GLU A  1 186 ? 48.159  64.765  24.284  1.00 24.83 ?  210  GLU A O   1 
ATOM   1483  C  CB  . GLU A  1 186 ? 48.112  62.146  22.382  1.00 24.59 ?  210  GLU A CB  1 
ATOM   1484  C  CG  . GLU A  1 186 ? 47.423  61.526  21.161  1.00 24.57 ?  210  GLU A CG  1 
ATOM   1485  C  CD  . GLU A  1 186 ? 47.097  60.046  21.335  1.00 24.92 ?  210  GLU A CD  1 
ATOM   1486  O  OE1 . GLU A  1 186 ? 47.628  59.405  22.269  1.00 25.29 ?  210  GLU A OE1 1 
ATOM   1487  O  OE2 . GLU A  1 186 ? 46.305  59.520  20.527  1.00 24.37 -1 210  GLU A OE2 1 
ATOM   1488  N  N   . ARG A  1 187 ? 50.267  64.091  23.816  1.00 25.27 ?  211  ARG A N   1 
ATOM   1489  C  CA  . ARG A  1 187 ? 50.879  64.710  24.999  1.00 25.57 ?  211  ARG A CA  1 
ATOM   1490  C  C   . ARG A  1 187 ? 50.587  66.205  25.056  1.00 25.98 ?  211  ARG A C   1 
ATOM   1491  O  O   . ARG A  1 187 ? 50.348  66.754  26.131  1.00 26.15 ?  211  ARG A O   1 
ATOM   1492  C  CB  . ARG A  1 187 ? 52.397  64.518  24.994  1.00 25.39 ?  211  ARG A CB  1 
ATOM   1493  C  CG  . ARG A  1 187 ? 52.885  63.103  25.260  1.00 25.03 ?  211  ARG A CG  1 
ATOM   1494  C  CD  . ARG A  1 187 ? 54.379  63.002  24.979  1.00 23.63 ?  211  ARG A CD  1 
ATOM   1495  N  NE  . ARG A  1 187 ? 54.911  61.671  25.259  1.00 23.60 ?  211  ARG A NE  1 
ATOM   1496  C  CZ  . ARG A  1 187 ? 55.401  61.291  26.435  1.00 23.23 ?  211  ARG A CZ  1 
ATOM   1497  N  NH1 . ARG A  1 187 ? 55.431  62.139  27.456  1.00 22.05 ?  211  ARG A NH1 1 
ATOM   1498  N  NH2 . ARG A  1 187 ? 55.859  60.056  26.590  1.00 23.62 ?  211  ARG A NH2 1 
ATOM   1499  N  N   . ASP A  1 188 ? 50.602  66.843  23.886  1.00 26.38 ?  212  ASP A N   1 
ATOM   1500  C  CA  . ASP A  1 188 ? 50.533  68.298  23.769  1.00 26.85 ?  212  ASP A CA  1 
ATOM   1501  C  C   . ASP A  1 188 ? 49.127  68.842  23.493  1.00 27.15 ?  212  ASP A C   1 
ATOM   1502  O  O   . ASP A  1 188 ? 48.852  70.006  23.788  1.00 27.29 ?  212  ASP A O   1 
ATOM   1503  C  CB  . ASP A  1 188 ? 51.503  68.784  22.680  1.00 26.88 ?  212  ASP A CB  1 
ATOM   1504  C  CG  . ASP A  1 188 ? 52.879  68.135  22.788  1.00 27.20 ?  212  ASP A CG  1 
ATOM   1505  O  OD1 . ASP A  1 188 ? 53.538  68.300  23.836  1.00 27.23 ?  212  ASP A OD1 1 
ATOM   1506  O  OD2 . ASP A  1 188 ? 53.301  67.461  21.823  1.00 27.03 -1 212  ASP A OD2 1 
ATOM   1507  N  N   . THR A  1 189 ? 48.247  68.015  22.923  1.00 27.42 ?  213  THR A N   1 
ATOM   1508  C  CA  . THR A  1 189 ? 46.883  68.456  22.585  1.00 27.69 ?  213  THR A CA  1 
ATOM   1509  C  C   . THR A  1 189 ? 45.844  68.153  23.664  1.00 28.00 ?  213  THR A C   1 
ATOM   1510  O  O   . THR A  1 189 ? 44.848  68.870  23.778  1.00 28.19 ?  213  THR A O   1 
ATOM   1511  C  CB  . THR A  1 189 ? 46.379  67.883  21.236  1.00 27.62 ?  213  THR A CB  1 
ATOM   1512  O  OG1 . THR A  1 189 ? 46.320  66.454  21.308  1.00 27.72 ?  213  THR A OG1 1 
ATOM   1513  C  CG2 . THR A  1 189 ? 47.290  68.300  20.089  1.00 27.37 ?  213  THR A CG2 1 
ATOM   1514  N  N   . MET A  1 190 ? 46.065  67.093  24.443  1.00 28.14 ?  214  MET A N   1 
ATOM   1515  C  CA  . MET A  1 190 ? 45.120  66.716  25.499  1.00 28.35 ?  214  MET A CA  1 
ATOM   1516  C  C   . MET A  1 190 ? 45.420  67.448  26.802  1.00 28.55 ?  214  MET A C   1 
ATOM   1517  O  O   . MET A  1 190 ? 45.823  66.848  27.804  1.00 28.47 ?  214  MET A O   1 
ATOM   1518  C  CB  . MET A  1 190 ? 45.072  65.193  25.707  1.00 28.34 ?  214  MET A CB  1 
ATOM   1519  C  CG  . MET A  1 190 ? 43.929  64.702  26.608  1.00 28.17 ?  214  MET A CG  1 
ATOM   1520  S  SD  . MET A  1 190 ? 42.263  65.039  25.989  1.00 29.09 ?  214  MET A SD  1 
ATOM   1521  C  CE  . MET A  1 190 ? 41.941  66.691  26.613  1.00 27.45 ?  214  MET A CE  1 
ATOM   1522  N  N   . VAL A  1 191 ? 45.218  68.761  26.768  1.00 28.84 ?  215  VAL A N   1 
ATOM   1523  C  CA  . VAL A  1 191 ? 45.414  69.605  27.933  1.00 29.12 ?  215  VAL A CA  1 
ATOM   1524  C  C   . VAL A  1 191 ? 44.049  70.108  28.379  1.00 29.19 ?  215  VAL A C   1 
ATOM   1525  O  O   . VAL A  1 191 ? 43.357  70.805  27.631  1.00 29.04 ?  215  VAL A O   1 
ATOM   1526  C  CB  . VAL A  1 191 ? 46.383  70.785  27.639  1.00 29.27 ?  215  VAL A CB  1 
ATOM   1527  C  CG1 . VAL A  1 191 ? 46.534  71.682  28.867  1.00 29.45 ?  215  VAL A CG1 1 
ATOM   1528  C  CG2 . VAL A  1 191 ? 47.745  70.260  27.201  1.00 29.26 ?  215  VAL A CG2 1 
ATOM   1529  N  N   . TRP A  1 192 ? 43.662  69.723  29.593  1.00 29.32 ?  216  TRP A N   1 
ATOM   1530  C  CA  . TRP A  1 192 ? 42.375  70.104  30.154  1.00 29.55 ?  216  TRP A CA  1 
ATOM   1531  C  C   . TRP A  1 192 ? 42.447  71.525  30.716  1.00 29.67 ?  216  TRP A C   1 
ATOM   1532  O  O   . TRP A  1 192 ? 43.455  71.898  31.315  1.00 29.78 ?  216  TRP A O   1 
ATOM   1533  C  CB  . TRP A  1 192 ? 41.932  69.092  31.218  1.00 29.53 ?  216  TRP A CB  1 
ATOM   1534  C  CG  . TRP A  1 192 ? 41.626  67.738  30.630  1.00 29.87 ?  216  TRP A CG  1 
ATOM   1535  C  CD1 . TRP A  1 192 ? 42.502  66.706  30.455  1.00 30.05 ?  216  TRP A CD1 1 
ATOM   1536  C  CD2 . TRP A  1 192 ? 40.363  67.284  30.123  1.00 29.47 ?  216  TRP A CD2 1 
ATOM   1537  N  NE1 . TRP A  1 192 ? 41.864  65.635  29.875  1.00 30.16 ?  216  TRP A NE1 1 
ATOM   1538  C  CE2 . TRP A  1 192 ? 40.551  65.962  29.661  1.00 29.87 ?  216  TRP A CE2 1 
ATOM   1539  C  CE3 . TRP A  1 192 ? 39.092  67.863  30.017  1.00 29.32 ?  216  TRP A CE3 1 
ATOM   1540  C  CZ2 . TRP A  1 192 ? 39.513  65.207  29.097  1.00 29.94 ?  216  TRP A CZ2 1 
ATOM   1541  C  CZ3 . TRP A  1 192 ? 38.061  67.115  29.455  1.00 29.60 ?  216  TRP A CZ3 1 
ATOM   1542  C  CH2 . TRP A  1 192 ? 38.279  65.799  29.005  1.00 29.43 ?  216  TRP A CH2 1 
ATOM   1543  N  N   . PRO A  1 193 ? 41.378  72.323  30.521  1.00 29.76 ?  217  PRO A N   1 
ATOM   1544  C  CA  . PRO A  1 193 ? 41.403  73.737  30.917  1.00 29.85 ?  217  PRO A CA  1 
ATOM   1545  C  C   . PRO A  1 193 ? 41.612  73.956  32.415  1.00 29.87 ?  217  PRO A C   1 
ATOM   1546  O  O   . PRO A  1 193 ? 42.151  74.993  32.808  1.00 30.17 ?  217  PRO A O   1 
ATOM   1547  C  CB  . PRO A  1 193 ? 40.016  74.249  30.500  1.00 29.81 ?  217  PRO A CB  1 
ATOM   1548  C  CG  . PRO A  1 193 ? 39.512  73.262  29.510  1.00 29.83 ?  217  PRO A CG  1 
ATOM   1549  C  CD  . PRO A  1 193 ? 40.083  71.947  29.924  1.00 29.72 ?  217  PRO A CD  1 
ATOM   1550  N  N   . ASN A  1 194 ? 41.197  72.987  33.232  1.00 29.74 ?  218  ASN A N   1 
ATOM   1551  C  CA  . ASN A  1 194 ? 41.270  73.098  34.693  1.00 29.45 ?  218  ASN A CA  1 
ATOM   1552  C  C   . ASN A  1 194 ? 41.954  71.902  35.363  1.00 29.29 ?  218  ASN A C   1 
ATOM   1553  O  O   . ASN A  1 194 ? 41.755  71.646  36.556  1.00 29.21 ?  218  ASN A O   1 
ATOM   1554  C  CB  . ASN A  1 194 ? 39.865  73.290  35.276  1.00 29.46 ?  218  ASN A CB  1 
ATOM   1555  C  CG  . ASN A  1 194 ? 39.055  74.317  34.513  1.00 29.79 ?  218  ASN A CG  1 
ATOM   1556  O  OD1 . ASN A  1 194 ? 38.222  73.966  33.674  1.00 29.96 ?  218  ASN A OD1 1 
ATOM   1557  N  ND2 . ASN A  1 194 ? 39.311  75.594  34.778  1.00 29.86 ?  218  ASN A ND2 1 
ATOM   1558  N  N   . GLY A  1 195 ? 42.758  71.175  34.589  1.00 29.12 ?  219  GLY A N   1 
ATOM   1559  C  CA  . GLY A  1 195 ? 43.477  70.002  35.087  1.00 29.00 ?  219  GLY A CA  1 
ATOM   1560  C  C   . GLY A  1 195 ? 42.581  68.860  35.542  1.00 28.99 ?  219  GLY A C   1 
ATOM   1561  O  O   . GLY A  1 195 ? 42.921  68.136  36.484  1.00 28.89 ?  219  GLY A O   1 
ATOM   1562  N  N   . GLN A  1 196 ? 41.436  68.707  34.875  1.00 28.76 ?  220  GLN A N   1 
ATOM   1563  C  CA  . GLN A  1 196 ? 40.500  67.609  35.134  1.00 28.62 ?  220  GLN A CA  1 
ATOM   1564  C  C   . GLN A  1 196 ? 41.226  66.261  35.131  1.00 28.43 ?  220  GLN A C   1 
ATOM   1565  O  O   . GLN A  1 196 ? 41.017  65.428  36.011  1.00 28.31 ?  220  GLN A O   1 
ATOM   1566  C  CB  . GLN A  1 196 ? 39.369  67.612  34.095  1.00 28.67 ?  220  GLN A CB  1 
ATOM   1567  C  CG  . GLN A  1 196 ? 38.299  68.698  34.298  1.00 28.74 ?  220  GLN A CG  1 
ATOM   1568  C  CD  . GLN A  1 196 ? 38.700  70.082  33.770  1.00 29.73 ?  220  GLN A CD  1 
ATOM   1569  O  OE1 . GLN A  1 196 ? 39.862  70.335  33.447  1.00 29.35 ?  220  GLN A OE1 1 
ATOM   1570  N  NE2 . GLN A  1 196 ? 37.725  70.983  33.688  1.00 30.16 ?  220  GLN A NE2 1 
ATOM   1571  N  N   . TRP A  1 197 ? 42.082  66.070  34.130  1.00 28.22 ?  221  TRP A N   1 
ATOM   1572  C  CA  . TRP A  1 197 ? 42.990  64.937  34.061  1.00 28.08 ?  221  TRP A CA  1 
ATOM   1573  C  C   . TRP A  1 197 ? 44.407  65.489  33.920  1.00 28.15 ?  221  TRP A C   1 
ATOM   1574  O  O   . TRP A  1 197 ? 44.575  66.634  33.483  1.00 28.28 ?  221  TRP A O   1 
ATOM   1575  C  CB  . TRP A  1 197 ? 42.679  64.086  32.831  1.00 28.11 ?  221  TRP A CB  1 
ATOM   1576  C  CG  . TRP A  1 197 ? 41.357  63.394  32.833  1.00 27.98 ?  221  TRP A CG  1 
ATOM   1577  C  CD1 . TRP A  1 197 ? 40.165  63.896  32.392  1.00 28.12 ?  221  TRP A CD1 1 
ATOM   1578  C  CD2 . TRP A  1 197 ? 41.095  62.054  33.261  1.00 28.07 ?  221  TRP A CD2 1 
ATOM   1579  N  NE1 . TRP A  1 197 ? 39.173  62.955  32.531  1.00 27.80 ?  221  TRP A NE1 1 
ATOM   1580  C  CE2 . TRP A  1 197 ? 39.716  61.814  33.063  1.00 27.82 ?  221  TRP A CE2 1 
ATOM   1581  C  CE3 . TRP A  1 197 ? 41.890  61.033  33.800  1.00 27.82 ?  221  TRP A CE3 1 
ATOM   1582  C  CZ2 . TRP A  1 197 ? 39.115  60.595  33.382  1.00 27.72 ?  221  TRP A CZ2 1 
ATOM   1583  C  CZ3 . TRP A  1 197 ? 41.289  59.821  34.123  1.00 27.75 ?  221  TRP A CZ3 1 
ATOM   1584  C  CH2 . TRP A  1 197 ? 39.917  59.612  33.910  1.00 28.32 ?  221  TRP A CH2 1 
ATOM   1585  N  N   . PRO A  1 198 ? 45.437  64.683  34.268  1.00 28.01 ?  222  PRO A N   1 
ATOM   1586  C  CA  . PRO A  1 198 ? 46.813  65.110  34.000  1.00 27.85 ?  222  PRO A CA  1 
ATOM   1587  C  C   . PRO A  1 198 ? 47.014  65.485  32.528  1.00 27.69 ?  222  PRO A C   1 
ATOM   1588  O  O   . PRO A  1 198 ? 46.359  64.912  31.648  1.00 27.48 ?  222  PRO A O   1 
ATOM   1589  C  CB  . PRO A  1 198 ? 47.637  63.867  34.344  1.00 27.84 ?  222  PRO A CB  1 
ATOM   1590  C  CG  . PRO A  1 198 ? 46.831  63.158  35.366  1.00 27.69 ?  222  PRO A CG  1 
ATOM   1591  C  CD  . PRO A  1 198 ? 45.396  63.391  34.984  1.00 28.05 ?  222  PRO A CD  1 
ATOM   1592  N  N   . ALA A  1 199 ? 47.903  66.444  32.275  1.00 27.45 ?  223  ALA A N   1 
ATOM   1593  C  CA  . ALA A  1 199 ? 48.185  66.908  30.913  1.00 27.34 ?  223  ALA A CA  1 
ATOM   1594  C  C   . ALA A  1 199 ? 48.634  65.751  30.024  1.00 27.10 ?  223  ALA A C   1 
ATOM   1595  O  O   . ALA A  1 199 ? 49.496  64.960  30.412  1.00 27.24 ?  223  ALA A O   1 
ATOM   1596  C  CB  . ALA A  1 199 ? 49.232  68.019  30.930  1.00 27.23 ?  223  ALA A CB  1 
ATOM   1597  N  N   . GLY A  1 200 ? 48.026  65.648  28.844  1.00 26.81 ?  224  GLY A N   1 
ATOM   1598  C  CA  . GLY A  1 200 ? 48.336  64.579  27.893  1.00 26.40 ?  224  GLY A CA  1 
ATOM   1599  C  C   . GLY A  1 200 ? 47.512  63.315  28.089  1.00 26.28 ?  224  GLY A C   1 
ATOM   1600  O  O   . GLY A  1 200 ? 47.707  62.327  27.379  1.00 26.31 ?  224  GLY A O   1 
ATOM   1601  N  N   . ARG A  1 201 ? 46.589  63.350  29.048  1.00 25.95 ?  225  ARG A N   1 
ATOM   1602  C  CA  . ARG A  1 201 ? 45.769  62.188  29.389  1.00 25.74 ?  225  ARG A CA  1 
ATOM   1603  C  C   . ARG A  1 201 ? 44.271  62.515  29.446  1.00 25.35 ?  225  ARG A C   1 
ATOM   1604  O  O   . ARG A  1 201 ? 43.899  63.637  29.789  1.00 25.44 ?  225  ARG A O   1 
ATOM   1605  C  CB  . ARG A  1 201 ? 46.245  61.584  30.713  1.00 25.75 ?  225  ARG A CB  1 
ATOM   1606  C  CG  . ARG A  1 201 ? 47.446  60.654  30.549  1.00 25.94 ?  225  ARG A CG  1 
ATOM   1607  C  CD  . ARG A  1 201 ? 48.183  60.439  31.852  1.00 26.59 ?  225  ARG A CD  1 
ATOM   1608  N  NE  . ARG A  1 201 ? 47.349  59.814  32.879  1.00 26.89 ?  225  ARG A NE  1 
ATOM   1609  C  CZ  . ARG A  1 201 ? 47.733  59.628  34.140  1.00 27.41 ?  225  ARG A CZ  1 
ATOM   1610  N  NH1 . ARG A  1 201 ? 48.943  60.021  34.533  1.00 26.77 ?  225  ARG A NH1 1 
ATOM   1611  N  NH2 . ARG A  1 201 ? 46.910  59.049  35.010  1.00 26.13 ?  225  ARG A NH2 1 
ATOM   1612  N  N   . PRO A  1 202 ? 43.407  61.538  29.097  1.00 24.98 ?  226  PRO A N   1 
ATOM   1613  C  CA  . PRO A  1 202 ? 43.756  60.186  28.638  1.00 24.73 ?  226  PRO A CA  1 
ATOM   1614  C  C   . PRO A  1 202 ? 44.214  60.148  27.180  1.00 24.50 ?  226  PRO A C   1 
ATOM   1615  O  O   . PRO A  1 202 ? 43.777  60.969  26.363  1.00 24.37 ?  226  PRO A O   1 
ATOM   1616  C  CB  . PRO A  1 202 ? 42.448  59.398  28.812  1.00 24.75 ?  226  PRO A CB  1 
ATOM   1617  C  CG  . PRO A  1 202 ? 41.529  60.299  29.615  1.00 24.83 ?  226  PRO A CG  1 
ATOM   1618  C  CD  . PRO A  1 202 ? 41.952  61.682  29.270  1.00 24.95 ?  226  PRO A CD  1 
ATOM   1619  N  N   . SER A  1 203 ? 45.100  59.202  26.872  1.00 24.22 ?  227  SER A N   1 
ATOM   1620  C  CA  . SER A  1 203 ? 45.652  59.051  25.528  1.00 24.16 ?  227  SER A CA  1 
ATOM   1621  C  C   . SER A  1 203 ? 46.366  57.718  25.376  1.00 24.02 ?  227  SER A C   1 
ATOM   1622  O  O   . SER A  1 203 ? 46.655  57.038  26.368  1.00 24.03 ?  227  SER A O   1 
ATOM   1623  C  CB  . SER A  1 203 ? 46.639  60.186  25.224  1.00 24.35 ?  227  SER A CB  1 
ATOM   1624  O  OG  . SER A  1 203 ? 47.773  60.111  26.075  1.00 24.39 ?  227  SER A OG  1 
ATOM   1625  N  N   . HIS A  1 204 ? 46.661  57.356  24.131  1.00 23.69 ?  228  HIS A N   1 
ATOM   1626  C  CA  . HIS A  1 204 ? 47.479  56.183  23.855  1.00 23.36 ?  228  HIS A CA  1 
ATOM   1627  C  C   . HIS A  1 204 ? 48.962  56.462  24.121  1.00 23.36 ?  228  HIS A C   1 
ATOM   1628  O  O   . HIS A  1 204 ? 49.709  55.556  24.501  1.00 23.56 ?  228  HIS A O   1 
ATOM   1629  C  CB  . HIS A  1 204 ? 47.235  55.669  22.433  1.00 23.12 ?  228  HIS A CB  1 
ATOM   1630  C  CG  . HIS A  1 204 ? 45.853  55.120  22.216  1.00 23.01 ?  228  HIS A CG  1 
ATOM   1631  N  ND1 . HIS A  1 204 ? 45.137  55.342  21.059  1.00 22.42 ?  228  HIS A ND1 1 
ATOM   1632  C  CD2 . HIS A  1 204 ? 45.050  54.376  23.017  1.00 22.20 ?  228  HIS A CD2 1 
ATOM   1633  C  CE1 . HIS A  1 204 ? 43.959  54.746  21.150  1.00 22.63 ?  228  HIS A CE1 1 
ATOM   1634  N  NE2 . HIS A  1 204 ? 43.878  54.153  22.330  1.00 22.84 ?  228  HIS A NE2 1 
ATOM   1635  N  N   . ALA A  1 205 ? 49.372  57.720  23.945  1.00 23.13 ?  229  ALA A N   1 
ATOM   1636  C  CA  . ALA A  1 205 ? 50.747  58.161  24.224  1.00 23.04 ?  229  ALA A CA  1 
ATOM   1637  C  C   . ALA A  1 205 ? 51.204  57.930  25.667  1.00 22.93 ?  229  ALA A C   1 
ATOM   1638  O  O   . ALA A  1 205 ? 52.394  57.747  25.918  1.00 23.19 ?  229  ALA A O   1 
ATOM   1639  C  CB  . ALA A  1 205 ? 50.923  59.637  23.848  1.00 22.86 ?  229  ALA A CB  1 
ATOM   1640  N  N   . LEU A  1 206 ? 50.263  57.952  26.608  1.00 22.80 ?  230  LEU A N   1 
ATOM   1641  C  CA  . LEU A  1 206 ? 50.588  57.818  28.029  1.00 22.70 ?  230  LEU A CA  1 
ATOM   1642  C  C   . LEU A  1 206 ? 49.774  56.737  28.749  1.00 22.72 ?  230  LEU A C   1 
ATOM   1643  O  O   . LEU A  1 206 ? 49.595  56.803  29.970  1.00 22.71 ?  230  LEU A O   1 
ATOM   1644  C  CB  . LEU A  1 206 ? 50.434  59.170  28.745  1.00 22.49 ?  230  LEU A CB  1 
ATOM   1645  C  CG  . LEU A  1 206 ? 51.452  60.271  28.416  1.00 22.87 ?  230  LEU A CG  1 
ATOM   1646  C  CD1 . LEU A  1 206 ? 50.964  61.639  28.905  1.00 23.30 ?  230  LEU A CD1 1 
ATOM   1647  C  CD2 . LEU A  1 206 ? 52.834  59.954  28.985  1.00 21.99 ?  230  LEU A CD2 1 
ATOM   1648  N  N   . ASP A  1 207 ? 49.300  55.739  28.004  1.00 22.56 ?  231  ASP A N   1 
ATOM   1649  C  CA  . ASP A  1 207 ? 48.509  54.659  28.605  1.00 22.85 ?  231  ASP A CA  1 
ATOM   1650  C  C   . ASP A  1 207 ? 49.315  53.799  29.579  1.00 22.87 ?  231  ASP A C   1 
ATOM   1651  O  O   . ASP A  1 207 ? 48.790  53.373  30.609  1.00 22.79 ?  231  ASP A O   1 
ATOM   1652  C  CB  . ASP A  1 207 ? 47.776  53.804  27.546  1.00 22.82 ?  231  ASP A CB  1 
ATOM   1653  C  CG  . ASP A  1 207 ? 48.714  53.060  26.605  1.00 23.29 ?  231  ASP A CG  1 
ATOM   1654  O  OD1 . ASP A  1 207 ? 49.917  53.376  26.542  1.00 23.43 ?  231  ASP A OD1 1 
ATOM   1655  O  OD2 . ASP A  1 207 ? 48.229  52.143  25.907  1.00 24.85 -1 231  ASP A OD2 1 
ATOM   1656  N  N   . TYR A  1 208 ? 50.589  53.574  29.260  1.00 23.04 ?  232  TYR A N   1 
ATOM   1657  C  CA  . TYR A  1 208 ? 51.473  52.809  30.132  1.00 23.25 ?  232  TYR A CA  1 
ATOM   1658  C  C   . TYR A  1 208 ? 51.864  53.600  31.377  1.00 23.37 ?  232  TYR A C   1 
ATOM   1659  O  O   . TYR A  1 208 ? 51.869  53.057  32.485  1.00 23.17 ?  232  TYR A O   1 
ATOM   1660  C  CB  . TYR A  1 208 ? 52.723  52.317  29.384  1.00 23.14 ?  232  TYR A CB  1 
ATOM   1661  C  CG  . TYR A  1 208 ? 53.571  51.396  30.232  1.00 23.12 ?  232  TYR A CG  1 
ATOM   1662  C  CD1 . TYR A  1 208 ? 53.150  50.095  30.517  1.00 22.61 ?  232  TYR A CD1 1 
ATOM   1663  C  CD2 . TYR A  1 208 ? 54.783  51.830  30.770  1.00 23.01 ?  232  TYR A CD2 1 
ATOM   1664  C  CE1 . TYR A  1 208 ? 53.918  49.251  31.312  1.00 23.40 ?  232  TYR A CE1 1 
ATOM   1665  C  CE2 . TYR A  1 208 ? 55.559  50.991  31.564  1.00 23.25 ?  232  TYR A CE2 1 
ATOM   1666  C  CZ  . TYR A  1 208 ? 55.123  49.706  31.830  1.00 23.11 ?  232  TYR A CZ  1 
ATOM   1667  O  OH  . TYR A  1 208 ? 55.884  48.878  32.621  1.00 23.50 ?  232  TYR A OH  1 
ATOM   1668  N  N   . THR A  1 209 ? 52.194  54.877  31.186  1.00 23.57 ?  233  THR A N   1 
ATOM   1669  C  CA  . THR A  1 209 ? 52.476  55.775  32.303  1.00 23.94 ?  233  THR A CA  1 
ATOM   1670  C  C   . THR A  1 209 ? 51.286  55.809  33.256  1.00 23.74 ?  233  THR A C   1 
ATOM   1671  O  O   . THR A  1 209 ? 51.455  55.648  34.457  1.00 23.72 ?  233  THR A O   1 
ATOM   1672  C  CB  . THR A  1 209 ? 52.828  57.200  31.823  1.00 24.03 ?  233  THR A CB  1 
ATOM   1673  O  OG1 . THR A  1 209 ? 54.090  57.172  31.146  1.00 24.84 ?  233  THR A OG1 1 
ATOM   1674  C  CG2 . THR A  1 209 ? 52.920  58.172  33.000  1.00 24.42 ?  233  THR A CG2 1 
ATOM   1675  N  N   . ALA A  1 210 ? 50.084  55.987  32.708  1.00 23.85 ?  234  ALA A N   1 
ATOM   1676  C  CA  . ALA A  1 210 ? 48.868  56.027  33.522  1.00 23.96 ?  234  ALA A CA  1 
ATOM   1677  C  C   . ALA A  1 210 ? 48.683  54.730  34.310  1.00 24.03 ?  234  ALA A C   1 
ATOM   1678  O  O   . ALA A  1 210 ? 48.271  54.756  35.471  1.00 24.06 ?  234  ALA A O   1 
ATOM   1679  C  CB  . ALA A  1 210 ? 47.659  56.308  32.661  1.00 23.69 ?  234  ALA A CB  1 
ATOM   1680  N  N   . ASN A  1 211 ? 49.009  53.610  33.667  1.00 24.02 ?  235  ASN A N   1 
ATOM   1681  C  CA  . ASN A  1 211 ? 48.939  52.283  34.272  1.00 24.09 ?  235  ASN A CA  1 
ATOM   1682  C  C   . ASN A  1 211 ? 49.879  52.126  35.476  1.00 24.13 ?  235  ASN A C   1 
ATOM   1683  O  O   . ASN A  1 211 ? 49.444  51.741  36.565  1.00 24.11 ?  235  ASN A O   1 
ATOM   1684  C  CB  . ASN A  1 211 ? 49.234  51.225  33.202  1.00 24.05 ?  235  ASN A CB  1 
ATOM   1685  C  CG  . ASN A  1 211 ? 49.302  49.816  33.756  1.00 24.55 ?  235  ASN A CG  1 
ATOM   1686  O  OD1 . ASN A  1 211 ? 50.379  49.224  33.832  1.00 26.70 ?  235  ASN A OD1 1 
ATOM   1687  N  ND2 . ASN A  1 211 ? 48.155  49.266  34.133  1.00 23.98 ?  235  ASN A ND2 1 
ATOM   1688  N  N   . ILE A  1 212 ? 51.158  52.437  35.280  1.00 24.00 ?  236  ILE A N   1 
ATOM   1689  C  CA  . ILE A  1 212 ? 52.165  52.245  36.330  1.00 24.02 ?  236  ILE A CA  1 
ATOM   1690  C  C   . ILE A  1 212 ? 52.123  53.329  37.410  1.00 23.96 ?  236  ILE A C   1 
ATOM   1691  O  O   . ILE A  1 212 ? 52.719  53.163  38.477  1.00 23.94 ?  236  ILE A O   1 
ATOM   1692  C  CB  . ILE A  1 212 ? 53.599  52.115  35.757  1.00 23.99 ?  236  ILE A CB  1 
ATOM   1693  C  CG1 . ILE A  1 212 ? 54.034  53.421  35.075  1.00 24.39 ?  236  ILE A CG1 1 
ATOM   1694  C  CG2 . ILE A  1 212 ? 53.688  50.913  34.812  1.00 24.07 ?  236  ILE A CG2 1 
ATOM   1695  C  CD1 . ILE A  1 212 ? 55.504  53.488  34.732  1.00 24.71 ?  236  ILE A CD1 1 
ATOM   1696  N  N   . GLU A  1 213 ? 51.422  54.427  37.127  1.00 23.80 ?  237  GLU A N   1 
ATOM   1697  C  CA  . GLU A  1 213 ? 51.235  55.502  38.108  1.00 23.95 ?  237  GLU A CA  1 
ATOM   1698  C  C   . GLU A  1 213 ? 49.940  55.351  38.920  1.00 23.87 ?  237  GLU A C   1 
ATOM   1699  O  O   . GLU A  1 213 ? 49.611  56.204  39.754  1.00 23.88 ?  237  GLU A O   1 
ATOM   1700  C  CB  . GLU A  1 213 ? 51.308  56.884  37.441  1.00 23.84 ?  237  GLU A CB  1 
ATOM   1701  C  CG  . GLU A  1 213 ? 52.694  57.277  36.921  1.00 24.22 ?  237  GLU A CG  1 
ATOM   1702  C  CD  . GLU A  1 213 ? 53.760  57.366  38.009  1.00 25.10 ?  237  GLU A CD  1 
ATOM   1703  O  OE1 . GLU A  1 213 ? 53.422  57.581  39.193  1.00 26.42 ?  237  GLU A OE1 1 
ATOM   1704  O  OE2 . GLU A  1 213 ? 54.951  57.223  37.677  1.00 25.29 -1 237  GLU A OE2 1 
ATOM   1705  N  N   . THR A  1 214 ? 49.222  54.258  38.675  1.00 23.77 ?  238  THR A N   1 
ATOM   1706  C  CA  . THR A  1 214 ? 48.041  53.903  39.453  1.00 23.62 ?  238  THR A CA  1 
ATOM   1707  C  C   . THR A  1 214 ? 48.492  53.159  40.705  1.00 23.65 ?  238  THR A C   1 
ATOM   1708  O  O   . THR A  1 214 ? 49.108  52.094  40.612  1.00 23.89 ?  238  THR A O   1 
ATOM   1709  C  CB  . THR A  1 214 ? 47.074  53.028  38.621  1.00 23.76 ?  238  THR A CB  1 
ATOM   1710  O  OG1 . THR A  1 214 ? 46.663  53.750  37.450  1.00 23.08 ?  238  THR A OG1 1 
ATOM   1711  C  CG2 . THR A  1 214 ? 45.844  52.627  39.437  1.00 23.17 ?  238  THR A CG2 1 
ATOM   1712  N  N   . THR A  1 215 ? 48.184  53.723  41.871  1.00 23.51 ?  239  THR A N   1 
ATOM   1713  C  CA  . THR A  1 215 ? 48.685  53.201  43.149  1.00 23.45 ?  239  THR A CA  1 
ATOM   1714  C  C   . THR A  1 215 ? 48.453  51.699  43.360  1.00 23.36 ?  239  THR A C   1 
ATOM   1715  O  O   . THR A  1 215 ? 49.397  50.967  43.658  1.00 23.45 ?  239  THR A O   1 
ATOM   1716  C  CB  . THR A  1 215 ? 48.129  53.999  44.351  1.00 23.50 ?  239  THR A CB  1 
ATOM   1717  O  OG1 . THR A  1 215 ? 48.362  55.398  44.144  1.00 24.09 ?  239  THR A OG1 1 
ATOM   1718  C  CG2 . THR A  1 215 ? 48.811  53.566  45.637  1.00 23.43 ?  239  THR A CG2 1 
ATOM   1719  N  N   . VAL A  1 216 ? 47.209  51.243  43.201  1.00 23.10 ?  240  VAL A N   1 
ATOM   1720  C  CA  . VAL A  1 216 ? 46.878  49.832  43.426  1.00 22.74 ?  240  VAL A CA  1 
ATOM   1721  C  C   . VAL A  1 216 ? 47.640  48.885  42.488  1.00 22.74 ?  240  VAL A C   1 
ATOM   1722  O  O   . VAL A  1 216 ? 48.043  47.802  42.908  1.00 22.66 ?  240  VAL A O   1 
ATOM   1723  C  CB  . VAL A  1 216 ? 45.335  49.558  43.404  1.00 22.86 ?  240  VAL A CB  1 
ATOM   1724  C  CG1 . VAL A  1 216 ? 44.758  49.668  41.997  1.00 21.53 ?  240  VAL A CG1 1 
ATOM   1725  C  CG2 . VAL A  1 216 ? 45.010  48.195  44.034  1.00 22.48 ?  240  VAL A CG2 1 
ATOM   1726  N  N   . TRP A  1 217 ? 47.846  49.299  41.237  1.00 22.76 ?  241  TRP A N   1 
ATOM   1727  C  CA  . TRP A  1 217 ? 48.647  48.516  40.292  1.00 22.70 ?  241  TRP A CA  1 
ATOM   1728  C  C   . TRP A  1 217 ? 50.048  48.272  40.844  1.00 22.66 ?  241  TRP A C   1 
ATOM   1729  O  O   . TRP A  1 217 ? 50.563  47.156  40.774  1.00 22.81 ?  241  TRP A O   1 
ATOM   1730  C  CB  . TRP A  1 217 ? 48.751  49.204  38.922  1.00 22.61 ?  241  TRP A CB  1 
ATOM   1731  C  CG  . TRP A  1 217 ? 49.493  48.355  37.921  1.00 22.62 ?  241  TRP A CG  1 
ATOM   1732  C  CD1 . TRP A  1 217 ? 48.953  47.428  37.080  1.00 22.10 ?  241  TRP A CD1 1 
ATOM   1733  C  CD2 . TRP A  1 217 ? 50.911  48.330  37.690  1.00 22.53 ?  241  TRP A CD2 1 
ATOM   1734  N  NE1 . TRP A  1 217 ? 49.938  46.838  36.328  1.00 22.68 ?  241  TRP A NE1 1 
ATOM   1735  C  CE2 . TRP A  1 217 ? 51.151  47.370  36.683  1.00 22.75 ?  241  TRP A CE2 1 
ATOM   1736  C  CE3 . TRP A  1 217 ? 51.999  49.033  38.230  1.00 22.51 ?  241  TRP A CE3 1 
ATOM   1737  C  CZ2 . TRP A  1 217 ? 52.439  47.089  36.203  1.00 22.84 ?  241  TRP A CZ2 1 
ATOM   1738  C  CZ3 . TRP A  1 217 ? 53.278  48.755  37.753  1.00 22.67 ?  241  TRP A CZ3 1 
ATOM   1739  C  CH2 . TRP A  1 217 ? 53.487  47.789  36.751  1.00 22.54 ?  241  TRP A CH2 1 
ATOM   1740  N  N   . ALA A  1 218 ? 50.659  49.323  41.385  1.00 22.59 ?  242  ALA A N   1 
ATOM   1741  C  CA  . ALA A  1 218 ? 52.005  49.227  41.943  1.00 22.65 ?  242  ALA A CA  1 
ATOM   1742  C  C   . ALA A  1 218 ? 52.021  48.574  43.322  1.00 22.69 ?  242  ALA A C   1 
ATOM   1743  O  O   . ALA A  1 218 ? 53.015  47.959  43.701  1.00 22.58 ?  242  ALA A O   1 
ATOM   1744  C  CB  . ALA A  1 218 ? 52.659  50.601  41.995  1.00 22.55 ?  242  ALA A CB  1 
ATOM   1745  N  N   . ALA A  1 219 ? 50.910  48.696  44.052  1.00 22.78 ?  243  ALA A N   1 
ATOM   1746  C  CA  . ALA A  1 219 ? 50.835  48.284  45.457  1.00 23.00 ?  243  ALA A CA  1 
ATOM   1747  C  C   . ALA A  1 219 ? 50.368  46.851  45.696  1.00 23.16 ?  243  ALA A C   1 
ATOM   1748  O  O   . ALA A  1 219 ? 50.775  46.229  46.684  1.00 23.33 ?  243  ALA A O   1 
ATOM   1749  C  CB  . ALA A  1 219 ? 49.953  49.255  46.247  1.00 23.01 ?  243  ALA A CB  1 
ATOM   1750  N  N   . MET A  1 220 ? 49.506  46.336  44.817  1.00 23.02 ?  244  MET A N   1 
ATOM   1751  C  CA  . MET A  1 220 ? 48.899  45.012  45.014  1.00 22.69 ?  244  MET A CA  1 
ATOM   1752  C  C   . MET A  1 220 ? 49.915  43.884  44.829  1.00 22.47 ?  244  MET A C   1 
ATOM   1753  O  O   . MET A  1 220 ? 50.848  44.020  44.036  1.00 22.72 ?  244  MET A O   1 
ATOM   1754  C  CB  . MET A  1 220 ? 47.663  44.812  44.113  1.00 22.62 ?  244  MET A CB  1 
ATOM   1755  C  CG  . MET A  1 220 ? 47.937  44.768  42.607  1.00 22.46 ?  244  MET A CG  1 
ATOM   1756  S  SD  . MET A  1 220 ? 46.438  44.901  41.598  1.00 22.80 ?  244  MET A SD  1 
ATOM   1757  C  CE  . MET A  1 220 ? 45.643  43.324  41.927  1.00 21.23 ?  244  MET A CE  1 
ATOM   1758  N  N   . PRO A  1 221 ? 49.750  42.778  45.579  1.00 22.18 ?  245  PRO A N   1 
ATOM   1759  C  CA  . PRO A  1 221 ? 50.677  41.655  45.437  1.00 22.11 ?  245  PRO A CA  1 
ATOM   1760  C  C   . PRO A  1 221 ? 50.378  40.706  44.269  1.00 22.19 ?  245  PRO A C   1 
ATOM   1761  O  O   . PRO A  1 221 ? 51.288  40.003  43.819  1.00 22.15 ?  245  PRO A O   1 
ATOM   1762  C  CB  . PRO A  1 221 ? 50.550  40.920  46.777  1.00 21.98 ?  245  PRO A CB  1 
ATOM   1763  C  CG  . PRO A  1 221 ? 49.176  41.244  47.256  1.00 22.22 ?  245  PRO A CG  1 
ATOM   1764  C  CD  . PRO A  1 221 ? 48.855  42.620  46.744  1.00 21.94 ?  245  PRO A CD  1 
ATOM   1765  N  N   . GLN A  1 222 ? 49.133  40.686  43.788  1.00 22.05 ?  246  GLN A N   1 
ATOM   1766  C  CA  . GLN A  1 222 ? 48.732  39.810  42.670  1.00 22.06 ?  246  GLN A CA  1 
ATOM   1767  C  C   . GLN A  1 222 ? 49.238  40.350  41.335  1.00 22.00 ?  246  GLN A C   1 
ATOM   1768  O  O   . GLN A  1 222 ? 48.466  40.903  40.551  1.00 22.24 ?  246  GLN A O   1 
ATOM   1769  C  CB  . GLN A  1 222 ? 47.204  39.642  42.611  1.00 21.81 ?  246  GLN A CB  1 
ATOM   1770  C  CG  . GLN A  1 222 ? 46.565  39.000  43.839  1.00 21.43 ?  246  GLN A CG  1 
ATOM   1771  C  CD  . GLN A  1 222 ? 46.297  39.991  44.971  1.00 21.58 ?  246  GLN A CD  1 
ATOM   1772  O  OE1 . GLN A  1 222 ? 46.590  41.184  44.859  1.00 20.55 ?  246  GLN A OE1 1 
ATOM   1773  N  NE2 . GLN A  1 222 ? 45.735  39.493  46.068  1.00 21.88 ?  246  GLN A NE2 1 
ATOM   1774  N  N   . ARG A  1 223 ? 50.531  40.170  41.073  1.00 22.02 ?  247  ARG A N   1 
ATOM   1775  C  CA  . ARG A  1 223 ? 51.187  40.765  39.898  1.00 21.87 ?  247  ARG A CA  1 
ATOM   1776  C  C   . ARG A  1 223 ? 50.586  40.336  38.560  1.00 21.96 ?  247  ARG A C   1 
ATOM   1777  O  O   . ARG A  1 223 ? 50.562  41.112  37.598  1.00 21.96 ?  247  ARG A O   1 
ATOM   1778  C  CB  . ARG A  1 223 ? 52.698  40.480  39.906  1.00 21.83 ?  247  ARG A CB  1 
ATOM   1779  C  CG  . ARG A  1 223 ? 53.449  40.950  41.160  1.00 21.67 ?  247  ARG A CG  1 
ATOM   1780  C  CD  . ARG A  1 223 ? 53.078  42.381  41.568  1.00 21.05 ?  247  ARG A CD  1 
ATOM   1781  N  NE  . ARG A  1 223 ? 53.187  43.333  40.462  1.00 20.50 ?  247  ARG A NE  1 
ATOM   1782  C  CZ  . ARG A  1 223 ? 52.568  44.510  40.426  1.00 20.12 ?  247  ARG A CZ  1 
ATOM   1783  N  NH1 . ARG A  1 223 ? 51.790  44.887  41.434  1.00 19.90 ?  247  ARG A NH1 1 
ATOM   1784  N  NH2 . ARG A  1 223 ? 52.723  45.311  39.380  1.00 19.59 ?  247  ARG A NH2 1 
ATOM   1785  N  N   . GLU A  1 224 ? 50.114  39.094  38.506  1.00 21.86 ?  248  GLU A N   1 
ATOM   1786  C  CA  . GLU A  1 224 ? 49.563  38.526  37.280  1.00 21.60 ?  248  GLU A CA  1 
ATOM   1787  C  C   . GLU A  1 224 ? 48.185  39.119  36.960  1.00 21.68 ?  248  GLU A C   1 
ATOM   1788  O  O   . GLU A  1 224 ? 47.791  39.206  35.793  1.00 21.64 ?  248  GLU A O   1 
ATOM   1789  C  CB  . GLU A  1 224 ? 49.521  36.998  37.382  1.00 21.64 ?  248  GLU A CB  1 
ATOM   1790  C  CG  . GLU A  1 224 ? 50.875  36.300  37.147  1.00 21.83 ?  248  GLU A CG  1 
ATOM   1791  C  CD  . GLU A  1 224 ? 51.917  36.542  38.246  1.00 22.55 ?  248  GLU A CD  1 
ATOM   1792  O  OE1 . GLU A  1 224 ? 51.544  36.916  39.378  1.00 23.06 ?  248  GLU A OE1 1 
ATOM   1793  O  OE2 . GLU A  1 224 ? 53.122  36.351  37.977  1.00 22.34 -1 248  GLU A OE2 1 
ATOM   1794  N  N   . VAL A  1 225 ? 47.470  39.539  38.003  1.00 21.50 ?  249  VAL A N   1 
ATOM   1795  C  CA  . VAL A  1 225 ? 46.220  40.277  37.850  1.00 21.57 ?  249  VAL A CA  1 
ATOM   1796  C  C   . VAL A  1 225 ? 46.529  41.697  37.372  1.00 21.83 ?  249  VAL A C   1 
ATOM   1797  O  O   . VAL A  1 225 ? 45.885  42.206  36.449  1.00 21.76 ?  249  VAL A O   1 
ATOM   1798  C  CB  . VAL A  1 225 ? 45.413  40.313  39.184  1.00 21.61 ?  249  VAL A CB  1 
ATOM   1799  C  CG1 . VAL A  1 225 ? 44.190  41.219  39.070  1.00 21.50 ?  249  VAL A CG1 1 
ATOM   1800  C  CG2 . VAL A  1 225 ? 45.000  38.907  39.599  1.00 21.34 ?  249  VAL A CG2 1 
ATOM   1801  N  N   . ALA A  1 226 ? 47.523  42.324  38.003  1.00 21.88 ?  250  ALA A N   1 
ATOM   1802  C  CA  . ALA A  1 226 ? 47.971  43.664  37.630  1.00 22.08 ?  250  ALA A CA  1 
ATOM   1803  C  C   . ALA A  1 226 ? 48.497  43.741  36.195  1.00 22.32 ?  250  ALA A C   1 
ATOM   1804  O  O   . ALA A  1 226 ? 48.280  44.739  35.508  1.00 22.44 ?  250  ALA A O   1 
ATOM   1805  C  CB  . ALA A  1 226 ? 49.032  44.170  38.617  1.00 22.01 ?  250  ALA A CB  1 
ATOM   1806  N  N   . GLU A  1 227 ? 49.179  42.691  35.742  1.00 22.52 ?  251  GLU A N   1 
ATOM   1807  C  CA  . GLU A  1 227 ? 49.729  42.677  34.384  1.00 22.90 ?  251  GLU A CA  1 
ATOM   1808  C  C   . GLU A  1 227 ? 48.651  42.516  33.306  1.00 22.51 ?  251  GLU A C   1 
ATOM   1809  O  O   . GLU A  1 227 ? 48.890  42.804  32.136  1.00 22.57 ?  251  GLU A O   1 
ATOM   1810  C  CB  . GLU A  1 227 ? 50.834  41.626  34.240  1.00 23.16 ?  251  GLU A CB  1 
ATOM   1811  C  CG  . GLU A  1 227 ? 51.885  41.966  33.175  1.00 25.31 ?  251  GLU A CG  1 
ATOM   1812  C  CD  . GLU A  1 227 ? 52.836  43.096  33.571  1.00 28.06 ?  251  GLU A CD  1 
ATOM   1813  O  OE1 . GLU A  1 227 ? 52.675  43.683  34.669  1.00 27.86 ?  251  GLU A OE1 1 
ATOM   1814  O  OE2 . GLU A  1 227 ? 53.762  43.392  32.773  1.00 29.25 -1 251  GLU A OE2 1 
ATOM   1815  N  N   . GLY A  1 228 ? 47.471  42.049  33.713  1.00 22.22 ?  252  GLY A N   1 
ATOM   1816  C  CA  . GLY A  1 228 ? 46.292  42.071  32.855  1.00 22.02 ?  252  GLY A CA  1 
ATOM   1817  C  C   . GLY A  1 228 ? 45.877  43.495  32.537  1.00 21.86 ?  252  GLY A C   1 
ATOM   1818  O  O   . GLY A  1 228 ? 45.481  43.793  31.413  1.00 21.69 ?  252  GLY A O   1 
ATOM   1819  N  N   . CYS A  1 229 ? 45.974  44.378  33.530  1.00 21.72 ?  253  CYS A N   1 
ATOM   1820  C  CA  . CYS A  1 229 ? 45.768  45.805  33.302  1.00 21.89 ?  253  CYS A CA  1 
ATOM   1821  C  C   . CYS A  1 229 ? 46.802  46.327  32.303  1.00 21.93 ?  253  CYS A C   1 
ATOM   1822  O  O   . CYS A  1 229 ? 46.457  47.055  31.370  1.00 22.13 ?  253  CYS A O   1 
ATOM   1823  C  CB  . CYS A  1 229 ? 45.840  46.586  34.615  1.00 21.86 ?  253  CYS A CB  1 
ATOM   1824  S  SG  . CYS A  1 229 ? 44.671  46.002  35.868  1.00 21.43 ?  253  CYS A SG  1 
ATOM   1825  N  N   . THR A  1 230 ? 48.054  45.915  32.490  1.00 21.72 ?  254  THR A N   1 
ATOM   1826  C  CA  . THR A  1 230 ? 49.165  46.329  31.633  1.00 21.78 ?  254  THR A CA  1 
ATOM   1827  C  C   . THR A  1 230 ? 48.934  45.986  30.160  1.00 21.76 ?  254  THR A C   1 
ATOM   1828  O  O   . THR A  1 230 ? 49.232  46.795  29.281  1.00 21.60 ?  254  THR A O   1 
ATOM   1829  C  CB  . THR A  1 230 ? 50.501  45.706  32.102  1.00 21.57 ?  254  THR A CB  1 
ATOM   1830  O  OG1 . THR A  1 230 ? 50.720  46.034  33.479  1.00 22.05 ?  254  THR A OG1 1 
ATOM   1831  C  CG2 . THR A  1 230 ? 51.665  46.224  31.270  1.00 21.46 ?  254  THR A CG2 1 
ATOM   1832  N  N   . MET A  1 231 ? 48.399  44.791  29.904  1.00 21.68 ?  255  MET A N   1 
ATOM   1833  C  CA  . MET A  1 231 ? 48.180  44.308  28.540  1.00 21.88 ?  255  MET A CA  1 
ATOM   1834  C  C   . MET A  1 231 ? 47.249  45.203  27.715  1.00 21.69 ?  255  MET A C   1 
ATOM   1835  O  O   . MET A  1 231 ? 47.343  45.232  26.484  1.00 21.53 ?  255  MET A O   1 
ATOM   1836  C  CB  . MET A  1 231 ? 47.684  42.857  28.556  1.00 22.26 ?  255  MET A CB  1 
ATOM   1837  C  CG  . MET A  1 231 ? 48.765  41.852  28.952  1.00 22.78 ?  255  MET A CG  1 
ATOM   1838  S  SD  . MET A  1 231 ? 48.231  40.134  28.953  1.00 25.63 ?  255  MET A SD  1 
ATOM   1839  C  CE  . MET A  1 231 ? 47.876  39.866  27.216  1.00 23.52 ?  255  MET A CE  1 
ATOM   1840  N  N   . CYS A  1 232 ? 46.367  45.928  28.402  1.00 21.49 ?  256  CYS A N   1 
ATOM   1841  C  CA  . CYS A  1 232 ? 45.483  46.912  27.774  1.00 21.52 ?  256  CYS A CA  1 
ATOM   1842  C  C   . CYS A  1 232 ? 46.118  48.299  27.693  1.00 21.33 ?  256  CYS A C   1 
ATOM   1843  O  O   . CYS A  1 232 ? 45.552  49.208  27.092  1.00 21.37 ?  256  CYS A O   1 
ATOM   1844  C  CB  . CYS A  1 232 ? 44.187  47.045  28.572  1.00 21.56 ?  256  CYS A CB  1 
ATOM   1845  S  SG  . CYS A  1 232 ? 43.015  45.692  28.419  1.00 21.71 ?  256  CYS A SG  1 
ATOM   1846  N  N   . HIS A  1 233 ? 47.284  48.458  28.306  1.00 21.13 ?  257  HIS A N   1 
ATOM   1847  C  CA  . HIS A  1 233 ? 47.896  49.772  28.461  1.00 21.17 ?  257  HIS A CA  1 
ATOM   1848  C  C   . HIS A  1 233 ? 49.329  49.814  27.879  1.00 21.06 ?  257  HIS A C   1 
ATOM   1849  O  O   . HIS A  1 233 ? 50.228  50.398  28.481  1.00 20.79 ?  257  HIS A O   1 
ATOM   1850  C  CB  . HIS A  1 233 ? 47.893  50.164  29.952  1.00 21.19 ?  257  HIS A CB  1 
ATOM   1851  C  CG  . HIS A  1 233 ? 46.563  50.634  30.478  1.00 21.67 ?  257  HIS A CG  1 
ATOM   1852  N  ND1 . HIS A  1 233 ? 46.288  51.965  30.709  1.00 21.73 ?  257  HIS A ND1 1 
ATOM   1853  C  CD2 . HIS A  1 233 ? 45.452  49.952  30.861  1.00 22.17 ?  257  HIS A CD2 1 
ATOM   1854  C  CE1 . HIS A  1 233 ? 45.062  52.086  31.195  1.00 22.54 ?  257  HIS A CE1 1 
ATOM   1855  N  NE2 . HIS A  1 233 ? 44.529  50.879  31.298  1.00 23.36 ?  257  HIS A NE2 1 
ATOM   1856  N  N   . THR A  1 234 ? 49.533  49.215  26.703  1.00 20.98 ?  258  THR A N   1 
ATOM   1857  C  CA  . THR A  1 234 ? 50.880  49.097  26.114  1.00 21.04 ?  258  THR A CA  1 
ATOM   1858  C  C   . THR A  1 234 ? 51.162  49.962  24.876  1.00 21.49 ?  258  THR A C   1 
ATOM   1859  O  O   . THR A  1 234 ? 52.298  49.975  24.382  1.00 21.64 ?  258  THR A O   1 
ATOM   1860  C  CB  . THR A  1 234 ? 51.224  47.633  25.750  1.00 20.90 ?  258  THR A CB  1 
ATOM   1861  O  OG1 . THR A  1 234 ? 50.178  47.082  24.947  1.00 20.99 ?  258  THR A OG1 1 
ATOM   1862  C  CG2 . THR A  1 234 ? 51.419  46.780  27.001  1.00 20.62 ?  258  THR A CG2 1 
ATOM   1863  N  N   . ASN A  1 235 ? 50.149  50.668  24.371  1.00 21.47 ?  259  ASN A N   1 
ATOM   1864  C  CA  . ASN A  1 235 ? 50.293  51.471  23.148  1.00 21.71 ?  259  ASN A CA  1 
ATOM   1865  C  C   . ASN A  1 235 ? 51.468  52.440  23.183  1.00 21.89 ?  259  ASN A C   1 
ATOM   1866  O  O   . ASN A  1 235 ? 52.144  52.639  22.171  1.00 21.96 ?  259  ASN A O   1 
ATOM   1867  C  CB  . ASN A  1 235 ? 49.005  52.237  22.840  1.00 21.60 ?  259  ASN A CB  1 
ATOM   1868  C  CG  . ASN A  1 235 ? 47.838  51.320  22.562  1.00 21.84 ?  259  ASN A CG  1 
ATOM   1869  O  OD1 . ASN A  1 235 ? 47.914  50.447  21.696  1.00 21.17 ?  259  ASN A OD1 1 
ATOM   1870  N  ND2 . ASN A  1 235 ? 46.746  51.511  23.298  1.00 21.38 ?  259  ASN A ND2 1 
ATOM   1871  N  N   . GLN A  1 236 ? 51.694  53.037  24.353  1.00 22.02 ?  260  GLN A N   1 
ATOM   1872  C  CA  . GLN A  1 236 ? 52.825  53.926  24.594  1.00 22.19 ?  260  GLN A CA  1 
ATOM   1873  C  C   . GLN A  1 236 ? 54.137  53.256  24.202  1.00 22.23 ?  260  GLN A C   1 
ATOM   1874  O  O   . GLN A  1 236 ? 54.998  53.884  23.590  1.00 22.28 ?  260  GLN A O   1 
ATOM   1875  C  CB  . GLN A  1 236 ? 52.850  54.346  26.072  1.00 22.16 ?  260  GLN A CB  1 
ATOM   1876  C  CG  . GLN A  1 236 ? 54.064  55.158  26.519  1.00 22.44 ?  260  GLN A CG  1 
ATOM   1877  C  CD  . GLN A  1 236 ? 53.921  55.700  27.935  1.00 23.49 ?  260  GLN A CD  1 
ATOM   1878  O  OE1 . GLN A  1 236 ? 52.861  55.588  28.560  1.00 24.17 ?  260  GLN A OE1 1 
ATOM   1879  N  NE2 . GLN A  1 236 ? 54.991  56.294  28.448  1.00 23.06 ?  260  GLN A NE2 1 
ATOM   1880  N  N   . ASN A  1 237 ? 54.257  51.969  24.531  1.00 22.18 ?  261  ASN A N   1 
ATOM   1881  C  CA  . ASN A  1 237 ? 55.499  51.222  24.370  1.00 21.99 ?  261  ASN A CA  1 
ATOM   1882  C  C   . ASN A  1 237 ? 55.644  50.519  23.026  1.00 22.10 ?  261  ASN A C   1 
ATOM   1883  O  O   . ASN A  1 237 ? 56.738  50.476  22.475  1.00 21.87 ?  261  ASN A O   1 
ATOM   1884  C  CB  . ASN A  1 237 ? 55.659  50.212  25.510  1.00 21.97 ?  261  ASN A CB  1 
ATOM   1885  C  CG  . ASN A  1 237 ? 55.706  50.876  26.879  1.00 22.23 ?  261  ASN A CG  1 
ATOM   1886  O  OD1 . ASN A  1 237 ? 55.947  52.079  26.991  1.00 22.33 ?  261  ASN A OD1 1 
ATOM   1887  N  ND2 . ASN A  1 237 ? 55.479  50.089  27.927  1.00 21.87 ?  261  ASN A ND2 1 
ATOM   1888  N  N   . LYS A  1 238 ? 54.550  49.961  22.508  1.00 22.09 ?  262  LYS A N   1 
ATOM   1889  C  CA  . LYS A  1 238 ? 54.591  49.246  21.227  1.00 22.02 ?  262  LYS A CA  1 
ATOM   1890  C  C   . LYS A  1 238 ? 53.416  49.596  20.308  1.00 21.98 ?  262  LYS A C   1 
ATOM   1891  O  O   . LYS A  1 238 ? 52.307  49.880  20.774  1.00 21.84 ?  262  LYS A O   1 
ATOM   1892  C  CB  . LYS A  1 238 ? 54.723  47.730  21.432  1.00 21.91 ?  262  LYS A CB  1 
ATOM   1893  C  CG  . LYS A  1 238 ? 53.610  47.081  22.240  1.00 22.57 ?  262  LYS A CG  1 
ATOM   1894  C  CD  . LYS A  1 238 ? 53.974  45.642  22.597  1.00 22.95 ?  262  LYS A CD  1 
ATOM   1895  C  CE  . LYS A  1 238 ? 52.798  44.898  23.213  1.00 23.08 ?  262  LYS A CE  1 
ATOM   1896  N  NZ  . LYS A  1 238 ? 51.687  44.695  22.241  1.00 23.23 ?  262  LYS A NZ  1 
ATOM   1897  N  N   . CYS A  1 239 ? 53.682  49.559  19.003  1.00 21.78 ?  263  CYS A N   1 
ATOM   1898  C  CA  . CYS A  1 239 ? 52.743  50.022  17.982  1.00 21.66 ?  263  CYS A CA  1 
ATOM   1899  C  C   . CYS A  1 239 ? 51.917  48.911  17.323  1.00 21.48 ?  263  CYS A C   1 
ATOM   1900  O  O   . CYS A  1 239 ? 51.318  49.137  16.269  1.00 21.64 ?  263  CYS A O   1 
ATOM   1901  C  CB  . CYS A  1 239 ? 53.503  50.798  16.898  1.00 21.46 ?  263  CYS A CB  1 
ATOM   1902  S  SG  . CYS A  1 239 ? 54.156  52.409  17.402  1.00 21.89 ?  263  CYS A SG  1 
ATOM   1903  N  N   . ASP A  1 240 ? 51.870  47.728  17.935  1.00 21.22 ?  264  ASP A N   1 
ATOM   1904  C  CA  . ASP A  1 240 ? 51.200  46.576  17.312  1.00 21.22 ?  264  ASP A CA  1 
ATOM   1905  C  C   . ASP A  1 240 ? 49.871  46.130  17.948  1.00 21.03 ?  264  ASP A C   1 
ATOM   1906  O  O   . ASP A  1 240 ? 49.487  44.963  17.828  1.00 20.80 ?  264  ASP A O   1 
ATOM   1907  C  CB  . ASP A  1 240 ? 52.169  45.385  17.206  1.00 21.21 ?  264  ASP A CB  1 
ATOM   1908  C  CG  . ASP A  1 240 ? 52.544  44.803  18.559  1.00 21.29 ?  264  ASP A CG  1 
ATOM   1909  O  OD1 . ASP A  1 240 ? 52.393  45.490  19.591  1.00 21.59 ?  264  ASP A OD1 1 
ATOM   1910  O  OD2 . ASP A  1 240 ? 53.001  43.644  18.589  1.00 21.82 -1 264  ASP A OD2 1 
ATOM   1911  N  N   . ASN A  1 241 ? 49.164  47.041  18.611  1.00 20.97 ?  265  ASN A N   1 
ATOM   1912  C  CA  . ASN A  1 241 ? 47.898  46.670  19.264  1.00 20.93 ?  265  ASN A CA  1 
ATOM   1913  C  C   . ASN A  1 241 ? 46.653  46.805  18.383  1.00 20.90 ?  265  ASN A C   1 
ATOM   1914  O  O   . ASN A  1 241 ? 45.668  46.102  18.600  1.00 20.84 ?  265  ASN A O   1 
ATOM   1915  C  CB  . ASN A  1 241 ? 47.707  47.421  20.585  1.00 20.87 ?  265  ASN A CB  1 
ATOM   1916  C  CG  . ASN A  1 241 ? 48.680  46.973  21.661  1.00 21.28 ?  265  ASN A CG  1 
ATOM   1917  O  OD1 . ASN A  1 241 ? 49.009  45.790  21.769  1.00 21.50 ?  265  ASN A OD1 1 
ATOM   1918  N  ND2 . ASN A  1 241 ? 49.145  47.922  22.469  1.00 21.34 ?  265  ASN A ND2 1 
ATOM   1919  N  N   . CYS A  1 242 ? 46.698  47.708  17.403  1.00 20.74 ?  266  CYS A N   1 
ATOM   1920  C  CA  . CYS A  1 242 ? 45.593  47.879  16.460  1.00 20.52 ?  266  CYS A CA  1 
ATOM   1921  C  C   . CYS A  1 242 ? 45.900  47.169  15.145  1.00 20.51 ?  266  CYS A C   1 
ATOM   1922  O  O   . CYS A  1 242 ? 45.094  46.360  14.675  1.00 20.45 ?  266  CYS A O   1 
ATOM   1923  C  CB  . CYS A  1 242 ? 45.286  49.361  16.230  1.00 20.34 ?  266  CYS A CB  1 
ATOM   1924  S  SG  . CYS A  1 242 ? 44.838  50.267  17.735  1.00 20.42 ?  266  CYS A SG  1 
ATOM   1925  N  N   . HIS A  1 243 ? 47.055  47.490  14.554  1.00 20.42 ?  267  HIS A N   1 
ATOM   1926  C  CA  . HIS A  1 243 ? 47.625  46.696  13.465  1.00 20.65 ?  267  HIS A CA  1 
ATOM   1927  C  C   . HIS A  1 243 ? 48.681  45.740  14.038  1.00 20.79 ?  267  HIS A C   1 
ATOM   1928  O  O   . HIS A  1 243 ? 49.813  46.147  14.320  1.00 20.88 ?  267  HIS A O   1 
ATOM   1929  C  CB  . HIS A  1 243 ? 48.173  47.561  12.297  1.00 20.63 ?  267  HIS A CB  1 
ATOM   1930  C  CG  . HIS A  1 243 ? 48.675  48.922  12.696  1.00 20.38 ?  267  HIS A CG  1 
ATOM   1931  N  ND1 . HIS A  1 243 ? 49.815  49.109  13.446  1.00 19.91 ?  267  HIS A ND1 1 
ATOM   1932  C  CD2 . HIS A  1 243 ? 48.213  50.163  12.402  1.00 20.00 ?  267  HIS A CD2 1 
ATOM   1933  C  CE1 . HIS A  1 243 ? 50.018  50.404  13.621  1.00 19.73 ?  267  HIS A CE1 1 
ATOM   1934  N  NE2 . HIS A  1 243 ? 49.062  51.069  12.996  1.00 20.01 ?  267  HIS A NE2 1 
ATOM   1935  N  N   . THR A  1 244 ? 48.287  44.478  14.226  1.00 20.78 ?  268  THR A N   1 
ATOM   1936  C  CA  . THR A  1 244 ? 49.098  43.482  14.942  1.00 20.93 ?  268  THR A CA  1 
ATOM   1937  C  C   . THR A  1 244 ? 50.304  42.961  14.155  1.00 21.15 ?  268  THR A C   1 
ATOM   1938  O  O   . THR A  1 244 ? 50.311  42.979  12.926  1.00 21.04 ?  268  THR A O   1 
ATOM   1939  C  CB  . THR A  1 244 ? 48.255  42.249  15.372  1.00 20.96 ?  268  THR A CB  1 
ATOM   1940  O  OG1 . THR A  1 244 ? 47.647  41.653  14.219  1.00 20.68 ?  268  THR A OG1 1 
ATOM   1941  C  CG2 . THR A  1 244 ? 47.171  42.635  16.389  1.00 20.61 ?  268  THR A CG2 1 
ATOM   1942  N  N   . ARG A  1 245 ? 51.315  42.491  14.885  1.00 21.37 ?  269  ARG A N   1 
ATOM   1943  C  CA  . ARG A  1 245 ? 52.401  41.687  14.310  1.00 21.78 ?  269  ARG A CA  1 
ATOM   1944  C  C   . ARG A  1 245 ? 51.841  40.334  13.845  1.00 21.94 ?  269  ARG A C   1 
ATOM   1945  O  O   . ARG A  1 245 ? 50.895  39.830  14.454  1.00 21.57 ?  269  ARG A O   1 
ATOM   1946  C  CB  . ARG A  1 245 ? 53.525  41.484  15.340  1.00 21.68 ?  269  ARG A CB  1 
ATOM   1947  C  CG  . ARG A  1 245 ? 53.118  40.731  16.609  1.00 21.85 ?  269  ARG A CG  1 
ATOM   1948  C  CD  . ARG A  1 245 ? 54.253  40.709  17.613  1.00 21.56 ?  269  ARG A CD  1 
ATOM   1949  N  NE  . ARG A  1 245 ? 54.022  39.806  18.744  1.00 21.42 ?  269  ARG A NE  1 
ATOM   1950  C  CZ  . ARG A  1 245 ? 53.384  40.138  19.864  1.00 21.47 ?  269  ARG A CZ  1 
ATOM   1951  N  NH1 . ARG A  1 245 ? 52.883  41.359  20.024  1.00 21.01 ?  269  ARG A NH1 1 
ATOM   1952  N  NH2 . ARG A  1 245 ? 53.243  39.243  20.832  1.00 21.13 ?  269  ARG A NH2 1 
ATOM   1953  N  N   . HIS A  1 246 ? 52.389  39.745  12.776  1.00 22.43 ?  270  HIS A N   1 
ATOM   1954  C  CA  . HIS A  1 246 ? 53.485  40.309  11.978  1.00 22.86 ?  270  HIS A CA  1 
ATOM   1955  C  C   . HIS A  1 246 ? 53.045  40.740  10.570  1.00 23.31 ?  270  HIS A C   1 
ATOM   1956  O  O   . HIS A  1 246 ? 53.883  41.004  9.706   1.00 22.97 ?  270  HIS A O   1 
ATOM   1957  C  CB  . HIS A  1 246 ? 54.653  39.313  11.899  1.00 22.72 ?  270  HIS A CB  1 
ATOM   1958  C  CG  . HIS A  1 246 ? 55.628  39.428  13.035  1.00 22.43 ?  270  HIS A CG  1 
ATOM   1959  N  ND1 . HIS A  1 246 ? 55.510  38.700  14.199  1.00 21.85 ?  270  HIS A ND1 1 
ATOM   1960  C  CD2 . HIS A  1 246 ? 56.735  40.194  13.182  1.00 22.08 ?  270  HIS A CD2 1 
ATOM   1961  C  CE1 . HIS A  1 246 ? 56.506  39.010  15.013  1.00 22.90 ?  270  HIS A CE1 1 
ATOM   1962  N  NE2 . HIS A  1 246 ? 57.268  39.911  14.418  1.00 22.57 ?  270  HIS A NE2 1 
ATOM   1963  N  N   . GLU A  1 247 ? 51.733  40.807  10.346  1.00 23.96 ?  271  GLU A N   1 
ATOM   1964  C  CA  . GLU A  1 247 ? 51.184  41.286  9.075   1.00 24.72 ?  271  GLU A CA  1 
ATOM   1965  C  C   . GLU A  1 247 ? 51.140  42.803  9.000   1.00 24.55 ?  271  GLU A C   1 
ATOM   1966  O  O   . GLU A  1 247 ? 51.200  43.371  7.908   1.00 24.68 ?  271  GLU A O   1 
ATOM   1967  C  CB  . GLU A  1 247 ? 49.781  40.722  8.831   1.00 25.20 ?  271  GLU A CB  1 
ATOM   1968  C  CG  . GLU A  1 247 ? 49.762  39.504  7.931   1.00 27.71 ?  271  GLU A CG  1 
ATOM   1969  C  CD  . GLU A  1 247 ? 48.513  38.664  8.103   1.00 31.47 ?  271  GLU A CD  1 
ATOM   1970  O  OE1 . GLU A  1 247 ? 48.641  37.420  8.111   1.00 33.45 ?  271  GLU A OE1 1 
ATOM   1971  O  OE2 . GLU A  1 247 ? 47.407  39.240  8.237   1.00 32.53 -1 271  GLU A OE2 1 
ATOM   1972  N  N   . PHE A  1 248 ? 51.030  43.448  10.162  1.00 24.29 ?  272  PHE A N   1 
ATOM   1973  C  CA  . PHE A  1 248 ? 50.927  44.909  10.258  1.00 24.23 ?  272  PHE A CA  1 
ATOM   1974  C  C   . PHE A  1 248 ? 50.029  45.494  9.163   1.00 24.10 ?  272  PHE A C   1 
ATOM   1975  O  O   . PHE A  1 248 ? 50.470  46.264  8.308   1.00 24.19 ?  272  PHE A O   1 
ATOM   1976  C  CB  . PHE A  1 248 ? 52.322  45.555  10.279  1.00 24.39 ?  272  PHE A CB  1 
ATOM   1977  C  CG  . PHE A  1 248 ? 53.146  45.166  11.480  1.00 23.88 ?  272  PHE A CG  1 
ATOM   1978  C  CD1 . PHE A  1 248 ? 52.876  45.714  12.733  1.00 23.39 ?  272  PHE A CD1 1 
ATOM   1979  C  CD2 . PHE A  1 248 ? 54.179  44.247  11.361  1.00 23.54 ?  272  PHE A CD2 1 
ATOM   1980  C  CE1 . PHE A  1 248 ? 53.627  45.354  13.852  1.00 22.99 ?  272  PHE A CE1 1 
ATOM   1981  C  CE2 . PHE A  1 248 ? 54.940  43.883  12.474  1.00 23.78 ?  272  PHE A CE2 1 
ATOM   1982  C  CZ  . PHE A  1 248 ? 54.658  44.439  13.723  1.00 23.25 ?  272  PHE A CZ  1 
ATOM   1983  N  N   . SER A  1 249 ? 48.763  45.094  9.203   1.00 23.74 ?  273  SER A N   1 
ATOM   1984  C  CA  . SER A  1 249 ? 47.780  45.474  8.201   1.00 23.33 ?  273  SER A CA  1 
ATOM   1985  C  C   . SER A  1 249 ? 46.994  46.712  8.636   1.00 23.16 ?  273  SER A C   1 
ATOM   1986  O  O   . SER A  1 249 ? 46.346  46.710  9.687   1.00 22.82 ?  273  SER A O   1 
ATOM   1987  C  CB  . SER A  1 249 ? 46.832  44.298  7.949   1.00 23.28 ?  273  SER A CB  1 
ATOM   1988  O  OG  . SER A  1 249 ? 45.747  44.672  7.120   1.00 23.36 ?  273  SER A OG  1 
ATOM   1989  N  N   . ALA A  1 250 ? 47.057  47.764  7.821   1.00 22.95 ?  274  ALA A N   1 
ATOM   1990  C  CA  . ALA A  1 250 ? 46.286  48.984  8.061   1.00 22.99 ?  274  ALA A CA  1 
ATOM   1991  C  C   . ALA A  1 250 ? 44.780  48.718  8.007   1.00 22.96 ?  274  ALA A C   1 
ATOM   1992  O  O   . ALA A  1 250 ? 44.014  49.310  8.774   1.00 23.06 ?  274  ALA A O   1 
ATOM   1993  C  CB  . ALA A  1 250 ? 46.673  50.070  7.061   1.00 23.05 ?  274  ALA A CB  1 
ATOM   1994  N  N   . ALA A  1 251 ? 44.372  47.828  7.102   1.00 22.71 ?  275  ALA A N   1 
ATOM   1995  C  CA  . ALA A  1 251 ? 42.974  47.416  6.971   1.00 22.75 ?  275  ALA A CA  1 
ATOM   1996  C  C   . ALA A  1 251 ? 42.426  46.847  8.278   1.00 22.70 ?  275  ALA A C   1 
ATOM   1997  O  O   . ALA A  1 251 ? 41.332  47.207  8.705   1.00 22.84 ?  275  ALA A O   1 
ATOM   1998  C  CB  . ALA A  1 251 ? 42.822  46.395  5.843   1.00 22.75 ?  275  ALA A CB  1 
ATOM   1999  N  N   . GLU A  1 252 ? 43.201  45.960  8.899   1.00 22.51 ?  276  GLU A N   1 
ATOM   2000  C  CA  . GLU A  1 252 ? 42.854  45.350  10.176  1.00 22.25 ?  276  GLU A CA  1 
ATOM   2001  C  C   . GLU A  1 252 ? 42.637  46.394  11.283  1.00 22.14 ?  276  GLU A C   1 
ATOM   2002  O  O   . GLU A  1 252 ? 41.681  46.295  12.060  1.00 21.97 ?  276  GLU A O   1 
ATOM   2003  C  CB  . GLU A  1 252 ? 43.950  44.353  10.572  1.00 22.27 ?  276  GLU A CB  1 
ATOM   2004  C  CG  . GLU A  1 252 ? 43.865  43.810  11.996  1.00 22.35 ?  276  GLU A CG  1 
ATOM   2005  C  CD  . GLU A  1 252 ? 45.117  43.056  12.400  1.00 22.65 ?  276  GLU A CD  1 
ATOM   2006  O  OE1 . GLU A  1 252 ? 45.702  42.362  11.540  1.00 22.49 ?  276  GLU A OE1 1 
ATOM   2007  O  OE2 . GLU A  1 252 ? 45.513  43.148  13.580  1.00 21.79 -1 276  GLU A OE2 1 
ATOM   2008  N  N   . SER A  1 253 ? 43.522  47.390  11.345  1.00 21.87 ?  277  SER A N   1 
ATOM   2009  C  CA  . SER A  1 253 ? 43.434  48.441  12.363  1.00 21.77 ?  277  SER A CA  1 
ATOM   2010  C  C   . SER A  1 253 ? 42.239  49.377  12.167  1.00 21.48 ?  277  SER A C   1 
ATOM   2011  O  O   . SER A  1 253 ? 41.827  50.055  13.103  1.00 21.30 ?  277  SER A O   1 
ATOM   2012  C  CB  . SER A  1 253 ? 44.732  49.252  12.426  1.00 21.67 ?  277  SER A CB  1 
ATOM   2013  O  OG  . SER A  1 253 ? 45.048  49.806  11.164  1.00 22.55 ?  277  SER A OG  1 
ATOM   2014  N  N   . ARG A  1 254 ? 41.695  49.415  10.950  1.00 21.52 ?  278  ARG A N   1 
ATOM   2015  C  CA  . ARG A  1 254 ? 40.516  50.230  10.652  1.00 21.53 ?  278  ARG A CA  1 
ATOM   2016  C  C   . ARG A  1 254 ? 39.214  49.550  11.076  1.00 21.53 ?  278  ARG A C   1 
ATOM   2017  O  O   . ARG A  1 254 ? 38.180  50.205  11.199  1.00 21.56 ?  278  ARG A O   1 
ATOM   2018  C  CB  . ARG A  1 254 ? 40.459  50.587  9.164   1.00 21.59 ?  278  ARG A CB  1 
ATOM   2019  C  CG  . ARG A  1 254 ? 41.549  51.541  8.715   1.00 21.68 ?  278  ARG A CG  1 
ATOM   2020  C  CD  . ARG A  1 254 ? 41.468  51.825  7.222   1.00 21.23 ?  278  ARG A CD  1 
ATOM   2021  N  NE  . ARG A  1 254 ? 42.671  52.516  6.757   1.00 21.08 ?  278  ARG A NE  1 
ATOM   2022  C  CZ  . ARG A  1 254 ? 43.566  52.004  5.916   1.00 20.92 ?  278  ARG A CZ  1 
ATOM   2023  N  NH1 . ARG A  1 254 ? 43.402  50.787  5.405   1.00 19.67 ?  278  ARG A NH1 1 
ATOM   2024  N  NH2 . ARG A  1 254 ? 44.625  52.724  5.571   1.00 21.33 ?  278  ARG A NH2 1 
ATOM   2025  N  N   . LYS A  1 255 ? 39.268  48.237  11.284  1.00 21.49 ?  279  LYS A N   1 
ATOM   2026  C  CA  . LYS A  1 255 ? 38.094  47.466  11.694  1.00 21.37 ?  279  LYS A CA  1 
ATOM   2027  C  C   . LYS A  1 255 ? 37.825  47.660  13.187  1.00 21.14 ?  279  LYS A C   1 
ATOM   2028  O  O   . LYS A  1 255 ? 38.767  47.708  13.980  1.00 21.10 ?  279  LYS A O   1 
ATOM   2029  C  CB  . LYS A  1 255 ? 38.282  45.983  11.351  1.00 21.37 ?  279  LYS A CB  1 
ATOM   2030  C  CG  . LYS A  1 255 ? 38.393  45.717  9.850   1.00 21.73 ?  279  LYS A CG  1 
ATOM   2031  C  CD  . LYS A  1 255 ? 38.584  44.238  9.527   1.00 22.18 ?  279  LYS A CD  1 
ATOM   2032  C  CE  . LYS A  1 255 ? 38.677  44.022  8.017   1.00 22.05 ?  279  LYS A CE  1 
ATOM   2033  N  NZ  . LYS A  1 255 ? 38.721  42.573  7.645   1.00 23.07 ?  279  LYS A NZ  1 
ATOM   2034  N  N   . PRO A  1 256 ? 36.538  47.792  13.573  1.00 20.89 ?  280  PRO A N   1 
ATOM   2035  C  CA  . PRO A  1 256 ? 36.143  48.033  14.964  1.00 20.66 ?  280  PRO A CA  1 
ATOM   2036  C  C   . PRO A  1 256 ? 36.679  46.999  15.954  1.00 20.48 ?  280  PRO A C   1 
ATOM   2037  O  O   . PRO A  1 256 ? 36.977  47.343  17.103  1.00 20.18 ?  280  PRO A O   1 
ATOM   2038  C  CB  . PRO A  1 256 ? 34.614  47.964  14.906  1.00 20.72 ?  280  PRO A CB  1 
ATOM   2039  C  CG  . PRO A  1 256 ? 34.284  48.370  13.520  1.00 20.96 ?  280  PRO A CG  1 
ATOM   2040  C  CD  . PRO A  1 256 ? 35.369  47.792  12.672  1.00 20.75 ?  280  PRO A CD  1 
ATOM   2041  N  N   . GLU A  1 257 ? 36.801  45.751  15.500  1.00 20.27 ?  281  GLU A N   1 
ATOM   2042  C  CA  . GLU A  1 257 ? 37.371  44.655  16.296  1.00 20.19 ?  281  GLU A CA  1 
ATOM   2043  C  C   . GLU A  1 257 ? 38.777  44.962  16.838  1.00 20.05 ?  281  GLU A C   1 
ATOM   2044  O  O   . GLU A  1 257 ? 39.157  44.471  17.906  1.00 20.03 ?  281  GLU A O   1 
ATOM   2045  C  CB  . GLU A  1 257 ? 37.415  43.363  15.464  1.00 20.27 ?  281  GLU A CB  1 
ATOM   2046  C  CG  . GLU A  1 257 ? 36.054  42.693  15.188  1.00 20.44 ?  281  GLU A CG  1 
ATOM   2047  C  CD  . GLU A  1 257 ? 35.261  43.335  14.050  1.00 21.57 ?  281  GLU A CD  1 
ATOM   2048  O  OE1 . GLU A  1 257 ? 35.810  44.191  13.317  1.00 20.48 ?  281  GLU A OE1 1 
ATOM   2049  O  OE2 . GLU A  1 257 ? 34.075  42.965  13.879  1.00 22.91 -1 281  GLU A OE2 1 
ATOM   2050  N  N   . ALA A  1 258 ? 39.540  45.771  16.101  1.00 19.71 ?  282  ALA A N   1 
ATOM   2051  C  CA  . ALA A  1 258 ? 40.911  46.137  16.490  1.00 19.69 ?  282  ALA A CA  1 
ATOM   2052  C  C   . ALA A  1 258 ? 40.998  46.869  17.835  1.00 19.47 ?  282  ALA A C   1 
ATOM   2053  O  O   . ALA A  1 258 ? 42.018  46.782  18.527  1.00 19.84 ?  282  ALA A O   1 
ATOM   2054  C  CB  . ALA A  1 258 ? 41.582  46.972  15.387  1.00 19.40 ?  282  ALA A CB  1 
ATOM   2055  N  N   . CYS A  1 259 ? 39.933  47.582  18.195  1.00 19.10 ?  283  CYS A N   1 
ATOM   2056  C  CA  . CYS A  1 259 ? 39.892  48.374  19.434  1.00 19.06 ?  283  CYS A CA  1 
ATOM   2057  C  C   . CYS A  1 259 ? 39.221  47.640  20.593  1.00 19.10 ?  283  CYS A C   1 
ATOM   2058  O  O   . CYS A  1 259 ? 39.231  48.131  21.723  1.00 19.16 ?  283  CYS A O   1 
ATOM   2059  C  CB  . CYS A  1 259 ? 39.127  49.685  19.204  1.00 18.89 ?  283  CYS A CB  1 
ATOM   2060  S  SG  . CYS A  1 259 ? 39.332  50.421  17.583  1.00 18.31 ?  283  CYS A SG  1 
ATOM   2061  N  N   . ALA A  1 260 ? 38.648  46.473  20.307  1.00 19.08 ?  284  ALA A N   1 
ATOM   2062  C  CA  . ALA A  1 260 ? 37.691  45.817  21.207  1.00 19.11 ?  284  ALA A CA  1 
ATOM   2063  C  C   . ALA A  1 260 ? 38.271  45.175  22.467  1.00 19.20 ?  284  ALA A C   1 
ATOM   2064  O  O   . ALA A  1 260 ? 37.647  45.223  23.527  1.00 19.52 ?  284  ALA A O   1 
ATOM   2065  C  CB  . ALA A  1 260 ? 36.872  44.798  20.436  1.00 19.06 ?  284  ALA A CB  1 
ATOM   2066  N  N   . THR A  1 261 ? 39.443  44.559  22.351  1.00 18.96 ?  285  THR A N   1 
ATOM   2067  C  CA  . THR A  1 261 ? 40.075  43.878  23.481  1.00 19.04 ?  285  THR A CA  1 
ATOM   2068  C  C   . THR A  1 261 ? 40.336  44.834  24.660  1.00 19.27 ?  285  THR A C   1 
ATOM   2069  O  O   . THR A  1 261 ? 40.202  44.454  25.829  1.00 19.24 ?  285  THR A O   1 
ATOM   2070  C  CB  . THR A  1 261 ? 41.379  43.151  23.034  1.00 19.10 ?  285  THR A CB  1 
ATOM   2071  O  OG1 . THR A  1 261 ? 41.111  42.363  21.864  1.00 18.86 ?  285  THR A OG1 1 
ATOM   2072  C  CG2 . THR A  1 261 ? 41.909  42.236  24.132  1.00 19.12 ?  285  THR A CG2 1 
ATOM   2073  N  N   . CYS A  1 262 ? 40.678  46.079  24.341  1.00 19.46 ?  286  CYS A N   1 
ATOM   2074  C  CA  . CYS A  1 262 ? 40.974  47.087  25.349  1.00 19.61 ?  286  CYS A CA  1 
ATOM   2075  C  C   . CYS A  1 262 ? 39.762  47.948  25.689  1.00 19.96 ?  286  CYS A C   1 
ATOM   2076  O  O   . CYS A  1 262 ? 39.496  48.219  26.863  1.00 20.12 ?  286  CYS A O   1 
ATOM   2077  C  CB  . CYS A  1 262 ? 42.116  47.985  24.879  1.00 19.69 ?  286  CYS A CB  1 
ATOM   2078  S  SG  . CYS A  1 262 ? 43.607  47.113  24.331  1.00 18.54 ?  286  CYS A SG  1 
ATOM   2079  N  N   . HIS A  1 263 ? 39.034  48.379  24.663  1.00 20.21 ?  287  HIS A N   1 
ATOM   2080  C  CA  . HIS A  1 263 ? 37.897  49.272  24.854  1.00 20.45 ?  287  HIS A CA  1 
ATOM   2081  C  C   . HIS A  1 263 ? 36.588  48.498  25.028  1.00 20.63 ?  287  HIS A C   1 
ATOM   2082  O  O   . HIS A  1 263 ? 35.665  48.587  24.209  1.00 20.79 ?  287  HIS A O   1 
ATOM   2083  C  CB  . HIS A  1 263 ? 37.815  50.281  23.714  1.00 20.58 ?  287  HIS A CB  1 
ATOM   2084  C  CG  . HIS A  1 263 ? 38.907  51.303  23.740  1.00 20.79 ?  287  HIS A CG  1 
ATOM   2085  N  ND1 . HIS A  1 263 ? 38.879  52.398  24.576  1.00 21.18 ?  287  HIS A ND1 1 
ATOM   2086  C  CD2 . HIS A  1 263 ? 40.060  51.394  23.036  1.00 20.39 ?  287  HIS A CD2 1 
ATOM   2087  C  CE1 . HIS A  1 263 ? 39.969  53.122  24.386  1.00 21.86 ?  287  HIS A CE1 1 
ATOM   2088  N  NE2 . HIS A  1 263 ? 40.703  52.535  23.457  1.00 21.99 ?  287  HIS A NE2 1 
ATOM   2089  N  N   . SER A  1 264 ? 36.537  47.733  26.111  1.00 20.51 ?  288  SER A N   1 
ATOM   2090  C  CA  . SER A  1 264 ? 35.373  46.939  26.477  1.00 20.62 ?  288  SER A CA  1 
ATOM   2091  C  C   . SER A  1 264 ? 35.359  46.758  27.990  1.00 20.56 ?  288  SER A C   1 
ATOM   2092  O  O   . SER A  1 264 ? 36.312  47.129  28.674  1.00 20.79 ?  288  SER A O   1 
ATOM   2093  C  CB  . SER A  1 264 ? 35.429  45.571  25.797  1.00 20.57 ?  288  SER A CB  1 
ATOM   2094  O  OG  . SER A  1 264 ? 36.645  44.902  26.103  1.00 20.18 ?  288  SER A OG  1 
ATOM   2095  N  N   . GLY A  1 265 ? 34.279  46.190  28.510  1.00 20.60 ?  289  GLY A N   1 
ATOM   2096  C  CA  . GLY A  1 265 ? 34.245  45.788  29.908  1.00 20.48 ?  289  GLY A CA  1 
ATOM   2097  C  C   . GLY A  1 265 ? 33.403  46.647  30.825  1.00 20.42 ?  289  GLY A C   1 
ATOM   2098  O  O   . GLY A  1 265 ? 32.766  47.614  30.394  1.00 20.21 ?  289  GLY A O   1 
ATOM   2099  N  N   . VAL A  1 266 ? 33.451  46.294  32.107  1.00 20.34 ?  290  VAL A N   1 
ATOM   2100  C  CA  . VAL A  1 266 ? 32.555  46.812  33.140  1.00 20.34 ?  290  VAL A CA  1 
ATOM   2101  C  C   . VAL A  1 266 ? 32.603  48.332  33.360  1.00 20.65 ?  290  VAL A C   1 
ATOM   2102  O  O   . VAL A  1 266 ? 31.632  48.906  33.845  1.00 20.66 ?  290  VAL A O   1 
ATOM   2103  C  CB  . VAL A  1 266 ? 32.768  46.039  34.485  1.00 20.35 ?  290  VAL A CB  1 
ATOM   2104  C  CG1 . VAL A  1 266 ? 34.008  46.541  35.234  1.00 19.88 ?  290  VAL A CG1 1 
ATOM   2105  C  CG2 . VAL A  1 266 ? 31.512  46.088  35.376  1.00 19.92 ?  290  VAL A CG2 1 
ATOM   2106  N  N   . ASP A  1 267 ? 33.714  48.978  32.998  1.00 20.93 ?  291  ASP A N   1 
ATOM   2107  C  CA  . ASP A  1 267 ? 33.878  50.414  33.254  1.00 21.16 ?  291  ASP A CA  1 
ATOM   2108  C  C   . ASP A  1 267 ? 34.085  51.278  32.002  1.00 21.06 ?  291  ASP A C   1 
ATOM   2109  O  O   . ASP A  1 267 ? 34.383  52.471  32.104  1.00 21.17 ?  291  ASP A O   1 
ATOM   2110  C  CB  . ASP A  1 267 ? 34.979  50.668  34.299  1.00 21.25 ?  291  ASP A CB  1 
ATOM   2111  C  CG  . ASP A  1 267 ? 36.362  50.277  33.815  1.00 22.22 ?  291  ASP A CG  1 
ATOM   2112  O  OD1 . ASP A  1 267 ? 36.481  49.391  32.943  1.00 23.74 ?  291  ASP A OD1 1 
ATOM   2113  O  OD2 . ASP A  1 267 ? 37.344  50.858  34.323  1.00 23.96 -1 291  ASP A OD2 1 
ATOM   2114  N  N   . HIS A  1 268 ? 33.929  50.664  30.832  1.00 20.99 ?  292  HIS A N   1 
ATOM   2115  C  CA  . HIS A  1 268 ? 33.936  51.356  29.537  1.00 20.94 ?  292  HIS A CA  1 
ATOM   2116  C  C   . HIS A  1 268 ? 33.599  50.346  28.447  1.00 20.76 ?  292  HIS A C   1 
ATOM   2117  O  O   . HIS A  1 268 ? 34.491  49.792  27.801  1.00 20.80 ?  292  HIS A O   1 
ATOM   2118  C  CB  . HIS A  1 268 ? 35.282  52.049  29.247  1.00 20.88 ?  292  HIS A CB  1 
ATOM   2119  C  CG  . HIS A  1 268 ? 36.479  51.264  29.683  1.00 21.53 ?  292  HIS A CG  1 
ATOM   2120  N  ND1 . HIS A  1 268 ? 36.889  50.112  29.045  1.00 22.35 ?  292  HIS A ND1 1 
ATOM   2121  C  CD2 . HIS A  1 268 ? 37.357  51.467  30.694  1.00 21.38 ?  292  HIS A CD2 1 
ATOM   2122  C  CE1 . HIS A  1 268 ? 37.967  49.639  29.644  1.00 22.12 ?  292  HIS A CE1 1 
ATOM   2123  N  NE2 . HIS A  1 268 ? 38.270  50.441  30.650  1.00 22.71 ?  292  HIS A NE2 1 
ATOM   2124  N  N   . ASN A  1 269 ? 32.304  50.112  28.251  1.00 20.62 ?  293  ASN A N   1 
ATOM   2125  C  CA  . ASN A  1 269 ? 31.834  49.053  27.357  1.00 20.45 ?  293  ASN A CA  1 
ATOM   2126  C  C   . ASN A  1 269 ? 31.613  49.528  25.918  1.00 20.32 ?  293  ASN A C   1 
ATOM   2127  O  O   . ASN A  1 269 ? 30.562  49.278  25.318  1.00 20.22 ?  293  ASN A O   1 
ATOM   2128  C  CB  . ASN A  1 269 ? 30.577  48.373  27.931  1.00 20.35 ?  293  ASN A CB  1 
ATOM   2129  C  CG  . ASN A  1 269 ? 29.366  49.299  27.984  1.00 20.59 ?  293  ASN A CG  1 
ATOM   2130  O  OD1 . ASN A  1 269 ? 29.496  50.522  28.020  1.00 20.75 ?  293  ASN A OD1 1 
ATOM   2131  N  ND2 . ASN A  1 269 ? 28.174  48.708  28.000  1.00 20.92 ?  293  ASN A ND2 1 
ATOM   2132  N  N   . ASN A  1 270 ? 32.626  50.199  25.373  1.00 20.12 ?  294  ASN A N   1 
ATOM   2133  C  CA  . ASN A  1 270 ? 32.548  50.810  24.047  1.00 20.05 ?  294  ASN A CA  1 
ATOM   2134  C  C   . ASN A  1 270 ? 32.269  49.813  22.919  1.00 19.98 ?  294  ASN A C   1 
ATOM   2135  O  O   . ASN A  1 270 ? 31.422  50.066  22.065  1.00 19.82 ?  294  ASN A O   1 
ATOM   2136  C  CB  . ASN A  1 270 ? 33.805  51.643  23.756  1.00 19.90 ?  294  ASN A CB  1 
ATOM   2137  C  CG  . ASN A  1 270 ? 34.108  52.648  24.855  1.00 19.92 ?  294  ASN A CG  1 
ATOM   2138  O  OD1 . ASN A  1 270 ? 34.504  52.275  25.960  1.00 19.28 ?  294  ASN A OD1 1 
ATOM   2139  N  ND2 . ASN A  1 270 ? 33.926  53.931  24.555  1.00 18.88 ?  294  ASN A ND2 1 
ATOM   2140  N  N   . TRP A  1 271 ? 32.971  48.681  22.935  1.00 20.05 ?  295  TRP A N   1 
ATOM   2141  C  CA  . TRP A  1 271 ? 32.736  47.603  21.968  1.00 20.16 ?  295  TRP A CA  1 
ATOM   2142  C  C   . TRP A  1 271 ? 31.310  47.065  22.046  1.00 20.23 ?  295  TRP A C   1 
ATOM   2143  O  O   . TRP A  1 271 ? 30.663  46.874  21.018  1.00 20.45 ?  295  TRP A O   1 
ATOM   2144  C  CB  . TRP A  1 271 ? 33.733  46.458  22.178  1.00 20.11 ?  295  TRP A CB  1 
ATOM   2145  C  CG  . TRP A  1 271 ? 33.395  45.201  21.416  1.00 19.95 ?  295  TRP A CG  1 
ATOM   2146  C  CD1 . TRP A  1 271 ? 32.961  44.018  21.942  1.00 19.63 ?  295  TRP A CD1 1 
ATOM   2147  C  CD2 . TRP A  1 271 ? 33.462  45.008  19.995  1.00 19.68 ?  295  TRP A CD2 1 
ATOM   2148  N  NE1 . TRP A  1 271 ? 32.763  43.097  20.941  1.00 19.82 ?  295  TRP A NE1 1 
ATOM   2149  C  CE2 . TRP A  1 271 ? 33.064  43.676  19.736  1.00 20.03 ?  295  TRP A CE2 1 
ATOM   2150  C  CE3 . TRP A  1 271 ? 33.834  45.826  18.916  1.00 20.32 ?  295  TRP A CE3 1 
ATOM   2151  C  CZ2 . TRP A  1 271 ? 33.015  43.142  18.440  1.00 20.29 ?  295  TRP A CZ2 1 
ATOM   2152  C  CZ3 . TRP A  1 271 ? 33.786  45.293  17.623  1.00 20.33 ?  295  TRP A CZ3 1 
ATOM   2153  C  CH2 . TRP A  1 271 ? 33.379  43.963  17.402  1.00 20.46 ?  295  TRP A CH2 1 
ATOM   2154  N  N   . GLU A  1 272 ? 30.832  46.825  23.266  1.00 20.30 ?  296  GLU A N   1 
ATOM   2155  C  CA  . GLU A  1 272 ? 29.489  46.294  23.490  1.00 20.59 ?  296  GLU A CA  1 
ATOM   2156  C  C   . GLU A  1 272 ? 28.415  47.296  23.060  1.00 20.67 ?  296  GLU A C   1 
ATOM   2157  O  O   . GLU A  1 272 ? 27.445  46.921  22.401  1.00 21.08 ?  296  GLU A O   1 
ATOM   2158  C  CB  . GLU A  1 272 ? 29.291  45.876  24.953  1.00 20.58 ?  296  GLU A CB  1 
ATOM   2159  C  CG  . GLU A  1 272 ? 30.275  44.804  25.469  1.00 21.04 ?  296  GLU A CG  1 
ATOM   2160  C  CD  . GLU A  1 272 ? 31.550  45.390  26.081  1.00 21.01 ?  296  GLU A CD  1 
ATOM   2161  O  OE1 . GLU A  1 272 ? 32.118  46.344  25.511  1.00 20.18 ?  296  GLU A OE1 1 
ATOM   2162  O  OE2 . GLU A  1 272 ? 31.993  44.888  27.141  1.00 21.74 -1 296  GLU A OE2 1 
ATOM   2163  N  N   . ALA A  1 273 ? 28.604  48.565  23.415  1.00 20.57 ?  297  ALA A N   1 
ATOM   2164  C  CA  . ALA A  1 273 ? 27.662  49.625  23.050  1.00 20.32 ?  297  ALA A CA  1 
ATOM   2165  C  C   . ALA A  1 273 ? 27.634  49.851  21.539  1.00 20.24 ?  297  ALA A C   1 
ATOM   2166  O  O   . ALA A  1 273 ? 26.566  49.845  20.928  1.00 20.00 ?  297  ALA A O   1 
ATOM   2167  C  CB  . ALA A  1 273 ? 27.995  50.922  23.786  1.00 20.06 ?  297  ALA A CB  1 
ATOM   2168  N  N   . TYR A  1 274 ? 28.813  50.033  20.946  1.00 20.22 ?  298  TYR A N   1 
ATOM   2169  C  CA  . TYR A  1 274 ? 28.930  50.256  19.505  1.00 20.26 ?  298  TYR A CA  1 
ATOM   2170  C  C   . TYR A  1 274 ? 28.322  49.143  18.658  1.00 20.17 ?  298  TYR A C   1 
ATOM   2171  O  O   . TYR A  1 274 ? 27.568  49.428  17.723  1.00 20.33 ?  298  TYR A O   1 
ATOM   2172  C  CB  . TYR A  1 274 ? 30.390  50.482  19.088  1.00 20.15 ?  298  TYR A CB  1 
ATOM   2173  C  CG  . TYR A  1 274 ? 30.591  50.454  17.590  1.00 20.33 ?  298  TYR A CG  1 
ATOM   2174  C  CD1 . TYR A  1 274 ? 30.203  51.533  16.801  1.00 19.83 ?  298  TYR A CD1 1 
ATOM   2175  C  CD2 . TYR A  1 274 ? 31.153  49.339  16.957  1.00 20.35 ?  298  TYR A CD2 1 
ATOM   2176  C  CE1 . TYR A  1 274 ? 30.369  51.511  15.428  1.00 19.76 ?  298  TYR A CE1 1 
ATOM   2177  C  CE2 . TYR A  1 274 ? 31.324  49.312  15.578  1.00 19.82 ?  298  TYR A CE2 1 
ATOM   2178  C  CZ  . TYR A  1 274 ? 30.932  50.405  14.823  1.00 20.05 ?  298  TYR A CZ  1 
ATOM   2179  O  OH  . TYR A  1 274 ? 31.095  50.400  13.454  1.00 21.01 ?  298  TYR A OH  1 
ATOM   2180  N  N   . THR A  1 275 ? 28.659  47.889  18.967  1.00 20.18 ?  299  THR A N   1 
ATOM   2181  C  CA  . THR A  1 275 ? 28.187  46.751  18.164  1.00 20.35 ?  299  THR A CA  1 
ATOM   2182  C  C   . THR A  1 275 ? 26.683  46.549  18.236  1.00 20.15 ?  299  THR A C   1 
ATOM   2183  O  O   . THR A  1 275 ? 26.089  46.048  17.290  1.00 20.14 ?  299  THR A O   1 
ATOM   2184  C  CB  . THR A  1 275 ? 28.876  45.411  18.526  1.00 20.46 ?  299  THR A CB  1 
ATOM   2185  O  OG1 . THR A  1 275 ? 28.727  45.142  19.922  1.00 21.49 ?  299  THR A OG1 1 
ATOM   2186  C  CG2 . THR A  1 275 ? 30.330  45.452  18.175  1.00 20.74 ?  299  THR A CG2 1 
ATOM   2187  N  N   . MET A  1 276 ? 26.079  46.929  19.360  1.00 20.25 ?  300  MET A N   1 
ATOM   2188  C  CA  . MET A  1 276 ? 24.638  46.770  19.556  1.00 20.28 ?  300  MET A CA  1 
ATOM   2189  C  C   . MET A  1 276 ? 23.828  47.912  18.936  1.00 20.24 ?  300  MET A C   1 
ATOM   2190  O  O   . MET A  1 276 ? 22.657  47.731  18.581  1.00 20.19 ?  300  MET A O   1 
ATOM   2191  C  CB  . MET A  1 276 ? 24.305  46.624  21.043  1.00 20.46 ?  300  MET A CB  1 
ATOM   2192  C  CG  . MET A  1 276 ? 24.691  45.269  21.656  1.00 20.81 ?  300  MET A CG  1 
ATOM   2193  S  SD  . MET A  1 276 ? 24.128  43.849  20.703  1.00 22.01 ?  300  MET A SD  1 
ATOM   2194  C  CE  . MET A  1 276 ? 22.347  44.040  20.809  1.00 21.05 ?  300  MET A CE  1 
ATOM   2195  N  N   . SER A  1 277 ? 24.457  49.080  18.808  1.00 20.11 ?  301  SER A N   1 
ATOM   2196  C  CA  . SER A  1 277 ? 23.849  50.224  18.133  1.00 20.16 ?  301  SER A CA  1 
ATOM   2197  C  C   . SER A  1 277 ? 23.594  49.889  16.663  1.00 20.26 ?  301  SER A C   1 
ATOM   2198  O  O   . SER A  1 277 ? 24.167  48.930  16.134  1.00 20.01 ?  301  SER A O   1 
ATOM   2199  C  CB  . SER A  1 277 ? 24.751  51.458  18.247  1.00 19.93 ?  301  SER A CB  1 
ATOM   2200  O  OG  . SER A  1 277 ? 25.762  51.481  17.247  1.00 20.01 ?  301  SER A OG  1 
ATOM   2201  N  N   . LYS A  1 278 ? 22.732  50.669  16.011  1.00 20.54 ?  302  LYS A N   1 
ATOM   2202  C  CA  . LYS A  1 278 ? 22.496  50.504  14.576  1.00 20.83 ?  302  LYS A CA  1 
ATOM   2203  C  C   . LYS A  1 278 ? 23.789  50.658  13.794  1.00 20.72 ?  302  LYS A C   1 
ATOM   2204  O  O   . LYS A  1 278 ? 24.050  49.890  12.863  1.00 20.73 ?  302  LYS A O   1 
ATOM   2205  C  CB  . LYS A  1 278 ? 21.458  51.501  14.057  1.00 21.10 ?  302  LYS A CB  1 
ATOM   2206  C  CG  . LYS A  1 278 ? 20.068  50.928  13.911  1.00 22.31 ?  302  LYS A CG  1 
ATOM   2207  C  CD  . LYS A  1 278 ? 20.023  49.830  12.841  1.00 22.65 ?  302  LYS A CD  1 
ATOM   2208  C  CE  . LYS A  1 278 ? 18.694  49.114  12.914  1.00 22.63 ?  302  LYS A CE  1 
ATOM   2209  N  NZ  . LYS A  1 278 ? 18.738  47.743  12.349  1.00 23.09 ?  302  LYS A NZ  1 
ATOM   2210  N  N   . HIS A  1 279 ? 24.593  51.649  14.185  1.00 20.66 ?  303  HIS A N   1 
ATOM   2211  C  CA  . HIS A  1 279 ? 25.902  51.891  13.575  1.00 20.65 ?  303  HIS A CA  1 
ATOM   2212  C  C   . HIS A  1 279 ? 26.715  50.600  13.494  1.00 20.57 ?  303  HIS A C   1 
ATOM   2213  O  O   . HIS A  1 279 ? 27.193  50.227  12.417  1.00 20.84 ?  303  HIS A O   1 
ATOM   2214  C  CB  . HIS A  1 279 ? 26.688  52.961  14.353  1.00 20.45 ?  303  HIS A CB  1 
ATOM   2215  C  CG  . HIS A  1 279 ? 26.156  54.355  14.196  1.00 20.54 ?  303  HIS A CG  1 
ATOM   2216  N  ND1 . HIS A  1 279 ? 26.350  55.332  15.150  1.00 20.73 ?  303  HIS A ND1 1 
ATOM   2217  C  CD2 . HIS A  1 279 ? 25.453  54.942  13.197  1.00 20.27 ?  303  HIS A CD2 1 
ATOM   2218  C  CE1 . HIS A  1 279 ? 25.795  56.460  14.743  1.00 20.80 ?  303  HIS A CE1 1 
ATOM   2219  N  NE2 . HIS A  1 279 ? 25.239  56.251  13.563  1.00 21.16 ?  303  HIS A NE2 1 
ATOM   2220  N  N   . GLY A  1 280 ? 26.838  49.912  14.628  1.00 20.42 ?  304  GLY A N   1 
ATOM   2221  C  CA  . GLY A  1 280 ? 27.651  48.702  14.736  1.00 20.47 ?  304  GLY A CA  1 
ATOM   2222  C  C   . GLY A  1 280 ? 27.059  47.488  14.050  1.00 20.55 ?  304  GLY A C   1 
ATOM   2223  O  O   . GLY A  1 280 ? 27.785  46.683  13.464  1.00 20.44 ?  304  GLY A O   1 
ATOM   2224  N  N   . LYS A  1 281 ? 25.738  47.356  14.121  1.00 20.75 ?  305  LYS A N   1 
ATOM   2225  C  CA  . LYS A  1 281 ? 25.038  46.254  13.463  1.00 20.99 ?  305  LYS A CA  1 
ATOM   2226  C  C   . LYS A  1 281 ? 25.144  46.347  11.942  1.00 21.31 ?  305  LYS A C   1 
ATOM   2227  O  O   . LYS A  1 281 ? 25.303  45.329  11.259  1.00 21.15 ?  305  LYS A O   1 
ATOM   2228  C  CB  . LYS A  1 281 ? 23.582  46.184  13.926  1.00 20.88 ?  305  LYS A CB  1 
ATOM   2229  C  CG  . LYS A  1 281 ? 23.415  45.569  15.323  1.00 20.82 ?  305  LYS A CG  1 
ATOM   2230  C  CD  . LYS A  1 281 ? 23.553  44.044  15.283  1.00 19.91 ?  305  LYS A CD  1 
ATOM   2231  C  CE  . LYS A  1 281 ? 23.844  43.435  16.652  1.00 19.31 ?  305  LYS A CE  1 
ATOM   2232  N  NZ  . LYS A  1 281 ? 25.279  43.525  17.042  1.00 19.82 ?  305  LYS A NZ  1 
ATOM   2233  N  N   . LEU A  1 282 ? 25.069  47.575  11.429  1.00 21.69 ?  306  LEU A N   1 
ATOM   2234  C  CA  . LEU A  1 282 ? 25.300  47.856  10.016  1.00 22.49 ?  306  LEU A CA  1 
ATOM   2235  C  C   . LEU A  1 282 ? 26.739  47.575  9.609   1.00 22.68 ?  306  LEU A C   1 
ATOM   2236  O  O   . LEU A  1 282 ? 26.979  47.052  8.529   1.00 22.74 ?  306  LEU A O   1 
ATOM   2237  C  CB  . LEU A  1 282 ? 24.948  49.309  9.682   1.00 22.52 ?  306  LEU A CB  1 
ATOM   2238  C  CG  . LEU A  1 282 ? 23.467  49.596  9.458   1.00 23.77 ?  306  LEU A CG  1 
ATOM   2239  C  CD1 . LEU A  1 282 ? 23.204  51.090  9.533   1.00 24.48 ?  306  LEU A CD1 1 
ATOM   2240  C  CD2 . LEU A  1 282 ? 23.030  49.024  8.115   1.00 25.05 ?  306  LEU A CD2 1 
ATOM   2241  N  N   . ALA A  1 283 ? 27.688  47.933  10.474  1.00 23.23 ?  307  ALA A N   1 
ATOM   2242  C  CA  . ALA A  1 283 ? 29.096  47.608  10.254  1.00 23.89 ?  307  ALA A CA  1 
ATOM   2243  C  C   . ALA A  1 283 ? 29.300  46.097  10.164  1.00 24.40 ?  307  ALA A C   1 
ATOM   2244  O  O   . ALA A  1 283 ? 30.060  45.628  9.318   1.00 24.19 ?  307  ALA A O   1 
ATOM   2245  C  CB  . ALA A  1 283 ? 29.969  48.201  11.350  1.00 23.59 ?  307  ALA A CB  1 
ATOM   2246  N  N   . GLU A  1 284 ? 28.616  45.351  11.036  1.00 25.04 ?  308  GLU A N   1 
ATOM   2247  C  CA  . GLU A  1 284 ? 28.630  43.885  10.997  1.00 25.92 ?  308  GLU A CA  1 
ATOM   2248  C  C   . GLU A  1 284 ? 28.017  43.358  9.688   1.00 26.25 ?  308  GLU A C   1 
ATOM   2249  O  O   . GLU A  1 284 ? 28.592  42.488  9.039   1.00 26.45 ?  308  GLU A O   1 
ATOM   2250  C  CB  . GLU A  1 284 ? 27.920  43.288  12.230  1.00 26.07 ?  308  GLU A CB  1 
ATOM   2251  C  CG  . GLU A  1 284 ? 28.694  43.469  13.550  1.00 27.19 ?  308  GLU A CG  1 
ATOM   2252  C  CD  . GLU A  1 284 ? 27.938  43.017  14.807  1.00 29.64 ?  308  GLU A CD  1 
ATOM   2253  O  OE1 . GLU A  1 284 ? 26.756  42.612  14.724  1.00 29.90 ?  308  GLU A OE1 1 
ATOM   2254  O  OE2 . GLU A  1 284 ? 28.544  43.071  15.902  1.00 31.36 -1 308  GLU A OE2 1 
ATOM   2255  N  N   . MET A  1 285 ? 26.871  43.916  9.298   1.00 26.59 ?  309  MET A N   1 
ATOM   2256  C  CA  . MET A  1 285 ? 26.155  43.488  8.089   1.00 27.03 ?  309  MET A CA  1 
ATOM   2257  C  C   . MET A  1 285 ? 26.837  43.864  6.771   1.00 27.57 ?  309  MET A C   1 
ATOM   2258  O  O   . MET A  1 285 ? 26.739  43.123  5.789   1.00 27.65 ?  309  MET A O   1 
ATOM   2259  C  CB  . MET A  1 285 ? 24.714  44.017  8.097   1.00 26.76 ?  309  MET A CB  1 
ATOM   2260  C  CG  . MET A  1 285 ? 23.798  43.301  9.093   1.00 26.34 ?  309  MET A CG  1 
ATOM   2261  S  SD  . MET A  1 285 ? 22.074  43.839  9.067   1.00 24.76 ?  309  MET A SD  1 
ATOM   2262  C  CE  . MET A  1 285 ? 22.171  45.438  9.880   1.00 25.90 ?  309  MET A CE  1 
ATOM   2263  N  N   . ASN A  1 286 ? 27.523  45.008  6.757   1.00 28.18 ?  310  ASN A N   1 
ATOM   2264  C  CA  . ASN A  1 286 ? 28.076  45.582  5.523   1.00 29.08 ?  310  ASN A CA  1 
ATOM   2265  C  C   . ASN A  1 286 ? 29.588  45.438  5.331   1.00 29.53 ?  310  ASN A C   1 
ATOM   2266  O  O   . ASN A  1 286 ? 30.132  45.922  4.336   1.00 29.72 ?  310  ASN A O   1 
ATOM   2267  C  CB  . ASN A  1 286 ? 27.698  47.066  5.416   1.00 29.14 ?  310  ASN A CB  1 
ATOM   2268  C  CG  . ASN A  1 286 ? 26.195  47.290  5.334   1.00 29.54 ?  310  ASN A CG  1 
ATOM   2269  O  OD1 . ASN A  1 286 ? 25.455  46.461  4.800   1.00 30.48 ?  310  ASN A OD1 1 
ATOM   2270  N  ND2 . ASN A  1 286 ? 25.740  48.419  5.859   1.00 29.67 ?  310  ASN A ND2 1 
ATOM   2271  N  N   . ARG A  1 287 ? 30.259  44.778  6.273   1.00 29.95 ?  311  ARG A N   1 
ATOM   2272  C  CA  . ARG A  1 287 ? 31.722  44.680  6.256   1.00 30.75 ?  311  ARG A CA  1 
ATOM   2273  C  C   . ARG A  1 287 ? 32.330  44.118  4.962   1.00 30.86 ?  311  ARG A C   1 
ATOM   2274  O  O   . ARG A  1 287 ? 33.416  44.538  4.560   1.00 30.69 ?  311  ARG A O   1 
ATOM   2275  C  CB  . ARG A  1 287 ? 32.244  43.908  7.472   1.00 30.78 ?  311  ARG A CB  1 
ATOM   2276  C  CG  . ARG A  1 287 ? 31.622  42.543  7.683   1.00 32.22 ?  311  ARG A CG  1 
ATOM   2277  C  CD  . ARG A  1 287 ? 32.429  41.740  8.686   1.00 34.28 ?  311  ARG A CD  1 
ATOM   2278  N  NE  . ARG A  1 287 ? 31.576  40.852  9.465   1.00 36.60 ?  311  ARG A NE  1 
ATOM   2279  C  CZ  . ARG A  1 287 ? 31.345  40.974  10.770  1.00 37.53 ?  311  ARG A CZ  1 
ATOM   2280  N  NH1 . ARG A  1 287 ? 31.919  41.944  11.476  1.00 37.92 ?  311  ARG A NH1 1 
ATOM   2281  N  NH2 . ARG A  1 287 ? 30.544  40.109  11.373  1.00 38.13 ?  311  ARG A NH2 1 
ATOM   2282  N  N   . ASP A  1 288 ? 31.629  43.184  4.320   1.00 31.16 ?  312  ASP A N   1 
ATOM   2283  C  CA  . ASP A  1 288 ? 32.106  42.572  3.075   1.00 31.57 ?  312  ASP A CA  1 
ATOM   2284  C  C   . ASP A  1 288 ? 31.915  43.459  1.855   1.00 31.30 ?  312  ASP A C   1 
ATOM   2285  O  O   . ASP A  1 288 ? 32.537  43.227  0.819   1.00 31.39 ?  312  ASP A O   1 
ATOM   2286  C  CB  . ASP A  1 288 ? 31.419  41.232  2.830   1.00 31.95 ?  312  ASP A CB  1 
ATOM   2287  C  CG  . ASP A  1 288 ? 31.557  40.297  3.994   1.00 33.70 ?  312  ASP A CG  1 
ATOM   2288  O  OD1 . ASP A  1 288 ? 30.653  39.452  4.164   1.00 36.81 ?  312  ASP A OD1 1 
ATOM   2289  O  OD2 . ASP A  1 288 ? 32.549  40.432  4.750   1.00 35.13 -1 312  ASP A OD2 1 
ATOM   2290  N  N   . LYS A  1 289 ? 31.051  44.462  1.970   1.00 31.02 ?  313  LYS A N   1 
ATOM   2291  C  CA  . LYS A  1 289 ? 30.801  45.369  0.851   1.00 30.88 ?  313  LYS A CA  1 
ATOM   2292  C  C   . LYS A  1 289 ? 31.797  46.525  0.824   1.00 30.09 ?  313  LYS A C   1 
ATOM   2293  O  O   . LYS A  1 289 ? 31.926  47.216  -0.186  1.00 30.38 ?  313  LYS A O   1 
ATOM   2294  C  CB  . LYS A  1 289 ? 29.356  45.879  0.873   1.00 31.09 ?  313  LYS A CB  1 
ATOM   2295  C  CG  . LYS A  1 289 ? 28.324  44.785  0.604   1.00 32.65 ?  313  LYS A CG  1 
ATOM   2296  C  CD  . LYS A  1 289 ? 26.920  45.353  0.451   1.00 34.84 ?  313  LYS A CD  1 
ATOM   2297  C  CE  . LYS A  1 289 ? 25.870  44.242  0.358   1.00 36.23 ?  313  LYS A CE  1 
ATOM   2298  N  NZ  . LYS A  1 289 ? 25.981  43.431  -0.892  1.00 36.90 ?  313  LYS A NZ  1 
ATOM   2299  N  N   . TRP A  1 290 ? 32.509  46.715  1.931   1.00 29.07 ?  314  TRP A N   1 
ATOM   2300  C  CA  . TRP A  1 290 ? 33.435  47.835  2.072   1.00 27.94 ?  314  TRP A CA  1 
ATOM   2301  C  C   . TRP A  1 290 ? 34.868  47.463  1.707   1.00 27.42 ?  314  TRP A C   1 
ATOM   2302  O  O   . TRP A  1 290 ? 35.288  46.320  1.892   1.00 27.30 ?  314  TRP A O   1 
ATOM   2303  C  CB  . TRP A  1 290 ? 33.401  48.386  3.501   1.00 27.66 ?  314  TRP A CB  1 
ATOM   2304  C  CG  . TRP A  1 290 ? 32.044  48.849  3.981   1.00 27.13 ?  314  TRP A CG  1 
ATOM   2305  C  CD1 . TRP A  1 290 ? 30.933  49.094  3.220   1.00 26.37 ?  314  TRP A CD1 1 
ATOM   2306  C  CD2 . TRP A  1 290 ? 31.681  49.165  5.330   1.00 25.81 ?  314  TRP A CD2 1 
ATOM   2307  N  NE1 . TRP A  1 290 ? 29.896  49.514  4.017   1.00 25.72 ?  314  TRP A NE1 1 
ATOM   2308  C  CE2 . TRP A  1 290 ? 30.329  49.572  5.316   1.00 25.59 ?  314  TRP A CE2 1 
ATOM   2309  C  CE3 . TRP A  1 290 ? 32.364  49.132  6.553   1.00 26.04 ?  314  TRP A CE3 1 
ATOM   2310  C  CZ2 . TRP A  1 290 ? 29.644  49.949  6.479   1.00 25.61 ?  314  TRP A CZ2 1 
ATOM   2311  C  CZ3 . TRP A  1 290 ? 31.684  49.506  7.710   1.00 25.65 ?  314  TRP A CZ3 1 
ATOM   2312  C  CH2 . TRP A  1 290 ? 30.337  49.910  7.661   1.00 25.25 ?  314  TRP A CH2 1 
ATOM   2313  N  N   . ASN A  1 291 ? 35.614  48.437  1.191   1.00 26.81 ?  315  ASN A N   1 
ATOM   2314  C  CA  . ASN A  1 291 ? 37.038  48.257  0.938   1.00 26.30 ?  315  ASN A CA  1 
ATOM   2315  C  C   . ASN A  1 291 ? 37.849  48.812  2.103   1.00 25.71 ?  315  ASN A C   1 
ATOM   2316  O  O   . ASN A  1 291 ? 38.128  50.011  2.162   1.00 25.44 ?  315  ASN A O   1 
ATOM   2317  C  CB  . ASN A  1 291 ? 37.457  48.909  -0.386  1.00 26.53 ?  315  ASN A CB  1 
ATOM   2318  C  CG  . ASN A  1 291 ? 38.832  48.439  -0.870  1.00 27.31 ?  315  ASN A CG  1 
ATOM   2319  O  OD1 . ASN A  1 291 ? 39.582  47.787  -0.137  1.00 28.11 ?  315  ASN A OD1 1 
ATOM   2320  N  ND2 . ASN A  1 291 ? 39.161  48.769  -2.115  1.00 27.24 ?  315  ASN A ND2 1 
ATOM   2321  N  N   . TRP A  1 292 ? 38.220  47.922  3.023   1.00 25.06 ?  316  TRP A N   1 
ATOM   2322  C  CA  . TRP A  1 292 ? 38.951  48.292  4.231   1.00 24.50 ?  316  TRP A CA  1 
ATOM   2323  C  C   . TRP A  1 292 ? 40.384  48.731  3.946   1.00 24.56 ?  316  TRP A C   1 
ATOM   2324  O  O   . TRP A  1 292 ? 41.022  49.343  4.802   1.00 24.72 ?  316  TRP A O   1 
ATOM   2325  C  CB  . TRP A  1 292 ? 38.970  47.131  5.229   1.00 24.24 ?  316  TRP A CB  1 
ATOM   2326  C  CG  . TRP A  1 292 ? 37.628  46.746  5.742   1.00 22.81 ?  316  TRP A CG  1 
ATOM   2327  C  CD1 . TRP A  1 292 ? 36.835  45.736  5.276   1.00 21.67 ?  316  TRP A CD1 1 
ATOM   2328  C  CD2 . TRP A  1 292 ? 36.912  47.357  6.821   1.00 21.44 ?  316  TRP A CD2 1 
ATOM   2329  N  NE1 . TRP A  1 292 ? 35.670  45.679  5.999   1.00 21.28 ?  316  TRP A NE1 1 
ATOM   2330  C  CE2 . TRP A  1 292 ? 35.688  46.663  6.953   1.00 21.41 ?  316  TRP A CE2 1 
ATOM   2331  C  CE3 . TRP A  1 292 ? 37.183  48.425  7.690   1.00 21.24 ?  316  TRP A CE3 1 
ATOM   2332  C  CZ2 . TRP A  1 292 ? 34.734  46.998  7.921   1.00 20.38 ?  316  TRP A CZ2 1 
ATOM   2333  C  CZ3 . TRP A  1 292 ? 36.234  48.760  8.655   1.00 20.61 ?  316  TRP A CZ3 1 
ATOM   2334  C  CH2 . TRP A  1 292 ? 35.025  48.043  8.763   1.00 20.60 ?  316  TRP A CH2 1 
ATOM   2335  N  N   . GLU A  1 293 ? 40.877  48.415  2.749   1.00 24.63 ?  317  GLU A N   1 
ATOM   2336  C  CA  . GLU A  1 293 ? 42.257  48.718  2.355   1.00 24.78 ?  317  GLU A CA  1 
ATOM   2337  C  C   . GLU A  1 293 ? 42.492  50.198  2.017   1.00 24.72 ?  317  GLU A C   1 
ATOM   2338  O  O   . GLU A  1 293 ? 43.636  50.668  2.046   1.00 24.42 ?  317  GLU A O   1 
ATOM   2339  C  CB  . GLU A  1 293 ? 42.703  47.831  1.179   1.00 24.68 ?  317  GLU A CB  1 
ATOM   2340  C  CG  . GLU A  1 293 ? 42.850  46.336  1.493   1.00 25.95 ?  317  GLU A CG  1 
ATOM   2341  C  CD  . GLU A  1 293 ? 43.992  46.008  2.464   1.00 27.91 ?  317  GLU A CD  1 
ATOM   2342  O  OE1 . GLU A  1 293 ? 44.947  46.810  2.603   1.00 28.81 ?  317  GLU A OE1 1 
ATOM   2343  O  OE2 . GLU A  1 293 ? 43.929  44.931  3.095   1.00 29.16 -1 317  GLU A OE2 1 
ATOM   2344  N  N   . VAL A  1 294 ? 41.424  50.924  1.683   1.00 24.71 ?  318  VAL A N   1 
ATOM   2345  C  CA  . VAL A  1 294 ? 41.547  52.357  1.391   1.00 24.85 ?  318  VAL A CA  1 
ATOM   2346  C  C   . VAL A  1 294 ? 41.787  53.123  2.690   1.00 25.15 ?  318  VAL A C   1 
ATOM   2347  O  O   . VAL A  1 294 ? 41.403  52.661  3.772   1.00 24.96 ?  318  VAL A O   1 
ATOM   2348  C  CB  . VAL A  1 294 ? 40.316  52.939  0.627   1.00 24.96 ?  318  VAL A CB  1 
ATOM   2349  C  CG1 . VAL A  1 294 ? 39.964  52.079  -0.582  1.00 24.62 ?  318  VAL A CG1 1 
ATOM   2350  C  CG2 . VAL A  1 294 ? 39.109  53.111  1.553   1.00 24.69 ?  318  VAL A CG2 1 
ATOM   2351  N  N   . ARG A  1 295 ? 42.433  54.283  2.585   1.00 25.42 ?  319  ARG A N   1 
ATOM   2352  C  CA  . ARG A  1 295 ? 42.709  55.100  3.763   1.00 25.73 ?  319  ARG A CA  1 
ATOM   2353  C  C   . ARG A  1 295 ? 41.418  55.675  4.337   1.00 25.61 ?  319  ARG A C   1 
ATOM   2354  O  O   . ARG A  1 295 ? 40.434  55.851  3.612   1.00 25.55 ?  319  ARG A O   1 
ATOM   2355  C  CB  . ARG A  1 295 ? 43.721  56.209  3.448   1.00 26.18 ?  319  ARG A CB  1 
ATOM   2356  C  CG  . ARG A  1 295 ? 43.291  57.176  2.361   1.00 27.44 ?  319  ARG A CG  1 
ATOM   2357  C  CD  . ARG A  1 295 ? 44.357  58.227  2.097   1.00 29.86 ?  319  ARG A CD  1 
ATOM   2358  N  NE  . ARG A  1 295 ? 43.894  59.195  1.108   1.00 32.18 ?  319  ARG A NE  1 
ATOM   2359  C  CZ  . ARG A  1 295 ? 44.269  60.472  1.059   1.00 33.70 ?  319  ARG A CZ  1 
ATOM   2360  N  NH1 . ARG A  1 295 ? 45.122  60.964  1.952   1.00 33.34 ?  319  ARG A NH1 1 
ATOM   2361  N  NH2 . ARG A  1 295 ? 43.777  61.263  0.113   1.00 34.47 ?  319  ARG A NH2 1 
ATOM   2362  N  N   . LEU A  1 296 ? 41.428  55.960  5.638   1.00 25.44 ?  320  LEU A N   1 
ATOM   2363  C  CA  . LEU A  1 296 ? 40.250  56.483  6.334   1.00 25.49 ?  320  LEU A CA  1 
ATOM   2364  C  C   . LEU A  1 296 ? 39.628  57.690  5.627   1.00 25.41 ?  320  LEU A C   1 
ATOM   2365  O  O   . LEU A  1 296 ? 38.409  57.847  5.625   1.00 25.24 ?  320  LEU A O   1 
ATOM   2366  C  CB  . LEU A  1 296 ? 40.585  56.837  7.788   1.00 25.28 ?  320  LEU A CB  1 
ATOM   2367  C  CG  . LEU A  1 296 ? 40.847  55.683  8.766   1.00 25.58 ?  320  LEU A CG  1 
ATOM   2368  C  CD1 . LEU A  1 296 ? 41.342  56.217  10.101  1.00 25.05 ?  320  LEU A CD1 1 
ATOM   2369  C  CD2 . LEU A  1 296 ? 39.609  54.818  8.960   1.00 25.53 ?  320  LEU A CD2 1 
ATOM   2370  N  N   . LYS A  1 297 ? 40.470  58.523  5.016   1.00 25.30 ?  321  LYS A N   1 
ATOM   2371  C  CA  . LYS A  1 297 ? 39.998  59.701  4.295   1.00 25.44 ?  321  LYS A CA  1 
ATOM   2372  C  C   . LYS A  1 297 ? 39.194  59.350  3.037   1.00 25.42 ?  321  LYS A C   1 
ATOM   2373  O  O   . LYS A  1 297 ? 38.343  60.130  2.609   1.00 25.28 ?  321  LYS A O   1 
ATOM   2374  C  CB  . LYS A  1 297 ? 41.159  60.644  3.957   1.00 25.41 ?  321  LYS A CB  1 
ATOM   2375  C  CG  . LYS A  1 297 ? 40.696  62.064  3.662   1.00 25.76 ?  321  LYS A CG  1 
ATOM   2376  C  CD  . LYS A  1 297 ? 41.839  63.047  3.607   1.00 26.39 ?  321  LYS A CD  1 
ATOM   2377  C  CE  . LYS A  1 297 ? 41.323  64.441  3.290   1.00 26.00 ?  321  LYS A CE  1 
ATOM   2378  N  NZ  . LYS A  1 297 ? 42.429  65.426  3.253   1.00 26.43 ?  321  LYS A NZ  1 
ATOM   2379  N  N   . ASP A  1 298 ? 39.464  58.173  2.470   1.00 25.38 ?  322  ASP A N   1 
ATOM   2380  C  CA  . ASP A  1 298 ? 38.759  57.678  1.286   1.00 25.37 ?  322  ASP A CA  1 
ATOM   2381  C  C   . ASP A  1 298 ? 37.670  56.658  1.622   1.00 25.49 ?  322  ASP A C   1 
ATOM   2382  O  O   . ASP A  1 298 ? 36.991  56.153  0.719   1.00 25.34 ?  322  ASP A O   1 
ATOM   2383  C  CB  . ASP A  1 298 ? 39.752  57.047  0.301   1.00 25.35 ?  322  ASP A CB  1 
ATOM   2384  C  CG  . ASP A  1 298 ? 40.775  58.043  -0.227  1.00 25.56 ?  322  ASP A CG  1 
ATOM   2385  O  OD1 . ASP A  1 298 ? 40.497  59.261  -0.217  1.00 26.22 ?  322  ASP A OD1 1 
ATOM   2386  O  OD2 . ASP A  1 298 ? 41.862  57.601  -0.657  1.00 25.39 -1 322  ASP A OD2 1 
ATOM   2387  N  N   . ALA A  1 299 ? 37.507  56.361  2.914   1.00 25.61 ?  323  ALA A N   1 
ATOM   2388  C  CA  . ALA A  1 299 ? 36.620  55.281  3.374   1.00 25.92 ?  323  ALA A CA  1 
ATOM   2389  C  C   . ALA A  1 299 ? 35.181  55.425  2.886   1.00 26.24 ?  323  ALA A C   1 
ATOM   2390  O  O   . ALA A  1 299 ? 34.564  54.448  2.466   1.00 26.13 ?  323  ALA A O   1 
ATOM   2391  C  CB  . ALA A  1 299 ? 36.652  55.168  4.888   1.00 25.77 ?  323  ALA A CB  1 
ATOM   2392  N  N   . PHE A  1 300 ? 34.664  56.650  2.935   1.00 26.77 ?  324  PHE A N   1 
ATOM   2393  C  CA  . PHE A  1 300 ? 33.273  56.925  2.594   1.00 27.46 ?  324  PHE A CA  1 
ATOM   2394  C  C   . PHE A  1 300 ? 33.039  57.151  1.101   1.00 27.87 ?  324  PHE A C   1 
ATOM   2395  O  O   . PHE A  1 300 ? 31.897  57.156  0.648   1.00 28.24 ?  324  PHE A O   1 
ATOM   2396  C  CB  . PHE A  1 300 ? 32.752  58.103  3.420   1.00 27.27 ?  324  PHE A CB  1 
ATOM   2397  C  CG  . PHE A  1 300 ? 32.918  57.912  4.898   1.00 27.43 ?  324  PHE A CG  1 
ATOM   2398  C  CD1 . PHE A  1 300 ? 32.164  56.960  5.578   1.00 27.31 ?  324  PHE A CD1 1 
ATOM   2399  C  CD2 . PHE A  1 300 ? 33.847  58.663  5.606   1.00 27.55 ?  324  PHE A CD2 1 
ATOM   2400  C  CE1 . PHE A  1 300 ? 32.322  56.772  6.947   1.00 28.08 ?  324  PHE A CE1 1 
ATOM   2401  C  CE2 . PHE A  1 300 ? 34.013  58.485  6.971   1.00 28.36 ?  324  PHE A CE2 1 
ATOM   2402  C  CZ  . PHE A  1 300 ? 33.247  57.536  7.647   1.00 28.28 ?  324  PHE A CZ  1 
ATOM   2403  N  N   . SER A  1 301 ? 34.118  57.334  0.345   1.00 28.33 ?  325  SER A N   1 
ATOM   2404  C  CA  . SER A  1 301 ? 34.029  57.457  -1.109  1.00 28.64 ?  325  SER A CA  1 
ATOM   2405  C  C   . SER A  1 301 ? 34.524  56.175  -1.780  1.00 28.78 ?  325  SER A C   1 
ATOM   2406  O  O   . SER A  1 301 ? 33.721  55.330  -2.200  1.00 29.19 ?  325  SER A O   1 
ATOM   2407  C  CB  . SER A  1 301 ? 34.789  58.693  -1.609  1.00 28.71 ?  325  SER A CB  1 
ATOM   2408  O  OG  . SER A  1 301 ? 36.096  58.766  -1.064  1.00 28.88 ?  325  SER A OG  1 
ATOM   2409  N  N   . LYS A  1 302 ? 35.843  56.015  -1.841  1.00 28.56 ?  326  LYS A N   1 
ATOM   2410  C  CA  . LYS A  1 302 ? 36.466  54.839  -2.450  1.00 28.22 ?  326  LYS A CA  1 
ATOM   2411  C  C   . LYS A  1 302 ? 36.170  53.543  -1.693  1.00 27.91 ?  326  LYS A C   1 
ATOM   2412  O  O   . LYS A  1 302 ? 36.088  52.472  -2.297  1.00 27.80 ?  326  LYS A O   1 
ATOM   2413  C  CB  . LYS A  1 302 ? 37.977  55.050  -2.579  1.00 28.33 ?  326  LYS A CB  1 
ATOM   2414  C  CG  . LYS A  1 302 ? 38.357  56.165  -3.543  1.00 28.95 ?  326  LYS A CG  1 
ATOM   2415  C  CD  . LYS A  1 302 ? 39.852  56.463  -3.517  1.00 30.82 ?  326  LYS A CD  1 
ATOM   2416  C  CE  . LYS A  1 302 ? 40.203  57.536  -4.545  1.00 31.47 ?  326  LYS A CE  1 
ATOM   2417  N  NZ  . LYS A  1 302 ? 41.559  58.085  -4.323  1.00 32.89 ?  326  LYS A NZ  1 
ATOM   2418  N  N   . GLY A  1 303 ? 36.005  53.646  -0.376  1.00 27.51 ?  327  GLY A N   1 
ATOM   2419  C  CA  . GLY A  1 303 ? 35.752  52.477  0.468   1.00 27.12 ?  327  GLY A CA  1 
ATOM   2420  C  C   . GLY A  1 303 ? 34.334  51.934  0.394   1.00 26.90 ?  327  GLY A C   1 
ATOM   2421  O  O   . GLY A  1 303 ? 34.119  50.732  0.559   1.00 26.83 ?  327  GLY A O   1 
ATOM   2422  N  N   . GLY A  1 304 ? 33.369  52.822  0.155   1.00 26.47 ?  328  GLY A N   1 
ATOM   2423  C  CA  . GLY A  1 304 ? 31.955  52.448  0.094   1.00 26.16 ?  328  GLY A CA  1 
ATOM   2424  C  C   . GLY A  1 304 ? 31.284  52.336  1.454   1.00 25.83 ?  328  GLY A C   1 
ATOM   2425  O  O   . GLY A  1 304 ? 30.153  51.869  1.555   1.00 25.79 ?  328  GLY A O   1 
ATOM   2426  N  N   . GLN A  1 305 ? 31.981  52.775  2.499   1.00 25.66 ?  329  GLN A N   1 
ATOM   2427  C  CA  . GLN A  1 305 ? 31.498  52.666  3.872   1.00 25.47 ?  329  GLN A CA  1 
ATOM   2428  C  C   . GLN A  1 305 ? 30.293  53.581  4.107   1.00 25.38 ?  329  GLN A C   1 
ATOM   2429  O  O   . GLN A  1 305 ? 30.342  54.772  3.797   1.00 25.35 ?  329  GLN A O   1 
ATOM   2430  C  CB  . GLN A  1 305 ? 32.637  52.990  4.843   1.00 25.41 ?  329  GLN A CB  1 
ATOM   2431  C  CG  . GLN A  1 305 ? 32.328  52.756  6.313   1.00 25.26 ?  329  GLN A CG  1 
ATOM   2432  C  CD  . GLN A  1 305 ? 33.556  52.902  7.202   1.00 25.45 ?  329  GLN A CD  1 
ATOM   2433  O  OE1 . GLN A  1 305 ? 34.674  52.558  6.808   1.00 25.40 ?  329  GLN A OE1 1 
ATOM   2434  N  NE2 . GLN A  1 305 ? 33.350  53.412  8.410   1.00 25.41 ?  329  GLN A NE2 1 
ATOM   2435  N  N   . ASN A  1 306 ? 29.209  53.015  4.633   1.00 25.11 ?  330  ASN A N   1 
ATOM   2436  C  CA  . ASN A  1 306 ? 27.993  53.794  4.896   1.00 24.94 ?  330  ASN A CA  1 
ATOM   2437  C  C   . ASN A  1 306 ? 27.566  53.811  6.365   1.00 24.48 ?  330  ASN A C   1 
ATOM   2438  O  O   . ASN A  1 306 ? 26.543  54.403  6.715   1.00 24.45 ?  330  ASN A O   1 
ATOM   2439  C  CB  . ASN A  1 306 ? 26.832  53.352  3.990   1.00 24.97 ?  330  ASN A CB  1 
ATOM   2440  C  CG  . ASN A  1 306 ? 26.300  51.974  4.339   1.00 25.86 ?  330  ASN A CG  1 
ATOM   2441  O  OD1 . ASN A  1 306 ? 27.064  51.025  4.537   1.00 26.96 ?  330  ASN A OD1 1 
ATOM   2442  N  ND2 . ASN A  1 306 ? 24.976  51.853  4.403   1.00 26.34 ?  330  ASN A ND2 1 
ATOM   2443  N  N   . ALA A  1 307 ? 28.358  53.164  7.216   1.00 23.87 ?  331  ALA A N   1 
ATOM   2444  C  CA  . ALA A  1 307 ? 28.147  53.209  8.658   1.00 23.26 ?  331  ALA A CA  1 
ATOM   2445  C  C   . ALA A  1 307 ? 29.471  53.543  9.358   1.00 22.87 ?  331  ALA A C   1 
ATOM   2446  O  O   . ALA A  1 307 ? 30.527  53.125  8.896   1.00 22.81 ?  331  ALA A O   1 
ATOM   2447  C  CB  . ALA A  1 307 ? 27.576  51.885  9.151   1.00 23.00 ?  331  ALA A CB  1 
ATOM   2448  N  N   . PRO A  1 308 ? 29.422  54.304  10.469  1.00 22.56 ?  332  PRO A N   1 
ATOM   2449  C  CA  . PRO A  1 308 ? 30.673  54.749  11.092  1.00 22.25 ?  332  PRO A CA  1 
ATOM   2450  C  C   . PRO A  1 308 ? 31.351  53.667  11.933  1.00 22.11 ?  332  PRO A C   1 
ATOM   2451  O  O   . PRO A  1 308 ? 30.704  52.709  12.361  1.00 22.17 ?  332  PRO A O   1 
ATOM   2452  C  CB  . PRO A  1 308 ? 30.223  55.912  11.978  1.00 22.23 ?  332  PRO A CB  1 
ATOM   2453  C  CG  . PRO A  1 308 ? 28.838  55.539  12.387  1.00 22.36 ?  332  PRO A CG  1 
ATOM   2454  C  CD  . PRO A  1 308 ? 28.240  54.803  11.198  1.00 22.50 ?  332  PRO A CD  1 
ATOM   2455  N  N   . THR A  1 309 ? 32.651  53.833  12.157  1.00 21.79 ?  333  THR A N   1 
ATOM   2456  C  CA  . THR A  1 309 ? 33.465  52.860  12.882  1.00 21.41 ?  333  THR A CA  1 
ATOM   2457  C  C   . THR A  1 309 ? 34.300  53.589  13.936  1.00 21.28 ?  333  THR A C   1 
ATOM   2458  O  O   . THR A  1 309 ? 34.440  54.811  13.873  1.00 21.37 ?  333  THR A O   1 
ATOM   2459  C  CB  . THR A  1 309 ? 34.400  52.104  11.920  1.00 21.35 ?  333  THR A CB  1 
ATOM   2460  O  OG1 . THR A  1 309 ? 35.132  53.052  11.135  1.00 21.30 ?  333  THR A OG1 1 
ATOM   2461  C  CG2 . THR A  1 309 ? 33.601  51.182  10.988  1.00 20.66 ?  333  THR A CG2 1 
ATOM   2462  N  N   . CYS A  1 310 ? 34.841  52.849  14.903  1.00 21.30 ?  334  CYS A N   1 
ATOM   2463  C  CA  . CYS A  1 310 ? 35.683  53.438  15.957  1.00 21.19 ?  334  CYS A CA  1 
ATOM   2464  C  C   . CYS A  1 310 ? 36.745  54.366  15.365  1.00 21.26 ?  334  CYS A C   1 
ATOM   2465  O  O   . CYS A  1 310 ? 36.840  55.536  15.741  1.00 21.13 ?  334  CYS A O   1 
ATOM   2466  C  CB  . CYS A  1 310 ? 36.385  52.356  16.783  1.00 21.17 ?  334  CYS A CB  1 
ATOM   2467  S  SG  . CYS A  1 310 ? 35.439  50.879  17.169  1.00 20.39 ?  334  CYS A SG  1 
ATOM   2468  N  N   . ALA A  1 311 ? 37.533  53.831  14.432  1.00 21.22 ?  335  ALA A N   1 
ATOM   2469  C  CA  . ALA A  1 311 ? 38.652  54.561  13.830  1.00 21.53 ?  335  ALA A CA  1 
ATOM   2470  C  C   . ALA A  1 311 ? 38.215  55.800  13.042  1.00 21.65 ?  335  ALA A C   1 
ATOM   2471  O  O   . ALA A  1 311 ? 38.821  56.863  13.181  1.00 21.64 ?  335  ALA A O   1 
ATOM   2472  C  CB  . ALA A  1 311 ? 39.489  53.626  12.950  1.00 21.53 ?  335  ALA A CB  1 
ATOM   2473  N  N   . ALA A  1 312 ? 37.161  55.665  12.233  1.00 21.73 ?  336  ALA A N   1 
ATOM   2474  C  CA  . ALA A  1 312 ? 36.675  56.774  11.407  1.00 22.05 ?  336  ALA A CA  1 
ATOM   2475  C  C   . ALA A  1 312 ? 36.128  57.937  12.232  1.00 22.31 ?  336  ALA A C   1 
ATOM   2476  O  O   . ALA A  1 312 ? 36.227  59.090  11.814  1.00 22.62 ?  336  ALA A O   1 
ATOM   2477  C  CB  . ALA A  1 312 ? 35.629  56.294  10.399  1.00 21.90 ?  336  ALA A CB  1 
ATOM   2478  N  N   . CYS A  1 313 ? 35.554  57.638  13.395  1.00 22.28 ?  337  CYS A N   1 
ATOM   2479  C  CA  . CYS A  1 313 ? 35.022  58.686  14.263  1.00 22.41 ?  337  CYS A CA  1 
ATOM   2480  C  C   . CYS A  1 313 ? 36.100  59.315  15.142  1.00 22.82 ?  337  CYS A C   1 
ATOM   2481  O  O   . CYS A  1 313 ? 36.141  60.539  15.306  1.00 23.09 ?  337  CYS A O   1 
ATOM   2482  C  CB  . CYS A  1 313 ? 33.879  58.159  15.136  1.00 22.16 ?  337  CYS A CB  1 
ATOM   2483  S  SG  . CYS A  1 313 ? 32.223  58.188  14.375  1.00 21.46 ?  337  CYS A SG  1 
ATOM   2484  N  N   . HIS A  1 314 ? 36.972  58.482  15.702  1.00 22.90 ?  338  HIS A N   1 
ATOM   2485  C  CA  . HIS A  1 314 ? 37.912  58.945  16.716  1.00 23.21 ?  338  HIS A CA  1 
ATOM   2486  C  C   . HIS A  1 314 ? 39.275  59.422  16.197  1.00 23.58 ?  338  HIS A C   1 
ATOM   2487  O  O   . HIS A  1 314 ? 39.944  60.206  16.870  1.00 23.51 ?  338  HIS A O   1 
ATOM   2488  C  CB  . HIS A  1 314 ? 38.062  57.894  17.817  1.00 22.95 ?  338  HIS A CB  1 
ATOM   2489  C  CG  . HIS A  1 314 ? 36.856  57.781  18.698  1.00 22.66 ?  338  HIS A CG  1 
ATOM   2490  N  ND1 . HIS A  1 314 ? 36.588  58.685  19.701  1.00 21.59 ?  338  HIS A ND1 1 
ATOM   2491  C  CD2 . HIS A  1 314 ? 35.840  56.882  18.719  1.00 21.60 ?  338  HIS A CD2 1 
ATOM   2492  C  CE1 . HIS A  1 314 ? 35.465  58.347  20.308  1.00 21.64 ?  338  HIS A CE1 1 
ATOM   2493  N  NE2 . HIS A  1 314 ? 34.991  57.253  19.736  1.00 21.51 ?  338  HIS A NE2 1 
ATOM   2494  N  N   . MET A  1 315 ? 39.678  58.965  15.012  1.00 23.98 ?  339  MET A N   1 
ATOM   2495  C  CA  . MET A  1 315 ? 40.899  59.474  14.372  1.00 24.60 ?  339  MET A CA  1 
ATOM   2496  C  C   . MET A  1 315 ? 40.638  60.693  13.475  1.00 24.78 ?  339  MET A C   1 
ATOM   2497  O  O   . MET A  1 315 ? 41.579  61.368  13.040  1.00 24.80 ?  339  MET A O   1 
ATOM   2498  C  CB  . MET A  1 315 ? 41.627  58.369  13.599  1.00 24.64 ?  339  MET A CB  1 
ATOM   2499  C  CG  . MET A  1 315 ? 42.433  57.430  14.492  1.00 25.42 ?  339  MET A CG  1 
ATOM   2500  S  SD  . MET A  1 315 ? 43.169  56.031  13.630  1.00 29.69 ?  339  MET A SD  1 
ATOM   2501  C  CE  . MET A  1 315 ? 44.447  56.795  12.645  1.00 28.54 ?  339  MET A CE  1 
ATOM   2502  N  N   . GLU A  1 316 ? 39.363  60.969  13.213  1.00 24.91 ?  340  GLU A N   1 
ATOM   2503  C  CA  . GLU A  1 316 ? 38.958  62.121  12.410  1.00 25.25 ?  340  GLU A CA  1 
ATOM   2504  C  C   . GLU A  1 316 ? 39.005  63.407  13.231  1.00 25.55 ?  340  GLU A C   1 
ATOM   2505  O  O   . GLU A  1 316 ? 38.618  63.424  14.402  1.00 25.45 ?  340  GLU A O   1 
ATOM   2506  C  CB  . GLU A  1 316 ? 37.549  61.912  11.841  1.00 25.25 ?  340  GLU A CB  1 
ATOM   2507  C  CG  . GLU A  1 316 ? 37.121  62.913  10.760  1.00 25.21 ?  340  GLU A CG  1 
ATOM   2508  C  CD  . GLU A  1 316 ? 36.571  64.221  11.324  1.00 25.59 ?  340  GLU A CD  1 
ATOM   2509  O  OE1 . GLU A  1 316 ? 36.157  64.253  12.499  1.00 26.00 ?  340  GLU A OE1 1 
ATOM   2510  O  OE2 . GLU A  1 316 ? 36.552  65.226  10.586  1.00 26.96 -1 340  GLU A OE2 1 
ATOM   2511  N  N   . TYR A  1 317 ? 39.485  64.476  12.604  1.00 25.91 ?  341  TYR A N   1 
ATOM   2512  C  CA  . TYR A  1 317 ? 39.466  65.810  13.195  1.00 26.40 ?  341  TYR A CA  1 
ATOM   2513  C  C   . TYR A  1 317 ? 39.499  66.849  12.088  1.00 26.63 ?  341  TYR A C   1 
ATOM   2514  O  O   . TYR A  1 317 ? 40.458  66.908  11.314  1.00 26.61 ?  341  TYR A O   1 
ATOM   2515  C  CB  . TYR A  1 317 ? 40.642  66.007  14.159  1.00 26.43 ?  341  TYR A CB  1 
ATOM   2516  C  CG  . TYR A  1 317 ? 40.646  67.340  14.874  1.00 27.48 ?  341  TYR A CG  1 
ATOM   2517  C  CD1 . TYR A  1 317 ? 39.689  67.639  15.848  1.00 28.43 ?  341  TYR A CD1 1 
ATOM   2518  C  CD2 . TYR A  1 317 ? 41.613  68.302  14.586  1.00 28.25 ?  341  TYR A CD2 1 
ATOM   2519  C  CE1 . TYR A  1 317 ? 39.692  68.865  16.508  1.00 28.55 ?  341  TYR A CE1 1 
ATOM   2520  C  CE2 . TYR A  1 317 ? 41.629  69.529  15.243  1.00 28.30 ?  341  TYR A CE2 1 
ATOM   2521  C  CZ  . TYR A  1 317 ? 40.667  69.802  16.201  1.00 28.57 ?  341  TYR A CZ  1 
ATOM   2522  O  OH  . TYR A  1 317 ? 40.678  71.013  16.849  1.00 28.45 ?  341  TYR A OH  1 
ATOM   2523  N  N   . GLU A  1 318 ? 38.436  67.648  12.013  1.00 27.07 ?  342  GLU A N   1 
ATOM   2524  C  CA  . GLU A  1 318 ? 38.297  68.718  11.018  1.00 27.54 ?  342  GLU A CA  1 
ATOM   2525  C  C   . GLU A  1 318 ? 38.575  68.258  9.577   1.00 27.43 ?  342  GLU A C   1 
ATOM   2526  O  O   . GLU A  1 318 ? 39.221  68.968  8.809   1.00 27.48 ?  342  GLU A O   1 
ATOM   2527  C  CB  . GLU A  1 318 ? 39.172  69.929  11.387  1.00 27.76 ?  342  GLU A CB  1 
ATOM   2528  C  CG  . GLU A  1 318 ? 38.854  70.578  12.746  1.00 29.10 ?  342  GLU A CG  1 
ATOM   2529  C  CD  . GLU A  1 318 ? 37.495  71.265  12.785  1.00 30.65 ?  342  GLU A CD  1 
ATOM   2530  O  OE1 . GLU A  1 318 ? 37.155  71.986  11.823  1.00 32.04 ?  342  GLU A OE1 1 
ATOM   2531  O  OE2 . GLU A  1 318 ? 36.764  71.085  13.783  1.00 31.54 -1 342  GLU A OE2 1 
ATOM   2532  N  N   . GLY A  1 319 ? 38.089  67.069  9.223   1.00 27.48 ?  343  GLY A N   1 
ATOM   2533  C  CA  . GLY A  1 319 ? 38.188  66.563  7.849   1.00 27.47 ?  343  GLY A CA  1 
ATOM   2534  C  C   . GLY A  1 319 ? 39.454  65.788  7.519   1.00 27.69 ?  343  GLY A C   1 
ATOM   2535  O  O   . GLY A  1 319 ? 39.618  65.313  6.393   1.00 27.62 ?  343  GLY A O   1 
ATOM   2536  N  N   . GLU A  1 320 ? 40.345  65.660  8.499   1.00 27.70 ?  344  GLU A N   1 
ATOM   2537  C  CA  . GLU A  1 320 ? 41.586  64.914  8.329   1.00 27.84 ?  344  GLU A CA  1 
ATOM   2538  C  C   . GLU A  1 320 ? 41.695  63.777  9.353   1.00 27.39 ?  344  GLU A C   1 
ATOM   2539  O  O   . GLU A  1 320 ? 40.974  63.758  10.351  1.00 27.21 ?  344  GLU A O   1 
ATOM   2540  C  CB  . GLU A  1 320 ? 42.799  65.858  8.411   1.00 28.07 ?  344  GLU A CB  1 
ATOM   2541  C  CG  . GLU A  1 320 ? 44.098  65.273  7.854   1.00 29.49 ?  344  GLU A CG  1 
ATOM   2542  C  CD  . GLU A  1 320 ? 43.928  64.687  6.456   1.00 31.44 ?  344  GLU A CD  1 
ATOM   2543  O  OE1 . GLU A  1 320 ? 43.848  65.471  5.485   1.00 32.63 ?  344  GLU A OE1 1 
ATOM   2544  O  OE2 . GLU A  1 320 ? 43.875  63.443  6.331   1.00 31.68 -1 344  GLU A OE2 1 
ATOM   2545  N  N   . TYR A  1 321 ? 42.599  62.836  9.088   1.00 26.92 ?  345  TYR A N   1 
ATOM   2546  C  CA  . TYR A  1 321 ? 42.773  61.653  9.921   1.00 26.47 ?  345  TYR A CA  1 
ATOM   2547  C  C   . TYR A  1 321 ? 44.219  61.509  10.382  1.00 26.13 ?  345  TYR A C   1 
ATOM   2548  O  O   . TYR A  1 321 ? 45.141  61.536  9.566   1.00 26.08 ?  345  TYR A O   1 
ATOM   2549  C  CB  . TYR A  1 321 ? 42.314  60.403  9.159   1.00 26.38 ?  345  TYR A CB  1 
ATOM   2550  C  CG  . TYR A  1 321 ? 40.843  60.429  8.809   1.00 26.52 ?  345  TYR A CG  1 
ATOM   2551  C  CD1 . TYR A  1 321 ? 40.386  61.106  7.674   1.00 26.60 ?  345  TYR A CD1 1 
ATOM   2552  C  CD2 . TYR A  1 321 ? 39.901  59.794  9.622   1.00 26.25 ?  345  TYR A CD2 1 
ATOM   2553  C  CE1 . TYR A  1 321 ? 39.035  61.148  7.356   1.00 26.48 ?  345  TYR A CE1 1 
ATOM   2554  C  CE2 . TYR A  1 321 ? 38.547  59.817  9.303   1.00 26.72 ?  345  TYR A CE2 1 
ATOM   2555  C  CZ  . TYR A  1 321 ? 38.122  60.501  8.171   1.00 26.94 ?  345  TYR A CZ  1 
ATOM   2556  O  OH  . TYR A  1 321 ? 36.784  60.536  7.852   1.00 27.06 ?  345  TYR A OH  1 
ATOM   2557  N  N   . THR A  1 322 ? 44.406  61.380  11.696  1.00 25.75 ?  346  THR A N   1 
ATOM   2558  C  CA  . THR A  1 322 ? 45.733  61.208  12.294  1.00 25.43 ?  346  THR A CA  1 
ATOM   2559  C  C   . THR A  1 322 ? 45.682  60.182  13.427  1.00 25.43 ?  346  THR A C   1 
ATOM   2560  O  O   . THR A  1 322 ? 44.600  59.838  13.911  1.00 25.12 ?  346  THR A O   1 
ATOM   2561  C  CB  . THR A  1 322 ? 46.334  62.548  12.836  1.00 25.49 ?  346  THR A CB  1 
ATOM   2562  O  OG1 . THR A  1 322 ? 45.743  62.887  14.097  1.00 25.26 ?  346  THR A OG1 1 
ATOM   2563  C  CG2 . THR A  1 322 ? 46.152  63.709  11.843  1.00 25.27 ?  346  THR A CG2 1 
ATOM   2564  N  N   . HIS A  1 323 ? 46.855  59.709  13.853  1.00 25.30 ?  347  HIS A N   1 
ATOM   2565  C  CA  . HIS A  1 323 ? 46.964  58.768  14.974  1.00 25.20 ?  347  HIS A CA  1 
ATOM   2566  C  C   . HIS A  1 323 ? 46.691  59.433  16.333  1.00 25.22 ?  347  HIS A C   1 
ATOM   2567  O  O   . HIS A  1 323 ? 46.766  58.781  17.375  1.00 25.60 ?  347  HIS A O   1 
ATOM   2568  C  CB  . HIS A  1 323 ? 48.338  58.069  14.975  1.00 25.00 ?  347  HIS A CB  1 
ATOM   2569  C  CG  . HIS A  1 323 ? 48.392  56.814  14.149  1.00 24.75 ?  347  HIS A CG  1 
ATOM   2570  N  ND1 . HIS A  1 323 ? 48.275  56.817  12.777  1.00 23.81 ?  347  HIS A ND1 1 
ATOM   2571  C  CD2 . HIS A  1 323 ? 48.568  55.518  14.506  1.00 24.21 ?  347  HIS A CD2 1 
ATOM   2572  C  CE1 . HIS A  1 323 ? 48.371  55.578  12.325  1.00 23.99 ?  347  HIS A CE1 1 
ATOM   2573  N  NE2 . HIS A  1 323 ? 48.553  54.768  13.353  1.00 23.82 ?  347  HIS A NE2 1 
ATOM   2574  N  N   . ASN A  1 324 ? 46.380  60.728  16.316  1.00 25.05 ?  348  ASN A N   1 
ATOM   2575  C  CA  . ASN A  1 324 ? 45.995  61.465  17.522  1.00 24.97 ?  348  ASN A CA  1 
ATOM   2576  C  C   . ASN A  1 324 ? 44.482  61.348  17.725  1.00 24.99 ?  348  ASN A C   1 
ATOM   2577  O  O   . ASN A  1 324 ? 43.707  61.834  16.905  1.00 25.23 ?  348  ASN A O   1 
ATOM   2578  C  CB  . ASN A  1 324 ? 46.428  62.937  17.402  1.00 24.71 ?  348  ASN A CB  1 
ATOM   2579  C  CG  . ASN A  1 324 ? 46.144  63.756  18.662  1.00 24.54 ?  348  ASN A CG  1 
ATOM   2580  O  OD1 . ASN A  1 324 ? 45.116  63.588  19.321  1.00 23.72 ?  348  ASN A OD1 1 
ATOM   2581  N  ND2 . ASN A  1 324 ? 47.058  64.668  18.985  1.00 23.87 ?  348  ASN A ND2 1 
ATOM   2582  N  N   . ILE A  1 325 ? 44.069  60.706  18.815  1.00 24.92 ?  349  ILE A N   1 
ATOM   2583  C  CA  . ILE A  1 325 ? 42.643  60.443  19.065  1.00 24.76 ?  349  ILE A CA  1 
ATOM   2584  C  C   . ILE A  1 325 ? 42.030  61.267  20.204  1.00 24.78 ?  349  ILE A C   1 
ATOM   2585  O  O   . ILE A  1 325 ? 40.991  60.887  20.751  1.00 24.80 ?  349  ILE A O   1 
ATOM   2586  C  CB  . ILE A  1 325 ? 42.362  58.915  19.306  1.00 24.68 ?  349  ILE A CB  1 
ATOM   2587  C  CG1 . ILE A  1 325 ? 43.406  58.271  20.229  1.00 24.26 ?  349  ILE A CG1 1 
ATOM   2588  C  CG2 . ILE A  1 325 ? 42.332  58.165  17.994  1.00 24.17 ?  349  ILE A CG2 1 
ATOM   2589  C  CD1 . ILE A  1 325 ? 43.313  58.657  21.705  1.00 22.94 ?  349  ILE A CD1 1 
ATOM   2590  N  N   . THR A  1 326 ? 42.657  62.394  20.542  1.00 24.89 ?  350  THR A N   1 
ATOM   2591  C  CA  . THR A  1 326 ? 42.311  63.143  21.758  1.00 25.07 ?  350  THR A CA  1 
ATOM   2592  C  C   . THR A  1 326 ? 41.603  64.486  21.558  1.00 25.29 ?  350  THR A C   1 
ATOM   2593  O  O   . THR A  1 326 ? 41.078  65.052  22.521  1.00 25.33 ?  350  THR A O   1 
ATOM   2594  C  CB  . THR A  1 326 ? 43.566  63.436  22.609  1.00 25.25 ?  350  THR A CB  1 
ATOM   2595  O  OG1 . THR A  1 326 ? 44.440  64.317  21.886  1.00 25.48 ?  350  THR A OG1 1 
ATOM   2596  C  CG2 . THR A  1 326 ? 44.299  62.153  22.965  1.00 24.73 ?  350  THR A CG2 1 
ATOM   2597  N  N   . ARG A  1 327 ? 41.589  65.002  20.332  1.00 25.43 ?  351  ARG A N   1 
ATOM   2598  C  CA  . ARG A  1 327 ? 41.238  66.416  20.119  1.00 25.71 ?  351  ARG A CA  1 
ATOM   2599  C  C   . ARG A  1 327 ? 39.754  66.779  20.209  1.00 25.59 ?  351  ARG A C   1 
ATOM   2600  O  O   . ARG A  1 327 ? 39.408  67.961  20.283  1.00 25.57 ?  351  ARG A O   1 
ATOM   2601  C  CB  . ARG A  1 327 ? 41.868  66.952  18.830  1.00 25.80 ?  351  ARG A CB  1 
ATOM   2602  C  CG  . ARG A  1 327 ? 43.383  67.097  18.937  1.00 26.40 ?  351  ARG A CG  1 
ATOM   2603  C  CD  . ARG A  1 327 ? 44.009  67.533  17.634  1.00 27.12 ?  351  ARG A CD  1 
ATOM   2604  N  NE  . ARG A  1 327 ? 43.922  66.504  16.596  1.00 27.52 ?  351  ARG A NE  1 
ATOM   2605  C  CZ  . ARG A  1 327 ? 44.521  66.594  15.410  1.00 27.29 ?  351  ARG A CZ  1 
ATOM   2606  N  NH1 . ARG A  1 327 ? 45.251  67.662  15.114  1.00 26.99 ?  351  ARG A NH1 1 
ATOM   2607  N  NH2 . ARG A  1 327 ? 44.396  65.618  14.521  1.00 27.10 ?  351  ARG A NH2 1 
ATOM   2608  N  N   . LYS A  1 328 ? 38.887  65.771  20.230  1.00 25.44 ?  352  LYS A N   1 
ATOM   2609  C  CA  . LYS A  1 328 ? 37.449  66.004  20.358  1.00 25.17 ?  352  LYS A CA  1 
ATOM   2610  C  C   . LYS A  1 328 ? 36.896  65.522  21.703  1.00 25.07 ?  352  LYS A C   1 
ATOM   2611  O  O   . LYS A  1 328 ? 35.683  65.553  21.927  1.00 25.09 ?  352  LYS A O   1 
ATOM   2612  C  CB  . LYS A  1 328 ? 36.696  65.333  19.206  1.00 25.10 ?  352  LYS A CB  1 
ATOM   2613  C  CG  . LYS A  1 328 ? 37.098  65.814  17.817  1.00 24.98 ?  352  LYS A CG  1 
ATOM   2614  C  CD  . LYS A  1 328 ? 36.226  65.198  16.725  1.00 24.52 ?  352  LYS A CD  1 
ATOM   2615  C  CE  . LYS A  1 328 ? 36.405  63.682  16.639  1.00 24.40 ?  352  LYS A CE  1 
ATOM   2616  N  NZ  . LYS A  1 328 ? 35.777  63.123  15.413  1.00 25.15 ?  352  LYS A NZ  1 
ATOM   2617  N  N   . THR A  1 329 ? 37.788  65.083  22.589  1.00 24.88 ?  353  THR A N   1 
ATOM   2618  C  CA  . THR A  1 329 ? 37.398  64.497  23.874  1.00 24.74 ?  353  THR A CA  1 
ATOM   2619  C  C   . THR A  1 329 ? 36.801  65.527  24.833  1.00 24.56 ?  353  THR A C   1 
ATOM   2620  O  O   . THR A  1 329 ? 37.443  66.530  25.159  1.00 24.63 ?  353  THR A O   1 
ATOM   2621  C  CB  . THR A  1 329 ? 38.589  63.794  24.560  1.00 24.89 ?  353  THR A CB  1 
ATOM   2622  O  OG1 . THR A  1 329 ? 39.078  62.744  23.717  1.00 24.97 ?  353  THR A OG1 1 
ATOM   2623  C  CG2 . THR A  1 329 ? 38.169  63.205  25.915  1.00 24.57 ?  353  THR A CG2 1 
ATOM   2624  N  N   . ARG A  1 330 ? 35.579  65.257  25.290  1.00 24.14 ?  354  ARG A N   1 
ATOM   2625  C  CA  . ARG A  1 330 ? 34.856  66.160  26.191  1.00 23.77 ?  354  ARG A CA  1 
ATOM   2626  C  C   . ARG A  1 330 ? 34.544  65.497  27.531  1.00 23.66 ?  354  ARG A C   1 
ATOM   2627  O  O   . ARG A  1 330 ? 34.824  66.060  28.597  1.00 23.62 ?  354  ARG A O   1 
ATOM   2628  C  CB  . ARG A  1 330 ? 33.558  66.646  25.530  1.00 23.65 ?  354  ARG A CB  1 
ATOM   2629  C  CG  . ARG A  1 330 ? 33.775  67.410  24.227  1.00 23.38 ?  354  ARG A CG  1 
ATOM   2630  C  CD  . ARG A  1 330 ? 32.509  67.528  23.388  1.00 22.97 ?  354  ARG A CD  1 
ATOM   2631  N  NE  . ARG A  1 330 ? 31.484  68.386  23.988  1.00 21.89 ?  354  ARG A NE  1 
ATOM   2632  C  CZ  . ARG A  1 330 ? 30.348  67.943  24.522  1.00 21.61 ?  354  ARG A CZ  1 
ATOM   2633  N  NH1 . ARG A  1 330 ? 30.078  66.642  24.552  1.00 20.92 ?  354  ARG A NH1 1 
ATOM   2634  N  NH2 . ARG A  1 330 ? 29.476  68.805  25.029  1.00 21.65 ?  354  ARG A NH2 1 
ATOM   2635  N  N   . TRP A  1 331 ? 33.967  64.297  27.473  1.00 23.29 ?  355  TRP A N   1 
ATOM   2636  C  CA  . TRP A  1 331 ? 33.512  63.604  28.675  1.00 23.00 ?  355  TRP A CA  1 
ATOM   2637  C  C   . TRP A  1 331 ? 34.574  62.689  29.278  1.00 23.05 ?  355  TRP A C   1 
ATOM   2638  O  O   . TRP A  1 331 ? 34.630  62.518  30.499  1.00 22.71 ?  355  TRP A O   1 
ATOM   2639  C  CB  . TRP A  1 331 ? 32.239  62.811  28.384  1.00 22.92 ?  355  TRP A CB  1 
ATOM   2640  C  CG  . TRP A  1 331 ? 30.985  63.635  28.446  1.00 22.43 ?  355  TRP A CG  1 
ATOM   2641  C  CD1 . TRP A  1 331 ? 30.216  64.042  27.388  1.00 22.12 ?  355  TRP A CD1 1 
ATOM   2642  C  CD2 . TRP A  1 331 ? 30.348  64.145  29.624  1.00 21.88 ?  355  TRP A CD2 1 
ATOM   2643  N  NE1 . TRP A  1 331 ? 29.144  64.773  27.838  1.00 21.74 ?  355  TRP A NE1 1 
ATOM   2644  C  CE2 . TRP A  1 331 ? 29.201  64.855  29.205  1.00 21.89 ?  355  TRP A CE2 1 
ATOM   2645  C  CE3 . TRP A  1 331 ? 30.638  64.075  30.995  1.00 22.25 ?  355  TRP A CE3 1 
ATOM   2646  C  CZ2 . TRP A  1 331 ? 28.338  65.493  30.108  1.00 21.62 ?  355  TRP A CZ2 1 
ATOM   2647  C  CZ3 . TRP A  1 331 ? 29.782  64.713  31.894  1.00 22.23 ?  355  TRP A CZ3 1 
ATOM   2648  C  CH2 . TRP A  1 331 ? 28.643  65.411  31.442  1.00 21.96 ?  355  TRP A CH2 1 
ATOM   2649  N  N   . ALA A  1 332 ? 35.399  62.097  28.410  1.00 23.03 ?  356  ALA A N   1 
ATOM   2650  C  CA  . ALA A  1 332 ? 36.484  61.203  28.819  1.00 23.28 ?  356  ALA A CA  1 
ATOM   2651  C  C   . ALA A  1 332 ? 36.001  60.039  29.702  1.00 23.37 ?  356  ALA A C   1 
ATOM   2652  O  O   . ALA A  1 332 ? 36.600  59.729  30.734  1.00 23.27 ?  356  ALA A O   1 
ATOM   2653  C  CB  . ALA A  1 332 ? 37.633  61.996  29.491  1.00 23.00 ?  356  ALA A CB  1 
ATOM   2654  N  N   . ASN A  1 333 ? 34.894  59.426  29.279  1.00 23.74 ?  357  ASN A N   1 
ATOM   2655  C  CA  . ASN A  1 333 ? 34.356  58.183  29.850  1.00 23.82 ?  357  ASN A CA  1 
ATOM   2656  C  C   . ASN A  1 333 ? 33.749  58.234  31.252  1.00 24.02 ?  357  ASN A C   1 
ATOM   2657  O  O   . ASN A  1 333 ? 32.641  57.742  31.447  1.00 23.86 ?  357  ASN A O   1 
ATOM   2658  C  CB  . ASN A  1 333 ? 35.379  57.043  29.778  1.00 23.83 ?  357  ASN A CB  1 
ATOM   2659  C  CG  . ASN A  1 333 ? 34.762  55.688  30.069  1.00 23.73 ?  357  ASN A CG  1 
ATOM   2660  O  OD1 . ASN A  1 333 ? 34.066  55.121  29.230  1.00 23.00 ?  357  ASN A OD1 1 
ATOM   2661  N  ND2 . ASN A  1 333 ? 35.019  55.162  31.261  1.00 23.45 ?  357  ASN A ND2 1 
ATOM   2662  N  N   . TYR A  1 334 ? 34.483  58.794  32.216  1.00 24.39 ?  358  TYR A N   1 
ATOM   2663  C  CA  . TYR A  1 334 ? 34.056  58.828  33.621  1.00 24.61 ?  358  TYR A CA  1 
ATOM   2664  C  C   . TYR A  1 334 ? 33.465  60.201  33.986  1.00 25.03 ?  358  TYR A C   1 
ATOM   2665  O  O   . TYR A  1 334 ? 34.207  61.117  34.352  1.00 25.24 ?  358  TYR A O   1 
ATOM   2666  C  CB  . TYR A  1 334 ? 35.230  58.494  34.559  1.00 24.74 ?  358  TYR A CB  1 
ATOM   2667  C  CG  . TYR A  1 334 ? 35.921  57.165  34.290  1.00 24.30 ?  358  TYR A CG  1 
ATOM   2668  C  CD1 . TYR A  1 334 ? 35.484  55.988  34.908  1.00 23.89 ?  358  TYR A CD1 1 
ATOM   2669  C  CD2 . TYR A  1 334 ? 37.018  57.089  33.430  1.00 23.84 ?  358  TYR A CD2 1 
ATOM   2670  C  CE1 . TYR A  1 334 ? 36.121  54.762  34.667  1.00 23.67 ?  358  TYR A CE1 1 
ATOM   2671  C  CE2 . TYR A  1 334 ? 37.664  55.868  33.179  1.00 24.02 ?  358  TYR A CE2 1 
ATOM   2672  C  CZ  . TYR A  1 334 ? 37.211  54.713  33.802  1.00 24.06 ?  358  TYR A CZ  1 
ATOM   2673  O  OH  . TYR A  1 334 ? 37.843  53.514  33.558  1.00 23.20 ?  358  TYR A OH  1 
ATOM   2674  N  N   . PRO A  1 335 ? 32.127  60.342  33.901  1.00 25.22 ?  359  PRO A N   1 
ATOM   2675  C  CA  . PRO A  1 335 ? 31.431  61.628  34.083  1.00 25.45 ?  359  PRO A CA  1 
ATOM   2676  C  C   . PRO A  1 335 ? 31.518  62.223  35.492  1.00 25.63 ?  359  PRO A C   1 
ATOM   2677  O  O   . PRO A  1 335 ? 31.153  63.382  35.689  1.00 25.54 ?  359  PRO A O   1 
ATOM   2678  C  CB  . PRO A  1 335 ? 29.966  61.282  33.763  1.00 25.28 ?  359  PRO A CB  1 
ATOM   2679  C  CG  . PRO A  1 335 ? 30.031  60.004  32.985  1.00 25.27 ?  359  PRO A CG  1 
ATOM   2680  C  CD  . PRO A  1 335 ? 31.170  59.261  33.604  1.00 25.32 ?  359  PRO A CD  1 
ATOM   2681  N  N   . PHE A  1 336 ? 31.994  61.434  36.454  1.00 26.00 ?  360  PHE A N   1 
ATOM   2682  C  CA  . PHE A  1 336 ? 32.072  61.857  37.854  1.00 26.38 ?  360  PHE A CA  1 
ATOM   2683  C  C   . PHE A  1 336 ? 33.390  62.554  38.224  1.00 26.43 ?  360  PHE A C   1 
ATOM   2684  O  O   . PHE A  1 336 ? 33.518  63.093  39.321  1.00 26.35 ?  360  PHE A O   1 
ATOM   2685  C  CB  . PHE A  1 336 ? 31.843  60.657  38.779  1.00 26.35 ?  360  PHE A CB  1 
ATOM   2686  C  CG  . PHE A  1 336 ? 32.829  59.537  38.576  1.00 26.82 ?  360  PHE A CG  1 
ATOM   2687  C  CD1 . PHE A  1 336 ? 34.058  59.542  39.234  1.00 27.08 ?  360  PHE A CD1 1 
ATOM   2688  C  CD2 . PHE A  1 336 ? 32.528  58.476  37.725  1.00 26.86 ?  360  PHE A CD2 1 
ATOM   2689  C  CE1 . PHE A  1 336 ? 34.971  58.506  39.045  1.00 27.39 ?  360  PHE A CE1 1 
ATOM   2690  C  CE2 . PHE A  1 336 ? 33.430  57.438  37.533  1.00 26.77 ?  360  PHE A CE2 1 
ATOM   2691  C  CZ  . PHE A  1 336 ? 34.653  57.451  38.196  1.00 27.09 ?  360  PHE A CZ  1 
ATOM   2692  N  N   . VAL A  1 337 ? 34.364  62.525  37.319  1.00 26.76 ?  361  VAL A N   1 
ATOM   2693  C  CA  . VAL A  1 337 ? 35.662  63.166  37.558  1.00 27.02 ?  361  VAL A CA  1 
ATOM   2694  C  C   . VAL A  1 337 ? 35.458  64.660  37.840  1.00 27.13 ?  361  VAL A C   1 
ATOM   2695  O  O   . VAL A  1 337 ? 34.766  65.342  37.078  1.00 26.92 ?  361  VAL A O   1 
ATOM   2696  C  CB  . VAL A  1 337 ? 36.635  62.936  36.369  1.00 27.04 ?  361  VAL A CB  1 
ATOM   2697  C  CG1 . VAL A  1 337 ? 37.900  63.780  36.507  1.00 26.96 ?  361  VAL A CG1 1 
ATOM   2698  C  CG2 . VAL A  1 337 ? 36.993  61.457  36.261  1.00 27.18 ?  361  VAL A CG2 1 
ATOM   2699  N  N   . PRO A  1 338 ? 36.025  65.163  38.959  1.00 27.35 ?  362  PRO A N   1 
ATOM   2700  C  CA  . PRO A  1 338 ? 35.809  66.564  39.325  1.00 27.36 ?  362  PRO A CA  1 
ATOM   2701  C  C   . PRO A  1 338 ? 36.152  67.521  38.187  1.00 27.44 ?  362  PRO A C   1 
ATOM   2702  O  O   . PRO A  1 338 ? 37.210  67.399  37.563  1.00 27.44 ?  362  PRO A O   1 
ATOM   2703  C  CB  . PRO A  1 338 ? 36.750  66.764  40.517  1.00 27.42 ?  362  PRO A CB  1 
ATOM   2704  C  CG  . PRO A  1 338 ? 36.838  65.412  41.143  1.00 27.72 ?  362  PRO A CG  1 
ATOM   2705  C  CD  . PRO A  1 338 ? 36.813  64.444  39.980  1.00 27.32 ?  362  PRO A CD  1 
ATOM   2706  N  N   . GLY A  1 339 ? 35.234  68.439  37.901  1.00 27.44 ?  363  GLY A N   1 
ATOM   2707  C  CA  . GLY A  1 339 ? 35.450  69.454  36.875  1.00 27.35 ?  363  GLY A CA  1 
ATOM   2708  C  C   . GLY A  1 339 ? 35.002  69.096  35.468  1.00 27.35 ?  363  GLY A C   1 
ATOM   2709  O  O   . GLY A  1 339 ? 34.969  69.971  34.598  1.00 27.40 ?  363  GLY A O   1 
ATOM   2710  N  N   . ILE A  1 340 ? 34.665  67.825  35.233  1.00 27.04 ?  364  ILE A N   1 
ATOM   2711  C  CA  . ILE A  1 340 ? 34.287  67.365  33.887  1.00 26.82 ?  364  ILE A CA  1 
ATOM   2712  C  C   . ILE A  1 340 ? 32.881  67.825  33.485  1.00 26.80 ?  364  ILE A C   1 
ATOM   2713  O  O   . ILE A  1 340 ? 32.692  68.375  32.399  1.00 26.86 ?  364  ILE A O   1 
ATOM   2714  C  CB  . ILE A  1 340 ? 34.461  65.826  33.716  1.00 26.74 ?  364  ILE A CB  1 
ATOM   2715  C  CG1 . ILE A  1 340 ? 35.949  65.452  33.697  1.00 26.30 ?  364  ILE A CG1 1 
ATOM   2716  C  CG2 . ILE A  1 340 ? 33.758  65.314  32.445  1.00 26.17 ?  364  ILE A CG2 1 
ATOM   2717  C  CD1 . ILE A  1 340 ? 36.677  65.763  32.380  1.00 25.58 ?  364  ILE A CD1 1 
ATOM   2718  N  N   . ALA A  1 341 ? 31.912  67.589  34.365  1.00 26.96 ?  365  ALA A N   1 
ATOM   2719  C  CA  . ALA A  1 341 ? 30.532  68.042  34.165  1.00 27.22 ?  365  ALA A CA  1 
ATOM   2720  C  C   . ALA A  1 341 ? 30.447  69.566  34.102  1.00 27.20 ?  365  ALA A C   1 
ATOM   2721  O  O   . ALA A  1 341 ? 29.778  70.121  33.231  1.00 27.25 ?  365  ALA A O   1 
ATOM   2722  C  CB  . ALA A  1 341 ? 29.636  67.512  35.276  1.00 26.93 ?  365  ALA A CB  1 
ATOM   2723  N  N   . GLU A  1 342 ? 31.133  70.227  35.034  1.00 27.33 ?  366  GLU A N   1 
ATOM   2724  C  CA  . GLU A  1 342 ? 31.171  71.689  35.113  1.00 27.51 ?  366  GLU A CA  1 
ATOM   2725  C  C   . GLU A  1 342 ? 31.776  72.312  33.855  1.00 27.51 ?  366  GLU A C   1 
ATOM   2726  O  O   . GLU A  1 342 ? 31.478  73.455  33.518  1.00 27.57 ?  366  GLU A O   1 
ATOM   2727  C  CB  . GLU A  1 342 ? 31.964  72.138  36.350  1.00 27.45 ?  366  GLU A CB  1 
ATOM   2728  C  CG  . GLU A  1 342 ? 31.332  71.768  37.699  1.00 27.71 ?  366  GLU A CG  1 
ATOM   2729  C  CD  . GLU A  1 342 ? 31.750  70.394  38.216  1.00 28.39 ?  366  GLU A CD  1 
ATOM   2730  O  OE1 . GLU A  1 342 ? 32.233  69.550  37.421  1.00 29.34 ?  366  GLU A OE1 1 
ATOM   2731  O  OE2 . GLU A  1 342 ? 31.593  70.155  39.430  1.00 28.10 -1 366  GLU A OE2 1 
ATOM   2732  N  N   . ASN A  1 343 ? 32.626  71.548  33.174  1.00 27.74 ?  367  ASN A N   1 
ATOM   2733  C  CA  . ASN A  1 343 ? 33.326  72.005  31.977  1.00 27.96 ?  367  ASN A CA  1 
ATOM   2734  C  C   . ASN A  1 343 ? 32.540  71.797  30.680  1.00 28.27 ?  367  ASN A C   1 
ATOM   2735  O  O   . ASN A  1 343 ? 32.912  72.333  29.631  1.00 28.10 ?  367  ASN A O   1 
ATOM   2736  C  CB  . ASN A  1 343 ? 34.692  71.314  31.886  1.00 27.82 ?  367  ASN A CB  1 
ATOM   2737  C  CG  . ASN A  1 343 ? 35.499  71.750  30.678  1.00 27.80 ?  367  ASN A CG  1 
ATOM   2738  O  OD1 . ASN A  1 343 ? 35.757  72.938  30.482  1.00 27.39 ?  367  ASN A OD1 1 
ATOM   2739  N  ND2 . ASN A  1 343 ? 35.907  70.783  29.863  1.00 27.03 ?  367  ASN A ND2 1 
ATOM   2740  N  N   . ILE A  1 344 ? 31.453  71.031  30.746  1.00 28.84 ?  368  ILE A N   1 
ATOM   2741  C  CA  . ILE A  1 344 ? 30.720  70.653  29.529  1.00 29.61 ?  368  ILE A CA  1 
ATOM   2742  C  C   . ILE A  1 344 ? 30.089  71.843  28.775  1.00 30.05 ?  368  ILE A C   1 
ATOM   2743  O  O   . ILE A  1 344 ? 29.813  71.739  27.581  1.00 30.23 ?  368  ILE A O   1 
ATOM   2744  C  CB  . ILE A  1 344 ? 29.692  69.496  29.793  1.00 29.62 ?  368  ILE A CB  1 
ATOM   2745  C  CG1 . ILE A  1 344 ? 29.568  68.582  28.566  1.00 29.99 ?  368  ILE A CG1 1 
ATOM   2746  C  CG2 . ILE A  1 344 ? 28.330  70.030  30.233  1.00 29.44 ?  368  ILE A CG2 1 
ATOM   2747  C  CD1 . ILE A  1 344 ? 30.843  67.820  28.215  1.00 30.22 ?  368  ILE A CD1 1 
ATOM   2748  N  N   . THR A  1 345 ? 29.894  72.966  29.468  1.00 30.71 ?  369  THR A N   1 
ATOM   2749  C  CA  . THR A  1 345 ? 29.315  74.174  28.862  1.00 31.41 ?  369  THR A CA  1 
ATOM   2750  C  C   . THR A  1 345 ? 30.352  75.210  28.414  1.00 31.76 ?  369  THR A C   1 
ATOM   2751  O  O   . THR A  1 345 ? 29.985  76.243  27.851  1.00 32.19 ?  369  THR A O   1 
ATOM   2752  C  CB  . THR A  1 345 ? 28.299  74.871  29.810  1.00 31.41 ?  369  THR A CB  1 
ATOM   2753  O  OG1 . THR A  1 345 ? 28.925  75.155  31.068  1.00 32.14 ?  369  THR A OG1 1 
ATOM   2754  C  CG2 . THR A  1 345 ? 27.083  73.994  30.043  1.00 31.30 ?  369  THR A CG2 1 
ATOM   2755  N  N   . SER A  1 346 ? 31.635  74.939  28.659  1.00 32.05 ?  370  SER A N   1 
ATOM   2756  C  CA  . SER A  1 346 ? 32.706  75.880  28.315  1.00 32.36 ?  370  SER A CA  1 
ATOM   2757  C  C   . SER A  1 346 ? 32.892  76.019  26.801  1.00 32.58 ?  370  SER A C   1 
ATOM   2758  O  O   . SER A  1 346 ? 32.426  75.172  26.034  1.00 32.76 ?  370  SER A O   1 
ATOM   2759  C  CB  . SER A  1 346 ? 34.026  75.467  28.980  1.00 32.41 ?  370  SER A CB  1 
ATOM   2760  O  OG  . SER A  1 346 ? 34.575  74.304  28.380  1.00 32.38 ?  370  SER A OG  1 
ATOM   2761  N  N   . ASP A  1 347 ? 33.572  77.090  26.384  1.00 32.70 ?  371  ASP A N   1 
ATOM   2762  C  CA  . ASP A  1 347 ? 33.890  77.329  24.970  1.00 32.80 ?  371  ASP A CA  1 
ATOM   2763  C  C   . ASP A  1 347 ? 34.841  76.263  24.428  1.00 32.62 ?  371  ASP A C   1 
ATOM   2764  O  O   . ASP A  1 347 ? 34.808  75.927  23.240  1.00 32.46 ?  371  ASP A O   1 
ATOM   2765  C  CB  . ASP A  1 347 ? 34.523  78.712  24.781  1.00 32.92 ?  371  ASP A CB  1 
ATOM   2766  C  CG  . ASP A  1 347 ? 33.547  79.853  25.032  1.00 34.03 ?  371  ASP A CG  1 
ATOM   2767  O  OD1 . ASP A  1 347 ? 32.323  79.666  24.843  1.00 35.33 ?  371  ASP A OD1 1 
ATOM   2768  O  OD2 . ASP A  1 347 ? 34.013  80.950  25.408  1.00 34.55 -1 371  ASP A OD2 1 
ATOM   2769  N  N   . TRP A  1 348 ? 35.697  75.760  25.313  1.00 32.38 ?  372  TRP A N   1 
ATOM   2770  C  CA  . TRP A  1 348 ? 36.629  74.682  25.011  1.00 32.18 ?  372  TRP A CA  1 
ATOM   2771  C  C   . TRP A  1 348 ? 35.875  73.402  24.628  1.00 31.85 ?  372  TRP A C   1 
ATOM   2772  O  O   . TRP A  1 348 ? 36.168  72.787  23.603  1.00 31.96 ?  372  TRP A O   1 
ATOM   2773  C  CB  . TRP A  1 348 ? 37.534  74.453  26.223  1.00 32.15 ?  372  TRP A CB  1 
ATOM   2774  C  CG  . TRP A  1 348 ? 38.610  73.424  26.042  1.00 32.65 ?  372  TRP A CG  1 
ATOM   2775  C  CD1 . TRP A  1 348 ? 39.875  73.631  25.562  1.00 32.35 ?  372  TRP A CD1 1 
ATOM   2776  C  CD2 . TRP A  1 348 ? 38.529  72.031  26.373  1.00 32.78 ?  372  TRP A CD2 1 
ATOM   2777  N  NE1 . TRP A  1 348 ? 40.579  72.449  25.562  1.00 32.51 ?  372  TRP A NE1 1 
ATOM   2778  C  CE2 . TRP A  1 348 ? 39.778  71.453  26.058  1.00 32.60 ?  372  TRP A CE2 1 
ATOM   2779  C  CE3 . TRP A  1 348 ? 37.520  71.214  26.904  1.00 32.68 ?  372  TRP A CE3 1 
ATOM   2780  C  CZ2 . TRP A  1 348 ? 40.047  70.097  26.259  1.00 33.00 ?  372  TRP A CZ2 1 
ATOM   2781  C  CZ3 . TRP A  1 348 ? 37.786  69.863  27.096  1.00 32.58 ?  372  TRP A CZ3 1 
ATOM   2782  C  CH2 . TRP A  1 348 ? 39.040  69.320  26.773  1.00 32.60 ?  372  TRP A CH2 1 
ATOM   2783  N  N   . SER A  1 349 ? 34.894  73.024  25.444  1.00 31.50 ?  373  SER A N   1 
ATOM   2784  C  CA  . SER A  1 349 ? 34.073  71.843  25.182  1.00 31.25 ?  373  SER A CA  1 
ATOM   2785  C  C   . SER A  1 349 ? 33.143  72.057  23.991  1.00 31.10 ?  373  SER A C   1 
ATOM   2786  O  O   . SER A  1 349 ? 32.871  71.122  23.230  1.00 30.95 ?  373  SER A O   1 
ATOM   2787  C  CB  . SER A  1 349 ? 33.257  71.461  26.418  1.00 31.22 ?  373  SER A CB  1 
ATOM   2788  O  OG  . SER A  1 349 ? 34.101  71.155  27.516  1.00 31.19 ?  373  SER A OG  1 
ATOM   2789  N  N   . GLU A  1 350 ? 32.670  73.291  23.837  1.00 30.93 ?  374  GLU A N   1 
ATOM   2790  C  CA  . GLU A  1 350 ? 31.756  73.658  22.758  1.00 30.88 ?  374  GLU A CA  1 
ATOM   2791  C  C   . GLU A  1 350 ? 32.438  73.599  21.392  1.00 30.59 ?  374  GLU A C   1 
ATOM   2792  O  O   . GLU A  1 350 ? 31.811  73.221  20.402  1.00 30.76 ?  374  GLU A O   1 
ATOM   2793  C  CB  . GLU A  1 350 ? 31.157  75.048  23.014  1.00 31.00 ?  374  GLU A CB  1 
ATOM   2794  C  CG  . GLU A  1 350 ? 29.839  75.329  22.295  1.00 32.05 ?  374  GLU A CG  1 
ATOM   2795  C  CD  . GLU A  1 350 ? 28.665  74.482  22.794  1.00 33.09 ?  374  GLU A CD  1 
ATOM   2796  O  OE1 . GLU A  1 350 ? 28.747  73.875  23.887  1.00 34.24 ?  374  GLU A OE1 1 
ATOM   2797  O  OE2 . GLU A  1 350 ? 27.646  74.431  22.081  1.00 33.46 -1 374  GLU A OE2 1 
ATOM   2798  N  N   . ALA A  1 351 ? 33.717  73.970  21.346  1.00 30.07 ?  375  ALA A N   1 
ATOM   2799  C  CA  . ALA A  1 351 ? 34.505  73.885  20.116  1.00 29.76 ?  375  ALA A CA  1 
ATOM   2800  C  C   . ALA A  1 351 ? 34.755  72.433  19.713  1.00 29.40 ?  375  ALA A C   1 
ATOM   2801  O  O   . ALA A  1 351 ? 34.754  72.103  18.522  1.00 29.46 ?  375  ALA A O   1 
ATOM   2802  C  CB  . ALA A  1 351 ? 35.825  74.632  20.269  1.00 29.85 ?  375  ALA A CB  1 
ATOM   2803  N  N   . ARG A  1 352 ? 34.972  71.575  20.711  1.00 28.75 ?  376  ARG A N   1 
ATOM   2804  C  CA  . ARG A  1 352 ? 35.142  70.139  20.482  1.00 28.23 ?  376  ARG A CA  1 
ATOM   2805  C  C   . ARG A  1 352 ? 33.821  69.493  20.076  1.00 27.82 ?  376  ARG A C   1 
ATOM   2806  O  O   . ARG A  1 352 ? 33.813  68.499  19.347  1.00 27.73 ?  376  ARG A O   1 
ATOM   2807  C  CB  . ARG A  1 352 ? 35.749  69.451  21.714  1.00 28.14 ?  376  ARG A CB  1 
ATOM   2808  C  CG  . ARG A  1 352 ? 37.221  69.784  21.902  1.00 28.53 ?  376  ARG A CG  1 
ATOM   2809  C  CD  . ARG A  1 352 ? 37.811  69.291  23.210  1.00 28.77 ?  376  ARG A CD  1 
ATOM   2810  N  NE  . ARG A  1 352 ? 39.265  69.442  23.184  1.00 29.33 ?  376  ARG A NE  1 
ATOM   2811  C  CZ  . ARG A  1 352 ? 40.146  68.476  23.438  1.00 29.83 ?  376  ARG A CZ  1 
ATOM   2812  N  NH1 . ARG A  1 352 ? 39.744  67.259  23.785  1.00 29.45 ?  376  ARG A NH1 1 
ATOM   2813  N  NH2 . ARG A  1 352 ? 41.446  68.739  23.365  1.00 29.71 ?  376  ARG A NH2 1 
ATOM   2814  N  N   . LEU A  1 353 ? 32.713  70.068  20.542  1.00 27.36 ?  377  LEU A N   1 
ATOM   2815  C  CA  . LEU A  1 353 ? 31.383  69.647  20.107  1.00 27.11 ?  377  LEU A CA  1 
ATOM   2816  C  C   . LEU A  1 353 ? 31.161  69.938  18.622  1.00 26.93 ?  377  LEU A C   1 
ATOM   2817  O  O   . LEU A  1 353 ? 30.687  69.065  17.887  1.00 26.90 ?  377  LEU A O   1 
ATOM   2818  C  CB  . LEU A  1 353 ? 30.283  70.289  20.961  1.00 27.00 ?  377  LEU A CB  1 
ATOM   2819  C  CG  . LEU A  1 353 ? 28.832  69.914  20.630  1.00 26.87 ?  377  LEU A CG  1 
ATOM   2820  C  CD1 . LEU A  1 353 ? 28.600  68.403  20.735  1.00 27.12 ?  377  LEU A CD1 1 
ATOM   2821  C  CD2 . LEU A  1 353 ? 27.855  70.676  21.515  1.00 26.18 ?  377  LEU A CD2 1 
ATOM   2822  N  N   . ASP A  1 354 ? 31.514  71.152  18.187  1.00 26.64 ?  378  ASP A N   1 
ATOM   2823  C  CA  . ASP A  1 354 ? 31.449  71.518  16.766  1.00 26.72 ?  378  ASP A CA  1 
ATOM   2824  C  C   . ASP A  1 354 ? 32.233  70.526  15.906  1.00 26.32 ?  378  ASP A C   1 
ATOM   2825  O  O   . ASP A  1 354 ? 31.784  70.154  14.823  1.00 26.19 ?  378  ASP A O   1 
ATOM   2826  C  CB  . ASP A  1 354 ? 31.983  72.941  16.514  1.00 26.94 ?  378  ASP A CB  1 
ATOM   2827  C  CG  . ASP A  1 354 ? 31.107  74.032  17.125  1.00 27.61 ?  378  ASP A CG  1 
ATOM   2828  O  OD1 . ASP A  1 354 ? 29.900  73.808  17.360  1.00 28.47 ?  378  ASP A OD1 1 
ATOM   2829  O  OD2 . ASP A  1 354 ? 31.640  75.139  17.357  1.00 29.48 -1 378  ASP A OD2 1 
ATOM   2830  N  N   . SER A  1 355 ? 33.404  70.113  16.397  1.00 26.01 ?  379  SER A N   1 
ATOM   2831  C  CA  . SER A  1 355 ? 34.235  69.109  15.726  1.00 25.85 ?  379  SER A CA  1 
ATOM   2832  C  C   . SER A  1 355 ? 33.532  67.752  15.605  1.00 25.70 ?  379  SER A C   1 
ATOM   2833  O  O   . SER A  1 355 ? 33.596  67.117  14.551  1.00 25.68 ?  379  SER A O   1 
ATOM   2834  C  CB  . SER A  1 355 ? 35.585  68.950  16.436  1.00 25.91 ?  379  SER A CB  1 
ATOM   2835  O  OG  . SER A  1 355 ? 36.379  70.121  16.309  1.00 25.81 ?  379  SER A OG  1 
ATOM   2836  N  N   . TRP A  1 356 ? 32.863  67.313  16.674  1.00 25.35 ?  380  TRP A N   1 
ATOM   2837  C  CA  . TRP A  1 356 ? 32.076  66.073  16.625  1.00 25.09 ?  380  TRP A CA  1 
ATOM   2838  C  C   . TRP A  1 356 ? 30.941  66.166  15.607  1.00 25.14 ?  380  TRP A C   1 
ATOM   2839  O  O   . TRP A  1 356 ? 30.737  65.253  14.808  1.00 24.89 ?  380  TRP A O   1 
ATOM   2840  C  CB  . TRP A  1 356 ? 31.517  65.700  18.004  1.00 24.80 ?  380  TRP A CB  1 
ATOM   2841  C  CG  . TRP A  1 356 ? 32.449  64.866  18.837  1.00 24.20 ?  380  TRP A CG  1 
ATOM   2842  C  CD1 . TRP A  1 356 ? 32.988  65.203  20.042  1.00 23.76 ?  380  TRP A CD1 1 
ATOM   2843  C  CD2 . TRP A  1 356 ? 32.945  63.552  18.529  1.00 23.39 ?  380  TRP A CD2 1 
ATOM   2844  N  NE1 . TRP A  1 356 ? 33.793  64.190  20.503  1.00 23.67 ?  380  TRP A NE1 1 
ATOM   2845  C  CE2 . TRP A  1 356 ? 33.788  63.165  19.594  1.00 23.49 ?  380  TRP A CE2 1 
ATOM   2846  C  CE3 . TRP A  1 356 ? 32.767  62.671  17.453  1.00 23.48 ?  380  TRP A CE3 1 
ATOM   2847  C  CZ2 . TRP A  1 356 ? 34.450  61.930  19.620  1.00 23.17 ?  380  TRP A CZ2 1 
ATOM   2848  C  CZ3 . TRP A  1 356 ? 33.427  61.442  17.477  1.00 23.32 ?  380  TRP A CZ3 1 
ATOM   2849  C  CH2 . TRP A  1 356 ? 34.260  61.086  18.554  1.00 23.13 ?  380  TRP A CH2 1 
ATOM   2850  N  N   . VAL A  1 357 ? 30.214  67.280  15.645  1.00 25.32 ?  381  VAL A N   1 
ATOM   2851  C  CA  . VAL A  1 357 ? 29.103  67.532  14.732  1.00 25.44 ?  381  VAL A CA  1 
ATOM   2852  C  C   . VAL A  1 357 ? 29.562  67.366  13.281  1.00 25.78 ?  381  VAL A C   1 
ATOM   2853  O  O   . VAL A  1 357 ? 28.904  66.681  12.492  1.00 25.94 ?  381  VAL A O   1 
ATOM   2854  C  CB  . VAL A  1 357 ? 28.477  68.932  14.987  1.00 25.46 ?  381  VAL A CB  1 
ATOM   2855  C  CG1 . VAL A  1 357 ? 27.524  69.330  13.865  1.00 25.55 ?  381  VAL A CG1 1 
ATOM   2856  C  CG2 . VAL A  1 357 ? 27.759  68.946  16.328  1.00 25.21 ?  381  VAL A CG2 1 
ATOM   2857  N  N   . LEU A  1 358 ? 30.708  67.966  12.957  1.00 25.80 ?  382  LEU A N   1 
ATOM   2858  C  CA  . LEU A  1 358 ? 31.336  67.824  11.647  1.00 26.03 ?  382  LEU A CA  1 
ATOM   2859  C  C   . LEU A  1 358 ? 31.484  66.350  11.262  1.00 25.83 ?  382  LEU A C   1 
ATOM   2860  O  O   . LEU A  1 358 ? 31.072  65.947  10.168  1.00 26.08 ?  382  LEU A O   1 
ATOM   2861  C  CB  . LEU A  1 358 ? 32.716  68.486  11.651  1.00 26.15 ?  382  LEU A CB  1 
ATOM   2862  C  CG  . LEU A  1 358 ? 33.206  69.412  10.531  1.00 27.16 ?  382  LEU A CG  1 
ATOM   2863  C  CD1 . LEU A  1 358 ? 34.640  69.037  10.173  1.00 27.44 ?  382  LEU A CD1 1 
ATOM   2864  C  CD2 . LEU A  1 358 ? 32.326  69.421  9.282   1.00 27.39 ?  382  LEU A CD2 1 
ATOM   2865  N  N   . THR A  1 359 ? 32.078  65.564  12.163  1.00 25.34 ?  383  THR A N   1 
ATOM   2866  C  CA  . THR A  1 359 ? 32.243  64.115  11.989  1.00 25.15 ?  383  THR A CA  1 
ATOM   2867  C  C   . THR A  1 359 ? 30.929  63.426  11.610  1.00 24.96 ?  383  THR A C   1 
ATOM   2868  O  O   . THR A  1 359 ? 30.889  62.643  10.660  1.00 24.90 ?  383  THR A O   1 
ATOM   2869  C  CB  . THR A  1 359 ? 32.801  63.450  13.278  1.00 25.05 ?  383  THR A CB  1 
ATOM   2870  O  OG1 . THR A  1 359 ? 33.994  64.124  13.693  1.00 24.75 ?  383  THR A OG1 1 
ATOM   2871  C  CG2 . THR A  1 359 ? 33.101  61.967  13.057  1.00 24.73 ?  383  THR A CG2 1 
ATOM   2872  N  N   . CYS A  1 360 ? 29.866  63.730  12.354  1.00 24.75 ?  384  CYS A N   1 
ATOM   2873  C  CA  . CYS A  1 360 ? 28.546  63.134  12.119  1.00 24.76 ?  384  CYS A CA  1 
ATOM   2874  C  C   . CYS A  1 360 ? 27.941  63.521  10.771  1.00 24.92 ?  384  CYS A C   1 
ATOM   2875  O  O   . CYS A  1 360 ? 27.250  62.703  10.148  1.00 25.03 ?  384  CYS A O   1 
ATOM   2876  C  CB  . CYS A  1 360 ? 27.571  63.510  13.236  1.00 24.52 ?  384  CYS A CB  1 
ATOM   2877  S  SG  . CYS A  1 360 ? 28.161  63.180  14.901  1.00 23.78 ?  384  CYS A SG  1 
ATOM   2878  N  N   . THR A  1 361 ? 28.207  64.753  10.322  1.00 25.03 ?  385  THR A N   1 
ATOM   2879  C  CA  . THR A  1 361 ? 27.599  65.282  9.087   1.00 25.31 ?  385  THR A CA  1 
ATOM   2880  C  C   . THR A  1 361 ? 28.149  64.661  7.802   1.00 25.51 ?  385  THR A C   1 
ATOM   2881  O  O   . THR A  1 361 ? 27.696  64.995  6.702   1.00 25.76 ?  385  THR A O   1 
ATOM   2882  C  CB  . THR A  1 361 ? 27.650  66.830  8.989   1.00 25.25 ?  385  THR A CB  1 
ATOM   2883  O  OG1 . THR A  1 361 ? 29.007  67.282  9.072   1.00 26.22 ?  385  THR A OG1 1 
ATOM   2884  C  CG2 . THR A  1 361 ? 26.819  67.463  10.087  1.00 24.51 ?  385  THR A CG2 1 
ATOM   2885  N  N   . GLN A  1 362 ? 29.123  63.767  7.944   1.00 25.62 ?  386  GLN A N   1 
ATOM   2886  C  CA  . GLN A  1 362 ? 29.520  62.879  6.857   1.00 25.91 ?  386  GLN A CA  1 
ATOM   2887  C  C   . GLN A  1 362 ? 28.279  62.157  6.327   1.00 25.64 ?  386  GLN A C   1 
ATOM   2888  O  O   . GLN A  1 362 ? 28.223  61.764  5.158   1.00 25.69 ?  386  GLN A O   1 
ATOM   2889  C  CB  . GLN A  1 362 ? 30.540  61.858  7.368   1.00 26.22 ?  386  GLN A CB  1 
ATOM   2890  C  CG  . GLN A  1 362 ? 31.206  61.010  6.290   1.00 28.01 ?  386  GLN A CG  1 
ATOM   2891  C  CD  . GLN A  1 362 ? 32.218  61.782  5.456   1.00 29.71 ?  386  GLN A CD  1 
ATOM   2892  O  OE1 . GLN A  1 362 ? 32.176  61.740  4.225   1.00 31.31 ?  386  GLN A OE1 1 
ATOM   2893  N  NE2 . GLN A  1 362 ? 33.134  62.482  6.120   1.00 29.91 ?  386  GLN A NE2 1 
ATOM   2894  N  N   . CYS A  1 363 ? 27.283  62.007  7.200   1.00 25.30 ?  387  CYS A N   1 
ATOM   2895  C  CA  . CYS A  1 363 ? 26.059  61.282  6.884   1.00 24.96 ?  387  CYS A CA  1 
ATOM   2896  C  C   . CYS A  1 363 ? 24.813  62.045  7.338   1.00 24.92 ?  387  CYS A C   1 
ATOM   2897  O  O   . CYS A  1 363 ? 24.006  62.459  6.513   1.00 24.94 ?  387  CYS A O   1 
ATOM   2898  C  CB  . CYS A  1 363 ? 26.100  59.889  7.518   1.00 24.78 ?  387  CYS A CB  1 
ATOM   2899  S  SG  . CYS A  1 363 ? 27.671  59.026  7.266   1.00 23.59 ?  387  CYS A SG  1 
ATOM   2900  N  N   . HIS A  1 364 ? 24.666  62.230  8.649   1.00 24.96 ?  388  HIS A N   1 
ATOM   2901  C  CA  . HIS A  1 364 ? 23.505  62.920  9.214   1.00 25.13 ?  388  HIS A CA  1 
ATOM   2902  C  C   . HIS A  1 364 ? 23.545  64.431  8.945   1.00 25.52 ?  388  HIS A C   1 
ATOM   2903  O  O   . HIS A  1 364 ? 24.608  64.995  8.669   1.00 25.43 ?  388  HIS A O   1 
ATOM   2904  C  CB  . HIS A  1 364 ? 23.410  62.671  10.726  1.00 24.96 ?  388  HIS A CB  1 
ATOM   2905  C  CG  . HIS A  1 364 ? 23.351  61.223  11.113  1.00 24.54 ?  388  HIS A CG  1 
ATOM   2906  N  ND1 . HIS A  1 364 ? 22.262  60.421  10.844  1.00 23.45 ?  388  HIS A ND1 1 
ATOM   2907  C  CD2 . HIS A  1 364 ? 24.236  60.442  11.779  1.00 23.65 ?  388  HIS A CD2 1 
ATOM   2908  C  CE1 . HIS A  1 364 ? 22.486  59.206  11.314  1.00 23.37 ?  388  HIS A CE1 1 
ATOM   2909  N  NE2 . HIS A  1 364 ? 23.675  59.192  11.889  1.00 23.49 ?  388  HIS A NE2 1 
ATOM   2910  N  N   . SER A  1 365 ? 22.388  65.086  9.020   1.00 25.77 ?  389  SER A N   1 
ATOM   2911  C  CA  . SER A  1 365 ? 22.348  66.547  9.000   1.00 25.84 ?  389  SER A CA  1 
ATOM   2912  C  C   . SER A  1 365 ? 22.924  67.089  10.306  1.00 26.03 ?  389  SER A C   1 
ATOM   2913  O  O   . SER A  1 365 ? 22.988  66.368  11.309  1.00 25.93 ?  389  SER A O   1 
ATOM   2914  C  CB  . SER A  1 365 ? 20.921  67.062  8.793   1.00 25.81 ?  389  SER A CB  1 
ATOM   2915  O  OG  . SER A  1 365 ? 20.089  66.743  9.894   1.00 25.78 ?  389  SER A OG  1 
ATOM   2916  N  N   . GLU A  1 366 ? 23.347  68.351  10.285  1.00 26.22 ?  390  GLU A N   1 
ATOM   2917  C  CA  . GLU A  1 366 ? 23.893  69.013  11.469  1.00 26.65 ?  390  GLU A CA  1 
ATOM   2918  C  C   . GLU A  1 366 ? 22.866  69.055  12.601  1.00 26.62 ?  390  GLU A C   1 
ATOM   2919  O  O   . GLU A  1 366 ? 23.192  68.777  13.760  1.00 26.73 ?  390  GLU A O   1 
ATOM   2920  C  CB  . GLU A  1 366 ? 24.383  70.425  11.117  1.00 26.72 ?  390  GLU A CB  1 
ATOM   2921  C  CG  . GLU A  1 366 ? 24.763  71.272  12.325  1.00 27.62 ?  390  GLU A CG  1 
ATOM   2922  C  CD  . GLU A  1 366 ? 25.538  72.526  11.974  1.00 28.91 ?  390  GLU A CD  1 
ATOM   2923  O  OE1 . GLU A  1 366 ? 25.716  72.824  10.772  1.00 29.19 ?  390  GLU A OE1 1 
ATOM   2924  O  OE2 . GLU A  1 366 ? 25.968  73.221  12.919  1.00 29.62 -1 390  GLU A OE2 1 
ATOM   2925  N  N   . ARG A  1 367 ? 21.627  69.385  12.236  1.00 26.59 ?  391  ARG A N   1 
ATOM   2926  C  CA  . ARG A  1 367 ? 20.504  69.502  13.162  1.00 26.44 ?  391  ARG A CA  1 
ATOM   2927  C  C   . ARG A  1 367 ? 20.202  68.179  13.864  1.00 26.32 ?  391  ARG A C   1 
ATOM   2928  O  O   . ARG A  1 367 ? 19.895  68.162  15.058  1.00 26.48 ?  391  ARG A O   1 
ATOM   2929  C  CB  . ARG A  1 367 ? 19.267  69.976  12.393  1.00 26.54 ?  391  ARG A CB  1 
ATOM   2930  C  CG  . ARG A  1 367 ? 18.088  70.408  13.248  1.00 26.16 ?  391  ARG A CG  1 
ATOM   2931  C  CD  . ARG A  1 367 ? 16.837  70.404  12.398  1.00 26.82 ?  391  ARG A CD  1 
ATOM   2932  N  NE  . ARG A  1 367 ? 15.711  71.077  13.035  1.00 26.64 ?  391  ARG A NE  1 
ATOM   2933  C  CZ  . ARG A  1 367 ? 14.500  71.174  12.496  1.00 27.10 ?  391  ARG A CZ  1 
ATOM   2934  N  NH1 . ARG A  1 367 ? 14.248  70.627  11.311  1.00 26.29 ?  391  ARG A NH1 1 
ATOM   2935  N  NH2 . ARG A  1 367 ? 13.533  71.806  13.148  1.00 26.86 ?  391  ARG A NH2 1 
ATOM   2936  N  N   . PHE A  1 368 ? 20.269  67.082  13.110  1.00 26.15 ?  392  PHE A N   1 
ATOM   2937  C  CA  . PHE A  1 368 ? 20.078  65.742  13.660  1.00 25.91 ?  392  PHE A CA  1 
ATOM   2938  C  C   . PHE A  1 368 ? 21.178  65.424  14.677  1.00 25.95 ?  392  PHE A C   1 
ATOM   2939  O  O   . PHE A  1 368 ? 20.892  65.006  15.799  1.00 26.06 ?  392  PHE A O   1 
ATOM   2940  C  CB  . PHE A  1 368 ? 20.047  64.692  12.535  1.00 25.86 ?  392  PHE A CB  1 
ATOM   2941  C  CG  . PHE A  1 368 ? 19.833  63.279  13.020  1.00 25.64 ?  392  PHE A CG  1 
ATOM   2942  C  CD1 . PHE A  1 368 ? 20.918  62.462  13.334  1.00 25.49 ?  392  PHE A CD1 1 
ATOM   2943  C  CD2 . PHE A  1 368 ? 18.547  62.767  13.164  1.00 25.05 ?  392  PHE A CD2 1 
ATOM   2944  C  CE1 . PHE A  1 368 ? 20.724  61.153  13.788  1.00 25.49 ?  392  PHE A CE1 1 
ATOM   2945  C  CE2 . PHE A  1 368 ? 18.345  61.465  13.622  1.00 25.20 ?  392  PHE A CE2 1 
ATOM   2946  C  CZ  . PHE A  1 368 ? 19.438  60.658  13.933  1.00 25.10 ?  392  PHE A CZ  1 
ATOM   2947  N  N   . ALA A  1 369 ? 22.428  65.642  14.278  1.00 25.93 ?  393  ALA A N   1 
ATOM   2948  C  CA  . ALA A  1 369 ? 23.584  65.336  15.116  1.00 26.25 ?  393  ALA A CA  1 
ATOM   2949  C  C   . ALA A  1 369 ? 23.592  66.143  16.414  1.00 26.33 ?  393  ALA A C   1 
ATOM   2950  O  O   . ALA A  1 369 ? 23.842  65.591  17.489  1.00 26.41 ?  393  ALA A O   1 
ATOM   2951  C  CB  . ALA A  1 369 ? 24.877  65.550  14.339  1.00 26.36 ?  393  ALA A CB  1 
ATOM   2952  N  N   . ARG A  1 370 ? 23.294  67.438  16.307  1.00 26.18 ?  394  ARG A N   1 
ATOM   2953  C  CA  . ARG A  1 370 ? 23.201  68.312  17.474  1.00 26.15 ?  394  ARG A CA  1 
ATOM   2954  C  C   . ARG A  1 370 ? 22.065  67.908  18.415  1.00 25.84 ?  394  ARG A C   1 
ATOM   2955  O  O   . ARG A  1 370 ? 22.212  67.994  19.633  1.00 25.72 ?  394  ARG A O   1 
ATOM   2956  C  CB  . ARG A  1 370 ? 23.055  69.779  17.052  1.00 26.26 ?  394  ARG A CB  1 
ATOM   2957  C  CG  . ARG A  1 370 ? 24.323  70.361  16.436  1.00 26.85 ?  394  ARG A CG  1 
ATOM   2958  C  CD  . ARG A  1 370 ? 24.212  71.866  16.195  1.00 27.82 ?  394  ARG A CD  1 
ATOM   2959  N  NE  . ARG A  1 370 ? 25.409  72.380  15.529  1.00 28.45 ?  394  ARG A NE  1 
ATOM   2960  C  CZ  . ARG A  1 370 ? 26.530  72.737  16.151  1.00 28.57 ?  394  ARG A CZ  1 
ATOM   2961  N  NH1 . ARG A  1 370 ? 26.630  72.652  17.473  1.00 28.36 ?  394  ARG A NH1 1 
ATOM   2962  N  NH2 . ARG A  1 370 ? 27.558  73.182  15.443  1.00 29.05 ?  394  ARG A NH2 1 
ATOM   2963  N  N   . SER A  1 371 ? 20.947  67.464  17.842  1.00 25.60 ?  395  SER A N   1 
ATOM   2964  C  CA  . SER A  1 371 ? 19.820  66.945  18.622  1.00 25.37 ?  395  SER A CA  1 
ATOM   2965  C  C   . SER A  1 371 ? 20.224  65.737  19.462  1.00 24.99 ?  395  SER A C   1 
ATOM   2966  O  O   . SER A  1 371 ? 19.880  65.661  20.642  1.00 25.02 ?  395  SER A O   1 
ATOM   2967  C  CB  . SER A  1 371 ? 18.641  66.574  17.714  1.00 25.43 ?  395  SER A CB  1 
ATOM   2968  O  OG  . SER A  1 371 ? 18.137  67.713  17.033  1.00 26.05 ?  395  SER A OG  1 
ATOM   2969  N  N   . TYR A  1 372 ? 20.956  64.798  18.864  1.00 24.56 ?  396  TYR A N   1 
ATOM   2970  C  CA  . TYR A  1 372 ? 21.375  63.613  19.612  1.00 24.27 ?  396  TYR A CA  1 
ATOM   2971  C  C   . TYR A  1 372 ? 22.500  63.877  20.618  1.00 24.14 ?  396  TYR A C   1 
ATOM   2972  O  O   . TYR A  1 372 ? 22.488  63.321  21.718  1.00 24.05 ?  396  TYR A O   1 
ATOM   2973  C  CB  . TYR A  1 372 ? 21.742  62.421  18.711  1.00 24.18 ?  396  TYR A CB  1 
ATOM   2974  C  CG  . TYR A  1 372 ? 21.991  61.191  19.556  1.00 23.79 ?  396  TYR A CG  1 
ATOM   2975  C  CD1 . TYR A  1 372 ? 20.925  60.439  20.047  1.00 22.85 ?  396  TYR A CD1 1 
ATOM   2976  C  CD2 . TYR A  1 372 ? 23.287  60.831  19.936  1.00 22.58 ?  396  TYR A CD2 1 
ATOM   2977  C  CE1 . TYR A  1 372 ? 21.140  59.339  20.851  1.00 22.68 ?  396  TYR A CE1 1 
ATOM   2978  C  CE2 . TYR A  1 372 ? 23.511  59.740  20.743  1.00 22.84 ?  396  TYR A CE2 1 
ATOM   2979  C  CZ  . TYR A  1 372 ? 22.434  58.994  21.196  1.00 22.78 ?  396  TYR A CZ  1 
ATOM   2980  O  OH  . TYR A  1 372 ? 22.647  57.903  21.996  1.00 22.85 ?  396  TYR A OH  1 
ATOM   2981  N  N   . LEU A  1 373 ? 23.467  64.714  20.247  1.00 23.98 ?  397  LEU A N   1 
ATOM   2982  C  CA  . LEU A  1 373 ? 24.587  65.004  21.147  1.00 23.85 ?  397  LEU A CA  1 
ATOM   2983  C  C   . LEU A  1 373 ? 24.125  65.793  22.372  1.00 23.80 ?  397  LEU A C   1 
ATOM   2984  O  O   . LEU A  1 373 ? 24.689  65.649  23.458  1.00 24.00 ?  397  LEU A O   1 
ATOM   2985  C  CB  . LEU A  1 373 ? 25.744  65.696  20.408  1.00 23.66 ?  397  LEU A CB  1 
ATOM   2986  C  CG  . LEU A  1 373 ? 26.451  64.854  19.332  1.00 22.98 ?  397  LEU A CG  1 
ATOM   2987  C  CD1 . LEU A  1 373 ? 27.309  65.716  18.416  1.00 20.83 ?  397  LEU A CD1 1 
ATOM   2988  C  CD2 . LEU A  1 373 ? 27.274  63.705  19.934  1.00 21.90 ?  397  LEU A CD2 1 
ATOM   2989  N  N   . ASP A  1 374 ? 23.082  66.600  22.194  1.00 23.96 ?  398  ASP A N   1 
ATOM   2990  C  CA  . ASP A  1 374 ? 22.420  67.277  23.311  1.00 24.01 ?  398  ASP A CA  1 
ATOM   2991  C  C   . ASP A  1 374 ? 21.796  66.253  24.258  1.00 23.80 ?  398  ASP A C   1 
ATOM   2992  O  O   . ASP A  1 374 ? 21.888  66.387  25.481  1.00 23.80 ?  398  ASP A O   1 
ATOM   2993  C  CB  . ASP A  1 374 ? 21.346  68.237  22.796  1.00 24.31 ?  398  ASP A CB  1 
ATOM   2994  C  CG  . ASP A  1 374 ? 20.633  68.966  23.915  1.00 25.13 ?  398  ASP A CG  1 
ATOM   2995  O  OD1 . ASP A  1 374 ? 19.471  68.614  24.209  1.00 26.01 ?  398  ASP A OD1 1 
ATOM   2996  O  OD2 . ASP A  1 374 ? 21.241  69.880  24.510  1.00 27.40 -1 398  ASP A OD2 1 
ATOM   2997  N  N   . LEU A  1 375 ? 21.162  65.237  23.674  1.00 23.61 ?  399  LEU A N   1 
ATOM   2998  C  CA  . LEU A  1 375 ? 20.608  64.116  24.423  1.00 23.41 ?  399  LEU A CA  1 
ATOM   2999  C  C   . LEU A  1 375 ? 21.715  63.417  25.217  1.00 23.15 ?  399  LEU A C   1 
ATOM   3000  O  O   . LEU A  1 375 ? 21.545  63.138  26.408  1.00 23.22 ?  399  LEU A O   1 
ATOM   3001  C  CB  . LEU A  1 375 ? 19.899  63.134  23.472  1.00 23.31 ?  399  LEU A CB  1 
ATOM   3002  C  CG  . LEU A  1 375 ? 19.061  61.953  23.988  1.00 23.22 ?  399  LEU A CG  1 
ATOM   3003  C  CD1 . LEU A  1 375 ? 18.180  61.397  22.883  1.00 22.81 ?  399  LEU A CD1 1 
ATOM   3004  C  CD2 . LEU A  1 375 ? 19.917  60.837  24.566  1.00 23.03 ?  399  LEU A CD2 1 
ATOM   3005  N  N   . MET A  1 376 ? 22.841  63.154  24.554  1.00 22.81 ?  400  MET A N   1 
ATOM   3006  C  CA  . MET A  1 376 ? 23.982  62.473  25.172  1.00 22.79 ?  400  MET A CA  1 
ATOM   3007  C  C   . MET A  1 376 ? 24.500  63.233  26.393  1.00 22.76 ?  400  MET A C   1 
ATOM   3008  O  O   . MET A  1 376 ? 24.713  62.639  27.453  1.00 22.44 ?  400  MET A O   1 
ATOM   3009  C  CB  . MET A  1 376 ? 25.108  62.265  24.149  1.00 22.68 ?  400  MET A CB  1 
ATOM   3010  C  CG  . MET A  1 376 ? 26.408  61.691  24.726  1.00 22.43 ?  400  MET A CG  1 
ATOM   3011  S  SD  . MET A  1 376 ? 27.857  61.972  23.674  1.00 22.90 ?  400  MET A SD  1 
ATOM   3012  C  CE  . MET A  1 376 ? 28.093  63.740  23.886  1.00 22.14 ?  400  MET A CE  1 
ATOM   3013  N  N   . ASP A  1 377 ? 24.686  64.545  26.233  1.00 22.91 ?  401  ASP A N   1 
ATOM   3014  C  CA  . ASP A  1 377 ? 25.177  65.400  27.310  1.00 23.17 ?  401  ASP A CA  1 
ATOM   3015  C  C   . ASP A  1 377 ? 24.230  65.407  28.501  1.00 23.21 ?  401  ASP A C   1 
ATOM   3016  O  O   . ASP A  1 377 ? 24.666  65.245  29.639  1.00 23.53 ?  401  ASP A O   1 
ATOM   3017  C  CB  . ASP A  1 377 ? 25.424  66.833  26.813  1.00 23.23 ?  401  ASP A CB  1 
ATOM   3018  C  CG  . ASP A  1 377 ? 26.712  66.967  26.008  1.00 23.74 ?  401  ASP A CG  1 
ATOM   3019  O  OD1 . ASP A  1 377 ? 27.602  66.092  26.122  1.00 22.73 ?  401  ASP A OD1 1 
ATOM   3020  O  OD2 . ASP A  1 377 ? 26.835  67.960  25.257  1.00 24.51 -1 401  ASP A OD2 1 
ATOM   3021  N  N   . LYS A  1 378 ? 22.936  65.568  28.232  1.00 23.33 ?  402  LYS A N   1 
ATOM   3022  C  CA  . LYS A  1 378 ? 21.934  65.675  29.295  1.00 23.50 ?  402  LYS A CA  1 
ATOM   3023  C  C   . LYS A  1 378 ? 21.608  64.340  29.953  1.00 23.34 ?  402  LYS A C   1 
ATOM   3024  O  O   . LYS A  1 378 ? 21.417  64.276  31.166  1.00 23.55 ?  402  LYS A O   1 
ATOM   3025  C  CB  . LYS A  1 378 ? 20.665  66.357  28.784  1.00 23.54 ?  402  LYS A CB  1 
ATOM   3026  C  CG  . LYS A  1 378 ? 20.797  67.861  28.684  1.00 24.19 ?  402  LYS A CG  1 
ATOM   3027  C  CD  . LYS A  1 378 ? 19.628  68.476  27.942  1.00 25.85 ?  402  LYS A CD  1 
ATOM   3028  C  CE  . LYS A  1 378 ? 19.890  69.943  27.648  1.00 26.13 ?  402  LYS A CE  1 
ATOM   3029  N  NZ  . LYS A  1 378 ? 19.016  70.427  26.547  1.00 27.14 ?  402  LYS A NZ  1 
ATOM   3030  N  N   . GLY A  1 379 ? 21.549  63.278  29.154  1.00 23.10 ?  403  GLY A N   1 
ATOM   3031  C  CA  . GLY A  1 379 ? 21.379  61.927  29.687  1.00 22.83 ?  403  GLY A CA  1 
ATOM   3032  C  C   . GLY A  1 379 ? 22.506  61.568  30.637  1.00 22.63 ?  403  GLY A C   1 
ATOM   3033  O  O   . GLY A  1 379 ? 22.280  60.949  31.675  1.00 22.50 ?  403  GLY A O   1 
ATOM   3034  N  N   . THR A  1 380 ? 23.722  61.974  30.274  1.00 22.73 ?  404  THR A N   1 
ATOM   3035  C  CA  . THR A  1 380 ? 24.915  61.741  31.087  1.00 22.46 ?  404  THR A CA  1 
ATOM   3036  C  C   . THR A  1 380 ? 24.817  62.458  32.437  1.00 22.62 ?  404  THR A C   1 
ATOM   3037  O  O   . THR A  1 380 ? 25.079  61.858  33.485  1.00 22.73 ?  404  THR A O   1 
ATOM   3038  C  CB  . THR A  1 380 ? 26.191  62.169  30.328  1.00 22.41 ?  404  THR A CB  1 
ATOM   3039  O  OG1 . THR A  1 380 ? 26.290  61.421  29.107  1.00 22.68 ?  404  THR A OG1 1 
ATOM   3040  C  CG2 . THR A  1 380 ? 27.444  61.929  31.161  1.00 22.12 ?  404  THR A CG2 1 
ATOM   3041  N  N   . LEU A  1 381 ? 24.421  63.731  32.409  1.00 22.43 ?  405  LEU A N   1 
ATOM   3042  C  CA  . LEU A  1 381 ? 24.248  64.511  33.635  1.00 22.32 ?  405  LEU A CA  1 
ATOM   3043  C  C   . LEU A  1 381 ? 23.132  63.946  34.528  1.00 22.37 ?  405  LEU A C   1 
ATOM   3044  O  O   . LEU A  1 381 ? 23.242  63.967  35.761  1.00 21.97 ?  405  LEU A O   1 
ATOM   3045  C  CB  . LEU A  1 381 ? 23.989  65.986  33.309  1.00 22.27 ?  405  LEU A CB  1 
ATOM   3046  C  CG  . LEU A  1 381 ? 25.123  66.816  32.690  1.00 22.42 ?  405  LEU A CG  1 
ATOM   3047  C  CD1 . LEU A  1 381 ? 24.568  68.045  31.986  1.00 22.27 ?  405  LEU A CD1 1 
ATOM   3048  C  CD2 . LEU A  1 381 ? 26.169  67.217  33.733  1.00 21.96 ?  405  LEU A CD2 1 
ATOM   3049  N  N   . GLU A  1 382 ? 22.069  63.438  33.901  1.00 22.23 ?  406  GLU A N   1 
ATOM   3050  C  CA  . GLU A  1 382 ? 20.963  62.805  34.633  1.00 22.35 ?  406  GLU A CA  1 
ATOM   3051  C  C   . GLU A  1 382 ? 21.422  61.561  35.400  1.00 22.26 ?  406  GLU A C   1 
ATOM   3052  O  O   . GLU A  1 382 ? 20.987  61.320  36.525  1.00 22.21 ?  406  GLU A O   1 
ATOM   3053  C  CB  . GLU A  1 382 ? 19.805  62.471  33.684  1.00 22.43 ?  406  GLU A CB  1 
ATOM   3054  C  CG  . GLU A  1 382 ? 18.962  63.683  33.310  1.00 22.92 ?  406  GLU A CG  1 
ATOM   3055  C  CD  . GLU A  1 382 ? 18.327  63.585  31.930  1.00 24.82 ?  406  GLU A CD  1 
ATOM   3056  O  OE1 . GLU A  1 382 ? 18.176  62.465  31.390  1.00 24.91 ?  406  GLU A OE1 1 
ATOM   3057  O  OE2 . GLU A  1 382 ? 17.971  64.648  31.382  1.00 25.33 -1 406  GLU A OE2 1 
ATOM   3058  N  N   . GLY A  1 383 ? 22.303  60.778  34.782  1.00 22.24 ?  407  GLY A N   1 
ATOM   3059  C  CA  . GLY A  1 383 ? 22.934  59.647  35.450  1.00 22.27 ?  407  GLY A CA  1 
ATOM   3060  C  C   . GLY A  1 383 ? 23.843  60.095  36.585  1.00 22.35 ?  407  GLY A C   1 
ATOM   3061  O  O   . GLY A  1 383 ? 23.823  59.504  37.671  1.00 22.11 ?  407  GLY A O   1 
ATOM   3062  N  N   . LEU A  1 384 ? 24.636  61.138  36.332  1.00 22.38 ?  408  LEU A N   1 
ATOM   3063  C  CA  . LEU A  1 384 ? 25.551  61.687  37.336  1.00 22.77 ?  408  LEU A CA  1 
ATOM   3064  C  C   . LEU A  1 384 ? 24.790  62.160  38.573  1.00 22.90 ?  408  LEU A C   1 
ATOM   3065  O  O   . LEU A  1 384 ? 25.219  61.914  39.709  1.00 23.21 ?  408  LEU A O   1 
ATOM   3066  C  CB  . LEU A  1 384 ? 26.407  62.821  36.746  1.00 22.83 ?  408  LEU A CB  1 
ATOM   3067  C  CG  . LEU A  1 384 ? 27.385  63.577  37.662  1.00 23.05 ?  408  LEU A CG  1 
ATOM   3068  C  CD1 . LEU A  1 384 ? 28.393  62.649  38.339  1.00 23.59 ?  408  LEU A CD1 1 
ATOM   3069  C  CD2 . LEU A  1 384 ? 28.110  64.674  36.895  1.00 22.99 ?  408  LEU A CD2 1 
ATOM   3070  N  N   . ALA A  1 385 ? 23.653  62.812  38.341  1.00 22.94 ?  409  ALA A N   1 
ATOM   3071  C  CA  . ALA A  1 385 ? 22.766  63.263  39.409  1.00 23.24 ?  409  ALA A CA  1 
ATOM   3072  C  C   . ALA A  1 385 ? 22.311  62.103  40.289  1.00 23.43 ?  409  ALA A C   1 
ATOM   3073  O  O   . ALA A  1 385 ? 22.359  62.197  41.520  1.00 23.43 ?  409  ALA A O   1 
ATOM   3074  C  CB  . ALA A  1 385 ? 21.563  63.991  38.826  1.00 23.00 ?  409  ALA A CB  1 
ATOM   3075  N  N   . LYS A  1 386 ? 21.878  61.014  39.651  1.00 23.41 ?  410  LYS A N   1 
ATOM   3076  C  CA  . LYS A  1 386 ? 21.416  59.830  40.370  1.00 23.51 ?  410  LYS A CA  1 
ATOM   3077  C  C   . LYS A  1 386 ? 22.512  59.295  41.290  1.00 23.64 ?  410  LYS A C   1 
ATOM   3078  O  O   . LYS A  1 386 ? 22.259  59.043  42.470  1.00 23.42 ?  410  LYS A O   1 
ATOM   3079  C  CB  . LYS A  1 386 ? 20.930  58.748  39.395  1.00 23.45 ?  410  LYS A CB  1 
ATOM   3080  C  CG  . LYS A  1 386 ? 20.133  57.609  40.035  1.00 23.01 ?  410  LYS A CG  1 
ATOM   3081  C  CD  . LYS A  1 386 ? 18.777  58.068  40.568  1.00 22.82 ?  410  LYS A CD  1 
ATOM   3082  C  CE  . LYS A  1 386 ? 17.937  56.883  41.022  1.00 23.20 ?  410  LYS A CE  1 
ATOM   3083  N  NZ  . LYS A  1 386 ? 16.707  57.297  41.770  1.00 24.24 ?  410  LYS A NZ  1 
ATOM   3084  N  N   . TYR A  1 387 ? 23.724  59.144  40.750  1.00 23.88 ?  411  TYR A N   1 
ATOM   3085  C  CA  . TYR A  1 387 ? 24.873  58.704  41.543  1.00 24.30 ?  411  TYR A CA  1 
ATOM   3086  C  C   . TYR A  1 387 ? 25.171  59.649  42.712  1.00 24.56 ?  411  TYR A C   1 
ATOM   3087  O  O   . TYR A  1 387 ? 25.381  59.192  43.837  1.00 24.58 ?  411  TYR A O   1 
ATOM   3088  C  CB  . TYR A  1 387 ? 26.128  58.512  40.676  1.00 24.07 ?  411  TYR A CB  1 
ATOM   3089  C  CG  . TYR A  1 387 ? 27.422  58.672  41.455  1.00 24.56 ?  411  TYR A CG  1 
ATOM   3090  C  CD1 . TYR A  1 387 ? 27.827  57.709  42.393  1.00 24.85 ?  411  TYR A CD1 1 
ATOM   3091  C  CD2 . TYR A  1 387 ? 28.227  59.796  41.280  1.00 24.42 ?  411  TYR A CD2 1 
ATOM   3092  C  CE1 . TYR A  1 387 ? 29.002  57.862  43.125  1.00 25.05 ?  411  TYR A CE1 1 
ATOM   3093  C  CE2 . TYR A  1 387 ? 29.409  59.958  42.011  1.00 25.39 ?  411  TYR A CE2 1 
ATOM   3094  C  CZ  . TYR A  1 387 ? 29.791  58.986  42.926  1.00 25.44 ?  411  TYR A CZ  1 
ATOM   3095  O  OH  . TYR A  1 387 ? 30.959  59.140  43.642  1.00 26.63 ?  411  TYR A OH  1 
ATOM   3096  N  N   . GLN A  1 388 ? 25.186  60.954  42.436  1.00 25.08 ?  412  GLN A N   1 
ATOM   3097  C  CA  . GLN A  1 388 ? 25.524  61.971  43.440  1.00 25.66 ?  412  GLN A CA  1 
ATOM   3098  C  C   . GLN A  1 388 ? 24.598  61.964  44.654  1.00 26.03 ?  412  GLN A C   1 
ATOM   3099  O  O   . GLN A  1 388 ? 25.051  62.175  45.785  1.00 26.20 ?  412  GLN A O   1 
ATOM   3100  C  CB  . GLN A  1 388 ? 25.567  63.366  42.816  1.00 25.70 ?  412  GLN A CB  1 
ATOM   3101  C  CG  . GLN A  1 388 ? 26.866  63.676  42.088  1.00 26.07 ?  412  GLN A CG  1 
ATOM   3102  C  CD  . GLN A  1 388 ? 26.842  65.019  41.380  1.00 26.85 ?  412  GLN A CD  1 
ATOM   3103  O  OE1 . GLN A  1 388 ? 25.783  65.633  41.212  1.00 27.13 ?  412  GLN A OE1 1 
ATOM   3104  N  NE2 . GLN A  1 388 ? 28.013  65.479  40.951  1.00 26.25 ?  412  GLN A NE2 1 
ATOM   3105  N  N   . GLU A  1 389 ? 23.313  61.704  44.425  1.00 26.47 ?  413  GLU A N   1 
ATOM   3106  C  CA  . GLU A  1 389 ? 22.358  61.591  45.527  1.00 27.05 ?  413  GLU A CA  1 
ATOM   3107  C  C   . GLU A  1 389 ? 22.654  60.358  46.378  1.00 27.28 ?  413  GLU A C   1 
ATOM   3108  O  O   . GLU A  1 389 ? 22.564  60.408  47.609  1.00 27.47 ?  413  GLU A O   1 
ATOM   3109  C  CB  . GLU A  1 389 ? 20.915  61.554  45.016  1.00 27.02 ?  413  GLU A CB  1 
ATOM   3110  C  CG  . GLU A  1 389 ? 19.885  61.768  46.124  1.00 27.53 ?  413  GLU A CG  1 
ATOM   3111  C  CD  . GLU A  1 389 ? 18.472  61.408  45.712  1.00 27.63 ?  413  GLU A CD  1 
ATOM   3112  O  OE1 . GLU A  1 389 ? 18.108  61.632  44.538  1.00 27.71 ?  413  GLU A OE1 1 
ATOM   3113  O  OE2 . GLU A  1 389 ? 17.719  60.908  46.574  1.00 27.53 -1 413  GLU A OE2 1 
ATOM   3114  N  N   . ALA A  1 390 ? 23.014  59.259  45.717  1.00 27.46 ?  414  ALA A N   1 
ATOM   3115  C  CA  . ALA A  1 390 ? 23.390  58.026  46.408  1.00 27.70 ?  414  ALA A CA  1 
ATOM   3116  C  C   . ALA A  1 390 ? 24.695  58.188  47.193  1.00 27.80 ?  414  ALA A C   1 
ATOM   3117  O  O   . ALA A  1 390 ? 24.799  57.727  48.332  1.00 27.91 ?  414  ALA A O   1 
ATOM   3118  C  CB  . ALA A  1 390 ? 23.490  56.870  45.425  1.00 27.45 ?  414  ALA A CB  1 
ATOM   3119  N  N   . ASN A  1 391 ? 25.677  58.855  46.588  1.00 28.03 ?  415  ASN A N   1 
ATOM   3120  C  CA  . ASN A  1 391 ? 26.975  59.073  47.233  1.00 28.31 ?  415  ASN A CA  1 
ATOM   3121  C  C   . ASN A  1 391 ? 26.873  59.902  48.515  1.00 28.38 ?  415  ASN A C   1 
ATOM   3122  O  O   . ASN A  1 391 ? 27.565  59.625  49.494  1.00 28.27 ?  415  ASN A O   1 
ATOM   3123  C  CB  . ASN A  1 391 ? 27.978  59.703  46.260  1.00 28.36 ?  415  ASN A CB  1 
ATOM   3124  C  CG  . ASN A  1 391 ? 29.387  59.775  46.838  1.00 28.61 ?  415  ASN A CG  1 
ATOM   3125  O  OD1 . ASN A  1 391 ? 29.989  58.752  47.173  1.00 29.12 ?  415  ASN A OD1 1 
ATOM   3126  N  ND2 . ASN A  1 391 ? 29.912  60.986  46.963  1.00 28.79 ?  415  ASN A ND2 1 
ATOM   3127  N  N   . ALA A  1 392 ? 25.994  60.902  48.505  1.00 28.72 ?  416  ALA A N   1 
ATOM   3128  C  CA  . ALA A  1 392 ? 25.754  61.747  49.675  1.00 29.04 ?  416  ALA A CA  1 
ATOM   3129  C  C   . ALA A  1 392 ? 25.388  60.922  50.912  1.00 29.36 ?  416  ALA A C   1 
ATOM   3130  O  O   . ALA A  1 392 ? 25.797  61.253  52.026  1.00 29.39 ?  416  ALA A O   1 
ATOM   3131  C  CB  . ALA A  1 392 ? 24.674  62.779  49.375  1.00 28.96 ?  416  ALA A CB  1 
ATOM   3132  N  N   . ILE A  1 393 ? 24.633  59.845  50.699  1.00 29.47 ?  417  ILE A N   1 
ATOM   3133  C  CA  . ILE A  1 393 ? 24.209  58.943  51.771  1.00 29.85 ?  417  ILE A CA  1 
ATOM   3134  C  C   . ILE A  1 393 ? 25.385  58.150  52.359  1.00 30.19 ?  417  ILE A C   1 
ATOM   3135  O  O   . ILE A  1 393 ? 25.614  58.187  53.572  1.00 29.95 ?  417  ILE A O   1 
ATOM   3136  C  CB  . ILE A  1 393 ? 23.088  57.979  51.285  1.00 29.82 ?  417  ILE A CB  1 
ATOM   3137  C  CG1 . ILE A  1 393 ? 21.787  58.753  51.038  1.00 29.89 ?  417  ILE A CG1 1 
ATOM   3138  C  CG2 . ILE A  1 393 ? 22.865  56.839  52.282  1.00 29.74 ?  417  ILE A CG2 1 
ATOM   3139  C  CD1 . ILE A  1 393 ? 20.802  58.042  50.144  1.00 30.36 ?  417  ILE A CD1 1 
ATOM   3140  N  N   . VAL A  1 394 ? 26.125  57.450  51.496  1.00 30.57 ?  418  VAL A N   1 
ATOM   3141  C  CA  . VAL A  1 394 ? 27.236  56.599  51.928  1.00 31.00 ?  418  VAL A CA  1 
ATOM   3142  C  C   . VAL A  1 394 ? 28.408  57.430  52.464  1.00 31.55 ?  418  VAL A C   1 
ATOM   3143  O  O   . VAL A  1 394 ? 29.080  57.019  53.416  1.00 31.68 ?  418  VAL A O   1 
ATOM   3144  C  CB  . VAL A  1 394 ? 27.726  55.648  50.801  1.00 30.89 ?  418  VAL A CB  1 
ATOM   3145  C  CG1 . VAL A  1 394 ? 28.665  54.578  51.364  1.00 30.56 ?  418  VAL A CG1 1 
ATOM   3146  C  CG2 . VAL A  1 394 ? 26.550  54.978  50.106  1.00 30.67 ?  418  VAL A CG2 1 
ATOM   3147  N  N   . HIS A  1 395 ? 28.647  58.591  51.851  1.00 31.99 ?  419  HIS A N   1 
ATOM   3148  C  CA  . HIS A  1 395 ? 29.706  59.496  52.293  1.00 32.62 ?  419  HIS A CA  1 
ATOM   3149  C  C   . HIS A  1 395 ? 29.412  60.053  53.690  1.00 32.88 ?  419  HIS A C   1 
ATOM   3150  O  O   . HIS A  1 395 ? 30.325  60.192  54.507  1.00 32.82 ?  419  HIS A O   1 
ATOM   3151  C  CB  . HIS A  1 395 ? 29.917  60.633  51.288  1.00 32.86 ?  419  HIS A CB  1 
ATOM   3152  C  CG  . HIS A  1 395 ? 31.027  61.567  51.657  1.00 33.91 ?  419  HIS A CG  1 
ATOM   3153  N  ND1 . HIS A  1 395 ? 32.356  61.254  51.471  1.00 35.16 ?  419  HIS A ND1 1 
ATOM   3154  C  CD2 . HIS A  1 395 ? 31.006  62.805  52.204  1.00 34.87 ?  419  HIS A CD2 1 
ATOM   3155  C  CE1 . HIS A  1 395 ? 33.106  62.260  51.886  1.00 35.36 ?  419  HIS A CE1 1 
ATOM   3156  N  NE2 . HIS A  1 395 ? 32.311  63.214  52.335  1.00 35.05 ?  419  HIS A NE2 1 
ATOM   3157  N  N   . LYS A  1 396 ? 28.140  60.359  53.957  1.00 33.13 ?  420  LYS A N   1 
ATOM   3158  C  CA  . LYS A  1 396 ? 27.714  60.791  55.289  1.00 33.58 ?  420  LYS A CA  1 
ATOM   3159  C  C   . LYS A  1 396 ? 28.013  59.717  56.338  1.00 33.54 ?  420  LYS A C   1 
ATOM   3160  O  O   . LYS A  1 396 ? 28.525  60.025  57.416  1.00 33.63 ?  420  LYS A O   1 
ATOM   3161  C  CB  . LYS A  1 396 ? 26.228  61.186  55.301  1.00 33.67 ?  420  LYS A CB  1 
ATOM   3162  C  CG  . LYS A  1 396 ? 25.699  61.700  56.653  1.00 34.93 ?  420  LYS A CG  1 
ATOM   3163  C  CD  . LYS A  1 396 ? 26.482  62.913  57.158  1.00 36.69 ?  420  LYS A CD  1 
ATOM   3164  C  CE  . LYS A  1 396 ? 26.015  63.349  58.544  1.00 37.93 ?  420  LYS A CE  1 
ATOM   3165  N  NZ  . LYS A  1 396 ? 27.045  64.188  59.228  1.00 38.25 ?  420  LYS A NZ  1 
ATOM   3166  N  N   . MET A  1 397 ? 27.708  58.463  56.008  1.00 33.58 ?  421  MET A N   1 
ATOM   3167  C  CA  . MET A  1 397 ? 28.005  57.332  56.890  1.00 33.66 ?  421  MET A CA  1 
ATOM   3168  C  C   . MET A  1 397 ? 29.504  57.212  57.189  1.00 33.80 ?  421  MET A C   1 
ATOM   3169  O  O   . MET A  1 397 ? 29.894  56.946  58.332  1.00 33.77 ?  421  MET A O   1 
ATOM   3170  C  CB  . MET A  1 397 ? 27.471  56.025  56.300  1.00 33.65 ?  421  MET A CB  1 
ATOM   3171  C  CG  . MET A  1 397 ? 25.956  55.975  56.174  1.00 33.48 ?  421  MET A CG  1 
ATOM   3172  S  SD  . MET A  1 397 ? 25.337  54.329  55.783  1.00 33.96 ?  421  MET A SD  1 
ATOM   3173  C  CE  . MET A  1 397 ? 25.595  53.476  57.338  1.00 33.27 ?  421  MET A CE  1 
ATOM   3174  N  N   . TYR A  1 398 ? 30.332  57.416  56.165  1.00 33.85 ?  422  TYR A N   1 
ATOM   3175  C  CA  . TYR A  1 398 ? 31.787  57.436  56.336  1.00 34.23 ?  422  TYR A CA  1 
ATOM   3176  C  C   . TYR A  1 398 ? 32.229  58.539  57.301  1.00 34.51 ?  422  TYR A C   1 
ATOM   3177  O  O   . TYR A  1 398 ? 32.999  58.283  58.227  1.00 34.51 ?  422  TYR A O   1 
ATOM   3178  C  CB  . TYR A  1 398 ? 32.503  57.584  54.988  1.00 34.07 ?  422  TYR A CB  1 
ATOM   3179  C  CG  . TYR A  1 398 ? 34.014  57.607  55.096  1.00 33.83 ?  422  TYR A CG  1 
ATOM   3180  C  CD1 . TYR A  1 398 ? 34.732  56.439  55.360  1.00 33.79 ?  422  TYR A CD1 1 
ATOM   3181  C  CD2 . TYR A  1 398 ? 34.727  58.796  54.930  1.00 33.66 ?  422  TYR A CD2 1 
ATOM   3182  C  CE1 . TYR A  1 398 ? 36.126  56.456  55.466  1.00 33.75 ?  422  TYR A CE1 1 
ATOM   3183  C  CE2 . TYR A  1 398 ? 36.119  58.824  55.029  1.00 33.55 ?  422  TYR A CE2 1 
ATOM   3184  C  CZ  . TYR A  1 398 ? 36.810  57.650  55.295  1.00 33.66 ?  422  TYR A CZ  1 
ATOM   3185  O  OH  . TYR A  1 398 ? 38.182  57.668  55.393  1.00 33.92 ?  422  TYR A OH  1 
ATOM   3186  N  N   . GLU A  1 399 ? 31.735  59.756  57.076  1.00 34.92 ?  423  GLU A N   1 
ATOM   3187  C  CA  . GLU A  1 399 ? 32.014  60.889  57.963  1.00 35.29 ?  423  GLU A CA  1 
ATOM   3188  C  C   . GLU A  1 399 ? 31.584  60.604  59.400  1.00 35.02 ?  423  GLU A C   1 
ATOM   3189  O  O   . GLU A  1 399 ? 32.277  60.985  60.344  1.00 35.04 ?  423  GLU A O   1 
ATOM   3190  C  CB  . GLU A  1 399 ? 31.315  62.153  57.464  1.00 35.59 ?  423  GLU A CB  1 
ATOM   3191  C  CG  . GLU A  1 399 ? 31.954  62.790  56.244  1.00 37.23 ?  423  GLU A CG  1 
ATOM   3192  C  CD  . GLU A  1 399 ? 31.332  64.134  55.911  1.00 39.57 ?  423  GLU A CD  1 
ATOM   3193  O  OE1 . GLU A  1 399 ? 32.007  65.165  56.125  1.00 40.82 ?  423  GLU A OE1 1 
ATOM   3194  O  OE2 . GLU A  1 399 ? 30.165  64.161  55.456  1.00 40.76 -1 423  GLU A OE2 1 
ATOM   3195  N  N   . ASP A  1 400 ? 30.443  59.931  59.549  1.00 34.69 ?  424  ASP A N   1 
ATOM   3196  C  CA  . ASP A  1 400 ? 29.898  59.576  60.860  1.00 34.46 ?  424  ASP A CA  1 
ATOM   3197  C  C   . ASP A  1 400 ? 30.620  58.390  61.492  1.00 34.02 ?  424  ASP A C   1 
ATOM   3198  O  O   . ASP A  1 400 ? 30.498  58.157  62.694  1.00 34.08 ?  424  ASP A O   1 
ATOM   3199  C  CB  . ASP A  1 400 ? 28.397  59.277  60.757  1.00 34.61 ?  424  ASP A CB  1 
ATOM   3200  C  CG  . ASP A  1 400 ? 27.567  60.518  60.462  1.00 35.11 ?  424  ASP A CG  1 
ATOM   3201  O  OD1 . ASP A  1 400 ? 28.114  61.642  60.509  1.00 35.91 ?  424  ASP A OD1 1 
ATOM   3202  O  OD2 . ASP A  1 400 ? 26.358  60.366  60.186  1.00 35.77 -1 424  ASP A OD2 1 
ATOM   3203  N  N   . GLY A  1 401 ? 31.364  57.646  60.675  1.00 33.63 ?  425  GLY A N   1 
ATOM   3204  C  CA  . GLY A  1 401 ? 32.074  56.448  61.125  1.00 32.84 ?  425  GLY A CA  1 
ATOM   3205  C  C   . GLY A  1 401 ? 31.163  55.250  61.336  1.00 32.28 ?  425  GLY A C   1 
ATOM   3206  O  O   . GLY A  1 401 ? 31.497  54.341  62.099  1.00 32.15 ?  425  GLY A O   1 
ATOM   3207  N  N   . THR A  1 402 ? 30.022  55.241  60.644  1.00 31.75 ?  426  THR A N   1 
ATOM   3208  C  CA  . THR A  1 402 ? 28.975  54.234  60.868  1.00 31.17 ?  426  THR A CA  1 
ATOM   3209  C  C   . THR A  1 402 ? 28.929  53.099  59.834  1.00 30.90 ?  426  THR A C   1 
ATOM   3210  O  O   . THR A  1 402 ? 28.050  52.230  59.900  1.00 30.81 ?  426  THR A O   1 
ATOM   3211  C  CB  . THR A  1 402 ? 27.573  54.885  60.978  1.00 31.19 ?  426  THR A CB  1 
ATOM   3212  O  OG1 . THR A  1 402 ? 27.292  55.627  59.785  1.00 31.09 ?  426  THR A OG1 1 
ATOM   3213  C  CG2 . THR A  1 402 ? 27.494  55.814  62.195  1.00 30.68 ?  426  THR A CG2 1 
ATOM   3214  N  N   . LEU A  1 403 ? 29.868  53.100  58.890  1.00 30.37 ?  427  LEU A N   1 
ATOM   3215  C  CA  . LEU A  1 403 ? 29.971  52.011  57.918  1.00 30.05 ?  427  LEU A CA  1 
ATOM   3216  C  C   . LEU A  1 403 ? 30.323  50.709  58.627  1.00 29.84 ?  427  LEU A C   1 
ATOM   3217  O  O   . LEU A  1 403 ? 31.031  50.715  59.636  1.00 29.74 ?  427  LEU A O   1 
ATOM   3218  C  CB  . LEU A  1 403 ? 31.020  52.317  56.842  1.00 29.94 ?  427  LEU A CB  1 
ATOM   3219  C  CG  . LEU A  1 403 ? 30.755  53.429  55.817  1.00 29.82 ?  427  LEU A CG  1 
ATOM   3220  C  CD1 . LEU A  1 403 ? 32.020  53.719  55.023  1.00 29.01 ?  427  LEU A CD1 1 
ATOM   3221  C  CD2 . LEU A  1 403 ? 29.598  53.086  54.879  1.00 29.26 ?  427  LEU A CD2 1 
ATOM   3222  N  N   . THR A  1 404 ? 29.819  49.599  58.098  1.00 29.71 ?  428  THR A N   1 
ATOM   3223  C  CA  . THR A  1 404 ? 30.087  48.282  58.670  1.00 29.57 ?  428  THR A CA  1 
ATOM   3224  C  C   . THR A  1 404 ? 31.594  48.033  58.774  1.00 29.58 ?  428  THR A C   1 
ATOM   3225  O  O   . THR A  1 404 ? 32.320  48.110  57.776  1.00 29.29 ?  428  THR A O   1 
ATOM   3226  C  CB  . THR A  1 404 ? 29.396  47.168  57.853  1.00 29.55 ?  428  THR A CB  1 
ATOM   3227  O  OG1 . THR A  1 404 ? 27.979  47.378  57.872  1.00 29.65 ?  428  THR A OG1 1 
ATOM   3228  C  CG2 . THR A  1 404 ? 29.702  45.791  58.430  1.00 29.48 ?  428  THR A CG2 1 
ATOM   3229  N  N   . GLY A  1 405 ? 32.050  47.776  59.999  1.00 29.53 ?  429  GLY A N   1 
ATOM   3230  C  CA  . GLY A  1 405 ? 33.446  47.444  60.275  1.00 29.49 ?  429  GLY A CA  1 
ATOM   3231  C  C   . GLY A  1 405 ? 34.443  48.588  60.214  1.00 29.60 ?  429  GLY A C   1 
ATOM   3232  O  O   . GLY A  1 405 ? 35.649  48.354  60.316  1.00 29.55 ?  429  GLY A O   1 
ATOM   3233  N  N   . GLN A  1 406 ? 33.949  49.820  60.069  1.00 29.71 ?  430  GLN A N   1 
ATOM   3234  C  CA  . GLN A  1 406 ? 34.809  50.998  59.880  1.00 29.96 ?  430  GLN A CA  1 
ATOM   3235  C  C   . GLN A  1 406 ? 35.817  51.221  61.011  1.00 30.31 ?  430  GLN A C   1 
ATOM   3236  O  O   . GLN A  1 406 ? 36.940  51.663  60.765  1.00 30.58 ?  430  GLN A O   1 
ATOM   3237  C  CB  . GLN A  1 406 ? 33.972  52.269  59.667  1.00 29.81 ?  430  GLN A CB  1 
ATOM   3238  C  CG  . GLN A  1 406 ? 34.782  53.466  59.150  1.00 29.52 ?  430  GLN A CG  1 
ATOM   3239  C  CD  . GLN A  1 406 ? 33.932  54.662  58.740  1.00 28.86 ?  430  GLN A CD  1 
ATOM   3240  O  OE1 . GLN A  1 406 ? 32.718  54.555  58.561  1.00 28.42 ?  430  GLN A OE1 1 
ATOM   3241  N  NE2 . GLN A  1 406 ? 34.576  55.811  58.587  1.00 28.14 ?  430  GLN A NE2 1 
ATOM   3242  N  N   . LYS A  1 407 ? 35.410  50.920  62.241  1.00 30.63 ?  431  LYS A N   1 
ATOM   3243  C  CA  . LYS A  1 407 ? 36.244  51.173  63.415  1.00 31.04 ?  431  LYS A CA  1 
ATOM   3244  C  C   . LYS A  1 407 ? 36.754  49.882  64.051  1.00 30.97 ?  431  LYS A C   1 
ATOM   3245  O  O   . LYS A  1 407 ? 37.503  49.923  65.030  1.00 31.30 ?  431  LYS A O   1 
ATOM   3246  C  CB  . LYS A  1 407 ? 35.468  51.994  64.459  1.00 31.29 ?  431  LYS A CB  1 
ATOM   3247  C  CG  . LYS A  1 407 ? 34.800  53.273  63.934  1.00 31.77 ?  431  LYS A CG  1 
ATOM   3248  C  CD  . LYS A  1 407 ? 35.702  54.505  64.031  1.00 33.11 ?  431  LYS A CD  1 
ATOM   3249  C  CE  . LYS A  1 407 ? 36.454  54.779  62.734  1.00 33.36 ?  431  LYS A CE  1 
ATOM   3250  N  NZ  . LYS A  1 407 ? 36.859  56.209  62.619  1.00 33.34 ?  431  LYS A NZ  1 
ATOM   3251  N  N   . THR A  1 408 ? 36.355  48.741  63.490  1.00 30.75 ?  432  THR A N   1 
ATOM   3252  C  CA  . THR A  1 408 ? 36.639  47.437  64.098  1.00 30.58 ?  432  THR A CA  1 
ATOM   3253  C  C   . THR A  1 408 ? 37.398  46.466  63.189  1.00 30.42 ?  432  THR A C   1 
ATOM   3254  O  O   . THR A  1 408 ? 38.063  45.545  63.678  1.00 30.53 ?  432  THR A O   1 
ATOM   3255  C  CB  . THR A  1 408 ? 35.342  46.739  64.573  1.00 30.55 ?  432  THR A CB  1 
ATOM   3256  O  OG1 . THR A  1 408 ? 34.458  46.554  63.458  1.00 30.96 ?  432  THR A OG1 1 
ATOM   3257  C  CG2 . THR A  1 408 ? 34.637  47.564  65.651  1.00 30.78 ?  432  THR A CG2 1 
ATOM   3258  N  N   . ASN A  1 409 ? 37.286  46.659  61.875  1.00 29.96 ?  433  ASN A N   1 
ATOM   3259  C  CA  . ASN A  1 409 ? 37.868  45.731  60.904  1.00 29.53 ?  433  ASN A CA  1 
ATOM   3260  C  C   . ASN A  1 409 ? 38.107  46.386  59.539  1.00 29.29 ?  433  ASN A C   1 
ATOM   3261  O  O   . ASN A  1 409 ? 37.653  45.887  58.508  1.00 29.33 ?  433  ASN A O   1 
ATOM   3262  C  CB  . ASN A  1 409 ? 36.983  44.479  60.770  1.00 29.50 ?  433  ASN A CB  1 
ATOM   3263  C  CG  . ASN A  1 409 ? 37.711  43.302  60.135  1.00 29.17 ?  433  ASN A CG  1 
ATOM   3264  O  OD1 . ASN A  1 409 ? 38.940  43.264  60.083  1.00 29.14 ?  433  ASN A OD1 1 
ATOM   3265  N  ND2 . ASN A  1 409 ? 36.948  42.329  59.655  1.00 28.31 ?  433  ASN A ND2 1 
ATOM   3266  N  N   . ARG A  1 410 ? 38.828  47.505  59.546  1.00 28.85 ?  434  ARG A N   1 
ATOM   3267  C  CA  . ARG A  1 410 ? 39.115  48.255  58.324  1.00 28.47 ?  434  ARG A CA  1 
ATOM   3268  C  C   . ARG A  1 410 ? 40.627  48.445  58.151  1.00 28.31 ?  434  ARG A C   1 
ATOM   3269  O  O   . ARG A  1 410 ? 41.148  49.543  58.372  1.00 28.36 ?  434  ARG A O   1 
ATOM   3270  C  CB  . ARG A  1 410 ? 38.387  49.603  58.348  1.00 28.37 ?  434  ARG A CB  1 
ATOM   3271  C  CG  . ARG A  1 410 ? 38.321  50.318  57.007  1.00 27.97 ?  434  ARG A CG  1 
ATOM   3272  C  CD  . ARG A  1 410 ? 37.660  51.680  57.156  1.00 27.01 ?  434  ARG A CD  1 
ATOM   3273  N  NE  . ARG A  1 410 ? 37.738  52.468  55.925  1.00 25.91 ?  434  ARG A NE  1 
ATOM   3274  C  CZ  . ARG A  1 410 ? 36.868  52.391  54.919  1.00 25.18 ?  434  ARG A CZ  1 
ATOM   3275  N  NH1 . ARG A  1 410 ? 35.834  51.558  54.980  1.00 23.58 ?  434  ARG A NH1 1 
ATOM   3276  N  NH2 . ARG A  1 410 ? 37.036  53.153  53.845  1.00 24.26 ?  434  ARG A NH2 1 
ATOM   3277  N  N   . PRO A  1 411 ? 41.340  47.368  57.760  1.00 28.16 ?  435  PRO A N   1 
ATOM   3278  C  CA  . PRO A  1 411 ? 42.799  47.437  57.662  1.00 28.09 ?  435  PRO A CA  1 
ATOM   3279  C  C   . PRO A  1 411 ? 43.259  48.354  56.533  1.00 27.82 ?  435  PRO A C   1 
ATOM   3280  O  O   . PRO A  1 411 ? 42.537  48.541  55.551  1.00 27.74 ?  435  PRO A O   1 
ATOM   3281  C  CB  . PRO A  1 411 ? 43.204  45.988  57.374  1.00 28.10 ?  435  PRO A CB  1 
ATOM   3282  C  CG  . PRO A  1 411 ? 42.007  45.377  56.742  1.00 28.18 ?  435  PRO A CG  1 
ATOM   3283  C  CD  . PRO A  1 411 ? 40.820  46.049  57.352  1.00 28.13 ?  435  PRO A CD  1 
ATOM   3284  N  N   . ASN A  1 412 ? 44.450  48.923  56.690  1.00 27.58 ?  436  ASN A N   1 
ATOM   3285  C  CA  . ASN A  1 412 ? 45.015  49.834  55.701  1.00 27.50 ?  436  ASN A CA  1 
ATOM   3286  C  C   . ASN A  1 412 ? 45.407  49.116  54.409  1.00 27.22 ?  436  ASN A C   1 
ATOM   3287  O  O   . ASN A  1 412 ? 45.890  47.984  54.456  1.00 26.93 ?  436  ASN A O   1 
ATOM   3288  C  CB  . ASN A  1 412 ? 46.228  50.563  56.283  1.00 27.66 ?  436  ASN A CB  1 
ATOM   3289  C  CG  . ASN A  1 412 ? 45.850  51.553  57.377  1.00 28.54 ?  436  ASN A CG  1 
ATOM   3290  O  OD1 . ASN A  1 412 ? 44.953  52.380  57.201  1.00 29.53 ?  436  ASN A OD1 1 
ATOM   3291  N  ND2 . ASN A  1 412 ? 46.544  51.476  58.511  1.00 28.14 ?  436  ASN A ND2 1 
ATOM   3292  N  N   . PRO A  1 413 ? 45.196  49.777  53.251  1.00 27.11 ?  437  PRO A N   1 
ATOM   3293  C  CA  . PRO A  1 413 ? 45.597  49.242  51.946  1.00 26.98 ?  437  PRO A CA  1 
ATOM   3294  C  C   . PRO A  1 413 ? 47.120  49.132  51.813  1.00 26.95 ?  437  PRO A C   1 
ATOM   3295  O  O   . PRO A  1 413 ? 47.841  49.828  52.528  1.00 26.74 ?  437  PRO A O   1 
ATOM   3296  C  CB  . PRO A  1 413 ? 45.040  50.274  50.959  1.00 27.08 ?  437  PRO A CB  1 
ATOM   3297  C  CG  . PRO A  1 413 ? 44.895  51.528  51.760  1.00 26.87 ?  437  PRO A CG  1 
ATOM   3298  C  CD  . PRO A  1 413 ? 44.496  51.070  53.118  1.00 26.88 ?  437  PRO A CD  1 
ATOM   3299  N  N   . PRO A  1 414 ? 47.610  48.257  50.909  1.00 26.97 ?  438  PRO A N   1 
ATOM   3300  C  CA  . PRO A  1 414 ? 49.058  48.043  50.796  1.00 26.86 ?  438  PRO A CA  1 
ATOM   3301  C  C   . PRO A  1 414 ? 49.799  49.301  50.352  1.00 26.83 ?  438  PRO A C   1 
ATOM   3302  O  O   . PRO A  1 414 ? 49.283  50.065  49.536  1.00 26.49 ?  438  PRO A O   1 
ATOM   3303  C  CB  . PRO A  1 414 ? 49.172  46.954  49.725  1.00 26.82 ?  438  PRO A CB  1 
ATOM   3304  C  CG  . PRO A  1 414 ? 47.910  47.065  48.933  1.00 26.80 ?  438  PRO A CG  1 
ATOM   3305  C  CD  . PRO A  1 414 ? 46.861  47.460  49.919  1.00 26.78 ?  438  PRO A CD  1 
ATOM   3306  N  N   . GLU A  1 415 ? 50.997  49.498  50.900  1.00 27.00 ?  439  GLU A N   1 
ATOM   3307  C  CA  . GLU A  1 415 ? 51.856  50.637  50.557  1.00 27.34 ?  439  GLU A CA  1 
ATOM   3308  C  C   . GLU A  1 415 ? 52.106  50.743  49.046  1.00 27.29 ?  439  GLU A C   1 
ATOM   3309  O  O   . GLU A  1 415 ? 52.290  49.719  48.379  1.00 27.06 ?  439  GLU A O   1 
ATOM   3310  C  CB  . GLU A  1 415 ? 53.186  50.554  51.324  1.00 27.28 ?  439  GLU A CB  1 
ATOM   3311  C  CG  . GLU A  1 415 ? 54.010  49.295  51.046  1.00 27.94 ?  439  GLU A CG  1 
ATOM   3312  C  CD  . GLU A  1 415 ? 55.331  49.258  51.804  1.00 28.61 ?  439  GLU A CD  1 
ATOM   3313  O  OE1 . GLU A  1 415 ? 55.689  50.256  52.466  1.00 29.44 ?  439  GLU A OE1 1 
ATOM   3314  O  OE2 . GLU A  1 415 ? 56.019  48.222  51.730  1.00 29.36 -1 439  GLU A OE2 1 
ATOM   3315  N  N   . PRO A  1 416 ? 52.145  51.980  48.508  1.00 27.58 ?  440  PRO A N   1 
ATOM   3316  C  CA  . PRO A  1 416 ? 52.103  53.249  49.241  1.00 27.93 ?  440  PRO A CA  1 
ATOM   3317  C  C   . PRO A  1 416 ? 50.724  53.921  49.294  1.00 28.18 ?  440  PRO A C   1 
ATOM   3318  O  O   . PRO A  1 416 ? 50.647  55.146  49.427  1.00 28.03 ?  440  PRO A O   1 
ATOM   3319  C  CB  . PRO A  1 416 ? 53.067  54.119  48.436  1.00 27.90 ?  440  PRO A CB  1 
ATOM   3320  C  CG  . PRO A  1 416 ? 52.858  53.659  47.019  1.00 27.62 ?  440  PRO A CG  1 
ATOM   3321  C  CD  . PRO A  1 416 ? 52.395  52.210  47.072  1.00 27.41 ?  440  PRO A CD  1 
ATOM   3322  N  N   . GLU A  1 417 ? 49.653  53.138  49.187  1.00 28.59 ?  441  GLU A N   1 
ATOM   3323  C  CA  . GLU A  1 417 ? 48.303  53.697  49.249  1.00 29.12 ?  441  GLU A CA  1 
ATOM   3324  C  C   . GLU A  1 417 ? 47.974  54.250  50.637  1.00 29.55 ?  441  GLU A C   1 
ATOM   3325  O  O   . GLU A  1 417 ? 48.439  53.730  51.656  1.00 29.48 ?  441  GLU A O   1 
ATOM   3326  C  CB  . GLU A  1 417 ? 47.251  52.665  48.814  1.00 29.00 ?  441  GLU A CB  1 
ATOM   3327  C  CG  . GLU A  1 417 ? 45.810  53.201  48.685  1.00 28.99 ?  441  GLU A CG  1 
ATOM   3328  C  CD  . GLU A  1 417 ? 45.652  54.301  47.640  1.00 28.95 ?  441  GLU A CD  1 
ATOM   3329  O  OE1 . GLU A  1 417 ? 46.057  55.453  47.901  1.00 28.65 ?  441  GLU A OE1 1 
ATOM   3330  O  OE2 . GLU A  1 417 ? 45.103  54.018  46.556  1.00 29.54 -1 441  GLU A OE2 1 
ATOM   3331  N  N   . LYS A  1 418 ? 47.184  55.319  50.650  1.00 30.10 ?  442  LYS A N   1 
ATOM   3332  C  CA  . LYS A  1 418 ? 46.617  55.872  51.872  1.00 30.76 ?  442  LYS A CA  1 
ATOM   3333  C  C   . LYS A  1 418 ? 45.151  55.459  52.004  1.00 30.66 ?  442  LYS A C   1 
ATOM   3334  O  O   . LYS A  1 418 ? 44.427  55.429  51.009  1.00 30.71 ?  442  LYS A O   1 
ATOM   3335  C  CB  . LYS A  1 418 ? 46.736  57.399  51.877  1.00 30.97 ?  442  LYS A CB  1 
ATOM   3336  C  CG  . LYS A  1 418 ? 48.132  57.912  52.214  1.00 32.88 ?  442  LYS A CG  1 
ATOM   3337  C  CD  . LYS A  1 418 ? 48.050  59.234  52.974  1.00 35.80 ?  442  LYS A CD  1 
ATOM   3338  C  CE  . LYS A  1 418 ? 49.338  59.523  53.729  1.00 37.14 ?  442  LYS A CE  1 
ATOM   3339  N  NZ  . LYS A  1 418 ? 49.194  60.695  54.645  1.00 38.41 ?  442  LYS A NZ  1 
ATOM   3340  N  N   . PRO A  1 419 ? 44.707  55.141  53.235  1.00 30.76 ?  443  PRO A N   1 
ATOM   3341  C  CA  . PRO A  1 419 ? 43.297  54.818  53.473  1.00 30.68 ?  443  PRO A CA  1 
ATOM   3342  C  C   . PRO A  1 419 ? 42.367  55.978  53.105  1.00 30.54 ?  443  PRO A C   1 
ATOM   3343  O  O   . PRO A  1 419 ? 42.760  57.141  53.182  1.00 30.46 ?  443  PRO A O   1 
ATOM   3344  C  CB  . PRO A  1 419 ? 43.246  54.544  54.982  1.00 30.76 ?  443  PRO A CB  1 
ATOM   3345  C  CG  . PRO A  1 419 ? 44.475  55.205  55.541  1.00 30.79 ?  443  PRO A CG  1 
ATOM   3346  C  CD  . PRO A  1 419 ? 45.504  55.059  54.474  1.00 30.79 ?  443  PRO A CD  1 
ATOM   3347  N  N   . GLY A  1 420 ? 41.146  55.647  52.698  1.00 30.44 ?  444  GLY A N   1 
ATOM   3348  C  CA  . GLY A  1 420 ? 40.172  56.643  52.265  1.00 30.17 ?  444  GLY A CA  1 
ATOM   3349  C  C   . GLY A  1 420 ? 38.818  56.028  51.959  1.00 29.84 ?  444  GLY A C   1 
ATOM   3350  O  O   . GLY A  1 420 ? 38.618  54.823  52.145  1.00 29.75 ?  444  GLY A O   1 
ATOM   3351  N  N   . PHE A  1 421 ? 37.892  56.863  51.487  1.00 29.38 ?  445  PHE A N   1 
ATOM   3352  C  CA  . PHE A  1 421 ? 36.534  56.427  51.162  1.00 29.02 ?  445  PHE A CA  1 
ATOM   3353  C  C   . PHE A  1 421 ? 36.334  56.312  49.660  1.00 28.66 ?  445  PHE A C   1 
ATOM   3354  O  O   . PHE A  1 421 ? 36.582  57.265  48.922  1.00 28.82 ?  445  PHE A O   1 
ATOM   3355  C  CB  . PHE A  1 421 ? 35.500  57.391  51.756  1.00 28.98 ?  445  PHE A CB  1 
ATOM   3356  C  CG  . PHE A  1 421 ? 34.095  57.184  51.240  1.00 29.41 ?  445  PHE A CG  1 
ATOM   3357  C  CD1 . PHE A  1 421 ? 33.333  56.095  51.661  1.00 29.41 ?  445  PHE A CD1 1 
ATOM   3358  C  CD2 . PHE A  1 421 ? 33.531  58.087  50.338  1.00 29.81 ?  445  PHE A CD2 1 
ATOM   3359  C  CE1 . PHE A  1 421 ? 32.034  55.904  51.186  1.00 30.08 ?  445  PHE A CE1 1 
ATOM   3360  C  CE2 . PHE A  1 421 ? 32.230  57.904  49.858  1.00 30.28 ?  445  PHE A CE2 1 
ATOM   3361  C  CZ  . PHE A  1 421 ? 31.480  56.812  50.283  1.00 29.31 ?  445  PHE A CZ  1 
ATOM   3362  N  N   . GLY A  1 422 ? 35.875  55.145  49.216  1.00 28.35 ?  446  GLY A N   1 
ATOM   3363  C  CA  . GLY A  1 422 ? 35.523  54.932  47.813  1.00 27.73 ?  446  GLY A CA  1 
ATOM   3364  C  C   . GLY A  1 422 ? 36.669  55.286  46.887  1.00 27.33 ?  446  GLY A C   1 
ATOM   3365  O  O   . GLY A  1 422 ? 36.533  56.135  46.008  1.00 27.30 ?  446  GLY A O   1 
ATOM   3366  N  N   . ILE A  1 423 ? 37.809  54.643  47.116  1.00 26.94 ?  447  ILE A N   1 
ATOM   3367  C  CA  . ILE A  1 423 ? 39.006  54.865  46.313  1.00 26.22 ?  447  ILE A CA  1 
ATOM   3368  C  C   . ILE A  1 423 ? 39.194  53.727  45.311  1.00 25.69 ?  447  ILE A C   1 
ATOM   3369  O  O   . ILE A  1 423 ? 38.803  52.588  45.576  1.00 25.47 ?  447  ILE A O   1 
ATOM   3370  C  CB  . ILE A  1 423 ? 40.274  55.045  47.199  1.00 26.42 ?  447  ILE A CB  1 
ATOM   3371  C  CG1 . ILE A  1 423 ? 40.478  53.846  48.140  1.00 26.24 ?  447  ILE A CG1 1 
ATOM   3372  C  CG2 . ILE A  1 423 ? 40.202  56.370  47.978  1.00 26.21 ?  447  ILE A CG2 1 
ATOM   3373  C  CD1 . ILE A  1 423 ? 41.818  53.854  48.883  1.00 26.92 ?  447  ILE A CD1 1 
ATOM   3374  N  N   . PHE A  1 424 ? 39.790  54.046  44.163  1.00 25.13 ?  448  PHE A N   1 
ATOM   3375  C  CA  . PHE A  1 424 ? 40.002  53.075  43.086  1.00 24.71 ?  448  PHE A CA  1 
ATOM   3376  C  C   . PHE A  1 424 ? 40.625  51.764  43.575  1.00 24.40 ?  448  PHE A C   1 
ATOM   3377  O  O   . PHE A  1 424 ? 40.277  50.686  43.094  1.00 24.27 ?  448  PHE A O   1 
ATOM   3378  C  CB  . PHE A  1 424 ? 40.860  53.686  41.970  1.00 24.54 ?  448  PHE A CB  1 
ATOM   3379  C  CG  . PHE A  1 424 ? 41.057  52.775  40.792  1.00 24.67 ?  448  PHE A CG  1 
ATOM   3380  C  CD1 . PHE A  1 424 ? 40.082  52.673  39.804  1.00 24.62 ?  448  PHE A CD1 1 
ATOM   3381  C  CD2 . PHE A  1 424 ? 42.216  52.012  40.670  1.00 24.48 ?  448  PHE A CD2 1 
ATOM   3382  C  CE1 . PHE A  1 424 ? 40.258  51.819  38.712  1.00 24.35 ?  448  PHE A CE1 1 
ATOM   3383  C  CE2 . PHE A  1 424 ? 42.401  51.160  39.582  1.00 24.41 ?  448  PHE A CE2 1 
ATOM   3384  C  CZ  . PHE A  1 424 ? 41.420  51.068  38.602  1.00 24.34 ?  448  PHE A CZ  1 
ATOM   3385  N  N   . THR A  1 425 ? 41.539  51.876  44.536  1.00 24.04 ?  449  THR A N   1 
ATOM   3386  C  CA  . THR A  1 425 ? 42.228  50.736  45.133  1.00 23.86 ?  449  THR A CA  1 
ATOM   3387  C  C   . THR A  1 425 ? 41.272  49.636  45.611  1.00 23.82 ?  449  THR A C   1 
ATOM   3388  O  O   . THR A  1 425 ? 41.580  48.447  45.496  1.00 23.77 ?  449  THR A O   1 
ATOM   3389  C  CB  . THR A  1 425 ? 43.146  51.219  46.289  1.00 23.89 ?  449  THR A CB  1 
ATOM   3390  O  OG1 . THR A  1 425 ? 44.261  51.922  45.731  1.00 24.02 ?  449  THR A OG1 1 
ATOM   3391  C  CG2 . THR A  1 425 ? 43.662  50.061  47.136  1.00 23.39 ?  449  THR A CG2 1 
ATOM   3392  N  N   . GLN A  1 426 ? 40.108  50.047  46.116  1.00 23.60 ?  450  GLN A N   1 
ATOM   3393  C  CA  . GLN A  1 426 ? 39.112  49.131  46.669  1.00 23.49 ?  450  GLN A CA  1 
ATOM   3394  C  C   . GLN A  1 426 ? 38.426  48.243  45.626  1.00 23.22 ?  450  GLN A C   1 
ATOM   3395  O  O   . GLN A  1 426 ? 37.674  47.333  45.978  1.00 23.04 ?  450  GLN A O   1 
ATOM   3396  C  CB  . GLN A  1 426 ? 38.081  49.912  47.491  1.00 23.52 ?  450  GLN A CB  1 
ATOM   3397  C  CG  . GLN A  1 426 ? 38.671  50.524  48.765  1.00 23.36 ?  450  GLN A CG  1 
ATOM   3398  C  CD  . GLN A  1 426 ? 37.821  51.636  49.341  1.00 23.74 ?  450  GLN A CD  1 
ATOM   3399  O  OE1 . GLN A  1 426 ? 37.120  52.340  48.611  1.00 22.99 ?  450  GLN A OE1 1 
ATOM   3400  N  NE2 . GLN A  1 426 ? 37.889  51.812  50.658  1.00 23.26 ?  450  GLN A NE2 1 
ATOM   3401  N  N   . LEU A  1 427 ? 38.695  48.504  44.351  1.00 23.13 ?  451  LEU A N   1 
ATOM   3402  C  CA  . LEU A  1 427 ? 38.224  47.642  43.271  1.00 23.12 ?  451  LEU A CA  1 
ATOM   3403  C  C   . LEU A  1 427 ? 39.167  46.462  43.047  1.00 23.01 ?  451  LEU A C   1 
ATOM   3404  O  O   . LEU A  1 427 ? 38.736  45.399  42.598  1.00 23.29 ?  451  LEU A O   1 
ATOM   3405  C  CB  . LEU A  1 427 ? 38.071  48.439  41.971  1.00 23.18 ?  451  LEU A CB  1 
ATOM   3406  C  CG  . LEU A  1 427 ? 36.983  49.518  41.916  1.00 23.54 ?  451  LEU A CG  1 
ATOM   3407  C  CD1 . LEU A  1 427 ? 37.258  50.491  40.776  1.00 23.19 ?  451  LEU A CD1 1 
ATOM   3408  C  CD2 . LEU A  1 427 ? 35.590  48.899  41.783  1.00 23.43 ?  451  LEU A CD2 1 
ATOM   3409  N  N   . PHE A  1 428 ? 40.448  46.654  43.365  1.00 22.86 ?  452  PHE A N   1 
ATOM   3410  C  CA  . PHE A  1 428 ? 41.481  45.651  43.090  1.00 22.66 ?  452  PHE A CA  1 
ATOM   3411  C  C   . PHE A  1 428 ? 42.164  45.102  44.342  1.00 22.64 ?  452  PHE A C   1 
ATOM   3412  O  O   . PHE A  1 428 ? 42.985  44.181  44.259  1.00 22.58 ?  452  PHE A O   1 
ATOM   3413  C  CB  . PHE A  1 428 ? 42.508  46.200  42.090  1.00 22.49 ?  452  PHE A CB  1 
ATOM   3414  C  CG  . PHE A  1 428 ? 42.028  46.174  40.671  1.00 22.32 ?  452  PHE A CG  1 
ATOM   3415  C  CD1 . PHE A  1 428 ? 42.368  45.121  39.830  1.00 21.75 ?  452  PHE A CD1 1 
ATOM   3416  C  CD2 . PHE A  1 428 ? 41.208  47.189  40.182  1.00 22.79 ?  452  PHE A CD2 1 
ATOM   3417  C  CE1 . PHE A  1 428 ? 41.911  45.085  38.512  1.00 22.14 ?  452  PHE A CE1 1 
ATOM   3418  C  CE2 . PHE A  1 428 ? 40.747  47.162  38.869  1.00 22.49 ?  452  PHE A CE2 1 
ATOM   3419  C  CZ  . PHE A  1 428 ? 41.099  46.104  38.034  1.00 22.38 ?  452  PHE A CZ  1 
ATOM   3420  N  N   . TRP A  1 429 ? 41.814  45.672  45.493  1.00 22.59 ?  453  TRP A N   1 
ATOM   3421  C  CA  . TRP A  1 429 ? 42.267  45.181  46.790  1.00 22.51 ?  453  TRP A CA  1 
ATOM   3422  C  C   . TRP A  1 429 ? 41.168  45.325  47.843  1.00 22.70 ?  453  TRP A C   1 
ATOM   3423  O  O   . TRP A  1 429 ? 40.525  46.371  47.949  1.00 22.62 ?  453  TRP A O   1 
ATOM   3424  C  CB  . TRP A  1 429 ? 43.525  45.919  47.257  1.00 22.34 ?  453  TRP A CB  1 
ATOM   3425  C  CG  . TRP A  1 429 ? 43.980  45.491  48.634  1.00 22.58 ?  453  TRP A CG  1 
ATOM   3426  C  CD1 . TRP A  1 429 ? 44.838  44.472  48.934  1.00 22.25 ?  453  TRP A CD1 1 
ATOM   3427  C  CD2 . TRP A  1 429 ? 43.581  46.062  49.889  1.00 22.14 ?  453  TRP A CD2 1 
ATOM   3428  N  NE1 . TRP A  1 429 ? 45.004  44.377  50.292  1.00 22.28 ?  453  TRP A NE1 1 
ATOM   3429  C  CE2 . TRP A  1 429 ? 44.240  45.338  50.903  1.00 22.53 ?  453  TRP A CE2 1 
ATOM   3430  C  CE3 . TRP A  1 429 ? 42.732  47.119  50.252  1.00 22.39 ?  453  TRP A CE3 1 
ATOM   3431  C  CZ2 . TRP A  1 429 ? 44.089  45.641  52.263  1.00 23.14 ?  453  TRP A CZ2 1 
ATOM   3432  C  CZ3 . TRP A  1 429 ? 42.570  47.413  51.608  1.00 22.94 ?  453  TRP A CZ3 1 
ATOM   3433  C  CH2 . TRP A  1 429 ? 43.250  46.675  52.594  1.00 22.79 ?  453  TRP A CH2 1 
ATOM   3434  N  N   . SER A  1 430 ? 40.978  44.264  48.622  1.00 22.68 ?  454  SER A N   1 
ATOM   3435  C  CA  . SER A  1 430 ? 40.054  44.266  49.746  1.00 22.85 ?  454  SER A CA  1 
ATOM   3436  C  C   . SER A  1 430 ? 40.562  43.344  50.851  1.00 23.06 ?  454  SER A C   1 
ATOM   3437  O  O   . SER A  1 430 ? 41.168  42.305  50.577  1.00 23.08 ?  454  SER A O   1 
ATOM   3438  C  CB  . SER A  1 430 ? 38.653  43.829  49.303  1.00 22.87 ?  454  SER A CB  1 
ATOM   3439  O  OG  . SER A  1 430 ? 38.678  42.546  48.697  1.00 22.12 ?  454  SER A OG  1 
ATOM   3440  N  N   . LYS A  1 431 ? 40.321  43.745  52.096  1.00 23.24 ?  455  LYS A N   1 
ATOM   3441  C  CA  . LYS A  1 431 ? 40.652  42.939  53.270  1.00 23.45 ?  455  LYS A CA  1 
ATOM   3442  C  C   . LYS A  1 431 ? 39.732  43.368  54.406  1.00 23.44 ?  455  LYS A C   1 
ATOM   3443  O  O   . LYS A  1 431 ? 39.492  44.563  54.598  1.00 23.31 ?  455  LYS A O   1 
ATOM   3444  C  CB  . LYS A  1 431 ? 42.118  43.133  53.672  1.00 23.64 ?  455  LYS A CB  1 
ATOM   3445  C  CG  . LYS A  1 431 ? 42.652  42.091  54.657  1.00 24.45 ?  455  LYS A CG  1 
ATOM   3446  C  CD  . LYS A  1 431 ? 44.041  42.472  55.152  1.00 26.26 ?  455  LYS A CD  1 
ATOM   3447  C  CE  . LYS A  1 431 ? 44.580  41.471  56.172  1.00 26.87 ?  455  LYS A CE  1 
ATOM   3448  N  NZ  . LYS A  1 431 ? 44.939  40.166  55.536  1.00 27.25 ?  455  LYS A NZ  1 
ATOM   3449  N  N   . GLY A  1 432 ? 39.220  42.394  55.153  1.00 23.48 ?  456  GLY A N   1 
ATOM   3450  C  CA  . GLY A  1 432 ? 38.237  42.666  56.199  1.00 23.72 ?  456  GLY A CA  1 
ATOM   3451  C  C   . GLY A  1 432 ? 37.084  43.466  55.622  1.00 23.96 ?  456  GLY A C   1 
