data_4R21
# 
_entry.id   4R21 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4R21         
RCSB  RCSB086799   
WWPDB D_1000086799 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4R1Z . unspecified 
PDB 4R20 . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4R21 
_pdbx_database_status.recvd_initial_deposition_date   2014-08-08 
_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 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Pallan, P.S.' 1 
'Egli, M.'     2 
# 
_citation.id                        primary 
_citation.title                     
;Structural and Kinetic Basis of Steroid 17 alpha, 20-Lyase Activity in Teleost Fish Cytochrome P450 17A1 and Its Absence in Cytochrome P450 17A2.
;
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            290 
_citation.page_first                3248 
_citation.page_last                 3268 
_citation.year                      2015 
_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   25533464 
_citation.pdbx_database_id_DOI      10.1074/jbc.M114.627265 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Pallan, P.S.'     1  
primary 'Nagy, L.D.'       2  
primary 'Lei, L.'          3  
primary 'Gonzalez, E.'     4  
primary 'Kramlinger, V.M.' 5  
primary 'Azumaya, C.M.'    6  
primary 'Wawrzak, Z.'      7  
primary 'Waterman, M.R.'   8  
primary 'Guengerich, F.P.' 9  
primary 'Egli, M.'         10 
# 
_cell.entry_id           4R21 
_cell.length_a           55.940 
_cell.length_b           78.630 
_cell.length_c           95.410 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.03 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_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                         4R21 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_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 'Cytochrome P450 family 17 polypeptide 2' 54146.156 2  ? ? 'UNP residues 26-495' ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'         616.487   2  ? ? ?                     ? 
3 non-polymer syn PROGESTERONE                              314.462   2  ? ? ?                     ? 
4 water       nat water                                     18.015    17 ? ? ?                     ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAKKTSSKGKEGVGSSSVSFPCLPRLPLLGSLLHLRSNLPPHLLFTQLSSQYGPLFGLYAGPHLTLVVSEIGLVREVLLQ
RGREFAGRPKMVTTDLLTQGGKDIAFADYSPLWKNHRRLVHSSFTLFGEGSNKLQTIVQEAADSLCEELQACRGQSSDLS
VVLMRAVTNVICRLVFSSSYQPSDPELQTVIQYNDGIVQTIARGGLVDIFPWLRIFPNKDLKRLKECVSIRDQLLYKKLL
EHKKSLTPGEPRDLLDALLIGQQRGSGGADDITEDHVLMTAAEAFGAGVETTSTTLLWTIAFLLHHPQLQERVQAELDEC
VGVDRPPCLSDRPHLPLLDAVLCEVMRIRPVSPILIPHVAMQDTSLGGHSVPKGTRVLVNMWAIHHDPKHWDQPEQFNPE
RFLEPSGKKKTQSSFLPFGAGPRVCVGESLARIELFLFVSRPLQRFSFSCPSEASLPDLQGRFGVVLQPERYTVTVTPRH
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAKKTSSKGKEGVGSSSVSFPCLPRLPLLGSLLHLRSNLPPHLLFTQLSSQYGPLFGLYAGPHLTLVVSEIGLVREVLLQ
RGREFAGRPKMVTTDLLTQGGKDIAFADYSPLWKNHRRLVHSSFTLFGEGSNKLQTIVQEAADSLCEELQACRGQSSDLS
VVLMRAVTNVICRLVFSSSYQPSDPELQTVIQYNDGIVQTIARGGLVDIFPWLRIFPNKDLKRLKECVSIRDQLLYKKLL
EHKKSLTPGEPRDLLDALLIGQQRGSGGADDITEDHVLMTAAEAFGAGVETTSTTLLWTIAFLLHHPQLQERVQAELDEC
VGVDRPPCLSDRPHLPLLDAVLCEVMRIRPVSPILIPHVAMQDTSLGGHSVPKGTRVLVNMWAIHHDPKHWDQPEQFNPE
RFLEPSGKKKTQSSFLPFGAGPRVCVGESLARIELFLFVSRPLQRFSFSCPSEASLPDLQGRFGVVLQPERYTVTVTPRH
HHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   LYS n 
1 4   LYS n 
1 5   THR n 
1 6   SER n 
1 7   SER n 
1 8   LYS n 
1 9   GLY n 
1 10  LYS n 
1 11  GLU n 
1 12  GLY n 
1 13  VAL n 
1 14  GLY n 
1 15  SER n 
1 16  SER n 
1 17  SER n 
1 18  VAL n 
1 19  SER n 
1 20  PHE n 
1 21  PRO n 
1 22  CYS n 
1 23  LEU n 
1 24  PRO n 
1 25  ARG n 
1 26  LEU n 
1 27  PRO n 
1 28  LEU n 
1 29  LEU n 
1 30  GLY n 
1 31  SER n 
1 32  LEU n 
1 33  LEU n 
1 34  HIS n 
1 35  LEU n 
1 36  ARG n 
1 37  SER n 
1 38  ASN n 
1 39  LEU n 
1 40  PRO n 
1 41  PRO n 
1 42  HIS n 
1 43  LEU n 
1 44  LEU n 
1 45  PHE n 
1 46  THR n 
1 47  GLN n 
1 48  LEU n 
1 49  SER n 
1 50  SER n 
1 51  GLN n 
1 52  TYR n 
1 53  GLY n 
1 54  PRO n 
1 55  LEU n 
1 56  PHE n 
1 57  GLY n 
1 58  LEU n 
1 59  TYR n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  LEU n 
1 65  THR n 
1 66  LEU n 
1 67  VAL n 
1 68  VAL n 
1 69  SER n 
1 70  GLU n 
1 71  ILE n 
1 72  GLY n 
1 73  LEU n 
1 74  VAL n 
1 75  ARG n 
1 76  GLU n 
1 77  VAL n 
1 78  LEU n 
1 79  LEU n 
1 80  GLN n 
1 81  ARG n 
1 82  GLY n 
1 83  ARG n 
1 84  GLU n 
1 85  PHE n 
1 86  ALA n 
1 87  GLY n 
1 88  ARG n 
1 89  PRO n 
1 90  LYS n 
1 91  MET n 
1 92  VAL n 
1 93  THR n 
1 94  THR n 
1 95  ASP n 
1 96  LEU n 
1 97  LEU n 
1 98  THR n 
1 99  GLN n 
1 100 GLY n 
1 101 GLY n 
1 102 LYS n 
1 103 ASP n 
1 104 ILE n 
1 105 ALA n 
1 106 PHE n 
1 107 ALA n 
1 108 ASP n 
1 109 TYR n 
1 110 SER n 
1 111 PRO n 
1 112 LEU n 
1 113 TRP n 
1 114 LYS n 
1 115 ASN n 
1 116 HIS n 
1 117 ARG n 
1 118 ARG n 
1 119 LEU n 
1 120 VAL n 
1 121 HIS n 
1 122 SER n 
1 123 SER n 
1 124 PHE n 
1 125 THR n 
1 126 LEU n 
1 127 PHE n 
1 128 GLY n 
1 129 GLU n 
1 130 GLY n 
1 131 SER n 
1 132 ASN n 
1 133 LYS n 
1 134 LEU n 
1 135 GLN n 
1 136 THR n 
1 137 ILE n 
1 138 VAL n 
1 139 GLN n 
1 140 GLU n 
1 141 ALA n 
1 142 ALA n 
1 143 ASP n 
1 144 SER n 
1 145 LEU n 
1 146 CYS n 
1 147 GLU n 
1 148 GLU n 
1 149 LEU n 
1 150 GLN n 
1 151 ALA n 
1 152 CYS n 
1 153 ARG n 
1 154 GLY n 
1 155 GLN n 
1 156 SER n 
1 157 SER n 
1 158 ASP n 
1 159 LEU n 
1 160 SER n 
1 161 VAL n 
1 162 VAL n 
1 163 LEU n 
1 164 MET n 
1 165 ARG n 
1 166 ALA n 
1 167 VAL n 
1 168 THR n 
1 169 ASN n 
1 170 VAL n 
1 171 ILE n 
1 172 CYS n 
1 173 ARG n 
1 174 LEU n 
1 175 VAL n 
1 176 PHE n 
1 177 SER n 
1 178 SER n 
1 179 SER n 
1 180 TYR n 
1 181 GLN n 
1 182 PRO n 
1 183 SER n 
1 184 ASP n 
1 185 PRO n 
1 186 GLU n 
1 187 LEU n 
1 188 GLN n 
1 189 THR n 
1 190 VAL n 
1 191 ILE n 
1 192 GLN n 
1 193 TYR n 
1 194 ASN n 
1 195 ASP n 
1 196 GLY n 
1 197 ILE n 
1 198 VAL n 
1 199 GLN n 
1 200 THR n 
1 201 ILE n 
1 202 ALA n 
1 203 ARG n 
1 204 GLY n 
1 205 GLY n 
1 206 LEU n 
1 207 VAL n 
1 208 ASP n 
1 209 ILE n 
1 210 PHE n 
1 211 PRO n 
1 212 TRP n 
1 213 LEU n 
1 214 ARG n 
1 215 ILE n 
1 216 PHE n 
1 217 PRO n 
1 218 ASN n 
1 219 LYS n 
1 220 ASP n 
1 221 LEU n 
1 222 LYS n 
1 223 ARG n 
1 224 LEU n 
1 225 LYS n 
1 226 GLU n 
1 227 CYS n 
1 228 VAL n 
1 229 SER n 
1 230 ILE n 
1 231 ARG n 
1 232 ASP n 
1 233 GLN n 
1 234 LEU n 
1 235 LEU n 
1 236 TYR n 
1 237 LYS n 
1 238 LYS n 
1 239 LEU n 
1 240 LEU n 
1 241 GLU n 
1 242 HIS n 
1 243 LYS n 
1 244 LYS n 
1 245 SER n 
1 246 LEU n 
1 247 THR n 
1 248 PRO n 
1 249 GLY n 
1 250 GLU n 
1 251 PRO n 
1 252 ARG n 
1 253 ASP n 
1 254 LEU n 
1 255 LEU n 
1 256 ASP n 
1 257 ALA n 
1 258 LEU n 
1 259 LEU n 
1 260 ILE n 
1 261 GLY n 
1 262 GLN n 
1 263 GLN n 
1 264 ARG n 
1 265 GLY n 
1 266 SER n 
1 267 GLY n 
1 268 GLY n 
1 269 ALA n 
1 270 ASP n 
1 271 ASP n 
1 272 ILE n 
1 273 THR n 
1 274 GLU n 
1 275 ASP n 
1 276 HIS n 
1 277 VAL n 
1 278 LEU n 
1 279 MET n 
1 280 THR n 
1 281 ALA n 
1 282 ALA n 
1 283 GLU n 
1 284 ALA n 
1 285 PHE n 
1 286 GLY n 
1 287 ALA n 
1 288 GLY n 
1 289 VAL n 
1 290 GLU n 
1 291 THR n 
1 292 THR n 
1 293 SER n 
1 294 THR n 
1 295 THR n 
1 296 LEU n 
1 297 LEU n 
1 298 TRP n 
1 299 THR n 
1 300 ILE n 
1 301 ALA n 
1 302 PHE n 
1 303 LEU n 
1 304 LEU n 
1 305 HIS n 
1 306 HIS n 
1 307 PRO n 
1 308 GLN n 
1 309 LEU n 
1 310 GLN n 
1 311 GLU n 
1 312 ARG n 
1 313 VAL n 
1 314 GLN n 
1 315 ALA n 
1 316 GLU n 
1 317 LEU n 
1 318 ASP n 
1 319 GLU n 
1 320 CYS n 
1 321 VAL n 
1 322 GLY n 
1 323 VAL n 
1 324 ASP n 
1 325 ARG n 
1 326 PRO n 
1 327 PRO n 
1 328 CYS n 
1 329 LEU n 
1 330 SER n 
1 331 ASP n 
1 332 ARG n 
1 333 PRO n 
1 334 HIS n 
1 335 LEU n 
1 336 PRO n 
1 337 LEU n 
1 338 LEU n 
1 339 ASP n 
1 340 ALA n 
1 341 VAL n 
1 342 LEU n 
1 343 CYS n 
1 344 GLU n 
1 345 VAL n 
1 346 MET n 
1 347 ARG n 
1 348 ILE n 
1 349 ARG n 
1 350 PRO n 
1 351 VAL n 
1 352 SER n 
1 353 PRO n 
1 354 ILE n 
1 355 LEU n 
1 356 ILE n 
1 357 PRO n 
1 358 HIS n 
1 359 VAL n 
1 360 ALA n 
1 361 MET n 
1 362 GLN n 
1 363 ASP n 
1 364 THR n 
1 365 SER n 
1 366 LEU n 
1 367 GLY n 
1 368 GLY n 
1 369 HIS n 
1 370 SER n 
1 371 VAL n 
1 372 PRO n 
1 373 LYS n 
1 374 GLY n 
1 375 THR n 
1 376 ARG n 
1 377 VAL n 
1 378 LEU n 
1 379 VAL n 
1 380 ASN n 
1 381 MET n 
1 382 TRP n 
1 383 ALA n 
1 384 ILE n 
1 385 HIS n 
1 386 HIS n 
1 387 ASP n 
1 388 PRO n 
1 389 LYS n 
1 390 HIS n 
1 391 TRP n 
1 392 ASP n 
1 393 GLN n 
1 394 PRO n 
1 395 GLU n 
1 396 GLN n 
1 397 PHE n 
1 398 ASN n 
1 399 PRO n 
1 400 GLU n 
1 401 ARG n 
1 402 PHE n 
1 403 LEU n 
1 404 GLU n 
1 405 PRO n 
1 406 SER n 
1 407 GLY n 
1 408 LYS n 
1 409 LYS n 
1 410 LYS n 
1 411 THR n 
1 412 GLN n 
1 413 SER n 
1 414 SER n 
1 415 PHE n 
1 416 LEU n 
1 417 PRO n 
1 418 PHE n 
1 419 GLY n 
1 420 ALA n 
1 421 GLY n 
1 422 PRO n 
1 423 ARG n 
1 424 VAL n 
1 425 CYS n 
1 426 VAL n 
1 427 GLY n 
1 428 GLU n 
1 429 SER n 
1 430 LEU n 
1 431 ALA n 
1 432 ARG n 
1 433 ILE n 
1 434 GLU n 
1 435 LEU n 
1 436 PHE n 
1 437 LEU n 
1 438 PHE n 
1 439 VAL n 
1 440 SER n 
1 441 ARG n 
1 442 PRO n 
1 443 LEU n 
1 444 GLN n 
1 445 ARG n 
1 446 PHE n 
1 447 SER n 
1 448 PHE n 
1 449 SER n 
1 450 CYS n 
1 451 PRO n 
1 452 SER n 
1 453 GLU n 
1 454 ALA n 
1 455 SER n 
1 456 LEU n 
1 457 PRO n 
1 458 ASP n 
1 459 LEU n 
1 460 GLN n 
1 461 GLY n 
1 462 ARG n 
1 463 PHE n 
1 464 GLY n 
1 465 VAL n 
1 466 VAL n 
1 467 LEU n 
1 468 GLN n 
1 469 PRO n 
1 470 GLU n 
1 471 ARG n 
1 472 TYR n 
1 473 THR n 
1 474 VAL n 
1 475 THR n 
1 476 VAL n 
1 477 THR n 
1 478 PRO n 
1 479 ARG n 
1 480 HIS n 
1 481 HIS n 
1 482 HIS n 
1 483 HIS n 
1 484 HIS n 
1 485 HIS n 
1 486 HIS n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                zebrafish 
_entity_src_nat.pdbx_organism_scientific   'Danio rerio' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      7955 
_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                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A7U483_DANRE 
_struct_ref.pdbx_db_accession          A7U483 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EGVGSSSVSFPCLPRLPLLGSLLHLRSNLPPHLLFTQLSSQYGPLFGLYAGPHLTLVVSEIGLVREVLLQRGREFAGRPK
MVTTDLLTQGGKDIAFADYSPLWKNHRRLVHSSFTLFGEGSNKLQTIVQEAADSLCEELQACRGQSSDLSVVLMRAVTNV
ICRLVFSSSYQPSDPELQTVIQYNDGIVQTIARGGLVDIFPWLRIFPNKDLKRLKECVSIRDQLLYKKLLEHKKSLTPGE
PRDLLDALLIGQQRGSGGADDITEDHVLMTAAEAFGAGVETTSTTLLWTIAFLLHHPQLQERVQAELDECVGVDRPPCLS
DRPHLPLLDAVLCEVMRIRPVSPILIPHVAMQDTSLGGHSVPKGTRVLVNMWAIHHDPKHWDQPEQFNPERFLEPSGKKK
TQSSFLPFGAGPRVCVGESLARIELFLFVSRPLQRFSFSCPSEASLPDLQGRFGVVLQPERYTVTVTPRH
;
_struct_ref.pdbx_align_begin           26 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4R21 A 11 ? 480 ? A7U483 26 ? 495 ? 26 495 
2 1 4R21 B 11 ? 480 ? A7U483 26 ? 495 ? 26 495 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4R21 MET A 1   ? UNP A7U483 ? ? 'EXPRESSION TAG' 16  1  
1 4R21 ALA A 2   ? UNP A7U483 ? ? 'EXPRESSION TAG' 17  2  
1 4R21 LYS A 3   ? UNP A7U483 ? ? 'EXPRESSION TAG' 18  3  
1 4R21 LYS A 4   ? UNP A7U483 ? ? 'EXPRESSION TAG' 19  4  
1 4R21 THR A 5   ? UNP A7U483 ? ? 'EXPRESSION TAG' 20  5  
1 4R21 SER A 6   ? UNP A7U483 ? ? 'EXPRESSION TAG' 21  6  
1 4R21 SER A 7   ? UNP A7U483 ? ? 'EXPRESSION TAG' 22  7  
1 4R21 LYS A 8   ? UNP A7U483 ? ? 'EXPRESSION TAG' 23  8  
1 4R21 GLY A 9   ? UNP A7U483 ? ? 'EXPRESSION TAG' 24  9  
1 4R21 LYS A 10  ? UNP A7U483 ? ? 'EXPRESSION TAG' 25  10 
1 4R21 HIS A 481 ? UNP A7U483 ? ? 'EXPRESSION TAG' 496 11 
1 4R21 HIS A 482 ? UNP A7U483 ? ? 'EXPRESSION TAG' 497 12 
1 4R21 HIS A 483 ? UNP A7U483 ? ? 'EXPRESSION TAG' 498 13 
1 4R21 HIS A 484 ? UNP A7U483 ? ? 'EXPRESSION TAG' 499 14 
1 4R21 HIS A 485 ? UNP A7U483 ? ? 'EXPRESSION TAG' 500 15 
1 4R21 HIS A 486 ? UNP A7U483 ? ? 'EXPRESSION TAG' 501 16 
2 4R21 MET B 1   ? UNP A7U483 ? ? 'EXPRESSION TAG' 16  17 
2 4R21 ALA B 2   ? UNP A7U483 ? ? 'EXPRESSION TAG' 17  18 
2 4R21 LYS B 3   ? UNP A7U483 ? ? 'EXPRESSION TAG' 18  19 
2 4R21 LYS B 4   ? UNP A7U483 ? ? 'EXPRESSION TAG' 19  20 
2 4R21 THR B 5   ? UNP A7U483 ? ? 'EXPRESSION TAG' 20  21 
2 4R21 SER B 6   ? UNP A7U483 ? ? 'EXPRESSION TAG' 21  22 
2 4R21 SER B 7   ? UNP A7U483 ? ? 'EXPRESSION TAG' 22  23 
2 4R21 LYS B 8   ? UNP A7U483 ? ? 'EXPRESSION TAG' 23  24 
2 4R21 GLY B 9   ? UNP A7U483 ? ? 'EXPRESSION TAG' 24  25 
2 4R21 LYS B 10  ? UNP A7U483 ? ? 'EXPRESSION TAG' 25  26 
2 4R21 HIS B 481 ? UNP A7U483 ? ? 'EXPRESSION TAG' 496 27 
2 4R21 HIS B 482 ? UNP A7U483 ? ? 'EXPRESSION TAG' 497 28 
2 4R21 HIS B 483 ? UNP A7U483 ? ? 'EXPRESSION TAG' 498 29 
2 4R21 HIS B 484 ? UNP A7U483 ? ? 'EXPRESSION TAG' 499 30 
2 4R21 HIS B 485 ? UNP A7U483 ? ? 'EXPRESSION TAG' 500 31 
2 4R21 HIS B 486 ? UNP A7U483 ? ? 'EXPRESSION TAG' 501 32 
# 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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 
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 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
STR non-polymer         . PROGESTERONE                      ?    'C21 H30 O2'       314.462 
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          4R21 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.94 
_exptl_crystal.density_percent_sol   36.48 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
;50 mM sodium HEPES buffer, 25 mM MgCl2 and 15% (v/v) polyethylene glycol monomethyl ether 3550, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
;
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   2013-07-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'C(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97872 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 21-ID-F' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-F 
_diffrn_source.pdbx_wavelength             0.97872 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4R21 
_reflns.observed_criterion_sigma_I   5.000 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             17.080 
_reflns.d_resolution_high            2.700 
_reflns.number_obs                   22643 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.0 
_reflns.pdbx_Rmerge_I_obs            0.07400 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.4000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.700 
_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_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.73 
_reflns_shell.d_res_low              2.81 
_reflns_shell.percent_possible_all   98.2 
_reflns_shell.Rmerge_I_obs           0.66800 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.200 
_reflns_shell.pdbx_redundancy        4.80 
_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       ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4R21 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     21459 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             17.08 
_refine.ls_d_res_high                            2.70 
_refine.ls_percent_reflns_obs                    98.8 
_refine.ls_R_factor_obs                          0.209 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.205 
_refine.ls_R_factor_R_free                       0.283 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  1159 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.943 
_refine.correlation_coeff_Fo_to_Fc_free          0.883 
_refine.B_iso_mean                               60.10 
_refine.aniso_B[1][1]                            2.10000 
_refine.aniso_B[2][2]                            -1.98000 
_refine.aniso_B[3][3]                            -0.08000 
_refine.aniso_B[1][2]                            -0.00000 
_refine.aniso_B[1][3]                            -0.57000 
_refine.aniso_B[2][3]                            -0.00000 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_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                      ? 
_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                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.437 
_refine.overall_SU_ML                            0.376 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             41.570 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6605 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         130 
_refine_hist.number_atoms_solvent             17 
_refine_hist.number_atoms_total               6752 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        17.08 
# 
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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.011  0.019  ? 6887  'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.020  ? 6638  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.615  2.002  ? 9397  'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.869  3.003  ? 15268 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.906  5.000  ? 838   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       34.771 23.446 ? 296   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       20.057 15.000 ? 1132  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       22.695 15.000 ? 54    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.096  0.200  ? 1066  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.021  ? 7690  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.003  0.020  ? 1556  '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                  1.901  3.037  ? 3373  'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.901  3.037  ? 3372  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.287  4.548  ? 4204  'X-RAY DIFFRACTION' ? 
r_mcangle_other              3.287  4.548  ? 4205  'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.941  3.161  ? 3514  'X-RAY DIFFRACTION' ? 
r_scbond_other               1.940  3.161  ? 3515  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              3.224  4.653  ? 5194  'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       5.889  24.252 ? 8030  'X-RAY DIFFRACTION' ? 
r_long_range_B_other         5.889  24.254 ? 8031  '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_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.70 
_refine_ls_shell.d_res_low                        2.77 
_refine_ls_shell.number_reflns_R_work             1556 
_refine_ls_shell.R_factor_R_work                  0.2850 
_refine_ls_shell.percent_reflns_obs               97.45 
_refine_ls_shell.R_factor_R_free                  0.3700 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             85 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  4R21 
_struct.title                     'Zebra fish cytochrome P450 17A2 with Progesterone' 
_struct.pdbx_descriptor           'Cytochrome P450 family 17 polypeptide 2' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4R21 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
'Cytochrome P450 17A2, progesterone, P450 17A2, 17 (alpha)-hydroxylation, steroid biosynthesis, enzyme kinetics, 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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_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 40  ? SER A 50  ? PRO A 55  SER A 65  1 ? 11 
HELX_P HELX_P2  2  GLU A 70  ? LEU A 79  ? GLU A 85  LEU A 94  1 ? 10 
HELX_P HELX_P3  3  MET A 91  ? THR A 98  ? MET A 106 THR A 113 1 ? 8  
HELX_P HELX_P4  4  SER A 110 ? GLU A 129 ? SER A 125 GLU A 144 1 ? 20 
HELX_P HELX_P5  5  ASN A 132 ? ARG A 153 ? ASN A 147 ARG A 168 1 ? 22 
HELX_P HELX_P6  6  SER A 160 ? SER A 177 ? SER A 175 SER A 192 1 ? 18 
HELX_P HELX_P7  7  ASP A 184 ? GLY A 204 ? ASP A 199 GLY A 219 1 ? 21 
HELX_P HELX_P8  8  ASP A 220 ? SER A 245 ? ASP A 235 SER A 260 1 ? 26 
HELX_P HELX_P9  9  ASP A 253 ? ARG A 264 ? ASP A 268 ARG A 279 1 ? 12 
HELX_P HELX_P10 10 THR A 273 ? HIS A 306 ? THR A 288 HIS A 321 1 ? 34 
HELX_P HELX_P11 11 HIS A 306 ? VAL A 321 ? HIS A 321 VAL A 336 1 ? 16 
HELX_P HELX_P12 12 CYS A 328 ? HIS A 334 ? CYS A 343 HIS A 349 5 ? 7  
HELX_P HELX_P13 13 LEU A 335 ? ARG A 349 ? LEU A 350 ARG A 364 1 ? 15 
HELX_P HELX_P14 14 ASN A 380 ? ASP A 387 ? ASN A 395 ASP A 402 1 ? 8  
HELX_P HELX_P15 15 ASN A 398 ? LEU A 403 ? ASN A 413 LEU A 418 5 ? 6  
HELX_P HELX_P16 16 ALA A 420 ? VAL A 424 ? ALA A 435 VAL A 439 5 ? 5  
HELX_P HELX_P17 17 GLY A 427 ? ARG A 445 ? GLY A 442 ARG A 460 1 ? 19 
HELX_P HELX_P18 18 PRO B 40  ? TYR B 52  ? PRO B 55  TYR B 67  1 ? 13 
HELX_P HELX_P19 19 GLU B 70  ? LEU B 79  ? GLU B 85  LEU B 94  1 ? 10 
HELX_P HELX_P20 20 MET B 91  ? GLN B 99  ? MET B 106 GLN B 114 1 ? 9  
HELX_P HELX_P21 21 SER B 110 ? LEU B 126 ? SER B 125 LEU B 141 1 ? 17 
HELX_P HELX_P22 22 ASN B 132 ? ALA B 151 ? ASN B 147 ALA B 166 1 ? 20 
HELX_P HELX_P23 23 SER B 160 ? SER B 177 ? SER B 175 SER B 192 1 ? 18 
HELX_P HELX_P24 24 ASP B 184 ? ARG B 203 ? ASP B 199 ARG B 218 1 ? 20 
HELX_P HELX_P25 25 LEU B 221 ? SER B 245 ? LEU B 236 SER B 260 1 ? 25 
HELX_P HELX_P26 26 ASP B 253 ? ARG B 264 ? ASP B 268 ARG B 279 1 ? 12 
HELX_P HELX_P27 27 GLU B 274 ? ALA B 287 ? GLU B 289 ALA B 302 1 ? 14 
HELX_P HELX_P28 28 GLU B 290 ? HIS B 306 ? GLU B 305 HIS B 321 1 ? 17 
HELX_P HELX_P29 29 HIS B 306 ? VAL B 321 ? HIS B 321 VAL B 336 1 ? 16 
HELX_P HELX_P30 30 CYS B 328 ? ARG B 332 ? CYS B 343 ARG B 347 5 ? 5  
HELX_P HELX_P31 31 LEU B 335 ? ARG B 349 ? LEU B 350 ARG B 364 1 ? 15 
HELX_P HELX_P32 32 ASN B 380 ? ASP B 387 ? ASN B 395 ASP B 402 1 ? 8  
HELX_P HELX_P33 33 ASN B 398 ? LEU B 403 ? ASN B 413 LEU B 418 5 ? 6  
HELX_P HELX_P34 34 ALA B 420 ? VAL B 424 ? ALA B 435 VAL B 439 5 ? 5  
HELX_P HELX_P35 35 GLY B 427 ? PHE B 446 ? GLY B 442 PHE B 461 1 ? 20 
# 
_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 
metalc1 metalc ? ? B CYS 425 SG ? ? ? 1_555 E HEM . FE ? ? B CYS 440 B HEM 600 1_555 ? ? ? ? ? ? ? 2.287 ? 
metalc2 metalc ? ? A CYS 425 SG ? ? ? 1_555 C HEM . FE ? ? A CYS 440 A HEM 600 1_555 ? ? ? ? ? ? ? 2.334 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 ARG 153 A . ? ARG 168 A GLY 154 A ? GLY 169 A 1 -1.05 
2 LYS 219 A . ? LYS 234 A ASP 220 A ? ASP 235 A 1 24.93 
3 GLU 250 A . ? GLU 265 A PRO 251 A ? PRO 266 A 1 19.44 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 2 ? 
C ? 2 ? 
D ? 2 ? 
E ? 4 ? 
F ? 3 ? 
G ? 2 ? 
H ? 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 
A 2 3 ? parallel      
A 3 4 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? parallel      
E 3 4 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
G 1 2 ? anti-parallel 
H 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 LEU A 55  ? ALA A 60  ? LEU A 70  ALA A 75  
A 2 HIS A 63  ? VAL A 68  ? HIS A 78  VAL A 83  
A 3 ARG A 376 ? VAL A 379 ? ARG A 391 VAL A 394 
A 4 HIS A 358 ? VAL A 359 ? HIS A 373 VAL A 374 
B 1 THR A 364 ? LEU A 366 ? THR A 379 LEU A 381 
B 2 HIS A 369 ? VAL A 371 ? HIS A 384 VAL A 386 
C 1 PHE A 446 ? SER A 449 ? PHE A 461 SER A 464 
C 2 THR A 475 ? PRO A 478 ? THR A 490 PRO A 493 
D 1 ARG A 462 ? PHE A 463 ? ARG A 477 PHE A 478 
D 2 LEU A 467 ? GLN A 468 ? LEU A 482 GLN A 483 
E 1 LEU B 55  ? ALA B 60  ? LEU B 70  ALA B 75  
E 2 HIS B 63  ? VAL B 68  ? HIS B 78  VAL B 83  
E 3 ARG B 376 ? VAL B 379 ? ARG B 391 VAL B 394 
E 4 HIS B 358 ? VAL B 359 ? HIS B 373 VAL B 374 
F 1 SER B 157 ? ASP B 158 ? SER B 172 ASP B 173 
F 2 THR B 473 ? VAL B 476 ? THR B 488 VAL B 491 
F 3 PHE B 448 ? SER B 449 ? PHE B 463 SER B 464 
G 1 THR B 364 ? LEU B 366 ? THR B 379 LEU B 381 
G 2 HIS B 369 ? VAL B 371 ? HIS B 384 VAL B 386 
H 1 ARG B 462 ? PHE B 463 ? ARG B 477 PHE B 478 
H 2 LEU B 467 ? GLN B 468 ? LEU B 482 GLN B 483 
# 
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 LEU A 58  ? N LEU A 73  O THR A 65  ? O THR A 80  
A 2 3 N LEU A 66  ? N LEU A 81  O LEU A 378 ? O LEU A 393 
A 3 4 O VAL A 377 ? O VAL A 392 N HIS A 358 ? N HIS A 373 
B 1 2 N THR A 364 ? N THR A 379 O VAL A 371 ? O VAL A 386 
C 1 2 N SER A 447 ? N SER A 462 O THR A 477 ? O THR A 492 
D 1 2 N ARG A 462 ? N ARG A 477 O GLN A 468 ? O GLN A 483 
E 1 2 N PHE B 56  ? N PHE B 71  O VAL B 67  ? O VAL B 82  
E 2 3 N LEU B 66  ? N LEU B 81  O ARG B 376 ? O ARG B 391 
E 3 4 O VAL B 377 ? O VAL B 392 N HIS B 358 ? N HIS B 373 
F 1 2 N SER B 157 ? N SER B 172 O VAL B 474 ? O VAL B 489 
F 2 3 O THR B 475 ? O THR B 490 N SER B 449 ? N SER B 464 
G 1 2 N THR B 364 ? N THR B 379 O VAL B 371 ? O VAL B 386 
H 1 2 N ARG B 462 ? N ARG B 477 O GLN B 468 ? O GLN B 483 
# 
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 ? ? ? ? 16 'BINDING SITE FOR RESIDUE HEM A 600' 
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE STR A 601' 
AC3 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE HEM B 600' 
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE STR B 601' 
# 
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 16 ARG A 88  ? ARG A 103 . ? 1_555 ? 
2  AC1 16 TRP A 113 ? TRP A 128 . ? 1_555 ? 
3  AC1 16 ALA A 284 ? ALA A 299 . ? 1_555 ? 
4  AC1 16 ALA A 287 ? ALA A 302 . ? 1_555 ? 
5  AC1 16 GLY A 288 ? GLY A 303 . ? 1_555 ? 
6  AC1 16 THR A 291 ? THR A 306 . ? 1_555 ? 
7  AC1 16 THR A 292 ? THR A 307 . ? 1_555 ? 
8  AC1 16 VAL A 351 ? VAL A 366 . ? 1_555 ? 
9  AC1 16 LEU A 355 ? LEU A 370 . ? 1_555 ? 
10 AC1 16 HIS A 358 ? HIS A 373 . ? 1_555 ? 
11 AC1 16 PRO A 417 ? PRO A 432 . ? 1_555 ? 
12 AC1 16 PHE A 418 ? PHE A 433 . ? 1_555 ? 
13 AC1 16 ARG A 423 ? ARG A 438 . ? 1_555 ? 
14 AC1 16 CYS A 425 ? CYS A 440 . ? 1_555 ? 
15 AC1 16 VAL A 426 ? VAL A 441 . ? 1_555 ? 
16 AC1 16 STR D .   ? STR A 601 . ? 1_555 ? 
17 AC2 5  ILE A 197 ? ILE A 212 . ? 1_555 ? 
18 AC2 5  GLY A 286 ? GLY A 301 . ? 1_555 ? 
19 AC2 5  SER A 352 ? SER A 367 . ? 1_555 ? 
20 AC2 5  ILE A 356 ? ILE A 371 . ? 1_555 ? 
21 AC2 5  HEM C .   ? HEM A 600 . ? 1_555 ? 
22 AC3 15 ARG B 88  ? ARG B 103 . ? 1_555 ? 
23 AC3 15 TRP B 113 ? TRP B 128 . ? 1_555 ? 
24 AC3 15 PHE B 124 ? PHE B 139 . ? 1_555 ? 
25 AC3 15 ALA B 287 ? ALA B 302 . ? 1_555 ? 
26 AC3 15 GLY B 288 ? GLY B 303 . ? 1_555 ? 
27 AC3 15 THR B 292 ? THR B 307 . ? 1_555 ? 
28 AC3 15 HIS B 358 ? HIS B 373 . ? 1_555 ? 
29 AC3 15 PRO B 417 ? PRO B 432 . ? 1_555 ? 
30 AC3 15 PHE B 418 ? PHE B 433 . ? 1_555 ? 
31 AC3 15 ARG B 423 ? ARG B 438 . ? 1_555 ? 
32 AC3 15 VAL B 424 ? VAL B 439 . ? 1_555 ? 
33 AC3 15 CYS B 425 ? CYS B 440 . ? 1_555 ? 
34 AC3 15 VAL B 426 ? VAL B 441 . ? 1_555 ? 
35 AC3 15 ALA B 431 ? ALA B 446 . ? 1_555 ? 
36 AC3 15 STR F .   ? STR B 601 . ? 1_555 ? 
37 AC4 7  ALA B 105 ? ALA B 120 . ? 1_555 ? 
38 AC4 7  ILE B 197 ? ILE B 212 . ? 1_555 ? 
39 AC4 7  GLY B 286 ? GLY B 301 . ? 1_555 ? 
40 AC4 7  ALA B 287 ? ALA B 302 . ? 1_555 ? 
41 AC4 7  THR B 291 ? THR B 306 . ? 1_555 ? 
42 AC4 7  SER B 352 ? SER B 367 . ? 1_555 ? 
43 AC4 7  HEM E .   ? HEM B 600 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4R21 
_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                    4R21 
_atom_sites.fract_transf_matrix[1][1]   0.017876 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000634 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012718 
_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]   0.010488 
_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 
N  
O  
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   . ASN A 1 38  ? -3.729  -8.159  -18.399 1.00   74.66  ? 53  ASN A N   1 
ATOM   2    C  CA  . ASN A 1 38  ? -2.854  -8.609  -19.537 1.00   74.09  ? 53  ASN A CA  1 
ATOM   3    C  C   . ASN A 1 38  ? -1.376  -8.519  -19.155 1.00   71.40  ? 53  ASN A C   1 
ATOM   4    O  O   . ASN A 1 38  ? -0.669  -9.532  -19.172 1.00   80.39  ? 53  ASN A O   1 
ATOM   5    C  CB  . ASN A 1 38  ? -3.130  -7.803  -20.808 1.00   73.29  ? 53  ASN A CB  1 
ATOM   6    N  N   . LEU A 1 39  ? -0.910  -7.326  -18.788 1.00   62.84  ? 54  LEU A N   1 
ATOM   7    C  CA  . LEU A 1 39  ? 0.523   -7.101  -18.580 1.00   56.11  ? 54  LEU A CA  1 
ATOM   8    C  C   . LEU A 1 39  ? 0.756   -5.927  -17.639 1.00   50.36  ? 54  LEU A C   1 
ATOM   9    O  O   . LEU A 1 39  ? 0.180   -4.871  -17.807 1.00   49.12  ? 54  LEU A O   1 
ATOM   10   C  CB  . LEU A 1 39  ? 1.187   -6.841  -19.940 1.00   56.08  ? 54  LEU A CB  1 
ATOM   11   C  CG  . LEU A 1 39  ? 2.703   -6.885  -20.066 1.00   55.14  ? 54  LEU A CG  1 
ATOM   12   C  CD1 . LEU A 1 39  ? 3.230   -8.276  -19.756 1.00   55.40  ? 54  LEU A CD1 1 
ATOM   13   C  CD2 . LEU A 1 39  ? 3.127   -6.467  -21.464 1.00   55.57  ? 54  LEU A CD2 1 
ATOM   14   N  N   . PRO A 1 40  ? 1.611   -6.097  -16.638 1.00   47.20  ? 55  PRO A N   1 
ATOM   15   C  CA  . PRO A 1 40  ? 1.663   -5.019  -15.653 1.00   44.21  ? 55  PRO A CA  1 
ATOM   16   C  C   . PRO A 1 40  ? 2.110   -3.690  -16.247 1.00   42.39  ? 55  PRO A C   1 
ATOM   17   O  O   . PRO A 1 40  ? 2.906   -3.646  -17.170 1.00   43.18  ? 55  PRO A O   1 
ATOM   18   C  CB  . PRO A 1 40  ? 2.692   -5.511  -14.653 1.00   43.67  ? 55  PRO A CB  1 
ATOM   19   C  CG  . PRO A 1 40  ? 2.772   -6.982  -14.862 1.00   45.31  ? 55  PRO A CG  1 
ATOM   20   C  CD  . PRO A 1 40  ? 2.560   -7.174  -16.323 1.00   46.70  ? 55  PRO A CD  1 
ATOM   21   N  N   . PRO A 1 41  ? 1.597   -2.594  -15.719 1.00   40.51  ? 56  PRO A N   1 
ATOM   22   C  CA  . PRO A 1 41  ? 1.999   -1.325  -16.310 1.00   40.08  ? 56  PRO A CA  1 
ATOM   23   C  C   . PRO A 1 41  ? 3.521   -1.093  -16.472 1.00   39.57  ? 56  PRO A C   1 
ATOM   24   O  O   . PRO A 1 41  ? 3.921   -0.469  -17.468 1.00   41.12  ? 56  PRO A O   1 
ATOM   25   C  CB  . PRO A 1 41  ? 1.390   -0.300  -15.354 1.00   39.03  ? 56  PRO A CB  1 
ATOM   26   C  CG  . PRO A 1 41  ? 0.189   -0.996  -14.814 1.00   39.49  ? 56  PRO A CG  1 
ATOM   27   C  CD  . PRO A 1 41  ? 0.588   -2.429  -14.660 1.00   39.57  ? 56  PRO A CD  1 
ATOM   28   N  N   . HIS A 1 42  ? 4.357   -1.559  -15.541 1.00   37.72  ? 57  HIS A N   1 
ATOM   29   C  CA  . HIS A 1 42  ? 5.785   -1.243  -15.638 1.00   36.97  ? 57  HIS A CA  1 
ATOM   30   C  C   . HIS A 1 42  ? 6.407   -1.893  -16.846 1.00   37.77  ? 57  HIS A C   1 
ATOM   31   O  O   . HIS A 1 42  ? 7.247   -1.271  -17.499 1.00   37.92  ? 57  HIS A O   1 
ATOM   32   C  CB  . HIS A 1 42  ? 6.609   -1.552  -14.364 1.00   36.11  ? 57  HIS A CB  1 
ATOM   33   C  CG  . HIS A 1 42  ? 6.679   -2.999  -13.976 1.00   35.95  ? 57  HIS A CG  1 
ATOM   34   N  ND1 . HIS A 1 42  ? 5.619   -3.679  -13.405 1.00   36.09  ? 57  HIS A ND1 1 
ATOM   35   C  CD2 . HIS A 1 42  ? 7.711   -3.871  -13.998 1.00   36.28  ? 57  HIS A CD2 1 
ATOM   36   C  CE1 . HIS A 1 42  ? 5.981   -4.922  -13.135 1.00   36.22  ? 57  HIS A CE1 1 
ATOM   37   N  NE2 . HIS A 1 42  ? 7.244   -5.069  -13.491 1.00   36.98  ? 57  HIS A NE2 1 
ATOM   38   N  N   . LEU A 1 43  ? 5.996   -3.125  -17.146 1.00   38.07  ? 58  LEU A N   1 
ATOM   39   C  CA  . LEU A 1 43  ? 6.449   -3.801  -18.370 1.00   39.38  ? 58  LEU A CA  1 
ATOM   40   C  C   . LEU A 1 43  ? 5.773   -3.255  -19.633 1.00   40.50  ? 58  LEU A C   1 
ATOM   41   O  O   . LEU A 1 43  ? 6.401   -3.126  -20.684 1.00   40.59  ? 58  LEU A O   1 
ATOM   42   C  CB  . LEU A 1 43  ? 6.178   -5.298  -18.284 1.00   39.92  ? 58  LEU A CB  1 
ATOM   43   C  CG  . LEU A 1 43  ? 6.875   -6.033  -17.139 1.00   38.90  ? 58  LEU A CG  1 
ATOM   44   C  CD1 . LEU A 1 43  ? 6.484   -7.500  -17.171 1.00   39.84  ? 58  LEU A CD1 1 
ATOM   45   C  CD2 . LEU A 1 43  ? 8.378   -5.899  -17.246 1.00   38.58  ? 58  LEU A CD2 1 
ATOM   46   N  N   . LEU A 1 44  ? 4.493   -2.926  -19.523 1.00   41.05  ? 59  LEU A N   1 
ATOM   47   C  CA  . LEU A 1 44  ? 3.748   -2.454  -20.680 1.00   42.80  ? 59  LEU A CA  1 
ATOM   48   C  C   . LEU A 1 44  ? 4.403   -1.217  -21.255 1.00   41.76  ? 59  LEU A C   1 
ATOM   49   O  O   . LEU A 1 44  ? 4.699   -1.176  -22.432 1.00   42.27  ? 59  LEU A O   1 
ATOM   50   C  CB  . LEU A 1 44  ? 2.295   -2.178  -20.305 1.00   43.67  ? 59  LEU A CB  1 
ATOM   51   C  CG  . LEU A 1 44  ? 1.245   -1.879  -21.394 1.00   45.43  ? 59  LEU A CG  1 
ATOM   52   C  CD1 . LEU A 1 44  ? 1.017   -0.391  -21.598 1.00   45.07  ? 59  LEU A CD1 1 
ATOM   53   C  CD2 . LEU A 1 44  ? 1.573   -2.561  -22.714 1.00   47.48  ? 59  LEU A CD2 1 
ATOM   54   N  N   . PHE A 1 45  ? 4.680   -0.235  -20.404 1.00   40.49  ? 60  PHE A N   1 
ATOM   55   C  CA  . PHE A 1 45  ? 5.251   1.035   -20.860 1.00   39.70  ? 60  PHE A CA  1 
ATOM   56   C  C   . PHE A 1 45  ? 6.723   0.874   -21.190 1.00   39.50  ? 60  PHE A C   1 
ATOM   57   O  O   . PHE A 1 45  ? 7.270   1.629   -21.995 1.00   39.84  ? 60  PHE A O   1 
ATOM   58   C  CB  . PHE A 1 45  ? 5.035   2.150   -19.837 1.00   38.50  ? 60  PHE A CB  1 
ATOM   59   C  CG  . PHE A 1 45  ? 3.598   2.458   -19.612 1.00   39.20  ? 60  PHE A CG  1 
ATOM   60   C  CD1 . PHE A 1 45  ? 2.851   3.085   -20.616 1.00   40.72  ? 60  PHE A CD1 1 
ATOM   61   C  CD2 . PHE A 1 45  ? 2.955   2.063   -18.444 1.00   38.55  ? 60  PHE A CD2 1 
ATOM   62   C  CE1 . PHE A 1 45  ? 1.487   3.337   -20.451 1.00   41.27  ? 60  PHE A CE1 1 
ATOM   63   C  CE2 . PHE A 1 45  ? 1.606   2.322   -18.259 1.00   39.46  ? 60  PHE A CE2 1 
ATOM   64   C  CZ  . PHE A 1 45  ? 0.869   2.962   -19.258 1.00   41.04  ? 60  PHE A CZ  1 
ATOM   65   N  N   . THR A 1 46  ? 7.369   -0.114  -20.589 1.00   38.72  ? 61  THR A N   1 
ATOM   66   C  CA  . THR A 1 46  ? 8.741   -0.378  -20.967 1.00   39.32  ? 61  THR A CA  1 
ATOM   67   C  C   . THR A 1 46  ? 8.749   -0.863  -22.423 1.00   41.37  ? 61  THR A C   1 
ATOM   68   O  O   . THR A 1 46  ? 9.459   -0.308  -23.252 1.00   41.16  ? 61  THR A O   1 
ATOM   69   C  CB  . THR A 1 46  ? 9.407   -1.396  -20.048 1.00   37.97  ? 61  THR A CB  1 
ATOM   70   O  OG1 . THR A 1 46  ? 9.532   -0.821  -18.757 1.00   36.69  ? 61  THR A OG1 1 
ATOM   71   C  CG2 . THR A 1 46  ? 10.750  -1.728  -20.555 1.00   38.07  ? 61  THR A CG2 1 
ATOM   72   N  N   . GLN A 1 47  ? 7.921   -1.870  -22.692 1.00   42.90  ? 62  GLN A N   1 
ATOM   73   C  CA  . GLN A 1 47  ? 7.710   -2.427  -24.012 1.00   45.78  ? 62  GLN A CA  1 
ATOM   74   C  C   . GLN A 1 47  ? 7.274   -1.411  -25.084 1.00   46.26  ? 62  GLN A C   1 
ATOM   75   O  O   . GLN A 1 47  ? 7.697   -1.505  -26.229 1.00   47.16  ? 62  GLN A O   1 
ATOM   76   C  CB  . GLN A 1 47  ? 6.638   -3.477  -23.903 1.00   48.17  ? 62  GLN A CB  1 
ATOM   77   C  CG  . GLN A 1 47  ? 6.857   -4.722  -24.707 1.00   51.41  ? 62  GLN A CG  1 
ATOM   78   C  CD  . GLN A 1 47  ? 6.259   -5.923  -23.988 1.00   54.07  ? 62  GLN A CD  1 
ATOM   79   O  OE1 . GLN A 1 47  ? 6.774   -6.358  -22.920 1.00   53.54  ? 62  GLN A OE1 1 
ATOM   80   N  NE2 . GLN A 1 47  ? 5.151   -6.461  -24.547 1.00   55.19  ? 62  GLN A NE2 1 
ATOM   81   N  N   . LEU A 1 48  ? 6.450   -0.433  -24.738 1.00   45.60  ? 63  LEU A N   1 
ATOM   82   C  CA  . LEU A 1 48  ? 6.020   0.520   -25.765 1.00   47.30  ? 63  LEU A CA  1 
ATOM   83   C  C   . LEU A 1 48  ? 7.089   1.526   -26.102 1.00   47.52  ? 63  LEU A C   1 
ATOM   84   O  O   . LEU A 1 48  ? 6.949   2.254   -27.069 1.00   48.73  ? 63  LEU A O   1 
ATOM   85   C  CB  . LEU A 1 48  ? 4.750   1.303   -25.360 1.00   47.02  ? 63  LEU A CB  1 
ATOM   86   C  CG  . LEU A 1 48  ? 3.488   0.514   -25.036 1.00   46.74  ? 63  LEU A CG  1 
ATOM   87   C  CD1 . LEU A 1 48  ? 2.310   1.448   -24.886 1.00   46.81  ? 63  LEU A CD1 1 
ATOM   88   C  CD2 . LEU A 1 48  ? 3.236   -0.531  -26.089 1.00   48.08  ? 63  LEU A CD2 1 
ATOM   89   N  N   . SER A 1 49  ? 8.132   1.611   -25.294 1.00   48.01  ? 64  SER A N   1 
ATOM   90   C  CA  . SER A 1 49  ? 9.083   2.694   -25.443 1.00   48.84  ? 64  SER A CA  1 
ATOM   91   C  C   . SER A 1 49  ? 9.979   2.489   -26.629 1.00   51.37  ? 64  SER A C   1 
ATOM   92   O  O   . SER A 1 49  ? 10.438  3.439   -27.237 1.00   50.72  ? 64  SER A O   1 
ATOM   93   C  CB  . SER A 1 49  ? 9.854   2.865   -24.166 1.00   48.05  ? 64  SER A CB  1 
ATOM   94   O  OG  . SER A 1 49  ? 8.895   3.142   -23.144 1.00   49.08  ? 64  SER A OG  1 
ATOM   95   N  N   . SER A 1 50  ? 10.184  1.236   -26.989 1.00   54.94  ? 65  SER A N   1 
ATOM   96   C  CA  . SER A 1 50  ? 10.873  0.912   -28.215 1.00   59.95  ? 65  SER A CA  1 
ATOM   97   C  C   . SER A 1 50  ? 10.198  1.577   -29.411 1.00   63.03  ? 65  SER A C   1 
ATOM   98   O  O   . SER A 1 50  ? 10.806  2.389   -30.116 1.00   66.03  ? 65  SER A O   1 
ATOM   99   C  CB  . SER A 1 50  ? 10.864  -0.606  -28.411 1.00   62.40  ? 65  SER A CB  1 
ATOM   100  O  OG  . SER A 1 50  ? 11.027  -1.255  -27.159 1.00   62.69  ? 65  SER A OG  1 
ATOM   101  N  N   . GLN A 1 51  ? 8.931   1.249   -29.629 1.00   62.42  ? 66  GLN A N   1 
ATOM   102  C  CA  . GLN A 1 51  ? 8.291   1.590   -30.908 1.00   64.07  ? 66  GLN A CA  1 
ATOM   103  C  C   . GLN A 1 51  ? 7.712   2.992   -30.881 1.00   59.99  ? 66  GLN A C   1 
ATOM   104  O  O   . GLN A 1 51  ? 7.883   3.746   -31.829 1.00   59.08  ? 66  GLN A O   1 
ATOM   105  C  CB  . GLN A 1 51  ? 7.231   0.540   -31.319 1.00   67.85  ? 66  GLN A CB  1 
ATOM   106  C  CG  . GLN A 1 51  ? 6.340   -0.007  -30.187 1.00   68.13  ? 66  GLN A CG  1 
ATOM   107  C  CD  . GLN A 1 51  ? 6.313   -1.528  -30.121 1.00   70.03  ? 66  GLN A CD  1 
ATOM   108  O  OE1 . GLN A 1 51  ? 6.412   -2.216  -31.162 1.00   76.41  ? 66  GLN A OE1 1 
ATOM   109  N  NE2 . GLN A 1 51  ? 6.153   -2.069  -28.908 1.00   66.51  ? 66  GLN A NE2 1 
ATOM   110  N  N   . TYR A 1 52  ? 7.034   3.331   -29.790 1.00   55.73  ? 67  TYR A N   1 
ATOM   111  C  CA  . TYR A 1 52  ? 6.463   4.660   -29.607 1.00   53.98  ? 67  TYR A CA  1 
ATOM   112  C  C   . TYR A 1 52  ? 7.424   5.291   -28.632 1.00   52.23  ? 67  TYR A C   1 
ATOM   113  O  O   . TYR A 1 52  ? 8.421   4.665   -28.300 1.00   53.65  ? 67  TYR A O   1 
ATOM   114  C  CB  . TYR A 1 52  ? 5.005   4.552   -29.127 1.00   53.56  ? 67  TYR A CB  1 
ATOM   115  C  CG  . TYR A 1 52  ? 4.165   3.590   -30.002 1.00   54.89  ? 67  TYR A CG  1 
ATOM   116  C  CD1 . TYR A 1 52  ? 3.622   4.006   -31.215 1.00   55.93  ? 67  TYR A CD1 1 
ATOM   117  C  CD2 . TYR A 1 52  ? 3.960   2.252   -29.627 1.00   54.60  ? 67  TYR A CD2 1 
ATOM   118  C  CE1 . TYR A 1 52  ? 2.889   3.130   -32.011 1.00   57.52  ? 67  TYR A CE1 1 
ATOM   119  C  CE2 . TYR A 1 52  ? 3.213   1.376   -30.404 1.00   55.19  ? 67  TYR A CE2 1 
ATOM   120  C  CZ  . TYR A 1 52  ? 2.684   1.814   -31.599 1.00   57.62  ? 67  TYR A CZ  1 
ATOM   121  O  OH  . TYR A 1 52  ? 1.958   0.945   -32.411 1.00   59.17  ? 67  TYR A OH  1 
ATOM   122  N  N   . GLY A 1 53  ? 7.225   6.521   -28.192 1.00   50.83  ? 68  GLY A N   1 
ATOM   123  C  CA  . GLY A 1 53  ? 8.307   7.163   -27.392 1.00   50.05  ? 68  GLY A CA  1 
ATOM   124  C  C   . GLY A 1 53  ? 8.589   6.577   -25.998 1.00   47.86  ? 68  GLY A C   1 
ATOM   125  O  O   . GLY A 1 53  ? 8.076   5.519   -25.633 1.00   48.04  ? 68  GLY A O   1 
ATOM   126  N  N   . PRO A 1 54  ? 9.414   7.267   -25.198 1.00   46.01  ? 69  PRO A N   1 
ATOM   127  C  CA  . PRO A 1 54  ? 9.598   6.936   -23.772 1.00   43.83  ? 69  PRO A CA  1 
ATOM   128  C  C   . PRO A 1 54  ? 8.808   7.844   -22.797 1.00   42.09  ? 69  PRO A C   1 
ATOM   129  O  O   . PRO A 1 54  ? 8.853   7.656   -21.605 1.00   40.76  ? 69  PRO A O   1 
ATOM   130  C  CB  . PRO A 1 54  ? 11.107  7.096   -23.579 1.00   43.34  ? 69  PRO A CB  1 
ATOM   131  C  CG  . PRO A 1 54  ? 11.483  8.159   -24.555 1.00   44.58  ? 69  PRO A CG  1 
ATOM   132  C  CD  . PRO A 1 54  ? 10.474  8.169   -25.678 1.00   46.12  ? 69  PRO A CD  1 
ATOM   133  N  N   . LEU A 1 55  ? 8.071   8.796   -23.333 1.00   42.28  ? 70  LEU A N   1 
ATOM   134  C  CA  . LEU A 1 55  ? 7.174   9.639   -22.578 1.00   41.42  ? 70  LEU A CA  1 
ATOM   135  C  C   . LEU A 1 55  ? 5.716   9.458   -23.110 1.00   43.13  ? 70  LEU A C   1 
ATOM   136  O  O   . LEU A 1 55  ? 5.430   9.615   -24.298 1.00   45.00  ? 70  LEU A O   1 
ATOM   137  C  CB  . LEU A 1 55  ? 7.659   11.075  -22.717 1.00   40.74  ? 70  LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 55  ? 6.879   12.173  -22.019 1.00   39.84  ? 70  LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 55  ? 6.968   11.986  -20.520 1.00   38.79  ? 70  LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 55  ? 7.375   13.547  -22.457 1.00   40.19  ? 70  LEU A CD2 1 
ATOM   141  N  N   . PHE A 1 56  ? 4.811   9.141   -22.200 1.00   43.95  ? 71  PHE A N   1 
ATOM   142  C  CA  . PHE A 1 56  ? 3.445   8.764   -22.498 1.00   45.20  ? 71  PHE A CA  1 
ATOM   143  C  C   . PHE A 1 56  ? 2.523   9.547   -21.616 1.00   44.23  ? 71  PHE A C   1 
ATOM   144  O  O   . PHE A 1 56  ? 2.773   9.640   -20.428 1.00   44.02  ? 71  PHE A O   1 
ATOM   145  C  CB  . PHE A 1 56  ? 3.241   7.312   -22.130 1.00   46.51  ? 71  PHE A CB  1 
ATOM   146  C  CG  . PHE A 1 56  ? 3.195   6.422   -23.283 1.00   49.49  ? 71  PHE A CG  1 
ATOM   147  C  CD1 . PHE A 1 56  ? 4.374   5.995   -23.888 1.00   51.55  ? 71  PHE A CD1 1 
ATOM   148  C  CD2 . PHE A 1 56  ? 1.961   6.020   -23.803 1.00   52.03  ? 71  PHE A CD2 1 
ATOM   149  C  CE1 . PHE A 1 56  ? 4.328   5.165   -25.007 1.00   53.99  ? 71  PHE A CE1 1 
ATOM   150  C  CE2 . PHE A 1 56  ? 1.904   5.185   -24.909 1.00   53.82  ? 71  PHE A CE2 1 
ATOM   151  C  CZ  . PHE A 1 56  ? 3.093   4.759   -25.515 1.00   54.73  ? 71  PHE A CZ  1 
ATOM   152  N  N   . GLY A 1 57  ? 1.432   10.041  -22.180 1.00   44.40  ? 72  GLY A N   1 
ATOM   153  C  CA  . GLY A 1 57  ? 0.429   10.796  -21.443 1.00   43.97  ? 72  GLY A CA  1 
ATOM   154  C  C   . GLY A 1 57  ? -0.904  10.064  -21.381 1.00   44.35  ? 72  GLY A C   1 
ATOM   155  O  O   . GLY A 1 57  ? -1.560  9.807   -22.395 1.00   45.21  ? 72  GLY A O   1 
ATOM   156  N  N   . LEU A 1 58  ? -1.290  9.719   -20.169 1.00   43.71  ? 73  LEU A N   1 
ATOM   157  C  CA  . LEU A 1 58  ? -2.548  9.080   -19.904 1.00   43.90  ? 73  LEU A CA  1 
ATOM   158  C  C   . LEU A 1 58  ? -3.473  10.155  -19.371 1.00   45.76  ? 73  LEU A C   1 
ATOM   159  O  O   . LEU A 1 58  ? -3.022  11.033  -18.619 1.00   45.15  ? 73  LEU A O   1 
ATOM   160  C  CB  . LEU A 1 58  ? -2.338  8.006   -18.865 1.00   41.70  ? 73  LEU A CB  1 
ATOM   161  C  CG  . LEU A 1 58  ? -1.220  7.071   -19.278 1.00   41.56  ? 73  LEU A CG  1 
ATOM   162  C  CD1 . LEU A 1 58  ? -0.668  6.311   -18.097 1.00   40.89  ? 73  LEU A CD1 1 
ATOM   163  C  CD2 . LEU A 1 58  ? -1.685  6.106   -20.335 1.00   43.24  ? 73  LEU A CD2 1 
ATOM   164  N  N   . TYR A 1 59  ? -4.749  10.100  -19.758 1.00   48.29  ? 74  TYR A N   1 
ATOM   165  C  CA  . TYR A 1 59  ? -5.737  11.039  -19.237 1.00   51.10  ? 74  TYR A CA  1 
ATOM   166  C  C   . TYR A 1 59  ? -6.816  10.361  -18.402 1.00   55.25  ? 74  TYR A C   1 
ATOM   167  O  O   . TYR A 1 59  ? -7.296  9.299   -18.750 1.00   59.74  ? 74  TYR A O   1 
ATOM   168  C  CB  . TYR A 1 59  ? -6.355  11.814  -20.376 1.00   51.19  ? 74  TYR A CB  1 
ATOM   169  C  CG  . TYR A 1 59  ? -5.330  12.628  -21.110 1.00   51.10  ? 74  TYR A CG  1 
ATOM   170  C  CD1 . TYR A 1 59  ? -4.462  12.040  -22.014 1.00   50.95  ? 74  TYR A CD1 1 
ATOM   171  C  CD2 . TYR A 1 59  ? -5.218  13.992  -20.887 1.00   51.85  ? 74  TYR A CD2 1 
ATOM   172  C  CE1 . TYR A 1 59  ? -3.504  12.791  -22.679 1.00   51.82  ? 74  TYR A CE1 1 
ATOM   173  C  CE2 . TYR A 1 59  ? -4.273  14.754  -21.542 1.00   52.03  ? 74  TYR A CE2 1 
ATOM   174  C  CZ  . TYR A 1 59  ? -3.416  14.152  -22.444 1.00   52.05  ? 74  TYR A CZ  1 
ATOM   175  O  OH  . TYR A 1 59  ? -2.478  14.920  -23.095 1.00   51.81  ? 74  TYR A OH  1 
ATOM   176  N  N   . ALA A 1 60  ? -7.187  10.978  -17.287 1.00   59.88  ? 75  ALA A N   1 
ATOM   177  C  CA  . ALA A 1 60  ? -8.272  10.470  -16.444 1.00   63.59  ? 75  ALA A CA  1 
ATOM   178  C  C   . ALA A 1 60  ? -8.750  11.544  -15.477 1.00   67.03  ? 75  ALA A C   1 
ATOM   179  O  O   . ALA A 1 60  ? -8.064  11.887  -14.541 1.00   64.31  ? 75  ALA A O   1 
ATOM   180  C  CB  . ALA A 1 60  ? -7.819  9.243   -15.672 1.00   63.06  ? 75  ALA A CB  1 
ATOM   181  N  N   . GLY A 1 61  ? -9.946  12.063  -15.703 1.00   78.57  ? 76  GLY A N   1 
ATOM   182  C  CA  . GLY A 1 61  ? -10.459 13.152  -14.886 1.00   84.47  ? 76  GLY A CA  1 
ATOM   183  C  C   . GLY A 1 61  ? -9.806  14.441  -15.337 1.00   87.76  ? 76  GLY A C   1 
ATOM   184  O  O   . GLY A 1 61  ? -9.560  14.627  -16.525 1.00   86.66  ? 76  GLY A O   1 
ATOM   185  N  N   . PRO A 1 62  ? -9.515  15.340  -14.393 1.00   90.57  ? 77  PRO A N   1 
ATOM   186  C  CA  . PRO A 1 62  ? -8.884  16.580  -14.806 1.00   87.96  ? 77  PRO A CA  1 
ATOM   187  C  C   . PRO A 1 62  ? -7.359  16.471  -14.907 1.00   81.27  ? 77  PRO A C   1 
ATOM   188  O  O   . PRO A 1 62  ? -6.746  17.331  -15.534 1.00   81.12  ? 77  PRO A O   1 
ATOM   189  C  CB  . PRO A 1 62  ? -9.282  17.548  -13.689 1.00   91.70  ? 77  PRO A CB  1 
ATOM   190  C  CG  . PRO A 1 62  ? -9.433  16.684  -12.468 1.00   90.97  ? 77  PRO A CG  1 
ATOM   191  C  CD  . PRO A 1 62  ? -9.733  15.282  -12.933 1.00   90.00  ? 77  PRO A CD  1 
ATOM   192  N  N   . HIS A 1 63  ? -6.754  15.437  -14.312 1.00   74.28  ? 78  HIS A N   1 
ATOM   193  C  CA  . HIS A 1 63  ? -5.289  15.365  -14.194 1.00   70.67  ? 78  HIS A CA  1 
ATOM   194  C  C   . HIS A 1 63  ? -4.607  14.600  -15.320 1.00   61.79  ? 78  HIS A C   1 
ATOM   195  O  O   . HIS A 1 63  ? -4.987  13.477  -15.669 1.00   60.75  ? 78  HIS A O   1 
ATOM   196  C  CB  . HIS A 1 63  ? -4.871  14.726  -12.866 1.00   76.24  ? 78  HIS A CB  1 
ATOM   197  C  CG  . HIS A 1 63  ? -5.341  15.475  -11.661 1.00   84.43  ? 78  HIS A CG  1 
ATOM   198  N  ND1 . HIS A 1 63  ? -4.824  16.703  -11.301 1.00   89.45  ? 78  HIS A ND1 1 
ATOM   199  C  CD2 . HIS A 1 63  ? -6.284  15.175  -10.736 1.00   87.65  ? 78  HIS A CD2 1 
ATOM   200  C  CE1 . HIS A 1 63  ? -5.430  17.128  -10.207 1.00   90.96  ? 78  HIS A CE1 1 
ATOM   201  N  NE2 . HIS A 1 63  ? -6.318  16.218  -9.843  1.00   91.72  ? 78  HIS A NE2 1 
ATOM   202  N  N   . LEU A 1 64  ? -3.563  15.203  -15.865 1.00   54.05  ? 79  LEU A N   1 
ATOM   203  C  CA  . LEU A 1 64  ? -2.734  14.510  -16.821 1.00   49.97  ? 79  LEU A CA  1 
ATOM   204  C  C   . LEU A 1 64  ? -1.752  13.643  -16.043 1.00   46.30  ? 79  LEU A C   1 
ATOM   205  O  O   . LEU A 1 64  ? -1.275  14.042  -14.980 1.00   45.61  ? 79  LEU A O   1 
ATOM   206  C  CB  . LEU A 1 64  ? -2.034  15.517  -17.741 1.00   49.75  ? 79  LEU A CB  1 
ATOM   207  C  CG  . LEU A 1 64  ? -0.872  15.053  -18.625 1.00   49.27  ? 79  LEU A CG  1 
ATOM   208  C  CD1 . LEU A 1 64  ? -1.249  13.961  -19.602 1.00   48.66  ? 79  LEU A CD1 1 
ATOM   209  C  CD2 . LEU A 1 64  ? -0.329  16.264  -19.352 1.00   50.16  ? 79  LEU A CD2 1 
ATOM   210  N  N   . THR A 1 65  ? -1.480  12.445  -16.558 1.00   44.07  ? 80  THR A N   1 
ATOM   211  C  CA  . THR A 1 65  ? -0.474  11.569  -15.969 1.00   42.08  ? 80  THR A CA  1 
ATOM   212  C  C   . THR A 1 65  ? 0.592   11.143  -17.011 1.00   41.97  ? 80  THR A C   1 
ATOM   213  O  O   . THR A 1 65  ? 0.286   10.381  -17.945 1.00   42.73  ? 80  THR A O   1 
ATOM   214  C  CB  . THR A 1 65  ? -1.125  10.334  -15.324 1.00   41.43  ? 80  THR A CB  1 
ATOM   215  O  OG1 . THR A 1 65  ? -1.948  10.733  -14.212 1.00   40.86  ? 80  THR A OG1 1 
ATOM   216  C  CG2 . THR A 1 65  ? -0.063  9.377   -14.832 1.00   40.40  ? 80  THR A CG2 1 
ATOM   217  N  N   . LEU A 1 66  ? 1.827   11.638  -16.842 1.00   39.50  ? 81  LEU A N   1 
ATOM   218  C  CA  . LEU A 1 66  ? 2.933   11.296  -17.720 1.00   39.00  ? 81  LEU A CA  1 
ATOM   219  C  C   . LEU A 1 66  ? 3.669   10.058  -17.209 1.00   38.46  ? 81  LEU A C   1 
ATOM   220  O  O   . LEU A 1 66  ? 3.932   9.935   -16.037 1.00   38.64  ? 81  LEU A O   1 
ATOM   221  C  CB  . LEU A 1 66  ? 3.919   12.466  -17.787 1.00   38.90  ? 81  LEU A CB  1 
ATOM   222  C  CG  . LEU A 1 66  ? 3.808   13.611  -18.804 1.00   40.26  ? 81  LEU A CG  1 
ATOM   223  C  CD1 . LEU A 1 66  ? 2.487   13.674  -19.566 1.00   41.42  ? 81  LEU A CD1 1 
ATOM   224  C  CD2 . LEU A 1 66  ? 4.082   14.938  -18.123 1.00   39.83  ? 81  LEU A CD2 1 
ATOM   225  N  N   . VAL A 1 67  ? 4.047   9.146   -18.079 1.00   39.05  ? 82  VAL A N   1 
ATOM   226  C  CA  . VAL A 1 67  ? 4.876   8.036   -17.657 1.00   38.35  ? 82  VAL A CA  1 
ATOM   227  C  C   . VAL A 1 67  ? 6.226   8.165   -18.358 1.00   38.78  ? 82  VAL A C   1 
ATOM   228  O  O   . VAL A 1 67  ? 6.281   8.248   -19.598 1.00   39.90  ? 82  VAL A O   1 
ATOM   229  C  CB  . VAL A 1 67  ? 4.237   6.706   -18.035 1.00   39.25  ? 82  VAL A CB  1 
ATOM   230  C  CG1 . VAL A 1 67  ? 5.062   5.549   -17.490 1.00   39.10  ? 82  VAL A CG1 1 
ATOM   231  C  CG2 . VAL A 1 67  ? 2.814   6.631   -17.497 1.00   39.56  ? 82  VAL A CG2 1 
ATOM   232  N  N   . VAL A 1 68  ? 7.299   8.140   -17.564 1.00   37.00  ? 83  VAL A N   1 
ATOM   233  C  CA  . VAL A 1 68  ? 8.658   8.402   -18.033 1.00   36.54  ? 83  VAL A CA  1 
ATOM   234  C  C   . VAL A 1 68  ? 9.552   7.157   -17.991 1.00   35.88  ? 83  VAL A C   1 
ATOM   235  O  O   . VAL A 1 68  ? 9.885   6.686   -16.896 1.00   35.31  ? 83  VAL A O   1 
ATOM   236  C  CB  . VAL A 1 68  ? 9.349   9.450   -17.149 1.00   36.27  ? 83  VAL A CB  1 
ATOM   237  C  CG1 . VAL A 1 68  ? 10.636  9.863   -17.815 1.00   37.10  ? 83  VAL A CG1 1 
ATOM   238  C  CG2 . VAL A 1 68  ? 8.491   10.680  -16.961 1.00   36.60  ? 83  VAL A CG2 1 
ATOM   239  N  N   . SER A 1 69  ? 9.979   6.659   -19.159 1.00   36.01  ? 84  SER A N   1 
ATOM   240  C  CA  . SER A 1 69  ? 10.722  5.384   -19.249 1.00   36.27  ? 84  SER A CA  1 
ATOM   241  C  C   . SER A 1 69  ? 12.154  5.465   -19.791 1.00   36.71  ? 84  SER A C   1 
ATOM   242  O  O   . SER A 1 69  ? 12.645  4.513   -20.357 1.00   37.74  ? 84  SER A O   1 
ATOM   243  C  CB  . SER A 1 69  ? 9.915   4.369   -20.068 1.00   36.63  ? 84  SER A CB  1 
ATOM   244  O  OG  . SER A 1 69  ? 8.666   4.127   -19.452 1.00   36.32  ? 84  SER A OG  1 
ATOM   245  N  N   . GLU A 1 70  ? 12.831  6.581   -19.596 1.00   36.94  ? 85  GLU A N   1 
ATOM   246  C  CA  . GLU A 1 70  ? 14.160  6.748   -20.142 1.00   38.74  ? 85  GLU A CA  1 
ATOM   247  C  C   . GLU A 1 70  ? 14.941  7.663   -19.236 1.00   39.15  ? 85  GLU A C   1 
ATOM   248  O  O   . GLU A 1 70  ? 14.411  8.692   -18.801 1.00   38.15  ? 85  GLU A O   1 
ATOM   249  C  CB  . GLU A 1 70  ? 14.073  7.345   -21.541 1.00   40.90  ? 85  GLU A CB  1 
ATOM   250  C  CG  . GLU A 1 70  ? 15.376  7.487   -22.320 1.00   42.02  ? 85  GLU A CG  1 
ATOM   251  C  CD  . GLU A 1 70  ? 16.174  8.738   -21.995 1.00   42.20  ? 85  GLU A CD  1 
ATOM   252  O  OE1 . GLU A 1 70  ? 15.596  9.840   -21.830 1.00   41.66  ? 85  GLU A OE1 1 
ATOM   253  O  OE2 . GLU A 1 70  ? 17.413  8.606   -21.927 1.00   43.09  ? 85  GLU A OE2 1 
ATOM   254  N  N   . ILE A 1 71  ? 16.210  7.286   -18.993 1.00   40.37  ? 86  ILE A N   1 
ATOM   255  C  CA  . ILE A 1 71  ? 17.079  7.893   -17.966 1.00   39.68  ? 86  ILE A CA  1 
ATOM   256  C  C   . ILE A 1 71  ? 17.199  9.399   -18.060 1.00   39.49  ? 86  ILE A C   1 
ATOM   257  O  O   . ILE A 1 71  ? 17.027  10.074  -17.068 1.00   39.60  ? 86  ILE A O   1 
ATOM   258  C  CB  . ILE A 1 71  ? 18.502  7.255   -17.915 1.00   40.94  ? 86  ILE A CB  1 
ATOM   259  C  CG1 . ILE A 1 71  ? 19.316  7.845   -16.773 1.00   40.77  ? 86  ILE A CG1 1 
ATOM   260  C  CG2 . ILE A 1 71  ? 19.292  7.440   -19.209 1.00   42.71  ? 86  ILE A CG2 1 
ATOM   261  C  CD1 . ILE A 1 71  ? 18.752  7.543   -15.395 1.00   40.13  ? 86  ILE A CD1 1 
ATOM   262  N  N   . GLY A 1 72  ? 17.454  9.946   -19.234 1.00   39.98  ? 87  GLY A N   1 
ATOM   263  C  CA  . GLY A 1 72  ? 17.546  11.409  -19.355 1.00   40.22  ? 87  GLY A CA  1 
ATOM   264  C  C   . GLY A 1 72  ? 16.268  12.100  -18.937 1.00   39.03  ? 87  GLY A C   1 
ATOM   265  O  O   . GLY A 1 72  ? 16.263  13.112  -18.246 1.00   39.11  ? 87  GLY A O   1 
ATOM   266  N  N   . LEU A 1 73  ? 15.154  11.551  -19.360 1.00   38.40  ? 88  LEU A N   1 
ATOM   267  C  CA  . LEU A 1 73  ? 13.911  12.139  -18.962 1.00   37.44  ? 88  LEU A CA  1 
ATOM   268  C  C   . LEU A 1 73  ? 13.803  11.988  -17.489 1.00   36.08  ? 88  LEU A C   1 
ATOM   269  O  O   . LEU A 1 73  ? 13.562  12.981  -16.820 1.00   36.47  ? 88  LEU A O   1 
ATOM   270  C  CB  . LEU A 1 73  ? 12.723  11.498  -19.667 1.00   37.06  ? 88  LEU A CB  1 
ATOM   271  C  CG  . LEU A 1 73  ? 12.731  11.854  -21.130 1.00   37.94  ? 88  LEU A CG  1 
ATOM   272  C  CD1 . LEU A 1 73  ? 11.800  10.917  -21.862 1.00   38.46  ? 88  LEU A CD1 1 
ATOM   273  C  CD2 . LEU A 1 73  ? 12.327  13.298  -21.314 1.00   38.24  ? 88  LEU A CD2 1 
ATOM   274  N  N   . VAL A 1 74  ? 14.017  10.791  -16.944 1.00   35.27  ? 89  VAL A N   1 
ATOM   275  C  CA  . VAL A 1 74  ? 13.814  10.691  -15.504 1.00   34.79  ? 89  VAL A CA  1 
ATOM   276  C  C   . VAL A 1 74  ? 14.780  11.609  -14.760 1.00   34.95  ? 89  VAL A C   1 
ATOM   277  O  O   . VAL A 1 74  ? 14.404  12.216  -13.774 1.00   33.86  ? 89  VAL A O   1 
ATOM   278  C  CB  . VAL A 1 74  ? 13.859  9.274   -14.898 1.00   34.68  ? 89  VAL A CB  1 
ATOM   279  C  CG1 . VAL A 1 74  ? 13.331  8.208   -15.839 1.00   34.84  ? 89  VAL A CG1 1 
ATOM   280  C  CG2 . VAL A 1 74  ? 15.245  8.921   -14.408 1.00   35.46  ? 89  VAL A CG2 1 
ATOM   281  N  N   . ARG A 1 75  ? 16.001  11.761  -15.261 1.00   36.26  ? 90  ARG A N   1 
ATOM   282  C  CA  . ARG A 1 75  ? 16.932  12.631  -14.598 1.00   37.65  ? 90  ARG A CA  1 
ATOM   283  C  C   . ARG A 1 75  ? 16.392  14.038  -14.633 1.00   37.46  ? 90  ARG A C   1 
ATOM   284  O  O   . ARG A 1 75  ? 16.593  14.815  -13.721 1.00   37.05  ? 90  ARG A O   1 
ATOM   285  C  CB  . ARG A 1 75  ? 18.322  12.551  -15.217 1.00   40.77  ? 90  ARG A CB  1 
ATOM   286  C  CG  . ARG A 1 75  ? 19.049  11.226  -14.976 1.00   42.42  ? 90  ARG A CG  1 
ATOM   287  C  CD  . ARG A 1 75  ? 20.506  11.262  -15.490 1.00   45.42  ? 90  ARG A CD  1 
ATOM   288  N  NE  . ARG A 1 75  ? 21.432  11.458  -14.375 1.00   47.96  ? 90  ARG A NE  1 
ATOM   289  C  CZ  . ARG A 1 75  ? 21.972  10.483  -13.637 1.00   49.01  ? 90  ARG A CZ  1 
ATOM   290  N  NH1 . ARG A 1 75  ? 21.741  9.193   -13.899 1.00   48.59  ? 90  ARG A NH1 1 
ATOM   291  N  NH2 . ARG A 1 75  ? 22.778  10.808  -12.638 1.00   50.94  ? 90  ARG A NH2 1 
ATOM   292  N  N   . GLU A 1 76  ? 15.693  14.386  -15.691 1.00   38.38  ? 91  GLU A N   1 
ATOM   293  C  CA  . GLU A 1 76  ? 15.169  15.734  -15.780 1.00   39.09  ? 91  GLU A CA  1 
ATOM   294  C  C   . GLU A 1 76  ? 14.178  15.977  -14.649 1.00   38.73  ? 91  GLU A C   1 
ATOM   295  O  O   . GLU A 1 76  ? 14.134  17.059  -14.073 1.00   37.17  ? 91  GLU A O   1 
ATOM   296  C  CB  . GLU A 1 76  ? 14.514  15.960  -17.125 1.00   40.00  ? 91  GLU A CB  1 
ATOM   297  C  CG  . GLU A 1 76  ? 14.194  17.415  -17.387 1.00   41.21  ? 91  GLU A CG  1 
ATOM   298  C  CD  . GLU A 1 76  ? 13.638  17.679  -18.777 1.00   42.43  ? 91  GLU A CD  1 
ATOM   299  O  OE1 . GLU A 1 76  ? 13.667  16.811  -19.682 1.00   41.91  ? 91  GLU A OE1 1 
ATOM   300  O  OE2 . GLU A 1 76  ? 13.157  18.802  -18.953 1.00   44.43  ? 91  GLU A OE2 1 
ATOM   301  N  N   . VAL A 1 77  ? 13.389  14.945  -14.339 1.00   39.37  ? 92  VAL A N   1 
ATOM   302  C  CA  . VAL A 1 77  ? 12.329  15.049  -13.328 1.00   39.21  ? 92  VAL A CA  1 
ATOM   303  C  C   . VAL A 1 77  ? 12.907  15.012  -11.915 1.00   39.76  ? 92  VAL A C   1 
ATOM   304  O  O   . VAL A 1 77  ? 12.385  15.689  -11.024 1.00   42.85  ? 92  VAL A O   1 
ATOM   305  C  CB  . VAL A 1 77  ? 11.312  13.898  -13.435 1.00   38.29  ? 92  VAL A CB  1 
ATOM   306  C  CG1 . VAL A 1 77  ? 10.247  14.032  -12.363 1.00   37.66  ? 92  VAL A CG1 1 
ATOM   307  C  CG2 . VAL A 1 77  ? 10.677  13.839  -14.812 1.00   38.65  ? 92  VAL A CG2 1 
ATOM   308  N  N   . LEU A 1 78  ? 13.962  14.231  -11.699 1.00   38.15  ? 93  LEU A N   1 
ATOM   309  C  CA  . LEU A 1 78  ? 14.427  14.008  -10.357 1.00   37.89  ? 93  LEU A CA  1 
ATOM   310  C  C   . LEU A 1 78  ? 15.494  15.008  -9.949  1.00   40.18  ? 93  LEU A C   1 
ATOM   311  O  O   . LEU A 1 78  ? 15.357  15.666  -8.920  1.00   39.96  ? 93  LEU A O   1 
ATOM   312  C  CB  . LEU A 1 78  ? 14.936  12.582  -10.197 1.00   36.92  ? 93  LEU A CB  1 
ATOM   313  C  CG  . LEU A 1 78  ? 13.946  11.434  -10.362 1.00   36.26  ? 93  LEU A CG  1 
ATOM   314  C  CD1 . LEU A 1 78  ? 14.664  10.111  -10.138 1.00   36.20  ? 93  LEU A CD1 1 
ATOM   315  C  CD2 . LEU A 1 78  ? 12.745  11.532  -9.421  1.00   35.64  ? 93  LEU A CD2 1 
ATOM   316  N  N   . LEU A 1 79  ? 16.569  15.085  -10.741 1.00   42.52  ? 94  LEU A N   1 
ATOM   317  C  CA  . LEU A 1 79  ? 17.610  16.079  -10.580 1.00   42.79  ? 94  LEU A CA  1 
ATOM   318  C  C   . LEU A 1 79  ? 17.283  17.414  -11.231 1.00   44.35  ? 94  LEU A C   1 
ATOM   319  O  O   . LEU A 1 79  ? 17.040  18.375  -10.532 1.00   45.55  ? 94  LEU A O   1 
ATOM   320  C  CB  . LEU A 1 79  ? 18.929  15.588  -11.167 1.00   44.22  ? 94  LEU A CB  1 
ATOM   321  C  CG  . LEU A 1 79  ? 19.825  14.698  -10.310 1.00   44.53  ? 94  LEU A CG  1 
ATOM   322  C  CD1 . LEU A 1 79  ? 19.738  14.981  -8.808  1.00   43.53  ? 94  LEU A CD1 1 
ATOM   323  C  CD2 . LEU A 1 79  ? 19.455  13.262  -10.609 1.00   45.16  ? 94  LEU A CD2 1 
ATOM   324  N  N   . GLN A 1 80  ? 17.296  17.478  -12.562 1.00   46.41  ? 95  GLN A N   1 
ATOM   325  C  CA  . GLN A 1 80  ? 17.390  18.765  -13.289 1.00   48.61  ? 95  GLN A CA  1 
ATOM   326  C  C   . GLN A 1 80  ? 16.302  19.775  -12.942 1.00   49.06  ? 95  GLN A C   1 
ATOM   327  O  O   . GLN A 1 80  ? 16.589  20.954  -12.815 1.00   49.14  ? 95  GLN A O   1 
ATOM   328  C  CB  . GLN A 1 80  ? 17.428  18.537  -14.807 1.00   50.45  ? 95  GLN A CB  1 
ATOM   329  C  CG  . GLN A 1 80  ? 17.795  19.756  -15.655 1.00   53.32  ? 95  GLN A CG  1 
ATOM   330  C  CD  . GLN A 1 80  ? 17.477  19.564  -17.140 1.00   54.65  ? 95  GLN A CD  1 
ATOM   331  O  OE1 . GLN A 1 80  ? 17.860  18.566  -17.737 1.00   53.60  ? 95  GLN A OE1 1 
ATOM   332  N  NE2 . GLN A 1 80  ? 16.762  20.525  -17.734 1.00   56.61  ? 95  GLN A NE2 1 
ATOM   333  N  N   . ARG A 1 81  ? 15.058  19.324  -12.836 1.00   51.16  ? 96  ARG A N   1 
ATOM   334  C  CA  . ARG A 1 81  ? 13.956  20.173  -12.370 1.00   53.47  ? 96  ARG A CA  1 
ATOM   335  C  C   . ARG A 1 81  ? 13.300  19.430  -11.213 1.00   52.06  ? 96  ARG A C   1 
ATOM   336  O  O   . ARG A 1 81  ? 12.062  19.338  -11.124 1.00   50.92  ? 96  ARG A O   1 
ATOM   337  C  CB  . ARG A 1 81  ? 12.913  20.503  -13.464 1.00   56.16  ? 96  ARG A CB  1 
ATOM   338  C  CG  . ARG A 1 81  ? 13.236  20.093  -14.892 1.00   60.50  ? 96  ARG A CG  1 
ATOM   339  C  CD  . ARG A 1 81  ? 12.482  20.938  -15.918 1.00   64.94  ? 96  ARG A CD  1 
ATOM   340  N  NE  . ARG A 1 81  ? 13.342  21.970  -16.522 1.00   70.33  ? 96  ARG A NE  1 
ATOM   341  C  CZ  . ARG A 1 81  ? 13.489  22.181  -17.826 1.00   77.01  ? 96  ARG A CZ  1 
ATOM   342  N  NH1 . ARG A 1 81  ? 12.822  21.459  -18.717 1.00   82.28  ? 96  ARG A NH1 1 
ATOM   343  N  NH2 . ARG A 1 81  ? 14.297  23.141  -18.248 1.00   82.97  ? 96  ARG A NH2 1 
ATOM   344  N  N   . GLY A 1 82  ? 14.153  18.898  -10.338 1.00   49.73  ? 97  GLY A N   1 
ATOM   345  C  CA  . GLY A 1 82  ? 13.725  18.180  -9.159  1.00   48.93  ? 97  GLY A CA  1 
ATOM   346  C  C   . GLY A 1 82  ? 12.741  18.953  -8.302  1.00   50.19  ? 97  GLY A C   1 
ATOM   347  O  O   . GLY A 1 82  ? 11.791  18.371  -7.774  1.00   51.51  ? 97  GLY A O   1 
ATOM   348  N  N   . ARG A 1 83  ? 12.953  20.258  -8.171  1.00   51.53  ? 98  ARG A N   1 
ATOM   349  C  CA  . ARG A 1 83  ? 12.131  21.092  -7.301  1.00   53.86  ? 98  ARG A CA  1 
ATOM   350  C  C   . ARG A 1 83  ? 10.724  21.310  -7.857  1.00   53.38  ? 98  ARG A C   1 
ATOM   351  O  O   . ARG A 1 83  ? 9.730   21.266  -7.134  1.00   53.16  ? 98  ARG A O   1 
ATOM   352  C  CB  . ARG A 1 83  ? 12.817  22.432  -7.081  1.00   58.44  ? 98  ARG A CB  1 
ATOM   353  C  CG  . ARG A 1 83  ? 14.180  22.327  -6.408  1.00   62.59  ? 98  ARG A CG  1 
ATOM   354  C  CD  . ARG A 1 83  ? 14.698  23.689  -5.963  1.00   68.74  ? 98  ARG A CD  1 
ATOM   355  N  NE  . ARG A 1 83  ? 15.459  24.385  -7.006  1.00   76.31  ? 98  ARG A NE  1 
ATOM   356  C  CZ  . ARG A 1 83  ? 14.956  25.202  -7.936  1.00   86.41  ? 98  ARG A CZ  1 
ATOM   357  N  NH1 . ARG A 1 83  ? 13.643  25.470  -7.999  1.00   94.77  ? 98  ARG A NH1 1 
ATOM   358  N  NH2 . ARG A 1 83  ? 15.777  25.759  -8.829  1.00   86.08  ? 98  ARG A NH2 1 
ATOM   359  N  N   . GLU A 1 84  ? 10.643  21.514  -9.162  1.00   52.95  ? 99  GLU A N   1 
ATOM   360  C  CA  . GLU A 1 84  ? 9.360   21.706  -9.826  1.00   51.56  ? 99  GLU A CA  1 
ATOM   361  C  C   . GLU A 1 84  ? 8.417   20.501  -9.673  1.00   48.53  ? 99  GLU A C   1 
ATOM   362  O  O   . GLU A 1 84  ? 7.191   20.652  -9.542  1.00   48.85  ? 99  GLU A O   1 
ATOM   363  C  CB  . GLU A 1 84  ? 9.590   22.013  -11.310 1.00   53.17  ? 99  GLU A CB  1 
ATOM   364  C  CG  . GLU A 1 84  ? 10.161  23.396  -11.569 1.00   55.32  ? 99  GLU A CG  1 
ATOM   365  C  CD  . GLU A 1 84  ? 11.676  23.399  -11.635 1.00   58.11  ? 99  GLU A CD  1 
ATOM   366  O  OE1 . GLU A 1 84  ? 12.359  23.021  -10.645 1.00   56.11  ? 99  GLU A OE1 1 
ATOM   367  O  OE2 . GLU A 1 84  ? 12.187  23.778  -12.710 1.00   63.10  ? 99  GLU A OE2 1 
ATOM   368  N  N   . PHE A 1 85  ? 9.001   19.310  -9.697  1.00   44.68  ? 100 PHE A N   1 
ATOM   369  C  CA  . PHE A 1 85  ? 8.249   18.081  -9.758  1.00   42.07  ? 100 PHE A CA  1 
ATOM   370  C  C   . PHE A 1 85  ? 8.280   17.388  -8.410  1.00   39.25  ? 100 PHE A C   1 
ATOM   371  O  O   . PHE A 1 85  ? 8.075   16.188  -8.332  1.00   36.21  ? 100 PHE A O   1 
ATOM   372  C  CB  . PHE A 1 85  ? 8.861   17.160  -10.815 1.00   42.96  ? 100 PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 85  ? 8.579   17.567  -12.239 1.00   44.79  ? 100 PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 85  ? 7.307   17.495  -12.751 1.00   45.02  ? 100 PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 85  ? 9.606   17.968  -13.079 1.00   46.67  ? 100 PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 85  ? 7.045   17.836  -14.066 1.00   46.66  ? 100 PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 85  ? 9.357   18.305  -14.396 1.00   47.29  ? 100 PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 85  ? 8.067   18.241  -14.894 1.00   47.64  ? 100 PHE A CZ  1 
ATOM   379  N  N   . ALA A 1 86  ? 8.515   18.157  -7.349  1.00   39.17  ? 101 ALA A N   1 
ATOM   380  C  CA  . ALA A 1 86  ? 8.676   17.612  -5.982  1.00   38.42  ? 101 ALA A CA  1 
ATOM   381  C  C   . ALA A 1 86  ? 7.384   17.611  -5.159  1.00   37.41  ? 101 ALA A C   1 
ATOM   382  O  O   . ALA A 1 86  ? 7.419   17.577  -3.902  1.00   36.80  ? 101 ALA A O   1 
ATOM   383  C  CB  . ALA A 1 86  ? 9.776   18.382  -5.235  1.00   39.04  ? 101 ALA A CB  1 
ATOM   384  N  N   . GLY A 1 87  ? 6.249   17.618  -5.861  1.00   36.12  ? 102 GLY A N   1 
ATOM   385  C  CA  . GLY A 1 87  ? 4.950   17.649  -5.202  1.00   35.40  ? 102 GLY A CA  1 
ATOM   386  C  C   . GLY A 1 87  ? 4.465   16.240  -5.082  1.00   33.59  ? 102 GLY A C   1 
ATOM   387  O  O   . GLY A 1 87  ? 4.963   15.380  -5.784  1.00   32.88  ? 102 GLY A O   1 
ATOM   388  N  N   . ARG A 1 88  ? 3.505   16.006  -4.191  1.00   33.40  ? 103 ARG A N   1 
ATOM   389  C  CA  . ARG A 1 88  ? 2.841   14.693  -4.045  1.00   32.72  ? 103 ARG A CA  1 
ATOM   390  C  C   . ARG A 1 88  ? 1.327   14.811  -4.117  1.00   34.06  ? 103 ARG A C   1 
ATOM   391  O  O   . ARG A 1 88  ? 0.737   15.872  -3.903  1.00   34.68  ? 103 ARG A O   1 
ATOM   392  C  CB  . ARG A 1 88  ? 3.237   14.004  -2.741  1.00   31.37  ? 103 ARG A CB  1 
ATOM   393  C  CG  . ARG A 1 88  ? 4.713   13.682  -2.621  1.00   30.08  ? 103 ARG A CG  1 
ATOM   394  C  CD  . ARG A 1 88  ? 5.194   12.689  -3.659  1.00   29.07  ? 103 ARG A CD  1 
ATOM   395  N  NE  . ARG A 1 88  ? 6.370   11.976  -3.183  1.00   28.00  ? 103 ARG A NE  1 
ATOM   396  C  CZ  . ARG A 1 88  ? 7.188   11.240  -3.926  1.00   27.20  ? 103 ARG A CZ  1 
ATOM   397  N  NH1 . ARG A 1 88  ? 7.018   11.078  -5.237  1.00   27.22  ? 103 ARG A NH1 1 
ATOM   398  N  NH2 . ARG A 1 88  ? 8.187   10.627  -3.333  1.00   26.86  ? 103 ARG A NH2 1 
ATOM   399  N  N   . PRO A 1 89  ? 0.683   13.713  -4.438  1.00   35.96  ? 104 PRO A N   1 
ATOM   400  C  CA  . PRO A 1 89  ? -0.750  13.753  -4.683  1.00   38.75  ? 104 PRO A CA  1 
ATOM   401  C  C   . PRO A 1 89  ? -1.515  13.455  -3.411  1.00   41.02  ? 104 PRO A C   1 
ATOM   402  O  O   . PRO A 1 89  ? -1.072  12.638  -2.614  1.00   40.99  ? 104 PRO A O   1 
ATOM   403  C  CB  . PRO A 1 89  ? -0.929  12.636  -5.702  1.00   38.47  ? 104 PRO A CB  1 
ATOM   404  C  CG  . PRO A 1 89  ? 0.078   11.616  -5.260  1.00   37.12  ? 104 PRO A CG  1 
ATOM   405  C  CD  . PRO A 1 89  ? 1.253   12.392  -4.747  1.00   36.00  ? 104 PRO A CD  1 
ATOM   406  N  N   . LYS A 1 90  ? -2.645  14.120  -3.204  1.00   44.96  ? 105 LYS A N   1 
ATOM   407  C  CA  . LYS A 1 90  ? -3.369  13.970  -1.956  1.00   47.71  ? 105 LYS A CA  1 
ATOM   408  C  C   . LYS A 1 90  ? -4.550  13.021  -2.145  1.00   50.76  ? 105 LYS A C   1 
ATOM   409  O  O   . LYS A 1 90  ? -5.645  13.427  -2.507  1.00   51.36  ? 105 LYS A O   1 
ATOM   410  C  CB  . LYS A 1 90  ? -3.805  15.324  -1.443  1.00   48.77  ? 105 LYS A CB  1 
ATOM   411  C  CG  . LYS A 1 90  ? -4.546  15.222  -0.122  1.00   51.07  ? 105 LYS A CG  1 
ATOM   412  C  CD  . LYS A 1 90  ? -5.396  16.453  0.164   1.00   52.78  ? 105 LYS A CD  1 
ATOM   413  C  CE  . LYS A 1 90  ? -4.932  17.159  1.410   1.00   53.01  ? 105 LYS A CE  1 
ATOM   414  N  NZ  . LYS A 1 90  ? -5.148  16.243  2.570   1.00   54.29  ? 105 LYS A NZ  1 
ATOM   415  N  N   . MET A 1 91  ? -4.300  11.740  -1.908  1.00   54.73  ? 106 MET A N   1 
ATOM   416  C  CA  . MET A 1 91  ? -5.314  10.715  -2.063  1.00   59.31  ? 106 MET A CA  1 
ATOM   417  C  C   . MET A 1 91  ? -5.948  10.555  -0.688  1.00   61.50  ? 106 MET A C   1 
ATOM   418  O  O   . MET A 1 91  ? -5.450  11.107  0.303   1.00   62.81  ? 106 MET A O   1 
ATOM   419  C  CB  . MET A 1 91  ? -4.689  9.395   -2.524  1.00   62.65  ? 106 MET A CB  1 
ATOM   420  C  CG  . MET A 1 91  ? -3.810  9.486   -3.778  1.00   65.64  ? 106 MET A CG  1 
ATOM   421  S  SD  . MET A 1 91  ? -2.690  8.067   -3.922  1.00   70.33  ? 106 MET A SD  1 
ATOM   422  C  CE  . MET A 1 91  ? -1.635  8.489   -5.322  1.00   70.32  ? 106 MET A CE  1 
ATOM   423  N  N   . VAL A 1 92  ? -7.047  9.807   -0.614  1.00   60.38  ? 107 VAL A N   1 
ATOM   424  C  CA  . VAL A 1 92  ? -7.705  9.576   0.671   1.00   57.62  ? 107 VAL A CA  1 
ATOM   425  C  C   . VAL A 1 92  ? -7.103  8.439   1.488   1.00   53.69  ? 107 VAL A C   1 
ATOM   426  O  O   . VAL A 1 92  ? -7.087  8.528   2.698   1.00   53.90  ? 107 VAL A O   1 
ATOM   427  C  CB  . VAL A 1 92  ? -9.218  9.369   0.492   1.00   60.46  ? 107 VAL A CB  1 
ATOM   428  C  CG1 . VAL A 1 92  ? -9.853  8.618   1.665   1.00   60.65  ? 107 VAL A CG1 1 
ATOM   429  C  CG2 . VAL A 1 92  ? -9.887  10.721  0.349   1.00   64.28  ? 107 VAL A CG2 1 
ATOM   430  N  N   . THR A 1 93  ? -6.662  7.360   0.857   1.00   50.58  ? 108 THR A N   1 
ATOM   431  C  CA  . THR A 1 93  ? -5.927  6.350   1.578   1.00   51.30  ? 108 THR A CA  1 
ATOM   432  C  C   . THR A 1 93  ? -4.717  7.022   2.256   1.00   50.21  ? 108 THR A C   1 
ATOM   433  O  O   . THR A 1 93  ? -4.553  6.945   3.469   1.00   48.86  ? 108 THR A O   1 
ATOM   434  C  CB  . THR A 1 93  ? -5.397  5.269   0.636   1.00   52.81  ? 108 THR A CB  1 
ATOM   435  O  OG1 . THR A 1 93  ? -4.669  5.896   -0.426  1.00   57.16  ? 108 THR A OG1 1 
ATOM   436  C  CG2 . THR A 1 93  ? -6.510  4.467   0.051   1.00   54.38  ? 108 THR A CG2 1 
ATOM   437  N  N   . THR A 1 94  ? -3.904  7.715   1.458   1.00   47.66  ? 109 THR A N   1 
ATOM   438  C  CA  . THR A 1 94  ? -2.707  8.368   1.950   1.00   45.93  ? 109 THR A CA  1 
ATOM   439  C  C   . THR A 1 94  ? -3.006  9.293   3.107   1.00   45.38  ? 109 THR A C   1 
ATOM   440  O  O   . THR A 1 94  ? -2.309  9.277   4.123   1.00   45.96  ? 109 THR A O   1 
ATOM   441  C  CB  . THR A 1 94  ? -1.957  9.169   0.853   1.00   46.00  ? 109 THR A CB  1 
ATOM   442  O  OG1 . THR A 1 94  ? -2.784  10.191  0.276   1.00   46.80  ? 109 THR A OG1 1 
ATOM   443  C  CG2 . THR A 1 94  ? -1.481  8.251   -0.231  1.00   46.01  ? 109 THR A CG2 1 
ATOM   444  N  N   . ASP A 1 95  ? -4.022  10.118  2.958   1.00   45.74  ? 110 ASP A N   1 
ATOM   445  C  CA  . ASP A 1 95  ? -4.445  10.988  4.065   1.00   47.26  ? 110 ASP A CA  1 
ATOM   446  C  C   . ASP A 1 95  ? -4.652  10.210  5.381   1.00   48.16  ? 110 ASP A C   1 
ATOM   447  O  O   . ASP A 1 95  ? -4.181  10.630  6.451   1.00   48.57  ? 110 ASP A O   1 
ATOM   448  C  CB  . ASP A 1 95  ? -5.729  11.730  3.697   1.00   48.44  ? 110 ASP A CB  1 
ATOM   449  C  CG  . ASP A 1 95  ? -5.471  13.029  3.006   1.00   48.08  ? 110 ASP A CG  1 
ATOM   450  O  OD1 . ASP A 1 95  ? -4.299  13.448  2.943   1.00   48.65  ? 110 ASP A OD1 1 
ATOM   451  O  OD2 . ASP A 1 95  ? -6.445  13.661  2.556   1.00   48.63  ? 110 ASP A OD2 1 
ATOM   452  N  N   . LEU A 1 96  ? -5.337  9.073   5.299   1.00   47.61  ? 111 LEU A N   1 
ATOM   453  C  CA  . LEU A 1 96  ? -5.513  8.233   6.472   1.00   48.58  ? 111 LEU A CA  1 
ATOM   454  C  C   . LEU A 1 96  ? -4.169  7.804   7.022   1.00   46.35  ? 111 LEU A C   1 
ATOM   455  O  O   . LEU A 1 96  ? -3.909  7.870   8.217   1.00   46.73  ? 111 LEU A O   1 
ATOM   456  C  CB  . LEU A 1 96  ? -6.322  6.985   6.129   1.00   49.91  ? 111 LEU A CB  1 
ATOM   457  C  CG  . LEU A 1 96  ? -7.775  7.188   5.703   1.00   52.76  ? 111 LEU A CG  1 
ATOM   458  C  CD1 . LEU A 1 96  ? -8.391  5.842   5.334   1.00   53.25  ? 111 LEU A CD1 1 
ATOM   459  C  CD2 . LEU A 1 96  ? -8.586  7.896   6.796   1.00   54.26  ? 111 LEU A CD2 1 
ATOM   460  N  N   . LEU A 1 97  ? -3.336  7.334   6.118   1.00   44.79  ? 112 LEU A N   1 
ATOM   461  C  CA  . LEU A 1 97  ? -2.023  6.834   6.453   1.00   44.47  ? 112 LEU A CA  1 
ATOM   462  C  C   . LEU A 1 97  ? -1.110  7.831   7.175   1.00   42.63  ? 112 LEU A C   1 
ATOM   463  O  O   . LEU A 1 97  ? -0.393  7.460   8.100   1.00   40.89  ? 112 LEU A O   1 
ATOM   464  C  CB  . LEU A 1 97  ? -1.316  6.362   5.183   1.00   44.43  ? 112 LEU A CB  1 
ATOM   465  C  CG  . LEU A 1 97  ? -1.147  4.859   5.015   1.00   45.85  ? 112 LEU A CG  1 
ATOM   466  C  CD1 . LEU A 1 97  ? -2.302  4.064   5.592   1.00   47.38  ? 112 LEU A CD1 1 
ATOM   467  C  CD2 . LEU A 1 97  ? -0.977  4.577   3.524   1.00   46.58  ? 112 LEU A CD2 1 
ATOM   468  N  N   . THR A 1 98  ? -1.165  9.081   6.740   1.00   40.80  ? 113 THR A N   1 
ATOM   469  C  CA  . THR A 1 98  ? -0.169  10.059  7.095   1.00   38.97  ? 113 THR A CA  1 
ATOM   470  C  C   . THR A 1 98  ? -0.833  11.146  7.915   1.00   39.71  ? 113 THR A C   1 
ATOM   471  O  O   . THR A 1 98  ? -0.332  12.257  8.015   1.00   40.04  ? 113 THR A O   1 
ATOM   472  C  CB  . THR A 1 98  ? 0.488   10.641  5.801   1.00   37.24  ? 113 THR A CB  1 
ATOM   473  O  OG1 . THR A 1 98  ? -0.481  11.345  5.015   1.00   36.25  ? 113 THR A OG1 1 
ATOM   474  C  CG2 . THR A 1 98  ? 1.062   9.529   4.961   1.00   35.92  ? 113 THR A CG2 1 
ATOM   475  N  N   . GLN A 1 99  ? -1.982  10.837  8.491   1.00   41.02  ? 114 GLN A N   1 
ATOM   476  C  CA  . GLN A 1 99  ? -2.742  11.834  9.204   1.00   42.16  ? 114 GLN A CA  1 
ATOM   477  C  C   . GLN A 1 99  ? -2.743  13.117  8.410   1.00   41.57  ? 114 GLN A C   1 
ATOM   478  O  O   . GLN A 1 99  ? -2.317  14.155  8.893   1.00   41.45  ? 114 GLN A O   1 
ATOM   479  C  CB  . GLN A 1 99  ? -2.097  12.057  10.542  1.00   43.58  ? 114 GLN A CB  1 
ATOM   480  C  CG  . GLN A 1 99  ? -3.034  12.436  11.658  1.00   45.96  ? 114 GLN A CG  1 
ATOM   481  C  CD  . GLN A 1 99  ? -2.357  12.209  12.997  1.00   47.25  ? 114 GLN A CD  1 
ATOM   482  O  OE1 . GLN A 1 99  ? -1.916  11.091  13.308  1.00   45.63  ? 114 GLN A OE1 1 
ATOM   483  N  NE2 . GLN A 1 99  ? -2.245  13.272  13.787  1.00   49.06  ? 114 GLN A NE2 1 
ATOM   484  N  N   . GLY A 1 100 ? -3.201  13.026  7.168   1.00   41.23  ? 115 GLY A N   1 
ATOM   485  C  CA  . GLY A 1 100 ? -3.334  14.188  6.308   1.00   41.52  ? 115 GLY A CA  1 
ATOM   486  C  C   . GLY A 1 100 ? -2.021  14.719  5.751   1.00   40.80  ? 115 GLY A C   1 
ATOM   487  O  O   . GLY A 1 100 ? -1.806  15.921  5.745   1.00   42.34  ? 115 GLY A O   1 
ATOM   488  N  N   . GLY A 1 101 ? -1.138  13.849  5.280   1.00   39.12  ? 116 GLY A N   1 
ATOM   489  C  CA  . GLY A 1 101 ? 0.070   14.319  4.629   1.00   38.62  ? 116 GLY A CA  1 
ATOM   490  C  C   . GLY A 1 101 ? 1.123   14.931  5.548   1.00   39.46  ? 116 GLY A C   1 
ATOM   491  O  O   . GLY A 1 101 ? 1.931   15.775  5.113   1.00   39.01  ? 116 GLY A O   1 
ATOM   492  N  N   . LYS A 1 102 ? 1.150   14.485  6.808   1.00   39.92  ? 117 LYS A N   1 
ATOM   493  C  CA  . LYS A 1 102 ? 2.183   14.918  7.765   1.00   39.64  ? 117 LYS A CA  1 
ATOM   494  C  C   . LYS A 1 102 ? 3.436   14.025  7.785   1.00   36.86  ? 117 LYS A C   1 
ATOM   495  O  O   . LYS A 1 102 ? 4.329   14.238  8.591   1.00   36.81  ? 117 LYS A O   1 
ATOM   496  C  CB  . LYS A 1 102 ? 1.583   15.002  9.161   1.00   42.07  ? 117 LYS A CB  1 
ATOM   497  C  CG  . LYS A 1 102 ? 0.485   16.034  9.278   1.00   44.64  ? 117 LYS A CG  1 
ATOM   498  C  CD  . LYS A 1 102 ? 0.111   16.235  10.736  1.00   47.75  ? 117 LYS A CD  1 
ATOM   499  C  CE  . LYS A 1 102 ? -0.790  17.445  10.938  1.00   50.16  ? 117 LYS A CE  1 
ATOM   500  N  NZ  . LYS A 1 102 ? -2.122  17.241  10.314  1.00   51.55  ? 117 LYS A NZ  1 
ATOM   501  N  N   . ASP A 1 103 ? 3.530   13.039  6.901   1.00   34.38  ? 118 ASP A N   1 
ATOM   502  C  CA  . ASP A 1 103 ? 4.725   12.204  6.860   1.00   32.66  ? 118 ASP A CA  1 
ATOM   503  C  C   . ASP A 1 103 ? 5.787   12.865  5.988   1.00   32.34  ? 118 ASP A C   1 
ATOM   504  O  O   . ASP A 1 103 ? 5.790   14.077  5.814   1.00   32.42  ? 118 ASP A O   1 
ATOM   505  C  CB  . ASP A 1 103 ? 4.359   10.807  6.358   1.00   31.70  ? 118 ASP A CB  1 
ATOM   506  C  CG  . ASP A 1 103 ? 4.019   10.791  4.920   1.00   30.89  ? 118 ASP A CG  1 
ATOM   507  O  OD1 . ASP A 1 103 ? 3.642   11.861  4.433   1.00   31.35  ? 118 ASP A OD1 1 
ATOM   508  O  OD2 . ASP A 1 103 ? 4.140   9.743   4.258   1.00   29.66  ? 118 ASP A OD2 1 
ATOM   509  N  N   . ILE A 1 104 ? 6.694   12.071  5.437   1.00   32.53  ? 119 ILE A N   1 
ATOM   510  C  CA  . ILE A 1 104 ? 7.605   12.539  4.382   1.00   33.03  ? 119 ILE A CA  1 
ATOM   511  C  C   . ILE A 1 104 ? 7.192   12.157  2.940   1.00   32.67  ? 119 ILE A C   1 
ATOM   512  O  O   . ILE A 1 104 ? 7.244   12.988  2.015   1.00   33.13  ? 119 ILE A O   1 
ATOM   513  C  CB  . ILE A 1 104 ? 9.014   11.971  4.615   1.00   32.94  ? 119 ILE A CB  1 
ATOM   514  C  CG1 . ILE A 1 104 ? 9.580   12.506  5.926   1.00   33.51  ? 119 ILE A CG1 1 
ATOM   515  C  CG2 . ILE A 1 104 ? 9.927   12.275  3.416   1.00   32.65  ? 119 ILE A CG2 1 
ATOM   516  C  CD1 . ILE A 1 104 ? 9.737   14.016  5.954   1.00   34.22  ? 119 ILE A CD1 1 
ATOM   517  N  N   . ALA A 1 105 ? 6.808   10.906  2.746   1.00   32.41  ? 120 ALA A N   1 
ATOM   518  C  CA  . ALA A 1 105 ? 6.624   10.370  1.391   1.00   32.64  ? 120 ALA A CA  1 
ATOM   519  C  C   . ALA A 1 105 ? 5.448   11.018  0.632   1.00   32.99  ? 120 ALA A C   1 
ATOM   520  O  O   . ALA A 1 105 ? 5.588   11.385  -0.532  1.00   32.16  ? 120 ALA A O   1 
ATOM   521  C  CB  . ALA A 1 105 ? 6.485   8.844   1.434   1.00   32.06  ? 120 ALA A CB  1 
ATOM   522  N  N   . PHE A 1 106 ? 4.324   11.185  1.313   1.00   33.75  ? 121 PHE A N   1 
ATOM   523  C  CA  . PHE A 1 106 ? 3.133   11.724  0.690   1.00   35.16  ? 121 PHE A CA  1 
ATOM   524  C  C   . PHE A 1 106 ? 2.828   13.177  1.031   1.00   37.05  ? 121 PHE A C   1 
ATOM   525  O  O   . PHE A 1 106 ? 1.675   13.612  0.887   1.00   38.80  ? 121 PHE A O   1 
ATOM   526  C  CB  . PHE A 1 106 ? 1.956   10.823  1.034   1.00   35.48  ? 121 PHE A CB  1 
ATOM   527  C  CG  . PHE A 1 106 ? 2.099   9.450   0.455   1.00   35.05  ? 121 PHE A CG  1 
ATOM   528  C  CD1 . PHE A 1 106 ? 1.924   9.243   -0.883  1.00   34.81  ? 121 PHE A CD1 1 
ATOM   529  C  CD2 . PHE A 1 106 ? 2.458   8.389   1.246   1.00   35.94  ? 121 PHE A CD2 1 
ATOM   530  C  CE1 . PHE A 1 106 ? 2.080   7.992   -1.430  1.00   35.29  ? 121 PHE A CE1 1 
ATOM   531  C  CE2 . PHE A 1 106 ? 2.639   7.132   0.722   1.00   35.76  ? 121 PHE A CE2 1 
ATOM   532  C  CZ  . PHE A 1 106 ? 2.429   6.930   -0.626  1.00   36.20  ? 121 PHE A CZ  1 
ATOM   533  N  N   . ALA A 1 107 ? 3.841   13.938  1.452   1.00   37.40  ? 122 ALA A N   1 
ATOM   534  C  CA  . ALA A 1 107 ? 3.660   15.365  1.672   1.00   38.48  ? 122 ALA A CA  1 
ATOM   535  C  C   . ALA A 1 107 ? 4.301   16.196  0.554   1.00   39.79  ? 122 ALA A C   1 
ATOM   536  O  O   . ALA A 1 107 ? 5.259   15.765  -0.065  1.00   37.98  ? 122 ALA A O   1 
ATOM   537  C  CB  . ALA A 1 107 ? 4.252   15.747  2.996   1.00   39.06  ? 122 ALA A CB  1 
ATOM   538  N  N   . ASP A 1 108 ? 3.770   17.398  0.333   1.00   42.34  ? 123 ASP A N   1 
ATOM   539  C  CA  . ASP A 1 108 ? 4.256   18.319  -0.686  1.00   43.92  ? 123 ASP A CA  1 
ATOM   540  C  C   . ASP A 1 108 ? 5.535   18.991  -0.246  1.00   46.05  ? 123 ASP A C   1 
ATOM   541  O  O   . ASP A 1 108 ? 5.716   19.235  0.941   1.00   51.03  ? 123 ASP A O   1 
ATOM   542  C  CB  . ASP A 1 108 ? 3.208   19.428  -0.951  1.00   45.84  ? 123 ASP A CB  1 
ATOM   543  C  CG  . ASP A 1 108 ? 2.348   19.183  -2.217  1.00   45.49  ? 123 ASP A CG  1 
ATOM   544  O  OD1 . ASP A 1 108 ? 2.604   18.236  -2.975  1.00   45.53  ? 123 ASP A OD1 1 
ATOM   545  O  OD2 . ASP A 1 108 ? 1.410   19.966  -2.454  1.00   46.26  ? 123 ASP A OD2 1 
ATOM   546  N  N   . TYR A 1 109 ? 6.410   19.302  -1.202  1.00   47.58  ? 124 TYR A N   1 
ATOM   547  C  CA  . TYR A 1 109 ? 7.632   20.089  -0.968  1.00   48.02  ? 124 TYR A CA  1 
ATOM   548  C  C   . TYR A 1 109 ? 7.293   21.476  -0.475  1.00   49.35  ? 124 TYR A C   1 
ATOM   549  O  O   . TYR A 1 109 ? 6.472   22.159  -1.090  1.00   51.28  ? 124 TYR A O   1 
ATOM   550  C  CB  . TYR A 1 109 ? 8.388   20.234  -2.275  1.00   48.98  ? 124 TYR A CB  1 
ATOM   551  C  CG  . TYR A 1 109 ? 9.709   20.960  -2.209  1.00   50.56  ? 124 TYR A CG  1 
ATOM   552  C  CD1 . TYR A 1 109 ? 9.788   22.335  -2.409  1.00   52.88  ? 124 TYR A CD1 1 
ATOM   553  C  CD2 . TYR A 1 109 ? 10.893  20.258  -2.004  1.00   50.28  ? 124 TYR A CD2 1 
ATOM   554  C  CE1 . TYR A 1 109 ? 11.008  22.993  -2.360  1.00   53.91  ? 124 TYR A CE1 1 
ATOM   555  C  CE2 . TYR A 1 109 ? 12.116  20.901  -1.973  1.00   51.55  ? 124 TYR A CE2 1 
ATOM   556  C  CZ  . TYR A 1 109 ? 12.168  22.264  -2.154  1.00   53.63  ? 124 TYR A CZ  1 
ATOM   557  O  OH  . TYR A 1 109 ? 13.390  22.886  -2.121  1.00   56.77  ? 124 TYR A OH  1 
ATOM   558  N  N   . SER A 1 110 ? 7.950   21.911  0.599   1.00   48.65  ? 125 SER A N   1 
ATOM   559  C  CA  . SER A 1 110 ? 7.555   23.123  1.302   1.00   49.62  ? 125 SER A CA  1 
ATOM   560  C  C   . SER A 1 110 ? 8.516   23.424  2.422   1.00   51.57  ? 125 SER A C   1 
ATOM   561  O  O   . SER A 1 110 ? 9.178   22.506  2.942   1.00   52.98  ? 125 SER A O   1 
ATOM   562  C  CB  . SER A 1 110 ? 6.180   22.920  1.960   1.00   49.87  ? 125 SER A CB  1 
ATOM   563  O  OG  . SER A 1 110 ? 6.204   21.833  2.880   1.00   47.66  ? 125 SER A OG  1 
ATOM   564  N  N   . PRO A 1 111 ? 8.548   24.691  2.867   1.00   51.46  ? 126 PRO A N   1 
ATOM   565  C  CA  . PRO A 1 111 ? 9.333   25.070  4.042   1.00   51.26  ? 126 PRO A CA  1 
ATOM   566  C  C   . PRO A 1 111 ? 9.239   24.073  5.201   1.00   50.22  ? 126 PRO A C   1 
ATOM   567  O  O   . PRO A 1 111 ? 10.262  23.712  5.793   1.00   50.57  ? 126 PRO A O   1 
ATOM   568  C  CB  . PRO A 1 111 ? 8.725   26.403  4.439   1.00   52.50  ? 126 PRO A CB  1 
ATOM   569  C  CG  . PRO A 1 111 ? 8.260   26.993  3.158   1.00   52.73  ? 126 PRO A CG  1 
ATOM   570  C  CD  . PRO A 1 111 ? 7.888   25.853  2.254   1.00   51.74  ? 126 PRO A CD  1 
ATOM   571  N  N   . LEU A 1 112 ? 8.027   23.616  5.496   1.00   49.19  ? 127 LEU A N   1 
ATOM   572  C  CA  . LEU A 1 112 ? 7.799   22.711  6.616   1.00   48.14  ? 127 LEU A CA  1 
ATOM   573  C  C   . LEU A 1 112 ? 8.397   21.371  6.307   1.00   46.89  ? 127 LEU A C   1 
ATOM   574  O  O   . LEU A 1 112 ? 8.952   20.705  7.182   1.00   47.82  ? 127 LEU A O   1 
ATOM   575  C  CB  . LEU A 1 112 ? 6.306   22.558  6.880   1.00   48.53  ? 127 LEU A CB  1 
ATOM   576  C  CG  . LEU A 1 112 ? 5.794   21.536  7.896   1.00   48.66  ? 127 LEU A CG  1 
ATOM   577  C  CD1 . LEU A 1 112 ? 6.444   21.682  9.267   1.00   50.33  ? 127 LEU A CD1 1 
ATOM   578  C  CD2 . LEU A 1 112 ? 4.282   21.694  8.044   1.00   49.30  ? 127 LEU A CD2 1 
ATOM   579  N  N   . TRP A 1 113 ? 8.299   20.974  5.048   1.00   45.98  ? 128 TRP A N   1 
ATOM   580  C  CA  . TRP A 1 113 ? 8.759   19.648  4.641   1.00   44.51  ? 128 TRP A CA  1 
ATOM   581  C  C   . TRP A 1 113 ? 10.295  19.599  4.529   1.00   46.09  ? 128 TRP A C   1 
ATOM   582  O  O   . TRP A 1 113 ? 10.909  18.564  4.785   1.00   46.06  ? 128 TRP A O   1 
ATOM   583  C  CB  . TRP A 1 113 ? 8.054   19.222  3.337   1.00   41.93  ? 128 TRP A CB  1 
ATOM   584  C  CG  . TRP A 1 113 ? 8.460   17.899  2.833   1.00   38.42  ? 128 TRP A CG  1 
ATOM   585  C  CD1 . TRP A 1 113 ? 7.839   16.723  3.042   1.00   37.43  ? 128 TRP A CD1 1 
ATOM   586  C  CD2 . TRP A 1 113 ? 9.590   17.625  2.009   1.00   37.08  ? 128 TRP A CD2 1 
ATOM   587  N  NE1 . TRP A 1 113 ? 8.506   15.707  2.385   1.00   36.35  ? 128 TRP A NE1 1 
ATOM   588  C  CE2 . TRP A 1 113 ? 9.597   16.244  1.754   1.00   36.20  ? 128 TRP A CE2 1 
ATOM   589  C  CE3 . TRP A 1 113 ? 10.604  18.419  1.454   1.00   36.55  ? 128 TRP A CE3 1 
ATOM   590  C  CZ2 . TRP A 1 113 ? 10.597  15.636  0.995   1.00   34.96  ? 128 TRP A CZ2 1 
ATOM   591  C  CZ3 . TRP A 1 113 ? 11.564  17.818  0.680   1.00   35.35  ? 128 TRP A CZ3 1 
ATOM   592  C  CH2 . TRP A 1 113 ? 11.568  16.446  0.470   1.00   34.42  ? 128 TRP A CH2 1 
ATOM   593  N  N   . LYS A 1 114 ? 10.917  20.709  4.152   1.00   49.18  ? 129 LYS A N   1 
ATOM   594  C  CA  . LYS A 1 114 ? 12.380  20.760  4.128   1.00   51.30  ? 129 LYS A CA  1 
ATOM   595  C  C   . LYS A 1 114 ? 12.990  20.651  5.548   1.00   51.88  ? 129 LYS A C   1 
ATOM   596  O  O   . LYS A 1 114 ? 13.926  19.886  5.761   1.00   52.95  ? 129 LYS A O   1 
ATOM   597  C  CB  . LYS A 1 114 ? 12.888  22.021  3.426   1.00   53.43  ? 129 LYS A CB  1 
ATOM   598  C  CG  . LYS A 1 114 ? 12.201  22.352  2.112   1.00   54.40  ? 129 LYS A CG  1 
ATOM   599  C  CD  . LYS A 1 114 ? 13.162  22.987  1.131   1.00   57.10  ? 129 LYS A CD  1 
ATOM   600  C  CE  . LYS A 1 114 ? 13.762  24.286  1.645   1.00   62.04  ? 129 LYS A CE  1 
ATOM   601  N  NZ  . LYS A 1 114 ? 13.028  25.491  1.171   1.00   65.64  ? 129 LYS A NZ  1 
ATOM   602  N  N   . ASN A 1 115 ? 12.465  21.393  6.520   1.00   52.43  ? 130 ASN A N   1 
ATOM   603  C  CA  . ASN A 1 115 ? 12.967  21.274  7.901   1.00   52.68  ? 130 ASN A CA  1 
ATOM   604  C  C   . ASN A 1 115 ? 12.719  19.888  8.452   1.00   50.36  ? 130 ASN A C   1 
ATOM   605  O  O   . ASN A 1 115 ? 13.535  19.321  9.171   1.00   47.81  ? 130 ASN A O   1 
ATOM   606  C  CB  . ASN A 1 115 ? 12.304  22.295  8.811   1.00   54.70  ? 130 ASN A CB  1 
ATOM   607  C  CG  . ASN A 1 115 ? 12.545  23.711  8.347   1.00   57.63  ? 130 ASN A CG  1 
ATOM   608  O  OD1 . ASN A 1 115 ? 13.560  23.991  7.712   1.00   60.10  ? 130 ASN A OD1 1 
ATOM   609  N  ND2 . ASN A 1 115 ? 11.609  24.612  8.643   1.00   59.42  ? 130 ASN A ND2 1 
ATOM   610  N  N   . HIS A 1 116 ? 11.569  19.346  8.085   1.00   49.34  ? 131 HIS A N   1 
ATOM   611  C  CA  . HIS A 1 116 ? 11.141  18.063  8.595   1.00   47.11  ? 131 HIS A CA  1 
ATOM   612  C  C   . HIS A 1 116 ? 12.088  16.989  8.111   1.00   45.54  ? 131 HIS A C   1 
ATOM   613  O  O   . HIS A 1 116 ? 12.537  16.156  8.906   1.00   44.93  ? 131 HIS A O   1 
ATOM   614  C  CB  . HIS A 1 116 ? 9.675   17.787  8.198   1.00   45.09  ? 131 HIS A CB  1 
ATOM   615  C  CG  . HIS A 1 116 ? 9.158   16.475  8.686   1.00   43.05  ? 131 HIS A CG  1 
ATOM   616  N  ND1 . HIS A 1 116 ? 7.979   15.931  8.238   1.00   42.16  ? 131 HIS A ND1 1 
ATOM   617  C  CD2 . HIS A 1 116 ? 9.670   15.587  9.566   1.00   42.68  ? 131 HIS A CD2 1 
ATOM   618  C  CE1 . HIS A 1 116 ? 7.790   14.759  8.811   1.00   41.71  ? 131 HIS A CE1 1 
ATOM   619  N  NE2 . HIS A 1 116 ? 8.808   14.523  9.616   1.00   42.24  ? 131 HIS A NE2 1 
ATOM   620  N  N   . ARG A 1 117 ? 12.419  17.043  6.823   1.00   44.22  ? 132 ARG A N   1 
ATOM   621  C  CA  . ARG A 1 117 ? 13.263  16.034  6.213   1.00   43.75  ? 132 ARG A CA  1 
ATOM   622  C  C   . ARG A 1 117 ? 14.694  16.273  6.624   1.00   43.96  ? 132 ARG A C   1 
ATOM   623  O  O   . ARG A 1 117 ? 15.413  15.335  6.930   1.00   43.26  ? 132 ARG A O   1 
ATOM   624  C  CB  . ARG A 1 117 ? 13.126  16.057  4.687   1.00   44.77  ? 132 ARG A CB  1 
ATOM   625  C  CG  . ARG A 1 117 ? 13.866  14.946  3.958   1.00   44.21  ? 132 ARG A CG  1 
ATOM   626  C  CD  . ARG A 1 117 ? 14.217  15.336  2.523   1.00   45.15  ? 132 ARG A CD  1 
ATOM   627  N  NE  . ARG A 1 117 ? 14.677  14.167  1.773   1.00   45.47  ? 132 ARG A NE  1 
ATOM   628  C  CZ  . ARG A 1 117 ? 15.909  13.665  1.851   1.00   46.03  ? 132 ARG A CZ  1 
ATOM   629  N  NH1 . ARG A 1 117 ? 16.835  14.215  2.635   1.00   46.40  ? 132 ARG A NH1 1 
ATOM   630  N  NH2 . ARG A 1 117 ? 16.205  12.575  1.168   1.00   46.59  ? 132 ARG A NH2 1 
ATOM   631  N  N   . ARG A 1 118 ? 15.128  17.523  6.645   1.00   45.88  ? 133 ARG A N   1 
ATOM   632  C  CA  . ARG A 1 118 ? 16.444  17.793  7.204   1.00   48.41  ? 133 ARG A CA  1 
ATOM   633  C  C   . ARG A 1 118 ? 16.553  17.139  8.589   1.00   48.34  ? 133 ARG A C   1 
ATOM   634  O  O   . ARG A 1 118 ? 17.551  16.463  8.872   1.00   47.66  ? 133 ARG A O   1 
ATOM   635  C  CB  . ARG A 1 118 ? 16.753  19.276  7.293   1.00   51.10  ? 133 ARG A CB  1 
ATOM   636  C  CG  . ARG A 1 118 ? 18.173  19.545  7.765   1.00   54.82  ? 133 ARG A CG  1 
ATOM   637  C  CD  . ARG A 1 118 ? 18.531  21.023  7.707   1.00   59.41  ? 133 ARG A CD  1 
ATOM   638  N  NE  . ARG A 1 118 ? 17.809  21.659  6.602   1.00   62.33  ? 133 ARG A NE  1 
ATOM   639  C  CZ  . ARG A 1 118 ? 16.825  22.555  6.726   1.00   65.77  ? 133 ARG A CZ  1 
ATOM   640  N  NH1 . ARG A 1 118 ? 16.433  23.008  7.928   1.00   66.29  ? 133 ARG A NH1 1 
ATOM   641  N  NH2 . ARG A 1 118 ? 16.234  23.025  5.623   1.00   66.64  ? 133 ARG A NH2 1 
ATOM   642  N  N   . LEU A 1 119 ? 15.521  17.299  9.425   1.00   47.46  ? 134 LEU A N   1 
ATOM   643  C  CA  . LEU A 1 119 ? 15.513  16.678  10.744  1.00   47.36  ? 134 LEU A CA  1 
ATOM   644  C  C   . LEU A 1 119 ? 15.598  15.188  10.635  1.00   47.07  ? 134 LEU A C   1 
ATOM   645  O  O   . LEU A 1 119 ? 16.305  14.546  11.378  1.00   47.45  ? 134 LEU A O   1 
ATOM   646  C  CB  . LEU A 1 119 ? 14.256  17.024  11.516  1.00   48.31  ? 134 LEU A CB  1 
ATOM   647  C  CG  . LEU A 1 119 ? 14.087  16.323  12.863  1.00   49.22  ? 134 LEU A CG  1 
ATOM   648  C  CD1 . LEU A 1 119 ? 15.275  16.629  13.777  1.00   50.55  ? 134 LEU A CD1 1 
ATOM   649  C  CD2 . LEU A 1 119 ? 12.775  16.755  13.506  1.00   49.40  ? 134 LEU A CD2 1 
ATOM   650  N  N   . VAL A 1 120 ? 14.858  14.613  9.710   1.00   48.56  ? 135 VAL A N   1 
ATOM   651  C  CA  . VAL A 1 120 ? 14.880  13.171  9.607   1.00   48.40  ? 135 VAL A CA  1 
ATOM   652  C  C   . VAL A 1 120 ? 16.276  12.717  9.181   1.00   50.00  ? 135 VAL A C   1 
ATOM   653  O  O   . VAL A 1 120 ? 16.919  11.931  9.882   1.00   50.37  ? 135 VAL A O   1 
ATOM   654  C  CB  . VAL A 1 120 ? 13.812  12.678  8.648   1.00   46.08  ? 135 VAL A CB  1 
ATOM   655  C  CG1 . VAL A 1 120 ? 13.930  11.186  8.451   1.00   44.94  ? 135 VAL A CG1 1 
ATOM   656  C  CG2 . VAL A 1 120 ? 12.452  13.016  9.212   1.00   47.66  ? 135 VAL A CG2 1 
ATOM   657  N  N   . HIS A 1 121 ? 16.737  13.241  8.047   1.00   51.14  ? 136 HIS A N   1 
ATOM   658  C  CA  . HIS A 1 121 ? 17.974  12.796  7.413   1.00   51.16  ? 136 HIS A CA  1 
ATOM   659  C  C   . HIS A 1 121 ? 19.131  12.722  8.394   1.00   50.22  ? 136 HIS A C   1 
ATOM   660  O  O   . HIS A 1 121 ? 19.874  11.743  8.423   1.00   49.23  ? 136 HIS A O   1 
ATOM   661  C  CB  . HIS A 1 121 ? 18.346  13.748  6.280   1.00   53.77  ? 136 HIS A CB  1 
ATOM   662  C  CG  . HIS A 1 121 ? 19.735  13.548  5.767   1.00   54.46  ? 136 HIS A CG  1 
ATOM   663  N  ND1 . HIS A 1 121 ? 20.041  12.607  4.808   1.00   54.66  ? 136 HIS A ND1 1 
ATOM   664  C  CD2 . HIS A 1 121 ? 20.900  14.153  6.094   1.00   54.84  ? 136 HIS A CD2 1 
ATOM   665  C  CE1 . HIS A 1 121 ? 21.337  12.644  4.561   1.00   57.15  ? 136 HIS A CE1 1 
ATOM   666  N  NE2 . HIS A 1 121 ? 21.883  13.568  5.335   1.00   57.29  ? 136 HIS A NE2 1 
ATOM   667  N  N   . SER A 1 122 ? 19.263  13.775  9.190   1.00   50.11  ? 137 SER A N   1 
ATOM   668  C  CA  . SER A 1 122 ? 20.322  13.876  10.175  1.00   49.34  ? 137 SER A CA  1 
ATOM   669  C  C   . SER A 1 122 ? 20.133  12.794  11.223  1.00   49.20  ? 137 SER A C   1 
ATOM   670  O  O   . SER A 1 122 ? 21.074  12.089  11.561  1.00   50.82  ? 137 SER A O   1 
ATOM   671  C  CB  . SER A 1 122 ? 20.366  15.288  10.786  1.00   50.37  ? 137 SER A CB  1 
ATOM   672  O  OG  . SER A 1 122 ? 19.904  15.308  12.122  1.00   52.47  ? 137 SER A OG  1 
ATOM   673  N  N   . SER A 1 123 ? 18.915  12.616  11.716  1.00   50.25  ? 138 SER A N   1 
ATOM   674  C  CA  . SER A 1 123 ? 18.667  11.548  12.683  1.00   51.33  ? 138 SER A CA  1 
ATOM   675  C  C   . SER A 1 123 ? 19.272  10.230  12.200  1.00   53.26  ? 138 SER A C   1 
ATOM   676  O  O   . SER A 1 123 ? 20.001  9.594   12.942  1.00   53.29  ? 138 SER A O   1 
ATOM   677  C  CB  . SER A 1 123 ? 17.172  11.364  12.971  1.00   51.07  ? 138 SER A CB  1 
ATOM   678  O  OG  . SER A 1 123 ? 16.544  12.581  13.345  1.00   50.95  ? 138 SER A OG  1 
ATOM   679  N  N   . PHE A 1 124 ? 18.991  9.834   10.955  1.00   55.88  ? 139 PHE A N   1 
ATOM   680  C  CA  . PHE A 1 124 ? 19.474  8.542   10.440  1.00   57.33  ? 139 PHE A CA  1 
ATOM   681  C  C   . PHE A 1 124 ? 20.983  8.505   10.347  1.00   61.72  ? 139 PHE A C   1 
ATOM   682  O  O   . PHE A 1 124 ? 21.604  7.514   10.730  1.00   64.45  ? 139 PHE A O   1 
ATOM   683  C  CB  . PHE A 1 124 ? 18.902  8.242   9.058   1.00   57.68  ? 139 PHE A CB  1 
ATOM   684  C  CG  . PHE A 1 124 ? 17.464  7.801   9.070   1.00   55.73  ? 139 PHE A CG  1 
ATOM   685  C  CD1 . PHE A 1 124 ? 17.094  6.626   9.706   1.00   56.15  ? 139 PHE A CD1 1 
ATOM   686  C  CD2 . PHE A 1 124 ? 16.489  8.541   8.438   1.00   52.50  ? 139 PHE A CD2 1 
ATOM   687  C  CE1 . PHE A 1 124 ? 15.766  6.210   9.719   1.00   54.33  ? 139 PHE A CE1 1 
ATOM   688  C  CE2 . PHE A 1 124 ? 15.168  8.127   8.459   1.00   52.58  ? 139 PHE A CE2 1 
ATOM   689  C  CZ  . PHE A 1 124 ? 14.801  6.968   9.097   1.00   51.51  ? 139 PHE A CZ  1 
ATOM   690  N  N   . THR A 1 125 ? 21.557  9.591   9.827   1.00   66.74  ? 140 THR A N   1 
ATOM   691  C  CA  . THR A 1 125 ? 22.999  9.722   9.638   1.00   67.37  ? 140 THR A CA  1 
ATOM   692  C  C   . THR A 1 125 ? 23.721  9.430   10.932  1.00   73.20  ? 140 THR A C   1 
ATOM   693  O  O   . THR A 1 125 ? 24.732  8.739   10.926  1.00   80.05  ? 140 THR A O   1 
ATOM   694  C  CB  . THR A 1 125 ? 23.394  11.148  9.198   1.00   68.05  ? 140 THR A CB  1 
ATOM   695  O  OG1 . THR A 1 125 ? 22.701  11.512  7.992   1.00   68.37  ? 140 THR A OG1 1 
ATOM   696  C  CG2 . THR A 1 125 ? 24.912  11.246  8.972   1.00   69.75  ? 140 THR A CG2 1 
ATOM   697  N  N   . LEU A 1 126 ? 23.203  9.981   12.031  1.00   75.92  ? 141 LEU A N   1 
ATOM   698  C  CA  . LEU A 1 126 ? 23.801  9.830   13.366  1.00   77.61  ? 141 LEU A CA  1 
ATOM   699  C  C   . LEU A 1 126 ? 23.824  8.375   13.857  1.00   79.73  ? 141 LEU A C   1 
ATOM   700  O  O   . LEU A 1 126 ? 24.792  7.923   14.490  1.00   80.69  ? 141 LEU A O   1 
ATOM   701  C  CB  . LEU A 1 126 ? 23.042  10.704  14.371  1.00   77.35  ? 141 LEU A CB  1 
ATOM   702  C  CG  . LEU A 1 126 ? 23.174  10.381  15.863  1.00   77.06  ? 141 LEU A CG  1 
ATOM   703  C  CD1 . LEU A 1 126 ? 24.628  10.426  16.325  1.00   77.31  ? 141 LEU A CD1 1 
ATOM   704  C  CD2 . LEU A 1 126 ? 22.314  11.350  16.666  1.00   75.58  ? 141 LEU A CD2 1 
ATOM   705  N  N   . PHE A 1 127 ? 22.758  7.646   13.564  1.00   79.28  ? 142 PHE A N   1 
ATOM   706  C  CA  . PHE A 1 127 ? 22.635  6.267   14.018  1.00   81.41  ? 142 PHE A CA  1 
ATOM   707  C  C   . PHE A 1 127 ? 23.422  5.250   13.176  1.00   83.94  ? 142 PHE A C   1 
ATOM   708  O  O   . PHE A 1 127 ? 23.905  4.240   13.720  1.00   80.44  ? 142 PHE A O   1 
ATOM   709  C  CB  . PHE A 1 127 ? 21.169  5.898   14.082  1.00   82.19  ? 142 PHE A CB  1 
ATOM   710  C  CG  . PHE A 1 127 ? 20.459  6.559   15.207  1.00   86.56  ? 142 PHE A CG  1 
ATOM   711  C  CD1 . PHE A 1 127 ? 20.237  7.921   15.198  1.00   88.76  ? 142 PHE A CD1 1 
ATOM   712  C  CD2 . PHE A 1 127 ? 20.051  5.833   16.297  1.00   92.17  ? 142 PHE A CD2 1 
ATOM   713  C  CE1 . PHE A 1 127 ? 19.594  8.546   16.244  1.00   90.37  ? 142 PHE A CE1 1 
ATOM   714  C  CE2 . PHE A 1 127 ? 19.412  6.454   17.359  1.00   96.44  ? 142 PHE A CE2 1 
ATOM   715  C  CZ  . PHE A 1 127 ? 19.185  7.812   17.329  1.00   92.67  ? 142 PHE A CZ  1 
ATOM   716  N  N   . GLY A 1 128 ? 23.554  5.525   11.869  1.00   82.13  ? 143 GLY A N   1 
ATOM   717  C  CA  . GLY A 1 128 ? 24.331  4.688   10.936  1.00   80.24  ? 143 GLY A CA  1 
ATOM   718  C  C   . GLY A 1 128 ? 25.813  5.038   10.786  1.00   81.39  ? 143 GLY A C   1 
ATOM   719  O  O   . GLY A 1 128 ? 26.677  4.316   11.277  1.00   78.35  ? 143 GLY A O   1 
ATOM   720  N  N   . GLU A 1 129 ? 26.104  6.126   10.079  1.00   88.15  ? 144 GLU A N   1 
ATOM   721  C  CA  . GLU A 1 129 ? 27.486  6.601   9.882   1.00   96.02  ? 144 GLU A CA  1 
ATOM   722  C  C   . GLU A 1 129 ? 28.099  7.141   11.180  1.00   97.15  ? 144 GLU A C   1 
ATOM   723  O  O   . GLU A 1 129 ? 29.185  6.717   11.583  1.00   101.20 ? 144 GLU A O   1 
ATOM   724  C  CB  . GLU A 1 129 ? 27.534  7.686   8.782   1.00   101.61 ? 144 GLU A CB  1 
ATOM   725  C  CG  . GLU A 1 129 ? 28.816  8.536   8.717   1.00   105.55 ? 144 GLU A CG  1 
ATOM   726  C  CD  . GLU A 1 129 ? 29.970  7.870   7.971   1.00   108.12 ? 144 GLU A CD  1 
ATOM   727  O  OE1 . GLU A 1 129 ? 29.713  7.299   6.891   1.00   114.70 ? 144 GLU A OE1 1 
ATOM   728  O  OE2 . GLU A 1 129 ? 31.135  7.935   8.442   1.00   104.59 ? 144 GLU A OE2 1 
ATOM   729  N  N   . GLY A 1 130 ? 27.402  8.082   11.816  1.00   98.69  ? 145 GLY A N   1 
ATOM   730  C  CA  . GLY A 1 130 ? 27.882  8.748   13.032  1.00   103.43 ? 145 GLY A CA  1 
ATOM   731  C  C   . GLY A 1 130 ? 28.432  7.834   14.120  1.00   106.62 ? 145 GLY A C   1 
ATOM   732  O  O   . GLY A 1 130 ? 29.403  8.189   14.797  1.00   110.70 ? 145 GLY A O   1 
ATOM   733  N  N   . SER A 1 131 ? 27.817  6.665   14.300  1.00   104.61 ? 146 SER A N   1 
ATOM   734  C  CA  . SER A 1 131 ? 28.310  5.685   15.276  1.00   104.19 ? 146 SER A CA  1 
ATOM   735  C  C   . SER A 1 131 ? 27.892  4.244   14.923  1.00   95.06  ? 146 SER A C   1 
ATOM   736  O  O   . SER A 1 131 ? 27.700  3.928   13.748  1.00   93.54  ? 146 SER A O   1 
ATOM   737  C  CB  . SER A 1 131 ? 27.868  6.091   16.691  1.00   108.35 ? 146 SER A CB  1 
ATOM   738  O  OG  . SER A 1 131 ? 28.355  7.386   17.013  1.00   112.97 ? 146 SER A OG  1 
ATOM   739  N  N   . ASN A 1 132 ? 27.764  3.379   15.929  1.00   86.28  ? 147 ASN A N   1 
ATOM   740  C  CA  . ASN A 1 132 ? 27.522  1.956   15.708  1.00   81.27  ? 147 ASN A CA  1 
ATOM   741  C  C   . ASN A 1 132 ? 26.242  1.453   16.372  1.00   74.46  ? 147 ASN A C   1 
ATOM   742  O  O   . ASN A 1 132 ? 26.109  0.257   16.622  1.00   73.81  ? 147 ASN A O   1 
ATOM   743  C  CB  . ASN A 1 132 ? 28.734  1.143   16.187  1.00   82.99  ? 147 ASN A CB  1 
ATOM   744  C  CG  . ASN A 1 132 ? 29.307  1.669   17.486  1.00   87.57  ? 147 ASN A CG  1 
ATOM   745  O  OD1 . ASN A 1 132 ? 28.867  2.703   17.995  1.00   89.63  ? 147 ASN A OD1 1 
ATOM   746  N  ND2 . ASN A 1 132 ? 30.301  0.970   18.027  1.00   90.99  ? 147 ASN A ND2 1 
ATOM   747  N  N   . LYS A 1 133 ? 25.298  2.349   16.650  1.00   69.57  ? 148 LYS A N   1 
ATOM   748  C  CA  . LYS A 1 133 ? 24.008  1.921   17.200  1.00   70.91  ? 148 LYS A CA  1 
ATOM   749  C  C   . LYS A 1 133 ? 23.233  1.101   16.153  1.00   64.45  ? 148 LYS A C   1 
ATOM   750  O  O   . LYS A 1 133 ? 22.694  0.040   16.460  1.00   61.77  ? 148 LYS A O   1 
ATOM   751  C  CB  . LYS A 1 133 ? 23.175  3.112   17.695  1.00   75.13  ? 148 LYS A CB  1 
ATOM   752  C  CG  . LYS A 1 133 ? 21.978  2.716   18.561  1.00   81.07  ? 148 LYS A CG  1 
ATOM   753  C  CD  . LYS A 1 133 ? 21.025  3.891   18.789  1.00   87.25  ? 148 LYS A CD  1 
ATOM   754  C  CE  . LYS A 1 133 ? 19.584  3.464   19.104  1.00   90.89  ? 148 LYS A CE  1 
ATOM   755  N  NZ  . LYS A 1 133 ? 19.379  3.170   20.547  1.00   96.38  ? 148 LYS A NZ  1 
ATOM   756  N  N   . LEU A 1 134 ? 23.204  1.574   14.914  1.00   58.24  ? 149 LEU A N   1 
ATOM   757  C  CA  . LEU A 1 134 ? 22.588  0.801   13.874  1.00   54.44  ? 149 LEU A CA  1 
ATOM   758  C  C   . LEU A 1 134 ? 23.347  -0.497  13.657  1.00   51.97  ? 149 LEU A C   1 
ATOM   759  O  O   . LEU A 1 134 ? 22.748  -1.556  13.548  1.00   53.80  ? 149 LEU A O   1 
ATOM   760  C  CB  . LEU A 1 134 ? 22.513  1.580   12.568  1.00   54.65  ? 149 LEU A CB  1 
ATOM   761  C  CG  . LEU A 1 134 ? 21.903  0.777   11.412  1.00   54.75  ? 149 LEU A CG  1 
ATOM   762  C  CD1 . LEU A 1 134 ? 20.466  0.396   11.746  1.00   55.61  ? 149 LEU A CD1 1 
ATOM   763  C  CD2 . LEU A 1 134 ? 21.954  1.589   10.126  1.00   54.94  ? 149 LEU A CD2 1 
ATOM   764  N  N   . GLN A 1 135 ? 24.662  -0.428  13.586  1.00   49.57  ? 150 GLN A N   1 
ATOM   765  C  CA  . GLN A 1 135 ? 25.449  -1.624  13.305  1.00   48.18  ? 150 GLN A CA  1 
ATOM   766  C  C   . GLN A 1 135 ? 25.132  -2.677  14.350  1.00   46.74  ? 150 GLN A C   1 
ATOM   767  O  O   . GLN A 1 135 ? 24.893  -3.838  14.047  1.00   46.65  ? 150 GLN A O   1 
ATOM   768  C  CB  . GLN A 1 135 ? 26.931  -1.275  13.314  1.00   49.61  ? 150 GLN A CB  1 
ATOM   769  C  CG  . GLN A 1 135 ? 27.877  -2.367  12.873  1.00   50.72  ? 150 GLN A CG  1 
ATOM   770  C  CD  . GLN A 1 135 ? 29.295  -1.837  12.737  1.00   52.79  ? 150 GLN A CD  1 
ATOM   771  O  OE1 . GLN A 1 135 ? 29.933  -2.006  11.710  1.00   55.95  ? 150 GLN A OE1 1 
ATOM   772  N  NE2 . GLN A 1 135 ? 29.785  -1.177  13.774  1.00   55.22  ? 150 GLN A NE2 1 
ATOM   773  N  N   . THR A 1 136 ? 25.093  -2.245  15.593  1.00   45.73  ? 151 THR A N   1 
ATOM   774  C  CA  . THR A 1 136 ? 24.837  -3.143  16.681  1.00   45.49  ? 151 THR A CA  1 
ATOM   775  C  C   . THR A 1 136 ? 23.417  -3.671  16.570  1.00   44.22  ? 151 THR A C   1 
ATOM   776  O  O   . THR A 1 136 ? 23.200  -4.877  16.585  1.00   44.05  ? 151 THR A O   1 
ATOM   777  C  CB  . THR A 1 136 ? 25.105  -2.426  18.018  1.00   46.99  ? 151 THR A CB  1 
ATOM   778  O  OG1 . THR A 1 136 ? 26.522  -2.347  18.214  1.00   47.36  ? 151 THR A OG1 1 
ATOM   779  C  CG2 . THR A 1 136 ? 24.439  -3.139  19.219  1.00   47.56  ? 151 THR A CG2 1 
ATOM   780  N  N   . ILE A 1 137 ? 22.450  -2.772  16.442  1.00   43.39  ? 152 ILE A N   1 
ATOM   781  C  CA  . ILE A 1 137 ? 21.066  -3.186  16.293  1.00   42.98  ? 152 ILE A CA  1 
ATOM   782  C  C   . ILE A 1 137 ? 21.003  -4.249  15.208  1.00   42.55  ? 152 ILE A C   1 
ATOM   783  O  O   . ILE A 1 137 ? 20.397  -5.291  15.382  1.00   42.79  ? 152 ILE A O   1 
ATOM   784  C  CB  . ILE A 1 137 ? 20.157  -2.029  15.852  1.00   42.74  ? 152 ILE A CB  1 
ATOM   785  C  CG1 . ILE A 1 137 ? 20.037  -0.960  16.921  1.00   44.21  ? 152 ILE A CG1 1 
ATOM   786  C  CG2 . ILE A 1 137 ? 18.745  -2.522  15.564  1.00   42.27  ? 152 ILE A CG2 1 
ATOM   787  C  CD1 . ILE A 1 137 ? 19.412  0.311   16.376  1.00   44.15  ? 152 ILE A CD1 1 
ATOM   788  N  N   . VAL A 1 138 ? 21.650  -3.999  14.082  1.00   42.34  ? 153 VAL A N   1 
ATOM   789  C  CA  . VAL A 1 138 ? 21.461  -4.870  12.920  1.00   42.98  ? 153 VAL A CA  1 
ATOM   790  C  C   . VAL A 1 138 ? 22.261  -6.176  13.062  1.00   44.99  ? 153 VAL A C   1 
ATOM   791  O  O   . VAL A 1 138 ? 21.813  -7.263  12.651  1.00   44.55  ? 153 VAL A O   1 
ATOM   792  C  CB  . VAL A 1 138 ? 21.736  -4.116  11.589  1.00   41.30  ? 153 VAL A CB  1 
ATOM   793  C  CG1 . VAL A 1 138 ? 21.630  -5.048  10.414  1.00   40.26  ? 153 VAL A CG1 1 
ATOM   794  C  CG2 . VAL A 1 138 ? 20.753  -2.961  11.410  1.00   40.64  ? 153 VAL A CG2 1 
ATOM   795  N  N   . GLN A 1 139 ? 23.431  -6.092  13.671  1.00   47.79  ? 154 GLN A N   1 
ATOM   796  C  CA  . GLN A 1 139 ? 24.174  -7.313  13.944  1.00   49.82  ? 154 GLN A CA  1 
ATOM   797  C  C   . GLN A 1 139 ? 23.414  -8.181  14.945  1.00   51.00  ? 154 GLN A C   1 
ATOM   798  O  O   . GLN A 1 139 ? 23.205  -9.369  14.702  1.00   49.88  ? 154 GLN A O   1 
ATOM   799  C  CB  . GLN A 1 139 ? 25.593  -6.997  14.423  1.00   51.97  ? 154 GLN A CB  1 
ATOM   800  C  CG  . GLN A 1 139 ? 26.609  -6.842  13.288  1.00   52.67  ? 154 GLN A CG  1 
ATOM   801  C  CD  . GLN A 1 139 ? 27.899  -6.161  13.717  1.00   55.44  ? 154 GLN A CD  1 
ATOM   802  O  OE1 . GLN A 1 139 ? 28.005  -5.610  14.828  1.00   55.28  ? 154 GLN A OE1 1 
ATOM   803  N  NE2 . GLN A 1 139 ? 28.895  -6.186  12.829  1.00   56.89  ? 154 GLN A NE2 1 
ATOM   804  N  N   . GLU A 1 140 ? 22.955  -7.589  16.048  1.00   52.87  ? 155 GLU A N   1 
ATOM   805  C  CA  . GLU A 1 140 ? 22.333  -8.383  17.107  1.00   54.45  ? 155 GLU A CA  1 
ATOM   806  C  C   . GLU A 1 140 ? 21.044  -9.021  16.653  1.00   53.29  ? 155 GLU A C   1 
ATOM   807  O  O   . GLU A 1 140 ? 20.636  -10.052 17.191  1.00   52.60  ? 155 GLU A O   1 
ATOM   808  C  CB  . GLU A 1 140 ? 22.088  -7.549  18.355  1.00   57.46  ? 155 GLU A CB  1 
ATOM   809  C  CG  . GLU A 1 140 ? 23.237  -7.568  19.351  1.00   58.78  ? 155 GLU A CG  1 
ATOM   810  C  CD  . GLU A 1 140 ? 22.906  -6.724  20.539  1.00   61.38  ? 155 GLU A CD  1 
ATOM   811  O  OE1 . GLU A 1 140 ? 22.731  -7.275  21.646  1.00   68.88  ? 155 GLU A OE1 1 
ATOM   812  O  OE2 . GLU A 1 140 ? 22.758  -5.505  20.346  1.00   61.16  ? 155 GLU A OE2 1 
ATOM   813  N  N   . ALA A 1 141 ? 20.413  -8.394  15.665  1.00   52.85  ? 156 ALA A N   1 
ATOM   814  C  CA  . ALA A 1 141 ? 19.209  -8.918  15.045  1.00   53.85  ? 156 ALA A CA  1 
ATOM   815  C  C   . ALA A 1 141 ? 19.538  -10.024 14.058  1.00   54.13  ? 156 ALA A C   1 
ATOM   816  O  O   . ALA A 1 141 ? 18.873  -11.058 14.028  1.00   58.04  ? 156 ALA A O   1 
ATOM   817  C  CB  . ALA A 1 141 ? 18.455  -7.803  14.347  1.00   54.30  ? 156 ALA A CB  1 
ATOM   818  N  N   . ALA A 1 142 ? 20.566  -9.825  13.252  1.00   53.00  ? 157 ALA A N   1 
ATOM   819  C  CA  . ALA A 1 142 ? 21.020  -10.903 12.386  1.00   54.64  ? 157 ALA A CA  1 
ATOM   820  C  C   . ALA A 1 142 ? 21.366  -12.158 13.195  1.00   56.05  ? 157 ALA A C   1 
ATOM   821  O  O   . ALA A 1 142 ? 21.250  -13.270 12.690  1.00   56.37  ? 157 ALA A O   1 
ATOM   822  C  CB  . ALA A 1 142 ? 22.205  -10.458 11.530  1.00   54.34  ? 157 ALA A CB  1 
ATOM   823  N  N   . ASP A 1 143 ? 21.796  -11.984 14.442  1.00   59.91  ? 158 ASP A N   1 
ATOM   824  C  CA  . ASP A 1 143 ? 22.010  -13.125 15.345  1.00   62.56  ? 158 ASP A CA  1 
ATOM   825  C  C   . ASP A 1 143 ? 20.734  -13.884 15.495  1.00   60.40  ? 158 ASP A C   1 
ATOM   826  O  O   . ASP A 1 143 ? 20.669  -15.078 15.203  1.00   58.54  ? 158 ASP A O   1 
ATOM   827  C  CB  . ASP A 1 143 ? 22.429  -12.664 16.743  1.00   66.02  ? 158 ASP A CB  1 
ATOM   828  C  CG  . ASP A 1 143 ? 23.876  -12.326 16.817  1.00   69.75  ? 158 ASP A CG  1 
ATOM   829  O  OD1 . ASP A 1 143 ? 24.647  -13.094 16.217  1.00   74.14  ? 158 ASP A OD1 1 
ATOM   830  O  OD2 . ASP A 1 143 ? 24.262  -11.318 17.458  1.00   73.29  ? 158 ASP A OD2 1 
ATOM   831  N  N   . SER A 1 144 ? 19.716  -13.168 15.964  1.00   59.22  ? 159 SER A N   1 
ATOM   832  C  CA  . SER A 1 144 ? 18.453  -13.789 16.240  1.00   60.03  ? 159 SER A CA  1 
ATOM   833  C  C   . SER A 1 144 ? 18.041  -14.474 14.961  1.00   60.62  ? 159 SER A C   1 
ATOM   834  O  O   . SER A 1 144 ? 17.673  -15.655 14.987  1.00   63.86  ? 159 SER A O   1 
ATOM   835  C  CB  . SER A 1 144 ? 17.404  -12.778 16.700  1.00   59.23  ? 159 SER A CB  1 
ATOM   836  O  OG  . SER A 1 144 ? 17.769  -12.208 17.943  1.00   60.83  ? 159 SER A OG  1 
ATOM   837  N  N   . LEU A 1 145 ? 18.142  -13.757 13.838  1.00   57.43  ? 160 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 145 ? 17.720  -14.324 12.564  1.00   56.90  ? 160 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 145 ? 18.490  -15.611 12.301  1.00   58.77  ? 160 LEU A C   1 
ATOM   840  O  O   . LEU A 1 145 ? 17.887  -16.637 11.969  1.00   59.07  ? 160 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 145 ? 17.896  -13.342 11.385  1.00   54.81  ? 160 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 145 ? 17.654  -13.978 9.997   1.00   52.52  ? 160 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 145 ? 16.265  -14.570 9.931   1.00   52.57  ? 160 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 145 ? 17.852  -12.992 8.857   1.00   51.10  ? 160 LEU A CD2 1 
ATOM   845  N  N   . CYS A 1 146 ? 19.813  -15.554 12.455  1.00   59.03  ? 161 CYS A N   1 
ATOM   846  C  CA  . CYS A 1 146 ? 20.636  -16.742 12.266  1.00   60.66  ? 161 CYS A CA  1 
ATOM   847  C  C   . CYS A 1 146 ? 20.180  -17.836 13.223  1.00   63.41  ? 161 CYS A C   1 
ATOM   848  O  O   . CYS A 1 146 ? 19.960  -18.965 12.803  1.00   65.15  ? 161 CYS A O   1 
ATOM   849  C  CB  . CYS A 1 146 ? 22.139  -16.443 12.422  1.00   59.48  ? 161 CYS A CB  1 
ATOM   850  S  SG  . CYS A 1 146 ? 22.918  -15.597 11.011  1.00   54.81  ? 161 CYS A SG  1 
ATOM   851  N  N   . GLU A 1 147 ? 19.983  -17.501 14.491  1.00   66.65  ? 162 GLU A N   1 
ATOM   852  C  CA  . GLU A 1 147 ? 19.519  -18.501 15.452  1.00   71.26  ? 162 GLU A CA  1 
ATOM   853  C  C   . GLU A 1 147 ? 18.206  -19.162 15.011  1.00   69.92  ? 162 GLU A C   1 
ATOM   854  O  O   . GLU A 1 147 ? 18.131  -20.382 14.913  1.00   68.81  ? 162 GLU A O   1 
ATOM   855  C  CB  . GLU A 1 147 ? 19.394  -17.909 16.860  1.00   76.09  ? 162 GLU A CB  1 
ATOM   856  C  CG  . GLU A 1 147 ? 20.736  -17.580 17.502  1.00   80.35  ? 162 GLU A CG  1 
ATOM   857  C  CD  . GLU A 1 147 ? 20.969  -18.323 18.809  1.00   87.65  ? 162 GLU A CD  1 
ATOM   858  O  OE1 . GLU A 1 147 ? 20.016  -18.457 19.612  1.00   91.19  ? 162 GLU A OE1 1 
ATOM   859  O  OE2 . GLU A 1 147 ? 22.115  -18.777 19.033  1.00   92.19  ? 162 GLU A OE2 1 
ATOM   860  N  N   . GLU A 1 148 ? 17.188  -18.357 14.718  1.00   69.82  ? 163 GLU A N   1 
ATOM   861  C  CA  . GLU A 1 148 ? 15.923  -18.873 14.173  1.00   70.54  ? 163 GLU A CA  1 
ATOM   862  C  C   . GLU A 1 148 ? 16.117  -19.842 13.018  1.00   70.55  ? 163 GLU A C   1 
ATOM   863  O  O   . GLU A 1 148 ? 15.391  -20.813 12.898  1.00   70.43  ? 163 GLU A O   1 
ATOM   864  C  CB  . GLU A 1 148 ? 15.032  -17.735 13.682  1.00   71.15  ? 163 GLU A CB  1 
ATOM   865  C  CG  . GLU A 1 148 ? 14.416  -16.890 14.785  1.00   73.24  ? 163 GLU A CG  1 
ATOM   866  C  CD  . GLU A 1 148 ? 13.033  -16.375 14.431  1.00   74.71  ? 163 GLU A CD  1 
ATOM   867  O  OE1 . GLU A 1 148 ? 12.180  -17.161 13.960  1.00   73.41  ? 163 GLU A OE1 1 
ATOM   868  O  OE2 . GLU A 1 148 ? 12.797  -15.172 14.641  1.00   79.34  ? 163 GLU A OE2 1 
ATOM   869  N  N   . LEU A 1 149 ? 17.090  -19.563 12.159  1.00   72.31  ? 164 LEU A N   1 
ATOM   870  C  CA  . LEU A 1 149 ? 17.353  -20.408 11.000  1.00   74.43  ? 164 LEU A CA  1 
ATOM   871  C  C   . LEU A 1 149 ? 18.000  -21.741 11.372  1.00   79.84  ? 164 LEU A C   1 
ATOM   872  O  O   . LEU A 1 149 ? 17.719  -22.761 10.740  1.00   81.86  ? 164 LEU A O   1 
ATOM   873  C  CB  . LEU A 1 149 ? 18.209  -19.659 9.976   1.00   73.31  ? 164 LEU A CB  1 
ATOM   874  C  CG  . LEU A 1 149 ? 17.479  -18.486 9.301   1.00   69.74  ? 164 LEU A CG  1 
ATOM   875  C  CD1 . LEU A 1 149 ? 18.433  -17.417 8.802   1.00   68.20  ? 164 LEU A CD1 1 
ATOM   876  C  CD2 . LEU A 1 149 ? 16.620  -18.988 8.163   1.00   69.49  ? 164 LEU A CD2 1 
ATOM   877  N  N   . GLN A 1 150 ? 18.856  -21.749 12.392  1.00   83.33  ? 165 GLN A N   1 
ATOM   878  C  CA  . GLN A 1 150 ? 19.426  -23.007 12.877  1.00   86.98  ? 165 GLN A CA  1 
ATOM   879  C  C   . GLN A 1 150 ? 18.286  -23.981 13.186  1.00   91.52  ? 165 GLN A C   1 
ATOM   880  O  O   . GLN A 1 150 ? 18.216  -25.071 12.623  1.00   93.37  ? 165 GLN A O   1 
ATOM   881  C  CB  . GLN A 1 150 ? 20.294  -22.788 14.126  1.00   85.15  ? 165 GLN A CB  1 
ATOM   882  C  CG  . GLN A 1 150 ? 21.586  -22.017 13.878  1.00   84.18  ? 165 GLN A CG  1 
ATOM   883  C  CD  . GLN A 1 150 ? 22.634  -22.827 13.135  1.00   84.12  ? 165 GLN A CD  1 
ATOM   884  O  OE1 . GLN A 1 150 ? 22.423  -23.999 12.827  1.00   83.00  ? 165 GLN A OE1 1 
ATOM   885  N  NE2 . GLN A 1 150 ? 23.776  -22.201 12.843  1.00   82.54  ? 165 GLN A NE2 1 
ATOM   886  N  N   . ALA A 1 151 ? 17.369  -23.551 14.048  1.00   94.62  ? 166 ALA A N   1 
ATOM   887  C  CA  . ALA A 1 151 ? 16.239  -24.374 14.467  1.00   97.75  ? 166 ALA A CA  1 
ATOM   888  C  C   . ALA A 1 151 ? 15.382  -24.849 13.292  1.00   104.73 ? 166 ALA A C   1 
ATOM   889  O  O   . ALA A 1 151 ? 14.753  -25.905 13.367  1.00   105.68 ? 166 ALA A O   1 
ATOM   890  C  CB  . ALA A 1 151 ? 15.385  -23.603 15.461  1.00   95.49  ? 166 ALA A CB  1 
ATOM   891  N  N   . CYS A 1 152 ? 15.346  -24.066 12.215  1.00   114.48 ? 167 CYS A N   1 
ATOM   892  C  CA  . CYS A 1 152 ? 14.587  -24.441 11.019  1.00   122.45 ? 167 CYS A CA  1 
ATOM   893  C  C   . CYS A 1 152 ? 15.271  -25.552 10.204  1.00   124.07 ? 167 CYS A C   1 
ATOM   894  O  O   . CYS A 1 152 ? 14.610  -26.198 9.401   1.00   124.90 ? 167 CYS A O   1 
ATOM   895  C  CB  . CYS A 1 152 ? 14.304  -23.220 10.132  1.00   124.17 ? 167 CYS A CB  1 
ATOM   896  S  SG  . CYS A 1 152 ? 15.690  -22.718 9.087   1.00   132.96 ? 167 CYS A SG  1 
ATOM   897  N  N   . ARG A 1 153 ? 16.579  -25.770 10.383  1.00   122.96 ? 168 ARG A N   1 
ATOM   898  C  CA  . ARG A 1 153 ? 17.211  -26.987 9.851   1.00   121.10 ? 168 ARG A CA  1 
ATOM   899  C  C   . ARG A 1 153 ? 16.530  -28.185 10.536  1.00   121.57 ? 168 ARG A C   1 
ATOM   900  O  O   . ARG A 1 153 ? 16.163  -28.090 11.708  1.00   121.65 ? 168 ARG A O   1 
ATOM   901  C  CB  . ARG A 1 153 ? 18.749  -26.989 10.063  1.00   120.36 ? 168 ARG A CB  1 
ATOM   902  C  CG  . ARG A 1 153 ? 19.422  -28.373 10.102  1.00   121.30 ? 168 ARG A CG  1 
ATOM   903  C  CD  . ARG A 1 153 ? 20.763  -28.453 9.367   1.00   120.25 ? 168 ARG A CD  1 
ATOM   904  N  NE  . ARG A 1 153 ? 21.943  -28.358 10.239  1.00   120.72 ? 168 ARG A NE  1 
ATOM   905  C  CZ  . ARG A 1 153 ? 22.503  -29.369 10.911  1.00   118.50 ? 168 ARG A CZ  1 
ATOM   906  N  NH1 . ARG A 1 153 ? 21.996  -30.600 10.864  1.00   119.51 ? 168 ARG A NH1 1 
ATOM   907  N  NH2 . ARG A 1 153 ? 23.584  -29.145 11.653  1.00   114.45 ? 168 ARG A NH2 1 
ATOM   908  N  N   . GLY A 1 154 ? 16.316  -29.294 9.828   1.00   121.95 ? 169 GLY A N   1 
ATOM   909  C  CA  . GLY A 1 154 ? 16.666  -29.454 8.419   1.00   123.35 ? 169 GLY A CA  1 
ATOM   910  C  C   . GLY A 1 154 ? 15.441  -29.386 7.537   1.00   124.75 ? 169 GLY A C   1 
ATOM   911  O  O   . GLY A 1 154 ? 15.237  -30.252 6.687   1.00   131.22 ? 169 GLY A O   1 
ATOM   912  N  N   . GLN A 1 155 ? 14.622  -28.355 7.735   1.00   122.20 ? 170 GLN A N   1 
ATOM   913  C  CA  . GLN A 1 155 ? 13.416  -28.174 6.930   1.00   116.55 ? 170 GLN A CA  1 
ATOM   914  C  C   . GLN A 1 155 ? 13.758  -27.513 5.602   1.00   107.20 ? 170 GLN A C   1 
ATOM   915  O  O   . GLN A 1 155 ? 14.884  -27.071 5.371   1.00   100.98 ? 170 GLN A O   1 
ATOM   916  C  CB  . GLN A 1 155 ? 12.356  -27.325 7.663   1.00   118.30 ? 170 GLN A CB  1 
ATOM   917  C  CG  . GLN A 1 155 ? 12.127  -27.623 9.145   1.00   120.77 ? 170 GLN A CG  1 
ATOM   918  C  CD  . GLN A 1 155 ? 12.151  -29.099 9.509   1.00   124.31 ? 170 GLN A CD  1 
ATOM   919  O  OE1 . GLN A 1 155 ? 12.093  -29.978 8.646   1.00   124.94 ? 170 GLN A OE1 1 
ATOM   920  N  NE2 . GLN A 1 155 ? 12.230  -29.375 10.809  1.00   126.71 ? 170 GLN A NE2 1 
ATOM   921  N  N   . SER A 1 156 ? 12.766  -27.466 4.728   1.00   101.42 ? 171 SER A N   1 
ATOM   922  C  CA  . SER A 1 156 ? 12.850  -26.675 3.527   1.00   96.91  ? 171 SER A CA  1 
ATOM   923  C  C   . SER A 1 156 ? 11.963  -25.459 3.770   1.00   95.14  ? 171 SER A C   1 
ATOM   924  O  O   . SER A 1 156 ? 10.959  -25.231 3.098   1.00   97.39  ? 171 SER A O   1 
ATOM   925  C  CB  . SER A 1 156 ? 12.431  -27.518 2.338   1.00   96.87  ? 171 SER A CB  1 
ATOM   926  O  OG  . SER A 1 156 ? 13.384  -28.558 2.157   1.00   96.44  ? 171 SER A OG  1 
ATOM   927  N  N   . SER A 1 157 ? 12.377  -24.678 4.761   1.00   92.92  ? 172 SER A N   1 
ATOM   928  C  CA  . SER A 1 157 ? 11.570  -23.611 5.334   1.00   88.47  ? 172 SER A CA  1 
ATOM   929  C  C   . SER A 1 157 ? 11.139  -22.585 4.300   1.00   85.94  ? 172 SER A C   1 
ATOM   930  O  O   . SER A 1 157 ? 11.801  -22.419 3.284   1.00   82.13  ? 172 SER A O   1 
ATOM   931  C  CB  . SER A 1 157 ? 12.385  -22.910 6.431   1.00   86.77  ? 172 SER A CB  1 
ATOM   932  O  OG  . SER A 1 157 ? 11.653  -21.859 7.029   1.00   83.95  ? 172 SER A OG  1 
ATOM   933  N  N   . ASP A 1 158 ? 10.016  -21.915 4.553   1.00   85.89  ? 173 ASP A N   1 
ATOM   934  C  CA  . ASP A 1 158 ? 9.790   -20.610 3.952   1.00   83.28  ? 173 ASP A CA  1 
ATOM   935  C  C   . ASP A 1 158 ? 10.266  -19.540 4.930   1.00   79.44  ? 173 ASP A C   1 
ATOM   936  O  O   . ASP A 1 158 ? 9.755   -19.421 6.046   1.00   78.46  ? 173 ASP A O   1 
ATOM   937  C  CB  . ASP A 1 158 ? 8.327   -20.354 3.606   1.00   85.98  ? 173 ASP A CB  1 
ATOM   938  C  CG  . ASP A 1 158 ? 8.103   -18.931 3.037   1.00   86.44  ? 173 ASP A CG  1 
ATOM   939  O  OD1 . ASP A 1 158 ? 8.090   -17.940 3.808   1.00   81.84  ? 173 ASP A OD1 1 
ATOM   940  O  OD2 . ASP A 1 158 ? 7.938   -18.794 1.808   1.00   88.83  ? 173 ASP A OD2 1 
ATOM   941  N  N   . LEU A 1 159 ? 11.255  -18.770 4.501   1.00   74.95  ? 174 LEU A N   1 
ATOM   942  C  CA  . LEU A 1 159 ? 11.643  -17.558 5.208   1.00   72.06  ? 174 LEU A CA  1 
ATOM   943  C  C   . LEU A 1 159 ? 10.829  -16.473 4.586   1.00   68.41  ? 174 LEU A C   1 
ATOM   944  O  O   . LEU A 1 159 ? 10.266  -16.679 3.527   1.00   78.23  ? 174 LEU A O   1 
ATOM   945  C  CB  . LEU A 1 159 ? 13.135  -17.268 5.062   1.00   73.96  ? 174 LEU A CB  1 
ATOM   946  C  CG  . LEU A 1 159 ? 13.879  -17.640 3.774   1.00   75.91  ? 174 LEU A CG  1 
ATOM   947  C  CD1 . LEU A 1 159 ? 13.305  -16.954 2.542   1.00   75.68  ? 174 LEU A CD1 1 
ATOM   948  C  CD2 . LEU A 1 159 ? 15.359  -17.308 3.927   1.00   77.23  ? 174 LEU A CD2 1 
ATOM   949  N  N   . SER A 1 160 ? 10.754  -15.323 5.221   1.00   62.84  ? 175 SER A N   1 
ATOM   950  C  CA  . SER A 1 160 ? 9.851   -14.262 4.780   1.00   61.10  ? 175 SER A CA  1 
ATOM   951  C  C   . SER A 1 160 ? 9.149   -13.741 5.989   1.00   59.91  ? 175 SER A C   1 
ATOM   952  O  O   . SER A 1 160 ? 9.097   -12.541 6.210   1.00   59.90  ? 175 SER A O   1 
ATOM   953  C  CB  . SER A 1 160 ? 8.765   -14.732 3.820   1.00   59.76  ? 175 SER A CB  1 
ATOM   954  O  OG  . SER A 1 160 ? 7.884   -13.661 3.581   1.00   59.38  ? 175 SER A OG  1 
ATOM   955  N  N   . VAL A 1 161 ? 8.588   -14.668 6.751   1.00   58.48  ? 176 VAL A N   1 
ATOM   956  C  CA  . VAL A 1 161 ? 8.083   -14.369 8.064   1.00   57.85  ? 176 VAL A CA  1 
ATOM   957  C  C   . VAL A 1 161 ? 9.258   -14.030 8.920   1.00   56.11  ? 176 VAL A C   1 
ATOM   958  O  O   . VAL A 1 161 ? 9.302   -12.978 9.562   1.00   55.71  ? 176 VAL A O   1 
ATOM   959  C  CB  . VAL A 1 161 ? 7.408   -15.593 8.669   1.00   60.06  ? 176 VAL A CB  1 
ATOM   960  C  CG1 . VAL A 1 161 ? 6.981   -15.324 10.111  1.00   60.48  ? 176 VAL A CG1 1 
ATOM   961  C  CG2 . VAL A 1 161 ? 6.231   -15.997 7.793   1.00   60.92  ? 176 VAL A CG2 1 
ATOM   962  N  N   . VAL A 1 162 ? 10.225  -14.936 8.898   1.00   56.80  ? 177 VAL A N   1 
ATOM   963  C  CA  . VAL A 1 162 ? 11.373  -14.817 9.761   1.00   57.98  ? 177 VAL A CA  1 
ATOM   964  C  C   . VAL A 1 162 ? 12.065  -13.493 9.448   1.00   57.63  ? 177 VAL A C   1 
ATOM   965  O  O   . VAL A 1 162 ? 12.320  -12.736 10.366  1.00   60.17  ? 177 VAL A O   1 
ATOM   966  C  CB  . VAL A 1 162 ? 12.312  -16.055 9.681   1.00   59.87  ? 177 VAL A CB  1 
ATOM   967  C  CG1 . VAL A 1 162 ? 11.517  -17.344 9.858   1.00   60.47  ? 177 VAL A CG1 1 
ATOM   968  C  CG2 . VAL A 1 162 ? 13.088  -16.108 8.371   1.00   60.24  ? 177 VAL A CG2 1 
ATOM   969  N  N   . LEU A 1 163 ? 12.280  -13.175 8.165   1.00   56.68  ? 178 LEU A N   1 
ATOM   970  C  CA  . LEU A 1 163 ? 12.971  -11.931 7.760   1.00   56.13  ? 178 LEU A CA  1 
ATOM   971  C  C   . LEU A 1 163 ? 12.165  -10.701 8.066   1.00   55.51  ? 178 LEU A C   1 
ATOM   972  O  O   . LEU A 1 163 ? 12.695  -9.678  8.489   1.00   52.57  ? 178 LEU A O   1 
ATOM   973  C  CB  . LEU A 1 163 ? 13.245  -11.904 6.252   1.00   56.14  ? 178 LEU A CB  1 
ATOM   974  C  CG  . LEU A 1 163 ? 14.157  -12.974 5.663   1.00   56.34  ? 178 LEU A CG  1 
ATOM   975  C  CD1 . LEU A 1 163 ? 14.282  -12.772 4.162   1.00   55.82  ? 178 LEU A CD1 1 
ATOM   976  C  CD2 . LEU A 1 163 ? 15.507  -12.943 6.346   1.00   55.79  ? 178 LEU A CD2 1 
ATOM   977  N  N   . MET A 1 164 ? 10.881  -10.795 7.762   1.00   59.84  ? 179 MET A N   1 
ATOM   978  C  CA  . MET A 1 164 ? 9.914   -9.786  8.150   1.00   60.72  ? 179 MET A CA  1 
ATOM   979  C  C   . MET A 1 164 ? 10.092  -9.477  9.595   1.00   55.66  ? 179 MET A C   1 
ATOM   980  O  O   . MET A 1 164 ? 10.157  -8.328  9.987   1.00   55.42  ? 179 MET A O   1 
ATOM   981  C  CB  . MET A 1 164 ? 8.495   -10.311 7.975   1.00   68.73  ? 179 MET A CB  1 
ATOM   982  C  CG  . MET A 1 164 ? 7.815   -9.862  6.693   1.00   74.04  ? 179 MET A CG  1 
ATOM   983  S  SD  . MET A 1 164 ? 7.389   -8.112  6.696   1.00   84.12  ? 179 MET A SD  1 
ATOM   984  C  CE  . MET A 1 164 ? 6.735   -7.882  8.359   1.00   82.08  ? 179 MET A CE  1 
ATOM   985  N  N   . ARG A 1 165 ? 10.146  -10.518 10.397  1.00   52.31  ? 180 ARG A N   1 
ATOM   986  C  CA  . ARG A 1 165 ? 10.294  -10.315 11.801  1.00   53.05  ? 180 ARG A CA  1 
ATOM   987  C  C   . ARG A 1 165 ? 11.579  -9.541  12.098  1.00   49.92  ? 180 ARG A C   1 
ATOM   988  O  O   . ARG A 1 165 ? 11.584  -8.539  12.812  1.00   50.32  ? 180 ARG A O   1 
ATOM   989  C  CB  . ARG A 1 165 ? 10.306  -11.660 12.508  1.00   57.28  ? 180 ARG A CB  1 
ATOM   990  C  CG  . ARG A 1 165 ? 10.051  -11.558 14.000  1.00   59.51  ? 180 ARG A CG  1 
ATOM   991  C  CD  . ARG A 1 165 ? 9.985   -12.933 14.622  1.00   61.57  ? 180 ARG A CD  1 
ATOM   992  N  NE  . ARG A 1 165 ? 8.762   -13.640 14.258  1.00   64.34  ? 180 ARG A NE  1 
ATOM   993  C  CZ  . ARG A 1 165 ? 8.698   -14.801 13.603  1.00   67.97  ? 180 ARG A CZ  1 
ATOM   994  N  NH1 . ARG A 1 165 ? 9.803   -15.441 13.213  1.00   68.16  ? 180 ARG A NH1 1 
ATOM   995  N  NH2 . ARG A 1 165 ? 7.503   -15.344 13.355  1.00   70.31  ? 180 ARG A NH2 1 
ATOM   996  N  N   . ALA A 1 166 ? 12.670  -10.007 11.521  1.00   46.96  ? 181 ALA A N   1 
ATOM   997  C  CA  . ALA A 1 166 ? 13.952  -9.455  11.806  1.00   43.98  ? 181 ALA A CA  1 
ATOM   998  C  C   . ALA A 1 166 ? 14.004  -7.995  11.435  1.00   42.67  ? 181 ALA A C   1 
ATOM   999  O  O   . ALA A 1 166 ? 14.435  -7.183  12.260  1.00   41.58  ? 181 ALA A O   1 
ATOM   1000 C  CB  . ALA A 1 166 ? 15.011  -10.236 11.079  1.00   44.19  ? 181 ALA A CB  1 
ATOM   1001 N  N   . VAL A 1 167 ? 13.538  -7.627  10.235  1.00   41.80  ? 182 VAL A N   1 
ATOM   1002 C  CA  . VAL A 1 167 ? 13.650  -6.200  9.837   1.00   41.77  ? 182 VAL A CA  1 
ATOM   1003 C  C   . VAL A 1 167 ? 12.672  -5.347  10.623  1.00   41.34  ? 182 VAL A C   1 
ATOM   1004 O  O   . VAL A 1 167 ? 13.009  -4.238  11.041  1.00   41.96  ? 182 VAL A O   1 
ATOM   1005 C  CB  . VAL A 1 167 ? 13.552  -5.881  8.315   1.00   41.66  ? 182 VAL A CB  1 
ATOM   1006 C  CG1 . VAL A 1 167 ? 14.129  -7.002  7.471   1.00   42.22  ? 182 VAL A CG1 1 
ATOM   1007 C  CG2 . VAL A 1 167 ? 12.139  -5.516  7.879   1.00   42.24  ? 182 VAL A CG2 1 
ATOM   1008 N  N   . THR A 1 168 ? 11.479  -5.870  10.860  1.00   41.08  ? 183 THR A N   1 
ATOM   1009 C  CA  . THR A 1 168 ? 10.551  -5.185  11.748  1.00   41.38  ? 183 THR A CA  1 
ATOM   1010 C  C   . THR A 1 168 ? 11.193  -4.946  13.108  1.00   40.34  ? 183 THR A C   1 
ATOM   1011 O  O   . THR A 1 168 ? 11.157  -3.827  13.583  1.00   38.54  ? 183 THR A O   1 
ATOM   1012 C  CB  . THR A 1 168 ? 9.214   -5.937  11.862  1.00   43.19  ? 183 THR A CB  1 
ATOM   1013 O  OG1 . THR A 1 168 ? 8.717   -6.199  10.540  1.00   43.28  ? 183 THR A OG1 1 
ATOM   1014 C  CG2 . THR A 1 168 ? 8.180   -5.113  12.634  1.00   44.09  ? 183 THR A CG2 1 
ATOM   1015 N  N   . ASN A 1 169 ? 11.834  -5.968  13.689  1.00   41.69  ? 184 ASN A N   1 
ATOM   1016 C  CA  . ASN A 1 169 ? 12.467  -5.818  15.013  1.00   43.12  ? 184 ASN A CA  1 
ATOM   1017 C  C   . ASN A 1 169 ? 13.547  -4.767  14.971  1.00   42.04  ? 184 ASN A C   1 
ATOM   1018 O  O   . ASN A 1 169 ? 13.630  -3.929  15.853  1.00   41.97  ? 184 ASN A O   1 
ATOM   1019 C  CB  . ASN A 1 169 ? 13.047  -7.128  15.555  1.00   45.05  ? 184 ASN A CB  1 
ATOM   1020 C  CG  . ASN A 1 169 ? 12.904  -7.255  17.084  1.00   48.23  ? 184 ASN A CG  1 
ATOM   1021 O  OD1 . ASN A 1 169 ? 12.721  -6.265  17.808  1.00   49.68  ? 184 ASN A OD1 1 
ATOM   1022 N  ND2 . ASN A 1 169 ? 12.980  -8.491  17.579  1.00   49.25  ? 184 ASN A ND2 1 
ATOM   1023 N  N   . VAL A 1 170 ? 14.354  -4.780  13.918  1.00   41.54  ? 185 VAL A N   1 
ATOM   1024 C  CA  . VAL A 1 170 ? 15.387  -3.751  13.752  1.00   41.25  ? 185 VAL A CA  1 
ATOM   1025 C  C   . VAL A 1 170 ? 14.799  -2.341  13.866  1.00   40.80  ? 185 VAL A C   1 
ATOM   1026 O  O   . VAL A 1 170 ? 15.408  -1.477  14.496  1.00   40.87  ? 185 VAL A O   1 
ATOM   1027 C  CB  . VAL A 1 170 ? 16.078  -3.854  12.375  1.00   41.59  ? 185 VAL A CB  1 
ATOM   1028 C  CG1 . VAL A 1 170 ? 16.934  -2.626  12.100  1.00   41.44  ? 185 VAL A CG1 1 
ATOM   1029 C  CG2 . VAL A 1 170 ? 16.943  -5.103  12.296  1.00   42.72  ? 185 VAL A CG2 1 
ATOM   1030 N  N   . ILE A 1 171 ? 13.631  -2.118  13.234  1.00   39.24  ? 186 ILE A N   1 
ATOM   1031 C  CA  . ILE A 1 171 ? 13.002  -0.802  13.152  1.00   37.26  ? 186 ILE A CA  1 
ATOM   1032 C  C   . ILE A 1 171 ? 12.304  -0.472  14.473  1.00   37.41  ? 186 ILE A C   1 
ATOM   1033 O  O   . ILE A 1 171 ? 12.341  0.677   14.908  1.00   36.33  ? 186 ILE A O   1 
ATOM   1034 C  CB  . ILE A 1 171 ? 12.006  -0.737  11.974  1.00   37.06  ? 186 ILE A CB  1 
ATOM   1035 C  CG1 . ILE A 1 171 ? 12.682  -1.103  10.645  1.00   37.09  ? 186 ILE A CG1 1 
ATOM   1036 C  CG2 . ILE A 1 171 ? 11.348  0.632   11.861  1.00   36.68  ? 186 ILE A CG2 1 
ATOM   1037 C  CD1 . ILE A 1 171 ? 13.467  0.017   10.002  1.00   36.51  ? 186 ILE A CD1 1 
ATOM   1038 N  N   . CYS A 1 172 ? 11.662  -1.455  15.105  1.00   38.48  ? 187 CYS A N   1 
ATOM   1039 C  CA  . CYS A 1 172 ? 11.213  -1.277  16.506  1.00   41.57  ? 187 CYS A CA  1 
ATOM   1040 C  C   . CYS A 1 172 ? 12.352  -0.790  17.388  1.00   42.47  ? 187 CYS A C   1 
ATOM   1041 O  O   . CYS A 1 172 ? 12.168  0.153   18.143  1.00   41.84  ? 187 CYS A O   1 
ATOM   1042 C  CB  . CYS A 1 172 ? 10.677  -2.557  17.127  1.00   42.45  ? 187 CYS A CB  1 
ATOM   1043 S  SG  . CYS A 1 172 ? 9.350   -3.304  16.189  1.00   44.57  ? 187 CYS A SG  1 
ATOM   1044 N  N   . ARG A 1 173 ? 13.513  -1.445  17.266  1.00   44.02  ? 188 ARG A N   1 
ATOM   1045 C  CA  . ARG A 1 173 ? 14.731  -1.118  18.040  1.00   46.84  ? 188 ARG A CA  1 
ATOM   1046 C  C   . ARG A 1 173 ? 15.218  0.294   17.746  1.00   46.85  ? 188 ARG A C   1 
ATOM   1047 O  O   . ARG A 1 173 ? 15.438  1.088   18.648  1.00   49.77  ? 188 ARG A O   1 
ATOM   1048 C  CB  . ARG A 1 173 ? 15.883  -2.114  17.729  1.00   47.69  ? 188 ARG A CB  1 
ATOM   1049 C  CG  . ARG A 1 173 ? 16.014  -3.297  18.679  1.00   48.91  ? 188 ARG A CG  1 
ATOM   1050 C  CD  . ARG A 1 173 ? 17.114  -3.094  19.723  1.00   49.96  ? 188 ARG A CD  1 
ATOM   1051 N  NE  . ARG A 1 173 ? 18.200  -4.062  19.560  1.00   51.23  ? 188 ARG A NE  1 
ATOM   1052 C  CZ  . ARG A 1 173 ? 19.399  -3.986  20.147  1.00   53.19  ? 188 ARG A CZ  1 
ATOM   1053 N  NH1 . ARG A 1 173 ? 19.714  -2.977  20.942  1.00   54.65  ? 188 ARG A NH1 1 
ATOM   1054 N  NH2 . ARG A 1 173 ? 20.314  -4.922  19.936  1.00   54.06  ? 188 ARG A NH2 1 
ATOM   1055 N  N   . LEU A 1 174 ? 15.380  0.598   16.471  1.00   45.51  ? 189 LEU A N   1 
ATOM   1056 C  CA  . LEU A 1 174 ? 15.933  1.870   16.041  1.00   45.39  ? 189 LEU A CA  1 
ATOM   1057 C  C   . LEU A 1 174 ? 15.009  3.063   16.345  1.00   45.85  ? 189 LEU A C   1 
ATOM   1058 O  O   . LEU A 1 174 ? 15.470  4.165   16.713  1.00   46.54  ? 189 LEU A O   1 
ATOM   1059 C  CB  . LEU A 1 174 ? 16.217  1.785   14.546  1.00   44.95  ? 189 LEU A CB  1 
ATOM   1060 C  CG  . LEU A 1 174 ? 16.688  3.064   13.881  1.00   45.13  ? 189 LEU A CG  1 
ATOM   1061 C  CD1 . LEU A 1 174 ? 17.974  3.561   14.527  1.00   47.03  ? 189 LEU A CD1 1 
ATOM   1062 C  CD2 . LEU A 1 174 ? 16.875  2.778   12.416  1.00   44.38  ? 189 LEU A CD2 1 
ATOM   1063 N  N   . VAL A 1 175 ? 13.709  2.851   16.197  1.00   45.18  ? 190 VAL A N   1 
ATOM   1064 C  CA  . VAL A 1 175 ? 12.758  3.896   16.513  1.00   45.85  ? 190 VAL A CA  1 
ATOM   1065 C  C   . VAL A 1 175 ? 12.354  4.014   17.999  1.00   47.38  ? 190 VAL A C   1 
ATOM   1066 O  O   . VAL A 1 175 ? 12.271  5.135   18.481  1.00   47.60  ? 190 VAL A O   1 
ATOM   1067 C  CB  . VAL A 1 175 ? 11.507  3.765   15.640  1.00   45.28  ? 190 VAL A CB  1 
ATOM   1068 C  CG1 . VAL A 1 175 ? 10.477  4.860   15.982  1.00   45.26  ? 190 VAL A CG1 1 
ATOM   1069 C  CG2 . VAL A 1 175 ? 11.908  3.810   14.175  1.00   42.82  ? 190 VAL A CG2 1 
ATOM   1070 N  N   . PHE A 1 176 ? 12.065  2.915   18.711  1.00   49.46  ? 191 PHE A N   1 
ATOM   1071 C  CA  . PHE A 1 176 ? 11.635  3.022   20.150  1.00   52.45  ? 191 PHE A CA  1 
ATOM   1072 C  C   . PHE A 1 176 ? 12.628  2.520   21.163  1.00   53.03  ? 191 PHE A C   1 
ATOM   1073 O  O   . PHE A 1 176 ? 12.363  2.665   22.352  1.00   57.96  ? 191 PHE A O   1 
ATOM   1074 C  CB  . PHE A 1 176 ? 10.399  2.206   20.559  1.00   53.55  ? 191 PHE A CB  1 
ATOM   1075 C  CG  . PHE A 1 176 ? 9.513   1.807   19.455  1.00   55.26  ? 191 PHE A CG  1 
ATOM   1076 C  CD1 . PHE A 1 176 ? 9.229   2.682   18.428  1.00   57.32  ? 191 PHE A CD1 1 
ATOM   1077 C  CD2 . PHE A 1 176 ? 8.927   0.546   19.466  1.00   56.10  ? 191 PHE A CD2 1 
ATOM   1078 C  CE1 . PHE A 1 176 ? 8.390   2.301   17.392  1.00   59.37  ? 191 PHE A CE1 1 
ATOM   1079 C  CE2 . PHE A 1 176 ? 8.093   0.155   18.442  1.00   57.80  ? 191 PHE A CE2 1 
ATOM   1080 C  CZ  . PHE A 1 176 ? 7.813   1.036   17.403  1.00   58.86  ? 191 PHE A CZ  1 
ATOM   1081 N  N   . SER A 1 177 ? 13.708  1.877   20.732  1.00   50.85  ? 192 SER A N   1 
ATOM   1082 C  CA  . SER A 1 177 ? 14.570  1.094   21.644  1.00   50.10  ? 192 SER A CA  1 
ATOM   1083 C  C   . SER A 1 177 ? 13.789  -0.073  22.220  1.00   51.55  ? 192 SER A C   1 
ATOM   1084 O  O   . SER A 1 177 ? 13.954  -0.407  23.384  1.00   52.08  ? 192 SER A O   1 
ATOM   1085 C  CB  . SER A 1 177 ? 15.175  1.929   22.787  1.00   49.32  ? 192 SER A CB  1 
ATOM   1086 O  OG  . SER A 1 177 ? 16.061  2.922   22.319  1.00   47.92  ? 192 SER A OG  1 
ATOM   1087 N  N   . SER A 1 178 ? 12.938  -0.690  21.402  1.00   51.69  ? 193 SER A N   1 
ATOM   1088 C  CA  . SER A 1 178 ? 12.275  -1.922  21.806  1.00   53.07  ? 193 SER A CA  1 
ATOM   1089 C  C   . SER A 1 178 ? 13.299  -3.003  22.143  1.00   54.58  ? 193 SER A C   1 
ATOM   1090 O  O   . SER A 1 178 ? 14.446  -2.995  21.662  1.00   54.75  ? 193 SER A O   1 
ATOM   1091 C  CB  . SER A 1 178 ? 11.365  -2.458  20.703  1.00   52.79  ? 193 SER A CB  1 
ATOM   1092 O  OG  . SER A 1 178 ? 12.057  -3.427  19.904  1.00   53.18  ? 193 SER A OG  1 
ATOM   1093 N  N   . SER A 1 179 ? 12.869  -3.958  22.953  1.00   57.12  ? 194 SER A N   1 
ATOM   1094 C  CA  . SER A 1 179 ? 13.737  -5.052  23.341  1.00   58.96  ? 194 SER A CA  1 
ATOM   1095 C  C   . SER A 1 179 ? 13.072  -6.398  23.156  1.00   60.25  ? 194 SER A C   1 
ATOM   1096 O  O   . SER A 1 179 ? 13.459  -7.392  23.770  1.00   61.01  ? 194 SER A O   1 
ATOM   1097 C  CB  . SER A 1 179 ? 14.196  -4.868  24.781  1.00   59.76  ? 194 SER A CB  1 
ATOM   1098 O  OG  . SER A 1 179 ? 15.464  -5.465  24.893  1.00   60.56  ? 194 SER A OG  1 
ATOM   1099 N  N   . TYR A 1 180 ? 12.093  -6.415  22.264  1.00   62.37  ? 195 TYR A N   1 
ATOM   1100 C  CA  . TYR A 1 180 ? 11.347  -7.611  21.931  1.00   64.62  ? 195 TYR A CA  1 
ATOM   1101 C  C   . TYR A 1 180 ? 12.290  -8.703  21.552  1.00   66.58  ? 195 TYR A C   1 
ATOM   1102 O  O   . TYR A 1 180 ? 13.326  -8.454  20.945  1.00   68.41  ? 195 TYR A O   1 
ATOM   1103 C  CB  . TYR A 1 180 ? 10.443  -7.382  20.709  1.00   63.81  ? 195 TYR A CB  1 
ATOM   1104 C  CG  . TYR A 1 180 ? 9.581   -6.169  20.808  1.00   62.51  ? 195 TYR A CG  1 
ATOM   1105 C  CD1 . TYR A 1 180 ? 8.881   -5.903  21.983  1.00   62.20  ? 195 TYR A CD1 1 
ATOM   1106 C  CD2 . TYR A 1 180 ? 9.452   -5.288  19.726  1.00   60.48  ? 195 TYR A CD2 1 
ATOM   1107 C  CE1 . TYR A 1 180 ? 8.082   -4.791  22.094  1.00   62.93  ? 195 TYR A CE1 1 
ATOM   1108 C  CE2 . TYR A 1 180 ? 8.646   -4.170  19.824  1.00   60.75  ? 195 TYR A CE2 1 
ATOM   1109 C  CZ  . TYR A 1 180 ? 7.968   -3.929  21.015  1.00   62.51  ? 195 TYR A CZ  1 
ATOM   1110 O  OH  . TYR A 1 180 ? 7.176   -2.829  21.157  1.00   63.85  ? 195 TYR A OH  1 
ATOM   1111 N  N   . GLN A 1 181 ? 11.912  -9.919  21.899  1.00   71.58  ? 196 GLN A N   1 
ATOM   1112 C  CA  . GLN A 1 181 ? 12.507  -11.097 21.301  1.00   74.67  ? 196 GLN A CA  1 
ATOM   1113 C  C   . GLN A 1 181 ? 11.470  -11.661 20.324  1.00   73.34  ? 196 GLN A C   1 
ATOM   1114 O  O   . GLN A 1 181 ? 10.354  -11.164 20.278  1.00   76.63  ? 196 GLN A O   1 
ATOM   1115 C  CB  . GLN A 1 181 ? 12.971  -12.068 22.400  1.00   78.05  ? 196 GLN A CB  1 
ATOM   1116 C  CG  . GLN A 1 181 ? 14.445  -11.853 22.753  1.00   79.00  ? 196 GLN A CG  1 
ATOM   1117 C  CD  . GLN A 1 181 ? 14.805  -12.202 24.188  1.00   86.19  ? 196 GLN A CD  1 
ATOM   1118 O  OE1 . GLN A 1 181 ? 13.936  -12.309 25.061  1.00   90.43  ? 196 GLN A OE1 1 
ATOM   1119 N  NE2 . GLN A 1 181 ? 16.105  -12.378 24.445  1.00   88.16  ? 196 GLN A NE2 1 
ATOM   1120 N  N   . PRO A 1 182 ? 11.844  -12.645 19.495  1.00   73.58  ? 197 PRO A N   1 
ATOM   1121 C  CA  . PRO A 1 182 ? 10.947  -13.131 18.437  1.00   74.17  ? 197 PRO A CA  1 
ATOM   1122 C  C   . PRO A 1 182 ? 9.516   -13.443 18.868  1.00   75.77  ? 197 PRO A C   1 
ATOM   1123 O  O   . PRO A 1 182 ? 8.566   -13.048 18.185  1.00   78.10  ? 197 PRO A O   1 
ATOM   1124 C  CB  . PRO A 1 182 ? 11.639  -14.410 17.968  1.00   74.64  ? 197 PRO A CB  1 
ATOM   1125 C  CG  . PRO A 1 182 ? 13.083  -14.086 18.116  1.00   74.67  ? 197 PRO A CG  1 
ATOM   1126 C  CD  . PRO A 1 182 ? 13.183  -13.249 19.374  1.00   74.40  ? 197 PRO A CD  1 
ATOM   1127 N  N   . SER A 1 183 ? 9.371   -14.144 19.988  1.00   75.29  ? 198 SER A N   1 
ATOM   1128 C  CA  . SER A 1 183 ? 8.065   -14.597 20.448  1.00   75.68  ? 198 SER A CA  1 
ATOM   1129 C  C   . SER A 1 183 ? 7.152   -13.429 20.856  1.00   76.35  ? 198 SER A C   1 
ATOM   1130 O  O   . SER A 1 183 ? 5.920   -13.526 20.768  1.00   77.73  ? 198 SER A O   1 
ATOM   1131 C  CB  . SER A 1 183 ? 8.252   -15.545 21.626  1.00   76.99  ? 198 SER A CB  1 
ATOM   1132 O  OG  . SER A 1 183 ? 8.500   -14.824 22.828  1.00   78.85  ? 198 SER A OG  1 
ATOM   1133 N  N   . ASP A 1 184 ? 7.776   -12.332 21.288  1.00   74.83  ? 199 ASP A N   1 
ATOM   1134 C  CA  . ASP A 1 184 ? 7.092   -11.220 21.950  1.00   73.54  ? 199 ASP A CA  1 
ATOM   1135 C  C   . ASP A 1 184 ? 5.779   -10.893 21.278  1.00   70.57  ? 199 ASP A C   1 
ATOM   1136 O  O   . ASP A 1 184 ? 5.721   -10.756 20.054  1.00   71.46  ? 199 ASP A O   1 
ATOM   1137 C  CB  . ASP A 1 184 ? 7.975   -9.964  21.998  1.00   72.71  ? 199 ASP A CB  1 
ATOM   1138 C  CG  . ASP A 1 184 ? 7.424   -8.895  22.933  1.00   73.84  ? 199 ASP A CG  1 
ATOM   1139 O  OD1 . ASP A 1 184 ? 6.399   -8.264  22.585  1.00   69.85  ? 199 ASP A OD1 1 
ATOM   1140 O  OD2 . ASP A 1 184 ? 8.035   -8.678  24.012  1.00   76.33  ? 199 ASP A OD2 1 
ATOM   1141 N  N   . PRO A 1 185 ? 4.724   -10.762 22.081  1.00   67.59  ? 200 PRO A N   1 
ATOM   1142 C  CA  . PRO A 1 185 ? 3.417   -10.420 21.546  1.00   65.42  ? 200 PRO A CA  1 
ATOM   1143 C  C   . PRO A 1 185 ? 3.286   -9.008  20.972  1.00   61.66  ? 200 PRO A C   1 
ATOM   1144 O  O   . PRO A 1 185 ? 2.546   -8.829  20.012  1.00   61.49  ? 200 PRO A O   1 
ATOM   1145 C  CB  . PRO A 1 185 ? 2.497   -10.567 22.755  1.00   68.33  ? 200 PRO A CB  1 
ATOM   1146 C  CG  . PRO A 1 185 ? 3.241   -11.430 23.718  1.00   70.03  ? 200 PRO A CG  1 
ATOM   1147 C  CD  . PRO A 1 185 ? 4.673   -11.110 23.513  1.00   68.56  ? 200 PRO A CD  1 
ATOM   1148 N  N   . GLU A 1 186 ? 3.951   -8.013  21.556  1.00   59.46  ? 201 GLU A N   1 
ATOM   1149 C  CA  . GLU A 1 186 ? 3.775   -6.629  21.098  1.00   57.85  ? 201 GLU A CA  1 
ATOM   1150 C  C   . GLU A 1 186 ? 4.412   -6.447  19.734  1.00   55.31  ? 201 GLU A C   1 
ATOM   1151 O  O   . GLU A 1 186 ? 3.918   -5.689  18.919  1.00   54.51  ? 201 GLU A O   1 
ATOM   1152 C  CB  . GLU A 1 186 ? 4.334   -5.591  22.089  1.00   58.52  ? 201 GLU A CB  1 
ATOM   1153 C  CG  . GLU A 1 186 ? 3.938   -4.156  21.713  1.00   59.26  ? 201 GLU A CG  1 
ATOM   1154 C  CD  . GLU A 1 186 ? 4.382   -3.087  22.705  1.00   61.01  ? 201 GLU A CD  1 
ATOM   1155 O  OE1 . GLU A 1 186 ? 5.594   -2.998  23.010  1.00   61.49  ? 201 GLU A OE1 1 
ATOM   1156 O  OE2 . GLU A 1 186 ? 3.518   -2.296  23.155  1.00   62.90  ? 201 GLU A OE2 1 
ATOM   1157 N  N   . LEU A 1 187 ? 5.518   -7.140  19.507  1.00   54.18  ? 202 LEU A N   1 
ATOM   1158 C  CA  . LEU A 1 187 ? 6.148   -7.185  18.205  1.00   53.78  ? 202 LEU A CA  1 
ATOM   1159 C  C   . LEU A 1 187 ? 5.165   -7.803  17.229  1.00   54.11  ? 202 LEU A C   1 
ATOM   1160 O  O   . LEU A 1 187 ? 4.953   -7.288  16.140  1.00   50.54  ? 202 LEU A O   1 
ATOM   1161 C  CB  . LEU A 1 187 ? 7.453   -8.009  18.259  1.00   53.91  ? 202 LEU A CB  1 
ATOM   1162 C  CG  . LEU A 1 187 ? 8.090   -8.580  16.976  1.00   52.33  ? 202 LEU A CG  1 
ATOM   1163 C  CD1 . LEU A 1 187 ? 8.604   -7.490  16.071  1.00   50.41  ? 202 LEU A CD1 1 
ATOM   1164 C  CD2 . LEU A 1 187 ? 9.224   -9.539  17.317  1.00   52.98  ? 202 LEU A CD2 1 
ATOM   1165 N  N   . GLN A 1 188 ? 4.570   -8.909  17.652  1.00   57.55  ? 203 GLN A N   1 
ATOM   1166 C  CA  . GLN A 1 188 ? 3.570   -9.619  16.869  1.00   60.62  ? 203 GLN A CA  1 
ATOM   1167 C  C   . GLN A 1 188 ? 2.367   -8.728  16.505  1.00   58.82  ? 203 GLN A C   1 
ATOM   1168 O  O   . GLN A 1 188 ? 1.824   -8.837  15.406  1.00   56.68  ? 203 GLN A O   1 
ATOM   1169 C  CB  . GLN A 1 188 ? 3.116   -10.870 17.638  1.00   67.10  ? 203 GLN A CB  1 
ATOM   1170 C  CG  . GLN A 1 188 ? 2.515   -11.959 16.775  1.00   73.18  ? 203 GLN A CG  1 
ATOM   1171 C  CD  . GLN A 1 188 ? 3.406   -12.308 15.598  1.00   76.67  ? 203 GLN A CD  1 
ATOM   1172 O  OE1 . GLN A 1 188 ? 4.640   -12.399 15.743  1.00   78.53  ? 203 GLN A OE1 1 
ATOM   1173 N  NE2 . GLN A 1 188 ? 2.793   -12.484 14.413  1.00   77.83  ? 203 GLN A NE2 1 
ATOM   1174 N  N   . THR A 1 189 ? 1.971   -7.846  17.423  1.00   57.82  ? 204 THR A N   1 
ATOM   1175 C  CA  . THR A 1 189 ? 0.924   -6.854  17.161  1.00   57.99  ? 204 THR A CA  1 
ATOM   1176 C  C   . THR A 1 189 ? 1.269   -5.965  15.975  1.00   55.88  ? 204 THR A C   1 
ATOM   1177 O  O   . THR A 1 189 ? 0.433   -5.723  15.110  1.00   57.88  ? 204 THR A O   1 
ATOM   1178 C  CB  . THR A 1 189 ? 0.710   -5.937  18.386  1.00   58.99  ? 204 THR A CB  1 
ATOM   1179 O  OG1 . THR A 1 189 ? 0.186   -6.701  19.486  1.00   60.27  ? 204 THR A OG1 1 
ATOM   1180 C  CG2 . THR A 1 189 ? -0.243  -4.784  18.055  1.00   58.77  ? 204 THR A CG2 1 
ATOM   1181 N  N   . VAL A 1 190 ? 2.507   -5.478  15.977  1.00   53.96  ? 205 VAL A N   1 
ATOM   1182 C  CA  . VAL A 1 190 ? 3.038   -4.538  14.992  1.00   51.79  ? 205 VAL A CA  1 
ATOM   1183 C  C   . VAL A 1 190 ? 3.103   -5.164  13.624  1.00   50.91  ? 205 VAL A C   1 
ATOM   1184 O  O   . VAL A 1 190 ? 2.738   -4.549  12.635  1.00   50.05  ? 205 VAL A O   1 
ATOM   1185 C  CB  . VAL A 1 190 ? 4.476   -4.100  15.368  1.00   51.42  ? 205 VAL A CB  1 
ATOM   1186 C  CG1 . VAL A 1 190 ? 5.120   -3.299  14.248  1.00   49.84  ? 205 VAL A CG1 1 
ATOM   1187 C  CG2 . VAL A 1 190 ? 4.483   -3.302  16.661  1.00   52.03  ? 205 VAL A CG2 1 
ATOM   1188 N  N   . ILE A 1 191 ? 3.603   -6.387  13.561  1.00   51.89  ? 206 ILE A N   1 
ATOM   1189 C  CA  . ILE A 1 191 ? 3.634   -7.087  12.290  1.00   52.15  ? 206 ILE A CA  1 
ATOM   1190 C  C   . ILE A 1 191 ? 2.215   -7.258  11.802  1.00   52.41  ? 206 ILE A C   1 
ATOM   1191 O  O   . ILE A 1 191 ? 1.977   -7.192  10.615  1.00   51.34  ? 206 ILE A O   1 
ATOM   1192 C  CB  . ILE A 1 191 ? 4.298   -8.471  12.371  1.00   52.27  ? 206 ILE A CB  1 
ATOM   1193 C  CG1 . ILE A 1 191 ? 5.803   -8.317  12.375  1.00   51.88  ? 206 ILE A CG1 1 
ATOM   1194 C  CG2 . ILE A 1 191 ? 3.907   -9.344  11.178  1.00   52.13  ? 206 ILE A CG2 1 
ATOM   1195 C  CD1 . ILE A 1 191 ? 6.348   -7.955  13.707  1.00   53.50  ? 206 ILE A CD1 1 
ATOM   1196 N  N   . GLN A 1 192 ? 1.284   -7.498  12.719  1.00   55.31  ? 207 GLN A N   1 
ATOM   1197 C  CA  . GLN A 1 192 ? -0.103  -7.696  12.326  1.00   57.61  ? 207 GLN A CA  1 
ATOM   1198 C  C   . GLN A 1 192 ? -0.783  -6.422  11.814  1.00   55.83  ? 207 GLN A C   1 
ATOM   1199 O  O   . GLN A 1 192 ? -1.533  -6.513  10.836  1.00   55.93  ? 207 GLN A O   1 
ATOM   1200 C  CB  . GLN A 1 192 ? -0.923  -8.354  13.423  1.00   60.77  ? 207 GLN A CB  1 
ATOM   1201 C  CG  . GLN A 1 192 ? -0.508  -9.795  13.712  1.00   64.67  ? 207 GLN A CG  1 
ATOM   1202 C  CD  . GLN A 1 192 ? -0.358  -10.675 12.475  1.00   66.71  ? 207 GLN A CD  1 
ATOM   1203 O  OE1 . GLN A 1 192 ? 0.752   -10.873 11.977  1.00   66.35  ? 207 GLN A OE1 1 
ATOM   1204 N  NE2 . GLN A 1 192 ? -1.479  -11.221 11.981  1.00   70.28  ? 207 GLN A NE2 1 
ATOM   1205 N  N   . TYR A 1 193 ? -0.515  -5.249  12.394  1.00   53.17  ? 208 TYR A N   1 
ATOM   1206 C  CA  . TYR A 1 193 ? -1.128  -4.050  11.826  1.00   53.01  ? 208 TYR A CA  1 
ATOM   1207 C  C   . TYR A 1 193 ? -0.424  -3.539  10.575  1.00   50.75  ? 208 TYR A C   1 
ATOM   1208 O  O   . TYR A 1 193 ? -1.096  -3.121  9.620   1.00   47.92  ? 208 TYR A O   1 
ATOM   1209 C  CB  . TYR A 1 193 ? -1.381  -2.942  12.839  1.00   54.70  ? 208 TYR A CB  1 
ATOM   1210 C  CG  . TYR A 1 193 ? -0.206  -2.263  13.476  1.00   56.10  ? 208 TYR A CG  1 
ATOM   1211 C  CD1 . TYR A 1 193 ? 0.698   -1.476  12.732  1.00   55.12  ? 208 TYR A CD1 1 
ATOM   1212 C  CD2 . TYR A 1 193 ? -0.038  -2.334  14.855  1.00   57.66  ? 208 TYR A CD2 1 
ATOM   1213 C  CE1 . TYR A 1 193 ? 1.754   -0.834  13.359  1.00   54.81  ? 208 TYR A CE1 1 
ATOM   1214 C  CE2 . TYR A 1 193 ? 0.998   -1.680  15.483  1.00   57.05  ? 208 TYR A CE2 1 
ATOM   1215 C  CZ  . TYR A 1 193 ? 1.883   -0.941  14.745  1.00   55.84  ? 208 TYR A CZ  1 
ATOM   1216 O  OH  . TYR A 1 193 ? 2.876   -0.326  15.442  1.00   57.13  ? 208 TYR A OH  1 
ATOM   1217 N  N   . ASN A 1 194 ? 0.912   -3.581  10.573  1.00   49.44  ? 209 ASN A N   1 
ATOM   1218 C  CA  . ASN A 1 194 ? 1.655   -3.359  9.346   1.00   47.29  ? 209 ASN A CA  1 
ATOM   1219 C  C   . ASN A 1 194 ? 1.098   -4.291  8.268   1.00   48.13  ? 209 ASN A C   1 
ATOM   1220 O  O   . ASN A 1 194 ? 0.639   -3.818  7.230   1.00   46.86  ? 209 ASN A O   1 
ATOM   1221 C  CB  . ASN A 1 194 ? 3.143   -3.582  9.544   1.00   46.48  ? 209 ASN A CB  1 
ATOM   1222 C  CG  . ASN A 1 194 ? 3.825   -2.431  10.288  1.00   46.60  ? 209 ASN A CG  1 
ATOM   1223 O  OD1 . ASN A 1 194 ? 3.330   -1.303  10.319  1.00   46.11  ? 209 ASN A OD1 1 
ATOM   1224 N  ND2 . ASN A 1 194 ? 5.001   -2.712  10.862  1.00   46.54  ? 209 ASN A ND2 1 
ATOM   1225 N  N   . ASP A 1 195 ? 1.073   -5.596  8.533   1.00   49.62  ? 210 ASP A N   1 
ATOM   1226 C  CA  . ASP A 1 195 ? 0.549   -6.578  7.557   1.00   52.13  ? 210 ASP A CA  1 
ATOM   1227 C  C   . ASP A 1 195 ? -0.848  -6.211  7.003   1.00   54.28  ? 210 ASP A C   1 
ATOM   1228 O  O   . ASP A 1 195 ? -1.090  -6.269  5.784   1.00   52.26  ? 210 ASP A O   1 
ATOM   1229 C  CB  . ASP A 1 195 ? 0.524   -7.978  8.169   1.00   54.35  ? 210 ASP A CB  1 
ATOM   1230 C  CG  . ASP A 1 195 ? 0.245   -9.065  7.153   1.00   56.87  ? 210 ASP A CG  1 
ATOM   1231 O  OD1 . ASP A 1 195 ? 1.006   -9.166  6.172   1.00   57.80  ? 210 ASP A OD1 1 
ATOM   1232 O  OD2 . ASP A 1 195 ? -0.707  -9.854  7.355   1.00   60.07  ? 210 ASP A OD2 1 
ATOM   1233 N  N   . GLY A 1 196 ? -1.752  -5.814  7.900   1.00   55.51  ? 211 GLY A N   1 
ATOM   1234 C  CA  . GLY A 1 196 ? -3.098  -5.401  7.499   1.00   55.44  ? 211 GLY A CA  1 
ATOM   1235 C  C   . GLY A 1 196 ? -3.115  -4.229  6.535   1.00   53.70  ? 211 GLY A C   1 
ATOM   1236 O  O   . GLY A 1 196 ? -3.896  -4.200  5.596   1.00   55.14  ? 211 GLY A O   1 
ATOM   1237 N  N   . ILE A 1 197 ? -2.250  -3.260  6.786   1.00   51.53  ? 212 ILE A N   1 
ATOM   1238 C  CA  . ILE A 1 197 ? -2.127  -2.089  5.941   1.00   50.16  ? 212 ILE A CA  1 
ATOM   1239 C  C   . ILE A 1 197 ? -1.624  -2.481  4.545   1.00   51.03  ? 212 ILE A C   1 
ATOM   1240 O  O   . ILE A 1 197 ? -2.220  -2.091  3.520   1.00   52.49  ? 212 ILE A O   1 
ATOM   1241 C  CB  . ILE A 1 197 ? -1.200  -1.045  6.599   1.00   48.06  ? 212 ILE A CB  1 
ATOM   1242 C  CG1 . ILE A 1 197 ? -1.896  -0.464  7.836   1.00   48.41  ? 212 ILE A CG1 1 
ATOM   1243 C  CG2 . ILE A 1 197 ? -0.854  0.057   5.613   1.00   46.89  ? 212 ILE A CG2 1 
ATOM   1244 C  CD1 . ILE A 1 197 ? -1.090  0.518   8.650   1.00   47.87  ? 212 ILE A CD1 1 
ATOM   1245 N  N   . VAL A 1 198 ? -0.554  -3.276  4.516   1.00   50.59  ? 213 VAL A N   1 
ATOM   1246 C  CA  . VAL A 1 198 ? -0.027  -3.827  3.277   1.00   50.61  ? 213 VAL A CA  1 
ATOM   1247 C  C   . VAL A 1 198 ? -1.141  -4.541  2.495   1.00   53.37  ? 213 VAL A C   1 
ATOM   1248 O  O   . VAL A 1 198 ? -1.384  -4.219  1.342   1.00   53.30  ? 213 VAL A O   1 
ATOM   1249 C  CB  . VAL A 1 198 ? 1.130   -4.816  3.528   1.00   50.24  ? 213 VAL A CB  1 
ATOM   1250 C  CG1 . VAL A 1 198 ? 1.531   -5.499  2.232   1.00   49.48  ? 213 VAL A CG1 1 
ATOM   1251 C  CG2 . VAL A 1 198 ? 2.347   -4.120  4.161   1.00   49.86  ? 213 VAL A CG2 1 
ATOM   1252 N  N   . GLN A 1 199 ? -1.816  -5.493  3.136   1.00   56.19  ? 214 GLN A N   1 
ATOM   1253 C  CA  . GLN A 1 199 ? -2.878  -6.286  2.497   1.00   57.80  ? 214 GLN A CA  1 
ATOM   1254 C  C   . GLN A 1 199 ? -3.917  -5.349  1.889   1.00   58.16  ? 214 GLN A C   1 
ATOM   1255 O  O   . GLN A 1 199 ? -4.400  -5.551  0.759   1.00   56.02  ? 214 GLN A O   1 
ATOM   1256 C  CB  . GLN A 1 199 ? -3.575  -7.225  3.525   1.00   61.60  ? 214 GLN A CB  1 
ATOM   1257 C  CG  . GLN A 1 199 ? -3.877  -8.652  3.030   1.00   65.47  ? 214 GLN A CG  1 
ATOM   1258 C  CD  . GLN A 1 199 ? -5.305  -9.180  3.352   1.00   69.96  ? 214 GLN A CD  1 
ATOM   1259 O  OE1 . GLN A 1 199 ? -6.328  -8.627  2.904   1.00   69.15  ? 214 GLN A OE1 1 
ATOM   1260 N  NE2 . GLN A 1 199 ? -5.368  -10.283 4.082   1.00   71.94  ? 214 GLN A NE2 1 
ATOM   1261 N  N   . THR A 1 200 ? -4.265  -4.323  2.656   1.00   57.71  ? 215 THR A N   1 
ATOM   1262 C  CA  . THR A 1 200 ? -5.383  -3.468  2.303   1.00   60.33  ? 215 THR A CA  1 
ATOM   1263 C  C   . THR A 1 200 ? -5.045  -2.696  1.038   1.00   59.26  ? 215 THR A C   1 
ATOM   1264 O  O   . THR A 1 200 ? -5.769  -2.737  0.066   1.00   60.66  ? 215 THR A O   1 
ATOM   1265 C  CB  . THR A 1 200 ? -5.723  -2.488  3.452   1.00   61.80  ? 215 THR A CB  1 
ATOM   1266 O  OG1 . THR A 1 200 ? -5.951  -3.216  4.666   1.00   62.69  ? 215 THR A OG1 1 
ATOM   1267 C  CG2 . THR A 1 200 ? -6.964  -1.665  3.122   1.00   62.71  ? 215 THR A CG2 1 
ATOM   1268 N  N   . ILE A 1 201 ? -3.920  -2.002  1.076   1.00   59.18  ? 216 ILE A N   1 
ATOM   1269 C  CA  . ILE A 1 201 ? -3.429  -1.208  -0.051  1.00   57.80  ? 216 ILE A CA  1 
ATOM   1270 C  C   . ILE A 1 201 ? -3.123  -2.057  -1.286  1.00   58.00  ? 216 ILE A C   1 
ATOM   1271 O  O   . ILE A 1 201 ? -3.317  -1.606  -2.402  1.00   57.11  ? 216 ILE A O   1 
ATOM   1272 C  CB  . ILE A 1 201 ? -2.145  -0.455  0.370   1.00   56.06  ? 216 ILE A CB  1 
ATOM   1273 C  CG1 . ILE A 1 201 ? -2.499  0.609   1.404   1.00   54.99  ? 216 ILE A CG1 1 
ATOM   1274 C  CG2 . ILE A 1 201 ? -1.426  0.161   -0.834  1.00   54.27  ? 216 ILE A CG2 1 
ATOM   1275 C  CD1 . ILE A 1 201 ? -1.292  1.124   2.144   1.00   55.07  ? 216 ILE A CD1 1 
ATOM   1276 N  N   . ALA A 1 202 ? -2.626  -3.272  -1.068  1.00   59.41  ? 217 ALA A N   1 
ATOM   1277 C  CA  . ALA A 1 202 ? -2.274  -4.191  -2.144  1.00   59.76  ? 217 ALA A CA  1 
ATOM   1278 C  C   . ALA A 1 202 ? -3.446  -4.435  -3.073  1.00   62.81  ? 217 ALA A C   1 
ATOM   1279 O  O   . ALA A 1 202 ? -3.279  -4.415  -4.290  1.00   64.59  ? 217 ALA A O   1 
ATOM   1280 C  CB  . ALA A 1 202 ? -1.793  -5.514  -1.571  1.00   59.80  ? 217 ALA A CB  1 
ATOM   1281 N  N   . ARG A 1 203 ? -4.621  -4.680  -2.499  1.00   66.21  ? 218 ARG A N   1 
ATOM   1282 C  CA  . ARG A 1 203 ? -5.825  -4.908  -3.286  1.00   68.60  ? 218 ARG A CA  1 
ATOM   1283 C  C   . ARG A 1 203 ? -6.198  -3.634  -4.011  1.00   69.62  ? 218 ARG A C   1 
ATOM   1284 O  O   . ARG A 1 203 ? -6.497  -3.683  -5.197  1.00   68.47  ? 218 ARG A O   1 
ATOM   1285 C  CB  . ARG A 1 203 ? -6.998  -5.338  -2.414  1.00   70.50  ? 218 ARG A CB  1 
ATOM   1286 C  CG  . ARG A 1 203 ? -6.798  -6.674  -1.726  1.00   74.30  ? 218 ARG A CG  1 
ATOM   1287 C  CD  . ARG A 1 203 ? -7.984  -7.052  -0.839  1.00   81.29  ? 218 ARG A CD  1 
ATOM   1288 N  NE  . ARG A 1 203 ? -8.228  -6.098  0.261   1.00   84.89  ? 218 ARG A NE  1 
ATOM   1289 C  CZ  . ARG A 1 203 ? -8.839  -6.381  1.419   1.00   87.82  ? 218 ARG A CZ  1 
ATOM   1290 N  NH1 . ARG A 1 203 ? -9.284  -7.605  1.677   1.00   92.68  ? 218 ARG A NH1 1 
ATOM   1291 N  NH2 . ARG A 1 203 ? -9.004  -5.431  2.344   1.00   86.01  ? 218 ARG A NH2 1 
ATOM   1292 N  N   . GLY A 1 204 ? -6.147  -2.502  -3.303  1.00   70.26  ? 219 GLY A N   1 
ATOM   1293 C  CA  . GLY A 1 204 ? -6.777  -1.257  -3.753  1.00   73.01  ? 219 GLY A CA  1 
ATOM   1294 C  C   . GLY A 1 204 ? -5.877  -0.125  -4.217  1.00   76.40  ? 219 GLY A C   1 
ATOM   1295 O  O   . GLY A 1 204 ? -4.962  -0.336  -5.010  1.00   82.75  ? 219 GLY A O   1 
ATOM   1296 N  N   . GLY A 1 205 ? -6.127  1.078   -3.698  1.00   81.03  ? 220 GLY A N   1 
ATOM   1297 C  CA  . GLY A 1 205 ? -5.650  2.317   -4.322  1.00   83.17  ? 220 GLY A CA  1 
ATOM   1298 C  C   . GLY A 1 205 ? -4.396  3.068   -3.858  1.00   84.12  ? 220 GLY A C   1 
ATOM   1299 O  O   . GLY A 1 205 ? -4.178  3.283   -2.670  1.00   79.29  ? 220 GLY A O   1 
ATOM   1300 N  N   . LEU A 1 206 ? -3.553  3.388   -4.850  1.00   87.43  ? 221 LEU A N   1 
ATOM   1301 C  CA  . LEU A 1 206 ? -2.861  4.687   -5.008  1.00   84.69  ? 221 LEU A CA  1 
ATOM   1302 C  C   . LEU A 1 206 ? -3.748  5.577   -5.887  1.00   80.10  ? 221 LEU A C   1 
ATOM   1303 O  O   . LEU A 1 206 ? -3.661  6.802   -5.925  1.00   75.81  ? 221 LEU A O   1 
ATOM   1304 C  CB  . LEU A 1 206 ? -1.607  4.485   -5.845  1.00   86.67  ? 221 LEU A CB  1 
ATOM   1305 C  CG  . LEU A 1 206 ? -0.405  3.707   -5.335  1.00   91.05  ? 221 LEU A CG  1 
ATOM   1306 C  CD1 . LEU A 1 206 ? 0.470   3.427   -6.545  1.00   95.56  ? 221 LEU A CD1 1 
ATOM   1307 C  CD2 . LEU A 1 206 ? 0.370   4.503   -4.294  1.00   90.60  ? 221 LEU A CD2 1 
ATOM   1308 N  N   . VAL A 1 207 ? -4.624  4.876   -6.585  1.00   77.43  ? 222 VAL A N   1 
ATOM   1309 C  CA  . VAL A 1 207 ? -5.180  5.224   -7.880  1.00   74.16  ? 222 VAL A CA  1 
ATOM   1310 C  C   . VAL A 1 207 ? -4.350  6.091   -8.831  1.00   71.43  ? 222 VAL A C   1 
ATOM   1311 O  O   . VAL A 1 207 ? -4.884  6.971   -9.495  1.00   71.85  ? 222 VAL A O   1 
ATOM   1312 C  CB  . VAL A 1 207 ? -6.640  5.717   -7.758  1.00   74.35  ? 222 VAL A CB  1 
ATOM   1313 C  CG1 . VAL A 1 207 ? -7.389  5.391   -9.042  1.00   80.77  ? 222 VAL A CG1 1 
ATOM   1314 C  CG2 . VAL A 1 207 ? -7.357  5.027   -6.605  1.00   74.42  ? 222 VAL A CG2 1 
ATOM   1315 N  N   . ASP A 1 208 ? -3.051  5.814   -8.938  1.00   70.41  ? 223 ASP A N   1 
ATOM   1316 C  CA  . ASP A 1 208 ? -2.335  6.132   -10.169 1.00   66.75  ? 223 ASP A CA  1 
ATOM   1317 C  C   . ASP A 1 208 ? -2.932  5.129   -11.152 1.00   66.70  ? 223 ASP A C   1 
ATOM   1318 O  O   . ASP A 1 208 ? -3.300  4.021   -10.742 1.00   68.33  ? 223 ASP A O   1 
ATOM   1319 C  CB  . ASP A 1 208 ? -0.807  6.019   -10.002 1.00   64.14  ? 223 ASP A CB  1 
ATOM   1320 C  CG  . ASP A 1 208 ? -0.276  4.566   -10.013 1.00   65.93  ? 223 ASP A CG  1 
ATOM   1321 O  OD1 . ASP A 1 208 ? -0.893  3.693   -10.662 1.00   64.08  ? 223 ASP A OD1 1 
ATOM   1322 O  OD2 . ASP A 1 208 ? 0.810   4.310   -9.409  1.00   64.37  ? 223 ASP A OD2 1 
ATOM   1323 N  N   . ILE A 1 209 ? -3.110  5.516   -12.410 1.00   65.13  ? 224 ILE A N   1 
ATOM   1324 C  CA  . ILE A 1 209 ? -3.652  4.585   -13.411 1.00   65.59  ? 224 ILE A CA  1 
ATOM   1325 C  C   . ILE A 1 209 ? -5.037  4.084   -12.955 1.00   67.74  ? 224 ILE A C   1 
ATOM   1326 O  O   . ILE A 1 209 ? -5.824  3.535   -13.733 1.00   69.96  ? 224 ILE A O   1 
ATOM   1327 C  CB  . ILE A 1 209 ? -2.674  3.382   -13.646 1.00   64.54  ? 224 ILE A CB  1 
ATOM   1328 C  CG1 . ILE A 1 209 ? -1.370  3.835   -14.347 1.00   60.94  ? 224 ILE A CG1 1 
ATOM   1329 C  CG2 . ILE A 1 209 ? -3.350  2.268   -14.433 1.00   66.55  ? 224 ILE A CG2 1 
ATOM   1330 C  CD1 . ILE A 1 209 ? -0.211  2.875   -14.192 1.00   57.34  ? 224 ILE A CD1 1 
ATOM   1331 N  N   . LYS A 1 219 ? -15.600 -0.919  -0.266  1.00   81.07  ? 234 LYS A N   1 
ATOM   1332 C  CA  . LYS A 1 219 ? -14.385 -0.715  0.500   1.00   81.15  ? 234 LYS A CA  1 
ATOM   1333 C  C   . LYS A 1 219 ? -14.675 -0.290  1.918   1.00   83.29  ? 234 LYS A C   1 
ATOM   1334 O  O   . LYS A 1 219 ? -15.526 0.549   2.116   1.00   86.76  ? 234 LYS A O   1 
ATOM   1335 C  CB  . LYS A 1 219 ? -13.466 0.300   -0.177  0.0000 51.80  ? 234 LYS A CB  1 
ATOM   1336 C  CG  . LYS A 1 219 ? -14.088 1.662   -0.453  0.0000 52.05  ? 234 LYS A CG  1 
ATOM   1337 C  CD  . LYS A 1 219 ? -13.264 2.436   -1.469  0.0000 50.60  ? 234 LYS A CD  1 
ATOM   1338 C  CE  . LYS A 1 219 ? -12.865 1.565   -2.660  0.0000 50.20  ? 234 LYS A CE  1 
ATOM   1339 N  NZ  . LYS A 1 219 ? -12.031 2.269   -3.671  0.0000 48.92  ? 234 LYS A NZ  1 
ATOM   1340 N  N   . ASP A 1 220 ? -14.032 -0.873  2.925   1.00   93.21  ? 235 ASP A N   1 
ATOM   1341 C  CA  . ASP A 1 220 ? -12.721 -1.536  2.900   1.00   93.17  ? 235 ASP A CA  1 
ATOM   1342 C  C   . ASP A 1 220 ? -11.633 -0.491  3.099   1.00   85.51  ? 235 ASP A C   1 
ATOM   1343 O  O   . ASP A 1 220 ? -10.551 -0.804  3.509   1.00   76.36  ? 235 ASP A O   1 
ATOM   1344 C  CB  . ASP A 1 220 ? -12.504 -2.453  1.685   1.00   93.60  ? 235 ASP A CB  1 
ATOM   1345 C  CG  . ASP A 1 220 ? -11.076 -2.690  1.382   1.00   93.29  ? 235 ASP A CG  1 
ATOM   1346 O  OD1 . ASP A 1 220 ? -10.361 -3.053  2.336   1.00   96.37  ? 235 ASP A OD1 1 
ATOM   1347 O  OD2 . ASP A 1 220 ? -10.686 -2.520  0.200   1.00   87.50  ? 235 ASP A OD2 1 
ATOM   1348 N  N   . LEU A 1 221 ? -11.954 0.764   2.851   1.00   82.57  ? 236 LEU A N   1 
ATOM   1349 C  CA  . LEU A 1 221 ? -11.085 1.820   3.334   1.00   79.91  ? 236 LEU A CA  1 
ATOM   1350 C  C   . LEU A 1 221 ? -11.319 2.000   4.829   1.00   76.84  ? 236 LEU A C   1 
ATOM   1351 O  O   . LEU A 1 221 ? -10.724 2.865   5.443   1.00   78.15  ? 236 LEU A O   1 
ATOM   1352 C  CB  . LEU A 1 221 ? -11.345 3.141   2.599   1.00   82.30  ? 236 LEU A CB  1 
ATOM   1353 C  CG  . LEU A 1 221 ? -11.311 3.208   1.047   1.00   88.00  ? 236 LEU A CG  1 
ATOM   1354 C  CD1 . LEU A 1 221 ? -10.267 2.275   0.415   1.00   86.79  ? 236 LEU A CD1 1 
ATOM   1355 C  CD2 . LEU A 1 221 ? -12.695 3.016   0.391   1.00   91.18  ? 236 LEU A CD2 1 
ATOM   1356 N  N   . LYS A 1 222 ? -12.198 1.200   5.418   1.00   77.29  ? 237 LYS A N   1 
ATOM   1357 C  CA  . LYS A 1 222 ? -12.380 1.210   6.871   1.00   79.34  ? 237 LYS A CA  1 
ATOM   1358 C  C   . LYS A 1 222 ? -11.401 0.256   7.583   1.00   74.48  ? 237 LYS A C   1 
ATOM   1359 O  O   . LYS A 1 222 ? -11.007 0.496   8.718   1.00   73.23  ? 237 LYS A O   1 
ATOM   1360 C  CB  . LYS A 1 222 ? -13.836 0.893   7.243   1.00   82.58  ? 237 LYS A CB  1 
ATOM   1361 C  CG  . LYS A 1 222 ? -14.759 2.112   7.286   1.00   87.25  ? 237 LYS A CG  1 
ATOM   1362 C  CD  . LYS A 1 222 ? -14.984 2.774   5.928   1.00   88.92  ? 237 LYS A CD  1 
ATOM   1363 C  CE  . LYS A 1 222 ? -16.173 3.729   5.975   1.00   92.67  ? 237 LYS A CE  1 
ATOM   1364 N  NZ  . LYS A 1 222 ? -16.346 4.533   4.733   1.00   94.81  ? 237 LYS A NZ  1 
ATOM   1365 N  N   . ARG A 1 223 ? -11.002 -0.811  6.904   1.00   68.95  ? 238 ARG A N   1 
ATOM   1366 C  CA  . ARG A 1 223 ? -10.061 -1.781  7.456   1.00   65.52  ? 238 ARG A CA  1 
ATOM   1367 C  C   . ARG A 1 223 ? -8.682  -1.159  7.689   1.00   63.27  ? 238 ARG A C   1 
ATOM   1368 O  O   . ARG A 1 223 ? -7.923  -1.574  8.571   1.00   60.32  ? 238 ARG A O   1 
ATOM   1369 C  CB  . ARG A 1 223 ? -9.936  -2.950  6.485   1.00   64.91  ? 238 ARG A CB  1 
ATOM   1370 C  CG  . ARG A 1 223 ? -9.747  -4.289  7.149   1.00   65.83  ? 238 ARG A CG  1 
ATOM   1371 C  CD  . ARG A 1 223 ? -8.293  -4.661  7.296   1.00   66.50  ? 238 ARG A CD  1 
ATOM   1372 N  NE  . ARG A 1 223 ? -8.079  -5.362  8.559   1.00   68.94  ? 238 ARG A NE  1 
ATOM   1373 C  CZ  . ARG A 1 223 ? -7.121  -6.254  8.798   1.00   67.86  ? 238 ARG A CZ  1 
ATOM   1374 N  NH1 . ARG A 1 223 ? -6.258  -6.616  7.862   1.00   66.21  ? 238 ARG A NH1 1 
ATOM   1375 N  NH2 . ARG A 1 223 ? -7.043  -6.801  10.001  1.00   71.43  ? 238 ARG A NH2 1 
ATOM   1376 N  N   . LEU A 1 224 ? -8.367  -0.167  6.865   1.00   62.32  ? 239 LEU A N   1 
ATOM   1377 C  CA  . LEU A 1 224 ? -7.129  0.575   6.964   1.00   60.28  ? 239 LEU A CA  1 
ATOM   1378 C  C   . LEU A 1 224 ? -7.135  1.469   8.202   1.00   63.56  ? 239 LEU A C   1 
ATOM   1379 O  O   . LEU A 1 224 ? -6.182  1.438   8.985   1.00   65.95  ? 239 LEU A O   1 
ATOM   1380 C  CB  . LEU A 1 224 ? -6.941  1.425   5.714   1.00   56.62  ? 239 LEU A CB  1 
ATOM   1381 C  CG  . LEU A 1 224 ? -5.603  2.139   5.629   1.00   53.81  ? 239 LEU A CG  1 
ATOM   1382 C  CD1 . LEU A 1 224 ? -4.501  1.191   5.208   1.00   52.42  ? 239 LEU A CD1 1 
ATOM   1383 C  CD2 . LEU A 1 224 ? -5.749  3.254   4.632   1.00   53.81  ? 239 LEU A CD2 1 
ATOM   1384 N  N   . LYS A 1 225 ? -8.204  2.261   8.359   1.00   66.80  ? 240 LYS A N   1 
ATOM   1385 C  CA  . LYS A 1 225 ? -8.409  3.147   9.524   1.00   66.92  ? 240 LYS A CA  1 
ATOM   1386 C  C   . LYS A 1 225 ? -8.236  2.389   10.813  1.00   63.10  ? 240 LYS A C   1 
ATOM   1387 O  O   . LYS A 1 225 ? -7.684  2.905   11.774  1.00   61.62  ? 240 LYS A O   1 
ATOM   1388 C  CB  . LYS A 1 225 ? -9.827  3.755   9.534   1.00   73.34  ? 240 LYS A CB  1 
ATOM   1389 C  CG  . LYS A 1 225 ? -10.128 4.718   8.394   1.00   78.21  ? 240 LYS A CG  1 
ATOM   1390 C  CD  . LYS A 1 225 ? -11.301 5.657   8.689   1.00   84.94  ? 240 LYS A CD  1 
ATOM   1391 C  CE  . LYS A 1 225 ? -12.637 4.924   8.821   1.00   90.60  ? 240 LYS A CE  1 