ATOM   3452  O  O   . GLY A  1 432 ? 36.552  43.123  54.561  1.00 23.66 ?  456  GLY A O   1 
ATOM   3453  N  N   . ASN A  1 433 ? 36.718  44.545  56.310  1.00 23.95 ?  457  ASN A N   1 
ATOM   3454  C  CA  . ASN A  1 433 ? 35.689  45.458  55.819  1.00 23.99 ?  457  ASN A CA  1 
ATOM   3455  C  C   . ASN A  1 433 ? 36.265  46.719  55.168  1.00 24.01 ?  457  ASN A C   1 
ATOM   3456  O  O   . ASN A  1 433 ? 35.660  47.790  55.223  1.00 24.00 ?  457  ASN A O   1 
ATOM   3457  C  CB  . ASN A  1 433 ? 34.701  45.818  56.938  1.00 24.03 ?  457  ASN A CB  1 
ATOM   3458  C  CG  . ASN A  1 433 ? 34.075  44.595  57.582  1.00 23.72 ?  457  ASN A CG  1 
ATOM   3459  O  OD1 . ASN A  1 433 ? 34.134  44.426  58.799  1.00 23.13 ?  457  ASN A OD1 1 
ATOM   3460  N  ND2 . ASN A  1 433 ? 33.476  43.734  56.768  1.00 22.88 ?  457  ASN A ND2 1 
ATOM   3461  N  N   . ASN A  1 434 ? 37.442  46.586  54.560  1.00 24.06 ?  458  ASN A N   1 
ATOM   3462  C  CA  . ASN A  1 434 ? 37.962  47.621  53.672  1.00 23.99 ?  458  ASN A CA  1 
ATOM   3463  C  C   . ASN A  1 434 ? 37.966  47.108  52.232  1.00 23.89 ?  458  ASN A C   1 
ATOM   3464  O  O   . ASN A  1 434 ? 38.858  46.352  51.851  1.00 24.14 ?  458  ASN A O   1 
ATOM   3465  C  CB  . ASN A  1 434 ? 39.364  48.081  54.090  1.00 23.72 ?  458  ASN A CB  1 
ATOM   3466  C  CG  . ASN A  1 434 ? 39.768  49.401  53.439  1.00 24.11 ?  458  ASN A CG  1 
ATOM   3467  O  OD1 . ASN A  1 434 ? 39.057  49.935  52.583  1.00 23.52 ?  458  ASN A OD1 1 
ATOM   3468  N  ND2 . ASN A  1 434 ? 40.917  49.937  53.851  1.00 23.86 ?  458  ASN A ND2 1 
ATOM   3469  N  N   . PRO A  1 435 ? 36.965  47.513  51.428  1.00 23.74 ?  459  PRO A N   1 
ATOM   3470  C  CA  . PRO A  1 435 ? 35.872  48.421  51.776  1.00 23.71 ?  459  PRO A CA  1 
ATOM   3471  C  C   . PRO A  1 435 ? 34.665  47.719  52.405  1.00 23.68 ?  459  PRO A C   1 
ATOM   3472  O  O   . PRO A  1 435 ? 34.619  46.484  52.478  1.00 23.64 ?  459  PRO A O   1 
ATOM   3473  C  CB  . PRO A  1 435 ? 35.462  48.977  50.416  1.00 23.62 ?  459  PRO A CB  1 
ATOM   3474  C  CG  . PRO A  1 435 ? 35.656  47.812  49.498  1.00 23.80 ?  459  PRO A CG  1 
ATOM   3475  C  CD  . PRO A  1 435 ? 36.901  47.114  50.009  1.00 23.79 ?  459  PRO A CD  1 
ATOM   3476  N  N   . ALA A  1 436 ? 33.706  48.518  52.862  1.00 23.67 ?  460  ALA A N   1 
ATOM   3477  C  CA  . ALA A  1 436 ? 32.395  48.012  53.250  1.00 23.74 ?  460  ALA A CA  1 
ATOM   3478  C  C   . ALA A  1 436 ? 31.571  47.796  51.984  1.00 23.80 ?  460  ALA A C   1 
ATOM   3479  O  O   . ALA A  1 436 ? 31.859  48.396  50.942  1.00 23.47 ?  460  ALA A O   1 
ATOM   3480  C  CB  . ALA A  1 436 ? 31.699  49.000  54.175  1.00 23.82 ?  460  ALA A CB  1 
ATOM   3481  N  N   . SER A  1 437 ? 30.551  46.946  52.070  1.00 23.93 ?  461  SER A N   1 
ATOM   3482  C  CA  . SER A  1 437 ? 29.693  46.679  50.913  1.00 24.30 ?  461  SER A CA  1 
ATOM   3483  C  C   . SER A  1 437 ? 29.019  47.943  50.364  1.00 24.28 ?  461  SER A C   1 
ATOM   3484  O  O   . SER A  1 437 ? 29.048  48.174  49.157  1.00 24.45 ?  461  SER A O   1 
ATOM   3485  C  CB  . SER A  1 437 ? 28.656  45.602  51.225  1.00 24.25 ?  461  SER A CB  1 
ATOM   3486  O  OG  . SER A  1 437 ? 27.900  45.295  50.069  1.00 24.77 ?  461  SER A OG  1 
ATOM   3487  N  N   . LEU A  1 438 ? 28.430  48.759  51.244  1.00 24.30 ?  462  LEU A N   1 
ATOM   3488  C  CA  . LEU A  1 438 ? 27.799  50.023  50.828  1.00 24.40 ?  462  LEU A CA  1 
ATOM   3489  C  C   . LEU A  1 438 ? 28.768  50.932  50.083  1.00 24.25 ?  462  LEU A C   1 
ATOM   3490  O  O   . LEU A  1 438 ? 28.396  51.591  49.108  1.00 24.02 ?  462  LEU A O   1 
ATOM   3491  C  CB  . LEU A  1 438 ? 27.243  50.791  52.029  1.00 24.35 ?  462  LEU A CB  1 
ATOM   3492  C  CG  . LEU A  1 438 ? 25.736  50.801  52.293  1.00 25.27 ?  462  LEU A CG  1 
ATOM   3493  C  CD1 . LEU A  1 438 ? 25.440  51.693  53.483  1.00 25.80 ?  462  LEU A CD1 1 
ATOM   3494  C  CD2 . LEU A  1 438 ? 24.928  51.255  51.076  1.00 24.63 ?  462  LEU A CD2 1 
ATOM   3495  N  N   . GLU A  1 439 ? 30.005  50.963  50.575  1.00 24.04 ?  463  GLU A N   1 
ATOM   3496  C  CA  . GLU A  1 439 ? 31.075  51.792  50.034  1.00 23.95 ?  463  GLU A CA  1 
ATOM   3497  C  C   . GLU A  1 439 ? 31.487  51.340  48.628  1.00 23.65 ?  463  GLU A C   1 
ATOM   3498  O  O   . GLU A  1 439 ? 31.679  52.168  47.741  1.00 23.48 ?  463  GLU A O   1 
ATOM   3499  C  CB  . GLU A  1 439 ? 32.262  51.749  50.999  1.00 24.10 ?  463  GLU A CB  1 
ATOM   3500  C  CG  . GLU A  1 439 ? 33.498  52.523  50.583  1.00 24.38 ?  463  GLU A CG  1 
ATOM   3501  C  CD  . GLU A  1 439 ? 34.620  52.376  51.591  1.00 24.61 ?  463  GLU A CD  1 
ATOM   3502  O  OE1 . GLU A  1 439 ? 34.548  51.458  52.435  1.00 23.83 ?  463  GLU A OE1 1 
ATOM   3503  O  OE2 . GLU A  1 439 ? 35.575  53.181  51.540  1.00 25.69 -1 463  GLU A OE2 1 
ATOM   3504  N  N   . LEU A  1 440 ? 31.610  50.028  48.438  1.00 23.46 ?  464  LEU A N   1 
ATOM   3505  C  CA  . LEU A  1 440 ? 31.952  49.449  47.138  1.00 23.49 ?  464  LEU A CA  1 
ATOM   3506  C  C   . LEU A  1 440 ? 30.801  49.638  46.147  1.00 23.29 ?  464  LEU A C   1 
ATOM   3507  O  O   . LEU A  1 440 ? 31.022  49.928  44.971  1.00 23.20 ?  464  LEU A O   1 
ATOM   3508  C  CB  . LEU A  1 440 ? 32.250  47.948  47.283  1.00 23.22 ?  464  LEU A CB  1 
ATOM   3509  C  CG  . LEU A  1 440 ? 33.254  47.214  46.371  1.00 23.78 ?  464  LEU A CG  1 
ATOM   3510  C  CD1 . LEU A  1 440 ? 32.681  45.869  45.948  1.00 22.29 ?  464  LEU A CD1 1 
ATOM   3511  C  CD2 . LEU A  1 440 ? 33.719  48.008  45.138  1.00 23.60 ?  464  LEU A CD2 1 
ATOM   3512  N  N   . LYS A  1 441 ? 29.575  49.468  46.639  1.00 23.16 ?  465  LYS A N   1 
ATOM   3513  C  CA  . LYS A  1 441 ? 28.381  49.555  45.800  1.00 23.34 ?  465  LYS A CA  1 
ATOM   3514  C  C   . LYS A  1 441 ? 28.221  50.924  45.140  1.00 23.17 ?  465  LYS A C   1 
ATOM   3515  O  O   . LYS A  1 441 ? 27.919  51.007  43.948  1.00 23.06 ?  465  LYS A O   1 
ATOM   3516  C  CB  . LYS A  1 441 ? 27.121  49.194  46.594  1.00 23.09 ?  465  LYS A CB  1 
ATOM   3517  C  CG  . LYS A  1 441 ? 25.912  48.890  45.704  1.00 23.33 ?  465  LYS A CG  1 
ATOM   3518  C  CD  . LYS A  1 441 ? 24.756  48.291  46.487  1.00 23.43 ?  465  LYS A CD  1 
ATOM   3519  C  CE  . LYS A  1 441 ? 25.009  46.833  46.847  1.00 23.21 ?  465  LYS A CE  1 
ATOM   3520  N  NZ  . LYS A  1 441 ? 23.900  46.301  47.683  1.00 23.35 ?  465  LYS A NZ  1 
ATOM   3521  N  N   . VAL A  1 442 ? 28.429  51.986  45.916  1.00 23.24 ?  466  VAL A N   1 
ATOM   3522  C  CA  . VAL A  1 442 ? 28.281  53.349  45.403  1.00 23.29 ?  466  VAL A CA  1 
ATOM   3523  C  C   . VAL A  1 442 ? 29.479  53.735  44.526  1.00 23.51 ?  466  VAL A C   1 
ATOM   3524  O  O   . VAL A  1 442 ? 29.352  54.561  43.616  1.00 23.63 ?  466  VAL A O   1 
ATOM   3525  C  CB  . VAL A  1 442 ? 28.007  54.387  46.541  1.00 23.20 ?  466  VAL A CB  1 
ATOM   3526  C  CG1 . VAL A  1 442 ? 29.259  54.662  47.375  1.00 23.04 ?  466  VAL A CG1 1 
ATOM   3527  C  CG2 . VAL A  1 442 ? 27.431  55.686  45.965  1.00 22.88 ?  466  VAL A CG2 1 
ATOM   3528  N  N   . LEU A  1 443 ? 30.629  53.120  44.799  1.00 23.64 ?  467  LEU A N   1 
ATOM   3529  C  CA  . LEU A  1 443 ? 31.825  53.299  43.982  1.00 23.84 ?  467  LEU A CA  1 
ATOM   3530  C  C   . LEU A  1 443 ? 31.577  52.733  42.587  1.00 23.79 ?  467  LEU A C   1 
ATOM   3531  O  O   . LEU A  1 443 ? 31.788  53.422  41.586  1.00 23.96 ?  467  LEU A O   1 
ATOM   3532  C  CB  . LEU A  1 443 ? 33.029  52.590  44.621  1.00 23.82 ?  467  LEU A CB  1 
ATOM   3533  C  CG  . LEU A  1 443 ? 34.467  53.097  44.424  1.00 24.24 ?  467  LEU A CG  1 
ATOM   3534  C  CD1 . LEU A  1 443 ? 35.464  51.958  44.690  1.00 24.03 ?  467  LEU A CD1 1 
ATOM   3535  C  CD2 . LEU A  1 443 ? 34.734  53.729  43.062  1.00 23.60 ?  467  LEU A CD2 1 
ATOM   3536  N  N   . GLU A  1 444 ? 31.121  51.483  42.530  1.00 23.69 ?  468  GLU A N   1 
ATOM   3537  C  CA  . GLU A  1 444 ? 30.828  50.821  41.254  1.00 23.58 ?  468  GLU A CA  1 
ATOM   3538  C  C   . GLU A  1 444 ? 29.666  51.486  40.519  1.00 23.48 ?  468  GLU A C   1 
ATOM   3539  O  O   . GLU A  1 444 ? 29.598  51.441  39.291  1.00 23.38 ?  468  GLU A O   1 
ATOM   3540  C  CB  . GLU A  1 444 ? 30.570  49.329  41.462  1.00 23.50 ?  468  GLU A CB  1 
ATOM   3541  C  CG  . GLU A  1 444 ? 31.808  48.587  41.948  1.00 24.09 ?  468  GLU A CG  1 
ATOM   3542  C  CD  . GLU A  1 444 ? 31.560  47.130  42.279  1.00 25.18 ?  468  GLU A CD  1 
ATOM   3543  O  OE1 . GLU A  1 444 ? 30.456  46.787  42.756  1.00 24.72 ?  468  GLU A OE1 1 
ATOM   3544  O  OE2 . GLU A  1 444 ? 32.492  46.323  42.068  1.00 26.83 -1 468  GLU A OE2 1 
ATOM   3545  N  N   . MET A  1 445 ? 28.770  52.115  41.277  1.00 23.44 ?  469  MET A N   1 
ATOM   3546  C  CA  . MET A  1 445 ? 27.668  52.885  40.704  1.00 23.41 ?  469  MET A CA  1 
ATOM   3547  C  C   . MET A  1 445 ? 28.189  53.976  39.758  1.00 23.43 ?  469  MET A C   1 
ATOM   3548  O  O   . MET A  1 445 ? 27.649  54.165  38.665  1.00 23.33 ?  469  MET A O   1 
ATOM   3549  C  CB  . MET A  1 445 ? 26.800  53.486  41.817  1.00 23.31 ?  469  MET A CB  1 
ATOM   3550  C  CG  . MET A  1 445 ? 25.537  54.181  41.329  1.00 23.52 ?  469  MET A CG  1 
ATOM   3551  S  SD  . MET A  1 445 ? 24.600  54.932  42.677  1.00 24.36 ?  469  MET A SD  1 
ATOM   3552  C  CE  . MET A  1 445 ? 23.103  55.411  41.819  1.00 23.73 ?  469  MET A CE  1 
ATOM   3553  N  N   . ALA A  1 446 ? 29.244  54.673  40.181  1.00 23.44 ?  470  ALA A N   1 
ATOM   3554  C  CA  . ALA A  1 446 ? 29.882  55.695  39.352  1.00 23.50 ?  470  ALA A CA  1 
ATOM   3555  C  C   . ALA A  1 446 ? 30.898  55.102  38.377  1.00 23.49 ?  470  ALA A C   1 
ATOM   3556  O  O   . ALA A  1 446 ? 30.849  55.385  37.177  1.00 23.18 ?  470  ALA A O   1 
ATOM   3557  C  CB  . ALA A  1 446 ? 30.549  56.748  40.224  1.00 23.55 ?  470  ALA A CB  1 
ATOM   3558  N  N   . GLU A  1 447 ? 31.811  54.289  38.911  1.00 23.50 ?  471  GLU A N   1 
ATOM   3559  C  CA  . GLU A  1 447 ? 32.942  53.740  38.163  1.00 23.73 ?  471  GLU A CA  1 
ATOM   3560  C  C   . GLU A  1 447 ? 32.519  52.851  37.000  1.00 23.47 ?  471  GLU A C   1 
ATOM   3561  O  O   . GLU A  1 447 ? 33.095  52.928  35.914  1.00 23.45 ?  471  GLU A O   1 
ATOM   3562  C  CB  . GLU A  1 447 ? 33.858  52.944  39.107  1.00 24.05 ?  471  GLU A CB  1 
ATOM   3563  C  CG  . GLU A  1 447 ? 35.181  52.502  38.497  1.00 24.92 ?  471  GLU A CG  1 
ATOM   3564  C  CD  . GLU A  1 447 ? 36.201  53.629  38.379  1.00 26.36 ?  471  GLU A CD  1 
ATOM   3565  O  OE1 . GLU A  1 447 ? 36.009  54.689  39.008  1.00 27.32 ?  471  GLU A OE1 1 
ATOM   3566  O  OE2 . GLU A  1 447 ? 37.203  53.452  37.655  1.00 27.23 -1 471  GLU A OE2 1 
ATOM   3567  N  N   . ASN A  1 448 ? 31.524  52.002  37.246  1.00 23.07 ?  472  ASN A N   1 
ATOM   3568  C  CA  . ASN A  1 448 ? 31.052  51.049  36.251  1.00 22.93 ?  472  ASN A CA  1 
ATOM   3569  C  C   . ASN A  1 448 ? 29.770  51.495  35.566  1.00 22.79 ?  472  ASN A C   1 
ATOM   3570  O  O   . ASN A  1 448 ? 29.733  51.661  34.346  1.00 22.78 ?  472  ASN A O   1 
ATOM   3571  C  CB  . ASN A  1 448 ? 30.829  49.667  36.884  1.00 22.81 ?  472  ASN A CB  1 
ATOM   3572  C  CG  . ASN A  1 448 ? 32.088  49.093  37.494  1.00 23.01 ?  472  ASN A CG  1 
ATOM   3573  O  OD1 . ASN A  1 448 ? 33.204  49.457  37.112  1.00 22.19 ?  472  ASN A OD1 1 
ATOM   3574  N  ND2 . ASN A  1 448 ? 31.916  48.185  38.449  1.00 22.45 ?  472  ASN A ND2 1 
ATOM   3575  N  N   . ASN A  1 449 ? 28.721  51.690  36.359  1.00 22.53 ?  473  ASN A N   1 
ATOM   3576  C  CA  . ASN A  1 449 ? 27.380  51.837  35.806  1.00 22.46 ?  473  ASN A CA  1 
ATOM   3577  C  C   . ASN A  1 449 ? 27.057  53.215  35.230  1.00 22.23 ?  473  ASN A C   1 
ATOM   3578  O  O   . ASN A  1 449 ? 26.376  53.311  34.210  1.00 22.32 ?  473  ASN A O   1 
ATOM   3579  C  CB  . ASN A  1 449 ? 26.339  51.342  36.811  1.00 22.40 ?  473  ASN A CB  1 
ATOM   3580  C  CG  . ASN A  1 449 ? 26.531  49.866  37.149  1.00 22.82 ?  473  ASN A CG  1 
ATOM   3581  O  OD1 . ASN A  1 449 ? 26.804  49.508  38.299  1.00 23.73 ?  473  ASN A OD1 1 
ATOM   3582  N  ND2 . ASN A  1 449 ? 26.434  49.008  36.136  1.00 20.73 ?  473  ASN A ND2 1 
ATOM   3583  N  N   . LEU A  1 450 ? 27.569  54.269  35.864  1.00 21.94 ?  474  LEU A N   1 
ATOM   3584  C  CA  . LEU A  1 450 ? 27.479  55.615  35.306  1.00 21.82 ?  474  LEU A CA  1 
ATOM   3585  C  C   . LEU A  1 450 ? 28.367  55.739  34.062  1.00 21.38 ?  474  LEU A C   1 
ATOM   3586  O  O   . LEU A  1 450 ? 27.967  56.330  33.066  1.00 20.99 ?  474  LEU A O   1 
ATOM   3587  C  CB  . LEU A  1 450 ? 27.890  56.666  36.340  1.00 21.79 ?  474  LEU A CB  1 
ATOM   3588  C  CG  . LEU A  1 450 ? 27.283  58.077  36.338  1.00 23.06 ?  474  LEU A CG  1 
ATOM   3589  C  CD1 . LEU A  1 450 ? 28.314  59.080  36.873  1.00 23.07 ?  474  LEU A CD1 1 
ATOM   3590  C  CD2 . LEU A  1 450 ? 26.725  58.549  34.988  1.00 23.15 ?  474  LEU A CD2 1 
ATOM   3591  N  N   . ALA A  1 451 ? 29.575  55.188  34.130  1.00 21.23 ?  475  ALA A N   1 
ATOM   3592  C  CA  . ALA A  1 451 ? 30.466  55.201  32.975  1.00 21.19 ?  475  ALA A CA  1 
ATOM   3593  C  C   . ALA A  1 451 ? 29.846  54.467  31.774  1.00 21.20 ?  475  ALA A C   1 
ATOM   3594  O  O   . ALA A  1 451 ? 29.851  54.998  30.665  1.00 21.14 ?  475  ALA A O   1 
ATOM   3595  C  CB  . ALA A  1 451 ? 31.838  54.637  33.332  1.00 21.21 ?  475  ALA A CB  1 
ATOM   3596  N  N   . LYS A  1 452 ? 29.288  53.275  31.999  1.00 20.95 ?  476  LYS A N   1 
ATOM   3597  C  CA  . LYS A  1 452 ? 28.633  52.521  30.914  1.00 21.02 ?  476  LYS A CA  1 
ATOM   3598  C  C   . LYS A  1 452 ? 27.400  53.235  30.356  1.00 20.86 ?  476  LYS A C   1 
ATOM   3599  O  O   . LYS A  1 452 ? 27.141  53.176  29.150  1.00 20.86 ?  476  LYS A O   1 
ATOM   3600  C  CB  . LYS A  1 452 ? 28.291  51.086  31.337  1.00 21.11 ?  476  LYS A CB  1 
ATOM   3601  C  CG  . LYS A  1 452 ? 29.515  50.165  31.456  1.00 21.08 ?  476  LYS A CG  1 
ATOM   3602  C  CD  . LYS A  1 452 ? 29.126  48.680  31.533  1.00 20.30 ?  476  LYS A CD  1 
ATOM   3603  C  CE  . LYS A  1 452 ? 28.606  48.289  32.910  1.00 19.97 ?  476  LYS A CE  1 
ATOM   3604  N  NZ  . LYS A  1 452 ? 28.230  46.843  32.968  1.00 19.16 ?  476  LYS A NZ  1 
ATOM   3605  N  N   . MET A  1 453 ? 26.658  53.914  31.231  1.00 20.84 ?  477  MET A N   1 
ATOM   3606  C  CA  . MET A  1 453 ? 25.534  54.756  30.812  1.00 20.83 ?  477  MET A CA  1 
ATOM   3607  C  C   . MET A  1 453 ? 25.975  55.798  29.790  1.00 20.68 ?  477  MET A C   1 
ATOM   3608  O  O   . MET A  1 453 ? 25.357  55.934  28.730  1.00 20.54 ?  477  MET A O   1 
ATOM   3609  C  CB  . MET A  1 453 ? 24.884  55.462  32.008  1.00 20.89 ?  477  MET A CB  1 
ATOM   3610  C  CG  . MET A  1 453 ? 23.627  56.239  31.632  1.00 21.12 ?  477  MET A CG  1 
ATOM   3611  S  SD  . MET A  1 453 ? 22.768  56.961  33.041  1.00 21.96 ?  477  MET A SD  1 
ATOM   3612  C  CE  . MET A  1 453 ? 21.448  57.827  32.203  1.00 20.77 ?  477  MET A CE  1 
ATOM   3613  N  N   . HIS A  1 454 ? 27.034  56.537  30.121  1.00 20.49 ?  478  HIS A N   1 
ATOM   3614  C  CA  . HIS A  1 454 ? 27.597  57.512  29.190  1.00 20.39 ?  478  HIS A CA  1 
ATOM   3615  C  C   . HIS A  1 454 ? 28.072  56.861  27.890  1.00 19.89 ?  478  HIS A C   1 
ATOM   3616  O  O   . HIS A  1 454 ? 27.816  57.388  26.813  1.00 20.01 ?  478  HIS A O   1 
ATOM   3617  C  CB  . HIS A  1 454 ? 28.748  58.311  29.804  1.00 20.46 ?  478  HIS A CB  1 
ATOM   3618  C  CG  . HIS A  1 454 ? 29.511  59.101  28.787  1.00 21.12 ?  478  HIS A CG  1 
ATOM   3619  N  ND1 . HIS A  1 454 ? 28.980  60.209  28.163  1.00 21.37 ?  478  HIS A ND1 1 
ATOM   3620  C  CD2 . HIS A  1 454 ? 30.732  58.907  28.237  1.00 21.08 ?  478  HIS A CD2 1 
ATOM   3621  C  CE1 . HIS A  1 454 ? 29.851  60.679  27.289  1.00 21.27 ?  478  HIS A CE1 1 
ATOM   3622  N  NE2 . HIS A  1 454 ? 30.923  59.907  27.314  1.00 22.17 ?  478  HIS A NE2 1 
ATOM   3623  N  N   . VAL A  1 455 ? 28.767  55.729  27.998  1.00 19.65 ?  479  VAL A N   1 
ATOM   3624  C  CA  . VAL A  1 455 ? 29.229  54.994  26.813  1.00 19.64 ?  479  VAL A CA  1 
ATOM   3625  C  C   . VAL A  1 455 ? 28.053  54.620  25.905  1.00 19.62 ?  479  VAL A C   1 
ATOM   3626  O  O   . VAL A  1 455 ? 28.129  54.794  24.693  1.00 19.93 ?  479  VAL A O   1 
ATOM   3627  C  CB  . VAL A  1 455 ? 30.067  53.735  27.176  1.00 19.78 ?  479  VAL A CB  1 
ATOM   3628  C  CG1 . VAL A  1 455 ? 30.454  52.959  25.909  1.00 19.27 ?  479  VAL A CG1 1 
ATOM   3629  C  CG2 . VAL A  1 455 ? 31.318  54.125  27.945  1.00 19.06 ?  479  VAL A CG2 1 
ATOM   3630  N  N   . GLY A  1 456 ? 26.967  54.136  26.503  1.00 19.68 ?  480  GLY A N   1 
ATOM   3631  C  CA  . GLY A  1 456 ? 25.755  53.791  25.765  1.00 19.74 ?  480  GLY A CA  1 
ATOM   3632  C  C   . GLY A  1 456 ? 25.159  54.976  25.028  1.00 19.88 ?  480  GLY A C   1 
ATOM   3633  O  O   . GLY A  1 456 ? 24.775  54.857  23.862  1.00 19.85 ?  480  GLY A O   1 
ATOM   3634  N  N   . LEU A  1 457 ? 25.082  56.114  25.717  1.00 19.89 ?  481  LEU A N   1 
ATOM   3635  C  CA  . LEU A  1 457 ? 24.619  57.371  25.127  1.00 20.00 ?  481  LEU A CA  1 
ATOM   3636  C  C   . LEU A  1 457 ? 25.536  57.844  24.006  1.00 19.94 ?  481  LEU A C   1 
ATOM   3637  O  O   . LEU A  1 457 ? 25.065  58.166  22.913  1.00 19.96 ?  481  LEU A O   1 
ATOM   3638  C  CB  . LEU A  1 457 ? 24.495  58.465  26.196  1.00 19.91 ?  481  LEU A CB  1 
ATOM   3639  C  CG  . LEU A  1 457 ? 23.306  58.371  27.156  1.00 20.30 ?  481  LEU A CG  1 
ATOM   3640  C  CD1 . LEU A  1 457 ? 23.615  59.043  28.486  1.00 19.40 ?  481  LEU A CD1 1 
ATOM   3641  C  CD2 . LEU A  1 457 ? 22.055  58.972  26.532  1.00 20.37 ?  481  LEU A CD2 1 
ATOM   3642  N  N   . ALA A  1 458 ? 26.842  57.875  24.277  1.00 19.67 ?  482  ALA A N   1 
ATOM   3643  C  CA  . ALA A  1 458 ? 27.822  58.324  23.287  1.00 19.62 ?  482  ALA A CA  1 
ATOM   3644  C  C   . ALA A  1 458 ? 27.823  57.468  22.016  1.00 19.42 ?  482  ALA A C   1 
ATOM   3645  O  O   . ALA A  1 458 ? 28.036  57.987  20.920  1.00 19.63 ?  482  ALA A O   1 
ATOM   3646  C  CB  . ALA A  1 458 ? 29.223  58.384  23.897  1.00 19.36 ?  482  ALA A CB  1 
ATOM   3647  N  N   . HIS A  1 459 ? 27.569  56.171  22.163  1.00 19.17 ?  483  HIS A N   1 
ATOM   3648  C  CA  . HIS A  1 459 ? 27.668  55.246  21.026  1.00 19.17 ?  483  HIS A CA  1 
ATOM   3649  C  C   . HIS A  1 459 ? 26.317  54.724  20.502  1.00 19.07 ?  483  HIS A C   1 
ATOM   3650  O  O   . HIS A  1 459 ? 26.268  53.792  19.695  1.00 19.11 ?  483  HIS A O   1 
ATOM   3651  C  CB  . HIS A  1 459 ? 28.706  54.155  21.323  1.00 19.25 ?  483  HIS A CB  1 
ATOM   3652  C  CG  . HIS A  1 459 ? 30.081  54.713  21.550  1.00 19.77 ?  483  HIS A CG  1 
ATOM   3653  N  ND1 . HIS A  1 459 ? 30.528  55.120  22.790  1.00 20.01 ?  483  HIS A ND1 1 
ATOM   3654  C  CD2 . HIS A  1 459 ? 31.077  55.000  20.680  1.00 18.99 ?  483  HIS A CD2 1 
ATOM   3655  C  CE1 . HIS A  1 459 ? 31.756  55.599  22.677  1.00 20.02 ?  483  HIS A CE1 1 
ATOM   3656  N  NE2 . HIS A  1 459 ? 32.112  55.545  21.404  1.00 20.50 ?  483  HIS A NE2 1 
ATOM   3657  N  N   . VAL A  1 460 ? 25.234  55.360  20.957  1.00 18.70 ?  484  VAL A N   1 
ATOM   3658  C  CA  . VAL A  1 460 ? 23.889  55.226  20.371  1.00 18.58 ?  484  VAL A CA  1 
ATOM   3659  C  C   . VAL A  1 460 ? 23.258  53.828  20.526  1.00 18.49 ?  484  VAL A C   1 
ATOM   3660  O  O   . VAL A  1 460 ? 22.566  53.336  19.632  1.00 18.16 ?  484  VAL A O   1 
ATOM   3661  C  CB  . VAL A  1 460 ? 23.837  55.714  18.879  1.00 18.59 ?  484  VAL A CB  1 
ATOM   3662  C  CG1 . VAL A  1 460 ? 22.410  56.009  18.466  1.00 18.57 ?  484  VAL A CG1 1 
ATOM   3663  C  CG2 . VAL A  1 460 ? 24.698  56.967  18.675  1.00 18.57 ?  484  VAL A CG2 1 
ATOM   3664  N  N   . ASN A  1 461 ? 23.500  53.198  21.670  1.00 18.41 ?  485  ASN A N   1 
ATOM   3665  C  CA  . ASN A  1 461 ? 22.827  51.950  22.005  1.00 18.43 ?  485  ASN A CA  1 
ATOM   3666  C  C   . ASN A  1 461 ? 21.766  52.199  23.074  1.00 18.26 ?  485  ASN A C   1 
ATOM   3667  O  O   . ASN A  1 461 ? 22.093  52.238  24.258  1.00 18.39 ?  485  ASN A O   1 
ATOM   3668  C  CB  . ASN A  1 461 ? 23.827  50.891  22.472  1.00 18.31 ?  485  ASN A CB  1 
ATOM   3669  C  CG  . ASN A  1 461 ? 23.168  49.550  22.756  1.00 18.45 ?  485  ASN A CG  1 
ATOM   3670  O  OD1 . ASN A  1 461 ? 22.222  49.155  22.078  1.00 17.28 ?  485  ASN A OD1 1 
ATOM   3671  N  ND2 . ASN A  1 461 ? 23.668  48.847  23.768  1.00 18.72 ?  485  ASN A ND2 1 
ATOM   3672  N  N   . PRO A  1 462 ? 20.494  52.357  22.657  1.00 18.42 ?  486  PRO A N   1 
ATOM   3673  C  CA  . PRO A  1 462 ? 19.397  52.765  23.544  1.00 18.66 ?  486  PRO A CA  1 
ATOM   3674  C  C   . PRO A  1 462 ? 19.263  51.921  24.813  1.00 18.77 ?  486  PRO A C   1 
ATOM   3675  O  O   . PRO A  1 462 ? 19.016  52.471  25.887  1.00 18.68 ?  486  PRO A O   1 
ATOM   3676  C  CB  . PRO A  1 462 ? 18.151  52.610  22.664  1.00 18.39 ?  486  PRO A CB  1 
ATOM   3677  C  CG  . PRO A  1 462 ? 18.655  52.725  21.280  1.00 18.81 ?  486  PRO A CG  1 
ATOM   3678  C  CD  . PRO A  1 462 ? 20.006  52.086  21.290  1.00 18.41 ?  486  PRO A CD  1 
ATOM   3679  N  N   . GLY A  1 463 ? 19.424  50.605  24.686  1.00 18.99 ?  487  GLY A N   1 
ATOM   3680  C  CA  . GLY A  1 463 ? 19.349  49.705  25.839  1.00 19.26 ?  487  GLY A CA  1 
ATOM   3681  C  C   . GLY A  1 463 ? 20.499  49.898  26.813  1.00 19.47 ?  487  GLY A C   1 
ATOM   3682  O  O   . GLY A  1 463 ? 20.378  49.565  27.995  1.00 19.52 ?  487  GLY A O   1 
ATOM   3683  N  N   . GLY A  1 464 ? 21.606  50.446  26.311  1.00 19.57 ?  488  GLY A N   1 
ATOM   3684  C  CA  . GLY A  1 464 ? 22.833  50.642  27.087  1.00 19.72 ?  488  GLY A CA  1 
ATOM   3685  C  C   . GLY A  1 464 ? 22.843  51.843  28.017  1.00 20.09 ?  488  GLY A C   1 
ATOM   3686  O  O   . GLY A  1 464 ? 23.810  52.055  28.753  1.00 20.14 ?  488  GLY A O   1 
ATOM   3687  N  N   . TRP A  1 465 ? 21.785  52.646  27.985  1.00 20.19 ?  489  TRP A N   1 
ATOM   3688  C  CA  . TRP A  1 465 ? 21.640  53.698  28.988  1.00 20.34 ?  489  TRP A CA  1 
ATOM   3689  C  C   . TRP A  1 465 ? 20.306  53.637  29.718  1.00 20.59 ?  489  TRP A C   1 
ATOM   3690  O  O   . TRP A  1 465 ? 20.068  54.412  30.635  1.00 20.86 ?  489  TRP A O   1 
ATOM   3691  C  CB  . TRP A  1 465 ? 21.943  55.095  28.414  1.00 19.91 ?  489  TRP A CB  1 
ATOM   3692  C  CG  . TRP A  1 465 ? 20.874  55.746  27.570  1.00 19.60 ?  489  TRP A CG  1 
ATOM   3693  C  CD1 . TRP A  1 465 ? 19.769  56.424  28.020  1.00 19.54 ?  489  TRP A CD1 1 
ATOM   3694  C  CD2 . TRP A  1 465 ? 20.842  55.839  26.138  1.00 18.78 ?  489  TRP A CD2 1 
ATOM   3695  N  NE1 . TRP A  1 465 ? 19.045  56.912  26.956  1.00 19.33 ?  489  TRP A NE1 1 
ATOM   3696  C  CE2 . TRP A  1 465 ? 19.679  56.568  25.791  1.00 19.16 ?  489  TRP A CE2 1 
ATOM   3697  C  CE3 . TRP A  1 465 ? 21.680  55.376  25.114  1.00 18.36 ?  489  TRP A CE3 1 
ATOM   3698  C  CZ2 . TRP A  1 465 ? 19.336  56.846  24.461  1.00 18.70 ?  489  TRP A CZ2 1 
ATOM   3699  C  CZ3 . TRP A  1 465 ? 21.338  55.646  23.795  1.00 17.74 ?  489  TRP A CZ3 1 
ATOM   3700  C  CH2 . TRP A  1 465 ? 20.172  56.372  23.479  1.00 19.50 ?  489  TRP A CH2 1 
ATOM   3701  N  N   . THR A  1 466 ? 19.464  52.681  29.332  1.00 20.98 ?  490  THR A N   1 
ATOM   3702  C  CA  . THR A  1 466 ? 18.125  52.545  29.909  1.00 21.37 ?  490  THR A CA  1 
ATOM   3703  C  C   . THR A  1 466 ? 17.952  51.261  30.730  1.00 21.51 ?  490  THR A C   1 
ATOM   3704  O  O   . THR A  1 466 ? 18.266  51.241  31.922  1.00 21.56 ?  490  THR A O   1 
ATOM   3705  C  CB  . THR A  1 466 ? 17.039  52.630  28.819  1.00 21.43 ?  490  THR A CB  1 
ATOM   3706  O  OG1 . THR A  1 466 ? 17.342  51.691  27.781  1.00 21.83 ?  490  THR A OG1 1 
ATOM   3707  C  CG2 . THR A  1 466 ? 16.990  54.032  28.218  1.00 21.21 ?  490  THR A CG2 1 
ATOM   3708  N  N   . TYR A  1 467 ? 17.462  50.199  30.087  1.00 21.71 ?  491  TYR A N   1 
ATOM   3709  C  CA  . TYR A  1 467 ? 17.111  48.948  30.766  1.00 21.84 ?  491  TYR A CA  1 
ATOM   3710  C  C   . TYR A  1 467 ? 18.311  48.131  31.219  1.00 22.05 ?  491  TYR A C   1 
ATOM   3711  O  O   . TYR A  1 467 ? 18.349  47.652  32.351  1.00 22.22 ?  491  TYR A O   1 
ATOM   3712  C  CB  . TYR A  1 467 ? 16.293  48.042  29.841  1.00 21.83 ?  491  TYR A CB  1 
ATOM   3713  C  CG  . TYR A  1 467 ? 14.863  48.438  29.604  1.00 21.83 ?  491  TYR A CG  1 
ATOM   3714  C  CD1 . TYR A  1 467 ? 13.831  47.943  30.404  1.00 21.41 ?  491  TYR A CD1 1 
ATOM   3715  C  CD2 . TYR A  1 467 ? 14.532  49.271  28.545  1.00 21.71 ?  491  TYR A CD2 1 
ATOM   3716  C  CE1 . TYR A  1 467 ? 12.501  48.298  30.159  1.00 21.86 ?  491  TYR A CE1 1 
ATOM   3717  C  CE2 . TYR A  1 467 ? 13.227  49.619  28.293  1.00 21.91 ?  491  TYR A CE2 1 
ATOM   3718  C  CZ  . TYR A  1 467 ? 12.212  49.140  29.098  1.00 22.14 ?  491  TYR A CZ  1 
ATOM   3719  O  OH  . TYR A  1 467 ? 10.918  49.517  28.812  1.00 23.30 ?  491  TYR A OH  1 
ATOM   3720  N  N   . THR A  1 468 ? 19.268  47.948  30.314  1.00 22.21 ?  492  THR A N   1 
ATOM   3721  C  CA  . THR A  1 468 ? 20.287  46.910  30.464  1.00 22.30 ?  492  THR A CA  1 
ATOM   3722  C  C   . THR A  1 468 ? 21.583  47.417  31.099  1.00 22.31 ?  492  THR A C   1 
ATOM   3723  O  O   . THR A  1 468 ? 22.115  46.788  32.013  1.00 22.35 ?  492  THR A O   1 
ATOM   3724  C  CB  . THR A  1 468 ? 20.550  46.222  29.106  1.00 22.30 ?  492  THR A CB  1 
ATOM   3725  O  OG1 . THR A  1 468 ? 19.306  45.738  28.588  1.00 22.34 ?  492  THR A OG1 1 
ATOM   3726  C  CG2 . THR A  1 468 ? 21.527  45.055  29.247  1.00 21.91 ?  492  THR A CG2 1 
ATOM   3727  N  N   . GLU A  1 469 ? 22.092  48.542  30.609  1.00 22.24 ?  493  GLU A N   1 
ATOM   3728  C  CA  . GLU A  1 469 ? 23.216  49.207  31.262  1.00 22.28 ?  493  GLU A CA  1 
ATOM   3729  C  C   . GLU A  1 469 ? 22.808  50.625  31.630  1.00 22.32 ?  493  GLU A C   1 
ATOM   3730  O  O   . GLU A  1 469 ? 21.834  51.158  31.090  1.00 22.19 ?  493  GLU A O   1 
ATOM   3731  C  CB  . GLU A  1 469 ? 24.470  49.228  30.371  1.00 22.44 ?  493  GLU A CB  1 
ATOM   3732  C  CG  . GLU A  1 469 ? 24.963  47.864  29.871  1.00 22.39 ?  493  GLU A CG  1 
ATOM   3733  C  CD  . GLU A  1 469 ? 25.600  46.988  30.951  1.00 23.10 ?  493  GLU A CD  1 
ATOM   3734  O  OE1 . GLU A  1 469 ? 25.619  47.366  32.142  1.00 22.65 ?  493  GLU A OE1 1 
ATOM   3735  O  OE2 . GLU A  1 469 ? 26.086  45.895  30.596  1.00 24.72 -1 493  GLU A OE2 1 
ATOM   3736  N  N   . GLY A  1 470 ? 23.553  51.227  32.551  1.00 22.30 ?  494  GLY A N   1 
ATOM   3737  C  CA  . GLY A  1 470 ? 23.314  52.602  32.950  1.00 22.52 ?  494  GLY A CA  1 
ATOM   3738  C  C   . GLY A  1 470 ? 22.157  52.746  33.913  1.00 22.65 ?  494  GLY A C   1 
ATOM   3739  O  O   . GLY A  1 470 ? 22.283  52.401  35.087  1.00 22.73 ?  494  GLY A O   1 
ATOM   3740  N  N   . TRP A  1 471 ? 21.029  53.244  33.410  1.00 22.75 ?  495  TRP A N   1 
ATOM   3741  C  CA  . TRP A  1 471 ? 19.901  53.628  34.269  1.00 23.03 ?  495  TRP A CA  1 
ATOM   3742  C  C   . TRP A  1 471 ? 19.368  52.509  35.163  1.00 22.79 ?  495  TRP A C   1 
ATOM   3743  O  O   . TRP A  1 471 ? 19.180  52.717  36.359  1.00 22.80 ?  495  TRP A O   1 
ATOM   3744  C  CB  . TRP A  1 471 ? 18.764  54.248  33.451  1.00 23.04 ?  495  TRP A CB  1 
ATOM   3745  C  CG  . TRP A  1 471 ? 17.816  55.070  34.280  1.00 23.72 ?  495  TRP A CG  1 
ATOM   3746  C  CD1 . TRP A  1 471 ? 16.505  54.789  34.549  1.00 24.02 ?  495  TRP A CD1 1 
ATOM   3747  C  CD2 . TRP A  1 471 ? 18.113  56.294  34.966  1.00 23.66 ?  495  TRP A CD2 1 
ATOM   3748  N  NE1 . TRP A  1 471 ? 15.966  55.768  35.349  1.00 24.06 ?  495  TRP A NE1 1 
ATOM   3749  C  CE2 . TRP A  1 471 ? 16.931  56.703  35.621  1.00 24.07 ?  495  TRP A CE2 1 
ATOM   3750  C  CE3 . TRP A  1 471 ? 19.261  57.087  35.088  1.00 23.70 ?  495  TRP A CE3 1 
ATOM   3751  C  CZ2 . TRP A  1 471 ? 16.862  57.874  36.383  1.00 23.90 ?  495  TRP A CZ2 1 
ATOM   3752  C  CZ3 . TRP A  1 471 ? 19.192  58.249  35.845  1.00 24.10 ?  495  TRP A CZ3 1 
ATOM   3753  C  CH2 . TRP A  1 471 ? 17.999  58.629  36.485  1.00 24.05 ?  495  TRP A CH2 1 
ATOM   3754  N  N   . GLY A  1 472 ? 19.140  51.335  34.577  1.00 22.69 ?  496  GLY A N   1 
ATOM   3755  C  CA  . GLY A  1 472 ? 18.633  50.166  35.302  1.00 22.74 ?  496  GLY A CA  1 
ATOM   3756  C  C   . GLY A  1 472 ? 19.514  49.706  36.458  1.00 22.91 ?  496  GLY A C   1 
ATOM   3757  O  O   . GLY A  1 472 ? 19.040  49.608  37.593  1.00 22.70 ?  496  GLY A O   1 
ATOM   3758  N  N   . PRO A  1 473 ? 20.800  49.404  36.174  1.00 23.06 ?  497  PRO A N   1 
ATOM   3759  C  CA  . PRO A  1 473 ? 21.763  49.060  37.228  1.00 23.27 ?  497  PRO A CA  1 
ATOM   3760  C  C   . PRO A  1 473 ? 22.002  50.177  38.248  1.00 23.38 ?  497  PRO A C   1 
ATOM   3761  O  O   . PRO A  1 473 ? 22.195  49.888  39.427  1.00 23.30 ?  497  PRO A O   1 
ATOM   3762  C  CB  . PRO A  1 473 ? 23.043  48.758  36.443  1.00 23.27 ?  497  PRO A CB  1 
ATOM   3763  C  CG  . PRO A  1 473 ? 22.544  48.271  35.128  1.00 23.27 ?  497  PRO A CG  1 
ATOM   3764  C  CD  . PRO A  1 473 ? 21.360  49.146  34.834  1.00 22.76 ?  497  PRO A CD  1 
ATOM   3765  N  N   . MET A  1 474 ? 21.983  51.434  37.806  1.00 23.61 ?  498  MET A N   1 
ATOM   3766  C  CA  . MET A  1 474 ? 22.096  52.558  38.743  1.00 23.87 ?  498  MET A CA  1 
ATOM   3767  C  C   . MET A  1 474 ? 20.876  52.664  39.664  1.00 23.87 ?  498  MET A C   1 
ATOM   3768  O  O   . MET A  1 474 ? 21.015  52.915  40.867  1.00 23.92 ?  498  MET A O   1 
ATOM   3769  C  CB  . MET A  1 474 ? 22.346  53.876  38.013  1.00 23.69 ?  498  MET A CB  1 
ATOM   3770  C  CG  . MET A  1 474 ? 23.794  54.059  37.573  1.00 24.59 ?  498  MET A CG  1 
ATOM   3771  S  SD  . MET A  1 474 ? 24.158  55.717  36.962  1.00 26.29 ?  498  MET A SD  1 
ATOM   3772  C  CE  . MET A  1 474 ? 23.180  55.743  35.487  1.00 25.89 ?  498  MET A CE  1 
ATOM   3773  N  N   . ASN A  1 475 ? 19.691  52.456  39.095  1.00 23.96 ?  499  ASN A N   1 
ATOM   3774  C  CA  . ASN A  1 475 ? 18.453  52.389  39.869  1.00 24.20 ?  499  ASN A CA  1 
ATOM   3775  C  C   . ASN A  1 475 ? 18.511  51.321  40.966  1.00 24.22 ?  499  ASN A C   1 
ATOM   3776  O  O   . ASN A  1 475 ? 18.126  51.584  42.104  1.00 24.51 ?  499  ASN A O   1 
ATOM   3777  C  CB  . ASN A  1 475 ? 17.253  52.155  38.944  1.00 24.23 ?  499  ASN A CB  1 
ATOM   3778  C  CG  . ASN A  1 475 ? 15.934  52.125  39.693  1.00 24.12 ?  499  ASN A CG  1 
ATOM   3779  O  OD1 . ASN A  1 475 ? 15.454  53.151  40.178  1.00 23.50 ?  499  ASN A OD1 1 
ATOM   3780  N  ND2 . ASN A  1 475 ? 15.337  50.944  39.781  1.00 23.46 ?  499  ASN A ND2 1 
ATOM   3781  N  N   . ARG A  1 476 ? 19.004  50.130  40.622  1.00 24.37 ?  500  ARG A N   1 
ATOM   3782  C  CA  . ARG A  1 476 ? 19.167  49.040  41.589  1.00 24.36 ?  500  ARG A CA  1 
ATOM   3783  C  C   . ARG A  1 476 ? 20.138  49.420  42.706  1.00 24.22 ?  500  ARG A C   1 
ATOM   3784  O  O   . ARG A  1 476 ? 19.848  49.209  43.891  1.00 24.20 ?  500  ARG A O   1 
ATOM   3785  C  CB  . ARG A  1 476 ? 19.630  47.746  40.900  1.00 24.34 ?  500  ARG A CB  1 
ATOM   3786  C  CG  . ARG A  1 476 ? 19.798  46.555  41.863  1.00 25.16 ?  500  ARG A CG  1 
ATOM   3787  C  CD  . ARG A  1 476 ? 20.501  45.354  41.212  1.00 25.73 ?  500  ARG A CD  1 
ATOM   3788  N  NE  . ARG A  1 476 ? 19.800  44.918  40.012  1.00 26.94 ?  500  ARG A NE  1 
ATOM   3789  C  CZ  . ARG A  1 476 ? 20.288  44.980  38.774  1.00 26.85 ?  500  ARG A CZ  1 
ATOM   3790  N  NH1 . ARG A  1 476 ? 21.516  45.429  38.542  1.00 26.14 ?  500  ARG A NH1 1 
ATOM   3791  N  NH2 . ARG A  1 476 ? 19.539  44.571  37.764  1.00 26.35 ?  500  ARG A NH2 1 
ATOM   3792  N  N   . ALA A  1 477 ? 21.286  49.974  42.324  1.00 24.04 ?  501  ALA A N   1 
ATOM   3793  C  CA  . ALA A  1 477 ? 22.269  50.450  43.297  1.00 24.22 ?  501  ALA A CA  1 
ATOM   3794  C  C   . ALA A  1 477 ? 21.642  51.472  44.249  1.00 24.13 ?  501  ALA A C   1 
ATOM   3795  O  O   . ALA A  1 477 ? 21.767  51.345  45.462  1.00 24.33 ?  501  ALA A O   1 
ATOM   3796  C  CB  . ALA A  1 477 ? 23.480  51.039  42.596  1.00 23.97 ?  501  ALA A CB  1 
ATOM   3797  N  N   . TYR A  1 478 ? 20.948  52.458  43.687  1.00 24.26 ?  502  TYR A N   1 
ATOM   3798  C  CA  . TYR A  1 478 ? 20.271  53.493  44.467  1.00 24.45 ?  502  TYR A CA  1 
ATOM   3799  C  C   . TYR A  1 478 ? 19.271  52.880  45.445  1.00 24.45 ?  502  TYR A C   1 
ATOM   3800  O  O   . TYR A  1 478 ? 19.255  53.239  46.626  1.00 24.52 ?  502  TYR A O   1 
ATOM   3801  C  CB  . TYR A  1 478 ? 19.582  54.505  43.536  1.00 24.48 ?  502  TYR A CB  1 
ATOM   3802  C  CG  . TYR A  1 478 ? 18.787  55.597  44.235  1.00 24.56 ?  502  TYR A CG  1 
ATOM   3803  C  CD1 . TYR A  1 478 ? 17.483  55.364  44.675  1.00 24.84 ?  502  TYR A CD1 1 
ATOM   3804  C  CD2 . TYR A  1 478 ? 19.330  56.868  44.432  1.00 24.89 ?  502  TYR A CD2 1 
ATOM   3805  C  CE1 . TYR A  1 478 ? 16.744  56.360  45.306  1.00 24.94 ?  502  TYR A CE1 1 
ATOM   3806  C  CE2 . TYR A  1 478 ? 18.595  57.878  45.060  1.00 24.95 ?  502  TYR A CE2 1 
ATOM   3807  C  CZ  . TYR A  1 478 ? 17.304  57.612  45.495  1.00 25.10 ?  502  TYR A CZ  1 
ATOM   3808  O  OH  . TYR A  1 478 ? 16.568  58.589  46.119  1.00 25.46 ?  502  TYR A OH  1 
ATOM   3809  N  N   . VAL A  1 479 ? 18.455  51.949  44.948  1.00 24.53 ?  503  VAL A N   1 
ATOM   3810  C  CA  . VAL A  1 479 ? 17.446  51.268  45.761  1.00 24.45 ?  503  VAL A CA  1 
ATOM   3811  C  C   . VAL A  1 479 ? 18.091  50.492  46.916  1.00 24.71 ?  503  VAL A C   1 
ATOM   3812  O  O   . VAL A  1 479 ? 17.634  50.575  48.062  1.00 24.57 ?  503  VAL A O   1 
ATOM   3813  C  CB  . VAL A  1 479 ? 16.569  50.309  44.900  1.00 24.51 ?  503  VAL A CB  1 
ATOM   3814  C  CG1 . VAL A  1 479 ? 15.715  49.403  45.779  1.00 24.20 ?  503  VAL A CG1 1 
ATOM   3815  C  CG2 . VAL A  1 479 ? 15.680  51.092  43.938  1.00 24.24 ?  503  VAL A CG2 1 
ATOM   3816  N  N   . GLU A  1 480 ? 19.149  49.745  46.605  1.00 24.73 ?  504  GLU A N   1 
ATOM   3817  C  CA  . GLU A  1 480 ? 19.807  48.891  47.591  1.00 24.96 ?  504  GLU A CA  1 
ATOM   3818  C  C   . GLU A  1 480 ? 20.594  49.694  48.618  1.00 25.04 ?  504  GLU A C   1 
ATOM   3819  O  O   . GLU A  1 480 ? 20.666  49.305  49.784  1.00 25.07 ?  504  GLU A O   1 
ATOM   3820  C  CB  . GLU A  1 480 ? 20.693  47.843  46.914  1.00 24.91 ?  504  GLU A CB  1 
ATOM   3821  C  CG  . GLU A  1 480 ? 19.904  46.777  46.164  1.00 25.39 ?  504  GLU A CG  1 
ATOM   3822  C  CD  . GLU A  1 480 ? 20.767  45.665  45.596  1.00 26.32 ?  504  GLU A CD  1 
ATOM   3823  O  OE1 . GLU A  1 480 ? 22.009  45.716  45.734  1.00 27.09 ?  504  GLU A OE1 1 
ATOM   3824  O  OE2 . GLU A  1 480 ? 20.194  44.725  45.009  1.00 26.88 -1 504  GLU A OE2 1 
ATOM   3825  N  N   . ILE A  1 481 ? 21.172  50.811  48.180  1.00 25.25 ?  505  ILE A N   1 
ATOM   3826  C  CA  . ILE A  1 481 ? 21.845  51.748  49.079  1.00 25.43 ?  505  ILE A CA  1 
ATOM   3827  C  C   . ILE A  1 481 ? 20.848  52.342  50.079  1.00 25.72 ?  505  ILE A C   1 
ATOM   3828  O  O   . ILE A  1 481 ? 21.118  52.381  51.280  1.00 25.98 ?  505  ILE A O   1 
ATOM   3829  C  CB  . ILE A  1 481 ? 22.587  52.868  48.295  1.00 25.45 ?  505  ILE A CB  1 
ATOM   3830  C  CG1 . ILE A  1 481 ? 23.847  52.302  47.622  1.00 25.25 ?  505  ILE A CG1 1 
ATOM   3831  C  CG2 . ILE A  1 481 ? 22.949  54.039  49.213  1.00 25.39 ?  505  ILE A CG2 1 
ATOM   3832  C  CD1 . ILE A  1 481 ? 24.385  53.145  46.470  1.00 24.40 ?  505  ILE A CD1 1 
ATOM   3833  N  N   . GLN A  1 482 ? 19.693  52.779  49.578  1.00 25.80 ?  506  GLN A N   1 
ATOM   3834  C  CA  . GLN A  1 482 ? 18.642  53.352  50.417  1.00 26.02 ?  506  GLN A CA  1 
ATOM   3835  C  C   . GLN A  1 482 ? 18.110  52.334  51.414  1.00 26.19 ?  506  GLN A C   1 
ATOM   3836  O  O   . GLN A  1 482 ? 17.872  52.653  52.583  1.00 26.08 ?  506  GLN A O   1 
ATOM   3837  C  CB  . GLN A  1 482 ? 17.494  53.885  49.555  1.00 25.86 ?  506  GLN A CB  1 
ATOM   3838  C  CG  . GLN A  1 482 ? 17.844  55.115  48.714  1.00 25.67 ?  506  GLN A CG  1 
ATOM   3839  C  CD  . GLN A  1 482 ? 17.703  56.425  49.473  1.00 25.81 ?  506  GLN A CD  1 
ATOM   3840  O  OE1 . GLN A  1 482 ? 17.646  56.447  50.700  1.00 25.08 ?  506  GLN A OE1 1 
ATOM   3841  N  NE2 . GLN A  1 482 ? 17.651  57.529  48.736  1.00 26.42 ?  506  GLN A NE2 1 
ATOM   3842  N  N   . ASP A  1 483 ? 17.937  51.106  50.938  1.00 26.49 ?  507  ASP A N   1 
ATOM   3843  C  CA  . ASP A  1 483 ? 17.406  50.016  51.741  1.00 26.83 ?  507  ASP A CA  1 
ATOM   3844  C  C   . ASP A  1 483 ? 18.338  49.669  52.902  1.00 27.37 ?  507  ASP A C   1 
ATOM   3845  O  O   . ASP A  1 483 ? 17.896  49.582  54.049  1.00 27.24 ?  507  ASP A O   1 
ATOM   3846  C  CB  . ASP A  1 483 ? 17.139  48.798  50.851  1.00 26.60 ?  507  ASP A CB  1 
ATOM   3847  C  CG  . ASP A  1 483 ? 16.448  47.670  51.589  1.00 26.22 ?  507  ASP A CG  1 
ATOM   3848  O  OD1 . ASP A  1 483 ? 17.124  46.986  52.385  1.00 25.41 ?  507  ASP A OD1 1 
ATOM   3849  O  OD2 . ASP A  1 483 ? 15.239  47.453  51.356  1.00 24.86 -1 507  ASP A OD2 1 
ATOM   3850  N  N   . GLU A  1 484 ? 19.624  49.480  52.604  1.00 28.15 ?  508  GLU A N   1 
ATOM   3851  C  CA  . GLU A  1 484 ? 20.618  49.180  53.639  1.00 28.74 ?  508  GLU A CA  1 
ATOM   3852  C  C   . GLU A  1 484 ? 20.775  50.342  54.624  1.00 29.15 ?  508  GLU A C   1 
ATOM   3853  O  O   . GLU A  1 484 ? 20.945  50.123  55.826  1.00 29.08 ?  508  GLU A O   1 
ATOM   3854  C  CB  . GLU A  1 484 ? 21.968  48.822  53.013  1.00 28.72 ?  508  GLU A CB  1 
ATOM   3855  C  CG  . GLU A  1 484 ? 23.003  48.280  54.003  1.00 29.01 ?  508  GLU A CG  1 
ATOM   3856  C  CD  . GLU A  1 484 ? 24.309  47.869  53.338  1.00 30.21 ?  508  GLU A CD  1 
ATOM   3857  O  OE1 . GLU A  1 484 ? 24.325  47.673  52.104  1.00 30.40 ?  508  GLU A OE1 1 
ATOM   3858  O  OE2 . GLU A  1 484 ? 25.327  47.743  54.052  1.00 30.26 -1 508  GLU A OE2 1 
ATOM   3859  N  N   . TYR A  1 485 ? 20.714  51.567  54.106  1.00 29.72 ?  509  TYR A N   1 
ATOM   3860  C  CA  . TYR A  1 485 ? 20.798  52.771  54.933  1.00 30.58 ?  509  TYR A CA  1 
ATOM   3861  C  C   . TYR A  1 485 ? 19.686  52.793  55.977  1.00 30.72 ?  509  TYR A C   1 
ATOM   3862  O  O   . TYR A  1 485 ? 19.943  53.035  57.158  1.00 30.83 ?  509  TYR A O   1 
ATOM   3863  C  CB  . TYR A  1 485 ? 20.747  54.028  54.058  1.00 30.83 ?  509  TYR A CB  1 
ATOM   3864  C  CG  . TYR A  1 485 ? 20.885  55.337  54.809  1.00 31.92 ?  509  TYR A CG  1 
ATOM   3865  C  CD1 . TYR A  1 485 ? 21.991  55.586  55.624  1.00 33.32 ?  509  TYR A CD1 1 
ATOM   3866  C  CD2 . TYR A  1 485 ? 19.919  56.336  54.685  1.00 33.55 ?  509  TYR A CD2 1 
ATOM   3867  C  CE1 . TYR A  1 485 ? 22.125  56.790  56.311  1.00 34.61 ?  509  TYR A CE1 1 
ATOM   3868  C  CE2 . TYR A  1 485 ? 20.045  57.550  55.365  1.00 34.88 ?  509  TYR A CE2 1 
ATOM   3869  C  CZ  . TYR A  1 485 ? 21.148  57.767  56.176  1.00 35.37 ?  509  TYR A CZ  1 
ATOM   3870  O  OH  . TYR A  1 485 ? 21.275  58.959  56.850  1.00 36.99 ?  509  TYR A OH  1 
ATOM   3871  N  N   . THR A  1 486 ? 18.460  52.518  55.530  1.00 30.98 ?  510  THR A N   1 
ATOM   3872  C  CA  . THR A  1 486 ? 17.292  52.462  56.400  1.00 31.06 ?  510  THR A CA  1 
ATOM   3873  C  C   . THR A  1 486 ? 17.399  51.312  57.405  1.00 31.46 ?  510  THR A C   1 
ATOM   3874  O  O   . THR A  1 486 ? 17.153  51.516  58.594  1.00 31.42 ?  510  THR A O   1 
ATOM   3875  C  CB  . THR A  1 486 ? 15.971  52.374  55.586  1.00 31.12 ?  510  THR A CB  1 
ATOM   3876  O  OG1 . THR A  1 486 ? 15.848  53.530  54.747  1.00 30.49 ?  510  THR A OG1 1 
ATOM   3877  C  CG2 . THR A  1 486 ? 14.756  52.303  56.515  1.00 30.76 ?  510  THR A CG2 1 
ATOM   3878  N  N   . LYS A  1 487 ? 17.775  50.121  56.932  1.00 31.78 ?  511  LYS A N   1 
ATOM   3879  C  CA  . LYS A  1 487 ? 17.951  48.955  57.812  1.00 32.40 ?  511  LYS A CA  1 
ATOM   3880  C  C   . LYS A  1 487 ? 18.984  49.207  58.913  1.00 32.96 ?  511  LYS A C   1 
ATOM   3881  O  O   . LYS A  1 487 ? 18.773  48.822  60.064  1.00 32.97 ?  511  LYS A O   1 
ATOM   3882  C  CB  . LYS A  1 487 ? 18.334  47.689  57.028  1.00 32.06 ?  511  LYS A CB  1 
ATOM   3883  C  CG  . LYS A  1 487 ? 17.228  47.089  56.171  1.00 31.97 ?  511  LYS A CG  1 
ATOM   3884  C  CD  . LYS A  1 487 ? 17.282  45.562  56.202  1.00 31.58 ?  511  LYS A CD  1 
ATOM   3885  C  CE  . LYS A  1 487 ? 17.085  44.919  54.827  1.00 31.13 ?  511  LYS A CE  1 
ATOM   3886  N  NZ  . LYS A  1 487 ? 15.811  45.270  54.128  1.00 29.24 ?  511  LYS A NZ  1 
ATOM   3887  N  N   . MET A  1 488 ? 20.094  49.849  58.550  1.00 33.75 ?  512  MET A N   1 
ATOM   3888  C  CA  . MET A  1 488 ? 21.150  50.181  59.507  1.00 34.77 ?  512  MET A CA  1 
ATOM   3889  C  C   . MET A  1 488 ? 20.726  51.279  60.487  1.00 35.48 ?  512  MET A C   1 
ATOM   3890  O  O   . MET A  1 488 ? 21.117  51.253  61.655  1.00 35.51 ?  512  MET A O   1 
ATOM   3891  C  CB  . MET A  1 488 ? 22.449  50.561  58.788  1.00 34.46 ?  512  MET A CB  1 
ATOM   3892  C  CG  . MET A  1 488 ? 23.145  49.377  58.117  1.00 34.58 ?  512  MET A CG  1 
ATOM   3893  S  SD  . MET A  1 488 ? 24.701  49.785  57.299  1.00 34.03 ?  512  MET A SD  1 
ATOM   3894  C  CE  . MET A  1 488 ? 25.804  49.949  58.705  1.00 33.52 ?  512  MET A CE  1 
ATOM   3895  N  N   . GLN A  1 489 ? 19.924  52.230  60.009  1.00 36.51 ?  513  GLN A N   1 
ATOM   3896  C  CA  . GLN A  1 489 ? 19.369  53.282  60.866  1.00 37.57 ?  513  GLN A CA  1 
ATOM   3897  C  C   . GLN A  1 489 ? 18.521  52.712  61.997  1.00 37.93 ?  513  GLN A C   1 
ATOM   3898  O  O   . GLN A  1 489 ? 18.685  53.097  63.153  1.00 38.09 ?  513  GLN A O   1 
ATOM   3899  C  CB  . GLN A  1 489 ? 18.526  54.266  60.056  1.00 37.70 ?  513  GLN A CB  1 
ATOM   3900  C  CG  . GLN A  1 489 ? 19.298  55.411  59.440  1.00 38.81 ?  513  GLN A CG  1 
ATOM   3901  C  CD  . GLN A  1 489 ? 18.379  56.408  58.758  1.00 40.80 ?  513  GLN A CD  1 
ATOM   3902  O  OE1 . GLN A  1 489 ? 18.229  56.394  57.535  1.00 41.59 ?  513  GLN A OE1 1 
ATOM   3903  N  NE2 . GLN A  1 489 ? 17.742  57.269  59.550  1.00 41.00 ?  513  GLN A NE2 1 
ATOM   3904  N  N   . GLU A  1 490 ? 17.617  51.795  61.660  1.00 38.49 ?  514  GLU A N   1 
ATOM   3905  C  CA  . GLU A  1 490 ? 16.721  51.216  62.661  1.00 39.14 ?  514  GLU A CA  1 
ATOM   3906  C  C   . GLU A  1 490 ? 17.396  50.148  63.521  1.00 39.50 ?  514  GLU A C   1 
ATOM   3907  O  O   . GLU A  1 490 ? 16.939  49.860  64.626  1.00 39.59 ?  514  GLU A O   1 
ATOM   3908  C  CB  . GLU A  1 490 ? 15.408  50.715  62.035  1.00 39.20 ?  514  GLU A CB  1 
ATOM   3909  C  CG  . GLU A  1 490 ? 15.555  49.818  60.825  1.00 39.35 ?  514  GLU A CG  1 
ATOM   3910  C  CD  . GLU A  1 490 ? 14.298  49.770  59.965  1.00 39.19 ?  514  GLU A CD  1 
ATOM   3911  O  OE1 . GLU A  1 490 ? 13.650  50.819  59.755  1.00 39.79 ?  514  GLU A OE1 1 
ATOM   3912  O  OE2 . GLU A  1 490 ? 13.961  48.676  59.484  1.00 39.01 -1 514  GLU A OE2 1 
ATOM   3913  N  N   . LEU A  1 491 ? 18.489  49.576  63.021  1.00 40.02 ?  515  LEU A N   1 
ATOM   3914  C  CA  . LEU A  1 491 ? 19.290  48.655  63.818  1.00 40.57 ?  515  LEU A CA  1 
ATOM   3915  C  C   . LEU A  1 491 ? 20.074  49.398  64.906  1.00 40.88 ?  515  LEU A C   1 
ATOM   3916  O  O   . LEU A  1 491 ? 20.185  48.913  66.036  1.00 40.81 ?  515  LEU A O   1 
ATOM   3917  C  CB  . LEU A  1 491 ? 20.223  47.820  62.935  1.00 40.61 ?  515  LEU A CB  1 
ATOM   3918  C  CG  . LEU A  1 491 ? 21.076  46.736  63.605  1.00 41.13 ?  515  LEU A CG  1 
ATOM   3919  C  CD1 . LEU A  1 491 ? 20.231  45.764  64.426  1.00 41.40 ?  515  LEU A CD1 1 
ATOM   3920  C  CD2 . LEU A  1 491 ? 21.898  45.986  62.562  1.00 41.70 ?  515  LEU A CD2 1 
ATOM   3921  N  N   . SER A  1 492 ? 20.603  50.572  64.570  1.00 41.29 ?  516  SER A N   1 
ATOM   3922  C  CA  . SER A  1 492 ? 21.290  51.402  65.560  1.00 41.97 ?  516  SER A CA  1 
ATOM   3923  C  C   . SER A  1 492 ? 20.291  52.022  66.542  1.00 42.39 ?  516  SER A C   1 
ATOM   3924  O  O   . SER A  1 492 ? 20.622  52.247  67.708  1.00 42.36 ?  516  SER A O   1 
ATOM   3925  C  CB  . SER A  1 492 ? 22.156  52.478  64.893  1.00 41.80 ?  516  SER A CB  1 
ATOM   3926  O  OG  . SER A  1 492 ? 21.368  53.506  64.331  1.00 42.04 ?  516  SER A OG  1 
ATOM   3927  N  N   . ALA A  1 493 ? 19.071  52.280  66.065  1.00 42.98 ?  517  ALA A N   1 
ATOM   3928  C  CA  . ALA A  1 493 ? 17.974  52.729  66.927  1.00 43.67 ?  517  ALA A CA  1 
ATOM   3929  C  C   . ALA A  1 493 ? 17.609  51.657  67.955  1.00 44.11 ?  517  ALA A C   1 
ATOM   3930  O  O   . ALA A  1 493 ? 17.404  51.963  69.129  1.00 44.27 ?  517  ALA A O   1 
ATOM   3931  C  CB  . ALA A  1 493 ? 16.754  53.114  66.097  1.00 43.56 ?  517  ALA A CB  1 
ATOM   3932  N  N   . LEU A  1 494 ? 17.541  50.404  67.505  1.00 44.65 ?  518  LEU A N   1 
ATOM   3933  C  CA  . LEU A  1 494 ? 17.269  49.267  68.383  1.00 45.35 ?  518  LEU A CA  1 
ATOM   3934  C  C   . LEU A  1 494 ? 18.395  49.063  69.402  1.00 45.93 ?  518  LEU A C   1 
ATOM   3935  O  O   . LEU A  1 494 ? 18.135  48.776  70.572  1.00 45.97 ?  518  LEU A O   1 
ATOM   3936  C  CB  . LEU A  1 494 ? 17.049  47.991  67.559  1.00 45.23 ?  518  LEU A CB  1 
ATOM   3937  C  CG  . LEU A  1 494 ? 16.630  46.702  68.281  1.00 45.23 ?  518  LEU A CG  1 
ATOM   3938  C  CD1 . LEU A  1 494 ? 15.202  46.787  68.808  1.00 45.09 ?  518  LEU A CD1 1 
ATOM   3939  C  CD2 . LEU A  1 494 ? 16.786  45.496  67.367  1.00 44.73 ?  518  LEU A CD2 1 
ATOM   3940  N  N   . GLN A  1 495 ? 19.636  49.221  68.946  1.00 46.65 ?  519  GLN A N   1 
ATOM   3941  C  CA  . GLN A  1 495 ? 20.816  49.101  69.799  1.00 47.44 ?  519  GLN A CA  1 
ATOM   3942  C  C   . GLN A  1 495 ? 20.840  50.186  70.881  1.00 47.86 ?  519  GLN A C   1 
ATOM   3943  O  O   . GLN A  1 495 ? 21.225  49.923  72.024  1.00 47.82 ?  519  GLN A O   1 
ATOM   3944  C  CB  . GLN A  1 495 ? 22.091  49.159  68.949  1.00 47.50 ?  519  GLN A CB  1 
ATOM   3945  C  CG  . GLN A  1 495 ? 23.381  48.912  69.723  1.00 48.25 ?  519  GLN A CG  1 
ATOM   3946  C  CD  . GLN A  1 495 ? 24.597  48.769  68.826  1.00 49.44 ?  519  GLN A CD  1 
ATOM   3947  O  OE1 . GLN A  1 495 ? 25.640  49.374  69.079  1.00 49.87 ?  519  GLN A OE1 1 
ATOM   3948  N  NE2 . GLN A  1 495 ? 24.471  47.964  67.772  1.00 49.77 ?  519  GLN A NE2 1 
ATOM   3949  N  N   . ALA A  1 496 ? 20.425  51.396  70.507  1.00 48.40 ?  520  ALA A N   1 
ATOM   3950  C  CA  . ALA A  1 496 ? 20.318  52.518  71.436  1.00 48.97 ?  520  ALA A CA  1 
ATOM   3951  C  C   . ALA A  1 496 ? 19.288  52.242  72.531  1.00 49.44 ?  520  ALA A C   1 
ATOM   3952  O  O   . ALA A  1 496 ? 19.493  52.613  73.687  1.00 49.43 ?  520  ALA A O   1 
ATOM   3953  C  CB  . ALA A  1 496 ? 19.975  53.799  70.686  1.00 48.86 ?  520  ALA A CB  1 
ATOM   3954  N  N   . ARG A  1 497 ? 18.189  51.587  72.156  1.00 50.09 ?  521  ARG A N   1 
ATOM   3955  C  CA  . ARG A  1 497 ? 17.148  51.184  73.105  1.00 50.76 ?  521  ARG A CA  1 
ATOM   3956  C  C   . ARG A  1 497 ? 17.640  50.100  74.067  1.00 51.20 ?  521  ARG A C   1 
ATOM   3957  O  O   . ARG A  1 497 ? 17.226  50.062  75.228  1.00 51.29 ?  521  ARG A O   1 
ATOM   3958  C  CB  . ARG A  1 497 ? 15.888  50.712  72.373  1.00 50.65 ?  521  ARG A CB  1 
ATOM   3959  C  CG  . ARG A  1 497 ? 15.142  51.819  71.637  1.00 51.18 ?  521  ARG A CG  1 
ATOM   3960  C  CD  . ARG A  1 497 ? 13.669  51.478  71.443  1.00 51.69 ?  521  ARG A CD  1 
ATOM   3961  N  NE  . ARG A  1 497 ? 13.458  50.437  70.441  1.00 52.40 ?  521  ARG A NE  1 
ATOM   3962  C  CZ  . ARG A  1 497 ? 12.350  49.706  70.328  1.00 52.50 ?  521  ARG A CZ  1 
ATOM   3963  N  NH1 . ARG A  1 497 ? 11.334  49.880  71.164  1.00 52.64 ?  521  ARG A NH1 1 
ATOM   3964  N  NH2 . ARG A  1 497 ? 12.263  48.788  69.377  1.00 52.68 ?  521  ARG A NH2 1 
ATOM   3965  N  N   . VAL A  1 498 ? 18.519  49.228  73.575  1.00 51.79 ?  522  VAL A N   1 
ATOM   3966  C  CA  . VAL A  1 498 ? 19.154  48.198  74.400  1.00 52.42 ?  522  VAL A CA  1 
ATOM   3967  C  C   . VAL A  1 498 ? 20.137  48.843  75.382  1.00 52.93 ?  522  VAL A C   1 
ATOM   3968  O  O   . VAL A  1 498 ? 20.205  48.449  76.549  1.00 52.99 ?  522  VAL A O   1 
ATOM   3969  C  CB  . VAL A  1 498 ? 19.856  47.113  73.533  1.00 52.35 ?  522  VAL A CB  1 
ATOM   3970  C  CG1 . VAL A  1 498 ? 20.624  46.120  74.400  1.00 52.27 ?  522  VAL A CG1 1 
ATOM   3971  C  CG2 . VAL A  1 498 ? 18.839  46.373  72.674  1.00 52.26 ?  522  VAL A CG2 1 
ATOM   3972  N  N   . ASN A  1 499 ? 20.879  49.842  74.902  1.00 53.61 ?  523  ASN A N   1 
ATOM   3973  C  CA  . ASN A  1 499 ? 21.770  50.641  75.744  1.00 54.29 ?  523  ASN A CA  1 
ATOM   3974  C  C   . ASN A  1 499 ? 21.033  51.288  76.918  1.00 54.76 ?  523  ASN A C   1 
ATOM   3975  O  O   . ASN A  1 499 ? 21.566  51.360  78.027  1.00 54.77 ?  523  ASN A O   1 
ATOM   3976  C  CB  . ASN A  1 499 ? 22.478  51.724  74.919  1.00 54.30 ?  523  ASN A CB  1 
ATOM   3977  C  CG  . ASN A  1 499 ? 23.506  51.158  73.949  1.00 54.61 ?  523  ASN A CG  1 
ATOM   3978  O  OD1 . ASN A  1 499 ? 23.942  50.011  74.072  1.00 55.20 ?  523  ASN A OD1 1 
ATOM   3979  N  ND2 . ASN A  1 499 ? 23.905  51.974  72.977  1.00 54.52 ?  523  ASN A ND2 1 
ATOM   3980  N  N   . LYS A  1 500 ? 19.810  51.755  76.661  1.00 55.38 ?  524  LYS A N   1 
ATOM   3981  C  CA  . LYS A  1 500 ? 18.960  52.358  77.691  1.00 56.04 ?  524  LYS A CA  1 
ATOM   3982  C  C   . LYS A  1 500 ? 18.487  51.329  78.715  1.00 56.30 ?  524  LYS A C   1 
ATOM   3983  O  O   . LYS A  1 500 ? 18.410  51.627  79.909  1.00 56.34 ?  524  LYS A O   1 
ATOM   3984  C  CB  . LYS A  1 500 ? 17.753  53.065  77.064  1.00 56.15 ?  524  LYS A CB  1 
ATOM   3985  C  CG  . LYS A  1 500 ? 18.079  54.395  76.398  1.00 56.64 ?  524  LYS A CG  1 
ATOM   3986  C  CD  . LYS A  1 500 ? 16.835  55.013  75.768  1.00 57.40 ?  524  LYS A CD  1 
ATOM   3987  C  CE  . LYS A  1 500 ? 17.142  56.356  75.107  1.00 57.91 ?  524  LYS A CE  1 
ATOM   3988  N  NZ  . LYS A  1 500 ? 17.373  57.446  76.099  1.00 57.93 ?  524  LYS A NZ  1 
ATOM   3989  N  N   . LEU A  1 501 ? 18.178  50.123  78.240  1.00 56.62 ?  525  LEU A N   1 
ATOM   3990  C  CA  . LEU A  1 501 ? 17.766  49.019  79.110  1.00 57.00 ?  525  LEU A CA  1 
ATOM   3991  C  C   . LEU A  1 501 ? 18.921  48.471  79.953  1.00 57.32 ?  525  LEU A C   1 
ATOM   3992  O  O   . LEU A  1 501 ? 18.698  47.744  80.925  1.00 57.43 ?  525  LEU A O   1 
ATOM   3993  C  CB  . LEU A  1 501 ? 17.126  47.893  78.291  1.00 56.94 ?  525  LEU A CB  1 
ATOM   3994  C  CG  . LEU A  1 501 ? 15.714  48.118  77.741  1.00 56.89 ?  525  LEU A CG  1 
ATOM   3995  C  CD1 . LEU A  1 501 ? 15.407  47.116  76.638  1.00 56.72 ?  525  LEU A CD1 1 
ATOM   3996  C  CD2 . LEU A  1 501 ? 14.661  48.047  78.846  1.00 56.78 ?  525  LEU A CD2 1 
ATOM   3997  N  N   . GLU A  1 502 ? 20.148  48.825  79.574  1.00 57.68 ?  526  GLU A N   1 
ATOM   3998  C  CA  . GLU A  1 502 ? 21.345  48.438  80.319  1.00 57.98 ?  526  GLU A CA  1 
ATOM   3999  C  C   . GLU A  1 502 ? 21.735  49.492  81.355  1.00 58.30 ?  526  GLU A C   1 
ATOM   4000  O  O   . GLU A  1 502 ? 22.559  49.230  82.235  1.00 58.28 ?  526  GLU A O   1 
ATOM   4001  C  CB  . GLU A  1 502 ? 22.513  48.173  79.366  1.00 57.88 ?  526  GLU A CB  1 
ATOM   4002  C  CG  . GLU A  1 502 ? 22.380  46.885  78.568  1.00 57.68 ?  526  GLU A CG  1 
ATOM   4003  C  CD  . GLU A  1 502 ? 23.519  46.670  77.583  1.00 57.46 ?  526  GLU A CD  1 
ATOM   4004  O  OE1 . GLU A  1 502 ? 24.206  47.649  77.216  1.00 56.93 ?  526  GLU A OE1 1 
ATOM   4005  O  OE2 . GLU A  1 502 ? 23.722  45.510  77.172  1.00 57.03 ?  526  GLU A OE2 1 
ATOM   4006  N  N   . GLY A  1 503 ? 21.139  50.680  81.241  1.00 58.70 ?  527  GLY A N   1 
ATOM   4007  C  CA  . GLY A  1 503 ? 21.324  51.754  82.220  1.00 59.24 ?  527  GLY A CA  1 
ATOM   4008  C  C   . GLY A  1 503 ? 20.765  51.386  83.585  1.00 59.58 ?  527  GLY A C   1 
ATOM   4009  O  O   . GLY A  1 503 ? 21.274  51.841  84.612  1.00 59.66 ?  527  GLY A O   1 
ATOM   4010  N  N   . LYS A  1 504 ? 19.712  50.565  83.574  1.00 59.89 ?  528  LYS A N   1 
ATOM   4011  C  CA  . LYS A  1 504 ? 19.092  49.965  84.770  1.00 60.14 ?  528  LYS A CA  1 
ATOM   4012  C  C   . LYS A  1 504 ? 18.888  50.915  85.953  1.00 60.20 ?  528  LYS A C   1 
ATOM   4013  O  O   . LYS A  1 504 ? 18.213  50.577  86.928  1.00 60.26 ?  528  LYS A O   1 
ATOM   4014  C  CB  . LYS A  1 504 ? 19.849  48.696  85.208  1.00 60.17 ?  528  LYS A CB  1 
ATOM   4015  C  CG  . LYS A  1 504 ? 21.096  48.936  86.057  1.00 60.47 ?  528  LYS A CG  1 
ATOM   4016  C  CD  . LYS A  1 504 ? 21.421  47.726  86.919  1.00 60.90 ?  528  LYS A CD  1 
ATOM   4017  C  CE  . LYS A  1 504 ? 22.435  48.074  88.002  1.00 61.35 ?  528  LYS A CE  1 
ATOM   4018  N  NZ  . LYS A  1 504 ? 22.644  46.948  88.957  1.00 61.45 ?  528  LYS A NZ  1 
ATOM   4019  N  N   . SER B  2 2   ? 41.144  75.613  38.841  1.00 42.85 ?  29   SER B N   1 
ATOM   4020  C  CA  . SER B  2 2   ? 40.166  74.560  39.246  1.00 42.81 ?  29   SER B CA  1 
ATOM   4021  C  C   . SER B  2 2   ? 38.745  75.117  39.344  1.00 42.48 ?  29   SER B C   1 
ATOM   4022  O  O   . SER B  2 2   ? 38.509  76.143  39.991  1.00 42.63 ?  29   SER B O   1 
ATOM   4023  C  CB  . SER B  2 2   ? 40.580  73.925  40.576  1.00 42.90 ?  29   SER B CB  1 
ATOM   4024  O  OG  . SER B  2 2   ? 39.742  72.828  40.898  1.00 43.64 ?  29   SER B OG  1 
ATOM   4025  N  N   . LEU B  2 3   ? 37.809  74.431  38.692  1.00 42.00 ?  30   LEU B N   1 
ATOM   4026  C  CA  . LEU B  2 3   ? 36.391  74.800  38.699  1.00 41.38 ?  30   LEU B CA  1 
ATOM   4027  C  C   . LEU B  2 3   ? 35.726  74.519  40.043  1.00 40.90 ?  30   LEU B C   1 
ATOM   4028  O  O   . LEU B  2 3   ? 35.892  73.438  40.611  1.00 40.83 ?  30   LEU B O   1 
ATOM   4029  C  CB  . LEU B  2 3   ? 35.648  74.040  37.592  1.00 41.51 ?  30   LEU B CB  1 
ATOM   4030  C  CG  . LEU B  2 3   ? 35.256  74.706  36.265  1.00 41.48 ?  30   LEU B CG  1 
ATOM   4031  C  CD1 . LEU B  2 3   ? 36.171  75.858  35.856  1.00 41.36 ?  30   LEU B CD1 1 
ATOM   4032  C  CD2 . LEU B  2 3   ? 35.178  73.655  35.164  1.00 40.94 ?  30   LEU B CD2 1 
ATOM   4033  N  N   . ALA B  2 4   ? 34.978  75.499  40.549  1.00 40.30 ?  31   ALA B N   1 
ATOM   4034  C  CA  . ALA B  2 4   ? 34.157  75.306  41.743  1.00 39.61 ?  31   ALA B CA  1 
ATOM   4035  C  C   . ALA B  2 4   ? 33.058  74.281  41.442  1.00 39.08 ?  31   ALA B C   1 
ATOM   4036  O  O   . ALA B  2 4   ? 32.479  74.304  40.351  1.00 38.83 ?  31   ALA B O   1 
ATOM   4037  C  CB  . ALA B  2 4   ? 33.551  76.624  42.195  1.00 39.71 ?  31   ALA B CB  1 
ATOM   4038  N  N   . PRO B  2 5   ? 32.775  73.377  42.404  1.00 38.47 ?  32   PRO B N   1 
ATOM   4039  C  CA  . PRO B  2 5   ? 31.826  72.283  42.178  1.00 37.97 ?  32   PRO B CA  1 
ATOM   4040  C  C   . PRO B  2 5   ? 30.386  72.743  41.941  1.00 37.39 ?  32   PRO B C   1 
ATOM   4041  O  O   . PRO B  2 5   ? 29.841  73.530  42.720  1.00 37.25 ?  32   PRO B O   1 
ATOM   4042  C  CB  . PRO B  2 5   ? 31.918  71.458  43.472  1.00 38.08 ?  32   PRO B CB  1 
ATOM   4043  C  CG  . PRO B  2 5   ? 33.227  71.844  44.086  1.00 38.25 ?  32   PRO B CG  1 
ATOM   4044  C  CD  . PRO B  2 5   ? 33.392  73.289  43.740  1.00 38.48 ?  32   PRO B CD  1 
ATOM   4045  N  N   . ILE B  2 6   ? 29.798  72.256  40.849  1.00 36.59 ?  33   ILE B N   1 
ATOM   4046  C  CA  . ILE B  2 6   ? 28.377  72.429  40.567  1.00 35.91 ?  33   ILE B CA  1 
ATOM   4047  C  C   . ILE B  2 6   ? 27.772  71.040  40.376  1.00 35.51 ?  33   ILE B C   1 
ATOM   4048  O  O   . ILE B  2 6   ? 28.258  70.257  39.558  1.00 35.36 ?  33   ILE B O   1 
ATOM   4049  C  CB  . ILE B  2 6   ? 28.135  73.278  39.290  1.00 35.91 ?  33   ILE B CB  1 
ATOM   4050  C  CG1 . ILE B  2 6   ? 28.865  74.625  39.378  1.00 35.85 ?  33   ILE B CG1 1 
ATOM   4051  C  CG2 . ILE B  2 6   ? 26.638  73.485  39.053  1.00 35.46 ?  33   ILE B CG2 1 
ATOM   4052  C  CD1 . ILE B  2 6   ? 29.037  75.325  38.036  1.00 35.83 ?  33   ILE B CD1 1 
ATOM   4053  N  N   . SER B  2 7   ? 26.719  70.738  41.131  1.00 34.93 ?  34   SER B N   1 
ATOM   4054  C  CA  . SER B  2 7   ? 26.052  69.437  41.046  1.00 34.45 ?  34   SER B CA  1 
ATOM   4055  C  C   . SER B  2 7   ? 25.387  69.216  39.683  1.00 34.10 ?  34   SER B C   1 
ATOM   4056  O  O   . SER B  2 7   ? 25.051  70.172  38.979  1.00 33.82 ?  34   SER B O   1 
ATOM   4057  C  CB  . SER B  2 7   ? 25.032  69.273  42.178  1.00 34.43 ?  34   SER B CB  1 
ATOM   4058  O  OG  . SER B  2 7   ? 23.875  70.057  41.945  1.00 34.47 ?  34   SER B OG  1 
ATOM   4059  N  N   . ALA B  2 8   ? 25.209  67.946  39.323  1.00 33.71 ?  35   ALA B N   1 
ATOM   4060  C  CA  . ALA B  2 8   ? 24.628  67.568  38.035  1.00 33.43 ?  35   ALA B CA  1 
ATOM   4061  C  C   . ALA B  2 8   ? 23.212  68.117  37.829  1.00 33.22 ?  35   ALA B C   1 
ATOM   4062  O  O   . ALA B  2 8   ? 22.896  68.613  36.745  1.00 32.94 ?  35   ALA B O   1 
ATOM   4063  C  CB  . ALA B  2 8   ? 24.646  66.062  37.870  1.00 33.46 ?  35   ALA B CB  1 
ATOM   4064  N  N   . LYS B  2 9   ? 22.372  68.030  38.864  1.00 33.10 ?  36   LYS B N   1 
ATOM   4065  C  CA  . LYS B  2 9   ? 21.011  68.582  38.802  1.00 33.14 ?  36   LYS B CA  1 
ATOM   4066  C  C   . LYS B  2 9   ? 21.021  70.093  38.545  1.00 32.76 ?  36   LYS B C   1 
ATOM   4067  O  O   . LYS B  2 9   ? 20.237  70.597  37.739  1.00 32.56 ?  36   LYS B O   1 
ATOM   4068  C  CB  . LYS B  2 9   ? 20.193  68.238  40.058  1.00 33.29 ?  36   LYS B CB  1 
ATOM   4069  C  CG  . LYS B  2 9   ? 20.756  68.749  41.385  1.00 34.37 ?  36   LYS B CG  1 
ATOM   4070  C  CD  . LYS B  2 9   ? 19.722  68.658  42.506  1.00 35.87 ?  36   LYS B CD  1 
ATOM   4071  C  CE  . LYS B  2 9   ? 18.830  69.897  42.568  1.00 37.24 ?  36   LYS B CE  1 
ATOM   4072  N  NZ  . LYS B  2 9   ? 19.563  71.103  43.068  1.00 37.68 ?  36   LYS B NZ  1 
ATOM   4073  N  N   . ASP B  2 10  ? 21.931  70.797  39.217  1.00 32.44 ?  37   ASP B N   1 
ATOM   4074  C  CA  . ASP B  2 10  ? 22.106  72.235  39.021  1.00 32.28 ?  37   ASP B CA  1 
ATOM   4075  C  C   . ASP B  2 10  ? 22.601  72.564  37.610  1.00 32.15 ?  37   ASP B C   1 
ATOM   4076  O  O   . ASP B  2 10  ? 22.182  73.564  37.023  1.00 31.89 ?  37   ASP B O   1 
ATOM   4077  C  CB  . ASP B  2 10  ? 23.043  72.813  40.088  1.00 32.26 ?  37   ASP B CB  1 
ATOM   4078  C  CG  . ASP B  2 10  ? 22.397  72.867  41.465  1.00 32.20 ?  37   ASP B CG  1 
ATOM   4079  O  OD1 . ASP B  2 10  ? 23.130  72.836  42.477  1.00 32.51 ?  37   ASP B OD1 1 
ATOM   4080  O  OD2 . ASP B  2 10  ? 21.153  72.938  41.540  1.00 32.14 ?  37   ASP B OD2 1 
ATOM   4081  N  N   . MET B  2 11  ? 23.475  71.710  37.074  1.00 32.07 ?  38   MET B N   1 
ATOM   4082  C  CA  . MET B  2 11  ? 23.930  71.816  35.682  1.00 32.22 ?  38   MET B CA  1 
ATOM   4083  C  C   . MET B  2 11  ? 22.777  71.657  34.683  1.00 32.11 ?  38   MET B C   1 
ATOM   4084  O  O   . MET B  2 11  ? 22.664  72.442  33.741  1.00 32.00 ?  38   MET B O   1 
ATOM   4085  C  CB  . MET B  2 11  ? 25.035  70.795  35.377  1.00 32.27 ?  38   MET B CB  1 
ATOM   4086  C  CG  . MET B  2 11  ? 26.395  71.093  36.012  1.00 32.85 ?  38   MET B CG  1 
ATOM   4087  S  SD  . MET B  2 11  ? 27.148  72.656  35.499  1.00 33.68 ?  38   MET B SD  1 
ATOM   4088  C  CE  . MET B  2 11  ? 27.368  72.418  33.733  1.00 33.02 ?  38   MET B CE  1 
ATOM   4089  N  N   . LEU B  2 12  ? 21.938  70.637  34.893  1.00 32.29 ?  39   LEU B N   1 
ATOM   4090  C  CA  . LEU B  2 12  ? 20.745  70.405  34.067  1.00 32.50 ?  39   LEU B CA  1 
ATOM   4091  C  C   . LEU B  2 12  ? 19.795  71.603  34.074  1.00 32.74 ?  39   LEU B C   1 
ATOM   4092  O  O   . LEU B  2 12  ? 19.343  72.054  33.018  1.00 32.72 ?  39   LEU B O   1 
ATOM   4093  C  CB  . LEU B  2 12  ? 19.976  69.157  34.526  1.00 32.32 ?  39   LEU B CB  1 
ATOM   4094  C  CG  . LEU B  2 12  ? 20.162  67.760  33.908  1.00 32.32 ?  39   LEU B CG  1 
ATOM   4095  C  CD1 . LEU B  2 12  ? 20.763  67.791  32.501  1.00 31.07 ?  39   LEU B CD1 1 
ATOM   4096  C  CD2 . LEU B  2 12  ? 20.956  66.847  34.827  1.00 31.35 ?  39   LEU B CD2 1 
ATOM   4097  N  N   . ASP B  2 13  ? 19.498  72.105  35.271  1.00 33.16 ?  40   ASP B N   1 
ATOM   4098  C  CA  . ASP B  2 13  ? 18.620  73.261  35.437  1.00 33.94 ?  40   ASP B CA  1 
ATOM   4099  C  C   . ASP B  2 13  ? 19.185  74.517  34.770  1.00 34.46 ?  40   ASP B C   1 
ATOM   4100  O  O   . ASP B  2 13  ? 18.431  75.311  34.207  1.00 34.37 ?  40   ASP B O   1 
ATOM   4101  C  CB  . ASP B  2 13  ? 18.324  73.508  36.921  1.00 33.76 ?  40   ASP B CB  1 
ATOM   4102  C  CG  . ASP B  2 13  ? 17.623  72.327  37.586  1.00 33.55 ?  40   ASP B CG  1 
ATOM   4103  O  OD1 . ASP B  2 13  ? 17.066  71.471  36.865  1.00 33.22 ?  40   ASP B OD1 1 
ATOM   4104  O  OD2 . ASP B  2 13  ? 17.631  72.253  38.831  1.00 33.00 ?  40   ASP B OD2 1 
ATOM   4105  N  N   . TYR B  2 14  ? 20.509  74.677  34.824  1.00 35.29 ?  41   TYR B N   1 
ATOM   4106  C  CA  . TYR B  2 14  ? 21.195  75.775  34.137  1.00 36.29 ?  41   TYR B CA  1 
ATOM   4107  C  C   . TYR B  2 14  ? 21.040  75.663  32.616  1.00 36.71 ?  41   TYR B C   1 
ATOM   4108  O  O   . TYR B  2 14  ? 20.701  76.644  31.949  1.00 36.67 ?  41   TYR B O   1 
ATOM   4109  C  CB  . TYR B  2 14  ? 22.677  75.832  34.535  1.00 36.45 ?  41   TYR B CB  1 
ATOM   4110  C  CG  . TYR B  2 14  ? 23.460  76.943  33.861  1.00 37.58 ?  41   TYR B CG  1 
ATOM   4111  C  CD1 . TYR B  2 14  ? 23.285  78.277  34.238  1.00 38.70 ?  41   TYR B CD1 1 
ATOM   4112  C  CD2 . TYR B  2 14  ? 24.376  76.660  32.848  1.00 38.30 ?  41   TYR B CD2 1 
ATOM   4113  C  CE1 . TYR B  2 14  ? 24.000  79.302  33.619  1.00 39.31 ?  41   TYR B CE1 1 
ATOM   4114  C  CE2 . TYR B  2 14  ? 25.097  77.674  32.224  1.00 39.29 ?  41   TYR B CE2 1 
ATOM   4115  C  CZ  . TYR B  2 14  ? 24.904  78.991  32.615  1.00 39.79 ?  41   TYR B CZ  1 
ATOM   4116  O  OH  . TYR B  2 14  ? 25.614  79.996  32.001  1.00 40.62 ?  41   TYR B OH  1 
ATOM   4117  N  N   . LEU B  2 15  ? 21.288  74.464  32.087  1.00 37.24 ?  42   LEU B N   1 
ATOM   4118  C  CA  . LEU B  2 15  ? 21.060  74.145  30.673  1.00 37.81 ?  42   LEU B CA  1 
ATOM   4119  C  C   . LEU B  2 15  ? 19.626  74.422  30.224  1.00 38.28 ?  42   LEU B C   1 
ATOM   4120  O  O   . LEU B  2 15  ? 19.404  74.957  29.137  1.00 37.98 ?  42   LEU B O   1 
ATOM   4121  C  CB  . LEU B  2 15  ? 21.401  72.677  30.405  1.00 37.67 ?  42   LEU B CB  1 
ATOM   4122  C  CG  . LEU B  2 15  ? 22.643  72.283  29.596  1.00 37.88 ?  42   LEU B CG  1 
ATOM   4123  C  CD1 . LEU B  2 15  ? 23.621  73.428  29.363  1.00 36.96 ?  42   LEU B CD1 1 
ATOM   4124  C  CD2 . LEU B  2 15  ? 23.331  71.094  30.254  1.00 37.14 ?  42   LEU B CD2 1 
ATOM   4125  N  N   . ALA B  2 16  ? 18.667  74.053  31.073  1.00 39.12 ?  43   ALA B N   1 
ATOM   4126  C  CA  . ALA B  2 16  ? 17.240  74.228  30.787  1.00 39.89 ?  43   ALA B CA  1 
ATOM   4127  C  C   . ALA B  2 16  ? 16.836  75.700  30.760  1.00 40.52 ?  43   ALA B C   1 
ATOM   4128  O  O   . ALA B  2 16  ? 15.847  76.067  30.124  1.00 40.63 ?  43   ALA B O   1 
ATOM   4129  C  CB  . ALA B  2 16  ? 16.401  73.465  31.808  1.00 39.66 ?  43   ALA B CB  1 
ATOM   4130  N  N   . CYS B  2 17  ? 17.614  76.533  31.446  1.00 41.33 ?  44   CYS B N   1 
ATOM   4131  C  CA  . CYS B  2 17  ? 17.294  77.949  31.602  1.00 42.16 ?  44   CYS B CA  1 
ATOM   4132  C  C   . CYS B  2 17  ? 18.003  78.879  30.619  1.00 43.00 ?  44   CYS B C   1 
ATOM   4133  O  O   . CYS B  2 17  ? 17.859  80.102  30.705  1.00 43.11 ?  44   CYS B O   1 
ATOM   4134  C  CB  . CYS B  2 17  ? 17.561  78.387  33.038  1.00 41.96 ?  44   CYS B CB  1 
ATOM   4135  S  SG  . CYS B  2 17  ? 16.228  77.931  34.138  1.00 41.62 ?  44   CYS B SG  1 
ATOM   4136  N  N   . LYS B  2 18  ? 18.756  78.301  29.686  1.00 44.00 ?  45   LYS B N   1 
ATOM   4137  C  CA  . LYS B  2 18  ? 19.442  79.089  28.665  1.00 44.92 ?  45   LYS B CA  1 
ATOM   4138  C  C   . LYS B  2 18  ? 18.477  79.641  27.616  1.00 45.35 ?  45   LYS B C   1 
ATOM   4139  O  O   . LYS B  2 18  ? 17.551  78.946  27.182  1.00 45.53 ?  45   LYS B O   1 
ATOM   4140  C  CB  . LYS B  2 18  ? 20.578  78.294  28.015  1.00 45.08 ?  45   LYS B CB  1 
ATOM   4141  C  CG  . LYS B  2 18  ? 21.889  78.367  28.799  1.00 45.63 ?  45   LYS B CG  1 
ATOM   4142  C  CD  . LYS B  2 18  ? 23.078  77.853  27.990  1.00 46.98 ?  45   LYS B CD  1 
ATOM   4143  C  CE  . LYS B  2 18  ? 23.522  78.853  26.925  1.00 47.71 ?  45   LYS B CE  1 
ATOM   4144  N  NZ  . LYS B  2 18  ? 24.802  78.442  26.286  1.00 48.08 ?  45   LYS B NZ  1 
ATOM   4145  N  N   . ASP B  2 19  ? 18.713  80.894  27.225  1.00 45.84 ?  46   ASP B N   1 
ATOM   4146  C  CA  . ASP B  2 19  ? 17.839  81.649  26.316  1.00 46.16 ?  46   ASP B CA  1 
ATOM   4147  C  C   . ASP B  2 19  ? 16.436  81.897  26.899  1.00 46.23 ?  46   ASP B C   1 
ATOM   4148  O  O   . ASP B  2 19  ? 15.455  82.027  26.160  1.00 46.28 ?  46   ASP B O   1 
ATOM   4149  C  CB  . ASP B  2 19  ? 17.776  80.999  24.922  1.00 46.34 ?  46   ASP B CB  1 
ATOM   4150  C  CG  . ASP B  2 19  ? 18.956  81.391  24.028  1.00 46.92 ?  46   ASP B CG  1 
ATOM   4151  O  OD1 . ASP B  2 19  ? 19.523  82.492  24.211  1.00 47.30 ?  46   ASP B OD1 1 
ATOM   4152  O  OD2 . ASP B  2 19  ? 19.306  80.598  23.126  1.00 47.30 ?  46   ASP B OD2 1 
ATOM   4153  N  N   . LYS B  2 20  ? 16.356  81.970  28.226  1.00 46.19 ?  47   LYS B N   1 
ATOM   4154  C  CA  . LYS B  2 20  ? 15.095  82.240  28.918  1.00 46.23 ?  47   LYS B CA  1 
ATOM   4155  C  C   . LYS B  2 20  ? 15.226  83.378  29.935  1.00 46.13 ?  47   LYS B C   1 
ATOM   4156  O  O   . LYS B  2 20  ? 16.334  83.766  30.311  1.00 46.21 ?  47   LYS B O   1 
ATOM   4157  C  CB  . LYS B  2 20  ? 14.559  80.971  29.591  1.00 46.31 ?  47   LYS B CB  1 
ATOM   4158  C  CG  . LYS B  2 20  ? 13.996  79.943  28.614  1.00 46.50 ?  47   LYS B CG  1 
ATOM   4159  C  CD  . LYS B  2 20  ? 13.241  78.840  29.339  1.00 46.98 ?  47   LYS B CD  1 
ATOM   4160  C  CE  . LYS B  2 20  ? 13.053  77.608  28.459  1.00 47.23 ?  47   LYS B CE  1 
ATOM   4161  N  NZ  . LYS B  2 20  ? 12.173  77.846  27.278  1.00 47.20 ?  47   LYS B NZ  1 
ATOM   4162  N  N   . LYS B  2 21  ? 14.084  83.907  30.367  1.00 45.94 ?  48   LYS B N   1 
ATOM   4163  C  CA  . LYS B  2 21  ? 14.046  85.033  31.301  1.00 45.70 ?  48   LYS B CA  1 
ATOM   4164  C  C   . LYS B  2 21  ? 14.285  84.565  32.739  1.00 45.36 ?  48   LYS B C   1 
ATOM   4165  O  O   . LYS B  2 21  ? 13.993  83.414  33.069  1.00 45.42 ?  48   LYS B O   1 
ATOM   4166  C  CB  . LYS B  2 21  ? 12.706  85.774  31.198  1.00 45.78 ?  48   LYS B CB  1 
ATOM   4167  C  CG  . LYS B  2 21  ? 12.320  86.183  29.783  1.00 46.18 ?  48   LYS B CG  1 
ATOM   4168  C  CD  . LYS B  2 21  ? 10.948  86.846  29.744  1.00 47.10 ?  48   LYS B CD  1 
ATOM   4169  C  CE  . LYS B  2 21  ? 10.219  86.553  28.434  1.00 47.52 ?  48   LYS B CE  1 
ATOM   4170  N  NZ  . LYS B  2 21  ? 10.995  86.951  27.222  1.00 48.10 ?  48   LYS B NZ  1 
ATOM   4171  N  N   . PRO B  2 22  ? 14.824  85.456  33.598  1.00 44.95 ?  49   PRO B N   1 
ATOM   4172  C  CA  . PRO B  2 22  ? 15.022  85.145  35.018  1.00 44.51 ?  49   PRO B CA  1 
ATOM   4173  C  C   . PRO B  2 22  ? 13.745  84.735  35.761  1.00 43.97 ?  49   PRO B C   1 
ATOM   4174  O  O   . PRO B  2 22  ? 13.822  83.968  36.723  1.00 44.10 ?  49   PRO B O   1 
ATOM   4175  C  CB  . PRO B  2 22  ? 15.567  86.459  35.587  1.00 44.59 ?  49   PRO B CB  1 
ATOM   4176  C  CG  . PRO B  2 22  ? 16.268  87.087  34.445  1.00 44.79 ?  49   PRO B CG  1 
ATOM   4177  C  CD  . PRO B  2 22  ? 15.434  86.752  33.240  1.00 44.96 ?  49   PRO B CD  1 
ATOM   4178  N  N   . THR B  2 23  ? 12.591  85.234  35.318  1.00 43.15 ?  50   THR B N   1 
ATOM   4179  C  CA  . THR B  2 23  ? 11.309  84.922  35.963  1.00 42.39 ?  50   THR B CA  1 
ATOM   4180  C  C   . THR B  2 23  ? 10.686  83.613  35.473  1.00 41.74 ?  50   THR B C   1 
ATOM   4181  O  O   . THR B  2 23  ? 9.804   83.058  36.136  1.00 41.66 ?  50   THR B O   1 
ATOM   4182  C  CB  . THR B  2 23  ? 10.277  86.063  35.788  1.00 42.47 ?  50   THR B CB  1 
ATOM   4183  O  OG1 . THR B  2 23  ? 10.231  86.464  34.413  1.00 42.46 ?  50   THR B OG1 1 
ATOM   4184  C  CG2 . THR B  2 23  ? 10.639  87.260  36.662  1.00 42.43 ?  50   THR B CG2 1 
ATOM   4185  N  N   . ASP B  2 24  ? 11.146  83.132  34.318  1.00 40.96 ?  51   ASP B N   1 
ATOM   4186  C  CA  . ASP B  2 24  ? 10.669  81.875  33.738  1.00 40.17 ?  51   ASP B CA  1 
ATOM   4187  C  C   . ASP B  2 24  ? 10.933  80.681  34.654  1.00 39.45 ?  51   ASP B C   1 
ATOM   4188  O  O   . ASP B  2 24  ? 11.970  80.614  35.316  1.00 39.49 ?  51   ASP B O   1 
ATOM   4189  C  CB  . ASP B  2 24  ? 11.316  81.630  32.372  1.00 40.29 ?  51   ASP B CB  1 
ATOM   4190  C  CG  . ASP B  2 24  ? 10.723  82.496  31.270  1.00 40.66 ?  51   ASP B CG  1 
ATOM   4191  O  OD1 . ASP B  2 24  ? 11.450  82.779  30.294  1.00 41.05 ?  51   ASP B OD1 1 
ATOM   4192  O  OD2 . ASP B  2 24  ? 9.538   82.888  31.368  1.00 41.03 ?  51   ASP B OD2 1 
ATOM   4193  N  N   . VAL B  2 25  ? 9.985   79.748  34.682  1.00 38.53 ?  52   VAL B N   1 
ATOM   4194  C  CA  . VAL B  2 25  ? 10.106  78.529  35.480  1.00 37.56 ?  52   VAL B CA  1 
ATOM   4195  C  C   . VAL B  2 25  ? 10.206  77.286  34.581  1.00 36.93 ?  52   VAL B C   1 
ATOM   4196  O  O   . VAL B  2 25  ? 9.433   77.124  33.636  1.00 36.77 ?  52   VAL B O   1 
ATOM   4197  C  CB  . VAL B  2 25  ? 8.937   78.389  36.497  1.00 37.62 ?  52   VAL B CB  1 
ATOM   4198  C  CG1 . VAL B  2 25  ? 9.039   77.089  37.272  1.00 37.56 ?  52   VAL B CG1 1 
ATOM   4199  C  CG2 . VAL B  2 25  ? 8.920   79.568  37.469  1.00 37.50 ?  52   VAL B CG2 1 
ATOM   4200  N  N   . VAL B  2 26  ? 11.174  76.423  34.883  1.00 36.02 ?  53   VAL B N   1 
ATOM   4201  C  CA  . VAL B  2 26  ? 11.385  75.182  34.137  1.00 35.11 ?  53   VAL B CA  1 
ATOM   4202  C  C   . VAL B  2 26  ? 11.192  73.954  35.028  1.00 34.51 ?  53   VAL B C   1 
ATOM   4203  O  O   . VAL B  2 26  ? 11.247  74.051  36.258  1.00 34.18 ?  53   VAL B O   1 
ATOM   4204  C  CB  . VAL B  2 26  ? 12.799  75.126  33.488  1.00 35.10 ?  53   VAL B CB  1 
ATOM   4205  C  CG1 . VAL B  2 26  ? 12.958  76.218  32.431  1.00 35.02 ?  53   VAL B CG1 1 
ATOM   4206  C  CG2 . VAL B  2 26  ? 13.898  75.230  34.547  1.00 35.12 ?  53   VAL B CG2 1 
ATOM   4207  N  N   . LYS B  2 27  ? 10.968  72.804  34.398  1.00 33.75 ?  54   LYS B N   1 
ATOM   4208  C  CA  . LYS B  2 27  ? 10.954  71.530  35.107  1.00 33.18 ?  54   LYS B CA  1 
ATOM   4209  C  C   . LYS B  2 27  ? 12.369  71.074  35.441  1.00 32.51 ?  54   LYS B C   1 
ATOM   4210  O  O   . LYS B  2 27  ? 13.309  71.333  34.685  1.00 32.52 ?  54   LYS B O   1 
ATOM   4211  C  CB  . LYS B  2 27  ? 10.291  70.449  34.262  1.00 33.32 ?  54   LYS B CB  1 
ATOM   4212  C  CG  . LYS B  2 27  ? 8.786   70.436  34.298  1.00 34.02 ?  54   LYS B CG  1 
ATOM   4213  C  CD  . LYS B  2 27  ? 8.295   69.144  33.686  1.00 34.78 ?  54   LYS B CD  1 
ATOM   4214  C  CE  . LYS B  2 27  ? 6.992   69.341  32.965  1.00 35.41 ?  54   LYS B CE  1 
ATOM   4215  N  NZ  . LYS B  2 27  ? 6.726   68.204  32.046  1.00 35.66 ?  54   LYS B NZ  1 
ATOM   4216  N  N   . SER B  2 28  ? 12.506  70.393  36.576  1.00 31.68 ?  55   SER B N   1 
ATOM   4217  C  CA  . SER B  2 28  ? 13.734  69.681  36.920  1.00 30.89 ?  55   SER B CA  1 
ATOM   4218  C  C   . SER B  2 28  ? 13.902  68.487  35.984  1.00 30.45 ?  55   SER B C   1 
ATOM   4219  O  O   . SER B  2 28  ? 12.915  67.925  35.503  1.00 30.27 ?  55   SER B O   1 
ATOM   4220  C  CB  . SER B  2 28  ? 13.678  69.198  38.372  1.00 30.78 ?  55   SER B CB  1 
ATOM   4221  O  OG  . SER B  2 28  ? 14.767  68.349  38.686  1.00 30.56 ?  55   SER B OG  1 
ATOM   4222  N  N   . HIS B  2 29  ? 15.149  68.107  35.722  1.00 29.90 ?  56   HIS B N   1 
ATOM   4223  C  CA  . HIS B  2 29  ? 15.433  66.908  34.935  1.00 29.36 ?  56   HIS B CA  1 
ATOM   4224  C  C   . HIS B  2 29  ? 15.647  65.692  35.835  1.00 29.01 ?  56   HIS B C   1 
ATOM   4225  O  O   . HIS B  2 29  ? 15.768  64.570  35.345  1.00 28.84 ?  56   HIS B O   1 
ATOM   4226  C  CB  . HIS B  2 29  ? 16.676  67.114  34.064  1.00 29.44 ?  56   HIS B CB  1 
ATOM   4227  C  CG  . HIS B  2 29  ? 16.415  67.834  32.776  1.00 29.69 ?  56   HIS B CG  1 
ATOM   4228  N  ND1 . HIS B  2 29  ? 16.294  69.206  32.700  1.00 29.59 ?  56   HIS B ND1 1 
ATOM   4229  C  CD2 . HIS B  2 29  ? 16.287  67.376  31.508  1.00 29.54 ?  56   HIS B CD2 1 
ATOM   4230  C  CE1 . HIS B  2 29  ? 16.088  69.560  31.444  1.00 29.84 ?  56   HIS B CE1 1 
ATOM   4231  N  NE2 . HIS B  2 29  ? 16.081  68.469  30.699  1.00 30.22 ?  56   HIS B NE2 1 
ATOM   4232  N  N   . THR B  2 30  ? 15.688  65.911  37.149  1.00 28.58 ?  57   THR B N   1 
ATOM   4233  C  CA  . THR B  2 30  ? 16.164  64.877  38.070  1.00 28.25 ?  57   THR B CA  1 
ATOM   4234  C  C   . THR B  2 30  ? 15.344  64.707  39.350  1.00 28.26 ?  57   THR B C   1 
ATOM   4235  O  O   . THR B  2 30  ? 15.368  63.633  39.958  1.00 27.96 ?  57   THR B O   1 
ATOM   4236  C  CB  . THR B  2 30  ? 17.633  65.131  38.484  1.00 28.12 ?  57   THR B CB  1 
ATOM   4237  O  OG1 . THR B  2 30  ? 17.733  66.414  39.110  1.00 28.02 ?  57   THR B OG1 1 
ATOM   4238  C  CG2 . THR B  2 30  ? 18.565  65.082  37.279  1.00 27.79 ?  57   THR B CG2 1 
ATOM   4239  N  N   . GLU B  2 31  ? 14.627  65.757  39.750  1.00 28.33 ?  58   GLU B N   1 
ATOM   4240  C  CA  . GLU B  2 31  ? 14.001  65.807  41.074  1.00 28.56 ?  58   GLU B CA  1 
ATOM   4241  C  C   . GLU B  2 31  ? 12.489  65.632  41.062  1.00 28.70 ?  58   GLU B C   1 
ATOM   4242  O  O   . GLU B  2 31  ? 11.779  66.279  40.293  1.00 28.76 ?  58   GLU B O   1 
ATOM   4243  C  CB  . GLU B  2 31  ? 14.361  67.113  41.804  1.00 28.45 ?  58   GLU B CB  1 
ATOM   4244  C  CG  . GLU B  2 31  ? 15.857  67.423  41.886  1.00 28.41 ?  58   GLU B CG  1 
ATOM   4245  C  CD  . GLU B  2 31  ? 16.674  66.278  42.464  1.00 28.28 ?  58   GLU B CD  1 
ATOM   4246  O  OE1 . GLU B  2 31  ? 17.554  65.768  41.744  1.00 27.27 ?  58   GLU B OE1 1 
ATOM   4247  O  OE2 . GLU B  2 31  ? 16.429  65.883  43.626  1.00 28.49 ?  58   GLU B OE2 1 
ATOM   4248  N  N   . VAL B  2 32  ? 12.018  64.739  41.929  1.00 29.11 ?  59   VAL B N   1 
ATOM   4249  C  CA  . VAL B  2 32  ? 10.596  64.575  42.220  1.00 29.57 ?  59   VAL B CA  1 
ATOM   4250  C  C   . VAL B  2 32  ? 10.398  64.757  43.724  1.00 30.01 ?  59   VAL B C   1 
ATOM   4251  O  O   . VAL B  2 32  ? 11.111  64.153  44.524  1.00 29.87 ?  59   VAL B O   1 
ATOM   4252  C  CB  . VAL B  2 32  ? 10.063  63.184  41.772  1.00 29.53 ?  59   VAL B CB  1 
ATOM   4253  C  CG1 . VAL B  2 32  ? 8.641   62.940  42.281  1.00 29.36 ?  59   VAL B CG1 1 
ATOM   4254  C  CG2 . VAL B  2 32  ? 10.111  63.045  40.255  1.00 29.33 ?  59   VAL B CG2 1 
ATOM   4255  N  N   . GLU B  2 33  ? 9.451   65.620  44.093  1.00 30.71 ?  60   GLU B N   1 
ATOM   4256  C  CA  . GLU B  2 33  ? 9.056   65.831  45.487  1.00 31.33 ?  60   GLU B CA  1 
ATOM   4257  C  C   . GLU B  2 33  ? 7.534   65.927  45.561  1.00 31.84 ?  60   GLU B C   1 
ATOM   4258  O  O   . GLU B  2 33  ? 6.906   66.560  44.704  1.00 31.90 ?  60   GLU B O   1 
ATOM   4259  C  CB  . GLU B  2 33  ? 9.680   67.111  46.065  1.00 31.37 ?  60   GLU B CB  1 
ATOM   4260  C  CG  . GLU B  2 33  ? 11.214  67.159  46.118  1.00 31.57 ?  60   GLU B CG  1 
ATOM   4261  C  CD  . GLU B  2 33  ? 11.835  66.244  47.167  1.00 32.00 ?  60   GLU B CD  1 
ATOM   4262  O  OE1 . GLU B  2 33  ? 13.035  65.922  47.027  1.00 31.47 ?  60   GLU B OE1 1 
ATOM   4263  O  OE2 . GLU B  2 33  ? 11.142  65.852  48.131  1.00 32.55 ?  60   GLU B OE2 1 
ATOM   4264  N  N   . ASN B  2 34  ? 6.951   65.298  46.583  1.00 32.34 ?  61   ASN B N   1 
ATOM   4265  C  CA  . ASN B  2 34  ? 5.495   65.290  46.806  1.00 32.92 ?  61   ASN B CA  1 
ATOM   4266  C  C   . ASN B  2 34  ? 4.687   64.827  45.588  1.00 33.00 ?  61   ASN B C   1 
ATOM   4267  O  O   . ASN B  2 34  ? 3.604   65.353  45.308  1.00 32.90 ?  61   ASN B O   1 
ATOM   4268  C  CB  . ASN B  2 34  ? 4.996   66.658  47.308  1.00 33.16 ?  61   ASN B CB  1 
ATOM   4269  C  CG  . ASN B  2 34  ? 5.633   67.076  48.627  1.00 34.28 ?  61   ASN B CG  1 
ATOM   4270  O  OD1 . ASN B  2 34  ? 6.247   68.142  48.720  1.00 35.76 ?  61   ASN B OD1 1 
ATOM   4271  N  ND2 . ASN B  2 34  ? 5.489   66.241  49.654  1.00 35.22 ?  61   ASN B ND2 1 
ATOM   4272  N  N   . GLY B  2 35  ? 5.232   63.847  44.869  1.00 33.10 ?  62   GLY B N   1 
ATOM   4273  C  CA  . GLY B  2 35  ? 4.549   63.227  43.736  1.00 33.24 ?  62   GLY B CA  1 
ATOM   4274  C  C   . GLY B  2 35  ? 4.595   64.018  42.443  1.00 33.39 ?  62   GLY B C   1 
ATOM   4275  O  O   . GLY B  2 35  ? 3.867   63.707  41.500  1.00 33.47 ?  62   GLY B O   1 
ATOM   4276  N  N   . LYS B  2 36  ? 5.451   65.037  42.394  1.00 33.65 ?  63   LYS B N   1 
ATOM   4277  C  CA  . LYS B  2 36  ? 5.543   65.921  41.228  1.00 33.94 ?  63   LYS B CA  1 
ATOM   4278  C  C   . LYS B  2 36  ? 6.986   66.300  40.910  1.00 33.78 ?  63   LYS B C   1 
ATOM   4279  O  O   . LYS B  2 36  ? 7.812   66.428  41.812  1.00 33.72 ?  63   LYS B O   1 
ATOM   4280  C  CB  . LYS B  2 36  ? 4.716   67.198  41.450  1.00 34.05 ?  63   LYS B CB  1 
ATOM   4281  C  CG  . LYS B  2 36  ? 3.213   66.971  41.601  1.00 34.98 ?  63   LYS B CG  1 
ATOM   4282  C  CD  . LYS B  2 36  ? 2.427   68.252  41.376  1.00 37.09 ?  63   LYS B CD  1 
ATOM   4283  C  CE  . LYS B  2 36  ? 0.929   68.001  41.486  1.00 38.14 ?  63   LYS B CE  1 
ATOM   4284  N  NZ  . LYS B  2 36  ? 0.131   69.208  41.118  1.00 39.16 ?  63   LYS B NZ  1 
ATOM   4285  N  N   . ILE B  2 37  ? 7.280   66.478  39.623  1.00 33.91 ?  64   ILE B N   1 
ATOM   4286  C  CA  . ILE B  2 37  ? 8.574   67.008  39.190  1.00 33.80 ?  64   ILE B CA  1 
ATOM   4287  C  C   . ILE B  2 37  ? 8.747   68.414  39.769  1.00 34.04 ?  64   ILE B C   1 
ATOM   4288  O  O   . ILE B  2 37  ? 7.864   69.262  39.632  1.00 33.97 ?  64   ILE B O   1 
ATOM   4289  C  CB  . ILE B  2 37  ? 8.704   67.034  37.642  1.00 33.75 ?  64   ILE B CB  1 
ATOM   4290  C  CG1 . ILE B  2 37  ? 8.718   65.608  37.076  1.00 33.50 ?  64   ILE B CG1 1 
ATOM   4291  C  CG2 . ILE B  2 37  ? 9.962   67.790  37.207  1.00 33.45 ?  64   ILE B CG2 1 
ATOM   4292  C  CD1 . ILE B  2 37  ? 8.517   65.528  35.571  1.00 32.81 ?  64   ILE B CD1 1 
ATOM   4293  N  N   . VAL B  2 38  ? 9.877   68.635  40.436  1.00 34.35 ?  65   VAL B N   1 
ATOM   4294  C  CA  . VAL B  2 38  ? 10.199  69.926  41.046  1.00 34.58 ?  65   VAL B CA  1 
ATOM   4295  C  C   . VAL B  2 38  ? 10.314  71.014  39.978  1.00 34.80 ?  65   VAL B C   1 
ATOM   4296  O  O   . VAL B  2 38  ? 10.889  70.793  38.908  1.00 34.63 ?  65   VAL B O   1 
ATOM   4297  C  CB  . VAL B  2 38  ? 11.508  69.843  41.883  1.00 34.65 ?  65   VAL B CB  1 
ATOM   4298  C  CG1 . VAL B  2 38  ? 11.883  71.202  42.482  1.00 34.49 ?  65   VAL B CG1 1 
ATOM   4299  C  CG2 . VAL B  2 38  ? 11.363  68.814  42.987  1.00 34.55 ?  65   VAL B CG2 1 
ATOM   4300  N  N   . ARG B  2 39  ? 9.737   72.176  40.270  1.00 35.15 ?  66   ARG B N   1 
ATOM   4301  C  CA  . ARG B  2 39  ? 9.854   73.343  39.402  1.00 35.66 ?  66   ARG B CA  1 
ATOM   4302  C  C   . ARG B  2 39  ? 10.937  74.284  39.917  1.00 35.98 ?  66   ARG B C   1 
ATOM   4303  O  O   . ARG B  2 39  ? 11.078  74.475  41.128  1.00 35.89 ?  66   ARG B O   1 
ATOM   4304  C  CB  . ARG B  2 39  ? 8.511   74.072  39.290  1.00 35.64 ?  66   ARG B CB  1 
ATOM   4305  C  CG  . ARG B  2 39  ? 7.652   73.652  38.093  1.00 35.97 ?  66   ARG B CG  1 
ATOM   4306  C  CD  . ARG B  2 39  ? 7.010   72.279  38.269  1.00 36.35 ?  66   ARG B CD  1 
ATOM   4307  N  NE  . ARG B  2 39  ? 6.183   71.926  37.113  1.00 37.09 ?  66   ARG B NE  1 
ATOM   4308  C  CZ  . ARG B  2 39  ? 5.637   70.730  36.902  1.00 37.04 ?  66   ARG B CZ  1 
ATOM   4309  N  NH1 . ARG B  2 39  ? 4.903   70.527  35.817  1.00 37.45 ?  66   ARG B NH1 1 
ATOM   4310  N  NH2 . ARG B  2 39  ? 5.825   69.734  37.764  1.00 37.00 ?  66   ARG B NH2 1 
ATOM   4311  N  N   . VAL B  2 40  ? 11.701  74.861  38.992  1.00 36.38 ?  67   VAL B N   1 
ATOM   4312  C  CA  . VAL B  2 40  ? 12.814  75.745  39.338  1.00 37.01 ?  67   VAL B CA  1 
ATOM   4313  C  C   . VAL B  2 40  ? 12.708  77.075  38.592  1.00 37.45 ?  67   VAL B C   1 
ATOM   4314  O  O   . VAL B  2 40  ? 12.484  77.097  37.381  1.00 37.43 ?  67   VAL B O   1 
ATOM   4315  C  CB  . VAL B  2 40  ? 14.192  75.072  39.049  1.00 36.91 ?  67   VAL B CB  1 
ATOM   4316  C  CG1 . VAL B  2 40  ? 15.351  76.027  39.331  1.00 36.98 ?  67   VAL B CG1 1 
ATOM   4317  C  CG2 . VAL B  2 40  ? 14.354  73.800  39.874  1.00 36.87 ?  67   VAL B CG2 1 
ATOM   4318  N  N   . LYS B  2 41  ? 12.858  78.178  39.326  1.00 38.14 ?  68   LYS B N   1 
ATOM   4319  C  CA  . LYS B  2 41  ? 12.923  79.504  38.717  1.00 38.81 ?  68   LYS B CA  1 
ATOM   4320  C  C   . LYS B  2 41  ? 14.322  79.737  38.152  1.00 39.24 ?  68   LYS B C   1 
ATOM   4321  O  O   . LYS B  2 41  ? 15.325  79.522  38.837  1.00 39.31 ?  68   LYS B O   1 
ATOM   4322  C  CB  . LYS B  2 41  ? 12.554  80.603  39.724  1.00 38.82 ?  68   LYS B CB  1 
ATOM   4323  C  CG  . LYS B  2 41  ? 12.329  81.982  39.082  1.00 39.40 ?  68   LYS B CG  1 
ATOM   4324  C  CD  . LYS B  2 41  ? 11.914  83.046  40.096  1.00 40.45 ?  68   LYS B CD  1 
ATOM   4325  C  CE  . LYS B  2 41  ? 13.115  83.600  40.862  1.00 40.94 ?  68   LYS B CE  1 
ATOM   4326  N  NZ  . LYS B  2 41  ? 12.700  84.495  41.978  1.00 41.31 ?  68   LYS B NZ  1 
ATOM   4327  N  N   . CYS B  2 42  ? 14.375  80.177  36.899  1.00 39.93 ?  69   CYS B N   1 
ATOM   4328  C  CA  . CYS B  2 42  ? 15.636  80.377  36.188  1.00 40.48 ?  69   CYS B CA  1 
ATOM   4329  C  C   . CYS B  2 42  ? 16.580  81.381  36.852  1.00 41.05 ?  69   CYS B C   1 
ATOM   4330  O  O   . CYS B  2 42  ? 17.800  81.217  36.791  1.00 41.14 ?  69   CYS B O   1 
ATOM   4331  C  CB  . CYS B  2 42  ? 15.366  80.752  34.731  1.00 40.46 ?  69   CYS B CB  1 
ATOM   4332  S  SG  . CYS B  2 42  ? 14.815  79.341  33.748  1.00 40.20 ?  69   CYS B SG  1 
ATOM   4333  N  N   . GLY B  2 43  ? 16.011  82.399  37.496  1.00 41.63 ?  70   GLY B N   1 
ATOM   4334  C  CA  . GLY B  2 43  ? 16.787  83.393  38.238  1.00 42.29 ?  70   GLY B CA  1 
ATOM   4335  C  C   . GLY B  2 43  ? 17.636  82.796  39.345  1.00 42.82 ?  70   GLY B C   1 
ATOM   4336  O  O   . GLY B  2 43  ? 18.790  83.189  39.524  1.00 42.89 ?  70   GLY B O   1 
ATOM   4337  N  N   . ASP B  2 44  ? 17.063  81.840  40.077  1.00 43.34 ?  71   ASP B N   1 
ATOM   4338  C  CA  . ASP B  2 44  ? 17.750  81.167  41.183  1.00 43.95 ?  71   ASP B CA  1 
ATOM   4339  C  C   . ASP B  2 44  ? 18.938  80.322  40.723  1.00 44.46 ?  71   ASP B C   1 
ATOM   4340  O  O   . ASP B  2 44  ? 20.027  80.411  41.297  1.00 44.53 ?  71   ASP B O   1 
ATOM   4341  C  CB  . ASP B  2 44  ? 16.770  80.297  41.982  1.00 43.81 ?  71   ASP B CB  1 
ATOM   4342  C  CG  . ASP B  2 44  ? 15.744  81.117  42.755  1.00 44.00 ?  71   ASP B CG  1 
ATOM   4343  O  OD1 . ASP B  2 44  ? 16.008  82.301  43.058  1.00 43.42 ?  71   ASP B OD1 1 
ATOM   4344  O  OD2 . ASP B  2 44  ? 14.666  80.566  43.065  1.00 44.14 ?  71   ASP B OD2 1 
ATOM   4345  N  N   . ILE B  2 45  ? 18.729  79.505  39.693  1.00 45.09 ?  72   ILE B N   1 
ATOM   4346  C  CA  . ILE B  2 45  ? 19.786  78.624  39.198  1.00 45.88 ?  72   ILE B CA  1 
ATOM   4347  C  C   . ILE B  2 45  ? 20.920  79.397  38.511  1.00 46.50 ?  72   ILE B C   1 
ATOM   4348  O  O   . ILE B  2 45  ? 22.091  79.065  38.692  1.00 46.39 ?  72   ILE B O   1 
ATOM   4349  C  CB  . ILE B  2 45  ? 19.238  77.450  38.313  1.00 45.74 ?  72   ILE B CB  1 
ATOM   4350  C  CG1 . ILE B  2 45  ? 20.339  76.424  38.022  1.00 45.59 ?  72   ILE B CG1 1 
ATOM   4351  C  CG2 . ILE B  2 45  ? 18.607  77.955  37.019  1.00 45.76 ?  72   ILE B CG2 1 
ATOM   4352  C  CD1 . ILE B  2 45  ? 20.888  75.741  39.262  1.00 44.87 ?  72   ILE B CD1 1 
ATOM   4353  N  N   . VAL B  2 46  ? 20.566  80.432  37.749  1.00 47.46 ?  73   VAL B N   1 
ATOM   4354  C  CA  . VAL B  2 46  ? 21.557  81.313  37.126  1.00 48.46 ?  73   VAL B CA  1 
ATOM   4355  C  C   . VAL B  2 46  ? 22.436  81.965  38.196  1.00 49.23 ?  73   VAL B C   1 
ATOM   4356  O  O   . VAL B  2 46  ? 23.663  81.939  38.092  1.00 49.27 ?  73   VAL B O   1 
ATOM   4357  C  CB  . VAL B  2 46  ? 20.895  82.377  36.202  1.00 48.37 ?  73   VAL B CB  1 
ATOM   4358  C  CG1 . VAL B  2 46  ? 21.858  83.520  35.881  1.00 48.34 ?  73   VAL B CG1 1 
ATOM   4359  C  CG2 . VAL B  2 46  ? 20.404  81.726  34.912  1.00 48.48 ?  73   VAL B CG2 1 
ATOM   4360  N  N   . ALA B  2 47  ? 21.799  82.515  39.231  1.00 50.26 ?  74   ALA B N   1 
ATOM   4361  C  CA  . ALA B  2 47  ? 22.499  83.158  40.344  1.00 51.35 ?  74   ALA B CA  1 
ATOM   4362  C  C   . ALA B  2 47  ? 23.482  82.218  41.047  1.00 52.11 ?  74   ALA B C   1 
ATOM   4363  O  O   . ALA B  2 47  ? 24.640  82.583  41.271  1.00 52.21 ?  74   ALA B O   1 
ATOM   4364  C  CB  . ALA B  2 47  ? 21.499  83.737  41.344  1.00 51.27 ?  74   ALA B CB  1 
ATOM   4365  N  N   . LEU B  2 48  ? 23.017  81.012  41.379  1.00 53.04 ?  75   LEU B N   1 
ATOM   4366  C  CA  . LEU B  2 48  ? 23.847  79.999  42.041  1.00 53.97 ?  75   LEU B CA  1 
ATOM   4367  C  C   . LEU B  2 48  ? 25.066  79.614  41.200  1.00 54.62 ?  75   LEU B C   1 
ATOM   4368  O  O   . LEU B  2 48  ? 26.164  79.446  41.733  1.00 54.65 ?  75   LEU B O   1 
ATOM   4369  C  CB  . LEU B  2 48  ? 23.016  78.756  42.386  1.00 53.97 ?  75   LEU B CB  1 
ATOM   4370  C  CG  . LEU B  2 48  ? 23.667  77.642  43.218  1.00 54.24 ?  75   LEU B CG  1 
ATOM   4371  C  CD1 . LEU B  2 48  ? 23.930  78.086  44.659  1.00 54.57 ?  75   LEU B CD1 1 
ATOM   4372  C  CD2 . LEU B  2 48  ? 22.805  76.388  43.197  1.00 54.45 ?  75   LEU B CD2 1 
ATOM   4373  N  N   . VAL B  2 49  ? 24.864  79.481  39.890  1.00 55.49 ?  76   VAL B N   1 
ATOM   4374  C  CA  . VAL B  2 49  ? 25.954  79.198  38.957  1.00 56.44 ?  76   VAL B CA  1 
ATOM   4375  C  C   . VAL B  2 49  ? 26.926  80.381  38.883  1.00 57.24 ?  76   VAL B C   1 
ATOM   4376  O  O   . VAL B  2 49  ? 28.144  80.186  38.873  1.00 57.31 ?  76   VAL B O   1 
ATOM   4377  C  CB  . VAL B  2 49  ? 25.419  78.818  37.546  1.00 56.38 ?  76   VAL B CB  1 
ATOM   4378  C  CG1 . VAL B  2 49  ? 26.530  78.842  36.497  1.00 56.33 ?  76   VAL B CG1 1 
ATOM   4379  C  CG2 . VAL B  2 49  ? 24.754  77.446  37.582  1.00 56.35 ?  76   VAL B CG2 1 
ATOM   4380  N  N   . GLN B  2 50  ? 26.381  81.598  38.859  1.00 58.21 ?  77   GLN B N   1 
ATOM   4381  C  CA  . GLN B  2 50  ? 27.190  82.819  38.757  1.00 59.23 ?  77   GLN B CA  1 
ATOM   4382  C  C   . GLN B  2 50  ? 28.121  83.036  39.953  1.00 59.83 ?  77   GLN B C   1 
ATOM   4383  O  O   . GLN B  2 50  ? 29.250  83.496  39.779  1.00 59.91 ?  77   GLN B O   1 
ATOM   4384  C  CB  . GLN B  2 50  ? 26.309  84.054  38.523  1.00 59.22 ?  77   GLN B CB  1 
ATOM   4385  C  CG  . GLN B  2 50  ? 25.754  84.152  37.102  1.00 59.63 ?  77   GLN B CG  1 
ATOM   4386  C  CD  . GLN B  2 50  ? 25.085  85.486  36.796  1.00 60.29 ?  77   GLN B CD  1 
ATOM   4387  O  OE1 . GLN B  2 50  ? 25.272  86.047  35.714  1.00 60.55 ?  77   GLN B OE1 1 
ATOM   4388  N  NE2 . GLN B  2 50  ? 24.298  85.996  37.742  1.00 60.11 ?  77   GLN B NE2 1 
ATOM   4389  N  N   . LYS B  2 51  ? 27.656  82.695  41.154  1.00 60.68 ?  78   LYS B N   1 
ATOM   4390  C  CA  . LYS B  2 51  ? 28.485  82.806  42.359  1.00 61.54 ?  78   LYS B CA  1 
ATOM   4391  C  C   . LYS B  2 51  ? 29.532  81.687  42.450  1.00 62.14 ?  78   LYS B C   1 
ATOM   4392  O  O   . LYS B  2 51  ? 30.411  81.718  43.318  1.00 62.22 ?  78   LYS B O   1 
ATOM   4393  C  CB  . LYS B  2 51  ? 27.623  82.872  43.630  1.00 61.55 ?  78   LYS B CB  1 
ATOM   4394  C  CG  . LYS B  2 51  ? 27.024  81.544  44.083  1.00 61.90 ?  78   LYS B CG  1 
ATOM   4395  C  CD  . LYS B  2 51  ? 26.108  81.710  45.294  1.00 62.28 ?  78   LYS B CD  1 
ATOM   4396  C  CE  . LYS B  2 51  ? 26.888  81.774  46.604  1.00 62.58 ?  78   LYS B CE  1 
ATOM   4397  N  NZ  . LYS B  2 51  ? 25.977  81.794  47.784  1.00 62.56 ?  78   LYS B NZ  1 
ATOM   4398  N  N   . ALA B  2 52  ? 29.427  80.708  41.550  1.00 62.85 ?  79   ALA B N   1 
ATOM   4399  C  CA  . ALA B  2 52  ? 30.400  79.619  41.446  1.00 63.49 ?  79   ALA B CA  1 
ATOM   4400  C  C   . ALA B  2 52  ? 31.469  79.902  40.387  1.00 63.95 ?  79   ALA B C   1 
ATOM   4401  O  O   . ALA B  2 52  ? 32.617  79.479  40.537  1.00 64.02 ?  79   ALA B O   1 
ATOM   4402  C  CB  . ALA B  2 52  ? 29.698  78.297  41.161  1.00 63.46 ?  79   ALA B CB  1 
ATOM   4403  N  N   . ARG B  2 53  ? 31.086  80.610  39.322  1.00 64.55 ?  80   ARG B N   1 
ATOM   4404  C  CA  . ARG B  2 53  ? 32.031  81.036  38.281  1.00 65.16 ?  80   ARG B CA  1 
ATOM   4405  C  C   . ARG B  2 53  ? 32.945  82.152  38.794  1.00 65.58 ?  80   ARG B C   1 
ATOM   4406  O  O   . ARG B  2 53  ? 34.074  82.309  38.321  1.00 65.63 ?  80   ARG B O   1 
ATOM   4407  C  CB  . ARG B  2 53  ? 31.300  81.510  37.015  1.00 65.14 ?  80   ARG B CB  1 
ATOM   4408  C  CG  . ARG B  2 53  ? 30.286  80.533  36.412  1.00 65.30 ?  80   ARG B CG  1 
ATOM   4409  C  CD  . ARG B  2 53  ? 30.933  79.311  35.765  1.00 65.59 ?  80   ARG B CD  1 
ATOM   4410  N  NE  . ARG B  2 53  ? 29.991  78.606  34.893  1.00 65.73 ?  80   ARG B NE  1 
ATOM   4411  C  CZ  . ARG B  2 53  ? 30.031  77.302  34.620  1.00 65.72 ?  80   ARG B CZ  1 
ATOM   4412  N  NH1 . ARG B  2 53  ? 30.966  76.524  35.157  1.00 65.63 ?  80   ARG B NH1 1 
ATOM   4413  N  NH2 . ARG B  2 53  ? 29.123  76.772  33.812  1.00 65.46 ?  80   ARG B NH2 1 
ATOM   4414  N  N   . GLU B  2 54  ? 32.441  82.923  39.758  1.00 66.10 ?  81   GLU B N   1 
ATOM   4415  C  CA  . GLU B  2 54  ? 33.211  83.982  40.416  1.00 66.67 ?  81   GLU B CA  1 
ATOM   4416  C  C   . GLU B  2 54  ? 34.251  83.412  41.382  1.00 66.92 ?  81   GLU B C   1 
ATOM   4417  O  O   . GLU B  2 54  ? 35.261  84.059  41.669  1.00 66.99 ?  81   GLU B O   1 
ATOM   4418  C  CB  . GLU B  2 54  ? 32.275  84.939  41.164  1.00 66.70 ?  81   GLU B CB  1 
ATOM   4419  C  CG  . GLU B  2 54  ? 31.473  85.877  40.261  1.00 67.20 ?  81   GLU B CG  1 
ATOM   4420  C  CD  . GLU B  2 54  ? 30.230  86.447  40.939  1.00 67.72 ?  81   GLU B CD  1 
ATOM   4421  O  OE1 . GLU B  2 54  ? 29.297  86.858  40.213  1.00 67.63 ?  81   GLU B OE1 1 
ATOM   4422  O  OE2 . GLU B  2 54  ? 30.181  86.485  42.190  1.00 68.00 ?  81   GLU B OE2 1 
ATOM   4423  N  N   . GLN B  2 55  ? 33.991  82.205  41.882  1.00 67.27 ?  82   GLN B N   1 
ATOM   4424  C  CA  . GLN B  2 55  ? 34.897  81.525  42.812  1.00 67.56 ?  82   GLN B CA  1 
ATOM   4425  C  C   . GLN B  2 55  ? 35.785  80.489  42.107  1.00 67.71 ?  82   GLN B C   1 
ATOM   4426  O  O   . GLN B  2 55  ? 36.566  79.784  42.755  1.00 67.69 ?  82   GLN B O   1 
ATOM   4427  C  CB  . GLN B  2 55  ? 34.104  80.879  43.955  1.00 67.59 ?  82   GLN B CB  1 
ATOM   4428  C  CG  . GLN B  2 55  ? 33.437  81.880  44.901  1.00 67.79 ?  82   GLN B CG  1 
ATOM   4429  C  CD  . GLN B  2 55  ? 32.414  81.240  45.831  1.00 68.02 ?  82   GLN B CD  1 
ATOM   4430  O  OE1 . GLN B  2 55  ? 32.403  80.023  46.029  1.00 68.12 ?  82   GLN B OE1 1 
ATOM   4431  N  NE2 . GLN B  2 55  ? 31.547  82.065  46.408  1.00 68.07 ?  82   GLN B NE2 1 
ATOM   4432  N  N   . SER B  2 56  ? 35.659  80.409  40.782  1.00 67.88 ?  83   SER B N   1 
ATOM   4433  C  CA  . SER B  2 56  ? 36.488  79.526  39.959  1.00 68.04 ?  83   SER B CA  1 
ATOM   4434  C  C   . SER B  2 56  ? 37.751  80.239  39.480  1.00 68.17 ?  83   SER B C   1 
ATOM   4435  O  O   . SER B  2 56  ? 37.726  81.440  39.192  1.00 68.18 ?  83   SER B O   1 
ATOM   4436  C  CB  . SER B  2 56  ? 35.698  79.005  38.752  1.00 68.00 ?  83   SER B CB  1 
ATOM   4437  O  OG  . SER B  2 56  ? 34.741  78.032  39.133  1.00 67.97 ?  83   SER B OG  1 
ATOM   4438  N  N   . GLY B  2 57  ? 38.848  79.488  39.394  1.00 68.28 ?  84   GLY B N   1 
ATOM   4439  C  CA  . GLY B  2 57  ? 40.132  80.019  38.936  1.00 68.41 ?  84   GLY B CA  1 
ATOM   4440  C  C   . GLY B  2 57  ? 40.155  80.333  37.450  1.00 68.52 ?  84   GLY B C   1 
ATOM   4441  O  O   . GLY B  2 57  ? 39.561  79.618  36.641  1.00 68.57 ?  84   GLY B O   1 
ATOM   4442  N  N   . ASP C  1 1   ? 45.406  -1.041  11.724  1.00 38.76 ?  25   ASP C N   1 
ATOM   4443  C  CA  . ASP C  1 1   ? 45.860  -0.013  12.696  1.00 38.59 ?  25   ASP C CA  1 
ATOM   4444  C  C   . ASP C  1 1   ? 45.404  1.386   12.286  1.00 38.31 ?  25   ASP C C   1 
ATOM   4445  O  O   . ASP C  1 1   ? 45.394  1.728   11.100  1.00 38.33 ?  25   ASP C O   1 
ATOM   4446  C  CB  . ASP C  1 1   ? 47.384  -0.050  12.819  1.00 38.92 ?  25   ASP C CB  1 
ATOM   4447  C  CG  . ASP C  1 1   ? 47.890  0.630   14.077  1.00 39.76 ?  25   ASP C CG  1 
ATOM   4448  O  OD1 . ASP C  1 1   ? 47.310  0.402   15.163  1.00 41.47 ?  25   ASP C OD1 1 
ATOM   4449  O  OD2 . ASP C  1 1   ? 48.880  1.384   13.983  1.00 40.62 -1 25   ASP C OD2 1 
ATOM   4450  N  N   . ILE C  1 2   ? 45.017  2.182   13.279  1.00 37.79 ?  26   ILE C N   1 
ATOM   4451  C  CA  . ILE C  1 2   ? 44.720  3.595   13.077  1.00 37.43 ?  26   ILE C CA  1 
ATOM   4452  C  C   . ILE C  1 2   ? 45.856  4.404   13.706  1.00 37.05 ?  26   ILE C C   1 
ATOM   4453  O  O   . ILE C  1 2   ? 46.031  4.387   14.930  1.00 36.80 ?  26   ILE C O   1 
ATOM   4454  C  CB  . ILE C  1 2   ? 43.354  3.997   13.700  1.00 37.51 ?  26   ILE C CB  1 
ATOM   4455  C  CG1 . ILE C  1 2   ? 42.231  3.089   13.186  1.00 37.56 ?  26   ILE C CG1 1 
ATOM   4456  C  CG2 . ILE C  1 2   ? 43.041  5.458   13.401  1.00 37.71 ?  26   ILE C CG2 1 
ATOM   4457  C  CD1 . ILE C  1 2   ? 40.989  3.072   14.062  1.00 37.93 ?  26   ILE C CD1 1 
ATOM   4458  N  N   . SER C  1 3   ? 46.614  5.106   12.861  1.00 36.56 ?  27   SER C N   1 
ATOM   4459  C  CA  . SER C  1 3   ? 47.846  5.802   13.269  1.00 36.22 ?  27   SER C CA  1 
ATOM   4460  C  C   . SER C  1 3   ? 47.669  6.844   14.377  1.00 35.96 ?  27   SER C C   1 
ATOM   4461  O  O   . SER C  1 3   ? 48.573  7.048   15.194  1.00 35.84 ?  27   SER C O   1 
ATOM   4462  C  CB  . SER C  1 3   ? 48.523  6.453   12.058  1.00 36.17 ?  27   SER C CB  1 
ATOM   4463  O  OG  . SER C  1 3   ? 47.727  7.497   11.519  1.00 36.20 ?  27   SER C OG  1 
ATOM   4464  N  N   . THR C  1 4   ? 46.507  7.492   14.397  1.00 35.69 ?  28   THR C N   1 
ATOM   4465  C  CA  . THR C  1 4   ? 46.238  8.590   15.335  1.00 35.49 ?  28   THR C CA  1 
ATOM   4466  C  C   . THR C  1 4   ? 45.548  8.162   16.636  1.00 35.46 ?  28   THR C C   1 
ATOM   4467  O  O   . THR C  1 4   ? 45.160  9.008   17.445  1.00 35.39 ?  28   THR C O   1 
ATOM   4468  C  CB  . THR C  1 4   ? 45.409  9.700   14.667  1.00 35.46 ?  28   THR C CB  1 
ATOM   4469  O  OG1 . THR C  1 4   ? 44.313  9.112   13.952  1.00 35.15 ?  28   THR C OG1 1 
ATOM   4470  C  CG2 . THR C  1 4   ? 46.271  10.510  13.710  1.00 35.03 ?  28   THR C CG2 1 
ATOM   4471  N  N   . VAL C  1 5   ? 45.394  6.856   16.831  1.00 35.36 ?  29   VAL C N   1 
ATOM   4472  C  CA  . VAL C  1 5   ? 44.834  6.322   18.072  1.00 35.59 ?  29   VAL C CA  1 
ATOM   4473  C  C   . VAL C  1 5   ? 45.973  5.859   18.987  1.00 35.89 ?  29   VAL C C   1 
ATOM   4474  O  O   . VAL C  1 5   ? 46.855  5.122   18.547  1.00 35.92 ?  29   VAL C O   1 
ATOM   4475  C  CB  . VAL C  1 5   ? 43.820  5.180   17.802  1.00 35.53 ?  29   VAL C CB  1 
ATOM   4476  C  CG1 . VAL C  1 5   ? 43.404  4.486   19.096  1.00 35.41 ?  29   VAL C CG1 1 
ATOM   4477  C  CG2 . VAL C  1 5   ? 42.600  5.726   17.089  1.00 35.12 ?  29   VAL C CG2 1 
ATOM   4478  N  N   . PRO C  1 6   ? 45.970  6.315   20.256  1.00 36.25 ?  30   PRO C N   1 
ATOM   4479  C  CA  . PRO C  1 6   ? 47.036  5.987   21.213  1.00 36.38 ?  30   PRO C CA  1 
ATOM   4480  C  C   . PRO C  1 6   ? 47.087  4.513   21.619  1.00 36.64 ?  30   PRO C C   1 
ATOM   4481  O  O   . PRO C  1 6   ? 46.091  3.796   21.482  1.00 36.45 ?  30   PRO C O   1 
ATOM   4482  C  CB  . PRO C  1 6   ? 46.699  6.859   22.428  1.00 36.44 ?  30   PRO C CB  1 
ATOM   4483  C  CG  . PRO C  1 6   ? 45.256  7.196   22.278  1.00 36.41 ?  30   PRO C CG  1 
ATOM   4484  C  CD  . PRO C  1 6   ? 45.018  7.293   20.813  1.00 36.25 ?  30   PRO C CD  1 
ATOM   4485  N  N   . ASP C  1 7   ? 48.249  4.085   22.117  1.00 36.91 ?  31   ASP C N   1 
ATOM   4486  C  CA  . ASP C  1 7   ? 48.481  2.707   22.558  1.00 37.23 ?  31   ASP C CA  1 
ATOM   4487  C  C   . ASP C  1 7   ? 47.525  2.261   23.660  1.00 37.31 ?  31   ASP C C   1 
ATOM   4488  O  O   . ASP C  1 7   ? 47.036  1.129   23.643  1.00 37.34 ?  31   ASP C O   1 
ATOM   4489  C  CB  . ASP C  1 7   ? 49.928  2.531   23.048  1.00 37.42 ?  31   ASP C CB  1 
ATOM   4490  C  CG  . ASP C  1 7   ? 50.947  2.529   21.914  1.00 37.76 ?  31   ASP C CG  1 
ATOM   4491  O  OD1 . ASP C  1 7   ? 50.565  2.294   20.749  1.00 38.13 ?  31   ASP C OD1 1 
ATOM   4492  O  OD2 . ASP C  1 7   ? 52.143  2.754   22.196  1.00 38.35 -1 31   ASP C OD2 1 
ATOM   4493  N  N   . GLU C  1 8   ? 47.266  3.154   24.614  1.00 37.49 ?  32   GLU C N   1 
ATOM   4494  C  CA  . GLU C  1 8   ? 46.442  2.842   25.788  1.00 37.74 ?  32   GLU C CA  1 
ATOM   4495  C  C   . GLU C  1 8   ? 44.991  2.472   25.457  1.00 37.69 ?  32   GLU C C   1 
ATOM   4496  O  O   . GLU C  1 8   ? 44.329  1.795   26.246  1.00 37.78 ?  32   GLU C O   1 
ATOM   4497  C  CB  . GLU C  1 8   ? 46.500  3.971   26.833  1.00 37.93 ?  32   GLU C CB  1 
ATOM   4498  C  CG  . GLU C  1 8   ? 46.530  5.396   26.279  1.00 39.07 ?  32   GLU C CG  1 
ATOM   4499  C  CD  . GLU C  1 8   ? 47.942  5.902   26.012  1.00 40.43 ?  32   GLU C CD  1 
ATOM   4500  O  OE1 . GLU C  1 8   ? 48.569  5.454   25.027  1.00 40.64 ?  32   GLU C OE1 1 
ATOM   4501  O  OE2 . GLU C  1 8   ? 48.420  6.764   26.780  1.00 41.35 -1 32   GLU C OE2 1 
ATOM   4502  N  N   . THR C  1 9   ? 44.510  2.904   24.293  1.00 37.50 ?  33   THR C N   1 
ATOM   4503  C  CA  . THR C  1 9   ? 43.180  2.527   23.821  1.00 37.45 ?  33   THR C CA  1 
ATOM   4504  C  C   . THR C  1 9   ? 43.141  1.062   23.381  1.00 37.40 ?  33   THR C C   1 
ATOM   4505  O  O   . THR C  1 9   ? 42.268  0.307   23.812  1.00 37.03 ?  33   THR C O   1 
ATOM   4506  C  CB  . THR C  1 9   ? 42.695  3.449   22.681  1.00 37.36 ?  33   THR C CB  1 
ATOM   4507  O  OG1 . THR C  1 9   ? 42.641  4.797   23.158  1.00 37.63 ?  33   THR C OG1 1 
ATOM   4508  C  CG2 . THR C  1 9   ? 41.308  3.037   22.196  1.00 37.24 ?  33   THR C CG2 1 
ATOM   4509  N  N   . TYR C  1 10  ? 44.091  0.675   22.528  1.00 37.65 ?  34   TYR C N   1 
ATOM   4510  C  CA  . TYR C  1 10  ? 44.219  -0.708  22.067  1.00 37.88 ?  34   TYR C CA  1 
ATOM   4511  C  C   . TYR C  1 10  ? 44.396  -1.678  23.233  1.00 38.22 ?  34   TYR C C   1 
ATOM   4512  O  O   . TYR C  1 10  ? 43.779  -2.745  23.256  1.00 38.10 ?  34   TYR C O   1 
ATOM   4513  C  CB  . TYR C  1 10  ? 45.372  -0.845  21.066  1.00 37.70 ?  34   TYR C CB  1 
ATOM   4514  C  CG  . TYR C  1 10  ? 45.056  -0.285  19.696  1.00 37.22 ?  34   TYR C CG  1 
ATOM   4515  C  CD1 . TYR C  1 10  ? 44.333  -1.033  18.767  1.00 36.22 ?  34   TYR C CD1 1 
ATOM   4516  C  CD2 . TYR C  1 10  ? 45.479  0.992   19.329  1.00 36.42 ?  34   TYR C CD2 1 
ATOM   4517  C  CE1 . TYR C  1 10  ? 44.037  -0.525  17.511  1.00 35.98 ?  34   TYR C CE1 1 
ATOM   4518  C  CE2 . TYR C  1 10  ? 45.191  1.509   18.072  1.00 36.26 ?  34   TYR C CE2 1 
ATOM   4519  C  CZ  . TYR C  1 10  ? 44.466  0.746   17.169  1.00 36.15 ?  34   TYR C CZ  1 
ATOM   4520  O  OH  . TYR C  1 10  ? 44.179  1.250   15.922  1.00 35.47 ?  34   TYR C OH  1 
ATOM   4521  N  N   . ASP C  1 11  ? 45.222  -1.283  24.204  1.00 38.79 ?  35   ASP C N   1 
ATOM   4522  C  CA  . ASP C  1 11  ? 45.430  -2.059  25.430  1.00 39.49 ?  35   ASP C CA  1 
ATOM   4523  C  C   . ASP C  1 11  ? 44.146  -2.206  26.250  1.00 39.80 ?  35   ASP C C   1 
ATOM   4524  O  O   . ASP C  1 11  ? 43.865  -3.285  26.770  1.00 39.89 ?  35   ASP C O   1 
ATOM   4525  C  CB  . ASP C  1 11  ? 46.541  -1.436  26.290  1.00 39.62 ?  35   ASP C CB  1 
ATOM   4526  C  CG  . ASP C  1 11  ? 47.906  -1.462  25.608  1.00 40.20 ?  35   ASP C CG  1 
ATOM   4527  O  OD1 . ASP C  1 11  ? 48.157  -2.357  24.769  1.00 41.04 ?  35   ASP C OD1 1 
ATOM   4528  O  OD2 . ASP C  1 11  ? 48.738  -0.583  25.920  1.00 41.04 -1 35   ASP C OD2 1 
ATOM   4529  N  N   . ALA C  1 12  ? 43.369  -1.126  26.352  1.00 40.19 ?  36   ALA C N   1 
ATOM   4530  C  CA  . ALA C  1 12  ? 42.112  -1.134  27.110  1.00 40.60 ?  36   ALA C CA  1 
ATOM   4531  C  C   . ALA C  1 12  ? 41.018  -1.970  26.443  1.00 40.90 ?  36   ALA C C   1 
ATOM   4532  O  O   . ALA C  1 12  ? 40.104  -2.455  27.114  1.00 40.91 ?  36   ALA C O   1 
ATOM   4533  C  CB  . ALA C  1 12  ? 41.622  0.289   27.358  1.00 40.55 ?  36   ALA C CB  1 
ATOM   4534  N  N   . LEU C  1 13  ? 41.122  -2.138  25.128  1.00 41.36 ?  37   LEU C N   1 
ATOM   4535  C  CA  . LEU C  1 13  ? 40.168  -2.943  24.363  1.00 41.98 ?  37   LEU C CA  1 
ATOM   4536  C  C   . LEU C  1 13  ? 40.648  -4.383  24.137  1.00 42.41 ?  37   LEU C C   1 
ATOM   4537  O  O   . LEU C  1 13  ? 39.941  -5.186  23.520  1.00 42.39 ?  37   LEU C O   1 
ATOM   4538  C  CB  . LEU C  1 13  ? 39.868  -2.279  23.014  1.00 41.90 ?  37   LEU C CB  1 
ATOM   4539  C  CG  . LEU C  1 13  ? 39.203  -0.900  22.976  1.00 41.87 ?  37   LEU C CG  1 
ATOM   4540  C  CD1 . LEU C  1 13  ? 39.361  -0.311  21.586  1.00 42.14 ?  37   LEU C CD1 1 
ATOM   4541  C  CD2 . LEU C  1 13  ? 37.734  -0.956  23.375  1.00 41.98 ?  37   LEU C CD2 1 
ATOM   4542  N  N   . LYS C  1 14  ? 41.842  -4.696  24.647  1.00 42.96 ?  38   LYS C N   1 
ATOM   4543  C  CA  . LYS C  1 14  ? 42.487  -6.009  24.477  1.00 43.47 ?  38   LYS C CA  1 
ATOM   4544  C  C   . LYS C  1 14  ? 42.760  -6.305  23.002  1.00 43.60 ?  38   LYS C C   1 
ATOM   4545  O  O   . LYS C  1 14  ? 42.384  -7.357  22.484  1.00 43.65 ?  38   LYS C O   1 
ATOM   4546  C  CB  . LYS C  1 14  ? 41.665  -7.138  25.125  1.00 43.50 ?  38   LYS C CB  1 
ATOM   4547  C  CG  . LYS C  1 14  ? 41.373  -6.940  26.607  1.00 44.52 ?  38   LYS C CG  1 
ATOM   4548  C  CD  . LYS C  1 14  ? 40.234  -7.838  27.072  1.00 45.77 ?  38   LYS C CD  1 
ATOM   4549  C  CE  . LYS C  1 14  ? 39.583  -7.287  28.336  1.00 46.54 ?  38   LYS C CE  1 
ATOM   4550  N  NZ  . LYS C  1 14  ? 38.371  -8.065  28.722  1.00 47.28 ?  38   LYS C NZ  1 
ATOM   4551  N  N   . LEU C  1 15  ? 43.418  -5.361  22.334  1.00 43.88 ?  39   LEU C N   1 
ATOM   4552  C  CA  . LEU C  1 15  ? 43.727  -5.488  20.914  1.00 44.09 ?  39   LEU C CA  1 
ATOM   4553  C  C   . LEU C  1 15  ? 45.213  -5.305  20.638  1.00 44.20 ?  39   LEU C C   1 
ATOM   4554  O  O   . LEU C  1 15  ? 45.894  -4.539  21.325  1.00 44.29 ?  39   LEU C O   1 
ATOM   4555  C  CB  . LEU C  1 15  ? 42.916  -4.480  20.090  1.00 44.04 ?  39   LEU C CB  1 
ATOM   4556  C  CG  . LEU C  1 15  ? 41.398  -4.658  19.967  1.00 44.36 ?  39   LEU C CG  1 
ATOM   4557  C  CD1 . LEU C  1 15  ? 40.784  -3.434  19.303  1.00 44.36 ?  39   LEU C CD1 1 
ATOM   4558  C  CD2 . LEU C  1 15  ? 41.032  -5.930  19.196  1.00 44.31 ?  39   LEU C CD2 1 
ATOM   4559  N  N   . ASP C  1 16  ? 45.700  -6.014  19.623  1.00 44.27 ?  40   ASP C N   1 
ATOM   4560  C  CA  . ASP C  1 16  ? 47.076  -5.891  19.160  1.00 44.46 ?  40   ASP C CA  1 
ATOM   4561  C  C   . ASP C  1 16  ? 47.106  -4.964  17.946  1.00 44.27 ?  40   ASP C C   1 
ATOM   4562  O  O   . ASP C  1 16  ? 46.505  -5.271  16.919  1.00 44.46 ?  40   ASP C O   1 
ATOM   4563  C  CB  . ASP C  1 16  ? 47.634  -7.281  18.815  1.00 44.61 ?  40   ASP C CB  1 
ATOM   4564  C  CG  . ASP C  1 16  ? 49.090  -7.250  18.374  1.00 45.24 ?  40   ASP C CG  1 
ATOM   4565  O  OD1 . ASP C  1 16  ? 49.779  -6.226  18.571  1.00 46.09 ?  40   ASP C OD1 1 
ATOM   4566  O  OD2 . ASP C  1 16  ? 49.552  -8.274  17.828  1.00 46.49 -1 40   ASP C OD2 1 
ATOM   4567  N  N   . ARG C  1 17  ? 47.800  -3.832  18.085  1.00 44.08 ?  41   ARG C N   1 
ATOM   4568  C  CA  . ARG C  1 17  ? 47.893  -2.794  17.046  1.00 43.83 ?  41   ARG C CA  1 
ATOM   4569  C  C   . ARG C  1 17  ? 48.188  -3.322  15.648  1.00 43.68 ?  41   ARG C C   1 
ATOM   4570  O  O   . ARG C  1 17  ? 47.468  -3.010  14.698  1.00 43.70 ?  41   ARG C O   1 
ATOM   4571  C  CB  . ARG C  1 17  ? 48.981  -1.773  17.393  1.00 43.91 ?  41   ARG C CB  1 
ATOM   4572  C  CG  . ARG C  1 17  ? 48.565  -0.665  18.325  1.00 43.72 ?  41   ARG C CG  1 
ATOM   4573  C  CD  . ARG C  1 17  ? 49.553  0.480   18.231  1.00 43.24 ?  41   ARG C CD  1 
ATOM   4574  N  NE  . ARG C  1 17  ? 49.098  1.513   17.305  1.00 42.81 ?  41   ARG C NE  1 
ATOM   4575  C  CZ  . ARG C  1 17  ? 48.525  2.651   17.684  1.00 42.61 ?  41   ARG C CZ  1 
ATOM   4576  N  NH1 . ARG C  1 17  ? 48.344  2.912   18.973  1.00 42.62 ?  41   ARG C NH1 1 
ATOM   4577  N  NH2 . ARG C  1 17  ? 48.136  3.535   16.777  1.00 42.54 ?  41   ARG C NH2 1 
ATOM   4578  N  N   . GLY C  1 18  ? 49.260  -4.103  15.529  1.00 43.45 ?  42   GLY C N   1 
ATOM   4579  C  CA  . GLY C  1 18  ? 49.746  -4.569  14.229  1.00 43.11 ?  42   GLY C CA  1 
ATOM   4580  C  C   . GLY C  1 18  ? 48.953  -5.719  13.640  1.00 42.77 ?  42   GLY C C   1 
ATOM   4581  O  O   . GLY C  1 18  ? 49.291  -6.224  12.569  1.00 42.94 ?  42   GLY C O   1 
ATOM   4582  N  N   . LYS C  1 19  ? 47.890  -6.118  14.335  1.00 42.37 ?  43   LYS C N   1 
ATOM   4583  C  CA  . LYS C  1 19  ? 47.096  -7.284  13.961  1.00 41.94 ?  43   LYS C CA  1 
ATOM   4584  C  C   . LYS C  1 19  ? 45.612  -6.944  13.770  1.00 41.37 ?  43   LYS C C   1 
ATOM   4585  O  O   . LYS C  1 19  ? 44.960  -7.483  12.871  1.00 41.25 ?  43   LYS C O   1 
ATOM   4586  C  CB  . LYS C  1 19  ? 47.275  -8.374  15.024  1.00 42.26 ?  43   LYS C CB  1 
ATOM   4587  C  CG  . LYS C  1 19  ? 46.631  -9.724  14.713  1.00 43.05 ?  43   LYS C CG  1 
ATOM   4588  C  CD  . LYS C  1 19  ? 47.294  -10.865 15.502  1.00 44.18 ?  43   LYS C CD  1 
ATOM   4589  C  CE  . LYS C  1 19  ? 47.140  -10.712 17.020  1.00 44.87 ?  43   LYS C CE  1 
ATOM   4590  N  NZ  . LYS C  1 19  ? 45.742  -10.944 17.490  1.00 45.42 ?  43   LYS C NZ  1 
ATOM   4591  N  N   . ALA C  1 20  ? 45.096  -6.044  14.608  1.00 40.55 ?  44   ALA C N   1 
ATOM   4592  C  CA  . ALA C  1 20  ? 43.664  -5.726  14.647  1.00 39.80 ?  44   ALA C CA  1 
ATOM   4593  C  C   . ALA C  1 20  ? 43.163  -5.061  13.368  1.00 39.17 ?  44   ALA C C   1 
ATOM   4594  O  O   . ALA C  1 20  ? 43.797  -4.147  12.842  1.00 39.25 ?  44   ALA C O   1 
ATOM   4595  C  CB  . ALA C  1 20  ? 43.339  -4.862  15.863  1.00 39.86 ?  44   ALA C CB  1 
ATOM   4596  N  N   . THR C  1 21  ? 42.024  -5.542  12.874  1.00 38.41 ?  45   THR C N   1 
ATOM   4597  C  CA  . THR C  1 21  ? 41.401  -5.014  11.661  1.00 37.60 ?  45   THR C CA  1 
ATOM   4598  C  C   . THR C  1 21  ? 40.413  -3.896  12.012  1.00 36.97 ?  45   THR C C   1 
ATOM   4599  O  O   . THR C  1 21  ? 40.051  -3.744  13.182  1.00 36.72 ?  45   THR C O   1 
ATOM   4600  C  CB  . THR C  1 21  ? 40.651  -6.123  10.879  1.00 37.64 ?  45   THR C CB  1 
ATOM   4601  O  OG1 . THR C  1 21  ? 39.595  -6.655  11.688  1.00 37.56 ?  45   THR C OG1 1 
ATOM   4602  C  CG2 . THR C  1 21  ? 41.601  -7.245  10.458  1.00 37.71 ?  45   THR C CG2 1 
ATOM   4603  N  N   . PRO C  1 22  ? 39.980  -3.105  11.003  1.00 36.40 ?  46   PRO C N   1 
ATOM   4604  C  CA  . PRO C  1 22  ? 38.930  -2.107  11.222  1.00 35.95 ?  46   PRO C CA  1 
ATOM   4605  C  C   . PRO C  1 22  ? 37.652  -2.693  11.826  1.00 35.57 ?  46   PRO C C   1 
ATOM   4606  O  O   . PRO C  1 22  ? 37.091  -2.109  12.755  1.00 35.39 ?  46   PRO C O   1 
ATOM   4607  C  CB  . PRO C  1 22  ? 38.663  -1.573  9.813   1.00 35.90 ?  46   PRO C CB  1 
ATOM   4608  C  CG  . PRO C  1 22  ? 39.963  -1.701  9.127   1.00 36.14 ?  46   PRO C CG  1 
ATOM   4609  C  CD  . PRO C  1 22  ? 40.583  -2.967  9.662   1.00 36.40 ?  46   PRO C CD  1 
ATOM   4610  N  N   . LYS C  1 23  ? 37.212  -3.841  11.309  1.00 35.20 ?  47   LYS C N   1 
ATOM   4611  C  CA  . LYS C  1 23  ? 36.033  -4.536  11.830  1.00 34.89 ?  47   LYS C CA  1 
ATOM   4612  C  C   . LYS C  1 23  ? 36.198  -4.894  13.309  1.00 34.64 ?  47   LYS C C   1 
ATOM   4613  O  O   . LYS C  1 23  ? 35.294  -4.657  14.113  1.00 34.40 ?  47   LYS C O   1 
ATOM   4614  C  CB  . LYS C  1 23  ? 35.721  -5.785  10.986  1.00 35.07 ?  47   LYS C CB  1 
ATOM   4615  C  CG  . LYS C  1 23  ? 34.709  -6.749  11.603  1.00 35.12 ?  47   LYS C CG  1 
ATOM   4616  C  CD  . LYS C  1 23  ? 34.173  -7.741  10.574  1.00 36.27 ?  47   LYS C CD  1 
ATOM   4617  C  CE  . LYS C  1 23  ? 33.602  -9.003  11.224  1.00 36.25 ?  47   LYS C CE  1 
ATOM   4618  N  NZ  . LYS C  1 23  ? 32.583  -8.722  12.279  1.00 36.89 ?  47   LYS C NZ  1 
ATOM   4619  N  N   . GLU C  1 24  ? 37.359  -5.445  13.661  1.00 34.36 ?  48   GLU C N   1 
ATOM   4620  C  CA  . GLU C  1 24  ? 37.638  -5.845  15.043  1.00 34.15 ?  48   GLU C CA  1 
ATOM   4621  C  C   . GLU C  1 24  ? 37.741  -4.641  15.975  1.00 33.64 ?  48   GLU C C   1 
ATOM   4622  O  O   . GLU C  1 24  ? 37.244  -4.681  17.101  1.00 33.47 ?  48   GLU C O   1 
ATOM   4623  C  CB  . GLU C  1 24  ? 38.917  -6.682  15.123  1.00 34.32 ?  48   GLU C CB  1 
ATOM   4624  C  CG  . GLU C  1 24  ? 38.799  -8.077  14.506  1.00 35.19 ?  48   GLU C CG  1 
ATOM   4625  C  CD  . GLU C  1 24  ? 40.149  -8.755  14.312  1.00 36.52 ?  48   GLU C CD  1 
ATOM   4626  O  OE1 . GLU C  1 24  ? 41.160  -8.046  14.106  1.00 36.64 ?  48   GLU C OE1 1 
ATOM   4627  O  OE2 . GLU C  1 24  ? 40.195  -10.003 14.357  1.00 37.80 -1 48   GLU C OE2 1 
ATOM   4628  N  N   . THR C  1 25  ? 38.384  -3.578  15.495  1.00 33.14 ?  49   THR C N   1 
ATOM   4629  C  CA  . THR C  1 25  ? 38.556  -2.349  16.270  1.00 32.89 ?  49   THR C CA  1 
ATOM   4630  C  C   . THR C  1 25  ? 37.207  -1.673  16.531  1.00 32.52 ?  49   THR C C   1 
ATOM   4631  O  O   . THR C  1 25  ? 36.927  -1.265  17.654  1.00 32.39 ?  49   THR C O   1 
ATOM   4632  C  CB  . THR C  1 25  ? 39.542  -1.370  15.580  1.00 32.85 ?  49   THR C CB  1 
ATOM   4633  O  OG1 . THR C  1 25  ? 40.780  -2.044  15.318  1.00 33.13 ?  49   THR C OG1 1 
ATOM   4634  C  CG2 . THR C  1 25  ? 39.820  -0.164  16.465  1.00 32.93 ?  49   THR C CG2 1 
ATOM   4635  N  N   . TYR C  1 26  ? 36.378  -1.580  15.491  1.00 32.29 ?  50   TYR C N   1 
ATOM   4636  C  CA  . TYR C  1 26  ? 35.030  -1.019  15.606  1.00 32.24 ?  50   TYR C CA  1 
ATOM   4637  C  C   . TYR C  1 26  ? 34.187  -1.770  16.639  1.00 32.30 ?  50   TYR C C   1 
ATOM   4638  O  O   . TYR C  1 26  ? 33.633  -1.159  17.556  1.00 32.22 ?  50   TYR C O   1 
ATOM   4639  C  CB  . TYR C  1 26  ? 34.333  -1.003  14.237  1.00 32.05 ?  50   TYR C CB  1 
ATOM   4640  C  CG  . TYR C  1 26  ? 32.890  -0.537  14.260  1.00 31.87 ?  50   TYR C CG  1 
ATOM   4641  C  CD1 . TYR C  1 26  ? 32.575  0.820   14.360  1.00 31.13 ?  50   TYR C CD1 1 
ATOM   4642  C  CD2 . TYR C  1 26  ? 31.838  -1.454  14.174  1.00 31.42 ?  50   TYR C CD2 1 
ATOM   4643  C  CE1 . TYR C  1 26  ? 31.257  1.254   14.384  1.00 30.79 ?  50   TYR C CE1 1 
ATOM   4644  C  CE2 . TYR C  1 26  ? 30.512  -1.028  14.194  1.00 31.63 ?  50   TYR C CE2 1 
ATOM   4645  C  CZ  . TYR C  1 26  ? 30.231  0.329   14.296  1.00 31.02 ?  50   TYR C CZ  1 
ATOM   4646  O  OH  . TYR C  1 26  ? 28.928  0.759   14.316  1.00 30.69 ?  50   TYR C OH  1 
ATOM   4647  N  N   . GLU C  1 27  ? 34.115  -3.094  16.497  1.00 32.36 ?  51   GLU C N   1 
ATOM   4648  C  CA  . GLU C  1 27  ? 33.286  -3.934  17.366  1.00 32.47 ?  51   GLU C CA  1 
ATOM   4649  C  C   . GLU C  1 27  ? 33.677  -3.849  18.844  1.00 32.27 ?  51   GLU C C   1 
ATOM   4650  O  O   . GLU C  1 27  ? 32.807  -3.849  19.715  1.00 32.41 ?  51   GLU C O   1 
ATOM   4651  C  CB  . GLU C  1 27  ? 33.288  -5.390  16.881  1.00 32.71 ?  51   GLU C CB  1 
ATOM   4652  C  CG  . GLU C  1 27  ? 32.528  -5.609  15.563  1.00 33.74 ?  51   GLU C CG  1 
ATOM   4653  C  CD  . GLU C  1 27  ? 32.425  -7.076  15.153  1.00 35.36 ?  51   GLU C CD  1 
ATOM   4654  O  OE1 . GLU C  1 27  ? 33.380  -7.845  15.400  1.00 36.12 ?  51   GLU C OE1 1 
ATOM   4655  O  OE2 . GLU C  1 27  ? 31.384  -7.458  14.569  1.00 35.93 -1 51   GLU C OE2 1 
ATOM   4656  N  N   . ALA C  1 28  ? 34.978  -3.766  19.119  1.00 31.90 ?  52   ALA C N   1 
ATOM   4657  C  CA  . ALA C  1 28  ? 35.480  -3.626  20.487  1.00 31.63 ?  52   ALA C CA  1 
ATOM   4658  C  C   . ALA C  1 28  ? 35.151  -2.245  21.063  1.00 31.56 ?  52   ALA C C   1 
ATOM   4659  O  O   . ALA C  1 28  ? 34.702  -2.127  22.210  1.00 31.22 ?  52   ALA C O   1 
ATOM   4660  C  CB  . ALA C  1 28  ? 36.984  -3.886  20.533  1.00 31.59 ?  52   ALA C CB  1 
ATOM   4661  N  N   . LEU C  1 29  ? 35.385  -1.210  20.255  1.00 31.46 ?  53   LEU C N   1 
ATOM   4662  C  CA  . LEU C  1 29  ? 35.016  0.166   20.590  1.00 31.42 ?  53   LEU C CA  1 
ATOM   4663  C  C   . LEU C  1 29  ? 33.544  0.277   20.964  1.00 31.33 ?  53   LEU C C   1 
ATOM   4664  O  O   . LEU C  1 29  ? 33.206  0.878   21.980  1.00 31.21 ?  53   LEU C O   1 
ATOM   4665  C  CB  . LEU C  1 29  ? 35.312  1.091   19.406  1.00 31.35 ?  53   LEU C CB  1 
ATOM   4666  C  CG  . LEU C  1 29  ? 36.395  2.179   19.420  1.00 31.65 ?  53   LEU C CG  1 
ATOM   4667  C  CD1 . LEU C  1 29  ? 37.261  2.225   20.680  1.00 31.04 ?  53   LEU C CD1 1 
ATOM   4668  C  CD2 . LEU C  1 29  ? 37.245  2.072   18.160  1.00 31.36 ?  53   LEU C CD2 1 
ATOM   4669  N  N   . VAL C  1 30  ? 32.683  -0.309  20.134  1.00 31.53 ?  54   VAL C N   1 
ATOM   4670  C  CA  . VAL C  1 30  ? 31.231  -0.248  20.322  1.00 31.79 ?  54   VAL C CA  1 
ATOM   4671  C  C   . VAL C  1 30  ? 30.778  -1.078  21.530  1.00 32.03 ?  54   VAL C C   1 
ATOM   4672  O  O   . VAL C  1 30  ? 29.881  -0.665  22.269  1.00 31.90 ?  54   VAL C O   1 
ATOM   4673  C  CB  . VAL C  1 30  ? 30.475  -0.666  19.031  1.00 31.86 ?  54   VAL C CB  1 
ATOM   4674  C  CG1 . VAL C  1 30  ? 28.962  -0.650  19.239  1.00 31.51 ?  54   VAL C CG1 1 
ATOM   4675  C  CG2 . VAL C  1 30  ? 30.850  0.263   17.879  1.00 31.62 ?  54   VAL C CG2 1 
ATOM   4676  N  N   . LYS C  1 31  ? 31.414  -2.235  21.726  1.00 32.32 ?  55   LYS C N   1 
ATOM   4677  C  CA  . LYS C  1 31  ? 31.150  -3.100  22.882  1.00 32.74 ?  55   LYS C CA  1 
ATOM   4678  C  C   . LYS C  1 31  ? 31.333  -2.345  24.205  1.00 32.59 ?  55   LYS C C   1 
ATOM   4679  O  O   . LYS C  1 31  ? 30.520  -2.485  25.118  1.00 32.88 ?  55   LYS C O   1 
ATOM   4680  C  CB  . LYS C  1 31  ? 32.037  -4.351  22.823  1.00 33.03 ?  55   LYS C CB  1 
ATOM   4681  C  CG  . LYS C  1 31  ? 31.816  -5.371  23.935  1.00 34.49 ?  55   LYS C CG  1 
ATOM   4682  C  CD  . LYS C  1 31  ? 32.331  -6.751  23.515  1.00 36.72 ?  55   LYS C CD  1 
ATOM   4683  C  CE  . LYS C  1 31  ? 33.068  -7.459  24.651  1.00 37.89 ?  55   LYS C CE  1 
ATOM   4684  N  NZ  . LYS C  1 31  ? 32.213  -7.720  25.844  1.00 39.46 ?  55   LYS C NZ  1 
ATOM   4685  N  N   . ARG C  1 32  ? 32.392  -1.543  24.298  1.00 32.31 ?  56   ARG C N   1 
ATOM   4686  C  CA  . ARG C  1 32  ? 32.593  -0.657  25.443  1.00 32.06 ?  56   ARG C CA  1 
ATOM   4687  C  C   . ARG C  1 32  ? 31.608  0.521   25.412  1.00 31.97 ?  56   ARG C C   1 
ATOM   4688  O  O   . ARG C  1 32  ? 31.046  0.897   26.443  1.00 31.80 ?  56   ARG C O   1 
ATOM   4689  C  CB  . ARG C  1 32  ? 34.041  -0.155  25.488  1.00 31.91 ?  56   ARG C CB  1 
ATOM   4690  C  CG  . ARG C  1 32  ? 34.337  0.816   26.634  1.00 31.63 ?  56   ARG C CG  1 
ATOM   4691  C  CD  . ARG C  1 32  ? 35.820  1.123   26.770  1.00 30.17 ?  56   ARG C CD  1 
ATOM   4692  N  NE  . ARG C  1 32  ? 36.336  1.902   25.644  1.00 29.33 ?  56   ARG C NE  1 
ATOM   4693  C  CZ  . ARG C  1 32  ? 37.527  2.493   25.624  1.00 28.65 ?  56   ARG C CZ  1 
ATOM   4694  N  NH1 . ARG C  1 32  ? 38.336  2.411   26.673  1.00 28.22 ?  56   ARG C NH1 1 
ATOM   4695  N  NH2 . ARG C  1 32  ? 37.908  3.180   24.557  1.00 28.49 ?  56   ARG C NH2 1 
ATOM   4696  N  N   . TYR C  1 33  ? 31.401  1.079   24.218  1.00 31.88 ?  57   TYR C N   1 
ATOM   4697  C  CA  . TYR C  1 33  ? 30.547  2.253   24.007  1.00 31.87 ?  57   TYR C CA  1 
ATOM   4698  C  C   . TYR C  1 33  ? 29.100  2.059   24.468  1.00 32.15 ?  57   TYR C C   1 
ATOM   4699  O  O   . TYR C  1 33  ? 28.501  2.971   25.032  1.00 31.91 ?  57   TYR C O   1 
ATOM   4700  C  CB  . TYR C  1 33  ? 30.582  2.671   22.526  1.00 31.63 ?  57   TYR C CB  1 
ATOM   4701  C  CG  . TYR C  1 33  ? 29.690  3.838   22.174  1.00 30.85 ?  57   TYR C CG  1 
ATOM   4702  C  CD1 . TYR C  1 33  ? 29.999  5.128   22.600  1.00 30.25 ?  57   TYR C CD1 1 
ATOM   4703  C  CD2 . TYR C  1 33  ? 28.540  3.655   21.405  1.00 30.44 ?  57   TYR C CD2 1 
ATOM   4704  C  CE1 . TYR C  1 33  ? 29.183  6.205   22.286  1.00 29.37 ?  57   TYR C CE1 1 
ATOM   4705  C  CE2 . TYR C  1 33  ? 27.714  4.728   21.079  1.00 29.77 ?  57   TYR C CE2 1 
ATOM   4706  C  CZ  . TYR C  1 33  ? 28.045  6.001   21.524  1.00 29.32 ?  57   TYR C CZ  1 
ATOM   4707  O  OH  . TYR C  1 33  ? 27.239  7.067   21.213  1.00 27.29 ?  57   TYR C OH  1 
ATOM   4708  N  N   . LYS C  1 34  ? 28.550  0.872   24.221  1.00 32.71 ?  58   LYS C N   1 
ATOM   4709  C  CA  . LYS C  1 34  ? 27.153  0.574   24.550  1.00 33.26 ?  58   LYS C CA  1 
ATOM   4710  C  C   . LYS C  1 34  ? 26.990  -0.117  25.904  1.00 33.41 ?  58   LYS C C   1 
ATOM   4711  O  O   . LYS C  1 34  ? 25.878  -0.456  26.305  1.00 33.66 ?  58   LYS C O   1 
ATOM   4712  C  CB  . LYS C  1 34  ? 26.520  -0.275  23.449  1.00 33.38 ?  58   LYS C CB  1 
ATOM   4713  C  CG  . LYS C  1 34  ? 26.051  0.513   22.240  1.00 34.20 ?  58   LYS C CG  1 
ATOM   4714  C  CD  . LYS C  1 34  ? 25.329  -0.404  21.272  1.00 35.55 ?  58   LYS C CD  1 
ATOM   4715  C  CE  . LYS C  1 34  ? 24.319  0.343   20.423  1.00 36.37 ?  58   LYS C CE  1 
ATOM   4716  N  NZ  . LYS C  1 34  ? 23.489  -0.610  19.625  1.00 36.59 ?  58   LYS C NZ  1 
ATOM   4717  N  N   . ASP C  1 35  ? 28.100  -0.311  26.608  1.00 33.66 ?  59   ASP C N   1 
ATOM   4718  C  CA  . ASP C  1 35  ? 28.088  -0.980  27.903  1.00 33.96 ?  59   ASP C CA  1 
ATOM   4719  C  C   . ASP C  1 35  ? 27.668  -0.020  29.024  1.00 33.86 ?  59   ASP C C   1 
ATOM   4720  O  O   . ASP C  1 35  ? 28.297  1.023   29.212  1.00 33.68 ?  59   ASP C O   1 
ATOM   4721  C  CB  . ASP C  1 35  ? 29.465  -1.598  28.188  1.00 33.96 ?  59   ASP C CB  1 
ATOM   4722  C  CG  . ASP C  1 35  ? 29.483  -2.454  29.444  1.00 34.58 ?  59   ASP C CG  1 
ATOM   4723  O  OD1 . ASP C  1 35  ? 28.428  -2.988  29.839  1.00 35.79 ?  59   ASP C OD1 1 
ATOM   4724  O  OD2 . ASP C  1 35  ? 30.566  -2.601  30.041  1.00 36.36 -1 59   ASP C OD2 1 
ATOM   4725  N  N   . PRO C  1 36  ? 26.597  -0.369  29.768  1.00 34.06 ?  60   PRO C N   1 
ATOM   4726  C  CA  . PRO C  1 36  ? 26.138  0.450   30.897  1.00 34.20 ?  60   PRO C CA  1 
ATOM   4727  C  C   . PRO C  1 36  ? 27.226  0.688   31.945  1.00 34.41 ?  60   PRO C C   1 
ATOM   4728  O  O   . PRO C  1 36  ? 27.302  1.782   32.517  1.00 34.41 ?  60   PRO C O   1 
ATOM   4729  C  CB  . PRO C  1 36  ? 24.995  -0.379  31.486  1.00 34.26 ?  60   PRO C CB  1 
ATOM   4730  C  CG  . PRO C  1 36  ? 24.463  -1.145  30.319  1.00 34.21 ?  60   PRO C CG  1 
ATOM   4731  C  CD  . PRO C  1 36  ? 25.676  -1.493  29.503  1.00 34.03 ?  60   PRO C CD  1 
ATOM   4732  N  N   . ALA C  1 37  ? 28.065  -0.324  32.175  1.00 34.45 ?  61   ALA C N   1 
ATOM   4733  C  CA  . ALA C  1 37  ? 29.184  -0.225  33.116  1.00 34.54 ?  61   ALA C CA  1 
ATOM   4734  C  C   . ALA C  1 37  ? 30.186  0.857   32.713  1.00 34.45 ?  61   ALA C C   1 
ATOM   4735  O  O   . ALA C  1 37  ? 30.858  1.437   33.571  1.00 34.61 ?  61   ALA C O   1 
ATOM   4736  C  CB  . ALA C  1 37  ? 29.884  -1.575  33.255  1.00 34.57 ?  61   ALA C CB  1 
ATOM   4737  N  N   . HIS C  1 38  ? 30.280  1.117   31.409  1.00 34.32 ?  62   HIS C N   1 
ATOM   4738  C  CA  . HIS C  1 38  ? 31.169  2.149   30.872  1.00 34.17 ?  62   HIS C CA  1 
ATOM   4739  C  C   . HIS C  1 38  ? 30.450  3.480   30.577  1.00 33.85 ?  62   HIS C C   1 
ATOM   4740  O  O   . HIS C  1 38  ? 31.021  4.385   29.953  1.00 33.72 ?  62   HIS C O   1 
ATOM   4741  C  CB  . HIS C  1 38  ? 31.915  1.627   29.635  1.00 34.35 ?  62   HIS C CB  1 
ATOM   4742  C  CG  . HIS C  1 38  ? 32.985  0.627   29.954  1.00 34.85 ?  62   HIS C CG  1 
ATOM   4743  N  ND1 . HIS C  1 38  ? 32.728  -0.721  30.091  1.00 35.38 ?  62   HIS C ND1 1 
ATOM   4744  C  CD2 . HIS C  1 38  ? 34.314  0.779   30.168  1.00 35.15 ?  62   HIS C CD2 1 
ATOM   4745  C  CE1 . HIS C  1 38  ? 33.852  -1.356  30.374  1.00 35.15 ?  62   HIS C CE1 1 
ATOM   4746  N  NE2 . HIS C  1 38  ? 34.829  -0.469  30.424  1.00 35.15 ?  62   HIS C NE2 1 
ATOM   4747  N  N   . GLY C  1 39  ? 29.199  3.586   31.024  1.00 33.50 ?  63   GLY C N   1 
ATOM   4748  C  CA  . GLY C  1 39  ? 28.487  4.864   31.034  1.00 33.08 ?  63   GLY C CA  1 
ATOM   4749  C  C   . GLY C  1 39  ? 27.199  4.962   30.234  1.00 32.90 ?  63   GLY C C   1 
ATOM   4750  O  O   . GLY C  1 39  ? 26.480  5.955   30.355  1.00 32.96 ?  63   GLY C O   1 
ATOM   4751  N  N   . ALA C  1 40  ? 26.907  3.944   29.421  1.00 32.56 ?  64   ALA C N   1 
ATOM   4752  C  CA  . ALA C  1 40  ? 25.701  3.923   28.585  1.00 32.38 ?  64   ALA C CA  1 
ATOM   4753  C  C   . ALA C  1 40  ? 24.418  3.718   29.401  1.00 32.20 ?  64   ALA C C   1 
ATOM   4754  O  O   . ALA C  1 40  ? 24.473  3.306   30.561  1.00 32.26 ?  64   ALA C O   1 
ATOM   4755  C  CB  . ALA C  1 40  ? 25.822  2.858   27.495  1.00 32.32 ?  64   ALA C CB  1 
ATOM   4756  N  N   . GLY C  1 41  ? 23.273  4.017   28.788  1.00 31.97 ?  65   GLY C N   1 
ATOM   4757  C  CA  . GLY C  1 41  ? 21.966  3.854   29.436  1.00 31.62 ?  65   GLY C CA  1 
ATOM   4758  C  C   . GLY C  1 41  ? 21.553  5.014   30.329  1.00 31.54 ?  65   GLY C C   1 
ATOM   4759  O  O   . GLY C  1 41  ? 22.007  6.149   30.139  1.00 31.64 ?  65   GLY C O   1 
ATOM   4760  N  N   . LYS C  1 42  ? 20.696  4.721   31.309  1.00 31.23 ?  66   LYS C N   1 
ATOM   4761  C  CA  . LYS C  1 42  ? 20.118  5.745   32.189  1.00 31.06 ?  66   LYS C CA  1 
ATOM   4762  C  C   . LYS C  1 42  ? 21.012  6.114   33.376  1.00 31.08 ?  66   LYS C C   1 
ATOM   4763  O  O   . LYS C  1 42  ? 20.791  7.140   34.031  1.00 30.97 ?  66   LYS C O   1 
ATOM   4764  C  CB  . LYS C  1 42  ? 18.734  5.313   32.695  1.00 30.84 ?  66   LYS C CB  1 
ATOM   4765  C  CG  . LYS C  1 42  ? 17.637  5.313   31.633  1.00 30.73 ?  66   LYS C CG  1 
ATOM   4766  C  CD  . LYS C  1 42  ? 16.248  5.105   32.237  1.00 30.33 ?  66   LYS C CD  1 
ATOM   4767  C  CE  . LYS C  1 42  ? 15.764  6.347   32.985  1.00 30.11 ?  66   LYS C CE  1 
ATOM   4768  N  NZ  . LYS C  1 42  ? 14.493  6.113   33.723  1.00 30.23 ?  66   LYS C NZ  1 
ATOM   4769  N  N   . GLY C  1 43  ? 22.006  5.273   33.651  1.00 30.95 ?  67   GLY C N   1 
ATOM   4770  C  CA  . GLY C  1 43  ? 22.954  5.515   34.736  1.00 30.98 ?  67   GLY C CA  1 
ATOM   4771  C  C   . GLY C  1 43  ? 22.497  5.017   36.095  1.00 31.06 ?  67   GLY C C   1 
ATOM   4772  O  O   . GLY C  1 43  ? 21.466  4.352   36.212  1.00 31.32 ?  67   GLY C O   1 
ATOM   4773  N  N   . THR C  1 44  ? 23.268  5.363   37.123  1.00 31.11 ?  68   THR C N   1 
ATOM   4774  C  CA  . THR C  1 44  ? 23.064  4.864   38.487  1.00 31.12 ?  68   THR C CA  1 
ATOM   4775  C  C   . THR C  1 44  ? 21.829  5.440   39.184  1.00 31.16 ?  68   THR C C   1 
ATOM   4776  O  O   . THR C  1 44  ? 21.367  4.891   40.191  1.00 31.27 ?  68   THR C O   1 
ATOM   4777  C  CB  . THR C  1 44  ? 24.300  5.134   39.381  1.00 31.13 ?  68   THR C CB  1 
ATOM   4778  O  OG1 . THR C  1 44  ? 24.435  6.543   39.605  1.00 31.13 ?  68   THR C OG1 1 
ATOM   4779  C  CG2 . THR C  1 44  ? 25.575  4.596   38.735  1.00 31.12 ?  68   THR C CG2 1 
ATOM   4780  N  N   . MET C  1 45  ? 21.300  6.542   38.655  1.00 30.97 ?  69   MET C N   1 
ATOM   4781  C  CA  . MET C  1 45  ? 20.142  7.207   39.259  1.00 30.81 ?  69   MET C CA  1 
ATOM   4782  C  C   . MET C  1 45  ? 18.911  7.211   38.352  1.00 30.76 ?  69   MET C C   1 
ATOM   4783  O  O   . MET C  1 45  ? 18.026  8.061   38.499  1.00 30.69 ?  69   MET C O   1 
ATOM   4784  C  CB  . MET C  1 45  ? 20.507  8.630   39.696  1.00 30.92 ?  69   MET C CB  1 
ATOM   4785  C  CG  . MET C  1 45  ? 21.459  8.680   40.887  1.00 30.67 ?  69   MET C CG  1 
ATOM   4786  S  SD  . MET C  1 45  ? 22.023  10.344  41.271  1.00 31.82 ?  69   MET C SD  1 
ATOM   4787  C  CE  . MET C  1 45  ? 23.157  10.654  39.923  1.00 30.79 ?  69   MET C CE  1 
ATOM   4788  N  N   . GLY C  1 46  ? 18.854  6.240   37.440  1.00 30.52 ?  70   GLY C N   1 
ATOM   4789  C  CA  . GLY C  1 46  ? 17.759  6.110   36.481  1.00 30.47 ?  70   GLY C CA  1 
ATOM   4790  C  C   . GLY C  1 46  ? 16.370  5.866   37.054  1.00 30.51 ?  70   GLY C C   1 
ATOM   4791  O  O   . GLY C  1 46  ? 15.369  6.045   36.355  1.00 30.21 ?  70   GLY C O   1 
ATOM   4792  N  N   . ASP C  1 47  ? 16.302  5.450   38.318  1.00 30.57 ?  71   ASP C N   1 
ATOM   4793  C  CA  . ASP C  1 47  ? 15.015  5.236   38.991  1.00 30.69 ?  71   ASP C CA  1 
ATOM   4794  C  C   . ASP C  1 47  ? 14.408  6.537   39.500  1.00 30.45 ?  71   ASP C C   1 
ATOM   4795  O  O   . ASP C  1 47  ? 13.242  6.575   39.912  1.00 30.44 ?  71   ASP C O   1 
ATOM   4796  C  CB  . ASP C  1 47  ? 15.167  4.245   40.149  1.00 31.02 ?  71   ASP C CB  1 
ATOM   4797  C  CG  . ASP C  1 47  ? 15.405  2.825   39.674  1.00 31.85 ?  71   ASP C CG  1 
ATOM   4798  O  OD1 . ASP C  1 47  ? 14.744  2.398   38.702  1.00 33.16 ?  71   ASP C OD1 1 
ATOM   4799  O  OD2 . ASP C  1 47  ? 16.256  2.136   40.274  1.00 33.36 -1 71   ASP C OD2 1 
ATOM   4800  N  N   . TYR C  1 48  ? 15.202  7.604   39.471  1.00 30.23 ?  72   TYR C N   1 
ATOM   4801  C  CA  . TYR C  1 48  ? 14.769  8.895   39.988  1.00 29.75 ?  72   TYR C CA  1 
ATOM   4802  C  C   . TYR C  1 48  ? 14.216  9.823   38.911  1.00 29.21 ?  72   TYR C C   1 
ATOM   4803  O  O   . TYR C  1 48  ? 13.553  10.810  39.228  1.00 29.21 ?  72   TYR C O   1 
ATOM   4804  C  CB  . TYR C  1 48  ? 15.908  9.563   40.765  1.00 30.05 ?  72   TYR C CB  1 
ATOM   4805  C  CG  . TYR C  1 48  ? 16.263  8.825   42.037  1.00 30.59 ?  72   TYR C CG  1 
ATOM   4806  C  CD1 . TYR C  1 48  ? 17.321  7.914   42.068  1.00 31.07 ?  72   TYR C CD1 1 
ATOM   4807  C  CD2 . TYR C  1 48  ? 15.528  9.024   43.207  1.00 31.26 ?  72   TYR C CD2 1 
ATOM   4808  C  CE1 . TYR C  1 48  ? 17.643  7.225   43.237  1.00 31.76 ?  72   TYR C CE1 1 
ATOM   4809  C  CE2 . TYR C  1 48  ? 15.841  8.341   44.380  1.00 31.63 ?  72   TYR C CE2 1 
ATOM   4810  C  CZ  . TYR C  1 48  ? 16.897  7.445   44.387  1.00 31.71 ?  72   TYR C CZ  1 
ATOM   4811  O  OH  . TYR C  1 48  ? 17.207  6.776   45.546  1.00 32.37 ?  72   TYR C OH  1 
ATOM   4812  N  N   . TRP C  1 49  ? 14.475  9.497   37.645  1.00 28.73 ?  73   TRP C N   1 
ATOM   4813  C  CA  . TRP C  1 49  ? 14.056  10.344  36.525  1.00 28.24 ?  73   TRP C CA  1 
ATOM   4814  C  C   . TRP C  1 49  ? 13.513  9.549   35.338  1.00 28.02 ?  73   TRP C C   1 
ATOM   4815  O  O   . TRP C  1 49  ? 13.854  8.381   35.143  1.00 27.77 ?  73   TRP C O   1 
ATOM   4816  C  CB  . TRP C  1 49  ? 15.202  11.262  36.070  1.00 28.12 ?  73   TRP C CB  1 
ATOM   4817  C  CG  . TRP C  1 49  ? 16.382  10.534  35.472  1.00 27.83 ?  73   TRP C CG  1 
ATOM   4818  C  CD1 . TRP C  1 49  ? 17.460  10.038  36.144  1.00 27.39 ?  73   TRP C CD1 1 
ATOM   4819  C  CD2 . TRP C  1 49  ? 16.602  10.233  34.085  1.00 27.08 ?  73   TRP C CD2 1 
ATOM   4820  N  NE1 . TRP C  1 49  ? 18.335  9.445   35.267  1.00 27.17 ?  73   TRP C NE1 1 
ATOM   4821  C  CE2 . TRP C  1 49  ? 17.833  9.546   33.997  1.00 26.96 ?  73   TRP C CE2 1 
ATOM   4822  C  CE3 . TRP C  1 49  ? 15.878  10.475  32.910  1.00 27.27 ?  73   TRP C CE3 1 
ATOM   4823  C  CZ2 . TRP C  1 49  ? 18.364  9.104   32.780  1.00 26.87 ?  73   TRP C CZ2 1 
ATOM   4824  C  CZ3 . TRP C  1 49  ? 16.404  10.029  31.695  1.00 27.67 ?  73   TRP C CZ3 1 
ATOM   4825  C  CH2 . TRP C  1 49  ? 17.636  9.351   31.644  1.00 27.39 ?  73   TRP C CH2 1 
ATOM   4826  N  N   . GLU C  1 50  ? 12.666  10.209  34.552  1.00 27.83 ?  74   GLU C N   1 
ATOM   4827  C  CA  . GLU C  1 50  ? 12.060  9.627   33.361  1.00 27.79 ?  74   GLU C CA  1 
ATOM   4828  C  C   . GLU C  1 50  ? 12.338  10.535  32.163  1.00 27.53 ?  74   GLU C C   1 
ATOM   4829  O  O   . GLU C  1 50  ? 12.451  11.754  32.326  1.00 27.47 ?  74   GLU C O   1 
ATOM   4830  C  CB  . GLU C  1 50  ? 10.544  9.457   33.550  1.00 28.01 ?  74   GLU C CB  1 
ATOM   4831  C  CG  . GLU C  1 50  ? 10.134  8.364   34.556  1.00 28.92 ?  74   GLU C CG  1 
ATOM   4832  C  CD  . GLU C  1 50  ? 10.408  8.756   35.994  1.00 30.02 ?  74   GLU C CD  1 
ATOM   4833  O  OE1 . GLU C  1 50  ? 9.955   9.840   36.414  1.00 30.74 ?  74   GLU C OE1 1 
ATOM   4834  O  OE2 . GLU C  1 50  ? 11.086  7.985   36.704  1.00 31.27 -1 74   GLU C OE2 1 
ATOM   4835  N  N   . PRO C  1 51  ? 12.445  9.948   30.956  1.00 27.14 ?  75   PRO C N   1 
ATOM   4836  C  CA  . PRO C  1 51  ? 12.652  10.743  29.746  1.00 26.88 ?  75   PRO C CA  1 
ATOM   4837  C  C   . PRO C  1 51  ? 11.477  11.672  29.459  1.00 26.51 ?  75   PRO C C   1 
ATOM   4838  O  O   . PRO C  1 51  ? 10.349  11.392  29.867  1.00 26.49 ?  75   PRO C O   1 
ATOM   4839  C  CB  . PRO C  1 51  ? 12.739  9.680   28.644  1.00 27.08 ?  75   PRO C CB  1 
ATOM   4840  C  CG  . PRO C  1 51  ? 11.983  8.500   29.195  1.00 27.13 ?  75   PRO C CG  1 
ATOM   4841  C  CD  . PRO C  1 51  ? 12.350  8.508   30.649  1.00 27.19 ?  75   PRO C CD  1 
ATOM   4842  N  N   . ILE C  1 52  ? 11.749  12.775  28.772  1.00 26.08 ?  76   ILE C N   1 
ATOM   4843  C  CA  . ILE C  1 52  ? 10.686  13.602  28.205  1.00 25.56 ?  76   ILE C CA  1 
ATOM   4844  C  C   . ILE C  1 52  ? 10.704  13.437  26.687  1.00 25.30 ?  76   ILE C C   1 
ATOM   4845  O  O   . ILE C  1 52  ? 11.506  12.659  26.167  1.00 25.05 ?  76   ILE C O   1 
ATOM   4846  C  CB  . ILE C  1 52  ? 10.781  15.086  28.646  1.00 25.63 ?  76   ILE C CB  1 
ATOM   4847  C  CG1 . ILE C  1 52  ? 12.128  15.708  28.242  1.00 25.61 ?  76   ILE C CG1 1 
ATOM   4848  C  CG2 . ILE C  1 52  ? 10.519  15.202  30.155  1.00 25.49 ?  76   ILE C CG2 1 
ATOM   4849  C  CD1 . ILE C  1 52  ? 12.185  17.231  28.410  1.00 25.70 ?  76   ILE C CD1 1 
ATOM   4850  N  N   . ALA C  1 53  ? 9.826   14.147  25.979  1.00 25.00 ?  77   ALA C N   1 
ATOM   4851  C  CA  . ALA C  1 53  ? 9.656   13.925  24.539  1.00 24.86 ?  77   ALA C CA  1 
ATOM   4852  C  C   . ALA C  1 53  ? 10.956  14.096  23.740  1.00 24.94 ?  77   ALA C C   1 
ATOM   4853  O  O   . ALA C  1 53  ? 11.268  13.278  22.872  1.00 24.79 ?  77   ALA C O   1 
ATOM   4854  C  CB  . ALA C  1 53  ? 8.553   14.810  23.981  1.00 24.90 ?  77   ALA C CB  1 
ATOM   4855  N  N   . ILE C  1 54  ? 11.712  15.151  24.051  1.00 24.79 ?  78   ILE C N   1 
ATOM   4856  C  CA  . ILE C  1 54  ? 12.961  15.446  23.349  1.00 24.58 ?  78   ILE C CA  1 
ATOM   4857  C  C   . ILE C  1 54  ? 14.069  14.419  23.637  1.00 24.61 ?  78   ILE C C   1 
ATOM   4858  O  O   . ILE C  1 54  ? 14.978  14.248  22.821  1.00 24.42 ?  78   ILE C O   1 
ATOM   4859  C  CB  . ILE C  1 54  ? 13.453  16.910  23.621  1.00 24.72 ?  78   ILE C CB  1 
ATOM   4860  C  CG1 . ILE C  1 54  ? 14.348  17.423  22.485  1.00 24.35 ?  78   ILE C CG1 1 
ATOM   4861  C  CG2 . ILE C  1 54  ? 14.152  17.029  24.981  1.00 24.30 ?  78   ILE C CG2 1 
ATOM   4862  C  CD1 . ILE C  1 54  ? 13.596  17.859  21.245  1.00 25.20 ?  78   ILE C CD1 1 
ATOM   4863  N  N   . SER C  1 55  ? 13.971  13.726  24.777  1.00 24.56 ?  79   SER C N   1 
ATOM   4864  C  CA  . SER C  1 55  ? 14.987  12.748  25.205  1.00 24.61 ?  79   SER C CA  1 
ATOM   4865  C  C   . SER C  1 55  ? 15.289  11.650  24.179  1.00 24.64 ?  79   SER C C   1 
ATOM   4866  O  O   . SER C  1 55  ? 16.370  11.056  24.206  1.00 24.36 ?  79   SER C O   1 
ATOM   4867  C  CB  . SER C  1 55  ? 14.600  12.100  26.537  1.00 24.49 ?  79   SER C CB  1 
ATOM   4868  O  OG  . SER C  1 55  ? 14.391  13.074  27.544  1.00 24.92 ?  79   SER C OG  1 
ATOM   4869  N  N   . ILE C  1 56  ? 14.340  11.386  23.281  1.00 24.69 ?  80   ILE C N   1 
ATOM   4870  C  CA  . ILE C  1 56  ? 14.529  10.354  22.250  1.00 24.87 ?  80   ILE C CA  1 
ATOM   4871  C  C   . ILE C  1 56  ? 15.599  10.753  21.221  1.00 24.77 ?  80   ILE C C   1 
ATOM   4872  O  O   . ILE C  1 56  ? 16.210  9.892   20.580  1.00 24.74 ?  80   ILE C O   1 
ATOM   4873  C  CB  . ILE C  1 56  ? 13.187  9.933   21.559  1.00 24.83 ?  80   ILE C CB  1 
ATOM   4874  C  CG1 . ILE C  1 56  ? 12.628  11.059  20.683  1.00 24.90 ?  80   ILE C CG1 1 
ATOM   4875  C  CG2 . ILE C  1 56  ? 12.154  9.485   22.605  1.00 24.86 ?  80   ILE C CG2 1 
ATOM   4876  C  CD1 . ILE C  1 56  ? 11.538  10.616  19.719  1.00 24.87 ?  80   ILE C CD1 1 
ATOM   4877  N  N   . TYR C  1 57  ? 15.825  12.059  21.083  1.00 24.69 ?  81   TYR C N   1 
ATOM   4878  C  CA  . TYR C  1 57  ? 16.876  12.576  20.205  1.00 24.66 ?  81   TYR C CA  1 
ATOM   4879  C  C   . TYR C  1 57  ? 18.182  12.812  20.969  1.00 24.83 ?  81   TYR C C   1 
ATOM   4880  O  O   . TYR C  1 57  ? 19.262  12.836  20.373  1.00 24.52 ?  81   TYR C O   1 
ATOM   4881  C  CB  . TYR C  1 57  ? 16.416  13.855  19.492  1.00 24.50 ?  81   TYR C CB  1 
ATOM   4882  C  CG  . TYR C  1 57  ? 15.104  13.694  18.749  1.00 24.21 ?  81   TYR C CG  1 
ATOM   4883  C  CD1 . TYR C  1 57  ? 15.058  13.077  17.491  1.00 23.52 ?  81   TYR C CD1 1 
ATOM   4884  C  CD2 . TYR C  1 57  ? 13.908  14.146  19.308  1.00 23.11 ?  81   TYR C CD2 1 
ATOM   4885  C  CE1 . TYR C  1 57  ? 13.846  12.921  16.809  1.00 23.56 ?  81   TYR C CE1 1 
ATOM   4886  C  CE2 . TYR C  1 57  ? 12.695  13.998  18.636  1.00 23.42 ?  81   TYR C CE2 1 
ATOM   4887  C  CZ  . TYR C  1 57  ? 12.669  13.383  17.391  1.00 23.56 ?  81   TYR C CZ  1 
ATOM   4888  O  OH  . TYR C  1 57  ? 11.466  13.236  16.734  1.00 22.75 ?  81   TYR C OH  1 
ATOM   4889  N  N   . MET C  1 58  ? 18.072  12.966  22.288  1.00 25.00 ?  82   MET C N   1 
ATOM   4890  C  CA  . MET C  1 58  ? 19.226  13.245  23.141  1.00 25.68 ?  82   MET C CA  1 
ATOM   4891  C  C   . MET C  1 58  ? 19.997  11.973  23.471  1.00 25.93 ?  82   MET C C   1 
ATOM   4892  O  O   . MET C  1 58  ? 21.224  11.956  23.394  1.00 25.96 ?  82   MET C O   1 
ATOM   4893  C  CB  . MET C  1 58  ? 18.802  13.971  24.426  1.00 25.63 ?  82   MET C CB  1 
ATOM   4894  C  CG  . MET C  1 58  ? 18.131  15.329  24.210  1.00 25.55 ?  82   MET C CG  1 
ATOM   4895  S  SD  . MET C  1 58  ? 19.189  16.597  23.475  1.00 25.73 ?  82   MET C SD  1 
ATOM   4896  C  CE  . MET C  1 58  ? 18.761  16.503  21.739  1.00 25.91 ?  82   MET C CE  1 
ATOM   4897  N  N   . ASP C  1 59  ? 19.272  10.919  23.849  1.00 26.23 ?  83   ASP C N   1 
ATOM   4898  C  CA  . ASP C  1 59  ? 19.860  9.592   24.043  1.00 26.41 ?  83   ASP C CA  1 
ATOM   4899  C  C   . ASP C  1 59  ? 19.087  8.549   23.226  1.00 26.56 ?  83   ASP C C   1 
ATOM   4900  O  O   . ASP C  1 59  ? 18.275  7.807   23.780  1.00 26.60 ?  83   ASP C O   1 
ATOM   4901  C  CB  . ASP C  1 59  ? 19.894  9.217   25.533  1.00 26.23 ?  83   ASP C CB  1 
ATOM   4902  C  CG  . ASP C  1 59  ? 20.648  7.912   25.803  1.00 26.28 ?  83   ASP C CG  1 
ATOM   4903  O  OD1 . ASP C  1 59  ? 21.229  7.327   24.862  1.00 25.59 ?  83   ASP C OD1 1 
ATOM   4904  O  OD2 . ASP C  1 59  ? 20.659  7.469   26.969  1.00 26.23 -1 83   ASP C OD2 1 
ATOM   4905  N  N   . PRO C  1 60  ? 19.336  8.495   21.900  1.00 26.89 ?  84   PRO C N   1 
ATOM   4906  C  CA  . PRO C  1 60  ? 18.604  7.584   21.016  1.00 27.16 ?  84   PRO C CA  1 
ATOM   4907  C  C   . PRO C  1 60  ? 18.779  6.092   21.326  1.00 27.62 ?  84   PRO C C   1 
ATOM   4908  O  O   . PRO C  1 60  ? 17.822  5.331   21.185  1.00 27.61 ?  84   PRO C O   1 
ATOM   4909  C  CB  . PRO C  1 60  ? 19.171  7.909   19.630  1.00 27.10 ?  84   PRO C CB  1 
ATOM   4910  C  CG  . PRO C  1 60  ? 19.683  9.287   19.751  1.00 26.77 ?  84   PRO C CG  1 
ATOM   4911  C  CD  . PRO C  1 60  ? 20.238  9.373   21.131  1.00 26.76 ?  84   PRO C CD  1 
ATOM   4912  N  N   . ASN C  1 61  ? 19.974  5.675   21.745  1.00 28.00 ?  85   ASN C N   1 
ATOM   4913  C  CA  . ASN C  1 61  ? 20.204  4.256   22.045  1.00 28.61 ?  85   ASN C CA  1 
ATOM   4914  C  C   . ASN C  1 61  ? 19.377  3.730   23.219  1.00 28.70 ?  85   ASN C C   1 
ATOM   4915  O  O   . ASN C  1 61  ? 19.011  2.555   23.244  1.00 28.76 ?  85   ASN C O   1 
ATOM   4916  C  CB  . ASN C  1 61  ? 21.693  3.950   22.239  1.00 28.73 ?  85   ASN C CB  1 
ATOM   4917  C  CG  . ASN C  1 61  ? 22.450  3.873   20.920  1.00 29.46 ?  85   ASN C CG  1 
ATOM   4918  O  OD1 . ASN C  1 61  ? 21.883  3.527   19.877  1.00 30.00 ?  85   ASN C OD1 1 
ATOM   4919  N  ND2 . ASN C  1 61  ? 23.740  4.195   20.960  1.00 29.89 ?  85   ASN C ND2 1 
ATOM   4920  N  N   . THR C  1 62  ? 19.071  4.606   24.174  1.00 28.81 ?  86   THR C N   1 
ATOM   4921  C  CA  . THR C  1 62  ? 18.230  4.237   25.311  1.00 28.89 ?  86   THR C CA  1 
ATOM   4922  C  C   . THR C  1 62  ? 16.739  4.456   25.023  1.00 29.04 ?  86   THR C C   1 
ATOM   4923  O  O   . THR C  1 62  ? 15.904  3.633   25.406  1.00 28.95 ?  86   THR C O   1 
ATOM   4924  C  CB  . THR C  1 62  ? 18.648  4.995   26.603  1.00 29.00 ?  86   THR C CB  1 
ATOM   4925  O  OG1 . THR C  1 62  ? 20.050  4.814   26.830  1.00 28.69 ?  86   THR C OG1 1 
ATOM   4926  C  CG2 . THR C  1 62  ? 17.884  4.484   27.827  1.00 29.01 ?  86   THR C CG2 1 
ATOM   4927  N  N   . PHE C  1 63  ? 16.409  5.540   24.321  1.00 29.17 ?  87   PHE C N   1 
ATOM   4928  C  CA  . PHE C  1 63  ? 15.021  6.002   24.275  1.00 29.37 ?  87   PHE C CA  1 
ATOM   4929  C  C   . PHE C  1 63  ? 14.310  6.006   22.919  1.00 29.53 ?  87   PHE C C   1 
ATOM   4930  O  O   . PHE C  1 63  ? 13.079  6.068   22.882  1.00 29.40 ?  87   PHE C O   1 
ATOM   4931  C  CB  . PHE C  1 63  ? 14.893  7.382   24.938  1.00 29.23 ?  87   PHE C CB  1 
ATOM   4932  C  CG  . PHE C  1 63  ? 15.266  7.394   26.396  1.00 29.21 ?  87   PHE C CG  1 
ATOM   4933  C  CD1 . PHE C  1 63  ? 14.620  6.556   27.304  1.00 29.21 ?  87   PHE C CD1 1 
ATOM   4934  C  CD2 . PHE C  1 63  ? 16.257  8.252   26.865  1.00 29.20 ?  87   PHE C CD2 1 
ATOM   4935  C  CE1 . PHE C  1 63  ? 14.965  6.565   28.656  1.00 28.92 ?  87   PHE C CE1 1 
ATOM   4936  C  CE2 . PHE C  1 63  ? 16.608  8.271   28.215  1.00 28.54 ?  87   PHE C CE2 1 
ATOM   4937  C  CZ  . PHE C  1 63  ? 15.961  7.426   29.109  1.00 28.95 ?  87   PHE C CZ  1 
ATOM   4938  N  N   . TYR C  1 64  ? 15.056  5.942   21.817  1.00 29.83 ?  88   TYR C N   1 
ATOM   4939  C  CA  . TYR C  1 64  ? 14.428  6.114   20.506  1.00 30.26 ?  88   TYR C CA  1 
ATOM   4940  C  C   . TYR C  1 64  ? 13.699  4.887   19.967  1.00 30.97 ?  88   TYR C C   1 
ATOM   4941  O  O   . TYR C  1 64  ? 14.216  3.770   19.993  1.00 31.05 ?  88   TYR C O   1 
ATOM   4942  C  CB  . TYR C  1 64  ? 15.399  6.655   19.447  1.00 29.99 ?  88   TYR C CB  1 
ATOM   4943  C  CG  . TYR C  1 64  ? 14.695  7.016   18.150  1.00 28.97 ?  88   TYR C CG  1 
ATOM   4944  C  CD1 . TYR C  1 64  ? 14.023  8.233   18.014  1.00 28.25 ?  88   TYR C CD1 1 
ATOM   4945  C  CD2 . TYR C  1 64  ? 14.669  6.126   17.073  1.00 27.92 ?  88   TYR C CD2 1 
ATOM   4946  C  CE1 . TYR C  1 64  ? 13.356  8.559   16.832  1.00 27.59 ?  88   TYR C CE1 1 
ATOM   4947  C  CE2 . TYR C  1 64  ? 14.009  6.443   15.890  1.00 27.26 ?  88   TYR C CE2 1 
ATOM   4948  C  CZ  . TYR C  1 64  ? 13.357  7.660   15.776  1.00 27.51 ?  88   TYR C CZ  1 
ATOM   4949  O  OH  . TYR C  1 64  ? 12.707  7.976   14.603  1.00 27.73 ?  88   TYR C OH  1 
ATOM   4950  N  N   . LYS C  1 65  ? 12.486  5.135   19.484  1.00 31.78 ?  89   LYS C N   1 
ATOM   4951  C  CA  . LYS C  1 65  ? 11.740  4.203   18.655  1.00 32.66 ?  89   LYS C CA  1 
ATOM   4952  C  C   . LYS C  1 65  ? 11.092  5.019   17.540  1.00 33.04 ?  89   LYS C C   1 
ATOM   4953  O  O   . LYS C  1 65  ? 10.607  6.123   17.790  1.00 33.17 ?  89   LYS C O   1 
ATOM   4954  C  CB  . LYS C  1 65  ? 10.688  3.450   19.479  1.00 32.79 ?  89   LYS C CB  1 
ATOM   4955  C  CG  . LYS C  1 65  ? 11.186  2.134   20.085  1.00 33.74 ?  89   LYS C CG  1 
ATOM   4956  C  CD  . LYS C  1 65  ? 11.009  0.963   19.108  1.00 36.08 ?  89   LYS C CD  1 
ATOM   4957  C  CE  . LYS C  1 65  ? 11.530  -0.359  19.681  1.00 36.84 ?  89   LYS C CE  1 
ATOM   4958  N  NZ  . LYS C  1 65  ? 13.020  -0.469  19.592  1.00 37.42 ?  89   LYS C NZ  1 
ATOM   4959  N  N   . PRO C  1 66  ? 11.103  4.495   16.300  1.00 33.54 ?  90   PRO C N   1 
ATOM   4960  C  CA  . PRO C  1 66  ? 10.533  5.208   15.152  1.00 33.96 ?  90   PRO C CA  1 
ATOM   4961  C  C   . PRO C  1 66  ? 9.043   5.546   15.340  1.00 34.51 ?  90   PRO C C   1 
ATOM   4962  O  O   . PRO C  1 66  ? 8.375   4.918   16.161  1.00 34.32 ?  90   PRO C O   1 
ATOM   4963  C  CB  . PRO C  1 66  ? 10.739  4.229   13.986  1.00 34.08 ?  90   PRO C CB  1 
ATOM   4964  C  CG  . PRO C  1 66  ? 11.031  2.908   14.615  1.00 33.87 ?  90   PRO C CG  1 
ATOM   4965  C  CD  . PRO C  1 66  ? 11.705  3.210   15.905  1.00 33.56 ?  90   PRO C CD  1 
ATOM   4966  N  N   . PRO C  1 67  ? 8.527   6.544   14.593  1.00 35.00 ?  91   PRO C N   1 
ATOM   4967  C  CA  . PRO C  1 67  ? 7.139   6.965   14.789  1.00 35.48 ?  91   PRO C CA  1 
ATOM   4968  C  C   . PRO C  1 67  ? 6.132   5.952   14.239  1.00 35.98 ?  91   PRO C C   1 
ATOM   4969  O  O   . PRO C  1 67  ? 6.421   5.258   13.259  1.00 35.89 ?  91   PRO C O   1 
ATOM   4970  C  CB  . PRO C  1 67  ? 7.047   8.283   14.000  1.00 35.46 ?  91   PRO C CB  1 
ATOM   4971  C  CG  . PRO C  1 67  ? 8.425   8.569   13.482  1.00 35.26 ?  91   PRO C CG  1 
ATOM   4972  C  CD  . PRO C  1 67  ? 9.161   7.276   13.484  1.00 35.12 ?  91   PRO C CD  1 
ATOM   4973  N  N   . VAL C  1 68  ? 4.960   5.884   14.872  1.00 36.59 ?  92   VAL C N   1 
ATOM   4974  C  CA  . VAL C  1 68  ? 3.879   4.973   14.467  1.00 37.22 ?  92   VAL C CA  1 
ATOM   4975  C  C   . VAL C  1 68  ? 3.295   5.336   13.100  1.00 37.62 ?  92   VAL C C   1 
ATOM   4976  O  O   . VAL C  1 68  ? 2.594   4.531   12.478  1.00 37.69 ?  92   VAL C O   1 
ATOM   4977  C  CB  . VAL C  1 68  ? 2.731   4.923   15.519  1.00 37.25 ?  92   VAL C CB  1 
ATOM   4978  C  CG1 . VAL C  1 68  ? 3.231   4.346   16.840  1.00 37.60 ?  92   VAL C CG1 1 
ATOM   4979  C  CG2 . VAL C  1 68  ? 2.108   6.306   15.730  1.00 37.56 ?  92   VAL C CG2 1 
ATOM   4980  N  N   . SER C  1 69  ? 3.596   6.552   12.649  1.00 37.98 ?  93   SER C N   1 
ATOM   4981  C  CA  . SER C  1 69  ? 3.098   7.087   11.390  1.00 38.45 ?  93   SER C CA  1 
ATOM   4982  C  C   . SER C  1 69  ? 4.198   7.947   10.750  1.00 38.77 ?  93   SER C C   1 
ATOM   4983  O  O   . SER C  1 69  ? 4.869   8.709   11.450  1.00 38.90 ?  93   SER C O   1 
ATOM   4984  C  CB  . SER C  1 69  ? 1.834   7.913   11.649  1.00 38.34 ?  93   SER C CB  1 
ATOM   4985  O  OG  . SER C  1 69  ? 1.290   8.430   10.450  1.00 38.94 ?  93   SER C OG  1 
ATOM   4986  N  N   . PRO C  1 70  ? 4.388   7.840   9.419   1.00 39.17 ?  94   PRO C N   1 
ATOM   4987  C  CA  . PRO C  1 70  ? 3.590   7.088   8.450   1.00 39.50 ?  94   PRO C CA  1 
ATOM   4988  C  C   . PRO C  1 70  ? 3.930   5.598   8.373   1.00 39.88 ?  94   PRO C C   1 
ATOM   4989  O  O   . PRO C  1 70  ? 5.074   5.197   8.606   1.00 39.64 ?  94   PRO C O   1 
ATOM   4990  C  CB  . PRO C  1 70  ? 3.932   7.771   7.126   1.00 39.47 ?  94   PRO C CB  1 
ATOM   4991  C  CG  . PRO C  1 70  ? 5.339   8.226   7.303   1.00 39.26 ?  94   PRO C CG  1 
ATOM   4992  C  CD  . PRO C  1 70  ? 5.537   8.505   8.773   1.00 39.14 ?  94   PRO C CD  1 
ATOM   4993  N  N   . LYS C  1 71  ? 2.917   4.798   8.053   1.00 40.43 ?  95   LYS C N   1 
ATOM   4994  C  CA  . LYS C  1 71  ? 3.086   3.372   7.825   1.00 41.02 ?  95   LYS C CA  1 
ATOM   4995  C  C   . LYS C  1 71  ? 3.540   3.204   6.378   1.00 41.22 ?  95   LYS C C   1 
ATOM   4996  O  O   . LYS C  1 71  ? 2.722   3.077   5.463   1.00 41.64 ?  95   LYS C O   1 
ATOM   4997  C  CB  . LYS C  1 71  ? 1.773   2.625   8.103   1.00 41.18 ?  95   LYS C CB  1 
ATOM   4998  C  CG  . LYS C  1 71  ? 1.194   2.879   9.501   1.00 41.73 ?  95   LYS C CG  1 
ATOM   4999  C  CD  . LYS C  1 71  ? -0.305  2.608   9.547   1.00 42.86 ?  95   LYS C CD  1 
ATOM   5000  C  CE  . LYS C  1 71  ? -0.992  3.396   10.661  1.00 43.53 ?  95   LYS C CE  1 
ATOM   5001  N  NZ  . LYS C  1 71  ? -0.773  2.811   12.016  1.00 44.20 ?  95   LYS C NZ  1 
ATOM   5002  N  N   . GLU C  1 72  ? 4.855   3.234   6.183   1.00 41.27 ?  96   GLU C N   1 
ATOM   5003  C  CA  . GLU C  1 72  ? 5.451   3.241   4.852   1.00 41.26 ?  96   GLU C CA  1 
ATOM   5004  C  C   . GLU C  1 72  ? 6.618   2.266   4.737   1.00 40.94 ?  96   GLU C C   1 
ATOM   5005  O  O   . GLU C  1 72  ? 7.501   2.229   5.599   1.00 41.11 ?  96   GLU C O   1 
ATOM   5006  C  CB  . GLU C  1 72  ? 5.933   4.653   4.498   1.00 41.53 ?  96   GLU C CB  1 
ATOM   5007  C  CG  . GLU C  1 72  ? 4.835   5.623   4.061   1.00 42.51 ?  96   GLU C CG  1 
ATOM   5008  C  CD  . GLU C  1 72  ? 4.355   5.375   2.642   1.00 43.74 ?  96   GLU C CD  1 
ATOM   5009  O  OE1 . GLU C  1 72  ? 5.201   5.125   1.756   1.00 44.89 ?  96   GLU C OE1 1 
ATOM   5010  O  OE2 . GLU C  1 72  ? 3.129   5.438   2.408   1.00 44.66 -1 96   GLU C OE2 1 
ATOM   5011  N  N   . VAL C  1 73  ? 6.604   1.473   3.671   1.00 40.46 ?  97   VAL C N   1 
ATOM   5012  C  CA  . VAL C  1 73  ? 7.762   0.675   3.279   1.00 39.89 ?  97   VAL C CA  1 
ATOM   5013  C  C   . VAL C  1 73  ? 8.430   1.423   2.125   1.00 39.42 ?  97   VAL C C   1 
ATOM   5014  O  O   . VAL C  1 73  ? 7.779   1.731   1.124   1.00 39.46 ?  97   VAL C O   1 
ATOM   5015  C  CB  . VAL C  1 73  ? 7.363   -0.765  2.873   1.00 39.96 ?  97   VAL C CB  1 
ATOM   5016  C  CG1 . VAL C  1 73  ? 8.576   -1.551  2.403   1.00 39.98 ?  97   VAL C CG1 1 
ATOM   5017  C  CG2 . VAL C  1 73  ? 6.697   -1.486  4.041   1.00 39.81 ?  97   VAL C CG2 1 
ATOM   5018  N  N   . ALA C  1 74  ? 9.717   1.731   2.275   1.00 38.66 ?  98   ALA C N   1 
ATOM   5019  C  CA  . ALA C  1 74  ? 10.389  2.656   1.361   1.00 38.17 ?  98   ALA C CA  1 
ATOM   5020  C  C   . ALA C  1 74  ? 11.781  2.217   0.910   1.00 37.81 ?  98   ALA C C   1 
ATOM   5021  O  O   . ALA C  1 74  ? 12.528  1.585   1.662   1.00 37.67 ?  98   ALA C O   1 
ATOM   5022  C  CB  . ALA C  1 74  ? 10.453  4.051   1.980   1.00 38.08 ?  98   ALA C CB  1 
ATOM   5023  N  N   . GLU C  1 75  ? 12.115  2.577   -0.325  1.00 37.39 ?  99   GLU C N   1 
ATOM   5024  C  CA  . GLU C  1 75  ? 13.458  2.384   -0.863  1.00 37.05 ?  99   GLU C CA  1 
ATOM   5025  C  C   . GLU C  1 75  ? 14.275  3.674   -0.735  1.00 36.62 ?  99   GLU C C   1 
ATOM   5026  O  O   . GLU C  1 75  ? 13.730  4.729   -0.389  1.00 36.46 ?  99   GLU C O   1 
ATOM   5027  C  CB  . GLU C  1 75  ? 13.384  1.928   -2.324  1.00 37.10 ?  99   GLU C CB  1 
ATOM   5028  C  CG  . GLU C  1 75  ? 12.926  0.484   -2.490  1.00 37.74 ?  99   GLU C CG  1 
ATOM   5029  C  CD  . GLU C  1 75  ? 12.544  0.126   -3.915  1.00 38.71 ?  99   GLU C CD  1 
ATOM   5030  O  OE1 . GLU C  1 75  ? 12.502  -1.084  -4.223  1.00 39.50 ?  99   GLU C OE1 1 
ATOM   5031  O  OE2 . GLU C  1 75  ? 12.274  1.041   -4.724  1.00 39.48 -1 99   GLU C OE2 1 
ATOM   5032  N  N   . ARG C  1 76  ? 15.577  3.572   -1.011  1.00 36.07 ?  100  ARG C N   1 
ATOM   5033  C  CA  . ARG C  1 76  ? 16.518  4.698   -0.963  1.00 35.39 ?  100  ARG C CA  1 
ATOM   5034  C  C   . ARG C  1 76  ? 15.976  5.979   -1.616  1.00 35.23 ?  100  ARG C C   1 
ATOM   5035  O  O   . ARG C  1 76  ? 16.032  7.057   -1.017  1.00 35.01 ?  100  ARG C O   1 
ATOM   5036  C  CB  . ARG C  1 76  ? 17.852  4.285   -1.607  1.00 35.31 ?  100  ARG C CB  1 
ATOM   5037  C  CG  . ARG C  1 76  ? 18.880  5.405   -1.779  1.00 34.53 ?  100  ARG C CG  1 
ATOM   5038  C  CD  . ARG C  1 76  ? 20.179  4.886   -2.391  1.00 33.39 ?  100  ARG C CD  1 
ATOM   5039  N  NE  . ARG C  1 76  ? 20.809  3.879   -1.538  1.00 32.87 ?  100  ARG C NE  1 
ATOM   5040  C  CZ  . ARG C  1 76  ? 21.684  4.141   -0.570  1.00 32.39 ?  100  ARG C CZ  1 
ATOM   5041  N  NH1 . ARG C  1 76  ? 22.057  5.391   -0.317  1.00 31.75 ?  100  ARG C NH1 1 
ATOM   5042  N  NH2 . ARG C  1 76  ? 22.187  3.146   0.149   1.00 32.07 ?  100  ARG C NH2 1 
ATOM   5043  N  N   . LYS C  1 77  ? 15.450  5.847   -2.834  1.00 34.89 ?  101  LYS C N   1 
ATOM   5044  C  CA  . LYS C  1 77  ? 14.932  6.986   -3.602  1.00 34.63 ?  101  LYS C CA  1 
ATOM   5045  C  C   . LYS C  1 77  ? 13.676  7.608   -2.973  1.00 34.12 ?  101  LYS C C   1 
ATOM   5046  O  O   . LYS C  1 77  ? 13.462  8.819   -3.074  1.00 33.94 ?  101  LYS C O   1 
ATOM   5047  C  CB  . LYS C  1 77  ? 14.651  6.570   -5.053  1.00 34.68 ?  101  LYS C CB  1 
ATOM   5048  C  CG  . LYS C  1 77  ? 14.262  7.726   -5.975  1.00 35.78 ?  101  LYS C CG  1 
ATOM   5049  C  CD  . LYS C  1 77  ? 13.686  7.241   -7.303  1.00 36.76 ?  101  LYS C CD  1 
ATOM   5050  C  CE  . LYS C  1 77  ? 14.781  6.891   -8.303  1.00 37.34 ?  101  LYS C CE  1 
ATOM   5051  N  NZ  . LYS C  1 77  ? 14.234  6.116   -9.452  1.00 37.98 ?  101  LYS C NZ  1 
ATOM   5052  N  N   . ASP C  1 78  ? 12.857  6.772   -2.332  1.00 33.46 ?  102  ASP C N   1 
ATOM   5053  C  CA  . ASP C  1 78  ? 11.618  7.219   -1.690  1.00 32.92 ?  102  ASP C CA  1 
ATOM   5054  C  C   . ASP C  1 78  ? 11.873  8.169   -0.517  1.00 32.57 ?  102  ASP C C   1 
ATOM   5055  O  O   . ASP C  1 78  ? 11.115  9.124   -0.319  1.00 32.30 ?  102  ASP C O   1 
ATOM   5056  C  CB  . ASP C  1 78  ? 10.782  6.021   -1.227  1.00 32.99 ?  102  ASP C CB  1 
ATOM   5057  C  CG  . ASP C  1 78  ? 10.422  5.078   -2.365  1.00 33.10 ?  102  ASP C CG  1 
ATOM   5058  O  OD1 . ASP C  1 78  ? 10.175  5.553   -3.495  1.00 33.09 ?  102  ASP C OD1 1 
ATOM   5059  O  OD2 . ASP C  1 78  ? 10.385  3.853   -2.124  1.00 33.91 -1 102  ASP C OD2 1 
ATOM   5060  N  N   . CYS C  1 79  ? 12.934  7.891   0.249   1.00 32.08 ?  103  CYS C N   1 
ATOM   5061  C  CA  . CYS C  1 79  ? 13.391  8.763   1.333   1.00 31.56 ?  103  CYS C CA  1 
ATOM   5062  C  C   . CYS C  1 79  ? 13.515  10.201  0.837   1.00 31.61 ?  103  CYS C C   1 
ATOM   5063  O  O   . CYS C  1 79  ? 12.907  11.118  1.396   1.00 31.60 ?  103  CYS C O   1 
ATOM   5064  C  CB  . CYS C  1 79  ? 14.758  8.309   1.864   1.00 31.50 ?  103  CYS C CB  1 
ATOM   5065  S  SG  . CYS C  1 79  ? 14.905  6.590   2.411   1.00 30.10 ?  103  CYS C SG  1 
ATOM   5066  N  N   . VAL C  1 80  ? 14.299  10.368  -0.228  1.00 31.48 ?  104  VAL C N   1 
ATOM   5067  C  CA  . VAL C  1 80  ? 14.607  11.668  -0.820  1.00 31.48 ?  104  VAL C CA  1 
ATOM   5068  C  C   . VAL C  1 80  ? 13.372  12.361  -1.398  1.00 31.48 ?  104  VAL C C   1 
ATOM   5069  O  O   . VAL C  1 80  ? 13.177  13.561  -1.192  1.00 31.45 ?  104  VAL C O   1 
ATOM   5070  C  CB  . VAL C  1 80  ? 15.696  11.534  -1.923  1.00 31.44 ?  104  VAL C CB  1 
ATOM   5071  C  CG1 . VAL C  1 80  ? 16.079  12.900  -2.495  1.00 31.20 ?  104  VAL C CG1 1 
ATOM   5072  C  CG2 . VAL C  1 80  ? 16.930  10.821  -1.374  1.00 31.62 ?  104  VAL C CG2 1 
ATOM   5073  N  N   . GLU C  1 81  ? 12.544  11.597  -2.110  1.00 31.41 ?  105  GLU C N   1 
ATOM   5074  C  CA  . GLU C  1 81  ? 11.392  12.148  -2.828  1.00 31.48 ?  105  GLU C CA  1 
ATOM   5075  C  C   . GLU C  1 81  ? 10.280  12.667  -1.914  1.00 30.89 ?  105  GLU C C   1 
ATOM   5076  O  O   . GLU C  1 81  ? 9.803   13.787  -2.093  1.00 30.77 ?  105  GLU C O   1 
ATOM   5077  C  CB  . GLU C  1 81  ? 10.833  11.124  -3.819  1.00 31.77 ?  105  GLU C CB  1 
ATOM   5078  C  CG  . GLU C  1 81  ? 11.725  10.900  -5.029  1.00 33.35 ?  105  GLU C CG  1 
ATOM   5079  C  CD  . GLU C  1 81  ? 11.030  10.147  -6.149  1.00 35.50 ?  105  GLU C CD  1 
ATOM   5080  O  OE1 . GLU C  1 81  ? 11.508  10.240  -7.300  1.00 36.22 ?  105  GLU C OE1 1 
ATOM   5081  O  OE2 . GLU C  1 81  ? 10.012  9.466   -5.885  1.00 36.75 -1 105  GLU C OE2 1 
ATOM   5082  N  N   . CYS C  1 82  ? 9.879   11.854  -0.940  1.00 30.49 ?  106  CYS C N   1 
ATOM   5083  C  CA  . CYS C  1 82  ? 8.815   12.229  -0.009  1.00 30.15 ?  106  CYS C CA  1 
ATOM   5084  C  C   . CYS C  1 82  ? 9.262   13.319  0.970   1.00 29.97 ?  106  CYS C C   1 
ATOM   5085  O  O   . CYS C  1 82  ? 8.519   14.269  1.226   1.00 29.84 ?  106  CYS C O   1 
ATOM   5086  C  CB  . CYS C  1 82  ? 8.306   10.996  0.738   1.00 30.16 ?  106  CYS C CB  1 
ATOM   5087  S  SG  . CYS C  1 82  ? 6.998   11.293  1.962   1.00 29.92 ?  106  CYS C SG  1 
ATOM   5088  N  N   . HIS C  1 83  ? 10.479  13.193  1.496   1.00 29.79 ?  107  HIS C N   1 
ATOM   5089  C  CA  . HIS C  1 83  ? 11.014  14.190  2.426   1.00 29.67 ?  107  HIS C CA  1 
ATOM   5090  C  C   . HIS C  1 83  ? 11.378  15.507  1.728   1.00 29.86 ?  107  HIS C C   1 
ATOM   5091  O  O   . HIS C  1 83  ? 11.642  16.508  2.394   1.00 29.76 ?  107  HIS C O   1 
ATOM   5092  C  CB  . HIS C  1 83  ? 12.186  13.626  3.239   1.00 29.44 ?  107  HIS C CB  1 
ATOM   5093  C  CG  . HIS C  1 83  ? 11.765  12.707  4.348   1.00 29.13 ?  107  HIS C CG  1 
ATOM   5094  N  ND1 . HIS C  1 83  ? 11.629  13.133  5.651   1.00 28.75 ?  107  HIS C ND1 1 
ATOM   5095  C  CD2 . HIS C  1 83  ? 11.444  11.389  4.349   1.00 29.29 ?  107  HIS C CD2 1 
ATOM   5096  C  CE1 . HIS C  1 83  ? 11.244  12.119  6.407   1.00 29.17 ?  107  HIS C CE1 1 
ATOM   5097  N  NE2 . HIS C  1 83  ? 11.124  11.046  5.643   1.00 28.76 ?  107  HIS C NE2 1 
ATOM   5098  N  N   . SER C  1 84  ? 11.372  15.508  0.392   1.00 29.99 ?  108  SER C N   1 
ATOM   5099  C  CA  . SER C  1 84  ? 11.475  16.751  -0.380  1.00 30.30 ?  108  SER C CA  1 
ATOM   5100  C  C   . SER C  1 84  ? 10.263  17.643  -0.109  1.00 30.43 ?  108  SER C C   1 
ATOM   5101  O  O   . SER C  1 84  ? 10.345  18.865  -0.238  1.00 30.35 ?  108  SER C O   1 
ATOM   5102  C  CB  . SER C  1 84  ? 11.585  16.472  -1.879  1.00 30.27 ?  108  SER C CB  1 
ATOM   5103  O  OG  . SER C  1 84  ? 12.855  15.942  -2.216  1.00 31.16 ?  108  SER C OG  1 
ATOM   5104  N  N   . ASP C  1 85  ? 9.148   17.011  0.262   1.00 30.68 ?  109  ASP C N   1 
ATOM   5105  C  CA  . ASP C  1 85  ? 7.935   17.711  0.686   1.00 31.04 ?  109  ASP C CA  1 
ATOM   5106  C  C   . ASP C  1 85  ? 7.842   17.832  2.207   1.00 30.72 ?  109  ASP C C   1 
ATOM   5107  O  O   . ASP C  1 85  ? 7.450   18.880  2.723   1.00 30.80 ?  109  ASP C O   1 
ATOM   5108  C  CB  . ASP C  1 85  ? 6.684   16.991  0.170   1.00 31.25 ?  109  ASP C CB  1 
ATOM   5109  C  CG  . ASP C  1 85  ? 6.559   17.029  -1.340  1.00 32.62 ?  109  ASP C CG  1 
ATOM   5110  O  OD1 . ASP C  1 85  ? 6.883   18.072  -1.951  1.00 34.36 ?  109  ASP C OD1 1 
ATOM   5111  O  OD2 . ASP C  1 85  ? 6.117   16.010  -1.919  1.00 34.63 -1 109  ASP C OD2 1 
ATOM   5112  N  N   . GLU C  1 86  ? 8.196   16.758  2.912   1.00 30.36 ?  110  GLU C N   1 
ATOM   5113  C  CA  . GLU C  1 86  ? 7.998   16.671  4.365   1.00 30.13 ?  110  GLU C CA  1 
ATOM   5114  C  C   . GLU C  1 86  ? 9.010   17.462  5.191   1.00 29.60 ?  110  GLU C C   1 
ATOM   5115  O  O   . GLU C  1 86  ? 8.632   18.199  6.104   1.00 29.33 ?  110  GLU C O   1 
ATOM   5116  C  CB  . GLU C  1 86  ? 7.966   15.210  4.824   1.00 30.29 ?  110  GLU C CB  1 
ATOM   5117  C  CG  . GLU C  1 86  ? 6.689   14.468  4.437   1.00 31.66 ?  110  GLU C CG  1 
ATOM   5118  C  CD  . GLU C  1 86  ? 5.433   15.110  5.011   1.00 32.79 ?  110  GLU C CD  1 
ATOM   5119  O  OE1 . GLU C  1 86  ? 5.481   15.621  6.155   1.00 32.99 ?  110  GLU C OE1 1 
ATOM   5120  O  OE2 . GLU C  1 86  ? 4.399   15.106  4.312   1.00 33.69 -1 110  GLU C OE2 1 
ATOM   5121  N  N   . THR C  1 87  ? 10.291  17.292  4.873   1.00 28.97 ?  111  THR C N   1 
ATOM   5122  C  CA  . THR C  1 87  ? 11.364  18.069  5.490   1.00 28.35 ?  111  THR C CA  1 
ATOM   5123  C  C   . THR C  1 87  ? 12.252  18.622  4.369   1.00 28.00 ?  111  THR C C   1 
ATOM   5124  O  O   . THR C  1 87  ? 13.369  18.133  4.170   1.00 28.08 ?  111  THR C O   1 
ATOM   5125  C  CB  . THR C  1 87  ? 12.207  17.204  6.466   1.00 28.33 ?  111  THR C CB  1 
ATOM   5126  O  OG1 . THR C  1 87  ? 12.702  16.047  5.783   1.00 28.12 ?  111  THR C OG1 1 
ATOM   5127  C  CG2 . THR C  1 87  ? 11.384  16.753  7.659   1.00 28.07 ?  111  THR C CG2 1 
ATOM   5128  N  N   . PRO C  1 88  ? 11.748  19.623  3.611   1.00 27.56 ?  112  PRO C N   1 
ATOM   5129  C  CA  . PRO C  1 88  ? 12.422  20.028  2.362   1.00 27.34 ?  112  PRO C CA  1 
ATOM   5130  C  C   . PRO C  1 88  ? 13.878  20.461  2.527   1.00 27.04 ?  112  PRO C C   1 
ATOM   5131  O  O   . PRO C  1 88  ? 14.721  20.098  1.703   1.00 27.02 ?  112  PRO C O   1 
ATOM   5132  C  CB  . PRO C  1 88  ? 11.561  21.194  1.840   1.00 27.24 ?  112  PRO C CB  1 
ATOM   5133  C  CG  . PRO C  1 88  ? 10.672  21.593  2.989   1.00 27.45 ?  112  PRO C CG  1 
ATOM   5134  C  CD  . PRO C  1 88  ? 10.488  20.365  3.820   1.00 27.57 ?  112  PRO C CD  1 
ATOM   5135  N  N   . VAL C  1 89  ? 14.167  21.219  3.584   1.00 26.58 ?  113  VAL C N   1 
ATOM   5136  C  CA  . VAL C  1 89  ? 15.512  21.763  3.798   1.00 26.21 ?  113  VAL C CA  1 
ATOM   5137  C  C   . VAL C  1 89  ? 16.535  20.681  4.176   1.00 25.97 ?  113  VAL C C   1 
ATOM   5138  O  O   . VAL C  1 89  ? 17.704  20.776  3.792   1.00 25.76 ?  113  VAL C O   1 
ATOM   5139  C  CB  . VAL C  1 89  ? 15.505  22.946  4.809   1.00 26.17 ?  113  VAL C CB  1 
ATOM   5140  C  CG1 . VAL C  1 89  ? 16.923  23.433  5.121   1.00 25.78 ?  113  VAL C CG1 1 
ATOM   5141  C  CG2 . VAL C  1 89  ? 14.667  24.096  4.265   1.00 26.33 ?  113  VAL C CG2 1 
ATOM   5142  N  N   . TRP C  1 90  ? 16.100  19.648  4.899   1.00 25.85 ?  114  TRP C N   1 
ATOM   5143  C  CA  . TRP C  1 90  ? 16.983  18.510  5.180   1.00 25.84 ?  114  TRP C CA  1 
ATOM   5144  C  C   . TRP C  1 90  ? 17.496  17.878  3.882   1.00 25.91 ?  114  TRP C C   1 
ATOM   5145  O  O   . TRP C  1 90  ? 18.654  17.472  3.807   1.00 25.86 ?  114  TRP C O   1 
ATOM   5146  C  CB  . TRP C  1 90  ? 16.306  17.448  6.050   1.00 25.69 ?  114  TRP C CB  1 
ATOM   5147  C  CG  . TRP C  1 90  ? 16.268  17.713  7.549   1.00 25.62 ?  114  TRP C CG  1 
ATOM   5148  C  CD1 . TRP C  1 90  ? 15.619  16.957  8.479   1.00 25.40 ?  114  TRP C CD1 1 
ATOM   5149  C  CD2 . TRP C  1 90  ? 16.879  18.800  8.275   1.00 25.43 ?  114  TRP C CD2 1 
ATOM   5150  N  NE1 . TRP C  1 90  ? 15.791  17.488  9.734   1.00 26.05 ?  114  TRP C NE1 1 
ATOM   5151  C  CE2 . TRP C  1 90  ? 16.558  18.619  9.639   1.00 25.28 ?  114  TRP C CE2 1 
ATOM   5152  C  CE3 . TRP C  1 90  ? 17.673  19.898  7.909   1.00 25.25 ?  114  TRP C CE3 1 
ATOM   5153  C  CZ2 . TRP C  1 90  ? 16.997  19.496  10.637  1.00 25.29 ?  114  TRP C CZ2 1 
ATOM   5154  C  CZ3 . TRP C  1 90  ? 18.107  20.773  8.903   1.00 24.92 ?  114  TRP C CZ3 1 
ATOM   5155  C  CH2 . TRP C  1 90  ? 17.767  20.564  10.251  1.00 25.48 ?  114  TRP C CH2 1 
ATOM   5156  N  N   . VAL C  1 91  ? 16.634  17.818  2.867   1.00 26.11 ?  115  VAL C N   1 
ATOM   5157  C  CA  . VAL C  1 91  ? 16.993  17.264  1.554   1.00 26.14 ?  115  VAL C CA  1 
ATOM   5158  C  C   . VAL C  1 91  ? 17.971  18.178  0.810   1.00 26.38 ?  115  VAL C C   1 
ATOM   5159  O  O   . VAL C  1 91  ? 18.957  17.706  0.239   1.00 26.27 ?  115  VAL C O   1 
ATOM   5160  C  CB  . VAL C  1 91  ? 15.732  16.973  0.684   1.00 26.22 ?  115  VAL C CB  1 
ATOM   5161  C  CG1 . VAL C  1 91  ? 16.110  16.625  -0.764  1.00 26.12 ?  115  VAL C CG1 1 
ATOM   5162  C  CG2 . VAL C  1 91  ? 14.901  15.852  1.304   1.00 25.77 ?  115  VAL C CG2 1 
ATOM   5163  N  N   . ARG C  1 92  ? 17.698  19.482  0.832   1.00 26.67 ?  116  ARG C N   1 
ATOM   5164  C  CA  . ARG C  1 92  ? 18.547  20.464  0.155   1.00 26.88 ?  116  ARG C CA  1 
ATOM   5165  C  C   . ARG C  1 92  ? 19.918  20.578  0.821   1.00 26.79 ?  116  ARG C C   1 
ATOM   5166  O  O   . ARG C  1 92  ? 20.934  20.697  0.131   1.00 26.82 ?  116  ARG C O   1 
ATOM   5167  C  CB  . ARG C  1 92  ? 17.864  21.836  0.079   1.00 27.06 ?  116  ARG C CB  1 
ATOM   5168  C  CG  . ARG C  1 92  ? 16.551  21.851  -0.700  1.00 28.02 ?  116  ARG C CG  1 
ATOM   5169  C  CD  . ARG C  1 92  ? 15.978  23.263  -0.781  1.00 30.42 ?  116  ARG C CD  1 
ATOM   5170  N  NE  . ARG C  1 92  ? 14.611  23.287  -1.304  1.00 31.97 ?  116  ARG C NE  1 
ATOM   5171  C  CZ  . ARG C  1 92  ? 13.536  23.644  -0.600  1.00 33.35 ?  116  ARG C CZ  1 
ATOM   5172  N  NH1 . ARG C  1 92  ? 13.652  24.027  0.667   1.00 33.44 ?  116  ARG C NH1 1 
ATOM   5173  N  NH2 . ARG C  1 92  ? 12.337  23.629  -1.168  1.00 33.73 ?  116  ARG C NH2 1 
ATOM   5174  N  N   . ALA C  1 93  ? 19.944  20.536  2.153   1.00 26.65 ?  117  ALA C N   1 
ATOM   5175  C  CA  . ALA C  1 93  ? 21.205  20.557  2.899   1.00 26.77 ?  117  ALA C CA  1 
ATOM   5176  C  C   . ALA C  1 93  ? 22.034  19.311  2.591   1.00 26.97 ?  117  ALA C C   1 
ATOM   5177  O  O   . ALA C  1 93  ? 23.235  19.405  2.333   1.00 27.05 ?  117  ALA C O   1 
ATOM   5178  C  CB  . ALA C  1 93  ? 20.951  20.687  4.400   1.00 26.58 ?  117  ALA C CB  1 
ATOM   5179  N  N   . TRP C  1 94  ? 21.378  18.152  2.602   1.00 27.17 ?  118  TRP C N   1 
ATOM   5180  C  CA  . TRP C  1 94  ? 22.030  16.884  2.280   1.00 27.59 ?  118  TRP C CA  1 
ATOM   5181  C  C   . TRP C  1 94  ? 22.548  16.850  0.837   1.00 27.95 ?  118  TRP C C   1 
ATOM   5182  O  O   . TRP C  1 94  ? 23.673  16.416  0.593   1.00 27.89 ?  118  TRP C O   1 
ATOM   5183  C  CB  . TRP C  1 94  ? 21.086  15.704  2.555   1.00 27.32 ?  118  TRP C CB  1 
ATOM   5184  C  CG  . TRP C  1 94  ? 21.564  14.409  1.977   1.00 27.44 ?  118  TRP C CG  1 
ATOM   5185  C  CD1 . TRP C  1 94  ? 22.482  13.556  2.522   1.00 27.13 ?  118  TRP C CD1 1 
ATOM   5186  C  CD2 . TRP C  1 94  ? 21.157  13.822  0.733   1.00 26.97 ?  118  TRP C CD2 1 
ATOM   5187  N  NE1 . TRP C  1 94  ? 22.671  12.474  1.693   1.00 27.12 ?  118  TRP C NE1 1 
ATOM   5188  C  CE2 . TRP C  1 94  ? 21.867  12.610  0.592   1.00 27.35 ?  118  TRP C CE2 1 
ATOM   5189  C  CE3 . TRP C  1 94  ? 20.262  14.205  -0.275  1.00 27.19 ?  118  TRP C CE3 1 
ATOM   5190  C  CZ2 . TRP C  1 94  ? 21.713  11.775  -0.523  1.00 27.46 ?  118  TRP C CZ2 1 
ATOM   5191  C  CZ3 . TRP C  1 94  ? 20.105  13.372  -1.383  1.00 27.18 ?  118  TRP C CZ3 1 
ATOM   5192  C  CH2 . TRP C  1 94  ? 20.827  12.171  -1.495  1.00 27.50 ?  118  TRP C CH2 1 
ATOM   5193  N  N   . LYS C  1 95  ? 21.730  17.328  -0.100  1.00 28.50 ?  119  LYS C N   1 
ATOM   5194  C  CA  . LYS C  1 95  ? 22.070  17.325  -1.528  1.00 29.10 ?  119  LYS C CA  1 
ATOM   5195  C  C   . LYS C  1 95  ? 23.338  18.124  -1.835  1.00 29.21 ?  119  LYS C C   1 
ATOM   5196  O  O   . LYS C  1 95  ? 24.107  17.755  -2.726  1.00 29.30 ?  119  LYS C O   1 
ATOM   5197  C  CB  . LYS C  1 95  ? 20.894  17.850  -2.361  1.00 29.39 ?  119  LYS C CB  1 
ATOM   5198  C  CG  . LYS C  1 95  ? 21.006  17.577  -3.857  1.00 30.66 ?  119  LYS C CG  1 
ATOM   5199  C  CD  . LYS C  1 95  ? 19.717  17.935  -4.593  1.00 32.35 ?  119  LYS C CD  1 
ATOM   5200  C  CE  . LYS C  1 95  ? 19.729  17.403  -6.020  1.00 33.28 ?  119  LYS C CE  1 
ATOM   5201  N  NZ  . LYS C  1 95  ? 20.857  17.951  -6.826  1.00 34.45 ?  119  LYS C NZ  1 
ATOM   5202  N  N   . ARG C  1 96  ? 23.555  19.215  -1.100  1.00 29.17 ?  120  ARG C N   1 
ATOM   5203  C  CA  . ARG C  1 96  ? 24.770  20.011  -1.277  1.00 29.43 ?  120  ARG C CA  1 
ATOM   5204  C  C   . ARG C  1 96  ? 25.940  19.546  -0.394  1.00 28.94 ?  120  ARG C C   1 
ATOM   5205  O  O   . ARG C  1 96  ? 27.032  20.107  -0.466  1.00 29.07 ?  120  ARG C O   1 
ATOM   5206  C  CB  . ARG C  1 96  ? 24.496  21.520  -1.126  1.00 29.73 ?  120  ARG C CB  1 
ATOM   5207  C  CG  . ARG C  1 96  ? 24.046  21.987  0.255   1.00 31.42 ?  120  ARG C CG  1 
ATOM   5208  C  CD  . ARG C  1 96  ? 23.830  23.505  0.275   1.00 34.18 ?  120  ARG C CD  1 
ATOM   5209  N  NE  . ARG C  1 96  ? 22.968  23.919  1.382   1.00 35.96 ?  120  ARG C NE  1 
ATOM   5210  C  CZ  . ARG C  1 96  ? 21.704  24.322  1.253   1.00 37.14 ?  120  ARG C CZ  1 
ATOM   5211  N  NH1 . ARG C  1 96  ? 21.127  24.392  0.058   1.00 37.34 ?  120  ARG C NH1 1 
ATOM   5212  N  NH2 . ARG C  1 96  ? 21.013  24.666  2.328   1.00 38.32 ?  120  ARG C NH2 1 
ATOM   5213  N  N   . SER C  1 97  ? 25.714  18.514  0.420   1.00 28.47 ?  121  SER C N   1 
ATOM   5214  C  CA  . SER C  1 97  ? 26.770  17.977  1.279   1.00 27.81 ?  121  SER C CA  1 
ATOM   5215  C  C   . SER C  1 97  ? 27.682  16.997  0.541   1.00 27.45 ?  121  SER C C   1 
ATOM   5216  O  O   . SER C  1 97  ? 27.275  16.359  -0.440  1.00 27.20 ?  121  SER C O   1 
ATOM   5217  C  CB  . SER C  1 97  ? 26.188  17.316  2.528   1.00 27.75 ?  121  SER C CB  1 
ATOM   5218  O  OG  . SER C  1 97  ? 25.705  16.013  2.255   1.00 27.75 ?  121  SER C OG  1 
ATOM   5219  N  N   . THR C  1 98  ? 28.916  16.899  1.029   1.00 26.99 ?  122  THR C N   1 
ATOM   5220  C  CA  . THR C  1 98  ? 29.901  15.927  0.563   1.00 26.67 ?  122  THR C CA  1 
ATOM   5221  C  C   . THR C  1 98  ? 29.328  14.502  0.531   1.00 26.47 ?  122  THR C C   1 
ATOM   5222  O  O   . THR C  1 98  ? 29.529  13.773  -0.446  1.00 26.39 ?  122  THR C O   1 
ATOM   5223  C  CB  . THR C  1 98  ? 31.173  15.989  1.439   1.00 26.57 ?  122  THR C CB  1 
ATOM   5224  O  OG1 . THR C  1 98  ? 31.796  17.267  1.274   1.00 26.57 ?  122  THR C OG1 1 
ATOM   5225  C  CG2 . THR C  1 98  ? 32.165  14.910  1.058   1.00 26.47 ?  122  THR C CG2 1 
ATOM   5226  N  N   . HIS C  1 99  ? 28.598  14.136  1.586   1.00 26.15 ?  123  HIS C N   1 
ATOM   5227  C  CA  . HIS C  1 99  ? 27.942  12.828  1.696   1.00 26.29 ?  123  HIS C CA  1 
ATOM   5228  C  C   . HIS C  1 99  ? 27.110  12.445  0.468   1.00 26.43 ?  123  HIS C C   1 
ATOM   5229  O  O   . HIS C  1 99  ? 27.003  11.265  0.130   1.00 26.33 ?  123  HIS C O   1 
ATOM   5230  C  CB  . HIS C  1 99  ? 27.058  12.770  2.953   1.00 26.18 ?  123  HIS C CB  1 
ATOM   5231  C  CG  . HIS C  1 99  ? 27.814  12.526  4.226   1.00 26.24 ?  123  HIS C CG  1 
ATOM   5232  N  ND1 . HIS C  1 99  ? 27.455  13.104  5.425   1.00 25.75 ?  123  HIS C ND1 1 
ATOM   5233  C  CD2 . HIS C  1 99  ? 28.901  11.762  4.489   1.00 26.45 ?  123  HIS C CD2 1 
ATOM   5234  C  CE1 . HIS C  1 99  ? 28.289  12.707  6.371   1.00 25.70 ?  123  HIS C CE1 1 
ATOM   5235  N  NE2 . HIS C  1 99  ? 29.178  11.891  5.831   1.00 26.00 ?  123  HIS C NE2 1 
ATOM   5236  N  N   . ALA C  1 100 ? 26.521  13.446  -0.186  1.00 26.60 ?  124  ALA C N   1 
ATOM   5237  C  CA  . ALA C  1 100 ? 25.699  13.225  -1.373  1.00 26.96 ?  124  ALA C CA  1 
ATOM   5238  C  C   . ALA C  1 100 ? 26.458  13.415  -2.691  1.00 27.16 ?  124  ALA C C   1 
ATOM   5239  O  O   . ALA C  1 100 ? 25.901  13.173  -3.763  1.00 27.48 ?  124  ALA C O   1 
ATOM   5240  C  CB  . ALA C  1 100 ? 24.469  14.123  -1.337  1.00 26.84 ?  124  ALA C CB  1 
ATOM   5241  N  N   . ASN C  1 101 ? 27.714  13.852  -2.608  1.00 27.29 ?  125  ASN C N   1 
ATOM   5242  C  CA  . ASN C  1 101 ? 28.532  14.122  -3.795  1.00 27.49 ?  125  ASN C CA  1 
ATOM   5243  C  C   . ASN C  1 101 ? 29.899  13.427  -3.744  1.00 27.75 ?  125  ASN C C   1 
ATOM   5244  O  O   . ASN C  1 101 ? 30.941  14.070  -3.916  1.00 27.40 ?  125  ASN C O   1 
ATOM   5245  C  CB  . ASN C  1 101 ? 28.723  15.633  -3.993  1.00 27.37 ?  125  ASN C CB  1 
ATOM   5246  C  CG  . ASN C  1 101 ? 27.419  16.369  -4.242  1.00 27.44 ?  125  ASN C CG  1 
ATOM   5247  O  OD1 . ASN C  1 101 ? 27.065  16.656  -5.385  1.00 27.50 ?  125  ASN C OD1 1 
ATOM   5248  N  ND2 . ASN C  1 101 ? 26.704  16.689  -3.170  1.00 27.42 ?  125  ASN C ND2 1 
ATOM   5249  N  N   . LEU C  1 102 ? 29.887  12.116  -3.514  1.00 28.16 ?  126  LEU C N   1 
ATOM   5250  C  CA  . LEU C  1 102 ? 31.122  11.342  -3.352  1.00 28.87 ?  126  LEU C CA  1 
ATOM   5251  C  C   . LEU C  1 102 ? 31.996  11.248  -4.612  1.00 29.37 ?  126  LEU C C   1 
ATOM   5252  O  O   . LEU C  1 102 ? 33.220  11.160  -4.510  1.00 29.41 ?  126  LEU C O   1 
ATOM   5253  C  CB  . LEU C  1 102 ? 30.830  9.946   -2.783  1.00 28.64 ?  126  LEU C CB  1 
ATOM   5254  C  CG  . LEU C  1 102 ? 30.311  9.876   -1.341  1.00 28.49 ?  126  LEU C CG  1 
ATOM   5255  C  CD1 . LEU C  1 102 ? 30.188  8.431   -0.883  1.00 27.65 ?  126  LEU C CD1 1 
ATOM   5256  C  CD2 . LEU C  1 102 ? 31.206  10.661  -0.379  1.00 28.07 ?  126  LEU C CD2 1 
ATOM   5257  N  N   . ASP C  1 103 ? 31.371  11.278  -5.788  1.00 30.06 ?  127  ASP C N   1 
ATOM   5258  C  CA  . ASP C  1 103 ? 32.110  11.269  -7.052  1.00 30.87 ?  127  ASP C CA  1 
ATOM   5259  C  C   . ASP C  1 103 ? 32.941  12.534  -7.255  1.00 31.10 ?  127  ASP C C   1 
ATOM   5260  O  O   . ASP C  1 103 ? 33.966  12.500  -7.939  1.00 31.16 ?  127  ASP C O   1 
ATOM   5261  C  CB  . ASP C  1 103 ? 31.176  11.044  -8.247  1.00 31.07 ?  127  ASP C CB  1 
ATOM   5262  C  CG  . ASP C  1 103 ? 30.978  9.567   -8.571  1.00 32.24 ?  127  ASP C CG  1 
ATOM   5263  O  OD1 . ASP C  1 103 ? 31.801  8.730   -8.135  1.00 34.18 ?  127  ASP C OD1 1 
ATOM   5264  O  OD2 . ASP C  1 103 ? 29.998  9.239   -9.272  1.00 33.55 -1 127  ASP C OD2 1 
ATOM   5265  N  N   . LYS C  1 104 ? 32.499  13.643  -6.660  1.00 31.42 ?  128  LYS C N   1 
ATOM   5266  C  CA  . LYS C  1 104 ? 33.264  14.888  -6.679  1.00 31.77 ?  128  LYS C CA  1 
ATOM   5267  C  C   . LYS C  1 104 ? 34.555  14.734  -5.873  1.00 31.75 ?  128  LYS C C   1 
ATOM   5268  O  O   . LYS C  1 104 ? 35.605  15.240  -6.269  1.00 31.50 ?  128  LYS C O   1 
ATOM   5269  C  CB  . LYS C  1 104 ? 32.430  16.056  -6.143  1.00 31.84 ?  128  LYS C CB  1 
ATOM   5270  C  CG  . LYS C  1 104 ? 32.843  17.408  -6.715  1.00 32.94 ?  128  LYS C CG  1 
ATOM   5271  C  CD  . LYS C  1 104 ? 31.979  18.555  -6.192  1.00 34.59 ?  128  LYS C CD  1 
ATOM   5272  C  CE  . LYS C  1 104 ? 32.625  19.250  -5.001  1.00 35.03 ?  128  LYS C CE  1 
ATOM   5273  N  NZ  . LYS C  1 104 ? 31.999  20.577  -4.741  1.00 35.47 ?  128  LYS C NZ  1 
ATOM   5274  N  N   . ILE C  1 105 ? 34.460  14.026  -4.748  1.00 32.02 ?  129  ILE C N   1 
ATOM   5275  C  CA  . ILE C  1 105 ? 35.612  13.699  -3.906  1.00 32.39 ?  129  ILE C CA  1 
ATOM   5276  C  C   . ILE C  1 105 ? 36.577  12.746  -4.637  1.00 32.89 ?  129  ILE C C   1 
ATOM   5277  O  O   . ILE C  1 105 ? 37.798  12.883  -4.522  1.00 32.74 ?  129  ILE C O   1 
ATOM   5278  C  CB  . ILE C  1 105 ? 35.161  13.117  -2.525  1.00 32.30 ?  129  ILE C CB  1 
ATOM   5279  C  CG1 . ILE C  1 105 ? 34.307  14.134  -1.745  1.00 32.23 ?  129  ILE C CG1 1 
ATOM   5280  C  CG2 . ILE C  1 105 ? 36.347  12.641  -1.690  1.00 31.62 ?  129  ILE C CG2 1 
ATOM   5281  C  CD1 . ILE C  1 105 ? 35.008  15.468  -1.391  1.00 31.37 ?  129  ILE C CD1 1 
ATOM   5282  N  N   . ARG C  1 106 ? 36.023  11.802  -5.401  1.00 33.46 ?  130  ARG C N   1 
ATOM   5283  C  CA  . ARG C  1 106 ? 36.835  10.893  -6.229  1.00 34.04 ?  130  ARG C CA  1 
ATOM   5284  C  C   . ARG C  1 106 ? 37.580  11.609  -7.354  1.00 34.39 ?  130  ARG C C   1 
ATOM   5285  O  O   . ARG C  1 106 ? 38.635  11.150  -7.788  1.00 34.72 ?  130  ARG C O   1 
ATOM   5286  C  CB  . ARG C  1 106 ? 35.987  9.752   -6.807  1.00 33.89 ?  130  ARG C CB  1 
ATOM   5287  C  CG  . ARG C  1 106 ? 35.811  8.602   -5.843  1.00 33.75 ?  130  ARG C CG  1 
ATOM   5288  C  CD  . ARG C  1 106 ? 35.024  7.435   -6.417  1.00 33.42 ?  130  ARG C CD  1 
ATOM   5289  N  NE  . ARG C  1 106 ? 34.467  6.650   -5.316  1.00 33.23 ?  130  ARG C NE  1 
ATOM   5290  C  CZ  . ARG C  1 106 ? 33.214  6.743   -4.877  1.00 32.90 ?  130  ARG C CZ  1 
ATOM   5291  N  NH1 . ARG C  1 106 ? 32.348  7.559   -5.463  1.00 32.81 ?  130  ARG C NH1 1 
ATOM   5292  N  NH2 . ARG C  1 106 ? 32.820  5.999   -3.855  1.00 33.22 ?  130  ARG C NH2 1 
ATOM   5293  N  N   . ASN C  1 107 ? 37.031  12.729  -7.815  1.00 34.86 ?  131  ASN C N   1 
ATOM   5294  C  CA  . ASN C  1 107 ? 37.613  13.489  -8.922  1.00 35.49 ?  131  ASN C CA  1 
ATOM   5295  C  C   . ASN C  1 107 ? 38.660  14.526  -8.503  1.00 35.60 ?  131  ASN C C   1 
ATOM   5296  O  O   . ASN C  1 107 ? 39.295  15.152  -9.360  1.00 35.47 ?  131  ASN C O   1 
ATOM   5297  C  CB  . ASN C  1 107 ? 36.509  14.154  -9.756  1.00 35.60 ?  131  ASN C CB  1 
ATOM   5298  C  CG  . ASN C  1 107 ? 35.727  13.156  -10.601 1.00 36.65 ?  131  ASN C CG  1 
ATOM   5299  O  OD1 . ASN C  1 107 ? 36.181  12.035  -10.852 1.00 37.49 ?  131  ASN C OD1 1 
ATOM   5300  N  ND2 . ASN C  1 107 ? 34.546  13.566  -11.052 1.00 37.16 ?  131  ASN C ND2 1 
ATOM   5301  N  N   . LEU C  1 108 ? 38.830  14.711  -7.194  1.00 35.88 ?  132  LEU C N   1 
ATOM   5302  C  CA  . LEU C  1 108 ? 39.822  15.653  -6.666  1.00 36.19 ?  132  LEU C CA  1 
ATOM   5303  C  C   . LEU C  1 108 ? 41.216  15.346  -7.210  1.00 36.43 ?  132  LEU C C   1 
ATOM   5304  O  O   . LEU C  1 108 ? 41.668  14.197  -7.183  1.00 36.32 ?  132  LEU C O   1 
ATOM   5305  C  CB  . LEU C  1 108 ? 39.844  15.640  -5.132  1.00 36.11 ?  132  LEU C CB  1 
ATOM   5306  C  CG  . LEU C  1 108 ? 38.604  16.089  -4.347  1.00 35.87 ?  132  LEU C CG  1 
ATOM   5307  C  CD1 . LEU C  1 108 ? 38.802  15.826  -2.862  1.00 35.35 ?  132  LEU C CD1 1 
ATOM   5308  C  CD2 . LEU C  1 108 ? 38.264  17.555  -4.596  1.00 35.84 ?  132  LEU C CD2 1 
ATOM   5309  N  N   . LYS C  1 109 ? 41.879  16.380  -7.717  1.00 36.82 ?  133  LYS C N   1 
ATOM   5310  C  CA  . LYS C  1 109 ? 43.231  16.250  -8.254  1.00 37.23 ?  133  LYS C CA  1 
ATOM   5311  C  C   . LYS C  1 109 ? 44.261  16.647  -7.194  1.00 37.08 ?  133  LYS C C   1 
ATOM   5312  O  O   . LYS C  1 109 ? 43.928  17.349  -6.236  1.00 37.09 ?  133  LYS C O   1 
ATOM   5313  C  CB  . LYS C  1 109 ? 43.379  17.089  -9.525  1.00 37.45 ?  133  LYS C CB  1 
ATOM   5314  C  CG  . LYS C  1 109 ? 42.674  16.486  -10.738 1.00 38.87 ?  133  LYS C CG  1 
ATOM   5315  C  CD  . LYS C  1 109 ? 42.294  17.547  -11.765 1.00 41.05 ?  133  LYS C CD  1 
ATOM   5316  C  CE  . LYS C  1 109 ? 40.877  18.075  -11.538 1.00 42.41 ?  133  LYS C CE  1 
ATOM   5317  N  NZ  . LYS C  1 109 ? 39.832  17.075  -11.920 1.00 43.10 ?  133  LYS C NZ  1 
ATOM   5318  N  N   . SER C  1 110 ? 45.503  16.197  -7.376  1.00 36.90 ?  134  SER C N   1 
ATOM   5319  C  CA  . SER C  1 110 ? 46.557  16.330  -6.359  1.00 36.70 ?  134  SER C CA  1 
ATOM   5320  C  C   . SER C  1 110 ? 47.027  17.762  -6.101  1.00 36.52 ?  134  SER C C   1 
ATOM   5321  O  O   . SER C  1 110 ? 47.752  18.013  -5.137  1.00 36.50 ?  134  SER C O   1 
ATOM   5322  C  CB  . SER C  1 110 ? 47.753  15.438  -6.710  1.00 36.77 ?  134  SER C CB  1 
ATOM   5323  O  OG  . SER C  1 110 ? 48.383  15.873  -7.902  1.00 36.88 ?  134  SER C OG  1 
ATOM   5324  N  N   . ASP C  1 111 ? 46.621  18.689  -6.966  1.00 36.40 ?  135  ASP C N   1 
ATOM   5325  C  CA  . ASP C  1 111 ? 46.910  20.111  -6.783  1.00 36.39 ?  135  ASP C CA  1 
ATOM   5326  C  C   . ASP C  1 111 ? 45.737  20.862  -6.126  1.00 36.08 ?  135  ASP C C   1 
ATOM   5327  O  O   . ASP C  1 111 ? 45.762  22.093  -6.008  1.00 36.09 ?  135  ASP C O   1 
ATOM   5328  C  CB  . ASP C  1 111 ? 47.293  20.758  -8.119  1.00 36.52 ?  135  ASP C CB  1 
ATOM   5329  C  CG  . ASP C  1 111 ? 46.142  20.777  -9.112  1.00 37.65 ?  135  ASP C CG  1 
ATOM   5330  O  OD1 . ASP C  1 111 ? 46.008  21.783  -9.843  1.00 39.01 ?  135  ASP C OD1 1 
ATOM   5331  O  OD2 . ASP C  1 111 ? 45.367  19.796  -9.158  1.00 38.15 -1 135  ASP C OD2 1 
ATOM   5332  N  N   . ASP C  1 112 ? 44.712  20.116  -5.712  1.00 35.44 ?  136  ASP C N   1 
ATOM   5333  C  CA  . ASP C  1 112 ? 43.584  20.683  -4.968  1.00 34.95 ?  136  ASP C CA  1 
ATOM   5334  C  C   . ASP C  1 112 ? 43.901  20.567  -3.480  1.00 34.25 ?  136  ASP C C   1 
ATOM   5335  O  O   . ASP C  1 112 ? 44.215  19.475  -3.005  1.00 34.24 ?  136  ASP C O   1 
ATOM   5336  C  CB  . ASP C  1 112 ? 42.288  19.929  -5.301  1.00 35.05 ?  136  ASP C CB  1 
ATOM   5337  C  CG  . ASP C  1 112 ? 41.029  20.695  -4.907  1.00 35.46 ?  136  ASP C CG  1 
ATOM   5338  O  OD1 . ASP C  1 112 ? 40.946  21.215  -3.773  1.00 35.61 ?  136  ASP C OD1 1 
ATOM   5339  O  OD2 . ASP C  1 112 ? 40.096  20.753  -5.737  1.00 36.11 -1 136  ASP C OD2 1 
ATOM   5340  N  N   . PRO C  1 113 ? 43.838  21.692  -2.739  1.00 33.70 ?  137  PRO C N   1 
ATOM   5341  C  CA  . PRO C  1 113 ? 44.103  21.677  -1.294  1.00 33.15 ?  137  PRO C CA  1 
ATOM   5342  C  C   . PRO C  1 113 ? 43.175  20.749  -0.504  1.00 32.63 ?  137  PRO C C   1 
ATOM   5343  O  O   . PRO C  1 113 ? 43.477  20.410  0.643   1.00 32.29 ?  137  PRO C O   1 
ATOM   5344  C  CB  . PRO C  1 113 ? 43.878  23.139  -0.872  1.00 33.28 ?  137  PRO C CB  1 
ATOM   5345  C  CG  . PRO C  1 113 ? 43.181  23.790  -2.014  1.00 33.40 ?  137  PRO C CG  1 
ATOM   5346  C  CD  . PRO C  1 113 ? 43.622  23.062  -3.236  1.00 33.64 ?  137  PRO C CD  1 
ATOM   5347  N  N   . LEU C  1 114 ? 42.067  20.337  -1.120  1.00 32.04 ?  138  LEU C N   1 
ATOM   5348  C  CA  . LEU C  1 114 ? 41.099  19.446  -0.470  1.00 31.58 ?  138  LEU C CA  1 
ATOM   5349  C  C   . LEU C  1 114 ? 41.364  17.971  -0.771  1.00 31.17 ?  138  LEU C C   1 
ATOM   5350  O  O   . LEU C  1 114 ? 40.625  17.096  -0.313  1.00 31.01 ?  138  LEU C O   1 
ATOM   5351  C  CB  . LEU C  1 114 ? 39.661  19.824  -0.858  1.00 31.55 ?  138  LEU C CB  1 
ATOM   5352  C  CG  . LEU C  1 114 ? 39.200  21.278  -0.685  1.00 31.45 ?  138  LEU C CG  1 
ATOM   5353  C  CD1 . LEU C  1 114 ? 37.696  21.382  -0.885  1.00 30.85 ?  138  LEU C CD1 1 
ATOM   5354  C  CD2 . LEU C  1 114 ? 39.604  21.838  0.674   1.00 31.43 ?  138  LEU C CD2 1 
ATOM   5355  N  N   . TYR C  1 115 ? 42.437  17.713  -1.521  1.00 30.85 ?  139  TYR C N   1 
ATOM   5356  C  CA  . TYR C  1 115 ? 42.833  16.366  -1.958  1.00 30.60 ?  139  TYR C CA  1 
ATOM   5357  C  C   . TYR C  1 115 ? 42.786  15.298  -0.867  1.00 30.15 ?  139  TYR C C   1 
ATOM   5358  O  O   . TYR C  1 115 ? 42.495  14.134  -1.151  1.00 30.04 ?  139  TYR C O   1 
ATOM   5359  C  CB  . TYR C  1 115 ? 44.237  16.411  -2.573  1.00 30.92 ?  139  TYR C CB  1 
ATOM   5360  C  CG  . TYR C  1 115 ? 44.696  15.125  -3.229  1.00 31.73 ?  139  TYR C CG  1 
ATOM   5361  C  CD1 . TYR C  1 115 ? 44.026  14.605  -4.337  1.00 32.66 ?  139  TYR C CD1 1 
ATOM   5362  C  CD2 . TYR C  1 115 ? 45.816  14.439  -2.755  1.00 32.65 ?  139  TYR C CD2 1 
ATOM   5363  C  CE1 . TYR C  1 115 ? 44.453  13.429  -4.951  1.00 33.25 ?  139  TYR C CE1 1 
ATOM   5364  C  CE2 . TYR C  1 115 ? 46.252  13.261  -3.363  1.00 32.95 ?  139  TYR C CE2 1 
ATOM   5365  C  CZ  . TYR C  1 115 ? 45.564  12.764  -4.459  1.00 33.19 ?  139  TYR C CZ  1 
ATOM   5366  O  OH  . TYR C  1 115 ? 45.982  11.603  -5.068  1.00 33.68 ?  139  TYR C OH  1 
ATOM   5367  N  N   . TYR C  1 116 ? 43.067  15.700  0.373   1.00 29.49 ?  140  TYR C N   1 
ATOM   5368  C  CA  . TYR C  1 116 ? 43.086  14.783  1.513   1.00 28.91 ?  140  TYR C CA  1 
ATOM   5369  C  C   . TYR C  1 116 ? 41.753  14.041  1.683   1.00 28.79 ?  140  TYR C C   1 
ATOM   5370  O  O   . TYR C  1 116 ? 41.722  12.929  2.215   1.00 28.67 ?  140  TYR C O   1 
ATOM   5371  C  CB  . TYR C  1 116 ? 43.449  15.535  2.803   1.00 28.74 ?  140  TYR C CB  1 
ATOM   5372  C  CG  . TYR C  1 116 ? 42.281  16.259  3.452   1.00 27.90 ?  140  TYR C CG  1 
ATOM   5373  C  CD1 . TYR C  1 116 ? 41.948  17.564  3.083   1.00 26.87 ?  140  TYR C CD1 1 
ATOM   5374  C  CD2 . TYR C  1 116 ? 41.508  15.634  4.430   1.00 27.11 ?  140  TYR C CD2 1 
ATOM   5375  C  CE1 . TYR C  1 116 ? 40.871  18.228  3.674   1.00 26.22 ?  140  TYR C CE1 1 
ATOM   5376  C  CE2 . TYR C  1 116 ? 40.430  16.287  5.023   1.00 26.84 ?  140  TYR C CE2 1 
ATOM   5377  C  CZ  . TYR C  1 116 ? 40.119  17.582  4.643   1.00 25.57 ?  140  TYR C CZ  1 
ATOM   5378  O  OH  . TYR C  1 116 ? 39.060  18.223  5.234   1.00 24.04 ?  140  TYR C OH  1 
ATOM   5379  N  N   . LYS C  1 117 ? 40.663  14.664  1.228   1.00 28.51 ?  141  LYS C N   1 
ATOM   5380  C  CA  . LYS C  1 117 ? 39.320  14.082  1.335   1.00 28.42 ?  141  LYS C CA  1 
ATOM   5381  C  C   . LYS C  1 117 ? 39.169  12.795  0.522   1.00 28.17 ?  141  LYS C C   1 
ATOM   5382  O  O   . LYS C  1 117 ? 38.469  11.873  0.941   1.00 28.02 ?  141  LYS C O   1 
ATOM   5383  C  CB  . LYS C  1 117 ? 38.248  15.102  0.931   1.00 28.37 ?  141  LYS C CB  1 
ATOM   5384  C  CG  . LYS C  1 117 ? 38.134  16.283  1.884   1.00 28.02 ?  141  LYS C CG  1 
ATOM   5385  C  CD  . LYS C  1 117 ? 37.163  17.328  1.366   1.00 27.02 ?  141  LYS C CD  1 
ATOM   5386  C  CE  . LYS C  1 117 ? 37.004  18.469  2.363   1.00 26.96 ?  141  LYS C CE  1 
ATOM   5387  N  NZ  . LYS C  1 117 ? 36.372  18.017  3.634   1.00 25.95 ?  141  LYS C NZ  1 
ATOM   5388  N  N   . LYS C  1 118 ? 39.829  12.749  -0.636  1.00 28.23 ?  142  LYS C N   1 
ATOM   5389  C  CA  . LYS C  1 118 ? 39.858  11.556  -1.488  1.00 28.11 ?  142  LYS C CA  1 
ATOM   5390  C  C   . LYS C  1 118 ? 40.405  10.357  -0.719  1.00 27.94 ?  142  LYS C C   1 
ATOM   5391  O  O   . LYS C  1 118 ? 39.814  9.277   -0.740  1.00 27.90 ?  142  LYS C O   1 
ATOM   5392  C  CB  . LYS C  1 118 ? 40.685  11.822  -2.753  1.00 28.37 ?  142  LYS C CB  1 
ATOM   5393  C  CG  . LYS C  1 118 ? 40.729  10.665  -3.754  1.00 28.62 ?  142  LYS C CG  1 
ATOM   5394  C  CD  . LYS C  1 118 ? 41.526  11.049  -4.998  1.00 29.65 ?  142  LYS C CD  1 
ATOM   5395  C  CE  . LYS C  1 118 ? 41.653  9.886   -5.984  1.00 30.12 ?  142  LYS C CE  1 
ATOM   5396  N  NZ  . LYS C  1 118 ? 42.514  8.782   -5.467  1.00 30.45 ?  142  LYS C NZ  1 
ATOM   5397  N  N   . GLY C  1 119 ? 41.523  10.565  -0.027  1.00 27.93 ?  143  GLY C N   1 
ATOM   5398  C  CA  . GLY C  1 119 ? 42.130  9.533   0.814   1.00 28.02 ?  143  GLY C CA  1 
ATOM   5399  C  C   . GLY C  1 119 ? 41.279  9.162   2.016   1.00 28.05 ?  143  GLY C C   1 
ATOM   5400  O  O   . GLY C  1 119 ? 41.313  8.017   2.477   1.00 28.11 ?  143  GLY C O   1 
ATOM   5401  N  N   . LYS C  1 120 ? 40.520  10.129  2.531   1.00 27.98 ?  144  LYS C N   1 
ATOM   5402  C  CA  . LYS C  1 120 ? 39.600  9.876   3.643   1.00 27.98 ?  144  LYS C CA  1 
ATOM   5403  C  C   . LYS C  1 120 ? 38.402  9.039   3.199   1.00 27.87 ?  144  LYS C C   1 
ATOM   5404  O  O   . LYS C  1 120 ? 37.929  8.184   3.947   1.00 27.89 ?  144  LYS C O   1 
ATOM   5405  C  CB  . LYS C  1 120 ? 39.136  11.183  4.283   1.00 28.02 ?  144  LYS C CB  1 
ATOM   5406  C  CG  . LYS C  1 120 ? 40.142  11.787  5.244   1.00 28.27 ?  144  LYS C CG  1 
ATOM   5407  C  CD  . LYS C  1 120 ? 39.489  12.851  6.109   1.00 29.25 ?  144  LYS C CD  1 
ATOM   5408  C  CE  . LYS C  1 120 ? 40.148  12.922  7.470   1.00 29.80 ?  144  LYS C CE  1 
ATOM   5409  N  NZ  . LYS C  1 120 ? 39.870  11.684  8.249   1.00 30.95 ?  144  LYS C NZ  1 
ATOM   5410  N  N   . LEU C  1 121 ? 37.922  9.290   1.984   1.00 27.82 ?  145  LEU C N   1 
ATOM   5411  C  CA  . LEU C  1 121 ? 36.874  8.470   1.374   1.00 28.02 ?  145  LEU C CA  1 
ATOM   5412  C  C   . LEU C  1 121 ? 37.335  7.015   1.218   1.00 28.12 ?  145  LEU C C   1 
ATOM   5413  O  O   . LEU C  1 121 ? 36.601  6.086   1.553   1.00 28.05 ?  145  LEU C O   1 
ATOM   5414  C  CB  . LEU C  1 121 ? 36.443  9.062   0.021   1.00 27.80 ?  145  LEU C CB  1 
ATOM   5415  C  CG  . LEU C  1 121 ? 35.743  8.212   -1.055  1.00 28.12 ?  145  LEU C CG  1 
ATOM   5416  C  CD1 . LEU C  1 121 ? 34.433  7.585   -0.581  1.00 27.55 ?  145  LEU C CD1 1 
ATOM   5417  C  CD2 . LEU C  1 121 ? 35.502  9.048   -2.305  1.00 28.01 ?  145  LEU C CD2 1 
ATOM   5418  N  N   . GLU C  1 122 ? 38.555  6.834   0.718   1.00 28.37 ?  146  GLU C N   1 
ATOM   5419  C  CA  . GLU C  1 122 ? 39.115  5.502   0.495   1.00 28.75 ?  146  GLU C CA  1 
ATOM   5420  C  C   . GLU C  1 122 ? 39.298  4.731   1.806   1.00 28.83 ?  146  GLU C C   1 
ATOM   5421  O  O   . GLU C  1 122 ? 39.047  3.524   1.864   1.00 28.92 ?  146  GLU C O   1 
ATOM   5422  C  CB  . GLU C  1 122 ? 40.424  5.594   -0.295  1.00 28.75 ?  146  GLU C CB  1 
ATOM   5423  C  CG  . GLU C  1 122 ? 40.218  5.997   -1.764  1.00 29.30 ?  146  GLU C CG  1 
ATOM   5424  C  CD  . GLU C  1 122 ? 41.459  6.588   -2.414  1.00 30.46 ?  146  GLU C CD  1 
ATOM   5425  O  OE1 . GLU C  1 122 ? 42.516  6.650   -1.754  1.00 32.16 ?  146  GLU C OE1 1 
ATOM   5426  O  OE2 . GLU C  1 122 ? 41.380  7.001   -3.592  1.00 31.18 -1 146  GLU C OE2 1 
ATOM   5427  N  N   . GLU C  1 123 ? 39.708  5.441   2.856   1.00 28.90 ?  147  GLU C N   1 
ATOM   5428  C  CA  . GLU C  1 123 ? 39.809  4.860   4.194   1.00 29.09 ?  147  GLU C CA  1 
ATOM   5429  C  C   . GLU C  1 123 ? 38.434  4.419   4.704   1.00 28.78 ?  147  GLU C C   1 
ATOM   5430  O  O   . GLU C  1 123 ? 38.309  3.360   5.323   1.00 28.64 ?  147  GLU C O   1 
ATOM   5431  C  CB  . GLU C  1 123 ? 40.466  5.847   5.168   1.00 29.31 ?  147  GLU C CB  1 
ATOM   5432  C  CG  . GLU C  1 123 ? 40.630  5.312   6.585   1.00 30.39 ?  147  GLU C CG  1 
ATOM   5433  C  CD  . GLU C  1 123 ? 41.546  6.168   7.431   1.00 32.02 ?  147  GLU C CD  1 
ATOM   5434  O  OE1 . GLU C  1 123 ? 42.780  6.019   7.315   1.00 33.25 ?  147  GLU C OE1 1 
ATOM   5435  O  OE2 . GLU C  1 123 ? 41.031  6.981   8.223   1.00 32.71 -1 147  GLU C OE2 1 
ATOM   5436  N  N   . VAL C  1 124 ? 37.410  5.226   4.430   1.00 28.43 ?  148  VAL C N   1 
ATOM   5437  C  CA  . VAL C  1 124 ? 36.025  4.857   4.745   1.00 28.32 ?  148  VAL C CA  1 
ATOM   5438  C  C   . VAL C  1 124 ? 35.627  3.555   4.039   1.00 28.18 ?  148  VAL C C   1 
ATOM   5439  O  O   . VAL C  1 124 ? 35.044  2.661   4.655   1.00 27.97 ?  148  VAL C O   1 
ATOM   5440  C  CB  . VAL C  1 124 ? 35.027  6.003   4.403   1.00 28.27 ?  148  VAL C CB  1 
ATOM   5441  C  CG1 . VAL C  1 124 ? 33.601  5.478   4.270   1.00 27.95 ?  148  VAL C CG1 1 
ATOM   5442  C  CG2 . VAL C  1 124 ? 35.102  7.114   5.456   1.00 28.08 ?  148  VAL C CG2 1 
ATOM   5443  N  N   . GLU C  1 125 ? 35.955  3.457   2.753   1.00 28.34 ?  149  GLU C N   1 
ATOM   5444  C  CA  . GLU C  1 125 ? 35.655  2.264   1.963   1.00 28.54 ?  149  GLU C CA  1 
ATOM   5445  C  C   . GLU C  1 125 ? 36.410  1.040   2.492   1.00 28.67 ?  149  GLU C C   1 
ATOM   5446  O  O   . GLU C  1 125 ? 35.831  -0.038  2.622   1.00 28.74 ?  149  GLU C O   1 
ATOM   5447  C  CB  . GLU C  1 125 ? 35.934  2.516   0.474   1.00 28.51 ?  149  GLU C CB  1 
ATOM   5448  C  CG  . GLU C  1 125 ? 35.009  3.570   -0.141  1.00 28.54 ?  149  GLU C CG  1 
ATOM   5449  C  CD  . GLU C  1 125 ? 35.339  3.903   -1.585  1.00 28.40 ?  149  GLU C CD  1 
ATOM   5450  O  OE1 . GLU C  1 125 ? 36.527  4.115   -1.907  1.00 28.76 ?  149  GLU C OE1 1 
ATOM   5451  O  OE2 . GLU C  1 125 ? 34.398  3.967   -2.402  1.00 28.17 -1 149  GLU C OE2 1 
ATOM   5452  N  N   . ASN C  1 126 ? 37.686  1.224   2.831   1.00 28.83 ?  150  ASN C N   1 
ATOM   5453  C  CA  . ASN C  1 126 ? 38.489  0.185   3.484   1.00 28.97 ?  150  ASN C CA  1 
ATOM   5454  C  C   . ASN C  1 126 ? 37.807  -0.355  4.750   1.00 28.93 ?  150  ASN C C   1 
ATOM   5455  O  O   . ASN C  1 126 ? 37.715  -1.572  4.941   1.00 28.83 ?  150  ASN C O   1 
ATOM   5456  C  CB  . ASN C  1 126 ? 39.893  0.721   3.809   1.00 29.13 ?  150  ASN C CB  1 
ATOM   5457  C  CG  . ASN C  1 126 ? 40.845  -0.366  4.288   1.00 29.61 ?  150  ASN C CG  1 
ATOM   5458  O  OD1 . ASN C  1 126 ? 40.982  -0.599  5.486   1.00 31.02 ?  150  ASN C OD1 1 
ATOM   5459  N  ND2 . ASN C  1 126 ? 41.502  -1.038  3.352   1.00 30.05 ?  150  ASN C ND2 1 
ATOM   5460  N  N   . ASN C  1 127 ? 37.324  0.559   5.596   1.00 28.89 ?  151  ASN C N   1 
ATOM   5461  C  CA  . ASN C  1 127 ? 36.593  0.210   6.817   1.00 28.80 ?  151  ASN C CA  1 
ATOM   5462  C  C   . ASN C  1 127 ? 35.355  -0.641  6.548   1.00 28.79 ?  151  ASN C C   1 
ATOM   5463  O  O   . ASN C  1 127 ? 35.156  -1.674  7.190   1.00 28.78 ?  151  ASN C O   1 
ATOM   5464  C  CB  . ASN C  1 127 ? 36.181  1.472   7.584   1.00 28.94 ?  151  ASN C CB  1 
ATOM   5465  C  CG  . ASN C  1 127 ? 37.364  2.212   8.186   1.00 29.19 ?  151  ASN C CG  1 
ATOM   5466  O  OD1 . ASN C  1 127 ? 38.305  1.602   8.698   1.00 30.48 ?  151  ASN C OD1 1 
ATOM   5467  N  ND2 . ASN C  1 127 ? 37.308  3.536   8.149   1.00 28.41 ?  151  ASN C ND2 1 
ATOM   5468  N  N   . LEU C  1 128 ? 34.537  -0.201  5.591   1.00 28.73 ?  152  LEU C N   1 
ATOM   5469  C  CA  . LEU C  1 128 ? 33.279  -0.867  5.255   1.00 28.81 ?  152  LEU C CA  1 
ATOM   5470  C  C   . LEU C  1 128 ? 33.493  -2.249  4.642   1.00 28.96 ?  152  LEU C C   1 
ATOM   5471  O  O   . LEU C  1 128 ? 32.768  -3.192  4.954   1.00 28.71 ?  152  LEU C O   1 
ATOM   5472  C  CB  . LEU C  1 128 ? 32.444  0.007   4.310   1.00 28.68 ?  152  LEU C CB  1 
ATOM   5473  C  CG  . LEU C  1 128 ? 31.876  1.307   4.895   1.00 28.65 ?  152  LEU C CG  1 
ATOM   5474  C  CD1 . LEU C  1 128 ? 31.175  2.124   3.815   1.00 28.38 ?  152  LEU C CD1 1 
ATOM   5475  C  CD2 . LEU C  1 128 ? 30.941  1.022   6.073   1.00 27.51 ?  152  LEU C CD2 1 
ATOM   5476  N  N   . ARG C  1 129 ? 34.496  -2.349  3.772   1.00 29.31 ?  153  ARG C N   1 
ATOM   5477  C  CA  . ARG C  1 129 ? 34.865  -3.606  3.133   1.00 29.71 ?  153  ARG C CA  1 
ATOM   5478  C  C   . ARG C  1 129 ? 35.339  -4.629  4.167   1.00 29.95 ?  153  ARG C C   1 
ATOM   5479  O  O   . ARG C  1 129 ? 34.938  -5.789  4.122   1.00 29.96 ?  153  ARG C O   1 
ATOM   5480  C  CB  . ARG C  1 129 ? 35.907  -3.357  2.038   1.00 29.64 ?  153  ARG C CB  1 
ATOM   5481  C  CG  . ARG C  1 129 ? 35.415  -2.338  1.008   1.00 30.03 ?  153  ARG C CG  1 
ATOM   5482  C  CD  . ARG C  1 129 ? 36.098  -2.460  -0.328  1.00 30.07 ?  153  ARG C CD  1 
ATOM   5483  N  NE  . ARG C  1 129 ? 37.097  -1.433  -0.595  1.00 30.52 ?  153  ARG C NE  1 
ATOM   5484  C  CZ  . ARG C  1 129 ? 36.987  -0.488  -1.528  1.00 29.77 ?  153  ARG C CZ  1 
ATOM   5485  N  NH1 . ARG C  1 129 ? 35.909  -0.411  -2.297  1.00 29.01 ?  153  ARG C NH1 1 
ATOM   5486  N  NH2 . ARG C  1 129 ? 37.968  0.387   -1.690  1.00 29.17 ?  153  ARG C NH2 1 
ATOM   5487  N  N   . SER C  1 130 ? 36.156  -4.172  5.116   1.00 30.42 ?  154  SER C N   1 
ATOM   5488  C  CA  . SER C  1 130 ? 36.582  -4.977  6.265   1.00 30.58 ?  154  SER C CA  1 
ATOM   5489  C  C   . SER C  1 130 ? 35.386  -5.475  7.084   1.00 31.01 ?  154  SER C C   1 
ATOM   5490  O  O   . SER C  1 130 ? 35.417  -6.578  7.640   1.00 31.06 ?  154  SER C O   1 
ATOM   5491  C  CB  . SER C  1 130 ? 37.539  -4.163  7.148   1.00 30.51 ?  154  SER C CB  1 
ATOM   5492  O  OG  . SER C  1 130 ? 37.750  -4.773  8.414   1.00 30.29 ?  154  SER C OG  1 
ATOM   5493  N  N   . MET C  1 131 ? 34.333  -4.662  7.146   1.00 31.33 ?  155  MET C N   1 
ATOM   5494  C  CA  . MET C  1 131 ? 33.132  -5.000  7.914   1.00 31.84 ?  155  MET C CA  1 
ATOM   5495  C  C   . MET C  1 131 ? 32.116  -5.813  7.113   1.00 31.84 ?  155  MET C C   1 
ATOM   5496  O  O   . MET C  1 131 ? 31.159  -6.351  7.680   1.00 31.96 ?  155  MET C O   1 
ATOM   5497  C  CB  . MET C  1 131 ? 32.476  -3.731  8.459   1.00 32.08 ?  155  MET C CB  1 
ATOM   5498  C  CG  . MET C  1 131 ? 33.353  -2.960  9.433   1.00 32.91 ?  155  MET C CG  1 
ATOM   5499  S  SD  . MET C  1 131 ? 32.784  -1.273  9.692   1.00 34.19 ?  155  MET C SD  1 
ATOM   5500  C  CE  . MET C  1 131 ? 31.366  -1.591  10.735  1.00 35.27 ?  155  MET C CE  1 
ATOM   5501  N  N   . GLY C  1 132 ? 32.329  -5.903  5.802   1.00 31.81 ?  156  GLY C N   1 
ATOM   5502  C  CA  . GLY C  1 132 ? 31.427  -6.635  4.917   1.00 31.84 ?  156  GLY C CA  1 
ATOM   5503  C  C   . GLY C  1 132 ? 30.172  -5.863  4.544   1.00 31.86 ?  156  GLY C C   1 
ATOM   5504  O  O   . GLY C  1 132 ? 29.142  -6.463  4.231   1.00 31.84 ?  156  GLY C O   1 
ATOM   5505  N  N   . LYS C  1 133 ? 30.257  -4.533  4.577   1.00 31.84 ?  157  LYS C N   1 
ATOM   5506  C  CA  . LYS C  1 133 ? 29.132  -3.670  4.199   1.00 31.83 ?  157  LYS C CA  1 
ATOM   5507  C  C   . LYS C  1 133 ? 29.289  -3.191  2.759   1.00 31.60 ?  157  LYS C C   1 
ATOM   5508  O  O   . LYS C  1 133 ? 28.338  -2.694  2.144   1.00 31.65 ?  157  LYS C O   1 
ATOM   5509  C  CB  . LYS C  1 133 ? 29.017  -2.462  5.145   1.00 31.95 ?  157  LYS C CB  1 
ATOM   5510  C  CG  . LYS C  1 133 ? 28.906  -2.793  6.638   1.00 32.67 ?  157  LYS C CG  1 
ATOM   5511  C  CD  . LYS C  1 133 ? 27.691  -3.655  6.979   1.00 33.87 ?  157  LYS C CD  1 
ATOM   5512  C  CE  . LYS C  1 133 ? 26.417  -2.832  7.114   1.00 34.85 ?  157  LYS C CE  1 
ATOM   5513  N  NZ  . LYS C  1 133 ? 25.272  -3.681  7.553   1.00 35.04 ?  157  LYS C NZ  1 
ATOM   5514  N  N   . LEU C  1 134 ? 30.500  -3.352  2.234   1.00 31.30 ?  158  LEU C N   1 
ATOM   5515  C  CA  . LEU C  1 134 ? 30.846  -2.900  0.899   1.00 31.17 ?  158  LEU C CA  1 
ATOM   5516  C  C   . LEU C  1 134 ? 31.695  -3.966  0.214   1.00 31.21 ?  158  LEU C C   1 
ATOM   5517  O  O   . LEU C  1 134 ? 32.534  -4.603  0.855   1.00 31.16 ?  158  LEU C O   1 
ATOM   5518  C  CB  . LEU C  1 134 ? 31.619  -1.577  0.984   1.00 31.04 ?  158  LEU C CB  1 
ATOM   5519  C  CG  . LEU C  1 134 ? 31.863  -0.756  -0.287  1.00 30.98 ?  158  LEU C CG  1 
ATOM   5520  C  CD1 . LEU C  1 134 ? 30.575  -0.126  -0.804  1.00 30.40 ?  158  LEU C CD1 1 
ATOM   5521  C  CD2 . LEU C  1 134 ? 32.914  0.313   -0.033  1.00 29.88 ?  158  LEU C CD2 1 
ATOM   5522  N  N   . GLY C  1 135 ? 31.465  -4.164  -1.083  1.00 31.12 ?  159  GLY C N   1 
ATOM   5523  C  CA  . GLY C  1 135 ? 32.284  -5.079  -1.877  1.00 31.08 ?  159  GLY C CA  1 
ATOM   5524  C  C   . GLY C  1 135 ? 33.694  -4.541  -2.034  1.00 31.00 ?  159  GLY C C   1 
ATOM   5525  O  O   . GLY C  1 135 ? 33.891  -3.323  -2.076  1.00 31.05 ?  159  GLY C O   1 
ATOM   5526  N  N   . GLU C  1 136 ? 34.668  -5.448  -2.123  1.00 30.98 ?  160  GLU C N   1 
ATOM   5527  C  CA  . GLU C  1 136 ? 36.092  -5.094  -2.250  1.00 30.99 ?  160  GLU C CA  1 
ATOM   5528  C  C   . GLU C  1 136 ? 36.375  -4.090  -3.371  1.00 30.64 ?  160  GLU C C   1 
ATOM   5529  O  O   . GLU C  1 136 ? 37.285  -3.267  -3.263  1.00 30.47 ?  160  GLU C O   1 
ATOM   5530  C  CB  . GLU C  1 136 ? 36.959  -6.344  -2.447  1.00 31.32 ?  160  GLU C CB  1 
ATOM   5531  C  CG  . GLU C  1 136 ? 37.015  -7.285  -1.244  1.00 33.08 ?  160  GLU C CG  1 
ATOM   5532  C  CD  . GLU C  1 136 ? 35.942  -8.366  -1.279  1.00 35.46 ?  160  GLU C CD  1 
ATOM   5533  O  OE1 . GLU C  1 136 ? 35.796  -9.088  -0.272  1.00 36.59 ?  160  GLU C OE1 1 
ATOM   5534  O  OE2 . GLU C  1 136 ? 35.246  -8.497  -2.309  1.00 36.63 -1 160  GLU C OE2 1 
ATOM   5535  N  N   . LYS C  1 137 ? 35.590  -4.160  -4.442  1.00 30.29 ?  161  LYS C N   1 
ATOM   5536  C  CA  . LYS C  1 137 ? 35.782  -3.279  -5.593  1.00 30.05 ?  161  LYS C CA  1 
ATOM   5537  C  C   . LYS C  1 137 ? 34.533  -2.451  -5.904  1.00 29.92 ?  161  LYS C C   1 
ATOM   5538  O  O   . LYS C  1 137 ? 34.437  -1.822  -6.960  1.00 30.01 ?  161  LYS C O   1 
ATOM   5539  C  CB  . LYS C  1 137 ? 36.233  -4.088  -6.817  1.00 29.84 ?  161  LYS C CB  1 
ATOM   5540  C  CG  . LYS C  1 137 ? 37.573  -4.790  -6.637  1.00 29.43 ?  161  LYS C CG  1 
ATOM   5541  C  CD  . LYS C  1 137 ? 38.682  -3.792  -6.360  1.00 28.77 ?  161  LYS C CD  1 
ATOM   5542  C  CE  . LYS C  1 137 ? 39.907  -4.461  -5.786  1.00 28.25 ?  161  LYS C CE  1 
ATOM   5543  N  NZ  . LYS C  1 137 ? 41.026  -3.484  -5.671  1.00 27.73 ?  161  LYS C NZ  1 
ATOM   5544  N  N   . GLU C  1 138 ? 33.583  -2.470  -4.974  1.00 29.80 ?  162  GLU C N   1 
ATOM   5545  C  CA  . GLU C  1 138 ? 32.373  -1.668  -5.062  1.00 29.57 ?  162  GLU C CA  1 
ATOM   5546  C  C   . GLU C  1 138 ? 32.645  -0.295  -4.455  1.00 29.51 ?  162  GLU C C   1 
ATOM   5547  O  O   . GLU C  1 138 ? 33.031  -0.198  -3.290  1.00 29.62 ?  162  GLU C O   1 
ATOM   5548  C  CB  . GLU C  1 138 ? 31.229  -2.365  -4.313  1.00 29.57 ?  162  GLU C CB  1 
ATOM   5549  C  CG  . GLU C  1 138 ? 29.908  -1.594  -4.300  1.00 29.39 ?  162  GLU C CG  1 
ATOM   5550  C  CD  . GLU C  1 138 ? 28.866  -2.185  -3.360  1.00 29.47 ?  162  GLU C CD  1 
ATOM   5551  O  OE1 . GLU C  1 138 ? 29.179  -3.128  -2.597  1.00 28.87 ?  162  GLU C OE1 1 
ATOM   5552  O  OE2 . GLU C  1 138 ? 27.718  -1.695  -3.386  1.00 30.32 -1 162  GLU C OE2 1 
ATOM   5553  N  N   . THR C  1 139 ? 32.466  0.759   -5.247  1.00 29.29 ?  163  THR C N   1 
ATOM   5554  C  CA  . THR C  1 139 ? 32.573  2.120   -4.728  1.00 29.33 ?  163  THR C CA  1 
ATOM   5555  C  C   . THR C  1 139 ? 31.341  2.453   -3.894  1.00 29.07 ?  163  THR C C   1 
ATOM   5556  O  O   . THR C  1 139 ? 30.224  2.043   -4.230  1.00 28.99 ?  163  THR C O   1 
ATOM   5557  C  CB  . THR C  1 139 ? 32.716  3.179   -5.845  1.00 29.43 ?  163  THR C CB  1 
ATOM   5558  O  OG1 . THR C  1 139 ? 31.634  3.054   -6.775  1.00 30.15 ?  163  THR C OG1 1 
ATOM   5559  C  CG2 . THR C  1 139 ? 34.046  3.033   -6.585  1.00 29.61 ?  163  THR C CG2 1 
ATOM   5560  N  N   . LEU C  1 140 ? 31.559  3.175   -2.797  1.00 28.68 ?  164  LEU C N   1 
ATOM   5561  C  CA  . LEU C  1 140 ? 30.471  3.719   -1.996  1.00 28.34 ?  164  LEU C CA  1 
ATOM   5562  C  C   . LEU C  1 140 ? 29.802  4.840   -2.788  1.00 28.29 ?  164  LEU C C   1 
ATOM   5563  O  O   . LEU C  1 140 ? 30.404  5.894   -3.011  1.00 28.22 ?  164  LEU C O   1 
ATOM   5564  C  CB  . LEU C  1 140 ? 31.002  4.244   -0.655  1.00 28.22 ?  164  LEU C CB  1 
ATOM   5565  C  CG  . LEU C  1 140 ? 29.989  4.786   0.361   1.00 27.89 ?  164  LEU C CG  1 
ATOM   5566  C  CD1 . LEU C  1 140 ? 29.052  3.692   0.871   1.00 26.88 ?  164  LEU C CD1 1 
ATOM   5567  C  CD2 . LEU C  1 140 ? 30.713  5.461   1.519   1.00 26.72 ?  164  LEU C CD2 1 
ATOM   5568  N  N   . LYS C  1 141 ? 28.564  4.601   -3.215  1.00 27.92 ?  165  LYS C N   1 
ATOM   5569  C  CA  . LYS C  1 141 ? 27.860  5.517   -4.117  1.00 27.91 ?  165  LYS C CA  1 
ATOM   5570  C  C   . LYS C  1 141 ? 27.507  6.853   -3.463  1.00 27.73 ?  165  LYS C C   1 
ATOM   5571  O  O   . LYS C  1 141 ? 27.715  7.920   -4.053  1.00 27.85 ?  165  LYS C O   1 
ATOM   5572  C  CB  . LYS C  1 141 ? 26.606  4.847   -4.703  1.00 28.04 ?  165  LYS C CB  1 
ATOM   5573  C  CG  . LYS C  1 141 ? 26.878  3.522   -5.447  1.00 28.03 ?  165  LYS C CG  1 
ATOM   5574  C  CD  . LYS C  1 141 ? 27.858  3.716   -6.602  1.00 28.45 ?  165  LYS C CD  1 
ATOM   5575  C  CE  . LYS C  1 141 ? 28.142  2.415   -7.351  1.00 29.18 ?  165  LYS C CE  1 
ATOM   5576  N  NZ  . LYS C  1 141 ? 29.132  1.539   -6.661  1.00 27.47 ?  165  LYS C NZ  1 
ATOM   5577  N  N   . GLU C  1 142 ? 26.978  6.780   -2.246  1.00 27.28 ?  166  GLU C N   1 
ATOM   5578  C  CA  . GLU C  1 142 ? 26.580  7.957   -1.488  1.00 26.93 ?  166  GLU C CA  1 
ATOM   5579  C  C   . GLU C  1 142 ? 26.386  7.596   -0.024  1.00 26.64 ?  166  GLU C C   1 
ATOM   5580  O  O   . GLU C  1 142 ? 26.394  6.419   0.343   1.00 26.33 ?  166  GLU C O   1 
ATOM   5581  C  CB  . GLU C  1 142 ? 25.278  8.557   -2.044  1.00 27.05 ?  166  GLU C CB  1 
ATOM   5582  C  CG  . GLU C  1 142 ? 24.071  7.621   -1.971  1.00 26.86 ?  166  GLU C CG  1 
ATOM   5583  C  CD  . GLU C  1 142 ? 22.747  8.315   -2.263  1.00 26.71 ?  166  GLU C CD  1 
ATOM   5584  O  OE1 . GLU C  1 142 ? 22.728  9.306   -3.028  1.00 25.83 ?  166  GLU C OE1 1 
ATOM   5585  O  OE2 . GLU C  1 142 ? 21.719  7.852   -1.726  1.00 26.04 -1 166  GLU C OE2 1 
ATOM   5586  N  N   . VAL C  1 143 ? 26.220  8.625   0.801   1.00 26.16 ?  167  VAL C N   1 
ATOM   5587  C  CA  . VAL C  1 143 ? 25.759  8.463   2.166   1.00 25.75 ?  167  VAL C CA  1 
ATOM   5588  C  C   . VAL C  1 143 ? 24.441  9.226   2.243   1.00 25.75 ?  167  VAL C C   1 
ATOM   5589  O  O   . VAL C  1 143 ? 24.425  10.453  2.409   1.00 25.72 ?  167  VAL C O   1 
ATOM   5590  C  CB  . VAL C  1 143 ? 26.780  9.010   3.190   1.00 25.95 ?  167  VAL C CB  1 
ATOM   5591  C  CG1 . VAL C  1 143 ? 26.363  8.658   4.618   1.00 25.49 ?  167  VAL C CG1 1 
ATOM   5592  C  CG2 . VAL C  1 143 ? 28.180  8.480   2.889   1.00 25.83 ?  167  VAL C CG2 1 
ATOM   5593  N  N   . GLY C  1 144 ? 23.340  8.494   2.087   1.00 25.46 ?  168  GLY C N   1 
ATOM   5594  C  CA  . GLY C  1 144 ? 22.011  9.096   2.019   1.00 25.23 ?  168  GLY C CA  1 
ATOM   5595  C  C   . GLY C  1 144 ? 21.169  8.851   3.251   1.00 24.92 ?  168  GLY C C   1 
ATOM   5596  O  O   . GLY C  1 144 ? 21.637  8.250   4.222   1.00 25.17 ?  168  GLY C O   1 
ATOM   5597  N  N   . CYS C  1 145 ? 19.924  9.319   3.205   1.00 24.65 ?  169  CYS C N   1 
ATOM   5598  C  CA  . CYS C  1 145 ? 18.979  9.181   4.316   1.00 24.52 ?  169  CYS C CA  1 
ATOM   5599  C  C   . CYS C  1 145 ? 18.974  7.761   4.880   1.00 24.63 ?  169  CYS C C   1 
ATOM   5600  O  O   . CYS C  1 145 ? 19.139  7.572   6.090   1.00 24.40 ?  169  CYS C O   1 
ATOM   5601  C  CB  . CYS C  1 145 ? 17.554  9.562   3.883   1.00 24.46 ?  169  CYS C CB  1 
ATOM   5602  S  SG  . CYS C  1 145 ? 17.400  10.974  2.746   1.00 24.57 ?  169  CYS C SG  1 
ATOM   5603  N  N   . ILE C  1 146 ? 18.805  6.778   3.989   1.00 24.68 ?  170  ILE C N   1 
ATOM   5604  C  CA  . ILE C  1 146 ? 18.684  5.361   4.359   1.00 24.96 ?  170  ILE C CA  1 
ATOM   5605  C  C   . ILE C  1 146 ? 19.940  4.793   5.034   1.00 25.09 ?  170  ILE C C   1 
ATOM   5606  O  O   . ILE C  1 146 ? 19.847  3.889   5.861   1.00 25.35 ?  170  ILE C O   1 
ATOM   5607  C  CB  . ILE C  1 146 ? 18.263  4.474   3.130   1.00 24.95 ?  170  ILE C CB  1 
ATOM   5608  C  CG1 . ILE C  1 146 ? 17.603  3.170   3.596   1.00 24.89 ?  170  ILE C CG1 1 
ATOM   5609  C  CG2 . ILE C  1 146 ? 19.448  4.222   2.187   1.00 24.98 ?  170  ILE C CG2 1 
ATOM   5610  C  CD1 . ILE C  1 146 ? 16.900  2.379   2.498   1.00 24.72 ?  170  ILE C CD1 1 
ATOM   5611  N  N   . ASP C  1 147 ? 21.105  5.333   4.691   1.00 25.38 ?  171  ASP C N   1 
ATOM   5612  C  CA  . ASP C  1 147 ? 22.371  4.832   5.228   1.00 25.55 ?  171  ASP C CA  1 
ATOM   5613  C  C   . ASP C  1 147 ? 22.533  5.144   6.715   1.00 25.78 ?  171  ASP C C   1 
ATOM   5614  O  O   . ASP C  1 147 ? 22.761  4.239   7.523   1.00 25.70 ?  171  ASP C O   1 
ATOM   5615  C  CB  . ASP C  1 147 ? 23.549  5.375   4.416   1.00 25.40 ?  171  ASP C CB  1 
ATOM   5616  C  CG  . ASP C  1 147 ? 23.537  4.882   2.980   1.00 25.31 ?  171  ASP C CG  1 
ATOM   5617  O  OD1 . ASP C  1 147 ? 23.538  3.651   2.772   1.00 25.14 ?  171  ASP C OD1 1 
ATOM   5618  O  OD2 . ASP C  1 147 ? 23.520  5.721   2.060   1.00 24.89 -1 171  ASP C OD2 1 
ATOM   5619  N  N   . CYS C  1 148 ? 22.400  6.420   7.069   1.00 25.91 ?  172  CYS C N   1 
ATOM   5620  C  CA  . CYS C  1 148 ? 22.533  6.851   8.458   1.00 26.35 ?  172  CYS C CA  1 
ATOM   5621  C  C   . CYS C  1 148 ? 21.319  6.461   9.295   1.00 26.49 ?  172  CYS C C   1 
ATOM   5622  O  O   . CYS C  1 148 ? 21.468  6.046   10.443  1.00 26.48 ?  172  CYS C O   1 
ATOM   5623  C  CB  . CYS C  1 148 ? 22.758  8.362   8.544   1.00 26.21 ?  172  CYS C CB  1 
ATOM   5624  S  SG  . CYS C  1 148 ? 24.316  8.966   7.835   1.00 26.33 ?  172  CYS C SG  1 
ATOM   5625  N  N   . HIS C  1 149 ? 20.127  6.586   8.714   1.00 26.96 ?  173  HIS C N   1 
ATOM   5626  C  CA  . HIS C  1 149 ? 18.879  6.370   9.452   1.00 27.54 ?  173  HIS C CA  1 
ATOM   5627  C  C   . HIS C  1 149 ? 18.317  4.934   9.410   1.00 28.13 ?  173  HIS C C   1 
ATOM   5628  O  O   . HIS C  1 149 ? 17.340  4.639   10.102  1.00 28.25 ?  173  HIS C O   1 
ATOM   5629  C  CB  . HIS C  1 149 ? 17.808  7.382   9.017   1.00 27.38 ?  173  HIS C CB  1 
ATOM   5630  C  CG  . HIS C  1 149 ? 18.121  8.804   9.386   1.00 26.93 ?  173  HIS C CG  1 
ATOM   5631  N  ND1 . HIS C  1 149 ? 17.996  9.280   10.673  1.00 25.95 ?  173  HIS C ND1 1 
ATOM   5632  C  CD2 . HIS C  1 149 ? 18.531  9.856   8.634   1.00 25.79 ?  173  HIS C CD2 1 
ATOM   5633  C  CE1 . HIS C  1 149 ? 18.323  10.559  10.701  1.00 25.54 ?  173  HIS C CE1 1 
ATOM   5634  N  NE2 . HIS C  1 149 ? 18.654  10.936  9.478   1.00 25.65 ?  173  HIS C NE2 1 
ATOM   5635  N  N   . VAL C  1 150 ? 18.917  4.047   8.611   1.00 28.75 ?  174  VAL C N   1 
ATOM   5636  C  CA  . VAL C  1 150 ? 18.514  2.625   8.608   1.00 29.49 ?  174  VAL C CA  1 
ATOM   5637  C  C   . VAL C  1 150 ? 19.721  1.682   8.727   1.00 30.04 ?  174  VAL C C   1 
ATOM   5638  O  O   . VAL C  1 150 ? 19.909  1.042   9.758   1.00 29.98 ?  174  VAL C O   1 
ATOM   5639  C  CB  . VAL C  1 150 ? 17.623  2.230   7.373   1.00 29.50 ?  174  VAL C CB  1 
ATOM   5640  C  CG1 . VAL C  1 150 ? 17.166  0.772   7.479   1.00 29.14 ?  174  VAL C CG1 1 
ATOM   5641  C  CG2 . VAL C  1 150 ? 16.405  3.146   7.240   1.00 28.94 ?  174  VAL C CG2 1 
ATOM   5642  N  N   . ASP C  1 151 ? 20.528  1.608   7.670   1.00 30.91 ?  175  ASP C N   1 
ATOM   5643  C  CA  . ASP C  1 151 ? 21.697  0.728   7.626   1.00 31.85 ?  175  ASP C CA  1 
ATOM   5644  C  C   . ASP C  1 151 ? 22.627  1.155   6.500   1.00 32.28 ?  175  ASP C C   1 
ATOM   5645  O  O   . ASP C  1 151 ? 22.175  1.448   5.392   1.00 32.27 ?  175  ASP C O   1 
ATOM   5646  C  CB  . ASP C  1 151 ? 21.272  -0.737  7.436   1.00 32.02 ?  175  ASP C CB  1 
ATOM   5647  C  CG  . ASP C  1 151 ? 22.399  -1.724  7.720   1.00 32.71 ?  175  ASP C CG  1 
ATOM   5648  O  OD1 . ASP C  1 151 ? 23.086  -1.586  8.753   1.00 33.03 ?  175  ASP C OD1 1 
ATOM   5649  O  OD2 . ASP C  1 151 ? 22.591  -2.655  6.909   1.00 34.88 -1 175  ASP C OD2 1 
ATOM   5650  N  N   . VAL C  1 152 ? 23.925  1.182   6.791   1.00 33.08 ?  176  VAL C N   1 
ATOM   5651  C  CA  . VAL C  1 152 ? 24.945  1.593   5.821   1.00 34.00 ?  176  VAL C CA  1 
ATOM   5652  C  C   . VAL C  1 152 ? 24.933  0.723   4.556   1.00 34.58 ?  176  VAL C C   1 
ATOM   5653  O  O   . VAL C  1 152 ? 24.988  -0.506  4.638   1.00 34.57 ?  176  VAL C O   1 
ATOM   5654  C  CB  . VAL C  1 152 ? 26.360  1.612   6.464   1.00 33.96 ?  176  VAL C CB  1 
ATOM   5655  C  CG1 . VAL C  1 152 ? 27.438  1.854   5.414   1.00 34.38 ?  176  VAL C CG1 1 
ATOM   5656  C  CG2 . VAL C  1 152 ? 26.437  2.677   7.555   1.00 33.98 ?  176  VAL C CG2 1 
ATOM   5657  N  N   . ASN C  1 153 ? 24.851  1.386   3.399   1.00 35.50 ?  177  ASN C N   1 
ATOM   5658  C  CA  . ASN C  1 153 ? 24.876  0.751   2.070   1.00 36.45 ?  177  ASN C CA  1 
ATOM   5659  C  C   . ASN C  1 153 ? 23.706  -0.211  1.809   1.00 37.01 ?  177  ASN C C   1 
ATOM   5660  O  O   . ASN C  1 153 ? 23.848  -1.202  1.085   1.00 36.93 ?  177  ASN C O   1 
ATOM   5661  C  CB  . ASN C  1 153 ? 26.240  0.089   1.791   1.00 36.53 ?  177  ASN C CB  1 
ATOM   5662  C  CG  . ASN C  1 153 ? 26.528  -0.066  0.302   1.00 36.98 ?  177  ASN C CG  1 
ATOM   5663  O  OD1 . ASN C  1 153 ? 26.388  0.880   -0.475  1.00 37.37 ?  177  ASN C OD1 1 
ATOM   5664  N  ND2 . ASN C  1 153 ? 26.939  -1.266  -0.100  1.00 37.18 ?  177  ASN C ND2 1 
ATOM   5665  N  N   . LYS C  1 154 ? 22.551  0.100   2.396   1.00 37.70 ?  178  LYS C N   1 
ATOM   5666  C  CA  . LYS C  1 154 ? 21.344  -0.712  2.235   1.00 38.38 ?  178  LYS C CA  1 
ATOM   5667  C  C   . LYS C  1 154 ? 20.801  -0.639  0.806   1.00 38.78 ?  178  LYS C C   1 
ATOM   5668  O  O   . LYS C  1 154 ? 20.715  0.442   0.216   1.00 38.82 ?  178  LYS C O   1 
ATOM   5669  C  CB  . LYS C  1 154 ? 20.274  -0.288  3.243   1.00 38.41 ?  178  LYS C CB  1 
ATOM   5670  C  CG  . LYS C  1 154 ? 19.092  -1.237  3.341   1.00 38.58 ?  178  LYS C CG  1 
ATOM   5671  C  CD  . LYS C  1 154 ? 18.155  -0.820  4.454   1.00 39.07 ?  178  LYS C CD  1 
ATOM   5672  C  CE  . LYS C  1 154 ? 16.802  -1.506  4.351   1.00 39.47 ?  178  LYS C CE  1 
ATOM   5673  N  NZ  . LYS C  1 154 ? 16.866  -2.986  4.514   1.00 39.96 ?  178  LYS C NZ  1 
ATOM   5674  N  N   . LYS C  1 155 ? 20.432  -1.800  0.269   1.00 39.32 ?  179  LYS C N   1 
ATOM   5675  C  CA  . LYS C  1 155 ? 20.028  -1.928  -1.131  1.00 39.77 ?  179  LYS C CA  1 
ATOM   5676  C  C   . LYS C  1 155 ? 18.527  -2.153  -1.300  1.00 39.85 ?  179  LYS C C   1 
ATOM   5677  O  O   . LYS C  1 155 ? 17.974  -1.909  -2.377  1.00 39.93 ?  179  LYS C O   1 
ATOM   5678  C  CB  . LYS C  1 155 ? 20.807  -3.069  -1.804  1.00 40.00 ?  179  LYS C CB  1 
ATOM   5679  C  CG  . LYS C  1 155 ? 22.325  -2.867  -1.856  1.00 40.71 ?  179  LYS C CG  1 
ATOM   5680  C  CD  . LYS C  1 155 ? 22.725  -1.761  -2.840  1.00 41.27 ?  179  LYS C CD  1 
ATOM   5681  C  CE  . LYS C  1 155 ? 24.217  -1.450  -2.763  1.00 41.65 ?  179  LYS C CE  1 
ATOM   5682  N  NZ  . LYS C  1 155 ? 25.083  -2.611  -3.143  1.00 42.02 ?  179  LYS C NZ  1 
ATOM   5683  N  N   . ASP C  1 156 ? 17.875  -2.613  -0.234  1.00 39.93 ?  180  ASP C N   1 
ATOM   5684  C  CA  . ASP C  1 156 ? 16.455  -2.965  -0.281  1.00 39.94 ?  180  ASP C CA  1 
ATOM   5685  C  C   . ASP C  1 156 ? 15.555  -2.033  0.548   1.00 39.76 ?  180  ASP C C   1 
ATOM   5686  O  O   . ASP C  1 156 ? 15.957  -0.924  0.915   1.00 39.75 ?  180  ASP C O   1 
ATOM   5687  C  CB  . ASP C  1 156 ? 16.252  -4.439  0.112   1.00 40.16 ?  180  ASP C CB  1 
ATOM   5688  C  CG  . ASP C  1 156 ? 16.817  -4.772  1.485   1.00 40.93 ?  180  ASP C CG  1 
ATOM   5689  O  OD1 . ASP C  1 156 ? 17.517  -3.926  2.085   1.00 41.94 ?  180  ASP C OD1 1 
ATOM   5690  O  OD2 . ASP C  1 156 ? 16.562  -5.896  1.968   1.00 42.43 -1 180  ASP C OD2 1 
ATOM   5691  N  N   . LYS C  1 157 ? 14.341  -2.500  0.833   1.00 39.39 ?  181  LYS C N   1 
ATOM   5692  C  CA  . LYS C  1 157 ? 13.293  -1.689  1.450   1.00 39.01 ?  181  LYS C CA  1 
ATOM   5693  C  C   . LYS C  1 157 ? 13.436  -1.555  2.964   1.00 38.53 ?  181  LYS C C   1 
ATOM   5694  O  O   . LYS C  1 157 ? 13.937  -2.459  3.631   1.00 38.54 ?  181  LYS C O   1 
ATOM   5695  C  CB  . LYS C  1 157 ? 11.919  -2.276  1.116   1.00 39.17 ?  181  LYS C CB  1 
ATOM   5696  C  CG  . LYS C  1 157 ? 11.542  -2.188  -0.353  1.00 40.23 ?  181  LYS C CG  1 
ATOM   5697  C  CD  . LYS C  1 157 ? 10.301  -3.014  -0.667  1.00 41.71 ?  181  LYS C CD  1 
ATOM   5698  C  CE  . LYS C  1 157 ? 9.860   -2.828  -2.118  1.00 42.65 ?  181  LYS C CE  1 
ATOM   5699  N  NZ  . LYS C  1 157 ? 9.217   -1.499  -2.353  1.00 43.18 ?  181  LYS C NZ  1 
ATOM   5700  N  N   . ALA C  1 158 ? 12.981  -0.419  3.493   1.00 37.88 ?  182  ALA C N   1 
ATOM   5701  C  CA  . ALA C  1 158 ? 12.948  -0.176  4.935   1.00 37.31 ?  182  ALA C CA  1 
ATOM   5702  C  C   . ALA C  1 158 ? 11.535  0.155   5.408   1.00 36.90 ?  182  ALA C C   1 
ATOM   5703  O  O   . ALA C  1 158 ? 10.776  0.832   4.711   1.00 36.79 ?  182  ALA C O   1 
ATOM   5704  C  CB  . ALA C  1 158 ? 13.913  0.944   5.316   1.00 37.26 ?  182  ALA C CB  1 
ATOM   5705  N  N   . ASP C  1 159 ? 11.198  -0.332  6.597   1.00 36.41 ?  183  ASP C N   1 
ATOM   5706  C  CA  . ASP C  1 159 ? 9.908   -0.072  7.229   1.00 35.95 ?  183  ASP C CA  1 
ATOM   5707  C  C   . ASP C  1 159 ? 10.047  1.164   8.120   1.00 35.28 ?  183  ASP C C   1 
ATOM   5708  O  O   . ASP C  1 159 ? 10.778  1.132   9.111   1.00 35.19 ?  183  ASP C O   1 
ATOM   5709  C  CB  . ASP C  1 159 ? 9.488   -1.306  8.046   1.00 36.15 ?  183  ASP C CB  1 
ATOM   5710  C  CG  . ASP C  1 159 ? 8.140   -1.143  8.743   1.00 36.83 ?  183  ASP C CG  1 
ATOM   5711  O  OD1 . ASP C  1 159 ? 7.558   -0.035  8.743   1.00 37.68 ?  183  ASP C OD1 1 
ATOM   5712  O  OD2 . ASP C  1 159 ? 7.660   -2.148  9.310   1.00 37.78 -1 183  ASP C OD2 1 
ATOM   5713  N  N   . HIS C  1 160 ? 9.344   2.242   7.762   1.00 34.55 ?  184  HIS C N   1 
ATOM   5714  C  CA  . HIS C  1 160 ? 9.432   3.531   8.477   1.00 33.87 ?  184  HIS C CA  1 
ATOM   5715  C  C   . HIS C  1 160 ? 9.101   3.389   9.966   1.00 33.74 ?  184  HIS C C   1 
ATOM   5716  O  O   . HIS C  1 160 ? 9.685   4.081   10.803  1.00 33.74 ?  184  HIS C O   1 
ATOM   5717  C  CB  . HIS C  1 160 ? 8.520   4.586   7.823   1.00 33.65 ?  184  HIS C CB  1 
ATOM   5718  C  CG  . HIS C  1 160 ? 9.073   5.984   7.841   1.00 32.67 ?  184  HIS C CG  1 
ATOM   5719  N  ND1 . HIS C  1 160 ? 9.053   6.782   8.965   1.00 31.72 ?  184  HIS C ND1 1 
ATOM   5720  C  CD2 . HIS C  1 160 ? 9.633   6.735   6.861   1.00 31.58 ?  184  HIS C CD2 1 
ATOM   5721  C  CE1 . HIS C  1 160 ? 9.590   7.957   8.681   1.00 31.87 ?  184  HIS C CE1 1 
ATOM   5722  N  NE2 . HIS C  1 160 ? 9.949   7.958   7.409   1.00 30.99 ?  184  HIS C NE2 1 
ATOM   5723  N  N   . THR C  1 161 ? 8.187   2.473   10.289  1.00 33.37 ?  185  THR C N   1 
ATOM   5724  C  CA  . THR C  1 161 ? 7.725   2.270   11.666  1.00 33.09 ?  185  THR C CA  1 
ATOM   5725  C  C   . THR C  1 161 ? 8.612   1.348   12.515  1.00 32.93 ?  185  THR C C   1 
ATOM   5726  O  O   . THR C  1 161 ? 8.359   1.181   13.709  1.00 32.91 ?  185  THR C O   1 
ATOM   5727  C  CB  . THR C  1 161 ? 6.274   1.710   11.708  1.00 33.24 ?  185  THR C CB  1 
ATOM   5728  O  OG1 . THR C  1 161 ? 6.239   0.411   11.099  1.00 33.29 ?  185  THR C OG1 1 
ATOM   5729  C  CG2 . THR C  1 161 ? 5.301   2.641   10.992  1.00 33.02 ?  185  THR C CG2 1 
ATOM   5730  N  N   . LYS C  1 162 ? 9.645   0.760   11.912  1.00 32.79 ?  186  LYS C N   1 
ATOM   5731  C  CA  . LYS C  1 162 ? 10.439  -0.275  12.582  1.00 32.80 ?  186  LYS C CA  1 
ATOM   5732  C  C   . LYS C  1 162 ? 11.956  -0.110  12.414  1.00 32.61 ?  186  LYS C C   1 
ATOM   5733  O  O   . LYS C  1 162 ? 12.722  -0.374  13.347  1.00 32.61 ?  186  LYS C O   1 
ATOM   5734  C  CB  . LYS C  1 162 ? 10.006  -1.665  12.083  1.00 33.09 ?  186  LYS C CB  1 
ATOM   5735  C  CG  . LYS C  1 162 ? 10.661  -2.851  12.801  1.00 33.86 ?  186  LYS C CG  1 
ATOM   5736  C  CD  . LYS C  1 162 ? 10.469  -4.168  12.041  1.00 35.86 ?  186  LYS C CD  1 
ATOM   5737  C  CE  . LYS C  1 162 ? 9.047   -4.720  12.170  1.00 36.85 ?  186  LYS C CE  1 
ATOM   5738  N  NZ  . LYS C  1 162 ? 8.880   -6.037  11.476  1.00 36.81 ?  186  LYS C NZ  1 
ATOM   5739  N  N   . ASP C  1 163 ? 12.380  0.319   11.226  1.00 32.15 ?  187  ASP C N   1 
ATOM   5740  C  CA  . ASP C  1 163 ? 13.799  0.324   10.859  1.00 31.82 ?  187  ASP C CA  1 
ATOM   5741  C  C   . ASP C  1 163 ? 14.489  1.684   11.011  1.00 31.56 ?  187  ASP C C   1 
ATOM   5742  O  O   . ASP C  1 163 ? 15.720  1.759   10.965  1.00 31.41 ?  187  ASP C O   1 
ATOM   5743  C  CB  . ASP C  1 163 ? 13.982  -0.202  9.427   1.00 31.76 ?  187  ASP C CB  1 
ATOM   5744  C  CG  . ASP C  1 163 ? 13.340  -1.571  9.211   1.00 32.19 ?  187  ASP C CG  1 
ATOM   5745  O  OD1 . ASP C  1 163 ? 13.212  -2.345  10.189  1.00 32.13 ?  187  ASP C OD1 1 
ATOM   5746  O  OD2 . ASP C  1 163 ? 12.962  -1.870  8.056   1.00 32.22 -1 187  ASP C OD2 1 
ATOM   5747  N  N   . ILE C  1 164 ? 13.703  2.747   11.182  1.00 31.11 ?  188  ILE C N   1 
ATOM   5748  C  CA  . ILE C  1 164 ? 14.257  4.095   11.334  1.00 30.82 ?  188  ILE C CA  1 
ATOM   5749  C  C   . ILE C  1 164 ? 14.939  4.252   12.690  1.00 30.49 ?  188  ILE C C   1 
ATOM   5750  O  O   . ILE C  1 164 ? 14.356  3.947   13.732  1.00 30.43 ?  188  ILE C O   1 
ATOM   5751  C  CB  . ILE C  1 164 ? 13.182  5.212   11.129  1.00 30.81 ?  188  ILE C CB  1 
ATOM   5752  C  CG1 . ILE C  1 164 ? 12.635  5.202   9.695   1.00 30.86 ?  188  ILE C CG1 1 
ATOM   5753  C  CG2 . ILE C  1 164 ? 13.736  6.599   11.488  1.00 30.90 ?  188  ILE C CG2 1 
ATOM   5754  C  CD1 . ILE C  1 164 ? 13.672  5.371   8.599   1.00 29.82 ?  188  ILE C CD1 1 
ATOM   5755  N  N   . ARG C  1 165 ? 16.185  4.712   12.657  1.00 30.18 ?  189  ARG C N   1 
ATOM   5756  C  CA  . ARG C  1 165 ? 16.936  5.020   13.871  1.00 29.88 ?  189  ARG C CA  1 
ATOM   5757  C  C   . ARG C  1 165 ? 17.410  6.478   13.820  1.00 29.41 ?  189  ARG C C   1 
ATOM   5758  O  O   . ARG C  1 165 ? 17.466  7.084   12.748  1.00 29.44 ?  189  ARG C O   1 
ATOM   5759  C  CB  . ARG C  1 165 ? 18.138  4.073   14.010  1.00 29.85 ?  189  ARG C CB  1 
ATOM   5760  C  CG  . ARG C  1 165 ? 19.211  4.304   12.949  1.00 30.29 ?  189  ARG C CG  1 
ATOM   5761  C  CD  . ARG C  1 165 ? 20.331  3.281   12.969  1.00 30.64 ?  189  ARG C CD  1 
ATOM   5762  N  NE  . ARG C  1 165 ? 21.195  3.465   11.800  1.00 30.63 ?  189  ARG C NE  1 
ATOM   5763  C  CZ  . ARG C  1 165 ? 22.122  2.603   11.394  1.00 31.37 ?  189  ARG C CZ  1 
ATOM   5764  N  NH1 . ARG C  1 165 ? 22.325  1.472   12.060  1.00 31.45 ?  189  ARG C NH1 1 
ATOM   5765  N  NH2 . ARG C  1 165 ? 22.846  2.871   10.312  1.00 31.26 ?  189  ARG C NH2 1 
ATOM   5766  N  N   . MET C  1 166 ? 17.731  7.035   14.983  1.00 28.97 ?  190  MET C N   1 
ATOM   5767  C  CA  . MET C  1 166 ? 18.507  8.268   15.051  1.00 28.47 ?  190  MET C CA  1 
ATOM   5768  C  C   . MET C  1 166 ? 19.979  7.871   15.083  1.00 28.35 ?  190  MET C C   1 
ATOM   5769  O  O   . MET C  1 166 ? 20.376  7.052   15.920  1.00 28.23 ?  190  MET C O   1 
ATOM   5770  C  CB  . MET C  1 166 ? 18.148  9.085   16.296  1.00 28.46 ?  190  MET C CB  1 
ATOM   5771  C  CG  . MET C  1 166 ? 16.789  9.770   16.253  1.00 27.76 ?  190  MET C CG  1 
ATOM   5772  S  SD  . MET C  1 166 ? 16.617  10.911  14.872  1.00 27.22 ?  190  MET C SD  1 
ATOM   5773  C  CE  . MET C  1 166 ? 15.519  9.995   13.785  1.00 27.59 ?  190  MET C CE  1 
ATOM   5774  N  N   . PRO C  1 167 ? 20.792  8.436   14.166  1.00 28.16 ?  191  PRO C N   1 
ATOM   5775  C  CA  . PRO C  1 167 ? 22.193  8.046   14.049  1.00 28.13 ?  191  PRO C CA  1 
ATOM   5776  C  C   . PRO C  1 167 ? 23.031  8.526   15.228  1.00 28.00 ?  191  PRO C C   1 
ATOM   5777  O  O   . PRO C  1 167 ? 23.088  9.724   15.525  1.00 28.21 ?  191  PRO C O   1 
ATOM   5778  C  CB  . PRO C  1 167 ? 22.643  8.709   12.737  1.00 28.01 ?  191  PRO C CB  1 
ATOM   5779  C  CG  . PRO C  1 167 ? 21.368  9.034   12.018  1.00 28.51 ?  191  PRO C CG  1 
ATOM   5780  C  CD  . PRO C  1 167 ? 20.425  9.401   13.119  1.00 28.15 ?  191  PRO C CD  1 
ATOM   5781  N  N   . THR C  1 168 ? 23.665  7.568   15.889  1.00 27.75 ?  192  THR C N   1 
ATOM   5782  C  CA  . THR C  1 168 ? 24.458  7.815   17.081  1.00 27.44 ?  192  THR C CA  1 
ATOM   5783  C  C   . THR C  1 168 ? 25.949  7.791   16.733  1.00 27.28 ?  192  THR C C   1 
ATOM   5784  O  O   . THR C  1 168 ? 26.308  7.630   15.567  1.00 27.34 ?  192  THR C O   1 
ATOM   5785  C  CB  . THR C  1 168 ? 24.128  6.774   18.167  1.00 27.39 ?  192  THR C CB  1 
ATOM   5786  O  OG1 . THR C  1 168 ? 23.999  5.483   17.560  1.00 27.18 ?  192  THR C OG1 1 
ATOM   5787  C  CG2 . THR C  1 168 ? 22.820  7.122   18.857  1.00 27.52 ?  192  THR C CG2 1 
ATOM   5788  N  N   . ALA C  1 169 ? 26.812  7.965   17.733  1.00 27.12 ?  193  ALA C N   1 
ATOM   5789  C  CA  . ALA C  1 169 ? 28.261  8.011   17.501  1.00 27.15 ?  193  ALA C CA  1 
ATOM   5790  C  C   . ALA C  1 169 ? 28.789  6.751   16.807  1.00 27.07 ?  193  ALA C C   1 
ATOM   5791  O  O   . ALA C  1 169 ? 29.605  6.841   15.885  1.00 27.10 ?  193  ALA C O   1 
ATOM   5792  C  CB  . ALA C  1 169 ? 29.013  8.273   18.808  1.00 27.27 ?  193  ALA C CB  1 
ATOM   5793  N  N   . ASP C  1 170 ? 28.297  5.590   17.237  1.00 26.85 ?  194  ASP C N   1 
ATOM   5794  C  CA  . ASP C  1 170 ? 28.660  4.310   16.629  1.00 26.80 ?  194  ASP C CA  1 
ATOM   5795  C  C   . ASP C  1 170 ? 28.147  4.151   15.193  1.00 26.59 ?  194  ASP C C   1 
ATOM   5796  O  O   . ASP C  1 170 ? 28.727  3.397   14.409  1.00 26.56 ?  194  ASP C O   1 
ATOM   5797  C  CB  . ASP C  1 170 ? 28.180  3.141   17.495  1.00 26.97 ?  194  ASP C CB  1 
ATOM   5798  C  CG  . ASP C  1 170 ? 26.677  3.135   17.692  1.00 27.46 ?  194  ASP C CG  1 
ATOM   5799  O  OD1 . ASP C  1 170 ? 26.145  4.145   18.194  1.00 28.13 ?  194  ASP C OD1 1 
ATOM   5800  O  OD2 . ASP C  1 170 ? 26.030  2.119   17.355  1.00 28.20 -1 194  ASP C OD2 1 
ATOM   5801  N  N   . THR C  1 171 ? 27.061  4.850   14.859  1.00 26.26 ?  195  THR C N   1 
ATOM   5802  C  CA  . THR C  1 171 ? 26.523  4.838   13.498  1.00 25.85 ?  195  THR C CA  1 
ATOM   5803  C  C   . THR C  1 171 ? 27.503  5.534   12.552  1.00 25.53 ?  195  THR C C   1 
ATOM   5804  O  O   . THR C  1 171 ? 27.890  4.966   11.529  1.00 25.35 ?  195  THR C O   1 
ATOM   5805  C  CB  . THR C  1 171 ? 25.143  5.521   13.413  1.00 26.01 ?  195  THR C CB  1 
ATOM   5806  O  OG1 . THR C  1 171 ? 24.269  4.983   14.415  1.00 26.39 ?  195  THR C OG1 1 
ATOM   5807  C  CG2 . THR C  1 171 ? 24.526  5.320   12.036  1.00 25.73 ?  195  THR C CG2 1 
ATOM   5808  N  N   . CYS C  1 172 ? 27.896  6.758   12.907  1.00 25.14 ?  196  CYS C N   1 
ATOM   5809  C  CA  . CYS C  1 172 ? 28.930  7.502   12.180  1.00 24.72 ?  196  CYS C CA  1 
ATOM   5810  C  C   . CYS C  1 172 ? 30.250  6.727   12.159  1.00 24.69 ?  196  CYS C C   1 
ATOM   5811  O  O   . CYS C  1 172 ? 30.941  6.689   11.138  1.00 24.41 ?  196  CYS C O   1 
ATOM   5812  C  CB  . CYS C  1 172 ? 29.162  8.873   12.823  1.00 24.69 ?  196  CYS C CB  1 
ATOM   5813  S  SG  . CYS C  1 172 ? 27.689  9.887   13.095  1.00 23.83 ?  196  CYS C SG  1 
ATOM   5814  N  N   . GLY C  1 173 ? 30.576  6.111   13.296  1.00 24.72 ?  197  GLY C N   1 
ATOM   5815  C  CA  . GLY C  1 173 ? 31.819  5.363   13.484  1.00 25.09 ?  197  GLY C CA  1 
ATOM   5816  C  C   . GLY C  1 173 ? 32.002  4.153   12.585  1.00 25.33 ?  197  GLY C C   1 
ATOM   5817  O  O   . GLY C  1 173 ? 33.126  3.688   12.405  1.00 25.47 ?  197  GLY C O   1 
ATOM   5818  N  N   . THR C  1 174 ? 30.895  3.645   12.035  1.00 25.35 ?  198  THR C N   1 
ATOM   5819  C  CA  . THR C  1 174 ? 30.901  2.553   11.056  1.00 25.47 ?  198  THR C CA  1 
ATOM   5820  C  C   . THR C  1 174 ? 31.782  2.905   9.859   1.00 25.43 ?  198  THR C C   1 
ATOM   5821  O  O   . THR C  1 174 ? 32.547  2.071   9.368   1.00 25.27 ?  198  THR C O   1 
ATOM   5822  C  CB  . THR C  1 174 ? 29.461  2.224   10.569  1.00 25.34 ?  198  THR C CB  1 
ATOM   5823  O  OG1 . THR C  1 174 ? 28.626  1.939   11.697  1.00 25.91 ?  198  THR C OG1 1 
ATOM   5824  C  CG2 . THR C  1 174 ? 29.445  1.023   9.635   1.00 25.50 ?  198  THR C CG2 1 
ATOM   5825  N  N   . CYS C  1 175 ? 31.667  4.147   9.398   1.00 25.49 ?  199  CYS C N   1 
ATOM   5826  C  CA  . CYS C  1 175 ? 32.479  4.637   8.290   1.00 25.52 ?  199  CYS C CA  1 
ATOM   5827  C  C   . CYS C  1 175 ? 33.671  5.431   8.805   1.00 25.33 ?  199  CYS C C   1 
ATOM   5828  O  O   . CYS C  1 175 ? 34.812  5.174   8.425   1.00 25.48 ?  199  CYS C O   1 
ATOM   5829  C  CB  . CYS C  1 175 ? 31.639  5.507   7.361   1.00 25.56 ?  199  CYS C CB  1 
ATOM   5830  S  SG  . CYS C  1 175 ? 30.304  4.623   6.529   1.00 25.92 ?  199  CYS C SG  1 
ATOM   5831  N  N   . HIS C  1 176 ? 33.395  6.389   9.683   1.00 25.08 ?  200  HIS C N   1 
ATOM   5832  C  CA  . HIS C  1 176 ? 34.422  7.259   10.231  1.00 24.66 ?  200  HIS C CA  1 
ATOM   5833  C  C   . HIS C  1 176 ? 35.033  6.640   11.490  1.00 24.58 ?  200  HIS C C   1 
ATOM   5834  O  O   . HIS C  1 176 ? 34.888  7.171   12.598  1.00 24.53 ?  200  HIS C O   1 
ATOM   5835  C  CB  . HIS C  1 176 ? 33.837  8.651   10.501  1.00 24.59 ?  200  HIS C CB  1 
ATOM   5836  C  CG  . HIS C  1 176 ? 33.183  9.278   9.304   1.00 24.34 ?  200  HIS C CG  1 
ATOM   5837  N  ND1 . HIS C  1 176 ? 33.833  9.432   8.098   1.00 23.46 ?  200  HIS C ND1 1 
ATOM   5838  C  CD2 . HIS C  1 176 ? 31.950  9.816   9.138   1.00 24.00 ?  200  HIS C CD2 1 
ATOM   5839  C  CE1 . HIS C  1 176 ? 33.025  10.027  7.238   1.00 23.69 ?  200  HIS C CE1 1 
ATOM   5840  N  NE2 . HIS C  1 176 ? 31.875  10.272  7.842   1.00 24.30 ?  200  HIS C NE2 1 
ATOM   5841  N  N   . LEU C  1 177 ? 35.707  5.501   11.304  1.00 24.41 ?  201  LEU C N   1 
ATOM   5842  C  CA  . LEU C  1 177 ? 36.300  4.733   12.404  1.00 24.36 ?  201  LEU C CA  1 
ATOM   5843  C  C   . LEU C  1 177 ? 37.401  5.516   13.108  1.00 24.21 ?  201  LEU C C   1 
ATOM   5844  O  O   . LEU C  1 177 ? 37.507  5.472   14.334  1.00 24.22 ?  201  LEU C O   1 
ATOM   5845  C  CB  . LEU C  1 177 ? 36.882  3.402   11.895  1.00 24.23 ?  201  LEU C CB  1 
ATOM   5846  C  CG  . LEU C  1 177 ? 36.791  2.115   12.734  1.00 24.89 ?  201  LEU C CG  1 
ATOM   5847  C  CD1 . LEU C  1 177 ? 37.939  1.173   12.387  1.00 24.25 ?  201  LEU C CD1 1 
ATOM   5848  C  CD2 . LEU C  1 177 ? 36.734  2.323   14.253  1.00 23.95 ?  201  LEU C CD2 1 
ATOM   5849  N  N   . ARG C  1 178 ? 38.218  6.215   12.323  1.00 24.12 ?  202  ARG C N   1 
ATOM   5850  C  CA  . ARG C  1 178 ? 39.341  6.979   12.849  1.00 24.35 ?  202  ARG C CA  1 
ATOM   5851  C  C   . ARG C  1 178 ? 38.876  7.996   13.885  1.00 24.29 ?  202  ARG C C   1 
ATOM   5852  O  O   . ARG C  1 178 ? 39.343  7.986   15.028  1.00 23.99 ?  202  ARG C O   1 
ATOM   5853  C  CB  . ARG C  1 178 ? 40.095  7.686   11.719  1.00 24.37 ?  202  ARG C CB  1 
ATOM   5854  C  CG  . ARG C  1 178 ? 41.313  8.461   12.194  1.00 25.52 ?  202  ARG C CG  1 
ATOM   5855  C  CD  . ARG C  1 178 ? 42.033  9.170   11.063  1.00 26.37 ?  202  ARG C CD  1 
ATOM   5856  N  NE  . ARG C  1 178 ? 42.670  8.250   10.122  1.00 27.66 ?  202  ARG C NE  1 
ATOM   5857  C  CZ  . ARG C  1 178 ? 43.865  7.684   10.293  1.00 28.50 ?  202  ARG C CZ  1 
ATOM   5858  N  NH1 . ARG C  1 178 ? 44.581  7.912   11.390  1.00 28.20 ?  202  ARG C NH1 1 
ATOM   5859  N  NH2 . ARG C  1 178 ? 44.343  6.875   9.361   1.00 28.79 ?  202  ARG C NH2 1 
ATOM   5860  N  N   . GLU C  1 179 ? 37.940  8.849   13.470  1.00 24.24 ?  203  GLU C N   1 
ATOM   5861  C  CA  . GLU C  1 179 ? 37.441  9.952   14.294  1.00 24.29 ?  203  GLU C CA  1 
ATOM   5862  C  C   . GLU C  1 179 ? 36.687  9.457   15.524  1.00 24.15 ?  203  GLU C C   1 
ATOM   5863  O  O   . GLU C  1 179 ? 36.817  10.027  16.606  1.00 24.17 ?  203  GLU C O   1 
ATOM   5864  C  CB  . GLU C  1 179 ? 36.553  10.888  13.458  1.00 24.24 ?  203  GLU C CB  1 
ATOM   5865  C  CG  . GLU C  1 179 ? 37.308  11.725  12.423  1.00 24.33 ?  203  GLU C CG  1 
ATOM   5866  C  CD  . GLU C  1 179 ? 37.564  10.998  11.106  1.00 25.09 ?  203  GLU C CD  1 
ATOM   5867  O  OE1 . GLU C  1 179 ? 37.167  9.819   10.965  1.00 24.13 ?  203  GLU C OE1 1 
ATOM   5868  O  OE2 . GLU C  1 179 ? 38.161  11.621  10.198  1.00 25.16 -1 203  GLU C OE2 1 
ATOM   5869  N  N   . PHE C  1 180 ? 35.903  8.397   15.346  1.00 24.19 ?  204  PHE C N   1 
ATOM   5870  C  CA  . PHE C  1 180 ? 35.152  7.779   16.443  1.00 24.08 ?  204  PHE C CA  1 
ATOM   5871  C  C   . PHE C  1 180 ? 36.098  7.141   17.461  1.00 24.00 ?  204  PHE C C   1 
ATOM   5872  O  O   . PHE C  1 180 ? 35.887  7.265   18.666  1.00 24.05 ?  204  PHE C O   1 
ATOM   5873  C  CB  . PHE C  1 180 ? 34.150  6.750   15.892  1.00 24.02 ?  204  PHE C CB  1 
ATOM   5874  C  CG  . PHE C  1 180 ? 33.390  5.992   16.957  1.00 24.44 ?  204  PHE C CG  1 
ATOM   5875  C  CD1 . PHE C  1 180 ? 32.644  6.667   17.925  1.00 23.75 ?  204  PHE C CD1 1 
ATOM   5876  C  CD2 . PHE C  1 180 ? 33.399  4.600   16.971  1.00 24.23 ?  204  PHE C CD2 1 
ATOM   5877  C  CE1 . PHE C  1 180 ? 31.940  5.968   18.904  1.00 23.88 ?  204  PHE C CE1 1 
ATOM   5878  C  CE2 . PHE C  1 180 ? 32.692  3.888   17.946  1.00 24.59 ?  204  PHE C CE2 1 
ATOM   5879  C  CZ  . PHE C  1 180 ? 31.963  4.575   18.915  1.00 24.48 ?  204  PHE C CZ  1 
ATOM   5880  N  N   . ALA C  1 181 ? 37.143  6.476   16.966  1.00 23.94 ?  205  ALA C N   1 
ATOM   5881  C  CA  . ALA C  1 181 ? 38.176  5.890   17.824  1.00 23.95 ?  205  ALA C CA  1 
ATOM   5882  C  C   . ALA C  1 181 ? 38.977  6.975   18.548  1.00 23.86 ?  205  ALA C C   1 
ATOM   5883  O  O   . ALA C  1 181 ? 39.198  6.884   19.756  1.00 23.54 ?  205  ALA C O   1 
ATOM   5884  C  CB  . ALA C  1 181 ? 39.100  4.985   17.016  1.00 23.79 ?  205  ALA C CB  1 
ATOM   5885  N  N   . GLU C  1 182 ? 39.395  7.999   17.803  1.00 24.10 ?  206  GLU C N   1 
ATOM   5886  C  CA  . GLU C  1 182 ? 40.060  9.174   18.382  1.00 24.54 ?  206  GLU C CA  1 
ATOM   5887  C  C   . GLU C  1 182 ? 39.234  9.753   19.528  1.00 24.66 ?  206  GLU C C   1 
ATOM   5888  O  O   . GLU C  1 182 ? 39.753  9.997   20.616  1.00 24.58 ?  206  GLU C O   1 
ATOM   5889  C  CB  . GLU C  1 182 ? 40.274  10.254  17.324  1.00 24.40 ?  206  GLU C CB  1 
ATOM   5890  C  CG  . GLU C  1 182 ? 41.380  9.966   16.328  1.00 24.77 ?  206  GLU C CG  1 
ATOM   5891  C  CD  . GLU C  1 182 ? 41.449  11.006  15.225  1.00 25.51 ?  206  GLU C CD  1 
ATOM   5892  O  OE1 . GLU C  1 182 ? 40.651  11.969  15.245  1.00 26.12 ?  206  GLU C OE1 1 
ATOM   5893  O  OE2 . GLU C  1 182 ? 42.309  10.867  14.333  1.00 26.23 -1 206  GLU C OE2 1 
ATOM   5894  N  N   . ARG C  1 183 ? 37.945  9.951   19.267  1.00 24.91 ?  207  ARG C N   1 
ATOM   5895  C  CA  . ARG C  1 183 ? 37.000  10.460  20.256  1.00 25.29 ?  207  ARG C CA  1 
ATOM   5896  C  C   . ARG C  1 183 ? 36.909  9.527   21.464  1.00 25.51 ?  207  ARG C C   1 
ATOM   5897  O  O   . ARG C  1 183 ? 37.003  9.977   22.604  1.00 25.71 ?  207  ARG C O   1 
ATOM   5898  C  CB  . ARG C  1 183 ? 35.614  10.639  19.616  1.00 25.16 ?  207  ARG C CB  1 
ATOM   5899  C  CG  . ARG C  1 183 ? 34.736  11.717  20.249  1.00 24.78 ?  207  ARG C CG  1 
ATOM   5900  C  CD  . ARG C  1 183 ? 34.178  11.318  21.617  1.00 24.93 ?  207  ARG C CD  1 
ATOM   5901  N  NE  . ARG C  1 183 ? 33.323  10.129  21.583  1.00 24.80 ?  207  ARG C NE  1 
ATOM   5902  C  CZ  . ARG C  1 183 ? 32.028  10.134  21.266  1.00 25.13 ?  207  ARG C CZ  1 
ATOM   5903  N  NH1 . ARG C  1 183 ? 31.419  11.267  20.939  1.00 24.21 ?  207  ARG C NH1 1 
ATOM   5904  N  NH2 . ARG C  1 183 ? 31.338  8.997   21.271  1.00 25.21 ?  207  ARG C NH2 1 
ATOM   5905  N  N   . GLU C  1 184 ? 36.725  8.234   21.209  1.00 25.86 ?  208  GLU C N   1 
ATOM   5906  C  CA  . GLU C  1 184 ? 36.621  7.242   22.286  1.00 26.35 ?  208  GLU C CA  1 
ATOM   5907  C  C   . GLU C  1 184 ? 37.901  7.078   23.110  1.00 26.52 ?  208  GLU C C   1 
ATOM   5908  O  O   . GLU C  1 184 ? 37.837  6.694   24.281  1.00 26.48 ?  208  GLU C O   1 
ATOM   5909  C  CB  . GLU C  1 184 ? 36.153  5.890   21.742  1.00 26.33 ?  208  GLU C CB  1 
ATOM   5910  C  CG  . GLU C  1 184 ? 34.662  5.846   21.416  1.00 26.70 ?  208  GLU C CG  1 
ATOM   5911  C  CD  . GLU C  1 184 ? 33.793  6.049   22.646  1.00 27.25 ?  208  GLU C CD  1 
ATOM   5912  O  OE1 . GLU C  1 184 ? 33.715  5.123   23.481  1.00 27.10 ?  208  GLU C OE1 1 
ATOM   5913  O  OE2 . GLU C  1 184 ? 33.191  7.137   22.777  1.00 27.69 -1 208  GLU C OE2 1 
ATOM   5914  N  N   . SER C  1 185 ? 39.047  7.392   22.503  1.00 26.77 ?  209  SER C N   1 
ATOM   5915  C  CA  . SER C  1 185 ? 40.353  7.329   23.177  1.00 27.06 ?  209  SER C CA  1 
ATOM   5916  C  C   . SER C  1 185 ? 40.494  8.319   24.339  1.00 27.35 ?  209  SER C C   1 
ATOM   5917  O  O   . SER C  1 185 ? 41.438  8.218   25.137  1.00 27.45 ?  209  SER C O   1 
ATOM   5918  C  CB  . SER C  1 185 ? 41.494  7.529   22.172  1.00 27.09 ?  209  SER C CB  1 
ATOM   5919  O  OG  . SER C  1 185 ? 41.645  8.887   21.806  1.00 26.96 ?  209  SER C OG  1 
ATOM   5920  N  N   . GLU C  1 186 ? 39.558  9.267   24.429  1.00 27.43 ?  210  GLU C N   1 
ATOM   5921  C  CA  . GLU C  1 186 ? 39.497  10.205  25.555  1.00 27.34 ?  210  GLU C CA  1 
ATOM   5922  C  C   . GLU C  1 186 ? 39.244  9.466   26.870  1.00 27.37 ?  210  GLU C C   1 
ATOM   5923  O  O   . GLU C  1 186 ? 39.683  9.910   27.936  1.00 27.13 ?  210  GLU C O   1 
ATOM   5924  C  CB  . GLU C  1 186 ? 38.422  11.274  25.323  1.00 27.35 ?  210  GLU C CB  1 
ATOM   5925  C  CG  . GLU C  1 186 ? 38.711  12.201  24.142  1.00 27.46 ?  210  GLU C CG  1 
ATOM   5926  C  CD  . GLU C  1 186 ? 37.614  13.227  23.882  1.00 27.74 ?  210  GLU C CD  1 
ATOM   5927  O  OE1 . GLU C  1 186 ? 36.502  13.103  24.438  1.00 27.80 ?  210  GLU C OE1 1 
ATOM   5928  O  OE2 . GLU C  1 186 ? 37.868  14.164  23.101  1.00 28.02 -1 210  GLU C OE2 1 
ATOM   5929  N  N   . ARG C  1 187 ? 38.540  8.337   26.778  1.00 27.55 ?  211  ARG C N   1 
ATOM   5930  C  CA  . ARG C  1 187 ? 38.317  7.438   27.916  1.00 27.77 ?  211  ARG C CA  1 
ATOM   5931  C  C   . ARG C  1 187 ? 39.630  6.931   28.509  1.00 28.07 ?  211  ARG C C   1 
ATOM   5932  O  O   . ARG C  1 187 ? 39.737  6.726   29.722  1.00 28.10 ?  211  ARG C O   1 
ATOM   5933  C  CB  . ARG C  1 187 ? 37.489  6.226   27.489  1.00 27.63 ?  211  ARG C CB  1 
ATOM   5934  C  CG  . ARG C  1 187 ? 36.058  6.521   27.079  1.00 27.51 ?  211  ARG C CG  1 
ATOM   5935  C  CD  . ARG C  1 187 ? 35.453  5.288   26.427  1.00 27.44 ?  211  ARG C CD  1 
ATOM   5936  N  NE  . ARG C  1 187 ? 34.024  5.428   26.172  1.00 27.48 ?  211  ARG C NE  1 
ATOM   5937  C  CZ  . ARG C  1 187 ? 33.072  5.166   27.063  1.00 27.47 ?  211  ARG C CZ  1 
ATOM   5938  N  NH1 . ARG C  1 187 ? 33.385  4.749   28.282  1.00 27.32 ?  211  ARG C NH1 1 
ATOM   5939  N  NH2 . ARG C  1 187 ? 31.799  5.319   26.730  1.00 28.07 ?  211  ARG C NH2 1 
ATOM   5940  N  N   . ASP C  1 188 ? 40.621  6.739   27.639  1.00 28.34 ?  212  ASP C N   1 
ATOM   5941  C  CA  . ASP C  1 188 ? 41.889  6.114   28.009  1.00 28.59 ?  212  ASP C CA  1 
ATOM   5942  C  C   . ASP C  1 188 ? 43.032  7.105   28.258  1.00 28.83 ?  212  ASP C C   1 
ATOM   5943  O  O   . ASP C  1 188 ? 43.987  6.783   28.974  1.00 29.09 ?  212  ASP C O   1 
ATOM   5944  C  CB  . ASP C  1 188 ? 42.286  5.101   26.931  1.00 28.65 ?  212  ASP C CB  1 
ATOM   5945  C  CG  . ASP C  1 188 ? 41.129  4.201   26.526  1.00 28.69 ?  212  ASP C CG  1 
ATOM   5946  O  OD1 . ASP C  1 188 ? 40.572  3.507   27.405  1.00 28.62 ?  212  ASP C OD1 1 
ATOM   5947  O  OD2 . ASP C  1 188 ? 40.768  4.196   25.330  1.00 29.13 -1 212  ASP C OD2 1 
ATOM   5948  N  N   . THR C  1 189 ? 42.938  8.301   27.675  1.00 28.91 ?  213  THR C N   1 
ATOM   5949  C  CA  . THR C  1 189 ? 43.986  9.320   27.834  1.00 28.99 ?  213  THR C CA  1 
ATOM   5950  C  C   . THR C  1 189 ? 43.730  10.304  28.976  1.00 29.37 ?  213  THR C C   1 
ATOM   5951  O  O   . THR C  1 189 ? 44.681  10.814  29.570  1.00 29.55 ?  213  THR C O   1 
ATOM   5952  C  CB  . THR C  1 189 ? 44.234  10.130  26.539  1.00 28.86 ?  213  THR C CB  1 
ATOM   5953  O  OG1 . THR C  1 189 ? 43.026  10.784  26.138  1.00 28.48 ?  213  THR C OG1 1 
ATOM   5954  C  CG2 . THR C  1 189 ? 44.731  9.231   25.415  1.00 28.84 ?  213  THR C CG2 1 
ATOM   5955  N  N   . MET C  1 190 ? 42.463  10.582  29.282  1.00 29.59 ?  214  MET C N   1 
ATOM   5956  C  CA  . MET C  1 190 ? 42.153  11.558  30.328  1.00 29.67 ?  214  MET C CA  1 
ATOM   5957  C  C   . MET C  1 190 ? 42.067  10.921  31.714  1.00 29.87 ?  214  MET C C   1 
ATOM   5958  O  O   . MET C  1 190 ? 41.000  10.868  32.339  1.00 30.02 ?  214  MET C O   1 
ATOM   5959  C  CB  . MET C  1 190 ? 40.904  12.389  29.999  1.00 29.58 ?  214  MET C CB  1 
ATOM   5960  C  CG  . MET C  1 190 ? 40.655  13.591  30.941  1.00 29.63 ?  214  MET C CG  1 
ATOM   5961  S  SD  . MET C  1 190 ? 41.976  14.836  31.041  1.00 29.18 ?  214  MET C SD  1 
ATOM   5962  C  CE  . MET C  1 190 ? 43.127  14.108  32.210  1.00 29.07 ?  214  MET C CE  1 
ATOM   5963  N  N   . VAL C  1 191 ? 43.213  10.433  32.177  1.00 29.90 ?  215  VAL C N   1 
ATOM   5964  C  CA  . VAL C  1 191 ? 43.325  9.826   33.495  1.00 29.93 ?  215  VAL C CA  1 
ATOM   5965  C  C   . VAL C  1 191 ? 44.191  10.729  34.369  1.00 29.97 ?  215  VAL C C   1 
ATOM   5966  O  O   . VAL C  1 191 ? 45.353  11.000  34.050  1.00 29.93 ?  215  VAL C O   1 
ATOM   5967  C  CB  . VAL C  1 191 ? 43.900  8.385   33.425  1.00 30.08 ?  215  VAL C CB  1 
ATOM   5968  C  CG1 . VAL C  1 191 ? 43.872  7.722   34.804  1.00 29.88 ?  215  VAL C CG1 1 
ATOM   5969  C  CG2 . VAL C  1 191 ? 43.110  7.543   32.428  1.00 29.85 ?  215  VAL C CG2 1 
ATOM   5970  N  N   . TRP C  1 192 ? 43.599  11.212  35.456  1.00 29.98 ?  216  TRP C N   1 
ATOM   5971  C  CA  . TRP C  1 192 ? 44.279  12.107  36.382  1.00 30.10 ?  216  TRP C CA  1 
ATOM   5972  C  C   . TRP C  1 192 ? 45.211  11.321  37.301  1.00 30.33 ?  216  TRP C C   1 
ATOM   5973  O  O   . TRP C  1 192 ? 44.892  10.192  37.685  1.00 30.45 ?  216  TRP C O   1 
ATOM   5974  C  CB  . TRP C  1 192 ? 43.256  12.925  37.178  1.00 29.97 ?  216  TRP C CB  1 
ATOM   5975  C  CG  . TRP C  1 192 ? 42.492  13.854  36.291  1.00 29.60 ?  216  TRP C CG  1 
ATOM   5976  C  CD1 . TRP C  1 192 ? 41.346  13.572  35.604  1.00 29.33 ?  216  TRP C CD1 1 
ATOM   5977  C  CD2 . TRP C  1 192 ? 42.843  15.200  35.952  1.00 29.23 ?  216  TRP C CD2 1 
ATOM   5978  N  NE1 . TRP C  1 192 ? 40.952  14.664  34.870  1.00 28.82 ?  216  TRP C NE1 1 
ATOM   5979  C  CE2 . TRP C  1 192 ? 41.850  15.679  35.067  1.00 28.96 ?  216  TRP C CE2 1 
ATOM   5980  C  CE3 . TRP C  1 192 ? 43.893  16.053  36.316  1.00 28.77 ?  216  TRP C CE3 1 
ATOM   5981  C  CZ2 . TRP C  1 192 ? 41.877  16.975  34.538  1.00 28.60 ?  216  TRP C CZ2 1 
ATOM   5982  C  CZ3 . TRP C  1 192 ? 43.919  17.343  35.788  1.00 28.53 ?  216  TRP C CZ3 1 
ATOM   5983  C  CH2 . TRP C  1 192 ? 42.916  17.788  34.909  1.00 28.48 ?  216  TRP C CH2 1 
ATOM   5984  N  N   . PRO C  1 193 ? 46.378  11.904  37.637  1.00 30.46 ?  217  PRO C N   1 
ATOM   5985  C  CA  . PRO C  1 193 ? 47.359  11.182  38.455  1.00 30.52 ?  217  PRO C CA  1 
ATOM   5986  C  C   . PRO C  1 193 ? 46.860  10.857  39.867  1.00 30.63 ?  217  PRO C C   1 
ATOM   5987  O  O   . PRO C  1 193 ? 47.274  9.848   40.441  1.00 30.85 ?  217  PRO C O   1 
ATOM   5988  C  CB  . PRO C  1 193 ? 48.559  12.138  38.503  1.00 30.44 ?  217  PRO C CB  1 
ATOM   5989  C  CG  . PRO C  1 193 ? 48.006  13.482  38.173  1.00 30.60 ?  217  PRO C CG  1 
ATOM   5990  C  CD  . PRO C  1 193 ? 46.870  13.235  37.229  1.00 30.44 ?  217  PRO C CD  1 
ATOM   5991  N  N   . ASN C  1 194 ? 45.976  11.694  40.408  1.00 30.51 ?  218  ASN C N   1 
ATOM   5992  C  CA  . ASN C  1 194 ? 45.430  11.498  41.753  1.00 30.46 ?  218  ASN C CA  1 
ATOM   5993  C  C   . ASN C  1 194 ? 43.902  11.405  41.788  1.00 30.31 ?  218  ASN C C   1 
ATOM   5994  O  O   . ASN C  1 194 ? 43.280  11.682  42.817  1.00 30.37 ?  218  ASN C O   1 
ATOM   5995  C  CB  . ASN C  1 194 ? 45.912  12.618  42.684  1.00 30.51 ?  218  ASN C CB  1 
ATOM   5996  C  CG  . ASN C  1 194 ? 47.390  12.904  42.529  1.00 31.14 ?  218  ASN C CG  1 
ATOM   5997  O  OD1 . ASN C  1 194 ? 47.776  13.936  41.975  1.00 31.17 ?  218  ASN C OD1 1 
ATOM   5998  N  ND2 . ASN C  1 194 ? 48.229  11.975  42.989  1.00 31.47 ?  218  ASN C ND2 1 
ATOM   5999  N  N   . GLY C  1 195 ? 43.305  11.007  40.666  1.00 30.18 ?  219  GLY C N   1 
ATOM   6000  C  CA  . GLY C  1 195 ? 41.847  10.924  40.540  1.00 29.75 ?  219  GLY C CA  1 
ATOM   6001  C  C   . GLY C  1 195 ? 41.120  12.240  40.782  1.00 29.43 ?  219  GLY C C   1 
ATOM   6002  O  O   . GLY C  1 195 ? 40.022  12.250  41.343  1.00 29.37 ?  219  GLY C O   1 
ATOM   6003  N  N   . GLN C  1 196 ? 41.732  13.347  40.355  1.00 28.99 ?  220  GLN C N   1 
ATOM   6004  C  CA  . GLN C  1 196 ? 41.149  14.688  40.496  1.00 28.70 ?  220  GLN C CA  1 
ATOM   6005  C  C   . GLN C  1 196 ? 39.735  14.749  39.915  1.00 28.61 ?  220  GLN C C   1 
ATOM   6006  O  O   . GLN C  1 196 ? 38.819  15.302  40.528  1.00 28.38 ?  220  GLN C O   1 
ATOM   6007  C  CB  . GLN C  1 196 ? 42.042  15.733  39.821  1.00 28.55 ?  220  GLN C CB  1 
ATOM   6008  C  CG  . GLN C  1 196 ? 43.222  16.213  40.670  1.00 28.49 ?  220  GLN C CG  1 
ATOM   6009  C  CD  . GLN C  1 196 ? 44.456  15.315  40.607  1.00 28.65 ?  220  GLN C CD  1 
ATOM   6010  O  OE1 . GLN C  1 196 ? 44.441  14.231  40.018  1.00 28.59 ?  220  GLN C OE1 1 
ATOM   6011  N  NE2 . GLN C  1 196 ? 45.537  15.773  41.230  1.00 28.81 ?  220  GLN C NE2 1 
ATOM   6012  N  N   . TRP C  1 197 ? 39.587  14.181  38.722  1.00 28.49 ?  221  TRP C N   1 
ATOM   6013  C  CA  . TRP C  1 197 ? 38.298  13.939  38.103  1.00 28.55 ?  221  TRP C CA  1 
ATOM   6014  C  C   . TRP C  1 197 ? 38.180  12.429  37.877  1.00 28.47 ?  221  TRP C C   1 
ATOM   6015  O  O   . TRP C  1 197 ? 39.196  11.729  37.888  1.00 28.57 ?  221  TRP C O   1 
ATOM   6016  C  CB  . TRP C  1 197 ? 38.213  14.673  36.764  1.00 28.55 ?  221  TRP C CB  1 
ATOM   6017  C  CG  . TRP C  1 197 ? 38.200  16.162  36.880  1.00 28.69 ?  221  TRP C CG  1 
ATOM   6018  C  CD1 . TRP C  1 197 ? 39.283  16.986  36.997  1.00 28.47 ?  221  TRP C CD1 1 
ATOM   6019  C  CD2 . TRP C  1 197 ? 37.046  17.012  36.881  1.00 28.46 ?  221  TRP C CD2 1 
ATOM   6020  N  NE1 . TRP C  1 197 ? 38.876  18.294  37.076  1.00 29.12 ?  221  TRP C NE1 1 
ATOM   6021  C  CE2 . TRP C  1 197 ? 37.507  18.340  37.007  1.00 28.67 ?  221  TRP C CE2 1 
ATOM   6022  C  CE3 . TRP C  1 197 ? 35.667  16.779  36.793  1.00 28.19 ?  221  TRP C CE3 1 
ATOM   6023  C  CZ2 . TRP C  1 197 ? 36.638  19.436  37.041  1.00 28.73 ?  221  TRP C CZ2 1 
ATOM   6024  C  CZ3 . TRP C  1 197 ? 34.802  17.868  36.833  1.00 28.23 ?  221  TRP C CZ3 1 
ATOM   6025  C  CH2 . TRP C  1 197 ? 35.292  19.180  36.953  1.00 28.54 ?  221  TRP C CH2 1 
ATOM   6026  N  N   . PRO C  1 198 ? 36.947  11.915  37.674  1.00 28.38 ?  222  PRO C N   1 
ATOM   6027  C  CA  . PRO C  1 198 ? 36.799  10.497  37.317  1.00 28.17 ?  222  PRO C CA  1 
ATOM   6028  C  C   . PRO C  1 198 ? 37.526  10.179  36.013  1.00 28.03 ?  222  PRO C C   1 
ATOM   6029  O  O   . PRO C  1 198 ? 37.607  11.038  35.125  1.00 27.87 ?  222  PRO C O   1 
ATOM   6030  C  CB  . PRO C  1 198 ? 35.286  10.340  37.129  1.00 28.25 ?  222  PRO C CB  1 
ATOM   6031  C  CG  . PRO C  1 198 ? 34.687  11.433  37.949  1.00 28.15 ?  222  PRO C CG  1 
ATOM   6032  C  CD  . PRO C  1 198 ? 35.639  12.581  37.820  1.00 28.29 ?  222  PRO C CD  1 
ATOM   6033  N  N   . ALA C  1 199 ? 38.052  8.958   35.906  1.00 27.75 ?  223  ALA C N   1 
ATOM   6034  C  CA  . ALA C  1 199 ? 38.830  8.545   34.739  1.00 27.49 ?  223  ALA C CA  1 
ATOM   6035  C  C   . ALA C  1 199 ? 38.032  8.714   33.451  1.00 27.28 ?  223  ALA C C   1 
ATOM   6036  O  O   . ALA C  1 199 ? 36.866  8.327   33.379  1.00 27.34 ?  223  ALA C O   1 
ATOM   6037  C  CB  . ALA C  1 199 ? 39.316  7.103   34.893  1.00 27.73 ?  223  ALA C CB  1 
ATOM   6038  N  N   . GLY C  1 200 ? 38.670  9.311   32.446  1.00 26.96 ?  224  GLY C N   1 
ATOM   6039  C  CA  . GLY C  1 200 ? 38.024  9.609   31.171  1.00 26.40 ?  224  GLY C CA  1 
ATOM   6040  C  C   . GLY C  1 200 ? 37.326  10.961  31.128  1.00 25.98 ?  224  GLY C C   1 
ATOM   6041  O  O   . GLY C  1 200 ? 36.688  11.299  30.132  1.00 25.85 ?  224  GLY C O   1 
ATOM   6042  N  N   . ARG C  1 201 ? 37.461  11.741  32.199  1.00 25.51 ?  225  ARG C N   1 
ATOM   6043  C  CA  . ARG C  1 201 ? 36.736  13.005  32.339  1.00 25.10 ?  225  ARG C CA  1 
ATOM   6044  C  C   . ARG C  1 201 ? 37.624  14.153  32.835  1.00 24.75 ?  225  ARG C C   1 
ATOM   6045  O  O   . ARG C  1 201 ? 38.581  13.917  33.575  1.00 24.64 ?  225  ARG C O   1 
ATOM   6046  C  CB  . ARG C  1 201 ? 35.523  12.821  33.260  1.00 25.15 ?  225  ARG C CB  1 
ATOM   6047  C  CG  . ARG C  1 201 ? 34.287  12.282  32.551  1.00 25.65 ?  225  ARG C CG  1 
ATOM   6048  C  CD  . ARG C  1 201 ? 33.279  11.669  33.524  1.00 26.42 ?  225  ARG C CD  1 
ATOM   6049  N  NE  . ARG C  1 201 ? 32.734  12.650  34.465  1.00 26.91 ?  225  ARG C NE  1 
ATOM   6050  C  CZ  . ARG C  1 201 ? 31.908  12.358  35.467  1.00 27.84 ?  225  ARG C CZ  1 
ATOM   6051  N  NH1 . ARG C  1 201 ? 31.512  11.104  35.674  1.00 28.13 ?  225  ARG C NH1 1 
ATOM   6052  N  NH2 . ARG C  1 201 ? 31.473  13.323  36.269  1.00 28.02 ?  225  ARG C NH2 1 
ATOM   6053  N  N   . PRO C  1 202 ? 37.319  15.401  32.417  1.00 24.50 ?  226  PRO C N   1 
ATOM   6054  C  CA  . PRO C  1 202 ? 36.238  15.781  31.496  1.00 24.23 ?  226  PRO C CA  1 
ATOM   6055  C  C   . PRO C  1 202 ? 36.572  15.452  30.045  1.00 23.94 ?  226  PRO C C   1 
ATOM   6056  O  O   . PRO C  1 202 ? 37.745  15.423  29.671  1.00 23.86 ?  226  PRO C O   1 
ATOM   6057  C  CB  . PRO C  1 202 ? 36.129  17.306  31.683  1.00 24.13 ?  226  PRO C CB  1 
ATOM   6058  C  CG  . PRO C  1 202 ? 36.925  17.615  32.926  1.00 24.45 ?  226  PRO C CG  1 
ATOM   6059  C  CD  . PRO C  1 202 ? 38.017  16.592  32.927  1.00 24.43 ?  226  PRO C CD  1 
ATOM   6060  N  N   . SER C  1 203 ? 35.541  15.203  29.242  1.00 23.85 ?  227  SER C N   1 
ATOM   6061  C  CA  . SER C  1 203 ? 35.717  14.818  27.841  1.00 23.62 ?  227  SER C CA  1 
ATOM   6062  C  C   . SER C  1 203 ? 34.398  14.847  27.081  1.00 23.40 ?  227  SER C C   1 
ATOM   6063  O  O   . SER C  1 203 ? 33.323  14.865  27.683  1.00 23.45 ?  227  SER C O   1 
ATOM   6064  C  CB  . SER C  1 203 ? 36.293  13.406  27.760  1.00 23.62 ?  227  SER C CB  1 
ATOM   6065  O  OG  . SER C  1 203 ? 35.360  12.469  28.271  1.00 23.65 ?  227  SER C OG  1 
ATOM   6066  N  N   . HIS C  1 204 ? 34.487  14.833  25.755  1.00 23.11 ?  228  HIS C N   1 
ATOM   6067  C  CA  . HIS C  1 204 ? 33.306  14.710  24.911  1.00 22.94 ?  228  HIS C CA  1 
ATOM   6068  C  C   . HIS C  1 204 ? 32.808  13.262  24.889  1.00 22.97 ?  228  HIS C C   1 
ATOM   6069  O  O   . HIS C  1 204 ? 31.620  13.007  24.672  1.00 22.93 ?  228  HIS C O   1 
ATOM   6070  C  CB  . HIS C  1 204 ? 33.589  15.223  23.491  1.00 22.55 ?  228  HIS C CB  1 
ATOM   6071  C  CG  . HIS C  1 204 ? 33.771  16.710  23.407  1.00 22.43 ?  228  HIS C CG  1 
ATOM   6072  N  ND1 . HIS C  1 204 ? 34.636  17.304  22.513  1.00 21.94 ?  228  HIS C ND1 1 
ATOM   6073  C  CD2 . HIS C  1 204 ? 33.208  17.722  24.111  1.00 21.89 ?  228  HIS C CD2 1 
ATOM   6074  C  CE1 . HIS C  1 204 ? 34.592  18.617  22.663  1.00 21.59 ?  228  HIS C CE1 1 
ATOM   6075  N  NE2 . HIS C  1 204 ? 33.733  18.899  23.628  1.00 21.80 ?  228  HIS C NE2 1 
ATOM   6076  N  N   . ALA C  1 205 ? 33.723  12.322  25.131  1.00 22.93 ?  229  ALA C N   1 
ATOM   6077  C  CA  . ALA C  1 205 ? 33.403  10.894  25.131  1.00 22.85 ?  229  ALA C CA  1 
ATOM   6078  C  C   . ALA C  1 205 ? 32.447  10.516  26.252  1.00 22.77 ?  229  ALA C C   1 
ATOM   6079  O  O   . ALA C  1 205 ? 31.616  9.631   26.077  1.00 22.83 ?  229  ALA C O   1 
ATOM   6080  C  CB  . ALA C  1 205 ? 34.680  10.047  25.206  1.00 22.80 ?  229  ALA C CB  1 
ATOM   6081  N  N   . LEU C  1 206 ? 32.568  11.190  27.394  1.00 22.71 ?  230  LEU C N   1 
ATOM   6082  C  CA  . LEU C  1 206 ? 31.725  10.910  28.552  1.00 22.77 ?  230  LEU C CA  1 
ATOM   6083  C  C   . LEU C  1 206 ? 30.896  12.115  29.014  1.00 22.78 ?  230  LEU C C   1 
ATOM   6084  O  O   . LEU C  1 206 ? 30.545  12.211  30.196  1.00 22.54 ?  230  LEU C O   1 
ATOM   6085  C  CB  . LEU C  1 206 ? 32.573  10.368  29.718  1.00 22.79 ?  230  LEU C CB  1 
ATOM   6086  C  CG  . LEU C  1 206 ? 33.279  9.018   29.525  1.00 23.28 ?  230  LEU C CG  1 
ATOM   6087  C  CD1 . LEU C  1 206 ? 34.238  8.731   30.679  1.00 23.07 ?  230  LEU C CD1 1 
ATOM   6088  C  CD2 . LEU C  1 206 ? 32.270  7.880   29.362  1.00 23.14 ?  230  LEU C CD2 1 
ATOM   6089  N  N   . ASP C  1 207 ? 30.567  13.019  28.088  1.00 22.88 ?  231  ASP C N   1 
ATOM   6090  C  CA  . ASP C  1 207 ? 29.794  14.217  28.446  1.00 23.06 ?  231  ASP C CA  1 
ATOM   6091  C  C   . ASP C  1 207 ? 28.360  13.921  28.883  1.00 23.14 ?  231  ASP C C   1 
ATOM   6092  O  O   . ASP C  1 207 ? 27.860  14.538  29.827  1.00 23.27 ?  231  ASP C O   1 
ATOM   6093  C  CB  . ASP C  1 207 ? 29.870  15.321  27.368  1.00 23.06 ?  231  ASP C CB  1 
ATOM   6094  C  CG  . ASP C  1 207 ? 29.112  14.989  26.083  1.00 23.33 ?  231  ASP C CG  1 
ATOM   6095  O  OD1 . ASP C  1 207 ? 28.781  13.812  25.823  1.00 23.84 ?  231  ASP C OD1 1 
ATOM   6096  O  OD2 . ASP C  1 207 ? 28.852  15.944  25.313  1.00 23.51 -1 231  ASP C OD2 1 
ATOM   6097  N  N   . TYR C  1 208 ? 27.719  12.963  28.218  1.00 23.34 ?  232  TYR C N   1 
ATOM   6098  C  CA  . TYR C  1 208 ? 26.367  12.549  28.588  1.00 23.73 ?  232  TYR C CA  1 
ATOM   6099  C  C   . TYR C  1 208 ? 26.328  11.779  29.907  1.00 23.75 ?  232  TYR C C   1 
ATOM   6100  O  O   . TYR C  1 208 ? 25.431  11.998  30.722  1.00 24.10 ?  232  TYR C O   1 
ATOM   6101  C  CB  . TYR C  1 208 ? 25.689  11.748  27.468  1.00 23.67 ?  232  TYR C CB  1 
ATOM   6102  C  CG  . TYR C  1 208 ? 24.248  11.408  27.782  1.00 24.35 ?  232  TYR C CG  1 
ATOM   6103  C  CD1 . TYR C  1 208 ? 23.237  12.356  27.624  1.00 24.19 ?  232  TYR C CD1 1 
ATOM   6104  C  CD2 . TYR C  1 208 ? 23.898  10.144  28.258  1.00 24.71 ?  232  TYR C CD2 1 
ATOM   6105  C  CE1 . TYR C  1 208 ? 21.912  12.052  27.919  1.00 25.22 ?  232  TYR C CE1 1 
ATOM   6106  C  CE2 . TYR C  1 208 ? 22.578  9.829   28.558  1.00 25.34 ?  232  TYR C CE2 1 
ATOM   6107  C  CZ  . TYR C  1 208 ? 21.591  10.786  28.386  1.00 25.55 ?  232  TYR C CZ  1 
ATOM   6108  O  OH  . TYR C  1 208 ? 20.287  10.476  28.687  1.00 25.71 ?  232  TYR C OH  1 
ATOM   6109  N  N   . THR C  1 209 ? 27.292  10.884  30.111  1.00 23.97 ?  233  THR C N   1 
ATOM   6110  C  CA  . THR C  1 209 ? 27.398  10.137  31.368  1.00 24.20 ?  233  THR C CA  1 
ATOM   6111  C  C   . THR C  1 209 ? 27.528  11.099  32.552  1.00 24.32 ?  233  THR C C   1 
ATOM   6112  O  O   . THR C  1 209 ? 26.791  10.976  33.530  1.00 24.46 ?  233  THR C O   1 
ATOM   6113  C  CB  . THR C  1 209 ? 28.579  9.127   31.351  1.00 24.21 ?  233  THR C CB  1 
ATOM   6114  O  OG1 . THR C  1 209 ? 28.365  8.152   30.322  1.00 24.53 ?  233  THR C OG1 1 
ATOM   6115  C  CG2 . THR C  1 209 ? 28.717  8.414   32.696  1.00 23.66 ?  233  THR C CG2 1 
ATOM   6116  N  N   . ALA C  1 210 ? 28.445  12.062  32.442  1.00 24.44 ?  234  ALA C N   1 
ATOM   6117  C  CA  . ALA C  1 210 ? 28.653  13.082  33.482  1.00 24.68 ?  234  ALA C CA  1 
ATOM   6118  C  C   . ALA C  1 210 ? 27.372  13.841  33.825  1.00 24.74 ?  234  ALA C C   1 
ATOM   6119  O  O   . ALA C  1 210 ? 27.096  14.107  34.999  1.00 25.07 ?  234  ALA C O   1 
ATOM   6120  C  CB  . ALA C  1 210 ? 29.756  14.055  33.068  1.00 24.67 ?  234  ALA C CB  1 
ATOM   6121  N  N   . ASN C  1 211 ? 26.601  14.179  32.793  1.00 24.77 ?  235  ASN C N   1 
ATOM   6122  C  CA  . ASN C  1 211 ? 25.312  14.853  32.947  1.00 24.77 ?  235  ASN C CA  1 
ATOM   6123  C  C   . ASN C  1 211 ? 24.330  14.047  33.800  1.00 24.70 ?  235  ASN C C   1 
ATOM   6124  O  O   . ASN C  1 211 ? 23.827  14.543  34.809  1.00 24.74 ?  235  ASN C O   1 
ATOM   6125  C  CB  . ASN C  1 211 ? 24.712  15.146  31.563  1.00 24.71 ?  235  ASN C CB  1 
ATOM   6126  C  CG  . ASN C  1 211 ? 23.358  15.825  31.635  1.00 24.89 ?  235  ASN C CG  1 
ATOM   6127  O  OD1 . ASN C  1 211 ? 23.251  16.985  32.033  1.00 25.19 ?  235  ASN C OD1 1 
ATOM   6128  N  ND2 . ASN C  1 211 ? 22.316  15.111  31.222  1.00 24.92 ?  235  ASN C ND2 1 
ATOM   6129  N  N   . ILE C  1 212 ? 24.074  12.802  33.396  1.00 24.68 ?  236  ILE C N   1 
ATOM   6130  C  CA  . ILE C  1 212 ? 23.086  11.949  34.067  1.00 24.52 ?  236  ILE C CA  1 
ATOM   6131  C  C   . ILE C  1 212 ? 23.558  11.409  35.428  1.00 24.67 ?  236  ILE C C   1 
ATOM   6132  O  O   . ILE C  1 212 ? 22.742  10.939  36.227  1.00 24.75 ?  236  ILE C O   1 
ATOM   6133  C  CB  . ILE C  1 212 ? 22.588  10.787  33.154  1.00 24.53 ?  236  ILE C CB  1 
ATOM   6134  C  CG1 . ILE C  1 212 ? 23.704  9.767   32.892  1.00 24.62 ?  236  ILE C CG1 1 
ATOM   6135  C  CG2 . ILE C  1 212 ? 21.994  11.339  31.850  1.00 24.38 ?  236  ILE C CG2 1 
ATOM   6136  C  CD1 . ILE C  1 212 ? 23.286  8.582   32.043  1.00 23.54 ?  236  ILE C CD1 1 
ATOM   6137  N  N   . GLU C  1 213 ? 24.865  11.488  35.684  1.00 24.68 ?  237  GLU C N   1 
ATOM   6138  C  CA  . GLU C  1 213 ? 25.439  11.112  36.979  1.00 24.70 ?  237  GLU C CA  1 
ATOM   6139  C  C   . GLU C  1 213 ? 25.544  12.296  37.941  1.00 24.83 ?  237  GLU C C   1 
ATOM   6140  O  O   . GLU C  1 213 ? 26.072  12.158  39.049  1.00 24.81 ?  237  GLU C O   1 
ATOM   6141  C  CB  . GLU C  1 213 ? 26.811  10.447  36.812  1.00 24.72 ?  237  GLU C CB  1 
ATOM   6142  C  CG  . GLU C  1 213 ? 26.788  9.059   36.158  1.00 25.00 ?  237  GLU C CG  1 
ATOM   6143  C  CD  . GLU C  1 213 ? 26.013  8.017   36.951  1.00 25.44 ?  237  GLU C CD  1 
ATOM   6144  O  OE1 . GLU C  1 213 ? 25.809  8.205   38.172  1.00 26.35 ?  237  GLU C OE1 1 
ATOM   6145  O  OE2 . GLU C  1 213 ? 25.612  7.001   36.348  1.00 25.40 -1 237  GLU C OE2 1 
ATOM   6146  N  N   . THR C  1 214 ? 25.047  13.456  37.511  1.00 24.89 ?  238  THR C N   1 
ATOM   6147  C  CA  . THR C  1 214 ? 24.932  14.619  38.388  1.00 24.93 ?  238  THR C CA  1 
ATOM   6148  C  C   . THR C  1 214 ? 23.640  14.491  39.193  1.00 25.01 ?  238  THR C C   1 
ATOM   6149  O  O   . THR C  1 214 ? 22.545  14.391  38.624  1.00 24.96 ?  238  THR C O   1 
ATOM   6150  C  CB  . THR C  1 214 ? 24.952  15.946  37.593  1.00 25.03 ?  238  THR C CB  1 
ATOM   6151  O  OG1 . THR C  1 214 ? 26.131  16.001  36.781  1.00 24.88 ?  238  THR C OG1 1 
ATOM   6152  C  CG2 . THR C  1 214 ? 24.938  17.147  38.534  1.00 25.06 ?  238  THR C CG2 1 
ATOM   6153  N  N   . THR C  1 215 ? 23.776  14.490  40.518  1.00 24.90 ?  239  THR C N   1 
ATOM   6154  C  CA  . THR C  1 215 ? 22.648  14.214  41.411  1.00 24.90 ?  239  THR C CA  1 
ATOM   6155  C  C   . THR C  1 215 ? 21.455  15.137  41.169  1.00 24.83 ?  239  THR C C   1 
ATOM   6156  O  O   . THR C  1 215 ? 20.347  14.657  40.945  1.00 25.14 ?  239  THR C O   1 
ATOM   6157  C  CB  . THR C  1 215 ? 23.062  14.241  42.898  1.00 24.81 ?  239  THR C CB  1 
ATOM   6158  O  OG1 . THR C  1 215 ? 24.262  13.481  43.070  1.00 24.22 ?  239  THR C OG1 1 
ATOM   6159  C  CG2 . THR C  1 215 ? 21.971  13.631  43.766  1.00 24.95 ?  239  THR C CG2 1 
ATOM   6160  N  N   . VAL C  1 216 ? 21.690  16.449  41.183  1.00 24.77 ?  240  VAL C N   1 
ATOM   6161  C  CA  . VAL C  1 216 ? 20.609  17.426  41.011  1.00 24.38 ?  240  VAL C CA  1 
ATOM   6162  C  C   . VAL C  1 216 ? 19.873  17.276  39.672  1.00 24.37 ?  240  VAL C C   1 
ATOM   6163  O  O   . VAL C  1 216 ? 18.653  17.448  39.612  1.00 24.38 ?  240  VAL C O   1 
ATOM   6164  C  CB  . VAL C  1 216 ? 21.091  18.889  41.245  1.00 24.67 ?  240  VAL C CB  1 
ATOM   6165  C  CG1 . VAL C  1 216 ? 21.967  19.394  40.091  1.00 24.01 ?  240  VAL C CG1 1 
ATOM   6166  C  CG2 . VAL C  1 216 ? 19.902  19.820  41.492  1.00 24.33 ?  240  VAL C CG2 1 
ATOM   6167  N  N   . TRP C  1 217 ? 20.610  16.939  38.615  1.00 24.17 ?  241  TRP C N   1 
ATOM   6168  C  CA  . TRP C  1 217 ? 20.008  16.673  37.310  1.00 23.81 ?  241  TRP C CA  1 
ATOM   6169  C  C   . TRP C  1 217 ? 18.965  15.559  37.404  1.00 23.76 ?  241  TRP C C   1 
ATOM   6170  O  O   . TRP C  1 217 ? 17.882  15.666  36.823  1.00 23.45 ?  241  TRP C O   1 
ATOM   6171  C  CB  . TRP C  1 217 ? 21.073  16.307  36.271  1.00 23.50 ?  241  TRP C CB  1 
ATOM   6172  C  CG  . TRP C  1 217 ? 20.491  16.103  34.893  1.00 23.41 ?  241  TRP C CG  1 
ATOM   6173  C  CD1 . TRP C  1 217 ? 20.344  17.049  33.918  1.00 22.50 ?  241  TRP C CD1 1 
ATOM   6174  C  CD2 . TRP C  1 217 ? 19.960  14.882  34.351  1.00 22.88 ?  241  TRP C CD2 1 
ATOM   6175  N  NE1 . TRP C  1 217 ? 19.764  16.494  32.802  1.00 22.71 ?  241  TRP C NE1 1 
ATOM   6176  C  CE2 . TRP C  1 217 ? 19.514  15.167  33.039  1.00 22.81 ?  241  TRP C CE2 1 
ATOM   6177  C  CE3 . TRP C  1 217 ? 19.824  13.575  34.844  1.00 22.79 ?  241  TRP C CE3 1 
ATOM   6178  C  CZ2 . TRP C  1 217 ? 18.941  14.191  32.210  1.00 22.29 ?  241  TRP C CZ2 1 
ATOM   6179  C  CZ3 . TRP C  1 217 ? 19.252  12.605  34.021  1.00 22.18 ?  241  TRP C CZ3 1 
ATOM   6180  C  CH2 . TRP C  1 217 ? 18.816  12.921  32.718  1.00 22.69 ?  241  TRP C CH2 1 
ATOM   6181  N  N   . ALA C  1 218 ? 19.310  14.493  38.124  1.00 23.87 ?  242  ALA C N   1 
ATOM   6182  C  CA  . ALA C  1 218 ? 18.421  13.348  38.310  1.00 24.11 ?  242  ALA C CA  1 
ATOM   6183  C  C   . ALA C  1 218 ? 17.330  13.623  39.343  1.00 24.25 ?  242  ALA C C   1 
ATOM   6184  O  O   . ALA C  1 218 ? 16.212  13.119  39.213  1.00 24.62 ?  242  ALA C O   1 
ATOM   6185  C  CB  . ALA C  1 218 ? 19.223  12.110  38.701  1.00 24.04 ?  242  ALA C CB  1 
ATOM   6186  N  N   . ALA C  1 219 ? 17.660  14.430  40.352  1.00 24.21 ?  243  ALA C N   1 
ATOM   6187  C  CA  . ALA C  1 219 ? 16.786  14.664  41.508  1.00 24.16 ?  243  ALA C CA  1 
ATOM   6188  C  C   . ALA C  1 219 ? 15.707  15.743  41.329  1.00 24.19 ?  243  ALA C C   1 
ATOM   6189  O  O   . ALA C  1 219 ? 14.620  15.625  41.900  1.00 23.98 ?  243  ALA C O   1 
ATOM   6190  C  CB  . ALA C  1 219 ? 17.630  14.967  42.749  1.00 24.24 ?  243  ALA C CB  1 
ATOM   6191  N  N   . MET C  1 220 ? 16.013  16.795  40.566  1.00 24.22 ?  244  MET C N   1 
ATOM   6192  C  CA  . MET C  1 220 ? 15.106  17.945  40.421  1.00 23.99 ?  244  MET C CA  1 
ATOM   6193  C  C   . MET C  1 220 ? 13.841  17.606  39.618  1.00 24.08 ?  244  MET C C   1 
ATOM   6194  O  O   . MET C  1 220 ? 13.898  16.809  38.685  1.00 24.23 ?  244  MET C O   1 
ATOM   6195  C  CB  . MET C  1 220 ? 15.841  19.164  39.826  1.00 24.10 ?  244  MET C CB  1 
ATOM   6196  C  CG  . MET C  1 220 ? 16.261  19.037  38.356  1.00 23.35 ?  244  MET C CG  1 
ATOM   6197  S  SD  . MET C  1 220 ? 17.496  20.258  37.853  1.00 23.82 ?  244  MET C SD  1 
ATOM   6198  C  CE  . MET C  1 220 ? 16.492  21.741  37.709  1.00 22.88 ?  244  MET C CE  1 
ATOM   6199  N  N   . PRO C  1 221 ? 12.691  18.200  39.997  1.00 24.14 ?  245  PRO C N   1 
ATOM   6200  C  CA  . PRO C  1 221 ? 11.430  17.976  39.280  1.00 24.19 ?  245  PRO C CA  1 
ATOM   6201  C  C   . PRO C  1 221 ? 11.307  18.713  37.934  1.00 24.08 ?  245  PRO C C   1 
ATOM   6202  O  O   . PRO C  1 221 ? 10.571  18.258  37.058  1.00 24.00 ?  245  PRO C O   1 
ATOM   6203  C  CB  . PRO C  1 221 ? 10.378  18.500  40.261  1.00 24.08 ?  245  PRO C CB  1 
ATOM   6204  C  CG  . PRO C  1 221 ? 11.097  19.551  41.042  1.00 24.34 ?  245  PRO C CG  1 
ATOM   6205  C  CD  . PRO C  1 221 ? 12.494  19.025  41.205  1.00 24.14 ?  245  PRO C CD  1 
ATOM   6206  N  N   . GLN C  1 222 ? 12.007  19.838  37.785  1.00 23.94 ?  246  GLN C N   1 
ATOM   6207  C  CA  . GLN C  1 222 ? 11.932  20.651  36.564  1.00 24.01 ?  246  GLN C CA  1 
ATOM   6208  C  C   . GLN C  1 222 ? 12.685  19.984  35.405  1.00 23.86 ?  246  GLN C C   1 
ATOM   6209  O  O   . GLN C  1 222 ? 13.804  20.378  35.072  1.00 24.01 ?  246  GLN C O   1 
ATOM   6210  C  CB  . GLN C  1 222 ? 12.475  22.069  36.813  1.00 23.83 ?  246  GLN C CB  1 
ATOM   6211  C  CG  . GLN C  1 222 ? 11.774  22.858  37.929  1.00 23.74 ?  246  GLN C CG  1 
ATOM   6212  C  CD  . GLN C  1 222 ? 12.332  22.577  39.318  1.00 23.34 ?  246  GLN C CD  1 
ATOM   6213  O  OE1 . GLN C  1 222 ? 13.216  21.742  39.488  1.00 24.56 ?  246  GLN C OE1 1 
ATOM   6214  N  NE2 . GLN C  1 222 ? 11.813  23.279  40.319  1.00 23.51 ?  246  GLN C NE2 1 
ATOM   6215  N  N   . ARG C  1 223 ? 12.059  18.981  34.791  1.00 23.70 ?  247  ARG C N   1 
ATOM   6216  C  CA  . ARG C  1 223 ? 12.722  18.160  33.774  1.00 23.58 ?  247  ARG C CA  1 
ATOM   6217  C  C   . ARG C  1 223 ? 13.169  18.971  32.557  1.00 23.38 ?  247  ARG C C   1 
ATOM   6218  O  O   . ARG C  1 223 ? 14.238  18.724  31.995  1.00 23.46 ?  247  ARG C O   1 
ATOM   6219  C  CB  . ARG C  1 223 ? 11.834  16.985  33.340  1.00 23.66 ?  247  ARG C CB  1 
ATOM   6220  C  CG  . ARG C  1 223 ? 11.501  15.947  34.442  1.00 24.01 ?  247  ARG C CG  1 
ATOM   6221  C  CD  . ARG C  1 223 ? 12.714  15.550  35.298  1.00 23.97 ?  247  ARG C CD  1 
ATOM   6222  N  NE  . ARG C  1 223 ? 13.842  15.079  34.491  1.00 24.48 ?  247  ARG C NE  1 
ATOM   6223  C  CZ  . ARG C  1 223 ? 15.096  14.996  34.926  1.00 24.14 ?  247  ARG C CZ  1 
ATOM   6224  N  NH1 . ARG C  1 223 ? 15.398  15.345  36.168  1.00 24.93 ?  247  ARG C NH1 1 
ATOM   6225  N  NH2 . ARG C  1 223 ? 16.053  14.564  34.117  1.00 23.91 ?  247  ARG C NH2 1 
ATOM   6226  N  N   . GLU C  1 224 ? 12.352  19.945  32.173  1.00 22.95 ?  248  GLU C N   1 
ATOM   6227  C  CA  . GLU C  1 224 ? 12.626  20.785  31.019  1.00 22.74 ?  248  GLU C CA  1 
ATOM   6228  C  C   . GLU C  1 224 ? 13.825  21.710  31.262  1.00 22.69 ?  248  GLU C C   1 
ATOM   6229  O  O   . GLU C  1 224 ? 14.555  22.042  30.324  1.00 22.57 ?  248  GLU C O   1 
ATOM   6230  C  CB  . GLU C  1 224 ? 11.369  21.566  30.621  1.00 22.76 ?  248  GLU C CB  1 
ATOM   6231  C  CG  . GLU C  1 224 ? 10.303  20.729  29.886  1.00 22.92 ?  248  GLU C CG  1 
ATOM   6232  C  CD  . GLU C  1 224 ? 9.642   19.635  30.732  1.00 23.78 ?  248  GLU C CD  1 
ATOM   6233  O  OE1 . GLU C  1 224 ? 9.633   19.726  31.982  1.00 23.43 ?  248  GLU C OE1 1 
ATOM   6234  O  OE2 . GLU C  1 224 ? 9.111   18.674  30.135  1.00 24.65 -1 248  GLU C OE2 1 
ATOM   6235  N  N   . VAL C  1 225 ? 14.028  22.106  32.520  1.00 22.35 ?  249  VAL C N   1 
ATOM   6236  C  CA  . VAL C  1 225 ? 15.239  22.819  32.927  1.00 22.35 ?  249  VAL C CA  1 
ATOM   6237  C  C   . VAL C  1 225 ? 16.452  21.882  32.880  1.00 22.41 ?  249  VAL C C   1 
ATOM   6238  O  O   . VAL C  1 225 ? 17.462  22.200  32.250  1.00 22.41 ?  249  VAL C O   1 
ATOM   6239  C  CB  . VAL C  1 225 ? 15.105  23.449  34.341  1.00 22.49 ?  249  VAL C CB  1 
ATOM   6240  C  CG1 . VAL C  1 225 ? 16.419  24.102  34.772  1.00 22.64 ?  249  VAL C CG1 1 
ATOM   6241  C  CG2 . VAL C  1 225 ? 13.970  24.461  34.375  1.00 21.74 ?  249  VAL C CG2 1 
ATOM   6242  N  N   . ALA C  1 226 ? 16.336  20.723  33.528  1.00 22.48 ?  250  ALA C N   1 
ATOM   6243  C  CA  . ALA C  1 226 ? 17.397  19.707  33.529  1.00 22.72 ?  250  ALA C CA  1 
ATOM   6244  C  C   . ALA C  1 226 ? 17.819  19.285  32.124  1.00 22.83 ?  250  ALA C C   1 
ATOM   6245  O  O   . ALA C  1 226 ? 18.980  18.965  31.896  1.00 23.08 ?  250  ALA C O   1 
ATOM   6246  C  CB  . ALA C  1 226 ? 16.973  18.484  34.348  1.00 22.60 ?  250  ALA C CB  1 
ATOM   6247  N  N   . GLU C  1 227 ? 16.879  19.308  31.183  1.00 23.09 ?  251  GLU C N   1 
ATOM   6248  C  CA  . GLU C  1 227 ? 17.144  18.870  29.814  1.00 23.36 ?  251  GLU C CA  1 
ATOM   6249  C  C   . GLU C  1 227 ? 17.937  19.883  28.987  1.00 23.06 ?  251  GLU C C   1 
ATOM   6250  O  O   . GLU C  1 227 ? 18.535  19.529  27.967  1.00 22.91 ?  251  GLU C O   1 
ATOM   6251  C  CB  . GLU C  1 227 ? 15.838  18.506  29.109  1.00 23.75 ?  251  GLU C CB  1 
ATOM   6252  C  CG  . GLU C  1 227 ? 15.906  17.184  28.375  1.00 25.79 ?  251  GLU C CG  1 
ATOM   6253  C  CD  . GLU C  1 227 ? 16.268  16.028  29.301  1.00 28.12 ?  251  GLU C CD  1 
ATOM   6254  O  OE1 . GLU C  1 227 ? 15.510  15.747  30.258  1.00 29.82 ?  251  GLU C OE1 1 
ATOM   6255  O  OE2 . GLU C  1 227 ? 17.313  15.398  29.067  1.00 28.14 -1 251  GLU C OE2 1 
ATOM   6256  N  N   . GLY C  1 228 ? 17.928  21.142  29.421  1.00 22.90 ?  252  GLY C N   1 
ATOM   6257  C  CA  . GLY C  1 228 ? 18.814  22.164  28.857  1.00 22.62 ?  252  GLY C CA  1 
ATOM   6258  C  C   . GLY C  1 228 ? 20.272  21.798  29.083  1.00 22.51 ?  252  GLY C C   1 
ATOM   6259  O  O   . GLY C  1 228 ? 21.108  21.970  28.197  1.00 22.65 ?  252  GLY C O   1 
ATOM   6260  N  N   . CYS C  1 229 ? 20.569  21.283  30.274  1.00 22.34 ?  253  CYS C N   1 
ATOM   6261  C  CA  . CYS C  1 229 ? 21.892  20.747  30.584  1.00 22.28 ?  253  CYS C CA  1 
ATOM   6262  C  C   . CYS C  1 229 ? 22.249  19.610  29.621  1.00 22.31 ?  253  CYS C C   1 
ATOM   6263  O  O   . CYS C  1 229 ? 23.340  19.587  29.055  1.00 22.35 ?  253  CYS C O   1 
ATOM   6264  C  CB  . CYS C  1 229 ? 21.951  20.271  32.040  1.00 22.06 ?  253  CYS C CB  1 
ATOM   6265  S  SG  . CYS C  1 229 ? 21.547  21.549  33.279  1.00 21.61 ?  253  CYS C SG  1 
ATOM   6266  N  N   . THR C  1 230 ? 21.301  18.698  29.414  1.00 22.43 ?  254  THR C N   1 
ATOM   6267  C  CA  . THR C  1 230 ? 21.469  17.561  28.508  1.00 22.41 ?  254  THR C CA  1 
ATOM   6268  C  C   . THR C  1 230 ? 21.859  17.989  27.094  1.00 22.58 ?  254  THR C C   1 
ATOM   6269  O  O   . THR C  1 230 ? 22.694  17.344  26.458  1.00 22.45 ?  254  THR C O   1 
ATOM   6270  C  CB  . THR C  1 230 ? 20.183  16.701  28.458  1.00 22.36 ?  254  THR C CB  1 
ATOM   6271  O  OG1 . THR C  1 230 ? 19.797  16.350  29.791  1.00 22.48 ?  254  THR C OG1 1 
ATOM   6272  C  CG2 . THR C  1 230 ? 20.394  15.429  27.649  1.00 22.32 ?  254  THR C CG2 1 
ATOM   6273  N  N   . MET C  1 231 ? 21.261  19.080  26.617  1.00 22.71 ?  255  MET C N   1 
ATOM   6274  C  CA  . MET C  1 231 ? 21.489  19.576  25.255  1.00 23.10 ?  255  MET C CA  1 
ATOM   6275  C  C   . MET C  1 231 ? 22.940  19.986  24.973  1.00 22.94 ?  255  MET C C   1 
ATOM   6276  O  O   . MET C  1 231 ? 23.401  19.906  23.835  1.00 23.16 ?  255  MET C O   1 
ATOM   6277  C  CB  . MET C  1 231 ? 20.515  20.712  24.925  1.00 23.13 ?  255  MET C CB  1 
ATOM   6278  C  CG  . MET C  1 231 ? 19.078  20.224  24.719  1.00 24.49 ?  255  MET C CG  1 
ATOM   6279  S  SD  . MET C  1 231 ? 17.884  21.497  24.256  1.00 26.81 ?  255  MET C SD  1 
ATOM   6280  C  CE  . MET C  1 231 ? 18.587  22.078  22.712  1.00 25.50 ?  255  MET C CE  1 
ATOM   6281  N  N   . CYS C  1 232 ? 23.648  20.424  26.012  1.00 22.94 ?  256  CYS C N   1 
ATOM   6282  C  CA  . CYS C  1 232 ? 25.072  20.747  25.916  1.00 22.71 ?  256  CYS C CA  1 
ATOM   6283  C  C   . CYS C  1 232 ? 25.947  19.520  26.153  1.00 22.66 ?  256  CYS C C   1 
ATOM   6284  O  O   . CYS C  1 232 ? 27.169  19.586  26.013  1.00 22.77 ?  256  CYS C O   1 
ATOM   6285  C  CB  . CYS C  1 232 ? 25.446  21.787  26.968  1.00 22.85 ?  256  CYS C CB  1 
ATOM   6286  S  SG  . CYS C  1 232 ? 24.842  23.463  26.722  1.00 22.59 ?  256  CYS C SG  1 
ATOM   6287  N  N   . HIS C  1 233 ? 25.324  18.410  26.536  1.00 22.46 ?  257  HIS C N   1 
ATOM   6288  C  CA  . HIS C  1 233 ? 26.057  17.234  26.986  1.00 22.22 ?  257  HIS C CA  1 
ATOM   6289  C  C   . HIS C  1 233 ? 25.745  15.988  26.130  1.00 22.09 ?  257  HIS C C   1 
ATOM   6290  O  O   . HIS C  1 233 ? 25.666  14.885  26.656  1.00 22.00 ?  257  HIS C O   1 
ATOM   6291  C  CB  . HIS C  1 233 ? 25.743  16.966  28.474  1.00 22.32 ?  257  HIS C CB  1 
ATOM   6292  C  CG  . HIS C  1 233 ? 26.460  17.869  29.441  1.00 22.20 ?  257  HIS C CG  1 
ATOM   6293  N  ND1 . HIS C  1 233 ? 27.585  17.470  30.132  1.00 21.61 ?  257  HIS C ND1 1 
ATOM   6294  C  CD2 . HIS C  1 233 ? 26.189  19.130  29.867  1.00 22.16 ?  257  HIS C CD2 1 
ATOM   6295  C  CE1 . HIS C  1 233 ? 27.991  18.452  30.919  1.00 22.20 ?  257  HIS C CE1 1 
ATOM   6296  N  NE2 . HIS C  1 233 ? 27.163  19.474  30.780  1.00 22.28 ?  257  HIS C NE2 1 
ATOM   6297  N  N   . THR C  1 234 ? 25.583  16.164  24.816  1.00 21.96 ?  258  THR C N   1 
ATOM   6298  C  CA  . THR C  1 234 ? 25.181  15.054  23.920  1.00 21.81 ?  258  THR C CA  1 
ATOM   6299  C  C   . THR C  1 234 ? 26.255  14.470  22.989  1.00 21.78 ?  258  THR C C   1 
ATOM   6300  O  O   . THR C  1 234 ? 25.966  13.529  22.234  1.00 21.46 ?  258  THR C O   1 
ATOM   6301  C  CB  . THR C  1 234 ? 24.012  15.457  23.004  1.00 21.76 ?  258  THR C CB  1 
ATOM   6302  O  OG1 . THR C  1 234 ? 24.276  16.752  22.452  1.00 22.31 ?  258  THR C OG1 1 
ATOM   6303  C  CG2 . THR C  1 234 ? 22.695  15.470  23.761  1.00 21.24 ?  258  THR C CG2 1 
ATOM   6304  N  N   . ASN C  1 235 ? 27.469  15.022  23.018  1.00 21.72 ?  259  ASN C N   1 
ATOM   6305  C  CA  . ASN C  1 235 ? 28.543  14.572  22.119  1.00 22.01 ?  259  ASN C CA  1 
ATOM   6306  C  C   . ASN C  1 235 ? 28.804  13.065  22.163  1.00 22.05 ?  259  ASN C C   1 
ATOM   6307  O  O   . ASN C  1 235 ? 29.032  12.439  21.127  1.00 21.97 ?  259  ASN C O   1 
ATOM   6308  C  CB  . ASN C  1 235 ? 29.838  15.345  22.375  1.00 21.90 ?  259  ASN C CB  1 
ATOM   6309  C  CG  . ASN C  1 235 ? 29.703  16.822  22.058  1.00 22.26 ?  259  ASN C CG  1 
ATOM   6310  O  OD1 . ASN C  1 235 ? 29.333  17.202  20.945  1.00 21.80 ?  259  ASN C OD1 1 
ATOM   6311  N  ND2 . ASN C  1 235 ? 30.002  17.663  23.039  1.00 22.17 ?  259  ASN C ND2 1 
ATOM   6312  N  N   . GLN C  1 236 ? 28.762  12.503  23.368  1.00 22.11 ?  260  GLN C N   1 
ATOM   6313  C  CA  . GLN C  1 236 ? 28.878  11.063  23.592  1.00 22.31 ?  260  GLN C CA  1 
ATOM   6314  C  C   . GLN C  1 236 ? 27.878  10.266  22.750  1.00 22.36 ?  260  GLN C C   1 
ATOM   6315  O  O   . GLN C  1 236 ? 28.212  9.208   22.219  1.00 22.39 ?  260  GLN C O   1 
ATOM   6316  C  CB  . GLN C  1 236 ? 28.680  10.761  25.082  1.00 22.30 ?  260  GLN C CB  1 
ATOM   6317  C  CG  . GLN C  1 236 ? 28.551  9.282   25.447  1.00 22.77 ?  260  GLN C CG  1 
ATOM   6318  C  CD  . GLN C  1 236 ? 28.560  9.042   26.946  1.00 23.05 ?  260  GLN C CD  1 
ATOM   6319  O  OE1 . GLN C  1 236 ? 28.553  9.984   27.745  1.00 23.25 ?  260  GLN C OE1 1 
ATOM   6320  N  NE2 . GLN C  1 236 ? 28.581  7.772   27.337  1.00 23.25 ?  260  GLN C NE2 1 
ATOM   6321  N  N   . ASN C  1 237 ? 26.662  10.795  22.621  1.00 22.30 ?  261  ASN C N   1 
ATOM   6322  C  CA  . ASN C  1 237 ? 25.577  10.099  21.940  1.00 22.02 ?  261  ASN C CA  1 
ATOM   6323  C  C   . ASN C  1 237 ? 25.503  10.346  20.439  1.00 22.00 ?  261  ASN C C   1 
ATOM   6324  O  O   . ASN C  1 237 ? 25.247  9.418   19.677  1.00 22.15 ?  261  ASN C O   1 
ATOM   6325  C  CB  . ASN C  1 237 ? 24.238  10.416  22.619  1.00 21.94 ?  261  ASN C CB  1 
ATOM   6326  C  CG  . ASN C  1 237 ? 24.182  9.907   24.052  1.00 21.93 ?  261  ASN C CG  1 
ATOM   6327  O  OD1 . ASN C  1 237 ? 24.987  9.068   24.451  1.00 21.85 ?  261  ASN C OD1 1 
ATOM   6328  N  ND2 . ASN C  1 237 ? 23.234  10.411  24.829  1.00 21.74 ?  261  ASN C ND2 1 
ATOM   6329  N  N   . LYS C  1 238 ? 25.729  11.589  20.018  1.00 21.77 ?  262  LYS C N   1 
ATOM   6330  C  CA  . LYS C  1 238 ? 25.619  11.955  18.606  1.00 21.65 ?  262  LYS C CA  1 
ATOM   6331  C  C   . LYS C  1 238 ? 26.743  12.900  18.171  1.00 21.69 ?  262  LYS C C   1 
ATOM   6332  O  O   . LYS C  1 238 ? 27.244  13.693  18.974  1.00 21.65 ?  262  LYS C O   1 
ATOM   6333  C  CB  . LYS C  1 238 ? 24.232  12.542  18.291  1.00 21.53 ?  262  LYS C CB  1 
ATOM   6334  C  CG  . LYS C  1 238 ? 23.873  13.802  19.070  1.00 21.73 ?  262  LYS C CG  1 
ATOM   6335  C  CD  . LYS C  1 238 ? 22.450  14.258  18.769  1.00 21.77 ?  262  LYS C CD  1 
ATOM   6336  C  CE  . LYS C  1 238 ? 22.136  15.583  19.451  1.00 22.17 ?  262  LYS C CE  1 
ATOM   6337  N  NZ  . LYS C  1 238 ? 22.802  16.738  18.783  1.00 22.19 ?  262  LYS C NZ  1 
ATOM   6338  N  N   . CYS C  1 239 ? 27.115  12.810  16.895  1.00 21.54 ?  263  CYS C N   1 
ATOM   6339  C  CA  . CYS C  1 239 ? 28.308  13.469  16.358  1.00 21.60 ?  263  CYS C CA  1 
ATOM   6340  C  C   . CYS C  1 239 ? 28.019  14.759  15.581  1.00 21.52 ?  263  CYS C C   1 
ATOM   6341  O  O   . CYS C  1 239 ? 28.861  15.217  14.805  1.00 21.59 ?  263  CYS C O   1 
ATOM   6342  C  CB  . CYS C  1 239 ? 29.062  12.500  15.440  1.00 21.49 ?  263  CYS C CB  1 
ATOM   6343  S  SG  . CYS C  1 239 ? 29.875  11.117  16.256  1.00 22.18 ?  263  CYS C SG  1 
ATOM   6344  N  N   . ASP C  1 240 ? 26.845  15.349  15.787  1.00 21.50 ?  264  ASP C N   1 
ATOM   6345  C  CA  . ASP C  1 240 ? 26.426  16.494  14.974  1.00 21.43 ?  264  ASP C CA  1 
ATOM   6346  C  C   . ASP C  1 240 ? 26.355  17.829  15.719  1.00 21.39 ?  264  ASP C C   1 
ATOM   6347  O  O   . ASP C  1 240 ? 25.602  18.724  15.321  1.00 21.52 ?  264  ASP C O   1 
ATOM   6348  C  CB  . ASP C  1 240 ? 25.088  16.192  14.274  1.00 21.53 ?  264  ASP C CB  1 
ATOM   6349  C  CG  . ASP C  1 240 ? 23.934  16.013  15.252  1.00 21.30 ?  264  ASP C CG  1 
ATOM   6350  O  OD1 . ASP C  1 240 ? 24.180  15.837  16.466  1.00 20.93 ?  264  ASP C OD1 1 
ATOM   6351  O  OD2 . ASP C  1 240 ? 22.772  16.041  14.797  1.00 21.66 -1 264  ASP C OD2 1 
ATOM   6352  N  N   . ASN C  1 241 ? 27.136  17.973  16.786  1.00 21.32 ?  265  ASN C N   1 
ATOM   6353  C  CA  . ASN C  1 241 ? 27.125  19.215  17.565  1.00 21.30 ?  265  ASN C CA  1 
ATOM   6354  C  C   . ASN C  1 241 ? 28.152  20.261  17.097  1.00 21.34 ?  265  ASN C C   1 
ATOM   6355  O  O   . ASN C  1 241 ? 27.966  21.458  17.332  1.00 21.44 ?  265  ASN C O   1 
ATOM   6356  C  CB  . ASN C  1 241 ? 27.275  18.929  19.064  1.00 21.20 ?  265  ASN C CB  1 
ATOM   6357  C  CG  . ASN C  1 241 ? 26.060  18.212  19.661  1.00 21.49 ?  265  ASN C CG  1 
ATOM   6358  O  OD1 . ASN C  1 241 ? 24.913  18.476  19.292  1.00 21.70 ?  265  ASN C OD1 1 
ATOM   6359  N  ND2 . ASN C  1 241 ? 26.316  17.308  20.599  1.00 20.03 ?  265  ASN C ND2 1 
ATOM   6360  N  N   . CYS C  1 242 ? 29.225  19.810  16.444  1.00 21.09 ?  266  CYS C N   1 
ATOM   6361  C  CA  . CYS C  1 242 ? 30.226  20.713  15.856  1.00 21.00 ?  266  CYS C CA  1 
ATOM   6362  C  C   . CYS C  1 242 ? 30.046  20.849  14.345  1.00 20.98 ?  266  CYS C C   1 
ATOM   6363  O  O   . CYS C  1 242 ? 29.965  21.963  13.823  1.00 20.95 ?  266  CYS C O   1 
ATOM   6364  C  CB  . CYS C  1 242 ? 31.647  20.241  16.175  1.00 20.88 ?  266  CYS C CB  1 
ATOM   6365  S  SG  . CYS C  1 242 ? 32.019  20.154  17.939  1.00 20.58 ?  266  CYS C SG  1 
ATOM   6366  N  N   . HIS C  1 243 ? 30.025  19.713  13.648  1.00 20.94 ?  267  HIS C N   1 
ATOM   6367  C  CA  . HIS C  1 243 ? 29.576  19.668  12.260  1.00 20.91 ?  267  HIS C CA  1 
ATOM   6368  C  C   . HIS C  1 243 ? 28.127  19.169  12.243  1.00 20.94 ?  267  HIS C C   1 
ATOM   6369  O  O   . HIS C  1 243 ? 27.874  17.968  12.358  1.00 20.94 ?  267  HIS C O   1 
ATOM   6370  C  CB  . HIS C  1 243 ? 30.508  18.831  11.342  1.00 20.83 ?  267  HIS C CB  1 
ATOM   6371  C  CG  . HIS C  1 243 ? 31.270  17.735  12.036  1.00 20.94 ?  267  HIS C CG  1 
ATOM   6372  N  ND1 . HIS C  1 243 ? 30.665  16.599  12.529  1.00 21.12 ?  267  HIS C ND1 1 
ATOM   6373  C  CD2 . HIS C  1 243 ? 32.597  17.586  12.275  1.00 20.35 ?  267  HIS C CD2 1 
ATOM   6374  C  CE1 . HIS C  1 243 ? 31.581  15.810  13.063  1.00 21.00 ?  267  HIS C CE1 1 
ATOM   6375  N  NE2 . HIS C  1 243 ? 32.765  16.386  12.927  1.00 21.36 ?  267  HIS C NE2 1 
ATOM   6376  N  N   . THR C  1 244 ? 27.190  20.110  12.117  1.00 20.95 ?  268  THR C N   1 
ATOM   6377  C  CA  . THR C  1 244 ? 25.752  19.851  12.285  1.00 20.98 ?  268  THR C CA  1 
ATOM   6378  C  C   . THR C  1 244 ? 25.108  19.063  11.145  1.00 21.35 ?  268  THR C C   1 
ATOM   6379  O  O   . THR C  1 244 ? 25.647  19.002  10.040  1.00 21.42 ?  268  THR C O   1 
ATOM   6380  C  CB  . THR C  1 244 ? 24.950  21.172  12.444  1.00 21.10 ?  268  THR C CB  1 
ATOM   6381  O  OG1 . THR C  1 244 ? 25.187  22.028  11.317  1.00 20.13 ?  268  THR C OG1 1 
ATOM   6382  C  CG2 . THR C  1 244 ? 25.333  21.897  13.738  1.00 20.52 ?  268  THR C CG2 1 
ATOM   6383  N  N   . ARG C  1 245 ? 23.950  18.464  11.429  1.00 21.46 ?  269  ARG C N   1 
ATOM   6384  C  CA  . ARG C  1 245 ? 23.074  17.924  10.388  1.00 21.89 ?  269  ARG C CA  1 
ATOM   6385  C  C   . ARG C  1 245 ? 22.409  19.081  9.633   1.00 21.98 ?  269  ARG C C   1 
ATOM   6386  O  O   . ARG C  1 245 ? 22.195  20.143  10.214  1.00 21.98 ?  269  ARG C O   1 
ATOM   6387  C  CB  . ARG C  1 245 ? 22.016  16.990  10.996  1.00 21.81 ?  269  ARG C CB  1 
ATOM   6388  C  CG  . ARG C  1 245 ? 21.015  17.653  11.949  1.00 21.91 ?  269  ARG C CG  1 
ATOM   6389  C  CD  . ARG C  1 245 ? 20.198  16.601  12.665  1.00 22.03 ?  269  ARG C CD  1 
ATOM   6390  N  NE  . ARG C  1 245 ? 19.089  17.141  13.456  1.00 22.94 ?  269  ARG C NE  1 
ATOM   6391  C  CZ  . ARG C  1 245 ? 19.162  17.493  14.738  1.00 21.88 ?  269  ARG C CZ  1 
ATOM   6392  N  NH1 . ARG C  1 245 ? 20.305  17.392  15.404  1.00 21.84 ?  269  ARG C NH1 1 
ATOM   6393  N  NH2 . ARG C  1 245 ? 18.083  17.958  15.356  1.00 22.32 ?  269  ARG C NH2 1 
ATOM   6394  N  N   . HIS C  1 246 ? 22.102  18.910  8.346   1.00 22.38 ?  270  HIS C N   1 
ATOM   6395  C  CA  . HIS C  1 246 ? 22.422  17.718  7.566   1.00 22.78 ?  270  HIS C CA  1 
ATOM   6396  C  C   . HIS C  1 246 ? 23.511  18.003  6.524   1.00 23.39 ?  270  HIS C C   1 
ATOM   6397  O  O   . HIS C  1 246 ? 23.686  17.248  5.567   1.00 23.21 ?  270  HIS C O   1 
ATOM   6398  C  CB  . HIS C  1 246 ? 21.155  17.170  6.900   1.00 22.64 ?  270  HIS C CB  1 
ATOM   6399  C  CG  . HIS C  1 246 ? 20.377  16.227  7.766   1.00 22.25 ?  270  HIS C CG  1 
ATOM   6400  N  ND1 . HIS C  1 246 ? 19.352  16.638  8.591   1.00 21.92 ?  270  HIS C ND1 1 
ATOM   6401  C  CD2 . HIS C  1 246 ? 20.487  14.889  7.945   1.00 22.13 ?  270  HIS C CD2 1 
ATOM   6402  C  CE1 . HIS C  1 246 ? 18.855  15.593  9.229   1.00 21.99 ?  270  HIS C CE1 1 
ATOM   6403  N  NE2 . HIS C  1 246 ? 19.523  14.516  8.852   1.00 22.46 ?  270  HIS C NE2 1 
ATOM   6404  N  N   . GLU C  1 247 ? 24.242  19.099  6.726   1.00 24.04 ?  271  GLU C N   1 
ATOM   6405  C  CA  . GLU C  1 247 ? 25.364  19.450  5.857   1.00 24.91 ?  271  GLU C CA  1 
ATOM   6406  C  C   . GLU C  1 247 ? 26.648  18.713  6.253   1.00 24.54 ?  271  GLU C C   1 
ATOM   6407  O  O   . GLU C  1 247 ? 27.456  18.366  5.386   1.00 24.57 ?  271  GLU C O   1 
ATOM   6408  C  CB  . GLU C  1 247 ? 25.586  20.969  5.844   1.00 25.26 ?  271  GLU C CB  1 
ATOM   6409  C  CG  . GLU C  1 247 ? 26.597  21.445  4.806   1.00 28.15 ?  271  GLU C CG  1 
ATOM   6410  C  CD  . GLU C  1 247 ? 26.515  22.940  4.510   1.00 31.75 ?  271  GLU C CD  1 
ATOM   6411  O  OE1 . GLU C  1 247 ? 25.869  23.693  5.282   1.00 32.30 ?  271  GLU C OE1 1 
ATOM   6412  O  OE2 . GLU C  1 247 ? 27.110  23.362  3.492   1.00 34.05 -1 271  GLU C OE2 1 
ATOM   6413  N  N   . PHE C  1 248 ? 26.821  18.473  7.554   1.00 24.12 ?  272  PHE C N   1 
ATOM   6414  C  CA  . PHE C  1 248 ? 28.030  17.833  8.099   1.00 23.95 ?  272  PHE C CA  1 
ATOM   6415  C  C   . PHE C  1 248 ? 29.305  18.384  7.453   1.00 23.98 ?  272  PHE C C   1 
ATOM   6416  O  O   . PHE C  1 248 ? 30.082  17.653  6.834   1.00 24.01 ?  272  PHE C O   1 
ATOM   6417  C  CB  . PHE C  1 248 ? 27.951  16.302  7.991   1.00 23.70 ?  272  PHE C CB  1 
ATOM   6418  C  CG  . PHE C  1 248 ? 26.773  15.708  8.709   1.00 23.56 ?  272  PHE C CG  1 
ATOM   6419  C  CD1 . PHE C  1 248 ? 26.791  15.555  10.094  1.00 22.71 ?  272  PHE C CD1 1 
ATOM   6420  C  CD2 . PHE C  1 248 ? 25.634  15.323  8.004   1.00 23.11 ?  272  PHE C CD2 1 
ATOM   6421  C  CE1 . PHE C  1 248 ? 25.702  15.017  10.766  1.00 22.58 ?  272  PHE C CE1 1 
ATOM   6422  C  CE2 . PHE C  1 248 ? 24.538  14.780  8.670   1.00 23.57 ?  272  PHE C CE2 1 
ATOM   6423  C  CZ  . PHE C  1 248 ? 24.574  14.626  10.057  1.00 22.87 ?  272  PHE C CZ  1 
ATOM   6424  N  N   . SER C  1 249 ? 29.487  19.693  7.596   1.00 23.79 ?  273  SER C N   1 
ATOM   6425  C  CA  . SER C  1 249 ? 30.622  20.399  7.029   1.00 23.79 ?  273  SER C CA  1 
ATOM   6426  C  C   . SER C  1 249 ? 31.775  20.423  8.028   1.00 23.67 ?  273  SER C C   1 
ATOM   6427  O  O   . SER C  1 249 ? 31.603  20.849  9.172   1.00 23.59 ?  273  SER C O   1 
ATOM   6428  C  CB  . SER C  1 249 ? 30.203  21.823  6.646   1.00 23.56 ?  273  SER C CB  1 
ATOM   6429  O  OG  . SER C  1 249 ? 31.324  22.630  6.332   1.00 24.42 ?  273  SER C OG  1 
ATOM   6430  N  N   . ALA C  1 250 ? 32.943  19.945  7.598   1.00 23.68 ?  274  ALA C N   1 
ATOM   6431  C  CA  . ALA C  1 250 ? 34.154  20.009  8.421   1.00 23.54 ?  274  ALA C CA  1 
ATOM   6432  C  C   . ALA C  1 250 ? 34.611  21.457  8.612   1.00 23.62 ?  274  ALA C C   1 
ATOM   6433  O  O   . ALA C  1 250 ? 35.114  21.816  9.685   1.00 23.69 ?  274  ALA C O   1 
ATOM   6434  C  CB  . ALA C  1 250 ? 35.273  19.170  7.813   1.00 23.40 ?  274  ALA C CB  1 
ATOM   6435  N  N   . ALA C  1 251 ? 34.426  22.280  7.577   1.00 23.40 ?  275  ALA C N   1 
ATOM   6436  C  CA  . ALA C  1 251 ? 34.774  23.704  7.633   1.00 23.29 ?  275  ALA C CA  1 
ATOM   6437  C  C   . ALA C  1 251 ? 34.011  24.407  8.751   1.00 23.15 ?  275  ALA C C   1 
ATOM   6438  O  O   . ALA C  1 251 ? 34.595  25.163  9.537   1.00 23.35 ?  275  ALA C O   1 
ATOM   6439  C  CB  . ALA C  1 251 ? 34.509  24.384  6.287   1.00 23.41 ?  275  ALA C CB  1 
ATOM   6440  N  N   . GLU C  1 252 ? 32.707  24.145  8.812   1.00 22.73 ?  276  GLU C N   1 
ATOM   6441  C  CA  . GLU C  1 252 ? 31.848  24.602  9.903   1.00 22.17 ?  276  GLU C CA  1 
ATOM   6442  C  C   . GLU C  1 252 ? 32.404  24.236  11.286  1.00 21.95 ?  276  GLU C C   1 
ATOM   6443  O  O   . GLU C  1 252 ? 32.511  25.098  12.165  1.00 21.83 ?  276  GLU C O   1 
ATOM   6444  C  CB  . GLU C  1 252 ? 30.445  24.017  9.730   1.00 22.18 ?  276  GLU C CB  1 
ATOM   6445  C  CG  . GLU C  1 252 ? 29.462  24.369  10.838  1.00 22.05 ?  276  GLU C CG  1 
ATOM   6446  C  CD  . GLU C  1 252 ? 28.155  23.614  10.712  1.00 21.71 ?  276  GLU C CD  1 
ATOM   6447  O  OE1 . GLU C  1 252 ? 27.582  23.579  9.604   1.00 22.79 ?  276  GLU C OE1 1 
ATOM   6448  O  OE2 . GLU C  1 252 ? 27.695  23.053  11.721  1.00 21.89 -1 276  GLU C OE2 1 
ATOM   6449  N  N   . SER C  1 253 ? 32.752  22.961  11.477  1.00 21.50 ?  277  SER C N   1 
ATOM   6450  C  CA  . SER C  1 253 ? 33.255  22.487  12.771  1.00 21.13 ?  277  SER C CA  1 
ATOM   6451  C  C   . SER C  1 253 ? 34.605  23.101  13.157  1.00 20.90 ?  277  SER C C   1 
ATOM   6452  O  O   . SER C  1 253 ? 34.962  23.132  14.334  1.00 20.61 ?  277  SER C O   1 
ATOM   6453  C  CB  . SER C  1 253 ? 33.320  20.954  12.813  1.00 21.14 ?  277  SER C CB  1 
ATOM   6454  O  OG  . SER C  1 253 ? 34.104  20.427  11.755  1.00 21.25 ?  277  SER C OG  1 
ATOM   6455  N  N   . ARG C  1 254 ? 35.334  23.611  12.164  1.00 20.79 ?  278  ARG C N   1 
ATOM   6456  C  CA  . ARG C  1 254 ? 36.617  24.286  12.400  1.00 20.60 ?  278  ARG C CA  1 
ATOM   6457  C  C   . ARG C  1 254 ? 36.460  25.713  12.928  1.00 20.53 ?  278  ARG C C   1 
ATOM   6458  O  O   . ARG C  1 254 ? 37.383  26.261  13.541  1.00 20.40 ?  278  ARG C O   1 
ATOM   6459  C  CB  . ARG C  1 254 ? 37.477  24.275  11.130  1.00 20.46 ?  278  ARG C CB  1 
ATOM   6460  C  CG  . ARG C  1 254 ? 38.045  22.897  10.801  1.00 20.52 ?  278  ARG C CG  1 
ATOM   6461  C  CD  . ARG C  1 254 ? 38.914  22.906  9.558   1.00 20.11 ?  278  ARG C CD  1 
ATOM   6462  N  NE  . ARG C  1 254 ? 39.188  21.539  9.121   1.00 20.44 ?  278  ARG C NE  1 
ATOM   6463  C  CZ  . ARG C  1 254 ? 38.669  20.972  8.034   1.00 20.30 ?  278  ARG C CZ  1 
ATOM   6464  N  NH1 . ARG C  1 254 ? 37.853  21.657  7.234   1.00 18.82 ?  278  ARG C NH1 1 
ATOM   6465  N  NH2 . ARG C  1 254 ? 38.974  19.713  7.741   1.00 19.53 ?  278  ARG C NH2 1 
ATOM   6466  N  N   . LYS C  1 255 ? 35.296  26.312  12.685  1.00 20.42 ?  279  LYS C N   1 
ATOM   6467  C  CA  . LYS C  1 255 ? 35.039  27.692  13.092  1.00 20.38 ?  279  LYS C CA  1 
ATOM   6468  C  C   . LYS C  1 255 ? 34.762  27.776  14.597  1.00 20.20 ?  279  LYS C C   1 
ATOM   6469  O  O   . LYS C  1 255 ? 34.128  26.882  15.156  1.00 20.51 ?  279  LYS C O   1 
ATOM   6470  C  CB  . LYS C  1 255 ? 33.884  28.286  12.279  1.00 20.41 ?  279  LYS C CB  1 
ATOM   6471  C  CG  . LYS C  1 255 ? 34.181  28.397  10.787  1.00 20.80 ?  279  LYS C CG  1 
ATOM   6472  C  CD  . LYS C  1 255 ? 33.017  28.990  10.008  1.00 20.32 ?  279  LYS C CD  1 
ATOM   6473  C  CE  . LYS C  1 255 ? 33.339  29.047  8.517   1.00 20.91 ?  279  LYS C CE  1 
ATOM   6474  N  NZ  . LYS C  1 255 ? 32.262  29.697  7.710   1.00 20.71 ?  279  LYS C NZ  1 
ATOM   6475  N  N   . PRO C  1 256 ? 35.253  28.841  15.262  1.00 20.15 ?  280  PRO C N   1 
ATOM   6476  C  CA  . PRO C  1 256 ? 35.069  28.992  16.715  1.00 19.99 ?  280  PRO C CA  1 
ATOM   6477  C  C   . PRO C  1 256 ? 33.606  28.935  17.148  1.00 19.79 ?  280  PRO C C   1 
ATOM   6478  O  O   . PRO C  1 256 ? 33.304  28.451  18.231  1.00 19.79 ?  280  PRO C O   1 
ATOM   6479  C  CB  . PRO C  1 256 ? 35.649  30.380  16.992  1.00 19.94 ?  280  PRO C CB  1 
ATOM   6480  C  CG  . PRO C  1 256 ? 36.678  30.557  15.934  1.00 19.97 ?  280  PRO C CG  1 
ATOM   6481  C  CD  . PRO C  1 256 ? 36.094  29.921  14.710  1.00 19.95 ?  280  PRO C CD  1 
ATOM   6482  N  N   . GLU C  1 257 ? 32.718  29.422  16.287  1.00 20.01 ?  281  GLU C N   1 
ATOM   6483  C  CA  . GLU C  1 257 ? 31.278  29.435  16.530  1.00 20.12 ?  281  GLU C CA  1 
ATOM   6484  C  C   . GLU C  1 257 ? 30.671  28.050  16.794  1.00 19.94 ?  281  GLU C C   1 
ATOM   6485  O  O   . GLU C  1 257 ? 29.674  27.936  17.512  1.00 19.97 ?  281  GLU C O   1 
ATOM   6486  C  CB  . GLU C  1 257 ? 30.550  30.105  15.360  1.00 20.16 ?  281  GLU C CB  1 
ATOM   6487  C  CG  . GLU C  1 257 ? 30.732  31.633  15.263  1.00 20.65 ?  281  GLU C CG  1 
ATOM   6488  C  CD  . GLU C  1 257 ? 32.032  32.044  14.587  1.00 21.85 ?  281  GLU C CD  1 
ATOM   6489  O  OE1 . GLU C  1 257 ? 32.715  31.177  13.997  1.00 22.36 ?  281  GLU C OE1 1 
ATOM   6490  O  OE2 . GLU C  1 257 ? 32.370  33.244  14.642  1.00 22.71 -1 281  GLU C OE2 1 
ATOM   6491  N  N   . ALA C  1 258 ? 31.276  27.008  16.227  1.00 19.65 ?  282  ALA C N   1 
ATOM   6492  C  CA  . ALA C  1 258 ? 30.768  25.641  16.396  1.00 19.44 ?  282  ALA C CA  1 
ATOM   6493  C  C   . ALA C  1 258 ? 30.816  25.152  17.847  1.00 19.26 ?  282  ALA C C   1 
ATOM   6494  O  O   . ALA C  1 258 ? 30.018  24.292  18.234  1.00 19.17 ?  282  ALA C O   1 
ATOM   6495  C  CB  . ALA C  1 258 ? 31.501  24.674  15.475  1.00 19.35 ?  282  ALA C CB  1 
ATOM   6496  N  N   . CYS C  1 259 ? 31.737  25.715  18.636  1.00 19.06 ?  283  CYS C N   1 
ATOM   6497  C  CA  . CYS C  1 259 ? 31.926  25.346  20.048  1.00 19.02 ?  283  CYS C CA  1 
ATOM   6498  C  C   . CYS C  1 259 ? 31.137  26.237  21.015  1.00 18.94 ?  283  CYS C C   1 
ATOM   6499  O  O   . CYS C  1 259 ? 31.047  25.938  22.206  1.00 18.94 ?  283  CYS C O   1 
ATOM   6500  C  CB  . CYS C  1 259 ? 33.411  25.447  20.440  1.00 18.97 ?  283  CYS C CB  1 
ATOM   6501  S  SG  . CYS C  1 259 ? 34.626  24.833  19.249  1.00 19.55 ?  283  CYS C SG  1 
ATOM   6502  N  N   . ALA C  1 260 ? 30.581  27.328  20.498  1.00 18.76 ?  284  ALA C N   1 
ATOM   6503  C  CA  . ALA C  1 260 ? 30.085  28.427  21.332  1.00 18.71 ?  284  ALA C CA  1 
ATOM   6504  C  C   . ALA C  1 260 ? 28.805  28.143  22.112  1.00 18.64 ?  284  ALA C C   1 
ATOM   6505  O  O   . ALA C  1 260 ? 28.644  28.625  23.236  1.00 18.49 ?  284  ALA C O   1 
ATOM   6506  C  CB  . ALA C  1 260 ? 29.910  29.680  20.494  1.00 18.52 ?  284  ALA C CB  1 
ATOM   6507  N  N   . THR C  1 261 ? 27.895  27.376  21.518  1.00 18.53 ?  285  THR C N   1 
ATOM   6508  C  CA  . THR C  1 261 ? 26.619  27.079  22.167  1.00 18.70 ?  285  THR C CA  1 
ATOM   6509  C  C   . THR C  1 261 ? 26.845  26.360  23.498  1.00 18.59 ?  285  THR C C   1 
ATOM   6510  O  O   . THR C  1 261 ? 26.149  26.619  24.479  1.00 18.98 ?  285  THR C O   1 
ATOM   6511  C  CB  . THR C  1 261 ? 25.672  26.280  21.238  1.00 18.62 ?  285  THR C CB  1 
ATOM   6512  O  OG1 . THR C  1 261 ? 25.490  27.005  20.015  1.00 18.43 ?  285  THR C OG1 1 
ATOM   6513  C  CG2 . THR C  1 261 ? 24.311  26.062  21.894  1.00 18.52 ?  285  THR C CG2 1 
ATOM   6514  N  N   . CYS C  1 262 ? 27.849  25.493  23.537  1.00 18.44 ?  286  CYS C N   1 
ATOM   6515  C  CA  . CYS C  1 262 ? 28.141  24.733  24.746  1.00 18.30 ?  286  CYS C CA  1 
ATOM   6516  C  C   . CYS C  1 262 ? 29.221  25.362  25.616  1.00 18.24 ?  286  CYS C C   1 
ATOM   6517  O  O   . CYS C  1 262 ? 29.079  25.406  26.833  1.00 18.20 ?  286  CYS C O   1 
ATOM   6518  C  CB  . CYS C  1 262 ? 28.536  23.309  24.391  1.00 18.08 ?  286  CYS C CB  1 
ATOM   6519  S  SG  . CYS C  1 262 ? 27.345  22.466  23.362  1.00 17.68 ?  286  CYS C SG  1 
ATOM   6520  N  N   . HIS C  1 263 ? 30.294  25.844  24.992  1.00 18.21 ?  287  HIS C N   1 
ATOM   6521  C  CA  . HIS C  1 263 ? 31.435  26.370  25.739  1.00 18.57 ?  287  HIS C CA  1 
ATOM   6522  C  C   . HIS C  1 263 ? 31.307  27.874  26.000  1.00 18.65 ?  287  HIS C C   1 
ATOM   6523  O  O   . HIS C  1 263 ? 32.128  28.680  25.557  1.00 18.51 ?  287  HIS C O   1 
ATOM   6524  C  CB  . HIS C  1 263 ? 32.760  26.004  25.055  1.00 18.46 ?  287  HIS C CB  1 
ATOM   6525  C  CG  . HIS C  1 263 ? 33.126  24.553  25.175  1.00 18.77 ?  287  HIS C CG  1 
ATOM   6526  N  ND1 . HIS C  1 263 ? 33.682  24.018  26.318  1.00 19.35 ?  287  HIS C ND1 1 
ATOM   6527  C  CD2 . HIS C  1 263 ? 33.017  23.528  24.296  1.00 18.86 ?  287  HIS C CD2 1 
ATOM   6528  C  CE1 . HIS C  1 263 ? 33.895  22.725  26.140  1.00 19.31 ?  287  HIS C CE1 1 
ATOM   6529  N  NE2 . HIS C  1 263 ? 33.501  22.400  24.921  1.00 19.58 ?  287  HIS C NE2 1 
ATOM   6530  N  N   . SER C  1 264 ? 30.253  28.232  26.729  1.00 18.90 ?  288  SER C N   1 
ATOM   6531  C  CA  . SER C  1 264 ? 29.968  29.619  27.095  1.00 19.18 ?  288  SER C CA  1 
ATOM   6532  C  C   . SER C  1 264 ? 29.218  29.653  28.428  1.00 19.29 ?  288  SER C C   1 
ATOM   6533  O  O   . SER C  1 264 ? 28.809  28.607  28.926  1.00 19.33 ?  288  SER C O   1 
ATOM   6534  C  CB  . SER C  1 264 ? 29.141  30.291  25.999  1.00 19.24 ?  288  SER C CB  1 
ATOM   6535  O  OG  . SER C  1 264 ? 27.959  29.554  25.736  1.00 18.98 ?  288  SER C OG  1 
ATOM   6536  N  N   . GLY C  1 265 ? 29.062  30.842  29.010  1.00 19.61 ?  289  GLY C N   1 
ATOM   6537  C  CA  . GLY C  1 265 ? 28.252  31.015  30.220  1.00 19.82 ?  289  GLY C CA  1 
ATOM   6538  C  C   . GLY C  1 265 ? 28.988  31.280  31.526  1.00 20.11 ?  289  GLY C C   1 
ATOM   6539  O  O   . GLY C  1 265 ? 30.222  31.355  31.549  1.00 20.03 ?  289  GLY C O   1 
ATOM   6540  N  N   . VAL C  1 266 ? 28.217  31.385  32.616  1.00 20.23 ?  290  VAL C N   1 
ATOM   6541  C  CA  . VAL C  1 266 ? 28.722  31.840  33.921  1.00 20.73 ?  290  VAL C CA  1 
ATOM   6542  C  C   . VAL C  1 266 ? 29.833  31.016  34.548  1.00 20.73 ?  290  VAL C C   1 
ATOM   6543  O  O   . VAL C  1 266 ? 30.561  31.533  35.380  1.00 20.88 ?  290  VAL C O   1 
ATOM   6544  C  CB  . VAL C  1 266 ? 27.614  31.951  35.026  1.00 20.92 ?  290  VAL C CB  1 
ATOM   6545  C  CG1 . VAL C  1 266 ? 26.945  33.308  35.007  1.00 21.47 ?  290  VAL C CG1 1 
ATOM   6546  C  CG2 . VAL C  1 266 ? 26.622  30.799  34.960  1.00 20.68 ?  290  VAL C CG2 1 
ATOM   6547  N  N   . ASP C  1 267 ? 29.939  29.740  34.191  1.00 20.78 ?  291  ASP C N   1 
ATOM   6548  C  CA  . ASP C  1 267 ? 30.907  28.860  34.850  1.00 21.01 ?  291  ASP C CA  1 
ATOM   6549  C  C   . ASP C  1 267 ? 31.996  28.334  33.906  1.00 20.82 ?  291  ASP C C   1 
ATOM   6550  O  O   . ASP C  1 267 ? 32.809  27.484  34.287  1.00 20.58 ?  291  ASP C O   1 
ATOM   6551  C  CB  . ASP C  1 267 ? 30.189  27.721  35.595  1.00 21.21 ?  291  ASP C CB  1 
ATOM   6552  C  CG  . ASP C  1 267 ? 29.449  26.781  34.666  1.00 22.42 ?  291  ASP C CG  1 
ATOM   6553  O  OD1 . ASP C  1 267 ? 28.953  27.237  33.611  1.00 23.26 ?  291  ASP C OD1 1 
ATOM   6554  O  OD2 . ASP C  1 267 ? 29.358  25.575  35.003  1.00 24.14 -1 291  ASP C OD2 1 
ATOM   6555  N  N   . HIS C  1 268 ? 31.996  28.858  32.681  1.00 20.52 ?  292  HIS C N   1 
ATOM   6556  C  CA  . HIS C  1 268 ? 33.005  28.564  31.663  1.00 20.39 ?  292  HIS C CA  1 
ATOM   6557  C  C   . HIS C  1 268 ? 32.745  29.412  30.415  1.00 20.18 ?  292  HIS C C   1 
ATOM   6558  O  O   . HIS C  1 268 ? 32.148  28.941  29.446  1.00 19.97 ?  292  HIS C O   1 
ATOM   6559  C  CB  . HIS C  1 268 ? 33.063  27.061  31.315  1.00 20.45 ?  292  HIS C CB  1 
ATOM   6560  C  CG  . HIS C  1 268 ? 31.722  26.404  31.178  1.00 20.93 ?  292  HIS C CG  1 
ATOM   6561  N  ND1 . HIS C  1 268 ? 30.831  26.723  30.176  1.00 20.98 ?  292  HIS C ND1 1 
ATOM   6562  C  CD2 . HIS C  1 268 ? 31.132  25.424  31.905  1.00 21.84 ?  292  HIS C CD2 1 
ATOM   6563  C  CE1 . HIS C  1 268 ? 29.746  25.979  30.299  1.00 21.17 ?  292  HIS C CE1 1 
ATOM   6564  N  NE2 . HIS C  1 268 ? 29.899  25.187  31.344  1.00 21.43 ?  292  HIS C NE2 1 
ATOM   6565  N  N   . ASN C  1 269 ? 33.194  30.665  30.450  1.00 20.09 ?  293  ASN C N   1 
ATOM   6566  C  CA  . ASN C  1 269 ? 32.909  31.624  29.376  1.00 19.97 ?  293  ASN C CA  1 
ATOM   6567  C  C   . ASN C  1 269 ? 33.959  31.619  28.260  1.00 20.02 ?  293  ASN C C   1 
ATOM   6568  O  O   . ASN C  1 269 ? 34.470  32.672  27.864  1.00 19.99 ?  293  ASN C O   1 
ATOM   6569  C  CB  . ASN C  1 269 ? 32.700  33.042  29.945  1.00 19.85 ?  293  ASN C CB  1 
ATOM   6570  C  CG  . ASN C  1 269 ? 33.965  33.630  30.567  1.00 19.93 ?  293  ASN C CG  1 
ATOM   6571  O  OD1 . ASN C  1 269 ? 34.858  32.903  31.010  1.00 19.60 ?  293  ASN C OD1 1 
ATOM   6572  N  ND2 . ASN C  1 269 ? 34.043  34.961  30.600  1.00 19.56 ?  293  ASN C ND2 1 
ATOM   6573  N  N   . ASN C  1 270 ? 34.266  30.433  27.747  1.00 20.05 ?  294  ASN C N   1 
ATOM   6574  C  CA  . ASN C  1 270 ? 35.340  30.286  26.764  1.00 20.42 ?  294  ASN C CA  1 
ATOM   6575  C  C   . ASN C  1 270 ? 35.092  31.087  25.492  1.00 20.35 ?  294  ASN C C   1 
ATOM   6576  O  O   . ASN C  1 270 ? 35.968  31.823  25.050  1.00 20.44 ?  294  ASN C O   1 
ATOM   6577  C  CB  . ASN C  1 270 ? 35.619  28.812  26.471  1.00 20.24 ?  294  ASN C CB  1 
ATOM   6578  C  CG  . ASN C  1 270 ? 35.847  28.014  27.734  1.00 20.71 ?  294  ASN C CG  1 
ATOM   6579  O  OD1 . ASN C  1 270 ? 34.923  27.812  28.528  1.00 21.44 ?  294  ASN C OD1 1 
ATOM   6580  N  ND2 . ASN C  1 270 ? 37.085  27.571  27.942  1.00 20.16 ?  294  ASN C ND2 1 
ATOM   6581  N  N   . TRP C  1 271 ? 33.886  30.962  24.937  1.00 20.51 ?  295  TRP C N   1 
ATOM   6582  C  CA  . TRP C  1 271 ? 33.472  31.751  23.777  1.00 20.67 ?  295  TRP C CA  1 
ATOM   6583  C  C   . TRP C  1 271 ? 33.682  33.245  24.009  1.00 20.71 ?  295  TRP C C   1 
ATOM   6584  O  O   . TRP C  1 271 ? 34.328  33.917  23.206  1.00 20.68 ?  295  TRP C O   1 
ATOM   6585  C  CB  . TRP C  1 271 ? 32.005  31.465  23.428  1.00 20.72 ?  295  TRP C CB  1 
ATOM   6586  C  CG  . TRP C  1 271 ? 31.419  32.397  22.398  1.00 20.84 ?  295  TRP C CG  1 
ATOM   6587  C  CD1 . TRP C  1 271 ? 30.442  33.333  22.601  1.00 20.87 ?  295  TRP C CD1 1 
ATOM   6588  C  CD2 . TRP C  1 271 ? 31.775  32.485  21.009  1.00 21.26 ?  295  TRP C CD2 1 
ATOM   6589  N  NE1 . TRP C  1 271 ? 30.163  33.991  21.427  1.00 20.75 ?  295  TRP C NE1 1 
ATOM   6590  C  CE2 . TRP C  1 271 ? 30.967  33.495  20.435  1.00 21.24 ?  295  TRP C CE2 1 
ATOM   6591  C  CE3 . TRP C  1 271 ? 32.700  31.812  20.195  1.00 21.35 ?  295  TRP C CE3 1 
ATOM   6592  C  CZ2 . TRP C  1 271 ? 31.055  33.850  19.082  1.00 21.78 ?  295  TRP C CZ2 1 
ATOM   6593  C  CZ3 . TRP C  1 271 ? 32.782  32.161  18.847  1.00 21.81 ?  295  TRP C CZ3 1 
ATOM   6594  C  CH2 . TRP C  1 271 ? 31.962  33.173  18.307  1.00 21.73 ?  295  TRP C CH2 1 
ATOM   6595  N  N   . GLU C  1 272 ? 33.135  33.747  25.115  1.00 20.81 ?  296  GLU C N   1 
ATOM   6596  C  CA  . GLU C  1 272 ? 33.225  35.158  25.468  1.00 20.90 ?  296  GLU C CA  1 
ATOM   6597  C  C   . GLU C  1 272 ? 34.684  35.614  25.595  1.00 20.88 ?  296  GLU C C   1 
ATOM   6598  O  O   . GLU C  1 272 ? 35.068  36.629  25.016  1.00 20.69 ?  296  GLU C O   1 
ATOM   6599  C  CB  . GLU C  1 272 ? 32.447  35.443  26.761  1.00 21.17 ?  296  GLU C CB  1 
ATOM   6600  C  CG  . GLU C  1 272 ? 30.944  35.085  26.702  1.00 21.46 ?  296  GLU C CG  1 
ATOM   6601  C  CD  . GLU C  1 272 ? 30.645  33.640  27.103  1.00 22.40 ?  296  GLU C CD  1 
ATOM   6602  O  OE1 . GLU C  1 272 ? 31.397  32.719  26.713  1.00 22.00 ?  296  GLU C OE1 1 
ATOM   6603  O  OE2 . GLU C  1 272 ? 29.641  33.421  27.814  1.00 23.42 -1 296  GLU C OE2 1 
ATOM   6604  N  N   . ALA C  1 273 ? 35.486  34.844  26.330  1.00 20.72 ?  297  ALA C N   1 
ATOM   6605  C  CA  . ALA C  1 273 ? 36.897  35.159  26.548  1.00 20.73 ?  297  ALA C CA  1 
ATOM   6606  C  C   . ALA C  1 273 ? 37.707  35.095  25.252  1.00 20.72 ?  297  ALA C C   1 
ATOM   6607  O  O   . ALA C  1 273 ? 38.433  36.031  24.923  1.00 20.47 ?  297  ALA C O   1 
ATOM   6608  C  CB  . ALA C  1 273 ? 37.496  34.229  27.600  1.00 20.78 ?  297  ALA C CB  1 
ATOM   6609  N  N   . TYR C  1 274 ? 37.568  33.994  24.517  1.00 20.73 ?  298  TYR C N   1 
ATOM   6610  C  CA  . TYR C  1 274 ? 38.299  33.828  23.268  1.00 20.70 ?  298  TYR C CA  1 
ATOM   6611  C  C   . TYR C  1 274 ? 37.993  34.934  22.258  1.00 20.63 ?  298  TYR C C   1 
ATOM   6612  O  O   . TYR C  1 274 ? 38.919  35.559  21.739  1.00 20.78 ?  298  TYR C O   1 
ATOM   6613  C  CB  . TYR C  1 274 ? 38.069  32.446  22.646  1.00 20.67 ?  298  TYR C CB  1 
ATOM   6614  C  CG  . TYR C  1 274 ? 38.535  32.375  21.206  1.00 20.47 ?  298  TYR C CG  1 
ATOM   6615  C  CD1 . TYR C  1 274 ? 39.888  32.246  20.899  1.00 19.91 ?  298  TYR C CD1 1 
ATOM   6616  C  CD2 . TYR C  1 274 ? 37.623  32.468  20.151  1.00 20.01 ?  298  TYR C CD2 1 
ATOM   6617  C  CE1 . TYR C  1 274 ? 40.325  32.201  19.586  1.00 19.67 ?  298  TYR C CE1 1 
ATOM   6618  C  CE2 . TYR C  1 274 ? 38.052  32.418  18.827  1.00 19.99 ?  298  TYR C CE2 1 
ATOM   6619  C  CZ  . TYR C  1 274 ? 39.403  32.283  18.554  1.00 19.68 ?  298  TYR C CZ  1 
ATOM   6620  O  OH  . TYR C  1 274 ? 39.840  32.236  17.253  1.00 18.91 ?  298  TYR C OH  1 
ATOM   6621  N  N   . THR C  1 275 ? 36.710  35.174  21.983  1.00 20.43 ?  299  THR C N   1 
ATOM   6622  C  CA  . THR C  1 275 ? 36.319  36.177  20.984  1.00 20.58 ?  299  THR C CA  1 
ATOM   6623  C  C   . THR C  1 275 ? 36.846  37.566  21.305  1.00 20.57 ?  299  THR C C   1 
ATOM   6624  O  O   . THR C  1 275 ? 37.177  38.323  20.394  1.00 20.55 ?  299  THR C O   1 
ATOM   6625  C  CB  . THR C  1 275 ? 34.787  36.287  20.792  1.00 20.73 ?  299  THR C CB  1 
ATOM   6626  O  OG1 . THR C  1 275 ? 34.150  36.510  22.060  1.00 21.03 ?  299  THR C OG1 1 
ATOM   6627  C  CG2 . THR C  1 275 ? 34.245  35.042  20.160  1.00 20.63 ?  299  THR C CG2 1 
ATOM   6628  N  N   . MET C  1 276 ? 36.917  37.885  22.597  1.00 20.42 ?  300  MET C N   1 
ATOM   6629  C  CA  . MET C  1 276 ? 37.348  39.202  23.056  1.00 20.47 ?  300  MET C CA  1 
ATOM   6630  C  C   . MET C  1 276 ? 38.864  39.378  23.050  1.00 20.58 ?  300  MET C C   1 
ATOM   6631  O  O   . MET C  1 276 ? 39.348  40.500  23.060  1.00 20.51 ?  300  MET C O   1 
ATOM   6632  C  CB  . MET C  1 276 ? 36.787  39.507  24.453  1.00 20.34 ?  300  MET C CB  1 
ATOM   6633  C  CG  . MET C  1 276 ? 35.288  39.818  24.484  1.00 19.88 ?  300  MET C CG  1 
ATOM   6634  S  SD  . MET C  1 276 ? 34.733  40.987  23.224  1.00 18.16 ?  300  MET C SD  1 
ATOM   6635  C  CE  . MET C  1 276 ? 35.638  42.466  23.687  1.00 19.44 ?  300  MET C CE  1 
ATOM   6636  N  N   . SER C  1 277 ? 39.605  38.270  23.043  1.00 20.85 ?  301  SER C N   1 
ATOM   6637  C  CA  . SER C  1 277 ? 41.065  38.314  22.948  1.00 20.97 ?  301  SER C CA  1 
ATOM   6638  C  C   . SER C  1 277 ? 41.499  38.785  21.562  1.00 20.94 ?  301  SER C C   1 
ATOM   6639  O  O   . SER C  1 277 ? 40.706  38.757  20.620  1.00 20.98 ?  301  SER C O   1 
ATOM   6640  C  CB  . SER C  1 277 ? 41.656  36.931  23.216  1.00 20.95 ?  301  SER C CB  1 
ATOM   6641  O  OG  . SER C  1 277 ? 41.470  36.069  22.105  1.00 21.58 ?  301  SER C OG  1 
ATOM   6642  N  N   . LYS C  1 278 ? 42.755  39.210  21.440  1.00 21.08 ?  302  LYS C N   1 
ATOM   6643  C  CA  . LYS C  1 278 ? 43.348  39.481  20.128  1.00 21.27 ?  302  LYS C CA  1 
ATOM   6644  C  C   . LYS C  1 278 ? 43.194  38.288  19.200  1.00 20.95 ?  302  LYS C C   1 
ATOM   6645  O  O   . LYS C  1 278 ? 42.786  38.446  18.051  1.00 21.27 ?  302  LYS C O   1 
ATOM   6646  C  CB  . LYS C  1 278 ? 44.833  39.839  20.243  1.00 21.14 ?  302  LYS C CB  1 
ATOM   6647  C  CG  . LYS C  1 278 ? 45.124  41.313  20.167  1.00 22.57 ?  302  LYS C CG  1 
ATOM   6648  C  CD  . LYS C  1 278 ? 44.595  41.933  18.878  1.00 22.74 ?  302  LYS C CD  1 
ATOM   6649  C  CE  . LYS C  1 278 ? 44.440  43.422  19.066  1.00 22.87 ?  302  LYS C CE  1 
ATOM   6650  N  NZ  . LYS C  1 278 ? 43.569  44.049  18.047  1.00 22.46 ?  302  LYS C NZ  1 
ATOM   6651  N  N   . HIS C  1 279 ? 43.527  37.100  19.705  1.00 20.74 ?  303  HIS C N   1 
ATOM   6652  C  CA  . HIS C  1 279 ? 43.379  35.856  18.944  1.00 20.68 ?  303  HIS C CA  1 
ATOM   6653  C  C   . HIS C  1 279 ? 42.007  35.770  18.255  1.00 20.66 ?  303  HIS C C   1 
ATOM   6654  O  O   . HIS C  1 279 ? 41.925  35.554  17.041  1.00 21.06 ?  303  HIS C O   1 
ATOM   6655  C  CB  . HIS C  1 279 ? 43.598  34.630  19.849  1.00 20.48 ?  303  HIS C CB  1 
ATOM   6656  C  CG  . HIS C  1 279 ? 45.019  34.432  20.292  1.00 20.38 ?  303  HIS C CG  1 
ATOM   6657  N  ND1 . HIS C  1 279 ? 45.346  33.783  21.464  1.00 20.70 ?  303  HIS C ND1 1 
ATOM   6658  C  CD2 . HIS C  1 279 ? 46.196  34.791  19.722  1.00 19.65 ?  303  HIS C CD2 1 
ATOM   6659  C  CE1 . HIS C  1 279 ? 46.661  33.750  21.596  1.00 20.72 ?  303  HIS C CE1 1 
ATOM   6660  N  NE2 . HIS C  1 279 ? 47.202  34.354  20.550  1.00 20.63 ?  303  HIS C NE2 1 
ATOM   6661  N  N   . GLY C  1 280 ? 40.942  35.961  19.036  1.00 20.37 ?  304  GLY C N   1 
ATOM   6662  C  CA  . GLY C  1 280 ? 39.570  35.827  18.551  1.00 19.93 ?  304  GLY C CA  1 
ATOM   6663  C  C   . GLY C  1 280 ? 39.082  36.997  17.720  1.00 19.65 ?  304  GLY C C   1 
ATOM   6664  O  O   . GLY C  1 280 ? 38.309  36.815  16.785  1.00 19.46 ?  304  GLY C O   1 
ATOM   6665  N  N   . LYS C  1 281 ? 39.519  38.203  18.070  1.00 19.59 ?  305  LYS C N   1 
ATOM   6666  C  CA  . LYS C  1 281 ? 39.183  39.393  17.289  1.00 19.57 ?  305  LYS C CA  1 
ATOM   6667  C  C   . LYS C  1 281 ? 39.827  39.334  15.896  1.00 19.78 ?  305  LYS C C   1 
ATOM   6668  O  O   . LYS C  1 281 ? 39.231  39.781  14.909  1.00 19.67 ?  305  LYS C O   1 
ATOM   6669  C  CB  . LYS C  1 281 ? 39.560  40.674  18.046  1.00 19.37 ?  305  LYS C CB  1 
ATOM   6670  C  CG  . LYS C  1 281 ? 38.574  41.044  19.169  1.00 18.87 ?  305  LYS C CG  1 
ATOM   6671  C  CD  . LYS C  1 281 ? 37.275  41.629  18.599  1.00 18.90 ?  305  LYS C CD  1 
ATOM   6672  C  CE  . LYS C  1 281 ? 36.094  41.483  19.543  1.00 17.23 ?  305  LYS C CE  1 
ATOM   6673  N  NZ  . LYS C  1 281 ? 35.441  40.157  19.432  1.00 17.57 ?  305  LYS C NZ  1 
ATOM   6674  N  N   . LEU C  1 282 ? 41.026  38.757  15.823  1.00 19.89 ?  306  LEU C N   1 
ATOM   6675  C  CA  . LEU C  1 282 ? 41.691  38.515  14.542  1.00 20.43 ?  306  LEU C CA  1 
ATOM   6676  C  C   . LEU C  1 282 ? 40.970  37.465  13.709  1.00 20.54 ?  306  LEU C C   1 
ATOM   6677  O  O   . LEU C  1 282 ? 40.851  37.612  12.494  1.00 20.56 ?  306  LEU C O   1 
ATOM   6678  C  CB  . LEU C  1 282 ? 43.155  38.117  14.744  1.00 20.31 ?  306  LEU C CB  1 
ATOM   6679  C  CG  . LEU C  1 282 ? 44.131  39.271  14.989  1.00 20.80 ?  306  LEU C CG  1 
ATOM   6680  C  CD1 . LEU C  1 282 ? 45.440  38.737  15.529  1.00 21.05 ?  306  LEU C CD1 1 
ATOM   6681  C  CD2 . LEU C  1 282 ? 44.355  40.063  13.713  1.00 20.38 ?  306  LEU C CD2 1 
ATOM   6682  N  N   . ALA C  1 283 ? 40.492  36.409  14.366  1.00 20.88 ?  307  ALA C N   1 
ATOM   6683  C  CA  . ALA C  1 283 ? 39.716  35.369  13.693  1.00 21.31 ?  307  ALA C CA  1 
ATOM   6684  C  C   . ALA C  1 283 ? 38.432  35.934  13.085  1.00 21.70 ?  307  ALA C C   1 
ATOM   6685  O  O   . ALA C  1 283 ? 38.024  35.519  11.997  1.00 21.55 ?  307  ALA C O   1 
ATOM   6686  C  CB  . ALA C  1 283 ? 39.409  34.215  14.641  1.00 20.98 ?  307  ALA C CB  1 
ATOM   6687  N  N   . GLU C  1 284 ? 37.806  36.877  13.791  1.00 22.27 ?  308  GLU C N   1 
ATOM   6688  C  CA  . GLU C  1 284 ? 36.615  37.572  13.289  1.00 23.09 ?  308  GLU C CA  1 
ATOM   6689  C  C   . GLU C  1 284 ? 36.941  38.476  12.093  1.00 23.50 ?  308  GLU C C   1 
ATOM   6690  O  O   . GLU C  1 284 ? 36.234  38.458  11.082  1.00 23.48 ?  308  GLU C O   1 
ATOM   6691  C  CB  . GLU C  1 284 ? 35.933  38.371  14.409  1.00 23.01 ?  308  GLU C CB  1 
ATOM   6692  C  CG  . GLU C  1 284 ? 35.220  37.493  15.428  1.00 23.71 ?  308  GLU C CG  1 
ATOM   6693  C  CD  . GLU C  1 284 ? 34.774  38.227  16.690  1.00 24.43 ?  308  GLU C CD  1 
ATOM   6694  O  OE1 . GLU C  1 284 ? 34.899  39.468  16.778  1.00 24.46 ?  308  GLU C OE1 1 
ATOM   6695  O  OE2 . GLU C  1 284 ? 34.283  37.541  17.607  1.00 26.24 -1 308  GLU C OE2 1 
ATOM   6696  N  N   . MET C  1 285 ? 38.021  39.245  12.209  1.00 24.14 ?  309  MET C N   1 
ATOM   6697  C  CA  . MET C  1 285 ? 38.442  40.159  11.142  1.00 24.87 ?  309  MET C CA  1 
ATOM   6698  C  C   . MET C  1 285 ? 38.937  39.442  9.888   1.00 25.62 ?  309  MET C C   1 
ATOM   6699  O  O   . MET C  1 285 ? 38.767  39.943  8.777   1.00 25.54 ?  309  MET C O   1 
ATOM   6700  C  CB  . MET C  1 285 ? 39.523  41.120  11.644  1.00 24.67 ?  309  MET C CB  1 
ATOM   6701  C  CG  . MET C  1 285 ? 39.009  42.194  12.582  1.00 24.11 ?  309  MET C CG  1 
ATOM   6702  S  SD  . MET C  1 285 ? 40.260  43.401  13.073  1.00 23.65 ?  309  MET C SD  1 
ATOM   6703  C  CE  . MET C  1 285 ? 41.124  42.536  14.384  1.00 22.99 ?  309  MET C CE  1 
ATOM   6704  N  N   . ASN C  1 286 ? 39.544  38.272  10.070  1.00 26.61 ?  310  ASN C N   1 
ATOM   6705  C  CA  . ASN C  1 286 ? 40.218  37.588  8.970   1.00 27.96 ?  310  ASN C CA  1 
ATOM   6706  C  C   . ASN C  1 286 ? 39.480  36.380  8.403   1.00 28.64 ?  310  ASN C C   1 
ATOM   6707  O  O   . ASN C  1 286 ? 39.975  35.744  7.472   1.00 28.72 ?  310  ASN C O   1 
ATOM   6708  C  CB  . ASN C  1 286 ? 41.647  37.195  9.374   1.00 27.96 ?  310  ASN C CB  1 
ATOM   6709  C  CG  . ASN C  1 286 ? 42.530  38.401  9.662   1.00 28.87 ?  310  ASN C CG  1 
ATOM   6710  O  OD1 . ASN C  1 286 ? 42.446  39.423  8.987   1.00 30.39 ?  310  ASN C OD1 1 
ATOM   6711  N  ND2 . ASN C  1 286 ? 43.392  38.277  10.664  1.00 30.36 ?  310  ASN C ND2 1 
ATOM   6712  N  N   . ARG C  1 287 ? 38.303  36.066  8.945   1.00 29.55 ?  311  ARG C N   1 
ATOM   6713  C  CA  . ARG C  1 287 ? 37.586  34.843  8.548   1.00 30.81 ?  311  ARG C CA  1 
ATOM   6714  C  C   . ARG C  1 287 ? 37.342  34.694  7.040   1.00 31.26 ?  311  ARG C C   1 
ATOM   6715  O  O   . ARG C  1 287 ? 37.305  33.571  6.524   1.00 31.60 ?  311  ARG C O   1 
ATOM   6716  C  CB  . ARG C  1 287 ? 36.284  34.648  9.343   1.00 30.94 ?  311  ARG C CB  1 
ATOM   6717  C  CG  . ARG C  1 287 ? 35.237  35.744  9.207   1.00 31.97 ?  311  ARG C CG  1 
ATOM   6718  C  CD  . ARG C  1 287 ? 34.065  35.449  10.138  1.00 34.08 ?  311  ARG C CD  1 
ATOM   6719  N  NE  . ARG C  1 287 ? 33.546  36.676  10.736  1.00 35.97 ?  311  ARG C NE  1 
ATOM   6720  C  CZ  . ARG C  1 287 ? 33.056  36.771  11.968  1.00 36.32 ?  311  ARG C CZ  1 
ATOM   6721  N  NH1 . ARG C  1 287 ? 33.002  35.709  12.763  1.00 36.64 ?  311  ARG C NH1 1 
ATOM   6722  N  NH2 . ARG C  1 287 ? 32.622  37.943  12.409  1.00 36.89 ?  311  ARG C NH2 1 
ATOM   6723  N  N   . ASP C  1 288 ? 37.197  35.822  6.347   1.00 31.81 ?  312  ASP C N   1 
ATOM   6724  C  CA  . ASP C  1 288 ? 37.004  35.837  4.893   1.00 32.31 ?  312  ASP C CA  1 
ATOM   6725  C  C   . ASP C  1 288 ? 38.283  35.627  4.093   1.00 32.01 ?  312  ASP C C   1 
ATOM   6726  O  O   . ASP C  1 288 ? 38.238  35.403  2.880   1.00 32.27 ?  312  ASP C O   1 
ATOM   6727  C  CB  . ASP C  1 288 ? 36.352  37.147  4.461   1.00 32.79 ?  312  ASP C CB  1 
ATOM   6728  C  CG  . ASP C  1 288 ? 34.858  37.027  4.321   1.00 35.05 ?  312  ASP C CG  1 
ATOM   6729  O  OD1 . ASP C  1 288 ? 34.224  36.351  5.166   1.00 35.60 ?  312  ASP C OD1 1 
ATOM   6730  O  OD2 . ASP C  1 288 ? 34.310  37.607  3.356   1.00 37.63 -1 312  ASP C OD2 1 
ATOM   6731  N  N   . LYS C  1 289 ? 39.420  35.718  4.770   1.00 31.76 ?  313  LYS C N   1 
ATOM   6732  C  CA  . LYS C  1 289 ? 40.718  35.574  4.125   1.00 31.32 ?  313  LYS C CA  1 
ATOM   6733  C  C   . LYS C  1 289 ? 41.227  34.145  4.230   1.00 30.68 ?  313  LYS C C   1 
ATOM   6734  O  O   . LYS C  1 289 ? 42.104  33.733  3.467   1.00 30.72 ?  313  LYS C O   1 
ATOM   6735  C  CB  . LYS C  1 289 ? 41.724  36.555  4.732   1.00 31.48 ?  313  LYS C CB  1 
ATOM   6736  C  CG  . LYS C  1 289 ? 41.386  38.017  4.455   1.00 32.38 ?  313  LYS C CG  1 
ATOM   6737  C  CD  . LYS C  1 289 ? 42.426  38.964  5.040   1.00 33.98 ?  313  LYS C CD  1 
ATOM   6738  C  CE  . LYS C  1 289 ? 42.093  40.417  4.711   1.00 35.40 ?  313  LYS C CE  1 
ATOM   6739  N  NZ  . LYS C  1 289 ? 40.837  40.889  5.380   1.00 36.09 ?  313  LYS C NZ  1 
ATOM   6740  N  N   . TRP C  1 290 ? 40.663  33.393  5.170   1.00 29.81 ?  314  TRP C N   1 
ATOM   6741  C  CA  . TRP C  1 290 ? 41.093  32.027  5.426   1.00 28.99 ?  314  TRP C CA  1 
ATOM   6742  C  C   . TRP C  1 290 ? 40.280  31.004  4.646   1.00 28.70 ?  314  TRP C C   1 
ATOM   6743  O  O   . TRP C  1 290 ? 39.084  31.190  4.411   1.00 28.58 ?  314  TRP C O   1 
ATOM   6744  C  CB  . TRP C  1 290 ? 40.994  31.698  6.915   1.00 28.74 ?  314  TRP C CB  1 
ATOM   6745  C  CG  . TRP C  1 290 ? 41.782  32.589  7.823   1.00 27.96 ?  314  TRP C CG  1 
ATOM   6746  C  CD1 . TRP C  1 290 ? 42.772  33.472  7.475   1.00 26.80 ?  314  TRP C CD1 1 
ATOM   6747  C  CD2 . TRP C  1 290 ? 41.670  32.654  9.249   1.00 26.94 ?  314  TRP C CD2 1 
ATOM   6748  N  NE1 . TRP C  1 290 ? 43.266  34.093  8.598   1.00 26.23 ?  314  TRP C NE1 1 
ATOM   6749  C  CE2 . TRP C  1 290 ? 42.610  33.609  9.700   1.00 26.51 ?  314  TRP C CE2 1 
ATOM   6750  C  CE3 . TRP C  1 290 ? 40.856  32.006  10.189  1.00 26.79 ?  314  TRP C CE3 1 
ATOM   6751  C  CZ2 . TRP C  1 290 ? 42.761  33.932  11.055  1.00 26.56 ?  314  TRP C CZ2 1 
ATOM   6752  C  CZ3 . TRP C  1 290 ? 41.009  32.327  11.544  1.00 27.01 ?  314  TRP C CZ3 1 
ATOM   6753  C  CH2 . TRP C  1 290 ? 41.956  33.280  11.958  1.00 26.28 ?  314  TRP C CH2 1 
ATOM   6754  N  N   . ASN C  1 291 ? 40.942  29.922  4.250   1.00 28.26 ?  315  ASN C N   1 
ATOM   6755  C  CA  . ASN C  1 291 ? 40.263  28.774  3.671   1.00 27.91 ?  315  ASN C CA  1 
ATOM   6756  C  C   . ASN C  1 291 ? 39.925  27.786  4.785   1.00 27.68 ?  315  ASN C C   1 
ATOM   6757  O  O   . ASN C  1 291 ? 40.798  27.069  5.276   1.00 27.73 ?  315  ASN C O   1 
ATOM   6758  C  CB  . ASN C  1 291 ? 41.127  28.114  2.584   1.00 27.79 ?  315  ASN C CB  1 
ATOM   6759  C  CG  . ASN C  1 291 ? 40.363  27.066  1.768   1.00 27.64 ?  315  ASN C CG  1 
ATOM   6760  O  OD1 . ASN C  1 291 ? 39.283  26.618  2.156   1.00 27.39 ?  315  ASN C OD1 1 
ATOM   6761  N  ND2 . ASN C  1 291 ? 40.936  26.668  0.636   1.00 26.84 ?  315  ASN C ND2 1 
ATOM   6762  N  N   . TRP C  1 292 ? 38.657  27.766  5.188   1.00 27.37 ?  316  TRP C N   1 
ATOM   6763  C  CA  . TRP C  1 292 ? 38.199  26.889  6.267   1.00 26.98 ?  316  TRP C CA  1 
ATOM   6764  C  C   . TRP C  1 292 ? 38.050  25.430  5.826   1.00 27.05 ?  316  TRP C C   1 
ATOM   6765  O  O   . TRP C  1 292 ? 38.018  24.524  6.666   1.00 26.75 ?  316  TRP C O   1 
ATOM   6766  C  CB  . TRP C  1 292 ? 36.875  27.398  6.846   1.00 26.83 ?  316  TRP C CB  1 
ATOM   6767  C  CG  . TRP C  1 292 ? 36.978  28.741  7.505   1.00 25.96 ?  316  TRP C CG  1 
ATOM   6768  C  CD1 . TRP C  1 292 ? 36.724  29.957  6.936   1.00 24.73 ?  316  TRP C CD1 1 
ATOM   6769  C  CD2 . TRP C  1 292 ? 37.367  29.004  8.861   1.00 25.01 ?  316  TRP C CD2 1 
ATOM   6770  N  NE1 . TRP C  1 292 ? 36.929  30.959  7.853   1.00 24.77 ?  316  TRP C NE1 1 
ATOM   6771  C  CE2 . TRP C  1 292 ? 37.320  30.403  9.043   1.00 24.78 ?  316  TRP C CE2 1 
ATOM   6772  C  CE3 . TRP C  1 292 ? 37.746  28.192  9.939   1.00 24.78 ?  316  TRP C CE3 1 
ATOM   6773  C  CZ2 . TRP C  1 292 ? 37.632  31.010  10.262  1.00 24.48 ?  316  TRP C CZ2 1 
ATOM   6774  C  CZ3 . TRP C  1 292 ? 38.059  28.797  11.152  1.00 24.80 ?  316  TRP C CZ3 1 
ATOM   6775  C  CH2 . TRP C  1 292 ? 38.000  30.193  11.302  1.00 24.51 ?  316  TRP C CH2 1 
ATOM   6776  N  N   . GLU C  1 293 ? 37.967  25.214  4.513   1.00 27.11 ?  317  GLU C N   1 
ATOM   6777  C  CA  . GLU C  1 293 ? 37.777  23.877  3.933   1.00 27.42 ?  317  GLU C CA  1 
ATOM   6778  C  C   . GLU C  1 293 ? 39.021  22.996  4.065   1.00 27.33 ?  317  GLU C C   1 
ATOM   6779  O  O   . GLU C  1 293 ? 38.942  21.763  4.036   1.00 27.15 ?  317  GLU C O   1 
ATOM   6780  C  CB  . GLU C  1 293 ? 37.372  23.987  2.458   1.00 27.57 ?  317  GLU C CB  1 
ATOM   6781  C  CG  . GLU C  1 293 ? 36.033  24.685  2.207   1.00 28.46 ?  317  GLU C CG  1 
ATOM   6782  C  CD  . GLU C  1 293 ? 34.831  23.874  2.671   1.00 30.00 ?  317  GLU C CD  1 
ATOM   6783  O  OE1 . GLU C  1 293 ? 34.947  22.639  2.826   1.00 30.94 ?  317  GLU C OE1 1 
ATOM   6784  O  OE2 . GLU C  1 293 ? 33.760  24.479  2.877   1.00 31.36 -1 317  GLU C OE2 1 
ATOM   6785  N  N   . VAL C  1 294 ? 40.164  23.657  4.192   1.00 27.24 ?  318  VAL C N   1 
ATOM   6786  C  CA  . VAL C  1 294 ? 41.455  23.021  4.402   1.00 27.26 ?  318  VAL C CA  1 
ATOM   6787  C  C   . VAL C  1 294 ? 41.488  22.329  5.775   1.00 27.25 ?  318  VAL C C   1 
ATOM   6788  O  O   . VAL C  1 294 ? 40.929  22.847  6.746   1.00 27.16 ?  318  VAL C O   1 
ATOM   6789  C  CB  . VAL C  1 294 ? 42.570  24.097  4.227   1.00 27.40 ?  318  VAL C CB  1 
ATOM   6790  C  CG1 . VAL C  1 294 ? 43.626  24.035  5.313   1.00 27.24 ?  318  VAL C CG1 1 
ATOM   6791  C  CG2 . VAL C  1 294 ? 43.172  24.026  2.830   1.00 27.11 ?  318  VAL C CG2 1 
ATOM   6792  N  N   . ARG C  1 295 ? 42.113  21.152  5.848   1.00 27.18 ?  319  ARG C N   1 
ATOM   6793  C  CA  . ARG C  1 295 ? 42.218  20.431  7.121   1.00 27.28 ?  319  ARG C CA  1 
ATOM   6794  C  C   . ARG C  1 295 ? 43.113  21.182  8.116   1.00 26.90 ?  319  ARG C C   1 
ATOM   6795  O  O   . ARG C  1 295 ? 43.970  21.975  7.716   1.00 26.75 ?  319  ARG C O   1 
ATOM   6796  C  CB  . ARG C  1 295 ? 42.676  18.976  6.914   1.00 27.49 ?  319  ARG C CB  1 
ATOM   6797  C  CG  . ARG C  1 295 ? 44.164  18.794  6.669   1.00 28.94 ?  319  ARG C CG  1 
ATOM   6798  C  CD  . ARG C  1 295 ? 44.501  17.384  6.210   1.00 31.04 ?  319  ARG C CD  1 
ATOM   6799  N  NE  . ARG C  1 295 ? 45.935  17.256  5.955   1.00 33.96 ?  319  ARG C NE  1 
ATOM   6800  C  CZ  . ARG C  1 295 ? 46.542  16.151  5.524   1.00 35.47 ?  319  ARG C CZ  1 
ATOM   6801  N  NH1 . ARG C  1 295 ? 45.851  15.044  5.279   1.00 35.84 ?  319  ARG C NH1 1 
ATOM   6802  N  NH2 . ARG C  1 295 ? 47.852  16.157  5.331   1.00 36.22 ?  319  ARG C NH2 1 
ATOM   6803  N  N   . LEU C  1 296 ? 42.890  20.945  9.406   1.00 26.65 ?  320  LEU C N   1 
ATOM   6804  C  CA  . LEU C  1 296 ? 43.608  21.654  10.471  1.00 26.56 ?  320  LEU C CA  1 
ATOM   6805  C  C   . LEU C  1 296 ? 45.138  21.640  10.316  1.00 26.65 ?  320  LEU C C   1 
ATOM   6806  O  O   . LEU C  1 296 ? 45.792  22.675  10.482  1.00 26.76 ?  320  LEU C O   1 
ATOM   6807  C  CB  . LEU C  1 296 ? 43.185  21.116  11.842  1.00 26.43 ?  320  LEU C CB  1 
ATOM   6808  C  CG  . LEU C  1 296 ? 42.305  21.948  12.794  1.00 26.32 ?  320  LEU C CG  1 
ATOM   6809  C  CD1 . LEU C  1 296 ? 41.558  23.111  12.135  1.00 25.94 ?  320  LEU C CD1 1 
ATOM   6810  C  CD2 . LEU C  1 296 ? 41.344  21.058  13.563  1.00 25.43 ?  320  LEU C CD2 1 
ATOM   6811  N  N   . LYS C  1 297 ? 45.690  20.472  9.984   1.00 26.39 ?  321  LYS C N   1 
ATOM   6812  C  CA  . LYS C  1 297 ? 47.126  20.299  9.725   1.00 26.39 ?  321  LYS C CA  1 
ATOM   6813  C  C   . LYS C  1 297 ? 47.663  21.286  8.680   1.00 26.08 ?  321  LYS C C   1 
ATOM   6814  O  O   . LYS C  1 297 ? 48.833  21.674  8.730   1.00 25.88 ?  321  LYS C O   1 
ATOM   6815  C  CB  . LYS C  1 297 ? 47.403  18.846  9.296   1.00 26.54 ?  321  LYS C CB  1 
ATOM   6816  C  CG  . LYS C  1 297 ? 48.872  18.433  9.228   1.00 27.81 ?  321  LYS C CG  1 
ATOM   6817  C  CD  . LYS C  1 297 ? 49.427  18.044  10.594  1.00 29.49 ?  321  LYS C CD  1 
ATOM   6818  C  CE  . LYS C  1 297 ? 50.779  17.356  10.468  1.00 31.19 ?  321  LYS C CE  1 
ATOM   6819  N  NZ  . LYS C  1 297 ? 50.663  15.920  10.053  1.00 32.01 ?  321  LYS C NZ  1 
ATOM   6820  N  N   . ASP C  1 298 ? 46.801  21.693  7.746   1.00 25.87 ?  322  ASP C N   1 
ATOM   6821  C  CA  . ASP C  1 298 ? 47.164  22.638  6.682   1.00 25.65 ?  322  ASP C CA  1 
ATOM   6822  C  C   . ASP C  1 298 ? 46.658  24.068  6.907   1.00 25.55 ?  322  ASP C C   1 
ATOM   6823  O  O   . ASP C  1 298 ? 46.906  24.949  6.077   1.00 25.31 ?  322  ASP C O   1 
ATOM   6824  C  CB  . ASP C  1 298 ? 46.646  22.142  5.328   1.00 25.65 ?  322  ASP C CB  1 
ATOM   6825  C  CG  . ASP C  1 298 ? 47.208  20.790  4.939   1.00 25.88 ?  322  ASP C CG  1 
ATOM   6826  O  OD1 . ASP C  1 298 ? 48.376  20.495  5.276   1.00 25.54 ?  322  ASP C OD1 1 
ATOM   6827  O  OD2 . ASP C  1 298 ? 46.471  20.022  4.286   1.00 26.29 -1 322  ASP C OD2 1 
ATOM   6828  N  N   . ALA C  1 299 ? 45.945  24.294  8.011   1.00 25.47 ?  323  ALA C N   1 
ATOM   6829  C  CA  . ALA C  1 299 ? 45.311  25.592  8.291   1.00 25.50 ?  323  ALA C CA  1 
ATOM   6830  C  C   . ALA C  1 299 ? 46.275  26.775  8.204   1.00 25.61 ?  323  ALA C C   1 
ATOM   6831  O  O   . ALA C  1 299 ? 45.987  27.767  7.526   1.00 25.53 ?  323  ALA C O   1 
ATOM   6832  C  CB  . ALA C  1 299 ? 44.605  25.572  9.654   1.00 25.33 ?  323  ALA C CB  1 
ATOM   6833  N  N   . PHE C  1 300 ? 47.422  26.660  8.872   1.00 25.65 ?  324  PHE C N   1 
ATOM   6834  C  CA  . PHE C  1 300 ? 48.389  27.760  8.931   1.00 26.06 ?  324  PHE C CA  1 
ATOM   6835  C  C   . PHE C  1 300 ? 49.198  27.955  7.642   1.00 26.21 ?  324  PHE C C   1 
ATOM   6836  O  O   . PHE C  1 300 ? 49.868  28.973  7.493   1.00 26.33 ?  324  PHE C O   1 
ATOM   6837  C  CB  . PHE C  1 300 ? 49.329  27.620  10.143  1.00 25.89 ?  324  PHE C CB  1 
ATOM   6838  C  CG  . PHE C  1 300 ? 48.616  27.551  11.473  1.00 26.02 ?  324  PHE C CG  1 
ATOM   6839  C  CD1 . PHE C  1 300 ? 47.568  28.415  11.771  1.00 25.65 ?  324  PHE C CD1 1 
ATOM   6840  C  CD2 . PHE C  1 300 ? 49.011  26.631  12.437  1.00 26.59 ?  324  PHE C CD2 1 
ATOM   6841  C  CE1 . PHE C  1 300 ? 46.913  28.350  12.997  1.00 25.49 ?  324  PHE C CE1 1 
ATOM   6842  C  CE2 . PHE C  1 300 ? 48.361  26.563  13.673  1.00 26.32 ?  324  PHE C CE2 1 
ATOM   6843  C  CZ  . PHE C  1 300 ? 47.313  27.426  13.949  1.00 25.78 ?  324  PHE C CZ  1 
ATOM   6844  N  N   . SER C  1 301 ? 49.131  26.991  6.723   1.00 26.50 ?  325  SER C N   1 
ATOM   6845  C  CA  . SER C  1 301 ? 49.830  27.091  5.433   1.00 26.83 ?  325  SER C CA  1 
ATOM   6846  C  C   . SER C  1 301 ? 48.865  27.257  4.258   1.00 26.86 ?  325  SER C C   1 
ATOM   6847  O  O   . SER C  1 301 ? 48.710  28.359  3.724   1.00 27.06 ?  325  SER C O   1 
ATOM   6848  C  CB  . SER C  1 301 ? 50.753  25.887  5.207   1.00 26.84 ?  325  SER C CB  1 
ATOM   6849  O  OG  . SER C  1 301 ? 50.039  24.665  5.304   1.00 27.32 ?  325  SER C OG  1 
ATOM   6850  N  N   . LYS C  1 302 ? 48.216  26.163  3.864   1.00 26.82 ?  326  LYS C N   1 
ATOM   6851  C  CA  . LYS C  1 302 ? 47.257  26.180  2.759   1.00 26.80 ?  326  LYS C CA  1 
ATOM   6852  C  C   . LYS C  1 302 ? 46.042  27.063  3.057   1.00 26.61 ?  326  LYS C C   1 
ATOM   6853  O  O   . LYS C  1 302 ? 45.550  27.772  2.173   1.00 26.42 ?  326  LYS C O   1 
ATOM   6854  C  CB  . LYS C  1 302 ? 46.816  24.759  2.406   1.00 27.03 ?  326  LYS C CB  1 
ATOM   6855  C  CG  . LYS C  1 302 ? 47.879  23.947  1.685   1.00 27.44 ?  326  LYS C CG  1 
ATOM   6856  C  CD  . LYS C  1 302 ? 47.489  22.489  1.574   1.00 28.71 ?  326  LYS C CD  1 
ATOM   6857  C  CE  . LYS C  1 302 ? 48.560  21.700  0.829   1.00 29.91 ?  326  LYS C CE  1 
ATOM   6858  N  NZ  . LYS C  1 302 ? 48.603  20.283  1.279   1.00 31.18 ?  326  LYS C NZ  1 
ATOM   6859  N  N   . GLY C  1 303 ? 45.580  27.031  4.305   1.00 26.23 ?  327  GLY C N   1 
ATOM   6860  C  CA  . GLY C  1 303 ? 44.418  27.815  4.719   1.00 26.17 ?  327  GLY C CA  1 
ATOM   6861  C  C   . GLY C  1 303 ? 44.686  29.304  4.830   1.00 26.12 ?  327  GLY C C   1 
ATOM   6862  O  O   . GLY C  1 303 ? 43.769  30.111  4.704   1.00 26.14 ?  327  GLY C O   1 
ATOM   6863  N  N   . GLY C  1 304 ? 45.945  29.669  5.067   1.00 26.17 ?  328  GLY C N   1 
ATOM   6864  C  CA  . GLY C  1 304 ? 46.331  31.070  5.262   1.00 25.98 ?  328  GLY C CA  1 
ATOM   6865  C  C   . GLY C  1 304 ? 45.999  31.606  6.647   1.00 25.91 ?  328  GLY C C   1 
ATOM   6866  O  O   . GLY C  1 304 ? 46.065  32.814  6.884   1.00 26.10 ?  328  GLY C O   1 
ATOM   6867  N  N   . GLN C  1 305 ? 45.648  30.708  7.565   1.00 25.82 ?  329  GLN C N   1 
ATOM   6868  C  CA  . GLN C  1 305 ? 45.231  31.091  8.916   1.00 25.76 ?  329  GLN C CA  1 
ATOM   6869  C  C   . GLN C  1 305 ? 46.397  31.656  9.725   1.00 25.65 ?  329  GLN C C   1 
ATOM   6870  O  O   . GLN C  1 305 ? 47.440  31.010  9.865   1.00 25.54 ?  329  GLN C O   1 
ATOM   6871  C  CB  . GLN C  1 305 ? 44.600  29.897  9.638   1.00 25.78 ?  329  GLN C CB  1 
ATOM   6872  C  CG  . GLN C  1 305 ? 43.825  30.261  10.900  1.00 25.62 ?  329  GLN C CG  1 
ATOM   6873  C  CD  . GLN C  1 305 ? 43.021  29.101  11.453  1.00 26.08 ?  329  GLN C CD  1 
ATOM   6874  O  OE1 . GLN C  1 305 ? 42.492  28.275  10.701  1.00 26.35 ?  329  GLN C OE1 1 
ATOM   6875  N  NE2 . GLN C  1 305 ? 42.925  29.030  12.777  1.00 25.79 ?  329  GLN C NE2 1 
ATOM   6876  N  N   . ASN C  1 306 ? 46.215  32.864  10.253  1.00 25.49 ?  330  ASN C N   1 
ATOM   6877  C  CA  . ASN C  1 306 ? 47.280  33.536  11.003  1.00 25.46 ?  330  ASN C CA  1 
ATOM   6878  C  C   . ASN C  1 306 ? 46.939  33.819  12.465  1.00 25.02 ?  330  ASN C C   1 
ATOM   6879  O  O   . ASN C  1 306 ? 47.727  34.441  13.190  1.00 25.07 ?  330  ASN C O   1 
ATOM   6880  C  CB  . ASN C  1 306 ? 47.723  34.816  10.285  1.00 25.63 ?  330  ASN C CB  1 
ATOM   6881  C  CG  . ASN C  1 306 ? 46.637  35.868  10.237  1.00 26.84 ?  330  ASN C CG  1 
ATOM   6882  O  OD1 . ASN C  1 306 ? 45.474  35.574  9.945   1.00 28.10 ?  330  ASN C OD1 1 
ATOM   6883  N  ND2 . ASN C  1 306 ? 47.012  37.111  10.518  1.00 28.19 ?  330  ASN C ND2 1 
ATOM   6884  N  N   . ALA C  1 307 ? 45.767  33.350  12.891  1.00 24.44 ?  331  ALA C N   1 
ATOM   6885  C  CA  . ALA C  1 307 ? 45.346  33.455  14.286  1.00 23.81 ?  331  ALA C CA  1 
ATOM   6886  C  C   . ALA C  1 307 ? 44.769  32.122  14.755  1.00 23.25 ?  331  ALA C C   1 
ATOM   6887  O  O   . ALA C  1 307 ? 44.110  31.428  13.980  1.00 23.36 ?  331  ALA C O   1 
ATOM   6888  C  CB  . ALA C  1 307 ? 44.328  34.580  14.461  1.00 23.82 ?  331  ALA C CB  1 
ATOM   6889  N  N   . PRO C  1 308 ? 45.018  31.753  16.025  1.00 22.65 ?  332  PRO C N   1 
ATOM   6890  C  CA  . PRO C  1 308 ? 44.547  30.456  16.502  1.00 22.25 ?  332  PRO C CA  1 
ATOM   6891  C  C   . PRO C  1 308 ? 43.037  30.431  16.752  1.00 21.68 ?  332  PRO C C   1 
ATOM   6892  O  O   . PRO C  1 308 ? 42.418  31.478  16.957  1.00 21.46 ?  332  PRO C O   1 
ATOM   6893  C  CB  . PRO C  1 308 ? 45.317  30.268  17.811  1.00 22.17 ?  332  PRO C CB  1 
ATOM   6894  C  CG  . PRO C  1 308 ? 45.541  31.651  18.299  1.00 22.19 ?  332  PRO C CG  1 
ATOM   6895  C  CD  . PRO C  1 308 ? 45.718  32.507  17.082  1.00 22.56 ?  332  PRO C CD  1 
ATOM   6896  N  N   . THR C  1 309 ? 42.468  29.232  16.714  1.00 21.20 ?  333  THR C N   1 
ATOM   6897  C  CA  . THR C  1 309 ? 41.044  29.007  16.941  1.00 20.77 ?  333  THR C CA  1 
ATOM   6898  C  C   . THR C  1 309 ? 40.895  27.865  17.946  1.00 20.65 ?  333  THR C C   1 
ATOM   6899  O  O   . THR C  1 309 ? 41.867  27.143  18.201  1.00 20.34 ?  333  THR C O   1 
ATOM   6900  C  CB  . THR C  1 309 ? 40.341  28.599  15.642  1.00 20.77 ?  333  THR C CB  1 
ATOM   6901  O  OG1 . THR C  1 309 ? 41.097  27.556  15.015  1.00 20.70 ?  333  THR C OG1 1 
ATOM   6902  C  CG2 . THR C  1 309 ? 40.214  29.788  14.687  1.00 20.44 ?  333  THR C CG2 1 
ATOM   6903  N  N   . CYS C  1 310 ? 39.690  27.700  18.500  1.00 20.29 ?  334  CYS C N   1 
ATOM   6904  C  CA  . CYS C  1 310 ? 39.406  26.630  19.463  1.00 20.28 ?  334  CYS C CA  1 
ATOM   6905  C  C   . CYS C  1 310 ? 39.923  25.287  18.970  1.00 20.46 ?  334  CYS C C   1 
ATOM   6906  O  O   . CYS C  1 310 ? 40.694  24.618  19.661  1.00 20.55 ?  334  CYS C O   1 
ATOM   6907  C  CB  . CYS C  1 310 ? 37.900  26.493  19.730  1.00 20.49 ?  334  CYS C CB  1 
ATOM   6908  S  SG  . CYS C  1 310 ? 36.947  28.021  19.797  1.00 18.98 ?  334  CYS C SG  1 
ATOM   6909  N  N   . ALA C  1 311 ? 39.491  24.908  17.770  1.00 20.57 ?  335  ALA C N   1 
ATOM   6910  C  CA  . ALA C  1 311 ? 39.826  23.614  17.186  1.00 20.77 ?  335  ALA C CA  1 
ATOM   6911  C  C   . ALA C  1 311 ? 41.332  23.459  16.975  1.00 20.87 ?  335  ALA C C   1 
ATOM   6912  O  O   . ALA C  1 311 ? 41.910  22.458  17.383  1.00 21.09 ?  335  ALA C O   1 
ATOM   6913  C  CB  . ALA C  1 311 ? 39.068  23.407  15.876  1.00 20.70 ?  335  ALA C CB  1 
ATOM   6914  N  N   . ALA C  1 312 ? 41.958  24.462  16.360  1.00 20.99 ?  336  ALA C N   1 
ATOM   6915  C  CA  . ALA C  1 312 ? 43.403  24.445  16.117  1.00 21.21 ?  336  ALA C CA  1 
ATOM   6916  C  C   . ALA C  1 312 ? 44.223  24.274  17.403  1.00 21.26 ?  336  ALA C C   1 
ATOM   6917  O  O   . ALA C  1 312 ? 45.204  23.541  17.419  1.00 21.41 ?  336  ALA C O   1 
ATOM   6918  C  CB  . ALA C  1 312 ? 43.842  25.701  15.353  1.00 20.87 ?  336  ALA C CB  1 
ATOM   6919  N  N   . CYS C  1 313 ? 43.818  24.936  18.481  1.00 21.49 ?  337  CYS C N   1 
ATOM   6920  C  CA  . CYS C  1 313 ? 44.543  24.811  19.746  1.00 21.60 ?  337  CYS C CA  1 
ATOM   6921  C  C   . CYS C  1 313 ? 44.225  23.520  20.490  1.00 22.03 ?  337  CYS C C   1 
ATOM   6922  O  O   . CYS C  1 313 ? 45.128  22.869  21.013  1.00 21.91 ?  337  CYS C O   1 
ATOM   6923  C  CB  . CYS C  1 313 ? 44.280  26.009  20.656  1.00 21.48 ?  337  CYS C CB  1 
ATOM   6924  S  SG  . CYS C  1 313 ? 45.314  27.461  20.354  1.00 20.88 ?  337  CYS C SG  1 
ATOM   6925  N  N   . HIS C  1 314 ? 42.947  23.148  20.536  1.00 22.38 ?  338  HIS C N   1 
ATOM   6926  C  CA  . HIS C  1 314 ? 42.522  22.043  21.395  1.00 22.77 ?  338  HIS C CA  1 
ATOM   6927  C  C   . HIS C  1 314 ? 42.578  20.657  20.759  1.00 23.31 ?  338  HIS C C   1 
ATOM   6928  O  O   . HIS C  1 314 ? 42.686  19.663  21.474  1.00 23.26 ?  338  HIS C O   1 
ATOM   6929  C  CB  . HIS C  1 314 ? 41.161  22.345  22.038  1.00 22.56 ?  338  HIS C CB  1 
ATOM   6930  C  CG  . HIS C  1 314 ? 41.233  23.410  23.089  1.00 21.87 ?  338  HIS C CG  1 
ATOM   6931  N  ND1 . HIS C  1 314 ? 41.785  23.184  24.331  1.00 20.63 ?  338  HIS C ND1 1 
ATOM   6932  C  CD2 . HIS C  1 314 ? 40.862  24.714  23.073  1.00 20.38 ?  338  HIS C CD2 1 
ATOM   6933  C  CE1 . HIS C  1 314 ? 41.741  24.298  25.038  1.00 20.11 ?  338  HIS C CE1 1 
ATOM   6934  N  NE2 . HIS C  1 314 ? 41.180  25.241  24.302  1.00 19.94 ?  338  HIS C NE2 1 
ATOM   6935  N  N   . MET C  1 315 ? 42.527  20.588  19.429  1.00 23.94 ?  339  MET C N   1 
ATOM   6936  C  CA  . MET C  1 315 ? 42.679  19.305  18.731  1.00 24.65 ?  339  MET C CA  1 
ATOM   6937  C  C   . MET C  1 315 ? 44.134  18.992  18.372  1.00 24.89 ?  339  MET C C   1 
ATOM   6938  O  O   . MET C  1 315 ? 44.446  17.874  17.955  1.00 24.92 ?  339  MET C O   1 
ATOM   6939  C  CB  . MET C  1 315 ? 41.797  19.242  17.479  1.00 24.72 ?  339  MET C CB  1 
ATOM   6940  C  CG  . MET C  1 315 ? 40.321  19.025  17.768  1.00 25.98 ?  339  MET C CG  1 
ATOM   6941  S  SD  . MET C  1 315 ? 39.315  19.103  16.275  1.00 28.75 ?  339  MET C SD  1 
ATOM   6942  C  CE  . MET C  1 315 ? 39.220  17.398  15.780  1.00 28.97 ?  339  MET C CE  1 
ATOM   6943  N  N   . GLU C  1 316 ? 45.013  19.983  18.528  1.00 25.23 ?  340  GLU C N   1 
ATOM   6944  C  CA  . GLU C  1 316 ? 46.442  19.811  18.267  1.00 25.55 ?  340  GLU C CA  1 
ATOM   6945  C  C   . GLU C  1 316 ? 47.095  19.066  19.421  1.00 25.79 ?  340  GLU C C   1 
ATOM   6946  O  O   . GLU C  1 316 ? 46.842  19.377  20.587  1.00 25.79 ?  340  GLU C O   1 
ATOM   6947  C  CB  . GLU C  1 316 ? 47.124  21.172  18.078  1.00 25.55 ?  340  GLU C CB  1 
ATOM   6948  C  CG  . GLU C  1 316 ? 48.514  21.126  17.420  1.00 25.98 ?  340  GLU C CG  1 
ATOM   6949  C  CD  . GLU C  1 316 ? 49.644  20.770  18.383  1.00 26.59 ?  340  GLU C CD  1 
ATOM   6950  O  OE1 . GLU C  1 316 ? 49.537  21.043  19.602  1.00 26.84 ?  340  GLU C OE1 1 
ATOM   6951  O  OE2 . GLU C  1 316 ? 50.657  20.217  17.914  1.00 27.32 -1 340  GLU C OE2 1 
ATOM   6952  N  N   . TYR C  1 317 ? 47.930  18.083  19.089  1.00 26.03 ?  341  TYR C N   1 
ATOM   6953  C  CA  . TYR C  1 317 ? 48.774  17.413  20.079  1.00 26.45 ?  341  TYR C CA  1 
ATOM   6954  C  C   . TYR C  1 317 ? 50.060  16.893  19.449  1.00 26.83 ?  341  TYR C C   1 
ATOM   6955  O  O   . TYR C  1 317 ? 50.019  16.068  18.535  1.00 26.82 ?  341  TYR C O   1 
ATOM   6956  C  CB  . TYR C  1 317 ? 48.024  16.276  20.788  1.00 26.29 ?  341  TYR C CB  1 
ATOM   6957  C  CG  . TYR C  1 317 ? 48.821  15.618  21.898  1.00 26.28 ?  341  TYR C CG  1 
ATOM   6958  C  CD1 . TYR C  1 317 ? 49.111  16.307  23.081  1.00 25.75 ?  341  TYR C CD1 1 
ATOM   6959  C  CD2 . TYR C  1 317 ? 49.289  14.309  21.767  1.00 25.96 ?  341  TYR C CD2 1 
ATOM   6960  C  CE1 . TYR C  1 317 ? 49.841  15.709  24.108  1.00 25.24 ?  341  TYR C CE1 1 
ATOM   6961  C  CE2 . TYR C  1 317 ? 50.023  13.698  22.791  1.00 26.14 ?  341  TYR C CE2 1 
ATOM   6962  C  CZ  . TYR C  1 317 ? 50.295  14.407  23.957  1.00 26.01 ?  341  TYR C CZ  1 
ATOM   6963  O  OH  . TYR C  1 317 ? 51.014  13.813  24.972  1.00 26.01 ?  341  TYR C OH  1 
ATOM   6964  N  N   . GLU C  1 318 ? 51.194  17.388  19.950  1.00 27.37 ?  342  GLU C N   1 
ATOM   6965  C  CA  . GLU C  1 318 ? 52.530  16.982  19.481  1.00 28.12 ?  342  GLU C CA  1 
ATOM   6966  C  C   . GLU C  1 318 ? 52.666  16.965  17.954  1.00 28.27 ?  342  GLU C C   1 
ATOM   6967  O  O   . GLU C  1 318 ? 53.265  16.052  17.388  1.00 28.56 ?  342  GLU C O   1 
ATOM   6968  C  CB  . GLU C  1 318 ? 52.936  15.621  20.079  1.00 28.30 ?  342  GLU C CB  1 
ATOM   6969  C  CG  . GLU C  1 318 ? 53.082  15.599  21.610  1.00 29.27 ?  342  GLU C CG  1 
ATOM   6970  C  CD  . GLU C  1 318 ? 54.145  16.558  22.127  1.00 30.33 ?  342  GLU C CD  1 
ATOM   6971  O  OE1 . GLU C  1 318 ? 53.973  17.088  23.240  1.00 30.60 ?  342  GLU C OE1 1 
ATOM   6972  O  OE2 . GLU C  1 318 ? 55.153  16.787  21.423  1.00 31.87 -1 342  GLU C OE2 1 
ATOM   6973  N  N   . GLY C  1 319 ? 52.098  17.972  17.295  1.00 28.54 ?  343  GLY C N   1 
ATOM   6974  C  CA  . GLY C  1 319 ? 52.186  18.094  15.839  1.00 28.94 ?  343  GLY C CA  1 
ATOM   6975  C  C   . GLY C  1 319 ? 51.090  17.412  15.034  1.00 29.17 ?  343  GLY C C   1 
ATOM   6976  O  O   . GLY C  1 319 ? 51.037  17.570  13.815  1.00 29.47 ?  343  GLY C O   1 
ATOM   6977  N  N   . GLU C  1 320 ? 50.217  16.657  15.704  1.00 29.07 ?  344  GLU C N   1 
ATOM   6978  C  CA  . GLU C  1 320 ? 49.114  15.958  15.033  1.00 29.28 ?  344  GLU C CA  1 
ATOM   6979  C  C   . GLU C  1 320 ? 47.748  16.529  15.430  1.00 28.61 ?  344  GLU C C   1 
ATOM   6980  O  O   . GLU C  1 320 ? 47.606  17.129  16.499  1.00 28.50 ?  344  GLU C O   1 
ATOM   6981  C  CB  . GLU C  1 320 ? 49.160  14.447  15.327  1.00 29.75 ?  344  GLU C CB  1 
ATOM   6982  C  CG  . GLU C  1 320 ? 50.413  13.732  14.810  1.00 32.40 ?  344  GLU C CG  1 
ATOM   6983  C  CD  . GLU C  1 320 ? 50.327  12.207  14.905  1.00 36.17 ?  344  GLU C CD  1 
ATOM   6984  O  OE1 . GLU C  1 320 ? 50.540  11.533  13.864  1.00 37.13 ?  344  GLU C OE1 1 
ATOM   6985  O  OE2 . GLU C  1 320 ? 50.047  11.681  16.011  1.00 37.21 -1 344  GLU C OE2 1 
ATOM   6986  N  N   . TYR C  1 321 ? 46.750  16.342  14.565  1.00 27.72 ?  345  TYR C N   1 
ATOM   6987  C  CA  . TYR C  1 321 ? 45.375  16.739  14.870  1.00 27.08 ?  345  TYR C CA  1 
ATOM   6988  C  C   . TYR C  1 321 ? 44.438  15.527  14.961  1.00 26.67 ?  345  TYR C C   1 
ATOM   6989  O  O   . TYR C  1 321 ? 44.412  14.690  14.061  1.00 26.55 ?  345  TYR C O   1 
ATOM   6990  C  CB  . TYR C  1 321 ? 44.862  17.767  13.853  1.00 27.01 ?  345  TYR C CB  1 
ATOM   6991  C  CG  . TYR C  1 321 ? 45.560  19.114  13.935  1.00 26.68 ?  345  TYR C CG  1 
ATOM   6992  C  CD1 . TYR C  1 321 ? 46.744  19.349  13.242  1.00 26.64 ?  345  TYR C CD1 1 
ATOM   6993  C  CD2 . TYR C  1 321 ? 45.038  20.149  14.711  1.00 26.50 ?  345  TYR C CD2 1 
ATOM   6994  C  CE1 . TYR C  1 321 ? 47.392  20.575  13.316  1.00 26.74 ?  345  TYR C CE1 1 
ATOM   6995  C  CE2 . TYR C  1 321 ? 45.679  21.383  14.792  1.00 25.94 ?  345  TYR C CE2 1 
ATOM   6996  C  CZ  . TYR C  1 321 ? 46.854  21.588  14.091  1.00 26.32 ?  345  TYR C CZ  1 
ATOM   6997  O  OH  . TYR C  1 321 ? 47.498  22.798  14.156  1.00 25.73 ?  345  TYR C OH  1 
ATOM   6998  N  N   . THR C  1 322 ? 43.694  15.432  16.066  1.00 26.13 ?  346  THR C N   1 
ATOM   6999  C  CA  . THR C  1 322 ? 42.727  14.344  16.283  1.00 25.75 ?  346  THR C CA  1 
ATOM   7000  C  C   . THR C  1 322 ? 41.458  14.862  16.973  1.00 25.84 ?  346  THR C C   1 
ATOM   7001  O  O   . THR C  1 322 ? 41.441  15.979  17.493  1.00 25.54 ?  346  THR C O   1 
ATOM   7002  C  CB  . THR C  1 322 ? 43.304  13.175  17.153  1.00 25.59 ?  346  THR C CB  1 
ATOM   7003  O  OG1 . THR C  1 322 ? 43.223  13.514  18.542  1.00 25.40 ?  346  THR C OG1 1 
ATOM   7004  C  CG2 . THR C  1 322 ? 44.753  12.822  16.780  1.00 25.40 ?  346  THR C CG2 1 
ATOM   7005  N  N   . HIS C  1 323 ? 40.416  14.026  17.004  1.00 25.78 ?  347  HIS C N   1 
ATOM   7006  C  CA  . HIS C  1 323 ? 39.166  14.337  17.708  1.00 25.61 ?  347  HIS C CA  1 
ATOM   7007  C  C   . HIS C  1 323 ? 39.285  14.211  19.241  1.00 25.79 ?  347  HIS C C   1 
ATOM   7008  O  O   . HIS C  1 323 ? 38.304  14.416  19.959  1.00 25.88 ?  347  HIS C O   1 
ATOM   7009  C  CB  . HIS C  1 323 ? 38.012  13.464  17.182  1.00 25.23 ?  347  HIS C CB  1 
ATOM   7010  C  CG  . HIS C  1 323 ? 37.246  14.073  16.044  1.00 24.81 ?  347  HIS C CG  1 
ATOM   7011  N  ND1 . HIS C  1 323 ? 37.801  14.297  14.802  1.00 23.88 ?  347  HIS C ND1 1 
ATOM   7012  C  CD2 . HIS C  1 323 ? 35.954  14.475  15.953  1.00 23.91 ?  347  HIS C CD2 1 
ATOM   7013  C  CE1 . HIS C  1 323 ? 36.891  14.826  14.002  1.00 23.58 ?  347  HIS C CE1 1 
ATOM   7014  N  NE2 . HIS C  1 323 ? 35.757  14.944  14.673  1.00 23.89 ?  347  HIS C NE2 1 
ATOM   7015  N  N   . ASN C  1 324 ? 40.477  13.867  19.732  1.00 25.79 ?  348  ASN C N   1 
ATOM   7016  C  CA  . ASN C  1 324 ? 40.752  13.800  21.172  1.00 25.65 ?  348  ASN C CA  1 
ATOM   7017  C  C   . ASN C  1 324 ? 41.186  15.177  21.677  1.00 25.64 ?  348  ASN C C   1 
ATOM   7018  O  O   . ASN C  1 324 ? 42.208  15.709  21.234  1.00 25.80 ?  348  ASN C O   1 
ATOM   7019  C  CB  . ASN C  1 324 ? 41.833  12.740  21.460  1.00 25.73 ?  348  ASN C CB  1 
ATOM   7020  C  CG  . ASN C  1 324 ? 42.052  12.486  22.955  1.00 25.16 ?  348  ASN C CG  1 
ATOM   7021  O  OD1 . ASN C  1 324 ? 41.996  13.399  23.779  1.00 25.75 ?  348  ASN C OD1 1 
ATOM   7022  N  ND2 . ASN C  1 324 ? 42.324  11.237  23.299  1.00 24.00 ?  348  ASN C ND2 1 
ATOM   7023  N  N   . ILE C  1 325 ? 40.408  15.750  22.594  1.00 25.66 ?  349  ILE C N   1 
ATOM   7024  C  CA  . ILE C  1 325 ? 40.677  17.101  23.112  1.00 25.51 ?  349  ILE C CA  1 
ATOM   7025  C  C   . ILE C  1 325 ? 41.188  17.137  24.568  1.00 25.61 ?  349  ILE C C   1 
ATOM   7026  O  O   . ILE C  1 325 ? 41.164  18.189  25.216  1.00 25.62 ?  349  ILE C O   1 
ATOM   7027  C  CB  . ILE C  1 325 ? 39.438  18.056  22.948  1.00 25.60 ?  349  ILE C CB  1 
ATOM   7028  C  CG1 . ILE C  1 325 ? 38.122  17.379  23.361  1.00 25.29 ?  349  ILE C CG1 1 
ATOM   7029  C  CG2 . ILE C  1 325 ? 39.318  18.555  21.509  1.00 25.35 ?  349  ILE C CG2 1 
ATOM   7030  C  CD1 . ILE C  1 325 ? 37.963  17.101  24.845  1.00 25.24 ?  349  ILE C CD1 1 
ATOM   7031  N  N   . THR C  1 326 ? 41.672  16.002  25.070  1.00 25.58 ?  350  THR C N   1 
ATOM   7032  C  CA  . THR C  1 326 ? 41.964  15.865  26.508  1.00 25.57 ?  350  THR C CA  1 
ATOM   7033  C  C   . THR C  1 326 ? 43.439  15.881  26.914  1.00 25.45 ?  350  THR C C   1 
ATOM   7034  O  O   . THR C  1 326 ? 43.752  16.079  28.091  1.00 25.45 ?  350  THR C O   1 
ATOM   7035  C  CB  . THR C  1 326 ? 41.362  14.563  27.082  1.00 25.61 ?  350  THR C CB  1 
ATOM   7036  O  OG1 . THR C  1 326 ? 41.992  13.432  26.462  1.00 25.73 ?  350  THR C OG1 1 
ATOM   7037  C  CG2 . THR C  1 326 ? 39.854  14.510  26.859  1.00 25.47 ?  350  THR C CG2 1 
ATOM   7038  N  N   . ARG C  1 327 ? 44.335  15.673  25.954  1.00 25.49 ?  351  ARG C N   1 
ATOM   7039  C  CA  . ARG C  1 327 ? 45.732  15.340  26.267  1.00 25.69 ?  351  ARG C CA  1 
ATOM   7040  C  C   . ARG C  1 327 ? 46.614  16.474  26.803  1.00 25.47 ?  351  ARG C C   1 
ATOM   7041  O  O   . ARG C  1 327 ? 47.708  16.214  27.308  1.00 25.78 ?  351  ARG C O   1 
ATOM   7042  C  CB  . ARG C  1 327 ? 46.401  14.640  25.079  1.00 25.78 ?  351  ARG C CB  1 
ATOM   7043  C  CG  . ARG C  1 327 ? 45.842  13.240  24.816  1.00 26.76 ?  351  ARG C CG  1 
ATOM   7044  C  CD  . ARG C  1 327 ? 46.499  12.570  23.625  1.00 27.14 ?  351  ARG C CD  1 
ATOM   7045  N  NE  . ARG C  1 327 ? 46.157  13.230  22.365  1.00 28.84 ?  351  ARG C NE  1 
ATOM   7046  C  CZ  . ARG C  1 327 ? 46.309  12.683  21.161  1.00 29.32 ?  351  ARG C CZ  1 
ATOM   7047  N  NH1 . ARG C  1 327 ? 46.787  11.450  21.039  1.00 30.15 ?  351  ARG C NH1 1 
ATOM   7048  N  NH2 . ARG C  1 327 ? 45.974  13.367  20.074  1.00 29.44 ?  351  ARG C NH2 1 
ATOM   7049  N  N   . LYS C  1 328 ? 46.145  17.715  26.707  1.00 25.09 ?  352  LYS C N   1 
ATOM   7050  C  CA  . LYS C  1 328 ? 46.907  18.861  27.221  1.00 24.64 ?  352  LYS C CA  1 
ATOM   7051  C  C   . LYS C  1 328 ? 46.220  19.537  28.410  1.00 24.52 ?  352  LYS C C   1 
ATOM   7052  O  O   . LYS C  1 328 ? 46.678  20.575  28.893  1.00 24.48 ?  352  LYS C O   1 
ATOM   7053  C  CB  . LYS C  1 328 ? 47.187  19.882  26.111  1.00 24.43 ?  352  LYS C CB  1 
ATOM   7054  C  CG  . LYS C  1 328 ? 47.962  19.326  24.917  1.00 24.31 ?  352  LYS C CG  1 
ATOM   7055  C  CD  . LYS C  1 328 ? 48.300  20.403  23.890  1.00 23.57 ?  352  LYS C CD  1 
ATOM   7056  C  CE  . LYS C  1 328 ? 47.050  21.012  23.251  1.00 22.88 ?  352  LYS C CE  1 
ATOM   7057  N  NZ  . LYS C  1 328 ? 47.378  21.755  22.006  1.00 22.45 ?  352  LYS C NZ  1 
ATOM   7058  N  N   . THR C  1 329 ? 45.131  18.936  28.881  1.00 24.53 ?  353  THR C N   1 
ATOM   7059  C  CA  . THR C  1 329 ? 44.345  19.494  29.983  1.00 24.60 ?  353  THR C CA  1 
ATOM   7060  C  C   . THR C  1 329 ? 45.109  19.438  31.306  1.00 24.50 ?  353  THR C C   1 
ATOM   7061  O  O   . THR C  1 329 ? 45.571  18.374  31.715  1.00 24.56 ?  353  THR C O   1 
ATOM   7062  C  CB  . THR C  1 329 ? 42.983  18.771  30.131  1.00 24.59 ?  353  THR C CB  1 
ATOM   7063  O  OG1 . THR C  1 329 ? 42.284  18.802  28.879  1.00 25.33 ?  353  THR C OG1 1 
ATOM   7064  C  CG2 . THR C  1 329 ? 42.124  19.441  31.196  1.00 24.31 ?  353  THR C CG2 1 
ATOM   7065  N  N   . ARG C  1 330 ? 45.230  20.589  31.966  1.00 24.41 ?  354  ARG C N   1 
ATOM   7066  C  CA  . ARG C  1 330 ? 45.904  20.677  33.269  1.00 24.38 ?  354  ARG C CA  1 
ATOM   7067  C  C   . ARG C  1 330 ? 44.990  21.244  34.358  1.00 24.17 ?  354  ARG C C   1 
ATOM   7068  O  O   . ARG C  1 330 ? 44.897  20.685  35.451  1.00 24.23 ?  354  ARG C O   1 
ATOM   7069  C  CB  . ARG C  1 330 ? 47.166  21.540  33.173  1.00 24.38 ?  354  ARG C CB  1 
ATOM   7070  C  CG  . ARG C  1 330 ? 48.260  21.026  32.232  1.00 24.91 ?  354  ARG C CG  1 
ATOM   7071  C  CD  . ARG C  1 330 ? 49.515  21.888  32.365  1.00 25.83 ?  354  ARG C CD  1 
ATOM   7072  N  NE  . ARG C  1 330 ? 49.145  23.295  32.353  1.00 28.69 ?  354  ARG C NE  1 
ATOM   7073  C  CZ  . ARG C  1 330 ? 49.712  24.256  33.073  1.00 27.97 ?  354  ARG C CZ  1 
ATOM   7074  N  NH1 . ARG C  1 330 ? 50.733  24.016  33.890  1.00 27.74 ?  354  ARG C NH1 1 
ATOM   7075  N  NH2 . ARG C  1 330 ? 49.243  25.479  32.956  1.00 28.65 ?  354  ARG C NH2 1 
ATOM   7076  N  N   . TRP C  1 331 ? 44.327  22.359  34.054  1.00 24.04 ?  355  TRP C N   1 
ATOM   7077  C  CA  . TRP C  1 331 ? 43.471  23.052  35.021  1.00 23.68 ?  355  TRP C CA  1 
ATOM   7078  C  C   . TRP C  1 331 ? 42.031  22.560  35.025  1.00 23.50 ?  355  TRP C C   1 
ATOM   7079  O  O   . TRP C  1 331 ? 41.364  22.586  36.065  1.00 23.39 ?  355  TRP C O   1 
ATOM   7080  C  CB  . TRP C  1 331 ? 43.490  24.554  34.763  1.00 23.70 ?  355  TRP C CB  1 
ATOM   7081  C  CG  . TRP C  1 331 ? 44.667  25.237  35.360  1.00 23.58 ?  355  TRP C CG  1 
ATOM   7082  C  CD1 . TRP C  1 331 ? 45.751  25.727  34.697  1.00 23.08 ?  355  TRP C CD1 1 
ATOM   7083  C  CD2 . TRP C  1 331 ? 44.888  25.505  36.750  1.00 23.45 ?  355  TRP C CD2 1 
ATOM   7084  N  NE1 . TRP C  1 331 ? 46.631  26.293  35.585  1.00 23.66 ?  355  TRP C NE1 1 
ATOM   7085  C  CE2 . TRP C  1 331 ? 46.126  26.172  36.853  1.00 23.30 ?  355  TRP C CE2 1 
ATOM   7086  C  CE3 . TRP C  1 331 ? 44.157  25.249  37.919  1.00 23.52 ?  355  TRP C CE3 1 
ATOM   7087  C  CZ2 . TRP C  1 331 ? 46.659  26.580  38.080  1.00 23.07 ?  355  TRP C CZ2 1 
ATOM   7088  C  CZ3 . TRP C  1 331 ? 44.685  25.658  39.141  1.00 23.68 ?  355  TRP C CZ3 1 
ATOM   7089  C  CH2 . TRP C  1 331 ? 45.922  26.321  39.209  1.00 23.22 ?  355  TRP C CH2 1 
ATOM   7090  N  N   . ALA C  1 332 ? 41.565  22.123  33.857  1.00 23.33 ?  356  ALA C N   1 
ATOM   7091  C  CA  . ALA C  1 332 ? 40.192  21.637  33.652  1.00 23.27 ?  356  ALA C CA  1 
ATOM   7092  C  C   . ALA C  1 332 ? 39.091  22.589  34.148  1.00 23.16 ?  356  ALA C C   1 
ATOM   7093  O  O   . ALA C  1 332 ? 38.126  22.161  34.788  1.00 23.35 ?  356  ALA C O   1 
ATOM   7094  C  CB  . ALA C  1 332 ? 40.021  20.222  34.228  1.00 23.19 ?  356  ALA C CB  1 
ATOM   7095  N  N   . ASN C  1 333 ? 39.261  23.879  33.852  1.00 23.10 ?  357  ASN C N   1 
ATOM   7096  C  CA  . ASN C  1 333 ? 38.230  24.918  34.054  1.00 23.05 ?  357  ASN C CA  1 
ATOM   7097  C  C   . ASN C  1 333 ? 37.956  25.354  35.495  1.00 23.34 ?  357  ASN C C   1 
ATOM   7098  O  O   . ASN C  1 333 ? 37.911  26.554  35.770  1.00 23.32 ?  357  ASN C O   1 
ATOM   7099  C  CB  . ASN C  1 333 ? 36.915  24.547  33.350  1.00 22.90 ?  357  ASN C CB  1 
ATOM   7100  C  CG  . ASN C  1 333 ? 35.913  25.691  33.328  1.00 22.31 ?  357  ASN C CG  1 
ATOM   7101  O  OD1 . ASN C  1 333 ? 36.062  26.641  32.569  1.00 22.42 ?  357  ASN C OD1 1 
ATOM   7102  N  ND2 . ASN C  1 333 ? 34.880  25.594  34.155  1.00 21.22 ?  357  ASN C ND2 1 
ATOM   7103  N  N   . TYR C  1 334 ? 37.762  24.394  36.401  1.00 23.54 ?  358  TYR C N   1 
ATOM   7104  C  CA  . TYR C  1 334 ? 37.436  24.704  37.800  1.00 23.67 ?  358  TYR C CA  1 
ATOM   7105  C  C   . TYR C  1 334 ? 38.670  24.538  38.701  1.00 23.69 ?  358  TYR C C   1 
ATOM   7106  O  O   . TYR C  1 334 ? 39.020  23.418  39.081  1.00 23.85 ?  358  TYR C O   1 
ATOM   7107  C  CB  . TYR C  1 334 ? 36.270  23.838  38.307  1.00 23.71 ?  358  TYR C CB  1 
ATOM   7108  C  CG  . TYR C  1 334 ? 35.014  23.874  37.446  1.00 24.44 ?  358  TYR C CG  1 
ATOM   7109  C  CD1 . TYR C  1 334 ? 34.045  24.863  37.625  1.00 25.01 ?  358  TYR C CD1 1 
ATOM   7110  C  CD2 . TYR C  1 334 ? 34.790  22.906  36.463  1.00 24.83 ?  358  TYR C CD2 1 
ATOM   7111  C  CE1 . TYR C  1 334 ? 32.888  24.896  36.838  1.00 25.27 ?  358  TYR C CE1 1 
ATOM   7112  C  CE2 . TYR C  1 334 ? 33.637  22.927  35.672  1.00 25.58 ?  358  TYR C CE2 1 
ATOM   7113  C  CZ  . TYR C  1 334 ? 32.692  23.924  35.866  1.00 25.83 ?  358  TYR C CZ  1 
ATOM   7114  O  OH  . TYR C  1 334 ? 31.557  23.947  35.087  1.00 26.12 ?  358  TYR C OH  1 
ATOM   7115  N  N   . PRO C  1 335 ? 39.329  25.659  39.051  1.00 23.80 ?  359  PRO C N   1 
ATOM   7116  C  CA  . PRO C  1 335 ? 40.626  25.626  39.739  1.00 23.83 ?  359  PRO C CA  1 
ATOM   7117  C  C   . PRO C  1 335 ? 40.536  25.178  41.199  1.00 24.03 ?  359  PRO C C   1 
ATOM   7118  O  O   . PRO C  1 335 ? 41.561  24.864  41.808  1.00 23.80 ?  359  PRO C O   1 
ATOM   7119  C  CB  . PRO C  1 335 ? 41.093  27.087  39.678  1.00 23.63 ?  359  PRO C CB  1 
ATOM   7120  C  CG  . PRO C  1 335 ? 40.171  27.772  38.707  1.00 23.53 ?  359  PRO C CG  1 
ATOM   7121  C  CD  . PRO C  1 335 ? 38.881  27.044  38.830  1.00 23.53 ?  359  PRO C CD  1 
ATOM   7122  N  N   . PHE C  1 336 ? 39.318  25.157  41.736  1.00 24.28 ?  360  PHE C N   1 
ATOM   7123  C  CA  . PHE C  1 336 ? 39.061  24.802  43.132  1.00 24.77 ?  360  PHE C CA  1 
ATOM   7124  C  C   . PHE C  1 336 ? 38.881  23.300  43.361  1.00 24.98 ?  360  PHE C C   1 
ATOM   7125  O  O   . PHE C  1 336 ? 38.792  22.861  44.508  1.00 25.13 ?  360  PHE C O   1 
ATOM   7126  C  CB  . PHE C  1 336 ? 37.828  25.560  43.652  1.00 24.80 ?  360  PHE C CB  1 
ATOM   7127  C  CG  . PHE C  1 336 ? 36.571  25.289  42.868  1.00 25.14 ?  360  PHE C CG  1 
ATOM   7128  C  CD1 . PHE C  1 336 ? 35.710  24.257  43.240  1.00 25.86 ?  360  PHE C CD1 1 
ATOM   7129  C  CD2 . PHE C  1 336 ? 36.251  26.062  41.752  1.00 25.32 ?  360  PHE C CD2 1 
ATOM   7130  C  CE1 . PHE C  1 336 ? 34.546  23.996  42.513  1.00 26.14 ?  360  PHE C CE1 1 
ATOM   7131  C  CE2 . PHE C  1 336 ? 35.095  25.817  41.022  1.00 26.32 ?  360  PHE C CE2 1 
ATOM   7132  C  CZ  . PHE C  1 336 ? 34.237  24.777  41.399  1.00 26.33 ?  360  PHE C CZ  1 
ATOM   7133  N  N   . VAL C  1 337 ? 38.810  22.516  42.284  1.00 25.25 ?  361  VAL C N   1 
ATOM   7134  C  CA  . VAL C  1 337 ? 38.659  21.060  42.412  1.00 25.52 ?  361  VAL C CA  1 
ATOM   7135  C  C   . VAL C  1 337 ? 39.859  20.491  43.180  1.00 25.86 ?  361  VAL C C   1 
ATOM   7136  O  O   . VAL C  1 337 ? 41.008  20.732  42.794  1.00 25.69 ?  361  VAL C O   1 
ATOM   7137  C  CB  . VAL C  1 337 ? 38.475  20.359  41.036  1.00 25.48 ?  361  VAL C CB  1 
ATOM   7138  C  CG1 . VAL C  1 337 ? 38.674  18.839  41.148  1.00 25.62 ?  361  VAL C CG1 1 
ATOM   7139  C  CG2 . VAL C  1 337 ? 37.102  20.663  40.458  1.00 25.38 ?  361  VAL C CG2 1 
ATOM   7140  N  N   . PRO C  1 338 ? 39.596  19.765  44.290  1.00 26.05 ?  362  PRO C N   1 
ATOM   7141  C  CA  . PRO C  1 338 ? 40.683  19.233  45.120  1.00 26.15 ?  362  PRO C CA  1 
ATOM   7142  C  C   . PRO C  1 338 ? 41.715  18.447  44.315  1.00 26.22 ?  362  PRO C C   1 
ATOM   7143  O  O   . PRO C  1 338 ? 41.359  17.631  43.456  1.00 26.39 ?  362  PRO C O   1 
ATOM   7144  C  CB  . PRO C  1 338 ? 39.953  18.326  46.113  1.00 26.22 ?  362  PRO C CB  1 
ATOM   7145  C  CG  . PRO C  1 338 ? 38.605  18.974  46.258  1.00 26.18 ?  362  PRO C CG  1 
ATOM   7146  C  CD  . PRO C  1 338 ? 38.271  19.463  44.868  1.00 26.01 ?  362  PRO C CD  1 
ATOM   7147  N  N   . GLY C  1 339 ? 42.985  18.729  44.582  1.00 26.07 ?  363  GLY C N   1 
ATOM   7148  C  CA  . GLY C  1 339 ? 44.083  18.065  43.901  1.00 25.93 ?  363  GLY C CA  1 
ATOM   7149  C  C   . GLY C  1 339 ? 44.572  18.759  42.644  1.00 25.76 ?  363  GLY C C   1 
ATOM   7150  O  O   . GLY C  1 339 ? 45.654  18.435  42.153  1.00 25.92 ?  363  GLY C O   1 
ATOM   7151  N  N   . ILE C  1 340 ? 43.788  19.703  42.118  1.00 25.51 ?  364  ILE C N   1 
ATOM   7152  C  CA  . ILE C  1 340 ? 44.127  20.379  40.854  1.00 25.35 ?  364  ILE C CA  1 
ATOM   7153  C  C   . ILE C  1 340 ? 45.271  21.386  40.991  1.00 25.51 ?  364  ILE C C   1 
ATOM   7154  O  O   . ILE C  1 340 ? 46.235  21.343  40.223  1.00 25.57 ?  364  ILE C O   1 
ATOM   7155  C  CB  . ILE C  1 340 ? 42.883  21.030  40.167  1.00 25.34 ?  364  ILE C CB  1 
ATOM   7156  C  CG1 . ILE C  1 340 ? 41.881  19.955  39.713  1.00 24.66 ?  364  ILE C CG1 1 
ATOM   7157  C  CG2 . ILE C  1 340 ? 43.295  21.922  38.986  1.00 24.93 ?  364  ILE C CG2 1 
ATOM   7158  C  CD1 . ILE C  1 340 ? 42.356  19.065  38.560  1.00 24.53 ?  364  ILE C CD1 1 
ATOM   7159  N  N   . ALA C  1 341 ? 45.153  22.297  41.953  1.00 25.72 ?  365  ALA C N   1 
ATOM   7160  C  CA  . ALA C  1 341 ? 46.197  23.291  42.205  1.00 25.82 ?  365  ALA C CA  1 
ATOM   7161  C  C   . ALA C  1 341 ? 47.511  22.628  42.635  1.00 25.93 ?  365  ALA C C   1 
ATOM   7162  O  O   . ALA C  1 341 ? 48.586  22.991  42.152  1.00 25.53 ?  365  ALA C O   1 
ATOM   7163  C  CB  . ALA C  1 341 ? 45.737  24.291  43.247  1.00 25.69 ?  365  ALA C CB  1 
ATOM   7164  N  N   . GLU C  1 342 ? 47.406  21.647  43.531  1.00 26.19 ?  366  GLU C N   1 
ATOM   7165  C  CA  . GLU C  1 342 ? 48.567  20.906  44.039  1.00 26.69 ?  366  GLU C CA  1 
ATOM   7166  C  C   . GLU C  1 342 ? 49.296  20.137  42.925  1.00 26.87 ?  366  GLU C C   1 
ATOM   7167  O  O   . GLU C  1 342 ? 50.505  19.917  43.001  1.00 27.00 ?  366  GLU C O   1 
ATOM   7168  C  CB  . GLU C  1 342 ? 48.144  19.943  45.158  1.00 26.68 ?  366  GLU C CB  1 
ATOM   7169  C  CG  . GLU C  1 342 ? 47.564  20.613  46.415  1.00 27.50 ?  366  GLU C CG  1 
ATOM   7170  C  CD  . GLU C  1 342 ? 46.057  20.872  46.345  1.00 28.23 ?  366  GLU C CD  1 
ATOM   7171  O  OE1 . GLU C  1 342 ? 45.447  20.703  45.269  1.00 29.02 ?  366  GLU C OE1 1 
ATOM   7172  O  OE2 . GLU C  1 342 ? 45.473  21.248  47.380  1.00 29.00 -1 366  GLU C OE2 1 
ATOM   7173  N  N   . ASN C  1 343 ? 48.547  19.752  41.892  1.00 27.04 ?  367  ASN C N   1 
ATOM   7174  C  CA  . ASN C  1 343 ? 49.065  18.971  40.773  1.00 27.27 ?  367  ASN C CA  1 
ATOM   7175  C  C   . ASN C  1 343 ? 49.743  19.813  39.682  1.00 27.46 ?  367  ASN C C   1 
ATOM   7176  O  O   . ASN C  1 343 ? 50.389  19.265  38.786  1.00 27.12 ?  367  ASN C O   1 
ATOM   7177  C  CB  . ASN C  1 343 ? 47.933  18.116  40.175  1.00 27.25 ?  367  ASN C CB  1 
ATOM   7178  C  CG  . ASN C  1 343 ? 48.384  17.267  38.997  1.00 27.55 ?  367  ASN C CG  1 
ATOM   7179  O  OD1 . ASN C  1 343 ? 49.317  16.464  39.110  1.00 27.69 ?  367  ASN C OD1 1 
ATOM   7180  N  ND2 . ASN C  1 343 ? 47.724  17.446  37.854  1.00 26.63 ?  367  ASN C ND2 1 
ATOM   7181  N  N   . ILE C  1 344 ? 49.613  21.138  39.767  1.00 27.98 ?  368  ILE C N   1 
ATOM   7182  C  CA  . ILE C  1 344 ? 50.117  22.030  38.710  1.00 28.37 ?  368  ILE C CA  1 
ATOM   7183  C  C   . ILE C  1 344 ? 51.648  22.022  38.544  1.00 29.01 ?  368  ILE C C   1 
ATOM   7184  O  O   . ILE C  1 344 ? 52.161  22.401  37.489  1.00 29.18 ?  368  ILE C O   1 
ATOM   7185  C  CB  . ILE C  1 344 ? 49.550  23.480  38.837  1.00 28.35 ?  368  ILE C CB  1 
ATOM   7186  C  CG1 . ILE C  1 344 ? 49.374  24.114  37.451  1.00 27.86 ?  368  ILE C CG1 1 
ATOM   7187  C  CG2 . ILE C  1 344 ? 50.414  24.359  39.752  1.00 28.23 ?  368  ILE C CG2 1 
ATOM   7188  C  CD1 . ILE C  1 344 ? 48.294  23.460  36.604  1.00 26.74 ?  368  ILE C CD1 1 
ATOM   7189  N  N   . THR C  1 345 ? 52.362  21.580  39.580  1.00 29.71 ?  369  THR C N   1 
ATOM   7190  C  CA  . THR C  1 345 ? 53.827  21.523  39.560  1.00 30.20 ?  369  THR C CA  1 
ATOM   7191  C  C   . THR C  1 345 ? 54.378  20.153  39.140  1.00 30.42 ?  369  THR C C   1 
ATOM   7192  O  O   . THR C  1 345 ? 55.573  20.018  38.871  1.00 30.62 ?  369  THR C O   1 
ATOM   7193  C  CB  . THR C  1 345 ? 54.421  21.892  40.938  1.00 30.30 ?  369  THR C CB  1 
ATOM   7194  O  OG1 . THR C  1 345 ? 53.849  21.052  41.948  1.00 31.02 ?  369  THR C OG1 1 
ATOM   7195  C  CG2 . THR C  1 345 ? 54.137  23.350  41.280  1.00 30.40 ?  369  THR C CG2 1 
ATOM   7196  N  N   . SER C  1 346 ? 53.508  19.147  39.077  1.00 30.57 ?  370  SER C N   1 
ATOM   7197  C  CA  . SER C  1 346 ? 53.923  17.769  38.801  1.00 30.85 ?  370  SER C CA  1 
ATOM   7198  C  C   . SER C  1 346 ? 54.505  17.586  37.396  1.00 30.95 ?  370  SER C C   1 
ATOM   7199  O  O   . SER C  1 346 ? 54.261  18.401  36.500  1.00 31.07 ?  370  SER C O   1 
ATOM   7200  C  CB  . SER C  1 346 ? 52.756  16.799  39.028  1.00 30.79 ?  370  SER C CB  1 
ATOM   7201  O  OG  . SER C  1 346 ? 51.854  16.806  37.933  1.00 30.72 ?  370  SER C OG  1 
ATOM   7202  N  N   . ASP C  1 347 ? 55.276  16.514  37.217  1.00 30.92 ?  371  ASP C N   1 
ATOM   7203  C  CA  . ASP C  1 347 ? 55.857  16.171  35.912  1.00 31.04 ?  371  ASP C CA  1 
ATOM   7204  C  C   . ASP C  1 347 ? 54.776  15.879  34.873  1.00 30.56 ?  371  ASP C C   1 
ATOM   7205  O  O   . ASP C  1 347 ? 54.975  16.099  33.677  1.00 30.44 ?  371  ASP C O   1 
ATOM   7206  C  CB  . ASP C  1 347 ? 56.807  14.974  36.041  1.00 31.24 ?  371  ASP C CB  1 
ATOM   7207  C  CG  . ASP C  1 347 ? 58.038  15.290  36.883  1.00 32.25 ?  371  ASP C CG  1 
ATOM   7208  O  OD1 . ASP C  1 347 ? 58.536  16.436  36.820  1.00 32.79 ?  371  ASP C OD1 1 
ATOM   7209  O  OD2 . ASP C  1 347 ? 58.510  14.387  37.610  1.00 33.63 -1 371  ASP C OD2 1 
ATOM   7210  N  N   . TRP C  1 348 ? 53.638  15.384  35.353  1.00 30.09 ?  372  TRP C N   1 
ATOM   7211  C  CA  . TRP C  1 348 ? 52.453  15.142  34.534  1.00 29.74 ?  372  TRP C CA  1 
ATOM   7212  C  C   . TRP C  1 348 ? 51.926  16.449  33.940  1.00 29.45 ?  372  TRP C C   1 
ATOM   7213  O  O   . TRP C  1 348 ? 51.660  16.527  32.741  1.00 29.34 ?  372  TRP C O   1 
ATOM   7214  C  CB  . TRP C  1 348 ? 51.379  14.466  35.389  1.00 29.72 ?  372  TRP C CB  1 
ATOM   7215  C  CG  . TRP C  1 348 ? 50.147  14.017  34.653  1.00 29.89 ?  372  TRP C CG  1 
ATOM   7216  C  CD1 . TRP C  1 348 ? 49.949  12.807  34.046  1.00 29.89 ?  372  TRP C CD1 1 
ATOM   7217  C  CD2 . TRP C  1 348 ? 48.929  14.758  34.479  1.00 29.41 ?  372  TRP C CD2 1 
ATOM   7218  N  NE1 . TRP C  1 348 ? 48.691  12.754  33.494  1.00 29.86 ?  372  TRP C NE1 1 
ATOM   7219  C  CE2 . TRP C  1 348 ? 48.041  13.934  33.747  1.00 29.62 ?  372  TRP C CE2 1 
ATOM   7220  C  CE3 . TRP C  1 348 ? 48.504  16.038  34.865  1.00 29.20 ?  372  TRP C CE3 1 
ATOM   7221  C  CZ2 . TRP C  1 348 ? 46.752  14.348  33.394  1.00 28.94 ?  372  TRP C CZ2 1 
ATOM   7222  C  CZ3 . TRP C  1 348 ? 47.219  16.451  34.512  1.00 28.96 ?  372  TRP C CZ3 1 
ATOM   7223  C  CH2 . TRP C  1 348 ? 46.360  15.605  33.781  1.00 29.13 ?  372  TRP C CH2 1 
ATOM   7224  N  N   . SER C  1 349 ? 51.796  17.476  34.781  1.00 29.19 ?  373  SER C N   1 
ATOM   7225  C  CA  . SER C  1 349 ? 51.316  18.784  34.333  1.00 28.90 ?  373  SER C CA  1 
ATOM   7226  C  C   . SER C  1 349 ? 52.358  19.518  33.495  1.00 28.75 ?  373  SER C C   1 
ATOM   7227  O  O   . SER C  1 349 ? 52.011  20.222  32.541  1.00 28.63 ?  373  SER C O   1 
ATOM   7228  C  CB  . SER C  1 349 ? 50.891  19.644  35.521  1.00 28.81 ?  373  SER C CB  1 
ATOM   7229  O  OG  . SER C  1 349 ? 49.851  19.021  36.246  1.00 28.67 ?  373  SER C OG  1 
ATOM   7230  N  N   . GLU C  1 350 ? 53.631  19.341  33.843  1.00 28.49 ?  374  GLU C N   1 
ATOM   7231  C  CA  . GLU C  1 350 ? 54.724  19.986  33.114  1.00 28.35 ?  374  GLU C CA  1 
ATOM   7232  C  C   . GLU C  1 350 ? 54.875  19.439  31.697  1.00 27.76 ?  374  GLU C C   1 
ATOM   7233  O  O   . GLU C  1 350 ? 55.204  20.185  30.772  1.00 27.55 ?  374  GLU C O   1 
ATOM   7234  C  CB  . GLU C  1 350 ? 56.043  19.866  33.885  1.00 28.61 ?  374  GLU C CB  1 
ATOM   7235  C  CG  . GLU C  1 350 ? 57.107  20.879  33.466  1.00 30.39 ?  374  GLU C CG  1 
ATOM   7236  C  CD  . GLU C  1 350 ? 56.714  22.325  33.750  1.00 32.50 ?  374  GLU C CD  1 
ATOM   7237  O  OE1 . GLU C  1 350 ? 55.860  22.572  34.631  1.00 33.42 ?  374  GLU C OE1 1 
ATOM   7238  O  OE2 . GLU C  1 350 ? 57.271  23.225  33.090  1.00 34.41 -1 374  GLU C OE2 1 
ATOM   7239  N  N   . ALA C  1 351 ? 54.630  18.140  31.536  1.00 27.30 ?  375  ALA C N   1 
ATOM   7240  C  CA  . ALA C  1 351 ? 54.669  17.498  30.222  1.00 26.94 ?  375  ALA C CA  1 
ATOM   7241  C  C   . ALA C  1 351 ? 53.551  18.028  29.327  1.00 26.70 ?  375  ALA C C   1 
ATOM   7242  O  O   . ALA C  1 351 ? 53.754  18.250  28.128  1.00 26.40 ?  375  ALA C O   1 
ATOM   7243  C  CB  . ALA C  1 351 ? 54.570  15.983  30.359  1.00 27.07 ?  375  ALA C CB  1 
ATOM   7244  N  N   . ARG C  1 352 ? 52.374  18.230  29.921  1.00 26.28 ?  376  ARG C N   1 
ATOM   7245  C  CA  . ARG C  1 352 ? 51.225  18.773  29.202  1.00 26.08 ?  376  ARG C CA  1 
ATOM   7246  C  C   . ARG C  1 352 ? 51.430  20.252  28.870  1.00 25.87 ?  376  ARG C C   1 
ATOM   7247  O  O   . ARG C  1 352 ? 50.993  20.721  27.820  1.00 25.79 ?  376  ARG C O   1 
ATOM   7248  C  CB  . ARG C  1 352 ? 49.929  18.534  29.984  1.00 26.00 ?  376  ARG C CB  1 
ATOM   7249  C  CG  . ARG C  1 352 ? 49.402  17.116  29.810  1.00 26.07 ?  376  ARG C CG  1 
ATOM   7250  C  CD  . ARG C  1 352 ? 48.294  16.736  30.783  1.00 25.63 ?  376  ARG C CD  1 
ATOM   7251  N  NE  . ARG C  1 352 ? 47.795  15.402  30.457  1.00 25.65 ?  376  ARG C NE  1 
ATOM   7252  C  CZ  . ARG C  1 352 ? 46.527  15.091  30.190  1.00 25.08 ?  376  ARG C CZ  1 
ATOM   7253  N  NH1 . ARG C  1 352 ? 45.566  16.008  30.250  1.00 23.75 ?  376  ARG C NH1 1 
ATOM   7254  N  NH2 . ARG C  1 352 ? 46.217  13.836  29.888  1.00 24.39 ?  376  ARG C NH2 1 
ATOM   7255  N  N   . LEU C  1 353 ? 52.111  20.970  29.763  1.00 25.63 ?  377  LEU C N   1 
ATOM   7256  C  CA  . LEU C  1 353 ? 52.544  22.340  29.495  1.00 25.55 ?  377  LEU C CA  1 
ATOM   7257  C  C   . LEU C  1 353 ? 53.500  22.407  28.293  1.00 25.50 ?  377  LEU C C   1 
ATOM   7258  O  O   . LEU C  1 353 ? 53.325  23.253  27.412  1.00 25.61 ?  377  LEU C O   1 
ATOM   7259  C  CB  . LEU C  1 353 ? 53.193  22.960  30.736  1.00 25.58 ?  377  LEU C CB  1 
ATOM   7260  C  CG  . LEU C  1 353 ? 53.601  24.435  30.642  1.00 25.88 ?  377  LEU C CG  1 
ATOM   7261  C  CD1 . LEU C  1 353 ? 52.374  25.345  30.596  1.00 26.12 ?  377  LEU C CD1 1 
ATOM   7262  C  CD2 . LEU C  1 353 ? 54.512  24.821  31.795  1.00 25.25 ?  377  LEU C CD2 1 
ATOM   7263  N  N   . ASP C  1 354 ? 54.492  21.511  28.258  1.00 25.09 ?  378  ASP C N   1 
ATOM   7264  C  CA  . ASP C  1 354 ? 55.416  21.401  27.120  1.00 24.97 ?  378  ASP C CA  1 
ATOM   7265  C  C   . ASP C  1 354 ? 54.653  21.225  25.804  1.00 24.67 ?  378  ASP C C   1 
ATOM   7266  O  O   . ASP C  1 354 ? 55.007  21.828  24.789  1.00 24.57 ?  378  ASP C O   1 
ATOM   7267  C  CB  . ASP C  1 354 ? 56.390  20.225  27.298  1.00 24.94 ?  378  ASP C CB  1 
ATOM   7268  C  CG  . ASP C  1 354 ? 57.472  20.491  28.339  1.00 25.72 ?  378  ASP C CG  1 
ATOM   7269  O  OD1 . ASP C  1 354 ? 57.719  21.661  28.699  1.00 25.95 ?  378  ASP C OD1 1 
ATOM   7270  O  OD2 . ASP C  1 354 ? 58.094  19.508  28.791  1.00 27.10 -1 378  ASP C OD2 1 
ATOM   7271  N  N   . SER C  1 355 ? 53.608  20.398  25.835  1.00 24.37 ?  379  SER C N   1 
ATOM   7272  C  CA  . SER C  1 355 ? 52.758  20.175  24.668  1.00 24.13 ?  379  SER C CA  1 
ATOM   7273  C  C   . SER C  1 355 ? 52.036  21.460  24.253  1.00 23.80 ?  379  SER C C   1 
ATOM   7274  O  O   . SER C  1 355 ? 51.949  21.765  23.065  1.00 23.71 ?  379  SER C O   1 
ATOM   7275  C  CB  . SER C  1 355 ? 51.763  19.039  24.924  1.00 24.19 ?  379  SER C CB  1 
ATOM   7276  O  OG  . SER C  1 355 ? 52.432  17.792  25.036  1.00 24.71 ?  379  SER C OG  1 
ATOM   7277  N  N   . TRP C  1 356 ? 51.534  22.212  25.233  1.00 23.39 ?  380  TRP C N   1 
ATOM   7278  C  CA  . TRP C  1 356 ? 50.950  23.530  24.968  1.00 23.13 ?  380  TRP C CA  1 
ATOM   7279  C  C   . TRP C  1 356 ? 51.971  24.502  24.374  1.00 23.23 ?  380  TRP C C   1 
ATOM   7280  O  O   . TRP C  1 356 ? 51.664  25.233  23.431  1.00 23.07 ?  380  TRP C O   1 
ATOM   7281  C  CB  . TRP C  1 356 ? 50.346  24.136  26.237  1.00 22.79 ?  380  TRP C CB  1 
ATOM   7282  C  CG  . TRP C  1 356 ? 48.917  23.738  26.492  1.00 22.38 ?  380  TRP C CG  1 
ATOM   7283  C  CD1 . TRP C  1 356 ? 48.435  23.062  27.577  1.00 20.58 ?  380  TRP C CD1 1 
ATOM   7284  C  CD2 . TRP C  1 356 ? 47.788  23.997  25.646  1.00 21.48 ?  380  TRP C CD2 1 
ATOM   7285  N  NE1 . TRP C  1 356 ? 47.078  22.888  27.463  1.00 20.29 ?  380  TRP C NE1 1 
ATOM   7286  C  CE2 . TRP C  1 356 ? 46.654  23.452  26.287  1.00 21.28 ?  380  TRP C CE2 1 
ATOM   7287  C  CE3 . TRP C  1 356 ? 47.625  24.641  24.408  1.00 21.76 ?  380  TRP C CE3 1 
ATOM   7288  C  CZ2 . TRP C  1 356 ? 45.372  23.525  25.733  1.00 20.68 ?  380  TRP C CZ2 1 
ATOM   7289  C  CZ3 . TRP C  1 356 ? 46.349  24.715  23.858  1.00 21.03 ?  380  TRP C CZ3 1 
ATOM   7290  C  CH2 . TRP C  1 356 ? 45.241  24.157  24.522  1.00 21.46 ?  380  TRP C CH2 1 
ATOM   7291  N  N   . VAL C  1 357 ? 53.182  24.506  24.931  1.00 23.32 ?  381  VAL C N   1 
ATOM   7292  C  CA  . VAL C  1 357 ? 54.244  25.373  24.437  1.00 23.51 ?  381  VAL C CA  1 
ATOM   7293  C  C   . VAL C  1 357 ? 54.492  25.085  22.954  1.00 23.78 ?  381  VAL C C   1 
ATOM   7294  O  O   . VAL C  1 357 ? 54.607  26.010  22.149  1.00 23.88 ?  381  VAL C O   1 
ATOM   7295  C  CB  . VAL C  1 357 ? 55.537  25.244  25.288  1.00 23.55 ?  381  VAL C CB  1 
ATOM   7296  C  CG1 . VAL C  1 357 ? 56.713  25.947  24.617  1.00 23.20 ?  381  VAL C CG1 1 
ATOM   7297  C  CG2 . VAL C  1 357 ? 55.310  25.820  26.684  1.00 23.13 ?  381  VAL C CG2 1 
ATOM   7298  N  N   . LEU C  1 358 ? 54.534  23.804  22.599  1.00 24.03 ?  382  LEU C N   1 
ATOM   7299  C  CA  . LEU C  1 358 ? 54.632  23.383  21.201  1.00 24.53 ?  382  LEU C CA  1 
ATOM   7300  C  C   . LEU C  1 358 ? 53.510  23.995  20.345  1.00 24.25 ?  382  LEU C C   1 
ATOM   7301  O  O   . LEU C  1 358 ? 53.758  24.437  19.223  1.00 24.50 ?  382  LEU C O   1 
ATOM   7302  C  CB  . LEU C  1 358 ? 54.625  21.848  21.107  1.00 24.71 ?  382  LEU C CB  1 
ATOM   7303  C  CG  . LEU C  1 358 ? 54.982  21.090  19.813  1.00 26.28 ?  382  LEU C CG  1 
ATOM   7304  C  CD1 . LEU C  1 358 ? 53.812  21.015  18.828  1.00 27.62 ?  382  LEU C CD1 1 
ATOM   7305  C  CD2 . LEU C  1 358 ? 56.253  21.628  19.127  1.00 27.17 ?  382  LEU C CD2 1 
ATOM   7306  N  N   . THR C  1 359 ? 52.289  24.022  20.882  1.00 23.77 ?  383  THR C N   1 
ATOM   7307  C  CA  . THR C  1 359 ? 51.141  24.610  20.187  1.00 23.49 ?  383  THR C CA  1 
ATOM   7308  C  C   . THR C  1 359 ? 51.357  26.108  19.927  1.00 23.35 ?  383  THR C C   1 
ATOM   7309  O  O   . THR C  1 359 ? 51.196  26.573  18.799  1.00 23.15 ?  383  THR C O   1 
ATOM   7310  C  CB  . THR C  1 359 ? 49.820  24.397  20.980  1.00 23.55 ?  383  THR C CB  1 
ATOM   7311  O  OG1 . THR C  1 359 ? 49.684  23.014  21.331  1.00 23.42 ?  383  THR C OG1 1 
ATOM   7312  C  CG2 . THR C  1 359 ? 48.598  24.843  20.165  1.00 22.99 ?  383  THR C CG2 1 
ATOM   7313  N  N   . CYS C  1 360 ? 51.732  26.846  20.971  1.00 23.11 ?  384  CYS C N   1 
ATOM   7314  C  CA  . CYS C  1 360 ? 51.953  28.291  20.868  1.00 23.04 ?  384  CYS C CA  1 
ATOM   7315  C  C   . CYS C  1 360 ? 53.126  28.653  19.957  1.00 23.20 ?  384  CYS C C   1 
ATOM   7316  O  O   . CYS C  1 360 ? 53.068  29.652  19.237  1.00 22.95 ?  384  CYS C O   1 
ATOM   7317  C  CB  . CYS C  1 360 ? 52.171  28.907  22.253  1.00 22.92 ?  384  CYS C CB  1 
ATOM   7318  S  SG  . CYS C  1 360 ? 50.963  28.413  23.505  1.00 22.12 ?  384  CYS C SG  1 
ATOM   7319  N  N   . THR C  1 361 ? 54.176  27.830  19.982  1.00 23.49 ?  385  THR C N   1 
ATOM   7320  C  CA  . THR C  1 361 ? 55.414  28.125  19.244  1.00 23.65 ?  385  THR C CA  1 
ATOM   7321  C  C   . THR C  1 361 ? 55.342  27.871  17.737  1.00 23.92 ?  385  THR C C   1 
ATOM   7322  O  O   . THR C  1 361 ? 56.350  27.973  17.032  1.00 23.95 ?  385  THR C O   1 
ATOM   7323  C  CB  . THR C  1 361 ? 56.668  27.440  19.860  1.00 23.74 ?  385  THR C CB  1 
ATOM   7324  O  OG1 . THR C  1 361 ? 56.554  26.013  19.765  1.00 23.47 ?  385  THR C OG1 1 
ATOM   7325  C  CG2 . THR C  1 361 ? 56.839  27.853  21.314  1.00 23.10 ?  385  THR C CG2 1 
ATOM   7326  N  N   . GLN C  1 362 ? 54.147  27.552  17.244  1.00 24.14 ?  386  GLN C N   1 
ATOM   7327  C  CA  . GLN C  1 362 ? 53.885  27.592  15.807  1.00 24.28 ?  386  GLN C CA  1 
ATOM   7328  C  C   . GLN C  1 362 ? 53.922  29.045  15.345  1.00 24.07 ?  386  GLN C C   1 
ATOM   7329  O  O   . GLN C  1 362 ? 54.184  29.333  14.173  1.00 24.12 ?  386  GLN C O   1 
ATOM   7330  C  CB  . GLN C  1 362 ? 52.531  26.963  15.478  1.00 24.42 ?  386  GLN C CB  1 
ATOM   7331  C  CG  . GLN C  1 362 ? 52.439  25.480  15.817  1.00 25.39 ?  386  GLN C CG  1 
ATOM   7332  C  CD  . GLN C  1 362 ? 51.062  24.914  15.569  1.00 27.03 ?  386  GLN C CD  1 
ATOM   7333  O  OE1 . GLN C  1 362 ? 50.803  24.330  14.516  1.00 28.43 ?  386  GLN C OE1 1 
ATOM   7334  N  NE2 . GLN C  1 362 ? 50.161  25.094  16.532  1.00 27.48 ?  386  GLN C NE2 1 
ATOM   7335  N  N   . CYS C  1 363 ? 53.670  29.957  16.281  1.00 23.69 ?  387  CYS C N   1 
ATOM   7336  C  CA  . CYS C  1 363 ? 53.712  31.385  16.001  1.00 23.69 ?  387  CYS C CA  1 
ATOM   7337  C  C   . CYS C  1 363 ? 54.691  32.115  16.925  1.00 23.61 ?  387  CYS C C   1 
ATOM   7338  O  O   . CYS C  1 363 ? 55.690  32.656  16.455  1.00 23.47 ?  387  CYS C O   1 
ATOM   7339  C  CB  . CYS C  1 363 ? 52.309  31.993  16.090  1.00 23.80 ?  387  CYS C CB  1 
ATOM   7340  S  SG  . CYS C  1 363 ? 51.037  31.053  15.190  1.00 23.24 ?  387  CYS C SG  1 
ATOM   7341  N  N   . HIS C  1 364 ? 54.406  32.110  18.229  1.00 23.54 ?  388  HIS C N   1 
ATOM   7342  C  CA  . HIS C  1 364 ? 55.207  32.835  19.224  1.00 23.51 ?  388  HIS C CA  1 
ATOM   7343  C  C   . HIS C  1 364 ? 56.562  32.154  19.504  1.00 23.67 ?  388  HIS C C   1 
ATOM   7344  O  O   . HIS C  1 364 ? 56.752  30.973  19.198  1.00 23.60 ?  388  HIS C O   1 
ATOM   7345  C  CB  . HIS C  1 364 ? 54.429  33.001  20.548  1.00 23.45 ?  388  HIS C CB  1 
ATOM   7346  C  CG  . HIS C  1 364 ? 53.081  33.656  20.408  1.00 23.64 ?  388  HIS C CG  1 
ATOM   7347  N  ND1 . HIS C  1 364 ? 52.921  35.018  20.262  1.00 23.89 ?  388  HIS C ND1 1 
ATOM   7348  C  CD2 . HIS C  1 364 ? 51.828  33.136  20.435  1.00 23.21 ?  388  HIS C CD2 1 
ATOM   7349  C  CE1 . HIS C  1 364 ? 51.632  35.307  20.186  1.00 24.11 ?  388  HIS C CE1 1 
ATOM   7350  N  NE2 . HIS C  1 364 ? 50.944  34.183  20.293  1.00 23.74 ?  388  HIS C NE2 1 
ATOM   7351  N  N   . SER C  1 365 ? 57.502  32.901  20.081  1.00 23.66 ?  389  SER C N   1 
ATOM   7352  C  CA  . SER C  1 365 ? 58.724  32.296  20.603  1.00 23.75 ?  389  SER C CA  1 
ATOM   7353  C  C   . SER C  1 365 ? 58.396  31.520  21.871  1.00 23.85 ?  389  SER C C   1 
ATOM   7354  O  O   . SER C  1 365 ? 57.403  31.818  22.545  1.00 23.75 ?  389  SER C O   1 
ATOM   7355  C  CB  . SER C  1 365 ? 59.808  33.347  20.875  1.00 23.73 ?  389  SER C CB  1 
ATOM   7356  O  OG  . SER C  1 365 ? 59.464  34.213  21.945  1.00 23.39 ?  389  SER C OG  1 
ATOM   7357  N  N   . GLU C  1 366 ? 59.217  30.517  22.178  1.00 24.08 ?  390  GLU C N   1 
ATOM   7358  C  CA  . GLU C  1 366 ? 59.071  29.733  23.407  1.00 24.38 ?  390  GLU C CA  1 
ATOM   7359  C  C   . GLU C  1 366 ? 59.132  30.607  24.665  1.00 24.10 ?  390  GLU C C   1 
ATOM   7360  O  O   . GLU C  1 366 ? 58.342  30.424  25.594  1.00 24.33 ?  390  GLU C O   1 
ATOM   7361  C  CB  . GLU C  1 366 ? 60.128  28.623  23.468  1.00 24.60 ?  390  GLU C CB  1 
ATOM   7362  C  CG  . GLU C  1 366 ? 60.124  27.835  24.776  1.00 25.85 ?  390  GLU C CG  1 
ATOM   7363  C  CD  . GLU C  1 366 ? 60.767  26.467  24.657  1.00 27.72 ?  390  GLU C CD  1 
ATOM   7364  O  OE1 . GLU C  1 366 ? 61.380  26.171  23.607  1.00 28.99 ?  390  GLU C OE1 1 
ATOM   7365  O  OE2 . GLU C  1 366 ? 60.651  25.685  25.624  1.00 28.21 -1 390  GLU C OE2 1 
ATOM   7366  N  N   . ARG C  1 367 ? 60.065  31.557  24.677  1.00 23.72 ?  391  ARG C N   1 
ATOM   7367  C  CA  . ARG C  1 367 ? 60.232  32.489  25.794  1.00 23.42 ?  391  ARG C CA  1 
ATOM   7368  C  C   . ARG C  1 367 ? 58.942  33.275  26.045  1.00 23.11 ?  391  ARG C C   1 
ATOM   7369  O  O   . ARG C  1 367 ? 58.530  33.461  27.195  1.00 22.74 ?  391  ARG C O   1 
ATOM   7370  C  CB  . ARG C  1 367 ? 61.392  33.447  25.511  1.00 23.35 ?  391  ARG C CB  1 
ATOM   7371  C  CG  . ARG C  1 367 ? 61.969  34.155  26.735  1.00 23.71 ?  391  ARG C CG  1 
ATOM   7372  C  CD  . ARG C  1 367 ? 62.976  35.204  26.288  1.00 24.18 ?  391  ARG C CD  1 
ATOM   7373  N  NE  . ARG C  1 367 ? 63.711  35.817  27.391  1.00 24.41 ?  391  ARG C NE  1 
ATOM   7374  C  CZ  . ARG C  1 367 ? 64.502  36.880  27.258  1.00 24.71 ?  391  ARG C CZ  1 
ATOM   7375  N  NH1 . ARG C  1 367 ? 64.648  37.462  26.074  1.00 25.14 ?  391  ARG C NH1 1 
ATOM   7376  N  NH2 . ARG C  1 367 ? 65.139  37.373  28.311  1.00 24.29 ?  391  ARG C NH2 1 
ATOM   7377  N  N   . PHE C  1 368 ? 58.310  33.721  24.960  1.00 22.70 ?  392  PHE C N   1 
ATOM   7378  C  CA  . PHE C  1 368 ? 57.051  34.460  25.044  1.00 22.53 ?  392  PHE C CA  1 
ATOM   7379  C  C   . PHE C  1 368 ? 55.914  33.573  25.558  1.00 22.48 ?  392  PHE C C   1 
ATOM   7380  O  O   . PHE C  1 368 ? 55.202  33.948  26.494  1.00 22.31 ?  392  PHE C O   1 
ATOM   7381  C  CB  . PHE C  1 368 ? 56.683  35.069  23.688  1.00 22.32 ?  392  PHE C CB  1 
ATOM   7382  C  CG  . PHE C  1 368 ? 55.430  35.901  23.720  1.00 21.57 ?  392  PHE C CG  1 
ATOM   7383  C  CD1 . PHE C  1 368 ? 54.195  35.340  23.385  1.00 20.03 ?  392  PHE C CD1 1 
ATOM   7384  C  CD2 . PHE C  1 368 ? 55.482  37.243  24.092  1.00 19.82 ?  392  PHE C CD2 1 
ATOM   7385  C  CE1 . PHE C  1 368 ? 53.037  36.101  23.415  1.00 20.10 ?  392  PHE C CE1 1 
ATOM   7386  C  CE2 . PHE C  1 368 ? 54.326  38.016  24.127  1.00 19.79 ?  392  PHE C CE2 1 
ATOM   7387  C  CZ  . PHE C  1 368 ? 53.101  37.447  23.788  1.00 20.06 ?  392  PHE C CZ  1 
ATOM   7388  N  N   . ALA C  1 369 ? 55.766  32.402  24.943  1.00 22.32 ?  393  ALA C N   1 
ATOM   7389  C  CA  . ALA C  1 369 ? 54.717  31.455  25.294  1.00 22.42 ?  393  ALA C CA  1 
ATOM   7390  C  C   . ALA C  1 369 ? 54.791  31.048  26.764  1.00 22.57 ?  393  ALA C C   1 
ATOM   7391  O  O   . ALA C  1 369 ? 53.773  31.046  27.458  1.00 22.43 ?  393  ALA C O   1 