ATOM   1392 N  NZ  . LYS A 1 225 ? -13.748 5.564   8.032   1.00   92.70  ? 240 LYS A NZ  1 
ATOM   1393 N  N   . GLU A 1 226 ? -8.757  1.172   10.830  1.00   61.94  ? 241 GLU A N   1 
ATOM   1394 C  CA  . GLU A 1 226 ? -8.665  0.322   11.996  1.00   61.88  ? 241 GLU A CA  1 
ATOM   1395 C  C   . GLU A 1 226 ? -7.207  -0.004  12.208  1.00   59.67  ? 241 GLU A C   1 
ATOM   1396 O  O   . GLU A 1 226 ? -6.666  0.235   13.296  1.00   61.74  ? 241 GLU A O   1 
ATOM   1397 C  CB  . GLU A 1 226 ? -9.447  -0.969  11.805  1.00   62.46  ? 241 GLU A CB  1 
ATOM   1398 C  CG  . GLU A 1 226 ? -10.950 -0.814  11.862  1.00   63.81  ? 241 GLU A CG  1 
ATOM   1399 C  CD  . GLU A 1 226 ? -11.646 -2.157  11.862  1.00   65.70  ? 241 GLU A CD  1 
ATOM   1400 O  OE1 . GLU A 1 226 ? -12.889 -2.194  11.986  1.00   66.05  ? 241 GLU A OE1 1 
ATOM   1401 O  OE2 . GLU A 1 226 ? -10.932 -3.178  11.745  1.00   66.07  ? 241 GLU A OE2 1 
ATOM   1402 N  N   . CYS A 1 227 ? -6.561  -0.543  11.174  1.00   55.54  ? 242 CYS A N   1 
ATOM   1403 C  CA  . CYS A 1 227 ? -5.133  -0.842  11.276  1.00   51.68  ? 242 CYS A CA  1 
ATOM   1404 C  C   . CYS A 1 227 ? -4.366  0.399   11.683  1.00   49.19  ? 242 CYS A C   1 
ATOM   1405 O  O   . CYS A 1 227 ? -3.496  0.359   12.537  1.00   48.03  ? 242 CYS A O   1 
ATOM   1406 C  CB  . CYS A 1 227 ? -4.605  -1.371  9.969   1.00   49.70  ? 242 CYS A CB  1 
ATOM   1407 S  SG  . CYS A 1 227 ? -5.256  -2.992  9.606   1.00   51.10  ? 242 CYS A SG  1 
ATOM   1408 N  N   . VAL A 1 228 ? -4.729  1.515   11.085  1.00   47.86  ? 243 VAL A N   1 
ATOM   1409 C  CA  . VAL A 1 228 ? -4.012  2.739   11.316  1.00   47.23  ? 243 VAL A CA  1 
ATOM   1410 C  C   . VAL A 1 228 ? -4.159  3.175   12.762  1.00   48.15  ? 243 VAL A C   1 
ATOM   1411 O  O   . VAL A 1 228 ? -3.182  3.568   13.376  1.00   48.71  ? 243 VAL A O   1 
ATOM   1412 C  CB  . VAL A 1 228 ? -4.407  3.819   10.273  1.00   46.62  ? 243 VAL A CB  1 
ATOM   1413 C  CG1 . VAL A 1 228 ? -4.198  5.241   10.783  1.00   47.43  ? 243 VAL A CG1 1 
ATOM   1414 C  CG2 . VAL A 1 228 ? -3.572  3.605   9.031   1.00   44.43  ? 243 VAL A CG2 1 
ATOM   1415 N  N   . SER A 1 229 ? -5.352  3.039   13.330  1.00   49.98  ? 244 SER A N   1 
ATOM   1416 C  CA  . SER A 1 229 ? -5.602  3.443   14.735  1.00   50.33  ? 244 SER A CA  1 
ATOM   1417 C  C   . SER A 1 229 ? -4.747  2.712   15.799  1.00   49.62  ? 244 SER A C   1 
ATOM   1418 O  O   . SER A 1 229 ? -4.119  3.337   16.647  1.00   49.07  ? 244 SER A O   1 
ATOM   1419 C  CB  . SER A 1 229 ? -7.068  3.253   15.073  1.00   52.01  ? 244 SER A CB  1 
ATOM   1420 O  OG  . SER A 1 229 ? -7.328  3.787   16.353  1.00   53.86  ? 244 SER A OG  1 
ATOM   1421 N  N   . ILE A 1 230 ? -4.742  1.389   15.749  1.00   49.16  ? 245 ILE A N   1 
ATOM   1422 C  CA  . ILE A 1 230 ? -3.939  0.581   16.660  1.00   48.87  ? 245 ILE A CA  1 
ATOM   1423 C  C   . ILE A 1 230 ? -2.481  0.980   16.518  1.00   48.18  ? 245 ILE A C   1 
ATOM   1424 O  O   . ILE A 1 230 ? -1.743  1.078   17.509  1.00   46.78  ? 245 ILE A O   1 
ATOM   1425 C  CB  . ILE A 1 230 ? -4.179  -0.921  16.381  1.00   48.82  ? 245 ILE A CB  1 
ATOM   1426 C  CG1 . ILE A 1 230 ? -5.512  -1.327  17.065  1.00   51.09  ? 245 ILE A CG1 1 
ATOM   1427 C  CG2 . ILE A 1 230 ? -3.017  -1.765  16.862  1.00   47.96  ? 245 ILE A CG2 1 
ATOM   1428 C  CD1 . ILE A 1 230 ? -6.112  -2.648  16.634  1.00   51.43  ? 245 ILE A CD1 1 
ATOM   1429 N  N   . ARG A 1 231 ? -2.085  1.253   15.265  1.00   47.65  ? 246 ARG A N   1 
ATOM   1430 C  CA  . ARG A 1 231 ? -0.733  1.701   14.970  1.00   45.87  ? 246 ARG A CA  1 
ATOM   1431 C  C   . ARG A 1 231 ? -0.506  3.068   15.601  1.00   46.01  ? 246 ARG A C   1 
ATOM   1432 O  O   . ARG A 1 231 ? 0.429   3.256   16.383  1.00   45.33  ? 246 ARG A O   1 
ATOM   1433 C  CB  . ARG A 1 231 ? -0.507  1.746   13.465  1.00   44.86  ? 246 ARG A CB  1 
ATOM   1434 C  CG  . ARG A 1 231 ? 0.864   2.248   13.034  1.00   43.58  ? 246 ARG A CG  1 
ATOM   1435 C  CD  . ARG A 1 231 ? 0.843   2.916   11.679  1.00   42.63  ? 246 ARG A CD  1 
ATOM   1436 N  NE  . ARG A 1 231 ? 0.159   4.215   11.666  1.00   43.07  ? 246 ARG A NE  1 
ATOM   1437 C  CZ  . ARG A 1 231 ? 0.214   5.081   10.646  1.00   42.60  ? 246 ARG A CZ  1 
ATOM   1438 N  NH1 . ARG A 1 231 ? 0.943   4.804   9.572   1.00   41.00  ? 246 ARG A NH1 1 
ATOM   1439 N  NH2 . ARG A 1 231 ? -0.424  6.245   10.702  1.00   42.92  ? 246 ARG A NH2 1 
ATOM   1440 N  N   . ASP A 1 232 ? -1.372  4.019   15.283  1.00   46.34  ? 247 ASP A N   1 
ATOM   1441 C  CA  . ASP A 1 232 ? -1.208  5.347   15.837  1.00   47.63  ? 247 ASP A CA  1 
ATOM   1442 C  C   . ASP A 1 232 ? -1.160  5.317   17.372  1.00   49.05  ? 247 ASP A C   1 
ATOM   1443 O  O   . ASP A 1 232 ? -0.425  6.079   17.973  1.00   48.26  ? 247 ASP A O   1 
ATOM   1444 C  CB  . ASP A 1 232 ? -2.289  6.309   15.332  1.00   48.93  ? 247 ASP A CB  1 
ATOM   1445 C  CG  . ASP A 1 232 ? -2.085  6.711   13.858  1.00   49.68  ? 247 ASP A CG  1 
ATOM   1446 O  OD1 . ASP A 1 232 ? -1.034  6.301   13.298  1.00   49.89  ? 247 ASP A OD1 1 
ATOM   1447 O  OD2 . ASP A 1 232 ? -2.964  7.415   13.252  1.00   50.54  ? 247 ASP A OD2 1 
ATOM   1448 N  N   . GLN A 1 233 ? -1.908  4.431   18.015  1.00   50.36  ? 248 GLN A N   1 
ATOM   1449 C  CA  . GLN A 1 233 ? -1.977  4.474   19.478  1.00   52.49  ? 248 GLN A CA  1 
ATOM   1450 C  C   . GLN A 1 233 ? -0.708  3.928   20.088  1.00   51.55  ? 248 GLN A C   1 
ATOM   1451 O  O   . GLN A 1 233 ? -0.046  4.593   20.849  1.00   51.46  ? 248 GLN A O   1 
ATOM   1452 C  CB  . GLN A 1 233 ? -3.181  3.690   20.009  1.00   54.94  ? 248 GLN A CB  1 
ATOM   1453 C  CG  . GLN A 1 233 ? -4.535  4.283   19.659  1.00   56.27  ? 248 GLN A CG  1 
ATOM   1454 C  CD  . GLN A 1 233 ? -5.630  3.253   19.799  1.00   58.36  ? 248 GLN A CD  1 
ATOM   1455 O  OE1 . GLN A 1 233 ? -5.793  2.670   20.857  1.00   62.26  ? 248 GLN A OE1 1 
ATOM   1456 N  NE2 . GLN A 1 233 ? -6.372  3.013   18.735  1.00   58.35  ? 248 GLN A NE2 1 
ATOM   1457 N  N   . LEU A 1 234 ? -0.375  2.707   19.716  1.00   51.76  ? 249 LEU A N   1 
ATOM   1458 C  CA  . LEU A 1 234 ? 0.870   2.065   20.128  1.00   52.00  ? 249 LEU A CA  1 
ATOM   1459 C  C   . LEU A 1 234 ? 2.130   2.924   20.001  1.00   50.45  ? 249 LEU A C   1 
ATOM   1460 O  O   . LEU A 1 234 ? 2.970   2.883   20.869  1.00   49.27  ? 249 LEU A O   1 
ATOM   1461 C  CB  . LEU A 1 234 ? 1.071   0.793   19.321  1.00   51.90  ? 249 LEU A CB  1 
ATOM   1462 C  CG  . LEU A 1 234 ? 2.181   -0.117  19.834  1.00   52.83  ? 249 LEU A CG  1 
ATOM   1463 C  CD1 . LEU A 1 234 ? 1.751   -1.572  19.716  1.00   53.99  ? 249 LEU A CD1 1 
ATOM   1464 C  CD2 . LEU A 1 234 ? 3.488   0.115   19.093  1.00   51.79  ? 249 LEU A CD2 1 
ATOM   1465 N  N   . LEU A 1 235 ? 2.271   3.673   18.913  1.00   50.29  ? 250 LEU A N   1 
ATOM   1466 C  CA  . LEU A 1 235 ? 3.418   4.565   18.757  1.00   50.12  ? 250 LEU A CA  1 
ATOM   1467 C  C   . LEU A 1 235 ? 3.309   5.750   19.672  1.00   51.44  ? 250 LEU A C   1 
ATOM   1468 O  O   . LEU A 1 235 ? 4.294   6.095   20.341  1.00   52.69  ? 250 LEU A O   1 
ATOM   1469 C  CB  . LEU A 1 235 ? 3.578   5.066   17.328  1.00   49.71  ? 250 LEU A CB  1 
ATOM   1470 C  CG  . LEU A 1 235 ? 4.413   4.173   16.419  1.00   49.69  ? 250 LEU A CG  1 
ATOM   1471 C  CD1 . LEU A 1 235 ? 4.026   2.718   16.644  1.00   50.94  ? 250 LEU A CD1 1 
ATOM   1472 C  CD2 . LEU A 1 235 ? 4.259   4.581   14.953  1.00   48.15  ? 250 LEU A CD2 1 
ATOM   1473 N  N   . TYR A 1 236 ? 2.135   6.381   19.695  1.00   51.56  ? 251 TYR A N   1 
ATOM   1474 C  CA  . TYR A 1 236 ? 1.903   7.533   20.560  1.00   53.08  ? 251 TYR A CA  1 
ATOM   1475 C  C   . TYR A 1 236 ? 2.299   7.169   21.985  1.00   54.86  ? 251 TYR A C   1 
ATOM   1476 O  O   . TYR A 1 236 ? 2.927   7.966   22.684  1.00   55.48  ? 251 TYR A O   1 
ATOM   1477 C  CB  . TYR A 1 236 ? 0.446   7.991   20.521  1.00   53.79  ? 251 TYR A CB  1 
ATOM   1478 C  CG  . TYR A 1 236 ? 0.212   9.285   21.256  1.00   55.76  ? 251 TYR A CG  1 
ATOM   1479 C  CD1 . TYR A 1 236 ? 0.799   10.462  20.819  1.00   55.95  ? 251 TYR A CD1 1 
ATOM   1480 C  CD2 . TYR A 1 236 ? -0.607  9.336   22.398  1.00   59.23  ? 251 TYR A CD2 1 
ATOM   1481 C  CE1 . TYR A 1 236 ? 0.588   11.664  21.482  1.00   58.62  ? 251 TYR A CE1 1 
ATOM   1482 C  CE2 . TYR A 1 236 ? -0.825  10.531  23.087  1.00   60.89  ? 251 TYR A CE2 1 
ATOM   1483 C  CZ  . TYR A 1 236 ? -0.220  11.695  22.628  1.00   61.65  ? 251 TYR A CZ  1 
ATOM   1484 O  OH  . TYR A 1 236 ? -0.413  12.884  23.312  1.00   64.50  ? 251 TYR A OH  1 
ATOM   1485 N  N   . LYS A 1 237 ? 1.952   5.951   22.395  1.00   55.84  ? 252 LYS A N   1 
ATOM   1486 C  CA  . LYS A 1 237 ? 2.294   5.463   23.721  1.00   58.33  ? 252 LYS A CA  1 
ATOM   1487 C  C   . LYS A 1 237 ? 3.792   5.477   23.858  1.00   56.44  ? 252 LYS A C   1 
ATOM   1488 O  O   . LYS A 1 237 ? 4.342   6.139   24.714  1.00   58.53  ? 252 LYS A O   1 
ATOM   1489 C  CB  . LYS A 1 237 ? 1.768   4.049   23.943  1.00   60.70  ? 252 LYS A CB  1 
ATOM   1490 C  CG  . LYS A 1 237 ? 2.415   3.338   25.116  1.00   63.24  ? 252 LYS A CG  1 
ATOM   1491 C  CD  . LYS A 1 237 ? 1.713   2.022   25.389  1.00   65.47  ? 252 LYS A CD  1 
ATOM   1492 C  CE  . LYS A 1 237 ? 2.506   1.145   26.339  1.00   66.54  ? 252 LYS A CE  1 
ATOM   1493 N  NZ  . LYS A 1 237 ? 2.327   -0.277  25.952  1.00   66.91  ? 252 LYS A NZ  1 
ATOM   1494 N  N   . LYS A 1 238 ? 4.457   4.763   22.980  1.00   53.85  ? 253 LYS A N   1 
ATOM   1495 C  CA  . LYS A 1 238 ? 5.891   4.849   22.919  1.00   52.22  ? 253 LYS A CA  1 
ATOM   1496 C  C   . LYS A 1 238 ? 6.363   6.316   22.933  1.00   52.38  ? 253 LYS A C   1 
ATOM   1497 O  O   . LYS A 1 238 ? 7.247   6.679   23.678  1.00   52.63  ? 253 LYS A O   1 
ATOM   1498 C  CB  . LYS A 1 238 ? 6.397   4.091   21.705  1.00   49.69  ? 253 LYS A CB  1 
ATOM   1499 C  CG  . LYS A 1 238 ? 7.708   3.386   21.962  1.00   49.70  ? 253 LYS A CG  1 
ATOM   1500 C  CD  . LYS A 1 238 ? 7.670   2.219   22.971  1.00   50.44  ? 253 LYS A CD  1 
ATOM   1501 C  CE  . LYS A 1 238 ? 8.845   2.286   23.975  1.00   50.54  ? 253 LYS A CE  1 
ATOM   1502 N  NZ  . LYS A 1 238 ? 9.645   1.016   24.115  1.00   50.13  ? 253 LYS A NZ  1 
ATOM   1503 N  N   . LEU A 1 239 ? 5.729   7.170   22.148  1.00   52.97  ? 254 LEU A N   1 
ATOM   1504 C  CA  . LEU A 1 239 ? 6.094   8.591   22.102  1.00   52.69  ? 254 LEU A CA  1 
ATOM   1505 C  C   . LEU A 1 239 ? 5.983   9.267   23.469  1.00   54.24  ? 254 LEU A C   1 
ATOM   1506 O  O   . LEU A 1 239 ? 6.895   9.988   23.882  1.00   53.94  ? 254 LEU A O   1 
ATOM   1507 C  CB  . LEU A 1 239 ? 5.253   9.296   21.031  1.00   51.62  ? 254 LEU A CB  1 
ATOM   1508 C  CG  . LEU A 1 239 ? 5.146   10.809  20.832  1.00   51.73  ? 254 LEU A CG  1 
ATOM   1509 C  CD1 . LEU A 1 239 ? 6.371   11.596  21.206  1.00   52.31  ? 254 LEU A CD1 1 
ATOM   1510 C  CD2 . LEU A 1 239 ? 4.835   11.092  19.367  1.00   50.45  ? 254 LEU A CD2 1 
ATOM   1511 N  N   . LEU A 1 240 ? 4.889   9.022   24.182  1.00   55.80  ? 255 LEU A N   1 
ATOM   1512 C  CA  . LEU A 1 240 ? 4.728   9.549   25.565  1.00   58.04  ? 255 LEU A CA  1 
ATOM   1513 C  C   . LEU A 1 240 ? 5.802   9.059   26.536  1.00   58.31  ? 255 LEU A C   1 
ATOM   1514 O  O   . LEU A 1 240 ? 6.386   9.840   27.277  1.00   59.48  ? 255 LEU A O   1 
ATOM   1515 C  CB  . LEU A 1 240 ? 3.360   9.171   26.127  1.00   59.07  ? 255 LEU A CB  1 
ATOM   1516 C  CG  . LEU A 1 240 ? 2.251   10.211  26.003  1.00   59.96  ? 255 LEU A CG  1 
ATOM   1517 C  CD1 . LEU A 1 240 ? 2.551   11.278  24.963  1.00   58.72  ? 255 LEU A CD1 1 
ATOM   1518 C  CD2 . LEU A 1 240 ? 0.936   9.512   25.715  1.00   60.05  ? 255 LEU A CD2 1 
ATOM   1519 N  N   . GLU A 1 241 ? 6.033   7.755   26.512  1.00   57.46  ? 256 GLU A N   1 
ATOM   1520 C  CA  . GLU A 1 241 ? 7.102   7.125   27.257  1.00   58.30  ? 256 GLU A CA  1 
ATOM   1521 C  C   . GLU A 1 241 ? 8.471   7.759   26.979  1.00   58.30  ? 256 GLU A C   1 
ATOM   1522 O  O   . GLU A 1 241 ? 9.314   7.849   27.869  1.00   62.40  ? 256 GLU A O   1 
ATOM   1523 C  CB  . GLU A 1 241 ? 7.138   5.629   26.930  1.00   57.15  ? 256 GLU A CB  1 
ATOM   1524 C  CG  . GLU A 1 241 ? 5.907   4.883   27.421  1.00   57.93  ? 256 GLU A CG  1 
ATOM   1525 C  CD  . GLU A 1 241 ? 5.976   3.384   27.191  1.00   57.84  ? 256 GLU A CD  1 
ATOM   1526 O  OE1 . GLU A 1 241 ? 6.459   2.935   26.111  1.00   55.39  ? 256 GLU A OE1 1 
ATOM   1527 O  OE2 . GLU A 1 241 ? 5.529   2.648   28.105  1.00   59.72  ? 256 GLU A OE2 1 
ATOM   1528 N  N   . HIS A 1 242 ? 8.678   8.199   25.748  1.00   56.25  ? 257 HIS A N   1 
ATOM   1529 C  CA  . HIS A 1 242 ? 9.925   8.834   25.329  1.00   55.29  ? 257 HIS A CA  1 
ATOM   1530 C  C   . HIS A 1 242 ? 10.017  10.299  25.725  1.00   58.21  ? 257 HIS A C   1 
ATOM   1531 O  O   . HIS A 1 242 ? 11.065  10.745  26.156  1.00   58.81  ? 257 HIS A O   1 
ATOM   1532 C  CB  . HIS A 1 242 ? 10.112  8.704   23.795  1.00   52.10  ? 257 HIS A CB  1 
ATOM   1533 C  CG  . HIS A 1 242 ? 10.725  7.406   23.385  1.00   49.06  ? 257 HIS A CG  1 
ATOM   1534 N  ND1 . HIS A 1 242 ? 10.064  6.206   23.499  1.00   48.54  ? 257 HIS A ND1 1 
ATOM   1535 C  CD2 . HIS A 1 242 ? 11.960  7.111   22.931  1.00   47.29  ? 257 HIS A CD2 1 
ATOM   1536 C  CE1 . HIS A 1 242 ? 10.862  5.227   23.123  1.00   46.98  ? 257 HIS A CE1 1 
ATOM   1537 N  NE2 . HIS A 1 242 ? 12.016  5.751   22.768  1.00   46.46  ? 257 HIS A NE2 1 
ATOM   1538 N  N   . LYS A 1 243 ? 8.937   11.057  25.565  1.00   61.97  ? 258 LYS A N   1 
ATOM   1539 C  CA  . LYS A 1 243 ? 8.990   12.489  25.862  1.00   65.71  ? 258 LYS A CA  1 
ATOM   1540 C  C   . LYS A 1 243 ? 9.335   12.749  27.327  1.00   71.21  ? 258 LYS A C   1 
ATOM   1541 O  O   . LYS A 1 243 ? 10.012  13.743  27.626  1.00   71.25  ? 258 LYS A O   1 
ATOM   1542 C  CB  . LYS A 1 243 ? 7.676   13.181  25.512  1.00   65.94  ? 258 LYS A CB  1 
ATOM   1543 C  CG  . LYS A 1 243 ? 7.856   14.659  25.204  1.00   66.43  ? 258 LYS A CG  1 
ATOM   1544 C  CD  . LYS A 1 243 ? 6.624   15.481  25.525  1.00   67.70  ? 258 LYS A CD  1 
ATOM   1545 C  CE  . LYS A 1 243 ? 5.373   14.949  24.844  1.00   67.83  ? 258 LYS A CE  1 
ATOM   1546 N  NZ  . LYS A 1 243 ? 4.118   15.542  25.412  1.00   69.20  ? 258 LYS A NZ  1 
ATOM   1547 N  N   . LYS A 1 244 ? 8.863   11.852  28.214  1.00   77.15  ? 259 LYS A N   1 
ATOM   1548 C  CA  . LYS A 1 244 ? 9.135   11.904  29.670  1.00   82.74  ? 259 LYS A CA  1 
ATOM   1549 C  C   . LYS A 1 244 ? 10.620  11.700  30.028  1.00   83.35  ? 259 LYS A C   1 
ATOM   1550 O  O   . LYS A 1 244 ? 11.151  12.429  30.853  1.00   82.95  ? 259 LYS A O   1 
ATOM   1551 C  CB  . LYS A 1 244 ? 8.234   10.915  30.469  1.00   85.02  ? 259 LYS A CB  1 
ATOM   1552 C  CG  . LYS A 1 244 ? 8.422   9.415   30.210  1.00   85.14  ? 259 LYS A CG  1 
ATOM   1553 C  CD  . LYS A 1 244 ? 8.142   8.564   31.458  1.00   88.25  ? 259 LYS A CD  1 
ATOM   1554 C  CE  . LYS A 1 244 ? 8.117   7.056   31.173  1.00   86.64  ? 259 LYS A CE  1 
ATOM   1555 N  NZ  . LYS A 1 244 ? 9.446   6.386   31.109  1.00   85.49  ? 259 LYS A NZ  1 
ATOM   1556 N  N   . SER A 1 245 ? 11.269  10.718  29.402  1.00   84.77  ? 260 SER A N   1 
ATOM   1557 C  CA  . SER A 1 245 ? 12.701  10.477  29.563  1.00   87.12  ? 260 SER A CA  1 
ATOM   1558 C  C   . SER A 1 245 ? 13.408  11.009  28.329  1.00   87.80  ? 260 SER A C   1 
ATOM   1559 O  O   . SER A 1 245 ? 13.373  10.360  27.278  1.00   89.68  ? 260 SER A O   1 
ATOM   1560 C  CB  . SER A 1 245 ? 12.983  8.982   29.719  1.00   87.70  ? 260 SER A CB  1 
ATOM   1561 O  OG  . SER A 1 245 ? 12.825  8.578   31.071  1.00   96.15  ? 260 SER A OG  1 
ATOM   1562 N  N   . LEU A 1 246 ? 14.047  12.177  28.444  1.00   88.09  ? 261 LEU A N   1 
ATOM   1563 C  CA  . LEU A 1 246 ? 14.598  12.863  27.267  1.00   86.09  ? 261 LEU A CA  1 
ATOM   1564 C  C   . LEU A 1 246 ? 15.853  13.675  27.540  1.00   87.41  ? 261 LEU A C   1 
ATOM   1565 O  O   . LEU A 1 246 ? 15.777  14.737  28.147  1.00   92.39  ? 261 LEU A O   1 
ATOM   1566 C  CB  . LEU A 1 246 ? 13.544  13.800  26.684  1.00   85.36  ? 261 LEU A CB  1 
ATOM   1567 C  CG  . LEU A 1 246 ? 13.815  14.287  25.262  1.00   80.29  ? 261 LEU A CG  1 
ATOM   1568 C  CD1 . LEU A 1 246 ? 13.949  13.095  24.339  1.00   77.82  ? 261 LEU A CD1 1 
ATOM   1569 C  CD2 . LEU A 1 246 ? 12.696  15.201  24.797  1.00   79.96  ? 261 LEU A CD2 1 
ATOM   1570 N  N   . THR A 1 247 ? 16.993  13.186  27.054  1.00   86.63  ? 262 THR A N   1 
ATOM   1571 C  CA  . THR A 1 247 ? 18.287  13.856  27.214  1.00   84.75  ? 262 THR A CA  1 
ATOM   1572 C  C   . THR A 1 247 ? 18.744  14.359  25.833  1.00   81.73  ? 262 THR A C   1 
ATOM   1573 O  O   . THR A 1 247 ? 19.125  13.556  24.984  1.00   79.16  ? 262 THR A O   1 
ATOM   1574 C  CB  . THR A 1 247 ? 19.324  12.888  27.837  1.00   84.59  ? 262 THR A CB  1 
ATOM   1575 O  OG1 . THR A 1 247 ? 18.817  12.389  29.079  1.00   84.37  ? 262 THR A OG1 1 
ATOM   1576 C  CG2 . THR A 1 247 ? 20.672  13.570  28.091  1.00   84.73  ? 262 THR A CG2 1 
ATOM   1577 N  N   . PRO A 1 248 ? 18.665  15.684  25.593  1.00   82.96  ? 263 PRO A N   1 
ATOM   1578 C  CA  . PRO A 1 248 ? 19.040  16.333  24.323  1.00   85.10  ? 263 PRO A CA  1 
ATOM   1579 C  C   . PRO A 1 248 ? 20.477  16.142  23.822  1.00   89.57  ? 263 PRO A C   1 
ATOM   1580 O  O   . PRO A 1 248 ? 20.665  15.948  22.620  1.00   87.41  ? 263 PRO A O   1 
ATOM   1581 C  CB  . PRO A 1 248 ? 18.779  17.812  24.600  1.00   83.83  ? 263 PRO A CB  1 
ATOM   1582 C  CG  . PRO A 1 248 ? 17.641  17.788  25.535  1.00   84.10  ? 263 PRO A CG  1 
ATOM   1583 C  CD  . PRO A 1 248 ? 17.865  16.597  26.426  1.00   84.92  ? 263 PRO A CD  1 
ATOM   1584 N  N   . GLY A 1 249 ? 21.468  16.244  24.710  1.00   98.90  ? 264 GLY A N   1 
ATOM   1585 C  CA  . GLY A 1 249 ? 22.868  16.010  24.335  1.00   104.30 ? 264 GLY A CA  1 
ATOM   1586 C  C   . GLY A 1 249 ? 22.891  14.783  23.453  1.00   107.11 ? 264 GLY A C   1 
ATOM   1587 O  O   . GLY A 1 249 ? 23.085  14.888  22.244  1.00   107.30 ? 264 GLY A O   1 
ATOM   1588 N  N   . GLU A 1 250 ? 22.690  13.624  24.079  1.00   113.75 ? 265 GLU A N   1 
ATOM   1589 C  CA  . GLU A 1 250 ? 22.209  12.404  23.404  1.00   116.71 ? 265 GLU A CA  1 
ATOM   1590 C  C   . GLU A 1 250 ? 21.417  11.606  24.454  1.00   113.81 ? 265 GLU A C   1 
ATOM   1591 O  O   . GLU A 1 250 ? 21.492  11.963  25.632  1.00   116.00 ? 265 GLU A O   1 
ATOM   1592 C  CB  . GLU A 1 250 ? 23.356  11.564  22.832  1.00   123.30 ? 265 GLU A CB  1 
ATOM   1593 C  CG  . GLU A 1 250 ? 24.618  12.305  22.429  1.00   127.15 ? 265 GLU A CG  1 
ATOM   1594 C  CD  . GLU A 1 250 ? 25.450  11.509  21.447  1.00   128.19 ? 265 GLU A CD  1 
ATOM   1595 O  OE1 . GLU A 1 250 ? 24.910  11.119  20.383  1.00   124.71 ? 265 GLU A OE1 1 
ATOM   1596 O  OE2 . GLU A 1 250 ? 26.645  11.282  21.735  1.00   135.04 ? 265 GLU A OE2 1 
ATOM   1597 N  N   . PRO A 1 251 ? 20.721  10.515  24.095  1.00   105.94 ? 266 PRO A N   1 
ATOM   1598 C  CA  . PRO A 1 251 ? 20.935  9.744   22.868  1.00   97.38  ? 266 PRO A CA  1 
ATOM   1599 C  C   . PRO A 1 251 ? 19.625  9.682   22.042  1.00   83.76  ? 266 PRO A C   1 
ATOM   1600 O  O   . PRO A 1 251 ? 19.431  10.636  21.301  1.00   80.17  ? 266 PRO A O   1 
ATOM   1601 C  CB  . PRO A 1 251 ? 21.541  8.418   23.412  1.00   101.97 ? 266 PRO A CB  1 
ATOM   1602 C  CG  . PRO A 1 251 ? 21.391  8.471   24.929  1.00   104.86 ? 266 PRO A CG  1 
ATOM   1603 C  CD  . PRO A 1 251 ? 20.434  9.601   25.213  1.00   107.48 ? 266 PRO A CD  1 
ATOM   1604 N  N   . ARG A 1 252 ? 18.754  8.657   22.058  1.00   74.73  ? 267 ARG A N   1 
ATOM   1605 C  CA  . ARG A 1 252 ? 19.022  7.204   22.178  1.00   70.78  ? 267 ARG A CA  1 
ATOM   1606 C  C   . ARG A 1 252 ? 18.151  6.430   21.205  1.00   62.55  ? 267 ARG A C   1 
ATOM   1607 O  O   . ARG A 1 252 ? 17.975  5.231   21.324  1.00   60.14  ? 267 ARG A O   1 
ATOM   1608 C  CB  . ARG A 1 252 ? 18.691  6.672   23.585  1.00   75.71  ? 267 ARG A CB  1 
ATOM   1609 C  CG  . ARG A 1 252 ? 17.226  6.767   24.016  1.00   77.34  ? 267 ARG A CG  1 
ATOM   1610 C  CD  . ARG A 1 252 ? 17.016  7.943   24.947  1.00   79.43  ? 267 ARG A CD  1 
ATOM   1611 N  NE  . ARG A 1 252 ? 15.621  8.122   25.353  1.00   80.95  ? 267 ARG A NE  1 
ATOM   1612 C  CZ  . ARG A 1 252 ? 15.045  7.537   26.398  1.00   81.29  ? 267 ARG A CZ  1 
ATOM   1613 N  NH1 . ARG A 1 252 ? 15.731  6.708   27.177  1.00   81.31  ? 267 ARG A NH1 1 
ATOM   1614 N  NH2 . ARG A 1 252 ? 13.761  7.787   26.661  1.00   81.54  ? 267 ARG A NH2 1 
ATOM   1615 N  N   . ASP A 1 253 ? 17.591  7.138   20.245  1.00   57.91  ? 268 ASP A N   1 
ATOM   1616 C  CA  . ASP A 1 253 ? 16.471  6.647   19.490  1.00   54.77  ? 268 ASP A CA  1 
ATOM   1617 C  C   . ASP A 1 253 ? 16.154  7.604   18.403  1.00   53.29  ? 268 ASP A C   1 
ATOM   1618 O  O   . ASP A 1 253 ? 16.324  8.820   18.563  1.00   52.85  ? 268 ASP A O   1 
ATOM   1619 C  CB  . ASP A 1 253 ? 15.211  6.584   20.360  1.00   54.87  ? 268 ASP A CB  1 
ATOM   1620 C  CG  . ASP A 1 253 ? 14.791  5.210   20.631  1.00   54.81  ? 268 ASP A CG  1 
ATOM   1621 O  OD1 . ASP A 1 253 ? 15.132  4.327   19.810  1.00   57.55  ? 268 ASP A OD1 1 
ATOM   1622 O  OD2 . ASP A 1 253 ? 14.127  5.001   21.649  1.00   54.50  ? 268 ASP A OD2 1 
ATOM   1623 N  N   . LEU A 1 254 ? 15.618  7.063   17.324  1.00   50.76  ? 269 LEU A N   1 
ATOM   1624 C  CA  . LEU A 1 254 ? 15.148  7.901   16.264  1.00   50.35  ? 269 LEU A CA  1 
ATOM   1625 C  C   . LEU A 1 254 ? 14.028  8.774   16.792  1.00   48.19  ? 269 LEU A C   1 
ATOM   1626 O  O   . LEU A 1 254 ? 13.906  9.953   16.447  1.00   46.50  ? 269 LEU A O   1 
ATOM   1627 C  CB  . LEU A 1 254 ? 14.661  7.035   15.118  1.00   52.42  ? 269 LEU A CB  1 
ATOM   1628 C  CG  . LEU A 1 254 ? 14.567  7.778   13.795  1.00   55.35  ? 269 LEU A CG  1 
ATOM   1629 C  CD1 . LEU A 1 254 ? 14.896  6.799   12.690  1.00   57.24  ? 269 LEU A CD1 1 
ATOM   1630 C  CD2 . LEU A 1 254 ? 13.201  8.433   13.559  1.00   55.44  ? 269 LEU A CD2 1 
ATOM   1631 N  N   . LEU A 1 255 ? 13.203  8.182   17.642  1.00   48.26  ? 270 LEU A N   1 
ATOM   1632 C  CA  . LEU A 1 255 ? 12.054  8.886   18.213  1.00   49.31  ? 270 LEU A CA  1 
ATOM   1633 C  C   . LEU A 1 255 ? 12.509  10.030  19.152  1.00   51.28  ? 270 LEU A C   1 
ATOM   1634 O  O   . LEU A 1 255 ? 12.035  11.165  19.047  1.00   52.64  ? 270 LEU A O   1 
ATOM   1635 C  CB  . LEU A 1 255 ? 11.167  7.867   18.913  1.00   49.25  ? 270 LEU A CB  1 
ATOM   1636 C  CG  . LEU A 1 255 ? 9.729   8.225   19.203  1.00   50.69  ? 270 LEU A CG  1 
ATOM   1637 C  CD1 . LEU A 1 255 ? 8.997   8.586   17.929  1.00   50.05  ? 270 LEU A CD1 1 
ATOM   1638 C  CD2 . LEU A 1 255 ? 9.074   7.035   19.892  1.00   51.99  ? 270 LEU A CD2 1 
ATOM   1639 N  N   . ASP A 1 256 ? 13.452  9.738   20.041  1.00   51.10  ? 271 ASP A N   1 
ATOM   1640 C  CA  . ASP A 1 256 ? 14.135  10.786  20.769  1.00   52.70  ? 271 ASP A CA  1 
ATOM   1641 C  C   . ASP A 1 256 ? 14.624  11.892  19.863  1.00   50.00  ? 271 ASP A C   1 
ATOM   1642 O  O   . ASP A 1 256 ? 14.284  13.049  20.083  1.00   51.01  ? 271 ASP A O   1 
ATOM   1643 C  CB  . ASP A 1 256 ? 15.319  10.219  21.535  1.00   55.89  ? 271 ASP A CB  1 
ATOM   1644 C  CG  . ASP A 1 256 ? 14.959  9.823   22.936  1.00   58.75  ? 271 ASP A CG  1 
ATOM   1645 O  OD1 . ASP A 1 256 ? 14.035  9.029   23.131  1.00   61.29  ? 271 ASP A OD1 1 
ATOM   1646 O  OD2 . ASP A 1 256 ? 15.595  10.313  23.878  1.00   65.47  ? 271 ASP A OD2 1 
ATOM   1647 N  N   . ALA A 1 257 ? 15.421  11.522  18.860  1.00   47.08  ? 272 ALA A N   1 
ATOM   1648 C  CA  . ALA A 1 257 ? 16.021  12.469  17.876  1.00   46.02  ? 272 ALA A CA  1 
ATOM   1649 C  C   . ALA A 1 257 ? 15.044  13.419  17.179  1.00   45.43  ? 272 ALA A C   1 
ATOM   1650 O  O   . ALA A 1 257 ? 15.359  14.585  16.972  1.00   45.00  ? 272 ALA A O   1 
ATOM   1651 C  CB  . ALA A 1 257 ? 16.829  11.709  16.825  1.00   44.16  ? 272 ALA A CB  1 
ATOM   1652 N  N   . LEU A 1 258 ? 13.876  12.906  16.807  1.00   45.47  ? 273 LEU A N   1 
ATOM   1653 C  CA  . LEU A 1 258 ? 12.810  13.743  16.271  1.00   46.83  ? 273 LEU A CA  1 
ATOM   1654 C  C   . LEU A 1 258 ? 12.239  14.661  17.347  1.00   49.36  ? 273 LEU A C   1 
ATOM   1655 O  O   . LEU A 1 258 ? 12.005  15.849  17.104  1.00   50.70  ? 273 LEU A O   1 
ATOM   1656 C  CB  . LEU A 1 258 ? 11.667  12.883  15.718  1.00   46.74  ? 273 LEU A CB  1 
ATOM   1657 C  CG  . LEU A 1 258 ? 11.900  11.986  14.491  1.00   44.91  ? 273 LEU A CG  1 
ATOM   1658 C  CD1 . LEU A 1 258 ? 10.778  10.980  14.287  1.00   44.14  ? 273 LEU A CD1 1 
ATOM   1659 C  CD2 . LEU A 1 258 ? 12.047  12.849  13.260  1.00   44.94  ? 273 LEU A CD2 1 
ATOM   1660 N  N   . LEU A 1 259 ? 11.996  14.111  18.535  1.00   50.59  ? 274 LEU A N   1 
ATOM   1661 C  CA  . LEU A 1 259 ? 11.373  14.890  19.605  1.00   51.87  ? 274 LEU A CA  1 
ATOM   1662 C  C   . LEU A 1 259 ? 12.231  16.041  20.052  1.00   53.26  ? 274 LEU A C   1 
ATOM   1663 O  O   . LEU A 1 259 ? 11.712  17.146  20.245  1.00   55.25  ? 274 LEU A O   1 
ATOM   1664 C  CB  . LEU A 1 259 ? 11.048  14.018  20.795  1.00   52.65  ? 274 LEU A CB  1 
ATOM   1665 C  CG  . LEU A 1 259 ? 9.872   13.089  20.548  1.00   51.87  ? 274 LEU A CG  1 
ATOM   1666 C  CD1 . LEU A 1 259 ? 9.865   12.048  21.651  1.00   52.43  ? 274 LEU A CD1 1 
ATOM   1667 C  CD2 . LEU A 1 259 ? 8.566   13.875  20.500  1.00   52.47  ? 274 LEU A CD2 1 
ATOM   1668 N  N   . ILE A 1 260 ? 13.529  15.787  20.216  1.00   52.82  ? 275 ILE A N   1 
ATOM   1669 C  CA  . ILE A 1 260 ? 14.503  16.869  20.361  1.00   53.85  ? 275 ILE A CA  1 
ATOM   1670 C  C   . ILE A 1 260 ? 14.286  17.904  19.252  1.00   53.05  ? 275 ILE A C   1 
ATOM   1671 O  O   . ILE A 1 260 ? 14.127  19.088  19.509  1.00   53.58  ? 275 ILE A O   1 
ATOM   1672 C  CB  . ILE A 1 260 ? 15.967  16.383  20.213  1.00   53.89  ? 275 ILE A CB  1 
ATOM   1673 C  CG1 . ILE A 1 260 ? 16.306  15.193  21.132  1.00   54.93  ? 275 ILE A CG1 1 
ATOM   1674 C  CG2 . ILE A 1 260 ? 16.934  17.537  20.424  1.00   54.60  ? 275 ILE A CG2 1 
ATOM   1675 C  CD1 . ILE A 1 260 ? 15.727  15.240  22.524  1.00   56.49  ? 275 ILE A CD1 1 
ATOM   1676 N  N   . GLY A 1 261 ? 14.296  17.452  18.009  1.00   51.81  ? 276 GLY A N   1 
ATOM   1677 C  CA  . GLY A 1 261 ? 14.208  18.376  16.889  1.00   53.27  ? 276 GLY A CA  1 
ATOM   1678 C  C   . GLY A 1 261 ? 12.941  19.202  16.957  1.00   54.95  ? 276 GLY A C   1 
ATOM   1679 O  O   . GLY A 1 261 ? 12.921  20.384  16.600  1.00   55.04  ? 276 GLY A O   1 
ATOM   1680 N  N   . GLN A 1 262 ? 11.886  18.557  17.430  1.00   56.16  ? 277 GLN A N   1 
ATOM   1681 C  CA  . GLN A 1 262 ? 10.599  19.177  17.558  1.00   58.60  ? 277 GLN A CA  1 
ATOM   1682 C  C   . GLN A 1 262 ? 10.558  20.026  18.839  1.00   62.23  ? 277 GLN A C   1 
ATOM   1683 O  O   . GLN A 1 262 ? 9.889   21.061  18.884  1.00   63.53  ? 277 GLN A O   1 
ATOM   1684 C  CB  . GLN A 1 262 ? 9.528   18.083  17.511  1.00   57.24  ? 277 GLN A CB  1 
ATOM   1685 C  CG  . GLN A 1 262 ? 8.113   18.603  17.392  1.00   57.02  ? 277 GLN A CG  1 
ATOM   1686 C  CD  . GLN A 1 262 ? 7.469   18.790  18.729  1.00   58.12  ? 277 GLN A CD  1 
ATOM   1687 O  OE1 . GLN A 1 262 ? 7.946   18.260  19.733  1.00   60.49  ? 277 GLN A OE1 1 
ATOM   1688 N  NE2 . GLN A 1 262 ? 6.382   19.544  18.762  1.00   58.80  ? 277 GLN A NE2 1 
ATOM   1689 N  N   . GLN A 1 263 ? 11.281  19.594  19.865  1.00   65.19  ? 278 GLN A N   1 
ATOM   1690 C  CA  . GLN A 1 263 ? 11.605  20.458  21.008  1.00   71.25  ? 278 GLN A CA  1 
ATOM   1691 C  C   . GLN A 1 263 ? 11.980  21.862  20.552  1.00   72.23  ? 278 GLN A C   1 
ATOM   1692 O  O   . GLN A 1 263 ? 11.436  22.841  21.038  1.00   74.57  ? 278 GLN A O   1 
ATOM   1693 C  CB  . GLN A 1 263 ? 12.796  19.901  21.795  1.00   74.44  ? 278 GLN A CB  1 
ATOM   1694 C  CG  . GLN A 1 263 ? 12.529  19.430  23.209  1.00   78.32  ? 278 GLN A CG  1 
ATOM   1695 C  CD  . GLN A 1 263 ? 13.796  19.514  24.067  1.00   82.01  ? 278 GLN A CD  1 
ATOM   1696 O  OE1 . GLN A 1 263 ? 14.120  20.574  24.619  1.00   84.14  ? 278 GLN A OE1 1 
ATOM   1697 N  NE2 . GLN A 1 263 ? 14.515  18.397  24.181  1.00   80.28  ? 278 GLN A NE2 1 
ATOM   1698 N  N   . ARG A 1 264 ? 12.914  21.944  19.612  1.00   73.84  ? 279 ARG A N   1 
ATOM   1699 C  CA  . ARG A 1 264 ? 13.408  23.227  19.113  1.00   77.78  ? 279 ARG A CA  1 
ATOM   1700 C  C   . ARG A 1 264 ? 12.386  23.754  18.116  1.00   78.73  ? 279 ARG A C   1 
ATOM   1701 O  O   . ARG A 1 264 ? 12.601  23.650  16.924  1.00   79.80  ? 279 ARG A O   1 
ATOM   1702 C  CB  . ARG A 1 264 ? 14.753  23.049  18.400  1.00   80.36  ? 279 ARG A CB  1 
ATOM   1703 C  CG  . ARG A 1 264 ? 15.750  22.112  19.078  1.00   85.50  ? 279 ARG A CG  1 
ATOM   1704 C  CD  . ARG A 1 264 ? 16.890  21.749  18.134  1.00   89.57  ? 279 ARG A CD  1 
ATOM   1705 N  NE  . ARG A 1 264 ? 17.790  22.886  17.952  1.00   96.34  ? 279 ARG A NE  1 
ATOM   1706 C  CZ  . ARG A 1 264 ? 19.118  22.864  18.120  1.00   103.22 ? 279 ARG A CZ  1 
ATOM   1707 N  NH1 . ARG A 1 264 ? 19.770  21.742  18.447  1.00   103.81 ? 279 ARG A NH1 1 
ATOM   1708 N  NH2 . ARG A 1 264 ? 19.812  23.988  17.943  1.00   105.75 ? 279 ARG A NH2 1 
ATOM   1709 N  N   . GLY A 1 265 ? 11.270  24.298  18.593  1.00   79.72  ? 280 GLY A N   1 
ATOM   1710 C  CA  . GLY A 1 265 ? 10.111  24.518  17.735  1.00   79.08  ? 280 GLY A CA  1 
ATOM   1711 C  C   . GLY A 1 265 ? 9.396   25.831  17.954  1.00   81.32  ? 280 GLY A C   1 
ATOM   1712 O  O   . GLY A 1 265 ? 8.180   25.858  18.197  1.00   80.36  ? 280 GLY A O   1 
ATOM   1713 N  N   . SER A 1 266 ? 10.156  26.915  17.826  1.00   82.97  ? 281 SER A N   1 
ATOM   1714 C  CA  . SER A 1 266 ? 9.643   28.282  17.975  1.00   85.26  ? 281 SER A CA  1 
ATOM   1715 C  C   . SER A 1 266 ? 8.134   28.424  17.703  1.00   85.75  ? 281 SER A C   1 
ATOM   1716 O  O   . SER A 1 266 ? 7.355   28.426  18.653  1.00   84.72  ? 281 SER A O   1 
ATOM   1717 C  CB  . SER A 1 266 ? 10.455  29.253  17.098  1.00   85.65  ? 281 SER A CB  1 
ATOM   1718 O  OG  . SER A 1 266 ? 10.559  28.794  15.755  1.00   83.46  ? 281 SER A OG  1 
ATOM   1719 N  N   . GLY A 1 267 ? 7.732   28.511  16.428  1.00   86.01  ? 282 GLY A N   1 
ATOM   1720 C  CA  . GLY A 1 267 ? 6.347   28.845  16.062  1.00   86.82  ? 282 GLY A CA  1 
ATOM   1721 C  C   . GLY A 1 267 ? 5.848   28.269  14.741  1.00   87.26  ? 282 GLY A C   1 
ATOM   1722 O  O   . GLY A 1 267 ? 6.617   27.969  13.834  1.00   88.92  ? 282 GLY A O   1 
ATOM   1723 N  N   . GLY A 1 268 ? 4.531   28.169  14.632  1.00   87.55  ? 283 GLY A N   1 
ATOM   1724 C  CA  . GLY A 1 268 ? 3.851   27.392  13.595  1.00   86.68  ? 283 GLY A CA  1 
ATOM   1725 C  C   . GLY A 1 268 ? 4.405   27.281  12.187  1.00   83.88  ? 283 GLY A C   1 
ATOM   1726 O  O   . GLY A 1 268 ? 4.726   26.180  11.739  1.00   82.81  ? 283 GLY A O   1 
ATOM   1727 N  N   . ALA A 1 269 ? 4.492   28.408  11.482  1.00   84.14  ? 284 ALA A N   1 
ATOM   1728 C  CA  . ALA A 1 269 ? 4.701   28.412  10.017  1.00   82.38  ? 284 ALA A CA  1 
ATOM   1729 C  C   . ALA A 1 269 ? 5.370   27.142  9.453   1.00   77.64  ? 284 ALA A C   1 
ATOM   1730 O  O   . ALA A 1 269 ? 4.706   26.298  8.844   1.00   77.59  ? 284 ALA A O   1 
ATOM   1731 C  CB  . ALA A 1 269 ? 5.469   29.665  9.584   1.00   83.71  ? 284 ALA A CB  1 
ATOM   1732 N  N   . ASP A 1 270 ? 6.676   27.007  9.670   1.00   72.36  ? 285 ASP A N   1 
ATOM   1733 C  CA  . ASP A 1 270 ? 7.452   25.958  9.026   1.00   68.00  ? 285 ASP A CA  1 
ATOM   1734 C  C   . ASP A 1 270 ? 8.021   24.990  10.062  1.00   65.48  ? 285 ASP A C   1 
ATOM   1735 O  O   . ASP A 1 270 ? 8.940   24.228  9.756   1.00   64.28  ? 285 ASP A O   1 
ATOM   1736 C  CB  . ASP A 1 270 ? 8.605   26.566  8.186   1.00   67.74  ? 285 ASP A CB  1 
ATOM   1737 C  CG  . ASP A 1 270 ? 8.160   27.758  7.284   1.00   65.65  ? 285 ASP A CG  1 
ATOM   1738 O  OD1 . ASP A 1 270 ? 6.953   27.877  6.939   1.00   61.78  ? 285 ASP A OD1 1 
ATOM   1739 O  OD2 . ASP A 1 270 ? 9.052   28.566  6.916   1.00   61.92  ? 285 ASP A OD2 1 
ATOM   1740 N  N   . ASP A 1 271 ? 7.477   25.019  11.280  1.00   64.22  ? 286 ASP A N   1 
ATOM   1741 C  CA  . ASP A 1 271 ? 7.922   24.133  12.362  1.00   61.71  ? 286 ASP A CA  1 
ATOM   1742 C  C   . ASP A 1 271 ? 7.079   22.890  12.446  1.00   60.64  ? 286 ASP A C   1 
ATOM   1743 O  O   . ASP A 1 271 ? 5.878   22.935  12.208  1.00   62.48  ? 286 ASP A O   1 
ATOM   1744 C  CB  . ASP A 1 271 ? 7.817   24.825  13.710  1.00   63.26  ? 286 ASP A CB  1 
ATOM   1745 C  CG  . ASP A 1 271 ? 8.926   25.799  13.953  1.00   63.08  ? 286 ASP A CG  1 
ATOM   1746 O  OD1 . ASP A 1 271 ? 9.844   25.879  13.115  1.00   60.58  ? 286 ASP A OD1 1 
ATOM   1747 O  OD2 . ASP A 1 271 ? 8.859   26.497  14.986  1.00   64.53  ? 286 ASP A OD2 1 
ATOM   1748 N  N   . ILE A 1 272 ? 7.709   21.784  12.822  1.00   59.27  ? 287 ILE A N   1 
ATOM   1749 C  CA  . ILE A 1 272 ? 7.014   20.509  12.887  1.00   58.78  ? 287 ILE A CA  1 
ATOM   1750 C  C   . ILE A 1 272 ? 6.240   20.377  14.188  1.00   58.88  ? 287 ILE A C   1 
ATOM   1751 O  O   . ILE A 1 272 ? 6.749   20.644  15.261  1.00   60.45  ? 287 ILE A O   1 
ATOM   1752 C  CB  . ILE A 1 272 ? 7.956   19.289  12.677  1.00   58.40  ? 287 ILE A CB  1 
ATOM   1753 C  CG1 . ILE A 1 272 ? 9.056   19.204  13.732  1.00   59.82  ? 287 ILE A CG1 1 
ATOM   1754 C  CG2 . ILE A 1 272 ? 8.607   19.336  11.300  1.00   57.44  ? 287 ILE A CG2 1 
ATOM   1755 C  CD1 . ILE A 1 272 ? 9.726   17.846  13.752  1.00   58.72  ? 287 ILE A CD1 1 
ATOM   1756 N  N   . THR A 1 273 ? 4.976   20.007  14.075  1.00   59.56  ? 288 THR A N   1 
ATOM   1757 C  CA  . THR A 1 273 ? 4.232   19.569  15.236  1.00   60.21  ? 288 THR A CA  1 
ATOM   1758 C  C   . THR A 1 273 ? 4.723   18.193  15.643  1.00   57.73  ? 288 THR A C   1 
ATOM   1759 O  O   . THR A 1 273 ? 5.522   17.564  14.967  1.00   54.28  ? 288 THR A O   1 
ATOM   1760 C  CB  . THR A 1 273 ? 2.699   19.442  15.024  1.00   63.07  ? 288 THR A CB  1 
ATOM   1761 O  OG1 . THR A 1 273 ? 2.323   18.043  15.026  1.00   63.62  ? 288 THR A OG1 1 
ATOM   1762 C  CG2 . THR A 1 273 ? 2.195   20.127  13.727  1.00   64.18  ? 288 THR A CG2 1 
ATOM   1763 N  N   . GLU A 1 274 ? 4.194   17.748  16.773  1.00   59.10  ? 289 GLU A N   1 
ATOM   1764 C  CA  . GLU A 1 274 ? 4.380   16.395  17.293  1.00   57.46  ? 289 GLU A CA  1 
ATOM   1765 C  C   . GLU A 1 274 ? 3.768   15.306  16.367  1.00   53.81  ? 289 GLU A C   1 
ATOM   1766 O  O   . GLU A 1 274 ? 4.214   14.158  16.384  1.00   52.40  ? 289 GLU A O   1 
ATOM   1767 C  CB  . GLU A 1 274 ? 3.731   16.329  18.682  1.00   59.82  ? 289 GLU A CB  1 
ATOM   1768 C  CG  . GLU A 1 274 ? 4.581   15.678  19.745  1.00   62.73  ? 289 GLU A CG  1 
ATOM   1769 C  CD  . GLU A 1 274 ? 3.933   15.781  21.116  1.00   67.48  ? 289 GLU A CD  1 
ATOM   1770 O  OE1 . GLU A 1 274 ? 2.789   15.290  21.235  1.00   73.37  ? 289 GLU A OE1 1 
ATOM   1771 O  OE2 . GLU A 1 274 ? 4.535   16.356  22.059  1.00   66.18  ? 289 GLU A OE2 1 
ATOM   1772 N  N   . ASP A 1 275 ? 2.748   15.655  15.583  1.00   50.09  ? 290 ASP A N   1 
ATOM   1773 C  CA  . ASP A 1 275 ? 2.081   14.680  14.751  1.00   48.33  ? 290 ASP A CA  1 
ATOM   1774 C  C   . ASP A 1 275 ? 3.001   14.146  13.657  1.00   45.54  ? 290 ASP A C   1 
ATOM   1775 O  O   . ASP A 1 275 ? 2.925   12.983  13.299  1.00   43.04  ? 290 ASP A O   1 
ATOM   1776 C  CB  . ASP A 1 275 ? 0.784   15.274  14.177  1.00   50.00  ? 290 ASP A CB  1 
ATOM   1777 C  CG  . ASP A 1 275 ? -0.277  15.542  15.276  1.00   53.00  ? 290 ASP A CG  1 
ATOM   1778 O  OD1 . ASP A 1 275 ? -0.179  14.892  16.353  1.00   53.81  ? 290 ASP A OD1 1 
ATOM   1779 O  OD2 . ASP A 1 275 ? -1.191  16.401  15.083  1.00   53.34  ? 290 ASP A OD2 1 
ATOM   1780 N  N   . HIS A 1 276 ? 3.887   15.002  13.152  1.00   45.49  ? 291 HIS A N   1 
ATOM   1781 C  CA  . HIS A 1 276 ? 4.948   14.618  12.206  1.00   43.87  ? 291 HIS A CA  1 
ATOM   1782 C  C   . HIS A 1 276 ? 5.958   13.644  12.809  1.00   43.23  ? 291 HIS A C   1 
ATOM   1783 O  O   . HIS A 1 276 ? 6.521   12.810  12.109  1.00   43.33  ? 291 HIS A O   1 
ATOM   1784 C  CB  . HIS A 1 276 ? 5.738   15.846  11.767  1.00   44.25  ? 291 HIS A CB  1 
ATOM   1785 C  CG  . HIS A 1 276 ? 4.920   16.889  11.070  1.00   46.28  ? 291 HIS A CG  1 
ATOM   1786 N  ND1 . HIS A 1 276 ? 4.497   18.041  11.696  1.00   48.44  ? 291 HIS A ND1 1 
ATOM   1787 C  CD2 . HIS A 1 276 ? 4.466   16.967  9.796   1.00   46.75  ? 291 HIS A CD2 1 
ATOM   1788 C  CE1 . HIS A 1 276 ? 3.813   18.781  10.839  1.00   49.55  ? 291 HIS A CE1 1 
ATOM   1789 N  NE2 . HIS A 1 276 ? 3.773   18.148  9.680   1.00   47.99  ? 291 HIS A NE2 1 
ATOM   1790 N  N   . VAL A 1 277 ? 6.231   13.775  14.098  1.00   43.32  ? 292 VAL A N   1 
ATOM   1791 C  CA  . VAL A 1 277 ? 7.145   12.852  14.758  1.00   42.64  ? 292 VAL A CA  1 
ATOM   1792 C  C   . VAL A 1 277 ? 6.523   11.494  14.690  1.00   41.54  ? 292 VAL A C   1 
ATOM   1793 O  O   . VAL A 1 277 ? 7.137   10.520  14.251  1.00   40.85  ? 292 VAL A O   1 
ATOM   1794 C  CB  . VAL A 1 277 ? 7.401   13.175  16.254  1.00   44.27  ? 292 VAL A CB  1 
ATOM   1795 C  CG1 . VAL A 1 277 ? 8.353   12.154  16.856  1.00   44.15  ? 292 VAL A CG1 1 
ATOM   1796 C  CG2 . VAL A 1 277 ? 7.984   14.572  16.438  1.00   45.41  ? 292 VAL A CG2 1 
ATOM   1797 N  N   . LEU A 1 278 ? 5.289   11.426  15.148  1.00   41.81  ? 293 LEU A N   1 
ATOM   1798 C  CA  . LEU A 1 278 ? 4.592   10.175  15.141  1.00   41.20  ? 293 LEU A CA  1 
ATOM   1799 C  C   . LEU A 1 278 ? 4.540   9.634   13.699  1.00   39.96  ? 293 LEU A C   1 
ATOM   1800 O  O   . LEU A 1 278 ? 4.924   8.495   13.441  1.00   39.49  ? 293 LEU A O   1 
ATOM   1801 C  CB  . LEU A 1 278 ? 3.214   10.363  15.743  1.00   42.44  ? 293 LEU A CB  1 
ATOM   1802 C  CG  . LEU A 1 278 ? 2.488   9.054   16.014  1.00   43.35  ? 293 LEU A CG  1 
ATOM   1803 C  CD1 . LEU A 1 278 ? 3.118   8.350   17.215  1.00   44.15  ? 293 LEU A CD1 1 
ATOM   1804 C  CD2 . LEU A 1 278 ? 0.988   9.297   16.219  1.00   44.41  ? 293 LEU A CD2 1 
ATOM   1805 N  N   . MET A 1 279 ? 4.117   10.459  12.748  1.00   39.33  ? 294 MET A N   1 
ATOM   1806 C  CA  . MET A 1 279 ? 4.005   9.988   11.376  1.00   38.19  ? 294 MET A CA  1 
ATOM   1807 C  C   . MET A 1 279 ? 5.349   9.537   10.818  1.00   37.76  ? 294 MET A C   1 
ATOM   1808 O  O   . MET A 1 279 ? 5.437   8.509   10.147  1.00   37.88  ? 294 MET A O   1 
ATOM   1809 C  CB  . MET A 1 279 ? 3.339   11.036  10.489  1.00   37.83  ? 294 MET A CB  1 
ATOM   1810 C  CG  . MET A 1 279 ? 1.879   11.292  10.852  1.00   38.16  ? 294 MET A CG  1 
ATOM   1811 S  SD  . MET A 1 279 ? 0.847   9.822   10.741  1.00   37.87  ? 294 MET A SD  1 
ATOM   1812 C  CE  . MET A 1 279 ? 0.896   9.098   12.356  1.00   39.10  ? 294 MET A CE  1 
ATOM   1813 N  N   . THR A 1 280 ? 6.413   10.251  11.135  1.00   37.88  ? 295 THR A N   1 
ATOM   1814 C  CA  . THR A 1 280 ? 7.714   9.815   10.685  1.00   37.39  ? 295 THR A CA  1 
ATOM   1815 C  C   . THR A 1 280 ? 8.144   8.464   11.282  1.00   37.16  ? 295 THR A C   1 
ATOM   1816 O  O   . THR A 1 280 ? 8.836   7.677   10.629  1.00   36.05  ? 295 THR A O   1 
ATOM   1817 C  CB  . THR A 1 280 ? 8.743   10.886  10.969  1.00   38.83  ? 295 THR A CB  1 
ATOM   1818 O  OG1 . THR A 1 280 ? 8.411   12.043  10.184  1.00   39.21  ? 295 THR A OG1 1 
ATOM   1819 C  CG2 . THR A 1 280 ? 10.191  10.373  10.637  1.00   38.42  ? 295 THR A CG2 1 
ATOM   1820 N  N   . ALA A 1 281 ? 7.739   8.192   12.519  1.00   37.97  ? 296 ALA A N   1 
ATOM   1821 C  CA  . ALA A 1 281 ? 8.018   6.894   13.143  1.00   37.18  ? 296 ALA A CA  1 
ATOM   1822 C  C   . ALA A 1 281 ? 7.223   5.793   12.459  1.00   36.77  ? 296 ALA A C   1 
ATOM   1823 O  O   . ALA A 1 281 ? 7.718   4.695   12.243  1.00   35.49  ? 296 ALA A O   1 
ATOM   1824 C  CB  . ALA A 1 281 ? 7.649   6.948   14.593  1.00   38.41  ? 296 ALA A CB  1 
ATOM   1825 N  N   . ALA A 1 282 ? 5.972   6.093   12.128  1.00   37.13  ? 297 ALA A N   1 
ATOM   1826 C  CA  . ALA A 1 282 ? 5.112   5.119   11.488  1.00   36.85  ? 297 ALA A CA  1 
ATOM   1827 C  C   . ALA A 1 282 ? 5.692   4.805   10.142  1.00   35.90  ? 297 ALA A C   1 
ATOM   1828 O  O   . ALA A 1 282 ? 5.791   3.643   9.742   1.00   35.68  ? 297 ALA A O   1 
ATOM   1829 C  CB  . ALA A 1 282 ? 3.714   5.672   11.331  1.00   37.51  ? 297 ALA A CB  1 
ATOM   1830 N  N   . GLU A 1 283 ? 6.107   5.852   9.448   1.00   35.41  ? 298 GLU A N   1 
ATOM   1831 C  CA  . GLU A 1 283 ? 6.679   5.687   8.120   1.00   34.89  ? 298 GLU A CA  1 
ATOM   1832 C  C   . GLU A 1 283 ? 7.986   4.895   8.095   1.00   34.64  ? 298 GLU A C   1 
ATOM   1833 O  O   . GLU A 1 283 ? 8.288   4.260   7.104   1.00   34.47  ? 298 GLU A O   1 
ATOM   1834 C  CB  . GLU A 1 283 ? 6.908   7.043   7.477   1.00   34.79  ? 298 GLU A CB  1 
ATOM   1835 C  CG  . GLU A 1 283 ? 7.216   6.935   6.010   1.00   34.77  ? 298 GLU A CG  1 
ATOM   1836 C  CD  . GLU A 1 283 ? 6.627   8.089   5.248   1.00   35.38  ? 298 GLU A CD  1 
ATOM   1837 O  OE1 . GLU A 1 283 ? 7.333   9.105   5.032   1.00   35.46  ? 298 GLU A OE1 1 
ATOM   1838 O  OE2 . GLU A 1 283 ? 5.435   7.988   4.902   1.00   36.49  ? 298 GLU A OE2 1 
ATOM   1839 N  N   . ALA A 1 284 ? 8.772   4.926   9.171   1.00   35.08  ? 299 ALA A N   1 
ATOM   1840 C  CA  . ALA A 1 284 ? 10.002  4.163   9.153   1.00   34.98  ? 299 ALA A CA  1 
ATOM   1841 C  C   . ALA A 1 284 ? 9.704   2.689   8.919   1.00   34.47  ? 299 ALA A C   1 
ATOM   1842 O  O   . ALA A 1 284 ? 10.485  1.980   8.306   1.00   34.56  ? 299 ALA A O   1 
ATOM   1843 C  CB  . ALA A 1 284 ? 10.823  4.390   10.409  1.00   35.51  ? 299 ALA A CB  1 
ATOM   1844 N  N   . PHE A 1 285 ? 8.548   2.253   9.381   1.00   35.12  ? 300 PHE A N   1 
ATOM   1845 C  CA  . PHE A 1 285 ? 8.037   0.925   9.084   1.00   35.12  ? 300 PHE A CA  1 
ATOM   1846 C  C   . PHE A 1 285 ? 7.434   0.931   7.693   1.00   34.23  ? 300 PHE A C   1 
ATOM   1847 O  O   . PHE A 1 285 ? 7.884   0.241   6.794   1.00   33.73  ? 300 PHE A O   1 
ATOM   1848 C  CB  . PHE A 1 285 ? 6.953   0.539   10.105  1.00   36.22  ? 300 PHE A CB  1 
ATOM   1849 C  CG  . PHE A 1 285 ? 7.450   0.440   11.515  1.00   36.70  ? 300 PHE A CG  1 
ATOM   1850 C  CD1 . PHE A 1 285 ? 7.935   -0.756  12.003  1.00   37.43  ? 300 PHE A CD1 1 
ATOM   1851 C  CD2 . PHE A 1 285 ? 7.439   1.540   12.352  1.00   36.97  ? 300 PHE A CD2 1 
ATOM   1852 C  CE1 . PHE A 1 285 ? 8.398   -0.852  13.304  1.00   38.04  ? 300 PHE A CE1 1 
ATOM   1853 C  CE2 . PHE A 1 285 ? 7.900   1.445   13.657  1.00   37.45  ? 300 PHE A CE2 1 
ATOM   1854 C  CZ  . PHE A 1 285 ? 8.385   0.253   14.127  1.00   37.85  ? 300 PHE A CZ  1 
ATOM   1855 N  N   . GLY A 1 286 ? 6.412   1.732   7.507   1.00   34.51  ? 301 GLY A N   1 
ATOM   1856 C  CA  . GLY A 1 286 ? 5.740   1.791   6.197   1.00   35.76  ? 301 GLY A CA  1 
ATOM   1857 C  C   . GLY A 1 286 ? 6.664   1.689   4.991   1.00   34.99  ? 301 GLY A C   1 
ATOM   1858 O  O   . GLY A 1 286 ? 6.504   0.816   4.160   1.00   35.15  ? 301 GLY A O   1 
ATOM   1859 N  N   . ALA A 1 287 ? 7.661   2.559   4.953   1.00   35.12  ? 302 ALA A N   1 
ATOM   1860 C  CA  . ALA A 1 287 ? 8.640   2.605   3.886   1.00   34.52  ? 302 ALA A CA  1 
ATOM   1861 C  C   . ALA A 1 287 ? 9.765   1.608   4.040   1.00   34.64  ? 302 ALA A C   1 
ATOM   1862 O  O   . ALA A 1 287 ? 10.389  1.213   3.045   1.00   36.53  ? 302 ALA A O   1 
ATOM   1863 C  CB  . ALA A 1 287 ? 9.238   3.994   3.825   1.00   34.12  ? 302 ALA A CB  1 
ATOM   1864 N  N   . GLY A 1 288 ? 10.076  1.230   5.269   1.00   33.77  ? 303 GLY A N   1 
ATOM   1865 C  CA  . GLY A 1 288 ? 11.309  0.494   5.527   1.00   32.93  ? 303 GLY A CA  1 
ATOM   1866 C  C   . GLY A 1 288 ? 11.245  -1.013  5.564   1.00   33.30  ? 303 GLY A C   1 
ATOM   1867 O  O   . GLY A 1 288 ? 12.231  -1.684  5.298   1.00   34.08  ? 303 GLY A O   1 
ATOM   1868 N  N   . VAL A 1 289 ? 10.098  -1.574  5.911   1.00   33.79  ? 304 VAL A N   1 
ATOM   1869 C  CA  . VAL A 1 289 ? 10.036  -3.000  6.165   1.00   34.19  ? 304 VAL A CA  1 
ATOM   1870 C  C   . VAL A 1 289 ? 9.904   -3.778  4.878   1.00   35.80  ? 304 VAL A C   1 
ATOM   1871 O  O   . VAL A 1 289 ? 10.805  -4.562  4.513   1.00   37.02  ? 304 VAL A O   1 
ATOM   1872 C  CB  . VAL A 1 289 ? 8.883   -3.341  7.109   1.00   33.85  ? 304 VAL A CB  1 
ATOM   1873 C  CG1 . VAL A 1 289 ? 8.619   -4.835  7.143   1.00   34.26  ? 304 VAL A CG1 1 
ATOM   1874 C  CG2 . VAL A 1 289 ? 9.230   -2.838  8.486   1.00   34.17  ? 304 VAL A CG2 1 
ATOM   1875 N  N   . GLU A 1 290 ? 8.790   -3.559  4.189   1.00   36.14  ? 305 GLU A N   1 
ATOM   1876 C  CA  . GLU A 1 290 ? 8.492   -4.372  3.066   1.00   37.30  ? 305 GLU A CA  1 
ATOM   1877 C  C   . GLU A 1 290 ? 9.550   -4.203  1.951   1.00   37.02  ? 305 GLU A C   1 
ATOM   1878 O  O   . GLU A 1 290 ? 9.877   -5.167  1.252   1.00   38.14  ? 305 GLU A O   1 
ATOM   1879 C  CB  . GLU A 1 290 ? 7.097   -4.054  2.578   1.00   39.09  ? 305 GLU A CB  1 
ATOM   1880 C  CG  . GLU A 1 290 ? 6.502   -5.170  1.753   1.00   40.72  ? 305 GLU A CG  1 
ATOM   1881 C  CD  . GLU A 1 290 ? 5.735   -6.177  2.582   1.00   43.28  ? 305 GLU A CD  1 
ATOM   1882 O  OE1 . GLU A 1 290 ? 5.216   -5.837  3.666   1.00   44.14  ? 305 GLU A OE1 1 
ATOM   1883 O  OE2 . GLU A 1 290 ? 5.616   -7.328  2.116   1.00   48.80  ? 305 GLU A OE2 1 
ATOM   1884 N  N   . THR A 1 291 ? 10.115  -3.005  1.806   1.00   35.90  ? 306 THR A N   1 
ATOM   1885 C  CA  . THR A 1 291 ? 11.209  -2.794  0.864   1.00   35.54  ? 306 THR A CA  1 
ATOM   1886 C  C   . THR A 1 291 ? 12.449  -3.591  1.240   1.00   38.34  ? 306 THR A C   1 
ATOM   1887 O  O   . THR A 1 291 ? 13.115  -4.194  0.369   1.00   38.89  ? 306 THR A O   1 
ATOM   1888 C  CB  . THR A 1 291 ? 11.625  -1.323  0.811   1.00   34.52  ? 306 THR A CB  1 
ATOM   1889 O  OG1 . THR A 1 291 ? 11.886  -0.843  2.146   1.00   33.80  ? 306 THR A OG1 1 
ATOM   1890 C  CG2 . THR A 1 291 ? 10.530  -0.474  0.131   1.00   33.78  ? 306 THR A CG2 1 
ATOM   1891 N  N   . THR A 1 292 ? 12.793  -3.574  2.530   1.00   39.68  ? 307 THR A N   1 
ATOM   1892 C  CA  . THR A 1 292 ? 14.010  -4.231  2.946   1.00   42.07  ? 307 THR A CA  1 
ATOM   1893 C  C   . THR A 1 292 ? 13.778  -5.726  2.912   1.00   41.06  ? 307 THR A C   1 
ATOM   1894 O  O   . THR A 1 292 ? 14.526  -6.429  2.221   1.00   42.24  ? 307 THR A O   1 
ATOM   1895 C  CB  . THR A 1 292 ? 14.469  -3.778  4.333   1.00   45.78  ? 307 THR A CB  1 
ATOM   1896 O  OG1 . THR A 1 292 ? 13.321  -3.710  5.196   1.00   57.26  ? 307 THR A OG1 1 
ATOM   1897 C  CG2 . THR A 1 292 ? 15.082  -2.426  4.267   1.00   43.78  ? 307 THR A CG2 1 
ATOM   1898 N  N   . SER A 1 293 ? 12.763  -6.222  3.628   1.00   38.84  ? 308 SER A N   1 
ATOM   1899 C  CA  . SER A 1 293 ? 12.470  -7.664  3.584   1.00   40.01  ? 308 SER A CA  1 
ATOM   1900 C  C   . SER A 1 293 ? 12.443  -8.182  2.144   1.00   38.69  ? 308 SER A C   1 
ATOM   1901 O  O   . SER A 1 293 ? 12.995  -9.243  1.857   1.00   39.15  ? 308 SER A O   1 
ATOM   1902 C  CB  . SER A 1 293 ? 11.117  -8.033  4.193   1.00   41.80  ? 308 SER A CB  1 
ATOM   1903 O  OG  . SER A 1 293 ? 10.824  -7.289  5.347   1.00   45.53  ? 308 SER A OG  1 
ATOM   1904 N  N   . THR A 1 294 ? 11.780  -7.471  1.241   1.00   36.07  ? 309 THR A N   1 
ATOM   1905 C  CA  . THR A 1 294 ? 11.674  -7.996  -0.116  1.00   36.41  ? 309 THR A CA  1 
ATOM   1906 C  C   . THR A 1 294 ? 13.035  -8.054  -0.836  1.00   35.57  ? 309 THR A C   1 
ATOM   1907 O  O   . THR A 1 294 ? 13.331  -9.023  -1.544  1.00   35.10  ? 309 THR A O   1 
ATOM   1908 C  CB  . THR A 1 294 ? 10.677  -7.208  -0.980  1.00   35.71  ? 309 THR A CB  1 
ATOM   1909 O  OG1 . THR A 1 294 ? 9.377   -7.345  -0.427  1.00   35.69  ? 309 THR A OG1 1 
ATOM   1910 C  CG2 . THR A 1 294 ? 10.662  -7.748  -2.377  1.00   35.81  ? 309 THR A CG2 1 
ATOM   1911 N  N   . THR A 1 295 ? 13.848  -7.018  -0.656  1.00   34.44  ? 310 THR A N   1 
ATOM   1912 C  CA  . THR A 1 295 ? 15.151  -7.004  -1.274  1.00   34.79  ? 310 THR A CA  1 
ATOM   1913 C  C   . THR A 1 295 ? 15.969  -8.208  -0.800  1.00   35.76  ? 310 THR A C   1 
ATOM   1914 O  O   . THR A 1 295 ? 16.683  -8.821  -1.599  1.00   37.20  ? 310 THR A O   1 
ATOM   1915 C  CB  . THR A 1 295 ? 15.878  -5.699  -0.986  1.00   35.05  ? 310 THR A CB  1 
ATOM   1916 O  OG1 . THR A 1 295 ? 15.051  -4.583  -1.353  1.00   35.44  ? 310 THR A OG1 1 
ATOM   1917 C  CG2 . THR A 1 295 ? 17.139  -5.634  -1.763  1.00   35.82  ? 310 THR A CG2 1 
ATOM   1918 N  N   . LEU A 1 296 ? 15.836  -8.577  0.478   1.00   35.52  ? 311 LEU A N   1 
ATOM   1919 C  CA  . LEU A 1 296 ? 16.434  -9.817  0.991   1.00   35.87  ? 311 LEU A CA  1 
ATOM   1920 C  C   . LEU A 1 296 ? 15.828  -11.061 0.330   1.00   36.32  ? 311 LEU A C   1 
ATOM   1921 O  O   . LEU A 1 296 ? 16.545  -12.016 -0.023  1.00   37.01  ? 311 LEU A O   1 
ATOM   1922 C  CB  . LEU A 1 296 ? 16.233  -9.937  2.510   1.00   36.39  ? 311 LEU A CB  1 
ATOM   1923 C  CG  . LEU A 1 296 ? 16.862  -8.881  3.413   1.00   35.88  ? 311 LEU A CG  1 
ATOM   1924 C  CD1 . LEU A 1 296 ? 16.327  -9.000  4.834   1.00   35.74  ? 311 LEU A CD1 1 
ATOM   1925 C  CD2 . LEU A 1 296 ? 18.383  -9.032  3.361   1.00   36.05  ? 311 LEU A CD2 1 
ATOM   1926 N  N   . LEU A 1 297 ? 14.502  -11.082 0.202   1.00   35.63  ? 312 LEU A N   1 
ATOM   1927 C  CA  . LEU A 1 297 ? 13.849  -12.243 -0.400  1.00   35.45  ? 312 LEU A CA  1 
ATOM   1928 C  C   . LEU A 1 297 ? 14.322  -12.451 -1.828  1.00   35.71  ? 312 LEU A C   1 
ATOM   1929 O  O   . LEU A 1 297 ? 14.534  -13.588 -2.219  1.00   36.92  ? 312 LEU A O   1 
ATOM   1930 C  CB  . LEU A 1 297 ? 12.350  -12.130 -0.352  1.00   34.84  ? 312 LEU A CB  1 
ATOM   1931 C  CG  . LEU A 1 297 ? 11.752  -12.529 0.981   1.00   34.98  ? 312 LEU A CG  1 
ATOM   1932 C  CD1 . LEU A 1 297 ? 10.307  -12.068 1.067   1.00   34.81  ? 312 LEU A CD1 1 
ATOM   1933 C  CD2 . LEU A 1 297 ? 11.878  -14.031 1.201   1.00   36.11  ? 312 LEU A CD2 1 
ATOM   1934 N  N   . TRP A 1 298 ? 14.534  -11.372 -2.583  1.00   34.56  ? 313 TRP A N   1 
ATOM   1935 C  CA  . TRP A 1 298 ? 15.060  -11.504 -3.950  1.00   34.98  ? 313 TRP A CA  1 
ATOM   1936 C  C   . TRP A 1 298 ? 16.517  -12.019 -3.953  1.00   35.87  ? 313 TRP A C   1 
ATOM   1937 O  O   . TRP A 1 298 ? 16.878  -12.929 -4.712  1.00   35.62  ? 313 TRP A O   1 
ATOM   1938 C  CB  . TRP A 1 298 ? 14.971  -10.170 -4.726  1.00   34.01  ? 313 TRP A CB  1 
ATOM   1939 C  CG  . TRP A 1 298 ? 13.628  -9.881  -5.387  1.00   34.01  ? 313 TRP A CG  1 
ATOM   1940 C  CD1 . TRP A 1 298 ? 12.828  -8.787  -5.188  1.00   33.42  ? 313 TRP A CD1 1 
ATOM   1941 C  CD2 . TRP A 1 298 ? 12.955  -10.690 -6.339  1.00   34.33  ? 313 TRP A CD2 1 
ATOM   1942 N  NE1 . TRP A 1 298 ? 11.699  -8.876  -5.949  1.00   33.08  ? 313 TRP A NE1 1 
ATOM   1943 C  CE2 . TRP A 1 298 ? 11.752  -10.042 -6.663  1.00   34.53  ? 313 TRP A CE2 1 
ATOM   1944 C  CE3 . TRP A 1 298 ? 13.247  -11.905 -6.945  1.00   35.58  ? 313 TRP A CE3 1 
ATOM   1945 C  CZ2 . TRP A 1 298 ? 10.831  -10.578 -7.587  1.00   35.96  ? 313 TRP A CZ2 1 
ATOM   1946 C  CZ3 . TRP A 1 298 ? 12.323  -12.448 -7.844  1.00   36.94  ? 313 TRP A CZ3 1 
ATOM   1947 C  CH2 . TRP A 1 298 ? 11.138  -11.776 -8.163  1.00   36.65  ? 313 TRP A CH2 1 
ATOM   1948 N  N   . THR A 1 299 ? 17.344  -11.421 -3.093  1.00   35.84  ? 314 THR A N   1 
ATOM   1949 C  CA  . THR A 1 299 ? 18.742  -11.774 -3.009  1.00   36.44  ? 314 THR A CA  1 
ATOM   1950 C  C   . THR A 1 299 ? 18.895  -13.283 -2.903  1.00   38.76  ? 314 THR A C   1 
ATOM   1951 O  O   . THR A 1 299 ? 19.617  -13.917 -3.677  1.00   41.70  ? 314 THR A O   1 
ATOM   1952 C  CB  . THR A 1 299 ? 19.370  -11.094 -1.797  1.00   35.61  ? 314 THR A CB  1 
ATOM   1953 O  OG1 . THR A 1 299 ? 19.322  -9.676  -1.999  1.00   34.54  ? 314 THR A OG1 1 
ATOM   1954 C  CG2 . THR A 1 299 ? 20.810  -11.547 -1.582  1.00   36.04  ? 314 THR A CG2 1 
ATOM   1955 N  N   . ILE A 1 300 ? 18.196  -13.854 -1.947  1.00   39.38  ? 315 ILE A N   1 
ATOM   1956 C  CA  . ILE A 1 300 ? 18.252  -15.273 -1.686  1.00   40.97  ? 315 ILE A CA  1 
ATOM   1957 C  C   . ILE A 1 300 ? 17.659  -16.004 -2.854  1.00   42.10  ? 315 ILE A C   1 
ATOM   1958 O  O   . ILE A 1 300 ? 18.180  -17.023 -3.287  1.00   43.60  ? 315 ILE A O   1 
ATOM   1959 C  CB  . ILE A 1 300 ? 17.473  -15.591 -0.379  1.00   41.79  ? 315 ILE A CB  1 
ATOM   1960 C  CG1 . ILE A 1 300 ? 18.353  -15.233 0.817   1.00   42.61  ? 315 ILE A CG1 1 
ATOM   1961 C  CG2 . ILE A 1 300 ? 17.075  -17.048 -0.298  1.00   42.45  ? 315 ILE A CG2 1 
ATOM   1962 C  CD1 . ILE A 1 300 ? 17.594  -15.009 2.093   1.00   43.30  ? 315 ILE A CD1 1 
ATOM   1963 N  N   . ALA A 1 301 ? 16.548  -15.495 -3.371  1.00   42.09  ? 316 ALA A N   1 
ATOM   1964 C  CA  . ALA A 1 301 ? 15.904  -16.151 -4.504  1.00   42.89  ? 316 ALA A CA  1 
ATOM   1965 C  C   . ALA A 1 301 ? 16.878  -16.288 -5.672  1.00   43.36  ? 316 ALA A C   1 
ATOM   1966 O  O   . ALA A 1 301 ? 16.922  -17.331 -6.329  1.00   44.75  ? 316 ALA A O   1 
ATOM   1967 C  CB  . ALA A 1 301 ? 14.636  -15.411 -4.922  1.00   42.09  ? 316 ALA A CB  1 
ATOM   1968 N  N   . PHE A 1 302 ? 17.675  -15.253 -5.903  1.00   42.93  ? 317 PHE A N   1 
ATOM   1969 C  CA  . PHE A 1 302 ? 18.596  -15.262 -7.013  1.00   44.71  ? 317 PHE A CA  1 
ATOM   1970 C  C   . PHE A 1 302 ? 19.807  -16.144 -6.733  1.00   47.13  ? 317 PHE A C   1 
ATOM   1971 O  O   . PHE A 1 302 ? 20.362  -16.758 -7.647  1.00   50.96  ? 317 PHE A O   1 
ATOM   1972 C  CB  . PHE A 1 302 ? 19.014  -13.837 -7.407  1.00   44.24  ? 317 PHE A CB  1 
ATOM   1973 C  CG  . PHE A 1 302 ? 18.044  -13.161 -8.351  1.00   43.75  ? 317 PHE A CG  1 
ATOM   1974 C  CD1 . PHE A 1 302 ? 17.999  -13.520 -9.693  1.00   44.87  ? 317 PHE A CD1 1 
ATOM   1975 C  CD2 . PHE A 1 302 ? 17.179  -12.184 -7.901  1.00   42.76  ? 317 PHE A CD2 1 
ATOM   1976 C  CE1 . PHE A 1 302 ? 17.098  -12.928 -10.571 1.00   44.88  ? 317 PHE A CE1 1 
ATOM   1977 C  CE2 . PHE A 1 302 ? 16.272  -11.588 -8.762  1.00   42.96  ? 317 PHE A CE2 1 
ATOM   1978 C  CZ  . PHE A 1 302 ? 16.236  -11.951 -10.104 1.00   44.11  ? 317 PHE A CZ  1 
ATOM   1979 N  N   . LEU A 1 303 ? 20.222  -16.230 -5.482  1.00   47.56  ? 318 LEU A N   1 
ATOM   1980 C  CA  . LEU A 1 303 ? 21.368  -17.061 -5.150  1.00   48.29  ? 318 LEU A CA  1 
ATOM   1981 C  C   . LEU A 1 303 ? 21.011  -18.519 -5.309  1.00   48.88  ? 318 LEU A C   1 
ATOM   1982 O  O   . LEU A 1 303 ? 21.871  -19.330 -5.575  1.00   49.55  ? 318 LEU A O   1 
ATOM   1983 C  CB  . LEU A 1 303 ? 21.846  -16.777 -3.729  1.00   49.11  ? 318 LEU A CB  1 
ATOM   1984 C  CG  . LEU A 1 303 ? 22.408  -15.361 -3.501  1.00   49.13  ? 318 LEU A CG  1 
ATOM   1985 C  CD1 . LEU A 1 303 ? 22.584  -15.085 -2.002  1.00   49.29  ? 318 LEU A CD1 1 
ATOM   1986 C  CD2 . LEU A 1 303 ? 23.721  -15.139 -4.259  1.00   49.25  ? 318 LEU A CD2 1 
ATOM   1987 N  N   . LEU A 1 304 ? 19.740  -18.864 -5.165  1.00   49.51  ? 319 LEU A N   1 
ATOM   1988 C  CA  . LEU A 1 304 ? 19.325  -20.230 -5.472  1.00   52.14  ? 319 LEU A CA  1 
ATOM   1989 C  C   . LEU A 1 304 ? 19.562  -20.558 -6.937  1.00   53.33  ? 319 LEU A C   1 
ATOM   1990 O  O   . LEU A 1 304 ? 20.097  -21.614 -7.249  1.00   55.05  ? 319 LEU A O   1 
ATOM   1991 C  CB  . LEU A 1 304 ? 17.866  -20.494 -5.093  1.00   52.76  ? 319 LEU A CB  1 
ATOM   1992 C  CG  . LEU A 1 304 ? 17.707  -21.198 -3.748  1.00   53.53  ? 319 LEU A CG  1 
ATOM   1993 C  CD1 . LEU A 1 304 ? 18.422  -20.394 -2.691  1.00   53.26  ? 319 LEU A CD1 1 
ATOM   1994 C  CD2 . LEU A 1 304 ? 16.248  -21.388 -3.357  1.00   54.22  ? 319 LEU A CD2 1 
ATOM   1995 N  N   . HIS A 1 305 ? 19.215  -19.644 -7.835  1.00   53.80  ? 320 HIS A N   1 
ATOM   1996 C  CA  . HIS A 1 305 ? 19.442  -19.884 -9.268  1.00   56.38  ? 320 HIS A CA  1 
ATOM   1997 C  C   . HIS A 1 305 ? 20.929  -19.873 -9.616  1.00   56.44  ? 320 HIS A C   1 
ATOM   1998 O  O   . HIS A 1 305 ? 21.343  -20.434 -10.628 1.00   57.46  ? 320 HIS A O   1 
ATOM   1999 C  CB  . HIS A 1 305 ? 18.682  -18.876 -10.126 1.00   56.36  ? 320 HIS A CB  1 
ATOM   2000 C  CG  . HIS A 1 305 ? 17.209  -19.125 -10.169 1.00   57.89  ? 320 HIS A CG  1 
ATOM   2001 N  ND1 . HIS A 1 305 ? 16.524  -19.336 -11.344 1.00   58.96  ? 320 HIS A ND1 1 
ATOM   2002 C  CD2 . HIS A 1 305 ? 16.288  -19.196 -9.177  1.00   58.97  ? 320 HIS A CD2 1 
ATOM   2003 C  CE1 . HIS A 1 305 ? 15.244  -19.540 -11.072 1.00   60.86  ? 320 HIS A CE1 1 
ATOM   2004 N  NE2 . HIS A 1 305 ? 15.073  -19.457 -9.764  1.00   59.55  ? 320 HIS A NE2 1 
ATOM   2005 N  N   . HIS A 1 306 ? 21.733  -19.255 -8.766  1.00   55.18  ? 321 HIS A N   1 
ATOM   2006 C  CA  . HIS A 1 306 ? 23.139  -19.126 -9.033  1.00   56.51  ? 321 HIS A CA  1 
ATOM   2007 C  C   . HIS A 1 306 ? 24.020  -19.686 -7.907  1.00   56.37  ? 321 HIS A C   1 
ATOM   2008 O  O   . HIS A 1 306 ? 24.760  -18.933 -7.284  1.00   55.29  ? 321 HIS A O   1 
ATOM   2009 C  CB  . HIS A 1 306 ? 23.431  -17.649 -9.303  1.00   55.78  ? 321 HIS A CB  1 
ATOM   2010 C  CG  . HIS A 1 306 ? 22.729  -17.118 -10.515 1.00   56.37  ? 321 HIS A CG  1 
ATOM   2011 N  ND1 . HIS A 1 306 ? 21.442  -16.621 -10.472 1.00   56.27  ? 321 HIS A ND1 1 
ATOM   2012 C  CD2 . HIS A 1 306 ? 23.123  -17.032 -11.808 1.00   57.08  ? 321 HIS A CD2 1 
ATOM   2013 C  CE1 . HIS A 1 306 ? 21.082  -16.231 -11.682 1.00   55.65  ? 321 HIS A CE1 1 
ATOM   2014 N  NE2 . HIS A 1 306 ? 22.084  -16.472 -12.512 1.00   56.30  ? 321 HIS A NE2 1 
ATOM   2015 N  N   . PRO A 1 307 ? 23.977  -21.019 -7.674  1.00   57.78  ? 322 PRO A N   1 
ATOM   2016 C  CA  . PRO A 1 307 ? 24.720  -21.582 -6.545  1.00   58.69  ? 322 PRO A CA  1 
ATOM   2017 C  C   . PRO A 1 307 ? 26.213  -21.277 -6.606  1.00   61.11  ? 322 PRO A C   1 
ATOM   2018 O  O   . PRO A 1 307 ? 26.839  -21.076 -5.558  1.00   59.80  ? 322 PRO A O   1 
ATOM   2019 C  CB  . PRO A 1 307 ? 24.488  -23.093 -6.664  1.00   58.91  ? 322 PRO A CB  1 
ATOM   2020 C  CG  . PRO A 1 307 ? 23.331  -23.249 -7.556  1.00   59.93  ? 322 PRO A CG  1 
ATOM   2021 C  CD  . PRO A 1 307 ? 23.369  -22.079 -8.493  1.00   59.47  ? 322 PRO A CD  1 
ATOM   2022 N  N   . GLN A 1 308 ? 26.771  -21.254 -7.820  1.00   63.23  ? 323 GLN A N   1 
ATOM   2023 C  CA  . GLN A 1 308 ? 28.193  -20.943 -8.005  1.00   65.13  ? 323 GLN A CA  1 
ATOM   2024 C  C   . GLN A 1 308 ? 28.486  -19.576 -7.407  1.00   62.57  ? 323 GLN A C   1 
ATOM   2025 O  O   . GLN A 1 308 ? 29.384  -19.426 -6.578  1.00   63.94  ? 323 GLN A O   1 
ATOM   2026 C  CB  . GLN A 1 308 ? 28.630  -21.048 -9.490  1.00   67.75  ? 323 GLN A CB  1 
ATOM   2027 C  CG  . GLN A 1 308 ? 28.047  -20.029 -10.482 1.00   69.12  ? 323 GLN A CG  1 
ATOM   2028 C  CD  . GLN A 1 308 ? 26.540  -20.198 -10.782 1.00   69.62  ? 323 GLN A CD  1 
ATOM   2029 O  OE1 . GLN A 1 308 ? 26.016  -21.318 -10.839 1.00   71.25  ? 323 GLN A OE1 1 
ATOM   2030 N  NE2 . GLN A 1 308 ? 25.851  -19.079 -11.008 1.00   66.94  ? 323 GLN A NE2 1 
ATOM   2031 N  N   . LEU A 1 309 ? 27.667  -18.602 -7.776  1.00   61.40  ? 324 LEU A N   1 
ATOM   2032 C  CA  . LEU A 1 309 ? 27.810  -17.223 -7.317  1.00   59.44  ? 324 LEU A CA  1 
ATOM   2033 C  C   . LEU A 1 309 ? 27.667  -17.129 -5.800  1.00   57.54  ? 324 LEU A C   1 
ATOM   2034 O  O   . LEU A 1 309 ? 28.351  -16.340 -5.166  1.00   57.29  ? 324 LEU A O   1 
ATOM   2035 C  CB  . LEU A 1 309 ? 26.765  -16.335 -8.019  1.00   58.80  ? 324 LEU A CB  1 
ATOM   2036 C  CG  . LEU A 1 309 ? 26.707  -14.830 -7.729  1.00   58.13  ? 324 LEU A CG  1 
ATOM   2037 C  CD1 . LEU A 1 309 ? 28.037  -14.139 -7.942  1.00   59.57  ? 324 LEU A CD1 1 
ATOM   2038 C  CD2 . LEU A 1 309 ? 25.651  -14.167 -8.592  1.00   57.78  ? 324 LEU A CD2 1 
ATOM   2039 N  N   . GLN A 1 310 ? 26.778  -17.934 -5.222  1.00   56.83  ? 325 GLN A N   1 
ATOM   2040 C  CA  . GLN A 1 310 ? 26.615  -17.969 -3.775  1.00   55.99  ? 325 GLN A CA  1 
ATOM   2041 C  C   . GLN A 1 310 ? 27.892  -18.453 -3.112  1.00   56.59  ? 325 GLN A C   1 
ATOM   2042 O  O   . GLN A 1 310 ? 28.291  -17.920 -2.072  1.00   55.51  ? 325 GLN A O   1 
ATOM   2043 C  CB  . GLN A 1 310 ? 25.449  -18.875 -3.388  1.00   56.39  ? 325 GLN A CB  1 
ATOM   2044 C  CG  . GLN A 1 310 ? 25.323  -19.074 -1.881  1.00   56.17  ? 325 GLN A CG  1 
ATOM   2045 C  CD  . GLN A 1 310 ? 24.143  -19.936 -1.455  1.00   56.59  ? 325 GLN A CD  1 
ATOM   2046 O  OE1 . GLN A 1 310 ? 23.964  -20.180 -0.253  1.00   55.11  ? 325 GLN A OE1 1 
ATOM   2047 N  NE2 . GLN A 1 310 ? 23.325  -20.397 -2.422  1.00   56.75  ? 325 GLN A NE2 1 
ATOM   2048 N  N   . GLU A 1 311 ? 28.514  -19.469 -3.725  1.00   58.79  ? 326 GLU A N   1 
ATOM   2049 C  CA  . GLU A 1 311 ? 29.833  -19.988 -3.308  1.00   59.38  ? 326 GLU A CA  1 
ATOM   2050 C  C   . GLU A 1 311 ? 30.909  -18.927 -3.477  1.00   57.66  ? 326 GLU A C   1 
ATOM   2051 O  O   . GLU A 1 311 ? 31.778  -18.785 -2.622  1.00   55.97  ? 326 GLU A O   1 
ATOM   2052 C  CB  . GLU A 1 311 ? 30.214  -21.273 -4.072  1.00   62.35  ? 326 GLU A CB  1 
ATOM   2053 C  CG  . GLU A 1 311 ? 29.696  -22.571 -3.438  1.00   65.50  ? 326 GLU A CG  1 
ATOM   2054 C  CD  . GLU A 1 311 ? 29.702  -23.780 -4.396  1.00   70.50  ? 326 GLU A CD  1 
ATOM   2055 O  OE1 . GLU A 1 311 ? 30.762  -24.448 -4.531  1.00   73.08  ? 326 GLU A OE1 1 
ATOM   2056 O  OE2 . GLU A 1 311 ? 28.636  -24.090 -5.006  1.00   71.90  ? 326 GLU A OE2 1 
ATOM   2057 N  N   . ARG A 1 312 ? 30.850  -18.155 -4.556  1.00   56.31  ? 327 ARG A N   1 
ATOM   2058 C  CA  . ARG A 1 312 ? 31.866  -17.122 -4.750  1.00   57.11  ? 327 ARG A CA  1 
ATOM   2059 C  C   . ARG A 1 312 ? 31.839  -15.994 -3.723  1.00   56.31  ? 327 ARG A C   1 
ATOM   2060 O  O   . ARG A 1 312 ? 32.885  -15.502 -3.311  1.00   56.04  ? 327 ARG A O   1 
ATOM   2061 C  CB  . ARG A 1 312 ? 31.798  -16.574 -6.152  1.00   57.09  ? 327 ARG A CB  1 
ATOM   2062 C  CG  . ARG A 1 312 ? 32.295  -17.598 -7.146  1.00   59.54  ? 327 ARG A CG  1 
ATOM   2063 C  CD  . ARG A 1 312 ? 32.011  -17.140 -8.553  1.00   61.57  ? 327 ARG A CD  1 
ATOM   2064 N  NE  . ARG A 1 312 ? 32.601  -15.827 -8.794  1.00   62.09  ? 327 ARG A NE  1 
ATOM   2065 C  CZ  . ARG A 1 312 ? 32.076  -14.893 -9.585  1.00   63.08  ? 327 ARG A CZ  1 
ATOM   2066 N  NH1 . ARG A 1 312 ? 30.917  -15.105 -10.230 1.00   62.52  ? 327 ARG A NH1 1 
ATOM   2067 N  NH2 . ARG A 1 312 ? 32.714  -13.734 -9.730  1.00   62.58  ? 327 ARG A NH2 1 
ATOM   2068 N  N   . VAL A 1 313 ? 30.639  -15.591 -3.323  1.00   55.95  ? 328 VAL A N   1 
ATOM   2069 C  CA  . VAL A 1 313 ? 30.452  -14.600 -2.258  1.00   53.83  ? 328 VAL A CA  1 
ATOM   2070 C  C   . VAL A 1 313 ? 30.842  -15.201 -0.914  1.00   53.82  ? 328 VAL A C   1 
ATOM   2071 O  O   . VAL A 1 313 ? 31.344  -14.509 -0.045  1.00   54.04  ? 328 VAL A O   1 
ATOM   2072 C  CB  . VAL A 1 313 ? 28.982  -14.131 -2.194  1.00   51.80  ? 328 VAL A CB  1 
ATOM   2073 C  CG1 . VAL A 1 313 ? 28.728  -13.258 -0.969  1.00   50.70  ? 328 VAL A CG1 1 
ATOM   2074 C  CG2 . VAL A 1 313 ? 28.613  -13.376 -3.461  1.00   50.89  ? 328 VAL A CG2 1 
ATOM   2075 N  N   . GLN A 1 314 ? 30.562  -16.485 -0.735  1.00   54.60  ? 329 GLN A N   1 
ATOM   2076 C  CA  . GLN A 1 314 ? 30.927  -17.170 0.498   1.00   55.04  ? 329 GLN A CA  1 
ATOM   2077 C  C   . GLN A 1 314 ? 32.450  -17.275 0.630   1.00   55.40  ? 329 GLN A C   1 
ATOM   2078 O  O   . GLN A 1 314 ? 32.964  -17.296 1.742   1.00   55.34  ? 329 GLN A O   1 
ATOM   2079 C  CB  . GLN A 1 314 ? 30.291  -18.561 0.567   1.00   55.67  ? 329 GLN A CB  1 
ATOM   2080 C  CG  . GLN A 1 314 ? 28.856  -18.564 1.047   1.00   54.71  ? 329 GLN A CG  1 
ATOM   2081 C  CD  . GLN A 1 314 ? 28.080  -19.796 0.606   1.00   56.56  ? 329 GLN A CD  1 
ATOM   2082 O  OE1 . GLN A 1 314 ? 28.514  -20.567 -0.255  1.00   57.70  ? 329 GLN A OE1 1 
ATOM   2083 N  NE2 . GLN A 1 314 ? 26.912  -19.981 1.192   1.00   57.22  ? 329 GLN A NE2 1 
ATOM   2084 N  N   . ALA A 1 315 ? 33.162  -17.337 -0.500  1.00   56.40  ? 330 ALA A N   1 
ATOM   2085 C  CA  . ALA A 1 315 ? 34.638  -17.362 -0.495  1.00   56.38  ? 330 ALA A CA  1 
ATOM   2086 C  C   . ALA A 1 315 ? 35.133  -15.998 -0.100  1.00   55.68  ? 330 ALA A C   1 
ATOM   2087 O  O   . ALA A 1 315 ? 36.086  -15.871 0.669   1.00   56.84  ? 330 ALA A O   1 
ATOM   2088 C  CB  . ALA A 1 315 ? 35.196  -17.748 -1.856  1.00   56.35  ? 330 ALA A CB  1 
ATOM   2089 N  N   . GLU A 1 316 ? 34.458  -14.976 -0.611  1.00   54.50  ? 331 GLU A N   1 
ATOM   2090 C  CA  . GLU A 1 316 ? 34.855  -13.614 -0.348  1.00   54.19  ? 331 GLU A CA  1 
ATOM   2091 C  C   . GLU A 1 316 ? 34.816  -13.380 1.153   1.00   54.04  ? 331 GLU A C   1 
ATOM   2092 O  O   . GLU A 1 316 ? 35.761  -12.866 1.729   1.00   54.65  ? 331 GLU A O   1 
ATOM   2093 C  CB  . GLU A 1 316 ? 33.971  -12.622 -1.099  1.00   52.98  ? 331 GLU A CB  1 
ATOM   2094 C  CG  . GLU A 1 316 ? 34.602  -11.253 -1.258  1.00   54.10  ? 331 GLU A CG  1 
ATOM   2095 C  CD  . GLU A 1 316 ? 33.768  -10.289 -2.099  1.00   55.58  ? 331 GLU A CD  1 
ATOM   2096 O  OE1 . GLU A 1 316 ? 32.589  -9.997  -1.744  1.00   56.60  ? 331 GLU A OE1 1 
ATOM   2097 O  OE2 . GLU A 1 316 ? 34.308  -9.793  -3.108  1.00   56.05  ? 331 GLU A OE2 1 
ATOM   2098 N  N   . LEU A 1 317 ? 33.724  -13.797 1.778   1.00   53.37  ? 332 LEU A N   1 
ATOM   2099 C  CA  . LEU A 1 317 ? 33.527  -13.617 3.206   1.00   52.24  ? 332 LEU A CA  1 
ATOM   2100 C  C   . LEU A 1 317 ? 34.582  -14.347 4.044   1.00   53.57  ? 332 LEU A C   1 
ATOM   2101 O  O   . LEU A 1 317 ? 35.075  -13.809 5.016   1.00   52.79  ? 332 LEU A O   1 
ATOM   2102 C  CB  . LEU A 1 317 ? 32.141  -14.112 3.582   1.00   50.16  ? 332 LEU A CB  1 
ATOM   2103 C  CG  . LEU A 1 317 ? 31.065  -13.113 3.230   1.00   49.06  ? 332 LEU A CG  1 
ATOM   2104 C  CD1 . LEU A 1 317 ? 29.705  -13.796 3.228   1.00   48.32  ? 332 LEU A CD1 1 
ATOM   2105 C  CD2 . LEU A 1 317 ? 31.100  -11.945 4.208   1.00   48.14  ? 332 LEU A CD2 1 
ATOM   2106 N  N   . ASP A 1 318 ? 34.904  -15.568 3.639   1.00   55.10  ? 333 ASP A N   1 
ATOM   2107 C  CA  . ASP A 1 318 ? 35.869  -16.419 4.325   1.00   57.48  ? 333 ASP A CA  1 
ATOM   2108 C  C   . ASP A 1 318 ? 37.286  -15.845 4.306   1.00   60.31  ? 333 ASP A C   1 
ATOM   2109 O  O   . ASP A 1 318 ? 37.963  -15.870 5.332   1.00   64.16  ? 333 ASP A O   1 
ATOM   2110 C  CB  . ASP A 1 318 ? 35.889  -17.818 3.691   1.00   57.82  ? 333 ASP A CB  1 
ATOM   2111 C  CG  . ASP A 1 318 ? 34.550  -18.542 3.808   1.00   56.52  ? 333 ASP A CG  1 
ATOM   2112 O  OD1 . ASP A 1 318 ? 33.738  -18.136 4.653   1.00   55.21  ? 333 ASP A OD1 1 
ATOM   2113 O  OD2 . ASP A 1 318 ? 34.303  -19.502 3.041   1.00   56.01  ? 333 ASP A OD2 1 
ATOM   2114 N  N   . GLU A 1 319 ? 37.728  -15.347 3.152   1.00   60.90  ? 334 GLU A N   1 
ATOM   2115 C  CA  . GLU A 1 319 ? 39.043  -14.741 3.015   1.00   62.83  ? 334 GLU A CA  1 
ATOM   2116 C  C   . GLU A 1 319 ? 39.111  -13.476 3.838   1.00   63.11  ? 334 GLU A C   1 
ATOM   2117 O  O   . GLU A 1 319 ? 40.016  -13.302 4.680   1.00   67.74  ? 334 GLU A O   1 
ATOM   2118 C  CB  . GLU A 1 319 ? 39.353  -14.401 1.550   1.00   64.63  ? 334 GLU A CB  1 
ATOM   2119 C  CG  . GLU A 1 319 ? 39.327  -15.588 0.582   1.00   66.25  ? 334 GLU A CG  1 
ATOM   2120 C  CD  . GLU A 1 319 ? 38.825  -15.227 -0.817  1.00   67.52  ? 334 GLU A CD  1 
ATOM   2121 O  OE1 . GLU A 1 319 ? 38.153  -14.176 -0.979  1.00   66.52  ? 334 GLU A OE1 1 
ATOM   2122 O  OE2 . GLU A 1 319 ? 39.096  -16.003 -1.760  1.00   67.80  ? 334 GLU A OE2 1 
ATOM   2123 N  N   . CYS A 1 320 ? 38.137  -12.607 3.610   1.00   61.72  ? 335 CYS A N   1 
ATOM   2124 C  CA  . CYS A 1 320 ? 38.137  -11.261 4.166   1.00   63.58  ? 335 CYS A CA  1 
ATOM   2125 C  C   . CYS A 1 320 ? 37.692  -11.228 5.623   1.00   61.38  ? 335 CYS A C   1 
ATOM   2126 O  O   . CYS A 1 320 ? 38.368  -10.669 6.471   1.00   61.39  ? 335 CYS A O   1 
ATOM   2127 C  CB  . CYS A 1 320 ? 37.262  -10.350 3.307   1.00   65.63  ? 335 CYS A CB  1 
ATOM   2128 S  SG  . CYS A 1 320 ? 37.497  -10.641 1.521   1.00   74.72  ? 335 CYS A SG  1 
ATOM   2129 N  N   . VAL A 1 321 ? 36.561  -11.838 5.918   1.00   61.30  ? 336 VAL A N   1 
ATOM   2130 C  CA  . VAL A 1 321 ? 36.085  -11.925 7.295   1.00   62.11  ? 336 VAL A CA  1 
ATOM   2131 C  C   . VAL A 1 321 ? 36.514  -13.268 7.839   1.00   64.39  ? 336 VAL A C   1 
ATOM   2132 O  O   . VAL A 1 321 ? 36.873  -14.173 7.080   1.00   64.61  ? 336 VAL A O   1 
ATOM   2133 C  CB  . VAL A 1 321 ? 34.547  -11.834 7.372   1.00   60.74  ? 336 VAL A CB  1 
ATOM   2134 C  CG1 . VAL A 1 321 ? 34.089  -11.662 8.810   1.00   60.57  ? 336 VAL A CG1 1 
ATOM   2135 C  CG2 . VAL A 1 321 ? 34.038  -10.691 6.509   1.00   60.04  ? 336 VAL A CG2 1 
ATOM   2136 N  N   . GLY A 1 322 ? 36.482  -13.423 9.150   1.00   66.47  ? 337 GLY A N   1 
ATOM   2137 C  CA  . GLY A 1 322 ? 36.698  -14.747 9.717   1.00   70.44  ? 337 GLY A CA  1 
ATOM   2138 C  C   . GLY A 1 322 ? 35.599  -15.695 9.260   1.00   70.81  ? 337 GLY A C   1 
ATOM   2139 O  O   . GLY A 1 322 ? 34.814  -15.380 8.379   1.00   65.78  ? 337 GLY A O   1 
ATOM   2140 N  N   . VAL A 1 323 ? 35.579  -16.882 9.839   1.00   75.23  ? 338 VAL A N   1 
ATOM   2141 C  CA  . VAL A 1 323 ? 34.371  -17.672 9.873   1.00   76.76  ? 338 VAL A CA  1 
ATOM   2142 C  C   . VAL A 1 323 ? 33.692  -17.487 11.242  1.00   77.90  ? 338 VAL A C   1 
ATOM   2143 O  O   . VAL A 1 323 ? 32.531  -17.864 11.397  1.00   82.23  ? 338 VAL A O   1 
ATOM   2144 C  CB  . VAL A 1 323 ? 34.643  -19.158 9.542   1.00   78.91  ? 338 VAL A CB  1 
ATOM   2145 C  CG1 . VAL A 1 323 ? 35.161  -19.919 10.761  1.00   80.33  ? 338 VAL A CG1 1 
ATOM   2146 C  CG2 . VAL A 1 323 ? 33.386  -19.815 8.974   1.00   79.84  ? 338 VAL A CG2 1 
ATOM   2147 N  N   . ASP A 1 324 ? 34.388  -16.881 12.214  1.00   76.95  ? 339 ASP A N   1 
ATOM   2148 C  CA  . ASP A 1 324 ? 33.777  -16.557 13.516  1.00   77.84  ? 339 ASP A CA  1 
ATOM   2149 C  C   . ASP A 1 324 ? 33.274  -15.100 13.615  1.00   76.89  ? 339 ASP A C   1 
ATOM   2150 O  O   . ASP A 1 324 ? 32.073  -14.870 13.836  1.00   78.89  ? 339 ASP A O   1 
ATOM   2151 C  CB  . ASP A 1 324 ? 34.691  -16.924 14.695  1.00   80.96  ? 339 ASP A CB  1 
ATOM   2152 C  CG  . ASP A 1 324 ? 36.150  -16.503 14.488  1.00   86.70  ? 339 ASP A CG  1 
ATOM   2153 O  OD1 . ASP A 1 324 ? 36.488  -16.022 13.379  1.00   89.37  ? 339 ASP A OD1 1 
ATOM   2154 O  OD2 . ASP A 1 324 ? 36.962  -16.660 15.439  1.00   84.07  ? 339 ASP A OD2 1 
ATOM   2155 N  N   . ARG A 1 325 ? 34.160  -14.125 13.421  1.00   73.63  ? 340 ARG A N   1 
ATOM   2156 C  CA  . ARG A 1 325 ? 33.803  -12.704 13.543  1.00   69.66  ? 340 ARG A CA  1 
ATOM   2157 C  C   . ARG A 1 325 ? 32.507  -12.420 12.803  1.00   69.24  ? 340 ARG A C   1 
ATOM   2158 O  O   . ARG A 1 325 ? 32.244  -13.036 11.779  1.00   72.47  ? 340 ARG A O   1 
ATOM   2159 C  CB  . ARG A 1 325 ? 34.915  -11.827 12.951  1.00   68.50  ? 340 ARG A CB  1 
ATOM   2160 C  CG  . ARG A 1 325 ? 34.825  -10.342 13.290  1.00   67.27  ? 340 ARG A CG  1 
ATOM   2161 C  CD  . ARG A 1 325 ? 36.109  -9.577  12.929  1.00   66.17  ? 340 ARG A CD  1 
ATOM   2162 N  NE  . ARG A 1 325 ? 36.504  -9.690  11.513  1.00   64.79  ? 340 ARG A NE  1 
ATOM   2163 C  CZ  . ARG A 1 325 ? 35.998  -8.972  10.497  1.00   61.99  ? 340 ARG A CZ  1 
ATOM   2164 N  NH1 . ARG A 1 325 ? 35.036  -8.068  10.691  1.00   60.62  ? 340 ARG A NH1 1 
ATOM   2165 N  NH2 . ARG A 1 325 ? 36.442  -9.180  9.261   1.00   59.63  ? 340 ARG A NH2 1 
ATOM   2166 N  N   . PRO A 1 326 ? 31.679  -11.497 13.319  1.00   67.26  ? 341 PRO A N   1 
ATOM   2167 C  CA  . PRO A 1 326 ? 30.572  -11.012 12.510  1.00   61.91  ? 341 PRO A CA  1 
ATOM   2168 C  C   . PRO A 1 326 ? 31.064  -9.938  11.537  1.00   60.95  ? 341 PRO A C   1 
ATOM   2169 O  O   . PRO A 1 326 ? 31.912  -9.129  11.907  1.00   63.59  ? 341 PRO A O   1 
ATOM   2170 C  CB  . PRO A 1 326 ? 29.640  -10.412 13.542  1.00   61.79  ? 341 PRO A CB  1 
ATOM   2171 C  CG  . PRO A 1 326 ? 30.523  -9.938  14.628  1.00   64.11  ? 341 PRO A CG  1 
ATOM   2172 C  CD  . PRO A 1 326 ? 31.719  -10.849 14.643  1.00   67.49  ? 341 PRO A CD  1 
ATOM   2173 N  N   . PRO A 1 327 ? 30.568  -9.937  10.289  1.00   59.33  ? 342 PRO A N   1 
ATOM   2174 C  CA  . PRO A 1 327 ? 30.990  -8.880  9.390   1.00   58.65  ? 342 PRO A CA  1 
ATOM   2175 C  C   . PRO A 1 327 ? 30.403  -7.548  9.818   1.00   59.00  ? 342 PRO A C   1 
ATOM   2176 O  O   . PRO A 1 327 ? 29.248  -7.493  10.266  1.00   60.71  ? 342 PRO A O   1 
ATOM   2177 C  CB  . PRO A 1 327 ? 30.429  -9.316  8.035   1.00   58.34  ? 342 PRO A CB  1 
ATOM   2178 C  CG  . PRO A 1 327 ? 30.218  -10.774 8.146   1.00   58.57  ? 342 PRO A CG  1 
ATOM   2179 C  CD  . PRO A 1 327 ? 29.833  -10.993 9.575   1.00   59.70  ? 342 PRO A CD  1 
ATOM   2180 N  N   . CYS A 1 328 ? 31.196  -6.487  9.672   1.00   58.52  ? 343 CYS A N   1 
ATOM   2181 C  CA  . CYS A 1 328 ? 30.807  -5.157  10.127  1.00   57.61  ? 343 CYS A CA  1 
ATOM   2182 C  C   . CYS A 1 328 ? 31.072  -4.199  8.999   1.00   54.63  ? 343 CYS A C   1 
ATOM   2183 O  O   . CYS A 1 328 ? 31.651  -4.584  7.993   1.00   51.86  ? 343 CYS A O   1 
ATOM   2184 C  CB  . CYS A 1 328 ? 31.626  -4.778  11.350  1.00   60.00  ? 343 CYS A CB  1 
ATOM   2185 S  SG  . CYS A 1 328 ? 33.364  -5.030  11.036  1.00   63.56  ? 343 CYS A SG  1 
ATOM   2186 N  N   . LEU A 1 329 ? 30.649  -2.953  9.153   1.00   53.81  ? 344 LEU A N   1 
ATOM   2187 C  CA  . LEU A 1 329 ? 30.630  -2.055  8.010   1.00   54.01  ? 344 LEU A CA  1 
ATOM   2188 C  C   . LEU A 1 329 ? 32.032  -1.807  7.444   1.00   54.25  ? 344 LEU A C   1 
ATOM   2189 O  O   . LEU A 1 329 ? 32.202  -1.665  6.244   1.00   51.57  ? 344 LEU A O   1 
ATOM   2190 C  CB  . LEU A 1 329 ? 29.903  -0.754  8.340   1.00   53.39  ? 344 LEU A CB  1 
ATOM   2191 C  CG  . LEU A 1 329 ? 28.447  -0.898  8.808   1.00   53.08  ? 344 LEU A CG  1 
ATOM   2192 C  CD1 . LEU A 1 329 ? 27.880  0.459   9.220   1.00   52.75  ? 344 LEU A CD1 1 
ATOM   2193 C  CD2 . LEU A 1 329 ? 27.536  -1.523  7.757   1.00   53.17  ? 344 LEU A CD2 1 
ATOM   2194 N  N   . SER A 1 330 ? 33.052  -1.798  8.288   1.00   57.27  ? 345 SER A N   1 
ATOM   2195 C  CA  . SER A 1 330 ? 34.415  -1.544  7.783   1.00   59.20  ? 345 SER A CA  1 
ATOM   2196 C  C   . SER A 1 330 ? 34.899  -2.585  6.745   1.00   59.53  ? 345 SER A C   1 
ATOM   2197 O  O   . SER A 1 330 ? 35.824  -2.299  5.963   1.00   61.36  ? 345 SER A O   1 
ATOM   2198 C  CB  . SER A 1 330 ? 35.413  -1.450  8.924   1.00   59.30  ? 345 SER A CB  1 
ATOM   2199 O  OG  . SER A 1 330 ? 35.679  -2.738  9.455   1.00   62.86  ? 345 SER A OG  1 
ATOM   2200 N  N   . ASP A 1 331 ? 34.280  -3.770  6.731   1.00   57.04  ? 346 ASP A N   1 
ATOM   2201 C  CA  . ASP A 1 331 ? 34.616  -4.809  5.752   1.00   56.11  ? 346 ASP A CA  1 
ATOM   2202 C  C   . ASP A 1 331 ? 34.089  -4.491  4.363   1.00   57.96  ? 346 ASP A C   1 
ATOM   2203 O  O   . ASP A 1 331 ? 34.570  -5.080  3.390   1.00   59.15  ? 346 ASP A O   1 
ATOM   2204 C  CB  . ASP A 1 331 ? 34.051  -6.169  6.165   1.00   55.25  ? 346 ASP A CB  1 
ATOM   2205 C  CG  . ASP A 1 331 ? 34.545  -6.638  7.526   1.00   54.86  ? 346 ASP A CG  1 
ATOM   2206 O  OD1 . ASP A 1 331 ? 35.775  -6.729  7.687   1.00   58.36  ? 346 ASP A OD1 1 
ATOM   2207 O  OD2 . ASP A 1 331 ? 33.714  -6.949  8.417   1.00   51.68  ? 346 ASP A OD2 1 
ATOM   2208 N  N   . ARG A 1 332 ? 33.106  -3.579  4.276   1.00   59.03  ? 347 ARG A N   1 
ATOM   2209 C  CA  . ARG A 1 332 ? 32.418  -3.242  3.016   1.00   59.63  ? 347 ARG A CA  1 
ATOM   2210 C  C   . ARG A 1 332 ? 33.330  -3.072  1.801   1.00   59.36  ? 347 ARG A C   1 
ATOM   2211 O  O   . ARG A 1 332 ? 33.131  -3.749  0.798   1.00   59.18  ? 347 ARG A O   1 
ATOM   2212 C  CB  . ARG A 1 332 ? 31.506  -2.016  3.184   1.00   62.61  ? 347 ARG A CB  1 
ATOM   2213 C  CG  . ARG A 1 332 ? 30.218  -2.323  3.947   1.00   65.54  ? 347 ARG A CG  1 
ATOM   2214 C  CD  . ARG A 1 332 ? 29.227  -1.163  3.970   1.00   67.15  ? 347 ARG A CD  1 
ATOM   2215 N  NE  . ARG A 1 332 ? 28.308  -1.269  2.837   1.00   71.54  ? 347 ARG A NE  1 
ATOM   2216 C  CZ  . ARG A 1 332 ? 27.052  -0.811  2.794   1.00   70.72  ? 347 ARG A CZ  1 
ATOM   2217 N  NH1 . ARG A 1 332 ? 26.514  -0.177  3.838   1.00   69.00  ? 347 ARG A NH1 1 
ATOM   2218 N  NH2 . ARG A 1 332 ? 26.335  -0.990  1.677   1.00   67.80  ? 347 ARG A NH2 1 
ATOM   2219 N  N   . PRO A 1 333 ? 34.339  -2.181  1.889   1.00   59.72  ? 348 PRO A N   1 
ATOM   2220 C  CA  . PRO A 1 333 ? 35.304  -1.997  0.792   1.00   60.18  ? 348 PRO A CA  1 
ATOM   2221 C  C   . PRO A 1 333 ? 36.006  -3.291  0.374   1.00   59.85  ? 348 PRO A C   1 
ATOM   2222 O  O   . PRO A 1 333 ? 36.312  -3.467  -0.813  1.00   60.33  ? 348 PRO A O   1 
ATOM   2223 C  CB  . PRO A 1 333 ? 36.331  -1.029  1.382   1.00   60.83  ? 348 PRO A CB  1 
ATOM   2224 C  CG  . PRO A 1 333 ? 35.617  -0.338  2.478   1.00   60.78  ? 348 PRO A CG  1 
ATOM   2225 C  CD  . PRO A 1 333 ? 34.685  -1.347  3.051   1.00   59.71  ? 348 PRO A CD  1 
ATOM   2226 N  N   . HIS A 1 334 ? 36.227  -4.184  1.340   1.00   56.24  ? 349 HIS A N   1 
ATOM   2227 C  CA  . HIS A 1 334 ? 36.846  -5.473  1.091   1.00   55.92  ? 349 HIS A CA  1 
ATOM   2228 C  C   . HIS A 1 334 ? 35.919  -6.601  0.658   1.00   54.01  ? 349 HIS A C   1 
ATOM   2229 O  O   . HIS A 1 334 ? 36.366  -7.741  0.556   1.00   52.10  ? 349 HIS A O   1 
ATOM   2230 C  CB  . HIS A 1 334 ? 37.617  -5.870  2.339   1.00   59.10  ? 349 HIS A CB  1 
ATOM   2231 C  CG  . HIS A 1 334 ? 38.606  -4.828  2.743   1.00   61.57  ? 349 HIS A CG  1 
ATOM   2232 N  ND1 . HIS A 1 334 ? 39.677  -4.492  1.943   1.00   63.00  ? 349 HIS A ND1 1 
ATOM   2233 C  CD2 . HIS A 1 334 ? 38.640  -3.984  3.801   1.00   62.21  ? 349 HIS A CD2 1 
ATOM   2234 C  CE1 . HIS A 1 334 ? 40.346  -3.508  2.507   1.00   64.52  ? 349 HIS A CE1 1 
ATOM   2235 N  NE2 . HIS A 1 334 ? 39.748  -3.188  3.641   1.00   64.55  ? 349 HIS A NE2 1 
ATOM   2236 N  N   . LEU A 1 335 ? 34.651  -6.282  0.363   1.00   53.09  ? 350 LEU A N   1 
ATOM   2237 C  CA  . LEU A 1 335 ? 33.676  -7.274  -0.127  1.00   52.50  ? 350 LEU A CA  1 
ATOM   2238 C  C   . LEU A 1 335 ? 32.995  -6.853  -1.459  1.00   50.75  ? 350 LEU A C   1 
ATOM   2239 O  O   . LEU A 1 335 ? 31.783  -6.729  -1.534  1.00   48.84  ? 350 LEU A O   1 
ATOM   2240 C  CB  . LEU A 1 335 ? 32.659  -7.584  0.988   1.00   52.80  ? 350 LEU A CB  1 
ATOM   2241 C  CG  . LEU A 1 335 ? 33.263  -8.099  2.333   1.00   53.40  ? 350 LEU A CG  1 
ATOM   2242 C  CD1 . LEU A 1 335 ? 32.196  -8.360  3.401   1.00   52.06  ? 350 LEU A CD1 1 
ATOM   2243 C  CD2 . LEU A 1 335 ? 34.116  -9.355  2.147   1.00   54.31  ? 350 LEU A CD2 1 
ATOM   2244 N  N   . PRO A 1 336 ? 33.797  -6.675  -2.528  1.00   51.27  ? 351 PRO A N   1 
ATOM   2245 C  CA  . PRO A 1 336 ? 33.354  -6.051  -3.778  1.00   50.28  ? 351 PRO A CA  1 
ATOM   2246 C  C   . PRO A 1 336 ? 32.252  -6.808  -4.516  1.00   50.50  ? 351 PRO A C   1 
ATOM   2247 O  O   . PRO A 1 336 ? 31.359  -6.197  -5.134  1.00   49.31  ? 351 PRO A O   1 
ATOM   2248 C  CB  . PRO A 1 336 ? 34.629  -6.034  -4.632  1.00   51.91  ? 351 PRO A CB  1 
ATOM   2249 C  CG  . PRO A 1 336 ? 35.554  -7.023  -4.012  1.00   52.50  ? 351 PRO A CG  1 
ATOM   2250 C  CD  . PRO A 1 336 ? 35.235  -7.018  -2.566  1.00   51.99  ? 351 PRO A CD  1 
ATOM   2251 N  N   . LEU A 1 337 ? 32.329  -8.130  -4.469  1.00   50.25  ? 352 LEU A N   1 
ATOM   2252 C  CA  . LEU A 1 337 ? 31.353  -8.963  -5.136  1.00   49.72  ? 352 LEU A CA  1 
ATOM   2253 C  C   . LEU A 1 337 ? 30.008  -8.813  -4.430  1.00   48.34  ? 352 LEU A C   1 
ATOM   2254 O  O   . LEU A 1 337 ? 29.029  -8.385  -5.025  1.00   47.81  ? 352 LEU A O   1 
ATOM   2255 C  CB  . LEU A 1 337 ? 31.827  -10.429 -5.148  1.00   50.56  ? 352 LEU A CB  1 
ATOM   2256 C  CG  . LEU A 1 337 ? 31.030  -11.424 -6.010  1.00   50.37  ? 352 LEU A CG  1 
ATOM   2257 C  CD1 . LEU A 1 337 ? 31.113  -11.064 -7.491  1.00   51.37  ? 352 LEU A CD1 1 
ATOM   2258 C  CD2 . LEU A 1 337 ? 31.506  -12.852 -5.777  1.00   50.84  ? 352 LEU A CD2 1 
ATOM   2259 N  N   . LEU A 1 338 ? 29.977  -9.131  -3.143  1.00   48.10  ? 353 LEU A N   1 
ATOM   2260 C  CA  . LEU A 1 338 ? 28.767  -8.940  -2.351  1.00   46.84  ? 353 LEU A CA  1 
ATOM   2261 C  C   . LEU A 1 338 ? 28.069  -7.645  -2.731  1.00   44.93  ? 353 LEU A C   1 
ATOM   2262 O  O   . LEU A 1 338 ? 26.886  -7.648  -2.998  1.00   43.11  ? 353 LEU A O   1 
ATOM   2263 C  CB  . LEU A 1 338 ? 29.073  -8.936  -0.846  1.00   45.88  ? 353 LEU A CB  1 
ATOM   2264 C  CG  . LEU A 1 338 ? 27.890  -8.691  0.081   1.00   44.81  ? 353 LEU A CG  1 
ATOM   2265 C  CD1 . LEU A 1 338 ? 26.664  -9.471  -0.366  1.00   46.52  ? 353 LEU A CD1 1 
ATOM   2266 C  CD2 . LEU A 1 338 ? 28.226  -9.108  1.488   1.00   45.34  ? 353 LEU A CD2 1 
ATOM   2267 N  N   . ASP A 1 339 ? 28.807  -6.544  -2.769  1.00   45.18  ? 354 ASP A N   1 
ATOM   2268 C  CA  . ASP A 1 339 ? 28.183  -5.269  -3.072  1.00   45.07  ? 354 ASP A CA  1 
ATOM   2269 C  C   . ASP A 1 339 ? 27.571  -5.259  -4.472  1.00   44.55  ? 354 ASP A C   1 
ATOM   2270 O  O   . ASP A 1 339 ? 26.514  -4.658  -4.712  1.00   43.09  ? 354 ASP A O   1 
ATOM   2271 C  CB  . ASP A 1 339 ? 29.162  -4.117  -2.953  1.00   45.60  ? 354 ASP A CB  1 
ATOM   2272 C  CG  . ASP A 1 339 ? 28.451  -2.799  -2.942  1.00   46.32  ? 354 ASP A CG  1 
ATOM   2273 O  OD1 . ASP A 1 339 ? 27.807  -2.487  -1.902  1.00   47.67  ? 354 ASP A OD1 1 
ATOM   2274 O  OD2 . ASP A 1 339 ? 28.470  -2.116  -3.987  1.00   47.17  ? 354 ASP A OD2 1 
ATOM   2275 N  N   . ALA A 1 340 ? 28.266  -5.921  -5.386  1.00   44.26  ? 355 ALA A N   1 
ATOM   2276 C  CA  . ALA A 1 340 ? 27.784  -6.086  -6.717  1.00   43.37  ? 355 ALA A CA  1 
ATOM   2277 C  C   . ALA A 1 340 ? 26.468  -6.868  -6.699  1.00   42.73  ? 355 ALA A C   1 
ATOM   2278 O  O   . ALA A 1 340 ? 25.489  -6.489  -7.340  1.00   43.24  ? 355 ALA A O   1 
ATOM   2279 C  CB  . ALA A 1 340 ? 28.830  -6.793  -7.556  1.00   44.65  ? 355 ALA A CB  1 
ATOM   2280 N  N   . VAL A 1 341 ? 26.441  -7.957  -5.955  1.00   42.14  ? 356 VAL A N   1 
ATOM   2281 C  CA  . VAL A 1 341 ? 25.266  -8.803  -5.893  1.00   41.26  ? 356 VAL A CA  1 
ATOM   2282 C  C   . VAL A 1 341 ? 24.095  -7.938  -5.471  1.00   40.76  ? 356 VAL A C   1 
ATOM   2283 O  O   . VAL A 1 341 ? 23.070  -7.904  -6.137  1.00   40.51  ? 356 VAL A O   1 
ATOM   2284 C  CB  . VAL A 1 341 ? 25.479  -9.970  -4.908  1.00   41.07  ? 356 VAL A CB  1 
ATOM   2285 C  CG1 . VAL A 1 341 ? 24.186  -10.694 -4.607  1.00   40.56  ? 356 VAL A CG1 1 
ATOM   2286 C  CG2 . VAL A 1 341 ? 26.493  -10.947 -5.479  1.00   42.80  ? 356 VAL A CG2 1 
ATOM   2287 N  N   . LEU A 1 342 ? 24.280  -7.211  -4.379  1.00   40.76  ? 357 LEU A N   1 
ATOM   2288 C  CA  . LEU A 1 342 ? 23.261  -6.339  -3.833  1.00   39.99  ? 357 LEU A CA  1 
ATOM   2289 C  C   . LEU A 1 342 ? 22.794  -5.296  -4.849  1.00   39.68  ? 357 LEU A C   1 
ATOM   2290 O  O   . LEU A 1 342 ? 21.603  -5.013  -4.981  1.00   38.29  ? 357 LEU A O   1 
ATOM   2291 C  CB  . LEU A 1 342 ? 23.818  -5.651  -2.596  1.00   40.22  ? 357 LEU A CB  1 
ATOM   2292 C  CG  . LEU A 1 342 ? 24.042  -6.595  -1.417  1.00   41.12  ? 357 LEU A CG  1 
ATOM   2293 C  CD1 . LEU A 1 342 ? 24.594  -5.873  -0.189  1.00   41.05  ? 357 LEU A CD1 1 
ATOM   2294 C  CD2 . LEU A 1 342 ? 22.723  -7.261  -1.056  1.00   41.17  ? 357 LEU A CD2 1 
ATOM   2295 N  N   . CYS A 1 343 ? 23.739  -4.718  -5.579  1.00   40.47  ? 358 CYS A N   1 
ATOM   2296 C  CA  . CYS A 1 343 ? 23.380  -3.703  -6.555  1.00   39.99  ? 358 CYS A CA  1 
ATOM   2297 C  C   . CYS A 1 343 ? 22.579  -4.355  -7.665  1.00   40.57  ? 358 CYS A C   1 
ATOM   2298 O  O   . CYS A 1 343 ? 21.674  -3.772  -8.208  1.00   40.33  ? 358 CYS A O   1 
ATOM   2299 C  CB  . CYS A 1 343 ? 24.619  -3.021  -7.106  1.00   40.21  ? 358 CYS A CB  1 
ATOM   2300 S  SG  . CYS A 1 343 ? 25.376  -1.840  -5.969  1.00   40.52  ? 358 CYS A SG  1 
ATOM   2301 N  N   . GLU A 1 344 ? 22.917  -5.582  -7.993  1.00   41.45  ? 359 GLU A N   1 
ATOM   2302 C  CA  . GLU A 1 344 ? 22.297  -6.224  -9.106  1.00   42.08  ? 359 GLU A CA  1 
ATOM   2303 C  C   . GLU A 1 344 ? 20.866  -6.579  -8.783  1.00   42.22  ? 359 GLU A C   1 
ATOM   2304 O  O   . GLU A 1 344 ? 19.990  -6.356  -9.608  1.00   45.40  ? 359 GLU A O   1 
ATOM   2305 C  CB  . GLU A 1 344 ? 23.075  -7.467  -9.492  1.00   42.92  ? 359 GLU A CB  1 
ATOM   2306 C  CG  . GLU A 1 344 ? 22.488  -8.194  -10.682 1.00   43.31  ? 359 GLU A CG  1 
ATOM   2307 C  CD  . GLU A 1 344 ? 22.749  -7.495  -11.983 1.00   42.91  ? 359 GLU A CD  1 
ATOM   2308 O  OE1 . GLU A 1 344 ? 23.110  -6.295  -11.985 1.00   42.44  ? 359 GLU A OE1 1 
ATOM   2309 O  OE2 . GLU A 1 344 ? 22.587  -8.164  -13.019 1.00   42.57  ? 359 GLU A OE2 1 
ATOM   2310 N  N   . VAL A 1 345 ? 20.638  -7.147  -7.604  1.00   41.75  ? 360 VAL A N   1 
ATOM   2311 C  CA  . VAL A 1 345 ? 19.302  -7.499  -7.100  1.00   40.49  ? 360 VAL A CA  1 
ATOM   2312 C  C   . VAL A 1 345 ? 18.422  -6.267  -7.131  1.00   39.41  ? 360 VAL A C   1 
ATOM   2313 O  O   . VAL A 1 345 ? 17.282  -6.318  -7.549  1.00   41.10  ? 360 VAL A O   1 
ATOM   2314 C  CB  . VAL A 1 345 ? 19.405  -8.004  -5.634  1.00   41.25  ? 360 VAL A CB  1 
ATOM   2315 C  CG1 . VAL A 1 345 ? 18.070  -8.001  -4.898  1.00   41.02  ? 360 VAL A CG1 1 
ATOM   2316 C  CG2 . VAL A 1 345 ? 20.009  -9.395  -5.584  1.00   42.74  ? 360 VAL A CG2 1 
ATOM   2317 N  N   . MET A 1 346 ? 18.951  -5.148  -6.673  1.00   38.41  ? 361 MET A N   1 
ATOM   2318 C  CA  . MET A 1 346 ? 18.177  -3.919  -6.663  1.00   37.64  ? 361 MET A CA  1 
ATOM   2319 C  C   . MET A 1 346 ? 17.860  -3.415  -8.059  1.00   37.45  ? 361 MET A C   1 
ATOM   2320 O  O   . MET A 1 346 ? 16.818  -2.801  -8.265  1.00   39.25  ? 361 MET A O   1 
ATOM   2321 C  CB  . MET A 1 346 ? 18.902  -2.830  -5.882  1.00   37.75  ? 361 MET A CB  1 
ATOM   2322 C  CG  . MET A 1 346 ? 18.865  -2.940  -4.354  1.00   37.00  ? 361 MET A CG  1 
ATOM   2323 S  SD  . MET A 1 346 ? 19.978  -1.631  -3.798  1.00   38.55  ? 361 MET A SD  1 
ATOM   2324 C  CE  . MET A 1 346 ? 19.620  -1.460  -2.081  1.00   39.35  ? 361 MET A CE  1 
ATOM   2325 N  N   . ARG A 1 347 ? 18.757  -3.646  -9.010  1.00   38.03  ? 362 ARG A N   1 
ATOM   2326 C  CA  . ARG A 1 347 ? 18.545  -3.273  -10.404 1.00   37.68  ? 362 ARG A CA  1 
ATOM   2327 C  C   . ARG A 1 347 ? 17.494  -4.135  -11.073 1.00   38.58  ? 362 ARG A C   1 
ATOM   2328 O  O   . ARG A 1 347 ? 16.534  -3.631  -11.644 1.00   38.69  ? 362 ARG A O   1 
ATOM   2329 C  CB  . ARG A 1 347 ? 19.817  -3.441  -11.196 1.00   38.60  ? 362 ARG A CB  1 
ATOM   2330 C  CG  . ARG A 1 347 ? 19.820  -2.701  -12.518 1.00   39.16  ? 362 ARG A CG  1 
ATOM   2331 C  CD  . ARG A 1 347 ? 20.731  -3.344  -13.533 1.00   40.32  ? 362 ARG A CD  1 
ATOM   2332 N  NE  . ARG A 1 347 ? 20.023  -4.373  -14.305 1.00   41.25  ? 362 ARG A NE  1 
ATOM   2333 C  CZ  . ARG A 1 347 ? 20.346  -5.657  -14.325 1.00   42.09  ? 362 ARG A CZ  1 
ATOM   2334 N  NH1 . ARG A 1 347 ? 21.361  -6.096  -13.624 1.00   43.41  ? 362 ARG A NH1 1 
ATOM   2335 N  NH2 . ARG A 1 347 ? 19.664  -6.511  -15.042 1.00   42.79  ? 362 ARG A NH2 1 
ATOM   2336 N  N   . ILE A 1 348 ? 17.695  -5.441  -11.007 1.00   39.19  ? 363 ILE A N   1 
ATOM   2337 C  CA  . ILE A 1 348 ? 16.943  -6.378  -11.830 1.00   39.66  ? 363 ILE A CA  1 
ATOM   2338 C  C   . ILE A 1 348 ? 15.487  -6.547  -11.365 1.00   40.27  ? 363 ILE A C   1 
ATOM   2339 O  O   . ILE A 1 348 ? 14.605  -6.872  -12.186 1.00   41.84  ? 363 ILE A O   1 
ATOM   2340 C  CB  . ILE A 1 348 ? 17.632  -7.754  -11.837 1.00   39.99  ? 363 ILE A CB  1 
ATOM   2341 C  CG1 . ILE A 1 348 ? 17.114  -8.599  -13.001 1.00   40.77  ? 363 ILE A CG1 1 
ATOM   2342 C  CG2 . ILE A 1 348 ? 17.437  -8.461  -10.496 1.00   39.44  ? 363 ILE A CG2 1 
ATOM   2343 C  CD1 . ILE A 1 348 ? 17.774  -9.959  -13.142 1.00   41.97  ? 363 ILE A CD1 1 
ATOM   2344 N  N   . ARG A 1 349 ? 15.237  -6.354  -10.063 1.00   38.39  ? 364 ARG A N   1 
ATOM   2345 C  CA  . ARG A 1 349 ? 13.884  -6.415  -9.513  1.00   37.20  ? 364 ARG A CA  1 
ATOM   2346 C  C   . ARG A 1 349 ? 13.575  -5.202  -8.603  1.00   36.20  ? 364 ARG A C   1 
ATOM   2347 O  O   . ARG A 1 349 ? 13.463  -5.323  -7.371  1.00   36.04  ? 364 ARG A O   1 
ATOM   2348 C  CB  . ARG A 1 349 ? 13.690  -7.718  -8.764  1.00   37.66  ? 364 ARG A CB  1 
ATOM   2349 C  CG  . ARG A 1 349 ? 13.729  -8.936  -9.663  1.00   39.10  ? 364 ARG A CG  1 
ATOM   2350 C  CD  . ARG A 1 349 ? 12.434  -9.109  -10.444 1.00   39.79  ? 364 ARG A CD  1 
ATOM   2351 N  NE  . ARG A 1 349 ? 12.475  -10.306 -11.287 1.00   41.21  ? 364 ARG A NE  1 
ATOM   2352 C  CZ  . ARG A 1 349 ? 13.071  -10.391 -12.480 1.00   40.38  ? 364 ARG A CZ  1 
ATOM   2353 N  NH1 . ARG A 1 349 ? 13.691  -9.342  -13.006 1.00   39.87  ? 364 ARG A NH1 1 
ATOM   2354 N  NH2 . ARG A 1 349 ? 13.038  -11.538 -13.144 1.00   40.34  ? 364 ARG A NH2 1 
ATOM   2355 N  N   . PRO A 1 350 ? 13.401  -4.025  -9.218  1.00   34.78  ? 365 PRO A N   1 
ATOM   2356 C  CA  . PRO A 1 350 ? 13.133  -2.858  -8.414  1.00   33.62  ? 365 PRO A CA  1 
ATOM   2357 C  C   . PRO A 1 350 ? 11.880  -3.025  -7.607  1.00   32.98  ? 365 PRO A C   1 
ATOM   2358 O  O   . PRO A 1 350 ? 10.821  -3.276  -8.182  1.00   33.74  ? 365 PRO A O   1 
ATOM   2359 C  CB  . PRO A 1 350 ? 12.951  -1.743  -9.444  1.00   33.88  ? 365 PRO A CB  1 
ATOM   2360 C  CG  . PRO A 1 350 ? 13.198  -2.357  -10.778 1.00   34.66  ? 365 PRO A CG  1 
ATOM   2361 C  CD  . PRO A 1 350 ? 13.015  -3.818  -10.619 1.00   35.04  ? 365 PRO A CD  1 
ATOM   2362 N  N   . VAL A 1 351 ? 12.016  -2.911  -6.287  1.00   32.03  ? 366 VAL A N   1 
ATOM   2363 C  CA  . VAL A 1 351 ? 10.886  -2.977  -5.343  1.00   31.35  ? 366 VAL A CA  1 
ATOM   2364 C  C   . VAL A 1 351 ? 9.657   -2.100  -5.711  1.00   31.11  ? 366 VAL A C   1 
ATOM   2365 O  O   . VAL A 1 351 ? 8.537   -2.503  -5.469  1.00   31.88  ? 366 VAL A O   1 
ATOM   2366 C  CB  . VAL A 1 351 ? 11.331  -2.663  -3.875  1.00   30.81  ? 366 VAL A CB  1 
ATOM   2367 C  CG1 . VAL A 1 351 ? 12.123  -3.819  -3.280  1.00   31.00  ? 366 VAL A CG1 1 
ATOM   2368 C  CG2 . VAL A 1 351 ? 12.138  -1.389  -3.793  1.00   30.07  ? 366 VAL A CG2 1 
ATOM   2369 N  N   . SER A 1 352 ? 9.857   -0.909  -6.257  1.00   30.86  ? 367 SER A N   1 
ATOM   2370 C  CA  . SER A 1 352 ? 8.747   -0.113  -6.780  1.00   31.26  ? 367 SER A CA  1 
ATOM   2371 C  C   . SER A 1 352 ? 9.021   0.295   -8.200  1.00   31.22  ? 367 SER A C   1 
ATOM   2372 O  O   . SER A 1 352 ? 9.366   1.449   -8.433  1.00   30.95  ? 367 SER A O   1 
ATOM   2373 C  CB  . SER A 1 352 ? 8.472   1.121   -5.963  1.00   31.11  ? 367 SER A CB  1 
ATOM   2374 O  OG  . SER A 1 352 ? 8.296   0.674   -4.659  1.00   33.28  ? 367 SER A OG  1 
ATOM   2375 N  N   . PRO A 1 353 ? 8.780   -0.632  -9.157  1.00   31.42  ? 368 PRO A N   1 
ATOM   2376 C  CA  . PRO A 1 353 ? 9.050   -0.440  -10.580 1.00   31.64  ? 368 PRO A CA  1 
ATOM   2377 C  C   . PRO A 1 353 ? 8.417   0.821   -11.147 1.00   31.11  ? 368 PRO A C   1 
ATOM   2378 O  O   . PRO A 1 353 ? 8.805   1.287   -12.197 1.00   30.86  ? 368 PRO A O   1 
ATOM   2379 C  CB  . PRO A 1 353 ? 8.385   -1.661  -11.216 1.00   32.64  ? 368 PRO A CB  1 
ATOM   2380 C  CG  . PRO A 1 353 ? 7.335   -2.067  -10.267 1.00   32.22  ? 368 PRO A CG  1 
ATOM   2381 C  CD  . PRO A 1 353 ? 7.903   -1.801  -8.925  1.00   31.51  ? 368 PRO A CD  1 
ATOM   2382 N  N   . ILE A 1 354 ? 7.424   1.343   -10.458 1.00   30.91  ? 369 ILE A N   1 
ATOM   2383 C  CA  . ILE A 1 354 ? 6.954   2.677   -10.705 1.00   31.19  ? 369 ILE A CA  1 
ATOM   2384 C  C   . ILE A 1 354 ? 6.961   3.435   -9.405  1.00   31.68  ? 369 ILE A C   1 
ATOM   2385 O  O   . ILE A 1 354 ? 6.382   2.973   -8.437  1.00   32.53  ? 369 ILE A O   1 
ATOM   2386 C  CB  . ILE A 1 354 ? 5.519   2.619   -11.225 1.00   31.31  ? 369 ILE A CB  1 
ATOM   2387 C  CG1 . ILE A 1 354 ? 5.532   2.052   -12.640 1.00   31.97  ? 369 ILE A CG1 1 
ATOM   2388 C  CG2 . ILE A 1 354 ? 4.905   3.991   -11.187 1.00   31.22  ? 369 ILE A CG2 1 
ATOM   2389 C  CD1 . ILE A 1 354 ? 4.187   1.981   -13.280 1.00   33.18  ? 369 ILE A CD1 1 
ATOM   2390 N  N   . LEU A 1 355 ? 7.581   4.605   -9.367  1.00   32.20  ? 370 LEU A N   1 
ATOM   2391 C  CA  . LEU A 1 355 ? 7.623   5.367   -8.128  1.00   32.85  ? 370 LEU A CA  1 
ATOM   2392 C  C   . LEU A 1 355 ? 6.252   5.974   -7.779  1.00   34.19  ? 370 LEU A C   1 
ATOM   2393 O  O   . LEU A 1 355 ? 5.348   5.985   -8.601  1.00   35.87  ? 370 LEU A O   1 
ATOM   2394 C  CB  . LEU A 1 355 ? 8.691   6.469   -8.182  1.00   32.26  ? 370 LEU A CB  1 
ATOM   2395 C  CG  . LEU A 1 355 ? 10.091  6.007   -8.545  1.00   32.65  ? 370 LEU A CG  1 
ATOM   2396 C  CD1 . LEU A 1 355 ? 11.075  7.175   -8.517  1.00   32.75  ? 370 LEU A CD1 1 
ATOM   2397 C  CD2 . LEU A 1 355 ? 10.522  4.879   -7.612  1.00   32.58  ? 370 LEU A CD2 1 
ATOM   2398 N  N   . ILE A 1 356 ? 6.137   6.490   -6.551  1.00   35.27  ? 371 ILE A N   1 
ATOM   2399 C  CA  . ILE A 1 356 ? 4.976   7.246   -6.104  1.00   36.45  ? 371 ILE A CA  1 
ATOM   2400 C  C   . ILE A 1 356 ? 4.986   8.414   -7.078  1.00   36.34  ? 371 ILE A C   1 
ATOM   2401 O  O   . ILE A 1 356 ? 6.054   8.841   -7.504  1.00   37.66  ? 371 ILE A O   1 
ATOM   2402 C  CB  . ILE A 1 356 ? 5.151   7.790   -4.634  1.00   38.70  ? 371 ILE A CB  1 
ATOM   2403 C  CG1 . ILE A 1 356 ? 5.493   6.715   -3.590  1.00   39.24  ? 371 ILE A CG1 1 
ATOM   2404 C  CG2 . ILE A 1 356 ? 3.916   8.519   -4.113  1.00   38.99  ? 371 ILE A CG2 1 
ATOM   2405 C  CD1 . ILE A 1 356 ? 6.309   7.298   -2.436  1.00   38.58  ? 371 ILE A CD1 1 
ATOM   2406 N  N   . PRO A 1 357 ? 3.818   8.962   -7.437  1.00   35.69  ? 372 PRO A N   1 
ATOM   2407 C  CA  . PRO A 1 357 ? 3.894   10.022  -8.468  1.00   34.93  ? 372 PRO A CA  1 
ATOM   2408 C  C   . PRO A 1 357 ? 4.680   11.228  -8.011  1.00   34.01  ? 372 PRO A C   1 
ATOM   2409 O  O   . PRO A 1 357 ? 4.631   11.554  -6.857  1.00   33.98  ? 372 PRO A O   1 
ATOM   2410 C  CB  . PRO A 1 357 ? 2.422   10.411  -8.688  1.00   35.40  ? 372 PRO A CB  1 
ATOM   2411 C  CG  . PRO A 1 357 ? 1.648   9.207   -8.251  1.00   35.51  ? 372 PRO A CG  1 
ATOM   2412 C  CD  . PRO A 1 357 ? 2.429   8.629   -7.086  1.00   35.25  ? 372 PRO A CD  1 
ATOM   2413 N  N   . HIS A 1 358 ? 5.400   11.872  -8.917  1.00   34.41  ? 373 HIS A N   1 
ATOM   2414 C  CA  . HIS A 1 358 ? 5.961   13.191  -8.675  1.00   34.32  ? 373 HIS A CA  1 
ATOM   2415 C  C   . HIS A 1 358 ? 5.051   14.209  -9.284  1.00   36.08  ? 373 HIS A C   1 
ATOM   2416 O  O   . HIS A 1 358 ? 4.847   14.185  -10.514 1.00   37.77  ? 373 HIS A O   1 
ATOM   2417 C  CB  . HIS A 1 358 ? 7.305   13.343  -9.356  1.00   33.74  ? 373 HIS A CB  1 
ATOM   2418 C  CG  . HIS A 1 358 ? 8.438   12.806  -8.558  1.00   33.46  ? 373 HIS A CG  1 
ATOM   2419 N  ND1 . HIS A 1 358 ? 8.601   11.458  -8.331  1.00   33.32  ? 373 HIS A ND1 1 
ATOM   2420 C  CD2 . HIS A 1 358 ? 9.470   13.422  -7.937  1.00   32.79  ? 373 HIS A CD2 1 
ATOM   2421 C  CE1 . HIS A 1 358 ? 9.675   11.265  -7.591  1.00   32.15  ? 373 HIS A CE1 1 
ATOM   2422 N  NE2 . HIS A 1 358 ? 10.223  12.440  -7.349  1.00   32.58  ? 373 HIS A NE2 1 
ATOM   2423 N  N   . VAL A 1 359 ? 4.541   15.136  -8.476  1.00   36.58  ? 374 VAL A N   1 
ATOM   2424 C  CA  . VAL A 1 359 ? 3.623   16.145  -8.999  1.00   37.82  ? 374 VAL A CA  1 
ATOM   2425 C  C   . VAL A 1 359 ? 4.282   17.456  -9.375  1.00   40.45  ? 374 VAL A C   1 
ATOM   2426 O  O   . VAL A 1 359 ? 5.146   17.964  -8.663  1.00   43.06  ? 374 VAL A O   1 
ATOM   2427 C  CB  . VAL A 1 359 ? 2.452   16.408  -8.054  1.00   37.29  ? 374 VAL A CB  1 
ATOM   2428 C  CG1 . VAL A 1 359 ? 1.509   17.417  -8.676  1.00   38.38  ? 374 VAL A CG1 1 
ATOM   2429 C  CG2 . VAL A 1 359 ? 1.711   15.104  -7.794  1.00   36.87  ? 374 VAL A CG2 1 
ATOM   2430 N  N   . ALA A 1 360 ? 3.829   18.011  -10.494 1.00   42.75  ? 375 ALA A N   1 
ATOM   2431 C  CA  . ALA A 1 360 ? 4.340   19.249  -11.016 1.00   44.83  ? 375 ALA A CA  1 
ATOM   2432 C  C   . ALA A 1 360 ? 3.839   20.417  -10.192 1.00   47.29  ? 375 ALA A C   1 
ATOM   2433 O  O   . ALA A 1 360 ? 2.704   20.870  -10.382 1.00   47.52  ? 375 ALA A O   1 
ATOM   2434 C  CB  . ALA A 1 360 ? 3.919   19.419  -12.469 1.00   45.96  ? 375 ALA A CB  1 
ATOM   2435 N  N   . MET A 1 361 ? 4.727   20.935  -9.337  1.00   49.36  ? 376 MET A N   1 
ATOM   2436 C  CA  . MET A 1 361 ? 4.418   22.016  -8.407  1.00   52.54  ? 376 MET A CA  1 
ATOM   2437 C  C   . MET A 1 361 ? 4.086   23.363  -9.049  1.00   55.25  ? 376 MET A C   1 
ATOM   2438 O  O   . MET A 1 361 ? 3.467   24.226  -8.410  1.00   58.91  ? 376 MET A O   1 
ATOM   2439 C  CB  . MET A 1 361 ? 5.615   22.242  -7.507  1.00   55.45  ? 376 MET A CB  1 
ATOM   2440 C  CG  . MET A 1 361 ? 5.988   21.059  -6.628  1.00   55.99  ? 376 MET A CG  1 
ATOM   2441 S  SD  . MET A 1 361 ? 5.091   21.074  -5.085  1.00   56.08  ? 376 MET A SD  1 
ATOM   2442 C  CE  . MET A 1 361 ? 5.814   22.480  -4.257  1.00   55.98  ? 376 MET A CE  1 
ATOM   2443 N  N   . GLN A 1 362 ? 4.542   23.565  -10.278 1.00   54.95  ? 377 GLN A N   1 
ATOM   2444 C  CA  . GLN A 1 362 ? 4.353   24.811  -10.998 1.00   54.79  ? 377 GLN A CA  1 
ATOM   2445 C  C   . GLN A 1 362 ? 4.306   24.425  -12.463 1.00   53.75  ? 377 GLN A C   1 
ATOM   2446 O  O   . GLN A 1 362 ? 4.661   23.303  -12.798 1.00   53.45  ? 377 GLN A O   1 
ATOM   2447 C  CB  . GLN A 1 362 ? 5.544   25.745  -10.741 1.00   56.48  ? 377 GLN A CB  1 
ATOM   2448 C  CG  . GLN A 1 362 ? 6.804   25.390  -11.540 1.00   57.55  ? 377 GLN A CG  1 
ATOM   2449 C  CD  . GLN A 1 362 ? 8.062   26.166  -11.137 1.00   60.45  ? 377 GLN A CD  1 
ATOM   2450 O  OE1 . GLN A 1 362 ? 8.202   26.636  -10.002 1.00   62.88  ? 377 GLN A OE1 1 
ATOM   2451 N  NE2 . GLN A 1 362 ? 8.997   26.279  -12.069 1.00   60.99  ? 377 GLN A NE2 1 
ATOM   2452 N  N   . ASP A 1 363 ? 3.904   25.328  -13.352 1.00   53.36  ? 378 ASP A N   1 
ATOM   2453 C  CA  . ASP A 1 363 ? 3.937   24.986  -14.768 1.00   53.24  ? 378 ASP A CA  1 
ATOM   2454 C  C   . ASP A 1 363 ? 5.400   24.787  -15.125 1.00   51.64  ? 378 ASP A C   1 
ATOM   2455 O  O   . ASP A 1 363 ? 6.217   25.666  -14.903 1.00   51.41  ? 378 ASP A O   1 
ATOM   2456 C  CB  . ASP A 1 363 ? 3.319   26.081  -15.670 1.00   55.59  ? 378 ASP A CB  1 
ATOM   2457 C  CG  . ASP A 1 363 ? 1.795   26.219  -15.512 1.00   56.58  ? 378 ASP A CG  1 
ATOM   2458 O  OD1 . ASP A 1 363 ? 1.124   25.284  -15.026 1.00   55.49  ? 378 ASP A OD1 1 
ATOM   2459 O  OD2 . ASP A 1 363 ? 1.259   27.285  -15.895 1.00   60.60  ? 378 ASP A OD2 1 
ATOM   2460 N  N   . THR A 1 364 ? 5.728   23.627  -15.671 1.00   50.84  ? 379 THR A N   1 
ATOM   2461 C  CA  . THR A 1 364 ? 7.087   23.353  -16.102 1.00   51.19  ? 379 THR A CA  1 
ATOM   2462 C  C   . THR A 1 364 ? 7.134   22.655  -17.460 1.00   50.41  ? 379 THR A C   1 
ATOM   2463 O  O   . THR A 1 364 ? 6.233   22.823  -18.276 1.00   51.10  ? 379 THR A O   1 
ATOM   2464 C  CB  . THR A 1 364 ? 7.832   22.521  -15.056 1.00   51.28  ? 379 THR A CB  1 
ATOM   2465 O  OG1 . THR A 1 364 ? 9.062   22.050  -15.632 1.00   54.20  ? 379 THR A OG1 1 
ATOM   2466 C  CG2 . THR A 1 364 ? 6.990   21.342  -14.588 1.00   49.71  ? 379 THR A CG2 1 
ATOM   2467 N  N   . SER A 1 365 ? 8.193   21.895  -17.702 1.00   49.52  ? 380 SER A N   1 
ATOM   2468 C  CA  . SER A 1 365 ? 8.410   21.263  -18.995 1.00   51.18  ? 380 SER A CA  1 
ATOM   2469 C  C   . SER A 1 365 ? 9.038   19.900  -18.762 1.00   50.80  ? 380 SER A C   1 
ATOM   2470 O  O   . SER A 1 365 ? 9.486   19.611  -17.676 1.00   49.54  ? 380 SER A O   1 
ATOM   2471 C  CB  . SER A 1 365 ? 9.348   22.102  -19.867 1.00   51.94  ? 380 SER A CB  1 
ATOM   2472 O  OG  . SER A 1 365 ? 10.633  21.494  -19.914 1.00   51.04  ? 380 SER A OG  1 
ATOM   2473 N  N   . LEU A 1 366 ? 9.051   19.059  -19.784 1.00   52.13  ? 381 LEU A N   1 
ATOM   2474 C  CA  . LEU A 1 366 ? 9.641   17.728  -19.680 1.00   52.98  ? 381 LEU A CA  1 
ATOM   2475 C  C   . LEU A 1 366 ? 9.767   17.278  -21.098 1.00   53.45  ? 381 LEU A C   1 
ATOM   2476 O  O   . LEU A 1 366 ? 8.905   17.593  -21.894 1.00   52.94  ? 381 LEU A O   1 
ATOM   2477 C  CB  . LEU A 1 366 ? 8.746   16.781  -18.893 1.00   53.25  ? 381 LEU A CB  1 
ATOM   2478 C  CG  . LEU A 1 366 ? 9.446   15.714  -18.047 1.00   54.60  ? 381 LEU A CG  1 
ATOM   2479 C  CD1 . LEU A 1 366 ? 8.373   14.910  -17.332 1.00   55.70  ? 381 LEU A CD1 1 
ATOM   2480 C  CD2 . LEU A 1 366 ? 10.325  14.789  -18.861 1.00   55.24  ? 381 LEU A CD2 1 
ATOM   2481 N  N   . GLY A 1 367 ? 10.857  16.606  -21.443 1.00   55.25  ? 382 GLY A N   1 
ATOM   2482 C  CA  . GLY A 1 367 ? 11.249  16.563  -22.843 1.00   58.81  ? 382 GLY A CA  1 
ATOM   2483 C  C   . GLY A 1 367 ? 11.339  18.043  -23.160 1.00   61.09  ? 382 GLY A C   1 
ATOM   2484 O  O   . GLY A 1 367 ? 11.711  18.832  -22.258 1.00   66.69  ? 382 GLY A O   1 
ATOM   2485 N  N   . GLY A 1 368 ? 10.980  18.445  -24.377 1.00   58.29  ? 383 GLY A N   1 
ATOM   2486 C  CA  . GLY A 1 368 ? 10.842  19.868  -24.671 1.00   59.05  ? 383 GLY A CA  1 
ATOM   2487 C  C   . GLY A 1 368 ? 9.389   20.318  -24.621 1.00   59.53  ? 383 GLY A C   1 
ATOM   2488 O  O   . GLY A 1 368 ? 9.000   21.269  -25.309 1.00   62.60  ? 383 GLY A O   1 
ATOM   2489 N  N   . HIS A 1 369 ? 8.579   19.628  -23.821 1.00   56.75  ? 384 HIS A N   1 
ATOM   2490 C  CA  . HIS A 1 369 ? 7.124   19.758  -23.874 1.00   54.63  ? 384 HIS A CA  1 
ATOM   2491 C  C   . HIS A 1 369 ? 6.652   20.380  -22.593 1.00   52.86  ? 384 HIS A C   1 
ATOM   2492 O  O   . HIS A 1 369 ? 7.140   20.040  -21.521 1.00   52.50  ? 384 HIS A O   1 
ATOM   2493 C  CB  . HIS A 1 369 ? 6.470   18.398  -24.005 1.00   53.55  ? 384 HIS A CB  1 
ATOM   2494 C  CG  . HIS A 1 369 ? 6.980   17.594  -25.149 1.00   55.07  ? 384 HIS A CG  1 
ATOM   2495 N  ND1 . HIS A 1 369 ? 6.405   17.642  -26.402 1.00   58.23  ? 384 HIS A ND1 1 
ATOM   2496 C  CD2 . HIS A 1 369 ? 8.002   16.710  -25.236 1.00   55.58  ? 384 HIS A CD2 1 
ATOM   2497 C  CE1 . HIS A 1 369 ? 7.058   16.830  -27.216 1.00   58.76  ? 384 HIS A CE1 1 
ATOM   2498 N  NE2 . HIS A 1 369 ? 8.028   16.245  -26.530 1.00   58.00  ? 384 HIS A NE2 1 
ATOM   2499 N  N   . SER A 1 370 ? 5.695   21.281  -22.686 1.00   52.37  ? 385 SER A N   1 
ATOM   2500 C  CA  . SER A 1 370 ? 5.270   21.988  -21.501 1.00   52.94  ? 385 SER A CA  1 
ATOM   2501 C  C   . SER A 1 370 ? 4.464   21.026  -20.630 1.00   51.79  ? 385 SER A C   1 
ATOM   2502 O  O   . SER A 1 370 ? 3.835   20.088  -21.130 1.00   53.38  ? 385 SER A O   1 
ATOM   2503 C  CB  . SER A 1 370 ? 4.474   23.246  -21.858 1.00   54.27  ? 385 SER A CB  1 
ATOM   2504 O  OG  . SER A 1 370 ? 3.100   23.059  -21.644 1.00   54.61  ? 385 SER A OG  1 
ATOM   2505 N  N   . VAL A 1 371 ? 4.515   21.243  -19.326 1.00   49.98  ? 386 VAL A N   1 
ATOM   2506 C  CA  . VAL A 1 371 ? 3.878   20.346  -18.377 1.00   48.66  ? 386 VAL A CA  1 
ATOM   2507 C  C   . VAL A 1 371 ? 3.117   21.177  -17.344 1.00   49.39  ? 386 VAL A C   1 
ATOM   2508 O  O   . VAL A 1 371 ? 3.723   21.719  -16.411 1.00   48.52  ? 386 VAL A O   1 
ATOM   2509 C  CB  . VAL A 1 371 ? 4.895   19.439  -17.656 1.00   46.07  ? 386 VAL A CB  1 
ATOM   2510 C  CG1 . VAL A 1 371 ? 4.170   18.457  -16.751 1.00   44.41  ? 386 VAL A CG1 1 
ATOM   2511 C  CG2 . VAL A 1 371 ? 5.751   18.701  -18.665 1.00   45.78  ? 386 VAL A CG2 1 
ATOM   2512 N  N   . PRO A 1 372 ? 1.783   21.281  -17.508 1.00   49.31  ? 387 PRO A N   1 
ATOM   2513 C  CA  . PRO A 1 372 ? 0.943   22.090  -16.609 1.00   49.10  ? 387 PRO A CA  1 
ATOM   2514 C  C   . PRO A 1 372 ? 1.183   21.767  -15.150 1.00   47.05  ? 387 PRO A C   1 
ATOM   2515 O  O   . PRO A 1 372 ? 1.407   20.613  -14.822 1.00   45.88  ? 387 PRO A O   1 
ATOM   2516 C  CB  . PRO A 1 372 ? -0.484  21.679  -16.963 1.00   48.95  ? 387 PRO A CB  1 
ATOM   2517 C  CG  . PRO A 1 372 ? -0.396  21.059  -18.303 1.00   50.18  ? 387 PRO A CG  1 
ATOM   2518 C  CD  . PRO A 1 372 ? 1.001   20.589  -18.540 1.00   49.25  ? 387 PRO A CD  1 
ATOM   2519 N  N   . LYS A 1 373 ? 1.126   22.777  -14.291 1.00   46.90  ? 388 LYS A N   1 
ATOM   2520 C  CA  . LYS A 1 373 ? 1.031   22.555  -12.857 1.00   47.16  ? 388 LYS A CA  1 
ATOM   2521 C  C   . LYS A 1 373 ? 0.042   21.426  -12.575 1.00   46.63  ? 388 LYS A C   1 
ATOM   2522 O  O   . LYS A 1 373 ? -0.922  21.227  -13.328 1.00   49.43  ? 388 LYS A O   1 
ATOM   2523 C  CB  . LYS A 1 373 ? 0.569   23.829  -12.152 1.00   48.66  ? 388 LYS A CB  1 
ATOM   2524 C  CG  . LYS A 1 373 ? 0.412   23.648  -10.653 1.00   50.27  ? 388 LYS A CG  1 
ATOM   2525 C  CD  . LYS A 1 373 ? 0.292   24.965  -9.895  1.00   52.47  ? 388 LYS A CD  1 
ATOM   2526 C  CE  . LYS A 1 373 ? -0.349  24.732  -8.519  1.00   53.85  ? 388 LYS A CE  1 
ATOM   2527 N  NZ  . LYS A 1 373 ? -0.713  25.971  -7.762  1.00   56.19  ? 388 LYS A NZ  1 
ATOM   2528 N  N   . GLY A 1 374 ? 0.278   20.672  -11.516 1.00   44.12  ? 389 GLY A N   1 
ATOM   2529 C  CA  . GLY A 1 374 ? -0.626  19.594  -11.147 1.00   42.78  ? 389 GLY A CA  1 
ATOM   2530 C  C   . GLY A 1 374 ? -0.418  18.269  -11.862 1.00   42.02  ? 389 GLY A C   1 
ATOM   2531 O  O   . GLY A 1 374 ? -0.988  17.262  -11.431 1.00   41.58  ? 389 GLY A O   1 
ATOM   2532 N  N   . THR A 1 375 ? 0.379   18.251  -12.937 1.00   41.56  ? 390 THR A N   1 
ATOM   2533 C  CA  . THR A 1 375 ? 0.614   17.030  -13.715 1.00   41.80  ? 390 THR A CA  1 
ATOM   2534 C  C   . THR A 1 375 ? 1.307   15.972  -12.850 1.00   41.17  ? 390 THR A C   1 
ATOM   2535 O  O   . THR A 1 375 ? 2.210   16.297  -12.079 1.00   37.96  ? 390 THR A O   1 
ATOM   2536 C  CB  . THR A 1 375 ? 1.495   17.309  -14.959 1.00   42.27  ? 390 THR A CB  1 
ATOM   2537 O  OG1 . THR A 1 375 ? 0.850   18.266  -15.790 1.00   45.56  ? 390 THR A OG1 1 
ATOM   2538 C  CG2 . THR A 1 375 ? 1.701   16.090  -15.781 1.00   41.88  ? 390 THR A CG2 1 
ATOM   2539 N  N   . ARG A 1 376 ? 0.872   14.718  -13.000 1.00   41.76  ? 391 ARG A N   1 
ATOM   2540 C  CA  . ARG A 1 376 ? 1.445   13.600  -12.266 1.00   42.49  ? 391 ARG A CA  1 
ATOM   2541 C  C   . ARG A 1 376 ? 2.466   12.934  -13.128 1.00   41.21  ? 391 ARG A C   1 
ATOM   2542 O  O   . ARG A 1 376 ? 2.212   12.735  -14.295 1.00   43.11  ? 391 ARG A O   1 
ATOM   2543 C  CB  . ARG A 1 376 ? 0.357   12.589  -11.879 1.00   44.80  ? 391 ARG A CB  1 
ATOM   2544 C  CG  . ARG A 1 376 ? -0.615  13.157  -10.862 1.00   48.03  ? 391 ARG A CG  1 
ATOM   2545 C  CD  . ARG A 1 376 ? -1.573  12.139  -10.282 1.00   52.64  ? 391 ARG A CD  1 
ATOM   2546 N  NE  . ARG A 1 376 ? -2.293  12.744  -9.152  1.00   61.92  ? 391 ARG A NE  1 
ATOM   2547 C  CZ  . ARG A 1 376 ? -3.153  12.108  -8.343  1.00   68.37  ? 391 ARG A CZ  1 
ATOM   2548 N  NH1 . ARG A 1 376 ? -3.427  10.812  -8.525  1.00   70.52  ? 391 ARG A NH1 1 
ATOM   2549 N  NH2 . ARG A 1 376 ? -3.742  12.773  -7.337  1.00   67.27  ? 391 ARG A NH2 1 
ATOM   2550 N  N   . VAL A 1 377 ? 3.616   12.575  -12.570 1.00   39.45  ? 392 VAL A N   1 
ATOM   2551 C  CA  . VAL A 1 377 ? 4.694   11.982  -13.382 1.00   38.53  ? 392 VAL A CA  1 
ATOM   2552 C  C   . VAL A 1 377 ? 5.137   10.646  -12.794 1.00   37.29  ? 392 VAL A C   1 
ATOM   2553 O  O   . VAL A 1 377 ? 5.734   10.608  -11.734 1.00   36.93  ? 392 VAL A O   1 
ATOM   2554 C  CB  . VAL A 1 377 ? 5.918   12.928  -13.480 1.00   38.17  ? 392 VAL A CB  1 
ATOM   2555 C  CG1 . VAL A 1 377 ? 7.104   12.224  -14.101 1.00   38.58  ? 392 VAL A CG1 1 
ATOM   2556 C  CG2 . VAL A 1 377 ? 5.587   14.174  -14.278 1.00   38.54  ? 392 VAL A CG2 1 
ATOM   2557 N  N   . LEU A 1 378 ? 4.858   9.560   -13.502 1.00   36.44  ? 393 LEU A N   1 
ATOM   2558 C  CA  . LEU A 1 378 ? 5.235   8.234   -13.059 1.00   35.25  ? 393 LEU A CA  1 
ATOM   2559 C  C   . LEU A 1 378 ? 6.620   7.896   -13.566 1.00   34.94  ? 393 LEU A C   1 
ATOM   2560 O  O   . LEU A 1 378 ? 6.862   7.915   -14.757 1.00   36.02  ? 393 LEU A O   1 
ATOM   2561 C  CB  . LEU A 1 378 ? 4.200   7.203   -13.512 1.00   35.47  ? 393 LEU A CB  1 
ATOM   2562 C  CG  . LEU A 1 378 ? 2.792   7.504   -12.972 1.00   36.06  ? 393 LEU A CG  1 
ATOM   2563 C  CD1 . LEU A 1 378 ? 1.840   6.376   -13.335 1.00   36.96  ? 393 LEU A CD1 1 
ATOM   2564 C  CD2 . LEU A 1 378 ? 2.787   7.734   -11.466 1.00   35.40  ? 393 LEU A CD2 1 
ATOM   2565 N  N   . VAL A 1 379 ? 7.548   7.637   -12.647 1.00   34.23  ? 394 VAL A N   1 
ATOM   2566 C  CA  . VAL A 1 379 ? 8.899   7.284   -13.036 1.00   33.41  ? 394 VAL A CA  1 
ATOM   2567 C  C   . VAL A 1 379 ? 8.948   5.786   -13.167 1.00   33.33  ? 394 VAL A C   1 
ATOM   2568 O  O   . VAL A 1 379 ? 8.568   5.077   -12.251 1.00   31.87  ? 394 VAL A O   1 
ATOM   2569 C  CB  . VAL A 1 379 ? 9.938   7.792   -12.035 1.00   32.59  ? 394 VAL A CB  1 
ATOM   2570 C  CG1 . VAL A 1 379 ? 11.269  7.097   -12.252 1.00   33.02  ? 394 VAL A CG1 1 
ATOM   2571 C  CG2 . VAL A 1 379 ? 10.113  9.292   -12.178 1.00   32.63  ? 394 VAL A CG2 1 
ATOM   2572 N  N   . ASN A 1 380 ? 9.392   5.313   -14.329 1.00   34.66  ? 395 ASN A N   1 
ATOM   2573 C  CA  . ASN A 1 380 ? 9.388   3.890   -14.611 1.00   35.35  ? 395 ASN A CA  1 
ATOM   2574 C  C   . ASN A 1 380 ? 10.765  3.335   -14.330 1.00   36.29  ? 395 ASN A C   1 
ATOM   2575 O  O   . ASN A 1 380 ? 11.658  3.338   -15.149 1.00   35.73  ? 395 ASN A O   1 
ATOM   2576 C  CB  . ASN A 1 380 ? 8.943   3.596   -16.034 1.00   35.42  ? 395 ASN A CB  1 
ATOM   2577 C  CG  . ASN A 1 380 ? 8.766   2.112   -16.291 1.00   35.55  ? 395 ASN A CG  1 
ATOM   2578 O  OD1 . ASN A 1 380 ? 9.119   1.268   -15.459 1.00   35.12  ? 395 ASN A OD1 1 
ATOM   2579 N  ND2 . ASN A 1 380 ? 8.217   1.784   -17.446 1.00   36.00  ? 395 ASN A ND2 1 
ATOM   2580 N  N   . MET A 1 381 ? 10.894  2.831   -13.129 1.00   38.88  ? 396 MET A N   1 
ATOM   2581 C  CA  . MET A 1 381 ? 12.156  2.388   -12.613 1.00   41.06  ? 396 MET A CA  1 
ATOM   2582 C  C   . MET A 1 381 ? 12.610  1.108   -13.303 1.00   39.89  ? 396 MET A C   1 
ATOM   2583 O  O   . MET A 1 381 ? 13.810  0.858   -13.434 1.00   41.74  ? 396 MET A O   1 
ATOM   2584 C  CB  . MET A 1 381 ? 12.051  2.212   -11.098 1.00   43.55  ? 396 MET A CB  1 
ATOM   2585 C  CG  . MET A 1 381 ? 13.409  2.282   -10.421 1.00   49.07  ? 396 MET A CG  1 
ATOM   2586 S  SD  . MET A 1 381 ? 13.709  3.753   -9.404  1.00   55.90  ? 396 MET A SD  1 
ATOM   2587 C  CE  . MET A 1 381 ? 13.810  5.003   -10.673 1.00   55.31  ? 396 MET A CE  1 
ATOM   2588 N  N   . TRP A 1 382 ? 11.669  0.298   -13.755 1.00   38.96  ? 397 TRP A N   1 
ATOM   2589 C  CA  . TRP A 1 382 ? 12.013  -0.948  -14.442 1.00   38.45  ? 397 TRP A CA  1 
ATOM   2590 C  C   . TRP A 1 382 ? 12.669  -0.622  -15.782 1.00   39.13  ? 397 TRP A C   1 
ATOM   2591 O  O   . TRP A 1 382 ? 13.688  -1.191  -16.122 1.00   40.45  ? 397 TRP A O   1 
ATOM   2592 C  CB  . TRP A 1 382 ? 10.769  -1.790  -14.648 1.00   38.72  ? 397 TRP A CB  1 
ATOM   2593 C  CG  . TRP A 1 382 ? 11.020  -3.027  -15.415 1.00   39.61  ? 397 TRP A CG  1 
ATOM   2594 C  CD1 . TRP A 1 382 ? 11.128  -3.147  -16.768 1.00   40.23  ? 397 TRP A CD1 1 
ATOM   2595 C  CD2 . TRP A 1 382 ? 11.175  -4.338  -14.882 1.00   39.78  ? 397 TRP A CD2 1 
ATOM   2596 N  NE1 . TRP A 1 382 ? 11.368  -4.448  -17.104 1.00   41.26  ? 397 TRP A NE1 1 
ATOM   2597 C  CE2 . TRP A 1 382 ? 11.392  -5.205  -15.965 1.00   40.97  ? 397 TRP A CE2 1 
ATOM   2598 C  CE3 . TRP A 1 382 ? 11.146  -4.866  -13.593 1.00   39.65  ? 397 TRP A CE3 1 
ATOM   2599 C  CZ2 . TRP A 1 382 ? 11.600  -6.572  -15.798 1.00   41.77  ? 397 TRP A CZ2 1 
ATOM   2600 C  CZ3 . TRP A 1 382 ? 11.347  -6.221  -13.426 1.00   40.48  ? 397 TRP A CZ3 1 
ATOM   2601 C  CH2 . TRP A 1 382 ? 11.581  -7.060  -14.523 1.00   41.11  ? 397 TRP A CH2 1 
ATOM   2602 N  N   . ALA A 1 383 ? 12.091  0.322   -16.518 1.00   38.76  ? 398 ALA A N   1 
ATOM   2603 C  CA  . ALA A 1 383 ? 12.587  0.723   -17.820 1.00   38.93  ? 398 ALA A CA  1 
ATOM   2604 C  C   . ALA A 1 383 ? 14.024  1.152   -17.722 1.00   39.11  ? 398 ALA A C   1 
ATOM   2605 O  O   . ALA A 1 383 ? 14.902  0.599   -18.392 1.00   39.99  ? 398 ALA A O   1 
ATOM   2606 C  CB  . ALA A 1 383 ? 11.738  1.859   -18.389 1.00   39.00  ? 398 ALA A CB  1 
ATOM   2607 N  N   . ILE A 1 384 ? 14.283  2.126   -16.866 1.00   39.20  ? 399 ILE A N   1 
ATOM   2608 C  CA  . ILE A 1 384 ? 15.636  2.681   -16.784 1.00   39.75  ? 399 ILE A CA  1 
ATOM   2609 C  C   . ILE A 1 384 ? 16.634  1.666   -16.230 1.00   39.61  ? 399 ILE A C   1 
ATOM   2610 O  O   . ILE A 1 384 ? 17.842  1.760   -16.501 1.00   39.95  ? 399 ILE A O   1 
ATOM   2611 C  CB  . ILE A 1 384 ? 15.714  3.969   -15.972 1.00   38.92  ? 399 ILE A CB  1 
ATOM   2612 C  CG1 . ILE A 1 384 ? 15.098  3.759   -14.611 1.00   38.39  ? 399 ILE A CG1 1 
ATOM   2613 C  CG2 . ILE A 1 384 ? 15.041  5.121   -16.714 1.00   39.13  ? 399 ILE A CG2 1 
ATOM   2614 C  CD1 . ILE A 1 384 ? 15.561  4.802   -13.617 1.00   39.47  ? 399 ILE A CD1 1 
ATOM   2615 N  N   . HIS A 1 385 ? 16.126  0.682   -15.503 1.00   38.66  ? 400 HIS A N   1 
ATOM   2616 C  CA  . HIS A 1 385 ? 16.964  -0.410  -15.063 1.00   39.64  ? 400 HIS A CA  1 
ATOM   2617 C  C   . HIS A 1 385 ? 17.041  -1.580  -15.989 1.00   40.32  ? 400 HIS A C   1 
ATOM   2618 O  O   . HIS A 1 385 ? 17.878  -2.467  -15.784 1.00   40.47  ? 400 HIS A O   1 
ATOM   2619 C  CB  . HIS A 1 385 ? 16.515  -0.881  -13.699 1.00   39.68  ? 400 HIS A CB  1 
ATOM   2620 C  CG  . HIS A 1 385 ? 16.889  0.072   -12.622 1.00   39.57  ? 400 HIS A CG  1 
ATOM   2621 N  ND1 . HIS A 1 385 ? 16.316  0.043   -11.378 1.00   40.44  ? 400 HIS A ND1 1 
ATOM   2622 C  CD2 . HIS A 1 385 ? 17.768  1.103   -12.618 1.00   39.47  ? 400 HIS A CD2 1 
ATOM   2623 C  CE1 . HIS A 1 385 ? 16.855  0.997   -10.638 1.00   40.46  ? 400 HIS A CE1 1 
ATOM   2624 N  NE2 . HIS A 1 385 ? 17.728  1.658   -11.374 1.00   39.07  ? 400 HIS A NE2 1 
ATOM   2625 N  N   . HIS A 1 386 ? 16.186  -1.600  -17.004 1.00   40.00  ? 401 HIS A N   1 
ATOM   2626 C  CA  . HIS A 1 386 ? 16.267  -2.650  -17.978 1.00   40.46  ? 401 HIS A CA  1 
ATOM   2627 C  C   . HIS A 1 386 ? 16.541  -2.135  -19.336 1.00   41.94  ? 401 HIS A C   1 
ATOM   2628 O  O   . HIS A 1 386 ? 16.425  -2.887  -20.296 1.00   44.70  ? 401 HIS A O   1 
ATOM   2629 C  CB  . HIS A 1 386 ? 15.012  -3.472  -17.953 1.00   40.06  ? 401 HIS A CB  1 
ATOM   2630 C  CG  . HIS A 1 386 ? 15.000  -4.452  -16.847 1.00   39.66  ? 401 HIS A CG  1 
ATOM   2631 N  ND1 . HIS A 1 386 ? 14.924  -4.069  -15.530 1.00   38.90  ? 401 HIS A ND1 1 
ATOM   2632 C  CD2 . HIS A 1 386 ? 15.122  -5.796  -16.850 1.00   40.39  ? 401 HIS A CD2 1 
ATOM   2633 C  CE1 . HIS A 1 386 ? 14.959  -5.145  -14.768 1.00   39.42  ? 401 HIS A CE1 1 
ATOM   2634 N  NE2 . HIS A 1 386 ? 15.098  -6.205  -15.545 1.00   39.92  ? 401 HIS A NE2 1 
ATOM   2635 N  N   . ASP A 1 387 ? 16.948  -0.876  -19.444 1.00   41.90  ? 402 ASP A N   1 
ATOM   2636 C  CA  . ASP A 1 387 ? 17.185  -0.313  -20.762 1.00   43.31  ? 402 ASP A CA  1 
ATOM   2637 C  C   . ASP A 1 387 ? 18.438  -0.899  -21.445 1.00   44.85  ? 402 ASP A C   1 
ATOM   2638 O  O   . ASP A 1 387 ? 19.557  -0.635  -20.990 1.00   43.61  ? 402 ASP A O   1 
ATOM   2639 C  CB  . ASP A 1 387 ? 17.292  1.198   -20.701 1.00   43.06  ? 402 ASP A CB  1 
ATOM   2640 C  CG  . ASP A 1 387 ? 17.291  1.814   -22.079 1.00   44.75  ? 402 ASP A CG  1 
ATOM   2641 O  OD1 . ASP A 1 387 ? 17.447  1.077   -23.074 1.00   46.06  ? 402 ASP A OD1 1 
ATOM   2642 O  OD2 . ASP A 1 387 ? 17.123  3.036   -22.179 1.00   45.64  ? 402 ASP A OD2 1 
ATOM   2643 N  N   . PRO A 1 388 ? 18.258  -1.655  -22.567 1.00   46.26  ? 403 PRO A N   1 
ATOM   2644 C  CA  . PRO A 1 388 ? 19.380  -2.299  -23.302 1.00   48.25  ? 403 PRO A CA  1 
ATOM   2645 C  C   . PRO A 1 388 ? 20.371  -1.314  -23.938 1.00   49.75  ? 403 PRO A C   1 
ATOM   2646 O  O   . PRO A 1 388 ? 21.542  -1.652  -24.243 1.00   49.22  ? 403 PRO A O   1 
ATOM   2647 C  CB  . PRO A 1 388 ? 18.670  -3.113  -24.385 1.00   48.76  ? 403 PRO A CB  1 
ATOM   2648 C  CG  . PRO A 1 388 ? 17.387  -2.403  -24.580 1.00   48.25  ? 403 PRO A CG  1 
ATOM   2649 C  CD  . PRO A 1 388 ? 16.974  -1.940  -23.221 1.00   46.14  ? 403 PRO A CD  1 
ATOM   2650 N  N   . LYS A 1 389 ? 19.884  -0.101  -24.134 1.00   50.37  ? 404 LYS A N   1 
ATOM   2651 C  CA  . LYS A 1 389 ? 20.738  0.997   -24.489 1.00   52.49  ? 404 LYS A CA  1 
ATOM   2652 C  C   . LYS A 1 389 ? 21.776  1.247   -23.409 1.00   51.29  ? 404 LYS A C   1 
ATOM   2653 O  O   . LYS A 1 389 ? 22.861  1.662   -23.689 1.00   50.99  ? 404 LYS A O   1 
ATOM   2654 C  CB  . LYS A 1 389 ? 19.899  2.253   -24.666 1.00   54.58  ? 404 LYS A CB  1 
ATOM   2655 C  CG  . LYS A 1 389 ? 20.553  3.348   -25.494 1.00   57.82  ? 404 LYS A CG  1 
ATOM   2656 C  CD  . LYS A 1 389 ? 19.761  3.652   -26.754 1.00   60.49  ? 404 LYS A CD  1 
ATOM   2657 C  CE  . LYS A 1 389 ? 20.191  4.984   -27.377 1.00   63.53  ? 404 LYS A CE  1 
ATOM   2658 N  NZ  . LYS A 1 389 ? 19.874  5.081   -28.852 1.00   66.21  ? 404 LYS A NZ  1 
ATOM   2659 N  N   . HIS A 1 390 ? 21.437  1.036   -22.147 1.00   51.10  ? 405 HIS A N   1 
ATOM   2660 C  CA  . HIS A 1 390 ? 22.389  1.357   -21.079 1.00   48.87  ? 405 HIS A CA  1 
ATOM   2661 C  C   . HIS A 1 390 ? 22.923  0.155   -20.341 1.00   47.72  ? 405 HIS A C   1 
ATOM   2662 O  O   . HIS A 1 390 ? 23.837  0.308   -19.593 1.00   48.07  ? 405 HIS A O   1 
ATOM   2663 C  CB  . HIS A 1 390 ? 21.772  2.379   -20.118 1.00   47.20  ? 405 HIS A CB  1 
ATOM   2664 C  CG  . HIS A 1 390 ? 21.422  3.668   -20.785 1.00   48.75  ? 405 HIS A CG  1 
ATOM   2665 N  ND1 . HIS A 1 390 ? 22.372  4.602   -21.145 1.00   50.67  ? 405 HIS A ND1 1 
ATOM   2666 C  CD2 . HIS A 1 390 ? 20.239  4.144   -21.242 1.00   49.38  ? 405 HIS A CD2 1 
ATOM   2667 C  CE1 . HIS A 1 390 ? 21.783  5.616   -21.757 1.00   50.66  ? 405 HIS A CE1 1 
ATOM   2668 N  NE2 . HIS A 1 390 ? 20.488  5.365   -21.827 1.00   49.79  ? 405 HIS A NE2 1 
ATOM   2669 N  N   . TRP A 1 391 ? 22.393  -1.040  -20.566 1.00   48.03  ? 406 TRP A N   1 
ATOM   2670 C  CA  . TRP A 1 391 ? 22.811  -2.218  -19.814 1.00   48.05  ? 406 TRP A CA  1 
ATOM   2671 C  C   . TRP A 1 391 ? 23.002  -3.393  -20.752 1.00   51.08  ? 406 TRP A C   1 
ATOM   2672 O  O   . TRP A 1 391 ? 22.125  -3.658  -21.574 1.00   51.87  ? 406 TRP A O   1 
ATOM   2673 C  CB  . TRP A 1 391 ? 21.733  -2.602  -18.805 1.00   46.14  ? 406 TRP A CB  1 
ATOM   2674 C  CG  . TRP A 1 391 ? 21.371  -1.541  -17.783 1.00   44.83  ? 406 TRP A CG  1 
ATOM   2675 C  CD1 . TRP A 1 391 ? 20.337  -0.634  -17.857 1.00   44.08  ? 406 TRP A CD1 1 
ATOM   2676 C  CD2 . TRP A 1 391 ? 21.994  -1.326  -16.511 1.00   43.52  ? 406 TRP A CD2 1 
ATOM   2677 N  NE1 . TRP A 1 391 ? 20.309  0.150   -16.727 1.00   43.01  ? 406 TRP A NE1 1 
ATOM   2678 C  CE2 . TRP A 1 391 ? 21.318  -0.253  -15.888 1.00   42.89  ? 406 TRP A CE2 1 
ATOM   2679 C  CE3 . TRP A 1 391 ? 23.067  -1.915  -15.852 1.00   43.20  ? 406 TRP A CE3 1 
ATOM   2680 C  CZ2 . TRP A 1 391 ? 21.690  0.237   -14.637 1.00   41.83  ? 406 TRP A CZ2 1 
ATOM   2681 C  CZ3 . TRP A 1 391 ? 23.445  -1.413  -14.621 1.00   42.64  ? 406 TRP A CZ3 1 
ATOM   2682 C  CH2 . TRP A 1 391 ? 22.753  -0.354  -14.023 1.00   41.35  ? 406 TRP A CH2 1 
ATOM   2683 N  N   . ASP A 1 392 ? 24.117  -4.115  -20.624 1.00   53.39  ? 407 ASP A N   1 
ATOM   2684 C  CA  . ASP A 1 392 ? 24.365  -5.255  -21.493 1.00   56.93  ? 407 ASP A CA  1 
ATOM   2685 C  C   . ASP A 1 392 ? 23.735  -6.478  -20.899 1.00   57.72  ? 407 ASP A C   1 
ATOM   2686 O  O   . ASP A 1 392 ? 24.103  -6.874  -19.821 1.00   56.90  ? 407 ASP A O   1 
ATOM   2687 C  CB  . ASP A 1 392 ? 25.862  -5.525  -21.704 1.00   59.36  ? 407 ASP A CB  1 
ATOM   2688 C  CG  . ASP A 1 392 ? 26.111  -6.632  -22.747 1.00   63.43  ? 407 ASP A CG  1 
ATOM   2689 O  OD1 . ASP A 1 392 ? 26.146  -6.315  -23.976 1.00   68.14  ? 407 ASP A OD1 1 
ATOM   2690 O  OD2 . ASP A 1 392 ? 26.213  -7.822  -22.348 1.00   62.86  ? 407 ASP A OD2 1 
ATOM   2691 N  N   . GLN A 1 393 ? 22.820  -7.106  -21.624 1.00   61.95  ? 408 GLN A N   1 
ATOM   2692 C  CA  . GLN A 1 393 ? 22.107  -8.283  -21.120 1.00   64.52  ? 408 GLN A CA  1 
ATOM   2693 C  C   . GLN A 1 393 ? 21.353  -7.895  -19.871 1.00   63.04  ? 408 GLN A C   1 
ATOM   2694 O  O   . GLN A 1 393 ? 21.518  -8.507  -18.812 1.00   64.68  ? 408 GLN A O   1 
ATOM   2695 C  CB  . GLN A 1 393 ? 23.051  -9.468  -20.835 1.00   67.04  ? 408 GLN A CB  1 
ATOM   2696 C  CG  . GLN A 1 393 ? 23.445  -10.273 -22.080 1.00   71.30  ? 408 GLN A CG  1 
ATOM   2697 C  CD  . GLN A 1 393 ? 24.017  -11.640 -21.722 1.00   74.44  ? 408 GLN A CD  1 
ATOM   2698 O  OE1 . GLN A 1 393 ? 24.366  -11.902 -20.561 1.00   75.62  ? 408 GLN A OE1 1 
ATOM   2699 N  NE2 . GLN A 1 393 ? 24.116  -12.518 -22.710 1.00   77.30  ? 408 GLN A NE2 1 
ATOM   2700 N  N   . PRO A 1 394 ? 20.500  -6.870  -19.989 1.00   61.51  ? 409 PRO A N   1 
ATOM   2701 C  CA  . PRO A 1 394 ? 19.874  -6.250  -18.807 1.00   57.76  ? 409 PRO A CA  1 
ATOM   2702 C  C   . PRO A 1 394 ? 18.921  -7.174  -18.080 1.00   56.90  ? 409 PRO A C   1 
ATOM   2703 O  O   . PRO A 1 394 ? 18.495  -6.872  -16.984 1.00   54.03  ? 409 PRO A O   1 
ATOM   2704 C  CB  . PRO A 1 394 ? 19.089  -5.088  -19.409 1.00   56.92  ? 409 PRO A CB  1 
ATOM   2705 C  CG  . PRO A 1 394 ? 18.778  -5.535  -20.794 1.00   58.16  ? 409 PRO A CG  1 
ATOM   2706 C  CD  . PRO A 1 394 ? 19.928  -6.379  -21.252 1.00   59.07  ? 409 PRO A CD  1 
ATOM   2707 N  N   . GLU A 1 395 ? 18.552  -8.275  -18.716 1.00   61.36  ? 410 GLU A N   1 
ATOM   2708 C  CA  . GLU A 1 395 ? 17.576  -9.187  -18.162 1.00   63.88  ? 410 GLU A CA  1 
ATOM   2709 C  C   . GLU A 1 395 ? 18.293  -10.376 -17.505 1.00   61.94  ? 410 GLU A C   1 
ATOM   2710 O  O   . GLU A 1 395 ? 17.651  -11.279 -16.983 1.00   61.64  ? 410 GLU A O   1 
ATOM   2711 C  CB  . GLU A 1 395 ? 16.589  -9.625  -19.273 1.00   68.65  ? 410 GLU A CB  1 
ATOM   2712 C  CG  . GLU A 1 395 ? 15.717  -8.497  -19.863 1.00   70.94  ? 410 GLU A CG  1 
ATOM   2713 C  CD  . GLU A 1 395 ? 15.470  -8.646  -21.384 1.00   80.32  ? 410 GLU A CD  1 
ATOM   2714 O  OE1 . GLU A 1 395 ? 16.448  -8.888  -22.143 1.00   86.27  ? 410 GLU A OE1 1 
ATOM   2715 O  OE2 . GLU A 1 395 ? 14.303  -8.512  -21.850 1.00   80.26  ? 410 GLU A OE2 1 
ATOM   2716 N  N   . GLN A 1 396 ? 19.624  -10.364 -17.511 1.00   60.94  ? 411 GLN A N   1 
ATOM   2717 C  CA  . GLN A 1 396 ? 20.400  -11.440 -16.899 1.00   62.40  ? 411 GLN A CA  1 
ATOM   2718 C  C   . GLN A 1 396 ? 21.078  -10.972 -15.590 1.00   57.47  ? 411 GLN A C   1 
ATOM   2719 O  O   . GLN A 1 396 ? 21.520  -9.821  -15.477 1.00   53.29  ? 411 GLN A O   1 
ATOM   2720 C  CB  . GLN A 1 396 ? 21.432  -12.007 -17.901 1.00   67.83  ? 411 GLN A CB  1 
ATOM   2721 C  CG  . GLN A 1 396 ? 21.782  -13.474 -17.652 1.00   72.66  ? 411 GLN A CG  1 
ATOM   2722 C  CD  . GLN A 1 396 ? 22.797  -14.034 -18.642 1.00   78.18  ? 411 GLN A CD  1 
ATOM   2723 O  OE1 . GLN A 1 396 ? 22.566  -14.017 -19.851 1.00   83.01  ? 411 GLN A OE1 1 
ATOM   2724 N  NE2 . GLN A 1 396 ? 23.918  -14.557 -18.132 1.00   78.75  ? 411 GLN A NE2 1 
ATOM   2725 N  N   . PHE A 1 397 ? 21.144  -11.883 -14.623 1.00   54.19  ? 412 PHE A N   1 
ATOM   2726 C  CA  . PHE A 1 397 ? 21.636  -11.569 -13.306 1.00   55.30  ? 412 PHE A CA  1 
ATOM   2727 C  C   . PHE A 1 397 ? 23.153  -11.679 -13.250 1.00   57.41  ? 412 PHE A C   1 
ATOM   2728 O  O   . PHE A 1 397 ? 23.717  -12.780 -13.153 1.00   59.20  ? 412 PHE A O   1 
ATOM   2729 C  CB  . PHE A 1 397 ? 21.020  -12.513 -12.280 1.00   55.74  ? 412 PHE A CB  1 
ATOM   2730 C  CG  . PHE A 1 397 ? 21.330  -12.137 -10.864 1.00   54.44  ? 412 PHE A CG  1 
ATOM   2731 C  CD1 . PHE A 1 397 ? 22.547  -12.465 -10.289 1.00   54.15  ? 412 PHE A CD1 1 
ATOM   2732 C  CD2 . PHE A 1 397 ? 20.405  -11.449 -10.113 1.00   54.25  ? 412 PHE A CD2 1 
ATOM   2733 C  CE1 . PHE A 1 397 ? 22.825  -12.124 -8.994  1.00   53.87  ? 412 PHE A CE1 1 
ATOM   2734 C  CE2 . PHE A 1 397 ? 20.680  -11.103 -8.803  1.00   54.02  ? 412 PHE A CE2 1 
ATOM   2735 C  CZ  . PHE A 1 397 ? 21.892  -11.447 -8.245  1.00   53.69  ? 412 PHE A CZ  1 
ATOM   2736 N  N   . ASN A 1 398 ? 23.824  -10.539 -13.276 1.00   57.24  ? 413 ASN A N   1 
ATOM   2737 C  CA  . ASN A 1 398 ? 25.260  -10.532 -13.499 1.00   58.34  ? 413 ASN A CA  1 
ATOM   2738 C  C   . ASN A 1 398 ? 26.003  -9.499  -12.643 1.00   57.18  ? 413 ASN A C   1 
ATOM   2739 O  O   . ASN A 1 398 ? 26.384  -8.440  -13.129 1.00   56.95  ? 413 ASN A O   1 
ATOM   2740 C  CB  . ASN A 1 398 ? 25.507  -10.306 -14.984 1.00   59.08  ? 413 ASN A CB  1 
ATOM   2741 C  CG  . ASN A 1 398 ? 26.932  -10.541 -15.362 1.00   61.71  ? 413 ASN A CG  1 
ATOM   2742 O  OD1 . ASN A 1 398 ? 27.847  -10.208 -14.604 1.00   62.35  ? 413 ASN A OD1 1 
ATOM   2743 N  ND2 . ASN A 1 398 ? 27.144  -11.125 -16.528 1.00   65.37  ? 413 ASN A ND2 1 
ATOM   2744 N  N   . PRO A 1 399 ? 26.241  -9.821  -11.371 1.00   56.43  ? 414 PRO A N   1 
ATOM   2745 C  CA  . PRO A 1 399 ? 26.823  -8.860  -10.434 1.00   57.07  ? 414 PRO A CA  1 
ATOM   2746 C  C   . PRO A 1 399 ? 28.103  -8.254  -10.956 1.00   57.70  ? 414 PRO A C   1 
ATOM   2747 O  O   . PRO A 1 399 ? 28.408  -7.110  -10.647 1.00   55.97  ? 414 PRO A O   1 
ATOM   2748 C  CB  . PRO A 1 399 ? 27.136  -9.708  -9.199  1.00   58.31  ? 414 PRO A CB  1 
ATOM   2749 C  CG  . PRO A 1 399 ? 26.272  -10.918 -9.337  1.00   58.63  ? 414 PRO A CG  1 
ATOM   2750 C  CD  . PRO A 1 399 ? 26.194  -11.175 -10.810 1.00   57.94  ? 414 PRO A CD  1 
ATOM   2751 N  N   . GLU A 1 400 ? 28.822  -9.035  -11.758 1.00   59.93  ? 415 GLU A N   1 
ATOM   2752 C  CA  . GLU A 1 400 ? 30.033  -8.588  -12.452 1.00   61.07  ? 415 GLU A CA  1 
ATOM   2753 C  C   . GLU A 1 400 ? 29.882  -7.307  -13.284 1.00   56.32  ? 415 GLU A C   1 
ATOM   2754 O  O   . GLU A 1 400 ? 30.862  -6.637  -13.536 1.00   53.60  ? 415 GLU A O   1 
ATOM   2755 C  CB  . GLU A 1 400 ? 30.586  -9.726  -13.328 1.00   66.97  ? 415 GLU A CB  1 
ATOM   2756 C  CG  . GLU A 1 400 ? 31.011  -10.967 -12.529 1.00   71.18  ? 415 GLU A CG  1 
ATOM   2757 C  CD  . GLU A 1 400 ? 30.294  -12.255 -12.948 1.00   76.40  ? 415 GLU A CD  1 
ATOM   2758 O  OE1 . GLU A 1 400 ? 29.098  -12.210 -13.340 1.00   76.96  ? 415 GLU A OE1 1 
ATOM   2759 O  OE2 . GLU A 1 400 ? 30.931  -13.331 -12.856 1.00   81.14  ? 415 GLU A OE2 1 
ATOM   2760 N  N   . ARG A 1 401 ? 28.665  -6.949  -13.686 1.00   54.39  ? 416 ARG A N   1 
ATOM   2761 C  CA  . ARG A 1 401 ? 28.443  -5.668  -14.391 1.00   52.28  ? 416 ARG A CA  1 
ATOM   2762 C  C   . ARG A 1 401 ? 28.668  -4.455  -13.487 1.00   51.87  ? 416 ARG A C   1 
ATOM   2763 O  O   . ARG A 1 401 ? 28.866  -3.367  -13.991 1.00   52.98  ? 416 ARG A O   1 
ATOM   2764 C  CB  . ARG A 1 401 ? 27.055  -5.587  -15.016 1.00   49.70  ? 416 ARG A CB  1 
ATOM   2765 C  CG  . ARG A 1 401 ? 26.027  -4.790  -14.212 1.00   48.42  ? 416 ARG A CG  1 
ATOM   2766 C  CD  . ARG A 1 401 ? 24.651  -5.398  -14.370 1.00   47.74  ? 416 ARG A CD  1 
ATOM   2767 N  NE  . ARG A 1 401 ? 24.329  -5.525  -15.791 1.00   48.51  ? 416 ARG A NE  1 
ATOM   2768 C  CZ  . ARG A 1 401 ? 23.645  -6.522  -16.343 1.00   48.24  ? 416 ARG A CZ  1 
ATOM   2769 N  NH1 . ARG A 1 401 ? 23.155  -7.540  -15.638 1.00   47.41  ? 416 ARG A NH1 1 
ATOM   2770 N  NH2 . ARG A 1 401 ? 23.450  -6.491  -17.637 1.00   50.02  ? 416 ARG A NH2 1 
ATOM   2771 N  N   . PHE A 1 402 ? 28.593  -4.631  -12.168 1.00   50.82  ? 417 PHE A N   1 
ATOM   2772 C  CA  . PHE A 1 402 ? 28.904  -3.549  -11.230 1.00   50.99  ? 417 PHE A CA  1 
ATOM   2773 C  C   . PHE A 1 402 ? 30.382  -3.591  -10.806 1.00   54.65  ? 417 PHE A C   1 
ATOM   2774 O  O   . PHE A 1 402 ? 30.820  -2.772  -10.012 1.00   54.48  ? 417 PHE A O   1 
ATOM   2775 C  CB  . PHE A 1 402 ? 27.979  -3.618  -10.003 1.00   48.35  ? 417 PHE A CB  1 
ATOM   2776 C  CG  . PHE A 1 402 ? 26.592  -3.135  -10.275 1.00   45.78  ? 417 PHE A CG  1 
ATOM   2777 C  CD1 . PHE A 1 402 ? 26.315  -1.780  -10.302 1.00   44.31  ? 417 PHE A CD1 1 
ATOM   2778 C  CD2 . PHE A 1 402 ? 25.565  -4.030  -10.549 1.00   45.97  ? 417 PHE A CD2 1 
ATOM   2779 C  CE1 . PHE A 1 402 ? 25.047  -1.314  -10.598 1.00   42.70  ? 417 PHE A CE1 1 
ATOM   2780 C  CE2 . PHE A 1 402 ? 24.282  -3.573  -10.843 1.00   44.03  ? 417 PHE A CE2 1 
ATOM   2781 C  CZ  . PHE A 1 402 ? 24.029  -2.212  -10.868 1.00   42.98  ? 417 PHE A CZ  1 
ATOM   2782 N  N   . LEU A 1 403 ? 31.135  -4.550  -11.343 1.00   59.08  ? 418 LEU A N   1 
ATOM   2783 C  CA  . LEU A 1 403 ? 32.564  -4.671  -11.097 1.00   62.53  ? 418 LEU A CA  1 
ATOM   2784 C  C   . LEU A 1 403 ? 33.396  -4.149  -12.264 1.00   70.59  ? 418 LEU A C   1 
ATOM   2785 O  O   . LEU A 1 403 ? 33.355  -4.671  -13.394 1.00   70.41  ? 418 LEU A O   1 
ATOM   2786 C  CB  . LEU A 1 403 ? 32.936  -6.132  -10.875 1.00   61.98  ? 418 LEU A CB  1 
ATOM   2787 C  CG  . LEU A 1 403 ? 32.366  -6.805  -9.647  1.00   60.37  ? 418 LEU A CG  1 
ATOM   2788 C  CD1 . LEU A 1 403 ? 32.693  -8.290  -9.669  1.00   60.93  ? 418 LEU A CD1 1 
ATOM   2789 C  CD2 . LEU A 1 403 ? 32.926  -6.122  -8.413  1.00   59.80  ? 418 LEU A CD2 1 
ATOM   2790 N  N   . GLU A 1 404 ? 34.168  -3.114  -11.979 1.00   79.74  ? 419 GLU A N   1 
ATOM   2791 C  CA  . GLU A 1 404 ? 35.306  -2.784  -12.818 1.00   88.96  ? 419 GLU A CA  1 
ATOM   2792 C  C   . GLU A 1 404 ? 36.282  -1.946  -12.011 1.00   89.87  ? 419 GLU A C   1 
ATOM   2793 O  O   . GLU A 1 404 ? 37.019  -2.488  -11.191 1.00   95.32  ? 419 GLU A O   1 
ATOM   2794 C  CB  . GLU A 1 404 ? 34.870  -2.045  -14.084 1.00   94.33  ? 419 GLU A CB  1 
ATOM   2795 C  CG  . GLU A 1 404 ? 36.012  -1.830  -15.071 1.00   100.50 ? 419 GLU A CG  1 
ATOM   2796 C  CD  . GLU A 1 404 ? 36.499  -0.386  -15.111 1.00   103.45 ? 419 GLU A CD  1 
ATOM   2797 O  OE1 . GLU A 1 404 ? 36.749  0.113   -16.231 1.00   115.36 ? 419 GLU A OE1 1 
ATOM   2798 O  OE2 . GLU A 1 404 ? 36.629  0.255   -14.043 1.00   100.36 ? 419 GLU A OE2 1 
ATOM   2799 N  N   . SER A 1 413 ? 25.674  4.703   -13.994 1.00   64.62  ? 428 SER A N   1 
ATOM   2800 C  CA  . SER A 1 413 ? 25.284  5.923   -14.719 1.00   65.44  ? 428 SER A CA  1 
ATOM   2801 C  C   . SER A 1 413 ? 23.769  6.132   -14.725 1.00   63.86  ? 428 SER A C   1 
ATOM   2802 O  O   . SER A 1 413 ? 23.318  7.187   -14.299 1.00   67.94  ? 428 SER A O   1 
ATOM   2803 C  CB  . SER A 1 413 ? 25.799  5.912   -16.162 1.00   67.18  ? 428 SER A CB  1 
ATOM   2804 O  OG  . SER A 1 413 ? 24.814  5.427   -17.055 1.00   65.50  ? 428 SER A OG  1 
ATOM   2805 N  N   . SER A 1 414 ? 22.994  5.151   -15.216 1.00   57.30  ? 429 SER A N   1 
ATOM   2806 C  CA  . SER A 1 414 ? 21.522  5.205   -15.120 1.00   52.09  ? 429 SER A CA  1 
ATOM   2807 C  C   . SER A 1 414 ? 20.990  4.237   -14.046 1.00   49.57  ? 429 SER A C   1 
ATOM   2808 O  O   . SER A 1 414 ? 19.929  3.636   -14.187 1.00   48.97  ? 429 SER A O   1 
ATOM   2809 C  CB  . SER A 1 414 ? 20.851  4.979   -16.499 1.00   51.83  ? 429 SER A CB  1 
ATOM   2810 O  OG  . SER A 1 414 ? 20.827  3.631   -16.892 1.00   51.00  ? 429 SER A OG  1 
ATOM   2811 N  N   . PHE A 1 415 ? 21.749  4.110   -12.958 1.00   48.77  ? 430 PHE A N   1 
ATOM   2812 C  CA  . PHE A 1 415 ? 21.384  3.303   -11.772 1.00   44.60  ? 430 PHE A CA  1 
ATOM   2813 C  C   . PHE A 1 415 ? 20.896  4.265   -10.701 1.00   41.06  ? 430 PHE A C   1 
ATOM   2814 O  O   . PHE A 1 415 ? 21.661  5.083   -10.212 1.00   40.88  ? 430 PHE A O   1 
ATOM   2815 C  CB  . PHE A 1 415 ? 22.641  2.566   -11.286 1.00   44.69  ? 430 PHE A CB  1 
ATOM   2816 C  CG  . PHE A 1 415 ? 22.404  1.550   -10.196 1.00   42.23  ? 430 PHE A CG  1 
ATOM   2817 C  CD1 . PHE A 1 415 ? 21.471  0.541   -10.346 1.00   41.24  ? 430 PHE A CD1 1 
ATOM   2818 C  CD2 . PHE A 1 415 ? 23.176  1.573   -9.055  1.00   41.53  ? 430 PHE A CD2 1 
ATOM   2819 C  CE1 . PHE A 1 415 ? 21.283  -0.404  -9.363  1.00   40.09  ? 430 PHE A CE1 1 
ATOM   2820 C  CE2 . PHE A 1 415 ? 23.001  0.630   -8.063  1.00   40.79  ? 430 PHE A CE2 1 
ATOM   2821 C  CZ  . PHE A 1 415 ? 22.066  -0.370  -8.229  1.00   40.54  ? 430 PHE A CZ  1 
ATOM   2822 N  N   . LEU A 1 416 ? 19.612  4.206   -10.390 1.00   39.36  ? 431 LEU A N   1 
ATOM   2823 C  CA  . LEU A 1 416 ? 19.001  5.016   -9.328  1.00   37.56  ? 431 LEU A CA  1 
ATOM   2824 C  C   . LEU A 1 416 ? 18.073  4.205   -8.458  1.00   36.39  ? 431 LEU A C   1 
ATOM   2825 O  O   . LEU A 1 416 ? 16.899  4.509   -8.398  1.00   36.42  ? 431 LEU A O   1 
ATOM   2826 C  CB  . LEU A 1 416 ? 18.219  6.177   -9.930  1.00   37.02  ? 431 LEU A CB  1 
ATOM   2827 C  CG  . LEU A 1 416 ? 19.077  7.154   -10.723 1.00   37.89  ? 431 LEU A CG  1 
ATOM   2828 C  CD1 . LEU A 1 416 ? 18.220  8.006   -11.657 1.00   37.86  ? 431 LEU A CD1 1 
ATOM   2829 C  CD2 . LEU A 1 416 ? 19.891  8.009   -9.748  1.00   38.26  ? 431 LEU A CD2 1 
ATOM   2830 N  N   . PRO A 1 417 ? 18.602  3.189   -7.751  1.00   36.98  ? 432 PRO A N   1 
ATOM   2831 C  CA  . PRO A 1 417 ? 17.799  2.355   -6.838  1.00   36.30  ? 432 PRO A CA  1 
ATOM   2832 C  C   . PRO A 1 417 ? 17.077  3.129   -5.761  1.00   34.57  ? 432 PRO A C   1 
ATOM   2833 O  O   . PRO A 1 417 ? 15.994  2.703   -5.331  1.00   35.61  ? 432 PRO A O   1 
ATOM   2834 C  CB  . PRO A 1 417 ? 18.823  1.410   -6.195  1.00   36.68  ? 432 PRO A CB  1 
ATOM   2835 C  CG  . PRO A 1 417 ? 20.124  2.099   -6.379  1.00   38.04  ? 432 PRO A CG  1 
ATOM   2836 C  CD  . PRO A 1 417 ? 20.019  2.800   -7.709  1.00   38.02  ? 432 PRO A CD  1 
ATOM   2837 N  N   . PHE A 1 418 ? 17.630  4.261   -5.363  1.00   32.91  ? 433 PHE A N   1 
ATOM   2838 C  CA  . PHE A 1 418 ? 16.989  5.067   -4.347  1.00   32.68  ? 433 PHE A CA  1 
ATOM   2839 C  C   . PHE A 1 418 ? 16.329  6.364   -4.848  1.00   32.08  ? 433 PHE A C   1 
ATOM   2840 O  O   . PHE A 1 418 ? 16.093  7.274   -4.088  1.00   32.05  ? 433 PHE A O   1 
ATOM   2841 C  CB  . PHE A 1 418 ? 18.030  5.358   -3.243  1.00   33.34  ? 433 PHE A CB  1 
ATOM   2842 C  CG  . PHE A 1 418 ? 18.482  4.128   -2.513  1.00   33.30  ? 433 PHE A CG  1 
ATOM   2843 C  CD1 . PHE A 1 418 ? 17.726  3.613   -1.463  1.00   32.81  ? 433 PHE A CD1 1 
ATOM   2844 C  CD2 . PHE A 1 418 ? 19.613  3.440   -2.919  1.00   33.45  ? 433 PHE A CD2 1 
ATOM   2845 C  CE1 . PHE A 1 418 ? 18.123  2.457   -0.812  1.00   33.00  ? 433 PHE A CE1 1 
ATOM   2846 C  CE2 . PHE A 1 418 ? 20.028  2.295   -2.246  1.00   33.82  ? 433 PHE A CE2 1 
ATOM   2847 C  CZ  . PHE A 1 418 ? 19.291  1.807   -1.188  1.00   33.15  ? 433 PHE A CZ  1 
ATOM   2848 N  N   . GLY A 1 419 ? 16.000  6.464   -6.119  1.00   31.98  ? 434 GLY A N   1 
ATOM   2849 C  CA  . GLY A 1 419 ? 15.676  7.778   -6.667  1.00   31.74  ? 434 GLY A CA  1 
ATOM   2850 C  C   . GLY A 1 419 ? 16.872  8.748   -6.623  1.00   31.97  ? 434 GLY A C   1 
ATOM   2851 O  O   . GLY A 1 419 ? 18.020  8.351   -6.753  1.00   31.85  ? 434 GLY A O   1 
ATOM   2852 N  N   . ALA A 1 420 ? 16.579  10.033  -6.457  1.00   31.85  ? 435 ALA A N   1 
ATOM   2853 C  CA  . ALA A 1 420 ? 17.578  11.087  -6.452  1.00   31.60  ? 435 ALA A CA  1 
ATOM   2854 C  C   . ALA A 1 420 ? 16.824  12.417  -6.384  1.00   31.19  ? 435 ALA A C   1 
ATOM   2855 O  O   . ALA A 1 420 ? 15.594  12.418  -6.374  1.00   32.20  ? 435 ALA A O   1 
ATOM   2856 C  CB  . ALA A 1 420 ? 18.405  11.006  -7.708  1.00   32.38  ? 435 ALA A CB  1 
ATOM   2857 N  N   . GLY A 1 421 ? 17.546  13.530  -6.317  1.00   30.86  ? 436 GLY A N   1 
ATOM   2858 C  CA  . GLY A 1 421 ? 16.946  14.853  -6.267  1.00   30.88  ? 436 GLY A CA  1 
ATOM   2859 C  C   . GLY A 1 421 ? 16.214  15.132  -4.981  1.00   30.76  ? 436 GLY A C   1 
ATOM   2860 O  O   . GLY A 1 421 ? 16.276  14.336  -4.043  1.00   31.23  ? 436 GLY A O   1 
ATOM   2861 N  N   . PRO A 1 422 ? 15.476  16.239  -4.911  1.00   30.93  ? 437 PRO A N   1 
ATOM   2862 C  CA  . PRO A 1 422 ? 14.877  16.536  -3.621  1.00   31.50  ? 437 PRO A CA  1 
ATOM   2863 C  C   . PRO A 1 422 ? 14.145  15.376  -2.922  1.00   31.66  ? 437 PRO A C   1 
ATOM   2864 O  O   . PRO A 1 422 ? 14.122  15.339  -1.709  1.00   32.88  ? 437 PRO A O   1 
ATOM   2865 C  CB  . PRO A 1 422 ? 13.902  17.673  -3.946  1.00   31.69  ? 437 PRO A CB  1 
ATOM   2866 C  CG  . PRO A 1 422 ? 14.417  18.276  -5.212  1.00   31.79  ? 437 PRO A CG  1 
ATOM   2867 C  CD  . PRO A 1 422 ? 14.947  17.108  -5.965  1.00   31.43  ? 437 PRO A CD  1 
ATOM   2868 N  N   . ARG A 1 423 ? 13.609  14.422  -3.674  1.00   31.87  ? 438 ARG A N   1 
ATOM   2869 C  CA  . ARG A 1 423 ? 12.744  13.370  -3.131  1.00   31.82  ? 438 ARG A CA  1 
ATOM   2870 C  C   . ARG A 1 423 ? 13.421  12.031  -2.945  1.00   30.50  ? 438 ARG A C   1 
ATOM   2871 O  O   . ARG A 1 423 ? 12.741  11.028  -2.777  1.00   28.96  ? 438 ARG A O   1 
ATOM   2872 C  CB  . ARG A 1 423 ? 11.535  13.177  -4.102  1.00   33.14  ? 438 ARG A CB  1 
ATOM   2873 C  CG  . ARG A 1 423 ? 10.472  14.260  -3.976  1.00   34.46  ? 438 ARG A CG  1 
ATOM   2874 C  CD  . ARG A 1 423 ? 9.854   14.068  -2.595  1.00   35.40  ? 438 ARG A CD  1 
ATOM   2875 N  NE  . ARG A 1 423 ? 9.042   15.155  -2.104  1.00   36.68  ? 438 ARG A NE  1 
ATOM   2876 C  CZ  . ARG A 1 423 ? 8.149   15.018  -1.133  1.00   38.95  ? 438 ARG A CZ  1 
ATOM   2877 N  NH1 . ARG A 1 423 ? 7.946   13.832  -0.542  1.00   39.21  ? 438 ARG A NH1 1 
ATOM   2878 N  NH2 . ARG A 1 423 ? 7.455   16.083  -0.739  1.00   41.33  ? 438 ARG A NH2 1 
ATOM   2879 N  N   . VAL A 1 424 ? 14.743  12.011  -3.051  1.00   30.61  ? 439 VAL A N   1 
ATOM   2880 C  CA  . VAL A 1 424 ? 15.575  10.804  -2.813  1.00   31.13  ? 439 VAL A CA  1 
ATOM   2881 C  C   . VAL A 1 424 ? 15.312  10.068  -1.501  1.00   31.04  ? 439 VAL A C   1 
ATOM   2882 O  O   . VAL A 1 424 ? 14.922  10.668  -0.502  1.00   31.53  ? 439 VAL A O   1 
ATOM   2883 C  CB  . VAL A 1 424 ? 17.092  11.188  -2.819  1.00   31.72  ? 439 VAL A CB  1 
ATOM   2884 C  CG1 . VAL A 1 424 ? 17.407  12.172  -1.708  1.00   31.68  ? 439 VAL A CG1 1 
ATOM   2885 C  CG2 . VAL A 1 424 ? 17.993  9.959   -2.743  1.00   31.41  ? 439 VAL A CG2 1 
ATOM   2886 N  N   . CYS A 1 425 ? 15.556  8.772   -1.485  1.00   31.48  ? 440 CYS A N   1 
ATOM   2887 C  CA  . CYS A 1 425 ? 15.250  8.002   -0.299  1.00   33.19  ? 440 CYS A CA  1 
ATOM   2888 C  C   . CYS A 1 425 ? 15.889  8.616   0.940   1.00   34.79  ? 440 CYS A C   1 
ATOM   2889 O  O   . CYS A 1 425 ? 17.079  8.912   0.945   1.00   36.12  ? 440 CYS A O   1 
ATOM   2890 C  CB  . CYS A 1 425 ? 15.729  6.582   -0.467  1.00   33.49  ? 440 CYS A CB  1 
ATOM   2891 S  SG  . CYS A 1 425 ? 15.174  5.503   0.865   1.00   35.14  ? 440 CYS A SG  1 
ATOM   2892 N  N   . VAL A 1 426 ? 15.097  8.862   1.970   1.00   37.02  ? 441 VAL A N   1 
ATOM   2893 C  CA  . VAL A 1 426 ? 15.665  9.342   3.247   1.00   39.60  ? 441 VAL A CA  1 
ATOM   2894 C  C   . VAL A 1 426 ? 16.253  8.226   4.112   1.00   37.98  ? 441 VAL A C   1 
ATOM   2895 O  O   . VAL A 1 426 ? 16.936  8.537   5.061   1.00   38.44  ? 441 VAL A O   1 
ATOM   2896 C  CB  . VAL A 1 426 ? 14.669  10.136  4.127   1.00   42.10  ? 441 VAL A CB  1 
ATOM   2897 C  CG1 . VAL A 1 426 ? 14.297  11.423  3.442   1.00   43.59  ? 441 VAL A CG1 1 
ATOM   2898 C  CG2 . VAL A 1 426 ? 13.410  9.340   4.403   1.00   42.62  ? 441 VAL A CG2 1 
ATOM   2899 N  N   . GLY A 1 427 ? 15.993  6.960   3.769   1.00   36.27  ? 442 GLY A N   1 
ATOM   2900 C  CA  . GLY A 1 427 ? 16.494  5.799   4.509   1.00   35.59  ? 442 GLY A CA  1 
ATOM   2901 C  C   . GLY A 1 427 ? 17.482  4.956   3.731   1.00   35.87  ? 442 GLY A C   1 
ATOM   2902 O  O   . GLY A 1 427 ? 17.598  3.749   3.974   1.00   33.99  ? 442 GLY A O   1 
ATOM   2903 N  N   . GLU A 1 428 ? 18.191  5.600   2.796   1.00   37.19  ? 443 GLU A N   1 
ATOM   2904 C  CA  . GLU A 1 428 ? 19.149  4.932   1.914   1.00   38.34  ? 443 GLU A CA  1 
ATOM   2905 C  C   . GLU A 1 428 ? 20.350  4.421   2.668   1.00   39.86  ? 443 GLU A C   1 
ATOM   2906 O  O   . GLU A 1 428 ? 20.728  3.272   2.515   1.00   38.92  ? 443 GLU A O   1 
ATOM   2907 C  CB  . GLU A 1 428 ? 19.627  5.891   0.824   1.00   39.97  ? 443 GLU A CB  1 
ATOM   2908 C  CG  . GLU A 1 428 ? 20.647  5.311   -0.164  1.00   41.10  ? 443 GLU A CG  1 
ATOM   2909 C  CD  . GLU A 1 428 ? 21.058  6.322   -1.215  1.00   42.66  ? 443 GLU A CD  1 
ATOM   2910 O  OE1 . GLU A 1 428 ? 20.632  7.502   -1.126  1.00   43.75  ? 443 GLU A OE1 1 
ATOM   2911 O  OE2 . GLU A 1 428 ? 21.815  5.948   -2.133  1.00   44.76  ? 443 GLU A OE2 1 
ATOM   2912 N  N   . SER A 1 429 ? 20.972  5.296   3.445   1.00   43.69  ? 444 SER A N   1 
ATOM   2913 C  CA  . SER A 1 429 ? 22.072  4.910   4.319   1.00   48.63  ? 444 SER A CA  1 
ATOM   2914 C  C   . SER A 1 429 ? 21.647  3.783   5.264   1.00   49.08  ? 444 SER A C   1 
ATOM   2915 O  O   . SER A 1 429 ? 22.381  2.821   5.516   1.00   52.08  ? 444 SER A O   1 
ATOM   2916 C  CB  . SER A 1 429 ? 22.539  6.105   5.143   1.00   51.19  ? 444 SER A CB  1 
ATOM   2917 O  OG  . SER A 1 429 ? 22.924  7.171   4.297   1.00   56.48  ? 444 SER A OG  1 
ATOM   2918 N  N   . LEU A 1 430 ? 20.452  3.888   5.784   1.00   46.54  ? 445 LEU A N   1 
ATOM   2919 C  CA  . LEU A 1 430 ? 20.013  2.870   6.688   1.00   47.57  ? 445 LEU A CA  1 
ATOM   2920 C  C   . LEU A 1 430 ? 19.760  1.556   5.965   1.00   43.75  ? 445 LEU A C   1 
ATOM   2921 O  O   . LEU A 1 430 ? 20.083  0.477   6.462   1.00   44.42  ? 445 LEU A O   1 
ATOM   2922 C  CB  . LEU A 1 430 ? 18.768  3.354   7.387   1.00   49.81  ? 445 LEU A CB  1 
ATOM   2923 C  CG  . LEU A 1 430 ? 18.362  2.389   8.461   1.00   54.44  ? 445 LEU A CG  1 
ATOM   2924 C  CD1 . LEU A 1 430 ? 17.712  3.198   9.554   1.00   58.52  ? 445 LEU A CD1 1 
ATOM   2925 C  CD2 . LEU A 1 430 ? 17.391  1.352   7.933   1.00   56.44  ? 445 LEU A CD2 1 
ATOM   2926 N  N   . ALA A 1 431 ? 19.149  1.658   4.801   1.00   41.12  ? 446 ALA A N   1 
ATOM   2927 C  CA  . ALA A 1 431 ? 18.831  0.500   3.975   1.00   39.51  ? 446 ALA A CA  1 
ATOM   2928 C  C   . ALA A 1 431 ? 20.079  -0.293  3.623   1.00   38.50  ? 446 ALA A C   1 
ATOM   2929 O  O   . ALA A 1 431 ? 20.165  -1.502  3.844   1.00   37.32  ? 446 ALA A O   1 
ATOM   2930 C  CB  . ALA A 1 431 ? 18.153  0.971   2.694   1.00   39.23  ? 446 ALA A CB  1 
ATOM   2931 N  N   . ARG A 1 432 ? 21.038  0.424   3.062   1.00   38.46  ? 447 ARG A N   1 
ATOM   2932 C  CA  . ARG A 1 432 ? 22.297  -0.139  2.590   1.00   39.23  ? 447 ARG A CA  1 
ATOM   2933 C  C   . ARG A 1 432 ? 23.052  -0.891  3.677   1.00   39.05  ? 447 ARG A C   1 
ATOM   2934 O  O   . ARG A 1 432 ? 23.475  -2.032  3.494   1.00   39.90  ? 447 ARG A O   1 
ATOM   2935 C  CB  . ARG A 1 432 ? 23.152  0.991   2.063   1.00   40.87  ? 447 ARG A CB  1 
ATOM   2936 C  CG  . ARG A 1 432 ? 22.663  1.500   0.731   1.00   42.07  ? 447 ARG A CG  1 
ATOM   2937 C  CD  . ARG A 1 432 ? 23.524  2.639   0.257   1.00   45.20  ? 447 ARG A CD  1 
ATOM   2938 N  NE  . ARG A 1 432 ? 23.177  2.949   -1.121  1.00   49.76  ? 447 ARG A NE  1 
ATOM   2939 C  CZ  . ARG A 1 432 ? 23.595  2.268   -2.186  1.00   49.39  ? 447 ARG A CZ  1 
ATOM   2940 N  NH1 . ARG A 1 432 ? 24.431  1.225   -2.050  1.00   51.26  ? 447 ARG A NH1 1 
ATOM   2941 N  NH2 . ARG A 1 432 ? 23.166  2.649   -3.387  1.00   46.79  ? 447 ARG A NH2 1 
ATOM   2942 N  N   . ILE A 1 433 ? 23.200  -0.229  4.814   1.00   37.66  ? 448 ILE A N   1 
ATOM   2943 C  CA  . ILE A 1 433 ? 23.712  -0.838  6.024   1.00   36.66  ? 448 ILE A CA  1 
ATOM   2944 C  C   . ILE A 1 433 ? 22.885  -2.049  6.474   1.00   36.15  ? 448 ILE A C   1 
ATOM   2945 O  O   . ILE A 1 433 ? 23.420  -3.111  6.727   1.00   36.06  ? 448 ILE A O   1 
ATOM   2946 C  CB  . ILE A 1 433 ? 23.727  0.217   7.119   1.00   36.48  ? 448 ILE A CB  1 
ATOM   2947 C  CG1 . ILE A 1 433 ? 24.922  1.135   6.912   1.00   36.60  ? 448 ILE A CG1 1 
ATOM   2948 C  CG2 . ILE A 1 433 ? 23.789  -0.440  8.469   1.00   37.77  ? 448 ILE A CG2 1 
ATOM   2949 C  CD1 . ILE A 1 433 ? 24.766  2.464   7.612   1.00   37.02  ? 448 ILE A CD1 1 
ATOM   2950 N  N   . GLU A 1 434 ? 21.576  -1.899  6.580   1.00   36.15  ? 449 GLU A N   1 
ATOM   2951 C  CA  . GLU A 1 434 ? 20.736  -3.060  6.848   1.00   36.48  ? 449 GLU A CA  1 
ATOM   2952 C  C   . GLU A 1 434 ? 21.119  -4.226  5.896   1.00   35.97  ? 449 GLU A C   1 
ATOM   2953 O  O   . GLU A 1 434 ? 21.494  -5.304  6.338   1.00   34.55  ? 449 GLU A O   1 
ATOM   2954 C  CB  . GLU A 1 434 ? 19.258  -2.682  6.717   1.00   36.83  ? 449 GLU A CB  1 
ATOM   2955 C  CG  . GLU A 1 434 ? 18.365  -3.039  7.900   1.00   38.42  ? 449 GLU A CG  1 
ATOM   2956 C  CD  . GLU A 1 434 ? 16.882  -2.568  7.746   1.00   39.39  ? 449 GLU A CD  1 
ATOM   2957 O  OE1 . GLU A 1 434 ? 16.566  -1.653  6.931   1.00   38.43  ? 449 GLU A OE1 1 
ATOM   2958 O  OE2 . GLU A 1 434 ? 15.999  -3.124  8.463   1.00   40.78  ? 449 GLU A OE2 1 
ATOM   2959 N  N   . LEU A 1 435 ? 21.071  -4.003  4.585   1.00   36.20  ? 450 LEU A N   1 
ATOM   2960 C  CA  . LEU A 1 435 ? 21.224  -5.137  3.642   1.00   37.37  ? 450 LEU A CA  1 
ATOM   2961 C  C   . LEU A 1 435 ? 22.635  -5.682  3.636   1.00   38.57  ? 450 LEU A C   1 
ATOM   2962 O  O   . LEU A 1 435 ? 22.851  -6.876  3.475   1.00   38.81  ? 450 LEU A O   1 
ATOM   2963 C  CB  . LEU A 1 435 ? 20.868  -4.759  2.210   1.00   37.08  ? 450 LEU A CB  1 
ATOM   2964 C  CG  . LEU A 1 435 ? 19.462  -4.251  1.932   1.00   36.79  ? 450 LEU A CG  1 
ATOM   2965 C  CD1 . LEU A 1 435 ? 19.499  -3.447  0.639   1.00   37.03  ? 450 LEU A CD1 1 
ATOM   2966 C  CD2 . LEU A 1 435 ? 18.476  -5.399  1.833   1.00   36.92  ? 450 LEU A CD2 1 
ATOM   2967 N  N   . PHE A 1 436 ? 23.615  -4.810  3.800   1.00   38.81  ? 451 PHE A N   1 
ATOM   2968 C  CA  . PHE A 1 436 ? 24.958  -5.310  3.854   1.00   39.18  ? 451 PHE A CA  1 
ATOM   2969 C  C   . PHE A 1 436 ? 25.081  -6.248  5.040   1.00   38.23  ? 451 PHE A C   1 
ATOM   2970 O  O   . PHE A 1 436 ? 25.430  -7.422  4.875   1.00   37.75  ? 451 PHE A O   1 
ATOM   2971 C  CB  . PHE A 1 436 ? 25.974  -4.190  3.935   1.00   40.59  ? 451 PHE A CB  1 
ATOM   2972 C  CG  . PHE A 1 436 ? 27.345  -4.681  4.247   1.00   43.27  ? 451 PHE A CG  1 
ATOM   2973 C  CD1 . PHE A 1 436 ? 28.124  -5.236  3.265   1.00   44.21  ? 451 PHE A CD1 1 
ATOM   2974 C  CD2 . PHE A 1 436 ? 27.825  -4.638  5.547   1.00   43.64  ? 451 PHE A CD2 1 
ATOM   2975 C  CE1 . PHE A 1 436 ? 29.384  -5.718  3.566   1.00   46.23  ? 451 PHE A CE1 1 
ATOM   2976 C  CE2 . PHE A 1 436 ? 29.066  -5.107  5.859   1.00   45.22  ? 451 PHE A CE2 1 
ATOM   2977 C  CZ  . PHE A 1 436 ? 29.857  -5.647  4.870   1.00   47.26  ? 451 PHE A CZ  1 
ATOM   2978 N  N   . LEU A 1 437 ? 24.768  -5.719  6.224   1.00   37.45  ? 452 LEU A N   1 
ATOM   2979 C  CA  . LEU A 1 437 ? 24.964  -6.441  7.484   1.00   37.35  ? 452 LEU A CA  1 
ATOM   2980 C  C   . LEU A 1 437 ? 24.140  -7.712  7.484   1.00   38.06  ? 452 LEU A C   1 
ATOM   2981 O  O   . LEU A 1 437 ? 24.623  -8.771  7.805   1.00   39.04  ? 452 LEU A O   1 
ATOM   2982 C  CB  . LEU A 1 437 ? 24.587  -5.562  8.676   1.00   36.89  ? 452 LEU A CB  1 
ATOM   2983 C  CG  . LEU A 1 437 ? 25.624  -4.809  9.538   1.00   37.42  ? 452 LEU A CG  1 
ATOM   2984 C  CD1 . LEU A 1 437 ? 26.938  -4.582  8.835   1.00   38.28  ? 452 LEU A CD1 1 
ATOM   2985 C  CD2 . LEU A 1 437 ? 25.100  -3.492  10.073  1.00   36.68  ? 452 LEU A CD2 1 
ATOM   2986 N  N   . PHE A 1 438 ? 22.888  -7.626  7.079   1.00   39.35  ? 453 PHE A N   1 
ATOM   2987 C  CA  . PHE A 1 438 ? 22.057  -8.819  7.090   1.00   40.41  ? 453 PHE A CA  1 
ATOM   2988 C  C   . PHE A 1 438 ? 22.604  -9.892  6.191   1.00   41.95  ? 453 PHE A C   1 
ATOM   2989 O  O   . PHE A 1 438 ? 22.485  -11.039 6.540   1.00   43.28  ? 453 PHE A O   1 
ATOM   2990 C  CB  . PHE A 1 438 ? 20.612  -8.555  6.638   1.00   39.09  ? 453 PHE A CB  1 
ATOM   2991 C  CG  . PHE A 1 438 ? 19.633  -8.380  7.766   1.00   39.48  ? 453 PHE A CG  1 
ATOM   2992 C  CD1 . PHE A 1 438 ? 19.648  -9.226  8.861   1.00   39.95  ? 453 PHE A CD1 1 
ATOM   2993 C  CD2 . PHE A 1 438 ? 18.658  -7.387  7.707   1.00   39.39  ? 453 PHE A CD2 1 
ATOM   2994 C  CE1 . PHE A 1 438 ? 18.741  -9.077  9.874   1.00   40.13  ? 453 PHE A CE1 1 
ATOM   2995 C  CE2 . PHE A 1 438 ? 17.739  -7.239  8.724   1.00   39.30  ? 453 PHE A CE2 1 
ATOM   2996 C  CZ  . PHE A 1 438 ? 17.782  -8.090  9.806   1.00   39.96  ? 453 PHE A CZ  1 
ATOM   2997 N  N   . VAL A 1 439 ? 23.145  -9.532  5.027   1.00   41.65  ? 454 VAL A N   1 
ATOM   2998 C  CA  . VAL A 1 439 ? 23.372  -10.506 3.987   1.00   42.42  ? 454 VAL A CA  1 
ATOM   2999 C  C   . VAL A 1 439 ? 24.727  -11.150 4.158   1.00   45.32  ? 454 VAL A C   1 
ATOM   3000 O  O   . VAL A 1 439 ? 24.917  -12.302 3.782   1.00   46.40  ? 454 VAL A O   1 
ATOM   3001 C  CB  . VAL A 1 439 ? 23.274  -9.869  2.595   1.00   43.09  ? 454 VAL A CB  1 
ATOM   3002 C  CG1 . VAL A 1 439 ? 23.343  -10.934 1.510   1.00   44.03  ? 454 VAL A CG1 1 
ATOM   3003 C  CG2 . VAL A 1 439 ? 21.954  -9.127  2.433   1.00   42.66  ? 454 VAL A CG2 1 
ATOM   3004 N  N   . SER A 1 440 ? 25.680  -10.410 4.715   1.00   47.40  ? 455 SER A N   1 
ATOM   3005 C  CA  . SER A 1 440 ? 26.986  -10.963 4.999   1.00   48.81  ? 455 SER A CA  1 
ATOM   3006 C  C   . SER A 1 440 ? 26.887  -12.037 6.065   1.00   51.20  ? 455 SER A C   1 
ATOM   3007 O  O   . SER A 1 440 ? 27.531  -13.080 5.942   1.00   52.40  ? 455 SER A O   1 
ATOM   3008 C  CB  . SER A 1 440 ? 27.950  -9.862  5.422   1.00   49.40  ? 455 SER A CB  1 
ATOM   3009 O  OG  . SER A 1 440 ? 27.404  -9.071  6.458   1.00   49.05  ? 455 SER A OG  1 
ATOM   3010 N  N   . ARG A 1 441 ? 26.067  -11.811 7.091   1.00   53.10  ? 456 ARG A N   1 
ATOM   3011 C  CA  . ARG A 1 441 ? 25.947  -12.799 8.155   1.00   56.21  ? 456 ARG A CA  1 
ATOM   3012 C  C   . ARG A 1 441 ? 25.301  -14.115 7.747   1.00   54.64  ? 456 ARG A C   1 
ATOM   3013 O  O   . ARG A 1 441 ? 25.834  -15.160 8.101   1.00   57.35  ? 456 ARG A O   1 
ATOM   3014 C  CB  . ARG A 1 441 ? 25.255  -12.229 9.381   1.00   61.52  ? 456 ARG A CB  1 
ATOM   3015 C  CG  . ARG A 1 441 ? 25.690  -12.907 10.675  1.00   69.93  ? 456 ARG A CG  1 
ATOM   3016 C  CD  . ARG A 1 441 ? 25.851  -11.852 11.751  1.00   78.51  ? 456 ARG A CD  1 
ATOM   3017 N  NE  . ARG A 1 441 ? 26.173  -12.402 13.069  1.00   88.69  ? 456 ARG A NE  1 
ATOM   3018 C  CZ  . ARG A 1 441 ? 25.907  -11.789 14.225  1.00   96.55  ? 456 ARG A CZ  1 
ATOM   3019 N  NH1 . ARG A 1 441 ? 24.783  -11.093 14.391  1.00   97.26  ? 456 ARG A NH1 1 
ATOM   3020 N  NH2 . ARG A 1 441 ? 26.772  -11.876 15.232  1.00   101.51 ? 456 ARG A NH2 1 
ATOM   3021 N  N   . PRO A 1 442 ? 24.171  -14.100 7.011   1.00   52.62  ? 457 PRO A N   1 
ATOM   3022 C  CA  . PRO A 1 442 ? 23.585  -15.386 6.713   1.00   53.15  ? 457 PRO A CA  1 
ATOM   3023 C  C   . PRO A 1 442 ? 24.446  -16.129 5.717   1.00   52.22  ? 457 PRO A C   1 
ATOM   3024 O  O   . PRO A 1 442 ? 24.508  -17.350 5.782   1.00   54.05  ? 457 PRO A O   1 
ATOM   3025 C  CB  . PRO A 1 442 ? 22.172  -15.045 6.134   1.00   53.16  ? 457 PRO A CB  1 
ATOM   3026 C  CG  . PRO A 1 442 ? 22.014  -13.573 6.258   1.00   52.05  ? 457 PRO A CG  1 
ATOM   3027 C  CD  . PRO A 1 442 ? 23.445  -13.055 6.291   1.00   52.41  ? 457 PRO A CD  1 
ATOM   3028 N  N   . LEU A 1 443 ? 25.142  -15.426 4.831   1.00   50.82  ? 458 LEU A N   1 
ATOM   3029 C  CA  . LEU A 1 443 ? 26.008  -16.118 3.869   1.00   51.29  ? 458 LEU A CA  1 
ATOM   3030 C  C   . LEU A 1 443 ? 27.224  -16.703 4.559   1.00   51.71  ? 458 LEU A C   1 
ATOM   3031 O  O   . LEU A 1 443 ? 27.643  -17.811 4.246   1.00   54.37  ? 458 LEU A O   1 
ATOM   3032 C  CB  . LEU A 1 443 ? 26.412  -15.201 2.713   1.00   50.21  ? 458 LEU A CB  1 
ATOM   3033 C  CG  . LEU A 1 443 ? 25.236  -14.791 1.814   1.00   50.16  ? 458 LEU A CG  1 
ATOM   3034 C  CD1 . LEU A 1 443 ? 25.781  -14.027 0.612   1.00   50.59  ? 458 LEU A CD1 1 
ATOM   3035 C  CD2 . LEU A 1 443 ? 24.364  -15.969 1.364   1.00   49.92  ? 458 LEU A CD2 1 
ATOM   3036 N  N   . GLN A 1 444 ? 27.773  -15.965 5.514   1.00   51.01  ? 459 GLN A N   1 
ATOM   3037 C  CA  . GLN A 1 444 ? 28.838  -16.476 6.364   1.00   51.14  ? 459 GLN A CA  1 
ATOM   3038 C  C   . GLN A 1 444 ? 28.374  -17.677 7.176   1.00   53.21  ? 459 GLN A C   1 
ATOM   3039 O  O   . GLN A 1 444 ? 29.085  -18.639 7.279   1.00   55.62  ? 459 GLN A O   1 
ATOM   3040 C  CB  . GLN A 1 444 ? 29.335  -15.375 7.292   1.00   49.23  ? 459 GLN A CB  1 
ATOM   3041 C  CG  . GLN A 1 444 ? 30.301  -15.833 8.350   1.00   49.70  ? 459 GLN A CG  1 
ATOM   3042 C  CD  . GLN A 1 444 ? 30.516  -14.782 9.413   1.00   48.98  ? 459 GLN A CD  1 
ATOM   3043 O  OE1 . GLN A 1 444 ? 29.576  -14.361 10.082  1.00   48.82  ? 459 GLN A OE1 1 
ATOM   3044 N  NE2 . GLN A 1 444 ? 31.755  -14.361 9.586   1.00   49.32  ? 459 GLN A NE2 1 
ATOM   3045 N  N   . ARG A 1 445 ? 27.188  -17.636 7.758   1.00   55.82  ? 460 ARG A N   1 
ATOM   3046 C  CA  . ARG A 1 445 ? 26.763  -18.732 8.623   1.00   58.82  ? 460 ARG A CA  1 
ATOM   3047 C  C   . ARG A 1 445 ? 26.003  -19.843 7.902   1.00   57.70  ? 460 ARG A C   1 
ATOM   3048 O  O   . ARG A 1 445 ? 25.927  -20.946 8.426   1.00   59.56  ? 460 ARG A O   1 
ATOM   3049 C  CB  . ARG A 1 445 ? 25.934  -18.219 9.809   1.00   61.56  ? 460 ARG A CB  1 
ATOM   3050 C  CG  . ARG A 1 445 ? 26.643  -17.175 10.688  1.00   64.75  ? 460 ARG A CG  1 
ATOM   3051 C  CD  . ARG A 1 445 ? 26.446  -17.324 12.213  1.00   68.89  ? 460 ARG A CD  1 
ATOM   3052 N  NE  . ARG A 1 445 ? 25.317  -18.178 12.638  1.00   73.73  ? 460 ARG A NE  1 
ATOM   3053 C  CZ  . ARG A 1 445 ? 24.835  -18.263 13.886  1.00   77.93  ? 460 ARG A CZ  1 
ATOM   3054 N  NH1 . ARG A 1 445 ? 25.314  -17.521 14.878  1.00   79.32  ? 460 ARG A NH1 1 
ATOM   3055 N  NH2 . ARG A 1 445 ? 23.826  -19.087 14.142  1.00   81.02  ? 460 ARG A NH2 1 
ATOM   3056 N  N   . PHE A 1 446 ? 25.446  -19.572 6.723   1.00   55.96  ? 461 PHE A N   1 
ATOM   3057 C  CA  . PHE A 1 446 ? 24.561  -20.531 6.037   1.00   54.91  ? 461 PHE A CA  1 
ATOM   3058 C  C   . PHE A 1 446 ? 24.740  -20.592 4.535   1.00   53.62  ? 461 PHE A C   1 
ATOM   3059 O  O   . PHE A 1 446 ? 25.073  -19.602 3.881   1.00   51.59  ? 461 PHE A O   1 
ATOM   3060 C  CB  . PHE A 1 446 ? 23.096  -20.177 6.249   1.00   55.32  ? 461 PHE A CB  1 
ATOM   3061 C  CG  . PHE A 1 446 ? 22.686  -20.088 7.676   1.00   57.20  ? 461 PHE A CG  1 
ATOM   3062 C  CD1 . PHE A 1 446 ? 22.496  -21.234 8.419   1.00   59.64  ? 461 PHE A CD1 1 
ATOM   3063 C  CD2 . PHE A 1 446 ? 22.461  -18.860 8.269   1.00   56.77  ? 461 PHE A CD2 1 
ATOM   3064 C  CE1 . PHE A 1 446 ? 22.102  -21.157 9.734   1.00   60.51  ? 461 PHE A CE1 1 
ATOM   3065 C  CE2 . PHE A 1 446 ? 22.067  -18.775 9.582   1.00   57.01  ? 461 PHE A CE2 1 
ATOM   3066 C  CZ  . PHE A 1 446 ? 21.888  -19.926 10.316  1.00   59.24  ? 461 PHE A CZ  1 
ATOM   3067 N  N   . SER A 1 447 ? 24.438  -21.766 4.000   1.00   54.26  ? 462 SER A N   1 
ATOM   3068 C  CA  . SER A 1 447 ? 24.329  -22.008 2.570   1.00   54.05  ? 462 SER A CA  1 
ATOM   3069 C  C   . SER A 1 447 ? 22.838  -22.285 2.232   1.00   53.25  ? 462 SER A C   1 
ATOM   3070 O  O   . SER A 1 447 ? 22.165  -23.094 2.881   1.00   52.32  ? 462 SER A O   1 
ATOM   3071 C  CB  . SER A 1 447 ? 25.227  -23.199 2.195   1.00   55.63  ? 462 SER A CB  1 
ATOM   3072 O  OG  . SER A 1 447 ? 25.802  -23.070 0.904   1.00   55.67  ? 462 SER A OG  1 
ATOM   3073 N  N   . PHE A 1 448 ? 22.336  -21.587 1.218   1.00   52.71  ? 463 PHE A N   1 
ATOM   3074 C  CA  . PHE A 1 448 ? 20.924  -21.641 0.825   1.00   51.89  ? 463 PHE A CA  1 
ATOM   3075 C  C   . PHE A 1 448 ? 20.793  -22.359 -0.491  1.00   53.38  ? 463 PHE A C   1 
ATOM   3076 O  O   . PHE A 1 448 ? 21.246  -21.838 -1.506  1.00   53.07  ? 463 PHE A O   1 
ATOM   3077 C  CB  . PHE A 1 448 ? 20.379  -20.236 0.627   1.00   49.54  ? 463 PHE A CB  1 