ATOM   7392  C  CB  . ALA C  1 369 ? 54.782  30.227  24.395  1.00 22.38 ?  393  ALA C CB  1 
ATOM   7393  N  N   . ARG C  1 370 ? 55.997  30.716  27.226  1.00 22.46 ?  394  ARG C N   1 
ATOM   7394  C  CA  . ARG C  1 370 ? 56.211  30.310  28.613  1.00 22.66 ?  394  ARG C CA  1 
ATOM   7395  C  C   . ARG C  1 370 ? 56.027  31.478  29.583  1.00 22.63 ?  394  ARG C C   1 
ATOM   7396  O  O   . ARG C  1 370 ? 55.551  31.284  30.701  1.00 22.57 ?  394  ARG C O   1 
ATOM   7397  C  CB  . ARG C  1 370 ? 57.586  29.650  28.794  1.00 22.86 ?  394  ARG C CB  1 
ATOM   7398  C  CG  . ARG C  1 370 ? 57.707  28.281  28.118  1.00 23.09 ?  394  ARG C CG  1 
ATOM   7399  C  CD  . ARG C  1 370 ? 59.037  27.607  28.426  1.00 24.06 ?  394  ARG C CD  1 
ATOM   7400  N  NE  . ARG C  1 370 ? 59.138  26.266  27.838  1.00 24.64 ?  394  ARG C NE  1 
ATOM   7401  C  CZ  . ARG C  1 370 ? 58.665  25.155  28.403  1.00 24.47 ?  394  ARG C CZ  1 
ATOM   7402  N  NH1 . ARG C  1 370 ? 58.039  25.207  29.572  1.00 23.92 ?  394  ARG C NH1 1 
ATOM   7403  N  NH2 . ARG C  1 370 ? 58.811  23.986  27.793  1.00 24.05 ?  394  ARG C NH2 1 
ATOM   7404  N  N   . SER C  1 371 ? 56.384  32.686  29.145  1.00 22.54 ?  395  SER C N   1 
ATOM   7405  C  CA  . SER C  1 371 ? 56.113  33.898  29.927  1.00 22.68 ?  395  SER C CA  1 
ATOM   7406  C  C   . SER C  1 371 ? 54.624  34.054  30.214  1.00 22.44 ?  395  SER C C   1 
ATOM   7407  O  O   . SER C  1 371 ? 54.231  34.295  31.362  1.00 22.52 ?  395  SER C O   1 
ATOM   7408  C  CB  . SER C  1 371 ? 56.645  35.152  29.228  1.00 22.51 ?  395  SER C CB  1 
ATOM   7409  O  OG  . SER C  1 371 ? 58.061  35.158  29.228  1.00 23.54 ?  395  SER C OG  1 
ATOM   7410  N  N   . TYR C  1 372 ? 53.796  33.906  29.180  1.00 22.04 ?  396  TYR C N   1 
ATOM   7411  C  CA  . TYR C  1 372 ? 52.358  34.042  29.369  1.00 21.94 ?  396  TYR C CA  1 
ATOM   7412  C  C   . TYR C  1 372 ? 51.706  32.883  30.128  1.00 21.97 ?  396  TYR C C   1 
ATOM   7413  O  O   . TYR C  1 372 ? 50.815  33.111  30.954  1.00 22.07 ?  396  TYR C O   1 
ATOM   7414  C  CB  . TYR C  1 372 ? 51.607  34.308  28.061  1.00 21.96 ?  396  TYR C CB  1 
ATOM   7415  C  CG  . TYR C  1 372 ? 50.172  34.648  28.349  1.00 21.99 ?  396  TYR C CG  1 
ATOM   7416  C  CD1 . TYR C  1 372 ? 49.815  35.923  28.800  1.00 21.80 ?  396  TYR C CD1 1 
ATOM   7417  C  CD2 . TYR C  1 372 ? 49.177  33.682  28.241  1.00 21.84 ?  396  TYR C CD2 1 
ATOM   7418  C  CE1 . TYR C  1 372 ? 48.492  36.231  29.102  1.00 22.24 ?  396  TYR C CE1 1 
ATOM   7419  C  CE2 . TYR C  1 372 ? 47.857  33.976  28.547  1.00 22.74 ?  396  TYR C CE2 1 
ATOM   7420  C  CZ  . TYR C  1 372 ? 47.520  35.248  28.972  1.00 22.21 ?  396  TYR C CZ  1 
ATOM   7421  O  OH  . TYR C  1 372 ? 46.211  35.529  29.266  1.00 22.98 ?  396  TYR C OH  1 
ATOM   7422  N  N   . LEU C  1 373 ? 52.128  31.651  29.845  1.00 21.85 ?  397  LEU C N   1 
ATOM   7423  C  CA  . LEU C  1 373 ? 51.542  30.487  30.511  1.00 22.08 ?  397  LEU C CA  1 
ATOM   7424  C  C   . LEU C  1 373 ? 51.857  30.483  32.011  1.00 22.20 ?  397  LEU C C   1 
ATOM   7425  O  O   . LEU C  1 373 ? 51.062  29.988  32.814  1.00 22.50 ?  397  LEU C O   1 
ATOM   7426  C  CB  . LEU C  1 373 ? 51.963  29.175  29.835  1.00 21.82 ?  397  LEU C CB  1 
ATOM   7427  C  CG  . LEU C  1 373 ? 51.451  28.931  28.403  1.00 22.10 ?  397  LEU C CG  1 
ATOM   7428  C  CD1 . LEU C  1 373 ? 52.180  27.768  27.743  1.00 21.22 ?  397  LEU C CD1 1 
ATOM   7429  C  CD2 . LEU C  1 373 ? 49.931  28.724  28.337  1.00 22.51 ?  397  LEU C CD2 1 
ATOM   7430  N  N   . ASP C  1 374 ? 53.004  31.057  32.373  1.00 22.08 ?  398  ASP C N   1 
ATOM   7431  C  CA  . ASP C  1 374 ? 53.374  31.279  33.771  1.00 22.30 ?  398  ASP C CA  1 
ATOM   7432  C  C   . ASP C  1 374 ? 52.425  32.288  34.418  1.00 22.07 ?  398  ASP C C   1 
ATOM   7433  O  O   . ASP C  1 374 ? 52.010  32.115  35.566  1.00 21.98 ?  398  ASP C O   1 
ATOM   7434  C  CB  . ASP C  1 374 ? 54.816  31.785  33.874  1.00 22.22 ?  398  ASP C CB  1 
ATOM   7435  C  CG  . ASP C  1 374 ? 55.284  31.919  35.307  1.00 23.61 ?  398  ASP C CG  1 
ATOM   7436  O  OD1 . ASP C  1 374 ? 55.422  33.064  35.795  1.00 24.70 ?  398  ASP C OD1 1 
ATOM   7437  O  OD2 . ASP C  1 374 ? 55.494  30.876  35.956  1.00 25.89 -1 398  ASP C OD2 1 
ATOM   7438  N  N   . LEU C  1 375 ? 52.098  33.342  33.673  1.00 21.81 ?  399  LEU C N   1 
ATOM   7439  C  CA  . LEU C  1 375 ? 51.115  34.328  34.107  1.00 21.94 ?  399  LEU C CA  1 
ATOM   7440  C  C   . LEU C  1 375 ? 49.742  33.676  34.318  1.00 21.80 ?  399  LEU C C   1 
ATOM   7441  O  O   . LEU C  1 375 ? 49.082  33.936  35.325  1.00 21.87 ?  399  LEU C O   1 
ATOM   7442  C  CB  . LEU C  1 375 ? 51.029  35.484  33.098  1.00 21.68 ?  399  LEU C CB  1 
ATOM   7443  C  CG  . LEU C  1 375 ? 50.163  36.704  33.432  1.00 21.99 ?  399  LEU C CG  1 
ATOM   7444  C  CD1 . LEU C  1 375 ? 50.678  37.940  32.711  1.00 21.95 ?  399  LEU C CD1 1 
ATOM   7445  C  CD2 . LEU C  1 375 ? 48.695  36.461  33.087  1.00 22.00 ?  399  LEU C CD2 1 
ATOM   7446  N  N   . MET C  1 376 ? 49.327  32.837  33.366  1.00 21.78 ?  400  MET C N   1 
ATOM   7447  C  CA  . MET C  1 376 ? 48.057  32.099  33.456  1.00 21.78 ?  400  MET C CA  1 
ATOM   7448  C  C   . MET C  1 376 ? 47.967  31.252  34.728  1.00 21.88 ?  400  MET C C   1 
ATOM   7449  O  O   . MET C  1 376 ? 46.961  31.308  35.439  1.00 21.96 ?  400  MET C O   1 
ATOM   7450  C  CB  . MET C  1 376 ? 47.843  31.211  32.216  1.00 21.57 ?  400  MET C CB  1 
ATOM   7451  C  CG  . MET C  1 376 ? 46.632  30.279  32.297  1.00 20.98 ?  400  MET C CG  1 
ATOM   7452  S  SD  . MET C  1 376 ? 46.566  29.036  30.982  1.00 20.27 ?  400  MET C SD  1 
ATOM   7453  C  CE  . MET C  1 376 ? 47.870  27.917  31.495  1.00 19.52 ?  400  MET C CE  1 
ATOM   7454  N  N   . ASP C  1 377 ? 49.012  30.469  34.997  1.00 21.84 ?  401  ASP C N   1 
ATOM   7455  C  CA  . ASP C  1 377 ? 49.045  29.581  36.164  1.00 22.01 ?  401  ASP C CA  1 
ATOM   7456  C  C   . ASP C  1 377 ? 48.978  30.352  37.480  1.00 21.93 ?  401  ASP C C   1 
ATOM   7457  O  O   . ASP C  1 377 ? 48.202  30.003  38.370  1.00 21.78 ?  401  ASP C O   1 
ATOM   7458  C  CB  . ASP C  1 377 ? 50.300  28.695  36.147  1.00 21.98 ?  401  ASP C CB  1 
ATOM   7459  C  CG  . ASP C  1 377 ? 50.211  27.566  35.132  1.00 22.69 ?  401  ASP C CG  1 
ATOM   7460  O  OD1 . ASP C  1 377 ? 49.092  27.244  34.673  1.00 21.82 ?  401  ASP C OD1 1 
ATOM   7461  O  OD2 . ASP C  1 377 ? 51.269  26.993  34.793  1.00 23.54 -1 401  ASP C OD2 1 
ATOM   7462  N  N   . LYS C  1 378 ? 49.794  31.399  37.588  1.00 22.03 ?  402  LYS C N   1 
ATOM   7463  C  CA  . LYS C  1 378 ? 49.890  32.188  38.816  1.00 22.05 ?  402  LYS C CA  1 
ATOM   7464  C  C   . LYS C  1 378 ? 48.658  33.056  39.049  1.00 21.77 ?  402  LYS C C   1 
ATOM   7465  O  O   . LYS C  1 378 ? 48.187  33.179  40.181  1.00 21.64 ?  402  LYS C O   1 
ATOM   7466  C  CB  . LYS C  1 378 ? 51.171  33.030  38.826  1.00 22.00 ?  402  LYS C CB  1 
ATOM   7467  C  CG  . LYS C  1 378 ? 52.422  32.213  39.112  1.00 22.91 ?  402  LYS C CG  1 
ATOM   7468  C  CD  . LYS C  1 378 ? 53.681  33.062  39.077  1.00 23.47 ?  402  LYS C CD  1 
ATOM   7469  C  CE  . LYS C  1 378 ? 54.922  32.187  39.108  1.00 23.36 ?  402  LYS C CE  1 
ATOM   7470  N  NZ  . LYS C  1 378 ? 56.111  32.916  38.578  1.00 24.30 ?  402  LYS C NZ  1 
ATOM   7471  N  N   . GLY C  1 379 ? 48.138  33.648  37.976  1.00 21.58 ?  403  GLY C N   1 
ATOM   7472  C  CA  . GLY C  1 379 ? 46.895  34.422  38.045  1.00 21.43 ?  403  GLY C CA  1 
ATOM   7473  C  C   . GLY C  1 379 ? 45.717  33.582  38.507  1.00 21.19 ?  403  GLY C C   1 
ATOM   7474  O  O   . GLY C  1 379 ? 44.875  34.045  39.277  1.00 21.18 ?  403  GLY C O   1 
ATOM   7475  N  N   . THR C  1 380 ? 45.664  32.340  38.033  1.00 21.04 ?  404  THR C N   1 
ATOM   7476  C  CA  . THR C  1 380 ? 44.623  31.393  38.433  1.00 20.90 ?  404  THR C CA  1 
ATOM   7477  C  C   . THR C  1 380 ? 44.683  31.096  39.936  1.00 21.03 ?  404  THR C C   1 
ATOM   7478  O  O   . THR C  1 380 ? 43.657  31.110  40.623  1.00 21.02 ?  404  THR C O   1 
ATOM   7479  C  CB  . THR C  1 380 ? 44.738  30.085  37.628  1.00 20.87 ?  404  THR C CB  1 
ATOM   7480  O  OG1 . THR C  1 380 ? 44.565  30.368  36.232  1.00 20.47 ?  404  THR C OG1 1 
ATOM   7481  C  CG2 . THR C  1 380 ? 43.687  29.069  38.073  1.00 20.84 ?  404  THR C CG2 1 
ATOM   7482  N  N   . LEU C  1 381 ? 45.890  30.838  40.436  1.00 21.06 ?  405  LEU C N   1 
ATOM   7483  C  CA  . LEU C  1 381 ? 46.099  30.538  41.850  1.00 21.21 ?  405  LEU C CA  1 
ATOM   7484  C  C   . LEU C  1 381 ? 45.772  31.730  42.743  1.00 21.26 ?  405  LEU C C   1 
ATOM   7485  O  O   . LEU C  1 381 ? 45.242  31.558  43.841  1.00 21.41 ?  405  LEU C O   1 
ATOM   7486  C  CB  . LEU C  1 381 ? 47.537  30.072  42.095  1.00 20.87 ?  405  LEU C CB  1 
ATOM   7487  C  CG  . LEU C  1 381 ? 47.900  28.658  41.652  1.00 21.20 ?  405  LEU C CG  1 
ATOM   7488  C  CD1 . LEU C  1 381 ? 49.415  28.470  41.643  1.00 21.05 ?  405  LEU C CD1 1 
ATOM   7489  C  CD2 . LEU C  1 381 ? 47.224  27.618  42.542  1.00 20.30 ?  405  LEU C CD2 1 
ATOM   7490  N  N   . GLU C  1 382 ? 46.098  32.930  42.261  1.00 21.34 ?  406  GLU C N   1 
ATOM   7491  C  CA  . GLU C  1 382 ? 45.769  34.182  42.947  1.00 21.38 ?  406  GLU C CA  1 
ATOM   7492  C  C   . GLU C  1 382 ? 44.261  34.330  43.131  1.00 21.36 ?  406  GLU C C   1 
ATOM   7493  O  O   . GLU C  1 382 ? 43.794  34.735  44.196  1.00 21.40 ?  406  GLU C O   1 
ATOM   7494  C  CB  . GLU C  1 382 ? 46.356  35.382  42.185  1.00 21.51 ?  406  GLU C CB  1 
ATOM   7495  C  CG  . GLU C  1 382 ? 47.857  35.570  42.411  1.00 21.59 ?  406  GLU C CG  1 
ATOM   7496  C  CD  . GLU C  1 382 ? 48.580  36.265  41.258  1.00 22.48 ?  406  GLU C CD  1 
ATOM   7497  O  OE1 . GLU C  1 382 ? 47.970  37.098  40.550  1.00 21.74 ?  406  GLU C OE1 1 
ATOM   7498  O  OE2 . GLU C  1 382 ? 49.783  35.976  41.073  1.00 22.55 -1 406  GLU C OE2 1 
ATOM   7499  N  N   . GLY C  1 383 ? 43.504  33.986  42.091  1.00 21.34 ?  407  GLY C N   1 
ATOM   7500  C  CA  . GLY C  1 383 ? 42.050  33.934  42.187  1.00 21.22 ?  407  GLY C CA  1 
ATOM   7501  C  C   . GLY C  1 383 ? 41.590  32.918  43.216  1.00 21.28 ?  407  GLY C C   1 
ATOM   7502  O  O   . GLY C  1 383 ? 40.722  33.208  44.040  1.00 21.13 ?  407  GLY C O   1 
ATOM   7503  N  N   . LEU C  1 384 ? 42.182  31.727  43.168  1.00 21.42 ?  408  LEU C N   1 
ATOM   7504  C  CA  . LEU C  1 384 ? 41.844  30.641  44.087  1.00 21.84 ?  408  LEU C CA  1 
ATOM   7505  C  C   . LEU C  1 384 ? 42.095  31.019  45.549  1.00 22.05 ?  408  LEU C C   1 
ATOM   7506  O  O   . LEU C  1 384 ? 41.272  30.726  46.415  1.00 22.23 ?  408  LEU C O   1 
ATOM   7507  C  CB  . LEU C  1 384 ? 42.606  29.361  43.714  1.00 21.94 ?  408  LEU C CB  1 
ATOM   7508  C  CG  . LEU C  1 384 ? 42.422  28.090  44.555  1.00 22.27 ?  408  LEU C CG  1 
ATOM   7509  C  CD1 . LEU C  1 384 ? 40.972  27.600  44.572  1.00 21.12 ?  408  LEU C CD1 1 
ATOM   7510  C  CD2 . LEU C  1 384 ? 43.348  27.008  44.038  1.00 22.55 ?  408  LEU C CD2 1 
ATOM   7511  N  N   . ALA C  1 385 ? 43.219  31.687  45.810  1.00 22.16 ?  409  ALA C N   1 
ATOM   7512  C  CA  . ALA C  1 385 ? 43.538  32.169  47.155  1.00 22.30 ?  409  ALA C CA  1 
ATOM   7513  C  C   . ALA C  1 385 ? 42.482  33.140  47.684  1.00 22.36 ?  409  ALA C C   1 
ATOM   7514  O  O   . ALA C  1 385 ? 42.122  33.086  48.861  1.00 22.21 ?  409  ALA C O   1 
ATOM   7515  C  CB  . ALA C  1 385 ? 44.921  32.813  47.184  1.00 22.18 ?  409  ALA C CB  1 
ATOM   7516  N  N   . LYS C  1 386 ? 41.988  34.016  46.807  1.00 22.50 ?  410  LYS C N   1 
ATOM   7517  C  CA  . LYS C  1 386 ? 40.945  34.977  47.170  1.00 22.67 ?  410  LYS C CA  1 
ATOM   7518  C  C   . LYS C  1 386 ? 39.665  34.265  47.605  1.00 22.87 ?  410  LYS C C   1 
ATOM   7519  O  O   . LYS C  1 386 ? 39.077  34.612  48.633  1.00 22.71 ?  410  LYS C O   1 
ATOM   7520  C  CB  . LYS C  1 386 ? 40.664  35.944  46.011  1.00 22.63 ?  410  LYS C CB  1 
ATOM   7521  C  CG  . LYS C  1 386 ? 39.826  37.170  46.387  1.00 22.71 ?  410  LYS C CG  1 
ATOM   7522  C  CD  . LYS C  1 386 ? 40.584  38.111  47.321  1.00 23.00 ?  410  LYS C CD  1 
ATOM   7523  C  CE  . LYS C  1 386 ? 39.794  39.386  47.597  1.00 22.68 ?  410  LYS C CE  1 
ATOM   7524  N  NZ  . LYS C  1 386 ? 40.427  40.185  48.682  1.00 21.94 ?  410  LYS C NZ  1 
ATOM   7525  N  N   . TYR C  1 387 ? 39.253  33.263  46.825  1.00 23.06 ?  411  TYR C N   1 
ATOM   7526  C  CA  . TYR C  1 387 ? 38.083  32.452  47.151  1.00 23.34 ?  411  TYR C CA  1 
ATOM   7527  C  C   . TYR C  1 387 ? 38.286  31.659  48.440  1.00 23.68 ?  411  TYR C C   1 
ATOM   7528  O  O   . TYR C  1 387 ? 37.393  31.615  49.282  1.00 23.76 ?  411  TYR C O   1 
ATOM   7529  C  CB  . TYR C  1 387 ? 37.712  31.498  45.999  1.00 23.09 ?  411  TYR C CB  1 
ATOM   7530  C  CG  . TYR C  1 387 ? 36.982  30.252  46.467  1.00 22.67 ?  411  TYR C CG  1 
ATOM   7531  C  CD1 . TYR C  1 387 ? 35.675  30.325  46.959  1.00 22.35 ?  411  TYR C CD1 1 
ATOM   7532  C  CD2 . TYR C  1 387 ? 37.613  29.005  46.452  1.00 22.56 ?  411  TYR C CD2 1 
ATOM   7533  C  CE1 . TYR C  1 387 ? 35.013  29.189  47.414  1.00 22.75 ?  411  TYR C CE1 1 
ATOM   7534  C  CE2 . TYR C  1 387 ? 36.959  27.864  46.895  1.00 22.70 ?  411  TYR C CE2 1 
ATOM   7535  C  CZ  . TYR C  1 387 ? 35.659  27.961  47.373  1.00 23.37 ?  411  TYR C CZ  1 
ATOM   7536  O  OH  . TYR C  1 387 ? 35.008  26.830  47.809  1.00 24.28 ?  411  TYR C OH  1 
ATOM   7537  N  N   . GLN C  1 388 ? 39.449  31.024  48.576  1.00 24.15 ?  412  GLN C N   1 
ATOM   7538  C  CA  . GLN C  1 388 ? 39.743  30.199  49.749  1.00 24.57 ?  412  GLN C CA  1 
ATOM   7539  C  C   . GLN C  1 388 ? 39.633  30.982  51.057  1.00 24.88 ?  412  GLN C C   1 
ATOM   7540  O  O   . GLN C  1 388 ? 39.125  30.461  52.050  1.00 24.87 ?  412  GLN C O   1 
ATOM   7541  C  CB  . GLN C  1 388 ? 41.114  29.524  49.624  1.00 24.53 ?  412  GLN C CB  1 
ATOM   7542  C  CG  . GLN C  1 388 ? 41.146  28.347  48.627  1.00 24.13 ?  412  GLN C CG  1 
ATOM   7543  C  CD  . GLN C  1 388 ? 42.537  27.769  48.440  1.00 23.89 ?  412  GLN C CD  1 
ATOM   7544  O  OE1 . GLN C  1 388 ? 43.545  28.419  48.735  1.00 24.21 ?  412  GLN C OE1 1 
ATOM   7545  N  NE2 . GLN C  1 388 ? 42.600  26.538  47.950  1.00 24.05 ?  412  GLN C NE2 1 
ATOM   7546  N  N   . GLU C  1 389 ? 40.093  32.234  51.047  1.00 25.32 ?  413  GLU C N   1 
ATOM   7547  C  CA  . GLU C  1 389 ? 39.968  33.095  52.220  1.00 25.87 ?  413  GLU C CA  1 
ATOM   7548  C  C   . GLU C  1 389 ? 38.499  33.369  52.552  1.00 26.02 ?  413  GLU C C   1 
ATOM   7549  O  O   . GLU C  1 389 ? 38.100  33.281  53.711  1.00 25.92 ?  413  GLU C O   1 
ATOM   7550  C  CB  . GLU C  1 389 ? 40.731  34.412  52.046  1.00 25.96 ?  413  GLU C CB  1 
ATOM   7551  C  CG  . GLU C  1 389 ? 40.796  35.228  53.348  1.00 26.59 ?  413  GLU C CG  1 
ATOM   7552  C  CD  . GLU C  1 389 ? 41.605  36.505  53.236  1.00 27.99 ?  413  GLU C CD  1 
ATOM   7553  O  OE1 . GLU C  1 389 ? 42.575  36.549  52.446  1.00 27.65 ?  413  GLU C OE1 1 
ATOM   7554  O  OE2 . GLU C  1 389 ? 41.267  37.469  53.959  1.00 28.78 -1 413  GLU C OE2 1 
ATOM   7555  N  N   . ALA C  1 390 ? 37.708  33.689  51.529  1.00 26.26 ?  414  ALA C N   1 
ATOM   7556  C  CA  . ALA C  1 390 ? 36.283  33.960  51.700  1.00 26.64 ?  414  ALA C CA  1 
ATOM   7557  C  C   . ALA C  1 390 ? 35.526  32.708  52.143  1.00 26.95 ?  414  ALA C C   1 
ATOM   7558  O  O   . ALA C  1 390 ? 34.645  32.779  53.004  1.00 27.02 ?  414  ALA C O   1 
ATOM   7559  C  CB  . ALA C  1 390 ? 35.688  34.531  50.414  1.00 26.22 ?  414  ALA C CB  1 
ATOM   7560  N  N   . ASN C  1 391 ? 35.886  31.569  51.553  1.00 27.43 ?  415  ASN C N   1 
ATOM   7561  C  CA  . ASN C  1 391 ? 35.307  30.274  51.908  1.00 28.07 ?  415  ASN C CA  1 
ATOM   7562  C  C   . ASN C  1 391 ? 35.558  29.869  53.366  1.00 28.25 ?  415  ASN C C   1 
ATOM   7563  O  O   . ASN C  1 391 ? 34.719  29.208  53.977  1.00 28.09 ?  415  ASN C O   1 
ATOM   7564  C  CB  . ASN C  1 391 ? 35.810  29.180  50.960  1.00 28.09 ?  415  ASN C CB  1 
ATOM   7565  C  CG  . ASN C  1 391 ? 35.106  27.851  51.173  1.00 29.10 ?  415  ASN C CG  1 
ATOM   7566  O  OD1 . ASN C  1 391 ? 33.915  27.714  50.895  1.00 30.84 ?  415  ASN C OD1 1 
ATOM   7567  N  ND2 . ASN C  1 391 ? 35.842  26.866  51.673  1.00 29.82 ?  415  ASN C ND2 1 
ATOM   7568  N  N   . ALA C  1 392 ? 36.705  30.273  53.915  1.00 28.45 ?  416  ALA C N   1 
ATOM   7569  C  CA  . ALA C  1 392 ? 37.041  29.977  55.311  1.00 28.94 ?  416  ALA C CA  1 
ATOM   7570  C  C   . ALA C  1 392 ? 36.022  30.598  56.268  1.00 29.19 ?  416  ALA C C   1 
ATOM   7571  O  O   . ALA C  1 392 ? 35.682  30.006  57.293  1.00 29.18 ?  416  ALA C O   1 
ATOM   7572  C  CB  . ALA C  1 392 ? 38.457  30.455  55.643  1.00 28.82 ?  416  ALA C CB  1 
ATOM   7573  N  N   . ILE C  1 393 ? 35.534  31.784  55.907  1.00 29.53 ?  417  ILE C N   1 
ATOM   7574  C  CA  . ILE C  1 393 ? 34.549  32.519  56.696  1.00 29.73 ?  417  ILE C CA  1 
ATOM   7575  C  C   . ILE C  1 393 ? 33.194  31.811  56.698  1.00 29.97 ?  417  ILE C C   1 
ATOM   7576  O  O   . ILE C  1 393 ? 32.665  31.472  57.763  1.00 30.07 ?  417  ILE C O   1 
ATOM   7577  C  CB  . ILE C  1 393 ? 34.406  33.974  56.180  1.00 29.75 ?  417  ILE C CB  1 
ATOM   7578  C  CG1 . ILE C  1 393 ? 35.722  34.736  56.388  1.00 29.91 ?  417  ILE C CG1 1 
ATOM   7579  C  CG2 . ILE C  1 393 ? 33.243  34.691  56.866  1.00 29.45 ?  417  ILE C CG2 1 
ATOM   7580  C  CD1 . ILE C  1 393 ? 35.930  35.901  55.450  1.00 29.68 ?  417  ILE C CD1 1 
ATOM   7581  N  N   . VAL C  1 394 ? 32.654  31.576  55.505  1.00 30.19 ?  418  VAL C N   1 
ATOM   7582  C  CA  . VAL C  1 394 ? 31.327  30.985  55.350  1.00 30.36 ?  418  VAL C CA  1 
ATOM   7583  C  C   . VAL C  1 394 ? 31.290  29.541  55.860  1.00 30.73 ?  418  VAL C C   1 
ATOM   7584  O  O   . VAL C  1 394 ? 30.304  29.125  56.474  1.00 30.63 ?  418  VAL C O   1 
ATOM   7585  C  CB  . VAL C  1 394 ? 30.813  31.071  53.883  1.00 30.28 ?  418  VAL C CB  1 
ATOM   7586  C  CG1 . VAL C  1 394 ? 29.321  30.735  53.809  1.00 29.65 ?  418  VAL C CG1 1 
ATOM   7587  C  CG2 . VAL C  1 394 ? 31.060  32.465  53.305  1.00 29.62 ?  418  VAL C CG2 1 
ATOM   7588  N  N   . HIS C  1 395 ? 32.366  28.792  55.626  1.00 31.26 ?  419  HIS C N   1 
ATOM   7589  C  CA  . HIS C  1 395 ? 32.460  27.412  56.111  1.00 32.04 ?  419  HIS C CA  1 
ATOM   7590  C  C   . HIS C  1 395 ? 32.495  27.336  57.645  1.00 32.23 ?  419  HIS C C   1 
ATOM   7591  O  O   . HIS C  1 395 ? 31.915  26.424  58.232  1.00 32.17 ?  419  HIS C O   1 
ATOM   7592  C  CB  . HIS C  1 395 ? 33.655  26.677  55.495  1.00 32.02 ?  419  HIS C CB  1 
ATOM   7593  C  CG  . HIS C  1 395 ? 33.771  25.247  55.924  1.00 33.35 ?  419  HIS C CG  1 
ATOM   7594  N  ND1 . HIS C  1 395 ? 32.945  24.254  55.439  1.00 34.22 ?  419  HIS C ND1 1 
ATOM   7595  C  CD2 . HIS C  1 395 ? 34.610  24.644  56.800  1.00 34.08 ?  419  HIS C CD2 1 
ATOM   7596  C  CE1 . HIS C  1 395 ? 33.273  23.101  55.996  1.00 34.17 ?  419  HIS C CE1 1 
ATOM   7597  N  NE2 . HIS C  1 395 ? 34.281  23.310  56.824  1.00 34.73 ?  419  HIS C NE2 1 
ATOM   7598  N  N   . LYS C  1 396 ? 33.161  28.300  58.280  1.00 32.76 ?  420  LYS C N   1 
ATOM   7599  C  CA  . LYS C  1 396 ? 33.180  28.403  59.743  1.00 33.39 ?  420  LYS C CA  1 
ATOM   7600  C  C   . LYS C  1 396 ? 31.767  28.632  60.295  1.00 33.51 ?  420  LYS C C   1 
ATOM   7601  O  O   . LYS C  1 396 ? 31.357  27.977  61.259  1.00 33.71 ?  420  LYS C O   1 
ATOM   7602  C  CB  . LYS C  1 396 ? 34.138  29.513  60.207  1.00 33.44 ?  420  LYS C CB  1 
ATOM   7603  C  CG  . LYS C  1 396 ? 34.226  29.715  61.730  1.00 34.58 ?  420  LYS C CG  1 
ATOM   7604  C  CD  . LYS C  1 396 ? 34.728  28.460  62.455  1.00 36.34 ?  420  LYS C CD  1 
ATOM   7605  C  CE  . LYS C  1 396 ? 34.752  28.652  63.969  1.00 37.09 ?  420  LYS C CE  1 
ATOM   7606  N  NZ  . LYS C  1 396 ? 34.584  27.363  64.692  1.00 36.92 ?  420  LYS C NZ  1 
ATOM   7607  N  N   . MET C  1 397 ? 31.029  29.550  59.673  1.00 33.42 ?  421  MET C N   1 
ATOM   7608  C  CA  . MET C  1 397 ? 29.636  29.797  60.041  1.00 33.48 ?  421  MET C CA  1 
ATOM   7609  C  C   . MET C  1 397 ? 28.792  28.527  59.949  1.00 33.51 ?  421  MET C C   1 
ATOM   7610  O  O   . MET C  1 397 ? 28.019  28.227  60.864  1.00 33.50 ?  421  MET C O   1 
ATOM   7611  C  CB  . MET C  1 397 ? 29.027  30.914  59.186  1.00 33.47 ?  421  MET C CB  1 
ATOM   7612  C  CG  . MET C  1 397 ? 29.610  32.292  59.477  1.00 33.45 ?  421  MET C CG  1 
ATOM   7613  S  SD  . MET C  1 397 ? 28.741  33.641  58.657  1.00 33.65 ?  421  MET C SD  1 
ATOM   7614  C  CE  . MET C  1 397 ? 27.241  33.737  59.633  1.00 33.51 ?  421  MET C CE  1 
ATOM   7615  N  N   . TYR C  1 398 ? 28.955  27.787  58.851  1.00 33.51 ?  422  TYR C N   1 
ATOM   7616  C  CA  . TYR C  1 398 ? 28.259  26.510  58.649  1.00 33.60 ?  422  TYR C CA  1 
ATOM   7617  C  C   . TYR C  1 398 ? 28.548  25.509  59.772  1.00 33.79 ?  422  TYR C C   1 
ATOM   7618  O  O   . TYR C  1 398 ? 27.626  24.877  60.298  1.00 33.84 ?  422  TYR C O   1 
ATOM   7619  C  CB  . TYR C  1 398 ? 28.613  25.898  57.287  1.00 33.35 ?  422  TYR C CB  1 
ATOM   7620  C  CG  . TYR C  1 398 ? 27.987  24.538  57.045  1.00 33.04 ?  422  TYR C CG  1 
ATOM   7621  C  CD1 . TYR C  1 398 ? 26.660  24.425  56.625  1.00 32.61 ?  422  TYR C CD1 1 
ATOM   7622  C  CD2 . TYR C  1 398 ? 28.718  23.365  57.245  1.00 32.55 ?  422  TYR C CD2 1 
ATOM   7623  C  CE1 . TYR C  1 398 ? 26.077  23.185  56.407  1.00 32.54 ?  422  TYR C CE1 1 
ATOM   7624  C  CE2 . TYR C  1 398 ? 28.144  22.117  57.030  1.00 32.75 ?  422  TYR C CE2 1 
ATOM   7625  C  CZ  . TYR C  1 398 ? 26.823  22.034  56.609  1.00 32.98 ?  422  TYR C CZ  1 
ATOM   7626  O  OH  . TYR C  1 398 ? 26.249  20.804  56.389  1.00 33.03 ?  422  TYR C OH  1 
ATOM   7627  N  N   . GLU C  1 399 ? 29.826  25.366  60.121  1.00 34.00 ?  423  GLU C N   1 
ATOM   7628  C  CA  . GLU C  1 399 ? 30.251  24.499  61.223  1.00 34.40 ?  423  GLU C CA  1 
ATOM   7629  C  C   . GLU C  1 399 ? 29.682  24.992  62.559  1.00 34.21 ?  423  GLU C C   1 
ATOM   7630  O  O   . GLU C  1 399 ? 29.319  24.188  63.416  1.00 34.30 ?  423  GLU C O   1 
ATOM   7631  C  CB  . GLU C  1 399 ? 31.781  24.427  61.301  1.00 34.58 ?  423  GLU C CB  1 
ATOM   7632  C  CG  . GLU C  1 399 ? 32.475  23.937  60.032  1.00 35.96 ?  423  GLU C CG  1 
ATOM   7633  C  CD  . GLU C  1 399 ? 32.792  22.452  60.052  1.00 38.36 ?  423  GLU C CD  1 
ATOM   7634  O  OE1 . GLU C  1 399 ? 31.848  21.630  60.095  1.00 38.94 ?  423  GLU C OE1 1 
ATOM   7635  O  OE2 . GLU C  1 399 ? 33.996  22.109  60.008  1.00 39.50 -1 423  GLU C OE2 1 
ATOM   7636  N  N   . ASP C  1 400 ? 29.611  26.313  62.722  1.00 33.97 ?  424  ASP C N   1 
ATOM   7637  C  CA  . ASP C  1 400 ? 29.030  26.935  63.916  1.00 33.91 ?  424  ASP C CA  1 
ATOM   7638  C  C   . ASP C  1 400 ? 27.508  26.795  63.974  1.00 33.75 ?  424  ASP C C   1 
ATOM   7639  O  O   . ASP C  1 400 ? 26.909  26.935  65.040  1.00 34.03 ?  424  ASP C O   1 
ATOM   7640  C  CB  . ASP C  1 400 ? 29.415  28.417  63.999  1.00 33.80 ?  424  ASP C CB  1 
ATOM   7641  C  CG  . ASP C  1 400 ? 30.865  28.632  64.415  1.00 33.93 ?  424  ASP C CG  1 
ATOM   7642  O  OD1 . ASP C  1 400 ? 31.597  27.644  64.632  1.00 34.10 ?  424  ASP C OD1 1 
ATOM   7643  O  OD2 . ASP C  1 400 ? 31.276  29.805  64.529  1.00 34.09 -1 424  ASP C OD2 1 
ATOM   7644  N  N   . GLY C  1 401 ? 26.894  26.520  62.828  1.00 33.58 ?  425  GLY C N   1 
ATOM   7645  C  CA  . GLY C  1 401 ? 25.443  26.412  62.721  1.00 33.27 ?  425  GLY C CA  1 
ATOM   7646  C  C   . GLY C  1 401 ? 24.768  27.771  62.680  1.00 33.20 ?  425  GLY C C   1 
ATOM   7647  O  O   . GLY C  1 401 ? 23.570  27.882  62.956  1.00 33.36 ?  425  GLY C O   1 
ATOM   7648  N  N   . THR C  1 402 ? 25.532  28.800  62.315  1.00 32.86 ?  426  THR C N   1 
ATOM   7649  C  CA  . THR C  1 402 ? 25.081  30.190  62.429  1.00 32.64 ?  426  THR C CA  1 
ATOM   7650  C  C   . THR C  1 402 ? 24.562  30.814  61.127  1.00 32.40 ?  426  THR C C   1 
ATOM   7651  O  O   . THR C  1 402 ? 24.160  31.983  61.120  1.00 32.31 ?  426  THR C O   1 
ATOM   7652  C  CB  . THR C  1 402 ? 26.188  31.097  63.030  1.00 32.77 ?  426  THR C CB  1 
ATOM   7653  O  OG1 . THR C  1 402 ? 27.408  30.918  62.302  1.00 32.89 ?  426  THR C OG1 1 
ATOM   7654  C  CG2 . THR C  1 402 ? 26.425  30.765  64.503  1.00 32.74 ?  426  THR C CG2 1 
ATOM   7655  N  N   . LEU C  1 403 ? 24.567  30.046  60.035  1.00 32.00 ?  427  LEU C N   1 
ATOM   7656  C  CA  . LEU C  1 403 ? 24.025  30.527  58.760  1.00 31.79 ?  427  LEU C CA  1 
ATOM   7657  C  C   . LEU C  1 403 ? 22.537  30.835  58.896  1.00 31.63 ?  427  LEU C C   1 
ATOM   7658  O  O   . LEU C  1 403 ? 21.821  30.148  59.627  1.00 31.62 ?  427  LEU C O   1 
ATOM   7659  C  CB  . LEU C  1 403 ? 24.242  29.512  57.629  1.00 31.62 ?  427  LEU C CB  1 
ATOM   7660  C  CG  . LEU C  1 403 ? 25.646  29.255  57.063  1.00 31.63 ?  427  LEU C CG  1 
ATOM   7661  C  CD1 . LEU C  1 403 ? 25.583  28.143  56.023  1.00 31.34 ?  427  LEU C CD1 1 
ATOM   7662  C  CD2 . LEU C  1 403 ? 26.272  30.507  56.457  1.00 31.06 ?  427  LEU C CD2 1 
ATOM   7663  N  N   . THR C  1 404 ? 22.085  31.874  58.198  1.00 31.42 ?  428  THR C N   1 
ATOM   7664  C  CA  . THR C  1 404 ? 20.685  32.288  58.239  1.00 31.38 ?  428  THR C CA  1 
ATOM   7665  C  C   . THR C  1 404 ? 19.777  31.114  57.887  1.00 31.44 ?  428  THR C C   1 
ATOM   7666  O  O   . THR C  1 404 ? 19.909  30.519  56.818  1.00 31.46 ?  428  THR C O   1 
ATOM   7667  C  CB  . THR C  1 404 ? 20.422  33.494  57.303  1.00 31.37 ?  428  THR C CB  1 
ATOM   7668  O  OG1 . THR C  1 404 ? 21.156  34.628  57.779  1.00 30.74 ?  428  THR C OG1 1 
ATOM   7669  C  CG2 . THR C  1 404 ? 18.936  33.847  57.255  1.00 31.22 ?  428  THR C CG2 1 
ATOM   7670  N  N   . GLY C  1 405 ? 18.894  30.768  58.824  1.00 31.47 ?  429  GLY C N   1 
ATOM   7671  C  CA  . GLY C  1 405 ? 17.922  29.689  58.650  1.00 31.43 ?  429  GLY C CA  1 
ATOM   7672  C  C   . GLY C  1 405 ? 18.445  28.263  58.751  1.00 31.55 ?  429  GLY C C   1 
ATOM   7673  O  O   . GLY C  1 405 ? 17.686  27.317  58.524  1.00 31.40 ?  429  GLY C O   1 
ATOM   7674  N  N   . GLN C  1 406 ? 19.722  28.101  59.107  1.00 31.57 ?  430  GLN C N   1 
ATOM   7675  C  CA  . GLN C  1 406 ? 20.374  26.781  59.110  1.00 31.84 ?  430  GLN C CA  1 
ATOM   7676  C  C   . GLN C  1 406 ? 19.703  25.743  60.019  1.00 32.07 ?  430  GLN C C   1 
ATOM   7677  O  O   . GLN C  1 406 ? 19.697  24.551  59.705  1.00 32.05 ?  430  GLN C O   1 
ATOM   7678  C  CB  . GLN C  1 406 ? 21.865  26.902  59.463  1.00 31.85 ?  430  GLN C CB  1 
ATOM   7679  C  CG  . GLN C  1 406 ? 22.702  25.677  59.073  1.00 31.42 ?  430  GLN C CG  1 
ATOM   7680  C  CD  . GLN C  1 406 ? 24.181  25.809  59.418  1.00 31.01 ?  430  GLN C CD  1 
ATOM   7681  O  OE1 . GLN C  1 406 ? 24.726  26.910  59.495  1.00 30.42 ?  430  GLN C OE1 1 
ATOM   7682  N  NE2 . GLN C  1 406 ? 24.837  24.673  59.617  1.00 30.79 ?  430  GLN C NE2 1 
ATOM   7683  N  N   . LYS C  1 407 ? 19.141  26.199  61.137  1.00 32.36 ?  431  LYS C N   1 
ATOM   7684  C  CA  . LYS C  1 407 ? 18.522  25.296  62.111  1.00 32.68 ?  431  LYS C CA  1 
ATOM   7685  C  C   . LYS C  1 407 ? 16.998  25.397  62.151  1.00 32.64 ?  431  LYS C C   1 
ATOM   7686  O  O   . LYS C  1 407 ? 16.337  24.566  62.781  1.00 32.95 ?  431  LYS C O   1 
ATOM   7687  C  CB  . LYS C  1 407 ? 19.101  25.534  63.516  1.00 32.83 ?  431  LYS C CB  1 
ATOM   7688  C  CG  . LYS C  1 407 ? 20.600  25.248  63.650  1.00 33.25 ?  431  LYS C CG  1 
ATOM   7689  C  CD  . LYS C  1 407 ? 20.922  23.778  63.385  1.00 34.28 ?  431  LYS C CD  1 
ATOM   7690  C  CE  . LYS C  1 407 ? 22.423  23.536  63.362  1.00 34.82 ?  431  LYS C CE  1 
ATOM   7691  N  NZ  . LYS C  1 407 ? 22.750  22.254  62.686  1.00 36.06 ?  431  LYS C NZ  1 
ATOM   7692  N  N   . THR C  1 408 ? 16.449  26.407  61.476  1.00 32.43 ?  432  THR C N   1 
ATOM   7693  C  CA  . THR C  1 408 ? 15.013  26.692  61.522  1.00 32.08 ?  432  THR C CA  1 
ATOM   7694  C  C   . THR C  1 408 ? 14.293  26.523  60.177  1.00 31.93 ?  432  THR C C   1 
ATOM   7695  O  O   . THR C  1 408 ? 13.097  26.230  60.150  1.00 31.91 ?  432  THR C O   1 
ATOM   7696  C  CB  . THR C  1 408 ? 14.737  28.120  62.046  1.00 32.07 ?  432  THR C CB  1 
ATOM   7697  O  OG1 . THR C  1 408 ? 15.386  29.079  61.200  1.00 31.96 ?  432  THR C OG1 1 
ATOM   7698  C  CG2 . THR C  1 408 ? 15.237  28.285  63.481  1.00 32.28 ?  432  THR C CG2 1 
ATOM   7699  N  N   . ASN C  1 409 ? 15.016  26.718  59.074  1.00 31.63 ?  433  ASN C N   1 
ATOM   7700  C  CA  . ASN C  1 409 ? 14.417  26.681  57.733  1.00 31.34 ?  433  ASN C CA  1 
ATOM   7701  C  C   . ASN C  1 409 ? 15.389  26.167  56.665  1.00 31.17 ?  433  ASN C C   1 
ATOM   7702  O  O   . ASN C  1 409 ? 15.677  26.857  55.685  1.00 30.91 ?  433  ASN C O   1 
ATOM   7703  C  CB  . ASN C  1 409 ? 13.880  28.072  57.358  1.00 31.37 ?  433  ASN C CB  1 
ATOM   7704  C  CG  . ASN C  1 409 ? 12.873  28.035  56.212  1.00 31.81 ?  433  ASN C CG  1 
ATOM   7705  O  OD1 . ASN C  1 409 ? 12.270  26.999  55.917  1.00 32.97 ?  433  ASN C OD1 1 
ATOM   7706  N  ND2 . ASN C  1 409 ? 12.684  29.177  55.566  1.00 31.36 ?  433  ASN C ND2 1 
ATOM   7707  N  N   . ARG C  1 410 ? 15.894  24.952  56.862  1.00 30.81 ?  434  ARG C N   1 
ATOM   7708  C  CA  . ARG C  1 410 ? 16.852  24.359  55.932  1.00 30.62 ?  434  ARG C CA  1 
ATOM   7709  C  C   . ARG C  1 410 ? 16.402  22.962  55.507  1.00 30.65 ?  434  ARG C C   1 
ATOM   7710  O  O   . ARG C  1 410 ? 16.881  21.959  56.044  1.00 30.68 ?  434  ARG C O   1 
ATOM   7711  C  CB  . ARG C  1 410 ? 18.256  24.328  56.547  1.00 30.54 ?  434  ARG C CB  1 
ATOM   7712  C  CG  . ARG C  1 410 ? 19.371  24.038  55.549  1.00 29.68 ?  434  ARG C CG  1 
ATOM   7713  C  CD  . ARG C  1 410 ? 20.727  24.063  56.223  1.00 27.88 ?  434  ARG C CD  1 
ATOM   7714  N  NE  . ARG C  1 410 ? 21.796  23.686  55.302  1.00 26.89 ?  434  ARG C NE  1 
ATOM   7715  C  CZ  . ARG C  1 410 ? 22.545  24.547  54.615  1.00 26.50 ?  434  ARG C CZ  1 
ATOM   7716  N  NH1 . ARG C  1 410 ? 22.359  25.857  54.739  1.00 25.81 ?  434  ARG C NH1 1 
ATOM   7717  N  NH2 . ARG C  1 410 ? 23.492  24.091  53.805  1.00 25.53 ?  434  ARG C NH2 1 
ATOM   7718  N  N   . PRO C  1 411 ? 15.474  22.892  54.535  1.00 30.65 ?  435  PRO C N   1 
ATOM   7719  C  CA  . PRO C  1 411 ? 14.919  21.600  54.134  1.00 30.65 ?  435  PRO C CA  1 
ATOM   7720  C  C   . PRO C  1 411 ? 15.891  20.778  53.292  1.00 30.84 ?  435  PRO C C   1 
ATOM   7721  O  O   . PRO C  1 411 ? 16.751  21.338  52.603  1.00 30.81 ?  435  PRO C O   1 
ATOM   7722  C  CB  . PRO C  1 411 ? 13.683  21.987  53.317  1.00 30.61 ?  435  PRO C CB  1 
ATOM   7723  C  CG  . PRO C  1 411 ? 13.990  23.342  52.777  1.00 30.67 ?  435  PRO C CG  1 
ATOM   7724  C  CD  . PRO C  1 411 ? 14.915  24.012  53.752  1.00 30.55 ?  435  PRO C CD  1 
ATOM   7725  N  N   . ASN C  1 412 ? 15.746  19.458  53.357  1.00 31.00 ?  436  ASN C N   1 
ATOM   7726  C  CA  . ASN C  1 412 ? 16.614  18.542  52.630  1.00 31.25 ?  436  ASN C CA  1 
ATOM   7727  C  C   . ASN C  1 412 ? 16.394  18.597  51.119  1.00 31.17 ?  436  ASN C C   1 
ATOM   7728  O  O   . ASN C  1 412 ? 15.257  18.733  50.661  1.00 31.16 ?  436  ASN C O   1 
ATOM   7729  C  CB  . ASN C  1 412 ? 16.437  17.106  53.143  1.00 31.20 ?  436  ASN C CB  1 
ATOM   7730  C  CG  . ASN C  1 412 ? 17.018  16.905  54.535  1.00 31.87 ?  436  ASN C CG  1 
ATOM   7731  O  OD1 . ASN C  1 412 ? 17.999  17.548  54.915  1.00 31.75 ?  436  ASN C OD1 1 
ATOM   7732  N  ND2 . ASN C  1 412 ? 16.412  16.001  55.302  1.00 32.04 ?  436  ASN C ND2 1 
ATOM   7733  N  N   . PRO C  1 413 ? 17.488  18.493  50.342  1.00 31.17 ?  437  PRO C N   1 
ATOM   7734  C  CA  . PRO C  1 413 ? 17.416  18.430  48.880  1.00 31.19 ?  437  PRO C CA  1 
ATOM   7735  C  C   . PRO C  1 413 ? 16.640  17.199  48.400  1.00 31.23 ?  437  PRO C C   1 
ATOM   7736  O  O   . PRO C  1 413 ? 16.513  16.229  49.156  1.00 31.34 ?  437  PRO C O   1 
ATOM   7737  C  CB  . PRO C  1 413 ? 18.888  18.325  48.461  1.00 31.06 ?  437  PRO C CB  1 
ATOM   7738  C  CG  . PRO C  1 413 ? 19.600  17.807  49.671  1.00 31.20 ?  437  PRO C CG  1 
ATOM   7739  C  CD  . PRO C  1 413 ? 18.881  18.438  50.822  1.00 31.13 ?  437  PRO C CD  1 
ATOM   7740  N  N   . PRO C  1 414 ? 16.116  17.235  47.156  1.00 31.06 ?  438  PRO C N   1 
ATOM   7741  C  CA  . PRO C  1 414 ? 15.401  16.078  46.623  1.00 31.11 ?  438  PRO C CA  1 
ATOM   7742  C  C   . PRO C  1 414 ? 16.288  14.840  46.564  1.00 31.23 ?  438  PRO C C   1 
ATOM   7743  O  O   . PRO C  1 414 ? 17.505  14.957  46.381  1.00 31.22 ?  438  PRO C O   1 
ATOM   7744  C  CB  . PRO C  1 414 ? 15.013  16.519  45.205  1.00 30.99 ?  438  PRO C CB  1 
ATOM   7745  C  CG  . PRO C  1 414 ? 15.909  17.661  44.885  1.00 30.90 ?  438  PRO C CG  1 
ATOM   7746  C  CD  . PRO C  1 414 ? 16.146  18.347  46.189  1.00 31.16 ?  438  PRO C CD  1 
ATOM   7747  N  N   . GLU C  1 415 ? 15.669  13.673  46.725  1.00 31.19 ?  439  GLU C N   1 
ATOM   7748  C  CA  . GLU C  1 415 ? 16.366  12.388  46.679  1.00 31.32 ?  439  GLU C CA  1 
ATOM   7749  C  C   . GLU C  1 415 ? 16.985  12.151  45.299  1.00 31.32 ?  439  GLU C C   1 
ATOM   7750  O  O   . GLU C  1 415 ? 16.395  12.546  44.291  1.00 31.30 ?  439  GLU C O   1 
ATOM   7751  C  CB  . GLU C  1 415 ? 15.398  11.252  47.031  1.00 31.20 ?  439  GLU C CB  1 
ATOM   7752  C  CG  . GLU C  1 415 ? 14.113  11.242  46.202  1.00 31.24 ?  439  GLU C CG  1 
ATOM   7753  C  CD  . GLU C  1 415 ? 13.197  10.071  46.514  1.00 31.16 ?  439  GLU C CD  1 
ATOM   7754  O  OE1 . GLU C  1 415 ? 13.580  9.185   47.307  1.00 31.47 ?  439  GLU C OE1 1 
ATOM   7755  O  OE2 . GLU C  1 415 ? 12.082  10.040  45.956  1.00 31.58 -1 439  GLU C OE2 1 
ATOM   7756  N  N   . PRO C  1 416 ? 18.158  11.487  45.242  1.00 31.39 ?  440  PRO C N   1 
ATOM   7757  C  CA  . PRO C  1 416 ? 18.917  10.883  46.341  1.00 31.49 ?  440  PRO C CA  1 
ATOM   7758  C  C   . PRO C  1 416 ? 20.014  11.773  46.933  1.00 31.60 ?  440  PRO C C   1 
ATOM   7759  O  O   . PRO C  1 416 ? 20.949  11.258  47.554  1.00 31.58 ?  440  PRO C O   1 
ATOM   7760  C  CB  . PRO C  1 416 ? 19.557  9.666   45.672  1.00 31.53 ?  440  PRO C CB  1 
ATOM   7761  C  CG  . PRO C  1 416 ? 19.813  10.122  44.272  1.00 31.24 ?  440  PRO C CG  1 
ATOM   7762  C  CD  . PRO C  1 416 ? 18.755  11.152  43.934  1.00 31.40 ?  440  PRO C CD  1 
ATOM   7763  N  N   . GLU C  1 417 ? 19.905  13.086  46.742  1.00 31.58 ?  441  GLU C N   1 
ATOM   7764  C  CA  . GLU C  1 417 ? 20.905  14.017  47.262  1.00 31.63 ?  441  GLU C CA  1 
ATOM   7765  C  C   . GLU C  1 417 ? 20.932  14.023  48.788  1.00 31.66 ?  441  GLU C C   1 
ATOM   7766  O  O   . GLU C  1 417 ? 19.894  13.884  49.439  1.00 31.71 ?  441  GLU C O   1 
ATOM   7767  C  CB  . GLU C  1 417 ? 20.683  15.435  46.711  1.00 31.52 ?  441  GLU C CB  1 
ATOM   7768  C  CG  . GLU C  1 417 ? 21.778  16.465  47.048  1.00 31.63 ?  441  GLU C CG  1 
ATOM   7769  C  CD  . GLU C  1 417 ? 23.185  16.026  46.649  1.00 31.89 ?  441  GLU C CD  1 
ATOM   7770  O  OE1 . GLU C  1 417 ? 23.742  15.116  47.300  1.00 31.99 ?  441  GLU C OE1 1 
ATOM   7771  O  OE2 . GLU C  1 417 ? 23.741  16.606  45.694  1.00 32.04 -1 441  GLU C OE2 1 
ATOM   7772  N  N   . LYS C  1 418 ? 22.134  14.164  49.338  1.00 31.75 ?  442  LYS C N   1 
ATOM   7773  C  CA  . LYS C  1 418 ? 22.336  14.315  50.774  1.00 32.10 ?  442  LYS C CA  1 
ATOM   7774  C  C   . LYS C  1 418 ? 22.645  15.781  51.086  1.00 31.88 ?  442  LYS C C   1 
ATOM   7775  O  O   . LYS C  1 418 ? 23.345  16.438  50.312  1.00 31.76 ?  442  LYS C O   1 
ATOM   7776  C  CB  . LYS C  1 418 ? 23.476  13.411  51.256  1.00 32.34 ?  442  LYS C CB  1 
ATOM   7777  C  CG  . LYS C  1 418 ? 23.216  11.920  51.041  1.00 33.87 ?  442  LYS C CG  1 
ATOM   7778  C  CD  . LYS C  1 418 ? 24.437  11.074  51.385  1.00 36.44 ?  442  LYS C CD  1 
ATOM   7779  C  CE  . LYS C  1 418 ? 24.253  9.632   50.917  1.00 37.57 ?  442  LYS C CE  1 
ATOM   7780  N  NZ  . LYS C  1 418 ? 25.306  8.729   51.463  1.00 38.96 ?  442  LYS C NZ  1 
ATOM   7781  N  N   . PRO C  1 419 ? 22.115  16.300  52.215  1.00 31.69 ?  443  PRO C N   1 
ATOM   7782  C  CA  . PRO C  1 419 ? 22.361  17.688  52.624  1.00 31.49 ?  443  PRO C CA  1 
ATOM   7783  C  C   . PRO C  1 419 ? 23.839  17.969  52.884  1.00 31.24 ?  443  PRO C C   1 
ATOM   7784  O  O   . PRO C  1 419 ? 24.578  17.071  53.290  1.00 31.32 ?  443  PRO C O   1 
ATOM   7785  C  CB  . PRO C  1 419 ? 21.563  17.822  53.927  1.00 31.66 ?  443  PRO C CB  1 
ATOM   7786  C  CG  . PRO C  1 419 ? 21.361  16.417  54.409  1.00 31.76 ?  443  PRO C CG  1 
ATOM   7787  C  CD  . PRO C  1 419 ? 21.220  15.606  53.160  1.00 31.67 ?  443  PRO C CD  1 
ATOM   7788  N  N   . GLY C  1 420 ? 24.256  19.210  52.645  1.00 31.01 ?  444  GLY C N   1 
ATOM   7789  C  CA  . GLY C  1 420 ? 25.648  19.615  52.836  1.00 30.37 ?  444  GLY C CA  1 
ATOM   7790  C  C   . GLY C  1 420 ? 25.874  21.086  52.555  1.00 30.07 ?  444  GLY C C   1 
ATOM   7791  O  O   . GLY C  1 420 ? 24.942  21.810  52.189  1.00 30.29 ?  444  GLY C O   1 
ATOM   7792  N  N   . PHE C  1 421 ? 27.120  21.522  52.719  1.00 29.53 ?  445  PHE C N   1 
ATOM   7793  C  CA  . PHE C  1 421 ? 27.495  22.924  52.555  1.00 29.10 ?  445  PHE C CA  1 
ATOM   7794  C  C   . PHE C  1 421 ? 28.024  23.235  51.152  1.00 28.61 ?  445  PHE C C   1 
ATOM   7795  O  O   . PHE C  1 421 ? 28.933  22.564  50.667  1.00 28.67 ?  445  PHE C O   1 
ATOM   7796  C  CB  . PHE C  1 421 ? 28.537  23.314  53.613  1.00 29.13 ?  445  PHE C CB  1 
ATOM   7797  C  CG  . PHE C  1 421 ? 29.145  24.674  53.402  1.00 29.49 ?  445  PHE C CG  1 
ATOM   7798  C  CD1 . PHE C  1 421 ? 28.399  25.828  53.624  1.00 29.71 ?  445  PHE C CD1 1 
ATOM   7799  C  CD2 . PHE C  1 421 ? 30.466  24.801  52.982  1.00 30.28 ?  445  PHE C CD2 1 
ATOM   7800  C  CE1 . PHE C  1 421 ? 28.960  27.088  53.429  1.00 30.18 ?  445  PHE C CE1 1 
ATOM   7801  C  CE2 . PHE C  1 421 ? 31.037  26.061  52.783  1.00 30.37 ?  445  PHE C CE2 1 
ATOM   7802  C  CZ  . PHE C  1 421 ? 30.282  27.204  53.009  1.00 30.09 ?  445  PHE C CZ  1 
ATOM   7803  N  N   . GLY C  1 422 ? 27.453  24.261  50.520  1.00 28.10 ?  446  GLY C N   1 
ATOM   7804  C  CA  . GLY C  1 422 ? 27.922  24.759  49.224  1.00 27.26 ?  446  GLY C CA  1 
ATOM   7805  C  C   . GLY C  1 422 ? 28.109  23.675  48.175  1.00 26.91 ?  446  GLY C C   1 
ATOM   7806  O  O   . GLY C  1 422 ? 29.178  23.558  47.581  1.00 27.07 ?  446  GLY C O   1 
ATOM   7807  N  N   . ILE C  1 423 ? 27.062  22.886  47.956  1.00 26.32 ?  447  ILE C N   1 
ATOM   7808  C  CA  . ILE C  1 423 ? 27.096  21.771  47.008  1.00 25.87 ?  447  ILE C CA  1 
ATOM   7809  C  C   . ILE C  1 423 ? 26.476  22.172  45.669  1.00 25.67 ?  447  ILE C C   1 
ATOM   7810  O  O   . ILE C  1 423 ? 25.649  23.087  45.614  1.00 25.46 ?  447  ILE C O   1 
ATOM   7811  C  CB  . ILE C  1 423 ? 26.388  20.518  47.580  1.00 25.84 ?  447  ILE C CB  1 
ATOM   7812  C  CG1 . ILE C  1 423 ? 24.968  20.865  48.059  1.00 25.70 ?  447  ILE C CG1 1 
ATOM   7813  C  CG2 . ILE C  1 423 ? 27.224  19.918  48.715  1.00 25.85 ?  447  ILE C CG2 1 
ATOM   7814  C  CD1 . ILE C  1 423 ? 24.056  19.657  48.284  1.00 26.31 ?  447  ILE C CD1 1 
ATOM   7815  N  N   . PHE C  1 424 ? 26.882  21.490  44.597  1.00 25.37 ?  448  PHE C N   1 
ATOM   7816  C  CA  . PHE C  1 424 ? 26.411  21.814  43.248  1.00 25.26 ?  448  PHE C CA  1 
ATOM   7817  C  C   . PHE C  1 424 ? 24.886  21.913  43.154  1.00 25.45 ?  448  PHE C C   1 
ATOM   7818  O  O   . PHE C  1 424 ? 24.354  22.813  42.495  1.00 25.51 ?  448  PHE C O   1 
ATOM   7819  C  CB  . PHE C  1 424 ? 26.942  20.810  42.220  1.00 25.15 ?  448  PHE C CB  1 
ATOM   7820  C  CG  . PHE C  1 424 ? 26.575  21.152  40.805  1.00 24.41 ?  448  PHE C CG  1 
ATOM   7821  C  CD1 . PHE C  1 424 ? 27.292  22.113  40.103  1.00 23.52 ?  448  PHE C CD1 1 
ATOM   7822  C  CD2 . PHE C  1 424 ? 25.503  20.520  40.176  1.00 24.02 ?  448  PHE C CD2 1 
ATOM   7823  C  CE1 . PHE C  1 424 ? 26.953  22.438  38.794  1.00 23.38 ?  448  PHE C CE1 1 
ATOM   7824  C  CE2 . PHE C  1 424 ? 25.156  20.842  38.865  1.00 23.94 ?  448  PHE C CE2 1 
ATOM   7825  C  CZ  . PHE C  1 424 ? 25.884  21.800  38.174  1.00 23.50 ?  448  PHE C CZ  1 
ATOM   7826  N  N   . THR C  1 425 ? 24.203  20.988  43.828  1.00 25.54 ?  449  THR C N   1 
ATOM   7827  C  CA  . THR C  1 425 ? 22.737  20.942  43.902  1.00 25.58 ?  449  THR C CA  1 
ATOM   7828  C  C   . THR C  1 425 ? 22.090  22.304  44.190  1.00 25.45 ?  449  THR C C   1 
ATOM   7829  O  O   . THR C  1 425 ? 21.041  22.631  43.632  1.00 25.43 ?  449  THR C O   1 
ATOM   7830  C  CB  . THR C  1 425 ? 22.283  19.882  44.940  1.00 25.61 ?  449  THR C CB  1 
ATOM   7831  O  OG1 . THR C  1 425 ? 22.657  18.580  44.473  1.00 26.08 ?  449  THR C OG1 1 
ATOM   7832  C  CG2 . THR C  1 425 ? 20.770  19.913  45.171  1.00 25.59 ?  449  THR C CG2 1 
ATOM   7833  N  N   . GLN C  1 426 ? 22.737  23.099  45.039  1.00 25.51 ?  450  GLN C N   1 
ATOM   7834  C  CA  . GLN C  1 426 ? 22.209  24.397  45.462  1.00 25.38 ?  450  GLN C CA  1 
ATOM   7835  C  C   . GLN C  1 426 ? 22.178  25.472  44.360  1.00 25.44 ?  450  GLN C C   1 
ATOM   7836  O  O   . GLN C  1 426 ? 21.613  26.551  44.558  1.00 25.42 ?  450  GLN C O   1 
ATOM   7837  C  CB  . GLN C  1 426 ? 22.959  24.883  46.702  1.00 25.66 ?  450  GLN C CB  1 
ATOM   7838  C  CG  . GLN C  1 426 ? 22.616  24.077  47.960  1.00 25.74 ?  450  GLN C CG  1 
ATOM   7839  C  CD  . GLN C  1 426 ? 23.601  24.283  49.097  1.00 26.55 ?  450  GLN C CD  1 
ATOM   7840  O  OE1 . GLN C  1 426 ? 24.777  24.570  48.873  1.00 26.50 ?  450  GLN C OE1 1 
ATOM   7841  N  NE2 . GLN C  1 426 ? 23.124  24.123  50.330  1.00 26.10 ?  450  GLN C NE2 1 
ATOM   7842  N  N   . LEU C  1 427 ? 22.767  25.162  43.204  1.00 25.34 ?  451  LEU C N   1 
ATOM   7843  C  CA  . LEU C  1 427 ? 22.697  26.027  42.022  1.00 25.23 ?  451  LEU C CA  1 
ATOM   7844  C  C   . LEU C  1 427 ? 21.455  25.765  41.171  1.00 25.27 ?  451  LEU C C   1 
ATOM   7845  O  O   . LEU C  1 427 ? 21.010  26.646  40.434  1.00 25.41 ?  451  LEU C O   1 
ATOM   7846  C  CB  . LEU C  1 427 ? 23.951  25.869  41.154  1.00 25.12 ?  451  LEU C CB  1 
ATOM   7847  C  CG  . LEU C  1 427 ? 25.288  26.310  41.758  1.00 24.87 ?  451  LEU C CG  1 
ATOM   7848  C  CD1 . LEU C  1 427 ? 26.435  25.669  40.999  1.00 24.32 ?  451  LEU C CD1 1 
ATOM   7849  C  CD2 . LEU C  1 427 ? 25.419  27.838  41.779  1.00 24.48 ?  451  LEU C CD2 1 
ATOM   7850  N  N   . PHE C  1 428 ? 20.901  24.559  41.272  1.00 25.26 ?  452  PHE C N   1 
ATOM   7851  C  CA  . PHE C  1 428 ? 19.729  24.182  40.474  1.00 25.33 ?  452  PHE C CA  1 
ATOM   7852  C  C   . PHE C  1 428 ? 18.481  23.836  41.292  1.00 25.26 ?  452  PHE C C   1 
ATOM   7853  O  O   . PHE C  1 428 ? 17.389  23.670  40.736  1.00 25.28 ?  452  PHE C O   1 
ATOM   7854  C  CB  . PHE C  1 428 ? 20.085  23.060  39.490  1.00 25.26 ?  452  PHE C CB  1 
ATOM   7855  C  CG  . PHE C  1 428 ? 20.843  23.543  38.290  1.00 25.45 ?  452  PHE C CG  1 
ATOM   7856  C  CD1 . PHE C  1 428 ? 20.168  23.912  37.127  1.00 25.39 ?  452  PHE C CD1 1 
ATOM   7857  C  CD2 . PHE C  1 428 ? 22.228  23.658  38.328  1.00 25.04 ?  452  PHE C CD2 1 
ATOM   7858  C  CE1 . PHE C  1 428 ? 20.863  24.377  36.015  1.00 24.79 ?  452  PHE C CE1 1 
ATOM   7859  C  CE2 . PHE C  1 428 ? 22.932  24.119  37.221  1.00 25.43 ?  452  PHE C CE2 1 
ATOM   7860  C  CZ  . PHE C  1 428 ? 22.249  24.481  36.062  1.00 25.06 ?  452  PHE C CZ  1 
ATOM   7861  N  N   . TRP C  1 429 ? 18.653  23.726  42.605  1.00 25.26 ?  453  TRP C N   1 
ATOM   7862  C  CA  . TRP C  1 429 ? 17.538  23.536  43.523  1.00 25.30 ?  453  TRP C CA  1 
ATOM   7863  C  C   . TRP C  1 429 ? 17.712  24.398  44.761  1.00 25.32 ?  453  TRP C C   1 
ATOM   7864  O  O   . TRP C  1 429 ? 18.783  24.420  45.374  1.00 25.27 ?  453  TRP C O   1 
ATOM   7865  C  CB  . TRP C  1 429 ? 17.391  22.067  43.936  1.00 25.34 ?  453  TRP C CB  1 
ATOM   7866  C  CG  . TRP C  1 429 ? 16.271  21.849  44.921  1.00 25.68 ?  453  TRP C CG  1 
ATOM   7867  C  CD1 . TRP C  1 429 ? 14.958  21.595  44.630  1.00 25.60 ?  453  TRP C CD1 1 
ATOM   7868  C  CD2 . TRP C  1 429 ? 16.364  21.882  46.354  1.00 25.93 ?  453  TRP C CD2 1 
ATOM   7869  N  NE1 . TRP C  1 429 ? 14.232  21.464  45.791  1.00 25.90 ?  453  TRP C NE1 1 
ATOM   7870  C  CE2 . TRP C  1 429 ? 15.069  21.637  46.862  1.00 26.20 ?  453  TRP C CE2 1 
ATOM   7871  C  CE3 . TRP C  1 429 ? 17.417  22.095  47.257  1.00 26.28 ?  453  TRP C CE3 1 
ATOM   7872  C  CZ2 . TRP C  1 429 ? 14.800  21.588  48.232  1.00 26.42 ?  453  TRP C CZ2 1 
ATOM   7873  C  CZ3 . TRP C  1 429 ? 17.147  22.053  48.620  1.00 26.53 ?  453  TRP C CZ3 1 
ATOM   7874  C  CH2 . TRP C  1 429 ? 15.846  21.801  49.093  1.00 26.33 ?  453  TRP C CH2 1 
ATOM   7875  N  N   . SER C  1 430 ? 16.643  25.098  45.123  1.00 25.22 ?  454  SER C N   1 
ATOM   7876  C  CA  . SER C  1 430 ? 16.592  25.859  46.358  1.00 25.30 ?  454  SER C CA  1 
ATOM   7877  C  C   . SER C  1 430 ? 15.196  25.788  46.962  1.00 25.41 ?  454  SER C C   1 
ATOM   7878  O  O   . SER C  1 430 ? 14.194  25.754  46.245  1.00 25.44 ?  454  SER C O   1 
ATOM   7879  C  CB  . SER C  1 430 ? 16.997  27.317  46.122  1.00 25.21 ?  454  SER C CB  1 
ATOM   7880  O  OG  . SER C  1 430 ? 16.185  27.921  45.130  1.00 24.93 ?  454  SER C OG  1 
ATOM   7881  N  N   . LYS C  1 431 ? 15.148  25.748  48.287  1.00 25.58 ?  455  LYS C N   1 
ATOM   7882  C  CA  . LYS C  1 431 ? 13.896  25.791  49.031  1.00 25.83 ?  455  LYS C CA  1 
ATOM   7883  C  C   . LYS C  1 431 ? 14.207  26.338  50.407  1.00 25.69 ?  455  LYS C C   1 
ATOM   7884  O  O   . LYS C  1 431 ? 15.229  25.983  50.996  1.00 25.87 ?  455  LYS C O   1 
ATOM   7885  C  CB  . LYS C  1 431 ? 13.272  24.401  49.145  1.00 25.95 ?  455  LYS C CB  1 
ATOM   7886  C  CG  . LYS C  1 431 ? 11.845  24.394  49.665  1.00 26.55 ?  455  LYS C CG  1 
ATOM   7887  C  CD  . LYS C  1 431 ? 11.394  22.981  50.019  1.00 27.58 ?  455  LYS C CD  1 
ATOM   7888  C  CE  . LYS C  1 431 ? 9.942   22.972  50.477  1.00 27.11 ?  455  LYS C CE  1 
ATOM   7889  N  NZ  . LYS C  1 431 ? 9.022   23.286  49.348  1.00 26.96 ?  455  LYS C NZ  1 
ATOM   7890  N  N   . GLY C  1 432 ? 13.330  27.204  50.910  1.00 25.67 ?  456  GLY C N   1 
ATOM   7891  C  CA  . GLY C  1 432 ? 13.536  27.855  52.198  1.00 25.64 ?  456  GLY C CA  1 
ATOM   7892  C  C   . GLY C  1 432 ? 14.889  28.538  52.244  1.00 25.73 ?  456  GLY C C   1 
ATOM   7893  O  O   . GLY C  1 432 ? 15.268  29.233  51.301  1.00 25.63 ?  456  GLY C O   1 
ATOM   7894  N  N   . ASN C  1 433 ? 15.618  28.326  53.337  1.00 25.76 ?  457  ASN C N   1 
ATOM   7895  C  CA  . ASN C  1 433 ? 16.981  28.840  53.475  1.00 25.73 ?  457  ASN C CA  1 
ATOM   7896  C  C   . ASN C  1 433 ? 18.048  27.797  53.136  1.00 25.73 ?  457  ASN C C   1 
ATOM   7897  O  O   . ASN C  1 433 ? 19.161  27.841  53.668  1.00 25.66 ?  457  ASN C O   1 
ATOM   7898  C  CB  . ASN C  1 433 ? 17.209  29.421  54.879  1.00 25.86 ?  457  ASN C CB  1 
ATOM   7899  C  CG  . ASN C  1 433 ? 16.360  30.654  55.152  1.00 25.92 ?  457  ASN C CG  1 
ATOM   7900  O  OD1 . ASN C  1 433 ? 15.657  30.722  56.160  1.00 25.56 ?  457  ASN C OD1 1 
ATOM   7901  N  ND2 . ASN C  1 433 ? 16.422  31.633  54.255  1.00 25.04 ?  457  ASN C ND2 1 
ATOM   7902  N  N   . ASN C  1 434 ? 17.701  26.856  52.256  1.00 25.72 ?  458  ASN C N   1 
ATOM   7903  C  CA  . ASN C  1 434 ? 18.680  25.947  51.669  1.00 25.85 ?  458  ASN C CA  1 
ATOM   7904  C  C   . ASN C  1 434 ? 18.834  26.215  50.167  1.00 25.90 ?  458  ASN C C   1 
ATOM   7905  O  O   . ASN C  1 434 ? 18.002  25.770  49.371  1.00 25.88 ?  458  ASN C O   1 
ATOM   7906  C  CB  . ASN C  1 434 ? 18.298  24.480  51.913  1.00 25.96 ?  458  ASN C CB  1 
ATOM   7907  C  CG  . ASN C  1 434 ? 19.446  23.519  51.621  1.00 26.43 ?  458  ASN C CG  1 
ATOM   7908  O  OD1 . ASN C  1 434 ? 20.523  23.929  51.183  1.00 27.29 ?  458  ASN C OD1 1 
ATOM   7909  N  ND2 . ASN C  1 434 ? 19.219  22.231  51.870  1.00 26.22 ?  458  ASN C ND2 1 
ATOM   7910  N  N   . PRO C  1 435 ? 19.907  26.931  49.769  1.00 25.79 ?  459  PRO C N   1 
ATOM   7911  C  CA  . PRO C  1 435 ? 21.006  27.413  50.609  1.00 25.57 ?  459  PRO C CA  1 
ATOM   7912  C  C   . PRO C  1 435 ? 20.723  28.758  51.274  1.00 25.25 ?  459  PRO C C   1 
ATOM   7913  O  O   . PRO C  1 435 ? 19.706  29.392  50.988  1.00 25.31 ?  459  PRO C O   1 
ATOM   7914  C  CB  . PRO C  1 435 ? 22.147  27.582  49.604  1.00 25.72 ?  459  PRO C CB  1 
ATOM   7915  C  CG  . PRO C  1 435 ? 21.449  27.979  48.330  1.00 25.91 ?  459  PRO C CG  1 
ATOM   7916  C  CD  . PRO C  1 435 ? 20.090  27.317  48.354  1.00 25.77 ?  459  PRO C CD  1 
ATOM   7917  N  N   . ALA C  1 436 ? 21.619  29.164  52.173  1.00 24.79 ?  460  ALA C N   1 
ATOM   7918  C  CA  . ALA C  1 436 ? 21.651  30.531  52.674  1.00 24.40 ?  460  ALA C CA  1 
ATOM   7919  C  C   . ALA C  1 436 ? 22.302  31.397  51.601  1.00 24.10 ?  460  ALA C C   1 
ATOM   7920  O  O   . ALA C  1 436 ? 23.026  30.881  50.745  1.00 24.11 ?  460  ALA C O   1 
ATOM   7921  C  CB  . ALA C  1 436 ? 22.439  30.604  53.979  1.00 24.25 ?  460  ALA C CB  1 
ATOM   7922  N  N   . SER C  1 437 ? 22.047  32.704  51.642  1.00 23.80 ?  461  SER C N   1 
ATOM   7923  C  CA  . SER C  1 437 ? 22.603  33.622  50.642  1.00 23.66 ?  461  SER C CA  1 
ATOM   7924  C  C   . SER C  1 437 ? 24.132  33.645  50.645  1.00 23.67 ?  461  SER C C   1 
ATOM   7925  O  O   . SER C  1 437 ? 24.753  33.593  49.580  1.00 23.12 ?  461  SER C O   1 
ATOM   7926  C  CB  . SER C  1 437 ? 22.051  35.038  50.820  1.00 23.59 ?  461  SER C CB  1 
ATOM   7927  O  OG  . SER C  1 437 ? 22.606  35.913  49.853  1.00 23.47 ?  461  SER C OG  1 
ATOM   7928  N  N   . LEU C  1 438 ? 24.722  33.735  51.842  1.00 23.69 ?  462  LEU C N   1 
ATOM   7929  C  CA  . LEU C  1 438 ? 26.178  33.691  52.013  1.00 24.02 ?  462  LEU C CA  1 
ATOM   7930  C  C   . LEU C  1 438 ? 26.772  32.429  51.414  1.00 23.84 ?  462  LEU C C   1 
ATOM   7931  O  O   . LEU C  1 438 ? 27.842  32.465  50.806  1.00 23.95 ?  462  LEU C O   1 
ATOM   7932  C  CB  . LEU C  1 438 ? 26.561  33.753  53.499  1.00 24.21 ?  462  LEU C CB  1 
ATOM   7933  C  CG  . LEU C  1 438 ? 26.964  35.092  54.118  1.00 25.02 ?  462  LEU C CG  1 
ATOM   7934  C  CD1 . LEU C  1 438 ? 27.178  34.938  55.623  1.00 25.96 ?  462  LEU C CD1 1 
ATOM   7935  C  CD2 . LEU C  1 438 ? 28.211  35.666  53.462  1.00 25.35 ?  462  LEU C CD2 1 
ATOM   7936  N  N   . GLU C  1 439 ? 26.062  31.320  51.608  1.00 23.70 ?  463  GLU C N   1 
ATOM   7937  C  CA  . GLU C  1 439 ? 26.473  30.005  51.139  1.00 23.45 ?  463  GLU C CA  1 
ATOM   7938  C  C   . GLU C  1 439 ? 26.478  29.944  49.612  1.00 23.29 ?  463  GLU C C   1 
ATOM   7939  O  O   . GLU C  1 439 ? 27.418  29.420  49.010  1.00 23.37 ?  463  GLU C O   1 
ATOM   7940  C  CB  . GLU C  1 439 ? 25.534  28.943  51.728  1.00 23.45 ?  463  GLU C CB  1 
ATOM   7941  C  CG  . GLU C  1 439 ? 25.886  27.502  51.425  1.00 23.02 ?  463  GLU C CG  1 
ATOM   7942  C  CD  . GLU C  1 439 ? 24.881  26.523  52.024  1.00 23.50 ?  463  GLU C CD  1 
ATOM   7943  O  OE1 . GLU C  1 439 ? 23.851  26.975  52.567  1.00 23.50 ?  463  GLU C OE1 1 
ATOM   7944  O  OE2 . GLU C  1 439 ? 25.113  25.300  51.939  1.00 23.30 -1 463  GLU C OE2 1 
ATOM   7945  N  N   . LEU C  1 440 ? 25.430  30.485  48.995  1.00 23.09 ?  464  LEU C N   1 
ATOM   7946  C  CA  . LEU C  1 440 ? 25.328  30.537  47.535  1.00 22.95 ?  464  LEU C CA  1 
ATOM   7947  C  C   . LEU C  1 440 ? 26.376  31.483  46.949  1.00 22.89 ?  464  LEU C C   1 
ATOM   7948  O  O   . LEU C  1 440 ? 26.985  31.181  45.917  1.00 22.70 ?  464  LEU C O   1 
ATOM   7949  C  CB  . LEU C  1 440 ? 23.937  31.011  47.115  1.00 22.86 ?  464  LEU C CB  1 
ATOM   7950  C  CG  . LEU C  1 440 ? 23.242  30.539  45.826  1.00 22.94 ?  464  LEU C CG  1 
ATOM   7951  C  CD1 . LEU C  1 440 ? 22.623  31.742  45.124  1.00 21.66 ?  464  LEU C CD1 1 
ATOM   7952  C  CD2 . LEU C  1 440 ? 24.118  29.742  44.848  1.00 21.85 ?  464  LEU C CD2 1 
ATOM   7953  N  N   . LYS C  1 441 ? 26.580  32.623  47.610  1.00 22.83 ?  465  LYS C N   1 
ATOM   7954  C  CA  . LYS C  1 441 ? 27.520  33.635  47.129  1.00 22.85 ?  465  LYS C CA  1 
ATOM   7955  C  C   . LYS C  1 441 ? 28.944  33.098  47.057  1.00 22.75 ?  465  LYS C C   1 
ATOM   7956  O  O   . LYS C  1 441 ? 29.639  33.321  46.071  1.00 22.68 ?  465  LYS C O   1 
ATOM   7957  C  CB  . LYS C  1 441 ? 27.470  34.892  47.997  1.00 23.16 ?  465  LYS C CB  1 
ATOM   7958  C  CG  . LYS C  1 441 ? 28.056  36.131  47.324  1.00 23.05 ?  465  LYS C CG  1 
ATOM   7959  C  CD  . LYS C  1 441 ? 27.813  37.389  48.152  1.00 24.59 ?  465  LYS C CD  1 
ATOM   7960  C  CE  . LYS C  1 441 ? 26.351  37.830  48.095  1.00 24.58 ?  465  LYS C CE  1 
ATOM   7961  N  NZ  . LYS C  1 441 ? 26.133  39.126  48.785  1.00 24.10 ?  465  LYS C NZ  1 
ATOM   7962  N  N   . VAL C  1 442 ? 29.366  32.380  48.095  1.00 22.84 ?  466  VAL C N   1 
ATOM   7963  C  CA  . VAL C  1 442 ? 30.716  31.833  48.136  1.00 22.78 ?  466  VAL C CA  1 
ATOM   7964  C  C   . VAL C  1 442 ? 30.852  30.633  47.202  1.00 22.92 ?  466  VAL C C   1 
ATOM   7965  O  O   . VAL C  1 442 ? 31.931  30.390  46.659  1.00 23.17 ?  466  VAL C O   1 
ATOM   7966  C  CB  . VAL C  1 442 ? 31.205  31.531  49.589  1.00 22.91 ?  466  VAL C CB  1 
ATOM   7967  C  CG1 . VAL C  1 442 ? 30.642  30.212  50.130  1.00 22.11 ?  466  VAL C CG1 1 
ATOM   7968  C  CG2 . VAL C  1 442 ? 32.733  31.539  49.645  1.00 22.90 ?  466  VAL C CG2 1 
ATOM   7969  N  N   . LEU C  1 443 ? 29.757  29.903  47.000  1.00 22.86 ?  467  LEU C N   1 
ATOM   7970  C  CA  . LEU C  1 443 ? 29.737  28.833  46.007  1.00 23.06 ?  467  LEU C CA  1 
ATOM   7971  C  C   . LEU C  1 443 ? 29.911  29.417  44.603  1.00 22.94 ?  467  LEU C C   1 
ATOM   7972  O  O   . LEU C  1 443 ? 30.741  28.936  43.829  1.00 23.36 ?  467  LEU C O   1 
ATOM   7973  C  CB  . LEU C  1 443 ? 28.448  28.002  46.108  1.00 23.18 ?  467  LEU C CB  1 
ATOM   7974  C  CG  . LEU C  1 443 ? 28.125  26.970  45.016  1.00 23.38 ?  467  LEU C CG  1 
ATOM   7975  C  CD1 . LEU C  1 443 ? 29.199  25.889  44.930  1.00 24.02 ?  467  LEU C CD1 1 
ATOM   7976  C  CD2 . LEU C  1 443 ? 26.754  26.342  45.263  1.00 23.70 ?  467  LEU C CD2 1 
ATOM   7977  N  N   . GLU C  1 444 ? 29.143  30.462  44.295  1.00 22.57 ?  468  GLU C N   1 
ATOM   7978  C  CA  . GLU C  1 444 ? 29.229  31.136  42.994  1.00 22.53 ?  468  GLU C CA  1 
ATOM   7979  C  C   . GLU C  1 444 ? 30.575  31.834  42.799  1.00 22.44 ?  468  GLU C C   1 
ATOM   7980  O  O   . GLU C  1 444 ? 31.081  31.908  41.678  1.00 22.24 ?  468  GLU C O   1 
ATOM   7981  C  CB  . GLU C  1 444 ? 28.049  32.099  42.780  1.00 22.23 ?  468  GLU C CB  1 
ATOM   7982  C  CG  . GLU C  1 444 ? 26.721  31.372  42.608  1.00 22.04 ?  468  GLU C CG  1 
ATOM   7983  C  CD  . GLU C  1 444 ? 25.518  32.282  42.402  1.00 22.72 ?  468  GLU C CD  1 
ATOM   7984  O  OE1 . GLU C  1 444 ? 25.540  33.465  42.818  1.00 22.60 ?  468  GLU C OE1 1 
ATOM   7985  O  OE2 . GLU C  1 444 ? 24.525  31.793  41.825  1.00 22.50 -1 468  GLU C OE2 1 
ATOM   7986  N  N   . MET C  1 445 ? 31.159  32.326  43.893  1.00 22.54 ?  469  MET C N   1 
ATOM   7987  C  CA  . MET C  1 445 ? 32.502  32.910  43.857  1.00 22.55 ?  469  MET C CA  1 
ATOM   7988  C  C   . MET C  1 445 ? 33.507  31.954  43.206  1.00 22.65 ?  469  MET C C   1 
ATOM   7989  O  O   . MET C  1 445 ? 34.311  32.369  42.371  1.00 22.80 ?  469  MET C O   1 
ATOM   7990  C  CB  . MET C  1 445 ? 32.967  33.294  45.264  1.00 22.51 ?  469  MET C CB  1 
ATOM   7991  C  CG  . MET C  1 445 ? 34.285  34.067  45.311  1.00 22.20 ?  469  MET C CG  1 
ATOM   7992  S  SD  . MET C  1 445 ? 34.701  34.561  46.992  1.00 22.60 ?  469  MET C SD  1 
ATOM   7993  C  CE  . MET C  1 445 ? 36.124  35.615  46.724  1.00 21.85 ?  469  MET C CE  1 
ATOM   7994  N  N   . ALA C  1 446 ? 33.447  30.680  43.589  1.00 22.81 ?  470  ALA C N   1 
ATOM   7995  C  CA  . ALA C  1 446 ? 34.316  29.655  43.016  1.00 23.01 ?  470  ALA C CA  1 
ATOM   7996  C  C   . ALA C  1 446 ? 33.765  29.096  41.706  1.00 23.02 ?  470  ALA C C   1 
ATOM   7997  O  O   . ALA C  1 446 ? 34.481  29.043  40.706  1.00 23.07 ?  470  ALA C O   1 
ATOM   7998  C  CB  . ALA C  1 446 ? 34.553  28.528  44.017  1.00 22.99 ?  470  ALA C CB  1 
ATOM   7999  N  N   . GLU C  1 447 ? 32.494  28.689  41.719  1.00 23.19 ?  471  GLU C N   1 
ATOM   8000  C  CA  . GLU C  1 447 ? 31.877  27.999  40.578  1.00 23.33 ?  471  GLU C CA  1 
ATOM   8001  C  C   . GLU C  1 447 ? 31.808  28.860  39.322  1.00 23.26 ?  471  GLU C C   1 
ATOM   8002  O  O   . GLU C  1 447 ? 32.027  28.368  38.210  1.00 23.47 ?  471  GLU C O   1 
ATOM   8003  C  CB  . GLU C  1 447 ? 30.471  27.504  40.940  1.00 23.43 ?  471  GLU C CB  1 
ATOM   8004  C  CG  . GLU C  1 447 ? 29.825  26.583  39.900  1.00 24.13 ?  471  GLU C CG  1 
ATOM   8005  C  CD  . GLU C  1 447 ? 30.294  25.136  39.993  1.00 25.55 ?  471  GLU C CD  1 
ATOM   8006  O  OE1 . GLU C  1 447 ? 30.940  24.766  40.997  1.00 25.71 ?  471  GLU C OE1 1 
ATOM   8007  O  OE2 . GLU C  1 447 ? 29.999  24.358  39.062  1.00 26.21 -1 471  GLU C OE2 1 
ATOM   8008  N  N   . ASN C  1 448 ? 31.499  30.140  39.505  1.00 22.93 ?  472  ASN C N   1 
ATOM   8009  C  CA  . ASN C  1 448 ? 31.287  31.041  38.380  1.00 22.78 ?  472  ASN C CA  1 
ATOM   8010  C  C   . ASN C  1 448 ? 32.480  31.947  38.129  1.00 22.64 ?  472  ASN C C   1 
ATOM   8011  O  O   . ASN C  1 448 ? 33.091  31.895  37.066  1.00 22.52 ?  472  ASN C O   1 
ATOM   8012  C  CB  . ASN C  1 448 ? 30.017  31.885  38.583  1.00 22.59 ?  472  ASN C CB  1 
ATOM   8013  C  CG  . ASN C  1 448 ? 28.746  31.045  38.644  1.00 23.16 ?  472  ASN C CG  1 
ATOM   8014  O  OD1 . ASN C  1 448 ? 28.722  29.883  38.230  1.00 23.26 ?  472  ASN C OD1 1 
ATOM   8015  N  ND2 . ASN C  1 448 ? 27.674  31.643  39.154  1.00 23.20 ?  472  ASN C ND2 1 
ATOM   8016  N  N   . ASN C  1 449 ? 32.816  32.757  39.129  1.00 22.48 ?  473  ASN C N   1 
ATOM   8017  C  CA  . ASN C  1 449 ? 33.744  33.866  38.949  1.00 22.49 ?  473  ASN C CA  1 
ATOM   8018  C  C   . ASN C  1 449 ? 35.226  33.490  38.957  1.00 22.36 ?  473  ASN C C   1 
ATOM   8019  O  O   . ASN C  1 449 ? 36.016  34.081  38.219  1.00 22.18 ?  473  ASN C O   1 
ATOM   8020  C  CB  . ASN C  1 449 ? 33.412  34.990  39.936  1.00 22.41 ?  473  ASN C CB  1 
ATOM   8021  C  CG  . ASN C  1 449 ? 31.973  35.478  39.786  1.00 22.85 ?  473  ASN C CG  1 
ATOM   8022  O  OD1 . ASN C  1 449 ? 31.161  35.347  40.701  1.00 24.15 ?  473  ASN C OD1 1 
ATOM   8023  N  ND2 . ASN C  1 449 ? 31.645  35.998  38.612  1.00 22.12 ?  473  ASN C ND2 1 
ATOM   8024  N  N   . LEU C  1 450 ? 35.594  32.501  39.769  1.00 22.32 ?  474  LEU C N   1 
ATOM   8025  C  CA  . LEU C  1 450 ? 36.951  31.946  39.740  1.00 22.06 ?  474  LEU C CA  1 
ATOM   8026  C  C   . LEU C  1 450 ? 37.176  31.190  38.430  1.00 21.61 ?  474  LEU C C   1 
ATOM   8027  O  O   . LEU C  1 450 ? 38.242  31.290  37.815  1.00 21.57 ?  474  LEU C O   1 
ATOM   8028  C  CB  . LEU C  1 450 ? 37.177  30.999  40.922  1.00 22.32 ?  474  LEU C CB  1 
ATOM   8029  C  CG  . LEU C  1 450 ? 38.544  30.846  41.614  1.00 23.46 ?  474  LEU C CG  1 
ATOM   8030  C  CD1 . LEU C  1 450 ? 38.644  29.448  42.211  1.00 23.51 ?  474  LEU C CD1 1 
ATOM   8031  C  CD2 . LEU C  1 450 ? 39.754  31.127  40.711  1.00 23.54 ?  474  LEU C CD2 1 
ATOM   8032  N  N   . ALA C  1 451 ? 36.169  30.427  38.013  1.00 21.07 ?  475  ALA C N   1 
ATOM   8033  C  CA  . ALA C  1 451 ? 36.248  29.653  36.777  1.00 20.45 ?  475  ALA C CA  1 
ATOM   8034  C  C   . ALA C  1 451 ? 36.421  30.574  35.569  1.00 20.01 ?  475  ALA C C   1 
ATOM   8035  O  O   . ALA C  1 451 ? 37.311  30.355  34.746  1.00 19.90 ?  475  ALA C O   1 
ATOM   8036  C  CB  . ALA C  1 451 ? 35.019  28.766  36.618  1.00 20.52 ?  475  ALA C CB  1 
ATOM   8037  N  N   . LYS C  1 452 ? 35.592  31.614  35.483  1.00 19.44 ?  476  LYS C N   1 
ATOM   8038  C  CA  . LYS C  1 452 ? 35.698  32.602  34.400  1.00 19.18 ?  476  LYS C CA  1 
ATOM   8039  C  C   . LYS C  1 452 ? 37.029  33.356  34.429  1.00 19.21 ?  476  LYS C C   1 
ATOM   8040  O  O   . LYS C  1 452 ? 37.588  33.663  33.370  1.00 18.87 ?  476  LYS C O   1 
ATOM   8041  C  CB  . LYS C  1 452 ? 34.515  33.574  34.408  1.00 18.93 ?  476  LYS C CB  1 
ATOM   8042  C  CG  . LYS C  1 452 ? 33.208  32.940  33.941  1.00 18.77 ?  476  LYS C CG  1 
ATOM   8043  C  CD  . LYS C  1 452 ? 32.109  33.965  33.692  1.00 18.44 ?  476  LYS C CD  1 
ATOM   8044  C  CE  . LYS C  1 452 ? 31.485  34.466  34.991  1.00 18.71 ?  476  LYS C CE  1 
ATOM   8045  N  NZ  . LYS C  1 452 ? 30.433  35.492  34.716  1.00 17.62 ?  476  LYS C NZ  1 
ATOM   8046  N  N   . MET C  1 453 ? 37.530  33.647  35.635  1.00 19.14 ?  477  MET C N   1 
ATOM   8047  C  CA  . MET C  1 453 ? 38.859  34.252  35.795  1.00 19.19 ?  477  MET C CA  1 
ATOM   8048  C  C   . MET C  1 453 ? 39.934  33.415  35.115  1.00 19.12 ?  477  MET C C   1 
ATOM   8049  O  O   . MET C  1 453 ? 40.756  33.945  34.362  1.00 18.96 ?  477  MET C O   1 
ATOM   8050  C  CB  . MET C  1 453 ? 39.222  34.448  37.271  1.00 19.19 ?  477  MET C CB  1 
ATOM   8051  C  CG  . MET C  1 453 ? 40.536  35.176  37.477  1.00 18.67 ?  477  MET C CG  1 
ATOM   8052  S  SD  . MET C  1 453 ? 40.968  35.479  39.200  1.00 19.73 ?  477  MET C SD  1 
ATOM   8053  C  CE  . MET C  1 453 ? 42.541  36.300  38.970  1.00 19.84 ?  477  MET C CE  1 
ATOM   8054  N  N   . HIS C  1 454 ? 39.919  32.112  35.388  1.00 19.27 ?  478  HIS C N   1 
ATOM   8055  C  CA  . HIS C  1 454 ? 40.861  31.188  34.767  1.00 19.40 ?  478  HIS C CA  1 
ATOM   8056  C  C   . HIS C  1 454 ? 40.678  31.118  33.250  1.00 19.19 ?  478  HIS C C   1 
ATOM   8057  O  O   . HIS C  1 454 ? 41.656  31.150  32.499  1.00 19.50 ?  478  HIS C O   1 
ATOM   8058  C  CB  . HIS C  1 454 ? 40.769  29.783  35.366  1.00 19.47 ?  478  HIS C CB  1 
ATOM   8059  C  CG  . HIS C  1 454 ? 41.451  28.749  34.526  1.00 20.09 ?  478  HIS C CG  1 
ATOM   8060  N  ND1 . HIS C  1 454 ? 42.823  28.658  34.437  1.00 20.78 ?  478  HIS C ND1 1 
ATOM   8061  C  CD2 . HIS C  1 454 ? 40.954  27.810  33.688  1.00 20.54 ?  478  HIS C CD2 1 
ATOM   8062  C  CE1 . HIS C  1 454 ? 43.142  27.692  33.594  1.00 21.98 ?  478  HIS C CE1 1 
ATOM   8063  N  NE2 . HIS C  1 454 ? 42.026  27.158  33.129  1.00 22.26 ?  478  HIS C NE2 1 
ATOM   8064  N  N   . VAL C  1 455 ? 39.427  31.016  32.808  1.00 19.16 ?  479  VAL C N   1 
ATOM   8065  C  CA  . VAL C  1 455 ? 39.109  31.002  31.377  1.00 18.90 ?  479  VAL C CA  1 
ATOM   8066  C  C   . VAL C  1 455 ? 39.638  32.265  30.700  1.00 18.63 ?  479  VAL C C   1 
ATOM   8067  O  O   . VAL C  1 455 ? 40.228  32.188  29.626  1.00 18.56 ?  479  VAL C O   1 
ATOM   8068  C  CB  . VAL C  1 455 ? 37.590  30.835  31.115  1.00 18.85 ?  479  VAL C CB  1 
ATOM   8069  C  CG1 . VAL C  1 455 ? 37.280  30.936  29.620  1.00 19.60 ?  479  VAL C CG1 1 
ATOM   8070  C  CG2 . VAL C  1 455 ? 37.105  29.504  31.642  1.00 19.04 ?  479  VAL C CG2 1 
ATOM   8071  N  N   . GLY C  1 456 ? 39.441  33.415  31.346  1.00 18.45 ?  480  GLY C N   1 
ATOM   8072  C  CA  . GLY C  1 456 ? 39.972  34.687  30.859  1.00 18.50 ?  480  GLY C CA  1 
ATOM   8073  C  C   . GLY C  1 456 ? 41.478  34.632  30.666  1.00 18.74 ?  480  GLY C C   1 
ATOM   8074  O  O   . GLY C  1 456 ? 41.994  35.028  29.616  1.00 18.75 ?  480  GLY C O   1 
ATOM   8075  N  N   . LEU C  1 457 ? 42.170  34.114  31.679  1.00 18.73 ?  481  LEU C N   1 
ATOM   8076  C  CA  . LEU C  1 457 ? 43.622  33.939  31.651  1.00 18.84 ?  481  LEU C CA  1 
ATOM   8077  C  C   . LEU C  1 457 ? 44.076  32.971  30.562  1.00 18.95 ?  481  LEU C C   1 
ATOM   8078  O  O   . LEU C  1 457 ? 44.971  33.293  29.781  1.00 19.28 ?  481  LEU C O   1 
ATOM   8079  C  CB  . LEU C  1 457 ? 44.135  33.484  33.024  1.00 18.49 ?  481  LEU C CB  1 
ATOM   8080  C  CG  . LEU C  1 457 ? 44.160  34.561  34.113  1.00 18.44 ?  481  LEU C CG  1 
ATOM   8081  C  CD1 . LEU C  1 457 ? 43.998  33.965  35.507  1.00 17.19 ?  481  LEU C CD1 1 
ATOM   8082  C  CD2 . LEU C  1 457 ? 45.440  35.393  34.024  1.00 17.71 ?  481  LEU C CD2 1 
ATOM   8083  N  N   . ALA C  1 458 ? 43.442  31.802  30.496  1.00 18.96 ?  482  ALA C N   1 
ATOM   8084  C  CA  . ALA C  1 458 ? 43.821  30.771  29.526  1.00 18.95 ?  482  ALA C CA  1 
ATOM   8085  C  C   . ALA C  1 458 ? 43.656  31.237  28.083  1.00 18.99 ?  482  ALA C C   1 
ATOM   8086  O  O   . ALA C  1 458 ? 44.385  30.796  27.192  1.00 19.09 ?  482  ALA C O   1 
ATOM   8087  C  CB  . ALA C  1 458 ? 43.021  29.492  29.766  1.00 18.77 ?  482  ALA C CB  1 
ATOM   8088  N  N   . HIS C  1 459 ? 42.703  32.139  27.862  1.00 18.90 ?  483  HIS C N   1 
ATOM   8089  C  CA  . HIS C  1 459 ? 42.334  32.537  26.509  1.00 18.81 ?  483  HIS C CA  1 
ATOM   8090  C  C   . HIS C  1 459 ? 42.656  33.992  26.174  1.00 18.67 ?  483  HIS C C   1 
ATOM   8091  O  O   . HIS C  1 459 ? 42.158  34.537  25.191  1.00 18.58 ?  483  HIS C O   1 
ATOM   8092  C  CB  . HIS C  1 459 ? 40.876  32.155  26.237  1.00 18.84 ?  483  HIS C CB  1 
ATOM   8093  C  CG  . HIS C  1 459 ? 40.644  30.676  26.294  1.00 19.22 ?  483  HIS C CG  1 
ATOM   8094  N  ND1 . HIS C  1 459 ? 40.301  30.018  27.456  1.00 19.01 ?  483  HIS C ND1 1 
ATOM   8095  C  CD2 . HIS C  1 459 ? 40.772  29.719  25.344  1.00 18.73 ?  483  HIS C CD2 1 
ATOM   8096  C  CE1 . HIS C  1 459 ? 40.194  28.724  27.210  1.00 18.82 ?  483  HIS C CE1 1 
ATOM   8097  N  NE2 . HIS C  1 459 ? 40.483  28.513  25.938  1.00 18.74 ?  483  HIS C NE2 1 
ATOM   8098  N  N   . VAL C  1 460 ? 43.510  34.594  27.006  1.00 18.70 ?  484  VAL C N   1 
ATOM   8099  C  CA  . VAL C  1 460 ? 44.203  35.857  26.717  1.00 18.47 ?  484  VAL C CA  1 
ATOM   8100  C  C   . VAL C  1 460 ? 43.254  37.057  26.548  1.00 18.81 ?  484  VAL C C   1 
ATOM   8101  O  O   . VAL C  1 460 ? 43.410  37.876  25.635  1.00 18.65 ?  484  VAL C O   1 
ATOM   8102  C  CB  . VAL C  1 460 ? 45.195  35.733  25.508  1.00 18.38 ?  484  VAL C CB  1 
ATOM   8103  C  CG1 . VAL C  1 460 ? 46.238  36.840  25.559  1.00 18.51 ?  484  VAL C CG1 1 
ATOM   8104  C  CG2 . VAL C  1 460 ? 45.890  34.366  25.490  1.00 17.99 ?  484  VAL C CG2 1 
ATOM   8105  N  N   . ASN C  1 461 ? 42.270  37.145  27.438  1.00 18.97 ?  485  ASN C N   1 
ATOM   8106  C  CA  . ASN C  1 461 ? 41.392  38.303  27.506  1.00 18.92 ?  485  ASN C CA  1 
ATOM   8107  C  C   . ASN C  1 461 ? 41.578  39.050  28.823  1.00 18.80 ?  485  ASN C C   1 
ATOM   8108  O  O   . ASN C  1 461 ? 40.990  38.667  29.834  1.00 18.92 ?  485  ASN C O   1 
ATOM   8109  C  CB  . ASN C  1 461 ? 39.926  37.905  27.325  1.00 18.96 ?  485  ASN C CB  1 
ATOM   8110  C  CG  . ASN C  1 461 ? 39.016  39.109  27.201  1.00 18.70 ?  485  ASN C CG  1 
ATOM   8111  O  OD1 . ASN C  1 461 ? 39.369  40.094  26.550  1.00 18.31 ?  485  ASN C OD1 1 
ATOM   8112  N  ND2 . ASN C  1 461 ? 37.841  39.043  27.830  1.00 17.62 ?  485  ASN C ND2 1 
ATOM   8113  N  N   . PRO C  1 462 ? 42.398  40.120  28.810  1.00 18.87 ?  486  PRO C N   1 
ATOM   8114  C  CA  . PRO C  1 462 ? 42.795  40.866  30.013  1.00 18.92 ?  486  PRO C CA  1 
ATOM   8115  C  C   . PRO C  1 462 ? 41.622  41.306  30.895  1.00 18.96 ?  486  PRO C C   1 
ATOM   8116  O  O   . PRO C  1 462 ? 41.650  41.075  32.101  1.00 19.33 ?  486  PRO C O   1 
ATOM   8117  C  CB  . PRO C  1 462 ? 43.533  42.079  29.444  1.00 18.91 ?  486  PRO C CB  1 
ATOM   8118  C  CG  . PRO C  1 462 ? 44.046  41.616  28.127  1.00 19.15 ?  486  PRO C CG  1 
ATOM   8119  C  CD  . PRO C  1 462 ? 42.991  40.701  27.590  1.00 18.75 ?  486  PRO C CD  1 
ATOM   8120  N  N   . GLY C  1 463 ? 40.606  41.927  30.299  1.00 18.99 ?  487  GLY C N   1 
ATOM   8121  C  CA  . GLY C  1 463 ? 39.406  42.323  31.035  1.00 18.91 ?  487  GLY C CA  1 
ATOM   8122  C  C   . GLY C  1 463 ? 38.673  41.137  31.646  1.00 18.98 ?  487  GLY C C   1 
ATOM   8123  O  O   . GLY C  1 463 ? 37.976  41.280  32.652  1.00 18.74 ?  487  GLY C O   1 
ATOM   8124  N  N   . GLY C  1 464 ? 38.847  39.964  31.038  1.00 18.90 ?  488  GLY C N   1 
ATOM   8125  C  CA  . GLY C  1 464 ? 38.230  38.732  31.513  1.00 19.14 ?  488  GLY C CA  1 
ATOM   8126  C  C   . GLY C  1 464 ? 38.818  38.109  32.767  1.00 19.42 ?  488  GLY C C   1 
ATOM   8127  O  O   . GLY C  1 464 ? 38.306  37.094  33.242  1.00 19.73 ?  488  GLY C O   1 
ATOM   8128  N  N   . TRP C  1 465 ? 39.889  38.692  33.307  1.00 19.55 ?  489  TRP C N   1 
ATOM   8129  C  CA  . TRP C  1 465 ? 40.403  38.256  34.608  1.00 19.70 ?  489  TRP C CA  1 
ATOM   8130  C  C   . TRP C  1 465 ? 40.652  39.389  35.592  1.00 19.96 ?  489  TRP C C   1 
ATOM   8131  O  O   . TRP C  1 465 ? 41.027  39.148  36.735  1.00 19.90 ?  489  TRP C O   1 
ATOM   8132  C  CB  . TRP C  1 465 ? 41.626  37.336  34.475  1.00 19.50 ?  489  TRP C CB  1 
ATOM   8133  C  CG  . TRP C  1 465 ? 42.963  37.994  34.202  1.00 19.24 ?  489  TRP C CG  1 
ATOM   8134  C  CD1 . TRP C  1 465 ? 43.781  38.619  35.110  1.00 19.23 ?  489  TRP C CD1 1 
ATOM   8135  C  CD2 . TRP C  1 465 ? 43.660  38.030  32.949  1.00 19.00 ?  489  TRP C CD2 1 
ATOM   8136  N  NE1 . TRP C  1 465 ? 44.933  39.058  34.490  1.00 18.81 ?  489  TRP C NE1 1 
ATOM   8137  C  CE2 . TRP C  1 465 ? 44.882  38.709  33.165  1.00 18.97 ?  489  TRP C CE2 1 
ATOM   8138  C  CE3 . TRP C  1 465 ? 43.366  37.563  31.661  1.00 18.82 ?  489  TRP C CE3 1 
ATOM   8139  C  CZ2 . TRP C  1 465 ? 45.806  38.927  32.141  1.00 18.57 ?  489  TRP C CZ2 1 
ATOM   8140  C  CZ3 . TRP C  1 465 ? 44.288  37.779  30.644  1.00 18.33 ?  489  TRP C CZ3 1 
ATOM   8141  C  CH2 . TRP C  1 465 ? 45.491  38.457  30.890  1.00 18.85 ?  489  TRP C CH2 1 
ATOM   8142  N  N   . THR C  1 466 ? 40.412  40.618  35.141  1.00 20.32 ?  490  THR C N   1 
ATOM   8143  C  CA  . THR C  1 466 ? 40.665  41.810  35.943  1.00 20.66 ?  490  THR C CA  1 
ATOM   8144  C  C   . THR C  1 466 ? 39.368  42.547  36.283  1.00 20.89 ?  490  THR C C   1 
ATOM   8145  O  O   . THR C  1 466 ? 38.695  42.199  37.252  1.00 21.20 ?  490  THR C O   1 
ATOM   8146  C  CB  . THR C  1 466 ? 41.647  42.768  35.227  1.00 20.77 ?  490  THR C CB  1 
ATOM   8147  O  OG1 . THR C  1 466 ? 41.156  43.047  33.909  1.00 20.32 ?  490  THR C OG1 1 
ATOM   8148  C  CG2 . THR C  1 466 ? 43.031  42.142  35.127  1.00 20.51 ?  490  THR C CG2 1 
ATOM   8149  N  N   . TYR C  1 467 ? 39.016  43.547  35.473  1.00 21.32 ?  491  TYR C N   1 
ATOM   8150  C  CA  . TYR C  1 467 ? 37.859  44.418  35.735  1.00 21.53 ?  491  TYR C CA  1 
ATOM   8151  C  C   . TYR C  1 467 ? 36.510  43.715  35.658  1.00 21.23 ?  491  TYR C C   1 
ATOM   8152  O  O   . TYR C  1 467 ? 35.677  43.850  36.560  1.00 21.50 ?  491  TYR C O   1 
ATOM   8153  C  CB  . TYR C  1 467 ? 37.829  45.590  34.750  1.00 21.63 ?  491  TYR C CB  1 
ATOM   8154  C  CG  . TYR C  1 467 ? 38.862  46.656  35.001  1.00 22.87 ?  491  TYR C CG  1 
ATOM   8155  C  CD1 . TYR C  1 467 ? 38.590  47.747  35.828  1.00 23.70 ?  491  TYR C CD1 1 
ATOM   8156  C  CD2 . TYR C  1 467 ? 40.110  46.583  34.400  1.00 23.46 ?  491  TYR C CD2 1 
ATOM   8157  C  CE1 . TYR C  1 467 ? 39.552  48.733  36.050  1.00 24.18 ?  491  TYR C CE1 1 
ATOM   8158  C  CE2 . TYR C  1 467 ? 41.065  47.554  34.612  1.00 23.88 ?  491  TYR C CE2 1 
ATOM   8159  C  CZ  . TYR C  1 467 ? 40.790  48.625  35.436  1.00 24.16 ?  491  TYR C CZ  1 
ATOM   8160  O  OH  . TYR C  1 467 ? 41.766  49.578  35.628  1.00 24.19 ?  491  TYR C OH  1 
ATOM   8161  N  N   . THR C  1 468 ? 36.314  42.962  34.579  1.00 21.02 ?  492  THR C N   1 
ATOM   8162  C  CA  . THR C  1 468 ? 34.982  42.570  34.124  1.00 20.63 ?  492  THR C CA  1 
ATOM   8163  C  C   . THR C  1 468 ? 34.578  41.165  34.573  1.00 20.78 ?  492  THR C C   1 
ATOM   8164  O  O   . THR C  1 468 ? 33.491  40.982  35.128  1.00 20.60 ?  492  THR C O   1 
ATOM   8165  C  CB  . THR C  1 468 ? 34.879  42.752  32.592  1.00 20.61 ?  492  THR C CB  1 
ATOM   8166  O  OG1 . THR C  1 468 ? 35.154  44.124  32.280  1.00 20.14 ?  492  THR C OG1 1 
ATOM   8167  C  CG2 . THR C  1 468 ? 33.493  42.374  32.056  1.00 20.13 ?  492  THR C CG2 1 
ATOM   8168  N  N   . GLU C  1 469 ? 35.444  40.183  34.328  1.00 20.62 ?  493  GLU C N   1 
ATOM   8169  C  CA  . GLU C  1 469 ? 35.255  38.844  34.881  1.00 20.66 ?  493  GLU C CA  1 
ATOM   8170  C  C   . GLU C  1 469 ? 36.433  38.486  35.779  1.00 20.75 ?  493  GLU C C   1 
ATOM   8171  O  O   . GLU C  1 469 ? 37.533  39.016  35.613  1.00 20.49 ?  493  GLU C O   1 
ATOM   8172  C  CB  . GLU C  1 469 ? 35.082  37.789  33.776  1.00 20.82 ?  493  GLU C CB  1 
ATOM   8173  C  CG  . GLU C  1 469 ? 33.935  38.041  32.785  1.00 21.11 ?  493  GLU C CG  1 
ATOM   8174  C  CD  . GLU C  1 469 ? 32.530  37.887  33.383  1.00 22.69 ?  493  GLU C CD  1 
ATOM   8175  O  OE1 . GLU C  1 469 ? 32.383  37.505  34.565  1.00 22.86 ?  493  GLU C OE1 1 
ATOM   8176  O  OE2 . GLU C  1 469 ? 31.555  38.155  32.652  1.00 23.57 -1 493  GLU C OE2 1 
ATOM   8177  N  N   . GLY C  1 470 ? 36.193  37.599  36.739  1.00 20.64 ?  494  GLY C N   1 
ATOM   8178  C  CA  . GLY C  1 470 ? 37.251  37.128  37.617  1.00 20.62 ?  494  GLY C CA  1 
ATOM   8179  C  C   . GLY C  1 470 ? 37.506  38.034  38.803  1.00 20.72 ?  494  GLY C C   1 
ATOM   8180  O  O   . GLY C  1 470 ? 36.727  38.040  39.753  1.00 20.92 ?  494  GLY C O   1 
ATOM   8181  N  N   . TRP C  1 471 ? 38.586  38.810  38.738  1.00 20.62 ?  495  TRP C N   1 
ATOM   8182  C  CA  . TRP C  1 471 ? 39.050  39.598  39.882  1.00 20.64 ?  495  TRP C CA  1 
ATOM   8183  C  C   . TRP C  1 471 ? 38.051  40.613  40.429  1.00 20.82 ?  495  TRP C C   1 
ATOM   8184  O  O   . TRP C  1 471 ? 37.875  40.714  41.650  1.00 20.95 ?  495  TRP C O   1 
ATOM   8185  C  CB  . TRP C  1 471 ? 40.371  40.298  39.566  1.00 20.53 ?  495  TRP C CB  1 
ATOM   8186  C  CG  . TRP C  1 471 ? 41.101  40.712  40.802  1.00 20.33 ?  495  TRP C CG  1 
ATOM   8187  C  CD1 . TRP C  1 471 ? 41.334  41.985  41.232  1.00 20.39 ?  495  TRP C CD1 1 
ATOM   8188  C  CD2 . TRP C  1 471 ? 41.679  39.846  41.779  1.00 19.90 ?  495  TRP C CD2 1 
ATOM   8189  N  NE1 . TRP C  1 471 ? 42.033  41.969  42.409  1.00 20.05 ?  495  TRP C NE1 1 
ATOM   8190  C  CE2 . TRP C  1 471 ? 42.256  40.667  42.773  1.00 20.44 ?  495  TRP C CE2 1 
ATOM   8191  C  CE3 . TRP C  1 471 ? 41.769  38.454  41.912  1.00 19.48 ?  495  TRP C CE3 1 
ATOM   8192  C  CZ2 . TRP C  1 471 ? 42.919  40.143  43.887  1.00 19.42 ?  495  TRP C CZ2 1 
ATOM   8193  C  CZ3 . TRP C  1 471 ? 42.431  37.932  43.024  1.00 20.06 ?  495  TRP C CZ3 1 
ATOM   8194  C  CH2 . TRP C  1 471 ? 42.994  38.777  43.995  1.00 19.18 ?  495  TRP C CH2 1 
ATOM   8195  N  N   . GLY C  1 472 ? 37.422  41.371  39.532  1.00 20.79 ?  496  GLY C N   1 
ATOM   8196  C  CA  . GLY C  1 472 ? 36.425  42.374  39.914  1.00 20.92 ?  496  GLY C CA  1 
ATOM   8197  C  C   . GLY C  1 472 ? 35.226  41.789  40.643  1.00 21.12 ?  496  GLY C C   1 
ATOM   8198  O  O   . GLY C  1 472 ? 34.899  42.230  41.754  1.00 21.16 ?  496  GLY C O   1 
ATOM   8199  N  N   . PRO C  1 473 ? 34.555  40.798  40.021  1.00 21.20 ?  497  PRO C N   1 
ATOM   8200  C  CA  . PRO C  1 473 ? 33.429  40.090  40.640  1.00 21.30 ?  497  PRO C CA  1 
ATOM   8201  C  C   . PRO C  1 473 ? 33.789  39.303  41.894  1.00 21.70 ?  497  PRO C C   1 
ATOM   8202  O  O   . PRO C  1 473 ? 32.988  39.259  42.830  1.00 21.63 ?  497  PRO C O   1 
ATOM   8203  C  CB  . PRO C  1 473 ? 32.964  39.147  39.529  1.00 21.32 ?  497  PRO C CB  1 
ATOM   8204  C  CG  . PRO C  1 473 ? 33.290  39.882  38.290  1.00 20.77 ?  497  PRO C CG  1 
ATOM   8205  C  CD  . PRO C  1 473 ? 34.623  40.517  38.573  1.00 21.04 ?  497  PRO C CD  1 
ATOM   8206  N  N   . MET C  1 474 ? 34.975  38.693  41.924  1.00 22.07 ?  498  MET C N   1 
ATOM   8207  C  CA  . MET C  1 474 ? 35.433  37.997  43.133  1.00 22.26 ?  498  MET C CA  1 
ATOM   8208  C  C   . MET C  1 474 ? 35.694  38.966  44.283  1.00 22.28 ?  498  MET C C   1 
ATOM   8209  O  O   . MET C  1 474 ? 35.445  38.640  45.447  1.00 22.44 ?  498  MET C O   1 
ATOM   8210  C  CB  . MET C  1 474 ? 36.676  37.154  42.857  1.00 22.40 ?  498  MET C CB  1 
ATOM   8211  C  CG  . MET C  1 474 ? 36.411  35.928  42.000  1.00 22.64 ?  498  MET C CG  1 
ATOM   8212  S  SD  . MET C  1 474 ? 37.864  34.877  41.873  1.00 24.49 ?  498  MET C SD  1 
ATOM   8213  C  CE  . MET C  1 474 ? 37.754  34.005  43.426  1.00 24.20 ?  498  MET C CE  1 
ATOM   8214  N  N   . ASN C  1 475 ? 36.190  40.155  43.946  1.00 22.23 ?  499  ASN C N   1 
ATOM   8215  C  CA  . ASN C  1 475 ? 36.389  41.228  44.920  1.00 22.15 ?  499  ASN C CA  1 
ATOM   8216  C  C   . ASN C  1 475 ? 35.072  41.620  45.593  1.00 22.24 ?  499  ASN C C   1 
ATOM   8217  O  O   . ASN C  1 475 ? 35.021  41.765  46.813  1.00 22.31 ?  499  ASN C O   1 
ATOM   8218  C  CB  . ASN C  1 475 ? 37.032  42.444  44.241  1.00 21.94 ?  499  ASN C CB  1 
ATOM   8219  C  CG  . ASN C  1 475 ? 37.336  43.571  45.207  1.00 21.90 ?  499  ASN C CG  1 
ATOM   8220  O  OD1 . ASN C  1 475 ? 38.213  43.452  46.070  1.00 22.14 ?  499  ASN C OD1 1 
ATOM   8221  N  ND2 . ASN C  1 475 ? 36.625  44.687  45.053  1.00 20.80 ?  499  ASN C ND2 1 
ATOM   8222  N  N   . ARG C  1 476 ? 34.016  41.783  44.791  1.00 22.28 ?  500  ARG C N   1 
ATOM   8223  C  CA  . ARG C  1 476 ? 32.686  42.135  45.296  1.00 22.29 ?  500  ARG C CA  1 
ATOM   8224  C  C   . ARG C  1 476 ? 32.139  41.061  46.229  1.00 22.20 ?  500  ARG C C   1 
ATOM   8225  O  O   . ARG C  1 476 ? 31.636  41.370  47.312  1.00 21.81 ?  500  ARG C O   1 
ATOM   8226  C  CB  . ARG C  1 476 ? 31.700  42.380  44.149  1.00 22.28 ?  500  ARG C CB  1 
ATOM   8227  C  CG  . ARG C  1 476 ? 30.304  42.836  44.610  1.00 22.57 ?  500  ARG C CG  1 
ATOM   8228  C  CD  . ARG C  1 476 ? 29.340  43.074  43.440  1.00 23.22 ?  500  ARG C CD  1 
ATOM   8229  N  NE  . ARG C  1 476 ? 29.964  43.867  42.389  1.00 24.86 ?  500  ARG C NE  1 
ATOM   8230  C  CZ  . ARG C  1 476 ? 30.245  43.423  41.166  1.00 24.48 ?  500  ARG C CZ  1 
ATOM   8231  N  NH1 . ARG C  1 476 ? 29.928  42.187  40.803  1.00 24.08 ?  500  ARG C NH1 1 
ATOM   8232  N  NH2 . ARG C  1 476 ? 30.834  44.232  40.298  1.00 24.99 ?  500  ARG C NH2 1 
ATOM   8233  N  N   . ALA C  1 477 ? 32.236  39.806  45.796  1.00 22.27 ?  501  ALA C N   1 
ATOM   8234  C  CA  . ALA C  1 477 ? 31.850  38.668  46.620  1.00 22.62 ?  501  ALA C CA  1 
ATOM   8235  C  C   . ALA C  1 477 ? 32.617  38.657  47.945  1.00 22.71 ?  501  ALA C C   1 
ATOM   8236  O  O   . ALA C  1 477 ? 32.018  38.454  48.995  1.00 22.63 ?  501  ALA C O   1 
ATOM   8237  C  CB  . ALA C  1 477 ? 32.057  37.366  45.867  1.00 22.50 ?  501  ALA C CB  1 
ATOM   8238  N  N   . TYR C  1 478 ? 33.929  38.896  47.889  1.00 22.92 ?  502  TYR C N   1 
ATOM   8239  C  CA  . TYR C  1 478 ? 34.760  38.933  49.096  1.00 23.13 ?  502  TYR C CA  1 
ATOM   8240  C  C   . TYR C  1 478 ? 34.269  40.032  50.038  1.00 23.27 ?  502  TYR C C   1 
ATOM   8241  O  O   . TYR C  1 478 ? 34.035  39.781  51.221  1.00 22.99 ?  502  TYR C O   1 
ATOM   8242  C  CB  . TYR C  1 478 ? 36.244  39.136  48.748  1.00 22.97 ?  502  TYR C CB  1 
ATOM   8243  C  CG  . TYR C  1 478 ? 37.172  39.227  49.955  1.00 23.15 ?  502  TYR C CG  1 
ATOM   8244  C  CD1 . TYR C  1 478 ? 37.322  40.425  50.657  1.00 23.22 ?  502  TYR C CD1 1 
ATOM   8245  C  CD2 . TYR C  1 478 ? 37.905  38.117  50.384  1.00 22.81 ?  502  TYR C CD2 1 
ATOM   8246  C  CE1 . TYR C  1 478 ? 38.168  40.519  51.761  1.00 23.56 ?  502  TYR C CE1 1 
ATOM   8247  C  CE2 . TYR C  1 478 ? 38.760  38.200  51.483  1.00 23.28 ?  502  TYR C CE2 1 
ATOM   8248  C  CZ  . TYR C  1 478 ? 38.884  39.405  52.168  1.00 24.19 ?  502  TYR C CZ  1 
ATOM   8249  O  OH  . TYR C  1 478 ? 39.717  39.499  53.261  1.00 23.98 ?  502  TYR C OH  1 
ATOM   8250  N  N   . VAL C  1 479 ? 34.098  41.234  49.490  1.00 23.53 ?  503  VAL C N   1 
ATOM   8251  C  CA  . VAL C  1 479 ? 33.661  42.402  50.252  1.00 23.87 ?  503  VAL C CA  1 
ATOM   8252  C  C   . VAL C  1 479 ? 32.310  42.152  50.923  1.00 24.25 ?  503  VAL C C   1 
ATOM   8253  O  O   . VAL C  1 479 ? 32.153  42.399  52.124  1.00 24.24 ?  503  VAL C O   1 
ATOM   8254  C  CB  . VAL C  1 479 ? 33.597  43.668  49.359  1.00 23.85 ?  503  VAL C CB  1 
ATOM   8255  C  CG1 . VAL C  1 479 ? 32.856  44.811  50.059  1.00 23.84 ?  503  VAL C CG1 1 
ATOM   8256  C  CG2 . VAL C  1 479 ? 34.993  44.112  48.968  1.00 23.57 ?  503  VAL C CG2 1 
ATOM   8257  N  N   . GLU C  1 480 ? 31.356  41.649  50.141  1.00 24.44 ?  504  GLU C N   1 
ATOM   8258  C  CA  . GLU C  1 480 ? 29.991  41.410  50.610  1.00 24.67 ?  504  GLU C CA  1 
ATOM   8259  C  C   . GLU C  1 480 ? 29.910  40.267  51.621  1.00 24.86 ?  504  GLU C C   1 
ATOM   8260  O  O   . GLU C  1 480 ? 29.054  40.281  52.505  1.00 24.92 ?  504  GLU C O   1 
ATOM   8261  C  CB  . GLU C  1 480 ? 29.044  41.161  49.428  1.00 24.54 ?  504  GLU C CB  1 
ATOM   8262  C  CG  . GLU C  1 480 ? 28.721  42.417  48.617  1.00 25.02 ?  504  GLU C CG  1 
ATOM   8263  C  CD  . GLU C  1 480 ? 27.788  42.167  47.435  1.00 25.72 ?  504  GLU C CD  1 
ATOM   8264  O  OE1 . GLU C  1 480 ? 27.361  41.012  47.228  1.00 26.34 ?  504  GLU C OE1 1 
ATOM   8265  O  OE2 . GLU C  1 480 ? 27.474  43.136  46.711  1.00 25.65 -1 504  GLU C OE2 1 
ATOM   8266  N  N   . ILE C  1 481 ? 30.796  39.282  51.480  1.00 25.26 ?  505  ILE C N   1 
ATOM   8267  C  CA  . ILE C  1 481 ? 30.910  38.192  52.451  1.00 25.62 ?  505  ILE C CA  1 
ATOM   8268  C  C   . ILE C  1 481 ? 31.394  38.729  53.805  1.00 25.81 ?  505  ILE C C   1 
ATOM   8269  O  O   . ILE C  1 481 ? 30.783  38.451  54.839  1.00 25.75 ?  505  ILE C O   1 
ATOM   8270  C  CB  . ILE C  1 481 ? 31.806  37.031  51.926  1.00 25.53 ?  505  ILE C CB  1 
ATOM   8271  C  CG1 . ILE C  1 481 ? 31.030  36.194  50.897  1.00 25.77 ?  505  ILE C CG1 1 
ATOM   8272  C  CG2 . ILE C  1 481 ? 32.284  36.133  53.071  1.00 25.85 ?  505  ILE C CG2 1 
ATOM   8273  C  CD1 . ILE C  1 481 ? 31.903  35.308  50.001  1.00 25.58 ?  505  ILE C CD1 1 
ATOM   8274  N  N   . GLN C  1 482 ? 32.466  39.518  53.782  1.00 26.09 ?  506  GLN C N   1 
ATOM   8275  C  CA  . GLN C  1 482 ? 33.017  40.127  54.994  1.00 26.61 ?  506  GLN C CA  1 
ATOM   8276  C  C   . GLN C  1 482 ? 32.010  41.052  55.678  1.00 26.80 ?  506  GLN C C   1 
ATOM   8277  O  O   . GLN C  1 482 ? 31.910  41.072  56.907  1.00 26.66 ?  506  GLN C O   1 
ATOM   8278  C  CB  . GLN C  1 482 ? 34.296  40.900  54.677  1.00 26.61 ?  506  GLN C CB  1 
ATOM   8279  C  CG  . GLN C  1 482 ? 35.470  40.034  54.230  1.00 27.59 ?  506  GLN C CG  1 
ATOM   8280  C  CD  . GLN C  1 482 ? 36.282  39.465  55.387  1.00 28.54 ?  506  GLN C CD  1 
ATOM   8281  O  OE1 . GLN C  1 482 ? 35.823  39.411  56.530  1.00 28.52 ?  506  GLN C OE1 1 
ATOM   8282  N  NE2 . GLN C  1 482 ? 37.500  39.031  55.086  1.00 29.45 ?  506  GLN C NE2 1 
ATOM   8283  N  N   . ASP C  1 483 ? 31.267  41.803  54.867  1.00 26.98 ?  507  ASP C N   1 
ATOM   8284  C  CA  . ASP C  1 483 ? 30.269  42.749  55.348  1.00 27.57 ?  507  ASP C CA  1 
ATOM   8285  C  C   . ASP C  1 483 ? 29.137  42.044  56.098  1.00 27.87 ?  507  ASP C C   1 
ATOM   8286  O  O   . ASP C  1 483 ? 28.825  42.405  57.232  1.00 27.79 ?  507  ASP C O   1 
ATOM   8287  C  CB  . ASP C  1 483 ? 29.719  43.571  54.176  1.00 27.53 ?  507  ASP C CB  1 
ATOM   8288  C  CG  . ASP C  1 483 ? 28.872  44.742  54.628  1.00 27.56 ?  507  ASP C CG  1 
ATOM   8289  O  OD1 . ASP C  1 483 ? 27.727  44.511  55.063  1.00 28.53 ?  507  ASP C OD1 1 
ATOM   8290  O  OD2 . ASP C  1 483 ? 29.344  45.895  54.531  1.00 27.24 -1 507  ASP C OD2 1 
ATOM   8291  N  N   . GLU C  1 484 ? 28.543  41.033  55.464  1.00 28.41 ?  508  GLU C N   1 
ATOM   8292  C  CA  . GLU C  1 484 ? 27.459  40.259  56.072  1.00 28.89 ?  508  GLU C CA  1 
ATOM   8293  C  C   . GLU C  1 484 ? 27.923  39.534  57.336  1.00 29.08 ?  508  GLU C C   1 
ATOM   8294  O  O   . GLU C  1 484 ? 27.192  39.474  58.323  1.00 29.03 ?  508  GLU C O   1 
ATOM   8295  C  CB  . GLU C  1 484 ? 26.866  39.266  55.064  1.00 28.81 ?  508  GLU C CB  1 
ATOM   8296  C  CG  . GLU C  1 484 ? 25.643  38.499  55.583  1.00 29.24 ?  508  GLU C CG  1 
ATOM   8297  C  CD  . GLU C  1 484 ? 24.928  37.695  54.504  1.00 29.81 ?  508  GLU C CD  1 
ATOM   8298  O  OE1 . GLU C  1 484 ? 25.228  37.882  53.304  1.00 29.74 ?  508  GLU C OE1 1 
ATOM   8299  O  OE2 . GLU C  1 484 ? 24.064  36.870  54.862  1.00 29.83 -1 508  GLU C OE2 1 
ATOM   8300  N  N   . TYR C  1 485 ? 29.138  38.993  57.294  1.00 29.50 ?  509  TYR C N   1 
ATOM   8301  C  CA  . TYR C  1 485 ? 29.743  38.326  58.448  1.00 29.91 ?  509  TYR C CA  1 
ATOM   8302  C  C   . TYR C  1 485 ? 29.861  39.264  59.656  1.00 29.99 ?  509  TYR C C   1 
ATOM   8303  O  O   . TYR C  1 485 ? 29.475  38.898  60.772  1.00 29.84 ?  509  TYR C O   1 
ATOM   8304  C  CB  . TYR C  1 485 ? 31.111  37.760  58.059  1.00 30.17 ?  509  TYR C CB  1 
ATOM   8305  C  CG  . TYR C  1 485 ? 31.874  37.066  59.165  1.00 31.14 ?  509  TYR C CG  1 
ATOM   8306  C  CD1 . TYR C  1 485 ? 31.378  35.912  59.771  1.00 32.15 ?  509  TYR C CD1 1 
ATOM   8307  C  CD2 . TYR C  1 485 ? 33.113  37.549  59.582  1.00 32.54 ?  509  TYR C CD2 1 
ATOM   8308  C  CE1 . TYR C  1 485 ? 32.090  35.265  60.780  1.00 33.69 ?  509  TYR C CE1 1 
ATOM   8309  C  CE2 . TYR C  1 485 ? 33.836  36.911  60.588  1.00 33.98 ?  509  TYR C CE2 1 
ATOM   8310  C  CZ  . TYR C  1 485 ? 33.318  35.771  61.181  1.00 34.33 ?  509  TYR C CZ  1 
ATOM   8311  O  OH  . TYR C  1 485 ? 34.030  35.142  62.175  1.00 36.09 ?  509  TYR C OH  1 
ATOM   8312  N  N   . THR C  1 486 ? 30.382  40.467  59.421  1.00 30.02 ?  510  THR C N   1 
ATOM   8313  C  CA  . THR C  1 486 ? 30.525  41.475  60.472  1.00 30.46 ?  510  THR C CA  1 
ATOM   8314  C  C   . THR C  1 486 ? 29.157  41.938  60.985  1.00 30.84 ?  510  THR C C   1 
ATOM   8315  O  O   . THR C  1 486 ? 28.952  42.027  62.200  1.00 30.99 ?  510  THR C O   1 
ATOM   8316  C  CB  . THR C  1 486 ? 31.391  42.677  60.007  1.00 30.41 ?  510  THR C CB  1 
ATOM   8317  O  OG1 . THR C  1 486 ? 32.715  42.219  59.707  1.00 30.05 ?  510  THR C OG1 1 
ATOM   8318  C  CG2 . THR C  1 486 ? 31.480  43.753  61.091  1.00 30.22 ?  510  THR C CG2 1 
ATOM   8319  N  N   . LYS C  1 487 ? 28.235  42.212  60.059  1.00 31.19 ?  511  LYS C N   1 
ATOM   8320  C  CA  . LYS C  1 487 ? 26.844  42.548  60.391  1.00 31.52 ?  511  LYS C CA  1 
ATOM   8321  C  C   . LYS C  1 487 ? 26.174  41.472  61.248  1.00 32.05 ?  511  LYS C C   1 
ATOM   8322  O  O   . LYS C  1 487 ? 25.520  41.788  62.247  1.00 32.15 ?  511  LYS C O   1 
ATOM   8323  C  CB  . LYS C  1 487 ? 26.015  42.767  59.121  1.00 31.30 ?  511  LYS C CB  1 
ATOM   8324  C  CG  . LYS C  1 487 ? 26.085  44.168  58.533  1.00 30.69 ?  511  LYS C CG  1 
ATOM   8325  C  CD  . LYS C  1 487 ? 25.049  44.322  57.423  1.00 29.74 ?  511  LYS C CD  1 
ATOM   8326  C  CE  . LYS C  1 487 ? 24.930  45.761  56.939  1.00 29.37 ?  511  LYS C CE  1 
ATOM   8327  N  NZ  . LYS C  1 487 ? 26.126  46.216  56.182  1.00 28.49 ?  511  LYS C NZ  1 
ATOM   8328  N  N   . MET C  1 488 ? 26.337  40.208  60.854  1.00 32.49 ?  512  MET C N   1 
ATOM   8329  C  CA  . MET C  1 488 ? 25.747  39.086  61.587  1.00 33.33 ?  512  MET C CA  1 
ATOM   8330  C  C   . MET C  1 488 ? 26.430  38.844  62.939  1.00 33.94 ?  512  MET C C   1 
ATOM   8331  O  O   . MET C  1 488 ? 25.795  38.359  63.874  1.00 33.80 ?  512  MET C O   1 
ATOM   8332  C  CB  . MET C  1 488 ? 25.738  37.803  60.743  1.00 33.09 ?  512  MET C CB  1 
ATOM   8333  C  CG  . MET C  1 488 ? 24.735  37.824  59.581  1.00 33.49 ?  512  MET C CG  1 
ATOM   8334  S  SD  . MET C  1 488 ? 24.642  36.280  58.644  1.00 33.32 ?  512  MET C SD  1 
ATOM   8335  C  CE  . MET C  1 488 ? 23.746  35.242  59.800  1.00 33.24 ?  512  MET C CE  1 
ATOM   8336  N  N   . GLN C  1 489 ? 27.715  39.187  63.031  1.00 34.81 ?  513  GLN C N   1 
ATOM   8337  C  CA  . GLN C  1 489 ? 28.447  39.110  64.296  1.00 35.88 ?  513  GLN C CA  1 
ATOM   8338  C  C   . GLN C  1 489 ? 27.910  40.101  65.320  1.00 36.29 ?  513  GLN C C   1 
ATOM   8339  O  O   . GLN C  1 489 ? 27.678  39.737  66.473  1.00 36.21 ?  513  GLN C O   1 
ATOM   8340  C  CB  . GLN C  1 489 ? 29.948  39.336  64.093  1.00 35.92 ?  513  GLN C CB  1 
ATOM   8341  C  CG  . GLN C  1 489 ? 30.753  38.063  63.854  1.00 37.07 ?  513  GLN C CG  1 
ATOM   8342  C  CD  . GLN C  1 489 ? 32.254  38.285  64.004  1.00 38.85 ?  513  GLN C CD  1 
ATOM   8343  O  OE1 . GLN C  1 489 ? 32.807  39.259  63.485  1.00 40.02 ?  513  GLN C OE1 1 
ATOM   8344  N  NE2 . GLN C  1 489 ? 32.919  37.380  64.718  1.00 39.01 ?  513  GLN C NE2 1 
ATOM   8345  N  N   . GLU C  1 490 ? 27.703  41.346  64.899  1.00 37.08 ?  514  GLU C N   1 
ATOM   8346  C  CA  . GLU C  1 490 ? 27.249  42.382  65.827  1.00 38.05 ?  514  GLU C CA  1 
ATOM   8347  C  C   . GLU C  1 490 ? 25.775  42.241  66.196  1.00 38.39 ?  514  GLU C C   1 
ATOM   8348  O  O   . GLU C  1 490 ? 25.371  42.616  67.298  1.00 38.60 ?  514  GLU C O   1 
ATOM   8349  C  CB  . GLU C  1 490 ? 27.593  43.797  65.331  1.00 38.14 ?  514  GLU C CB  1 
ATOM   8350  C  CG  . GLU C  1 490 ? 27.173  44.124  63.910  1.00 39.10 ?  514  GLU C CG  1 
ATOM   8351  C  CD  . GLU C  1 490 ? 28.018  45.223  63.273  1.00 39.97 ?  514  GLU C CD  1 
ATOM   8352  O  OE1 . GLU C  1 490 ? 29.157  45.476  63.726  1.00 40.29 ?  514  GLU C OE1 1 
ATOM   8353  O  OE2 . GLU C  1 490 ? 27.539  45.833  62.299  1.00 40.47 -1 514  GLU C OE2 1 
ATOM   8354  N  N   . LEU C  1 491 ? 24.990  41.675  65.280  1.00 38.91 ?  515  LEU C N   1 
ATOM   8355  C  CA  . LEU C  1 491 ? 23.587  41.354  65.531  1.00 39.43 ?  515  LEU C CA  1 
ATOM   8356  C  C   . LEU C  1 491 ? 23.466  40.183  66.511  1.00 39.75 ?  515  LEU C C   1 
ATOM   8357  O  O   . LEU C  1 491 ? 22.558  40.155  67.346  1.00 39.51 ?  515  LEU C O   1 
ATOM   8358  C  CB  . LEU C  1 491 ? 22.867  41.048  64.210  1.00 39.51 ?  515  LEU C CB  1 
ATOM   8359  C  CG  . LEU C  1 491 ? 21.335  40.994  64.102  1.00 40.00 ?  515  LEU C CG  1 
ATOM   8360  C  CD1 . LEU C  1 491 ? 20.801  39.573  64.269  1.00 40.86 ?  515  LEU C CD1 1 
ATOM   8361  C  CD2 . LEU C  1 491 ? 20.627  41.968  65.050  1.00 40.03 ?  515  LEU C CD2 1 
ATOM   8362  N  N   . SER C  1 492 ? 24.389  39.228  66.402  1.00 40.26 ?  516  SER C N   1 
ATOM   8363  C  CA  . SER C  1 492 ? 24.500  38.123  67.354  1.00 40.92 ?  516  SER C CA  1 
ATOM   8364  C  C   . SER C  1 492 ? 24.835  38.648  68.752  1.00 41.39 ?  516  SER C C   1 
ATOM   8365  O  O   . SER C  1 492 ? 24.239  38.218  69.741  1.00 41.33 ?  516  SER C O   1 
ATOM   8366  C  CB  . SER C  1 492 ? 25.561  37.124  66.893  1.00 40.80 ?  516  SER C CB  1 
ATOM   8367  O  OG  . SER C  1 492 ? 25.680  36.043  67.797  1.00 41.15 ?  516  SER C OG  1 
ATOM   8368  N  N   . ALA C  1 493 ? 25.781  39.584  68.814  1.00 42.04 ?  517  ALA C N   1 
ATOM   8369  C  CA  . ALA C  1 493 ? 26.195  40.219  70.066  1.00 42.86 ?  517  ALA C CA  1 
ATOM   8370  C  C   . ALA C  1 493 ? 25.073  41.053  70.683  1.00 43.49 ?  517  ALA C C   1 
ATOM   8371  O  O   . ALA C  1 493 ? 24.972  41.152  71.907  1.00 43.48 ?  517  ALA C O   1 
ATOM   8372  C  CB  . ALA C  1 493 ? 27.430  41.079  69.842  1.00 42.67 ?  517  ALA C CB  1 
ATOM   8373  N  N   . LEU C  1 494 ? 24.241  41.647  69.825  1.00 44.33 ?  518  LEU C N   1 
ATOM   8374  C  CA  . LEU C  1 494 ? 23.081  42.425  70.258  1.00 45.08 ?  518  LEU C CA  1 
ATOM   8375  C  C   . LEU C  1 494 ? 21.989  41.520  70.818  1.00 45.71 ?  518  LEU C C   1 
ATOM   8376  O  O   . LEU C  1 494 ? 21.329  41.874  71.798  1.00 45.79 ?  518  LEU C O   1 
ATOM   8377  C  CB  . LEU C  1 494 ? 22.533  43.279  69.108  1.00 45.00 ?  518  LEU C CB  1 
ATOM   8378  C  CG  . LEU C  1 494 ? 21.395  44.268  69.398  1.00 45.12 ?  518  LEU C CG  1 
ATOM   8379  C  CD1 . LEU C  1 494 ? 21.843  45.394  70.326  1.00 45.34 ?  518  LEU C CD1 1 
ATOM   8380  C  CD2 . LEU C  1 494 ? 20.831  44.841  68.103  1.00 45.22 ?  518  LEU C CD2 1 
ATOM   8381  N  N   . GLN C  1 495 ? 21.809  40.356  70.194  1.00 46.55 ?  519  GLN C N   1 
ATOM   8382  C  CA  . GLN C  1 495 ? 20.865  39.349  70.676  1.00 47.37 ?  519  GLN C CA  1 
ATOM   8383  C  C   . GLN C  1 495 ? 21.328  38.756  72.009  1.00 47.81 ?  519  GLN C C   1 
ATOM   8384  O  O   . GLN C  1 495 ? 20.504  38.379  72.846  1.00 47.93 ?  519  GLN C O   1 
ATOM   8385  C  CB  . GLN C  1 495 ? 20.663  38.240  69.635  1.00 47.50 ?  519  GLN C CB  1 
ATOM   8386  C  CG  . GLN C  1 495 ? 19.451  37.340  69.914  1.00 48.34 ?  519  GLN C CG  1 
ATOM   8387  C  CD  . GLN C  1 495 ? 19.171  36.334  68.806  1.00 49.43 ?  519  GLN C CD  1 
ATOM   8388  O  OE1 . GLN C  1 495 ? 20.062  35.603  68.370  1.00 49.95 ?  519  GLN C OE1 1 
ATOM   8389  N  NE2 . GLN C  1 495 ? 17.921  36.285  68.357  1.00 49.53 ?  519  GLN C NE2 1 
ATOM   8390  N  N   . ALA C  1 496 ? 22.645  38.680  72.194  1.00 48.28 ?  520  ALA C N   1 
ATOM   8391  C  CA  . ALA C  1 496 ? 23.235  38.198  73.441  1.00 48.82 ?  520  ALA C CA  1 
ATOM   8392  C  C   . ALA C  1 496 ? 22.974  39.168  74.597  1.00 49.19 ?  520  ALA C C   1 
ATOM   8393  O  O   . ALA C  1 496 ? 22.751  38.742  75.732  1.00 49.21 ?  520  ALA C O   1 
ATOM   8394  C  CB  . ALA C  1 496 ? 24.729  37.963  73.267  1.00 48.73 ?  520  ALA C CB  1 
ATOM   8395  N  N   . ARG C  1 497 ? 23.002  40.466  74.298  1.00 49.71 ?  521  ARG C N   1 
ATOM   8396  C  CA  . ARG C  1 497 ? 22.743  41.504  75.297  1.00 50.27 ?  521  ARG C CA  1 
ATOM   8397  C  C   . ARG C  1 497 ? 21.274  41.538  75.720  1.00 50.69 ?  521  ARG C C   1 
ATOM   8398  O  O   . ARG C  1 497 ? 20.967  41.807  76.885  1.00 50.78 ?  521  ARG C O   1 
ATOM   8399  C  CB  . ARG C  1 497 ? 23.193  42.877  74.792  1.00 50.19 ?  521  ARG C CB  1 
ATOM   8400  C  CG  . ARG C  1 497 ? 24.706  43.021  74.666  1.00 50.50 ?  521  ARG C CG  1 
ATOM   8401  C  CD  . ARG C  1 497 ? 25.138  44.477  74.711  1.00 50.74 ?  521  ARG C CD  1 
ATOM   8402  N  NE  . ARG C  1 497 ? 24.783  45.206  73.499  1.00 50.97 ?  521  ARG C NE  1 
ATOM   8403  C  CZ  . ARG C  1 497 ? 24.592  46.521  73.433  1.00 51.11 ?  521  ARG C CZ  1 
ATOM   8404  N  NH1 . ARG C  1 497 ? 24.702  47.281  74.517  1.00 51.13 ?  521  ARG C NH1 1 
ATOM   8405  N  NH2 . ARG C  1 497 ? 24.279  47.077  72.275  1.00 51.13 ?  521  ARG C NH2 1 
ATOM   8406  N  N   . VAL C  1 498 ? 20.380  41.262  74.773  1.00 51.16 ?  522  VAL C N   1 
ATOM   8407  C  CA  . VAL C  1 498 ? 18.950  41.135  75.054  1.00 51.72 ?  522  VAL C CA  1 
ATOM   8408  C  C   . VAL C  1 498 ? 18.694  39.848  75.848  1.00 52.23 ?  522  VAL C C   1 
ATOM   8409  O  O   . VAL C  1 498 ? 17.881  39.831  76.778  1.00 52.35 ?  522  VAL C O   1 
ATOM   8410  C  CB  . VAL C  1 498 ? 18.101  41.175  73.750  1.00 51.67 ?  522  VAL C CB  1 
ATOM   8411  C  CG1 . VAL C  1 498 ? 16.631  40.871  74.031  1.00 51.55 ?  522  VAL C CG1 1 
ATOM   8412  C  CG2 . VAL C  1 498 ? 18.234  42.535  73.070  1.00 51.53 ?  522  VAL C CG2 1 
ATOM   8413  N  N   . ASN C  1 499 ? 19.410  38.786  75.479  1.00 52.75 ?  523  ASN C N   1 
ATOM   8414  C  CA  . ASN C  1 499 ? 19.369  37.509  76.190  1.00 53.32 ?  523  ASN C CA  1 
ATOM   8415  C  C   . ASN C  1 499 ? 19.665  37.644  77.688  1.00 53.66 ?  523  ASN C C   1 
ATOM   8416  O  O   . ASN C  1 499 ? 18.940  37.084  78.514  1.00 53.72 ?  523  ASN C O   1 
ATOM   8417  C  CB  . ASN C  1 499 ? 20.325  36.502  75.528  1.00 53.25 ?  523  ASN C CB  1 
ATOM   8418  C  CG  . ASN C  1 499 ? 20.527  35.239  76.353  1.00 53.74 ?  523  ASN C CG  1 
ATOM   8419  O  OD1 . ASN C  1 499 ? 19.569  34.613  76.816  1.00 53.75 ?  523  ASN C OD1 1 
ATOM   8420  N  ND2 . ASN C  1 499 ? 21.787  34.849  76.526  1.00 54.25 ?  523  ASN C ND2 1 
ATOM   8421  N  N   . LYS C  1 500 ? 20.712  38.393  78.036  1.00 54.06 ?  524  LYS C N   1 
ATOM   8422  C  CA  . LYS C  1 500 ? 21.073  38.575  79.447  1.00 54.51 ?  524  LYS C CA  1 
ATOM   8423  C  C   . LYS C  1 500 ? 20.305  39.704  80.153  1.00 54.59 ?  524  LYS C C   1 
ATOM   8424  O  O   . LYS C  1 500 ? 20.586  40.027  81.311  1.00 54.57 ?  524  LYS C O   1 
ATOM   8425  C  CB  . LYS C  1 500 ? 22.599  38.673  79.648  1.00 54.57 ?  524  LYS C CB  1 
ATOM   8426  C  CG  . LYS C  1 500 ? 23.257  39.994  79.272  1.00 55.21 ?  524  LYS C CG  1 
ATOM   8427  C  CD  . LYS C  1 500 ? 24.691  40.027  79.804  1.00 56.09 ?  524  LYS C CD  1 
ATOM   8428  C  CE  . LYS C  1 500 ? 25.363  41.380  79.597  1.00 56.59 ?  524  LYS C CE  1 
ATOM   8429  N  NZ  . LYS C  1 500 ? 25.815  41.591  78.192  1.00 56.98 ?  524  LYS C NZ  1 
ATOM   8430  N  N   . LEU C  1 501 ? 19.340  40.295  79.448  1.00 54.71 ?  525  LEU C N   1 
ATOM   8431  C  CA  . LEU C  1 501 ? 18.387  41.228  80.054  1.00 54.96 ?  525  LEU C CA  1 
ATOM   8432  C  C   . LEU C  1 501 ? 17.089  40.514  80.426  1.00 55.10 ?  525  LEU C C   1 
ATOM   8433  O  O   . LEU C  1 501 ? 16.309  41.009  81.242  1.00 55.20 ?  525  LEU C O   1 
ATOM   8434  C  CB  . LEU C  1 501 ? 18.088  42.402  79.117  1.00 54.92 ?  525  LEU C CB  1 
ATOM   8435  C  CG  . LEU C  1 501 ? 19.087  43.560  79.064  1.00 55.04 ?  525  LEU C CG  1 
ATOM   8436  C  CD1 . LEU C  1 501 ? 18.793  44.452  77.868  1.00 55.25 ?  525  LEU C CD1 1 
ATOM   8437  C  CD2 . LEU C  1 501 ? 19.075  44.372  80.354  1.00 55.09 ?  525  LEU C CD2 1 
ATOM   8438  N  N   . GLU C  1 502 ? 16.870  39.350  79.818  1.00 55.28 ?  526  GLU C N   1 
ATOM   8439  C  CA  . GLU C  1 502 ? 15.700  38.524  80.100  1.00 55.41 ?  526  GLU C CA  1 
ATOM   8440  C  C   . GLU C  1 502 ? 15.968  37.556  81.251  1.00 55.44 ?  526  GLU C C   1 
ATOM   8441  O  O   . GLU C  1 502 ? 17.089  37.076  81.429  1.00 55.46 ?  526  GLU C O   1 
ATOM   8442  C  CB  . GLU C  1 502 ? 15.273  37.753  78.848  1.00 55.49 ?  526  GLU C CB  1 
ATOM   8443  C  CG  . GLU C  1 502 ? 14.773  38.635  77.710  1.00 55.63 ?  526  GLU C CG  1 
ATOM   8444  C  CD  . GLU C  1 502 ? 14.566  37.871  76.413  1.00 56.11 ?  526  GLU C CD  1 
ATOM   8445  O  OE1 . GLU C  1 502 ? 15.447  37.069  76.034  1.00 56.07 ?  526  GLU C OE1 1 
ATOM   8446  O  OE2 . GLU C  1 502 ? 13.521  38.083  75.763  1.00 56.41 ?  526  GLU C OE2 1 
ATOM   8447  N  N   . SER D  2 1   ? 45.748  7.292   45.311  1.00 46.42 ?  28   SER D N   1 
ATOM   8448  C  CA  . SER D  2 1   ? 45.501  8.110   46.537  1.00 46.23 ?  28   SER D CA  1 
ATOM   8449  C  C   . SER D  2 1   ? 45.692  9.604   46.277  1.00 45.92 ?  28   SER D C   1 
ATOM   8450  O  O   . SER D  2 1   ? 46.455  10.000  45.393  1.00 46.15 ?  28   SER D O   1 
ATOM   8451  C  CB  . SER D  2 1   ? 46.397  7.642   47.690  1.00 46.40 ?  28   SER D CB  1 
ATOM   8452  O  OG  . SER D  2 1   ? 47.751  7.543   47.282  1.00 47.03 ?  28   SER D OG  1 
ATOM   8453  N  N   . SER D  2 2   ? 44.992  10.420  47.061  1.00 45.37 ?  29   SER D N   1 
ATOM   8454  C  CA  . SER D  2 2   ? 44.970  11.868  46.880  1.00 44.69 ?  29   SER D CA  1 
ATOM   8455  C  C   . SER D  2 2   ? 46.274  12.551  47.292  1.00 44.12 ?  29   SER D C   1 
ATOM   8456  O  O   . SER D  2 2   ? 47.047  12.016  48.091  1.00 44.28 ?  29   SER D O   1 
ATOM   8457  C  CB  . SER D  2 2   ? 43.807  12.477  47.670  1.00 44.84 ?  29   SER D CB  1 
ATOM   8458  O  OG  . SER D  2 2   ? 42.567  11.913  47.282  1.00 45.18 ?  29   SER D OG  1 
ATOM   8459  N  N   . LEU D  2 3   ? 46.508  13.732  46.722  1.00 43.13 ?  30   LEU D N   1 
ATOM   8460  C  CA  . LEU D  2 3   ? 47.563  14.634  47.167  1.00 42.10 ?  30   LEU D CA  1 
ATOM   8461  C  C   . LEU D  2 3   ? 47.134  15.329  48.455  1.00 41.30 ?  30   LEU D C   1 
ATOM   8462  O  O   . LEU D  2 3   ? 45.945  15.587  48.661  1.00 41.19 ?  30   LEU D O   1 
ATOM   8463  C  CB  . LEU D  2 3   ? 47.844  15.686  46.090  1.00 42.22 ?  30   LEU D CB  1 
ATOM   8464  C  CG  . LEU D  2 3   ? 49.103  15.649  45.210  1.00 42.33 ?  30   LEU D CG  1 
ATOM   8465  C  CD1 . LEU D  2 3   ? 49.611  14.242  44.903  1.00 42.10 ?  30   LEU D CD1 1 
ATOM   8466  C  CD2 . LEU D  2 3   ? 48.851  16.434  43.922  1.00 42.33 ?  30   LEU D CD2 1 
ATOM   8467  N  N   . ALA D  2 4   ? 48.101  15.625  49.320  1.00 40.22 ?  31   ALA D N   1 
ATOM   8468  C  CA  . ALA D  2 4   ? 47.837  16.419  50.517  1.00 39.15 ?  31   ALA D CA  1 
ATOM   8469  C  C   . ALA D  2 4   ? 47.491  17.848  50.101  1.00 38.25 ?  31   ALA D C   1 
ATOM   8470  O  O   . ALA D  2 4   ? 48.173  18.419  49.246  1.00 38.21 ?  31   ALA D O   1 
ATOM   8471  C  CB  . ALA D  2 4   ? 49.036  16.407  51.447  1.00 39.16 ?  31   ALA D CB  1 
ATOM   8472  N  N   . PRO D  2 5   ? 46.425  18.422  50.694  1.00 37.34 ?  32   PRO D N   1 
ATOM   8473  C  CA  . PRO D  2 5   ? 45.974  19.769  50.328  1.00 36.58 ?  32   PRO D CA  1 
ATOM   8474  C  C   . PRO D  2 5   ? 47.008  20.851  50.641  1.00 35.78 ?  32   PRO D C   1 
ATOM   8475  O  O   . PRO D  2 5   ? 47.535  20.909  51.756  1.00 35.66 ?  32   PRO D O   1 
ATOM   8476  C  CB  . PRO D  2 5   ? 44.711  19.967  51.180  1.00 36.60 ?  32   PRO D CB  1 
ATOM   8477  C  CG  . PRO D  2 5   ? 44.276  18.589  51.559  1.00 37.10 ?  32   PRO D CG  1 
ATOM   8478  C  CD  . PRO D  2 5   ? 45.546  17.811  51.707  1.00 37.31 ?  32   PRO D CD  1 
ATOM   8479  N  N   . ILE D  2 6   ? 47.308  21.676  49.641  1.00 34.56 ?  33   ILE D N   1 
ATOM   8480  C  CA  . ILE D  2 6   ? 48.172  22.840  49.816  1.00 33.53 ?  33   ILE D CA  1 
ATOM   8481  C  C   . ILE D  2 6   ? 47.420  24.075  49.329  1.00 32.85 ?  33   ILE D C   1 
ATOM   8482  O  O   . ILE D  2 6   ? 46.954  24.116  48.184  1.00 32.67 ?  33   ILE D O   1 
ATOM   8483  C  CB  . ILE D  2 6   ? 49.519  22.709  49.050  1.00 33.52 ?  33   ILE D CB  1 
ATOM   8484  C  CG1 . ILE D  2 6   ? 50.218  21.384  49.381  1.00 33.82 ?  33   ILE D CG1 1 
ATOM   8485  C  CG2 . ILE D  2 6   ? 50.435  23.889  49.371  1.00 33.04 ?  33   ILE D CG2 1 
ATOM   8486  C  CD1 . ILE D  2 6   ? 51.382  21.039  48.458  1.00 34.00 ?  33   ILE D CD1 1 
ATOM   8487  N  N   . SER D  2 7   ? 47.302  25.074  50.200  1.00 31.90 ?  34   SER D N   1 
ATOM   8488  C  CA  . SER D  2 7   ? 46.570  26.298  49.876  1.00 31.16 ?  34   SER D CA  1 
ATOM   8489  C  C   . SER D  2 7   ? 47.211  27.028  48.699  1.00 30.62 ?  34   SER D C   1 
ATOM   8490  O  O   . SER D  2 7   ? 48.421  26.917  48.472  1.00 30.45 ?  34   SER D O   1 
ATOM   8491  C  CB  . SER D  2 7   ? 46.469  27.220  51.097  1.00 31.03 ?  34   SER D CB  1 
ATOM   8492  O  OG  . SER D  2 7   ? 47.673  27.931  51.310  1.00 30.74 ?  34   SER D OG  1 
ATOM   8493  N  N   . ALA D  2 8   ? 46.389  27.765  47.955  1.00 29.96 ?  35   ALA D N   1 
ATOM   8494  C  CA  . ALA D  2 8   ? 46.846  28.498  46.775  1.00 29.53 ?  35   ALA D CA  1 
ATOM   8495  C  C   . ALA D  2 8   ? 47.969  29.484  47.098  1.00 29.11 ?  35   ALA D C   1 
ATOM   8496  O  O   . ALA D  2 8   ? 48.930  29.605  46.337  1.00 28.59 ?  35   ALA D O   1 
ATOM   8497  C  CB  . ALA D  2 8   ? 45.684  29.205  46.103  1.00 29.30 ?  35   ALA D CB  1 
ATOM   8498  N  N   . LYS D  2 9   ? 47.851  30.168  48.235  1.00 28.94 ?  36   LYS D N   1 
ATOM   8499  C  CA  . LYS D  2 9   ? 48.872  31.120  48.673  1.00 28.92 ?  36   LYS D CA  1 
ATOM   8500  C  C   . LYS D  2 9   ? 50.226  30.438  48.895  1.00 28.62 ?  36   LYS D C   1 
ATOM   8501  O  O   . LYS D  2 9   ? 51.268  30.993  48.534  1.00 28.66 ?  36   LYS D O   1 
ATOM   8502  C  CB  . LYS D  2 9   ? 48.411  31.901  49.915  1.00 28.93 ?  36   LYS D CB  1 
ATOM   8503  C  CG  . LYS D  2 9   ? 48.850  31.346  51.261  1.00 30.09 ?  36   LYS D CG  1 
ATOM   8504  C  CD  . LYS D  2 9   ? 48.294  32.179  52.415  1.00 31.48 ?  36   LYS D CD  1 
ATOM   8505  C  CE  . LYS D  2 9   ? 49.195  32.102  53.650  1.00 32.42 ?  36   LYS D CE  1 
ATOM   8506  N  NZ  . LYS D  2 9   ? 49.486  30.705  54.083  1.00 32.07 ?  36   LYS D NZ  1 
ATOM   8507  N  N   . ASP D  2 10  ? 50.198  29.229  49.459  1.00 28.20 ?  37   ASP D N   1 
ATOM   8508  C  CA  . ASP D  2 10  ? 51.411  28.445  49.673  1.00 28.05 ?  37   ASP D CA  1 
ATOM   8509  C  C   . ASP D  2 10  ? 51.967  27.915  48.351  1.00 28.00 ?  37   ASP D C   1 
ATOM   8510  O  O   . ASP D  2 10  ? 53.182  27.866  48.162  1.00 27.90 ?  37   ASP D O   1 
ATOM   8511  C  CB  . ASP D  2 10  ? 51.170  27.305  50.677  1.00 27.94 ?  37   ASP D CB  1 
ATOM   8512  C  CG  . ASP D  2 10  ? 50.939  27.811  52.098  1.00 27.94 ?  37   ASP D CG  1 
ATOM   8513  O  OD1 . ASP D  2 10  ? 50.172  27.176  52.848  1.00 27.93 ?  37   ASP D OD1 1 
ATOM   8514  O  OD2 . ASP D  2 10  ? 51.516  28.852  52.470  1.00 28.47 ?  37   ASP D OD2 1 
ATOM   8515  N  N   . MET D  2 11  ? 51.072  27.539  47.440  1.00 28.02 ?  38   MET D N   1 
ATOM   8516  C  CA  . MET D  2 11  ? 51.454  27.137  46.083  1.00 28.28 ?  38   MET D CA  1 
ATOM   8517  C  C   . MET D  2 11  ? 52.149  28.274  45.331  1.00 28.22 ?  38   MET D C   1 
ATOM   8518  O  O   . MET D  2 11  ? 53.117  28.047  44.613  1.00 28.28 ?  38   MET D O   1 
ATOM   8519  C  CB  . MET D  2 11  ? 50.234  26.652  45.292  1.00 28.27 ?  38   MET D CB  1 
ATOM   8520  C  CG  . MET D  2 11  ? 49.708  25.272  45.690  1.00 28.76 ?  38   MET D CG  1 
ATOM   8521  S  SD  . MET D  2 11  ? 50.919  23.932  45.583  1.00 30.45 ?  38   MET D SD  1 
ATOM   8522  C  CE  . MET D  2 11  ? 51.404  23.997  43.856  1.00 29.59 ?  38   MET D CE  1 
ATOM   8523  N  N   . LEU D  2 12  ? 51.647  29.493  45.515  1.00 28.47 ?  39   LEU D N   1 
ATOM   8524  C  CA  . LEU D  2 12  ? 52.206  30.697  44.894  1.00 28.62 ?  39   LEU D CA  1 
ATOM   8525  C  C   . LEU D  2 12  ? 53.590  31.041  45.444  1.00 28.64 ?  39   LEU D C   1 
ATOM   8526  O  O   . LEU D  2 12  ? 54.506  31.354  44.684  1.00 28.65 ?  39   LEU D O   1 
ATOM   8527  C  CB  . LEU D  2 12  ? 51.257  31.878  45.105  1.00 28.45 ?  39   LEU D CB  1 
ATOM   8528  C  CG  . LEU D  2 12  ? 50.419  32.520  43.988  1.00 29.14 ?  39   LEU D CG  1 
ATOM   8529  C  CD1 . LEU D  2 12  ? 50.521  31.855  42.610  1.00 28.88 ?  39   LEU D CD1 1 
ATOM   8530  C  CD2 . LEU D  2 12  ? 48.968  32.670  44.444  1.00 28.22 ?  39   LEU D CD2 1 
ATOM   8531  N  N   . ASP D  2 13  ? 53.727  30.989  46.767  1.00 28.78 ?  40   ASP D N   1 
ATOM   8532  C  CA  . ASP D  2 13  ? 55.003  31.248  47.427  1.00 29.10 ?  40   ASP D CA  1 
ATOM   8533  C  C   . ASP D  2 13  ? 56.044  30.214  47.007  1.00 29.31 ?  40   ASP D C   1 
ATOM   8534  O  O   . ASP D  2 13  ? 57.198  30.561  46.745  1.00 29.32 ?  40   ASP D O   1 
ATOM   8535  C  CB  . ASP D  2 13  ? 54.832  31.266  48.950  1.00 28.87 ?  40   ASP D CB  1 
ATOM   8536  C  CG  . ASP D  2 13  ? 53.985  32.433  49.434  1.00 28.86 ?  40   ASP D CG  1 
ATOM   8537  O  OD1 . ASP D  2 13  ? 53.735  33.370  48.643  1.00 28.47 ?  40   ASP D OD1 1 
ATOM   8538  O  OD2 . ASP D  2 13  ? 53.570  32.414  50.614  1.00 28.51 ?  40   ASP D OD2 1 
ATOM   8539  N  N   . TYR D  2 14  ? 55.618  28.955  46.923  1.00 29.67 ?  41   TYR D N   1 
ATOM   8540  C  CA  . TYR D  2 14  ? 56.470  27.869  46.441  1.00 30.33 ?  41   TYR D CA  1 
ATOM   8541  C  C   . TYR D  2 14  ? 56.962  28.111  45.013  1.00 30.46 ?  41   TYR D C   1 
ATOM   8542  O  O   . TYR D  2 14  ? 58.134  27.877  44.713  1.00 30.39 ?  41   TYR D O   1 
ATOM   8543  C  CB  . TYR D  2 14  ? 55.738  26.525  46.536  1.00 30.51 ?  41   TYR D CB  1 
ATOM   8544  C  CG  . TYR D  2 14  ? 56.568  25.336  46.105  1.00 31.56 ?  41   TYR D CG  1 
ATOM   8545  C  CD1 . TYR D  2 14  ? 57.580  24.836  46.923  1.00 32.35 ?  41   TYR D CD1 1 
ATOM   8546  C  CD2 . TYR D  2 14  ? 56.339  24.709  44.878  1.00 32.66 ?  41   TYR D CD2 1 
ATOM   8547  C  CE1 . TYR D  2 14  ? 58.346  23.747  46.534  1.00 33.33 ?  41   TYR D CE1 1 
ATOM   8548  C  CE2 . TYR D  2 14  ? 57.102  23.611  44.478  1.00 33.35 ?  41   TYR D CE2 1 
ATOM   8549  C  CZ  . TYR D  2 14  ? 58.102  23.139  45.313  1.00 33.73 ?  41   TYR D CZ  1 
ATOM   8550  O  OH  . TYR D  2 14  ? 58.862  22.058  44.935  1.00 35.00 ?  41   TYR D OH  1 
ATOM   8551  N  N   . LEU D  2 15  ? 56.064  28.575  44.143  1.00 30.66 ?  42   LEU D N   1 
ATOM   8552  C  CA  . LEU D  2 15  ? 56.410  28.870  42.753  1.00 30.90 ?  42   LEU D CA  1 
ATOM   8553  C  C   . LEU D  2 15  ? 57.299  30.106  42.632  1.00 31.15 ?  42   LEU D C   1 
ATOM   8554  O  O   . LEU D  2 15  ? 58.210  30.136  41.805  1.00 31.00 ?  42   LEU D O   1 
ATOM   8555  C  CB  . LEU D  2 15  ? 55.153  29.029  41.893  1.00 30.84 ?  42   LEU D CB  1 
ATOM   8556  C  CG  . LEU D  2 15  ? 54.447  27.748  41.442  1.00 30.82 ?  42   LEU D CG  1 
ATOM   8557  C  CD1 . LEU D  2 15  ? 53.050  28.076  40.938  1.00 31.33 ?  42   LEU D CD1 1 
ATOM   8558  C  CD2 . LEU D  2 15  ? 55.251  27.004  40.374  1.00 30.24 ?  42   LEU D CD2 1 
ATOM   8559  N  N   . ALA D  2 16  ? 57.034  31.111  43.465  1.00 31.51 ?  43   ALA D N   1 
ATOM   8560  C  CA  . ALA D  2 16  ? 57.857  32.324  43.520  1.00 32.14 ?  43   ALA D CA  1 
ATOM   8561  C  C   . ALA D  2 16  ? 59.312  32.026  43.901  1.00 32.55 ?  43   ALA D C   1 
ATOM   8562  O  O   . ALA D  2 16  ? 60.199  32.855  43.693  1.00 32.62 ?  43   ALA D O   1 
ATOM   8563  C  CB  . ALA D  2 16  ? 57.252  33.331  44.490  1.00 31.97 ?  43   ALA D CB  1 
ATOM   8564  N  N   . CYS D  2 17  ? 59.543  30.834  44.443  1.00 33.13 ?  44   CYS D N   1 
ATOM   8565  C  CA  . CYS D  2 17  ? 60.860  30.437  44.933  1.00 33.96 ?  44   CYS D CA  1 
ATOM   8566  C  C   . CYS D  2 17  ? 61.614  29.469  44.014  1.00 34.78 ?  44   CYS D C   1 
ATOM   8567  O  O   . CYS D  2 17  ? 62.685  28.969  44.374  1.00 34.81 ?  44   CYS D O   1 
ATOM   8568  C  CB  . CYS D  2 17  ? 60.736  29.866  46.347  1.00 33.61 ?  44   CYS D CB  1 
ATOM   8569  S  SG  . CYS D  2 17  ? 60.412  31.150  47.567  1.00 32.70 ?  44   CYS D SG  1 
ATOM   8570  N  N   . LYS D  2 18  ? 61.064  29.215  42.828  1.00 35.74 ?  45   LYS D N   1 
ATOM   8571  C  CA  . LYS D  2 18  ? 61.753  28.385  41.841  1.00 36.64 ?  45   LYS D CA  1 
ATOM   8572  C  C   . LYS D  2 18  ? 62.942  29.133  41.243  1.00 36.84 ?  45   LYS D C   1 
ATOM   8573  O  O   . LYS D  2 18  ? 62.827  30.303  40.876  1.00 37.03 ?  45   LYS D O   1 
ATOM   8574  C  CB  . LYS D  2 18  ? 60.793  27.891  40.749  1.00 36.80 ?  45   LYS D CB  1 
ATOM   8575  C  CG  . LYS D  2 18  ? 59.841  26.759  41.188  1.00 37.89 ?  45   LYS D CG  1 
ATOM   8576  C  CD  . LYS D  2 18  ? 60.560  25.414  41.406  1.00 39.47 ?  45   LYS D CD  1 
ATOM   8577  C  CE  . LYS D  2 18  ? 60.936  25.191  42.872  1.00 40.28 ?  45   LYS D CE  1 
ATOM   8578  N  NZ  . LYS D  2 18  ? 62.042  24.197  43.026  1.00 41.06 ?  45   LYS D NZ  1 
ATOM   8579  N  N   . ASP D  2 19  ? 64.078  28.439  41.161  1.00 37.21 ?  46   ASP D N   1 
ATOM   8580  C  CA  . ASP D  2 19  ? 65.369  29.024  40.764  1.00 37.66 ?  46   ASP D CA  1 
ATOM   8581  C  C   . ASP D  2 19  ? 65.859  30.117  41.726  1.00 37.40 ?  46   ASP D C   1 
ATOM   8582  O  O   . ASP D  2 19  ? 66.603  31.026  41.337  1.00 37.44 ?  46   ASP D O   1 
ATOM   8583  C  CB  . ASP D  2 19  ? 65.346  29.521  39.308  1.00 38.02 ?  46   ASP D CB  1 
ATOM   8584  C  CG  . ASP D  2 19  ? 65.459  28.390  38.297  1.00 39.14 ?  46   ASP D CG  1 
ATOM   8585  O  OD1 . ASP D  2 19  ? 65.120  28.623  37.117  1.00 40.85 ?  46   ASP D OD1 1 
ATOM   8586  O  OD2 . ASP D  2 19  ? 65.882  27.272  38.673  1.00 40.49 ?  46   ASP D OD2 1 
ATOM   8587  N  N   . LYS D  2 20  ? 65.435  30.013  42.983  1.00 37.09 ?  47   LYS D N   1 
ATOM   8588  C  CA  . LYS D  2 20  ? 65.889  30.914  44.037  1.00 36.74 ?  47   LYS D CA  1 
ATOM   8589  C  C   . LYS D  2 20  ? 66.543  30.130  45.169  1.00 36.30 ?  47   LYS D C   1 
ATOM   8590  O  O   . LYS D  2 20  ? 66.293  28.932  45.337  1.00 36.30 ?  47   LYS D O   1 
ATOM   8591  C  CB  . LYS D  2 20  ? 64.738  31.782  44.563  1.00 36.81 ?  47   LYS D CB  1 
ATOM   8592  C  CG  . LYS D  2 20  ? 64.094  32.654  43.489  1.00 37.62 ?  47   LYS D CG  1 
ATOM   8593  C  CD  . LYS D  2 20  ? 63.995  34.109  43.915  1.00 38.74 ?  47   LYS D CD  1 
ATOM   8594  C  CE  . LYS D  2 20  ? 63.833  35.012  42.698  1.00 39.01 ?  47   LYS D CE  1 
ATOM   8595  N  NZ  . LYS D  2 20  ? 64.398  36.367  42.944  1.00 40.01 ?  47   LYS D NZ  1 
ATOM   8596  N  N   . LYS D  2 21  ? 67.398  30.808  45.927  1.00 35.69 ?  48   LYS D N   1 
ATOM   8597  C  CA  . LYS D  2 21  ? 68.059  30.201  47.076  1.00 35.18 ?  48   LYS D CA  1 
ATOM   8598  C  C   . LYS D  2 21  ? 67.084  30.100  48.249  1.00 34.48 ?  48   LYS D C   1 
ATOM   8599  O  O   . LYS D  2 21  ? 66.162  30.911  48.355  1.00 34.28 ?  48   LYS D O   1 
ATOM   8600  C  CB  . LYS D  2 21  ? 69.296  31.012  47.475  1.00 35.45 ?  48   LYS D CB  1 
ATOM   8601  C  CG  . LYS D  2 21  ? 70.396  31.042  46.421  1.00 36.15 ?  48   LYS D CG  1 
ATOM   8602  C  CD  . LYS D  2 21  ? 71.596  31.844  46.901  1.00 37.93 ?  48   LYS D CD  1 
ATOM   8603  C  CE  . LYS D  2 21  ? 72.545  32.152  45.751  1.00 39.23 ?  48   LYS D CE  1 
ATOM   8604  N  NZ  . LYS D  2 21  ? 73.798  32.807  46.224  1.00 40.80 ?  48   LYS D NZ  1 
ATOM   8605  N  N   . PRO D  2 22  ? 67.271  29.095  49.127  1.00 33.88 ?  49   PRO D N   1 
ATOM   8606  C  CA  . PRO D  2 22  ? 66.444  28.974  50.334  1.00 33.33 ?  49   PRO D CA  1 
ATOM   8607  C  C   . PRO D  2 22  ? 66.486  30.201  51.257  1.00 32.86 ?  49   PRO D C   1 
ATOM   8608  O  O   . PRO D  2 22  ? 65.536  30.434  52.007  1.00 32.73 ?  49   PRO D O   1 
ATOM   8609  C  CB  . PRO D  2 22  ? 67.038  27.755  51.040  1.00 33.22 ?  49   PRO D CB  1 
ATOM   8610  C  CG  . PRO D  2 22  ? 67.590  26.929  49.934  1.00 33.43 ?  49   PRO D CG  1 
ATOM   8611  C  CD  . PRO D  2 22  ? 68.142  27.916  48.946  1.00 33.75 ?  49   PRO D CD  1 
ATOM   8612  N  N   . THR D  2 23  ? 67.567  30.976  51.198  1.00 32.34 ?  50   THR D N   1 
ATOM   8613  C  CA  . THR D  2 23  ? 67.688  32.191  52.015  1.00 31.98 ?  50   THR D CA  1 
ATOM   8614  C  C   . THR D  2 23  ? 67.093  33.433  51.350  1.00 31.54 ?  50   THR D C   1 
ATOM   8615  O  O   . THR D  2 23  ? 66.996  34.488  51.978  1.00 31.25 ?  50   THR D O   1 
ATOM   8616  C  CB  . THR D  2 23  ? 69.149  32.488  52.411  1.00 31.97 ?  50   THR D CB  1 
ATOM   8617  O  OG1 . THR D  2 23  ? 69.977  32.468  51.244  1.00 32.20 ?  50   THR D OG1 1 
ATOM   8618  C  CG2 . THR D  2 23  ? 69.651  31.465  53.405  1.00 31.94 ?  50   THR D CG2 1 
ATOM   8619  N  N   . ASP D  2 24  ? 66.703  33.306  50.082  1.00 31.14 ?  51   ASP D N   1 
ATOM   8620  C  CA  . ASP D  2 24  ? 66.060  34.407  49.368  1.00 30.85 ?  51   ASP D CA  1 
ATOM   8621  C  C   . ASP D  2 24  ? 64.697  34.730  49.970  1.00 30.43 ?  51   ASP D C   1 
ATOM   8622  O  O   . ASP D  2 24  ? 63.955  33.832  50.381  1.00 30.10 ?  51   ASP D O   1 
ATOM   8623  C  CB  . ASP D  2 24  ? 65.916  34.087  47.879  1.00 31.03 ?  51   ASP D CB  1 
ATOM   8624  C  CG  . ASP D  2 24  ? 67.210  34.275  47.111  1.00 31.01 ?  51   ASP D CG  1 
ATOM   8625  O  OD1 . ASP D  2 24  ? 67.399  33.581  46.093  1.00 30.97 ?  51   ASP D OD1 1 
ATOM   8626  O  OD2 . ASP D  2 24  ? 68.034  35.118  47.519  1.00 31.74 ?  51   ASP D OD2 1 
ATOM   8627  N  N   . VAL D  2 25  ? 64.392  36.022  50.031  1.00 30.05 ?  52   VAL D N   1 
ATOM   8628  C  CA  . VAL D  2 25  ? 63.131  36.498  50.583  1.00 29.67 ?  52   VAL D CA  1 
ATOM   8629  C  C   . VAL D  2 25  ? 62.293  37.128  49.475  1.00 29.41 ?  52   VAL D C   1 
ATOM   8630  O  O   . VAL D  2 25  ? 62.700  38.113  48.857  1.00 29.71 ?  52   VAL D O   1 
ATOM   8631  C  CB  . VAL D  2 25  ? 63.353  37.495  51.748  1.00 29.78 ?  52   VAL D CB  1 
ATOM   8632  C  CG1 . VAL D  2 25  ? 62.022  38.031  52.264  1.00 29.51 ?  52   VAL D CG1 1 
ATOM   8633  C  CG2 . VAL D  2 25  ? 64.128  36.823  52.883  1.00 29.54 ?  52   VAL D CG2 1 
ATOM   8634  N  N   . VAL D  2 26  ? 61.130  36.537  49.223  1.00 29.00 ?  53   VAL D N   1 
ATOM   8635  C  CA  . VAL D  2 26  ? 60.218  37.012  48.185  1.00 28.51 ?  53   VAL D CA  1 
ATOM   8636  C  C   . VAL D  2 26  ? 58.944  37.616  48.781  1.00 28.19 ?  53   VAL D C   1 
ATOM   8637  O  O   . VAL D  2 26  ? 58.558  37.296  49.906  1.00 27.89 ?  53   VAL D O   1 
ATOM   8638  C  CB  . VAL D  2 26  ? 59.829  35.880  47.189  1.00 28.60 ?  53   VAL D CB  1 
ATOM   8639  C  CG1 . VAL D  2 26  ? 61.075  35.272  46.537  1.00 28.27 ?  53   VAL D CG1 1 
ATOM   8640  C  CG2 . VAL D  2 26  ? 58.981  34.796  47.877  1.00 27.99 ?  53   VAL D CG2 1 
ATOM   8641  N  N   . LYS D  2 27  ? 58.302  38.490  48.012  1.00 27.79 ?  54   LYS D N   1 
ATOM   8642  C  CA  . LYS D  2 27  ? 56.978  38.987  48.356  1.00 27.50 ?  54   LYS D CA  1 
ATOM   8643  C  C   . LYS D  2 27  ? 55.920  37.931  48.089  1.00 27.18 ?  54   LYS D C   1 
ATOM   8644  O  O   . LYS D  2 27  ? 56.010  37.181  47.111  1.00 27.23 ?  54   LYS D O   1 
ATOM   8645  C  CB  . LYS D  2 27  ? 56.648  40.254  47.563  1.00 27.57 ?  54   LYS D CB  1 
ATOM   8646  C  CG  . LYS D  2 27  ? 57.090  41.533  48.254  1.00 27.71 ?  54   LYS D CG  1 
ATOM   8647  C  CD  . LYS D  2 27  ? 56.684  42.774  47.471  1.00 27.58 ?  54   LYS D CD  1 
ATOM   8648  C  CE  . LYS D  2 27  ? 57.644  43.054  46.335  1.00 27.12 ?  54   LYS D CE  1 
ATOM   8649  N  NZ  . LYS D  2 27  ? 57.173  44.178  45.482  1.00 27.33 ?  54   LYS D NZ  1 
ATOM   8650  N  N   . SER D  2 28  ? 54.929  37.877  48.977  1.00 26.80 ?  55   SER D N   1 
ATOM   8651  C  CA  . SER D  2 28  ? 53.705  37.119  48.756  1.00 26.47 ?  55   SER D CA  1 
ATOM   8652  C  C   . SER D  2 28  ? 52.992  37.628  47.502  1.00 26.38 ?  55   SER D C   1 
ATOM   8653  O  O   . SER D  2 28  ? 53.166  38.781  47.100  1.00 26.36 ?  55   SER D O   1 
ATOM   8654  C  CB  . SER D  2 28  ? 52.777  37.254  49.970  1.00 26.56 ?  55   SER D CB  1 
ATOM   8655  O  OG  . SER D  2 28  ? 51.540  36.575  49.779  1.00 26.14 ?  55   SER D OG  1 
ATOM   8656  N  N   . HIS D  2 29  ? 52.205  36.757  46.882  1.00 26.24 ?  56   HIS D N   1 
ATOM   8657  C  CA  . HIS D  2 29  ? 51.360  37.156  45.759  1.00 26.37 ?  56   HIS D CA  1 
ATOM   8658  C  C   . HIS D  2 29  ? 49.931  37.464  46.212  1.00 26.22 ?  56   HIS D C   1 
ATOM   8659  O  O   . HIS D  2 29  ? 49.121  37.942  45.420  1.00 26.44 ?  56   HIS D O   1 
ATOM   8660  C  CB  . HIS D  2 29  ? 51.345  36.065  44.682  1.00 26.25 ?  56   HIS D CB  1 
ATOM   8661  C  CG  . HIS D  2 29  ? 52.580  36.031  43.833  1.00 26.33 ?  56   HIS D CG  1 
ATOM   8662  N  ND1 . HIS D  2 29  ? 53.773  35.500  44.273  1.00 25.82 ?  56   HIS D ND1 1 
ATOM   8663  C  CD2 . HIS D  2 29  ? 52.800  36.451  42.565  1.00 26.45 ?  56   HIS D CD2 1 
ATOM   8664  C  CE1 . HIS D  2 29  ? 54.678  35.601  43.315  1.00 26.00 ?  56   HIS D CE1 1 
ATOM   8665  N  NE2 . HIS D  2 29  ? 54.113  36.174  42.267  1.00 25.97 ?  56   HIS D NE2 1 
ATOM   8666  N  N   . THR D  2 30  ? 49.632  37.205  47.485  1.00 25.98 ?  57   THR D N   1 
ATOM   8667  C  CA  . THR D  2 30  ? 48.251  37.238  47.982  1.00 25.84 ?  57   THR D CA  1 
ATOM   8668  C  C   . THR D  2 30  ? 48.028  38.026  49.280  1.00 26.11 ?  57   THR D C   1 
ATOM   8669  O  O   . THR D  2 30  ? 46.948  38.588  49.491  1.00 25.73 ?  57   THR D O   1 
ATOM   8670  C  CB  . THR D  2 30  ? 47.709  35.805  48.200  1.00 25.89 ?  57   THR D CB  1 
ATOM   8671  O  OG1 . THR D  2 30  ? 48.511  35.127  49.178  1.00 25.13 ?  57   THR D OG1 1 
ATOM   8672  C  CG2 . THR D  2 30  ? 47.726  35.010  46.900  1.00 25.35 ?  57   THR D CG2 1 
ATOM   8673  N  N   . GLU D  2 31  ? 49.041  38.065  50.144  1.00 26.40 ?  58   GLU D N   1 
ATOM   8674  C  CA  . GLU D  2 31  ? 48.854  38.555  51.512  1.00 26.75 ?  58   GLU D CA  1 
ATOM   8675  C  C   . GLU D  2 31  ? 49.338  39.976  51.757  1.00 26.98 ?  58   GLU D C   1 
ATOM   8676  O  O   . GLU D  2 31  ? 50.451  40.347  51.383  1.00 27.11 ?  58   GLU D O   1 
ATOM   8677  C  CB  . GLU D  2 31  ? 49.504  37.602  52.527  1.00 26.89 ?  58   GLU D CB  1 
ATOM   8678  C  CG  . GLU D  2 31  ? 49.069  36.139  52.405  1.00 26.74 ?  58   GLU D CG  1 
ATOM   8679  C  CD  . GLU D  2 31  ? 47.563  35.965  52.423  1.00 27.57 ?  58   GLU D CD  1 
ATOM   8680  O  OE1 . GLU D  2 31  ? 46.994  35.557  51.383  1.00 27.38 ?  58   GLU D OE1 1 
ATOM   8681  O  OE2 . GLU D  2 31  ? 46.945  36.238  53.475  1.00 27.98 ?  58   GLU D OE2 1 
ATOM   8682  N  N   . VAL D  2 32  ? 48.474  40.765  52.388  1.00 27.28 ?  59   VAL D N   1 
ATOM   8683  C  CA  . VAL D  2 32  ? 48.808  42.103  52.858  1.00 27.47 ?  59   VAL D CA  1 
ATOM   8684  C  C   . VAL D  2 32  ? 48.479  42.164  54.349  1.00 27.57 ?  59   VAL D C   1 
ATOM   8685  O  O   . VAL D  2 32  ? 47.355  41.871  54.753  1.00 27.55 ?  59   VAL D O   1 
ATOM   8686  C  CB  . VAL D  2 32  ? 48.021  43.205  52.092  1.00 27.40 ?  59   VAL D CB  1 
ATOM   8687  C  CG1 . VAL D  2 32  ? 48.179  44.571  52.768  1.00 27.43 ?  59   VAL D CG1 1 
ATOM   8688  C  CG2 . VAL D  2 32  ? 48.465  43.284  50.639  1.00 27.50 ?  59   VAL D CG2 1 
ATOM   8689  N  N   . GLU D  2 33  ? 49.468  42.527  55.159  1.00 27.77 ?  60   GLU D N   1 
ATOM   8690  C  CA  . GLU D  2 33  ? 49.271  42.703  56.597  1.00 28.04 ?  60   GLU D CA  1 
ATOM   8691  C  C   . GLU D  2 33  ? 49.944  43.991  57.048  1.00 28.00 ?  60   GLU D C   1 
ATOM   8692  O  O   . GLU D  2 33  ? 51.078  44.269  56.663  1.00 27.87 ?  60   GLU D O   1 
ATOM   8693  C  CB  . GLU D  2 33  ? 49.818  41.507  57.391  1.00 28.03 ?  60   GLU D CB  1 
ATOM   8694  C  CG  . GLU D  2 33  ? 49.154  40.156  57.090  1.00 29.06 ?  60   GLU D CG  1 
ATOM   8695  C  CD  . GLU D  2 33  ? 47.720  40.039  57.601  1.00 30.42 ?  60   GLU D CD  1 
ATOM   8696  O  OE1 . GLU D  2 33  ? 46.993  39.160  57.094  1.00 30.90 ?  60   GLU D OE1 1 
ATOM   8697  O  OE2 . GLU D  2 33  ? 47.320  40.805  58.508  1.00 30.64 ?  60   GLU D OE2 1 
ATOM   8698  N  N   . ASN D  2 34  ? 49.230  44.773  57.855  1.00 28.26 ?  61   ASN D N   1 
ATOM   8699  C  CA  . ASN D  2 34  ? 49.729  46.048  58.389  1.00 28.72 ?  61   ASN D CA  1 
ATOM   8700  C  C   . ASN D  2 34  ? 50.171  47.044  57.306  1.00 28.51 ?  61   ASN D C   1 
ATOM   8701  O  O   . ASN D  2 34  ? 51.184  47.737  57.456  1.00 28.59 ?  61   ASN D O   1 
ATOM   8702  C  CB  . ASN D  2 34  ? 50.846  45.812  59.424  1.00 28.91 ?  61   ASN D CB  1 
ATOM   8703  C  CG  . ASN D  2 34  ? 50.412  44.893  60.559  1.00 30.46 ?  61   ASN D CG  1 
ATOM   8704  O  OD1 . ASN D  2 34  ? 51.094  43.915  60.875  1.00 32.64 ?  61   ASN D OD1 1 
ATOM   8705  N  ND2 . ASN D  2 34  ? 49.271  45.202  61.175  1.00 31.36 ?  61   ASN D ND2 1 
ATOM   8706  N  N   . GLY D  2 35  ? 49.407  47.101  56.216  1.00 28.34 ?  62   GLY D N   1 
ATOM   8707  C  CA  . GLY D  2 35  ? 49.684  48.016  55.107  1.00 28.12 ?  62   GLY D CA  1 
ATOM   8708  C  C   . GLY D  2 35  ? 50.871  47.647  54.231  1.00 28.20 ?  62   GLY D C   1 
ATOM   8709  O  O   . GLY D  2 35  ? 51.365  48.479  53.463  1.00 28.19 ?  62   GLY D O   1 
ATOM   8710  N  N   . LYS D  2 36  ? 51.336  46.403  54.341  1.00 28.19 ?  63   LYS D N   1 
ATOM   8711  C  CA  . LYS D  2 36  ? 52.469  45.929  53.543  1.00 28.49 ?  63   LYS D CA  1 
ATOM   8712  C  C   . LYS D  2 36  ? 52.232  44.507  53.048  1.00 28.34 ?  63   LYS D C   1 
ATOM   8713  O  O   . LYS D  2 36  ? 51.557  43.718  53.711  1.00 28.21 ?  63   LYS D O   1 
ATOM   8714  C  CB  . LYS D  2 36  ? 53.779  45.979  54.349  1.00 28.58 ?  63   LYS D CB  1 
ATOM   8715  C  CG  . LYS D  2 36  ? 54.183  47.371  54.843  1.00 29.38 ?  63   LYS D CG  1 
ATOM   8716  C  CD  . LYS D  2 36  ? 55.638  47.425  55.291  1.00 30.54 ?  63   LYS D CD  1 
ATOM   8717  C  CE  . LYS D  2 36  ? 55.976  48.801  55.860  1.00 31.96 ?  63   LYS D CE  1 
ATOM   8718  N  NZ  . LYS D  2 36  ? 57.413  49.171  55.671  1.00 32.70 ?  63   LYS D NZ  1 
ATOM   8719  N  N   . ILE D  2 37  ? 52.786  44.192  51.878  1.00 28.23 ?  64   ILE D N   1 
ATOM   8720  C  CA  . ILE D  2 37  ? 52.813  42.822  51.380  1.00 28.14 ?  64   ILE D CA  1 
ATOM   8721  C  C   . ILE D  2 37  ? 53.703  41.992  52.299  1.00 28.19 ?  64   ILE D C   1 
ATOM   8722  O  O   . ILE D  2 37  ? 54.819  42.399  52.627  1.00 28.23 ?  64   ILE D O   1 
ATOM   8723  C  CB  . ILE D  2 37  ? 53.339  42.741  49.924  1.00 28.16 ?  64   ILE D CB  1 
ATOM   8724  C  CG1 . ILE D  2 37  ? 52.439  43.548  48.977  1.00 28.29 ?  64   ILE D CG1 1 
ATOM   8725  C  CG2 . ILE D  2 37  ? 53.446  41.279  49.460  1.00 27.86 ?  64   ILE D CG2 1 
ATOM   8726  C  CD1 . ILE D  2 37  ? 53.028  43.758  47.576  1.00 28.26 ?  64   ILE D CD1 1 
ATOM   8727  N  N   . VAL D  2 38  ? 53.186  40.846  52.733  1.00 28.33 ?  65   VAL D N   1 
ATOM   8728  C  CA  . VAL D  2 38  ? 53.929  39.920  53.581  1.00 28.50 ?  65   VAL D CA  1 
ATOM   8729  C  C   . VAL D  2 38  ? 55.123  39.364  52.801  1.00 28.76 ?  65   VAL D C   1 
ATOM   8730  O  O   . VAL D  2 38  ? 54.999  39.048  51.612  1.00 28.71 ?  65   VAL D O   1 
ATOM   8731  C  CB  . VAL D  2 38  ? 53.009  38.770  54.088  1.00 28.52 ?  65   VAL D CB  1 
ATOM   8732  C  CG1 . VAL D  2 38  ? 53.789  37.738  54.906  1.00 28.39 ?  65   VAL D CG1 1 
ATOM   8733  C  CG2 . VAL D  2 38  ? 51.858  39.332  54.909  1.00 28.16 ?  65   VAL D CG2 1 
ATOM   8734  N  N   . ARG D  2 39  ? 56.279  39.277  53.459  1.00 28.84 ?  66   ARG D N   1 
ATOM   8735  C  CA  . ARG D  2 39  ? 57.460  38.661  52.850  1.00 29.12 ?  66   ARG D CA  1 
ATOM   8736  C  C   . ARG D  2 39  ? 57.581  37.216  53.315  1.00 29.21 ?  66   ARG D C   1 
ATOM   8737  O  O   . ARG D  2 39  ? 57.269  36.890  54.465  1.00 29.16 ?  66   ARG D O   1 
ATOM   8738  C  CB  . ARG D  2 39  ? 58.745  39.438  53.177  1.00 29.15 ?  66   ARG D CB  1 
ATOM   8739  C  CG  . ARG D  2 39  ? 58.606  40.964  53.192  1.00 30.11 ?  66   ARG D CG  1 
ATOM   8740  C  CD  . ARG D  2 39  ? 58.571  41.615  51.809  1.00 29.75 ?  66   ARG D CD  1 
ATOM   8741  N  NE  . ARG D  2 39  ? 57.525  42.634  51.780  1.00 30.98 ?  66   ARG D NE  1 
ATOM   8742  C  CZ  . ARG D  2 39  ? 57.521  43.736  51.033  1.00 30.15 ?  66   ARG D CZ  1 
ATOM   8743  N  NH1 . ARG D  2 39  ? 58.524  44.024  50.217  1.00 29.62 ?  66   ARG D NH1 1 
ATOM   8744  N  NH2 . ARG D  2 39  ? 56.494  44.563  51.117  1.00 29.79 ?  66   ARG D NH2 1 
ATOM   8745  N  N   . VAL D  2 40  ? 58.024  36.349  52.411  1.00 29.41 ?  67   VAL D N   1 
ATOM   8746  C  CA  . VAL D  2 40  ? 58.187  34.934  52.715  1.00 29.67 ?  67   VAL D CA  1 
ATOM   8747  C  C   . VAL D  2 40  ? 59.614  34.490  52.388  1.00 30.18 ?  67   VAL D C   1 
ATOM   8748  O  O   . VAL D  2 40  ? 60.139  34.763  51.295  1.00 29.83 ?  67   VAL D O   1 
ATOM   8749  C  CB  . VAL D  2 40  ? 57.150  34.051  51.951  1.00 29.88 ?  67   VAL D CB  1 
ATOM   8750  C  CG1 . VAL D  2 40  ? 57.375  32.565  52.232  1.00 29.58 ?  67   VAL D CG1 1 
ATOM   8751  C  CG2 . VAL D  2 40  ? 55.719  34.444  52.322  1.00 29.53 ?  67   VAL D CG2 1 
ATOM   8752  N  N   . LYS D  2 41  ? 60.237  33.819  53.353  1.00 30.48 ?  68   LYS D N   1 
ATOM   8753  C  CA  . LYS D  2 41  ? 61.544  33.211  53.152  1.00 31.04 ?  68   LYS D CA  1 
ATOM   8754  C  C   . LYS D  2 41  ? 61.371  31.904  52.384  1.00 31.06 ?  68   LYS D C   1 
ATOM   8755  O  O   . LYS D  2 41  ? 60.566  31.054  52.772  1.00 30.97 ?  68   LYS D O   1 
ATOM   8756  C  CB  . LYS D  2 41  ? 62.224  32.969  54.499  1.00 31.02 ?  68   LYS D CB  1 
ATOM   8757  C  CG  . LYS D  2 41  ? 63.639  32.429  54.406  1.00 32.23 ?  68   LYS D CG  1 
ATOM   8758  C  CD  . LYS D  2 41  ? 64.212  32.233  55.801  1.00 33.45 ?  68   LYS D CD  1 
ATOM   8759  C  CE  . LYS D  2 41  ? 65.277  31.172  55.803  1.00 33.99 ?  68   LYS D CE  1 
ATOM   8760  N  NZ  . LYS D  2 41  ? 65.508  30.641  57.176  1.00 34.85 ?  68   LYS D NZ  1 
ATOM   8761  N  N   . CYS D  2 42  ? 62.132  31.754  51.299  1.00 31.35 ?  69   CYS D N   1 
ATOM   8762  C  CA  . CYS D  2 42  ? 62.003  30.608  50.398  1.00 31.74 ?  69   CYS D CA  1 
ATOM   8763  C  C   . CYS D  2 42  ? 62.206  29.248  51.067  1.00 32.27 ?  69   CYS D C   1 
ATOM   8764  O  O   . CYS D  2 42  ? 61.482  28.297  50.767  1.00 32.08 ?  69   CYS D O   1 
ATOM   8765  C  CB  . CYS D  2 42  ? 62.922  30.765  49.185  1.00 31.72 ?  69   CYS D CB  1 
ATOM   8766  S  SG  . CYS D  2 42  ? 62.263  31.904  47.938  1.00 31.59 ?  69   CYS D SG  1 
ATOM   8767  N  N   . GLY D  2 43  ? 63.176  29.165  51.975  1.00 32.76 ?  70   GLY D N   1 
ATOM   8768  C  CA  . GLY D  2 43  ? 63.440  27.933  52.715  1.00 33.57 ?  70   GLY D CA  1 
ATOM   8769  C  C   . GLY D  2 43  ? 62.238  27.444  53.502  1.00 34.12 ?  70   GLY D C   1 
ATOM   8770  O  O   . GLY D  2 43  ? 61.975  26.242  53.550  1.00 34.28 ?  70   GLY D O   1 
ATOM   8771  N  N   . ASP D  2 44  ? 61.505  28.380  54.104  1.00 34.83 ?  71   ASP D N   1 
ATOM   8772  C  CA  . ASP D  2 44  ? 60.324  28.066  54.920  1.00 35.61 ?  71   ASP D CA  1 
ATOM   8773  C  C   . ASP D  2 44  ? 59.159  27.474  54.112  1.00 36.08 ?  71   ASP D C   1 
ATOM   8774  O  O   . ASP D  2 44  ? 58.543  26.494  54.536  1.00 36.18 ?  71   ASP D O   1 
ATOM   8775  C  CB  . ASP D  2 44  ? 59.852  29.307  55.692  1.00 35.48 ?  71   ASP D CB  1 
ATOM   8776  C  CG  . ASP D  2 44  ? 60.851  29.768  56.752  1.00 35.90 ?  71   ASP D CG  1 
ATOM   8777  O  OD1 . ASP D  2 44  ? 60.802  30.958  57.131  1.00 36.02 ?  71   ASP D OD1 1 
ATOM   8778  O  OD2 . ASP D  2 44  ? 61.681  28.954  57.213  1.00 36.09 ?  71   ASP D OD2 1 
ATOM   8779  N  N   . ILE D  2 45  ? 58.856  28.066  52.959  1.00 36.77 ?  72   ILE D N   1 
ATOM   8780  C  CA  . ILE D  2 45  ? 57.764  27.571  52.114  1.00 37.54 ?  72   ILE D CA  1 
ATOM   8781  C  C   . ILE D  2 45  ? 58.106  26.228  51.451  1.00 38.18 ?  72   ILE D C   1 
ATOM   8782  O  O   . ILE D  2 45  ? 57.250  25.345  51.354  1.00 37.94 ?  72   ILE D O   1 
ATOM   8783  C  CB  . ILE D  2 45  ? 57.263  28.630  51.073  1.00 37.41 ?  72   ILE D CB  1 
ATOM   8784  C  CG1 . ILE D  2 45  ? 56.132  28.062  50.209  1.00 37.27 ?  72   ILE D CG1 1 
ATOM   8785  C  CG2 . ILE D  2 45  ? 58.395  29.145  50.190  1.00 37.29 ?  72   ILE D CG2 1 
ATOM   8786  C  CD1 . ILE D  2 45  ? 54.858  27.753  50.971  1.00 37.37 ?  72   ILE D CD1 1 
ATOM   8787  N  N   . VAL D  2 46  ? 59.357  26.081  51.020  1.00 39.11 ?  73   VAL D N   1 
ATOM   8788  C  CA  . VAL D  2 46  ? 59.843  24.822  50.452  1.00 40.41 ?  73   VAL D CA  1 
ATOM   8789  C  C   . VAL D  2 46  ? 59.707  23.679  51.470  1.00 41.34 ?  73   VAL D C   1 
ATOM   8790  O  O   . VAL D  2 46  ? 59.287  22.574  51.115  1.00 41.45 ?  73   VAL D O   1 
ATOM   8791  C  CB  . VAL D  2 46  ? 61.304  24.949  49.923  1.00 40.26 ?  73   VAL D CB  1 
ATOM   8792  C  CG1 . VAL D  2 46  ? 61.877  23.591  49.540  1.00 40.61 ?  73   VAL D CG1 1 
ATOM   8793  C  CG2 . VAL D  2 46  ? 61.359  25.887  48.724  1.00 40.27 ?  73   VAL D CG2 1 
ATOM   8794  N  N   . ALA D  2 47  ? 60.040  23.962  52.730  1.00 42.48 ?  74   ALA D N   1 
ATOM   8795  C  CA  . ALA D  2 47  ? 59.914  22.985  53.815  1.00 43.75 ?  74   ALA D CA  1 
ATOM   8796  C  C   . ALA D  2 47  ? 58.455  22.626  54.102  1.00 44.55 ?  74   ALA D C   1 
ATOM   8797  O  O   . ALA D  2 47  ? 58.138  21.465  54.372  1.00 44.55 ?  74   ALA D O   1 
ATOM   8798  C  CB  . ALA D  2 47  ? 60.600  23.496  55.082  1.00 43.60 ?  74   ALA D CB  1 
ATOM   8799  N  N   . LEU D  2 48  ? 57.583  23.632  54.044  1.00 45.73 ?  75   LEU D N   1 
ATOM   8800  C  CA  . LEU D  2 48  ? 56.144  23.453  54.245  1.00 46.98 ?  75   LEU D CA  1 
ATOM   8801  C  C   . LEU D  2 48  ? 55.553  22.538  53.171  1.00 47.74 ?  75   LEU D C   1 
ATOM   8802  O  O   . LEU D  2 48  ? 54.747  21.656  53.474  1.00 47.94 ?  75   LEU D O   1 
ATOM   8803  C  CB  . LEU D  2 48  ? 55.436  24.819  54.256  1.00 46.99 ?  75   LEU D CB  1 
ATOM   8804  C  CG  . LEU D  2 48  ? 53.997  25.036  54.764  1.00 47.32 ?  75   LEU D CG  1 
ATOM   8805  C  CD1 . LEU D  2 48  ? 52.937  24.553  53.767  1.00 47.92 ?  75   LEU D CD1 1 
ATOM   8806  C  CD2 . LEU D  2 48  ? 53.761  24.436  56.154  1.00 47.77 ?  75   LEU D CD2 1 
ATOM   8807  N  N   . VAL D  2 49  ? 55.970  22.751  51.923  1.00 48.79 ?  76   VAL D N   1 
ATOM   8808  C  CA  . VAL D  2 49  ? 55.508  21.956  50.784  1.00 49.87 ?  76   VAL D CA  1 
ATOM   8809  C  C   . VAL D  2 49  ? 56.077  20.531  50.811  1.00 50.86 ?  76   VAL D C   1 
ATOM   8810  O  O   . VAL D  2 49  ? 55.346  19.568  50.574  1.00 50.90 ?  76   VAL D O   1 
ATOM   8811  C  CB  . VAL D  2 49  ? 55.811  22.664  49.431  1.00 49.75 ?  76   VAL D CB  1 
ATOM   8812  C  CG1 . VAL D  2 49  ? 55.570  21.736  48.248  1.00 49.56 ?  76   VAL D CG1 1 
ATOM   8813  C  CG2 . VAL D  2 49  ? 54.963  23.916  49.291  1.00 49.64 ?  76   VAL D CG2 1 
ATOM   8814  N  N   . GLN D  2 50  ? 57.373  20.407  51.109  1.00 52.14 ?  77   GLN D N   1 
ATOM   8815  C  CA  . GLN D  2 50  ? 58.031  19.100  51.246  1.00 53.43 ?  77   GLN D CA  1 
ATOM   8816  C  C   . GLN D  2 50  ? 57.335  18.182  52.251  1.00 54.16 ?  77   GLN D C   1 
ATOM   8817  O  O   . GLN D  2 50  ? 57.196  16.982  52.009  1.00 54.20 ?  77   GLN D O   1 
ATOM   8818  C  CB  . GLN D  2 50  ? 59.510  19.263  51.617  1.00 53.47 ?  77   GLN D CB  1 
ATOM   8819  C  CG  . GLN D  2 50  ? 60.494  18.767  50.552  1.00 54.16 ?  77   GLN D CG  1 
ATOM   8820  C  CD  . GLN D  2 50  ? 60.715  19.748  49.407  1.00 54.84 ?  77   GLN D CD  1 
ATOM   8821  O  OE1 . GLN D  2 50  ? 59.799  20.458  48.984  1.00 55.20 ?  77   GLN D OE1 1 
ATOM   8822  N  NE2 . GLN D  2 50  ? 61.940  19.777  48.890  1.00 55.02 ?  77   GLN D NE2 1 
ATOM   8823  N  N   . LYS D  2 51  ? 56.900  18.760  53.370  1.00 55.16 ?  78   LYS D N   1 
ATOM   8824  C  CA  . LYS D  2 51  ? 56.150  18.037  54.394  1.00 56.20 ?  78   LYS D CA  1 
ATOM   8825  C  C   . LYS D  2 51  ? 54.823  17.506  53.839  1.00 56.92 ?  78   LYS D C   1 
ATOM   8826  O  O   . LYS D  2 51  ? 54.422  16.381  54.149  1.00 57.06 ?  78   LYS D O   1 
ATOM   8827  C  CB  . LYS D  2 51  ? 55.908  18.941  55.606  1.00 56.21 ?  78   LYS D CB  1 
ATOM   8828  C  CG  . LYS D  2 51  ? 55.455  18.215  56.864  1.00 56.64 ?  78   LYS D CG  1 
ATOM   8829  C  CD  . LYS D  2 51  ? 55.340  19.180  58.036  1.00 57.30 ?  78   LYS D CD  1 
ATOM   8830  C  CE  . LYS D  2 51  ? 54.865  18.473  59.297  1.00 57.55 ?  78   LYS D CE  1 
ATOM   8831  N  NZ  . LYS D  2 51  ? 54.867  19.383  60.476  1.00 57.60 ?  78   LYS D NZ  1 
ATOM   8832  N  N   . ALA D  2 52  ? 54.161  18.318  53.013  1.00 57.79 ?  79   ALA D N   1 
ATOM   8833  C  CA  . ALA D  2 52  ? 52.901  17.942  52.369  1.00 58.65 ?  79   ALA D CA  1 
ATOM   8834  C  C   . ALA D  2 52  ? 53.092  16.873  51.290  1.00 59.29 ?  79   ALA D C   1 
ATOM   8835  O  O   . ALA D  2 52  ? 52.250  15.987  51.133  1.00 59.38 ?  79   ALA D O   1 
ATOM   8836  C  CB  . ALA D  2 52  ? 52.215  19.169  51.785  1.00 58.61 ?  79   ALA D CB  1 
ATOM   8837  N  N   . ARG D  2 53  ? 54.197  16.963  50.551  1.00 60.10 ?  80   ARG D N   1 
ATOM   8838  C  CA  . ARG D  2 53  ? 54.535  15.971  49.529  1.00 60.93 ?  80   ARG D CA  1 
ATOM   8839  C  C   . ARG D  2 53  ? 54.881  14.621  50.164  1.00 61.49 ?  80   ARG D C   1 
ATOM   8840  O  O   . ARG D  2 53  ? 54.739  13.572  49.530  1.00 61.57 ?  80   ARG D O   1 
ATOM   8841  C  CB  . ARG D  2 53  ? 55.694  16.464  48.651  1.00 60.95 ?  80   ARG D CB  1 
ATOM   8842  C  CG  . ARG D  2 53  ? 55.379  17.695  47.796  1.00 61.19 ?  80   ARG D CG  1 
ATOM   8843  C  CD  . ARG D  2 53  ? 54.670  17.335  46.490  1.00 61.62 ?  80   ARG D CD  1 
ATOM   8844  N  NE  . ARG D  2 53  ? 54.445  18.509  45.646  1.00 61.58 ?  80   ARG D NE  1 
ATOM   8845  C  CZ  . ARG D  2 53  ? 53.270  19.115  45.480  1.00 61.67 ?  80   ARG D CZ  1 
ATOM   8846  N  NH1 . ARG D  2 53  ? 52.179  18.664  46.091  1.00 61.53 ?  80   ARG D NH1 1 
ATOM   8847  N  NH2 . ARG D  2 53  ? 53.183  20.178  44.691  1.00 61.40 ?  80   ARG D NH2 1 
ATOM   8848  N  N   . GLU D  2 54  ? 55.329  14.668  51.419  1.00 62.21 ?  81   GLU D N   1 
ATOM   8849  C  CA  . GLU D  2 54  ? 55.660  13.478  52.203  1.00 62.90 ?  81   GLU D CA  1 
ATOM   8850  C  C   . GLU D  2 54  ? 54.441  12.963  52.978  1.00 63.29 ?  81   GLU D C   1 
ATOM   8851  O  O   . GLU D  2 54  ? 54.393  11.790  53.364  1.00 63.39 ?  81   GLU D O   1 
ATOM   8852  C  CB  . GLU D  2 54  ? 56.806  13.790  53.169  1.00 62.97 ?  81   GLU D CB  1 
ATOM   8853  C  CG  . GLU D  2 54  ? 57.627  12.579  53.599  1.00 63.54 ?  81   GLU D CG  1 
ATOM   8854  C  CD  . GLU D  2 54  ? 58.607  12.888  54.726  1.00 64.09 ?  81   GLU D CD  1 
ATOM   8855  O  OE1 . GLU D  2 54  ? 58.814  14.080  55.047  1.00 64.30 ?  81   GLU D OE1 1 
ATOM   8856  O  OE2 . GLU D  2 54  ? 59.172  11.929  55.294  1.00 64.23 ?  81   GLU D OE2 1 
ATOM   8857  N  N   . GLN D  2 55  ? 53.467  13.846  53.203  1.00 63.71 ?  82   GLN D N   1 
ATOM   8858  C  CA  . GLN D  2 55  ? 52.199  13.488  53.850  1.00 64.11 ?  82   GLN D CA  1 
ATOM   8859  C  C   . GLN D  2 55  ? 51.345  12.566  52.979  1.00 64.26 ?  82   GLN D C   1 
ATOM   8860  O  O   . GLN D  2 55  ? 50.573  11.754  53.495  1.00 64.33 ?  82   GLN D O   1 
ATOM   8861  C  CB  . GLN D  2 55  ? 51.400  14.748  54.200  1.00 64.16 ?  82   GLN D CB  1 
ATOM   8862  C  CG  . GLN D  2 55  ? 51.639  15.286  55.609  1.00 64.70 ?  82   GLN D CG  1 
ATOM   8863  C  CD  . GLN D  2 55  ? 50.640  14.752  56.626  1.00 65.35 ?  82   GLN D CD  1 
ATOM   8864  O  OE1 . GLN D  2 55  ? 49.425  14.802  56.411  1.00 65.27 ?  82   GLN D OE1 1 
ATOM   8865  N  NE2 . GLN D  2 55  ? 51.149  14.252  57.748  1.00 65.38 ?  82   GLN D NE2 1 
ATOM   8866  N  N   . SER D  2 56  ? 51.489  12.702  51.663  1.00 64.45 ?  83   SER D N   1 
ATOM   8867  C  CA  . SER D  2 56  ? 50.726  11.909  50.700  1.00 64.61 ?  83   SER D CA  1 
ATOM   8868  C  C   . SER D  2 56  ? 51.588  10.877  49.962  1.00 64.68 ?  83   SER D C   1 
ATOM   8869  O  O   . SER D  2 56  ? 51.118  10.215  49.032  1.00 64.68 ?  83   SER D O   1 
ATOM   8870  C  CB  . SER D  2 56  ? 50.010  12.827  49.703  1.00 64.65 ?  83   SER D CB  1 
ATOM   8871  O  OG  . SER D  2 56  ? 50.902  13.779  49.146  1.00 64.73 ?  83   SER D OG  1 
ATOM   8872  N  N   . GLY D  2 57  ? 52.844  10.744  50.386  1.00 64.74 ?  84   GLY D N   1 
ATOM   8873  C  CA  . GLY D  2 57  ? 53.772  9.779   49.799  1.00 64.79 ?  84   GLY D CA  1 
ATOM   8874  C  C   . GLY D  2 57  ? 54.323  10.230  48.460  1.00 64.82 ?  84   GLY D C   1 
ATOM   8875  O  O   . GLY D  2 57  ? 54.029  9.631   47.424  1.00 64.85 ?  84   GLY D O   1 
ATOM   8876  N  N   . ASP E  1 1   ? -7.315  44.307  -4.836  1.00 26.16 ?  25   ASP E N   1 
ATOM   8877  C  CA  . ASP E  1 1   ? -7.231  43.450  -3.620  1.00 26.65 ?  25   ASP E CA  1 
ATOM   8878  C  C   . ASP E  1 1   ? -5.777  43.127  -3.281  1.00 26.53 ?  25   ASP E C   1 
ATOM   8879  O  O   . ASP E  1 1   ? -5.048  42.577  -4.106  1.00 26.62 ?  25   ASP E O   1 
ATOM   8880  C  CB  . ASP E  1 1   ? -8.035  42.152  -3.816  1.00 26.70 ?  25   ASP E CB  1 
ATOM   8881  C  CG  . ASP E  1 1   ? -8.232  41.365  -2.516  1.00 27.12 ?  25   ASP E CG  1 
ATOM   8882  O  OD1 . ASP E  1 1   ? -7.482  41.583  -1.541  1.00 27.33 ?  25   ASP E OD1 1 
ATOM   8883  O  OD2 . ASP E  1 1   ? -9.146  40.511  -2.470  1.00 27.70 -1 25   ASP E OD2 1 
ATOM   8884  N  N   . ILE E  1 2   ? -5.365  43.492  -2.069  1.00 26.38 ?  26   ILE E N   1 
ATOM   8885  C  CA  . ILE E  1 2   ? -4.076  43.066  -1.528  1.00 26.22 ?  26   ILE E CA  1 
ATOM   8886  C  C   . ILE E  1 2   ? -4.336  41.777  -0.761  1.00 26.31 ?  26   ILE E C   1 
ATOM   8887  O  O   . ILE E  1 2   ? -4.818  41.814  0.374   1.00 26.19 ?  26   ILE E O   1 
ATOM   8888  C  CB  . ILE E  1 2   ? -3.436  44.132  -0.590  1.00 26.06 ?  26   ILE E CB  1 
ATOM   8889  C  CG1 . ILE E  1 2   ? -3.464  45.524  -1.236  1.00 25.61 ?  26   ILE E CG1 1 
ATOM   8890  C  CG2 . ILE E  1 2   ? -2.002  43.733  -0.228  1.00 25.39 ?  26   ILE E CG2 1 
ATOM   8891  C  CD1 . ILE E  1 2   ? -3.222  46.678  -0.260  1.00 24.89 ?  26   ILE E CD1 1 
ATOM   8892  N  N   . SER E  1 3   ? -4.023  40.645  -1.393  1.00 26.51 ?  27   SER E N   1 
ATOM   8893  C  CA  . SER E  1 3   ? -4.414  39.319  -0.892  1.00 26.69 ?  27   SER E CA  1 
ATOM   8894  C  C   . SER E  1 3   ? -3.684  38.878  0.380   1.00 27.00 ?  27   SER E C   1 
ATOM   8895  O  O   . SER E  1 3   ? -4.099  37.919  1.039   1.00 26.98 ?  27   SER E O   1 
ATOM   8896  C  CB  . SER E  1 3   ? -4.245  38.259  -1.984  1.00 26.66 ?  27   SER E CB  1 
ATOM   8897  O  OG  . SER E  1 3   ? -2.882  38.107  -2.346  1.00 26.16 ?  27   SER E OG  1 
ATOM   8898  N  N   . THR E  1 4   ? -2.605  39.581  0.715   1.00 27.21 ?  28   THR E N   1 
ATOM   8899  C  CA  . THR E  1 4   ? -1.821  39.300  1.919   1.00 27.56 ?  28   THR E CA  1 
ATOM   8900  C  C   . THR E  1 4   ? -2.341  40.042  3.157   1.00 27.94 ?  28   THR E C   1 
ATOM   8901  O  O   . THR E  1 4   ? -1.877  39.803  4.278   1.00 28.06 ?  28   THR E O   1 
ATOM   8902  C  CB  . THR E  1 4   ? -0.331  39.631  1.705   1.00 27.50 ?  28   THR E CB  1 
ATOM   8903  O  OG1 . THR E  1 4   ? -0.202  40.965  1.192   1.00 27.13 ?  28   THR E OG1 1 
ATOM   8904  C  CG2 . THR E  1 4   ? 0.303   38.646  0.724   1.00 27.31 ?  28   THR E CG2 1 
ATOM   8905  N  N   . VAL E  1 5   ? -3.303  40.938  2.945   1.00 28.07 ?  29   VAL E N   1 
ATOM   8906  C  CA  . VAL E  1 5   ? -3.972  41.651  4.031   1.00 28.20 ?  29   VAL E CA  1 
ATOM   8907  C  C   . VAL E  1 5   ? -5.220  40.875  4.480   1.00 28.45 ?  29   VAL E C   1 
ATOM   8908  O  O   . VAL E  1 5   ? -6.056  40.519  3.650   1.00 28.37 ?  29   VAL E O   1 
ATOM   8909  C  CB  . VAL E  1 5   ? -4.345  43.096  3.602   1.00 28.32 ?  29   VAL E CB  1 
ATOM   8910  C  CG1 . VAL E  1 5   ? -5.184  43.791  4.661   1.00 27.91 ?  29   VAL E CG1 1 
ATOM   8911  C  CG2 . VAL E  1 5   ? -3.086  43.906  3.316   1.00 28.23 ?  29   VAL E CG2 1 
ATOM   8912  N  N   . PRO E  1 6   ? -5.338  40.605  5.798   1.00 28.77 ?  30   PRO E N   1 
ATOM   8913  C  CA  . PRO E  1 6   ? -6.474  39.902  6.408   1.00 29.01 ?  30   PRO E CA  1 
ATOM   8914  C  C   . PRO E  1 6   ? -7.822  40.591  6.187   1.00 29.25 ?  30   PRO E C   1 
ATOM   8915  O  O   . PRO E  1 6   ? -7.879  41.821  6.059   1.00 29.17 ?  30   PRO E O   1 
ATOM   8916  C  CB  . PRO E  1 6   ? -6.132  39.930  7.903   1.00 29.04 ?  30   PRO E CB  1 
ATOM   8917  C  CG  . PRO E  1 6   ? -4.654  40.035  7.946   1.00 29.04 ?  30   PRO E CG  1 
ATOM   8918  C  CD  . PRO E  1 6   ? -4.298  40.917  6.798   1.00 28.75 ?  30   PRO E CD  1 
ATOM   8919  N  N   . ASP E  1 7   ? -8.889  39.791  6.159   1.00 29.61 ?  31   ASP E N   1 
ATOM   8920  C  CA  . ASP E  1 7   ? -10.268 40.296  6.066   1.00 30.02 ?  31   ASP E CA  1 
ATOM   8921  C  C   . ASP E  1 7   ? -10.581 41.293  7.176   1.00 30.19 ?  31   ASP E C   1 
ATOM   8922  O  O   . ASP E  1 7   ? -11.233 42.312  6.932   1.00 30.18 ?  31   ASP E O   1 
ATOM   8923  C  CB  . ASP E  1 7   ? -11.284 39.146  6.127   1.00 30.01 ?  31   ASP E CB  1 
ATOM   8924  C  CG  . ASP E  1 7   ? -11.310 38.303  4.860   1.00 30.38 ?  31   ASP E CG  1 
ATOM   8925  O  OD1 . ASP E  1 7   ? -11.099 38.848  3.758   1.00 30.05 ?  31   ASP E OD1 1 
ATOM   8926  O  OD2 . ASP E  1 7   ? -11.565 37.083  4.969   1.00 31.28 -1 31   ASP E OD2 1 
ATOM   8927  N  N   . GLU E  1 8   ? -10.100 40.993  8.386   1.00 30.36 ?  32   GLU E N   1 
ATOM   8928  C  CA  . GLU E  1 8   ? -10.334 41.822  9.577   1.00 30.75 ?  32   GLU E CA  1 
ATOM   8929  C  C   . GLU E  1 8   ? -9.936  43.275  9.367   1.00 30.57 ?  32   GLU E C   1 
ATOM   8930  O  O   . GLU E  1 8   ? -10.573 44.176  9.904   1.00 30.68 ?  32   GLU E O   1 
ATOM   8931  C  CB  . GLU E  1 8   ? -9.587  41.274  10.800  1.00 30.93 ?  32   GLU E CB  1 
ATOM   8932  C  CG  . GLU E  1 8   ? -9.844  39.811  11.123  1.00 32.30 ?  32   GLU E CG  1 
ATOM   8933  C  CD  . GLU E  1 8   ? -8.823  38.892  10.479  1.00 34.39 ?  32   GLU E CD  1 
ATOM   8934  O  OE1 . GLU E  1 8   ? -8.886  38.694  9.245   1.00 34.39 ?  32   GLU E OE1 1 
ATOM   8935  O  OE2 . GLU E  1 8   ? -7.951  38.372  11.210  1.00 36.15 -1 32   GLU E OE2 1 
ATOM   8936  N  N   . THR E  1 9   ? -8.880  43.492  8.587   1.00 30.49 ?  33   THR E N   1 
ATOM   8937  C  CA  . THR E  1 9   ? -8.401  44.835  8.283   1.00 30.34 ?  33   THR E CA  1 
ATOM   8938  C  C   . THR E  1 9   ? -9.370  45.588  7.368   1.00 30.46 ?  33   THR E C   1 
ATOM   8939  O  O   . THR E  1 9   ? -9.769  46.708  7.684   1.00 30.53 ?  33   THR E O   1 
ATOM   8940  C  CB  . THR E  1 9   ? -6.975  44.799  7.697   1.00 30.21 ?  33   THR E CB  1 
ATOM   8941  O  OG1 . THR E  1 9   ? -6.092  44.239  8.672   1.00 29.89 ?  33   THR E OG1 1 
ATOM   8942  C  CG2 . THR E  1 9   ? -6.484  46.197  7.333   1.00 29.94 ?  33   THR E CG2 1 
ATOM   8943  N  N   . TYR E  1 10  ? -9.747  44.969  6.250   1.00 30.61 ?  34   TYR E N   1 
ATOM   8944  C  CA  . TYR E  1 10  ? -10.731 45.553  5.334   1.00 30.79 ?  34   TYR E CA  1 
ATOM   8945  C  C   . TYR E  1 10  ? -12.062 45.810  6.034   1.00 31.05 ?  34   TYR E C   1 
ATOM   8946  O  O   . TYR E  1 10  ? -12.683 46.852  5.825   1.00 31.17 ?  34   TYR E O   1 
ATOM   8947  C  CB  . TYR E  1 10  ? -10.942 44.663  4.106   1.00 30.52 ?  34   TYR E CB  1 
ATOM   8948  C  CG  . TYR E  1 10  ? -9.838  44.759  3.077   1.00 29.70 ?  34   TYR E CG  1 
ATOM   8949  C  CD1 . TYR E  1 10  ? -9.790  45.822  2.171   1.00 28.93 ?  34   TYR E CD1 1 
ATOM   8950  C  CD2 . TYR E  1 10  ? -8.844  43.787  3.004   1.00 28.91 ?  34   TYR E CD2 1 
ATOM   8951  C  CE1 . TYR E  1 10  ? -8.777  45.913  1.221   1.00 27.91 ?  34   TYR E CE1 1 
ATOM   8952  C  CE2 . TYR E  1 10  ? -7.827  43.870  2.056   1.00 28.29 ?  34   TYR E CE2 1 
ATOM   8953  C  CZ  . TYR E  1 10  ? -7.801  44.932  1.170   1.00 27.90 ?  34   TYR E CZ  1 
ATOM   8954  O  OH  . TYR E  1 10  ? -6.794  45.010  0.237   1.00 27.65 ?  34   TYR E OH  1 
ATOM   8955  N  N   . ASP E  1 11  ? -12.478 44.858  6.867   1.00 31.61 ?  35   ASP E N   1 
ATOM   8956  C  CA  . ASP E  1 11  ? -13.699 44.972  7.667   1.00 32.25 ?  35   ASP E CA  1 
ATOM   8957  C  C   . ASP E  1 11  ? -13.647 46.138  8.655   1.00 32.61 ?  35   ASP E C   1 
ATOM   8958  O  O   . ASP E  1 11  ? -14.599 46.921  8.743   1.00 32.89 ?  35   ASP E O   1 
ATOM   8959  C  CB  . ASP E  1 11  ? -13.981 43.658  8.408   1.00 32.23 ?  35   ASP E CB  1 
ATOM   8960  C  CG  . ASP E  1 11  ? -14.355 42.519  7.464   1.00 32.71 ?  35   ASP E CG  1 
ATOM   8961  O  OD1 . ASP E  1 11  ? -14.688 42.790  6.290   1.00 33.09 ?  35   ASP E OD1 1 
ATOM   8962  O  OD2 . ASP E  1 11  ? -14.317 41.347  7.899   1.00 33.45 -1 35   ASP E OD2 1 
ATOM   8963  N  N   . ALA E  1 12  ? -12.536 46.253  9.385   1.00 32.84 ?  36   ALA E N   1 
ATOM   8964  C  CA  . ALA E  1 12  ? -12.335 47.353  10.341  1.00 32.94 ?  36   ALA E CA  1 
ATOM   8965  C  C   . ALA E  1 12  ? -12.250 48.703  9.635   1.00 33.09 ?  36   ALA E C   1 
ATOM   8966  O  O   . ALA E  1 12  ? -12.544 49.743  10.230  1.00 33.05 ?  36   ALA E O   1 
ATOM   8967  C  CB  . ALA E  1 12  ? -11.087 47.114  11.185  1.00 32.81 ?  36   ALA E CB  1 
ATOM   8968  N  N   . LEU E  1 13  ? -11.850 48.673  8.365   1.00 33.35 ?  37   LEU E N   1 
ATOM   8969  C  CA  . LEU E  1 13  ? -11.761 49.873  7.535   1.00 33.68 ?  37   LEU E CA  1 
ATOM   8970  C  C   . LEU E  1 13  ? -13.068 50.167  6.782   1.00 34.02 ?  37   LEU E C   1 
ATOM   8971  O  O   . LEU E  1 13  ? -13.172 51.178  6.079   1.00 33.89 ?  37   LEU E O   1 
ATOM   8972  C  CB  . LEU E  1 13  ? -10.597 49.738  6.545   1.00 33.72 ?  37   LEU E CB  1 
ATOM   8973  C  CG  . LEU E  1 13  ? -9.192  50.258  6.889   1.00 33.86 ?  37   LEU E CG  1 
ATOM   8974  C  CD1 . LEU E  1 13  ? -8.675  49.757  8.224   1.00 34.47 ?  37   LEU E CD1 1 
ATOM   8975  C  CD2 . LEU E  1 13  ? -8.222  49.887  5.781   1.00 33.64 ?  37   LEU E CD2 1 
ATOM   8976  N  N   . LYS E  1 14  ? -14.055 49.283  6.943   1.00 34.46 ?  38   LYS E N   1 
ATOM   8977  C  CA  . LYS E  1 14  ? -15.345 49.366  6.239   1.00 35.03 ?  38   LYS E CA  1 
ATOM   8978  C  C   . LYS E  1 14  ? -15.145 49.416  4.722   1.00 34.90 ?  38   LYS E C   1 
ATOM   8979  O  O   . LYS E  1 14  ? -15.704 50.273  4.034   1.00 35.04 ?  38   LYS E O   1 
ATOM   8980  C  CB  . LYS E  1 14  ? -16.185 50.563  6.722   1.00 35.10 ?  38   LYS E CB  1 
ATOM   8981  C  CG  . LYS E  1 14  ? -16.432 50.626  8.230   1.00 36.43 ?  38   LYS E CG  1 
ATOM   8982  C  CD  . LYS E  1 14  ? -17.463 49.602  8.698   1.00 37.80 ?  38   LYS E CD  1 
ATOM   8983  C  CE  . LYS E  1 14  ? -17.893 49.872  10.137  1.00 38.94 ?  38   LYS E CE  1 
ATOM   8984  N  NZ  . LYS E  1 14  ? -16.783 49.703  11.120  1.00 39.42 ?  38   LYS E NZ  1 
ATOM   8985  N  N   . LEU E  1 15  ? -14.331 48.494  4.216   1.00 34.92 ?  39   LEU E N   1 
ATOM   8986  C  CA  . LEU E  1 15  ? -14.012 48.440  2.796   1.00 34.73 ?  39   LEU E CA  1 
ATOM   8987  C  C   . LEU E  1 15  ? -14.311 47.071  2.202   1.00 34.62 ?  39   LEU E C   1 
ATOM   8988  O  O   . LEU E  1 15  ? -14.224 46.051  2.886   1.00 34.49 ?  39   LEU E O   1 
ATOM   8989  C  CB  . LEU E  1 15  ? -12.540 48.788  2.555   1.00 34.78 ?  39   LEU E CB  1 
ATOM   8990  C  CG  . LEU E  1 15  ? -12.032 50.221  2.730   1.00 35.09 ?  39   LEU E CG  1 
ATOM   8991  C  CD1 . LEU E  1 15  ? -10.519 50.233  2.576   1.00 35.50 ?  39   LEU E CD1 1 
ATOM   8992  C  CD2 . LEU E  1 15  ? -12.676 51.190  1.743   1.00 34.82 ?  39   LEU E CD2 1 
ATOM   8993  N  N   . ASP E  1 16  ? -14.663 47.069  0.920   1.00 34.50 ?  40   ASP E N   1 
ATOM   8994  C  CA  . ASP E  1 16  ? -14.835 45.845  0.153   1.00 34.47 ?  40   ASP E CA  1 
ATOM   8995  C  C   . ASP E  1 16  ? -13.523 45.495  -0.553  1.00 34.21 ?  40   ASP E C   1 
ATOM   8996  O  O   . ASP E  1 16  ? -12.996 46.304  -1.315  1.00 34.07 ?  40   ASP E O   1 
ATOM   8997  C  CB  . ASP E  1 16  ? -15.966 46.018  -0.866  1.00 34.52 ?  40   ASP E CB  1 
ATOM   8998  C  CG  . ASP E  1 16  ? -16.199 44.774  -1.695  1.00 34.96 ?  40   ASP E CG  1 
ATOM   8999  O  OD1 . ASP E  1 16  ? -17.267 44.160  -1.531  1.00 35.81 ?  40   ASP E OD1 1 
ATOM   9000  O  OD2 . ASP E  1 16  ? -15.316 44.399  -2.500  1.00 35.79 -1 40   ASP E OD2 1 
ATOM   9001  N  N   . ARG E  1 17  ? -13.024 44.283  -0.300  1.00 34.11 ?  41   ARG E N   1 
ATOM   9002  C  CA  . ARG E  1 17  ? -11.753 43.786  -0.858  1.00 34.07 ?  41   ARG E CA  1 
ATOM   9003  C  C   . ARG E  1 17  ? -11.619 43.973  -2.364  1.00 33.97 ?  41   ARG E C   1 
ATOM   9004  O  O   . ARG E  1 17  ? -10.599 44.465  -2.846  1.00 33.99 ?  41   ARG E O   1 
ATOM   9005  C  CB  . ARG E  1 17  ? -11.584 42.290  -0.577  1.00 34.09 ?  41   ARG E CB  1 
ATOM   9006  C  CG  . ARG E  1 17  ? -11.404 41.899  0.865   1.00 33.98 ?  41   ARG E CG  1 
ATOM   9007  C  CD  . ARG E  1 17  ? -10.816 40.509  0.940   1.00 33.23 ?  41   ARG E CD  1 
ATOM   9008  N  NE  . ARG E  1 17  ? -9.401  40.543  0.587   1.00 33.19 ?  41   ARG E NE  1 
ATOM   9009  C  CZ  . ARG E  1 17  ? -8.409  40.454  1.462   1.00 33.07 ?  41   ARG E CZ  1 
ATOM   9010  N  NH1 . ARG E  1 17  ? -8.667  40.293  2.755   1.00 33.16 ?  41   ARG E NH1 1 
ATOM   9011  N  NH2 . ARG E  1 17  ? -7.155  40.513  1.038   1.00 33.86 ?  41   ARG E NH2 1 
ATOM   9012  N  N   . GLY E  1 18  ? -12.647 43.553  -3.099  1.00 33.92 ?  42   GLY E N   1 
ATOM   9013  C  CA  . GLY E  1 18  ? -12.621 43.567  -4.560  1.00 33.71 ?  42   GLY E CA  1 
ATOM   9014  C  C   . GLY E  1 18  ? -12.797 44.939  -5.175  1.00 33.60 ?  42   GLY E C   1 
ATOM   9015  O  O   . GLY E  1 18  ? -12.196 45.241  -6.208  1.00 33.85 ?  42   GLY E O   1 
ATOM   9016  N  N   . LYS E  1 19  ? -13.620 45.771  -4.542  1.00 33.44 ?  43   LYS E N   1 
ATOM   9017  C  CA  . LYS E  1 19  ? -13.953 47.089  -5.081  1.00 33.15 ?  43   LYS E CA  1 
ATOM   9018  C  C   . LYS E  1 19  ? -12.939 48.175  -4.736  1.00 32.87 ?  43   LYS E C   1 
ATOM   9019  O  O   . LYS E  1 19  ? -12.630 49.028  -5.575  1.00 32.95 ?  43   LYS E O   1 
ATOM   9020  C  CB  . LYS E  1 19  ? -15.357 47.517  -4.637  1.00 33.35 ?  43   LYS E CB  1 
ATOM   9021  C  CG  . LYS E  1 19  ? -16.448 47.262  -5.669  1.00 33.76 ?  43   LYS E CG  1 
ATOM   9022  C  CD  . LYS E  1 19  ? -16.387 48.297  -6.784  1.00 34.38 ?  43   LYS E CD  1 
ATOM   9023  C  CE  . LYS E  1 19  ? -17.155 47.851  -8.009  1.00 34.53 ?  43   LYS E CE  1 
ATOM   9024  N  NZ  . LYS E  1 19  ? -16.871 48.749  -9.158  1.00 34.91 ?  43   LYS E NZ  1 
ATOM   9025  N  N   . ALA E  1 20  ? -12.430 48.148  -3.506  1.00 32.29 ?  44   ALA E N   1 
ATOM   9026  C  CA  . ALA E  1 20  ? -11.512 49.181  -3.028  1.00 31.82 ?  44   ALA E CA  1 
ATOM   9027  C  C   . ALA E  1 20  ? -10.330 49.393  -3.973  1.00 31.42 ?  44   ALA E C   1 
ATOM   9028  O  O   . ALA E  1 20  ? -9.687  48.437  -4.401  1.00 31.33 ?  44   ALA E O   1 
ATOM   9029  C  CB  . ALA E  1 20  ? -11.022 48.853  -1.622  1.00 31.77 ?  44   ALA E CB  1 
ATOM   9030  N  N   . THR E  1 21  ? -10.071 50.654  -4.307  1.00 30.99 ?  45   THR E N   1 
ATOM   9031  C  CA  . THR E  1 21  ? -8.895  51.026  -5.085  1.00 30.53 ?  45   THR E CA  1 
ATOM   9032  C  C   . THR E  1 21  ? -7.705  51.225  -4.143  1.00 30.48 ?  45   THR E C   1 
ATOM   9033  O  O   . THR E  1 21  ? -7.899  51.357  -2.929  1.00 30.48 ?  45   THR E O   1 
ATOM   9034  C  CB  . THR E  1 21  ? -9.125  52.331  -5.889  1.00 30.59 ?  45   THR E CB  1 
ATOM   9035  O  OG1 . THR E  1 21  ? -9.361  53.420  -4.987  1.00 29.54 ?  45   THR E OG1 1 
ATOM   9036  C  CG2 . THR E  1 21  ? -10.302 52.188  -6.855  1.00 30.09 ?  45   THR E CG2 1 
ATOM   9037  N  N   . PRO E  1 22  ? -6.471  51.225  -4.690  1.00 30.42 ?  46   PRO E N   1 
ATOM   9038  C  CA  . PRO E  1 22  ? -5.286  51.593  -3.901  1.00 30.39 ?  46   PRO E CA  1 
ATOM   9039  C  C   . PRO E  1 22  ? -5.437  52.933  -3.170  1.00 30.46 ?  46   PRO E C   1 
ATOM   9040  O  O   . PRO E  1 22  ? -5.094  53.032  -1.990  1.00 30.35 ?  46   PRO E O   1 
ATOM   9041  C  CB  . PRO E  1 22  ? -4.185  51.679  -4.962  1.00 30.22 ?  46   PRO E CB  1 
ATOM   9042  C  CG  . PRO E  1 22  ? -4.575  50.641  -5.960  1.00 30.30 ?  46   PRO E CG  1 
ATOM   9043  C  CD  . PRO E  1 22  ? -6.091  50.640  -5.993  1.00 30.32 ?  46   PRO E CD  1 
ATOM   9044  N  N   . LYS E  1 23  ? -5.952  53.942  -3.870  1.00 30.59 ?  47   LYS E N   1 
ATOM   9045  C  CA  . LYS E  1 23  ? -6.211  55.260  -3.290  1.00 30.74 ?  47   LYS E CA  1 
ATOM   9046  C  C   . LYS E  1 23  ? -7.131  55.152  -2.075  1.00 30.67 ?  47   LYS E C   1 
ATOM   9047  O  O   . LYS E  1 23  ? -6.846  55.722  -1.022  1.00 30.75 ?  47   LYS E O   1 
ATOM   9048  C  CB  . LYS E  1 23  ? -6.825  56.190  -4.343  1.00 30.82 ?  47   LYS E CB  1 
ATOM   9049  C  CG  . LYS E  1 23  ? -7.021  57.638  -3.905  1.00 31.39 ?  47   LYS E CG  1 
ATOM   9050  C  CD  . LYS E  1 23  ? -8.090  58.317  -4.757  1.00 32.99 ?  47   LYS E CD  1 
ATOM   9051  C  CE  . LYS E  1 23  ? -8.369  59.742  -4.301  1.00 33.87 ?  47   LYS E CE  1 
ATOM   9052  N  NZ  . LYS E  1 23  ? -7.380  60.705  -4.860  1.00 35.01 ?  47   LYS E NZ  1 
ATOM   9053  N  N   . GLU E  1 24  ? -8.224  54.408  -2.228  1.00 30.56 ?  48   GLU E N   1 
ATOM   9054  C  CA  . GLU E  1 24  ? -9.212  54.250  -1.162  1.00 30.58 ?  48   GLU E CA  1 
ATOM   9055  C  C   . GLU E  1 24  ? -8.657  53.492  0.039   1.00 30.32 ?  48   GLU E C   1 
ATOM   9056  O  O   . GLU E  1 24  ? -8.887  53.890  1.181   1.00 30.23 ?  48   GLU E O   1 
ATOM   9057  C  CB  . GLU E  1 24  ? -10.473 53.559  -1.684  1.00 30.66 ?  48   GLU E CB  1 
ATOM   9058  C  CG  . GLU E  1 24  ? -11.331 54.428  -2.596  1.00 31.16 ?  48   GLU E CG  1 
ATOM   9059  C  CD  . GLU E  1 24  ? -12.479 53.659  -3.219  1.00 32.13 ?  48   GLU E CD  1 
ATOM   9060  O  OE1 . GLU E  1 24  ? -12.276 52.490  -3.612  1.00 32.15 ?  48   GLU E OE1 1 
ATOM   9061  O  OE2 . GLU E  1 24  ? -13.587 54.228  -3.314  1.00 33.47 -1 48   GLU E OE2 1 
ATOM   9062  N  N   . THR E  1 25  ? -7.931  52.407  -0.227  1.00 30.18 ?  49   THR E N   1 
ATOM   9063  C  CA  . THR E  1 25  ? -7.340  51.587  0.833   1.00 30.07 ?  49   THR E CA  1 
ATOM   9064  C  C   . THR E  1 25  ? -6.282  52.379  1.608   1.00 30.10 ?  49   THR E C   1 
ATOM   9065  O  O   . THR E  1 25  ? -6.299  52.396  2.836   1.00 29.99 ?  49   THR E O   1 
ATOM   9066  C  CB  . THR E  1 25  ? -6.764  50.258  0.279   1.00 30.13 ?  49   THR E CB  1 
ATOM   9067  O  OG1 . THR E  1 25  ? -7.803  49.530  -0.388  1.00 29.76 ?  49   THR E OG1 1 
ATOM   9068  C  CG2 . THR E  1 25  ? -6.200  49.391  1.403   1.00 29.80 ?  49   THR E CG2 1 
ATOM   9069  N  N   . TYR E  1 26  ? -5.391  53.054  0.881   1.00 30.30 ?  50   TYR E N   1 
ATOM   9070  C  CA  . TYR E  1 26  ? -4.386  53.933  1.484   1.00 30.52 ?  50   TYR E CA  1 
ATOM   9071  C  C   . TYR E  1 26  ? -5.030  54.997  2.377   1.00 30.63 ?  50   TYR E C   1 
ATOM   9072  O  O   . TYR E  1 26  ? -4.635  55.159  3.533   1.00 30.54 ?  50   TYR E O   1 
ATOM   9073  C  CB  . TYR E  1 26  ? -3.515  54.587  0.400   1.00 30.51 ?  50   TYR E CB  1 
ATOM   9074  C  CG  . TYR E  1 26  ? -2.537  55.627  0.916   1.00 31.31 ?  50   TYR E CG  1 
ATOM   9075  C  CD1 . TYR E  1 26  ? -1.350  55.248  1.546   1.00 31.59 ?  50   TYR E CD1 1 
ATOM   9076  C  CD2 . TYR E  1 26  ? -2.801  56.992  0.773   1.00 31.85 ?  50   TYR E CD2 1 
ATOM   9077  C  CE1 . TYR E  1 26  ? -0.453  56.204  2.027   1.00 32.29 ?  50   TYR E CE1 1 
ATOM   9078  C  CE2 . TYR E  1 26  ? -1.914  57.955  1.250   1.00 32.33 ?  50   TYR E CE2 1 
ATOM   9079  C  CZ  . TYR E  1 26  ? -0.740  57.555  1.873   1.00 32.93 ?  50   TYR E CZ  1 
ATOM   9080  O  OH  . TYR E  1 26  ? 0.141   58.508  2.344   1.00 33.20 ?  50   TYR E OH  1 
ATOM   9081  N  N   . GLU E  1 27  ? -6.027  55.698  1.837   1.00 30.68 ?  51   GLU E N   1 
ATOM   9082  C  CA  . GLU E  1 27  ? -6.710  56.779  2.555   1.00 30.87 ?  51   GLU E CA  1 
ATOM   9083  C  C   . GLU E  1 27  ? -7.380  56.315  3.848   1.00 30.42 ?  51   GLU E C   1 
ATOM   9084  O  O   . GLU E  1 27  ? -7.321  57.013  4.863   1.00 30.54 ?  51   GLU E O   1 
ATOM   9085  C  CB  . GLU E  1 27  ? -7.730  57.475  1.646   1.00 31.04 ?  51   GLU E CB  1 
ATOM   9086  C  CG  . GLU E  1 27  ? -7.122  58.549  0.753   1.00 33.15 ?  51   GLU E CG  1 
ATOM   9087  C  CD  . GLU E  1 27  ? -8.094  59.098  -0.288  1.00 35.62 ?  51   GLU E CD  1 
ATOM   9088  O  OE1 . GLU E  1 27  ? -9.268  58.663  -0.324  1.00 36.48 ?  51   GLU E OE1 1 
ATOM   9089  O  OE2 . GLU E  1 27  ? -7.673  59.971  -1.079  1.00 36.82 -1 51   GLU E OE2 1 
ATOM   9090  N  N   . ALA E  1 28  ? -8.007  55.140  3.801   1.00 29.83 ?  52   ALA E N   1 
ATOM   9091  C  CA  . ALA E  1 28  ? -8.639  54.542  4.974   1.00 29.49 ?  52   ALA E CA  1 
ATOM   9092  C  C   . ALA E  1 28  ? -7.613  54.140  6.037   1.00 29.39 ?  52   ALA E C   1 
ATOM   9093  O  O   . ALA E  1 28  ? -7.827  54.369  7.229   1.00 29.18 ?  52   ALA E O   1 
ATOM   9094  C  CB  . ALA E  1 28  ? -9.487  53.345  4.570   1.00 29.29 ?  52   ALA E CB  1 
ATOM   9095  N  N   . LEU E  1 29  ? -6.504  53.544  5.599   1.00 29.26 ?  53   LEU E N   1 
ATOM   9096  C  CA  . LEU E  1 29  ? -5.426  53.156  6.509   1.00 29.18 ?  53   LEU E CA  1 
ATOM   9097  C  C   . LEU E  1 29  ? -4.808  54.373  7.198   1.00 29.29 ?  53   LEU E C   1 
ATOM   9098  O  O   . LEU E  1 29  ? -4.583  54.350  8.405   1.00 29.34 ?  53   LEU E O   1 
ATOM   9099  C  CB  . LEU E  1 29  ? -4.348  52.357  5.767   1.00 29.00 ?  53   LEU E CB  1 
ATOM   9100  C  CG  . LEU E  1 29  ? -4.676  50.920  5.349   1.00 28.38 ?  53   LEU E CG  1 
ATOM   9101  C  CD1 . LEU E  1 29  ? -3.753  50.498  4.237   1.00 27.89 ?  53   LEU E CD1 1 
ATOM   9102  C  CD2 . LEU E  1 29  ? -4.600  49.939  6.518   1.00 27.20 ?  53   LEU E CD2 1 
ATOM   9103  N  N   . VAL E  1 30  ? -4.560  55.429  6.422   1.00 29.55 ?  54   VAL E N   1 
ATOM   9104  C  CA  . VAL E  1 30  ? -3.971  56.675  6.922   1.00 30.01 ?  54   VAL E CA  1 
ATOM   9105  C  C   . VAL E  1 30  ? -4.901  57.412  7.895   1.00 30.21 ?  54   VAL E C   1 
ATOM   9106  O  O   . VAL E  1 30  ? -4.444  57.944  8.908   1.00 30.44 ?  54   VAL E O   1 
ATOM   9107  C  CB  . VAL E  1 30  ? -3.525  57.601  5.751   1.00 29.99 ?  54   VAL E CB  1 
ATOM   9108  C  CG1 . VAL E  1 30  ? -3.211  59.016  6.237   1.00 29.98 ?  54   VAL E CG1 1 
ATOM   9109  C  CG2 . VAL E  1 30  ? -2.313  57.010  5.044   1.00 30.05 ?  54   VAL E CG2 1 
ATOM   9110  N  N   . LYS E  1 31  ? -6.196  57.429  7.583   1.00 30.46 ?  55   LYS E N   1 
ATOM   9111  C  CA  . LYS E  1 31  ? -7.221  58.018  8.454   1.00 30.52 ?  55   LYS E CA  1 
ATOM   9112  C  C   . LYS E  1 31  ? -7.183  57.420  9.864   1.00 30.20 ?  55   LYS E C   1 
ATOM   9113  O  O   . LYS E  1 31  ? -7.243  58.156  10.854  1.00 30.27 ?  55   LYS E O   1 
ATOM   9114  C  CB  . LYS E  1 31  ? -8.617  57.840  7.836   1.00 30.67 ?  55   LYS E CB  1 
ATOM   9115  C  CG  . LYS E  1 31  ? -9.771  58.318  8.710   1.00 31.70 ?  55   LYS E CG  1 
ATOM   9116  C  CD  . LYS E  1 31  ? -11.094 57.680  8.300   1.00 33.05 ?  55   LYS E CD  1 
ATOM   9117  C  CE  . LYS E  1 31  ? -12.149 57.871  9.385   1.00 34.31 ?  55   LYS E CE  1 
ATOM   9118  N  NZ  . LYS E  1 31  ? -13.312 56.958  9.206   1.00 34.62 ?  55   LYS E NZ  1 
ATOM   9119  N  N   . ARG E  1 32  ? -7.092  56.093  9.946   1.00 29.86 ?  56   ARG E N   1 
ATOM   9120  C  CA  . ARG E  1 32  ? -6.965  55.400  11.233  1.00 29.63 ?  56   ARG E CA  1 
ATOM   9121  C  C   . ARG E  1 32  ? -5.578  55.630  11.841  1.00 29.64 ?  56   ARG E C   1 
ATOM   9122  O  O   . ARG E  1 32  ? -5.455  55.946  13.028  1.00 29.47 ?  56   ARG E O   1 
ATOM   9123  C  CB  . ARG E  1 32  ? -7.250  53.898  11.083  1.00 29.38 ?  56   ARG E CB  1 
ATOM   9124  C  CG  . ARG E  1 32  ? -7.113  53.108  12.387  1.00 28.91 ?  56   ARG E CG  1 
ATOM   9125  C  CD  . ARG E  1 32  ? -7.590  51.666  12.261  1.00 27.99 ?  56   ARG E CD  1 
ATOM   9126  N  NE  . ARG E  1 32  ? -6.713  50.858  11.413  1.00 26.88 ?  56   ARG E NE  1 
ATOM   9127  C  CZ  . ARG E  1 32  ? -6.802  49.539  11.273  1.00 25.91 ?  56   ARG E CZ  1 
ATOM   9128  N  NH1 . ARG E  1 32  ? -7.728  48.852  11.930  1.00 25.82 ?  56   ARG E NH1 1 
ATOM   9129  N  NH2 . ARG E  1 32  ? -5.955  48.902  10.474  1.00 25.03 ?  56   ARG E NH2 1 
ATOM   9130  N  N   . TYR E  1 33  ? -4.550  55.489  11.006  1.00 29.79 ?  57   TYR E N   1 
ATOM   9131  C  CA  . TYR E  1 33  ? -3.145  55.627  11.405  1.00 29.96 ?  57   TYR E CA  1 
ATOM   9132  C  C   . TYR E  1 33  ? -2.832  56.960  12.090  1.00 30.26 ?  57   TYR E C   1 
ATOM   9133  O  O   . TYR E  1 33  ? -2.026  57.011  13.018  1.00 30.15 ?  57   TYR E O   1 
ATOM   9134  C  CB  . TYR E  1 33  ? -2.244  55.437  10.174  1.00 29.76 ?  57   TYR E CB  1 
ATOM   9135  C  CG  . TYR E  1 33  ? -0.766  55.671  10.399  1.00 29.14 ?  57   TYR E CG  1 
ATOM   9136  C  CD1 . TYR E  1 33  ? 0.010   54.744  11.097  1.00 28.29 ?  57   TYR E CD1 1 
ATOM   9137  C  CD2 . TYR E  1 33  ? -0.137  56.810  9.889   1.00 28.43 ?  57   TYR E CD2 1 
ATOM   9138  C  CE1 . TYR E  1 33  ? 1.370   54.953  11.298  1.00 28.18 ?  57   TYR E CE1 1 
ATOM   9139  C  CE2 . TYR E  1 33  ? 1.227   57.028  10.081  1.00 28.44 ?  57   TYR E CE2 1 
ATOM   9140  C  CZ  . TYR E  1 33  ? 1.973   56.094  10.789  1.00 28.36 ?  57   TYR E CZ  1 
ATOM   9141  O  OH  . TYR E  1 33  ? 3.318   56.302  10.987  1.00 27.91 ?  57   TYR E OH  1 
ATOM   9142  N  N   . LYS E  1 34  ? -3.475  58.028  11.628  1.00 30.69 ?  58   LYS E N   1 
ATOM   9143  C  CA  . LYS E  1 34  ? -3.175  59.377  12.105  1.00 31.14 ?  58   LYS E CA  1 
ATOM   9144  C  C   . LYS E  1 34  ? -4.175  59.900  13.134  1.00 31.15 ?  58   LYS E C   1 
ATOM   9145  O  O   . LYS E  1 34  ? -4.078  61.048  13.574  1.00 31.02 ?  58   LYS E O   1 
ATOM   9146  C  CB  . LYS E  1 34  ? -3.081  60.344  10.926  1.00 31.31 ?  58   LYS E CB  1 
ATOM   9147  C  CG  . LYS E  1 34  ? -1.722  60.373  10.255  1.00 32.27 ?  58   LYS E CG  1 
ATOM   9148  C  CD  . LYS E  1 34  ? -1.720  61.382  9.119   1.00 33.99 ?  58   LYS E CD  1 
ATOM   9149  C  CE  . LYS E  1 34  ? -0.352  61.999  8.944   1.00 35.20 ?  58   LYS E CE  1 
ATOM   9150  N  NZ  . LYS E  1 34  ? -0.354  63.045  7.882   1.00 36.68 ?  58   LYS E NZ  1 
ATOM   9151  N  N   . ASP E  1 35  ? -5.123  59.048  13.517  1.00 31.30 ?  59   ASP E N   1 
ATOM   9152  C  CA  . ASP E  1 35  ? -6.155  59.412  14.479  1.00 31.47 ?  59   ASP E CA  1 
ATOM   9153  C  C   . ASP E  1 35  ? -5.637  59.249  15.910  1.00 31.42 ?  59   ASP E C   1 
ATOM   9154  O  O   . ASP E  1 35  ? -5.198  58.160  16.287  1.00 31.29 ?  59   ASP E O   1 
ATOM   9155  C  CB  . ASP E  1 35  ? -7.408  58.553  14.258  1.00 31.68 ?  59   ASP E CB  1 
ATOM   9156  C  CG  . ASP E  1 35  ? -8.601  59.023  15.078  1.00 32.27 ?  59   ASP E CG  1 
ATOM   9157  O  OD1 . ASP E  1 35  ? -8.703  60.234  15.365  1.00 33.32 ?  59   ASP E OD1 1 
ATOM   9158  O  OD2 . ASP E  1 35  ? -9.445  58.175  15.434  1.00 33.62 -1 59   ASP E OD2 1 
ATOM   9159  N  N   . PRO E  1 36  ? -5.673  60.338  16.708  1.00 31.41 ?  60   PRO E N   1 
ATOM   9160  C  CA  . PRO E  1 36  ? -5.254  60.281  18.114  1.00 31.38 ?  60   PRO E CA  1 
ATOM   9161  C  C   . PRO E  1 36  ? -5.955  59.181  18.912  1.00 31.21 ?  60   PRO E C   1 
ATOM   9162  O  O   . PRO E  1 36  ? -5.335  58.552  19.767  1.00 31.46 ?  60   PRO E O   1 
ATOM   9163  C  CB  . PRO E  1 36  ? -5.650  61.659  18.645  1.00 31.37 ?  60   PRO E CB  1 
ATOM   9164  C  CG  . PRO E  1 36  ? -5.509  62.548  17.466  1.00 31.43 ?  60   PRO E CG  1 
ATOM   9165  C  CD  . PRO E  1 36  ? -5.960  61.723  16.286  1.00 31.39 ?  60   PRO E CD  1 
ATOM   9166  N  N   . ALA E  1 37  ? -7.232  58.949  18.617  1.00 30.96 ?  61   ALA E N   1 
ATOM   9167  C  CA  . ALA E  1 37  ? -8.015  57.908  19.279  1.00 30.63 ?  61   ALA E CA  1 
ATOM   9168  C  C   . ALA E  1 37  ? -7.478  56.510  18.969  1.00 30.28 ?  61   ALA E C   1 
ATOM   9169  O  O   . ALA E  1 37  ? -7.699  55.574  19.736  1.00 30.32 ?  61   ALA E O   1 
ATOM   9170  C  CB  . ALA E  1 37  ? -9.490  58.019  18.880  1.00 30.58 ?  61   ALA E CB  1 
ATOM   9171  N  N   . HIS E  1 38  ? -6.781  56.381  17.841  1.00 29.92 ?  62   HIS E N   1 
ATOM   9172  C  CA  . HIS E  1 38  ? -6.166  55.114  17.441  1.00 29.56 ?  62   HIS E CA  1 
ATOM   9173  C  C   . HIS E  1 38  ? -4.663  55.039  17.749  1.00 29.26 ?  62   HIS E C   1 
ATOM   9174  O  O   . HIS E  1 38  ? -3.967  54.129  17.278  1.00 29.21 ?  62   HIS E O   1 
ATOM   9175  C  CB  . HIS E  1 38  ? -6.456  54.819  15.964  1.00 29.48 ?  62   HIS E CB  1 
ATOM   9176  C  CG  . HIS E  1 38  ? -7.844  54.312  15.712  1.00 29.63 ?  62   HIS E CG  1 
ATOM   9177  N  ND1 . HIS E  1 38  ? -8.902  55.146  15.420  1.00 29.69 ?  62   HIS E ND1 1 
ATOM   9178  C  CD2 . HIS E  1 38  ? -8.347  53.054  15.713  1.00 29.58 ?  62   HIS E CD2 1 
ATOM   9179  C  CE1 . HIS E  1 38  ? -9.995  54.424  15.246  1.00 30.00 ?  62   HIS E CE1 1 
ATOM   9180  N  NE2 . HIS E  1 38  ? -9.685  53.151  15.419  1.00 29.16 ?  62   HIS E NE2 1 
ATOM   9181  N  N   . GLY E  1 39  ? -4.169  55.995  18.539  1.00 28.92 ?  63   GLY E N   1 
ATOM   9182  C  CA  . GLY E  1 39  ? -2.806  55.930  19.077  1.00 28.62 ?  63   GLY E CA  1 
ATOM   9183  C  C   . GLY E  1 39  ? -1.821  57.015  18.670  1.00 28.35 ?  63   GLY E C   1 
ATOM   9184  O  O   . GLY E  1 39  ? -0.750  57.135  19.275  1.00 28.34 ?  63   GLY E O   1 
ATOM   9185  N  N   . ALA E  1 40  ? -2.171  57.798  17.650  1.00 28.03 ?  64   ALA E N   1 
ATOM   9186  C  CA  . ALA E  1 40  ? -1.297  58.862  17.145  1.00 27.91 ?  64   ALA E CA  1 
ATOM   9187  C  C   . ALA E  1 40  ? -1.203  60.052  18.107  1.00 27.76 ?  64   ALA E C   1 
ATOM   9188  O  O   . ALA E  1 40  ? -2.011  60.183  19.022  1.00 27.91 ?  64   ALA E O   1 
ATOM   9189  C  CB  . ALA E  1 40  ? -1.764  59.324  15.762  1.00 27.84 ?  64   ALA E CB  1 
ATOM   9190  N  N   . GLY E  1 41  ? -0.210  60.912  17.891  1.00 27.67 ?  65   GLY E N   1 
ATOM   9191  C  CA  . GLY E  1 41  ? -0.044  62.129  18.689  1.00 27.33 ?  65   GLY E CA  1 
ATOM   9192  C  C   . GLY E  1 41  ? 0.730   61.915  19.978  1.00 27.26 ?  65   GLY E C   1 
ATOM   9193  O  O   . GLY E  1 41  ? 1.605   61.047  20.055  1.00 27.09 ?  65   GLY E O   1 
ATOM   9194  N  N   . LYS E  1 42  ? 0.399   62.709  20.992  1.00 27.13 ?  66   LYS E N   1 
ATOM   9195  C  CA  . LYS E  1 42  ? 1.086   62.658  22.283  1.00 27.14 ?  66   LYS E CA  1 
ATOM   9196  C  C   . LYS E  1 42  ? 0.464   61.657  23.261  1.00 27.02 ?  66   LYS E C   1 
ATOM   9197  O  O   . LYS E  1 42  ? 1.052   61.348  24.305  1.00 27.03 ?  66   LYS E O   1 
ATOM   9198  C  CB  . LYS E  1 42  ? 1.142   64.052  22.915  1.00 27.18 ?  66   LYS E CB  1 
ATOM   9199  C  CG  . LYS E  1 42  ? 2.021   65.052  22.161  1.00 27.73 ?  66   LYS E CG  1 
ATOM   9200  C  CD  . LYS E  1 42  ? 2.230   66.343  22.955  1.00 28.66 ?  66   LYS E CD  1 
ATOM   9201  C  CE  . LYS E  1 42  ? 3.230   66.153  24.102  1.00 29.36 ?  66   LYS E CE  1 
ATOM   9202  N  NZ  . LYS E  1 42  ? 3.319   67.347  24.993  1.00 28.99 ?  66   LYS E NZ  1 
ATOM   9203  N  N   . GLY E  1 43  ? -0.720  61.153  22.924  1.00 26.86 ?  67   GLY E N   1 
ATOM   9204  C  CA  . GLY E  1 43  ? -1.406  60.178  23.773  1.00 27.05 ?  67   GLY E CA  1 
ATOM   9205  C  C   . GLY E  1 43  ? -2.032  60.782  25.016  1.00 27.11 ?  67   GLY E C   1 
ATOM   9206  O  O   . GLY E  1 43  ? -2.061  62.006  25.177  1.00 26.98 ?  67   GLY E O   1 
ATOM   9207  N  N   . THR E  1 44  ? -2.514  59.917  25.907  1.00 27.42 ?  68   THR E N   1 
ATOM   9208  C  CA  . THR E  1 44  ? -3.352  60.337  27.040  1.00 27.49 ?  68   THR E CA  1 
ATOM   9209  C  C   . THR E  1 44  ? -2.604  61.101  28.135  1.00 27.77 ?  68   THR E C   1 
ATOM   9210  O  O   . THR E  1 44  ? -3.223  61.804  28.940  1.00 27.87 ?  68   THR E O   1 
ATOM   9211  C  CB  . THR E  1 44  ? -4.104  59.144  27.686  1.00 27.63 ?  68   THR E CB  1 
ATOM   9212  O  OG1 . THR E  1 44  ? -3.194  58.356  28.469  1.00 27.59 ?  68   THR E OG1 1 
ATOM   9213  C  CG2 . THR E  1 44  ? -4.777  58.269  26.619  1.00 27.34 ?  68   THR E CG2 1 
ATOM   9214  N  N   . MET E  1 45  ? -1.282  60.955  28.171  1.00 27.83 ?  69   MET E N   1 
ATOM   9215  C  CA  . MET E  1 45  ? -0.469  61.611  29.195  1.00 27.97 ?  69   MET E CA  1 
ATOM   9216  C  C   . MET E  1 45  ? 0.400   62.730  28.610  1.00 28.07 ?  69   MET E C   1 
ATOM   9217  O  O   . MET E  1 45  ? 1.412   63.121  29.199  1.00 28.05 ?  69   MET E O   1 
ATOM   9218  C  CB  . MET E  1 45  ? 0.372   60.579  29.957  1.00 27.84 ?  69   MET E CB  1 
ATOM   9219  C  CG  . MET E  1 45  ? -0.449  59.646  30.844  1.00 27.81 ?  69   MET E CG  1 
ATOM   9220  S  SD  . MET E  1 45  ? 0.511   58.332  31.635  1.00 27.75 ?  69   MET E SD  1 
ATOM   9221  C  CE  . MET E  1 45  ? 0.956   57.336  30.212  1.00 27.85 ?  69   MET E CE  1 
ATOM   9222  N  N   . GLY E  1 46  ? -0.029  63.260  27.465  1.00 28.23 ?  70   GLY E N   1 
ATOM   9223  C  CA  . GLY E  1 46  ? 0.688   64.327  26.761  1.00 28.52 ?  70   GLY E CA  1 
ATOM   9224  C  C   . GLY E  1 46  ? 0.948   65.608  27.540  1.00 28.72 ?  70   GLY E C   1 
ATOM   9225  O  O   . GLY E  1 46  ? 1.885   66.345  27.225  1.00 28.94 ?  70   GLY E O   1 
ATOM   9226  N  N   . ASP E  1 47  ? 0.130   65.880  28.556  1.00 28.84 ?  71   ASP E N   1 
ATOM   9227  C  CA  . ASP E  1 47  ? 0.290   67.099  29.360  1.00 29.02 ?  71   ASP E CA  1 
ATOM   9228  C  C   . ASP E  1 47  ? 1.416   67.002  30.387  1.00 28.98 ?  71   ASP E C   1 
ATOM   9229  O  O   . ASP E  1 47  ? 1.733   67.986  31.066  1.00 29.12 ?  71   ASP E O   1 
ATOM   9230  C  CB  . ASP E  1 47  ? -1.025  67.476  30.055  1.00 29.20 ?  71   ASP E CB  1 
ATOM   9231  C  CG  . ASP E  1 47  ? -2.100  67.924  29.078  1.00 29.85 ?  71   ASP E CG  1 
ATOM   9232  O  OD1 . ASP E  1 47  ? -1.764  68.482  28.012  1.00 30.26 ?  71   ASP E OD1 1 
ATOM   9233  O  OD2 . ASP E  1 47  ? -3.291  67.719  29.381  1.00 31.59 -1 71   ASP E OD2 1 
ATOM   9234  N  N   . TYR E  1 48  ? 2.025   65.823  30.492  1.00 28.62 ?  72   TYR E N   1 
ATOM   9235  C  CA  . TYR E  1 48  ? 3.057   65.582  31.496  1.00 28.37 ?  72   TYR E CA  1 
ATOM   9236  C  C   . TYR E  1 48  ? 4.485   65.661  30.954  1.00 28.18 ?  72   TYR E C   1 
ATOM   9237  O  O   . TYR E  1 48  ? 5.439   65.746  31.731  1.00 28.04 ?  72   TYR E O   1 
ATOM   9238  C  CB  . TYR E  1 48  ? 2.815   64.236  32.186  1.00 28.53 ?  72   TYR E CB  1 
ATOM   9239  C  CG  . TYR E  1 48  ? 1.547   64.215  33.010  1.00 28.50 ?  72   TYR E CG  1 
ATOM   9240  C  CD1 . TYR E  1 48  ? 0.336   63.789  32.460  1.00 28.96 ?  72   TYR E CD1 1 
ATOM   9241  C  CD2 . TYR E  1 48  ? 1.555   64.639  34.335  1.00 28.69 ?  72   TYR E CD2 1 
ATOM   9242  C  CE1 . TYR E  1 48  ? -0.835  63.779  33.218  1.00 29.17 ?  72   TYR E CE1 1 
ATOM   9243  C  CE2 . TYR E  1 48  ? 0.398   64.632  35.098  1.00 29.24 ?  72   TYR E CE2 1 
ATOM   9244  C  CZ  . TYR E  1 48  ? -0.793  64.200  34.538  1.00 29.24 ?  72   TYR E CZ  1 
ATOM   9245  O  OH  . TYR E  1 48  ? -1.936  64.197  35.305  1.00 29.31 ?  72   TYR E OH  1 
ATOM   9246  N  N   . TRP E  1 49  ? 4.627   65.649  29.629  1.00 27.82 ?  73   TRP E N   1 
ATOM   9247  C  CA  . TRP E  1 49  ? 5.945   65.629  29.002  1.00 27.67 ?  73   TRP E CA  1 
ATOM   9248  C  C   . TRP E  1 49  ? 6.011   66.527  27.777  1.00 27.95 ?  73   TRP E C   1 
ATOM   9249  O  O   . TRP E  1 49  ? 5.004   66.762  27.112  1.00 27.96 ?  73   TRP E O   1 
ATOM   9250  C  CB  . TRP E  1 49  ? 6.348   64.197  28.619  1.00 27.37 ?  73   TRP E CB  1 
ATOM   9251  C  CG  . TRP E  1 49  ? 5.431   63.554  27.613  1.00 25.91 ?  73   TRP E CG  1 
ATOM   9252  C  CD1 . TRP E  1 49  ? 4.286   62.866  27.878  1.00 25.14 ?  73   TRP E CD1 1 
ATOM   9253  C  CD2 . TRP E  1 49  ? 5.586   63.540  26.186  1.00 24.70 ?  73   TRP E CD2 1 
ATOM   9254  N  NE1 . TRP E  1 49  ? 3.716   62.422  26.711  1.00 24.24 ?  73   TRP E NE1 1 
ATOM   9255  C  CE2 . TRP E  1 49  ? 4.490   62.825  25.656  1.00 24.17 ?  73   TRP E CE2 1 
ATOM   9256  C  CE3 . TRP E  1 49  ? 6.545   64.061  25.304  1.00 24.08 ?  73   TRP E CE3 1 
ATOM   9257  C  CZ2 . TRP E  1 49  ? 4.325   62.610  24.282  1.00 24.27 ?  73   TRP E CZ2 1 
ATOM   9258  C  CZ3 . TRP E  1 49  ? 6.378   63.852  23.935  1.00 24.24 ?  73   TRP E CZ3 1 
ATOM   9259  C  CH2 . TRP E  1 49  ? 5.277   63.130  23.439  1.00 23.55 ?  73   TRP E CH2 1 
ATOM   9260  N  N   . GLU E  1 50  ? 7.213   67.016  27.493  1.00 28.16 ?  74   GLU E N   1 
ATOM   9261  C  CA  . GLU E  1 50  ? 7.471   67.854  26.331  1.00 28.59 ?  74   GLU E CA  1 
ATOM   9262  C  C   . GLU E  1 50  ? 8.506   67.166  25.454  1.00 28.40 ?  74   GLU E C   1 
ATOM   9263  O  O   . GLU E  1 50  ? 9.377   66.459  25.967  1.00 28.42 ?  74   GLU E O   1 
ATOM   9264  C  CB  . GLU E  1 50  ? 7.981   69.239  26.761  1.00 28.85 ?  74   GLU E CB  1 
ATOM   9265  C  CG  . GLU E  1 50  ? 6.909   70.166  27.348  1.00 30.08 ?  74   GLU E CG  1 
ATOM   9266  C  CD  . GLU E  1 50  ? 6.384   69.691  28.691  1.00 32.34 ?  74   GLU E CD  1 
ATOM   9267  O  OE1 . GLU E  1 50  ? 5.148   69.667  28.879  1.00 33.93 ?  74   GLU E OE1 1 
ATOM   9268  O  OE2 . GLU E  1 50  ? 7.205   69.318  29.556  1.00 33.49 -1 74   GLU E OE2 1 
ATOM   9269  N  N   . PRO E  1 51  ? 8.418   67.361  24.128  1.00 28.26 ?  75   PRO E N   1 
ATOM   9270  C  CA  . PRO E  1 51  ? 9.426   66.786  23.241  1.00 28.08 ?  75   PRO E CA  1 
ATOM   9271  C  C   . PRO E  1 51  ? 10.801  67.400  23.490  1.00 27.79 ?  75   PRO E C   1 
ATOM   9272  O  O   . PRO E  1 51  ? 10.900  68.551  23.924  1.00 27.90 ?  75   PRO E O   1 
ATOM   9273  C  CB  . PRO E  1 51  ? 8.924   67.175  21.847  1.00 28.06 ?  75   PRO E CB  1 
ATOM   9274  C  CG  . PRO E  1 51  ? 8.077   68.392  22.073  1.00 28.15 ?  75   PRO E CG  1 
ATOM   9275  C  CD  . PRO E  1 51  ? 7.407   68.133  23.382  1.00 28.34 ?  75   PRO E CD  1 
ATOM   9276  N  N   . ILE E  1 52  ? 11.848  66.622  23.241  1.00 27.31 ?  76   ILE E N   1 
ATOM   9277  C  CA  . ILE E  1 52  ? 13.207  67.152  23.201  1.00 26.92 ?  76   ILE E CA  1 
ATOM   9278  C  C   . ILE E  1 52  ? 13.605  67.304  21.734  1.00 26.90 ?  76   ILE E C   1 
ATOM   9279  O  O   . ILE E  1 52  ? 12.798  67.024  20.845  1.00 27.12 ?  76   ILE E O   1 
ATOM   9280  C  CB  . ILE E  1 52  ? 14.211  66.286  24.016  1.00 26.94 ?  76   ILE E CB  1 
ATOM   9281  C  CG1 . ILE E  1 52  ? 14.231  64.832  23.520  1.00 26.45 ?  76   ILE E CG1 1 
ATOM   9282  C  CG2 . ILE E  1 52  ? 13.872  66.354  25.504  1.00 26.20 ?  76   ILE E CG2 1 
ATOM   9283  C  CD1 . ILE E  1 52  ? 15.280  63.950  24.205  1.00 26.13 ?  76   ILE E CD1 1 
ATOM   9284  N  N   . ALA E  1 53  ? 14.827  67.758  21.476  1.00 26.83 ?  77   ALA E N   1 
ATOM   9285  C  CA  . ALA E  1 53  ? 15.269  68.049  20.111  1.00 26.61 ?  77   ALA E CA  1 
ATOM   9286  C  C   . ALA E  1 53  ? 15.153  66.851  19.160  1.00 26.48 ?  77   ALA E C   1 
ATOM   9287  O  O   . ALA E  1 53  ? 14.717  67.003  18.018  1.00 26.40 ?  77   ALA E O   1 
ATOM   9288  C  CB  . ALA E  1 53  ? 16.691  68.603  20.118  1.00 26.63 ?  77   ALA E CB  1 
ATOM   9289  N  N   . ILE E  1 54  ? 15.529  65.666  19.640  1.00 26.29 ?  78   ILE E N   1 
ATOM   9290  C  CA  . ILE E  1 54  ? 15.522  64.451  18.821  1.00 26.07 ?  78   ILE E CA  1 
ATOM   9291  C  C   . ILE E  1 54  ? 14.098  63.951  18.518  1.00 25.97 ?  78   ILE E C   1 
ATOM   9292  O  O   . ILE E  1 54  ? 13.902  63.127  17.617  1.00 25.89 ?  78   ILE E O   1 
ATOM   9293  C  CB  . ILE E  1 54  ? 16.384  63.320  19.467  1.00 26.09 ?  78   ILE E CB  1 
ATOM   9294  C  CG1 . ILE E  1 54  ? 16.854  62.302  18.416  1.00 26.44 ?  78   ILE E CG1 1 
ATOM   9295  C  CG2 . ILE E  1 54  ? 15.634  62.627  20.601  1.00 25.97 ?  78   ILE E CG2 1 
ATOM   9296  C  CD1 . ILE E  1 54  ? 18.075  62.737  17.617  1.00 26.55 ?  78   ILE E CD1 1 
ATOM   9297  N  N   . SER E  1 55  ? 13.115  64.465  19.257  1.00 25.76 ?  79   SER E N   1 
ATOM   9298  C  CA  . SER E  1 55  ? 11.719  64.018  19.130  1.00 25.82 ?  79   SER E CA  1 
ATOM   9299  C  C   . SER E  1 55  ? 11.086  64.330  17.781  1.00 25.66 ?  79   SER E C   1 
ATOM   9300  O  O   . SER E  1 55  ? 10.108  63.689  17.403  1.00 25.74 ?  79   SER E O   1 
ATOM   9301  C  CB  . SER E  1 55  ? 10.849  64.595  20.246  1.00 25.55 ?  79   SER E CB  1 
ATOM   9302  O  OG  . SER E  1 55  ? 11.314  64.184  21.516  1.00 26.12 ?  79   SER E OG  1 
ATOM   9303  N  N   . ILE E  1 56  ? 11.643  65.307  17.063  1.00 25.70 ?  80   ILE E N   1 
ATOM   9304  C  CA  . ILE E  1 56  ? 11.141  65.681  15.736  1.00 25.58 ?  80   ILE E CA  1 
ATOM   9305  C  C   . ILE E  1 56  ? 11.426  64.589  14.697  1.00 25.36 ?  80   ILE E C   1 
ATOM   9306  O  O   . ILE E  1 56  ? 10.792  64.550  13.636  1.00 25.50 ?  80   ILE E O   1 
ATOM   9307  C  CB  . ILE E  1 56  ? 11.681  67.070  15.252  1.00 25.68 ?  80   ILE E CB  1 
ATOM   9308  C  CG1 . ILE E  1 56  ? 13.163  66.990  14.867  1.00 26.12 ?  80   ILE E CG1 1 
ATOM   9309  C  CG2 . ILE E  1 56  ? 11.432  68.156  16.314  1.00 25.68 ?  80   ILE E CG2 1 
ATOM   9310  C  CD1 . ILE E  1 56  ? 13.689  68.194  14.084  1.00 26.27 ?  80   ILE E CD1 1 
ATOM   9311  N  N   . TYR E  1 57  ? 12.374  63.706  15.015  1.00 24.90 ?  81   TYR E N   1 
ATOM   9312  C  CA  . TYR E  1 57  ? 12.721  62.578  14.151  1.00 24.59 ?  81   TYR E CA  1 
ATOM   9313  C  C   . TYR E  1 57  ? 12.042  61.285  14.605  1.00 24.68 ?  81   TYR E C   1 
ATOM   9314  O  O   . TYR E  1 57  ? 11.821  60.378  13.798  1.00 24.64 ?  81   TYR E O   1 
ATOM   9315  C  CB  . TYR E  1 57  ? 14.241  62.383  14.091  1.00 24.40 ?  81   TYR E CB  1 
ATOM   9316  C  CG  . TYR E  1 57  ? 15.002  63.615  13.655  1.00 23.91 ?  81   TYR E CG  1 
ATOM   9317  C  CD1 . TYR E  1 57  ? 15.076  63.977  12.306  1.00 23.39 ?  81   TYR E CD1 1 
ATOM   9318  C  CD2 . TYR E  1 57  ? 15.644  64.422  14.592  1.00 23.09 ?  81   TYR E CD2 1 
ATOM   9319  C  CE1 . TYR E  1 57  ? 15.773  65.116  11.903  1.00 23.05 ?  81   TYR E CE1 1 
ATOM   9320  C  CE2 . TYR E  1 57  ? 16.338  65.557  14.206  1.00 23.11 ?  81   TYR E CE2 1 
ATOM   9321  C  CZ  . TYR E  1 57  ? 16.403  65.900  12.864  1.00 22.99 ?  81   TYR E CZ  1 
ATOM   9322  O  OH  . TYR E  1 57  ? 17.092  67.028  12.496  1.00 21.82 ?  81   TYR E OH  1 
ATOM   9323  N  N   . MET E  1 58  ? 11.717  61.212  15.893  1.00 24.82 ?  82   MET E N   1 
ATOM   9324  C  CA  . MET E  1 58  ? 11.052  60.044  16.481  1.00 25.21 ?  82   MET E CA  1 
ATOM   9325  C  C   . MET E  1 58  ? 9.549   60.032  16.199  1.00 25.46 ?  82   MET E C   1 
ATOM   9326  O  O   . MET E  1 58  ? 8.985   58.982  15.873  1.00 25.37 ?  82   MET E O   1 
ATOM   9327  C  CB  . MET E  1 58  ? 11.299  59.982  17.992  1.00 25.22 ?  82   MET E CB  1 
ATOM   9328  C  CG  . MET E  1 58  ? 12.767  60.004  18.407  1.00 25.36 ?  82   MET E CG  1 
ATOM   9329  S  SD  . MET E  1 58  ? 13.683  58.493  18.026  1.00 25.74 ?  82   MET E SD  1 
ATOM   9330  C  CE  . MET E  1 58  ? 14.453  58.914  16.463  1.00 25.13 ?  82   MET E CE  1 
ATOM   9331  N  N   . ASP E  1 59  ? 8.911   61.197  16.336  1.00 25.49 ?  83   ASP E N   1 
ATOM   9332  C  CA  . ASP E  1 59  ? 7.497   61.366  15.987  1.00 25.81 ?  83   ASP E CA  1 
ATOM   9333  C  C   . ASP E  1 59  ? 7.322   62.603  15.089  1.00 25.92 ?  83   ASP E C   1 
ATOM   9334  O  O   . ASP E  1 59  ? 6.883   63.660  15.555  1.00 25.83 ?  83   ASP E O   1 
ATOM   9335  C  CB  . ASP E  1 59  ? 6.637   61.464  17.255  1.00 25.70 ?  83   ASP E CB  1 
ATOM   9336  C  CG  . ASP E  1 59  ? 5.136   61.495  16.961  1.00 26.48 ?  83   ASP E CG  1 
ATOM   9337  O  OD1 . ASP E  1 59  ? 4.714   61.257  15.805  1.00 27.05 ?  83   ASP E OD1 1 
ATOM   9338  O  OD2 . ASP E  1 59  ? 4.366   61.763  17.905  1.00 26.89 -1 83   ASP E OD2 1 
ATOM   9339  N  N   . PRO E  1 60  ? 7.686   62.476  13.798  1.00 26.00 ?  84   PRO E N   1 
ATOM   9340  C  CA  . PRO E  1 60  ? 7.646   63.618  12.881  1.00 26.30 ?  84   PRO E CA  1 
ATOM   9341  C  C   . PRO E  1 60  ? 6.256   64.219  12.662  1.00 26.52 ?  84   PRO E C   1 
ATOM   9342  O  O   . PRO E  1 60  ? 6.133   65.443  12.589  1.00 26.46 ?  84   PRO E O   1 
ATOM   9343  C  CB  . PRO E  1 60  ? 8.197   63.040  11.575  1.00 26.30 ?  84   PRO E CB  1 
ATOM   9344  C  CG  . PRO E  1 60  ? 9.037   61.887  12.009  1.00 26.14 ?  84   PRO E CG  1 
ATOM   9345  C  CD  . PRO E  1 60  ? 8.314   61.300  13.168  1.00 25.87 ?  84   PRO E CD  1 
ATOM   9346  N  N   . ASN E  1 61  ? 5.230   63.370  12.572  1.00 26.66 ?  85   ASN E N   1 
ATOM   9347  C  CA  . ASN E  1 61  ? 3.857   63.828  12.331  1.00 26.91 ?  85   ASN E CA  1 
ATOM   9348  C  C   . ASN E  1 61  ? 3.308   64.755  13.418  1.00 27.12 ?  85   ASN E C   1 
ATOM   9349  O  O   . ASN E  1 61  ? 2.481   65.625  13.136  1.00 27.33 ?  85   ASN E O   1 
ATOM   9350  C  CB  . ASN E  1 61  ? 2.908   62.642  12.080  1.00 26.73 ?  85   ASN E CB  1 
ATOM   9351  C  CG  . ASN E  1 61  ? 3.030   62.076  10.658  1.00 26.94 ?  85   ASN E CG  1 
ATOM   9352  O  OD1 . ASN E  1 61  ? 3.450   62.772  9.725   1.00 26.82 ?  85   ASN E OD1 1 
ATOM   9353  N  ND2 . ASN E  1 61  ? 2.654   60.812  10.491  1.00 25.77 ?  85   ASN E ND2 1 
ATOM   9354  N  N   . THR E  1 62  ? 3.780   64.577  14.648  1.00 27.20 ?  86   THR E N   1 
ATOM   9355  C  CA  . THR E  1 62  ? 3.383   65.444  15.757  1.00 27.42 ?  86   THR E CA  1 
ATOM   9356  C  C   . THR E  1 62  ? 4.323   66.640  15.914  1.00 27.49 ?  86   THR E C   1 
ATOM   9357  O  O   . THR E  1 62  ? 3.872   67.756  16.190  1.00 27.49 ?  86   THR E O   1 
ATOM   9358  C  CB  . THR E  1 62  ? 3.331   64.667  17.095  1.00 27.41 ?  86   THR E CB  1 
ATOM   9359  O  OG1 . THR E  1 62  ? 2.557   63.476  16.927  1.00 27.58 ?  86   THR E OG1 1 
ATOM   9360  C  CG2 . THR E  1 62  ? 2.711   65.515  18.212  1.00 27.50 ?  86   THR E CG2 1 
ATOM   9361  N  N   . PHE E  1 63  ? 5.620   66.408  15.721  1.00 27.48 ?  87   PHE E N   1 