ATOM   3078 C  CG  . PHE A 1 448 ? 20.489  -19.376 1.840   1.00   48.60  ? 463 PHE A CG  1 
ATOM   3079 C  CD1 . PHE A 1 448 ? 21.699  -18.766 2.169   1.00   48.28  ? 463 PHE A CD1 1 
ATOM   3080 C  CD2 . PHE A 1 448 ? 19.393  -19.173 2.661   1.00   47.71  ? 463 PHE A CD2 1 
ATOM   3081 C  CE1 . PHE A 1 448 ? 21.808  -17.965 3.298   1.00   47.38  ? 463 PHE A CE1 1 
ATOM   3082 C  CE2 . PHE A 1 448 ? 19.500  -18.378 3.785   1.00   47.93  ? 463 PHE A CE2 1 
ATOM   3083 C  CZ  . PHE A 1 448 ? 20.712  -17.771 4.112   1.00   46.84  ? 463 PHE A CZ  1 
ATOM   3084 N  N   . SER A 1 449 ? 20.170  -23.537 -0.482  1.00   55.50  ? 464 SER A N   1 
ATOM   3085 C  CA  . SER A 1 449 ? 19.957  -24.292 -1.705  1.00   58.11  ? 464 SER A CA  1 
ATOM   3086 C  C   . SER A 1 449 ? 18.492  -24.627 -1.900  1.00   62.19  ? 464 SER A C   1 
ATOM   3087 O  O   . SER A 1 449 ? 17.676  -24.502 -0.988  1.00   63.50  ? 464 SER A O   1 
ATOM   3088 C  CB  . SER A 1 449 ? 20.793  -25.573 -1.718  1.00   58.87  ? 464 SER A CB  1 
ATOM   3089 O  OG  . SER A 1 449 ? 20.353  -26.489 -0.736  1.00   59.52  ? 464 SER A OG  1 
ATOM   3090 N  N   . CYS A 1 450 ? 18.165  -25.054 -3.109  1.00   66.83  ? 465 CYS A N   1 
ATOM   3091 C  CA  . CYS A 1 450 ? 16.832  -25.524 -3.413  1.00   71.28  ? 465 CYS A CA  1 
ATOM   3092 C  C   . CYS A 1 450 ? 16.738  -26.951 -2.885  1.00   69.74  ? 465 CYS A C   1 
ATOM   3093 O  O   . CYS A 1 450 ? 17.707  -27.694 -2.979  1.00   70.18  ? 465 CYS A O   1 
ATOM   3094 C  CB  . CYS A 1 450 ? 16.631  -25.508 -4.920  1.00   77.91  ? 465 CYS A CB  1 
ATOM   3095 S  SG  . CYS A 1 450 ? 18.125  -26.086 -5.781  1.00   94.12  ? 465 CYS A SG  1 
ATOM   3096 N  N   . PRO A 1 451 ? 15.585  -27.341 -2.314  1.00   68.45  ? 466 PRO A N   1 
ATOM   3097 C  CA  . PRO A 1 451 ? 15.399  -28.740 -1.874  1.00   69.09  ? 466 PRO A CA  1 
ATOM   3098 C  C   . PRO A 1 451 ? 15.125  -29.734 -3.006  1.00   68.92  ? 466 PRO A C   1 
ATOM   3099 O  O   . PRO A 1 451 ? 15.859  -29.773 -3.990  1.00   66.10  ? 466 PRO A O   1 
ATOM   3100 C  CB  . PRO A 1 451 ? 14.194  -28.669 -0.930  1.00   69.10  ? 466 PRO A CB  1 
ATOM   3101 C  CG  . PRO A 1 451 ? 13.937  -27.218 -0.687  1.00   67.86  ? 466 PRO A CG  1 
ATOM   3102 C  CD  . PRO A 1 451 ? 14.509  -26.460 -1.835  1.00   67.20  ? 466 PRO A CD  1 
ATOM   3103 N  N   . SER A 1 455 ? 12.522  -27.972 -7.013  1.00   73.26  ? 470 SER A N   1 
ATOM   3104 C  CA  . SER A 1 455 ? 12.388  -27.059 -8.145  1.00   74.20  ? 470 SER A CA  1 
ATOM   3105 C  C   . SER A 1 455 ? 12.559  -25.576 -7.744  1.00   73.33  ? 470 SER A C   1 
ATOM   3106 O  O   . SER A 1 455 ? 12.037  -25.138 -6.714  1.00   72.97  ? 470 SER A O   1 
ATOM   3107 C  CB  . SER A 1 455 ? 11.039  -27.273 -8.832  1.00   74.99  ? 470 SER A CB  1 
ATOM   3108 O  OG  . SER A 1 455 ? 10.694  -26.158 -9.639  1.00   73.25  ? 470 SER A OG  1 
ATOM   3109 N  N   . LEU A 1 456 ? 13.258  -24.816 -8.598  1.00   73.60  ? 471 LEU A N   1 
ATOM   3110 C  CA  . LEU A 1 456 ? 13.727  -23.446 -8.289  1.00   71.50  ? 471 LEU A CA  1 
ATOM   3111 C  C   . LEU A 1 456 ? 12.605  -22.406 -8.276  1.00   68.99  ? 471 LEU A C   1 
ATOM   3112 O  O   . LEU A 1 456 ? 11.682  -22.478 -9.090  1.00   68.09  ? 471 LEU A O   1 
ATOM   3113 C  CB  . LEU A 1 456 ? 14.788  -22.988 -9.307  1.00   72.14  ? 471 LEU A CB  1 
ATOM   3114 C  CG  . LEU A 1 456 ? 16.147  -23.709 -9.327  1.00   73.84  ? 471 LEU A CG  1 
ATOM   3115 C  CD1 . LEU A 1 456 ? 16.851  -23.554 -10.669 1.00   74.10  ? 471 LEU A CD1 1 
ATOM   3116 C  CD2 . LEU A 1 456 ? 17.050  -23.209 -8.207  1.00   73.02  ? 471 LEU A CD2 1 
ATOM   3117 N  N   . PRO A 1 457 ? 12.706  -21.410 -7.371  1.00   65.14  ? 472 PRO A N   1 
ATOM   3118 C  CA  . PRO A 1 457 ? 11.664  -20.402 -7.250  1.00   62.03  ? 472 PRO A CA  1 
ATOM   3119 C  C   . PRO A 1 457 ? 11.484  -19.602 -8.520  1.00   60.90  ? 472 PRO A C   1 
ATOM   3120 O  O   . PRO A 1 457 ? 12.388  -19.525 -9.341  1.00   61.22  ? 472 PRO A O   1 
ATOM   3121 C  CB  . PRO A 1 457 ? 12.169  -19.499 -6.123  1.00   59.22  ? 472 PRO A CB  1 
ATOM   3122 C  CG  . PRO A 1 457 ? 13.623  -19.716 -6.092  1.00   59.74  ? 472 PRO A CG  1 
ATOM   3123 C  CD  . PRO A 1 457 ? 13.797  -21.163 -6.417  1.00   62.76  ? 472 PRO A CD  1 
ATOM   3124 N  N   . ASP A 1 458 ? 10.314  -18.996 -8.638  1.00   59.17  ? 473 ASP A N   1 
ATOM   3125 C  CA  . ASP A 1 458 ? 9.902   -18.314 -9.831  1.00   58.23  ? 473 ASP A CA  1 
ATOM   3126 C  C   . ASP A 1 458 ? 10.367  -16.890 -9.713  1.00   54.31  ? 473 ASP A C   1 
ATOM   3127 O  O   . ASP A 1 458 ? 9.950   -16.195 -8.787  1.00   54.70  ? 473 ASP A O   1 
ATOM   3128 C  CB  . ASP A 1 458 ? 8.373   -18.362 -9.932  1.00   59.97  ? 473 ASP A CB  1 
ATOM   3129 C  CG  . ASP A 1 458 ? 7.852   -17.874 -11.267 1.00   63.20  ? 473 ASP A CG  1 
ATOM   3130 O  OD1 . ASP A 1 458 ? 8.594   -17.900 -12.278 1.00   63.91  ? 473 ASP A OD1 1 
ATOM   3131 O  OD2 . ASP A 1 458 ? 6.673   -17.478 -11.309 1.00   67.57  ? 473 ASP A OD2 1 
ATOM   3132 N  N   . LEU A 1 459 ? 11.195  -16.444 -10.655 1.00   51.84  ? 474 LEU A N   1 
ATOM   3133 C  CA  . LEU A 1 459 ? 11.793  -15.103 -10.587 1.00   50.79  ? 474 LEU A CA  1 
ATOM   3134 C  C   . LEU A 1 459 ? 11.043  -14.008 -11.361 1.00   51.27  ? 474 LEU A C   1 
ATOM   3135 O  O   . LEU A 1 459 ? 11.602  -12.956 -11.658 1.00   50.21  ? 474 LEU A O   1 
ATOM   3136 C  CB  . LEU A 1 459 ? 13.270  -15.155 -11.024 1.00   49.66  ? 474 LEU A CB  1 
ATOM   3137 C  CG  . LEU A 1 459 ? 14.145  -16.079 -10.174 1.00   49.17  ? 474 LEU A CG  1 
ATOM   3138 C  CD1 . LEU A 1 459 ? 15.468  -16.295 -10.861 1.00   49.96  ? 474 LEU A CD1 1 
ATOM   3139 C  CD2 . LEU A 1 459 ? 14.361  -15.521 -8.783  1.00   47.57  ? 474 LEU A CD2 1 
ATOM   3140 N  N   . GLN A 1 460 ? 9.774   -14.231 -11.661 1.00   54.61  ? 475 GLN A N   1 
ATOM   3141 C  CA  . GLN A 1 460 ? 8.987   -13.221 -12.373 1.00   57.84  ? 475 GLN A CA  1 
ATOM   3142 C  C   . GLN A 1 460 ? 8.635   -12.073 -11.443 1.00   56.30  ? 475 GLN A C   1 
ATOM   3143 O  O   . GLN A 1 460 ? 8.903   -10.911 -11.759 1.00   56.68  ? 475 GLN A O   1 
ATOM   3144 C  CB  . GLN A 1 460 ? 7.705   -13.817 -12.946 1.00   60.77  ? 475 GLN A CB  1 
ATOM   3145 C  CG  . GLN A 1 460 ? 6.763   -12.774 -13.523 1.00   64.68  ? 475 GLN A CG  1 
ATOM   3146 C  CD  . GLN A 1 460 ? 5.311   -13.223 -13.473 1.00   71.45  ? 475 GLN A CD  1 
ATOM   3147 O  OE1 . GLN A 1 460 ? 5.012   -14.410 -13.660 1.00   75.80  ? 475 GLN A OE1 1 
ATOM   3148 N  NE2 . GLN A 1 460 ? 4.394   -12.276 -13.218 1.00   72.44  ? 475 GLN A NE2 1 
ATOM   3149 N  N   . GLY A 1 461 ? 8.005   -12.407 -10.324 1.00   54.42  ? 476 GLY A N   1 
ATOM   3150 C  CA  . GLY A 1 461 ? 7.596   -11.411 -9.371  1.00   55.31  ? 476 GLY A CA  1 
ATOM   3151 C  C   . GLY A 1 461 ? 6.119   -11.082 -9.403  1.00   58.19  ? 476 GLY A C   1 
ATOM   3152 O  O   . GLY A 1 461 ? 5.462   -11.168 -10.436 1.00   61.76  ? 476 GLY A O   1 
ATOM   3153 N  N   . ARG A 1 462 ? 5.620   -10.672 -8.247  1.00   59.24  ? 477 ARG A N   1 
ATOM   3154 C  CA  . ARG A 1 462 ? 4.229   -10.367 -8.022  1.00   60.46  ? 477 ARG A CA  1 
ATOM   3155 C  C   . ARG A 1 462 ? 4.241   -8.994  -7.414  1.00   56.33  ? 477 ARG A C   1 
ATOM   3156 O  O   . ARG A 1 462 ? 5.176   -8.650  -6.711  1.00   54.22  ? 477 ARG A O   1 
ATOM   3157 C  CB  . ARG A 1 462 ? 3.690   -11.358 -7.001  1.00   66.99  ? 477 ARG A CB  1 
ATOM   3158 C  CG  . ARG A 1 462 ? 2.228   -11.220 -6.669  1.00   72.19  ? 477 ARG A CG  1 
ATOM   3159 C  CD  . ARG A 1 462 ? 1.430   -12.361 -7.268  1.00   79.32  ? 477 ARG A CD  1 
ATOM   3160 N  NE  . ARG A 1 462 ? 1.526   -13.593 -6.485  1.00   85.63  ? 477 ARG A NE  1 
ATOM   3161 C  CZ  . ARG A 1 462 ? 0.937   -13.792 -5.301  1.00   90.57  ? 477 ARG A CZ  1 
ATOM   3162 N  NH1 . ARG A 1 462 ? 0.218   -12.828 -4.725  1.00   91.31  ? 477 ARG A NH1 1 
ATOM   3163 N  NH2 . ARG A 1 462 ? 1.075   -14.963 -4.677  1.00   91.11  ? 477 ARG A NH2 1 
ATOM   3164 N  N   . PHE A 1 463 ? 3.206   -8.209  -7.651  1.00   55.39  ? 478 PHE A N   1 
ATOM   3165 C  CA  . PHE A 1 463 ? 3.137   -6.879  -7.072  1.00   53.10  ? 478 PHE A CA  1 
ATOM   3166 C  C   . PHE A 1 463 ? 2.171   -6.820  -5.887  1.00   51.62  ? 478 PHE A C   1 
ATOM   3167 O  O   . PHE A 1 463 ? 0.977   -6.875  -6.042  1.00   51.31  ? 478 PHE A O   1 
ATOM   3168 C  CB  . PHE A 1 463 ? 2.758   -5.862  -8.133  1.00   53.17  ? 478 PHE A CB  1 
ATOM   3169 C  CG  . PHE A 1 463 ? 2.922   -4.467  -7.679  1.00   54.10  ? 478 PHE A CG  1 
ATOM   3170 C  CD1 . PHE A 1 463 ? 4.176   -3.926  -7.573  1.00   52.88  ? 478 PHE A CD1 1 
ATOM   3171 C  CD2 . PHE A 1 463 ? 1.818   -3.697  -7.317  1.00   56.98  ? 478 PHE A CD2 1 
ATOM   3172 C  CE1 . PHE A 1 463 ? 4.354   -2.633  -7.117  1.00   53.35  ? 478 PHE A CE1 1 
ATOM   3173 C  CE2 . PHE A 1 463 ? 1.985   -2.393  -6.867  1.00   57.03  ? 478 PHE A CE2 1 
ATOM   3174 C  CZ  . PHE A 1 463 ? 3.260   -1.860  -6.766  1.00   54.28  ? 478 PHE A CZ  1 
ATOM   3175 N  N   . GLY A 1 464 ? 2.715   -6.739  -4.684  1.00   52.62  ? 479 GLY A N   1 
ATOM   3176 C  CA  . GLY A 1 464 ? 1.910   -6.450  -3.501  1.00   51.80  ? 479 GLY A CA  1 
ATOM   3177 C  C   . GLY A 1 464 ? 1.793   -4.944  -3.397  1.00   48.33  ? 479 GLY A C   1 
ATOM   3178 O  O   . GLY A 1 464 ? 1.182   -4.297  -4.254  1.00   47.24  ? 479 GLY A O   1 
ATOM   3179 N  N   . VAL A 1 465 ? 2.395   -4.398  -2.347  1.00   45.14  ? 480 VAL A N   1 
ATOM   3180 C  CA  . VAL A 1 465 ? 2.664   -2.968  -2.268  1.00   42.43  ? 480 VAL A CA  1 
ATOM   3181 C  C   . VAL A 1 465 ? 4.096   -2.696  -2.732  1.00   40.11  ? 480 VAL A C   1 
ATOM   3182 O  O   . VAL A 1 465 ? 4.501   -1.564  -2.825  1.00   39.22  ? 480 VAL A O   1 
ATOM   3183 C  CB  . VAL A 1 465 ? 2.441   -2.452  -0.849  1.00   42.46  ? 480 VAL A CB  1 
ATOM   3184 C  CG1 . VAL A 1 465 ? 1.110   -2.949  -0.343  1.00   44.19  ? 480 VAL A CG1 1 
ATOM   3185 C  CG2 . VAL A 1 465 ? 3.528   -2.914  0.089   1.00   42.00  ? 480 VAL A CG2 1 
ATOM   3186 N  N   . VAL A 1 466 ? 4.847   -3.762  -3.000  1.00   39.26  ? 481 VAL A N   1 
ATOM   3187 C  CA  . VAL A 1 466 ? 6.132   -3.719  -3.688  1.00   38.49  ? 481 VAL A CA  1 
ATOM   3188 C  C   . VAL A 1 466 ? 6.189   -4.868  -4.706  1.00   38.76  ? 481 VAL A C   1 
ATOM   3189 O  O   . VAL A 1 466 ? 5.337   -5.759  -4.685  1.00   39.46  ? 481 VAL A O   1 
ATOM   3190 C  CB  . VAL A 1 466 ? 7.294   -3.907  -2.700  1.00   39.54  ? 481 VAL A CB  1 
ATOM   3191 C  CG1 . VAL A 1 466 ? 7.479   -2.666  -1.825  1.00   39.66  ? 481 VAL A CG1 1 
ATOM   3192 C  CG2 . VAL A 1 466 ? 7.076   -5.140  -1.823  1.00   40.04  ? 481 VAL A CG2 1 
ATOM   3193 N  N   . LEU A 1 467 ? 7.187   -4.864  -5.587  1.00   38.28  ? 482 LEU A N   1 
ATOM   3194 C  CA  . LEU A 1 467 ? 7.435   -6.009  -6.486  1.00   38.72  ? 482 LEU A CA  1 
ATOM   3195 C  C   . LEU A 1 467 ? 8.248   -7.110  -5.772  1.00   40.99  ? 482 LEU A C   1 
ATOM   3196 O  O   . LEU A 1 467 ? 9.383   -6.873  -5.312  1.00   42.01  ? 482 LEU A O   1 
ATOM   3197 C  CB  . LEU A 1 467 ? 8.165   -5.554  -7.753  1.00   37.18  ? 482 LEU A CB  1 
ATOM   3198 C  CG  . LEU A 1 467 ? 8.515   -6.705  -8.702  1.00   37.31  ? 482 LEU A CG  1 
ATOM   3199 C  CD1 . LEU A 1 467 ? 7.299   -7.204  -9.464  1.00   37.43  ? 482 LEU A CD1 1 
ATOM   3200 C  CD2 . LEU A 1 467 ? 9.597   -6.265  -9.665  1.00   37.44  ? 482 LEU A CD2 1 
ATOM   3201 N  N   . GLN A 1 468 ? 7.703   -8.320  -5.700  1.00   43.63  ? 483 GLN A N   1 
ATOM   3202 C  CA  . GLN A 1 468 ? 8.291   -9.344  -4.849  1.00   45.88  ? 483 GLN A CA  1 
ATOM   3203 C  C   . GLN A 1 468 ? 8.101   -10.735 -5.404  1.00   48.90  ? 483 GLN A C   1 
ATOM   3204 O  O   . GLN A 1 468 ? 7.122   -10.994 -6.104  1.00   50.19  ? 483 GLN A O   1 
ATOM   3205 C  CB  . GLN A 1 468 ? 7.699   -9.252  -3.451  1.00   47.00  ? 483 GLN A CB  1 
ATOM   3206 C  CG  . GLN A 1 468 ? 6.236   -9.600  -3.371  1.00   50.94  ? 483 GLN A CG  1 
ATOM   3207 C  CD  . GLN A 1 468 ? 5.603   -9.145  -2.074  1.00   54.09  ? 483 GLN A CD  1 
ATOM   3208 O  OE1 . GLN A 1 468 ? 6.290   -9.029  -1.042  1.00   55.88  ? 483 GLN A OE1 1 
ATOM   3209 N  NE2 . GLN A 1 468 ? 4.280   -8.884  -2.112  1.00   54.25  ? 483 GLN A NE2 1 
ATOM   3210 N  N   . PRO A 1 469 ? 9.029   -11.644 -5.076  1.00   51.12  ? 484 PRO A N   1 
ATOM   3211 C  CA  . PRO A 1 469 ? 8.975   -12.978 -5.613  1.00   53.47  ? 484 PRO A CA  1 
ATOM   3212 C  C   . PRO A 1 469 ? 7.880   -13.741 -4.934  1.00   57.45  ? 484 PRO A C   1 
ATOM   3213 O  O   . PRO A 1 469 ? 7.570   -13.435 -3.793  1.00   59.35  ? 484 PRO A O   1 
ATOM   3214 C  CB  . PRO A 1 469 ? 10.314  -13.568 -5.212  1.00   53.38  ? 484 PRO A CB  1 
ATOM   3215 C  CG  . PRO A 1 469 ? 10.684  -12.859 -3.953  1.00   52.39  ? 484 PRO A CG  1 
ATOM   3216 C  CD  . PRO A 1 469 ? 10.073  -11.503 -4.039  1.00   51.22  ? 484 PRO A CD  1 
ATOM   3217 N  N   . GLU A 1 470 ? 7.309   -14.730 -5.617  1.00   62.22  ? 485 GLU A N   1 
ATOM   3218 C  CA  . GLU A 1 470 ? 6.278   -15.568 -5.006  1.00   65.87  ? 485 GLU A CA  1 
ATOM   3219 C  C   . GLU A 1 470 ? 6.935   -16.393 -3.908  1.00   66.58  ? 485 GLU A C   1 
ATOM   3220 O  O   . GLU A 1 470 ? 8.097   -16.785 -4.040  1.00   65.33  ? 485 GLU A O   1 
ATOM   3221 C  CB  . GLU A 1 470 ? 5.592   -16.500 -6.020  1.00   69.18  ? 485 GLU A CB  1 
ATOM   3222 C  CG  . GLU A 1 470 ? 5.147   -15.821 -7.314  1.00   72.18  ? 485 GLU A CG  1 
ATOM   3223 C  CD  . GLU A 1 470 ? 3.703   -16.112 -7.720  1.00   75.66  ? 485 GLU A CD  1 
ATOM   3224 O  OE1 . GLU A 1 470 ? 3.029   -15.154 -8.167  1.00   75.24  ? 485 GLU A OE1 1 
ATOM   3225 O  OE2 . GLU A 1 470 ? 3.231   -17.271 -7.592  1.00   78.90  ? 485 GLU A OE2 1 
ATOM   3226 N  N   . ARG A 1 471 ? 6.173   -16.634 -2.840  1.00   66.96  ? 486 ARG A N   1 
ATOM   3227 C  CA  . ARG A 1 471 ? 6.571   -17.459 -1.713  1.00   67.11  ? 486 ARG A CA  1 
ATOM   3228 C  C   . ARG A 1 471 ? 7.327   -18.668 -2.232  1.00   63.74  ? 486 ARG A C   1 
ATOM   3229 O  O   . ARG A 1 471 ? 6.889   -19.270 -3.205  1.00   60.63  ? 486 ARG A O   1 
ATOM   3230 C  CB  . ARG A 1 471 ? 5.308   -17.894 -0.963  1.00   75.29  ? 486 ARG A CB  1 
ATOM   3231 C  CG  . ARG A 1 471 ? 5.527   -18.491 0.416   1.00   86.49  ? 486 ARG A CG  1 
ATOM   3232 C  CD  . ARG A 1 471 ? 4.216   -18.688 1.179   1.00   96.36  ? 486 ARG A CD  1 
ATOM   3233 N  NE  . ARG A 1 471 ? 4.402   -19.499 2.386   1.00   109.41 ? 486 ARG A NE  1 
ATOM   3234 C  CZ  . ARG A 1 471 ? 4.935   -19.062 3.528   1.00   121.36 ? 486 ARG A CZ  1 
ATOM   3235 N  NH1 . ARG A 1 471 ? 5.350   -17.801 3.654   1.00   128.87 ? 486 ARG A NH1 1 
ATOM   3236 N  NH2 . ARG A 1 471 ? 5.066   -19.895 4.559   1.00   126.68 ? 486 ARG A NH2 1 
ATOM   3237 N  N   . TYR A 1 472 ? 8.471   -19.000 -1.619  1.00   59.82  ? 487 TYR A N   1 
ATOM   3238 C  CA  . TYR A 1 472 ? 9.231   -20.193 -2.004  1.00   59.58  ? 487 TYR A CA  1 
ATOM   3239 C  C   . TYR A 1 472 ? 9.767   -20.933 -0.776  1.00   61.48  ? 487 TYR A C   1 
ATOM   3240 O  O   . TYR A 1 472 ? 9.904   -20.349 0.310   1.00   62.53  ? 487 TYR A O   1 
ATOM   3241 C  CB  . TYR A 1 472 ? 10.370  -19.844 -2.974  1.00   57.76  ? 487 TYR A CB  1 
ATOM   3242 C  CG  . TYR A 1 472 ? 11.352  -18.802 -2.458  1.00   57.36  ? 487 TYR A CG  1 
ATOM   3243 C  CD1 . TYR A 1 472 ? 11.134  -17.442 -2.655  1.00   56.22  ? 487 TYR A CD1 1 
ATOM   3244 C  CD2 . TYR A 1 472 ? 12.505  -19.173 -1.773  1.00   57.41  ? 487 TYR A CD2 1 
ATOM   3245 C  CE1 . TYR A 1 472 ? 12.023  -16.482 -2.174  1.00   54.25  ? 487 TYR A CE1 1 
ATOM   3246 C  CE2 . TYR A 1 472 ? 13.399  -18.224 -1.283  1.00   55.53  ? 487 TYR A CE2 1 
ATOM   3247 C  CZ  . TYR A 1 472 ? 13.160  -16.876 -1.487  1.00   54.69  ? 487 TYR A CZ  1 
ATOM   3248 O  OH  . TYR A 1 472 ? 14.058  -15.923 -1.019  1.00   51.79  ? 487 TYR A OH  1 
ATOM   3249 N  N   . THR A 1 473 ? 10.042  -22.228 -0.950  1.00   62.18  ? 488 THR A N   1 
ATOM   3250 C  CA  . THR A 1 473 ? 10.780  -23.018 0.037   1.00   61.48  ? 488 THR A CA  1 
ATOM   3251 C  C   . THR A 1 473 ? 12.248  -23.040 -0.339  1.00   60.23  ? 488 THR A C   1 
ATOM   3252 O  O   . THR A 1 473 ? 12.586  -23.135 -1.534  1.00   61.40  ? 488 THR A O   1 
ATOM   3253 C  CB  . THR A 1 473 ? 10.342  -24.496 0.076   1.00   63.99  ? 488 THR A CB  1 
ATOM   3254 O  OG1 . THR A 1 473 ? 10.754  -25.156 -1.131  1.00   64.02  ? 488 THR A OG1 1 
ATOM   3255 C  CG2 . THR A 1 473 ? 8.829   -24.627 0.278   1.00   65.35  ? 488 THR A CG2 1 
ATOM   3256 N  N   . VAL A 1 474 ? 13.106  -22.999 0.680   1.00   57.39  ? 489 VAL A N   1 
ATOM   3257 C  CA  . VAL A 1 474 ? 14.543  -23.105 0.497   1.00   56.26  ? 489 VAL A CA  1 
ATOM   3258 C  C   . VAL A 1 474 ? 15.208  -23.911 1.621   1.00   57.16  ? 489 VAL A C   1 
ATOM   3259 O  O   . VAL A 1 474 ? 14.936  -23.702 2.790   1.00   57.42  ? 489 VAL A O   1 
ATOM   3260 C  CB  . VAL A 1 474 ? 15.175  -21.708 0.392   1.00   54.01  ? 489 VAL A CB  1 
ATOM   3261 C  CG1 . VAL A 1 474 ? 14.507  -20.741 1.344   1.00   52.27  ? 489 VAL A CG1 1 
ATOM   3262 C  CG2 . VAL A 1 474 ? 16.685  -21.759 0.630   1.00   54.03  ? 489 VAL A CG2 1 
ATOM   3263 N  N   . THR A 1 475 ? 16.092  -24.826 1.249   1.00   58.75  ? 490 THR A N   1 
ATOM   3264 C  CA  . THR A 1 475 ? 16.921  -25.529 2.213   1.00   60.12  ? 490 THR A CA  1 
ATOM   3265 C  C   . THR A 1 475 ? 18.049  -24.631 2.765   1.00   60.33  ? 490 THR A C   1 
ATOM   3266 O  O   . THR A 1 475 ? 18.843  -24.063 1.996   1.00   57.54  ? 490 THR A O   1 
ATOM   3267 C  CB  . THR A 1 475 ? 17.504  -26.805 1.600   1.00   61.61  ? 490 THR A CB  1 
ATOM   3268 O  OG1 . THR A 1 475 ? 16.437  -27.726 1.356   1.00   63.82  ? 490 THR A OG1 1 
ATOM   3269 C  CG2 . THR A 1 475 ? 18.504  -27.459 2.543   1.00   62.53  ? 490 THR A CG2 1 
ATOM   3270 N  N   . VAL A 1 476 ? 18.093  -24.532 4.107   1.00   62.19  ? 491 VAL A N   1 
ATOM   3271 C  CA  . VAL A 1 476 ? 19.053  -23.704 4.869   1.00   62.75  ? 491 VAL A CA  1 
ATOM   3272 C  C   . VAL A 1 476 ? 20.068  -24.584 5.614   1.00   63.65  ? 491 VAL A C   1 
ATOM   3273 O  O   . VAL A 1 476 ? 19.684  -25.368 6.483   1.00   64.56  ? 491 VAL A O   1 
ATOM   3274 C  CB  . VAL A 1 476 ? 18.328  -22.820 5.916   1.00   62.86  ? 491 VAL A CB  1 
ATOM   3275 C  CG1 . VAL A 1 476 ? 19.260  -21.734 6.452   1.00   63.31  ? 491 VAL A CG1 1 
ATOM   3276 C  CG2 . VAL A 1 476 ? 17.070  -22.197 5.324   1.00   61.72  ? 491 VAL A CG2 1 
ATOM   3277 N  N   . THR A 1 477 ? 21.357  -24.427 5.298   1.00   64.26  ? 492 THR A N   1 
ATOM   3278 C  CA  . THR A 1 477 ? 22.408  -25.314 5.830   1.00   65.54  ? 492 THR A CA  1 
ATOM   3279 C  C   . THR A 1 477 ? 23.669  -24.554 6.223   1.00   65.74  ? 492 THR A C   1 
ATOM   3280 O  O   . THR A 1 477 ? 24.199  -23.813 5.400   1.00   65.01  ? 492 THR A O   1 
ATOM   3281 C  CB  . THR A 1 477 ? 22.812  -26.335 4.765   1.00   66.73  ? 492 THR A CB  1 
ATOM   3282 O  OG1 . THR A 1 477 ? 21.682  -26.602 3.914   1.00   65.95  ? 492 THR A OG1 1 
ATOM   3283 C  CG2 . THR A 1 477 ? 23.305  -27.604 5.423   1.00   67.76  ? 492 THR A CG2 1 
ATOM   3284 N  N   . PRO A 1 478 ? 24.157  -24.748 7.436   1.00   68.41  ? 493 PRO A N   1 
ATOM   3285 C  CA  . PRO A 1 478 ? 25.308  -23.995 7.910   1.00   67.47  ? 493 PRO A CA  1 
ATOM   3286 C  C   . PRO A 1 478 ? 26.566  -24.775 7.764   1.00   67.41  ? 493 PRO A C   1 
ATOM   3287 O  O   . PRO A 1 478 ? 26.621  -25.675 6.972   1.00   65.64  ? 493 PRO A O   1 
ATOM   3288 C  CB  . PRO A 1 478 ? 25.005  -23.840 9.381   1.00   67.92  ? 493 PRO A CB  1 
ATOM   3289 C  CG  . PRO A 1 478 ? 24.269  -25.078 9.724   1.00   69.10  ? 493 PRO A CG  1 
ATOM   3290 C  CD  . PRO A 1 478 ? 23.578  -25.569 8.503   1.00   69.24  ? 493 PRO A CD  1 
ATOM   3291 N  N   . ARG A 1 479 ? 27.568  -24.423 8.550   1.00   70.75  ? 494 ARG A N   1 
ATOM   3292 C  CA  . ARG A 1 479 ? 28.755  -25.250 8.739   1.00   70.85  ? 494 ARG A CA  1 
ATOM   3293 C  C   . ARG A 1 479 ? 28.640  -26.192 9.955   1.00   71.83  ? 494 ARG A C   1 
ATOM   3294 O  O   . ARG A 1 479 ? 29.360  -26.078 10.944  1.00   72.00  ? 494 ARG A O   1 
ATOM   3295 C  CB  . ARG A 1 479 ? 29.973  -24.383 8.880   1.00   68.89  ? 494 ARG A CB  1 
ATOM   3296 C  CG  . ARG A 1 479 ? 31.241  -25.185 8.964   1.00   56.26  ? 494 ARG A CG  1 
ATOM   3297 C  CD  . ARG A 1 479 ? 32.406  -24.271 9.189   1.00   56.13  ? 494 ARG A CD  1 
ATOM   3298 N  NE  . ARG A 1 479 ? 32.938  -23.765 7.949   1.00   55.79  ? 494 ARG A NE  1 
ATOM   3299 C  CZ  . ARG A 1 479 ? 32.765  -22.533 7.521   1.00   54.48  ? 494 ARG A CZ  1 
ATOM   3300 N  NH1 . ARG A 1 479 ? 32.045  -21.683 8.216   1.00   53.36  ? 494 ARG A NH1 1 
ATOM   3301 N  NH2 . ARG A 1 479 ? 33.307  -22.157 6.388   1.00   54.40  ? 494 ARG A NH2 1 
ATOM   3302 N  N   . ASN B 1 38  ? 0.956   -5.735  62.721  1.00   77.62  ? 53  ASN B N   1 
ATOM   3303 C  CA  . ASN B 1 38  ? 0.236   -6.919  63.309  1.00   77.51  ? 53  ASN B CA  1 
ATOM   3304 C  C   . ASN B 1 38  ? -1.253  -6.911  62.949  1.00   74.97  ? 53  ASN B C   1 
ATOM   3305 O  O   . ASN B 1 38  ? -1.797  -7.919  62.486  1.00   74.72  ? 53  ASN B O   1 
ATOM   3306 C  CB  . ASN B 1 38  ? 0.430   -6.991  64.836  1.00   80.25  ? 53  ASN B CB  1 
ATOM   3307 C  CG  . ASN B 1 38  ? -0.120  -5.768  65.572  1.00   82.85  ? 53  ASN B CG  1 
ATOM   3308 O  OD1 . ASN B 1 38  ? -0.328  -4.704  64.976  1.00   86.26  ? 53  ASN B OD1 1 
ATOM   3309 N  ND2 . ASN B 1 38  ? -0.358  -5.915  66.873  1.00   82.27  ? 53  ASN B ND2 1 
ATOM   3310 N  N   . LEU B 1 39  ? -1.887  -5.757  63.172  1.00   70.52  ? 54  LEU B N   1 
ATOM   3311 C  CA  . LEU B 1 39  ? -3.272  -5.475  62.800  1.00   64.15  ? 54  LEU B CA  1 
ATOM   3312 C  C   . LEU B 1 39  ? -3.265  -4.190  61.989  1.00   61.37  ? 54  LEU B C   1 
ATOM   3313 O  O   . LEU B 1 39  ? -2.585  -3.233  62.373  1.00   63.95  ? 54  LEU B O   1 
ATOM   3314 C  CB  . LEU B 1 39  ? -4.096  -5.236  64.046  1.00   62.17  ? 54  LEU B CB  1 
ATOM   3315 C  CG  . LEU B 1 39  ? -4.531  -6.496  64.760  1.00   63.75  ? 54  LEU B CG  1 
ATOM   3316 C  CD1 . LEU B 1 39  ? -5.061  -6.159  66.149  1.00   63.49  ? 54  LEU B CD1 1 
ATOM   3317 C  CD2 . LEU B 1 39  ? -5.586  -7.203  63.916  1.00   65.04  ? 54  LEU B CD2 1 
ATOM   3318 N  N   . PRO B 1 40  ? -4.008  -4.140  60.875  1.00   57.12  ? 55  PRO B N   1 
ATOM   3319 C  CA  . PRO B 1 40  ? -4.055  -2.876  60.141  1.00   53.39  ? 55  PRO B CA  1 
ATOM   3320 C  C   . PRO B 1 40  ? -4.605  -1.798  61.054  1.00   51.23  ? 55  PRO B C   1 
ATOM   3321 O  O   . PRO B 1 40  ? -5.431  -2.106  61.921  1.00   51.85  ? 55  PRO B O   1 
ATOM   3322 C  CB  . PRO B 1 40  ? -5.041  -3.149  59.001  1.00   52.93  ? 55  PRO B CB  1 
ATOM   3323 C  CG  . PRO B 1 40  ? -5.161  -4.621  58.923  1.00   55.24  ? 55  PRO B CG  1 
ATOM   3324 C  CD  . PRO B 1 40  ? -4.928  -5.137  60.312  1.00   57.85  ? 55  PRO B CD  1 
ATOM   3325 N  N   . PRO B 1 41  ? -4.149  -0.547  60.887  1.00   49.15  ? 56  PRO B N   1 
ATOM   3326 C  CA  . PRO B 1 41  ? -4.630  0.521   61.777  1.00   48.27  ? 56  PRO B CA  1 
ATOM   3327 C  C   . PRO B 1 41  ? -6.159  0.488   61.982  1.00   47.79  ? 56  PRO B C   1 
ATOM   3328 O  O   . PRO B 1 41  ? -6.613  0.488   63.138  1.00   52.20  ? 56  PRO B O   1 
ATOM   3329 C  CB  . PRO B 1 41  ? -4.195  1.812   61.069  1.00   47.62  ? 56  PRO B CB  1 
ATOM   3330 C  CG  . PRO B 1 41  ? -3.069  1.411   60.164  1.00   47.09  ? 56  PRO B CG  1 
ATOM   3331 C  CD  . PRO B 1 41  ? -3.208  -0.055  59.862  1.00   47.31  ? 56  PRO B CD  1 
ATOM   3332 N  N   . HIS B 1 42  ? -6.949  0.404   60.907  1.00   43.50  ? 57  HIS B N   1 
ATOM   3333 C  CA  . HIS B 1 42  ? -8.406  0.448   61.073  1.00   41.54  ? 57  HIS B CA  1 
ATOM   3334 C  C   . HIS B 1 42  ? -8.909  -0.588  62.077  1.00   41.20  ? 57  HIS B C   1 
ATOM   3335 O  O   . HIS B 1 42  ? -9.724  -0.267  62.926  1.00   43.14  ? 57  HIS B O   1 
ATOM   3336 C  CB  . HIS B 1 42  ? -9.178  0.414   59.724  1.00   41.30  ? 57  HIS B CB  1 
ATOM   3337 C  CG  . HIS B 1 42  ? -9.159  -0.905  59.002  1.00   40.61  ? 57  HIS B CG  1 
ATOM   3338 N  ND1 . HIS B 1 42  ? -8.168  -1.253  58.105  1.00   39.92  ? 57  HIS B ND1 1 
ATOM   3339 C  CD2 . HIS B 1 42  ? -10.037 -1.936  59.008  1.00   40.47  ? 57  HIS B CD2 1 
ATOM   3340 C  CE1 . HIS B 1 42  ? -8.422  -2.454  57.616  1.00   39.83  ? 57  HIS B CE1 1 
ATOM   3341 N  NE2 . HIS B 1 42  ? -9.544  -2.896  58.155  1.00   40.56  ? 57  HIS B NE2 1 
ATOM   3342 N  N   . LEU B 1 43  ? -8.404  -1.808  62.024  1.00   40.03  ? 58  LEU B N   1 
ATOM   3343 C  CA  . LEU B 1 43  ? -8.823  -2.802  62.983  1.00   40.82  ? 58  LEU B CA  1 
ATOM   3344 C  C   . LEU B 1 43  ? -8.221  -2.535  64.353  1.00   42.14  ? 58  LEU B C   1 
ATOM   3345 O  O   . LEU B 1 43  ? -8.802  -2.939  65.367  1.00   43.85  ? 58  LEU B O   1 
ATOM   3346 C  CB  . LEU B 1 43  ? -8.420  -4.206  62.553  1.00   40.72  ? 58  LEU B CB  1 
ATOM   3347 C  CG  . LEU B 1 43  ? -9.061  -4.826  61.317  1.00   40.70  ? 58  LEU B CG  1 
ATOM   3348 C  CD1 . LEU B 1 43  ? -8.600  -6.268  61.256  1.00   41.47  ? 58  LEU B CD1 1 
ATOM   3349 C  CD2 . LEU B 1 43  ? -10.584 -4.771  61.293  1.00   41.00  ? 58  LEU B CD2 1 
ATOM   3350 N  N   . LEU B 1 44  ? -7.048  -1.897  64.397  1.00   41.86  ? 59  LEU B N   1 
ATOM   3351 C  CA  . LEU B 1 44  ? -6.340  -1.680  65.681  1.00   42.32  ? 59  LEU B CA  1 
ATOM   3352 C  C   . LEU B 1 44  ? -7.090  -0.673  66.537  1.00   41.52  ? 59  LEU B C   1 
ATOM   3353 O  O   . LEU B 1 44  ? -7.550  -0.984  67.601  1.00   40.94  ? 59  LEU B O   1 
ATOM   3354 C  CB  . LEU B 1 44  ? -4.889  -1.204  65.461  1.00   41.97  ? 59  LEU B CB  1 
ATOM   3355 C  CG  . LEU B 1 44  ? -3.832  -1.518  66.552  1.00   43.36  ? 59  LEU B CG  1 
ATOM   3356 C  CD1 . LEU B 1 44  ? -2.759  -0.428  66.657  1.00   42.84  ? 59  LEU B CD1 1 
ATOM   3357 C  CD2 . LEU B 1 44  ? -4.419  -1.787  67.932  1.00   44.17  ? 59  LEU B CD2 1 
ATOM   3358 N  N   . PHE B 1 45  ? -7.240  0.525   66.015  1.00   42.23  ? 60  PHE B N   1 
ATOM   3359 C  CA  . PHE B 1 45  ? -7.929  1.583   66.698  1.00   44.15  ? 60  PHE B CA  1 
ATOM   3360 C  C   . PHE B 1 45  ? -9.402  1.326   66.869  1.00   45.17  ? 60  PHE B C   1 
ATOM   3361 O  O   . PHE B 1 45  ? -10.034 1.994   67.650  1.00   46.75  ? 60  PHE B O   1 
ATOM   3362 C  CB  . PHE B 1 45  ? -7.746  2.874   65.937  1.00   45.94  ? 60  PHE B CB  1 
ATOM   3363 C  CG  . PHE B 1 45  ? -6.309  3.304   65.836  1.00   49.64  ? 60  PHE B CG  1 
ATOM   3364 C  CD1 . PHE B 1 45  ? -5.595  3.666   66.987  1.00   51.53  ? 60  PHE B CD1 1 
ATOM   3365 C  CD2 . PHE B 1 45  ? -5.663  3.352   64.604  1.00   49.15  ? 60  PHE B CD2 1 
ATOM   3366 C  CE1 . PHE B 1 45  ? -4.270  4.067   66.896  1.00   52.78  ? 60  PHE B CE1 1 
ATOM   3367 C  CE2 . PHE B 1 45  ? -4.349  3.767   64.516  1.00   49.83  ? 60  PHE B CE2 1 
ATOM   3368 C  CZ  . PHE B 1 45  ? -3.649  4.117   65.659  1.00   51.04  ? 60  PHE B CZ  1 
ATOM   3369 N  N   . THR B 1 46  ? -9.970  0.384   66.130  1.00   46.55  ? 61  THR B N   1 
ATOM   3370 C  CA  . THR B 1 46  ? -11.293 -0.103  66.461  1.00   49.03  ? 61  THR B CA  1 
ATOM   3371 C  C   . THR B 1 46  ? -11.197 -0.895  67.773  1.00   52.09  ? 61  THR B C   1 
ATOM   3372 O  O   . THR B 1 46  ? -12.003 -0.692  68.677  1.00   55.32  ? 61  THR B O   1 
ATOM   3373 C  CB  . THR B 1 46  ? -11.896 -0.915  65.299  1.00   48.26  ? 61  THR B CB  1 
ATOM   3374 O  OG1 . THR B 1 46  ? -12.159 -0.017  64.226  1.00   48.09  ? 61  THR B OG1 1 
ATOM   3375 C  CG2 . THR B 1 46  ? -13.207 -1.557  65.670  1.00   48.31  ? 61  THR B CG2 1 
ATOM   3376 N  N   . GLN B 1 47  ? -10.182 -1.752  67.874  1.00   53.86  ? 62  GLN B N   1 
ATOM   3377 C  CA  . GLN B 1 47  ? -9.954  -2.610  69.041  1.00   55.99  ? 62  GLN B CA  1 
ATOM   3378 C  C   . GLN B 1 47  ? -9.733  -1.810  70.310  1.00   54.70  ? 62  GLN B C   1 
ATOM   3379 O  O   . GLN B 1 47  ? -10.246 -2.153  71.373  1.00   52.50  ? 62  GLN B O   1 
ATOM   3380 C  CB  . GLN B 1 47  ? -8.721  -3.479  68.808  1.00   59.37  ? 62  GLN B CB  1 
ATOM   3381 C  CG  . GLN B 1 47  ? -8.884  -4.915  69.254  1.00   64.95  ? 62  GLN B CG  1 
ATOM   3382 C  CD  . GLN B 1 47  ? -9.531  -5.791  68.190  1.00   69.43  ? 62  GLN B CD  1 
ATOM   3383 O  OE1 . GLN B 1 47  ? -9.365  -5.571  66.978  1.00   70.28  ? 62  GLN B OE1 1 
ATOM   3384 N  NE2 . GLN B 1 47  ? -10.260 -6.812  68.641  1.00   74.58  ? 62  GLN B NE2 1 
ATOM   3385 N  N   . LEU B 1 48  ? -8.947  -0.748  70.184  1.00   54.04  ? 63  LEU B N   1 
ATOM   3386 C  CA  . LEU B 1 48  ? -8.584  0.073   71.327  1.00   55.98  ? 63  LEU B CA  1 
ATOM   3387 C  C   . LEU B 1 48  ? -9.755  0.898   71.842  1.00   57.68  ? 63  LEU B C   1 
ATOM   3388 O  O   . LEU B 1 48  ? -9.927  1.031   73.050  1.00   57.14  ? 63  LEU B O   1 
ATOM   3389 C  CB  . LEU B 1 48  ? -7.416  0.995   70.980  1.00   55.13  ? 63  LEU B CB  1 
ATOM   3390 C  CG  . LEU B 1 48  ? -6.081  0.347   70.569  1.00   55.11  ? 63  LEU B CG  1 
ATOM   3391 C  CD1 . LEU B 1 48  ? -5.050  1.416   70.237  1.00   54.09  ? 63  LEU B CD1 1 
ATOM   3392 C  CD2 . LEU B 1 48  ? -5.517  -0.598  71.622  1.00   56.31  ? 63  LEU B CD2 1 
ATOM   3393 N  N   . SER B 1 49  ? -10.556 1.443   70.925  1.00   59.53  ? 64  SER B N   1 
ATOM   3394 C  CA  . SER B 1 49  ? -11.755 2.211   71.283  1.00   61.26  ? 64  SER B CA  1 
ATOM   3395 C  C   . SER B 1 49  ? -12.564 1.613   72.420  1.00   60.71  ? 64  SER B C   1 
ATOM   3396 O  O   . SER B 1 49  ? -12.958 2.307   73.353  1.00   59.96  ? 64  SER B O   1 
ATOM   3397 C  CB  . SER B 1 49  ? -12.669 2.329   70.081  1.00   64.24  ? 64  SER B CB  1 
ATOM   3398 O  OG  . SER B 1 49  ? -12.052 3.104   69.083  1.00   66.21  ? 64  SER B OG  1 
ATOM   3399 N  N   . SER B 1 50  ? -12.815 0.320   72.326  1.00   59.33  ? 65  SER B N   1 
ATOM   3400 C  CA  . SER B 1 50  ? -13.477 -0.396  73.392  1.00   61.15  ? 65  SER B CA  1 
ATOM   3401 C  C   . SER B 1 50  ? -12.943 0.019   74.744  1.00   59.99  ? 65  SER B C   1 
ATOM   3402 O  O   . SER B 1 50  ? -13.694 0.444   75.616  1.00   61.04  ? 65  SER B O   1 
ATOM   3403 C  CB  . SER B 1 50  ? -13.252 -1.891  73.208  1.00   62.78  ? 65  SER B CB  1 
ATOM   3404 O  OG  . SER B 1 50  ? -12.984 -2.151  71.842  1.00   66.49  ? 65  SER B OG  1 
ATOM   3405 N  N   . GLN B 1 51  ? -11.628 -0.075  74.892  1.00   58.30  ? 66  GLN B N   1 
ATOM   3406 C  CA  . GLN B 1 51  ? -11.003 -0.184  76.218  1.00   58.65  ? 66  GLN B CA  1 
ATOM   3407 C  C   . GLN B 1 51  ? -10.370 1.129   76.662  1.00   54.52  ? 66  GLN B C   1 
ATOM   3408 O  O   . GLN B 1 51  ? -10.657 1.616   77.750  1.00   55.90  ? 66  GLN B O   1 
ATOM   3409 C  CB  . GLN B 1 51  ? -10.015 -1.374  76.278  1.00   60.91  ? 66  GLN B CB  1 
ATOM   3410 C  CG  . GLN B 1 51  ? -9.321  -1.759  74.961  1.00   60.94  ? 66  GLN B CG  1 
ATOM   3411 C  CD  . GLN B 1 51  ? -8.677  -3.151  74.970  1.00   62.71  ? 66  GLN B CD  1 
ATOM   3412 O  OE1 . GLN B 1 51  ? -8.648  -3.839  75.993  1.00   67.91  ? 66  GLN B OE1 1 
ATOM   3413 N  NE2 . GLN B 1 51  ? -8.149  -3.564  73.818  1.00   61.51  ? 66  GLN B NE2 1 
ATOM   3414 N  N   . TYR B 1 52  ? -9.558  1.721   75.802  1.00   49.86  ? 67  TYR B N   1 
ATOM   3415 C  CA  . TYR B 1 52  ? -9.129  3.112   75.985  1.00   48.90  ? 67  TYR B CA  1 
ATOM   3416 C  C   . TYR B 1 52  ? -10.252 3.940   75.389  1.00   48.57  ? 67  TYR B C   1 
ATOM   3417 O  O   . TYR B 1 52  ? -11.277 3.372   75.080  1.00   52.33  ? 67  TYR B O   1 
ATOM   3418 C  CB  . TYR B 1 52  ? -7.754  3.324   75.344  1.00   46.90  ? 67  TYR B CB  1 
ATOM   3419 C  CG  . TYR B 1 52  ? -6.795  2.312   75.902  1.00   46.73  ? 67  TYR B CG  1 
ATOM   3420 C  CD1 . TYR B 1 52  ? -6.139  2.564   77.074  1.00   47.43  ? 67  TYR B CD1 1 
ATOM   3421 C  CD2 . TYR B 1 52  ? -6.644  1.056   75.321  1.00   46.60  ? 67  TYR B CD2 1 
ATOM   3422 C  CE1 . TYR B 1 52  ? -5.299  1.642   77.625  1.00   48.21  ? 67  TYR B CE1 1 
ATOM   3423 C  CE2 . TYR B 1 52  ? -5.807  0.110   75.867  1.00   47.23  ? 67  TYR B CE2 1 
ATOM   3424 C  CZ  . TYR B 1 52  ? -5.137  0.424   77.026  1.00   48.83  ? 67  TYR B CZ  1 
ATOM   3425 O  OH  . TYR B 1 52  ? -4.291  -0.483  77.630  1.00   51.64  ? 67  TYR B OH  1 
ATOM   3426 N  N   . GLY B 1 53  ? -10.136 5.242   75.206  1.00   48.30  ? 68  GLY B N   1 
ATOM   3427 C  CA  . GLY B 1 53  ? -11.262 5.965   74.511  1.00   49.45  ? 68  GLY B CA  1 
ATOM   3428 C  C   . GLY B 1 53  ? -11.507 5.686   73.007  1.00   47.48  ? 68  GLY B C   1 
ATOM   3429 O  O   . GLY B 1 53  ? -10.682 5.028   72.355  1.00   46.73  ? 68  GLY B O   1 
ATOM   3430 N  N   . PRO B 1 54  ? -12.609 6.237   72.430  1.00   47.25  ? 69  PRO B N   1 
ATOM   3431 C  CA  . PRO B 1 54  ? -12.859 6.246   70.964  1.00   45.76  ? 69  PRO B CA  1 
ATOM   3432 C  C   . PRO B 1 54  ? -12.129 7.351   70.204  1.00   44.75  ? 69  PRO B C   1 
ATOM   3433 O  O   . PRO B 1 54  ? -12.316 7.490   69.020  1.00   46.49  ? 69  PRO B O   1 
ATOM   3434 C  CB  . PRO B 1 54  ? -14.361 6.520   70.875  1.00   46.33  ? 69  PRO B CB  1 
ATOM   3435 C  CG  . PRO B 1 54  ? -14.620 7.419   72.028  1.00   47.71  ? 69  PRO B CG  1 
ATOM   3436 C  CD  . PRO B 1 54  ? -13.642 7.019   73.133  1.00   48.29  ? 69  PRO B CD  1 
ATOM   3437 N  N   . LEU B 1 55  ? -11.297 8.126   70.878  1.00   45.74  ? 70  LEU B N   1 
ATOM   3438 C  CA  . LEU B 1 55  ? -10.573 9.241   70.279  1.00   45.12  ? 70  LEU B CA  1 
ATOM   3439 C  C   . LEU B 1 55  ? -9.132  9.183   70.774  1.00   45.54  ? 70  LEU B C   1 
ATOM   3440 O  O   . LEU B 1 55  ? -8.873  9.429   71.938  1.00   47.26  ? 70  LEU B O   1 
ATOM   3441 C  CB  . LEU B 1 55  ? -11.231 10.534  70.718  1.00   45.88  ? 70  LEU B CB  1 
ATOM   3442 C  CG  . LEU B 1 55  ? -10.449 11.828  70.671  1.00   46.03  ? 70  LEU B CG  1 
ATOM   3443 C  CD1 . LEU B 1 55  ? -10.315 12.299  69.246  1.00   45.57  ? 70  LEU B CD1 1 
ATOM   3444 C  CD2 . LEU B 1 55  ? -11.131 12.890  71.517  1.00   47.39  ? 70  LEU B CD2 1 
ATOM   3445 N  N   . PHE B 1 56  ? -8.213  8.848   69.877  1.00   45.12  ? 71  PHE B N   1 
ATOM   3446 C  CA  . PHE B 1 56  ? -6.799  8.615   70.181  1.00   44.90  ? 71  PHE B CA  1 
ATOM   3447 C  C   . PHE B 1 56  ? -5.936  9.724   69.629  1.00   43.50  ? 71  PHE B C   1 
ATOM   3448 O  O   . PHE B 1 56  ? -6.139  10.162  68.503  1.00   43.57  ? 71  PHE B O   1 
ATOM   3449 C  CB  . PHE B 1 56  ? -6.341  7.355   69.473  1.00   45.55  ? 71  PHE B CB  1 
ATOM   3450 C  CG  . PHE B 1 56  ? -6.134  6.200   70.370  1.00   47.57  ? 71  PHE B CG  1 
ATOM   3451 C  CD1 . PHE B 1 56  ? -7.188  5.375   70.704  1.00   49.32  ? 71  PHE B CD1 1 
ATOM   3452 C  CD2 . PHE B 1 56  ? -4.865  5.908   70.865  1.00   49.32  ? 71  PHE B CD2 1 
ATOM   3453 C  CE1 . PHE B 1 56  ? -6.990  4.282   71.548  1.00   50.44  ? 71  PHE B CE1 1 
ATOM   3454 C  CE2 . PHE B 1 56  ? -4.661  4.823   71.704  1.00   49.79  ? 71  PHE B CE2 1 
ATOM   3455 C  CZ  . PHE B 1 56  ? -5.727  4.006   72.041  1.00   50.03  ? 71  PHE B CZ  1 
ATOM   3456 N  N   . GLY B 1 57  ? -4.938  10.135  70.386  1.00   42.67  ? 72  GLY B N   1 
ATOM   3457 C  CA  . GLY B 1 57  ? -3.988  11.115  69.909  1.00   42.17  ? 72  GLY B CA  1 
ATOM   3458 C  C   . GLY B 1 57  ? -2.689  10.424  69.583  1.00   42.36  ? 72  GLY B C   1 
ATOM   3459 O  O   . GLY B 1 57  ? -2.186  9.629   70.390  1.00   41.86  ? 72  GLY B O   1 
ATOM   3460 N  N   . LEU B 1 58  ? -2.150  10.699  68.395  1.00   42.74  ? 73  LEU B N   1 
ATOM   3461 C  CA  . LEU B 1 58  ? -0.799  10.274  68.045  1.00   42.91  ? 73  LEU B CA  1 
ATOM   3462 C  C   . LEU B 1 58  ? 0.053   11.500  67.886  1.00   44.83  ? 73  LEU B C   1 
ATOM   3463 O  O   . LEU B 1 58  ? -0.420  12.541  67.488  1.00   44.74  ? 73  LEU B O   1 
ATOM   3464 C  CB  . LEU B 1 58  ? -0.790  9.466   66.765  1.00   41.74  ? 73  LEU B CB  1 
ATOM   3465 C  CG  . LEU B 1 58  ? -1.660  8.214   66.832  1.00   42.33  ? 73  LEU B CG  1 
ATOM   3466 C  CD1 . LEU B 1 58  ? -1.928  7.622   65.451  1.00   41.80  ? 73  LEU B CD1 1 
ATOM   3467 C  CD2 . LEU B 1 58  ? -1.024  7.187   67.756  1.00   43.50  ? 73  LEU B CD2 1 
ATOM   3468 N  N   . TYR B 1 59  ? 1.318   11.386  68.237  1.00   49.36  ? 74  TYR B N   1 
ATOM   3469 C  CA  . TYR B 1 59  ? 2.259   12.479  68.041  1.00   53.06  ? 74  TYR B CA  1 
ATOM   3470 C  C   . TYR B 1 59  ? 3.411   11.963  67.216  1.00   57.87  ? 74  TYR B C   1 
ATOM   3471 O  O   . TYR B 1 59  ? 4.189   11.120  67.668  1.00   63.37  ? 74  TYR B O   1 
ATOM   3472 C  CB  . TYR B 1 59  ? 2.756   13.010  69.376  1.00   53.35  ? 74  TYR B CB  1 
ATOM   3473 C  CG  . TYR B 1 59  ? 1.649   13.532  70.251  1.00   51.98  ? 74  TYR B CG  1 
ATOM   3474 C  CD1 . TYR B 1 59  ? 0.844   12.668  70.965  1.00   51.50  ? 74  TYR B CD1 1 
ATOM   3475 C  CD2 . TYR B 1 59  ? 1.412   14.889  70.364  1.00   52.19  ? 74  TYR B CD2 1 
ATOM   3476 C  CE1 . TYR B 1 59  ? -0.168  13.138  71.772  1.00   52.34  ? 74  TYR B CE1 1 
ATOM   3477 C  CE2 . TYR B 1 59  ? 0.400   15.375  71.165  1.00   52.82  ? 74  TYR B CE2 1 
ATOM   3478 C  CZ  . TYR B 1 59  ? -0.390  14.490  71.865  1.00   53.24  ? 74  TYR B CZ  1 
ATOM   3479 O  OH  . TYR B 1 59  ? -1.417  14.948  72.651  1.00   55.36  ? 74  TYR B OH  1 
ATOM   3480 N  N   . ALA B 1 60  ? 3.479   12.436  65.984  1.00   63.45  ? 75  ALA B N   1 
ATOM   3481 C  CA  . ALA B 1 60  ? 4.603   12.168  65.111  1.00   67.88  ? 75  ALA B CA  1 
ATOM   3482 C  C   . ALA B 1 60  ? 4.804   13.419  64.299  1.00   71.92  ? 75  ALA B C   1 
ATOM   3483 O  O   . ALA B 1 60  ? 3.856   13.940  63.711  1.00   79.79  ? 75  ALA B O   1 
ATOM   3484 C  CB  . ALA B 1 60  ? 4.312   10.988  64.210  1.00   67.94  ? 75  ALA B CB  1 
ATOM   3485 N  N   . GLY B 1 61  ? 6.033   13.915  64.276  1.00   76.84  ? 76  GLY B N   1 
ATOM   3486 C  CA  . GLY B 1 61  ? 6.319   15.191  63.649  1.00   80.40  ? 76  GLY B CA  1 
ATOM   3487 C  C   . GLY B 1 61  ? 5.630   16.298  64.423  1.00   84.27  ? 76  GLY B C   1 
ATOM   3488 O  O   . GLY B 1 61  ? 5.160   16.073  65.547  1.00   81.78  ? 76  GLY B O   1 
ATOM   3489 N  N   . PRO B 1 62  ? 5.546   17.499  63.821  1.00   89.91  ? 77  PRO B N   1 
ATOM   3490 C  CA  . PRO B 1 62  ? 4.934   18.631  64.513  1.00   90.01  ? 77  PRO B CA  1 
ATOM   3491 C  C   . PRO B 1 62  ? 3.413   18.542  64.556  1.00   81.83  ? 77  PRO B C   1 
ATOM   3492 O  O   . PRO B 1 62  ? 2.776   19.364  65.214  1.00   82.54  ? 77  PRO B O   1 
ATOM   3493 C  CB  . PRO B 1 62  ? 5.376   19.833  63.673  1.00   93.93  ? 77  PRO B CB  1 
ATOM   3494 C  CG  . PRO B 1 62  ? 5.527   19.285  62.288  1.00   94.73  ? 77  PRO B CG  1 
ATOM   3495 C  CD  . PRO B 1 62  ? 5.928   17.838  62.434  1.00   92.44  ? 77  PRO B CD  1 
ATOM   3496 N  N   . HIS B 1 63  ? 2.842   17.555  63.866  1.00   73.76  ? 78  HIS B N   1 
ATOM   3497 C  CA  . HIS B 1 63  ? 1.396   17.427  63.790  1.00   70.78  ? 78  HIS B CA  1 
ATOM   3498 C  C   . HIS B 1 63  ? 0.813   16.337  64.663  1.00   64.03  ? 78  HIS B C   1 
ATOM   3499 O  O   . HIS B 1 63  ? 1.215   15.164  64.618  1.00   63.79  ? 78  HIS B O   1 
ATOM   3500 C  CB  . HIS B 1 63  ? 0.970   17.202  62.356  1.00   71.53  ? 78  HIS B CB  1 
ATOM   3501 C  CG  . HIS B 1 63  ? 1.389   18.308  61.453  1.00   76.13  ? 78  HIS B CG  1 
ATOM   3502 N  ND1 . HIS B 1 63  ? 0.940   19.601  61.618  1.00   78.04  ? 78  HIS B ND1 1 
ATOM   3503 C  CD2 . HIS B 1 63  ? 2.245   18.329  60.405  1.00   76.32  ? 78  HIS B CD2 1 
ATOM   3504 C  CE1 . HIS B 1 63  ? 1.484   20.369  60.691  1.00   80.12  ? 78  HIS B CE1 1 
ATOM   3505 N  NE2 . HIS B 1 63  ? 2.280   19.622  59.943  1.00   80.20  ? 78  HIS B NE2 1 
ATOM   3506 N  N   . LEU B 1 64  ? -0.158  16.755  65.455  1.00   56.67  ? 79  LEU B N   1 
ATOM   3507 C  CA  . LEU B 1 64  ? -1.013  15.840  66.137  1.00   53.02  ? 79  LEU B CA  1 
ATOM   3508 C  C   . LEU B 1 64  ? -1.829  15.140  65.073  1.00   49.68  ? 79  LEU B C   1 
ATOM   3509 O  O   . LEU B 1 64  ? -2.309  15.772  64.128  1.00   49.09  ? 79  LEU B O   1 
ATOM   3510 C  CB  . LEU B 1 64  ? -1.925  16.615  67.086  1.00   53.65  ? 79  LEU B CB  1 
ATOM   3511 C  CG  . LEU B 1 64  ? -2.872  15.851  68.003  1.00   52.98  ? 79  LEU B CG  1 
ATOM   3512 C  CD1 . LEU B 1 64  ? -2.137  14.913  68.953  1.00   53.42  ? 79  LEU B CD1 1 
ATOM   3513 C  CD2 . LEU B 1 64  ? -3.675  16.879  68.772  1.00   53.02  ? 79  LEU B CD2 1 
ATOM   3514 N  N   . THR B 1 65  ? -1.939  13.826  65.206  1.00   47.69  ? 80  THR B N   1 
ATOM   3515 C  CA  . THR B 1 65  ? -2.874  13.039  64.418  1.00   45.34  ? 80  THR B CA  1 
ATOM   3516 C  C   . THR B 1 65  ? -3.926  12.415  65.354  1.00   44.54  ? 80  THR B C   1 
ATOM   3517 O  O   . THR B 1 65  ? -3.602  11.532  66.173  1.00   42.94  ? 80  THR B O   1 
ATOM   3518 C  CB  . THR B 1 65  ? -2.145  11.942  63.664  1.00   44.56  ? 80  THR B CB  1 
ATOM   3519 O  OG1 . THR B 1 65  ? -1.240  12.544  62.746  1.00   45.51  ? 80  THR B OG1 1 
ATOM   3520 C  CG2 . THR B 1 65  ? -3.116  11.103  62.894  1.00   44.61  ? 80  THR B CG2 1 
ATOM   3521 N  N   . LEU B 1 66  ? -5.172  12.897  65.241  1.00   42.46  ? 81  LEU B N   1 
ATOM   3522 C  CA  . LEU B 1 66  ? -6.270  12.393  66.060  1.00   41.45  ? 81  LEU B CA  1 
ATOM   3523 C  C   . LEU B 1 66  ? -6.981  11.285  65.337  1.00   39.30  ? 81  LEU B C   1 
ATOM   3524 O  O   . LEU B 1 66  ? -7.305  11.431  64.195  1.00   37.90  ? 81  LEU B O   1 
ATOM   3525 C  CB  . LEU B 1 66  ? -7.265  13.509  66.382  1.00   43.00  ? 81  LEU B CB  1 
ATOM   3526 C  CG  . LEU B 1 66  ? -7.328  14.000  67.830  1.00   44.93  ? 81  LEU B CG  1 
ATOM   3527 C  CD1 . LEU B 1 66  ? -5.971  14.417  68.389  1.00   45.58  ? 81  LEU B CD1 1 
ATOM   3528 C  CD2 . LEU B 1 66  ? -8.271  15.182  67.909  1.00   45.81  ? 81  LEU B CD2 1 
ATOM   3529 N  N   . VAL B 1 67  ? -7.249  10.180  66.001  1.00   38.66  ? 82  VAL B N   1 
ATOM   3530 C  CA  . VAL B 1 67  ? -8.058  9.156   65.378  1.00   38.14  ? 82  VAL B CA  1 
ATOM   3531 C  C   . VAL B 1 67  ? -9.468  9.061   65.982  1.00   38.00  ? 82  VAL B C   1 
ATOM   3532 O  O   . VAL B 1 67  ? -9.628  8.703   67.123  1.00   39.19  ? 82  VAL B O   1 
ATOM   3533 C  CB  . VAL B 1 67  ? -7.385  7.786   65.479  1.00   37.96  ? 82  VAL B CB  1 
ATOM   3534 C  CG1 . VAL B 1 67  ? -8.201  6.759   64.678  1.00   38.04  ? 82  VAL B CG1 1 
ATOM   3535 C  CG2 . VAL B 1 67  ? -5.951  7.861   64.997  1.00   37.15  ? 82  VAL B CG2 1 
ATOM   3536 N  N   . VAL B 1 68  ? -10.484 9.311   65.181  1.00   37.85  ? 83  VAL B N   1 
ATOM   3537 C  CA  . VAL B 1 68  ? -11.861 9.251   65.643  1.00   39.06  ? 83  VAL B CA  1 
ATOM   3538 C  C   . VAL B 1 68  ? -12.595 7.965   65.244  1.00   38.04  ? 83  VAL B C   1 
ATOM   3539 O  O   . VAL B 1 68  ? -12.729 7.664   64.060  1.00   37.10  ? 83  VAL B O   1 
ATOM   3540 C  CB  . VAL B 1 68  ? -12.673 10.435  65.104  1.00   40.53  ? 83  VAL B CB  1 
ATOM   3541 C  CG1 . VAL B 1 68  ? -13.990 10.526  65.859  1.00   41.67  ? 83  VAL B CG1 1 
ATOM   3542 C  CG2 . VAL B 1 68  ? -11.897 11.743  65.273  1.00   40.89  ? 83  VAL B CG2 1 
ATOM   3543 N  N   . SER B 1 69  ? -13.093 7.232   66.240  1.00   37.35  ? 84  SER B N   1 
ATOM   3544 C  CA  . SER B 1 69  ? -13.706 5.927   66.006  1.00   37.28  ? 84  SER B CA  1 
ATOM   3545 C  C   . SER B 1 69  ? -15.166 5.815   66.504  1.00   37.81  ? 84  SER B C   1 
ATOM   3546 O  O   . SER B 1 69  ? -15.655 4.716   66.714  1.00   38.23  ? 84  SER B O   1 
ATOM   3547 C  CB  . SER B 1 69  ? -12.854 4.837   66.683  1.00   37.40  ? 84  SER B CB  1 
ATOM   3548 O  OG  . SER B 1 69  ? -11.652 4.575   65.977  1.00   36.09  ? 84  SER B OG  1 
ATOM   3549 N  N   . GLU B 1 70  ? -15.866 6.926   66.680  1.00   37.66  ? 85  GLU B N   1 
ATOM   3550 C  CA  . GLU B 1 70  ? -17.230 6.857   67.153  1.00   38.62  ? 85  GLU B CA  1 
ATOM   3551 C  C   . GLU B 1 70  ? -18.072 7.858   66.398  1.00   39.07  ? 85  GLU B C   1 
ATOM   3552 O  O   . GLU B 1 70  ? -17.617 8.962   66.093  1.00   38.57  ? 85  GLU B O   1 
ATOM   3553 C  CB  . GLU B 1 70  ? -17.275 7.114   68.662  1.00   39.72  ? 85  GLU B CB  1 
ATOM   3554 C  CG  . GLU B 1 70  ? -18.614 6.875   69.374  1.00   40.59  ? 85  GLU B CG  1 
ATOM   3555 C  CD  . GLU B 1 70  ? -19.555 8.058   69.358  1.00   41.11  ? 85  GLU B CD  1 
ATOM   3556 O  OE1 . GLU B 1 70  ? -19.115 9.196   69.125  1.00   40.34  ? 85  GLU B OE1 1 
ATOM   3557 O  OE2 . GLU B 1 70  ? -20.760 7.841   69.585  1.00   42.14  ? 85  GLU B OE2 1 
ATOM   3558 N  N   . ILE B 1 71  ? -19.313 7.451   66.112  1.00   39.89  ? 86  ILE B N   1 
ATOM   3559 C  CA  . ILE B 1 71  ? -20.239 8.231   65.295  1.00   40.23  ? 86  ILE B CA  1 
ATOM   3560 C  C   . ILE B 1 71  ? -20.458 9.680   65.734  1.00   41.33  ? 86  ILE B C   1 
ATOM   3561 O  O   . ILE B 1 71  ? -20.444 10.585  64.919  1.00   41.32  ? 86  ILE B O   1 
ATOM   3562 C  CB  . ILE B 1 71  ? -21.609 7.514   65.129  1.00   41.21  ? 86  ILE B CB  1 
ATOM   3563 C  CG1 . ILE B 1 71  ? -22.470 8.289   64.149  1.00   42.04  ? 86  ILE B CG1 1 
ATOM   3564 C  CG2 . ILE B 1 71  ? -22.357 7.368   66.431  1.00   42.33  ? 86  ILE B CG2 1 
ATOM   3565 C  CD1 . ILE B 1 71  ? -21.819 8.436   62.795  1.00   41.05  ? 86  ILE B CD1 1 
ATOM   3566 N  N   . GLY B 1 72  ? -20.691 9.909   67.015  1.00   42.99  ? 87  GLY B N   1 
ATOM   3567 C  CA  . GLY B 1 72  ? -20.877 11.268  67.509  1.00   44.11  ? 87  GLY B CA  1 
ATOM   3568 C  C   . GLY B 1 72  ? -19.671 12.079  67.131  1.00   43.06  ? 87  GLY B C   1 
ATOM   3569 O  O   . GLY B 1 72  ? -19.775 13.146  66.528  1.00   43.54  ? 87  GLY B O   1 
ATOM   3570 N  N   . LEU B 1 73  ? -18.510 11.536  67.445  1.00   42.22  ? 88  LEU B N   1 
ATOM   3571 C  CA  . LEU B 1 73  ? -17.275 12.252  67.205  1.00   41.86  ? 88  LEU B CA  1 
ATOM   3572 C  C   . LEU B 1 73  ? -17.025 12.486  65.752  1.00   41.87  ? 88  LEU B C   1 
ATOM   3573 O  O   . LEU B 1 73  ? -16.585 13.576  65.424  1.00   42.22  ? 88  LEU B O   1 
ATOM   3574 C  CB  . LEU B 1 73  ? -16.090 11.533  67.815  1.00   40.67  ? 88  LEU B CB  1 
ATOM   3575 C  CG  . LEU B 1 73  ? -16.024 11.703  69.317  1.00   41.44  ? 88  LEU B CG  1 
ATOM   3576 C  CD1 . LEU B 1 73  ? -15.044 10.702  69.897  1.00   41.20  ? 88  LEU B CD1 1 
ATOM   3577 C  CD2 . LEU B 1 73  ? -15.612 13.124  69.681  1.00   41.61  ? 88  LEU B CD2 1 
ATOM   3578 N  N   . VAL B 1 74  ? -17.325 11.507  64.885  1.00   42.50  ? 89  VAL B N   1 
ATOM   3579 C  CA  . VAL B 1 74  ? -17.089 11.703  63.450  1.00   43.20  ? 89  VAL B CA  1 
ATOM   3580 C  C   . VAL B 1 74  ? -18.130 12.605  62.807  1.00   45.33  ? 89  VAL B C   1 
ATOM   3581 O  O   . VAL B 1 74  ? -17.819 13.276  61.830  1.00   46.11  ? 89  VAL B O   1 
ATOM   3582 C  CB  . VAL B 1 74  ? -16.930 10.419  62.589  1.00   43.26  ? 89  VAL B CB  1 
ATOM   3583 C  CG1 . VAL B 1 74  ? -16.699 9.166   63.424  1.00   43.32  ? 89  VAL B CG1 1 
ATOM   3584 C  CG2 . VAL B 1 74  ? -18.082 10.230  61.637  1.00   43.67  ? 89  VAL B CG2 1 
ATOM   3585 N  N   . ARG B 1 75  ? -19.351 12.629  63.332  1.00   47.91  ? 90  ARG B N   1 
ATOM   3586 C  CA  . ARG B 1 75  ? -20.350 13.578  62.828  1.00   50.64  ? 90  ARG B CA  1 
ATOM   3587 C  C   . ARG B 1 75  ? -19.960 14.980  63.240  1.00   50.56  ? 90  ARG B C   1 
ATOM   3588 O  O   . ARG B 1 75  ? -20.247 15.933  62.522  1.00   51.68  ? 90  ARG B O   1 
ATOM   3589 C  CB  . ARG B 1 75  ? -21.779 13.280  63.314  1.00   53.86  ? 90  ARG B CB  1 
ATOM   3590 C  CG  . ARG B 1 75  ? -22.398 11.995  62.787  1.00   55.21  ? 90  ARG B CG  1 
ATOM   3591 C  CD  . ARG B 1 75  ? -23.886 11.913  63.098  1.00   59.70  ? 90  ARG B CD  1 
ATOM   3592 N  NE  . ARG B 1 75  ? -24.694 12.306  61.932  1.00   64.38  ? 90  ARG B NE  1 
ATOM   3593 C  CZ  . ARG B 1 75  ? -25.103 11.475  60.965  1.00   67.21  ? 90  ARG B CZ  1 
ATOM   3594 N  NH1 . ARG B 1 75  ? -24.830 10.164  61.008  1.00   67.52  ? 90  ARG B NH1 1 
ATOM   3595 N  NH2 . ARG B 1 75  ? -25.799 11.952  59.939  1.00   69.68  ? 90  ARG B NH2 1 
ATOM   3596 N  N   . GLU B 1 76  ? -19.315 15.125  64.396  1.00   49.40  ? 91  GLU B N   1 
ATOM   3597 C  CA  . GLU B 1 76  ? -18.856 16.442  64.786  1.00   49.17  ? 91  GLU B CA  1 
ATOM   3598 C  C   . GLU B 1 76  ? -17.720 16.895  63.899  1.00   46.72  ? 91  GLU B C   1 
ATOM   3599 O  O   . GLU B 1 76  ? -17.597 18.068  63.639  1.00   46.84  ? 91  GLU B O   1 
ATOM   3600 C  CB  . GLU B 1 76  ? -18.422 16.470  66.233  1.00   50.45  ? 91  GLU B CB  1 
ATOM   3601 C  CG  . GLU B 1 76  ? -17.945 17.844  66.692  1.00   51.61  ? 91  GLU B CG  1 
ATOM   3602 C  CD  . GLU B 1 76  ? -17.440 17.820  68.103  1.00   51.56  ? 91  GLU B CD  1 
ATOM   3603 O  OE1 . GLU B 1 76  ? -17.624 16.769  68.753  1.00   51.29  ? 91  GLU B OE1 1 
ATOM   3604 O  OE2 . GLU B 1 76  ? -16.860 18.842  68.536  1.00   52.21  ? 91  GLU B OE2 1 
ATOM   3605 N  N   . VAL B 1 77  ? -16.908 15.963  63.423  1.00   45.14  ? 92  VAL B N   1 
ATOM   3606 C  CA  . VAL B 1 77  ? -15.810 16.288  62.501  1.00   44.43  ? 92  VAL B CA  1 
ATOM   3607 C  C   . VAL B 1 77  ? -16.314 16.656  61.113  1.00   45.41  ? 92  VAL B C   1 
ATOM   3608 O  O   . VAL B 1 77  ? -16.021 17.737  60.601  1.00   46.91  ? 92  VAL B O   1 
ATOM   3609 C  CB  . VAL B 1 77  ? -14.841 15.108  62.359  1.00   43.30  ? 92  VAL B CB  1 
ATOM   3610 C  CG1 . VAL B 1 77  ? -13.813 15.359  61.258  1.00   42.88  ? 92  VAL B CG1 1 
ATOM   3611 C  CG2 . VAL B 1 77  ? -14.110 14.872  63.678  1.00   43.92  ? 92  VAL B CG2 1 
ATOM   3612 N  N   . LEU B 1 78  ? -17.075 15.757  60.502  1.00   44.69  ? 93  LEU B N   1 
ATOM   3613 C  CA  . LEU B 1 78  ? -17.537 15.975  59.165  1.00   44.79  ? 93  LEU B CA  1 
ATOM   3614 C  C   . LEU B 1 78  ? -18.584 17.102  59.130  1.00   47.27  ? 93  LEU B C   1 
ATOM   3615 O  O   . LEU B 1 78  ? -18.376 18.092  58.455  1.00   48.52  ? 93  LEU B O   1 
ATOM   3616 C  CB  . LEU B 1 78  ? -18.077 14.670  58.584  1.00   44.33  ? 93  LEU B CB  1 
ATOM   3617 C  CG  . LEU B 1 78  ? -17.085 13.494  58.528  1.00   42.81  ? 93  LEU B CG  1 
ATOM   3618 C  CD1 . LEU B 1 78  ? -17.708 12.229  57.945  1.00   42.26  ? 93  LEU B CD1 1 
ATOM   3619 C  CD2 . LEU B 1 78  ? -15.847 13.855  57.718  1.00   42.33  ? 93  LEU B CD2 1 
ATOM   3620 N  N   . LEU B 1 79  ? -19.686 16.973  59.868  1.00   48.46  ? 94  LEU B N   1 
ATOM   3621 C  CA  . LEU B 1 79  ? -20.767 17.982  59.837  1.00   50.32  ? 94  LEU B CA  1 
ATOM   3622 C  C   . LEU B 1 79  ? -20.594 19.194  60.770  1.00   51.91  ? 94  LEU B C   1 
ATOM   3623 O  O   . LEU B 1 79  ? -20.274 20.288  60.277  1.00   52.82  ? 94  LEU B O   1 
ATOM   3624 C  CB  . LEU B 1 79  ? -22.135 17.351  60.132  1.00   51.34  ? 94  LEU B CB  1 
ATOM   3625 C  CG  . LEU B 1 79  ? -22.937 16.656  59.030  1.00   51.19  ? 94  LEU B CG  1 
ATOM   3626 C  CD1 . LEU B 1 79  ? -22.647 17.256  57.660  1.00   50.75  ? 94  LEU B CD1 1 
ATOM   3627 C  CD2 . LEU B 1 79  ? -22.672 15.159  59.058  1.00   49.72  ? 94  LEU B CD2 1 
ATOM   3628 N  N   . GLN B 1 80  ? -20.829 19.016  62.084  1.00   51.28  ? 95  GLN B N   1 
ATOM   3629 C  CA  . GLN B 1 80  ? -20.880 20.141  63.016  1.00   52.57  ? 95  GLN B CA  1 
ATOM   3630 C  C   . GLN B 1 80  ? -19.784 21.174  62.774  1.00   53.90  ? 95  GLN B C   1 
ATOM   3631 O  O   . GLN B 1 80  ? -20.080 22.365  62.678  1.00   55.66  ? 95  GLN B O   1 
ATOM   3632 C  CB  . GLN B 1 80  ? -20.816 19.679  64.483  1.00   51.85  ? 95  GLN B CB  1 
ATOM   3633 C  CG  . GLN B 1 80  ? -21.066 20.801  65.493  1.00   52.20  ? 95  GLN B CG  1 
ATOM   3634 C  CD  . GLN B 1 80  ? -20.944 20.376  66.939  1.00   51.50  ? 95  GLN B CD  1 
ATOM   3635 O  OE1 . GLN B 1 80  ? -20.978 19.191  67.268  1.00   50.39  ? 95  GLN B OE1 1 
ATOM   3636 N  NE2 . GLN B 1 80  ? -20.807 21.356  67.818  1.00   52.07  ? 95  GLN B NE2 1 
ATOM   3637 N  N   . ARG B 1 81  ? -18.525 20.732  62.698  1.00   53.94  ? 96  ARG B N   1 
ATOM   3638 C  CA  . ARG B 1 81  ? -17.421 21.642  62.364  1.00   54.84  ? 96  ARG B CA  1 
ATOM   3639 C  C   . ARG B 1 81  ? -16.630 21.174  61.134  1.00   55.11  ? 96  ARG B C   1 
ATOM   3640 O  O   . ARG B 1 81  ? -15.403 21.198  61.105  1.00   55.05  ? 96  ARG B O   1 
ATOM   3641 C  CB  . ARG B 1 81  ? -16.542 21.924  63.586  1.00   54.44  ? 96  ARG B CB  1 
ATOM   3642 C  CG  . ARG B 1 81  ? -16.706 20.951  64.743  1.00   53.64  ? 96  ARG B CG  1 
ATOM   3643 C  CD  . ARG B 1 81  ? -16.098 21.490  66.028  1.00   53.22  ? 96  ARG B CD  1 
ATOM   3644 N  NE  . ARG B 1 81  ? -17.136 22.079  66.847  1.00   54.83  ? 96  ARG B NE  1 
ATOM   3645 C  CZ  . ARG B 1 81  ? -17.045 22.341  68.143  1.00   55.29  ? 96  ARG B CZ  1 
ATOM   3646 N  NH1 . ARG B 1 81  ? -15.937 22.101  68.812  1.00   54.94  ? 96  ARG B NH1 1 
ATOM   3647 N  NH2 . ARG B 1 81  ? -18.082 22.861  68.775  1.00   57.17  ? 96  ARG B NH2 1 
ATOM   3648 N  N   . GLY B 1 82  ? -17.380 20.802  60.099  1.00   57.12  ? 97  GLY B N   1 
ATOM   3649 C  CA  . GLY B 1 82  ? -16.840 20.316  58.836  1.00   57.17  ? 97  GLY B CA  1 
ATOM   3650 C  C   . GLY B 1 82  ? -15.963 21.275  58.071  1.00   58.62  ? 97  GLY B C   1 
ATOM   3651 O  O   . GLY B 1 82  ? -15.019 20.841  57.379  1.00   58.06  ? 97  GLY B O   1 
ATOM   3652 N  N   . ARG B 1 83  ? -16.275 22.565  58.167  1.00   60.19  ? 98  ARG B N   1 
ATOM   3653 C  CA  . ARG B 1 83  ? -15.471 23.585  57.505  1.00   62.68  ? 98  ARG B CA  1 
ATOM   3654 C  C   . ARG B 1 83  ? -14.125 23.757  58.174  1.00   60.50  ? 98  ARG B C   1 
ATOM   3655 O  O   . ARG B 1 83  ? -13.122 23.980  57.504  1.00   62.07  ? 98  ARG B O   1 
ATOM   3656 C  CB  . ARG B 1 83  ? -16.175 24.925  57.527  1.00   67.42  ? 98  ARG B CB  1 
ATOM   3657 C  CG  . ARG B 1 83  ? -15.363 26.061  56.920  1.00   70.64  ? 98  ARG B CG  1 
ATOM   3658 C  CD  . ARG B 1 83  ? -16.204 27.323  56.858  1.00   76.42  ? 98  ARG B CD  1 
ATOM   3659 N  NE  . ARG B 1 83  ? -16.615 27.840  58.179  1.00   77.95  ? 98  ARG B NE  1 
ATOM   3660 C  CZ  . ARG B 1 83  ? -15.890 28.672  58.920  1.00   79.92  ? 98  ARG B CZ  1 
ATOM   3661 N  NH1 . ARG B 1 83  ? -14.690 29.078  58.508  1.00   81.47  ? 98  ARG B NH1 1 
ATOM   3662 N  NH2 . ARG B 1 83  ? -16.359 29.092  60.085  1.00   82.03  ? 98  ARG B NH2 1 
ATOM   3663 N  N   . GLU B 1 84  ? -14.122 23.679  59.496  1.00   58.14  ? 99  GLU B N   1 
ATOM   3664 C  CA  . GLU B 1 84  ? -12.918 23.862  60.285  1.00   55.93  ? 99  GLU B CA  1 
ATOM   3665 C  C   . GLU B 1 84  ? -11.983 22.683  60.132  1.00   52.91  ? 99  GLU B C   1 
ATOM   3666 O  O   . GLU B 1 84  ? -10.774 22.849  60.274  1.00   53.21  ? 99  GLU B O   1 
ATOM   3667 C  CB  . GLU B 1 84  ? -13.256 24.029  61.776  1.00   56.92  ? 99  GLU B CB  1 
ATOM   3668 C  CG  . GLU B 1 84  ? -14.061 25.275  62.128  1.00   59.25  ? 99  GLU B CG  1 
ATOM   3669 C  CD  . GLU B 1 84  ? -15.531 24.985  62.372  1.00   59.83  ? 99  GLU B CD  1 
ATOM   3670 O  OE1 . GLU B 1 84  ? -16.179 24.330  61.519  1.00   57.75  ? 99  GLU B OE1 1 
ATOM   3671 O  OE2 . GLU B 1 84  ? -16.035 25.428  63.428  1.00   61.44  ? 99  GLU B OE2 1 
ATOM   3672 N  N   . PHE B 1 85  ? -12.533 21.495  59.882  1.00   50.53  ? 100 PHE B N   1 
ATOM   3673 C  CA  . PHE B 1 85  ? -11.724 20.314  59.582  1.00   48.56  ? 100 PHE B CA  1 
ATOM   3674 C  C   . PHE B 1 85  ? -11.663 19.981  58.071  1.00   48.09  ? 100 PHE B C   1 
ATOM   3675 O  O   . PHE B 1 85  ? -11.436 18.838  57.718  1.00   46.31  ? 100 PHE B O   1 
ATOM   3676 C  CB  . PHE B 1 85  ? -12.266 19.102  60.337  1.00   47.44  ? 100 PHE B CB  1 
ATOM   3677 C  CG  . PHE B 1 85  ? -12.058 19.167  61.806  1.00   48.67  ? 100 PHE B CG  1 
ATOM   3678 C  CD1 . PHE B 1 85  ? -10.778 18.972  62.354  1.00   48.86  ? 100 PHE B CD1 1 
ATOM   3679 C  CD2 . PHE B 1 85  ? -13.125 19.395  62.675  1.00   50.42  ? 100 PHE B CD2 1 
ATOM   3680 C  CE1 . PHE B 1 85  ? -10.566 19.027  63.720  1.00   47.85  ? 100 PHE B CE1 1 
ATOM   3681 C  CE2 . PHE B 1 85  ? -12.916 19.436  64.053  1.00   50.36  ? 100 PHE B CE2 1 
ATOM   3682 C  CZ  . PHE B 1 85  ? -11.636 19.256  64.569  1.00   49.02  ? 100 PHE B CZ  1 
ATOM   3683 N  N   . ALA B 1 86  ? -11.839 20.966  57.191  1.00   49.52  ? 101 ALA B N   1 
ATOM   3684 C  CA  . ALA B 1 86  ? -11.843 20.721  55.724  1.00   51.12  ? 101 ALA B CA  1 
ATOM   3685 C  C   . ALA B 1 86  ? -10.470 20.900  55.081  1.00   50.78  ? 101 ALA B C   1 
ATOM   3686 O  O   . ALA B 1 86  ? -10.361 21.053  53.852  1.00   50.30  ? 101 ALA B O   1 
ATOM   3687 C  CB  . ALA B 1 86  ? -12.865 21.614  55.007  1.00   52.33  ? 101 ALA B CB  1 
ATOM   3688 N  N   . GLY B 1 87  ? -9.429  20.877  55.906  1.00   50.01  ? 102 GLY B N   1 
ATOM   3689 C  CA  . GLY B 1 87  ? -8.076  21.027  55.416  1.00   49.35  ? 102 GLY B CA  1 
ATOM   3690 C  C   . GLY B 1 87  ? -7.602  19.696  54.916  1.00   47.59  ? 102 GLY B C   1 
ATOM   3691 O  O   . GLY B 1 87  ? -8.201  18.671  55.233  1.00   46.33  ? 102 GLY B O   1 
ATOM   3692 N  N   . ARG B 1 88  ? -6.548  19.727  54.111  1.00   48.03  ? 103 ARG B N   1 
ATOM   3693 C  CA  . ARG B 1 88  ? -5.948  18.523  53.554  1.00   48.03  ? 103 ARG B CA  1 
ATOM   3694 C  C   . ARG B 1 88  ? -4.434  18.616  53.682  1.00   48.48  ? 103 ARG B C   1 
ATOM   3695 O  O   . ARG B 1 88  ? -3.862  19.697  53.528  1.00   51.42  ? 103 ARG B O   1 
ATOM   3696 C  CB  . ARG B 1 88  ? -6.322  18.369  52.075  1.00   48.84  ? 103 ARG B CB  1 
ATOM   3697 C  CG  . ARG B 1 88  ? -7.776  18.009  51.798  1.00   48.81  ? 103 ARG B CG  1 
ATOM   3698 C  CD  . ARG B 1 88  ? -8.177  16.688  52.453  1.00   48.66  ? 103 ARG B CD  1 
ATOM   3699 N  NE  . ARG B 1 88  ? -9.316  16.055  51.787  1.00   49.54  ? 103 ARG B NE  1 
ATOM   3700 C  CZ  . ARG B 1 88  ? -10.152 15.180  52.350  1.00   49.74  ? 103 ARG B CZ  1 
ATOM   3701 N  NH1 . ARG B 1 88  ? -10.025 14.797  53.615  1.00   49.12  ? 103 ARG B NH1 1 
ATOM   3702 N  NH2 . ARG B 1 88  ? -11.140 14.682  51.632  1.00   51.07  ? 103 ARG B NH2 1 
ATOM   3703 N  N   . PRO B 1 89  ? -3.778  17.486  53.953  1.00   47.28  ? 104 PRO B N   1 
ATOM   3704 C  CA  . PRO B 1 89  ? -2.329  17.402  54.166  1.00   47.82  ? 104 PRO B CA  1 
ATOM   3705 C  C   . PRO B 1 89  ? -1.440  17.415  52.892  1.00   49.05  ? 104 PRO B C   1 
ATOM   3706 O  O   . PRO B 1 89  ? -1.787  16.786  51.876  1.00   46.87  ? 104 PRO B O   1 
ATOM   3707 C  CB  . PRO B 1 89  ? -2.188  16.048  54.846  1.00   46.51  ? 104 PRO B CB  1 
ATOM   3708 C  CG  . PRO B 1 89  ? -3.275  15.226  54.238  1.00   45.59  ? 104 PRO B CG  1 
ATOM   3709 C  CD  . PRO B 1 89  ? -4.427  16.172  54.103  1.00   45.99  ? 104 PRO B CD  1 
ATOM   3710 N  N   . LYS B 1 90  ? -0.295  18.099  52.970  1.00   51.74  ? 105 LYS B N   1 
ATOM   3711 C  CA  . LYS B 1 90  ? 0.706   18.101  51.874  1.00   55.96  ? 105 LYS B CA  1 
ATOM   3712 C  C   . LYS B 1 90  ? 1.778   17.004  52.043  1.00   57.60  ? 105 LYS B C   1 
ATOM   3713 O  O   . LYS B 1 90  ? 2.712   17.139  52.830  1.00   53.67  ? 105 LYS B O   1 
ATOM   3714 C  CB  . LYS B 1 90  ? 1.360   19.484  51.716  1.00   57.41  ? 105 LYS B CB  1 
ATOM   3715 C  CG  . LYS B 1 90  ? 2.611   19.475  50.854  1.00   60.67  ? 105 LYS B CG  1 
ATOM   3716 C  CD  . LYS B 1 90  ? 3.043   20.865  50.405  1.00   63.70  ? 105 LYS B CD  1 
ATOM   3717 C  CE  . LYS B 1 90  ? 2.196   21.384  49.251  1.00   64.28  ? 105 LYS B CE  1 
ATOM   3718 N  NZ  . LYS B 1 90  ? 2.326   20.543  48.042  1.00   63.60  ? 105 LYS B NZ  1 
ATOM   3719 N  N   . MET B 1 91  ? 1.615   15.919  51.285  1.00   64.48  ? 106 MET B N   1 
ATOM   3720 C  CA  . MET B 1 91  ? 2.594   14.820  51.220  1.00   67.97  ? 106 MET B CA  1 
ATOM   3721 C  C   . MET B 1 91  ? 3.287   14.883  49.845  1.00   65.02  ? 106 MET B C   1 
ATOM   3722 O  O   . MET B 1 91  ? 2.831   15.559  48.919  1.00   61.01  ? 106 MET B O   1 
ATOM   3723 C  CB  . MET B 1 91  ? 1.917   13.439  51.402  1.00   75.34  ? 106 MET B CB  1 
ATOM   3724 C  CG  . MET B 1 91  ? 0.668   13.438  52.287  1.00   86.85  ? 106 MET B CG  1 
ATOM   3725 S  SD  . MET B 1 91  ? -0.216  11.856  52.377  1.00   106.97 ? 106 MET B SD  1 
ATOM   3726 C  CE  . MET B 1 91  ? -1.810  12.332  53.069  1.00   100.70 ? 106 MET B CE  1 
ATOM   3727 N  N   . VAL B 1 92  ? 4.380   14.151  49.712  1.00   60.46  ? 107 VAL B N   1 
ATOM   3728 C  CA  . VAL B 1 92  ? 5.099   14.118  48.478  1.00   58.70  ? 107 VAL B CA  1 
ATOM   3729 C  C   . VAL B 1 92  ? 4.348   13.270  47.468  1.00   54.71  ? 107 VAL B C   1 
ATOM   3730 O  O   . VAL B 1 92  ? 4.217   13.642  46.285  1.00   54.00  ? 107 VAL B O   1 
ATOM   3731 C  CB  . VAL B 1 92  ? 6.554   13.633  48.697  1.00   63.39  ? 107 VAL B CB  1 
ATOM   3732 C  CG1 . VAL B 1 92  ? 6.861   12.302  48.023  1.00   66.00  ? 107 VAL B CG1 1 
ATOM   3733 C  CG2 . VAL B 1 92  ? 7.519   14.664  48.161  1.00   65.19  ? 107 VAL B CG2 1 
ATOM   3734 N  N   . THR B 1 93  ? 3.867   12.126  47.925  1.00   50.13  ? 108 THR B N   1 
ATOM   3735 C  CA  . THR B 1 93  ? 3.135   11.245  47.059  1.00   50.12  ? 108 THR B CA  1 
ATOM   3736 C  C   . THR B 1 93  ? 1.961   11.976  46.426  1.00   50.26  ? 108 THR B C   1 
ATOM   3737 O  O   . THR B 1 93  ? 1.796   11.943  45.202  1.00   52.29  ? 108 THR B O   1 
ATOM   3738 C  CB  . THR B 1 93  ? 2.621   10.030  47.821  1.00   50.09  ? 108 THR B CB  1 
ATOM   3739 O  OG1 . THR B 1 93  ? 2.499   10.367  49.211  1.00   54.43  ? 108 THR B OG1 1 
ATOM   3740 C  CG2 . THR B 1 93  ? 3.574   8.886   47.686  1.00   50.99  ? 108 THR B CG2 1 
ATOM   3741 N  N   . THR B 1 94  ? 1.169   12.657  47.249  1.00   47.55  ? 109 THR B N   1 
ATOM   3742 C  CA  . THR B 1 94  ? -0.018  13.329  46.765  1.00   47.03  ? 109 THR B CA  1 
ATOM   3743 C  C   . THR B 1 94  ? 0.352   14.490  45.888  1.00   47.33  ? 109 THR B C   1 
ATOM   3744 O  O   . THR B 1 94  ? -0.429  14.879  45.039  1.00   47.80  ? 109 THR B O   1 
ATOM   3745 C  CB  . THR B 1 94  ? -0.900  13.888  47.898  1.00   47.57  ? 109 THR B CB  1 
ATOM   3746 O  OG1 . THR B 1 94  ? -0.171  14.856  48.667  1.00   48.30  ? 109 THR B OG1 1 
ATOM   3747 C  CG2 . THR B 1 94  ? -1.407  12.766  48.796  1.00   47.50  ? 109 THR B CG2 1 
ATOM   3748 N  N   . ASP B 1 95  ? 1.525   15.067  46.111  1.00   47.64  ? 110 ASP B N   1 
ATOM   3749 C  CA  . ASP B 1 95  ? 1.964   16.182  45.301  1.00   48.92  ? 110 ASP B CA  1 
ATOM   3750 C  C   . ASP B 1 95  ? 2.175   15.727  43.890  1.00   50.21  ? 110 ASP B C   1 
ATOM   3751 O  O   . ASP B 1 95  ? 1.686   16.361  42.959  1.00   51.59  ? 110 ASP B O   1 
ATOM   3752 C  CB  . ASP B 1 95  ? 3.235   16.816  45.853  1.00   49.79  ? 110 ASP B CB  1 
ATOM   3753 C  CG  . ASP B 1 95  ? 2.949   17.803  46.969  1.00   50.32  ? 110 ASP B CG  1 
ATOM   3754 O  OD1 . ASP B 1 95  ? 1.753   17.911  47.362  1.00   51.10  ? 110 ASP B OD1 1 
ATOM   3755 O  OD2 . ASP B 1 95  ? 3.899   18.475  47.453  1.00   48.96  ? 110 ASP B OD2 1 
ATOM   3756 N  N   . LEU B 1 96  ? 2.869   14.612  43.727  1.00   49.76  ? 111 LEU B N   1 
ATOM   3757 C  CA  . LEU B 1 96  ? 3.119   14.106  42.390  1.00   51.10  ? 111 LEU B CA  1 
ATOM   3758 C  C   . LEU B 1 96  ? 1.797   13.729  41.712  1.00   51.55  ? 111 LEU B C   1 
ATOM   3759 O  O   . LEU B 1 96  ? 1.642   13.882  40.499  1.00   56.25  ? 111 LEU B O   1 
ATOM   3760 C  CB  . LEU B 1 96  ? 4.076   12.902  42.407  1.00   50.71  ? 111 LEU B CB  1 
ATOM   3761 C  CG  . LEU B 1 96  ? 5.439   13.081  43.080  1.00   50.79  ? 111 LEU B CG  1 
ATOM   3762 C  CD1 . LEU B 1 96  ? 6.241   11.795  43.010  1.00   51.03  ? 111 LEU B CD1 1 
ATOM   3763 C  CD2 . LEU B 1 96  ? 6.215   14.223  42.461  1.00   52.42  ? 111 LEU B CD2 1 
ATOM   3764 N  N   . LEU B 1 97  ? 0.837   13.239  42.483  1.00   49.70  ? 112 LEU B N   1 
ATOM   3765 C  CA  . LEU B 1 97  ? -0.442  12.847  41.906  1.00   48.28  ? 112 LEU B CA  1 
ATOM   3766 C  C   . LEU B 1 97  ? -1.279  14.008  41.426  1.00   48.03  ? 112 LEU B C   1 
ATOM   3767 O  O   . LEU B 1 97  ? -2.091  13.817  40.541  1.00   48.35  ? 112 LEU B O   1 
ATOM   3768 C  CB  . LEU B 1 97  ? -1.251  12.049  42.910  1.00   47.03  ? 112 LEU B CB  1 
ATOM   3769 C  CG  . LEU B 1 97  ? -1.030  10.546  42.929  1.00   46.91  ? 112 LEU B CG  1 
ATOM   3770 C  CD1 . LEU B 1 97  ? 0.250   10.115  42.245  1.00   47.48  ? 112 LEU B CD1 1 
ATOM   3771 C  CD2 . LEU B 1 97  ? -1.052  10.044  44.368  1.00   47.27  ? 112 LEU B CD2 1 
ATOM   3772 N  N   . THR B 1 98  ? -1.075  15.193  42.001  1.00   48.32  ? 113 THR B N   1 
ATOM   3773 C  CA  . THR B 1 98  ? -2.023  16.303  41.877  1.00   49.34  ? 113 THR B CA  1 
ATOM   3774 C  C   . THR B 1 98  ? -1.410  17.668  41.541  1.00   50.48  ? 113 THR B C   1 
ATOM   3775 O  O   . THR B 1 98  ? -2.076  18.685  41.643  1.00   50.80  ? 113 THR B O   1 
ATOM   3776 C  CB  . THR B 1 98  ? -2.802  16.476  43.205  1.00   48.44  ? 113 THR B CB  1 
ATOM   3777 O  OG1 . THR B 1 98  ? -1.907  16.970  44.219  1.00   48.23  ? 113 THR B OG1 1 
ATOM   3778 C  CG2 . THR B 1 98  ? -3.442  15.151  43.662  1.00   46.25  ? 113 THR B CG2 1 
ATOM   3779 N  N   . GLN B 1 99  ? -0.146  17.705  41.170  1.00   53.34  ? 114 GLN B N   1 
ATOM   3780 C  CA  . GLN B 1 99  ? 0.524   18.971  40.861  1.00   56.94  ? 114 GLN B CA  1 
ATOM   3781 C  C   . GLN B 1 99  ? 0.394   19.933  42.047  1.00   57.73  ? 114 GLN B C   1 
ATOM   3782 O  O   . GLN B 1 99  ? 0.000   21.099  41.894  1.00   59.34  ? 114 GLN B O   1 
ATOM   3783 C  CB  . GLN B 1 99  ? -0.068  19.557  39.563  1.00   59.33  ? 114 GLN B CB  1 
ATOM   3784 C  CG  . GLN B 1 99  ? 0.901   20.305  38.654  1.00   61.42  ? 114 GLN B CG  1 
ATOM   3785 C  CD  . GLN B 1 99  ? 0.406   20.332  37.212  1.00   63.91  ? 114 GLN B CD  1 
ATOM   3786 O  OE1 . GLN B 1 99  ? 0.606   19.389  36.451  1.00   65.36  ? 114 GLN B OE1 1 
ATOM   3787 N  NE2 . GLN B 1 99  ? -0.245  21.409  36.837  1.00   65.26  ? 114 GLN B NE2 1 
ATOM   3788 N  N   . GLY B 1 100 ? 0.702   19.420  43.238  1.00   56.41  ? 115 GLY B N   1 
ATOM   3789 C  CA  . GLY B 1 100 ? 0.618   20.213  44.462  1.00   55.74  ? 115 GLY B CA  1 
ATOM   3790 C  C   . GLY B 1 100 ? -0.809  20.562  44.869  1.00   55.62  ? 115 GLY B C   1 
ATOM   3791 O  O   . GLY B 1 100 ? -1.092  21.691  45.267  1.00   58.28  ? 115 GLY B O   1 
ATOM   3792 N  N   . GLY B 1 101 ? -1.718  19.602  44.804  1.00   52.82  ? 116 GLY B N   1 
ATOM   3793 C  CA  . GLY B 1 101 ? -3.094  19.874  45.191  1.00   52.59  ? 116 GLY B CA  1 
ATOM   3794 C  C   . GLY B 1 101 ? -3.806  20.867  44.287  1.00   53.63  ? 116 GLY B C   1 
ATOM   3795 O  O   . GLY B 1 101 ? -4.517  21.735  44.758  1.00   52.84  ? 116 GLY B O   1 
ATOM   3796 N  N   . LYS B 1 102 ? -3.604  20.741  42.977  1.00   56.16  ? 117 LYS B N   1 
ATOM   3797 C  CA  . LYS B 1 102 ? -4.497  21.391  41.983  1.00   59.05  ? 117 LYS B CA  1 
ATOM   3798 C  C   . LYS B 1 102 ? -5.647  20.448  41.571  1.00   57.47  ? 117 LYS B C   1 
ATOM   3799 O  O   . LYS B 1 102 ? -6.290  20.672  40.545  1.00   57.48  ? 117 LYS B O   1 
ATOM   3800 C  CB  . LYS B 1 102 ? -3.715  21.859  40.744  1.00   61.49  ? 117 LYS B CB  1 
ATOM   3801 C  CG  . LYS B 1 102 ? -2.741  22.995  41.033  1.00   64.33  ? 117 LYS B CG  1 
ATOM   3802 C  CD  . LYS B 1 102 ? -2.059  23.505  39.778  1.00   67.31  ? 117 LYS B CD  1 
ATOM   3803 C  CE  . LYS B 1 102 ? -1.066  24.625  40.063  1.00   70.47  ? 117 LYS B CE  1 
ATOM   3804 N  NZ  . LYS B 1 102 ? 0.149   24.158  40.791  1.00   71.33  ? 117 LYS B NZ  1 
ATOM   3805 N  N   . ASP B 1 103 ? -5.873  19.402  42.388  1.00   54.01  ? 118 ASP B N   1 
ATOM   3806 C  CA  . ASP B 1 103 ? -6.977  18.455  42.249  1.00   50.87  ? 118 ASP B CA  1 
ATOM   3807 C  C   . ASP B 1 103 ? -8.099  18.881  43.186  1.00   50.86  ? 118 ASP B C   1 
ATOM   3808 O  O   . ASP B 1 103 ? -8.191  20.063  43.506  1.00   52.67  ? 118 ASP B O   1 
ATOM   3809 C  CB  . ASP B 1 103 ? -6.487  17.042  42.571  1.00   48.29  ? 118 ASP B CB  1 
ATOM   3810 C  CG  . ASP B 1 103 ? -6.351  16.782  44.064  1.00   46.48  ? 118 ASP B CG  1 
ATOM   3811 O  OD1 . ASP B 1 103 ? -5.988  17.694  44.839  1.00   46.61  ? 118 ASP B OD1 1 
ATOM   3812 O  OD2 . ASP B 1 103 ? -6.628  15.649  44.471  1.00   43.82  ? 118 ASP B OD2 1 
ATOM   3813 N  N   . ILE B 1 104 ? -8.951  17.940  43.605  1.00   49.68  ? 119 ILE B N   1 
ATOM   3814 C  CA  . ILE B 1 104 ? -9.941  18.175  44.657  1.00   49.36  ? 119 ILE B CA  1 
ATOM   3815 C  C   . ILE B 1 104 ? -9.658  17.413  45.948  1.00   48.30  ? 119 ILE B C   1 
ATOM   3816 O  O   . ILE B 1 104 ? -9.851  17.953  47.043  1.00   50.08  ? 119 ILE B O   1 
ATOM   3817 C  CB  . ILE B 1 104 ? -11.336 17.731  44.196  1.00   50.41  ? 119 ILE B CB  1 
ATOM   3818 C  CG1 . ILE B 1 104 ? -11.852 18.621  43.046  1.00   52.10  ? 119 ILE B CG1 1 
ATOM   3819 C  CG2 . ILE B 1 104 ? -12.330 17.703  45.360  1.00   50.30  ? 119 ILE B CG2 1 
ATOM   3820 C  CD1 . ILE B 1 104 ? -12.468 19.940  43.464  1.00   53.31  ? 119 ILE B CD1 1 
ATOM   3821 N  N   . ALA B 1 105 ? -9.259  16.148  45.850  1.00   46.37  ? 120 ALA B N   1 
ATOM   3822 C  CA  . ALA B 1 105 ? -9.127  15.309  47.059  1.00   44.92  ? 120 ALA B CA  1 
ATOM   3823 C  C   . ALA B 1 105 ? -8.119  15.846  48.104  1.00   43.98  ? 120 ALA B C   1 
ATOM   3824 O  O   . ALA B 1 105 ? -8.428  15.900  49.298  1.00   43.80  ? 120 ALA B O   1 
ATOM   3825 C  CB  . ALA B 1 105 ? -8.795  13.868  46.685  1.00   43.34  ? 120 ALA B CB  1 
ATOM   3826 N  N   . PHE B 1 106 ? -6.943  16.263  47.646  1.00   43.58  ? 121 PHE B N   1 
ATOM   3827 C  CA  . PHE B 1 106 ? -5.869  16.713  48.528  1.00   43.42  ? 121 PHE B CA  1 
ATOM   3828 C  C   . PHE B 1 106 ? -5.587  18.195  48.389  1.00   44.50  ? 121 PHE B C   1 
ATOM   3829 O  O   . PHE B 1 106 ? -4.476  18.648  48.654  1.00   42.68  ? 121 PHE B O   1 
ATOM   3830 C  CB  . PHE B 1 106 ? -4.612  15.891  48.255  1.00   43.23  ? 121 PHE B CB  1 
ATOM   3831 C  CG  . PHE B 1 106 ? -4.882  14.418  48.206  1.00   43.23  ? 121 PHE B CG  1 
ATOM   3832 C  CD1 . PHE B 1 106 ? -4.891  13.669  49.359  1.00   43.16  ? 121 PHE B CD1 1 
ATOM   3833 C  CD2 . PHE B 1 106 ? -5.193  13.791  47.015  1.00   43.20  ? 121 PHE B CD2 1 
ATOM   3834 C  CE1 . PHE B 1 106 ? -5.185  12.314  49.319  1.00   42.62  ? 121 PHE B CE1 1 
ATOM   3835 C  CE2 . PHE B 1 106 ? -5.483  12.438  46.972  1.00   42.26  ? 121 PHE B CE2 1 
ATOM   3836 C  CZ  . PHE B 1 106 ? -5.485  11.699  48.124  1.00   41.69  ? 121 PHE B CZ  1 
ATOM   3837 N  N   . ALA B 1 107 ? -6.605  18.944  47.976  1.00   46.82  ? 122 ALA B N   1 
ATOM   3838 C  CA  . ALA B 1 107 ? -6.544  20.407  47.949  1.00   50.28  ? 122 ALA B CA  1 
ATOM   3839 C  C   . ALA B 1 107 ? -7.175  20.994  49.214  1.00   52.95  ? 122 ALA B C   1 
ATOM   3840 O  O   . ALA B 1 107 ? -8.154  20.452  49.726  1.00   53.58  ? 122 ALA B O   1 
ATOM   3841 C  CB  . ALA B 1 107 ? -7.277  20.938  46.728  1.00   51.32  ? 122 ALA B CB  1 
ATOM   3842 N  N   . ASP B 1 108 ? -6.631  22.104  49.708  1.00   54.57  ? 123 ASP B N   1 
ATOM   3843 C  CA  . ASP B 1 108 ? -7.210  22.771  50.861  1.00   55.34  ? 123 ASP B CA  1 
ATOM   3844 C  C   . ASP B 1 108 ? -8.543  23.392  50.527  1.00   58.04  ? 123 ASP B C   1 
ATOM   3845 O  O   . ASP B 1 108 ? -8.780  23.822  49.393  1.00   62.01  ? 123 ASP B O   1 
ATOM   3846 C  CB  . ASP B 1 108 ? -6.276  23.859  51.386  1.00   56.45  ? 123 ASP B CB  1 
ATOM   3847 C  CG  . ASP B 1 108 ? -5.452  23.391  52.555  1.00   56.00  ? 123 ASP B CG  1 
ATOM   3848 O  OD1 . ASP B 1 108 ? -5.948  22.525  53.315  1.00   54.62  ? 123 ASP B OD1 1 
ATOM   3849 O  OD2 . ASP B 1 108 ? -4.315  23.888  52.703  1.00   55.34  ? 123 ASP B OD2 1 
ATOM   3850 N  N   . TYR B 1 109 ? -9.413  23.452  51.524  1.00   58.13  ? 124 TYR B N   1 
ATOM   3851 C  CA  . TYR B 1 109 ? -10.670 24.173  51.390  1.00   60.08  ? 124 TYR B CA  1 
ATOM   3852 C  C   . TYR B 1 109 ? -10.336 25.651  51.203  1.00   62.69  ? 124 TYR B C   1 
ATOM   3853 O  O   . TYR B 1 109 ? -9.499  26.184  51.922  1.00   64.19  ? 124 TYR B O   1 
ATOM   3854 C  CB  . TYR B 1 109 ? -11.499 23.949  52.641  1.00   59.54  ? 124 TYR B CB  1 
ATOM   3855 C  CG  . TYR B 1 109 ? -12.871 24.528  52.651  1.00   60.28  ? 124 TYR B CG  1 
ATOM   3856 C  CD1 . TYR B 1 109 ? -13.090 25.863  52.977  1.00   62.39  ? 124 TYR B CD1 1 
ATOM   3857 C  CD2 . TYR B 1 109 ? -13.965 23.724  52.401  1.00   60.97  ? 124 TYR B CD2 1 
ATOM   3858 C  CE1 . TYR B 1 109 ? -14.374 26.386  53.018  1.00   64.76  ? 124 TYR B CE1 1 
ATOM   3859 C  CE2 . TYR B 1 109 ? -15.253 24.231  52.429  1.00   63.28  ? 124 TYR B CE2 1 
ATOM   3860 C  CZ  . TYR B 1 109 ? -15.459 25.557  52.742  1.00   65.27  ? 124 TYR B CZ  1 
ATOM   3861 O  OH  . TYR B 1 109 ? -16.761 26.020  52.763  1.00   69.03  ? 124 TYR B OH  1 
ATOM   3862 N  N   . SER B 1 110 ? -10.995 26.300  50.243  1.00   64.79  ? 125 SER B N   1 
ATOM   3863 C  CA  . SER B 1 110 ? -10.638 27.654  49.801  1.00   65.61  ? 125 SER B CA  1 
ATOM   3864 C  C   . SER B 1 110 ? -11.689 28.225  48.832  1.00   66.80  ? 125 SER B C   1 
ATOM   3865 O  O   . SER B 1 110 ? -12.425 27.475  48.182  1.00   65.95  ? 125 SER B O   1 
ATOM   3866 C  CB  . SER B 1 110 ? -9.276  27.635  49.084  1.00   65.83  ? 125 SER B CB  1 
ATOM   3867 O  OG  . SER B 1 110 ? -9.344  26.970  47.817  1.00   65.36  ? 125 SER B OG  1 
ATOM   3868 N  N   . PRO B 1 111 ? -11.750 29.558  48.708  1.00   67.92  ? 126 PRO B N   1 
ATOM   3869 C  CA  . PRO B 1 111 ? -12.563 30.084  47.615  1.00   69.45  ? 126 PRO B CA  1 
ATOM   3870 C  C   . PRO B 1 111 ? -12.248 29.385  46.271  1.00   68.95  ? 126 PRO B C   1 
ATOM   3871 O  O   . PRO B 1 111 ? -13.181 28.979  45.550  1.00   70.20  ? 126 PRO B O   1 
ATOM   3872 C  CB  . PRO B 1 111 ? -12.198 31.580  47.570  1.00   71.21  ? 126 PRO B CB  1 
ATOM   3873 C  CG  . PRO B 1 111 ? -11.131 31.806  48.602  1.00   70.56  ? 126 PRO B CG  1 
ATOM   3874 C  CD  . PRO B 1 111 ? -11.123 30.621  49.513  1.00   68.24  ? 126 PRO B CD  1 
ATOM   3875 N  N   . LEU B 1 112 ? -10.968 29.220  45.936  1.00   66.16  ? 127 LEU B N   1 
ATOM   3876 C  CA  . LEU B 1 112 ? -10.640 28.502  44.707  1.00   66.00  ? 127 LEU B CA  1 
ATOM   3877 C  C   . LEU B 1 112 ? -11.330 27.143  44.718  1.00   64.07  ? 127 LEU B C   1 
ATOM   3878 O  O   . LEU B 1 112 ? -12.055 26.789  43.794  1.00   64.73  ? 127 LEU B O   1 
ATOM   3879 C  CB  . LEU B 1 112 ? -9.123  28.342  44.522  1.00   65.69  ? 127 LEU B CB  1 
ATOM   3880 C  CG  . LEU B 1 112 ? -8.614  27.700  43.209  1.00   66.04  ? 127 LEU B CG  1 
ATOM   3881 C  CD1 . LEU B 1 112 ? -9.283  28.297  41.982  1.00   68.06  ? 127 LEU B CD1 1 
ATOM   3882 C  CD2 . LEU B 1 112 ? -7.093  27.797  43.036  1.00   65.27  ? 127 LEU B CD2 1 
ATOM   3883 N  N   . TRP B 1 113 ? -11.144 26.409  45.805  1.00   62.66  ? 128 TRP B N   1 
ATOM   3884 C  CA  . TRP B 1 113 ? -11.652 25.047  45.899  1.00   61.00  ? 128 TRP B CA  1 
ATOM   3885 C  C   . TRP B 1 113 ? -13.177 24.949  45.841  1.00   61.81  ? 128 TRP B C   1 
ATOM   3886 O  O   . TRP B 1 113 ? -13.713 24.019  45.249  1.00   60.70  ? 128 TRP B O   1 
ATOM   3887 C  CB  . TRP B 1 113 ? -11.134 24.381  47.175  1.00   59.12  ? 128 TRP B CB  1 
ATOM   3888 C  CG  . TRP B 1 113 ? -11.480 22.922  47.266  1.00   57.42  ? 128 TRP B CG  1 
ATOM   3889 C  CD1 . TRP B 1 113 ? -10.828 21.894  46.662  1.00   56.76  ? 128 TRP B CD1 1 
ATOM   3890 C  CD2 . TRP B 1 113 ? -12.571 22.332  47.996  1.00   56.75  ? 128 TRP B CD2 1 
ATOM   3891 N  NE1 . TRP B 1 113 ? -11.434 20.699  46.973  1.00   55.66  ? 128 TRP B NE1 1 
ATOM   3892 C  CE2 . TRP B 1 113 ? -12.504 20.941  47.794  1.00   55.17  ? 128 TRP B CE2 1 
ATOM   3893 C  CE3 . TRP B 1 113 ? -13.602 22.847  48.793  1.00   57.52  ? 128 TRP B CE3 1 
ATOM   3894 C  CZ2 . TRP B 1 113 ? -13.419 20.057  48.371  1.00   53.85  ? 128 TRP B CZ2 1 
ATOM   3895 C  CZ3 . TRP B 1 113 ? -14.502 21.969  49.360  1.00   56.11  ? 128 TRP B CZ3 1 
ATOM   3896 C  CH2 . TRP B 1 113 ? -14.403 20.589  49.145  1.00   54.35  ? 128 TRP B CH2 1 
ATOM   3897 N  N   . LYS B 1 114 ? -13.875 25.892  46.461  1.00   64.34  ? 129 LYS B N   1 
ATOM   3898 C  CA  . LYS B 1 114 ? -15.329 25.847  46.470  1.00   65.86  ? 129 LYS B CA  1 
ATOM   3899 C  C   . LYS B 1 114 ? -15.864 25.944  45.049  1.00   68.42  ? 129 LYS B C   1 
ATOM   3900 O  O   . LYS B 1 114 ? -16.750 25.173  44.676  1.00   68.23  ? 129 LYS B O   1 
ATOM   3901 C  CB  . LYS B 1 114 ? -15.918 26.961  47.320  1.00   67.69  ? 129 LYS B CB  1 
ATOM   3902 C  CG  . LYS B 1 114 ? -15.491 26.939  48.777  1.00   67.46  ? 129 LYS B CG  1 
ATOM   3903 C  CD  . LYS B 1 114 ? -16.674 27.048  49.731  1.00   69.08  ? 129 LYS B CD  1 
ATOM   3904 C  CE  . LYS B 1 114 ? -17.397 28.389  49.648  1.00   72.54  ? 129 LYS B CE  1 
ATOM   3905 N  NZ  . LYS B 1 114 ? -16.647 29.458  50.366  1.00   73.36  ? 129 LYS B NZ  1 
ATOM   3906 N  N   . ASN B 1 115 ? -15.324 26.881  44.260  1.00   70.75  ? 130 ASN B N   1 
ATOM   3907 C  CA  . ASN B 1 115 ? -15.730 27.047  42.843  1.00   72.59  ? 130 ASN B CA  1 
ATOM   3908 C  C   . ASN B 1 115 ? -15.374 25.808  42.068  1.00   69.75  ? 130 ASN B C   1 
ATOM   3909 O  O   . ASN B 1 115 ? -16.161 25.289  41.263  1.00   69.34  ? 130 ASN B O   1 
ATOM   3910 C  CB  . ASN B 1 115 ? -15.024 28.243  42.172  1.00   74.79  ? 130 ASN B CB  1 
ATOM   3911 C  CG  . ASN B 1 115 ? -15.515 29.592  42.686  1.00   77.83  ? 130 ASN B CG  1 
ATOM   3912 O  OD1 . ASN B 1 115 ? -16.653 29.726  43.148  1.00   78.66  ? 130 ASN B OD1 1 
ATOM   3913 N  ND2 . ASN B 1 115 ? -14.647 30.602  42.610  1.00   78.81  ? 130 ASN B ND2 1 
ATOM   3914 N  N   . HIS B 1 116 ? -14.165 25.332  42.327  1.00   66.68  ? 131 HIS B N   1 
ATOM   3915 C  CA  . HIS B 1 116 ? -13.688 24.147  41.663  1.00   64.82  ? 131 HIS B CA  1 
ATOM   3916 C  C   . HIS B 1 116 ? -14.650 22.972  41.889  1.00   65.14  ? 131 HIS B C   1 
ATOM   3917 O  O   . HIS B 1 116 ? -15.045 22.291  40.941  1.00   65.10  ? 131 HIS B O   1 
ATOM   3918 C  CB  . HIS B 1 116 ? -12.271 23.840  42.111  1.00   61.69  ? 131 HIS B CB  1 
ATOM   3919 C  CG  . HIS B 1 116 ? -11.602 22.789  41.295  1.00   60.30  ? 131 HIS B CG  1 
ATOM   3920 N  ND1 . HIS B 1 116 ? -10.455 22.152  41.706  1.00   58.84  ? 131 HIS B ND1 1 