ATOM   9362  C  CA  . PHE E  1 63  ? 6.630   67.372  16.154  1.00 27.65 ?  87   PHE E CA  1 
ATOM   9363  C  C   . PHE E  1 63  ? 7.474   68.058  15.077  1.00 27.72 ?  87   PHE E C   1 
ATOM   9364  O  O   . PHE E  1 63  ? 8.040   69.120  15.340  1.00 27.62 ?  87   PHE E O   1 
ATOM   9365  C  CB  . PHE E  1 63  ? 7.557   66.729  17.194  1.00 27.44 ?  87   PHE E CB  1 
ATOM   9366  C  CG  . PHE E  1 63  ? 6.856   66.299  18.450  1.00 27.28 ?  87   PHE E CG  1 
ATOM   9367  C  CD1 . PHE E  1 63  ? 6.061   67.195  19.167  1.00 27.17 ?  87   PHE E CD1 1 
ATOM   9368  C  CD2 . PHE E  1 63  ? 7.009   65.002  18.934  1.00 26.69 ?  87   PHE E CD2 1 
ATOM   9369  C  CE1 . PHE E  1 63  ? 5.413   66.798  20.338  1.00 27.07 ?  87   PHE E CE1 1 
ATOM   9370  C  CE2 . PHE E  1 63  ? 6.369   64.597  20.105  1.00 26.73 ?  87   PHE E CE2 1 
ATOM   9371  C  CZ  . PHE E  1 63  ? 5.569   65.498  20.807  1.00 27.00 ?  87   PHE E CZ  1 
ATOM   9372  N  N   . TYR E  1 64  ? 7.567   67.474  13.884  1.00 28.00 ?  88   TYR E N   1 
ATOM   9373  C  CA  . TYR E  1 64  ? 8.541   67.961  12.899  1.00 28.43 ?  88   TYR E CA  1 
ATOM   9374  C  C   . TYR E  1 64  ? 8.152   69.226  12.121  1.00 29.01 ?  88   TYR E C   1 
ATOM   9375  O  O   . TYR E  1 64  ? 7.081   69.311  11.521  1.00 28.83 ?  88   TYR E O   1 
ATOM   9376  C  CB  . TYR E  1 64  ? 8.974   66.868  11.914  1.00 28.12 ?  88   TYR E CB  1 
ATOM   9377  C  CG  . TYR E  1 64  ? 10.081  67.332  10.986  1.00 28.02 ?  88   TYR E CG  1 
ATOM   9378  C  CD1 . TYR E  1 64  ? 11.418  67.258  11.377  1.00 27.50 ?  88   TYR E CD1 1 
ATOM   9379  C  CD2 . TYR E  1 64  ? 9.789   67.876  9.732   1.00 27.32 ?  88   TYR E CD2 1 
ATOM   9380  C  CE1 . TYR E  1 64  ? 12.437  67.699  10.545  1.00 26.91 ?  88   TYR E CE1 1 
ATOM   9381  C  CE2 . TYR E  1 64  ? 10.802  68.322  8.892   1.00 27.26 ?  88   TYR E CE2 1 
ATOM   9382  C  CZ  . TYR E  1 64  ? 12.125  68.228  9.307   1.00 27.34 ?  88   TYR E CZ  1 
ATOM   9383  O  OH  . TYR E  1 64  ? 13.135  68.662  8.484   1.00 27.14 ?  88   TYR E OH  1 
ATOM   9384  N  N   . LYS E  1 65  ? 9.066   70.187  12.133  1.00 29.85 ?  89   LYS E N   1 
ATOM   9385  C  CA  . LYS E  1 65  ? 9.045   71.303  11.203  1.00 30.66 ?  89   LYS E CA  1 
ATOM   9386  C  C   . LYS E  1 65  ? 10.427  71.414  10.557  1.00 31.03 ?  89   LYS E C   1 
ATOM   9387  O  O   . LYS E  1 65  ? 11.436  71.123  11.207  1.00 31.09 ?  89   LYS E O   1 
ATOM   9388  C  CB  . LYS E  1 65  ? 8.641   72.604  11.907  1.00 30.78 ?  89   LYS E CB  1 
ATOM   9389  C  CG  . LYS E  1 65  ? 7.125   72.759  12.061  1.00 31.59 ?  89   LYS E CG  1 
ATOM   9390  C  CD  . LYS E  1 65  ? 6.730   74.185  12.447  1.00 33.68 ?  89   LYS E CD  1 
ATOM   9391  C  CE  . LYS E  1 65  ? 5.274   74.483  12.078  1.00 34.53 ?  89   LYS E CE  1 
ATOM   9392  N  NZ  . LYS E  1 65  ? 4.297   73.709  12.902  1.00 36.14 ?  89   LYS E NZ  1 
ATOM   9393  N  N   . PRO E  1 66  ? 10.476  71.799  9.267   1.00 31.48 ?  90   PRO E N   1 
ATOM   9394  C  CA  . PRO E  1 66  ? 11.745  71.948  8.545   1.00 31.96 ?  90   PRO E CA  1 
ATOM   9395  C  C   . PRO E  1 66  ? 12.648  73.029  9.158   1.00 32.46 ?  90   PRO E C   1 
ATOM   9396  O  O   . PRO E  1 66  ? 12.148  73.898  9.874   1.00 32.53 ?  90   PRO E O   1 
ATOM   9397  C  CB  . PRO E  1 66  ? 11.304  72.341  7.126   1.00 31.84 ?  90   PRO E CB  1 
ATOM   9398  C  CG  . PRO E  1 66  ? 9.884   72.776  7.253   1.00 31.68 ?  90   PRO E CG  1 
ATOM   9399  C  CD  . PRO E  1 66  ? 9.314   71.995  8.381   1.00 31.50 ?  90   PRO E CD  1 
ATOM   9400  N  N   . PRO E  1 67  ? 13.970  72.969  8.892   1.00 33.01 ?  91   PRO E N   1 
ATOM   9401  C  CA  . PRO E  1 67  ? 14.907  73.939  9.469   1.00 33.70 ?  91   PRO E CA  1 
ATOM   9402  C  C   . PRO E  1 67  ? 14.718  75.343  8.899   1.00 34.31 ?  91   PRO E C   1 
ATOM   9403  O  O   . PRO E  1 67  ? 14.322  75.488  7.740   1.00 34.19 ?  91   PRO E O   1 
ATOM   9404  C  CB  . PRO E  1 67  ? 16.286  73.399  9.058   1.00 33.63 ?  91   PRO E CB  1 
ATOM   9405  C  CG  . PRO E  1 67  ? 16.055  72.033  8.524   1.00 33.47 ?  91   PRO E CG  1 
ATOM   9406  C  CD  . PRO E  1 67  ? 14.657  72.008  8.012   1.00 33.17 ?  91   PRO E CD  1 
ATOM   9407  N  N   . VAL E  1 68  ? 15.008  76.357  9.714   1.00 35.17 ?  92   VAL E N   1 
ATOM   9408  C  CA  . VAL E  1 68  ? 14.903  77.763  9.295   1.00 36.03 ?  92   VAL E CA  1 
ATOM   9409  C  C   . VAL E  1 68  ? 15.950  78.154  8.245   1.00 36.65 ?  92   VAL E C   1 
ATOM   9410  O  O   . VAL E  1 68  ? 15.722  79.059  7.441   1.00 36.88 ?  92   VAL E O   1 
ATOM   9411  C  CB  . VAL E  1 68  ? 14.954  78.747  10.497  1.00 36.07 ?  92   VAL E CB  1 
ATOM   9412  C  CG1 . VAL E  1 68  ? 13.673  78.650  11.330  1.00 36.20 ?  92   VAL E CG1 1 
ATOM   9413  C  CG2 . VAL E  1 68  ? 16.196  78.515  11.359  1.00 36.03 ?  92   VAL E CG2 1 
ATOM   9414  N  N   . SER E  1 69  ? 17.094  77.475  8.270   1.00 37.34 ?  93   SER E N   1 
ATOM   9415  C  CA  . SER E  1 69  ? 18.121  77.627  7.241   1.00 37.98 ?  93   SER E CA  1 
ATOM   9416  C  C   . SER E  1 69  ? 18.679  76.249  6.859   1.00 38.33 ?  93   SER E C   1 
ATOM   9417  O  O   . SER E  1 69  ? 18.657  75.331  7.681   1.00 38.40 ?  93   SER E O   1 
ATOM   9418  C  CB  . SER E  1 69  ? 19.234  78.574  7.708   1.00 38.06 ?  93   SER E CB  1 
ATOM   9419  O  OG  . SER E  1 69  ? 20.133  77.931  8.591   1.00 38.66 ?  93   SER E OG  1 
ATOM   9420  N  N   . PRO E  1 70  ? 19.187  76.095  5.620   1.00 38.69 ?  94   PRO E N   1 
ATOM   9421  C  CA  . PRO E  1 70  ? 19.383  77.112  4.583   1.00 39.17 ?  94   PRO E CA  1 
ATOM   9422  C  C   . PRO E  1 70  ? 18.079  77.636  3.982   1.00 39.52 ?  94   PRO E C   1 
ATOM   9423  O  O   . PRO E  1 70  ? 17.091  76.901  3.892   1.00 39.33 ?  94   PRO E O   1 
ATOM   9424  C  CB  . PRO E  1 70  ? 20.193  76.368  3.519   1.00 39.01 ?  94   PRO E CB  1 
ATOM   9425  C  CG  . PRO E  1 70  ? 19.767  74.960  3.660   1.00 38.94 ?  94   PRO E CG  1 
ATOM   9426  C  CD  . PRO E  1 70  ? 19.556  74.753  5.134   1.00 38.75 ?  94   PRO E CD  1 
ATOM   9427  N  N   . LYS E  1 71  ? 18.090  78.908  3.592   1.00 40.11 ?  95   LYS E N   1 
ATOM   9428  C  CA  . LYS E  1 71  ? 16.972  79.516  2.890   1.00 40.59 ?  95   LYS E CA  1 
ATOM   9429  C  C   . LYS E  1 71  ? 17.170  79.259  1.398   1.00 40.78 ?  95   LYS E C   1 
ATOM   9430  O  O   . LYS E  1 71  ? 17.776  80.067  0.685   1.00 40.94 ?  95   LYS E O   1 
ATOM   9431  C  CB  . LYS E  1 71  ? 16.904  81.013  3.201   1.00 40.78 ?  95   LYS E CB  1 
ATOM   9432  C  CG  . LYS E  1 71  ? 15.510  81.625  3.086   1.00 41.59 ?  95   LYS E CG  1 
ATOM   9433  C  CD  . LYS E  1 71  ? 15.390  82.920  3.900   1.00 43.33 ?  95   LYS E CD  1 
ATOM   9434  C  CE  . LYS E  1 71  ? 15.380  82.643  5.410   1.00 44.29 ?  95   LYS E CE  1 
ATOM   9435  N  NZ  . LYS E  1 71  ? 15.151  83.866  6.237   1.00 44.67 ?  95   LYS E NZ  1 
ATOM   9436  N  N   . GLU E  1 72  ? 16.669  78.113  0.943   1.00 40.93 ?  96   GLU E N   1 
ATOM   9437  C  CA  . GLU E  1 72  ? 16.900  77.639  -0.420  1.00 41.21 ?  96   GLU E CA  1 
ATOM   9438  C  C   . GLU E  1 72  ? 15.615  77.164  -1.085  1.00 41.19 ?  96   GLU E C   1 
ATOM   9439  O  O   . GLU E  1 72  ? 14.704  76.666  -0.420  1.00 41.06 ?  96   GLU E O   1 
ATOM   9440  C  CB  . GLU E  1 72  ? 17.929  76.500  -0.426  1.00 41.40 ?  96   GLU E CB  1 
ATOM   9441  C  CG  . GLU E  1 72  ? 19.374  76.933  -0.186  1.00 42.18 ?  96   GLU E CG  1 
ATOM   9442  C  CD  . GLU E  1 72  ? 20.036  77.524  -1.421  1.00 43.60 ?  96   GLU E CD  1 
ATOM   9443  O  OE1 . GLU E  1 72  ? 19.611  77.196  -2.551  1.00 44.13 ?  96   GLU E OE1 1 
ATOM   9444  O  OE2 . GLU E  1 72  ? 20.994  78.311  -1.261  1.00 44.45 -1 96   GLU E OE2 1 
ATOM   9445  N  N   . VAL E  1 73  ? 15.556  77.336  -2.404  1.00 41.23 ?  97   VAL E N   1 
ATOM   9446  C  CA  . VAL E  1 73  ? 14.449  76.849  -3.219  1.00 41.38 ?  97   VAL E CA  1 
ATOM   9447  C  C   . VAL E  1 73  ? 15.060  75.972  -4.311  1.00 41.43 ?  97   VAL E C   1 
ATOM   9448  O  O   . VAL E  1 73  ? 15.778  76.462  -5.183  1.00 41.64 ?  97   VAL E O   1 
ATOM   9449  C  CB  . VAL E  1 73  ? 13.614  78.013  -3.826  1.00 41.45 ?  97   VAL E CB  1 
ATOM   9450  C  CG1 . VAL E  1 73  ? 12.430  77.476  -4.621  1.00 41.56 ?  97   VAL E CG1 1 
ATOM   9451  C  CG2 . VAL E  1 73  ? 13.119  78.958  -2.731  1.00 41.33 ?  97   VAL E CG2 1 
ATOM   9452  N  N   . ALA E  1 74  ? 14.779  74.672  -4.253  1.00 41.27 ?  98   ALA E N   1 
ATOM   9453  C  CA  . ALA E  1 74  ? 15.567  73.692  -4.996  1.00 41.07 ?  98   ALA E CA  1 
ATOM   9454  C  C   . ALA E  1 74  ? 14.759  72.756  -5.891  1.00 40.95 ?  98   ALA E C   1 
ATOM   9455  O  O   . ALA E  1 74  ? 13.642  72.359  -5.550  1.00 40.99 ?  98   ALA E O   1 
ATOM   9456  C  CB  . ALA E  1 74  ? 16.421  72.882  -4.025  1.00 41.00 ?  98   ALA E CB  1 
ATOM   9457  N  N   . GLU E  1 75  ? 15.351  72.405  -7.032  1.00 40.80 ?  99   GLU E N   1 
ATOM   9458  C  CA  . GLU E  1 75  ? 14.823  71.369  -7.920  1.00 40.75 ?  99   GLU E CA  1 
ATOM   9459  C  C   . GLU E  1 75  ? 15.269  69.981  -7.456  1.00 40.26 ?  99   GLU E C   1 
ATOM   9460  O  O   . GLU E  1 75  ? 16.159  69.856  -6.611  1.00 40.13 ?  99   GLU E O   1 
ATOM   9461  C  CB  . GLU E  1 75  ? 15.308  71.591  -9.355  1.00 40.97 ?  99   GLU E CB  1 
ATOM   9462  C  CG  . GLU E  1 75  ? 14.433  72.499  -10.203 1.00 42.33 ?  99   GLU E CG  1 
ATOM   9463  C  CD  . GLU E  1 75  ? 15.087  72.848  -11.530 1.00 44.39 ?  99   GLU E CD  1 
ATOM   9464  O  OE1 . GLU E  1 75  ? 14.510  72.515  -12.589 1.00 45.03 ?  99   GLU E OE1 1 
ATOM   9465  O  OE2 . GLU E  1 75  ? 16.188  73.448  -11.516 1.00 45.60 -1 99   GLU E OE2 1 
ATOM   9466  N  N   . ARG E  1 76  ? 14.646  68.953  -8.033  1.00 39.64 ?  100  ARG E N   1 
ATOM   9467  C  CA  . ARG E  1 76  ? 14.991  67.551  -7.798  1.00 39.13 ?  100  ARG E CA  1 
ATOM   9468  C  C   . ARG E  1 76  ? 16.502  67.297  -7.869  1.00 38.89 ?  100  ARG E C   1 
ATOM   9469  O  O   . ARG E  1 76  ? 17.074  66.656  -6.982  1.00 38.96 ?  100  ARG E O   1 
ATOM   9470  C  CB  . ARG E  1 76  ? 14.242  66.670  -8.806  1.00 39.15 ?  100  ARG E CB  1 
ATOM   9471  C  CG  . ARG E  1 76  ? 14.620  65.193  -8.808  1.00 38.77 ?  100  ARG E CG  1 
ATOM   9472  C  CD  . ARG E  1 76  ? 13.815  64.422  -9.853  1.00 38.11 ?  100  ARG E CD  1 
ATOM   9473  N  NE  . ARG E  1 76  ? 12.381  64.419  -9.564  1.00 37.45 ?  100  ARG E NE  1 
ATOM   9474  C  CZ  . ARG E  1 76  ? 11.771  63.547  -8.763  1.00 37.63 ?  100  ARG E CZ  1 
ATOM   9475  N  NH1 . ARG E  1 76  ? 12.466  62.589  -8.157  1.00 36.62 ?  100  ARG E NH1 1 
ATOM   9476  N  NH2 . ARG E  1 76  ? 10.459  63.632  -8.566  1.00 37.09 ?  100  ARG E NH2 1 
ATOM   9477  N  N   . LYS E  1 77  ? 17.137  67.816  -8.917  1.00 38.42 ?  101  LYS E N   1 
ATOM   9478  C  CA  . LYS E  1 77  ? 18.580  67.670  -9.120  1.00 38.09 ?  101  LYS E CA  1 
ATOM   9479  C  C   . LYS E  1 77  ? 19.432  68.432  -8.095  1.00 37.73 ?  101  LYS E C   1 
ATOM   9480  O  O   . LYS E  1 77  ? 20.567  68.038  -7.818  1.00 37.60 ?  101  LYS E O   1 
ATOM   9481  C  CB  . LYS E  1 77  ? 18.970  68.085  -10.545 1.00 38.15 ?  101  LYS E CB  1 
ATOM   9482  C  CG  . LYS E  1 77  ? 18.609  69.522  -10.919 1.00 38.14 ?  101  LYS E CG  1 
ATOM   9483  C  CD  . LYS E  1 77  ? 19.115  69.872  -12.310 1.00 38.46 ?  101  LYS E CD  1 
ATOM   9484  C  CE  . LYS E  1 77  ? 18.501  71.169  -12.825 1.00 38.63 ?  101  LYS E CE  1 
ATOM   9485  N  NZ  . LYS E  1 77  ? 18.928  72.368  -12.050 1.00 39.15 ?  101  LYS E NZ  1 
ATOM   9486  N  N   . ASP E  1 78  ? 18.883  69.516  -7.546  1.00 37.28 ?  102  ASP E N   1 
ATOM   9487  C  CA  . ASP E  1 78  ? 19.610  70.354  -6.590  1.00 36.96 ?  102  ASP E CA  1 
ATOM   9488  C  C   . ASP E  1 78  ? 19.788  69.676  -5.235  1.00 36.81 ?  102  ASP E C   1 
ATOM   9489  O  O   . ASP E  1 78  ? 20.797  69.896  -4.560  1.00 36.72 ?  102  ASP E O   1 
ATOM   9490  C  CB  . ASP E  1 78  ? 18.917  71.709  -6.403  1.00 36.90 ?  102  ASP E CB  1 
ATOM   9491  C  CG  . ASP E  1 78  ? 18.879  72.531  -7.674  1.00 36.54 ?  102  ASP E CG  1 
ATOM   9492  O  OD1 . ASP E  1 78  ? 19.862  72.501  -8.447  1.00 36.77 ?  102  ASP E OD1 1 
ATOM   9493  O  OD2 . ASP E  1 78  ? 17.865  73.222  -7.892  1.00 36.01 -1 102  ASP E OD2 1 
ATOM   9494  N  N   . CYS E  1 79  ? 18.808  68.858  -4.846  1.00 36.66 ?  103  CYS E N   1 
ATOM   9495  C  CA  . CYS E  1 79  ? 18.878  68.089  -3.597  1.00 36.59 ?  103  CYS E CA  1 
ATOM   9496  C  C   . CYS E  1 79  ? 20.144  67.245  -3.572  1.00 36.61 ?  103  CYS E C   1 
ATOM   9497  O  O   . CYS E  1 79  ? 20.872  67.230  -2.579  1.00 36.73 ?  103  CYS E O   1 
ATOM   9498  C  CB  . CYS E  1 79  ? 17.661  67.172  -3.446  1.00 36.48 ?  103  CYS E CB  1 
ATOM   9499  S  SG  . CYS E  1 79  ? 16.055  67.917  -3.803  1.00 35.59 ?  103  CYS E SG  1 
ATOM   9500  N  N   . VAL E  1 80  ? 20.399  66.562  -4.685  1.00 36.69 ?  104  VAL E N   1 
ATOM   9501  C  CA  . VAL E  1 80  ? 21.541  65.666  -4.838  1.00 36.96 ?  104  VAL E CA  1 
ATOM   9502  C  C   . VAL E  1 80  ? 22.870  66.433  -4.835  1.00 37.07 ?  104  VAL E C   1 
ATOM   9503  O  O   . VAL E  1 80  ? 23.788  66.090  -4.088  1.00 37.15 ?  104  VAL E O   1 
ATOM   9504  C  CB  . VAL E  1 80  ? 21.407  64.811  -6.136  1.00 36.91 ?  104  VAL E CB  1 
ATOM   9505  C  CG1 . VAL E  1 80  ? 22.608  63.892  -6.323  1.00 37.10 ?  104  VAL E CG1 1 
ATOM   9506  C  CG2 . VAL E  1 80  ? 20.108  64.000  -6.120  1.00 36.81 ?  104  VAL E CG2 1 
ATOM   9507  N  N   . GLU E  1 81  ? 22.948  67.476  -5.659  1.00 37.20 ?  105  GLU E N   1 
ATOM   9508  C  CA  . GLU E  1 81  ? 24.181  68.232  -5.883  1.00 37.39 ?  105  GLU E CA  1 
ATOM   9509  C  C   . GLU E  1 81  ? 24.735  68.859  -4.604  1.00 37.11 ?  105  GLU E C   1 
ATOM   9510  O  O   . GLU E  1 81  ? 25.924  68.727  -4.299  1.00 37.22 ?  105  GLU E O   1 
ATOM   9511  C  CB  . GLU E  1 81  ? 23.945  69.313  -6.947  1.00 37.69 ?  105  GLU E CB  1 
ATOM   9512  C  CG  . GLU E  1 81  ? 25.198  70.065  -7.396  1.00 39.08 ?  105  GLU E CG  1 
ATOM   9513  C  CD  . GLU E  1 81  ? 26.021  69.295  -8.418  1.00 40.60 ?  105  GLU E CD  1 
ATOM   9514  O  OE1 . GLU E  1 81  ? 26.212  69.818  -9.534  1.00 40.75 ?  105  GLU E OE1 1 
ATOM   9515  O  OE2 . GLU E  1 81  ? 26.475  68.170  -8.114  1.00 42.09 -1 105  GLU E OE2 1 
ATOM   9516  N  N   . CYS E  1 82  ? 23.864  69.534  -3.861  1.00 36.69 ?  106  CYS E N   1 
ATOM   9517  C  CA  . CYS E  1 82  ? 24.258  70.246  -2.651  1.00 36.20 ?  106  CYS E CA  1 
ATOM   9518  C  C   . CYS E  1 82  ? 24.535  69.317  -1.470  1.00 35.73 ?  106  CYS E C   1 
ATOM   9519  O  O   . CYS E  1 82  ? 25.494  69.521  -0.723  1.00 35.62 ?  106  CYS E O   1 
ATOM   9520  C  CB  . CYS E  1 82  ? 23.186  71.263  -2.280  1.00 36.18 ?  106  CYS E CB  1 
ATOM   9521  S  SG  . CYS E  1 82  ? 23.561  72.243  -0.829  1.00 36.64 ?  106  CYS E SG  1 
ATOM   9522  N  N   . HIS E  1 83  ? 23.697  68.299  -1.305  1.00 35.27 ?  107  HIS E N   1 
ATOM   9523  C  CA  . HIS E  1 83  ? 23.883  67.332  -0.225  1.00 34.86 ?  107  HIS E CA  1 
ATOM   9524  C  C   . HIS E  1 83  ? 25.064  66.385  -0.470  1.00 34.69 ?  107  HIS E C   1 
ATOM   9525  O  O   . HIS E  1 83  ? 25.514  65.705  0.452   1.00 34.49 ?  107  HIS E O   1 
ATOM   9526  C  CB  . HIS E  1 83  ? 22.586  66.562  0.056   1.00 34.68 ?  107  HIS E CB  1 
ATOM   9527  C  CG  . HIS E  1 83  ? 21.588  67.336  0.867   1.00 34.24 ?  107  HIS E CG  1 
ATOM   9528  N  ND1 . HIS E  1 83  ? 21.484  67.205  2.234   1.00 33.39 ?  107  HIS E ND1 1 
ATOM   9529  C  CD2 . HIS E  1 83  ? 20.654  68.251  0.506   1.00 33.87 ?  107  HIS E CD2 1 
ATOM   9530  C  CE1 . HIS E  1 83  ? 20.533  68.006  2.681   1.00 33.71 ?  107  HIS E CE1 1 
ATOM   9531  N  NE2 . HIS E  1 83  ? 20.012  68.653  1.654   1.00 33.40 ?  107  HIS E NE2 1 
ATOM   9532  N  N   . SER E  1 84  ? 25.578  66.369  -1.701  1.00 34.65 ?  108  SER E N   1 
ATOM   9533  C  CA  . SER E  1 84  ? 26.724  65.527  -2.070  1.00 34.69 ?  108  SER E CA  1 
ATOM   9534  C  C   . SER E  1 84  ? 27.977  65.804  -1.233  1.00 34.40 ?  108  SER E C   1 
ATOM   9535  O  O   . SER E  1 84  ? 28.874  64.966  -1.165  1.00 34.60 ?  108  SER E O   1 
ATOM   9536  C  CB  . SER E  1 84  ? 27.049  65.651  -3.564  1.00 34.82 ?  108  SER E CB  1 
ATOM   9537  O  OG  . SER E  1 84  ? 27.817  66.816  -3.822  1.00 35.63 ?  108  SER E OG  1 
ATOM   9538  N  N   . ASP E  1 85  ? 28.042  66.976  -0.607  1.00 34.26 ?  109  ASP E N   1 
ATOM   9539  C  CA  . ASP E  1 85  ? 29.075  67.233  0.400   1.00 34.00 ?  109  ASP E CA  1 
ATOM   9540  C  C   . ASP E  1 85  ? 28.505  67.718  1.736   1.00 33.43 ?  109  ASP E C   1 
ATOM   9541  O  O   . ASP E  1 85  ? 29.192  67.665  2.763   1.00 33.47 ?  109  ASP E O   1 
ATOM   9542  C  CB  . ASP E  1 85  ? 30.163  68.175  -0.128  1.00 34.34 ?  109  ASP E CB  1 
ATOM   9543  C  CG  . ASP E  1 85  ? 29.663  69.581  -0.359  1.00 35.19 ?  109  ASP E CG  1 
ATOM   9544  O  OD1 . ASP E  1 85  ? 30.475  70.516  -0.203  1.00 36.51 ?  109  ASP E OD1 1 
ATOM   9545  O  OD2 . ASP E  1 85  ? 28.471  69.754  -0.699  1.00 36.22 -1 109  ASP E OD2 1 
ATOM   9546  N  N   . GLU E  1 86  ? 27.253  68.174  1.722   1.00 32.65 ?  110  GLU E N   1 
ATOM   9547  C  CA  . GLU E  1 86  ? 26.554  68.526  2.960   1.00 32.05 ?  110  GLU E CA  1 
ATOM   9548  C  C   . GLU E  1 86  ? 26.259  67.285  3.811   1.00 31.48 ?  110  GLU E C   1 
ATOM   9549  O  O   . GLU E  1 86  ? 26.522  67.271  5.017   1.00 31.45 ?  110  GLU E O   1 
ATOM   9550  C  CB  . GLU E  1 86  ? 25.257  69.286  2.668   1.00 32.15 ?  110  GLU E CB  1 
ATOM   9551  C  CG  . GLU E  1 86  ? 24.644  69.925  3.908   1.00 32.04 ?  110  GLU E CG  1 
ATOM   9552  C  CD  . GLU E  1 86  ? 25.540  70.995  4.514   1.00 32.67 ?  110  GLU E CD  1 
ATOM   9553  O  OE1 . GLU E  1 86  ? 25.698  71.012  5.755   1.00 32.34 ?  110  GLU E OE1 1 
ATOM   9554  O  OE2 . GLU E  1 86  ? 26.082  71.820  3.745   1.00 32.56 -1 110  GLU E OE2 1 
ATOM   9555  N  N   . THR E  1 87  ? 25.703  66.260  3.169   1.00 30.67 ?  111  THR E N   1 
ATOM   9556  C  CA  . THR E  1 87  ? 25.489  64.951  3.786   1.00 29.97 ?  111  THR E CA  1 
ATOM   9557  C  C   . THR E  1 87  ? 25.919  63.864  2.786   1.00 29.67 ?  111  THR E C   1 
ATOM   9558  O  O   . THR E  1 87  ? 25.070  63.158  2.235   1.00 29.48 ?  111  THR E O   1 
ATOM   9559  C  CB  . THR E  1 87  ? 24.008  64.742  4.192   1.00 30.05 ?  111  THR E CB  1 
ATOM   9560  O  OG1 . THR E  1 87  ? 23.166  64.887  3.039   1.00 29.66 ?  111  THR E OG1 1 
ATOM   9561  C  CG2 . THR E  1 87  ? 23.580  65.740  5.275   1.00 29.38 ?  111  THR E CG2 1 
ATOM   9562  N  N   . PRO E  1 88  ? 27.242  63.737  2.546   1.00 29.32 ?  112  PRO E N   1 
ATOM   9563  C  CA  . PRO E  1 88  ? 27.791  62.969  1.413   1.00 29.10 ?  112  PRO E CA  1 
ATOM   9564  C  C   . PRO E  1 88  ? 27.310  61.524  1.318   1.00 28.88 ?  112  PRO E C   1 
ATOM   9565  O  O   . PRO E  1 88  ? 26.907  61.081  0.241   1.00 28.91 ?  112  PRO E O   1 
ATOM   9566  C  CB  . PRO E  1 88  ? 29.305  62.999  1.659   1.00 29.11 ?  112  PRO E CB  1 
ATOM   9567  C  CG  . PRO E  1 88  ? 29.535  64.159  2.549   1.00 29.20 ?  112  PRO E CG  1 
ATOM   9568  C  CD  . PRO E  1 88  ? 28.311  64.297  3.394   1.00 29.28 ?  112  PRO E CD  1 
ATOM   9569  N  N   . VAL E  1 89  ? 27.355  60.803  2.435   1.00 28.69 ?  113  VAL E N   1 
ATOM   9570  C  CA  . VAL E  1 89  ? 27.027  59.377  2.454   1.00 28.39 ?  113  VAL E CA  1 
ATOM   9571  C  C   . VAL E  1 89  ? 25.549  59.112  2.154   1.00 28.05 ?  113  VAL E C   1 
ATOM   9572  O  O   . VAL E  1 89  ? 25.224  58.119  1.509   1.00 27.80 ?  113  VAL E O   1 
ATOM   9573  C  CB  . VAL E  1 89  ? 27.488  58.703  3.772   1.00 28.40 ?  113  VAL E CB  1 
ATOM   9574  C  CG1 . VAL E  1 89  ? 26.947  57.284  3.900   1.00 28.46 ?  113  VAL E CG1 1 
ATOM   9575  C  CG2 . VAL E  1 89  ? 29.010  58.689  3.843   1.00 28.67 ?  113  VAL E CG2 1 
ATOM   9576  N  N   . TRP E  1 90  ? 24.665  60.003  2.598   1.00 27.99 ?  114  TRP E N   1 
ATOM   9577  C  CA  . TRP E  1 90  ? 23.249  59.902  2.236   1.00 28.15 ?  114  TRP E CA  1 
ATOM   9578  C  C   . TRP E  1 90  ? 23.079  59.872  0.716   1.00 28.19 ?  114  TRP E C   1 
ATOM   9579  O  O   . TRP E  1 90  ? 22.334  59.050  0.192   1.00 28.13 ?  114  TRP E O   1 
ATOM   9580  C  CB  . TRP E  1 90  ? 22.418  61.036  2.842   1.00 28.01 ?  114  TRP E CB  1 
ATOM   9581  C  CG  . TRP E  1 90  ? 22.084  60.904  4.319   1.00 28.21 ?  114  TRP E CG  1 
ATOM   9582  C  CD1 . TRP E  1 90  ? 21.418  61.822  5.080   1.00 28.34 ?  114  TRP E CD1 1 
ATOM   9583  C  CD2 . TRP E  1 90  ? 22.405  59.812  5.204   1.00 28.41 ?  114  TRP E CD2 1 
ATOM   9584  N  NE1 . TRP E  1 90  ? 21.296  61.373  6.373   1.00 28.64 ?  114  TRP E NE1 1 
ATOM   9585  C  CE2 . TRP E  1 90  ? 21.891  60.143  6.477   1.00 28.36 ?  114  TRP E CE2 1 
ATOM   9586  C  CE3 . TRP E  1 90  ? 23.069  58.586  5.043   1.00 28.23 ?  114  TRP E CE3 1 
ATOM   9587  C  CZ2 . TRP E  1 90  ? 22.022  59.296  7.584   1.00 28.39 ?  114  TRP E CZ2 1 
ATOM   9588  C  CZ3 . TRP E  1 90  ? 23.200  57.744  6.149   1.00 28.70 ?  114  TRP E CZ3 1 
ATOM   9589  C  CH2 . TRP E  1 90  ? 22.678  58.106  7.400   1.00 28.10 ?  114  TRP E CH2 1 
ATOM   9590  N  N   . VAL E  1 91  ? 23.794  60.756  0.022   1.00 28.30 ?  115  VAL E N   1 
ATOM   9591  C  CA  . VAL E  1 91  ? 23.779  60.804  -1.445  1.00 28.51 ?  115  VAL E CA  1 
ATOM   9592  C  C   . VAL E  1 91  ? 24.376  59.533  -2.064  1.00 28.64 ?  115  VAL E C   1 
ATOM   9593  O  O   . VAL E  1 91  ? 23.787  58.955  -2.982  1.00 28.55 ?  115  VAL E O   1 
ATOM   9594  C  CB  . VAL E  1 91  ? 24.483  62.085  -1.981  1.00 28.44 ?  115  VAL E CB  1 
ATOM   9595  C  CG1 . VAL E  1 91  ? 24.753  61.997  -3.486  1.00 28.75 ?  115  VAL E CG1 1 
ATOM   9596  C  CG2 . VAL E  1 91  ? 23.648  63.315  -1.665  1.00 28.07 ?  115  VAL E CG2 1 
ATOM   9597  N  N   . ARG E  1 92  ? 25.529  59.100  -1.550  1.00 28.70 ?  116  ARG E N   1 
ATOM   9598  C  CA  . ARG E  1 92  ? 26.193  57.892  -2.050  1.00 29.15 ?  116  ARG E CA  1 
ATOM   9599  C  C   . ARG E  1 92  ? 25.371  56.627  -1.790  1.00 29.18 ?  116  ARG E C   1 
ATOM   9600  O  O   . ARG E  1 92  ? 25.214  55.801  -2.686  1.00 29.20 ?  116  ARG E O   1 
ATOM   9601  C  CB  . ARG E  1 92  ? 27.616  57.756  -1.483  1.00 29.23 ?  116  ARG E CB  1 
ATOM   9602  C  CG  . ARG E  1 92  ? 28.588  58.801  -2.014  1.00 30.27 ?  116  ARG E CG  1 
ATOM   9603  C  CD  . ARG E  1 92  ? 30.010  58.580  -1.519  1.00 32.17 ?  116  ARG E CD  1 
ATOM   9604  N  NE  . ARG E  1 92  ? 30.882  59.712  -1.844  1.00 33.60 ?  116  ARG E NE  1 
ATOM   9605  C  CZ  . ARG E  1 92  ? 31.437  60.526  -0.946  1.00 34.63 ?  116  ARG E CZ  1 
ATOM   9606  N  NH1 . ARG E  1 92  ? 31.236  60.335  0.356   1.00 35.12 ?  116  ARG E NH1 1 
ATOM   9607  N  NH2 . ARG E  1 92  ? 32.208  61.530  -1.350  1.00 35.13 ?  116  ARG E NH2 1 
ATOM   9608  N  N   . ALA E  1 93  ? 24.843  56.489  -0.572  1.00 29.28 ?  117  ALA E N   1 
ATOM   9609  C  CA  . ALA E  1 93  ? 23.984  55.357  -0.212  1.00 29.48 ?  117  ALA E CA  1 
ATOM   9610  C  C   . ALA E  1 93  ? 22.702  55.328  -1.045  1.00 29.71 ?  117  ALA E C   1 
ATOM   9611  O  O   . ALA E  1 93  ? 22.273  54.262  -1.491  1.00 29.50 ?  117  ALA E O   1 
ATOM   9612  C  CB  . ALA E  1 93  ? 23.655  55.375  1.277   1.00 29.35 ?  117  ALA E CB  1 
ATOM   9613  N  N   . TRP E  1 94  ? 22.101  56.498  -1.253  1.00 30.03 ?  118  TRP E N   1 
ATOM   9614  C  CA  . TRP E  1 94  ? 20.916  56.612  -2.106  1.00 30.52 ?  118  TRP E CA  1 
ATOM   9615  C  C   . TRP E  1 94  ? 21.226  56.227  -3.557  1.00 30.68 ?  118  TRP E C   1 
ATOM   9616  O  O   . TRP E  1 94  ? 20.465  55.484  -4.182  1.00 30.61 ?  118  TRP E O   1 
ATOM   9617  C  CB  . TRP E  1 94  ? 20.314  58.020  -2.040  1.00 30.48 ?  118  TRP E CB  1 
ATOM   9618  C  CG  . TRP E  1 94  ? 19.283  58.261  -3.104  1.00 31.29 ?  118  TRP E CG  1 
ATOM   9619  C  CD1 . TRP E  1 94  ? 17.974  57.882  -3.075  1.00 31.68 ?  118  TRP E CD1 1 
ATOM   9620  C  CD2 . TRP E  1 94  ? 19.485  58.914  -4.365  1.00 32.10 ?  118  TRP E CD2 1 
ATOM   9621  N  NE1 . TRP E  1 94  ? 17.344  58.262  -4.236  1.00 32.48 ?  118  TRP E NE1 1 
ATOM   9622  C  CE2 . TRP E  1 94  ? 18.247  58.899  -5.046  1.00 32.38 ?  118  TRP E CE2 1 
ATOM   9623  C  CE3 . TRP E  1 94  ? 20.593  59.514  -4.984  1.00 32.21 ?  118  TRP E CE3 1 
ATOM   9624  C  CZ2 . TRP E  1 94  ? 18.080  59.462  -6.317  1.00 32.52 ?  118  TRP E CZ2 1 
ATOM   9625  C  CZ3 . TRP E  1 94  ? 20.429  60.075  -6.253  1.00 32.87 ?  118  TRP E CZ3 1 
ATOM   9626  C  CH2 . TRP E  1 94  ? 19.179  60.044  -6.903  1.00 32.82 ?  118  TRP E CH2 1 
ATOM   9627  N  N   . LYS E  1 95  ? 22.345  56.732  -4.077  1.00 31.00 ?  119  LYS E N   1 
ATOM   9628  C  CA  . LYS E  1 95  ? 22.789  56.440  -5.445  1.00 31.43 ?  119  LYS E CA  1 
ATOM   9629  C  C   . LYS E  1 95  ? 23.035  54.944  -5.667  1.00 31.35 ?  119  LYS E C   1 
ATOM   9630  O  O   . LYS E  1 95  ? 22.817  54.436  -6.765  1.00 31.52 ?  119  LYS E O   1 
ATOM   9631  C  CB  . LYS E  1 95  ? 24.042  57.259  -5.792  1.00 31.50 ?  119  LYS E CB  1 
ATOM   9632  C  CG  . LYS E  1 95  ? 24.360  57.322  -7.281  1.00 32.91 ?  119  LYS E CG  1 
ATOM   9633  C  CD  . LYS E  1 95  ? 25.423  58.368  -7.599  1.00 34.87 ?  119  LYS E CD  1 
ATOM   9634  C  CE  . LYS E  1 95  ? 25.716  58.412  -9.099  1.00 36.23 ?  119  LYS E CE  1 
ATOM   9635  N  NZ  . LYS E  1 95  ? 26.504  59.622  -9.487  1.00 37.17 ?  119  LYS E NZ  1 
ATOM   9636  N  N   . ARG E  1 96  ? 23.485  54.253  -4.620  1.00 31.53 ?  120  ARG E N   1 
ATOM   9637  C  CA  . ARG E  1 96  ? 23.659  52.794  -4.638  1.00 31.69 ?  120  ARG E CA  1 
ATOM   9638  C  C   . ARG E  1 96  ? 22.325  52.047  -4.625  1.00 31.31 ?  120  ARG E C   1 
ATOM   9639  O  O   . ARG E  1 96  ? 22.249  50.914  -5.098  1.00 31.23 ?  120  ARG E O   1 
ATOM   9640  C  CB  . ARG E  1 96  ? 24.479  52.311  -3.429  1.00 31.90 ?  120  ARG E CB  1 
ATOM   9641  C  CG  . ARG E  1 96  ? 25.868  52.907  -3.278  1.00 33.51 ?  120  ARG E CG  1 
ATOM   9642  C  CD  . ARG E  1 96  ? 26.648  52.214  -2.158  1.00 36.17 ?  120  ARG E CD  1 
ATOM   9643  N  NE  . ARG E  1 96  ? 27.375  53.156  -1.299  1.00 38.32 ?  120  ARG E NE  1 
ATOM   9644  C  CZ  . ARG E  1 96  ? 28.510  53.774  -1.624  1.00 39.40 ?  120  ARG E CZ  1 
ATOM   9645  N  NH1 . ARG E  1 96  ? 29.082  53.577  -2.810  1.00 40.40 ?  120  ARG E NH1 1 
ATOM   9646  N  NH2 . ARG E  1 96  ? 29.075  54.604  -0.759  1.00 40.44 ?  120  ARG E NH2 1 
ATOM   9647  N  N   . SER E  1 97  ? 21.288  52.676  -4.069  1.00 30.91 ?  121  SER E N   1 
ATOM   9648  C  CA  . SER E  1 97  ? 20.029  51.986  -3.762  1.00 30.60 ?  121  SER E CA  1 
ATOM   9649  C  C   . SER E  1 97  ? 19.111  51.748  -4.963  1.00 30.42 ?  121  SER E C   1 
ATOM   9650  O  O   . SER E  1 97  ? 19.182  52.454  -5.972  1.00 30.34 ?  121  SER E O   1 
ATOM   9651  C  CB  . SER E  1 97  ? 19.258  52.724  -2.656  1.00 30.56 ?  121  SER E CB  1 
ATOM   9652  O  OG  . SER E  1 97  ? 18.567  53.855  -3.157  1.00 30.01 ?  121  SER E OG  1 
ATOM   9653  N  N   . THR E  1 98  ? 18.243  50.747  -4.821  1.00 30.15 ?  122  THR E N   1 
ATOM   9654  C  CA  . THR E  1 98  ? 17.210  50.428  -5.807  1.00 29.78 ?  122  THR E CA  1 
ATOM   9655  C  C   . THR E  1 98  ? 16.354  51.656  -6.154  1.00 29.61 ?  122  THR E C   1 
ATOM   9656  O  O   . THR E  1 98  ? 16.043  51.892  -7.324  1.00 29.52 ?  122  THR E O   1 
ATOM   9657  C  CB  . THR E  1 98  ? 16.334  49.247  -5.313  1.00 29.80 ?  122  THR E CB  1 
ATOM   9658  O  OG1 . THR E  1 98  ? 17.129  48.054  -5.282  1.00 29.46 ?  122  THR E OG1 1 
ATOM   9659  C  CG2 . THR E  1 98  ? 15.134  49.013  -6.222  1.00 29.70 ?  122  THR E CG2 1 
ATOM   9660  N  N   . HIS E  1 99  ? 16.006  52.438  -5.134  1.00 29.37 ?  123  HIS E N   1 
ATOM   9661  C  CA  . HIS E  1 99  ? 15.241  53.673  -5.304  1.00 29.17 ?  123  HIS E CA  1 
ATOM   9662  C  C   . HIS E  1 99  ? 15.823  54.607  -6.378  1.00 29.24 ?  123  HIS E C   1 
ATOM   9663  O  O   . HIS E  1 99  ? 15.074  55.265  -7.101  1.00 29.05 ?  123  HIS E O   1 
ATOM   9664  C  CB  . HIS E  1 99  ? 15.095  54.408  -3.963  1.00 29.16 ?  123  HIS E CB  1 
ATOM   9665  C  CG  . HIS E  1 99  ? 14.078  53.801  -3.039  1.00 28.76 ?  123  HIS E CG  1 
ATOM   9666  N  ND1 . HIS E  1 99  ? 14.288  53.670  -1.683  1.00 28.20 ?  123  HIS E ND1 1 
ATOM   9667  C  CD2 . HIS E  1 99  ? 12.844  53.292  -3.276  1.00 28.18 ?  123  HIS E CD2 1 
ATOM   9668  C  CE1 . HIS E  1 99  ? 13.227  53.111  -1.124  1.00 27.86 ?  123  HIS E CE1 1 
ATOM   9669  N  NE2 . HIS E  1 99  ? 12.336  52.868  -2.070  1.00 27.48 ?  123  HIS E NE2 1 
ATOM   9670  N  N   . ALA E  1 100 ? 17.152  54.641  -6.489  1.00 29.16 ?  124  ALA E N   1 
ATOM   9671  C  CA  . ALA E  1 100 ? 17.837  55.463  -7.492  1.00 29.36 ?  124  ALA E CA  1 
ATOM   9672  C  C   . ALA E  1 100 ? 18.092  54.747  -8.826  1.00 29.55 ?  124  ALA E C   1 
ATOM   9673  O  O   . ALA E  1 100 ? 18.585  55.363  -9.778  1.00 29.46 ?  124  ALA E O   1 
ATOM   9674  C  CB  . ALA E  1 100 ? 19.148  55.992  -6.931  1.00 29.12 ?  124  ALA E CB  1 
ATOM   9675  N  N   . ASN E  1 101 ? 17.759  53.457  -8.889  1.00 29.76 ?  125  ASN E N   1 
ATOM   9676  C  CA  . ASN E  1 101 ? 18.108  52.616  -10.037 1.00 30.06 ?  125  ASN E CA  1 
ATOM   9677  C  C   . ASN E  1 101 ? 16.929  51.797  -10.569 1.00 30.22 ?  125  ASN E C   1 
ATOM   9678  O  O   . ASN E  1 101 ? 17.059  50.599  -10.820 1.00 30.00 ?  125  ASN E O   1 
ATOM   9679  C  CB  . ASN E  1 101 ? 19.276  51.691  -9.672  1.00 30.08 ?  125  ASN E CB  1 
ATOM   9680  C  CG  . ASN E  1 101 ? 20.569  52.447  -9.430  1.00 30.67 ?  125  ASN E CG  1 
ATOM   9681  O  OD1 . ASN E  1 101 ? 21.275  52.810  -10.372 1.00 31.17 ?  125  ASN E OD1 1 
ATOM   9682  N  ND2 . ASN E  1 101 ? 20.893  52.680  -8.161  1.00 30.75 ?  125  ASN E ND2 1 
ATOM   9683  N  N   . LEU E  1 102 ? 15.787  52.457  -10.759 1.00 30.78 ?  126  LEU E N   1 
ATOM   9684  C  CA  . LEU E  1 102 ? 14.545  51.776  -11.149 1.00 31.20 ?  126  LEU E CA  1 
ATOM   9685  C  C   . LEU E  1 102 ? 14.581  51.143  -12.543 1.00 31.72 ?  126  LEU E C   1 
ATOM   9686  O  O   . LEU E  1 102 ? 13.896  50.150  -12.791 1.00 31.55 ?  126  LEU E O   1 
ATOM   9687  C  CB  . LEU E  1 102 ? 13.338  52.712  -11.016 1.00 31.05 ?  126  LEU E CB  1 
ATOM   9688  C  CG  . LEU E  1 102 ? 12.907  53.157  -9.610  1.00 30.76 ?  126  LEU E CG  1 
ATOM   9689  C  CD1 . LEU E  1 102 ? 11.655  54.024  -9.684  1.00 30.31 ?  126  LEU E CD1 1 
ATOM   9690  C  CD2 . LEU E  1 102 ? 12.675  51.975  -8.671  1.00 29.84 ?  126  LEU E CD2 1 
ATOM   9691  N  N   . ASP E  1 103 ? 15.383  51.714  -13.443 1.00 32.53 ?  127  ASP E N   1 
ATOM   9692  C  CA  . ASP E  1 103 ? 15.515  51.183  -14.803 1.00 33.28 ?  127  ASP E CA  1 
ATOM   9693  C  C   . ASP E  1 103 ? 16.146  49.794  -14.807 1.00 33.38 ?  127  ASP E C   1 
ATOM   9694  O  O   . ASP E  1 103 ? 15.747  48.930  -15.586 1.00 33.44 ?  127  ASP E O   1 
ATOM   9695  C  CB  . ASP E  1 103 ? 16.305  52.145  -15.697 1.00 33.55 ?  127  ASP E CB  1 
ATOM   9696  C  CG  . ASP E  1 103 ? 15.468  53.320  -16.172 1.00 34.30 ?  127  ASP E CG  1 
ATOM   9697  O  OD1 . ASP E  1 103 ? 14.333  53.097  -16.648 1.00 35.14 ?  127  ASP E OD1 1 
ATOM   9698  O  OD2 . ASP E  1 103 ? 15.948  54.469  -16.079 1.00 36.11 -1 127  ASP E OD2 1 
ATOM   9699  N  N   . LYS E  1 104 ? 17.120  49.593  -13.920 1.00 33.71 ?  128  LYS E N   1 
ATOM   9700  C  CA  . LYS E  1 104 ? 17.772  48.298  -13.725 1.00 34.02 ?  128  LYS E CA  1 
ATOM   9701  C  C   . LYS E  1 104 ? 16.755  47.228  -13.298 1.00 34.12 ?  128  LYS E C   1 
ATOM   9702  O  O   . LYS E  1 104 ? 16.860  46.063  -13.695 1.00 34.22 ?  128  LYS E O   1 
ATOM   9703  C  CB  . LYS E  1 104 ? 18.896  48.440  -12.690 1.00 34.19 ?  128  LYS E CB  1 
ATOM   9704  C  CG  . LYS E  1 104 ? 19.677  47.170  -12.384 1.00 34.79 ?  128  LYS E CG  1 
ATOM   9705  C  CD  . LYS E  1 104 ? 20.677  47.408  -11.259 1.00 36.23 ?  128  LYS E CD  1 
ATOM   9706  C  CE  . LYS E  1 104 ? 21.192  46.095  -10.684 1.00 36.46 ?  128  LYS E CE  1 
ATOM   9707  N  NZ  . LYS E  1 104 ? 22.124  46.337  -9.546  1.00 37.04 ?  128  LYS E NZ  1 
ATOM   9708  N  N   . ILE E  1 105 ? 15.769  47.638  -12.504 1.00 34.17 ?  129  ILE E N   1 
ATOM   9709  C  CA  . ILE E  1 105 ? 14.682  46.754  -12.078 1.00 34.40 ?  129  ILE E CA  1 
ATOM   9710  C  C   . ILE E  1 105 ? 13.755  46.395  -13.251 1.00 34.66 ?  129  ILE E C   1 
ATOM   9711  O  O   . ILE E  1 105 ? 13.241  45.276  -13.320 1.00 34.68 ?  129  ILE E O   1 
ATOM   9712  C  CB  . ILE E  1 105 ? 13.888  47.371  -10.885 1.00 34.26 ?  129  ILE E CB  1 
ATOM   9713  C  CG1 . ILE E  1 105 ? 14.819  47.650  -9.691  1.00 34.14 ?  129  ILE E CG1 1 
ATOM   9714  C  CG2 . ILE E  1 105 ? 12.703  46.497  -10.476 1.00 33.73 ?  129  ILE E CG2 1 
ATOM   9715  C  CD1 . ILE E  1 105 ? 15.461  46.410  -9.046  1.00 33.15 ?  129  ILE E CD1 1 
ATOM   9716  N  N   . ARG E  1 106 ? 13.564  47.338  -14.174 1.00 35.12 ?  130  ARG E N   1 
ATOM   9717  C  CA  . ARG E  1 106 ? 12.756  47.107  -15.381 1.00 35.60 ?  130  ARG E CA  1 
ATOM   9718  C  C   . ARG E  1 106 ? 13.428  46.142  -16.352 1.00 36.03 ?  130  ARG E C   1 
ATOM   9719  O  O   . ARG E  1 106 ? 12.747  45.432  -17.095 1.00 36.17 ?  130  ARG E O   1 
ATOM   9720  C  CB  . ARG E  1 106 ? 12.452  48.422  -16.104 1.00 35.58 ?  130  ARG E CB  1 
ATOM   9721  C  CG  . ARG E  1 106 ? 11.484  49.310  -15.371 1.00 35.25 ?  130  ARG E CG  1 
ATOM   9722  C  CD  . ARG E  1 106 ? 10.997  50.477  -16.211 1.00 35.18 ?  130  ARG E CD  1 
ATOM   9723  N  NE  . ARG E  1 106 ? 10.109  51.323  -15.416 1.00 34.56 ?  130  ARG E NE  1 
ATOM   9724  C  CZ  . ARG E  1 106 ? 10.506  52.368  -14.694 1.00 34.54 ?  130  ARG E CZ  1 
ATOM   9725  N  NH1 . ARG E  1 106 ? 11.784  52.734  -14.676 1.00 33.82 ?  130  ARG E NH1 1 
ATOM   9726  N  NH2 . ARG E  1 106 ? 9.615   53.058  -13.995 1.00 34.36 ?  130  ARG E NH2 1 
ATOM   9727  N  N   . ASN E  1 107 ? 14.759  46.131  -16.343 1.00 36.35 ?  131  ASN E N   1 
ATOM   9728  C  CA  . ASN E  1 107 ? 15.545  45.281  -17.233 1.00 36.84 ?  131  ASN E CA  1 
ATOM   9729  C  C   . ASN E  1 107 ? 15.734  43.852  -16.731 1.00 36.91 ?  131  ASN E C   1 
ATOM   9730  O  O   . ASN E  1 107 ? 16.398  43.049  -17.390 1.00 36.91 ?  131  ASN E O   1 
ATOM   9731  C  CB  . ASN E  1 107 ? 16.917  45.911  -17.494 1.00 37.10 ?  131  ASN E CB  1 
ATOM   9732  C  CG  . ASN E  1 107 ? 16.899  46.916  -18.631 1.00 37.82 ?  131  ASN E CG  1 
ATOM   9733  O  OD1 . ASN E  1 107 ? 15.885  47.100  -19.310 1.00 38.99 ?  131  ASN E OD1 1 
ATOM   9734  N  ND2 . ASN E  1 107 ? 18.033  47.570  -18.850 1.00 38.68 ?  131  ASN E ND2 1 
ATOM   9735  N  N   . LEU E  1 108 ? 15.164  43.542  -15.566 1.00 37.00 ?  132  LEU E N   1 
ATOM   9736  C  CA  . LEU E  1 108 ? 15.323  42.217  -14.965 1.00 37.14 ?  132  LEU E CA  1 
ATOM   9737  C  C   . LEU E  1 108 ? 14.655  41.124  -15.795 1.00 37.34 ?  132  LEU E C   1 
ATOM   9738  O  O   . LEU E  1 108 ? 13.638  41.356  -16.451 1.00 37.14 ?  132  LEU E O   1 
ATOM   9739  C  CB  . LEU E  1 108 ? 14.821  42.196  -13.515 1.00 37.04 ?  132  LEU E CB  1 
ATOM   9740  C  CG  . LEU E  1 108 ? 15.654  42.959  -12.473 1.00 36.87 ?  132  LEU E CG  1 
ATOM   9741  C  CD1 . LEU E  1 108 ? 14.937  43.027  -11.127 1.00 36.43 ?  132  LEU E CD1 1 
ATOM   9742  C  CD2 . LEU E  1 108 ? 17.051  42.366  -12.310 1.00 36.38 ?  132  LEU E CD2 1 
ATOM   9743  N  N   . LYS E  1 109 ? 15.255  39.937  -15.768 1.00 37.66 ?  133  LYS E N   1 
ATOM   9744  C  CA  . LYS E  1 109 ? 14.785  38.802  -16.556 1.00 38.00 ?  133  LYS E CA  1 
ATOM   9745  C  C   . LYS E  1 109 ? 13.984  37.846  -15.679 1.00 37.95 ?  133  LYS E C   1 
ATOM   9746  O  O   . LYS E  1 109 ? 14.240  37.735  -14.482 1.00 37.87 ?  133  LYS E O   1 
ATOM   9747  C  CB  . LYS E  1 109 ? 15.971  38.091  -17.218 1.00 38.08 ?  133  LYS E CB  1 
ATOM   9748  C  CG  . LYS E  1 109 ? 16.658  38.932  -18.287 1.00 39.13 ?  133  LYS E CG  1 
ATOM   9749  C  CD  . LYS E  1 109 ? 18.173  38.843  -18.184 1.00 41.13 ?  133  LYS E CD  1 
ATOM   9750  C  CE  . LYS E  1 109 ? 18.835  40.059  -18.833 1.00 41.87 ?  133  LYS E CE  1 
ATOM   9751  N  NZ  . LYS E  1 109 ? 20.287  40.162  -18.497 1.00 42.52 ?  133  LYS E NZ  1 
ATOM   9752  N  N   . SER E  1 110 ? 13.016  37.164  -16.286 1.00 37.96 ?  134  SER E N   1 
ATOM   9753  C  CA  . SER E  1 110 ? 12.064  36.322  -15.558 1.00 37.98 ?  134  SER E CA  1 
ATOM   9754  C  C   . SER E  1 110 ? 12.702  35.109  -14.871 1.00 38.00 ?  134  SER E C   1 
ATOM   9755  O  O   . SER E  1 110 ? 12.080  34.487  -14.009 1.00 38.05 ?  134  SER E O   1 
ATOM   9756  C  CB  . SER E  1 110 ? 10.921  35.883  -16.486 1.00 38.12 ?  134  SER E CB  1 
ATOM   9757  O  OG  . SER E  1 110 ? 11.415  35.177  -17.612 1.00 37.97 ?  134  SER E OG  1 
ATOM   9758  N  N   . ASP E  1 111 ? 13.937  34.784  -15.250 1.00 37.90 ?  135  ASP E N   1 
ATOM   9759  C  CA  . ASP E  1 111 ? 14.684  33.692  -14.619 1.00 37.89 ?  135  ASP E CA  1 
ATOM   9760  C  C   . ASP E  1 111 ? 15.627  34.174  -13.505 1.00 37.48 ?  135  ASP E C   1 
ATOM   9761  O  O   . ASP E  1 111 ? 16.347  33.375  -12.901 1.00 37.49 ?  135  ASP E O   1 
ATOM   9762  C  CB  . ASP E  1 111 ? 15.450  32.868  -15.670 1.00 38.10 ?  135  ASP E CB  1 
ATOM   9763  C  CG  . ASP E  1 111 ? 16.421  33.707  -16.496 1.00 39.05 ?  135  ASP E CG  1 
ATOM   9764  O  OD1 . ASP E  1 111 ? 16.498  34.941  -16.298 1.00 39.90 ?  135  ASP E OD1 1 
ATOM   9765  O  OD2 . ASP E  1 111 ? 17.114  33.121  -17.356 1.00 40.83 -1 135  ASP E OD2 1 
ATOM   9766  N  N   . ASP E  1 112 ? 15.619  35.482  -13.251 1.00 36.87 ?  136  ASP E N   1 
ATOM   9767  C  CA  . ASP E  1 112 ? 16.366  36.075  -12.144 1.00 36.38 ?  136  ASP E CA  1 
ATOM   9768  C  C   . ASP E  1 112 ? 15.546  35.897  -10.862 1.00 35.97 ?  136  ASP E C   1 
ATOM   9769  O  O   . ASP E  1 112 ? 14.349  36.192  -10.853 1.00 36.01 ?  136  ASP E O   1 
ATOM   9770  C  CB  . ASP E  1 112 ? 16.617  37.565  -12.423 1.00 36.41 ?  136  ASP E CB  1 
ATOM   9771  C  CG  . ASP E  1 112 ? 17.686  38.176  -11.524 1.00 36.49 ?  136  ASP E CG  1 
ATOM   9772  O  OD1 . ASP E  1 112 ? 17.662  37.956  -10.294 1.00 36.17 ?  136  ASP E OD1 1 
ATOM   9773  O  OD2 . ASP E  1 112 ? 18.546  38.911  -12.055 1.00 36.89 -1 136  ASP E OD2 1 
ATOM   9774  N  N   . PRO E  1 113 ? 16.178  35.401  -9.777  1.00 35.45 ?  137  PRO E N   1 
ATOM   9775  C  CA  . PRO E  1 113 ? 15.464  35.290  -8.499  1.00 34.96 ?  137  PRO E CA  1 
ATOM   9776  C  C   . PRO E  1 113 ? 14.965  36.642  -7.975  1.00 34.34 ?  137  PRO E C   1 
ATOM   9777  O  O   . PRO E  1 113 ? 14.035  36.687  -7.169  1.00 34.38 ?  137  PRO E O   1 
ATOM   9778  C  CB  . PRO E  1 113 ? 16.516  34.697  -7.552  1.00 34.97 ?  137  PRO E CB  1 
ATOM   9779  C  CG  . PRO E  1 113 ? 17.836  34.909  -8.235  1.00 35.39 ?  137  PRO E CG  1 
ATOM   9780  C  CD  . PRO E  1 113 ? 17.533  34.826  -9.694  1.00 35.55 ?  137  PRO E CD  1 
ATOM   9781  N  N   . LEU E  1 114 ? 15.572  37.726  -8.452  1.00 33.48 ?  138  LEU E N   1 
ATOM   9782  C  CA  . LEU E  1 114 ? 15.192  39.079  -8.053  1.00 32.75 ?  138  LEU E CA  1 
ATOM   9783  C  C   . LEU E  1 114 ? 14.124  39.699  -8.958  1.00 32.30 ?  138  LEU E C   1 
ATOM   9784  O  O   . LEU E  1 114 ? 13.811  40.881  -8.817  1.00 32.18 ?  138  LEU E O   1 
ATOM   9785  C  CB  . LEU E  1 114 ? 16.424  39.995  -7.997  1.00 32.66 ?  138  LEU E CB  1 
ATOM   9786  C  CG  . LEU E  1 114 ? 17.659  39.530  -7.218  1.00 32.26 ?  138  LEU E CG  1 
ATOM   9787  C  CD1 . LEU E  1 114 ? 18.668  40.661  -7.113  1.00 31.68 ?  138  LEU E CD1 1 
ATOM   9788  C  CD2 . LEU E  1 114 ? 17.283  39.015  -5.840  1.00 32.04 ?  138  LEU E CD2 1 
ATOM   9789  N  N   . TYR E  1 115 ? 13.559  38.900  -9.866  1.00 31.82 ?  139  TYR E N   1 
ATOM   9790  C  CA  . TYR E  1 115 ? 12.554  39.395  -10.815 1.00 31.39 ?  139  TYR E CA  1 
ATOM   9791  C  C   . TYR E  1 115 ? 11.283  39.922  -10.142 1.00 31.08 ?  139  TYR E C   1 
ATOM   9792  O  O   . TYR E  1 115 ? 10.626  40.809  -10.681 1.00 31.09 ?  139  TYR E O   1 
ATOM   9793  C  CB  . TYR E  1 115 ? 12.203  38.339  -11.876 1.00 31.43 ?  139  TYR E CB  1 
ATOM   9794  C  CG  . TYR E  1 115 ? 11.234  38.848  -12.926 1.00 31.50 ?  139  TYR E CG  1 
ATOM   9795  C  CD1 . TYR E  1 115 ? 11.662  39.693  -13.949 1.00 31.85 ?  139  TYR E CD1 1 
ATOM   9796  C  CD2 . TYR E  1 115 ? 9.884   38.504  -12.881 1.00 31.67 ?  139  TYR E CD2 1 
ATOM   9797  C  CE1 . TYR E  1 115 ? 10.771  40.171  -14.911 1.00 32.18 ?  139  TYR E CE1 1 
ATOM   9798  C  CE2 . TYR E  1 115 ? 8.987   38.982  -13.832 1.00 31.64 ?  139  TYR E CE2 1 
ATOM   9799  C  CZ  . TYR E  1 115 ? 9.435   39.810  -14.844 1.00 31.97 ?  139  TYR E CZ  1 
ATOM   9800  O  OH  . TYR E  1 115 ? 8.544   40.283  -15.784 1.00 32.74 ?  139  TYR E OH  1 
ATOM   9801  N  N   . TYR E  1 116 ? 10.950  39.381  -8.968  1.00 30.79 ?  140  TYR E N   1 
ATOM   9802  C  CA  . TYR E  1 116 ? 9.775   39.817  -8.203  1.00 30.38 ?  140  TYR E CA  1 
ATOM   9803  C  C   . TYR E  1 116 ? 9.741   41.337  -8.006  1.00 30.33 ?  140  TYR E C   1 
ATOM   9804  O  O   . TYR E  1 116 ? 8.665   41.933  -7.913  1.00 30.33 ?  140  TYR E O   1 
ATOM   9805  C  CB  . TYR E  1 116 ? 9.713   39.099  -6.845  1.00 30.32 ?  140  TYR E CB  1 
ATOM   9806  C  CG  . TYR E  1 116 ? 10.624  39.677  -5.774  1.00 29.73 ?  140  TYR E CG  1 
ATOM   9807  C  CD1 . TYR E  1 116 ? 11.975  39.328  -5.710  1.00 29.53 ?  140  TYR E CD1 1 
ATOM   9808  C  CD2 . TYR E  1 116 ? 10.128  40.565  -4.819  1.00 29.71 ?  140  TYR E CD2 1 
ATOM   9809  C  CE1 . TYR E  1 116 ? 12.815  39.863  -4.723  1.00 29.13 ?  140  TYR E CE1 1 
ATOM   9810  C  CE2 . TYR E  1 116 ? 10.950  41.101  -3.833  1.00 29.12 ?  140  TYR E CE2 1 
ATOM   9811  C  CZ  . TYR E  1 116 ? 12.293  40.748  -3.789  1.00 28.94 ?  140  TYR E CZ  1 
ATOM   9812  O  OH  . TYR E  1 116 ? 13.100  41.278  -2.810  1.00 27.64 ?  140  TYR E OH  1 
ATOM   9813  N  N   . LYS E  1 117 ? 10.926  41.949  -7.948  1.00 30.00 ?  141  LYS E N   1 
ATOM   9814  C  CA  . LYS E  1 117 ? 11.067  43.396  -7.777  1.00 29.79 ?  141  LYS E CA  1 
ATOM   9815  C  C   . LYS E  1 117 ? 10.467  44.193  -8.937  1.00 29.70 ?  141  LYS E C   1 
ATOM   9816  O  O   . LYS E  1 117 ? 9.981   45.307  -8.734  1.00 29.47 ?  141  LYS E O   1 
ATOM   9817  C  CB  . LYS E  1 117 ? 12.540  43.782  -7.570  1.00 29.64 ?  141  LYS E CB  1 
ATOM   9818  C  CG  . LYS E  1 117 ? 13.135  43.323  -6.239  1.00 29.15 ?  141  LYS E CG  1 
ATOM   9819  C  CD  . LYS E  1 117 ? 14.631  43.614  -6.168  1.00 27.85 ?  141  LYS E CD  1 
ATOM   9820  C  CE  . LYS E  1 117 ? 15.279  42.941  -4.962  1.00 26.75 ?  141  LYS E CE  1 
ATOM   9821  N  NZ  . LYS E  1 117 ? 15.008  43.657  -3.682  1.00 25.83 ?  141  LYS E NZ  1 
ATOM   9822  N  N   . LYS E  1 118 ? 10.513  43.633  -10.147 1.00 29.78 ?  142  LYS E N   1 
ATOM   9823  C  CA  . LYS E  1 118 ? 9.877   44.272  -11.303 1.00 29.93 ?  142  LYS E CA  1 
ATOM   9824  C  C   . LYS E  1 118 ? 8.355   44.321  -11.133 1.00 29.80 ?  142  LYS E C   1 
ATOM   9825  O  O   . LYS E  1 118 ? 7.730   45.339  -11.419 1.00 29.82 ?  142  LYS E O   1 
ATOM   9826  C  CB  . LYS E  1 118 ? 10.264  43.588  -12.622 1.00 30.00 ?  142  LYS E CB  1 
ATOM   9827  C  CG  . LYS E  1 118 ? 9.663   44.270  -13.847 1.00 30.22 ?  142  LYS E CG  1 
ATOM   9828  C  CD  . LYS E  1 118 ? 9.970   43.532  -15.136 1.00 31.12 ?  142  LYS E CD  1 
ATOM   9829  C  CE  . LYS E  1 118 ? 8.990   43.909  -16.241 1.00 30.99 ?  142  LYS E CE  1 
ATOM   9830  N  NZ  . LYS E  1 118 ? 7.604   43.420  -15.964 1.00 31.63 ?  142  LYS E NZ  1 
ATOM   9831  N  N   . GLY E  1 119 ? 7.776   43.221  -10.652 1.00 29.91 ?  143  GLY E N   1 
ATOM   9832  C  CA  . GLY E  1 119 ? 6.342   43.156  -10.349 1.00 29.99 ?  143  GLY E CA  1 
ATOM   9833  C  C   . GLY E  1 119 ? 5.943   44.142  -9.263  1.00 30.09 ?  143  GLY E C   1 
ATOM   9834  O  O   . GLY E  1 119 ? 4.879   44.768  -9.334  1.00 29.96 ?  143  GLY E O   1 
ATOM   9835  N  N   . LYS E  1 120 ? 6.812   44.281  -8.264  1.00 30.06 ?  144  LYS E N   1 
ATOM   9836  C  CA  . LYS E  1 120 ? 6.612   45.231  -7.173  1.00 30.20 ?  144  LYS E CA  1 
ATOM   9837  C  C   . LYS E  1 120 ? 6.740   46.687  -7.623  1.00 30.15 ?  144  LYS E C   1 
ATOM   9838  O  O   . LYS E  1 120 ? 6.021   47.551  -7.119  1.00 30.06 ?  144  LYS E O   1 
ATOM   9839  C  CB  . LYS E  1 120 ? 7.568   44.937  -6.018  1.00 30.18 ?  144  LYS E CB  1 
ATOM   9840  C  CG  . LYS E  1 120 ? 7.192   43.700  -5.227  1.00 30.90 ?  144  LYS E CG  1 
ATOM   9841  C  CD  . LYS E  1 120 ? 7.695   43.786  -3.796  1.00 32.18 ?  144  LYS E CD  1 
ATOM   9842  C  CE  . LYS E  1 120 ? 6.713   43.130  -2.840  1.00 33.55 ?  144  LYS E CE  1 
ATOM   9843  N  NZ  . LYS E  1 120 ? 5.433   43.901  -2.746  1.00 34.22 ?  144  LYS E NZ  1 
ATOM   9844  N  N   . LEU E  1 121 ? 7.650   46.955  -8.561  1.00 30.08 ?  145  LEU E N   1 
ATOM   9845  C  CA  . LEU E  1 121 ? 7.771   48.288  -9.159  1.00 30.32 ?  145  LEU E CA  1 
ATOM   9846  C  C   . LEU E  1 121 ? 6.471   48.688  -9.861  1.00 30.50 ?  145  LEU E C   1 
ATOM   9847  O  O   . LEU E  1 121 ? 5.976   49.800  -9.678  1.00 30.56 ?  145  LEU E O   1 
ATOM   9848  C  CB  . LEU E  1 121 ? 8.957   48.356  -10.140 1.00 30.26 ?  145  LEU E CB  1 
ATOM   9849  C  CG  . LEU E  1 121 ? 9.029   49.500  -11.170 1.00 30.10 ?  145  LEU E CG  1 
ATOM   9850  C  CD1 . LEU E  1 121 ? 9.169   50.876  -10.525 1.00 29.85 ?  145  LEU E CD1 1 
ATOM   9851  C  CD2 . LEU E  1 121 ? 10.171  49.268  -12.139 1.00 30.48 ?  145  LEU E CD2 1 
ATOM   9852  N  N   . GLU E  1 122 ? 5.928   47.767  -10.655 1.00 30.86 ?  146  GLU E N   1 
ATOM   9853  C  CA  . GLU E  1 122 ? 4.682   47.992  -11.388 1.00 31.09 ?  146  GLU E CA  1 
ATOM   9854  C  C   . GLU E  1 122 ? 3.485   48.100  -10.447 1.00 31.15 ?  146  GLU E C   1 
ATOM   9855  O  O   . GLU E  1 122 ? 2.527   48.816  -10.734 1.00 31.28 ?  146  GLU E O   1 
ATOM   9856  C  CB  . GLU E  1 122 ? 4.466   46.890  -12.431 1.00 31.11 ?  146  GLU E CB  1 
ATOM   9857  C  CG  . GLU E  1 122 ? 5.399   47.016  -13.632 1.00 31.65 ?  146  GLU E CG  1 
ATOM   9858  C  CD  . GLU E  1 122 ? 5.194   45.938  -14.686 1.00 32.35 ?  146  GLU E CD  1 
ATOM   9859  O  OE1 . GLU E  1 122 ? 4.094   45.352  -14.756 1.00 33.00 ?  146  GLU E OE1 1 
ATOM   9860  O  OE2 . GLU E  1 122 ? 6.143   45.683  -15.457 1.00 32.49 -1 146  GLU E OE2 1 
ATOM   9861  N  N   . GLU E  1 123 ? 3.555   47.390  -9.325  1.00 31.36 ?  147  GLU E N   1 
ATOM   9862  C  CA  . GLU E  1 123 ? 2.553   47.488  -8.269  1.00 31.53 ?  147  GLU E CA  1 
ATOM   9863  C  C   . GLU E  1 123 ? 2.557   48.892  -7.657  1.00 31.28 ?  147  GLU E C   1 
ATOM   9864  O  O   . GLU E  1 123 ? 1.498   49.499  -7.470  1.00 31.37 ?  147  GLU E O   1 
ATOM   9865  C  CB  . GLU E  1 123 ? 2.807   46.424  -7.197  1.00 31.69 ?  147  GLU E CB  1 
ATOM   9866  C  CG  . GLU E  1 123 ? 1.829   46.460  -6.029  1.00 33.32 ?  147  GLU E CG  1 
ATOM   9867  C  CD  . GLU E  1 123 ? 2.067   45.348  -5.033  1.00 35.30 ?  147  GLU E CD  1 
ATOM   9868  O  OE1 . GLU E  1 123 ? 2.042   44.164  -5.436  1.00 36.63 ?  147  GLU E OE1 1 
ATOM   9869  O  OE2 . GLU E  1 123 ? 2.271   45.657  -3.843  1.00 36.73 -1 147  GLU E OE2 1 
ATOM   9870  N  N   . VAL E  1 124 ? 3.752   49.400  -7.360  1.00 31.05 ?  148  VAL E N   1 
ATOM   9871  C  CA  . VAL E  1 124 ? 3.926   50.771  -6.872  1.00 30.80 ?  148  VAL E CA  1 
ATOM   9872  C  C   . VAL E  1 124 ? 3.375   51.785  -7.877  1.00 30.87 ?  148  VAL E C   1 
ATOM   9873  O  O   . VAL E  1 124 ? 2.659   52.715  -7.496  1.00 30.60 ?  148  VAL E O   1 
ATOM   9874  C  CB  . VAL E  1 124 ? 5.412   51.081  -6.558  1.00 30.79 ?  148  VAL E CB  1 
ATOM   9875  C  CG1 . VAL E  1 124 ? 5.652   52.587  -6.468  1.00 30.32 ?  148  VAL E CG1 1 
ATOM   9876  C  CG2 . VAL E  1 124 ? 5.848   50.379  -5.269  1.00 30.47 ?  148  VAL E CG2 1 
ATOM   9877  N  N   . GLU E  1 125 ? 3.709   51.587  -9.153  1.00 30.79 ?  149  GLU E N   1 
ATOM   9878  C  CA  . GLU E  1 125 ? 3.243   52.452  -10.232 1.00 30.98 ?  149  GLU E CA  1 
ATOM   9879  C  C   . GLU E  1 125 ? 1.718   52.426  -10.353 1.00 31.05 ?  149  GLU E C   1 
ATOM   9880  O  O   . GLU E  1 125 ? 1.094   53.471  -10.545 1.00 31.17 ?  149  GLU E O   1 
ATOM   9881  C  CB  . GLU E  1 125 ? 3.901   52.066  -11.564 1.00 31.01 ?  149  GLU E CB  1 
ATOM   9882  C  CG  . GLU E  1 125 ? 5.378   52.449  -11.658 1.00 31.05 ?  149  GLU E CG  1 
ATOM   9883  C  CD  . GLU E  1 125 ? 6.023   52.032  -12.970 1.00 31.53 ?  149  GLU E CD  1 
ATOM   9884  O  OE1 . GLU E  1 125 ? 5.783   50.895  -13.429 1.00 32.16 ?  149  GLU E OE1 1 
ATOM   9885  O  OE2 . GLU E  1 125 ? 6.784   52.843  -13.539 1.00 31.86 -1 149  GLU E OE2 1 
ATOM   9886  N  N   . ASN E  1 126 ? 1.135   51.231  -10.233 1.00 30.97 ?  150  ASN E N   1 
ATOM   9887  C  CA  . ASN E  1 126 ? -0.320  51.053  -10.225 1.00 30.94 ?  150  ASN E CA  1 
ATOM   9888  C  C   . ASN E  1 126 ? -0.978  51.780  -9.051  1.00 30.81 ?  150  ASN E C   1 
ATOM   9889  O  O   . ASN E  1 126 ? -2.002  52.441  -9.228  1.00 30.67 ?  150  ASN E O   1 
ATOM   9890  C  CB  . ASN E  1 126 ? -0.684  49.564  -10.202 1.00 30.95 ?  150  ASN E CB  1 
ATOM   9891  C  CG  . ASN E  1 126 ? -2.170  49.311  -10.449 1.00 31.58 ?  150  ASN E CG  1 
ATOM   9892  O  OD1 . ASN E  1 126 ? -2.869  48.770  -9.588  1.00 31.75 ?  150  ASN E OD1 1 
ATOM   9893  N  ND2 . ASN E  1 126 ? -2.654  49.696  -11.626 1.00 31.05 ?  150  ASN E ND2 1 
ATOM   9894  N  N   . ASN E  1 127 ? -0.382  51.651  -7.862  1.00 30.75 ?  151  ASN E N   1 
ATOM   9895  C  CA  . ASN E  1 127 ? -0.822  52.394  -6.679  1.00 30.59 ?  151  ASN E CA  1 
ATOM   9896  C  C   . ASN E  1 127 ? -0.828  53.901  -6.934  1.00 30.63 ?  151  ASN E C   1 
ATOM   9897  O  O   . ASN E  1 127 ? -1.805  54.584  -6.623  1.00 30.53 ?  151  ASN E O   1 
ATOM   9898  C  CB  . ASN E  1 127 ? 0.070   52.094  -5.462  1.00 30.35 ?  151  ASN E CB  1 
ATOM   9899  C  CG  . ASN E  1 127 ? -0.078  50.667  -4.942  1.00 30.08 ?  151  ASN E CG  1 
ATOM   9900  O  OD1 . ASN E  1 127 ? -1.100  50.003  -5.148  1.00 28.78 ?  151  ASN E OD1 1 
ATOM   9901  N  ND2 . ASN E  1 127 ? 0.950   50.196  -4.241  1.00 29.03 ?  151  ASN E ND2 1 
ATOM   9902  N  N   . LEU E  1 128 ? 0.264   54.400  -7.512  1.00 30.81 ?  152  LEU E N   1 
ATOM   9903  C  CA  . LEU E  1 128 ? 0.473   55.838  -7.708  1.00 31.26 ?  152  LEU E CA  1 
ATOM   9904  C  C   . LEU E  1 128 ? -0.447  56.450  -8.766  1.00 31.63 ?  152  LEU E C   1 
ATOM   9905  O  O   . LEU E  1 128 ? -0.884  57.597  -8.620  1.00 31.63 ?  152  LEU E O   1 
ATOM   9906  C  CB  . LEU E  1 128 ? 1.942   56.136  -8.039  1.00 31.01 ?  152  LEU E CB  1 
ATOM   9907  C  CG  . LEU E  1 128 ? 2.990   55.889  -6.943  1.00 31.17 ?  152  LEU E CG  1 
ATOM   9908  C  CD1 . LEU E  1 128 ? 4.394   56.114  -7.481  1.00 30.00 ?  152  LEU E CD1 1 
ATOM   9909  C  CD2 . LEU E  1 128 ? 2.738   56.750  -5.704  1.00 30.73 ?  152  LEU E CD2 1 
ATOM   9910  N  N   . ARG E  1 129 ? -0.722  55.695  -9.830  1.00 32.05 ?  153  ARG E N   1 
ATOM   9911  C  CA  . ARG E  1 129 ? -1.684  56.127  -10.849 1.00 32.73 ?  153  ARG E CA  1 
ATOM   9912  C  C   . ARG E  1 129 ? -3.076  56.270  -10.233 1.00 32.75 ?  153  ARG E C   1 
ATOM   9913  O  O   . ARG E  1 129 ? -3.780  57.244  -10.500 1.00 32.73 ?  153  ARG E O   1 
ATOM   9914  C  CB  . ARG E  1 129 ? -1.715  55.168  -12.046 1.00 32.75 ?  153  ARG E CB  1 
ATOM   9915  C  CG  . ARG E  1 129 ? -0.392  55.047  -12.802 1.00 34.09 ?  153  ARG E CG  1 
ATOM   9916  C  CD  . ARG E  1 129 ? -0.536  54.167  -14.035 1.00 36.26 ?  153  ARG E CD  1 
ATOM   9917  N  NE  . ARG E  1 129 ? 0.550   53.191  -14.160 1.00 38.76 ?  153  ARG E NE  1 
ATOM   9918  C  CZ  . ARG E  1 129 ? 1.703   53.407  -14.788 1.00 39.20 ?  153  ARG E CZ  1 
ATOM   9919  N  NH1 . ARG E  1 129 ? 1.952   54.576  -15.361 1.00 39.97 ?  153  ARG E NH1 1 
ATOM   9920  N  NH2 . ARG E  1 129 ? 2.614   52.446  -14.840 1.00 39.85 ?  153  ARG E NH2 1 
ATOM   9921  N  N   . SER E  1 130 ? -3.450  55.304  -9.394  1.00 33.02 ?  154  SER E N   1 
ATOM   9922  C  CA  . SER E  1 130 ? -4.716  55.339  -8.658  1.00 33.32 ?  154  SER E CA  1 
ATOM   9923  C  C   . SER E  1 130 ? -4.819  56.564  -7.746  1.00 33.66 ?  154  SER E C   1 
ATOM   9924  O  O   . SER E  1 130 ? -5.903  57.124  -7.573  1.00 33.77 ?  154  SER E O   1 
ATOM   9925  C  CB  . SER E  1 130 ? -4.890  54.057  -7.840  1.00 33.22 ?  154  SER E CB  1 
ATOM   9926  O  OG  . SER E  1 130 ? -6.018  54.133  -6.987  1.00 33.04 ?  154  SER E OG  1 
ATOM   9927  N  N   . MET E  1 131 ? -3.689  56.974  -7.172  1.00 33.94 ?  155  MET E N   1 
ATOM   9928  C  CA  . MET E  1 131 ? -3.643  58.134  -6.278  1.00 34.42 ?  155  MET E CA  1 
ATOM   9929  C  C   . MET E  1 131 ? -3.525  59.461  -7.031  1.00 34.73 ?  155  MET E C   1 
ATOM   9930  O  O   . MET E  1 131 ? -3.593  60.528  -6.425  1.00 34.72 ?  155  MET E O   1 
ATOM   9931  C  CB  . MET E  1 131 ? -2.498  57.988  -5.270  1.00 34.30 ?  155  MET E CB  1 
ATOM   9932  C  CG  . MET E  1 131 ? -2.711  56.867  -4.262  1.00 34.54 ?  155  MET E CG  1 
ATOM   9933  S  SD  . MET E  1 131 ? -1.177  56.315  -3.494  1.00 34.00 ?  155  MET E SD  1 
ATOM   9934  C  CE  . MET E  1 131 ? -1.731  54.818  -2.681  1.00 33.63 ?  155  MET E CE  1 
ATOM   9935  N  N   . GLY E  1 132 ? -3.348  59.387  -8.349  1.00 35.21 ?  156  GLY E N   1 
ATOM   9936  C  CA  . GLY E  1 132 ? -3.224  60.578  -9.184  1.00 35.87 ?  156  GLY E CA  1 
ATOM   9937  C  C   . GLY E  1 132 ? -1.839  61.196  -9.156  1.00 36.40 ?  156  GLY E C   1 
ATOM   9938  O  O   . GLY E  1 132 ? -1.642  62.302  -9.653  1.00 36.44 ?  156  GLY E O   1 
ATOM   9939  N  N   . LYS E  1 133 ? -0.875  60.474  -8.583  1.00 36.93 ?  157  LYS E N   1 
ATOM   9940  C  CA  . LYS E  1 133 ? 0.502   60.961  -8.464  1.00 37.44 ?  157  LYS E CA  1 
ATOM   9941  C  C   . LYS E  1 133 ? 1.357   60.601  -9.681  1.00 37.64 ?  157  LYS E C   1 
ATOM   9942  O  O   . LYS E  1 133 ? 2.454   61.138  -9.866  1.00 37.70 ?  157  LYS E O   1 
ATOM   9943  C  CB  . LYS E  1 133 ? 1.146   60.441  -7.171  1.00 37.57 ?  157  LYS E CB  1 
ATOM   9944  C  CG  . LYS E  1 133 ? 0.617   61.097  -5.892  1.00 38.43 ?  157  LYS E CG  1 
ATOM   9945  C  CD  . LYS E  1 133 ? 1.045   62.558  -5.798  1.00 40.41 ?  157  LYS E CD  1 
ATOM   9946  C  CE  . LYS E  1 133 ? 0.531   63.219  -4.531  1.00 42.15 ?  157  LYS E CE  1 
ATOM   9947  N  NZ  . LYS E  1 133 ? 0.830   64.682  -4.525  1.00 43.11 ?  157  LYS E NZ  1 
ATOM   9948  N  N   . LEU E  1 134 ? 0.839   59.703  -10.512 1.00 37.89 ?  158  LEU E N   1 
ATOM   9949  C  CA  . LEU E  1 134 ? 1.545   59.242  -11.702 1.00 38.26 ?  158  LEU E CA  1 
ATOM   9950  C  C   . LEU E  1 134 ? 0.581   59.088  -12.880 1.00 38.57 ?  158  LEU E C   1 
ATOM   9951  O  O   . LEU E  1 134 ? -0.525  58.566  -12.721 1.00 38.57 ?  158  LEU E O   1 
ATOM   9952  C  CB  . LEU E  1 134 ? 2.247   57.911  -11.410 1.00 38.09 ?  158  LEU E CB  1 
ATOM   9953  C  CG  . LEU E  1 134 ? 3.238   57.347  -12.432 1.00 38.16 ?  158  LEU E CG  1 
ATOM   9954  C  CD1 . LEU E  1 134 ? 4.532   58.154  -12.458 1.00 37.93 ?  158  LEU E CD1 1 
ATOM   9955  C  CD2 . LEU E  1 134 ? 3.527   55.885  -12.130 1.00 37.74 ?  158  LEU E CD2 1 
ATOM   9956  N  N   . GLY E  1 135 ? 1.010   59.547  -14.054 1.00 38.90 ?  159  GLY E N   1 
ATOM   9957  C  CA  . GLY E  1 135 ? 0.217   59.430  -15.279 1.00 39.31 ?  159  GLY E CA  1 
ATOM   9958  C  C   . GLY E  1 135 ? 0.004   57.992  -15.724 1.00 39.74 ?  159  GLY E C   1 
ATOM   9959  O  O   . GLY E  1 135 ? 0.835   57.117  -15.453 1.00 39.50 ?  159  GLY E O   1 
ATOM   9960  N  N   . GLU E  1 136 ? -1.115  57.758  -16.411 1.00 40.12 ?  160  GLU E N   1 
ATOM   9961  C  CA  . GLU E  1 136 ? -1.489  56.429  -16.909 1.00 40.63 ?  160  GLU E CA  1 
ATOM   9962  C  C   . GLU E  1 136 ? -0.448  55.826  -17.853 1.00 40.57 ?  160  GLU E C   1 
ATOM   9963  O  O   . GLU E  1 136 ? -0.255  54.610  -17.875 1.00 40.79 ?  160  GLU E O   1 
ATOM   9964  C  CB  . GLU E  1 136 ? -2.857  56.476  -17.602 1.00 40.85 ?  160  GLU E CB  1 
ATOM   9965  C  CG  . GLU E  1 136 ? -4.055  56.512  -16.650 1.00 42.18 ?  160  GLU E CG  1 
ATOM   9966  C  CD  . GLU E  1 136 ? -4.339  55.166  -15.999 1.00 43.92 ?  160  GLU E CD  1 
ATOM   9967  O  OE1 . GLU E  1 136 ? -4.527  54.168  -16.735 1.00 44.37 ?  160  GLU E OE1 1 
ATOM   9968  O  OE2 . GLU E  1 136 ? -4.385  55.109  -14.749 1.00 44.12 -1 160  GLU E OE2 1 
ATOM   9969  N  N   . LYS E  1 137 ? 0.214   56.682  -18.627 1.00 40.48 ?  161  LYS E N   1 
ATOM   9970  C  CA  . LYS E  1 137 ? 1.257   56.247  -19.556 1.00 40.53 ?  161  LYS E CA  1 
ATOM   9971  C  C   . LYS E  1 137 ? 2.644   56.739  -19.117 1.00 40.10 ?  161  LYS E C   1 
ATOM   9972  O  O   . LYS E  1 137 ? 3.606   56.693  -19.888 1.00 40.14 ?  161  LYS E O   1 
ATOM   9973  C  CB  . LYS E  1 137 ? 0.936   56.721  -20.982 1.00 40.75 ?  161  LYS E CB  1 
ATOM   9974  C  CG  . LYS E  1 137 ? -0.402  56.211  -21.536 1.00 41.67 ?  161  LYS E CG  1 
ATOM   9975  C  CD  . LYS E  1 137 ? -0.681  56.753  -22.941 1.00 43.49 ?  161  LYS E CD  1 
ATOM   9976  C  CE  . LYS E  1 137 ? -1.019  58.250  -22.934 1.00 44.09 ?  161  LYS E CE  1 
ATOM   9977  N  NZ  . LYS E  1 137 ? -2.419  58.526  -22.495 1.00 44.59 ?  161  LYS E NZ  1 
ATOM   9978  N  N   . GLU E  1 138 ? 2.734   57.199  -17.871 1.00 39.48 ?  162  GLU E N   1 
ATOM   9979  C  CA  . GLU E  1 138 ? 3.976   57.733  -17.317 1.00 38.97 ?  162  GLU E CA  1 
ATOM   9980  C  C   . GLU E  1 138 ? 4.636   56.723  -16.376 1.00 38.49 ?  162  GLU E C   1 
ATOM   9981  O  O   . GLU E  1 138 ? 3.998   56.210  -15.457 1.00 38.31 ?  162  GLU E O   1 
ATOM   9982  C  CB  . GLU E  1 138 ? 3.697   59.046  -16.577 1.00 38.99 ?  162  GLU E CB  1 
ATOM   9983  C  CG  . GLU E  1 138 ? 4.931   59.730  -15.997 1.00 39.44 ?  162  GLU E CG  1 
ATOM   9984  C  CD  . GLU E  1 138 ? 4.597   60.788  -14.956 1.00 40.20 ?  162  GLU E CD  1 
ATOM   9985  O  OE1 . GLU E  1 138 ? 3.407   60.937  -14.598 1.00 39.96 ?  162  GLU E OE1 1 
ATOM   9986  O  OE2 . GLU E  1 138 ? 5.533   61.471  -14.488 1.00 40.81 -1 162  GLU E OE2 1 
ATOM   9987  N  N   . THR E  1 139 ? 5.913   56.440  -16.615 1.00 37.92 ?  163  THR E N   1 
ATOM   9988  C  CA  . THR E  1 139 ? 6.678   55.568  -15.726 1.00 37.35 ?  163  THR E CA  1 
ATOM   9989  C  C   . THR E  1 139 ? 7.282   56.382  -14.585 1.00 36.72 ?  163  THR E C   1 
ATOM   9990  O  O   . THR E  1 139 ? 7.611   57.559  -14.758 1.00 36.55 ?  163  THR E O   1 
ATOM   9991  C  CB  . THR E  1 139 ? 7.805   54.812  -16.470 1.00 37.39 ?  163  THR E CB  1 
ATOM   9992  O  OG1 . THR E  1 139 ? 8.670   55.750  -17.122 1.00 37.72 ?  163  THR E OG1 1 
ATOM   9993  C  CG2 . THR E  1 139 ? 7.230   53.854  -17.500 1.00 37.56 ?  163  THR E CG2 1 
ATOM   9994  N  N   . LEU E  1 140 ? 7.411   55.755  -13.418 1.00 36.04 ?  164  LEU E N   1 
ATOM   9995  C  CA  . LEU E  1 140 ? 8.117   56.360  -12.293 1.00 35.30 ?  164  LEU E CA  1 
ATOM   9996  C  C   . LEU E  1 140 ? 9.612   56.347  -12.601 1.00 34.88 ?  164  LEU E C   1 
ATOM   9997  O  O   . LEU E  1 140 ? 10.214  55.280  -12.742 1.00 34.79 ?  164  LEU E O   1 
ATOM   9998  C  CB  . LEU E  1 140 ? 7.815   55.607  -10.990 1.00 35.18 ?  164  LEU E CB  1 
ATOM   9999  C  CG  . LEU E  1 140 ? 8.357   56.160  -9.664  1.00 35.17 ?  164  LEU E CG  1 
ATOM   10000 C  CD1 . LEU E  1 140 ? 7.722   57.500  -9.294  1.00 34.68 ?  164  LEU E CD1 1 
ATOM   10001 C  CD2 . LEU E  1 140 ? 8.149   55.151  -8.546  1.00 34.95 ?  164  LEU E CD2 1 
ATOM   10002 N  N   . LYS E  1 141 ? 10.197  57.536  -12.722 1.00 34.31 ?  165  LYS E N   1 
ATOM   10003 C  CA  . LYS E  1 141 ? 11.594  57.682  -13.135 1.00 33.89 ?  165  LYS E CA  1 
ATOM   10004 C  C   . LYS E  1 141 ? 12.577  57.257  -12.044 1.00 33.37 ?  165  LYS E C   1 
ATOM   10005 O  O   . LYS E  1 141 ? 13.545  56.540  -12.322 1.00 33.34 ?  165  LYS E O   1 
ATOM   10006 C  CB  . LYS E  1 141 ? 11.884  59.121  -13.591 1.00 34.02 ?  165  LYS E CB  1 
ATOM   10007 C  CG  . LYS E  1 141 ? 11.063  59.595  -14.800 1.00 34.52 ?  165  LYS E CG  1 
ATOM   10008 C  CD  . LYS E  1 141 ? 11.363  58.785  -16.064 1.00 35.59 ?  165  LYS E CD  1 
ATOM   10009 C  CE  . LYS E  1 141 ? 10.595  59.314  -17.279 1.00 36.45 ?  165  LYS E CE  1 
ATOM   10010 N  NZ  . LYS E  1 141 ? 9.111   59.292  -17.083 1.00 36.53 ?  165  LYS E NZ  1 
ATOM   10011 N  N   . GLU E  1 142 ? 12.316  57.700  -10.813 1.00 32.57 ?  166  GLU E N   1 
ATOM   10012 C  CA  . GLU E  1 142 ? 13.148  57.374  -9.652  1.00 31.90 ?  166  GLU E CA  1 
ATOM   10013 C  C   . GLU E  1 142 ? 12.405  57.627  -8.342  1.00 31.43 ?  166  GLU E C   1 
ATOM   10014 O  O   . GLU E  1 142 ? 11.291  58.161  -8.333  1.00 31.15 ?  166  GLU E O   1 
ATOM   10015 C  CB  . GLU E  1 142 ? 14.451  58.190  -9.661  1.00 31.90 ?  166  GLU E CB  1 
ATOM   10016 C  CG  . GLU E  1 142 ? 14.254  59.695  -9.473  1.00 31.79 ?  166  GLU E CG  1 
ATOM   10017 C  CD  . GLU E  1 142 ? 15.551  60.457  -9.247  1.00 32.29 ?  166  GLU E CD  1 
ATOM   10018 O  OE1 . GLU E  1 142 ? 16.643  59.892  -9.483  1.00 32.51 ?  166  GLU E OE1 1 
ATOM   10019 O  OE2 . GLU E  1 142 ? 15.473  61.635  -8.834  1.00 31.96 -1 166  GLU E OE2 1 
ATOM   10020 N  N   . VAL E  1 143 ? 13.040  57.231  -7.241  1.00 30.88 ?  167  VAL E N   1 
ATOM   10021 C  CA  . VAL E  1 143 ? 12.605  57.603  -5.901  1.00 30.41 ?  167  VAL E CA  1 
ATOM   10022 C  C   . VAL E  1 143 ? 13.771  58.357  -5.261  1.00 30.30 ?  167  VAL E C   1 
ATOM   10023 O  O   . VAL E  1 143 ? 14.660  57.756  -4.647  1.00 30.22 ?  167  VAL E O   1 
ATOM   10024 C  CB  . VAL E  1 143 ? 12.187  56.373  -5.059  1.00 30.40 ?  167  VAL E CB  1 
ATOM   10025 C  CG1 . VAL E  1 143 ? 11.527  56.804  -3.757  1.00 30.09 ?  167  VAL E CG1 1 
ATOM   10026 C  CG2 . VAL E  1 143 ? 11.252  55.459  -5.858  1.00 30.11 ?  167  VAL E CG2 1 
ATOM   10027 N  N   . GLY E  1 144 ? 13.769  59.677  -5.444  1.00 30.11 ?  168  GLY E N   1 
ATOM   10028 C  CA  . GLY E  1 144 ? 14.863  60.538  -5.001  1.00 29.72 ?  168  GLY E CA  1 
ATOM   10029 C  C   . GLY E  1 144 ? 14.538  61.322  -3.749  1.00 29.50 ?  168  GLY E C   1 
ATOM   10030 O  O   . GLY E  1 144 ? 13.459  61.161  -3.172  1.00 29.44 ?  168  GLY E O   1 
ATOM   10031 N  N   . CYS E  1 145 ? 15.475  62.173  -3.331  1.00 29.41 ?  169  CYS E N   1 
ATOM   10032 C  CA  . CYS E  1 145 ? 15.330  62.969  -2.109  1.00 29.30 ?  169  CYS E CA  1 
ATOM   10033 C  C   . CYS E  1 145 ? 13.983  63.681  -2.039  1.00 29.31 ?  169  CYS E C   1 
ATOM   10034 O  O   . CYS E  1 145 ? 13.271  63.577  -1.039  1.00 29.29 ?  169  CYS E O   1 
ATOM   10035 C  CB  . CYS E  1 145 ? 16.450  64.011  -1.984  1.00 29.32 ?  169  CYS E CB  1 
ATOM   10036 S  SG  . CYS E  1 145 ? 18.068  63.520  -2.600  1.00 28.85 ?  169  CYS E SG  1 
ATOM   10037 N  N   . ILE E  1 146 ? 13.642  64.394  -3.113  1.00 29.32 ?  170  ILE E N   1 
ATOM   10038 C  CA  . ILE E  1 146 ? 12.436  65.230  -3.159  1.00 29.28 ?  170  ILE E CA  1 
ATOM   10039 C  C   . ILE E  1 146 ? 11.132  64.423  -3.079  1.00 29.08 ?  170  ILE E C   1 
ATOM   10040 O  O   . ILE E  1 146 ? 10.108  64.939  -2.640  1.00 29.19 ?  170  ILE E O   1 
ATOM   10041 C  CB  . ILE E  1 146 ? 12.440  66.182  -4.400  1.00 29.30 ?  170  ILE E CB  1 
ATOM   10042 C  CG1 . ILE E  1 146 ? 11.465  67.354  -4.195  1.00 29.89 ?  170  ILE E CG1 1 
ATOM   10043 C  CG2 . ILE E  1 146 ? 12.175  65.408  -5.707  1.00 29.20 ?  170  ILE E CG2 1 
ATOM   10044 C  CD1 . ILE E  1 146 ? 11.558  68.460  -5.252  1.00 30.08 ?  170  ILE E CD1 1 
ATOM   10045 N  N   . ASP E  1 147 ? 11.178  63.158  -3.490  1.00 29.08 ?  171  ASP E N   1 
ATOM   10046 C  CA  . ASP E  1 147 ? 9.991   62.300  -3.463  1.00 28.89 ?  171  ASP E CA  1 
ATOM   10047 C  C   . ASP E  1 147 ? 9.580   61.937  -2.034  1.00 28.85 ?  171  ASP E C   1 
ATOM   10048 O  O   . ASP E  1 147 ? 8.430   62.146  -1.641  1.00 28.67 ?  171  ASP E O   1 
ATOM   10049 C  CB  . ASP E  1 147 ? 10.214  61.046  -4.304  1.00 28.92 ?  171  ASP E CB  1 
ATOM   10050 C  CG  . ASP E  1 147 ? 10.487  61.364  -5.761  1.00 29.19 ?  171  ASP E CG  1 
ATOM   10051 O  OD1 . ASP E  1 147 ? 9.662   62.065  -6.388  1.00 29.35 ?  171  ASP E OD1 1 
ATOM   10052 O  OD2 . ASP E  1 147 ? 11.527  60.908  -6.279  1.00 29.12 -1 171  ASP E OD2 1 
ATOM   10053 N  N   . CYS E  1 148 ? 10.529  61.409  -1.263  1.00 28.64 ?  172  CYS E N   1 
ATOM   10054 C  CA  . CYS E  1 148 ? 10.274  61.035  0.126   1.00 28.47 ?  172  CYS E CA  1 
ATOM   10055 C  C   . CYS E  1 148 ? 10.193  62.249  1.045   1.00 28.35 ?  172  CYS E C   1 
ATOM   10056 O  O   . CYS E  1 148 ? 9.357   62.290  1.944   1.00 28.11 ?  172  CYS E O   1 
ATOM   10057 C  CB  . CYS E  1 148 ? 11.363  60.092  0.640   1.00 28.39 ?  172  CYS E CB  1 
ATOM   10058 S  SG  . CYS E  1 148 ? 11.356  58.431  -0.056  1.00 28.47 ?  172  CYS E SG  1 
ATOM   10059 N  N   . HIS E  1 149 ? 11.065  63.230  0.816   1.00 28.52 ?  173  HIS E N   1 
ATOM   10060 C  CA  . HIS E  1 149 ? 11.206  64.364  1.735   1.00 28.82 ?  173  HIS E CA  1 
ATOM   10061 C  C   . HIS E  1 149 ? 10.292  65.567  1.446   1.00 29.20 ?  173  HIS E C   1 
ATOM   10062 O  O   . HIS E  1 149 ? 10.214  66.484  2.261   1.00 28.92 ?  173  HIS E O   1 
ATOM   10063 C  CB  . HIS E  1 149 ? 12.676  64.802  1.842   1.00 28.64 ?  173  HIS E CB  1 
ATOM   10064 C  CG  . HIS E  1 149 ? 13.541  63.846  2.611   1.00 28.69 ?  173  HIS E CG  1 
ATOM   10065 N  ND1 . HIS E  1 149 ? 13.414  63.662  3.971   1.00 28.15 ?  173  HIS E ND1 1 
ATOM   10066 C  CD2 . HIS E  1 149 ? 14.551  63.032  2.215   1.00 28.06 ?  173  HIS E CD2 1 
ATOM   10067 C  CE1 . HIS E  1 149 ? 14.302  62.772  4.379   1.00 27.55 ?  173  HIS E CE1 1 
ATOM   10068 N  NE2 . HIS E  1 149 ? 15.007  62.373  3.335   1.00 27.75 ?  173  HIS E NE2 1 
ATOM   10069 N  N   . VAL E  1 150 ? 9.615   65.574  0.295   1.00 29.68 ?  174  VAL E N   1 
ATOM   10070 C  CA  . VAL E  1 150 ? 8.666   66.655  -0.025  1.00 30.31 ?  174  VAL E CA  1 
ATOM   10071 C  C   . VAL E  1 150 ? 7.326   66.100  -0.531  1.00 30.72 ?  174  VAL E C   1 
ATOM   10072 O  O   . VAL E  1 150 ? 6.306   66.204  0.155   1.00 30.75 ?  174  VAL E O   1 
ATOM   10073 C  CB  . VAL E  1 150 ? 9.248   67.701  -1.034  1.00 30.31 ?  174  VAL E CB  1 
ATOM   10074 C  CG1 . VAL E  1 150 ? 8.272   68.856  -1.234  1.00 30.30 ?  174  VAL E CG1 1 
ATOM   10075 C  CG2 . VAL E  1 150 ? 10.596  68.244  -0.561  1.00 30.31 ?  174  VAL E CG2 1 
ATOM   10076 N  N   . ASP E  1 151 ? 7.338   65.515  -1.728  1.00 31.25 ?  175  ASP E N   1 
ATOM   10077 C  CA  . ASP E  1 151 ? 6.139   64.921  -2.317  1.00 32.02 ?  175  ASP E CA  1 
ATOM   10078 C  C   . ASP E  1 151 ? 6.502   63.941  -3.429  1.00 32.34 ?  175  ASP E C   1 
ATOM   10079 O  O   . ASP E  1 151 ? 7.399   64.209  -4.233  1.00 32.30 ?  175  ASP E O   1 
ATOM   10080 C  CB  . ASP E  1 151 ? 5.201   66.009  -2.860  1.00 32.08 ?  175  ASP E CB  1 
ATOM   10081 C  CG  . ASP E  1 151 ? 3.847   65.461  -3.274  1.00 32.66 ?  175  ASP E CG  1 
ATOM   10082 O  OD1 . ASP E  1 151 ? 3.220   64.725  -2.479  1.00 32.95 ?  175  ASP E OD1 1 
ATOM   10083 O  OD2 . ASP E  1 151 ? 3.406   65.773  -4.399  1.00 34.08 -1 175  ASP E OD2 1 
ATOM   10084 N  N   . VAL E  1 152 ? 5.789   62.817  -3.468  1.00 32.79 ?  176  VAL E N   1 
ATOM   10085 C  CA  . VAL E  1 152 ? 6.035   61.751  -4.438  1.00 33.57 ?  176  VAL E CA  1 
ATOM   10086 C  C   . VAL E  1 152 ? 5.814   62.222  -5.878  1.00 34.21 ?  176  VAL E C   1 
ATOM   10087 O  O   . VAL E  1 152 ? 4.716   62.662  -6.237  1.00 34.24 ?  176  VAL E O   1 
ATOM   10088 C  CB  . VAL E  1 152 ? 5.173   60.490  -4.139  1.00 33.44 ?  176  VAL E CB  1 
ATOM   10089 C  CG1 . VAL E  1 152 ? 5.263   59.481  -5.278  1.00 33.28 ?  176  VAL E CG1 1 
ATOM   10090 C  CG2 . VAL E  1 152 ? 5.604   59.845  -2.826  1.00 33.43 ?  176  VAL E CG2 1 
ATOM   10091 N  N   . ASN E  1 153 ? 6.875   62.121  -6.681  1.00 34.96 ?  177  ASN E N   1 
ATOM   10092 C  CA  . ASN E  1 153 ? 6.868   62.485  -8.106  1.00 35.79 ?  177  ASN E CA  1 
ATOM   10093 C  C   . ASN E  1 153 ? 6.688   63.990  -8.359  1.00 36.34 ?  177  ASN E C   1 
ATOM   10094 O  O   . ASN E  1 153 ? 6.096   64.403  -9.362  1.00 36.44 ?  177  ASN E O   1 
ATOM   10095 C  CB  . ASN E  1 153 ? 5.851   61.633  -8.894  1.00 35.84 ?  177  ASN E CB  1 
ATOM   10096 C  CG  . ASN E  1 153 ? 6.110   61.638  -10.398 1.00 36.12 ?  177  ASN E CG  1 
ATOM   10097 O  OD1 . ASN E  1 153 ? 7.257   61.598  -10.849 1.00 36.21 ?  177  ASN E OD1 1 
ATOM   10098 N  ND2 . ASN E  1 153 ? 5.036   61.682  -11.179 1.00 36.13 ?  177  ASN E ND2 1 
ATOM   10099 N  N   . LYS E  1 154 ? 7.221   64.799  -7.443  1.00 36.94 ?  178  LYS E N   1 
ATOM   10100 C  CA  . LYS E  1 154 ? 7.205   66.259  -7.570  1.00 37.50 ?  178  LYS E CA  1 
ATOM   10101 C  C   . LYS E  1 154 ? 7.999   66.703  -8.799  1.00 37.84 ?  178  LYS E C   1 
ATOM   10102 O  O   . LYS E  1 154 ? 9.127   66.248  -9.019  1.00 37.85 ?  178  LYS E O   1 
ATOM   10103 C  CB  . LYS E  1 154 ? 7.756   66.911  -6.300  1.00 37.36 ?  178  LYS E CB  1 
ATOM   10104 C  CG  . LYS E  1 154 ? 7.587   68.423  -6.228  1.00 37.61 ?  178  LYS E CG  1 
ATOM   10105 C  CD  . LYS E  1 154 ? 7.774   68.917  -4.802  1.00 38.12 ?  178  LYS E CD  1 
ATOM   10106 C  CE  . LYS E  1 154 ? 7.987   70.426  -4.736  1.00 38.87 ?  178  LYS E CE  1 
ATOM   10107 N  NZ  . LYS E  1 154 ? 6.760   71.211  -5.057  1.00 39.01 ?  178  LYS E NZ  1 
ATOM   10108 N  N   A LYS E  1 155 ? 7.399   67.590  -9.591  0.50 38.05 ?  179  LYS E N   1 
ATOM   10109 N  N   B LYS E  1 155 ? 7.401   67.595  -9.586  0.50 38.08 ?  179  LYS E N   1 
ATOM   10110 C  CA  A LYS E  1 155 ? 7.998   68.050  -10.844 0.50 38.23 ?  179  LYS E CA  1 
ATOM   10111 C  CA  B LYS E  1 155 ? 7.988   68.051  -10.847 0.50 38.30 ?  179  LYS E CA  1 
ATOM   10112 C  C   A LYS E  1 155 ? 8.642   69.433  -10.733 0.50 38.41 ?  179  LYS E C   1 
ATOM   10113 C  C   B LYS E  1 155 ? 8.618   69.442  -10.751 0.50 38.45 ?  179  LYS E C   1 
ATOM   10114 O  O   A LYS E  1 155 ? 9.529   69.772  -11.520 0.50 38.46 ?  179  LYS E O   1 
ATOM   10115 O  O   B LYS E  1 155 ? 9.475   69.795  -11.566 0.50 38.51 ?  179  LYS E O   1 
ATOM   10116 C  CB  A LYS E  1 155 ? 6.955   68.048  -11.965 0.50 38.24 ?  179  LYS E CB  1 
ATOM   10117 C  CB  B LYS E  1 155 ? 6.929   68.033  -11.952 0.50 38.34 ?  179  LYS E CB  1 
ATOM   10118 C  CG  A LYS E  1 155 ? 6.284   66.701  -12.190 0.50 38.08 ?  179  LYS E CG  1 
ATOM   10119 C  CG  B LYS E  1 155 ? 5.671   68.802  -11.594 0.50 38.41 ?  179  LYS E CG  1 
ATOM   10120 C  CD  A LYS E  1 155 ? 7.288   65.651  -12.639 0.50 38.01 ?  179  LYS E CD  1 
ATOM   10121 C  CD  B LYS E  1 155 ? 5.225   68.465  -10.179 0.50 38.40 ?  179  LYS E CD  1 
ATOM   10122 C  CE  A LYS E  1 155 ? 6.620   64.303  -12.870 0.50 37.59 ?  179  LYS E CE  1 
ATOM   10123 C  CE  B LYS E  1 155 ? 4.263   69.502  -9.635  0.50 38.40 ?  179  LYS E CE  1 
ATOM   10124 N  NZ  A LYS E  1 155 ? 5.627   64.342  -13.978 0.50 37.34 ?  179  LYS E NZ  1 
ATOM   10125 N  NZ  B LYS E  1 155 ? 4.188   69.435  -8.150  0.50 38.05 ?  179  LYS E NZ  1 
ATOM   10126 N  N   . ASP E  1 156 ? 8.195   70.222  -9.757  1.00 38.51 ?  180  ASP E N   1 
ATOM   10127 C  CA  . ASP E  1 156 ? 8.663   71.607  -9.597  1.00 38.72 ?  180  ASP E CA  1 
ATOM   10128 C  C   . ASP E  1 156 ? 9.612   71.824  -8.406  1.00 38.59 ?  180  ASP E C   1 
ATOM   10129 O  O   . ASP E  1 156 ? 10.196  70.869  -7.883  1.00 38.65 ?  180  ASP E O   1 
ATOM   10130 C  CB  . ASP E  1 156 ? 7.468   72.578  -9.551  1.00 38.91 ?  180  ASP E CB  1 
ATOM   10131 C  CG  . ASP E  1 156 ? 6.481   72.259  -8.428  1.00 39.90 ?  180  ASP E CG  1 
ATOM   10132 O  OD1 . ASP E  1 156 ? 6.557   71.159  -7.836  1.00 40.47 ?  180  ASP E OD1 1 
ATOM   10133 O  OD2 . ASP E  1 156 ? 5.616   73.118  -8.142  1.00 40.99 -1 180  ASP E OD2 1 
ATOM   10134 N  N   . LYS E  1 157 ? 9.758   73.083  -7.995  1.00 38.36 ?  181  LYS E N   1 
ATOM   10135 C  CA  . LYS E  1 157 ? 10.711  73.477  -6.956  1.00 38.18 ?  181  LYS E CA  1 
ATOM   10136 C  C   . LYS E  1 157 ? 10.113  73.404  -5.551  1.00 37.74 ?  181  LYS E C   1 
ATOM   10137 O  O   . LYS E  1 157 ? 8.910   73.588  -5.366  1.00 37.61 ?  181  LYS E O   1 
ATOM   10138 C  CB  . LYS E  1 157 ? 11.252  74.887  -7.229  1.00 38.19 ?  181  LYS E CB  1 
ATOM   10139 C  CG  . LYS E  1 157 ? 12.205  74.970  -8.420  1.00 39.21 ?  181  LYS E CG  1 
ATOM   10140 C  CD  . LYS E  1 157 ? 12.414  76.406  -8.899  1.00 40.40 ?  181  LYS E CD  1 
ATOM   10141 C  CE  . LYS E  1 157 ? 13.463  77.140  -8.074  1.00 41.62 ?  181  LYS E CE  1 
ATOM   10142 N  NZ  . LYS E  1 157 ? 13.536  78.601  -8.399  1.00 42.27 ?  181  LYS E NZ  1 
ATOM   10143 N  N   . ALA E  1 158 ? 10.971  73.135  -4.571  1.00 37.33 ?  182  ALA E N   1 
ATOM   10144 C  CA  . ALA E  1 158 ? 10.560  73.030  -3.172  1.00 36.93 ?  182  ALA E CA  1 
ATOM   10145 C  C   . ALA E  1 158 ? 11.256  74.084  -2.322  1.00 36.58 ?  182  ALA E C   1 
ATOM   10146 O  O   . ALA E  1 158 ? 12.408  74.433  -2.580  1.00 36.80 ?  182  ALA E O   1 
ATOM   10147 C  CB  . ALA E  1 158 ? 10.867  71.637  -2.635  1.00 36.93 ?  182  ALA E CB  1 
ATOM   10148 N  N   . ASP E  1 159 ? 10.549  74.590  -1.317  1.00 36.11 ?  183  ASP E N   1 
ATOM   10149 C  CA  . ASP E  1 159 ? 11.136  75.488  -0.330  1.00 35.63 ?  183  ASP E CA  1 
ATOM   10150 C  C   . ASP E  1 159 ? 11.695  74.652  0.823   1.00 35.15 ?  183  ASP E C   1 
ATOM   10151 O  O   . ASP E  1 159 ? 10.936  73.996  1.541   1.00 34.78 ?  183  ASP E O   1 
ATOM   10152 C  CB  . ASP E  1 159 ? 10.089  76.495  0.169   1.00 35.69 ?  183  ASP E CB  1 
ATOM   10153 C  CG  . ASP E  1 159 ? 10.697  77.626  0.992   1.00 35.99 ?  183  ASP E CG  1 
ATOM   10154 O  OD1 . ASP E  1 159 ? 11.502  77.356  1.906   1.00 36.14 ?  183  ASP E OD1 1 
ATOM   10155 O  OD2 . ASP E  1 159 ? 10.356  78.798  0.730   1.00 37.28 -1 183  ASP E OD2 1 
ATOM   10156 N  N   . HIS E  1 160 ? 13.020  74.692  0.990   1.00 34.77 ?  184  HIS E N   1 
ATOM   10157 C  CA  . HIS E  1 160 ? 13.737  73.916  2.019   1.00 34.32 ?  184  HIS E CA  1 
ATOM   10158 C  C   . HIS E  1 160 ? 13.255  74.243  3.445   1.00 34.12 ?  184  HIS E C   1 
ATOM   10159 O  O   . HIS E  1 160 ? 13.324  73.396  4.337   1.00 33.92 ?  184  HIS E O   1 
ATOM   10160 C  CB  . HIS E  1 160 ? 15.255  74.143  1.892   1.00 34.24 ?  184  HIS E CB  1 
ATOM   10161 C  CG  . HIS E  1 160 ? 16.106  72.980  2.330   1.00 34.09 ?  184  HIS E CG  1 
ATOM   10162 N  ND1 . HIS E  1 160 ? 16.425  72.740  3.650   1.00 33.30 ?  184  HIS E ND1 1 
ATOM   10163 C  CD2 . HIS E  1 160 ? 16.748  72.025  1.612   1.00 33.30 ?  184  HIS E CD2 1 
ATOM   10164 C  CE1 . HIS E  1 160 ? 17.203  71.672  3.727   1.00 33.44 ?  184  HIS E CE1 1 
ATOM   10165 N  NE2 . HIS E  1 160 ? 17.422  71.221  2.504   1.00 33.20 ?  184  HIS E NE2 1 
ATOM   10166 N  N   . THR E  1 161 ? 12.749  75.461  3.642   1.00 33.89 ?  185  THR E N   1 
ATOM   10167 C  CA  . THR E  1 161 ? 12.320  75.930  4.968   1.00 33.78 ?  185  THR E CA  1 
ATOM   10168 C  C   . THR E  1 161 ? 10.843  75.660  5.268   1.00 33.71 ?  185  THR E C   1 
ATOM   10169 O  O   . THR E  1 161 ? 10.365  75.936  6.375   1.00 33.73 ?  185  THR E O   1 
ATOM   10170 C  CB  . THR E  1 161 ? 12.562  77.452  5.144   1.00 33.68 ?  185  THR E CB  1 
ATOM   10171 O  OG1 . THR E  1 161 ? 11.600  78.186  4.376   1.00 33.57 ?  185  THR E OG1 1 
ATOM   10172 C  CG2 . THR E  1 161 ? 13.965  77.839  4.708   1.00 33.76 ?  185  THR E CG2 1 
ATOM   10173 N  N   . LYS E  1 162 ? 10.125  75.125  4.286   1.00 33.58 ?  186  LYS E N   1 
ATOM   10174 C  CA  . LYS E  1 162 ? 8.672   75.030  4.370   1.00 33.50 ?  186  LYS E CA  1 
ATOM   10175 C  C   . LYS E  1 162 ? 8.130   73.665  3.939   1.00 33.11 ?  186  LYS E C   1 
ATOM   10176 O  O   . LYS E  1 162 ? 7.158   73.170  4.514   1.00 32.99 ?  186  LYS E O   1 
ATOM   10177 C  CB  . LYS E  1 162 ? 8.046   76.144  3.524   1.00 33.69 ?  186  LYS E CB  1 
ATOM   10178 C  CG  . LYS E  1 162 ? 6.595   76.476  3.856   1.00 34.90 ?  186  LYS E CG  1 
ATOM   10179 C  CD  . LYS E  1 162 ? 6.156   77.808  3.224   1.00 36.32 ?  186  LYS E CD  1 
ATOM   10180 C  CE  . LYS E  1 162 ? 6.227   77.794  1.695   1.00 36.67 ?  186  LYS E CE  1 
ATOM   10181 N  NZ  . LYS E  1 162 ? 5.457   76.665  1.093   1.00 37.86 ?  186  LYS E NZ  1 
ATOM   10182 N  N   . ASP E  1 163 ? 8.774   73.066  2.940   1.00 32.78 ?  187  ASP E N   1 
ATOM   10183 C  CA  . ASP E  1 163 ? 8.262   71.867  2.273   1.00 32.43 ?  187  ASP E CA  1 
ATOM   10184 C  C   . ASP E  1 163 ? 8.912   70.550  2.735   1.00 32.16 ?  187  ASP E C   1 
ATOM   10185 O  O   . ASP E  1 163 ? 8.346   69.473  2.522   1.00 32.18 ?  187  ASP E O   1 
ATOM   10186 C  CB  . ASP E  1 163 ? 8.405   72.016  0.749   1.00 32.75 ?  187  ASP E CB  1 
ATOM   10187 C  CG  . ASP E  1 163 ? 7.659   73.233  0.191   1.00 33.05 ?  187  ASP E CG  1 
ATOM   10188 O  OD1 . ASP E  1 163 ? 6.714   73.729  0.839   1.00 33.74 ?  187  ASP E OD1 1 
ATOM   10189 O  OD2 . ASP E  1 163 ? 8.018   73.689  -0.914  1.00 33.77 -1 187  ASP E OD2 1 
ATOM   10190 N  N   . ILE E  1 164 ? 10.091  70.635  3.355   1.00 31.64 ?  188  ILE E N   1 
ATOM   10191 C  CA  . ILE E  1 164 ? 10.824  69.447  3.818   1.00 31.03 ?  188  ILE E CA  1 
ATOM   10192 C  C   . ILE E  1 164 ? 10.091  68.759  4.969   1.00 30.52 ?  188  ILE E C   1 
ATOM   10193 O  O   . ILE E  1 164 ? 9.634   69.415  5.906   1.00 30.40 ?  188  ILE E O   1 
ATOM   10194 C  CB  . ILE E  1 164 ? 12.292  69.783  4.247   1.00 31.16 ?  188  ILE E CB  1 
ATOM   10195 C  CG1 . ILE E  1 164 ? 13.095  70.393  3.086   1.00 31.08 ?  188  ILE E CG1 1 
ATOM   10196 C  CG2 . ILE E  1 164 ? 13.006  68.550  4.828   1.00 31.31 ?  188  ILE E CG2 1 
ATOM   10197 C  CD1 . ILE E  1 164 ? 13.372  69.462  1.919   1.00 31.55 ?  188  ILE E CD1 1 
ATOM   10198 N  N   . ARG E  1 165 ? 9.988   67.435  4.877   1.00 29.92 ?  189  ARG E N   1 
ATOM   10199 C  CA  . ARG E  1 165 ? 9.351   66.603  5.897   1.00 29.48 ?  189  ARG E CA  1 
ATOM   10200 C  C   . ARG E  1 165 ? 10.219  65.374  6.193   1.00 28.93 ?  189  ARG E C   1 
ATOM   10201 O  O   . ARG E  1 165 ? 11.060  64.988  5.375   1.00 28.71 ?  189  ARG E O   1 
ATOM   10202 C  CB  . ARG E  1 165 ? 7.968   66.141  5.414   1.00 29.62 ?  189  ARG E CB  1 
ATOM   10203 C  CG  . ARG E  1 165 ? 8.035   65.085  4.309   1.00 30.21 ?  189  ARG E CG  1 
ATOM   10204 C  CD  . ARG E  1 165 ? 6.681   64.663  3.778   1.00 31.81 ?  189  ARG E CD  1 
ATOM   10205 N  NE  . ARG E  1 165 ? 6.840   63.884  2.550   1.00 32.94 ?  189  ARG E NE  1 
ATOM   10206 C  CZ  . ARG E  1 165 ? 5.841   63.470  1.774   1.00 33.66 ?  189  ARG E CZ  1 
ATOM   10207 N  NH1 . ARG E  1 165 ? 4.582   63.755  2.085   1.00 33.46 ?  189  ARG E NH1 1 
ATOM   10208 N  NH2 . ARG E  1 165 ? 6.108   62.772  0.675   1.00 33.22 ?  189  ARG E NH2 1 
ATOM   10209 N  N   . MET E  1 166 ? 10.007  64.764  7.356   1.00 28.24 ?  190  MET E N   1 
ATOM   10210 C  CA  . MET E  1 166 ? 10.594  63.461  7.651   1.00 27.87 ?  190  MET E CA  1 
ATOM   10211 C  C   . MET E  1 166 ? 9.638   62.363  7.182   1.00 27.73 ?  190  MET E C   1 
ATOM   10212 O  O   . MET E  1 166 ? 8.486   62.319  7.617   1.00 27.61 ?  190  MET E O   1 
ATOM   10213 C  CB  . MET E  1 166 ? 10.882  63.307  9.148   1.00 27.74 ?  190  MET E CB  1 
ATOM   10214 C  CG  . MET E  1 166 ? 12.070  64.098  9.675   1.00 27.13 ?  190  MET E CG  1 
ATOM   10215 S  SD  . MET E  1 166 ? 13.640  63.681  8.881   1.00 26.16 ?  190  MET E SD  1 
ATOM   10216 C  CE  . MET E  1 166 ? 13.919  65.144  7.887   1.00 26.25 ?  190  MET E CE  1 
ATOM   10217 N  N   . PRO E  1 167 ? 10.109  61.475  6.288   1.00 27.65 ?  191  PRO E N   1 
ATOM   10218 C  CA  . PRO E  1 167 ? 9.251   60.424  5.753   1.00 27.44 ?  191  PRO E CA  1 
ATOM   10219 C  C   . PRO E  1 167 ? 8.783   59.467  6.843   1.00 27.25 ?  191  PRO E C   1 
ATOM   10220 O  O   . PRO E  1 167 ? 9.598   58.811  7.504   1.00 27.27 ?  191  PRO E O   1 
ATOM   10221 C  CB  . PRO E  1 167 ? 10.156  59.713  4.739   1.00 27.39 ?  191  PRO E CB  1 
ATOM   10222 C  CG  . PRO E  1 167 ? 11.182  60.736  4.384   1.00 27.76 ?  191  PRO E CG  1 
ATOM   10223 C  CD  . PRO E  1 167 ? 11.450  61.424  5.684   1.00 27.67 ?  191  PRO E CD  1 
ATOM   10224 N  N   . THR E  1 168 ? 7.469   59.425  7.037   1.00 26.90 ?  192  THR E N   1 
ATOM   10225 C  CA  . THR E  1 168 ? 6.852   58.572  8.045   1.00 26.69 ?  192  THR E CA  1 
ATOM   10226 C  C   . THR E  1 168 ? 6.301   57.317  7.367   1.00 26.50 ?  192  THR E C   1 
ATOM   10227 O  O   . THR E  1 168 ? 6.450   57.159  6.151   1.00 26.38 ?  192  THR E O   1 
ATOM   10228 C  CB  . THR E  1 168 ? 5.744   59.326  8.817   1.00 26.60 ?  192  THR E CB  1 
ATOM   10229 O  OG1 . THR E  1 168 ? 4.877   59.991  7.890   1.00 27.17 ?  192  THR E OG1 1 
ATOM   10230 C  CG2 . THR E  1 168 ? 6.356   60.363  9.741   1.00 26.55 ?  192  THR E CG2 1 
ATOM   10231 N  N   . ALA E  1 169 ? 5.678   56.428  8.140   1.00 26.26 ?  193  ALA E N   1 
ATOM   10232 C  CA  . ALA E  1 169 ? 5.136   55.180  7.588   1.00 26.30 ?  193  ALA E CA  1 
ATOM   10233 C  C   . ALA E  1 169 ? 4.132   55.427  6.455   1.00 26.30 ?  193  ALA E C   1 
ATOM   10234 O  O   . ALA E  1 169 ? 4.139   54.714  5.444   1.00 26.13 ?  193  ALA E O   1 
ATOM   10235 C  CB  . ALA E  1 169 ? 4.517   54.328  8.680   1.00 26.10 ?  193  ALA E CB  1 
ATOM   10236 N  N   . ASP E  1 170 ? 3.290   56.445  6.623   1.00 26.25 ?  194  ASP E N   1 
ATOM   10237 C  CA  . ASP E  1 170 ? 2.325   56.829  5.589   1.00 26.61 ?  194  ASP E CA  1 
ATOM   10238 C  C   . ASP E  1 170 ? 2.990   57.385  4.321   1.00 26.49 ?  194  ASP E C   1 
ATOM   10239 O  O   . ASP E  1 170 ? 2.435   57.265  3.232   1.00 26.72 ?  194  ASP E O   1 
ATOM   10240 C  CB  . ASP E  1 170 ? 1.263   57.794  6.142   1.00 26.62 ?  194  ASP E CB  1 
ATOM   10241 C  CG  . ASP E  1 170 ? 1.861   59.045  6.755   1.00 26.82 ?  194  ASP E CG  1 
ATOM   10242 O  OD1 . ASP E  1 170 ? 2.629   58.927  7.733   1.00 26.61 ?  194  ASP E OD1 1 
ATOM   10243 O  OD2 . ASP E  1 170 ? 1.552   60.151  6.267   1.00 27.93 -1 194  ASP E OD2 1 
ATOM   10244 N  N   . THR E  1 171 ? 4.170   57.989  4.467   1.00 26.49 ?  195  THR E N   1 
ATOM   10245 C  CA  . THR E  1 171 ? 4.937   58.469  3.316   1.00 26.46 ?  195  THR E CA  1 
ATOM   10246 C  C   . THR E  1 171 ? 5.375   57.289  2.448   1.00 26.29 ?  195  THR E C   1 
ATOM   10247 O  O   . THR E  1 171 ? 5.119   57.278  1.241   1.00 26.17 ?  195  THR E O   1 
ATOM   10248 C  CB  . THR E  1 171 ? 6.177   59.300  3.731   1.00 26.59 ?  195  THR E CB  1 
ATOM   10249 O  OG1 . THR E  1 171 ? 5.809   60.275  4.714   1.00 27.02 ?  195  THR E OG1 1 
ATOM   10250 C  CG2 . THR E  1 171 ? 6.781   60.011  2.523   1.00 27.10 ?  195  THR E CG2 1 
ATOM   10251 N  N   . CYS E  1 172 ? 6.022   56.300  3.075   1.00 26.00 ?  196  CYS E N   1 
ATOM   10252 C  CA  . CYS E  1 172 ? 6.433   55.065  2.400   1.00 25.66 ?  196  CYS E CA  1 
ATOM   10253 C  C   . CYS E  1 172 ? 5.231   54.325  1.823   1.00 26.04 ?  196  CYS E C   1 
ATOM   10254 O  O   . CYS E  1 172 ? 5.296   53.787  0.715   1.00 26.17 ?  196  CYS E O   1 
ATOM   10255 C  CB  . CYS E  1 172 ? 7.163   54.129  3.370   1.00 25.67 ?  196  CYS E CB  1 
ATOM   10256 S  SG  . CYS E  1 172 ? 8.562   54.825  4.262   1.00 23.70 ?  196  CYS E SG  1 
ATOM   10257 N  N   . GLY E  1 173 ? 4.139   54.311  2.588   1.00 26.24 ?  197  GLY E N   1 
ATOM   10258 C  CA  . GLY E  1 173 ? 2.924   53.589  2.236   1.00 26.55 ?  197  GLY E CA  1 
ATOM   10259 C  C   . GLY E  1 173 ? 2.195   54.103  1.010   1.00 26.83 ?  197  GLY E C   1 
ATOM   10260 O  O   . GLY E  1 173 ? 1.376   53.388  0.436   1.00 26.90 ?  197  GLY E O   1 
ATOM   10261 N  N   . THR E  1 174 ? 2.484   55.345  0.619   1.00 26.94 ?  198  THR E N   1 
ATOM   10262 C  CA  . THR E  1 174 ? 1.948   55.934  -0.610  1.00 27.05 ?  198  THR E CA  1 
ATOM   10263 C  C   . THR E  1 174 ? 2.353   55.083  -1.812  1.00 27.02 ?  198  THR E C   1 
ATOM   10264 O  O   . THR E  1 174 ? 1.567   54.887  -2.743  1.00 26.96 ?  198  THR E O   1 
ATOM   10265 C  CB  . THR E  1 174 ? 2.441   57.391  -0.798  1.00 27.15 ?  198  THR E CB  1 
ATOM   10266 O  OG1 . THR E  1 174 ? 2.204   58.135  0.404   1.00 27.81 ?  198  THR E OG1 1 
ATOM   10267 C  CG2 . THR E  1 174 ? 1.720   58.080  -1.959  1.00 26.90 ?  198  THR E CG2 1 
ATOM   10268 N  N   . CYS E  1 175 ? 3.579   54.570  -1.776  1.00 26.72 ?  199  CYS E N   1 
ATOM   10269 C  CA  . CYS E  1 175 ? 4.070   53.682  -2.818  1.00 26.48 ?  199  CYS E CA  1 
ATOM   10270 C  C   . CYS E  1 175 ? 3.965   52.230  -2.372  1.00 26.40 ?  199  CYS E C   1 
ATOM   10271 O  O   . CYS E  1 175 ? 3.397   51.392  -3.080  1.00 26.52 ?  199  CYS E O   1 
ATOM   10272 C  CB  . CYS E  1 175 ? 5.512   54.020  -3.162  1.00 26.39 ?  199  CYS E CB  1 
ATOM   10273 S  SG  . CYS E  1 175 ? 5.716   55.559  -4.062  1.00 26.38 ?  199  CYS E SG  1 
ATOM   10274 N  N   . HIS E  1 176 ? 4.504   51.951  -1.188  1.00 26.10 ?  200  HIS E N   1 
ATOM   10275 C  CA  . HIS E  1 176 ? 4.526   50.604  -0.635  1.00 25.80 ?  200  HIS E CA  1 
ATOM   10276 C  C   . HIS E  1 176 ? 3.255   50.318  0.172   1.00 25.71 ?  200  HIS E C   1 
ATOM   10277 O  O   . HIS E  1 176 ? 3.305   50.107  1.385   1.00 25.63 ?  200  HIS E O   1 
ATOM   10278 C  CB  . HIS E  1 176 ? 5.804   50.383  0.193   1.00 25.68 ?  200  HIS E CB  1 
ATOM   10279 C  CG  . HIS E  1 176 ? 7.076   50.620  -0.572  1.00 25.34 ?  200  HIS E CG  1 
ATOM   10280 N  ND1 . HIS E  1 176 ? 7.353   49.995  -1.769  1.00 25.30 ?  200  HIS E ND1 1 
ATOM   10281 C  CD2 . HIS E  1 176 ? 8.151   51.400  -0.301  1.00 25.26 ?  200  HIS E CD2 1 
ATOM   10282 C  CE1 . HIS E  1 176 ? 8.541   50.382  -2.203  1.00 24.98 ?  200  HIS E CE1 1 
ATOM   10283 N  NE2 . HIS E  1 176 ? 9.049   51.236  -1.332  1.00 25.17 ?  200  HIS E NE2 1 
ATOM   10284 N  N   . LEU E  1 177 ? 2.115   50.310  -0.523  1.00 25.73 ?  201  LEU E N   1 
ATOM   10285 C  CA  . LEU E  1 177 ? 0.805   50.112  0.110   1.00 25.64 ?  201  LEU E CA  1 
ATOM   10286 C  C   . LEU E  1 177 ? 0.685   48.728  0.738   1.00 25.27 ?  201  LEU E C   1 
ATOM   10287 O  O   . LEU E  1 177 ? 0.192   48.596  1.856   1.00 25.18 ?  201  LEU E O   1 
ATOM   10288 C  CB  . LEU E  1 177 ? -0.331  50.305  -0.902  1.00 25.69 ?  201  LEU E CB  1 
ATOM   10289 C  CG  . LEU E  1 177 ? -1.693  50.902  -0.497  1.00 26.55 ?  201  LEU E CG  1 
ATOM   10290 C  CD1 . LEU E  1 177 ? -2.790  50.317  -1.374  1.00 25.82 ?  201  LEU E CD1 1 
ATOM   10291 C  CD2 . LEU E  1 177 ? -2.064  50.745  0.979   1.00 26.14 ?  201  LEU E CD2 1 
ATOM   10292 N  N   . ARG E  1 178 ? 1.129   47.704  0.013   1.00 24.93 ?  202  ARG E N   1 
ATOM   10293 C  CA  . ARG E  1 178 ? 1.069   46.329  0.510   1.00 24.85 ?  202  ARG E CA  1 
ATOM   10294 C  C   . ARG E  1 178 ? 1.718   46.213  1.888   1.00 24.61 ?  202  ARG E C   1 
ATOM   10295 O  O   . ARG E  1 178 ? 1.090   45.749  2.840   1.00 24.77 ?  202  ARG E O   1 
ATOM   10296 C  CB  . ARG E  1 178 ? 1.724   45.345  -0.469  1.00 24.70 ?  202  ARG E CB  1 
ATOM   10297 C  CG  . ARG E  1 178 ? 1.687   43.892  0.024   1.00 24.92 ?  202  ARG E CG  1 
ATOM   10298 C  CD  . ARG E  1 178 ? 2.456   42.928  -0.874  1.00 25.13 ?  202  ARG E CD  1 
ATOM   10299 N  NE  . ARG E  1 178 ? 1.992   42.963  -2.261  1.00 25.63 ?  202  ARG E NE  1 
ATOM   10300 C  CZ  . ARG E  1 178 ? 0.987   42.241  -2.750  1.00 25.14 ?  202  ARG E CZ  1 
ATOM   10301 N  NH1 . ARG E  1 178 ? 0.303   41.407  -1.973  1.00 23.92 ?  202  ARG E NH1 1 
ATOM   10302 N  NH2 . ARG E  1 178 ? 0.666   42.362  -4.030  1.00 25.23 ?  202  ARG E NH2 1 
ATOM   10303 N  N   . GLU E  1 179 ? 2.968   46.656  1.983   1.00 24.32 ?  203  GLU E N   1 
ATOM   10304 C  CA  . GLU E  1 179 ? 3.751   46.522  3.208   1.00 24.24 ?  203  GLU E CA  1 
ATOM   10305 C  C   . GLU E  1 179 ? 3.177   47.350  4.357   1.00 23.98 ?  203  GLU E C   1 
ATOM   10306 O  O   . GLU E  1 179 ? 3.128   46.882  5.496   1.00 23.86 ?  203  GLU E O   1 
ATOM   10307 C  CB  . GLU E  1 179 ? 5.219   46.876  2.947   1.00 24.17 ?  203  GLU E CB  1 
ATOM   10308 C  CG  . GLU E  1 179 ? 5.956   45.857  2.079   1.00 24.47 ?  203  GLU E CG  1 
ATOM   10309 C  CD  . GLU E  1 179 ? 5.725   46.041  0.581   1.00 25.86 ?  203  GLU E CD  1 
ATOM   10310 O  OE1 . GLU E  1 179 ? 5.081   47.038  0.169   1.00 25.29 ?  203  GLU E OE1 1 
ATOM   10311 O  OE2 . GLU E  1 179 ? 6.202   45.180  -0.193  1.00 26.51 -1 203  GLU E OE2 1 
ATOM   10312 N  N   . PHE E  1 180 ? 2.737   48.568  4.040   1.00 23.71 ?  204  PHE E N   1 
ATOM   10313 C  CA  . PHE E  1 180 ? 2.112   49.465  5.013   1.00 23.71 ?  204  PHE E CA  1 
ATOM   10314 C  C   . PHE E  1 180 ? 0.808   48.871  5.545   1.00 23.67 ?  204  PHE E C   1 
ATOM   10315 O  O   . PHE E  1 180 ? 0.540   48.937  6.747   1.00 23.67 ?  204  PHE E O   1 
ATOM   10316 C  CB  . PHE E  1 180 ? 1.883   50.854  4.391   1.00 23.70 ?  204  PHE E CB  1 
ATOM   10317 C  CG  . PHE E  1 180 ? 1.211   51.853  5.312   1.00 23.89 ?  204  PHE E CG  1 
ATOM   10318 C  CD1 . PHE E  1 180 ? 1.691   52.081  6.600   1.00 23.21 ?  204  PHE E CD1 1 
ATOM   10319 C  CD2 . PHE E  1 180 ? 0.114   52.596  4.866   1.00 24.09 ?  204  PHE E CD2 1 
ATOM   10320 C  CE1 . PHE E  1 180 ? 1.071   53.013  7.445   1.00 23.41 ?  204  PHE E CE1 1 
ATOM   10321 C  CE2 . PHE E  1 180 ? -0.510  53.530  5.696   1.00 23.44 ?  204  PHE E CE2 1 
ATOM   10322 C  CZ  . PHE E  1 180 ? -0.029  53.738  6.993   1.00 23.36 ?  204  PHE E CZ  1 
ATOM   10323 N  N   . ALA E  1 181 ? 0.019   48.280  4.646   1.00 23.42 ?  205  ALA E N   1 
ATOM   10324 C  CA  . ALA E  1 181 ? -1.251  47.647  4.998   1.00 23.34 ?  205  ALA E CA  1 
ATOM   10325 C  C   . ALA E  1 181 ? -1.046  46.381  5.830   1.00 23.37 ?  205  ALA E C   1 
ATOM   10326 O  O   . ALA E  1 181 ? -1.736  46.174  6.834   1.00 23.08 ?  205  ALA E O   1 
ATOM   10327 C  CB  . ALA E  1 181 ? -2.059  47.337  3.740   1.00 23.32 ?  205  ALA E CB  1 
ATOM   10328 N  N   . GLU E  1 182 ? -0.108  45.535  5.401   1.00 23.29 ?  206  GLU E N   1 
ATOM   10329 C  CA  . GLU E  1 182 ? 0.274   44.347  6.172   1.00 23.42 ?  206  GLU E CA  1 
ATOM   10330 C  C   . GLU E  1 182 ? 0.706   44.719  7.591   1.00 23.25 ?  206  GLU E C   1 
ATOM   10331 O  O   . GLU E  1 182 ? 0.260   44.105  8.560   1.00 23.15 ?  206  GLU E O   1 
ATOM   10332 C  CB  . GLU E  1 182 ? 1.402   43.587  5.480   1.00 23.31 ?  206  GLU E CB  1 
ATOM   10333 C  CG  . GLU E  1 182 ? 1.005   42.896  4.193   1.00 23.81 ?  206  GLU E CG  1 
ATOM   10334 C  CD  . GLU E  1 182 ? 2.196   42.288  3.480   1.00 24.27 ?  206  GLU E CD  1 
ATOM   10335 O  OE1 . GLU E  1 182 ? 3.345   42.545  3.908   1.00 24.47 ?  206  GLU E OE1 1 
ATOM   10336 O  OE2 . GLU E  1 182 ? 1.986   41.555  2.490   1.00 23.87 -1 206  GLU E OE2 1 
ATOM   10337 N  N   . ARG E  1 183 ? 1.568   45.728  7.705   1.00 23.43 ?  207  ARG E N   1 
ATOM   10338 C  CA  . ARG E  1 183 ? 2.035   46.196  9.015   1.00 23.64 ?  207  ARG E CA  1 
ATOM   10339 C  C   . ARG E  1 183 ? 0.872   46.724  9.857   1.00 23.64 ?  207  ARG E C   1 
ATOM   10340 O  O   . ARG E  1 183 ? 0.767   46.404  11.039  1.00 23.60 ?  207  ARG E O   1 
ATOM   10341 C  CB  . ARG E  1 183 ? 3.131   47.262  8.869   1.00 23.55 ?  207  ARG E CB  1 
ATOM   10342 C  CG  . ARG E  1 183 ? 3.984   47.468  10.127  1.00 24.24 ?  207  ARG E CG  1 
ATOM   10343 C  CD  . ARG E  1 183 ? 3.360   48.468  11.118  1.00 25.17 ?  207  ARG E CD  1 
ATOM   10344 N  NE  . ARG E  1 183 ? 3.673   49.850  10.758  1.00 27.43 ?  207  ARG E NE  1 
ATOM   10345 C  CZ  . ARG E  1 183 ? 3.078   50.922  11.267  1.00 28.46 ?  207  ARG E CZ  1 
ATOM   10346 N  NH1 . ARG E  1 183 ? 2.121   50.794  12.170  1.00 30.67 ?  207  ARG E NH1 1 
ATOM   10347 N  NH2 . ARG E  1 183 ? 3.431   52.132  10.869  1.00 29.35 ?  207  ARG E NH2 1 
ATOM   10348 N  N   . GLU E  1 184 ? 0.001   47.521  9.240   1.00 23.60 ?  208  GLU E N   1 
ATOM   10349 C  CA  . GLU E  1 184 ? -1.168  48.062  9.934   1.00 23.85 ?  208  GLU E CA  1 
ATOM   10350 C  C   . GLU E  1 184 ? -2.167  46.987  10.375  1.00 23.94 ?  208  GLU E C   1 
ATOM   10351 O  O   . GLU E  1 184 ? -2.854  47.158  11.380  1.00 23.80 ?  208  GLU E O   1 
ATOM   10352 C  CB  . GLU E  1 184 ? -1.862  49.139  9.090   1.00 23.73 ?  208  GLU E CB  1 
ATOM   10353 C  CG  . GLU E  1 184 ? -1.156  50.488  9.115   1.00 23.83 ?  208  GLU E CG  1 
ATOM   10354 C  CD  . GLU E  1 184 ? -1.058  51.068  10.516  1.00 24.42 ?  208  GLU E CD  1 
ATOM   10355 O  OE1 . GLU E  1 184 ? -2.105  51.442  11.093  1.00 24.17 ?  208  GLU E OE1 1 
ATOM   10356 O  OE2 . GLU E  1 184 ? 0.068   51.140  11.044  1.00 22.91 -1 208  GLU E OE2 1 
ATOM   10357 N  N   . SER E  1 185 ? -2.222  45.879  9.635   1.00 24.13 ?  209  SER E N   1 
ATOM   10358 C  CA  . SER E  1 185 ? -3.118  44.761  9.950   1.00 24.39 ?  209  SER E CA  1 
ATOM   10359 C  C   . SER E  1 185 ? -2.833  44.096  11.307  1.00 24.60 ?  209  SER E C   1 
ATOM   10360 O  O   . SER E  1 185 ? -3.639  43.299  11.790  1.00 24.51 ?  209  SER E O   1 
ATOM   10361 C  CB  . SER E  1 185 ? -3.104  43.715  8.823   1.00 24.47 ?  209  SER E CB  1 
ATOM   10362 O  OG  . SER E  1 185 ? -1.950  42.890  8.862   1.00 24.22 ?  209  SER E OG  1 
ATOM   10363 N  N   . GLU E  1 186 ? -1.688  44.429  11.906  1.00 24.82 ?  210  GLU E N   1 
ATOM   10364 C  CA  . GLU E  1 186 ? -1.363  44.013  13.276  1.00 25.31 ?  210  GLU E CA  1 
ATOM   10365 C  C   . GLU E  1 186 ? -2.375  44.556  14.297  1.00 25.35 ?  210  GLU E C   1 
ATOM   10366 O  O   . GLU E  1 186 ? -2.655  43.905  15.305  1.00 25.66 ?  210  GLU E O   1 
ATOM   10367 C  CB  . GLU E  1 186 ? 0.071   44.425  13.652  1.00 25.30 ?  210  GLU E CB  1 
ATOM   10368 C  CG  . GLU E  1 186 ? 1.164   43.703  12.850  1.00 26.15 ?  210  GLU E CG  1 
ATOM   10369 C  CD  . GLU E  1 186 ? 2.580   44.197  13.148  1.00 27.40 ?  210  GLU E CD  1 
ATOM   10370 O  OE1 . GLU E  1 186 ? 2.746   45.250  13.801  1.00 27.74 ?  210  GLU E OE1 1 
ATOM   10371 O  OE2 . GLU E  1 186 ? 3.540   43.524  12.711  1.00 27.82 -1 210  GLU E OE2 1 
ATOM   10372 N  N   . ARG E  1 187 ? -2.922  45.742  14.026  1.00 25.52 ?  211  ARG E N   1 
ATOM   10373 C  CA  . ARG E  1 187 ? -3.995  46.329  14.843  1.00 25.84 ?  211  ARG E CA  1 
ATOM   10374 C  C   . ARG E  1 187 ? -5.222  45.416  14.915  1.00 26.11 ?  211  ARG E C   1 
ATOM   10375 O  O   . ARG E  1 187 ? -5.949  45.408  15.911  1.00 26.15 ?  211  ARG E O   1 
ATOM   10376 C  CB  . ARG E  1 187 ? -4.438  47.680  14.266  1.00 25.89 ?  211  ARG E CB  1 
ATOM   10377 C  CG  . ARG E  1 187 ? -3.393  48.779  14.275  1.00 25.37 ?  211  ARG E CG  1 
ATOM   10378 C  CD  . ARG E  1 187 ? -3.885  49.960  13.456  1.00 25.14 ?  211  ARG E CD  1 
ATOM   10379 N  NE  . ARG E  1 187 ? -3.029  51.136  13.607  1.00 24.82 ?  211  ARG E NE  1 
ATOM   10380 C  CZ  . ARG E  1 187 ? -3.191  52.074  14.536  1.00 24.96 ?  211  ARG E CZ  1 
ATOM   10381 N  NH1 . ARG E  1 187 ? -4.183  51.987  15.417  1.00 25.00 ?  211  ARG E NH1 1 
ATOM   10382 N  NH2 . ARG E  1 187 ? -2.354  53.102  14.587  1.00 24.36 ?  211  ARG E NH2 1 
ATOM   10383 N  N   . ASP E  1 188 ? -5.442  44.655  13.847  1.00 26.27 ?  212  ASP E N   1 
ATOM   10384 C  CA  . ASP E  1 188 ? -6.662  43.873  13.685  1.00 26.42 ?  212  ASP E CA  1 
ATOM   10385 C  C   . ASP E  1 188 ? -6.478  42.386  13.976  1.00 26.42 ?  212  ASP E C   1 
ATOM   10386 O  O   . ASP E  1 188 ? -7.446  41.696  14.296  1.00 26.61 ?  212  ASP E O   1 
ATOM   10387 C  CB  . ASP E  1 188 ? -7.214  44.069  12.270  1.00 26.42 ?  212  ASP E CB  1 
ATOM   10388 C  CG  . ASP E  1 188 ? -7.279  45.529  11.868  1.00 26.51 ?  212  ASP E CG  1 
ATOM   10389 O  OD1 . ASP E  1 188 ? -8.012  46.297  12.525  1.00 26.92 ?  212  ASP E OD1 1 
ATOM   10390 O  OD2 . ASP E  1 188 ? -6.592  45.913  10.896  1.00 27.39 -1 212  ASP E OD2 1 
ATOM   10391 N  N   . THR E  1 189 ? -5.246  41.895  13.862  1.00 26.42 ?  213  THR E N   1 
ATOM   10392 C  CA  . THR E  1 189 ? -4.969  40.469  14.057  1.00 26.59 ?  213  THR E CA  1 
ATOM   10393 C  C   . THR E  1 189 ? -4.555  40.140  15.489  1.00 26.86 ?  213  THR E C   1 
ATOM   10394 O  O   . THR E  1 189 ? -4.895  39.076  16.008  1.00 26.95 ?  213  THR E O   1 
ATOM   10395 C  CB  . THR E  1 189 ? -3.900  39.930  13.065  1.00 26.65 ?  213  THR E CB  1 
ATOM   10396 O  OG1 . THR E  1 189 ? -2.699  40.707  13.164  1.00 26.63 ?  213  THR E OG1 1 
ATOM   10397 C  CG2 . THR E  1 189 ? -4.416  39.982  11.634  1.00 26.11 ?  213  THR E CG2 1 
ATOM   10398 N  N   . MET E  1 190 ? -3.831  41.053  16.130  1.00 27.13 ?  214  MET E N   1 
ATOM   10399 C  CA  . MET E  1 190 ? -3.341  40.803  17.483  1.00 27.41 ?  214  MET E CA  1 
ATOM   10400 C  C   . MET E  1 190 ? -4.404  41.129  18.535  1.00 27.53 ?  214  MET E C   1 
ATOM   10401 O  O   . MET E  1 190 ? -4.304  42.122  19.258  1.00 27.70 ?  214  MET E O   1 
ATOM   10402 C  CB  . MET E  1 190 ? -2.023  41.546  17.751  1.00 27.36 ?  214  MET E CB  1 
ATOM   10403 C  CG  . MET E  1 190 ? -1.321  41.160  19.060  1.00 27.64 ?  214  MET E CG  1 
ATOM   10404 S  SD  . MET E  1 190 ? -0.834  39.422  19.202  1.00 28.51 ?  214  MET E SD  1 
ATOM   10405 C  CE  . MET E  1 190 ? -2.336  38.621  19.755  1.00 27.42 ?  214  MET E CE  1 
ATOM   10406 N  N   . VAL E  1 191 ? -5.421  40.277  18.606  1.00 27.68 ?  215  VAL E N   1 
ATOM   10407 C  CA  . VAL E  1 191 ? -6.480  40.419  19.594  1.00 27.88 ?  215  VAL E CA  1 
ATOM   10408 C  C   . VAL E  1 191 ? -6.444  39.202  20.513  1.00 27.76 ?  215  VAL E C   1 
ATOM   10409 O  O   . VAL E  1 191 ? -6.597  38.064  20.064  1.00 27.79 ?  215  VAL E O   1 
ATOM   10410 C  CB  . VAL E  1 191 ? -7.881  40.581  18.937  1.00 28.07 ?  215  VAL E CB  1 
ATOM   10411 C  CG1 . VAL E  1 191 ? -8.965  40.777  20.007  1.00 28.43 ?  215  VAL E CG1 1 
ATOM   10412 C  CG2 . VAL E  1 191 ? -7.884  41.761  17.964  1.00 28.08 ?  215  VAL E CG2 1 
ATOM   10413 N  N   . TRP E  1 192 ? -6.212  39.455  21.796  1.00 27.67 ?  216  TRP E N   1 
ATOM   10414 C  CA  . TRP E  1 192 ? -6.118  38.396  22.792  1.00 27.57 ?  216  TRP E CA  1 
ATOM   10415 C  C   . TRP E  1 192 ? -7.508  37.886  23.202  1.00 27.63 ?  216  TRP E C   1 
ATOM   10416 O  O   . TRP E  1 192 ? -8.451  38.670  23.286  1.00 27.51 ?  216  TRP E O   1 
ATOM   10417 C  CB  . TRP E  1 192 ? -5.302  38.879  23.995  1.00 27.49 ?  216  TRP E CB  1 
ATOM   10418 C  CG  . TRP E  1 192 ? -3.859  39.062  23.638  1.00 26.94 ?  216  TRP E CG  1 
ATOM   10419 C  CD1 . TRP E  1 192 ? -3.271  40.196  23.156  1.00 26.38 ?  216  TRP E CD1 1 
ATOM   10420 C  CD2 . TRP E  1 192 ? -2.829  38.067  23.692  1.00 26.20 ?  216  TRP E CD2 1 
ATOM   10421 N  NE1 . TRP E  1 192 ? -1.937  39.973  22.917  1.00 25.96 ?  216  TRP E NE1 1 
ATOM   10422 C  CE2 . TRP E  1 192 ? -1.638  38.675  23.239  1.00 25.84 ?  216  TRP E CE2 1 
ATOM   10423 C  CE3 . TRP E  1 192 ? -2.796  36.722  24.089  1.00 26.01 ?  216  TRP E CE3 1 
ATOM   10424 C  CZ2 . TRP E  1 192 ? -0.421  37.985  23.171  1.00 25.59 ?  216  TRP E CZ2 1 
ATOM   10425 C  CZ3 . TRP E  1 192 ? -1.581  36.034  24.017  1.00 25.90 ?  216  TRP E CZ3 1 
ATOM   10426 C  CH2 . TRP E  1 192 ? -0.414  36.669  23.562  1.00 25.59 ?  216  TRP E CH2 1 
ATOM   10427 N  N   . PRO E  1 193 ? -7.637  36.566  23.443  1.00 27.86 ?  217  PRO E N   1 
ATOM   10428 C  CA  . PRO E  1 193 ? -8.950  35.979  23.744  1.00 28.04 ?  217  PRO E CA  1 
ATOM   10429 C  C   . PRO E  1 193 ? -9.553  36.494  25.046  1.00 28.26 ?  217  PRO E C   1 
ATOM   10430 O  O   . PRO E  1 193 ? -10.772 36.459  25.208  1.00 28.54 ?  217  PRO E O   1 
ATOM   10431 C  CB  . PRO E  1 193 ? -8.654  34.478  23.873  1.00 28.05 ?  217  PRO E CB  1 
ATOM   10432 C  CG  . PRO E  1 193 ? -7.314  34.278  23.252  1.00 27.98 ?  217  PRO E CG  1 
ATOM   10433 C  CD  . PRO E  1 193 ? -6.569  35.550  23.460  1.00 27.74 ?  217  PRO E CD  1 
ATOM   10434 N  N   . ASN E  1 194 ? -8.707  36.968  25.959  1.00 28.10 ?  218  ASN E N   1 
ATOM   10435 C  CA  . ASN E  1 194 ? -9.166  37.442  27.262  1.00 28.20 ?  218  ASN E CA  1 
ATOM   10436 C  C   . ASN E  1 194 ? -8.558  38.785  27.647  1.00 27.99 ?  218  ASN E C   1 
ATOM   10437 O  O   . ASN E  1 194 ? -8.466  39.119  28.830  1.00 27.94 ?  218  ASN E O   1 
ATOM   10438 C  CB  . ASN E  1 194 ? -8.876  36.390  28.340  1.00 28.24 ?  218  ASN E CB  1 
ATOM   10439 C  CG  . ASN E  1 194 ? -9.320  34.999  27.927  1.00 28.64 ?  218  ASN E CG  1 
ATOM   10440 O  OD1 . ASN E  1 194 ? -8.492  34.130  27.657  1.00 28.80 ?  218  ASN E OD1 1 
ATOM   10441 N  ND2 . ASN E  1 194 ? -10.633 34.788  27.855  1.00 28.88 ?  218  ASN E ND2 1 
ATOM   10442 N  N   . GLY E  1 195 ? -8.150  39.550  26.636  1.00 27.88 ?  219  GLY E N   1 
ATOM   10443 C  CA  . GLY E  1 195 ? -7.538  40.861  26.832  1.00 27.51 ?  219  GLY E CA  1 
ATOM   10444 C  C   . GLY E  1 195 ? -6.278  40.841  27.682  1.00 27.55 ?  219  GLY E C   1 
ATOM   10445 O  O   . GLY E  1 195 ? -6.060  41.750  28.492  1.00 27.48 ?  219  GLY E O   1 
ATOM   10446 N  N   . GLN E  1 196 ? -5.456  39.804  27.496  1.00 27.32 ?  220  GLN E N   1 
ATOM   10447 C  CA  . GLN E  1 196 ? -4.169  39.666  28.193  1.00 27.07 ?  220  GLN E CA  1 
ATOM   10448 C  C   . GLN E  1 196 ? -3.285  40.891  27.957  1.00 26.89 ?  220  GLN E C   1 
ATOM   10449 O  O   . GLN E  1 196 ? -2.606  41.369  28.867  1.00 26.94 ?  220  GLN E O   1 
ATOM   10450 C  CB  . GLN E  1 196 ? -3.439  38.397  27.734  1.00 26.95 ?  220  GLN E CB  1 
ATOM   10451 C  CG  . GLN E  1 196 ? -3.947  37.092  28.354  1.00 26.81 ?  220  GLN E CG  1 
ATOM   10452 C  CD  . GLN E  1 196 ? -5.185  36.508  27.666  1.00 26.52 ?  220  GLN E CD  1 
ATOM   10453 O  OE1 . GLN E  1 196 ? -5.739  37.095  26.735  1.00 26.08 ?  220  GLN E OE1 1 
ATOM   10454 N  NE2 . GLN E  1 196 ? -5.617  35.335  28.131  1.00 25.80 ?  220  GLN E NE2 1 
ATOM   10455 N  N   . TRP E  1 197 ? -3.303  41.374  26.719  1.00 26.74 ?  221  TRP E N   1 
ATOM   10456 C  CA  . TRP E  1 197 ? -2.661  42.621  26.323  1.00 26.65 ?  221  TRP E CA  1 
ATOM   10457 C  C   . TRP E  1 197 ? -3.731  43.465  25.637  1.00 26.47 ?  221  TRP E C   1 
ATOM   10458 O  O   . TRP E  1 197 ? -4.739  42.916  25.177  1.00 26.31 ?  221  TRP E O   1 
ATOM   10459 C  CB  . TRP E  1 197 ? -1.517  42.345  25.340  1.00 26.67 ?  221  TRP E CB  1 
ATOM   10460 C  CG  . TRP E  1 197 ? -0.358  41.595  25.933  1.00 27.42 ?  221  TRP E CG  1 
ATOM   10461 C  CD1 . TRP E  1 197 ? -0.206  40.240  26.004  1.00 27.64 ?  221  TRP E CD1 1 
ATOM   10462 C  CD2 . TRP E  1 197 ? 0.813   42.162  26.530  1.00 27.69 ?  221  TRP E CD2 1 
ATOM   10463 N  NE1 . TRP E  1 197 ? 0.983   39.929  26.617  1.00 27.60 ?  221  TRP E NE1 1 
ATOM   10464 C  CE2 . TRP E  1 197 ? 1.631   41.090  26.947  1.00 28.02 ?  221  TRP E CE2 1 
ATOM   10465 C  CE3 . TRP E  1 197 ? 1.250   43.473  26.756  1.00 28.42 ?  221  TRP E CE3 1 
ATOM   10466 C  CZ2 . TRP E  1 197 ? 2.864   41.288  27.579  1.00 28.58 ?  221  TRP E CZ2 1 
ATOM   10467 C  CZ3 . TRP E  1 197 ? 2.477   43.670  27.388  1.00 28.88 ?  221  TRP E CZ3 1 
ATOM   10468 C  CH2 . TRP E  1 197 ? 3.268   42.581  27.789  1.00 28.53 ?  221  TRP E CH2 1 
ATOM   10469 N  N   . PRO E  1 198 ? -3.528  44.799  25.565  1.00 26.38 ?  222  PRO E N   1 
ATOM   10470 C  CA  . PRO E  1 198 ? -4.448  45.642  24.795  1.00 26.19 ?  222  PRO E CA  1 
ATOM   10471 C  C   . PRO E  1 198 ? -4.550  45.179  23.344  1.00 25.96 ?  222  PRO E C   1 
ATOM   10472 O  O   . PRO E  1 198 ? -3.561  44.697  22.782  1.00 26.11 ?  222  PRO E O   1 
ATOM   10473 C  CB  . PRO E  1 198 ? -3.788  47.021  24.858  1.00 26.14 ?  222  PRO E CB  1 
ATOM   10474 C  CG  . PRO E  1 198 ? -3.026  47.005  26.134  1.00 26.52 ?  222  PRO E CG  1 
ATOM   10475 C  CD  . PRO E  1 198 ? -2.501  45.603  26.255  1.00 26.35 ?  222  PRO E CD  1 
ATOM   10476 N  N   . ALA E  1 199 ? -5.737  45.316  22.758  1.00 25.62 ?  223  ALA E N   1 
ATOM   10477 C  CA  . ALA E  1 199 ? -5.983  44.916  21.371  1.00 25.39 ?  223  ALA E CA  1 
ATOM   10478 C  C   . ALA E  1 199 ? -4.972  45.546  20.416  1.00 25.03 ?  223  ALA E C   1 
ATOM   10479 O  O   . ALA E  1 199 ? -4.734  46.760  20.454  1.00 24.94 ?  223  ALA E O   1 
ATOM   10480 C  CB  . ALA E  1 199 ? -7.411  45.271  20.953  1.00 25.47 ?  223  ALA E CB  1 
ATOM   10481 N  N   . GLY E  1 200 ? -4.371  44.712  19.573  1.00 24.49 ?  224  GLY E N   1 
ATOM   10482 C  CA  . GLY E  1 200 ? -3.359  45.173  18.623  1.00 24.06 ?  224  GLY E CA  1 
ATOM   10483 C  C   . GLY E  1 200 ? -1.948  45.166  19.184  1.00 23.63 ?  224  GLY E C   1 
ATOM   10484 O  O   . GLY E  1 200 ? -1.012  45.593  18.515  1.00 23.67 ?  224  GLY E O   1 
ATOM   10485 N  N   . ARG E  1 201 ? -1.792  44.674  20.409  1.00 23.42 ?  225  ARG E N   1 
ATOM   10486 C  CA  . ARG E  1 201 ? -0.488  44.658  21.067  1.00 23.18 ?  225  ARG E CA  1 
ATOM   10487 C  C   . ARG E  1 201 ? -0.142  43.290  21.678  1.00 22.76 ?  225  ARG E C   1 
ATOM   10488 O  O   . ARG E  1 201 ? -1.042  42.527  22.041  1.00 22.57 ?  225  ARG E O   1 
ATOM   10489 C  CB  . ARG E  1 201 ? -0.417  45.774  22.114  1.00 23.30 ?  225  ARG E CB  1 
ATOM   10490 C  CG  . ARG E  1 201 ? -0.233  47.166  21.497  1.00 23.92 ?  225  ARG E CG  1 
ATOM   10491 C  CD  . ARG E  1 201 ? -0.710  48.270  22.425  1.00 24.47 ?  225  ARG E CD  1 
ATOM   10492 N  NE  . ARG E  1 201 ? 0.098   48.354  23.640  1.00 25.75 ?  225  ARG E NE  1 
ATOM   10493 C  CZ  . ARG E  1 201 ? -0.132  49.197  24.644  1.00 26.10 ?  225  ARG E CZ  1 
ATOM   10494 N  NH1 . ARG E  1 201 ? -1.153  50.049  24.597  1.00 26.28 ?  225  ARG E NH1 1 
ATOM   10495 N  NH2 . ARG E  1 201 ? 0.664   49.189  25.701  1.00 26.14 ?  225  ARG E NH2 1 
ATOM   10496 N  N   . PRO E  1 202 ? 1.166   42.965  21.769  1.00 22.35 ?  226  PRO E N   1 
ATOM   10497 C  CA  . PRO E  1 202 ? 2.308   43.750  21.267  1.00 22.10 ?  226  PRO E CA  1 
ATOM   10498 C  C   . PRO E  1 202 ? 2.438   43.683  19.748  1.00 21.84 ?  226  PRO E C   1 
ATOM   10499 O  O   . PRO E  1 202 ? 2.068   42.671  19.141  1.00 22.11 ?  226  PRO E O   1 
ATOM   10500 C  CB  . PRO E  1 202 ? 3.523   43.079  21.924  1.00 21.84 ?  226  PRO E CB  1 
ATOM   10501 C  CG  . PRO E  1 202 ? 2.968   42.198  23.005  1.00 22.37 ?  226  PRO E CG  1 
ATOM   10502 C  CD  . PRO E  1 202 ? 1.614   41.786  22.527  1.00 22.26 ?  226  PRO E CD  1 
ATOM   10503 N  N   . SER E  1 203 ? 2.959   44.754  19.150  1.00 21.36 ?  227  SER E N   1 
ATOM   10504 C  CA  . SER E  1 203 ? 3.165   44.832  17.701  1.00 21.26 ?  227  SER E CA  1 
ATOM   10505 C  C   . SER E  1 203 ? 4.087   45.989  17.332  1.00 21.07 ?  227  SER E C   1 
ATOM   10506 O  O   . SER E  1 203 ? 4.352   46.871  18.153  1.00 20.81 ?  227  SER E O   1 
ATOM   10507 C  CB  . SER E  1 203 ? 1.827   45.017  16.975  1.00 21.19 ?  227  SER E CB  1 
ATOM   10508 O  OG  . SER E  1 203 ? 1.257   46.281  17.269  1.00 21.27 ?  227  SER E OG  1 
ATOM   10509 N  N   . HIS E  1 204 ? 4.560   45.981  16.089  1.00 20.96 ?  228  HIS E N   1 
ATOM   10510 C  CA  . HIS E  1 204 ? 5.293   47.113  15.539  1.00 21.18 ?  228  HIS E CA  1 
ATOM   10511 C  C   . HIS E  1 204 ? 4.337   48.252  15.170  1.00 21.21 ?  228  HIS E C   1 
ATOM   10512 O  O   . HIS E  1 204 ? 4.724   49.427  15.171  1.00 21.06 ?  228  HIS E O   1 
ATOM   10513 C  CB  . HIS E  1 204 ? 6.128   46.693  14.322  1.00 21.17 ?  228  HIS E CB  1 
ATOM   10514 C  CG  . HIS E  1 204 ? 7.281   45.790  14.657  1.00 21.34 ?  228  HIS E CG  1 
ATOM   10515 N  ND1 . HIS E  1 204 ? 7.774   44.854  13.772  1.00 21.28 ?  228  HIS E ND1 1 
ATOM   10516 C  CD2 . HIS E  1 204 ? 8.031   45.675  15.778  1.00 20.69 ?  228  HIS E CD2 1 
ATOM   10517 C  CE1 . HIS E  1 204 ? 8.783   44.210  14.331  1.00 20.92 ?  228  HIS E CE1 1 
ATOM   10518 N  NE2 . HIS E  1 204 ? 8.958   44.686  15.552  1.00 21.21 ?  228  HIS E NE2 1 
ATOM   10519 N  N   . ALA E  1 205 ? 3.090   47.897  14.864  1.00 21.34 ?  229  ALA E N   1 
ATOM   10520 C  CA  . ALA E  1 205 ? 2.076   48.876  14.473  1.00 21.48 ?  229  ALA E CA  1 
ATOM   10521 C  C   . ALA E  1 205 ? 1.774   49.869  15.592  1.00 21.45 ?  229  ALA E C   1 
ATOM   10522 O  O   . ALA E  1 205 ? 1.444   51.028  15.332  1.00 21.44 ?  229  ALA E O   1 
ATOM   10523 C  CB  . ALA E  1 205 ? 0.800   48.178  14.009  1.00 21.41 ?  229  ALA E CB  1 
ATOM   10524 N  N   . LEU E  1 206 ? 1.913   49.413  16.834  1.00 21.39 ?  230  LEU E N   1 
ATOM   10525 C  CA  . LEU E  1 206 ? 1.595   50.235  17.994  1.00 21.29 ?  230  LEU E CA  1 
ATOM   10526 C  C   . LEU E  1 206 ? 2.733   50.339  19.018  1.00 21.47 ?  230  LEU E C   1 
ATOM   10527 O  O   . LEU E  1 206 ? 2.481   50.571  20.204  1.00 21.12 ?  230  LEU E O   1 
ATOM   10528 C  CB  . LEU E  1 206 ? 0.319   49.715  18.663  1.00 21.41 ?  230  LEU E CB  1 
ATOM   10529 C  CG  . LEU E  1 206 ? -0.995  49.921  17.905  1.00 21.19 ?  230  LEU E CG  1 
ATOM   10530 C  CD1 . LEU E  1 206 ? -2.089  49.069  18.513  1.00 21.53 ?  230  LEU E CD1 1 
ATOM   10531 C  CD2 . LEU E  1 206 ? -1.396  51.398  17.889  1.00 21.63 ?  230  LEU E CD2 1 
ATOM   10532 N  N   . ASP E  1 207 ? 3.978   50.185  18.560  1.00 21.46 ?  231  ASP E N   1 
ATOM   10533 C  CA  . ASP E  1 207 ? 5.131   50.260  19.462  1.00 21.85 ?  231  ASP E CA  1 
ATOM   10534 C  C   . ASP E  1 207 ? 5.330   51.634  20.107  1.00 21.83 ?  231  ASP E C   1 
ATOM   10535 O  O   . ASP E  1 207 ? 5.670   51.711  21.283  1.00 21.84 ?  231  ASP E O   1 
ATOM   10536 C  CB  . ASP E  1 207 ? 6.428   49.747  18.802  1.00 21.81 ?  231  ASP E CB  1 
ATOM   10537 C  CG  . ASP E  1 207 ? 6.891   50.601  17.636  1.00 22.68 ?  231  ASP E CG  1 
ATOM   10538 O  OD1 . ASP E  1 207 ? 6.088   51.371  17.079  1.00 23.74 ?  231  ASP E OD1 1 
ATOM   10539 O  OD2 . ASP E  1 207 ? 8.078   50.488  17.263  1.00 24.58 -1 231  ASP E OD2 1 
ATOM   10540 N  N   . TYR E  1 208 ? 5.103   52.704  19.345  1.00 21.87 ?  232  TYR E N   1 
ATOM   10541 C  CA  . TYR E  1 208 ? 5.258   54.064  19.861  1.00 22.24 ?  232  TYR E CA  1 
ATOM   10542 C  C   . TYR E  1 208 ? 4.132   54.454  20.815  1.00 22.31 ?  232  TYR E C   1 
ATOM   10543 O  O   . TYR E  1 208 ? 4.375   55.091  21.845  1.00 22.52 ?  232  TYR E O   1 
ATOM   10544 C  CB  . TYR E  1 208 ? 5.371   55.086  18.721  1.00 22.26 ?  232  TYR E CB  1 
ATOM   10545 C  CG  . TYR E  1 208 ? 5.638   56.496  19.206  1.00 22.26 ?  232  TYR E CG  1 
ATOM   10546 C  CD1 . TYR E  1 208 ? 6.875   56.851  19.746  1.00 22.26 ?  232  TYR E CD1 1 
ATOM   10547 C  CD2 . TYR E  1 208 ? 4.650   57.476  19.127  1.00 22.22 ?  232  TYR E CD2 1 
ATOM   10548 C  CE1 . TYR E  1 208 ? 7.120   58.153  20.198  1.00 22.41 ?  232  TYR E CE1 1 
ATOM   10549 C  CE2 . TYR E  1 208 ? 4.884   58.775  19.570  1.00 22.07 ?  232  TYR E CE2 1 
ATOM   10550 C  CZ  . TYR E  1 208 ? 6.118   59.107  20.102  1.00 22.53 ?  232  TYR E CZ  1 
ATOM   10551 O  OH  . TYR E  1 208 ? 6.341   60.392  20.546  1.00 22.79 ?  232  TYR E OH  1 
ATOM   10552 N  N   . THR E  1 209 ? 2.907   54.077  20.454  1.00 22.35 ?  233  THR E N   1 
ATOM   10553 C  CA  . THR E  1 209 ? 1.745   54.237  21.321  1.00 22.44 ?  233  THR E CA  1 
ATOM   10554 C  C   . THR E  1 209 ? 1.978   53.531  22.658  1.00 22.45 ?  233  THR E C   1 
ATOM   10555 O  O   . THR E  1 209 ? 1.730   54.109  23.710  1.00 22.66 ?  233  THR E O   1 
ATOM   10556 C  CB  . THR E  1 209 ? 0.458   53.711  20.635  1.00 22.33 ?  233  THR E CB  1 
ATOM   10557 O  OG1 . THR E  1 209 ? 0.206   54.477  19.451  1.00 22.73 ?  233  THR E OG1 1 
ATOM   10558 C  CG2 . THR E  1 209 ? -0.756  53.813  21.564  1.00 22.56 ?  233  THR E CG2 1 
ATOM   10559 N  N   . ALA E  1 210 ? 2.469   52.293  22.613  1.00 22.44 ?  234  ALA E N   1 
ATOM   10560 C  CA  . ALA E  1 210 ? 2.776   51.541  23.837  1.00 22.55 ?  234  ALA E CA  1 
ATOM   10561 C  C   . ALA E  1 210 ? 3.773   52.302  24.718  1.00 22.47 ?  234  ALA E C   1 
ATOM   10562 O  O   . ALA E  1 210 ? 3.605   52.387  25.940  1.00 22.45 ?  234  ALA E O   1 
ATOM   10563 C  CB  . ALA E  1 210 ? 3.304   50.155  23.493  1.00 22.14 ?  234  ALA E CB  1 
ATOM   10564 N  N   . ASN E  1 211 ? 4.792   52.858  24.066  1.00 22.44 ?  235  ASN E N   1 
ATOM   10565 C  CA  . ASN E  1 211 ? 5.853   53.636  24.698  1.00 22.51 ?  235  ASN E CA  1 
ATOM   10566 C  C   . ASN E  1 211 ? 5.332   54.881  25.430  1.00 22.39 ?  235  ASN E C   1 
ATOM   10567 O  O   . ASN E  1 211 ? 5.621   55.076  26.612  1.00 22.30 ?  235  ASN E O   1 
ATOM   10568 C  CB  . ASN E  1 211 ? 6.894   54.020  23.631  1.00 22.51 ?  235  ASN E CB  1 
ATOM   10569 C  CG  . ASN E  1 211 ? 8.072   54.788  24.198  1.00 23.45 ?  235  ASN E CG  1 
ATOM   10570 O  OD1 . ASN E  1 211 ? 8.894   54.240  24.933  1.00 24.43 ?  235  ASN E OD1 1 
ATOM   10571 N  ND2 . ASN E  1 211 ? 8.169   56.065  23.842  1.00 24.13 ?  235  ASN E ND2 1 
ATOM   10572 N  N   . ILE E  1 212 ? 4.554   55.704  24.729  1.00 22.13 ?  236  ILE E N   1 
ATOM   10573 C  CA  . ILE E  1 212 ? 4.036   56.957  25.291  1.00 22.07 ?  236  ILE E CA  1 
ATOM   10574 C  C   . ILE E  1 212 ? 2.863   56.744  26.251  1.00 22.10 ?  236  ILE E C   1 
ATOM   10575 O  O   . ILE E  1 212 ? 2.492   57.656  26.995  1.00 22.00 ?  236  ILE E O   1 
ATOM   10576 C  CB  . ILE E  1 212 ? 3.637   57.984  24.188  1.00 21.92 ?  236  ILE E CB  1 
ATOM   10577 C  CG1 . ILE E  1 212 ? 2.406   57.499  23.402  1.00 21.82 ?  236  ILE E CG1 1 
ATOM   10578 C  CG2 . ILE E  1 212 ? 4.826   58.277  23.272  1.00 21.92 ?  236  ILE E CG2 1 
ATOM   10579 C  CD1 . ILE E  1 212 ? 1.914   58.466  22.330  1.00 21.85 ?  236  ILE E CD1 1 
ATOM   10580 N  N   . GLU E  1 213 ? 2.283   55.546  26.228  1.00 22.14 ?  237  GLU E N   1 
ATOM   10581 C  CA  . GLU E  1 213 ? 1.207   55.208  27.156  1.00 22.41 ?  237  GLU E CA  1 
ATOM   10582 C  C   . GLU E  1 213 ? 1.725   54.448  28.373  1.00 22.36 ?  237  GLU E C   1 
ATOM   10583 O  O   . GLU E  1 213 ? 0.941   53.933  29.176  1.00 22.48 ?  237  GLU E O   1 
ATOM   10584 C  CB  . GLU E  1 213 ? 0.079   54.433  26.459  1.00 22.58 ?  237  GLU E CB  1 
ATOM   10585 C  CG  . GLU E  1 213 ? -0.668  55.226  25.385  1.00 23.10 ?  237  GLU E CG  1 
ATOM   10586 C  CD  . GLU E  1 213 ? -1.467  56.403  25.931  1.00 24.51 ?  237  GLU E CD  1 
ATOM   10587 O  OE1 . GLU E  1 213 ? -1.812  56.414  27.136  1.00 25.03 ?  237  GLU E OE1 1 
ATOM   10588 O  OE2 . GLU E  1 213 ? -1.767  57.320  25.138  1.00 24.88 -1 237  GLU E OE2 1 
ATOM   10589 N  N   . THR E  1 214 ? 3.047   54.386  28.503  1.00 22.21 ?  238  THR E N   1 
ATOM   10590 C  CA  . THR E  1 214 ? 3.680   53.825  29.688  1.00 22.18 ?  238  THR E CA  1 
ATOM   10591 C  C   . THR E  1 214 ? 3.868   54.952  30.692  1.00 22.20 ?  238  THR E C   1 
ATOM   10592 O  O   . THR E  1 214 ? 4.477   55.978  30.371  1.00 22.07 ?  238  THR E O   1 
ATOM   10593 C  CB  . THR E  1 214 ? 5.030   53.175  29.346  1.00 22.18 ?  238  THR E CB  1 
ATOM   10594 O  OG1 . THR E  1 214 ? 4.824   52.137  28.376  1.00 21.87 ?  238  THR E OG1 1 
ATOM   10595 C  CG2 . THR E  1 214 ? 5.682   52.586  30.592  1.00 22.13 ?  238  THR E CG2 1 
ATOM   10596 N  N   . THR E  1 215 ? 3.342   54.755  31.901  1.00 22.35 ?  239  THR E N   1 
ATOM   10597 C  CA  . THR E  1 215 ? 3.288   55.828  32.903  1.00 22.55 ?  239  THR E CA  1 
ATOM   10598 C  C   . THR E  1 215 ? 4.637   56.476  33.269  1.00 22.51 ?  239  THR E C   1 
ATOM   10599 O  O   . THR E  1 215 ? 4.723   57.705  33.287  1.00 22.82 ?  239  THR E O   1 
ATOM   10600 C  CB  . THR E  1 215 ? 2.490   55.424  34.182  1.00 22.76 ?  239  THR E CB  1 
ATOM   10601 O  OG1 . THR E  1 215 ? 1.246   54.819  33.808  1.00 22.50 ?  239  THR E OG1 1 
ATOM   10602 C  CG2 . THR E  1 215 ? 2.187   56.652  35.029  1.00 22.59 ?  239  THR E CG2 1 
ATOM   10603 N  N   . VAL E  1 216 ? 5.679   55.688  33.551  1.00 22.36 ?  240  VAL E N   1 
ATOM   10604 C  CA  . VAL E  1 216 ? 6.986   56.295  33.892  1.00 22.29 ?  240  VAL E CA  1 
ATOM   10605 C  C   . VAL E  1 216 ? 7.599   57.077  32.754  1.00 22.21 ?  240  VAL E C   1 
ATOM   10606 O  O   . VAL E  1 216 ? 8.276   58.074  32.991  1.00 22.00 ?  240  VAL E O   1 
ATOM   10607 C  CB  . VAL E  1 216 ? 8.102   55.312  34.325  1.00 22.39 ?  240  VAL E CB  1 
ATOM   10608 C  CG1 . VAL E  1 216 ? 8.436   55.487  35.788  1.00 22.62 ?  240  VAL E CG1 1 
ATOM   10609 C  CG2 . VAL E  1 216 ? 7.825   53.884  33.912  1.00 21.92 ?  240  VAL E CG2 1 
ATOM   10610 N  N   . TRP E  1 217 ? 7.397   56.600  31.529  1.00 22.13 ?  241  TRP E N   1 
ATOM   10611 C  CA  . TRP E  1 217 ? 7.951   57.270  30.363  1.00 22.15 ?  241  TRP E CA  1 
ATOM   10612 C  C   . TRP E  1 217 ? 7.458   58.712  30.319  1.00 22.18 ?  241  TRP E C   1 
ATOM   10613 O  O   . TRP E  1 217 ? 8.234   59.632  30.062  1.00 22.15 ?  241  TRP E O   1 
ATOM   10614 C  CB  . TRP E  1 217 ? 7.589   56.533  29.076  1.00 21.98 ?  241  TRP E CB  1 
ATOM   10615 C  CG  . TRP E  1 217 ? 8.184   57.183  27.869  1.00 21.90 ?  241  TRP E CG  1 
ATOM   10616 C  CD1 . TRP E  1 217 ? 9.379   56.888  27.284  1.00 21.52 ?  241  TRP E CD1 1 
ATOM   10617 C  CD2 . TRP E  1 217 ? 7.619   58.262  27.113  1.00 21.82 ?  241  TRP E CD2 1 
ATOM   10618 N  NE1 . TRP E  1 217 ? 9.592   57.710  26.201  1.00 22.27 ?  241  TRP E NE1 1 
ATOM   10619 C  CE2 . TRP E  1 217 ? 8.527   58.564  26.076  1.00 22.03 ?  241  TRP E CE2 1 
ATOM   10620 C  CE3 . TRP E  1 217 ? 6.430   58.999  27.209  1.00 21.44 ?  241  TRP E CE3 1 
ATOM   10621 C  CZ2 . TRP E  1 217 ? 8.284   59.573  25.140  1.00 21.92 ?  241  TRP E CZ2 1 
ATOM   10622 C  CZ3 . TRP E  1 217 ? 6.189   59.998  26.282  1.00 21.62 ?  241  TRP E CZ3 1 
ATOM   10623 C  CH2 . TRP E  1 217 ? 7.113   60.277  25.259  1.00 21.87 ?  241  TRP E CH2 1 
ATOM   10624 N  N   . ALA E  1 218 ? 6.165   58.894  30.585  1.00 22.23 ?  242  ALA E N   1 
ATOM   10625 C  CA  . ALA E  1 218 ? 5.551   60.216  30.603  1.00 22.27 ?  242  ALA E CA  1 
ATOM   10626 C  C   . ALA E  1 218 ? 5.817   60.965  31.909  1.00 22.29 ?  242  ALA E C   1 
ATOM   10627 O  O   . ALA E  1 218 ? 5.915   62.190  31.907  1.00 22.43 ?  242  ALA E O   1 
ATOM   10628 C  CB  . ALA E  1 218 ? 4.050   60.109  30.340  1.00 22.12 ?  242  ALA E CB  1 
ATOM   10629 N  N   . ALA E  1 219 ? 5.950   60.229  33.012  1.00 22.40 ?  243  ALA E N   1 
ATOM   10630 C  CA  . ALA E  1 219 ? 6.028   60.846  34.344  1.00 22.44 ?  243  ALA E CA  1 
ATOM   10631 C  C   . ALA E  1 219 ? 7.440   61.231  34.805  1.00 22.42 ?  243  ALA E C   1 
ATOM   10632 O  O   . ALA E  1 219 ? 7.601   62.208  35.536  1.00 22.30 ?  243  ALA E O   1 
ATOM   10633 C  CB  . ALA E  1 219 ? 5.356   59.962  35.382  1.00 22.27 ?  243  ALA E CB  1 
ATOM   10634 N  N   . MET E  1 220 ? 8.451   60.473  34.382  1.00 22.44 ?  244  MET E N   1 
ATOM   10635 C  CA  . MET E  1 220 ? 9.828   60.689  34.860  1.00 22.32 ?  244  MET E CA  1 
ATOM   10636 C  C   . MET E  1 220 ? 10.437  61.989  34.325  1.00 22.47 ?  244  MET E C   1 
ATOM   10637 O  O   . MET E  1 220 ? 10.186  62.358  33.179  1.00 22.45 ?  244  MET E O   1 
ATOM   10638 C  CB  . MET E  1 220 ? 10.726  59.491  34.531  1.00 22.20 ?  244  MET E CB  1 
ATOM   10639 C  CG  . MET E  1 220 ? 11.057  59.314  33.051  1.00 21.88 ?  244  MET E CG  1 
ATOM   10640 S  SD  . MET E  1 220 ? 11.748  57.693  32.674  1.00 22.66 ?  244  MET E SD  1 
ATOM   10641 C  CE  . MET E  1 220 ? 13.436  57.873  33.257  1.00 20.40 ?  244  MET E CE  1 
ATOM   10642 N  N   . PRO E  1 221 ? 11.233  62.688  35.162  1.00 22.65 ?  245  PRO E N   1 
ATOM   10643 C  CA  . PRO E  1 221 ? 11.860  63.951  34.754  1.00 22.66 ?  245  PRO E CA  1 
ATOM   10644 C  C   . PRO E  1 221 ? 13.027  63.779  33.781  1.00 22.74 ?  245  PRO E C   1 
ATOM   10645 O  O   . PRO E  1 221 ? 13.320  64.693  33.004  1.00 22.73 ?  245  PRO E O   1 
ATOM   10646 C  CB  . PRO E  1 221 ? 12.351  64.543  36.078  1.00 22.59 ?  245  PRO E CB  1 
ATOM   10647 C  CG  . PRO E  1 221 ? 12.537  63.368  36.974  1.00 22.70 ?  245  PRO E CG  1 
ATOM   10648 C  CD  . PRO E  1 221 ? 11.459  62.401  36.593  1.00 22.67 ?  245  PRO E CD  1 
ATOM   10649 N  N   . GLN E  1 222 ? 13.674  62.615  33.818  1.00 22.75 ?  246  GLN E N   1 
ATOM   10650 C  CA  . GLN E  1 222 ? 14.834  62.343  32.971  1.00 22.73 ?  246  GLN E CA  1 
ATOM   10651 C  C   . GLN E  1 222 ? 14.388  62.046  31.539  1.00 22.74 ?  246  GLN E C   1 
ATOM   10652 O  O   . GLN E  1 222 ? 14.262  60.882  31.145  1.00 22.79 ?  246  GLN E O   1 
ATOM   10653 C  CB  . GLN E  1 222 ? 15.668  61.182  33.536  1.00 22.63 ?  246  GLN E CB  1 
ATOM   10654 C  CG  . GLN E  1 222 ? 16.205  61.391  34.954  1.00 21.98 ?  246  GLN E CG  1 
ATOM   10655 C  CD  . GLN E  1 222 ? 15.201  61.027  36.042  1.00 22.07 ?  246  GLN E CD  1 
ATOM   10656 O  OE1 . GLN E  1 222 ? 14.073  60.619  35.757  1.00 21.84 ?  246  GLN E OE1 1 
ATOM   10657 N  NE2 . GLN E  1 222 ? 15.614  61.168  37.301  1.00 21.69 ?  246  GLN E NE2 1 
ATOM   10658 N  N   . ARG E  1 223 ? 14.157  63.106  30.767  1.00 22.63 ?  247  ARG E N   1 
ATOM   10659 C  CA  . ARG E  1 223 ? 13.605  62.973  29.412  1.00 22.74 ?  247  ARG E CA  1 
ATOM   10660 C  C   . ARG E  1 223 ? 14.534  62.234  28.449  1.00 22.82 ?  247  ARG E C   1 
ATOM   10661 O  O   . ARG E  1 223 ? 14.079  61.440  27.617  1.00 22.64 ?  247  ARG E O   1 
ATOM   10662 C  CB  . ARG E  1 223 ? 13.229  64.344  28.829  1.00 22.62 ?  247  ARG E CB  1 
ATOM   10663 C  CG  . ARG E  1 223 ? 12.117  65.092  29.583  1.00 22.47 ?  247  ARG E CG  1 
ATOM   10664 C  CD  . ARG E  1 223 ? 10.931  64.194  29.933  1.00 21.91 ?  247  ARG E CD  1 
ATOM   10665 N  NE  . ARG E  1 223 ? 10.433  63.419  28.791  1.00 21.69 ?  247  ARG E NE  1 
ATOM   10666 C  CZ  . ARG E  1 223 ? 9.650   62.350  28.905  1.00 21.53 ?  247  ARG E CZ  1 
ATOM   10667 N  NH1 . ARG E  1 223 ? 9.271   61.929  30.105  1.00 21.37 ?  247  ARG E NH1 1 
ATOM   10668 N  NH2 . ARG E  1 223 ? 9.244   61.701  27.823  1.00 21.51 ?  247  ARG E NH2 1 
ATOM   10669 N  N   . GLU E  1 224 ? 15.830  62.509  28.569  1.00 22.61 ?  248  GLU E N   1 
ATOM   10670 C  CA  . GLU E  1 224 ? 16.830  61.917  27.691  1.00 22.84 ?  248  GLU E CA  1 
ATOM   10671 C  C   . GLU E  1 224 ? 16.986  60.413  27.951  1.00 22.97 ?  248  GLU E C   1 
ATOM   10672 O  O   . GLU E  1 224 ? 17.322  59.655  27.040  1.00 23.06 ?  248  GLU E O   1 
ATOM   10673 C  CB  . GLU E  1 224 ? 18.165  62.664  27.819  1.00 22.76 ?  248  GLU E CB  1 
ATOM   10674 C  CG  . GLU E  1 224 ? 18.199  64.033  27.103  1.00 22.29 ?  248  GLU E CG  1 
ATOM   10675 C  CD  . GLU E  1 224 ? 17.353  65.131  27.773  1.00 22.60 ?  248  GLU E CD  1 
ATOM   10676 O  OE1 . GLU E  1 224 ? 16.986  65.000  28.962  1.00 21.82 ?  248  GLU E OE1 1 
ATOM   10677 O  OE2 . GLU E  1 224 ? 17.059  66.142  27.098  1.00 21.92 -1 248  GLU E OE2 1 
ATOM   10678 N  N   . VAL E  1 225 ? 16.719  59.990  29.186  1.00 23.08 ?  249  VAL E N   1 
ATOM   10679 C  CA  . VAL E  1 225 ? 16.669  58.562  29.522  1.00 23.22 ?  249  VAL E CA  1 
ATOM   10680 C  C   . VAL E  1 225 ? 15.428  57.924  28.889  1.00 23.33 ?  249  VAL E C   1 
ATOM   10681 O  O   . VAL E  1 225 ? 15.534  56.922  28.178  1.00 23.17 ?  249  VAL E O   1 
ATOM   10682 C  CB  . VAL E  1 225 ? 16.673  58.313  31.054  1.00 23.09 ?  249  VAL E CB  1 
ATOM   10683 C  CG1 . VAL E  1 225 ? 16.560  56.822  31.362  1.00 23.31 ?  249  VAL E CG1 1 
ATOM   10684 C  CG2 . VAL E  1 225 ? 17.929  58.897  31.693  1.00 23.20 ?  249  VAL E CG2 1 
ATOM   10685 N  N   . ALA E  1 226 ? 14.261  58.519  29.144  1.00 23.42 ?  250  ALA E N   1 
ATOM   10686 C  CA  . ALA E  1 226 ? 12.993  58.043  28.581  1.00 23.49 ?  250  ALA E CA  1 
ATOM   10687 C  C   . ALA E  1 226 ? 13.038  57.893  27.062  1.00 23.47 ?  250  ALA E C   1 
ATOM   10688 O  O   . ALA E  1 226 ? 12.453  56.963  26.512  1.00 23.65 ?  250  ALA E O   1 
ATOM   10689 C  CB  . ALA E  1 226 ? 11.847  58.962  28.990  1.00 23.53 ?  250  ALA E CB  1 
ATOM   10690 N  N   . GLU E  1 227 ? 13.748  58.801  26.395  1.00 23.54 ?  251  GLU E N   1 
ATOM   10691 C  CA  . GLU E  1 227 ? 13.798  58.840  24.932  1.00 23.73 ?  251  GLU E CA  1 
ATOM   10692 C  C   . GLU E  1 227 ? 14.665  57.724  24.321  1.00 23.53 ?  251  GLU E C   1 
ATOM   10693 O  O   . GLU E  1 227 ? 14.581  57.448  23.121  1.00 23.57 ?  251  GLU E O   1 
ATOM   10694 C  CB  . GLU E  1 227 ? 14.255  60.223  24.450  1.00 23.95 ?  251  GLU E CB  1 
ATOM   10695 C  CG  . GLU E  1 227 ? 13.795  60.592  23.027  1.00 25.57 ?  251  GLU E CG  1 
ATOM   10696 C  CD  . GLU E  1 227 ? 12.285  60.858  22.901  1.00 26.76 ?  251  GLU E CD  1 
ATOM   10697 O  OE1 . GLU E  1 227 ? 11.547  60.746  23.905  1.00 26.38 ?  251  GLU E OE1 1 
ATOM   10698 O  OE2 . GLU E  1 227 ? 11.838  61.190  21.780  1.00 28.31 -1 251  GLU E OE2 1 
ATOM   10699 N  N   . GLY E  1 228 ? 15.494  57.097  25.150  1.00 23.16 ?  252  GLY E N   1 
ATOM   10700 C  CA  . GLY E  1 228 ? 16.175  55.865  24.775  1.00 22.84 ?  252  GLY E CA  1 
ATOM   10701 C  C   . GLY E  1 228 ? 15.168  54.756  24.523  1.00 22.63 ?  252  GLY E C   1 
ATOM   10702 O  O   . GLY E  1 228 ? 15.332  53.957  23.600  1.00 22.36 ?  252  GLY E O   1 
ATOM   10703 N  N   . CYS E  1 229 ? 14.119  54.721  25.344  1.00 22.25 ?  253  CYS E N   1 
ATOM   10704 C  CA  . CYS E  1 229 ? 13.012  53.787  25.153  1.00 22.14 ?  253  CYS E CA  1 
ATOM   10705 C  C   . CYS E  1 229 ? 12.312  54.058  23.828  1.00 21.76 ?  253  CYS E C   1 
ATOM   10706 O  O   . CYS E  1 229 ? 12.012  53.131  23.080  1.00 21.88 ?  253  CYS E O   1 
ATOM   10707 C  CB  . CYS E  1 229 ? 12.007  53.894  26.302  1.00 22.09 ?  253  CYS E CB  1 
ATOM   10708 S  SG  . CYS E  1 229 ? 12.746  53.794  27.933  1.00 22.96 ?  253  CYS E SG  1 
ATOM   10709 N  N   . THR E  1 230 ? 12.074  55.338  23.545  1.00 21.60 ?  254  THR E N   1 
ATOM   10710 C  CA  . THR E  1 230 ? 11.459  55.785  22.298  1.00 21.35 ?  254  THR E CA  1 
ATOM   10711 C  C   . THR E  1 230 ? 12.208  55.260  21.062  1.00 21.39 ?  254  THR E C   1 
ATOM   10712 O  O   . THR E  1 230 ? 11.584  54.823  20.094  1.00 21.32 ?  254  THR E O   1 
ATOM   10713 C  CB  . THR E  1 230 ? 11.363  57.335  22.252  1.00 21.38 ?  254  THR E CB  1 
ATOM   10714 O  OG1 . THR E  1 230 ? 10.672  57.813  23.416  1.00 21.34 ?  254  THR E OG1 1 
ATOM   10715 C  CG2 . THR E  1 230 ? 10.627  57.807  21.004  1.00 20.97 ?  254  THR E CG2 1 
ATOM   10716 N  N   . MET E  1 231 ? 13.536  55.295  21.108  1.00 21.29 ?  255  MET E N   1 
ATOM   10717 C  CA  . MET E  1 231 ? 14.371  54.865  19.979  1.00 21.60 ?  255  MET E CA  1 
ATOM   10718 C  C   . MET E  1 231 ? 14.166  53.394  19.574  1.00 21.43 ?  255  MET E C   1 
ATOM   10719 O  O   . MET E  1 231 ? 14.338  53.042  18.408  1.00 21.22 ?  255  MET E O   1 
ATOM   10720 C  CB  . MET E  1 231 ? 15.847  55.177  20.253  1.00 21.82 ?  255  MET E CB  1 
ATOM   10721 C  CG  . MET E  1 231 ? 16.155  56.684  20.245  1.00 23.18 ?  255  MET E CG  1 
ATOM   10722 S  SD  . MET E  1 231 ? 17.887  57.143  20.500  1.00 27.13 ?  255  MET E SD  1 
ATOM   10723 C  CE  . MET E  1 231 ? 18.673  56.334  19.113  1.00 24.15 ?  255  MET E CE  1 
ATOM   10724 N  N   . CYS E  1 232 ? 13.783  52.553  20.536  1.00 21.30 ?  256  CYS E N   1 
ATOM   10725 C  CA  . CYS E  1 232 ? 13.411  51.162  20.263  1.00 21.25 ?  256  CYS E CA  1 
ATOM   10726 C  C   . CYS E  1 232 ? 11.936  50.995  19.883  1.00 21.31 ?  256  CYS E C   1 
ATOM   10727 O  O   . CYS E  1 232 ? 11.502  49.892  19.550  1.00 21.57 ?  256  CYS E O   1 
ATOM   10728 C  CB  . CYS E  1 232 ? 13.675  50.293  21.485  1.00 21.18 ?  256  CYS E CB  1 
ATOM   10729 S  SG  . CYS E  1 232 ? 15.390  50.046  21.946  1.00 20.93 ?  256  CYS E SG  1 
ATOM   10730 N  N   . HIS E  1 233 ? 11.172  52.082  19.939  1.00 21.23 ?  257  HIS E N   1 
ATOM   10731 C  CA  . HIS E  1 233 ? 9.717   52.019  19.802  1.00 21.27 ?  257  HIS E CA  1 
ATOM   10732 C  C   . HIS E  1 233 ? 9.202   52.953  18.685  1.00 21.21 ?  257  HIS E C   1 
ATOM   10733 O  O   . HIS E  1 233 ? 8.123   53.524  18.803  1.00 21.15 ?  257  HIS E O   1 
ATOM   10734 C  CB  . HIS E  1 233 ? 9.044   52.364  21.152  1.00 21.20 ?  257  HIS E CB  1 
ATOM   10735 C  CG  . HIS E  1 233 ? 9.068   51.254  22.171  1.00 21.31 ?  257  HIS E CG  1 
ATOM   10736 N  ND1 . HIS E  1 233 ? 7.980   50.440  22.404  1.00 21.05 ?  257  HIS E ND1 1 
ATOM   10737 C  CD2 . HIS E  1 233 ? 10.027  50.850  23.043  1.00 21.33 ?  257  HIS E CD2 1 
ATOM   10738 C  CE1 . HIS E  1 233 ? 8.275   49.570  23.355  1.00 21.51 ?  257  HIS E CE1 1 
ATOM   10739 N  NE2 . HIS E  1 233 ? 9.510   49.798  23.768  1.00 21.36 ?  257  HIS E NE2 1 
ATOM   10740 N  N   . THR E  1 234 ? 9.958   53.091  17.595  1.00 21.18 ?  258  THR E N   1 
ATOM   10741 C  CA  . THR E  1 234 ? 9.582   54.029  16.522  1.00 21.22 ?  258  THR E CA  1 
ATOM   10742 C  C   . THR E  1 234 ? 9.005   53.413  15.239  1.00 21.25 ?  258  THR E C   1 
ATOM   10743 O  O   . THR E  1 234 ? 8.703   54.144  14.293  1.00 21.30 ?  258  THR E O   1 
ATOM   10744 C  CB  . THR E  1 234 ? 10.761  54.951  16.120  1.00 21.20 ?  258  THR E CB  1 
ATOM   10745 O  OG1 . THR E  1 234 ? 11.925  54.159  15.862  1.00 20.85 ?  258  THR E OG1 1 
ATOM   10746 C  CG2 . THR E  1 234 ? 11.063  55.956  17.218  1.00 20.96 ?  258  THR E CG2 1 
ATOM   10747 N  N   . ASN E  1 235 ? 8.857   52.089  15.197  1.00 21.30 ?  259  ASN E N   1 
ATOM   10748 C  CA  . ASN E  1 235 ? 8.350   51.410  13.995  1.00 21.54 ?  259  ASN E CA  1 
ATOM   10749 C  C   . ASN E  1 235 ? 6.987   51.924  13.541  1.00 21.62 ?  259  ASN E C   1 
ATOM   10750 O  O   . ASN E  1 235 ? 6.737   52.046  12.341  1.00 21.75 ?  259  ASN E O   1 
ATOM   10751 C  CB  . ASN E  1 235 ? 8.311   49.890  14.185  1.00 21.50 ?  259  ASN E CB  1 
ATOM   10752 C  CG  . ASN E  1 235 ? 9.688   49.296  14.390  1.00 21.61 ?  259  ASN E CG  1 
ATOM   10753 O  OD1 . ASN E  1 235 ? 10.576  49.445  13.546  1.00 20.59 ?  259  ASN E OD1 1 
ATOM   10754 N  ND2 . ASN E  1 235 ? 9.876   48.618  15.519  1.00 21.16 ?  259  ASN E ND2 1 
ATOM   10755 N  N   . GLN E  1 236 ? 6.119   52.227  14.508  1.00 21.83 ?  260  GLN E N   1 
ATOM   10756 C  CA  . GLN E  1 236 ? 4.837   52.878  14.250  1.00 21.83 ?  260  GLN E CA  1 
ATOM   10757 C  C   . GLN E  1 236 ? 5.026   54.103  13.362  1.00 21.88 ?  260  GLN E C   1 
ATOM   10758 O  O   . GLN E  1 236 ? 4.313   54.280  12.374  1.00 21.99 ?  260  GLN E O   1 
ATOM   10759 C  CB  . GLN E  1 236 ? 4.182   53.289  15.574  1.00 21.97 ?  260  GLN E CB  1 
ATOM   10760 C  CG  . GLN E  1 236 ? 2.785   53.923  15.460  1.00 22.17 ?  260  GLN E CG  1 
ATOM   10761 C  CD  . GLN E  1 236 ? 2.034   53.919  16.782  1.00 23.09 ?  260  GLN E CD  1 
ATOM   10762 O  OE1 . GLN E  1 236 ? 2.484   53.332  17.768  1.00 23.71 ?  260  GLN E OE1 1 
ATOM   10763 N  NE2 . GLN E  1 236 ? 0.881   54.572  16.807  1.00 23.91 ?  260  GLN E NE2 1 
ATOM   10764 N  N   . ASN E  1 237 ? 6.015   54.923  13.705  1.00 21.82 ?  261  ASN E N   1 
ATOM   10765 C  CA  . ASN E  1 237 ? 6.189   56.231  13.084  1.00 21.88 ?  261  ASN E CA  1 
ATOM   10766 C  C   . ASN E  1 237 ? 7.022   56.233  11.806  1.00 21.94 ?  261  ASN E C   1 
ATOM   10767 O  O   . ASN E  1 237 ? 6.736   56.996  10.889  1.00 22.09 ?  261  ASN E O   1 
ATOM   10768 C  CB  . ASN E  1 237 ? 6.778   57.219  14.097  1.00 21.83 ?  261  ASN E CB  1 
ATOM   10769 C  CG  . ASN E  1 237 ? 5.901   57.386  15.326  1.00 21.76 ?  261  ASN E CG  1 
ATOM   10770 O  OD1 . ASN E  1 237 ? 4.709   57.095  15.291  1.00 21.64 ?  261  ASN E OD1 1 
ATOM   10771 N  ND2 . ASN E  1 237 ? 6.493   57.857  16.420  1.00 22.23 ?  261  ASN E ND2 1 
ATOM   10772 N  N   . LYS E  1 238 ? 8.054   55.394  11.756  1.00 21.73 ?  262  LYS E N   1 
ATOM   10773 C  CA  . LYS E  1 238 ? 8.973   55.378  10.619  1.00 21.63 ?  262  LYS E CA  1 
ATOM   10774 C  C   . LYS E  1 238 ? 9.376   53.959  10.219  1.00 21.49 ?  262  LYS E C   1 
ATOM   10775 O  O   . LYS E  1 238 ? 9.520   53.076  11.068  1.00 21.33 ?  262  LYS E O   1 
ATOM   10776 C  CB  . LYS E  1 238 ? 10.205  56.259  10.893  1.00 21.77 ?  262  LYS E CB  1 
ATOM   10777 C  CG  . LYS E  1 238 ? 11.019  55.879  12.134  1.00 21.56 ?  262  LYS E CG  1 
ATOM   10778 C  CD  . LYS E  1 238 ? 12.082  56.930  12.443  1.00 22.29 ?  262  LYS E CD  1 
ATOM   10779 C  CE  . LYS E  1 238 ? 13.089  56.430  13.476  1.00 22.40 ?  262  LYS E CE  1 
ATOM   10780 N  NZ  . LYS E  1 238 ? 14.037  55.442  12.883  1.00 22.67 ?  262  LYS E NZ  1 
ATOM   10781 N  N   . CYS E  1 239 ? 9.551   53.759  8.917   1.00 21.60 ?  263  CYS E N   1 
ATOM   10782 C  CA  . CYS E  1 239 ? 9.788   52.439  8.340   1.00 21.65 ?  263  CYS E CA  1 
ATOM   10783 C  C   . CYS E  1 239 ? 11.265  52.092  8.101   1.00 21.66 ?  263  CYS E C   1 
ATOM   10784 O  O   . CYS E  1 239 ? 11.568  51.151  7.351   1.00 21.89 ?  263  CYS E O   1 
ATOM   10785 C  CB  . CYS E  1 239 ? 9.001   52.305  7.031   1.00 21.78 ?  263  CYS E CB  1 
ATOM   10786 S  SG  . CYS E  1 239 ? 7.213   52.194  7.245   1.00 22.45 ?  263  CYS E SG  1 
ATOM   10787 N  N   . ASP E  1 240 ? 12.178  52.818  8.746   1.00 21.38 ?  264  ASP E N   1 
ATOM   10788 C  CA  . ASP E  1 240 ? 13.610  52.660  8.458   1.00 21.51 ?  264  ASP E CA  1 
ATOM   10789 C  C   . ASP E  1 240 ? 14.443  51.954  9.540   1.00 21.55 ?  264  ASP E C   1 
ATOM   10790 O  O   . ASP E  1 240 ? 15.665  52.095  9.565   1.00 21.42 ?  264  ASP E O   1 
ATOM   10791 C  CB  . ASP E  1 240 ? 14.242  54.012  8.089   1.00 21.28 ?  264  ASP E CB  1 
ATOM   10792 C  CG  . ASP E  1 240 ? 14.224  55.009  9.239   1.00 22.03 ?  264  ASP E CG  1 
ATOM   10793 O  OD1 . ASP E  1 240 ? 13.446  54.826  10.207  1.00 22.20 ?  264  ASP E OD1 1 
ATOM   10794 O  OD2 . ASP E  1 240 ? 14.992  55.990  9.166   1.00 21.59 -1 264  ASP E OD2 1 
ATOM   10795 N  N   . ASN E  1 241 ? 13.793  51.184  10.411  1.00 21.60 ?  265  ASN E N   1 
ATOM   10796 C  CA  . ASN E  1 241 ? 14.503  50.516  11.508  1.00 21.77 ?  265  ASN E CA  1 
ATOM   10797 C  C   . ASN E  1 241 ? 15.086  49.131  11.167  1.00 21.86 ?  265  ASN E C   1 
ATOM   10798 O  O   . ASN E  1 241 ? 16.090  48.735  11.748  1.00 21.92 ?  265  ASN E O   1 
ATOM   10799 C  CB  . ASN E  1 241 ? 13.644  50.464  12.786  1.00 21.56 ?  265  ASN E CB  1 
ATOM   10800 C  CG  . ASN E  1 241 ? 13.342  51.858  13.367  1.00 22.02 ?  265  ASN E CG  1 
ATOM   10801 O  OD1 . ASN E  1 241 ? 14.192  52.750  13.367  1.00 22.29 ?  265  ASN E OD1 1 
ATOM   10802 N  ND2 . ASN E  1 241 ? 12.126  52.035  13.876  1.00 21.37 ?  265  ASN E ND2 1 
ATOM   10803 N  N   . CYS E  1 242 ? 14.468  48.398  10.239  1.00 22.02 ?  266  CYS E N   1 
ATOM   10804 C  CA  . CYS E  1 242 ? 15.025  47.109  9.793   1.00 22.32 ?  266  CYS E CA  1 
ATOM   10805 C  C   . CYS E  1 242 ? 15.823  47.259  8.498   1.00 22.49 ?  266  CYS E C   1 
ATOM   10806 O  O   . CYS E  1 242 ? 16.971  46.811  8.412   1.00 22.63 ?  266  CYS E O   1 
ATOM   10807 C  CB  . CYS E  1 242 ? 13.933  46.048  9.630   1.00 22.20 ?  266  CYS E CB  1 
ATOM   10808 S  SG  . CYS E  1 242 ? 12.975  45.745  11.126  1.00 22.50 ?  266  CYS E SG  1 
ATOM   10809 N  N   . HIS E  1 243 ? 15.193  47.856  7.489   1.00 22.68 ?  267  HIS E N   1 
ATOM   10810 C  CA  . HIS E  1 243 ? 15.902  48.335  6.303   1.00 22.52 ?  267  HIS E CA  1 
ATOM   10811 C  C   . HIS E  1 243 ? 16.147  49.838  6.483   1.00 22.62 ?  267  HIS E C   1 
ATOM   10812 O  O   . HIS E  1 243 ? 15.218  50.642  6.396   1.00 22.58 ?  267  HIS E O   1 
ATOM   10813 C  CB  . HIS E  1 243 ? 15.165  47.997  4.982   1.00 22.32 ?  267  HIS E CB  1 
ATOM   10814 C  CG  . HIS E  1 243 ? 13.675  47.831  5.110   1.00 22.01 ?  267  HIS E CG  1 
ATOM   10815 N  ND1 . HIS E  1 243 ? 12.817  48.895  5.276   1.00 21.98 ?  267  HIS E ND1 1 
ATOM   10816 C  CD2 . HIS E  1 243 ? 12.889  46.726  5.039   1.00 21.62 ?  267  HIS E CD2 1 
ATOM   10817 C  CE1 . HIS E  1 243 ? 11.571  48.453  5.331   1.00 21.88 ?  267  HIS E CE1 1 
ATOM   10818 N  NE2 . HIS E  1 243 ? 11.585  47.139  5.192   1.00 21.71 ?  267  HIS E NE2 1 
ATOM   10819 N  N   . THR E  1 244 ? 17.400  50.198  6.765   1.00 22.62 ?  268  THR E N   1 
ATOM   10820 C  CA  . THR E  1 244 ? 17.761  51.555  7.201   1.00 22.75 ?  268  THR E CA  1 
ATOM   10821 C  C   . THR E  1 244 ? 17.935  52.548  6.058   1.00 22.97 ?  268  THR E C   1 
ATOM   10822 O  O   . THR E  1 244 ? 18.217  52.159  4.921   1.00 22.94 ?  268  THR E O   1 
ATOM   10823 C  CB  . THR E  1 244 ? 19.080  51.568  8.040   1.00 22.74 ?  268  THR E CB  1 
ATOM   10824 O  OG1 . THR E  1 244 ? 20.157  51.017  7.267   1.00 22.63 ?  268  THR E OG1 1 
ATOM   10825 C  CG2 . THR E  1 244 ? 18.921  50.781  9.339   1.00 22.08 ?  268  THR E CG2 1 
ATOM   10826 N  N   . ARG E  1 245 ? 17.771  53.831  6.381   1.00 23.14 ?  269  ARG E N   1 
ATOM   10827 C  CA  . ARG E  1 245 ? 18.143  54.926  5.490   1.00 23.39 ?  269  ARG E CA  1 
ATOM   10828 C  C   . ARG E  1 245 ? 19.667  54.955  5.331   1.00 23.62 ?  269  ARG E C   1 
ATOM   10829 O  O   . ARG E  1 245 ? 20.385  54.620  6.279   1.00 23.28 ?  269  ARG E O   1 
ATOM   10830 C  CB  . ARG E  1 245 ? 17.622  56.271  6.035   1.00 23.37 ?  269  ARG E CB  1 
ATOM   10831 C  CG  . ARG E  1 245 ? 18.263  56.774  7.349   1.00 23.32 ?  269  ARG E CG  1 
ATOM   10832 C  CD  . ARG E  1 245 ? 17.592  58.068  7.786   1.00 24.04 ?  269  ARG E CD  1 
ATOM   10833 N  NE  . ARG E  1 245 ? 18.123  58.668  9.016   1.00 24.94 ?  269  ARG E NE  1 
ATOM   10834 C  CZ  . ARG E  1 245 ? 17.730  58.364  10.254  1.00 25.25 ?  269  ARG E CZ  1 
ATOM   10835 N  NH1 . ARG E  1 245 ? 16.809  57.435  10.469  1.00 24.90 ?  269  ARG E NH1 1 
ATOM   10836 N  NH2 . ARG E  1 245 ? 18.272  58.992  11.294  1.00 25.39 ?  269  ARG E NH2 1 
ATOM   10837 N  N   . HIS E  1 246 ? 20.174  55.325  4.151   1.00 24.10 ?  270  HIS E N   1 
ATOM   10838 C  CA  . HIS E  1 246 ? 19.376  55.675  2.968   1.00 24.52 ?  270  HIS E CA  1 
ATOM   10839 C  C   . HIS E  1 246 ? 19.533  54.635  1.848   1.00 24.93 ?  270  HIS E C   1 
ATOM   10840 O  O   . HIS E  1 246 ? 19.178  54.888  0.691   1.00 24.89 ?  270  HIS E O   1 
ATOM   10841 C  CB  . HIS E  1 246 ? 19.758  57.074  2.456   1.00 24.30 ?  270  HIS E CB  1 
ATOM   10842 C  CG  . HIS E  1 246 ? 19.038  58.195  3.147   1.00 24.27 ?  270  HIS E CG  1 
ATOM   10843 N  ND1 . HIS E  1 246 ? 19.489  58.764  4.318   1.00 23.83 ?  270  HIS E ND1 1 
ATOM   10844 C  CD2 . HIS E  1 246 ? 17.901  58.855  2.823   1.00 24.14 ?  270  HIS E CD2 1 
ATOM   10845 C  CE1 . HIS E  1 246 ? 18.659  59.726  4.686   1.00 24.33 ?  270  HIS E CE1 1 
ATOM   10846 N  NE2 . HIS E  1 246 ? 17.685  59.804  3.795   1.00 24.96 ?  270  HIS E NE2 1 
ATOM   10847 N  N   . GLU E  1 247 ? 20.066  53.468  2.206   1.00 25.26 ?  271  GLU E N   1 
ATOM   10848 C  CA  . GLU E  1 247 ? 20.217  52.353  1.275   1.00 25.64 ?  271  GLU E CA  1 
ATOM   10849 C  C   . GLU E  1 247 ? 18.885  51.617  1.081   1.00 25.18 ?  271  GLU E C   1 
ATOM   10850 O  O   . GLU E  1 247 ? 18.598  51.113  -0.010  1.00 25.06 ?  271  GLU E O   1 
ATOM   10851 C  CB  . GLU E  1 247 ? 21.302  51.395  1.782   1.00 26.17 ?  271  GLU E CB  1 
ATOM   10852 C  CG  . GLU E  1 247 ? 21.751  50.328  0.785   1.00 28.90 ?  271  GLU E CG  1 
ATOM   10853 C  CD  . GLU E  1 247 ? 23.033  49.605  1.206   1.00 32.76 ?  271  GLU E CD  1 
ATOM   10854 O  OE1 . GLU E  1 247 ? 23.388  49.623  2.406   1.00 33.88 ?  271  GLU E OE1 1 
ATOM   10855 O  OE2 . GLU E  1 247 ? 23.696  49.012  0.324   1.00 35.27 -1 271  GLU E OE2 1 
ATOM   10856 N  N   . PHE E  1 248 ? 18.073  51.581  2.140   1.00 24.63 ?  272  PHE E N   1 
ATOM   10857 C  CA  . PHE E  1 248 ? 16.790  50.861  2.151   1.00 24.07 ?  272  PHE E CA  1 
ATOM   10858 C  C   . PHE E  1 248 ? 16.877  49.478  1.489   1.00 23.86 ?  272  PHE E C   1 
ATOM   10859 O  O   . PHE E  1 248 ? 16.124  49.160  0.565   1.00 23.82 ?  272  PHE E O   1 
ATOM   10860 C  CB  . PHE E  1 248 ? 15.662  51.722  1.556   1.00 23.93 ?  272  PHE E CB  1 
ATOM   10861 C  CG  . PHE E  1 248 ? 15.388  52.982  2.336   1.00 23.69 ?  272  PHE E CG  1 
ATOM   10862 C  CD1 . PHE E  1 248 ? 14.657  52.938  3.521   1.00 23.70 ?  272  PHE E CD1 1 
ATOM   10863 C  CD2 . PHE E  1 248 ? 15.873  54.208  1.896   1.00 23.57 ?  272  PHE E CD2 1 
ATOM   10864 C  CE1 . PHE E  1 248 ? 14.412  54.099  4.259   1.00 23.57 ?  272  PHE E CE1 1 
ATOM   10865 C  CE2 . PHE E  1 248 ? 15.631  55.379  2.627   1.00 23.43 ?  272  PHE E CE2 1 
ATOM   10866 C  CZ  . PHE E  1 248 ? 14.896  55.320  3.809   1.00 23.25 ?  272  PHE E CZ  1 
ATOM   10867 N  N   . SER E  1 249 ? 17.804  48.662  1.987   1.00 23.51 ?  273  SER E N   1 
ATOM   10868 C  CA  . SER E  1 249 ? 18.049  47.328  1.444   1.00 23.27 ?  273  SER E CA  1 
ATOM   10869 C  C   . SER E  1 249 ? 17.187  46.271  2.128   1.00 23.20 ?  273  SER E C   1 
ATOM   10870 O  O   . SER E  1 249 ? 17.226  46.129  3.352   1.00 23.27 ?  273  SER E O   1 
ATOM   10871 C  CB  . SER E  1 249 ? 19.534  46.970  1.570   1.00 23.06 ?  273  SER E CB  1 
ATOM   10872 O  OG  . SER E  1 249 ? 19.751  45.576  1.424   1.00 23.08 ?  273  SER E OG  1 
ATOM   10873 N  N   . ALA E  1 250 ? 16.416  45.532  1.330   1.00 23.07 ?  274  ALA E N   1 
ATOM   10874 C  CA  . ALA E  1 250 ? 15.593  44.432  1.841   1.00 22.94 ?  274  ALA E CA  1 
ATOM   10875 C  C   . ALA E  1 250 ? 16.458  43.304  2.397   1.00 22.93 ?  274  ALA E C   1 
ATOM   10876 O  O   . ALA E  1 250 ? 16.108  42.686  3.409   1.00 22.75 ?  274  ALA E O   1 
ATOM   10877 C  CB  . ALA E  1 250 ? 14.666  43.900  0.752   1.00 22.89 ?  274  ALA E CB  1 
ATOM   10878 N  N   . ALA E  1 251 ? 17.581  43.043  1.724   1.00 22.85 ?  275  ALA E N   1 
ATOM   10879 C  CA  . ALA E  1 251 ? 18.544  42.027  2.153   1.00 22.83 ?  275  ALA E CA  1 
ATOM   10880 C  C   . ALA E  1 251 ? 19.049  42.310  3.563   1.00 22.64 ?  275  ALA E C   1 
ATOM   10881 O  O   . ALA E  1 251 ? 19.171  41.400  4.380   1.00 23.02 ?  275  ALA E O   1 
ATOM   10882 C  CB  . ALA E  1 251 ? 19.715  41.947  1.168   1.00 22.80 ?  275  ALA E CB  1 
ATOM   10883 N  N   . GLU E  1 252 ? 19.333  43.579  3.840   1.00 22.52 ?  276  GLU E N   1 
ATOM   10884 C  CA  . GLU E  1 252 ? 19.748  44.016  5.171   1.00 22.42 ?  276  GLU E CA  1 
ATOM   10885 C  C   . GLU E  1 252 ? 18.704  43.663  6.242   1.00 22.27 ?  276  GLU E C   1 
ATOM   10886 O  O   . GLU E  1 252 ? 19.049  43.133  7.305   1.00 22.07 ?  276  GLU E O   1 
ATOM   10887 C  CB  . GLU E  1 252 ? 20.025  45.518  5.160   1.00 22.33 ?  276  GLU E CB  1 
ATOM   10888 C  CG  . GLU E  1 252 ? 20.403  46.104  6.508   1.00 22.94 ?  276  GLU E CG  1 
ATOM   10889 C  CD  . GLU E  1 252 ? 20.414  47.616  6.499   1.00 23.64 ?  276  GLU E CD  1 
ATOM   10890 O  OE1 . GLU E  1 252 ? 21.020  48.209  5.583   1.00 24.57 ?  276  GLU E OE1 1 
ATOM   10891 O  OE2 . GLU E  1 252 ? 19.825  48.216  7.419   1.00 24.24 -1 276  GLU E OE2 1 
ATOM   10892 N  N   . SER E  1 253 ? 17.434  43.947  5.948   1.00 22.02 ?  277  SER E N   1 
ATOM   10893 C  CA  . SER E  1 253 ? 16.339  43.711  6.896   1.00 21.87 ?  277  SER E CA  1 
ATOM   10894 C  C   . SER E  1 253 ? 16.071  42.230  7.150   1.00 21.75 ?  277  SER E C   1 
ATOM   10895 O  O   . SER E  1 253 ? 15.467  41.868  8.166   1.00 22.21 ?  277  SER E O   1 
ATOM   10896 C  CB  . SER E  1 253 ? 15.059  44.428  6.452   1.00 21.84 ?  277  SER E CB  1 
ATOM   10897 O  OG  . SER E  1 253 ? 14.741  44.151  5.101   1.00 22.06 ?  277  SER E OG  1 
ATOM   10898 N  N   . ARG E  1 254 ? 16.534  41.382  6.236   1.00 21.36 ?  278  ARG E N   1 
ATOM   10899 C  CA  . ARG E  1 254 ? 16.416  39.930  6.383   1.00 21.00 ?  278  ARG E CA  1 
ATOM   10900 C  C   . ARG E  1 254 ? 17.470  39.348  7.332   1.00 20.67 ?  278  ARG E C   1 
ATOM   10901 O  O   . ARG E  1 254 ? 17.317  38.230  7.839   1.00 20.67 ?  278  ARG E O   1 
ATOM   10902 C  CB  . ARG E  1 254 ? 16.500  39.245  5.015   1.00 21.02 ?  278  ARG E CB  1 
ATOM   10903 C  CG  . ARG E  1 254 ? 15.322  39.543  4.099   1.00 20.84 ?  278  ARG E CG  1 
ATOM   10904 C  CD  . ARG E  1 254 ? 15.408  38.778  2.779   1.00 21.29 ?  278  ARG E CD  1 
ATOM   10905 N  NE  . ARG E  1 254 ? 14.387  39.247  1.843   1.00 21.75 ?  278  ARG E NE  1 
ATOM   10906 C  CZ  . ARG E  1 254 ? 14.618  40.040  0.799   1.00 22.34 ?  278  ARG E CZ  1 
ATOM   10907 N  NH1 . ARG E  1 254 ? 15.853  40.445  0.512   1.00 22.05 ?  278  ARG E NH1 1 
ATOM   10908 N  NH2 . ARG E  1 254 ? 13.607  40.416  0.025   1.00 22.11 ?  278  ARG E NH2 1 
ATOM   10909 N  N   . LYS E  1 255 ? 18.533  40.108  7.569   1.00 20.02 ?  279  LYS E N   1 
ATOM   10910 C  CA  . LYS E  1 255 ? 19.616  39.671  8.443   1.00 19.92 ?  279  LYS E CA  1 
ATOM   10911 C  C   . LYS E  1 255 ? 19.239  39.842  9.914   1.00 19.46 ?  279  LYS E C   1 
ATOM   10912 O  O   . LYS E  1 255 ? 18.642  40.850  10.283  1.00 19.48 ?  279  LYS E O   1 
ATOM   10913 C  CB  . LYS E  1 255 ? 20.903  40.435  8.122   1.00 19.89 ?  279  LYS E CB  1 
ATOM   10914 C  CG  . LYS E  1 255 ? 21.468  40.121  6.748   1.00 20.10 ?  279  LYS E CG  1 
ATOM   10915 C  CD  . LYS E  1 255 ? 22.683  40.967  6.439   1.00 20.75 ?  279  LYS E CD  1 
ATOM   10916 C  CE  . LYS E  1 255 ? 23.322  40.551  5.129   1.00 20.87 ?  279  LYS E CE  1 
ATOM   10917 N  NZ  . LYS E  1 255 ? 24.543  41.360  4.852   1.00 21.54 ?  279  LYS E NZ  1 
ATOM   10918 N  N   . PRO E  1 256 ? 19.589  38.854  10.760  1.00 19.26 ?  280  PRO E N   1 
ATOM   10919 C  CA  . PRO E  1 256 ? 19.242  38.870  12.194  1.00 18.97 ?  280  PRO E CA  1 
ATOM   10920 C  C   . PRO E  1 256 ? 19.709  40.129  12.930  1.00 18.86 ?  280  PRO E C   1 
ATOM   10921 O  O   . PRO E  1 256 ? 19.054  40.577  13.877  1.00 18.71 ?  280  PRO E O   1 
ATOM   10922 C  CB  . PRO E  1 256 ? 19.967  37.636  12.741  1.00 18.96 ?  280  PRO E CB  1 
ATOM   10923 C  CG  . PRO E  1 256 ? 20.099  36.727  11.564  1.00 18.91 ?  280  PRO E CG  1 
ATOM   10924 C  CD  . PRO E  1 256 ? 20.335  37.635  10.394  1.00 19.09 ?  280  PRO E CD  1 
ATOM   10925 N  N   . GLU E  1 257 ? 20.829  40.694  12.484  1.00 18.81 ?  281  GLU E N   1 
ATOM   10926 C  CA  . GLU E  1 257 ? 21.378  41.919  13.061  1.00 18.87 ?  281  GLU E CA  1 
ATOM   10927 C  C   . GLU E  1 257 ? 20.415  43.115  12.988  1.00 18.83 ?  281  GLU E C   1 
ATOM   10928 O  O   . GLU E  1 257 ? 20.456  43.999  13.845  1.00 18.93 ?  281  GLU E O   1 
ATOM   10929 C  CB  . GLU E  1 257 ? 22.705  42.276  12.385  1.00 18.95 ?  281  GLU E CB  1 
ATOM   10930 C  CG  . GLU E  1 257 ? 23.874  41.344  12.721  1.00 19.52 ?  281  GLU E CG  1 
ATOM   10931 C  CD  . GLU E  1 257 ? 23.911  40.067  11.870  1.00 19.47 ?  281  GLU E CD  1 
ATOM   10932 O  OE1 . GLU E  1 257 ? 23.092  39.916  10.938  1.00 19.07 ?  281  GLU E OE1 1 
ATOM   10933 O  OE2 . GLU E  1 257 ? 24.775  39.213  12.140  1.00 20.10 -1 281  GLU E OE2 1 
ATOM   10934 N  N   . ALA E  1 258 ? 19.555  43.138  11.970  1.00 18.68 ?  282  ALA E N   1 
ATOM   10935 C  CA  . ALA E  1 258 ? 18.570  44.219  11.794  1.00 18.60 ?  282  ALA E CA  1 
ATOM   10936 C  C   . ALA E  1 258 ? 17.579  44.368  12.965  1.00 18.41 ?  282  ALA E C   1 
ATOM   10937 O  O   . ALA E  1 258 ? 17.084  45.470  13.223  1.00 18.19 ?  282  ALA E O   1 
ATOM   10938 C  CB  . ALA E  1 258 ? 17.817  44.043  10.479  1.00 18.50 ?  282  ALA E CB  1 
ATOM   10939 N  N   . CYS E  1 259 ? 17.305  43.264  13.665  1.00 18.35 ?  283  CYS E N   1 
ATOM   10940 C  CA  . CYS E  1 259 ? 16.367  43.239  14.799  1.00 18.51 ?  283  CYS E CA  1 
ATOM   10941 C  C   . CYS E  1 259 ? 17.058  43.450  16.150  1.00 18.35 ?  283  CYS E C   1 
ATOM   10942 O  O   . CYS E  1 259 ? 16.396  43.679  17.170  1.00 18.34 ?  283  CYS E O   1 
ATOM   10943 C  CB  . CYS E  1 259 ? 15.626  41.898  14.857  1.00 18.48 ?  283  CYS E CB  1 
ATOM   10944 S  SG  . CYS E  1 259 ? 15.168  41.161  13.280  1.00 19.94 ?  283  CYS E SG  1 
ATOM   10945 N  N   . ALA E  1 260 ? 18.385  43.370  16.145  1.00 18.24 ?  284  ALA E N   1 
ATOM   10946 C  CA  . ALA E  1 260 ? 19.170  43.206  17.374  1.00 18.20 ?  284  ALA E CA  1 
ATOM   10947 C  C   . ALA E  1 260 ? 19.178  44.397  18.327  1.00 18.24 ?  284  ALA E C   1 
ATOM   10948 O  O   . ALA E  1 260 ? 19.191  44.212  19.545  1.00 17.85 ?  284  ALA E O   1 
ATOM   10949 C  CB  . ALA E  1 260 ? 20.578  42.812  17.034  1.00 17.86 ?  284  ALA E CB  1 
ATOM   10950 N  N   . THR E  1 261 ? 19.174  45.609  17.772  1.00 18.33 ?  285  THR E N   1 
ATOM   10951 C  CA  . THR E  1 261 ? 19.263  46.832  18.570  1.00 18.53 ?  285  THR E CA  1 
ATOM   10952 C  C   . THR E  1 261 ? 18.093  46.969  19.548  1.00 18.90 ?  285  THR E C   1 
ATOM   10953 O  O   . THR E  1 261 ? 18.276  47.416  20.685  1.00 19.36 ?  285  THR E O   1 
ATOM   10954 C  CB  . THR E  1 261 ? 19.387  48.095  17.664  1.00 18.50 ?  285  THR E CB  1 
ATOM   10955 O  OG1 . THR E  1 261 ? 20.535  47.961  16.816  1.00 17.60 ?  285  THR E OG1 1 
ATOM   10956 C  CG2 . THR E  1 261 ? 19.535  49.374  18.496  1.00 18.04 ?  285  THR E CG2 1 
ATOM   10957 N  N   . CYS E  1 262 ? 16.903  46.561  19.107  1.00 18.99 ?  286  CYS E N   1 
ATOM   10958 C  CA  . CYS E  1 262 ? 15.696  46.659  19.925  1.00 18.99 ?  286  CYS E CA  1 
ATOM   10959 C  C   . CYS E  1 262 ? 15.379  45.361  20.657  1.00 19.18 ?  286  CYS E C   1 
ATOM   10960 O  O   . CYS E  1 262 ? 15.038  45.384  21.836  1.00 19.22 ?  286  CYS E O   1 
ATOM   10961 C  CB  . CYS E  1 262 ? 14.492  47.056  19.069  1.00 18.99 ?  286  CYS E CB  1 
ATOM   10962 S  SG  . CYS E  1 262 ? 14.761  48.436  17.948  1.00 18.53 ?  286  CYS E SG  1 
ATOM   10963 N  N   . HIS E  1 263 ? 15.478  44.235  19.951  1.00 19.38 ?  287  HIS E N   1 
ATOM   10964 C  CA  . HIS E  1 263 ? 15.116  42.942  20.522  1.00 19.68 ?  287  HIS E CA  1 
ATOM   10965 C  C   . HIS E  1 263 ? 16.310  42.307  21.237  1.00 19.77 ?  287  HIS E C   1 
ATOM   10966 O  O   . HIS E  1 263 ? 16.788  41.229  20.874  1.00 19.79 ?  287  HIS E O   1 
ATOM   10967 C  CB  . HIS E  1 263 ? 14.515  42.020  19.455  1.00 19.73 ?  287  HIS E CB  1 
ATOM   10968 C  CG  . HIS E  1 263 ? 13.137  42.421  19.016  1.00 20.27 ?  287  HIS E CG  1 
ATOM   10969 N  ND1 . HIS E  1 263 ? 12.004  42.105  19.738  1.00 20.45 ?  287  HIS E ND1 1 
ATOM   10970 C  CD2 . HIS E  1 263 ? 12.712  43.115  17.933  1.00 19.99 ?  287  HIS E CD2 1 
ATOM   10971 C  CE1 . HIS E  1 263 ? 10.941  42.588  19.118  1.00 20.22 ?  287  HIS E CE1 1 
ATOM   10972 N  NE2 . HIS E  1 263 ? 11.342  43.204  18.019  1.00 20.63 ?  287  HIS E NE2 1 
ATOM   10973 N  N   . SER E  1 264 ? 16.783  43.009  22.261  1.00 19.78 ?  288  SER E N   1 
ATOM   10974 C  CA  . SER E  1 264 ? 17.926  42.580  23.046  1.00 19.81 ?  288  SER E CA  1 
ATOM   10975 C  C   . SER E  1 264 ? 17.817  43.163  24.445  1.00 20.00 ?  288  SER E C   1 
ATOM   10976 O  O   . SER E  1 264 ? 16.986  44.040  24.691  1.00 20.24 ?  288  SER E O   1 
ATOM   10977 C  CB  . SER E  1 264 ? 19.224  43.042  22.387  1.00 19.85 ?  288  SER E CB  1 
ATOM   10978 O  OG  . SER E  1 264 ? 19.254  44.453  22.257  1.00 19.30 ?  288  SER E OG  1 
ATOM   10979 N  N   . GLY E  1 265 ? 18.640  42.664  25.363  1.00 20.03 ?  289  GLY E N   1 
ATOM   10980 C  CA  . GLY E  1 265 ? 18.721  43.240  26.695  1.00 20.16 ?  289  GLY E CA  1 
ATOM   10981 C  C   . GLY E  1 265 ? 18.083  42.458  27.828  1.00 20.40 ?  289  GLY E C   1 
ATOM   10982 O  O   . GLY E  1 265 ? 17.617  41.331  27.655  1.00 20.52 ?  289  GLY E O   1 
ATOM   10983 N  N   . VAL E  1 266 ? 18.046  43.101  28.989  1.00 20.44 ?  290  VAL E N   1 
ATOM   10984 C  CA  . VAL E  1 266 ? 17.782  42.459  30.274  1.00 20.47 ?  290  VAL E CA  1 
ATOM   10985 C  C   . VAL E  1 266 ? 16.358  41.902  30.471  1.00 20.58 ?  290  VAL E C   1 
ATOM   10986 O  O   . VAL E  1 266 ? 16.162  41.009  31.289  1.00 20.55 ?  290  VAL E O   1 
ATOM   10987 C  CB  . VAL E  1 266 ? 18.173  43.424  31.433  1.00 20.45 ?  290  VAL E CB  1 
ATOM   10988 C  CG1 . VAL E  1 266 ? 17.091  44.484  31.657  1.00 20.31 ?  290  VAL E CG1 1 
ATOM   10989 C  CG2 . VAL E  1 266 ? 18.499  42.655  32.722  1.00 20.73 ?  290  VAL E CG2 1 
ATOM   10990 N  N   . ASP E  1 267 ? 15.376  42.420  29.731  1.00 20.62 ?  291  ASP E N   1 
ATOM   10991 C  CA  . ASP E  1 267 ? 13.997  41.924  29.840  1.00 20.80 ?  291  ASP E CA  1 
ATOM   10992 C  C   . ASP E  1 267 ? 13.473  41.221  28.570  1.00 20.69 ?  291  ASP E C   1 
ATOM   10993 O  O   . ASP E  1 267 ? 12.302  40.822  28.510  1.00 20.83 ?  291  ASP E O   1 
ATOM   10994 C  CB  . ASP E  1 267 ? 13.038  43.039  30.311  1.00 20.91 ?  291  ASP E CB  1 
ATOM   10995 C  CG  . ASP E  1 267 ? 12.942  44.202  29.330  1.00 21.63 ?  291  ASP E CG  1 
ATOM   10996 O  OD1 . ASP E  1 267 ? 13.864  44.388  28.502  1.00 22.54 ?  291  ASP E OD1 1 
ATOM   10997 O  OD2 . ASP E  1 267 ? 11.932  44.941  29.396  1.00 22.30 -1 291  ASP E OD2 1 
ATOM   10998 N  N   . HIS E  1 268 ? 14.347  41.079  27.571  1.00 20.35 ?  292  HIS E N   1 
ATOM   10999 C  CA  . HIS E  1 268 ? 14.068  40.336  26.333  1.00 20.26 ?  292  HIS E CA  1 
ATOM   11000 C  C   . HIS E  1 268 ? 15.355  40.180  25.520  1.00 20.31 ?  292  HIS E C   1 
ATOM   11001 O  O   . HIS E  1 268 ? 15.635  40.977  24.623  1.00 20.11 ?  292  HIS E O   1 
ATOM   11002 C  CB  . HIS E  1 268 ? 12.963  41.003  25.485  1.00 20.22 ?  292  HIS E CB  1 
ATOM   11003 C  CG  . HIS E  1 268 ? 13.029  42.499  25.468  1.00 20.27 ?  292  HIS E CG  1 
ATOM   11004 N  ND1 . HIS E  1 268 ? 14.080  43.193  24.909  1.00 20.72 ?  292  HIS E ND1 1 
ATOM   11005 C  CD2 . HIS E  1 268 ? 12.177  43.433  25.952  1.00 20.75 ?  292  HIS E CD2 1 
ATOM   11006 C  CE1 . HIS E  1 268 ? 13.873  44.491  25.047  1.00 20.55 ?  292  HIS E CE1 1 
ATOM   11007 N  NE2 . HIS E  1 268 ? 12.727  44.664  25.679  1.00 21.62 ?  292  HIS E NE2 1 
ATOM   11008 N  N   . ASN E  1 269 ? 16.134  39.148  25.838  1.00 20.47 ?  293  ASN E N   1 
ATOM   11009 C  CA  . ASN E  1 269 ? 17.449  38.962  25.218  1.00 20.72 ?  293  ASN E CA  1 
ATOM   11010 C  C   . ASN E  1 269 ? 17.420  38.092  23.958  1.00 20.65 ?  293  ASN E C   1 
ATOM   11011 O  O   . ASN E  1 269 ? 18.166  37.113  23.843  1.00 20.57 ?  293  ASN E O   1 
ATOM   11012 C  CB  . ASN E  1 269 ? 18.470  38.440  26.244  1.00 20.70 ?  293  ASN E CB  1 
ATOM   11013 C  CG  . ASN E  1 269 ? 18.116  37.066  26.790  1.00 21.09 ?  293  ASN E CG  1 
ATOM   11014 O  OD1 . ASN E  1 269 ? 16.970  36.612  26.692  1.00 21.51 ?  293  ASN E OD1 1 
ATOM   11015 N  ND2 . ASN E  1 269 ? 19.105  36.397  27.379  1.00 20.05 ?  293  ASN E ND2 1 
ATOM   11016 N  N   . ASN E  1 270 ? 16.568  38.475  23.011  1.00 20.62 ?  294  ASN E N   1 
ATOM   11017 C  CA  . ASN E  1 270 ? 16.354  37.693  21.795  1.00 20.72 ?  294  ASN E CA  1 
ATOM   11018 C  C   . ASN E  1 270 ? 17.591  37.588  20.908  1.00 20.90 ?  294  ASN E C   1 
ATOM   11019 O  O   . ASN E  1 270 ? 17.934  36.500  20.440  1.00 21.11 ?  294  ASN E O   1 
ATOM   11020 C  CB  . ASN E  1 270 ? 15.147  38.222  21.019  1.00 20.64 ?  294  ASN E CB  1 
ATOM   11021 C  CG  . ASN E  1 270 ? 13.886  38.255  21.867  1.00 20.95 ?  294  ASN E CG  1 
ATOM   11022 O  OD1 . ASN E  1 270 ? 13.744  39.104  22.751  1.00 21.08 ?  294  ASN E OD1 1 
ATOM   11023 N  ND2 . ASN E  1 270 ? 12.972  37.320  21.614  1.00 20.15 ?  294  ASN E ND2 1 
ATOM   11024 N  N   . TRP E  1 271 ? 18.262  38.715  20.690  1.00 20.74 ?  295  TRP E N   1 
ATOM   11025 C  CA  . TRP E  1 271 ? 19.517  38.719  19.952  1.00 20.92 ?  295  TRP E CA  1 
ATOM   11026 C  C   . TRP E  1 271 ? 20.526  37.796  20.625  1.00 20.83 ?  295  TRP E C   1 
ATOM   11027 O  O   . TRP E  1 271 ? 21.132  36.948  19.967  1.00 20.97 ?  295  TRP E O   1 
ATOM   11028 C  CB  . TRP E  1 271 ? 20.093  40.136  19.844  1.00 20.86 ?  295  TRP E CB  1 
ATOM   11029 C  CG  . TRP E  1 271 ? 21.497  40.156  19.300  1.00 21.05 ?  295  TRP E CG  1 
ATOM   11030 C  CD1 . TRP E  1 271 ? 22.635  40.500  19.976  1.00 21.31 ?  295  TRP E CD1 1 
ATOM   11031 C  CD2 . TRP E  1 271 ? 21.913  39.786  17.981  1.00 20.78 ?  295  TRP E CD2 1 
ATOM   11032 N  NE1 . TRP E  1 271 ? 23.728  40.387  19.153  1.00 20.46 ?  295  TRP E NE1 1 
ATOM   11033 C  CE2 . TRP E  1 271 ? 23.314  39.950  17.923  1.00 21.17 ?  295  TRP E CE2 1 
ATOM   11034 C  CE3 . TRP E  1 271 ? 21.234  39.342  16.836  1.00 21.45 ?  295  TRP E CE3 1 
ATOM   11035 C  CZ2 . TRP E  1 271 ? 24.054  39.684  16.765  1.00 21.39 ?  295  TRP E CZ2 1 
ATOM   11036 C  CZ3 . TRP E  1 271 ? 21.967  39.076  15.687  1.00 21.80 ?  295  TRP E CZ3 1 
ATOM   11037 C  CH2 . TRP E  1 271 ? 23.365  39.248  15.663  1.00 22.32 ?  295  TRP E CH2 1 
ATOM   11038 N  N   . GLU E  1 272 ? 20.689  37.970  21.935  1.00 20.63 ?  296  GLU E N   1 
ATOM   11039 C  CA  . GLU E  1 272 ? 21.634  37.186  22.724  1.00 20.67 ?  296  GLU E CA  1 
ATOM   11040 C  C   . GLU E  1 272 ? 21.334  35.683  22.653  1.00 20.64 ?  296  GLU E C   1 
ATOM   11041 O  O   . GLU E  1 272 ? 22.238  34.889  22.385  1.00 20.83 ?  296  GLU E O   1 
ATOM   11042 C  CB  . GLU E  1 272 ? 21.668  37.675  24.182  1.00 20.60 ?  296  GLU E CB  1 
ATOM   11043 C  CG  . GLU E  1 272 ? 22.104  39.139  24.360  1.00 20.98 ?  296  GLU E CG  1 
ATOM   11044 C  CD  . GLU E  1 272 ? 20.937  40.128  24.373  1.00 21.56 ?  296  GLU E CD  1 
ATOM   11045 O  OE1 . GLU E  1 272 ? 20.039  40.036  23.509  1.00 21.40 ?  296  GLU E OE1 1 
ATOM   11046 O  OE2 . GLU E  1 272 ? 20.919  41.009  25.257  1.00 22.01 -1 296  GLU E OE2 1 
ATOM   11047 N  N   . ALA E  1 273 ? 20.071  35.306  22.871  1.00 20.27 ?  297  ALA E N   1 
ATOM   11048 C  CA  . ALA E  1 273 ? 19.655  33.898  22.857  1.00 20.17 ?  297  ALA E CA  1 
ATOM   11049 C  C   . ALA E  1 273 ? 19.774  33.266  21.470  1.00 20.03 ?  297  ALA E C   1 
ATOM   11050 O  O   . ALA E  1 273 ? 20.353  32.189  21.320  1.00 20.01 ?  297  ALA E O   1 
ATOM   11051 C  CB  . ALA E  1 273 ? 18.228  33.742  23.396  1.00 19.89 ?  297  ALA E CB  1 
ATOM   11052 N  N   . TYR E  1 274 ? 19.232  33.945  20.464  1.00 20.16 ?  298  TYR E N   1 
ATOM   11053 C  CA  . TYR E  1 274 ? 19.273  33.445  19.096  1.00 20.15 ?  298  TYR E CA  1 
ATOM   11054 C  C   . TYR E  1 274 ? 20.703  33.208  18.608  1.00 20.30 ?  298  TYR E C   1 
ATOM   11055 O  O   . TYR E  1 274 ? 21.017  32.117  18.145  1.00 20.25 ?  298  TYR E O   1 
ATOM   11056 C  CB  . TYR E  1 274 ? 18.529  34.376  18.132  1.00 20.15 ?  298  TYR E CB  1 
ATOM   11057 C  CG  . TYR E  1 274 ? 18.825  34.075  16.677  1.00 19.98 ?  298  TYR E CG  1 
ATOM   11058 C  CD1 . TYR E  1 274 ? 18.253  32.970  16.052  1.00 19.72 ?  298  TYR E CD1 1 
ATOM   11059 C  CD2 . TYR E  1 274 ? 19.696  34.879  15.936  1.00 19.24 ?  298  TYR E CD2 1 
ATOM   11060 C  CE1 . TYR E  1 274 ? 18.523  32.675  14.730  1.00 19.44 ?  298  TYR E CE1 1 
ATOM   11061 C  CE2 . TYR E  1 274 ? 19.975  34.588  14.602  1.00 19.58 ?  298  TYR E CE2 1 
ATOM   11062 C  CZ  . TYR E  1 274 ? 19.380  33.481  14.010  1.00 19.58 ?  298  TYR E CZ  1 
ATOM   11063 O  OH  . TYR E  1 274 ? 19.634  33.167  12.699  1.00 20.93 ?  298  TYR E OH  1 
ATOM   11064 N  N   . THR E  1 275 ? 21.561  34.222  18.720  1.00 20.43 ?  299  THR E N   1 
ATOM   11065 C  CA  . THR E  1 275 ? 22.934  34.113  18.211  1.00 20.83 ?  299  THR E CA  1 
ATOM   11066 C  C   . THR E  1 275 ? 23.779  33.063  18.913  1.00 20.64 ?  299  THR E C   1 
ATOM   11067 O  O   . THR E  1 275 ? 24.701  32.516  18.312  1.00 20.46 ?  299  THR E O   1 
ATOM   11068 C  CB  . THR E  1 275 ? 23.691  35.458  18.215  1.00 20.98 ?  299  THR E CB  1 
ATOM   11069 O  OG1 . THR E  1 275 ? 23.779  35.977  19.548  1.00 21.40 ?  299  THR E OG1 1 
ATOM   11070 C  CG2 . THR E  1 275 ? 22.972  36.431  17.347  1.00 21.78 ?  299  THR E CG2 1 
ATOM   11071 N  N   . MET E  1 276 ? 23.461  32.786  20.176  1.00 20.72 ?  300  MET E N   1 
ATOM   11072 C  CA  . MET E  1 276 ? 24.166  31.758  20.946  1.00 20.74 ?  300  MET E CA  1 
ATOM   11073 C  C   . MET E  1 276 ? 23.643  30.347  20.656  1.00 20.86 ?  300  MET E C   1 
ATOM   11074 O  O   . MET E  1 276 ? 24.349  29.361  20.864  1.00 21.01 ?  300  MET E O   1 
ATOM   11075 C  CB  . MET E  1 276 ? 24.104  32.065  22.447  1.00 20.76 ?  300  MET E CB  1 
ATOM   11076 C  CG  . MET E  1 276 ? 24.993  33.237  22.901  1.00 21.05 ?  300  MET E CG  1 
ATOM   11077 S  SD  . MET E  1 276 ? 26.713  33.173  22.334  1.00 22.43 ?  300  MET E SD  1 
ATOM   11078 C  CE  . MET E  1 276 ? 27.231  31.575  22.966  1.00 21.90 ?  300  MET E CE  1 
ATOM   11079 N  N   . SER E  1 277 ? 22.407  30.254  20.171  1.00 20.96 ?  301  SER E N   1 
ATOM   11080 C  CA  . SER E  1 277 ? 21.826  28.970  19.780  1.00 20.93 ?  301  SER E CA  1 
ATOM   11081 C  C   . SER E  1 277 ? 22.564  28.403  18.571  1.00 20.91 ?  301  SER E C   1 
ATOM   11082 O  O   . SER E  1 277 ? 23.323  29.113  17.912  1.00 20.75 ?  301  SER E O   1 
ATOM   11083 C  CB  . SER E  1 277 ? 20.341  29.137  19.443  1.00 20.91 ?  301  SER E CB  1 
ATOM   11084 O  OG  . SER E  1 277 ? 20.160  29.726  18.163  1.00 20.49 ?  301  SER E OG  1 
ATOM   11085 N  N   . LYS E  1 278 ? 22.334  27.128  18.277  1.00 21.06 ?  302  LYS E N   1 
ATOM   11086 C  CA  . LYS E  1 278 ? 22.907  26.531  17.073  1.00 21.20 ?  302  LYS E CA  1 
ATOM   11087 C  C   . LYS E  1 278 ? 22.381  27.232  15.827  1.00 21.01 ?  302  LYS E C   1 
ATOM   11088 O  O   . LYS E  1 278 ? 23.155  27.553  14.925  1.00 20.98 ?  302  LYS E O   1 
ATOM   11089 C  CB  . LYS E  1 278 ? 22.642  25.026  17.002  1.00 21.16 ?  302  LYS E CB  1 
ATOM   11090 C  CG  . LYS E  1 278 ? 23.714  24.290  16.232  1.00 21.94 ?  302  LYS E CG  1 
ATOM   11091 C  CD  . LYS E  1 278 ? 24.974  24.177  17.079  1.00 23.54 ?  302  LYS E CD  1 
ATOM   11092 C  CE  . LYS E  1 278 ? 26.198  24.167  16.211  1.00 23.15 ?  302  LYS E CE  1 
ATOM   11093 N  NZ  . LYS E  1 278 ? 27.451  24.085  16.987  1.00 22.33 ?  302  LYS E NZ  1 
ATOM   11094 N  N   . HIS E  1 279 ? 21.069  27.480  15.801  1.00 20.90 ?  303  HIS E N   1 
ATOM   11095 C  CA  . HIS E  1 279 ? 20.426  28.241  14.727  1.00 20.95 ?  303  HIS E CA  1 
ATOM   11096 C  C   . HIS E  1 279 ? 21.209  29.520  14.400  1.00 20.95 ?  303  HIS E C   1 
ATOM   11097 O  O   . HIS E  1 279 ? 21.556  29.764  13.242  1.00 20.98 ?  303  HIS E O   1 
ATOM   11098 C  CB  . HIS E  1 279 ? 18.977  28.615  15.095  1.00 20.99 ?  303  HIS E CB  1 
ATOM   11099 C  CG  . HIS E  1 279 ? 18.011  27.463  15.113  1.00 21.11 ?  303  HIS E CG  1 
ATOM   11100 N  ND1 . HIS E  1 279 ? 16.879  27.466  15.900  1.00 21.86 ?  303  HIS E ND1 1 
ATOM   11101 C  CD2 . HIS E  1 279 ? 17.987  26.292  14.430  1.00 21.35 ?  303  HIS E CD2 1 
ATOM   11102 C  CE1 . HIS E  1 279 ? 16.202  26.347  15.705  1.00 21.56 ?  303  HIS E CE1 1 
ATOM   11103 N  NE2 . HIS E  1 279 ? 16.851  25.616  14.815  1.00 21.98 ?  303  HIS E NE2 1 
ATOM   11104 N  N   . GLY E  1 280 ? 21.498  30.317  15.429  1.00 20.91 ?  304  GLY E N   1 
ATOM   11105 C  CA  . GLY E  1 280 ? 22.135  31.626  15.254  1.00 20.91 ?  304  GLY E CA  1 
ATOM   11106 C  C   . GLY E  1 280 ? 23.625  31.582  14.970  1.00 21.04 ?  304  GLY E C   1 
ATOM   11107 O  O   . GLY E  1 280 ? 24.150  32.431  14.243  1.00 21.06 ?  304  GLY E O   1 
ATOM   11108 N  N   . LYS E  1 281 ? 24.308  30.600  15.555  1.00 21.15 ?  305  LYS E N   1 
ATOM   11109 C  CA  . LYS E  1 281 ? 25.724  30.371  15.278  1.00 21.35 ?  305  LYS E CA  1 
ATOM   11110 C  C   . LYS E  1 281 ? 25.947  29.889  13.844  1.00 21.54 ?  305  LYS E C   1 
ATOM   11111 O  O   . LYS E  1 281 ? 26.912  30.299  13.194  1.00 21.66 ?  305  LYS E O   1 
ATOM   11112 C  CB  . LYS E  1 281 ? 26.338  29.408  16.301  1.00 21.31 ?  305  LYS E CB  1 
ATOM   11113 C  CG  . LYS E  1 281 ? 26.628  30.059  17.663  1.00 21.33 ?  305  LYS E CG  1 
ATOM   11114 C  CD  . LYS E  1 281 ? 27.897  30.922  17.636  1.00 21.01 ?  305  LYS E CD  1 
ATOM   11115 C  CE  . LYS E  1 281 ? 27.944  31.943  18.778  1.00 21.21 ?  305  LYS E CE  1 
ATOM   11116 N  NZ  . LYS E  1 281 ? 27.273  33.235  18.431  1.00 22.43 ?  305  LYS E NZ  1 
ATOM   11117 N  N   . LEU E  1 282 ? 25.046  29.037  13.354  1.00 21.71 ?  306  LEU E N   1 
ATOM   11118 C  CA  . LEU E  1 282 ? 25.042  28.632  11.946  1.00 22.00 ?  306  LEU E CA  1 
ATOM   11119 C  C   . LEU E  1 282 ? 24.816  29.817  11.017  1.00 22.26 ?  306  LEU E C   1 
ATOM   11120 O  O   . LEU E  1 282 ? 25.454  29.917  9.967   1.00 22.29 ?  306  LEU E O   1 
ATOM   11121 C  CB  . LEU E  1 282 ? 23.973  27.569  11.678  1.00 21.88 ?  306  LEU E CB  1 
ATOM   11122 C  CG  . LEU E  1 282 ? 24.260  26.134  12.119  1.00 21.89 ?  306  LEU E CG  1 
ATOM   11123 C  CD1 . LEU E  1 282 ? 23.096  25.238  11.739  1.00 21.59 ?  306  LEU E CD1 1 
ATOM   11124 C  CD2 . LEU E  1 282 ? 25.542  25.628  11.498  1.00 22.04 ?  306  LEU E CD2 1 
ATOM   11125 N  N   . ALA E  1 283 ? 23.911  30.711  11.410  1.00 22.57 ?  307  ALA E N   1 
ATOM   11126 C  CA  . ALA E  1 283 ? 23.640  31.920  10.638  1.00 23.22 ?  307  ALA E CA  1 
ATOM   11127 C  C   . ALA E  1 283 ? 24.878  32.814  10.537  1.00 23.59 ?  307  ALA E C   1 
ATOM   11128 O  O   . ALA E  1 283 ? 25.148  33.382  9.479   1.00 23.51 ?  307  ALA E O   1 
ATOM   11129 C  CB  . ALA E  1 283 ? 22.461  32.686  11.231  1.00 22.98 ?  307  ALA E CB  1 
ATOM   11130 N  N   . GLU E  1 284 ? 25.622  32.928  11.639  1.00 24.18 ?  308  GLU E N   1 
ATOM   11131 C  CA  . GLU E  1 284 ? 26.893  33.661  11.652  1.00 24.70 ?  308  GLU E CA  1 
ATOM   11132 C  C   . GLU E  1 284 ? 27.928  32.988  10.745  1.00 24.69 ?  308  GLU E C   1 
ATOM   11133 O  O   . GLU E  1 284 ? 28.590  33.655  9.945   1.00 24.50 ?  308  GLU E O   1 
ATOM   11134 C  CB  . GLU E  1 284 ? 27.442  33.794  13.085  1.00 24.76 ?  308  GLU E CB  1 
ATOM   11135 C  CG  . GLU E  1 284 ? 26.617  34.721  13.977  1.00 26.10 ?  308  GLU E CG  1 
ATOM   11136 C  CD  . GLU E  1 284 ? 27.083  34.766  15.431  1.00 28.52 ?  308  GLU E CD  1 
ATOM   11137 O  OE1 . GLU E  1 284 ? 27.981  33.988  15.828  1.00 28.36 ?  308  GLU E OE1 1 
ATOM   11138 O  OE2 . GLU E  1 284 ? 26.533  35.598  16.187  1.00 30.67 -1 308  GLU E OE2 1 
ATOM   11139 N  N   . MET E  1 285 ? 28.047  31.667  10.870  1.00 24.82 ?  309  MET E N   1 
ATOM   11140 C  CA  . MET E  1 285 ? 29.031  30.892  10.111  1.00 25.37 ?  309  MET E CA  1 
ATOM   11141 C  C   . MET E  1 285 ? 28.747  30.847  8.613   1.00 25.83 ?  309  MET E C   1 
ATOM   11142 O  O   . MET E  1 285 ? 29.679  30.832  7.811   1.00 26.03 ?  309  MET E O   1 
ATOM   11143 C  CB  . MET E  1 285 ? 29.142  29.466  10.657  1.00 24.98 ?  309  MET E CB  1 
ATOM   11144 C  CG  . MET E  1 285 ? 29.910  29.371  11.956  1.00 24.65 ?  309  MET E CG  1 
ATOM   11145 S  SD  . MET E  1 285 ? 30.208  27.686  12.505  1.00 22.77 ?  309  MET E SD  1 
ATOM   11146 C  CE  . MET E  1 285 ? 28.719  27.338  13.452  1.00 22.40 ?  309  MET E CE  1 
ATOM   11147 N  N   . ASN E  1 286 ? 27.467  30.823  8.248   1.00 26.48 ?  310  ASN E N   1 
ATOM   11148 C  CA  . ASN E  1 286 ? 27.057  30.615  6.858   1.00 27.38 ?  310  ASN E CA  1 
ATOM   11149 C  C   . ASN E  1 286 ? 26.605  31.870  6.113   1.00 27.97 ?  310  ASN E C   1 
ATOM   11150 O  O   . ASN E  1 286 ? 26.150  31.773  4.970   1.00 28.15 ?  310  ASN E O   1 
ATOM   11151 C  CB  . ASN E  1 286 ? 25.938  29.564  6.786   1.00 27.36 ?  310  ASN E CB  1 
ATOM   11152 C  CG  . ASN E  1 286 ? 26.405  28.175  7.177   1.00 27.79 ?  310  ASN E CG  1 
ATOM   11153 O  OD1 . ASN E  1 286 ? 27.601  27.890  7.201   1.00 29.96 ?  310  ASN E OD1 1 
ATOM   11154 N  ND2 . ASN E  1 286 ? 25.456  27.297  7.478   1.00 28.03 ?  310  ASN E ND2 1 
ATOM   11155 N  N   . ARG E  1 287 ? 26.732  33.040  6.736   1.00 28.61 ?  311  ARG E N   1 
ATOM   11156 C  CA  . ARG E  1 287 ? 26.155  34.259  6.152   1.00 29.64 ?  311  ARG E CA  1 
ATOM   11157 C  C   . ARG E  1 287 ? 26.652  34.605  4.746   1.00 30.02 ?  311  ARG E C   1 
ATOM   11158 O  O   . ARG E  1 287 ? 25.948  35.275  3.988   1.00 30.44 ?  311  ARG E O   1 
ATOM   11159 C  CB  . ARG E  1 287 ? 26.251  35.466  7.098   1.00 29.60 ?  311  ARG E CB  1 
ATOM   11160 C  CG  . ARG E  1 287 ? 27.628  35.801  7.646   1.00 30.29 ?  311  ARG E CG  1 
ATOM   11161 C  CD  . ARG E  1 287 ? 27.495  36.860  8.739   1.00 31.68 ?  311  ARG E CD  1 
ATOM   11162 N  NE  . ARG E  1 287 ? 28.515  36.718  9.777   1.00 33.23 ?  311  ARG E NE  1 
ATOM   11163 C  CZ  . ARG E  1 287 ? 28.360  37.092  11.047  1.00 34.28 ?  311  ARG E CZ  1 
ATOM   11164 N  NH1 . ARG E  1 287 ? 27.217  37.637  11.456  1.00 33.42 ?  311  ARG E NH1 1 
ATOM   11165 N  NH2 . ARG E  1 287 ? 29.353  36.912  11.915  1.00 34.60 ?  311  ARG E NH2 1 
ATOM   11166 N  N   . ASP E  1 288 ? 27.841  34.124  4.392   1.00 30.39 ?  312  ASP E N   1 
ATOM   11167 C  CA  . ASP E  1 288 ? 28.437  34.431  3.092   1.00 30.69 ?  312  ASP E CA  1 
ATOM   11168 C  C   . ASP E  1 288 ? 28.112  33.402  2.034   1.00 30.40 ?  312  ASP E C   1 
ATOM   11169 O  O   . ASP E  1 288 ? 28.419  33.597  0.858   1.00 30.42 ?  312  ASP E O   1 
ATOM   11170 C  CB  . ASP E  1 288 ? 29.947  34.593  3.223   1.00 31.16 ?  312  ASP E CB  1 
ATOM   11171 C  CG  . ASP E  1 288 ? 30.315  35.566  4.300   1.00 32.71 ?  312  ASP E CG  1 
ATOM   11172 O  OD1 . ASP E  1 288 ? 29.665  36.636  4.366   1.00 34.25 ?  312  ASP E OD1 1 
ATOM   11173 O  OD2 . ASP E  1 288 ? 31.222  35.242  5.093   1.00 35.92 -1 312  ASP E OD2 1 
ATOM   11174 N  N   . LYS E  1 289 ? 27.490  32.307  2.458   1.00 30.16 ?  313  LYS E N   1 
ATOM   11175 C  CA  . LYS E  1 289 ? 27.062  31.263  1.539   1.00 30.06 ?  313  LYS E CA  1 
ATOM   11176 C  C   . LYS E  1 289 ? 25.603  31.466  1.131   1.00 29.50 ?  313  LYS E C   1 
ATOM   11177 O  O   . LYS E  1 289 ? 25.159  30.935  0.111   1.00 29.67 ?  313  LYS E O   1 
ATOM   11178 C  CB  . LYS E  1 289 ? 27.272  29.881  2.162   1.00 30.49 ?  313  LYS E CB  1 
ATOM   11179 C  CG  . LYS E  1 289 ? 28.634  29.715  2.827   1.00 31.86 ?  313  LYS E CG  1 
ATOM   11180 C  CD  . LYS E  1 289 ? 28.991  28.254  3.023   1.00 34.93 ?  313  LYS E CD  1 
ATOM   11181 C  CE  . LYS E  1 289 ? 30.438  28.115  3.471   1.00 36.30 ?  313  LYS E CE  1 
ATOM   11182 N  NZ  . LYS E  1 289 ? 30.929  26.715  3.315   1.00 37.84 ?  313  LYS E NZ  1 
ATOM   11183 N  N   . TRP E  1 290 ? 24.869  32.246  1.923   1.00 28.57 ?  314  TRP E N   1 
ATOM   11184 C  CA  . TRP E  1 290 ? 23.454  32.509  1.663   1.00 27.72 ?  314  TRP E CA  1 
ATOM   11185 C  C   . TRP E  1 290 ? 23.258  33.724  0.758   1.00 27.45 ?  314  TRP E C   1 
ATOM   11186 O  O   . TRP E  1 290 ? 23.960  34.723  0.892   1.00 27.29 ?  314  TRP E O   1 
ATOM   11187 C  CB  . TRP E  1 290 ? 22.682  32.729  2.971   1.00 27.36 ?  314  TRP E CB  1 
ATOM   11188 C  CG  . TRP E  1 290 ? 22.704  31.584  3.951   1.00 26.33 ?  314  TRP E CG  1 
ATOM   11189 C  CD1 . TRP E  1 290 ? 23.152  30.309  3.731   1.00 26.21 ?  314  TRP E CD1 1 
ATOM   11190 C  CD2 . TRP E  1 290 ? 22.207  31.605  5.295   1.00 25.71 ?  314  TRP E CD2 1 
ATOM   11191 N  NE1 . TRP E  1 290 ? 22.988  29.547  4.863   1.00 25.70 ?  314  TRP E NE1 1 
ATOM   11192 C  CE2 . TRP E  1 290 ? 22.407  30.316  5.836   1.00 25.17 ?  314  TRP E CE2 1 
ATOM   11193 C  CE3 . TRP E  1 290 ? 21.620  32.592  6.098   1.00 25.63 ?  314  TRP E CE3 1 
ATOM   11194 C  CZ2 . TRP E  1 290 ? 22.037  29.986  7.145   1.00 25.37 ?  314  TRP E CZ2 1 
ATOM   11195 C  CZ3 . TRP E  1 290 ? 21.255  32.263  7.406   1.00 25.40 ?  314  TRP E CZ3 1 
ATOM   11196 C  CH2 . TRP E  1 290 ? 21.465  30.970  7.912   1.00 24.93 ?  314  TRP E CH2 1 
ATOM   11197 N  N   . ASN E  1 291 ? 22.298  33.630  -0.160  1.00 27.23 ?  315  ASN E N   1 
ATOM   11198 C  CA  . ASN E  1 291 ? 21.899  34.781  -0.970  1.00 27.04 ?  315  ASN E CA  1 
ATOM   11199 C  C   . ASN E  1 291 ? 20.813  35.584  -0.254  1.00 26.69 ?  315  ASN E C   1 
ATOM   11200 O  O   . ASN E  1 291 ? 19.630  35.241  -0.304  1.00 26.79 ?  315  ASN E O   1 
ATOM   11201 C  CB  . ASN E  1 291 ? 21.442  34.344  -2.370  1.00 26.82 ?  315  ASN E CB  1 
ATOM   11202 C  CG  . ASN E  1 291 ? 21.286  35.517  -3.340  1.00 27.21 ?  315  ASN E CG  1 
ATOM   11203 O  OD1 . ASN E  1 291 ? 21.237  36.684  -2.937  1.00 26.14 ?  315  ASN E OD1 1 
ATOM   11204 N  ND2 . ASN E  1 291 ? 21.205  35.203  -4.631  1.00 27.09 ?  315  ASN E ND2 1 
ATOM   11205 N  N   . TRP E  1 292 ? 21.233  36.660  0.407   1.00 26.45 ?  316  TRP E N   1 
ATOM   11206 C  CA  . TRP E  1 292 ? 20.335  37.496  1.206   1.00 25.97 ?  316  TRP E CA  1 
ATOM   11207 C  C   . TRP E  1 292 ? 19.390  38.374  0.371   1.00 25.95 ?  316  TRP E C   1 
ATOM   11208 O  O   . TRP E  1 292 ? 18.394  38.880  0.892   1.00 25.59 ?  316  TRP E O   1 
ATOM   11209 C  CB  . TRP E  1 292 ? 21.143  38.377  2.165   1.00 25.77 ?  316  TRP E CB  1 
ATOM   11210 C  CG  . TRP E  1 292 ? 21.901  37.630  3.229   1.00 25.37 ?  316  TRP E CG  1 
ATOM   11211 C  CD1 . TRP E  1 292 ? 23.231  37.305  3.215   1.00 25.32 ?  316  TRP E CD1 1 
ATOM   11212 C  CD2 . TRP E  1 292 ? 21.381  37.137  4.473   1.00 24.66 ?  316  TRP E CD2 1 
ATOM   11213 N  NE1 . TRP E  1 292 ? 23.566  36.632  4.369   1.00 24.98 ?  316  TRP E NE1 1 
ATOM   11214 C  CE2 . TRP E  1 292 ? 22.450  36.516  5.157   1.00 24.56 ?  316  TRP E CE2 1 
ATOM   11215 C  CE3 . TRP E  1 292 ? 20.112  37.152  5.071   1.00 24.34 ?  316  TRP E CE3 1 
ATOM   11216 C  CZ2 . TRP E  1 292 ? 22.292  35.920  6.410   1.00 24.36 ?  316  TRP E CZ2 1 
ATOM   11217 C  CZ3 . TRP E  1 292 ? 19.955  36.557  6.320   1.00 24.36 ?  316  TRP E CZ3 1 
ATOM   11218 C  CH2 . TRP E  1 292 ? 21.041  35.950  6.975   1.00 24.01 ?  316  TRP E CH2 1 
ATOM   11219 N  N   . GLU E  1 293 ? 19.707  38.553  -0.912  1.00 26.01 ?  317  GLU E N   1 
ATOM   11220 C  CA  . GLU E  1 293 ? 18.927  39.427  -1.810  1.00 26.37 ?  317  GLU E CA  1 
ATOM   11221 C  C   . GLU E  1 293 ? 17.612  38.791  -2.252  1.00 26.27 ?  317  GLU E C   1 
ATOM   11222 O  O   . GLU E  1 293 ? 16.684  39.473  -2.695  1.00 26.55 ?  317  GLU E O   1 
ATOM   11223 C  CB  . GLU E  1 293 ? 19.756  39.814  -3.041  1.00 26.47 ?  317  GLU E CB  1 
ATOM   11224 C  CG  . GLU E  1 293 ? 20.959  40.704  -2.737  1.00 27.45 ?  317  GLU E CG  1 
ATOM   11225 C  CD  . GLU E  1 293 ? 20.583  42.136  -2.379  1.00 29.03 ?  317  GLU E CD  1 
ATOM   11226 O  OE1 . GLU E  1 293 ? 19.454  42.574  -2.694  1.00 30.03 ?  317  GLU E OE1 1 
ATOM   11227 O  OE2 . GLU E  1 293 ? 21.429  42.831  -1.782  1.00 30.27 -1 317  GLU E OE2 1 
ATOM   11228 N  N   . VAL E  1 294 ? 17.559  37.473  -2.133  1.00 26.12 ?  318  VAL E N   1 
ATOM   11229 C  CA  . VAL E  1 294 ? 16.386  36.679  -2.437  1.00 26.04 ?  318  VAL E CA  1 
ATOM   11230 C  C   . VAL E  1 294 ? 15.274  36.936  -1.405  1.00 26.10 ?  318  VAL E C   1 
ATOM   11231 O  O   . VAL E  1 294 ? 15.556  37.157  -0.220  1.00 26.01 ?  318  VAL E O   1 
ATOM   11232 C  CB  . VAL E  1 294 ? 16.816  35.186  -2.506  1.00 26.12 ?  318  VAL E CB  1 
ATOM   11233 C  CG1 . VAL E  1 294 ? 15.846  34.267  -1.816  1.00 25.97 ?  318  VAL E CG1 1 
ATOM   11234 C  CG2 . VAL E  1 294 ? 17.086  34.770  -3.945  1.00 25.79 ?  318  VAL E CG2 1 
ATOM   11235 N  N   . ARG E  1 295 ? 14.021  36.934  -1.857  1.00 25.97 ?  319  ARG E N   1 
ATOM   11236 C  CA  . ARG E  1 295 ? 12.885  37.137  -0.951  1.00 26.23 ?  319  ARG E CA  1 
ATOM   11237 C  C   . ARG E  1 295 ? 12.769  35.992  0.064   1.00 25.94 ?  319  ARG E C   1 
ATOM   11238 O  O   . ARG E  1 295 ? 13.218  34.877  -0.200  1.00 25.85 ?  319  ARG E O   1 
ATOM   11239 C  CB  . ARG E  1 295 ? 11.576  37.331  -1.734  1.00 26.36 ?  319  ARG E CB  1 
ATOM   11240 C  CG  . ARG E  1 295 ? 11.009  36.064  -2.334  1.00 27.33 ?  319  ARG E CG  1 
ATOM   11241 C  CD  . ARG E  1 295 ? 9.931   36.329  -3.385  1.00 28.93 ?  319  ARG E CD  1 
ATOM   11242 N  NE  . ARG E  1 295 ? 9.686   35.099  -4.133  1.00 30.19 ?  319  ARG E NE  1 
ATOM   11243 C  CZ  . ARG E  1 295 ? 8.588   34.814  -4.825  1.00 30.94 ?  319  ARG E CZ  1 
ATOM   11244 N  NH1 . ARG E  1 295 ? 7.573   35.671  -4.899  1.00 31.48 ?  319  ARG E NH1 1 
ATOM   11245 N  NH2 . ARG E  1 295 ? 8.510   33.648  -5.446  1.00 31.12 ?  319  ARG E NH2 1 
ATOM   11246 N  N   . LEU E  1 296 ? 12.183  36.276  1.226   1.00 25.86 ?  320  LEU E N   1 
ATOM   11247 C  CA  . LEU E  1 296 ? 12.072  35.282  2.300   1.00 25.80 ?  320  LEU E CA  1 
ATOM   11248 C  C   . LEU E  1 296 ? 11.416  33.974  1.844   1.00 26.04 ?  320  LEU E C   1 
ATOM   11249 O  O   . LEU E  1 296 ? 11.815  32.894  2.276   1.00 25.56 ?  320  LEU E O   1 
ATOM   11250 C  CB  . LEU E  1 296 ? 11.334  35.859  3.511   1.00 25.74 ?  320  LEU E CB  1 
ATOM   11251 C  CG  . LEU E  1 296 ? 12.070  36.868  4.402   1.00 25.51 ?  320  LEU E CG  1 
ATOM   11252 C  CD1 . LEU E  1 296 ? 11.104  37.483  5.396   1.00 25.04 ?  320  LEU E CD1 1 
ATOM   11253 C  CD2 . LEU E  1 296 ? 13.253  36.229  5.130   1.00 24.92 ?  320  LEU E CD2 1 
ATOM   11254 N  N   . LYS E  1 297 ? 10.429  34.089  0.955   1.00 26.54 ?  321  LYS E N   1 
ATOM   11255 C  CA  . LYS E  1 297 ? 9.743   32.939  0.366   1.00 27.24 ?  321  LYS E CA  1 
ATOM   11256 C  C   . LYS E  1 297 ? 10.705  32.008  -0.384  1.00 27.15 ?  321  LYS E C   1 
ATOM   11257 O  O   . LYS E  1 297 ? 10.485  30.795  -0.434  1.00 27.50 ?  321  LYS E O   1 
ATOM   11258 C  CB  . LYS E  1 297 ? 8.629   33.422  -0.569  1.00 27.60 ?  321  LYS E CB  1 
ATOM   11259 C  CG  . LYS E  1 297 ? 7.565   32.387  -0.878  1.00 29.73 ?  321  LYS E CG  1 
ATOM   11260 C  CD  . LYS E  1 297 ? 6.503   32.950  -1.818  1.00 32.57 ?  321  LYS E CD  1 
ATOM   11261 C  CE  . LYS E  1 297 ? 5.312   32.002  -1.912  1.00 33.93 ?  321  LYS E CE  1 
ATOM   11262 N  NZ  . LYS E  1 297 ? 4.304   32.448  -2.920  1.00 35.97 ?  321  LYS E NZ  1 
ATOM   11263 N  N   . ASP E  1 298 ? 11.767  32.581  -0.949  1.00 26.97 ?  322  ASP E N   1 
ATOM   11264 C  CA  . ASP E  1 298 ? 12.775  31.828  -1.704  1.00 26.91 ?  322  ASP E CA  1 
ATOM   11265 C  C   . ASP E  1 298 ? 14.044  31.510  -0.893  1.00 26.76 ?  322  ASP E C   1 
ATOM   11266 O  O   . ASP E  1 298 ? 14.943  30.830  -1.390  1.00 26.72 ?  322  ASP E O   1 
ATOM   11267 C  CB  . ASP E  1 298 ? 13.186  32.602  -2.966  1.00 26.86 ?  322  ASP E CB  1 
ATOM   11268 C  CG  . ASP E  1 298 ? 12.081  32.690  -4.008  1.00 27.30 ?  322  ASP E CG  1 
ATOM   11269 O  OD1 . ASP E  1 298 ? 11.166  31.838  -4.012  1.00 27.34 ?  322  ASP E OD1 1 
ATOM   11270 O  OD2 . ASP E  1 298 ? 12.141  33.623  -4.841  1.00 27.98 -1 322  ASP E OD2 1 
ATOM   11271 N  N   . ALA E  1 299 ? 14.122  32.014  0.338   1.00 26.56 ?  323  ALA E N   1 
ATOM   11272 C  CA  . ALA E  1 299 ? 15.347  31.922  1.139   1.00 26.50 ?  323  ALA E CA  1 
ATOM   11273 C  C   . ALA E  1 299 ? 15.871  30.493  1.291   1.00 26.63 ?  323  ALA E C   1 
ATOM   11274 O  O   . ALA E  1 299 ? 17.063  30.244  1.108   1.00 26.23 ?  323  ALA E O   1 
ATOM   11275 C  CB  . ALA E  1 299 ? 15.145  32.564  2.508   1.00 26.27 ?  323  ALA E CB  1 
ATOM   11276 N  N   . PHE E  1 300 ? 14.972  29.564  1.615   1.00 26.94 ?  324  PHE E N   1 
ATOM   11277 C  CA  . PHE E  1 300 ? 15.359  28.183  1.905   1.00 27.47 ?  324  PHE E CA  1 
ATOM   11278 C  C   . PHE E  1 300 ? 15.650  27.334  0.662   1.00 27.74 ?  324  PHE E C   1 
ATOM   11279 O  O   . PHE E  1 300 ? 16.192  26.238  0.784   1.00 28.09 ?  324  PHE E O   1 
ATOM   11280 C  CB  . PHE E  1 300 ? 14.315  27.493  2.794   1.00 27.42 ?  324  PHE E CB  1 
ATOM   11281 C  CG  . PHE E  1 300 ? 14.145  28.130  4.153   1.00 27.38 ?  324  PHE E CG  1 
ATOM   11282 C  CD1 . PHE E  1 300 ? 15.242  28.639  4.850   1.00 27.35 ?  324  PHE E CD1 1 
ATOM   11283 C  CD2 . PHE E  1 300 ? 12.888  28.194  4.747   1.00 26.89 ?  324  PHE E CD2 1 
ATOM   11284 C  CE1 . PHE E  1 300 ? 15.083  29.224  6.108   1.00 27.16 ?  324  PHE E CE1 1 
ATOM   11285 C  CE2 . PHE E  1 300 ? 12.718  28.774  6.005   1.00 27.10 ?  324  PHE E CE2 1 
ATOM   11286 C  CZ  . PHE E  1 300 ? 13.819  29.289  6.688   1.00 27.08 ?  324  PHE E CZ  1 
ATOM   11287 N  N   . SER E  1 301 ? 15.293  27.830  -0.520  1.00 27.96 ?  325  SER E N   1 
ATOM   11288 C  CA  . SER E  1 301 ? 15.602  27.122  -1.765  1.00 28.23 ?  325  SER E CA  1 
ATOM   11289 C  C   . SER E  1 301 ? 16.649  27.866  -2.595  1.00 28.26 ?  325  SER E C   1 
ATOM   11290 O  O   . SER E  1 301 ? 17.819  27.463  -2.636  1.00 28.35 ?  325  SER E O   1 
ATOM   11291 C  CB  . SER E  1 301 ? 14.331  26.843  -2.585  1.00 28.30 ?  325  SER E CB  1 
ATOM   11292 O  OG  . SER E  1 301 ? 13.563  28.019  -2.775  1.00 28.60 ?  325  SER E OG  1 
ATOM   11293 N  N   . LYS E  1 302 ? 16.229  28.959  -3.227  1.00 27.99 ?  326  LYS E N   1 
ATOM   11294 C  CA  . LYS E  1 302 ? 17.108  29.758  -4.083  1.00 28.01 ?  326  LYS E CA  1 
ATOM   11295 C  C   . LYS E  1 302 ? 18.192  30.517  -3.309  1.00 27.62 ?  326  LYS E C   1 
ATOM   11296 O  O   . LYS E  1 302 ? 19.234  30.855  -3.869  1.00 27.42 ?  326  LYS E O   1 
ATOM   11297 C  CB  . LYS E  1 302 ? 16.283  30.725  -4.931  1.00 28.33 ?  326  LYS E CB  1 
ATOM   11298 C  CG  . LYS E  1 302 ? 15.431  30.036  -5.986  1.00 29.47 ?  326  LYS E CG  1 
ATOM   11299 C  CD  . LYS E  1 302 ? 14.346  30.959  -6.506  1.00 30.90 ?  326  LYS E CD  1 
ATOM   11300 C  CE  . LYS E  1 302 ? 13.492  30.265  -7.559  1.00 31.78 ?  326  LYS E CE  1 
ATOM   11301 N  NZ  . LYS E  1 302 ? 12.465  31.196  -8.102  1.00 32.88 ?  326  LYS E NZ  1 
ATOM   11302 N  N   . GLY E  1 303 ? 17.943  30.780  -2.028  1.00 27.30 ?  327  GLY E N   1 
ATOM   11303 C  CA  . GLY E  1 303 ? 18.904  31.484  -1.183  1.00 26.98 ?  327  GLY E CA  1 
ATOM   11304 C  C   . GLY E  1 303 ? 19.981  30.580  -0.612  1.00 26.81 ?  327  GLY E C   1 
ATOM   11305 O  O   . GLY E  1 303 ? 21.076  31.043  -0.291  1.00 26.93 ?  327  GLY E O   1 
ATOM   11306 N  N   . GLY E  1 304 ? 19.669  29.291  -0.485  1.00 26.56 ?  328  GLY E N   1 
ATOM   11307 C  CA  . GLY E  1 304 ? 20.604  28.304  0.052   1.00 26.14 ?  328  GLY E CA  1 
ATOM   11308 C  C   . GLY E  1 304 ? 20.651  28.297  1.569   1.00 26.01 ?  328  GLY E C   1 
ATOM   11309 O  O   . GLY E  1 304 ? 21.518  27.652  2.163   1.00 26.11 ?  328  GLY E O   1 
ATOM   11310 N  N   . GLN E  1 305 ? 19.709  29.009  2.188   1.00 25.72 ?  329  GLN E N   1 
ATOM   11311 C  CA  . GLN E  1 305 ? 19.664  29.186  3.640   1.00 25.29 ?  329  GLN E CA  1 
ATOM   11312 C  C   . GLN E  1 305 ? 19.226  27.894  4.312   1.00 25.01 ?  329  GLN E C   1 
ATOM   11313 O  O   . GLN E  1 305 ? 18.182  27.336  3.976   1.00 25.11 ?  329  GLN E O   1 
ATOM   11314 C  CB  . GLN E  1 305 ? 18.728  30.345  4.008   1.00 25.35 ?  329  GLN E CB  1 
ATOM   11315 C  CG  . GLN E  1 305 ? 18.628  30.636  5.507   1.00 25.23 ?  329  GLN E CG  1 
ATOM   11316 C  CD  . GLN E  1 305 ? 17.926  31.954  5.827   1.00 25.14 ?  329  GLN E CD  1 
ATOM   11317 O  OE1 . GLN E  1 305 ? 17.881  32.872  5.005   1.00 24.91 ?  329  GLN E OE1 1 
ATOM   11318 N  NE2 . GLN E  1 305 ? 17.383  32.051  7.039   1.00 25.03 ?  329  GLN E NE2 1 
ATOM   11319 N  N   . ASN E  1 306 ? 20.038  27.419  5.253   1.00 24.58 ?  330  ASN E N   1 
ATOM   11320 C  CA  . ASN E  1 306 ? 19.799  26.129  5.892   1.00 24.28 ?  330  ASN E CA  1 
ATOM   11321 C  C   . ASN E  1 306 ? 19.559  26.236  7.394   1.00 23.94 ?  330  ASN E C   1 
ATOM   11322 O  O   . ASN E  1 306 ? 19.349  25.227  8.073   1.00 24.03 ?  330  ASN E O   1 
ATOM   11323 C  CB  . ASN E  1 306 ? 20.952  25.158  5.596   1.00 24.42 ?  330  ASN E CB  1 
ATOM   11324 C  CG  . ASN E  1 306 ? 22.206  25.469  6.397   1.00 25.08 ?  330  ASN E CG  1 
ATOM   11325 O  OD1 . ASN E  1 306 ? 22.707  26.598  6.394   1.00 25.52 ?  330  ASN E OD1 1 
ATOM   11326 N  ND2 . ASN E  1 306 ? 22.717  24.460  7.094   1.00 25.86 ?  330  ASN E ND2 1 
ATOM   11327 N  N   . ALA E  1 307 ? 19.602  27.463  7.902   1.00 23.43 ?  331  ALA E N   1 
ATOM   11328 C  CA  . ALA E  1 307 ? 19.343  27.734  9.310   1.00 23.01 ?  331  ALA E CA  1 
ATOM   11329 C  C   . ALA E  1 307 ? 18.371  28.905  9.422   1.00 22.59 ?  331  ALA E C   1 
ATOM   11330 O  O   . ALA E  1 307 ? 18.420  29.827  8.604   1.00 22.91 ?  331  ALA E O   1 
ATOM   11331 C  CB  . ALA E  1 307 ? 20.647  28.031  10.043  1.00 22.92 ?  331  ALA E CB  1 
ATOM   11332 N  N   . PRO E  1 308 ? 17.481  28.879  10.430  1.00 22.14 ?  332  PRO E N   1 
ATOM   11333 C  CA  . PRO E  1 308 ? 16.448  29.910  10.496  1.00 21.87 ?  332  PRO E CA  1 
ATOM   11334 C  C   . PRO E  1 308 ? 16.958  31.239  11.051  1.00 21.64 ?  332  PRO E C   1 
ATOM   11335 O  O   . PRO E  1 308 ? 17.947  31.279  11.790  1.00 21.49 ?  332  PRO E O   1 
ATOM   11336 C  CB  . PRO E  1 308 ? 15.412  29.300  11.439  1.00 21.79 ?  332  PRO E CB  1 
ATOM   11337 C  CG  . PRO E  1 308 ? 16.215  28.466  12.369  1.00 21.84 ?  332  PRO E CG  1 
ATOM   11338 C  CD  . PRO E  1 308 ? 17.387  27.938  11.562  1.00 22.01 ?  332  PRO E CD  1 
ATOM   11339 N  N   . THR E  1 309 ? 16.270  32.312  10.678  1.00 21.42 ?  333  THR E N   1 
ATOM   11340 C  CA  . THR E  1 309 ? 16.606  33.664  11.102  1.00 21.11 ?  333  THR E CA  1 
ATOM   11341 C  C   . THR E  1 309 ? 15.353  34.331  11.671  1.00 20.86 ?  333  THR E C   1 
ATOM   11342 O  O   . THR E  1 309 ? 14.237  33.853  11.436  1.00 20.87 ?  333  THR E O   1 
ATOM   11343 C  CB  . THR E  1 309 ? 17.110  34.492  9.911   1.00 21.12 ?  333  THR E CB  1 
ATOM   11344 O  OG1 . THR E  1 309 ? 16.188  34.354  8.828   1.00 21.03 ?  333  THR E OG1 1 
ATOM   11345 C  CG2 . THR E  1 309 ? 18.493  34.018  9.459   1.00 21.15 ?  333  THR E CG2 1 
ATOM   11346 N  N   . CYS E  1 310 ? 15.536  35.434  12.398  1.00 20.47 ?  334  CYS E N   1 
ATOM   11347 C  CA  . CYS E  1 310 ? 14.419  36.194  12.975  1.00 20.15 ?  334  CYS E CA  1 
ATOM   11348 C  C   . CYS E  1 310 ? 13.292  36.420  11.970  1.00 20.20 ?  334  CYS E C   1 
ATOM   11349 O  O   . CYS E  1 310 ? 12.139  36.080  12.237  1.00 20.07 ?  334  CYS E O   1 
ATOM   11350 C  CB  . CYS E  1 310 ? 14.881  37.555  13.497  1.00 20.07 ?  334  CYS E CB  1 
ATOM   11351 S  SG  . CYS E  1 310 ? 16.475  37.597  14.308  1.00 18.85 ?  334  CYS E SG  1 
ATOM   11352 N  N   . ALA E  1 311 ? 13.638  36.993  10.817  1.00 20.44 ?  335  ALA E N   1 
ATOM   11353 C  CA  . ALA E  1 311 ? 12.651  37.363  9.805   1.00 20.65 ?  335  ALA E CA  1 
ATOM   11354 C  C   . ALA E  1 311 ? 11.946  36.146  9.214   1.00 20.74 ?  335  ALA E C   1 
ATOM   11355 O  O   . ALA E  1 311 ? 10.722  36.141  9.091   1.00 20.86 ?  335  ALA E O   1 
ATOM   11356 C  CB  . ALA E  1 311 ? 13.288  38.214  8.706   1.00 20.50 ?  335  ALA E CB  1 
ATOM   11357 N  N   . ALA E  1 312 ? 12.714  35.114  8.869   1.00 21.03 ?  336  ALA E N   1 
ATOM   11358 C  CA  . ALA E  1 312 ? 12.150  33.886  8.295   1.00 21.18 ?  336  ALA E CA  1 
ATOM   11359 C  C   . ALA E  1 312 ? 11.172  33.191  9.249   1.00 21.38 ?  336  ALA E C   1 
ATOM   11360 O  O   . ALA E  1 312 ? 10.134  32.690  8.820   1.00 21.69 ?  336  ALA E O   1 
ATOM   11361 C  CB  . ALA E  1 312 ? 13.253  32.934  7.867   1.00 21.15 ?  336  ALA E CB  1 
ATOM   11362 N  N   . CYS E  1 313 ? 11.496  33.172  10.539  1.00 21.33 ?  337  CYS E N   1 
ATOM   11363 C  CA  . CYS E  1 313 ? 10.607  32.573  11.531  1.00 21.46 ?  337  CYS E CA  1 
ATOM   11364 C  C   . CYS E  1 313 ? 9.407   33.447  11.874  1.00 21.61 ?  337  CYS E C   1 
ATOM   11365 O  O   . CYS E  1 313 ? 8.278   32.959  11.934  1.00 21.61 ?  337  CYS E O   1 
ATOM   11366 C  CB  . CYS E  1 313 ? 11.367  32.215  12.808  1.00 21.38 ?  337  CYS E CB  1 
ATOM   11367 S  SG  . CYS E  1 313 ? 12.097  30.557  12.809  1.00 21.07 ?  337  CYS E SG  1 
ATOM   11368 N  N   . HIS E  1 314 ? 9.648   34.736  12.094  1.00 21.83 ?  338  HIS E N   1 
ATOM   11369 C  CA  . HIS E  1 314 ? 8.607   35.613  12.629  1.00 22.18 ?  338  HIS E CA  1 
ATOM   11370 C  C   . HIS E  1 314 ? 7.719   36.299  11.578  1.00 22.41 ?  338  HIS E C   1 
ATOM   11371 O  O   . HIS E  1 314 ? 6.600   36.697  11.891  1.00 22.45 ?  338  HIS E O   1 
ATOM   11372 C  CB  . HIS E  1 314 ? 9.195   36.614  13.636  1.00 21.89 ?  338  HIS E CB  1 
ATOM   11373 C  CG  . HIS E  1 314 ? 9.602   35.985  14.934  1.00 21.87 ?  338  HIS E CG  1 
ATOM   11374 N  ND1 . HIS E  1 314 ? 8.690   35.640  15.907  1.00 21.85 ?  338  HIS E ND1 1 
ATOM   11375 C  CD2 . HIS E  1 314 ? 10.817  35.630  15.418  1.00 21.59 ?  338  HIS E CD2 1 
ATOM   11376 C  CE1 . HIS E  1 314 ? 9.323   35.100  16.933  1.00 20.99 ?  338  HIS E CE1 1 
ATOM   11377 N  NE2 . HIS E  1 314 ? 10.617  35.085  16.666  1.00 21.10 ?  338  HIS E NE2 1 
ATOM   11378 N  N   . MET E  1 315 ? 8.203   36.417  10.342  1.00 22.93 ?  339  MET E N   1 
ATOM   11379 C  CA  . MET E  1 315 ? 7.382   36.962  9.250   1.00 23.69 ?  339  MET E CA  1 
ATOM   11380 C  C   . MET E  1 315 ? 6.637   35.891  8.447   1.00 24.04 ?  339  MET E C   1 
ATOM   11381 O  O   . MET E  1 315 ? 5.795   36.213  7.604   1.00 24.30 ?  339  MET E O   1 
ATOM   11382 C  CB  . MET E  1 315 ? 8.205   37.875  8.333   1.00 23.76 ?  339  MET E CB  1 
ATOM   11383 C  CG  . MET E  1 315 ? 8.448   39.257  8.931   1.00 24.53 ?  339  MET E CG  1 
ATOM   11384 S  SD  . MET E  1 315 ? 9.646   40.261  8.035   1.00 27.39 ?  339  MET E SD  1 
ATOM   11385 C  CE  . MET E  1 315 ? 8.702   40.785  6.604   1.00 25.64 ?  339  MET E CE  1 
ATOM   11386 N  N   . GLU E  1 316 ? 6.939   34.623  8.715   1.00 24.52 ?  340  GLU E N   1 
ATOM   11387 C  CA  . GLU E  1 316 ? 6.215   33.511  8.097   1.00 25.03 ?  340  GLU E CA  1 
ATOM   11388 C  C   . GLU E  1 316 ? 4.876   33.295  8.795   1.00 25.27 ?  340  GLU E C   1 
ATOM   11389 O  O   . GLU E  1 316 ? 4.785   33.357  10.019  1.00 25.29 ?  340  GLU E O   1 
ATOM   11390 C  CB  . GLU E  1 316 ? 7.047   32.219  8.147   1.00 24.83 ?  340  GLU E CB  1 
ATOM   11391 C  CG  . GLU E  1 316 ? 6.565   31.086  7.225   1.00 25.16 ?  340  GLU E CG  1 
ATOM   11392 C  CD  . GLU E  1 316 ? 5.494   30.188  7.847   1.00 25.96 ?  340  GLU E CD  1 
ATOM   11393 O  OE1 . GLU E  1 316 ? 5.396   30.117  9.087   1.00 26.37 ?  340  GLU E OE1 1 
ATOM   11394 O  OE2 . GLU E  1 316 ? 4.749   29.536  7.087   1.00 26.82 -1 340  GLU E OE2 1 
ATOM   11395 N  N   . TYR E  1 317 ? 3.838   33.052  8.002   1.00 25.88 ?  341  TYR E N   1 
ATOM   11396 C  CA  . TYR E  1 317 ? 2.545   32.629  8.528   1.00 26.36 ?  341  TYR E CA  1 
ATOM   11397 C  C   . TYR E  1 317 ? 1.787   31.811  7.492   1.00 26.67 ?  341  TYR E C   1 
ATOM   11398 O  O   . TYR E  1 317 ? 1.436   32.319  6.424   1.00 26.59 ?  341  TYR E O   1 
ATOM   11399 C  CB  . TYR E  1 317 ? 1.705   33.826  8.980   1.00 26.36 ?  341  TYR E CB  1 
ATOM   11400 C  CG  . TYR E  1 317 ? 0.405   33.416  9.628   1.00 26.55 ?  341  TYR E CG  1 
ATOM   11401 C  CD1 . TYR E  1 317 ? 0.393   32.831  10.893  1.00 26.02 ?  341  TYR E CD1 1 
ATOM   11402 C  CD2 . TYR E  1 317 ? -0.813  33.597  8.970   1.00 27.37 ?  341  TYR E CD2 1 
ATOM   11403 C  CE1 . TYR E  1 317 ? -0.798  32.442  11.495  1.00 26.64 ?  341  TYR E CE1 1 
ATOM   11404 C  CE2 . TYR E  1 317 ? -2.017  33.214  9.565   1.00 27.52 ?  341  TYR E CE2 1 
ATOM   11405 C  CZ  . TYR E  1 317 ? -1.997  32.638  10.829  1.00 27.40 ?  341  TYR E CZ  1 
ATOM   11406 O  OH  . TYR E  1 317 ? -3.172  32.253  11.427  1.00 28.16 ?  341  TYR E OH  1 
ATOM   11407 N  N   . GLU E  1 318 ? 1.550   30.541  7.823   1.00 27.07 ?  342  GLU E N   1 
ATOM   11408 C  CA  . GLU E  1 318 ? 0.803   29.607  6.966   1.00 27.59 ?  342  GLU E CA  1 
ATOM   11409 C  C   . GLU E  1 318 ? 1.285   29.578  5.503   1.00 27.66 ?  342  GLU E C   1 
ATOM   11410 O  O   . GLU E  1 318 ? 0.475   29.582  4.568   1.00 27.80 ?  342  GLU E O   1 
ATOM   11411 C  CB  . GLU E  1 318 ? -0.711  29.877  7.047   1.00 27.78 ?  342  GLU E CB  1 
ATOM   11412 C  CG  . GLU E  1 318 ? -1.325  29.672  8.437   1.00 28.68 ?  342  GLU E CG  1 
ATOM   11413 C  CD  . GLU E  1 318 ? -1.286  28.223  8.897   1.00 29.81 ?  342  GLU E CD  1 
ATOM   11414 O  OE1 . GLU E  1 318 ? -1.028  27.982  10.095  1.00 29.86 ?  342  GLU E OE1 1 
ATOM   11415 O  OE2 . GLU E  1 318 ? -1.503  27.322  8.059   1.00 31.01 -1 342  GLU E OE2 1 
ATOM   11416 N  N   . GLY E  1 319 ? 2.605   29.558  5.322   1.00 27.57 ?  343  GLY E N   1 
ATOM   11417 C  CA  . GLY E  1 319 ? 3.218   29.466  3.995   1.00 27.65 ?  343  GLY E CA  1 
ATOM   11418 C  C   . GLY E  1 319 ? 3.469   30.774  3.256   1.00 27.66 ?  343  GLY E C   1 
ATOM   11419 O  O   . GLY E  1 319 ? 3.963   30.762  2.130   1.00 27.85 ?  343  GLY E O   1 
ATOM   11420 N  N   . GLU E  1 320 ? 3.131   31.903  3.875   1.00 27.43 ?  344  GLU E N   1 
ATOM   11421 C  CA  . GLU E  1 320 ? 3.362   33.209  3.250   1.00 27.35 ?  344  GLU E CA  1 
ATOM   11422 C  C   . GLU E  1 320 ? 4.142   34.158  4.171   1.00 26.68 ?  344  GLU E C   1 
ATOM   11423 O  O   . GLU E  1 320 ? 4.191   33.962  5.383   1.00 26.46 ?  344  GLU E O   1 
ATOM   11424 C  CB  . GLU E  1 320 ? 2.030   33.829  2.794   1.00 27.72 ?  344  GLU E CB  1 
ATOM   11425 C  CG  . GLU E  1 320 ? 2.127   35.199  2.104   1.00 29.36 ?  344  GLU E CG  1 
ATOM   11426 C  CD  . GLU E  1 320 ? 2.879   35.161  0.776   1.00 31.56 ?  344  GLU E CD  1 
ATOM   11427 O  OE1 . GLU E  1 320 ? 4.133   35.147  0.787   1.00 31.26 ?  344  GLU E OE1 1 
ATOM   11428 O  OE2 . GLU E  1 320 ? 2.207   35.169  -0.280  1.00 32.98 -1 344  GLU E OE2 1 
ATOM   11429 N  N   . TYR E  1 321 ? 4.756   35.177  3.576   1.00 26.07 ?  345  TYR E N   1 
ATOM   11430 C  CA  . TYR E  1 321 ? 5.514   36.174  4.320   1.00 25.50 ?  345  TYR E CA  1 
ATOM   11431 C  C   . TYR E  1 321 ? 4.899   37.565  4.187   1.00 24.98 ?  345  TYR E C   1 
ATOM   11432 O  O   . TYR E  1 321 ? 4.649   38.041  3.073   1.00 24.89 ?  345  TYR E O   1 
ATOM   11433 C  CB  . TYR E  1 321 ? 6.978   36.183  3.861   1.00 25.57 ?  345  TYR E CB  1 
ATOM   11434 C  CG  . TYR E  1 321 ? 7.734   34.917  4.204   1.00 25.95 ?  345  TYR E CG  1 
ATOM   11435 C  CD1 . TYR E  1 321 ? 7.710   33.814  3.352   1.00 26.31 ?  345  TYR E CD1 1 
ATOM   11436 C  CD2 . TYR E  1 321 ? 8.463   34.819  5.388   1.00 26.26 ?  345  TYR E CD2 1 
ATOM   11437 C  CE1 . TYR E  1 321 ? 8.397   32.647  3.668   1.00 27.24 ?  345  TYR E CE1 1 
ATOM   11438 C  CE2 . TYR E  1 321 ? 9.158   33.663  5.711   1.00 26.91 ?  345  TYR E CE2 1 
ATOM   11439 C  CZ  . TYR E  1 321 ? 9.122   32.581  4.848   1.00 27.99 ?  345  TYR E CZ  1 
ATOM   11440 O  OH  . TYR E  1 321 ? 9.805   31.430  5.168   1.00 28.76 ?  345  TYR E OH  1 
ATOM   11441 N  N   . THR E  1 322 ? 4.643   38.200  5.331   1.00 24.42 ?  346  THR E N   1 
ATOM   11442 C  CA  . THR E  1 322 ? 4.116   39.571  5.382   1.00 23.87 ?  346  THR E CA  1 
ATOM   11443 C  C   . THR E  1 322 ? 4.852   40.407  6.439   1.00 23.92 ?  346  THR E C   1 
ATOM   11444 O  O   . THR E  1 322 ? 5.595   39.866  7.265   1.00 23.71 ?  346  THR E O   1 
ATOM   11445 C  CB  . THR E  1 322 ? 2.582   39.615  5.682   1.00 23.78 ?  346  THR E CB  1 
ATOM   11446 O  OG1 . THR E  1 322 ? 2.338   39.304  7.058   1.00 23.23 ?  346  THR E OG1 1 
ATOM   11447 C  CG2 . THR E  1 322 ? 1.783   38.655  4.779   1.00 23.10 ?  346  THR E CG2 1 
ATOM   11448 N  N   . HIS E  1 323 ? 4.630   41.721  6.413   1.00 23.78 ?  347  HIS E N   1 
ATOM   11449 C  CA  . HIS E  1 323 ? 5.143   42.628  7.443   1.00 23.71 ?  347  HIS E CA  1 
ATOM   11450 C  C   . HIS E  1 323 ? 4.335   42.564  8.752   1.00 23.75 ?  347  HIS E C   1 
ATOM   11451 O  O   . HIS E  1 323 ? 4.568   43.361  9.661   1.00 24.14 ?  347  HIS E O   1 
ATOM   11452 C  CB  . HIS E  1 323 ? 5.191   44.075  6.918   1.00 23.64 ?  347  HIS E CB  1 
ATOM   11453 C  CG  . HIS E  1 323 ? 6.453   44.426  6.183   1.00 23.32 ?  347  HIS E CG  1 
ATOM   11454 N  ND1 . HIS E  1 323 ? 6.823   43.822  5.002   1.00 22.35 ?  347  HIS E ND1 1 
ATOM   11455 C  CD2 . HIS E  1 323 ? 7.412   45.349  6.447   1.00 23.39 ?  347  HIS E CD2 1 
ATOM   11456 C  CE1 . HIS E  1 323 ? 7.963   44.342  4.580   1.00 22.56 ?  347  HIS E CE1 1 
ATOM   11457 N  NE2 . HIS E  1 323 ? 8.344   45.273  5.438   1.00 21.88 ?  347  HIS E NE2 1 
ATOM   11458 N  N   . ASN E  1 324 ? 3.378   41.641  8.837   1.00 23.57 ?  348  ASN E N   1 
ATOM   11459 C  CA  . ASN E  1 324 ? 2.625   41.389  10.075  1.00 23.52 ?  348  ASN E CA  1 
ATOM   11460 C  C   . ASN E  1 324 ? 3.331   40.287  10.858  1.00 23.40 ?  348  ASN E C   1 
ATOM   11461 O  O   . ASN E  1 324 ? 3.461   39.162  10.369  1.00 23.31 ?  348  ASN E O   1 
ATOM   11462 C  CB  . ASN E  1 324 ? 1.172   40.989  9.747   1.00 23.45 ?  348  ASN E CB  1 
ATOM   11463 C  CG  . ASN E  1 324 ? 0.307   40.744  10.995  1.00 23.74 ?  348  ASN E CG  1 
ATOM   11464 O  OD1 . ASN E  1 324 ? 0.759   40.184  11.996  1.00 23.90 ?  348  ASN E OD1 1 
ATOM   11465 N  ND2 . ASN E  1 324 ? -0.961  41.143  10.915  1.00 23.52 ?  348  ASN E ND2 1 
ATOM   11466 N  N   . ILE E  1 325 ? 3.791   40.613  12.068  1.00 23.36 ?  349  ILE E N   1 
ATOM   11467 C  CA  . ILE E  1 325 ? 4.590   39.670  12.865  1.00 23.14 ?  349  ILE E CA  1 
ATOM   11468 C  C   . ILE E  1 325 ? 3.883   39.101  14.102  1.00 22.96 ?  349  ILE E C   1 
ATOM   11469 O  O   . ILE E  1 325 ? 4.522   38.475  14.953  1.00 22.82 ?  349  ILE E O   1 
ATOM   11470 C  CB  . ILE E  1 325 ? 5.999   40.257  13.260  1.00 23.22 ?  349  ILE E CB  1 
ATOM   11471 C  CG1 . ILE E  1 325 ? 5.913   41.689  13.818  1.00 23.09 ?  349  ILE E CG1 1 
ATOM   11472 C  CG2 . ILE E  1 325 ? 6.927   40.242  12.063  1.00 23.31 ?  349  ILE E CG2 1 
ATOM   11473 C  CD1 . ILE E  1 325 ? 5.216   41.835  15.176  1.00 22.86 ?  349  ILE E CD1 1 
ATOM   11474 N  N   . THR E  1 326 ? 2.567   39.294  14.179  1.00 22.73 ?  350  THR E N   1 
ATOM   11475 C  CA  . THR E  1 326 ? 1.805   39.026  15.408  1.00 22.53 ?  350  THR E CA  1 
ATOM   11476 C  C   . THR E  1 326 ? 1.075   37.689  15.494  1.00 22.63 ?  350  THR E C   1 
ATOM   11477 O  O   . THR E  1 326 ? 0.688   37.270  16.587  1.00 22.82 ?  350  THR E O   1 
ATOM   11478 C  CB  . THR E  1 326 ? 0.721   40.106  15.635  1.00 22.64 ?  350  THR E CB  1 
ATOM   11479 O  OG1 . THR E  1 326 ? -0.181  40.117  14.521  1.00 22.04 ?  350  THR E OG1 1 
ATOM   11480 C  CG2 . THR E  1 326 ? 1.341   41.485  15.823  1.00 21.77 ?  350  THR E CG2 1 
ATOM   11481 N  N   . ARG E  1 327 ? 0.877   37.025  14.361  1.00 22.68 ?  351  ARG E N   1 
ATOM   11482 C  CA  . ARG E  1 327 ? -0.145  35.972  14.278  1.00 23.15 ?  351  ARG E CA  1 
ATOM   11483 C  C   . ARG E  1 327 ? 0.170   34.614  14.925  1.00 23.09 ?  351  ARG E C   1 
ATOM   11484 O  O   . ARG E  1 327 ? -0.729  33.780  15.068  1.00 23.37 ?  351  ARG E O   1 
ATOM   11485 C  CB  . ARG E  1 327 ? -0.641  35.809  12.838  1.00 23.23 ?  351  ARG E CB  1 
ATOM   11486 C  CG  . ARG E  1 327 ? -1.414  37.029  12.333  1.00 23.91 ?  351  ARG E CG  1 
ATOM   11487 C  CD  . ARG E  1 327 ? -1.790  36.905  10.870  1.00 24.92 ?  351  ARG E CD  1 
ATOM   11488 N  NE  . ARG E  1 327 ? -0.636  37.032  9.983   1.00 26.72 ?  351  ARG E NE  1 
ATOM   11489 C  CZ  . ARG E  1 327 ? -0.704  37.020  8.654   1.00 27.72 ?  351  ARG E CZ  1 
ATOM   11490 N  NH1 . ARG E  1 327 ? -1.877  36.888  8.042   1.00 28.12 ?  351  ARG E NH1 1 
ATOM   11491 N  NH2 . ARG E  1 327 ? 0.403   37.142  7.931   1.00 27.74 ?  351  ARG E NH2 1 
ATOM   11492 N  N   . LYS E  1 328 ? 1.418   34.402  15.339  1.00 22.87 ?  352  LYS E N   1 
ATOM   11493 C  CA  . LYS E  1 328 ? 1.809   33.140  15.982  1.00 22.46 ?  352  LYS E CA  1 
ATOM   11494 C  C   . LYS E  1 328 ? 2.175   33.318  17.458  1.00 22.32 ?  352  LYS E C   1 
ATOM   11495 O  O   . LYS E  1 328 ? 2.541   32.354  18.145  1.00 22.01 ?  352  LYS E O   1 
ATOM   11496 C  CB  . LYS E  1 328 ? 2.962   32.479  15.220  1.00 22.39 ?  352  LYS E CB  1 
ATOM   11497 C  CG  . LYS E  1 328 ? 2.604   32.045  13.797  1.00 22.13 ?  352  LYS E CG  1 
ATOM   11498 C  CD  . LYS E  1 328 ? 3.732   31.286  13.111  1.00 21.55 ?  352  LYS E CD  1 
ATOM   11499 C  CE  . LYS E  1 328 ? 5.027   32.097  13.044  1.00 21.23 ?  352  LYS E CE  1 
ATOM   11500 N  NZ  . LYS E  1 328 ? 5.954   31.527  12.039  1.00 21.38 ?  352  LYS E NZ  1 
ATOM   11501 N  N   . THR E  1 329 ? 2.061   34.554  17.937  1.00 22.09 ?  353  THR E N   1 
ATOM   11502 C  CA  . THR E  1 329 ? 2.444   34.914  19.301  1.00 21.93 ?  353  THR E CA  1 
ATOM   11503 C  C   . THR E  1 329 ? 1.522   34.284  20.341  1.00 21.91 ?  353  THR E C   1 
ATOM   11504 O  O   . THR E  1 329 ? 0.300   34.407  20.244  1.00 21.83 ?  353  THR E O   1 
ATOM   11505 C  CB  . THR E  1 329 ? 2.433   36.441  19.477  1.00 21.95 ?  353  THR E CB  1 
ATOM   11506 O  OG1 . THR E  1 329 ? 3.264   37.038  18.475  1.00 21.84 ?  353  THR E OG1 1 
ATOM   11507 C  CG2 . THR E  1 329 ? 2.936   36.829  20.861  1.00 21.42 ?  353  THR E CG2 1 
ATOM   11508 N  N   . ARG E  1 330 ? 2.120   33.632  21.339  1.00 21.83 ?  354  ARG E N   1 
ATOM   11509 C  CA  . ARG E  1 330 ? 1.374   32.933  22.388  1.00 21.90 ?  354  ARG E CA  1 
ATOM   11510 C  C   . ARG E  1 330 ? 1.790   33.387  23.796  1.00 21.83 ?  354  ARG E C   1 
ATOM   11511 O  O   . ARG E  1 330 ? 0.934   33.712  24.631  1.00 21.62 ?  354  ARG E O   1 
ATOM   11512 C  CB  . ARG E  1 330 ? 1.559   31.411  22.260  1.00 22.07 ?  354  ARG E CB  1 
ATOM   11513 C  CG  . ARG E  1 330 ? 1.208   30.807  20.888  1.00 22.46 ?  354  ARG E CG  1 
ATOM   11514 C  CD  . ARG E  1 330 ? 1.267   29.283  20.934  1.00 24.57 ?  354  ARG E CD  1 
ATOM   11515 N  NE  . ARG E  1 330 ? 2.499   28.864  21.588  1.00 27.37 ?  354  ARG E NE  1 
ATOM   11516 C  CZ  . ARG E  1 330 ? 2.617   27.851  22.435  1.00 26.75 ?  354  ARG E CZ  1 
ATOM   11517 N  NH1 . ARG E  1 330 ? 1.581   27.091  22.756  1.00 26.60 ?  354  ARG E NH1 1 
ATOM   11518 N  NH2 . ARG E  1 330 ? 3.799   27.607  22.962  1.00 28.29 ?  354  ARG E NH2 1 
ATOM   11519 N  N   . TRP E  1 331 ? 3.101   33.395  24.049  1.00 21.54 ?  355  TRP E N   1 
ATOM   11520 C  CA  . TRP E  1 331 ? 3.663   33.785  25.349  1.00 21.34 ?  355  TRP E CA  1 
ATOM   11521 C  C   . TRP E  1 331 ? 3.910   35.284  25.467  1.00 21.35 ?  355  TRP E C   1 
ATOM   11522 O  O   . TRP E  1 331 ? 3.827   35.841  26.563  1.00 21.21 ?  355  TRP E O   1 
ATOM   11523 C  CB  . TRP E  1 331 ? 4.981   33.048  25.606  1.00 21.26 ?  355  TRP E CB  1 
ATOM   11524 C  CG  . TRP E  1 331 ? 4.800   31.667  26.154  1.00 20.90 ?  355  TRP E CG  1 
ATOM   11525 C  CD1 . TRP E  1 331 ? 4.979   30.493  25.486  1.00 19.73 ?  355  TRP E CD1 1 
ATOM   11526 C  CD2 . TRP E  1 331 ? 4.401   31.317  27.484  1.00 20.18 ?  355  TRP E CD2 1 
ATOM   11527 N  NE1 . TRP E  1 331 ? 4.727   29.434  26.317  1.00 20.19 ?  355  TRP E NE1 1 
ATOM   11528 C  CE2 . TRP E  1 331 ? 4.364   29.910  27.550  1.00 20.13 ?  355  TRP E CE2 1 
ATOM   11529 C  CE3 . TRP E  1 331 ? 4.075   32.057  28.628  1.00 20.24 ?  355  TRP E CE3 1 
ATOM   11530 C  CZ2 . TRP E  1 331 ? 4.009   29.221  28.713  1.00 20.05 ?  355  TRP E CZ2 1 
ATOM   11531 C  CZ3 . TRP E  1 331 ? 3.718   31.369  29.791  1.00 20.30 ?  355  TRP E CZ3 1 
ATOM   11532 C  CH2 . TRP E  1 331 ? 3.694   29.967  29.822  1.00 19.54 ?  355  TRP E CH2 1 
ATOM   11533 N  N   . ALA E  1 332 ? 4.229   35.919  24.338  1.00 21.26 ?  356  ALA E N   1 
ATOM   11534 C  CA  . ALA E  1 332 ? 4.518   37.356  24.277  1.00 21.57 ?  356  ALA E CA  1 
ATOM   11535 C  C   . ALA E  1 332 ? 5.578   37.812  25.286  1.00 21.76 ?  356  ALA E C   1 
ATOM   11536 O  O   . ALA E  1 332 ? 5.371   38.781  26.023  1.00 21.78 ?  356  ALA E O   1 
ATOM   11537 C  CB  . ALA E  1 332 ? 3.225   38.189  24.416  1.00 21.38 ?  356  ALA E CB  1 
ATOM   11538 N  N   . ASN E  1 333 ? 6.701   37.093  25.315  1.00 21.98 ?  357  ASN E N   1 
ATOM   11539 C  CA  . ASN E  1 333 ? 7.891   37.464  26.104  1.00 22.29 ?  357  ASN E CA  1 
ATOM   11540 C  C   . ASN E  1 333 ? 7.781   37.367  27.626  1.00 22.42 ?  357  ASN E C   1 
ATOM   11541 O  O   . ASN E  1 333 ? 8.629   36.742  28.258  1.00 22.35 ?  357  ASN E O   1 
ATOM   11542 C  CB  . ASN E  1 333 ? 8.386   38.866  25.736  1.00 21.99 ?  357  ASN E CB  1 
ATOM   11543 C  CG  . ASN E  1 333 ? 9.780   39.150  26.266  1.00 22.21 ?  357  ASN E CG  1 
ATOM   11544 O  OD1 . ASN E  1 333 ? 10.763  38.588  25.782  1.00 22.25 ?  357  ASN E OD1 1 
ATOM   11545 N  ND2 . ASN E  1 333 ? 9.874   40.029  27.255  1.00 20.81 ?  357  ASN E ND2 1 
ATOM   11546 N  N   . TYR E  1 334 ? 6.769   38.022  28.199  1.00 22.69 ?  358  TYR E N   1 
ATOM   11547 C  CA  . TYR E  1 334 ? 6.614   38.129  29.650  1.00 22.90 ?  358  TYR E CA  1 
ATOM   11548 C  C   . TYR E  1 334 ? 5.602   37.096  30.162  1.00 23.16 ?  358  TYR E C   1 
ATOM   11549 O  O   . TYR E  1 334 ? 4.393   37.303  30.046  1.00 23.23 ?  358  TYR E O   1 
ATOM   11550 C  CB  . TYR E  1 334 ? 6.179   39.549  30.049  1.00 22.87 ?  358  TYR E CB  1 
ATOM   11551 C  CG  . TYR E  1 334 ? 7.090   40.664  29.567  1.00 23.03 ?  358  TYR E CG  1 
ATOM   11552 C  CD1 . TYR E  1 334 ? 8.259   40.988  30.263  1.00 23.32 ?  358  TYR E CD1 1 
ATOM   11553 C  CD2 . TYR E  1 334 ? 6.776   41.407  28.423  1.00 22.35 ?  358  TYR E CD2 1 
ATOM   11554 C  CE1 . TYR E  1 334 ? 9.097   42.014  29.831  1.00 23.11 ?  358  TYR E CE1 1 
ATOM   11555 C  CE2 . TYR E  1 334 ? 7.604   42.440  27.984  1.00 22.64 ?  358  TYR E CE2 1 
ATOM   11556 C  CZ  . TYR E  1 334 ? 8.763   42.735  28.695  1.00 23.30 ?  358  TYR E CZ  1 
ATOM   11557 O  OH  . TYR E  1 334 ? 9.596   43.744  28.275  1.00 24.07 ?  358  TYR E OH  1 
ATOM   11558 N  N   . PRO E  1 335 ? 6.095   35.983  30.738  1.00 23.49 ?  359  PRO E N   1 
ATOM   11559 C  CA  . PRO E  1 335 ? 5.257   34.824  31.077  1.00 23.69 ?  359  PRO E CA  1 
ATOM   11560 C  C   . PRO E  1 335 ? 4.360   35.011  32.304  1.00 23.87 ?  359  PRO E C   1 
ATOM   11561 O  O   . PRO E  1 335 ? 3.472   34.191  32.542  1.00 23.89 ?  359  PRO E O   1 
ATOM   11562 C  CB  . PRO E  1 335 ? 6.285   33.713  31.351  1.00 23.60 ?  359  PRO E CB  1 
ATOM   11563 C  CG  . PRO E  1 335 ? 7.621   34.266  30.889  1.00 23.79 ?  359  PRO E CG  1 
ATOM   11564 C  CD  . PRO E  1 335 ? 7.505   35.737  31.083  1.00 23.43 ?  359  PRO E CD  1 
ATOM   11565 N  N   . PHE E  1 336 ? 4.594   36.080  33.059  1.00 24.18 ?  360  PHE E N   1 
ATOM   11566 C  CA  . PHE E  1 336 ? 3.881   36.352  34.310  1.00 24.52 ?  360  PHE E CA  1 
ATOM   11567 C  C   . PHE E  1 336 ? 2.641   37.231  34.120  1.00 24.48 ?  360  PHE E C   1 
ATOM   11568 O  O   . PHE E  1 336 ? 1.851   37.408  35.050  1.00 24.57 ?  360  PHE E O   1 
ATOM   11569 C  CB  . PHE E  1 336 ? 4.832   37.010  35.315  1.00 24.52 ?  360  PHE E CB  1 
ATOM   11570 C  CG  . PHE E  1 336 ? 5.462   38.273  34.803  1.00 25.34 ?  360  PHE E CG  1 
ATOM   11571 C  CD1 . PHE E  1 336 ? 4.826   39.502  34.970  1.00 25.92 ?  360  PHE E CD1 1 
ATOM   11572 C  CD2 . PHE E  1 336 ? 6.682   38.235  34.130  1.00 25.82 ?  360  PHE E CD2 1 
ATOM   11573 C  CE1 . PHE E  1 336 ? 5.398   40.668  34.484  1.00 26.07 ?  360  PHE E CE1 1 
ATOM   11574 C  CE2 . PHE E  1 336 ? 7.262   39.401  33.643  1.00 25.84 ?  360  PHE E CE2 1 
ATOM   11575 C  CZ  . PHE E  1 336 ? 6.619   40.616  33.819  1.00 26.12 ?  360  PHE E CZ  1 
ATOM   11576 N  N   . VAL E  1 337 ? 2.484   37.793  32.924  1.00 24.54 ?  361  VAL E N   1 
ATOM   11577 C  CA  . VAL E  1 337 ? 1.343   38.657  32.614  1.00 24.46 ?  361  VAL E CA  1 
ATOM   11578 C  C   . VAL E  1 337 ? 0.022   37.892  32.811  1.00 24.58 ?  361  VAL E C   1 
ATOM   11579 O  O   . VAL E  1 337 ? -0.138  36.798  32.268  1.00 24.46 ?  361  VAL E O   1 
ATOM   11580 C  CB  . VAL E  1 337 ? 1.472   39.256  31.189  1.00 24.44 ?  361  VAL E CB  1 
ATOM   11581 C  CG1 . VAL E  1 337 ? 0.130   39.798  30.673  1.00 24.18 ?  361  VAL E CG1 1 
ATOM   11582 C  CG2 . VAL E  1 337 ? 2.540   40.349  31.177  1.00 23.78 ?  361  VAL E CG2 1 
ATOM   11583 N  N   . PRO E  1 338 ? -0.913  38.459  33.607  1.00 24.68 ?  362  PRO E N   1 
ATOM   11584 C  CA  . PRO E  1 338 ? -2.141  37.740  33.978  1.00 24.63 ?  362  PRO E CA  1 
ATOM   11585 C  C   . PRO E  1 338 ? -2.905  37.201  32.767  1.00 24.62 ?  362  PRO E C   1 
ATOM   11586 O  O   . PRO E  1 338 ? -3.170  37.941  31.814  1.00 24.48 ?  362  PRO E O   1 
ATOM   11587 C  CB  . PRO E  1 338 ? -2.975  38.802  34.707  1.00 24.56 ?  362  PRO E CB  1 
ATOM   11588 C  CG  . PRO E  1 338 ? -1.984  39.802  35.198  1.00 24.92 ?  362  PRO E CG  1 
ATOM   11589 C  CD  . PRO E  1 338 ? -0.882  39.824  34.173  1.00 24.67 ?  362  PRO E CD  1 
ATOM   11590 N  N   . GLY E  1 339 ? -3.236  35.915  32.814  1.00 24.36 ?  363  GLY E N   1 
ATOM   11591 C  CA  . GLY E  1 339 ? -4.006  35.269  31.759  1.00 24.52 ?  363  GLY E CA  1 
ATOM   11592 C  C   . GLY E  1 339 ? -3.184  34.542  30.708  1.00 24.45 ?  363  GLY E C   1 
ATOM   11593 O  O   . GLY E  1 339 ? -3.717  33.717  29.973  1.00 24.29 ?  363  GLY E O   1 
ATOM   11594 N  N   . ILE E  1 340 ? -1.889  34.847  30.634  1.00 24.73 ?  364  ILE E N   1 
ATOM   11595 C  CA  . ILE E  1 340 ? -1.020  34.300  29.583  1.00 24.84 ?  364  ILE E CA  1 
ATOM   11596 C  C   . ILE E  1 340 ? -0.756  32.806  29.768  1.00 25.19 ?  364  ILE E C   1 
ATOM   11597 O  O   . ILE E  1 340 ? -1.013  32.013  28.858  1.00 25.13 ?  364  ILE E O   1 
ATOM   11598 C  CB  . ILE E  1 340 ? 0.305   35.108  29.443  1.00 24.80 ?  364  ILE E CB  1 
ATOM   11599 C  CG1 . ILE E  1 340 ? 0.023   36.515  28.888  1.00 24.47 ?  364  ILE E CG1 1 
ATOM   11600 C  CG2 . ILE E  1 340 ? 1.329   34.366  28.564  1.00 24.30 ?  364  ILE E CG2 1 
ATOM   11601 C  CD1 . ILE E  1 340 ? -0.225  36.577  27.381  1.00 23.91 ?  364  ILE E CD1 1 
ATOM   11602 N  N   . ALA E  1 341 ? -0.261  32.426  30.946  1.00 25.68 ?  365  ALA E N   1 
ATOM   11603 C  CA  . ALA E  1 341 ? -0.025  31.019  31.266  1.00 26.28 ?  365  ALA E CA  1 
ATOM   11604 C  C   . ALA E  1 341 ? -1.321  30.207  31.193  1.00 26.78 ?  365  ALA E C   1 
ATOM   11605 O  O   . ALA E  1 341 ? -1.348  29.115  30.612  1.00 26.74 ?  365  ALA E O   1 
ATOM   11606 C  CB  . ALA E  1 341 ? 0.611   30.884  32.638  1.00 26.25 ?  365  ALA E CB  1 
ATOM   11607 N  N   . GLU E  1 342 ? -2.390  30.761  31.764  1.00 27.01 ?  366  GLU E N   1 
ATOM   11608 C  CA  . GLU E  1 342 ? -3.707  30.116  31.776  1.00 27.58 ?  366  GLU E CA  1 
ATOM   11609 C  C   . GLU E  1 342 ? -4.276  29.888  30.369  1.00 27.86 ?  366  GLU E C   1 
ATOM   11610 O  O   . GLU E  1 342 ? -5.044  28.951  30.155  1.00 28.13 ?  366  GLU E O   1 
ATOM   11611 C  CB  . GLU E  1 342 ? -4.701  30.935  32.615  1.00 27.50 ?  366  GLU E CB  1 
ATOM   11612 C  CG  . GLU E  1 342 ? -4.384  30.995  34.114  1.00 27.78 ?  366  GLU E CG  1 
ATOM   11613 C  CD  . GLU E  1 342 ? -3.511  32.184  34.515  1.00 28.17 ?  366  GLU E CD  1 
ATOM   11614 O  OE1 . GLU E  1 342 ? -2.973  32.879  33.629  1.00 27.14 ?  366  GLU E OE1 1 
ATOM   11615 O  OE2 . GLU E  1 342 ? -3.365  32.427  35.734  1.00 28.88 -1 366  GLU E OE2 1 
ATOM   11616 N  N   . ASN E  1 343 ? -3.897  30.753  29.428  1.00 28.20 ?  367  ASN E N   1 
ATOM   11617 C  CA  . ASN E  1 343 ? -4.341  30.670  28.033  1.00 28.50 ?  367  ASN E CA  1 
ATOM   11618 C  C   . ASN E  1 343 ? -3.507  29.722  27.164  1.00 28.63 ?  367  ASN E C   1 
ATOM   11619 O  O   . ASN E  1 343 ? -3.874  29.455  26.017  1.00 28.77 ?  367  ASN E O   1 
ATOM   11620 C  CB  . ASN E  1 343 ? -4.359  32.075  27.403  1.00 28.49 ?  367  ASN E CB  1 
ATOM   11621 C  CG  . ASN E  1 343 ? -4.797  32.071  25.937  1.00 28.89 ?  367  ASN E CG  1 
ATOM   11622 O  OD1 . ASN E  1 343 ? -5.904  31.648  25.603  1.00 28.98 ?  367  ASN E OD1 1 
ATOM   11623 N  ND2 . ASN E  1 343 ? -3.925  32.558  25.061  1.00 29.36 ?  367  ASN E ND2 1 
ATOM   11624 N  N   . ILE E  1 344 ? -2.399  29.208  27.699  1.00 28.83 ?  368  ILE E N   1 
ATOM   11625 C  CA  . ILE E  1 344 ? -1.455  28.433  26.881  1.00 29.18 ?  368  ILE E CA  1 
ATOM   11626 C  C   . ILE E  1 344 ? -2.036  27.120  26.333  1.00 29.48 ?  368  ILE E C   1 
ATOM   11627 O  O   . ILE E  1 344 ? -1.539  26.591  25.340  1.00 29.79 ?  368  ILE E O   1 
ATOM   11628 C  CB  . ILE E  1 344 ? -0.071  28.215  27.591  1.00 29.10 ?  368  ILE E CB  1 
ATOM   11629 C  CG1 . ILE E  1 344 ? 1.060   28.054  26.562  1.00 29.03 ?  368  ILE E CG1 1 
ATOM   11630 C  CG2 . ILE E  1 344 ? -0.108  27.026  28.555  1.00 28.82 ?  368  ILE E CG2 1 
ATOM   11631 C  CD1 . ILE E  1 344 ? 1.365   29.308  25.748  1.00 28.06 ?  368  ILE E CD1 1 
ATOM   11632 N  N   . THR E  1 345 ? -3.100  26.623  26.964  1.00 29.80 ?  369  THR E N   1 
ATOM   11633 C  CA  . THR E  1 345 ? -3.725  25.356  26.568  1.00 30.11 ?  369  THR E CA  1 
ATOM   11634 C  C   . THR E  1 345 ? -5.055  25.522  25.828  1.00 30.07 ?  369  THR E C   1 
ATOM   11635 O  O   . THR E  1 345 ? -5.769  24.541  25.599  1.00 30.21 ?  369  THR E O   1 
ATOM   11636 C  CB  . THR E  1 345 ? -3.960  24.437  27.785  1.00 30.20 ?  369  THR E CB  1 
ATOM   11637 O  OG1 . THR E  1 345 ? -4.841  25.086  28.710  1.00 30.95 ?  369  THR E OG1 1 
ATOM   11638 C  CG2 . THR E  1 345 ? -2.652  24.123  28.477  1.00 30.58 ?  369  THR E CG2 1 
ATOM   11639 N  N   . SER E  1 346 ? -5.385  26.757  25.457  1.00 29.97 ?  370  SER E N   1 
ATOM   11640 C  CA  . SER E  1 346 ? -6.629  27.040  24.744  1.00 29.82 ?  370  SER E CA  1 
ATOM   11641 C  C   . SER E  1 346 ? -6.520  26.665  23.261  1.00 29.85 ?  370  SER E C   1 
ATOM   11642 O  O   . SER E  1 346 ? -5.414  26.500  22.735  1.00 29.77 ?  370  SER E O   1 
ATOM   11643 C  CB  . SER E  1 346 ? -6.999  28.518  24.896  1.00 29.91 ?  370  SER E CB  1 
ATOM   11644 O  OG  . SER E  1 346 ? -6.130  29.351  24.140  1.00 29.73 ?  370  SER E OG  1 
ATOM   11645 N  N   . ASP E  1 347 ? -7.672  26.531  22.600  1.00 29.62 ?  371  ASP E N   1 
ATOM   11646 C  CA  . ASP E  1 347 ? -7.741  26.268  21.156  1.00 29.54 ?  371  ASP E CA  1 
ATOM   11647 C  C   . ASP E  1 347 ? -7.028  27.355  20.339  1.00 29.10 ?  371  ASP E C   1 
ATOM   11648 O  O   . ASP E  1 347 ? -6.431  27.076  19.298  1.00 28.92 ?  371  ASP E O   1 
ATOM   11649 C  CB  . ASP E  1 347 ? -9.207  26.165  20.703  1.00 29.70 ?  371  ASP E CB  1 
ATOM   11650 C  CG  . ASP E  1 347 ? -9.898  24.892  21.189  1.00 30.37 ?  371  ASP E CG  1 
ATOM   11651 O  OD1 . ASP E  1 347 ? -9.236  23.999  21.756  1.00 31.26 ?  371  ASP E OD1 1 
ATOM   11652 O  OD2 . ASP E  1 347 ? -11.124 24.781  20.990  1.00 32.21 -1 371  ASP E OD2 1 
ATOM   11653 N  N   . TRP E  1 348 ? -7.119  28.591  20.828  1.00 28.72 ?  372  TRP E N   1 
ATOM   11654 C  CA  . TRP E  1 348 ? -6.480  29.766  20.234  1.00 28.29 ?  372  TRP E CA  1 
ATOM   11655 C  C   . TRP E  1 348 ? -4.954  29.643  20.234  1.00 28.08 ?  372  TRP E C   1 
ATOM   11656 O  O   . TRP E  1 348 ? -4.302  29.917  19.223  1.00 27.94 ?  372  TRP E O   1 
ATOM   11657 C  CB  . TRP E  1 348 ? -6.918  31.008  21.018  1.00 28.13 ?  372  TRP E CB  1 
ATOM   11658 C  CG  . TRP E  1 348 ? -6.434  32.342  20.504  1.00 27.93 ?  372  TRP E CG  1 
ATOM   11659 C  CD1 . TRP E  1 348 ? -7.104  33.189  19.664  1.00 27.45 ?  372  TRP E CD1 1 
ATOM   11660 C  CD2 . TRP E  1 348 ? -5.204  33.006  20.845  1.00 27.08 ?  372  TRP E CD2 1 
ATOM   11661 N  NE1 . TRP E  1 348 ? -6.363  34.326  19.447  1.00 27.15 ?  372  TRP E NE1 1 
ATOM   11662 C  CE2 . TRP E  1 348 ? -5.195  34.242  20.161  1.00 26.98 ?  372  TRP E CE2 1 
ATOM   11663 C  CE3 . TRP E  1 348 ? -4.110  32.673  21.660  1.00 26.93 ?  372  TRP E CE3 1 
ATOM   11664 C  CZ2 . TRP E  1 348 ? -4.131  35.149  20.260  1.00 26.77 ?  372  TRP E CZ2 1 
ATOM   11665 C  CZ3 . TRP E  1 348 ? -3.049  33.576  21.758  1.00 26.89 ?  372  TRP E CZ3 1 
ATOM   11666 C  CH2 . TRP E  1 348 ? -3.069  34.798  21.058  1.00 26.89 ?  372  TRP E CH2 1 
ATOM   11667 N  N   . SER E  1 349 ? -4.388  29.237  21.367  1.00 27.90 ?  373  SER E N   1 
ATOM   11668 C  CA  . SER E  1 349 ? -2.938  29.068  21.473  1.00 27.91 ?  373  SER E CA  1 
ATOM   11669 C  C   . SER E  1 349 ? -2.489  27.830  20.708  1.00 27.81 ?  373  SER E C   1 
ATOM   11670 O  O   . SER E  1 349 ? -1.427  27.830  20.086  1.00 27.87 ?  373  SER E O   1 
ATOM   11671 C  CB  . SER E  1 349 ? -2.496  28.994  22.934  1.00 27.77 ?  373  SER E CB  1 
ATOM   11672 O  OG  . SER E  1 349 ? -2.806  30.196  23.620  1.00 28.07 ?  373  SER E OG  1 
ATOM   11673 N  N   . GLU E  1 350 ? -3.319  26.790  20.741  1.00 27.71 ?  374  GLU E N   1 
ATOM   11674 C  CA  . GLU E  1 350 ? -3.035  25.534  20.050  1.00 27.78 ?  374  GLU E CA  1 
ATOM   11675 C  C   . GLU E  1 350 ? -2.956  25.715  18.529  1.00 27.30 ?  374  GLU E C   1 
ATOM   11676 O  O   . GLU E  1 350 ? -2.087  25.128  17.879  1.00 27.26 ?  374  GLU E O   1 
ATOM   11677 C  CB  . GLU E  1 350 ? -4.077  24.475  20.425  1.00 27.97 ?  374  GLU E CB  1 
ATOM   11678 C  CG  . GLU E  1 350 ? -3.631  23.032  20.201  1.00 29.82 ?  374  GLU E CG  1 
ATOM   11679 C  CD  . GLU E  1 350 ? -2.502  22.577  21.129  1.00 31.08 ?  374  GLU E CD  1 
ATOM   11680 O  OE1 . GLU E  1 350 ? -2.246  23.221  22.167  1.00 32.06 ?  374  GLU E OE1 1 
ATOM   11681 O  OE2 . GLU E  1 350 ? -1.867  21.553  20.814  1.00 32.62 -1 374  GLU E OE2 1 
ATOM   11682 N  N   . ALA E  1 351 ? -3.853  26.533  17.977  1.00 26.63 ?  375  ALA E N   1 
ATOM   11683 C  CA  . ALA E  1 351 ? -3.838  26.860  16.548  1.00 26.24 ?  375  ALA E CA  1 
ATOM   11684 C  C   . ALA E  1 351 ? -2.572  27.633  16.177  1.00 25.84 ?  375  ALA E C   1 
ATOM   11685 O  O   . ALA E  1 351 ? -1.999  27.428  15.101  1.00 25.55 ?  375  ALA E O   1 
ATOM   11686 C  CB  . ALA E  1 351 ? -5.085  27.658  16.163  1.00 26.15 ?  375  ALA E CB  1 
ATOM   11687 N  N   . ARG E  1 352 ? -2.142  28.516  17.078  1.00 25.32 ?  376  ARG E N   1 
ATOM   11688 C  CA  . ARG E  1 352 ? -0.895  29.255  16.897  1.00 25.01 ?  376  ARG E CA  1 
ATOM   11689 C  C   . ARG E  1 352 ? 0.325   28.344  17.060  1.00 24.63 ?  376  ARG E C   1 
ATOM   11690 O  O   . ARG E  1 352 ? 1.336   28.530  16.382  1.00 24.64 ?  376  ARG E O   1 
ATOM   11691 C  CB  . ARG E  1 352 ? -0.836  30.473  17.823  1.00 24.95 ?  376  ARG E CB  1 
ATOM   11692 C  CG  . ARG E  1 352 ? -1.686  31.633  17.313  1.00 24.96 ?  376  ARG E CG  1 
ATOM   11693 C  CD  . ARG E  1 352 ? -1.844  32.764  18.326  1.00 24.69 ?  376  ARG E CD  1 
ATOM   11694 N  NE  . ARG E  1 352 ? -2.622  33.865  17.753  1.00 24.92 ?  376  ARG E NE  1 
ATOM   11695 C  CZ  . ARG E  1 352 ? -2.224  35.135  17.684  1.00 25.52 ?  376  ARG E CZ  1 
ATOM   11696 N  NH1 . ARG E  1 352 ? -1.054  35.508  18.190  1.00 24.77 ?  376  ARG E NH1 1 
ATOM   11697 N  NH2 . ARG E  1 352 ? -3.021  36.047  17.133  1.00 25.06 ?  376  ARG E NH2 1 
ATOM   11698 N  N   . LEU E  1 353 ? 0.215   27.348  17.937  1.00 24.33 ?  377  LEU E N   1 
ATOM   11699 C  CA  . LEU E  1 353 ? 1.250   26.321  18.054  1.00 24.15 ?  377  LEU E CA  1 
ATOM   11700 C  C   . LEU E  1 353 ? 1.361   25.514  16.749  1.00 24.04 ?  377  LEU E C   1 
ATOM   11701 O  O   . LEU E  1 353 ? 2.466   25.243  16.280  1.00 23.73 ?  377  LEU E O   1 
ATOM   11702 C  CB  . LEU E  1 353 ? 1.003   25.406  19.262  1.00 23.95 ?  377  LEU E CB  1 
ATOM   11703 C  CG  . LEU E  1 353 ? 2.103   24.387  19.607  1.00 24.28 ?  377  LEU E CG  1 
ATOM   11704 C  CD1 . LEU E  1 353 ? 3.357   25.072  20.139  1.00 24.36 ?  377  LEU E CD1 1 
ATOM   11705 C  CD2 . LEU E  1 353 ? 1.613   23.345  20.601  1.00 23.78 ?  377  LEU E CD2 1 
ATOM   11706 N  N   . ASP E  1 354 ? 0.215   25.156  16.164  1.00 24.03 ?  378  ASP E N   1 
ATOM   11707 C  CA  . ASP E  1 354 ? 0.171   24.470  14.868  1.00 24.36 ?  378  ASP E CA  1 
ATOM   11708 C  C   . ASP E  1 354 ? 0.909   25.254  13.784  1.00 24.25 ?  378  ASP E C   1 
ATOM   11709 O  O   . ASP E  1 354 ? 1.627   24.665  12.973  1.00 24.19 ?  378  ASP E O   1 
ATOM   11710 C  CB  . ASP E  1 354 ? -1.276  24.231  14.414  1.00 24.53 ?  378  ASP E CB  1 
ATOM   11711 C  CG  . ASP E  1 354 ? -1.932  23.047  15.107  1.00 25.68 ?  378  ASP E CG  1 
ATOM   11712 O  OD1 . ASP E  1 354 ? -1.244  22.279  15.819  1.00 26.93 ?  378  ASP E OD1 1 
ATOM   11713 O  OD2 . ASP E  1 354 ? -3.156  22.883  14.929  1.00 27.60 -1 378  ASP E OD2 1 
ATOM   11714 N  N   . SER E  1 355 ? 0.712   26.574  13.778  1.00 24.16 ?  379  SER E N   1 
ATOM   11715 C  CA  . SER E  1 355 ? 1.348   27.466  12.812  1.00 24.35 ?  379  SER E CA  1 
ATOM   11716 C  C   . SER E  1 355 ? 2.865   27.511  12.995  1.00 24.18 ?  379  SER E C   1 
ATOM   11717 O  O   . SER E  1 355 ? 3.605   27.559  12.009  1.00 24.34 ?  379  SER E O   1 
ATOM   11718 C  CB  . SER E  1 355 ? 0.757   28.875  12.901  1.00 24.51 ?  379  SER E CB  1 
ATOM   11719 O  OG  . SER E  1 355 ? -0.598  28.891  12.478  1.00 25.34 ?  379  SER E OG  1 
ATOM   11720 N  N   . TRP E  1 356 ? 3.314   27.495  14.252  1.00 23.78 ?  380  TRP E N   1 
ATOM   11721 C  CA  . TRP E  1 356 ? 4.737   27.385  14.578  1.00 23.55 ?  380  TRP E CA  1 
ATOM   11722 C  C   . TRP E  1 356 ? 5.324   26.068  14.100  1.00 23.84 ?  380  TRP E C   1 
ATOM   11723 O  O   . TRP E  1 356 ? 6.404   26.040  13.502  1.00 23.66 ?  380  TRP E O   1 
ATOM   11724 C  CB  . TRP E  1 356 ? 4.980   27.538  16.085  1.00 23.38 ?  380  TRP E CB  1 
ATOM   11725 C  CG  . TRP E  1 356 ? 5.161   28.960  16.517  1.00 22.26 ?  380  TRP E CG  1 
ATOM   11726 C  CD1 . TRP E  1 356 ? 4.391   29.651  17.409  1.00 21.37 ?  380  TRP E CD1 1 
ATOM   11727 C  CD2 . TRP E  1 356 ? 6.170   29.869  16.067  1.00 20.99 ?  380  TRP E CD2 1 
ATOM   11728 N  NE1 . TRP E  1 356 ? 4.865   30.932  17.551  1.00 20.82 ?  380  TRP E NE1 1 
ATOM   11729 C  CE2 . TRP E  1 356 ? 5.954   31.096  16.736  1.00 20.93 ?  380  TRP E CE2 1 
ATOM   11730 C  CE3 . TRP E  1 356 ? 7.240   29.766  15.165  1.00 20.59 ?  380  TRP E CE3 1 
ATOM   11731 C  CZ2 . TRP E  1 356 ? 6.765   32.214  16.529  1.00 19.92 ?  380  TRP E CZ2 1 
ATOM   11732 C  CZ3 . TRP E  1 356 ? 8.046   30.878  14.958  1.00 20.12 ?  380  TRP E CZ3 1 
ATOM   11733 C  CH2 . TRP E  1 356 ? 7.804   32.086  15.640  1.00 20.67 ?  380  TRP E CH2 1 
ATOM   11734 N  N   . VAL E  1 357 ? 4.602   24.981  14.366  1.00 24.12 ?  381  VAL E N   1 
ATOM   11735 C  CA  . VAL E  1 357 ? 5.021   23.647  13.939  1.00 24.28 ?  381  VAL E CA  1 
ATOM   11736 C  C   . VAL E  1 357 ? 5.280   23.630  12.436  1.00 24.41 ?  381  VAL E C   1 
ATOM   11737 O  O   . VAL E  1 357 ? 6.282   23.069  11.990  1.00 24.48 ?  381  VAL E O   1 
ATOM   11738 C  CB  . VAL E  1 357 ? 3.994   22.564  14.360  1.00 24.41 ?  381  VAL E CB  1 
ATOM   11739 C  CG1 . VAL E  1 357 ? 4.287   21.226  13.685  1.00 24.00 ?  381  VAL E CG1 1 
ATOM   11740 C  CG2 . VAL E  1 357 ? 3.986   22.414  15.879  1.00 24.06 ?  381  VAL E CG2 1 
ATOM   11741 N  N   . LEU E  1 358 ? 4.396   24.274  11.672  1.00 24.56 ?  382  LEU E N   1 
ATOM   11742 C  CA  . LEU E  1 358 ? 4.559   24.409  10.220  1.00 24.69 ?  382  LEU E CA  1 
ATOM   11743 C  C   . LEU E  1 358 ? 5.855   25.132  9.845   1.00 24.46 ?  382  LEU E C   1 
ATOM   11744 O  O   . LEU E  1 358 ? 6.539   24.732  8.903   1.00 24.66 ?  382  LEU E O   1 
ATOM   11745 C  CB  . LEU E  1 358 ? 3.357   25.129  9.596   1.00 24.92 ?  382  LEU E CB  1 
ATOM   11746 C  CG  . LEU E  1 358 ? 3.299   25.174  8.064   1.00 25.95 ?  382  LEU E CG  1 
ATOM   11747 C  CD1 . LEU E  1 358 ? 2.754   23.857  7.479   1.00 26.67 ?  382  LEU E CD1 1 
ATOM   11748 C  CD2 . LEU E  1 358 ? 2.464   26.349  7.590   1.00 26.29 ?  382  LEU E CD2 1 
ATOM   11749 N  N   . THR E  1 359 ? 6.176   26.197  10.577  1.00 24.23 ?  383  THR E N   1 
ATOM   11750 C  CA  . THR E  1 359 ? 7.433   26.930  10.399  1.00 23.95 ?  383  THR E CA  1 
ATOM   11751 C  C   . THR E  1 359 ? 8.641   26.014  10.617  1.00 23.80 ?  383  THR E C   1 
ATOM   11752 O  O   . THR E  1 359 ? 9.546   25.972  9.782   1.00 23.73 ?  383  THR E O   1 
ATOM   11753 C  CB  . THR E  1 359 ? 7.533   28.137  11.374  1.00 23.91 ?  383  THR E CB  1 
ATOM   11754 O  OG1 . THR E  1 359 ? 6.351   28.944  11.276  1.00 23.79 ?  383  THR E OG1 1 
ATOM   11755 C  CG2 . THR E  1 359 ? 8.767   28.987  11.078  1.00 23.88 ?  383  THR E CG2 1 
ATOM   11756 N  N   . CYS E  1 360 ? 8.640   25.287  11.735  1.00 23.75 ?  384  CYS E N   1 
ATOM   11757 C  CA  . CYS E  1 360 ? 9.758   24.415  12.112  1.00 24.03 ?  384  CYS E CA  1 
ATOM   11758 C  C   . CYS E  1 360 ? 9.926   23.244  11.149  1.00 24.20 ?  384  CYS E C   1 
ATOM   11759 O  O   . CYS E  1 360 ? 11.050  22.861  10.830  1.00 24.27 ?  384  CYS E O   1 
ATOM   11760 C  CB  . CYS E  1 360 ? 9.581   23.862  13.529  1.00 23.68 ?  384  CYS E CB  1 
ATOM   11761 S  SG  . CYS E  1 360 ? 9.312   25.079  14.819  1.00 23.92 ?  384  CYS E SG  1 
ATOM   11762 N  N   . THR E  1 361 ? 8.804   22.695  10.685  1.00 24.54 ?  385  THR E N   1 
ATOM   11763 C  CA  . THR E  1 361 ? 8.801   21.487  9.850   1.00 24.78 ?  385  THR E CA  1 
ATOM   11764 C  C   . THR E  1 361 ? 9.226   21.721  8.403   1.00 24.86 ?  385  THR E C   1 
ATOM   11765 O  O   . THR E  1 361 ? 9.200   20.798  7.590   1.00 24.94 ?  385  THR E O   1 
ATOM   11766 C  CB  . THR E  1 361 ? 7.432   20.763  9.871   1.00 24.92 ?  385  THR E CB  1 
ATOM   11767 O  OG1 . THR E  1 361 ? 6.398   21.681  9.501   1.00 25.52 ?  385  THR E OG1 1 
ATOM   11768 C  CG2 . THR E  1 361 ? 7.142   20.193  11.256  1.00 24.48 ?  385  THR E CG2 1 
ATOM   11769 N  N   . GLN E  1 362 ? 9.610   22.953  8.076   1.00 24.95 ?  386  GLN E N   1 
ATOM   11770 C  CA  . GLN E  1 362 ? 10.309  23.207  6.821   1.00 25.07 ?  386  GLN E CA  1 
ATOM   11771 C  C   . GLN E  1 362 ? 11.670  22.513  6.879   1.00 24.79 ?  386  GLN E C   1 
ATOM   11772 O  O   . GLN E  1 362 ? 12.267  22.206  5.845   1.00 24.51 ?  386  GLN E O   1 
ATOM   11773 C  CB  . GLN E  1 362 ? 10.492  24.707  6.582   1.00 25.23 ?  386  GLN E CB  1 
ATOM   11774 C  CG  . GLN E  1 362 ? 9.192   25.477  6.369   1.00 26.43 ?  386  GLN E CG  1 
ATOM   11775 C  CD  . GLN E  1 362 ? 9.401   26.982  6.351   1.00 27.64 ?  386  GLN E CD  1 
ATOM   11776 O  OE1 . GLN E  1 362 ? 9.326   27.614  5.298   1.00 28.60 ?  386  GLN E OE1 1 
ATOM   11777 N  NE2 . GLN E  1 362 ? 9.680   27.561  7.518   1.00 26.78 ?  386  GLN E NE2 1 
ATOM   11778 N  N   . CYS E  1 363 ? 12.141  22.261  8.103   1.00 24.52 ?  387  CYS E N   1 
ATOM   11779 C  CA  . CYS E  1 363 ? 13.426  21.607  8.327   1.00 24.20 ?  387  CYS E CA  1 
ATOM   11780 C  C   . CYS E  1 363 ? 13.291  20.348  9.176   1.00 24.27 ?  387  CYS E C   1 
ATOM   11781 O  O   . CYS E  1 363 ? 13.551  19.244  8.697   1.00 24.24 ?  387  CYS E O   1 
ATOM   11782 C  CB  . CYS E  1 363 ? 14.410  22.588  8.967   1.00 24.39 ?  387  CYS E CB  1 
ATOM   11783 S  SG  . CYS E  1 363 ? 14.577  24.151  8.063   1.00 23.56 ?  387  CYS E SG  1 
ATOM   11784 N  N   . HIS E  1 364 ? 12.880  20.515  10.433  1.00 24.24 ?  388  HIS E N   1 
ATOM   11785 C  CA  . HIS E  1 364 ? 12.769  19.400  11.370  1.00 24.18 ?  388  HIS E CA  1 
ATOM   11786 C  C   . HIS E  1 364 ? 11.533  18.530  11.089  1.00 24.29 ?  388  HIS E C   1 
ATOM   11787 O  O   . HIS E  1 364 ? 10.631  18.940  10.357  1.00 24.22 ?  388  HIS E O   1 
ATOM   11788 C  CB  . HIS E  1 364 ? 12.742  19.913  12.817  1.00 24.29 ?  388  HIS E CB  1 
ATOM   11789 C  CG  . HIS E  1 364 ? 13.919  20.771  13.188  1.00 24.24 ?  388  HIS E CG  1 
ATOM   11790 N  ND1 . HIS E  1 364 ? 15.173  20.254  13.431  1.00 23.96 ?  388  HIS E ND1 1 
ATOM   11791 C  CD2 . HIS E  1 364 ? 14.023  22.108  13.379  1.00 23.63 ?  388  HIS E CD2 1 
ATOM   11792 C  CE1 . HIS E  1 364 ? 16.001  21.236  13.746  1.00 24.08 ?  388  HIS E CE1 1 
ATOM   11793 N  NE2 . HIS E  1 364 ? 15.329  22.374  13.723  1.00 23.51 ?  388  HIS E NE2 1 
ATOM   11794 N  N   . SER E  1 365 ? 11.501  17.325  11.656  1.00 24.15 ?  389  SER E N   1 
ATOM   11795 C  CA  . SER E  1 365 ? 10.275  16.523  11.646  1.00 24.22 ?  389  SER E CA  1 
ATOM   11796 C  C   . SER E  1 365 ? 9.266   17.125  12.625  1.00 24.21 ?  389  SER E C   1 
ATOM   11797 O  O   . SER E  1 365 ? 9.648   17.835  13.558  1.00 23.84 ?  389  SER E O   1 
ATOM   11798 C  CB  . SER E  1 365 ? 10.565  15.062  12.002  1.00 24.07 ?  389  SER E CB  1 
ATOM   11799 O  OG  . SER E  1 365 ? 10.961  14.925  13.358  1.00 24.48 ?  389  SER E OG  1 
ATOM   11800 N  N   . GLU E  1 366 ? 7.983   16.846  12.404  1.00 24.66 ?  390  GLU E N   1 
ATOM   11801 C  CA  . GLU E  1 366 ? 6.921   17.326  13.289  1.00 24.90 ?  390  GLU E CA  1 
ATOM   11802 C  C   . GLU E  1 366 ? 7.108   16.788  14.700  1.00 24.98 ?  390  GLU E C   1 
ATOM   11803 O  O   . GLU E  1 366 ? 6.935   17.518  15.680  1.00 25.36 ?  390  GLU E O   1 
ATOM   11804 C  CB  . GLU E  1 366 ? 5.529   16.969  12.738  1.00 25.01 ?  390  GLU E CB  1 
ATOM   11805 C  CG  . GLU E  1 366 ? 4.374   17.442  13.632  1.00 25.97 ?  390  GLU E CG  1 
ATOM   11806 C  CD  . GLU E  1 366 ? 3.004   17.361  12.977  1.00 27.29 ?  390  GLU E CD  1 
ATOM   11807 O  OE1 . GLU E  1 366 ? 2.905   17.029  11.776  1.00 28.19 ?  390  GLU E OE1 1 
ATOM   11808 O  OE2 . GLU E  1 366 ? 2.013   17.642  13.678  1.00 29.07 -1 390  GLU E OE2 1 
ATOM   11809 N  N   . ARG E  1 367 ? 7.484   15.516  14.793  1.00 24.96 ?  391  ARG E N   1 
ATOM   11810 C  CA  . ARG E  1 367 ? 7.746   14.871  16.074  1.00 24.82 ?  391  ARG E CA  1 
ATOM   11811 C  C   . ARG E  1 367 ? 8.848   15.602  16.844  1.00 24.70 ?  391  ARG E C   1 
ATOM   11812 O  O   . ARG E  1 367 ? 8.726   15.818  18.051  1.00 24.64 ?  391  ARG E O   1 
ATOM   11813 C  CB  . ARG E  1 367 ? 8.122   13.407  15.857  1.00 24.58 ?  391  ARG E CB  1 
ATOM   11814 C  CG  . ARG E  1 367 ? 8.078   12.541  17.104  1.00 24.86 ?  391  ARG E CG  1 
ATOM   11815 C  CD  . ARG E  1 367 ? 8.709   11.192  16.804  1.00 25.39 ?  391  ARG E CD  1 
ATOM   11816 N  NE  . ARG E  1 367 ? 8.457   10.201  17.842  1.00 26.02 ?  391  ARG E NE  1 
ATOM   11817 C  CZ  . ARG E  1 367 ? 9.051   9.012   17.907  1.00 26.20 ?  391  ARG E CZ  1 
ATOM   11818 N  NH1 . ARG E  1 367 ? 9.960   8.668   17.005  1.00 26.06 ?  391  ARG E NH1 1 
ATOM   11819 N  NH2 . ARG E  1 367 ? 8.751   8.171   18.890  1.00 26.49 ?  391  ARG E NH2 1 
ATOM   11820 N  N   . PHE E  1 368 ? 9.914   15.983  16.140  1.00 24.64 ?  392  PHE E N   1 
ATOM   11821 C  CA  . PHE E  1 368 ? 11.011  16.740  16.746  1.00 24.46 ?  392  PHE E CA  1 
ATOM   11822 C  C   . PHE E  1 368 ? 10.526  18.112  17.218  1.00 24.53 ?  392  PHE E C   1 
ATOM   11823 O  O   . PHE E  1 368 ? 10.696  18.468  18.383  1.00 24.18 ?  392  PHE E O   1 
ATOM   11824 C  CB  . PHE E  1 368 ? 12.180  16.898  15.761  1.00 24.36 ?  392  PHE E CB  1 
ATOM   11825 C  CG  . PHE E  1 368 ? 13.376  17.604  16.346  1.00 24.09 ?  392  PHE E CG  1 
ATOM   11826 C  CD1 . PHE E  1 368 ? 13.536  18.979  16.189  1.00 24.21 ?  392  PHE E CD1 1 
ATOM   11827 C  CD2 . PHE E  1 368 ? 14.334  16.896  17.064  1.00 24.20 ?  392  PHE E CD2 1 
ATOM   11828 C  CE1 . PHE E  1 368 ? 14.632  19.639  16.738  1.00 24.12 ?  392  PHE E CE1 1 
ATOM   11829 C  CE2 . PHE E  1 368 ? 15.438  17.546  17.617  1.00 23.89 ?  392  PHE E CE2 1 
ATOM   11830 C  CZ  . PHE E  1 368 ? 15.585  18.920  17.453  1.00 24.12 ?  392  PHE E CZ  1 
ATOM   11831 N  N   . ALA E  1 369 ? 9.910   18.861  16.300  1.00 24.50 ?  393  ALA E N   1 
ATOM   11832 C  CA  . ALA E  1 369 ? 9.445   20.221  16.563  1.00 24.45 ?  393  ALA E CA  1 
ATOM   11833 C  C   . ALA E  1 369 ? 8.469   20.293  17.734  1.00 24.40 ?  393  ALA E C   1 
ATOM   11834 O  O   . ALA E  1 369 ? 8.589   21.169  18.591  1.00 24.42 ?  393  ALA E O   1 
ATOM   11835 C  CB  . ALA E  1 369 ? 8.824   20.819  15.305  1.00 24.47 ?  393  ALA E CB  1 
ATOM   11836 N  N   . ARG E  1 370 ? 7.517   19.364  17.774  1.00 24.31 ?  394  ARG E N   1 
ATOM   11837 C  CA  . ARG E  1 370 ? 6.534   19.311  18.861  1.00 24.25 ?  394  ARG E CA  1 
ATOM   11838 C  C   . ARG E  1 370 ? 7.169   18.930  20.198  1.00 24.20 ?  394  ARG E C   1 
ATOM   11839 O  O   . ARG E  1 370 ? 6.748   19.419  21.248  1.00 24.31 ?  394  ARG E O   1 
ATOM   11840 C  CB  . ARG E  1 370 ? 5.379   18.362  18.522  1.00 24.11 ?  394  ARG E CB  1 
ATOM   11841 C  CG  . ARG E  1 370 ? 4.455   18.898  17.433  1.00 24.21 ?  394  ARG E CG  1 
ATOM   11842 C  CD  . ARG E  1 370 ? 3.179   18.081  17.297  1.00 23.34 ?  394  ARG E CD  1 
ATOM   11843 N  NE  . ARG E  1 370 ? 2.293   18.645  16.278  1.00 23.97 ?  394  ARG E NE  1 
ATOM   11844 C  CZ  . ARG E  1 370 ? 1.404   19.611  16.499  1.00 24.05 ?  394  ARG E CZ  1 
ATOM   11845 N  NH1 . ARG E  1 370 ? 1.264   20.139  17.709  1.00 23.42 ?  394  ARG E NH1 1 
ATOM   11846 N  NH2 . ARG E  1 370 ? 0.647   20.053  15.506  1.00 25.00 ?  394  ARG E NH2 1 
ATOM   11847 N  N   . SER E  1 371 ? 8.180   18.065  20.148  1.00 23.98 ?  395  SER E N   1 
ATOM   11848 C  CA  . SER E  1 371 ? 8.914   17.654  21.340  1.00 23.94 ?  395  SER E CA  1 
ATOM   11849 C  C   . SER E  1 371 ? 9.603   18.841  22.012  1.00 23.96 ?  395  SER E C   1 
ATOM   11850 O  O   . SER E  1 371 ? 9.518   19.003  23.231  1.00 23.80 ?  395  SER E O   1 
ATOM   11851 C  CB  . SER E  1 371 ? 9.937   16.570  21.000  1.00 23.89 ?  395  SER E CB  1 
ATOM   11852 O  OG  . SER E  1 371 ? 9.288   15.407  20.510  1.00 24.38 ?  395  SER E OG  1 
ATOM   11853 N  N   . TYR E  1 372 ? 10.273  19.673  21.217  1.00 23.82 ?  396  TYR E N   1 
ATOM   11854 C  CA  . TYR E  1 372 ? 10.952  20.838  21.773  1.00 23.85 ?  396  TYR E CA  1 
ATOM   11855 C  C   . TYR E  1 372 ? 9.996   21.953  22.198  1.00 23.80 ?  396  TYR E C   1 
ATOM   11856 O  O   . TYR E  1 372 ? 10.216  22.596  23.227  1.00 23.92 ?  396  TYR E O   1 
ATOM   11857 C  CB  . TYR E  1 372 ? 12.030  21.396  20.833  1.00 23.83 ?  396  TYR E CB  1 
ATOM   11858 C  CG  . TYR E  1 372 ? 12.808  22.492  21.515  1.00 23.67 ?  396  TYR E CG  1 
ATOM   11859 C  CD1 . TYR E  1 372 ? 13.880  22.188  22.349  1.00 22.95 ?  396  TYR E CD1 1 
ATOM   11860 C  CD2 . TYR E  1 372 ? 12.429  23.828  21.382  1.00 23.45 ?  396  TYR E CD2 1 
ATOM   11861 C  CE1 . TYR E  1 372 ? 14.572  23.181  23.003  1.00 23.35 ?  396  TYR E CE1 1 
ATOM   11862 C  CE2 . TYR E  1 372 ? 13.113  24.828  22.038  1.00 23.15 ?  396  TYR E CE2 1 
ATOM   11863 C  CZ  . TYR E  1 372 ? 14.187  24.499  22.844  1.00 23.12 ?  396  TYR E CZ  1 
ATOM   11864 O  OH  . TYR E  1 372 ? 14.879  25.486  23.499  1.00 22.54 ?  396  TYR E OH  1 
ATOM   11865 N  N   . LEU E  1 373 ? 8.952   22.193  21.408  1.00 23.61 ?  397  LEU E N   1 
ATOM   11866 C  CA  . LEU E  1 373 ? 7.977   23.226  21.748  1.00 23.76 ?  397  LEU E CA  1 
ATOM   11867 C  C   . LEU E  1 373 ? 7.231   22.909  23.055  1.00 23.78 ?  397  LEU E C   1 
ATOM   11868 O  O   . LEU E  1 373 ? 6.855   23.828  23.790  1.00 23.70 ?  397  LEU E O   1 
ATOM   11869 C  CB  . LEU E  1 373 ? 7.018   23.505  20.580  1.00 23.62 ?  397  LEU E CB  1 
ATOM   11870 C  CG  . LEU E  1 373 ? 7.657   24.162  19.340  1.00 23.94 ?  397  LEU E CG  1 
ATOM   11871 C  CD1 . LEU E  1 373 ? 6.720   24.125  18.135  1.00 23.56 ?  397  LEU E CD1 1 
ATOM   11872 C  CD2 . LEU E  1 373 ? 8.118   25.592  19.610  1.00 23.13 ?  397  LEU E CD2 1 
ATOM   11873 N  N   . ASP E  1 374 ? 7.055   21.614  23.339  1.00 23.73 ?  398  ASP E N   1 
ATOM   11874 C  CA  . ASP E  1 374 ? 6.533   21.127  24.627  1.00 23.91 ?  398  ASP E CA  1 
ATOM   11875 C  C   . ASP E  1 374 ? 7.511   21.444  25.766  1.00 23.70 ?  398  ASP E C   1 
ATOM   11876 O  O   . ASP E  1 374 ? 7.095   21.824  26.864  1.00 23.72 ?  398  ASP E O   1 
ATOM   11877 C  CB  . ASP E  1 374 ? 6.267   19.615  24.562  1.00 24.06 ?  398  ASP E CB  1 
ATOM   11878 C  CG  . ASP E  1 374 ? 5.683   19.055  25.861  1.00 24.98 ?  398  ASP E CG  1 
ATOM   11879 O  OD1 . ASP E  1 374 ? 6.426   18.394  26.619  1.00 25.83 ?  398  ASP E OD1 1 
ATOM   11880 O  OD2 . ASP E  1 374 ? 4.485   19.274  26.129  1.00 26.13 -1 398  ASP E OD2 1 
ATOM   11881 N  N   . LEU E  1 375 ? 8.808   21.279  25.495  1.00 23.35 ?  399  LEU E N   1 
ATOM   11882 C  CA  . LEU E  1 375 ? 9.862   21.620  26.459  1.00 22.80 ?  399  LEU E CA  1 
ATOM   11883 C  C   . LEU E  1 375 ? 9.856   23.127  26.752  1.00 22.62 ?  399  LEU E C   1 
ATOM   11884 O  O   . LEU E  1 375 ? 9.979   23.542  27.910  1.00 22.51 ?  399  LEU E O   1 
ATOM   11885 C  CB  . LEU E  1 375 ? 11.232  21.151  25.940  1.00 22.82 ?  399  LEU E CB  1 
ATOM   11886 C  CG  . LEU E  1 375 ? 12.531  21.389  26.732  1.00 22.31 ?  399  LEU E CG  1 
ATOM   11887 C  CD1 . LEU E  1 375 ? 13.567  20.341  26.376  1.00 20.65 ?  399  LEU E CD1 1 
ATOM   11888 C  CD2 . LEU E  1 375 ? 13.097  22.780  26.480  1.00 21.36 ?  399  LEU E CD2 1 
ATOM   11889 N  N   . MET E  1 376 ? 9.695   23.930  25.698  1.00 22.17 ?  400  MET E N   1 
ATOM   11890 C  CA  . MET E  1 376 ? 9.622   25.387  25.812  1.00 22.04 ?  400  MET E CA  1 
ATOM   11891 C  C   . MET E  1 376 ? 8.464   25.830  26.709  1.00 21.85 ?  400  MET E C   1 
ATOM   11892 O  O   . MET E  1 376 ? 8.664   26.606  27.644  1.00 21.59 ?  400  MET E O   1 
ATOM   11893 C  CB  . MET E  1 376 ? 9.503   26.035  24.423  1.00 21.99 ?  400  MET E CB  1 
ATOM   11894 C  CG  . MET E  1 376 ? 9.332   27.552  24.442  1.00 22.23 ?  400  MET E CG  1 
ATOM   11895 S  SD  . MET E  1 376 ? 8.761   28.237  22.873  1.00 22.64 ?  400  MET E SD  1 
ATOM   11896 C  CE  . MET E  1 376 ? 7.054   27.692  22.862  1.00 22.33 ?  400  MET E CE  1 
ATOM   11897 N  N   . ASP E  1 377 ? 7.262   25.330  26.420  1.00 21.75 ?  401  ASP E N   1 
ATOM   11898 C  CA  . ASP E  1 377 ? 6.068   25.665  27.204  1.00 21.65 ?  401  ASP E CA  1 
ATOM   11899 C  C   . ASP E  1 377 ? 6.214   25.276  28.672  1.00 21.45 ?  401  ASP E C   1 
ATOM   11900 O  O   . ASP E  1 377 ? 5.986   26.094  29.555  1.00 21.47 ?  401  ASP E O   1 
ATOM   11901 C  CB  . ASP E  1 377 ? 4.822   24.996  26.620  1.00 21.43 ?  401  ASP E CB  1 
ATOM   11902 C  CG  . ASP E  1 377 ? 4.312   25.687  25.369  1.00 21.88 ?  401  ASP E CG  1 
ATOM   11903 O  OD1 . ASP E  1 377 ? 4.682   26.858  25.117  1.00 20.39 ?  401  ASP E OD1 1 
ATOM   11904 O  OD2 . ASP E  1 377 ? 3.524   25.050  24.637  1.00 22.59 -1 401  ASP E OD2 1 
ATOM   11905 N  N   . LYS E  1 378 ? 6.602   24.027  28.921  1.00 21.56 ?  402  LYS E N   1 
ATOM   11906 C  CA  . LYS E  1 378 ? 6.694   23.509  30.286  1.00 21.52 ?  402  LYS E CA  1 
ATOM   11907 C  C   . LYS E  1 378 ? 7.850   24.120  31.070  1.00 21.27 ?  402  LYS E C   1 
ATOM   11908 O  O   . LYS E  1 378 ? 7.731   24.344  32.273  1.00 21.59 ?  402  LYS E O   1 
ATOM   11909 C  CB  . LYS E  1 378 ? 6.789   21.981  30.282  1.00 21.68 ?  402  LYS E CB  1 
ATOM   11910 C  CG  . LYS E  1 378 ? 5.474   21.279  29.971  1.00 22.17 ?  402  LYS E CG  1 
ATOM   11911 C  CD  . LYS E  1 378 ? 5.655   19.772  29.947  1.00 23.17 ?  402  LYS E CD  1 
ATOM   11912 C  CE  . LYS E  1 378 ? 4.386   19.066  29.496  1.00 23.60 ?  402  LYS E CE  1 
ATOM   11913 N  NZ  . LYS E  1 378 ? 4.703   17.725  28.925  1.00 24.48 ?  402  LYS E NZ  1 
ATOM   11914 N  N   . GLY E  1 379 ? 8.961   24.392  30.390  1.00 21.14 ?  403  GLY E N   1 
ATOM   11915 C  CA  . GLY E  1 379 ? 10.098  25.066  31.020  1.00 21.03 ?  403  GLY E CA  1 
ATOM   11916 C  C   . GLY E  1 379 ? 9.759   26.489  31.432  1.00 20.98 ?  403  GLY E C   1 
ATOM   11917 O  O   . GLY E  1 379 ? 10.213  26.969  32.475  1.00 20.87 ?  403  GLY E O   1 
ATOM   11918 N  N   . THR E  1 380 ? 8.958   27.162  30.608  1.00 20.87 ?  404  THR E N   1 
ATOM   11919 C  CA  . THR E  1 380 ? 8.493   28.516  30.908  1.00 21.03 ?  404  THR E CA  1 
ATOM   11920 C  C   . THR E  1 380 ? 7.615   28.527  32.161  1.00 21.21 ?  404  THR E C   1 
ATOM   11921 O  O   . THR E  1 380 ? 7.784   29.375  33.042  1.00 21.21 ?  404  THR E O   1 
ATOM   11922 C  CB  . THR E  1 380 ? 7.734   29.134  29.716  1.00 20.87 ?  404  THR E CB  1 
ATOM   11923 O  OG1 . THR E  1 380 ? 8.573   29.119  28.554  1.00 20.25 ?  404  THR E OG1 1 
ATOM   11924 C  CG2 . THR E  1 380 ? 7.344   30.566  30.023  1.00 21.12 ?  404  THR E CG2 1 
ATOM   11925 N  N   . LEU E  1 381 ? 6.696   27.570  32.242  1.00 21.33 ?  405  LEU E N   1 
ATOM   11926 C  CA  . LEU E  1 381 ? 5.823   27.438  33.408  1.00 21.68 ?  405  LEU E CA  1 
ATOM   11927 C  C   . LEU E  1 381 ? 6.611   27.096  34.671  1.00 21.76 ?  405  LEU E C   1 
ATOM   11928 O  O   . LEU E  1 381 ? 6.303   27.601  35.753  1.00 21.68 ?  405  LEU E O   1 
ATOM   11929 C  CB  . LEU E  1 381 ? 4.743   26.384  33.156  1.00 21.67 ?  405  LEU E CB  1 
ATOM   11930 C  CG  . LEU E  1 381 ? 3.610   26.717  32.188  1.00 22.09 ?  405  LEU E CG  1 
ATOM   11931 C  CD1 . LEU E  1 381 ? 2.961   25.434  31.674  1.00 21.33 ?  405  LEU E CD1 1 
ATOM   11932 C  CD2 . LEU E  1 381 ? 2.578   27.642  32.850  1.00 21.89 ?  405  LEU E CD2 1 
ATOM   11933 N  N   . GLU E  1 382 ? 7.627   26.242  34.524  1.00 21.86 ?  406  GLU E N   1 
ATOM   11934 C  CA  . GLU E  1 382 ? 8.517   25.892  35.636  1.00 21.96 ?  406  GLU E CA  1 
ATOM   11935 C  C   . GLU E  1 382 ? 9.255   27.111  36.182  1.00 22.05 ?  406  GLU E C   1 
ATOM   11936 O  O   . GLU E  1 382 ? 9.420   27.252  37.395  1.00 22.13 ?  406  GLU E O   1 
ATOM   11937 C  CB  . GLU E  1 382 ? 9.497   24.791  35.228  1.00 21.80 ?  406  GLU E CB  1 
ATOM   11938 C  CG  . GLU E  1 382 ? 8.867   23.397  35.221  1.00 22.44 ?  406  GLU E CG  1 
ATOM   11939 C  CD  . GLU E  1 382 ? 9.488   22.455  34.195  1.00 23.39 ?  406  GLU E CD  1 
ATOM   11940 O  OE1 . GLU E  1 382 ? 10.659  22.652  33.802  1.00 22.01 ?  406  GLU E OE1 1 
ATOM   11941 O  OE2 . GLU E  1 382 ? 8.788   21.508  33.777  1.00 24.77 -1 406  GLU E OE2 1 
ATOM   11942 N  N   . GLY E  1 383 ? 9.682   27.994  35.282  1.00 22.20 ?  407  GLY E N   1 
ATOM   11943 C  CA  . GLY E  1 383 ? 10.265  29.275  35.677  1.00 22.16 ?  407  GLY E CA  1 
ATOM   11944 C  C   . GLY E  1 383 ? 9.249   30.159  36.384  1.00 22.17 ?  407  GLY E C   1 
ATOM   11945 O  O   . GLY E  1 383 ? 9.554   30.772  37.415  1.00 22.16 ?  407  GLY E O   1 
ATOM   11946 N  N   . LEU E  1 384 ? 8.039   30.214  35.827  1.00 22.03 ?  408  LEU E N   1 
ATOM   11947 C  CA  . LEU E  1 384 ? 6.947   31.006  36.394  1.00 22.12 ?  408  LEU E CA  1 
ATOM   11948 C  C   . LEU E  1 384 ? 6.581   30.560  37.806  1.00 22.23 ?  408  LEU E C   1 
ATOM   11949 O  O   . LEU E  1 384 ? 6.342   31.395  38.682  1.00 22.34 ?  408  LEU E O   1 
ATOM   11950 C  CB  . LEU E  1 384 ? 5.711   30.962  35.489  1.00 22.16 ?  408  LEU E CB  1 
ATOM   11951 C  CG  . LEU E  1 384 ? 4.484   31.788  35.901  1.00 21.89 ?  408  LEU E CG  1 
ATOM   11952 C  CD1 . LEU E  1 384 ? 4.837   33.256  36.149  1.00 21.53 ?  408  LEU E CD1 1 
ATOM   11953 C  CD2 . LEU E  1 384 ? 3.408   31.676  34.843  1.00 22.10 ?  408  LEU E CD2 1 
ATOM   11954 N  N   . ALA E  1 385 ? 6.549   29.247  38.017  1.00 22.43 ?  409  ALA E N   1 
ATOM   11955 C  CA  . ALA E  1 385 ? 6.273   28.669  39.330  1.00 22.61 ?  409  ALA E CA  1 
ATOM   11956 C  C   . ALA E  1 385 ? 7.287   29.147  40.365  1.00 22.57 ?  409  ALA E C   1 
ATOM   11957 O  O   . ALA E  1 385 ? 6.907   29.529  41.475  1.00 22.74 ?  409  ALA E O   1 
ATOM   11958 C  CB  . ALA E  1 385 ? 6.259   27.147  39.251  1.00 22.54 ?  409  ALA E CB  1 
ATOM   11959 N  N   . LYS E  1 386 ? 8.565   29.151  39.983  1.00 22.63 ?  410  LYS E N   1 
ATOM   11960 C  CA  . LYS E  1 386 ? 9.655   29.576  40.867  1.00 22.74 ?  410  LYS E CA  1 
ATOM   11961 C  C   . LYS E  1 386 ? 9.503   31.032  41.315  1.00 22.84 ?  410  LYS E C   1 
ATOM   11962 O  O   . LYS E  1 386 ? 9.672   31.343  42.498  1.00 22.82 ?  410  LYS E O   1 
ATOM   11963 C  CB  . LYS E  1 386 ? 11.022  29.352  40.201  1.00 22.64 ?  410  LYS E CB  1 
ATOM   11964 C  CG  . LYS E  1 386 ? 12.234  29.544  41.127  1.00 22.15 ?  410  LYS E CG  1 
ATOM   11965 C  CD  . LYS E  1 386 ? 12.355  28.408  42.143  1.00 22.01 ?  410  LYS E CD  1 
ATOM   11966 C  CE  . LYS E  1 386 ? 13.657  28.481  42.926  1.00 21.75 ?  410  LYS E CE  1 
ATOM   11967 N  NZ  . LYS E  1 386 ? 13.689  27.461  44.014  1.00 22.74 ?  410  LYS E NZ  1 
ATOM   11968 N  N   . TYR E  1 387 ? 9.182   31.908  40.364  1.00 23.13 ?  411  TYR E N   1 
ATOM   11969 C  CA  . TYR E  1 387 ? 8.907   33.313  40.649  1.00 23.50 ?  411  TYR E CA  1 
ATOM   11970 C  C   . TYR E  1 387 ? 7.674   33.490  41.535  1.00 23.81 ?  411  TYR E C   1 
ATOM   11971 O  O   . TYR E  1 387 ? 7.676   34.319  42.447  1.00 23.72 ?  411  TYR E O   1 
ATOM   11972 C  CB  . TYR E  1 387 ? 8.744   34.127  39.352  1.00 23.26 ?  411  TYR E CB  1 
ATOM   11973 C  CG  . TYR E  1 387 ? 7.877   35.363  39.521  1.00 23.68 ?  411  TYR E CG  1 
ATOM   11974 C  CD1 . TYR E  1 387 ? 8.342   36.479  40.220  1.00 24.11 ?  411  TYR E CD1 1 
ATOM   11975 C  CD2 . TYR E  1 387 ? 6.580   35.406  39.003  1.00 24.57 ?  411  TYR E CD2 1 
ATOM   11976 C  CE1 . TYR E  1 387 ? 7.539   37.610  40.395  1.00 24.24 ?  411  TYR E CE1 1 
ATOM   11977 C  CE2 . TYR E  1 387 ? 5.770   36.533  39.170  1.00 24.53 ?  411  TYR E CE2 1 
ATOM   11978 C  CZ  . TYR E  1 387 ? 6.259   37.629  39.862  1.00 24.55 ?  411  TYR E CZ  1 
ATOM   11979 O  OH  . TYR E  1 387 ? 5.466   38.743  40.024  1.00 25.45 ?  411  TYR E OH  1 
ATOM   11980 N  N   . GLN E  1 388 ? 6.623   32.722  41.246  1.00 24.34 ?  412  GLN E N   1 
ATOM   11981 C  CA  . GLN E  1 388 ? 5.359   32.835  41.976  1.00 24.59 ?  412  GLN E CA  1 
ATOM   11982 C  C   . GLN E  1 388 ? 5.513   32.508  43.458  1.00 24.83 ?  412  GLN E C   1 
ATOM   11983 O  O   . GLN E  1 388 ? 4.857   33.120  44.298  1.00 25.00 ?  412  GLN E O   1 
ATOM   11984 C  CB  . GLN E  1 388 ? 4.270   31.973  41.328  1.00 24.49 ?  412  GLN E CB  1 
ATOM   11985 C  CG  . GLN E  1 388 ? 3.644   32.623  40.099  1.00 24.54 ?  412  GLN E CG  1 
ATOM   11986 C  CD  . GLN E  1 388 ? 2.644   31.739  39.382  1.00 24.47 ?  412  GLN E CD  1 
ATOM   11987 O  OE1 . GLN E  1 388 ? 2.664   30.512  39.506  1.00 25.10 ?  412  GLN E OE1 1 
ATOM   11988 N  NE2 . GLN E  1 388 ? 1.762   32.363  38.615  1.00 24.28 ?  412  GLN E NE2 1 
ATOM   11989 N  N   . GLU E  1 389 ? 6.388   31.555  43.776  1.00 25.24 ?  413  GLU E N   1 
ATOM   11990 C  CA  . GLU E  1 389 ? 6.673   31.224  45.169  1.00 25.49 ?  413  GLU E CA  1 
ATOM   11991 C  C   . GLU E  1 389 ? 7.375   32.393  45.865  1.00 25.62 ?  413  GLU E C   1 
ATOM   11992 O  O   . GLU E  1 389 ? 7.002   32.773  46.977  1.00 25.61 ?  413  GLU E O   1 
ATOM   11993 C  CB  . GLU E  1 389 ? 7.508   29.947  45.275  1.00 25.66 ?  413  GLU E CB  1 
ATOM   11994 C  CG  . GLU E  1 389 ? 7.614   29.423  46.702  1.00 26.41 ?  413  GLU E CG  1 
ATOM   11995 C  CD  . GLU E  1 389 ? 8.350   28.105  46.812  1.00 27.52 ?  413  GLU E CD  1 
ATOM   11996 O  OE1 . GLU E  1 389 ? 8.220   27.251  45.905  1.00 26.94 ?  413  GLU E OE1 1 
ATOM   11997 O  OE2 . GLU E  1 389 ? 9.052   27.922  47.830  1.00 28.43 -1 413  GLU E OE2 1 
ATOM   11998 N  N   . ALA E  1 390 ? 8.368   32.969  45.189  1.00 25.63 ?  414  ALA E N   1 
ATOM   11999 C  CA  . ALA E  1 390 ? 9.113   34.113  45.710  1.00 25.65 ?  414  ALA E CA  1 
ATOM   12000 C  C   . ALA E  1 390 ? 8.241   35.361  45.854  1.00 25.79 ?  414  ALA E C   1 
ATOM   12001 O  O   . ALA E  1 390 ? 8.341   36.076  46.859  1.00 25.56 ?  414  ALA E O   1 
ATOM   12002 C  CB  . ALA E  1 390 ? 10.326  34.401  44.839  1.00 25.65 ?  414  ALA E CB  1 
ATOM   12003 N  N   . ASN E  1 391 ? 7.387   35.615  44.862  1.00 25.91 ?  415  ASN E N   1 
ATOM   12004 C  CA  . ASN E  1 391 ? 6.473   36.763  44.907  1.00 26.29 ?  415  ASN E CA  1 
ATOM   12005 C  C   . ASN E  1 391 ? 5.445   36.669  46.035  1.00 26.41 ?  415  ASN E C   1 
ATOM   12006 O  O   . ASN E  1 391 ? 5.054   37.690  46.606  1.00 26.64 ?  415  ASN E O   1 
ATOM   12007 C  CB  . ASN E  1 391 ? 5.764   36.984  43.567  1.00 26.14 ?  415  ASN E CB  1 
ATOM   12008 C  CG  . ASN E  1 391 ? 4.986   38.296  43.532  1.00 26.97 ?  415  ASN E CG  1 
ATOM   12009 O  OD1 . ASN E  1 391 ? 5.571   39.381  43.551  1.00 27.18 ?  415  ASN E OD1 1 
ATOM   12010 N  ND2 . ASN E  1 391 ? 3.658   38.199  43.489  1.00 27.36 ?  415  ASN E ND2 1 
ATOM   12011 N  N   . ALA E  1 392 ? 5.027   35.447  46.358  1.00 26.48 ?  416  ALA E N   1 
ATOM   12012 C  CA  . ALA E  1 392 ? 4.078   35.209  47.448  1.00 26.56 ?  416  ALA E CA  1 
ATOM   12013 C  C   . ALA E  1 392 ? 4.625   35.723  48.781  1.00 26.67 ?  416  ALA E C   1 
ATOM   12014 O  O   . ALA E  1 392 ? 3.885   36.285  49.585  1.00 26.71 ?  416  ALA E O   1 
ATOM   12015 C  CB  . ALA E  1 392 ? 3.727   33.726  47.539  1.00 26.39 ?  416  ALA E CB  1 
ATOM   12016 N  N   . ILE E  1 393 ? 5.928   35.536  48.989  1.00 26.82 ?  417  ILE E N   1 
ATOM   12017 C  CA  . ILE E  1 393 ? 6.634   36.037  50.167  1.00 26.97 ?  417  ILE E CA  1 
ATOM   12018 C  C   . ILE E  1 393 ? 6.673   37.570  50.209  1.00 27.00 ?  417  ILE E C   1 
ATOM   12019 O  O   . ILE E  1 393 ? 6.292   38.178  51.212  1.00 26.98 ?  417  ILE E O   1 
ATOM   12020 C  CB  . ILE E  1 393 ? 8.079   35.473  50.227  1.00 27.05 ?  417  ILE E CB  1 
ATOM   12021 C  CG1 . ILE E  1 393 ? 8.054   33.961  50.472  1.00 27.40 ?  417  ILE E CG1 1 
ATOM   12022 C  CG2 . ILE E  1 393 ? 8.907   36.182  51.299  1.00 27.30 ?  417  ILE E CG2 1 
ATOM   12023 C  CD1 . ILE E  1 393 ? 9.293   33.245  49.973  1.00 28.30 ?  417  ILE E CD1 1 
ATOM   12024 N  N   . VAL E  1 394 ? 7.129   38.184  49.119  1.00 27.19 ?  418  VAL E N   1 
ATOM   12025 C  CA  . VAL E  1 394 ? 7.366   39.631  49.086  1.00 27.23 ?  418  VAL E CA  1 
ATOM   12026 C  C   . VAL E  1 394 ? 6.056   40.420  49.018  1.00 27.64 ?  418  VAL E C   1 
ATOM   12027 O  O   . VAL E  1 394 ? 5.915   41.442  49.687  1.00 27.60 ?  418  VAL E O   1 
ATOM   12028 C  CB  . VAL E  1 394 ? 8.328   40.039  47.936  1.00 26.99 ?  418  VAL E CB  1 
ATOM   12029 C  CG1 . VAL E  1 394 ? 8.709   41.521  48.033  1.00 26.47 ?  418  VAL E CG1 1 
ATOM   12030 C  CG2 . VAL E  1 394 ? 9.585   39.176  47.956  1.00 26.43 ?  418  VAL E CG2 1 
ATOM   12031 N  N   . HIS E  1 395 ? 5.104   39.937  48.219  1.00 28.31 ?  419  HIS E N   1 
ATOM   12032 C  CA  . HIS E  1 395 ? 3.784   40.567  48.116  1.00 29.11 ?  419  HIS E CA  1 
ATOM   12033 C  C   . HIS E  1 395 ? 3.061   40.548  49.463  1.00 29.23 ?  419  HIS E C   1 
ATOM   12034 O  O   . HIS E  1 395 ? 2.404   41.522  49.826  1.00 29.20 ?  419  HIS E O   1 
ATOM   12035 C  CB  . HIS E  1 395 ? 2.930   39.903  47.024  1.00 29.30 ?  419  HIS E CB  1 
ATOM   12036 C  CG  . HIS E  1 395 ? 1.586   40.538  46.833  1.00 31.04 ?  419  HIS E CG  1 
ATOM   12037 N  ND1 . HIS E  1 395 ? 1.428   41.841  46.411  1.00 32.48 ?  419  HIS E ND1 1 
ATOM   12038 C  CD2 . HIS E  1 395 ? 0.335   40.045  46.999  1.00 32.53 ?  419  HIS E CD2 1 
ATOM   12039 C  CE1 . HIS E  1 395 ? 0.141   42.126  46.333  1.00 32.64 ?  419  HIS E CE1 1 
ATOM   12040 N  NE2 . HIS E  1 395 ? -0.544  41.052  46.681  1.00 33.41 ?  419  HIS E NE2 1 
ATOM   12041 N  N   . LYS E  1 396 ? 3.205   39.446  50.201  1.00 29.55 ?  420  LYS E N   1 
ATOM   12042 C  CA  . LYS E  1 396 ? 2.670   39.339  51.558  1.00 29.89 ?  420  LYS E CA  1 
ATOM   12043 C  C   . LYS E  1 396 ? 3.233   40.435  52.462  1.00 29.86 ?  420  LYS E C   1 
ATOM   12044 O  O   . LYS E  1 396 ? 2.482   41.087  53.193  1.00 29.77 ?  420  LYS E O   1 
ATOM   12045 C  CB  . LYS E  1 396 ? 2.945   37.951  52.148  1.00 30.05 ?  420  LYS E CB  1 
ATOM   12046 C  CG  . LYS E  1 396 ? 2.643   37.828  53.637  1.00 31.33 ?  420  LYS E CG  1 
ATOM   12047 C  CD  . LYS E  1 396 ? 3.100   36.484  54.205  1.00 33.16 ?  420  LYS E CD  1 
ATOM   12048 C  CE  . LYS E  1 396 ? 3.593   36.635  55.642  1.00 33.68 ?  420  LYS E CE  1 
ATOM   12049 N  NZ  . LYS E  1 396 ? 2.574   37.247  56.547  1.00 34.44 ?  420  LYS E NZ  1 
ATOM   12050 N  N   . MET E  1 397 ? 4.550   40.639  52.394  1.00 29.70 ?  421  MET E N   1 
ATOM   12051 C  CA  . MET E  1 397 ? 5.217   41.688  53.166  1.00 29.68 ?  421  MET E CA  1 
ATOM   12052 C  C   . MET E  1 397 ? 4.657   43.076  52.857  1.00 29.58 ?  421  MET E C   1 
ATOM   12053 O  O   . MET E  1 397 ? 4.417   43.867  53.773  1.00 29.41 ?  421  MET E O   1 
ATOM   12054 C  CB  . MET E  1 397 ? 6.731   41.667  52.933  1.00 29.71 ?  421  MET E CB  1 
ATOM   12055 C  CG  . MET E  1 397 ? 7.446   40.464  53.534  1.00 29.87 ?  421  MET E CG  1 
ATOM   12056 S  SD  . MET E  1 397 ? 9.240   40.609  53.430  1.00 30.63 ?  421  MET E SD  1 
ATOM   12057 C  CE  . MET E  1 397 ? 9.569   41.735  54.786  1.00 30.19 ?  421  MET E CE  1 
ATOM   12058 N  N   . TYR E  1 398 ? 4.447   43.360  51.571  1.00 29.60 ?  422  TYR E N   1 
ATOM   12059 C  CA  . TYR E  1 398 ? 3.866   44.633  51.142  1.00 29.75 ?  422  TYR E CA  1 
ATOM   12060 C  C   . TYR E  1 398 ? 2.485   44.857  51.751  1.00 30.12 ?  422  TYR E C   1 
ATOM   12061 O  O   . TYR E  1 398 ? 2.200   45.935  52.278  1.00 30.11 ?  422  TYR E O   1 
ATOM   12062 C  CB  . TYR E  1 398 ? 3.778   44.719  49.613  1.00 29.39 ?  422  TYR E CB  1 
ATOM   12063 C  CG  . TYR E  1 398 ? 3.011   45.932  49.120  1.00 28.82 ?  422  TYR E CG  1 
ATOM   12064 C  CD1 . TYR E  1 398 ? 3.636   47.173  48.989  1.00 28.37 ?  422  TYR E CD1 1 
ATOM   12065 C  CD2 . TYR E  1 398 ? 1.655   45.840  48.799  1.00 28.42 ?  422  TYR E CD2 1 
ATOM   12066 C  CE1 . TYR E  1 398 ? 2.929   48.289  48.542  1.00 27.90 ?  422  TYR E CE1 1 
ATOM   12067 C  CE2 . TYR E  1 398 ? 0.940   46.950  48.355  1.00 27.96 ?  422  TYR E CE2 1 
ATOM   12068 C  CZ  . TYR E  1 398 ? 1.581   48.167  48.229  1.00 27.80 ?  422  TYR E CZ  1 
ATOM   12069 O  OH  . TYR E  1 398 ? 0.873   49.257  47.783  1.00 27.40 ?  422  TYR E OH  1 
ATOM   12070 N  N   . GLU E  1 399 ? 1.635   43.837  51.666  1.00 30.59 ?  423  GLU E N   1 
ATOM   12071 C  CA  . GLU E  1 399 ? 0.279   43.916  52.205  1.00 31.22 ?  423  GLU E CA  1 
ATOM   12072 C  C   . GLU E  1 399 ? 0.273   43.965  53.733  1.00 31.19 ?  423  GLU E C   1 
ATOM   12073 O  O   . GLU E  1 399 ? -0.616  44.571  54.330  1.00 31.44 ?  423  GLU E O   1 
ATOM   12074 C  CB  . GLU E  1 399 ? -0.581  42.759  51.693  1.00 31.52 ?  423  GLU E CB  1 
ATOM   12075 C  CG  . GLU E  1 399 ? -0.918  42.845  50.207  1.00 33.06 ?  423  GLU E CG  1 
ATOM   12076 C  CD  . GLU E  1 399 ? -2.074  41.945  49.812  1.00 35.58 ?  423  GLU E CD  1 
ATOM   12077 O  OE1 . GLU E  1 399 ? -2.798  42.286  48.848  1.00 37.02 ?  423  GLU E OE1 1 
ATOM   12078 O  OE2 . GLU E  1 399 ? -2.267  40.898  50.463  1.00 36.26 -1 423  GLU E OE2 1 
ATOM   12079 N  N   . ASP E  1 400 ? 1.275   43.344  54.354  1.00 31.10 ?  424  ASP E N   1 
ATOM   12080 C  CA  . ASP E  1 400 ? 1.452   43.396  55.809  1.00 30.96 ?  424  ASP E CA  1 
ATOM   12081 C  C   . ASP E  1 400 ? 2.090   44.702  56.273  1.00 30.75 ?  424  ASP E C   1 
ATOM   12082 O  O   . ASP E  1 400 ? 2.137   44.983  57.473  1.00 30.71 ?  424  ASP E O   1 
ATOM   12083 C  CB  . ASP E  1 400 ? 2.300   42.220  56.294  1.00 30.96 ?  424  ASP E CB  1 
ATOM   12084 C  CG  . ASP E  1 400 ? 1.526   40.925  56.353  1.00 31.59 ?  424  ASP E CG  1 
ATOM   12085 O  OD1 . ASP E  1 400 ? 0.290   40.957  56.185  1.00 32.18 ?  424  ASP E OD1 1 
ATOM   12086 O  OD2 . ASP E  1 400 ? 2.157   39.868  56.574  1.00 32.75 -1 424  ASP E OD2 1 
ATOM   12087 N  N   . GLY E  1 401 ? 2.593   45.482  55.318  1.00 30.49 ?  425  GLY E N   1 
ATOM   12088 C  CA  . GLY E  1 401 ? 3.244   46.756  55.608  1.00 30.14 ?  425  GLY E CA  1 
ATOM   12089 C  C   . GLY E  1 401 ? 4.627   46.618  56.218  1.00 29.93 ?  425  GLY E C   1 
ATOM   12090 O  O   . GLY E  1 401 ? 5.098   47.536  56.893  1.00 30.07 ?  425  GLY E O   1 
ATOM   12091 N  N   . THR E  1 402 ? 5.289   45.488  55.964  1.00 29.51 ?  426  THR E N   1 
ATOM   12092 C  CA  . THR E  1 402 ? 6.561   45.170  56.627  1.00 29.26 ?  426  THR E CA  1 
ATOM   12093 C  C   . THR E  1 402 ? 7.828   45.353  55.777  1.00 29.17 ?  426  THR E C   1 
ATOM   12094 O  O   . THR E  1 402 ? 8.933   45.074  56.255  1.00 29.04 ?  426  THR E O   1 
ATOM   12095 C  CB  . THR E  1 402 ? 6.566   43.739  57.222  1.00 29.31 ?  426  THR E CB  1 
ATOM   12096 O  OG1 . THR E  1 402 ? 6.144   42.800  56.226  1.00 29.16 ?  426  THR E OG1 1 
ATOM   12097 C  CG2 . THR E  1 402 ? 5.646   43.650  58.442  1.00 29.25 ?  426  THR E CG2 1 
ATOM   12098 N  N   . LEU E  1 403 ? 7.678   45.820  54.537  1.00 28.80 ?  427  LEU E N   1 
ATOM   12099 C  CA  . LEU E  1 403 ? 8.843   46.140  53.708  1.00 28.65 ?  427  LEU E CA  1 
ATOM   12100 C  C   . LEU E  1 403 ? 9.634   47.301  54.309  1.00 28.62 ?  427  LEU E C   1 
ATOM   12101 O  O   . LEU E  1 403 ? 9.066   48.195  54.948  1.00 28.60 ?  427  LEU E O   1 
ATOM   12102 C  CB  . LEU E  1 403 ? 8.440   46.469  52.266  1.00 28.55 ?  427  LEU E CB  1 
ATOM   12103 C  CG  . LEU E  1 403 ? 7.844   45.376  51.372  1.00 28.27 ?  427  LEU E CG  1 
ATOM   12104 C  CD1 . LEU E  1 403 ? 7.319   45.996  50.086  1.00 27.90 ?  427  LEU E CD1 1 
ATOM   12105 C  CD2 . LEU E  1 403 ? 8.850   44.265  51.064  1.00 27.77 ?  427  LEU E CD2 1 
ATOM   12106 N  N   . THR E  1 404 ? 10.947  47.273  54.100  1.00 28.59 ?  428  THR E N   1 
ATOM   12107 C  CA  . THR E  1 404 ? 11.853  48.300  54.608  1.00 28.44 ?  428  THR E CA  1 
ATOM   12108 C  C   . THR E  1 404 ? 11.441  49.701  54.148  1.00 28.59 ?  428  THR E C   1 
ATOM   12109 O  O   . THR E  1 404 ? 11.265  49.949  52.951  1.00 28.45 ?  428  THR E O   1 
ATOM   12110 C  CB  . THR E  1 404 ? 13.321  47.979  54.221  1.00 28.35 ?  428  THR E CB  1 
ATOM   12111 O  OG1 . THR E  1 404 ? 13.710  46.752  54.846  1.00 28.19 ?  428  THR E OG1 1 
ATOM   12112 C  CG2 . THR E  1 404 ? 14.269  49.077  54.671  1.00 28.06 ?  428  THR E CG2 1 
ATOM   12113 N  N   . GLY E  1 405 ? 11.260  50.592  55.124  1.00 28.76 ?  429  GLY E N   1 
ATOM   12114 C  CA  . GLY E  1 405 ? 10.876  51.981  54.883  1.00 29.11 ?  429  GLY E CA  1 
ATOM   12115 C  C   . GLY E  1 405 ? 9.455   52.210  54.390  1.00 29.34 ?  429  GLY E C   1 
ATOM   12116 O  O   . GLY E  1 405 ? 9.090   53.343  54.067  1.00 29.41 ?  429  GLY E O   1 
ATOM   12117 N  N   . GLN E  1 406 ? 8.649   51.148  54.342  1.00 29.43 ?  430  GLN E N   1 
ATOM   12118 C  CA  . GLN E  1 406 ? 7.292   51.218  53.780  1.00 29.80 ?  430  GLN E CA  1 
ATOM   12119 C  C   . GLN E  1 406 ? 6.381   52.263  54.436  1.00 30.15 ?  430  GLN E C   1 
ATOM   12120 O  O   . GLN E  1 406 ? 5.568   52.891  53.757  1.00 30.34 ?  430  GLN E O   1 
ATOM   12121 C  CB  . GLN E  1 406 ? 6.617   49.845  53.804  1.00 29.69 ?  430  GLN E CB  1 
ATOM   12122 C  CG  . GLN E  1 406 ? 5.410   49.738  52.872  1.00 29.36 ?  430  GLN E CG  1 
ATOM   12123 C  CD  . GLN E  1 406 ? 4.827   48.343  52.804  1.00 28.94 ?  430  GLN E CD  1 
ATOM   12124 O  OE1 . GLN E  1 406 ? 5.438   47.373  53.251  1.00 28.92 ?  430  GLN E OE1 1 
ATOM   12125 N  NE2 . GLN E  1 406 ? 3.632   48.234  52.234  1.00 29.42 ?  430  GLN E NE2 1 
ATOM   12126 N  N   . LYS E  1 407 ? 6.522   52.440  55.747  1.00 30.52 ?  431  LYS E N   1 
ATOM   12127 C  CA  . LYS E  1 407 ? 5.687   53.380  56.499  1.00 30.90 ?  431  LYS E CA  1 
ATOM   12128 C  C   . LYS E  1 407 ? 6.485   54.595  56.964  1.00 30.89 ?  431  LYS E C   1 
ATOM   12129 O  O   . LYS E  1 407 ? 5.951   55.482  57.632  1.00 31.18 ?  431  LYS E O   1 
ATOM   12130 C  CB  . LYS E  1 407 ? 5.051   52.676  57.707  1.00 30.97 ?  431  LYS E CB  1 
ATOM   12131 C  CG  . LYS E  1 407 ? 4.160   51.487  57.356  1.00 31.61 ?  431  LYS E CG  1 
ATOM   12132 C  CD  . LYS E  1 407 ? 2.965   51.906  56.503  1.00 32.47 ?  431  LYS E CD  1 
ATOM   12133 C  CE  . LYS E  1 407 ? 2.122   50.704  56.113  1.00 33.15 ?  431  LYS E CE  1 
ATOM   12134 N  NZ  . LYS E  1 407 ? 1.070   51.078  55.131  1.00 33.17 ?  431  LYS E NZ  1 
ATOM   12135 N  N   . THR E  1 408 ? 7.757   54.632  56.580  1.00 30.80 ?  432  THR E N   1 
ATOM   12136 C  CA  . THR E  1 408 ? 8.723   55.592  57.107  1.00 30.59 ?  432  THR E CA  1 
ATOM   12137 C  C   . THR E  1 408 ? 9.363   56.442  56.003  1.00 30.22 ?  432  THR E C   1 
ATOM   12138 O  O   . THR E  1 408 ? 9.599   57.642  56.188  1.00 30.08 ?  432  THR E O   1 
ATOM   12139 C  CB  . THR E  1 408 ? 9.782   54.846  57.976  1.00 30.67 ?  432  THR E CB  1 
ATOM   12140 O  OG1 . THR E  1 408 ? 9.351   54.850  59.347  1.00 31.30 ?  432  THR E OG1 1 
ATOM   12141 C  CG2 . THR E  1 408 ? 11.166  55.476  57.885  1.00 31.37 ?  432  THR E CG2 1 
ATOM   12142 N  N   . ASN E  1 409 ? 9.618   55.825  54.852  1.00 29.73 ?  433  ASN E N   1 
ATOM   12143 C  CA  . ASN E  1 409 ? 10.316  56.495  53.759  1.00 29.47 ?  433  ASN E CA  1 
ATOM   12144 C  C   . ASN E  1 409 ? 9.956   55.935  52.378  1.00 29.22 ?  433  ASN E C   1 
ATOM   12145 O  O   . ASN E  1 409 ? 10.833  55.523  51.621  1.00 29.02 ?  433  ASN E O   1 
ATOM   12146 C  CB  . ASN E  1 409 ? 11.833  56.439  53.996  1.00 29.43 ?  433  ASN E CB  1 
ATOM   12147 C  CG  . ASN E  1 409 ? 12.604  57.429  53.132  1.00 29.66 ?  433  ASN E CG  1 
ATOM   12148 O  OD1 . ASN E  1 409 ? 12.103  58.501  52.792  1.00 29.04 ?  433  ASN E OD1 1 
ATOM   12149 N  ND2 . ASN E  1 409 ? 13.832  57.066  52.775  1.00 29.60 ?  433  ASN E ND2 1 
ATOM   12150 N  N   . ARG E  1 410 ? 8.661   55.917  52.064  1.00 28.90 ?  434  ARG E N   1 
ATOM   12151 C  CA  . ARG E  1 410 ? 8.181   55.494  50.750  1.00 28.79 ?  434  ARG E CA  1 
ATOM   12152 C  C   . ARG E  1 410 ? 7.423   56.634  50.053  1.00 28.61 ?  434  ARG E C   1 
ATOM   12153 O  O   . ARG E  1 410 ? 6.188   56.657  50.050  1.00 28.57 ?  434  ARG E O   1 
ATOM   12154 C  CB  . ARG E  1 410 ? 7.312   54.229  50.856  1.00 28.97 ?  434  ARG E CB  1 
ATOM   12155 C  CG  . ARG E  1 410 ? 6.787   53.717  49.512  1.00 29.31 ?  434  ARG E CG  1 
ATOM   12156 C  CD  . ARG E  1 410 ? 5.858   52.524  49.658  1.00 29.56 ?  434  ARG E CD  1 
ATOM   12157 N  NE  . ARG E  1 410 ? 6.624   51.289  49.678  1.00 31.15 ?  434  ARG E NE  1 
ATOM   12158 C  CZ  . ARG E  1 410 ? 6.733   50.435  48.663  1.00 30.33 ?  434  ARG E CZ  1 
ATOM   12159 N  NH1 . ARG E  1 410 ? 6.092   50.638  47.517  1.00 29.92 ?  434  ARG E NH1 1 
ATOM   12160 N  NH2 . ARG E  1 410 ? 7.481   49.356  48.815  1.00 30.46 ?  434  ARG E NH2 1 
ATOM   12161 N  N   . PRO E  1 411 ? 8.164   57.587  49.457  1.00 28.42 ?  435  PRO E N   1 
ATOM   12162 C  CA  . PRO E  1 411 ? 7.491   58.702  48.793  1.00 28.26 ?  435  PRO E CA  1 
ATOM   12163 C  C   . PRO E  1 411 ? 6.741   58.247  47.544  1.00 28.25 ?  435  PRO E C   1 
ATOM   12164 O  O   . PRO E  1 411 ? 7.122   57.257  46.906  1.00 27.89 ?  435  PRO E O   1 
ATOM   12165 C  CB  . PRO E  1 411 ? 8.643   59.636  48.417  1.00 28.19 ?  435  PRO E CB  1 
ATOM   12166 C  CG  . PRO E  1 411 ? 9.828   58.752  48.307  1.00 28.13 ?  435  PRO E CG  1 
ATOM   12167 C  CD  . PRO E  1 411 ? 9.631   57.673  49.329  1.00 28.38 ?  435  PRO E CD  1 
ATOM   12168 N  N   . ASN E  1 412 ? 5.679   58.972  47.212  1.00 28.22 ?  436  ASN E N   1 
ATOM   12169 C  CA  . ASN E  1 412 ? 4.848   58.639  46.064  1.00 28.17 ?  436  ASN E CA  1 
ATOM   12170 C  C   . ASN E  1 412 ? 5.568   58.873  44.736  1.00 27.83 ?  436  ASN E C   1 
ATOM   12171 O  O   . ASN E  1 412 ? 6.384   59.791  44.627  1.00 27.91 ?  436  ASN E O   1 
ATOM   12172 C  CB  . ASN E  1 412 ? 3.522   59.406  46.127  1.00 28.21 ?  436  ASN E CB  1 
ATOM   12173 C  CG  . ASN E  1 412 ? 2.668   58.995  47.322  1.00 28.88 ?  436  ASN E CG  1 
ATOM   12174 O  OD1 . ASN E  1 412 ? 2.596   57.818  47.673  1.00 29.85 ?  436  ASN E OD1 1 
ATOM   12175 N  ND2 . ASN E  1 412 ? 2.022   59.968  47.953  1.00 29.86 ?  436  ASN E ND2 1 
ATOM   12176 N  N   . PRO E  1 413 ? 5.284   58.026  43.730  1.00 27.71 ?  437  PRO E N   1 
ATOM   12177 C  CA  . PRO E  1 413 ? 5.833   58.196  42.379  1.00 27.58 ?  437  PRO E CA  1 
ATOM   12178 C  C   . PRO E  1 413 ? 5.336   59.477  41.706  1.00 27.63 ?  437  PRO E C   1 
ATOM   12179 O  O   . PRO E  1 413 ? 4.339   60.050  42.159  1.00 27.51 ?  437  PRO E O   1 
ATOM   12180 C  CB  . PRO E  1 413 ? 5.322   56.956  41.633  1.00 27.68 ?  437  PRO E CB  1 
ATOM   12181 C  CG  . PRO E  1 413 ? 4.180   56.448  42.448  1.00 27.59 ?  437  PRO E CG  1 
ATOM   12182 C  CD  . PRO E  1 413 ? 4.541   56.759  43.858  1.00 27.60 ?  437  PRO E CD  1 
ATOM   12183 N  N   . PRO E  1 414 ? 6.031   59.935  40.640  1.00 27.52 ?  438  PRO E N   1 
ATOM   12184 C  CA  . PRO E  1 414 ? 5.616   61.166  39.962  1.00 27.58 ?  438  PRO E CA  1 
ATOM   12185 C  C   . PRO E  1 414 ? 4.321   61.007  39.158  1.00 27.57 ?  438  PRO E C   1 
ATOM   12186 O  O   . PRO E  1 414 ? 4.095   59.970  38.530  1.00 27.53 ?  438  PRO E O   1 
ATOM   12187 C  CB  . PRO E  1 414 ? 6.792   61.470  39.025  1.00 27.43 ?  438  PRO E CB  1 
ATOM   12188 C  CG  . PRO E  1 414 ? 7.424   60.153  38.772  1.00 27.51 ?  438  PRO E CG  1 
ATOM   12189 C  CD  . PRO E  1 414 ? 7.253   59.363  40.039  1.00 27.56 ?  438  PRO E CD  1 
ATOM   12190 N  N   . GLU E  1 415 ? 3.494   62.049  39.189  1.00 27.60 ?  439  GLU E N   1 
ATOM   12191 C  CA  . GLU E  1 415 ? 2.209   62.091  38.485  1.00 27.61 ?  439  GLU E CA  1 
ATOM   12192 C  C   . GLU E  1 415 ? 2.340   61.754  36.991  1.00 27.38 ?  439  GLU E C   1 
ATOM   12193 O  O   . GLU E  1 415 ? 3.322   62.134  36.358  1.00 27.19 ?  439  GLU E O   1 
ATOM   12194 C  CB  . GLU E  1 415 ? 1.578   63.476  38.657  1.00 27.59 ?  439  GLU E CB  1 
ATOM   12195 C  CG  . GLU E  1 415 ? 2.505   64.622  38.249  1.00 28.02 ?  439  GLU E CG  1 
ATOM   12196 C  CD  . GLU E  1 415 ? 1.880   65.993  38.410  1.00 28.47 ?  439  GLU E CD  1 
ATOM   12197 O  OE1 . GLU E  1 415 ? 0.687   66.077  38.779  1.00 29.03 ?  439  GLU E OE1 1 
ATOM   12198 O  OE2 . GLU E  1 415 ? 2.593   66.989  38.160  1.00 28.22 -1 439  GLU E OE2 1 
ATOM   12199 N  N   . PRO E  1 416 ? 1.338   61.061  36.421  1.00 27.40 ?  440  PRO E N   1 
ATOM   12200 C  CA  . PRO E  1 416 ? 0.093   60.653  37.064  1.00 27.59 ?  440  PRO E CA  1 
ATOM   12201 C  C   . PRO E  1 416 ? 0.127   59.247  37.672  1.00 27.77 ?  440  PRO E C   1 
ATOM   12202 O  O   . PRO E  1 416 ? -0.927  58.629  37.844  1.00 27.98 ?  440  PRO E O   1 
ATOM   12203 C  CB  . PRO E  1 416 ? -0.910  60.708  35.908  1.00 27.64 ?  440  PRO E CB  1 
ATOM   12204 C  CG  . PRO E  1 416 ? -0.099  60.331  34.702  1.00 27.24 ?  440  PRO E CG  1 
ATOM   12205 C  CD  . PRO E  1 416 ? 1.347   60.702  34.990  1.00 27.45 ?  440  PRO E CD  1 
ATOM   12206 N  N   . GLU E  1 417 ? 1.316   58.748  38.005  1.00 27.89 ?  441  GLU E N   1 
ATOM   12207 C  CA  . GLU E  1 417 ? 1.431   57.411  38.588  1.00 27.97 ?  441  GLU E CA  1 
ATOM   12208 C  C   . GLU E  1 417 ? 0.843   57.345  39.993  1.00 28.26 ?  441  GLU E C   1 
ATOM   12209 O  O   . GLU E  1 417 ? 0.917   58.310  40.759  1.00 28.30 ?  441  GLU E O   1 
ATOM   12210 C  CB  . GLU E  1 417 ? 2.885   56.913  38.580  1.00 27.78 ?  441  GLU E CB  1 
ATOM   12211 C  CG  . GLU E  1 417 ? 3.088   55.463  39.060  1.00 27.13 ?  441  GLU E CG  1 
ATOM   12212 C  CD  . GLU E  1 417 ? 2.417   54.424  38.172  1.00 26.47 ?  441  GLU E CD  1 
ATOM   12213 O  OE1 . GLU E  1 417 ? 1.170   54.337  38.169  1.00 26.32 ?  441  GLU E OE1 1 
ATOM   12214 O  OE2 . GLU E  1 417 ? 3.140   53.674  37.489  1.00 25.88 -1 441  GLU E OE2 1 
ATOM   12215 N  N   . LYS E  1 418 ? 0.247   56.199  40.309  1.00 28.62 ?  442  LYS E N   1 
ATOM   12216 C  CA  . LYS E  1 418 ? -0.270  55.924  41.643  1.00 28.96 ?  442  LYS E CA  1 
ATOM   12217 C  C   . LYS E  1 418 ? 0.630   54.905  42.348  1.00 28.72 ?  442  LYS E C   1 
ATOM   12218 O  O   . LYS E  1 418 ? 1.251   54.070  41.684  1.00 28.68 ?  442  LYS E O   1 
ATOM   12219 C  CB  . LYS E  1 418 ? -1.715  55.417  41.566  1.00 29.22 ?  442  LYS E CB  1 
ATOM   12220 C  CG  . LYS E  1 418 ? -2.727  56.455  41.067  1.00 30.82 ?  442  LYS E CG  1 
ATOM   12221 C  CD  . LYS E  1 418 ? -2.797  57.659  42.005  1.00 34.09 ?  442  LYS E CD  1 
ATOM   12222 C  CE  . LYS E  1 418 ? -3.739  58.741  41.487  1.00 35.93 ?  442  LYS E CE  1 
ATOM   12223 N  NZ  . LYS E  1 418 ? -3.382  60.085  42.058  1.00 37.01 ?  442  LYS E NZ  1 
ATOM   12224 N  N   . PRO E  1 419 ? 0.713   54.976  43.692  1.00 28.53 ?  443  PRO E N   1 
ATOM   12225 C  CA  . PRO E  1 419 ? 1.547   54.030  44.447  1.00 28.33 ?  443  PRO E CA  1 
ATOM   12226 C  C   . PRO E  1 419 ? 1.036   52.588  44.391  1.00 28.06 ?  443  PRO E C   1 
ATOM   12227 O  O   . PRO E  1 419 ? -0.174  52.358  44.320  1.00 28.38 ?  443  PRO E O   1 
ATOM   12228 C  CB  . PRO E  1 419 ? 1.481   54.563  45.884  1.00 28.38 ?  443  PRO E CB  1 
ATOM   12229 C  CG  . PRO E  1 419 ? 0.246   55.400  45.937  1.00 28.64 ?  443  PRO E CG  1 
ATOM   12230 C  CD  . PRO E  1 419 ? 0.102   55.994  44.569  1.00 28.41 ?  443  PRO E CD  1 
ATOM   12231 N  N   . GLY E  1 420 ? 1.965   51.636  44.415  1.00 27.46 ?  444  GLY E N   1 
ATOM   12232 C  CA  . GLY E  1 420 ? 1.635   50.213  44.407  1.00 26.91 ?  444  GLY E CA  1 
ATOM   12233 C  C   . GLY E  1 420 ? 2.860   49.338  44.619  1.00 26.53 ?  444  GLY E C   1 
ATOM   12234 O  O   . GLY E  1 420 ? 3.959   49.845  44.848  1.00 26.20 ?  444  GLY E O   1 
ATOM   12235 N  N   . PHE E  1 421 ? 2.664   48.023  44.533  1.00 26.19 ?  445  PHE E N   1 
ATOM   12236 C  CA  . PHE E  1 421 ? 3.736   47.048  44.747  1.00 25.86 ?  445  PHE E CA  1 
ATOM   12237 C  C   . PHE E  1 421 ? 4.307   46.497  43.443  1.00 25.71 ?  445  PHE E C   1 
ATOM   12238 O  O   . PHE E  1 421 ? 3.558   46.104  42.552  1.00 25.72 ?  445  PHE E O   1 
ATOM   12239 C  CB  . PHE E  1 421 ? 3.235   45.889  45.619  1.00 25.82 ?  445  PHE E CB  1 
ATOM   12240 C  CG  . PHE E  1 421 ? 4.170   44.703  45.665  1.00 25.48 ?  445  PHE E CG  1 
ATOM   12241 C  CD1 . PHE E  1 421 ? 5.325   44.737  46.441  1.00 24.17 ?  445  PHE E CD1 1 
ATOM   12242 C  CD2 . PHE E  1 421 ? 3.887   43.549  44.933  1.00 25.57 ?  445  PHE E CD2 1 
ATOM   12243 C  CE1 . PHE E  1 421 ? 6.186   43.646  46.491  1.00 24.73 ?  445  PHE E CE1 1 
ATOM   12244 C  CE2 . PHE E  1 421 ? 4.746   42.445  44.974  1.00 26.02 ?  445  PHE E CE2 1 
ATOM   12245 C  CZ  . PHE E  1 421 ? 5.900   42.496  45.756  1.00 25.54 ?  445  PHE E CZ  1 
ATOM   12246 N  N   . GLY E  1 422 ? 5.636   46.446  43.357  1.00 25.50 ?  446  GLY E N   1 
ATOM   12247 C  CA  . GLY E  1 422 ? 6.328   45.833  42.220  1.00 25.15 ?  446  GLY E CA  1 
ATOM   12248 C  C   . GLY E  1 422 ? 5.814   46.304  40.872  1.00 24.96 ?  446  GLY E C   1 
ATOM   12249 O  O   . GLY E  1 422 ? 5.496   45.492  40.000  1.00 24.80 ?  446  GLY E O   1 
ATOM   12250 N  N   . ILE E  1 423 ? 5.727   47.622  40.713  1.00 24.70 ?  447  ILE E N   1 
ATOM   12251 C  CA  . ILE E  1 423 ? 5.187   48.221  39.496  1.00 24.77 ?  447  ILE E CA  1 
ATOM   12252 C  C   . ILE E  1 423 ? 6.300   48.584  38.522  1.00 24.67 ?  447  ILE E C   1 
ATOM   12253 O  O   . ILE E  1 423 ? 7.440   48.822  38.930  1.00 24.57 ?  447  ILE E O   1 
ATOM   12254 C  CB  . ILE E  1 423 ? 4.278   49.448  39.793  1.00 24.76 ?  447  ILE E CB  1 
ATOM   12255 C  CG1 . ILE E  1 423 ? 5.032   50.527  40.586  1.00 24.78 ?  447  ILE E CG1 1 
ATOM   12256 C  CG2 . ILE E  1 423 ? 2.998   48.993  40.506  1.00 24.82 ?  447  ILE E CG2 1 
ATOM   12257 C  CD1 . ILE E  1 423 ? 4.283   51.854  40.724  1.00 25.10 ?  447  ILE E CD1 1 
ATOM   12258 N  N   . PHE E  1 424 ? 5.961   48.626  37.236  1.00 24.70 ?  448  PHE E N   1 
ATOM   12259 C  CA  . PHE E  1 424 ? 6.942   48.901  36.188  1.00 24.78 ?  448  PHE E CA  1 
ATOM   12260 C  C   . PHE E  1 424 ? 7.708   50.198  36.448  1.00 24.58 ?  448  PHE E C   1 
ATOM   12261 O  O   . PHE E  1 424 ? 8.901   50.293  36.160  1.00 24.61 ?  448  PHE E O   1 
ATOM   12262 C  CB  . PHE E  1 424 ? 6.286   48.932  34.801  1.00 24.82 ?  448  PHE E CB  1 
ATOM   12263 C  CG  . PHE E  1 424 ? 7.265   49.166  33.685  1.00 25.08 ?  448  PHE E CG  1 
ATOM   12264 C  CD1 . PHE E  1 424 ? 8.001   48.109  33.156  1.00 24.49 ?  448  PHE E CD1 1 
ATOM   12265 C  CD2 . PHE E  1 424 ? 7.476   50.449  33.186  1.00 24.94 ?  448  PHE E CD2 1 
ATOM   12266 C  CE1 . PHE E  1 424 ? 8.925   48.325  32.138  1.00 25.18 ?  448  PHE E CE1 1 
ATOM   12267 C  CE2 . PHE E  1 424 ? 8.397   50.675  32.163  1.00 25.64 ?  448  PHE E CE2 1 
ATOM   12268 C  CZ  . PHE E  1 424 ? 9.120   49.611  31.637  1.00 25.21 ?  448  PHE E CZ  1 
ATOM   12269 N  N   . THR E  1 425 ? 7.005   51.179  37.009  1.00 24.48 ?  449  THR E N   1 
ATOM   12270 C  CA  . THR E  1 425 ? 7.570   52.478  37.367  1.00 24.38 ?  449  THR E CA  1 
ATOM   12271 C  C   . THR E  1 425 ? 8.852   52.383  38.206  1.00 24.00 ?  449  THR E C   1 
ATOM   12272 O  O   . THR E  1 425 ? 9.795   53.152  38.003  1.00 23.70 ?  449  THR E O   1 
ATOM   12273 C  CB  . THR E  1 425 ? 6.503   53.353  38.074  1.00 24.43 ?  449  THR E CB  1 
ATOM   12274 O  OG1 . THR E  1 425 ? 5.571   53.827  37.096  1.00 25.23 ?  449  THR E OG1 1 
ATOM   12275 C  CG2 . THR E  1 425 ? 7.129   54.557  38.793  1.00 24.50 ?  449  THR E CG2 1 
ATOM   12276 N  N   . GLN E  1 426 ? 8.883   51.422  39.123  1.00 23.62 ?  450  GLN E N   1 
ATOM   12277 C  CA  . GLN E  1 426 ? 10.015  51.241  40.033  1.00 23.68 ?  450  GLN E CA  1 
ATOM   12278 C  C   . GLN E  1 426 ? 11.319  50.786  39.353  1.00 23.55 ?  450  GLN E C   1 
ATOM   12279 O  O   . GLN E  1 426 ? 12.367  50.721  39.997  1.00 23.57 ?  450  GLN E O   1 
ATOM   12280 C  CB  . GLN E  1 426 ? 9.622   50.305  41.179  1.00 23.68 ?  450  GLN E CB  1 
ATOM   12281 C  CG  . GLN E  1 426 ? 8.628   50.951  42.150  1.00 23.70 ?  450  GLN E CG  1 
ATOM   12282 C  CD  . GLN E  1 426 ? 7.869   49.950  42.998  1.00 24.56 ?  450  GLN E CD  1 
ATOM   12283 O  OE1 . GLN E  1 426 ? 7.699   48.787  42.618  1.00 24.34 ?  450  GLN E OE1 1 
ATOM   12284 N  NE2 . GLN E  1 426 ? 7.392   50.405  44.155  1.00 24.63 ?  450  GLN E NE2 1 
ATOM   12285 N  N   . LEU E  1 427 ? 11.253  50.494  38.055  1.00 23.42 ?  451  LEU E N   1 
ATOM   12286 C  CA  . LEU E  1 427 ? 12.450  50.164  37.281  1.00 23.48 ?  451  LEU E CA  1 
ATOM   12287 C  C   . LEU E  1 427 ? 13.108  51.417  36.706  1.00 23.44 ?  451  LEU E C   1 
ATOM   12288 O  O   . LEU E  1 427 ? 14.318  51.432  36.478  1.00 23.35 ?  451  LEU E O   1 
ATOM   12289 C  CB  . LEU E  1 427 ? 12.131  49.169  36.159  1.00 23.35 ?  451  LEU E CB  1 
ATOM   12290 C  CG  . LEU E  1 427 ? 11.659  47.765  36.555  1.00 23.83 ?  451  LEU E CG  1 
ATOM   12291 C  CD1 . LEU E  1 427 ? 10.911  47.106  35.398  1.00 24.04 ?  451  LEU E CD1 1 
ATOM   12292 C  CD2 . LEU E  1 427 ? 12.815  46.887  37.023  1.00 23.14 ?  451  LEU E CD2 1 
ATOM   12293 N  N   . PHE E  1 428 ? 12.310  52.464  36.487  1.00 23.27 ?  452  PHE E N   1 
ATOM   12294 C  CA  . PHE E  1 428 ? 12.803  53.703  35.878  1.00 23.23 ?  452  PHE E CA  1 
ATOM   12295 C  C   . PHE E  1 428 ? 12.738  54.927  36.794  1.00 23.29 ?  452  PHE E C   1 
ATOM   12296 O  O   . PHE E  1 428 ? 13.190  56.013  36.422  1.00 23.37 ?  452  PHE E O   1 
ATOM   12297 C  CB  . PHE E  1 428 ? 12.095  53.959  34.541  1.00 23.36 ?  452  PHE E CB  1 
ATOM   12298 C  CG  . PHE E  1 428 ? 12.612  53.100  33.428  1.00 23.12 ?  452  PHE E CG  1 
ATOM   12299 C  CD1 . PHE E  1 428 ? 13.647  53.547  32.613  1.00 23.11 ?  452  PHE E CD1 1 
ATOM   12300 C  CD2 . PHE E  1 428 ? 12.099  51.825  33.223  1.00 23.01 ?  452  PHE E CD2 1 
ATOM   12301 C  CE1 . PHE E  1 428 ? 14.152  52.744  31.594  1.00 23.00 ?  452  PHE E CE1 1 
ATOM   12302 C  CE2 . PHE E  1 428 ? 12.596  51.011  32.208  1.00 22.95 ?  452  PHE E CE2 1 
ATOM   12303 C  CZ  . PHE E  1 428 ? 13.625  51.472  31.392  1.00 22.76 ?  452  PHE E CZ  1 
ATOM   12304 N  N   . TRP E  1 429 ? 12.188  54.738  37.991  1.00 23.10 ?  453  TRP E N   1 
ATOM   12305 C  CA  . TRP E  1 429 ? 12.159  55.776  39.013  1.00 23.15 ?  453  TRP E CA  1 
ATOM   12306 C  C   . TRP E  1 429 ? 12.253  55.178  40.414  1.00 23.12 ?  453  TRP E C   1 
ATOM   12307 O  O   . TRP E  1 429 ? 11.579  54.195  40.723  1.00 23.09 ?  453  TRP E O   1 
ATOM   12308 C  CB  . TRP E  1 429 ? 10.884  56.618  38.895  1.00 23.20 ?  453  TRP E CB  1 
ATOM   12309 C  CG  . TRP E  1 429 ? 10.761  57.660  39.970  1.00 22.67 ?  453  TRP E CG  1 
ATOM   12310 C  CD1 . TRP E  1 429 ? 11.252  58.934  39.934  1.00 22.61 ?  453  TRP E CD1 1 
ATOM   12311 C  CD2 . TRP E  1 429 ? 10.113  57.514  41.240  1.00 21.73 ?  453  TRP E CD2 1 
ATOM   12312 N  NE1 . TRP E  1 429 ? 10.946  59.591  41.101  1.00 22.70 ?  453  TRP E NE1 1 
ATOM   12313 C  CE2 . TRP E  1 429 ? 10.247  58.743  41.920  1.00 22.08 ?  453  TRP E CE2 1 
ATOM   12314 C  CE3 . TRP E  1 429 ? 9.430   56.462  41.871  1.00 22.05 ?  453  TRP E CE3 1 
ATOM   12315 C  CZ2 . TRP E  1 429 ? 9.719   58.954  43.200  1.00 21.93 ?  453  TRP E CZ2 1 
ATOM   12316 C  CZ3 . TRP E  1 429 ? 8.908   56.673  43.146  1.00 21.23 ?  453  TRP E CZ3 1 
ATOM   12317 C  CH2 . TRP E  1 429 ? 9.058   57.908  43.794  1.00 21.16 ?  453  TRP E CH2 1 
ATOM   12318 N  N   . SER E  1 430 ? 13.085  55.789  41.254  1.00 23.06 ?  454  SER E N   1 
ATOM   12319 C  CA  . SER E  1 430 ? 13.191  55.415  42.666  1.00 23.00 ?  454  SER E CA  1 
ATOM   12320 C  C   . SER E  1 430 ? 13.542  56.615  43.541  1.00 23.08 ?  454  SER E C   1 
ATOM   12321 O  O   . SER E  1 430 ? 14.233  57.536  43.100  1.00 23.17 ?  454  SER E O   1 
ATOM   12322 C  CB  . SER E  1 430 ? 14.223  54.304  42.863  1.00 22.84 ?  454  SER E CB  1 
ATOM   12323 O  OG  . SER E  1 430 ? 15.491  54.690  42.362  1.00 22.81 ?  454  SER E OG  1 
ATOM   12324 N  N   . LYS E  1 431 ? 13.048  56.596  44.776  1.00 23.33 ?  455  LYS E N   1 
ATOM   12325 C  CA  . LYS E  1 431 ? 13.279  57.669  45.746  1.00 23.57 ?  455  LYS E CA  1 
ATOM   12326 C  C   . LYS E  1 431 ? 13.037  57.116  47.142  1.00 23.55 ?  455  LYS E C   1 
ATOM   12327 O  O   . LYS E  1 431 ? 12.052  56.412  47.373  1.00 23.66 ?  455  LYS E O   1 
ATOM   12328 C  CB  . LYS E  1 431 ? 12.357  58.862  45.481  1.00 23.66 ?  455  LYS E CB  1 
ATOM   12329 C  CG  . LYS E  1 431 ? 12.791  60.142  46.176  1.00 24.77 ?  455  LYS E CG  1 
ATOM   12330 C  CD  . LYS E  1 431 ? 11.703  61.199  46.145  1.00 25.76 ?  455  LYS E CD  1 
ATOM   12331 C  CE  . LYS E  1 431 ? 12.080  62.376  47.033  1.00 26.85 ?  455  LYS E CE  1 
ATOM   12332 N  NZ  . LYS E  1 431 ? 13.191  63.191  46.444  1.00 27.50 ?  455  LYS E NZ  1 
ATOM   12333 N  N   . GLY E  1 432 ? 13.941  57.431  48.066  1.00 23.67 ?  456  GLY E N   1 
ATOM   12334 C  CA  . GLY E  1 432 ? 13.915  56.842  49.403  1.00 23.63 ?  456  GLY E CA  1 
ATOM   12335 C  C   . GLY E  1 432 ? 13.841  55.331  49.293  1.00 23.46 ?  456  GLY E C   1 
ATOM   12336 O  O   . GLY E  1 432 ? 14.609  54.723  48.550  1.00 23.74 ?  456  GLY E O   1 
ATOM   12337 N  N   . ASN E  1 433 ? 12.895  54.733  50.008  1.00 23.30 ?  457  ASN E N   1 
ATOM   12338 C  CA  . ASN E  1 433 ? 12.673  53.293  49.951  1.00 23.17 ?  457  ASN E CA  1 
ATOM   12339 C  C   . ASN E  1 433 ? 11.484  52.910  49.064  1.00 23.13 ?  457  ASN E C   1 
ATOM   12340 O  O   . ASN E  1 433 ? 10.805  51.910  49.312  1.00 23.03 ?  457  ASN E O   1 
ATOM   12341 C  CB  . ASN E  1 433 ? 12.523  52.713  51.362  1.00 23.16 ?  457  ASN E CB  1 
ATOM   12342 C  CG  . ASN E  1 433 ? 13.749  52.955  52.229  1.00 23.17 ?  457  ASN E CG  1 
ATOM   12343 O  OD1 . ASN E  1 433 ? 13.658  53.572  53.294  1.00 23.24 ?  457  ASN E OD1 1 
ATOM   12344 N  ND2 . ASN E  1 433 ? 14.904  52.477  51.773  1.00 21.97 ?  457  ASN E ND2 1 
ATOM   12345 N  N   . ASN E  1 434 ? 11.236  53.714  48.031  1.00 23.06 ?  458  ASN E N   1 
ATOM   12346 C  CA  . ASN E  1 434 ? 10.294  53.337  46.978  1.00 23.18 ?  458  ASN E CA  1 
ATOM   12347 C  C   . ASN E  1 434 ? 11.030  53.129  45.655  1.00 22.99 ?  458  ASN E C   1 
ATOM   12348 O  O   . ASN E  1 434 ? 11.386  54.104  44.994  1.00 22.80 ?  458  ASN E O   1 
ATOM   12349 C  CB  . ASN E  1 434 ? 9.188   54.385  46.808  1.00 23.21 ?  458  ASN E CB  1 
ATOM   12350 C  CG  . ASN E  1 434 ? 8.064   53.910  45.891  1.00 23.73 ?  458  ASN E CG  1 
ATOM   12351 O  OD1 . ASN E  1 434 ? 7.964   52.725  45.564  1.00 23.93 ?  458  ASN E OD1 1 
ATOM   12352 N  ND2 . ASN E  1 434 ? 7.206   54.838  45.481  1.00 24.48 ?  458  ASN E ND2 1 
ATOM   12353 N  N   . PRO E  1 435 ? 11.258  51.859  45.264  1.00 23.06 ?  459  PRO E N   1 
ATOM   12354 C  CA  . PRO E  1 435 ? 10.861  50.638  45.977  1.00 23.28 ?  459  PRO E CA  1 
ATOM   12355 C  C   . PRO E  1 435 ? 11.853  50.230  47.063  1.00 23.47 ?  459  PRO E C   1 
ATOM   12356 O  O   . PRO E  1 435 ? 12.927  50.828  47.181  1.00 23.45 ?  459  PRO E O   1 
ATOM   12357 C  CB  . PRO E  1 435 ? 10.886  49.582  44.871  1.00 23.15 ?  459  PRO E CB  1 
ATOM   12358 C  CG  . PRO E  1 435 ? 11.999  50.026  43.983  1.00 23.01 ?  459  PRO E CG  1 
ATOM   12359 C  CD  . PRO E  1 435 ? 11.943  51.544  43.993  1.00 23.05 ?  459  PRO E CD  1 
ATOM   12360 N  N   . ALA E  1 436 ? 11.476  49.223  47.848  1.00 23.74 ?  460  ALA E N   1 
ATOM   12361 C  CA  . ALA E  1 436 ? 12.407  48.528  48.737  1.00 24.04 ?  460  ALA E CA  1 
ATOM   12362 C  C   . ALA E  1 436 ? 13.237  47.546  47.907  1.00 24.13 ?  460  ALA E C   1 
ATOM   12363 O  O   . ALA E  1 436 ? 12.850  47.205  46.786  1.00 24.10 ?  460  ALA E O   1 
ATOM   12364 C  CB  . ALA E  1 436 ? 11.646  47.794  49.827  1.00 24.06 ?  460  ALA E CB  1 
ATOM   12365 N  N   . SER E  1 437 ? 14.369  47.102  48.452  1.00 24.04 ?  461  SER E N   1 
ATOM   12366 C  CA  . SER E  1 437 ? 15.263  46.175  47.748  1.00 24.15 ?  461  SER E CA  1 
ATOM   12367 C  C   . SER E  1 437 ? 14.581  44.856  47.383  1.00 24.25 ?  461  SER E C   1 
ATOM   12368 O  O   . SER E  1 437 ? 14.640  44.421  46.229  1.00 24.11 ?  461  SER E O   1 
ATOM   12369 C  CB  . SER E  1 437 ? 16.527  45.905  48.567  1.00 24.14 ?  461  SER E CB  1 
ATOM   12370 O  OG  . SER E  1 437 ? 17.490  45.203  47.798  1.00 23.67 ?  461  SER E OG  1 
ATOM   12371 N  N   . LEU E  1 438 ? 13.931  44.237  48.368  1.00 24.26 ?  462  LEU E N   1 
ATOM   12372 C  CA  . LEU E  1 438 ? 13.179  42.996  48.160  1.00 24.37 ?  462  LEU E CA  1 
ATOM   12373 C  C   . LEU E  1 438 ? 12.145  43.120  47.045  1.00 24.03 ?  462  LEU E C   1 
ATOM   12374 O  O   . LEU E  1 438 ? 11.965  42.200  46.242  1.00 23.69 ?  462  LEU E O   1 
ATOM   12375 C  CB  . LEU E  1 438 ? 12.468  42.582  49.449  1.00 24.52 ?  462  LEU E CB  1 
ATOM   12376 C  CG  . LEU E  1 438 ? 13.126  41.556  50.365  1.00 25.53 ?  462  LEU E CG  1 
ATOM   12377 C  CD1 . LEU E  1 438 ? 12.399  41.531  51.715  1.00 27.07 ?  462  LEU E CD1 1 
ATOM   12378 C  CD2 . LEU E  1 438 ? 13.141  40.169  49.735  1.00 24.71 ?  462  LEU E CD2 1 
ATOM   12379 N  N   . GLU E  1 439 ? 11.461  44.261  47.026  1.00 23.77 ?  463  GLU E N   1 
ATOM   12380 C  CA  . GLU E  1 439 ? 10.433  44.558  46.040  1.00 23.54 ?  463  GLU E CA  1 
ATOM   12381 C  C   . GLU E  1 439 ? 11.026  44.637  44.630  1.00 23.47 ?  463  GLU E C   1 
ATOM   12382 O  O   . GLU E  1 439 ? 10.508  44.013  43.706  1.00 23.36 ?  463  GLU E O   1 
ATOM   12383 C  CB  . GLU E  1 439 ? 9.726   45.863  46.414  1.00 23.63 ?  463  GLU E CB  1 
ATOM   12384 C  CG  . GLU E  1 439 ? 8.611   46.297  45.476  1.00 23.62 ?  463  GLU E CG  1 
ATOM   12385 C  CD  . GLU E  1 439 ? 7.942   47.580  45.937  1.00 24.42 ?  463  GLU E CD  1 
ATOM   12386 O  OE1 . GLU E  1 439 ? 8.507   48.272  46.813  1.00 24.20 ?  463  GLU E OE1 1 
ATOM   12387 O  OE2 . GLU E  1 439 ? 6.851   47.898  45.424  1.00 23.95 -1 463  GLU E OE2 1 
ATOM   12388 N  N   . LEU E  1 440 ? 12.113  45.395  44.477  1.00 23.03 ?  464  LEU E N   1 
ATOM   12389 C  CA  . LEU E  1 440 ? 12.810  45.486  43.194  1.00 23.10 ?  464  LEU E CA  1 
ATOM   12390 C  C   . LEU E  1 440 ? 13.317  44.116  42.743  1.00 22.79 ?  464  LEU E C   1 
ATOM   12391 O  O   . LEU E  1 440 ? 13.194  43.754  41.570  1.00 22.95 ?  464  LEU E O   1 
ATOM   12392 C  CB  . LEU E  1 440 ? 13.992  46.455  43.289  1.00 23.11 ?  464  LEU E CB  1 
ATOM   12393 C  CG  . LEU E  1 440 ? 14.370  47.367  42.108  1.00 23.52 ?  464  LEU E CG  1 
ATOM   12394 C  CD1 . LEU E  1 440 ? 15.885  47.495  42.027  1.00 22.46 ?  464  LEU E CD1 1 
ATOM   12395 C  CD2 . LEU E  1 440 ? 13.804  46.948  40.758  1.00 22.84 ?  464  LEU E CD2 1 
ATOM   12396 N  N   . LYS E  1 441 ? 13.874  43.364  43.690  1.00 22.42 ?  465  LYS E N   1 
ATOM   12397 C  CA  . LYS E  1 441 ? 14.461  42.055  43.425  1.00 22.38 ?  465  LYS E CA  1 
ATOM   12398 C  C   . LYS E  1 441 ? 13.454  41.051  42.856  1.00 22.31 ?  465  LYS E C   1 
ATOM   12399 O  O   . LYS E  1 441 ? 13.750  40.365  41.875  1.00 22.07 ?  465  LYS E O   1 
ATOM   12400 C  CB  . LYS E  1 441 ? 15.130  41.500  44.685  1.00 22.35 ?  465  LYS E CB  1 
ATOM   12401 C  CG  . LYS E  1 441 ? 16.058  40.309  44.428  1.00 23.07 ?  465  LYS E CG  1 
ATOM   12402 C  CD  . LYS E  1 441 ? 16.689  39.782  45.712  1.00 23.21 ?  465  LYS E CD  1 
ATOM   12403 C  CE  . LYS E  1 441 ? 18.053  40.404  45.981  1.00 24.43 ?  465  LYS E CE  1 
ATOM   12404 N  NZ  . LYS E  1 441 ? 17.979  41.770  46.549  1.00 26.28 ?  465  LYS E NZ  1 
ATOM   12405 N  N   . VAL E  1 442 ? 12.270  40.970  43.463  1.00 22.15 ?  466  VAL E N   1 
ATOM   12406 C  CA  . VAL E  1 442 ? 11.243  40.058  42.961  1.00 22.28 ?  466  VAL E CA  1 
ATOM   12407 C  C   . VAL E  1 442 ? 10.596  40.562  41.661  1.00 22.31 ?  466  VAL E C   1 
ATOM   12408 O  O   . VAL E  1 442 ? 10.137  39.765  40.845  1.00 22.40 ?  466  VAL E O   1 
ATOM   12409 C  CB  . VAL E  1 442 ? 10.194  39.688  44.039  1.00 22.20 ?  466  VAL E CB  1 
ATOM   12410 C  CG1 . VAL E  1 442 ? 9.142   40.795  44.216  1.00 22.12 ?  466  VAL E CG1 1 
ATOM   12411 C  CG2 . VAL E  1 442 ? 9.553   38.351  43.705  1.00 22.13 ?  466  VAL E CG2 1 
ATOM   12412 N  N   . LEU E  1 443 ? 10.583  41.881  41.478  1.00 22.39 ?  467  LEU E N   1 
ATOM   12413 C  CA  . LEU E  1 443 ? 10.103  42.497  40.245  1.00 22.52 ?  467  LEU E CA  1 
ATOM   12414 C  C   . LEU E  1 443 ? 11.033  42.106  39.098  1.00 22.36 ?  467  LEU E C   1 
ATOM   12415 O  O   . LEU E  1 443 ? 10.577  41.642  38.050  1.00 22.44 ?  467  LEU E O   1 
ATOM   12416 C  CB  . LEU E  1 443 ? 10.070  44.025  40.395  1.00 22.66 ?  467  LEU E CB  1 
ATOM   12417 C  CG  . LEU E  1 443 ? 9.184   44.936  39.528  1.00 23.56 ?  467  LEU E CG  1 
ATOM   12418 C  CD1 . LEU E  1 443 ? 9.607   46.389  39.719  1.00 23.36 ?  467  LEU E CD1 1 
ATOM   12419 C  CD2 . LEU E  1 443 ? 9.184   44.585  38.043  1.00 24.95 ?  467  LEU E CD2 1 
ATOM   12420 N  N   . GLU E  1 444 ? 12.336  42.285  39.314  1.00 22.09 ?  468  GLU E N   1 
ATOM   12421 C  CA  . GLU E  1 444 ? 13.353  41.941  38.319  1.00 22.02 ?  468  GLU E CA  1 
ATOM   12422 C  C   . GLU E  1 444 ? 13.440  40.442  38.076  1.00 21.86 ?  468  GLU E C   1 
ATOM   12423 O  O   . GLU E  1 444 ? 13.788  40.008  36.973  1.00 21.86 ?  468  GLU E O   1 
ATOM   12424 C  CB  . GLU E  1 444 ? 14.716  42.518  38.711  1.00 21.98 ?  468  GLU E CB  1 
ATOM   12425 C  CG  . GLU E  1 444 ? 14.783  44.033  38.528  1.00 22.73 ?  468  GLU E CG  1 
ATOM   12426 C  CD  . GLU E  1 444 ? 16.070  44.665  39.037  1.00 23.89 ?  468  GLU E CD  1 
ATOM   12427 O  OE1 . GLU E  1 444 ? 16.794  44.036  39.844  1.00 24.47 ?  468  GLU E OE1 1 
ATOM   12428 O  OE2 . GLU E  1 444 ? 16.348  45.815  38.631  1.00 24.67 -1 468  GLU E OE2 1 
ATOM   12429 N  N   . MET E  1 445 ? 13.101  39.656  39.096  1.00 21.56 ?  469  MET E N   1 
ATOM   12430 C  CA  . MET E  1 445 ? 13.029  38.202  38.960  1.00 21.67 ?  469  MET E CA  1 
ATOM   12431 C  C   . MET E  1 445 ? 12.044  37.803  37.853  1.00 21.62 ?  469  MET E C   1 
ATOM   12432 O  O   . MET E  1 445 ? 12.330  36.911  37.050  1.00 21.25 ?  469  MET E O   1 
ATOM   12433 C  CB  . MET E  1 445 ? 12.644  37.551  40.292  1.00 21.50 ?  469  MET E CB  1 
ATOM   12434 C  CG  . MET E  1 445 ? 12.822  36.051  40.322  1.00 21.61 ?  469  MET E CG  1 
ATOM   12435 S  SD  . MET E  1 445 ? 12.171  35.318  41.833  1.00 22.22 ?  469  MET E SD  1 
ATOM   12436 C  CE  . MET E  1 445 ? 12.475  33.584  41.511  1.00 20.73 ?  469  MET E CE  1 
ATOM   12437 N  N   . ALA E  1 446 ? 10.894  38.477  37.811  1.00 21.65 ?  470  ALA E N   1 
ATOM   12438 C  CA  . ALA E  1 446 ? 9.892   38.214  36.774  1.00 21.77 ?  470  ALA E CA  1 
ATOM   12439 C  C   . ALA E  1 446 ? 10.211  38.970  35.492  1.00 21.61 ?  470  ALA E C   1 
ATOM   12440 O  O   . ALA E  1 446 ? 10.298  38.374  34.421  1.00 21.54 ?  470  ALA E O   1 
ATOM   12441 C  CB  . ALA E  1 446 ? 8.502   38.573  37.264  1.00 21.49 ?  470  ALA E CB  1 
ATOM   12442 N  N   . GLU E  1 447 ? 10.390  40.283  35.630  1.00 21.65 ?  471  GLU E N   1 
ATOM   12443 C  CA  . GLU E  1 447 ? 10.549  41.203  34.509  1.00 21.85 ?  471  GLU E CA  1 
ATOM   12444 C  C   . GLU E  1 447 ? 11.772  40.888  33.659  1.00 21.77 ?  471  GLU E C   1 
ATOM   12445 O  O   . GLU E  1 447 ? 11.705  40.928  32.428  1.00 21.71 ?  471  GLU E O   1 
ATOM   12446 C  CB  . GLU E  1 447 ? 10.627  42.645  35.026  1.00 21.99 ?  471  GLU E CB  1 
ATOM   12447 C  CG  . GLU E  1 447 ? 10.597  43.720  33.951  1.00 23.20 ?  471  GLU E CG  1 
ATOM   12448 C  CD  . GLU E  1 447 ? 9.195   44.019  33.418  1.00 24.79 ?  471  GLU E CD  1 
ATOM   12449 O  OE1 . GLU E  1 447 ? 8.216   43.385  33.871  1.00 25.97 ?  471  GLU E OE1 1 
ATOM   12450 O  OE2 . GLU E  1 447 ? 9.075   44.900  32.539  1.00 24.07 -1 471  GLU E OE2 1 
ATOM   12451 N  N   . ASN E  1 448 ? 12.880  40.576  34.325  1.00 21.62 ?  472  ASN E N   1 
ATOM   12452 C  CA  . ASN E  1 448 ? 14.144  40.332  33.651  1.00 21.69 ?  472  ASN E CA  1 
ATOM   12453 C  C   . ASN E  1 448 ? 14.446  38.851  33.472  1.00 21.70 ?  472  ASN E C   1 
ATOM   12454 O  O   . ASN E  1 448 ? 14.544  38.363  32.350  1.00 21.93 ?  472  ASN E O   1 
ATOM   12455 C  CB  . ASN E  1 448 ? 15.297  41.011  34.402  1.00 21.47 ?  472  ASN E CB  1 
ATOM   12456 C  CG  . ASN E  1 448 ? 15.147  42.519  34.468  1.00 21.80 ?  472  ASN E CG  1 
ATOM   12457 O  OD1 . ASN E  1 448 ? 14.353  43.117  33.730  1.00 20.45 ?  472  ASN E OD1 1 
ATOM   12458 N  ND2 . ASN E  1 448 ? 15.916  43.147  35.356  1.00 21.17 ?  472  ASN E ND2 1 
ATOM   12459 N  N   . ASN E  1 449 ? 14.578  38.139  34.585  1.00 21.54 ?  473  ASN E N   1 
ATOM   12460 C  CA  . ASN E  1 449 ? 15.146  36.799  34.563  1.00 21.57 ?  473  ASN E CA  1 
ATOM   12461 C  C   . ASN E  1 449 ? 14.197  35.685  34.106  1.00 21.44 ?  473  ASN E C   1 
ATOM   12462 O  O   . ASN E  1 449 ? 14.631  34.734  33.452  1.00 21.38 ?  473  ASN E O   1 
ATOM   12463 C  CB  . ASN E  1 449 ? 15.813  36.496  35.909  1.00 21.57 ?  473  ASN E CB  1 
ATOM   12464 C  CG  . ASN E  1 449 ? 16.934  37.481  36.230  1.00 21.92 ?  473  ASN E CG  1 
ATOM   12465 O  OD1 . ASN E  1 449 ? 16.875  38.212  37.222  1.00 23.62 ?  473  ASN E OD1 1 
ATOM   12466 N  ND2 . ASN E  1 449 ? 17.948  37.522  35.374  1.00 20.79 ?  473  ASN E ND2 1 
ATOM   12467 N  N   . LEU E  1 450 ? 12.912  35.812  34.431  1.00 21.25 ?  474  LEU E N   1 
ATOM   12468 C  CA  . LEU E  1 450 ? 11.894  34.896  33.911  1.00 21.11 ?  474  LEU E CA  1 
ATOM   12469 C  C   . LEU E  1 450 ? 11.665  35.151  32.422  1.00 20.77 ?  474  LEU E C   1 
ATOM   12470 O  O   . LEU E  1 450 ? 11.555  34.208  31.637  1.00 20.52 ?  474  LEU E O   1 
ATOM   12471 C  CB  . LEU E  1 450 ? 10.570  35.058  34.660  1.00 21.15 ?  474  LEU E CB  1 
ATOM   12472 C  CG  . LEU E  1 450 ? 9.646   33.863  34.944  1.00 21.81 ?  474  LEU E CG  1 
ATOM   12473 C  CD1 . LEU E  1 450 ? 8.216   34.368  35.088  1.00 20.87 ?  474  LEU E CD1 1 
ATOM   12474 C  CD2 . LEU E  1 450 ? 9.714   32.717  33.924  1.00 20.21 ?  474  LEU E CD2 1 
ATOM   12475 N  N   . ALA E  1 451 ? 11.585  36.424  32.041  1.00 20.67 ?  475  ALA E N   1 
ATOM   12476 C  CA  . ALA E  1 451 ? 11.416  36.793  30.632  1.00 20.57 ?  475  ALA E CA  1 
ATOM   12477 C  C   . ALA E  1 451 ? 12.556  36.228  29.781  1.00 20.46 ?  475  ALA E C   1 
ATOM   12478 O  O   . ALA E  1 451 ? 12.305  35.600  28.756  1.00 20.36 ?  475  ALA E O   1 
ATOM   12479 C  CB  . ALA E  1 451 ? 11.322  38.301  30.476  1.00 20.41 ?  475  ALA E CB  1 
ATOM   12480 N  N   . LYS E  1 452 ? 13.795  36.437  30.231  1.00 20.37 ?  476  LYS E N   1 
ATOM   12481 C  CA  . LYS E  1 452 ? 14.988  35.896  29.565  1.00 20.40 ?  476  LYS E CA  1 
ATOM   12482 C  C   . LYS E  1 452 ? 15.033  34.367  29.581  1.00 20.39 ?  476  LYS E C   1 
ATOM   12483 O  O   . LYS E  1 452 ? 15.545  33.751  28.646  1.00 20.50 ?  476  LYS E O   1 
ATOM   12484 C  CB  . LYS E  1 452 ? 16.276  36.465  30.182  1.00 20.22 ?  476  LYS E CB  1 
ATOM   12485 C  CG  . LYS E  1 452 ? 16.557  37.929  29.828  1.00 20.56 ?  476  LYS E CG  1 
ATOM   12486 C  CD  . LYS E  1 452 ? 17.986  38.352  30.183  1.00 20.52 ?  476  LYS E CD  1 
ATOM   12487 C  CE  . LYS E  1 452 ? 18.151  38.625  31.674  1.00 20.72 ?  476  LYS E CE  1 
ATOM   12488 N  NZ  . LYS E  1 452 ? 19.496  39.180  31.984  1.00 21.15 ?  476  LYS E NZ  1 
ATOM   12489 N  N   . MET E  1 453 ? 14.506  33.756  30.640  1.00 20.37 ?  477  MET E N   1 
ATOM   12490 C  CA  . MET E  1 453 ? 14.375  32.302  30.670  1.00 20.25 ?  477  MET E CA  1 
ATOM   12491 C  C   . MET E  1 453 ? 13.499  31.826  29.518  1.00 20.19 ?  477  MET E C   1 
ATOM   12492 O  O   . MET E  1 453 ? 13.881  30.909  28.783  1.00 20.14 ?  477  MET E O   1 
ATOM   12493 C  CB  . MET E  1 453 ? 13.808  31.803  31.999  1.00 20.34 ?  477  MET E CB  1 
ATOM   12494 C  CG  . MET E  1 453 ? 13.801  30.285  32.098  1.00 20.48 ?  477  MET E CG  1 
ATOM   12495 S  SD  . MET E  1 453 ? 13.249  29.686  33.697  1.00 21.03 ?  477  MET E SD  1 
ATOM   12496 C  CE  . MET E  1 453 ? 13.266  27.920  33.422  1.00 19.82 ?  477  MET E CE  1 
ATOM   12497 N  N   . HIS E  1 454 ? 12.335  32.453  29.355  1.00 19.97 ?  478  HIS E N   1 
ATOM   12498 C  CA  . HIS E  1 454 ? 11.446  32.082  28.260  1.00 20.07 ?  478  HIS E CA  1 
ATOM   12499 C  C   . HIS E  1 454 ? 12.079  32.299  26.883  1.00 19.92 ?  478  HIS E C   1 
ATOM   12500 O  O   . HIS E  1 454 ? 11.977  31.430  26.013  1.00 20.17 ?  478  HIS E O   1 
ATOM   12501 C  CB  . HIS E  1 454 ? 10.092  32.798  28.318  1.00 19.97 ?  478  HIS E CB  1 
ATOM   12502 C  CG  . HIS E  1 454 ? 9.310   32.648  27.050  1.00 19.86 ?  478  HIS E CG  1 
ATOM   12503 N  ND1 . HIS E  1 454 ? 8.710   31.462  26.689  1.00 20.21 ?  478  HIS E ND1 1 
ATOM   12504 C  CD2 . HIS E  1 454 ? 9.102   33.503  26.023  1.00 20.04 ?  478  HIS E CD2 1 
ATOM   12505 C  CE1 . HIS E  1 454 ? 8.136   31.602  25.507  1.00 19.49 ?  478  HIS E CE1 1 
ATOM   12506 N  NE2 . HIS E  1 454 ? 8.360   32.831  25.080  1.00 20.38 ?  478  HIS E NE2 1 
ATOM   12507 N  N   . VAL E  1 455 ? 12.707  33.462  26.693  1.00 19.60 ?  479  VAL E N   1 
ATOM   12508 C  CA  . VAL E  1 455 ? 13.421  33.792  25.449  1.00 19.61 ?  479  VAL E CA  1 
ATOM   12509 C  C   . VAL E  1 455 ? 14.483  32.741  25.126  1.00 19.83 ?  479  VAL E C   1 
ATOM   12510 O  O   . VAL E  1 455 ? 14.600  32.296  23.982  1.00 20.20 ?  479  VAL E O   1 
ATOM   12511 C  CB  . VAL E  1 455 ? 14.086  35.199  25.513  1.00 19.50 ?  479  VAL E CB  1 
ATOM   12512 C  CG1 . VAL E  1 455 ? 14.868  35.492  24.241  1.00 19.21 ?  479  VAL E CG1 1 
ATOM   12513 C  CG2 . VAL E  1 455 ? 13.044  36.275  25.743  1.00 19.06 ?  479  VAL E CG2 1 
ATOM   12514 N  N   . GLY E  1 456 ? 15.250  32.349  26.140  1.00 20.01 ?  480  GLY E N   1 
ATOM   12515 C  CA  . GLY E  1 456 ? 16.240  31.279  25.998  1.00 20.32 ?  480  GLY E CA  1 
ATOM   12516 C  C   . GLY E  1 456 ? 15.614  29.983  25.517  1.00 20.29 ?  480  GLY E C   1 
ATOM   12517 O  O   . GLY E  1 456 ? 16.134  29.334  24.609  1.00 20.34 ?  480  GLY E O   1 
ATOM   12518 N  N   . LEU E  1 457 ? 14.486  29.618  26.124  1.00 20.26 ?  481  LEU E N   1 
ATOM   12519 C  CA  . LEU E  1 457 ? 13.736  28.422  25.731  1.00 20.04 ?  481  LEU E CA  1 
ATOM   12520 C  C   . LEU E  1 457 ? 13.182  28.530  24.312  1.00 19.98 ?  481  LEU E C   1 
ATOM   12521 O  O   . LEU E  1 457 ? 13.279  27.586  23.535  1.00 20.26 ?  481  LEU E O   1 
ATOM   12522 C  CB  . LEU E  1 457 ? 12.600  28.146  26.723  1.00 19.75 ?  481  LEU E CB  1 
ATOM   12523 C  CG  . LEU E  1 457 ? 13.004  27.531  28.068  1.00 19.62 ?  481  LEU E CG  1 
ATOM   12524 C  CD1 . LEU E  1 457 ? 12.025  27.929  29.164  1.00 18.41 ?  481  LEU E CD1 1 
ATOM   12525 C  CD2 . LEU E  1 457 ? 13.124  26.015  27.967  1.00 18.10 ?  481  LEU E CD2 1 
ATOM   12526 N  N   . ALA E  1 458 ? 12.613  29.683  23.982  1.00 19.98 ?  482  ALA E N   1 
ATOM   12527 C  CA  . ALA E  1 458 ? 11.988  29.895  22.676  1.00 20.34 ?  482  ALA E CA  1 
ATOM   12528 C  C   . ALA E  1 458 ? 13.008  29.888  21.542  1.00 20.38 ?  482  ALA E C   1 
ATOM   12529 O  O   . ALA E  1 458 ? 12.710  29.451  20.427  1.00 20.52 ?  482  ALA E O   1 
ATOM   12530 C  CB  . ALA E  1 458 ? 11.191  31.197  22.671  1.00 20.10 ?  482  ALA E CB  1 
ATOM   12531 N  N   . HIS E  1 459 ? 14.217  30.355  21.835  1.00 20.36 ?  483  HIS E N   1 
ATOM   12532 C  CA  . HIS E  1 459 ? 15.231  30.503  20.795  1.00 20.56 ?  483  HIS E CA  1 
ATOM   12533 C  C   . HIS E  1 459 ? 16.373  29.477  20.864  1.00 20.56 ?  483  HIS E C   1 
ATOM   12534 O  O   . HIS E  1 459 ? 17.372  29.597  20.158  1.00 20.82 ?  483  HIS E O   1 
ATOM   12535 C  CB  . HIS E  1 459 ? 15.671  31.970  20.698  1.00 20.24 ?  483  HIS E CB  1 
ATOM   12536 C  CG  . HIS E  1 459 ? 14.534  32.886  20.358  1.00 20.49 ?  483  HIS E CG  1 
ATOM   12537 N  ND1 . HIS E  1 459 ? 13.700  33.431  21.312  1.00 20.42 ?  483  HIS E ND1 1 
ATOM   12538 C  CD2 . HIS E  1 459 ? 14.045  33.288  19.161  1.00 19.58 ?  483  HIS E CD2 1 
ATOM   12539 C  CE1 . HIS E  1 459 ? 12.770  34.158  20.716  1.00 20.28 ?  483  HIS E CE1 1 
ATOM   12540 N  NE2 . HIS E  1 459 ? 12.953  34.085  19.409  1.00 19.50 ?  483  HIS E NE2 1 
ATOM   12541 N  N   . VAL E  1 460 ? 16.171  28.449  21.691  1.00 20.66 ?  484  VAL E N   1 
ATOM   12542 C  CA  . VAL E  1 460 ? 17.005  27.227  21.728  1.00 20.47 ?  484  VAL E CA  1 
ATOM   12543 C  C   . VAL E  1 460 ? 18.462  27.462  22.170  1.00 20.51 ?  484  VAL E C   1 
ATOM   12544 O  O   . VAL E  1 460 ? 19.414  26.976  21.550  1.00 20.32 ?  484  VAL E O   1 
ATOM   12545 C  CB  . VAL E  1 460 ? 16.936  26.403  20.397  1.00 20.60 ?  484  VAL E CB  1 
ATOM   12546 C  CG1 . VAL E  1 460 ? 17.313  24.943  20.657  1.00 20.15 ?  484  VAL E CG1 1 
ATOM   12547 C  CG2 . VAL E  1 460 ? 15.539  26.466  19.766  1.00 20.33 ?  484  VAL E CG2 1 
ATOM   12548 N  N   . ASN E  1 461 ? 18.622  28.207  23.257  1.00 20.35 ?  485  ASN E N   1 
ATOM   12549 C  CA  . ASN E  1 461 ? 19.935  28.421  23.837  1.00 20.14 ?  485  ASN E CA  1 
ATOM   12550 C  C   . ASN E  1 461 ? 19.986  27.821  25.237  1.00 20.05 ?  485  ASN E C   1 
ATOM   12551 O  O   . ASN E  1 461 ? 19.585  28.480  26.195  1.00 19.93 ?  485  ASN E O   1 
ATOM   12552 C  CB  . ASN E  1 461 ? 20.284  29.912  23.870  1.00 20.27 ?  485  ASN E CB  1 
ATOM   12553 C  CG  . ASN E  1 461 ? 21.688  30.167  24.382  1.00 20.31 ?  485  ASN E CG  1 
ATOM   12554 O  OD1 . ASN E  1 461 ? 22.628  29.451  24.027  1.00 19.87 ?  485  ASN E OD1 1 
ATOM   12555 N  ND2 . ASN E  1 461 ? 21.836  31.181  25.229  1.00 19.12 ?  485  ASN E ND2 1 
ATOM   12556 N  N   . PRO E  1 462 ? 20.477  26.566  25.355  1.00 19.74 ?  486  PRO E N   1 
ATOM   12557 C  CA  . PRO E  1 462 ? 20.468  25.816  26.618  1.00 19.68 ?  486  PRO E CA  1 
ATOM   12558 C  C   . PRO E  1 462 ? 20.977  26.600  27.827  1.00 19.46 ?  486  PRO E C   1 
ATOM   12559 O  O   . PRO E  1 462 ? 20.334  26.582  28.873  1.00 19.35 ?  486  PRO E O   1 
ATOM   12560 C  CB  . PRO E  1 462 ? 21.380  24.619  26.328  1.00 19.60 ?  486  PRO E CB  1 
ATOM   12561 C  CG  . PRO E  1 462 ? 21.277  24.428  24.849  1.00 19.77 ?  486  PRO E CG  1 
ATOM   12562 C  CD  . PRO E  1 462 ? 21.152  25.813  24.281  1.00 19.73 ?  486  PRO E CD  1 
ATOM   12563 N  N   . GLY E  1 463 ? 22.109  27.287  27.682  1.00 19.43 ?  487  GLY E N   1 
ATOM   12564 C  CA  . GLY E  1 463 ? 22.662  28.096  28.772  1.00 19.42 ?  487  GLY E CA  1 
ATOM   12565 C  C   . GLY E  1 463 ? 21.764  29.260  29.159  1.00 19.55 ?  487  GLY E C   1 
ATOM   12566 O  O   . GLY E  1 463 ? 21.787  29.721  30.304  1.00 19.69 ?  487  GLY E O   1 
ATOM   12567 N  N   . GLY E  1 464 ? 20.960  29.715  28.199  1.00 19.58 ?  488  GLY E N   1 
ATOM   12568 C  CA  . GLY E  1 464 ? 20.076  30.864  28.363  1.00 19.80 ?  488  GLY E CA  1 
ATOM   12569 C  C   . GLY E  1 464 ? 18.788  30.611  29.119  1.00 20.18 ?  488  GLY E C   1 
ATOM   12570 O  O   . GLY E  1 464 ? 18.000  31.537  29.323  1.00 20.14 ?  488  GLY E O   1 
ATOM   12571 N  N   . TRP E  1 465 ? 18.553  29.363  29.523  1.00 20.17 ?  489  TRP E N   1 
ATOM   12572 C  CA  . TRP E  1 465 ? 17.474  29.086  30.468  1.00 20.37 ?  489  TRP E CA  1 
ATOM   12573 C  C   . TRP E  1 465 ? 17.930  28.271  31.682  1.00 20.59 ?  489  TRP E C   1 
ATOM   12574 O  O   . TRP E  1 465 ? 17.144  28.032  32.606  1.00 20.27 ?  489  TRP E O   1 
ATOM   12575 C  CB  . TRP E  1 465 ? 16.243  28.485  29.776  1.00 20.12 ?  489  TRP E CB  1 
ATOM   12576 C  CG  . TRP E  1 465 ? 16.270  27.005  29.474  1.00 20.17 ?  489  TRP E CG  1 
ATOM   12577 C  CD1 . TRP E  1 465 ? 16.000  25.983  30.343  1.00 19.29 ?  489  TRP E CD1 1 
ATOM   12578 C  CD2 . TRP E  1 465 ? 16.514  26.393  28.200  1.00 19.60 ?  489  TRP E CD2 1 
ATOM   12579 N  NE1 . TRP E  1 465 ? 16.088  24.774  29.695  1.00 20.00 ?  489  TRP E NE1 1 
ATOM   12580 C  CE2 . TRP E  1 465 ? 16.400  24.996  28.379  1.00 19.88 ?  489  TRP E CE2 1 
ATOM   12581 C  CE3 . TRP E  1 465 ? 16.825  26.890  26.926  1.00 19.71 ?  489  TRP E CE3 1 
ATOM   12582 C  CZ2 . TRP E  1 465 ? 16.578  24.088  27.329  1.00 19.76 ?  489  TRP E CZ2 1 
ATOM   12583 C  CZ3 . TRP E  1 465 ? 17.007  25.986  25.881  1.00 19.42 ?  489  TRP E CZ3 1 
ATOM   12584 C  CH2 . TRP E  1 465 ? 16.889  24.601  26.092  1.00 19.88 ?  489  TRP E CH2 1 
ATOM   12585 N  N   . THR E  1 466 ? 19.209  27.885  31.682  1.00 20.72 ?  490  THR E N   1 
ATOM   12586 C  CA  . THR E  1 466 ? 19.774  27.049  32.742  1.00 20.96 ?  490  THR E CA  1 
ATOM   12587 C  C   . THR E  1 466 ? 20.788  27.785  33.633  1.00 21.05 ?  490  THR E C   1 
ATOM   12588 O  O   . THR E  1 466 ? 20.392  28.419  34.612  1.00 21.23 ?  490  THR E O   1 
ATOM   12589 C  CB  . THR E  1 466 ? 20.391  25.737  32.181  1.00 20.96 ?  490  THR E CB  1 
ATOM   12590 O  OG1 . THR E  1 466 ? 21.372  26.054  31.190  1.00 20.88 ?  490  THR E OG1 1 
ATOM   12591 C  CG2 . THR E  1 466 ? 19.314  24.848  31.560  1.00 20.69 ?  490  THR E CG2 1 
ATOM   12592 N  N   . TYR E  1 467 ? 22.078  27.703  33.291  1.00 21.07 ?  491  TYR E N   1 
ATOM   12593 C  CA  . TYR E  1 467 ? 23.165  28.241  34.131  1.00 21.03 ?  491  TYR E CA  1 
ATOM   12594 C  C   . TYR E  1 467 ? 23.243  29.759  34.152  1.00 20.85 ?  491  TYR E C   1 
ATOM   12595 O  O   . TYR E  1 467 ? 23.393  30.368  35.215  1.00 20.81 ?  491  TYR E O   1 
ATOM   12596 C  CB  . TYR E  1 467 ? 24.538  27.742  33.654  1.00 21.04 ?  491  TYR E CB  1 
ATOM   12597 C  CG  . TYR E  1 467 ? 24.883  26.316  34.008  1.00 21.59 ?  491  TYR E CG  1 
ATOM   12598 C  CD1 . TYR E  1 467 ? 25.527  25.998  35.208  1.00 21.69 ?  491  TYR E CD1 1 
ATOM   12599 C  CD2 . TYR E  1 467 ? 24.598  25.288  33.126  1.00 21.33 ?  491  TYR E CD2 1 
ATOM   12600 C  CE1 . TYR E  1 467 ? 25.858  24.671  35.516  1.00 22.10 ?  491  TYR E CE1 1 
ATOM   12601 C  CE2 . TYR E  1 467 ? 24.917  23.980  33.423  1.00 22.01 ?  491  TYR E CE2 1 
ATOM   12602 C  CZ  . TYR E  1 467 ? 25.538  23.669  34.611  1.00 22.18 ?  491  TYR E CZ  1 
ATOM   12603 O  OH  . TYR E  1 467 ? 25.835  22.348  34.863  1.00 23.98 ?  491  TYR E OH  1 
ATOM   12604 N  N   . THR E  1 468 ? 23.164  30.352  32.964  1.00 20.68 ?  492  THR E N   1 
ATOM   12605 C  CA  . THR E  1 468 ? 23.620  31.726  32.731  1.00 20.56 ?  492  THR E CA  1 
ATOM   12606 C  C   . THR E  1 468 ? 22.487  32.734  32.755  1.00 20.49 ?  492  THR E C   1 
ATOM   12607 O  O   . THR E  1 468 ? 22.623  33.806  33.330  1.00 20.45 ?  492  THR E O   1 
ATOM   12608 C  CB  . THR E  1 468 ? 24.396  31.809  31.395  1.00 20.40 ?  492  THR E CB  1 
ATOM   12609 O  OG1 . THR E  1 468 ? 25.469  30.867  31.439  1.00 20.38 ?  492  THR E OG1 1 
ATOM   12610 C  CG2 . THR E  1 468 ? 24.971  33.215  31.152  1.00 19.77 ?  492  THR E CG2 1 
ATOM   12611 N  N   . GLU E  1 469 ? 21.383  32.392  32.104  1.00 20.92 ?  493  GLU E N   1 
ATOM   12612 C  CA  . GLU E  1 469 ? 20.161  33.177  32.196  1.00 21.33 ?  493  GLU E CA  1 
ATOM   12613 C  C   . GLU E  1 469 ? 19.040  32.239  32.609  1.00 21.48 ?  493  GLU E C   1 
ATOM   12614 O  O   . GLU E  1 469 ? 19.154  31.023  32.452  1.00 21.63 ?  493  GLU E O   1 
ATOM   12615 C  CB  . GLU E  1 469 ? 19.828  33.868  30.863  1.00 21.51 ?  493  GLU E CB  1 
ATOM   12616 C  CG  . GLU E  1 469 ? 20.939  34.765  30.288  1.00 22.50 ?  493  GLU E CG  1 
ATOM   12617 C  CD  . GLU E  1 469 ? 21.142  36.073  31.050  1.00 24.57 ?  493  GLU E CD  1 
ATOM   12618 O  OE1 . GLU E  1 469 ? 20.508  36.278  32.109  1.00 24.38 ?  493  GLU E OE1 1 
ATOM   12619 O  OE2 . GLU E  1 469 ? 21.944  36.907  30.575  1.00 25.76 -1 493  GLU E OE2 1 
ATOM   12620 N  N   . GLY E  1 470 ? 17.969  32.803  33.154  1.00 21.74 ?  494  GLY E N   1 
ATOM   12621 C  CA  . GLY E  1 470 ? 16.812  32.020  33.558  1.00 21.66 ?  494  GLY E CA  1 
ATOM   12622 C  C   . GLY E  1 470 ? 16.947  31.408  34.930  1.00 21.79 ?  494  GLY E C   1 
ATOM   12623 O  O   . GLY E  1 470 ? 16.897  32.118  35.937  1.00 22.07 ?  494  GLY E O   1 
ATOM   12624 N  N   . TRP E  1 471 ? 17.139  30.090  34.961  1.00 21.73 ?  495  TRP E N   1 
ATOM   12625 C  CA  . TRP E  1 471 ? 17.123  29.308  36.197  1.00 21.93 ?  495  TRP E CA  1 
ATOM   12626 C  C   . TRP E  1 471 ? 18.205  29.707  37.200  1.00 22.03 ?  495  TRP E C   1 
ATOM   12627 O  O   . TRP E  1 471 ? 17.929  29.818  38.397  1.00 22.00 ?  495  TRP E O   1 
ATOM   12628 C  CB  . TRP E  1 471 ? 17.212  27.806  35.885  1.00 21.96 ?  495  TRP E CB  1 
ATOM   12629 C  CG  . TRP E  1 471 ? 16.715  26.928  36.998  1.00 22.31 ?  495  TRP E CG  1 
ATOM   12630 C  CD1 . TRP E  1 471 ? 17.458  26.080  37.768  1.00 22.33 ?  495  TRP E CD1 1 
ATOM   12631 C  CD2 . TRP E  1 471 ? 15.364  26.821  37.472  1.00 22.07 ?  495  TRP E CD2 1 
ATOM   12632 N  NE1 . TRP E  1 471 ? 16.656  25.448  38.686  1.00 22.24 ?  495  TRP E NE1 1 
ATOM   12633 C  CE2 . TRP E  1 471 ? 15.366  25.882  38.526  1.00 22.53 ?  495  TRP E CE2 1 
ATOM   12634 C  CE3 . TRP E  1 471 ? 14.153  27.425  37.106  1.00 22.10 ?  495  TRP E CE3 1 
ATOM   12635 C  CZ2 . TRP E  1 471 ? 14.203  25.533  39.224  1.00 22.76 ?  495  TRP E CZ2 1 
ATOM   12636 C  CZ3 . TRP E  1 471 ? 12.998  27.077  37.797  1.00 22.77 ?  495  TRP E CZ3 1 
ATOM   12637 C  CH2 . TRP E  1 471 ? 13.033  26.138  38.845  1.00 23.13 ?  495  TRP E CH2 1 
ATOM   12638 N  N   . GLY E  1 472 ? 19.424  29.924  36.707  1.00 22.08 ?  496  GLY E N   1 
ATOM   12639 C  CA  . GLY E  1 472 ? 20.544  30.361  37.543  1.00 22.08 ?  496  GLY E CA  1 
ATOM   12640 C  C   . GLY E  1 472 ? 20.265  31.652  38.301  1.00 22.23 ?  496  GLY E C   1 
ATOM   12641 O  O   . GLY E  1 472 ? 20.269  31.654  39.533  1.00 22.22 ?  496  GLY E O   1 
ATOM   12642 N  N   . PRO E  1 473 ? 20.033  32.763  37.569  1.00 22.31 ?  497  PRO E N   1 
ATOM   12643 C  CA  . PRO E  1 473 ? 19.698  34.044  38.198  1.00 22.53 ?  497  PRO E CA  1 
ATOM   12644 C  C   . PRO E  1 473 ? 18.414  34.029  39.037  1.00 22.79 ?  497  PRO E C   1 
ATOM   12645 O  O   . PRO E  1 473 ? 18.371  34.676  40.081  1.00 23.09 ?  497  PRO E O   1 
ATOM   12646 C  CB  . PRO E  1 473 ? 19.553  34.992  37.004  1.00 22.37 ?  497  PRO E CB  1 
ATOM   12647 C  CG  . PRO E  1 473 ? 20.461  34.406  35.971  1.00 22.53 ?  497  PRO E CG  1 
ATOM   12648 C  CD  . PRO E  1 473 ? 20.296  32.923  36.123  1.00 22.14 ?  497  PRO E CD  1 
ATOM   12649 N  N   . MET E  1 474 ? 17.387  33.304  38.592  1.00 23.05 ?  498  MET E N   1 
ATOM   12650 C  CA  . MET E  1 474 ? 16.160  33.165  39.384  1.00 23.30 ?  498  MET E CA  1 
ATOM   12651 C  C   . MET E  1 474 ? 16.390  32.395  40.683  1.00 23.05 ?  498  MET E C   1 
ATOM   12652 O  O   . MET E  1 474 ? 15.805  32.736  41.716  1.00 22.78 ?  498  MET E O   1 
ATOM   12653 C  CB  . MET E  1 474 ? 15.031  32.521  38.575  1.00 23.41 ?  498  MET E CB  1 
ATOM   12654 C  CG  . MET E  1 474 ? 14.309  33.497  37.649  1.00 24.58 ?  498  MET E CG  1 
ATOM   12655 S  SD  . MET E  1 474 ? 12.768  32.832  36.981  1.00 26.71 ?  498  MET E SD  1 
ATOM   12656 C  CE  . MET E  1 474 ? 13.383  31.419  36.094  1.00 26.11 ?  498  MET E CE  1 
ATOM   12657 N  N   . ASN E  1 475 ? 17.236  31.363  40.621  1.00 22.83 ?  499  ASN E N   1 
ATOM   12658 C  CA  . ASN E  1 475 ? 17.654  30.624  41.816  1.00 22.73 ?  499  ASN E CA  1 
ATOM   12659 C  C   . ASN E  1 475 ? 18.270  31.545  42.871  1.00 22.81 ?  499  ASN E C   1 
ATOM   12660 O  O   . ASN E  1 475 ? 17.937  31.446  44.047  1.00 22.84 ?  499  ASN E O   1 
ATOM   12661 C  CB  . ASN E  1 475 ? 18.636  29.501  41.455  1.00 22.61 ?  499  ASN E CB  1 
ATOM   12662 C  CG  . ASN E  1 475 ? 19.003  28.636  42.651  1.00 22.44 ?  499  ASN E CG  1 
ATOM   12663 O  OD1 . ASN E  1 475 ? 18.185  27.861  43.146  1.00 22.08 ?  499  ASN E OD1 1 
ATOM   12664 N  ND2 . ASN E  1 475 ? 20.242  28.762  43.117  1.00 21.17 ?  499  ASN E ND2 1 
ATOM   12665 N  N   . ARG E  1 476 ? 19.149  32.445  42.436  1.00 23.00 ?  500  ARG E N   1 
ATOM   12666 C  CA  . ARG E  1 476 ? 19.801  33.397  43.336  1.00 23.55 ?  500  ARG E CA  1 
ATOM   12667 C  C   . ARG E  1 476 ? 18.796  34.363  43.973  1.00 23.62 ?  500  ARG E C   1 
ATOM   12668 O  O   . ARG E  1 476 ? 18.813  34.561  45.189  1.00 23.74 ?  500  ARG E O   1 
ATOM   12669 C  CB  . ARG E  1 476 ? 20.916  34.167  42.610  1.00 23.29 ?  500  ARG E CB  1 
ATOM   12670 C  CG  . ARG E  1 476 ? 21.665  35.173  43.493  1.00 23.78 ?  500  ARG E CG  1 
ATOM   12671 C  CD  . ARG E  1 476 ? 22.988  35.646  42.868  1.00 23.99 ?  500  ARG E CD  1 
ATOM   12672 N  NE  . ARG E  1 476 ? 22.814  36.194  41.526  1.00 23.96 ?  500  ARG E NE  1 
ATOM   12673 C  CZ  . ARG E  1 476 ? 23.291  35.647  40.409  1.00 24.39 ?  500  ARG E CZ  1 
ATOM   12674 N  NH1 . ARG E  1 476 ? 24.005  34.527  40.444  1.00 23.26 ?  500  ARG E NH1 1 
ATOM   12675 N  NH2 . ARG E  1 476 ? 23.057  36.238  39.245  1.00 24.35 ?  500  ARG E NH2 1 
ATOM   12676 N  N   . ALA E  1 477 ? 17.928  34.947  43.146  1.00 23.66 ?  501  ALA E N   1 
ATOM   12677 C  CA  . ALA E  1 477 ? 16.877  35.843  43.629  1.00 23.81 ?  501  ALA E CA  1 
ATOM   12678 C  C   . ALA E  1 477 ? 16.022  35.158  44.695  1.00 23.73 ?  501  ALA E C   1 
ATOM   12679 O  O   . ALA E  1 477 ? 15.790  35.729  45.759  1.00 23.73 ?  501  ALA E O   1 
ATOM   12680 C  CB  . ALA E  1 477 ? 16.012  36.334  42.473  1.00 23.68 ?  501  ALA E CB  1 
ATOM   12681 N  N   . TYR E  1 478 ? 15.574  33.936  44.403  1.00 23.65 ?  502  TYR E N   1 
ATOM   12682 C  CA  . TYR E  1 478 ? 14.820  33.119  45.359  1.00 23.82 ?  502  TYR E CA  1 
ATOM   12683 C  C   . TYR E  1 478 ? 15.591  32.968  46.671  1.00 23.80 ?  502  TYR E C   1 
ATOM   12684 O  O   . TYR E  1 478 ? 15.042  33.198  47.751  1.00 23.46 ?  502  TYR E O   1 
ATOM   12685 C  CB  . TYR E  1 478 ? 14.509  31.739  44.760  1.00 23.86 ?  502  TYR E CB  1 
ATOM   12686 C  CG  . TYR E  1 478 ? 13.738  30.800  45.673  1.00 24.28 ?  502  TYR E CG  1 
ATOM   12687 C  CD1 . TYR E  1 478 ? 14.390  30.083  46.680  1.00 24.74 ?  502  TYR E CD1 1 
ATOM   12688 C  CD2 . TYR E  1 478 ? 12.363  30.611  45.515  1.00 25.08 ?  502  TYR E CD2 1 
ATOM   12689 C  CE1 . TYR E  1 478 ? 13.698  29.216  47.514  1.00 25.05 ?  502  TYR E CE1 1 
ATOM   12690 C  CE2 . TYR E  1 478 ? 11.653  29.740  46.349  1.00 25.51 ?  502  TYR E CE2 1 
ATOM   12691 C  CZ  . TYR E  1 478 ? 12.332  29.048  47.348  1.00 25.81 ?  502  TYR E CZ  1 
ATOM   12692 O  OH  . TYR E  1 478 ? 11.654  28.189  48.184  1.00 26.05 ?  502  TYR E OH  1 
ATOM   12693 N  N   . VAL E  1 479 ? 16.865  32.590  46.556  1.00 23.87 ?  503  VAL E N   1 
ATOM   12694 C  CA  . VAL E  1 479 ? 17.737  32.376  47.709  1.00 24.03 ?  503  VAL E CA  1 
ATOM   12695 C  C   . VAL E  1 479 ? 17.872  33.642  48.558  1.00 24.40 ?  503  VAL E C   1 
ATOM   12696 O  O   . VAL E  1 479 ? 17.754  33.587  49.783  1.00 24.37 ?  503  VAL E O   1 
ATOM   12697 C  CB  . VAL E  1 479 ? 19.138  31.850  47.271  1.00 24.02 ?  503  VAL E CB  1 
ATOM   12698 C  CG1 . VAL E  1 479 ? 20.132  31.878  48.427  1.00 23.58 ?  503  VAL E CG1 1 
ATOM   12699 C  CG2 . VAL E  1 479 ? 19.024  30.434  46.702  1.00 23.50 ?  503  VAL E CG2 1 
ATOM   12700 N  N   . GLU E  1 480 ? 18.096  34.775  47.896  1.00 24.54 ?  504  GLU E N   1 
ATOM   12701 C  CA  . GLU E  1 480 ? 18.303  36.047  48.578  1.00 24.83 ?  504  GLU E CA  1 
ATOM   12702 C  C   . GLU E  1 480 ? 17.003  36.605  49.163  1.00 24.95 ?  504  GLU E C   1 
ATOM   12703 O  O   . GLU E  1 480 ? 17.017  37.230  50.228  1.00 24.82 ?  504  GLU E O   1 
ATOM   12704 C  CB  . GLU E  1 480 ? 18.995  37.057  47.649  1.00 24.92 ?  504  GLU E CB  1 
ATOM   12705 C  CG  . GLU E  1 480 ? 20.406  36.607  47.230  1.00 25.44 ?  504  GLU E CG  1 
ATOM   12706 C  CD  . GLU E  1 480 ? 21.127  37.567  46.294  1.00 25.81 ?  504  GLU E CD  1 
ATOM   12707 O  OE1 . GLU E  1 480 ? 20.492  38.489  45.738  1.00 26.45 ?  504  GLU E OE1 1 
ATOM   12708 O  OE2 . GLU E  1 480 ? 22.350  37.389  46.110  1.00 25.99 -1 504  GLU E OE2 1 
ATOM   12709 N  N   . ILE E  1 481 ? 15.890  36.368  48.472  1.00 25.19 ?  505  ILE E N   1 
ATOM   12710 C  CA  . ILE E  1 481 ? 14.564  36.737  48.978  1.00 25.53 ?  505  ILE E CA  1 
ATOM   12711 C  C   . ILE E  1 481 ? 14.240  35.970  50.266  1.00 25.78 ?  505  ILE E C   1 
ATOM   12712 O  O   . ILE E  1 481 ? 13.838  36.573  51.263  1.00 25.71 ?  505  ILE E O   1 
ATOM   12713 C  CB  . ILE E  1 481 ? 13.454  36.545  47.897  1.00 25.59 ?  505  ILE E CB  1 
ATOM   12714 C  CG1 . ILE E  1 481 ? 13.489  37.704  46.892  1.00 25.27 ?  505  ILE E CG1 1 
ATOM   12715 C  CG2 . ILE E  1 481 ? 12.059  36.421  48.533  1.00 25.24 ?  505  ILE E CG2 1 
ATOM   12716 C  CD1 . ILE E  1 481 ? 12.843  37.383  45.552  1.00 25.77 ?  505  ILE E CD1 1 
ATOM   12717 N  N   . GLN E  1 482 ? 14.439  34.652  50.240  1.00 26.08 ?  506  GLN E N   1 
ATOM   12718 C  CA  . GLN E  1 482 ? 14.238  33.797  51.417  1.00 26.61 ?  506  GLN E CA  1 
ATOM   12719 C  C   . GLN E  1 482 ? 15.177  34.163  52.564  1.00 27.03 ?  506  GLN E C   1 
ATOM   12720 O  O   . GLN E  1 482 ? 14.786  34.109  53.738  1.00 26.84 ?  506  GLN E O   1 
ATOM   12721 C  CB  . GLN E  1 482 ? 14.425  32.321  51.057  1.00 26.50 ?  506  GLN E CB  1 
ATOM   12722 C  CG  . GLN E  1 482 ? 13.359  31.748  50.123  1.00 27.27 ?  506  GLN E CG  1 
ATOM   12723 C  CD  . GLN E  1 482 ? 12.106  31.274  50.846  1.00 28.06 ?  506  GLN E CD  1 
ATOM   12724 O  OE1 . GLN E  1 482 ? 11.847  31.644  51.993  1.00 28.03 ?  506  GLN E OE1 1 
ATOM   12725 N  NE2 . GLN E  1 482 ? 11.320  30.446  50.169  1.00 28.29 ?  506  GLN E NE2 1 
ATOM   12726 N  N   . ASP E  1 483 ? 16.409  34.535  52.218  1.00 27.40 ?  507  ASP E N   1 
ATOM   12727 C  CA  . ASP E  1 483 ? 17.413  34.915  53.209  1.00 27.98 ?  507  ASP E CA  1 
ATOM   12728 C  C   . ASP E  1 483 ? 17.051  36.215  53.927  1.00 28.15 ?  507  ASP E C   1 
ATOM   12729 O  O   . ASP E  1 483 ? 17.055  36.270  55.163  1.00 28.39 ?  507  ASP E O   1 
ATOM   12730 C  CB  . ASP E  1 483 ? 18.797  35.028  52.567  1.00 27.90 ?  507  ASP E CB  1 
ATOM   12731 C  CG  . ASP E  1 483 ? 19.905  35.152  53.595  1.00 28.32 ?  507  ASP E CG  1 
ATOM   12732 O  OD1 . ASP E  1 483 ? 20.046  36.238  54.196  1.00 28.53 ?  507  ASP E OD1 1 
ATOM   12733 O  OD2 . ASP E  1 483 ? 20.642  34.164  53.791  1.00 28.22 -1 507  ASP E OD2 1 
ATOM   12734 N  N   . GLU E  1 484 ? 16.743  37.250  53.148  1.00 28.35 ?  508  GLU E N   1 
ATOM   12735 C  CA  . GLU E  1 484 ? 16.332  38.537  53.695  1.00 28.67 ?  508  GLU E CA  1 
ATOM   12736 C  C   . GLU E  1 484 ? 15.030  38.407  54.493  1.00 28.88 ?  508  GLU E C   1 
ATOM   12737 O  O   . GLU E  1 484 ? 14.877  39.030  55.548  1.00 28.88 ?  508  GLU E O   1 
ATOM   12738 C  CB  . GLU E  1 484 ? 16.181  39.583  52.586  1.00 28.57 ?  508  GLU E CB  1 
ATOM   12739 C  CG  . GLU E  1 484 ? 15.983  41.009  53.118  1.00 28.71 ?  508  GLU E CG  1 
ATOM   12740 C  CD  . GLU E  1 484 ? 15.995  42.070  52.030  1.00 28.94 ?  508  GLU E CD  1 
ATOM   12741 O  OE1 . GLU E  1 484 ? 16.523  41.802  50.931  1.00 28.12 ?  508  GLU E OE1 1 
ATOM   12742 O  OE2 . GLU E  1 484 ? 15.475  43.179  52.280  1.00 28.97 -1 508  GLU E OE2 1 
ATOM   12743 N  N   . TYR E  1 485 ? 14.107  37.594  53.982  1.00 29.11 ?  509  TYR E N   1 
ATOM   12744 C  CA  . TYR E  1 485 ? 12.845  37.304  54.667  1.00 29.39 ?  509  TYR E CA  1 
ATOM   12745 C  C   . TYR E  1 485 ? 13.096  36.773  56.079  1.00 29.34 ?  509  TYR E C   1 
ATOM   12746 O  O   . TYR E  1 485 ? 12.545  37.298  57.047  1.00 29.30 ?  509  TYR E O   1 
ATOM   12747 C  CB  . TYR E  1 485 ? 12.010  36.311  53.849  1.00 29.50 ?  509  TYR E CB  1 
ATOM   12748 C  CG  . TYR E  1 485 ? 10.640  35.989  54.413  1.00 30.27 ?  509  TYR E CG  1 
ATOM   12749 C  CD1 . TYR E  1 485 ? 9.742   37.005  54.757  1.00 30.77 ?  509  TYR E CD1 1 
ATOM   12750 C  CD2 . TYR E  1 485 ? 10.228  34.667  54.568  1.00 31.46 ?  509  TYR E CD2 1 
ATOM   12751 C  CE1 . TYR E  1 485 ? 8.479   36.711  55.265  1.00 31.53 ?  509  TYR E CE1 1 
ATOM   12752 C  CE2 . TYR E  1 485 ? 8.961   34.360  55.069  1.00 32.69 ?  509  TYR E CE2 1 
ATOM   12753 C  CZ  . TYR E  1 485 ? 8.094   35.389  55.417  1.00 32.72 ?  509  TYR E CZ  1 
ATOM   12754 O  OH  . TYR E  1 485 ? 6.846   35.092  55.919  1.00 33.84 ?  509  TYR E OH  1 
ATOM   12755 N  N   . THR E  1 486 ? 13.944  35.751  56.183  1.00 29.34 ?  510  THR E N   1 
ATOM   12756 C  CA  . THR E  1 486 ? 14.270  35.128  57.466  1.00 29.44 ?  510  THR E CA  1 
ATOM   12757 C  C   . THR E  1 486 ? 15.008  36.086  58.407  1.00 29.87 ?  510  THR E C   1 
ATOM   12758 O  O   . THR E  1 486 ? 14.669  36.173  59.591  1.00 29.77 ?  510  THR E O   1 
ATOM   12759 C  CB  . THR E  1 486 ? 15.059  33.813  57.270  1.00 29.23 ?  510  THR E CB  1 
ATOM   12760 O  OG1 . THR E  1 486 ? 14.279  32.905  56.484  1.00 28.40 ?  510  THR E OG1 1 
ATOM   12761 C  CG2 . THR E  1 486 ? 15.385  33.155  58.608  1.00 29.21 ?  510  THR E CG2 1 
ATOM   12762 N  N   . LYS E  1 487 ? 15.994  36.814  57.876  1.00 30.28 ?  511  LYS E N   1 
ATOM   12763 C  CA  . LYS E  1 487 ? 16.707  37.836  58.646  1.00 30.89 ?  511  LYS E CA  1 
ATOM   12764 C  C   . LYS E  1 487 ? 15.748  38.885  59.212  1.00 31.31 ?  511  LYS E C   1 
ATOM   12765 O  O   . LYS E  1 487 ? 15.850  39.254  60.383  1.00 31.12 ?  511  LYS E O   1 
ATOM   12766 C  CB  . LYS E  1 487 ? 17.788  38.534  57.805  1.00 30.94 ?  511  LYS E CB  1 
ATOM   12767 C  CG  . LYS E  1 487 ? 19.044  37.711  57.509  1.00 30.92 ?  511  LYS E CG  1 
ATOM   12768 C  CD  . LYS E  1 487 ? 20.270  38.630  57.434  1.00 31.02 ?  511  LYS E CD  1 
ATOM   12769 C  CE  . LYS E  1 487 ? 21.272  38.224  56.352  1.00 30.78 ?  511  LYS E CE  1 
ATOM   12770 N  NZ  . LYS E  1 487 ? 21.762  36.821  56.440  1.00 29.04 ?  511  LYS E NZ  1 
ATOM   12771 N  N   . MET E  1 488 ? 14.824  39.357  58.376  1.00 31.94 ?  512  MET E N   1 
ATOM   12772 C  CA  . MET E  1 488 ? 13.860  40.384  58.785  1.00 32.78 ?  512  MET E CA  1 
ATOM   12773 C  C   . MET E  1 488 ? 12.831  39.892  59.811  1.00 33.43 ?  512  MET E C   1 
ATOM   12774 O  O   . MET E  1 488 ? 12.392  40.667  60.662  1.00 33.39 ?  512  MET E O   1 
ATOM   12775 C  CB  . MET E  1 488 ? 13.167  41.014  57.573  1.00 32.62 ?  512  MET E CB  1 
ATOM   12776 C  CG  . MET E  1 488 ? 14.059  41.982  56.800  1.00 32.75 ?  512  MET E CG  1 
ATOM   12777 S  SD  . MET E  1 488 ? 13.239  42.786  55.409  1.00 32.19 ?  512  MET E SD  1 
ATOM   12778 C  CE  . MET E  1 488 ? 12.247  44.019  56.255  1.00 33.54 ?  512  MET E CE  1 
ATOM   12779 N  N   . GLN E  1 489 ? 12.450  38.616  59.722  1.00 34.24 ?  513  GLN E N   1 
ATOM   12780 C  CA  . GLN E  1 489 ? 11.613  37.981  60.744  1.00 35.20 ?  513  GLN E CA  1 
ATOM   12781 C  C   . GLN E  1 489 ? 12.357  37.911  62.078  1.00 35.69 ?  513  GLN E C   1 
ATOM   12782 O  O   . GLN E  1 489 ? 11.803  38.259  63.125  1.00 35.81 ?  513  GLN E O   1 
ATOM   12783 C  CB  . GLN E  1 489 ? 11.178  36.573  60.319  1.00 35.21 ?  513  GLN E CB  1 
ATOM   12784 C  CG  . GLN E  1 489 ? 10.102  36.526  59.242  1.00 36.14 ?  513  GLN E CG  1 
ATOM   12785 C  CD  . GLN E  1 489 ? 9.750   35.104  58.839  1.00 37.76 ?  513  GLN E CD  1 
ATOM   12786 O  OE1 . GLN E  1 489 ? 10.325  34.553  57.900  1.00 39.20 ?  513  GLN E OE1 1 
ATOM   12787 N  NE2 . GLN E  1 489 ? 8.813   34.497  59.558  1.00 38.04 ?  513  GLN E NE2 1 
ATOM   12788 N  N   . GLU E  1 490 ? 13.615  37.470  62.026  1.00 36.36 ?  514  GLU E N   1 
ATOM   12789 C  CA  . GLU E  1 490 ? 14.463  37.340  63.216  1.00 37.08 ?  514  GLU E CA  1 
ATOM   12790 C  C   . GLU E  1 490 ? 14.667  38.682  63.913  1.00 37.53 ?  514  GLU E C   1 
ATOM   12791 O  O   . GLU E  1 490 ? 14.650  38.761  65.143  1.00 37.54 ?  514  GLU E O   1 
ATOM   12792 C  CB  . GLU E  1 490 ? 15.823  36.739  62.848  1.00 36.98 ?  514  GLU E CB  1 
ATOM   12793 C  CG  . GLU E  1 490 ? 15.789  35.258  62.490  1.00 37.29 ?  514  GLU E CG  1 
ATOM   12794 C  CD  . GLU E  1 490 ? 17.093  34.767  61.873  1.00 37.68 ?  514  GLU E CD  1 
ATOM   12795 O  OE1 . GLU E  1 490 ? 17.315  33.539  61.848  1.00 37.17 ?  514  GLU E OE1 1 
ATOM   12796 O  OE2 . GLU E  1 490 ? 17.898  35.605  61.411  1.00 38.35 -1 514  GLU E OE2 1 
ATOM   12797 N  N   . LEU E  1 491 ? 14.853  39.726  63.109  1.00 38.14 ?  515  LEU E N   1 
ATOM   12798 C  CA  . LEU E  1 491 ? 15.056  41.084  63.597  1.00 38.90 ?  515  LEU E CA  1 
ATOM   12799 C  C   . LEU E  1 491 ? 13.754  41.660  64.157  1.00 39.22 ?  515  LEU E C   1 
ATOM   12800 O  O   . LEU E  1 491 ? 13.773  42.432  65.120  1.00 39.34 ?  515  LEU E O   1 
ATOM   12801 C  CB  . LEU E  1 491 ? 15.599  41.962  62.464  1.00 39.03 ?  515  LEU E CB  1 
ATOM   12802 C  CG  . LEU E  1 491 ? 16.327  43.270  62.791  1.00 40.12 ?  515  LEU E CG  1 
ATOM   12803 C  CD1 . LEU E  1 491 ? 17.446  43.514  61.783  1.00 40.78 ?  515  LEU E CD1 1 
ATOM   12804 C  CD2 . LEU E  1 491 ? 15.368  44.462  62.839  1.00 41.10 ?  515  LEU E CD2 1 
ATOM   12805 N  N   . SER E  1 492 ? 12.632  41.279  63.547  1.00 39.52 ?  516  SER E N   1 
ATOM   12806 C  CA  . SER E  1 492 ? 11.302  41.678  64.010  1.00 39.91 ?  516  SER E CA  1 
ATOM   12807 C  C   . SER E  1 492 ? 10.990  41.082  65.384  1.00 40.11 ?  516  SER E C   1 
ATOM   12808 O  O   . SER E  1 492 ? 10.424  41.758  66.243  1.00 40.12 ?  516  SER E O   1 
ATOM   12809 C  CB  . SER E  1 492 ? 10.232  41.263  62.995  1.00 39.77 ?  516  SER E CB  1 
ATOM   12810 O  OG  . SER E  1 492 ? 8.948   41.707  63.392  1.00 39.84 ?  516  SER E OG  1 
ATOM   12811 N  N   . ALA E  1 493 ? 11.370  39.819  65.574  1.00 40.50 ?  517  ALA E N   1 
ATOM   12812 C  CA  . ALA E  1 493 ? 11.211  39.124  66.850  1.00 41.07 ?  517  ALA E CA  1 
ATOM   12813 C  C   . ALA E  1 493 ? 12.136  39.686  67.930  1.00 41.47 ?  517  ALA E C   1 
ATOM   12814 O  O   . ALA E  1 493 ? 11.764  39.745  69.103  1.00 41.51 ?  517  ALA E O   1 
ATOM   12815 C  CB  . ALA E  1 493 ? 11.445  37.631  66.673  1.00 40.95 ?  517  ALA E CB  1 
ATOM   12816 N  N   . LEU E  1 494 ? 13.337  40.099  67.529  1.00 42.03 ?  518  LEU E N   1 
ATOM   12817 C  CA  . LEU E  1 494 ? 14.275  40.745  68.444  1.00 42.67 ?  518  LEU E CA  1 
ATOM   12818 C  C   . LEU E  1 494 ? 13.753  42.116  68.883  1.00 43.22 ?  518  LEU E C   1 
ATOM   12819 O  O   . LEU E  1 494 ? 13.921  42.509  70.040  1.00 43.05 ?  518  LEU E O   1 
ATOM   12820 C  CB  . LEU E  1 494 ? 15.666  40.866  67.807  1.00 42.53 ?  518  LEU E CB  1 
ATOM   12821 C  CG  . LEU E  1 494 ? 16.850  41.301  68.683  1.00 42.62 ?  518  LEU E CG  1 
ATOM   12822 C  CD1 . LEU E  1 494 ? 17.043  40.380  69.886  1.00 42.11 ?  518  LEU E CD1 1 
ATOM   12823 C  CD2 . LEU E  1 494 ? 18.130  41.371  67.855  1.00 42.66 ?  518  LEU E CD2 1 
ATOM   12824 N  N   . GLN E  1 495 ? 13.115  42.827  67.954  1.00 43.96 ?  519  GLN E N   1 
ATOM   12825 C  CA  . GLN E  1 495 ? 12.493  44.117  68.243  1.00 44.84 ?  519  GLN E CA  1 
ATOM   12826 C  C   . GLN E  1 495 ? 11.308  43.942  69.193  1.00 45.20 ?  519  GLN E C   1 
ATOM   12827 O  O   . GLN E  1 495 ? 11.081  44.777  70.070  1.00 45.24 ?  519  GLN E O   1 
ATOM   12828 C  CB  . GLN E  1 495 ? 12.046  44.799  66.948  1.00 44.93 ?  519  GLN E CB  1 
ATOM   12829 C  CG  . GLN E  1 495 ? 11.657  46.266  67.104  1.00 45.83 ?  519  GLN E CG  1 
ATOM   12830 C  CD  . GLN E  1 495 ? 11.243  46.912  65.791  1.00 47.16 ?  519  GLN E CD  1 
ATOM   12831 O  OE1 . GLN E  1 495 ? 11.741  46.554  64.720  1.00 47.74 ?  519  GLN E OE1 1 
ATOM   12832 N  NE2 . GLN E  1 495 ? 10.333  47.878  65.870  1.00 47.40 ?  519  GLN E NE2 1 
ATOM   12833 N  N   . ALA E  1 496 ? 10.570  42.848  69.012  1.00 45.76 ?  520  ALA E N   1 
ATOM   12834 C  CA  . ALA E  1 496 ? 9.440   42.504  69.877  1.00 46.29 ?  520  ALA E CA  1 
ATOM   12835 C  C   . ALA E  1 496 ? 9.893   42.204  71.306  1.00 46.73 ?  520  ALA E C   1 
ATOM   12836 O  O   . ALA E  1 496 ? 9.191   42.531  72.267  1.00 46.83 ?  520  ALA E O   1 
ATOM   12837 C  CB  . ALA E  1 496 ? 8.669   41.321  69.301  1.00 46.06 ?  520  ALA E CB  1 
ATOM   12838 N  N   . ARG E  1 497 ? 11.065  41.587  71.437  1.00 47.29 ?  521  ARG E N   1 
ATOM   12839 C  CA  . ARG E  1 497 ? 11.630  41.266  72.749  1.00 47.93 ?  521  ARG E CA  1 
ATOM   12840 C  C   . ARG E  1 497 ? 12.115  42.505  73.503  1.00 48.20 ?  521  ARG E C   1 
ATOM   12841 O  O   . ARG E  1 497 ? 12.034  42.558  74.732  1.00 48.31 ?  521  ARG E O   1 
ATOM   12842 C  CB  . ARG E  1 497 ? 12.748  40.227  72.628  1.00 47.94 ?  521  ARG E CB  1 
ATOM   12843 C  CG  . ARG E  1 497 ? 12.250  38.828  72.286  1.00 48.63 ?  521  ARG E CG  1 
ATOM   12844 C  CD  . ARG E  1 497 ? 13.241  37.762  72.720  1.00 49.89 ?  521  ARG E CD  1 
ATOM   12845 N  NE  . ARG E  1 497 ? 14.319  37.563  71.757  1.00 51.02 ?  521  ARG E NE  1 
ATOM   12846 C  CZ  . ARG E  1 497 ? 15.503  37.026  72.045  1.00 51.75 ?  521  ARG E CZ  1 
ATOM   12847 N  NH1 . ARG E  1 497 ? 15.793  36.644  73.284  1.00 52.27 ?  521  ARG E NH1 1 
ATOM   12848 N  NH2 . ARG E  1 497 ? 16.409  36.883  71.089  1.00 51.87 ?  521  ARG E NH2 1 
ATOM   12849 N  N   . VAL E  1 498 ? 12.607  43.497  72.762  1.00 48.56 ?  522  VAL E N   1 
ATOM   12850 C  CA  . VAL E  1 498 ? 13.014  44.782  73.338  1.00 48.99 ?  522  VAL E CA  1 
ATOM   12851 C  C   . VAL E  1 498 ? 11.779  45.591  73.757  1.00 49.50 ?  522  VAL E C   1 
ATOM   12852 O  O   . VAL E  1 498 ? 11.802  46.284  74.779  1.00 49.41 ?  522  VAL E O   1 
ATOM   12853 C  CB  . VAL E  1 498 ? 13.923  45.592  72.366  1.00 48.91 ?  522  VAL E CB  1 
ATOM   12854 C  CG1 . VAL E  1 498 ? 14.207  46.993  72.900  1.00 48.72 ?  522  VAL E CG1 1 
ATOM   12855 C  CG2 . VAL E  1 498 ? 15.233  44.854  72.122  1.00 48.69 ?  522  VAL E CG2 1 
ATOM   12856 N  N   . ASN E  1 499 ? 10.707  45.484  72.970  1.00 50.09 ?  523  ASN E N   1 
ATOM   12857 C  CA  . ASN E  1 499 ? 9.413   46.082  73.309  1.00 50.79 ?  523  ASN E CA  1 
ATOM   12858 C  C   . ASN E  1 499 ? 8.850   45.558  74.633  1.00 51.14 ?  523  ASN E C   1 
ATOM   12859 O  O   . ASN E  1 499 ? 8.328   46.331  75.440  1.00 51.10 ?  523  ASN E O   1 
ATOM   12860 C  CB  . ASN E  1 499 ? 8.395   45.852  72.185  1.00 50.82 ?  523  ASN E CB  1 
ATOM   12861 C  CG  . ASN E  1 499 ? 8.628   46.749  70.979  1.00 51.26 ?  523  ASN E CG  1 
ATOM   12862 O  OD1 . ASN E  1 499 ? 9.239   47.815  71.082  1.00 51.96 ?  523  ASN E OD1 1 
ATOM   12863 N  ND2 . ASN E  1 499 ? 8.126   46.320  69.825  1.00 51.32 ?  523  ASN E ND2 1 
ATOM   12864 N  N   . LYS E  1 500 ? 8.961   44.244  74.837  1.00 51.64 ?  524  LYS E N   1 
ATOM   12865 C  CA  . LYS E  1 500 ? 8.521   43.581  76.066  1.00 52.14 ?  524  LYS E CA  1 
ATOM   12866 C  C   . LYS E  1 500 ? 9.257   44.101  77.298  1.00 52.43 ?  524  LYS E C   1 
ATOM   12867 O  O   . LYS E  1 500 ? 8.636   44.395  78.322  1.00 52.54 ?  524  LYS E O   1 
ATOM   12868 C  CB  . LYS E  1 500 ? 8.732   42.070  75.959  1.00 52.24 ?  524  LYS E CB  1 
ATOM   12869 C  CG  . LYS E  1 500 ? 7.611   41.303  75.271  1.00 52.60 ?  524  LYS E CG  1 
ATOM   12870 C  CD  . LYS E  1 500 ? 7.841   39.795  75.372  1.00 53.24 ?  524  LYS E CD  1 
ATOM   12871 C  CE  . LYS E  1 500 ? 7.749   39.298  76.814  1.00 53.82 ?  524  LYS E CE  1 
ATOM   12872 N  NZ  . LYS E  1 500 ? 8.391   37.966  76.993  1.00 54.22 ?  524  LYS E NZ  1 
ATOM   12873 N  N   . LEU E  1 501 ? 10.580  44.207  77.187  1.00 52.77 ?  525  LEU E N   1 
ATOM   12874 C  CA  . LEU E  1 501 ? 11.435  44.678  78.278  1.00 53.06 ?  525  LEU E CA  1 
ATOM   12875 C  C   . LEU E  1 501 ? 11.161  46.135  78.649  1.00 53.22 ?  525  LEU E C   1 
ATOM   12876 O  O   . LEU E  1 501 ? 11.424  46.554  79.777  1.00 53.28 ?  525  LEU E O   1 
ATOM   12877 C  CB  . LEU E  1 501 ? 12.914  44.501  77.916  1.00 53.01 ?  525  LEU E CB  1 
ATOM   12878 C  CG  . LEU E  1 501 ? 13.472  43.080  77.785  1.00 53.15 ?  525  LEU E CG  1 
ATOM   12879 C  CD1 . LEU E  1 501 ? 14.694  43.077  76.877  1.00 53.21 ?  525  LEU E CD1 1 
ATOM   12880 C  CD2 . LEU E  1 501 ? 13.802  42.470  79.147  1.00 52.97 ?  525  LEU E CD2 1 
ATOM   12881 N  N   . GLU E  1 502 ? 10.637  46.897  77.692  1.00 53.50 ?  526  GLU E N   1 
ATOM   12882 C  CA  . GLU E  1 502 ? 10.304  48.304  77.907  1.00 53.79 ?  526  GLU E CA  1 
ATOM   12883 C  C   . GLU E  1 502 ? 8.921   48.484  78.534  1.00 53.95 ?  526  GLU E C   1 
ATOM   12884 O  O   . GLU E  1 502 ? 8.721   49.389  79.348  1.00 54.02 ?  526  GLU E O   1 
ATOM   12885 C  CB  . GLU E  1 502 ? 10.395  49.083  76.593  1.00 53.76 ?  526  GLU E CB  1 
ATOM   12886 C  CG  . GLU E  1 502 ? 11.824  49.354  76.138  1.00 54.12 ?  526  GLU E CG  1 
ATOM   12887 C  CD  . GLU E  1 502 ? 11.915  49.871  74.712  1.00 54.18 ?  526  GLU E CD  1 
ATOM   12888 O  OE1 . GLU E  1 502 ? 10.977  49.643  73.919  1.00 54.23 ?  526  GLU E OE1 1 
ATOM   12889 O  OE2 . GLU E  1 502 ? 12.940  50.501  74.383  1.00 54.30 ?  526  GLU E OE2 1 
ATOM   12890 N  N   . GLY E  1 503 ? 7.980   47.619  78.152  1.00 54.07 ?  527  GLY E N   1 
ATOM   12891 C  CA  . GLY E  1 503 ? 6.597   47.692  78.631  1.00 54.28 ?  527  GLY E CA  1 
ATOM   12892 C  C   . GLY E  1 503 ? 6.446   47.440  80.121  1.00 54.36 ?  527  GLY E C   1 
ATOM   12893 O  O   . GLY E  1 503 ? 7.284   46.784  80.741  1.00 54.50 ?  527  GLY E O   1 
ATOM   12894 N  N   . SER F  2 1   ? -14.659 37.207  28.593  1.00 46.58 ?  28   SER F N   1 
ATOM   12895 C  CA  . SER F  2 1   ? -14.235 37.921  29.835  1.00 46.58 ?  28   SER F CA  1 
ATOM   12896 C  C   . SER F  2 1   ? -12.777 37.610  30.202  1.00 46.24 ?  28   SER F C   1 
ATOM   12897 O  O   . SER F  2 1   ? -11.951 37.352  29.324  1.00 46.23 ?  28   SER F O   1 
ATOM   12898 C  CB  . SER F  2 1   ? -15.181 37.581  30.995  1.00 46.72 ?  28   SER F CB  1 
ATOM   12899 O  OG  . SER F  2 1   ? -15.111 36.202  31.326  1.00 47.57 ?  28   SER F OG  1 
ATOM   12900 N  N   . SER F  2 2   ? -12.473 37.645  31.499  1.00 45.84 ?  29   SER F N   1 
ATOM   12901 C  CA  . SER F  2 2   ? -11.130 37.376  32.008  1.00 45.19 ?  29   SER F CA  1 
ATOM   12902 C  C   . SER F  2 2   ? -11.029 35.962  32.576  1.00 44.80 ?  29   SER F C   1 
ATOM   12903 O  O   . SER F  2 2   ? -11.984 35.450  33.167  1.00 44.92 ?  29   SER F O   1 
ATOM   12904 C  CB  . SER F  2 2   ? -10.763 38.400  33.083  1.00 45.25 ?  29   SER F CB  1 
ATOM   12905 O  OG  . SER F  2 2   ? -9.392  38.323  33.428  1.00 45.15 ?  29   SER F OG  1 
ATOM   12906 N  N   . LEU F  2 3   ? -9.866  35.341  32.396  1.00 44.14 ?  30   LEU F N   1 
ATOM   12907 C  CA  . LEU F  2 3   ? -9.621  33.981  32.872  1.00 43.41 ?  30   LEU F CA  1 
ATOM   12908 C  C   . LEU F  2 3   ? -9.366  33.946  34.374  1.00 42.92 ?  30   LEU F C   1 
ATOM   12909 O  O   . LEU F  2 3   ? -8.672  34.813  34.914  1.00 42.96 ?  30   LEU F O   1 
ATOM   12910 C  CB  . LEU F  2 3   ? -8.435  33.355  32.123  1.00 43.45 ?  30   LEU F CB  1 
ATOM   12911 C  CG  . LEU F  2 3   ? -8.642  32.235  31.089  1.00 43.55 ?  30   LEU F CG  1 
ATOM   12912 C  CD1 . LEU F  2 3   ? -9.913  32.387  30.253  1.00 43.58 ?  30   LEU F CD1 1 
ATOM   12913 C  CD2 . LEU F  2 3   ? -7.412  32.097  30.188  1.00 43.33 ?  30   LEU F CD2 1 
ATOM   12914 N  N   . ALA F  2 4   ? -9.936  32.945  35.042  1.00 42.07 ?  31   ALA F N   1 
ATOM   12915 C  CA  . ALA F  2 4   ? -9.656  32.707  36.454  1.00 41.34 ?  31   ALA F CA  1 
ATOM   12916 C  C   . ALA F  2 4   ? -8.201  32.265  36.609  1.00 40.64 ?  31   ALA F C   1 
ATOM   12917 O  O   . ALA F  2 4   ? -7.745  31.376  35.879  1.00 40.65 ?  31   ALA F O   1 
ATOM   12918 C  CB  . ALA F  2 4   ? -10.605 31.662  37.027  1.00 41.38 ?  31   ALA F CB  1 
ATOM   12919 N  N   . PRO F  2 5   ? -7.463  32.897  37.544  1.00 39.87 ?  32   PRO F N   1 
ATOM   12920 C  CA  . PRO F  2 5   ? -6.035  32.619  37.718  1.00 39.10 ?  32   PRO F CA  1 
ATOM   12921 C  C   . PRO F  2 5   ? -5.762  31.173  38.123  1.00 38.22 ?  32   PRO F C   1 
ATOM   12922 O  O   . PRO F  2 5   ? -6.424  30.642  39.017  1.00 38.08 ?  32   PRO F O   1 
ATOM   12923 C  CB  . PRO F  2 5   ? -5.621  33.578  38.845  1.00 39.18 ?  32   PRO F CB  1 
ATOM   12924 C  CG  . PRO F  2 5   ? -6.667  34.645  38.850  1.00 39.54 ?  32   PRO F CG  1 
ATOM   12925 C  CD  . PRO F  2 5   ? -7.932  33.940  38.476  1.00 39.91 ?  32   PRO F CD  1 
ATOM   12926 N  N   . ILE F  2 6   ? -4.811  30.545  37.436  1.00 37.20 ?  33   ILE F N   1 
ATOM   12927 C  CA  . ILE F  2 6   ? -4.319  29.216  37.794  1.00 36.30 ?  33   ILE F CA  1 
ATOM   12928 C  C   . ILE F  2 6   ? -2.801  29.306  37.938  1.00 35.66 ?  33   ILE F C   1 
ATOM   12929 O  O   . ILE F  2 6   ? -2.117  29.775  37.025  1.00 35.75 ?  33   ILE F O   1 
ATOM   12930 C  CB  . ILE F  2 6   ? -4.684  28.140  36.727  1.00 36.29 ?  33   ILE F CB  1 
ATOM   12931 C  CG1 . ILE F  2 6   ? -6.198  28.092  36.480  1.00 36.42 ?  33   ILE F CG1 1 
ATOM   12932 C  CG2 . ILE F  2 6   ? -4.170  26.764  37.148  1.00 35.96 ?  33   ILE F CG2 1 
ATOM   12933 C  CD1 . ILE F  2 6   ? -6.609  27.274  35.256  1.00 36.38 ?  33   ILE F CD1 1 
ATOM   12934 N  N   . SER F  2 7   ? -2.281  28.864  39.082  1.00 34.71 ?  34   SER F N   1 
ATOM   12935 C  CA  . SER F  2 7   ? -0.837  28.877  39.336  1.00 33.77 ?  34   SER F CA  1 
ATOM   12936 C  C   . SER F  2 7   ? -0.087  28.006  38.328  1.00 33.31 ?  34   SER F C   1 
ATOM   12937 O  O   . SER F  2 7   ? -0.634  27.033  37.804  1.00 33.13 ?  34   SER F O   1 
ATOM   12938 C  CB  . SER F  2 7   ? -0.526  28.419  40.765  1.00 33.72 ?  34   SER F CB  1 
ATOM   12939 O  OG  . SER F  2 7   ? -0.713  27.020  40.915  1.00 33.02 ?  34   SER F OG  1 
ATOM   12940 N  N   . ALA F  2 8   ? 1.166   28.368  38.065  1.00 32.76 ?  35   ALA F N   1 
ATOM   12941 C  CA  . ALA F  2 8   ? 1.993   27.653  37.097  1.00 32.30 ?  35   ALA F CA  1 
ATOM   12942 C  C   . ALA F  2 8   ? 2.192   26.195  37.501  1.00 31.94 ?  35   ALA F C   1 
ATOM   12943 O  O   . ALA F  2 8   ? 2.148   25.308  36.649  1.00 31.43 ?  35   ALA F O   1 
ATOM   12944 C  CB  . ALA F  2 8   ? 3.327   28.349  36.917  1.00 32.11 ?  35   ALA F CB  1 
ATOM   12945 N  N   . LYS F  2 9   ? 2.383   25.950  38.798  1.00 31.78 ?  36   LYS F N   1 
ATOM   12946 C  CA  . LYS F  2 9   ? 2.527   24.580  39.296  1.00 31.94 ?  36   LYS F CA  1 
ATOM   12947 C  C   . LYS F  2 9   ? 1.272   23.734  39.033  1.00 31.72 ?  36   LYS F C   1 
ATOM   12948 O  O   . LYS F  2 9   ? 1.380   22.547  38.716  1.00 31.53 ?  36   LYS F O   1 
ATOM   12949 C  CB  . LYS F  2 9   ? 2.939   24.547  40.775  1.00 31.89 ?  36   LYS F CB  1 
ATOM   12950 C  CG  . LYS F  2 9   ? 1.824   24.772  41.787  1.00 33.03 ?  36   LYS F CG  1 
ATOM   12951 C  CD  . LYS F  2 9   ? 2.262   24.314  43.175  1.00 34.82 ?  36   LYS F CD  1 
ATOM   12952 C  CE  . LYS F  2 9   ? 1.094   24.243  44.148  1.00 35.70 ?  36   LYS F CE  1 
ATOM   12953 N  NZ  . LYS F  2 9   ? 0.185   23.112  43.841  1.00 36.42 ?  36   LYS F NZ  1 
ATOM   12954 N  N   . ASP F  2 10  ? 0.098   24.355  39.149  1.00 31.62 ?  37   ASP F N   1 
ATOM   12955 C  CA  . ASP F  2 10  ? -1.167  23.686  38.840  1.00 31.72 ?  37   ASP F CA  1 
ATOM   12956 C  C   . ASP F  2 10  ? -1.347  23.459  37.338  1.00 31.68 ?  37   ASP F C   1 
ATOM   12957 O  O   . ASP F  2 10  ? -1.841  22.409  36.927  1.00 31.59 ?  37   ASP F O   1 
ATOM   12958 C  CB  . ASP F  2 10  ? -2.359  24.457  39.420  1.00 31.73 ?  37   ASP F CB  1 
ATOM   12959 C  CG  . ASP F  2 10  ? -2.455  24.347  40.944  1.00 32.39 ?  37   ASP F CG  1 
ATOM   12960 O  OD1 . ASP F  2 10  ? -3.107  25.219  41.553  1.00 33.02 ?  37   ASP F OD1 1 
ATOM   12961 O  OD2 . ASP F  2 10  ? -1.885  23.405  41.539  1.00 32.68 ?  37   ASP F OD2 1 
ATOM   12962 N  N   . MET F  2 11  ? -0.951  24.443  36.526  1.00 31.69 ?  38   MET F N   1 
ATOM   12963 C  CA  . MET F  2 11  ? -0.941  24.284  35.069  1.00 31.75 ?  38   MET F CA  1 
ATOM   12964 C  C   . MET F  2 11  ? -0.051  23.112  34.649  1.00 31.86 ?  38   MET F C   1 
ATOM   12965 O  O   . MET F  2 11  ? -0.418  22.344  33.760  1.00 31.48 ?  38   MET F O   1 
ATOM   12966 C  CB  . MET F  2 11  ? -0.484  25.569  34.361  1.00 31.70 ?  38   MET F CB  1 
ATOM   12967 C  CG  . MET F  2 11  ? -1.498  26.716  34.355  1.00 31.52 ?  38   MET F CG  1 
ATOM   12968 S  SD  . MET F  2 11  ? -3.067  26.398  33.504  1.00 31.00 ?  38   MET F SD  1 
ATOM   12969 C  CE  . MET F  2 11  ? -2.514  25.984  31.847  1.00 30.64 ?  38   MET F CE  1 
ATOM   12970 N  N   . LEU F  2 12  ? 1.109   22.981  35.298  1.00 32.21 ?  39   LEU F N   1 
ATOM   12971 C  CA  . LEU F  2 12  ? 2.038   21.880  35.025  1.00 32.75 ?  39   LEU F CA  1 
ATOM   12972 C  C   . LEU F  2 12  ? 1.423   20.515  35.345  1.00 33.19 ?  39   LEU F C   1 
ATOM   12973 O  O   . LEU F  2 12  ? 1.456   19.602  34.516  1.00 33.02 ?  39   LEU F O   1 
ATOM   12974 C  CB  . LEU F  2 12  ? 3.351   22.045  35.805  1.00 32.57 ?  39   LEU F CB  1 
ATOM   12975 C  CG  . LEU F  2 12  ? 4.645   22.638  35.215  1.00 32.60 ?  39   LEU F CG  1 
ATOM   12976 C  CD1 . LEU F  2 12  ? 4.778   22.481  33.689  1.00 31.15 ?  39   LEU F CD1 1 
ATOM   12977 C  CD2 . LEU F  2 12  ? 4.845   24.081  35.641  1.00 31.95 ?  39   LEU F CD2 1 
ATOM   12978 N  N   . ASP F  2 13  ? 0.865   20.389  36.549  1.00 33.72 ?  40   ASP F N   1 
ATOM   12979 C  CA  . ASP F  2 13  ? 0.246   19.141  37.000  1.00 34.64 ?  40   ASP F CA  1 
ATOM   12980 C  C   . ASP F  2 13  ? -0.929  18.745  36.103  1.00 35.36 ?  40   ASP F C   1 
ATOM   12981 O  O   . ASP F  2 13  ? -1.094  17.570  35.764  1.00 35.17 ?  40   ASP F O   1 
ATOM   12982 C  CB  . ASP F  2 13  ? -0.200  19.255  38.464  1.00 34.50 ?  40   ASP F CB  1 
ATOM   12983 C  CG  . ASP F  2 13  ? 0.966   19.457  39.428  1.00 34.18 ?  40   ASP F CG  1 
ATOM   12984 O  OD1 . ASP F  2 13  ? 2.136   19.266  39.028  1.00 33.64 ?  40   ASP F OD1 1 
ATOM   12985 O  OD2 . ASP F  2 13  ? 0.707   19.804  40.598  1.00 33.58 ?  40   ASP F OD2 1 
ATOM   12986 N  N   . TYR F  2 14  ? -1.728  19.738  35.714  1.00 36.29 ?  41   TYR F N   1 
ATOM   12987 C  CA  . TYR F  2 14  ? -2.819  19.543  34.760  1.00 37.36 ?  41   TYR F CA  1 
ATOM   12988 C  C   . TYR F  2 14  ? -2.292  18.988  33.432  1.00 37.81 ?  41   TYR F C   1 
ATOM   12989 O  O   . TYR F  2 14  ? -2.867  18.048  32.875  1.00 37.80 ?  41   TYR F O   1 
ATOM   12990 C  CB  . TYR F  2 14  ? -3.589  20.856  34.550  1.00 37.45 ?  41   TYR F CB  1 
ATOM   12991 C  CG  . TYR F  2 14  ? -4.689  20.785  33.511  1.00 39.09 ?  41   TYR F CG  1 
ATOM   12992 C  CD1 . TYR F  2 14  ? -5.904  20.152  33.790  1.00 40.16 ?  41   TYR F CD1 1 
ATOM   12993 C  CD2 . TYR F  2 14  ? -4.517  21.355  32.247  1.00 40.24 ?  41   TYR F CD2 1 
ATOM   12994 C  CE1 . TYR F  2 14  ? -6.917  20.084  32.837  1.00 40.86 ?  41   TYR F CE1 1 
ATOM   12995 C  CE2 . TYR F  2 14  ? -5.525  21.293  31.286  1.00 41.15 ?  41   TYR F CE2 1 
ATOM   12996 C  CZ  . TYR F  2 14  ? -6.721  20.657  31.589  1.00 41.54 ?  41   TYR F CZ  1 
ATOM   12997 O  OH  . TYR F  2 14  ? -7.719  20.594  30.644  1.00 42.32 ?  41   TYR F OH  1 
ATOM   12998 N  N   . LEU F  2 15  ? -1.190  19.565  32.949  1.00 38.53 ?  42   LEU F N   1 
ATOM   12999 C  CA  . LEU F  2 15  ? -0.532  19.124  31.716  1.00 39.31 ?  42   LEU F CA  1 
ATOM   13000 C  C   . LEU F  2 15  ? -0.011  17.689  31.803  1.00 39.96 ?  42   LEU F C   1 
ATOM   13001 O  O   . LEU F  2 15  ? -0.157  16.913  30.855  1.00 40.06 ?  42   LEU F O   1 
ATOM   13002 C  CB  . LEU F  2 15  ? 0.606   20.083  31.339  1.00 39.15 ?  42   LEU F CB  1 
ATOM   13003 C  CG  . LEU F  2 15  ? 0.358   21.191  30.308  1.00 39.31 ?  42   LEU F CG  1 
ATOM   13004 C  CD1 . LEU F  2 15  ? -0.926  21.960  30.564  1.00 39.74 ?  42   LEU F CD1 1 
ATOM   13005 C  CD2 . LEU F  2 15  ? 1.547   22.142  30.252  1.00 38.97 ?  42   LEU F CD2 1 
ATOM   13006 N  N   . ALA F  2 16  ? 0.586   17.345  32.943  1.00 40.80 ?  43   ALA F N   1 
ATOM   13007 C  CA  . ALA F  2 16  ? 1.112   15.997  33.182  1.00 41.80 ?  43   ALA F CA  1 
ATOM   13008 C  C   . ALA F  2 16  ? 0.001   14.946  33.265  1.00 42.58 ?  43   ALA F C   1 
ATOM   13009 O  O   . ALA F  2 16  ? 0.221   13.773  32.952  1.00 42.68 ?  43   ALA F O   1 
ATOM   13010 C  CB  . ALA F  2 16  ? 1.958   15.976  34.449  1.00 41.63 ?  43   ALA F CB  1 
ATOM   13011 N  N   . CYS F  2 17  ? -1.184  15.384  33.685  1.00 43.57 ?  44   CYS F N   1 
ATOM   13012 C  CA  . CYS F  2 17  ? -2.353  14.520  33.826  1.00 44.66 ?  44   CYS F CA  1 
ATOM   13013 C  C   . CYS F  2 17  ? -3.275  14.571  32.604  1.00 45.58 ?  44   CYS F C   1 
ATOM   13014 O  O   . CYS F  2 17  ? -4.331  13.931  32.590  1.00 45.70 ?  44   CYS F O   1 
ATOM   13015 C  CB  . CYS F  2 17  ? -3.138  14.905  35.085  1.00 44.57 ?  44   CYS F CB  1 
ATOM   13016 S  SG  . CYS F  2 17  ? -2.319  14.478  36.637  1.00 44.13 ?  44   CYS F SG  1 
ATOM   13017 N  N   . LYS F  2 18  ? -2.869  15.325  31.583  1.00 46.66 ?  45   LYS F N   1 
ATOM   13018 C  CA  . LYS F  2 18  ? -3.693  15.534  30.390  1.00 47.73 ?  45   LYS F CA  1 
ATOM   13019 C  C   . LYS F  2 18  ? -3.539  14.388  29.382  1.00 48.23 ?  45   LYS F C   1 
ATOM   13020 O  O   . LYS F  2 18  ? -2.921  14.556  28.321  1.00 48.48 ?  45   LYS F O   1 
ATOM   13021 C  CB  . LYS F  2 18  ? -3.361  16.886  29.741  1.00 47.87 ?  45   LYS F CB  1 
ATOM   13022 C  CG  . LYS F  2 18  ? -4.430  17.423  28.800  1.00 48.44 ?  45   LYS F CG  1 
ATOM   13023 C  CD  . LYS F  2 18  ? -3.827  18.396  27.790  1.00 49.32 ?  45   LYS F CD  1 
ATOM   13024 C  CE  . LYS F  2 18  ? -4.888  18.970  26.856  1.00 49.88 ?  45   LYS F CE  1 
ATOM   13025 N  NZ  . LYS F  2 18  ? -5.712  20.026  27.513  1.00 49.94 ?  45   LYS F NZ  1 
ATOM   13026 N  N   . ASP F  2 19  ? -4.096  13.228  29.742  1.00 48.70 ?  46   ASP F N   1 
ATOM   13027 C  CA  . ASP F  2 19  ? -4.168  12.031  28.888  1.00 49.00 ?  46   ASP F CA  1 
ATOM   13028 C  C   . ASP F  2 19  ? -4.223  10.750  29.730  1.00 48.98 ?  46   ASP F C   1 
ATOM   13029 O  O   . ASP F  2 19  ? -3.903  9.661   29.238  1.00 49.08 ?  46   ASP F O   1 
ATOM   13030 C  CB  . ASP F  2 19  ? -2.992  11.958  27.899  1.00 49.33 ?  46   ASP F CB  1 
ATOM   13031 C  CG  . ASP F  2 19  ? -3.384  11.346  26.556  1.00 50.22 ?  46   ASP F CG  1 
ATOM   13032 O  OD1 . ASP F  2 19  ? -2.621  10.501  26.042  1.00 51.11 ?  46   ASP F OD1 1 
ATOM   13033 O  OD2 . ASP F  2 19  ? -4.448  11.714  26.007  1.00 51.39 ?  46   ASP F OD2 1 
ATOM   13034 N  N   . LYS F  2 20  ? -4.625  10.875  30.995  1.00 48.77 ?  47   LYS F N   1 
ATOM   13035 C  CA  . LYS F  2 20  ? -4.700  9.706   31.881  1.00 48.60 ?  47   LYS F CA  1 
ATOM   13036 C  C   . LYS F  2 20  ? -5.834  9.712   32.918  1.00 48.33 ?  47   LYS F C   1 
ATOM   13037 O  O   . LYS F  2 20  ? -6.634  10.648  32.978  1.00 48.32 ?  47   LYS F O   1 
ATOM   13038 C  CB  . LYS F  2 20  ? -3.337  9.407   32.529  1.00 48.72 ?  47   LYS F CB  1 
ATOM   13039 C  CG  . LYS F  2 20  ? -2.721  10.537  33.346  1.00 48.71 ?  47   LYS F CG  1 
ATOM   13040 C  CD  . LYS F  2 20  ? -1.197  10.526  33.227  1.00 48.78 ?  47   LYS F CD  1 
ATOM   13041 C  CE  . LYS F  2 20  ? -0.597  9.154   33.523  1.00 49.03 ?  47   LYS F CE  1 
ATOM   13042 N  NZ  . LYS F  2 20  ? 0.810   9.054   33.050  1.00 48.95 ?  47   LYS F NZ  1 
ATOM   13043 N  N   . LYS F  2 21  ? -5.884  8.651   33.723  1.00 47.96 ?  48   LYS F N   1 
ATOM   13044 C  CA  . LYS F  2 21  ? -6.998  8.389   34.636  1.00 47.62 ?  48   LYS F CA  1 
ATOM   13045 C  C   . LYS F  2 21  ? -6.982  9.292   35.875  1.00 47.08 ?  48   LYS F C   1 
ATOM   13046 O  O   . LYS F  2 21  ? -5.912  9.703   36.325  1.00 47.07 ?  48   LYS F O   1 
ATOM   13047 C  CB  . LYS F  2 21  ? -6.990  6.915   35.061  1.00 47.78 ?  48   LYS F CB  1 
ATOM   13048 C  CG  . LYS F  2 21  ? -7.041  5.922   33.905  1.00 48.44 ?  48   LYS F CG  1 
ATOM   13049 C  CD  . LYS F  2 21  ? -6.769  4.505   34.395  1.00 49.63 ?  48   LYS F CD  1 
ATOM   13050 C  CE  . LYS F  2 21  ? -6.419  3.571   33.249  1.00 50.15 ?  48   LYS F CE  1 
ATOM   13051 N  NZ  . LYS F  2 21  ? -7.615  3.176   32.455  1.00 51.00 ?  48   LYS F NZ  1 
ATOM   13052 N  N   . PRO F  2 22  ? -8.174  9.598   36.433  1.00 46.60 ?  49   PRO F N   1 
ATOM   13053 C  CA  . PRO F  2 22  ? -8.277  10.410  37.654  1.00 46.07 ?  49   PRO F CA  1 
ATOM   13054 C  C   . PRO F  2 22  ? -7.617  9.744   38.862  1.00 45.50 ?  49   PRO F C   1 
ATOM   13055 O  O   . PRO F  2 22  ? -7.310  10.415  39.850  1.00 45.51 ?  49   PRO F O   1 
ATOM   13056 C  CB  . PRO F  2 22  ? -9.790  10.511  37.883  1.00 46.12 ?  49   PRO F CB  1 
ATOM   13057 C  CG  . PRO F  2 22  ? -10.403 10.247  36.554  1.00 46.53 ?  49   PRO F CG  1 
ATOM   13058 C  CD  . PRO F  2 22  ? -9.505  9.239   35.908  1.00 46.69 ?  49   PRO F CD  1 
ATOM   13059 N  N   . THR F  2 23  ? -7.405  8.435   38.767  1.00 44.76 ?  50   THR F N   1 
ATOM   13060 C  CA  . THR F  2 23  ? -6.823  7.646   39.847  1.00 44.04 ?  50   THR F CA  1 
ATOM   13061 C  C   . THR F  2 23  ? -5.292  7.583   39.762  1.00 43.42 ?  50   THR F C   1 
ATOM   13062 O  O   . THR F  2 23  ? -4.624  7.191   40.726  1.00 43.31 ?  50   THR F O   1 
ATOM   13063 C  CB  . THR F  2 23  ? -7.430  6.217   39.877  1.00 44.05 ?  50   THR F CB  1 
ATOM   13064 O  OG1 . THR F  2 23  ? -6.900  5.490   40.991  1.00 44.44 ?  50   THR F OG1 1 
ATOM   13065 C  CG2 . THR F  2 23  ? -7.132  5.461   38.583  1.00 43.91 ?  50   THR F CG2 1 
ATOM   13066 N  N   . ASP F  2 24  ? -4.751  7.977   38.609  1.00 42.64 ?  51   ASP F N   1 
ATOM   13067 C  CA  . ASP F  2 24  ? -3.310  7.944   38.356  1.00 41.83 ?  51   ASP F CA  1 
ATOM   13068 C  C   . ASP F  2 24  ? -2.547  9.006   39.143  1.00 41.14 ?  51   ASP F C   1 
ATOM   13069 O  O   . ASP F  2 24  ? -3.049  10.111  39.372  1.00 40.97 ?  51   ASP F O   1 
ATOM   13070 C  CB  . ASP F  2 24  ? -3.020  8.100   36.860  1.00 41.98 ?  51   ASP F CB  1 
ATOM   13071 C  CG  . ASP F  2 24  ? -3.217  6.806   36.081  1.00 42.42 ?  51   ASP F CG  1 
ATOM   13072 O  OD1 . ASP F  2 24  ? -2.936  6.807   34.864  1.00 42.74 ?  51   ASP F OD1 1 
ATOM   13073 O  OD2 . ASP F  2 24  ? -3.644  5.791   36.676  1.00 42.83 ?  51   ASP F OD2 1 
ATOM   13074 N  N   . VAL F  2 25  ? -1.332  8.650   39.552  1.00 40.23 ?  52   VAL F N   1 
ATOM   13075 C  CA  . VAL F  2 25  ? -0.458  9.549   40.299  1.00 39.28 ?  52   VAL F CA  1 
ATOM   13076 C  C   . VAL F  2 25  ? 0.772   9.907   39.458  1.00 38.64 ?  52   VAL F C   1 
ATOM   13077 O  O   . VAL F  2 25  ? 1.432   9.028   38.893  1.00 38.40 ?  52   VAL F O   1 
ATOM   13078 C  CB  . VAL F  2 25  ? -0.032  8.934   41.663  1.00 39.46 ?  52   VAL F CB  1 
ATOM   13079 C  CG1 . VAL F  2 25  ? 0.893   9.873   42.422  1.00 39.09 ?  52   VAL F CG1 1 
ATOM   13080 C  CG2 . VAL F  2 25  ? -1.258  8.600   42.515  1.00 39.37 ?  52   VAL F CG2 1 
ATOM   13081 N  N   . VAL F  2 26  ? 1.054   11.205  39.368  1.00 37.72 ?  53   VAL F N   1 
ATOM   13082 C  CA  . VAL F  2 26  ? 2.229   11.710  38.658  1.00 36.81 ?  53   VAL F CA  1 
ATOM   13083 C  C   . VAL F  2 26  ? 3.115   12.522  39.602  1.00 36.12 ?  53   VAL F C   1 
ATOM   13084 O  O   . VAL F  2 26  ? 2.676   12.928  40.683  1.00 35.93 ?  53   VAL F O   1 
ATOM   13085 C  CB  . VAL F  2 26  ? 1.848   12.590  37.429  1.00 36.86 ?  53   VAL F CB  1 
ATOM   13086 C  CG1 . VAL F  2 26  ? 1.040   11.794  36.412  1.00 36.92 ?  53   VAL F CG1 1 
ATOM   13087 C  CG2 . VAL F  2 26  ? 1.093   13.852  37.860  1.00 36.81 ?  53   VAL F CG2 1 
ATOM   13088 N  N   . LYS F  2 27  ? 4.359   12.754  39.189  1.00 35.09 ?  54   LYS F N   1 
ATOM   13089 C  CA  . LYS F  2 27  ? 5.257   13.627  39.938  1.00 34.17 ?  54   LYS F CA  1 
ATOM   13090 C  C   . LYS F  2 27  ? 5.009   15.095  39.607  1.00 33.27 ?  54   LYS F C   1 
ATOM   13091 O  O   . LYS F  2 27  ? 4.601   15.436  38.491  1.00 33.04 ?  54   LYS F O   1 
ATOM   13092 C  CB  . LYS F  2 27  ? 6.723   13.265  39.679  1.00 34.28 ?  54   LYS F CB  1 
ATOM   13093 C  CG  . LYS F  2 27  ? 7.189   12.020  40.422  1.00 34.77 ?  54   LYS F CG  1 
ATOM   13094 C  CD  . LYS F  2 27  ? 8.689   11.795  40.281  1.00 35.65 ?  54   LYS F CD  1 
ATOM   13095 C  CE  . LYS F  2 27  ? 9.027   11.065  38.996  1.00 36.05 ?  54   LYS F CE  1 
ATOM   13096 N  NZ  . LYS F  2 27  ? 10.501  10.850  38.846  1.00 36.00 ?  54   LYS F NZ  1 
ATOM   13097 N  N   . SER F  2 28  ? 5.246   15.952  40.597  1.00 32.21 ?  55   SER F N   1 
ATOM   13098 C  CA  . SER F  2 28  ? 5.253   17.396  40.405  1.00 31.33 ?  55   SER F CA  1 
ATOM   13099 C  C   . SER F  2 28  ? 6.396   17.803  39.471  1.00 30.83 ?  55   SER F C   1 
ATOM   13100 O  O   . SER F  2 28  ? 7.416   17.122  39.397  1.00 30.51 ?  55   SER F O   1 
ATOM   13101 C  CB  . SER F  2 28  ? 5.408   18.104  41.754  1.00 31.19 ?  55   SER F CB  1 
ATOM   13102 O  OG  . SER F  2 28  ? 5.517   19.508  41.591  1.00 30.45 ?  55   SER F OG  1 
ATOM   13103 N  N   . HIS F  2 29  ? 6.210   18.907  38.756  1.00 30.29 ?  56   HIS F N   1 
ATOM   13104 C  CA  . HIS F  2 29  ? 7.279   19.493  37.952  1.00 30.03 ?  56   HIS F CA  1 
ATOM   13105 C  C   . HIS F  2 29  ? 8.017   20.593  38.716  1.00 29.74 ?  56   HIS F C   1 
ATOM   13106 O  O   . HIS F  2 29  ? 8.962   21.181  38.190  1.00 29.68 ?  56   HIS F O   1 
ATOM   13107 C  CB  . HIS F  2 29  ? 6.718   20.078  36.652  1.00 30.01 ?  56   HIS F CB  1 
ATOM   13108 C  CG  . HIS F  2 29  ? 6.488   19.065  35.575  1.00 30.33 ?  56   HIS F CG  1 
ATOM   13109 N  ND1 . HIS F  2 29  ? 5.503   18.105  35.653  1.00 30.27 ?  56   HIS F ND1 1 
ATOM   13110 C  CD2 . HIS F  2 29  ? 7.106   18.874  34.385  1.00 30.30 ?  56   HIS F CD2 1 
ATOM   13111 C  CE1 . HIS F  2 29  ? 5.530   17.360  34.563  1.00 31.00 ?  56   HIS F CE1 1 
ATOM   13112 N  NE2 . HIS F  2 29  ? 6.491   17.808  33.776  1.00 30.85 ?  56   HIS F NE2 1 
ATOM   13113 N  N   . THR F  2 30  ? 7.590   20.870  39.951  1.00 29.36 ?  57   THR F N   1 
ATOM   13114 C  CA  . THR F  2 30  ? 8.042   22.070  40.665  1.00 29.02 ?  57   THR F CA  1 
ATOM   13115 C  C   . THR F  2 30  ? 8.277   21.913  42.169  1.00 29.09 ?  57   THR F C   1 
ATOM   13116 O  O   . THR F  2 30  ? 9.102   22.630  42.748  1.00 28.79 ?  57   THR F O   1 
ATOM   13117 C  CB  . THR F  2 30  ? 7.042   23.241  40.486  1.00 29.01 ?  57   THR F CB  1 
ATOM   13118 O  OG1 . THR F  2 30  ? 5.781   22.888  41.065  1.00 28.30 ?  57   THR F OG1 1 
ATOM   13119 C  CG2 . THR F  2 30  ? 6.853   23.597  39.011  1.00 28.66 ?  57   THR F CG2 1 
ATOM   13120 N  N   . GLU F  2 31  ? 7.550   20.992  42.796  1.00 29.33 ?  58   GLU F N   1 
ATOM   13121 C  CA  . GLU F  2 31  ? 7.487   20.929  44.260  1.00 29.75 ?  58   GLU F CA  1 
ATOM   13122 C  C   . GLU F  2 31  ? 8.314   19.806  44.880  1.00 29.95 ?  58   GLU F C   1 
ATOM   13123 O  O   . GLU F  2 31  ? 8.244   18.656  44.449  1.00 30.00 ?  58   GLU F O   1 
ATOM   13124 C  CB  . GLU F  2 31  ? 6.028   20.838  44.740  1.00 29.71 ?  58   GLU F CB  1 
ATOM   13125 C  CG  . GLU F  2 31  ? 5.101   21.952  44.237  1.00 30.13 ?  58   GLU F CG  1 
ATOM   13126 C  CD  . GLU F  2 31  ? 5.637   23.350  44.512  1.00 30.26 ?  58   GLU F CD  1 
ATOM   13127 O  OE1 . GLU F  2 31  ? 5.890   24.088  43.537  1.00 30.19 ?  58   GLU F OE1 1 
ATOM   13128 O  OE2 . GLU F  2 31  ? 5.819   23.707  45.695  1.00 30.23 ?  58   GLU F OE2 1 
ATOM   13129 N  N   . VAL F  2 32  ? 9.091   20.158  45.901  1.00 30.43 ?  59   VAL F N   1 
ATOM   13130 C  CA  . VAL F  2 32  ? 9.832   19.189  46.711  1.00 30.90 ?  59   VAL F CA  1 
ATOM   13131 C  C   . VAL F  2 32  ? 9.408   19.347  48.173  1.00 31.33 ?  59   VAL F C   1 
ATOM   13132 O  O   . VAL F  2 32  ? 9.431   20.454  48.714  1.00 31.17 ?  59   VAL F O   1 
ATOM   13133 C  CB  . VAL F  2 32  ? 11.369  19.383  46.581  1.00 30.74 ?  59   VAL F CB  1 
ATOM   13134 C  CG1 . VAL F  2 32  ? 12.126  18.488  47.566  1.00 31.08 ?  59   VAL F CG1 1 
ATOM   13135 C  CG2 . VAL F  2 32  ? 11.832  19.110  45.157  1.00 30.82 ?  59   VAL F CG2 1 
ATOM   13136 N  N   . GLU F  2 33  ? 8.997   18.247  48.801  1.00 31.88 ?  60   GLU F N   1 
ATOM   13137 C  CA  . GLU F  2 33  ? 8.680   18.253  50.234  1.00 32.68 ?  60   GLU F CA  1 
ATOM   13138 C  C   . GLU F  2 33  ? 9.225   16.997  50.902  1.00 33.03 ?  60   GLU F C   1 
ATOM   13139 O  O   . GLU F  2 33  ? 9.126   15.902  50.344  1.00 33.14 ?  60   GLU F O   1 
ATOM   13140 C  CB  . GLU F  2 33  ? 7.169   18.380  50.486  1.00 32.55 ?  60   GLU F CB  1 
ATOM   13141 C  CG  . GLU F  2 33  ? 6.501   19.658  49.963  1.00 33.04 ?  60   GLU F CG  1 
ATOM   13142 C  CD  . GLU F  2 33  ? 6.878   20.922  50.726  1.00 34.22 ?  60   GLU F CD  1 
ATOM   13143 O  OE1 . GLU F  2 33  ? 6.693   22.022  50.162  1.00 34.37 ?  60   GLU F OE1 1 
ATOM   13144 O  OE2 . GLU F  2 33  ? 7.346   20.832  51.882  1.00 34.57 ?  60   GLU F OE2 1 
ATOM   13145 N  N   . ASN F  2 34  ? 9.802   17.166  52.093  1.00 33.70 ?  61   ASN F N   1 
ATOM   13146 C  CA  . ASN F  2 34  ? 10.417  16.065  52.851  1.00 34.20 ?  61   ASN F CA  1 
ATOM   13147 C  C   . ASN F  2 34  ? 11.478  15.272  52.081  1.00 34.28 ?  61   ASN F C   1 
ATOM   13148 O  O   . ASN F  2 34  ? 11.557  14.042  52.193  1.00 34.29 ?  61   ASN F O   1 
ATOM   13149 C  CB  . ASN F  2 34  ? 9.344   15.125  53.416  1.00 34.54 ?  61   ASN F CB  1 
ATOM   13150 C  CG  . ASN F  2 34  ? 8.701   15.668  54.669  1.00 35.54 ?  61   ASN F CG  1 
ATOM   13151 O  OD1 . ASN F  2 34  ? 7.604   16.224  54.625  1.00 36.61 ?  61   ASN F OD1 1 
ATOM   13152 N  ND2 . ASN F  2 34  ? 9.389   15.522  55.800  1.00 37.06 ?  61   ASN F ND2 1 
ATOM   13153 N  N   . GLY F  2 35  ? 12.289  15.985  51.301  1.00 34.22 ?  62   GLY F N   1 
ATOM   13154 C  CA  . GLY F  2 35  ? 13.373  15.378  50.531  1.00 34.20 ?  62   GLY F CA  1 
ATOM   13155 C  C   . GLY F  2 35  ? 12.920  14.542  49.349  1.00 34.35 ?  62   GLY F C   1 
ATOM   13156 O  O   . GLY F  2 35  ? 13.681  13.712  48.846  1.00 34.38 ?  62   GLY F O   1 
ATOM   13157 N  N   . LYS F  2 36  ? 11.683  14.763  48.905  1.00 34.43 ?  63   LYS F N   1 
ATOM   13158 C  CA  . LYS F  2 36  ? 11.102  14.017  47.788  1.00 34.66 ?  63   LYS F CA  1 
ATOM   13159 C  C   . LYS F  2 36  ? 10.244  14.917  46.901  1.00 34.65 ?  63   LYS F C   1 
ATOM   13160 O  O   . LYS F  2 36  ? 9.614   15.861  47.389  1.00 34.48 ?  63   LYS F O   1 
ATOM   13161 C  CB  . LYS F  2 36  ? 10.258  12.843  48.307  1.00 34.82 ?  63   LYS F CB  1 
ATOM   13162 C  CG  . LYS F  2 36  ? 11.073  11.667  48.854  1.00 35.53 ?  63   LYS F CG  1 
ATOM   13163 C  CD  . LYS F  2 36  ? 10.193  10.575  49.452  1.00 37.10 ?  63   LYS F CD  1 
ATOM   13164 C  CE  . LYS F  2 36  ? 9.962   10.787  50.947  1.00 38.26 ?  63   LYS F CE  1 
ATOM   13165 N  NZ  . LYS F  2 36  ? 11.176  10.460  51.757  1.00 38.84 ?  63   LYS F NZ  1 
ATOM   13166 N  N   . ILE F  2 37  ? 10.224  14.624  45.600  1.00 34.51 ?  64   ILE F N   1 
ATOM   13167 C  CA  . ILE F  2 37  ? 9.313   15.304  44.679  1.00 34.62 ?  64   ILE F CA  1 
ATOM   13168 C  C   . ILE F  2 37  ? 7.879   14.939  45.067  1.00 35.01 ?  64   ILE F C   1 
ATOM   13169 O  O   . ILE F  2 37  ? 7.557   13.761  45.250  1.00 34.82 ?  64   ILE F O   1 
ATOM   13170 C  CB  . ILE F  2 37  ? 9.590   14.946  43.189  1.00 34.44 ?  64   ILE F CB  1 
ATOM   13171 C  CG1 . ILE F  2 37  ? 10.990  15.409  42.774  1.00 34.00 ?  64   ILE F CG1 1 
ATOM   13172 C  CG2 . ILE F  2 37  ? 8.545   15.586  42.271  1.00 34.22 ?  64   ILE F CG2 1 
ATOM   13173 C  CD1 . ILE F  2 37  ? 11.476  14.833  41.455  1.00 33.42 ?  64   ILE F CD1 1 
ATOM   13174 N  N   . VAL F  2 38  ? 7.041   15.965  45.213  1.00 35.44 ?  65   VAL F N   1 
ATOM   13175 C  CA  . VAL F  2 38  ? 5.639   15.805  45.587  1.00 36.00 ?  65   VAL F CA  1 
ATOM   13176 C  C   . VAL F  2 38  ? 4.886   15.013  44.517  1.00 36.55 ?  65   VAL F C   1 
ATOM   13177 O  O   . VAL F  2 38  ? 5.060   15.256  43.320  1.00 36.45 ?  65   VAL F O   1 
ATOM   13178 C  CB  . VAL F  2 38  ? 4.962   17.187  45.825  1.00 35.98 ?  65   VAL F CB  1 
ATOM   13179 C  CG1 . VAL F  2 38  ? 3.468   17.044  46.122  1.00 35.59 ?  65   VAL F CG1 1 
ATOM   13180 C  CG2 . VAL F  2 38  ? 5.655   17.928  46.960  1.00 36.12 ?  65   VAL F CG2 1 
ATOM   13181 N  N   . ARG F  2 39  ? 4.076   14.053  44.961  1.00 37.14 ?  66   ARG F N   1 
ATOM   13182 C  CA  . ARG F  2 39  ? 3.218   13.281  44.064  1.00 37.96 ?  66   ARG F CA  1 
ATOM   13183 C  C   . ARG F  2 39  ? 1.834   13.914  44.012  1.00 38.53 ?  66   ARG F C   1 
ATOM   13184 O  O   . ARG F  2 39  ? 1.334   14.420  45.020  1.00 38.42 ?  66   ARG F O   1 
ATOM   13185 C  CB  . ARG F  2 39  ? 3.110   11.820  44.518  1.00 37.95 ?  66   ARG F CB  1 
ATOM   13186 C  CG  . ARG F  2 39  ? 4.413   11.199  45.014  1.00 38.40 ?  66   ARG F CG  1 
ATOM   13187 C  CD  . ARG F  2 39  ? 5.385   10.876  43.886  1.00 38.48 ?  66   ARG F CD  1 
ATOM   13188 N  NE  . ARG F  2 39  ? 6.745   11.251  44.265  1.00 39.13 ?  66   ARG F NE  1 
ATOM   13189 C  CZ  . ARG F  2 39  ? 7.858   10.715  43.770  1.00 38.87 ?  66   ARG F CZ  1 
ATOM   13190 N  NH1 . ARG F  2 39  ? 7.805   9.745   42.868  1.00 39.03 ?  66   ARG F NH1 1 
ATOM   13191 N  NH2 . ARG F  2 39  ? 9.034   11.149  44.195  1.00 38.56 ?  66   ARG F NH2 1 
ATOM   13192 N  N   . VAL F  2 40  ? 1.224   13.895  42.830  1.00 39.29 ?  67   VAL F N   1 
ATOM   13193 C  CA  . VAL F  2 40  ? -0.097  14.484  42.642  1.00 40.13 ?  67   VAL F CA  1 
ATOM   13194 C  C   . VAL F  2 40  ? -1.063  13.461  42.045  1.00 40.75 ?  67   VAL F C   1 
ATOM   13195 O  O   . VAL F  2 40  ? -0.783  12.860  41.003  1.00 40.70 ?  67   VAL F O   1 
ATOM   13196 C  CB  . VAL F  2 40  ? -0.041  15.765  41.755  1.00 40.08 ?  67   VAL F CB  1 
ATOM   13197 C  CG1 . VAL F  2 40  ? -1.426  16.394  41.616  1.00 39.95 ?  67   VAL F CG1 1 
ATOM   13198 C  CG2 . VAL F  2 40  ? 0.951   16.787  42.325  1.00 40.11 ?  67   VAL F CG2 1 
ATOM   13199 N  N   . LYS F  2 41  ? -2.192  13.258  42.723  1.00 41.61 ?  68   LYS F N   1 
ATOM   13200 C  CA  . LYS F  2 41  ? -3.272  12.437  42.188  1.00 42.57 ?  68   LYS F CA  1 
ATOM   13201 C  C   . LYS F  2 41  ? -3.992  13.253  41.120  1.00 43.10 ?  68   LYS F C   1 
ATOM   13202 O  O   . LYS F  2 41  ? -4.400  14.388  41.371  1.00 43.15 ?  68   LYS F O   1 
ATOM   13203 C  CB  . LYS F  2 41  ? -4.241  12.014  43.295  1.00 42.57 ?  68   LYS F CB  1 
ATOM   13204 C  CG  . LYS F  2 41  ? -5.103  10.807  42.933  1.00 43.38 ?  68   LYS F CG  1 
ATOM   13205 C  CD  . LYS F  2 41  ? -6.191  10.546  43.971  1.00 44.68 ?  68   LYS F CD  1 
ATOM   13206 C  CE  . LYS F  2 41  ? -7.469  11.307  43.648  1.00 45.51 ?  68   LYS F CE  1 
ATOM   13207 N  NZ  . LYS F  2 41  ? -8.542  11.067  44.658  1.00 46.39 ?  68   LYS F NZ  1 
ATOM   13208 N  N   . CYS F  2 42  ? -4.135  12.672  39.932  1.00 43.90 ?  69   CYS F N   1 
ATOM   13209 C  CA  . CYS F  2 42  ? -4.646  13.400  38.768  1.00 44.91 ?  69   CYS F CA  1 
ATOM   13210 C  C   . CYS F  2 42  ? -6.079  13.919  38.917  1.00 45.63 ?  69   CYS F C   1 
ATOM   13211 O  O   . CYS F  2 42  ? -6.421  14.964  38.364  1.00 45.73 ?  69   CYS F O   1 
ATOM   13212 C  CB  . CYS F  2 42  ? -4.494  12.564  37.495  1.00 44.80 ?  69   CYS F CB  1 
ATOM   13213 S  SG  . CYS F  2 42  ? -2.793  12.510  36.879  1.00 45.18 ?  69   CYS F SG  1 
ATOM   13214 N  N   . GLY F  2 43  ? -6.901  13.194  39.672  1.00 46.45 ?  70   GLY F N   1 
ATOM   13215 C  CA  . GLY F  2 43  ? -8.276  13.608  39.940  1.00 47.45 ?  70   GLY F CA  1 
ATOM   13216 C  C   . GLY F  2 43  ? -8.373  14.949  40.644  1.00 48.23 ?  70   GLY F C   1 
ATOM   13217 O  O   . GLY F  2 43  ? -9.259  15.749  40.340  1.00 48.30 ?  70   GLY F O   1 
ATOM   13218 N  N   . ASP F  2 44  ? -7.453  15.194  41.575  1.00 49.07 ?  71   ASP F N   1 
ATOM   13219 C  CA  . ASP F  2 44  ? -7.448  16.421  42.377  1.00 49.93 ?  71   ASP F CA  1 
ATOM   13220 C  C   . ASP F  2 44  ? -7.125  17.677  41.566  1.00 50.53 ?  71   ASP F C   1 
ATOM   13221 O  O   . ASP F  2 44  ? -7.760  18.721  41.752  1.00 50.72 ?  71   ASP F O   1 
ATOM   13222 C  CB  . ASP F  2 44  ? -6.475  16.288  43.556  1.00 49.99 ?  71   ASP F CB  1 
ATOM   13223 C  CG  . ASP F  2 44  ? -6.867  15.178  44.525  1.00 50.29 ?  71   ASP F CG  1 
ATOM   13224 O  OD1 . ASP F  2 44  ? -6.149  14.992  45.529  1.00 50.85 ?  71   ASP F OD1 1 
ATOM   13225 O  OD2 . ASP F  2 44  ? -7.886  14.492  44.290  1.00 50.56 ?  71   ASP F OD2 1 
ATOM   13226 N  N   . ILE F  2 45  ? -6.144  17.577  40.671  1.00 51.23 ?  72   ILE F N   1 
ATOM   13227 C  CA  . ILE F  2 45  ? -5.726  18.724  39.862  1.00 51.98 ?  72   ILE F CA  1 
ATOM   13228 C  C   . ILE F  2 45  ? -6.726  19.085  38.750  1.00 52.64 ?  72   ILE F C   1 
ATOM   13229 O  O   . ILE F  2 45  ? -7.026  20.264  38.545  1.00 52.69 ?  72   ILE F O   1 
ATOM   13230 C  CB  . ILE F  2 45  ? -4.262  18.579  39.317  1.00 51.89 ?  72   ILE F CB  1 
ATOM   13231 C  CG1 . ILE F  2 45  ? -3.847  19.810  38.501  1.00 51.96 ?  72   ILE F CG1 1 
ATOM   13232 C  CG2 . ILE F  2 45  ? -4.084  17.306  38.492  1.00 51.83 ?  72   ILE F CG2 1 
ATOM   13233 C  CD1 . ILE F  2 45  ? -3.836  21.108  39.288  1.00 52.09 ?  72   ILE F CD1 1 
ATOM   13234 N  N   . VAL F  2 46  ? -7.243  18.071  38.054  1.00 53.45 ?  73   VAL F N   1 
ATOM   13235 C  CA  . VAL F  2 46  ? -8.227  18.275  36.986  1.00 54.30 ?  73   VAL F CA  1 
ATOM   13236 C  C   . VAL F  2 46  ? -9.512  18.912  37.538  1.00 54.93 ?  73   VAL F C   1 
ATOM   13237 O  O   . VAL F  2 46  ? -10.107 19.779  36.894  1.00 54.97 ?  73   VAL F O   1 
ATOM   13238 C  CB  . VAL F  2 46  ? -8.542  16.954  36.218  1.00 54.31 ?  73   VAL F CB  1 
ATOM   13239 C  CG1 . VAL F  2 46  ? -9.583  17.187  35.123  1.00 54.27 ?  73   VAL F CG1 1 
ATOM   13240 C  CG2 . VAL F  2 46  ? -7.272  16.364  35.609  1.00 54.25 ?  73   VAL F CG2 1 
ATOM   13241 N  N   . ALA F  2 47  ? -9.914  18.489  38.737  1.00 55.74 ?  74   ALA F N   1 
ATOM   13242 C  CA  . ALA F  2 47  ? -11.081 19.052  39.421  1.00 56.62 ?  74   ALA F CA  1 
ATOM   13243 C  C   . ALA F  2 47  ? -10.889 20.527  39.780  1.00 57.24 ?  74   ALA F C   1 
ATOM   13244 O  O   . ALA F  2 47  ? -11.817 21.325  39.644  1.00 57.23 ?  74   ALA F O   1 
ATOM   13245 C  CB  . ALA F  2 47  ? -11.422 18.238  40.666  1.00 56.52 ?  74   ALA F CB  1 
ATOM   13246 N  N   . LEU F  2 48  ? -9.684  20.876  40.232  1.00 58.09 ?  75   LEU F N   1 
ATOM   13247 C  CA  . LEU F  2 48  ? -9.338  22.259  40.574  1.00 58.99 ?  75   LEU F CA  1 
ATOM   13248 C  C   . LEU F  2 48  ? -9.291  23.160  39.333  1.00 59.62 ?  75   LEU F C   1 
ATOM   13249 O  O   . LEU F  2 48  ? -9.623  24.345  39.403  1.00 59.72 ?  75   LEU F O   1 
ATOM   13250 C  CB  . LEU F  2 48  ? -8.000  22.305  41.330  1.00 58.97 ?  75   LEU F CB  1 
ATOM   13251 C  CG  . LEU F  2 48  ? -7.493  23.630  41.922  1.00 59.11 ?  75   LEU F CG  1 
ATOM   13252 C  CD1 . LEU F  2 48  ? -8.352  24.100  43.098  1.00 59.29 ?  75   LEU F CD1 1 
ATOM   13253 C  CD2 . LEU F  2 48  ? -6.038  23.503  42.347  1.00 59.04 ?  75   LEU F CD2 1 
ATOM   13254 N  N   . VAL F  2 49  ? -8.878  22.589  38.204  1.00 60.45 ?  76   VAL F N   1 
ATOM   13255 C  CA  . VAL F  2 49  ? -8.828  23.315  36.936  1.00 61.34 ?  76   VAL F CA  1 
ATOM   13256 C  C   . VAL F  2 49  ? -10.233 23.513  36.348  1.00 61.99 ?  76   VAL F C   1 
ATOM   13257 O  O   . VAL F  2 49  ? -10.580 24.620  35.922  1.00 62.03 ?  76   VAL F O   1 
ATOM   13258 C  CB  . VAL F  2 49  ? -7.885  22.619  35.913  1.00 61.29 ?  76   VAL F CB  1 
ATOM   13259 C  CG1 . VAL F  2 49  ? -8.025  23.231  34.522  1.00 61.28 ?  76   VAL F CG1 1 
ATOM   13260 C  CG2 . VAL F  2 49  ? -6.437  22.705  36.380  1.00 61.38 ?  76   VAL F CG2 1 
ATOM   13261 N  N   . GLN F  2 50  ? -11.033 22.445  36.347  1.00 62.78 ?  77   GLN F N   1 
ATOM   13262 C  CA  . GLN F  2 50  ? -12.374 22.465  35.748  1.00 63.67 ?  77   GLN F CA  1 
ATOM   13263 C  C   . GLN F  2 50  ? -13.352 23.432  36.421  1.00 64.19 ?  77   GLN F C   1 
ATOM   13264 O  O   . GLN F  2 50  ? -14.230 23.987  35.755  1.00 64.30 ?  77   GLN F O   1 
ATOM   13265 C  CB  . GLN F  2 50  ? -12.970 21.055  35.682  1.00 63.69 ?  77   GLN F CB  1 
ATOM   13266 C  CG  . GLN F  2 50  ? -12.446 20.221  34.516  1.00 64.03 ?  77   GLN F CG  1 
ATOM   13267 C  CD  . GLN F  2 50  ? -13.177 18.898  34.344  1.00 64.58 ?  77   GLN F CD  1 
ATOM   13268 O  OE1 . GLN F  2 50  ? -14.215 18.657  34.964  1.00 64.63 ?  77   GLN F OE1 1 
ATOM   13269 N  NE2 . GLN F  2 50  ? -12.637 18.034  33.490  1.00 64.69 ?  77   GLN F NE2 1 
ATOM   13270 N  N   . LYS F  2 51  ? -13.204 23.627  37.730  1.00 64.85 ?  78   LYS F N   1 
ATOM   13271 C  CA  . LYS F  2 51  ? -14.005 24.618  38.451  1.00 65.57 ?  78   LYS F CA  1 
ATOM   13272 C  C   . LYS F  2 51  ? -13.579 26.048  38.101  1.00 65.96 ?  78   LYS F C   1 
ATOM   13273 O  O   . LYS F  2 51  ? -14.407 26.962  38.091  1.00 66.07 ?  78   LYS F O   1 
ATOM   13274 C  CB  . LYS F  2 51  ? -13.969 24.382  39.971  1.00 65.58 ?  78   LYS F CB  1 
ATOM   13275 C  CG  . LYS F  2 51  ? -12.577 24.372  40.599  1.00 66.00 ?  78   LYS F CG  1 
ATOM   13276 C  CD  . LYS F  2 51  ? -12.621 24.177  42.116  1.00 66.57 ?  78   LYS F CD  1 
ATOM   13277 C  CE  . LYS F  2 51  ? -12.470 25.496  42.874  1.00 66.80 ?  78   LYS F CE  1 
ATOM   13278 N  NZ  . LYS F  2 51  ? -13.669 26.375  42.776  1.00 67.02 ?  78   LYS F NZ  1 
ATOM   13279 N  N   . ALA F  2 52  ? -12.291 26.226  37.803  1.00 66.47 ?  79   ALA F N   1 
ATOM   13280 C  CA  . ALA F  2 52  ? -11.741 27.529  37.429  1.00 66.94 ?  79   ALA F CA  1 
ATOM   13281 C  C   . ALA F  2 52  ? -12.095 27.918  35.992  1.00 67.33 ?  79   ALA F C   1 
ATOM   13282 O  O   . ALA F  2 52  ? -12.261 29.102  35.690  1.00 67.40 ?  79   ALA F O   1 
ATOM   13283 C  CB  . ALA F  2 52  ? -10.233 27.551  37.637  1.00 66.93 ?  79   ALA F CB  1 
ATOM   13284 N  N   . ARG F  2 53  ? -12.202 26.921  35.112  1.00 67.82 ?  80   ARG F N   1 
ATOM   13285 C  CA  . ARG F  2 53  ? -12.661 27.135  33.736  1.00 68.35 ?  80   ARG F CA  1 
ATOM   13286 C  C   . ARG F  2 53  ? -14.134 27.546  33.722  1.00 68.66 ?  80   ARG F C   1 
ATOM   13287 O  O   . ARG F  2 53  ? -14.552 28.355  32.890  1.00 68.68 ?  80   ARG F O   1 
ATOM   13288 C  CB  . ARG F  2 53  ? -12.466 25.870  32.890  1.00 68.34 ?  80   ARG F CB  1 
ATOM   13289 C  CG  . ARG F  2 53  ? -11.014 25.445  32.675  1.00 68.66 ?  80   ARG F CG  1 
ATOM   13290 C  CD  . ARG F  2 53  ? -10.399 26.069  31.427  1.00 69.12 ?  80   ARG F CD  1 
ATOM   13291 N  NE  . ARG F  2 53  ? -9.096  25.477  31.119  1.00 69.51 ?  80   ARG F NE  1 
ATOM   13292 C  CZ  . ARG F  2 53  ? -7.919  26.042  31.383  1.00 69.59 ?  80   ARG F CZ  1 
ATOM   13293 N  NH1 . ARG F  2 53  ? -7.853  27.238  31.957  1.00 69.60 ?  80   ARG F NH1 1 
ATOM   13294 N  NH2 . ARG F  2 53  ? -6.798  25.409  31.063  1.00 69.45 ?  80   ARG F NH2 1 
ATOM   13295 N  N   . GLU F  2 54  ? -14.904 26.979  34.650  1.00 69.09 ?  81   GLU F N   1 
ATOM   13296 C  CA  . GLU F  2 54  ? -16.318 27.311  34.839  1.00 69.57 ?  81   GLU F CA  1 
ATOM   13297 C  C   . GLU F  2 54  ? -16.503 28.761  35.295  1.00 69.76 ?  81   GLU F C   1 
ATOM   13298 O  O   . GLU F  2 54  ? -17.426 29.447  34.848  1.00 69.85 ?  81   GLU F O   1 
ATOM   13299 C  CB  . GLU F  2 54  ? -16.950 26.351  35.856  1.00 69.64 ?  81   GLU F CB  1 
ATOM   13300 C  CG  . GLU F  2 54  ? -18.467 26.463  35.990  1.00 70.06 ?  81   GLU F CG  1 
ATOM   13301 C  CD  . GLU F  2 54  ? -19.010 25.717  37.198  1.00 70.68 ?  81   GLU F CD  1 