ATOM   3921 C  CD2 . HIS B 1 116 ? -11.935 22.237  40.106  1.00   61.01  ? 131 HIS B CD2 1 
ATOM   3922 C  CE1 . HIS B 1 116 ? -10.097 21.264  40.796  1.00   58.96  ? 131 HIS B CE1 1 
ATOM   3923 N  NE2 . HIS B 1 116 ? -10.979 21.296  39.815  1.00   60.50  ? 131 HIS B NE2 1 
ATOM   3924 N  N   . ARG B 1 117 ? -15.078 22.778  43.133  1.00   66.14  ? 132 ARG B N   1 
ATOM   3925 C  CA  . ARG B 1 117 ? -15.961 21.658  43.462  1.00   66.05  ? 132 ARG B CA  1 
ATOM   3926 C  C   . ARG B 1 117 ? -17.378 21.787  42.890  1.00   68.71  ? 132 ARG B C   1 
ATOM   3927 O  O   . ARG B 1 117 ? -17.951 20.794  42.435  1.00   68.86  ? 132 ARG B O   1 
ATOM   3928 C  CB  . ARG B 1 117 ? -16.030 21.458  44.971  1.00   64.81  ? 132 ARG B CB  1 
ATOM   3929 C  CG  . ARG B 1 117 ? -16.557 20.093  45.367  1.00   63.68  ? 132 ARG B CG  1 
ATOM   3930 C  CD  . ARG B 1 117 ? -16.717 19.968  46.881  1.00   63.21  ? 132 ARG B CD  1 
ATOM   3931 N  NE  . ARG B 1 117 ? -17.220 18.644  47.233  1.00   62.06  ? 132 ARG B NE  1 
ATOM   3932 C  CZ  . ARG B 1 117 ? -18.476 18.249  47.036  1.00   63.02  ? 132 ARG B CZ  1 
ATOM   3933 N  NH1 . ARG B 1 117 ? -19.384 19.070  46.506  1.00   63.63  ? 132 ARG B NH1 1 
ATOM   3934 N  NH2 . ARG B 1 117 ? -18.823 17.014  47.361  1.00   63.66  ? 132 ARG B NH2 1 
ATOM   3935 N  N   . ARG B 1 118 ? -17.940 22.997  42.929  1.00   72.46  ? 133 ARG B N   1 
ATOM   3936 C  CA  . ARG B 1 118 ? -19.309 23.249  42.431  1.00   75.45  ? 133 ARG B CA  1 
ATOM   3937 C  C   . ARG B 1 118 ? -19.383 22.921  40.949  1.00   78.11  ? 133 ARG B C   1 
ATOM   3938 O  O   . ARG B 1 118 ? -20.383 22.387  40.463  1.00   80.94  ? 133 ARG B O   1 
ATOM   3939 C  CB  . ARG B 1 118 ? -19.710 24.709  42.639  1.00   77.31  ? 133 ARG B CB  1 
ATOM   3940 C  CG  . ARG B 1 118 ? -21.210 24.962  42.659  1.00   80.59  ? 133 ARG B CG  1 
ATOM   3941 C  CD  . ARG B 1 118 ? -21.486 26.456  42.770  1.00   85.19  ? 133 ARG B CD  1 
ATOM   3942 N  NE  . ARG B 1 118 ? -20.893 27.025  43.990  1.00   87.94  ? 133 ARG B NE  1 
ATOM   3943 C  CZ  . ARG B 1 118 ? -20.277 28.209  44.090  1.00   89.94  ? 133 ARG B CZ  1 
ATOM   3944 N  NH1 . ARG B 1 118 ? -20.126 29.005  43.031  1.00   91.91  ? 133 ARG B NH1 1 
ATOM   3945 N  NH2 . ARG B 1 118 ? -19.789 28.596  45.270  1.00   88.58  ? 133 ARG B NH2 1 
ATOM   3946 N  N   . LEU B 1 119 ? -18.311 23.238  40.234  1.00   76.46  ? 134 LEU B N   1 
ATOM   3947 C  CA  . LEU B 1 119 ? -18.224 22.888  38.849  1.00   77.02  ? 134 LEU B CA  1 
ATOM   3948 C  C   . LEU B 1 119 ? -18.332 21.370  38.688  1.00   75.16  ? 134 LEU B C   1 
ATOM   3949 O  O   . LEU B 1 119 ? -19.153 20.867  37.909  1.00   76.68  ? 134 LEU B O   1 
ATOM   3950 C  CB  . LEU B 1 119 ? -16.907 23.405  38.292  1.00   77.81  ? 134 LEU B CB  1 
ATOM   3951 C  CG  . LEU B 1 119 ? -16.651 23.187  36.799  1.00   79.73  ? 134 LEU B CG  1 
ATOM   3952 C  CD1 . LEU B 1 119 ? -17.768 23.762  35.928  1.00   80.82  ? 134 LEU B CD1 1 
ATOM   3953 C  CD2 . LEU B 1 119 ? -15.296 23.793  36.449  1.00   79.40  ? 134 LEU B CD2 1 
ATOM   3954 N  N   . VAL B 1 120 ? -17.520 20.646  39.449  1.00   72.08  ? 135 VAL B N   1 
ATOM   3955 C  CA  . VAL B 1 120 ? -17.468 19.190  39.340  1.00   70.12  ? 135 VAL B CA  1 
ATOM   3956 C  C   . VAL B 1 120 ? -18.803 18.539  39.715  1.00   71.00  ? 135 VAL B C   1 
ATOM   3957 O  O   . VAL B 1 120 ? -19.327 17.723  38.968  1.00   69.70  ? 135 VAL B O   1 
ATOM   3958 C  CB  . VAL B 1 120 ? -16.343 18.595  40.210  1.00   66.64  ? 135 VAL B CB  1 
ATOM   3959 C  CG1 . VAL B 1 120 ? -16.387 17.077  40.161  1.00   64.68  ? 135 VAL B CG1 1 
ATOM   3960 C  CG2 . VAL B 1 120 ? -14.976 19.090  39.746  1.00   66.14  ? 135 VAL B CG2 1 
ATOM   3961 N  N   . HIS B 1 121 ? -19.353 18.897  40.871  1.00   73.85  ? 136 HIS B N   1 
ATOM   3962 C  CA  . HIS B 1 121 ? -20.624 18.311  41.301  1.00   76.44  ? 136 HIS B CA  1 
ATOM   3963 C  C   . HIS B 1 121 ? -21.713 18.602  40.268  1.00   79.61  ? 136 HIS B C   1 
ATOM   3964 O  O   . HIS B 1 121 ? -22.495 17.717  39.904  1.00   81.63  ? 136 HIS B O   1 
ATOM   3965 C  CB  . HIS B 1 121 ? -21.046 18.815  42.690  1.00   78.06  ? 136 HIS B CB  1 
ATOM   3966 C  CG  . HIS B 1 121 ? -22.367 18.268  43.149  1.00   80.04  ? 136 HIS B CG  1 
ATOM   3967 N  ND1 . HIS B 1 121 ? -22.477 17.213  44.031  1.00   76.71  ? 136 HIS B ND1 1 
ATOM   3968 C  CD2 . HIS B 1 121 ? -23.635 18.612  42.816  1.00   83.75  ? 136 HIS B CD2 1 
ATOM   3969 C  CE1 . HIS B 1 121 ? -23.752 16.930  44.221  1.00   79.89  ? 136 HIS B CE1 1 
ATOM   3970 N  NE2 . HIS B 1 121 ? -24.476 17.762  43.491  1.00   84.92  ? 136 HIS B NE2 1 
ATOM   3971 N  N   . SER B 1 122 ? -21.756 19.847  39.797  1.00   82.02  ? 137 SER B N   1 
ATOM   3972 C  CA  . SER B 1 122 ? -22.692 20.255  38.739  1.00   82.87  ? 137 SER B CA  1 
ATOM   3973 C  C   . SER B 1 122 ? -22.565 19.391  37.489  1.00   82.98  ? 137 SER B C   1 
ATOM   3974 O  O   . SER B 1 122 ? -23.568 18.991  36.895  1.00   84.70  ? 137 SER B O   1 
ATOM   3975 C  CB  . SER B 1 122 ? -22.448 21.713  38.356  1.00   84.54  ? 137 SER B CB  1 
ATOM   3976 O  OG  . SER B 1 122 ? -22.764 21.937  37.001  1.00   88.46  ? 137 SER B OG  1 
ATOM   3977 N  N   . SER B 1 123 ? -21.330 19.120  37.076  1.00   80.75  ? 138 SER B N   1 
ATOM   3978 C  CA  . SER B 1 123 ? -21.114 18.301  35.905  1.00   79.53  ? 138 SER B CA  1 
ATOM   3979 C  C   . SER B 1 123 ? -21.615 16.888  36.175  1.00   77.83  ? 138 SER B C   1 
ATOM   3980 O  O   . SER B 1 123 ? -22.526 16.434  35.498  1.00   78.29  ? 138 SER B O   1 
ATOM   3981 C  CB  . SER B 1 123 ? -19.650 18.328  35.494  1.00   79.48  ? 138 SER B CB  1 
ATOM   3982 O  OG  . SER B 1 123 ? -19.253 19.661  35.213  1.00   80.58  ? 138 SER B OG  1 
ATOM   3983 N  N   . PHE B 1 124 ? -21.082 16.218  37.196  1.00   75.93  ? 139 PHE B N   1 
ATOM   3984 C  CA  . PHE B 1 124 ? -21.556 14.867  37.547  1.00   75.51  ? 139 PHE B CA  1 
ATOM   3985 C  C   . PHE B 1 124 ? -23.066 14.746  37.719  1.00   76.99  ? 139 PHE B C   1 
ATOM   3986 O  O   . PHE B 1 124 ? -23.634 13.692  37.412  1.00   73.24  ? 139 PHE B O   1 
ATOM   3987 C  CB  . PHE B 1 124 ? -20.929 14.370  38.847  1.00   74.63  ? 139 PHE B CB  1 
ATOM   3988 C  CG  . PHE B 1 124 ? -19.489 13.976  38.728  1.00   75.79  ? 139 PHE B CG  1 
ATOM   3989 C  CD1 . PHE B 1 124 ? -19.009 13.309  37.600  1.00   74.66  ? 139 PHE B CD1 1 
ATOM   3990 C  CD2 . PHE B 1 124 ? -18.610 14.243  39.776  1.00   73.72  ? 139 PHE B CD2 1 
ATOM   3991 C  CE1 . PHE B 1 124 ? -17.674 12.952  37.517  1.00   75.38  ? 139 PHE B CE1 1 
ATOM   3992 C  CE2 . PHE B 1 124 ? -17.278 13.886  39.691  1.00   73.67  ? 139 PHE B CE2 1 
ATOM   3993 C  CZ  . PHE B 1 124 ? -16.805 13.245  38.558  1.00   73.83  ? 139 PHE B CZ  1 
ATOM   3994 N  N   . THR B 1 125 ? -23.694 15.797  38.259  1.00   80.01  ? 140 THR B N   1 
ATOM   3995 C  CA  . THR B 1 125 ? -25.144 15.812  38.449  1.00   83.28  ? 140 THR B CA  1 
ATOM   3996 C  C   . THR B 1 125 ? -25.893 15.930  37.117  1.00   87.43  ? 140 THR B C   1 
ATOM   3997 O  O   . THR B 1 125 ? -27.008 15.426  37.039  1.00   91.92  ? 140 THR B O   1 
ATOM   3998 C  CB  . THR B 1 125 ? -25.625 16.932  39.403  1.00   83.94  ? 140 THR B CB  1 
ATOM   3999 O  OG1 . THR B 1 125 ? -24.859 16.912  40.611  1.00   82.96  ? 140 THR B OG1 1 
ATOM   4000 C  CG2 . THR B 1 125 ? -27.103 16.750  39.762  1.00   84.16  ? 140 THR B CG2 1 
ATOM   4001 N  N   . LEU B 1 126 ? -25.322 16.562  36.077  1.00   88.45  ? 141 LEU B N   1 
ATOM   4002 C  CA  . LEU B 1 126 ? -25.957 16.540  34.730  1.00   91.53  ? 141 LEU B CA  1 
ATOM   4003 C  C   . LEU B 1 126 ? -25.945 15.100  34.191  1.00   94.41  ? 141 LEU B C   1 
ATOM   4004 O  O   . LEU B 1 126 ? -25.543 14.822  33.063  1.00   94.65  ? 141 LEU B O   1 
ATOM   4005 C  CB  . LEU B 1 126 ? -25.303 17.536  33.752  1.00   90.63  ? 141 LEU B CB  1 
ATOM   4006 C  CG  . LEU B 1 126 ? -25.883 17.635  32.321  1.00   91.48  ? 141 LEU B CG  1 
ATOM   4007 C  CD1 . LEU B 1 126 ? -26.449 19.009  31.985  1.00   93.52  ? 141 LEU B CD1 1 
ATOM   4008 C  CD2 . LEU B 1 126 ? -24.868 17.210  31.264  1.00   89.73  ? 141 LEU B CD2 1 
ATOM   4009 N  N   . PHE B 1 127 ? -26.393 14.197  35.062  1.00   98.19  ? 142 PHE B N   1 
ATOM   4010 C  CA  . PHE B 1 127 ? -26.497 12.750  34.837  1.00   97.41  ? 142 PHE B CA  1 
ATOM   4011 C  C   . PHE B 1 127 ? -27.565 12.165  35.816  1.00   97.55  ? 142 PHE B C   1 
ATOM   4012 O  O   . PHE B 1 127 ? -28.062 11.055  35.633  1.00   97.03  ? 142 PHE B O   1 
ATOM   4013 C  CB  . PHE B 1 127 ? -25.130 12.073  34.944  1.00   90.62  ? 142 PHE B CB  1 
ATOM   4014 C  CG  . PHE B 1 127 ? -24.100 12.637  33.997  1.00   90.84  ? 142 PHE B CG  1 
ATOM   4015 C  CD1 . PHE B 1 127 ? -23.957 12.139  32.717  1.00   93.65  ? 142 PHE B CD1 1 
ATOM   4016 C  CD2 . PHE B 1 127 ? -23.277 13.684  34.379  1.00   90.51  ? 142 PHE B CD2 1 
ATOM   4017 C  CE1 . PHE B 1 127 ? -22.995 12.658  31.849  1.00   94.49  ? 142 PHE B CE1 1 
ATOM   4018 C  CE2 . PHE B 1 127 ? -22.328 14.215  33.508  1.00   90.76  ? 142 PHE B CE2 1 
ATOM   4019 C  CZ  . PHE B 1 127 ? -22.181 13.699  32.246  1.00   90.24  ? 142 PHE B CZ  1 
ATOM   4020 N  N   . GLY B 1 128 ? -27.904 12.923  36.860  1.00   99.08  ? 143 GLY B N   1 
ATOM   4021 C  CA  . GLY B 1 128 ? -29.236 12.879  37.462  1.00   101.62 ? 143 GLY B CA  1 
ATOM   4022 C  C   . GLY B 1 128 ? -30.231 13.454  36.472  1.00   107.02 ? 143 GLY B C   1 
ATOM   4023 O  O   . GLY B 1 128 ? -31.432 13.188  36.560  1.00   110.06 ? 143 GLY B O   1 
ATOM   4024 N  N   . GLU B 1 129 ? -29.736 14.294  35.561  1.00   110.46 ? 144 GLU B N   1 
ATOM   4025 C  CA  . GLU B 1 129 ? -30.359 14.464  34.249  1.00   115.46 ? 144 GLU B CA  1 
ATOM   4026 C  C   . GLU B 1 129 ? -29.320 14.006  33.225  1.00   116.64 ? 144 GLU B C   1 
ATOM   4027 O  O   . GLU B 1 129 ? -28.967 12.829  33.193  1.00   119.05 ? 144 GLU B O   1 
ATOM   4028 C  CB  . GLU B 1 129 ? -30.838 15.909  34.019  1.00   117.29 ? 144 GLU B CB  1 
ATOM   4029 C  CG  . GLU B 1 129 ? -31.469 16.203  32.656  1.00   121.99 ? 144 GLU B CG  1 
ATOM   4030 C  CD  . GLU B 1 129 ? -32.556 15.217  32.247  1.00   126.56 ? 144 GLU B CD  1 
ATOM   4031 O  OE1 . GLU B 1 129 ? -32.536 14.062  32.727  1.00   127.09 ? 144 GLU B OE1 1 
ATOM   4032 O  OE2 . GLU B 1 129 ? -33.429 15.594  31.425  1.00   125.29 ? 144 GLU B OE2 1 
ATOM   4033 N  N   . GLY B 1 130 ? -28.806 14.917  32.407  1.00   116.82 ? 145 GLY B N   1 
ATOM   4034 C  CA  . GLY B 1 130 ? -27.803 14.584  31.422  1.00   110.94 ? 145 GLY B CA  1 
ATOM   4035 C  C   . GLY B 1 130 ? -28.007 13.583  30.309  1.00   107.05 ? 145 GLY B C   1 
ATOM   4036 O  O   . GLY B 1 130 ? -27.055 12.906  29.990  1.00   106.97 ? 145 GLY B O   1 
ATOM   4037 N  N   . SER B 1 131 ? -29.205 13.343  29.784  1.00   105.75 ? 146 SER B N   1 
ATOM   4038 C  CA  . SER B 1 131 ? -30.396 13.015  30.535  1.00   103.06 ? 146 SER B CA  1 
ATOM   4039 C  C   . SER B 1 131 ? -30.121 11.561  30.900  1.00   97.35  ? 146 SER B C   1 
ATOM   4040 O  O   . SER B 1 131 ? -30.387 11.116  31.998  1.00   95.72  ? 146 SER B O   1 
ATOM   4041 C  CB  . SER B 1 131 ? -31.654 13.077  29.652  1.00   106.59 ? 146 SER B CB  1 
ATOM   4042 O  OG  . SER B 1 131 ? -31.639 14.176  28.758  1.00   107.80 ? 146 SER B OG  1 
ATOM   4043 N  N   . ASN B 1 132 ? -29.603 10.830  29.922  1.00   96.22  ? 147 ASN B N   1 
ATOM   4044 C  CA  . ASN B 1 132 ? -29.171 9.467   30.083  1.00   93.67  ? 147 ASN B CA  1 
ATOM   4045 C  C   . ASN B 1 132 ? -27.766 9.289   29.489  1.00   94.28  ? 147 ASN B C   1 
ATOM   4046 O  O   . ASN B 1 132 ? -27.443 8.207   29.010  1.00   95.17  ? 147 ASN B O   1 
ATOM   4047 C  CB  . ASN B 1 132 ? -30.160 8.496   29.436  0.0000 73.20  ? 147 ASN B CB  1 
ATOM   4048 C  CG  . ASN B 1 132 ? -31.457 8.381   30.213  0.0000 74.56  ? 147 ASN B CG  1 
ATOM   4049 O  OD1 . ASN B 1 132 ? -31.504 8.662   31.410  0.0000 73.61  ? 147 ASN B OD1 1 
ATOM   4050 N  ND2 . ASN B 1 132 ? -32.520 7.966   29.533  0.0000 76.95  ? 147 ASN B ND2 1 
ATOM   4051 N  N   . LYS B 1 133 ? -26.932 10.338  29.514  1.00   96.64  ? 148 LYS B N   1 
ATOM   4052 C  CA  . LYS B 1 133 ? -25.534 10.227  29.047  1.00   96.90  ? 148 LYS B CA  1 
ATOM   4053 C  C   . LYS B 1 133 ? -24.831 9.149   29.815  1.00   89.25  ? 148 LYS B C   1 
ATOM   4054 O  O   . LYS B 1 133 ? -24.177 8.298   29.228  1.00   86.19  ? 148 LYS B O   1 
ATOM   4055 C  CB  . LYS B 1 133 ? -24.738 11.527  29.208  1.00   102.52 ? 148 LYS B CB  1 
ATOM   4056 C  CG  . LYS B 1 133 ? -25.010 12.567  28.126  1.00   114.87 ? 148 LYS B CG  1 
ATOM   4057 C  CD  . LYS B 1 133 ? -24.493 13.951  28.525  1.00   121.33 ? 148 LYS B CD  1 
ATOM   4058 C  CE  . LYS B 1 133 ? -25.226 15.063  27.775  1.00   124.29 ? 148 LYS B CE  1 
ATOM   4059 N  NZ  . LYS B 1 133 ? -25.115 14.918  26.301  1.00   125.93 ? 148 LYS B NZ  1 
ATOM   4060 N  N   . LEU B 1 134 ? -24.999 9.181   31.133  1.00   86.82  ? 149 LEU B N   1 
ATOM   4061 C  CA  . LEU B 1 134 ? -24.298 8.270   32.021  1.00   83.67  ? 149 LEU B CA  1 
ATOM   4062 C  C   . LEU B 1 134 ? -24.913 6.896   31.952  1.00   80.77  ? 149 LEU B C   1 
ATOM   4063 O  O   . LEU B 1 134 ? -24.205 5.892   31.857  1.00   79.55  ? 149 LEU B O   1 
ATOM   4064 C  CB  . LEU B 1 134 ? -24.361 8.764   33.457  1.00   85.08  ? 149 LEU B CB  1 
ATOM   4065 C  CG  . LEU B 1 134 ? -23.488 7.988   34.437  1.00   85.44  ? 149 LEU B CG  1 
ATOM   4066 C  CD1 . LEU B 1 134 ? -22.014 8.356   34.243  1.00   86.04  ? 149 LEU B CD1 1 
ATOM   4067 C  CD2 . LEU B 1 134 ? -23.933 8.267   35.862  1.00   85.31  ? 149 LEU B CD2 1 
ATOM   4068 N  N   . GLN B 1 135 ? -26.237 6.851   32.004  1.00   78.22  ? 150 GLN B N   1 
ATOM   4069 C  CA  . GLN B 1 135 ? -26.932 5.589   31.896  1.00   76.87  ? 150 GLN B CA  1 
ATOM   4070 C  C   . GLN B 1 135 ? -26.455 4.803   30.682  1.00   77.06  ? 150 GLN B C   1 
ATOM   4071 O  O   . GLN B 1 135 ? -26.129 3.627   30.792  1.00   78.38  ? 150 GLN B O   1 
ATOM   4072 C  CB  . GLN B 1 135 ? -28.429 5.815   31.800  1.00   78.39  ? 150 GLN B CB  1 
ATOM   4073 C  CG  . GLN B 1 135 ? -29.244 4.531   31.783  1.00   77.88  ? 150 GLN B CG  1 
ATOM   4074 C  CD  . GLN B 1 135 ? -30.676 4.776   32.195  1.00   79.13  ? 150 GLN B CD  1 
ATOM   4075 O  OE1 . GLN B 1 135 ? -30.999 4.691   33.376  1.00   77.65  ? 150 GLN B OE1 1 
ATOM   4076 N  NE2 . GLN B 1 135 ? -31.538 5.108   31.226  1.00   81.59  ? 150 GLN B NE2 1 
ATOM   4077 N  N   . THR B 1 136 ? -26.391 5.470   29.534  1.00   77.30  ? 151 THR B N   1 
ATOM   4078 C  CA  . THR B 1 136 ? -26.045 4.831   28.264  1.00   77.17  ? 151 THR B CA  1 
ATOM   4079 C  C   . THR B 1 136 ? -24.626 4.296   28.280  1.00   74.49  ? 151 THR B C   1 
ATOM   4080 O  O   . THR B 1 136 ? -24.371 3.102   28.064  1.00   72.21  ? 151 THR B O   1 
ATOM   4081 C  CB  . THR B 1 136 ? -26.152 5.845   27.111  1.00   79.59  ? 151 THR B CB  1 
ATOM   4082 O  OG1 . THR B 1 136 ? -27.496 6.325   27.016  1.00   81.08  ? 151 THR B OG1 1 
ATOM   4083 C  CG2 . THR B 1 136 ? -25.753 5.216   25.804  1.00   81.28  ? 151 THR B CG2 1 
ATOM   4084 N  N   . ILE B 1 137 ? -23.704 5.207   28.541  1.00   73.07  ? 152 ILE B N   1 
ATOM   4085 C  CA  . ILE B 1 137 ? -22.327 4.857   28.693  1.00   70.16  ? 152 ILE B CA  1 
ATOM   4086 C  C   . ILE B 1 137 ? -22.288 3.572   29.518  1.00   69.76  ? 152 ILE B C   1 
ATOM   4087 O  O   . ILE B 1 137 ? -21.729 2.563   29.065  1.00   69.57  ? 152 ILE B O   1 
ATOM   4088 C  CB  . ILE B 1 137 ? -21.556 6.007   29.378  1.00   69.25  ? 152 ILE B CB  1 
ATOM   4089 C  CG1 . ILE B 1 137 ? -21.352 7.166   28.398  1.00   70.15  ? 152 ILE B CG1 1 
ATOM   4090 C  CG2 . ILE B 1 137 ? -20.201 5.542   29.916  1.00   67.17  ? 152 ILE B CG2 1 
ATOM   4091 C  CD1 . ILE B 1 137 ? -21.037 8.482   29.080  1.00   69.66  ? 152 ILE B CD1 1 
ATOM   4092 N  N   . VAL B 1 138 ? -22.918 3.587   30.697  1.00   68.62  ? 153 VAL B N   1 
ATOM   4093 C  CA  . VAL B 1 138 ? -22.743 2.481   31.651  1.00   67.53  ? 153 VAL B CA  1 
ATOM   4094 C  C   . VAL B 1 138 ? -23.514 1.241   31.215  1.00   67.68  ? 153 VAL B C   1 
ATOM   4095 O  O   . VAL B 1 138 ? -23.139 0.109   31.537  1.00   64.47  ? 153 VAL B O   1 
ATOM   4096 C  CB  . VAL B 1 138 ? -23.110 2.880   33.105  1.00   67.26  ? 153 VAL B CB  1 
ATOM   4097 C  CG1 . VAL B 1 138 ? -22.896 1.705   34.061  1.00   65.93  ? 153 VAL B CG1 1 
ATOM   4098 C  CG2 . VAL B 1 138 ? -22.262 4.065   33.571  1.00   65.92  ? 153 VAL B CG2 1 
ATOM   4099 N  N   . GLN B 1 139 ? -24.584 1.457   30.463  1.00   71.30  ? 154 GLN B N   1 
ATOM   4100 C  CA  . GLN B 1 139 ? -25.384 0.350   29.954  1.00   73.11  ? 154 GLN B CA  1 
ATOM   4101 C  C   . GLN B 1 139 ? -24.624 -0.365  28.832  1.00   71.95  ? 154 GLN B C   1 
ATOM   4102 O  O   . GLN B 1 139 ? -24.520 -1.595  28.843  1.00   69.05  ? 154 GLN B O   1 
ATOM   4103 C  CB  . GLN B 1 139 ? -26.788 0.833   29.532  1.00   76.92  ? 154 GLN B CB  1 
ATOM   4104 C  CG  . GLN B 1 139 ? -27.734 1.056   30.713  1.00   78.35  ? 154 GLN B CG  1 
ATOM   4105 C  CD  . GLN B 1 139 ? -29.184 1.287   30.304  1.00   85.39  ? 154 GLN B CD  1 
ATOM   4106 O  OE1 . GLN B 1 139 ? -29.472 1.905   29.272  1.00   88.84  ? 154 GLN B OE1 1 
ATOM   4107 N  NE2 . GLN B 1 139 ? -30.116 0.800   31.126  1.00   88.87  ? 154 GLN B NE2 1 
ATOM   4108 N  N   . GLU B 1 140 ? -24.058 0.402   27.900  1.00   73.34  ? 155 GLU B N   1 
ATOM   4109 C  CA  . GLU B 1 140 ? -23.237 -0.176  26.818  1.00   75.16  ? 155 GLU B CA  1 
ATOM   4110 C  C   . GLU B 1 140 ? -21.927 -0.743  27.358  1.00   73.38  ? 155 GLU B C   1 
ATOM   4111 O  O   . GLU B 1 140 ? -21.440 -1.773  26.885  1.00   73.11  ? 155 GLU B O   1 
ATOM   4112 C  CB  . GLU B 1 140 ? -22.896 0.866   25.750  1.00   77.08  ? 155 GLU B CB  1 
ATOM   4113 C  CG  . GLU B 1 140 ? -24.068 1.399   24.949  1.00   79.46  ? 155 GLU B CG  1 
ATOM   4114 C  CD  . GLU B 1 140 ? -23.655 2.582   24.101  1.00   81.42  ? 155 GLU B CD  1 
ATOM   4115 O  OE1 . GLU B 1 140 ? -22.481 2.627   23.681  1.00   82.29  ? 155 GLU B OE1 1 
ATOM   4116 O  OE2 . GLU B 1 140 ? -24.492 3.468   23.853  1.00   83.84  ? 155 GLU B OE2 1 
ATOM   4117 N  N   . ALA B 1 141 ? -21.348 -0.059  28.337  1.00   71.32  ? 156 ALA B N   1 
ATOM   4118 C  CA  . ALA B 1 141 ? -20.181 -0.582  28.993  1.00   70.24  ? 156 ALA B CA  1 
ATOM   4119 C  C   . ALA B 1 141 ? -20.525 -1.901  29.678  1.00   69.54  ? 156 ALA B C   1 
ATOM   4120 O  O   . ALA B 1 141 ? -19.736 -2.843  29.643  1.00   71.22  ? 156 ALA B O   1 
ATOM   4121 C  CB  . ALA B 1 141 ? -19.634 0.419   29.984  1.00   69.90  ? 156 ALA B CB  1 
ATOM   4122 N  N   . ALA B 1 142 ? -21.706 -1.992  30.274  1.00   69.32  ? 157 ALA B N   1 
ATOM   4123 C  CA  . ALA B 1 142 ? -22.095 -3.233  30.924  1.00   70.70  ? 157 ALA B CA  1 
ATOM   4124 C  C   . ALA B 1 142 ? -22.248 -4.376  29.916  1.00   73.17  ? 157 ALA B C   1 
ATOM   4125 O  O   . ALA B 1 142 ? -21.947 -5.525  30.231  1.00   74.41  ? 157 ALA B O   1 
ATOM   4126 C  CB  . ALA B 1 142 ? -23.364 -3.042  31.733  1.00   71.67  ? 157 ALA B CB  1 
ATOM   4127 N  N   . ASP B 1 143 ? -22.684 -4.063  28.700  1.00   77.43  ? 158 ASP B N   1 
ATOM   4128 C  CA  . ASP B 1 143 ? -22.828 -5.086  27.646  1.00   77.97  ? 158 ASP B CA  1 
ATOM   4129 C  C   . ASP B 1 143 ? -21.509 -5.714  27.150  1.00   76.36  ? 158 ASP B C   1 
ATOM   4130 O  O   . ASP B 1 143 ? -21.438 -6.936  26.975  1.00   75.18  ? 158 ASP B O   1 
ATOM   4131 C  CB  . ASP B 1 143 ? -23.671 -4.554  26.489  1.00   80.26  ? 158 ASP B CB  1 
ATOM   4132 C  CG  . ASP B 1 143 ? -25.155 -4.849  26.682  1.00   86.13  ? 158 ASP B CG  1 
ATOM   4133 O  OD1 . ASP B 1 143 ? -25.476 -6.023  26.976  1.00   88.26  ? 158 ASP B OD1 1 
ATOM   4134 O  OD2 . ASP B 1 143 ? -26.003 -3.928  26.557  1.00   88.98  ? 158 ASP B OD2 1 
ATOM   4135 N  N   . SER B 1 144 ? -20.471 -4.900  26.944  1.00   74.40  ? 159 SER B N   1 
ATOM   4136 C  CA  . SER B 1 144 ? -19.159 -5.434  26.540  1.00   73.31  ? 159 SER B CA  1 
ATOM   4137 C  C   . SER B 1 144 ? -18.721 -6.438  27.614  1.00   74.24  ? 159 SER B C   1 
ATOM   4138 O  O   . SER B 1 144 ? -18.339 -7.576  27.307  1.00   72.38  ? 159 SER B O   1 
ATOM   4139 C  CB  . SER B 1 144 ? -18.095 -4.325  26.377  1.00   71.12  ? 159 SER B CB  1 
ATOM   4140 O  OG  . SER B 1 144 ? -18.654 -3.045  26.119  1.00   69.82  ? 159 SER B OG  1 
ATOM   4141 N  N   . LEU B 1 145 ? -18.809 -5.992  28.876  1.00   75.05  ? 160 LEU B N   1 
ATOM   4142 C  CA  . LEU B 1 145 ? -18.514 -6.817  30.050  1.00   72.98  ? 160 LEU B CA  1 
ATOM   4143 C  C   . LEU B 1 145 ? -19.330 -8.094  30.019  1.00   72.93  ? 160 LEU B C   1 
ATOM   4144 O  O   . LEU B 1 145 ? -18.796 -9.197  30.130  1.00   69.40  ? 160 LEU B O   1 
ATOM   4145 C  CB  . LEU B 1 145 ? -18.826 -6.037  31.335  1.00   73.42  ? 160 LEU B CB  1 
ATOM   4146 C  CG  . LEU B 1 145 ? -18.688 -6.728  32.702  1.00   72.00  ? 160 LEU B CG  1 
ATOM   4147 C  CD1 . LEU B 1 145 ? -17.316 -7.364  32.883  1.00   72.30  ? 160 LEU B CD1 1 
ATOM   4148 C  CD2 . LEU B 1 145 ? -18.931 -5.712  33.800  1.00   70.00  ? 160 LEU B CD2 1 
ATOM   4149 N  N   . CYS B 1 146 ? -20.636 -7.934  29.852  1.00   75.53  ? 161 CYS B N   1 
ATOM   4150 C  CA  . CYS B 1 146 ? -21.514 -9.086  29.774  1.00   77.21  ? 161 CYS B CA  1 
ATOM   4151 C  C   . CYS B 1 146 ? -21.077 -10.042 28.671  1.00   79.96  ? 161 CYS B C   1 
ATOM   4152 O  O   . CYS B 1 146 ? -21.061 -11.256 28.884  1.00   81.01  ? 161 CYS B O   1 
ATOM   4153 C  CB  . CYS B 1 146 ? -22.963 -8.661  29.598  1.00   77.80  ? 161 CYS B CB  1 
ATOM   4154 S  SG  . CYS B 1 146 ? -23.783 -8.439  31.183  1.00   76.48  ? 161 CYS B SG  1 
ATOM   4155 N  N   . GLU B 1 147 ? -20.689 -9.506  27.516  1.00   82.39  ? 162 GLU B N   1 
ATOM   4156 C  CA  . GLU B 1 147 ? -20.217 -10.354 26.422  1.00   85.72  ? 162 GLU B CA  1 
ATOM   4157 C  C   . GLU B 1 147 ? -18.996 -11.138 26.831  1.00   85.03  ? 162 GLU B C   1 
ATOM   4158 O  O   . GLU B 1 147 ? -18.984 -12.368 26.756  1.00   85.37  ? 162 GLU B O   1 
ATOM   4159 C  CB  . GLU B 1 147 ? -19.887 -9.538  25.178  1.00   88.23  ? 162 GLU B CB  1 
ATOM   4160 C  CG  . GLU B 1 147 ? -21.114 -9.140  24.385  1.00   92.46  ? 162 GLU B CG  1 
ATOM   4161 C  CD  . GLU B 1 147 ? -20.833 -9.088  22.908  1.00   94.46  ? 162 GLU B CD  1 
ATOM   4162 O  OE1 . GLU B 1 147 ? -19.758 -8.567  22.546  1.00   94.45  ? 162 GLU B OE1 1 
ATOM   4163 O  OE2 . GLU B 1 147 ? -21.683 -9.570  22.126  1.00   97.02  ? 162 GLU B OE2 1 
ATOM   4164 N  N   . GLU B 1 148 ? -17.978 -10.419 27.288  1.00   84.55  ? 163 GLU B N   1 
ATOM   4165 C  CA  . GLU B 1 148 ? -16.736 -11.054 27.706  1.00   86.39  ? 163 GLU B CA  1 
ATOM   4166 C  C   . GLU B 1 148 ? -17.002 -12.208 28.657  1.00   86.40  ? 163 GLU B C   1 
ATOM   4167 O  O   . GLU B 1 148 ? -16.236 -13.159 28.709  1.00   84.86  ? 163 GLU B O   1 
ATOM   4168 C  CB  . GLU B 1 148 ? -15.792 -10.048 28.374  1.00   87.52  ? 163 GLU B CB  1 
ATOM   4169 C  CG  . GLU B 1 148 ? -15.088 -9.116  27.398  1.00   92.51  ? 163 GLU B CG  1 
ATOM   4170 C  CD  . GLU B 1 148 ? -13.821 -8.490  27.963  1.00   98.02  ? 163 GLU B CD  1 
ATOM   4171 O  OE1 . GLU B 1 148 ? -13.070 -9.180  28.695  1.00   98.82  ? 163 GLU B OE1 1 
ATOM   4172 O  OE2 . GLU B 1 148 ? -13.560 -7.303  27.655  1.00   105.77 ? 163 GLU B OE2 1 
ATOM   4173 N  N   . LEU B 1 149 ? -18.092 -12.124 29.408  1.00   89.23  ? 164 LEU B N   1 
ATOM   4174 C  CA  . LEU B 1 149 ? -18.349 -13.085 30.470  1.00   91.11  ? 164 LEU B CA  1 
ATOM   4175 C  C   . LEU B 1 149 ? -18.961 -14.389 29.957  1.00   94.64  ? 164 LEU B C   1 
ATOM   4176 O  O   . LEU B 1 149 ? -18.458 -15.473 30.276  1.00   92.63  ? 164 LEU B O   1 
ATOM   4177 C  CB  . LEU B 1 149 ? -19.208 -12.433 31.562  1.00   89.30  ? 164 LEU B CB  1 
ATOM   4178 C  CG  . LEU B 1 149 ? -18.420 -11.378 32.343  1.00   85.23  ? 164 LEU B CG  1 
ATOM   4179 C  CD1 . LEU B 1 149 ? -19.319 -10.342 32.989  1.00   83.55  ? 164 LEU B CD1 1 
ATOM   4180 C  CD2 . LEU B 1 149 ? -17.545 -12.050 33.384  1.00   85.12  ? 164 LEU B CD2 1 
ATOM   4181 N  N   . GLN B 1 150 ? -20.028 -14.296 29.165  1.00   97.62  ? 165 GLN B N   1 
ATOM   4182 C  CA  . GLN B 1 150 ? -20.640 -15.504 28.594  1.00   103.19 ? 165 GLN B CA  1 
ATOM   4183 C  C   . GLN B 1 150 ? -19.700 -16.209 27.606  1.00   104.55 ? 165 GLN B C   1 
ATOM   4184 O  O   . GLN B 1 150 ? -19.870 -17.397 27.337  1.00   105.45 ? 165 GLN B O   1 
ATOM   4185 C  CB  . GLN B 1 150 ? -22.006 -15.210 27.946  1.00   106.36 ? 165 GLN B CB  1 
ATOM   4186 C  CG  . GLN B 1 150 ? -21.983 -14.332 26.700  1.00   107.08 ? 165 GLN B CG  1 
ATOM   4187 C  CD  . GLN B 1 150 ? -23.330 -13.677 26.411  1.00   107.75 ? 165 GLN B CD  1 
ATOM   4188 O  OE1 . GLN B 1 150 ? -24.250 -13.711 27.236  1.00   104.11 ? 165 GLN B OE1 1 
ATOM   4189 N  NE2 . GLN B 1 150 ? -23.444 -13.055 25.244  1.00   108.86 ? 165 GLN B NE2 1 
ATOM   4190 N  N   . ALA B 1 151 ? -18.706 -15.481 27.089  1.00   103.30 ? 166 ALA B N   1 
ATOM   4191 C  CA  . ALA B 1 151 ? -17.653 -16.073 26.253  1.00   105.78 ? 166 ALA B CA  1 
ATOM   4192 C  C   . ALA B 1 151 ? -16.721 -17.035 27.012  1.00   110.33 ? 166 ALA B C   1 
ATOM   4193 O  O   . ALA B 1 151 ? -16.083 -17.888 26.392  1.00   112.27 ? 166 ALA B O   1 
ATOM   4194 C  CB  . ALA B 1 151 ? -16.833 -14.978 25.579  1.00   101.75 ? 166 ALA B CB  1 
ATOM   4195 N  N   . CYS B 1 152 ? -16.629 -16.886 28.334  1.00   115.27 ? 167 CYS B N   1 
ATOM   4196 C  CA  . CYS B 1 152 ? -15.809 -17.767 29.168  1.00   117.64 ? 167 CYS B CA  1 
ATOM   4197 C  C   . CYS B 1 152 ? -16.659 -18.560 30.161  1.00   124.38 ? 167 CYS B C   1 
ATOM   4198 O  O   . CYS B 1 152 ? -16.224 -18.811 31.285  1.00   131.16 ? 167 CYS B O   1 
ATOM   4199 C  CB  . CYS B 1 152 ? -14.761 -16.944 29.921  1.00   116.10 ? 167 CYS B CB  1 
ATOM   4200 S  SG  . CYS B 1 152 ? -15.456 -15.501 30.761  1.00   120.82 ? 167 CYS B SG  1 
ATOM   4201 N  N   . ARG B 1 153 ? -17.871 -18.950 29.762  1.00   129.20 ? 168 ARG B N   1 
ATOM   4202 C  CA  . ARG B 1 153 ? -18.680 -19.845 30.596  1.00   127.59 ? 168 ARG B CA  1 
ATOM   4203 C  C   . ARG B 1 153 ? -18.003 -21.224 30.550  1.00   125.00 ? 168 ARG B C   1 
ATOM   4204 O  O   . ARG B 1 153 ? -17.351 -21.576 29.559  1.00   121.70 ? 168 ARG B O   1 
ATOM   4205 C  CB  . ARG B 1 153 ? -20.170 -19.852 30.167  1.00   130.79 ? 168 ARG B CB  1 
ATOM   4206 C  CG  . ARG B 1 153 ? -20.663 -21.001 29.280  1.00   135.05 ? 168 ARG B CG  1 
ATOM   4207 C  CD  . ARG B 1 153 ? -21.402 -22.084 30.072  1.00   135.88 ? 168 ARG B CD  1 
ATOM   4208 N  NE  . ARG B 1 153 ? -22.030 -23.095 29.205  1.00   134.42 ? 168 ARG B NE  1 
ATOM   4209 C  CZ  . ARG B 1 153 ? -21.569 -24.329 28.977  1.00   132.26 ? 168 ARG B CZ  1 
ATOM   4210 N  NH1 . ARG B 1 153 ? -20.449 -24.772 29.545  1.00   129.16 ? 168 ARG B NH1 1 
ATOM   4211 N  NH2 . ARG B 1 153 ? -22.243 -25.139 28.166  1.00   133.10 ? 168 ARG B NH2 1 
ATOM   4212 N  N   . GLY B 1 154 ? -18.109 -21.970 31.646  1.00   122.16 ? 169 GLY B N   1 
ATOM   4213 C  CA  . GLY B 1 154 ? -17.346 -23.207 31.821  1.00   119.71 ? 169 GLY B CA  1 
ATOM   4214 C  C   . GLY B 1 154 ? -15.902 -22.968 32.241  1.00   112.99 ? 169 GLY B C   1 
ATOM   4215 O  O   . GLY B 1 154 ? -15.112 -23.908 32.291  1.00   112.12 ? 169 GLY B O   1 
ATOM   4216 N  N   . GLN B 1 155 ? -15.564 -21.715 32.553  1.00   107.13 ? 170 GLN B N   1 
ATOM   4217 C  CA  . GLN B 1 155 ? -14.197 -21.326 32.899  1.00   103.85 ? 170 GLN B CA  1 
ATOM   4218 C  C   . GLN B 1 155 ? -14.161 -20.705 34.291  1.00   98.30  ? 170 GLN B C   1 
ATOM   4219 O  O   . GLN B 1 155 ? -14.940 -19.802 34.604  1.00   94.99  ? 170 GLN B O   1 
ATOM   4220 C  CB  . GLN B 1 155 ? -13.630 -20.291 31.912  1.00   104.78 ? 170 GLN B CB  1 
ATOM   4221 C  CG  . GLN B 1 155 ? -13.747 -20.622 30.429  1.00   106.60 ? 170 GLN B CG  1 
ATOM   4222 C  CD  . GLN B 1 155 ? -12.436 -21.098 29.828  1.00   106.58 ? 170 GLN B CD  1 
ATOM   4223 O  OE1 . GLN B 1 155 ? -11.905 -22.128 30.234  1.00   105.79 ? 170 GLN B OE1 1 
ATOM   4224 N  NE2 . GLN B 1 155 ? -11.910 -20.352 28.852  1.00   106.00 ? 170 GLN B NE2 1 
ATOM   4225 N  N   . SER B 1 156 ? -13.231 -21.181 35.109  1.00   95.22  ? 171 SER B N   1 
ATOM   4226 C  CA  . SER B 1 156 ? -12.944 -20.582 36.397  1.00   91.98  ? 171 SER B CA  1 
ATOM   4227 C  C   . SER B 1 156 ? -12.232 -19.238 36.189  1.00   88.98  ? 171 SER B C   1 
ATOM   4228 O  O   . SER B 1 156 ? -11.006 -19.152 36.279  1.00   93.59  ? 171 SER B O   1 
ATOM   4229 C  CB  . SER B 1 156 ? -12.077 -21.531 37.236  1.00   91.68  ? 171 SER B CB  1 
ATOM   4230 O  OG  . SER B 1 156 ? -12.631 -22.835 37.266  1.00   92.38  ? 171 SER B OG  1 
ATOM   4231 N  N   . SER B 1 157 ? -13.007 -18.192 35.914  1.00   84.17  ? 172 SER B N   1 
ATOM   4232 C  CA  . SER B 1 157 ? -12.443 -16.878 35.631  1.00   78.03  ? 172 SER B CA  1 
ATOM   4233 C  C   . SER B 1 157 ? -12.098 -16.061 36.888  1.00   77.25  ? 172 SER B C   1 
ATOM   4234 O  O   . SER B 1 157 ? -12.601 -16.294 37.984  1.00   77.26  ? 172 SER B O   1 
ATOM   4235 C  CB  . SER B 1 157 ? -13.390 -16.075 34.749  1.00   75.95  ? 172 SER B CB  1 
ATOM   4236 O  OG  . SER B 1 157 ? -12.903 -14.762 34.570  1.00   71.53  ? 172 SER B OG  1 
ATOM   4237 N  N   . ASP B 1 158 ? -11.227 -15.085 36.688  1.00   74.47  ? 173 ASP B N   1 
ATOM   4238 C  CA  . ASP B 1 158 ? -10.842 -14.125 37.703  1.00   68.28  ? 173 ASP B CA  1 
ATOM   4239 C  C   . ASP B 1 158 ? -11.390 -12.774 37.242  1.00   64.77  ? 173 ASP B C   1 
ATOM   4240 O  O   . ASP B 1 158 ? -10.850 -12.144 36.328  1.00   60.66  ? 173 ASP B O   1 
ATOM   4241 C  CB  . ASP B 1 158 ? -9.309  -14.104 37.792  1.00   68.00  ? 173 ASP B CB  1 
ATOM   4242 C  CG  . ASP B 1 158 ? -8.783  -13.281 38.956  1.00   65.88  ? 173 ASP B CG  1 
ATOM   4243 O  OD1 . ASP B 1 158 ? -9.176  -12.118 39.135  1.00   64.84  ? 173 ASP B OD1 1 
ATOM   4244 O  OD2 . ASP B 1 158 ? -7.932  -13.798 39.688  1.00   66.74  ? 173 ASP B OD2 1 
ATOM   4245 N  N   . LEU B 1 159 ? -12.490 -12.338 37.841  1.00   64.29  ? 174 LEU B N   1 
ATOM   4246 C  CA  . LEU B 1 159 ? -13.062 -11.040 37.475  1.00   63.54  ? 174 LEU B CA  1 
ATOM   4247 C  C   . LEU B 1 159 ? -12.053 -9.976  37.839  1.00   63.25  ? 174 LEU B C   1 
ATOM   4248 O  O   . LEU B 1 159 ? -10.975 -10.309 38.321  1.00   68.40  ? 174 LEU B O   1 
ATOM   4249 C  CB  . LEU B 1 159 ? -14.358 -10.817 38.224  1.00   64.46  ? 174 LEU B CB  1 
ATOM   4250 C  CG  . LEU B 1 159 ? -15.505 -11.704 37.771  1.00   64.96  ? 174 LEU B CG  1 
ATOM   4251 C  CD1 . LEU B 1 159 ? -16.580 -11.720 38.838  1.00   66.62  ? 174 LEU B CD1 1 
ATOM   4252 C  CD2 . LEU B 1 159 ? -16.065 -11.200 36.458  1.00   65.86  ? 174 LEU B CD2 1 
ATOM   4253 N  N   . SER B 1 160 ? -12.365 -8.702  37.627  1.00   60.70  ? 175 SER B N   1 
ATOM   4254 C  CA  . SER B 1 160 ? -11.431 -7.615  38.018  1.00   59.10  ? 175 SER B CA  1 
ATOM   4255 C  C   . SER B 1 160 ? -10.564 -7.226  36.863  1.00   57.74  ? 175 SER B C   1 
ATOM   4256 O  O   . SER B 1 160 ? -10.426 -6.038  36.563  1.00   57.59  ? 175 SER B O   1 
ATOM   4257 C  CB  . SER B 1 160 ? -10.490 -7.993  39.184  1.00   58.72  ? 175 SER B CB  1 
ATOM   4258 O  OG  . SER B 1 160 ? -9.381  -8.761  38.736  1.00   57.40  ? 175 SER B OG  1 
ATOM   4259 N  N   . VAL B 1 161 ? -9.971  -8.225  36.220  1.00   56.09  ? 176 VAL B N   1 
ATOM   4260 C  CA  . VAL B 1 161 ? -9.304  -7.958  34.984  1.00   58.83  ? 176 VAL B CA  1 
ATOM   4261 C  C   . VAL B 1 161 ? -10.367 -7.390  34.070  1.00   58.97  ? 176 VAL B C   1 
ATOM   4262 O  O   . VAL B 1 161 ? -10.186 -6.312  33.506  1.00   63.87  ? 176 VAL B O   1 
ATOM   4263 C  CB  . VAL B 1 161 ? -8.625  -9.191  34.336  1.00   61.48  ? 176 VAL B CB  1 
ATOM   4264 C  CG1 . VAL B 1 161 ? -7.554  -8.715  33.371  1.00   60.37  ? 176 VAL B CG1 1 
ATOM   4265 C  CG2 . VAL B 1 161 ? -7.994  -10.112 35.381  1.00   61.70  ? 176 VAL B CG2 1 
ATOM   4266 N  N   . VAL B 1 162 ? -11.483 -8.099  33.959  1.00   57.42  ? 177 VAL B N   1 
ATOM   4267 C  CA  . VAL B 1 162 ? -12.621 -7.635  33.159  1.00   57.25  ? 177 VAL B CA  1 
ATOM   4268 C  C   . VAL B 1 162 ? -13.318 -6.387  33.719  1.00   56.30  ? 177 VAL B C   1 
ATOM   4269 O  O   . VAL B 1 162 ? -13.748 -5.530  32.955  1.00   56.41  ? 177 VAL B O   1 
ATOM   4270 C  CB  . VAL B 1 162 ? -13.682 -8.751  32.947  1.00   58.85  ? 177 VAL B CB  1 
ATOM   4271 C  CG1 . VAL B 1 162 ? -13.089 -9.954  32.229  1.00   58.78  ? 177 VAL B CG1 1 
ATOM   4272 C  CG2 . VAL B 1 162 ? -14.308 -9.196  34.264  1.00   59.53  ? 177 VAL B CG2 1 
ATOM   4273 N  N   . LEU B 1 163 ? -13.456 -6.284  35.043  1.00   56.64  ? 178 LEU B N   1 
ATOM   4274 C  CA  . LEU B 1 163 ? -14.211 -5.157  35.638  1.00   56.21  ? 178 LEU B CA  1 
ATOM   4275 C  C   . LEU B 1 163 ? -13.421 -3.859  35.660  1.00   57.25  ? 178 LEU B C   1 
ATOM   4276 O  O   . LEU B 1 163 ? -14.023 -2.775  35.627  1.00   57.22  ? 178 LEU B O   1 
ATOM   4277 C  CB  . LEU B 1 163 ? -14.689 -5.461  37.055  1.00   54.26  ? 178 LEU B CB  1 
ATOM   4278 C  CG  . LEU B 1 163 ? -15.656 -6.623  37.233  1.00   54.03  ? 178 LEU B CG  1 
ATOM   4279 C  CD1 . LEU B 1 163 ? -15.911 -6.842  38.707  1.00   52.89  ? 178 LEU B CD1 1 
ATOM   4280 C  CD2 . LEU B 1 163 ? -16.946 -6.360  36.501  1.00   54.99  ? 178 LEU B CD2 1 
ATOM   4281 N  N   . MET B 1 164 ? -12.092 -3.959  35.733  1.00   56.43  ? 179 MET B N   1 
ATOM   4282 C  CA  . MET B 1 164 ? -11.267 -2.781  35.606  1.00   57.77  ? 179 MET B CA  1 
ATOM   4283 C  C   . MET B 1 164 ? -11.554 -2.138  34.269  1.00   57.14  ? 179 MET B C   1 
ATOM   4284 O  O   . MET B 1 164 ? -11.967 -0.976  34.200  1.00   54.57  ? 179 MET B O   1 
ATOM   4285 C  CB  . MET B 1 164 ? -9.794  -3.136  35.700  1.00   62.84  ? 179 MET B CB  1 
ATOM   4286 C  CG  . MET B 1 164 ? -9.278  -3.160  37.120  1.00   67.39  ? 179 MET B CG  1 
ATOM   4287 S  SD  . MET B 1 164 ? -9.241  -1.515  37.876  1.00   76.33  ? 179 MET B SD  1 
ATOM   4288 C  CE  . MET B 1 164 ? -8.055  -0.679  36.804  1.00   79.42  ? 179 MET B CE  1 
ATOM   4289 N  N   . ARG B 1 165 ? -11.350 -2.917  33.209  1.00   58.06  ? 180 ARG B N   1 
ATOM   4290 C  CA  . ARG B 1 165 ? -11.602 -2.468  31.846  1.00   59.59  ? 180 ARG B CA  1 
ATOM   4291 C  C   . ARG B 1 165 ? -12.953 -1.762  31.735  1.00   56.76  ? 180 ARG B C   1 
ATOM   4292 O  O   . ARG B 1 165 ? -13.033 -0.639  31.229  1.00   53.66  ? 180 ARG B O   1 
ATOM   4293 C  CB  . ARG B 1 165 ? -11.548 -3.657  30.884  1.00   65.05  ? 180 ARG B CB  1 
ATOM   4294 C  CG  . ARG B 1 165 ? -11.826 -3.271  29.431  1.00   71.73  ? 180 ARG B CG  1 
ATOM   4295 C  CD  . ARG B 1 165 ? -11.361 -4.313  28.421  1.00   76.47  ? 180 ARG B CD  1 
ATOM   4296 N  NE  . ARG B 1 165 ? -10.064 -4.867  28.802  1.00   80.43  ? 180 ARG B NE  1 
ATOM   4297 C  CZ  . ARG B 1 165 ? -9.830  -6.145  29.093  1.00   83.39  ? 180 ARG B CZ  1 
ATOM   4298 N  NH1 . ARG B 1 165 ? -10.797 -7.063  29.007  1.00   83.01  ? 180 ARG B NH1 1 
ATOM   4299 N  NH2 . ARG B 1 165 ? -8.602  -6.512  29.449  1.00   84.19  ? 180 ARG B NH2 1 
ATOM   4300 N  N   . ALA B 1 166 ? -13.996 -2.431  32.239  1.00   55.50  ? 181 ALA B N   1 
ATOM   4301 C  CA  . ALA B 1 166 ? -15.366 -1.889  32.268  1.00   54.37  ? 181 ALA B CA  1 
ATOM   4302 C  C   . ALA B 1 166 ? -15.435 -0.529  32.940  1.00   53.29  ? 181 ALA B C   1 
ATOM   4303 O  O   . ALA B 1 166 ? -15.869 0.434   32.309  1.00   51.32  ? 181 ALA B O   1 
ATOM   4304 C  CB  . ALA B 1 166 ? -16.310 -2.858  32.946  1.00   53.62  ? 181 ALA B CB  1 
ATOM   4305 N  N   . VAL B 1 167 ? -14.972 -0.421  34.196  1.00   53.63  ? 182 VAL B N   1 
ATOM   4306 C  CA  . VAL B 1 167 ? -15.041 0.905   34.858  1.00   54.26  ? 182 VAL B CA  1 
ATOM   4307 C  C   . VAL B 1 167 ? -14.096 1.882   34.125  1.00   54.25  ? 182 VAL B C   1 
ATOM   4308 O  O   . VAL B 1 167 ? -14.514 2.984   33.741  1.00   53.71  ? 182 VAL B O   1 
ATOM   4309 C  CB  . VAL B 1 167 ? -14.931 0.940   36.434  1.00   52.84  ? 182 VAL B CB  1 
ATOM   4310 C  CG1 . VAL B 1 167 ? -15.538 -0.288  37.098  1.00   52.55  ? 182 VAL B CG1 1 
ATOM   4311 C  CG2 . VAL B 1 167 ? -13.515 1.122   36.903  1.00   53.89  ? 182 VAL B CG2 1 
ATOM   4312 N  N   . THR B 1 168 ? -12.865 1.462   33.848  1.00   54.18  ? 183 THR B N   1 
ATOM   4313 C  CA  . THR B 1 168 ? -11.937 2.334   33.120  1.00   54.76  ? 183 THR B CA  1 
ATOM   4314 C  C   . THR B 1 168 ? -12.509 2.968   31.848  1.00   57.49  ? 183 THR B C   1 
ATOM   4315 O  O   . THR B 1 168 ? -12.316 4.170   31.636  1.00   58.03  ? 183 THR B O   1 
ATOM   4316 C  CB  . THR B 1 168 ? -10.675 1.600   32.748  1.00   54.44  ? 183 THR B CB  1 
ATOM   4317 O  OG1 . THR B 1 168 ? -10.351 0.700   33.803  1.00   55.85  ? 183 THR B OG1 1 
ATOM   4318 C  CG2 . THR B 1 168 ? -9.554  2.588   32.572  1.00   54.68  ? 183 THR B CG2 1 
ATOM   4319 N  N   . ASN B 1 169 ? -13.200 2.168   31.017  1.00   59.65  ? 184 ASN B N   1 
ATOM   4320 C  CA  . ASN B 1 169 ? -13.894 2.676   29.812  1.00   60.58  ? 184 ASN B CA  1 
ATOM   4321 C  C   . ASN B 1 169 ? -14.886 3.741   30.217  1.00   58.64  ? 184 ASN B C   1 
ATOM   4322 O  O   . ASN B 1 169 ? -14.802 4.885   29.793  1.00   57.26  ? 184 ASN B O   1 
ATOM   4323 C  CB  . ASN B 1 169 ? -14.647 1.556   29.066  1.00   63.87  ? 184 ASN B CB  1 
ATOM   4324 C  CG  . ASN B 1 169 ? -14.505 1.623   27.528  1.00   69.39  ? 184 ASN B CG  1 
ATOM   4325 O  OD1 . ASN B 1 169 ? -13.832 2.494   26.934  1.00   70.07  ? 184 ASN B OD1 1 
ATOM   4326 N  ND2 . ASN B 1 169 ? -15.136 0.658   26.875  1.00   72.39  ? 184 ASN B ND2 1 
ATOM   4327 N  N   . VAL B 1 170 ? -15.817 3.362   31.077  1.00   58.36  ? 185 VAL B N   1 
ATOM   4328 C  CA  . VAL B 1 170 ? -16.880 4.275   31.479  1.00   59.33  ? 185 VAL B CA  1 
ATOM   4329 C  C   . VAL B 1 170 ? -16.297 5.645   31.805  1.00   59.55  ? 185 VAL B C   1 
ATOM   4330 O  O   . VAL B 1 170 ? -16.785 6.655   31.331  1.00   62.43  ? 185 VAL B O   1 
ATOM   4331 C  CB  . VAL B 1 170 ? -17.680 3.728   32.679  1.00   59.30  ? 185 VAL B CB  1 
ATOM   4332 C  CG1 . VAL B 1 170 ? -18.574 4.798   33.282  1.00   59.56  ? 185 VAL B CG1 1 
ATOM   4333 C  CG2 . VAL B 1 170 ? -18.510 2.528   32.257  1.00   60.73  ? 185 VAL B CG2 1 
ATOM   4334 N  N   . ILE B 1 171 ? -15.230 5.673   32.586  1.00   59.41  ? 186 ILE B N   1 
ATOM   4335 C  CA  . ILE B 1 171 ? -14.592 6.930   32.966  1.00   60.88  ? 186 ILE B CA  1 
ATOM   4336 C  C   . ILE B 1 171 ? -13.941 7.607   31.754  1.00   61.99  ? 186 ILE B C   1 
ATOM   4337 O  O   . ILE B 1 171 ? -14.113 8.806   31.551  1.00   60.89  ? 186 ILE B O   1 
ATOM   4338 C  CB  . ILE B 1 171 ? -13.532 6.698   34.068  1.00   60.66  ? 186 ILE B CB  1 
ATOM   4339 C  CG1 . ILE B 1 171 ? -14.172 6.033   35.285  1.00   60.71  ? 186 ILE B CG1 1 
ATOM   4340 C  CG2 . ILE B 1 171 ? -12.871 8.009   34.485  1.00   61.32  ? 186 ILE B CG2 1 
ATOM   4341 C  CD1 . ILE B 1 171 ? -15.475 6.677   35.703  1.00   61.48  ? 186 ILE B CD1 1 
ATOM   4342 N  N   . CYS B 1 172 ? -13.185 6.838   30.973  1.00   61.62  ? 187 CYS B N   1 
ATOM   4343 C  CA  . CYS B 1 172 ? -12.634 7.336   29.726  1.00   64.83  ? 187 CYS B CA  1 
ATOM   4344 C  C   . CYS B 1 172 ? -13.696 8.010   28.868  1.00   67.65  ? 187 CYS B C   1 
ATOM   4345 O  O   . CYS B 1 172 ? -13.454 9.073   28.265  1.00   66.32  ? 187 CYS B O   1 
ATOM   4346 C  CB  . CYS B 1 172 ? -12.052 6.193   28.903  1.00   65.72  ? 187 CYS B CB  1 
ATOM   4347 S  SG  . CYS B 1 172 ? -10.498 5.565   29.493  1.00   63.29  ? 187 CYS B SG  1 
ATOM   4348 N  N   . ARG B 1 173 ? -14.857 7.361   28.794  1.00   69.11  ? 188 ARG B N   1 
ATOM   4349 C  CA  . ARG B 1 173 ? -15.941 7.857   27.987  1.00   72.74  ? 188 ARG B CA  1 
ATOM   4350 C  C   . ARG B 1 173 ? -16.482 9.087   28.676  1.00   69.89  ? 188 ARG B C   1 
ATOM   4351 O  O   . ARG B 1 173 ? -16.532 10.167  28.102  1.00   69.71  ? 188 ARG B O   1 
ATOM   4352 C  CB  . ARG B 1 173 ? -17.008 6.782   27.798  1.00   80.02  ? 188 ARG B CB  1 
ATOM   4353 C  CG  . ARG B 1 173 ? -16.490 5.600   27.007  1.00   86.75  ? 188 ARG B CG  1 
ATOM   4354 C  CD  . ARG B 1 173 ? -17.547 4.582   26.626  1.00   95.49  ? 188 ARG B CD  1 
ATOM   4355 N  NE  . ARG B 1 173 ? -16.984 3.706   25.595  1.00   111.19 ? 188 ARG B NE  1 
ATOM   4356 C  CZ  . ARG B 1 173 ? -17.600 2.656   25.052  1.00   123.50 ? 188 ARG B CZ  1 
ATOM   4357 N  NH1 . ARG B 1 173 ? -18.828 2.308   25.441  1.00   130.09 ? 188 ARG B NH1 1 
ATOM   4358 N  NH2 . ARG B 1 173 ? -16.975 1.943   24.115  1.00   123.75 ? 188 ARG B NH2 1 
ATOM   4359 N  N   . LEU B 1 174 ? -16.812 8.940   29.948  1.00   66.45  ? 189 LEU B N   1 
ATOM   4360 C  CA  . LEU B 1 174 ? -17.395 10.035  30.694  1.00   65.09  ? 189 LEU B CA  1 
ATOM   4361 C  C   . LEU B 1 174 ? -16.494 11.262  30.696  1.00   64.55  ? 189 LEU B C   1 
ATOM   4362 O  O   . LEU B 1 174 ? -16.951 12.384  30.812  1.00   64.32  ? 189 LEU B O   1 
ATOM   4363 C  CB  . LEU B 1 174 ? -17.691 9.568   32.100  1.00   63.35  ? 189 LEU B CB  1 
ATOM   4364 C  CG  . LEU B 1 174 ? -18.483 10.482  33.019  1.00   64.40  ? 189 LEU B CG  1 
ATOM   4365 C  CD1 . LEU B 1 174 ? -19.867 10.770  32.455  1.00   66.89  ? 189 LEU B CD1 1 
ATOM   4366 C  CD2 . LEU B 1 174 ? -18.572 9.806   34.379  1.00   63.10  ? 189 LEU B CD2 1 
ATOM   4367 N  N   . VAL B 1 175 ? -15.210 11.045  30.511  1.00   65.15  ? 190 VAL B N   1 
ATOM   4368 C  CA  . VAL B 1 175 ? -14.247 12.103  30.659  1.00   67.71  ? 190 VAL B CA  1 
ATOM   4369 C  C   . VAL B 1 175 ? -13.784 12.656  29.308  1.00   70.65  ? 190 VAL B C   1 
ATOM   4370 O  O   . VAL B 1 175 ? -13.830 13.873  29.147  1.00   71.05  ? 190 VAL B O   1 
ATOM   4371 C  CB  . VAL B 1 175 ? -13.064 11.613  31.543  1.00   66.92  ? 190 VAL B CB  1 
ATOM   4372 C  CG1 . VAL B 1 175 ? -11.979 12.675  31.675  1.00   67.78  ? 190 VAL B CG1 1 
ATOM   4373 C  CG2 . VAL B 1 175 ? -13.579 11.229  32.927  1.00   64.97  ? 190 VAL B CG2 1 
ATOM   4374 N  N   . PHE B 1 176 ? -13.338 11.786  28.372  1.00   72.41  ? 191 PHE B N   1 
ATOM   4375 C  CA  . PHE B 1 176 ? -12.888 12.208  27.017  1.00   75.40  ? 191 PHE B CA  1 
ATOM   4376 C  C   . PHE B 1 176 ? -13.913 11.966  25.925  1.00   77.95  ? 191 PHE B C   1 
ATOM   4377 O  O   . PHE B 1 176 ? -13.785 12.500  24.837  1.00   81.59  ? 191 PHE B O   1 
ATOM   4378 C  CB  . PHE B 1 176 ? -11.672 11.431  26.461  1.00   76.37  ? 191 PHE B CB  1 
ATOM   4379 C  CG  . PHE B 1 176 ? -10.796 10.775  27.472  1.00   75.04  ? 191 PHE B CG  1 
ATOM   4380 C  CD1 . PHE B 1 176 ? -10.422 11.429  28.623  1.00   74.97  ? 191 PHE B CD1 1 
ATOM   4381 C  CD2 . PHE B 1 176 ? -10.274 9.507   27.213  1.00   74.55  ? 191 PHE B CD2 1 
ATOM   4382 C  CE1 . PHE B 1 176 ? -9.583  10.812  29.538  1.00   75.09  ? 191 PHE B CE1 1 
ATOM   4383 C  CE2 . PHE B 1 176 ? -9.439  8.886   28.118  1.00   72.88  ? 191 PHE B CE2 1 
ATOM   4384 C  CZ  . PHE B 1 176 ? -9.084  9.541   29.281  1.00   72.60  ? 191 PHE B CZ  1 
ATOM   4385 N  N   . SER B 1 177 ? -14.878 11.101  26.183  1.00   78.74  ? 192 SER B N   1 
ATOM   4386 C  CA  . SER B 1 177 ? -15.635 10.453  25.127  1.00   80.21  ? 192 SER B CA  1 
ATOM   4387 C  C   . SER B 1 177 ? -14.670 9.618   24.256  1.00   79.72  ? 192 SER B C   1 
ATOM   4388 O  O   . SER B 1 177 ? -14.565 9.791   23.032  1.00   82.93  ? 192 SER B O   1 
ATOM   4389 C  CB  . SER B 1 177 ? -16.458 11.463  24.330  1.00   83.73  ? 192 SER B CB  1 
ATOM   4390 O  OG  . SER B 1 177 ? -17.330 10.794  23.444  1.00   92.31  ? 192 SER B OG  1 
ATOM   4391 N  N   . SER B 1 178 ? -13.961 8.712   24.927  1.00   77.08  ? 193 SER B N   1 
ATOM   4392 C  CA  . SER B 1 178 ? -13.204 7.645   24.270  1.00   76.89  ? 193 SER B CA  1 
ATOM   4393 C  C   . SER B 1 178 ? -14.134 6.787   23.444  1.00   78.50  ? 193 SER B C   1 
ATOM   4394 O  O   . SER B 1 178 ? -15.349 6.819   23.590  1.00   78.68  ? 193 SER B O   1 
ATOM   4395 C  CB  . SER B 1 178 ? -12.509 6.727   25.285  1.00   73.77  ? 193 SER B CB  1 
ATOM   4396 O  OG  . SER B 1 178 ? -13.346 5.626   25.638  1.00   70.79  ? 193 SER B OG  1 
ATOM   4397 N  N   . SER B 1 179 ? -13.536 6.001   22.578  1.00   81.14  ? 194 SER B N   1 
ATOM   4398 C  CA  . SER B 1 179 ? -14.285 5.146   21.705  1.00   83.25  ? 194 SER B CA  1 
ATOM   4399 C  C   . SER B 1 179 ? -13.707 3.742   21.819  1.00   83.91  ? 194 SER B C   1 
ATOM   4400 O  O   . SER B 1 179 ? -13.975 2.886   20.980  1.00   85.56  ? 194 SER B O   1 
ATOM   4401 C  CB  . SER B 1 179 ? -14.162 5.695   20.280  1.00   84.98  ? 194 SER B CB  1 
ATOM   4402 O  OG  . SER B 1 179 ? -15.417 5.744   19.641  1.00   86.10  ? 194 SER B OG  1 
ATOM   4403 N  N   . TYR B 1 180 ? -12.937 3.488   22.877  1.00   84.36  ? 195 TYR B N   1 
ATOM   4404 C  CA  . TYR B 1 180 ? -12.036 2.334   22.874  1.00   85.40  ? 195 TYR B CA  1 
ATOM   4405 C  C   . TYR B 1 180 ? -12.794 1.020   22.809  1.00   89.61  ? 195 TYR B C   1 
ATOM   4406 O  O   . TYR B 1 180 ? -13.909 0.912   23.328  1.00   90.70  ? 195 TYR B O   1 
ATOM   4407 C  CB  . TYR B 1 180 ? -11.140 2.294   24.112  1.00   80.90  ? 195 TYR B CB  1 
ATOM   4408 C  CG  . TYR B 1 180 ? -10.271 3.498   24.346  1.00   79.24  ? 195 TYR B CG  1 
ATOM   4409 C  CD1 . TYR B 1 180 ? -9.597  4.116   23.299  1.00   79.28  ? 195 TYR B CD1 1 
ATOM   4410 C  CD2 . TYR B 1 180 ? -10.081 3.990   25.641  1.00   77.49  ? 195 TYR B CD2 1 
ATOM   4411 C  CE1 . TYR B 1 180 ? -8.788  5.213   23.523  1.00   79.52  ? 195 TYR B CE1 1 
ATOM   4412 C  CE2 . TYR B 1 180 ? -9.275  5.082   25.879  1.00   77.21  ? 195 TYR B CE2 1 
ATOM   4413 C  CZ  . TYR B 1 180 ? -8.624  5.689   24.819  1.00   79.67  ? 195 TYR B CZ  1 
ATOM   4414 O  OH  . TYR B 1 180 ? -7.813  6.776   25.057  1.00   80.18  ? 195 TYR B OH  1 
ATOM   4415 N  N   . GLN B 1 181 ? -12.174 0.032   22.165  1.00   93.18  ? 196 GLN B N   1 
ATOM   4416 C  CA  . GLN B 1 181 ? -12.593 -1.354  22.288  1.00   95.81  ? 196 GLN B CA  1 
ATOM   4417 C  C   . GLN B 1 181 ? -11.421 -2.103  22.889  1.00   95.42  ? 196 GLN B C   1 
ATOM   4418 O  O   . GLN B 1 181 ? -10.285 -1.678  22.715  1.00   98.51  ? 196 GLN B O   1 
ATOM   4419 C  CB  . GLN B 1 181 ? -12.981 -1.926  20.930  1.00   99.85  ? 196 GLN B CB  1 
ATOM   4420 C  CG  . GLN B 1 181 ? -14.265 -2.742  20.983  1.00   100.85 ? 196 GLN B CG  1 
ATOM   4421 C  CD  . GLN B 1 181 ? -15.226 -2.373  19.887  1.00   102.88 ? 196 GLN B CD  1 
ATOM   4422 O  OE1 . GLN B 1 181 ? -15.412 -1.199  19.580  1.00   102.50 ? 196 GLN B OE1 1 
ATOM   4423 N  NE2 . GLN B 1 181 ? -15.851 -3.375  19.291  1.00   106.69 ? 196 GLN B NE2 1 
ATOM   4424 N  N   . PRO B 1 182 ? -11.682 -3.216  23.600  1.00   95.02  ? 197 PRO B N   1 
ATOM   4425 C  CA  . PRO B 1 182 ? -10.614 -3.857  24.359  1.00   92.17  ? 197 PRO B CA  1 
ATOM   4426 C  C   . PRO B 1 182 ? -9.265  -3.896  23.639  1.00   93.91  ? 197 PRO B C   1 
ATOM   4427 O  O   . PRO B 1 182 ? -8.234  -3.678  24.267  1.00   103.21 ? 197 PRO B O   1 
ATOM   4428 C  CB  . PRO B 1 182 ? -11.155 -5.267  24.582  1.00   92.59  ? 197 PRO B CB  1 
ATOM   4429 C  CG  . PRO B 1 182 ? -12.630 -5.068  24.676  1.00   93.36  ? 197 PRO B CG  1 
ATOM   4430 C  CD  . PRO B 1 182 ? -12.928 -4.008  23.652  1.00   95.58  ? 197 PRO B CD  1 
ATOM   4431 N  N   . SER B 1 183 ? -9.258  -4.137  22.334  1.00   93.33  ? 198 SER B N   1 
ATOM   4432 C  CA  . SER B 1 183 ? -7.995  -4.199  21.588  1.00   89.85  ? 198 SER B CA  1 
ATOM   4433 C  C   . SER B 1 183 ? -7.139  -2.927  21.671  1.00   85.10  ? 198 SER B C   1 
ATOM   4434 O  O   . SER B 1 183 ? -5.918  -3.018  21.657  1.00   85.91  ? 198 SER B O   1 
ATOM   4435 C  CB  . SER B 1 183 ? -8.262  -4.542  20.119  1.00   90.98  ? 198 SER B CB  1 
ATOM   4436 O  OG  . SER B 1 183 ? -9.176  -3.626  19.547  1.00   92.62  ? 198 SER B OG  1 
ATOM   4437 N  N   . ASP B 1 184 ? -7.771  -1.755  21.747  1.00   80.65  ? 199 ASP B N   1 
ATOM   4438 C  CA  . ASP B 1 184 ? -7.053  -0.474  21.705  1.00   78.51  ? 199 ASP B CA  1 
ATOM   4439 C  C   . ASP B 1 184 ? -5.888  -0.421  22.704  1.00   77.64  ? 199 ASP B C   1 
ATOM   4440 O  O   . ASP B 1 184 ? -6.076  -0.695  23.894  1.00   76.87  ? 199 ASP B O   1 
ATOM   4441 C  CB  . ASP B 1 184 ? -8.011  0.709   21.945  1.00   77.74  ? 199 ASP B CB  1 
ATOM   4442 C  CG  . ASP B 1 184 ? -8.781  1.125   20.675  1.00   79.39  ? 199 ASP B CG  1 
ATOM   4443 O  OD1 . ASP B 1 184 ? -8.888  0.313   19.731  1.00   80.77  ? 199 ASP B OD1 1 
ATOM   4444 O  OD2 . ASP B 1 184 ? -9.281  2.269   20.614  1.00   77.66  ? 199 ASP B OD2 1 
ATOM   4445 N  N   . PRO B 1 185 ? -4.666  -0.111  22.212  1.00   77.37  ? 200 PRO B N   1 
ATOM   4446 C  CA  . PRO B 1 185 ? -3.528  0.128   23.103  1.00   74.95  ? 200 PRO B CA  1 
ATOM   4447 C  C   . PRO B 1 185 ? -3.670  1.338   24.018  1.00   71.10  ? 200 PRO B C   1 
ATOM   4448 O  O   . PRO B 1 185 ? -3.130  1.317   25.110  1.00   69.06  ? 200 PRO B O   1 
ATOM   4449 C  CB  . PRO B 1 185 ? -2.356  0.348   22.129  1.00   76.87  ? 200 PRO B CB  1 
ATOM   4450 C  CG  . PRO B 1 185 ? -2.728  -0.424  20.925  1.00   77.95  ? 200 PRO B CG  1 
ATOM   4451 C  CD  . PRO B 1 185 ? -4.219  -0.245  20.808  1.00   79.34  ? 200 PRO B CD  1 
ATOM   4452 N  N   . GLU B 1 186 ? -4.357  2.385   23.571  1.00   69.84  ? 201 GLU B N   1 
ATOM   4453 C  CA  . GLU B 1 186 ? -4.626  3.522   24.440  1.00   70.22  ? 201 GLU B CA  1 
ATOM   4454 C  C   . GLU B 1 186 ? -5.444  3.100   25.688  1.00   70.86  ? 201 GLU B C   1 
ATOM   4455 O  O   . GLU B 1 186 ? -5.165  3.557   26.813  1.00   66.90  ? 201 GLU B O   1 
ATOM   4456 C  CB  . GLU B 1 186 ? -5.314  4.678   23.689  1.00   71.37  ? 201 GLU B CB  1 
ATOM   4457 C  CG  . GLU B 1 186 ? -4.346  5.725   23.130  1.00   72.92  ? 201 GLU B CG  1 
ATOM   4458 C  CD  . GLU B 1 186 ? -4.980  7.083   22.788  1.00   73.61  ? 201 GLU B CD  1 
ATOM   4459 O  OE1 . GLU B 1 186 ? -6.147  7.362   23.170  1.00   71.73  ? 201 GLU B OE1 1 
ATOM   4460 O  OE2 . GLU B 1 186 ? -4.279  7.894   22.136  1.00   73.61  ? 201 GLU B OE2 1 
ATOM   4461 N  N   . LEU B 1 187 ? -6.426  2.216   25.499  1.00   71.29  ? 202 LEU B N   1 
ATOM   4462 C  CA  . LEU B 1 187 ? -7.139  1.643   26.638  1.00   71.32  ? 202 LEU B CA  1 
ATOM   4463 C  C   . LEU B 1 187 ? -6.178  0.865   27.544  1.00   68.70  ? 202 LEU B C   1 
ATOM   4464 O  O   . LEU B 1 187 ? -6.211  0.996   28.759  1.00   63.54  ? 202 LEU B O   1 
ATOM   4465 C  CB  . LEU B 1 187 ? -8.288  0.730   26.185  1.00   73.20  ? 202 LEU B CB  1 
ATOM   4466 C  CG  . LEU B 1 187 ? -9.066  0.054   27.334  1.00   71.79  ? 202 LEU B CG  1 
ATOM   4467 C  CD1 . LEU B 1 187 ? -9.908  1.060   28.110  1.00   70.43  ? 202 LEU B CD1 1 
ATOM   4468 C  CD2 . LEU B 1 187 ? -9.923  -1.074  26.794  1.00   73.19  ? 202 LEU B CD2 1 
ATOM   4469 N  N   . GLN B 1 188 ? -5.325  0.054   26.939  1.00   70.41  ? 203 GLN B N   1 
ATOM   4470 C  CA  . GLN B 1 188 ? -4.374  -0.720  27.699  1.00   70.58  ? 203 GLN B CA  1 
ATOM   4471 C  C   . GLN B 1 188 ? -3.416  0.167   28.477  1.00   66.81  ? 203 GLN B C   1 
ATOM   4472 O  O   . GLN B 1 188 ? -2.967  -0.205  29.557  1.00   65.41  ? 203 GLN B O   1 
ATOM   4473 C  CB  . GLN B 1 188 ? -3.577  -1.634  26.775  1.00   76.88  ? 203 GLN B CB  1 
ATOM   4474 C  CG  . GLN B 1 188 ? -2.851  -2.740  27.523  1.00   81.52  ? 203 GLN B CG  1 
ATOM   4475 C  CD  . GLN B 1 188 ? -3.825  -3.677  28.212  1.00   82.86  ? 203 GLN B CD  1 
ATOM   4476 O  OE1 . GLN B 1 188 ? -4.711  -4.243  27.559  1.00   79.75  ? 203 GLN B OE1 1 
ATOM   4477 N  NE2 . GLN B 1 188 ? -3.681  -3.836  29.538  1.00   83.59  ? 203 GLN B NE2 1 
ATOM   4478 N  N   . THR B 1 189 ? -3.111  1.331   27.917  1.00   64.95  ? 204 THR B N   1 
ATOM   4479 C  CA  . THR B 1 189 ? -2.136  2.262   28.487  1.00   64.51  ? 204 THR B CA  1 
ATOM   4480 C  C   . THR B 1 189 ? -2.719  2.994   29.689  1.00   61.84  ? 204 THR B C   1 
ATOM   4481 O  O   . THR B 1 189 ? -2.021  3.286   30.669  1.00   59.30  ? 204 THR B O   1 
ATOM   4482 C  CB  . THR B 1 189 ? -1.725  3.316   27.435  1.00   67.09  ? 204 THR B CB  1 
ATOM   4483 O  OG1 . THR B 1 189 ? -1.453  2.678   26.177  1.00   70.17  ? 204 THR B OG1 1 
ATOM   4484 C  CG2 . THR B 1 189 ? -0.505  4.093   27.889  1.00   67.12  ? 204 THR B CG2 1 
ATOM   4485 N  N   . VAL B 1 190 ? -4.007  3.315   29.577  1.00   62.24  ? 205 VAL B N   1 
ATOM   4486 C  CA  . VAL B 1 190 ? -4.778  3.873   30.677  1.00   58.93  ? 205 VAL B CA  1 
ATOM   4487 C  C   . VAL B 1 190 ? -4.662  2.853   31.786  1.00   57.33  ? 205 VAL B C   1 
ATOM   4488 O  O   . VAL B 1 190 ? -4.129  3.174   32.851  1.00   58.18  ? 205 VAL B O   1 
ATOM   4489 C  CB  . VAL B 1 190 ? -6.258  4.127   30.304  1.00   59.32  ? 205 VAL B CB  1 
ATOM   4490 C  CG1 . VAL B 1 190 ? -7.057  4.537   31.523  1.00   58.78  ? 205 VAL B CG1 1 
ATOM   4491 C  CG2 . VAL B 1 190 ? -6.383  5.219   29.251  1.00   60.53  ? 205 VAL B CG2 1 
ATOM   4492 N  N   . ILE B 1 191 ? -5.085  1.615   31.527  1.00   56.13  ? 206 ILE B N   1 
ATOM   4493 C  CA  . ILE B 1 191 ? -4.972  0.571   32.553  1.00   56.92  ? 206 ILE B CA  1 
ATOM   4494 C  C   . ILE B 1 191 ? -3.541  0.391   33.086  1.00   57.67  ? 206 ILE B C   1 
ATOM   4495 O  O   . ILE B 1 191 ? -3.361  0.210   34.279  1.00   55.70  ? 206 ILE B O   1 
ATOM   4496 C  CB  . ILE B 1 191 ? -5.526  -0.814  32.114  1.00   57.64  ? 206 ILE B CB  1 
ATOM   4497 C  CG1 . ILE B 1 191 ? -7.061  -0.899  32.279  1.00   57.35  ? 206 ILE B CG1 1 
ATOM   4498 C  CG2 . ILE B 1 191 ? -4.931  -1.935  32.975  1.00   56.96  ? 206 ILE B CG2 1 
ATOM   4499 C  CD1 . ILE B 1 191 ? -7.873  -0.286  31.161  1.00   57.70  ? 206 ILE B CD1 1 
ATOM   4500 N  N   . GLN B 1 192 ? -2.532  0.429   32.222  1.00   61.42  ? 207 GLN B N   1 
ATOM   4501 C  CA  . GLN B 1 192 ? -1.191  0.076   32.668  1.00   64.47  ? 207 GLN B CA  1 
ATOM   4502 C  C   . GLN B 1 192 ? -0.599  1.103   33.593  1.00   63.03  ? 207 GLN B C   1 
ATOM   4503 O  O   . GLN B 1 192 ? 0.106   0.745   34.536  1.00   61.74  ? 207 GLN B O   1 
ATOM   4504 C  CB  . GLN B 1 192 ? -0.245  -0.197  31.497  1.00   72.30  ? 207 GLN B CB  1 
ATOM   4505 C  CG  . GLN B 1 192 ? -0.343  -1.618  30.954  1.00   79.77  ? 207 GLN B CG  1 
ATOM   4506 C  CD  . GLN B 1 192 ? -0.314  -2.679  32.061  1.00   86.20  ? 207 GLN B CD  1 
ATOM   4507 O  OE1 . GLN B 1 192 ? -1.347  -3.019  32.672  1.00   83.37  ? 207 GLN B OE1 1 
ATOM   4508 N  NE2 . GLN B 1 192 ? 0.879   -3.217  32.318  1.00   93.15  ? 207 GLN B NE2 1 
ATOM   4509 N  N   . TYR B 1 193 ? -0.901  2.372   33.359  1.00   61.95  ? 208 TYR B N   1 
ATOM   4510 C  CA  . TYR B 1 193 ? -0.318  3.407   34.186  1.00   61.01  ? 208 TYR B CA  1 
ATOM   4511 C  C   . TYR B 1 193 ? -1.177  3.836   35.371  1.00   59.00  ? 208 TYR B C   1 
ATOM   4512 O  O   . TYR B 1 193 ? -0.617  4.312   36.360  1.00   59.65  ? 208 TYR B O   1 
ATOM   4513 C  CB  . TYR B 1 193 ? 0.155   4.564   33.314  1.00   63.02  ? 208 TYR B CB  1 
ATOM   4514 C  CG  . TYR B 1 193 ? 1.387   4.144   32.538  1.00   65.26  ? 208 TYR B CG  1 
ATOM   4515 C  CD1 . TYR B 1 193 ? 2.615   4.010   33.181  1.00   65.36  ? 208 TYR B CD1 1 
ATOM   4516 C  CD2 . TYR B 1 193 ? 1.317   3.816   31.177  1.00   67.48  ? 208 TYR B CD2 1 
ATOM   4517 C  CE1 . TYR B 1 193 ? 3.744   3.598   32.498  1.00   66.40  ? 208 TYR B CE1 1 
ATOM   4518 C  CE2 . TYR B 1 193 ? 2.448   3.394   30.483  1.00   68.01  ? 208 TYR B CE2 1 
ATOM   4519 C  CZ  . TYR B 1 193 ? 3.654   3.285   31.159  1.00   68.02  ? 208 TYR B CZ  1 
ATOM   4520 O  OH  . TYR B 1 193 ? 4.793   2.890   30.509  1.00   70.50  ? 208 TYR B OH  1 
ATOM   4521 N  N   . ASN B 1 194 ? -2.505  3.642   35.301  1.00   58.16  ? 209 ASN B N   1 
ATOM   4522 C  CA  . ASN B 1 194 ? -3.365  3.718   36.508  1.00   56.42  ? 209 ASN B CA  1 
ATOM   4523 C  C   . ASN B 1 194 ? -2.898  2.638   37.476  1.00   55.60  ? 209 ASN B C   1 
ATOM   4524 O  O   . ASN B 1 194 ? -2.558  2.919   38.618  1.00   54.56  ? 209 ASN B O   1 
ATOM   4525 C  CB  . ASN B 1 194 ? -4.843  3.447   36.215  1.00   56.83  ? 209 ASN B CB  1 
ATOM   4526 C  CG  . ASN B 1 194 ? -5.558  4.600   35.522  1.00   56.82  ? 209 ASN B CG  1 
ATOM   4527 O  OD1 . ASN B 1 194 ? -5.055  5.735   35.443  1.00   53.82  ? 209 ASN B OD1 1 
ATOM   4528 N  ND2 . ASN B 1 194 ? -6.774  4.302   35.025  1.00   56.06  ? 209 ASN B ND2 1 
ATOM   4529 N  N   . ASP B 1 195 ? -2.853  1.401   36.995  1.00   55.31  ? 210 ASP B N   1 
ATOM   4530 C  CA  . ASP B 1 195 ? -2.349  0.310   37.797  1.00   56.46  ? 210 ASP B CA  1 
ATOM   4531 C  C   . ASP B 1 195 ? -0.887  0.526   38.272  1.00   58.94  ? 210 ASP B C   1 
ATOM   4532 O  O   . ASP B 1 195 ? -0.548  0.183   39.414  1.00   60.51  ? 210 ASP B O   1 
ATOM   4533 C  CB  . ASP B 1 195 ? -2.459  -1.014  37.058  1.00   57.23  ? 210 ASP B CB  1 
ATOM   4534 C  CG  . ASP B 1 195 ? -2.005  -2.168  37.915  1.00   59.82  ? 210 ASP B CG  1 
ATOM   4535 O  OD1 . ASP B 1 195 ? -2.847  -2.649  38.720  1.00   62.63  ? 210 ASP B OD1 1 
ATOM   4536 O  OD2 . ASP B 1 195 ? -0.809  -2.550  37.839  1.00   56.65  ? 210 ASP B OD2 1 
ATOM   4537 N  N   . GLY B 1 196 ? -0.025  1.070   37.408  1.00   58.62  ? 211 GLY B N   1 
ATOM   4538 C  CA  . GLY B 1 196 ? 1.314   1.464   37.831  1.00   56.94  ? 211 GLY B CA  1 
ATOM   4539 C  C   . GLY B 1 196 ? 1.212   2.389   39.039  1.00   57.03  ? 211 GLY B C   1 
ATOM   4540 O  O   . GLY B 1 196 ? 1.740   2.093   40.121  1.00   55.69  ? 211 GLY B O   1 
ATOM   4541 N  N   . ILE B 1 197 ? 0.495   3.497   38.878  1.00   55.41  ? 212 ILE B N   1 
ATOM   4542 C  CA  . ILE B 1 197 ? 0.364   4.438   39.964  1.00   54.03  ? 212 ILE B CA  1 
ATOM   4543 C  C   . ILE B 1 197 ? -0.055  3.690   41.216  1.00   56.88  ? 212 ILE B C   1 
ATOM   4544 O  O   . ILE B 1 197 ? 0.559   3.840   42.261  1.00   61.84  ? 212 ILE B O   1 
ATOM   4545 C  CB  . ILE B 1 197 ? -0.674  5.509   39.657  1.00   51.62  ? 212 ILE B CB  1 
ATOM   4546 C  CG1 . ILE B 1 197 ? -0.124  6.456   38.605  1.00   51.61  ? 212 ILE B CG1 1 
ATOM   4547 C  CG2 . ILE B 1 197 ? -1.052  6.272   40.931  1.00   49.69  ? 212 ILE B CG2 1 
ATOM   4548 C  CD1 . ILE B 1 197 ? -1.189  7.132   37.785  1.00   51.78  ? 212 ILE B CD1 1 
ATOM   4549 N  N   . VAL B 1 198 ? -1.096  2.874   41.100  1.00   57.71  ? 213 VAL B N   1 
ATOM   4550 C  CA  . VAL B 1 198 ? -1.612  2.116   42.238  1.00   56.65  ? 213 VAL B CA  1 
ATOM   4551 C  C   . VAL B 1 198 ? -0.519  1.271   42.887  1.00   58.21  ? 213 VAL B C   1 
ATOM   4552 O  O   . VAL B 1 198 ? -0.097  1.575   43.985  1.00   54.81  ? 213 VAL B O   1 
ATOM   4553 C  CB  . VAL B 1 198 ? -2.828  1.238   41.827  1.00   55.27  ? 213 VAL B CB  1 
ATOM   4554 C  CG1 . VAL B 1 198 ? -3.038  0.052   42.770  1.00   55.08  ? 213 VAL B CG1 1 
ATOM   4555 C  CG2 . VAL B 1 198 ? -4.084  2.092   41.766  1.00   54.47  ? 213 VAL B CG2 1 
ATOM   4556 N  N   . GLN B 1 199 ? -0.064  0.235   42.182  1.00   63.66  ? 214 GLN B N   1 
ATOM   4557 C  CA  . GLN B 1 199 ? 0.830   -0.766  42.747  1.00   68.10  ? 214 GLN B CA  1 
ATOM   4558 C  C   . GLN B 1 199 ? 1.944   -0.038  43.462  1.00   69.07  ? 214 GLN B C   1 
ATOM   4559 O  O   . GLN B 1 199 ? 2.188   -0.254  44.641  1.00   72.28  ? 214 GLN B O   1 
ATOM   4560 C  CB  . GLN B 1 199 ? 1.400   -1.698  41.660  1.00   74.86  ? 214 GLN B CB  1 
ATOM   4561 C  CG  . GLN B 1 199 ? 1.966   -3.009  42.219  1.00   83.71  ? 214 GLN B CG  1 
ATOM   4562 C  CD  . GLN B 1 199 ? 3.433   -3.299  41.843  1.00   87.07  ? 214 GLN B CD  1 
ATOM   4563 O  OE1 . GLN B 1 199 ? 4.332   -3.211  42.686  1.00   83.18  ? 214 GLN B OE1 1 
ATOM   4564 N  NE2 . GLN B 1 199 ? 3.671   -3.661  40.583  1.00   89.90  ? 214 GLN B NE2 1 
ATOM   4565 N  N   . THR B 1 200 ? 2.589   0.868   42.746  1.00   69.87  ? 215 THR B N   1 
ATOM   4566 C  CA  . THR B 1 200 ? 3.604   1.723   43.328  1.00   68.74  ? 215 THR B CA  1 
ATOM   4567 C  C   . THR B 1 200 ? 3.142   2.203   44.696  1.00   65.71  ? 215 THR B C   1 
ATOM   4568 O  O   . THR B 1 200 ? 3.696   1.812   45.702  1.00   66.37  ? 215 THR B O   1 
ATOM   4569 C  CB  . THR B 1 200 ? 3.925   2.902   42.380  1.00   70.94  ? 215 THR B CB  1 
ATOM   4570 O  OG1 . THR B 1 200 ? 4.453   2.388   41.139  1.00   72.47  ? 215 THR B OG1 1 
ATOM   4571 C  CG2 . THR B 1 200 ? 4.947   3.841   42.994  1.00   72.05  ? 215 THR B CG2 1 
ATOM   4572 N  N   . ILE B 1 201 ? 2.087   2.998   44.743  1.00   66.92  ? 216 ILE B N   1 
ATOM   4573 C  CA  . ILE B 1 201 ? 1.625   3.559   46.021  1.00   67.32  ? 216 ILE B CA  1 
ATOM   4574 C  C   . ILE B 1 201 ? 1.410   2.465   47.067  1.00   70.36  ? 216 ILE B C   1 
ATOM   4575 O  O   . ILE B 1 201 ? 1.577   2.699   48.262  1.00   73.47  ? 216 ILE B O   1 
ATOM   4576 C  CB  . ILE B 1 201 ? 0.297   4.340   45.881  1.00   64.24  ? 216 ILE B CB  1 
ATOM   4577 C  CG1 . ILE B 1 201 ? 0.451   5.557   44.970  1.00   62.28  ? 216 ILE B CG1 1 
ATOM   4578 C  CG2 . ILE B 1 201 ? -0.190  4.816   47.243  1.00   64.67  ? 216 ILE B CG2 1 
ATOM   4579 C  CD1 . ILE B 1 201 ? -0.861  6.241   44.666  1.00   59.79  ? 216 ILE B CD1 1 
ATOM   4580 N  N   . ALA B 1 202 ? 1.024   1.273   46.625  1.00   72.90  ? 217 ALA B N   1 
ATOM   4581 C  CA  . ALA B 1 202 ? 0.654   0.211   47.559  1.00   74.66  ? 217 ALA B CA  1 
ATOM   4582 C  C   . ALA B 1 202 ? 1.714   0.001   48.635  1.00   75.22  ? 217 ALA B C   1 
ATOM   4583 O  O   . ALA B 1 202 ? 1.374   -0.269  49.789  1.00   71.24  ? 217 ALA B O   1 
ATOM   4584 C  CB  . ALA B 1 202 ? 0.375   -1.096  46.826  1.00   72.91  ? 217 ALA B CB  1 
ATOM   4585 N  N   . ARG B 1 203 ? 2.984   0.132   48.253  1.00   75.84  ? 218 ARG B N   1 
ATOM   4586 C  CA  . ARG B 1 203 ? 4.092   -0.037  49.186  1.00   78.20  ? 218 ARG B CA  1 
ATOM   4587 C  C   . ARG B 1 203 ? 4.564   1.302   49.779  1.00   76.25  ? 218 ARG B C   1 
ATOM   4588 O  O   . ARG B 1 203 ? 5.686   1.745   49.548  1.00   72.40  ? 218 ARG B O   1 
ATOM   4589 C  CB  . ARG B 1 203 ? 5.218   -0.790  48.496  1.00   81.31  ? 218 ARG B CB  1 
ATOM   4590 C  CG  . ARG B 1 203 ? 4.786   -2.184  48.066  1.00   85.35  ? 218 ARG B CG  1 
ATOM   4591 C  CD  . ARG B 1 203 ? 5.651   -2.695  46.939  1.00   92.25  ? 218 ARG B CD  1 
ATOM   4592 N  NE  . ARG B 1 203 ? 5.264   -2.070  45.674  1.00   96.15  ? 218 ARG B NE  1 
ATOM   4593 C  CZ  . ARG B 1 203 ? 6.101   -1.716  44.695  1.00   104.54 ? 218 ARG B CZ  1 
ATOM   4594 N  NH1 . ARG B 1 203 ? 7.420   -1.895  44.804  1.00   106.92 ? 218 ARG B NH1 1 
ATOM   4595 N  NH2 . ARG B 1 203 ? 5.612   -1.165  43.587  1.00   106.09 ? 218 ARG B NH2 1 
ATOM   4596 N  N   . GLY B 1 204 ? 3.683   1.921   50.565  1.00   77.66  ? 219 GLY B N   1 
ATOM   4597 C  CA  . GLY B 1 204 ? 3.957   3.192   51.237  1.00   77.38  ? 219 GLY B CA  1 
ATOM   4598 C  C   . GLY B 1 204 ? 3.520   4.391   50.420  1.00   77.82  ? 219 GLY B C   1 
ATOM   4599 O  O   . GLY B 1 204 ? 3.094   4.257   49.277  1.00   82.49  ? 219 GLY B O   1 
ATOM   4600 N  N   . GLY B 1 205 ? 3.633   5.575   51.008  1.00   75.02  ? 220 GLY B N   1 
ATOM   4601 C  CA  . GLY B 1 205 ? 3.223   6.802   50.334  1.00   72.75  ? 220 GLY B CA  1 
ATOM   4602 C  C   . GLY B 1 205 ? 1.752   6.812   49.948  1.00   69.83  ? 220 GLY B C   1 
ATOM   4603 O  O   . GLY B 1 205 ? 0.902   6.257   50.652  1.00   71.44  ? 220 GLY B O   1 
ATOM   4604 N  N   . ASN B 1 218 ? 10.219  6.579   50.139  1.00   66.21  ? 233 ASN B N   1 
ATOM   4605 C  CA  . ASN B 1 218 ? 11.557  6.140   49.719  1.00   70.58  ? 233 ASN B CA  1 
ATOM   4606 C  C   . ASN B 1 218 ? 11.831  6.307   48.200  1.00   74.63  ? 233 ASN B C   1 
ATOM   4607 O  O   . ASN B 1 218 ? 10.945  6.052   47.374  1.00   73.30  ? 233 ASN B O   1 
ATOM   4608 C  CB  . ASN B 1 218 ? 11.780  4.682   50.124  1.00   76.05  ? 233 ASN B CB  1 
ATOM   4609 C  CG  . ASN B 1 218 ? 10.833  3.730   49.420  1.00   77.33  ? 233 ASN B CG  1 
ATOM   4610 O  OD1 . ASN B 1 218 ? 10.462  3.946   48.267  1.00   81.46  ? 233 ASN B OD1 1 
ATOM   4611 N  ND2 . ASN B 1 218 ? 10.437  2.669   50.113  1.00   77.93  ? 233 ASN B ND2 1 
ATOM   4612 N  N   . LYS B 1 219 ? 12.745  6.913   47.700  1.00   84.91  ? 234 LYS B N   1 
ATOM   4613 C  CA  . LYS B 1 219 ? 12.867  7.167   46.240  1.00   84.50  ? 234 LYS B CA  1 
ATOM   4614 C  C   . LYS B 1 219 ? 12.428  5.888   45.540  1.00   82.01  ? 234 LYS B C   1 
ATOM   4615 O  O   . LYS B 1 219 ? 12.427  4.826   46.166  1.00   84.67  ? 234 LYS B O   1 
ATOM   4616 C  CB  . LYS B 1 219 ? 14.288  7.583   45.815  0.0000 89.86  ? 234 LYS B CB  1 
ATOM   4617 C  CG  . LYS B 1 219 ? 15.040  8.513   46.780  0.0000 92.03  ? 234 LYS B CG  1 
ATOM   4618 C  CD  . LYS B 1 219 ? 14.184  9.645   47.369  0.0000 91.17  ? 234 LYS B CD  1 
ATOM   4619 C  CE  . LYS B 1 219 ? 14.809  10.261  48.616  0.0000 91.03  ? 234 LYS B CE  1 
ATOM   4620 N  NZ  . LYS B 1 219 ? 15.013  9.273   49.715  0.0000 90.93  ? 234 LYS B NZ  1 
ATOM   4621 N  N   . ASP B 1 220 ? 12.003  5.967   44.251  1.00   76.32  ? 235 ASP B N   1 
ATOM   4622 C  CA  . ASP B 1 220 ? 10.969  5.073   43.640  1.00   72.79  ? 235 ASP B CA  1 
ATOM   4623 C  C   . ASP B 1 220 ? 9.533   5.662   43.938  1.00   68.16  ? 235 ASP B C   1 
ATOM   4624 O  O   . ASP B 1 220 ? 8.507   5.012   43.743  1.00   64.06  ? 235 ASP B O   1 
ATOM   4625 C  CB  . ASP B 1 220 ? 11.113  3.588   44.043  1.00   72.64  ? 235 ASP B CB  1 
ATOM   4626 C  CG  . ASP B 1 220 ? 12.581  3.085   44.017  1.00   75.71  ? 235 ASP B CG  1 
ATOM   4627 O  OD1 . ASP B 1 220 ? 13.492  3.859   43.656  1.00   75.62  ? 235 ASP B OD1 1 
ATOM   4628 O  OD2 . ASP B 1 220 ? 12.836  1.914   44.401  1.00   77.63  ? 235 ASP B OD2 1 
ATOM   4629 N  N   . LEU B 1 221 ? 9.520   6.887   44.477  1.00   64.72  ? 236 LEU B N   1 
ATOM   4630 C  CA  . LEU B 1 221 ? 8.650   7.965   44.027  1.00   63.68  ? 236 LEU B CA  1 
ATOM   4631 C  C   . LEU B 1 221 ? 8.901   8.310   42.551  1.00   67.85  ? 236 LEU B C   1 
ATOM   4632 O  O   . LEU B 1 221 ? 8.025   8.829   41.867  1.00   68.28  ? 236 LEU B O   1 
ATOM   4633 C  CB  . LEU B 1 221 ? 8.966   9.265   44.768  1.00   61.86  ? 236 LEU B CB  1 
ATOM   4634 C  CG  . LEU B 1 221 ? 8.480   9.609   46.179  1.00   60.70  ? 236 LEU B CG  1 
ATOM   4635 C  CD1 . LEU B 1 221 ? 7.402   8.678   46.734  1.00   58.75  ? 236 LEU B CD1 1 
ATOM   4636 C  CD2 . LEU B 1 221 ? 9.678   9.678   47.102  1.00   62.54  ? 236 LEU B CD2 1 
ATOM   4637 N  N   . LYS B 1 222 ? 10.125  8.099   42.082  1.00   71.66  ? 237 LYS B N   1 
ATOM   4638 C  CA  . LYS B 1 222 ? 10.462  8.398   40.701  1.00   75.38  ? 237 LYS B CA  1 
ATOM   4639 C  C   . LYS B 1 222 ? 9.653   7.522   39.746  1.00   72.52  ? 237 LYS B C   1 
ATOM   4640 O  O   . LYS B 1 222 ? 9.184   7.997   38.709  1.00   72.20  ? 237 LYS B O   1 
ATOM   4641 C  CB  . LYS B 1 222 ? 11.978  8.263   40.453  1.00   81.65  ? 237 LYS B CB  1 
ATOM   4642 C  CG  . LYS B 1 222 ? 12.797  9.544   40.709  1.00   87.45  ? 237 LYS B CG  1 
ATOM   4643 C  CD  . LYS B 1 222 ? 12.406  10.262  42.010  1.00   90.02  ? 237 LYS B CD  1 
ATOM   4644 C  CE  . LYS B 1 222 ? 13.567  10.993  42.682  1.00   92.29  ? 237 LYS B CE  1 
ATOM   4645 N  NZ  . LYS B 1 222 ? 13.336  11.054  44.160  1.00   90.06  ? 237 LYS B NZ  1 
ATOM   4646 N  N   . ARG B 1 223 ? 9.462   6.258   40.110  1.00   69.16  ? 238 ARG B N   1 
ATOM   4647 C  CA  . ARG B 1 223 ? 8.665   5.360   39.289  1.00   68.17  ? 238 ARG B CA  1 
ATOM   4648 C  C   . ARG B 1 223 ? 7.211   5.808   39.284  1.00   68.51  ? 238 ARG B C   1 
ATOM   4649 O  O   . ARG B 1 223 ? 6.468   5.490   38.351  1.00   74.07  ? 238 ARG B O   1 
ATOM   4650 C  CB  . ARG B 1 223 ? 8.770   3.918   39.772  1.00   67.02  ? 238 ARG B CB  1 
ATOM   4651 C  CG  . ARG B 1 223 ? 8.491   2.904   38.676  1.00   67.80  ? 238 ARG B CG  1 
ATOM   4652 C  CD  . ARG B 1 223 ? 7.138   2.268   38.811  1.00   67.92  ? 238 ARG B CD  1 
ATOM   4653 N  NE  . ARG B 1 223 ? 6.718   1.585   37.586  1.00   73.13  ? 238 ARG B NE  1 
ATOM   4654 C  CZ  . ARG B 1 223 ? 5.619   0.819   37.479  1.00   76.86  ? 238 ARG B CZ  1 
ATOM   4655 N  NH1 . ARG B 1 223 ? 4.820   0.602   38.534  1.00   76.34  ? 238 ARG B NH1 1 
ATOM   4656 N  NH2 . ARG B 1 223 ? 5.310   0.248   36.312  1.00   75.74  ? 238 ARG B NH2 1 
ATOM   4657 N  N   . LEU B 1 224 ? 6.811   6.538   40.328  1.00   64.29  ? 239 LEU B N   1 
ATOM   4658 C  CA  . LEU B 1 224 ? 5.498   7.169   40.391  1.00   59.05  ? 239 LEU B CA  1 
ATOM   4659 C  C   . LEU B 1 224 ? 5.470   8.415   39.555  1.00   58.21  ? 239 LEU B C   1 
ATOM   4660 O  O   . LEU B 1 224 ? 4.484   8.678   38.887  1.00   57.40  ? 239 LEU B O   1 
ATOM   4661 C  CB  . LEU B 1 224 ? 5.144   7.552   41.821  1.00   57.26  ? 239 LEU B CB  1 
ATOM   4662 C  CG  . LEU B 1 224 ? 3.695   7.974   41.999  1.00   56.65  ? 239 LEU B CG  1 
ATOM   4663 C  CD1 . LEU B 1 224 ? 2.838   6.727   42.092  1.00   55.94  ? 239 LEU B CD1 1 
ATOM   4664 C  CD2 . LEU B 1 224 ? 3.538   8.849   43.234  1.00   57.30  ? 239 LEU B CD2 1 
ATOM   4665 N  N   . LYS B 1 225 ? 6.534   9.208   39.622  1.00   59.63  ? 240 LYS B N   1 
ATOM   4666 C  CA  . LYS B 1 225 ? 6.699   10.316  38.681  1.00   61.68  ? 240 LYS B CA  1 
ATOM   4667 C  C   . LYS B 1 225 ? 6.545   9.831   37.234  1.00   59.92  ? 240 LYS B C   1 
ATOM   4668 O  O   . LYS B 1 225 ? 5.826   10.435  36.460  1.00   57.87  ? 240 LYS B O   1 
ATOM   4669 C  CB  . LYS B 1 225 ? 8.036   11.029  38.861  1.00   64.05  ? 240 LYS B CB  1 
ATOM   4670 C  CG  . LYS B 1 225 ? 8.058   11.994  40.041  1.00   66.24  ? 240 LYS B CG  1 
ATOM   4671 C  CD  . LYS B 1 225 ? 9.267   12.938  40.027  1.00   70.94  ? 240 LYS B CD  1 
ATOM   4672 C  CE  . LYS B 1 225 ? 10.573  12.232  39.641  1.00   74.06  ? 240 LYS B CE  1 
ATOM   4673 N  NZ  . LYS B 1 225 ? 11.807  12.949  40.087  1.00   76.94  ? 240 LYS B NZ  1 
ATOM   4674 N  N   . GLU B 1 226 ? 7.183   8.728   36.883  1.00   59.12  ? 241 GLU B N   1 
ATOM   4675 C  CA  . GLU B 1 226 ? 6.976   8.170   35.563  1.00   61.65  ? 241 GLU B CA  1 
ATOM   4676 C  C   . GLU B 1 226 ? 5.491   7.947   35.255  1.00   61.80  ? 241 GLU B C   1 
ATOM   4677 O  O   . GLU B 1 226 ? 4.949   8.581   34.352  1.00   65.95  ? 241 GLU B O   1 
ATOM   4678 C  CB  . GLU B 1 226 ? 7.741   6.866   35.388  1.00   61.19  ? 241 GLU B CB  1 
ATOM   4679 C  CG  . GLU B 1 226 ? 9.205   7.085   35.133  1.00   62.64  ? 241 GLU B CG  1 
ATOM   4680 C  CD  . GLU B 1 226 ? 10.052  5.935   35.639  1.00   63.98  ? 241 GLU B CD  1 
ATOM   4681 O  OE1 . GLU B 1 226 ? 11.147  6.219   36.182  1.00   67.37  ? 241 GLU B OE1 1 
ATOM   4682 O  OE2 . GLU B 1 226 ? 9.631   4.758   35.500  1.00   62.29  ? 241 GLU B OE2 1 
ATOM   4683 N  N   . CYS B 1 227 ? 4.838   7.049   35.986  1.00   59.25  ? 242 CYS B N   1 
ATOM   4684 C  CA  . CYS B 1 227 ? 3.496   6.618   35.612  1.00   57.73  ? 242 CYS B CA  1 
ATOM   4685 C  C   . CYS B 1 227 ? 2.551   7.790   35.498  1.00   55.50  ? 242 CYS B C   1 
ATOM   4686 O  O   . CYS B 1 227 ? 1.733   7.848   34.598  1.00   58.24  ? 242 CYS B O   1 
ATOM   4687 C  CB  . CYS B 1 227 ? 2.948   5.624   36.625  1.00   58.31  ? 242 CYS B CB  1 
ATOM   4688 S  SG  . CYS B 1 227 ? 3.886   4.084   36.723  1.00   60.51  ? 242 CYS B SG  1 
ATOM   4689 N  N   . VAL B 1 228 ? 2.671   8.718   36.431  1.00   53.35  ? 243 VAL B N   1 
ATOM   4690 C  CA  . VAL B 1 228 ? 1.889   9.945   36.429  1.00   51.75  ? 243 VAL B CA  1 
ATOM   4691 C  C   . VAL B 1 228 ? 2.137   10.743  35.154  1.00   51.76  ? 243 VAL B C   1 
ATOM   4692 O  O   . VAL B 1 228 ? 1.205   11.252  34.547  1.00   52.04  ? 243 VAL B O   1 
ATOM   4693 C  CB  . VAL B 1 228 ? 2.214   10.795  37.688  1.00   50.56  ? 243 VAL B CB  1 
ATOM   4694 C  CG1 . VAL B 1 228 ? 1.764   12.243  37.536  1.00   51.15  ? 243 VAL B CG1 1 
ATOM   4695 C  CG2 . VAL B 1 228 ? 1.562   10.166  38.900  1.00   49.12  ? 243 VAL B CG2 1 
ATOM   4696 N  N   . SER B 1 229 ? 3.398   10.849  34.760  1.00   52.31  ? 244 SER B N   1 
ATOM   4697 C  CA  . SER B 1 229 ? 3.779   11.622  33.582  1.00   54.17  ? 244 SER B CA  1 
ATOM   4698 C  C   . SER B 1 229 ? 3.011   11.129  32.366  1.00   54.03  ? 244 SER B C   1 
ATOM   4699 O  O   . SER B 1 229 ? 2.337   11.909  31.691  1.00   53.49  ? 244 SER B O   1 
ATOM   4700 C  CB  . SER B 1 229 ? 5.282   11.528  33.321  1.00   55.49  ? 244 SER B CB  1 
ATOM   4701 O  OG  . SER B 1 229 ? 5.586   12.056  32.047  1.00   58.91  ? 244 SER B OG  1 
ATOM   4702 N  N   . ILE B 1 230 ? 3.080   9.827   32.123  1.00   53.77  ? 245 ILE B N   1 
ATOM   4703 C  CA  . ILE B 1 230 ? 2.341   9.230   31.022  1.00   55.01  ? 245 ILE B CA  1 
ATOM   4704 C  C   . ILE B 1 230 ? 0.841   9.423   31.186  1.00   55.00  ? 245 ILE B C   1 
ATOM   4705 O  O   . ILE B 1 230 ? 0.128   9.556   30.185  1.00   56.77  ? 245 ILE B O   1 
ATOM   4706 C  CB  . ILE B 1 230 ? 2.675   7.745   30.838  1.00   54.71  ? 245 ILE B CB  1 
ATOM   4707 C  CG1 . ILE B 1 230 ? 4.125   7.616   30.381  1.00   55.46  ? 245 ILE B CG1 1 
ATOM   4708 C  CG2 . ILE B 1 230 ? 1.741   7.094   29.814  1.00   54.94  ? 245 ILE B CG2 1 
ATOM   4709 C  CD1 . ILE B 1 230 ? 4.673   6.236   30.590  1.00   55.55  ? 245 ILE B CD1 1 
ATOM   4710 N  N   . ARG B 1 231 ? 0.356   9.450   32.425  1.00   53.19  ? 246 ARG B N   1 
ATOM   4711 C  CA  . ARG B 1 231 ? -1.063  9.670   32.641  1.00   53.14  ? 246 ARG B CA  1 
ATOM   4712 C  C   . ARG B 1 231 ? -1.443  11.085  32.227  1.00   53.80  ? 246 ARG B C   1 
ATOM   4713 O  O   . ARG B 1 231 ? -2.428  11.278  31.538  1.00   53.61  ? 246 ARG B O   1 
ATOM   4714 C  CB  . ARG B 1 231 ? -1.441  9.424   34.105  1.00   53.12  ? 246 ARG B CB  1 
ATOM   4715 C  CG  . ARG B 1 231 ? -2.941  9.591   34.436  1.00   52.84  ? 246 ARG B CG  1 
ATOM   4716 C  CD  . ARG B 1 231 ? -3.162  9.898   35.911  1.00   51.64  ? 246 ARG B CD  1 
ATOM   4717 N  NE  . ARG B 1 231 ? -2.585  11.200  36.268  1.00   52.32  ? 246 ARG B NE  1 
ATOM   4718 C  CZ  . ARG B 1 231 ? -2.529  11.700  37.509  1.00   51.16  ? 246 ARG B CZ  1 
ATOM   4719 N  NH1 . ARG B 1 231 ? -3.007  11.021  38.547  1.00   47.82  ? 246 ARG B NH1 1 
ATOM   4720 N  NH2 . ARG B 1 231 ? -1.991  12.901  37.709  1.00   52.17  ? 246 ARG B NH2 1 
ATOM   4721 N  N   . ASP B 1 232 ? -0.652  12.067  32.646  1.00   54.98  ? 247 ASP B N   1 
ATOM   4722 C  CA  . ASP B 1 232 ? -0.987  13.483  32.433  1.00   56.74  ? 247 ASP B CA  1 
ATOM   4723 C  C   . ASP B 1 232 ? -0.853  13.904  30.965  1.00   58.04  ? 247 ASP B C   1 
ATOM   4724 O  O   . ASP B 1 232 ? -1.703  14.616  30.448  1.00   60.32  ? 247 ASP B O   1 
ATOM   4725 C  CB  . ASP B 1 232 ? -0.074  14.397  33.274  1.00   57.68  ? 247 ASP B CB  1 
ATOM   4726 C  CG  . ASP B 1 232 ? -0.328  14.306  34.783  1.00   58.48  ? 247 ASP B CG  1 
ATOM   4727 O  OD1 . ASP B 1 232 ? -1.317  13.668  35.262  1.00   57.20  ? 247 ASP B OD1 1 
ATOM   4728 O  OD2 . ASP B 1 232 ? 0.503   14.911  35.504  1.00   61.66  ? 247 ASP B OD2 1 
ATOM   4729 N  N   . GLN B 1 233 ? 0.238   13.499  30.320  1.00   56.97  ? 248 GLN B N   1 
ATOM   4730 C  CA  . GLN B 1 233 ? 0.495   13.862  28.938  1.00   58.60  ? 248 GLN B CA  1 
ATOM   4731 C  C   . GLN B 1 233 ? -0.700  13.477  28.098  1.00   58.35  ? 248 GLN B C   1 
ATOM   4732 O  O   . GLN B 1 233 ? -1.290  14.310  27.419  1.00   58.96  ? 248 GLN B O   1 
ATOM   4733 C  CB  . GLN B 1 233 ? 1.741   13.134  28.400  1.00   59.06  ? 248 GLN B CB  1 
ATOM   4734 C  CG  . GLN B 1 233 ? 3.078   13.750  28.806  1.00   59.37  ? 248 GLN B CG  1 
ATOM   4735 C  CD  . GLN B 1 233 ? 4.271   12.941  28.304  1.00   61.10  ? 248 GLN B CD  1 
ATOM   4736 O  OE1 . GLN B 1 233 ? 4.489   12.793  27.093  1.00   63.37  ? 248 GLN B OE1 1 
ATOM   4737 N  NE2 . GLN B 1 233 ? 5.064   12.423  29.234  1.00   61.21  ? 248 GLN B NE2 1 
ATOM   4738 N  N   . LEU B 1 234 ? -1.049  12.200  28.181  1.00   56.80  ? 249 LEU B N   1 
ATOM   4739 C  CA  . LEU B 1 234 ? -2.135  11.635  27.419  1.00   56.95  ? 249 LEU B CA  1 
ATOM   4740 C  C   . LEU B 1 234 ? -3.397  12.454  27.630  1.00   59.13  ? 249 LEU B C   1 
ATOM   4741 O  O   . LEU B 1 234 ? -3.998  12.953  26.672  1.00   61.68  ? 249 LEU B O   1 
ATOM   4742 C  CB  . LEU B 1 234 ? -2.329  10.188  27.836  1.00   54.62  ? 249 LEU B CB  1 
ATOM   4743 C  CG  . LEU B 1 234 ? -3.513  9.435   27.256  1.00   54.76  ? 249 LEU B CG  1 
ATOM   4744 C  CD1 . LEU B 1 234 ? -3.255  7.940   27.319  1.00   54.15  ? 249 LEU B CD1 1 
ATOM   4745 C  CD2 . LEU B 1 234 ? -4.792  9.772   28.009  1.00   54.17  ? 249 LEU B CD2 1 
ATOM   4746 N  N   . LEU B 1 235 ? -3.793  12.603  28.887  1.00   59.21  ? 250 LEU B N   1 
ATOM   4747 C  CA  . LEU B 1 235 ? -4.890  13.492  29.229  1.00   60.77  ? 250 LEU B CA  1 
ATOM   4748 C  C   . LEU B 1 235 ? -4.698  14.874  28.603  1.00   64.20  ? 250 LEU B C   1 
ATOM   4749 O  O   . LEU B 1 235 ? -5.609  15.378  27.951  1.00   67.72  ? 250 LEU B O   1 
ATOM   4750 C  CB  . LEU B 1 235 ? -5.078  13.599  30.749  1.00   58.97  ? 250 LEU B CB  1 
ATOM   4751 C  CG  . LEU B 1 235 ? -6.188  12.753  31.417  1.00   58.93  ? 250 LEU B CG  1 
ATOM   4752 C  CD1 . LEU B 1 235 ? -6.488  11.435  30.711  1.00   59.51  ? 250 LEU B CD1 1 
ATOM   4753 C  CD2 . LEU B 1 235 ? -5.879  12.479  32.894  1.00   57.86  ? 250 LEU B CD2 1 
ATOM   4754 N  N   . TYR B 1 236 ? -3.518  15.466  28.760  1.00   64.93  ? 251 TYR B N   1 
ATOM   4755 C  CA  . TYR B 1 236 ? -3.273  16.814  28.260  1.00   67.61  ? 251 TYR B CA  1 
ATOM   4756 C  C   . TYR B 1 236 ? -3.526  16.911  26.745  1.00   71.04  ? 251 TYR B C   1 
ATOM   4757 O  O   . TYR B 1 236 ? -4.146  17.866  26.270  1.00   71.44  ? 251 TYR B O   1 
ATOM   4758 C  CB  . TYR B 1 236 ? -1.856  17.253  28.604  1.00   67.62  ? 251 TYR B CB  1 
ATOM   4759 C  CG  . TYR B 1 236 ? -1.602  18.731  28.421  1.00   70.44  ? 251 TYR B CG  1 
ATOM   4760 C  CD1 . TYR B 1 236 ? -2.256  19.681  29.212  1.00   71.09  ? 251 TYR B CD1 1 
ATOM   4761 C  CD2 . TYR B 1 236 ? -0.690  19.184  27.467  1.00   73.07  ? 251 TYR B CD2 1 
ATOM   4762 C  CE1 . TYR B 1 236 ? -2.008  21.043  29.052  1.00   73.36  ? 251 TYR B CE1 1 
ATOM   4763 C  CE2 . TYR B 1 236 ? -0.439  20.534  27.289  1.00   75.12  ? 251 TYR B CE2 1 