ATOM   13302 O  OE1 . GLU F  2 54  ? -18.471 24.642  37.540  1.00 70.98 ?  81   GLU F OE1 1 
ATOM   13303 O  OE2 . GLU F  2 54  ? -19.986 26.208  37.807  1.00 70.98 ?  81   GLU F OE2 1 
ATOM   13304 N  N   . GLN F  2 55  ? -15.617 29.218  36.180  1.00 69.97 ?  82   GLN F N   1 
ATOM   13305 C  CA  . GLN F  2 55  ? -15.653 30.587  36.702  1.00 70.13 ?  82   GLN F CA  1 
ATOM   13306 C  C   . GLN F  2 55  ? -15.129 31.629  35.704  1.00 70.21 ?  82   GLN F C   1 
ATOM   13307 O  O   . GLN F  2 55  ? -15.247 32.834  35.940  1.00 70.22 ?  82   GLN F O   1 
ATOM   13308 C  CB  . GLN F  2 55  ? -14.873 30.679  38.018  1.00 70.14 ?  82   GLN F CB  1 
ATOM   13309 C  CG  . GLN F  2 55  ? -15.540 29.977  39.194  1.00 70.26 ?  82   GLN F CG  1 
ATOM   13310 C  CD  . GLN F  2 55  ? -14.727 30.067  40.474  1.00 70.63 ?  82   GLN F CD  1 
ATOM   13311 O  OE1 . GLN F  2 55  ? -14.252 31.141  40.854  1.00 70.56 ?  82   GLN F OE1 1 
ATOM   13312 N  NE2 . GLN F  2 55  ? -14.569 28.936  41.154  1.00 70.54 ?  82   GLN F NE2 1 
ATOM   13313 N  N   . SER F  2 56  ? -14.555 31.160  34.596  1.00 70.30 ?  83   SER F N   1 
ATOM   13314 C  CA  . SER F  2 56  ? -14.025 32.042  33.554  1.00 70.41 ?  83   SER F CA  1 
ATOM   13315 C  C   . SER F  2 56  ? -15.138 32.627  32.685  1.00 70.43 ?  83   SER F C   1 
ATOM   13316 O  O   . SER F  2 56  ? -16.059 31.920  32.274  1.00 70.48 ?  83   SER F O   1 
ATOM   13317 C  CB  . SER F  2 56  ? -13.007 31.300  32.682  1.00 70.42 ?  83   SER F CB  1 
ATOM   13318 O  OG  . SER F  2 56  ? -11.918 30.824  33.457  1.00 70.44 ?  83   SER F OG  1 
HETATM 13319 FE FE  . HEC G  3 .   ? 48.814  52.930  13.072  1.00 22.57 ?  601  HEC A FE  1 
HETATM 13320 C  CHA . HEC G  3 .   ? 47.774  53.339  9.812   1.00 22.11 ?  601  HEC A CHA 1 
HETATM 13321 C  CHB . HEC G  3 .   ? 52.061  53.163  12.071  1.00 22.65 ?  601  HEC A CHB 1 
HETATM 13322 C  CHC . HEC G  3 .   ? 49.857  52.887  16.368  1.00 21.47 ?  601  HEC A CHC 1 
HETATM 13323 C  CHD . HEC G  3 .   ? 45.585  52.420  14.094  1.00 20.69 ?  601  HEC A CHD 1 
HETATM 13324 N  NA  . HEC G  3 .   ? 49.735  53.183  11.271  1.00 22.63 ?  601  HEC A NA  1 
HETATM 13325 C  C1A . HEC G  3 .   ? 49.130  53.348  10.042  1.00 22.98 ?  601  HEC A C1A 1 
HETATM 13326 C  C2A . HEC G  3 .   ? 50.172  53.532  9.050   1.00 23.32 ?  601  HEC A C2A 1 
HETATM 13327 C  C3A . HEC G  3 .   ? 51.345  53.480  9.687   1.00 23.13 ?  601  HEC A C3A 1 
HETATM 13328 C  C4A . HEC G  3 .   ? 51.100  53.259  11.089  1.00 22.65 ?  601  HEC A C4A 1 
HETATM 13329 C  CMA . HEC G  3 .   ? 52.734  53.625  9.040   1.00 23.22 ?  601  HEC A CMA 1 
HETATM 13330 C  CAA . HEC G  3 .   ? 49.969  53.767  7.535   1.00 22.55 ?  601  HEC A CAA 1 
HETATM 13331 C  CBA . HEC G  3 .   ? 49.802  52.456  6.786   1.00 23.44 ?  601  HEC A CBA 1 
HETATM 13332 C  CGA . HEC G  3 .   ? 48.980  52.660  5.539   1.00 23.21 ?  601  HEC A CGA 1 
HETATM 13333 O  O1A . HEC G  3 .   ? 49.388  52.161  4.458   1.00 23.71 ?  601  HEC A O1A 1 
HETATM 13334 O  O2A . HEC G  3 .   ? 47.911  53.312  5.624   1.00 23.04 ?  601  HEC A O2A 1 
HETATM 13335 N  NB  . HEC G  3 .   ? 50.644  52.967  14.055  1.00 22.01 ?  601  HEC A NB  1 
HETATM 13336 C  C1B . HEC G  3 .   ? 51.849  53.206  13.432  1.00 21.96 ?  601  HEC A C1B 1 
HETATM 13337 C  C2B . HEC G  3 .   ? 52.836  53.482  14.455  1.00 21.70 ?  601  HEC A C2B 1 
HETATM 13338 C  C3B . HEC G  3 .   ? 52.227  53.406  15.647  1.00 21.59 ?  601  HEC A C3B 1 
HETATM 13339 C  C4B . HEC G  3 .   ? 50.835  53.071  15.415  1.00 21.70 ?  601  HEC A C4B 1 
HETATM 13340 C  CMB . HEC G  3 .   ? 54.322  53.818  14.181  1.00 21.01 ?  601  HEC A CMB 1 
HETATM 13341 C  CAB . HEC G  3 .   ? 52.876  53.629  17.039  1.00 21.64 ?  601  HEC A CAB 1 
HETATM 13342 C  CBB . HEC G  3 .   ? 53.105  54.875  17.467  1.00 21.23 ?  601  HEC A CBB 1 
HETATM 13343 N  NC  . HEC G  3 .   ? 47.898  52.714  14.890  1.00 21.64 ?  601  HEC A NC  1 
HETATM 13344 C  C1C . HEC G  3 .   ? 48.513  52.678  16.127  1.00 21.53 ?  601  HEC A C1C 1 
HETATM 13345 C  C2C . HEC G  3 .   ? 47.495  52.394  17.123  1.00 20.92 ?  601  HEC A C2C 1 
HETATM 13346 C  C3C . HEC G  3 .   ? 46.321  52.271  16.491  1.00 20.74 ?  601  HEC A C3C 1 
HETATM 13347 C  C4C . HEC G  3 .   ? 46.549  52.471  15.075  1.00 21.61 ?  601  HEC A C4C 1 
HETATM 13348 C  CMC . HEC G  3 .   ? 47.742  52.260  18.644  1.00 20.89 ?  601  HEC A CMC 1 
HETATM 13349 C  CAC . HEC G  3 .   ? 44.950  51.965  17.135  1.00 20.85 ?  601  HEC A CAC 1 
HETATM 13350 C  CBC . HEC G  3 .   ? 44.457  52.814  18.050  1.00 21.07 ?  601  HEC A CBC 1 
HETATM 13351 N  ND  . HEC G  3 .   ? 46.968  52.840  12.095  1.00 21.44 ?  601  HEC A ND  1 
HETATM 13352 C  C1D . HEC G  3 .   ? 45.748  52.732  12.762  1.00 21.55 ?  601  HEC A C1D 1 
HETATM 13353 C  C2D . HEC G  3 .   ? 44.672  53.003  11.825  1.00 20.73 ?  601  HEC A C2D 1 
HETATM 13354 C  C3D . HEC G  3 .   ? 45.366  53.282  10.492  1.00 21.01 ?  601  HEC A C3D 1 
HETATM 13355 C  C4D . HEC G  3 .   ? 46.783  53.166  10.754  1.00 21.85 ?  601  HEC A C4D 1 
HETATM 13356 C  CMD . HEC G  3 .   ? 43.150  53.008  12.091  1.00 19.92 ?  601  HEC A CMD 1 
HETATM 13357 C  CAD . HEC G  3 .   ? 44.698  53.660  9.154   1.00 20.22 ?  601  HEC A CAD 1 
HETATM 13358 C  CBD . HEC G  3 .   ? 44.740  55.186  9.152   1.00 20.07 ?  601  HEC A CBD 1 
HETATM 13359 C  CGD . HEC G  3 .   ? 44.249  55.819  7.878   1.00 20.37 ?  601  HEC A CGD 1 
HETATM 13360 O  O1D . HEC G  3 .   ? 43.831  55.095  6.931   1.00 20.73 ?  601  HEC A O1D 1 
HETATM 13361 O  O2D . HEC G  3 .   ? 44.269  57.074  7.827   1.00 19.45 ?  601  HEC A O2D 1 
HETATM 13362 FE FE  . HEC H  3 .   ? 55.919  49.940  8.564   1.00 23.56 ?  602  HEC A FE  1 
HETATM 13363 C  CHA . HEC H  3 .   ? 53.863  49.754  5.851   1.00 23.88 ?  602  HEC A CHA 1 
HETATM 13364 C  CHB . HEC H  3 .   ? 53.248  49.698  10.647  1.00 22.88 ?  602  HEC A CHB 1 
HETATM 13365 C  CHC . HEC H  3 .   ? 58.048  49.407  11.206  1.00 22.75 ?  602  HEC A CHC 1 
HETATM 13366 C  CHD . HEC H  3 .   ? 58.549  50.959  6.648   1.00 24.00 ?  602  HEC A CHD 1 
HETATM 13367 N  NA  . HEC H  3 .   ? 53.904  49.758  8.292   1.00 23.81 ?  602  HEC A NA  1 
HETATM 13368 C  C1A . HEC H  3 .   ? 53.246  49.685  7.082   1.00 23.85 ?  602  HEC A C1A 1 
HETATM 13369 C  C2A . HEC H  3 .   ? 51.827  49.527  7.353   1.00 23.74 ?  602  HEC A C2A 1 
HETATM 13370 C  C3A . HEC H  3 .   ? 51.662  49.517  8.685   1.00 23.58 ?  602  HEC A C3A 1 
HETATM 13371 C  C4A . HEC H  3 .   ? 52.968  49.662  9.299   1.00 23.22 ?  602  HEC A C4A 1 
HETATM 13372 C  CMA . HEC H  3 .   ? 50.330  49.374  9.460   1.00 23.34 ?  602  HEC A CMA 1 
HETATM 13373 C  CAA . HEC H  3 .   ? 50.717  49.401  6.278   1.00 23.73 ?  602  HEC A CAA 1 
HETATM 13374 C  CBA . HEC H  3 .   ? 50.704  47.991  5.704   1.00 23.26 ?  602  HEC A CBA 1 
HETATM 13375 C  CGA . HEC H  3 .   ? 49.513  47.805  4.795   1.00 23.96 ?  602  HEC A CGA 1 
HETATM 13376 O  O1A . HEC H  3 .   ? 49.702  47.765  3.549   1.00 23.64 ?  602  HEC A O1A 1 
HETATM 13377 O  O2A . HEC H  3 .   ? 48.373  47.692  5.313   1.00 22.95 ?  602  HEC A O2A 1 
HETATM 13378 N  NB  . HEC H  3 .   ? 55.695  49.620  10.564  1.00 22.85 ?  602  HEC A NB  1 
HETATM 13379 C  C1B . HEC H  3 .   ? 54.488  49.538  11.225  1.00 22.65 ?  602  HEC A C1B 1 
HETATM 13380 C  C2B . HEC H  3 .   ? 54.762  49.263  12.623  1.00 22.96 ?  602  HEC A C2B 1 
HETATM 13381 C  C3B . HEC H  3 .   ? 56.093  49.183  12.777  1.00 22.81 ?  602  HEC A C3B 1 
HETATM 13382 C  C4B . HEC H  3 .   ? 56.702  49.404  11.481  1.00 22.90 ?  602  HEC A C4B 1 
HETATM 13383 C  CMB . HEC H  3 .   ? 53.688  49.096  13.723  1.00 22.52 ?  602  HEC A CMB 1 
HETATM 13384 C  CAB . HEC H  3 .   ? 56.870  48.902  14.084  1.00 22.36 ?  602  HEC A CAB 1 
HETATM 13385 C  CBB . HEC H  3 .   ? 56.766  47.712  14.693  1.00 22.16 ?  602  HEC A CBB 1 
HETATM 13386 N  NC  . HEC H  3 .   ? 57.940  50.128  8.870   1.00 23.64 ?  602  HEC A NC  1 
HETATM 13387 C  C1C . HEC H  3 .   ? 58.619  49.893  10.051  1.00 23.74 ?  602  HEC A C1C 1 
HETATM 13388 C  C2C . HEC H  3 .   ? 60.013  50.237  9.854   1.00 23.24 ?  602  HEC A C2C 1 
HETATM 13389 C  C3C . HEC H  3 .   ? 60.150  50.661  8.592   1.00 23.84 ?  602  HEC A C3C 1 
HETATM 13390 C  C4C . HEC H  3 .   ? 58.845  50.606  7.950   1.00 24.32 ?  602  HEC A C4C 1 
HETATM 13391 C  CMC . HEC H  3 .   ? 61.130  50.126  10.923  1.00 22.62 ?  602  HEC A CMC 1 
HETATM 13392 C  CAC . HEC H  3 .   ? 61.460  51.149  7.923   1.00 24.59 ?  602  HEC A CAC 1 
HETATM 13393 C  CBC . HEC H  3 .   ? 62.400  50.271  7.550   1.00 24.74 ?  602  HEC A CBC 1 
HETATM 13394 N  ND  . HEC H  3 .   ? 56.179  50.251  6.527   1.00 23.56 ?  602  HEC A ND  1 
HETATM 13395 C  C1D . HEC H  3 .   ? 57.340  50.807  5.997   1.00 23.81 ?  602  HEC A C1D 1 
HETATM 13396 C  C2D . HEC H  3 .   ? 57.067  51.213  4.636   1.00 23.94 ?  602  HEC A C2D 1 
HETATM 13397 C  C3D . HEC H  3 .   ? 55.600  50.844  4.375   1.00 24.05 ?  602  HEC A C3D 1 
HETATM 13398 C  C4D . HEC H  3 .   ? 55.133  50.246  5.611   1.00 23.95 ?  602  HEC A C4D 1 
HETATM 13399 C  CMD . HEC H  3 .   ? 58.052  51.882  3.659   1.00 23.65 ?  602  HEC A CMD 1 
HETATM 13400 C  CAD . HEC H  3 .   ? 54.799  51.064  3.073   1.00 23.88 ?  602  HEC A CAD 1 
HETATM 13401 C  CBD . HEC H  3 .   ? 54.168  52.455  3.076   1.00 23.54 ?  602  HEC A CBD 1 
HETATM 13402 C  CGD . HEC H  3 .   ? 52.871  52.459  3.852   1.00 24.42 ?  602  HEC A CGD 1 
HETATM 13403 O  O1D . HEC H  3 .   ? 52.776  53.180  4.884   1.00 23.22 ?  602  HEC A O1D 1 
HETATM 13404 O  O2D . HEC H  3 .   ? 51.919  51.749  3.434   1.00 24.54 ?  602  HEC A O2D 1 
HETATM 13405 FE FE  . HEC I  3 .   ? 65.857  34.283  16.379  1.00 24.39 ?  603  HEC A FE  1 
HETATM 13406 C  CHA . HEC I  3 .   ? 63.994  33.999  19.237  1.00 23.42 ?  603  HEC A CHA 1 
HETATM 13407 C  CHB . HEC I  3 .   ? 64.714  37.469  15.939  1.00 23.42 ?  603  HEC A CHB 1 
HETATM 13408 C  CHC . HEC I  3 .   ? 68.143  34.709  13.893  1.00 24.31 ?  603  HEC A CHC 1 
HETATM 13409 C  CHD . HEC I  3 .   ? 66.477  30.889  16.369  1.00 24.18 ?  603  HEC A CHD 1 
HETATM 13410 N  NA  . HEC I  3 .   ? 64.586  35.511  17.414  1.00 23.64 ?  603  HEC A NA  1 
HETATM 13411 C  C1A . HEC I  3 .   ? 63.914  35.203  18.576  1.00 23.54 ?  603  HEC A C1A 1 
HETATM 13412 C  C2A . HEC I  3 .   ? 63.120  36.358  18.954  1.00 23.54 ?  603  HEC A C2A 1 
HETATM 13413 C  C3A . HEC I  3 .   ? 63.324  37.311  18.040  1.00 23.62 ?  603  HEC A C3A 1 
HETATM 13414 C  C4A . HEC I  3 .   ? 64.245  36.797  17.048  1.00 23.85 ?  603  HEC A C4A 1 
HETATM 13415 C  CMA . HEC I  3 .   ? 62.697  38.722  18.022  1.00 23.00 ?  603  HEC A CMA 1 
HETATM 13416 C  CAA . HEC I  3 .   ? 62.211  36.474  20.201  1.00 23.31 ?  603  HEC A CAA 1 
HETATM 13417 C  CBA . HEC I  3 .   ? 63.100  36.631  21.430  1.00 22.79 ?  603  HEC A CBA 1 
HETATM 13418 C  CGA . HEC I  3 .   ? 62.293  36.729  22.697  1.00 22.84 ?  603  HEC A CGA 1 
HETATM 13419 O  O1A . HEC I  3 .   ? 61.175  36.150  22.776  1.00 22.32 ?  603  HEC A O1A 1 
HETATM 13420 O  O2A . HEC I  3 .   ? 62.788  37.392  23.645  1.00 23.32 ?  603  HEC A O2A 1 
HETATM 13421 N  NB  . HEC I  3 .   ? 66.324  35.808  15.134  1.00 23.68 ?  603  HEC A NB  1 
HETATM 13422 C  C1B . HEC I  3 .   ? 65.761  37.066  15.138  1.00 23.79 ?  603  HEC A C1B 1 
HETATM 13423 C  C2B . HEC I  3 .   ? 66.457  37.873  14.152  1.00 24.04 ?  603  HEC A C2B 1 
HETATM 13424 C  C3B . HEC I  3 .   ? 67.407  37.107  13.591  1.00 24.67 ?  603  HEC A C3B 1 
HETATM 13425 C  C4B . HEC I  3 .   ? 67.338  35.790  14.193  1.00 24.66 ?  603  HEC A C4B 1 
HETATM 13426 C  CMB . HEC I  3 .   ? 66.145  39.356  13.834  1.00 23.04 ?  603  HEC A CMB 1 
HETATM 13427 C  CAB . HEC I  3 .   ? 68.412  37.524  12.493  1.00 24.99 ?  603  HEC A CAB 1 
HETATM 13428 C  CBB . HEC I  3 .   ? 69.376  38.409  12.780  1.00 25.34 ?  603  HEC A CBB 1 
HETATM 13429 N  NC  . HEC I  3 .   ? 67.109  33.025  15.339  1.00 24.10 ?  603  HEC A NC  1 
HETATM 13430 C  C1C . HEC I  3 .   ? 67.938  33.409  14.307  1.00 24.35 ?  603  HEC A C1C 1 
HETATM 13431 C  C2C . HEC I  3 .   ? 68.547  32.213  13.752  1.00 25.15 ?  603  HEC A C2C 1 
HETATM 13432 C  C3C . HEC I  3 .   ? 68.084  31.149  14.436  1.00 25.00 ?  603  HEC A C3C 1 
HETATM 13433 C  C4C . HEC I  3 .   ? 67.168  31.649  15.448  1.00 24.90 ?  603  HEC A C4C 1 
HETATM 13434 C  CMC . HEC I  3 .   ? 69.548  32.210  12.571  1.00 24.46 ?  603  HEC A CMC 1 
HETATM 13435 C  CAC . HEC I  3 .   ? 68.411  29.646  14.215  1.00 25.94 ?  603  HEC A CAC 1 
HETATM 13436 C  CBC . HEC I  3 .   ? 69.648  29.209  13.928  1.00 26.21 ?  603  HEC A CBC 1 
HETATM 13437 N  ND  . HEC I  3 .   ? 65.336  32.687  17.627  1.00 23.56 ?  603  HEC A ND  1 
HETATM 13438 C  C1D . HEC I  3 .   ? 65.681  31.357  17.398  1.00 24.29 ?  603  HEC A C1D 1 
HETATM 13439 C  C2D . HEC I  3 .   ? 65.070  30.533  18.422  1.00 23.86 ?  603  HEC A C2D 1 
HETATM 13440 C  C3D . HEC I  3 .   ? 64.300  31.507  19.318  1.00 24.09 ?  603  HEC A C3D 1 
HETATM 13441 C  C4D . HEC I  3 .   ? 64.513  32.818  18.743  1.00 24.15 ?  603  HEC A C4D 1 
HETATM 13442 C  CMD . HEC I  3 .   ? 65.174  28.999  18.592  1.00 23.63 ?  603  HEC A CMD 1 
HETATM 13443 C  CAD . HEC I  3 .   ? 63.457  31.147  20.558  1.00 24.41 ?  603  HEC A CAD 1 
HETATM 13444 C  CBD . HEC I  3 .   ? 64.131  31.585  21.851  1.00 24.93 ?  603  HEC A CBD 1 
HETATM 13445 C  CGD . HEC I  3 .   ? 63.181  31.324  22.994  1.00 25.59 ?  603  HEC A CGD 1 
HETATM 13446 O  O1D . HEC I  3 .   ? 63.648  30.929  24.089  1.00 26.41 ?  603  HEC A O1D 1 
HETATM 13447 O  O2D . HEC I  3 .   ? 61.951  31.511  22.819  1.00 26.00 ?  603  HEC A O2D 1 
HETATM 13448 FE FE  . HEC J  3 .   ? 58.901  40.510  15.109  1.00 22.37 ?  604  HEC A FE  1 
HETATM 13449 C  CHA . HEC J  3 .   ? 57.902  40.351  18.398  1.00 20.64 ?  604  HEC A CHA 1 
HETATM 13450 C  CHB . HEC J  3 .   ? 60.022  37.270  15.308  1.00 21.24 ?  604  HEC A CHB 1 
HETATM 13451 C  CHC . HEC J  3 .   ? 59.765  40.634  11.805  1.00 22.10 ?  604  HEC A CHC 1 
HETATM 13452 C  CHD . HEC J  3 .   ? 57.917  43.832  14.914  1.00 21.22 ?  604  HEC A CHD 1 
HETATM 13453 N  NA  . HEC J  3 .   ? 58.952  39.061  16.595  1.00 21.55 ?  604  HEC A NA  1 
HETATM 13454 C  C1A . HEC J  3 .   ? 58.494  39.206  17.898  1.00 21.00 ?  604  HEC A C1A 1 
HETATM 13455 C  C2A . HEC J  3 .   ? 58.742  37.952  18.604  1.00 20.35 ?  604  HEC A C2A 1 
HETATM 13456 C  C3A . HEC J  3 .   ? 59.324  37.113  17.732  1.00 20.36 ?  604  HEC A C3A 1 
HETATM 13457 C  C4A . HEC J  3 .   ? 59.468  37.791  16.459  1.00 21.18 ?  604  HEC A C4A 1 
HETATM 13458 C  CMA . HEC J  3 .   ? 59.772  35.660  18.016  1.00 20.31 ?  604  HEC A CMA 1 
HETATM 13459 C  CAA . HEC J  3 .   ? 58.428  37.607  20.091  1.00 19.16 ?  604  HEC A CAA 1 
HETATM 13460 C  CBA . HEC J  3 .   ? 56.961  37.804  20.479  1.00 18.40 ?  604  HEC A CBA 1 
HETATM 13461 C  CGA . HEC J  3 .   ? 56.097  36.747  19.844  1.00 18.28 ?  604  HEC A CGA 1 
HETATM 13462 O  O1A . HEC J  3 .   ? 56.635  35.681  19.451  1.00 16.70 ?  604  HEC A O1A 1 
HETATM 13463 O  O2A . HEC J  3 .   ? 54.862  36.976  19.731  1.00 19.41 ?  604  HEC A O2A 1 
HETATM 13464 N  NB  . HEC J  3 .   ? 59.742  39.210  13.820  1.00 21.77 ?  604  HEC A NB  1 
HETATM 13465 C  C1B . HEC J  3 .   ? 60.119  37.909  14.090  1.00 21.81 ?  604  HEC A C1B 1 
HETATM 13466 C  C2B . HEC J  3 .   ? 60.622  37.332  12.859  1.00 21.95 ?  604  HEC A C2B 1 
HETATM 13467 C  C3B . HEC J  3 .   ? 60.551  38.258  11.900  1.00 22.19 ?  604  HEC A C3B 1 
HETATM 13468 C  C4B . HEC J  3 .   ? 59.997  39.459  12.482  1.00 22.00 ?  604  HEC A C4B 1 
HETATM 13469 C  CMB . HEC J  3 .   ? 61.152  35.893  12.701  1.00 22.52 ?  604  HEC A CMB 1 
HETATM 13470 C  CAB . HEC J  3 .   ? 60.965  38.093  10.419  1.00 23.28 ?  604  HEC A CAB 1 
HETATM 13471 C  CBB . HEC J  3 .   ? 60.167  37.393  9.602   1.00 22.39 ?  604  HEC A CBB 1 
HETATM 13472 N  NC  . HEC J  3 .   ? 58.809  41.970  13.616  1.00 21.45 ?  604  HEC A NC  1 
HETATM 13473 C  C1C . HEC J  3 .   ? 59.326  41.818  12.347  1.00 21.93 ?  604  HEC A C1C 1 
HETATM 13474 C  C2C . HEC J  3 .   ? 59.322  43.113  11.694  1.00 21.99 ?  604  HEC A C2C 1 
HETATM 13475 C  C3C . HEC J  3 .   ? 58.816  44.008  12.550  1.00 21.86 ?  604  HEC A C3C 1 
HETATM 13476 C  C4C . HEC J  3 .   ? 58.482  43.300  13.777  1.00 21.52 ?  604  HEC A C4C 1 
HETATM 13477 C  CMC . HEC J  3 .   ? 59.821  43.386  10.257  1.00 22.38 ?  604  HEC A CMC 1 
HETATM 13478 C  CAC . HEC J  3 .   ? 58.639  45.530  12.277  1.00 22.91 ?  604  HEC A CAC 1 
HETATM 13479 C  CBC . HEC J  3 .   ? 57.725  45.959  11.393  1.00 21.86 ?  604  HEC A CBC 1 
HETATM 13480 N  ND  . HEC J  3 .   ? 58.053  41.886  16.452  1.00 21.33 ?  604  HEC A ND  1 
HETATM 13481 C  C1D . HEC J  3 .   ? 57.664  43.184  16.108  1.00 21.22 ?  604  HEC A C1D 1 
HETATM 13482 C  C2D . HEC J  3 .   ? 56.952  43.765  17.226  1.00 21.17 ?  604  HEC A C2D 1 
HETATM 13483 C  C3D . HEC J  3 .   ? 56.952  42.682  18.308  1.00 21.23 ?  604  HEC A C3D 1 
HETATM 13484 C  C4D . HEC J  3 .   ? 57.659  41.547  17.744  1.00 20.84 ?  604  HEC A C4D 1 
HETATM 13485 C  CMD . HEC J  3 .   ? 56.321  45.173  17.323  1.00 20.98 ?  604  HEC A CMD 1 
HETATM 13486 C  CAD . HEC J  3 .   ? 56.312  42.790  19.709  1.00 21.91 ?  604  HEC A CAD 1 
HETATM 13487 C  CBD . HEC J  3 .   ? 57.288  43.480  20.655  1.00 21.74 ?  604  HEC A CBD 1 
HETATM 13488 C  CGD . HEC J  3 .   ? 56.765  43.440  22.067  1.00 21.33 ?  604  HEC A CGD 1 
HETATM 13489 O  O1D . HEC J  3 .   ? 55.732  42.774  22.330  1.00 21.40 ?  604  HEC A O1D 1 
HETATM 13490 O  O2D . HEC J  3 .   ? 57.391  44.083  22.943  1.00 22.00 ?  604  HEC A O2D 1 
HETATM 13491 FE FE  . HEC K  3 .   ? 33.466  56.467  20.480  1.00 19.94 ?  605  HEC A FE  1 
HETATM 13492 C  CHA . HEC K  3 .   ? 33.510  58.536  23.196  1.00 19.72 ?  605  HEC A CHA 1 
HETATM 13493 C  CHB . HEC K  3 .   ? 35.938  54.585  21.802  1.00 19.35 ?  605  HEC A CHB 1 
HETATM 13494 C  CHC . HEC K  3 .   ? 32.776  54.025  18.174  1.00 18.72 ?  605  HEC A CHC 1 
HETATM 13495 C  CHD . HEC K  3 .   ? 31.691  58.717  18.655  1.00 19.08 ?  605  HEC A CHD 1 
HETATM 13496 N  NA  . HEC K  3 .   ? 34.494  56.512  22.245  1.00 19.78 ?  605  HEC A NA  1 
HETATM 13497 C  C1A . HEC K  3 .   ? 34.480  57.553  23.149  1.00 20.12 ?  605  HEC A C1A 1 
HETATM 13498 C  C2A . HEC K  3 .   ? 35.642  57.412  24.006  1.00 20.19 ?  605  HEC A C2A 1 
HETATM 13499 C  C3A . HEC K  3 .   ? 36.308  56.314  23.614  1.00 19.87 ?  605  HEC A C3A 1 
HETATM 13500 C  C4A . HEC K  3 .   ? 35.594  55.725  22.501  1.00 20.04 ?  605  HEC A C4A 1 
HETATM 13501 C  CMA . HEC K  3 .   ? 37.611  55.737  24.218  1.00 19.47 ?  605  HEC A CMA 1 
HETATM 13502 C  CAA . HEC K  3 .   ? 36.017  58.381  25.159  1.00 20.90 ?  605  HEC A CAA 1 
HETATM 13503 C  CBA . HEC K  3 .   ? 36.788  59.582  24.595  1.00 21.64 ?  605  HEC A CBA 1 
HETATM 13504 C  CGA . HEC K  3 .   ? 35.893  60.746  24.230  1.00 22.39 ?  605  HEC A CGA 1 
HETATM 13505 O  O1A . HEC K  3 .   ? 35.949  61.192  23.052  1.00 22.33 ?  605  HEC A O1A 1 
HETATM 13506 O  O2A . HEC K  3 .   ? 35.131  61.241  25.107  1.00 22.03 ?  605  HEC A O2A 1 
HETATM 13507 N  NB  . HEC K  3 .   ? 34.234  54.638  20.040  1.00 19.24 ?  605  HEC A NB  1 
HETATM 13508 C  C1B . HEC K  3 .   ? 35.216  54.012  20.775  1.00 19.09 ?  605  HEC A C1B 1 
HETATM 13509 C  C2B . HEC K  3 .   ? 35.339  52.656  20.280  1.00 19.05 ?  605  HEC A C2B 1 
HETATM 13510 C  C3B . HEC K  3 .   ? 34.461  52.494  19.279  1.00 18.99 ?  605  HEC A C3B 1 
HETATM 13511 C  C4B . HEC K  3 .   ? 33.754  53.747  19.101  1.00 18.99 ?  605  HEC A C4B 1 
HETATM 13512 C  CMB . HEC K  3 .   ? 36.324  51.603  20.834  1.00 19.07 ?  605  HEC A CMB 1 
HETATM 13513 C  CAB . HEC K  3 .   ? 34.222  51.211  18.447  1.00 18.94 ?  605  HEC A CAB 1 
HETATM 13514 C  CBB . HEC K  3 .   ? 33.903  50.062  19.061  1.00 18.12 ?  605  HEC A CBB 1 
HETATM 13515 N  NC  . HEC K  3 .   ? 32.369  56.381  18.730  1.00 19.12 ?  605  HEC A NC  1 
HETATM 13516 C  C1C . HEC K  3 .   ? 32.345  55.305  17.863  1.00 20.15 ?  605  HEC A C1C 1 
HETATM 13517 C  C2C . HEC K  3 .   ? 31.802  55.774  16.604  1.00 19.66 ?  605  HEC A C2C 1 
HETATM 13518 C  C3C . HEC K  3 .   ? 31.504  57.074  16.732  1.00 19.70 ?  605  HEC A C3C 1 
HETATM 13519 C  C4C . HEC K  3 .   ? 31.849  57.474  18.083  1.00 19.50 ?  605  HEC A C4C 1 
HETATM 13520 C  CMC . HEC K  3 .   ? 31.601  54.912  15.344  1.00 19.05 ?  605  HEC A CMC 1 
HETATM 13521 C  CAC . HEC K  3 .   ? 30.914  57.988  15.624  1.00 20.15 ?  605  HEC A CAC 1 
HETATM 13522 C  CBC . HEC K  3 .   ? 29.624  57.851  15.292  1.00 19.80 ?  605  HEC A CBC 1 
HETATM 13523 N  ND  . HEC K  3 .   ? 32.722  58.364  20.871  1.00 19.27 ?  605  HEC A ND  1 
HETATM 13524 C  C1D . HEC K  3 .   ? 31.913  59.060  19.976  1.00 19.24 ?  605  HEC A C1D 1 
HETATM 13525 C  C2D . HEC K  3 .   ? 31.362  60.215  20.661  1.00 19.06 ?  605  HEC A C2D 1 
HETATM 13526 C  C3D . HEC K  3 .   ? 31.930  60.151  22.086  1.00 19.33 ?  605  HEC A C3D 1 
HETATM 13527 C  C4D . HEC K  3 .   ? 32.776  58.980  22.116  1.00 19.75 ?  605  HEC A C4D 1 
HETATM 13528 C  CMD . HEC K  3 .   ? 30.397  61.284  20.090  1.00 17.99 ?  605  HEC A CMD 1 
HETATM 13529 C  CAD . HEC K  3 .   ? 31.680  61.147  23.236  1.00 20.09 ?  605  HEC A CAD 1 
HETATM 13530 C  CBD . HEC K  3 .   ? 32.526  62.379  22.928  1.00 21.38 ?  605  HEC A CBD 1 
HETATM 13531 C  CGD . HEC K  3 .   ? 32.515  63.315  24.101  1.00 22.72 ?  605  HEC A CGD 1 
HETATM 13532 O  O1D . HEC K  3 .   ? 33.443  63.218  24.940  1.00 23.69 ?  605  HEC A O1D 1 
HETATM 13533 O  O2D . HEC K  3 .   ? 31.580  64.154  24.196  1.00 23.78 ?  605  HEC A O2D 1 
HETATM 13534 FE FE  . HEC L  3 .   ? 42.295  53.330  22.918  1.00 20.58 ?  606  HEC A FE  1 
HETATM 13535 C  CHA . HEC L  3 .   ? 42.419  55.903  25.179  1.00 20.38 ?  606  HEC A CHA 1 
HETATM 13536 C  CHB . HEC L  3 .   ? 40.251  55.231  20.898  1.00 19.98 ?  606  HEC A CHB 1 
HETATM 13537 C  CHC . HEC L  3 .   ? 42.647  51.034  20.415  1.00 18.71 ?  606  HEC A CHC 1 
HETATM 13538 C  CHD . HEC L  3 .   ? 43.718  51.176  25.137  1.00 19.95 ?  606  HEC A CHD 1 
HETATM 13539 N  NA  . HEC L  3 .   ? 41.504  55.244  23.007  1.00 20.13 ?  606  HEC A NA  1 
HETATM 13540 C  C1A . HEC L  3 .   ? 41.644  56.129  24.059  1.00 20.58 ?  606  HEC A C1A 1 
HETATM 13541 C  C2A . HEC L  3 .   ? 40.836  57.306  23.775  1.00 20.28 ?  606  HEC A C2A 1 
HETATM 13542 C  C3A . HEC L  3 .   ? 40.242  57.116  22.591  1.00 20.16 ?  606  HEC A C3A 1 
HETATM 13543 C  C4A . HEC L  3 .   ? 40.650  55.815  22.084  1.00 20.02 ?  606  HEC A C4A 1 
HETATM 13544 C  CMA . HEC L  3 .   ? 39.282  58.103  21.879  1.00 20.15 ?  606  HEC A CMA 1 
HETATM 13545 C  CAA . HEC L  3 .   ? 40.689  58.554  24.685  1.00 21.15 ?  606  HEC A CAA 1 
HETATM 13546 C  CBA . HEC L  3 .   ? 39.937  58.156  25.958  1.00 21.36 ?  606  HEC A CBA 1 
HETATM 13547 C  CGA . HEC L  3 .   ? 39.446  59.349  26.736  1.00 22.49 ?  606  HEC A CGA 1 
HETATM 13548 O  O1A . HEC L  3 .   ? 38.686  59.151  27.722  1.00 21.97 ?  606  HEC A O1A 1 
HETATM 13549 O  O2A . HEC L  3 .   ? 39.805  60.500  26.384  1.00 23.62 ?  606  HEC A O2A 1 
HETATM 13550 N  NB  . HEC L  3 .   ? 41.604  53.178  20.991  1.00 19.36 ?  606  HEC A NB  1 
HETATM 13551 C  C1B . HEC L  3 .   ? 40.699  54.033  20.385  1.00 19.56 ?  606  HEC A C1B 1 
HETATM 13552 C  C2B . HEC L  3 .   ? 40.315  53.451  19.115  1.00 19.41 ?  606  HEC A C2B 1 
HETATM 13553 C  C3B . HEC L  3 .   ? 40.977  52.292  18.974  1.00 19.07 ?  606  HEC A C3B 1 
HETATM 13554 C  C4B . HEC L  3 .   ? 41.803  52.096  20.155  1.00 19.33 ?  606  HEC A C4B 1 
HETATM 13555 C  CMB . HEC L  3 .   ? 39.312  54.081  18.117  1.00 19.81 ?  606  HEC A CMB 1 
HETATM 13556 C  CAB . HEC L  3 .   ? 40.884  51.316  17.774  1.00 18.83 ?  606  HEC A CAB 1 
HETATM 13557 C  CBB . HEC L  3 .   ? 41.355  51.694  16.575  1.00 18.99 ?  606  HEC A CBB 1 
HETATM 13558 N  NC  . HEC L  3 .   ? 43.038  51.440  22.806  1.00 19.66 ?  606  HEC A NC  1 
HETATM 13559 C  C1C . HEC L  3 .   ? 43.133  50.675  21.655  1.00 19.86 ?  606  HEC A C1C 1 
HETATM 13560 C  C2C . HEC L  3 .   ? 43.829  49.449  21.993  1.00 19.78 ?  606  HEC A C2C 1 
HETATM 13561 C  C3C . HEC L  3 .   ? 44.131  49.491  23.300  1.00 19.89 ?  606  HEC A C3C 1 
HETATM 13562 C  C4C . HEC L  3 .   ? 43.632  50.744  23.832  1.00 19.90 ?  606  HEC A C4C 1 
HETATM 13563 C  CMC . HEC L  3 .   ? 44.155  48.307  21.004  1.00 19.48 ?  606  HEC A CMC 1 
HETATM 13564 C  CAC . HEC L  3 .   ? 44.856  48.397  24.125  1.00 19.38 ?  606  HEC A CAC 1 
HETATM 13565 C  CBC . HEC L  3 .   ? 46.109  48.010  23.853  1.00 19.49 ?  606  HEC A CBC 1 
HETATM 13566 N  ND  . HEC L  3 .   ? 42.976  53.517  24.851  1.00 19.89 ?  606  HEC A ND  1 
HETATM 13567 C  C1D . HEC L  3 .   ? 43.476  52.453  25.589  1.00 19.87 ?  606  HEC A C1D 1 
HETATM 13568 C  C2D . HEC L  3 .   ? 43.719  52.902  26.935  1.00 20.22 ?  606  HEC A C2D 1 
HETATM 13569 C  C3D . HEC L  3 .   ? 43.320  54.383  26.960  1.00 20.42 ?  606  HEC A C3D 1 
HETATM 13570 C  C4D . HEC L  3 .   ? 42.870  54.676  25.620  1.00 20.15 ?  606  HEC A C4D 1 
HETATM 13571 C  CMD . HEC L  3 .   ? 44.272  52.050  28.092  1.00 19.28 ?  606  HEC A CMD 1 
HETATM 13572 C  CAD . HEC L  3 .   ? 43.393  55.344  28.168  1.00 21.59 ?  606  HEC A CAD 1 
HETATM 13573 C  CBD . HEC L  3 .   ? 44.871  55.595  28.431  1.00 23.03 ?  606  HEC A CBD 1 
HETATM 13574 C  CGD . HEC L  3 .   ? 45.083  56.211  29.781  1.00 23.84 ?  606  HEC A CGD 1 
HETATM 13575 O  O1D . HEC L  3 .   ? 45.223  57.455  29.827  1.00 24.78 ?  606  HEC A O1D 1 
HETATM 13576 O  O2D . HEC L  3 .   ? 45.121  55.463  30.791  1.00 24.45 ?  606  HEC A O2D 1 
HETATM 13577 FE FE  . HEC M  3 .   ? 24.528  57.824  12.835  1.00 21.64 ?  607  HEC A FE  1 
HETATM 13578 C  CHA . HEC M  3 .   ? 21.797  55.826  13.072  1.00 20.87 ?  607  HEC A CHA 1 
HETATM 13579 C  CHB . HEC M  3 .   ? 23.551  59.564  15.627  1.00 21.61 ?  607  HEC A CHB 1 
HETATM 13580 C  CHC . HEC M  3 .   ? 27.578  59.384  12.957  1.00 21.60 ?  607  HEC A CHC 1 
HETATM 13581 C  CHD . HEC M  3 .   ? 25.232  56.668  9.678   1.00 21.32 ?  607  HEC A CHD 1 
HETATM 13582 N  NA  . HEC M  3 .   ? 22.975  57.701  14.125  1.00 21.15 ?  607  HEC A NA  1 
HETATM 13583 C  C1A . HEC M  3 .   ? 21.913  56.824  14.022  1.00 21.37 ?  607  HEC A C1A 1 
HETATM 13584 C  C2A . HEC M  3 .   ? 20.967  57.145  15.080  1.00 20.99 ?  607  HEC A C2A 1 
HETATM 13585 C  C3A . HEC M  3 .   ? 21.460  58.176  15.775  1.00 21.18 ?  607  HEC A C3A 1 
HETATM 13586 C  C4A . HEC M  3 .   ? 22.732  58.545  15.191  1.00 21.49 ?  607  HEC A C4A 1 
HETATM 13587 C  CMA . HEC M  3 .   ? 20.815  58.880  16.989  1.00 20.80 ?  607  HEC A CMA 1 
HETATM 13588 C  CAA . HEC M  3 .   ? 19.627  56.423  15.347  1.00 22.34 ?  607  HEC A CAA 1 
HETATM 13589 C  CBA . HEC M  3 .   ? 18.609  56.872  14.301  1.00 22.56 ?  607  HEC A CBA 1 
HETATM 13590 C  CGA . HEC M  3 .   ? 17.257  56.251  14.545  1.00 22.98 ?  607  HEC A CGA 1 
HETATM 13591 O  O1A . HEC M  3 .   ? 16.339  56.579  13.766  1.00 24.30 ?  607  HEC A O1A 1 
HETATM 13592 O  O2A . HEC M  3 .   ? 17.074  55.439  15.489  1.00 22.95 ?  607  HEC A O2A 1 
HETATM 13593 N  NB  . HEC M  3 .   ? 25.410  59.235  14.078  1.00 21.12 ?  607  HEC A NB  1 
HETATM 13594 C  C1B . HEC M  3 .   ? 24.833  59.809  15.187  1.00 21.80 ?  607  HEC A C1B 1 
HETATM 13595 C  C2B . HEC M  3 .   ? 25.804  60.700  15.794  1.00 21.76 ?  607  HEC A C2B 1 
HETATM 13596 C  C3B . HEC M  3 .   ? 26.923  60.649  15.057  1.00 21.35 ?  607  HEC A C3B 1 
HETATM 13597 C  C4B . HEC M  3 .   ? 26.693  59.727  13.960  1.00 21.48 ?  607  HEC A C4B 1 
HETATM 13598 C  CMB . HEC M  3 .   ? 25.560  61.539  17.072  1.00 21.49 ?  607  HEC A CMB 1 
HETATM 13599 C  CAB . HEC M  3 .   ? 28.233  61.427  15.318  1.00 22.27 ?  607  HEC A CAB 1 
HETATM 13600 C  CBB . HEC M  3 .   ? 28.996  61.102  16.369  1.00 21.42 ?  607  HEC A CBB 1 
HETATM 13601 N  NC  . HEC M  3 .   ? 26.131  57.956  11.569  1.00 21.03 ?  607  HEC A NC  1 
HETATM 13602 C  C1C . HEC M  3 .   ? 27.256  58.734  11.781  1.00 21.67 ?  607  HEC A C1C 1 
HETATM 13603 C  C2C . HEC M  3 .   ? 28.033  58.744  10.552  1.00 22.04 ?  607  HEC A C2C 1 
HETATM 13604 C  C3C . HEC M  3 .   ? 27.386  57.991  9.648   1.00 22.05 ?  607  HEC A C3C 1 
HETATM 13605 C  C4C . HEC M  3 .   ? 26.176  57.484  10.271  1.00 21.84 ?  607  HEC A C4C 1 
HETATM 13606 C  CMC . HEC M  3 .   ? 29.372  59.497  10.354  1.00 21.90 ?  607  HEC A CMC 1 
HETATM 13607 C  CAC . HEC M  3 .   ? 27.820  57.709  8.189   1.00 22.85 ?  607  HEC A CAC 1 
HETATM 13608 C  CBC . HEC M  3 .   ? 28.810  56.842  7.936   1.00 23.65 ?  607  HEC A CBC 1 
HETATM 13609 N  ND  . HEC M  3 .   ? 23.649  56.443  11.561  1.00 20.55 ?  607  HEC A ND  1 
HETATM 13610 C  C1D . HEC M  3 .   ? 24.111  56.133  10.286  1.00 21.34 ?  607  HEC A C1D 1 
HETATM 13611 C  C2D . HEC M  3 .   ? 23.219  55.158  9.692   1.00 20.88 ?  607  HEC A C2D 1 
HETATM 13612 C  C3D . HEC M  3 .   ? 22.152  54.889  10.758  1.00 20.88 ?  607  HEC A C3D 1 
HETATM 13613 C  C4D . HEC M  3 .   ? 22.495  55.739  11.880  1.00 21.10 ?  607  HEC A C4D 1 
HETATM 13614 C  CMD . HEC M  3 .   ? 23.323  54.524  8.286   1.00 20.30 ?  607  HEC A CMD 1 
HETATM 13615 C  CAD . HEC M  3 .   ? 20.940  53.940  10.648  1.00 20.40 ?  607  HEC A CAD 1 
HETATM 13616 C  CBD . HEC M  3 .   ? 19.740  54.823  10.318  1.00 19.83 ?  607  HEC A CBD 1 
HETATM 13617 C  CGD . HEC M  3 .   ? 18.446  54.146  10.675  1.00 20.21 ?  607  HEC A CGD 1 
HETATM 13618 O  O1D . HEC M  3 .   ? 18.294  53.666  11.836  1.00 19.92 ?  607  HEC A O1D 1 
HETATM 13619 O  O2D . HEC M  3 .   ? 17.569  54.099  9.773   1.00 19.87 ?  607  HEC A O2D 1 
HETATM 13620 FE FE  . HEC N  3 .   ? 10.019  48.547  25.416  1.00 22.35 ?  608  HEC A FE  1 
HETATM 13621 C  CHA . HEC N  3 .   ? 8.048   45.799  25.206  1.00 23.26 ?  608  HEC A CHA 1 
HETATM 13622 C  CHB . HEC N  3 .   ? 7.604   50.434  26.493  1.00 23.01 ?  608  HEC A CHB 1 
HETATM 13623 C  CHC . HEC N  3 .   ? 12.496  50.247  27.153  1.00 21.52 ?  608  HEC A CHC 1 
HETATM 13624 C  CHD . HEC N  3 .   ? 12.334  47.167  23.404  1.00 21.66 ?  608  HEC A CHD 1 
HETATM 13625 N  NA  . HEC N  3 .   ? 8.213   48.177  25.886  1.00 22.85 ?  608  HEC A NA  1 
HETATM 13626 C  C1A . HEC N  3 .   ? 7.729   46.813  26.235  1.00 23.80 ?  608  HEC A C1A 1 
HETATM 13627 C  C2A . HEC N  3 .   ? 6.231   47.024  26.530  1.00 23.44 ?  608  HEC A C2A 1 
HETATM 13628 C  C3A . HEC N  3 .   ? 6.017   48.383  26.579  1.00 23.70 ?  608  HEC A C3A 1 
HETATM 13629 C  C4A . HEC N  3 .   ? 7.302   49.062  26.320  1.00 23.24 ?  608  HEC A C4A 1 
HETATM 13630 C  CMA . HEC N  3 .   ? 4.822   49.108  27.056  1.00 23.30 ?  608  HEC A CMA 1 
HETATM 13631 C  CAA . HEC N  3 .   ? 5.122   46.034  26.606  1.00 24.36 ?  608  HEC A CAA 1 
HETATM 13632 C  CBA . HEC N  3 .   ? 4.413   45.785  25.280  1.00 24.32 ?  608  HEC A CBA 1 
HETATM 13633 C  CGA . HEC N  3 .   ? 3.082   46.494  25.085  1.00 23.75 ?  608  HEC A CGA 1 
HETATM 13634 O  O1A . HEC N  3 .   ? 2.301   46.997  26.015  1.00 23.15 ?  608  HEC A O1A 1 
HETATM 13635 O  O2A . HEC N  3 .   ? 2.432   46.749  24.077  1.00 22.48 ?  608  HEC A O2A 1 
HETATM 13636 N  NB  . HEC N  3 .   ? 10.000  50.017  26.604  1.00 22.55 ?  608  HEC A NB  1 
HETATM 13637 C  C1B . HEC N  3 .   ? 8.886   50.816  26.826  1.00 23.00 ?  608  HEC A C1B 1 
HETATM 13638 C  C2B . HEC N  3 .   ? 9.293   51.989  27.613  1.00 23.23 ?  608  HEC A C2B 1 
HETATM 13639 C  C3B . HEC N  3 .   ? 10.559  51.767  28.090  1.00 22.23 ?  608  HEC A C3B 1 
HETATM 13640 C  C4B . HEC N  3 .   ? 11.010  50.375  27.608  1.00 22.25 ?  608  HEC A C4B 1 
HETATM 13641 C  CMB . HEC N  3 .   ? 8.396   53.123  27.936  1.00 22.82 ?  608  HEC A CMB 1 
HETATM 13642 C  CAB . HEC N  3 .   ? 11.478  52.764  28.710  1.00 22.05 ?  608  HEC A CAB 1 
HETATM 13643 C  CBB . HEC N  3 .   ? 10.947  53.543  29.901  1.00 20.81 ?  608  HEC A CBB 1 
HETATM 13644 N  NC  . HEC N  3 .   ? 11.887  48.925  25.115  1.00 21.60 ?  608  HEC A NC  1 
HETATM 13645 C  C1C . HEC N  3 .   ? 12.776  49.547  25.873  1.00 21.65 ?  608  HEC A C1C 1 
HETATM 13646 C  C2C . HEC N  3 .   ? 14.032  49.782  25.103  1.00 21.27 ?  608  HEC A C2C 1 
HETATM 13647 C  C3C . HEC N  3 .   ? 14.041  48.869  24.100  1.00 21.43 ?  608  HEC A C3C 1 
HETATM 13648 C  C4C . HEC N  3 .   ? 12.580  48.539  23.850  1.00 21.42 ?  608  HEC A C4C 1 
HETATM 13649 C  CMC . HEC N  3 .   ? 15.093  50.750  25.489  1.00 20.44 ?  608  HEC A CMC 1 
HETATM 13650 C  CAC . HEC N  3 .   ? 15.064  48.650  23.037  1.00 20.87 ?  608  HEC A CAC 1 
HETATM 13651 C  CBC . HEC N  3 .   ? 16.386  48.110  23.567  1.00 20.64 ?  608  HEC A CBC 1 
HETATM 13652 N  ND  . HEC N  3 .   ? 10.018  47.014  24.257  1.00 22.36 ?  608  HEC A ND  1 
HETATM 13653 C  C1D . HEC N  3 .   ? 11.172  46.497  23.616  1.00 22.12 ?  608  HEC A C1D 1 
HETATM 13654 C  C2D . HEC N  3 .   ? 10.784  45.286  22.915  1.00 22.47 ?  608  HEC A C2D 1 
HETATM 13655 C  C3D . HEC N  3 .   ? 9.528   44.936  23.381  1.00 22.47 ?  608  HEC A C3D 1 
HETATM 13656 C  C4D . HEC N  3 .   ? 9.187   45.876  24.447  1.00 23.04 ?  608  HEC A C4D 1 
HETATM 13657 C  CMD . HEC N  3 .   ? 11.531  44.676  21.795  1.00 21.67 ?  608  HEC A CMD 1 
HETATM 13658 C  CAD . HEC N  3 .   ? 8.771   43.697  23.079  1.00 22.43 ?  608  HEC A CAD 1 
HETATM 13659 C  CBD . HEC N  3 .   ? 9.259   42.523  23.927  1.00 21.97 ?  608  HEC A CBD 1 
HETATM 13660 C  CGD . HEC N  3 .   ? 8.537   41.213  23.445  1.00 22.58 ?  608  HEC A CGD 1 
HETATM 13661 O  O1D . HEC N  3 .   ? 7.300   41.135  23.582  1.00 23.05 ?  608  HEC A O1D 1 
HETATM 13662 O  O2D . HEC N  3 .   ? 9.254   40.286  22.929  1.00 20.95 ?  608  HEC A O2D 1 
HETATM 13663 K  K   . K   O  4 .   ? 32.316  37.634  5.079   1.00 38.56 ?  609  K   A K   1 
HETATM 13664 FE FE  . HEC P  3 .   ? 42.697  50.939  32.382  1.00 24.33 ?  601  HEC C FE  1 
HETATM 13665 C  CHA . HEC P  3 .   ? 41.535  54.025  31.611  1.00 23.43 ?  601  HEC C CHA 1 
HETATM 13666 C  CHB . HEC P  3 .   ? 44.767  52.153  34.635  1.00 22.80 ?  601  HEC C CHB 1 
HETATM 13667 C  CHC . HEC P  3 .   ? 42.391  47.864  33.992  1.00 22.82 ?  601  HEC C CHC 1 
HETATM 13668 C  CHD . HEC P  3 .   ? 41.227  49.630  29.674  1.00 22.61 ?  601  HEC C CHD 1 
HETATM 13669 N  NA  . HEC P  3 .   ? 42.980  52.690  33.093  1.00 23.37 ?  601  HEC C NA  1 
HETATM 13670 C  C1A . HEC P  3 .   ? 41.962  53.770  32.999  1.00 24.21 ?  601  HEC C C1A 1 
HETATM 13671 C  C2A . HEC P  3 .   ? 42.615  54.972  33.706  1.00 24.12 ?  601  HEC C C2A 1 
HETATM 13672 C  C3A . HEC P  3 .   ? 43.718  54.494  34.362  1.00 23.74 ?  601  HEC C C3A 1 
HETATM 13673 C  C4A . HEC P  3 .   ? 43.880  53.065  34.023  1.00 23.71 ?  601  HEC C C4A 1 
HETATM 13674 C  CMA . HEC P  3 .   ? 44.549  55.175  35.378  1.00 24.14 ?  601  HEC C CMA 1 
HETATM 13675 C  CAA . HEC P  3 .   ? 42.244  56.411  33.634  1.00 24.63 ?  601  HEC C CAA 1 
HETATM 13676 C  CBA . HEC P  3 .   ? 42.863  57.195  32.484  1.00 25.46 ?  601  HEC C CBA 1 
HETATM 13677 C  CGA . HEC P  3 .   ? 44.099  57.959  32.925  1.00 25.16 ?  601  HEC C CGA 1 
HETATM 13678 O  O1A . HEC P  3 .   ? 44.538  58.283  34.120  1.00 24.77 ?  601  HEC C O1A 1 
HETATM 13679 O  O2A . HEC P  3 .   ? 44.946  58.436  32.182  1.00 23.83 ?  601  HEC C O2A 1 
HETATM 13680 N  NB  . HEC P  3 .   ? 43.414  50.226  33.979  1.00 23.19 ?  601  HEC C NB  1 
HETATM 13681 C  C1B . HEC P  3 .   ? 44.430  50.824  34.726  1.00 22.81 ?  601  HEC C C1B 1 
HETATM 13682 C  C2B . HEC P  3 .   ? 44.937  49.857  35.702  1.00 22.66 ?  601  HEC C C2B 1 
HETATM 13683 C  C3B . HEC P  3 .   ? 44.001  48.864  35.823  1.00 22.28 ?  601  HEC C C3B 1 
HETATM 13684 C  C4B . HEC P  3 .   ? 42.889  49.112  34.784  1.00 23.14 ?  601  HEC C C4B 1 
HETATM 13685 C  CMB . HEC P  3 .   ? 46.093  50.110  36.595  1.00 21.65 ?  601  HEC C CMB 1 
HETATM 13686 C  CAB . HEC P  3 .   ? 44.150  47.586  36.562  1.00 21.87 ?  601  HEC C CAB 1 
HETATM 13687 C  CBB . HEC P  3 .   ? 44.434  47.698  38.045  1.00 21.11 ?  601  HEC C CBB 1 
HETATM 13688 N  NC  . HEC P  3 .   ? 42.342  49.124  31.823  1.00 22.74 ?  601  HEC C NC  1 
HETATM 13689 C  C1C . HEC P  3 .   ? 42.239  48.003  32.523  1.00 22.47 ?  601  HEC C C1C 1 
HETATM 13690 C  C2C . HEC P  3 .   ? 42.114  46.822  31.623  1.00 22.05 ?  601  HEC C C2C 1 
HETATM 13691 C  C3C . HEC P  3 .   ? 41.758  47.285  30.401  1.00 22.07 ?  601  HEC C C3C 1 
HETATM 13692 C  C4C . HEC P  3 .   ? 42.152  48.754  30.390  1.00 22.25 ?  601  HEC C C4C 1 
HETATM 13693 C  CMC . HEC P  3 .   ? 42.246  45.415  32.076  1.00 21.79 ?  601  HEC C CMC 1 
HETATM 13694 C  CAC . HEC P  3 .   ? 41.584  46.532  29.124  1.00 22.19 ?  601  HEC C CAC 1 
HETATM 13695 C  CBC . HEC P  3 .   ? 40.339  45.653  29.101  1.00 22.25 ?  601  HEC C CBC 1 
HETATM 13696 N  ND  . HEC P  3 .   ? 41.944  51.712  30.792  1.00 22.83 ?  601  HEC C ND  1 
HETATM 13697 C  C1D . HEC P  3 .   ? 41.284  50.979  29.774  1.00 23.01 ?  601  HEC C C1D 1 
HETATM 13698 C  C2D . HEC P  3 .   ? 40.816  51.925  28.777  1.00 22.75 ?  601  HEC C C2D 1 
HETATM 13699 C  C3D . HEC P  3 .   ? 40.748  53.152  29.416  1.00 22.81 ?  601  HEC C C3D 1 
HETATM 13700 C  C4D . HEC P  3 .   ? 41.321  52.989  30.748  1.00 23.06 ?  601  HEC C C4D 1 
HETATM 13701 C  CMD . HEC P  3 .   ? 40.293  51.573  27.442  1.00 22.08 ?  601  HEC C CMD 1 
HETATM 13702 C  CAD . HEC P  3 .   ? 40.231  54.437  28.887  1.00 22.55 ?  601  HEC C CAD 1 
HETATM 13703 C  CBD . HEC P  3 .   ? 38.751  54.615  29.220  1.00 22.63 ?  601  HEC C CBD 1 
HETATM 13704 C  CGD . HEC P  3 .   ? 38.198  55.864  28.442  1.00 23.32 ?  601  HEC C CGD 1 
HETATM 13705 O  O1D . HEC P  3 .   ? 38.550  56.998  28.807  1.00 24.53 ?  601  HEC C O1D 1 
HETATM 13706 O  O2D . HEC P  3 .   ? 37.410  55.668  27.460  1.00 22.82 ?  601  HEC C O2D 1 
HETATM 13707 FE FE  . HEC Q  3 .   ? 34.326  15.648  13.673  1.00 22.12 ?  602  HEC C FE  1 
HETATM 13708 C  CHA . HEC Q  3 .   ? 36.420  16.535  11.067  1.00 22.14 ?  602  HEC C CHA 1 
HETATM 13709 C  CHB . HEC Q  3 .   ? 33.509  12.790  12.034  1.00 21.86 ?  602  HEC C CHB 1 
HETATM 13710 C  CHC . HEC Q  3 .   ? 32.589  14.518  16.459  1.00 20.96 ?  602  HEC C CHC 1 
HETATM 13711 C  CHD . HEC Q  3 .   ? 34.846  18.628  15.207  1.00 20.54 ?  602  HEC C CHD 1 
HETATM 13712 N  NA  . HEC Q  3 .   ? 34.843  14.847  11.862  1.00 22.23 ?  602  HEC C NA  1 
HETATM 13713 C  C1A . HEC Q  3 .   ? 35.758  15.335  10.950  1.00 22.36 ?  602  HEC C C1A 1 
HETATM 13714 C  C2A . HEC Q  3 .   ? 35.887  14.372  9.870   1.00 22.49 ?  602  HEC C C2A 1 
HETATM 13715 C  C3A . HEC Q  3 .   ? 35.078  13.350  10.153  1.00 22.56 ?  602  HEC C C3A 1 
HETATM 13716 C  C4A . HEC Q  3 .   ? 34.409  13.619  11.407  1.00 22.27 ?  602  HEC C C4A 1 
HETATM 13717 C  CMA . HEC Q  3 .   ? 34.882  12.088  9.296   1.00 23.07 ?  602  HEC C CMA 1 
HETATM 13718 C  CAA . HEC Q  3 .   ? 36.798  14.493  8.621   1.00 22.49 ?  602  HEC C CAA 1 
HETATM 13719 C  CBA . HEC Q  3 .   ? 36.018  15.117  7.472   1.00 23.03 ?  602  HEC C CBA 1 
HETATM 13720 C  CGA . HEC Q  3 .   ? 36.902  15.894  6.527   1.00 23.44 ?  602  HEC C CGA 1 
HETATM 13721 O  O1A . HEC Q  3 .   ? 36.632  15.832  5.304   1.00 23.32 ?  602  HEC C O1A 1 
HETATM 13722 O  O2A . HEC Q  3 .   ? 37.862  16.583  6.974   1.00 23.45 ?  602  HEC C O2A 1 
HETATM 13723 N  NB  . HEC Q  3 .   ? 33.206  13.979  14.152  1.00 21.34 ?  602  HEC C NB  1 
HETATM 13724 C  C1B . HEC Q  3 .   ? 33.111  12.861  13.351  1.00 21.86 ?  602  HEC C C1B 1 
HETATM 13725 C  C2B . HEC Q  3 .   ? 32.509  11.799  14.136  1.00 21.88 ?  602  HEC C C2B 1 
HETATM 13726 C  C3B . HEC Q  3 .   ? 32.252  12.273  15.362  1.00 21.63 ?  602  HEC C C3B 1 
HETATM 13727 C  C4B . HEC Q  3 .   ? 32.682  13.657  15.392  1.00 21.84 ?  602  HEC C C4B 1 
HETATM 13728 C  CMB . HEC Q  3 .   ? 32.226  10.367  13.630  1.00 22.68 ?  602  HEC C CMB 1 
HETATM 13729 C  CAB . HEC Q  3 .   ? 31.614  11.500  16.544  1.00 21.78 ?  602  HEC C CAB 1 
HETATM 13730 C  CBB . HEC Q  3 .   ? 32.371  10.692  17.301  1.00 20.58 ?  602  HEC C CBB 1 
HETATM 13731 N  NC  . HEC Q  3 .   ? 33.825  16.412  15.497  1.00 21.10 ?  602  HEC C NC  1 
HETATM 13732 C  C1C . HEC Q  3 .   ? 33.061  15.813  16.485  1.00 21.17 ?  602  HEC C C1C 1 
HETATM 13733 C  C2C . HEC Q  3 .   ? 32.863  16.777  17.549  1.00 20.55 ?  602  HEC C C2C 1 
HETATM 13734 C  C3C . HEC Q  3 .   ? 33.489  17.906  17.198  1.00 20.76 ?  602  HEC C C3C 1 
HETATM 13735 C  C4C . HEC Q  3 .   ? 34.108  17.699  15.904  1.00 21.01 ?  602  HEC C C4C 1 
HETATM 13736 C  CMC . HEC Q  3 .   ? 32.062  16.537  18.850  1.00 20.93 ?  602  HEC C CMC 1 
HETATM 13737 C  CAC . HEC Q  3 .   ? 33.555  19.215  18.018  1.00 21.35 ?  602  HEC C CAC 1 
HETATM 13738 C  CBC . HEC Q  3 .   ? 34.264  19.233  19.154  1.00 21.47 ?  602  HEC C CBC 1 
HETATM 13739 N  ND  . HEC Q  3 .   ? 35.430  17.337  13.183  1.00 21.02 ?  602  HEC C ND  1 
HETATM 13740 C  C1D . HEC Q  3 .   ? 35.575  18.412  14.056  1.00 21.06 ?  602  HEC C C1D 1 
HETATM 13741 C  C2D . HEC Q  3 .   ? 36.620  19.280  13.563  1.00 20.35 ?  602  HEC C C2D 1 
HETATM 13742 C  C3D . HEC Q  3 .   ? 37.106  18.633  12.268  1.00 20.82 ?  602  HEC C C3D 1 
HETATM 13743 C  C4D . HEC Q  3 .   ? 36.316  17.430  12.114  1.00 21.80 ?  602  HEC C C4D 1 
HETATM 13744 C  CMD . HEC Q  3 .   ? 37.130  20.587  14.204  1.00 19.76 ?  602  HEC C CMD 1 
HETATM 13745 C  CAD . HEC Q  3 .   ? 38.236  19.129  11.345  1.00 20.89 ?  602  HEC C CAD 1 
HETATM 13746 C  CBD . HEC Q  3 .   ? 39.466  18.331  11.801  1.00 21.80 ?  602  HEC C CBD 1 
HETATM 13747 C  CGD . HEC Q  3 .   ? 40.713  18.567  10.989  1.00 22.06 ?  602  HEC C CGD 1 
HETATM 13748 O  O1D . HEC Q  3 .   ? 40.669  19.296  9.965   1.00 22.05 ?  602  HEC C O1D 1 
HETATM 13749 O  O2D . HEC Q  3 .   ? 41.772  18.009  11.385  1.00 22.32 ?  602  HEC C O2D 1 
HETATM 13750 FE FE  . HEC R  3 .   ? 30.536  11.197  6.911   1.00 23.51 ?  603  HEC C FE  1 
HETATM 13751 C  CHA . HEC R  3 .   ? 32.354  13.248  4.841   1.00 22.07 ?  603  HEC C CHA 1 
HETATM 13752 C  CHB . HEC R  3 .   ? 30.680  13.520  9.389   1.00 22.81 ?  603  HEC C CHB 1 
HETATM 13753 C  CHC . HEC R  3 .   ? 28.144  9.452   8.686   1.00 23.36 ?  603  HEC C CHC 1 
HETATM 13754 C  CHD . HEC R  3 .   ? 30.995  8.545   4.861   1.00 22.93 ?  603  HEC C CHD 1 
HETATM 13755 N  NA  . HEC R  3 .   ? 31.366  13.050  7.075   1.00 22.69 ?  603  HEC C NA  1 
HETATM 13756 C  C1A . HEC R  3 .   ? 32.070  13.729  6.103   1.00 22.86 ?  603  HEC C C1A 1 
HETATM 13757 C  C2A . HEC R  3 .   ? 32.444  15.016  6.655   1.00 22.57 ?  603  HEC C C2A 1 
HETATM 13758 C  C3A . HEC R  3 .   ? 31.988  15.090  7.910   1.00 22.42 ?  603  HEC C C3A 1 
HETATM 13759 C  C4A . HEC R  3 .   ? 31.297  13.853  8.199   1.00 22.78 ?  603  HEC C C4A 1 
HETATM 13760 C  CMA . HEC R  3 .   ? 32.156  16.283  8.888   1.00 22.50 ?  603  HEC C CMA 1 
HETATM 13761 C  CAA . HEC R  3 .   ? 33.242  16.108  5.915   1.00 22.72 ?  603  HEC C CAA 1 
HETATM 13762 C  CBA . HEC R  3 .   ? 32.392  16.737  4.820   1.00 22.93 ?  603  HEC C CBA 1 
HETATM 13763 C  CGA . HEC R  3 .   ? 33.143  17.923  4.281   1.00 22.91 ?  603  HEC C CGA 1 
HETATM 13764 O  O1A . HEC R  3 .   ? 33.562  17.874  3.098   1.00 23.04 ?  603  HEC C O1A 1 
HETATM 13765 O  O2A . HEC R  3 .   ? 33.331  18.909  5.041   1.00 22.84 ?  603  HEC C O2A 1 
HETATM 13766 N  NB  . HEC R  3 .   ? 29.579  11.436  8.708   1.00 22.51 ?  603  HEC C NB  1 
HETATM 13767 C  C1B . HEC R  3 .   ? 29.798  12.481  9.586   1.00 22.94 ?  603  HEC C C1B 1 
HETATM 13768 C  C2B . HEC R  3 .   ? 28.943  12.285  10.742  1.00 23.28 ?  603  HEC C C2B 1 
HETATM 13769 C  C3B . HEC R  3 .   ? 28.242  11.161  10.548  1.00 23.48 ?  603  HEC C C3B 1 
HETATM 13770 C  C4B . HEC R  3 .   ? 28.625  10.606  9.264   1.00 23.30 ?  603  HEC C C4B 1 
HETATM 13771 C  CMB . HEC R  3 .   ? 28.864  13.223  11.968  1.00 23.08 ?  603  HEC C CMB 1 
HETATM 13772 C  CAB . HEC R  3 .   ? 27.191  10.558  11.503  1.00 24.22 ?  603  HEC C CAB 1 
HETATM 13773 C  CBB . HEC R  3 .   ? 25.959  11.086  11.515  1.00 24.96 ?  603  HEC C CBB 1 
HETATM 13774 N  NC  . HEC R  3 .   ? 29.692  9.348   6.785   1.00 23.12 ?  603  HEC C NC  1 
HETATM 13775 C  C1C . HEC R  3 .   ? 28.763  8.790   7.646   1.00 23.16 ?  603  HEC C C1C 1 
HETATM 13776 C  C2C . HEC R  3 .   ? 28.572  7.405   7.266   1.00 23.24 ?  603  HEC C C2C 1 
HETATM 13777 C  C3C . HEC R  3 .   ? 29.361  7.157   6.206   1.00 23.73 ?  603  HEC C C3C 1 
HETATM 13778 C  C4C . HEC R  3 .   ? 30.085  8.376   5.885   1.00 23.34 ?  603  HEC C C4C 1 
HETATM 13779 C  CMC . HEC R  3 .   ? 27.613  6.417   7.973   1.00 23.27 ?  603  HEC C CMC 1 
HETATM 13780 C  CAC . HEC R  3 .   ? 29.498  5.813   5.444   1.00 24.67 ?  603  HEC C CAC 1 
HETATM 13781 C  CBC . HEC R  3 .   ? 28.455  5.310   4.766   1.00 24.10 ?  603  HEC C CBC 1 
HETATM 13782 N  ND  . HEC R  3 .   ? 31.502  10.956  5.082   1.00 22.36 ?  603  HEC C ND  1 
HETATM 13783 C  C1D . HEC R  3 .   ? 31.637  9.708   4.478   1.00 22.43 ?  603  HEC C C1D 1 
HETATM 13784 C  C2D . HEC R  3 .   ? 32.577  9.832   3.385   1.00 22.24 ?  603  HEC C C2D 1 
HETATM 13785 C  C3D . HEC R  3 .   ? 33.006  11.300  3.366   1.00 21.74 ?  603  HEC C C3D 1 
HETATM 13786 C  C4D . HEC R  3 .   ? 32.288  11.922  4.462   1.00 22.26 ?  603  HEC C C4D 1 
HETATM 13787 C  CMD . HEC R  3 .   ? 33.050  8.727   2.417   1.00 22.42 ?  603  HEC C CMD 1 
HETATM 13788 C  CAD . HEC R  3 .   ? 34.010  11.946  2.382   1.00 21.46 ?  603  HEC C CAD 1 
HETATM 13789 C  CBD . HEC R  3 .   ? 35.432  11.753  2.911   1.00 20.07 ?  603  HEC C CBD 1 
HETATM 13790 C  CGD . HEC R  3 .   ? 35.739  12.799  3.954   1.00 20.30 ?  603  HEC C CGD 1 
HETATM 13791 O  O1D . HEC R  3 .   ? 35.980  12.429  5.134   1.00 19.80 ?  603  HEC C O1D 1 
HETATM 13792 O  O2D . HEC R  3 .   ? 35.749  14.010  3.604   1.00 19.68 ?  603  HEC C O2D 1 
HETATM 13793 FE FE  . HEC S  3 .   ? 10.530  9.575   6.644   1.00 27.61 ?  604  HEC C FE  1 
HETATM 13794 C  CHA . HEC S  3 .   ? 9.965   11.230  9.627   1.00 26.85 ?  604  HEC C CHA 1 
HETATM 13795 C  CHB . HEC S  3 .   ? 13.789  9.118   7.512   1.00 26.69 ?  604  HEC C CHB 1 
HETATM 13796 C  CHC . HEC S  3 .   ? 10.927  7.495   3.934   1.00 28.64 ?  604  HEC C CHC 1 
HETATM 13797 C  CHD . HEC S  3 .   ? 7.461   10.530  5.470   1.00 28.72 ?  604  HEC C CHD 1 
HETATM 13798 N  NA  . HEC S  3 .   ? 11.670  10.092  8.279   1.00 26.94 ?  604  HEC C NA  1 
HETATM 13799 C  C1A . HEC S  3 .   ? 11.242  10.754  9.417   1.00 26.56 ?  604  HEC C C1A 1 
HETATM 13800 C  C2A . HEC S  3 .   ? 12.370  10.854  10.328  1.00 25.49 ?  604  HEC C C2A 1 
HETATM 13801 C  C3A . HEC S  3 .   ? 13.420  10.276  9.734   1.00 25.83 ?  604  HEC C C3A 1 
HETATM 13802 C  C4A . HEC S  3 .   ? 13.003  9.780   8.435   1.00 26.44 ?  604  HEC C C4A 1 
HETATM 13803 C  CMA . HEC S  3 .   ? 14.843  10.136  10.310  1.00 25.14 ?  604  HEC C CMA 1 
HETATM 13804 C  CAA . HEC S  3 .   ? 12.350  11.518  11.729  1.00 24.31 ?  604  HEC C CAA 1 
HETATM 13805 C  CBA . HEC S  3 .   ? 11.637  10.609  12.723  1.00 23.97 ?  604  HEC C CBA 1 
HETATM 13806 C  CGA . HEC S  3 .   ? 11.569  11.235  14.091  1.00 23.55 ?  604  HEC C CGA 1 
HETATM 13807 O  O1A . HEC S  3 .   ? 11.566  12.487  14.201  1.00 23.94 ?  604  HEC C O1A 1 
HETATM 13808 O  O2A . HEC S  3 .   ? 11.505  10.473  15.086  1.00 23.20 ?  604  HEC C O2A 1 
HETATM 13809 N  NB  . HEC S  3 .   ? 12.091  8.521   5.838   1.00 27.92 ?  604  HEC C NB  1 
HETATM 13810 C  C1B . HEC S  3 .   ? 13.347  8.420   6.406   1.00 27.58 ?  604  HEC C C1B 1 
HETATM 13811 C  C2B . HEC S  3 .   ? 14.104  7.450   5.642   1.00 28.17 ?  604  HEC C C2B 1 
HETATM 13812 C  C3B . HEC S  3 .   ? 13.319  7.002   4.651   1.00 28.75 ?  604  HEC C C3B 1 
HETATM 13813 C  C4B . HEC S  3 .   ? 12.030  7.668   4.753   1.00 28.74 ?  604  HEC C C4B 1 
HETATM 13814 C  CMB . HEC S  3 .   ? 15.566  7.028   5.934   1.00 28.21 ?  604  HEC C CMB 1 
HETATM 13815 C  CAB . HEC S  3 .   ? 13.706  5.951   3.588   1.00 29.07 ?  604  HEC C CAB 1 
HETATM 13816 C  CBB . HEC S  3 .   ? 13.831  4.667   3.946   1.00 28.62 ?  604  HEC C CBB 1 
HETATM 13817 N  NC  . HEC S  3 .   ? 9.378   9.063   5.015   1.00 28.20 ?  604  HEC C NC  1 
HETATM 13818 C  C1C . HEC S  3 .   ? 9.770   8.257   3.964   1.00 28.58 ?  604  HEC C C1C 1 
HETATM 13819 C  C2C . HEC S  3 .   ? 8.760   8.363   2.923   1.00 28.67 ?  604  HEC C C2C 1 
HETATM 13820 C  C3C . HEC S  3 .   ? 7.802   9.207   3.352   1.00 28.97 ?  604  HEC C C3C 1 
HETATM 13821 C  C4C . HEC S  3 .   ? 8.181   9.658   4.679   1.00 28.72 ?  604  HEC C C4C 1 
HETATM 13822 C  CMC . HEC S  3 .   ? 8.822   7.615   1.572   1.00 28.79 ?  604  HEC C CMC 1 
HETATM 13823 C  CAC . HEC S  3 .   ? 6.511   9.681   2.624   1.00 29.60 ?  604  HEC C CAC 1 
HETATM 13824 C  CBC . HEC S  3 .   ? 5.870   8.934   1.713   1.00 29.90 ?  604  HEC C CBC 1 
HETATM 13825 N  ND  . HEC S  3 .   ? 8.939   10.702  7.445   1.00 28.30 ?  604  HEC C ND  1 
HETATM 13826 C  C1D . HEC S  3 .   ? 7.770   10.974  6.740   1.00 28.50 ?  604  HEC C C1D 1 
HETATM 13827 C  C2D . HEC S  3 .   ? 6.920   11.807  7.560   1.00 28.45 ?  604  HEC C C2D 1 
HETATM 13828 C  C3D . HEC S  3 .   ? 7.700   12.033  8.860   1.00 28.54 ?  604  HEC C C3D 1 
HETATM 13829 C  C4D . HEC S  3 .   ? 8.947   11.312  8.697   1.00 27.92 ?  604  HEC C C4D 1 
HETATM 13830 C  CMD . HEC S  3 .   ? 5.517   12.354  7.214   1.00 28.70 ?  604  HEC C CMD 1 
HETATM 13831 C  CAD . HEC S  3 .   ? 7.229   12.865  10.073  1.00 28.46 ?  604  HEC C CAD 1 
HETATM 13832 C  CBD . HEC S  3 .   ? 6.860   11.945  11.225  1.00 29.48 ?  604  HEC C CBD 1 
HETATM 13833 C  CGD . HEC S  3 .   ? 6.599   12.768  12.458  1.00 29.98 ?  604  HEC C CGD 1 
HETATM 13834 O  O1D . HEC S  3 .   ? 5.719   12.368  13.253  1.00 30.34 ?  604  HEC C O1D 1 
HETATM 13835 O  O2D . HEC S  3 .   ? 7.262   13.821  12.653  1.00 31.30 ?  604  HEC C O2D 1 
HETATM 13836 FE FE  . HEC T  3 .   ? 19.066  12.742  9.224   1.00 23.80 ?  605  HEC C FE  1 
HETATM 13837 C  CHA . HEC T  3 .   ? 18.075  13.503  12.441  1.00 22.51 ?  605  HEC C CHA 1 
HETATM 13838 C  CHB . HEC T  3 .   ? 15.885  13.242  8.126   1.00 22.80 ?  605  HEC C CHB 1 
HETATM 13839 C  CHC . HEC T  3 .   ? 20.107  12.246  5.959   1.00 23.79 ?  605  HEC C CHC 1 
HETATM 13840 C  CHD . HEC T  3 .   ? 22.231  11.952  10.301  1.00 22.94 ?  605  HEC C CHD 1 
HETATM 13841 N  NA  . HEC T  3 .   ? 17.301  13.276  10.137  1.00 22.94 ?  605  HEC C NA  1 
HETATM 13842 C  C1A . HEC T  3 .   ? 17.089  13.546  11.478  1.00 22.76 ?  605  HEC C C1A 1 
HETATM 13843 C  C2A . HEC T  3 .   ? 15.677  13.872  11.657  1.00 22.34 ?  605  HEC C C2A 1 
HETATM 13844 C  C3A . HEC T  3 .   ? 15.093  13.793  10.452  1.00 22.18 ?  605  HEC C C3A 1 
HETATM 13845 C  C4A . HEC T  3 .   ? 16.099  13.427  9.476   1.00 22.61 ?  605  HEC C C4A 1 
HETATM 13846 C  CMA . HEC T  3 .   ? 13.607  14.058  10.114  1.00 21.38 ?  605  HEC C CMA 1 
HETATM 13847 C  CAA . HEC T  3 .   ? 14.946  14.222  12.982  1.00 22.27 ?  605  HEC C CAA 1 
HETATM 13848 C  CBA . HEC T  3 .   ? 15.513  15.436  13.718  1.00 22.80 ?  605  HEC C CBA 1 
HETATM 13849 C  CGA . HEC T  3 .   ? 15.241  16.713  12.973  1.00 23.20 ?  605  HEC C CGA 1 
HETATM 13850 O  O1A . HEC T  3 .   ? 14.314  16.754  12.123  1.00 23.73 ?  605  HEC C O1A 1 
HETATM 13851 O  O2A . HEC T  3 .   ? 15.970  17.703  13.236  1.00 23.38 ?  605  HEC C O2A 1 
HETATM 13852 N  NB  . HEC T  3 .   ? 18.174  12.743  7.397   1.00 23.26 ?  605  HEC C NB  1 
HETATM 13853 C  C1B . HEC T  3 .   ? 16.830  12.962  7.166   1.00 23.40 ?  605  HEC C C1B 1 
HETATM 13854 C  C2B . HEC T  3 .   ? 16.596  12.867  5.735   1.00 23.36 ?  605  HEC C C2B 1 
HETATM 13855 C  C3B . HEC T  3 .   ? 17.762  12.596  5.141   1.00 23.40 ?  605  HEC C C3B 1 
HETATM 13856 C  C4B . HEC T  3 .   ? 18.774  12.514  6.169   1.00 23.92 ?  605  HEC C C4B 1 
HETATM 13857 C  CMB . HEC T  3 .   ? 15.230  13.051  5.037   1.00 22.65 ?  605  HEC C CMB 1 
HETATM 13858 C  CAB . HEC T  3 .   ? 18.016  12.411  3.628   1.00 24.30 ?  605  HEC C CAB 1 
HETATM 13859 C  CBB . HEC T  3 .   ? 17.871  13.455  2.796   1.00 24.55 ?  605  HEC C CBB 1 
HETATM 13860 N  NC  . HEC T  3 .   ? 20.862  12.233  8.295   1.00 23.17 ?  605  HEC C NC  1 
HETATM 13861 C  C1C . HEC T  3 .   ? 21.032  11.983  6.943   1.00 23.65 ?  605  HEC C C1C 1 
HETATM 13862 C  C2C . HEC T  3 .   ? 22.341  11.403  6.747   1.00 23.28 ?  605  HEC C C2C 1 
HETATM 13863 C  C3C . HEC T  3 .   ? 22.933  11.313  7.946   1.00 23.39 ?  605  HEC C C3C 1 
HETATM 13864 C  C4C . HEC T  3 .   ? 22.011  11.839  8.944   1.00 23.04 ?  605  HEC C C4C 1 
HETATM 13865 C  CMC . HEC T  3 .   ? 22.917  10.972  5.379   1.00 23.38 ?  605  HEC C CMC 1 
HETATM 13866 C  CAC . HEC T  3 .   ? 24.346  10.734  8.222   1.00 24.53 ?  605  HEC C CAC 1 
HETATM 13867 C  CBC . HEC T  3 .   ? 25.432  11.386  7.789   1.00 24.40 ?  605  HEC C CBC 1 
HETATM 13868 N  ND  . HEC T  3 .   ? 20.001  12.696  11.096  1.00 22.85 ?  605  HEC C ND  1 
HETATM 13869 C  C1D . HEC T  3 .   ? 21.366  12.451  11.262  1.00 23.26 ?  605  HEC C C1D 1 
HETATM 13870 C  C2D . HEC T  3 .   ? 21.729  12.792  12.623  1.00 22.55 ?  605  HEC C C2D 1 
HETATM 13871 C  C3D . HEC T  3 .   ? 20.431  13.266  13.276  1.00 22.69 ?  605  HEC C C3D 1 
HETATM 13872 C  C4D . HEC T  3 .   ? 19.409  13.172  12.262  1.00 22.91 ?  605  HEC C C4D 1 
HETATM 13873 C  CMD . HEC T  3 .   ? 23.116  12.705  13.299  1.00 22.61 ?  605  HEC C CMD 1 
HETATM 13874 C  CAD . HEC T  3 .   ? 20.252  13.745  14.728  1.00 22.78 ?  605  HEC C CAD 1 
HETATM 13875 C  CBD . HEC T  3 .   ? 19.915  12.516  15.559  1.00 22.48 ?  605  HEC C CBD 1 
HETATM 13876 C  CGD . HEC T  3 .   ? 19.604  12.934  16.969  1.00 22.64 ?  605  HEC C CGD 1 
HETATM 13877 O  O1D . HEC T  3 .   ? 19.344  14.139  17.205  1.00 22.96 ?  605  HEC C O1D 1 
HETATM 13878 O  O2D . HEC T  3 .   ? 19.623  12.055  17.863  1.00 22.84 ?  605  HEC C O2D 1 
HETATM 13879 FE FE  . HEC U  3 .   ? 40.962  26.915  25.096  1.00 19.95 ?  606  HEC C FE  1 
HETATM 13880 C  CHA . HEC U  3 .   ? 41.580  25.762  28.266  1.00 20.08 ?  606  HEC C CHA 1 
HETATM 13881 C  CHB . HEC U  3 .   ? 37.848  25.634  25.190  1.00 18.96 ?  606  HEC C CHB 1 
HETATM 13882 C  CHC . HEC U  3 .   ? 40.201  28.749  22.289  1.00 18.40 ?  606  HEC C CHC 1 
HETATM 13883 C  CHD . HEC U  3 .   ? 44.265  27.466  24.572  1.00 20.35 ?  606  HEC C CHD 1 
HETATM 13884 N  NA  . HEC U  3 .   ? 39.878  25.929  26.521  1.00 19.25 ?  606  HEC C NA  1 
HETATM 13885 C  C1A . HEC U  3 .   ? 40.378  25.404  27.692  1.00 19.62 ?  606  HEC C C1A 1 
HETATM 13886 C  C2A . HEC U  3 .   ? 39.426  24.429  28.188  1.00 19.52 ?  606  HEC C C2A 1 
HETATM 13887 C  C3A . HEC U  3 .   ? 38.391  24.396  27.330  1.00 19.16 ?  606  HEC C C3A 1 
HETATM 13888 C  C4A . HEC U  3 .   ? 38.656  25.348  26.271  1.00 19.27 ?  606  HEC C C4A 1 
HETATM 13889 C  CMA . HEC U  3 .   ? 37.122  23.521  27.429  1.00 18.13 ?  606  HEC C CMA 1 
HETATM 13890 C  CAA . HEC U  3 .   ? 39.605  23.588  29.478  1.00 19.01 ?  606  HEC C CAA 1 
HETATM 13891 C  CBA . HEC U  3 .   ? 40.494  22.372  29.185  1.00 19.18 ?  606  HEC C CBA 1 
HETATM 13892 C  CGA . HEC U  3 .   ? 41.961  22.655  29.433  1.00 19.83 ?  606  HEC C CGA 1 
HETATM 13893 O  O1A . HEC U  3 .   ? 42.779  22.467  28.492  1.00 19.10 ?  606  HEC C O1A 1 
HETATM 13894 O  O2A . HEC U  3 .   ? 42.322  23.072  30.568  1.00 19.83 ?  606  HEC C O2A 1 
HETATM 13895 N  NB  . HEC U  3 .   ? 39.336  27.131  23.924  1.00 18.90 ?  606  HEC C NB  1 
HETATM 13896 C  C1B . HEC U  3 .   ? 38.109  26.566  24.206  1.00 18.70 ?  606  HEC C C1B 1 
HETATM 13897 C  C2B . HEC U  3 .   ? 37.147  27.138  23.293  1.00 18.55 ?  606  HEC C C2B 1 
HETATM 13898 C  C3B . HEC U  3 .   ? 37.790  27.997  22.490  1.00 18.15 ?  606  HEC C C3B 1 
HETATM 13899 C  C4B . HEC U  3 .   ? 39.187  28.007  22.867  1.00 18.86 ?  606  HEC C C4B 1 
HETATM 13900 C  CMB . HEC U  3 .   ? 35.644  26.779  23.272  1.00 17.78 ?  606  HEC C CMB 1 
HETATM 13901 C  CAB . HEC U  3 .   ? 37.170  28.855  21.367  1.00 19.20 ?  606  HEC C CAB 1 
HETATM 13902 C  CBB . HEC U  3 .   ? 36.126  29.655  21.648  1.00 18.62 ?  606  HEC C CBB 1 
HETATM 13903 N  NC  . HEC U  3 .   ? 42.045  27.976  23.691  1.00 19.33 ?  606  HEC C NC  1 
HETATM 13904 C  C1C . HEC U  3 .   ? 41.543  28.541  22.535  1.00 19.52 ?  606  HEC C C1C 1 
HETATM 13905 C  C2C . HEC U  3 .   ? 42.671  28.855  21.674  1.00 19.42 ?  606  HEC C C2C 1 
HETATM 13906 C  C3C . HEC U  3 .   ? 43.798  28.495  22.308  1.00 19.45 ?  606  HEC C C3C 1 
HETATM 13907 C  C4C . HEC U  3 .   ? 43.417  27.941  23.595  1.00 19.79 ?  606  HEC C C4C 1 
HETATM 13908 C  CMC . HEC U  3 .   ? 42.574  29.488  20.271  1.00 19.48 ?  606  HEC C CMC 1 
HETATM 13909 C  CAC . HEC U  3 .   ? 45.247  28.613  21.760  1.00 19.89 ?  606  HEC C CAC 1 
HETATM 13910 C  CBC . HEC U  3 .   ? 45.806  29.812  21.526  1.00 19.70 ?  606  HEC C CBC 1 
HETATM 13911 N  ND  . HEC U  3 .   ? 42.680  26.635  26.263  1.00 20.13 ?  606  HEC C ND  1 
HETATM 13912 C  C1D . HEC U  3 .   ? 43.940  27.037  25.844  1.00 20.44 ?  606  HEC C C1D 1 
HETATM 13913 C  C2D . HEC U  3 .   ? 44.855  26.922  26.962  1.00 20.46 ?  606  HEC C C2D 1 
HETATM 13914 C  C3D . HEC U  3 .   ? 44.016  26.387  28.130  1.00 20.83 ?  606  HEC C C3D 1 
HETATM 13915 C  C4D . HEC U  3 .   ? 42.683  26.231  27.590  1.00 20.48 ?  606  HEC C C4D 1 
HETATM 13916 C  CMD . HEC U  3 .   ? 46.358  27.273  26.972  1.00 20.57 ?  606  HEC C CMD 1 
HETATM 13917 C  CAD . HEC U  3 .   ? 44.494  26.067  29.568  1.00 21.56 ?  606  HEC C CAD 1 
HETATM 13918 C  CBD . HEC U  3 .   ? 45.190  24.702  29.534  1.00 22.42 ?  606  HEC C CBD 1 
HETATM 13919 C  CGD . HEC U  3 .   ? 45.568  24.264  30.927  1.00 23.57 ?  606  HEC C CGD 1 
HETATM 13920 O  O1D . HEC U  3 .   ? 44.778  23.520  31.563  1.00 24.28 ?  606  HEC C O1D 1 
HETATM 13921 O  O2D . HEC U  3 .   ? 46.662  24.655  31.409  1.00 23.84 ?  606  HEC C O2D 1 
HETATM 13922 FE FE  . HEC V  3 .   ? 33.559  20.633  24.317  1.00 19.89 ?  607  HEC C FE  1 
HETATM 13923 C  CHA . HEC V  3 .   ? 34.668  19.137  27.193  1.00 20.66 ?  607  HEC C CHA 1 
HETATM 13924 C  CHB . HEC V  3 .   ? 36.732  21.655  23.621  1.00 19.72 ?  607  HEC C CHB 1 
HETATM 13925 C  CHC . HEC V  3 .   ? 32.546  21.579  21.143  1.00 19.28 ?  607  HEC C CHC 1 
HETATM 13926 C  CHD . HEC V  3 .   ? 30.317  20.322  25.256  1.00 20.45 ?  607  HEC C CHD 1 
HETATM 13927 N  NA  . HEC V  3 .   ? 35.381  20.415  25.251  1.00 20.11 ?  607  HEC C NA  1 
HETATM 13928 C  C1A . HEC V  3 .   ? 35.631  19.772  26.444  1.00 20.30 ?  607  HEC C C1A 1 
HETATM 13929 C  C2A . HEC V  3 .   ? 37.048  19.894  26.744  1.00 20.83 ?  607  HEC C C2A 1 
HETATM 13930 C  C3A . HEC V  3 .   ? 37.611  20.591  25.748  1.00 20.29 ?  607  HEC C C3A 1 
HETATM 13931 C  C4A . HEC V  3 .   ? 36.573  20.937  24.791  1.00 20.11 ?  607  HEC C C4A 1 
HETATM 13932 C  CMA . HEC V  3 .   ? 39.105  20.972  25.623  1.00 19.87 ?  607  HEC C CMA 1 
HETATM 13933 C  CAA . HEC V  3 .   ? 37.769  19.317  27.995  1.00 22.17 ?  607  HEC C CAA 1 
HETATM 13934 C  CBA . HEC V  3 .   ? 37.293  20.096  29.229  1.00 23.53 ?  607  HEC C CBA 1 
HETATM 13935 C  CGA . HEC V  3 .   ? 38.229  19.974  30.410  1.00 24.64 ?  607  HEC C CGA 1 
HETATM 13936 O  O1A . HEC V  3 .   ? 38.107  20.814  31.338  1.00 24.95 ?  607  HEC C O1A 1 
HETATM 13937 O  O2A . HEC V  3 .   ? 39.088  19.053  30.448  1.00 24.66 ?  607  HEC C O2A 1 
HETATM 13938 N  NB  . HEC V  3 .   ? 34.468  21.454  22.666  1.00 18.97 ?  607  HEC C NB  1 
HETATM 13939 C  C1B . HEC V  3 .   ? 35.794  21.843  22.624  1.00 19.32 ?  607  HEC C C1B 1 
HETATM 13940 C  C2B . HEC V  3 .   ? 36.033  22.483  21.348  1.00 19.29 ?  607  HEC C C2B 1 
HETATM 13941 C  C3B . HEC V  3 .   ? 34.887  22.465  20.651  1.00 19.60 ?  607  HEC C C3B 1 
HETATM 13942 C  C4B . HEC V  3 .   ? 33.872  21.818  21.473  1.00 19.65 ?  607  HEC C C4B 1 
HETATM 13943 C  CMB . HEC V  3 .   ? 37.400  23.060  20.905  1.00 19.30 ?  607  HEC C CMB 1 
HETATM 13944 C  CAB . HEC V  3 .   ? 34.663  23.035  19.227  1.00 19.78 ?  607  HEC C CAB 1 
HETATM 13945 C  CBB . HEC V  3 .   ? 35.263  22.483  18.161  1.00 20.49 ?  607  HEC C CBB 1 
HETATM 13946 N  NC  . HEC V  3 .   ? 31.747  20.903  23.367  1.00 19.68 ?  607  HEC C NC  1 
HETATM 13947 C  C1C . HEC V  3 .   ? 31.543  21.263  22.047  1.00 19.92 ?  607  HEC C C1C 1 
HETATM 13948 C  C2C . HEC V  3 .   ? 30.110  21.255  21.802  1.00 19.25 ?  607  HEC C C2C 1 
HETATM 13949 C  C3C . HEC V  3 .   ? 29.492  20.904  22.937  1.00 19.14 ?  607  HEC C C3C 1 
HETATM 13950 C  C4C . HEC V  3 .   ? 30.518  20.684  23.943  1.00 19.66 ?  607  HEC C C4C 1 
HETATM 13951 C  CMC . HEC V  3 .   ? 29.451  21.589  20.443  1.00 19.51 ?  607  HEC C CMC 1 
HETATM 13952 C  CAC . HEC V  3 .   ? 27.961  20.775  23.187  1.00 18.58 ?  607  HEC C CAC 1 
HETATM 13953 C  CBC . HEC V  3 .   ? 27.182  19.901  22.537  1.00 17.41 ?  607  HEC C CBC 1 
HETATM 13954 N  ND  . HEC V  3 .   ? 32.643  19.819  25.956  1.00 20.57 ?  607  HEC C ND  1 
HETATM 13955 C  C1D . HEC V  3 .   ? 31.267  19.887  26.158  1.00 21.19 ?  607  HEC C C1D 1 
HETATM 13956 C  C2D . HEC V  3 .   ? 30.979  19.421  27.491  1.00 21.41 ?  607  HEC C C2D 1 
HETATM 13957 C  C3D . HEC V  3 .   ? 32.335  19.052  28.107  1.00 21.38 ?  607  HEC C C3D 1 
HETATM 13958 C  C4D . HEC V  3 .   ? 33.306  19.329  27.079  1.00 20.88 ?  607  HEC C C4D 1 
HETATM 13959 C  CMD . HEC V  3 .   ? 29.586  19.322  28.148  1.00 22.07 ?  607  HEC C CMD 1 
HETATM 13960 C  CAD . HEC V  3 .   ? 32.600  18.478  29.519  1.00 22.53 ?  607  HEC C CAD 1 
HETATM 13961 C  CBD . HEC V  3 .   ? 31.981  17.088  29.531  1.00 24.12 ?  607  HEC C CBD 1 
HETATM 13962 C  CGD . HEC V  3 .   ? 32.032  16.478  30.897  1.00 25.62 ?  607  HEC C CGD 1 
HETATM 13963 O  O1D . HEC V  3 .   ? 33.005  15.734  31.182  1.00 26.46 ?  607  HEC C O1D 1 
HETATM 13964 O  O2D . HEC V  3 .   ? 31.095  16.734  31.688  1.00 26.62 ?  607  HEC C O2D 1 
HETATM 13965 FE FE  . HEC W  3 .   ? 49.066  34.250  20.451  1.00 20.12 ?  608  HEC C FE  1 
HETATM 13966 C  CHA . HEC W  3 .   ? 48.537  37.583  20.589  1.00 19.84 ?  608  HEC C CHA 1 
HETATM 13967 C  CHB . HEC W  3 .   ? 49.789  34.242  23.842  1.00 19.10 ?  608  HEC C CHB 1 
HETATM 13968 C  CHC . HEC W  3 .   ? 48.912  30.890  20.426  1.00 19.83 ?  608  HEC C CHC 1 
HETATM 13969 C  CHD . HEC W  3 .   ? 49.147  34.311  16.987  1.00 19.49 ?  608  HEC C CHD 1 
HETATM 13970 N  NA  . HEC W  3 .   ? 49.138  35.656  21.967  1.00 19.31 ?  608  HEC C NA  1 
HETATM 13971 C  C1A . HEC W  3 .   ? 48.906  37.001  21.779  1.00 19.54 ?  608  HEC C C1A 1 
HETATM 13972 C  C2A . HEC W  3 .   ? 49.119  37.685  23.040  1.00 20.18 ?  608  HEC C C2A 1 
HETATM 13973 C  C3A . HEC W  3 .   ? 49.470  36.763  23.945  1.00 19.87 ?  608  HEC C C3A 1 
HETATM 13974 C  C4A . HEC W  3 .   ? 49.488  35.466  23.285  1.00 19.52 ?  608  HEC C C4A 1 
HETATM 13975 C  CMA . HEC W  3 .   ? 49.798  37.026  25.435  1.00 18.92 ?  608  HEC C CMA 1 
HETATM 13976 C  CAA . HEC W  3 .   ? 48.963  39.211  23.275  1.00 21.30 ?  608  HEC C CAA 1 
HETATM 13977 C  CBA . HEC W  3 .   ? 50.206  39.936  22.764  1.00 22.93 ?  608  HEC C CBA 1 
HETATM 13978 C  CGA . HEC W  3 .   ? 50.194  41.422  23.048  1.00 24.47 ?  608  HEC C CGA 1 
HETATM 13979 O  O1A . HEC W  3 .   ? 51.077  42.115  22.486  1.00 25.63 ?  608  HEC C O1A 1 
HETATM 13980 O  O2A . HEC W  3 .   ? 49.339  41.935  23.821  1.00 24.57 ?  608  HEC C O2A 1 
HETATM 13981 N  NB  . HEC W  3 .   ? 49.299  32.826  21.883  1.00 18.86 ?  608  HEC C NB  1 
HETATM 13982 C  C1B . HEC W  3 .   ? 49.605  33.021  23.219  1.00 19.29 ?  608  HEC C C1B 1 
HETATM 13983 C  C2B . HEC W  3 .   ? 49.693  31.717  23.844  1.00 19.32 ?  608  HEC C C2B 1 
HETATM 13984 C  C3B . HEC W  3 .   ? 49.451  30.793  22.903  1.00 18.87 ?  608  HEC C C3B 1 
HETATM 13985 C  C4B . HEC W  3 .   ? 49.199  31.472  21.648  1.00 19.21 ?  608  HEC C C4B 1 
HETATM 13986 C  CMB . HEC W  3 .   ? 50.012  31.469  25.341  1.00 18.19 ?  608  HEC C CMB 1 
HETATM 13987 C  CAB . HEC W  3 .   ? 49.428  29.264  23.111  1.00 20.00 ?  608  HEC C CAB 1 
HETATM 13988 C  CBB . HEC W  3 .   ? 48.428  28.716  23.812  1.00 19.12 ?  608  HEC C CBB 1 
HETATM 13989 N  NC  . HEC W  3 .   ? 48.982  32.854  18.957  1.00 19.48 ?  608  HEC C NC  1 
HETATM 13990 C  C1C . HEC W  3 .   ? 49.032  31.494  19.188  1.00 19.43 ?  608  HEC C C1C 1 
HETATM 13991 C  C2C . HEC W  3 .   ? 49.225  30.833  17.909  1.00 19.85 ?  608  HEC C C2C 1 
HETATM 13992 C  C3C . HEC W  3 .   ? 49.290  31.778  16.953  1.00 20.08 ?  608  HEC C C3C 1 
HETATM 13993 C  C4C . HEC W  3 .   ? 49.142  33.072  17.600  1.00 20.06 ?  608  HEC C C4C 1 
HETATM 13994 C  CMC . HEC W  3 .   ? 49.338  29.303  17.716  1.00 18.97 ?  608  HEC C CMC 1 
HETATM 13995 C  CAC . HEC W  3 .   ? 49.513  31.556  15.433  1.00 21.83 ?  608  HEC C CAC 1 
HETATM 13996 C  CBC . HEC W  3 .   ? 48.526  31.099  14.645  1.00 21.47 ?  608  HEC C CBC 1 
HETATM 13997 N  ND  . HEC W  3 .   ? 48.869  35.718  18.997  1.00 19.45 ?  608  HEC C ND  1 
HETATM 13998 C  C1D . HEC W  3 .   ? 48.939  35.524  17.613  1.00 20.29 ?  608  HEC C C1D 1 
HETATM 13999 C  C2D . HEC W  3 .   ? 48.769  36.808  16.959  1.00 19.69 ?  608  HEC C C2D 1 
HETATM 14000 C  C3D . HEC W  3 .   ? 48.576  37.814  18.099  1.00 19.48 ?  608  HEC C C3D 1 
HETATM 14001 C  C4D . HEC W  3 .   ? 48.664  37.051  19.320  1.00 19.49 ?  608  HEC C C4D 1 
HETATM 14002 C  CMD . HEC W  3 .   ? 48.770  37.115  15.443  1.00 20.03 ?  608  HEC C CMD 1 
HETATM 14003 C  CAD . HEC W  3 .   ? 48.361  39.338  17.987  1.00 19.72 ?  608  HEC C CAD 1 
HETATM 14004 C  CBD . HEC W  3 .   ? 49.738  39.970  18.156  1.00 20.34 ?  608  HEC C CBD 1 
HETATM 14005 C  CGD . HEC W  3 .   ? 49.635  41.407  18.590  1.00 20.95 ?  608  HEC C CGD 1 
HETATM 14006 O  O1D . HEC W  3 .   ? 48.895  41.713  19.564  1.00 21.42 ?  608  HEC C O1D 1 
HETATM 14007 O  O2D . HEC W  3 .   ? 50.312  42.248  17.950  1.00 20.60 ?  608  HEC C O2D 1 
HETATM 14008 FE FE  . HEC X  3 .   ? 27.761  21.016  32.107  1.00 23.74 ?  601  HEC E FE  1 
HETATM 14009 C  CHA . HEC X  3 .   ? 31.062  20.636  32.688  1.00 24.27 ?  601  HEC E CHA 1 
HETATM 14010 C  CHB . HEC X  3 .   ? 26.950  18.587  34.201  1.00 23.27 ?  601  HEC E CHB 1 
HETATM 14011 C  CHC . HEC X  3 .   ? 24.782  22.713  32.645  1.00 22.31 ?  601  HEC E CHC 1 
HETATM 14012 C  CHD . HEC X  3 .   ? 28.338  22.620  29.219  1.00 22.84 ?  601  HEC E CHD 1 
HETATM 14013 N  NA  . HEC X  3 .   ? 28.778  19.898  33.280  1.00 24.22 ?  601  HEC E NA  1 
HETATM 14014 C  C1A . HEC X  3 .   ? 30.132  20.272  33.772  1.00 24.57 ?  601  HEC E C1A 1 
HETATM 14015 C  C2A . HEC X  3 .   ? 30.573  19.060  34.611  1.00 25.36 ?  601  HEC E C2A 1 
HETATM 14016 C  C3A . HEC X  3 .   ? 29.433  18.339  34.873  1.00 25.06 ?  601  HEC E C3A 1 
HETATM 14017 C  C4A . HEC X  3 .   ? 28.321  18.918  34.085  1.00 24.33 ?  601  HEC E C4A 1 
HETATM 14018 C  CMA . HEC X  3 .   ? 29.303  17.087  35.648  1.00 24.85 ?  601  HEC E CMA 1 
HETATM 14019 C  CAA . HEC X  3 .   ? 31.995  18.788  34.968  1.00 25.75 ?  601  HEC E CAA 1 
HETATM 14020 C  CBA . HEC X  3 .   ? 32.751  17.784  34.114  1.00 26.02 ?  601  HEC E CBA 1 
HETATM 14021 C  CGA . HEC X  3 .   ? 32.716  16.320  34.525  1.00 26.45 ?  601  HEC E CGA 1 
HETATM 14022 O  O1A . HEC X  3 .   ? 32.388  15.758  35.669  1.00 25.70 ?  601  HEC E O1A 1 
HETATM 14023 O  O2A . HEC X  3 .   ? 32.993  15.326  33.871  1.00 25.44 ?  601  HEC E O2A 1 
HETATM 14024 N  NB  . HEC X  3 .   ? 26.243  20.690  33.191  1.00 23.20 ?  601  HEC E NB  1 
HETATM 14025 C  C1B . HEC X  3 .   ? 25.971  19.471  33.807  1.00 23.26 ?  601  HEC E C1B 1 
HETATM 14026 C  C2B . HEC X  3 .   ? 24.566  19.471  34.235  1.00 23.13 ?  601  HEC E C2B 1 
HETATM 14027 C  C3B . HEC X  3 .   ? 24.162  20.777  34.324  1.00 22.66 ?  601  HEC E C3B 1 
HETATM 14028 C  C4B . HEC X  3 .   ? 25.256  21.658  33.685  1.00 22.69 ?  601  HEC E C4B 1 
HETATM 14029 C  CMB . HEC X  3 .   ? 23.883  18.287  34.807  1.00 22.67 ?  601  HEC E CMB 1 
HETATM 14030 C  CAB . HEC X  3 .   ? 22.774  21.262  34.574  1.00 22.60 ?  601  HEC E CAB 1 
HETATM 14031 C  CBB . HEC X  3 .   ? 22.115  20.838  35.871  1.00 23.13 ?  601  HEC E CBB 1 
HETATM 14032 N  NC  . HEC X  3 .   ? 26.678  22.227  31.072  1.00 23.48 ?  601  HEC E NC  1 
HETATM 14033 C  C1C . HEC X  3 .   ? 25.595  22.912  31.415  1.00 23.23 ?  601  HEC E C1C 1 
HETATM 14034 C  C2C . HEC X  3 .   ? 25.046  23.637  30.233  1.00 23.02 ?  601  HEC E C2C 1 
HETATM 14035 C  C3C . HEC X  3 .   ? 26.046  23.721  29.314  1.00 23.20 ?  601  HEC E C3C 1 
HETATM 14036 C  C4C . HEC X  3 .   ? 26.931  22.525  29.627  1.00 23.58 ?  601  HEC E C4C 1 
HETATM 14037 C  CMC . HEC X  3 .   ? 23.604  23.949  30.053  1.00 22.49 ?  601  HEC E CMC 1 
HETATM 14038 C  CAC . HEC X  3 .   ? 25.957  24.233  27.915  1.00 22.64 ?  601  HEC E CAC 1 
HETATM 14039 C  CBC . HEC X  3 .   ? 25.719  25.736  27.842  1.00 21.87 ?  601  HEC E CBC 1 
HETATM 14040 N  ND  . HEC X  3 .   ? 29.330  21.373  31.062  1.00 24.01 ?  601  HEC E ND  1 
HETATM 14041 C  C1D . HEC X  3 .   ? 29.383  22.343  30.030  1.00 23.45 ?  601  HEC E C1D 1 
HETATM 14042 C  C2D . HEC X  3 .   ? 30.770  22.474  29.613  1.00 23.60 ?  601  HEC E C2D 1 
HETATM 14043 C  C3D . HEC X  3 .   ? 31.537  21.772  30.526  1.00 23.74 ?  601  HEC E C3D 1 
HETATM 14044 C  C4D . HEC X  3 .   ? 30.647  21.323  31.585  1.00 23.62 ?  601  HEC E C4D 1 
HETATM 14045 C  CMD . HEC X  3 .   ? 31.211  22.986  28.300  1.00 23.33 ?  601  HEC E CMD 1 
HETATM 14046 C  CAD . HEC X  3 .   ? 33.011  21.645  30.571  1.00 23.46 ?  601  HEC E CAD 1 
HETATM 14047 C  CBD . HEC X  3 .   ? 33.633  22.872  31.234  1.00 23.91 ?  601  HEC E CBD 1 
HETATM 14048 C  CGD . HEC X  3 .   ? 35.193  22.761  31.105  1.00 24.03 ?  601  HEC E CGD 1 
HETATM 14049 O  O1D . HEC X  3 .   ? 35.786  21.867  31.736  1.00 24.77 ?  601  HEC E O1D 1 
HETATM 14050 O  O2D . HEC X  3 .   ? 35.780  23.596  30.348  1.00 23.58 ?  601  HEC E O2D 1 
HETATM 14051 FE FE  . HEC Y  3 .   ? 9.951   46.213  5.249   1.00 21.63 ?  602  HEC E FE  1 
HETATM 14052 C  CHA . HEC Y  3 .   ? 10.729  44.062  2.642   1.00 21.64 ?  602  HEC E CHA 1 
HETATM 14053 C  CHB . HEC Y  3 .   ? 8.650   48.409  3.034   1.00 22.01 ?  602  HEC E CHB 1 
HETATM 14054 C  CHC . HEC Y  3 .   ? 8.840   48.155  7.870   1.00 21.19 ?  602  HEC E CHC 1 
HETATM 14055 C  CHD . HEC Y  3 .   ? 11.565  44.163  7.444   1.00 21.37 ?  602  HEC E CHD 1 
HETATM 14056 N  NA  . HEC Y  3 .   ? 9.755   46.232  3.218   1.00 21.49 ?  602  HEC E NA  1 
HETATM 14057 C  C1A . HEC Y  3 .   ? 10.128  45.250  2.321   1.00 21.59 ?  602  HEC E C1A 1 
HETATM 14058 C  C2A . HEC Y  3 .   ? 9.768   45.673  0.986   1.00 21.64 ?  602  HEC E C2A 1 
HETATM 14059 C  C3A . HEC Y  3 .   ? 9.194   46.876  1.099   1.00 21.70 ?  602  HEC E C3A 1 
HETATM 14060 C  C4A . HEC Y  3 .   ? 9.169   47.250  2.502   1.00 21.75 ?  602  HEC E C4A 1 
HETATM 14061 C  CMA . HEC Y  3 .   ? 8.645   47.726  -0.056  1.00 21.07 ?  602  HEC E CMA 1 
HETATM 14062 C  CAA . HEC Y  3 .   ? 9.997   44.859  -0.316  1.00 22.21 ?  602  HEC E CAA 1 
HETATM 14063 C  CBA . HEC Y  3 .   ? 11.204  45.348  -1.107  1.00 22.59 ?  602  HEC E CBA 1 
HETATM 14064 C  CGA . HEC Y  3 .   ? 11.822  44.228  -1.911  1.00 23.28 ?  602  HEC E CGA 1 
HETATM 14065 O  O1A . HEC Y  3 .   ? 12.352  44.503  -3.021  1.00 23.58 ?  602  HEC E O1A 1 
HETATM 14066 O  O2A . HEC Y  3 .   ? 11.802  43.058  -1.451  1.00 22.92 ?  602  HEC E O2A 1 
HETATM 14067 N  NB  . HEC Y  3 .   ? 8.972   48.001  5.430   1.00 21.69 ?  602  HEC E NB  1 
HETATM 14068 C  C1B . HEC Y  3 .   ? 8.395   48.661  4.367   1.00 21.64 ?  602  HEC E C1B 1 
HETATM 14069 C  C2B . HEC Y  3 .   ? 7.490   49.655  4.906   1.00 21.34 ?  602  HEC E C2B 1 
HETATM 14070 C  C3B . HEC Y  3 .   ? 7.540   49.586  6.246   1.00 21.52 ?  602  HEC E C3B 1 
HETATM 14071 C  C4B . HEC Y  3 .   ? 8.483   48.547  6.600   1.00 21.62 ?  602  HEC E C4B 1 
HETATM 14072 C  CMB . HEC Y  3 .   ? 6.628   50.613  4.056   1.00 21.65 ?  602  HEC E CMB 1 
HETATM 14073 C  CAB . HEC Y  3 .   ? 6.750   50.454  7.258   1.00 21.78 ?  602  HEC E CAB 1 
HETATM 14074 C  CBB . HEC Y  3 .   ? 5.467   50.181  7.527   1.00 21.63 ?  602  HEC E CBB 1 
HETATM 14075 N  NC  . HEC Y  3 .   ? 10.148  46.166  7.279   1.00 21.18 ?  602  HEC E NC  1 
HETATM 14076 C  C1C . HEC Y  3 .   ? 9.645   47.082  8.184   1.00 20.99 ?  602  HEC E C1C 1 
HETATM 14077 C  C2C . HEC Y  3 .   ? 10.101  46.706  9.509   1.00 20.77 ?  602  HEC E C2C 1 
HETATM 14078 C  C3C . HEC Y  3 .   ? 10.849  45.604  9.380   1.00 20.83 ?  602  HEC E C3C 1 
HETATM 14079 C  C4C . HEC Y  3 .   ? 10.891  45.241  7.977   1.00 21.25 ?  602  HEC E C4C 1 
HETATM 14080 C  CMC . HEC Y  3 .   ? 9.771   47.458  10.821  1.00 19.96 ?  602  HEC E CMC 1 
HETATM 14081 C  CAC . HEC Y  3 .   ? 11.548  44.831  10.515  1.00 21.39 ?  602  HEC E CAC 1 
HETATM 14082 C  CBC . HEC Y  3 .   ? 10.787  44.191  11.411  1.00 21.29 ?  602  HEC E CBC 1 
HETATM 14083 N  ND  . HEC Y  3 .   ? 11.022  44.399  5.059   1.00 21.35 ?  602  HEC E ND  1 
HETATM 14084 C  C1D . HEC Y  3 .   ? 11.510  43.694  6.151   1.00 21.10 ?  602  HEC E C1D 1 
HETATM 14085 C  C2D . HEC Y  3 .   ? 11.945  42.385  5.706   1.00 21.51 ?  602  HEC E C2D 1 
HETATM 14086 C  C3D . HEC Y  3 .   ? 11.682  42.359  4.198   1.00 21.61 ?  602  HEC E C3D 1 
HETATM 14087 C  C4D . HEC Y  3 .   ? 11.111  43.650  3.894   1.00 21.57 ?  602  HEC E C4D 1 
HETATM 14088 C  CMD . HEC Y  3 .   ? 12.557  41.246  6.549   1.00 20.56 ?  602  HEC E CMD 1 
HETATM 14089 C  CAD . HEC Y  3 .   ? 11.937  41.197  3.217   1.00 21.39 ?  602  HEC E CAD 1 
HETATM 14090 C  CBD . HEC Y  3 .   ? 10.581  40.496  3.075   1.00 21.62 ?  602  HEC E CBD 1 
HETATM 14091 C  CGD . HEC Y  3 .   ? 10.596  39.304  2.148   1.00 21.83 ?  602  HEC E CGD 1 
HETATM 14092 O  O1D . HEC Y  3 .   ? 11.630  39.030  1.486   1.00 21.75 ?  602  HEC E O1D 1 
HETATM 14093 O  O2D . HEC Y  3 .   ? 9.551   38.609  2.073   1.00 21.70 ?  602  HEC E O2D 1 
HETATM 14094 FE FE  . HEC Z  3 .   ? 10.745  51.981  -1.641  1.00 24.90 ?  603  HEC E FE  1 
HETATM 14095 C  CHA . HEC Z  3 .   ? 12.374  49.471  -3.271  1.00 24.09 ?  603  HEC E CHA 1 
HETATM 14096 C  CHB . HEC Z  3 .   ? 11.473  50.533  1.382   1.00 24.24 ?  603  HEC E CHB 1 
HETATM 14097 C  CHC . HEC Z  3 .   ? 9.820   54.871  -0.042  1.00 24.45 ?  603  HEC E CHC 1 
HETATM 14098 C  CHD . HEC Z  3 .   ? 9.205   53.015  -4.477  1.00 24.67 ?  603  HEC E CHD 1 
HETATM 14099 N  NA  . HEC Z  3 .   ? 11.742  50.284  -1.051  1.00 24.17 ?  603  HEC E NA  1 
HETATM 14100 C  C1A . HEC Z  3 .   ? 12.379  49.393  -1.890  1.00 24.04 ?  603  HEC E C1A 1 
HETATM 14101 C  C2A . HEC Z  3 .   ? 13.034  48.398  -1.057  1.00 23.94 ?  603  HEC E C2A 1 
HETATM 14102 C  C3A . HEC Z  3 .   ? 12.774  48.695  0.227   1.00 24.04 ?  603  HEC E C3A 1 
HETATM 14103 C  C4A . HEC Z  3 .   ? 11.957  49.892  0.256   1.00 24.22 ?  603  HEC E C4A 1 
HETATM 14104 C  CMA . HEC Z  3 .   ? 13.256  47.920  1.478   1.00 23.82 ?  603  HEC E CMA 1 
HETATM 14105 C  CAA . HEC Z  3 .   ? 13.872  47.199  -1.568  1.00 22.91 ?  603  HEC E CAA 1 
HETATM 14106 C  CBA . HEC Z  3 .   ? 15.238  47.631  -2.090  1.00 22.39 ?  603  HEC E CBA 1 
HETATM 14107 C  CGA . HEC Z  3 .   ? 16.013  46.396  -2.471  1.00 23.36 ?  603  HEC E CGA 1 
HETATM 14108 O  O1A . HEC Z  3 .   ? 16.218  46.155  -3.690  1.00 23.34 ?  603  HEC E O1A 1 
HETATM 14109 O  O2A . HEC Z  3 .   ? 16.418  45.636  -1.555  1.00 23.75 ?  603  HEC E O2A 1 
HETATM 14110 N  NB  . HEC Z  3 .   ? 10.669  52.596  0.327   1.00 24.23 ?  603  HEC E NB  1 
HETATM 14111 C  C1B . HEC Z  3 .   ? 11.006  51.833  1.427   1.00 24.40 ?  603  HEC E C1B 1 
HETATM 14112 C  C2B . HEC Z  3 .   ? 10.774  52.639  2.610   1.00 23.94 ?  603  HEC E C2B 1 
HETATM 14113 C  C3B . HEC Z  3 .   ? 10.318  53.838  2.214   1.00 24.21 ?  603  HEC E C3B 1 
HETATM 14114 C  C4B . HEC Z  3 .   ? 10.245  53.836  0.770   1.00 24.66 ?  603  HEC E C4B 1 
HETATM 14115 C  CMB . HEC Z  3 .   ? 11.019  52.173  4.062   1.00 23.32 ?  603  HEC E CMB 1 
HETATM 14116 C  CAB . HEC Z  3 .   ? 9.938   55.034  3.119   1.00 24.39 ?  603  HEC E CAB 1 
HETATM 14117 C  CBB . HEC Z  3 .   ? 10.922  55.744  3.684   1.00 24.46 ?  603  HEC E CBB 1 
HETATM 14118 N  NC  . HEC Z  3 .   ? 9.731   53.666  -2.176  1.00 24.39 ?  603  HEC E NC  1 
HETATM 14119 C  C1C . HEC Z  3 .   ? 9.390   54.718  -1.346  1.00 24.39 ?  603  HEC E C1C 1 
HETATM 14120 C  C2C . HEC Z  3 .   ? 8.507   55.606  -2.085  1.00 24.25 ?  603  HEC E C2C 1 
HETATM 14121 C  C3C . HEC Z  3 .   ? 8.338   55.089  -3.313  1.00 24.49 ?  603  HEC E C3C 1 
HETATM 14122 C  C4C . HEC Z  3 .   ? 9.106   53.857  -3.391  1.00 24.81 ?  603  HEC E C4C 1 
HETATM 14123 C  CMC . HEC Z  3 .   ? 7.883   56.911  -1.530  1.00 24.23 ?  603  HEC E CMC 1 
HETATM 14124 C  CAC . HEC Z  3 .   ? 7.476   55.682  -4.458  1.00 25.13 ?  603  HEC E CAC 1 
HETATM 14125 C  CBC . HEC Z  3 .   ? 7.860   56.810  -5.071  1.00 23.90 ?  603  HEC E CBC 1 
HETATM 14126 N  ND  . HEC Z  3 .   ? 10.835  51.365  -3.606  1.00 24.24 ?  603  HEC E ND  1 
HETATM 14127 C  C1D . HEC Z  3 .   ? 9.985   51.878  -4.584  1.00 24.84 ?  603  HEC E C1D 1 
HETATM 14128 C  C2D . HEC Z  3 .   ? 10.046  51.014  -5.742  1.00 24.42 ?  603  HEC E C2D 1 
HETATM 14129 C  C3D . HEC Z  3 .   ? 11.034  49.899  -5.381  1.00 24.27 ?  603  HEC E C3D 1 
HETATM 14130 C  C4D . HEC Z  3 .   ? 11.476  50.200  -4.029  1.00 24.40 ?  603  HEC E C4D 1 
HETATM 14131 C  CMD . HEC Z  3 .   ? 9.276   51.179  -7.068  1.00 24.33 ?  603  HEC E CMD 1 
HETATM 14132 C  CAD . HEC Z  3 .   ? 11.444  48.721  -6.291  1.00 23.91 ?  603  HEC E CAD 1 
HETATM 14133 C  CBD . HEC Z  3 .   ? 10.401  47.613  -6.178  1.00 24.34 ?  603  HEC E CBD 1 
HETATM 14134 C  CGD . HEC Z  3 .   ? 10.700  46.759  -4.965  1.00 24.91 ?  603  HEC E CGD 1 
HETATM 14135 O  O1D . HEC Z  3 .   ? 9.846   46.683  -4.045  1.00 24.07 ?  603  HEC E O1D 1 
HETATM 14136 O  O2D . HEC Z  3 .   ? 11.799  46.148  -4.916  1.00 25.26 ?  603  HEC E O2D 1 
HETATM 14137 FE FE  . HEC AA 3 .   ? 18.804  69.990  2.157   1.00 31.59 ?  604  HEC E FE  1 
HETATM 14138 C  CHA . HEC AA 3 .   ? 19.172  69.591  5.587   1.00 30.32 ?  604  HEC E CHA 1 
HETATM 14139 C  CHB . HEC AA 3 .   ? 16.586  67.416  2.082   1.00 30.89 ?  604  HEC E CHB 1 
HETATM 14140 C  CHC . HEC AA 3 .   ? 18.019  70.757  -1.141  1.00 31.83 ?  604  HEC E CHC 1 
HETATM 14141 C  CHD . HEC AA 3 .   ? 21.396  72.171  2.048   1.00 31.93 ?  604  HEC E CHD 1 
HETATM 14142 N  NA  . HEC AA 3 .   ? 18.031  68.727  3.590   1.00 30.86 ?  604  HEC E NA  1 
HETATM 14143 C  C1A . HEC AA 3 .   ? 18.292  68.734  4.949   1.00 30.11 ?  604  HEC E C1A 1 
HETATM 14144 C  C2A . HEC AA 3 .   ? 17.479  67.694  5.556   1.00 29.54 ?  604  HEC E C2A 1 
HETATM 14145 C  C3A . HEC AA 3 .   ? 16.775  67.100  4.584   1.00 30.00 ?  604  HEC E C3A 1 
HETATM 14146 C  C4A . HEC AA 3 .   ? 17.104  67.738  3.323   1.00 30.79 ?  604  HEC E C4A 1 
HETATM 14147 C  CMA . HEC AA 3 .   ? 15.776  65.936  4.756   1.00 29.73 ?  604  HEC E CMA 1 
HETATM 14148 C  CAA . HEC AA 3 .   ? 17.434  67.329  7.058   1.00 27.98 ?  604  HEC E CAA 1 
HETATM 14149 C  CBA . HEC AA 3 .   ? 16.624  68.383  7.798   1.00 27.27 ?  604  HEC E CBA 1 
HETATM 14150 C  CGA . HEC AA 3 .   ? 16.541  68.083  9.272   1.00 26.70 ?  604  HEC E CGA 1 
HETATM 14151 O  O1A . HEC AA 3 .   ? 17.515  67.541  9.868   1.00 26.20 ?  604  HEC E O1A 1 
HETATM 14152 O  O2A . HEC AA 3 .   ? 15.477  68.399  9.853   1.00 26.17 ?  604  HEC E O2A 1 
HETATM 14153 N  NB  . HEC AA 3 .   ? 17.554  69.206  0.706   1.00 31.38 ?  604  HEC E NB  1 
HETATM 14154 C  C1B . HEC AA 3 .   ? 16.668  68.171  0.926   1.00 31.57 ?  604  HEC E C1B 1 
HETATM 14155 C  C2B . HEC AA 3 .   ? 15.854  68.021  -0.267  1.00 31.75 ?  604  HEC E C2B 1 
HETATM 14156 C  C3B . HEC AA 3 .   ? 16.246  68.945  -1.155  1.00 32.06 ?  604  HEC E C3B 1 
HETATM 14157 C  C4B . HEC AA 3 .   ? 17.327  69.709  -0.563  1.00 32.05 ?  604  HEC E C4B 1 
HETATM 14158 C  CMB . HEC AA 3 .   ? 14.727  66.975  -0.463  1.00 31.72 ?  604  HEC E CMB 1 
HETATM 14159 C  CAB . HEC AA 3 .   ? 15.661  69.167  -2.571  1.00 32.89 ?  604  HEC E CAB 1 
HETATM 14160 C  CBB . HEC AA 3 .   ? 14.366  69.471  -2.727  1.00 32.08 ?  604  HEC E CBB 1 
HETATM 14161 N  NC  . HEC AA 3 .   ? 19.540  71.274  0.718   1.00 31.71 ?  604  HEC E NC  1 
HETATM 14162 C  C1C . HEC AA 3 .   ? 19.139  71.366  -0.602  1.00 32.03 ?  604  HEC E C1C 1 
HETATM 14163 C  C2C . HEC AA 3 .   ? 20.094  72.211  -1.298  1.00 32.49 ?  604  HEC E C2C 1 
HETATM 14164 C  C3C . HEC AA 3 .   ? 21.027  72.598  -0.412  1.00 32.79 ?  604  HEC E C3C 1 
HETATM 14165 C  C4C . HEC AA 3 .   ? 20.692  72.014  0.874   1.00 32.21 ?  604  HEC E C4C 1 
HETATM 14166 C  CMC . HEC AA 3 .   ? 20.024  72.577  -2.800  1.00 31.93 ?  604  HEC E CMC 1 
HETATM 14167 C  CAC . HEC AA 3 .   ? 22.265  73.491  -0.674  1.00 34.07 ?  604  HEC E CAC 1 
HETATM 14168 C  CBC . HEC AA 3 .   ? 22.147  74.725  -1.177  1.00 34.19 ?  604  HEC E CBC 1 
HETATM 14169 N  ND  . HEC AA 3 .   ? 20.091  70.760  3.614   1.00 31.32 ?  604  HEC E ND  1 
HETATM 14170 C  C1D . HEC AA 3 .   ? 21.090  71.676  3.302   1.00 31.37 ?  604  HEC E C1D 1 
HETATM 14171 C  C2D . HEC AA 3 .   ? 21.775  72.037  4.519   1.00 31.23 ?  604  HEC E C2D 1 
HETATM 14172 C  C3D . HEC AA 3 .   ? 21.085  71.240  5.639   1.00 31.21 ?  604  HEC E C3D 1 
HETATM 14173 C  C4D . HEC AA 3 .   ? 20.053  70.467  4.979   1.00 31.06 ?  604  HEC E C4D 1 
HETATM 14174 C  CMD . HEC AA 3 .   ? 22.949  73.035  4.654   1.00 31.00 ?  604  HEC E CMD 1 
HETATM 14175 C  CAD . HEC AA 3 .   ? 21.452  71.256  7.142   1.00 31.77 ?  604  HEC E CAD 1 
HETATM 14176 C  CBD . HEC AA 3 .   ? 20.396  71.923  8.017   1.00 32.85 ?  604  HEC E CBD 1 
HETATM 14177 C  CGD . HEC AA 3 .   ? 20.712  71.630  9.466   1.00 34.15 ?  604  HEC E CGD 1 
HETATM 14178 O  O1D . HEC AA 3 .   ? 20.611  72.557  10.312  1.00 34.51 ?  604  HEC E O1D 1 
HETATM 14179 O  O2D . HEC AA 3 .   ? 21.064  70.462  9.786   1.00 34.95 ?  604  HEC E O2D 1 
HETATM 14180 FE FE  . HEC BA 3 .   ? 16.250  60.996  3.583   1.00 26.16 ?  605  HEC E FE  1 
HETATM 14181 C  CHA . HEC BA 3 .   ? 15.994  61.385  6.999   1.00 23.51 ?  605  HEC E CHA 1 
HETATM 14182 C  CHB . HEC BA 3 .   ? 18.629  63.445  3.487   1.00 23.89 ?  605  HEC E CHB 1 
HETATM 14183 C  CHC . HEC BA 3 .   ? 16.611  60.524  0.172   1.00 25.10 ?  605  HEC E CHC 1 
HETATM 14184 C  CHD . HEC BA 3 .   ? 13.784  58.621  3.596   1.00 24.95 ?  605  HEC E CHD 1 
HETATM 14185 N  NA  . HEC BA 3 .   ? 17.152  62.185  4.999   1.00 24.02 ?  605  HEC E NA  1 
HETATM 14186 C  C1A . HEC BA 3 .   ? 16.888  62.213  6.355   1.00 23.98 ?  605  HEC E C1A 1 
HETATM 14187 C  C2A . HEC BA 3 .   ? 17.711  63.252  6.957   1.00 23.44 ?  605  HEC E C2A 1 
HETATM 14188 C  C3A . HEC BA 3 .   ? 18.433  63.810  5.973   1.00 23.70 ?  605  HEC E C3A 1 
HETATM 14189 C  C4A . HEC BA 3 .   ? 18.102  63.148  4.728   1.00 24.05 ?  605  HEC E C4A 1 
HETATM 14190 C  CMA . HEC BA 3 .   ? 19.467  64.952  6.107   1.00 23.06 ?  605  HEC E CMA 1 
HETATM 14191 C  CAA . HEC BA 3 .   ? 17.741  63.669  8.455   1.00 23.04 ?  605  HEC E CAA 1 
HETATM 14192 C  CBA . HEC BA 3 .   ? 18.169  62.560  9.416   1.00 22.74 ?  605  HEC E CBA 1 
HETATM 14193 C  CGA . HEC BA 3 .   ? 19.583  62.115  9.152   1.00 22.42 ?  605  HEC E CGA 1 
HETATM 14194 O  O1A . HEC BA 3 .   ? 20.416  62.953  8.730   1.00 22.52 ?  605  HEC E O1A 1 
HETATM 14195 O  O2A . HEC BA 3 .   ? 19.879  60.912  9.366   1.00 23.07 ?  605  HEC E O2A 1 
HETATM 14196 N  NB  . HEC BA 3 .   ? 17.396  61.820  2.113   1.00 24.57 ?  605  HEC E NB  1 
HETATM 14197 C  C1B . HEC BA 3 .   ? 18.309  62.843  2.288   1.00 24.78 ?  605  HEC E C1B 1 
HETATM 14198 C  C2B . HEC BA 3 .   ? 18.889  63.148  0.993   1.00 24.94 ?  605  HEC E C2B 1 
HETATM 14199 C  C3B . HEC BA 3 .   ? 18.334  62.340  0.090   1.00 25.15 ?  605  HEC E C3B 1 
HETATM 14200 C  C4B . HEC BA 3 .   ? 17.386  61.491  0.770   1.00 25.13 ?  605  HEC E C4B 1 
HETATM 14201 C  CMB . HEC BA 3 .   ? 19.964  64.221  0.710   1.00 25.04 ?  605  HEC E CMB 1 
HETATM 14202 C  CAB . HEC BA 3 .   ? 18.646  62.295  -1.421  1.00 27.08 ?  605  HEC E CAB 1 
HETATM 14203 C  CBB . HEC BA 3 .   ? 19.791  61.736  -1.839  1.00 26.77 ?  605  HEC E CBB 1 
HETATM 14204 N  NC  . HEC BA 3 .   ? 15.380  59.766  2.147   1.00 24.83 ?  605  HEC E NC  1 
HETATM 14205 C  C1C . HEC BA 3 .   ? 15.613  59.805  0.785   1.00 25.44 ?  605  HEC E C1C 1 
HETATM 14206 C  C2C . HEC BA 3 .   ? 14.632  58.964  0.126   1.00 25.43 ?  605  HEC E C2C 1 
HETATM 14207 C  C3C . HEC BA 3 .   ? 13.841  58.439  1.072   1.00 24.87 ?  605  HEC E C3C 1 
HETATM 14208 C  C4C . HEC BA 3 .   ? 14.304  58.932  2.361   1.00 25.16 ?  605  HEC E C4C 1 
HETATM 14209 C  CMC . HEC BA 3 .   ? 14.531  58.734  -1.403  1.00 25.05 ?  605  HEC E CMC 1 
HETATM 14210 C  CAC . HEC BA 3 .   ? 12.641  57.492  0.824   1.00 26.00 ?  605  HEC E CAC 1 
HETATM 14211 C  CBC . HEC BA 3 .   ? 12.864  56.202  0.556   1.00 24.97 ?  605  HEC E CBC 1 
HETATM 14212 N  ND  . HEC BA 3 .   ? 15.040  60.165  5.065   1.00 24.58 ?  605  HEC E ND  1 
HETATM 14213 C  C1D . HEC BA 3 .   ? 14.187  59.087  4.831   1.00 24.61 ?  605  HEC E C1D 1 
HETATM 14214 C  C2D . HEC BA 3 .   ? 13.772  58.538  6.107   1.00 24.32 ?  605  HEC E C2D 1 
HETATM 14215 C  C3D . HEC BA 3 .   ? 14.460  59.404  7.163   1.00 23.80 ?  605  HEC E C3D 1 
HETATM 14216 C  C4D . HEC BA 3 .   ? 15.223  60.391  6.429   1.00 24.27 ?  605  HEC E C4D 1 
HETATM 14217 C  CMD . HEC BA 3 .   ? 12.835  57.339  6.374   1.00 24.56 ?  605  HEC E CMD 1 
HETATM 14218 C  CAD . HEC BA 3 .   ? 14.350  59.252  8.691   1.00 23.00 ?  605  HEC E CAD 1 
HETATM 14219 C  CBD . HEC BA 3 .   ? 13.112  60.017  9.143   1.00 22.39 ?  605  HEC E CBD 1 
HETATM 14220 C  CGD . HEC BA 3 .   ? 13.083  60.137  10.643  1.00 23.15 ?  605  HEC E CGD 1 
HETATM 14221 O  O1D . HEC BA 3 .   ? 14.076  59.747  11.322  1.00 22.53 ?  605  HEC E O1D 1 
HETATM 14222 O  O2D . HEC BA 3 .   ? 12.049  60.636  11.160  1.00 23.67 ?  605  HEC E O2D 1 
HETATM 14223 FE FE  . HEC CA 3 .   ? 11.741  34.480  18.035  1.00 19.30 ?  606  HEC E FE  1 
HETATM 14224 C  CHA . HEC CA 3 .   ? 9.328   34.401  20.433  1.00 18.71 ?  606  HEC E CHA 1 
HETATM 14225 C  CHB . HEC CA 3 .   ? 12.008  37.849  18.298  1.00 18.51 ?  606  HEC E CHB 1 
HETATM 14226 C  CHC . HEC CA 3 .   ? 14.667  34.339  16.274  1.00 18.66 ?  606  HEC E CHC 1 
HETATM 14227 C  CHD . HEC CA 3 .   ? 10.955  31.324  16.986  1.00 18.72 ?  606  HEC E CHD 1 
HETATM 14228 N  NA  . HEC CA 3 .   ? 10.875  35.879  19.225  1.00 18.45 ?  606  HEC E NA  1 
HETATM 14229 C  C1A . HEC CA 3 .   ? 9.771   35.653  20.026  1.00 18.66 ?  606  HEC E C1A 1 
HETATM 14230 C  C2A . HEC CA 3 .   ? 9.194   36.949  20.343  1.00 18.49 ?  606  HEC E C2A 1 
HETATM 14231 C  C3A . HEC CA 3 .   ? 9.937   37.893  19.746  1.00 18.25 ?  606  HEC E C3A 1 
HETATM 14232 C  C4A . HEC CA 3 .   ? 11.015  37.239  19.036  1.00 18.57 ?  606  HEC E C4A 1 
HETATM 14233 C  CMA . HEC CA 3 .   ? 9.720   39.424  19.794  1.00 18.68 ?  606  HEC E CMA 1 
HETATM 14234 C  CAA . HEC CA 3 .   ? 7.925   37.173  21.204  1.00 18.81 ?  606  HEC E CAA 1 
HETATM 14235 C  CBA . HEC CA 3 .   ? 6.703   36.981  20.299  1.00 18.88 ?  606  HEC E CBA 1 
HETATM 14236 C  CGA . HEC CA 3 .   ? 6.176   35.564  20.339  1.00 19.75 ?  606  HEC E CGA 1 
HETATM 14237 O  O1A . HEC CA 3 .   ? 5.930   34.981  19.253  1.00 19.16 ?  606  HEC E O1A 1 
HETATM 14238 O  O2A . HEC CA 3 .   ? 5.983   35.007  21.454  1.00 20.35 ?  606  HEC E O2A 1 
HETATM 14239 N  NB  . HEC CA 3 .   ? 13.086  35.852  17.382  1.00 18.15 ?  606  HEC E NB  1 
HETATM 14240 C  C1B . HEC CA 3 .   ? 13.047  37.200  17.662  1.00 18.88 ?  606  HEC E C1B 1 
HETATM 14241 C  C2B . HEC CA 3 .   ? 14.284  37.786  17.174  1.00 18.53 ?  606  HEC E C2B 1 
HETATM 14242 C  C3B . HEC CA 3 .   ? 15.019  36.812  16.623  1.00 18.90 ?  606  HEC E C3B 1 
HETATM 14243 C  C4B . HEC CA 3 .   ? 14.276  35.578  16.732  1.00 18.58 ?  606  HEC E C4B 1 
HETATM 14244 C  CMB . HEC CA 3 .   ? 14.672  39.274  17.280  1.00 17.71 ?  606  HEC E CMB 1 
HETATM 14245 C  CAB . HEC CA 3 .   ? 16.417  36.956  15.983  1.00 19.59 ?  606  HEC E CAB 1 
HETATM 14246 C  CBB . HEC CA 3 .   ? 17.442  37.420  16.718  1.00 19.28 ?  606  HEC E CBB 1 
HETATM 14247 N  NC  . HEC CA 3 .   ? 12.678  33.037  16.872  1.00 18.33 ?  606  HEC E NC  1 
HETATM 14248 C  C1C . HEC CA 3 .   ? 13.806  33.267  16.106  1.00 19.06 ?  606  HEC E C1C 1 
HETATM 14249 C  C2C . HEC CA 3 .   ? 13.897  32.197  15.129  1.00 18.53 ?  606  HEC E C2C 1 
HETATM 14250 C  C3C . HEC CA 3 .   ? 12.863  31.360  15.321  1.00 18.36 ?  606  HEC E C3C 1 
HETATM 14251 C  C4C . HEC CA 3 .   ? 12.086  31.874  16.434  1.00 18.74 ?  606  HEC E C4C 1 
HETATM 14252 C  CMC . HEC CA 3 .   ? 14.998  32.055  14.059  1.00 18.09 ?  606  HEC E CMC 1 
HETATM 14253 C  CAC . HEC CA 3 .   ? 12.553  30.086  14.496  1.00 18.64 ?  606  HEC E CAC 1 
HETATM 14254 C  CBC . HEC CA 3 .   ? 13.351  29.015  14.569  1.00 17.15 ?  606  HEC E CBC 1 
HETATM 14255 N  ND  . HEC CA 3 .   ? 10.325  33.067  18.628  1.00 18.64 ?  606  HEC E ND  1 
HETATM 14256 C  C1D . HEC CA 3 .   ? 10.266  31.780  18.094  1.00 18.76 ?  606  HEC E C1D 1 
HETATM 14257 C  C2D . HEC CA 3 .   ? 9.347   30.997  18.893  1.00 18.87 ?  606  HEC E C2D 1 
HETATM 14258 C  C3D . HEC CA 3 .   ? 8.837   31.956  19.978  1.00 18.48 ?  606  HEC E C3D 1 
HETATM 14259 C  C4D . HEC CA 3 .   ? 9.488   33.224  19.724  1.00 18.79 ?  606  HEC E C4D 1 
HETATM 14260 C  CMD . HEC CA 3 .   ? 8.961   29.511  18.701  1.00 17.32 ?  606  HEC E CMD 1 
HETATM 14261 C  CAD . HEC CA 3 .   ? 7.814   31.624  21.083  1.00 18.71 ?  606  HEC E CAD 1 
HETATM 14262 C  CBD . HEC CA 3 .   ? 6.458   31.519  20.386  1.00 18.67 ?  606  HEC E CBD 1 
HETATM 14263 C  CGD . HEC CA 3 .   ? 5.356   31.503  21.410  1.00 19.31 ?  606  HEC E CGD 1 
HETATM 14264 O  O1D . HEC CA 3 .   ? 4.926   32.609  21.827  1.00 18.52 ?  606  HEC E O1D 1 
HETATM 14265 O  O2D . HEC CA 3 .   ? 4.917   30.389  21.800  1.00 19.35 ?  606  HEC E O2D 1 
HETATM 14266 FE FE  . HEC DA 3 .   ? 10.128  43.919  16.795  1.00 20.15 ?  607  HEC E FE  1 
HETATM 14267 C  CHA . HEC DA 3 .   ? 7.337   43.632  18.689  1.00 19.94 ?  607  HEC E CHA 1 
HETATM 14268 C  CHB . HEC DA 3 .   ? 9.837   40.671  15.785  1.00 19.78 ?  607  HEC E CHB 1 
HETATM 14269 C  CHC . HEC DA 3 .   ? 12.493  44.476  14.393  1.00 19.40 ?  607  HEC E CHC 1 
HETATM 14270 C  CHD . HEC DA 3 .   ? 11.003  46.841  18.321  1.00 19.49 ?  607  HEC E CHD 1 
HETATM 14271 N  NA  . HEC DA 3 .   ? 8.815   42.434  17.158  1.00 19.90 ?  607  HEC E NA  1 
HETATM 14272 C  C1A . HEC DA 3 .   ? 7.721   42.507  17.996  1.00 19.97 ?  607  HEC E C1A 1 
HETATM 14273 C  C2A . HEC DA 3 .   ? 7.068   41.210  18.003  1.00 19.64 ?  607  HEC E C2A 1 
HETATM 14274 C  C3A . HEC DA 3 .   ? 7.765   40.397  17.195  1.00 19.43 ?  607  HEC E C3A 1 
HETATM 14275 C  C4A . HEC DA 3 .   ? 8.878   41.150  16.652  1.00 20.05 ?  607  HEC E C4A 1 
HETATM 14276 C  CMA . HEC DA 3 .   ? 7.466   38.912  16.877  1.00 19.10 ?  607  HEC E CMA 1 
HETATM 14277 C  CAA . HEC DA 3 .   ? 5.800   40.849  18.815  1.00 19.58 ?  607  HEC E CAA 1 
HETATM 14278 C  CBA . HEC DA 3 .   ? 6.192   40.801  20.298  1.00 21.30 ?  607  HEC E CBA 1 
HETATM 14279 C  CGA . HEC DA 3 .   ? 5.217   40.018  21.145  1.00 21.75 ?  607  HEC E CGA 1 
HETATM 14280 O  O1A . HEC DA 3 .   ? 5.615   39.625  22.271  1.00 21.57 ?  607  HEC E O1A 1 
HETATM 14281 O  O2A . HEC DA 3 .   ? 4.051   39.791  20.722  1.00 21.39 ?  607  HEC E O2A 1 
HETATM 14282 N  NB  . HEC DA 3 .   ? 10.983  42.786  15.318  1.00 19.93 ?  607  HEC E NB  1 
HETATM 14283 C  C1B . HEC DA 3 .   ? 10.794  41.431  15.150  1.00 20.26 ?  607  HEC E C1B 1 
HETATM 14284 C  C2B . HEC DA 3 .   ? 11.765  40.963  14.184  1.00 20.00 ?  607  HEC E C2B 1 
HETATM 14285 C  C3B . HEC DA 3 .   ? 12.500  42.019  13.791  1.00 19.53 ?  607  HEC E C3B 1 
HETATM 14286 C  C4B . HEC DA 3 .   ? 12.020  43.184  14.502  1.00 19.63 ?  607  HEC E C4B 1 
HETATM 14287 C  CMB . HEC DA 3 .   ? 11.890  39.493  13.712  1.00 19.55 ?  607  HEC E CMB 1 
HETATM 14288 C  CAB . HEC DA 3 .   ? 13.667  42.021  12.771  1.00 19.77 ?  607  HEC E CAB 1 
HETATM 14289 C  CBB . HEC DA 3 .   ? 13.418  41.881  11.462  1.00 19.79 ?  607  HEC E CBB 1 
HETATM 14290 N  NC  . HEC DA 3 .   ? 11.498  45.389  16.428  1.00 19.40 ?  607  HEC E NC  1 
HETATM 14291 C  C1C . HEC DA 3 .   ? 12.373  45.446  15.361  1.00 19.57 ?  607  HEC E C1C 1 
HETATM 14292 C  C2C . HEC DA 3 .   ? 13.121  46.688  15.448  1.00 19.15 ?  607  HEC E C2C 1 
HETATM 14293 C  C3C . HEC DA 3 .   ? 12.706  47.345  16.537  1.00 18.83 ?  607  HEC E C3C 1 
HETATM 14294 C  C4C . HEC DA 3 .   ? 11.684  46.534  17.170  1.00 19.51 ?  607  HEC E C4C 1 
HETATM 14295 C  CMC . HEC DA 3 .   ? 14.201  47.152  14.442  1.00 19.19 ?  607  HEC E CMC 1 
HETATM 14296 C  CAC . HEC DA 3 .   ? 13.218  48.713  17.058  1.00 19.72 ?  607  HEC E CAC 1 
HETATM 14297 C  CBC . HEC DA 3 .   ? 13.094  49.836  16.331  1.00 20.05 ?  607  HEC E CBC 1 
HETATM 14298 N  ND  . HEC DA 3 .   ? 9.279   45.076  18.260  1.00 19.83 ?  607  HEC E ND  1 
HETATM 14299 C  C1D . HEC DA 3 .   ? 9.875   46.214  18.788  1.00 19.94 ?  607  HEC E C1D 1 
HETATM 14300 C  C2D . HEC DA 3 .   ? 9.116   46.655  19.930  1.00 20.02 ?  607  HEC E C2D 1 
HETATM 14301 C  C3D . HEC DA 3 .   ? 7.964   45.653  20.059  1.00 20.38 ?  607  HEC E C3D 1 
HETATM 14302 C  C4D . HEC DA 3 .   ? 8.145   44.712  18.975  1.00 20.31 ?  607  HEC E C4D 1 
HETATM 14303 C  CMD . HEC DA 3 .   ? 9.427   47.876  20.818  1.00 19.21 ?  607  HEC E CMD 1 
HETATM 14304 C  CAD . HEC DA 3 .   ? 6.845   45.668  21.117  1.00 21.08 ?  607  HEC E CAD 1 
HETATM 14305 C  CBD . HEC DA 3 .   ? 6.004   46.897  20.826  1.00 22.55 ?  607  HEC E CBD 1 
HETATM 14306 C  CGD . HEC DA 3 .   ? 5.036   47.130  21.942  1.00 23.66 ?  607  HEC E CGD 1 
HETATM 14307 O  O1D . HEC DA 3 .   ? 3.878   46.653  21.827  1.00 23.30 ?  607  HEC E O1D 1 
HETATM 14308 O  O2D . HEC DA 3 .   ? 5.435   47.800  22.925  1.00 24.76 ?  607  HEC E O2D 1 
HETATM 14309 FE FE  . HEC EA 3 .   ? 16.046  23.990  14.338  1.00 21.17 ?  608  HEC E FE  1 
HETATM 14310 C  CHA . HEC EA 3 .   ? 18.980  22.877  15.686  1.00 20.98 ?  608  HEC E CHA 1 
HETATM 14311 C  CHB . HEC EA 3 .   ? 14.419  23.252  17.250  1.00 21.44 ?  608  HEC E CHB 1 
HETATM 14312 C  CHC . HEC EA 3 .   ? 13.342  25.762  13.280  1.00 21.47 ?  608  HEC E CHC 1 
HETATM 14313 C  CHD . HEC EA 3 .   ? 17.379  24.032  11.201  1.00 20.72 ?  608  HEC E CHD 1 
HETATM 14314 N  NA  . HEC EA 3 .   ? 16.608  23.223  16.142  1.00 20.98 ?  608  HEC E NA  1 
HETATM 14315 C  C1A . HEC EA 3 .   ? 17.869  22.789  16.495  1.00 20.91 ?  608  HEC E C1A 1 
HETATM 14316 C  C2A . HEC EA 3 .   ? 17.801  22.241  17.838  1.00 21.44 ?  608  HEC E C2A 1 
HETATM 14317 C  C3A . HEC EA 3 .   ? 16.533  22.345  18.261  1.00 21.36 ?  608  HEC E C3A 1 
HETATM 14318 C  C4A . HEC EA 3 .   ? 15.763  22.970  17.206  1.00 21.50 ?  608  HEC E C4A 1 
HETATM 14319 C  CMA . HEC EA 3 .   ? 15.962  21.896  19.627  1.00 20.25 ?  608  HEC E CMA 1 
HETATM 14320 C  CAA . HEC EA 3 .   ? 18.981  21.635  18.637  1.00 22.15 ?  608  HEC E CAA 1 
HETATM 14321 C  CBA . HEC EA 3 .   ? 19.177  20.188  18.188  1.00 22.67 ?  608  HEC E CBA 1 
HETATM 14322 C  CGA . HEC EA 3 .   ? 20.337  19.509  18.872  1.00 22.67 ?  608  HEC E CGA 1 
HETATM 14323 O  O1A . HEC EA 3 .   ? 20.681  18.390  18.423  1.00 23.71 ?  608  HEC E O1A 1 
HETATM 14324 O  O2A . HEC EA 3 .   ? 20.923  20.050  19.846  1.00 22.96 ?  608  HEC E O2A 1 
HETATM 14325 N  NB  . HEC EA 3 .   ? 14.201  24.424  15.120  1.00 20.71 ?  608  HEC E NB  1 
HETATM 14326 C  C1B . HEC EA 3 .   ? 13.732  24.031  16.353  1.00 20.93 ?  608  HEC E C1B 1 
HETATM 14327 C  C2B . HEC EA 3 .   ? 12.404  24.579  16.533  1.00 21.02 ?  608  HEC E C2B 1 
HETATM 14328 C  C3B . HEC EA 3 .   ? 12.099  25.276  15.428  1.00 20.96 ?  608  HEC E C3B 1 
HETATM 14329 C  C4B . HEC EA 3 .   ? 13.226  25.191  14.524  1.00 20.75 ?  608  HEC E C4B 1 
HETATM 14330 C  CMB . HEC EA 3 .   ? 11.517  24.374  17.785  1.00 20.22 ?  608  HEC E CMB 1 
HETATM 14331 C  CAB . HEC EA 3 .   ? 10.790  26.050  15.164  1.00 22.15 ?  608  HEC E CAB 1 
HETATM 14332 C  CBB . HEC EA 3 .   ? 10.514  27.137  15.898  1.00 21.99 ?  608  HEC E CBB 1 
HETATM 14333 N  NC  . HEC EA 3 .   ? 15.493  24.789  12.578  1.00 20.70 ?  608  HEC E NC  1 
HETATM 14334 C  C1C . HEC EA 3 .   ? 14.283  25.415  12.333  1.00 21.16 ?  608  HEC E C1C 1 
HETATM 14335 C  C2C . HEC EA 3 .   ? 14.170  25.638  10.909  1.00 21.01 ?  608  HEC E C2C 1 
HETATM 14336 C  C3C . HEC EA 3 .   ? 15.282  25.161  10.330  1.00 21.41 ?  608  HEC E C3C 1 
HETATM 14337 C  C4C . HEC EA 3 .   ? 16.139  24.617  11.372  1.00 21.12 ?  608  HEC E C4C 1 
HETATM 14338 C  CMC . HEC EA 3 .   ? 12.960  26.302  10.208  1.00 21.00 ?  608  HEC E CMC 1 
HETATM 14339 C  CAC . HEC EA 3 .   ? 15.598  25.167  8.812   1.00 22.68 ?  608  HEC E CAC 1 
HETATM 14340 C  CBC . HEC EA 3 .   ? 16.030  26.295  8.232   1.00 22.27 ?  608  HEC E CBC 1 
HETATM 14341 N  ND  . HEC EA 3 .   ? 17.912  23.527  13.555  1.00 20.75 ?  608  HEC E ND  1 
HETATM 14342 C  C1D . HEC EA 3 .   ? 18.235  23.613  12.202  1.00 20.98 ?  608  HEC E C1D 1 
HETATM 14343 C  C2D . HEC EA 3 .   ? 19.610  23.185  12.026  1.00 20.73 ?  608  HEC E C2D 1 
HETATM 14344 C  C3D . HEC EA 3 .   ? 20.097  22.835  13.439  1.00 21.08 ?  608  HEC E C3D 1 
HETATM 14345 C  C4D . HEC EA 3 .   ? 18.977  23.071  14.319  1.00 20.88 ?  608  HEC E C4D 1 
HETATM 14346 C  CMD . HEC EA 3 .   ? 20.421  23.109  10.710  1.00 19.52 ?  608  HEC E CMD 1 
HETATM 14347 C  CAD . HEC EA 3 .   ? 21.484  22.310  13.853  1.00 21.18 ?  608  HEC E CAD 1 
HETATM 14348 C  CBD . HEC EA 3 .   ? 21.332  20.797  13.981  1.00 21.39 ?  608  HEC E CBD 1 
HETATM 14349 C  CGD . HEC EA 3 .   ? 22.412  20.216  14.852  1.00 21.91 ?  608  HEC E CGD 1 
HETATM 14350 O  O1D . HEC EA 3 .   ? 22.600  20.677  16.015  1.00 21.66 ?  608  HEC E O1D 1 
HETATM 14351 O  O2D . HEC EA 3 .   ? 23.084  19.275  14.361  1.00 21.65 ?  608  HEC E O2D 1 
HETATM 14352 P  P   . PO4 FA 5 .   ? -15.673 50.314  -1.300  1.00 53.60 ?  609  PO4 E P   1 
HETATM 14353 O  O1  . PO4 FA 5 .   ? -14.748 51.027  -2.261  1.00 54.22 ?  609  PO4 E O1  1 
HETATM 14354 O  O2  . PO4 FA 5 .   ? -14.852 49.528  -0.308  1.00 53.55 ?  609  PO4 E O2  1 
HETATM 14355 O  O3  . PO4 FA 5 .   ? -16.566 49.368  -2.068  1.00 53.28 ?  609  PO4 E O3  1 
HETATM 14356 O  O4  . PO4 FA 5 .   ? -16.514 51.332  -0.569  1.00 53.15 ?  609  PO4 E O4  1 
HETATM 14357 O  O   . HOH GA 6 .   ? 69.853  34.518  21.778  1.00 27.22 ?  701  HOH A O   1 
HETATM 14358 O  O   . HOH GA 6 .   ? 17.925  46.763  26.656  1.00 25.47 ?  702  HOH A O   1 
HETATM 14359 O  O   . HOH GA 6 .   ? 19.208  47.162  9.866   1.00 16.74 ?  703  HOH A O   1 
HETATM 14360 O  O   . HOH GA 6 .   ? 42.084  45.879  21.361  1.00 22.69 ?  704  HOH A O   1 
HETATM 14361 O  O   . HOH GA 6 .   ? 36.237  62.152  32.849  1.00 19.59 ?  705  HOH A O   1 
HETATM 14362 O  O   . HOH GA 6 .   ? 27.949  48.120  53.931  1.00 25.29 ?  706  HOH A O   1 
HETATM 14363 O  O   . HOH GA 6 .   ? 27.826  45.918  28.395  1.00 24.40 ?  707  HOH A O   1 
HETATM 14364 O  O   . HOH GA 6 .   ? 40.410  40.123  57.146  1.00 32.26 ?  708  HOH A O   1 
HETATM 14365 O  O   . HOH GA 6 .   ? 16.088  59.087  13.229  1.00 21.52 ?  709  HOH A O   1 
HETATM 14366 O  O   . HOH GA 6 .   ? 25.399  49.531  33.699  1.00 17.87 ?  710  HOH A O   1 
HETATM 14367 O  O   . HOH GA 6 .   ? 33.515  59.861  26.772  1.00 19.11 ?  711  HOH A O   1 
HETATM 14368 O  O   . HOH GA 6 .   ? 28.692  57.007  18.304  1.00 20.53 ?  712  HOH A O   1 
HETATM 14369 O  O   . HOH GA 6 .   ? 18.664  61.729  37.853  1.00 19.61 ?  713  HOH A O   1 
HETATM 14370 O  O   . HOH GA 6 .   ? 23.074  66.333  41.457  1.00 22.08 ?  714  HOH A O   1 
HETATM 14371 O  O   . HOH GA 6 .   ? 36.054  66.774  13.471  1.00 25.81 ?  715  HOH A O   1 
HETATM 14372 O  O   . HOH GA 6 .   ? 36.211  44.072  52.150  1.00 17.17 ?  716  HOH A O   1 
HETATM 14373 O  O   . HOH GA 6 .   ? 61.409  54.228  27.421  1.00 52.17 ?  717  HOH A O   1 
HETATM 14374 O  O   . HOH GA 6 .   ? 51.392  53.161  52.658  1.00 38.70 ?  718  HOH A O   1 
HETATM 14375 O  O   . HOH GA 6 .   ? 55.280  53.134  39.510  1.00 23.88 ?  719  HOH A O   1 
HETATM 14376 O  O   . HOH GA 6 .   ? 28.977  41.839  4.951   1.00 35.86 ?  720  HOH A O   1 
HETATM 14377 O  O   . HOH GA 6 .   ? 42.312  63.924  17.504  1.00 35.47 ?  721  HOH A O   1 
HETATM 14378 O  O   . HOH GA 6 .   ? 59.357  46.137  46.125  1.00 29.93 ?  722  HOH A O   1 
HETATM 14379 O  O   . HOH GA 6 .   ? 43.145  63.070  14.517  1.00 22.25 ?  723  HOH A O   1 
HETATM 14380 O  O   . HOH GA 6 .   ? 55.611  42.702  8.644   1.00 19.03 ?  724  HOH A O   1 
HETATM 14381 O  O   . HOH GA 6 .   ? 35.893  59.396  1.948   1.00 37.55 ?  725  HOH A O   1 
HETATM 14382 O  O   . HOH GA 6 .   ? 60.588  43.978  -0.065  1.00 24.81 ?  726  HOH A O   1 
HETATM 14383 O  O   . HOH GA 6 .   ? 55.212  36.393  39.671  1.00 22.88 ?  727  HOH A O   1 
HETATM 14384 O  O   . HOH GA 6 .   ? 49.812  49.875  19.717  1.00 21.48 ?  728  HOH A O   1 
HETATM 14385 O  O   . HOH GA 6 .   ? 48.512  48.837  59.841  1.00 49.23 ?  729  HOH A O   1 
HETATM 14386 O  O   . HOH GA 6 .   ? 66.046  52.621  26.740  1.00 54.64 ?  730  HOH A O   1 
HETATM 14387 O  O   . HOH GA 6 .   ? 57.530  62.672  22.577  1.00 23.99 ?  731  HOH A O   1 
HETATM 14388 O  O   . HOH GA 6 .   ? 31.902  63.314  49.055  1.00 59.85 ?  732  HOH A O   1 
HETATM 14389 O  O   . HOH GA 6 .   ? 24.475  71.826  19.585  1.00 31.12 ?  733  HOH A O   1 
HETATM 14390 O  O   . HOH GA 6 .   ? 44.717  36.773  46.203  1.00 22.22 ?  734  HOH A O   1 
HETATM 14391 O  O   . HOH GA 6 .   ? 33.068  44.568  53.851  1.00 18.57 ?  735  HOH A O   1 
HETATM 14392 O  O   . HOH GA 6 .   ? 57.434  25.151  8.667   1.00 35.05 ?  736  HOH A O   1 
HETATM 14393 O  O   . HOH GA 6 .   ? 72.754  41.041  7.555   1.00 26.09 ?  737  HOH A O   1 
HETATM 14394 O  O   . HOH GA 6 .   ? 59.140  54.343  44.114  1.00 30.31 ?  738  HOH A O   1 
HETATM 14395 O  O   . HOH GA 6 .   ? 25.547  49.172  25.676  1.00 18.36 ?  739  HOH A O   1 
HETATM 14396 O  O   . HOH GA 6 .   ? 40.143  48.667  61.797  1.00 40.86 ?  740  HOH A O   1 
HETATM 14397 O  O   . HOH GA 6 .   ? 33.843  69.208  40.374  1.00 29.11 ?  741  HOH A O   1 
HETATM 14398 O  O   . HOH GA 6 .   ? 54.750  58.284  24.651  1.00 30.71 ?  742  HOH A O   1 
HETATM 14399 O  O   . HOH GA 6 .   ? 50.594  59.498  0.118   1.00 37.46 ?  743  HOH A O   1 
HETATM 14400 O  O   . HOH GA 6 .   ? 19.825  48.614  22.471  1.00 11.90 ?  744  HOH A O   1 
HETATM 14401 O  O   . HOH GA 6 .   ? 46.740  57.234  19.303  1.00 20.41 ?  745  HOH A O   1 
HETATM 14402 O  O   . HOH GA 6 .   ? 22.972  48.042  49.864  1.00 28.49 ?  746  HOH A O   1 
HETATM 14403 O  O   . HOH GA 6 .   ? 40.073  53.750  55.331  1.00 47.17 ?  747  HOH A O   1 
HETATM 14404 O  O   . HOH GA 6 .   ? 48.027  61.236  -1.152  1.00 53.36 ?  748  HOH A O   1 
HETATM 14405 O  O   . HOH GA 6 .   ? 41.476  62.009  24.938  1.00 25.36 ?  749  HOH A O   1 
HETATM 14406 O  O   . HOH GA 6 .   ? 30.036  44.898  31.691  1.00 21.71 ?  750  HOH A O   1 
HETATM 14407 O  O   . HOH GA 6 .   ? 34.859  44.224  10.691  1.00 26.36 ?  751  HOH A O   1 
HETATM 14408 O  O   . HOH GA 6 .   ? 71.491  37.945  4.425   1.00 35.54 ?  752  HOH A O   1 
HETATM 14409 O  O   . HOH GA 6 .   ? 27.878  54.436  17.576  1.00 14.10 ?  753  HOH A O   1 
HETATM 14410 O  O   . HOH GA 6 .   ? 58.141  50.222  33.567  1.00 18.89 ?  754  HOH A O   1 
HETATM 14411 O  O   . HOH GA 6 .   ? 54.754  64.960  27.757  1.00 37.80 ?  755  HOH A O   1 
HETATM 14412 O  O   . HOH GA 6 .   ? 24.928  50.551  39.743  1.00 48.54 ?  756  HOH A O   1 
HETATM 14413 O  O   . HOH GA 6 .   ? 43.959  58.511  -2.169  1.00 30.93 ?  757  HOH A O   1 
HETATM 14414 O  O   . HOH GA 6 .   ? 30.531  63.623  41.698  1.00 34.01 ?  758  HOH A O   1 
HETATM 14415 O  O   . HOH GA 6 .   ? 45.489  70.159  16.212  1.00 32.35 ?  759  HOH A O   1 
HETATM 14416 O  O   . HOH GA 6 .   ? 51.102  58.093  -3.534  1.00 38.50 ?  760  HOH A O   1 
HETATM 14417 O  O   . HOH GA 6 .   ? 49.535  54.437  20.291  1.00 27.45 ?  761  HOH A O   1 
HETATM 14418 O  O   . HOH GA 6 .   ? 64.272  39.815  6.119   1.00 22.61 ?  762  HOH A O   1 
HETATM 14419 O  O   . HOH GA 6 .   ? 42.957  55.224  -0.295  1.00 24.65 ?  763  HOH A O   1 
HETATM 14420 O  O   . HOH GA 6 .   ? 48.645  49.337  16.128  1.00 17.89 ?  764  HOH A O   1 
HETATM 14421 O  O   . HOH GA 6 .   ? 55.262  56.945  7.711   1.00 37.83 ?  765  HOH A O   1 
HETATM 14422 O  O   . HOH GA 6 .   ? 34.838  62.412  54.568  1.00 55.42 ?  766  HOH A O   1 
HETATM 14423 O  O   . HOH GA 6 .   ? 43.452  58.617  5.979   1.00 21.12 ?  767  HOH A O   1 
HETATM 14424 O  O   . HOH GA 6 .   ? 56.326  49.031  18.247  1.00 20.53 ?  768  HOH A O   1 
HETATM 14425 O  O   . HOH GA 6 .   ? 54.855  59.484  -6.842  1.00 61.06 ?  769  HOH A O   1 
HETATM 14426 O  O   . HOH GA 6 .   ? 55.801  45.891  33.307  1.00 38.83 ?  770  HOH A O   1 
HETATM 14427 O  O   . HOH GA 6 .   ? 47.906  61.496  8.757   1.00 24.81 ?  771  HOH A O   1 
HETATM 14428 O  O   . HOH GA 6 .   ? 60.707  54.428  -3.683  1.00 35.72 ?  772  HOH A O   1 
HETATM 14429 O  O   . HOH GA 6 .   ? 56.592  59.421  8.117   1.00 23.51 ?  773  HOH A O   1 
HETATM 14430 O  O   . HOH GA 6 .   ? 37.321  50.872  36.824  1.00 28.11 ?  774  HOH A O   1 
HETATM 14431 O  O   . HOH GA 6 .   ? 34.493  55.687  26.608  1.00 18.48 ?  775  HOH A O   1 
HETATM 14432 O  O   . HOH GA 6 .   ? 70.579  30.471  7.682   1.00 40.01 ?  776  HOH A O   1 
HETATM 14433 O  O   . HOH GA 6 .   ? 18.366  60.342  49.219  1.00 34.13 ?  777  HOH A O   1 
HETATM 14434 O  O   . HOH GA 6 .   ? 30.038  71.513  24.876  1.00 28.31 ?  778  HOH A O   1 
HETATM 14435 O  O   . HOH GA 6 .   ? 41.113  43.439  19.354  1.00 22.48 ?  779  HOH A O   1 
HETATM 14436 O  O   . HOH GA 6 .   ? 22.864  43.183  78.295  1.00 47.84 ?  780  HOH A O   1 
HETATM 14437 O  O   . HOH GA 6 .   ? 48.322  62.526  52.712  1.00 59.33 ?  781  HOH A O   1 
HETATM 14438 O  O   . HOH GA 6 .   ? 47.422  43.698  21.514  1.00 27.77 ?  782  HOH A O   1 
HETATM 14439 O  O   . HOH GA 6 .   ? 44.665  52.851  43.072  1.00 22.78 ?  783  HOH A O   1 
HETATM 14440 O  O   . HOH GA 6 .   ? 59.248  40.797  43.298  1.00 39.89 ?  784  HOH A O   1 
HETATM 14441 O  O   . HOH GA 6 .   ? 47.115  55.597  6.438   1.00 28.54 ?  785  HOH A O   1 
HETATM 14442 O  O   . HOH GA 6 .   ? 34.360  68.361  30.114  1.00 25.39 ?  786  HOH A O   1 
HETATM 14443 O  O   . HOH GA 6 .   ? 55.330  46.748  47.438  1.00 22.97 ?  787  HOH A O   1 
HETATM 14444 O  O   . HOH GA 6 .   ? 5.683   42.703  24.947  1.00 26.78 ?  788  HOH A O   1 
HETATM 14445 O  O   . HOH GA 6 .   ? 34.565  44.803  42.749  1.00 17.95 ?  789  HOH A O   1 
HETATM 14446 O  O   . HOH GA 6 .   ? 33.430  42.070  27.027  1.00 41.24 ?  790  HOH A O   1 
HETATM 14447 O  O   . HOH GA 6 .   ? 63.047  53.474  35.658  1.00 31.46 ?  791  HOH A O   1 
HETATM 14448 O  O   . HOH GA 6 .   ? 37.307  52.303  7.652   1.00 22.85 ?  792  HOH A O   1 
HETATM 14449 O  O   . HOH GA 6 .   ? 62.570  46.614  -2.625  1.00 33.54 ?  793  HOH A O   1 
HETATM 14450 O  O   . HOH GA 6 .   ? 32.164  65.585  36.662  1.00 22.28 ?  794  HOH A O   1 
HETATM 14451 O  O   . HOH GA 6 .   ? 27.631  46.524  35.575  1.00 22.59 ?  795  HOH A O   1 
HETATM 14452 O  O   . HOH GA 6 .   ? 67.389  66.174  6.335   1.00 42.68 ?  796  HOH A O   1 
HETATM 14453 O  O   . HOH GA 6 .   ? 26.360  50.921  27.813  1.00 26.49 ?  797  HOH A O   1 
HETATM 14454 O  O   . HOH GA 6 .   ? 37.485  52.477  10.234  1.00 23.96 ?  798  HOH A O   1 
HETATM 14455 O  O   . HOH GA 6 .   ? 71.342  54.029  14.345  1.00 54.07 ?  799  HOH A O   1 
HETATM 14456 O  O   . HOH GA 6 .   ? 48.146  43.321  11.259  1.00 22.86 ?  800  HOH A O   1 
HETATM 14457 O  O   . HOH GA 6 .   ? 20.685  44.509  35.286  1.00 23.99 ?  801  HOH A O   1 
HETATM 14458 O  O   . HOH GA 6 .   ? 24.950  43.740  48.632  1.00 28.12 ?  802  HOH A O   1 
HETATM 14459 O  O   . HOH GA 6 .   ? 64.594  51.931  21.938  1.00 38.95 ?  803  HOH A O   1 
HETATM 14460 O  O   . HOH GA 6 .   ? 61.291  54.134  39.633  1.00 42.62 ?  804  HOH A O   1 
HETATM 14461 O  O   . HOH GA 6 .   ? 65.787  39.446  8.423   1.00 27.51 ?  805  HOH A O   1 
HETATM 14462 O  O   . HOH GA 6 .   ? 71.836  42.985  5.587   1.00 31.84 ?  806  HOH A O   1 
HETATM 14463 O  O   . HOH GA 6 .   ? 28.560  64.136  53.239  1.00 46.88 ?  807  HOH A O   1 
HETATM 14464 O  O   . HOH GA 6 .   ? 49.640  44.452  25.168  1.00 22.11 ?  808  HOH A O   1 
HETATM 14465 O  O   . HOH GA 6 .   ? 45.728  41.033  48.435  1.00 24.97 ?  809  HOH A O   1 
HETATM 14466 O  O   . HOH GA 6 .   ? 62.948  46.140  38.633  1.00 26.10 ?  810  HOH A O   1 
HETATM 14467 O  O   . HOH GA 6 .   ? 54.728  43.029  38.190  1.00 23.02 ?  811  HOH A O   1 
HETATM 14468 O  O   . HOH GA 6 .   ? 48.561  59.641  7.031   1.00 26.17 ?  812  HOH A O   1 
HETATM 14469 O  O   . HOH GA 6 .   ? 60.218  63.034  4.660   1.00 35.46 ?  813  HOH A O   1 
HETATM 14470 O  O   . HOH GA 6 .   ? 45.511  49.647  3.552   1.00 20.86 ?  814  HOH A O   1 
HETATM 14471 O  O   . HOH GA 6 .   ? 50.530  44.286  5.322   1.00 22.04 ?  815  HOH A O   1 
HETATM 14472 O  O   . HOH GA 6 .   ? 27.598  63.421  46.363  1.00 36.57 ?  816  HOH A O   1 
HETATM 14473 O  O   . HOH GA 6 .   ? 73.779  59.066  0.391   1.00 46.92 ?  817  HOH A O   1 
HETATM 14474 O  O   . HOH GA 6 .   ? 47.589  57.095  36.801  1.00 36.20 ?  818  HOH A O   1 
HETATM 14475 O  O   . HOH GA 6 .   ? 53.940  66.727  5.385   1.00 40.24 ?  819  HOH A O   1 
HETATM 14476 O  O   . HOH GA 6 .   ? 28.749  46.429  44.897  1.00 27.32 ?  820  HOH A O   1 
HETATM 14477 O  O   . HOH GA 6 .   ? 39.002  52.720  5.233   1.00 32.98 ?  821  HOH A O   1 
HETATM 14478 O  O   . HOH GA 6 .   ? 60.013  43.949  -2.674  1.00 28.80 ?  822  HOH A O   1 
HETATM 14479 O  O   . HOH GA 6 .   ? 66.450  46.123  24.509  1.00 39.51 ?  823  HOH A O   1 
HETATM 14480 O  O   . HOH GA 6 .   ? 64.406  26.946  7.046   1.00 27.17 ?  824  HOH A O   1 
HETATM 14481 O  O   . HOH GA 6 .   ? 46.154  46.445  5.106   1.00 31.74 ?  825  HOH A O   1 
HETATM 14482 O  O   . HOH GA 6 .   ? 58.468  57.918  34.674  1.00 34.13 ?  826  HOH A O   1 
HETATM 14483 O  O   . HOH GA 6 .   ? 46.149  47.622  58.692  1.00 41.86 ?  827  HOH A O   1 
HETATM 14484 O  O   . HOH GA 6 .   ? 25.245  69.189  23.300  1.00 27.51 ?  828  HOH A O   1 
HETATM 14485 O  O   . HOH GA 6 .   ? 42.950  54.469  44.947  1.00 29.73 ?  829  HOH A O   1 
HETATM 14486 O  O   . HOH GA 6 .   ? 56.244  42.741  42.095  1.00 30.67 ?  830  HOH A O   1 
HETATM 14487 O  O   . HOH GA 6 .   ? 35.448  50.287  5.556   1.00 36.19 ?  831  HOH A O   1 
HETATM 14488 O  O   . HOH GA 6 .   ? 57.033  53.990  31.445  1.00 28.33 ?  832  HOH A O   1 
HETATM 14489 O  O   . HOH GA 6 .   ? 31.171  51.688  62.209  1.00 30.87 ?  833  HOH A O   1 
HETATM 14490 O  O   . HOH GA 6 .   ? 36.448  77.505  27.659  1.00 46.45 ?  834  HOH A O   1 
HETATM 14491 O  O   . HOH GA 6 .   ? 34.669  49.631  56.790  1.00 27.67 ?  835  HOH A O   1 
HETATM 14492 O  O   . HOH GA 6 .   ? 61.628  47.508  42.684  1.00 30.65 ?  836  HOH A O   1 
HETATM 14493 O  O   . HOH GA 6 .   ? 13.452  47.003  57.855  1.00 24.52 ?  837  HOH A O   1 
HETATM 14494 O  O   . HOH GA 6 .   ? 62.692  30.095  26.273  1.00 31.86 ?  838  HOH A O   1 
HETATM 14495 O  O   . HOH GA 6 .   ? 30.161  44.634  28.979  1.00 28.69 ?  839  HOH A O   1 
HETATM 14496 O  O   . HOH GA 6 .   ? 47.133  59.656  3.489   1.00 45.22 ?  840  HOH A O   1 
HETATM 14497 O  O   . HOH GA 6 .   ? 57.308  75.720  14.843  1.00 30.74 ?  841  HOH A O   1 
HETATM 14498 O  O   . HOH GA 6 .   ? 78.486  39.911  8.472   1.00 34.60 ?  842  HOH A O   1 
HETATM 14499 O  O   . HOH GA 6 .   ? 50.459  55.987  -12.484 1.00 41.59 ?  843  HOH A O   1 
HETATM 14500 O  O   . HOH GA 6 .   ? 27.710  47.105  41.613  1.00 30.20 ?  844  HOH A O   1 
HETATM 14501 O  O   . HOH GA 6 .   ? 37.767  76.626  29.662  1.00 40.17 ?  845  HOH A O   1 
HETATM 14502 O  O   . HOH GA 6 .   ? 33.777  46.031  39.678  1.00 26.52 ?  846  HOH A O   1 
HETATM 14503 O  O   . HOH GA 6 .   ? 40.049  62.912  16.724  1.00 24.32 ?  847  HOH A O   1 
HETATM 14504 O  O   . HOH GA 6 .   ? 57.161  57.003  26.869  1.00 34.70 ?  848  HOH A O   1 
HETATM 14505 O  O   . HOH GA 6 .   ? 39.646  66.221  38.232  1.00 26.52 ?  849  HOH A O   1 
HETATM 14506 O  O   . HOH GA 6 .   ? 64.447  51.836  18.921  1.00 34.28 ?  850  HOH A O   1 
HETATM 14507 O  O   . HOH GA 6 .   ? 48.891  57.086  8.367   1.00 26.10 ?  851  HOH A O   1 
HETATM 14508 O  O   . HOH GA 6 .   ? 45.397  68.510  31.675  1.00 30.11 ?  852  HOH A O   1 
HETATM 14509 O  O   . HOH GA 6 .   ? 27.960  49.978  56.040  1.00 25.59 ?  853  HOH A O   1 
HETATM 14510 O  O   . HOH GA 6 .   ? 30.416  45.999  14.649  1.00 30.85 ?  854  HOH A O   1 
HETATM 14511 O  O   . HOH GA 6 .   ? 23.225  54.442  4.739   1.00 26.09 ?  855  HOH A O   1 
HETATM 14512 O  O   . HOH GA 6 .   ? 21.258  42.807  43.725  1.00 29.74 ?  856  HOH A O   1 
HETATM 14513 O  O   . HOH GA 6 .   ? 26.919  49.616  41.850  1.00 21.55 ?  857  HOH A O   1 
HETATM 14514 O  O   . HOH GA 6 .   ? 37.917  61.269  21.047  1.00 23.61 ?  858  HOH A O   1 
HETATM 14515 O  O   . HOH GA 6 .   ? 48.963  40.036  12.165  1.00 34.47 ?  859  HOH A O   1 
HETATM 14516 O  O   . HOH GA 6 .   ? 24.939  72.543  8.213   1.00 30.74 ?  860  HOH A O   1 
HETATM 14517 O  O   . HOH GA 6 .   ? 64.476  61.451  -0.217  1.00 42.74 ?  861  HOH A O   1 
HETATM 14518 O  O   . HOH GA 6 .   ? 54.739  57.627  5.343   1.00 35.38 ?  862  HOH A O   1 
HETATM 14519 O  O   . HOH GA 6 .   ? 70.207  48.681  -0.377  1.00 42.55 ?  863  HOH A O   1 
HETATM 14520 O  O   . HOH GA 6 .   ? 46.378  67.189  12.693  1.00 36.65 ?  864  HOH A O   1 
HETATM 14521 O  O   . HOH GA 6 .   ? 67.072  50.978  14.183  1.00 38.10 ?  865  HOH A O   1 
HETATM 14522 O  O   . HOH GA 6 .   ? 38.572  45.113  2.247   1.00 27.55 ?  866  HOH A O   1 
HETATM 14523 O  O   . HOH GA 6 .   ? 63.944  45.930  23.321  1.00 19.97 ?  867  HOH A O   1 
HETATM 14524 O  O   . HOH GA 6 .   ? 67.443  62.857  -1.198  1.00 46.99 ?  868  HOH A O   1 
HETATM 14525 O  O   . HOH GA 6 .   ? 65.806  52.975  15.443  1.00 40.29 ?  869  HOH A O   1 
HETATM 14526 O  O   . HOH GA 6 .   ? 24.448  46.903  2.138   1.00 43.23 ?  870  HOH A O   1 
HETATM 14527 O  O   . HOH GA 6 .   ? 56.025  67.983  26.933  1.00 41.85 ?  871  HOH A O   1 
HETATM 14528 O  O   . HOH GA 6 .   ? 35.738  48.844  37.803  1.00 23.91 ?  872  HOH A O   1 
HETATM 14529 O  O   . HOH GA 6 .   ? 64.884  67.116  4.584   1.00 50.37 ?  873  HOH A O   1 
HETATM 14530 O  O   . HOH GA 6 .   ? 35.049  59.879  9.646   1.00 33.99 ?  874  HOH A O   1 
HETATM 14531 O  O   . HOH GA 6 .   ? 72.129  41.608  32.325  1.00 55.75 ?  875  HOH A O   1 
HETATM 14532 O  O   . HOH GA 6 .   ? 59.000  63.456  8.083   1.00 33.10 ?  876  HOH A O   1 
HETATM 14533 O  O   . HOH GA 6 .   ? 22.197  46.142  24.943  1.00 25.20 ?  877  HOH A O   1 
HETATM 14534 O  O   . HOH GA 6 .   ? 55.829  58.089  35.459  1.00 39.01 ?  878  HOH A O   1 
HETATM 14535 O  O   . HOH GA 6 .   ? 57.180  35.797  35.909  1.00 31.15 ?  879  HOH A O   1 
HETATM 14536 O  O   . HOH GA 6 .   ? 59.055  67.798  11.326  1.00 26.82 ?  880  HOH A O   1 
HETATM 14537 O  O   . HOH GA 6 .   ? 36.858  51.754  3.746   1.00 34.39 ?  881  HOH A O   1 
HETATM 14538 O  O   . HOH GA 6 .   ? 48.255  49.677  -9.151  1.00 45.82 ?  882  HOH A O   1 
HETATM 14539 O  O   . HOH GA 6 .   ? 40.732  52.718  52.332  1.00 30.58 ?  883  HOH A O   1 
HETATM 14540 O  O   . HOH GA 6 .   ? 78.230  35.461  21.663  1.00 50.21 ?  884  HOH A O   1 
HETATM 14541 O  O   . HOH GA 6 .   ? 40.954  56.644  44.029  1.00 33.94 ?  885  HOH A O   1 
HETATM 14542 O  O   . HOH GA 6 .   ? 55.974  52.950  51.772  1.00 31.14 ?  886  HOH A O   1 
HETATM 14543 O  O   . HOH GA 6 .   ? 67.285  27.078  16.110  1.00 38.24 ?  887  HOH A O   1 
HETATM 14544 O  O   . HOH GA 6 .   ? 58.005  56.890  -9.446  1.00 37.79 ?  888  HOH A O   1 
HETATM 14545 O  O   . HOH GA 6 .   ? 45.432  43.899  24.744  1.00 23.10 ?  889  HOH A O   1 
HETATM 14546 O  O   . HOH GA 6 .   ? 63.303  49.871  40.701  1.00 41.49 ?  890  HOH A O   1 
HETATM 14547 O  O   . HOH GA 6 .   ? 59.900  70.361  10.403  1.00 38.55 ?  891  HOH A O   1 
HETATM 14548 O  O   . HOH GA 6 .   ? 25.294  45.549  50.619  1.00 38.56 ?  892  HOH A O   1 
HETATM 14549 O  O   . HOH GA 6 .   ? 72.917  27.898  20.898  1.00 44.62 ?  893  HOH A O   1 
HETATM 14550 O  O   . HOH GA 6 .   ? 58.572  48.000  52.518  1.00 53.14 ?  894  HOH A O   1 
HETATM 14551 O  O   . HOH GA 6 .   ? 53.370  45.771  6.466   1.00 22.69 ?  895  HOH A O   1 
HETATM 14552 O  O   . HOH GA 6 .   ? 69.330  66.853  10.394  1.00 27.41 ?  896  HOH A O   1 
HETATM 14553 O  O   . HOH GA 6 .   ? 42.874  57.294  41.522  1.00 42.98 ?  897  HOH A O   1 
HETATM 14554 O  O   . HOH GA 6 .   ? 61.047  68.158  7.896   1.00 41.67 ?  898  HOH A O   1 
HETATM 14555 O  O   . HOH GA 6 .   ? 37.586  50.457  -3.463  1.00 35.97 ?  899  HOH A O   1 
HETATM 14556 O  O   . HOH GA 6 .   ? 32.413  66.499  53.870  1.00 51.67 ?  900  HOH A O   1 
HETATM 14557 O  O   . HOH GA 6 .   ? 61.829  80.017  14.952  1.00 41.56 ?  901  HOH A O   1 
HETATM 14558 O  O   . HOH GA 6 .   ? 68.185  44.353  23.345  1.00 55.89 ?  902  HOH A O   1 
HETATM 14559 O  O   . HOH GA 6 .   ? 47.539  46.692  1.869   1.00 33.60 ?  903  HOH A O   1 
HETATM 14560 O  O   . HOH GA 6 .   ? 65.264  40.704  30.461  1.00 39.99 ?  904  HOH A O   1 
HETATM 14561 O  O   . HOH GA 6 .   ? 16.687  55.614  53.084  1.00 24.27 ?  905  HOH A O   1 
HETATM 14562 O  O   . HOH GA 6 .   ? 31.369  67.005  38.757  1.00 23.73 ?  906  HOH A O   1 
HETATM 14563 O  O   . HOH GA 6 .   ? 32.820  49.782  63.335  1.00 32.84 ?  907  HOH A O   1 
HETATM 14564 O  O   . HOH GA 6 .   ? 18.610  53.300  16.914  1.00 26.44 ?  908  HOH A O   1 
HETATM 14565 O  O   . HOH GA 6 .   ? 71.374  37.466  26.484  1.00 31.26 ?  909  HOH A O   1 
HETATM 14566 O  O   . HOH GA 6 .   ? 48.531  42.705  4.605   1.00 37.21 ?  910  HOH A O   1 
HETATM 14567 O  O   . HOH GA 6 .   ? 53.227  45.266  44.402  1.00 25.91 ?  911  HOH A O   1 
HETATM 14568 O  O   . HOH GA 6 .   ? 75.265  31.433  10.239  1.00 44.91 ?  912  HOH A O   1 
HETATM 14569 O  O   . HOH GA 6 .   ? 33.309  61.868  9.036   1.00 29.29 ?  913  HOH A O   1 
HETATM 14570 O  O   . HOH GA 6 .   ? 23.069  70.578  26.614  1.00 44.59 ?  914  HOH A O   1 
HETATM 14571 O  O   . HOH GA 6 .   ? 61.497  41.384  0.848   1.00 26.15 ?  915  HOH A O   1 
HETATM 14572 O  O   . HOH GA 6 .   ? 32.594  38.446  7.823   1.00 48.28 ?  916  HOH A O   1 
HETATM 14573 O  O   . HOH GA 6 .   ? 32.462  65.158  40.562  1.00 35.04 ?  917  HOH A O   1 
HETATM 14574 O  O   . HOH GA 6 .   ? 47.330  68.523  6.906   1.00 46.31 ?  918  HOH A O   1 
HETATM 14575 O  O   . HOH GA 6 .   ? 68.229  55.786  25.414  1.00 61.65 ?  919  HOH A O   1 
HETATM 14576 O  O   . HOH GA 6 .   ? 32.096  44.688  13.102  1.00 46.70 ?  920  HOH A O   1 
HETATM 14577 O  O   . HOH GA 6 .   ? 73.617  51.839  14.550  1.00 43.72 ?  921  HOH A O   1 
HETATM 14578 O  O   . HOH GA 6 .   ? 15.804  47.449  33.721  1.00 22.72 ?  922  HOH A O   1 
HETATM 14579 O  O   . HOH GA 6 .   ? 46.851  45.980  55.875  1.00 33.04 ?  923  HOH A O   1 
HETATM 14580 O  O   . HOH GA 6 .   ? 29.122  39.502  13.146  1.00 37.19 ?  924  HOH A O   1 
HETATM 14581 O  O   . HOH GA 6 .   ? 50.426  37.472  12.244  1.00 24.90 ?  925  HOH A O   1 
HETATM 14582 O  O   . HOH GA 6 .   ? 32.516  45.848  10.726  1.00 33.59 ?  926  HOH A O   1 
HETATM 14583 O  O   . HOH GA 6 .   ? 25.392  42.433  51.057  1.00 39.47 ?  927  HOH A O   1 
HETATM 14584 O  O   . HOH GA 6 .   ? 70.193  65.130  8.579   1.00 31.71 ?  928  HOH A O   1 
HETATM 14585 O  O   . HOH GA 6 .   ? 43.766  47.913  -5.126  1.00 34.82 ?  929  HOH A O   1 
HETATM 14586 O  O   . HOH GA 6 .   ? 19.442  44.676  52.363  1.00 48.24 ?  930  HOH A O   1 
HETATM 14587 O  O   . HOH GA 6 .   ? 66.118  60.749  26.991  1.00 51.03 ?  931  HOH A O   1 
HETATM 14588 O  O   . HOH GA 6 .   ? 59.919  52.699  29.442  1.00 27.34 ?  932  HOH A O   1 
HETATM 14589 O  O   . HOH GA 6 .   ? 50.628  64.399  32.727  1.00 36.42 ?  933  HOH A O   1 
HETATM 14590 O  O   . HOH GA 6 .   ? 59.175  45.887  53.897  1.00 46.92 ?  934  HOH A O   1 
HETATM 14591 O  O   . HOH GA 6 .   ? 51.984  65.558  28.948  1.00 42.91 ?  935  HOH A O   1 
HETATM 14592 O  O   . HOH GA 6 .   ? 48.045  52.175  53.752  1.00 34.89 ?  936  HOH A O   1 
HETATM 14593 O  O   . HOH GA 6 .   ? 57.410  47.014  49.502  1.00 31.40 ?  937  HOH A O   1 
HETATM 14594 O  O   . HOH GA 6 .   ? 30.885  81.902  24.747  1.00 47.25 ?  938  HOH A O   1 
HETATM 14595 O  O   . HOH GA 6 .   ? 58.461  54.923  -5.124  1.00 29.97 ?  939  HOH A O   1 
HETATM 14596 O  O   . HOH GA 6 .   ? 37.800  71.633  18.208  1.00 38.95 ?  940  HOH A O   1 
HETATM 14597 O  O   . HOH GA 6 .   ? 38.664  59.552  51.452  1.00 40.95 ?  941  HOH A O   1 
HETATM 14598 O  O   . HOH GA 6 .   ? 29.348  64.125  48.856  1.00 42.07 ?  942  HOH A O   1 
HETATM 14599 O  O   . HOH GA 6 .   ? 17.523  44.890  44.673  1.00 25.24 ?  943  HOH A O   1 
HETATM 14600 O  O   . HOH GA 6 .   ? 34.393  68.211  43.007  1.00 53.67 ?  944  HOH A O   1 
HETATM 14601 O  O   . HOH GA 6 .   ? 43.598  41.164  50.789  1.00 30.89 ?  945  HOH A O   1 
HETATM 14602 O  O   . HOH GA 6 .   ? 60.648  56.396  35.842  1.00 36.38 ?  946  HOH A O   1 
HETATM 14603 O  O   . HOH GA 6 .   ? 57.783  64.750  36.346  1.00 52.94 ?  947  HOH A O   1 
HETATM 14604 O  O   . HOH GA 6 .   ? 37.580  59.727  -4.494  1.00 54.57 ?  948  HOH A O   1 
HETATM 14605 O  O   . HOH GA 6 .   ? 57.883  36.961  39.048  1.00 49.48 ?  949  HOH A O   1 
HETATM 14606 O  O   . HOH GA 6 .   ? 25.923  75.836  11.483  1.00 52.96 ?  950  HOH A O   1 
HETATM 14607 O  O   . HOH GA 6 .   ? 15.654  71.544  17.093  1.00 46.49 ?  951  HOH A O   1 
HETATM 14608 O  O   . HOH GA 6 .   ? 23.570  46.915  43.306  1.00 39.97 ?  952  HOH A O   1 
HETATM 14609 O  O   . HOH GA 6 .   ? 60.074  65.850  9.422   1.00 33.44 ?  953  HOH A O   1 
HETATM 14610 O  O   . HOH GA 6 .   ? 51.307  58.882  40.905  1.00 41.55 ?  954  HOH A O   1 
HETATM 14611 O  O   . HOH GA 6 .   ? 56.155  58.578  -10.230 1.00 49.09 ?  955  HOH A O   1 
HETATM 14612 O  O   . HOH GA 6 .   ? 22.581  53.010  87.516  1.00 52.11 ?  956  HOH A O   1 
HETATM 14613 O  O   . HOH GA 6 .   ? 45.588  67.600  10.287  1.00 36.06 ?  957  HOH A O   1 
HETATM 14614 O  O   . HOH GA 6 .   ? 32.007  56.938  25.608  1.00 21.28 ?  958  HOH A O   1 
HETATM 14615 O  O   . HOH GA 6 .   ? 52.055  68.763  28.358  1.00 51.89 ?  959  HOH A O   1 
HETATM 14616 O  O   . HOH GA 6 .   ? 31.254  79.848  29.029  1.00 42.66 ?  960  HOH A O   1 
HETATM 14617 O  O   . HOH GA 6 .   ? 57.613  67.184  32.774  1.00 41.98 ?  961  HOH A O   1 
HETATM 14618 O  O   . HOH GA 6 .   ? 66.414  61.251  29.627  1.00 44.44 ?  962  HOH A O   1 
HETATM 14619 O  O   . HOH GA 6 .   ? 55.222  61.484  -9.052  1.00 50.08 ?  963  HOH A O   1 
HETATM 14620 O  O   . HOH GA 6 .   ? 50.060  58.220  43.139  1.00 45.93 ?  964  HOH A O   1 
HETATM 14621 O  O   . HOH GA 6 .   ? 36.902  68.825  43.758  1.00 51.90 ?  965  HOH A O   1 
HETATM 14622 O  O   . HOH GA 6 .   ? 14.813  44.900  58.831  1.00 32.59 ?  966  HOH A O   1 
HETATM 14623 O  O   . HOH GA 6 .   ? 54.503  62.044  -11.613 1.00 45.41 ?  967  HOH A O   1 
HETATM 14624 O  O   . HOH GA 6 .   ? 39.984  50.631  33.075  1.00 24.57 ?  968  HOH A O   1 
HETATM 14625 O  O   . HOH GA 6 .   ? 38.260  47.546  31.901  1.00 40.20 ?  969  HOH A O   1 
HETATM 14626 O  O   . HOH GA 6 .   ? 37.492  43.792  28.487  1.00 20.40 ?  970  HOH A O   1 
HETATM 14627 O  O   . HOH GA 6 .   ? 11.025  47.024  27.061  1.00 28.12 ?  971  HOH A O   1 
HETATM 14628 O  O   . HOH GA 6 .   ? 44.648  42.735  46.126  1.00 22.07 ?  972  HOH A O   1 
HETATM 14629 O  O   . HOH GA 6 .   ? 61.584  33.081  1.760   1.00 30.76 ?  973  HOH A O   1 
HETATM 14630 O  O   . HOH GA 6 .   ? 52.027  40.701  -0.793  1.00 35.25 ?  974  HOH A O   1 
HETATM 14631 O  O   . HOH GA 6 .   ? 59.228  50.118  26.147  1.00 23.00 ?  975  HOH A O   1 
HETATM 14632 O  O   . HOH GA 6 .   ? 16.844  60.234  42.514  1.00 18.29 ?  976  HOH A O   1 
HETATM 14633 O  O   . HOH GA 6 .   ? 57.192  29.512  7.687   1.00 24.40 ?  977  HOH A O   1 
HETATM 14634 O  O   . HOH GA 6 .   ? 17.528  65.667  22.135  1.00 26.48 ?  978  HOH A O   1 
HETATM 14635 O  O   . HOH GA 6 .   ? 45.369  58.629  9.751   1.00 38.75 ?  979  HOH A O   1 
HETATM 14636 O  O   . HOH GA 6 .   ? 59.032  52.704  25.298  1.00 24.80 ?  980  HOH A O   1 
HETATM 14637 O  O   . HOH GA 6 .   ? 57.064  30.816  5.357   1.00 29.99 ?  981  HOH A O   1 
HETATM 14638 O  O   . HOH GA 6 .   ? 52.887  47.052  48.359  1.00 18.35 ?  982  HOH A O   1 
HETATM 14639 O  O   . HOH GA 6 .   ? 30.352  48.324  62.178  1.00 28.33 ?  983  HOH A O   1 
HETATM 14640 O  O   . HOH GA 6 .   ? 52.017  38.997  -3.715  1.00 45.03 ?  984  HOH A O   1 
HETATM 14641 O  O   . HOH GA 6 .   ? 67.307  72.928  11.065  1.00 42.44 ?  985  HOH A O   1 
HETATM 14642 O  O   . HOH GA 6 .   ? 60.816  26.410  6.497   1.00 20.92 ?  986  HOH A O   1 
HETATM 14643 O  O   . HOH GA 6 .   ? 24.777  46.101  38.770  1.00 32.52 ?  987  HOH A O   1 
HETATM 14644 O  O   . HOH GA 6 .   ? 21.680  64.493  42.638  1.00 25.89 ?  988  HOH A O   1 
HETATM 14645 O  O   . HOH GA 6 .   ? 24.517  50.077  64.998  1.00 48.91 ?  989  HOH A O   1 
HETATM 14646 O  O   . HOH GA 6 .   ? 47.872  58.488  10.482  1.00 26.25 ?  990  HOH A O   1 
HETATM 14647 O  O   . HOH GA 6 .   ? 35.621  41.641  6.276   1.00 46.29 ?  991  HOH A O   1 
HETATM 14648 O  O   . HOH GA 6 .   ? 41.116  64.010  -0.087  1.00 41.96 ?  992  HOH A O   1 
HETATM 14649 O  O   . HOH GA 6 .   ? 24.391  69.394  20.686  1.00 29.89 ?  993  HOH A O   1 
HETATM 14650 O  O   . HOH GA 6 .   ? 50.974  52.382  19.799  1.00 31.12 ?  994  HOH A O   1 
HETATM 14651 O  O   . HOH GA 6 .   ? 45.146  56.153  -2.828  1.00 38.62 ?  995  HOH A O   1 
HETATM 14652 O  O   . HOH GA 6 .   ? 31.546  57.157  45.531  1.00 33.89 ?  996  HOH A O   1 
HETATM 14653 O  O   . HOH GA 6 .   ? 29.726  42.638  33.096  1.00 35.97 ?  997  HOH A O   1 
HETATM 14654 O  O   . HOH GA 6 .   ? 38.054  42.066  4.788   1.00 40.14 ?  998  HOH A O   1 
HETATM 14655 O  O   . HOH GA 6 .   ? 53.199  69.565  26.032  1.00 40.56 ?  999  HOH A O   1 
HETATM 14656 O  O   . HOH GA 6 .   ? 43.325  42.883  6.603   1.00 48.01 ?  1000 HOH A O   1 
HETATM 14657 O  O   . HOH GA 6 .   ? 16.544  46.755  59.979  1.00 52.19 ?  1001 HOH A O   1 
HETATM 14658 O  O   . HOH GA 6 .   ? 33.964  57.857  44.587  1.00 32.08 ?  1002 HOH A O   1 
HETATM 14659 O  O   . HOH GA 6 .   ? 54.336  35.606  35.657  1.00 21.19 ?  1003 HOH A O   1 
HETATM 14660 O  O   . HOH GA 6 .   ? 39.172  63.070  19.257  1.00 28.99 ?  1004 HOH A O   1 
HETATM 14661 O  O   . HOH GA 6 .   ? 32.484  40.224  20.650  1.00 31.24 ?  1005 HOH A O   1 
HETATM 14662 O  O   . HOH GA 6 .   ? 77.296  33.189  9.666   1.00 35.37 ?  1006 HOH A O   1 
HETATM 14663 O  O   . HOH GA 6 .   ? 44.682  45.049  21.913  1.00 28.44 ?  1007 HOH A O   1 
HETATM 14664 O  O   . HOH GA 6 .   ? 36.045  42.058  9.099   1.00 31.64 ?  1008 HOH A O   1 
HETATM 14665 O  O   . HOH GA 6 .   ? 28.671  46.942  38.845  1.00 42.36 ?  1009 HOH A O   1 
HETATM 14666 O  O   . HOH GA 6 .   ? 40.968  42.348  58.408  1.00 30.73 ?  1010 HOH A O   1 
HETATM 14667 O  O   . HOH GA 6 .   ? 39.945  60.882  -3.875  1.00 40.91 ?  1011 HOH A O   1 
HETATM 14668 O  O   . HOH GA 6 .   ? 45.296  55.819  42.359  1.00 35.27 ?  1012 HOH A O   1 
HETATM 14669 O  O   . HOH GA 6 .   ? 15.872  69.204  16.724  1.00 38.87 ?  1013 HOH A O   1 
HETATM 14670 O  O   . HOH GA 6 .   ? 28.218  49.923  61.446  1.00 33.74 ?  1014 HOH A O   1 
HETATM 14671 O  O   . HOH GA 6 .   ? 32.004  79.324  22.181  1.00 68.90 ?  1015 HOH A O   1 
HETATM 14672 O  O   . HOH GA 6 .   ? 63.629  66.241  31.942  1.00 45.52 ?  1016 HOH A O   1 
HETATM 14673 O  O   . HOH GA 6 .   ? 20.487  44.807  88.382  1.00 60.15 ?  1017 HOH A O   1 
HETATM 14674 O  O   . HOH GA 6 .   ? 69.267  46.223  28.180  1.00 61.47 ?  1018 HOH A O   1 
HETATM 14675 O  O   . HOH GA 6 .   ? 73.814  54.876  11.247  1.00 48.67 ?  1019 HOH A O   1 
HETATM 14676 O  O   . HOH GA 6 .   ? 73.009  53.239  9.449   1.00 40.97 ?  1020 HOH A O   1 
HETATM 14677 O  O   . HOH GA 6 .   ? 33.214  77.696  20.349  1.00 42.72 ?  1021 HOH A O   1 
HETATM 14678 O  O   . HOH GA 6 .   ? 67.775  46.871  30.486  1.00 40.70 ?  1022 HOH A O   1 
HETATM 14679 O  O   . HOH GA 6 .   ? 18.764  55.247  37.836  1.00 22.58 ?  1023 HOH A O   1 
HETATM 14680 O  O   . HOH GA 6 .   ? 15.869  55.296  38.472  1.00 25.45 ?  1024 HOH A O   1 
HETATM 14681 O  O   . HOH GA 6 .   ? 14.949  57.660  39.705  1.00 15.68 ?  1025 HOH A O   1 
HETATM 14682 O  O   . HOH GA 6 .   ? 39.556  50.167  14.515  1.00 23.60 ?  1026 HOH A O   1 
HETATM 14683 O  O   . HOH GA 6 .   ? 37.283  50.999  13.585  1.00 19.62 ?  1027 HOH A O   1 
HETATM 14684 O  O   . HOH GA 6 .   ? 23.322  53.869  15.694  1.00 26.02 ?  1028 HOH A O   1 
HETATM 14685 O  O   . HOH GA 6 .   ? 21.273  53.009  17.313  1.00 18.33 ?  1029 HOH A O   1 
HETATM 14686 O  O   . HOH GA 6 .   ? 17.747  62.098  40.407  1.00 29.55 ?  1030 HOH A O   1 
HETATM 14687 O  O   . HOH HA 6 .   ? 17.658  68.788  37.074  1.00 20.63 ?  101  HOH B O   1 
HETATM 14688 O  O   . HOH HA 6 .   ? 15.906  63.441  44.689  1.00 24.19 ?  102  HOH B O   1 
HETATM 14689 O  O   . HOH HA 6 .   ? 26.095  82.950  33.936  1.00 56.62 ?  103  HOH B O   1 
HETATM 14690 O  O   . HOH HA 6 .   ? 10.774  86.500  41.727  1.00 49.04 ?  104  HOH B O   1 
HETATM 14691 O  O   . HOH HA 6 .   ? 13.005  75.435  25.903  1.00 54.93 ?  105  HOH B O   1 
HETATM 14692 O  O   . HOH HA 6 .   ? 14.888  67.099  45.469  1.00 31.10 ?  106  HOH B O   1 
HETATM 14693 O  O   . HOH HA 6 .   ? 9.873   78.978  29.812  1.00 59.77 ?  107  HOH B O   1 
HETATM 14694 O  O   . HOH HA 6 .   ? 11.692  66.903  33.367  1.00 25.65 ?  108  HOH B O   1 
HETATM 14695 O  O   . HOH HA 6 .   ? 15.961  71.243  34.540  1.00 23.49 ?  109  HOH B O   1 
HETATM 14696 O  O   . HOH HA 6 .   ? 35.767  79.407  35.459  1.00 58.97 ?  110  HOH B O   1 
HETATM 14697 O  O   . HOH HA 6 .   ? 16.379  70.247  40.060  1.00 36.57 ?  111  HOH B O   1 
HETATM 14698 O  O   . HOH HA 6 .   ? 13.574  78.246  42.300  1.00 47.53 ?  112  HOH B O   1 
HETATM 14699 O  O   . HOH HA 6 .   ? 10.285  72.715  31.665  1.00 39.34 ?  113  HOH B O   1 
HETATM 14700 O  O   . HOH HA 6 .   ? 15.890  68.221  28.139  1.00 26.81 ?  114  HOH B O   1 
HETATM 14701 O  O   . HOH HA 6 .   ? 36.432  82.882  37.266  1.00 50.37 ?  115  HOH B O   1 
HETATM 14702 O  O   . HOH HA 6 .   ? 9.135   66.296  32.040  1.00 27.30 ?  116  HOH B O   1 
HETATM 14703 O  O   . HOH HA 6 .   ? 20.765  81.926  29.218  1.00 40.45 ?  117  HOH B O   1 
HETATM 14704 O  O   . HOH HA 6 .   ? 38.539  78.520  34.469  1.00 46.39 ?  118  HOH B O   1 
HETATM 14705 O  O   . HOH HA 6 .   ? 19.023  63.686  42.453  1.00 24.79 ?  119  HOH B O   1 
HETATM 14706 O  O   . HOH HA 6 .   ? 13.630  78.580  24.975  1.00 51.84 ?  120  HOH B O   1 
HETATM 14707 O  O   . HOH HA 6 .   ? 25.668  72.592  43.160  1.00 32.63 ?  121  HOH B O   1 
HETATM 14708 O  O   . HOH HA 6 .   ? 8.411   72.397  42.758  1.00 40.03 ?  122  HOH B O   1 
HETATM 14709 O  O   . HOH HA 6 .   ? 28.606  67.616  39.156  1.00 24.58 ?  123  HOH B O   1 
HETATM 14710 O  O   . HOH HA 6 .   ? 14.806  64.753  48.642  1.00 43.14 ?  124  HOH B O   1 
HETATM 14711 O  O   . HOH HA 6 .   ? 15.766  71.433  42.410  1.00 60.30 ?  125  HOH B O   1 
HETATM 14712 O  O   . HOH HA 6 .   ? 7.658   80.327  33.239  1.00 40.96 ?  126  HOH B O   1 
HETATM 14713 O  O   . HOH HA 6 .   ? 6.762   69.097  43.944  1.00 45.21 ?  127  HOH B O   1 
HETATM 14714 O  O   . HOH HA 6 .   ? 8.434   63.138  48.202  1.00 45.62 ?  128  HOH B O   1 
HETATM 14715 O  O   . HOH HA 6 .   ? 32.337  76.357  37.861  1.00 41.29 ?  129  HOH B O   1 
HETATM 14716 O  O   . HOH HA 6 .   ? 16.222  85.283  41.881  1.00 51.18 ?  130  HOH B O   1 
HETATM 14717 O  O   . HOH HA 6 .   ? 18.027  83.577  33.290  1.00 52.77 ?  131  HOH B O   1 
HETATM 14718 O  O   . HOH HA 6 .   ? 17.232  86.305  27.396  1.00 50.35 ?  132  HOH B O   1 
HETATM 14719 O  O   . HOH HA 6 .   ? 15.379  87.763  28.409  1.00 58.57 ?  133  HOH B O   1 
HETATM 14720 O  O   . HOH HA 6 .   ? 14.293  90.275  33.020  1.00 49.28 ?  134  HOH B O   1 
HETATM 14721 O  O   . HOH HA 6 .   ? 15.898  91.962  31.460  1.00 44.33 ?  135  HOH B O   1 
HETATM 14722 O  O   . HOH HA 6 .   ? 13.800  61.395  39.782  1.00 28.66 ?  136  HOH B O   1 
HETATM 14723 O  O   . HOH HA 6 .   ? 38.099  71.656  37.680  1.00 41.01 ?  137  HOH B O   1 
HETATM 14724 O  O   . HOH HA 6 .   ? 8.630   85.027  32.739  1.00 39.21 ?  138  HOH B O   1 
HETATM 14725 O  O   . HOH HA 6 .   ? 36.080  70.955  40.076  1.00 39.78 ?  139  HOH B O   1 
HETATM 14726 O  O   . HOH HA 6 .   ? 12.323  87.432  39.630  1.00 37.25 ?  140  HOH B O   1 
HETATM 14727 O  O   . HOH HA 6 .   ? 28.165  84.474  34.778  1.00 64.42 ?  141  HOH B O   1 
HETATM 14728 O  O   . HOH HA 6 .   ? 13.254  68.566  28.661  1.00 35.05 ?  142  HOH B O   1 
HETATM 14729 O  O   . HOH IA 6 .   ? 2.666   8.614   3.547   1.00 55.75 ?  701  HOH C O   1 
HETATM 14730 O  O   . HOH IA 6 .   ? 41.084  24.920  32.046  1.00 18.13 ?  702  HOH C O   1 
HETATM 14731 O  O   . HOH IA 6 .   ? 39.550  21.239  37.620  1.00 17.17 ?  703  HOH C O   1 
HETATM 14732 O  O   . HOH IA 6 .   ? 36.963  53.223  26.464  1.00 19.92 ?  704  HOH C O   1 
HETATM 14733 O  O   . HOH IA 6 .   ? 28.225  25.432  37.384  1.00 23.29 ?  705  HOH C O   1 
HETATM 14734 O  O   . HOH IA 6 .   ? 51.089  19.788  21.509  1.00 24.82 ?  706  HOH C O   1 
HETATM 14735 O  O   . HOH IA 6 .   ? 24.181  17.678  41.998  1.00 20.69 ?  707  HOH C O   1 
HETATM 14736 O  O   . HOH IA 6 .   ? 27.572  21.010  8.998   1.00 20.39 ?  708  HOH C O   1 
HETATM 14737 O  O   . HOH IA 6 .   ? 28.472  11.195  -6.222  1.00 41.31 ?  709  HOH C O   1 
HETATM 14738 O  O   . HOH IA 6 .   ? 41.673  16.537  13.781  1.00 27.52 ?  710  HOH C O   1 
HETATM 14739 O  O   . HOH IA 6 .   ? 44.747  18.011  0.806   1.00 24.46 ?  711  HOH C O   1 
HETATM 14740 O  O   . HOH IA 6 .   ? 30.292  17.374  15.721  1.00 17.97 ?  712  HOH C O   1 
HETATM 14741 O  O   . HOH IA 6 .   ? 28.446  24.614  20.444  1.00 20.75 ?  713  HOH C O   1 
HETATM 14742 O  O   . HOH IA 6 .   ? 18.542  4.587   40.259  1.00 32.58 ?  714  HOH C O   1 
HETATM 14743 O  O   . HOH IA 6 .   ? 39.943  27.703  30.347  1.00 16.17 ?  715  HOH C O   1 
HETATM 14744 O  O   . HOH IA 6 .   ? 19.312  9.084   -3.721  1.00 42.63 ?  716  HOH C O   1 
HETATM 14745 O  O   . HOH IA 6 .   ? 28.318  23.969  14.258  1.00 17.31 ?  717  HOH C O   1 
HETATM 14746 O  O   . HOH IA 6 .   ? 22.188  20.965  51.642  1.00 27.65 ?  718  HOH C O   1 
HETATM 14747 O  O   . HOH IA 6 .   ? 43.893  44.109  15.560  1.00 17.48 ?  719  HOH C O   1 
HETATM 14748 O  O   . HOH IA 6 .   ? 17.998  7.744   1.066   1.00 24.54 ?  720  HOH C O   1 
HETATM 14749 O  O   . HOH IA 6 .   ? 25.227  34.867  45.145  1.00 23.51 ?  721  HOH C O   1 
HETATM 14750 O  O   . HOH IA 6 .   ? 41.163  10.325  36.452  1.00 27.28 ?  722  HOH C O   1 
HETATM 14751 O  O   . HOH IA 6 .   ? 27.323  10.518  -3.758  1.00 24.50 ?  723  HOH C O   1 
HETATM 14752 O  O   . HOH IA 6 .   ? 44.438  -8.635  30.438  1.00 53.40 ?  724  HOH C O   1 
HETATM 14753 O  O   . HOH IA 6 .   ? 43.871  20.569  3.153   1.00 24.78 ?  725  HOH C O   1 
HETATM 14754 O  O   . HOH IA 6 .   ? 24.911  15.124  4.633   1.00 21.02 ?  726  HOH C O   1 
HETATM 14755 O  O   . HOH IA 6 .   ? 25.708  18.569  44.799  1.00 24.52 ?  727  HOH C O   1 
HETATM 14756 O  O   . HOH IA 6 .   ? 22.316  7.318   22.338  1.00 28.27 ?  728  HOH C O   1 
HETATM 14757 O  O   . HOH IA 6 .   ? 37.477  26.112  30.295  1.00 16.67 ?  729  HOH C O   1 
HETATM 14758 O  O   . HOH IA 6 .   ? 50.532  14.260  31.268  1.00 37.35 ?  730  HOH C O   1 
HETATM 14759 O  O   . HOH IA 6 .   ? 38.820  27.499  52.212  1.00 38.43 ?  731  HOH C O   1 
HETATM 14760 O  O   . HOH IA 6 .   ? 29.130  35.221  29.798  1.00 24.41 ?  732  HOH C O   1 
HETATM 14761 O  O   . HOH IA 6 .   ? 27.407  26.573  18.197  1.00 25.33 ?  733  HOH C O   1 
HETATM 14762 O  O   . HOH IA 6 .   ? 17.261  29.251  49.384  1.00 25.49 ?  734  HOH C O   1 
HETATM 14763 O  O   . HOH IA 6 .   ? 22.478  18.511  21.872  1.00 20.04 ?  735  HOH C O   1 
HETATM 14764 O  O   . HOH IA 6 .   ? 36.689  20.642  4.863   1.00 22.10 ?  736  HOH C O   1 
HETATM 14765 O  O   . HOH IA 6 .   ? 25.900  3.903   33.287  1.00 32.30 ?  737  HOH C O   1 
HETATM 14766 O  O   . HOH IA 6 .   ? 27.225  25.888  4.468   1.00 45.90 ?  738  HOH C O   1 
HETATM 14767 O  O   . HOH IA 6 .   ? 47.524  21.805  -2.640  1.00 45.60 ?  739  HOH C O   1 
HETATM 14768 O  O   . HOH IA 6 .   ? 34.685  2.704   23.312  1.00 27.55 ?  740  HOH C O   1 
HETATM 14769 O  O   . HOH IA 6 .   ? 23.165  37.380  63.237  1.00 43.11 ?  741  HOH C O   1 
HETATM 14770 O  O   . HOH IA 6 .   ? 36.663  5.410   -4.209  1.00 28.85 ?  742  HOH C O   1 
HETATM 14771 O  O   . HOH IA 6 .   ? 45.187  30.155  49.740  1.00 17.57 ?  743  HOH C O   1 
HETATM 14772 O  O   . HOH IA 6 .   ? 33.533  36.776  36.845  1.00 20.86 ?  744  HOH C O   1 
HETATM 14773 O  O   . HOH IA 6 .   ? 47.360  10.676  32.291  1.00 36.52 ?  745  HOH C O   1 
HETATM 14774 O  O   . HOH IA 6 .   ? 27.553  1.869   -2.525  1.00 35.96 ?  746  HOH C O   1 
HETATM 14775 O  O   . HOH IA 6 .   ? 41.551  24.737  8.608   1.00 27.88 ?  747  HOH C O   1 
HETATM 14776 O  O   . HOH IA 6 .   ? 33.237  40.874  15.408  1.00 24.34 ?  748  HOH C O   1 
HETATM 14777 O  O   . HOH IA 6 .   ? 49.072  -2.825  20.602  1.00 36.95 ?  749  HOH C O   1 
HETATM 14778 O  O   . HOH IA 6 .   ? 24.385  6.945   29.033  1.00 25.02 ?  750  HOH C O   1 
HETATM 14779 O  O   . HOH IA 6 .   ? 24.246  2.250   15.085  1.00 39.43 ?  751  HOH C O   1 
HETATM 14780 O  O   . HOH IA 6 .   ? 31.278  0.391   -7.942  1.00 23.19 ?  752  HOH C O   1 
HETATM 14781 O  O   . HOH IA 6 .   ? 36.779  35.595  31.698  1.00 16.42 ?  753  HOH C O   1 
HETATM 14782 O  O   . HOH IA 6 .   ? 12.575  18.877  51.357  1.00 31.99 ?  754  HOH C O   1 
HETATM 14783 O  O   . HOH IA 6 .   ? 19.854  7.976   29.431  1.00 28.10 ?  755  HOH C O   1 
HETATM 14784 O  O   . HOH IA 6 .   ? 13.117  15.846  54.952  1.00 45.05 ?  756  HOH C O   1 
HETATM 14785 O  O   . HOH IA 6 .   ? 18.851  20.234  54.801  1.00 30.59 ?  757  HOH C O   1 
HETATM 14786 O  O   . HOH IA 6 .   ? 7.665   15.593  27.198  1.00 24.00 ?  758  HOH C O   1 
HETATM 14787 O  O   . HOH IA 6 .   ? 13.739  14.378  31.824  1.00 35.04 ?  759  HOH C O   1 
HETATM 14788 O  O   . HOH IA 6 .   ? 31.379  7.260   24.775  1.00 27.78 ?  760  HOH C O   1 
HETATM 14789 O  O   . HOH IA 6 .   ? 12.567  5.914   36.639  1.00 30.65 ?  761  HOH C O   1 
HETATM 14790 O  O   . HOH IA 6 .   ? 25.747  10.626  15.493  1.00 19.74 ?  762  HOH C O   1 
HETATM 14791 O  O   . HOH IA 6 .   ? 15.499  22.876  59.026  1.00 45.46 ?  763  HOH C O   1 
HETATM 14792 O  O   . HOH IA 6 .   ? 42.538  22.873  43.241  1.00 21.97 ?  764  HOH C O   1 
HETATM 14793 O  O   . HOH IA 6 .   ? 43.300  19.633  47.535  1.00 35.31 ?  765  HOH C O   1 
HETATM 14794 O  O   . HOH IA 6 .   ? 47.391  24.415  16.375  1.00 20.07 ?  766  HOH C O   1 
HETATM 14795 O  O   . HOH IA 6 .   ? 36.189  15.191  21.261  1.00 22.32 ?  767  HOH C O   1 
HETATM 14796 O  O   . HOH IA 6 .   ? 41.681  42.211  8.402   1.00 27.15 ?  768  HOH C O   1 
HETATM 14797 O  O   . HOH IA 6 .   ? 35.753  3.639   29.674  1.00 34.38 ?  769  HOH C O   1 
HETATM 14798 O  O   . HOH IA 6 .   ? 39.726  16.150  8.917   1.00 32.75 ?  770  HOH C O   1 
HETATM 14799 O  O   . HOH IA 6 .   ? 18.053  5.439   17.159  1.00 30.76 ?  771  HOH C O   1 
HETATM 14800 O  O   . HOH IA 6 .   ? 27.000  38.865  51.562  1.00 23.10 ?  772  HOH C O   1 
HETATM 14801 O  O   . HOH IA 6 .   ? 36.858  8.811   8.487   1.00 33.67 ?  773  HOH C O   1 
HETATM 14802 O  O   . HOH IA 6 .   ? 25.593  14.472  45.080  1.00 37.02 ?  774  HOH C O   1 
HETATM 14803 O  O   . HOH IA 6 .   ? 46.355  19.937  37.748  1.00 22.79 ?  775  HOH C O   1 
HETATM 14804 O  O   . HOH IA 6 .   ? 53.509  41.145  23.251  1.00 28.06 ?  776  HOH C O   1 
HETATM 14805 O  O   . HOH IA 6 .   ? 44.205  11.774  -0.854  1.00 36.77 ?  777  HOH C O   1 
HETATM 14806 O  O   . HOH IA 6 .   ? 4.236   13.951  15.298  1.00 34.98 ?  778  HOH C O   1 
HETATM 14807 O  O   . HOH IA 6 .   ? 31.162  14.221  -10.579 1.00 49.15 ?  779  HOH C O   1 
HETATM 14808 O  O   . HOH IA 6 .   ? 34.668  23.911  52.039  1.00 45.51 ?  780  HOH C O   1 
HETATM 14809 O  O   . HOH IA 6 .   ? 24.845  6.327   22.142  1.00 24.45 ?  781  HOH C O   1 
HETATM 14810 O  O   . HOH IA 6 .   ? 31.378  23.639  3.818   1.00 37.90 ?  782  HOH C O   1 
HETATM 14811 O  O   . HOH IA 6 .   ? 13.683  13.847  38.753  1.00 28.51 ?  783  HOH C O   1 
HETATM 14812 O  O   . HOH IA 6 .   ? 43.353  12.570  12.638  1.00 26.50 ?  784  HOH C O   1 
HETATM 14813 O  O   . HOH IA 6 .   ? 20.627  27.811  55.899  1.00 27.70 ?  785  HOH C O   1 
HETATM 14814 O  O   . HOH IA 6 .   ? 30.940  43.143  37.685  1.00 32.64 ?  786  HOH C O   1 
HETATM 14815 O  O   . HOH IA 6 .   ? 23.353  39.223  48.163  1.00 32.00 ?  787  HOH C O   1 
HETATM 14816 O  O   . HOH IA 6 .   ? 57.757  27.400  31.642  1.00 36.71 ?  788  HOH C O   1 
HETATM 14817 O  O   . HOH IA 6 .   ? 21.158  8.610   36.238  1.00 24.93 ?  789  HOH C O   1 
HETATM 14818 O  O   . HOH IA 6 .   ? 21.565  32.857  78.427  1.00 49.33 ?  790  HOH C O   1 
HETATM 14819 O  O   . HOH IA 6 .   ? 28.988  45.581  47.335  1.00 21.36 ?  791  HOH C O   1 
HETATM 14820 O  O   . HOH IA 6 .   ? 11.436  25.810  0.854   1.00 42.02 ?  792  HOH C O   1 
HETATM 14821 O  O   . HOH IA 6 .   ? 31.475  36.538  30.098  1.00 30.20 ?  793  HOH C O   1 
HETATM 14822 O  O   . HOH IA 6 .   ? 24.551  0.499   9.646   1.00 36.26 ?  794  HOH C O   1 
HETATM 14823 O  O   . HOH IA 6 .   ? 37.802  7.179   38.221  1.00 37.42 ?  795  HOH C O   1 
HETATM 14824 O  O   . HOH IA 6 .   ? 23.669  8.560   54.029  1.00 47.84 ?  796  HOH C O   1 
HETATM 14825 O  O   . HOH IA 6 .   ? 44.280  15.651  22.908  1.00 31.39 ?  797  HOH C O   1 
HETATM 14826 O  O   . HOH IA 6 .   ? 33.531  21.383  4.691   1.00 25.00 ?  798  HOH C O   1 
HETATM 14827 O  O   . HOH IA 6 .   ? 11.168  25.519  53.588  1.00 33.96 ?  799  HOH C O   1 
HETATM 14828 O  O   . HOH IA 6 .   ? 52.054  15.604  26.698  1.00 37.50 ?  800  HOH C O   1 
HETATM 14829 O  O   . HOH IA 6 .   ? 36.704  24.369  53.680  1.00 46.04 ?  801  HOH C O   1 
HETATM 14830 O  O   . HOH IA 6 .   ? 44.320  18.800  24.909  1.00 40.06 ?  802  HOH C O   1 
HETATM 14831 O  O   . HOH IA 6 .   ? 36.433  37.115  29.378  1.00 22.16 ?  803  HOH C O   1 
HETATM 14832 O  O   . HOH IA 6 .   ? 20.811  22.104  59.744  1.00 49.82 ?  804  HOH C O   1 
HETATM 14833 O  O   . HOH IA 6 .   ? 18.073  15.084  50.979  1.00 30.66 ?  805  HOH C O   1 
HETATM 14834 O  O   . HOH IA 6 .   ? 33.574  31.587  64.775  1.00 51.91 ?  806  HOH C O   1 
HETATM 14835 O  O   . HOH IA 6 .   ? 16.936  1.042   -1.126  1.00 37.31 ?  807  HOH C O   1 
HETATM 14836 O  O   . HOH IA 6 .   ? 35.859  41.497  28.250  1.00 26.66 ?  808  HOH C O   1 
HETATM 14837 O  O   . HOH IA 6 .   ? 39.665  25.431  47.237  1.00 37.13 ?  809  HOH C O   1 
HETATM 14838 O  O   . HOH IA 6 .   ? 26.258  22.296  62.312  1.00 36.98 ?  810  HOH C O   1 
HETATM 14839 O  O   . HOH IA 6 .   ? 33.185  -9.118  0.735   1.00 36.96 ?  811  HOH C O   1 
HETATM 14840 O  O   . HOH IA 6 .   ? 46.396  41.454  24.093  1.00 27.15 ?  812  HOH C O   1 
HETATM 14841 O  O   . HOH IA 6 .   ? 35.210  1.770   33.092  1.00 45.64 ?  813  HOH C O   1 
HETATM 14842 O  O   . HOH IA 6 .   ? 38.534  2.694   -3.014  1.00 30.63 ?  814  HOH C O   1 
HETATM 14843 O  O   . HOH IA 6 .   ? 52.999  22.482  34.947  1.00 17.29 ?  815  HOH C O   1 
HETATM 14844 O  O   . HOH IA 6 .   ? 24.949  31.008  39.281  1.00 23.95 ?  816  HOH C O   1 
HETATM 14845 O  O   . HOH IA 6 .   ? 3.857   10.653  12.834  1.00 39.96 ?  817  HOH C O   1 
HETATM 14846 O  O   . HOH IA 6 .   ? 51.284  -4.321  20.130  1.00 49.91 ?  818  HOH C O   1 
HETATM 14847 O  O   . HOH IA 6 .   ? 57.198  25.778  33.710  1.00 50.55 ?  819  HOH C O   1 
HETATM 14848 O  O   . HOH IA 6 .   ? 28.056  35.487  20.131  1.00 21.55 ?  820  HOH C O   1 
HETATM 14849 O  O   . HOH IA 6 .   ? 36.506  33.247  12.781  1.00 23.71 ?  821  HOH C O   1 
HETATM 14850 O  O   . HOH IA 6 .   ? 62.912  27.525  21.295  1.00 34.99 ?  822  HOH C O   1 
HETATM 14851 O  O   . HOH IA 6 .   ? 36.552  28.807  3.563   1.00 28.27 ?  823  HOH C O   1 
HETATM 14852 O  O   . HOH IA 6 .   ? 33.829  20.185  1.769   1.00 40.43 ?  824  HOH C O   1 
HETATM 14853 O  O   . HOH IA 6 .   ? 17.978  11.589  49.706  1.00 30.27 ?  825  HOH C O   1 
HETATM 14854 O  O   . HOH IA 6 .   ? 37.841  39.613  58.612  1.00 31.31 ?  826  HOH C O   1 
HETATM 14855 O  O   . HOH IA 6 .   ? 33.068  -6.129  -5.032  1.00 30.44 ?  827  HOH C O   1 
HETATM 14856 O  O   . HOH IA 6 .   ? 32.238  27.407  49.052  1.00 30.41 ?  828  HOH C O   1 
HETATM 14857 O  O   . HOH IA 6 .   ? 28.650  35.122  32.332  1.00 22.43 ?  829  HOH C O   1 
HETATM 14858 O  O   . HOH IA 6 .   ? 38.986  8.529   6.859   1.00 47.58 ?  830  HOH C O   1 
HETATM 14859 O  O   . HOH IA 6 .   ? 40.284  19.053  -7.830  1.00 36.84 ?  831  HOH C O   1 
HETATM 14860 O  O   . HOH IA 6 .   ? 16.079  7.692   47.632  1.00 28.10 ?  832  HOH C O   1 
HETATM 14861 O  O   . HOH IA 6 .   ? 42.368  38.654  50.270  1.00 28.83 ?  833  HOH C O   1 
HETATM 14862 O  O   . HOH IA 6 .   ? 39.409  14.237  10.849  1.00 21.79 ?  834  HOH C O   1 
HETATM 14863 O  O   . HOH IA 6 .   ? 29.413  35.984  37.023  1.00 22.27 ?  835  HOH C O   1 
HETATM 14864 O  O   . HOH IA 6 .   ? 23.998  21.868  8.676   1.00 23.72 ?  836  HOH C O   1 
HETATM 14865 O  O   . HOH IA 6 .   ? 43.172  22.801  45.896  1.00 23.68 ?  837  HOH C O   1 
HETATM 14866 O  O   . HOH IA 6 .   ? 5.571   -1.649  13.568  1.00 47.07 ?  838  HOH C O   1 
HETATM 14867 O  O   . HOH IA 6 .   ? 19.615  2.166   31.585  1.00 32.75 ?  839  HOH C O   1 
HETATM 14868 O  O   . HOH IA 6 .   ? 42.439  20.872  26.285  1.00 32.05 ?  840  HOH C O   1 
HETATM 14869 O  O   . HOH IA 6 .   ? 47.791  18.767  -1.636  1.00 40.57 ?  841  HOH C O   1 
HETATM 14870 O  O   . HOH IA 6 .   ? 53.122  13.125  17.349  1.00 45.23 ?  842  HOH C O   1 
HETATM 14871 O  O   . HOH IA 6 .   ? 15.330  3.157   34.885  1.00 45.78 ?  843  HOH C O   1 
HETATM 14872 O  O   . HOH IA 6 .   ? 18.634  28.863  62.286  1.00 42.39 ?  844  HOH C O   1 
HETATM 14873 O  O   . HOH IA 6 .   ? 11.917  40.225  76.144  1.00 44.15 ?  845  HOH C O   1 
HETATM 14874 O  O   . HOH IA 6 .   ? 16.041  12.958  30.058  1.00 49.44 ?  846  HOH C O   1 
HETATM 14875 O  O   . HOH IA 6 .   ? 44.096  11.173  3.507   1.00 58.89 ?  847  HOH C O   1 
HETATM 14876 O  O   . HOH IA 6 .   ? 42.698  -0.418  14.516  1.00 26.52 ?  848  HOH C O   1 
HETATM 14877 O  O   . HOH IA 6 .   ? 44.684  37.872  53.521  1.00 27.45 ?  849  HOH C O   1 
HETATM 14878 O  O   . HOH IA 6 .   ? 41.103  1.693   6.844   1.00 32.33 ?  850  HOH C O   1 
HETATM 14879 O  O   . HOH IA 6 .   ? 39.838  57.411  30.936  1.00 30.30 ?  851  HOH C O   1 
HETATM 14880 O  O   . HOH IA 6 .   ? 12.672  11.502  41.691  1.00 32.20 ?  852  HOH C O   1 
HETATM 14881 O  O   . HOH IA 6 .   ? 44.205  -8.014  18.344  1.00 45.84 ?  853  HOH C O   1 
HETATM 14882 O  O   . HOH IA 6 .   ? 6.769   5.928   10.730  1.00 27.62 ?  854  HOH C O   1 
HETATM 14883 O  O   . HOH IA 6 .   ? 22.017  10.681  53.976  1.00 53.56 ?  855  HOH C O   1 
HETATM 14884 O  O   . HOH IA 6 .   ? 12.640  5.345   31.803  1.00 32.09 ?  856  HOH C O   1 
HETATM 14885 O  O   . HOH IA 6 .   ? 40.154  17.045  29.170  1.00 24.44 ?  857  HOH C O   1 
HETATM 14886 O  O   . HOH IA 6 .   ? 25.662  -2.890  19.203  1.00 45.12 ?  858  HOH C O   1 
HETATM 14887 O  O   . HOH IA 6 .   ? 25.490  24.064  8.037   1.00 25.79 ?  859  HOH C O   1 
HETATM 14888 O  O   . HOH IA 6 .   ? 28.929  19.575  54.462  1.00 44.60 ?  860  HOH C O   1 
HETATM 14889 O  O   . HOH IA 6 .   ? 23.463  22.133  59.323  1.00 42.66 ?  861  HOH C O   1 
HETATM 14890 O  O   . HOH IA 6 .   ? 48.872  14.120  2.479   1.00 48.33 ?  862  HOH C O   1 
HETATM 14891 O  O   . HOH IA 6 .   ? 38.441  6.063   9.377   1.00 37.97 ?  863  HOH C O   1 
HETATM 14892 O  O   . HOH IA 6 .   ? 33.507  43.694  38.086  1.00 31.02 ?  864  HOH C O   1 
HETATM 14893 O  O   . HOH IA 6 .   ? 46.413  4.928   10.073  1.00 40.77 ?  865  HOH C O   1 
HETATM 14894 O  O   . HOH IA 6 .   ? 23.978  37.773  50.874  1.00 38.74 ?  866  HOH C O   1 
HETATM 14895 O  O   . HOH IA 6 .   ? 30.526  35.110  15.250  1.00 30.72 ?  867  HOH C O   1 
HETATM 14896 O  O   . HOH IA 6 .   ? 28.609  19.340  45.029  1.00 28.94 ?  868  HOH C O   1 
HETATM 14897 O  O   . HOH IA 6 .   ? 10.270  27.106  51.746  1.00 30.05 ?  869  HOH C O   1 
HETATM 14898 O  O   . HOH IA 6 .   ? 29.826  35.281  43.985  1.00 24.43 ?  870  HOH C O   1 
HETATM 14899 O  O   . HOH IA 6 .   ? 33.216  30.722  5.269   1.00 39.44 ?  871  HOH C O   1 
HETATM 14900 O  O   . HOH IA 6 .   ? 22.046  30.579  41.403  1.00 25.47 ?  872  HOH C O   1 
HETATM 14901 O  O   . HOH IA 6 .   ? 44.175  18.032  10.188  1.00 22.16 ?  873  HOH C O   1 
HETATM 14902 O  O   . HOH IA 6 .   ? 42.218  27.137  7.560   1.00 31.68 ?  874  HOH C O   1 
HETATM 14903 O  O   . HOH IA 6 .   ? 38.989  25.760  49.855  1.00 49.15 ?  875  HOH C O   1 
HETATM 14904 O  O   . HOH IA 6 .   ? 49.649  31.387  8.271   1.00 28.05 ?  876  HOH C O   1 
HETATM 14905 O  O   . HOH IA 6 .   ? 39.442  23.471  -3.574  1.00 36.49 ?  877  HOH C O   1 
HETATM 14906 O  O   . HOH IA 6 .   ? 14.605  20.479  58.089  1.00 56.34 ?  878  HOH C O   1 
HETATM 14907 O  O   . HOH IA 6 .   ? 39.089  16.076  43.086  1.00 27.50 ?  879  HOH C O   1 
HETATM 14908 O  O   . HOH IA 6 .   ? 25.990  43.184  44.324  1.00 32.79 ?  880  HOH C O   1 
HETATM 14909 O  O   . HOH IA 6 .   ? 27.025  8.302   49.433  1.00 41.06 ?  881  HOH C O   1 
HETATM 14910 O  O   . HOH IA 6 .   ? 60.720  29.434  19.961  1.00 37.76 ?  882  HOH C O   1 
HETATM 14911 O  O   . HOH IA 6 .   ? 15.798  3.401   -4.402  1.00 29.97 ?  883  HOH C O   1 
HETATM 14912 O  O   . HOH IA 6 .   ? 47.004  18.163  2.492   1.00 35.11 ?  884  HOH C O   1 
HETATM 14913 O  O   . HOH IA 6 .   ? 50.202  14.925  41.175  1.00 40.15 ?  885  HOH C O   1 
HETATM 14914 O  O   . HOH IA 6 .   ? 28.199  34.818  39.991  1.00 37.63 ?  886  HOH C O   1 
HETATM 14915 O  O   . HOH IA 6 .   ? 23.904  22.375  22.140  1.00 29.39 ?  887  HOH C O   1 
HETATM 14916 O  O   . HOH IA 6 .   ? 11.678  9.315   43.113  1.00 26.23 ?  888  HOH C O   1 
HETATM 14917 O  O   . HOH IA 6 .   ? 32.427  8.573   34.604  1.00 42.23 ?  889  HOH C O   1 
HETATM 14918 O  O   . HOH IA 6 .   ? 29.055  5.614   25.559  1.00 37.75 ?  890  HOH C O   1 
HETATM 14919 O  O   . HOH IA 6 .   ? 26.068  22.608  20.018  1.00 31.87 ?  891  HOH C O   1 
HETATM 14920 O  O   . HOH IA 6 .   ? 55.370  23.850  16.586  1.00 46.22 ?  892  HOH C O   1 
HETATM 14921 O  O   . HOH IA 6 .   ? 24.893  45.233  67.854  1.00 54.68 ?  893  HOH C O   1 
HETATM 14922 O  O   . HOH IA 6 .   ? 24.001  33.472  56.624  1.00 28.89 ?  894  HOH C O   1 
HETATM 14923 O  O   . HOH IA 6 .   ? 36.131  34.876  17.286  1.00 30.07 ?  895  HOH C O   1 
HETATM 14924 O  O   . HOH IA 6 .   ? 27.219  35.402  42.546  1.00 23.45 ?  896  HOH C O   1 
HETATM 14925 O  O   . HOH IA 6 .   ? 44.453  15.679  19.470  1.00 22.45 ?  897  HOH C O   1 
HETATM 14926 O  O   . HOH IA 6 .   ? 56.136  18.379  24.104  1.00 40.33 ?  898  HOH C O   1 
HETATM 14927 O  O   . HOH IA 6 .   ? 39.453  37.124  56.216  1.00 45.61 ?  899  HOH C O   1 
HETATM 14928 O  O   . HOH IA 6 .   ? 32.877  10.794  -11.359 1.00 55.06 ?  900  HOH C O   1 
HETATM 14929 O  O   . HOH IA 6 .   ? 26.848  -0.244  16.351  1.00 48.26 ?  901  HOH C O   1 
HETATM 14930 O  O   . HOH IA 6 .   ? 11.135  12.582  35.570  1.00 31.38 ?  902  HOH C O   1 
HETATM 14931 O  O   . HOH IA 6 .   ? 33.330  -6.864  2.031   1.00 44.99 ?  903  HOH C O   1 
HETATM 14932 O  O   . HOH IA 6 .   ? 50.650  17.762  -8.597  1.00 47.46 ?  904  HOH C O   1 
HETATM 14933 O  O   . HOH IA 6 .   ? 29.298  19.301  51.783  1.00 54.65 ?  905  HOH C O   1 
HETATM 14934 O  O   . HOH IA 6 .   ? 13.099  18.480  54.567  1.00 29.80 ?  906  HOH C O   1 
HETATM 14935 O  O   . HOH IA 6 .   ? 8.562   17.801  8.732   1.00 36.12 ?  907  HOH C O   1 
HETATM 14936 O  O   . HOH IA 6 .   ? 31.618  39.006  14.355  1.00 38.22 ?  908  HOH C O   1 
HETATM 14937 O  O   . HOH IA 6 .   ? 35.001  33.863  15.049  1.00 34.48 ?  909  HOH C O   1 
HETATM 14938 O  O   . HOH IA 6 .   ? 20.488  21.807  -2.491  1.00 34.17 ?  910  HOH C O   1 
HETATM 14939 O  O   . HOH IA 6 .   ? 42.429  13.513  44.528  1.00 49.68 ?  911  HOH C O   1 
HETATM 14940 O  O   . HOH IA 6 .   ? 49.737  14.206  27.410  1.00 37.02 ?  912  HOH C O   1 
HETATM 14941 O  O   . HOH IA 6 .   ? 25.418  4.059   -0.319  1.00 41.36 ?  913  HOH C O   1 
HETATM 14942 O  O   . HOH IA 6 .   ? 24.275  10.995  -4.213  1.00 32.00 ?  914  HOH C O   1 
HETATM 14943 O  O   . HOH IA 6 .   ? 50.422  18.143  1.449   1.00 49.71 ?  915  HOH C O   1 
HETATM 14944 O  O   . HOH IA 6 .   ? 33.105  -8.420  -3.690  1.00 35.59 ?  916  HOH C O   1 
HETATM 14945 O  O   . HOH IA 6 .   ? 36.517  31.811  3.982   1.00 37.98 ?  917  HOH C O   1 
HETATM 14946 O  O   . HOH IA 6 .   ? 26.361  36.457  32.782  1.00 38.40 ?  918  HOH C O   1 
HETATM 14947 O  O   . HOH IA 6 .   ? 46.765  7.561   29.949  1.00 52.67 ?  919  HOH C O   1 
HETATM 14948 O  O   . HOH IA 6 .   ? 30.115  39.241  35.443  1.00 44.25 ?  920  HOH C O   1 
HETATM 14949 O  O   . HOH IA 6 .   ? 37.696  38.340  61.017  1.00 51.75 ?  921  HOH C O   1 
HETATM 14950 O  O   . HOH IA 6 .   ? 26.788  40.991  42.669  1.00 38.11 ?  922  HOH C O   1 
HETATM 14951 O  O   . HOH IA 6 .   ? 11.545  -4.946  -4.364  1.00 47.61 ?  923  HOH C O   1 
HETATM 14952 O  O   . HOH IA 6 .   ? 8.872   8.024   -3.959  1.00 33.88 ?  924  HOH C O   1 
HETATM 14953 O  O   . HOH IA 6 .   ? 53.212  27.068  36.821  1.00 41.64 ?  925  HOH C O   1 
HETATM 14954 O  O   . HOH IA 6 .   ? 27.899  39.527  45.129  1.00 52.01 ?  926  HOH C O   1 
HETATM 14955 O  O   . HOH IA 6 .   ? 19.728  9.033   -0.480  1.00 28.15 ?  927  HOH C O   1 
HETATM 14956 O  O   . HOH IA 6 .   ? 25.524  20.936  60.283  1.00 42.07 ?  928  HOH C O   1 
HETATM 14957 O  O   . HOH IA 6 .   ? 26.321  0.711   12.101  1.00 37.18 ?  929  HOH C O   1 
HETATM 14958 O  O   . HOH IA 6 .   ? 51.895  12.004  31.641  1.00 42.32 ?  930  HOH C O   1 
HETATM 14959 O  O   . HOH IA 6 .   ? 18.287  28.090  66.403  1.00 68.96 ?  931  HOH C O   1 
HETATM 14960 O  O   . HOH IA 6 .   ? 31.450  4.993   -8.818  1.00 46.19 ?  932  HOH C O   1 
HETATM 14961 O  O   . HOH IA 6 .   ? 33.935  38.333  29.382  1.00 53.87 ?  933  HOH C O   1 
HETATM 14962 O  O   . HOH IA 6 .   ? 36.252  46.286  38.603  1.00 34.27 ?  934  HOH C O   1 
HETATM 14963 O  O   . HOH IA 6 .   ? 57.872  19.027  37.719  1.00 39.62 ?  935  HOH C O   1 
HETATM 14964 O  O   . HOH IA 6 .   ? 37.272  6.222   31.504  1.00 51.28 ?  936  HOH C O   1 
HETATM 14965 O  O   . HOH IA 6 .   ? 39.694  -6.558  7.680   1.00 32.27 ?  937  HOH C O   1 
HETATM 14966 O  O   . HOH IA 6 .   ? 55.177  28.602  31.660  1.00 23.90 ?  938  HOH C O   1 
HETATM 14967 O  O   . HOH IA 6 .   ? 35.534  33.724  2.050   1.00 35.79 ?  939  HOH C O   1 
HETATM 14968 O  O   . HOH IA 6 .   ? 45.820  1.513   29.030  1.00 54.61 ?  940  HOH C O   1 
HETATM 14969 O  O   . HOH IA 6 .   ? 21.629  20.984  54.971  1.00 36.23 ?  941  HOH C O   1 
HETATM 14970 O  O   . HOH IA 6 .   ? 7.499   10.715  35.203  1.00 39.83 ?  942  HOH C O   1 
HETATM 14971 O  O   . HOH IA 6 .   ? 46.416  -3.550  12.344  1.00 39.09 ?  943  HOH C O   1 
HETATM 14972 O  O   . HOH IA 6 .   ? 31.164  19.755  49.878  1.00 46.05 ?  944  HOH C O   1 
HETATM 14973 O  O   . HOH IA 6 .   ? 65.538  27.973  22.639  1.00 38.04 ?  945  HOH C O   1 
HETATM 14974 O  O   . HOH IA 6 .   ? 22.234  6.570   52.941  1.00 54.18 ?  946  HOH C O   1 
HETATM 14975 O  O   . HOH IA 6 .   ? 53.577  27.897  33.713  1.00 31.59 ?  947  HOH C O   1 
HETATM 14976 O  O   . HOH IA 6 .   ? 47.082  6.311   32.237  1.00 54.66 ?  948  HOH C O   1 
HETATM 14977 O  O   . HOH IA 6 .   ? 17.514  25.540  66.958  1.00 36.97 ?  949  HOH C O   1 
HETATM 14978 O  O   . HOH IA 6 .   ? 40.140  39.384  61.639  1.00 47.80 ?  950  HOH C O   1 
HETATM 14979 O  O   . HOH IA 6 .   ? 29.417  39.385  37.997  1.00 43.43 ?  951  HOH C O   1 
HETATM 14980 O  O   . HOH IA 6 .   ? 56.390  19.198  15.704  1.00 46.73 ?  952  HOH C O   1 
HETATM 14981 O  O   . HOH IA 6 .   ? 48.527  1.930   31.265  1.00 49.59 ?  953  HOH C O   1 
HETATM 14982 O  O   . HOH IA 6 .   ? 50.974  10.747  44.360  1.00 40.51 ?  954  HOH C O   1 
HETATM 14983 O  O   . HOH IA 6 .   ? 28.921  38.309  40.370  1.00 29.59 ?  955  HOH C O   1 
HETATM 14984 O  O   . HOH IA 6 .   ? 56.484  12.118  41.497  1.00 47.67 ?  956  HOH C O   1 
HETATM 14985 O  O   . HOH IA 6 .   ? 56.754  16.711  16.674  1.00 52.08 ?  957  HOH C O   1 
HETATM 14986 O  O   . HOH IA 6 .   ? 23.758  33.658  66.279  1.00 50.19 ?  958  HOH C O   1 
HETATM 14987 O  O   . HOH IA 6 .   ? 37.418  44.985  31.119  1.00 23.12 ?  959  HOH C O   1 
HETATM 14988 O  O   . HOH IA 6 .   ? 39.647  42.505  27.534  1.00 16.31 ?  960  HOH C O   1 
HETATM 14989 O  O   . HOH IA 6 .   ? 25.664  29.187  27.506  1.00 20.41 ?  961  HOH C O   1 
HETATM 14990 O  O   . HOH IA 6 .   ? 44.491  30.813  24.424  1.00 23.71 ?  962  HOH C O   1 
HETATM 14991 O  O   . HOH IA 6 .   ? 40.972  26.255  10.818  1.00 16.86 ?  963  HOH C O   1 
HETATM 14992 O  O   . HOH IA 6 .   ? 12.686  -0.246  16.480  1.00 50.53 ?  964  HOH C O   1 
HETATM 14993 O  O   . HOH IA 6 .   ? 54.585  36.431  33.173  1.00 19.84 ?  965  HOH C O   1 
HETATM 14994 O  O   . HOH IA 6 .   ? 47.639  14.886  12.284  1.00 30.13 ?  966  HOH C O   1 
HETATM 14995 O  O   . HOH IA 6 .   ? 56.109  14.926  39.888  1.00 40.32 ?  967  HOH C O   1 
HETATM 14996 O  O   . HOH IA 6 .   ? 28.668  13.476  37.112  1.00 27.67 ?  968  HOH C O   1 
HETATM 14997 O  O   . HOH IA 6 .   ? 30.992  27.106  7.061   1.00 46.98 ?  969  HOH C O   1 
HETATM 14998 O  O   . HOH IA 6 .   ? 58.576  22.663  30.952  1.00 50.71 ?  970  HOH C O   1 
HETATM 14999 O  O   . HOH IA 6 .   ? 34.027  32.174  11.923  1.00 22.63 ?  971  HOH C O   1 
HETATM 15000 O  O   . HOH IA 6 .   ? 12.929  -5.117  10.101  1.00 41.88 ?  972  HOH C O   1 
HETATM 15001 O  O   . HOH IA 6 .   ? 29.504  18.681  3.417   1.00 23.17 ?  973  HOH C O   1 
HETATM 15002 O  O   . HOH IA 6 .   ? 39.334  39.786  43.901  1.00 18.17 ?  974  HOH C O   1 
HETATM 15003 O  O   . HOH IA 6 .   ? 40.510  41.958  45.383  1.00 22.66 ?  975  HOH C O   1 
HETATM 15004 O  O   . HOH IA 6 .   ? 40.402  14.230  13.321  1.00 28.76 ?  976  HOH C O   1 
HETATM 15005 O  O   . HOH IA 6 .   ? 28.944  15.466  4.186   1.00 22.86 ?  977  HOH C O   1 
HETATM 15006 O  O   . HOH IA 6 .   ? 31.016  21.017  55.414  1.00 56.66 ?  978  HOH C O   1 
HETATM 15007 O  O   . HOH IA 6 .   ? 41.531  -3.264  6.039   1.00 36.63 ?  979  HOH C O   1 
HETATM 15008 O  O   . HOH IA 6 .   ? 27.062  47.563  60.741  1.00 31.23 ?  980  HOH C O   1 
HETATM 15009 O  O   . HOH IA 6 .   ? 20.564  36.812  65.921  1.00 56.60 ?  981  HOH C O   1 
HETATM 15010 O  O   . HOH IA 6 .   ? 41.213  11.922  -8.596  1.00 32.98 ?  982  HOH C O   1 
HETATM 15011 O  O   . HOH IA 6 .   ? 42.380  41.806  47.307  1.00 21.37 ?  983  HOH C O   1 
HETATM 15012 O  O   . HOH IA 6 .   ? 25.140  -4.989  10.086  1.00 51.35 ?  984  HOH C O   1 
HETATM 15013 O  O   . HOH IA 6 .   ? 26.376  16.154  42.390  1.00 32.89 ?  985  HOH C O   1 
HETATM 15014 O  O   . HOH IA 6 .   ? 24.411  47.317  60.562  1.00 28.22 ?  986  HOH C O   1 
HETATM 15015 O  O   . HOH IA 6 .   ? 27.010  26.898  31.461  1.00 31.02 ?  987  HOH C O   1 
HETATM 15016 O  O   . HOH IA 6 .   ? 48.588  9.891   23.218  1.00 43.97 ?  988  HOH C O   1 
HETATM 15017 O  O   . HOH IA 6 .   ? 41.950  -8.328  30.980  1.00 38.74 ?  989  HOH C O   1 
HETATM 15018 O  O   . HOH IA 6 .   ? 30.929  41.778  35.387  1.00 35.82 ?  990  HOH C O   1 
HETATM 15019 O  O   . HOH IA 6 .   ? 23.907  10.312  46.334  1.00 45.72 ?  991  HOH C O   1 
HETATM 15020 O  O   . HOH IA 6 .   ? 42.307  13.253  10.083  1.00 41.76 ?  992  HOH C O   1 
HETATM 15021 O  O   . HOH IA 6 .   ? 34.120  24.473  63.815  1.00 57.47 ?  993  HOH C O   1 
HETATM 15022 O  O   . HOH IA 6 .   ? 26.533  6.231   33.979  1.00 33.68 ?  994  HOH C O   1 
HETATM 15023 O  O   . HOH IA 6 .   ? 14.733  22.533  41.606  1.00 28.62 ?  995  HOH C O   1 
HETATM 15024 O  O   . HOH IA 6 .   ? 41.892  13.214  -10.753 1.00 51.59 ?  996  HOH C O   1 
HETATM 15025 O  O   . HOH IA 6 .   ? 29.433  7.956   -6.053  1.00 35.45 ?  997  HOH C O   1 
HETATM 15026 O  O   . HOH IA 6 .   ? 44.882  18.224  22.202  1.00 19.76 ?  998  HOH C O   1 
HETATM 15027 O  O   . HOH IA 6 .   ? 42.548  38.881  55.896  1.00 31.05 ?  999  HOH C O   1 
HETATM 15028 O  O   . HOH IA 6 .   ? 13.932  2.723   28.298  1.00 47.30 ?  1000 HOH C O   1 
HETATM 15029 O  O   . HOH IA 6 .   ? 61.751  23.526  23.721  1.00 34.58 ?  1001 HOH C O   1 
HETATM 15030 O  O   . HOH IA 6 .   ? 15.321  31.676  61.933  1.00 43.91 ?  1002 HOH C O   1 
HETATM 15031 O  O   . HOH IA 6 .   ? 14.218  3.684   -7.650  1.00 53.32 ?  1003 HOH C O   1 
HETATM 15032 O  O   . HOH IA 6 .   ? 28.655  16.016  -7.359  1.00 38.35 ?  1004 HOH C O   1 
HETATM 15033 O  O   . HOH IA 6 .   ? 29.434  13.594  -7.016  1.00 40.99 ?  1005 HOH C O   1 
HETATM 15034 O  O   . HOH IA 6 .   ? 13.870  13.396  43.302  1.00 28.58 ?  1006 HOH C O   1 
HETATM 15035 O  O   . HOH IA 6 .   ? 55.589  13.301  21.300  1.00 49.25 ?  1007 HOH C O   1 
HETATM 15036 O  O   . HOH IA 6 .   ? 23.229  1.762   17.575  1.00 37.51 ?  1008 HOH C O   1 
HETATM 15037 O  O   . HOH IA 6 .   ? 11.208  8.353   39.846  1.00 31.57 ?  1009 HOH C O   1 
HETATM 15038 O  O   . HOH IA 6 .   ? 64.190  24.241  24.294  1.00 51.32 ?  1010 HOH C O   1 
HETATM 15039 O  O   . HOH IA 6 .   ? 49.544  23.392  12.342  1.00 39.65 ?  1011 HOH C O   1 
HETATM 15040 O  O   . HOH IA 6 .   ? 20.816  -4.337  2.997   1.00 47.65 ?  1012 HOH C O   1 
HETATM 15041 O  O   . HOH IA 6 .   ? 26.988  27.759  37.844  1.00 26.39 ?  1013 HOH C O   1 
HETATM 15042 O  O   . HOH IA 6 .   ? -1.639  5.957   12.858  1.00 65.07 ?  1014 HOH C O   1 
HETATM 15043 O  O   . HOH IA 6 .   ? 26.456  16.522  49.559  1.00 44.49 ?  1015 HOH C O   1 
HETATM 15044 O  O   . HOH IA 6 .   ? 33.438  32.875  6.780   1.00 41.22 ?  1016 HOH C O   1 
HETATM 15045 O  O   . HOH IA 6 .   ? 32.286  36.256  42.871  1.00 40.00 ?  1017 HOH C O   1 
HETATM 15046 O  O   . HOH IA 6 .   ? 28.054  18.743  56.920  1.00 47.09 ?  1018 HOH C O   1 
HETATM 15047 O  O   . HOH IA 6 .   ? 45.332  37.101  22.093  1.00 19.99 ?  1019 HOH C O   1 
HETATM 15048 O  O   . HOH IA 6 .   ? 44.877  39.255  23.599  1.00 17.36 ?  1020 HOH C O   1 
HETATM 15049 O  O   . HOH IA 6 .   ? 43.109  32.810  22.970  1.00 18.52 ?  1021 HOH C O   1 
HETATM 15050 O  O   . HOH IA 6 .   ? 40.070  26.015  13.359  1.00 16.14 ?  1022 HOH C O   1 
HETATM 15051 O  O   . HOH IA 6 .   ? 28.699  15.930  18.612  1.00 26.22 ?  1023 HOH C O   1 
HETATM 15052 O  O   . HOH IA 6 .   ? 30.203  13.791  19.219  1.00 22.51 ?  1024 HOH C O   1 
HETATM 15053 O  O   . HOH IA 6 .   ? 37.727  26.570  16.273  1.00 20.88 ?  1025 HOH C O   1 
HETATM 15054 O  O   . HOH IA 6 .   ? 35.668  24.944  16.051  1.00 17.40 ?  1026 HOH C O   1 
HETATM 15055 O  O   . HOH IA 6 .   ? 50.083  24.315  8.301   1.00 25.76 ?  1027 HOH C O   1 
HETATM 15056 O  O   . HOH IA 6 .   ? 48.148  24.278  10.227  1.00 29.81 ?  1028 HOH C O   1 
HETATM 15057 O  O   . HOH JA 6 .   ? 55.769  14.650  58.181  1.00 48.16 ?  101  HOH D O   1 
HETATM 15058 O  O   . HOH JA 6 .   ? 51.896  34.339  51.303  1.00 24.64 ?  102  HOH D O   1 
HETATM 15059 O  O   . HOH JA 6 .   ? 55.259  16.567  43.080  1.00 51.97 ?  103  HOH D O   1 
HETATM 15060 O  O   . HOH JA 6 .   ? 54.907  34.637  46.603  1.00 20.36 ?  104  HOH D O   1 
HETATM 15061 O  O   . HOH JA 6 .   ? 45.041  22.466  53.504  1.00 51.37 ?  105  HOH D O   1 
HETATM 15062 O  O   . HOH JA 6 .   ? 48.816  25.068  52.654  1.00 24.85 ?  106  HOH D O   1 
HETATM 15063 O  O   . HOH JA 6 .   ? 44.215  17.114  47.187  1.00 38.48 ?  107  HOH D O   1 
HETATM 15064 O  O   . HOH JA 6 .   ? 44.854  33.870  54.625  1.00 42.79 ?  108  HOH D O   1 
HETATM 15065 O  O   . HOH JA 6 .   ? 50.940  34.051  47.973  1.00 25.22 ?  109  HOH D O   1 
HETATM 15066 O  O   . HOH JA 6 .   ? 57.279  37.337  44.732  1.00 34.15 ?  110  HOH D O   1 
HETATM 15067 O  O   . HOH JA 6 .   ? 47.916  36.986  55.743  1.00 24.09 ?  111  HOH D O   1 
HETATM 15068 O  O   . HOH JA 6 .   ? 53.744  40.464  45.002  1.00 25.37 ?  112  HOH D O   1 
HETATM 15069 O  O   . HOH JA 6 .   ? 56.455  40.457  56.216  1.00 27.80 ?  113  HOH D O   1 
HETATM 15070 O  O   . HOH JA 6 .   ? 44.366  35.292  50.751  1.00 25.90 ?  114  HOH D O   1 
HETATM 15071 O  O   . HOH JA 6 .   ? 63.461  27.228  56.402  1.00 43.41 ?  115  HOH D O   1 
HETATM 15072 O  O   . HOH JA 6 .   ? 58.120  31.320  39.529  1.00 31.08 ?  116  HOH D O   1 
HETATM 15073 O  O   . HOH JA 6 .   ? 59.382  39.131  45.394  1.00 29.76 ?  117  HOH D O   1 
HETATM 15074 O  O   . HOH JA 6 .   ? 44.668  24.999  46.715  1.00 27.15 ?  118  HOH D O   1 
HETATM 15075 O  O   . HOH JA 6 .   ? 57.503  25.885  57.108  1.00 40.56 ?  119  HOH D O   1 
HETATM 15076 O  O   . HOH JA 6 .   ? 76.133  31.485  44.982  1.00 49.74 ?  120  HOH D O   1 
HETATM 15077 O  O   . HOH JA 6 .   ? 65.180  27.531  47.307  1.00 42.92 ?  121  HOH D O   1 
HETATM 15078 O  O   . HOH JA 6 .   ? 50.043  28.693  55.831  1.00 49.94 ?  122  HOH D O   1 
HETATM 15079 O  O   . HOH JA 6 .   ? 45.572  40.248  52.556  1.00 18.30 ?  123  HOH D O   1 
HETATM 15080 O  O   . HOH JA 6 .   ? 67.009  34.904  54.662  1.00 46.29 ?  124  HOH D O   1 
HETATM 15081 O  O   . HOH JA 6 .   ? 53.643  30.453  52.600  1.00 29.97 ?  125  HOH D O   1 
HETATM 15082 O  O   . HOH JA 6 .   ? 54.920  43.080  44.377  1.00 31.00 ?  126  HOH D O   1 
HETATM 15083 O  O   . HOH JA 6 .   ? 51.700  34.442  54.091  1.00 32.41 ?  127  HOH D O   1 
HETATM 15084 O  O   . HOH JA 6 .   ? 63.672  23.979  53.324  1.00 45.77 ?  128  HOH D O   1 
HETATM 15085 O  O   . HOH JA 6 .   ? 44.180  37.145  48.789  1.00 21.85 ?  129  HOH D O   1 
HETATM 15086 O  O   . HOH JA 6 .   ? 64.901  18.665  46.628  1.00 53.30 ?  130  HOH D O   1 
HETATM 15087 O  O   . HOH JA 6 .   ? 64.737  20.779  48.293  1.00 63.28 ?  131  HOH D O   1 
HETATM 15088 O  O   . HOH JA 6 .   ? 54.526  46.087  50.425  1.00 21.09 ?  132  HOH D O   1 
HETATM 15089 O  O   . HOH JA 6 .   ? 66.328  37.069  44.753  1.00 38.95 ?  133  HOH D O   1 
HETATM 15090 O  O   . HOH JA 6 .   ? 67.277  35.976  42.427  1.00 39.33 ?  134  HOH D O   1 
HETATM 15091 O  O   . HOH JA 6 .   ? 44.522  4.910   46.439  1.00 55.03 ?  135  HOH D O   1 
HETATM 15092 O  O   . HOH JA 6 .   ? 44.449  15.020  45.505  1.00 42.09 ?  136  HOH D O   1 
HETATM 15093 O  O   . HOH JA 6 .   ? 44.748  7.445   42.160  1.00 63.57 ?  137  HOH D O   1 
HETATM 15094 O  O   . HOH KA 6 .   ? 18.301  35.551  33.543  1.00 20.58 ?  701  HOH E O   1 
HETATM 15095 O  O   . HOH KA 6 .   ? 12.407  48.711  8.391   1.00 20.31 ?  702  HOH E O   1 
HETATM 15096 O  O   . HOH KA 6 .   ? 17.562  57.686  -10.742 1.00 24.74 ?  703  HOH E O   1 
HETATM 15097 O  O   . HOH KA 6 .   ? 34.346  25.170  28.768  1.00 15.72 ?  704  HOH E O   1 
HETATM 15098 O  O   . HOH KA 6 .   ? 19.197  49.611  4.298   1.00 20.02 ?  705  HOH E O   1 
HETATM 15099 O  O   . HOH KA 6 .   ? 7.445   34.907  23.734  1.00 14.34 ?  706  HOH E O   1 
HETATM 15100 O  O   . HOH KA 6 .   ? 1.892   37.214  11.451  1.00 34.03 ?  707  HOH E O   1 
HETATM 15101 O  O   . HOH KA 6 .   ? 15.000  50.904  49.105  1.00 21.13 ?  708  HOH E O   1 
HETATM 15102 O  O   . HOH KA 6 .   ? 23.697  43.882  4.442   1.00 31.92 ?  709  HOH E O   1 
HETATM 15103 O  O   . HOH KA 6 .   ? 23.154  34.476  54.218  1.00 26.35 ?  710  HOH E O   1 
HETATM 15104 O  O   . HOH KA 6 .   ? 23.398  35.057  14.330  1.00 20.35 ?  711  HOH E O   1 
HETATM 15105 O  O   . HOH KA 6 .   ? 15.873  51.217  -2.294  1.00 29.75 ?  712  HOH E O   1 
HETATM 15106 O  O   . HOH KA 6 .   ? 10.559  37.629  23.273  1.00 17.77 ?  713  HOH E O   1 
HETATM 15107 O  O   . HOH KA 6 .   ? 11.387  45.731  31.745  1.00 25.16 ?  714  HOH E O   1 
HETATM 15108 O  O   . HOH KA 6 .   ? 14.355  53.026  46.419  1.00 22.48 ?  715  HOH E O   1 
HETATM 15109 O  O   . HOH KA 6 .   ? 12.299  30.189  2.260   1.00 40.49 ?  716  HOH E O   1 
HETATM 15110 O  O   . HOH KA 6 .   ? 2.496   39.798  18.613  1.00 21.93 ?  717  HOH E O   1 
HETATM 15111 O  O   . HOH KA 6 .   ? -1.630  59.685  45.152  1.00 58.29 ?  718  HOH E O   1 
HETATM 15112 O  O   . HOH KA 6 .   ? 14.423  54.835  16.274  1.00 17.07 ?  719  HOH E O   1 
HETATM 15113 O  O   . HOH KA 6 .   ? 2.890   38.089  28.053  1.00 17.85 ?  720  HOH E O   1 
HETATM 15114 O  O   . HOH KA 6 .   ? 17.073  46.787  15.787  1.00 23.58 ?  721  HOH E O   1 
HETATM 15115 O  O   . HOH KA 6 .   ? 16.580  42.032  -1.967  1.00 24.00 ?  722  HOH E O   1 
HETATM 15116 O  O   . HOH KA 6 .   ? -18.433 47.359  2.374   1.00 50.35 ?  723  HOH E O   1 
HETATM 15117 O  O   . HOH KA 6 .   ? 17.134  54.950  -1.149  1.00 26.24 ?  724  HOH E O   1 
HETATM 15118 O  O   . HOH KA 6 .   ? 25.766  36.716  0.753   1.00 38.02 ?  725  HOH E O   1 
HETATM 15119 O  O   . HOH KA 6 .   ? 18.125  33.687  27.769  1.00 15.58 ?  726  HOH E O   1 
HETATM 15120 O  O   . HOH KA 6 .   ? 17.298  39.697  49.312  1.00 28.60 ?  727  HOH E O   1 
HETATM 15121 O  O   . HOH KA 6 .   ? 13.813  29.525  17.797  1.00 24.78 ?  728  HOH E O   1 
HETATM 15122 O  O   . HOH KA 6 .   ? 10.812  50.720  11.094  1.00 18.70 ?  729  HOH E O   1 
HETATM 15123 O  O   . HOH KA 6 .   ? -10.152 26.247  24.348  1.00 46.64 ?  730  HOH E O   1 
HETATM 15124 O  O   . HOH KA 6 .   ? 9.166   55.866  7.232   1.00 18.42 ?  731  HOH E O   1 
HETATM 15125 O  O   . HOH KA 6 .   ? 18.135  31.676  51.883  1.00 18.54 ?  732  HOH E O   1 
HETATM 15126 O  O   . HOH KA 6 .   ? -3.776  35.149  35.736  1.00 32.58 ?  733  HOH E O   1 
HETATM 15127 O  O   . HOH KA 6 .   ? 0.702   34.347  32.941  1.00 21.54 ?  734  HOH E O   1 
HETATM 15128 O  O   . HOH KA 6 .   ? 9.692   25.532  39.568  1.00 20.25 ?  735  HOH E O   1 
HETATM 15129 O  O   . HOH KA 6 .   ? 2.288   51.000  51.491  1.00 32.31 ?  736  HOH E O   1 
HETATM 15130 O  O   . HOH KA 6 .   ? 15.428  62.205  47.687  1.00 29.94 ?  737  HOH E O   1 
HETATM 15131 O  O   . HOH KA 6 .   ? 5.074   40.283  56.681  1.00 34.26 ?  738  HOH E O   1 
HETATM 15132 O  O   . HOH KA 6 .   ? 15.747  64.790  -5.196  1.00 26.30 ?  739  HOH E O   1 
HETATM 15133 O  O   . HOH KA 6 .   ? 17.942  39.752  -14.645 1.00 27.75 ?  740  HOH E O   1 
HETATM 15134 O  O   . HOH KA 6 .   ? 20.247  46.608  14.389  1.00 15.62 ?  741  HOH E O   1 
HETATM 15135 O  O   . HOH KA 6 .   ? 3.546   49.860  -14.832 1.00 32.20 ?  742  HOH E O   1 
HETATM 15136 O  O   . HOH KA 6 .   ? 2.359   62.502  7.304   1.00 35.96 ?  743  HOH E O   1 
HETATM 15137 O  O   . HOH KA 6 .   ? -0.212  60.813  40.580  1.00 37.53 ?  744  HOH E O   1 
HETATM 15138 O  O   . HOH KA 6 .   ? 17.826  66.492  24.634  1.00 26.08 ?  745  HOH E O   1 
HETATM 15139 O  O   . HOH KA 6 .   ? 5.297   66.550  37.660  1.00 24.29 ?  746  HOH E O   1 
HETATM 15140 O  O   . HOH KA 6 .   ? 16.007  39.332  40.432  1.00 13.96 ?  747  HOH E O   1 
HETATM 15141 O  O   . HOH KA 6 .   ? 14.212  45.091  51.074  1.00 29.12 ?  748  HOH E O   1 
HETATM 15142 O  O   . HOH KA 6 .   ? 3.057   29.312  10.049  1.00 22.99 ?  749  HOH E O   1 
HETATM 15143 O  O   . HOH KA 6 .   ? 20.095  37.784  -9.267  1.00 39.54 ?  750  HOH E O   1 
HETATM 15144 O  O   . HOH KA 6 .   ? 10.624  78.574  -11.534 1.00 45.76 ?  751  HOH E O   1 
HETATM 15145 O  O   . HOH KA 6 .   ? -3.101  40.663  31.368  1.00 24.28 ?  752  HOH E O   1 
HETATM 15146 O  O   . HOH KA 6 .   ? 34.762  20.430  33.816  1.00 26.03 ?  753  HOH E O   1 
HETATM 15147 O  O   . HOH KA 6 .   ? 5.956   41.857  3.081   1.00 25.06 ?  754  HOH E O   1 
HETATM 15148 O  O   . HOH KA 6 .   ? 3.644   39.822  1.291   1.00 16.74 ?  755  HOH E O   1 
HETATM 15149 O  O   . HOH KA 6 .   ? 6.690   38.416  -4.065  1.00 36.82 ?  756  HOH E O   1 
HETATM 15150 O  O   . HOH KA 6 .   ? 18.649  16.729  18.186  1.00 27.10 ?  757  HOH E O   1 
HETATM 15151 O  O   . HOH KA 6 .   ? 4.188   35.366  11.685  1.00 21.67 ?  758  HOH E O   1 
HETATM 15152 O  O   . HOH KA 6 .   ? -6.950  47.232  -1.418  1.00 18.00 ?  759  HOH E O   1 
HETATM 15153 O  O   . HOH KA 6 .   ? 15.626  68.262  -11.745 1.00 36.86 ?  760  HOH E O   1 
HETATM 15154 O  O   . HOH KA 6 .   ? 0.378   59.884  -18.849 1.00 51.37 ?  761  HOH E O   1 
HETATM 15155 O  O   . HOH KA 6 .   ? -1.207  32.828  26.272  1.00 25.19 ?  762  HOH E O   1 
HETATM 15156 O  O   . HOH KA 6 .   ? -10.439 55.975  -5.817  1.00 42.71 ?  763  HOH E O   1 
HETATM 15157 O  O   . HOH KA 6 .   ? 3.444   61.486  4.423   1.00 36.11 ?  764  HOH E O   1 
HETATM 15158 O  O   . HOH KA 6 .   ? 18.557  44.462  -0.807  1.00 28.34 ?  765  HOH E O   1 
HETATM 15159 O  O   . HOH KA 6 .   ? 10.395  17.624  25.355  1.00 25.43 ?  766  HOH E O   1 
HETATM 15160 O  O   . HOH KA 6 .   ? 16.932  62.534  -6.804  1.00 32.74 ?  767  HOH E O   1 
HETATM 15161 O  O   . HOH KA 6 .   ? 19.140  31.736  61.404  1.00 31.35 ?  768  HOH E O   1 
HETATM 15162 O  O   . HOH KA 6 .   ? 9.991   30.358  7.641   1.00 29.58 ?  769  HOH E O   1 
HETATM 15163 O  O   . HOH KA 6 .   ? -4.310  51.807  9.881   1.00 18.37 ?  770  HOH E O   1 
HETATM 15164 O  O   . HOH KA 6 .   ? 5.561   63.943  36.302  1.00 24.56 ?  771  HOH E O   1 
HETATM 15165 O  O   . HOH KA 6 .   ? 9.368   50.725  51.230  1.00 19.05 ?  772  HOH E O   1 
HETATM 15166 O  O   . HOH KA 6 .   ? -2.408  47.904  -3.714  1.00 36.74 ?  773  HOH E O   1 
HETATM 15167 O  O   . HOH KA 6 .   ? 15.092  46.449  27.057  1.00 33.82 ?  774  HOH E O   1 
HETATM 15168 O  O   . HOH KA 6 .   ? -4.701  36.447  9.318   1.00 38.66 ?  775  HOH E O   1 
HETATM 15169 O  O   . HOH KA 6 .   ? 21.634  22.633  20.405  1.00 21.70 ?  776  HOH E O   1 
HETATM 15170 O  O   . HOH KA 6 .   ? -1.021  25.802  22.870  1.00 22.04 ?  777  HOH E O   1 
HETATM 15171 O  O   . HOH KA 6 .   ? 10.745  34.801  23.280  1.00 20.18 ?  778  HOH E O   1 
HETATM 15172 O  O   . HOH KA 6 .   ? 11.999  40.921  22.228  1.00 16.02 ?  779  HOH E O   1 
HETATM 15173 O  O   . HOH KA 6 .   ? 11.905  44.696  52.864  1.00 24.61 ?  780  HOH E O   1 
HETATM 15174 O  O   . HOH KA 6 .   ? 4.125   61.848  20.483  1.00 28.51 ?  781  HOH E O   1 
HETATM 15175 O  O   . HOH KA 6 .   ? 24.006  21.060  18.462  1.00 29.01 ?  782  HOH E O   1 
HETATM 15176 O  O   . HOH KA 6 .   ? 3.099   28.128  40.792  1.00 23.76 ?  783  HOH E O   1 
HETATM 15177 O  O   . HOH KA 6 .   ? 18.615  49.107  -2.154  1.00 25.44 ?  784  HOH E O   1 
HETATM 15178 O  O   . HOH KA 6 .   ? 16.390  35.693  1.942   1.00 30.37 ?  785  HOH E O   1 
HETATM 15179 O  O   . HOH KA 6 .   ? 24.341  34.726  36.954  1.00 28.48 ?  786  HOH E O   1 
HETATM 15180 O  O   . HOH KA 6 .   ? 12.596  32.060  54.582  1.00 35.33 ?  787  HOH E O   1 
HETATM 15181 O  O   . HOH KA 6 .   ? -6.387  50.385  15.737  1.00 25.08 ?  788  HOH E O   1 
HETATM 15182 O  O   . HOH KA 6 .   ? 16.575  48.550  38.484  1.00 28.65 ?  789  HOH E O   1 
HETATM 15183 O  O   . HOH KA 6 .   ? 1.989   47.968  -2.794  1.00 33.00 ?  790  HOH E O   1 
HETATM 15184 O  O   . HOH KA 6 .   ? 1.373   60.171  26.714  1.00 20.87 ?  791  HOH E O   1 
HETATM 15185 O  O   . HOH KA 6 .   ? 21.464  72.987  13.028  1.00 24.06 ?  792  HOH E O   1 
HETATM 15186 O  O   . HOH KA 6 .   ? 5.618   44.572  11.519  1.00 19.13 ?  793  HOH E O   1 
HETATM 15187 O  O   . HOH KA 6 .   ? 4.077   68.930  31.928  1.00 37.30 ?  794  HOH E O   1 
HETATM 15188 O  O   . HOH KA 6 .   ? 2.890   68.757  27.917  1.00 28.32 ?  795  HOH E O   1 
HETATM 15189 O  O   . HOH KA 6 .   ? 8.125   50.406  10.386  1.00 24.32 ?  796  HOH E O   1 
HETATM 15190 O  O   . HOH KA 6 .   ? -1.846  56.967  22.478  1.00 22.82 ?  797  HOH E O   1 
HETATM 15191 O  O   . HOH KA 6 .   ? 3.888   51.173  36.618  1.00 27.13 ?  798  HOH E O   1 
HETATM 15192 O  O   . HOH KA 6 .   ? 8.947   36.476  0.680   1.00 21.23 ?  799  HOH E O   1 
HETATM 15193 O  O   . HOH KA 6 .   ? 14.655  69.421  -13.928 1.00 55.40 ?  800  HOH E O   1 
HETATM 15194 O  O   . HOH KA 6 .   ? -6.355  41.947  23.009  1.00 32.11 ?  801  HOH E O   1 
HETATM 15195 O  O   . HOH KA 6 .   ? 5.037   52.787  34.310  1.00 18.99 ?  802  HOH E O   1 
HETATM 15196 O  O   . HOH KA 6 .   ? 4.374   21.034  21.251  1.00 24.12 ?  803  HOH E O   1 
HETATM 15197 O  O   . HOH KA 6 .   ? 8.736   18.263  27.653  1.00 28.98 ?  804  HOH E O   1 
HETATM 15198 O  O   . HOH KA 6 .   ? 1.639   58.335  18.717  1.00 35.38 ?  805  HOH E O   1 
HETATM 15199 O  O   . HOH KA 6 .   ? 1.817   59.190  43.152  1.00 30.44 ?  806  HOH E O   1 
HETATM 15200 O  O   . HOH KA 6 .   ? -8.859  46.392  -3.088  1.00 29.29 ?  807  HOH E O   1 
HETATM 15201 O  O   . HOH KA 6 .   ? 16.683  49.623  15.444  1.00 19.44 ?  808  HOH E O   1 
HETATM 15202 O  O   . HOH KA 6 .   ? 13.886  76.916  -12.933 1.00 44.12 ?  809  HOH E O   1 
HETATM 15203 O  O   . HOH KA 6 .   ? 3.469   22.562  23.403  1.00 24.71 ?  810  HOH E O   1 
HETATM 15204 O  O   . HOH KA 6 .   ? -2.474  64.376  29.386  1.00 37.05 ?  811  HOH E O   1 
HETATM 15205 O  O   . HOH KA 6 .   ? 2.322   58.024  16.156  1.00 24.58 ?  812  HOH E O   1 
HETATM 15206 O  O   . HOH KA 6 .   ? 8.636   25.981  49.516  1.00 27.69 ?  813  HOH E O   1 
HETATM 15207 O  O   . HOH KA 6 .   ? 4.875   28.362  42.761  1.00 16.38 ?  814  HOH E O   1 
HETATM 15208 O  O   . HOH KA 6 .   ? 16.549  29.866  17.633  1.00 16.70 ?  815  HOH E O   1 
HETATM 15209 O  O   . HOH KA 6 .   ? 15.918  36.085  7.161   1.00 18.70 ?  816  HOH E O   1 
HETATM 15210 O  O   . HOH KA 6 .   ? 18.358  25.387  1.828   1.00 24.94 ?  817  HOH E O   1 
HETATM 15211 O  O   . HOH KA 6 .   ? 16.820  52.043  13.893  1.00 27.43 ?  818  HOH E O   1 
HETATM 15212 O  O   . HOH KA 6 .   ? 16.494  45.830  35.814  1.00 19.47 ?  819  HOH E O   1 
HETATM 15213 O  O   . HOH KA 6 .   ? 16.633  35.384  4.579   1.00 16.35 ?  820  HOH E O   1 
HETATM 15214 O  O   . HOH KA 6 .   ? 2.265   19.601  20.217  1.00 22.97 ?  821  HOH E O   1 
HETATM 15215 O  O   . HOH KA 6 .   ? 12.681  48.295  81.673  1.00 50.92 ?  822  HOH E O   1 
HETATM 15216 O  O   . HOH KA 6 .   ? -4.232  69.843  27.696  1.00 43.82 ?  823  HOH E O   1 
HETATM 15217 O  O   . HOH KA 6 .   ? 23.034  49.894  4.832   1.00 29.94 ?  824  HOH E O   1 
HETATM 15218 O  O   . HOH KA 6 .   ? 12.366  28.636  -0.109  1.00 32.06 ?  825  HOH E O   1 
HETATM 15219 O  O   . HOH KA 6 .   ? 3.208   37.213  8.336   1.00 27.02 ?  826  HOH E O   1 
HETATM 15220 O  O   . HOH KA 6 .   ? 16.434  68.894  23.677  1.00 21.85 ?  827  HOH E O   1 
HETATM 15221 O  O   . HOH KA 6 .   ? -7.559  36.469  8.714   1.00 46.87 ?  828  HOH E O   1 
HETATM 15222 O  O   . HOH KA 6 .   ? 15.922  75.071  5.599   1.00 23.87 ?  829  HOH E O   1 
HETATM 15223 O  O   . HOH KA 6 .   ? 13.521  35.832  -4.716  1.00 32.55 ?  830  HOH E O   1 
HETATM 15224 O  O   . HOH KA 6 .   ? 17.153  75.245  -9.431  1.00 40.90 ?  831  HOH E O   1 
HETATM 15225 O  O   . HOH KA 6 .   ? 5.193   47.863  -2.470  1.00 37.56 ?  832  HOH E O   1 
HETATM 15226 O  O   . HOH KA 6 .   ? 19.528  39.598  34.650  1.00 24.14 ?  833  HOH E O   1 
HETATM 15227 O  O   . HOH KA 6 .   ? -8.250  36.961  5.852   1.00 37.43 ?  834  HOH E O   1 
HETATM 15228 O  O   . HOH KA 6 .   ? 4.254   55.699  48.075  1.00 30.88 ?  835  HOH E O   1 
HETATM 15229 O  O   . HOH KA 6 .   ? 17.146  43.396  42.511  1.00 14.08 ?  836  HOH E O   1 
HETATM 15230 O  O   . HOH KA 6 .   ? -1.319  37.111  5.264   1.00 36.68 ?  837  HOH E O   1 
HETATM 15231 O  O   . HOH KA 6 .   ? -8.544  31.701  26.822  1.00 35.91 ?  838  HOH E O   1 
HETATM 15232 O  O   . HOH KA 6 .   ? 19.629  37.380  40.538  1.00 41.04 ?  839  HOH E O   1 
HETATM 15233 O  O   . HOH KA 6 .   ? 11.485  66.979  -10.752 1.00 44.47 ?  840  HOH E O   1 
HETATM 15234 O  O   . HOH KA 6 .   ? 1.231   52.931  53.110  1.00 40.46 ?  841  HOH E O   1 
HETATM 15235 O  O   . HOH KA 6 .   ? 12.476  43.041  -18.038 1.00 38.03 ?  842  HOH E O   1 
HETATM 15236 O  O   . HOH KA 6 .   ? 3.281   48.290  36.358  1.00 35.79 ?  843  HOH E O   1 
HETATM 15237 O  O   . HOH KA 6 .   ? 7.722   48.779  57.273  1.00 26.04 ?  844  HOH E O   1 
HETATM 15238 O  O   . HOH KA 6 .   ? 8.148   75.605  -8.519  1.00 53.36 ?  845  HOH E O   1 
HETATM 15239 O  O   . HOH KA 6 .   ? 15.689  36.855  66.685  1.00 51.37 ?  846  HOH E O   1 
HETATM 15240 O  O   . HOH KA 6 .   ? 7.691   65.128  8.720   1.00 26.48 ?  847  HOH E O   1 
HETATM 15241 O  O   . HOH KA 6 .   ? -7.804  46.263  24.528  1.00 52.33 ?  848  HOH E O   1 
HETATM 15242 O  O   . HOH KA 6 .   ? 11.015  64.230  26.028  1.00 23.19 ?  849  HOH E O   1 
HETATM 15243 O  O   . HOH KA 6 .   ? 2.249   42.806  -8.023  1.00 37.62 ?  850  HOH E O   1 
HETATM 15244 O  O   . HOH KA 6 .   ? 9.754   41.435  -0.513  1.00 31.02 ?  851  HOH E O   1 
HETATM 15245 O  O   . HOH KA 6 .   ? 2.182   60.722  15.568  1.00 28.76 ?  852  HOH E O   1 
HETATM 15246 O  O   . HOH KA 6 .   ? 0.737   52.958  35.754  1.00 38.82 ?  853  HOH E O   1 
HETATM 15247 O  O   . HOH KA 6 .   ? 20.197  38.742  38.296  1.00 39.46 ?  854  HOH E O   1 
HETATM 15248 O  O   . HOH KA 6 .   ? 9.410   70.894  29.575  1.00 49.48 ?  855  HOH E O   1 
HETATM 15249 O  O   . HOH KA 6 .   ? -12.178 37.452  1.583   1.00 38.44 ?  856  HOH E O   1 
HETATM 15250 O  O   . HOH KA 6 .   ? 10.767  46.758  57.838  1.00 32.30 ?  857  HOH E O   1 
HETATM 15251 O  O   . HOH KA 6 .   ? 7.655   50.185  -15.276 1.00 34.44 ?  858  HOH E O   1 
HETATM 15252 O  O   . HOH KA 6 .   ? 20.396  33.341  26.321  1.00 21.27 ?  859  HOH E O   1 
HETATM 15253 O  O   . HOH KA 6 .   ? -5.149  48.996  21.940  1.00 39.40 ?  860  HOH E O   1 
HETATM 15254 O  O   . HOH KA 6 .   ? 13.671  80.847  7.509   1.00 50.49 ?  861  HOH E O   1 
HETATM 15255 O  O   . HOH KA 6 .   ? 7.891   61.290  -15.672 1.00 32.53 ?  862  HOH E O   1 
HETATM 15256 O  O   . HOH KA 6 .   ? 10.702  26.540  44.689  1.00 24.28 ?  863  HOH E O   1 
HETATM 15257 O  O   . HOH KA 6 .   ? 24.648  48.818  -5.153  1.00 42.59 ?  864  HOH E O   1 
HETATM 15258 O  O   . HOH KA 6 .   ? 26.611  39.922  14.015  1.00 29.68 ?  865  HOH E O   1 
HETATM 15259 O  O   . HOH KA 6 .   ? 0.094   20.056  21.828  1.00 43.14 ?  866  HOH E O   1 
HETATM 15260 O  O   . HOH KA 6 .   ? 24.354  28.743  37.450  1.00 21.97 ?  867  HOH E O   1 
HETATM 15261 O  O   . HOH KA 6 .   ? -15.704 45.164  4.929   1.00 43.95 ?  868  HOH E O   1 
HETATM 15262 O  O   . HOH KA 6 .   ? 4.523   69.554  23.348  1.00 32.63 ?  869  HOH E O   1 
HETATM 15263 O  O   . HOH KA 6 .   ? 1.676   51.284  27.463  1.00 32.20 ?  870  HOH E O   1 
HETATM 15264 O  O   . HOH KA 6 .   ? -9.418  29.182  22.728  1.00 40.96 ?  871  HOH E O   1 
HETATM 15265 O  O   . HOH KA 6 .   ? 26.046  62.212  -7.812  1.00 52.20 ?  872  HOH E O   1 
HETATM 15266 O  O   . HOH KA 6 .   ? -5.028  48.010  -3.004  1.00 30.45 ?  873  HOH E O   1 
HETATM 15267 O  O   . HOH KA 6 .   ? -1.942  54.841  29.299  1.00 46.73 ?  874  HOH E O   1 
HETATM 15268 O  O   . HOH KA 6 .   ? 7.649   42.746  0.975   1.00 25.74 ?  875  HOH E O   1 
HETATM 15269 O  O   . HOH KA 6 .   ? -0.610  33.654  35.235  1.00 22.14 ?  876  HOH E O   1 
HETATM 15270 O  O   . HOH KA 6 .   ? 2.915   63.110  -13.168 1.00 48.87 ?  877  HOH E O   1 
HETATM 15271 O  O   . HOH KA 6 .   ? 16.673  51.583  17.382  1.00 22.74 ?  878  HOH E O   1 