ATOM   4764 C  CZ  . TYR B 1 236 ? -1.093  21.459  28.081  1.00   76.30  ? 251 TYR B CZ  1 
ATOM   4765 O  OH  . TYR B 1 236 ? -0.818  22.791  27.887  1.00   78.53  ? 251 TYR B OH  1 
ATOM   4766 N  N   . LYS B 1 237 ? -3.063  15.912  25.997  1.00   73.04  ? 252 LYS B N   1 
ATOM   4767 C  CA  . LYS B 1 237 ? -3.360  15.820  24.570  1.00   75.94  ? 252 LYS B CA  1 
ATOM   4768 C  C   . LYS B 1 237 ? -4.858  15.785  24.430  1.00   76.38  ? 252 LYS B C   1 
ATOM   4769 O  O   . LYS B 1 237 ? -5.444  16.591  23.717  1.00   80.74  ? 252 LYS B O   1 
ATOM   4770 C  CB  . LYS B 1 237 ? -2.755  14.550  23.948  1.00   76.83  ? 252 LYS B CB  1 
ATOM   4771 C  CG  . LYS B 1 237 ? -3.287  14.167  22.559  1.00   80.17  ? 252 LYS B CG  1 
ATOM   4772 C  CD  . LYS B 1 237 ? -3.142  12.675  22.261  1.00   80.58  ? 252 LYS B CD  1 
ATOM   4773 C  CE  . LYS B 1 237 ? -4.307  12.084  21.475  1.00   82.83  ? 252 LYS B CE  1 
ATOM   4774 N  NZ  . LYS B 1 237 ? -4.288  10.595  21.373  1.00   82.40  ? 252 LYS B NZ  1 
ATOM   4775 N  N   . LYS B 1 238 ? -5.482  14.857  25.132  1.00   74.29  ? 253 LYS B N   1 
ATOM   4776 C  CA  . LYS B 1 238 ? -6.919  14.684  25.024  1.00   74.77  ? 253 LYS B CA  1 
ATOM   4777 C  C   . LYS B 1 238 ? -7.663  15.990  25.414  1.00   75.16  ? 253 LYS B C   1 
ATOM   4778 O  O   . LYS B 1 238 ? -8.764  16.260  24.936  1.00   76.17  ? 253 LYS B O   1 
ATOM   4779 C  CB  . LYS B 1 238 ? -7.340  13.467  25.862  1.00   73.00  ? 253 LYS B CB  1 
ATOM   4780 C  CG  . LYS B 1 238 ? -8.546  12.701  25.348  1.00   74.15  ? 253 LYS B CG  1 
ATOM   4781 C  CD  . LYS B 1 238 ? -8.343  11.997  24.003  1.00   75.81  ? 253 LYS B CD  1 
ATOM   4782 C  CE  . LYS B 1 238 ? -9.592  12.135  23.107  1.00   78.13  ? 253 LYS B CE  1 
ATOM   4783 N  NZ  . LYS B 1 238 ? -10.116 10.852  22.545  1.00   77.47  ? 253 LYS B NZ  1 
ATOM   4784 N  N   . LEU B 1 239 ? -7.031  16.814  26.246  1.00   74.40  ? 254 LEU B N   1 
ATOM   4785 C  CA  . LEU B 1 239 ? -7.551  18.147  26.590  1.00   75.13  ? 254 LEU B CA  1 
ATOM   4786 C  C   . LEU B 1 239 ? -7.484  19.128  25.426  1.00   75.73  ? 254 LEU B C   1 
ATOM   4787 O  O   . LEU B 1 239 ? -8.506  19.692  25.037  1.00   75.40  ? 254 LEU B O   1 
ATOM   4788 C  CB  . LEU B 1 239 ? -6.809  18.715  27.818  1.00   75.45  ? 254 LEU B CB  1 
ATOM   4789 C  CG  . LEU B 1 239 ? -6.696  20.219  28.121  1.00   77.51  ? 254 LEU B CG  1 
ATOM   4790 C  CD1 . LEU B 1 239 ? -8.009  20.966  27.999  1.00   80.80  ? 254 LEU B CD1 1 
ATOM   4791 C  CD2 . LEU B 1 239 ? -6.172  20.386  29.538  1.00   76.80  ? 254 LEU B CD2 1 
ATOM   4792 N  N   . LEU B 1 240 ? -6.279  19.355  24.905  1.00   74.77  ? 255 LEU B N   1 
ATOM   4793 C  CA  . LEU B 1 240 ? -6.090  20.257  23.768  1.00   75.91  ? 255 LEU B CA  1 
ATOM   4794 C  C   . LEU B 1 240 ? -7.073  19.885  22.664  1.00   77.09  ? 255 LEU B C   1 
ATOM   4795 O  O   . LEU B 1 240 ? -7.801  20.742  22.165  1.00   77.57  ? 255 LEU B O   1 
ATOM   4796 C  CB  . LEU B 1 240 ? -4.633  20.224  23.270  1.00   75.75  ? 255 LEU B CB  1 
ATOM   4797 C  CG  . LEU B 1 240 ? -3.656  21.322  23.755  1.00   75.84  ? 255 LEU B CG  1 
ATOM   4798 C  CD1 . LEU B 1 240 ? -4.028  21.905  25.112  1.00   75.21  ? 255 LEU B CD1 1 
ATOM   4799 C  CD2 . LEU B 1 240 ? -2.223  20.811  23.789  1.00   74.63  ? 255 LEU B CD2 1 
ATOM   4800 N  N   . GLU B 1 241 ? -7.116  18.591  22.341  1.00   76.62  ? 256 GLU B N   1 
ATOM   4801 C  CA  . GLU B 1 241 ? -8.096  18.015  21.411  1.00   77.80  ? 256 GLU B CA  1 
ATOM   4802 C  C   . GLU B 1 241 ? -9.542  18.398  21.715  1.00   78.69  ? 256 GLU B C   1 
ATOM   4803 O  O   . GLU B 1 241 ? -10.362 18.454  20.828  1.00   80.91  ? 256 GLU B O   1 
ATOM   4804 C  CB  . GLU B 1 241 ? -7.969  16.487  21.393  1.00   76.46  ? 256 GLU B CB  1 
ATOM   4805 C  CG  . GLU B 1 241 ? -6.720  16.008  20.663  1.00   77.66  ? 256 GLU B CG  1 
ATOM   4806 C  CD  . GLU B 1 241 ? -6.571  14.489  20.579  1.00   76.75  ? 256 GLU B CD  1 
ATOM   4807 O  OE1 . GLU B 1 241 ? -7.441  13.721  21.060  1.00   75.79  ? 256 GLU B OE1 1 
ATOM   4808 O  OE2 . GLU B 1 241 ? -5.544  14.062  20.014  1.00   76.90  ? 256 GLU B OE2 1 
ATOM   4809 N  N   . HIS B 1 242 ? -9.861  18.626  22.980  1.00   80.25  ? 257 HIS B N   1 
ATOM   4810 C  CA  . HIS B 1 242 ? -11.217 19.038  23.376  1.00   80.30  ? 257 HIS B CA  1 
ATOM   4811 C  C   . HIS B 1 242 ? -11.458 20.512  23.152  1.00   82.98  ? 257 HIS B C   1 
ATOM   4812 O  O   . HIS B 1 242 ? -12.571 20.915  22.800  1.00   84.37  ? 257 HIS B O   1 
ATOM   4813 C  CB  . HIS B 1 242 ? -11.500 18.666  24.838  1.00   76.21  ? 257 HIS B CB  1 
ATOM   4814 C  CG  . HIS B 1 242 ? -12.172 17.344  24.977  1.00   74.69  ? 257 HIS B CG  1 
ATOM   4815 N  ND1 . HIS B 1 242 ? -11.710 16.219  24.334  1.00   73.92  ? 257 HIS B ND1 1 
ATOM   4816 C  CD2 . HIS B 1 242 ? -13.283 16.967  25.651  1.00   74.51  ? 257 HIS B CD2 1 
ATOM   4817 C  CE1 . HIS B 1 242 ? -12.503 15.202  24.605  1.00   73.39  ? 257 HIS B CE1 1 
ATOM   4818 N  NE2 . HIS B 1 242 ? -13.462 15.626  25.409  1.00   74.11  ? 257 HIS B NE2 1 
ATOM   4819 N  N   . LYS B 1 243 ? -10.412 21.307  23.359  1.00   84.02  ? 258 LYS B N   1 
ATOM   4820 C  CA  . LYS B 1 243 ? -10.535 22.743  23.276  1.00   87.75  ? 258 LYS B CA  1 
ATOM   4821 C  C   . LYS B 1 243 ? -10.943 23.196  21.875  1.00   93.40  ? 258 LYS B C   1 
ATOM   4822 O  O   . LYS B 1 243 ? -11.626 24.203  21.740  1.00   94.62  ? 258 LYS B O   1 
ATOM   4823 C  CB  . LYS B 1 243 ? -9.257  23.439  23.729  1.00   86.31  ? 258 LYS B CB  1 
ATOM   4824 C  CG  . LYS B 1 243 ? -9.531  24.878  24.121  1.00   88.05  ? 258 LYS B CG  1 
ATOM   4825 C  CD  . LYS B 1 243 ? -8.268  25.644  24.422  1.00   87.21  ? 258 LYS B CD  1 
ATOM   4826 C  CE  . LYS B 1 243 ? -7.662  25.231  25.736  1.00   83.11  ? 258 LYS B CE  1 
ATOM   4827 N  NZ  . LYS B 1 243 ? -6.500  26.112  26.007  1.00   83.10  ? 258 LYS B NZ  1 
ATOM   4828 N  N   . LYS B 1 244 ? -10.536 22.457  20.843  1.00   97.97  ? 259 LYS B N   1 
ATOM   4829 C  CA  . LYS B 1 244 ? -11.124 22.653  19.532  1.00   103.13 ? 259 LYS B CA  1 
ATOM   4830 C  C   . LYS B 1 244 ? -12.645 22.405  19.625  1.00   105.52 ? 259 LYS B C   1 
ATOM   4831 O  O   . LYS B 1 244 ? -13.392 23.352  19.871  1.00   107.43 ? 259 LYS B O   1 
ATOM   4832 C  CB  . LYS B 1 244 ? -10.418 21.836  18.432  1.00   106.16 ? 259 LYS B CB  1 
ATOM   4833 C  CG  . LYS B 1 244 ? -10.355 20.320  18.603  1.00   107.22 ? 259 LYS B CG  1 
ATOM   4834 C  CD  . LYS B 1 244 ? -9.711  19.623  17.408  1.00   112.26 ? 259 LYS B CD  1 
ATOM   4835 C  CE  . LYS B 1 244 ? -10.393 18.302  17.026  1.00   114.17 ? 259 LYS B CE  1 
ATOM   4836 N  NZ  . LYS B 1 244 ? -11.281 18.388  15.812  1.00   115.80 ? 259 LYS B NZ  1 
ATOM   4837 N  N   . SER B 1 245 ? -13.105 21.156  19.532  1.00   106.70 ? 260 SER B N   1 
ATOM   4838 C  CA  . SER B 1 245 ? -14.531 20.878  19.271  1.00   110.32 ? 260 SER B CA  1 
ATOM   4839 C  C   . SER B 1 245 ? -15.348 21.181  20.514  1.00   108.92 ? 260 SER B C   1 
ATOM   4840 O  O   . SER B 1 245 ? -15.541 20.306  21.354  1.00   108.53 ? 260 SER B O   1 
ATOM   4841 C  CB  . SER B 1 245 ? -14.751 19.418  18.814  1.00   111.40 ? 260 SER B CB  1 
ATOM   4842 O  OG  . SER B 1 245 ? -14.617 19.273  17.397  1.00   113.12 ? 260 SER B OG  1 
ATOM   4843 N  N   . LEU B 1 246 ? -15.822 22.419  20.634  1.00   109.46 ? 261 LEU B N   1 
ATOM   4844 C  CA  . LEU B 1 246 ? -16.300 22.910  21.924  1.00   109.88 ? 261 LEU B CA  1 
ATOM   4845 C  C   . LEU B 1 246 ? -17.733 23.451  21.914  1.00   112.66 ? 261 LEU B C   1 
ATOM   4846 O  O   . LEU B 1 246 ? -17.985 24.533  21.399  1.00   115.22 ? 261 LEU B O   1 
ATOM   4847 C  CB  . LEU B 1 246 ? -15.328 23.973  22.456  1.00   110.16 ? 261 LEU B CB  1 
ATOM   4848 C  CG  . LEU B 1 246 ? -15.321 24.245  23.978  1.00   108.68 ? 261 LEU B CG  1 
ATOM   4849 C  CD1 . LEU B 1 246 ? -15.551 22.997  24.821  1.00   104.87 ? 261 LEU B CD1 1 
ATOM   4850 C  CD2 . LEU B 1 246 ? -14.015 24.913  24.392  1.00   107.10 ? 261 LEU B CD2 1 
ATOM   4851 N  N   . THR B 1 247 ? -18.652 22.703  22.534  1.00   112.71 ? 262 THR B N   1 
ATOM   4852 C  CA  . THR B 1 247 ? -20.088 23.018  22.529  1.00   112.45 ? 262 THR B CA  1 
ATOM   4853 C  C   . THR B 1 247 ? -20.566 23.396  23.953  1.00   111.49 ? 262 THR B C   1 
ATOM   4854 O  O   . THR B 1 247 ? -20.963 22.521  24.737  1.00   109.93 ? 262 THR B O   1 
ATOM   4855 C  CB  . THR B 1 247 ? -20.898 21.816  21.975  1.00   111.48 ? 262 THR B CB  1 
ATOM   4856 O  OG1 . THR B 1 247 ? -20.175 21.202  20.898  1.00   110.00 ? 262 THR B OG1 1 
ATOM   4857 C  CG2 . THR B 1 247 ? -22.281 22.247  21.477  1.00   113.81 ? 262 THR B CG2 1 
ATOM   4858 N  N   . PRO B 1 248 ? -20.500 24.702  24.304  1.00   111.00 ? 263 PRO B N   1 
ATOM   4859 C  CA  . PRO B 1 248 ? -20.988 25.190  25.601  1.00   111.17 ? 263 PRO B CA  1 
ATOM   4860 C  C   . PRO B 1 248 ? -22.447 24.847  25.944  1.00   115.37 ? 263 PRO B C   1 
ATOM   4861 O  O   . PRO B 1 248 ? -22.785 24.773  27.133  1.00   115.89 ? 263 PRO B O   1 
ATOM   4862 C  CB  . PRO B 1 248 ? -20.818 26.708  25.489  1.00   111.39 ? 263 PRO B CB  1 
ATOM   4863 C  CG  . PRO B 1 248 ? -19.685 26.896  24.553  1.00   110.91 ? 263 PRO B CG  1 
ATOM   4864 C  CD  . PRO B 1 248 ? -19.667 25.715  23.626  1.00   110.97 ? 263 PRO B CD  1 
ATOM   4865 N  N   . GLY B 1 249 ? -23.290 24.644  24.929  1.00   118.34 ? 264 GLY B N   1 
ATOM   4866 C  CA  . GLY B 1 249 ? -24.711 24.341  25.132  1.00   120.60 ? 264 GLY B CA  1 
ATOM   4867 C  C   . GLY B 1 249 ? -24.978 22.908  25.557  1.00   118.56 ? 264 GLY B C   1 
ATOM   4868 O  O   . GLY B 1 249 ? -25.431 22.663  26.678  1.00   117.47 ? 264 GLY B O   1 
ATOM   4869 N  N   . GLU B 1 250 ? -24.709 21.970  24.650  1.00   119.52 ? 265 GLU B N   1 
ATOM   4870 C  CA  . GLU B 1 250 ? -24.823 20.537  24.932  1.00   119.26 ? 265 GLU B CA  1 
ATOM   4871 C  C   . GLU B 1 250 ? -23.399 19.999  25.185  1.00   117.96 ? 265 GLU B C   1 
ATOM   4872 O  O   . GLU B 1 250 ? -22.649 19.775  24.230  1.00   124.13 ? 265 GLU B O   1 
ATOM   4873 C  CB  . GLU B 1 250 ? -25.477 19.755  23.763  1.00   120.06 ? 265 GLU B CB  1 
ATOM   4874 C  CG  . GLU B 1 250 ? -26.393 20.526  22.807  1.00   125.05 ? 265 GLU B CG  1 
ATOM   4875 C  CD  . GLU B 1 250 ? -27.738 20.917  23.396  1.00   125.77 ? 265 GLU B CD  1 
ATOM   4876 O  OE1 . GLU B 1 250 ? -28.179 20.290  24.383  1.00   126.19 ? 265 GLU B OE1 1 
ATOM   4877 O  OE2 . GLU B 1 250 ? -28.359 21.855  22.853  1.00   125.33 ? 265 GLU B OE2 1 
ATOM   4878 N  N   . PRO B 1 251 ? -23.010 19.800  26.460  1.00   111.75 ? 266 PRO B N   1 
ATOM   4879 C  CA  . PRO B 1 251 ? -21.672 19.259  26.740  1.00   107.67 ? 266 PRO B CA  1 
ATOM   4880 C  C   . PRO B 1 251 ? -21.599 17.730  26.632  1.00   103.70 ? 266 PRO B C   1 
ATOM   4881 O  O   . PRO B 1 251 ? -22.451 17.018  27.175  1.00   101.66 ? 266 PRO B O   1 
ATOM   4882 C  CB  . PRO B 1 251 ? -21.414 19.702  28.178  1.00   108.03 ? 266 PRO B CB  1 
ATOM   4883 C  CG  . PRO B 1 251 ? -22.773 19.781  28.797  1.00   110.38 ? 266 PRO B CG  1 
ATOM   4884 C  CD  . PRO B 1 251 ? -23.770 20.056  27.696  1.00   112.34 ? 266 PRO B CD  1 
ATOM   4885 N  N   . ARG B 1 252 ? -20.556 17.245  25.960  1.00   100.90 ? 267 ARG B N   1 
ATOM   4886 C  CA  . ARG B 1 252 ? -20.422 15.820  25.609  1.00   96.88  ? 267 ARG B CA  1 
ATOM   4887 C  C   . ARG B 1 252 ? -19.590 15.053  26.620  1.00   91.17  ? 267 ARG B C   1 
ATOM   4888 O  O   . ARG B 1 252 ? -19.680 13.828  26.705  1.00   88.14  ? 267 ARG B O   1 
ATOM   4889 C  CB  . ARG B 1 252 ? -19.831 15.647  24.191  1.00   99.68  ? 267 ARG B CB  1 
ATOM   4890 C  CG  . ARG B 1 252 ? -18.624 16.521  23.853  1.00   101.13 ? 267 ARG B CG  1 
ATOM   4891 C  CD  . ARG B 1 252 ? -18.391 16.630  22.355  1.00   103.47 ? 267 ARG B CD  1 
ATOM   4892 N  NE  . ARG B 1 252 ? -17.311 17.569  22.047  1.00   105.43 ? 267 ARG B NE  1 
ATOM   4893 C  CZ  . ARG B 1 252 ? -16.013 17.271  22.068  1.00   107.18 ? 267 ARG B CZ  1 
ATOM   4894 N  NH1 . ARG B 1 252 ? -15.539 16.346  22.897  1.00   108.31 ? 267 ARG B NH1 1 
ATOM   4895 N  NH2 . ARG B 1 252 ? -15.174 17.902  21.259  1.00   108.67 ? 267 ARG B NH2 1 
ATOM   4896 N  N   . ASP B 1 253 ? -18.806 15.784  27.405  1.00   88.53  ? 268 ASP B N   1 
ATOM   4897 C  CA  . ASP B 1 253 ? -17.776 15.198  28.245  1.00   84.50  ? 268 ASP B CA  1 
ATOM   4898 C  C   . ASP B 1 253 ? -17.594 15.979  29.522  1.00   83.19  ? 268 ASP B C   1 
ATOM   4899 O  O   . ASP B 1 253 ? -17.988 17.143  29.616  1.00   82.48  ? 268 ASP B O   1 
ATOM   4900 C  CB  . ASP B 1 253 ? -16.451 15.170  27.476  1.00   84.08  ? 268 ASP B CB  1 
ATOM   4901 C  CG  . ASP B 1 253 ? -16.364 13.997  26.549  1.00   85.45  ? 268 ASP B CG  1 
ATOM   4902 O  OD1 . ASP B 1 253 ? -16.517 12.879  27.077  1.00   88.16  ? 268 ASP B OD1 1 
ATOM   4903 O  OD2 . ASP B 1 253 ? -16.174 14.176  25.318  1.00   82.95  ? 268 ASP B OD2 1 
ATOM   4904 N  N   . LEU B 1 254 ? -16.972 15.327  30.500  1.00   80.69  ? 269 LEU B N   1 
ATOM   4905 C  CA  . LEU B 1 254 ? -16.591 15.990  31.734  1.00   78.87  ? 269 LEU B CA  1 
ATOM   4906 C  C   . LEU B 1 254 ? -15.471 16.959  31.462  1.00   76.65  ? 269 LEU B C   1 
ATOM   4907 O  O   . LEU B 1 254 ? -15.456 18.080  31.959  1.00   73.26  ? 269 LEU B O   1 
ATOM   4908 C  CB  . LEU B 1 254 ? -16.131 14.974  32.764  1.00   79.57  ? 269 LEU B CB  1 
ATOM   4909 C  CG  . LEU B 1 254 ? -16.124 15.587  34.163  1.00   82.58  ? 269 LEU B CG  1 
ATOM   4910 C  CD1 . LEU B 1 254 ? -16.828 14.642  35.113  1.00   83.98  ? 269 LEU B CD1 1 
ATOM   4911 C  CD2 . LEU B 1 254 ? -14.720 15.925  34.649  1.00   82.06  ? 269 LEU B CD2 1 
ATOM   4912 N  N   . LEU B 1 255 ? -14.525 16.503  30.656  1.00   77.70  ? 270 LEU B N   1 
ATOM   4913 C  CA  . LEU B 1 255 ? -13.450 17.351  30.187  1.00   79.35  ? 270 LEU B CA  1 
ATOM   4914 C  C   . LEU B 1 255 ? -14.037 18.613  29.560  1.00   83.03  ? 270 LEU B C   1 
ATOM   4915 O  O   . LEU B 1 255 ? -13.579 19.730  29.820  1.00   85.85  ? 270 LEU B O   1 
ATOM   4916 C  CB  . LEU B 1 255 ? -12.614 16.579  29.175  1.00   78.73  ? 270 LEU B CB  1 
ATOM   4917 C  CG  . LEU B 1 255 ? -11.351 17.220  28.617  1.00   79.33  ? 270 LEU B CG  1 
ATOM   4918 C  CD1 . LEU B 1 255 ? -10.443 17.732  29.738  1.00   78.26  ? 270 LEU B CD1 1 
ATOM   4919 C  CD2 . LEU B 1 255 ? -10.650 16.181  27.747  1.00   78.37  ? 270 LEU B CD2 1 
ATOM   4920 N  N   . ASP B 1 256 ? -15.072 18.415  28.750  1.00   84.93  ? 271 ASP B N   1 
ATOM   4921 C  CA  . ASP B 1 256 ? -15.841 19.515  28.166  1.00   85.86  ? 271 ASP B CA  1 
ATOM   4922 C  C   . ASP B 1 256 ? -16.337 20.453  29.247  1.00   82.30  ? 271 ASP B C   1 
ATOM   4923 O  O   . ASP B 1 256 ? -15.927 21.608  29.316  1.00   80.85  ? 271 ASP B O   1 
ATOM   4924 C  CB  . ASP B 1 256 ? -17.040 18.965  27.378  1.00   87.63  ? 271 ASP B CB  1 
ATOM   4925 C  CG  . ASP B 1 256 ? -17.041 19.401  25.952  1.00   90.20  ? 271 ASP B CG  1 
ATOM   4926 O  OD1 . ASP B 1 256 ? -15.970 19.827  25.468  1.00   90.38  ? 271 ASP B OD1 1 
ATOM   4927 O  OD2 . ASP B 1 256 ? -18.112 19.303  25.315  1.00   94.55  ? 271 ASP B OD2 1 
ATOM   4928 N  N   . ALA B 1 257 ? -17.200 19.932  30.107  1.00   79.70  ? 272 ALA B N   1 
ATOM   4929 C  CA  . ALA B 1 257 ? -17.810 20.740  31.147  1.00   81.00  ? 272 ALA B CA  1 
ATOM   4930 C  C   . ALA B 1 257 ? -16.750 21.540  31.888  1.00   80.31  ? 272 ALA B C   1 
ATOM   4931 O  O   . ALA B 1 257 ? -16.914 22.735  32.132  1.00   82.68  ? 272 ALA B O   1 
ATOM   4932 C  CB  . ALA B 1 257 ? -18.603 19.868  32.116  1.00   79.58  ? 272 ALA B CB  1 
ATOM   4933 N  N   . LEU B 1 258 ? -15.654 20.878  32.231  1.00   77.50  ? 273 LEU B N   1 
ATOM   4934 C  CA  . LEU B 1 258 ? -14.602 21.533  32.962  1.00   76.84  ? 273 LEU B CA  1 
ATOM   4935 C  C   . LEU B 1 258 ? -14.072 22.726  32.192  1.00   79.83  ? 273 LEU B C   1 
ATOM   4936 O  O   . LEU B 1 258 ? -13.935 23.805  32.745  1.00   80.72  ? 273 LEU B O   1 
ATOM   4937 C  CB  . LEU B 1 258 ? -13.498 20.535  33.314  1.00   75.64  ? 273 LEU B CB  1 
ATOM   4938 C  CG  . LEU B 1 258 ? -13.868 19.518  34.417  1.00   73.83  ? 273 LEU B CG  1 
ATOM   4939 C  CD1 . LEU B 1 258 ? -12.703 18.572  34.652  1.00   71.57  ? 273 LEU B CD1 1 
ATOM   4940 C  CD2 . LEU B 1 258 ? -14.278 20.189  35.730  1.00   73.01  ? 273 LEU B CD2 1 
ATOM   4941 N  N   . LEU B 1 259 ? -13.824 22.556  30.904  1.00   83.16  ? 274 LEU B N   1 
ATOM   4942 C  CA  . LEU B 1 259 ? -13.436 23.689  30.073  1.00   87.40  ? 274 LEU B CA  1 
ATOM   4943 C  C   . LEU B 1 259 ? -14.544 24.760  29.985  1.00   91.66  ? 274 LEU B C   1 
ATOM   4944 O  O   . LEU B 1 259 ? -14.263 25.947  30.165  1.00   91.75  ? 274 LEU B O   1 
ATOM   4945 C  CB  . LEU B 1 259 ? -13.009 23.204  28.684  1.00   88.78  ? 274 LEU B CB  1 
ATOM   4946 C  CG  . LEU B 1 259 ? -11.628 22.529  28.706  1.00   86.66  ? 274 LEU B CG  1 
ATOM   4947 C  CD1 . LEU B 1 259 ? -11.467 21.491  27.607  1.00   85.71  ? 274 LEU B CD1 1 
ATOM   4948 C  CD2 . LEU B 1 259 ? -10.540 23.589  28.624  1.00   87.88  ? 274 LEU B CD2 1 
ATOM   4949 N  N   . ILE B 1 260 ? -15.791 24.342  29.743  1.00   95.04  ? 275 ILE B N   1 
ATOM   4950 C  CA  . ILE B 1 260 ? -16.938 25.278  29.671  1.00   99.62  ? 275 ILE B CA  1 
ATOM   4951 C  C   . ILE B 1 260 ? -16.934 26.221  30.868  1.00   102.51 ? 275 ILE B C   1 
ATOM   4952 O  O   . ILE B 1 260 ? -17.018 27.441  30.712  1.00   106.50 ? 275 ILE B O   1 
ATOM   4953 C  CB  . ILE B 1 260 ? -18.325 24.571  29.679  1.00   99.80  ? 275 ILE B CB  1 
ATOM   4954 C  CG1 . ILE B 1 260 ? -18.447 23.494  28.585  1.00   99.08  ? 275 ILE B CG1 1 
ATOM   4955 C  CG2 . ILE B 1 260 ? -19.446 25.602  29.550  1.00   102.38 ? 275 ILE B CG2 1 
ATOM   4956 C  CD1 . ILE B 1 260 ? -17.954 23.914  27.225  1.00   101.31 ? 275 ILE B CD1 1 
ATOM   4957 N  N   . GLY B 1 261 ? -16.864 25.636  32.061  1.00   100.93 ? 276 GLY B N   1 
ATOM   4958 C  CA  . GLY B 1 261 ? -16.757 26.404  33.293  1.00   102.57 ? 276 GLY B CA  1 
ATOM   4959 C  C   . GLY B 1 261 ? -15.457 27.183  33.389  1.00   101.98 ? 276 GLY B C   1 
ATOM   4960 O  O   . GLY B 1 261 ? -15.452 28.347  33.791  1.00   103.71 ? 276 GLY B O   1 
ATOM   4961 N  N   . GLN B 1 262 ? -14.353 26.547  33.013  1.00   99.71  ? 277 GLN B N   1 
ATOM   4962 C  CA  . GLN B 1 262 ? -13.047 27.187  33.086  1.00   100.91 ? 277 GLN B CA  1 
ATOM   4963 C  C   . GLN B 1 262 ? -12.933 28.362  32.110  1.00   104.96 ? 277 GLN B C   1 
ATOM   4964 O  O   . GLN B 1 262 ? -12.163 29.289  32.359  1.00   107.85 ? 277 GLN B O   1 
ATOM   4965 C  CB  . GLN B 1 262 ? -11.946 26.153  32.859  1.00   99.59  ? 277 GLN B CB  1 
ATOM   4966 C  CG  . GLN B 1 262 ? -10.539 26.678  33.060  1.00   100.09 ? 277 GLN B CG  1 
ATOM   4967 C  CD  . GLN B 1 262 ? -9.928  27.191  31.780  1.00   104.91 ? 277 GLN B CD  1 
ATOM   4968 O  OE1 . GLN B 1 262 ? -10.287 26.754  30.680  1.00   107.82 ? 277 GLN B OE1 1 
ATOM   4969 N  NE2 . GLN B 1 262 ? -9.002  28.131  31.910  1.00   106.83 ? 277 GLN B NE2 1 
ATOM   4970 N  N   . GLN B 1 263 ? -13.703 28.326  31.018  1.00   106.83 ? 278 GLN B N   1 
ATOM   4971 C  CA  . GLN B 1 263 ? -13.851 29.475  30.106  1.00   109.96 ? 278 GLN B CA  1 
ATOM   4972 C  C   . GLN B 1 263 ? -14.199 30.751  30.857  1.00   108.61 ? 278 GLN B C   1 
ATOM   4973 O  O   . GLN B 1 263 ? -13.651 31.818  30.589  1.00   111.58 ? 278 GLN B O   1 
ATOM   4974 C  CB  . GLN B 1 263 ? -14.970 29.230  29.076  1.00   114.53 ? 278 GLN B CB  1 
ATOM   4975 C  CG  . GLN B 1 263 ? -14.511 28.943  27.648  1.00   118.23 ? 278 GLN B CG  1 
ATOM   4976 C  CD  . GLN B 1 263 ? -15.637 29.071  26.613  1.00   120.40 ? 278 GLN B CD  1 
ATOM   4977 O  OE1 . GLN B 1 263 ? -16.455 29.994  26.671  1.00   123.23 ? 278 GLN B OE1 1 
ATOM   4978 N  NE2 . GLN B 1 263 ? -15.671 28.151  25.655  1.00   118.85 ? 278 GLN B NE2 1 
ATOM   4979 N  N   . ARG B 1 264 ? -15.106 30.615  31.814  1.00   104.94 ? 279 ARG B N   1 
ATOM   4980 C  CA  . ARG B 1 264 ? -15.782 31.746  32.432  1.00   106.26 ? 279 ARG B CA  1 
ATOM   4981 C  C   . ARG B 1 264 ? -14.890 32.259  33.552  1.00   105.39 ? 279 ARG B C   1 
ATOM   4982 O  O   . ARG B 1 264 ? -15.198 32.142  34.735  1.00   102.28 ? 279 ARG B O   1 
ATOM   4983 C  CB  . ARG B 1 264 ? -17.159 31.307  32.946  1.00   105.77 ? 279 ARG B CB  1 
ATOM   4984 C  CG  . ARG B 1 264 ? -17.768 30.166  32.135  1.00   105.54 ? 279 ARG B CG  1 
ATOM   4985 C  CD  . ARG B 1 264 ? -19.136 29.777  32.635  1.00   106.20 ? 279 ARG B CD  1 
ATOM   4986 N  NE  . ARG B 1 264 ? -20.161 30.666  32.105  1.00   110.66 ? 279 ARG B NE  1 
ATOM   4987 C  CZ  . ARG B 1 264 ? -21.365 30.837  32.642  1.00   113.61 ? 279 ARG B CZ  1 
ATOM   4988 N  NH1 . ARG B 1 264 ? -21.714 30.183  33.751  1.00   112.91 ? 279 ARG B NH1 1 
ATOM   4989 N  NH2 . ARG B 1 264 ? -22.226 31.676  32.068  1.00   118.01 ? 279 ARG B NH2 1 
ATOM   4990 N  N   . GLY B 1 265 ? -13.756 32.819  33.162  1.00   107.03 ? 280 GLY B N   1 
ATOM   4991 C  CA  . GLY B 1 265 ? -12.726 33.152  34.121  1.00   107.24 ? 280 GLY B CA  1 
ATOM   4992 C  C   . GLY B 1 265 ? -11.820 34.245  33.616  1.00   111.29 ? 280 GLY B C   1 
ATOM   4993 O  O   . GLY B 1 265 ? -11.505 34.319  32.423  1.00   109.29 ? 280 GLY B O   1 
ATOM   4994 N  N   . SER B 1 266 ? -11.435 35.116  34.542  1.00   114.90 ? 281 SER B N   1 
ATOM   4995 C  CA  . SER B 1 266 ? -10.382 36.086  34.319  1.00   117.77 ? 281 SER B CA  1 
ATOM   4996 C  C   . SER B 1 266 ? -9.123  35.534  34.997  1.00   116.10 ? 281 SER B C   1 
ATOM   4997 O  O   . SER B 1 266 ? -9.122  34.401  35.495  1.00   110.42 ? 281 SER B O   1 
ATOM   4998 C  CB  . SER B 1 266 ? -10.789 37.436  34.922  1.00   118.73 ? 281 SER B CB  1 
ATOM   4999 O  OG  . SER B 1 266 ? -11.179 37.280  36.278  1.00   113.94 ? 281 SER B OG  1 
ATOM   5000 N  N   . GLY B 1 267 ? -8.046  36.318  34.978  1.00   118.92 ? 282 GLY B N   1 
ATOM   5001 C  CA  . GLY B 1 267 ? -6.924  36.104  35.887  1.00   116.57 ? 282 GLY B CA  1 
ATOM   5002 C  C   . GLY B 1 267 ? -7.355  36.606  37.256  1.00   115.75 ? 282 GLY B C   1 
ATOM   5003 O  O   . GLY B 1 267 ? -7.202  37.790  37.572  1.00   118.29 ? 282 GLY B O   1 
ATOM   5004 N  N   . GLY B 1 268 ? -7.925  35.709  38.058  1.00   110.93 ? 283 GLY B N   1 
ATOM   5005 C  CA  . GLY B 1 268 ? -8.520  36.093  39.333  1.00   109.90 ? 283 GLY B CA  1 
ATOM   5006 C  C   . GLY B 1 268 ? -7.943  35.330  40.501  1.00   105.91 ? 283 GLY B C   1 
ATOM   5007 O  O   . GLY B 1 268 ? -7.136  34.419  40.329  1.00   103.54 ? 283 GLY B O   1 
ATOM   5008 N  N   . ALA B 1 269 ? -8.359  35.705  41.702  1.00   104.57 ? 284 ALA B N   1 
ATOM   5009 C  CA  . ALA B 1 269 ? -7.860  35.054  42.904  1.00   101.76 ? 284 ALA B CA  1 
ATOM   5010 C  C   . ALA B 1 269 ? -8.375  33.619  43.038  1.00   96.95  ? 284 ALA B C   1 
ATOM   5011 O  O   . ALA B 1 269 ? -7.663  32.744  43.514  1.00   93.57  ? 284 ALA B O   1 
ATOM   5012 C  CB  . ALA B 1 269 ? -8.240  35.862  44.131  1.00   103.56 ? 284 ALA B CB  1 
ATOM   5013 N  N   . ASP B 1 270 ? -9.610  33.390  42.604  1.00   96.37  ? 285 ASP B N   1 
ATOM   5014 C  CA  . ASP B 1 270 ? -10.317 32.145  42.887  1.00   92.66  ? 285 ASP B CA  1 
ATOM   5015 C  C   . ASP B 1 270 ? -10.733 31.399  41.614  1.00   91.83  ? 285 ASP B C   1 
ATOM   5016 O  O   . ASP B 1 270 ? -11.583 30.506  41.663  1.00   89.70  ? 285 ASP B O   1 
ATOM   5017 C  CB  . ASP B 1 270 ? -11.562 32.456  43.724  1.00   94.35  ? 285 ASP B CB  1 
ATOM   5018 C  CG  . ASP B 1 270 ? -11.362 33.644  44.674  1.00   97.36  ? 285 ASP B CG  1 
ATOM   5019 O  OD1 . ASP B 1 270 ? -10.286 33.742  45.319  1.00   96.53  ? 285 ASP B OD1 1 
ATOM   5020 O  OD2 . ASP B 1 270 ? -12.298 34.475  44.776  1.00   99.59  ? 285 ASP B OD2 1 
ATOM   5021 N  N   . ASP B 1 271 ? -10.144 31.763  40.475  1.00   92.17  ? 286 ASP B N   1 
ATOM   5022 C  CA  . ASP B 1 271 ? -10.460 31.112  39.202  1.00   90.78  ? 286 ASP B CA  1 
ATOM   5023 C  C   . ASP B 1 271 ? -9.577  29.890  39.020  1.00   88.03  ? 286 ASP B C   1 
ATOM   5024 O  O   . ASP B 1 271 ? -8.387  29.928  39.351  1.00   86.67  ? 286 ASP B O   1 
ATOM   5025 C  CB  . ASP B 1 271 ? -10.263 32.081  38.033  1.00   91.93  ? 286 ASP B CB  1 
ATOM   5026 C  CG  . ASP B 1 271 ? -11.199 33.256  38.101  1.00   93.53  ? 286 ASP B CG  1 
ATOM   5027 O  OD1 . ASP B 1 271 ? -12.329 33.085  38.589  1.00   91.39  ? 286 ASP B OD1 1 
ATOM   5028 O  OD2 . ASP B 1 271 ? -10.813 34.358  37.673  1.00   97.78  ? 286 ASP B OD2 1 
ATOM   5029 N  N   . ILE B 1 272 ? -10.151 28.806  38.502  1.00   85.47  ? 287 ILE B N   1 
ATOM   5030 C  CA  . ILE B 1 272 ? -9.367  27.594  38.281  1.00   82.80  ? 287 ILE B CA  1 
ATOM   5031 C  C   . ILE B 1 272 ? -8.591  27.655  36.968  1.00   82.70  ? 287 ILE B C   1 
ATOM   5032 O  O   . ILE B 1 272 ? -9.159  27.864  35.897  1.00   86.37  ? 287 ILE B O   1 
ATOM   5033 C  CB  . ILE B 1 272 ? -10.183 26.283  38.398  1.00   80.75  ? 287 ILE B CB  1 
ATOM   5034 C  CG1 . ILE B 1 272 ? -11.374 26.237  37.460  1.00   81.70  ? 287 ILE B CG1 1 
ATOM   5035 C  CG2 . ILE B 1 272 ? -10.668 26.096  39.822  1.00   80.30  ? 287 ILE B CG2 1 
ATOM   5036 C  CD1 . ILE B 1 272 ? -12.006 24.870  37.417  1.00   80.58  ? 287 ILE B CD1 1 
ATOM   5037 N  N   . THR B 1 273 ? -7.273  27.513  37.088  1.00   79.49  ? 288 THR B N   1 
ATOM   5038 C  CA  . THR B 1 273 ? -6.383  27.347  35.955  1.00   78.00  ? 288 THR B CA  1 
ATOM   5039 C  C   . THR B 1 273 ? -6.701  26.033  35.190  1.00   75.86  ? 288 THR B C   1 
ATOM   5040 O  O   . THR B 1 273 ? -7.642  25.309  35.529  1.00   74.13  ? 288 THR B O   1 
ATOM   5041 C  CB  . THR B 1 273 ? -4.898  27.483  36.414  1.00   77.50  ? 288 THR B CB  1 
ATOM   5042 O  OG1 . THR B 1 273 ? -4.052  27.747  35.296  1.00   83.77  ? 288 THR B OG1 1 
ATOM   5043 C  CG2 . THR B 1 273 ? -4.385  26.261  37.119  1.00   75.75  ? 288 THR B CG2 1 
ATOM   5044 N  N   . GLU B 1 274 ? -5.956  25.768  34.123  1.00   76.02  ? 289 GLU B N   1 
ATOM   5045 C  CA  . GLU B 1 274 ? -6.154  24.557  33.328  1.00   74.40  ? 289 GLU B CA  1 
ATOM   5046 C  C   . GLU B 1 274 ? -5.481  23.336  33.967  1.00   70.15  ? 289 GLU B C   1 
ATOM   5047 O  O   . GLU B 1 274 ? -5.836  22.190  33.665  1.00   68.55  ? 289 GLU B O   1 
ATOM   5048 C  CB  . GLU B 1 274 ? -5.617  24.762  31.914  1.00   76.28  ? 289 GLU B CB  1 
ATOM   5049 C  CG  . GLU B 1 274 ? -6.566  25.513  31.000  1.00   78.76  ? 289 GLU B CG  1 
ATOM   5050 C  CD  . GLU B 1 274 ? -6.057  25.595  29.566  1.00   80.64  ? 289 GLU B CD  1 
ATOM   5051 O  OE1 . GLU B 1 274 ? -4.824  25.517  29.352  1.00   80.23  ? 289 GLU B OE1 1 
ATOM   5052 O  OE2 . GLU B 1 274 ? -6.892  25.734  28.651  1.00   80.60  ? 289 GLU B OE2 1 
ATOM   5053 N  N   . ASP B 1 275 ? -4.489  23.589  34.815  1.00   67.64  ? 290 ASP B N   1 
ATOM   5054 C  CA  . ASP B 1 275 ? -3.892  22.540  35.624  1.00   65.57  ? 290 ASP B CA  1 
ATOM   5055 C  C   . ASP B 1 275 ? -4.990  21.828  36.445  1.00   64.57  ? 290 ASP B C   1 
ATOM   5056 O  O   . ASP B 1 275 ? -4.957  20.603  36.556  1.00   63.77  ? 290 ASP B O   1 
ATOM   5057 C  CB  . ASP B 1 275 ? -2.811  23.102  36.560  1.00   65.06  ? 290 ASP B CB  1 
ATOM   5058 C  CG  . ASP B 1 275 ? -1.579  23.681  35.824  1.00   67.52  ? 290 ASP B CG  1 
ATOM   5059 O  OD1 . ASP B 1 275 ? -1.137  23.165  34.757  1.00   69.95  ? 290 ASP B OD1 1 
ATOM   5060 O  OD2 . ASP B 1 275 ? -1.002  24.647  36.366  1.00   67.71  ? 290 ASP B OD2 1 
ATOM   5061 N  N   . HIS B 1 276 ? -5.960  22.583  36.984  1.00   64.21  ? 291 HIS B N   1 
ATOM   5062 C  CA  . HIS B 1 276 ? -7.087  22.021  37.751  1.00   64.17  ? 291 HIS B CA  1 
ATOM   5063 C  C   . HIS B 1 276 ? -8.050  21.170  36.949  1.00   64.55  ? 291 HIS B C   1 
ATOM   5064 O  O   . HIS B 1 276 ? -8.705  20.268  37.472  1.00   63.53  ? 291 HIS B O   1 
ATOM   5065 C  CB  . HIS B 1 276 ? -7.932  23.130  38.340  1.00   67.05  ? 291 HIS B CB  1 
ATOM   5066 C  CG  . HIS B 1 276 ? -7.239  23.930  39.388  1.00   68.84  ? 291 HIS B CG  1 
ATOM   5067 N  ND1 . HIS B 1 276 ? -6.589  25.109  39.103  1.00   70.36  ? 291 HIS B ND1 1 
ATOM   5068 C  CD2 . HIS B 1 276 ? -7.100  23.732  40.721  1.00   68.19  ? 291 HIS B CD2 1 
ATOM   5069 C  CE1 . HIS B 1 276 ? -6.079  25.606  40.216  1.00   71.62  ? 291 HIS B CE1 1 
ATOM   5070 N  NE2 . HIS B 1 276 ? -6.379  24.792  41.214  1.00   69.40  ? 291 HIS B NE2 1 
ATOM   5071 N  N   . VAL B 1 277 ? -8.174  21.509  35.681  1.00   66.59  ? 292 VAL B N   1 
ATOM   5072 C  CA  . VAL B 1 277 ? -9.002  20.767  34.756  1.00   66.85  ? 292 VAL B CA  1 
ATOM   5073 C  C   . VAL B 1 277 ? -8.386  19.395  34.550  1.00   63.06  ? 292 VAL B C   1 
ATOM   5074 O  O   . VAL B 1 277 ? -9.046  18.364  34.669  1.00   62.74  ? 292 VAL B O   1 
ATOM   5075 C  CB  . VAL B 1 277 ? -9.047  21.483  33.393  1.00   71.03  ? 292 VAL B CB  1 
ATOM   5076 C  CG1 . VAL B 1 277 ? -9.869  20.671  32.394  1.00   72.77  ? 292 VAL B CG1 1 
ATOM   5077 C  CG2 . VAL B 1 277 ? -9.580  22.912  33.540  1.00   72.93  ? 292 VAL B CG2 1 
ATOM   5078 N  N   . LEU B 1 278 ? -7.099  19.415  34.243  1.00   60.47  ? 293 LEU B N   1 
ATOM   5079 C  CA  . LEU B 1 278 ? -6.337  18.220  33.996  1.00   58.19  ? 293 LEU B CA  1 
ATOM   5080 C  C   . LEU B 1 278 ? -6.251  17.313  35.218  1.00   56.25  ? 293 LEU B C   1 
ATOM   5081 O  O   . LEU B 1 278 ? -6.502  16.108  35.105  1.00   55.19  ? 293 LEU B O   1 
ATOM   5082 C  CB  . LEU B 1 278 ? -4.942  18.637  33.579  1.00   58.88  ? 293 LEU B CB  1 
ATOM   5083 C  CG  . LEU B 1 278 ? -4.018  17.541  33.087  1.00   58.38  ? 293 LEU B CG  1 
ATOM   5084 C  CD1 . LEU B 1 278 ? -4.623  16.821  31.894  1.00   59.41  ? 293 LEU B CD1 1 
ATOM   5085 C  CD2 . LEU B 1 278 ? -2.706  18.196  32.715  1.00   59.71  ? 293 LEU B CD2 1 
ATOM   5086 N  N   . MET B 1 279 ? -5.887  17.895  36.372  1.00   55.40  ? 294 MET B N   1 
ATOM   5087 C  CA  . MET B 1 279 ? -5.822  17.170  37.668  1.00   53.75  ? 294 MET B CA  1 
ATOM   5088 C  C   . MET B 1 279 ? -7.143  16.567  38.107  1.00   52.48  ? 294 MET B C   1 
ATOM   5089 O  O   . MET B 1 279 ? -7.159  15.507  38.732  1.00   49.80  ? 294 MET B O   1 
ATOM   5090 C  CB  . MET B 1 279 ? -5.319  18.081  38.799  1.00   53.62  ? 294 MET B CB  1 
ATOM   5091 C  CG  . MET B 1 279 ? -3.884  18.540  38.640  1.00   53.32  ? 294 MET B CG  1 
ATOM   5092 S  SD  . MET B 1 279 ? -2.785  17.190  38.205  1.00   51.77  ? 294 MET B SD  1 
ATOM   5093 C  CE  . MET B 1 279 ? -2.844  17.181  36.418  1.00   53.92  ? 294 MET B CE  1 
ATOM   5094 N  N   . THR B 1 280 ? -8.238  17.240  37.779  1.00   54.07  ? 295 THR B N   1 
ATOM   5095 C  CA  . THR B 1 280 ? -9.567  16.692  38.037  1.00   55.37  ? 295 THR B CA  1 
ATOM   5096 C  C   . THR B 1 280 ? -9.899  15.555  37.058  1.00   54.48  ? 295 THR B C   1 
ATOM   5097 O  O   . THR B 1 280 ? -10.474 14.525  37.440  1.00   51.28  ? 295 THR B O   1 
ATOM   5098 C  CB  . THR B 1 280 ? -10.644 17.799  37.989  1.00   58.13  ? 295 THR B CB  1 
ATOM   5099 O  OG1 . THR B 1 280 ? -10.182 18.955  38.709  1.00   59.05  ? 295 THR B OG1 1 
ATOM   5100 C  CG2 . THR B 1 280 ? -11.953 17.310  38.629  1.00   58.47  ? 295 THR B CG2 1 
ATOM   5101 N  N   . ALA B 1 281 ? -9.525  15.744  35.799  1.00   56.11  ? 296 ALA B N   1 
ATOM   5102 C  CA  . ALA B 1 281 ? -9.675  14.688  34.791  1.00   57.20  ? 296 ALA B CA  1 
ATOM   5103 C  C   . ALA B 1 281 ? -8.931  13.437  35.244  1.00   55.10  ? 296 ALA B C   1 
ATOM   5104 O  O   . ALA B 1 281 ? -9.464  12.326  35.171  1.00   55.19  ? 296 ALA B O   1 
ATOM   5105 C  CB  . ALA B 1 281 ? -9.164  15.149  33.425  1.00   58.18  ? 296 ALA B CB  1 
ATOM   5106 N  N   . ALA B 1 282 ? -7.704  13.625  35.705  1.00   53.55  ? 297 ALA B N   1 
ATOM   5107 C  CA  . ALA B 1 282 ? -6.945  12.530  36.279  1.00   53.48  ? 297 ALA B CA  1 
ATOM   5108 C  C   . ALA B 1 282 ? -7.652  11.920  37.508  1.00   52.76  ? 297 ALA B C   1 
ATOM   5109 O  O   . ALA B 1 282 ? -7.833  10.709  37.596  1.00   52.11  ? 297 ALA B O   1 
ATOM   5110 C  CB  . ALA B 1 282 ? -5.554  13.009  36.659  1.00   53.27  ? 297 ALA B CB  1 
ATOM   5111 N  N   . GLU B 1 283 ? -8.069  12.757  38.449  1.00   53.03  ? 298 GLU B N   1 
ATOM   5112 C  CA  . GLU B 1 283 ? -8.712  12.254  39.675  1.00   53.89  ? 298 GLU B CA  1 
ATOM   5113 C  C   . GLU B 1 283 ? -9.958  11.379  39.478  1.00   55.51  ? 298 GLU B C   1 
ATOM   5114 O  O   . GLU B 1 283 ? -10.352 10.635  40.395  1.00   53.96  ? 298 GLU B O   1 
ATOM   5115 C  CB  . GLU B 1 283 ? -9.125  13.414  40.555  1.00   53.49  ? 298 GLU B CB  1 
ATOM   5116 C  CG  . GLU B 1 283 ? -9.366  13.030  41.996  1.00   51.51  ? 298 GLU B CG  1 
ATOM   5117 C  CD  . GLU B 1 283 ? -8.811  14.089  42.901  1.00   51.26  ? 298 GLU B CD  1 
ATOM   5118 O  OE1 . GLU B 1 283 ? -9.269  15.249  42.799  1.00   53.13  ? 298 GLU B OE1 1 
ATOM   5119 O  OE2 . GLU B 1 283 ? -7.890  13.777  43.670  1.00   48.88  ? 298 GLU B OE2 1 
ATOM   5120 N  N   . ALA B 1 284 ? -10.590 11.509  38.310  1.00   55.90  ? 299 ALA B N   1 
ATOM   5121 C  CA  . ALA B 1 284 ? -11.764 10.737  37.988  1.00   56.50  ? 299 ALA B CA  1 
ATOM   5122 C  C   . ALA B 1 284 ? -11.380 9.294   37.748  1.00   55.39  ? 299 ALA B C   1 
ATOM   5123 O  O   . ALA B 1 284 ? -12.198 8.392   37.900  1.00   54.65  ? 299 ALA B O   1 
ATOM   5124 C  CB  . ALA B 1 284 ? -12.447 11.320  36.761  1.00   59.19  ? 299 ALA B CB  1 
ATOM   5125 N  N   . PHE B 1 285 ? -10.145 9.068   37.338  1.00   55.72  ? 300 PHE B N   1 
ATOM   5126 C  CA  . PHE B 1 285 ? -9.644  7.708   37.297  1.00   57.85  ? 300 PHE B CA  1 
ATOM   5127 C  C   . PHE B 1 285 ? -9.106  7.306   38.662  1.00   57.14  ? 300 PHE B C   1 
ATOM   5128 O  O   . PHE B 1 285 ? -9.476  6.263   39.200  1.00   57.68  ? 300 PHE B O   1 
ATOM   5129 C  CB  . PHE B 1 285 ? -8.559  7.558   36.246  1.00   59.35  ? 300 PHE B CB  1 
ATOM   5130 C  CG  . PHE B 1 285 ? -9.073  7.657   34.857  1.00   61.34  ? 300 PHE B CG  1 
ATOM   5131 C  CD1 . PHE B 1 285 ? -9.644  6.551   34.248  1.00   62.01  ? 300 PHE B CD1 1 
ATOM   5132 C  CD2 . PHE B 1 285 ? -9.002  8.853   34.165  1.00   62.88  ? 300 PHE B CD2 1 
ATOM   5133 C  CE1 . PHE B 1 285 ? -10.135 6.636   32.965  1.00   63.11  ? 300 PHE B CE1 1 
ATOM   5134 C  CE2 . PHE B 1 285 ? -9.497  8.949   32.889  1.00   63.91  ? 300 PHE B CE2 1 
ATOM   5135 C  CZ  . PHE B 1 285 ? -10.065 7.839   32.288  1.00   64.59  ? 300 PHE B CZ  1 
ATOM   5136 N  N   . GLY B 1 286 ? -8.230  8.142   39.211  1.00   56.90  ? 301 GLY B N   1 
ATOM   5137 C  CA  . GLY B 1 286 ? -7.648  7.902   40.526  1.00   55.79  ? 301 GLY B CA  1 
ATOM   5138 C  C   . GLY B 1 286 ? -8.700  7.491   41.525  1.00   54.15  ? 301 GLY B C   1 
ATOM   5139 O  O   . GLY B 1 286 ? -8.691  6.359   42.001  1.00   54.26  ? 301 GLY B O   1 
ATOM   5140 N  N   . ALA B 1 287 ? -9.633  8.400   41.794  1.00   53.03  ? 302 ALA B N   1 
ATOM   5141 C  CA  . ALA B 1 287 ? -10.678 8.164   42.795  1.00   52.86  ? 302 ALA B CA  1 
ATOM   5142 C  C   . ALA B 1 287 ? -11.843 7.313   42.312  1.00   53.14  ? 302 ALA B C   1 
ATOM   5143 O  O   . ALA B 1 287 ? -12.630 6.859   43.138  1.00   56.32  ? 302 ALA B O   1 
ATOM   5144 C  CB  . ALA B 1 287 ? -11.216 9.490   43.321  1.00   52.23  ? 302 ALA B CB  1 
ATOM   5145 N  N   . GLY B 1 288 ? -11.979 7.106   41.004  1.00   50.86  ? 303 GLY B N   1 
ATOM   5146 C  CA  . GLY B 1 288 ? -13.186 6.480   40.467  1.00   50.63  ? 303 GLY B CA  1 
ATOM   5147 C  C   . GLY B 1 288 ? -13.043 5.004   40.201  1.00   50.03  ? 303 GLY B C   1 
ATOM   5148 O  O   . GLY B 1 288 ? -13.870 4.207   40.594  1.00   49.75  ? 303 GLY B O   1 
ATOM   5149 N  N   . VAL B 1 289 ? -11.984 4.647   39.496  1.00   51.65  ? 304 VAL B N   1 
ATOM   5150 C  CA  . VAL B 1 289 ? -11.680 3.257   39.209  1.00   50.81  ? 304 VAL B CA  1 
ATOM   5151 C  C   . VAL B 1 289 ? -11.209 2.781   40.536  1.00   50.23  ? 304 VAL B C   1 
ATOM   5152 O  O   . VAL B 1 289 ? -10.703 3.575   41.326  1.00   54.23  ? 304 VAL B O   1 
ATOM   5153 C  CB  . VAL B 1 289 ? -10.539 3.125   38.170  1.00   49.68  ? 304 VAL B CB  1 
ATOM   5154 C  CG1 . VAL B 1 289 ? -10.240 1.670   37.870  1.00   49.75  ? 304 VAL B CG1 1 
ATOM   5155 C  CG2 . VAL B 1 289 ? -10.887 3.852   36.877  1.00   50.90  ? 304 VAL B CG2 1 
ATOM   5156 N  N   . GLU B 1 290 ? -11.361 1.509   40.820  1.00   49.29  ? 305 GLU B N   1 
ATOM   5157 C  CA  . GLU B 1 290 ? -10.785 0.990   42.059  1.00   48.56  ? 305 GLU B CA  1 
ATOM   5158 C  C   . GLU B 1 290 ? -11.798 1.033   43.194  1.00   44.47  ? 305 GLU B C   1 
ATOM   5159 O  O   . GLU B 1 290 ? -12.128 0.005   43.754  1.00   41.50  ? 305 GLU B O   1 
ATOM   5160 C  CB  . GLU B 1 290 ? -9.502  1.741   42.451  1.00   49.90  ? 305 GLU B CB  1 
ATOM   5161 C  CG  . GLU B 1 290 ? -8.505  0.842   43.141  1.00   52.15  ? 305 GLU B CG  1 
ATOM   5162 C  CD  . GLU B 1 290 ? -7.603  0.159   42.175  1.00   52.64  ? 305 GLU B CD  1 
ATOM   5163 O  OE1 . GLU B 1 290 ? -7.394  0.747   41.109  1.00   56.08  ? 305 GLU B OE1 1 
ATOM   5164 O  OE2 . GLU B 1 290 ? -7.090  -0.936  42.492  1.00   56.54  ? 305 GLU B OE2 1 
ATOM   5165 N  N   . THR B 1 291 ? -12.321 2.208   43.502  1.00   43.28  ? 306 THR B N   1 
ATOM   5166 C  CA  . THR B 1 291 ? -13.484 2.300   44.389  1.00   43.74  ? 306 THR B CA  1 
ATOM   5167 C  C   . THR B 1 291 ? -14.670 1.472   43.859  1.00   44.73  ? 306 THR B C   1 
ATOM   5168 O  O   . THR B 1 291 ? -15.290 0.672   44.571  1.00   44.93  ? 306 THR B O   1 
ATOM   5169 C  CB  . THR B 1 291 ? -13.928 3.758   44.521  1.00   44.37  ? 306 THR B CB  1 
ATOM   5170 O  OG1 . THR B 1 291 ? -13.608 4.434   43.302  1.00   44.60  ? 306 THR B OG1 1 
ATOM   5171 C  CG2 . THR B 1 291 ? -13.206 4.450   45.691  1.00   43.40  ? 306 THR B CG2 1 
ATOM   5172 N  N   . THR B 1 292 ? -14.968 1.655   42.588  1.00   45.08  ? 307 THR B N   1 
ATOM   5173 C  CA  . THR B 1 292 ? -16.110 1.010   41.997  1.00   46.81  ? 307 THR B CA  1 
ATOM   5174 C  C   . THR B 1 292 ? -15.763 -0.451  41.663  1.00   46.60  ? 307 THR B C   1 
ATOM   5175 O  O   . THR B 1 292 ? -16.559 -1.369  41.937  1.00   48.05  ? 307 THR B O   1 
ATOM   5176 C  CB  . THR B 1 292 ? -16.578 1.780   40.754  1.00   48.10  ? 307 THR B CB  1 
ATOM   5177 O  OG1 . THR B 1 292 ? -15.545 1.730   39.760  1.00   54.42  ? 307 THR B OG1 1 
ATOM   5178 C  CG2 . THR B 1 292 ? -16.844 3.220   41.089  1.00   47.18  ? 307 THR B CG2 1 
ATOM   5179 N  N   . SER B 1 293 ? -14.583 -0.667  41.081  1.00   44.72  ? 308 SER B N   1 
ATOM   5180 C  CA  . SER B 1 293 ? -14.145 -2.008  40.709  1.00   44.17  ? 308 SER B CA  1 
ATOM   5181 C  C   . SER B 1 293 ? -14.153 -2.834  41.968  1.00   42.26  ? 308 SER B C   1 
ATOM   5182 O  O   . SER B 1 293 ? -14.692 -3.931  42.021  1.00   41.60  ? 308 SER B O   1 
ATOM   5183 C  CB  . SER B 1 293 ? -12.727 -1.967  40.126  1.00   44.38  ? 308 SER B CB  1 
ATOM   5184 O  OG  . SER B 1 293 ? -12.394 -0.639  39.717  1.00   44.96  ? 308 SER B OG  1 
ATOM   5185 N  N   . THR B 1 294 ? -13.570 -2.259  43.004  1.00   40.94  ? 309 THR B N   1 
ATOM   5186 C  CA  . THR B 1 294 ? -13.437 -2.950  44.277  1.00   40.41  ? 309 THR B CA  1 
ATOM   5187 C  C   . THR B 1 294 ? -14.786 -3.263  44.869  1.00   39.39  ? 309 THR B C   1 
ATOM   5188 O  O   . THR B 1 294 ? -15.022 -4.397  45.310  1.00   37.66  ? 309 THR B O   1 
ATOM   5189 C  CB  . THR B 1 294 ? -12.552 -2.152  45.267  1.00   39.77  ? 309 THR B CB  1 
ATOM   5190 O  OG1 . THR B 1 294 ? -11.231 -2.005  44.692  1.00   41.09  ? 309 THR B OG1 1 
ATOM   5191 C  CG2 . THR B 1 294 ? -12.432 -2.867  46.609  1.00   39.10  ? 309 THR B CG2 1 
ATOM   5192 N  N   . THR B 1 295 ? -15.659 -2.264  44.863  1.00   39.87  ? 310 THR B N   1 
ATOM   5193 C  CA  . THR B 1 295 ? -17.008 -2.452  45.354  1.00   42.36  ? 310 THR B CA  1 
ATOM   5194 C  C   . THR B 1 295 ? -17.739 -3.538  44.554  1.00   43.83  ? 310 THR B C   1 
ATOM   5195 O  O   . THR B 1 295 ? -18.468 -4.369  45.114  1.00   45.92  ? 310 THR B O   1 
ATOM   5196 C  CB  . THR B 1 295 ? -17.798 -1.155  45.249  1.00   44.19  ? 310 THR B CB  1 
ATOM   5197 O  OG1 . THR B 1 295 ? -17.084 -0.120  45.930  1.00   44.23  ? 310 THR B OG1 1 
ATOM   5198 C  CG2 . THR B 1 295 ? -19.214 -1.322  45.857  1.00   46.07  ? 310 THR B CG2 1 
ATOM   5199 N  N   . LEU B 1 296 ? -17.529 -3.528  43.246  1.00   43.20  ? 311 LEU B N   1 
ATOM   5200 C  CA  . LEU B 1 296 ? -18.090 -4.536  42.397  1.00   44.23  ? 311 LEU B CA  1 
ATOM   5201 C  C   . LEU B 1 296 ? -17.555 -5.908  42.739  1.00   43.76  ? 311 LEU B C   1 
ATOM   5202 O  O   . LEU B 1 296 ? -18.321 -6.864  42.809  1.00   45.33  ? 311 LEU B O   1 
ATOM   5203 C  CB  . LEU B 1 296 ? -17.847 -4.192  40.920  1.00   44.76  ? 311 LEU B CB  1 
ATOM   5204 C  CG  . LEU B 1 296 ? -18.703 -3.014  40.434  1.00   45.69  ? 311 LEU B CG  1 
ATOM   5205 C  CD1 . LEU B 1 296 ? -18.266 -2.558  39.058  1.00   46.73  ? 311 LEU B CD1 1 
ATOM   5206 C  CD2 . LEU B 1 296 ? -20.185 -3.363  40.410  1.00   47.07  ? 311 LEU B CD2 1 
ATOM   5207 N  N   . LEU B 1 297 ? -16.247 -6.010  42.937  1.00   42.44  ? 312 LEU B N   1 
ATOM   5208 C  CA  . LEU B 1 297 ? -15.643 -7.261  43.387  1.00   41.79  ? 312 LEU B CA  1 
ATOM   5209 C  C   . LEU B 1 297 ? -16.164 -7.704  44.755  1.00   41.09  ? 312 LEU B C   1 
ATOM   5210 O  O   . LEU B 1 297 ? -16.513 -8.855  44.918  1.00   41.38  ? 312 LEU B O   1 
ATOM   5211 C  CB  . LEU B 1 297 ? -14.134 -7.137  43.444  1.00   41.40  ? 312 LEU B CB  1 
ATOM   5212 C  CG  . LEU B 1 297 ? -13.366 -7.373  42.165  1.00   42.16  ? 312 LEU B CG  1 
ATOM   5213 C  CD1 . LEU B 1 297 ? -12.189 -6.420  42.044  1.00   41.46  ? 312 LEU B CD1 1 
ATOM   5214 C  CD2 . LEU B 1 297 ? -12.918 -8.823  42.140  1.00   43.24  ? 312 LEU B CD2 1 
ATOM   5215 N  N   . TRP B 1 298 ? -16.209 -6.820  45.739  1.00   40.29  ? 313 TRP B N   1 
ATOM   5216 C  CA  . TRP B 1 298 ? -16.808 -7.209  47.042  1.00   41.73  ? 313 TRP B CA  1 
ATOM   5217 C  C   . TRP B 1 298 ? -18.223 -7.786  46.898  1.00   43.25  ? 313 TRP B C   1 
ATOM   5218 O  O   . TRP B 1 298 ? -18.532 -8.863  47.430  1.00   43.97  ? 313 TRP B O   1 
ATOM   5219 C  CB  . TRP B 1 298 ? -16.888 -6.038  48.027  1.00   40.90  ? 313 TRP B CB  1 
ATOM   5220 C  CG  . TRP B 1 298 ? -15.610 -5.724  48.740  1.00   39.96  ? 313 TRP B CG  1 
ATOM   5221 C  CD1 . TRP B 1 298 ? -14.957 -4.525  48.745  1.00   38.80  ? 313 TRP B CD1 1 
ATOM   5222 C  CD2 . TRP B 1 298 ? -14.835 -6.608  49.561  1.00   39.88  ? 313 TRP B CD2 1 
ATOM   5223 N  NE1 . TRP B 1 298 ? -13.838 -4.605  49.519  1.00   38.46  ? 313 TRP B NE1 1 
ATOM   5224 C  CE2 . TRP B 1 298 ? -13.737 -5.871  50.041  1.00   39.48  ? 313 TRP B CE2 1 
ATOM   5225 C  CE3 . TRP B 1 298 ? -14.964 -7.946  49.941  1.00   41.22  ? 313 TRP B CE3 1 
ATOM   5226 C  CZ2 . TRP B 1 298 ? -12.744 -6.440  50.885  1.00   39.71  ? 313 TRP B CZ2 1 
ATOM   5227 C  CZ3 . TRP B 1 298 ? -13.982 -8.510  50.797  1.00   41.46  ? 313 TRP B CZ3 1 
ATOM   5228 C  CH2 . TRP B 1 298 ? -12.890 -7.755  51.245  1.00   40.34  ? 313 TRP B CH2 1 
ATOM   5229 N  N   . THR B 1 299 ? -19.082 -7.069  46.187  1.00   43.50  ? 314 THR B N   1 
ATOM   5230 C  CA  . THR B 1 299 ? -20.443 -7.545  45.996  1.00   46.01  ? 314 THR B CA  1 
ATOM   5231 C  C   . THR B 1 299 ? -20.486 -9.004  45.560  1.00   47.42  ? 314 THR B C   1 
ATOM   5232 O  O   . THR B 1 299 ? -21.110 -9.839  46.198  1.00   48.43  ? 314 THR B O   1 
ATOM   5233 C  CB  . THR B 1 299 ? -21.206 -6.715  44.950  1.00   46.78  ? 314 THR B CB  1 
ATOM   5234 O  OG1 . THR B 1 299 ? -21.074 -5.313  45.241  1.00   45.87  ? 314 THR B OG1 1 
ATOM   5235 C  CG2 . THR B 1 299 ? -22.685 -7.112  44.953  1.00   48.23  ? 314 THR B CG2 1 
ATOM   5236 N  N   . ILE B 1 300 ? -19.796 -9.303  44.474  1.00   48.21  ? 315 ILE B N   1 
ATOM   5237 C  CA  . ILE B 1 300 ? -19.782 -10.648 43.942  1.00   49.80  ? 315 ILE B CA  1 
ATOM   5238 C  C   . ILE B 1 300 ? -19.155 -11.623 44.919  1.00   49.62  ? 315 ILE B C   1 
ATOM   5239 O  O   . ILE B 1 300 ? -19.649 -12.737 45.087  1.00   51.44  ? 315 ILE B O   1 
ATOM   5240 C  CB  . ILE B 1 300 ? -19.087 -10.689 42.575  1.00   50.78  ? 315 ILE B CB  1 
ATOM   5241 C  CG1 . ILE B 1 300 ? -20.033 -10.084 41.527  1.00   52.63  ? 315 ILE B CG1 1 
ATOM   5242 C  CG2 . ILE B 1 300 ? -18.725 -12.117 42.192  1.00   51.51  ? 315 ILE B CG2 1 
ATOM   5243 C  CD1 . ILE B 1 300 ? -19.369 -9.743  40.208  1.00   53.38  ? 315 ILE B CD1 1 
ATOM   5244 N  N   . ALA B 1 301 ? -18.092 -11.204 45.590  1.00   48.20  ? 316 ALA B N   1 
ATOM   5245 C  CA  . ALA B 1 301 ? -17.471 -12.055 46.597  1.00   47.88  ? 316 ALA B CA  1 
ATOM   5246 C  C   . ALA B 1 301 ? -18.498 -12.464 47.632  1.00   49.21  ? 316 ALA B C   1 
ATOM   5247 O  O   . ALA B 1 301 ? -18.508 -13.619 48.034  1.00   49.59  ? 316 ALA B O   1 
ATOM   5248 C  CB  . ALA B 1 301 ? -16.289 -11.361 47.262  1.00   46.30  ? 316 ALA B CB  1 
ATOM   5249 N  N   . PHE B 1 302 ? -19.362 -11.534 48.057  1.00   50.13  ? 317 PHE B N   1 
ATOM   5250 C  CA  . PHE B 1 302 ? -20.380 -11.854 49.076  1.00   51.75  ? 317 PHE B CA  1 
ATOM   5251 C  C   . PHE B 1 302 ? -21.517 -12.699 48.478  1.00   53.95  ? 317 PHE B C   1 
ATOM   5252 O  O   . PHE B 1 302 ? -22.071 -13.603 49.122  1.00   54.99  ? 317 PHE B O   1 
ATOM   5253 C  CB  . PHE B 1 302 ? -20.921 -10.590 49.758  1.00   51.01  ? 317 PHE B CB  1 
ATOM   5254 C  CG  . PHE B 1 302 ? -20.020 -10.057 50.815  1.00   50.32  ? 317 PHE B CG  1 
ATOM   5255 C  CD1 . PHE B 1 302 ? -19.886 -10.722 52.025  1.00   50.85  ? 317 PHE B CD1 1 
ATOM   5256 C  CD2 . PHE B 1 302 ? -19.273 -8.905  50.605  1.00   50.19  ? 317 PHE B CD2 1 
ATOM   5257 C  CE1 . PHE B 1 302 ? -19.031 -10.250 53.004  1.00   49.14  ? 317 PHE B CE1 1 
ATOM   5258 C  CE2 . PHE B 1 302 ? -18.410 -8.428  51.588  1.00   48.18  ? 317 PHE B CE2 1 
ATOM   5259 C  CZ  . PHE B 1 302 ? -18.300 -9.101  52.786  1.00   47.97  ? 317 PHE B CZ  1 
ATOM   5260 N  N   . LEU B 1 303 ? -21.852 -12.443 47.229  1.00   54.95  ? 318 LEU B N   1 
ATOM   5261 C  CA  . LEU B 1 303 ? -22.922 -13.222 46.631  1.00   57.17  ? 318 LEU B CA  1 
ATOM   5262 C  C   . LEU B 1 303 ? -22.454 -14.639 46.340  1.00   58.29  ? 318 LEU B C   1 
ATOM   5263 O  O   . LEU B 1 303 ? -23.290 -15.539 46.262  1.00   61.91  ? 318 LEU B O   1 
ATOM   5264 C  CB  . LEU B 1 303 ? -23.511 -12.524 45.409  1.00   56.95  ? 318 LEU B CB  1 
ATOM   5265 C  CG  . LEU B 1 303 ? -24.288 -11.251 45.787  1.00   57.48  ? 318 LEU B CG  1 
ATOM   5266 C  CD1 . LEU B 1 303 ? -24.786 -10.530 44.550  1.00   58.89  ? 318 LEU B CD1 1 
ATOM   5267 C  CD2 . LEU B 1 303 ? -25.466 -11.527 46.707  1.00   58.89  ? 318 LEU B CD2 1 
ATOM   5268 N  N   . LEU B 1 304 ? -21.141 -14.849 46.216  1.00   55.79  ? 319 LEU B N   1 
ATOM   5269 C  CA  . LEU B 1 304 ? -20.613 -16.203 46.139  1.00   56.60  ? 319 LEU B CA  1 
ATOM   5270 C  C   . LEU B 1 304 ? -20.853 -16.944 47.444  1.00   57.55  ? 319 LEU B C   1 
ATOM   5271 O  O   . LEU B 1 304 ? -21.242 -18.121 47.411  1.00   59.52  ? 319 LEU B O   1 
ATOM   5272 C  CB  . LEU B 1 304 ? -19.125 -16.229 45.762  1.00   56.69  ? 319 LEU B CB  1 
ATOM   5273 C  CG  . LEU B 1 304 ? -18.825 -16.467 44.275  1.00   58.00  ? 319 LEU B CG  1 
ATOM   5274 C  CD1 . LEU B 1 304 ? -19.382 -15.329 43.439  1.00   58.89  ? 319 LEU B CD1 1 
ATOM   5275 C  CD2 . LEU B 1 304 ? -17.348 -16.646 43.962  1.00   57.19  ? 319 LEU B CD2 1 
ATOM   5276 N  N   . HIS B 1 305 ? -20.652 -16.250 48.573  1.00   56.23  ? 320 HIS B N   1 
ATOM   5277 C  CA  . HIS B 1 305 ? -20.867 -16.817 49.925  1.00   57.35  ? 320 HIS B CA  1 
ATOM   5278 C  C   . HIS B 1 305 ? -22.339 -16.957 50.300  1.00   60.10  ? 320 HIS B C   1 
ATOM   5279 O  O   . HIS B 1 305 ? -22.697 -17.803 51.124  1.00   61.73  ? 320 HIS B O   1 
ATOM   5280 C  CB  . HIS B 1 305 ? -20.166 -15.979 51.017  1.00   56.00  ? 320 HIS B CB  1 
ATOM   5281 C  CG  . HIS B 1 305 ? -18.700 -16.250 51.136  1.00   54.67  ? 320 HIS B CG  1 
ATOM   5282 N  ND1 . HIS B 1 305 ? -18.190 -17.222 51.970  1.00   55.26  ? 320 HIS B ND1 1 
ATOM   5283 C  CD2 . HIS B 1 305 ? -17.641 -15.708 50.493  1.00   52.90  ? 320 HIS B CD2 1 
ATOM   5284 C  CE1 . HIS B 1 305 ? -16.875 -17.256 51.846  1.00   54.65  ? 320 HIS B CE1 1 
ATOM   5285 N  NE2 . HIS B 1 305 ? -16.517 -16.353 50.950  1.00   53.51  ? 320 HIS B NE2 1 
ATOM   5286 N  N   . HIS B 1 306 ? -23.194 -16.137 49.700  1.00   61.04  ? 321 HIS B N   1 
ATOM   5287 C  CA  . HIS B 1 306 ? -24.598 -16.154 50.029  1.00   63.05  ? 321 HIS B CA  1 
ATOM   5288 C  C   . HIS B 1 306 ? -25.441 -16.470 48.787  1.00   67.20  ? 321 HIS B C   1 
ATOM   5289 O  O   . HIS B 1 306 ? -26.143 -15.609 48.247  1.00   68.11  ? 321 HIS B O   1 
ATOM   5290 C  CB  . HIS B 1 306 ? -24.939 -14.844 50.715  1.00   61.25  ? 321 HIS B CB  1 
ATOM   5291 C  CG  . HIS B 1 306 ? -24.318 -14.729 52.080  1.00   60.56  ? 321 HIS B CG  1 
ATOM   5292 N  ND1 . HIS B 1 306 ? -23.453 -13.715 52.436  1.00   58.23  ? 321 HIS B ND1 1 
ATOM   5293 C  CD2 . HIS B 1 306 ? -24.411 -15.533 53.168  1.00   61.74  ? 321 HIS B CD2 1 
ATOM   5294 C  CE1 . HIS B 1 306 ? -23.061 -13.887 53.685  1.00   57.71  ? 321 HIS B CE1 1 
ATOM   5295 N  NE2 . HIS B 1 306 ? -23.622 -14.986 54.151  1.00   59.41  ? 321 HIS B NE2 1 
ATOM   5296 N  N   . PRO B 1 307 ? -25.382 -17.741 48.336  1.00   70.01  ? 322 PRO B N   1 
ATOM   5297 C  CA  . PRO B 1 307 ? -26.052 -18.107 47.097  1.00   71.50  ? 322 PRO B CA  1 
ATOM   5298 C  C   . PRO B 1 307 ? -27.558 -17.928 47.157  1.00   76.04  ? 322 PRO B C   1 
ATOM   5299 O  O   . PRO B 1 307 ? -28.147 -17.505 46.164  1.00   80.56  ? 322 PRO B O   1 
ATOM   5300 C  CB  . PRO B 1 307 ? -25.713 -19.592 46.914  1.00   71.87  ? 322 PRO B CB  1 
ATOM   5301 C  CG  . PRO B 1 307 ? -24.712 -19.937 47.943  1.00   71.43  ? 322 PRO B CG  1 
ATOM   5302 C  CD  . PRO B 1 307 ? -24.813 -18.914 49.025  1.00   70.52  ? 322 PRO B CD  1 
ATOM   5303 N  N   . GLN B 1 308 ? -28.182 -18.281 48.279  1.00   77.85  ? 323 GLN B N   1 
ATOM   5304 C  CA  . GLN B 1 308 ? -29.645 -18.086 48.445  1.00   81.27  ? 323 GLN B CA  1 
ATOM   5305 C  C   . GLN B 1 308 ? -30.057 -16.631 48.159  1.00   79.76  ? 323 GLN B C   1 
ATOM   5306 O  O   . GLN B 1 308 ? -31.054 -16.363 47.480  1.00   81.35  ? 323 GLN B O   1 
ATOM   5307 C  CB  . GLN B 1 308 ? -30.136 -18.567 49.833  1.00   82.80  ? 323 GLN B CB  1 
ATOM   5308 C  CG  . GLN B 1 308 ? -29.746 -17.715 51.049  1.00   84.09  ? 323 GLN B CG  1 
ATOM   5309 C  CD  . GLN B 1 308 ? -28.237 -17.643 51.337  1.00   82.71  ? 323 GLN B CD  1 
ATOM   5310 O  OE1 . GLN B 1 308 ? -27.439 -18.466 50.873  1.00   83.67  ? 323 GLN B OE1 1 
ATOM   5311 N  NE2 . GLN B 1 308 ? -27.849 -16.646 52.111  1.00   82.55  ? 323 GLN B NE2 1 
ATOM   5312 N  N   . LEU B 1 309 ? -29.231 -15.711 48.628  1.00   77.52  ? 324 LEU B N   1 
ATOM   5313 C  CA  . LEU B 1 309 ? -29.452 -14.286 48.475  1.00   77.68  ? 324 LEU B CA  1 
ATOM   5314 C  C   . LEU B 1 309 ? -29.223 -13.784 47.040  1.00   76.78  ? 324 LEU B C   1 
ATOM   5315 O  O   . LEU B 1 309 ? -29.888 -12.849 46.585  1.00   76.83  ? 324 LEU B O   1 
ATOM   5316 C  CB  . LEU B 1 309 ? -28.510 -13.569 49.426  1.00   77.38  ? 324 LEU B CB  1 
ATOM   5317 C  CG  . LEU B 1 309 ? -28.685 -12.083 49.664  1.00   79.12  ? 324 LEU B CG  1 
ATOM   5318 C  CD1 . LEU B 1 309 ? -30.102 -11.768 50.090  1.00   82.29  ? 324 LEU B CD1 1 
ATOM   5319 C  CD2 . LEU B 1 309 ? -27.695 -11.664 50.746  1.00   80.54  ? 324 LEU B CD2 1 
ATOM   5320 N  N   . GLN B 1 310 ? -28.268 -14.391 46.339  1.00   74.51  ? 325 GLN B N   1 
ATOM   5321 C  CA  . GLN B 1 310 ? -28.107 -14.158 44.905  1.00   72.84  ? 325 GLN B CA  1 
ATOM   5322 C  C   . GLN B 1 310 ? -29.448 -14.447 44.192  1.00   75.21  ? 325 GLN B C   1 
ATOM   5323 O  O   . GLN B 1 310 ? -30.009 -13.571 43.527  1.00   76.21  ? 325 GLN B O   1 
ATOM   5324 C  CB  . GLN B 1 310 ? -26.971 -15.034 44.341  1.00   71.23  ? 325 GLN B CB  1 
ATOM   5325 C  CG  . GLN B 1 310 ? -26.636 -14.757 42.876  1.00   71.47  ? 325 GLN B CG  1 
ATOM   5326 C  CD  . GLN B 1 310 ? -25.366 -15.432 42.350  1.00   70.94  ? 325 GLN B CD  1 
ATOM   5327 O  OE1 . GLN B 1 310 ? -24.993 -15.212 41.195  1.00   70.23  ? 325 GLN B OE1 1 
ATOM   5328 N  NE2 . GLN B 1 310 ? -24.699 -16.248 43.177  1.00   70.48  ? 325 GLN B NE2 1 
ATOM   5329 N  N   . GLU B 1 311 ? -29.974 -15.658 44.365  1.00   75.91  ? 326 GLU B N   1 
ATOM   5330 C  CA  . GLU B 1 311 ? -31.278 -16.038 43.795  1.00   77.71  ? 326 GLU B CA  1 
ATOM   5331 C  C   . GLU B 1 311 ? -32.377 -14.996 44.036  1.00   76.64  ? 326 GLU B C   1 
ATOM   5332 O  O   . GLU B 1 311 ? -33.154 -14.687 43.139  1.00   75.74  ? 326 GLU B O   1 
ATOM   5333 C  CB  . GLU B 1 311 ? -31.736 -17.380 44.368  1.00   80.89  ? 326 GLU B CB  1 
ATOM   5334 C  CG  . GLU B 1 311 ? -30.928 -18.572 43.875  1.00   81.97  ? 326 GLU B CG  1 
ATOM   5335 C  CD  . GLU B 1 311 ? -30.811 -19.666 44.920  1.00   85.05  ? 326 GLU B CD  1 
ATOM   5336 O  OE1 . GLU B 1 311 ? -31.750 -20.487 45.045  1.00   89.11  ? 326 GLU B OE1 1 
ATOM   5337 O  OE2 . GLU B 1 311 ? -29.770 -19.699 45.621  1.00   85.10  ? 326 GLU B OE2 1 
ATOM   5338 N  N   . ARG B 1 312 ? -32.435 -14.452 45.242  1.00   75.63  ? 327 ARG B N   1 
ATOM   5339 C  CA  . ARG B 1 312 ? -33.508 -13.534 45.582  1.00   77.60  ? 327 ARG B CA  1 
ATOM   5340 C  C   . ARG B 1 312 ? -33.419 -12.224 44.813  1.00   74.93  ? 327 ARG B C   1 
ATOM   5341 O  O   . ARG B 1 312 ? -34.421 -11.736 44.298  1.00   77.30  ? 327 ARG B O   1 
ATOM   5342 C  CB  . ARG B 1 312 ? -33.528 -13.265 47.079  1.00   79.98  ? 327 ARG B CB  1 
ATOM   5343 C  CG  . ARG B 1 312 ? -33.834 -14.481 47.945  1.00   83.14  ? 327 ARG B CG  1 
ATOM   5344 C  CD  . ARG B 1 312 ? -33.396 -14.229 49.385  1.00   85.43  ? 327 ARG B CD  1 
ATOM   5345 N  NE  . ARG B 1 312 ? -34.146 -13.129 49.987  1.00   88.26  ? 327 ARG B NE  1 
ATOM   5346 C  CZ  . ARG B 1 312 ? -33.835 -12.516 51.127  1.00   91.29  ? 327 ARG B CZ  1 
ATOM   5347 N  NH1 . ARG B 1 312 ? -32.764 -12.877 51.828  1.00   89.27  ? 327 ARG B NH1 1 
ATOM   5348 N  NH2 . ARG B 1 312 ? -34.619 -11.531 51.572  1.00   95.09  ? 327 ARG B NH2 1 
ATOM   5349 N  N   . VAL B 1 313 ? -32.227 -11.661 44.718  1.00   71.15  ? 328 VAL B N   1 
ATOM   5350 C  CA  . VAL B 1 313 ? -32.055 -10.405 43.998  1.00   69.47  ? 328 VAL B CA  1 
ATOM   5351 C  C   . VAL B 1 313 ? -32.428 -10.681 42.558  1.00   70.18  ? 328 VAL B C   1 
ATOM   5352 O  O   . VAL B 1 313 ? -33.216 -9.952  41.954  1.00   71.10  ? 328 VAL B O   1 
ATOM   5353 C  CB  . VAL B 1 313 ? -30.606 -9.870  44.057  1.00   66.95  ? 328 VAL B CB  1 
ATOM   5354 C  CG1 . VAL B 1 313 ? -30.540 -8.461  43.475  1.00   65.85  ? 328 VAL B CG1 1 
ATOM   5355 C  CG2 . VAL B 1 313 ? -30.071 -9.886  45.494  1.00   65.98  ? 328 VAL B CG2 1 
ATOM   5356 N  N   . GLN B 1 314 ? -31.874 -11.760 42.019  1.00   69.32  ? 329 GLN B N   1 
ATOM   5357 C  CA  . GLN B 1 314 ? -32.210 -12.194 40.663  1.00   70.69  ? 329 GLN B CA  1 
ATOM   5358 C  C   . GLN B 1 314 ? -33.726 -12.258 40.459  1.00   73.77  ? 329 GLN B C   1 
ATOM   5359 O  O   . GLN B 1 314 ? -34.238 -11.812 39.431  1.00   73.40  ? 329 GLN B O   1 
ATOM   5360 C  CB  . GLN B 1 314 ? -31.542 -13.539 40.329  1.00   70.07  ? 329 GLN B CB  1 
ATOM   5361 C  CG  . GLN B 1 314 ? -30.184 -13.377 39.651  1.00   68.60  ? 329 GLN B CG  1 
ATOM   5362 C  CD  . GLN B 1 314 ? -29.283 -14.590 39.784  1.00   68.67  ? 329 GLN B CD  1 
ATOM   5363 O  OE1 . GLN B 1 314 ? -29.315 -15.306 40.787  1.00   70.23  ? 329 GLN B OE1 1 
ATOM   5364 N  NE2 . GLN B 1 314 ? -28.453 -14.814 38.783  1.00   68.55  ? 329 GLN B NE2 1 
ATOM   5365 N  N   . ALA B 1 315 ? -34.431 -12.797 41.451  1.00   75.42  ? 330 ALA B N   1 
ATOM   5366 C  CA  . ALA B 1 315 ? -35.886 -12.895 41.388  1.00   79.43  ? 330 ALA B CA  1 
ATOM   5367 C  C   . ALA B 1 315 ? -36.543 -11.530 41.524  1.00   79.58  ? 330 ALA B C   1 
ATOM   5368 O  O   . ALA B 1 315 ? -37.580 -11.276 40.932  1.00   81.06  ? 330 ALA B O   1 
ATOM   5369 C  CB  . ALA B 1 315 ? -36.412 -13.838 42.463  1.00   80.99  ? 330 ALA B CB  1 
ATOM   5370 N  N   . GLU B 1 316 ? -35.959 -10.658 42.332  1.00   77.68  ? 331 GLU B N   1 
ATOM   5371 C  CA  . GLU B 1 316 ? -36.491 -9.317  42.449  1.00   77.77  ? 331 GLU B CA  1 
ATOM   5372 C  C   . GLU B 1 316 ? -36.432 -8.676  41.075  1.00   77.62  ? 331 GLU B C   1 
ATOM   5373 O  O   . GLU B 1 316 ? -37.394 -8.079  40.605  1.00   78.84  ? 331 GLU B O   1 
ATOM   5374 C  CB  . GLU B 1 316 ? -35.684 -8.500  43.451  1.00   75.70  ? 331 GLU B CB  1 
ATOM   5375 C  CG  . GLU B 1 316 ? -36.345 -7.187  43.800  1.00   77.19  ? 331 GLU B CG  1 
ATOM   5376 C  CD  . GLU B 1 316 ? -35.482 -6.309  44.669  1.00   75.51  ? 331 GLU B CD  1 
ATOM   5377 O  OE1 . GLU B 1 316 ? -34.356 -5.960  44.230  1.00   75.38  ? 331 GLU B OE1 1 
ATOM   5378 O  OE2 . GLU B 1 316 ? -35.937 -5.961  45.781  1.00   74.39  ? 331 GLU B OE2 1 
ATOM   5379 N  N   . LEU B 1 317 ? -35.278 -8.816  40.435  1.00   76.25  ? 332 LEU B N   1 
ATOM   5380 C  CA  . LEU B 1 317 ? -35.077 -8.271  39.113  1.00   76.16  ? 332 LEU B CA  1 
ATOM   5381 C  C   . LEU B 1 317 ? -36.065 -8.922  38.163  1.00   78.99  ? 332 LEU B C   1 
ATOM   5382 O  O   . LEU B 1 317 ? -36.760 -8.225  37.435  1.00   81.18  ? 332 LEU B O   1 
ATOM   5383 C  CB  . LEU B 1 317 ? -33.635 -8.503  38.635  1.00   74.10  ? 332 LEU B CB  1 
ATOM   5384 C  CG  . LEU B 1 317 ? -32.647 -7.367  38.952  1.00   72.83  ? 332 LEU B CG  1 
ATOM   5385 C  CD1 . LEU B 1 317 ? -31.240 -7.861  39.332  1.00   70.89  ? 332 LEU B CD1 1 
ATOM   5386 C  CD2 . LEU B 1 317 ? -32.591 -6.364  37.806  1.00   71.64  ? 332 LEU B CD2 1 
ATOM   5387 N  N   . ASP B 1 318 ? -36.140 -10.250 38.185  1.00   79.13  ? 333 ASP B N   1 
ATOM   5388 C  CA  . ASP B 1 318 ? -36.964 -10.981 37.224  1.00   82.18  ? 333 ASP B CA  1 
ATOM   5389 C  C   . ASP B 1 318 ? -38.400 -10.484 37.222  1.00   86.85  ? 333 ASP B C   1 
ATOM   5390 O  O   . ASP B 1 318 ? -38.974 -10.240 36.178  1.00   87.23  ? 333 ASP B O   1 
ATOM   5391 C  CB  . ASP B 1 318 ? -36.909 -12.490 37.479  1.00   81.75  ? 333 ASP B CB  1 
ATOM   5392 C  CG  . ASP B 1 318 ? -35.666 -13.152 36.858  1.00   80.00  ? 333 ASP B CG  1 
ATOM   5393 O  OD1 . ASP B 1 318 ? -34.850 -12.480 36.168  1.00   76.32  ? 333 ASP B OD1 1 
ATOM   5394 O  OD2 . ASP B 1 318 ? -35.517 -14.374 37.056  1.00   81.00  ? 333 ASP B OD2 1 
ATOM   5395 N  N   . GLU B 1 319 ? -38.956 -10.302 38.404  1.00   91.17  ? 334 GLU B N   1 
ATOM   5396 C  CA  . GLU B 1 319 ? -40.291 -9.763  38.549  1.00   97.51  ? 334 GLU B CA  1 
ATOM   5397 C  C   . GLU B 1 319 ? -40.417 -8.307  38.115  1.00   100.48 ? 334 GLU B C   1 
ATOM   5398 O  O   . GLU B 1 319 ? -41.389 -7.918  37.490  1.00   104.12 ? 334 GLU B O   1 
ATOM   5399 C  CB  . GLU B 1 319 ? -40.712 -9.904  40.007  1.00   99.48  ? 334 GLU B CB  1 
ATOM   5400 C  CG  . GLU B 1 319 ? -42.040 -9.265  40.374  1.00   103.07 ? 334 GLU B CG  1 
ATOM   5401 C  CD  . GLU B 1 319 ? -42.605 -9.883  41.627  1.00   106.35 ? 334 GLU B CD  1 
ATOM   5402 O  OE1 . GLU B 1 319 ? -41.809 -10.563 42.319  1.00   105.57 ? 334 GLU B OE1 1 
ATOM   5403 O  OE2 . GLU B 1 319 ? -43.820 -9.702  41.920  1.00   111.78 ? 334 GLU B OE2 1 
ATOM   5404 N  N   . CYS B 1 320 ? -39.443 -7.493  38.470  1.00   104.00 ? 335 CYS B N   1 
ATOM   5405 C  CA  . CYS B 1 320 ? -39.568 -6.061  38.273  1.00   108.93 ? 335 CYS B CA  1 
ATOM   5406 C  C   . CYS B 1 320 ? -39.137 -5.636  36.887  1.00   108.99 ? 335 CYS B C   1 
ATOM   5407 O  O   . CYS B 1 320 ? -39.654 -4.663  36.360  1.00   113.00 ? 335 CYS B O   1 
ATOM   5408 C  CB  . CYS B 1 320 ? -38.781 -5.323  39.348  1.00   108.94 ? 335 CYS B CB  1 
ATOM   5409 S  SG  . CYS B 1 320 ? -39.575 -5.527  40.961  1.00   117.63 ? 335 CYS B SG  1 
ATOM   5410 N  N   . VAL B 1 321 ? -38.186 -6.368  36.316  1.00   107.78 ? 336 VAL B N   1 
ATOM   5411 C  CA  . VAL B 1 321 ? -37.730 -6.187  34.938  1.00   107.60 ? 336 VAL B CA  1 
ATOM   5412 C  C   . VAL B 1 321 ? -37.885 -7.564  34.299  1.00   108.52 ? 336 VAL B C   1 
ATOM   5413 O  O   . VAL B 1 321 ? -37.926 -8.562  34.995  1.00   108.42 ? 336 VAL B O   1 
ATOM   5414 C  CB  . VAL B 1 321 ? -36.245 -5.735  34.899  1.00   103.77 ? 336 VAL B CB  1 
ATOM   5415 C  CG1 . VAL B 1 321 ? -35.795 -5.447  33.472  1.00   104.21 ? 336 VAL B CG1 1 
ATOM   5416 C  CG2 . VAL B 1 321 ? -36.030 -4.505  35.777  1.00   100.87 ? 336 VAL B CG2 1 
ATOM   5417 N  N   . GLY B 1 322 ? -37.989 -7.649  32.988  1.00   110.72 ? 337 GLY B N   1 
ATOM   5418 C  CA  . GLY B 1 322 ? -38.020 -8.967  32.376  1.00   115.85 ? 337 GLY B CA  1 
ATOM   5419 C  C   . GLY B 1 322 ? -36.650 -9.622  32.455  1.00   117.35 ? 337 GLY B C   1 
ATOM   5420 O  O   . GLY B 1 322 ? -35.655 -8.957  32.764  1.00   110.84 ? 337 GLY B O   1 
ATOM   5421 N  N   . VAL B 1 323 ? -36.601 -10.927 32.167  1.00   125.12 ? 338 VAL B N   1 
ATOM   5422 C  CA  . VAL B 1 323 ? -35.328 -11.638 31.881  1.00   126.93 ? 338 VAL B CA  1 
ATOM   5423 C  C   . VAL B 1 323 ? -34.858 -11.309 30.448  1.00   131.03 ? 338 VAL B C   1 
ATOM   5424 O  O   . VAL B 1 323 ? -34.275 -12.127 29.730  1.00   134.79 ? 338 VAL B O   1 
ATOM   5425 C  CB  . VAL B 1 323 ? -35.440 -13.174 32.116  1.00   127.08 ? 338 VAL B CB  1 
ATOM   5426 C  CG1 . VAL B 1 323 ? -36.416 -13.835 31.138  1.00   129.39 ? 338 VAL B CG1 1 
ATOM   5427 C  CG2 . VAL B 1 323 ? -34.066 -13.846 32.061  1.00   122.89 ? 338 VAL B CG2 1 
ATOM   5428 N  N   . ASP B 1 324 ? -35.117 -10.064 30.072  1.00   131.01 ? 339 ASP B N   1 
ATOM   5429 C  CA  . ASP B 1 324 ? -34.804 -9.488  28.787  1.00   126.65 ? 339 ASP B CA  1 
ATOM   5430 C  C   . ASP B 1 324 ? -35.008 -8.020  29.101  1.00   125.47 ? 339 ASP B C   1 
ATOM   5431 O  O   . ASP B 1 324 ? -35.807 -7.702  29.988  1.00   127.52 ? 339 ASP B O   1 
ATOM   5432 C  CB  . ASP B 1 324 ? -35.809 -9.930  27.739  1.00   127.74 ? 339 ASP B CB  1 
ATOM   5433 C  CG  . ASP B 1 324 ? -37.219 -9.534  28.101  1.00   130.79 ? 339 ASP B CG  1 
ATOM   5434 O  OD1 . ASP B 1 324 ? -37.669 -9.898  29.210  1.00   130.15 ? 339 ASP B OD1 1 
ATOM   5435 O  OD2 . ASP B 1 324 ? -37.867 -8.839  27.290  1.00   135.72 ? 339 ASP B OD2 1 
ATOM   5436 N  N   . ARG B 1 325 ? -34.294 -7.132  28.416  1.00   121.62 ? 340 ARG B N   1 
ATOM   5437 C  CA  . ARG B 1 325 ? -34.400 -5.679  28.655  1.00   115.47 ? 340 ARG B CA  1 
ATOM   5438 C  C   . ARG B 1 325 ? -33.398 -5.202  29.721  1.00   108.21 ? 340 ARG B C   1 
ATOM   5439 O  O   . ARG B 1 325 ? -33.242 -5.841  30.770  1.00   106.01 ? 340 ARG B O   1 
ATOM   5440 C  CB  . ARG B 1 325 ? -35.850 -5.267  29.016  1.00   113.68 ? 340 ARG B CB  1 
ATOM   5441 C  CG  . ARG B 1 325 ? -36.021 -3.993  29.837  1.00   110.51 ? 340 ARG B CG  1 
ATOM   5442 C  CD  . ARG B 1 325 ? -37.363 -3.976  30.559  1.00   109.17 ? 340 ARG B CD  1 
ATOM   5443 N  NE  . ARG B 1 325 ? -37.520 -2.799  31.412  1.00   107.27 ? 340 ARG B NE  1 
ATOM   5444 C  CZ  . ARG B 1 325 ? -37.850 -1.585  30.977  1.00   105.85 ? 340 ARG B CZ  1 
ATOM   5445 N  NH1 . ARG B 1 325 ? -38.058 -1.361  29.692  1.00   107.10 ? 340 ARG B NH1 1 
ATOM   5446 N  NH2 . ARG B 1 325 ? -37.978 -0.584  31.835  1.00   105.34 ? 340 ARG B NH2 1 
ATOM   5447 N  N   . PRO B 1 326 ? -32.742 -4.055  29.470  1.00   101.61 ? 341 PRO B N   1 
ATOM   5448 C  CA  . PRO B 1 326 ? -31.767 -3.576  30.408  1.00   98.08  ? 341 PRO B CA  1 
ATOM   5449 C  C   . PRO B 1 326 ? -32.460 -2.791  31.541  1.00   94.97  ? 341 PRO B C   1 
ATOM   5450 O  O   . PRO B 1 326 ? -33.351 -1.984  31.258  1.00   97.02  ? 341 PRO B O   1 
ATOM   5451 C  CB  . PRO B 1 326 ? -30.904 -2.666  29.535  1.00   97.10  ? 341 PRO B CB  1 
ATOM   5452 C  CG  . PRO B 1 326 ? -31.854 -2.095  28.551  1.00   99.78  ? 341 PRO B CG  1 
ATOM   5453 C  CD  . PRO B 1 326 ? -33.034 -3.026  28.458  1.00   103.32 ? 341 PRO B CD  1 
ATOM   5454 N  N   . PRO B 1 327 ? -32.078 -3.044  32.816  1.00   88.37  ? 342 PRO B N   1 
ATOM   5455 C  CA  . PRO B 1 327 ? -32.596 -2.233  33.913  1.00   85.20  ? 342 PRO B CA  1 
ATOM   5456 C  C   . PRO B 1 327 ? -32.026 -0.827  33.882  1.00   83.07  ? 342 PRO B C   1 
ATOM   5457 O  O   . PRO B 1 327 ? -30.815 -0.654  33.795  1.00   85.04  ? 342 PRO B O   1 
ATOM   5458 C  CB  . PRO B 1 327 ? -32.116 -2.976  35.166  1.00   82.66  ? 342 PRO B CB  1 
ATOM   5459 C  CG  . PRO B 1 327 ? -31.720 -4.336  34.707  1.00   82.96  ? 342 PRO B CG  1 
ATOM   5460 C  CD  . PRO B 1 327 ? -31.223 -4.134  33.320  1.00   85.71  ? 342 PRO B CD  1 
ATOM   5461 N  N   . CYS B 1 328 ? -32.892 0.167   33.951  1.00   82.61  ? 343 CYS B N   1 
ATOM   5462 C  CA  . CYS B 1 328 ? -32.477 1.557   33.930  1.00   80.91  ? 343 CYS B CA  1 
ATOM   5463 C  C   . CYS B 1 328 ? -32.784 2.147   35.294  1.00   79.87  ? 343 CYS B C   1 
ATOM   5464 O  O   . CYS B 1 328 ? -33.393 1.485   36.122  1.00   80.02  ? 343 CYS B O   1 
ATOM   5465 C  CB  . CYS B 1 328 ? -33.279 2.285   32.871  1.00   83.26  ? 343 CYS B CB  1 
ATOM   5466 S  SG  . CYS B 1 328 ? -35.031 2.116   33.227  1.00   84.16  ? 343 CYS B SG  1 
ATOM   5467 N  N   . LEU B 1 329 ? -32.391 3.401   35.504  1.00   79.63  ? 344 LEU B N   1 
ATOM   5468 C  CA  . LEU B 1 329 ? -32.455 4.053   36.820  1.00   79.05  ? 344 LEU B CA  1 
ATOM   5469 C  C   . LEU B 1 329 ? -33.850 4.218   37.412  1.00   81.06  ? 344 LEU B C   1 
ATOM   5470 O  O   . LEU B 1 329 ? -34.016 4.295   38.625  1.00   77.35  ? 344 LEU B O   1 
ATOM   5471 C  CB  . LEU B 1 329 ? -31.779 5.421   36.744  1.00   79.16  ? 344 LEU B CB  1 
ATOM   5472 C  CG  . LEU B 1 329 ? -30.262 5.316   36.633  1.00   78.76  ? 344 LEU B CG  1 
ATOM   5473 C  CD1 . LEU B 1 329 ? -29.616 6.665   36.362  1.00   79.59  ? 344 LEU B CD1 1 
ATOM   5474 C  CD2 . LEU B 1 329 ? -29.692 4.730   37.911  1.00   77.45  ? 344 LEU B CD2 1 
ATOM   5475 N  N   . SER B 1 330 ? -34.858 4.280   36.552  1.00   85.20  ? 345 SER B N   1 
ATOM   5476 C  CA  . SER B 1 330 ? -36.238 4.401   37.019  1.00   87.46  ? 345 SER B CA  1 
ATOM   5477 C  C   . SER B 1 330 ? -36.726 3.131   37.727  1.00   85.65  ? 345 SER B C   1 
ATOM   5478 O  O   . SER B 1 330 ? -37.744 3.160   38.397  1.00   85.30  ? 345 SER B O   1 
ATOM   5479 C  CB  . SER B 1 330 ? -37.124 4.758   35.836  1.00   91.63  ? 345 SER B CB  1 
ATOM   5480 O  OG  . SER B 1 330 ? -36.389 4.567   34.637  1.00   93.26  ? 345 SER B OG  1 
ATOM   5481 N  N   . ASP B 1 331 ? -35.982 2.032   37.582  1.00   83.95  ? 346 ASP B N   1 
ATOM   5482 C  CA  . ASP B 1 331 ? -36.272 0.769   38.269  1.00   83.43  ? 346 ASP B CA  1 
ATOM   5483 C  C   . ASP B 1 331 ? -35.803 0.693   39.713  1.00   82.01  ? 346 ASP B C   1 
ATOM   5484 O  O   . ASP B 1 331 ? -36.150 -0.258  40.413  1.00   80.81  ? 346 ASP B O   1 
ATOM   5485 C  CB  . ASP B 1 331 ? -35.606 -0.398  37.534  1.00   82.02  ? 346 ASP B CB  1 
ATOM   5486 C  CG  . ASP B 1 331 ? -36.238 -0.690  36.218  1.00   81.97  ? 346 ASP B CG  1 
ATOM   5487 O  OD1 . ASP B 1 331 ? -37.452 -0.490  36.102  1.00   86.07  ? 346 ASP B OD1 1 
ATOM   5488 O  OD2 . ASP B 1 331 ? -35.531 -1.134  35.302  1.00   80.56  ? 346 ASP B OD2 1 
ATOM   5489 N  N   . ARG B 1 332 ? -35.007 1.663   40.153  1.00   82.04  ? 347 ARG B N   1 
ATOM   5490 C  CA  . ARG B 1 332 ? -34.397 1.597   41.487  1.00   81.84  ? 347 ARG B CA  1 
ATOM   5491 C  C   . ARG B 1 332 ? -35.437 1.451   42.588  1.00   83.48  ? 347 ARG B C   1 
ATOM   5492 O  O   . ARG B 1 332 ? -35.339 0.550   43.423  1.00   84.41  ? 347 ARG B O   1 
ATOM   5493 C  CB  . ARG B 1 332 ? -33.525 2.827   41.785  1.00   81.93  ? 347 ARG B CB  1 
ATOM   5494 C  CG  . ARG B 1 332 ? -32.292 2.993   40.918  1.00   81.62  ? 347 ARG B CG  1 
ATOM   5495 C  CD  . ARG B 1 332 ? -31.513 4.222   41.353  1.00   82.93  ? 347 ARG B CD  1 
ATOM   5496 N  NE  . ARG B 1 332 ? -30.604 3.864   42.445  1.00   82.75  ? 347 ARG B NE  1 
ATOM   5497 C  CZ  . ARG B 1 332 ? -29.371 4.345   42.619  1.00   83.23  ? 347 ARG B CZ  1 
ATOM   5498 N  NH1 . ARG B 1 332 ? -28.851 5.264   41.802  1.00   82.89  ? 347 ARG B NH1 1 
ATOM   5499 N  NH2 . ARG B 1 332 ? -28.641 3.892   43.635  1.00   84.91  ? 347 ARG B NH2 1 
ATOM   5500 N  N   . PRO B 1 333 ? -36.440 2.337   42.610  1.00   85.63  ? 348 PRO B N   1 
ATOM   5501 C  CA  . PRO B 1 333 ? -37.430 2.243   43.706  1.00   86.32  ? 348 PRO B CA  1 
ATOM   5502 C  C   . PRO B 1 333 ? -38.111 0.853   43.836  1.00   85.91  ? 348 PRO B C   1 
ATOM   5503 O  O   . PRO B 1 333 ? -38.429 0.422   44.949  1.00   83.66  ? 348 PRO B O   1 
ATOM   5504 C  CB  . PRO B 1 333 ? -38.452 3.330   43.336  1.00   90.16  ? 348 PRO B CB  1 
ATOM   5505 C  CG  . PRO B 1 333 ? -37.689 4.283   42.456  1.00   89.03  ? 348 PRO B CG  1 
ATOM   5506 C  CD  . PRO B 1 333 ? -36.755 3.425   41.668  1.00   85.68  ? 348 PRO B CD  1 
ATOM   5507 N  N   . HIS B 1 334 ? -38.294 0.160   42.704  1.00   85.41  ? 349 HIS B N   1 
ATOM   5508 C  CA  . HIS B 1 334 ? -38.874 -1.201  42.669  1.00   86.17  ? 349 HIS B CA  1 
ATOM   5509 C  C   . HIS B 1 334 ? -37.856 -2.327  42.905  1.00   84.33  ? 349 HIS B C   1 
ATOM   5510 O  O   . HIS B 1 334 ? -38.168 -3.497  42.665  1.00   82.74  ? 349 HIS B O   1 
ATOM   5511 C  CB  . HIS B 1 334 ? -39.577 -1.462  41.321  1.00   88.39  ? 349 HIS B CB  1 
ATOM   5512 C  CG  . HIS B 1 334 ? -40.482 -0.355  40.887  1.00   89.58  ? 349 HIS B CG  1 
ATOM   5513 N  ND1 . HIS B 1 334 ? -41.585 0.026   41.622  1.00   92.00  ? 349 HIS B ND1 1 
ATOM   5514 C  CD2 . HIS B 1 334 ? -40.428 0.476   39.821  1.00   88.59  ? 349 HIS B CD2 1 
ATOM   5515 C  CE1 . HIS B 1 334 ? -42.179 1.038   41.018  1.00   93.84  ? 349 HIS B CE1 1 
ATOM   5516 N  NE2 . HIS B 1 334 ? -41.491 1.335   39.929  1.00   92.50  ? 349 HIS B NE2 1 
ATOM   5517 N  N   . LEU B 1 335 ? -36.652 -1.973  43.373  1.00   83.60  ? 350 LEU B N   1 
ATOM   5518 C  CA  . LEU B 1 335 ? -35.555 -2.920  43.590  1.00   80.46  ? 350 LEU B CA  1 
ATOM   5519 C  C   . LEU B 1 335 ? -34.897 -2.591  44.929  1.00   78.97  ? 350 LEU B C   1 
ATOM   5520 O  O   . LEU B 1 335 ? -33.725 -2.175  44.980  1.00   78.60  ? 350 LEU B O   1 
ATOM   5521 C  CB  . LEU B 1 335 ? -34.554 -2.846  42.432  1.00   79.33  ? 350 LEU B CB  1 
ATOM   5522 C  CG  . LEU B 1 335 ? -35.123 -3.288  41.070  1.00   81.93  ? 350 LEU B CG  1 
ATOM   5523 C  CD1 . LEU B 1 335 ? -34.211 -2.934  39.907  1.00   80.18  ? 350 LEU B CD1 1 
ATOM   5524 C  CD2 . LEU B 1 335 ? -35.416 -4.782  41.076  1.00   83.53  ? 350 LEU B CD2 1 
ATOM   5525 N  N   . PRO B 1 336 ? -35.664 -2.757  46.021  1.00   78.90  ? 351 PRO B N   1 
ATOM   5526 C  CA  . PRO B 1 336 ? -35.207 -2.420  47.364  1.00   77.01  ? 351 PRO B CA  1 
ATOM   5527 C  C   . PRO B 1 336 ? -34.130 -3.359  47.905  1.00   74.45  ? 351 PRO B C   1 
ATOM   5528 O  O   . PRO B 1 336 ? -33.267 -2.913  48.688  1.00   74.67  ? 351 PRO B O   1 
ATOM   5529 C  CB  . PRO B 1 336 ? -36.484 -2.551  48.205  1.00   79.15  ? 351 PRO B CB  1 
ATOM   5530 C  CG  . PRO B 1 336 ? -37.309 -3.553  47.477  1.00   81.07  ? 351 PRO B CG  1 
ATOM   5531 C  CD  . PRO B 1 336 ? -37.072 -3.210  46.035  1.00   81.39  ? 351 PRO B CD  1 
ATOM   5532 N  N   . LEU B 1 337 ? -34.198 -4.637  47.514  1.00   71.87  ? 352 LEU B N   1 
ATOM   5533 C  CA  . LEU B 1 337 ? -33.230 -5.647  47.962  1.00   68.73  ? 352 LEU B CA  1 
ATOM   5534 C  C   . LEU B 1 337 ? -31.873 -5.390  47.340  1.00   65.62  ? 352 LEU B C   1 
ATOM   5535 O  O   . LEU B 1 337 ? -30.898 -5.236  48.049  1.00   63.32  ? 352 LEU B O   1 
ATOM   5536 C  CB  . LEU B 1 337 ? -33.713 -7.069  47.648  1.00   68.84  ? 352 LEU B CB  1 
ATOM   5537 C  CG  . LEU B 1 337 ? -32.964 -8.286  48.210  1.00   67.21  ? 352 LEU B CG  1 
ATOM   5538 C  CD1 . LEU B 1 337 ? -32.658 -8.158  49.685  1.00   66.35  ? 352 LEU B CD1 1 
ATOM   5539 C  CD2 . LEU B 1 337 ? -33.773 -9.549  47.995  1.00   68.59  ? 352 LEU B CD2 1 
ATOM   5540 N  N   . LEU B 1 338 ? -31.819 -5.310  46.018  1.00   67.46  ? 353 LEU B N   1 
ATOM   5541 C  CA  . LEU B 1 338 ? -30.557 -5.016  45.338  1.00   66.56  ? 353 LEU B CA  1 
ATOM   5542 C  C   . LEU B 1 338 ? -29.906 -3.806  45.971  1.00   64.88  ? 353 LEU B C   1 
ATOM   5543 O  O   . LEU B 1 338 ? -28.766 -3.892  46.416  1.00   64.17  ? 353 LEU B O   1 
ATOM   5544 C  CB  . LEU B 1 338 ? -30.758 -4.779  43.845  1.00   67.56  ? 353 LEU B CB  1 
ATOM   5545 C  CG  . LEU B 1 338 ? -29.538 -4.271  43.059  1.00   65.16  ? 353 LEU B CG  1 
ATOM   5546 C  CD1 . LEU B 1 338 ? -28.361 -5.217  43.184  1.00   64.76  ? 353 LEU B CD1 1 
ATOM   5547 C  CD2 . LEU B 1 338 ? -29.894 -4.095  41.598  1.00   66.67  ? 353 LEU B CD2 1 
ATOM   5548 N  N   . ASP B 1 339 ? -30.640 -2.700  46.048  1.00   65.60  ? 354 ASP B N   1 
ATOM   5549 C  CA  . ASP B 1 339 ? -30.150 -1.500  46.724  1.00   65.14  ? 354 ASP B CA  1 
ATOM   5550 C  C   . ASP B 1 339 ? -29.531 -1.829  48.091  1.00   62.92  ? 354 ASP B C   1 
ATOM   5551 O  O   . ASP B 1 339 ? -28.405 -1.436  48.392  1.00   57.97  ? 354 ASP B O   1 
ATOM   5552 C  CB  . ASP B 1 339 ? -31.286 -0.513  46.933  1.00   67.87  ? 354 ASP B CB  1 
ATOM   5553 C  CG  . ASP B 1 339 ? -30.816 0.769   47.567  1.00   68.25  ? 354 ASP B CG  1 
ATOM   5554 O  OD1 . ASP B 1 339 ? -30.186 0.703   48.636  1.00   70.31  ? 354 ASP B OD1 1 
ATOM   5555 O  OD2 . ASP B 1 339 ? -31.066 1.850   47.010  1.00   70.27  ? 354 ASP B OD2 1 
ATOM   5556 N  N   . ALA B 1 340 ? -30.304 -2.552  48.899  1.00   64.34  ? 355 ALA B N   1 
ATOM   5557 C  CA  . ALA B 1 340 ? -29.908 -2.939  50.244  1.00   63.06  ? 355 ALA B CA  1 
ATOM   5558 C  C   . ALA B 1 340 ? -28.596 -3.687  50.227  1.00   61.58  ? 355 ALA B C   1 
ATOM   5559 O  O   . ALA B 1 340 ? -27.754 -3.480  51.097  1.00   61.27  ? 355 ALA B O   1 
ATOM   5560 C  CB  . ALA B 1 340 ? -30.986 -3.789  50.890  1.00   65.19  ? 355 ALA B CB  1 
ATOM   5561 N  N   . VAL B 1 341 ? -28.404 -4.533  49.227  1.00   61.03  ? 356 VAL B N   1 
ATOM   5562 C  CA  . VAL B 1 341 ? -27.135 -5.235  49.094  1.00   60.01  ? 356 VAL B CA  1 
ATOM   5563 C  C   . VAL B 1 341 ? -25.952 -4.259  48.859  1.00   58.76  ? 356 VAL B C   1 
ATOM   5564 O  O   . VAL B 1 341 ? -24.954 -4.286  49.595  1.00   59.04  ? 356 VAL B O   1 
ATOM   5565 C  CB  . VAL B 1 341 ? -27.213 -6.332  48.009  1.00   59.53  ? 356 VAL B CB  1 
ATOM   5566 C  CG1 . VAL B 1 341 ? -25.830 -6.925  47.745  1.00   57.19  ? 356 VAL B CG1 1 
ATOM   5567 C  CG2 . VAL B 1 341 ? -28.216 -7.413  48.421  1.00   60.16  ? 356 VAL B CG2 1 
ATOM   5568 N  N   . LEU B 1 342 ? -26.063 -3.388  47.858  1.00   59.54  ? 357 LEU B N   1 
ATOM   5569 C  CA  . LEU B 1 342 ? -25.055 -2.322  47.637  1.00   57.05  ? 357 LEU B CA  1 
ATOM   5570 C  C   . LEU B 1 342 ? -24.777 -1.528  48.930  1.00   55.86  ? 357 LEU B C   1 
ATOM   5571 O  O   . LEU B 1 342 ? -23.665 -1.069  49.147  1.00   54.82  ? 357 LEU B O   1 
ATOM   5572 C  CB  . LEU B 1 342 ? -25.518 -1.355  46.532  1.00   57.27  ? 357 LEU B CB  1 
ATOM   5573 C  CG  . LEU B 1 342 ? -25.535 -1.928  45.117  1.00   58.15  ? 357 LEU B CG  1 
ATOM   5574 C  CD1 . LEU B 1 342 ? -26.433 -1.120  44.182  1.00   59.20  ? 357 LEU B CD1 1 
ATOM   5575 C  CD2 . LEU B 1 342 ? -24.103 -2.000  44.571  1.00   56.54  ? 357 LEU B CD2 1 
ATOM   5576 N  N   . CYS B 1 343 ? -25.794 -1.347  49.771  1.00   55.06  ? 358 CYS B N   1 
ATOM   5577 C  CA  . CYS B 1 343 ? -25.596 -0.617  50.986  1.00   54.98  ? 358 CYS B CA  1 
ATOM   5578 C  C   . CYS B 1 343 ? -24.786 -1.461  51.992  1.00   54.35  ? 358 CYS B C   1 
ATOM   5579 O  O   . CYS B 1 343 ? -23.756 -1.008  52.553  1.00   51.50  ? 358 CYS B O   1 
ATOM   5580 C  CB  . CYS B 1 343 ? -26.930 -0.190  51.558  1.00   57.10  ? 358 CYS B CB  1 
ATOM   5581 S  SG  . CYS B 1 343 ? -27.653 1.174   50.627  1.00   60.08  ? 358 CYS B SG  1 
ATOM   5582 N  N   . GLU B 1 344 ? -25.245 -2.695  52.192  1.00   53.57  ? 359 GLU B N   1 
ATOM   5583 C  CA  . GLU B 1 344 ? -24.598 -3.599  53.107  1.00   51.44  ? 359 GLU B CA  1 
ATOM   5584 C  C   . GLU B 1 344 ? -23.160 -3.810  52.667  1.00   50.93  ? 359 GLU B C   1 
ATOM   5585 O  O   . GLU B 1 344 ? -22.255 -3.881  53.523  1.00   48.96  ? 359 GLU B O   1 
ATOM   5586 C  CB  . GLU B 1 344 ? -25.343 -4.923  53.180  1.00   51.92  ? 359 GLU B CB  1 
ATOM   5587 C  CG  . GLU B 1 344 ? -24.694 -5.954  54.084  1.00   52.18  ? 359 GLU B CG  1 
ATOM   5588 C  CD  . GLU B 1 344 ? -24.828 -5.661  55.587  1.00   53.15  ? 359 GLU B CD  1 
ATOM   5589 O  OE1 . GLU B 1 344 ? -25.187 -4.529  55.995  1.00   52.95  ? 359 GLU B OE1 1 
ATOM   5590 O  OE2 . GLU B 1 344 ? -24.559 -6.577  56.411  1.00   53.11  ? 359 GLU B OE2 1 
ATOM   5591 N  N   . VAL B 1 345 ? -22.925 -3.896  51.350  1.00   50.55  ? 360 VAL B N   1 
ATOM   5592 C  CA  . VAL B 1 345 ? -21.547 -4.145  50.883  1.00   49.47  ? 360 VAL B CA  1 
ATOM   5593 C  C   . VAL B 1 345 ? -20.672 -2.953  51.259  1.00   47.93  ? 360 VAL B C   1 
ATOM   5594 O  O   . VAL B 1 345 ? -19.699 -3.124  51.985  1.00   47.21  ? 360 VAL B O   1 
ATOM   5595 C  CB  . VAL B 1 345 ? -21.428 -4.433  49.366  1.00   48.67  ? 360 VAL B CB  1 
ATOM   5596 C  CG1 . VAL B 1 345 ? -19.966 -4.510  48.966  1.00   46.61  ? 360 VAL B CG1 1 
ATOM   5597 C  CG2 . VAL B 1 345 ? -22.119 -5.739  49.015  1.00   49.81  ? 360 VAL B CG2 1 
ATOM   5598 N  N   . MET B 1 346 ? -21.051 -1.757  50.793  1.00   47.63  ? 361 MET B N   1 
ATOM   5599 C  CA  . MET B 1 346 ? -20.385 -0.506  51.198  1.00   46.83  ? 361 MET B CA  1 
ATOM   5600 C  C   . MET B 1 346 ? -20.152 -0.382  52.730  1.00   46.19  ? 361 MET B C   1 
ATOM   5601 O  O   . MET B 1 346 ? -19.190 0.253   53.186  1.00   43.77  ? 361 MET B O   1 
ATOM   5602 C  CB  . MET B 1 346 ? -21.179 0.708   50.690  1.00   48.22  ? 361 MET B CB  1 
ATOM   5603 C  CG  . MET B 1 346 ? -21.150 0.946   49.171  1.00   48.57  ? 361 MET B CG  1 
ATOM   5604 S  SD  . MET B 1 346 ? -22.251 2.278   48.576  1.00   50.67  ? 361 MET B SD  1 
ATOM   5605 C  CE  . MET B 1 346 ? -21.792 2.230   46.874  1.00   53.81  ? 361 MET B CE  1 
ATOM   5606 N  N   . ARG B 1 347 ? -21.043 -0.976  53.520  1.00   47.56  ? 362 ARG B N   1 