HETATM 15272 O  O   . HOH KA 6 .   ? -3.635  58.773  37.776  1.00 41.65 ?  879  HOH E O   1 
HETATM 15273 O  O   . HOH KA 6 .   ? 30.138  72.953  0.166   1.00 25.76 ?  880  HOH E O   1 
HETATM 15274 O  O   . HOH KA 6 .   ? 7.336   61.957  45.801  1.00 25.38 ?  881  HOH E O   1 
HETATM 15275 O  O   . HOH KA 6 .   ? 23.476  35.082  47.199  1.00 23.53 ?  882  HOH E O   1 
HETATM 15276 O  O   . HOH KA 6 .   ? 5.024   65.952  34.521  1.00 29.92 ?  883  HOH E O   1 
HETATM 15277 O  O   . HOH KA 6 .   ? 3.789   62.333  -1.226  1.00 28.52 ?  884  HOH E O   1 
HETATM 15278 O  O   . HOH KA 6 .   ? 8.621   47.412  -15.201 1.00 41.73 ?  885  HOH E O   1 
HETATM 15279 O  O   . HOH KA 6 .   ? 6.962   39.563  2.425   1.00 33.68 ?  886  HOH E O   1 
HETATM 15280 O  O   . HOH KA 6 .   ? -1.590  18.242  22.906  1.00 42.92 ?  887  HOH E O   1 
HETATM 15281 O  O   . HOH KA 6 .   ? 32.160  15.604  38.865  1.00 41.91 ?  888  HOH E O   1 
HETATM 15282 O  O   . HOH KA 6 .   ? 22.102  39.438  -9.505  1.00 46.30 ?  889  HOH E O   1 
HETATM 15283 O  O   . HOH KA 6 .   ? 20.866  41.086  29.917  1.00 27.33 ?  890  HOH E O   1 
HETATM 15284 O  O   . HOH KA 6 .   ? 18.566  44.381  -4.569  1.00 29.48 ?  891  HOH E O   1 
HETATM 15285 O  O   . HOH KA 6 .   ? 23.410  39.012  32.088  1.00 42.11 ?  892  HOH E O   1 
HETATM 15286 O  O   . HOH KA 6 .   ? 22.201  48.315  -1.752  1.00 59.09 ?  893  HOH E O   1 
HETATM 15287 O  O   . HOH KA 6 .   ? 17.893  41.586  39.927  1.00 33.58 ?  894  HOH E O   1 
HETATM 15288 O  O   . HOH KA 6 .   ? 3.796   52.791  47.206  1.00 41.95 ?  895  HOH E O   1 
HETATM 15289 O  O   . HOH KA 6 .   ? 26.298  41.737  19.150  1.00 24.53 ?  896  HOH E O   1 
HETATM 15290 O  O   . HOH KA 6 .   ? 21.580  52.182  5.020   1.00 27.43 ?  897  HOH E O   1 
HETATM 15291 O  O   . HOH KA 6 .   ? -3.036  50.840  22.451  1.00 30.97 ?  898  HOH E O   1 
HETATM 15292 O  O   . HOH KA 6 .   ? -0.051  64.101  15.930  1.00 48.61 ?  899  HOH E O   1 
HETATM 15293 O  O   . HOH KA 6 .   ? 4.660   37.394  -2.907  1.00 35.29 ?  900  HOH E O   1 
HETATM 15294 O  O   . HOH KA 6 .   ? 24.644  31.918  26.676  1.00 30.40 ?  901  HOH E O   1 
HETATM 15295 O  O   . HOH KA 6 .   ? 7.983   63.888  32.161  1.00 27.46 ?  902  HOH E O   1 
HETATM 15296 O  O   . HOH KA 6 .   ? 6.695   48.431  11.490  1.00 36.23 ?  903  HOH E O   1 
HETATM 15297 O  O   . HOH KA 6 .   ? -3.978  65.872  31.032  1.00 40.30 ?  904  HOH E O   1 
HETATM 15298 O  O   . HOH KA 6 .   ? -18.300 44.750  2.974   1.00 47.48 ?  905  HOH E O   1 
HETATM 15299 O  O   . HOH KA 6 .   ? 8.482   29.233  0.939   1.00 31.65 ?  906  HOH E O   1 
HETATM 15300 O  O   . HOH KA 6 .   ? 15.076  60.230  49.541  1.00 42.01 ?  907  HOH E O   1 
HETATM 15301 O  O   . HOH KA 6 .   ? -1.541  64.795  38.211  1.00 31.47 ?  908  HOH E O   1 
HETATM 15302 O  O   . HOH KA 6 .   ? 9.473   80.750  3.159   1.00 43.74 ?  909  HOH E O   1 
HETATM 15303 O  O   . HOH KA 6 .   ? 17.684  42.905  48.981  1.00 28.99 ?  910  HOH E O   1 
HETATM 15304 O  O   . HOH KA 6 .   ? 21.985  79.826  1.143   1.00 50.57 ?  911  HOH E O   1 
HETATM 15305 O  O   . HOH KA 6 .   ? 9.665   62.693  23.727  1.00 44.87 ?  912  HOH E O   1 
HETATM 15306 O  O   . HOH KA 6 .   ? 0.264   31.340  36.452  1.00 25.02 ?  913  HOH E O   1 
HETATM 15307 O  O   . HOH KA 6 .   ? 21.212  52.502  -13.040 1.00 44.24 ?  914  HOH E O   1 
HETATM 15308 O  O   . HOH KA 6 .   ? -1.380  47.876  -7.115  1.00 31.74 ?  915  HOH E O   1 
HETATM 15309 O  O   . HOH KA 6 .   ? -9.101  34.358  9.447   1.00 36.79 ?  916  HOH E O   1 
HETATM 15310 O  O   . HOH KA 6 .   ? 2.534   20.301  10.160  1.00 38.24 ?  917  HOH E O   1 
HETATM 15311 O  O   . HOH KA 6 .   ? 0.409   17.749  10.945  1.00 43.32 ?  918  HOH E O   1 
HETATM 15312 O  O   . HOH KA 6 .   ? 22.803  33.205  28.094  1.00 31.93 ?  919  HOH E O   1 
HETATM 15313 O  O   . HOH KA 6 .   ? 12.532  59.824  50.511  1.00 34.20 ?  920  HOH E O   1 
HETATM 15314 O  O   . HOH KA 6 .   ? -8.956  33.969  6.466   1.00 42.99 ?  921  HOH E O   1 
HETATM 15315 O  O   . HOH KA 6 .   ? 24.265  26.588  3.119   1.00 49.46 ?  922  HOH E O   1 
HETATM 15316 O  O   . HOH KA 6 .   ? 6.695   57.774  53.408  1.00 38.86 ?  923  HOH E O   1 
HETATM 15317 O  O   . HOH KA 6 .   ? -10.129 42.810  14.546  1.00 37.49 ?  924  HOH E O   1 
HETATM 15318 O  O   . HOH KA 6 .   ? 8.657   29.714  50.364  1.00 42.86 ?  925  HOH E O   1 
HETATM 15319 O  O   . HOH KA 6 .   ? 3.716   35.666  14.454  1.00 42.02 ?  926  HOH E O   1 
HETATM 15320 O  O   . HOH KA 6 .   ? 1.562   66.028  9.999   1.00 51.41 ?  927  HOH E O   1 
HETATM 15321 O  O   . HOH KA 6 .   ? 12.783  43.325  60.399  1.00 34.49 ?  928  HOH E O   1 
HETATM 15322 O  O   . HOH KA 6 .   ? -2.843  61.781  20.938  1.00 29.96 ?  929  HOH E O   1 
HETATM 15323 O  O   . HOH KA 6 .   ? 10.549  60.242  -10.150 1.00 37.43 ?  930  HOH E O   1 
HETATM 15324 O  O   . HOH KA 6 .   ? 3.760   74.939  0.026   1.00 52.32 ?  931  HOH E O   1 
HETATM 15325 O  O   . HOH KA 6 .   ? -12.159 43.675  12.031  1.00 40.32 ?  932  HOH E O   1 
HETATM 15326 O  O   . HOH KA 6 .   ? 18.258  33.733  1.646   1.00 43.30 ?  933  HOH E O   1 
HETATM 15327 O  O   . HOH KA 6 .   ? 8.563   51.366  57.800  1.00 37.00 ?  934  HOH E O   1 
HETATM 15328 O  O   . HOH KA 6 .   ? 10.513  32.087  56.787  1.00 40.66 ?  935  HOH E O   1 
HETATM 15329 O  O   . HOH KA 6 .   ? 14.734  52.115  75.548  1.00 43.86 ?  936  HOH E O   1 
HETATM 15330 O  O   . HOH KA 6 .   ? 4.388   71.660  32.400  1.00 43.53 ?  937  HOH E O   1 
HETATM 15331 O  O   . HOH KA 6 .   ? 6.079   67.863  2.180   1.00 48.93 ?  938  HOH E O   1 
HETATM 15332 O  O   . HOH KA 6 .   ? 6.542   73.118  32.103  1.00 32.07 ?  939  HOH E O   1 
HETATM 15333 O  O   . HOH KA 6 .   ? 3.581   69.735  13.476  1.00 47.17 ?  940  HOH E O   1 
HETATM 15334 O  O   . HOH KA 6 .   ? -10.395 49.257  18.756  1.00 50.92 ?  941  HOH E O   1 
HETATM 15335 O  O   . HOH KA 6 .   ? -13.445 39.559  9.529   1.00 51.67 ?  942  HOH E O   1 
HETATM 15336 O  O   . HOH KA 6 .   ? 8.063   60.050  52.778  1.00 47.62 ?  943  HOH E O   1 
HETATM 15337 O  O   . HOH KA 6 .   ? 20.730  81.054  -0.807  1.00 45.79 ?  944  HOH E O   1 
HETATM 15338 O  O   . HOH KA 6 .   ? -11.837 40.811  14.829  1.00 45.05 ?  945  HOH E O   1 
HETATM 15339 O  O   . HOH KA 6 .   ? -9.755  51.856  19.255  1.00 46.46 ?  946  HOH E O   1 
HETATM 15340 O  O   . HOH KA 6 .   ? -12.143 53.119  19.459  1.00 54.15 ?  947  HOH E O   1 
HETATM 15341 O  O   . HOH KA 6 .   ? 28.337  23.367  33.259  1.00 24.85 ?  948  HOH E O   1 
HETATM 15342 O  O   . HOH KA 6 .   ? 25.628  28.626  30.109  1.00 19.99 ?  949  HOH E O   1 
HETATM 15343 O  O   . HOH KA 6 .   ? 24.045  28.021  25.559  1.00 16.79 ?  950  HOH E O   1 
HETATM 15344 O  O   . HOH KA 6 .   ? 16.381  37.876  10.267  1.00 16.65 ?  951  HOH E O   1 
HETATM 15345 O  O   . HOH KA 6 .   ? -0.513  47.821  55.737  1.00 41.26 ?  952  HOH E O   1 
HETATM 15346 O  O   . HOH KA 6 .   ? 20.298  35.139  60.350  1.00 32.06 ?  953  HOH E O   1 
HETATM 15347 O  O   . HOH KA 6 .   ? 0.236   52.313  13.463  1.00 16.96 ?  954  HOH E O   1 
HETATM 15348 O  O   . HOH KA 6 .   ? 5.234   60.345  13.319  1.00 25.81 ?  955  HOH E O   1 
HETATM 15349 O  O   . HOH KA 6 .   ? 4.973   47.551  75.624  1.00 49.38 ?  956  HOH E O   1 
HETATM 15350 O  O   . HOH KA 6 .   ? 5.345   61.717  48.697  1.00 34.38 ?  957  HOH E O   1 
HETATM 15351 O  O   . HOH KA 6 .   ? 19.546  46.531  24.219  1.00 19.36 ?  958  HOH E O   1 
HETATM 15352 O  O   . HOH KA 6 .   ? 6.537   41.252  41.562  1.00 33.24 ?  959  HOH E O   1 
HETATM 15353 O  O   . HOH KA 6 .   ? 21.771  37.631  27.874  1.00 20.67 ?  960  HOH E O   1 
HETATM 15354 O  O   . HOH KA 6 .   ? 2.973   76.199  13.955  1.00 49.44 ?  961  HOH E O   1 
HETATM 15355 O  O   . HOH KA 6 .   ? 9.292   67.133  29.559  1.00 32.50 ?  962  HOH E O   1 
HETATM 15356 O  O   . HOH KA 6 .   ? 23.647  35.776  9.744   1.00 25.33 ?  963  HOH E O   1 
HETATM 15357 O  O   . HOH KA 6 .   ? 15.951  55.617  -11.221 1.00 27.41 ?  964  HOH E O   1 
HETATM 15358 O  O   . HOH KA 6 .   ? 21.855  40.285  27.576  1.00 25.34 ?  965  HOH E O   1 
HETATM 15359 O  O   . HOH KA 6 .   ? 13.689  62.469  43.607  1.00 32.77 ?  966  HOH E O   1 
HETATM 15360 O  O   . HOH KA 6 .   ? 1.856   52.127  32.093  1.00 40.88 ?  967  HOH E O   1 
HETATM 15361 O  O   . HOH KA 6 .   ? 10.028  29.423  3.517   1.00 41.00 ?  968  HOH E O   1 
HETATM 15362 O  O   . HOH KA 6 .   ? -3.115  30.194  13.775  1.00 33.50 ?  969  HOH E O   1 
HETATM 15363 O  O   . HOH KA 6 .   ? 14.204  60.104  42.329  1.00 25.01 ?  970  HOH E O   1 
HETATM 15364 O  O   . HOH KA 6 .   ? 23.681  38.066  -0.276  1.00 24.33 ?  971  HOH E O   1 
HETATM 15365 O  O   . HOH KA 6 .   ? -2.369  61.264  -22.012 1.00 58.39 ?  972  HOH E O   1 
HETATM 15366 O  O   . HOH KA 6 .   ? 17.044  54.551  -13.413 1.00 39.74 ?  973  HOH E O   1 
HETATM 15367 O  O   . HOH KA 6 .   ? 28.921  62.275  -3.707  1.00 42.01 ?  974  HOH E O   1 
HETATM 15368 O  O   . HOH KA 6 .   ? 10.359  62.883  -12.247 1.00 51.46 ?  975  HOH E O   1 
HETATM 15369 O  O   . HOH KA 6 .   ? -5.051  32.223  16.919  1.00 37.29 ?  976  HOH E O   1 
HETATM 15370 O  O   . HOH KA 6 .   ? 19.648  34.318  -14.456 1.00 63.03 ?  977  HOH E O   1 
HETATM 15371 O  O   . HOH KA 6 .   ? 3.675   34.660  -4.255  1.00 33.82 ?  978  HOH E O   1 
HETATM 15372 O  O   . HOH KA 6 .   ? -0.963  22.021  18.403  1.00 42.91 ?  979  HOH E O   1 
HETATM 15373 O  O   . HOH KA 6 .   ? 13.694  45.658  33.081  1.00 22.75 ?  980  HOH E O   1 
HETATM 15374 O  O   . HOH KA 6 .   ? 20.071  36.988  -20.363 1.00 48.66 ?  981  HOH E O   1 
HETATM 15375 O  O   . HOH KA 6 .   ? 22.925  43.891  2.127   1.00 41.79 ?  982  HOH E O   1 
HETATM 15376 O  O   . HOH KA 6 .   ? 31.874  58.187  -4.343  1.00 41.39 ?  983  HOH E O   1 
HETATM 15377 O  O   . HOH KA 6 .   ? 10.925  47.337  61.958  1.00 45.46 ?  984  HOH E O   1 
HETATM 15378 O  O   . HOH KA 6 .   ? -3.611  33.617  14.275  1.00 43.73 ?  985  HOH E O   1 
HETATM 15379 O  O   . HOH KA 6 .   ? -14.165 43.136  1.966   1.00 29.63 ?  986  HOH E O   1 
HETATM 15380 O  O   . HOH KA 6 .   ? 11.045  67.970  27.519  1.00 39.72 ?  987  HOH E O   1 
HETATM 15381 O  O   . HOH KA 6 .   ? 26.204  39.965  2.885   1.00 30.54 ?  988  HOH E O   1 
HETATM 15382 O  O   . HOH KA 6 .   ? -14.633 51.952  -5.078  1.00 47.41 ?  989  HOH E O   1 
HETATM 15383 O  O   . HOH KA 6 .   ? 20.911  36.602  -13.709 1.00 44.35 ?  990  HOH E O   1 
HETATM 15384 O  O   . HOH KA 6 .   ? 12.103  33.065  61.951  1.00 45.08 ?  991  HOH E O   1 
HETATM 15385 O  O   . HOH KA 6 .   ? 23.412  32.340  37.309  1.00 27.27 ?  992  HOH E O   1 
HETATM 15386 O  O   . HOH KA 6 .   ? 19.518  74.916  10.205  1.00 38.27 ?  993  HOH E O   1 
HETATM 15387 O  O   . HOH KA 6 .   ? -14.476 53.779  -7.110  1.00 40.37 ?  994  HOH E O   1 
HETATM 15388 O  O   . HOH KA 6 .   ? 27.608  72.730  -8.925  1.00 38.89 ?  995  HOH E O   1 
HETATM 15389 O  O   . HOH KA 6 .   ? -18.200 46.482  9.935   1.00 69.40 ?  996  HOH E O   1 
HETATM 15390 O  O   . HOH KA 6 .   ? 10.899  49.530  57.729  1.00 39.11 ?  997  HOH E O   1 
HETATM 15391 O  O   . HOH KA 6 .   ? 16.278  36.760  39.304  1.00 40.81 ?  998  HOH E O   1 
HETATM 15392 O  O   . HOH KA 6 .   ? -20.543 47.859  9.726   1.00 67.97 ?  999  HOH E O   1 
HETATM 15393 O  O   . HOH KA 6 .   ? 19.430  25.385  -1.926  1.00 46.62 ?  1000 HOH E O   1 
HETATM 15394 O  O   . HOH KA 6 .   ? 18.952  45.028  -14.863 1.00 33.29 ?  1001 HOH E O   1 
HETATM 15395 O  O   . HOH KA 6 .   ? 21.131  76.125  -4.550  1.00 51.26 ?  1002 HOH E O   1 
HETATM 15396 O  O   . HOH KA 6 .   ? 0.012   47.408  43.524  1.00 47.49 ?  1003 HOH E O   1 
HETATM 15397 O  O   . HOH KA 6 .   ? 27.637  61.081  -5.651  1.00 45.16 ?  1004 HOH E O   1 
HETATM 15398 O  O   . HOH KA 6 .   ? -8.708  56.156  -7.735  1.00 45.68 ?  1005 HOH E O   1 
HETATM 15399 O  O   . HOH KA 6 .   ? 9.855   78.505  -8.698  1.00 50.46 ?  1006 HOH E O   1 
HETATM 15400 O  O   . HOH KA 6 .   ? 13.281  58.556  37.537  1.00 19.32 ?  1007 HOH E O   1 
HETATM 15401 O  O   . HOH KA 6 .   ? 15.511  29.007  39.754  1.00 20.51 ?  1008 HOH E O   1 
HETATM 15402 O  O   . HOH KA 6 .   ? 16.408  26.614  41.582  1.00 23.97 ?  1009 HOH E O   1 
HETATM 15403 O  O   . HOH KA 6 .   ? 19.295  25.777  17.683  1.00 20.28 ?  1010 HOH E O   1 
HETATM 15404 O  O   . HOH KA 6 .   ? 20.772  25.146  19.853  1.00 16.93 ?  1011 HOH E O   1 
HETATM 15405 O  O   . HOH KA 6 .   ? 25.763  39.857  7.354   1.00 25.62 ?  1012 HOH E O   1 
HETATM 15406 O  O   . HOH KA 6 .   ? 24.081  38.439  8.905   1.00 25.17 ?  1013 HOH E O   1 
HETATM 15407 O  O   . HOH KA 6 .   ? 16.072  40.334  10.347  1.00 20.82 ?  1014 HOH E O   1 
HETATM 15408 O  O   . HOH LA 6 .   ? 3.378   17.777  37.143  1.00 19.46 ?  101  HOH F O   1 
HETATM 15409 O  O   . HOH LA 6 .   ? -15.955 40.786  29.180  1.00 53.17 ?  102  HOH F O   1 
HETATM 15410 O  O   . HOH LA 6 .   ? 11.824  22.561  43.218  1.00 19.46 ?  103  HOH F O   1 
HETATM 15411 O  O   . HOH LA 6 .   ? 7.380   16.838  31.384  1.00 27.64 ?  104  HOH F O   1 
HETATM 15412 O  O   . HOH LA 6 .   ? -5.979  0.411   32.356  1.00 45.82 ?  105  HOH F O   1 
HETATM 15413 O  O   . HOH LA 6 .   ? -10.232 10.098  42.211  1.00 59.39 ?  106  HOH F O   1 
HETATM 15414 O  O   . HOH LA 6 .   ? 7.449   23.408  52.737  1.00 34.99 ?  107  HOH F O   1 
HETATM 15415 O  O   . HOH LA 6 .   ? 6.961   26.434  43.687  1.00 25.90 ?  108  HOH F O   1 
HETATM 15416 O  O   . HOH LA 6 .   ? 10.164  20.088  53.037  1.00 42.77 ?  109  HOH F O   1 
HETATM 15417 O  O   . HOH LA 6 .   ? 8.087   24.623  47.003  1.00 31.01 ?  110  HOH F O   1 
HETATM 15418 O  O   . HOH LA 6 .   ? -14.512 33.716  29.473  1.00 67.68 ?  111  HOH F O   1 
HETATM 15419 O  O   . HOH LA 6 .   ? 6.825   14.317  30.468  1.00 53.81 ?  112  HOH F O   1 
HETATM 15420 O  O   . HOH LA 6 .   ? 5.243   11.599  36.721  1.00 37.52 ?  113  HOH F O   1 
HETATM 15421 O  O   . HOH LA 6 .   ? -3.122  15.148  45.068  1.00 56.86 ?  114  HOH F O   1 
HETATM 15422 O  O   . HOH LA 6 .   ? -14.521 34.975  26.967  1.00 55.04 ?  115  HOH F O   1 
HETATM 15423 O  O   . HOH LA 6 .   ? 5.034   14.559  33.098  1.00 37.33 ?  116  HOH F O   1 
HETATM 15424 O  O   . HOH LA 6 .   ? -1.771  20.214  41.787  1.00 48.68 ?  117  HOH F O   1 
HETATM 15425 O  O   . HOH LA 6 .   ? 9.814   22.720  46.566  1.00 26.60 ?  118  HOH F O   1 
HETATM 15426 O  O   . HOH LA 6 .   ? -4.926  17.567  46.412  1.00 45.52 ?  119  HOH F O   1 
HETATM 15427 O  O   . HOH LA 6 .   ? 11.141  13.566  38.164  1.00 32.69 ?  120  HOH F O   1 
HETATM 15428 O  O   . HOH LA 6 .   ? -7.099  36.624  32.140  1.00 40.01 ?  121  HOH F O   1 
HETATM 15429 O  O   . HOH LA 6 .   ? -8.625  31.277  40.405  1.00 50.23 ?  122  HOH F O   1 
HETATM 15430 O  O   . HOH LA 6 .   ? 9.185   15.881  37.795  1.00 23.13 ?  123  HOH F O   1 
HETATM 15431 O  O   . HOH LA 6 .   ? 2.889   20.262  41.998  1.00 26.61 ?  124  HOH F O   1 
HETATM 15432 O  O   . HOH LA 6 .   ? -5.132  20.551  44.822  1.00 59.08 ?  125  HOH F O   1 
HETATM 15433 O  O   . HOH LA 6 .   ? 8.451   7.451   40.963  1.00 33.78 ?  126  HOH F O   1 
HETATM 15434 O  O   . HOH LA 6 .   ? -4.135  7.722   44.180  1.00 61.39 ?  127  HOH F O   1 
HETATM 15435 O  O   . HOH LA 6 .   ? 9.196   25.699  42.406  1.00 29.08 ?  128  HOH F O   1 
HETATM 15436 O  O   . HOH LA 6 .   ? -0.766  5.526   37.799  1.00 49.02 ?  129  HOH F O   1 
HETATM 15437 O  O   . HOH LA 6 .   ? -4.054  27.441  41.091  1.00 30.54 ?  130  HOH F O   1 
HETATM 15438 O  O   . HOH LA 6 .   ? -6.086  35.933  34.552  1.00 34.76 ?  131  HOH F O   1 
HETATM 15439 O  O   . HOH LA 6 .   ? 3.997   13.444  47.632  1.00 41.47 ?  132  HOH F O   1 
HETATM 15440 O  O   . HOH LA 6 .   ? -12.997 31.563  28.781  1.00 37.62 ?  133  HOH F O   1 
HETATM 15441 O  O   . HOH LA 6 .   ? 7.773   14.967  35.362  1.00 34.19 ?  134  HOH F O   1 
HETATM 15442 O  O   . HOH LA 6 .   ? -15.795 32.610  27.315  1.00 49.89 ?  135  HOH F O   1 
HETATM 15443 O  O   . HOH LA 6 .   ? 11.448  12.318  44.446  1.00 27.08 ?  136  HOH F O   1 
HETATM 15444 O  O   . HOH LA 6 .   ? 3.501   9.506   34.443  1.00 44.62 ?  137  HOH F O   1 
HETATM 15445 O  O   . HOH LA 6 .   ? 4.399   21.179  39.046  1.00 27.57 ?  138  HOH F O   1 
HETATM 15446 O  O   . HOH LA 6 .   ? -1.215  12.665  30.700  1.00 63.31 ?  139  HOH F O   1 
HETATM 15447 O  O   . HOH LA 6 .   ? -11.508 21.625  31.537  1.00 58.86 ?  140  HOH F O   1 
HETATM 15448 O  O   . HOH LA 6 .   ? -14.336 36.561  34.030  1.00 52.39 ?  141  HOH F O   1 
HETATM 15449 O  O   . HOH LA 6 .   ? 5.122   14.419  35.812  1.00 29.53 ?  142  HOH F O   1 
HETATM 15450 O  O   . HOH LA 6 .   ? 8.306   7.919   51.683  1.00 58.67 ?  143  HOH F O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASP 1   25  25  ASP ASP A . n 
A 1 2   ILE 2   26  26  ILE ILE A . n 
A 1 3   SER 3   27  27  SER SER A . n 
A 1 4   THR 4   28  28  THR THR A . n 
A 1 5   VAL 5   29  29  VAL VAL A . n 
A 1 6   PRO 6   30  30  PRO PRO A . n 
A 1 7   ASP 7   31  31  ASP ASP A . n 
A 1 8   GLU 8   32  32  GLU GLU A . n 
A 1 9   THR 9   33  33  THR THR A . n 
A 1 10  TYR 10  34  34  TYR TYR A . n 
A 1 11  ASP 11  35  35  ASP ASP A . n 
A 1 12  ALA 12  36  36  ALA ALA A . n 
A 1 13  LEU 13  37  37  LEU LEU A . n 
A 1 14  LYS 14  38  38  LYS LYS A . n 
A 1 15  LEU 15  39  39  LEU LEU A . n 
A 1 16  ASP 16  40  40  ASP ASP A . n 
A 1 17  ARG 17  41  41  ARG ARG A . n 
A 1 18  GLY 18  42  42  GLY GLY A . n 
A 1 19  LYS 19  43  43  LYS LYS A . n 
A 1 20  ALA 20  44  44  ALA ALA A . n 
A 1 21  THR 21  45  45  THR THR A . n 
A 1 22  PRO 22  46  46  PRO PRO A . n 
A 1 23  LYS 23  47  47  LYS LYS A . n 
A 1 24  GLU 24  48  48  GLU GLU A . n 
A 1 25  THR 25  49  49  THR THR A . n 
A 1 26  TYR 26  50  50  TYR TYR A . n 
A 1 27  GLU 27  51  51  GLU GLU A . n 
A 1 28  ALA 28  52  52  ALA ALA A . n 
A 1 29  LEU 29  53  53  LEU LEU A . n 
A 1 30  VAL 30  54  54  VAL VAL A . n 
A 1 31  LYS 31  55  55  LYS LYS A . n 
A 1 32  ARG 32  56  56  ARG ARG A . n 
A 1 33  TYR 33  57  57  TYR TYR A . n 
A 1 34  LYS 34  58  58  LYS LYS A . n 
A 1 35  ASP 35  59  59  ASP ASP A . n 
A 1 36  PRO 36  60  60  PRO PRO A . n 
A 1 37  ALA 37  61  61  ALA ALA A . n 
A 1 38  HIS 38  62  62  HIS HIS A . n 
A 1 39  GLY 39  63  63  GLY GLY A . n 
A 1 40  ALA 40  64  64  ALA ALA A . n 
A 1 41  GLY 41  65  65  GLY GLY A . n 
A 1 42  LYS 42  66  66  LYS LYS A . n 
A 1 43  GLY 43  67  67  GLY GLY A . n 
A 1 44  THR 44  68  68  THR THR A . n 
A 1 45  MET 45  69  69  MET MET A . n 
A 1 46  GLY 46  70  70  GLY GLY A . n 
A 1 47  ASP 47  71  71  ASP ASP A . n 
A 1 48  TYR 48  72  72  TYR TYR A . n 
A 1 49  TRP 49  73  73  TRP TRP A . n 
A 1 50  GLU 50  74  74  GLU GLU A . n 
A 1 51  PRO 51  75  75  PRO PRO A . n 
A 1 52  ILE 52  76  76  ILE ILE A . n 
A 1 53  ALA 53  77  77  ALA ALA A . n 
A 1 54  ILE 54  78  78  ILE ILE A . n 
A 1 55  SER 55  79  79  SER SER A . n 
A 1 56  ILE 56  80  80  ILE ILE A . n 
A 1 57  TYR 57  81  81  TYR TYR A . n 
A 1 58  MET 58  82  82  MET MET A . n 
A 1 59  ASP 59  83  83  ASP ASP A . n 
A 1 60  PRO 60  84  84  PRO PRO A . n 
A 1 61  ASN 61  85  85  ASN ASN A . n 
A 1 62  THR 62  86  86  THR THR A . n 
A 1 63  PHE 63  87  87  PHE PHE A . n 
A 1 64  TYR 64  88  88  TYR TYR A . n 
A 1 65  LYS 65  89  89  LYS LYS A . n 
A 1 66  PRO 66  90  90  PRO PRO A . n 
A 1 67  PRO 67  91  91  PRO PRO A . n 
A 1 68  VAL 68  92  92  VAL VAL A . n 
A 1 69  SER 69  93  93  SER SER A . n 
A 1 70  PRO 70  94  94  PRO PRO A . n 
A 1 71  LYS 71  95  95  LYS LYS A . n 
A 1 72  GLU 72  96  96  GLU GLU A . n 
A 1 73  VAL 73  97  97  VAL VAL A . n 
A 1 74  ALA 74  98  98  ALA ALA A . n 
A 1 75  GLU 75  99  99  GLU GLU A . n 
A 1 76  ARG 76  100 100 ARG ARG A . n 
A 1 77  LYS 77  101 101 LYS LYS A . n 
A 1 78  ASP 78  102 102 ASP ASP A . n 
A 1 79  CYS 79  103 103 CYS CYS A . n 
A 1 80  VAL 80  104 104 VAL VAL A . n 
A 1 81  GLU 81  105 105 GLU GLU A . n 
A 1 82  CYS 82  106 106 CYS CYS A . n 
A 1 83  HIS 83  107 107 HIS HIS A . n 
A 1 84  SER 84  108 108 SER SER A . n 
A 1 85  ASP 85  109 109 ASP ASP A . n 
A 1 86  GLU 86  110 110 GLU GLU A . n 
A 1 87  THR 87  111 111 THR THR A . n 
A 1 88  PRO 88  112 112 PRO PRO A . n 
A 1 89  VAL 89  113 113 VAL VAL A . n 
A 1 90  TRP 90  114 114 TRP TRP A . n 
A 1 91  VAL 91  115 115 VAL VAL A . n 
A 1 92  ARG 92  116 116 ARG ARG A . n 
A 1 93  ALA 93  117 117 ALA ALA A . n 
A 1 94  TRP 94  118 118 TRP TRP A . n 
A 1 95  LYS 95  119 119 LYS LYS A . n 
A 1 96  ARG 96  120 120 ARG ARG A . n 
A 1 97  SER 97  121 121 SER SER A . n 
A 1 98  THR 98  122 122 THR THR A . n 
A 1 99  HIS 99  123 123 HIS HIS A . n 
A 1 100 ALA 100 124 124 ALA ALA A . n 
A 1 101 ASN 101 125 125 ASN ASN A . n 
A 1 102 LEU 102 126 126 LEU LEU A . n 
A 1 103 ASP 103 127 127 ASP ASP A . n 
A 1 104 LYS 104 128 128 LYS LYS A . n 
A 1 105 ILE 105 129 129 ILE ILE A . n 
A 1 106 ARG 106 130 130 ARG ARG A . n 
A 1 107 ASN 107 131 131 ASN ASN A . n 
A 1 108 LEU 108 132 132 LEU LEU A . n 
A 1 109 LYS 109 133 133 LYS LYS A . n 
A 1 110 SER 110 134 134 SER SER A . n 
A 1 111 ASP 111 135 135 ASP ASP A . n 
A 1 112 ASP 112 136 136 ASP ASP A . n 
A 1 113 PRO 113 137 137 PRO PRO A . n 
A 1 114 LEU 114 138 138 LEU LEU A . n 
A 1 115 TYR 115 139 139 TYR TYR A . n 
A 1 116 TYR 116 140 140 TYR TYR A . n 
A 1 117 LYS 117 141 141 LYS LYS A . n 
A 1 118 LYS 118 142 142 LYS LYS A . n 
A 1 119 GLY 119 143 143 GLY GLY A . n 
A 1 120 LYS 120 144 144 LYS LYS A . n 
A 1 121 LEU 121 145 145 LEU LEU A . n 
A 1 122 GLU 122 146 146 GLU GLU A . n 
A 1 123 GLU 123 147 147 GLU GLU A . n 
A 1 124 VAL 124 148 148 VAL VAL A . n 
A 1 125 GLU 125 149 149 GLU GLU A . n 
A 1 126 ASN 126 150 150 ASN ASN A . n 
A 1 127 ASN 127 151 151 ASN ASN A . n 
A 1 128 LEU 128 152 152 LEU LEU A . n 
A 1 129 ARG 129 153 153 ARG ARG A . n 
A 1 130 SER 130 154 154 SER SER A . n 
A 1 131 MET 131 155 155 MET MET A . n 
A 1 132 GLY 132 156 156 GLY GLY A . n 
A 1 133 LYS 133 157 157 LYS LYS A . n 
A 1 134 LEU 134 158 158 LEU LEU A . n 
A 1 135 GLY 135 159 159 GLY GLY A . n 
A 1 136 GLU 136 160 160 GLU GLU A . n 
A 1 137 LYS 137 161 161 LYS LYS A . n 
A 1 138 GLU 138 162 162 GLU GLU A . n 
A 1 139 THR 139 163 163 THR THR A . n 
A 1 140 LEU 140 164 164 LEU LEU A . n 
A 1 141 LYS 141 165 165 LYS LYS A . n 
A 1 142 GLU 142 166 166 GLU GLU A . n 
A 1 143 VAL 143 167 167 VAL VAL A . n 
A 1 144 GLY 144 168 168 GLY GLY A . n 
A 1 145 CYS 145 169 169 CYS CYS A . n 
A 1 146 ILE 146 170 170 ILE ILE A . n 
A 1 147 ASP 147 171 171 ASP ASP A . n 
A 1 148 CYS 148 172 172 CYS CYS A . n 
A 1 149 HIS 149 173 173 HIS HIS A . n 
A 1 150 VAL 150 174 174 VAL VAL A . n 
A 1 151 ASP 151 175 175 ASP ASP A . n 
A 1 152 VAL 152 176 176 VAL VAL A . n 
A 1 153 ASN 153 177 177 ASN ASN A . n 
A 1 154 LYS 154 178 178 LYS LYS A . n 
A 1 155 LYS 155 179 179 LYS LYS A . n 
A 1 156 ASP 156 180 180 ASP ASP A . n 
A 1 157 LYS 157 181 181 LYS LYS A . n 
A 1 158 ALA 158 182 182 ALA ALA A . n 
A 1 159 ASP 159 183 183 ASP ASP A . n 
A 1 160 HIS 160 184 184 HIS HIS A . n 
A 1 161 THR 161 185 185 THR THR A . n 
A 1 162 LYS 162 186 186 LYS LYS A . n 
A 1 163 ASP 163 187 187 ASP ASP A . n 
A 1 164 ILE 164 188 188 ILE ILE A . n 
A 1 165 ARG 165 189 189 ARG ARG A . n 
A 1 166 MET 166 190 190 MET MET A . n 
A 1 167 PRO 167 191 191 PRO PRO A . n 
A 1 168 THR 168 192 192 THR THR A . n 
A 1 169 ALA 169 193 193 ALA ALA A . n 
A 1 170 ASP 170 194 194 ASP ASP A . n 
A 1 171 THR 171 195 195 THR THR A . n 
A 1 172 CYS 172 196 196 CYS CYS A . n 
A 1 173 GLY 173 197 197 GLY GLY A . n 
A 1 174 THR 174 198 198 THR THR A . n 
A 1 175 CYS 175 199 199 CYS CYS A . n 
A 1 176 HIS 176 200 200 HIS HIS A . n 
A 1 177 LEU 177 201 201 LEU LEU A . n 
A 1 178 ARG 178 202 202 ARG ARG A . n 
A 1 179 GLU 179 203 203 GLU GLU A . n 
A 1 180 PHE 180 204 204 PHE PHE A . n 
A 1 181 ALA 181 205 205 ALA ALA A . n 
A 1 182 GLU 182 206 206 GLU GLU A . n 
A 1 183 ARG 183 207 207 ARG ARG A . n 
A 1 184 GLU 184 208 208 GLU GLU A . n 
A 1 185 SER 185 209 209 SER SER A . n 
A 1 186 GLU 186 210 210 GLU GLU A . n 
A 1 187 ARG 187 211 211 ARG ARG A . n 
A 1 188 ASP 188 212 212 ASP ASP A . n 
A 1 189 THR 189 213 213 THR THR A . n 
A 1 190 MET 190 214 214 MET MET A . n 
A 1 191 VAL 191 215 215 VAL VAL A . n 
A 1 192 TRP 192 216 216 TRP TRP A . n 
A 1 193 PRO 193 217 217 PRO PRO A . n 
A 1 194 ASN 194 218 218 ASN ASN A . n 
A 1 195 GLY 195 219 219 GLY GLY A . n 
A 1 196 GLN 196 220 220 GLN GLN A . n 
A 1 197 TRP 197 221 221 TRP TRP A . n 
A 1 198 PRO 198 222 222 PRO PRO A . n 
A 1 199 ALA 199 223 223 ALA ALA A . n 
A 1 200 GLY 200 224 224 GLY GLY A . n 
A 1 201 ARG 201 225 225 ARG ARG A . n 
A 1 202 PRO 202 226 226 PRO PRO A . n 
A 1 203 SER 203 227 227 SER SER A . n 
A 1 204 HIS 204 228 228 HIS HIS A . n 
A 1 205 ALA 205 229 229 ALA ALA A . n 
A 1 206 LEU 206 230 230 LEU LEU A . n 
A 1 207 ASP 207 231 231 ASP ASP A . n 
A 1 208 TYR 208 232 232 TYR TYR A . n 
A 1 209 THR 209 233 233 THR THR A . n 
A 1 210 ALA 210 234 234 ALA ALA A . n 
A 1 211 ASN 211 235 235 ASN ASN A . n 
A 1 212 ILE 212 236 236 ILE ILE A . n 
A 1 213 GLU 213 237 237 GLU GLU A . n 
A 1 214 THR 214 238 238 THR THR A . n 
A 1 215 THR 215 239 239 THR THR A . n 
A 1 216 VAL 216 240 240 VAL VAL A . n 
A 1 217 TRP 217 241 241 TRP TRP A . n 
A 1 218 ALA 218 242 242 ALA ALA A . n 
A 1 219 ALA 219 243 243 ALA ALA A . n 
A 1 220 MET 220 244 244 MET MET A . n 
A 1 221 PRO 221 245 245 PRO PRO A . n 
A 1 222 GLN 222 246 246 GLN GLN A . n 
A 1 223 ARG 223 247 247 ARG ARG A . n 
A 1 224 GLU 224 248 248 GLU GLU A . n 
A 1 225 VAL 225 249 249 VAL VAL A . n 
A 1 226 ALA 226 250 250 ALA ALA A . n 
A 1 227 GLU 227 251 251 GLU GLU A . n 
A 1 228 GLY 228 252 252 GLY GLY A . n 
A 1 229 CYS 229 253 253 CYS CYS A . n 
A 1 230 THR 230 254 254 THR THR A . n 
A 1 231 MET 231 255 255 MET MET A . n 
A 1 232 CYS 232 256 256 CYS CYS A . n 
A 1 233 HIS 233 257 257 HIS HIS A . n 
A 1 234 THR 234 258 258 THR THR A . n 
A 1 235 ASN 235 259 259 ASN ASN A . n 
A 1 236 GLN 236 260 260 GLN GLN A . n 
A 1 237 ASN 237 261 261 ASN ASN A . n 
A 1 238 LYS 238 262 262 LYS LYS A . n 
A 1 239 CYS 239 263 263 CYS CYS A . n 
A 1 240 ASP 240 264 264 ASP ASP A . n 
A 1 241 ASN 241 265 265 ASN ASN A . n 
A 1 242 CYS 242 266 266 CYS CYS A . n 
A 1 243 HIS 243 267 267 HIS HIS A . n 
A 1 244 THR 244 268 268 THR THR A . n 
A 1 245 ARG 245 269 269 ARG ARG A . n 
A 1 246 HIS 246 270 270 HIS HIS A . n 
A 1 247 GLU 247 271 271 GLU GLU A . n 
A 1 248 PHE 248 272 272 PHE PHE A . n 
A 1 249 SER 249 273 273 SER SER A . n 
A 1 250 ALA 250 274 274 ALA ALA A . n 
A 1 251 ALA 251 275 275 ALA ALA A . n 
A 1 252 GLU 252 276 276 GLU GLU A . n 
A 1 253 SER 253 277 277 SER SER A . n 
A 1 254 ARG 254 278 278 ARG ARG A . n 
A 1 255 LYS 255 279 279 LYS LYS A . n 
A 1 256 PRO 256 280 280 PRO PRO A . n 
A 1 257 GLU 257 281 281 GLU GLU A . n 
A 1 258 ALA 258 282 282 ALA ALA A . n 
A 1 259 CYS 259 283 283 CYS CYS A . n 
A 1 260 ALA 260 284 284 ALA ALA A . n 
A 1 261 THR 261 285 285 THR THR A . n 
A 1 262 CYS 262 286 286 CYS CYS A . n 
A 1 263 HIS 263 287 287 HIS HIS A . n 
A 1 264 SER 264 288 288 SER SER A . n 
A 1 265 GLY 265 289 289 GLY GLY A . n 
A 1 266 VAL 266 290 290 VAL VAL A . n 
A 1 267 ASP 267 291 291 ASP ASP A . n 
A 1 268 HIS 268 292 292 HIS HIS A . n 
A 1 269 ASN 269 293 293 ASN ASN A . n 
A 1 270 ASN 270 294 294 ASN ASN A . n 
A 1 271 TRP 271 295 295 TRP TRP A . n 
A 1 272 GLU 272 296 296 GLU GLU A . n 
A 1 273 ALA 273 297 297 ALA ALA A . n 
A 1 274 TYR 274 298 298 TYR TYR A . n 
A 1 275 THR 275 299 299 THR THR A . n 
A 1 276 MET 276 300 300 MET MET A . n 
A 1 277 SER 277 301 301 SER SER A . n 
A 1 278 LYS 278 302 302 LYS LYS A . n 
A 1 279 HIS 279 303 303 HIS HIS A . n 
A 1 280 GLY 280 304 304 GLY GLY A . n 
A 1 281 LYS 281 305 305 LYS LYS A . n 
A 1 282 LEU 282 306 306 LEU LEU A . n 
A 1 283 ALA 283 307 307 ALA ALA A . n 
A 1 284 GLU 284 308 308 GLU GLU A . n 
A 1 285 MET 285 309 309 MET MET A . n 
A 1 286 ASN 286 310 310 ASN ASN A . n 
A 1 287 ARG 287 311 311 ARG ARG A . n 
A 1 288 ASP 288 312 312 ASP ASP A . n 
A 1 289 LYS 289 313 313 LYS LYS A . n 
A 1 290 TRP 290 314 314 TRP TRP A . n 
A 1 291 ASN 291 315 315 ASN ASN A . n 
A 1 292 TRP 292 316 316 TRP TRP A . n 
A 1 293 GLU 293 317 317 GLU GLU A . n 
A 1 294 VAL 294 318 318 VAL VAL A . n 
A 1 295 ARG 295 319 319 ARG ARG A . n 
A 1 296 LEU 296 320 320 LEU LEU A . n 
A 1 297 LYS 297 321 321 LYS LYS A . n 
A 1 298 ASP 298 322 322 ASP ASP A . n 
A 1 299 ALA 299 323 323 ALA ALA A . n 
A 1 300 PHE 300 324 324 PHE PHE A . n 
A 1 301 SER 301 325 325 SER SER A . n 
A 1 302 LYS 302 326 326 LYS LYS A . n 
A 1 303 GLY 303 327 327 GLY GLY A . n 
A 1 304 GLY 304 328 328 GLY GLY A . n 
A 1 305 GLN 305 329 329 GLN GLN A . n 
A 1 306 ASN 306 330 330 ASN ASN A . n 
A 1 307 ALA 307 331 331 ALA ALA A . n 
A 1 308 PRO 308 332 332 PRO PRO A . n 
A 1 309 THR 309 333 333 THR THR A . n 
A 1 310 CYS 310 334 334 CYS CYS A . n 
A 1 311 ALA 311 335 335 ALA ALA A . n 
A 1 312 ALA 312 336 336 ALA ALA A . n 
A 1 313 CYS 313 337 337 CYS CYS A . n 
A 1 314 HIS 314 338 338 HIS HIS A . n 
A 1 315 MET 315 339 339 MET MET A . n 
A 1 316 GLU 316 340 340 GLU GLU A . n 
A 1 317 TYR 317 341 341 TYR TYR A . n 
A 1 318 GLU 318 342 342 GLU GLU A . n 
A 1 319 GLY 319 343 343 GLY GLY A . n 
A 1 320 GLU 320 344 344 GLU GLU A . n 
A 1 321 TYR 321 345 345 TYR TYR A . n 
A 1 322 THR 322 346 346 THR THR A . n 
A 1 323 HIS 323 347 347 HIS HIS A . n 
A 1 324 ASN 324 348 348 ASN ASN A . n 
A 1 325 ILE 325 349 349 ILE ILE A . n 
A 1 326 THR 326 350 350 THR THR A . n 
A 1 327 ARG 327 351 351 ARG ARG A . n 
A 1 328 LYS 328 352 352 LYS LYS A . n 
A 1 329 THR 329 353 353 THR THR A . n 
A 1 330 ARG 330 354 354 ARG ARG A . n 
A 1 331 TRP 331 355 355 TRP TRP A . n 
A 1 332 ALA 332 356 356 ALA ALA A . n 
A 1 333 ASN 333 357 357 ASN ASN A . n 
A 1 334 TYR 334 358 358 TYR TYR A . n 
A 1 335 PRO 335 359 359 PRO PRO A . n 
A 1 336 PHE 336 360 360 PHE PHE A . n 
A 1 337 VAL 337 361 361 VAL VAL A . n 
A 1 338 PRO 338 362 362 PRO PRO A . n 
A 1 339 GLY 339 363 363 GLY GLY A . n 
A 1 340 ILE 340 364 364 ILE ILE A . n 
A 1 341 ALA 341 365 365 ALA ALA A . n 
A 1 342 GLU 342 366 366 GLU GLU A . n 
A 1 343 ASN 343 367 367 ASN ASN A . n 
A 1 344 ILE 344 368 368 ILE ILE A . n 
A 1 345 THR 345 369 369 THR THR A . n 
A 1 346 SER 346 370 370 SER SER A . n 
A 1 347 ASP 347 371 371 ASP ASP A . n 
A 1 348 TRP 348 372 372 TRP TRP A . n 
A 1 349 SER 349 373 373 SER SER A . n 
A 1 350 GLU 350 374 374 GLU GLU A . n 
A 1 351 ALA 351 375 375 ALA ALA A . n 
A 1 352 ARG 352 376 376 ARG ARG A . n 
A 1 353 LEU 353 377 377 LEU LEU A . n 
A 1 354 ASP 354 378 378 ASP ASP A . n 
A 1 355 SER 355 379 379 SER SER A . n 
A 1 356 TRP 356 380 380 TRP TRP A . n 
A 1 357 VAL 357 381 381 VAL VAL A . n 
A 1 358 LEU 358 382 382 LEU LEU A . n 
A 1 359 THR 359 383 383 THR THR A . n 
A 1 360 CYS 360 384 384 CYS CYS A . n 
A 1 361 THR 361 385 385 THR THR A . n 
A 1 362 GLN 362 386 386 GLN GLN A . n 
A 1 363 CYS 363 387 387 CYS CYS A . n 
A 1 364 HIS 364 388 388 HIS HIS A . n 
A 1 365 SER 365 389 389 SER SER A . n 
A 1 366 GLU 366 390 390 GLU GLU A . n 
A 1 367 ARG 367 391 391 ARG ARG A . n 
A 1 368 PHE 368 392 392 PHE PHE A . n 
A 1 369 ALA 369 393 393 ALA ALA A . n 
A 1 370 ARG 370 394 394 ARG ARG A . n 
A 1 371 SER 371 395 395 SER SER A . n 
A 1 372 TYR 372 396 396 TYR TYR A . n 
A 1 373 LEU 373 397 397 LEU LEU A . n 
A 1 374 ASP 374 398 398 ASP ASP A . n 
A 1 375 LEU 375 399 399 LEU LEU A . n 
A 1 376 MET 376 400 400 MET MET A . n 
A 1 377 ASP 377 401 401 ASP ASP A . n 
A 1 378 LYS 378 402 402 LYS LYS A . n 
A 1 379 GLY 379 403 403 GLY GLY A . n 
A 1 380 THR 380 404 404 THR THR A . n 
A 1 381 LEU 381 405 405 LEU LEU A . n 
A 1 382 GLU 382 406 406 GLU GLU A . n 
A 1 383 GLY 383 407 407 GLY GLY A . n 
A 1 384 LEU 384 408 408 LEU LEU A . n 
A 1 385 ALA 385 409 409 ALA ALA A . n 
A 1 386 LYS 386 410 410 LYS LYS A . n 
A 1 387 TYR 387 411 411 TYR TYR A . n 
A 1 388 GLN 388 412 412 GLN GLN A . n 
A 1 389 GLU 389 413 413 GLU GLU A . n 
A 1 390 ALA 390 414 414 ALA ALA A . n 
A 1 391 ASN 391 415 415 ASN ASN A . n 
A 1 392 ALA 392 416 416 ALA ALA A . n 
A 1 393 ILE 393 417 417 ILE ILE A . n 
A 1 394 VAL 394 418 418 VAL VAL A . n 
A 1 395 HIS 395 419 419 HIS HIS A . n 
A 1 396 LYS 396 420 420 LYS LYS A . n 
A 1 397 MET 397 421 421 MET MET A . n 
A 1 398 TYR 398 422 422 TYR TYR A . n 
A 1 399 GLU 399 423 423 GLU GLU A . n 
A 1 400 ASP 400 424 424 ASP ASP A . n 
A 1 401 GLY 401 425 425 GLY GLY A . n 
A 1 402 THR 402 426 426 THR THR A . n 
A 1 403 LEU 403 427 427 LEU LEU A . n 
A 1 404 THR 404 428 428 THR THR A . n 
A 1 405 GLY 405 429 429 GLY GLY A . n 
A 1 406 GLN 406 430 430 GLN GLN A . n 
A 1 407 LYS 407 431 431 LYS LYS A . n 
A 1 408 THR 408 432 432 THR THR A . n 
A 1 409 ASN 409 433 433 ASN ASN A . n 
A 1 410 ARG 410 434 434 ARG ARG A . n 
A 1 411 PRO 411 435 435 PRO PRO A . n 
A 1 412 ASN 412 436 436 ASN ASN A . n 
A 1 413 PRO 413 437 437 PRO PRO A . n 
A 1 414 PRO 414 438 438 PRO PRO A . n 
A 1 415 GLU 415 439 439 GLU GLU A . n 
A 1 416 PRO 416 440 440 PRO PRO A . n 
A 1 417 GLU 417 441 441 GLU GLU A . n 
A 1 418 LYS 418 442 442 LYS LYS A . n 
A 1 419 PRO 419 443 443 PRO PRO A . n 
A 1 420 GLY 420 444 444 GLY GLY A . n 
A 1 421 PHE 421 445 445 PHE PHE A . n 
A 1 422 GLY 422 446 446 GLY GLY A . n 
A 1 423 ILE 423 447 447 ILE ILE A . n 
A 1 424 PHE 424 448 448 PHE PHE A . n 
A 1 425 THR 425 449 449 THR THR A . n 
A 1 426 GLN 426 450 450 GLN GLN A . n 
A 1 427 LEU 427 451 451 LEU LEU A . n 
A 1 428 PHE 428 452 452 PHE PHE A . n 
A 1 429 TRP 429 453 453 TRP TRP A . n 
A 1 430 SER 430 454 454 SER SER A . n 
A 1 431 LYS 431 455 455 LYS LYS A . n 
A 1 432 GLY 432 456 456 GLY GLY A . n 
A 1 433 ASN 433 457 457 ASN ASN A . n 
A 1 434 ASN 434 458 458 ASN ASN A . n 
A 1 435 PRO 435 459 459 PRO PRO A . n 
A 1 436 ALA 436 460 460 ALA ALA A . n 
A 1 437 SER 437 461 461 SER SER A . n 
A 1 438 LEU 438 462 462 LEU LEU A . n 
A 1 439 GLU 439 463 463 GLU GLU A . n 
A 1 440 LEU 440 464 464 LEU LEU A . n 
A 1 441 LYS 441 465 465 LYS LYS A . n 
A 1 442 VAL 442 466 466 VAL VAL A . n 
A 1 443 LEU 443 467 467 LEU LEU A . n 
A 1 444 GLU 444 468 468 GLU GLU A . n 
A 1 445 MET 445 469 469 MET MET A . n 
A 1 446 ALA 446 470 470 ALA ALA A . n 
A 1 447 GLU 447 471 471 GLU GLU A . n 
A 1 448 ASN 448 472 472 ASN ASN A . n 
A 1 449 ASN 449 473 473 ASN ASN A . n 
A 1 450 LEU 450 474 474 LEU LEU A . n 
A 1 451 ALA 451 475 475 ALA ALA A . n 
A 1 452 LYS 452 476 476 LYS LYS A . n 
A 1 453 MET 453 477 477 MET MET A . n 
A 1 454 HIS 454 478 478 HIS HIS A . n 
A 1 455 VAL 455 479 479 VAL VAL A . n 
A 1 456 GLY 456 480 480 GLY GLY A . n 
A 1 457 LEU 457 481 481 LEU LEU A . n 
A 1 458 ALA 458 482 482 ALA ALA A . n 
A 1 459 HIS 459 483 483 HIS HIS A . n 
A 1 460 VAL 460 484 484 VAL VAL A . n 
A 1 461 ASN 461 485 485 ASN ASN A . n 
A 1 462 PRO 462 486 486 PRO PRO A . n 
A 1 463 GLY 463 487 487 GLY GLY A . n 
A 1 464 GLY 464 488 488 GLY GLY A . n 
A 1 465 TRP 465 489 489 TRP TRP A . n 
A 1 466 THR 466 490 490 THR THR A . n 
A 1 467 TYR 467 491 491 TYR TYR A . n 
A 1 468 THR 468 492 492 THR THR A . n 
A 1 469 GLU 469 493 493 GLU GLU A . n 
A 1 470 GLY 470 494 494 GLY GLY A . n 
A 1 471 TRP 471 495 495 TRP TRP A . n 
A 1 472 GLY 472 496 496 GLY GLY A . n 
A 1 473 PRO 473 497 497 PRO PRO A . n 
A 1 474 MET 474 498 498 MET MET A . n 
A 1 475 ASN 475 499 499 ASN ASN A . n 
A 1 476 ARG 476 500 500 ARG ARG A . n 
A 1 477 ALA 477 501 501 ALA ALA A . n 
A 1 478 TYR 478 502 502 TYR TYR A . n 
A 1 479 VAL 479 503 503 VAL VAL A . n 
A 1 480 GLU 480 504 504 GLU GLU A . n 
A 1 481 ILE 481 505 505 ILE ILE A . n 
A 1 482 GLN 482 506 506 GLN GLN A . n 
A 1 483 ASP 483 507 507 ASP ASP A . n 
A 1 484 GLU 484 508 508 GLU GLU A . n 
A 1 485 TYR 485 509 509 TYR TYR A . n 
A 1 486 THR 486 510 510 THR THR A . n 
A 1 487 LYS 487 511 511 LYS LYS A . n 
A 1 488 MET 488 512 512 MET MET A . n 
A 1 489 GLN 489 513 513 GLN GLN A . n 
A 1 490 GLU 490 514 514 GLU GLU A . n 
A 1 491 LEU 491 515 515 LEU LEU A . n 
A 1 492 SER 492 516 516 SER SER A . n 
A 1 493 ALA 493 517 517 ALA ALA A . n 
A 1 494 LEU 494 518 518 LEU LEU A . n 
A 1 495 GLN 495 519 519 GLN GLN A . n 
A 1 496 ALA 496 520 520 ALA ALA A . n 
A 1 497 ARG 497 521 521 ARG ARG A . n 
A 1 498 VAL 498 522 522 VAL VAL A . n 
A 1 499 ASN 499 523 523 ASN ASN A . n 
A 1 500 LYS 500 524 524 LYS LYS A . n 
A 1 501 LEU 501 525 525 LEU LEU A . n 
A 1 502 GLU 502 526 526 GLU GLU A . n 
A 1 503 GLY 503 527 527 GLY GLY A . n 
A 1 504 LYS 504 528 528 LYS LYS A . n 
A 1 505 GLN 505 529 ?   ?   ?   A . n 
A 1 506 THR 506 530 ?   ?   ?   A . n 
A 1 507 SER 507 531 ?   ?   ?   A . n 
A 1 508 LEU 508 532 ?   ?   ?   A . n 
A 1 509 LEU 509 533 ?   ?   ?   A . n 
A 1 510 ASP 510 534 ?   ?   ?   A . n 
A 1 511 LEU 511 535 ?   ?   ?   A . n 
A 1 512 LYS 512 536 ?   ?   ?   A . n 
A 1 513 GLY 513 537 ?   ?   ?   A . n 
A 1 514 THR 514 538 ?   ?   ?   A . n 
A 1 515 GLY 515 539 ?   ?   ?   A . n 
A 1 516 GLU 516 540 ?   ?   ?   A . n 
A 1 517 LYS 517 541 ?   ?   ?   A . n 
A 1 518 ILE 518 542 ?   ?   ?   A . n 
A 1 519 SER 519 543 ?   ?   ?   A . n 
A 1 520 LEU 520 544 ?   ?   ?   A . n 
A 1 521 GLY 521 545 ?   ?   ?   A . n 
A 1 522 GLY 522 546 ?   ?   ?   A . n 
A 1 523 LEU 523 547 ?   ?   ?   A . n 
A 1 524 GLY 524 548 ?   ?   ?   A . n 
A 1 525 GLY 525 549 ?   ?   ?   A . n 
A 1 526 GLY 526 550 ?   ?   ?   A . n 
A 1 527 MET 527 551 ?   ?   ?   A . n 
A 1 528 LEU 528 552 ?   ?   ?   A . n 
A 1 529 LEU 529 553 ?   ?   ?   A . n 
A 1 530 ALA 530 554 ?   ?   ?   A . n 
A 1 531 GLY 531 555 ?   ?   ?   A . n 
A 1 532 ALA 532 556 ?   ?   ?   A . n 
A 1 533 LEU 533 557 ?   ?   ?   A . n 
A 1 534 ALA 534 558 ?   ?   ?   A . n 
A 1 535 LEU 535 559 ?   ?   ?   A . n 
A 1 536 ILE 536 560 ?   ?   ?   A . n 
A 1 537 GLY 537 561 ?   ?   ?   A . n 
A 1 538 TRP 538 562 ?   ?   ?   A . n 
A 1 539 ARG 539 563 ?   ?   ?   A . n 
A 1 540 LYS 540 564 ?   ?   ?   A . n 
A 1 541 ARG 541 565 ?   ?   ?   A . n 
A 1 542 LYS 542 566 ?   ?   ?   A . n 
A 1 543 GLN 543 567 ?   ?   ?   A . n 
A 1 544 THR 544 568 ?   ?   ?   A . n 
A 1 545 ARG 545 569 ?   ?   ?   A . n 
A 1 546 ALA 546 570 ?   ?   ?   A . n 
B 2 1   SER 1   28  ?   ?   ?   B . n 
B 2 2   SER 2   29  29  SER SER B . n 
B 2 3   LEU 3   30  30  LEU LEU B . n 
B 2 4   ALA 4   31  31  ALA ALA B . n 
B 2 5   PRO 5   32  32  PRO PRO B . n 
B 2 6   ILE 6   33  33  ILE ILE B . n 
B 2 7   SER 7   34  34  SER SER B . n 
B 2 8   ALA 8   35  35  ALA ALA B . n 
B 2 9   LYS 9   36  36  LYS LYS B . n 
B 2 10  ASP 10  37  37  ASP ASP B . n 
B 2 11  MET 11  38  38  MET MET B . n 
B 2 12  LEU 12  39  39  LEU LEU B . n 
B 2 13  ASP 13  40  40  ASP ASP B . n 
B 2 14  TYR 14  41  41  TYR TYR B . n 
B 2 15  LEU 15  42  42  LEU LEU B . n 
B 2 16  ALA 16  43  43  ALA ALA B . n 
B 2 17  CYS 17  44  44  CYS CYS B . n 
B 2 18  LYS 18  45  45  LYS LYS B . n 
B 2 19  ASP 19  46  46  ASP ASP B . n 
B 2 20  LYS 20  47  47  LYS LYS B . n 
B 2 21  LYS 21  48  48  LYS LYS B . n 
B 2 22  PRO 22  49  49  PRO PRO B . n 
B 2 23  THR 23  50  50  THR THR B . n 
B 2 24  ASP 24  51  51  ASP ASP B . n 
B 2 25  VAL 25  52  52  VAL VAL B . n 
B 2 26  VAL 26  53  53  VAL VAL B . n 
B 2 27  LYS 27  54  54  LYS LYS B . n 
B 2 28  SER 28  55  55  SER SER B . n 
B 2 29  HIS 29  56  56  HIS HIS B . n 
B 2 30  THR 30  57  57  THR THR B . n 
B 2 31  GLU 31  58  58  GLU GLU B . n 
B 2 32  VAL 32  59  59  VAL VAL B . n 
B 2 33  GLU 33  60  60  GLU GLU B . n 
B 2 34  ASN 34  61  61  ASN ASN B . n 
B 2 35  GLY 35  62  62  GLY GLY B . n 
B 2 36  LYS 36  63  63  LYS LYS B . n 
B 2 37  ILE 37  64  64  ILE ILE B . n 
B 2 38  VAL 38  65  65  VAL VAL B . n 
B 2 39  ARG 39  66  66  ARG ARG B . n 
B 2 40  VAL 40  67  67  VAL VAL B . n 
B 2 41  LYS 41  68  68  LYS LYS B . n 
B 2 42  CYS 42  69  69  CYS CYS B . n 
B 2 43  GLY 43  70  70  GLY GLY B . n 
B 2 44  ASP 44  71  71  ASP ASP B . n 
B 2 45  ILE 45  72  72  ILE ILE B . n 
B 2 46  VAL 46  73  73  VAL VAL B . n 
B 2 47  ALA 47  74  74  ALA ALA B . n 
B 2 48  LEU 48  75  75  LEU LEU B . n 
B 2 49  VAL 49  76  76  VAL VAL B . n 
B 2 50  GLN 50  77  77  GLN GLN B . n 
B 2 51  LYS 51  78  78  LYS LYS B . n 
B 2 52  ALA 52  79  79  ALA ALA B . n 
B 2 53  ARG 53  80  80  ARG ARG B . n 
B 2 54  GLU 54  81  81  GLU GLU B . n 
B 2 55  GLN 55  82  82  GLN GLN B . n 
B 2 56  SER 56  83  83  SER SER B . n 
B 2 57  GLY 57  84  84  GLY GLY B . n 
C 1 1   ASP 1   25  25  ASP ASP C . n 
C 1 2   ILE 2   26  26  ILE ILE C . n 
C 1 3   SER 3   27  27  SER SER C . n 
C 1 4   THR 4   28  28  THR THR C . n 
C 1 5   VAL 5   29  29  VAL VAL C . n 
C 1 6   PRO 6   30  30  PRO PRO C . n 
C 1 7   ASP 7   31  31  ASP ASP C . n 
C 1 8   GLU 8   32  32  GLU GLU C . n 
C 1 9   THR 9   33  33  THR THR C . n 
C 1 10  TYR 10  34  34  TYR TYR C . n 
C 1 11  ASP 11  35  35  ASP ASP C . n 
C 1 12  ALA 12  36  36  ALA ALA C . n 
C 1 13  LEU 13  37  37  LEU LEU C . n 
C 1 14  LYS 14  38  38  LYS LYS C . n 
C 1 15  LEU 15  39  39  LEU LEU C . n 
C 1 16  ASP 16  40  40  ASP ASP C . n 
C 1 17  ARG 17  41  41  ARG ARG C . n 
C 1 18  GLY 18  42  42  GLY GLY C . n 
C 1 19  LYS 19  43  43  LYS LYS C . n 
C 1 20  ALA 20  44  44  ALA ALA C . n 
C 1 21  THR 21  45  45  THR THR C . n 
C 1 22  PRO 22  46  46  PRO PRO C . n 
C 1 23  LYS 23  47  47  LYS LYS C . n 
C 1 24  GLU 24  48  48  GLU GLU C . n 
C 1 25  THR 25  49  49  THR THR C . n 
C 1 26  TYR 26  50  50  TYR TYR C . n 
C 1 27  GLU 27  51  51  GLU GLU C . n 
C 1 28  ALA 28  52  52  ALA ALA C . n 
C 1 29  LEU 29  53  53  LEU LEU C . n 
C 1 30  VAL 30  54  54  VAL VAL C . n 
C 1 31  LYS 31  55  55  LYS LYS C . n 
C 1 32  ARG 32  56  56  ARG ARG C . n 
C 1 33  TYR 33  57  57  TYR TYR C . n 
C 1 34  LYS 34  58  58  LYS LYS C . n 
C 1 35  ASP 35  59  59  ASP ASP C . n 
C 1 36  PRO 36  60  60  PRO PRO C . n 
C 1 37  ALA 37  61  61  ALA ALA C . n 
C 1 38  HIS 38  62  62  HIS HIS C . n 
C 1 39  GLY 39  63  63  GLY GLY C . n 
C 1 40  ALA 40  64  64  ALA ALA C . n 
C 1 41  GLY 41  65  65  GLY GLY C . n 
C 1 42  LYS 42  66  66  LYS LYS C . n 
C 1 43  GLY 43  67  67  GLY GLY C . n 
C 1 44  THR 44  68  68  THR THR C . n 
C 1 45  MET 45  69  69  MET MET C . n 
C 1 46  GLY 46  70  70  GLY GLY C . n 
C 1 47  ASP 47  71  71  ASP ASP C . n 
C 1 48  TYR 48  72  72  TYR TYR C . n 
C 1 49  TRP 49  73  73  TRP TRP C . n 
C 1 50  GLU 50  74  74  GLU GLU C . n 
C 1 51  PRO 51  75  75  PRO PRO C . n 
C 1 52  ILE 52  76  76  ILE ILE C . n 
C 1 53  ALA 53  77  77  ALA ALA C . n 
C 1 54  ILE 54  78  78  ILE ILE C . n 
C 1 55  SER 55  79  79  SER SER C . n 
C 1 56  ILE 56  80  80  ILE ILE C . n 
C 1 57  TYR 57  81  81  TYR TYR C . n 
C 1 58  MET 58  82  82  MET MET C . n 
C 1 59  ASP 59  83  83  ASP ASP C . n 
C 1 60  PRO 60  84  84  PRO PRO C . n 
C 1 61  ASN 61  85  85  ASN ASN C . n 
C 1 62  THR 62  86  86  THR THR C . n 
C 1 63  PHE 63  87  87  PHE PHE C . n 
C 1 64  TYR 64  88  88  TYR TYR C . n 
C 1 65  LYS 65  89  89  LYS LYS C . n 
C 1 66  PRO 66  90  90  PRO PRO C . n 
C 1 67  PRO 67  91  91  PRO PRO C . n 
C 1 68  VAL 68  92  92  VAL VAL C . n 
C 1 69  SER 69  93  93  SER SER C . n 
C 1 70  PRO 70  94  94  PRO PRO C . n 
C 1 71  LYS 71  95  95  LYS LYS C . n 
C 1 72  GLU 72  96  96  GLU GLU C . n 
C 1 73  VAL 73  97  97  VAL VAL C . n 
C 1 74  ALA 74  98  98  ALA ALA C . n 
C 1 75  GLU 75  99  99  GLU GLU C . n 
C 1 76  ARG 76  100 100 ARG ARG C . n 
C 1 77  LYS 77  101 101 LYS LYS C . n 
C 1 78  ASP 78  102 102 ASP ASP C . n 
C 1 79  CYS 79  103 103 CYS CYS C . n 
C 1 80  VAL 80  104 104 VAL VAL C . n 
C 1 81  GLU 81  105 105 GLU GLU C . n 
C 1 82  CYS 82  106 106 CYS CYS C . n 
C 1 83  HIS 83  107 107 HIS HIS C . n 
C 1 84  SER 84  108 108 SER SER C . n 
C 1 85  ASP 85  109 109 ASP ASP C . n 
C 1 86  GLU 86  110 110 GLU GLU C . n 
C 1 87  THR 87  111 111 THR THR C . n 
C 1 88  PRO 88  112 112 PRO PRO C . n 
C 1 89  VAL 89  113 113 VAL VAL C . n 
C 1 90  TRP 90  114 114 TRP TRP C . n 
C 1 91  VAL 91  115 115 VAL VAL C . n 
C 1 92  ARG 92  116 116 ARG ARG C . n 
C 1 93  ALA 93  117 117 ALA ALA C . n 
C 1 94  TRP 94  118 118 TRP TRP C . n 
C 1 95  LYS 95  119 119 LYS LYS C . n 
C 1 96  ARG 96  120 120 ARG ARG C . n 
C 1 97  SER 97  121 121 SER SER C . n 
C 1 98  THR 98  122 122 THR THR C . n 
C 1 99  HIS 99  123 123 HIS HIS C . n 
C 1 100 ALA 100 124 124 ALA ALA C . n 
C 1 101 ASN 101 125 125 ASN ASN C . n 
C 1 102 LEU 102 126 126 LEU LEU C . n 
C 1 103 ASP 103 127 127 ASP ASP C . n 
C 1 104 LYS 104 128 128 LYS LYS C . n 
C 1 105 ILE 105 129 129 ILE ILE C . n 
C 1 106 ARG 106 130 130 ARG ARG C . n 
C 1 107 ASN 107 131 131 ASN ASN C . n 
C 1 108 LEU 108 132 132 LEU LEU C . n 
C 1 109 LYS 109 133 133 LYS LYS C . n 
C 1 110 SER 110 134 134 SER SER C . n 
C 1 111 ASP 111 135 135 ASP ASP C . n 
C 1 112 ASP 112 136 136 ASP ASP C . n 
C 1 113 PRO 113 137 137 PRO PRO C . n 
C 1 114 LEU 114 138 138 LEU LEU C . n 
C 1 115 TYR 115 139 139 TYR TYR C . n 
C 1 116 TYR 116 140 140 TYR TYR C . n 
C 1 117 LYS 117 141 141 LYS LYS C . n 
C 1 118 LYS 118 142 142 LYS LYS C . n 
C 1 119 GLY 119 143 143 GLY GLY C . n 
C 1 120 LYS 120 144 144 LYS LYS C . n 
C 1 121 LEU 121 145 145 LEU LEU C . n 
C 1 122 GLU 122 146 146 GLU GLU C . n 
C 1 123 GLU 123 147 147 GLU GLU C . n 
C 1 124 VAL 124 148 148 VAL VAL C . n 
C 1 125 GLU 125 149 149 GLU GLU C . n 
C 1 126 ASN 126 150 150 ASN ASN C . n 
C 1 127 ASN 127 151 151 ASN ASN C . n 
C 1 128 LEU 128 152 152 LEU LEU C . n 
C 1 129 ARG 129 153 153 ARG ARG C . n 
C 1 130 SER 130 154 154 SER SER C . n 
C 1 131 MET 131 155 155 MET MET C . n 
C 1 132 GLY 132 156 156 GLY GLY C . n 
C 1 133 LYS 133 157 157 LYS LYS C . n 
C 1 134 LEU 134 158 158 LEU LEU C . n 
C 1 135 GLY 135 159 159 GLY GLY C . n 
C 1 136 GLU 136 160 160 GLU GLU C . n 
C 1 137 LYS 137 161 161 LYS LYS C . n 
C 1 138 GLU 138 162 162 GLU GLU C . n 
C 1 139 THR 139 163 163 THR THR C . n 
C 1 140 LEU 140 164 164 LEU LEU C . n 
C 1 141 LYS 141 165 165 LYS LYS C . n 
C 1 142 GLU 142 166 166 GLU GLU C . n 
C 1 143 VAL 143 167 167 VAL VAL C . n 
C 1 144 GLY 144 168 168 GLY GLY C . n 
C 1 145 CYS 145 169 169 CYS CYS C . n 
C 1 146 ILE 146 170 170 ILE ILE C . n 
C 1 147 ASP 147 171 171 ASP ASP C . n 
C 1 148 CYS 148 172 172 CYS CYS C . n 
C 1 149 HIS 149 173 173 HIS HIS C . n 
C 1 150 VAL 150 174 174 VAL VAL C . n 
C 1 151 ASP 151 175 175 ASP ASP C . n 
C 1 152 VAL 152 176 176 VAL VAL C . n 
C 1 153 ASN 153 177 177 ASN ASN C . n 
C 1 154 LYS 154 178 178 LYS LYS C . n 
C 1 155 LYS 155 179 179 LYS LYS C . n 
C 1 156 ASP 156 180 180 ASP ASP C . n 
C 1 157 LYS 157 181 181 LYS LYS C . n 
C 1 158 ALA 158 182 182 ALA ALA C . n 
C 1 159 ASP 159 183 183 ASP ASP C . n 
C 1 160 HIS 160 184 184 HIS HIS C . n 
C 1 161 THR 161 185 185 THR THR C . n 
C 1 162 LYS 162 186 186 LYS LYS C . n 
C 1 163 ASP 163 187 187 ASP ASP C . n 
C 1 164 ILE 164 188 188 ILE ILE C . n 
C 1 165 ARG 165 189 189 ARG ARG C . n 
C 1 166 MET 166 190 190 MET MET C . n 
C 1 167 PRO 167 191 191 PRO PRO C . n 
C 1 168 THR 168 192 192 THR THR C . n 
C 1 169 ALA 169 193 193 ALA ALA C . n 
C 1 170 ASP 170 194 194 ASP ASP C . n 
C 1 171 THR 171 195 195 THR THR C . n 
C 1 172 CYS 172 196 196 CYS CYS C . n 
C 1 173 GLY 173 197 197 GLY GLY C . n 
C 1 174 THR 174 198 198 THR THR C . n 
C 1 175 CYS 175 199 199 CYS CYS C . n 
C 1 176 HIS 176 200 200 HIS HIS C . n 
C 1 177 LEU 177 201 201 LEU LEU C . n 
C 1 178 ARG 178 202 202 ARG ARG C . n 
C 1 179 GLU 179 203 203 GLU GLU C . n 
C 1 180 PHE 180 204 204 PHE PHE C . n 
C 1 181 ALA 181 205 205 ALA ALA C . n 
C 1 182 GLU 182 206 206 GLU GLU C . n 
C 1 183 ARG 183 207 207 ARG ARG C . n 
C 1 184 GLU 184 208 208 GLU GLU C . n 
C 1 185 SER 185 209 209 SER SER C . n 
C 1 186 GLU 186 210 210 GLU GLU C . n 
C 1 187 ARG 187 211 211 ARG ARG C . n 
C 1 188 ASP 188 212 212 ASP ASP C . n 
C 1 189 THR 189 213 213 THR THR C . n 
C 1 190 MET 190 214 214 MET MET C . n 
C 1 191 VAL 191 215 215 VAL VAL C . n 
C 1 192 TRP 192 216 216 TRP TRP C . n 
C 1 193 PRO 193 217 217 PRO PRO C . n 
C 1 194 ASN 194 218 218 ASN ASN C . n 
C 1 195 GLY 195 219 219 GLY GLY C . n 
C 1 196 GLN 196 220 220 GLN GLN C . n 
C 1 197 TRP 197 221 221 TRP TRP C . n 
C 1 198 PRO 198 222 222 PRO PRO C . n 
C 1 199 ALA 199 223 223 ALA ALA C . n 
C 1 200 GLY 200 224 224 GLY GLY C . n 
C 1 201 ARG 201 225 225 ARG ARG C . n 
C 1 202 PRO 202 226 226 PRO PRO C . n 
C 1 203 SER 203 227 227 SER SER C . n 
C 1 204 HIS 204 228 228 HIS HIS C . n 
C 1 205 ALA 205 229 229 ALA ALA C . n 
C 1 206 LEU 206 230 230 LEU LEU C . n 
C 1 207 ASP 207 231 231 ASP ASP C . n 
C 1 208 TYR 208 232 232 TYR TYR C . n 
C 1 209 THR 209 233 233 THR THR C . n 
C 1 210 ALA 210 234 234 ALA ALA C . n 
C 1 211 ASN 211 235 235 ASN ASN C . n 
C 1 212 ILE 212 236 236 ILE ILE C . n 
C 1 213 GLU 213 237 237 GLU GLU C . n 
C 1 214 THR 214 238 238 THR THR C . n 
C 1 215 THR 215 239 239 THR THR C . n 
C 1 216 VAL 216 240 240 VAL VAL C . n 
C 1 217 TRP 217 241 241 TRP TRP C . n 
C 1 218 ALA 218 242 242 ALA ALA C . n 
C 1 219 ALA 219 243 243 ALA ALA C . n 
C 1 220 MET 220 244 244 MET MET C . n 
C 1 221 PRO 221 245 245 PRO PRO C . n 
C 1 222 GLN 222 246 246 GLN GLN C . n 
C 1 223 ARG 223 247 247 ARG ARG C . n 
C 1 224 GLU 224 248 248 GLU GLU C . n 
C 1 225 VAL 225 249 249 VAL VAL C . n 
C 1 226 ALA 226 250 250 ALA ALA C . n 
C 1 227 GLU 227 251 251 GLU GLU C . n 
C 1 228 GLY 228 252 252 GLY GLY C . n 
C 1 229 CYS 229 253 253 CYS CYS C . n 
C 1 230 THR 230 254 254 THR THR C . n 
C 1 231 MET 231 255 255 MET MET C . n 
C 1 232 CYS 232 256 256 CYS CYS C . n 
C 1 233 HIS 233 257 257 HIS HIS C . n 
C 1 234 THR 234 258 258 THR THR C . n 
C 1 235 ASN 235 259 259 ASN ASN C . n 
C 1 236 GLN 236 260 260 GLN GLN C . n 
C 1 237 ASN 237 261 261 ASN ASN C . n 
C 1 238 LYS 238 262 262 LYS LYS C . n 
C 1 239 CYS 239 263 263 CYS CYS C . n 
C 1 240 ASP 240 264 264 ASP ASP C . n 
C 1 241 ASN 241 265 265 ASN ASN C . n 
C 1 242 CYS 242 266 266 CYS CYS C . n 
C 1 243 HIS 243 267 267 HIS HIS C . n 
C 1 244 THR 244 268 268 THR THR C . n 
C 1 245 ARG 245 269 269 ARG ARG C . n 
C 1 246 HIS 246 270 270 HIS HIS C . n 
C 1 247 GLU 247 271 271 GLU GLU C . n 
C 1 248 PHE 248 272 272 PHE PHE C . n 
C 1 249 SER 249 273 273 SER SER C . n 
C 1 250 ALA 250 274 274 ALA ALA C . n 
C 1 251 ALA 251 275 275 ALA ALA C . n 
C 1 252 GLU 252 276 276 GLU GLU C . n 
C 1 253 SER 253 277 277 SER SER C . n 
C 1 254 ARG 254 278 278 ARG ARG C . n 
C 1 255 LYS 255 279 279 LYS LYS C . n 
C 1 256 PRO 256 280 280 PRO PRO C . n 
C 1 257 GLU 257 281 281 GLU GLU C . n 
C 1 258 ALA 258 282 282 ALA ALA C . n 
C 1 259 CYS 259 283 283 CYS CYS C . n 
C 1 260 ALA 260 284 284 ALA ALA C . n 
C 1 261 THR 261 285 285 THR THR C . n 
C 1 262 CYS 262 286 286 CYS CYS C . n 
C 1 263 HIS 263 287 287 HIS HIS C . n 
C 1 264 SER 264 288 288 SER SER C . n 
C 1 265 GLY 265 289 289 GLY GLY C . n 
C 1 266 VAL 266 290 290 VAL VAL C . n 
C 1 267 ASP 267 291 291 ASP ASP C . n 
C 1 268 HIS 268 292 292 HIS HIS C . n 
C 1 269 ASN 269 293 293 ASN ASN C . n 
C 1 270 ASN 270 294 294 ASN ASN C . n 
C 1 271 TRP 271 295 295 TRP TRP C . n 
C 1 272 GLU 272 296 296 GLU GLU C . n 
C 1 273 ALA 273 297 297 ALA ALA C . n 
C 1 274 TYR 274 298 298 TYR TYR C . n 
C 1 275 THR 275 299 299 THR THR C . n 
C 1 276 MET 276 300 300 MET MET C . n 
C 1 277 SER 277 301 301 SER SER C . n 
C 1 278 LYS 278 302 302 LYS LYS C . n 
C 1 279 HIS 279 303 303 HIS HIS C . n 
C 1 280 GLY 280 304 304 GLY GLY C . n 
C 1 281 LYS 281 305 305 LYS LYS C . n 
C 1 282 LEU 282 306 306 LEU LEU C . n 
C 1 283 ALA 283 307 307 ALA ALA C . n 
C 1 284 GLU 284 308 308 GLU GLU C . n 
C 1 285 MET 285 309 309 MET MET C . n 
C 1 286 ASN 286 310 310 ASN ASN C . n 
C 1 287 ARG 287 311 311 ARG ARG C . n 
C 1 288 ASP 288 312 312 ASP ASP C . n 
C 1 289 LYS 289 313 313 LYS LYS C . n 
C 1 290 TRP 290 314 314 TRP TRP C . n 
C 1 291 ASN 291 315 315 ASN ASN C . n 
C 1 292 TRP 292 316 316 TRP TRP C . n 
C 1 293 GLU 293 317 317 GLU GLU C . n 
C 1 294 VAL 294 318 318 VAL VAL C . n 
C 1 295 ARG 295 319 319 ARG ARG C . n 
C 1 296 LEU 296 320 320 LEU LEU C . n 
C 1 297 LYS 297 321 321 LYS LYS C . n 
C 1 298 ASP 298 322 322 ASP ASP C . n 
C 1 299 ALA 299 323 323 ALA ALA C . n 
C 1 300 PHE 300 324 324 PHE PHE C . n 
C 1 301 SER 301 325 325 SER SER C . n 
C 1 302 LYS 302 326 326 LYS LYS C . n 
C 1 303 GLY 303 327 327 GLY GLY C . n 
C 1 304 GLY 304 328 328 GLY GLY C . n 
C 1 305 GLN 305 329 329 GLN GLN C . n 
C 1 306 ASN 306 330 330 ASN ASN C . n 
C 1 307 ALA 307 331 331 ALA ALA C . n 
C 1 308 PRO 308 332 332 PRO PRO C . n 
C 1 309 THR 309 333 333 THR THR C . n 
C 1 310 CYS 310 334 334 CYS CYS C . n 
C 1 311 ALA 311 335 335 ALA ALA C . n 
C 1 312 ALA 312 336 336 ALA ALA C . n 
C 1 313 CYS 313 337 337 CYS CYS C . n 
C 1 314 HIS 314 338 338 HIS HIS C . n 
C 1 315 MET 315 339 339 MET MET C . n 
C 1 316 GLU 316 340 340 GLU GLU C . n 
C 1 317 TYR 317 341 341 TYR TYR C . n 
C 1 318 GLU 318 342 342 GLU GLU C . n 
C 1 319 GLY 319 343 343 GLY GLY C . n 
C 1 320 GLU 320 344 344 GLU GLU C . n 
C 1 321 TYR 321 345 345 TYR TYR C . n 
C 1 322 THR 322 346 346 THR THR C . n 
C 1 323 HIS 323 347 347 HIS HIS C . n 
C 1 324 ASN 324 348 348 ASN ASN C . n 
C 1 325 ILE 325 349 349 ILE ILE C . n 
C 1 326 THR 326 350 350 THR THR C . n 
C 1 327 ARG 327 351 351 ARG ARG C . n 
C 1 328 LYS 328 352 352 LYS LYS C . n 
C 1 329 THR 329 353 353 THR THR C . n 
C 1 330 ARG 330 354 354 ARG ARG C . n 
C 1 331 TRP 331 355 355 TRP TRP C . n 
C 1 332 ALA 332 356 356 ALA ALA C . n 
C 1 333 ASN 333 357 357 ASN ASN C . n 
C 1 334 TYR 334 358 358 TYR TYR C . n 
C 1 335 PRO 335 359 359 PRO PRO C . n 
C 1 336 PHE 336 360 360 PHE PHE C . n 
C 1 337 VAL 337 361 361 VAL VAL C . n 
C 1 338 PRO 338 362 362 PRO PRO C . n 
C 1 339 GLY 339 363 363 GLY GLY C . n 
C 1 340 ILE 340 364 364 ILE ILE C . n 
C 1 341 ALA 341 365 365 ALA ALA C . n 
C 1 342 GLU 342 366 366 GLU GLU C . n 
C 1 343 ASN 343 367 367 ASN ASN C . n 
C 1 344 ILE 344 368 368 ILE ILE C . n 
C 1 345 THR 345 369 369 THR THR C . n 
C 1 346 SER 346 370 370 SER SER C . n 
C 1 347 ASP 347 371 371 ASP ASP C . n 
C 1 348 TRP 348 372 372 TRP TRP C . n 
C 1 349 SER 349 373 373 SER SER C . n 
C 1 350 GLU 350 374 374 GLU GLU C . n 
C 1 351 ALA 351 375 375 ALA ALA C . n 
C 1 352 ARG 352 376 376 ARG ARG C . n 
C 1 353 LEU 353 377 377 LEU LEU C . n 
C 1 354 ASP 354 378 378 ASP ASP C . n 
C 1 355 SER 355 379 379 SER SER C . n 
C 1 356 TRP 356 380 380 TRP TRP C . n 
C 1 357 VAL 357 381 381 VAL VAL C . n 
C 1 358 LEU 358 382 382 LEU LEU C . n 
C 1 359 THR 359 383 383 THR THR C . n 
C 1 360 CYS 360 384 384 CYS CYS C . n 
C 1 361 THR 361 385 385 THR THR C . n 
C 1 362 GLN 362 386 386 GLN GLN C . n 
C 1 363 CYS 363 387 387 CYS CYS C . n 
C 1 364 HIS 364 388 388 HIS HIS C . n 
C 1 365 SER 365 389 389 SER SER C . n 
C 1 366 GLU 366 390 390 GLU GLU C . n 
C 1 367 ARG 367 391 391 ARG ARG C . n 
C 1 368 PHE 368 392 392 PHE PHE C . n 
C 1 369 ALA 369 393 393 ALA ALA C . n 
C 1 370 ARG 370 394 394 ARG ARG C . n 
C 1 371 SER 371 395 395 SER SER C . n 
C 1 372 TYR 372 396 396 TYR TYR C . n 
C 1 373 LEU 373 397 397 LEU LEU C . n 
C 1 374 ASP 374 398 398 ASP ASP C . n 
C 1 375 LEU 375 399 399 LEU LEU C . n 
C 1 376 MET 376 400 400 MET MET C . n 
C 1 377 ASP 377 401 401 ASP ASP C . n 
C 1 378 LYS 378 402 402 LYS LYS C . n 
C 1 379 GLY 379 403 403 GLY GLY C . n 
C 1 380 THR 380 404 404 THR THR C . n 
C 1 381 LEU 381 405 405 LEU LEU C . n 
C 1 382 GLU 382 406 406 GLU GLU C . n 
C 1 383 GLY 383 407 407 GLY GLY C . n 
C 1 384 LEU 384 408 408 LEU LEU C . n 
C 1 385 ALA 385 409 409 ALA ALA C . n 
C 1 386 LYS 386 410 410 LYS LYS C . n 
C 1 387 TYR 387 411 411 TYR TYR C . n 
C 1 388 GLN 388 412 412 GLN GLN C . n 
C 1 389 GLU 389 413 413 GLU GLU C . n 
C 1 390 ALA 390 414 414 ALA ALA C . n 
C 1 391 ASN 391 415 415 ASN ASN C . n 
C 1 392 ALA 392 416 416 ALA ALA C . n 
C 1 393 ILE 393 417 417 ILE ILE C . n 
C 1 394 VAL 394 418 418 VAL VAL C . n 
C 1 395 HIS 395 419 419 HIS HIS C . n 
C 1 396 LYS 396 420 420 LYS LYS C . n 
C 1 397 MET 397 421 421 MET MET C . n 
C 1 398 TYR 398 422 422 TYR TYR C . n 
C 1 399 GLU 399 423 423 GLU GLU C . n 
C 1 400 ASP 400 424 424 ASP ASP C . n 
C 1 401 GLY 401 425 425 GLY GLY C . n 
C 1 402 THR 402 426 426 THR THR C . n 
C 1 403 LEU 403 427 427 LEU LEU C . n 
C 1 404 THR 404 428 428 THR THR C . n 
C 1 405 GLY 405 429 429 GLY GLY C . n 
C 1 406 GLN 406 430 430 GLN GLN C . n 
C 1 407 LYS 407 431 431 LYS LYS C . n 
C 1 408 THR 408 432 432 THR THR C . n 
C 1 409 ASN 409 433 433 ASN ASN C . n 
C 1 410 ARG 410 434 434 ARG ARG C . n 
C 1 411 PRO 411 435 435 PRO PRO C . n 
C 1 412 ASN 412 436 436 ASN ASN C . n 
C 1 413 PRO 413 437 437 PRO PRO C . n 
C 1 414 PRO 414 438 438 PRO PRO C . n 
C 1 415 GLU 415 439 439 GLU GLU C . n 
C 1 416 PRO 416 440 440 PRO PRO C . n 
C 1 417 GLU 417 441 441 GLU GLU C . n 
C 1 418 LYS 418 442 442 LYS LYS C . n 
C 1 419 PRO 419 443 443 PRO PRO C . n 
C 1 420 GLY 420 444 444 GLY GLY C . n 
C 1 421 PHE 421 445 445 PHE PHE C . n 
C 1 422 GLY 422 446 446 GLY GLY C . n 
C 1 423 ILE 423 447 447 ILE ILE C . n 
C 1 424 PHE 424 448 448 PHE PHE C . n 
C 1 425 THR 425 449 449 THR THR C . n 
C 1 426 GLN 426 450 450 GLN GLN C . n 
C 1 427 LEU 427 451 451 LEU LEU C . n 
C 1 428 PHE 428 452 452 PHE PHE C . n 
C 1 429 TRP 429 453 453 TRP TRP C . n 
C 1 430 SER 430 454 454 SER SER C . n 
C 1 431 LYS 431 455 455 LYS LYS C . n 
C 1 432 GLY 432 456 456 GLY GLY C . n 
C 1 433 ASN 433 457 457 ASN ASN C . n 
C 1 434 ASN 434 458 458 ASN ASN C . n 
C 1 435 PRO 435 459 459 PRO PRO C . n 
C 1 436 ALA 436 460 460 ALA ALA C . n 
C 1 437 SER 437 461 461 SER SER C . n 
C 1 438 LEU 438 462 462 LEU LEU C . n 
C 1 439 GLU 439 463 463 GLU GLU C . n 
C 1 440 LEU 440 464 464 LEU LEU C . n 
C 1 441 LYS 441 465 465 LYS LYS C . n 
C 1 442 VAL 442 466 466 VAL VAL C . n 
C 1 443 LEU 443 467 467 LEU LEU C . n 
C 1 444 GLU 444 468 468 GLU GLU C . n 
C 1 445 MET 445 469 469 MET MET C . n 
C 1 446 ALA 446 470 470 ALA ALA C . n 
C 1 447 GLU 447 471 471 GLU GLU C . n 
C 1 448 ASN 448 472 472 ASN ASN C . n 
C 1 449 ASN 449 473 473 ASN ASN C . n 
C 1 450 LEU 450 474 474 LEU LEU C . n 
C 1 451 ALA 451 475 475 ALA ALA C . n 
C 1 452 LYS 452 476 476 LYS LYS C . n 
C 1 453 MET 453 477 477 MET MET C . n 
C 1 454 HIS 454 478 478 HIS HIS C . n 
C 1 455 VAL 455 479 479 VAL VAL C . n 
C 1 456 GLY 456 480 480 GLY GLY C . n 
C 1 457 LEU 457 481 481 LEU LEU C . n 
C 1 458 ALA 458 482 482 ALA ALA C . n 
C 1 459 HIS 459 483 483 HIS HIS C . n 
C 1 460 VAL 460 484 484 VAL VAL C . n 
C 1 461 ASN 461 485 485 ASN ASN C . n 
C 1 462 PRO 462 486 486 PRO PRO C . n 
C 1 463 GLY 463 487 487 GLY GLY C . n 
C 1 464 GLY 464 488 488 GLY GLY C . n 
C 1 465 TRP 465 489 489 TRP TRP C . n 
C 1 466 THR 466 490 490 THR THR C . n 
C 1 467 TYR 467 491 491 TYR TYR C . n 
C 1 468 THR 468 492 492 THR THR C . n 
C 1 469 GLU 469 493 493 GLU GLU C . n 
C 1 470 GLY 470 494 494 GLY GLY C . n 
C 1 471 TRP 471 495 495 TRP TRP C . n 
C 1 472 GLY 472 496 496 GLY GLY C . n 
C 1 473 PRO 473 497 497 PRO PRO C . n 
C 1 474 MET 474 498 498 MET MET C . n 
C 1 475 ASN 475 499 499 ASN ASN C . n 
C 1 476 ARG 476 500 500 ARG ARG C . n 
C 1 477 ALA 477 501 501 ALA ALA C . n 
C 1 478 TYR 478 502 502 TYR TYR C . n 
C 1 479 VAL 479 503 503 VAL VAL C . n 
C 1 480 GLU 480 504 504 GLU GLU C . n 
C 1 481 ILE 481 505 505 ILE ILE C . n 
C 1 482 GLN 482 506 506 GLN GLN C . n 
C 1 483 ASP 483 507 507 ASP ASP C . n 
C 1 484 GLU 484 508 508 GLU GLU C . n 
C 1 485 TYR 485 509 509 TYR TYR C . n 
C 1 486 THR 486 510 510 THR THR C . n 
C 1 487 LYS 487 511 511 LYS LYS C . n 
C 1 488 MET 488 512 512 MET MET C . n 
C 1 489 GLN 489 513 513 GLN GLN C . n 
C 1 490 GLU 490 514 514 GLU GLU C . n 
C 1 491 LEU 491 515 515 LEU LEU C . n 
C 1 492 SER 492 516 516 SER SER C . n 
C 1 493 ALA 493 517 517 ALA ALA C . n 
C 1 494 LEU 494 518 518 LEU LEU C . n 
C 1 495 GLN 495 519 519 GLN GLN C . n 
C 1 496 ALA 496 520 520 ALA ALA C . n 
C 1 497 ARG 497 521 521 ARG ARG C . n 
C 1 498 VAL 498 522 522 VAL VAL C . n 
C 1 499 ASN 499 523 523 ASN ASN C . n 
C 1 500 LYS 500 524 524 LYS LYS C . n 
C 1 501 LEU 501 525 525 LEU LEU C . n 
C 1 502 GLU 502 526 526 GLU GLU C . n 
C 1 503 GLY 503 527 ?   ?   ?   C . n 
C 1 504 LYS 504 528 ?   ?   ?   C . n 
C 1 505 GLN 505 529 ?   ?   ?   C . n 
C 1 506 THR 506 530 ?   ?   ?   C . n 
C 1 507 SER 507 531 ?   ?   ?   C . n 
C 1 508 LEU 508 532 ?   ?   ?   C . n 
C 1 509 LEU 509 533 ?   ?   ?   C . n 
C 1 510 ASP 510 534 ?   ?   ?   C . n 
C 1 511 LEU 511 535 ?   ?   ?   C . n 
C 1 512 LYS 512 536 ?   ?   ?   C . n 
C 1 513 GLY 513 537 ?   ?   ?   C . n 
C 1 514 THR 514 538 ?   ?   ?   C . n 
C 1 515 GLY 515 539 ?   ?   ?   C . n 
C 1 516 GLU 516 540 ?   ?   ?   C . n 
C 1 517 LYS 517 541 ?   ?   ?   C . n 
C 1 518 ILE 518 542 ?   ?   ?   C . n 
C 1 519 SER 519 543 ?   ?   ?   C . n 
C 1 520 LEU 520 544 ?   ?   ?   C . n 
C 1 521 GLY 521 545 ?   ?   ?   C . n 
C 1 522 GLY 522 546 ?   ?   ?   C . n 
C 1 523 LEU 523 547 ?   ?   ?   C . n 
C 1 524 GLY 524 548 ?   ?   ?   C . n 
C 1 525 GLY 525 549 ?   ?   ?   C . n 
C 1 526 GLY 526 550 ?   ?   ?   C . n 
C 1 527 MET 527 551 ?   ?   ?   C . n 
C 1 528 LEU 528 552 ?   ?   ?   C . n 
C 1 529 LEU 529 553 ?   ?   ?   C . n 
C 1 530 ALA 530 554 ?   ?   ?   C . n 
C 1 531 GLY 531 555 ?   ?   ?   C . n 
C 1 532 ALA 532 556 ?   ?   ?   C . n 
C 1 533 LEU 533 557 ?   ?   ?   C . n 
C 1 534 ALA 534 558 ?   ?   ?   C . n 
C 1 535 LEU 535 559 ?   ?   ?   C . n 
C 1 536 ILE 536 560 ?   ?   ?   C . n 
C 1 537 GLY 537 561 ?   ?   ?   C . n 
C 1 538 TRP 538 562 ?   ?   ?   C . n 
C 1 539 ARG 539 563 ?   ?   ?   C . n 
C 1 540 LYS 540 564 ?   ?   ?   C . n 
C 1 541 ARG 541 565 ?   ?   ?   C . n 
C 1 542 LYS 542 566 ?   ?   ?   C . n 
C 1 543 GLN 543 567 ?   ?   ?   C . n 
C 1 544 THR 544 568 ?   ?   ?   C . n 
C 1 545 ARG 545 569 ?   ?   ?   C . n 
C 1 546 ALA 546 570 ?   ?   ?   C . n 
D 2 1   SER 1   28  28  SER SER D . n 
D 2 2   SER 2   29  29  SER SER D . n 
D 2 3   LEU 3   30  30  LEU LEU D . n 
D 2 4   ALA 4   31  31  ALA ALA D . n 
D 2 5   PRO 5   32  32  PRO PRO D . n 
D 2 6   ILE 6   33  33  ILE ILE D . n 
D 2 7   SER 7   34  34  SER SER D . n 
D 2 8   ALA 8   35  35  ALA ALA D . n 
D 2 9   LYS 9   36  36  LYS LYS D . n 
D 2 10  ASP 10  37  37  ASP ASP D . n 
D 2 11  MET 11  38  38  MET MET D . n 
D 2 12  LEU 12  39  39  LEU LEU D . n 
D 2 13  ASP 13  40  40  ASP ASP D . n 
D 2 14  TYR 14  41  41  TYR TYR D . n 
D 2 15  LEU 15  42  42  LEU LEU D . n 
D 2 16  ALA 16  43  43  ALA ALA D . n 
D 2 17  CYS 17  44  44  CYS CYS D . n 
D 2 18  LYS 18  45  45  LYS LYS D . n 
D 2 19  ASP 19  46  46  ASP ASP D . n 
D 2 20  LYS 20  47  47  LYS LYS D . n 
D 2 21  LYS 21  48  48  LYS LYS D . n 
D 2 22  PRO 22  49  49  PRO PRO D . n 
D 2 23  THR 23  50  50  THR THR D . n 
D 2 24  ASP 24  51  51  ASP ASP D . n 
D 2 25  VAL 25  52  52  VAL VAL D . n 
D 2 26  VAL 26  53  53  VAL VAL D . n 
D 2 27  LYS 27  54  54  LYS LYS D . n 
D 2 28  SER 28  55  55  SER SER D . n 
D 2 29  HIS 29  56  56  HIS HIS D . n 
D 2 30  THR 30  57  57  THR THR D . n 
D 2 31  GLU 31  58  58  GLU GLU D . n 
D 2 32  VAL 32  59  59  VAL VAL D . n 
D 2 33  GLU 33  60  60  GLU GLU D . n 
D 2 34  ASN 34  61  61  ASN ASN D . n 
D 2 35  GLY 35  62  62  GLY GLY D . n 
D 2 36  LYS 36  63  63  LYS LYS D . n 
D 2 37  ILE 37  64  64  ILE ILE D . n 
D 2 38  VAL 38  65  65  VAL VAL D . n 
D 2 39  ARG 39  66  66  ARG ARG D . n 
D 2 40  VAL 40  67  67  VAL VAL D . n 
D 2 41  LYS 41  68  68  LYS LYS D . n 
D 2 42  CYS 42  69  69  CYS CYS D . n 
D 2 43  GLY 43  70  70  GLY GLY D . n 
D 2 44  ASP 44  71  71  ASP ASP D . n 
D 2 45  ILE 45  72  72  ILE ILE D . n 
D 2 46  VAL 46  73  73  VAL VAL D . n 
D 2 47  ALA 47  74  74  ALA ALA D . n 
D 2 48  LEU 48  75  75  LEU LEU D . n 
D 2 49  VAL 49  76  76  VAL VAL D . n 
D 2 50  GLN 50  77  77  GLN GLN D . n 
D 2 51  LYS 51  78  78  LYS LYS D . n 
D 2 52  ALA 52  79  79  ALA ALA D . n 
D 2 53  ARG 53  80  80  ARG ARG D . n 
D 2 54  GLU 54  81  81  GLU GLU D . n 
D 2 55  GLN 55  82  82  GLN GLN D . n 
D 2 56  SER 56  83  83  SER SER D . n 
D 2 57  GLY 57  84  84  GLY GLY D . n 
E 1 1   ASP 1   25  25  ASP ASP E . n 
E 1 2   ILE 2   26  26  ILE ILE E . n 
E 1 3   SER 3   27  27  SER SER E . n 
E 1 4   THR 4   28  28  THR THR E . n 
E 1 5   VAL 5   29  29  VAL VAL E . n 
E 1 6   PRO 6   30  30  PRO PRO E . n 
E 1 7   ASP 7   31  31  ASP ASP E . n 
E 1 8   GLU 8   32  32  GLU GLU E . n 
E 1 9   THR 9   33  33  THR THR E . n 
E 1 10  TYR 10  34  34  TYR TYR E . n 
E 1 11  ASP 11  35  35  ASP ASP E . n 
E 1 12  ALA 12  36  36  ALA ALA E . n 
E 1 13  LEU 13  37  37  LEU LEU E . n 
E 1 14  LYS 14  38  38  LYS LYS E . n 
E 1 15  LEU 15  39  39  LEU LEU E . n 
E 1 16  ASP 16  40  40  ASP ASP E . n 
E 1 17  ARG 17  41  41  ARG ARG E . n 
E 1 18  GLY 18  42  42  GLY GLY E . n 
E 1 19  LYS 19  43  43  LYS LYS E . n 
E 1 20  ALA 20  44  44  ALA ALA E . n 
E 1 21  THR 21  45  45  THR THR E . n 
E 1 22  PRO 22  46  46  PRO PRO E . n 
E 1 23  LYS 23  47  47  LYS LYS E . n 
E 1 24  GLU 24  48  48  GLU GLU E . n 
E 1 25  THR 25  49  49  THR THR E . n 
E 1 26  TYR 26  50  50  TYR TYR E . n 
E 1 27  GLU 27  51  51  GLU GLU E . n 
E 1 28  ALA 28  52  52  ALA ALA E . n 
E 1 29  LEU 29  53  53  LEU LEU E . n 
E 1 30  VAL 30  54  54  VAL VAL E . n 
E 1 31  LYS 31  55  55  LYS LYS E . n 
E 1 32  ARG 32  56  56  ARG ARG E . n 
E 1 33  TYR 33  57  57  TYR TYR E . n 
E 1 34  LYS 34  58  58  LYS LYS E . n 
E 1 35  ASP 35  59  59  ASP ASP E . n 
E 1 36  PRO 36  60  60  PRO PRO E . n 
E 1 37  ALA 37  61  61  ALA ALA E . n 
E 1 38  HIS 38  62  62  HIS HIS E . n 
E 1 39  GLY 39  63  63  GLY GLY E . n 
E 1 40  ALA 40  64  64  ALA ALA E . n 
E 1 41  GLY 41  65  65  GLY GLY E . n 
E 1 42  LYS 42  66  66  LYS LYS E . n 
E 1 43  GLY 43  67  67  GLY GLY E . n 
E 1 44  THR 44  68  68  THR THR E . n 
E 1 45  MET 45  69  69  MET MET E . n 
E 1 46  GLY 46  70  70  GLY GLY E . n 
E 1 47  ASP 47  71  71  ASP ASP E . n 
E 1 48  TYR 48  72  72  TYR TYR E . n 
E 1 49  TRP 49  73  73  TRP TRP E . n 
E 1 50  GLU 50  74  74  GLU GLU E . n 
E 1 51  PRO 51  75  75  PRO PRO E . n 
E 1 52  ILE 52  76  76  ILE ILE E . n 
E 1 53  ALA 53  77  77  ALA ALA E . n 
E 1 54  ILE 54  78  78  ILE ILE E . n 
E 1 55  SER 55  79  79  SER SER E . n 
E 1 56  ILE 56  80  80  ILE ILE E . n 
E 1 57  TYR 57  81  81  TYR TYR E . n 
E 1 58  MET 58  82  82  MET MET E . n 
E 1 59  ASP 59  83  83  ASP ASP E . n 
E 1 60  PRO 60  84  84  PRO PRO E . n 
E 1 61  ASN 61  85  85  ASN ASN E . n 
E 1 62  THR 62  86  86  THR THR E . n 
E 1 63  PHE 63  87  87  PHE PHE E . n 
E 1 64  TYR 64  88  88  TYR TYR E . n 
E 1 65  LYS 65  89  89  LYS LYS E . n 
E 1 66  PRO 66  90  90  PRO PRO E . n 
E 1 67  PRO 67  91  91  PRO PRO E . n 
E 1 68  VAL 68  92  92  VAL VAL E . n 
E 1 69  SER 69  93  93  SER SER E . n 
E 1 70  PRO 70  94  94  PRO PRO E . n 
E 1 71  LYS 71  95  95  LYS LYS E . n 
E 1 72  GLU 72  96  96  GLU GLU E . n 
E 1 73  VAL 73  97  97  VAL VAL E . n 
E 1 74  ALA 74  98  98  ALA ALA E . n 
E 1 75  GLU 75  99  99  GLU GLU E . n 
E 1 76  ARG 76  100 100 ARG ARG E . n 
E 1 77  LYS 77  101 101 LYS LYS E . n 
E 1 78  ASP 78  102 102 ASP ASP E . n 
E 1 79  CYS 79  103 103 CYS CYS E . n 
E 1 80  VAL 80  104 104 VAL VAL E . n 
E 1 81  GLU 81  105 105 GLU GLU E . n 
E 1 82  CYS 82  106 106 CYS CYS E . n 
E 1 83  HIS 83  107 107 HIS HIS E . n 
E 1 84  SER 84  108 108 SER SER E . n 
E 1 85  ASP 85  109 109 ASP ASP E . n 
E 1 86  GLU 86  110 110 GLU GLU E . n 
E 1 87  THR 87  111 111 THR THR E . n 
E 1 88  PRO 88  112 112 PRO PRO E . n 
E 1 89  VAL 89  113 113 VAL VAL E . n 
E 1 90  TRP 90  114 114 TRP TRP E . n 
E 1 91  VAL 91  115 115 VAL VAL E . n 
E 1 92  ARG 92  116 116 ARG ARG E . n 
E 1 93  ALA 93  117 117 ALA ALA E . n 
E 1 94  TRP 94  118 118 TRP TRP E . n 
E 1 95  LYS 95  119 119 LYS LYS E . n 
E 1 96  ARG 96  120 120 ARG ARG E . n 
E 1 97  SER 97  121 121 SER SER E . n 
E 1 98  THR 98  122 122 THR THR E . n 
E 1 99  HIS 99  123 123 HIS HIS E . n 
E 1 100 ALA 100 124 124 ALA ALA E . n 
E 1 101 ASN 101 125 125 ASN ASN E . n 
E 1 102 LEU 102 126 126 LEU LEU E . n 
E 1 103 ASP 103 127 127 ASP ASP E . n 
E 1 104 LYS 104 128 128 LYS LYS E . n 
E 1 105 ILE 105 129 129 ILE ILE E . n 
E 1 106 ARG 106 130 130 ARG ARG E . n 
E 1 107 ASN 107 131 131 ASN ASN E . n 
E 1 108 LEU 108 132 132 LEU LEU E . n 
E 1 109 LYS 109 133 133 LYS LYS E . n 
E 1 110 SER 110 134 134 SER SER E . n 
E 1 111 ASP 111 135 135 ASP ASP E . n 
E 1 112 ASP 112 136 136 ASP ASP E . n 
E 1 113 PRO 113 137 137 PRO PRO E . n 
E 1 114 LEU 114 138 138 LEU LEU E . n 
E 1 115 TYR 115 139 139 TYR TYR E . n 
E 1 116 TYR 116 140 140 TYR TYR E . n 
E 1 117 LYS 117 141 141 LYS LYS E . n 
E 1 118 LYS 118 142 142 LYS LYS E . n 
E 1 119 GLY 119 143 143 GLY GLY E . n 
E 1 120 LYS 120 144 144 LYS LYS E . n 
E 1 121 LEU 121 145 145 LEU LEU E . n 
E 1 122 GLU 122 146 146 GLU GLU E . n 
E 1 123 GLU 123 147 147 GLU GLU E . n 
E 1 124 VAL 124 148 148 VAL VAL E . n 
E 1 125 GLU 125 149 149 GLU GLU E . n 
E 1 126 ASN 126 150 150 ASN ASN E . n 
E 1 127 ASN 127 151 151 ASN ASN E . n 
E 1 128 LEU 128 152 152 LEU LEU E . n 
E 1 129 ARG 129 153 153 ARG ARG E . n 
E 1 130 SER 130 154 154 SER SER E . n 
E 1 131 MET 131 155 155 MET MET E . n 
E 1 132 GLY 132 156 156 GLY GLY E . n 
E 1 133 LYS 133 157 157 LYS LYS E . n 
E 1 134 LEU 134 158 158 LEU LEU E . n 
E 1 135 GLY 135 159 159 GLY GLY E . n 
E 1 136 GLU 136 160 160 GLU GLU E . n 
E 1 137 LYS 137 161 161 LYS LYS E . n 
E 1 138 GLU 138 162 162 GLU GLU E . n 
E 1 139 THR 139 163 163 THR THR E . n 
E 1 140 LEU 140 164 164 LEU LEU E . n 
E 1 141 LYS 141 165 165 LYS LYS E . n 
E 1 142 GLU 142 166 166 GLU GLU E . n 
E 1 143 VAL 143 167 167 VAL VAL E . n 
E 1 144 GLY 144 168 168 GLY GLY E . n 
E 1 145 CYS 145 169 169 CYS CYS E . n 
E 1 146 ILE 146 170 170 ILE ILE E . n 
E 1 147 ASP 147 171 171 ASP ASP E . n 
E 1 148 CYS 148 172 172 CYS CYS E . n 
E 1 149 HIS 149 173 173 HIS HIS E . n 
E 1 150 VAL 150 174 174 VAL VAL E . n 
E 1 151 ASP 151 175 175 ASP ASP E . n 
E 1 152 VAL 152 176 176 VAL VAL E . n 
E 1 153 ASN 153 177 177 ASN ASN E . n 
E 1 154 LYS 154 178 178 LYS LYS E . n 
E 1 155 LYS 155 179 179 LYS LYS E . n 
E 1 156 ASP 156 180 180 ASP ASP E . n 
E 1 157 LYS 157 181 181 LYS LYS E . n 
E 1 158 ALA 158 182 182 ALA ALA E . n 
E 1 159 ASP 159 183 183 ASP ASP E . n 
E 1 160 HIS 160 184 184 HIS HIS E . n 
E 1 161 THR 161 185 185 THR THR E . n 
E 1 162 LYS 162 186 186 LYS LYS E . n 
E 1 163 ASP 163 187 187 ASP ASP E . n 
E 1 164 ILE 164 188 188 ILE ILE E . n 
E 1 165 ARG 165 189 189 ARG ARG E . n 
E 1 166 MET 166 190 190 MET MET E . n 
E 1 167 PRO 167 191 191 PRO PRO E . n 
E 1 168 THR 168 192 192 THR THR E . n 
E 1 169 ALA 169 193 193 ALA ALA E . n 
E 1 170 ASP 170 194 194 ASP ASP E . n 
E 1 171 THR 171 195 195 THR THR E . n 
E 1 172 CYS 172 196 196 CYS CYS E . n 
E 1 173 GLY 173 197 197 GLY GLY E . n 
E 1 174 THR 174 198 198 THR THR E . n 
E 1 175 CYS 175 199 199 CYS CYS E . n 
E 1 176 HIS 176 200 200 HIS HIS E . n 
E 1 177 LEU 177 201 201 LEU LEU E . n 
E 1 178 ARG 178 202 202 ARG ARG E . n 
E 1 179 GLU 179 203 203 GLU GLU E . n 
E 1 180 PHE 180 204 204 PHE PHE E . n 
E 1 181 ALA 181 205 205 ALA ALA E . n 
E 1 182 GLU 182 206 206 GLU GLU E . n 
E 1 183 ARG 183 207 207 ARG ARG E . n 
E 1 184 GLU 184 208 208 GLU GLU E . n 
E 1 185 SER 185 209 209 SER SER E . n 
E 1 186 GLU 186 210 210 GLU GLU E . n 
E 1 187 ARG 187 211 211 ARG ARG E . n 
E 1 188 ASP 188 212 212 ASP ASP E . n 
E 1 189 THR 189 213 213 THR THR E . n 
E 1 190 MET 190 214 214 MET MET E . n 
E 1 191 VAL 191 215 215 VAL VAL E . n 
E 1 192 TRP 192 216 216 TRP TRP E . n 
E 1 193 PRO 193 217 217 PRO PRO E . n 
E 1 194 ASN 194 218 218 ASN ASN E . n 
E 1 195 GLY 195 219 219 GLY GLY E . n 
E 1 196 GLN 196 220 220 GLN GLN E . n 
E 1 197 TRP 197 221 221 TRP TRP E . n 
E 1 198 PRO 198 222 222 PRO PRO E . n 
E 1 199 ALA 199 223 223 ALA ALA E . n 
E 1 200 GLY 200 224 224 GLY GLY E . n 
E 1 201 ARG 201 225 225 ARG ARG E . n 
E 1 202 PRO 202 226 226 PRO PRO E . n 
E 1 203 SER 203 227 227 SER SER E . n 
E 1 204 HIS 204 228 228 HIS HIS E . n 
E 1 205 ALA 205 229 229 ALA ALA E . n 
E 1 206 LEU 206 230 230 LEU LEU E . n 
E 1 207 ASP 207 231 231 ASP ASP E . n 
E 1 208 TYR 208 232 232 TYR TYR E . n 
E 1 209 THR 209 233 233 THR THR E . n 
E 1 210 ALA 210 234 234 ALA ALA E . n 
E 1 211 ASN 211 235 235 ASN ASN E . n 
E 1 212 ILE 212 236 236 ILE ILE E . n 
E 1 213 GLU 213 237 237 GLU GLU E . n 
E 1 214 THR 214 238 238 THR THR E . n 
E 1 215 THR 215 239 239 THR THR E . n 
E 1 216 VAL 216 240 240 VAL VAL E . n 
E 1 217 TRP 217 241 241 TRP TRP E . n 
E 1 218 ALA 218 242 242 ALA ALA E . n 
E 1 219 ALA 219 243 243 ALA ALA E . n 
E 1 220 MET 220 244 244 MET MET E . n 
E 1 221 PRO 221 245 245 PRO PRO E . n 
E 1 222 GLN 222 246 246 GLN GLN E . n 
E 1 223 ARG 223 247 247 ARG ARG E . n 
E 1 224 GLU 224 248 248 GLU GLU E . n 
E 1 225 VAL 225 249 249 VAL VAL E . n 
E 1 226 ALA 226 250 250 ALA ALA E . n 
E 1 227 GLU 227 251 251 GLU GLU E . n 
E 1 228 GLY 228 252 252 GLY GLY E . n 
E 1 229 CYS 229 253 253 CYS CYS E . n 
E 1 230 THR 230 254 254 THR THR E . n 
E 1 231 MET 231 255 255 MET MET E . n 
E 1 232 CYS 232 256 256 CYS CYS E . n 
E 1 233 HIS 233 257 257 HIS HIS E . n 
E 1 234 THR 234 258 258 THR THR E . n 
E 1 235 ASN 235 259 259 ASN ASN E . n 
E 1 236 GLN 236 260 260 GLN GLN E . n 
E 1 237 ASN 237 261 261 ASN ASN E . n 
E 1 238 LYS 238 262 262 LYS LYS E . n 
E 1 239 CYS 239 263 263 CYS CYS E . n 
E 1 240 ASP 240 264 264 ASP ASP E . n 
E 1 241 ASN 241 265 265 ASN ASN E . n 
E 1 242 CYS 242 266 266 CYS CYS E . n 
E 1 243 HIS 243 267 267 HIS HIS E . n 
E 1 244 THR 244 268 268 THR THR E . n 
E 1 245 ARG 245 269 269 ARG ARG E . n 
E 1 246 HIS 246 270 270 HIS HIS E . n 
E 1 247 GLU 247 271 271 GLU GLU E . n 
E 1 248 PHE 248 272 272 PHE PHE E . n 
E 1 249 SER 249 273 273 SER SER E . n 
E 1 250 ALA 250 274 274 ALA ALA E . n 
E 1 251 ALA 251 275 275 ALA ALA E . n 
E 1 252 GLU 252 276 276 GLU GLU E . n 
E 1 253 SER 253 277 277 SER SER E . n 
E 1 254 ARG 254 278 278 ARG ARG E . n 
E 1 255 LYS 255 279 279 LYS LYS E . n 
E 1 256 PRO 256 280 280 PRO PRO E . n 
E 1 257 GLU 257 281 281 GLU GLU E . n 
E 1 258 ALA 258 282 282 ALA ALA E . n 
E 1 259 CYS 259 283 283 CYS CYS E . n 
E 1 260 ALA 260 284 284 ALA ALA E . n 
E 1 261 THR 261 285 285 THR THR E . n 
E 1 262 CYS 262 286 286 CYS CYS E . n 
E 1 263 HIS 263 287 287 HIS HIS E . n 
E 1 264 SER 264 288 288 SER SER E . n 
E 1 265 GLY 265 289 289 GLY GLY E . n 
E 1 266 VAL 266 290 290 VAL VAL E . n 
E 1 267 ASP 267 291 291 ASP ASP E . n 
E 1 268 HIS 268 292 292 HIS HIS E . n 
E 1 269 ASN 269 293 293 ASN ASN E . n 
E 1 270 ASN 270 294 294 ASN ASN E . n 
E 1 271 TRP 271 295 295 TRP TRP E . n 
E 1 272 GLU 272 296 296 GLU GLU E . n 
E 1 273 ALA 273 297 297 ALA ALA E . n 
E 1 274 TYR 274 298 298 TYR TYR E . n 
E 1 275 THR 275 299 299 THR THR E . n 
E 1 276 MET 276 300 300 MET MET E . n 
E 1 277 SER 277 301 301 SER SER E . n 
E 1 278 LYS 278 302 302 LYS LYS E . n 
E 1 279 HIS 279 303 303 HIS HIS E . n 
E 1 280 GLY 280 304 304 GLY GLY E . n 
E 1 281 LYS 281 305 305 LYS LYS E . n 
E 1 282 LEU 282 306 306 LEU LEU E . n 
E 1 283 ALA 283 307 307 ALA ALA E . n 
E 1 284 GLU 284 308 308 GLU GLU E . n 
E 1 285 MET 285 309 309 MET MET E . n 
E 1 286 ASN 286 310 310 ASN ASN E . n 
E 1 287 ARG 287 311 311 ARG ARG E . n 
E 1 288 ASP 288 312 312 ASP ASP E . n 
E 1 289 LYS 289 313 313 LYS LYS E . n 
E 1 290 TRP 290 314 314 TRP TRP E . n 
E 1 291 ASN 291 315 315 ASN ASN E . n 
E 1 292 TRP 292 316 316 TRP TRP E . n 
E 1 293 GLU 293 317 317 GLU GLU E . n 
E 1 294 VAL 294 318 318 VAL VAL E . n 
E 1 295 ARG 295 319 319 ARG ARG E . n 
E 1 296 LEU 296 320 320 LEU LEU E . n 
E 1 297 LYS 297 321 321 LYS LYS E . n 
E 1 298 ASP 298 322 322 ASP ASP E . n 
E 1 299 ALA 299 323 323 ALA ALA E . n 
E 1 300 PHE 300 324 324 PHE PHE E . n 
E 1 301 SER 301 325 325 SER SER E . n 
E 1 302 LYS 302 326 326 LYS LYS E . n 
E 1 303 GLY 303 327 327 GLY GLY E . n 
E 1 304 GLY 304 328 328 GLY GLY E . n 
E 1 305 GLN 305 329 329 GLN GLN E . n 
E 1 306 ASN 306 330 330 ASN ASN E . n 
E 1 307 ALA 307 331 331 ALA ALA E . n 
E 1 308 PRO 308 332 332 PRO PRO E . n 
E 1 309 THR 309 333 333 THR THR E . n 
E 1 310 CYS 310 334 334 CYS CYS E . n 
E 1 311 ALA 311 335 335 ALA ALA E . n 
E 1 312 ALA 312 336 336 ALA ALA E . n 
E 1 313 CYS 313 337 337 CYS CYS E . n 
E 1 314 HIS 314 338 338 HIS HIS E . n 
E 1 315 MET 315 339 339 MET MET E . n 
E 1 316 GLU 316 340 340 GLU GLU E . n 
E 1 317 TYR 317 341 341 TYR TYR E . n 
E 1 318 GLU 318 342 342 GLU GLU E . n 
E 1 319 GLY 319 343 343 GLY GLY E . n 
E 1 320 GLU 320 344 344 GLU GLU E . n 
E 1 321 TYR 321 345 345 TYR TYR E . n 
E 1 322 THR 322 346 346 THR THR E . n 
E 1 323 HIS 323 347 347 HIS HIS E . n 
E 1 324 ASN 324 348 348 ASN ASN E . n 
E 1 325 ILE 325 349 349 ILE ILE E . n 
E 1 326 THR 326 350 350 THR THR E . n 
E 1 327 ARG 327 351 351 ARG ARG E . n 
E 1 328 LYS 328 352 352 LYS LYS E . n 
E 1 329 THR 329 353 353 THR THR E . n 
E 1 330 ARG 330 354 354 ARG ARG E . n 
E 1 331 TRP 331 355 355 TRP TRP E . n 
E 1 332 ALA 332 356 356 ALA ALA E . n 
E 1 333 ASN 333 357 357 ASN ASN E . n 
E 1 334 TYR 334 358 358 TYR TYR E . n 
E 1 335 PRO 335 359 359 PRO PRO E . n 
E 1 336 PHE 336 360 360 PHE PHE E . n 
E 1 337 VAL 337 361 361 VAL VAL E . n 
E 1 338 PRO 338 362 362 PRO PRO E . n 
E 1 339 GLY 339 363 363 GLY GLY E . n 
E 1 340 ILE 340 364 364 ILE ILE E . n 
E 1 341 ALA 341 365 365 ALA ALA E . n 
E 1 342 GLU 342 366 366 GLU GLU E . n 
E 1 343 ASN 343 367 367 ASN ASN E . n 
E 1 344 ILE 344 368 368 ILE ILE E . n 
E 1 345 THR 345 369 369 THR THR E . n 
E 1 346 SER 346 370 370 SER SER E . n 
E 1 347 ASP 347 371 371 ASP ASP E . n 
E 1 348 TRP 348 372 372 TRP TRP E . n 
E 1 349 SER 349 373 373 SER SER E . n 
E 1 350 GLU 350 374 374 GLU GLU E . n 
E 1 351 ALA 351 375 375 ALA ALA E . n 
E 1 352 ARG 352 376 376 ARG ARG E . n 
E 1 353 LEU 353 377 377 LEU LEU E . n 
E 1 354 ASP 354 378 378 ASP ASP E . n 
E 1 355 SER 355 379 379 SER SER E . n 
E 1 356 TRP 356 380 380 TRP TRP E . n 
E 1 357 VAL 357 381 381 VAL VAL E . n 
E 1 358 LEU 358 382 382 LEU LEU E . n 
E 1 359 THR 359 383 383 THR THR E . n 
E 1 360 CYS 360 384 384 CYS CYS E . n 
E 1 361 THR 361 385 385 THR THR E . n 
E 1 362 GLN 362 386 386 GLN GLN E . n 
E 1 363 CYS 363 387 387 CYS CYS E . n 
E 1 364 HIS 364 388 388 HIS HIS E . n 
E 1 365 SER 365 389 389 SER SER E . n 
E 1 366 GLU 366 390 390 GLU GLU E . n 
E 1 367 ARG 367 391 391 ARG ARG E . n 
E 1 368 PHE 368 392 392 PHE PHE E . n 
E 1 369 ALA 369 393 393 ALA ALA E . n 
E 1 370 ARG 370 394 394 ARG ARG E . n 
E 1 371 SER 371 395 395 SER SER E . n 
E 1 372 TYR 372 396 396 TYR TYR E . n 
E 1 373 LEU 373 397 397 LEU LEU E . n 
E 1 374 ASP 374 398 398 ASP ASP E . n 
E 1 375 LEU 375 399 399 LEU LEU E . n 
E 1 376 MET 376 400 400 MET MET E . n 
E 1 377 ASP 377 401 401 ASP ASP E . n 
E 1 378 LYS 378 402 402 LYS LYS E . n 
E 1 379 GLY 379 403 403 GLY GLY E . n 
E 1 380 THR 380 404 404 THR THR E . n 
E 1 381 LEU 381 405 405 LEU LEU E . n 
E 1 382 GLU 382 406 406 GLU GLU E . n 
E 1 383 GLY 383 407 407 GLY GLY E . n 
E 1 384 LEU 384 408 408 LEU LEU E . n 
E 1 385 ALA 385 409 409 ALA ALA E . n 
E 1 386 LYS 386 410 410 LYS LYS E . n 
E 1 387 TYR 387 411 411 TYR TYR E . n 
E 1 388 GLN 388 412 412 GLN GLN E . n 
E 1 389 GLU 389 413 413 GLU GLU E . n 
E 1 390 ALA 390 414 414 ALA ALA E . n 
E 1 391 ASN 391 415 415 ASN ASN E . n 
E 1 392 ALA 392 416 416 ALA ALA E . n 
E 1 393 ILE 393 417 417 ILE ILE E . n 
E 1 394 VAL 394 418 418 VAL VAL E . n 
E 1 395 HIS 395 419 419 HIS HIS E . n 
E 1 396 LYS 396 420 420 LYS LYS E . n 
E 1 397 MET 397 421 421 MET MET E . n 
E 1 398 TYR 398 422 422 TYR TYR E . n 
E 1 399 GLU 399 423 423 GLU GLU E . n 
E 1 400 ASP 400 424 424 ASP ASP E . n 
E 1 401 GLY 401 425 425 GLY GLY E . n 
E 1 402 THR 402 426 426 THR THR E . n 
E 1 403 LEU 403 427 427 LEU LEU E . n 
E 1 404 THR 404 428 428 THR THR E . n 
E 1 405 GLY 405 429 429 GLY GLY E . n 
E 1 406 GLN 406 430 430 GLN GLN E . n 
E 1 407 LYS 407 431 431 LYS LYS E . n 
E 1 408 THR 408 432 432 THR THR E . n 
E 1 409 ASN 409 433 433 ASN ASN E . n 
E 1 410 ARG 410 434 434 ARG ARG E . n 
E 1 411 PRO 411 435 435 PRO PRO E . n 
E 1 412 ASN 412 436 436 ASN ASN E . n 
E 1 413 PRO 413 437 437 PRO PRO E . n 
E 1 414 PRO 414 438 438 PRO PRO E . n 
E 1 415 GLU 415 439 439 GLU GLU E . n 
E 1 416 PRO 416 440 440 PRO PRO E . n 
E 1 417 GLU 417 441 441 GLU GLU E . n 
E 1 418 LYS 418 442 442 LYS LYS E . n 
E 1 419 PRO 419 443 443 PRO PRO E . n 
E 1 420 GLY 420 444 444 GLY GLY E . n 
E 1 421 PHE 421 445 445 PHE PHE E . n 
E 1 422 GLY 422 446 446 GLY GLY E . n 
E 1 423 ILE 423 447 447 ILE ILE E . n 
E 1 424 PHE 424 448 448 PHE PHE E . n 
E 1 425 THR 425 449 449 THR THR E . n 
E 1 426 GLN 426 450 450 GLN GLN E . n 
E 1 427 LEU 427 451 451 LEU LEU E . n 
E 1 428 PHE 428 452 452 PHE PHE E . n 
E 1 429 TRP 429 453 453 TRP TRP E . n 
E 1 430 SER 430 454 454 SER SER E . n 
E 1 431 LYS 431 455 455 LYS LYS E . n 
E 1 432 GLY 432 456 456 GLY GLY E . n 
E 1 433 ASN 433 457 457 ASN ASN E . n 
E 1 434 ASN 434 458 458 ASN ASN E . n 
E 1 435 PRO 435 459 459 PRO PRO E . n 
E 1 436 ALA 436 460 460 ALA ALA E . n 
E 1 437 SER 437 461 461 SER SER E . n 
E 1 438 LEU 438 462 462 LEU LEU E . n 
E 1 439 GLU 439 463 463 GLU GLU E . n 
E 1 440 LEU 440 464 464 LEU LEU E . n 
E 1 441 LYS 441 465 465 LYS LYS E . n 
E 1 442 VAL 442 466 466 VAL VAL E . n 
E 1 443 LEU 443 467 467 LEU LEU E . n 
E 1 444 GLU 444 468 468 GLU GLU E . n 
E 1 445 MET 445 469 469 MET MET E . n 
E 1 446 ALA 446 470 470 ALA ALA E . n 
E 1 447 GLU 447 471 471 GLU GLU E . n 
E 1 448 ASN 448 472 472 ASN ASN E . n 
E 1 449 ASN 449 473 473 ASN ASN E . n 
E 1 450 LEU 450 474 474 LEU LEU E . n 
E 1 451 ALA 451 475 475 ALA ALA E . n 
E 1 452 LYS 452 476 476 LYS LYS E . n 
E 1 453 MET 453 477 477 MET MET E . n 
E 1 454 HIS 454 478 478 HIS HIS E . n 
E 1 455 VAL 455 479 479 VAL VAL E . n 
E 1 456 GLY 456 480 480 GLY GLY E . n 
E 1 457 LEU 457 481 481 LEU LEU E . n 
E 1 458 ALA 458 482 482 ALA ALA E . n 
E 1 459 HIS 459 483 483 HIS HIS E . n 
E 1 460 VAL 460 484 484 VAL VAL E . n 
E 1 461 ASN 461 485 485 ASN ASN E . n 
E 1 462 PRO 462 486 486 PRO PRO E . n 
E 1 463 GLY 463 487 487 GLY GLY E . n 
E 1 464 GLY 464 488 488 GLY GLY E . n 
E 1 465 TRP 465 489 489 TRP TRP E . n 
E 1 466 THR 466 490 490 THR THR E . n 
E 1 467 TYR 467 491 491 TYR TYR E . n 
E 1 468 THR 468 492 492 THR THR E . n 
E 1 469 GLU 469 493 493 GLU GLU E . n 
E 1 470 GLY 470 494 494 GLY GLY E . n 
E 1 471 TRP 471 495 495 TRP TRP E . n 
E 1 472 GLY 472 496 496 GLY GLY E . n 
E 1 473 PRO 473 497 497 PRO PRO E . n 
E 1 474 MET 474 498 498 MET MET E . n 
E 1 475 ASN 475 499 499 ASN ASN E . n 
E 1 476 ARG 476 500 500 ARG ARG E . n 
E 1 477 ALA 477 501 501 ALA ALA E . n 
E 1 478 TYR 478 502 502 TYR TYR E . n 
E 1 479 VAL 479 503 503 VAL VAL E . n 
E 1 480 GLU 480 504 504 GLU GLU E . n 
E 1 481 ILE 481 505 505 ILE ILE E . n 
E 1 482 GLN 482 506 506 GLN GLN E . n 
E 1 483 ASP 483 507 507 ASP ASP E . n 
E 1 484 GLU 484 508 508 GLU GLU E . n 
E 1 485 TYR 485 509 509 TYR TYR E . n 
E 1 486 THR 486 510 510 THR THR E . n 
E 1 487 LYS 487 511 511 LYS LYS E . n 
E 1 488 MET 488 512 512 MET MET E . n 
E 1 489 GLN 489 513 513 GLN GLN E . n 
E 1 490 GLU 490 514 514 GLU GLU E . n 
E 1 491 LEU 491 515 515 LEU LEU E . n 
E 1 492 SER 492 516 516 SER SER E . n 
E 1 493 ALA 493 517 517 ALA ALA E . n 
E 1 494 LEU 494 518 518 LEU LEU E . n 
E 1 495 GLN 495 519 519 GLN GLN E . n 
E 1 496 ALA 496 520 520 ALA ALA E . n 
E 1 497 ARG 497 521 521 ARG ARG E . n 
E 1 498 VAL 498 522 522 VAL VAL E . n 
E 1 499 ASN 499 523 523 ASN ASN E . n 
E 1 500 LYS 500 524 524 LYS LYS E . n 
E 1 501 LEU 501 525 525 LEU LEU E . n 
E 1 502 GLU 502 526 526 GLU GLU E . n 
E 1 503 GLY 503 527 527 GLY GLY E . n 
E 1 504 LYS 504 528 ?   ?   ?   E . n 
E 1 505 GLN 505 529 ?   ?   ?   E . n 
E 1 506 THR 506 530 ?   ?   ?   E . n 
E 1 507 SER 507 531 ?   ?   ?   E . n 
E 1 508 LEU 508 532 ?   ?   ?   E . n 
E 1 509 LEU 509 533 ?   ?   ?   E . n 
E 1 510 ASP 510 534 ?   ?   ?   E . n 
E 1 511 LEU 511 535 ?   ?   ?   E . n 
E 1 512 LYS 512 536 ?   ?   ?   E . n 
E 1 513 GLY 513 537 ?   ?   ?   E . n 
E 1 514 THR 514 538 ?   ?   ?   E . n 
E 1 515 GLY 515 539 ?   ?   ?   E . n 
E 1 516 GLU 516 540 ?   ?   ?   E . n 
E 1 517 LYS 517 541 ?   ?   ?   E . n 
E 1 518 ILE 518 542 ?   ?   ?   E . n 
E 1 519 SER 519 543 ?   ?   ?   E . n 
E 1 520 LEU 520 544 ?   ?   ?   E . n 
E 1 521 GLY 521 545 ?   ?   ?   E . n 
E 1 522 GLY 522 546 ?   ?   ?   E . n 
E 1 523 LEU 523 547 ?   ?   ?   E . n 
E 1 524 GLY 524 548 ?   ?   ?   E . n 
E 1 525 GLY 525 549 ?   ?   ?   E . n 
E 1 526 GLY 526 550 ?   ?   ?   E . n 
E 1 527 MET 527 551 ?   ?   ?   E . n 
E 1 528 LEU 528 552 ?   ?   ?   E . n 
E 1 529 LEU 529 553 ?   ?   ?   E . n 
E 1 530 ALA 530 554 ?   ?   ?   E . n 
E 1 531 GLY 531 555 ?   ?   ?   E . n 
E 1 532 ALA 532 556 ?   ?   ?   E . n 
E 1 533 LEU 533 557 ?   ?   ?   E . n 
E 1 534 ALA 534 558 ?   ?   ?   E . n 
E 1 535 LEU 535 559 ?   ?   ?   E . n 
E 1 536 ILE 536 560 ?   ?   ?   E . n 
E 1 537 GLY 537 561 ?   ?   ?   E . n 
E 1 538 TRP 538 562 ?   ?   ?   E . n 
E 1 539 ARG 539 563 ?   ?   ?   E . n 
E 1 540 LYS 540 564 ?   ?   ?   E . n 
E 1 541 ARG 541 565 ?   ?   ?   E . n 
E 1 542 LYS 542 566 ?   ?   ?   E . n 
E 1 543 GLN 543 567 ?   ?   ?   E . n 
E 1 544 THR 544 568 ?   ?   ?   E . n 
E 1 545 ARG 545 569 ?   ?   ?   E . n 
E 1 546 ALA 546 570 ?   ?   ?   E . n 
F 2 1   SER 1   28  28  SER SER F . n 
F 2 2   SER 2   29  29  SER SER F . n 
F 2 3   LEU 3   30  30  LEU LEU F . n 
F 2 4   ALA 4   31  31  ALA ALA F . n 
F 2 5   PRO 5   32  32  PRO PRO F . n 
F 2 6   ILE 6   33  33  ILE ILE F . n 
F 2 7   SER 7   34  34  SER SER F . n 
F 2 8   ALA 8   35  35  ALA ALA F . n 
F 2 9   LYS 9   36  36  LYS LYS F . n 
F 2 10  ASP 10  37  37  ASP ASP F . n 
F 2 11  MET 11  38  38  MET MET F . n 
F 2 12  LEU 12  39  39  LEU LEU F . n 
F 2 13  ASP 13  40  40  ASP ASP F . n 
F 2 14  TYR 14  41  41  TYR TYR F . n 
F 2 15  LEU 15  42  42  LEU LEU F . n 
F 2 16  ALA 16  43  43  ALA ALA F . n 
F 2 17  CYS 17  44  44  CYS CYS F . n 
F 2 18  LYS 18  45  45  LYS LYS F . n 
F 2 19  ASP 19  46  46  ASP ASP F . n 
F 2 20  LYS 20  47  47  LYS LYS F . n 
F 2 21  LYS 21  48  48  LYS LYS F . n 
F 2 22  PRO 22  49  49  PRO PRO F . n 
F 2 23  THR 23  50  50  THR THR F . n 
F 2 24  ASP 24  51  51  ASP ASP F . n 
F 2 25  VAL 25  52  52  VAL VAL F . n 
F 2 26  VAL 26  53  53  VAL VAL F . n 
F 2 27  LYS 27  54  54  LYS LYS F . n 
F 2 28  SER 28  55  55  SER SER F . n 
F 2 29  HIS 29  56  56  HIS HIS F . n 
F 2 30  THR 30  57  57  THR THR F . n 
F 2 31  GLU 31  58  58  GLU GLU F . n 
F 2 32  VAL 32  59  59  VAL VAL F . n 
F 2 33  GLU 33  60  60  GLU GLU F . n 
F 2 34  ASN 34  61  61  ASN ASN F . n 
F 2 35  GLY 35  62  62  GLY GLY F . n 
F 2 36  LYS 36  63  63  LYS LYS F . n 
F 2 37  ILE 37  64  64  ILE ILE F . n 
F 2 38  VAL 38  65  65  VAL VAL F . n 
F 2 39  ARG 39  66  66  ARG ARG F . n 
F 2 40  VAL 40  67  67  VAL VAL F . n 
F 2 41  LYS 41  68  68  LYS LYS F . n 
F 2 42  CYS 42  69  69  CYS CYS F . n 
F 2 43  GLY 43  70  70  GLY GLY F . n 
F 2 44  ASP 44  71  71  ASP ASP F . n 
F 2 45  ILE 45  72  72  ILE ILE F . n 
F 2 46  VAL 46  73  73  VAL VAL F . n 
F 2 47  ALA 47  74  74  ALA ALA F . n 
F 2 48  LEU 48  75  75  LEU LEU F . n 
F 2 49  VAL 49  76  76  VAL VAL F . n 
F 2 50  GLN 50  77  77  GLN GLN F . n 
F 2 51  LYS 51  78  78  LYS LYS F . n 
F 2 52  ALA 52  79  79  ALA ALA F . n 
F 2 53  ARG 53  80  80  ARG ARG F . n 
F 2 54  GLU 54  81  81  GLU GLU F . n 
F 2 55  GLN 55  82  82  GLN GLN F . n 
F 2 56  SER 56  83  83  SER SER F . n 
F 2 57  GLY 57  84  ?   ?   ?   F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G  3 HEC 1   601  605  HEC HEM A . 
H  3 HEC 1   602  603  HEC HEM A . 
I  3 HEC 1   603  601  HEC HEM A . 
J  3 HEC 1   604  602  HEC HEM A . 
K  3 HEC 1   605  607  HEC HEM A . 
L  3 HEC 1   606  606  HEC HEM A . 
M  3 HEC 1   607  608  HEC HEM A . 
N  3 HEC 1   608  604  HEC HEC A . 
O  4 K   1   609  1    K   K   A . 
P  3 HEC 1   601  604  HEC HEC C . 
Q  3 HEC 1   602  605  HEC HEM C . 
R  3 HEC 1   603  603  HEC HEM C . 
S  3 HEC 1   604  601  HEC HEM C . 
T  3 HEC 1   605  602  HEC HEM C . 
U  3 HEC 1   606  607  HEC HEM C . 
V  3 HEC 1   607  606  HEC HEM C . 
W  3 HEC 1   608  608  HEC HEM C . 
X  3 HEC 1   601  604  HEC HEC E . 
Y  3 HEC 1   602  605  HEC HEM E . 
Z  3 HEC 1   603  603  HEC HEM E . 
AA 3 HEC 1   604  601  HEC HEM E . 
BA 3 HEC 1   605  602  HEC HEM E . 
CA 3 HEC 1   606  607  HEC HEM E . 
DA 3 HEC 1   607  606  HEC HEM E . 
EA 3 HEC 1   608  608  HEC HEM E . 
FA 5 PO4 1   609  1    PO4 PO4 E . 
GA 6 HOH 1   701  4    HOH HOH A . 
GA 6 HOH 2   702  8    HOH HOH A . 
GA 6 HOH 3   703  12   HOH HOH A . 
GA 6 HOH 4   704  14   HOH HOH A . 
GA 6 HOH 5   705  17   HOH HOH A . 
GA 6 HOH 6   706  27   HOH HOH A . 
GA 6 HOH 7   707  30   HOH HOH A . 
GA 6 HOH 8   708  34   HOH HOH A . 
GA 6 HOH 9   709  36   HOH HOH A . 
GA 6 HOH 10  710  38   HOH HOH A . 
GA 6 HOH 11  711  40   HOH HOH A . 
GA 6 HOH 12  712  44   HOH HOH A . 
GA 6 HOH 13  713  45   HOH HOH A . 
GA 6 HOH 14  714  46   HOH HOH A . 
GA 6 HOH 15  715  47   HOH HOH A . 
GA 6 HOH 16  716  51   HOH HOH A . 
GA 6 HOH 17  717  52   HOH HOH A . 
GA 6 HOH 18  718  54   HOH HOH A . 
GA 6 HOH 19  719  56   HOH HOH A . 
GA 6 HOH 20  720  62   HOH HOH A . 
GA 6 HOH 21  721  76   HOH HOH A . 
GA 6 HOH 22  722  81   HOH HOH A . 
GA 6 HOH 23  723  82   HOH HOH A . 
GA 6 HOH 24  724  85   HOH HOH A . 
GA 6 HOH 25  725  90   HOH HOH A . 
GA 6 HOH 26  726  92   HOH HOH A . 
GA 6 HOH 27  727  94   HOH HOH A . 
GA 6 HOH 28  728  95   HOH HOH A . 
GA 6 HOH 29  729  100  HOH HOH A . 
GA 6 HOH 30  730  106  HOH HOH A . 
GA 6 HOH 31  731  107  HOH HOH A . 
GA 6 HOH 32  732  111  HOH HOH A . 
GA 6 HOH 33  733  122  HOH HOH A . 
GA 6 HOH 34  734  123  HOH HOH A . 
GA 6 HOH 35  735  126  HOH HOH A . 
GA 6 HOH 36  736  129  HOH HOH A . 
GA 6 HOH 37  737  130  HOH HOH A . 
GA 6 HOH 38  738  131  HOH HOH A . 
GA 6 HOH 39  739  133  HOH HOH A . 
GA 6 HOH 40  740  135  HOH HOH A . 
GA 6 HOH 41  741  139  HOH HOH A . 
GA 6 HOH 42  742  143  HOH HOH A . 
GA 6 HOH 43  743  144  HOH HOH A . 
GA 6 HOH 44  744  151  HOH HOH A . 
GA 6 HOH 45  745  152  HOH HOH A . 
GA 6 HOH 46  746  153  HOH HOH A . 
GA 6 HOH 47  747  154  HOH HOH A . 
GA 6 HOH 48  748  155  HOH HOH A . 
GA 6 HOH 49  749  159  HOH HOH A . 
GA 6 HOH 50  750  161  HOH HOH A . 
GA 6 HOH 51  751  162  HOH HOH A . 
GA 6 HOH 52  752  167  HOH HOH A . 
GA 6 HOH 53  753  168  HOH HOH A . 
GA 6 HOH 54  754  169  HOH HOH A . 
GA 6 HOH 55  755  173  HOH HOH A . 
GA 6 HOH 56  756  178  HOH HOH A . 
GA 6 HOH 57  757  179  HOH HOH A . 
GA 6 HOH 58  758  180  HOH HOH A . 
GA 6 HOH 59  759  181  HOH HOH A . 
GA 6 HOH 60  760  183  HOH HOH A . 
GA 6 HOH 61  761  187  HOH HOH A . 
GA 6 HOH 62  762  188  HOH HOH A . 
GA 6 HOH 63  763  190  HOH HOH A . 
GA 6 HOH 64  764  194  HOH HOH A . 
GA 6 HOH 65  765  196  HOH HOH A . 
GA 6 HOH 66  766  197  HOH HOH A . 
GA 6 HOH 67  767  199  HOH HOH A . 
GA 6 HOH 68  768  201  HOH HOH A . 
GA 6 HOH 69  769  203  HOH HOH A . 
GA 6 HOH 70  770  204  HOH HOH A . 
GA 6 HOH 71  771  217  HOH HOH A . 
GA 6 HOH 72  772  219  HOH HOH A . 
GA 6 HOH 73  773  225  HOH HOH A . 
GA 6 HOH 74  774  227  HOH HOH A . 
GA 6 HOH 75  775  228  HOH HOH A . 
GA 6 HOH 76  776  231  HOH HOH A . 
GA 6 HOH 77  777  233  HOH HOH A . 
GA 6 HOH 78  778  234  HOH HOH A . 
GA 6 HOH 79  779  235  HOH HOH A . 
GA 6 HOH 80  780  239  HOH HOH A . 
GA 6 HOH 81  781  249  HOH HOH A . 
GA 6 HOH 82  782  254  HOH HOH A . 
GA 6 HOH 83  783  255  HOH HOH A . 
GA 6 HOH 84  784  271  HOH HOH A . 
GA 6 HOH 85  785  273  HOH HOH A . 
GA 6 HOH 86  786  279  HOH HOH A . 
GA 6 HOH 87  787  280  HOH HOH A . 
GA 6 HOH 88  788  281  HOH HOH A . 
GA 6 HOH 89  789  284  HOH HOH A . 
GA 6 HOH 90  790  293  HOH HOH A . 
GA 6 HOH 91  791  295  HOH HOH A . 
GA 6 HOH 92  792  297  HOH HOH A . 
GA 6 HOH 93  793  300  HOH HOH A . 
GA 6 HOH 94  794  302  HOH HOH A . 
GA 6 HOH 95  795  314  HOH HOH A . 
GA 6 HOH 96  796  319  HOH HOH A . 
GA 6 HOH 97  797  320  HOH HOH A . 
GA 6 HOH 98  798  329  HOH HOH A . 
GA 6 HOH 99  799  331  HOH HOH A . 
GA 6 HOH 100 800  332  HOH HOH A . 
GA 6 HOH 101 801  337  HOH HOH A . 
GA 6 HOH 102 802  347  HOH HOH A . 
GA 6 HOH 103 803  350  HOH HOH A . 
GA 6 HOH 104 804  355  HOH HOH A . 
GA 6 HOH 105 805  357  HOH HOH A . 
GA 6 HOH 106 806  359  HOH HOH A . 
GA 6 HOH 107 807  362  HOH HOH A . 
GA 6 HOH 108 808  366  HOH HOH A . 
GA 6 HOH 109 809  376  HOH HOH A . 
GA 6 HOH 110 810  384  HOH HOH A . 
GA 6 HOH 111 811  387  HOH HOH A . 
GA 6 HOH 112 812  397  HOH HOH A . 
GA 6 HOH 113 813  398  HOH HOH A . 
GA 6 HOH 114 814  406  HOH HOH A . 
GA 6 HOH 115 815  413  HOH HOH A . 
GA 6 HOH 116 816  424  HOH HOH A . 
GA 6 HOH 117 817  425  HOH HOH A . 
GA 6 HOH 118 818  441  HOH HOH A . 
GA 6 HOH 119 819  448  HOH HOH A . 
GA 6 HOH 120 820  449  HOH HOH A . 
GA 6 HOH 121 821  450  HOH HOH A . 
GA 6 HOH 122 822  451  HOH HOH A . 
GA 6 HOH 123 823  457  HOH HOH A . 
GA 6 HOH 124 824  458  HOH HOH A . 
GA 6 HOH 125 825  461  HOH HOH A . 
GA 6 HOH 126 826  466  HOH HOH A . 
GA 6 HOH 127 827  471  HOH HOH A . 
GA 6 HOH 128 828  472  HOH HOH A . 
GA 6 HOH 129 829  476  HOH HOH A . 
GA 6 HOH 130 830  479  HOH HOH A . 
GA 6 HOH 131 831  481  HOH HOH A . 
GA 6 HOH 132 832  490  HOH HOH A . 
GA 6 HOH 133 833  500  HOH HOH A . 
GA 6 HOH 134 834  504  HOH HOH A . 
GA 6 HOH 135 835  513  HOH HOH A . 
GA 6 HOH 136 836  515  HOH HOH A . 
GA 6 HOH 137 837  517  HOH HOH A . 
GA 6 HOH 138 838  524  HOH HOH A . 
GA 6 HOH 139 839  525  HOH HOH A . 
GA 6 HOH 140 840  530  HOH HOH A . 
GA 6 HOH 141 841  531  HOH HOH A . 
GA 6 HOH 142 842  532  HOH HOH A . 
GA 6 HOH 143 843  535  HOH HOH A . 
GA 6 HOH 144 844  536  HOH HOH A . 
GA 6 HOH 145 845  541  HOH HOH A . 
GA 6 HOH 146 846  543  HOH HOH A . 
GA 6 HOH 147 847  544  HOH HOH A . 
GA 6 HOH 148 848  560  HOH HOH A . 
GA 6 HOH 149 849  561  HOH HOH A . 
GA 6 HOH 150 850  562  HOH HOH A . 
GA 6 HOH 151 851  563  HOH HOH A . 
GA 6 HOH 152 852  569  HOH HOH A . 
GA 6 HOH 153 853  574  HOH HOH A . 
GA 6 HOH 154 854  576  HOH HOH A . 
GA 6 HOH 155 855  578  HOH HOH A . 
GA 6 HOH 156 856  580  HOH HOH A . 
GA 6 HOH 157 857  581  HOH HOH A . 
GA 6 HOH 158 858  591  HOH HOH A . 
GA 6 HOH 159 859  592  HOH HOH A . 
GA 6 HOH 160 860  600  HOH HOH A . 
GA 6 HOH 161 861  602  HOH HOH A . 
GA 6 HOH 162 862  603  HOH HOH A . 
GA 6 HOH 163 863  604  HOH HOH A . 
GA 6 HOH 164 864  606  HOH HOH A . 
GA 6 HOH 165 865  607  HOH HOH A . 
GA 6 HOH 166 866  611  HOH HOH A . 
GA 6 HOH 167 867  637  HOH HOH A . 
GA 6 HOH 168 868  640  HOH HOH A . 
GA 6 HOH 169 869  643  HOH HOH A . 
GA 6 HOH 170 870  660  HOH HOH A . 
GA 6 HOH 171 871  667  HOH HOH A . 
GA 6 HOH 172 872  668  HOH HOH A . 
GA 6 HOH 173 873  669  HOH HOH A . 
GA 6 HOH 174 874  675  HOH HOH A . 
GA 6 HOH 175 875  678  HOH HOH A . 
GA 6 HOH 176 876  684  HOH HOH A . 
GA 6 HOH 177 877  689  HOH HOH A . 
GA 6 HOH 178 878  690  HOH HOH A . 
GA 6 HOH 179 879  696  HOH HOH A . 
GA 6 HOH 180 880  700  HOH HOH A . 
GA 6 HOH 181 881  704  HOH HOH A . 
GA 6 HOH 182 882  710  HOH HOH A . 
GA 6 HOH 183 883  713  HOH HOH A . 
GA 6 HOH 184 884  718  HOH HOH A . 
GA 6 HOH 185 885  727  HOH HOH A . 
GA 6 HOH 186 886  732  HOH HOH A . 
GA 6 HOH 187 887  733  HOH HOH A . 
GA 6 HOH 188 888  751  HOH HOH A . 
GA 6 HOH 189 889  752  HOH HOH A . 
GA 6 HOH 190 890  755  HOH HOH A . 
GA 6 HOH 191 891  758  HOH HOH A . 
GA 6 HOH 192 892  775  HOH HOH A . 
GA 6 HOH 193 893  776  HOH HOH A . 
GA 6 HOH 194 894  779  HOH HOH A . 
GA 6 HOH 195 895  781  HOH HOH A . 
GA 6 HOH 196 896  793  HOH HOH A . 
GA 6 HOH 197 897  803  HOH HOH A . 
GA 6 HOH 198 898  807  HOH HOH A . 
GA 6 HOH 199 899  811  HOH HOH A . 
GA 6 HOH 200 900  815  HOH HOH A . 
GA 6 HOH 201 901  826  HOH HOH A . 
GA 6 HOH 202 902  830  HOH HOH A . 
GA 6 HOH 203 903  851  HOH HOH A . 
GA 6 HOH 204 904  854  HOH HOH A . 
GA 6 HOH 205 905  855  HOH HOH A . 
GA 6 HOH 206 906  856  HOH HOH A . 
GA 6 HOH 207 907  857  HOH HOH A . 
GA 6 HOH 208 908  860  HOH HOH A . 
GA 6 HOH 209 909  863  HOH HOH A . 
GA 6 HOH 210 910  865  HOH HOH A . 
GA 6 HOH 211 911  872  HOH HOH A . 
GA 6 HOH 212 912  874  HOH HOH A . 
GA 6 HOH 213 913  881  HOH HOH A . 
GA 6 HOH 214 914  892  HOH HOH A . 
GA 6 HOH 215 915  893  HOH HOH A . 
GA 6 HOH 216 916  896  HOH HOH A . 
GA 6 HOH 217 917  904  HOH HOH A . 
GA 6 HOH 218 918  905  HOH HOH A . 
GA 6 HOH 219 919  921  HOH HOH A . 
GA 6 HOH 220 920  926  HOH HOH A . 
GA 6 HOH 221 921  927  HOH HOH A . 
GA 6 HOH 222 922  935  HOH HOH A . 
GA 6 HOH 223 923  939  HOH HOH A . 
GA 6 HOH 224 924  941  HOH HOH A . 
GA 6 HOH 225 925  964  HOH HOH A . 
GA 6 HOH 226 926  969  HOH HOH A . 
GA 6 HOH 227 927  973  HOH HOH A . 
GA 6 HOH 228 928  987  HOH HOH A . 
GA 6 HOH 229 929  1010 HOH HOH A . 
GA 6 HOH 230 930  1015 HOH HOH A . 
GA 6 HOH 231 931  1020 HOH HOH A . 
GA 6 HOH 232 932  1028 HOH HOH A . 
GA 6 HOH 233 933  1036 HOH HOH A . 
GA 6 HOH 234 934  1045 HOH HOH A . 
GA 6 HOH 235 935  1049 HOH HOH A . 
GA 6 HOH 236 936  1058 HOH HOH A . 
GA 6 HOH 237 937  1061 HOH HOH A . 
GA 6 HOH 238 938  1076 HOH HOH A . 
GA 6 HOH 239 939  1077 HOH HOH A . 
GA 6 HOH 240 940  1082 HOH HOH A . 
GA 6 HOH 241 941  1083 HOH HOH A . 
GA 6 HOH 242 942  1086 HOH HOH A . 
GA 6 HOH 243 943  1094 HOH HOH A . 
GA 6 HOH 244 944  1120 HOH HOH A . 
GA 6 HOH 245 945  1123 HOH HOH A . 
GA 6 HOH 246 946  1131 HOH HOH A . 
GA 6 HOH 247 947  1132 HOH HOH A . 
GA 6 HOH 248 948  1139 HOH HOH A . 
GA 6 HOH 249 949  1142 HOH HOH A . 
GA 6 HOH 250 950  1159 HOH HOH A . 
GA 6 HOH 251 951  1165 HOH HOH A . 
GA 6 HOH 252 952  1175 HOH HOH A . 
GA 6 HOH 253 953  1186 HOH HOH A . 
GA 6 HOH 254 954  1196 HOH HOH A . 
GA 6 HOH 255 955  1197 HOH HOH A . 
GA 6 HOH 256 956  1203 HOH HOH A . 
GA 6 HOH 257 957  1207 HOH HOH A . 
GA 6 HOH 258 958  1226 HOH HOH A . 
GA 6 HOH 259 959  1228 HOH HOH A . 
GA 6 HOH 260 960  1229 HOH HOH A . 
GA 6 HOH 261 961  1233 HOH HOH A . 
GA 6 HOH 262 962  1237 HOH HOH A . 
GA 6 HOH 263 963  1249 HOH HOH A . 
GA 6 HOH 264 964  1262 HOH HOH A . 
GA 6 HOH 265 965  1263 HOH HOH A . 
GA 6 HOH 266 966  1270 HOH HOH A . 
GA 6 HOH 267 967  1271 HOH HOH A . 
GA 6 HOH 268 968  1285 HOH HOH A . 
GA 6 HOH 269 969  1286 HOH HOH A . 
GA 6 HOH 270 970  1288 HOH HOH A . 
GA 6 HOH 271 971  1295 HOH HOH A . 
GA 6 HOH 272 972  1313 HOH HOH A . 
GA 6 HOH 273 973  1314 HOH HOH A . 
GA 6 HOH 274 974  1315 HOH HOH A . 
GA 6 HOH 275 975  1326 HOH HOH A . 
GA 6 HOH 276 976  1330 HOH HOH A . 
GA 6 HOH 277 977  1334 HOH HOH A . 
GA 6 HOH 278 978  1338 HOH HOH A . 
GA 6 HOH 279 979  1341 HOH HOH A . 
GA 6 HOH 280 980  1342 HOH HOH A . 
GA 6 HOH 281 981  1343 HOH HOH A . 
GA 6 HOH 282 982  1346 HOH HOH A . 
GA 6 HOH 283 983  1347 HOH HOH A . 
GA 6 HOH 284 984  1351 HOH HOH A . 
GA 6 HOH 285 985  1354 HOH HOH A . 
GA 6 HOH 286 986  1356 HOH HOH A . 
GA 6 HOH 287 987  1358 HOH HOH A . 
GA 6 HOH 288 988  1361 HOH HOH A . 
GA 6 HOH 289 989  1367 HOH HOH A . 
GA 6 HOH 290 990  1381 HOH HOH A . 
GA 6 HOH 291 991  1384 HOH HOH A . 
GA 6 HOH 292 992  1386 HOH HOH A . 
GA 6 HOH 293 993  1389 HOH HOH A . 
GA 6 HOH 294 994  1406 HOH HOH A . 
GA 6 HOH 295 995  1409 HOH HOH A . 
GA 6 HOH 296 996  1415 HOH HOH A . 
GA 6 HOH 297 997  1418 HOH HOH A . 
GA 6 HOH 298 998  1419 HOH HOH A . 
GA 6 HOH 299 999  1421 HOH HOH A . 
GA 6 HOH 300 1000 1434 HOH HOH A . 
GA 6 HOH 301 1001 1439 HOH HOH A . 
GA 6 HOH 302 1002 1449 HOH HOH A . 
GA 6 HOH 303 1003 1450 HOH HOH A . 
GA 6 HOH 304 1004 1453 HOH HOH A . 
GA 6 HOH 305 1005 1458 HOH HOH A . 
GA 6 HOH 306 1006 1460 HOH HOH A . 
GA 6 HOH 307 1007 1464 HOH HOH A . 
GA 6 HOH 308 1008 1465 HOH HOH A . 
GA 6 HOH 309 1009 1485 HOH HOH A . 
GA 6 HOH 310 1010 1490 HOH HOH A . 
GA 6 HOH 311 1011 1504 HOH HOH A . 
GA 6 HOH 312 1012 1509 HOH HOH A . 
GA 6 HOH 313 1013 1511 HOH HOH A . 
GA 6 HOH 314 1014 1515 HOH HOH A . 
GA 6 HOH 315 1015 1522 HOH HOH A . 
GA 6 HOH 316 1016 1532 HOH HOH A . 
GA 6 HOH 317 1017 1533 HOH HOH A . 
GA 6 HOH 318 1018 1534 HOH HOH A . 
GA 6 HOH 319 1019 1536 HOH HOH A . 
GA 6 HOH 320 1020 1543 HOH HOH A . 
GA 6 HOH 321 1021 1549 HOH HOH A . 
GA 6 HOH 322 1022 1550 HOH HOH A . 
GA 6 HOH 323 1023 1553 HOH HOH A . 
GA 6 HOH 324 1024 1554 HOH HOH A . 
GA 6 HOH 325 1025 1555 HOH HOH A . 
GA 6 HOH 326 1026 1567 HOH HOH A . 
GA 6 HOH 327 1027 1568 HOH HOH A . 
GA 6 HOH 328 1028 1571 HOH HOH A . 
GA 6 HOH 329 1029 1572 HOH HOH A . 
GA 6 HOH 330 1030 963  HOH HOH A . 
HA 6 HOH 1   101  19   HOH HOH B . 
HA 6 HOH 2   102  24   HOH HOH B . 
HA 6 HOH 3   103  61   HOH HOH B . 
HA 6 HOH 4   104  63   HOH HOH B . 
HA 6 HOH 5   105  91   HOH HOH B . 
HA 6 HOH 6   106  99   HOH HOH B . 
HA 6 HOH 7   107  157  HOH HOH B . 
HA 6 HOH 8   108  186  HOH HOH B . 
HA 6 HOH 9   109  191  HOH HOH B . 
HA 6 HOH 10  110  205  HOH HOH B . 
HA 6 HOH 11  111  211  HOH HOH B . 
HA 6 HOH 12  112  244  HOH HOH B . 
HA 6 HOH 13  113  253  HOH HOH B . 
HA 6 HOH 14  114  259  HOH HOH B . 
HA 6 HOH 15  115  274  HOH HOH B . 
HA 6 HOH 16  116  301  HOH HOH B . 
HA 6 HOH 17  117  343  HOH HOH B . 
HA 6 HOH 18  118  496  HOH HOH B . 
HA 6 HOH 19  119  545  HOH HOH B . 
HA 6 HOH 20  120  553  HOH HOH B . 
HA 6 HOH 21  121  619  HOH HOH B . 
HA 6 HOH 22  122  646  HOH HOH B . 
HA 6 HOH 23  123  661  HOH HOH B . 
HA 6 HOH 24  124  804  HOH HOH B . 
HA 6 HOH 25  125  820  HOH HOH B . 
HA 6 HOH 26  126  824  HOH HOH B . 
HA 6 HOH 27  127  901  HOH HOH B . 
HA 6 HOH 28  128  908  HOH HOH B . 
HA 6 HOH 29  129  950  HOH HOH B . 
HA 6 HOH 30  130  966  HOH HOH B . 
HA 6 HOH 31  131  1095 HOH HOH B . 
HA 6 HOH 32  132  1209 HOH HOH B . 
HA 6 HOH 33  133  1238 HOH HOH B . 
HA 6 HOH 34  134  1254 HOH HOH B . 
HA 6 HOH 35  135  1256 HOH HOH B . 
HA 6 HOH 36  136  1335 HOH HOH B . 
HA 6 HOH 37  137  1357 HOH HOH B . 
HA 6 HOH 38  138  1445 HOH HOH B . 
HA 6 HOH 39  139  1446 HOH HOH B . 
HA 6 HOH 40  140  1463 HOH HOH B . 
HA 6 HOH 41  141  1499 HOH HOH B . 
HA 6 HOH 42  142  1548 HOH HOH B . 
IA 6 HOH 1   701  1547 HOH HOH C . 
IA 6 HOH 2   702  2    HOH HOH C . 
IA 6 HOH 3   703  3    HOH HOH C . 
IA 6 HOH 4   704  6    HOH HOH C . 
IA 6 HOH 5   705  7    HOH HOH C . 
IA 6 HOH 6   706  10   HOH HOH C . 
IA 6 HOH 7   707  16   HOH HOH C . 
IA 6 HOH 8   708  18   HOH HOH C . 
IA 6 HOH 9   709  26   HOH HOH C . 
IA 6 HOH 10  710  28   HOH HOH C . 
IA 6 HOH 11  711  29   HOH HOH C . 
IA 6 HOH 12  712  32   HOH HOH C . 
IA 6 HOH 13  713  37   HOH HOH C . 
IA 6 HOH 14  714  39   HOH HOH C . 
IA 6 HOH 15  715  41   HOH HOH C . 
IA 6 HOH 16  716  48   HOH HOH C . 
IA 6 HOH 17  717  66   HOH HOH C . 
IA 6 HOH 18  718  70   HOH HOH C . 
IA 6 HOH 19  719  72   HOH HOH C . 
IA 6 HOH 20  720  73   HOH HOH C . 
IA 6 HOH 21  721  77   HOH HOH C . 
IA 6 HOH 22  722  78   HOH HOH C . 
IA 6 HOH 23  723  93   HOH HOH C . 
IA 6 HOH 24  724  97   HOH HOH C . 
IA 6 HOH 25  725  103  HOH HOH C . 
IA 6 HOH 26  726  104  HOH HOH C . 
IA 6 HOH 27  727  105  HOH HOH C . 
IA 6 HOH 28  728  112  HOH HOH C . 
IA 6 HOH 29  729  113  HOH HOH C . 
IA 6 HOH 30  730  116  HOH HOH C . 
IA 6 HOH 31  731  117  HOH HOH C . 
IA 6 HOH 32  732  124  HOH HOH C . 
IA 6 HOH 33  733  128  HOH HOH C . 
IA 6 HOH 34  734  138  HOH HOH C . 
IA 6 HOH 35  735  141  HOH HOH C . 
IA 6 HOH 36  736  142  HOH HOH C . 
IA 6 HOH 37  737  146  HOH HOH C . 
IA 6 HOH 38  738  174  HOH HOH C . 
IA 6 HOH 39  739  176  HOH HOH C . 
IA 6 HOH 40  740  177  HOH HOH C . 
IA 6 HOH 41  741  182  HOH HOH C . 
IA 6 HOH 42  742  185  HOH HOH C . 
IA 6 HOH 43  743  189  HOH HOH C . 
IA 6 HOH 44  744  192  HOH HOH C . 
IA 6 HOH 45  745  193  HOH HOH C . 
IA 6 HOH 46  746  195  HOH HOH C . 
IA 6 HOH 47  747  198  HOH HOH C . 
IA 6 HOH 48  748  200  HOH HOH C . 
IA 6 HOH 49  749  202  HOH HOH C . 
IA 6 HOH 50  750  207  HOH HOH C . 
IA 6 HOH 51  751  208  HOH HOH C . 
IA 6 HOH 52  752  210  HOH HOH C . 
IA 6 HOH 53  753  212  HOH HOH C . 
IA 6 HOH 54  754  218  HOH HOH C . 
IA 6 HOH 55  755  236  HOH HOH C . 
IA 6 HOH 56  756  237  HOH HOH C . 
IA 6 HOH 57  757  240  HOH HOH C . 
IA 6 HOH 58  758  243  HOH HOH C . 
IA 6 HOH 59  759  246  HOH HOH C . 
IA 6 HOH 60  760  251  HOH HOH C . 
IA 6 HOH 61  761  252  HOH HOH C . 
IA 6 HOH 62  762  256  HOH HOH C . 
IA 6 HOH 63  763  260  HOH HOH C . 
IA 6 HOH 64  764  261  HOH HOH C . 
IA 6 HOH 65  765  262  HOH HOH C . 
IA 6 HOH 66  766  264  HOH HOH C . 
IA 6 HOH 67  767  266  HOH HOH C . 
IA 6 HOH 68  768  270  HOH HOH C . 
IA 6 HOH 69  769  275  HOH HOH C . 
IA 6 HOH 70  770  283  HOH HOH C . 
IA 6 HOH 71  771  288  HOH HOH C . 
IA 6 HOH 72  772  292  HOH HOH C . 
IA 6 HOH 73  773  298  HOH HOH C . 
IA 6 HOH 74  774  304  HOH HOH C . 
IA 6 HOH 75  775  307  HOH HOH C . 
IA 6 HOH 76  776  309  HOH HOH C . 
IA 6 HOH 77  777  311  HOH HOH C . 
IA 6 HOH 78  778  317  HOH HOH C . 
IA 6 HOH 79  779  323  HOH HOH C . 
IA 6 HOH 80  780  324  HOH HOH C . 
IA 6 HOH 81  781  328  HOH HOH C . 
IA 6 HOH 82  782  330  HOH HOH C . 
IA 6 HOH 83  783  334  HOH HOH C . 
IA 6 HOH 84  784  336  HOH HOH C . 
IA 6 HOH 85  785  339  HOH HOH C . 
IA 6 HOH 86  786  344  HOH HOH C . 
IA 6 HOH 87  787  348  HOH HOH C . 
IA 6 HOH 88  788  349  HOH HOH C . 
IA 6 HOH 89  789  351  HOH HOH C . 
IA 6 HOH 90  790  356  HOH HOH C . 
IA 6 HOH 91  791  360  HOH HOH C . 
IA 6 HOH 92  792  361  HOH HOH C . 
IA 6 HOH 93  793  365  HOH HOH C . 
IA 6 HOH 94  794  369  HOH HOH C . 
IA 6 HOH 95  795  371  HOH HOH C . 
IA 6 HOH 96  796  372  HOH HOH C . 
IA 6 HOH 97  797  373  HOH HOH C . 
IA 6 HOH 98  798  375  HOH HOH C . 
IA 6 HOH 99  799  377  HOH HOH C . 
IA 6 HOH 100 800  379  HOH HOH C . 
IA 6 HOH 101 801  380  HOH HOH C . 
IA 6 HOH 102 802  385  HOH HOH C . 
IA 6 HOH 103 803  393  HOH HOH C . 
IA 6 HOH 104 804  394  HOH HOH C . 
IA 6 HOH 105 805  395  HOH HOH C . 
IA 6 HOH 106 806  396  HOH HOH C . 
IA 6 HOH 107 807  399  HOH HOH C . 
IA 6 HOH 108 808  400  HOH HOH C . 
IA 6 HOH 109 809  403  HOH HOH C . 
IA 6 HOH 110 810  414  HOH HOH C . 
IA 6 HOH 111 811  417  HOH HOH C . 
IA 6 HOH 112 812  418  HOH HOH C . 
IA 6 HOH 113 813  419  HOH HOH C . 
IA 6 HOH 114 814  426  HOH HOH C . 
IA 6 HOH 115 815  429  HOH HOH C . 
IA 6 HOH 116 816  432  HOH HOH C . 
IA 6 HOH 117 817  434  HOH HOH C . 
IA 6 HOH 118 818  439  HOH HOH C . 
IA 6 HOH 119 819  463  HOH HOH C . 
IA 6 HOH 120 820  474  HOH HOH C . 
IA 6 HOH 121 821  484  HOH HOH C . 
IA 6 HOH 122 822  487  HOH HOH C . 
IA 6 HOH 123 823  488  HOH HOH C . 
IA 6 HOH 124 824  493  HOH HOH C . 
IA 6 HOH 125 825  494  HOH HOH C . 
IA 6 HOH 126 826  498  HOH HOH C . 
IA 6 HOH 127 827  499  HOH HOH C . 
IA 6 HOH 128 828  501  HOH HOH C . 
IA 6 HOH 129 829  506  HOH HOH C . 
IA 6 HOH 130 830  511  HOH HOH C . 
IA 6 HOH 131 831  512  HOH HOH C . 
IA 6 HOH 132 832  514  HOH HOH C . 
IA 6 HOH 133 833  528  HOH HOH C . 
IA 6 HOH 134 834  533  HOH HOH C . 
IA 6 HOH 135 835  539  HOH HOH C . 
IA 6 HOH 136 836  548  HOH HOH C . 
IA 6 HOH 137 837  549  HOH HOH C . 
IA 6 HOH 138 838  552  HOH HOH C . 
IA 6 HOH 139 839  554  HOH HOH C . 
IA 6 HOH 140 840  556  HOH HOH C . 
IA 6 HOH 141 841  559  HOH HOH C . 
IA 6 HOH 142 842  565  HOH HOH C . 
IA 6 HOH 143 843  573  HOH HOH C . 
IA 6 HOH 144 844  579  HOH HOH C . 
IA 6 HOH 145 845  584  HOH HOH C . 
IA 6 HOH 146 846  588  HOH HOH C . 
IA 6 HOH 147 847  589  HOH HOH C . 
IA 6 HOH 148 848  593  HOH HOH C . 
IA 6 HOH 149 849  597  HOH HOH C . 
IA 6 HOH 150 850  599  HOH HOH C . 
IA 6 HOH 151 851  609  HOH HOH C . 
IA 6 HOH 152 852  610  HOH HOH C . 
IA 6 HOH 153 853  613  HOH HOH C . 
IA 6 HOH 154 854  617  HOH HOH C . 
IA 6 HOH 155 855  618  HOH HOH C . 
IA 6 HOH 156 856  623  HOH HOH C . 
IA 6 HOH 157 857  624  HOH HOH C . 
IA 6 HOH 158 858  628  HOH HOH C . 
IA 6 HOH 159 859  634  HOH HOH C . 
IA 6 HOH 160 860  645  HOH HOH C . 
IA 6 HOH 161 861  647  HOH HOH C . 
IA 6 HOH 162 862  677  HOH HOH C . 
IA 6 HOH 163 863  686  HOH HOH C . 
IA 6 HOH 164 864  688  HOH HOH C . 
IA 6 HOH 165 865  692  HOH HOH C . 
IA 6 HOH 166 866  706  HOH HOH C . 
IA 6 HOH 167 867  714  HOH HOH C . 
IA 6 HOH 168 868  719  HOH HOH C . 
IA 6 HOH 169 869  736  HOH HOH C . 
IA 6 HOH 170 870  741  HOH HOH C . 
IA 6 HOH 171 871  742  HOH HOH C . 
IA 6 HOH 172 872  746  HOH HOH C . 
IA 6 HOH 173 873  747  HOH HOH C . 
IA 6 HOH 174 874  748  HOH HOH C . 
IA 6 HOH 175 875  756  HOH HOH C . 
IA 6 HOH 176 876  767  HOH HOH C . 
IA 6 HOH 177 877  771  HOH HOH C . 
IA 6 HOH 178 878  777  HOH HOH C . 
IA 6 HOH 179 879  783  HOH HOH C . 
IA 6 HOH 180 880  784  HOH HOH C . 
IA 6 HOH 181 881  788  HOH HOH C . 
IA 6 HOH 182 882  794  HOH HOH C . 
IA 6 HOH 183 883  796  HOH HOH C . 
IA 6 HOH 184 884  798  HOH HOH C . 
IA 6 HOH 185 885  799  HOH HOH C . 
IA 6 HOH 186 886  805  HOH HOH C . 
IA 6 HOH 187 887  806  HOH HOH C . 
IA 6 HOH 188 888  810  HOH HOH C . 
IA 6 HOH 189 889  814  HOH HOH C . 
IA 6 HOH 190 890  818  HOH HOH C . 
IA 6 HOH 191 891  819  HOH HOH C . 
IA 6 HOH 192 892  821  HOH HOH C . 
IA 6 HOH 193 893  827  HOH HOH C . 
IA 6 HOH 194 894  841  HOH HOH C . 
IA 6 HOH 195 895  843  HOH HOH C . 
IA 6 HOH 196 896  852  HOH HOH C . 
IA 6 HOH 197 897  871  HOH HOH C . 
IA 6 HOH 198 898  879  HOH HOH C . 
IA 6 HOH 199 899  890  HOH HOH C . 
IA 6 HOH 200 900  906  HOH HOH C . 
IA 6 HOH 201 901  915  HOH HOH C . 
IA 6 HOH 202 902  925  HOH HOH C . 
IA 6 HOH 203 903  930  HOH HOH C . 
IA 6 HOH 204 904  931  HOH HOH C . 
IA 6 HOH 205 905  934  HOH HOH C . 
IA 6 HOH 206 906  942  HOH HOH C . 
IA 6 HOH 207 907  944  HOH HOH C . 
IA 6 HOH 208 908  947  HOH HOH C . 
IA 6 HOH 209 909  948  HOH HOH C . 
IA 6 HOH 210 910  961  HOH HOH C . 
IA 6 HOH 211 911  962  HOH HOH C . 
IA 6 HOH 212 912  974  HOH HOH C . 
IA 6 HOH 213 913  983  HOH HOH C . 
IA 6 HOH 214 914  989  HOH HOH C . 
IA 6 HOH 215 915  997  HOH HOH C . 
IA 6 HOH 216 916  1003 HOH HOH C . 
IA 6 HOH 217 917  1008 HOH HOH C . 
IA 6 HOH 218 918  1014 HOH HOH C . 
IA 6 HOH 219 919  1026 HOH HOH C . 
IA 6 HOH 220 920  1035 HOH HOH C . 
IA 6 HOH 221 921  1040 HOH HOH C . 
IA 6 HOH 222 922  1041 HOH HOH C . 
IA 6 HOH 223 923  1046 HOH HOH C . 
IA 6 HOH 224 924  1060 HOH HOH C . 
IA 6 HOH 225 925  1064 HOH HOH C . 
IA 6 HOH 226 926  1065 HOH HOH C . 
IA 6 HOH 227 927  1067 HOH HOH C . 
IA 6 HOH 228 928  1070 HOH HOH C . 
IA 6 HOH 229 929  1073 HOH HOH C . 
IA 6 HOH 230 930  1080 HOH HOH C . 
IA 6 HOH 231 931  1087 HOH HOH C . 
IA 6 HOH 232 932  1101 HOH HOH C . 
IA 6 HOH 233 933  1103 HOH HOH C . 
IA 6 HOH 234 934  1108 HOH HOH C . 
IA 6 HOH 235 935  1118 HOH HOH C . 
IA 6 HOH 236 936  1121 HOH HOH C . 
IA 6 HOH 237 937  1135 HOH HOH C . 
IA 6 HOH 238 938  1138 HOH HOH C . 
IA 6 HOH 239 939  1156 HOH HOH C . 
IA 6 HOH 240 940  1176 HOH HOH C . 
IA 6 HOH 241 941  1177 HOH HOH C . 
IA 6 HOH 242 942  1179 HOH HOH C . 
IA 6 HOH 243 943  1184 HOH HOH C . 
IA 6 HOH 244 944  1190 HOH HOH C . 
IA 6 HOH 245 945  1192 HOH HOH C . 
IA 6 HOH 246 946  1195 HOH HOH C . 
IA 6 HOH 247 947  1208 HOH HOH C . 
IA 6 HOH 248 948  1242 HOH HOH C . 
IA 6 HOH 249 949  1246 HOH HOH C . 
IA 6 HOH 250 950  1248 HOH HOH C . 
IA 6 HOH 251 951  1257 HOH HOH C . 
IA 6 HOH 252 952  1261 HOH HOH C . 
IA 6 HOH 253 953  1266 HOH HOH C . 
IA 6 HOH 254 954  1273 HOH HOH C . 
IA 6 HOH 255 955  1274 HOH HOH C . 
IA 6 HOH 256 956  1276 HOH HOH C . 
IA 6 HOH 257 957  1279 HOH HOH C . 
IA 6 HOH 258 958  1283 HOH HOH C . 
IA 6 HOH 259 959  1287 HOH HOH C . 
IA 6 HOH 260 960  1289 HOH HOH C . 
IA 6 HOH 261 961  1293 HOH HOH C . 
IA 6 HOH 262 962  1297 HOH HOH C . 
IA 6 HOH 263 963  1298 HOH HOH C . 
IA 6 HOH 264 964  1303 HOH HOH C . 
IA 6 HOH 265 965  1305 HOH HOH C . 
IA 6 HOH 266 966  1309 HOH HOH C . 
IA 6 HOH 267 967  1311 HOH HOH C . 
IA 6 HOH 268 968  1312 HOH HOH C . 
IA 6 HOH 269 969  1316 HOH HOH C . 
IA 6 HOH 270 970  1323 HOH HOH C . 
IA 6 HOH 271 971  1324 HOH HOH C . 
IA 6 HOH 272 972  1325 HOH HOH C . 
IA 6 HOH 273 973  1327 HOH HOH C . 
IA 6 HOH 274 974  1328 HOH HOH C . 
IA 6 HOH 275 975  1337 HOH HOH C . 
IA 6 HOH 276 976  1344 HOH HOH C . 
IA 6 HOH 277 977  1352 HOH HOH C . 
IA 6 HOH 278 978  1359 HOH HOH C . 
IA 6 HOH 279 979  1360 HOH HOH C . 
IA 6 HOH 280 980  1363 HOH HOH C . 
IA 6 HOH 281 981  1370 HOH HOH C . 
IA 6 HOH 282 982  1371 HOH HOH C . 
IA 6 HOH 283 983  1374 HOH HOH C . 
IA 6 HOH 284 984  1376 HOH HOH C . 
IA 6 HOH 285 985  1385 HOH HOH C . 
IA 6 HOH 286 986  1392 HOH HOH C . 
IA 6 HOH 287 987  1393 HOH HOH C . 
IA 6 HOH 288 988  1401 HOH HOH C . 
IA 6 HOH 289 989  1408 HOH HOH C . 
IA 6 HOH 290 990  1410 HOH HOH C . 
IA 6 HOH 291 991  1416 HOH HOH C . 
IA 6 HOH 292 992  1423 HOH HOH C . 
IA 6 HOH 293 993  1425 HOH HOH C . 
IA 6 HOH 294 994  1427 HOH HOH C . 
IA 6 HOH 295 995  1428 HOH HOH C . 
IA 6 HOH 296 996  1430 HOH HOH C . 
IA 6 HOH 297 997  1432 HOH HOH C . 
IA 6 HOH 298 998  1438 HOH HOH C . 
IA 6 HOH 299 999  1440 HOH HOH C . 
IA 6 HOH 300 1000 1443 HOH HOH C . 
IA 6 HOH 301 1001 1448 HOH HOH C . 
IA 6 HOH 302 1002 1456 HOH HOH C . 
IA 6 HOH 303 1003 1459 HOH HOH C . 
IA 6 HOH 304 1004 1462 HOH HOH C . 
IA 6 HOH 305 1005 1466 HOH HOH C . 
IA 6 HOH 306 1006 1480 HOH HOH C . 
IA 6 HOH 307 1007 1482 HOH HOH C . 
IA 6 HOH 308 1008 1489 HOH HOH C . 
IA 6 HOH 309 1009 1494 HOH HOH C . 
IA 6 HOH 310 1010 1501 HOH HOH C . 
IA 6 HOH 311 1011 1503 HOH HOH C . 
IA 6 HOH 312 1012 1505 HOH HOH C . 
IA 6 HOH 313 1013 1508 HOH HOH C . 
IA 6 HOH 314 1014 1518 HOH HOH C . 
IA 6 HOH 315 1015 1524 HOH HOH C . 
IA 6 HOH 316 1016 1526 HOH HOH C . 
IA 6 HOH 317 1017 1528 HOH HOH C . 
IA 6 HOH 318 1018 1545 HOH HOH C . 
IA 6 HOH 319 1019 1559 HOH HOH C . 
IA 6 HOH 320 1020 1560 HOH HOH C . 
IA 6 HOH 321 1021 1561 HOH HOH C . 
IA 6 HOH 322 1022 1562 HOH HOH C . 
IA 6 HOH 323 1023 1563 HOH HOH C . 
IA 6 HOH 324 1024 1564 HOH HOH C . 
IA 6 HOH 325 1025 1565 HOH HOH C . 
IA 6 HOH 326 1026 1566 HOH HOH C . 
IA 6 HOH 327 1027 1573 HOH HOH C . 
IA 6 HOH 328 1028 1574 HOH HOH C . 
JA 6 HOH 1   101  59   HOH HOH D . 
JA 6 HOH 2   102  67   HOH HOH D . 
JA 6 HOH 3   103  69   HOH HOH D . 
JA 6 HOH 4   104  88   HOH HOH D . 
JA 6 HOH 5   105  175  HOH HOH D . 
JA 6 HOH 6   106  245  HOH HOH D . 
JA 6 HOH 7   107  321  HOH HOH D . 
JA 6 HOH 8   108  354  HOH HOH D . 
JA 6 HOH 9   109  374  HOH HOH D . 
JA 6 HOH 10  110  402  HOH HOH D . 
JA 6 HOH 11  111  435  HOH HOH D . 
JA 6 HOH 12  112  445  HOH HOH D . 
JA 6 HOH 13  113  462  HOH HOH D . 
JA 6 HOH 14  114  477  HOH HOH D . 
JA 6 HOH 15  115  478  HOH HOH D . 
JA 6 HOH 16  116  538  HOH HOH D . 
JA 6 HOH 17  117  596  HOH HOH D . 
JA 6 HOH 18  118  627  HOH HOH D . 
JA 6 HOH 19  119  694  HOH HOH D . 
JA 6 HOH 20  120  699  HOH HOH D . 
JA 6 HOH 21  121  722  HOH HOH D . 
JA 6 HOH 22  122  760  HOH HOH D . 
JA 6 HOH 23  123  785  HOH HOH D . 
JA 6 HOH 24  124  869  HOH HOH D . 
JA 6 HOH 25  125  876  HOH HOH D . 
JA 6 HOH 26  126  878  HOH HOH D . 
JA 6 HOH 27  127  882  HOH HOH D . 
JA 6 HOH 28  128  975  HOH HOH D . 
JA 6 HOH 29  129  981  HOH HOH D . 
JA 6 HOH 30  130  1202 HOH HOH D . 
JA 6 HOH 31  131  1245 HOH HOH D . 
JA 6 HOH 32  132  1318 HOH HOH D . 
JA 6 HOH 33  133  1320 HOH HOH D . 
JA 6 HOH 34  134  1365 HOH HOH D . 
JA 6 HOH 35  135  1395 HOH HOH D . 
JA 6 HOH 36  136  1398 HOH HOH D . 
JA 6 HOH 37  137  1519 HOH HOH D . 
KA 6 HOH 1   701  1    HOH HOH E . 
KA 6 HOH 2   702  9    HOH HOH E . 
KA 6 HOH 3   703  13   HOH HOH E . 
KA 6 HOH 4   704  20   HOH HOH E . 
KA 6 HOH 5   705  21   HOH HOH E . 
KA 6 HOH 6   706  23   HOH HOH E . 
KA 6 HOH 7   707  25   HOH HOH E . 
KA 6 HOH 8   708  31   HOH HOH E . 
KA 6 HOH 9   709  35   HOH HOH E . 
KA 6 HOH 10  710  42   HOH HOH E . 
KA 6 HOH 11  711  43   HOH HOH E . 
KA 6 HOH 12  712  50   HOH HOH E . 
KA 6 HOH 13  713  55   HOH HOH E . 
KA 6 HOH 14  714  57   HOH HOH E . 
KA 6 HOH 15  715  60   HOH HOH E . 
KA 6 HOH 16  716  64   HOH HOH E . 
KA 6 HOH 17  717  65   HOH HOH E . 
KA 6 HOH 18  718  68   HOH HOH E . 
KA 6 HOH 19  719  71   HOH HOH E . 
KA 6 HOH 20  720  74   HOH HOH E . 
KA 6 HOH 21  721  75   HOH HOH E . 
KA 6 HOH 22  722  79   HOH HOH E . 
KA 6 HOH 23  723  80   HOH HOH E . 
KA 6 HOH 24  724  83   HOH HOH E . 
KA 6 HOH 25  725  86   HOH HOH E . 
KA 6 HOH 26  726  87   HOH HOH E . 
KA 6 HOH 27  727  96   HOH HOH E . 
KA 6 HOH 28  728  98   HOH HOH E . 
KA 6 HOH 29  729  109  HOH HOH E . 
KA 6 HOH 30  730  110  HOH HOH E . 
KA 6 HOH 31  731  114  HOH HOH E . 
KA 6 HOH 32  732  119  HOH HOH E . 
KA 6 HOH 33  733  132  HOH HOH E . 
KA 6 HOH 34  734  134  HOH HOH E . 
KA 6 HOH 35  735  136  HOH HOH E . 
KA 6 HOH 36  736  137  HOH HOH E . 
KA 6 HOH 37  737  145  HOH HOH E . 
KA 6 HOH 38  738  147  HOH HOH E . 
KA 6 HOH 39  739  148  HOH HOH E . 
KA 6 HOH 40  740  149  HOH HOH E . 
KA 6 HOH 41  741  150  HOH HOH E . 
KA 6 HOH 42  742  156  HOH HOH E . 
KA 6 HOH 43  743  160  HOH HOH E . 
KA 6 HOH 44  744  171  HOH HOH E . 
KA 6 HOH 45  745  184  HOH HOH E . 
KA 6 HOH 46  746  206  HOH HOH E . 
KA 6 HOH 47  747  209  HOH HOH E . 
KA 6 HOH 48  748  213  HOH HOH E . 
KA 6 HOH 49  749  215  HOH HOH E . 
KA 6 HOH 50  750  216  HOH HOH E . 
KA 6 HOH 51  751  220  HOH HOH E . 
KA 6 HOH 52  752  221  HOH HOH E . 
KA 6 HOH 53  753  224  HOH HOH E . 
KA 6 HOH 54  754  229  HOH HOH E . 
KA 6 HOH 55  755  232  HOH HOH E . 
KA 6 HOH 56  756  238  HOH HOH E . 
KA 6 HOH 57  757  241  HOH HOH E . 
KA 6 HOH 58  758  242  HOH HOH E . 
KA 6 HOH 59  759  248  HOH HOH E . 
KA 6 HOH 60  760  250  HOH HOH E . 
KA 6 HOH 61  761  257  HOH HOH E . 
KA 6 HOH 62  762  258  HOH HOH E . 
KA 6 HOH 63  763  263  HOH HOH E . 
KA 6 HOH 64  764  267  HOH HOH E . 
KA 6 HOH 65  765  269  HOH HOH E . 
KA 6 HOH 66  766  272  HOH HOH E . 
KA 6 HOH 67  767  276  HOH HOH E . 
KA 6 HOH 68  768  277  HOH HOH E . 
KA 6 HOH 69  769  278  HOH HOH E . 
KA 6 HOH 70  770  282  HOH HOH E . 
KA 6 HOH 71  771  285  HOH HOH E . 
KA 6 HOH 72  772  286  HOH HOH E . 
KA 6 HOH 73  773  287  HOH HOH E . 
KA 6 HOH 74  774  289  HOH HOH E . 
KA 6 HOH 75  775  290  HOH HOH E . 
KA 6 HOH 76  776  294  HOH HOH E . 
KA 6 HOH 77  777  296  HOH HOH E . 
KA 6 HOH 78  778  299  HOH HOH E . 
KA 6 HOH 79  779  303  HOH HOH E . 
KA 6 HOH 80  780  305  HOH HOH E . 
KA 6 HOH 81  781  306  HOH HOH E . 
KA 6 HOH 82  782  308  HOH HOH E . 
KA 6 HOH 83  783  310  HOH HOH E . 
KA 6 HOH 84  784  312  HOH HOH E . 
KA 6 HOH 85  785  313  HOH HOH E . 
KA 6 HOH 86  786  316  HOH HOH E . 
KA 6 HOH 87  787  318  HOH HOH E . 
KA 6 HOH 88  788  322  HOH HOH E . 
KA 6 HOH 89  789  327  HOH HOH E . 
KA 6 HOH 90  790  333  HOH HOH E . 
KA 6 HOH 91  791  340  HOH HOH E . 
KA 6 HOH 92  792  345  HOH HOH E . 
KA 6 HOH 93  793  346  HOH HOH E . 
KA 6 HOH 94  794  352  HOH HOH E . 
KA 6 HOH 95  795  353  HOH HOH E . 
KA 6 HOH 96  796  358  HOH HOH E . 
KA 6 HOH 97  797  363  HOH HOH E . 
KA 6 HOH 98  798  364  HOH HOH E . 
KA 6 HOH 99  799  367  HOH HOH E . 
KA 6 HOH 100 800  368  HOH HOH E . 
KA 6 HOH 101 801  370  HOH HOH E . 
KA 6 HOH 102 802  382  HOH HOH E . 
KA 6 HOH 103 803  386  HOH HOH E . 
KA 6 HOH 104 804  391  HOH HOH E . 
KA 6 HOH 105 805  404  HOH HOH E . 
KA 6 HOH 106 806  405  HOH HOH E . 
KA 6 HOH 107 807  407  HOH HOH E . 
KA 6 HOH 108 808  408  HOH HOH E . 
KA 6 HOH 109 809  410  HOH HOH E . 
KA 6 HOH 110 810  415  HOH HOH E . 
KA 6 HOH 111 811  416  HOH HOH E . 
KA 6 HOH 112 812  420  HOH HOH E . 
KA 6 HOH 113 813  421  HOH HOH E . 
KA 6 HOH 114 814  423  HOH HOH E . 
KA 6 HOH 115 815  427  HOH HOH E . 
KA 6 HOH 116 816  430  HOH HOH E . 
KA 6 HOH 117 817  431  HOH HOH E . 
KA 6 HOH 118 818  436  HOH HOH E . 
KA 6 HOH 119 819  438  HOH HOH E . 
KA 6 HOH 120 820  440  HOH HOH E . 
KA 6 HOH 121 821  442  HOH HOH E . 
KA 6 HOH 122 822  452  HOH HOH E . 
KA 6 HOH 123 823  456  HOH HOH E . 
KA 6 HOH 124 824  459  HOH HOH E . 
KA 6 HOH 125 825  473  HOH HOH E . 
KA 6 HOH 126 826  475  HOH HOH E . 
KA 6 HOH 127 827  480  HOH HOH E . 
KA 6 HOH 128 828  482  HOH HOH E . 
KA 6 HOH 129 829  491  HOH HOH E . 
KA 6 HOH 130 830  492  HOH HOH E . 
KA 6 HOH 131 831  502  HOH HOH E . 
KA 6 HOH 132 832  505  HOH HOH E . 
KA 6 HOH 133 833  508  HOH HOH E . 
KA 6 HOH 134 834  510  HOH HOH E . 
KA 6 HOH 135 835  516  HOH HOH E . 
KA 6 HOH 136 836  519  HOH HOH E . 
KA 6 HOH 137 837  520  HOH HOH E . 
KA 6 HOH 138 838  522  HOH HOH E . 
KA 6 HOH 139 839  523  HOH HOH E . 
KA 6 HOH 140 840  542  HOH HOH E . 
KA 6 HOH 141 841  546  HOH HOH E . 
KA 6 HOH 142 842  550  HOH HOH E . 
KA 6 HOH 143 843  557  HOH HOH E . 
KA 6 HOH 144 844  570  HOH HOH E . 
KA 6 HOH 145 845  571  HOH HOH E . 
KA 6 HOH 146 846  577  HOH HOH E . 
KA 6 HOH 147 847  585  HOH HOH E . 
KA 6 HOH 148 848  586  HOH HOH E . 
KA 6 HOH 149 849  595  HOH HOH E . 
KA 6 HOH 150 850  601  HOH HOH E . 
KA 6 HOH 151 851  612  HOH HOH E . 
KA 6 HOH 152 852  614  HOH HOH E . 
KA 6 HOH 153 853  616  HOH HOH E . 
KA 6 HOH 154 854  621  HOH HOH E . 
KA 6 HOH 155 855  631  HOH HOH E . 
KA 6 HOH 156 856  638  HOH HOH E . 
KA 6 HOH 157 857  644  HOH HOH E . 
KA 6 HOH 158 858  648  HOH HOH E . 
KA 6 HOH 159 859  650  HOH HOH E . 
KA 6 HOH 160 860  651  HOH HOH E . 
KA 6 HOH 161 861  655  HOH HOH E . 
KA 6 HOH 162 862  659  HOH HOH E . 
KA 6 HOH 163 863  670  HOH HOH E . 
KA 6 HOH 164 864  673  HOH HOH E . 
KA 6 HOH 165 865  681  HOH HOH E . 
KA 6 HOH 166 866  691  HOH HOH E . 
KA 6 HOH 167 867  693  HOH HOH E . 
KA 6 HOH 168 868  702  HOH HOH E . 
KA 6 HOH 169 869  707  HOH HOH E . 
KA 6 HOH 170 870  708  HOH HOH E . 
KA 6 HOH 171 871  711  HOH HOH E . 
KA 6 HOH 172 872  724  HOH HOH E . 
KA 6 HOH 173 873  728  HOH HOH E . 
KA 6 HOH 174 874  729  HOH HOH E . 
KA 6 HOH 175 875  734  HOH HOH E . 
KA 6 HOH 176 876  740  HOH HOH E . 
KA 6 HOH 177 877  750  HOH HOH E . 
KA 6 HOH 178 878  754  HOH HOH E . 
KA 6 HOH 179 879  761  HOH HOH E . 
KA 6 HOH 180 880  762  HOH HOH E . 
KA 6 HOH 181 881  764  HOH HOH E . 
KA 6 HOH 182 882  769  HOH HOH E . 
KA 6 HOH 183 883  772  HOH HOH E . 
KA 6 HOH 184 884  797  HOH HOH E . 
KA 6 HOH 185 885  809  HOH HOH E . 
KA 6 HOH 186 886  832  HOH HOH E . 
KA 6 HOH 187 887  833  HOH HOH E . 
KA 6 HOH 188 888  840  HOH HOH E . 
KA 6 HOH 189 889  845  HOH HOH E . 
KA 6 HOH 190 890  846  HOH HOH E . 
KA 6 HOH 191 891  848  HOH HOH E . 
KA 6 HOH 192 892  849  HOH HOH E . 
KA 6 HOH 193 893  858  HOH HOH E . 
KA 6 HOH 194 894  862  HOH HOH E . 
KA 6 HOH 195 895  866  HOH HOH E . 
KA 6 HOH 196 896  877  HOH HOH E . 
KA 6 HOH 197 897  884  HOH HOH E . 
KA 6 HOH 198 898  887  HOH HOH E . 
KA 6 HOH 199 899  897  HOH HOH E . 
KA 6 HOH 200 900  898  HOH HOH E . 
KA 6 HOH 201 901  911  HOH HOH E . 
KA 6 HOH 202 902  912  HOH HOH E . 
KA 6 HOH 203 903  932  HOH HOH E . 
KA 6 HOH 204 904  943  HOH HOH E . 
KA 6 HOH 205 905  946  HOH HOH E . 
KA 6 HOH 206 906  949  HOH HOH E . 
KA 6 HOH 207 907  951  HOH HOH E . 
KA 6 HOH 208 908  953  HOH HOH E . 
KA 6 HOH 209 909  976  HOH HOH E . 
KA 6 HOH 210 910  978  HOH HOH E . 
KA 6 HOH 211 911  979  HOH HOH E . 
KA 6 HOH 212 912  992  HOH HOH E . 
KA 6 HOH 213 913  1005 HOH HOH E . 
KA 6 HOH 214 914  1021 HOH HOH E . 
KA 6 HOH 215 915  1022 HOH HOH E . 
KA 6 HOH 216 916  1029 HOH HOH E . 
KA 6 HOH 217 917  1032 HOH HOH E . 
KA 6 HOH 218 918  1044 HOH HOH E . 
KA 6 HOH 219 919  1066 HOH HOH E . 
KA 6 HOH 220 920  1078 HOH HOH E . 
KA 6 HOH 221 921  1081 HOH HOH E . 
KA 6 HOH 222 922  1085 HOH HOH E . 
KA 6 HOH 223 923  1097 HOH HOH E . 
KA 6 HOH 224 924  1100 HOH HOH E . 
KA 6 HOH 225 925  1129 HOH HOH E . 
KA 6 HOH 226 926  1130 HOH HOH E . 
KA 6 HOH 227 927  1146 HOH HOH E . 
KA 6 HOH 228 928  1148 HOH HOH E . 
KA 6 HOH 229 929  1153 HOH HOH E . 
KA 6 HOH 230 930  1160 HOH HOH E . 
KA 6 HOH 231 931  1170 HOH HOH E . 
KA 6 HOH 232 932  1174 HOH HOH E . 
KA 6 HOH 233 933  1178 HOH HOH E . 
KA 6 HOH 234 934  1204 HOH HOH E . 
KA 6 HOH 235 935  1214 HOH HOH E . 
KA 6 HOH 236 936  1216 HOH HOH E . 
KA 6 HOH 237 937  1218 HOH HOH E . 
KA 6 HOH 238 938  1222 HOH HOH E . 
KA 6 HOH 239 939  1227 HOH HOH E . 
KA 6 HOH 240 940  1232 HOH HOH E . 
KA 6 HOH 241 941  1250 HOH HOH E . 
KA 6 HOH 242 942  1251 HOH HOH E . 
KA 6 HOH 243 943  1255 HOH HOH E . 
KA 6 HOH 244 944  1259 HOH HOH E . 
KA 6 HOH 245 945  1260 HOH HOH E . 
KA 6 HOH 246 946  1277 HOH HOH E . 
KA 6 HOH 247 947  1284 HOH HOH E . 
KA 6 HOH 248 948  1290 HOH HOH E . 
KA 6 HOH 249 949  1292 HOH HOH E . 
KA 6 HOH 250 950  1294 HOH HOH E . 
KA 6 HOH 251 951  1296 HOH HOH E . 
KA 6 HOH 252 952  1304 HOH HOH E . 
KA 6 HOH 253 953  1306 HOH HOH E . 
KA 6 HOH 254 954  1307 HOH HOH E . 
KA 6 HOH 255 955  1308 HOH HOH E . 
KA 6 HOH 256 956  1317 HOH HOH E . 
KA 6 HOH 257 957  1319 HOH HOH E . 
KA 6 HOH 258 958  1321 HOH HOH E . 
KA 6 HOH 259 959  1322 HOH HOH E . 
KA 6 HOH 260 960  1336 HOH HOH E . 
KA 6 HOH 261 961  1339 HOH HOH E . 
KA 6 HOH 262 962  1349 HOH HOH E . 
KA 6 HOH 263 963  1353 HOH HOH E . 
KA 6 HOH 264 964  1355 HOH HOH E . 
KA 6 HOH 265 965  1364 HOH HOH E . 
KA 6 HOH 266 966  1369 HOH HOH E . 
KA 6 HOH 267 967  1372 HOH HOH E . 
KA 6 HOH 268 968  1373 HOH HOH E . 
KA 6 HOH 269 969  1375 HOH HOH E . 
KA 6 HOH 270 970  1377 HOH HOH E . 
KA 6 HOH 271 971  1380 HOH HOH E . 
KA 6 HOH 272 972  1382 HOH HOH E . 
KA 6 HOH 273 973  1388 HOH HOH E . 
KA 6 HOH 274 974  1391 HOH HOH E . 
KA 6 HOH 275 975  1394 HOH HOH E . 
KA 6 HOH 276 976  1396 HOH HOH E . 
KA 6 HOH 277 977  1400 HOH HOH E . 
KA 6 HOH 278 978  1407 HOH HOH E . 
KA 6 HOH 279 979  1411 HOH HOH E . 
KA 6 HOH 280 980  1414 HOH HOH E . 
KA 6 HOH 281 981  1424 HOH HOH E . 
KA 6 HOH 282 982  1429 HOH HOH E . 
KA 6 HOH 283 983  1435 HOH HOH E . 
KA 6 HOH 284 984  1436 HOH HOH E . 
KA 6 HOH 285 985  1437 HOH HOH E . 
KA 6 HOH 286 986  1441 HOH HOH E . 
KA 6 HOH 287 987  1451 HOH HOH E . 
KA 6 HOH 288 988  1454 HOH HOH E . 
KA 6 HOH 289 989  1461 HOH HOH E . 
KA 6 HOH 290 990  1469 HOH HOH E . 
KA 6 HOH 291 991  1470 HOH HOH E . 
KA 6 HOH 292 992  1471 HOH HOH E . 
KA 6 HOH 293 993  1474 HOH HOH E . 
KA 6 HOH 294 994  1484 HOH HOH E . 
KA 6 HOH 295 995  1491 HOH HOH E . 
KA 6 HOH 296 996  1506 HOH HOH E . 
KA 6 HOH 297 997  1507 HOH HOH E . 
KA 6 HOH 298 998  1510 HOH HOH E . 
KA 6 HOH 299 999  1517 HOH HOH E . 
KA 6 HOH 300 1000 1525 HOH HOH E . 
KA 6 HOH 301 1001 1530 HOH HOH E . 
KA 6 HOH 302 1002 1531 HOH HOH E . 
KA 6 HOH 303 1003 1535 HOH HOH E . 
KA 6 HOH 304 1004 1542 HOH HOH E . 
KA 6 HOH 305 1005 1544 HOH HOH E . 
KA 6 HOH 306 1006 1546 HOH HOH E . 
KA 6 HOH 307 1007 1556 HOH HOH E . 
KA 6 HOH 308 1008 1557 HOH HOH E . 
KA 6 HOH 309 1009 1558 HOH HOH E . 
KA 6 HOH 310 1010 1569 HOH HOH E . 
KA 6 HOH 311 1011 1570 HOH HOH E . 
KA 6 HOH 312 1012 1575 HOH HOH E . 
KA 6 HOH 313 1013 1576 HOH HOH E . 
KA 6 HOH 314 1014 1577 HOH HOH E . 
LA 6 HOH 1   101  11   HOH HOH F . 
LA 6 HOH 2   102  15   HOH HOH F . 
LA 6 HOH 3   103  22   HOH HOH F . 
LA 6 HOH 4   104  125  HOH HOH F . 
LA 6 HOH 5   105  172  HOH HOH F . 
LA 6 HOH 6   106  291  HOH HOH F . 
LA 6 HOH 7   107  389  HOH HOH F . 
LA 6 HOH 8   108  412  HOH HOH F . 
LA 6 HOH 9   109  422  HOH HOH F . 
LA 6 HOH 10  110  489  HOH HOH F . 
LA 6 HOH 11  111  572  HOH HOH F . 
LA 6 HOH 12  112  605  HOH HOH F . 
LA 6 HOH 13  113  630  HOH HOH F . 
LA 6 HOH 14  114  632  HOH HOH F . 
LA 6 HOH 15  115  639  HOH HOH F . 
LA 6 HOH 16  116  652  HOH HOH F . 
LA 6 HOH 17  117  654  HOH HOH F . 
LA 6 HOH 18  118  662  HOH HOH F . 
LA 6 HOH 19  119  665  HOH HOH F . 
LA 6 HOH 20  120  795  HOH HOH F . 
LA 6 HOH 21  121  802  HOH HOH F . 
LA 6 HOH 22  122  817  HOH HOH F . 
LA 6 HOH 23  123  838  HOH HOH F . 
LA 6 HOH 24  124  886  HOH HOH F . 
LA 6 HOH 25  125  900  HOH HOH F . 
LA 6 HOH 26  126  952  HOH HOH F . 
LA 6 HOH 27  127  959  HOH HOH F . 
LA 6 HOH 28  128  971  HOH HOH F . 
LA 6 HOH 29  129  1019 HOH HOH F . 
LA 6 HOH 30  130  1023 HOH HOH F . 
LA 6 HOH 31  131  1059 HOH HOH F . 
LA 6 HOH 32  132  1147 HOH HOH F . 
LA 6 HOH 33  133  1167 HOH HOH F . 
LA 6 HOH 34  134  1230 HOH HOH F . 
LA 6 HOH 35  135  1240 HOH HOH F . 
LA 6 HOH 36  136  1300 HOH HOH F . 
LA 6 HOH 37  137  1332 HOH HOH F . 
LA 6 HOH 38  138  1333 HOH HOH F . 
LA 6 HOH 39  139  1348 HOH HOH F . 
LA 6 HOH 40  140  1405 HOH HOH F . 
LA 6 HOH 41  141  1447 HOH HOH F . 
LA 6 HOH 42  142  1472 HOH HOH F . 
LA 6 HOH 43  143  1512 HOH HOH F . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 52140 ? 
1 MORE         -685  ? 
1 'SSA (A^2)'  57100 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   NE2 ? A  HIS 83  ? A HIS 107 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NA  ? I  HEC .   ? A HEC 603 ? 1_555 87.4  ? 
2   NE2 ? A  HIS 83  ? A HIS 107 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NB  ? I  HEC .   ? A HEC 603 ? 1_555 86.8  ? 
3   NA  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NB  ? I  HEC .   ? A HEC 603 ? 1_555 90.1  ? 
4   NE2 ? A  HIS 83  ? A HIS 107 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NC  ? I  HEC .   ? A HEC 603 ? 1_555 92.0  ? 
5   NA  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NC  ? I  HEC .   ? A HEC 603 ? 1_555 179.0 ? 
6   NB  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NC  ? I  HEC .   ? A HEC 603 ? 1_555 90.5  ? 
7   NE2 ? A  HIS 83  ? A HIS 107 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 ND  ? I  HEC .   ? A HEC 603 ? 1_555 91.6  ? 
8   NA  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 ND  ? I  HEC .   ? A HEC 603 ? 1_555 90.1  ? 
9   NB  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 ND  ? I  HEC .   ? A HEC 603 ? 1_555 178.4 ? 
10  NC  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 ND  ? I  HEC .   ? A HEC 603 ? 1_555 89.2  ? 
11  NE2 ? A  HIS 83  ? A HIS 107 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NE2 ? A  HIS 160 ? A HIS 184 ? 1_555 174.5 ? 
12  NA  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NE2 ? A  HIS 160 ? A HIS 184 ? 1_555 93.0  ? 
13  NB  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NE2 ? A  HIS 160 ? A HIS 184 ? 1_555 87.7  ? 
14  NC  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NE2 ? A  HIS 160 ? A HIS 184 ? 1_555 87.8  ? 
15  ND  ? I  HEC .   ? A HEC 603 ? 1_555 FE ? I  HEC . ? A HEC 603 ? 1_555 NE2 ? A  HIS 160 ? A HIS 184 ? 1_555 93.9  ? 
16  NE2 ? A  HIS 99  ? A HIS 123 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NA  ? H  HEC .   ? A HEC 602 ? 1_555 90.1  ? 
17  NE2 ? A  HIS 99  ? A HIS 123 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NB  ? H  HEC .   ? A HEC 602 ? 1_555 95.5  ? 
18  NA  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NB  ? H  HEC .   ? A HEC 602 ? 1_555 90.5  ? 
19  NE2 ? A  HIS 99  ? A HIS 123 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NC  ? H  HEC .   ? A HEC 602 ? 1_555 90.2  ? 
20  NA  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NC  ? H  HEC .   ? A HEC 602 ? 1_555 179.1 ? 
21  NB  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NC  ? H  HEC .   ? A HEC 602 ? 1_555 88.6  ? 
22  NE2 ? A  HIS 99  ? A HIS 123 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 ND  ? H  HEC .   ? A HEC 602 ? 1_555 84.0  ? 
23  NA  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 ND  ? H  HEC .   ? A HEC 602 ? 1_555 90.4  ? 
24  NB  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 ND  ? H  HEC .   ? A HEC 602 ? 1_555 179.0 ? 
25  NC  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 ND  ? H  HEC .   ? A HEC 602 ? 1_555 90.5  ? 
26  NE2 ? A  HIS 99  ? A HIS 123 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NE2 ? A  HIS 176 ? A HIS 200 ? 1_555 172.5 ? 
27  NA  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NE2 ? A  HIS 176 ? A HIS 200 ? 1_555 95.1  ? 
28  NB  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NE2 ? A  HIS 176 ? A HIS 200 ? 1_555 89.8  ? 
29  NC  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NE2 ? A  HIS 176 ? A HIS 200 ? 1_555 84.7  ? 
30  ND  ? H  HEC .   ? A HEC 602 ? 1_555 FE ? H  HEC . ? A HEC 602 ? 1_555 NE2 ? A  HIS 176 ? A HIS 200 ? 1_555 90.6  ? 
31  NE2 ? A  HIS 149 ? A HIS 173 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NA  ? J  HEC .   ? A HEC 604 ? 1_555 92.7  ? 
32  NE2 ? A  HIS 149 ? A HIS 173 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NB  ? J  HEC .   ? A HEC 604 ? 1_555 87.5  ? 
33  NA  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NB  ? J  HEC .   ? A HEC 604 ? 1_555 89.8  ? 
34  NE2 ? A  HIS 149 ? A HIS 173 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NC  ? J  HEC .   ? A HEC 604 ? 1_555 88.3  ? 
35  NA  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NC  ? J  HEC .   ? A HEC 604 ? 1_555 178.9 ? 
36  NB  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NC  ? J  HEC .   ? A HEC 604 ? 1_555 90.7  ? 
37  NE2 ? A  HIS 149 ? A HIS 173 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 ND  ? J  HEC .   ? A HEC 604 ? 1_555 91.6  ? 
38  NA  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 ND  ? J  HEC .   ? A HEC 604 ? 1_555 90.5  ? 
39  NB  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 ND  ? J  HEC .   ? A HEC 604 ? 1_555 179.0 ? 
40  NC  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 ND  ? J  HEC .   ? A HEC 604 ? 1_555 88.9  ? 
41  NE2 ? A  HIS 149 ? A HIS 173 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NE2 ? A  HIS 246 ? A HIS 270 ? 1_555 170.6 ? 
42  NA  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NE2 ? A  HIS 246 ? A HIS 270 ? 1_555 93.6  ? 
43  NB  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NE2 ? A  HIS 246 ? A HIS 270 ? 1_555 85.5  ? 
44  NC  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NE2 ? A  HIS 246 ? A HIS 270 ? 1_555 85.5  ? 
45  ND  ? J  HEC .   ? A HEC 604 ? 1_555 FE ? J  HEC . ? A HEC 604 ? 1_555 NE2 ? A  HIS 246 ? A HIS 270 ? 1_555 95.4  ? 
46  NE2 ? A  HIS 204 ? A HIS 228 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NA  ? L  HEC .   ? A HEC 606 ? 1_555 86.0  ? 
47  NE2 ? A  HIS 204 ? A HIS 228 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NB  ? L  HEC .   ? A HEC 606 ? 1_555 91.3  ? 
48  NA  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NB  ? L  HEC .   ? A HEC 606 ? 1_555 88.9  ? 
49  NE2 ? A  HIS 204 ? A HIS 228 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NC  ? L  HEC .   ? A HEC 606 ? 1_555 94.7  ? 
50  NA  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NC  ? L  HEC .   ? A HEC 606 ? 1_555 178.8 ? 
51  NB  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NC  ? L  HEC .   ? A HEC 606 ? 1_555 90.1  ? 
52  NE2 ? A  HIS 204 ? A HIS 228 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 ND  ? L  HEC .   ? A HEC 606 ? 1_555 88.6  ? 
53  NA  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 ND  ? L  HEC .   ? A HEC 606 ? 1_555 90.1  ? 
54  NB  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 ND  ? L  HEC .   ? A HEC 606 ? 1_555 179.0 ? 
55  NC  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 ND  ? L  HEC .   ? A HEC 606 ? 1_555 90.9  ? 
56  NE2 ? A  HIS 204 ? A HIS 228 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 287 ? 1_555 178.4 ? 
57  NA  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 287 ? 1_555 93.2  ? 
58  NB  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 287 ? 1_555 87.3  ? 
59  NC  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 287 ? 1_555 86.1  ? 
60  ND  ? L  HEC .   ? A HEC 606 ? 1_555 FE ? L  HEC . ? A HEC 606 ? 1_555 NE2 ? A  HIS 263 ? A HIS 287 ? 1_555 92.9  ? 
61  NE2 ? A  HIS 233 ? A HIS 257 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 NA  ? P  HEC .   ? C HEC 601 ? 1_555 95.0  ? 
62  NE2 ? A  HIS 233 ? A HIS 257 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 NB  ? P  HEC .   ? C HEC 601 ? 1_555 95.3  ? 
63  NA  ? P  HEC .   ? C HEC 601 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 NB  ? P  HEC .   ? C HEC 601 ? 1_555 88.6  ? 
64  NE2 ? A  HIS 233 ? A HIS 257 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 NC  ? P  HEC .   ? C HEC 601 ? 1_555 89.1  ? 
65  NA  ? P  HEC .   ? C HEC 601 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 NC  ? P  HEC .   ? C HEC 601 ? 1_555 174.7 ? 
66  NB  ? P  HEC .   ? C HEC 601 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 NC  ? P  HEC .   ? C HEC 601 ? 1_555 87.7  ? 
67  NE2 ? A  HIS 233 ? A HIS 257 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 ND  ? P  HEC .   ? C HEC 601 ? 1_555 85.8  ? 
68  NA  ? P  HEC .   ? C HEC 601 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 ND  ? P  HEC .   ? C HEC 601 ? 1_555 89.8  ? 
69  NB  ? P  HEC .   ? C HEC 601 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 ND  ? P  HEC .   ? C HEC 601 ? 1_555 178.1 ? 
70  NC  ? P  HEC .   ? C HEC 601 ? 1_555 FE ? P  HEC . ? C HEC 601 ? 1_555 ND  ? P  HEC .   ? C HEC 601 ? 1_555 93.8  ? 
71  NE2 ? A  HIS 243 ? A HIS 267 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NA  ? G  HEC .   ? A HEC 601 ? 1_555 91.6  ? 
72  NE2 ? A  HIS 243 ? A HIS 267 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NB  ? G  HEC .   ? A HEC 601 ? 1_555 85.4  ? 
73  NA  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NB  ? G  HEC .   ? A HEC 601 ? 1_555 91.0  ? 
74  NE2 ? A  HIS 243 ? A HIS 267 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NC  ? G  HEC .   ? A HEC 601 ? 1_555 89.5  ? 
75  NA  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NC  ? G  HEC .   ? A HEC 601 ? 1_555 178.9 ? 
76  NB  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NC  ? G  HEC .   ? A HEC 601 ? 1_555 88.6  ? 
77  NE2 ? A  HIS 243 ? A HIS 267 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 ND  ? G  HEC .   ? A HEC 601 ? 1_555 93.2  ? 
78  NA  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 ND  ? G  HEC .   ? A HEC 601 ? 1_555 89.5  ? 
79  NB  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 ND  ? G  HEC .   ? A HEC 601 ? 1_555 178.5 ? 
80  NC  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 ND  ? G  HEC .   ? A HEC 601 ? 1_555 90.9  ? 
81  NE2 ? A  HIS 243 ? A HIS 267 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NE2 ? A  HIS 323 ? A HIS 347 ? 1_555 173.7 ? 
82  NA  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NE2 ? A  HIS 323 ? A HIS 347 ? 1_555 94.2  ? 
83  NB  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NE2 ? A  HIS 323 ? A HIS 347 ? 1_555 92.0  ? 
84  NC  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NE2 ? A  HIS 323 ? A HIS 347 ? 1_555 84.7  ? 
85  ND  ? G  HEC .   ? A HEC 601 ? 1_555 FE ? G  HEC . ? A HEC 601 ? 1_555 NE2 ? A  HIS 323 ? A HIS 347 ? 1_555 89.4  ? 
86  NE2 ? A  HIS 279 ? A HIS 303 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NA  ? M  HEC .   ? A HEC 607 ? 1_555 89.6  ? 
87  NE2 ? A  HIS 279 ? A HIS 303 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NB  ? M  HEC .   ? A HEC 607 ? 1_555 100.2 ? 
88  NA  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NB  ? M  HEC .   ? A HEC 607 ? 1_555 89.2  ? 
89  NE2 ? A  HIS 279 ? A HIS 303 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NC  ? M  HEC .   ? A HEC 607 ? 1_555 89.8  ? 
90  NA  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NC  ? M  HEC .   ? A HEC 607 ? 1_555 178.6 ? 
91  NB  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NC  ? M  HEC .   ? A HEC 607 ? 1_555 89.6  ? 
92  NE2 ? A  HIS 279 ? A HIS 303 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 ND  ? M  HEC .   ? A HEC 607 ? 1_555 80.8  ? 
93  NA  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 ND  ? M  HEC .   ? A HEC 607 ? 1_555 91.5  ? 
94  NB  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 ND  ? M  HEC .   ? A HEC 607 ? 1_555 178.8 ? 
95  NC  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 ND  ? M  HEC .   ? A HEC 607 ? 1_555 89.7  ? 
96  NE2 ? A  HIS 279 ? A HIS 303 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NE2 ? A  HIS 364 ? A HIS 388 ? 1_555 169.8 ? 
97  NA  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NE2 ? A  HIS 364 ? A HIS 388 ? 1_555 91.0  ? 
98  NB  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NE2 ? A  HIS 364 ? A HIS 388 ? 1_555 90.0  ? 
99  NC  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NE2 ? A  HIS 364 ? A HIS 388 ? 1_555 89.8  ? 
100 ND  ? M  HEC .   ? A HEC 607 ? 1_555 FE ? M  HEC . ? A HEC 607 ? 1_555 NE2 ? A  HIS 364 ? A HIS 388 ? 1_555 89.0  ? 
101 OD1 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? A  ASP 288 ? A ASP 312 ? 1_555 47.7  ? 
102 OD1 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 O   ? GA HOH .   ? A HOH 916 ? 1_555 101.4 ? 
103 OD2 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 O   ? GA HOH .   ? A HOH 916 ? 1_555 79.8  ? 
104 OD1 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? C  ASP 288 ? C ASP 312 ? 1_555 157.5 ? 
105 OD2 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? C  ASP 288 ? C ASP 312 ? 1_555 119.2 ? 
106 O   ? GA HOH .   ? A HOH 916 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? C  ASP 288 ? C ASP 312 ? 1_555 92.4  ? 
107 OD1 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? C  ASP 288 ? C ASP 312 ? 1_555 105.0 ? 
108 OD2 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? C  ASP 288 ? C ASP 312 ? 1_555 82.6  ? 
109 O   ? GA HOH .   ? A HOH 916 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? C  ASP 288 ? C ASP 312 ? 1_555 123.6 ? 
110 OD1 ? C  ASP 288 ? C ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? C  ASP 288 ? C ASP 312 ? 1_555 52.5  ? 
111 OD1 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? E  ASP 288 ? E ASP 312 ? 1_555 111.6 ? 
112 OD2 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? E  ASP 288 ? E ASP 312 ? 1_555 159.2 ? 
113 O   ? GA HOH .   ? A HOH 916 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? E  ASP 288 ? E ASP 312 ? 1_555 107.0 ? 
114 OD1 ? C  ASP 288 ? C ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? E  ASP 288 ? E ASP 312 ? 1_555 80.7  ? 
115 OD2 ? C  ASP 288 ? C ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD2 ? E  ASP 288 ? E ASP 312 ? 1_555 108.0 ? 
116 OD1 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? E  ASP 288 ? E ASP 312 ? 1_555 65.0  ? 
117 OD2 ? A  ASP 288 ? A ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? E  ASP 288 ? E ASP 312 ? 1_555 112.6 ? 
118 O   ? GA HOH .   ? A HOH 916 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? E  ASP 288 ? E ASP 312 ? 1_555 114.7 ? 
119 OD1 ? C  ASP 288 ? C ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? E  ASP 288 ? E ASP 312 ? 1_555 124.8 ? 
120 OD2 ? C  ASP 288 ? C ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? E  ASP 288 ? E ASP 312 ? 1_555 121.6 ? 
121 OD2 ? E  ASP 288 ? E ASP 312 ? 1_555 K  ? O  K   . ? A K   609 ? 1_555 OD1 ? E  ASP 288 ? E ASP 312 ? 1_555 46.6  ? 
122 NE2 ? A  HIS 314 ? A HIS 338 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NA  ? K  HEC .   ? A HEC 605 ? 1_555 85.6  ? 
123 NE2 ? A  HIS 314 ? A HIS 338 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NB  ? K  HEC .   ? A HEC 605 ? 1_555 89.1  ? 
124 NA  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NB  ? K  HEC .   ? A HEC 605 ? 1_555 91.0  ? 
125 NE2 ? A  HIS 314 ? A HIS 338 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NC  ? K  HEC .   ? A HEC 605 ? 1_555 96.5  ? 
126 NA  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NC  ? K  HEC .   ? A HEC 605 ? 1_555 177.8 ? 
127 NB  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NC  ? K  HEC .   ? A HEC 605 ? 1_555 88.8  ? 
128 NE2 ? A  HIS 314 ? A HIS 338 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 ND  ? K  HEC .   ? A HEC 605 ? 1_555 89.0  ? 
129 NA  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 ND  ? K  HEC .   ? A HEC 605 ? 1_555 89.9  ? 
130 NB  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 ND  ? K  HEC .   ? A HEC 605 ? 1_555 177.9 ? 
131 NC  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 ND  ? K  HEC .   ? A HEC 605 ? 1_555 90.4  ? 
132 NE2 ? A  HIS 314 ? A HIS 338 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NE2 ? A  HIS 459 ? A HIS 483 ? 1_555 171.3 ? 
133 NA  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NE2 ? A  HIS 459 ? A HIS 483 ? 1_555 87.1  ? 
134 NB  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NE2 ? A  HIS 459 ? A HIS 483 ? 1_555 86.4  ? 
135 NC  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NE2 ? A  HIS 459 ? A HIS 483 ? 1_555 90.8  ? 
136 ND  ? K  HEC .   ? A HEC 605 ? 1_555 FE ? K  HEC . ? A HEC 605 ? 1_555 NE2 ? A  HIS 459 ? A HIS 483 ? 1_555 95.6  ? 
137 O   ? GA HOH .   ? A HOH 971 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NA  ? N  HEC .   ? A HEC 608 ? 1_555 95.9  ? 
138 O   ? GA HOH .   ? A HOH 971 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NB  ? N  HEC .   ? A HEC 608 ? 1_555 93.7  ? 
139 NA  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NB  ? N  HEC .   ? A HEC 608 ? 1_555 89.2  ? 
140 O   ? GA HOH .   ? A HOH 971 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NC  ? N  HEC .   ? A HEC 608 ? 1_555 80.2  ? 
141 NA  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NC  ? N  HEC .   ? A HEC 608 ? 1_555 174.7 ? 
142 NB  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NC  ? N  HEC .   ? A HEC 608 ? 1_555 87.4  ? 
143 O   ? GA HOH .   ? A HOH 971 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 ND  ? N  HEC .   ? A HEC 608 ? 1_555 84.8  ? 
144 NA  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 ND  ? N  HEC .   ? A HEC 608 ? 1_555 89.6  ? 
145 NB  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 ND  ? N  HEC .   ? A HEC 608 ? 1_555 178.1 ? 
146 NC  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 ND  ? N  HEC .   ? A HEC 608 ? 1_555 93.6  ? 
147 O   ? GA HOH .   ? A HOH 971 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NE2 ? E  HIS 233 ? E HIS 257 ? 1_555 168.4 ? 
148 NA  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NE2 ? E  HIS 233 ? E HIS 257 ? 1_555 94.5  ? 
149 NB  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NE2 ? E  HIS 233 ? E HIS 257 ? 1_555 91.6  ? 
150 NC  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NE2 ? E  HIS 233 ? E HIS 257 ? 1_555 89.7  ? 
151 ND  ? N  HEC .   ? A HEC 608 ? 1_555 FE ? N  HEC . ? A HEC 608 ? 1_555 NE2 ? E  HIS 233 ? E HIS 257 ? 1_555 90.1  ? 
152 NE2 ? C  HIS 83  ? C HIS 107 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NA  ? S  HEC .   ? C HEC 604 ? 1_555 93.0  ? 
153 NE2 ? C  HIS 83  ? C HIS 107 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NB  ? S  HEC .   ? C HEC 604 ? 1_555 87.3  ? 
154 NA  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NB  ? S  HEC .   ? C HEC 604 ? 1_555 91.1  ? 
155 NE2 ? C  HIS 83  ? C HIS 107 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NC  ? S  HEC .   ? C HEC 604 ? 1_555 87.1  ? 
156 NA  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NC  ? S  HEC .   ? C HEC 604 ? 1_555 179.6 ? 
157 NB  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NC  ? S  HEC .   ? C HEC 604 ? 1_555 89.3  ? 
158 NE2 ? C  HIS 83  ? C HIS 107 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 ND  ? S  HEC .   ? C HEC 604 ? 1_555 91.3  ? 
159 NA  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 ND  ? S  HEC .   ? C HEC 604 ? 1_555 89.0  ? 
160 NB  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 ND  ? S  HEC .   ? C HEC 604 ? 1_555 178.6 ? 
161 NC  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 ND  ? S  HEC .   ? C HEC 604 ? 1_555 90.6  ? 
162 NE2 ? C  HIS 83  ? C HIS 107 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NE2 ? C  HIS 160 ? C HIS 184 ? 1_555 171.5 ? 
163 NA  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NE2 ? C  HIS 160 ? C HIS 184 ? 1_555 93.7  ? 
164 NB  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NE2 ? C  HIS 160 ? C HIS 184 ? 1_555 87.3  ? 
165 NC  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NE2 ? C  HIS 160 ? C HIS 184 ? 1_555 86.3  ? 
166 ND  ? S  HEC .   ? C HEC 604 ? 1_555 FE ? S  HEC . ? C HEC 604 ? 1_555 NE2 ? C  HIS 160 ? C HIS 184 ? 1_555 94.1  ? 
167 NE2 ? C  HIS 99  ? C HIS 123 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NA  ? R  HEC .   ? C HEC 603 ? 1_555 90.3  ? 
168 NE2 ? C  HIS 99  ? C HIS 123 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NB  ? R  HEC .   ? C HEC 603 ? 1_555 97.1  ? 
169 NA  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NB  ? R  HEC .   ? C HEC 603 ? 1_555 90.8  ? 
170 NE2 ? C  HIS 99  ? C HIS 123 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NC  ? R  HEC .   ? C HEC 603 ? 1_555 90.0  ? 
171 NA  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NC  ? R  HEC .   ? C HEC 603 ? 1_555 178.9 ? 
172 NB  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NC  ? R  HEC .   ? C HEC 603 ? 1_555 88.1  ? 
173 NE2 ? C  HIS 99  ? C HIS 123 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 ND  ? R  HEC .   ? C HEC 603 ? 1_555 82.7  ? 
174 NA  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 ND  ? R  HEC .   ? C HEC 603 ? 1_555 89.3  ? 
175 NB  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 ND  ? R  HEC .   ? C HEC 603 ? 1_555 179.8 ? 
176 NC  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 ND  ? R  HEC .   ? C HEC 603 ? 1_555 91.9  ? 
177 NE2 ? C  HIS 99  ? C HIS 123 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NE2 ? C  HIS 176 ? C HIS 200 ? 1_555 171.6 ? 
178 NA  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NE2 ? C  HIS 176 ? C HIS 200 ? 1_555 96.8  ? 
179 NB  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NE2 ? C  HIS 176 ? C HIS 200 ? 1_555 87.5  ? 
180 NC  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NE2 ? C  HIS 176 ? C HIS 200 ? 1_555 83.0  ? 
181 ND  ? R  HEC .   ? C HEC 603 ? 1_555 FE ? R  HEC . ? C HEC 603 ? 1_555 NE2 ? C  HIS 176 ? C HIS 200 ? 1_555 92.7  ? 
182 NE2 ? C  HIS 149 ? C HIS 173 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NA  ? T  HEC .   ? C HEC 605 ? 1_555 90.1  ? 
183 NE2 ? C  HIS 149 ? C HIS 173 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NB  ? T  HEC .   ? C HEC 605 ? 1_555 91.5  ? 
184 NA  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NB  ? T  HEC .   ? C HEC 605 ? 1_555 91.3  ? 
185 NE2 ? C  HIS 149 ? C HIS 173 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NC  ? T  HEC .   ? C HEC 605 ? 1_555 90.8  ? 
186 NA  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NC  ? T  HEC .   ? C HEC 605 ? 1_555 179.1 ? 
187 NB  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NC  ? T  HEC .   ? C HEC 605 ? 1_555 88.7  ? 
188 NE2 ? C  HIS 149 ? C HIS 173 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 ND  ? T  HEC .   ? C HEC 605 ? 1_555 87.5  ? 
189 NA  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 ND  ? T  HEC .   ? C HEC 605 ? 1_555 89.5  ? 
190 NB  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 ND  ? T  HEC .   ? C HEC 605 ? 1_555 178.7 ? 
191 NC  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 ND  ? T  HEC .   ? C HEC 605 ? 1_555 90.5  ? 
192 NE2 ? C  HIS 149 ? C HIS 173 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NE2 ? C  HIS 246 ? C HIS 270 ? 1_555 176.0 ? 
193 NA  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NE2 ? C  HIS 246 ? C HIS 270 ? 1_555 93.0  ? 
194 NB  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NE2 ? C  HIS 246 ? C HIS 270 ? 1_555 85.9  ? 
195 NC  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NE2 ? C  HIS 246 ? C HIS 270 ? 1_555 86.1  ? 
196 ND  ? T  HEC .   ? C HEC 605 ? 1_555 FE ? T  HEC . ? C HEC 605 ? 1_555 NE2 ? C  HIS 246 ? C HIS 270 ? 1_555 95.1  ? 
197 NE2 ? C  HIS 204 ? C HIS 228 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NA  ? V  HEC .   ? C HEC 607 ? 1_555 89.2  ? 
198 NE2 ? C  HIS 204 ? C HIS 228 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NB  ? V  HEC .   ? C HEC 607 ? 1_555 91.9  ? 
199 NA  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NB  ? V  HEC .   ? C HEC 607 ? 1_555 90.9  ? 
200 NE2 ? C  HIS 204 ? C HIS 228 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NC  ? V  HEC .   ? C HEC 607 ? 1_555 91.9  ? 
201 NA  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NC  ? V  HEC .   ? C HEC 607 ? 1_555 178.5 ? 
202 NB  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NC  ? V  HEC .   ? C HEC 607 ? 1_555 88.1  ? 
203 NE2 ? C  HIS 204 ? C HIS 228 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 ND  ? V  HEC .   ? C HEC 607 ? 1_555 88.2  ? 
204 NA  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 ND  ? V  HEC .   ? C HEC 607 ? 1_555 89.5  ? 
205 NB  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 ND  ? V  HEC .   ? C HEC 607 ? 1_555 179.7 ? 
206 NC  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 ND  ? V  HEC .   ? C HEC 607 ? 1_555 91.6  ? 
207 NE2 ? C  HIS 204 ? C HIS 228 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NE2 ? C  HIS 263 ? C HIS 287 ? 1_555 175.5 ? 
208 NA  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NE2 ? C  HIS 263 ? C HIS 287 ? 1_555 88.9  ? 
209 NB  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NE2 ? C  HIS 263 ? C HIS 287 ? 1_555 84.0  ? 
210 NC  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NE2 ? C  HIS 263 ? C HIS 287 ? 1_555 89.9  ? 
211 ND  ? V  HEC .   ? C HEC 607 ? 1_555 FE ? V  HEC . ? C HEC 607 ? 1_555 NE2 ? C  HIS 263 ? C HIS 287 ? 1_555 95.9  ? 
212 NE2 ? C  HIS 233 ? C HIS 257 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 NA  ? X  HEC .   ? E HEC 601 ? 1_555 96.2  ? 
213 NE2 ? C  HIS 233 ? C HIS 257 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 NB  ? X  HEC .   ? E HEC 601 ? 1_555 90.4  ? 
214 NA  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 NB  ? X  HEC .   ? E HEC 601 ? 1_555 88.5  ? 
215 NE2 ? C  HIS 233 ? C HIS 257 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 NC  ? X  HEC .   ? E HEC 601 ? 1_555 87.8  ? 
216 NA  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 NC  ? X  HEC .   ? E HEC 601 ? 1_555 174.7 ? 
217 NB  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 NC  ? X  HEC .   ? E HEC 601 ? 1_555 88.0  ? 
218 NE2 ? C  HIS 233 ? C HIS 257 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 ND  ? X  HEC .   ? E HEC 601 ? 1_555 91.4  ? 
219 NA  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 ND  ? X  HEC .   ? E HEC 601 ? 1_555 90.5  ? 
220 NB  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 ND  ? X  HEC .   ? E HEC 601 ? 1_555 178.0 ? 
221 NC  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 ND  ? X  HEC .   ? E HEC 601 ? 1_555 92.9  ? 
222 NE2 ? C  HIS 233 ? C HIS 257 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 O   ? KA HOH .   ? E HOH 948 ? 1_555 165.3 ? 
223 NA  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 O   ? KA HOH .   ? E HOH 948 ? 1_555 97.7  ? 
224 NB  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 O   ? KA HOH .   ? E HOH 948 ? 1_555 94.4  ? 
225 NC  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 O   ? KA HOH .   ? E HOH 948 ? 1_555 78.5  ? 
226 ND  ? X  HEC .   ? E HEC 601 ? 1_555 FE ? X  HEC . ? E HEC 601 ? 1_555 O   ? KA HOH .   ? E HOH 948 ? 1_555 84.0  ? 
227 NE2 ? C  HIS 243 ? C HIS 267 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NA  ? Q  HEC .   ? C HEC 602 ? 1_555 90.7  ? 
228 NE2 ? C  HIS 243 ? C HIS 267 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NB  ? Q  HEC .   ? C HEC 602 ? 1_555 87.7  ? 
229 NA  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NB  ? Q  HEC .   ? C HEC 602 ? 1_555 91.5  ? 
230 NE2 ? C  HIS 243 ? C HIS 267 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NC  ? Q  HEC .   ? C HEC 602 ? 1_555 90.2  ? 
231 NA  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NC  ? Q  HEC .   ? C HEC 602 ? 1_555 178.8 ? 
232 NB  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NC  ? Q  HEC .   ? C HEC 602 ? 1_555 87.8  ? 
233 NE2 ? C  HIS 243 ? C HIS 267 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 ND  ? Q  HEC .   ? C HEC 602 ? 1_555 91.6  ? 
234 NA  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 ND  ? Q  HEC .   ? C HEC 602 ? 1_555 88.6  ? 
235 NB  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 ND  ? Q  HEC .   ? C HEC 602 ? 1_555 179.3 ? 
236 NC  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 ND  ? Q  HEC .   ? C HEC 602 ? 1_555 92.1  ? 
237 NE2 ? C  HIS 243 ? C HIS 267 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NE2 ? C  HIS 323 ? C HIS 347 ? 1_555 171.2 ? 
238 NA  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NE2 ? C  HIS 323 ? C HIS 347 ? 1_555 97.6  ? 
239 NB  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NE2 ? C  HIS 323 ? C HIS 347 ? 1_555 89.2  ? 
240 NC  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NE2 ? C  HIS 323 ? C HIS 347 ? 1_555 81.5  ? 
241 ND  ? Q  HEC .   ? C HEC 602 ? 1_555 FE ? Q  HEC . ? C HEC 602 ? 1_555 NE2 ? C  HIS 323 ? C HIS 347 ? 1_555 91.5  ? 
242 NE2 ? C  HIS 279 ? C HIS 303 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NA  ? W  HEC .   ? C HEC 608 ? 1_555 87.6  ? 
243 NE2 ? C  HIS 279 ? C HIS 303 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NB  ? W  HEC .   ? C HEC 608 ? 1_555 96.7  ? 
244 NA  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NB  ? W  HEC .   ? C HEC 608 ? 1_555 87.5  ? 
245 NE2 ? C  HIS 279 ? C HIS 303 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NC  ? W  HEC .   ? C HEC 608 ? 1_555 92.0  ? 
246 NA  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NC  ? W  HEC .   ? C HEC 608 ? 1_555 179.6 ? 
247 NB  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NC  ? W  HEC .   ? C HEC 608 ? 1_555 92.4  ? 
248 NE2 ? C  HIS 279 ? C HIS 303 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 ND  ? W  HEC .   ? C HEC 608 ? 1_555 84.4  ? 
249 NA  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 ND  ? W  HEC .   ? C HEC 608 ? 1_555 92.1  ? 
250 NB  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 ND  ? W  HEC .   ? C HEC 608 ? 1_555 178.8 ? 
251 NC  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 ND  ? W  HEC .   ? C HEC 608 ? 1_555 88.1  ? 
252 NE2 ? C  HIS 279 ? C HIS 303 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NE2 ? C  HIS 364 ? C HIS 388 ? 1_555 177.9 ? 
253 NA  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NE2 ? C  HIS 364 ? C HIS 388 ? 1_555 92.9  ? 
254 NB  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NE2 ? C  HIS 364 ? C HIS 388 ? 1_555 85.4  ? 
255 NC  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NE2 ? C  HIS 364 ? C HIS 388 ? 1_555 87.4  ? 
256 ND  ? W  HEC .   ? C HEC 608 ? 1_555 FE ? W  HEC . ? C HEC 608 ? 1_555 NE2 ? C  HIS 364 ? C HIS 388 ? 1_555 93.5  ? 
257 NE2 ? C  HIS 314 ? C HIS 338 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NA  ? U  HEC .   ? C HEC 606 ? 1_555 85.7  ? 
258 NE2 ? C  HIS 314 ? C HIS 338 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NB  ? U  HEC .   ? C HEC 606 ? 1_555 86.7  ? 
259 NA  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NB  ? U  HEC .   ? C HEC 606 ? 1_555 91.7  ? 
260 NE2 ? C  HIS 314 ? C HIS 338 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NC  ? U  HEC .   ? C HEC 606 ? 1_555 96.3  ? 
261 NA  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NC  ? U  HEC .   ? C HEC 606 ? 1_555 177.9 ? 
262 NB  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NC  ? U  HEC .   ? C HEC 606 ? 1_555 88.4  ? 
263 NE2 ? C  HIS 314 ? C HIS 338 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 ND  ? U  HEC .   ? C HEC 606 ? 1_555 91.2  ? 
264 NA  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 ND  ? U  HEC .   ? C HEC 606 ? 1_555 89.0  ? 
265 NB  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 ND  ? U  HEC .   ? C HEC 606 ? 1_555 177.8 ? 
266 NC  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 ND  ? U  HEC .   ? C HEC 606 ? 1_555 91.0  ? 
267 NE2 ? C  HIS 314 ? C HIS 338 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NE2 ? C  HIS 459 ? C HIS 483 ? 1_555 171.5 ? 
268 NA  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NE2 ? C  HIS 459 ? C HIS 483 ? 1_555 87.8  ? 
269 NB  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NE2 ? C  HIS 459 ? C HIS 483 ? 1_555 87.9  ? 
270 NC  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NE2 ? C  HIS 459 ? C HIS 483 ? 1_555 90.1  ? 
271 ND  ? U  HEC .   ? C HEC 606 ? 1_555 FE ? U  HEC . ? C HEC 606 ? 1_555 NE2 ? C  HIS 459 ? C HIS 483 ? 1_555 94.2  ? 
272 NE2 ? E  HIS 83  ? E HIS 107 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NA  ? AA HEC .   ? E HEC 604 ? 1_555 89.5  ? 
273 NE2 ? E  HIS 83  ? E HIS 107 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NB  ? AA HEC .   ? E HEC 604 ? 1_555 86.0  ? 
274 NA  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NB  ? AA HEC .   ? E HEC 604 ? 1_555 91.7  ? 
275 NE2 ? E  HIS 83  ? E HIS 107 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NC  ? AA HEC .   ? E HEC 604 ? 1_555 91.5  ? 
276 NA  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NC  ? AA HEC .   ? E HEC 604 ? 1_555 178.8 ? 
277 NB  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NC  ? AA HEC .   ? E HEC 604 ? 1_555 87.8  ? 
278 NE2 ? E  HIS 83  ? E HIS 107 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 ND  ? AA HEC .   ? E HEC 604 ? 1_555 93.0  ? 
279 NA  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 ND  ? AA HEC .   ? E HEC 604 ? 1_555 88.4  ? 
280 NB  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 ND  ? AA HEC .   ? E HEC 604 ? 1_555 179.1 ? 
281 NC  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 ND  ? AA HEC .   ? E HEC 604 ? 1_555 92.1  ? 
282 NE2 ? E  HIS 83  ? E HIS 107 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NE2 ? E  HIS 160 ? E HIS 184 ? 1_555 172.2 ? 
283 NA  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NE2 ? E  HIS 160 ? E HIS 184 ? 1_555 89.8  ? 
284 NB  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NE2 ? E  HIS 160 ? E HIS 184 ? 1_555 86.2  ? 
285 NC  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NE2 ? E  HIS 160 ? E HIS 184 ? 1_555 89.1  ? 
286 ND  ? AA HEC .   ? E HEC 604 ? 1_555 FE ? AA HEC . ? E HEC 604 ? 1_555 NE2 ? E  HIS 160 ? E HIS 184 ? 1_555 94.7  ? 
287 NE2 ? E  HIS 99  ? E HIS 123 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NA  ? Z  HEC .   ? E HEC 603 ? 1_555 92.6  ? 
288 NE2 ? E  HIS 99  ? E HIS 123 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NB  ? Z  HEC .   ? E HEC 603 ? 1_555 96.2  ? 
289 NA  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NB  ? Z  HEC .   ? E HEC 603 ? 1_555 89.4  ? 
290 NE2 ? E  HIS 99  ? E HIS 123 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NC  ? Z  HEC .   ? E HEC 603 ? 1_555 88.3  ? 
291 NA  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NC  ? Z  HEC .   ? E HEC 603 ? 1_555 178.4 ? 
292 NB  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NC  ? Z  HEC .   ? E HEC 603 ? 1_555 89.2  ? 
293 NE2 ? E  HIS 99  ? E HIS 123 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 ND  ? Z  HEC .   ? E HEC 603 ? 1_555 83.5  ? 
294 NA  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 ND  ? Z  HEC .   ? E HEC 603 ? 1_555 90.3  ? 
295 NB  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 ND  ? Z  HEC .   ? E HEC 603 ? 1_555 179.6 ? 
296 NC  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 ND  ? Z  HEC .   ? E HEC 603 ? 1_555 91.1  ? 
297 NE2 ? E  HIS 99  ? E HIS 123 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NE2 ? E  HIS 176 ? E HIS 200 ? 1_555 173.5 ? 
298 NA  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NE2 ? E  HIS 176 ? E HIS 200 ? 1_555 93.6  ? 
299 NB  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NE2 ? E  HIS 176 ? E HIS 200 ? 1_555 85.9  ? 
300 NC  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NE2 ? E  HIS 176 ? E HIS 200 ? 1_555 85.5  ? 
301 ND  ? Z  HEC .   ? E HEC 603 ? 1_555 FE ? Z  HEC . ? E HEC 603 ? 1_555 NE2 ? E  HIS 176 ? E HIS 200 ? 1_555 94.5  ? 
302 NE2 ? E  HIS 149 ? E HIS 173 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NA  ? BA HEC .   ? E HEC 605 ? 1_555 87.5  ? 
303 NE2 ? E  HIS 149 ? E HIS 173 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NB  ? BA HEC .   ? E HEC 605 ? 1_555 88.9  ? 
304 NA  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NB  ? BA HEC .   ? E HEC 605 ? 1_555 90.9  ? 
305 NE2 ? E  HIS 149 ? E HIS 173 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NC  ? BA HEC .   ? E HEC 605 ? 1_555 93.8  ? 
306 NA  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NC  ? BA HEC .   ? E HEC 605 ? 1_555 178.6 ? 
307 NB  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NC  ? BA HEC .   ? E HEC 605 ? 1_555 88.6  ? 
308 NE2 ? E  HIS 149 ? E HIS 173 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 ND  ? BA HEC .   ? E HEC 605 ? 1_555 90.1  ? 
309 NA  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 ND  ? BA HEC .   ? E HEC 605 ? 1_555 89.7  ? 
310 NB  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 ND  ? BA HEC .   ? E HEC 605 ? 1_555 178.8 ? 
311 NC  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 ND  ? BA HEC .   ? E HEC 605 ? 1_555 90.7  ? 
312 NE2 ? E  HIS 149 ? E HIS 173 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NE2 ? E  HIS 246 ? E HIS 270 ? 1_555 171.8 ? 
313 NA  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NE2 ? E  HIS 246 ? E HIS 270 ? 1_555 87.4  ? 
314 NB  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NE2 ? E  HIS 246 ? E HIS 270 ? 1_555 84.7  ? 
315 NC  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NE2 ? E  HIS 246 ? E HIS 270 ? 1_555 91.3  ? 
316 ND  ? BA HEC .   ? E HEC 605 ? 1_555 FE ? BA HEC . ? E HEC 605 ? 1_555 NE2 ? E  HIS 246 ? E HIS 270 ? 1_555 96.3  ? 
317 NE2 ? E  HIS 204 ? E HIS 228 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NA  ? DA HEC .   ? E HEC 607 ? 1_555 90.8  ? 
318 NE2 ? E  HIS 204 ? E HIS 228 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NB  ? DA HEC .   ? E HEC 607 ? 1_555 90.5  ? 
319 NA  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NB  ? DA HEC .   ? E HEC 607 ? 1_555 89.7  ? 
320 NE2 ? E  HIS 204 ? E HIS 228 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NC  ? DA HEC .   ? E HEC 607 ? 1_555 90.3  ? 
321 NA  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NC  ? DA HEC .   ? E HEC 607 ? 1_555 178.5 ? 
322 NB  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NC  ? DA HEC .   ? E HEC 607 ? 1_555 89.3  ? 
323 NE2 ? E  HIS 204 ? E HIS 228 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 ND  ? DA HEC .   ? E HEC 607 ? 1_555 89.1  ? 
324 NA  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 ND  ? DA HEC .   ? E HEC 607 ? 1_555 91.0  ? 
325 NB  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 ND  ? DA HEC .   ? E HEC 607 ? 1_555 179.2 ? 
326 NC  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 ND  ? DA HEC .   ? E HEC 607 ? 1_555 90.0  ? 
327 NE2 ? E  HIS 204 ? E HIS 228 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NE2 ? E  HIS 263 ? E HIS 287 ? 1_555 177.8 ? 
328 NA  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NE2 ? E  HIS 263 ? E HIS 287 ? 1_555 91.3  ? 
329 NB  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NE2 ? E  HIS 263 ? E HIS 287 ? 1_555 89.4  ? 
330 NC  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NE2 ? E  HIS 263 ? E HIS 287 ? 1_555 87.6  ? 
331 ND  ? DA HEC .   ? E HEC 607 ? 1_555 FE ? DA HEC . ? E HEC 607 ? 1_555 NE2 ? E  HIS 263 ? E HIS 287 ? 1_555 91.0  ? 
332 NE2 ? E  HIS 243 ? E HIS 267 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NA  ? Y  HEC .   ? E HEC 602 ? 1_555 92.8  ? 
333 NE2 ? E  HIS 243 ? E HIS 267 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NB  ? Y  HEC .   ? E HEC 602 ? 1_555 89.3  ? 
334 NA  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NB  ? Y  HEC .   ? E HEC 602 ? 1_555 91.9  ? 
335 NE2 ? E  HIS 243 ? E HIS 267 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NC  ? Y  HEC .   ? E HEC 602 ? 1_555 87.6  ? 
336 NA  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NC  ? Y  HEC .   ? E HEC 602 ? 1_555 179.2 ? 
337 NB  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NC  ? Y  HEC .   ? E HEC 602 ? 1_555 88.8  ? 
338 NE2 ? E  HIS 243 ? E HIS 267 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 ND  ? Y  HEC .   ? E HEC 602 ? 1_555 88.8  ? 
339 NA  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 ND  ? Y  HEC .   ? E HEC 602 ? 1_555 88.1  ? 
340 NB  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 ND  ? Y  HEC .   ? E HEC 602 ? 1_555 178.2 ? 
341 NC  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 ND  ? Y  HEC .   ? E HEC 602 ? 1_555 91.2  ? 
342 NE2 ? E  HIS 243 ? E HIS 267 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NE2 ? E  HIS 323 ? E HIS 347 ? 1_555 175.9 ? 
343 NA  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NE2 ? E  HIS 323 ? E HIS 347 ? 1_555 91.3  ? 
344 NB  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NE2 ? E  HIS 323 ? E HIS 347 ? 1_555 91.1  ? 
345 NC  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NE2 ? E  HIS 323 ? E HIS 347 ? 1_555 88.3  ? 
346 ND  ? Y  HEC .   ? E HEC 602 ? 1_555 FE ? Y  HEC . ? E HEC 602 ? 1_555 NE2 ? E  HIS 323 ? E HIS 347 ? 1_555 90.8  ? 
347 NE2 ? E  HIS 279 ? E HIS 303 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NA  ? EA HEC .   ? E HEC 608 ? 1_555 89.0  ? 
348 NE2 ? E  HIS 279 ? E HIS 303 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NB  ? EA HEC .   ? E HEC 608 ? 1_555 96.1  ? 
349 NA  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NB  ? EA HEC .   ? E HEC 608 ? 1_555 89.4  ? 
350 NE2 ? E  HIS 279 ? E HIS 303 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NC  ? EA HEC .   ? E HEC 608 ? 1_555 89.8  ? 
351 NA  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NC  ? EA HEC .   ? E HEC 608 ? 1_555 178.7 ? 
352 NB  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NC  ? EA HEC .   ? E HEC 608 ? 1_555 90.1  ? 
353 NE2 ? E  HIS 279 ? E HIS 303 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 ND  ? EA HEC .   ? E HEC 608 ? 1_555 84.5  ? 
354 NA  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 ND  ? EA HEC .   ? E HEC 608 ? 1_555 90.1  ? 
355 NB  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 ND  ? EA HEC .   ? E HEC 608 ? 1_555 179.3 ? 
356 NC  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 ND  ? EA HEC .   ? E HEC 608 ? 1_555 90.3  ? 
357 NE2 ? E  HIS 279 ? E HIS 303 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NE2 ? E  HIS 364 ? E HIS 388 ? 1_555 175.0 ? 
358 NA  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NE2 ? E  HIS 364 ? E HIS 388 ? 1_555 94.1  ? 
359 NB  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NE2 ? E  HIS 364 ? E HIS 388 ? 1_555 87.9  ? 
360 NC  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NE2 ? E  HIS 364 ? E HIS 388 ? 1_555 87.1  ? 
361 ND  ? EA HEC .   ? E HEC 608 ? 1_555 FE ? EA HEC . ? E HEC 608 ? 1_555 NE2 ? E  HIS 364 ? E HIS 388 ? 1_555 91.6  ? 
362 NE2 ? E  HIS 314 ? E HIS 338 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NA  ? CA HEC .   ? E HEC 606 ? 1_555 87.1  ? 
363 NE2 ? E  HIS 314 ? E HIS 338 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NB  ? CA HEC .   ? E HEC 606 ? 1_555 86.8  ? 
364 NA  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NB  ? CA HEC .   ? E HEC 606 ? 1_555 90.3  ? 
365 NE2 ? E  HIS 314 ? E HIS 338 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NC  ? CA HEC .   ? E HEC 606 ? 1_555 94.9  ? 
366 NA  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NC  ? CA HEC .   ? E HEC 606 ? 1_555 177.9 ? 
367 NB  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NC  ? CA HEC .   ? E HEC 606 ? 1_555 89.5  ? 
368 NE2 ? E  HIS 314 ? E HIS 338 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 ND  ? CA HEC .   ? E HEC 606 ? 1_555 91.1  ? 
369 NA  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 ND  ? CA HEC .   ? E HEC 606 ? 1_555 90.6  ? 
370 NB  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 ND  ? CA HEC .   ? E HEC 606 ? 1_555 177.7 ? 
371 NC  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 ND  ? CA HEC .   ? E HEC 606 ? 1_555 89.7  ? 
372 NE2 ? E  HIS 314 ? E HIS 338 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NE2 ? E  HIS 459 ? E HIS 483 ? 1_555 173.0 ? 
373 NA  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NE2 ? E  HIS 459 ? E HIS 483 ? 1_555 89.5  ? 
374 NB  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NE2 ? E  HIS 459 ? E HIS 483 ? 1_555 87.1  ? 
375 NC  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NE2 ? E  HIS 459 ? E HIS 483 ? 1_555 88.4  ? 
376 ND  ? CA HEC .   ? E HEC 606 ? 1_555 FE ? CA HEC . ? E HEC 606 ? 1_555 NE2 ? E  HIS 459 ? E HIS 483 ? 1_555 95.0  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-12-11 
2 'Structure model' 1 1 2014-01-15 
3 'Structure model' 1 2 2014-02-05 
4 'Structure model' 1 3 2014-04-09 
5 'Structure model' 2 0 2021-03-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'      
2 3 'Structure model' 'Database references'      
3 4 'Structure model' 'Experimental preparation' 
4 5 'Structure model' 'Atomic model'             
5 5 'Structure model' 'Data collection'          
6 5 'Structure model' 'Derived calculations'     
7 5 'Structure model' 'Non-polymer description'  
8 5 'Structure model' 'Structure summary'        
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1  5 'Structure model' atom_site              
2  5 'Structure model' chem_comp              
3  5 'Structure model' entity                 
4  5 'Structure model' pdbx_entity_nonpoly    
5  5 'Structure model' pdbx_nonpoly_scheme    
6  5 'Structure model' pdbx_struct_conn_angle 
7  5 'Structure model' struct_asym            
8  5 'Structure model' struct_conn            
9  5 'Structure model' struct_conn_type       
10 5 'Structure model' struct_site            
11 5 'Structure model' struct_site_gen        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  5 'Structure model' '_atom_site.B_iso_or_equiv'                   
2  5 'Structure model' '_atom_site.Cartn_x'                          
3  5 'Structure model' '_atom_site.Cartn_y'                          
4  5 'Structure model' '_atom_site.Cartn_z'                          
5  5 'Structure model' '_atom_site.auth_atom_id'                     
6  5 'Structure model' '_atom_site.auth_comp_id'                     
7  5 'Structure model' '_atom_site.label_atom_id'                    
8  5 'Structure model' '_atom_site.label_comp_id'                    
9  5 'Structure model' '_atom_site.label_entity_id'                  
10 5 'Structure model' '_atom_site.type_symbol'                      
11 5 'Structure model' '_chem_comp.formula'                          
12 5 'Structure model' '_chem_comp.formula_weight'                   
13 5 'Structure model' '_chem_comp.id'                               
14 5 'Structure model' '_chem_comp.mon_nstd_flag'                    
15 5 'Structure model' '_chem_comp.name'                             
16 5 'Structure model' '_chem_comp.pdbx_synonyms'                    
17 5 'Structure model' '_chem_comp.type'                             
18 5 'Structure model' '_pdbx_nonpoly_scheme.entity_id'              
19 5 'Structure model' '_pdbx_nonpoly_scheme.mon_id'                 
20 5 'Structure model' '_pdbx_nonpoly_scheme.pdb_mon_id'             
21 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
22 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
23 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
24 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
25 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
26 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
27 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
28 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
29 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_comp_id'  
30 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id'   
31 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
32 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_atom_id' 
33 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_comp_id' 
34 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
35 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
36 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
37 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
38 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
39 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
40 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
41 5 'Structure model' '_pdbx_struct_conn_angle.value'               
42 5 'Structure model' '_struct_asym.entity_id'                      
43 5 'Structure model' '_struct_conn.conn_type_id'                   
44 5 'Structure model' '_struct_conn.id'                             
45 5 'Structure model' '_struct_conn.pdbx_dist_value'                
46 5 'Structure model' '_struct_conn.pdbx_leaving_atom_flag'         
47 5 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
48 5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
49 5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
50 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
51 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
52 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
53 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
54 5 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
55 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
56 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
57 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
58 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
59 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
60 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
61 5 'Structure model' '_struct_conn_type.id'                        
62 5 'Structure model' '_struct_site.details'                        
63 5 'Structure model' '_struct_site.pdbx_auth_asym_id'              
64 5 'Structure model' '_struct_site.pdbx_auth_comp_id'              
65 5 'Structure model' '_struct_site.pdbx_auth_seq_id'               
66 5 'Structure model' '_struct_site_gen.auth_comp_id'               
67 5 'Structure model' '_struct_site_gen.label_comp_id'              
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HEIDI  'data collection' .        ? 1 
PHASER phasing           .        ? 2 
REFMAC refinement        5.5.0102 ? 3 
XDS    'data reduction'  .        ? 4 
XSCALE 'data scaling'    .        ? 5 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 VAL A 174 ? ? -132.03 -64.01  
2  1 HIS A 292 ? ? -174.72 83.51   
3  1 ASN A 293 ? ? -91.07  50.27   
4  1 SER A 325 ? ? -105.58 -77.80  
5  1 ASN A 357 ? ? 70.14   -51.04  
6  1 CYS A 387 ? ? -134.35 -64.44  
7  1 ASN A 433 ? ? -157.52 53.95   
8  1 THR A 490 ? ? -113.38 -93.04  
9  1 VAL C 174 ? ? -130.92 -70.32  
10 1 ASP C 180 ? ? -112.26 -162.64 
11 1 LYS C 186 ? ? -135.42 -37.80  
12 1 HIS C 292 ? ? -176.15 81.50   
13 1 SER C 325 ? ? -110.95 -76.16  
14 1 ASN C 357 ? ? 73.40   -48.82  
15 1 CYS C 387 ? ? -123.41 -63.91  
16 1 ASN C 433 ? ? -148.47 58.00   
17 1 ASN C 472 ? ? -102.40 -60.60  
18 1 THR C 490 ? ? -114.43 -94.63  
19 1 THR D 57  ? ? -131.91 -30.46  
20 1 VAL E 174 ? ? -132.13 -69.06  
21 1 ASP E 180 ? ? -106.90 -161.72 
22 1 ASP E 180 ? ? -108.49 -161.72 
23 1 LYS E 186 ? ? -134.82 -35.63  
24 1 HIS E 292 ? ? -170.63 85.16   
25 1 ASN E 293 ? ? -91.63  53.95   
26 1 SER E 325 ? ? -111.24 -74.45  
27 1 ARG E 354 ? ? -126.06 -50.05  
28 1 ASN E 357 ? ? 69.47   -54.10  
29 1 CYS E 387 ? ? -123.60 -64.78  
30 1 ASN E 433 ? ? -152.97 55.15   
31 1 ARG E 434 ? ? -119.29 79.68   
32 1 ASN E 472 ? ? -99.38  -62.18  
33 1 THR E 490 ? ? -111.10 -92.70  
34 1 ASP F 46  ? ? 152.82  20.89   
35 1 THR F 57  ? ? -142.58 -28.53  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLN 529 ? A GLN 505 
2   1 Y 1 A THR 530 ? A THR 506 
3   1 Y 1 A SER 531 ? A SER 507 
4   1 Y 1 A LEU 532 ? A LEU 508 
5   1 Y 1 A LEU 533 ? A LEU 509 
6   1 Y 1 A ASP 534 ? A ASP 510 
7   1 Y 1 A LEU 535 ? A LEU 511 
8   1 Y 1 A LYS 536 ? A LYS 512 
9   1 Y 1 A GLY 537 ? A GLY 513 
10  1 Y 1 A THR 538 ? A THR 514 
11  1 Y 1 A GLY 539 ? A GLY 515 
12  1 Y 1 A GLU 540 ? A GLU 516 
13  1 Y 1 A LYS 541 ? A LYS 517 
14  1 Y 1 A ILE 542 ? A ILE 518 
15  1 Y 1 A SER 543 ? A SER 519 
16  1 Y 1 A LEU 544 ? A LEU 520 
17  1 Y 1 A GLY 545 ? A GLY 521 
18  1 Y 1 A GLY 546 ? A GLY 522 
19  1 Y 1 A LEU 547 ? A LEU 523 
20  1 Y 1 A GLY 548 ? A GLY 524 
21  1 Y 1 A GLY 549 ? A GLY 525 
22  1 Y 1 A GLY 550 ? A GLY 526 
23  1 Y 1 A MET 551 ? A MET 527 
24  1 Y 1 A LEU 552 ? A LEU 528 
25  1 Y 1 A LEU 553 ? A LEU 529 
26  1 Y 1 A ALA 554 ? A ALA 530 
27  1 Y 1 A GLY 555 ? A GLY 531 
28  1 Y 1 A ALA 556 ? A ALA 532 
29  1 Y 1 A LEU 557 ? A LEU 533 
30  1 Y 1 A ALA 558 ? A ALA 534 
31  1 Y 1 A LEU 559 ? A LEU 535 
32  1 Y 1 A ILE 560 ? A ILE 536 
33  1 Y 1 A GLY 561 ? A GLY 537 
34  1 Y 1 A TRP 562 ? A TRP 538 
35  1 Y 1 A ARG 563 ? A ARG 539 
36  1 Y 1 A LYS 564 ? A LYS 540 
37  1 Y 1 A ARG 565 ? A ARG 541 
38  1 Y 1 A LYS 566 ? A LYS 542 
39  1 Y 1 A GLN 567 ? A GLN 543 
40  1 Y 1 A THR 568 ? A THR 544 
41  1 Y 1 A ARG 569 ? A ARG 545 
42  1 Y 1 A ALA 570 ? A ALA 546 
43  1 Y 1 B SER 28  ? B SER 1   
44  1 Y 1 C GLY 527 ? C GLY 503 
45  1 Y 1 C LYS 528 ? C LYS 504 
46  1 Y 1 C GLN 529 ? C GLN 505 
47  1 Y 1 C THR 530 ? C THR 506 
48  1 Y 1 C SER 531 ? C SER 507 
49  1 Y 1 C LEU 532 ? C LEU 508 
50  1 Y 1 C LEU 533 ? C LEU 509 
51  1 Y 1 C ASP 534 ? C ASP 510 
52  1 Y 1 C LEU 535 ? C LEU 511 
53  1 Y 1 C LYS 536 ? C LYS 512 
54  1 Y 1 C GLY 537 ? C GLY 513 
55  1 Y 1 C THR 538 ? C THR 514 
56  1 Y 1 C GLY 539 ? C GLY 515 
57  1 Y 1 C GLU 540 ? C GLU 516 
58  1 Y 1 C LYS 541 ? C LYS 517 
59  1 Y 1 C ILE 542 ? C ILE 518 
60  1 Y 1 C SER 543 ? C SER 519 
61  1 Y 1 C LEU 544 ? C LEU 520 
62  1 Y 1 C GLY 545 ? C GLY 521 
63  1 Y 1 C GLY 546 ? C GLY 522 
64  1 Y 1 C LEU 547 ? C LEU 523 
65  1 Y 1 C GLY 548 ? C GLY 524 
66  1 Y 1 C GLY 549 ? C GLY 525 
67  1 Y 1 C GLY 550 ? C GLY 526 
68  1 Y 1 C MET 551 ? C MET 527 
69  1 Y 1 C LEU 552 ? C LEU 528 
70  1 Y 1 C LEU 553 ? C LEU 529 
71  1 Y 1 C ALA 554 ? C ALA 530 
72  1 Y 1 C GLY 555 ? C GLY 531 
73  1 Y 1 C ALA 556 ? C ALA 532 
74  1 Y 1 C LEU 557 ? C LEU 533 
75  1 Y 1 C ALA 558 ? C ALA 534 
76  1 Y 1 C LEU 559 ? C LEU 535 
77  1 Y 1 C ILE 560 ? C ILE 536 
78  1 Y 1 C GLY 561 ? C GLY 537 
79  1 Y 1 C TRP 562 ? C TRP 538 
80  1 Y 1 C ARG 563 ? C ARG 539 
81  1 Y 1 C LYS 564 ? C LYS 540 
82  1 Y 1 C ARG 565 ? C ARG 541 
83  1 Y 1 C LYS 566 ? C LYS 542 
84  1 Y 1 C GLN 567 ? C GLN 543 
85  1 Y 1 C THR 568 ? C THR 544 
86  1 Y 1 C ARG 569 ? C ARG 545 
87  1 Y 1 C ALA 570 ? C ALA 546 
88  1 Y 1 E LYS 528 ? E LYS 504 
89  1 Y 1 E GLN 529 ? E GLN 505 
90  1 Y 1 E THR 530 ? E THR 506 
91  1 Y 1 E SER 531 ? E SER 507 
92  1 Y 1 E LEU 532 ? E LEU 508 
93  1 Y 1 E LEU 533 ? E LEU 509 
94  1 Y 1 E ASP 534 ? E ASP 510 
95  1 Y 1 E LEU 535 ? E LEU 511 
96  1 Y 1 E LYS 536 ? E LYS 512 
97  1 Y 1 E GLY 537 ? E GLY 513 
98  1 Y 1 E THR 538 ? E THR 514 
99  1 Y 1 E GLY 539 ? E GLY 515 
100 1 Y 1 E GLU 540 ? E GLU 516 
101 1 Y 1 E LYS 541 ? E LYS 517 
102 1 Y 1 E ILE 542 ? E ILE 518 
103 1 Y 1 E SER 543 ? E SER 519 
104 1 Y 1 E LEU 544 ? E LEU 520 
105 1 Y 1 E GLY 545 ? E GLY 521 
106 1 Y 1 E GLY 546 ? E GLY 522 
107 1 Y 1 E LEU 547 ? E LEU 523 
108 1 Y 1 E GLY 548 ? E GLY 524 
109 1 Y 1 E GLY 549 ? E GLY 525 
110 1 Y 1 E GLY 550 ? E GLY 526 
111 1 Y 1 E MET 551 ? E MET 527 
112 1 Y 1 E LEU 552 ? E LEU 528 
113 1 Y 1 E LEU 553 ? E LEU 529 
114 1 Y 1 E ALA 554 ? E ALA 530 
115 1 Y 1 E GLY 555 ? E GLY 531 
116 1 Y 1 E ALA 556 ? E ALA 532 
117 1 Y 1 E LEU 557 ? E LEU 533 
118 1 Y 1 E ALA 558 ? E ALA 534 
119 1 Y 1 E LEU 559 ? E LEU 535 
120 1 Y 1 E ILE 560 ? E ILE 536 
121 1 Y 1 E GLY 561 ? E GLY 537 
122 1 Y 1 E TRP 562 ? E TRP 538 
123 1 Y 1 E ARG 563 ? E ARG 539 
124 1 Y 1 E LYS 564 ? E LYS 540 
125 1 Y 1 E ARG 565 ? E ARG 541 
126 1 Y 1 E LYS 566 ? E LYS 542 
127 1 Y 1 E GLN 567 ? E GLN 543 
128 1 Y 1 E THR 568 ? E THR 544 
129 1 Y 1 E ARG 569 ? E ARG 545 
130 1 Y 1 E ALA 570 ? E ALA 546 
131 1 Y 1 F GLY 84  ? F GLY 57  
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'HEME C'        HEC 
4 'POTASSIUM ION' K   
5 'PHOSPHATE ION' PO4 
6 water           HOH 
# 