ATOM   5607 C  CA  . ARG B 1 347 ? -20.948 -0.899  54.969  1.00   48.07  ? 362 ARG B CA  1 
ATOM   5608 C  C   . ARG B 1 347 ? -19.916 -1.862  55.568  1.00   46.49  ? 362 ARG B C   1 
ATOM   5609 O  O   . ARG B 1 347 ? -19.132 -1.487  56.429  1.00   45.52  ? 362 ARG B O   1 
ATOM   5610 C  CB  . ARG B 1 347 ? -22.296 -1.208  55.553  1.00   51.26  ? 362 ARG B CB  1 
ATOM   5611 C  CG  . ARG B 1 347 ? -22.442 -0.903  57.025  1.00   53.53  ? 362 ARG B CG  1 
ATOM   5612 C  CD  . ARG B 1 347 ? -23.312 -1.947  57.719  1.00   56.17  ? 362 ARG B CD  1 
ATOM   5613 N  NE  . ARG B 1 347 ? -22.473 -2.903  58.446  1.00   56.84  ? 362 ARG B NE  1 
ATOM   5614 C  CZ  . ARG B 1 347 ? -22.669 -4.217  58.516  1.00   57.56  ? 362 ARG B CZ  1 
ATOM   5615 N  NH1 . ARG B 1 347 ? -23.760 -4.777  58.058  1.00   58.93  ? 362 ARG B NH1 1 
ATOM   5616 N  NH2 . ARG B 1 347 ? -21.741 -4.988  59.042  1.00   59.09  ? 362 ARG B NH2 1 
ATOM   5617 N  N   . ILE B 1 348 ? -19.925 -3.099  55.099  1.00   45.70  ? 363 ILE B N   1 
ATOM   5618 C  CA  . ILE B 1 348 ? -19.197 -4.174  55.734  1.00   44.92  ? 363 ILE B CA  1 
ATOM   5619 C  C   . ILE B 1 348 ? -17.732 -4.251  55.309  1.00   44.07  ? 363 ILE B C   1 
ATOM   5620 O  O   . ILE B 1 348 ? -16.933 -4.948  55.948  1.00   44.40  ? 363 ILE B O   1 
ATOM   5621 C  CB  . ILE B 1 348 ? -19.893 -5.518  55.453  1.00   46.06  ? 363 ILE B CB  1 
ATOM   5622 C  CG1 . ILE B 1 348 ? -19.582 -6.528  56.553  1.00   47.11  ? 363 ILE B CG1 1 
ATOM   5623 C  CG2 . ILE B 1 348 ? -19.493 -6.065  54.099  1.00   46.18  ? 363 ILE B CG2 1 
ATOM   5624 C  CD1 . ILE B 1 348 ? -20.252 -7.876  56.361  1.00   48.56  ? 363 ILE B CD1 1 
ATOM   5625 N  N   . ARG B 1 349 ? -17.372 -3.573  54.230  1.00   42.69  ? 364 ARG B N   1 
ATOM   5626 C  CA  . ARG B 1 349 ? -15.967 -3.489  53.822  1.00   41.63  ? 364 ARG B CA  1 
ATOM   5627 C  C   . ARG B 1 349 ? -15.684 -2.106  53.215  1.00   41.07  ? 364 ARG B C   1 
ATOM   5628 O  O   . ARG B 1 349 ? -15.464 -1.963  52.024  1.00   41.04  ? 364 ARG B O   1 
ATOM   5629 C  CB  . ARG B 1 349 ? -15.609 -4.588  52.810  1.00   41.55  ? 364 ARG B CB  1 
ATOM   5630 C  CG  . ARG B 1 349 ? -15.594 -6.010  53.353  1.00   42.18  ? 364 ARG B CG  1 
ATOM   5631 C  CD  . ARG B 1 349 ? -14.520 -6.240  54.412  1.00   41.84  ? 364 ARG B CD  1 
ATOM   5632 N  NE  . ARG B 1 349 ? -14.568 -7.627  54.902  1.00   42.97  ? 364 ARG B NE  1 
ATOM   5633 C  CZ  . ARG B 1 349 ? -15.376 -8.088  55.870  1.00   42.11  ? 364 ARG B CZ  1 
ATOM   5634 N  NH1 . ARG B 1 349 ? -16.230 -7.296  56.516  1.00   41.39  ? 364 ARG B NH1 1 
ATOM   5635 N  NH2 . ARG B 1 349 ? -15.307 -9.362  56.202  1.00   42.30  ? 364 ARG B NH2 1 
ATOM   5636 N  N   . PRO B 1 350 ? -15.695 -1.068  54.046  1.00   40.58  ? 365 PRO B N   1 
ATOM   5637 C  CA  . PRO B 1 350 ? -15.517 0.270   53.485  1.00   40.03  ? 365 PRO B CA  1 
ATOM   5638 C  C   . PRO B 1 350 ? -14.271 0.352   52.630  1.00   40.32  ? 365 PRO B C   1 
ATOM   5639 O  O   . PRO B 1 350 ? -13.285 -0.304  52.905  1.00   39.05  ? 365 PRO B O   1 
ATOM   5640 C  CB  . PRO B 1 350 ? -15.397 1.163   54.700  1.00   40.20  ? 365 PRO B CB  1 
ATOM   5641 C  CG  . PRO B 1 350 ? -15.558 0.294   55.915  1.00   40.06  ? 365 PRO B CG  1 
ATOM   5642 C  CD  . PRO B 1 350 ? -15.822 -1.108  55.506  1.00   39.95  ? 365 PRO B CD  1 
ATOM   5643 N  N   . VAL B 1 351 ? -14.330 1.109   51.548  1.00   43.43  ? 366 VAL B N   1 
ATOM   5644 C  CA  . VAL B 1 351 ? -13.169 1.196   50.638  1.00   43.16  ? 366 VAL B CA  1 
ATOM   5645 C  C   . VAL B 1 351 ? -12.051 2.073   51.216  1.00   42.21  ? 366 VAL B C   1 
ATOM   5646 O  O   . VAL B 1 351 ? -10.895 1.961   50.804  1.00   42.70  ? 366 VAL B O   1 
ATOM   5647 C  CB  . VAL B 1 351 ? -13.542 1.694   49.212  1.00   43.34  ? 366 VAL B CB  1 
ATOM   5648 C  CG1 . VAL B 1 351 ? -14.444 0.687   48.506  1.00   44.06  ? 366 VAL B CG1 1 
ATOM   5649 C  CG2 . VAL B 1 351 ? -14.174 3.082   49.245  1.00   43.52  ? 366 VAL B CG2 1 
ATOM   5650 N  N   . SER B 1 352 ? -12.411 2.967   52.131  1.00   41.97  ? 367 SER B N   1 
ATOM   5651 C  CA  . SER B 1 352 ? -11.426 3.713   52.898  1.00   41.94  ? 367 SER B CA  1 
ATOM   5652 C  C   . SER B 1 352 ? -11.816 3.520   54.349  1.00   41.12  ? 367 SER B C   1 
ATOM   5653 O  O   . SER B 1 352 ? -12.452 4.376   54.955  1.00   41.13  ? 367 SER B O   1 
ATOM   5654 C  CB  . SER B 1 352 ? -11.418 5.184   52.513  1.00   43.92  ? 367 SER B CB  1 
ATOM   5655 O  OG  . SER B 1 352 ? -11.378 5.329   51.094  1.00   46.91  ? 367 SER B OG  1 
ATOM   5656 N  N   . PRO B 1 353 ? -11.458 2.363   54.910  1.00   39.32  ? 368 PRO B N   1 
ATOM   5657 C  CA  . PRO B 1 353 ? -11.770 2.116   56.310  1.00   39.17  ? 368 PRO B CA  1 
ATOM   5658 C  C   . PRO B 1 353 ? -11.250 3.250   57.231  1.00   37.94  ? 368 PRO B C   1 
ATOM   5659 O  O   . PRO B 1 353 ? -11.771 3.431   58.346  1.00   38.20  ? 368 PRO B O   1 
ATOM   5660 C  CB  . PRO B 1 353 ? -11.037 0.801   56.617  1.00   40.12  ? 368 PRO B CB  1 
ATOM   5661 C  CG  . PRO B 1 353 ? -10.075 0.570   55.492  1.00   39.40  ? 368 PRO B CG  1 
ATOM   5662 C  CD  . PRO B 1 353 ? -10.402 1.486   54.369  1.00   38.50  ? 368 PRO B CD  1 
ATOM   5663 N  N   . ILE B 1 354 ? -10.217 3.967   56.774  1.00   35.48  ? 369 ILE B N   1 
ATOM   5664 C  CA  . ILE B 1 354 ? -9.870  5.272   57.303  1.00   35.16  ? 369 ILE B CA  1 
ATOM   5665 C  C   . ILE B 1 354 ? -9.869  6.287   56.172  1.00   34.84  ? 369 ILE B C   1 
ATOM   5666 O  O   . ILE B 1 354 ? -9.320  6.025   55.113  1.00   34.68  ? 369 ILE B O   1 
ATOM   5667 C  CB  . ILE B 1 354 ? -8.462  5.271   57.927  1.00   35.61  ? 369 ILE B CB  1 
ATOM   5668 C  CG1 . ILE B 1 354 ? -8.416  4.385   59.166  1.00   36.24  ? 369 ILE B CG1 1 
ATOM   5669 C  CG2 . ILE B 1 354 ? -8.045  6.681   58.303  1.00   35.85  ? 369 ILE B CG2 1 
ATOM   5670 C  CD1 . ILE B 1 354 ? -7.023  4.306   59.720  1.00   36.94  ? 369 ILE B CD1 1 
ATOM   5671 N  N   . LEU B 1 355 ? -10.458 7.459   56.395  1.00   34.92  ? 370 LEU B N   1 
ATOM   5672 C  CA  . LEU B 1 355 ? -10.565 8.463   55.333  1.00   34.91  ? 370 LEU B CA  1 
ATOM   5673 C  C   . LEU B 1 355 ? -9.259  9.244   55.063  1.00   35.76  ? 370 LEU B C   1 
ATOM   5674 O  O   . LEU B 1 355 ? -8.253  9.107   55.755  1.00   35.64  ? 370 LEU B O   1 
ATOM   5675 C  CB  . LEU B 1 355 ? -11.713 9.440   55.633  1.00   34.40  ? 370 LEU B CB  1 
ATOM   5676 C  CG  . LEU B 1 355 ? -13.075 8.786   55.877  1.00   34.78  ? 370 LEU B CG  1 
ATOM   5677 C  CD1 . LEU B 1 355 ? -14.226 9.801   55.832  1.00   35.59  ? 370 LEU B CD1 1 
ATOM   5678 C  CD2 . LEU B 1 355 ? -13.348 7.620   54.949  1.00   34.31  ? 370 LEU B CD2 1 
ATOM   5679 N  N   . ILE B 1 356 ? -9.297  10.090  54.049  1.00   37.21  ? 371 ILE B N   1 
ATOM   5680 C  CA  . ILE B 1 356 ? -8.208  11.006  53.836  1.00   38.35  ? 371 ILE B CA  1 
ATOM   5681 C  C   . ILE B 1 356 ? -8.187  11.934  55.032  1.00   38.50  ? 371 ILE B C   1 
ATOM   5682 O  O   . ILE B 1 356 ? -9.170  12.585  55.300  1.00   40.86  ? 371 ILE B O   1 
ATOM   5683 C  CB  . ILE B 1 356 ? -8.451  11.871  52.578  1.00   40.09  ? 371 ILE B CB  1 
ATOM   5684 C  CG1 . ILE B 1 356 ? -8.553  11.017  51.299  1.00   40.45  ? 371 ILE B CG1 1 
ATOM   5685 C  CG2 . ILE B 1 356 ? -7.334  12.892  52.403  1.00   40.55  ? 371 ILE B CG2 1 
ATOM   5686 C  CD1 . ILE B 1 356 ? -9.250  11.719  50.145  1.00   40.73  ? 371 ILE B CD1 1 
ATOM   5687 N  N   . PRO B 1 357 ? -7.072  12.031  55.746  1.00   39.06  ? 372 PRO B N   1 
ATOM   5688 C  CA  . PRO B 1 357 ? -6.986  13.057  56.804  1.00   39.50  ? 372 PRO B CA  1 
ATOM   5689 C  C   . PRO B 1 357 ? -7.850  14.317  56.571  1.00   41.14  ? 372 PRO B C   1 
ATOM   5690 O  O   . PRO B 1 357 ? -7.986  14.778  55.430  1.00   41.11  ? 372 PRO B O   1 
ATOM   5691 C  CB  . PRO B 1 357 ? -5.505  13.448  56.762  1.00   38.98  ? 372 PRO B CB  1 
ATOM   5692 C  CG  . PRO B 1 357 ? -4.809  12.207  56.336  1.00   38.44  ? 372 PRO B CG  1 
ATOM   5693 C  CD  . PRO B 1 357 ? -5.773  11.367  55.530  1.00   38.47  ? 372 PRO B CD  1 
ATOM   5694 N  N   . HIS B 1 358 ? -8.426  14.843  57.650  1.00   42.50  ? 373 HIS B N   1 
ATOM   5695 C  CA  . HIS B 1 358 ? -9.140  16.119  57.646  1.00   44.24  ? 373 HIS B CA  1 
ATOM   5696 C  C   . HIS B 1 358 ? -8.374  17.056  58.528  1.00   46.07  ? 373 HIS B C   1 
ATOM   5697 O  O   . HIS B 1 358 ? -8.361  16.858  59.732  1.00   51.04  ? 373 HIS B O   1 
ATOM   5698 C  CB  . HIS B 1 358 ? -10.513 15.963  58.276  1.00   44.22  ? 373 HIS B CB  1 
ATOM   5699 C  CG  . HIS B 1 358 ? -11.563 15.514  57.329  1.00   44.61  ? 373 HIS B CG  1 
ATOM   5700 N  ND1 . HIS B 1 358 ? -11.494 14.304  56.676  1.00   44.07  ? 373 HIS B ND1 1 
ATOM   5701 C  CD2 . HIS B 1 358 ? -12.711 16.107  56.915  1.00   45.96  ? 373 HIS B CD2 1 
ATOM   5702 C  CE1 . HIS B 1 358 ? -12.559 14.167  55.902  1.00   44.47  ? 373 HIS B CE1 1 
ATOM   5703 N  NE2 . HIS B 1 358 ? -13.310 15.249  56.022  1.00   45.27  ? 373 HIS B NE2 1 
ATOM   5704 N  N   . VAL B 1 359 ? -7.757  18.082  57.969  1.00   45.89  ? 374 VAL B N   1 
ATOM   5705 C  CA  . VAL B 1 359 ? -6.906  18.962  58.750  1.00   44.73  ? 374 VAL B CA  1 
ATOM   5706 C  C   . VAL B 1 359 ? -7.719  20.087  59.382  1.00   46.42  ? 374 VAL B C   1 
ATOM   5707 O  O   . VAL B 1 359 ? -8.662  20.615  58.805  1.00   46.30  ? 374 VAL B O   1 
ATOM   5708 C  CB  . VAL B 1 359 ? -5.781  19.553  57.897  1.00   44.46  ? 374 VAL B CB  1 
ATOM   5709 C  CG1 . VAL B 1 359 ? -4.747  20.268  58.766  1.00   44.49  ? 374 VAL B CG1 1 
ATOM   5710 C  CG2 . VAL B 1 359 ? -5.127  18.452  57.080  1.00   44.14  ? 374 VAL B CG2 1 
ATOM   5711 N  N   . ALA B 1 360 ? -7.346  20.453  60.591  1.00   47.72  ? 375 ALA B N   1 
ATOM   5712 C  CA  . ALA B 1 360 ? -7.990  21.546  61.225  1.00   50.74  ? 375 ALA B CA  1 
ATOM   5713 C  C   . ALA B 1 360 ? -7.471  22.768  60.501  1.00   53.09  ? 375 ALA B C   1 
ATOM   5714 O  O   . ALA B 1 360 ? -6.269  23.017  60.516  1.00   54.12  ? 375 ALA B O   1 
ATOM   5715 C  CB  . ALA B 1 360 ? -7.647  21.580  62.712  1.00   51.59  ? 375 ALA B CB  1 
ATOM   5716 N  N   . MET B 1 361 ? -8.362  23.507  59.839  1.00   55.85  ? 376 MET B N   1 
ATOM   5717 C  CA  . MET B 1 361 ? -7.993  24.766  59.181  1.00   57.54  ? 376 MET B CA  1 
ATOM   5718 C  C   . MET B 1 361 ? -7.828  25.906  60.183  1.00   57.61  ? 376 MET B C   1 
ATOM   5719 O  O   . MET B 1 361 ? -7.362  26.988  59.819  1.00   57.34  ? 376 MET B O   1 
ATOM   5720 C  CB  . MET B 1 361 ? -9.047  25.178  58.161  1.00   60.94  ? 376 MET B CB  1 
ATOM   5721 C  CG  . MET B 1 361 ? -9.347  24.153  57.066  1.00   63.12  ? 376 MET B CG  1 
ATOM   5722 S  SD  . MET B 1 361 ? -8.705  24.428  55.392  1.00   66.29  ? 376 MET B SD  1 
ATOM   5723 C  CE  . MET B 1 361 ? -8.607  26.216  55.262  1.00   68.18  ? 376 MET B CE  1 
ATOM   5724 N  N   . GLN B 1 362 ? -8.243  25.686  61.431  1.00   57.36  ? 377 GLN B N   1 
ATOM   5725 C  CA  . GLN B 1 362 ? -7.975  26.645  62.515  1.00   58.11  ? 377 GLN B CA  1 
ATOM   5726 C  C   . GLN B 1 362 ? -8.076  26.000  63.889  1.00   55.54  ? 377 GLN B C   1 
ATOM   5727 O  O   . GLN B 1 362 ? -8.386  24.818  64.021  1.00   53.44  ? 377 GLN B O   1 
ATOM   5728 C  CB  . GLN B 1 362 ? -8.946  27.819  62.429  1.00   61.62  ? 377 GLN B CB  1 
ATOM   5729 C  CG  . GLN B 1 362 ? -10.375 27.458  62.790  1.00   63.33  ? 377 GLN B CG  1 
ATOM   5730 C  CD  . GLN B 1 362 ? -11.398 28.322  62.077  1.00   66.31  ? 377 GLN B CD  1 
ATOM   5731 O  OE1 . GLN B 1 362 ? -11.393 28.420  60.852  1.00   69.07  ? 377 GLN B OE1 1 
ATOM   5732 N  NE2 . GLN B 1 362 ? -12.297 28.928  62.836  1.00   67.75  ? 377 GLN B NE2 1 
ATOM   5733 N  N   . ASP B 1 363 ? -7.810  26.781  64.923  1.00   55.37  ? 378 ASP B N   1 
ATOM   5734 C  CA  . ASP B 1 363 ? -8.048  26.292  66.265  1.00   54.65  ? 378 ASP B CA  1 
ATOM   5735 C  C   . ASP B 1 363 ? -9.514  25.987  66.380  1.00   54.24  ? 378 ASP B C   1 
ATOM   5736 O  O   . ASP B 1 363 ? -10.366 26.702  65.847  1.00   55.66  ? 378 ASP B O   1 
ATOM   5737 C  CB  . ASP B 1 363 ? -7.631  27.304  67.309  1.00   56.17  ? 378 ASP B CB  1 
ATOM   5738 C  CG  . ASP B 1 363 ? -6.139  27.440  67.400  1.00   56.42  ? 378 ASP B CG  1 
ATOM   5739 O  OD1 . ASP B 1 363 ? -5.432  26.707  66.673  1.00   55.65  ? 378 ASP B OD1 1 
ATOM   5740 O  OD2 . ASP B 1 363 ? -5.675  28.286  68.190  1.00   57.75  ? 378 ASP B OD2 1 
ATOM   5741 N  N   . THR B 1 364 ? -9.802  24.904  67.066  1.00   52.40  ? 379 THR B N   1 
ATOM   5742 C  CA  . THR B 1 364 ? -11.112 24.317  67.019  1.00   52.55  ? 379 THR B CA  1 
ATOM   5743 C  C   . THR B 1 364 ? -11.178 23.346  68.186  1.00   52.53  ? 379 THR B C   1 
ATOM   5744 O  O   . THR B 1 364 ? -10.168 23.103  68.860  1.00   52.26  ? 379 THR B O   1 
ATOM   5745 C  CB  . THR B 1 364 ? -11.350 23.637  65.629  1.00   51.41  ? 379 THR B CB  1 
ATOM   5746 O  OG1 . THR B 1 364 ? -12.657 23.062  65.548  1.00   51.51  ? 379 THR B OG1 1 
ATOM   5747 C  CG2 . THR B 1 364 ? -10.355 22.552  65.357  1.00   49.92  ? 379 THR B CG2 1 
ATOM   5748 N  N   . SER B 1 365 ? -12.360 22.822  68.466  1.00   52.09  ? 380 SER B N   1 
ATOM   5749 C  CA  . SER B 1 365 ? -12.457 21.792  69.463  1.00   51.61  ? 380 SER B CA  1 
ATOM   5750 C  C   . SER B 1 365 ? -12.865 20.535  68.767  1.00   48.58  ? 380 SER B C   1 
ATOM   5751 O  O   . SER B 1 365 ? -13.307 20.577  67.646  1.00   46.94  ? 380 SER B O   1 
ATOM   5752 C  CB  . SER B 1 365 ? -13.457 22.190  70.565  1.00   55.04  ? 380 SER B CB  1 
ATOM   5753 O  OG  . SER B 1 365 ? -14.473 21.197  70.784  1.00   56.61  ? 380 SER B OG  1 
ATOM   5754 N  N   . LEU B 1 366 ? -12.689 19.414  69.442  1.00   47.48  ? 381 LEU B N   1 
ATOM   5755 C  CA  . LEU B 1 366 ? -13.309 18.174  69.025  1.00   47.08  ? 381 LEU B CA  1 
ATOM   5756 C  C   . LEU B 1 366 ? -13.619 17.386  70.294  1.00   47.77  ? 381 LEU B C   1 
ATOM   5757 O  O   . LEU B 1 366 ? -12.765 17.305  71.177  1.00   47.48  ? 381 LEU B O   1 
ATOM   5758 C  CB  . LEU B 1 366 ? -12.349 17.423  68.134  1.00   45.73  ? 381 LEU B CB  1 
ATOM   5759 C  CG  . LEU B 1 366 ? -12.844 16.265  67.283  1.00   45.07  ? 381 LEU B CG  1 
ATOM   5760 C  CD1 . LEU B 1 366 ? -11.622 15.521  66.760  1.00   43.83  ? 381 LEU B CD1 1 
ATOM   5761 C  CD2 . LEU B 1 366 ? -13.755 15.307  68.001  1.00   45.28  ? 381 LEU B CD2 1 
ATOM   5762 N  N   . GLY B 1 367 ? -14.823 16.826  70.418  1.00   47.81  ? 382 GLY B N   1 
ATOM   5763 C  CA  . GLY B 1 367 ? -15.198 16.250  71.684  1.00   49.51  ? 382 GLY B CA  1 
ATOM   5764 C  C   . GLY B 1 367 ? -15.034 17.404  72.660  1.00   51.35  ? 382 GLY B C   1 
ATOM   5765 O  O   . GLY B 1 367 ? -15.131 18.550  72.242  1.00   54.00  ? 382 GLY B O   1 
ATOM   5766 N  N   . GLY B 1 368 ? -14.744 17.156  73.925  1.00   51.26  ? 383 GLY B N   1 
ATOM   5767 C  CA  . GLY B 1 368 ? -14.533 18.283  74.846  1.00   53.66  ? 383 GLY B CA  1 
ATOM   5768 C  C   . GLY B 1 368 ? -13.295 19.179  74.655  1.00   53.43  ? 383 GLY B C   1 
ATOM   5769 O  O   . GLY B 1 368 ? -13.159 20.211  75.311  1.00   55.42  ? 383 GLY B O   1 
ATOM   5770 N  N   . HIS B 1 369 ? -12.412 18.821  73.730  1.00   51.26  ? 384 HIS B N   1 
ATOM   5771 C  CA  . HIS B 1 369 ? -11.019 19.204  73.820  1.00   50.04  ? 384 HIS B CA  1 
ATOM   5772 C  C   . HIS B 1 369 ? -10.533 20.093  72.699  1.00   49.58  ? 384 HIS B C   1 
ATOM   5773 O  O   . HIS B 1 369 ? -10.948 19.942  71.547  1.00   50.57  ? 384 HIS B O   1 
ATOM   5774 C  CB  . HIS B 1 369 ? -10.220 17.927  73.812  1.00   49.16  ? 384 HIS B CB  1 
ATOM   5775 C  CG  . HIS B 1 369 ? -10.804 16.877  74.692  1.00   49.85  ? 384 HIS B CG  1 
ATOM   5776 N  ND1 . HIS B 1 369 ? -10.398 16.697  75.994  1.00   50.79  ? 384 HIS B ND1 1 
ATOM   5777 C  CD2 . HIS B 1 369 ? -11.803 15.988  74.477  1.00   49.99  ? 384 HIS B CD2 1 
ATOM   5778 C  CE1 . HIS B 1 369 ? -11.104 15.719  76.532  1.00   51.26  ? 384 HIS B CE1 1 
ATOM   5779 N  NE2 . HIS B 1 369 ? -11.966 15.274  75.634  1.00   50.11  ? 384 HIS B NE2 1 
ATOM   5780 N  N   . SER B 1 370 ? -9.643  21.017  73.040  1.00   49.21  ? 385 SER B N   1 
ATOM   5781 C  CA  . SER B 1 370 ? -9.102  21.936  72.077  1.00   48.98  ? 385 SER B CA  1 
ATOM   5782 C  C   . SER B 1 370 ? -8.314  21.151  71.058  1.00   48.41  ? 385 SER B C   1 
ATOM   5783 O  O   . SER B 1 370 ? -7.823  20.075  71.338  1.00   48.90  ? 385 SER B O   1 
ATOM   5784 C  CB  . SER B 1 370 ? -8.214  22.974  72.735  1.00   49.79  ? 385 SER B CB  1 
ATOM   5785 O  OG  . SER B 1 370 ? -7.415  23.616  71.759  1.00   49.52  ? 385 SER B OG  1 
ATOM   5786 N  N   . VAL B 1 371 ? -8.241  21.686  69.854  1.00   48.40  ? 386 VAL B N   1 
ATOM   5787 C  CA  . VAL B 1 371 ? -7.661  20.993  68.734  1.00   46.67  ? 386 VAL B CA  1 
ATOM   5788 C  C   . VAL B 1 371 ? -6.995  22.103  67.946  1.00   47.07  ? 386 VAL B C   1 
ATOM   5789 O  O   . VAL B 1 371 ? -7.682  22.900  67.326  1.00   47.22  ? 386 VAL B O   1 
ATOM   5790 C  CB  . VAL B 1 371 ? -8.748  20.266  67.946  1.00   46.02  ? 386 VAL B CB  1 
ATOM   5791 C  CG1 . VAL B 1 371 ? -8.296  19.976  66.522  1.00   45.11  ? 386 VAL B CG1 1 
ATOM   5792 C  CG2 . VAL B 1 371 ? -9.120  18.981  68.673  1.00   45.40  ? 386 VAL B CG2 1 
ATOM   5793 N  N   . PRO B 1 372 ? -5.653  22.210  68.048  1.00   47.29  ? 387 PRO B N   1 
ATOM   5794 C  CA  . PRO B 1 372 ? -4.927  23.304  67.412  1.00   47.27  ? 387 PRO B CA  1 
ATOM   5795 C  C   . PRO B 1 372 ? -4.999  23.202  65.924  1.00   45.78  ? 387 PRO B C   1 
ATOM   5796 O  O   . PRO B 1 372 ? -5.144  22.122  65.388  1.00   43.60  ? 387 PRO B O   1 
ATOM   5797 C  CB  . PRO B 1 372 ? -3.470  23.080  67.836  1.00   47.32  ? 387 PRO B CB  1 
ATOM   5798 C  CG  . PRO B 1 372 ? -3.493  22.057  68.917  1.00   47.05  ? 387 PRO B CG  1 
ATOM   5799 C  CD  . PRO B 1 372 ? -4.743  21.272  68.734  1.00   46.69  ? 387 PRO B CD  1 
ATOM   5800 N  N   . LYS B 1 373 ? -4.892  24.335  65.270  1.00   47.05  ? 388 LYS B N   1 
ATOM   5801 C  CA  . LYS B 1 373 ? -4.733  24.359  63.836  1.00   48.24  ? 388 LYS B CA  1 
ATOM   5802 C  C   . LYS B 1 373 ? -3.519  23.506  63.362  1.00   47.76  ? 388 LYS B C   1 
ATOM   5803 O  O   . LYS B 1 373 ? -2.418  23.523  63.956  1.00   48.48  ? 388 LYS B O   1 
ATOM   5804 C  CB  . LYS B 1 373 ? -4.555  25.805  63.404  1.00   50.46  ? 388 LYS B CB  1 
ATOM   5805 C  CG  . LYS B 1 373 ? -4.452  26.016  61.906  1.00   51.20  ? 388 LYS B CG  1 
ATOM   5806 C  CD  . LYS B 1 373 ? -3.829  27.361  61.623  1.00   52.64  ? 388 LYS B CD  1 
ATOM   5807 C  CE  . LYS B 1 373 ? -3.996  27.743  60.179  1.00   53.66  ? 388 LYS B CE  1 
ATOM   5808 N  NZ  . LYS B 1 373 ? -3.416  29.095  60.006  1.00   56.34  ? 388 LYS B NZ  1 
ATOM   5809 N  N   . GLY B 1 374 ? -3.719  22.754  62.291  1.00   45.93  ? 389 GLY B N   1 
ATOM   5810 C  CA  . GLY B 1 374 ? -2.671  21.893  61.785  1.00   44.55  ? 389 GLY B CA  1 
ATOM   5811 C  C   . GLY B 1 374 ? -2.942  20.463  62.143  1.00   43.21  ? 389 GLY B C   1 
ATOM   5812 O  O   . GLY B 1 374 ? -2.402  19.579  61.529  1.00   42.95  ? 389 GLY B O   1 
ATOM   5813 N  N   . THR B 1 375 ? -3.801  20.226  63.119  1.00   44.12  ? 390 THR B N   1 
ATOM   5814 C  CA  . THR B 1 375 ? -4.104  18.871  63.554  1.00   44.37  ? 390 THR B CA  1 
ATOM   5815 C  C   . THR B 1 375 ? -4.799  18.091  62.467  1.00   45.34  ? 390 THR B C   1 
ATOM   5816 O  O   . THR B 1 375 ? -5.578  18.639  61.697  1.00   45.23  ? 390 THR B O   1 
ATOM   5817 C  CB  . THR B 1 375 ? -5.050  18.874  64.765  1.00   44.12  ? 390 THR B CB  1 
ATOM   5818 O  OG1 . THR B 1 375 ? -4.479  19.671  65.800  1.00   46.80  ? 390 THR B OG1 1 
ATOM   5819 C  CG2 . THR B 1 375 ? -5.290  17.471  65.283  1.00   42.75  ? 390 THR B CG2 1 
ATOM   5820 N  N   . ARG B 1 376 ? -4.549  16.791  62.456  1.00   47.16  ? 391 ARG B N   1 
ATOM   5821 C  CA  . ARG B 1 376 ? -5.108  15.893  61.460  1.00   48.01  ? 391 ARG B CA  1 
ATOM   5822 C  C   . ARG B 1 376 ? -6.032  14.910  62.122  1.00   45.68  ? 391 ARG B C   1 
ATOM   5823 O  O   . ARG B 1 376 ? -5.739  14.418  63.221  1.00   48.36  ? 391 ARG B O   1 
ATOM   5824 C  CB  . ARG B 1 376 ? -3.962  15.158  60.782  1.00   49.33  ? 391 ARG B CB  1 
ATOM   5825 C  CG  . ARG B 1 376 ? -3.046  16.148  60.122  1.00   52.86  ? 391 ARG B CG  1 
ATOM   5826 C  CD  . ARG B 1 376 ? -1.701  15.561  59.852  1.00   58.50  ? 391 ARG B CD  1 
ATOM   5827 N  NE  . ARG B 1 376 ? -0.920  16.513  59.078  1.00   64.64  ? 391 ARG B NE  1 
ATOM   5828 C  CZ  . ARG B 1 376 ? 0.180   16.204  58.405  1.00   71.09  ? 391 ARG B CZ  1 
ATOM   5829 N  NH1 . ARG B 1 376 ? 0.653   14.954  58.420  1.00   72.42  ? 391 ARG B NH1 1 
ATOM   5830 N  NH2 . ARG B 1 376 ? 0.806   17.156  57.714  1.00   75.35  ? 391 ARG B NH2 1 
ATOM   5831 N  N   . VAL B 1 377 ? -7.136  14.611  61.458  1.00   42.03  ? 392 VAL B N   1 
ATOM   5832 C  CA  . VAL B 1 377 ? -8.131  13.750  62.036  1.00   40.13  ? 392 VAL B CA  1 
ATOM   5833 C  C   . VAL B 1 377 ? -8.411  12.604  61.078  1.00   38.91  ? 392 VAL B C   1 
ATOM   5834 O  O   . VAL B 1 377 ? -8.840  12.793  59.942  1.00   41.87  ? 392 VAL B O   1 
ATOM   5835 C  CB  . VAL B 1 377 ? -9.406  14.546  62.365  1.00   40.76  ? 392 VAL B CB  1 
ATOM   5836 C  CG1 . VAL B 1 377 ? -10.444 13.645  62.985  1.00   41.03  ? 392 VAL B CG1 1 
ATOM   5837 C  CG2 . VAL B 1 377 ? -9.096  15.681  63.329  1.00   41.41  ? 392 VAL B CG2 1 
ATOM   5838 N  N   . LEU B 1 378 ? -8.163  11.399  61.533  1.00   37.01  ? 393 LEU B N   1 
ATOM   5839 C  CA  . LEU B 1 378 ? -8.431  10.228  60.747  1.00   35.60  ? 393 LEU B CA  1 
ATOM   5840 C  C   . LEU B 1 378 ? -9.778  9.641   61.148  1.00   35.40  ? 393 LEU B C   1 
ATOM   5841 O  O   . LEU B 1 378 ? -9.936  9.109   62.231  1.00   34.46  ? 393 LEU B O   1 
ATOM   5842 C  CB  . LEU B 1 378 ? -7.322  9.190   60.947  1.00   34.77  ? 393 LEU B CB  1 
ATOM   5843 C  CG  . LEU B 1 378 ? -5.930  9.695   60.641  1.00   34.90  ? 393 LEU B CG  1 
ATOM   5844 C  CD1 . LEU B 1 378 ? -4.946  8.556   60.813  1.00   35.08  ? 393 LEU B CD1 1 
ATOM   5845 C  CD2 . LEU B 1 378 ? -5.791  10.278  59.244  1.00   35.09  ? 393 LEU B CD2 1 
ATOM   5846 N  N   . VAL B 1 379 ? -10.746 9.691   60.240  1.00   35.51  ? 394 VAL B N   1 
ATOM   5847 C  CA  . VAL B 1 379 ? -12.049 9.136   60.544  1.00   35.08  ? 394 VAL B CA  1 
ATOM   5848 C  C   . VAL B 1 379 ? -11.985 7.662   60.349  1.00   35.00  ? 394 VAL B C   1 
ATOM   5849 O  O   . VAL B 1 379 ? -11.679 7.226   59.276  1.00   35.15  ? 394 VAL B O   1 
ATOM   5850 C  CB  . VAL B 1 379 ? -13.117 9.739   59.659  1.00   35.13  ? 394 VAL B CB  1 
ATOM   5851 C  CG1 . VAL B 1 379 ? -14.391 8.911   59.717  1.00   36.07  ? 394 VAL B CG1 1 
ATOM   5852 C  CG2 . VAL B 1 379 ? -13.359 11.189  60.058  1.00   35.51  ? 394 VAL B CG2 1 
ATOM   5853 N  N   . ASN B 1 380 ? -12.217 6.902   61.409  1.00   36.36  ? 395 ASN B N   1 
ATOM   5854 C  CA  . ASN B 1 380 ? -12.234 5.444   61.330  1.00   37.17  ? 395 ASN B CA  1 
ATOM   5855 C  C   . ASN B 1 380 ? -13.621 5.007   60.881  1.00   38.59  ? 395 ASN B C   1 
ATOM   5856 O  O   . ASN B 1 380 ? -14.521 4.694   61.674  1.00   39.99  ? 395 ASN B O   1 
ATOM   5857 C  CB  . ASN B 1 380 ? -11.831 4.763   62.663  1.00   36.96  ? 395 ASN B CB  1 
ATOM   5858 C  CG  . ASN B 1 380 ? -11.608 3.259   62.509  1.00   36.28  ? 395 ASN B CG  1 
ATOM   5859 O  OD1 . ASN B 1 380 ? -11.884 2.697   61.467  1.00   36.18  ? 395 ASN B OD1 1 
ATOM   5860 N  ND2 . ASN B 1 380 ? -11.108 2.611   63.541  1.00   36.48  ? 395 ASN B ND2 1 
ATOM   5861 N  N   . MET B 1 381 ? -13.759 4.982   59.578  1.00   39.26  ? 396 MET B N   1 
ATOM   5862 C  CA  . MET B 1 381 ? -14.959 4.537   58.908  1.00   41.15  ? 396 MET B CA  1 
ATOM   5863 C  C   . MET B 1 381 ? -15.206 3.062   59.188  1.00   40.07  ? 396 MET B C   1 
ATOM   5864 O  O   . MET B 1 381 ? -16.347 2.588   59.080  1.00   40.77  ? 396 MET B O   1 
ATOM   5865 C  CB  . MET B 1 381 ? -14.763 4.738   57.412  1.00   43.57  ? 396 MET B CB  1 
ATOM   5866 C  CG  . MET B 1 381 ? -15.968 4.494   56.562  1.00   48.39  ? 396 MET B CG  1 
ATOM   5867 S  SD  . MET B 1 381 ? -16.579 6.067   55.946  1.00   57.73  ? 396 MET B SD  1 
ATOM   5868 C  CE  . MET B 1 381 ? -16.932 6.883   57.509  1.00   54.10  ? 396 MET B CE  1 
ATOM   5869 N  N   . TRP B 1 382 ? -14.153 2.309   59.505  1.00   38.06  ? 397 TRP B N   1 
ATOM   5870 C  CA  . TRP B 1 382 ? -14.382 0.920   59.833  1.00   38.33  ? 397 TRP B CA  1 
ATOM   5871 C  C   . TRP B 1 382 ? -15.186 0.886   61.137  1.00   39.77  ? 397 TRP B C   1 
ATOM   5872 O  O   . TRP B 1 382 ? -16.246 0.288   61.229  1.00   41.41  ? 397 TRP B O   1 
ATOM   5873 C  CB  . TRP B 1 382 ? -13.083 0.145   59.985  1.00   37.31  ? 397 TRP B CB  1 
ATOM   5874 C  CG  . TRP B 1 382 ? -13.361 -1.268  60.364  1.00   38.16  ? 397 TRP B CG  1 
ATOM   5875 C  CD1 . TRP B 1 382 ? -13.489 -1.755  61.620  1.00   38.99  ? 397 TRP B CD1 1 
ATOM   5876 C  CD2 . TRP B 1 382 ? -13.614 -2.371  59.480  1.00   38.65  ? 397 TRP B CD2 1 
ATOM   5877 N  NE1 . TRP B 1 382 ? -13.784 -3.098  61.589  1.00   39.57  ? 397 TRP B NE1 1 
ATOM   5878 C  CE2 . TRP B 1 382 ? -13.852 -3.507  60.286  1.00   39.44  ? 397 TRP B CE2 1 
ATOM   5879 C  CE3 . TRP B 1 382 ? -13.637 -2.519  58.084  1.00   38.34  ? 397 TRP B CE3 1 
ATOM   5880 C  CZ2 . TRP B 1 382 ? -14.127 -4.777  59.744  1.00   39.93  ? 397 TRP B CZ2 1 
ATOM   5881 C  CZ3 . TRP B 1 382 ? -13.899 -3.780  57.549  1.00   38.66  ? 397 TRP B CZ3 1 
ATOM   5882 C  CH2 . TRP B 1 382 ? -14.148 -4.893  58.382  1.00   39.26  ? 397 TRP B CH2 1 
ATOM   5883 N  N   . ALA B 1 383 ? -14.672 1.592   62.132  1.00   39.84  ? 398 ALA B N   1 
ATOM   5884 C  CA  . ALA B 1 383 ? -15.192 1.561   63.459  1.00   40.10  ? 398 ALA B CA  1 
ATOM   5885 C  C   . ALA B 1 383 ? -16.668 1.896   63.430  1.00   40.62  ? 398 ALA B C   1 
ATOM   5886 O  O   . ALA B 1 383 ? -17.493 1.109   63.876  1.00   41.13  ? 398 ALA B O   1 
ATOM   5887 C  CB  . ALA B 1 383 ? -14.426 2.555   64.309  1.00   40.45  ? 398 ALA B CB  1 
ATOM   5888 N  N   . ILE B 1 384 ? -17.006 3.036   62.853  1.00   40.17  ? 399 ILE B N   1 
ATOM   5889 C  CA  . ILE B 1 384 ? -18.381 3.447   62.874  1.00   41.99  ? 399 ILE B CA  1 
ATOM   5890 C  C   . ILE B 1 384 ? -19.298 2.480   62.126  1.00   42.38  ? 399 ILE B C   1 
ATOM   5891 O  O   . ILE B 1 384 ? -20.465 2.377   62.456  1.00   43.43  ? 399 ILE B O   1 
ATOM   5892 C  CB  . ILE B 1 384 ? -18.594 4.884   62.380  1.00   42.54  ? 399 ILE B CB  1 
ATOM   5893 C  CG1 . ILE B 1 384 ? -18.400 4.966   60.871  1.00   43.06  ? 399 ILE B CG1 1 
ATOM   5894 C  CG2 . ILE B 1 384 ? -17.680 5.837   63.140  1.00   41.87  ? 399 ILE B CG2 1 
ATOM   5895 C  CD1 . ILE B 1 384 ? -18.598 6.359   60.317  1.00   43.86  ? 399 ILE B CD1 1 
ATOM   5896 N  N   . HIS B 1 385 ? -18.783 1.747   61.150  1.00   41.89  ? 400 HIS B N   1 
ATOM   5897 C  CA  . HIS B 1 385 ? -19.650 0.821   60.397  1.00   42.77  ? 400 HIS B CA  1 
ATOM   5898 C  C   . HIS B 1 385 ? -19.797 -0.547  61.027  1.00   42.46  ? 400 HIS B C   1 
ATOM   5899 O  O   . HIS B 1 385 ? -20.678 -1.336  60.589  1.00   42.62  ? 400 HIS B O   1 
ATOM   5900 C  CB  . HIS B 1 385 ? -19.129 0.614   58.973  1.00   42.59  ? 400 HIS B CB  1 
ATOM   5901 C  CG  . HIS B 1 385 ? -19.543 1.678   58.015  1.00   42.90  ? 400 HIS B CG  1 
ATOM   5902 N  ND1 . HIS B 1 385 ? -19.331 1.565   56.657  1.00   42.99  ? 400 HIS B ND1 1 
ATOM   5903 C  CD2 . HIS B 1 385 ? -20.141 2.875   58.208  1.00   43.44  ? 400 HIS B CD2 1 
ATOM   5904 C  CE1 . HIS B 1 385 ? -19.771 2.655   56.056  1.00   43.52  ? 400 HIS B CE1 1 
ATOM   5905 N  NE2 . HIS B 1 385 ? -20.274 3.462   56.972  1.00   43.86  ? 400 HIS B NE2 1 
ATOM   5906 N  N   . HIS B 1 386 ? -18.914 -0.845  61.986  1.00   41.20  ? 401 HIS B N   1 
ATOM   5907 C  CA  . HIS B 1 386 ? -18.893 -2.152  62.635  1.00   42.05  ? 401 HIS B CA  1 
ATOM   5908 C  C   . HIS B 1 386 ? -19.250 -2.111  64.122  1.00   43.35  ? 401 HIS B C   1 
ATOM   5909 O  O   . HIS B 1 386 ? -19.237 -3.131  64.829  1.00   44.19  ? 401 HIS B O   1 
ATOM   5910 C  CB  . HIS B 1 386 ? -17.538 -2.788  62.430  1.00   40.98  ? 401 HIS B CB  1 
ATOM   5911 C  CG  . HIS B 1 386 ? -17.417 -3.550  61.154  1.00   40.99  ? 401 HIS B CG  1 
ATOM   5912 N  ND1 . HIS B 1 386 ? -17.171 -2.939  59.936  1.00   40.55  ? 401 HIS B ND1 1 
ATOM   5913 C  CD2 . HIS B 1 386 ? -17.481 -4.878  60.905  1.00   41.66  ? 401 HIS B CD2 1 
ATOM   5914 C  CE1 . HIS B 1 386 ? -17.087 -3.857  58.992  1.00   40.48  ? 401 HIS B CE1 1 
ATOM   5915 N  NE2 . HIS B 1 386 ? -17.287 -5.040  59.549  1.00   41.95  ? 401 HIS B NE2 1 
ATOM   5916 N  N   . ASP B 1 387 ? -19.619 -0.923  64.568  1.00   43.98  ? 402 ASP B N   1 
ATOM   5917 C  CA  . ASP B 1 387 ? -19.846 -0.619  65.977  1.00   44.67  ? 402 ASP B CA  1 
ATOM   5918 C  C   . ASP B 1 387 ? -21.072 -1.349  66.544  1.00   46.14  ? 402 ASP B C   1 
ATOM   5919 O  O   . ASP B 1 387 ? -22.205 -1.018  66.182  1.00   47.15  ? 402 ASP B O   1 
ATOM   5920 C  CB  . ASP B 1 387 ? -20.041 0.892   66.056  1.00   44.49  ? 402 ASP B CB  1 
ATOM   5921 C  CG  . ASP B 1 387 ? -20.105 1.393   67.438  1.00   45.38  ? 402 ASP B CG  1 
ATOM   5922 O  OD1 . ASP B 1 387 ? -20.580 0.650   68.325  1.00   46.33  ? 402 ASP B OD1 1 
ATOM   5923 O  OD2 . ASP B 1 387 ? -19.702 2.562   67.605  1.00   45.05  ? 402 ASP B OD2 1 
ATOM   5924 N  N   . PRO B 1 388 ? -20.869 -2.314  67.465  1.00   46.78  ? 403 PRO B N   1 
ATOM   5925 C  CA  . PRO B 1 388 ? -22.037 -3.087  67.940  1.00   48.34  ? 403 PRO B CA  1 
ATOM   5926 C  C   . PRO B 1 388 ? -23.018 -2.291  68.744  1.00   49.55  ? 403 PRO B C   1 
ATOM   5927 O  O   . PRO B 1 388 ? -24.072 -2.794  69.061  1.00   51.43  ? 403 PRO B O   1 
ATOM   5928 C  CB  . PRO B 1 388 ? -21.438 -4.203  68.800  1.00   48.36  ? 403 PRO B CB  1 
ATOM   5929 C  CG  . PRO B 1 388 ? -20.080 -3.762  69.139  1.00   47.40  ? 403 PRO B CG  1 
ATOM   5930 C  CD  . PRO B 1 388 ? -19.640 -2.684  68.175  1.00   46.14  ? 403 PRO B CD  1 
ATOM   5931 N  N   . LYS B 1 389 ? -22.704 -1.052  69.063  1.00   49.57  ? 404 LYS B N   1 
ATOM   5932 C  CA  . LYS B 1 389 ? -23.664 -0.242  69.774  1.00   52.02  ? 404 LYS B CA  1 
ATOM   5933 C  C   . LYS B 1 389 ? -24.690 0.345   68.804  1.00   52.00  ? 404 LYS B C   1 
ATOM   5934 O  O   . LYS B 1 389 ? -25.745 0.754   69.240  1.00   53.99  ? 404 LYS B O   1 
ATOM   5935 C  CB  . LYS B 1 389 ? -22.951 0.844   70.609  1.00   52.95  ? 404 LYS B CB  1 
ATOM   5936 C  CG  . LYS B 1 389 ? -23.875 1.708   71.456  1.00   55.74  ? 404 LYS B CG  1 
ATOM   5937 C  CD  . LYS B 1 389 ? -23.177 2.676   72.412  1.00   55.75  ? 404 LYS B CD  1 
ATOM   5938 C  CE  . LYS B 1 389 ? -24.228 3.474   73.198  1.00   58.08  ? 404 LYS B CE  1 
ATOM   5939 N  NZ  . LYS B 1 389 ? -24.066 3.338   74.681  1.00   60.08  ? 404 LYS B NZ  1 
ATOM   5940 N  N   . HIS B 1 390 ? -24.391 0.375   67.502  1.00   50.59  ? 405 HIS B N   1 
ATOM   5941 C  CA  . HIS B 1 390 ? -25.319 0.928   66.490  1.00   50.34  ? 405 HIS B CA  1 
ATOM   5942 C  C   . HIS B 1 390 ? -25.695 -0.037  65.387  1.00   50.73  ? 405 HIS B C   1 
ATOM   5943 O  O   . HIS B 1 390 ? -26.535 0.286   64.554  1.00   50.76  ? 405 HIS B O   1 
ATOM   5944 C  CB  . HIS B 1 390 ? -24.762 2.198   65.860  1.00   48.41  ? 405 HIS B CB  1 
ATOM   5945 C  CG  . HIS B 1 390 ? -24.471 3.271   66.859  1.00   48.72  ? 405 HIS B CG  1 
ATOM   5946 N  ND1 . HIS B 1 390 ? -25.461 3.938   67.544  1.00   50.51  ? 405 HIS B ND1 1 
ATOM   5947 C  CD2 . HIS B 1 390 ? -23.303 3.760   67.325  1.00   47.05  ? 405 HIS B CD2 1 
ATOM   5948 C  CE1 . HIS B 1 390 ? -24.919 4.823   68.353  1.00   49.78  ? 405 HIS B CE1 1 
ATOM   5949 N  NE2 . HIS B 1 390 ? -23.610 4.741   68.228  1.00   48.38  ? 405 HIS B NE2 1 
ATOM   5950 N  N   . TRP B 1 391 ? -25.114 -1.227  65.389  1.00   51.19  ? 406 TRP B N   1 
ATOM   5951 C  CA  . TRP B 1 391 ? -25.436 -2.214  64.375  1.00   52.55  ? 406 TRP B CA  1 
ATOM   5952 C  C   . TRP B 1 391 ? -25.605 -3.559  65.025  1.00   55.26  ? 406 TRP B C   1 
ATOM   5953 O  O   . TRP B 1 391 ? -24.759 -3.943  65.837  1.00   54.92  ? 406 TRP B O   1 
ATOM   5954 C  CB  . TRP B 1 391 ? -24.292 -2.343  63.371  1.00   50.13  ? 406 TRP B CB  1 
ATOM   5955 C  CG  . TRP B 1 391 ? -23.967 -1.127  62.598  1.00   49.09  ? 406 TRP B CG  1 
ATOM   5956 C  CD1 . TRP B 1 391 ? -22.919 -0.273  62.814  1.00   48.31  ? 406 TRP B CD1 1 
ATOM   5957 C  CD2 . TRP B 1 391 ? -24.644 -0.643  61.439  1.00   49.91  ? 406 TRP B CD2 1 
ATOM   5958 N  NE1 . TRP B 1 391 ? -22.916 0.732   61.865  1.00   47.99  ? 406 TRP B NE1 1 
ATOM   5959 C  CE2 . TRP B 1 391 ? -23.960 0.524   61.005  1.00   49.32  ? 406 TRP B CE2 1 
ATOM   5960 C  CE3 . TRP B 1 391 ? -25.759 -1.077  60.723  1.00   51.11  ? 406 TRP B CE3 1 
ATOM   5961 C  CZ2 . TRP B 1 391 ? -24.357 1.255   59.885  1.00   49.98  ? 406 TRP B CZ2 1 
ATOM   5962 C  CZ3 . TRP B 1 391 ? -26.159 -0.351  59.632  1.00   52.13  ? 406 TRP B CZ3 1 
ATOM   5963 C  CH2 . TRP B 1 391 ? -25.456 0.808   59.212  1.00   51.37  ? 406 TRP B CH2 1 
ATOM   5964 N  N   . ASP B 1 392 ? -26.659 -4.288  64.654  1.00   59.22  ? 407 ASP B N   1 
ATOM   5965 C  CA  . ASP B 1 392 ? -26.859 -5.635  65.187  1.00   64.25  ? 407 ASP B CA  1 
ATOM   5966 C  C   . ASP B 1 392 ? -26.058 -6.631  64.404  1.00   64.44  ? 407 ASP B C   1 
ATOM   5967 O  O   . ASP B 1 392 ? -26.207 -6.706  63.202  1.00   66.28  ? 407 ASP B O   1 
ATOM   5968 C  CB  . ASP B 1 392 ? -28.313 -6.065  65.131  1.00   68.78  ? 407 ASP B CB  1 
ATOM   5969 C  CG  . ASP B 1 392 ? -28.569 -7.303  65.960  1.00   72.79  ? 407 ASP B CG  1 
ATOM   5970 O  OD1 . ASP B 1 392 ? -28.562 -7.158  67.208  1.00   78.94  ? 407 ASP B OD1 1 
ATOM   5971 O  OD2 . ASP B 1 392 ? -28.766 -8.403  65.387  1.00   73.09  ? 407 ASP B OD2 1 
ATOM   5972 N  N   . GLN B 1 393 ? -25.244 -7.421  65.090  1.00   66.63  ? 408 GLN B N   1 
ATOM   5973 C  CA  . GLN B 1 393 ? -24.338 -8.362  64.440  1.00   67.41  ? 408 GLN B CA  1 
ATOM   5974 C  C   . GLN B 1 393 ? -23.630 -7.728  63.220  1.00   64.52  ? 408 GLN B C   1 
ATOM   5975 O  O   . GLN B 1 393 ? -23.719 -8.233  62.073  1.00   63.86  ? 408 GLN B O   1 
ATOM   5976 C  CB  . GLN B 1 393 ? -25.080 -9.651  64.073  1.00   71.92  ? 408 GLN B CB  1 
ATOM   5977 C  CG  . GLN B 1 393 ? -25.521 -10.466 65.294  1.00   77.46  ? 408 GLN B CG  1 
ATOM   5978 C  CD  . GLN B 1 393 ? -25.729 -11.947 64.986  1.00   80.76  ? 408 GLN B CD  1 
ATOM   5979 O  OE1 . GLN B 1 393 ? -25.339 -12.431 63.921  1.00   84.46  ? 408 GLN B OE1 1 
ATOM   5980 N  NE2 . GLN B 1 393 ? -26.348 -12.670 65.916  1.00   81.91  ? 408 GLN B NE2 1 
ATOM   5981 N  N   . PRO B 1 394 ? -22.899 -6.625  63.472  1.00   60.26  ? 409 PRO B N   1 
ATOM   5982 C  CA  . PRO B 1 394 ? -22.190 -5.882  62.424  1.00   57.81  ? 409 PRO B CA  1 
ATOM   5983 C  C   . PRO B 1 394 ? -21.202 -6.727  61.611  1.00   56.22  ? 409 PRO B C   1 
ATOM   5984 O  O   . PRO B 1 394 ? -20.758 -6.315  60.548  1.00   53.39  ? 409 PRO B O   1 
ATOM   5985 C  CB  . PRO B 1 394 ? -21.432 -4.803  63.211  1.00   56.43  ? 409 PRO B CB  1 
ATOM   5986 C  CG  . PRO B 1 394 ? -21.361 -5.302  64.603  1.00   57.16  ? 409 PRO B CG  1 
ATOM   5987 C  CD  . PRO B 1 394 ? -22.587 -6.121  64.816  1.00   59.43  ? 409 PRO B CD  1 
ATOM   5988 N  N   . GLU B 1 395 ? -20.854 -7.894  62.126  1.00   57.99  ? 410 GLU B N   1 
ATOM   5989 C  CA  . GLU B 1 395 ? -19.879 -8.755  61.494  1.00   58.41  ? 410 GLU B CA  1 
ATOM   5990 C  C   . GLU B 1 395 ? -20.527 -9.777  60.551  1.00   58.59  ? 410 GLU B C   1 
ATOM   5991 O  O   . GLU B 1 395 ? -19.872 -10.309 59.676  1.00   57.27  ? 410 GLU B O   1 
ATOM   5992 C  CB  . GLU B 1 395 ? -18.968 -9.401  62.560  1.00   59.72  ? 410 GLU B CB  1 
ATOM   5993 C  CG  . GLU B 1 395 ? -19.602 -10.485 63.420  1.00   63.44  ? 410 GLU B CG  1 
ATOM   5994 C  CD  . GLU B 1 395 ? -20.944 -10.086 64.045  1.00   66.77  ? 410 GLU B CD  1 
ATOM   5995 O  OE1 . GLU B 1 395 ? -21.064 -8.968  64.599  1.00   65.39  ? 410 GLU B OE1 1 
ATOM   5996 O  OE2 . GLU B 1 395 ? -21.904 -10.895 63.973  1.00   72.13  ? 410 GLU B OE2 1 
ATOM   5997 N  N   . GLN B 1 396 ? -21.817 -10.050 60.693  1.00   61.85  ? 411 GLN B N   1 
ATOM   5998 C  CA  . GLN B 1 396 ? -22.465 -10.907 59.704  1.00   62.33  ? 411 GLN B CA  1 
ATOM   5999 C  C   . GLN B 1 396 ? -23.021 -10.075 58.526  1.00   59.96  ? 411 GLN B C   1 
ATOM   6000 O  O   . GLN B 1 396 ? -23.443 -8.932  58.704  1.00   58.41  ? 411 GLN B O   1 
ATOM   6001 C  CB  . GLN B 1 396 ? -23.518 -11.794 60.359  1.00   65.23  ? 411 GLN B CB  1 
ATOM   6002 C  CG  . GLN B 1 396 ? -23.849 -12.997 59.480  1.00   68.77  ? 411 GLN B CG  1 
ATOM   6003 C  CD  . GLN B 1 396 ? -24.432 -14.183 60.230  1.00   72.18  ? 411 GLN B CD  1 
ATOM   6004 O  OE1 . GLN B 1 396 ? -24.681 -14.115 61.445  1.00   75.17  ? 411 GLN B OE1 1 
ATOM   6005 N  NE2 . GLN B 1 396 ? -24.655 -15.287 59.509  1.00   71.25  ? 411 GLN B NE2 1 
ATOM   6006 N  N   . PHE B 1 397 ? -22.981 -10.631 57.319  1.00   58.89  ? 412 PHE B N   1 
ATOM   6007 C  CA  . PHE B 1 397 ? -23.428 -9.884  56.142  1.00   61.08  ? 412 PHE B CA  1 
ATOM   6008 C  C   . PHE B 1 397 ? -24.970 -9.999  55.928  1.00   62.98  ? 412 PHE B C   1 
ATOM   6009 O  O   . PHE B 1 397 ? -25.466 -11.003 55.402  1.00   63.66  ? 412 PHE B O   1 
ATOM   6010 C  CB  . PHE B 1 397 ? -22.648 -10.354 54.905  1.00   62.43  ? 412 PHE B CB  1 
ATOM   6011 C  CG  . PHE B 1 397 ? -23.028 -9.646  53.632  1.00   63.41  ? 412 PHE B CG  1 
ATOM   6012 C  CD1 . PHE B 1 397 ? -22.430 -8.453  53.289  1.00   64.49  ? 412 PHE B CD1 1 
ATOM   6013 C  CD2 . PHE B 1 397 ? -23.970 -10.169 52.791  1.00   64.13  ? 412 PHE B CD2 1 
ATOM   6014 C  CE1 . PHE B 1 397 ? -22.765 -7.794  52.122  1.00   64.32  ? 412 PHE B CE1 1 
ATOM   6015 C  CE2 . PHE B 1 397 ? -24.321 -9.514  51.630  1.00   66.41  ? 412 PHE B CE2 1 
ATOM   6016 C  CZ  . PHE B 1 397 ? -23.717 -8.327  51.291  1.00   65.37  ? 412 PHE B CZ  1 
ATOM   6017 N  N   . ASN B 1 398 ? -25.711 -8.957  56.320  1.00   62.34  ? 413 ASN B N   1 
ATOM   6018 C  CA  . ASN B 1 398 ? -27.177 -8.981  56.303  1.00   63.39  ? 413 ASN B CA  1 
ATOM   6019 C  C   . ASN B 1 398 ? -27.884 -7.724  55.725  1.00   64.15  ? 413 ASN B C   1 
ATOM   6020 O  O   . ASN B 1 398 ? -28.313 -6.847  56.486  1.00   64.42  ? 413 ASN B O   1 
ATOM   6021 C  CB  . ASN B 1 398 ? -27.703 -9.275  57.710  1.00   63.56  ? 413 ASN B CB  1 
ATOM   6022 C  CG  . ASN B 1 398 ? -29.139 -9.758  57.696  1.00   65.58  ? 413 ASN B CG  1 
ATOM   6023 O  OD1 . ASN B 1 398 ? -29.707 -9.972  56.619  1.00   66.31  ? 413 ASN B OD1 1 
ATOM   6024 N  ND2 . ASN B 1 398 ? -29.737 -9.934  58.878  1.00   65.53  ? 413 ASN B ND2 1 
ATOM   6025 N  N   . PRO B 1 399 ? -28.056 -7.663  54.380  1.00   64.55  ? 414 PRO B N   1 
ATOM   6026 C  CA  . PRO B 1 399 ? -28.784 -6.558  53.690  1.00   65.00  ? 414 PRO B CA  1 
ATOM   6027 C  C   . PRO B 1 399 ? -30.177 -6.213  54.264  1.00   65.83  ? 414 PRO B C   1 
ATOM   6028 O  O   . PRO B 1 399 ? -30.669 -5.090  54.105  1.00   64.47  ? 414 PRO B O   1 
ATOM   6029 C  CB  . PRO B 1 399 ? -28.930 -7.060  52.240  1.00   64.73  ? 414 PRO B CB  1 
ATOM   6030 C  CG  . PRO B 1 399 ? -27.970 -8.176  52.076  1.00   64.01  ? 414 PRO B CG  1 
ATOM   6031 C  CD  . PRO B 1 399 ? -27.579 -8.695  53.434  1.00   64.29  ? 414 PRO B CD  1 
ATOM   6032 N  N   . GLU B 1 400 ? -30.806 -7.169  54.927  1.00   67.29  ? 415 GLU B N   1 
ATOM   6033 C  CA  . GLU B 1 400 ? -32.119 -6.913  55.500  1.00   71.53  ? 415 GLU B CA  1 
ATOM   6034 C  C   . GLU B 1 400 ? -32.073 -5.830  56.575  1.00   69.98  ? 415 GLU B C   1 
ATOM   6035 O  O   . GLU B 1 400 ? -33.083 -5.192  56.849  1.00   71.75  ? 415 GLU B O   1 
ATOM   6036 C  CB  . GLU B 1 400 ? -32.768 -8.210  56.022  1.00   75.16  ? 415 GLU B CB  1 
ATOM   6037 C  CG  . GLU B 1 400 ? -33.711 -8.865  55.017  1.00   78.71  ? 415 GLU B CG  1 
ATOM   6038 C  CD  . GLU B 1 400 ? -33.507 -10.361 54.884  1.00   81.98  ? 415 GLU B CD  1 
ATOM   6039 O  OE1 . GLU B 1 400 ? -32.367 -10.782 54.567  1.00   84.77  ? 415 GLU B OE1 1 
ATOM   6040 O  OE2 . GLU B 1 400 ? -34.493 -11.112 55.053  1.00   84.43  ? 415 GLU B OE2 1 
ATOM   6041 N  N   . ARG B 1 401 ? -30.900 -5.595  57.151  1.00   67.37  ? 416 ARG B N   1 
ATOM   6042 C  CA  . ARG B 1 401 ? -30.736 -4.538  58.139  1.00   64.97  ? 416 ARG B CA  1 
ATOM   6043 C  C   . ARG B 1 401 ? -31.110 -3.162  57.560  1.00   65.04  ? 416 ARG B C   1 
ATOM   6044 O  O   . ARG B 1 401 ? -31.456 -2.250  58.311  1.00   64.41  ? 416 ARG B O   1 
ATOM   6045 C  CB  . ARG B 1 401 ? -29.305 -4.543  58.673  1.00   61.74  ? 416 ARG B CB  1 
ATOM   6046 C  CG  . ARG B 1 401 ? -28.330 -3.721  57.856  1.00   59.95  ? 416 ARG B CG  1 
ATOM   6047 C  CD  . ARG B 1 401 ? -26.877 -4.149  58.028  1.00   57.74  ? 416 ARG B CD  1 
ATOM   6048 N  NE  . ARG B 1 401 ? -26.566 -4.650  59.372  1.00   57.95  ? 416 ARG B NE  1 
ATOM   6049 C  CZ  . ARG B 1 401 ? -26.059 -5.854  59.645  1.00   56.94  ? 416 ARG B CZ  1 
ATOM   6050 N  NH1 . ARG B 1 401 ? -25.770 -6.703  58.673  1.00   56.88  ? 416 ARG B NH1 1 
ATOM   6051 N  NH2 . ARG B 1 401 ? -25.816 -6.207  60.896  1.00   56.02  ? 416 ARG B NH2 1 
ATOM   6052 N  N   . PHE B 1 402 ? -31.023 -3.023  56.232  1.00   65.43  ? 417 PHE B N   1 
ATOM   6053 C  CA  . PHE B 1 402 ? -31.484 -1.821  55.527  1.00   66.65  ? 417 PHE B CA  1 
ATOM   6054 C  C   . PHE B 1 402 ? -32.923 -1.960  55.041  1.00   72.25  ? 417 PHE B C   1 
ATOM   6055 O  O   . PHE B 1 402 ? -33.497 -1.017  54.495  1.00   71.45  ? 417 PHE B O   1 
ATOM   6056 C  CB  . PHE B 1 402 ? -30.588 -1.531  54.345  1.00   63.76  ? 417 PHE B CB  1 
ATOM   6057 C  CG  . PHE B 1 402 ? -29.198 -1.162  54.731  1.00   61.53  ? 417 PHE B CG  1 
ATOM   6058 C  CD1 . PHE B 1 402 ? -28.237 -2.142  54.918  1.00   59.58  ? 417 PHE B CD1 1 
ATOM   6059 C  CD2 . PHE B 1 402 ? -28.848 0.170   54.925  1.00   60.57  ? 417 PHE B CD2 1 
ATOM   6060 C  CE1 . PHE B 1 402 ? -26.956 -1.801  55.294  1.00   57.43  ? 417 PHE B CE1 1 
ATOM   6061 C  CE2 . PHE B 1 402 ? -27.568 0.514   55.293  1.00   58.16  ? 417 PHE B CE2 1 
ATOM   6062 C  CZ  . PHE B 1 402 ? -26.618 -0.474  55.477  1.00   57.14  ? 417 PHE B CZ  1 
ATOM   6063 N  N   . LEU B 1 403 ? -33.490 -3.147  55.222  1.00   77.80  ? 418 LEU B N   1 
ATOM   6064 C  CA  . LEU B 1 403 ? -34.923 -3.345  55.056  1.00   84.38  ? 418 LEU B CA  1 
ATOM   6065 C  C   . LEU B 1 403 ? -35.706 -3.148  56.354  1.00   93.12  ? 418 LEU B C   1 
ATOM   6066 O  O   . LEU B 1 403 ? -35.819 -4.033  57.216  1.00   94.67  ? 418 LEU B O   1 
ATOM   6067 C  CB  . LEU B 1 403 ? -35.230 -4.707  54.440  1.00   82.23  ? 418 LEU B CB  1 
ATOM   6068 C  CG  . LEU B 1 403 ? -34.703 -4.825  53.020  1.00   79.32  ? 418 LEU B CG  1 
ATOM   6069 C  CD1 . LEU B 1 403 ? -35.025 -6.208  52.492  1.00   79.63  ? 418 LEU B CD1 1 
ATOM   6070 C  CD2 . LEU B 1 403 ? -35.279 -3.732  52.125  1.00   79.65  ? 418 LEU B CD2 1 
ATOM   6071 N  N   . GLU B 1 404 ? -36.145 -1.910  56.507  1.00   101.39 ? 419 GLU B N   1 
ATOM   6072 C  CA  . GLU B 1 404 ? -37.469 -1.599  57.024  1.00   105.89 ? 419 GLU B CA  1 
ATOM   6073 C  C   . GLU B 1 404 ? -38.150 -0.767  55.930  1.00   108.04 ? 419 GLU B C   1 
ATOM   6074 O  O   . GLU B 1 404 ? -39.346 -0.929  55.682  1.00   113.97 ? 419 GLU B O   1 
ATOM   6075 C  CB  . GLU B 1 404 ? -37.388 -0.846  58.350  1.00   105.92 ? 419 GLU B CB  1 
ATOM   6076 C  CG  . GLU B 1 404 ? -38.674 -0.887  59.158  1.00   108.74 ? 419 GLU B CG  1 
ATOM   6077 C  CD  . GLU B 1 404 ? -38.396 -1.000  60.640  1.00   108.24 ? 419 GLU B CD  1 
ATOM   6078 O  OE1 . GLU B 1 404 ? -37.929 -2.070  61.068  1.00   106.38 ? 419 GLU B OE1 1 
ATOM   6079 O  OE2 . GLU B 1 404 ? -38.636 -0.027  61.379  1.00   111.16 ? 419 GLU B OE2 1 
ATOM   6080 N  N   . PRO B 1 405 ? -37.369 0.113   55.285  1.00   105.18 ? 420 PRO B N   1 
ATOM   6081 C  CA  . PRO B 1 405 ? -37.769 0.839   54.083  1.00   104.50 ? 420 PRO B CA  1 
ATOM   6082 C  C   . PRO B 1 405 ? -37.373 0.046   52.842  1.00   106.51 ? 420 PRO B C   1 
ATOM   6083 O  O   . PRO B 1 405 ? -36.199 -0.317  52.671  1.00   102.88 ? 420 PRO B O   1 
ATOM   6084 C  CB  . PRO B 1 405 ? -37.103 2.207   54.063  1.00   101.69 ? 420 PRO B CB  1 
ATOM   6085 N  N   . GLN B 1 412 ? -27.962 2.599   61.329  1.00   90.95  ? 427 GLN B N   1 
ATOM   6086 C  CA  . GLN B 1 412 ? -28.373 2.997   59.981  1.00   91.52  ? 427 GLN B CA  1 
ATOM   6087 C  C   . GLN B 1 412 ? -28.567 4.513   59.876  1.00   89.77  ? 427 GLN B C   1 
ATOM   6088 O  O   . GLN B 1 412 ? -29.132 5.006   58.901  1.00   94.53  ? 427 GLN B O   1 
ATOM   6089 C  CB  . GLN B 1 412 ? -29.648 2.263   59.533  1.00   94.40  ? 427 GLN B CB  1 
ATOM   6090 C  CG  . GLN B 1 412 ? -29.516 0.748   59.423  1.00   95.92  ? 427 GLN B CG  1 
ATOM   6091 C  CD  . GLN B 1 412 ? -29.583 0.025   60.769  1.00   99.37  ? 427 GLN B CD  1 
ATOM   6092 O  OE1 . GLN B 1 412 ? -29.709 0.648   61.826  1.00   103.61 ? 427 GLN B OE1 1 
ATOM   6093 N  NE2 . GLN B 1 412 ? -29.503 -1.302  60.731  1.00   100.19 ? 427 GLN B NE2 1 
ATOM   6094 N  N   . SER B 1 413 ? -28.143 5.237   60.905  1.00   84.99  ? 428 SER B N   1 
ATOM   6095 C  CA  . SER B 1 413 ? -27.880 6.671   60.801  1.00   83.36  ? 428 SER B CA  1 
ATOM   6096 C  C   . SER B 1 413 ? -26.383 6.933   61.023  1.00   79.85  ? 428 SER B C   1 
ATOM   6097 O  O   . SER B 1 413 ? -25.870 7.990   60.666  1.00   82.76  ? 428 SER B O   1 
ATOM   6098 C  CB  . SER B 1 413 ? -28.703 7.454   61.829  1.00   86.39  ? 428 SER B CB  1 
ATOM   6099 O  OG  . SER B 1 413 ? -28.031 7.533   63.079  1.00   83.13  ? 428 SER B OG  1 
ATOM   6100 N  N   . SER B 1 414 ? -25.686 5.984   61.643  1.00   71.81  ? 429 SER B N   1 
ATOM   6101 C  CA  . SER B 1 414 ? -24.247 6.014   61.685  1.00   64.28  ? 429 SER B CA  1 
ATOM   6102 C  C   . SER B 1 414 ? -23.781 5.232   60.467  1.00   61.18  ? 429 SER B C   1 
ATOM   6103 O  O   . SER B 1 414 ? -23.185 4.165   60.564  1.00   58.25  ? 429 SER B O   1 
ATOM   6104 C  CB  . SER B 1 414 ? -23.729 5.425   63.005  1.00   63.33  ? 429 SER B CB  1 
ATOM   6105 O  OG  . SER B 1 414 ? -23.997 4.050   63.106  1.00   62.92  ? 429 SER B OG  1 
ATOM   6106 N  N   . PHE B 1 415 ? -24.090 5.786   59.307  1.00   60.57  ? 430 PHE B N   1 
ATOM   6107 C  CA  . PHE B 1 415 ? -23.852 5.132   58.040  1.00   59.41  ? 430 PHE B CA  1 
ATOM   6108 C  C   . PHE B 1 415 ? -23.504 6.244   57.083  1.00   58.67  ? 430 PHE B C   1 
ATOM   6109 O  O   . PHE B 1 415 ? -24.367 7.037   56.695  1.00   58.17  ? 430 PHE B O   1 
ATOM   6110 C  CB  . PHE B 1 415 ? -25.091 4.374   57.573  1.00   61.42  ? 430 PHE B CB  1 
ATOM   6111 C  CG  . PHE B 1 415 ? -24.991 3.855   56.168  1.00   61.24  ? 430 PHE B CG  1 
ATOM   6112 C  CD1 . PHE B 1 415 ? -24.151 2.787   55.867  1.00   61.69  ? 430 PHE B CD1 1 
ATOM   6113 C  CD2 . PHE B 1 415 ? -25.726 4.430   55.141  1.00   61.69  ? 430 PHE B CD2 1 
ATOM   6114 C  CE1 . PHE B 1 415 ? -24.040 2.306   54.557  1.00   61.15  ? 430 PHE B CE1 1 
ATOM   6115 C  CE2 . PHE B 1 415 ? -25.613 3.956   53.830  1.00   62.36  ? 430 PHE B CE2 1 
ATOM   6116 C  CZ  . PHE B 1 415 ? -24.780 2.886   53.542  1.00   60.13  ? 430 PHE B CZ  1 
ATOM   6117 N  N   . LEU B 1 416 ? -22.213 6.332   56.779  1.00   56.22  ? 431 LEU B N   1 
ATOM   6118 C  CA  . LEU B 1 416 ? -21.674 7.353   55.910  1.00   55.56  ? 431 LEU B CA  1 
ATOM   6119 C  C   . LEU B 1 416 ? -20.651 6.748   54.959  1.00   54.68  ? 431 LEU B C   1 
ATOM   6120 O  O   . LEU B 1 416 ? -19.447 6.864   55.174  1.00   53.55  ? 431 LEU B O   1 
ATOM   6121 C  CB  . LEU B 1 416 ? -21.031 8.447   56.743  1.00   54.72  ? 431 LEU B CB  1 
ATOM   6122 C  CG  . LEU B 1 416 ? -21.945 9.112   57.761  1.00   56.61  ? 431 LEU B CG  1 
ATOM   6123 C  CD1 . LEU B 1 416 ? -21.097 9.811   58.821  1.00   57.93  ? 431 LEU B CD1 1 
ATOM   6124 C  CD2 . LEU B 1 416 ? -22.888 10.083  57.091  1.00   57.15  ? 431 LEU B CD2 1 
ATOM   6125 N  N   . PRO B 1 417 ? -21.131 6.113   53.879  1.00   54.82  ? 432 PRO B N   1 
ATOM   6126 C  CA  . PRO B 1 417 ? -20.235 5.421   52.957  1.00   51.93  ? 432 PRO B CA  1 
ATOM   6127 C  C   . PRO B 1 417 ? -19.417 6.364   52.070  1.00   50.52  ? 432 PRO B C   1 
ATOM   6128 O  O   . PRO B 1 417 ? -18.307 6.012   51.640  1.00   51.63  ? 432 PRO B O   1 
ATOM   6129 C  CB  . PRO B 1 417 ? -21.188 4.562   52.132  1.00   53.13  ? 432 PRO B CB  1 
ATOM   6130 C  CG  . PRO B 1 417 ? -22.491 5.283   52.170  1.00   55.64  ? 432 PRO B CG  1 
ATOM   6131 C  CD  . PRO B 1 417 ? -22.543 6.044   53.458  1.00   56.17  ? 432 PRO B CD  1 
ATOM   6132 N  N   . PHE B 1 418 ? -19.948 7.549   51.807  1.00   49.69  ? 433 PHE B N   1 
ATOM   6133 C  CA  . PHE B 1 418 ? -19.295 8.512   50.928  1.00   48.61  ? 433 PHE B CA  1 
ATOM   6134 C  C   . PHE B 1 418 ? -18.830 9.731   51.709  1.00   47.52  ? 433 PHE B C   1 
ATOM   6135 O  O   . PHE B 1 418 ? -18.388 10.723  51.105  1.00   47.95  ? 433 PHE B O   1 
ATOM   6136 C  CB  . PHE B 1 418 ? -20.278 8.977   49.834  1.00   50.51  ? 433 PHE B CB  1 
ATOM   6137 C  CG  . PHE B 1 418 ? -20.703 7.886   48.889  1.00   50.75  ? 433 PHE B CG  1 
ATOM   6138 C  CD1 . PHE B 1 418 ? -19.904 7.551   47.794  1.00   50.00  ? 433 PHE B CD1 1 
ATOM   6139 C  CD2 . PHE B 1 418 ? -21.903 7.200   49.085  1.00   50.76  ? 433 PHE B CD2 1 
ATOM   6140 C  CE1 . PHE B 1 418 ? -20.288 6.549   46.929  1.00   49.77  ? 433 PHE B CE1 1 
ATOM   6141 C  CE2 . PHE B 1 418 ? -22.290 6.193   48.227  1.00   50.61  ? 433 PHE B CE2 1 
ATOM   6142 C  CZ  . PHE B 1 418 ? -21.483 5.872   47.150  1.00   51.04  ? 433 PHE B CZ  1 
ATOM   6143 N  N   . GLY B 1 419 ? -18.947 9.674   53.039  1.00   45.87  ? 434 GLY B N   1 
ATOM   6144 C  CA  . GLY B 1 419 ? -18.515 10.776  53.892  1.00   45.17  ? 434 GLY B CA  1 
ATOM   6145 C  C   . GLY B 1 419 ? -19.672 11.739  54.093  1.00   46.91  ? 434 GLY B C   1 
ATOM   6146 O  O   . GLY B 1 419 ? -20.834 11.390  53.840  1.00   48.74  ? 434 GLY B O   1 
ATOM   6147 N  N   . ALA B 1 420 ? -19.354 12.948  54.551  1.00   45.79  ? 435 ALA B N   1 
ATOM   6148 C  CA  . ALA B 1 420 ? -20.357 13.939  54.869  1.00   45.91  ? 435 ALA B CA  1 
ATOM   6149 C  C   . ALA B 1 420 ? -19.755 15.334  55.033  1.00   46.30  ? 435 ALA B C   1 
ATOM   6150 O  O   . ALA B 1 420 ? -18.521 15.516  55.263  1.00   45.82  ? 435 ALA B O   1 
ATOM   6151 C  CB  . ALA B 1 420 ? -21.096 13.533  56.121  1.00   45.76  ? 435 ALA B CB  1 
ATOM   6152 N  N   . GLY B 1 421 ? -20.636 16.326  54.933  1.00   46.79  ? 436 GLY B N   1 
ATOM   6153 C  CA  . GLY B 1 421 ? -20.228 17.715  55.085  1.00   46.64  ? 436 GLY B CA  1 
ATOM   6154 C  C   . GLY B 1 421 ? -19.426 18.114  53.874  1.00   45.26  ? 436 GLY B C   1 
ATOM   6155 O  O   . GLY B 1 421 ? -19.526 17.462  52.865  1.00   43.85  ? 436 GLY B O   1 
ATOM   6156 N  N   . PRO B 1 422 ? -18.587 19.154  53.990  1.00   45.43  ? 437 PRO B N   1 
ATOM   6157 C  CA  . PRO B 1 422 ? -18.029 19.834  52.824  1.00   46.50  ? 437 PRO B CA  1 
ATOM   6158 C  C   . PRO B 1 422 ? -17.166 18.966  51.901  1.00   46.35  ? 437 PRO B C   1 
ATOM   6159 O  O   . PRO B 1 422 ? -17.073 19.271  50.733  1.00   48.06  ? 437 PRO B O   1 
ATOM   6160 C  CB  . PRO B 1 422 ? -17.162 20.949  53.437  1.00   46.12  ? 437 PRO B CB  1 
ATOM   6161 C  CG  . PRO B 1 422 ? -17.548 21.028  54.858  1.00   46.08  ? 437 PRO B CG  1 
ATOM   6162 C  CD  . PRO B 1 422 ? -17.984 19.652  55.231  1.00   45.23  ? 437 PRO B CD  1 
ATOM   6163 N  N   . ARG B 1 423 ? -16.557 17.918  52.458  1.00   45.42  ? 438 ARG B N   1 
ATOM   6164 C  CA  . ARG B 1 423 ? -15.662 17.017  51.787  1.00   44.32  ? 438 ARG B CA  1 
ATOM   6165 C  C   . ARG B 1 423 ? -16.336 15.731  51.384  1.00   44.26  ? 438 ARG B C   1 
ATOM   6166 O  O   . ARG B 1 423 ? -15.673 14.709  51.159  1.00   44.03  ? 438 ARG B O   1 
ATOM   6167 C  CB  . ARG B 1 423 ? -14.485 16.698  52.722  1.00   43.67  ? 438 ARG B CB  1 
ATOM   6168 C  CG  . ARG B 1 423 ? -13.617 17.908  52.974  1.00   44.89  ? 438 ARG B CG  1 
ATOM   6169 C  CD  . ARG B 1 423 ? -13.102 18.321  51.613  1.00   46.90  ? 438 ARG B CD  1 
ATOM   6170 N  NE  . ARG B 1 423 ? -11.981 19.223  51.645  1.00   47.69  ? 438 ARG B NE  1 
ATOM   6171 C  CZ  . ARG B 1 423 ? -10.957 19.160  50.818  1.00   49.04  ? 438 ARG B CZ  1 
ATOM   6172 N  NH1 . ARG B 1 423 ? -10.873 18.216  49.878  1.00   48.55  ? 438 ARG B NH1 1 
ATOM   6173 N  NH2 . ARG B 1 423 ? -9.993  20.053  50.957  1.00   52.40  ? 438 ARG B NH2 1 
ATOM   6174 N  N   . VAL B 1 424 ? -17.644 15.773  51.221  1.00   45.32  ? 439 VAL B N   1 
ATOM   6175 C  CA  . VAL B 1 424 ? -18.366 14.585  50.772  1.00   45.71  ? 439 VAL B CA  1 
ATOM   6176 C  C   . VAL B 1 424 ? -17.904 14.182  49.359  1.00   45.76  ? 439 VAL B C   1 
ATOM   6177 O  O   . VAL B 1 424 ? -17.363 15.006  48.584  1.00   45.79  ? 439 VAL B O   1 
ATOM   6178 C  CB  . VAL B 1 424 ? -19.907 14.801  50.848  1.00   46.88  ? 439 VAL B CB  1 
ATOM   6179 C  CG1 . VAL B 1 424 ? -20.393 15.588  49.649  1.00   47.60  ? 439 VAL B CG1 1 
ATOM   6180 C  CG2 . VAL B 1 424 ? -20.641 13.477  50.989  1.00   46.55  ? 439 VAL B CG2 1 
ATOM   6181 N  N   . CYS B 1 425 ? -18.093 12.906  49.051  1.00   45.73  ? 440 CYS B N   1 
ATOM   6182 C  CA  . CYS B 1 425 ? -17.739 12.391  47.750  1.00   47.20  ? 440 CYS B CA  1 
ATOM   6183 C  C   . CYS B 1 425 ? -18.406 13.205  46.643  1.00   50.17  ? 440 CYS B C   1 
ATOM   6184 O  O   . CYS B 1 425 ? -19.630 13.299  46.599  1.00   54.39  ? 440 CYS B O   1 
ATOM   6185 C  CB  . CYS B 1 425 ? -18.157 10.933  47.641  1.00   46.89  ? 440 CYS B CB  1 
ATOM   6186 S  SG  . CYS B 1 425 ? -17.483 10.141  46.172  1.00   49.11  ? 440 CYS B SG  1 
ATOM   6187 N  N   . VAL B 1 426 ? -17.626 13.810  45.752  1.00   51.03  ? 441 VAL B N   1 
ATOM   6188 C  CA  . VAL B 1 426 ? -18.232 14.468  44.571  1.00   53.56  ? 441 VAL B CA  1 
ATOM   6189 C  C   . VAL B 1 426 ? -18.775 13.470  43.550  1.00   53.39  ? 441 VAL B C   1 
ATOM   6190 O  O   . VAL B 1 426 ? -19.589 13.847  42.721  1.00   53.96  ? 441 VAL B O   1 
ATOM   6191 C  CB  . VAL B 1 426 ? -17.277 15.408  43.797  1.00   54.31  ? 441 VAL B CB  1 
ATOM   6192 C  CG1 . VAL B 1 426 ? -17.328 16.833  44.318  1.00   55.71  ? 441 VAL B CG1 1 
ATOM   6193 C  CG2 . VAL B 1 426 ? -15.863 14.873  43.815  1.00   52.94  ? 441 VAL B CG2 1 
ATOM   6194 N  N   . GLY B 1 427 ? -18.303 12.223  43.600  1.00   52.00  ? 442 GLY B N   1 
ATOM   6195 C  CA  . GLY B 1 427 ? -18.794 11.164  42.723  1.00   52.62  ? 442 GLY B CA  1 
ATOM   6196 C  C   . GLY B 1 427 ? -19.994 10.370  43.230  1.00   53.60  ? 442 GLY B C   1 
ATOM   6197 O  O   . GLY B 1 427 ? -20.424 9.408   42.592  1.00   53.77  ? 442 GLY B O   1 
ATOM   6198 N  N   . GLU B 1 428 ? -20.552 10.747  44.370  1.00   54.37  ? 443 GLU B N   1 
ATOM   6199 C  CA  . GLU B 1 428 ? -21.533 9.878   44.984  1.00   55.66  ? 443 GLU B CA  1 
ATOM   6200 C  C   . GLU B 1 428 ? -22.632 9.513   43.972  1.00   56.67  ? 443 GLU B C   1 
ATOM   6201 O  O   . GLU B 1 428 ? -22.904 8.335   43.780  1.00   55.09  ? 443 GLU B O   1 
ATOM   6202 C  CB  . GLU B 1 428 ? -22.101 10.497  46.265  1.00   57.08  ? 443 GLU B CB  1 
ATOM   6203 C  CG  . GLU B 1 428 ? -23.076 9.591   46.994  1.00   58.75  ? 443 GLU B CG  1 
ATOM   6204 C  CD  . GLU B 1 428 ? -23.679 10.254  48.203  1.00   61.53  ? 443 GLU B CD  1 
ATOM   6205 O  OE1 . GLU B 1 428 ? -23.504 11.476  48.309  1.00   65.89  ? 443 GLU B OE1 1 
ATOM   6206 O  OE2 . GLU B 1 428 ? -24.333 9.573   49.033  1.00   62.36  ? 443 GLU B OE2 1 
ATOM   6207 N  N   . SER B 1 429 ? -23.245 10.503  43.323  1.00   59.60  ? 444 SER B N   1 
ATOM   6208 C  CA  . SER B 1 429 ? -24.254 10.215  42.267  1.00   63.35  ? 444 SER B CA  1 
ATOM   6209 C  C   . SER B 1 429 ? -23.688 9.270   41.231  1.00   64.29  ? 444 SER B C   1 
ATOM   6210 O  O   . SER B 1 429 ? -24.256 8.207   40.932  1.00   66.51  ? 444 SER B O   1 
ATOM   6211 C  CB  . SER B 1 429 ? -24.685 11.470  41.510  1.00   64.31  ? 444 SER B CB  1 
ATOM   6212 O  OG  . SER B 1 429 ? -25.866 12.000  42.040  1.00   67.39  ? 444 SER B OG  1 
ATOM   6213 N  N   . LEU B 1 430 ? -22.564 9.679   40.665  1.00   62.32  ? 445 LEU B N   1 
ATOM   6214 C  CA  . LEU B 1 430 ? -21.933 8.876   39.654  1.00   62.08  ? 445 LEU B CA  1 
ATOM   6215 C  C   . LEU B 1 430 ? -21.870 7.424   40.121  1.00   58.49  ? 445 LEU B C   1 
ATOM   6216 O  O   . LEU B 1 430 ? -22.425 6.530   39.476  1.00   58.43  ? 445 LEU B O   1 
ATOM   6217 C  CB  . LEU B 1 430 ? -20.552 9.443   39.351  1.00   62.64  ? 445 LEU B CB  1 
ATOM   6218 C  CG  . LEU B 1 430 ? -19.610 8.584   38.537  1.00   64.10  ? 445 LEU B CG  1 
ATOM   6219 C  CD1 . LEU B 1 430 ? -20.313 8.032   37.303  1.00   66.56  ? 445 LEU B CD1 1 
ATOM   6220 C  CD2 . LEU B 1 430 ? -18.390 9.413   38.168  1.00   64.26  ? 445 LEU B CD2 1 
ATOM   6221 N  N   . ALA B 1 431 ? -21.244 7.203   41.271  1.00   55.13  ? 446 ALA B N   1 
ATOM   6222 C  CA  . ALA B 1 431 ? -20.961 5.843   41.725  1.00   53.28  ? 446 ALA B CA  1 
ATOM   6223 C  C   . ALA B 1 431 ? -22.228 5.042   42.019  1.00   53.88  ? 446 ALA B C   1 
ATOM   6224 O  O   . ALA B 1 431 ? -22.349 3.863   41.686  1.00   51.06  ? 446 ALA B O   1 
ATOM   6225 C  CB  . ALA B 1 431 ? -20.039 5.867   42.932  1.00   51.11  ? 446 ALA B CB  1 
ATOM   6226 N  N   . ARG B 1 432 ? -23.187 5.691   42.642  1.00   57.75  ? 447 ARG B N   1 
ATOM   6227 C  CA  . ARG B 1 432 ? -24.425 5.010   42.980  1.00   60.91  ? 447 ARG B CA  1 
ATOM   6228 C  C   . ARG B 1 432 ? -25.066 4.436   41.725  1.00   63.45  ? 447 ARG B C   1 
ATOM   6229 O  O   . ARG B 1 432 ? -25.325 3.234   41.641  1.00   67.25  ? 447 ARG B O   1 
ATOM   6230 C  CB  . ARG B 1 432 ? -25.362 5.968   43.697  1.00   62.12  ? 447 ARG B CB  1 
ATOM   6231 C  CG  . ARG B 1 432 ? -24.877 6.288   45.105  1.00   61.04  ? 447 ARG B CG  1 
ATOM   6232 C  CD  . ARG B 1 432 ? -25.814 7.243   45.829  1.00   62.34  ? 447 ARG B CD  1 
ATOM   6233 N  NE  . ARG B 1 432 ? -25.584 7.182   47.266  1.00   62.00  ? 447 ARG B NE  1 
ATOM   6234 C  CZ  . ARG B 1 432 ? -25.968 6.178   48.060  1.00   61.57  ? 447 ARG B CZ  1 
ATOM   6235 N  NH1 . ARG B 1 432 ? -26.631 5.124   47.566  1.00   62.13  ? 447 ARG B NH1 1 
ATOM   6236 N  NH2 . ARG B 1 432 ? -25.687 6.228   49.361  1.00   59.51  ? 447 ARG B NH2 1 
ATOM   6237 N  N   . ILE B 1 433 ? -25.283 5.302   40.743  1.00   63.39  ? 448 ILE B N   1 
ATOM   6238 C  CA  . ILE B 1 433 ? -25.849 4.904   39.463  1.00   63.47  ? 448 ILE B CA  1 
ATOM   6239 C  C   . ILE B 1 433 ? -25.017 3.791   38.861  1.00   63.03  ? 448 ILE B C   1 
ATOM   6240 O  O   . ILE B 1 433 ? -25.533 2.734   38.497  1.00   64.42  ? 448 ILE B O   1 
ATOM   6241 C  CB  . ILE B 1 433 ? -25.834 6.098   38.494  1.00   63.08  ? 448 ILE B CB  1 
ATOM   6242 C  CG1 . ILE B 1 433 ? -26.941 7.085   38.866  1.00   64.86  ? 448 ILE B CG1 1 
ATOM   6243 C  CG2 . ILE B 1 433 ? -25.927 5.631   37.053  1.00   62.98  ? 448 ILE B CG2 1 
ATOM   6244 C  CD1 . ILE B 1 433 ? -26.669 8.502   38.409  1.00   65.98  ? 448 ILE B CD1 1 
ATOM   6245 N  N   . GLU B 1 434 ? -23.720 4.065   38.750  1.00   61.07  ? 449 GLU B N   1 
ATOM   6246 C  CA  . GLU B 1 434 ? -22.781 3.175   38.102  1.00   60.22  ? 449 GLU B CA  1 
ATOM   6247 C  C   . GLU B 1 434 ? -22.962 1.758   38.665  1.00   58.92  ? 449 GLU B C   1 
ATOM   6248 O  O   . GLU B 1 434 ? -23.061 0.791   37.919  1.00   59.45  ? 449 GLU B O   1 
ATOM   6249 C  CB  . GLU B 1 434 ? -21.368 3.711   38.355  1.00   60.22  ? 449 GLU B CB  1 
ATOM   6250 C  CG  . GLU B 1 434 ? -20.253 3.260   37.414  1.00   60.42  ? 449 GLU B CG  1 
ATOM   6251 C  CD  . GLU B 1 434 ? -18.999 4.138   37.569  1.00   60.69  ? 449 GLU B CD  1 
ATOM   6252 O  OE1 . GLU B 1 434 ? -18.276 4.009   38.579  1.00   58.63  ? 449 GLU B OE1 1 
ATOM   6253 O  OE2 . GLU B 1 434 ? -18.738 4.991   36.696  1.00   62.16  ? 449 GLU B OE2 1 
ATOM   6254 N  N   . LEU B 1 435 ? -23.064 1.659   39.986  1.00   56.91  ? 450 LEU B N   1 
ATOM   6255 C  CA  . LEU B 1 435 ? -23.087 0.376   40.663  1.00   55.52  ? 450 LEU B CA  1 
ATOM   6256 C  C   . LEU B 1 435 ? -24.385 -0.340  40.493  1.00   56.62  ? 450 LEU B C   1 
ATOM   6257 O  O   . LEU B 1 435 ? -24.396 -1.549  40.388  1.00   55.49  ? 450 LEU B O   1 
ATOM   6258 C  CB  . LEU B 1 435 ? -22.869 0.562   42.152  1.00   54.71  ? 450 LEU B CB  1 
ATOM   6259 C  CG  . LEU B 1 435 ? -21.469 0.948   42.555  1.00   53.38  ? 450 LEU B CG  1 
ATOM   6260 C  CD1 . LEU B 1 435 ? -21.540 1.299   44.020  1.00   53.67  ? 450 LEU B CD1 1 
ATOM   6261 C  CD2 . LEU B 1 435 ? -20.481 -0.175  42.320  1.00   52.34  ? 450 LEU B CD2 1 
ATOM   6262 N  N   . PHE B 1 436 ? -25.482 0.406   40.547  1.00   59.05  ? 451 PHE B N   1 
ATOM   6263 C  CA  . PHE B 1 436 ? -26.805 -0.138  40.243  1.00   62.10  ? 451 PHE B CA  1 
ATOM   6264 C  C   . PHE B 1 436 ? -26.794 -0.812  38.869  1.00   62.27  ? 451 PHE B C   1 
ATOM   6265 O  O   . PHE B 1 436 ? -27.004 -2.032  38.752  1.00   61.60  ? 451 PHE B O   1 
ATOM   6266 C  CB  . PHE B 1 436 ? -27.839 0.978   40.251  1.00   63.82  ? 451 PHE B CB  1 
ATOM   6267 C  CG  . PHE B 1 436 ? -29.224 0.524   39.931  1.00   66.90  ? 451 PHE B CG  1 
ATOM   6268 C  CD1 . PHE B 1 436 ? -29.980 -0.157  40.868  1.00   68.37  ? 451 PHE B CD1 1 
ATOM   6269 C  CD2 . PHE B 1 436 ? -29.795 0.812   38.709  1.00   69.04  ? 451 PHE B CD2 1 
ATOM   6270 C  CE1 . PHE B 1 436 ? -31.281 -0.554  40.582  1.00   69.90  ? 451 PHE B CE1 1 
ATOM   6271 C  CE2 . PHE B 1 436 ? -31.092 0.423   38.421  1.00   70.80  ? 451 PHE B CE2 1 
ATOM   6272 C  CZ  . PHE B 1 436 ? -31.829 -0.268  39.355  1.00   71.32  ? 451 PHE B CZ  1 
ATOM   6273 N  N   . LEU B 1 437 ? -26.503 -0.010  37.845  1.00   61.91  ? 452 LEU B N   1 
ATOM   6274 C  CA  . LEU B 1 437 ? -26.499 -0.485  36.469  1.00   62.59  ? 452 LEU B CA  1 
ATOM   6275 C  C   . LEU B 1 437 ? -25.589 -1.685  36.315  1.00   61.31  ? 452 LEU B C   1 
ATOM   6276 O  O   . LEU B 1 437 ? -25.940 -2.662  35.660  1.00   60.30  ? 452 LEU B O   1 
ATOM   6277 C  CB  . LEU B 1 437 ? -26.080 0.637   35.517  1.00   62.92  ? 452 LEU B CB  1 
ATOM   6278 C  CG  . LEU B 1 437 ? -27.187 1.433   34.795  1.00   66.05  ? 452 LEU B CG  1 
ATOM   6279 C  CD1 . LEU B 1 437 ? -28.627 1.135   35.215  1.00   67.17  ? 452 LEU B CD1 1 
ATOM   6280 C  CD2 . LEU B 1 437 ? -26.918 2.923   34.916  1.00   66.79  ? 452 LEU B CD2 1 
ATOM   6281 N  N   . PHE B 1 438 ? -24.429 -1.633  36.955  1.00   60.24  ? 453 PHE B N   1 
ATOM   6282 C  CA  . PHE B 1 438 ? -23.534 -2.759  36.860  1.00   59.92  ? 453 PHE B CA  1 
ATOM   6283 C  C   . PHE B 1 438 ? -24.101 -3.998  37.506  1.00   60.44  ? 453 PHE B C   1 
ATOM   6284 O  O   . PHE B 1 438 ? -24.157 -5.002  36.858  1.00   61.48  ? 453 PHE B O   1 
ATOM   6285 C  CB  . PHE B 1 438 ? -22.125 -2.457  37.386  1.00   58.73  ? 453 PHE B CB  1 
ATOM   6286 C  CG  . PHE B 1 438 ? -21.224 -1.885  36.345  1.00   58.11  ? 453 PHE B CG  1 
ATOM   6287 C  CD1 . PHE B 1 438 ? -21.105 -2.505  35.127  1.00   58.25  ? 453 PHE B CD1 1 
ATOM   6288 C  CD2 . PHE B 1 438 ? -20.528 -0.715  36.571  1.00   58.25  ? 453 PHE B CD2 1 
ATOM   6289 C  CE1 . PHE B 1 438 ? -20.296 -1.981  34.154  1.00   59.20  ? 453 PHE B CE1 1 
ATOM   6290 C  CE2 . PHE B 1 438 ? -19.711 -0.182  35.598  1.00   58.48  ? 453 PHE B CE2 1 
ATOM   6291 C  CZ  . PHE B 1 438 ? -19.598 -0.818  34.386  1.00   59.32  ? 453 PHE B CZ  1 
ATOM   6292 N  N   . VAL B 1 439 ? -24.551 -3.939  38.747  1.00   60.60  ? 454 VAL B N   1 
ATOM   6293 C  CA  . VAL B 1 439 ? -24.934 -5.171  39.450  1.00   62.03  ? 454 VAL B CA  1 
ATOM   6294 C  C   . VAL B 1 439 ? -26.233 -5.824  38.932  1.00   64.32  ? 454 VAL B C   1 
ATOM   6295 O  O   . VAL B 1 439 ? -26.324 -7.059  38.813  1.00   63.71  ? 454 VAL B O   1 
ATOM   6296 C  CB  . VAL B 1 439 ? -25.063 -4.925  40.960  1.00   62.57  ? 454 VAL B CB  1 
ATOM   6297 C  CG1 . VAL B 1 439 ? -25.249 -6.237  41.711  1.00   62.55  ? 454 VAL B CG1 1 
ATOM   6298 C  CG2 . VAL B 1 439 ? -23.839 -4.173  41.472  1.00   61.18  ? 454 VAL B CG2 1 
ATOM   6299 N  N   . SER B 1 440 ? -27.241 -5.013  38.632  1.00   66.27  ? 455 SER B N   1 
ATOM   6300 C  CA  . SER B 1 440 ? -28.493 -5.555  38.105  1.00   68.19  ? 455 SER B CA  1 
ATOM   6301 C  C   . SER B 1 440 ? -28.230 -6.445  36.903  1.00   69.59  ? 455 SER B C   1 
ATOM   6302 O  O   . SER B 1 440 ? -28.647 -7.595  36.894  1.00   70.62  ? 455 SER B O   1 
ATOM   6303 C  CB  . SER B 1 440 ? -29.486 -4.444  37.750  1.00   69.11  ? 455 SER B CB  1 
ATOM   6304 O  OG  . SER B 1 440 ? -28.863 -3.353  37.095  1.00   68.20  ? 455 SER B OG  1 
ATOM   6305 N  N   . ARG B 1 441 ? -27.490 -5.927  35.926  1.00   71.47  ? 456 ARG B N   1 
ATOM   6306 C  CA  . ARG B 1 441 ? -27.244 -6.634  34.659  1.00   74.58  ? 456 ARG B CA  1 
ATOM   6307 C  C   . ARG B 1 441 ? -26.533 -7.981  34.727  1.00   73.93  ? 456 ARG B C   1 
ATOM   6308 O  O   . ARG B 1 441 ? -27.001 -8.935  34.109  1.00   76.80  ? 456 ARG B O   1 
ATOM   6309 C  CB  . ARG B 1 441 ? -26.513 -5.723  33.693  1.00   76.08  ? 456 ARG B CB  1 
ATOM   6310 C  CG  . ARG B 1 441 ? -27.466 -4.763  33.044  1.00   80.85  ? 456 ARG B CG  1 
ATOM   6311 C  CD  . ARG B 1 441 ? -27.972 -5.285  31.701  1.00   86.17  ? 456 ARG B CD  1 
ATOM   6312 N  NE  . ARG B 1 441 ? -27.260 -4.594  30.641  1.00   88.98  ? 456 ARG B NE  1 
ATOM   6313 C  CZ  . ARG B 1 441 ? -27.385 -3.290  30.392  1.00   93.73  ? 456 ARG B CZ  1 
ATOM   6314 N  NH1 . ARG B 1 441 ? -28.220 -2.528  31.110  1.00   94.76  ? 456 ARG B NH1 1 
ATOM   6315 N  NH2 . ARG B 1 441 ? -26.671 -2.742  29.418  1.00   97.16  ? 456 ARG B NH2 1 
ATOM   6316 N  N   . PRO B 1 442 ? -25.398 -8.065  35.438  1.00   72.05  ? 457 PRO B N   1 
ATOM   6317 C  CA  . PRO B 1 442 ? -24.778 -9.353  35.592  1.00   72.28  ? 457 PRO B CA  1 
ATOM   6318 C  C   . PRO B 1 442 ? -25.641 -10.296 36.369  1.00   72.31  ? 457 PRO B C   1 
ATOM   6319 O  O   . PRO B 1 442 ? -25.627 -11.482 36.076  1.00   73.46  ? 457 PRO B O   1 
ATOM   6320 C  CB  . PRO B 1 442 ? -23.477 -9.035  36.364  1.00   72.72  ? 457 PRO B CB  1 
ATOM   6321 C  CG  . PRO B 1 442 ? -23.131 -7.649  35.961  1.00   71.16  ? 457 PRO B CG  1 
ATOM   6322 C  CD  . PRO B 1 442 ? -24.513 -7.008  35.940  1.00   72.58  ? 457 PRO B CD  1 
ATOM   6323 N  N   . LEU B 1 443 ? -26.396 -9.784  37.338  1.00   72.96  ? 458 LEU B N   1 
ATOM   6324 C  CA  . LEU B 1 443 ? -27.344 -10.623 38.059  1.00   72.40  ? 458 LEU B CA  1 
ATOM   6325 C  C   . LEU B 1 443 ? -28.501 -10.967 37.136  1.00   75.27  ? 458 LEU B C   1 
ATOM   6326 O  O   . LEU B 1 443 ? -28.890 -12.121 37.044  1.00   78.40  ? 458 LEU B O   1 
ATOM   6327 C  CB  . LEU B 1 443 ? -27.782 -9.958  39.364  1.00   71.64  ? 458 LEU B CB  1 
ATOM   6328 C  CG  . LEU B 1 443 ? -26.625 -9.903  40.386  1.00   70.74  ? 458 LEU B CG  1 
ATOM   6329 C  CD1 . LEU B 1 443 ? -27.057 -9.294  41.712  1.00   70.57  ? 458 LEU B CD1 1 
ATOM   6330 C  CD2 . LEU B 1 443 ? -25.984 -11.267 40.645  1.00   70.36  ? 458 LEU B CD2 1 
ATOM   6331 N  N   . GLN B 1 444 ? -29.013 -9.980  36.411  1.00   76.73  ? 459 GLN B N   1 
ATOM   6332 C  CA  . GLN B 1 444 ? -29.999 -10.231 35.351  1.00   80.97  ? 459 GLN B CA  1 
ATOM   6333 C  C   . GLN B 1 444 ? -29.533 -11.359 34.422  1.00   82.27  ? 459 GLN B C   1 
ATOM   6334 O  O   . GLN B 1 444 ? -30.156 -12.411 34.374  1.00   83.77  ? 459 GLN B O   1 
ATOM   6335 C  CB  . GLN B 1 444 ? -30.264 -8.957  34.535  1.00   80.25  ? 459 GLN B CB  1 
ATOM   6336 C  CG  . GLN B 1 444 ? -31.535 -8.997  33.726  1.00   82.14  ? 459 GLN B CG  1 
ATOM   6337 C  CD  . GLN B 1 444 ? -31.621 -7.869  32.711  1.00   83.78  ? 459 GLN B CD  1 
ATOM   6338 O  OE1 . GLN B 1 444 ? -30.689 -7.647  31.921  1.00   82.13  ? 459 GLN B OE1 1 
ATOM   6339 N  NE2 . GLN B 1 444 ? -32.754 -7.170  32.700  1.00   84.84  ? 459 GLN B NE2 1 
ATOM   6340 N  N   . ARG B 1 445 ? -28.408 -11.143 33.739  1.00   82.11  ? 460 ARG B N   1 
ATOM   6341 C  CA  . ARG B 1 445 ? -27.887 -12.082 32.736  1.00   83.39  ? 460 ARG B CA  1 
ATOM   6342 C  C   . ARG B 1 445 ? -27.253 -13.346 33.334  1.00   80.19  ? 460 ARG B C   1 
ATOM   6343 O  O   . ARG B 1 445 ? -27.372 -14.426 32.754  1.00   80.48  ? 460 ARG B O   1 
ATOM   6344 C  CB  . ARG B 1 445 ? -26.823 -11.404 31.849  1.00   85.15  ? 460 ARG B CB  1 
ATOM   6345 C  CG  . ARG B 1 445 ? -27.243 -10.099 31.170  1.00   88.58  ? 460 ARG B CG  1 
ATOM   6346 C  CD  . ARG B 1 445 ? -27.443 -10.202 29.648  1.00   92.76  ? 460 ARG B CD  1 
ATOM   6347 N  NE  . ARG B 1 445 ? -26.291 -10.781 28.927  1.00   94.20  ? 460 ARG B NE  1 
ATOM   6348 C  CZ  . ARG B 1 445 ? -25.972 -10.538 27.648  1.00   95.99  ? 460 ARG B CZ  1 
ATOM   6349 N  NH1 . ARG B 1 445 ? -26.685 -9.699  26.902  1.00   100.48 ? 460 ARG B NH1 1 
ATOM   6350 N  NH2 . ARG B 1 445 ? -24.910 -11.126 27.105  1.00   92.96  ? 460 ARG B NH2 1 
ATOM   6351 N  N   . PHE B 1 446 ? -26.575 -13.212 34.476  1.00   75.57  ? 461 PHE B N   1 
ATOM   6352 C  CA  . PHE B 1 446 ? -25.693 -14.271 34.980  1.00   72.52  ? 461 PHE B CA  1 
ATOM   6353 C  C   . PHE B 1 446 ? -25.899 -14.709 36.440  1.00   69.61  ? 461 PHE B C   1 
ATOM   6354 O  O   . PHE B 1 446 ? -26.461 -14.001 37.276  1.00   66.77  ? 461 PHE B O   1 
ATOM   6355 C  CB  . PHE B 1 446 ? -24.224 -13.854 34.849  1.00   70.90  ? 461 PHE B CB  1 
ATOM   6356 C  CG  . PHE B 1 446 ? -23.789 -13.566 33.460  1.00   72.72  ? 461 PHE B CG  1 
ATOM   6357 C  CD1 . PHE B 1 446 ? -23.639 -14.600 32.545  1.00   76.54  ? 461 PHE B CD1 1 
ATOM   6358 C  CD2 . PHE B 1 446 ? -23.479 -12.272 33.066  1.00   72.86  ? 461 PHE B CD2 1 
ATOM   6359 C  CE1 . PHE B 1 446 ? -23.207 -14.349 31.249  1.00   77.37  ? 461 PHE B CE1 1 
ATOM   6360 C  CE2 . PHE B 1 446 ? -23.051 -12.011 31.771  1.00   75.64  ? 461 PHE B CE2 1 
ATOM   6361 C  CZ  . PHE B 1 446 ? -22.916 -13.053 30.858  1.00   76.99  ? 461 PHE B CZ  1 
ATOM   6362 N  N   . SER B 1 447 ? -25.328 -15.875 36.720  1.00   68.37  ? 462 SER B N   1 
ATOM   6363 C  CA  . SER B 1 447 ? -25.288 -16.494 38.023  1.00   66.11  ? 462 SER B CA  1 
ATOM   6364 C  C   . SER B 1 447 ? -23.824 -16.876 38.270  1.00   64.18  ? 462 SER B C   1 
ATOM   6365 O  O   . SER B 1 447 ? -23.121 -17.349 37.347  1.00   61.00  ? 462 SER B O   1 
ATOM   6366 C  CB  . SER B 1 447 ? -26.150 -17.737 38.027  1.00   68.03  ? 462 SER B CB  1 
ATOM   6367 O  OG  . SER B 1 447 ? -26.310 -18.227 39.331  1.00   68.59  ? 462 SER B OG  1 
ATOM   6368 N  N   . PHE B 1 448 ? -23.375 -16.670 39.512  1.00   62.17  ? 463 PHE B N   1 
ATOM   6369 C  CA  . PHE B 1 448 ? -21.964 -16.765 39.841  1.00   60.47  ? 463 PHE B CA  1 
ATOM   6370 C  C   . PHE B 1 448 ? -21.728 -17.802 40.933  1.00   61.30  ? 463 PHE B C   1 
ATOM   6371 O  O   . PHE B 1 448 ? -22.228 -17.650 42.050  1.00   62.48  ? 463 PHE B O   1 
ATOM   6372 C  CB  . PHE B 1 448 ? -21.474 -15.412 40.327  1.00   58.54  ? 463 PHE B CB  1 
ATOM   6373 C  CG  . PHE B 1 448 ? -21.610 -14.302 39.319  1.00   57.22  ? 463 PHE B CG  1 
ATOM   6374 C  CD1 . PHE B 1 448 ? -22.764 -13.529 39.266  1.00   56.69  ? 463 PHE B CD1 1 
ATOM   6375 C  CD2 . PHE B 1 448 ? -20.559 -13.994 38.456  1.00   56.09  ? 463 PHE B CD2 1 
ATOM   6376 C  CE1 . PHE B 1 448 ? -22.879 -12.485 38.358  1.00   56.24  ? 463 PHE B CE1 1 
ATOM   6377 C  CE2 . PHE B 1 448 ? -20.675 -12.955 37.545  1.00   55.77  ? 463 PHE B CE2 1 
ATOM   6378 C  CZ  . PHE B 1 448 ? -21.836 -12.202 37.492  1.00   55.65  ? 463 PHE B CZ  1 
ATOM   6379 N  N   . SER B 1 449 ? -20.974 -18.853 40.629  1.00   61.33  ? 464 SER B N   1 
ATOM   6380 C  CA  . SER B 1 449 ? -20.673 -19.855 41.641  1.00   63.01  ? 464 SER B CA  1 
ATOM   6381 C  C   . SER B 1 449 ? -19.175 -20.053 41.794  1.00   64.82  ? 464 SER B C   1 
ATOM   6382 O  O   . SER B 1 449 ? -18.379 -19.617 40.958  1.00   62.82  ? 464 SER B O   1 
ATOM   6383 C  CB  . SER B 1 449 ? -21.338 -21.177 41.314  1.00   64.31  ? 464 SER B CB  1 
ATOM   6384 O  OG  . SER B 1 449 ? -20.991 -21.581 40.018  1.00   64.20  ? 464 SER B OG  1 
ATOM   6385 N  N   . CYS B 1 450 ? -18.800 -20.707 42.888  1.00   67.43  ? 465 CYS B N   1 
ATOM   6386 C  CA  . CYS B 1 450 ? -17.399 -20.917 43.201  1.00   68.31  ? 465 CYS B CA  1 
ATOM   6387 C  C   . CYS B 1 450 ? -16.877 -22.221 42.591  1.00   69.86  ? 465 CYS B C   1 
ATOM   6388 O  O   . CYS B 1 450 ? -17.219 -23.306 43.068  1.00   71.29  ? 465 CYS B O   1 
ATOM   6389 C  CB  . CYS B 1 450 ? -17.190 -20.933 44.706  1.00   69.01  ? 465 CYS B CB  1 
ATOM   6390 S  SG  . CYS B 1 450 ? -15.445 -20.985 45.110  1.00   68.10  ? 465 CYS B SG  1 
ATOM   6391 N  N   . PRO B 1 451 ? -16.021 -22.113 41.558  1.00   70.41  ? 466 PRO B N   1 
ATOM   6392 C  CA  . PRO B 1 451 ? -15.525 -23.243 40.795  1.00   73.09  ? 466 PRO B CA  1 
ATOM   6393 C  C   . PRO B 1 451 ? -15.356 -24.505 41.605  1.00   75.32  ? 466 PRO B C   1 
ATOM   6394 O  O   . PRO B 1 451 ? -14.839 -24.458 42.702  1.00   74.61  ? 466 PRO B O   1 
ATOM   6395 C  CB  . PRO B 1 451 ? -14.146 -22.764 40.333  1.00   71.45  ? 466 PRO B CB  1 
ATOM   6396 C  CG  . PRO B 1 451 ? -14.314 -21.303 40.147  1.00   69.32  ? 466 PRO B CG  1 
ATOM   6397 C  CD  . PRO B 1 451 ? -15.312 -20.871 41.186  1.00   69.63  ? 466 PRO B CD  1 
ATOM   6398 N  N   . SER B 1 452 ? -15.767 -25.630 41.035  1.00   80.52  ? 467 SER B N   1 
ATOM   6399 C  CA  . SER B 1 452 ? -15.554 -26.945 41.627  1.00   83.54  ? 467 SER B CA  1 
ATOM   6400 C  C   . SER B 1 452 ? -14.375 -26.964 42.605  1.00   81.73  ? 467 SER B C   1 
ATOM   6401 O  O   . SER B 1 452 ? -14.506 -27.465 43.721  1.00   83.23  ? 467 SER B O   1 
ATOM   6402 C  CB  . SER B 1 452 ? -15.342 -27.981 40.510  1.00   86.73  ? 467 SER B CB  1 
ATOM   6403 O  OG  . SER B 1 452 ? -15.043 -29.263 41.035  1.00   90.70  ? 467 SER B OG  1 
ATOM   6404 N  N   . GLU B 1 453 ? -13.237 -26.406 42.197  1.00   79.96  ? 468 GLU B N   1 
ATOM   6405 C  CA  . GLU B 1 453 ? -12.033 -26.497 43.014  1.00   80.25  ? 468 GLU B CA  1 
ATOM   6406 C  C   . GLU B 1 453 ? -11.182 -25.215 43.106  1.00   74.19  ? 468 GLU B C   1 
ATOM   6407 O  O   . GLU B 1 453 ? -9.958  -25.259 43.070  1.00   71.66  ? 468 GLU B O   1 
ATOM   6408 C  CB  . GLU B 1 453 ? -11.220 -27.721 42.563  1.00   86.85  ? 468 GLU B CB  1 
ATOM   6409 C  CG  . GLU B 1 453 ? -11.942 -29.036 42.873  1.00   92.07  ? 468 GLU B CG  1 
ATOM   6410 C  CD  . GLU B 1 453 ? -11.200 -30.282 42.425  1.00   97.76  ? 468 GLU B CD  1 
ATOM   6411 O  OE1 . GLU B 1 453 ? -11.056 -31.208 43.266  1.00   100.08 ? 468 GLU B OE1 1 
ATOM   6412 O  OE2 . GLU B 1 453 ? -10.788 -30.339 41.236  1.00   98.14  ? 468 GLU B OE2 1 
ATOM   6413 N  N   . ALA B 1 454 ? -11.853 -24.078 43.258  1.00   69.87  ? 469 ALA B N   1 
ATOM   6414 C  CA  . ALA B 1 454 ? -11.234 -22.882 43.825  1.00   66.78  ? 469 ALA B CA  1 
ATOM   6415 C  C   . ALA B 1 454 ? -11.854 -22.592 45.211  1.00   65.36  ? 469 ALA B C   1 
ATOM   6416 O  O   . ALA B 1 454 ? -12.934 -23.109 45.561  1.00   64.84  ? 469 ALA B O   1 
ATOM   6417 C  CB  . ALA B 1 454 ? -11.403 -21.692 42.898  1.00   65.38  ? 469 ALA B CB  1 
ATOM   6418 N  N   . SER B 1 455 ? -11.148 -21.794 46.012  1.00   62.07  ? 470 SER B N   1 
ATOM   6419 C  CA  . SER B 1 455 ? -11.609 -21.470 47.351  1.00   59.67  ? 470 SER B CA  1 
ATOM   6420 C  C   . SER B 1 455 ? -12.709 -20.450 47.294  1.00   59.07  ? 470 SER B C   1 
ATOM   6421 O  O   . SER B 1 455 ? -12.736 -19.607 46.403  1.00   58.29  ? 470 SER B O   1 
ATOM   6422 C  CB  . SER B 1 455 ? -10.465 -20.934 48.195  1.00   58.00  ? 470 SER B CB  1 
ATOM   6423 O  OG  . SER B 1 455 ? -9.641  -21.999 48.616  1.00   58.84  ? 470 SER B OG  1 
ATOM   6424 N  N   . LEU B 1 456 ? -13.630 -20.524 48.246  1.00   60.80  ? 471 LEU B N   1 
ATOM   6425 C  CA  . LEU B 1 456 ? -14.547 -19.422 48.443  1.00   60.39  ? 471 LEU B CA  1 
ATOM   6426 C  C   . LEU B 1 456 ? -13.661 -18.208 48.620  1.00   58.48  ? 471 LEU B C   1 
ATOM   6427 O  O   . LEU B 1 456 ? -12.609 -18.314 49.244  1.00   58.78  ? 471 LEU B O   1 
ATOM   6428 C  CB  . LEU B 1 456 ? -15.428 -19.652 49.664  1.00   61.28  ? 471 LEU B CB  1 
ATOM   6429 C  CG  . LEU B 1 456 ? -16.500 -20.722 49.420  1.00   63.63  ? 471 LEU B CG  1 
ATOM   6430 C  CD1 . LEU B 1 456 ? -17.171 -21.091 50.733  1.00   64.37  ? 471 LEU B CD1 1 
ATOM   6431 C  CD2 . LEU B 1 456 ? -17.526 -20.252 48.388  1.00   63.72  ? 471 LEU B CD2 1 
ATOM   6432 N  N   . PRO B 1 457 ? -14.046 -17.068 48.037  1.00   57.75  ? 472 PRO B N   1 
ATOM   6433 C  CA  . PRO B 1 457 ? -13.173 -15.908 48.170  1.00   56.43  ? 472 PRO B CA  1 
ATOM   6434 C  C   . PRO B 1 457 ? -12.960 -15.502 49.631  1.00   58.45  ? 472 PRO B C   1 
ATOM   6435 O  O   . PRO B 1 457 ? -13.881 -15.625 50.476  1.00   61.16  ? 472 PRO B O   1 
ATOM   6436 C  CB  . PRO B 1 457 ? -13.915 -14.801 47.420  1.00   56.10  ? 472 PRO B CB  1 
ATOM   6437 C  CG  . PRO B 1 457 ? -15.318 -15.292 47.236  1.00   56.77  ? 472 PRO B CG  1 
ATOM   6438 C  CD  . PRO B 1 457 ? -15.252 -16.784 47.238  1.00   58.05  ? 472 PRO B CD  1 
ATOM   6439 N  N   . ASP B 1 458 ? -11.752 -15.020 49.918  1.00   55.96  ? 473 ASP B N   1 
ATOM   6440 C  CA  . ASP B 1 458 ? -11.421 -14.570 51.245  1.00   54.06  ? 473 ASP B CA  1 
ATOM   6441 C  C   . ASP B 1 458 ? -11.984 -13.184 51.500  1.00   51.54  ? 473 ASP B C   1 
ATOM   6442 O  O   . ASP B 1 458 ? -11.686 -12.211 50.785  1.00   48.64  ? 473 ASP B O   1 
ATOM   6443 C  CB  . ASP B 1 458 ? -9.907  -14.543 51.453  1.00   55.46  ? 473 ASP B CB  1 
ATOM   6444 C  CG  . ASP B 1 458 ? -9.518  -14.783 52.893  1.00   54.97  ? 473 ASP B CG  1 
ATOM   6445 O  OD1 . ASP B 1 458 ? -10.242 -14.330 53.811  1.00   53.01  ? 473 ASP B OD1 1 
ATOM   6446 O  OD2 . ASP B 1 458 ? -8.482  -15.447 53.080  1.00   57.37  ? 473 ASP B OD2 1 
ATOM   6447 N  N   . LEU B 1 459 ? -12.753 -13.098 52.574  1.00   51.25  ? 474 LEU B N   1 
ATOM   6448 C  CA  . LEU B 1 459 ? -13.405 -11.870 52.940  1.00   50.04  ? 474 LEU B CA  1 
ATOM   6449 C  C   . LEU B 1 459 ? -12.589 -11.040 53.935  1.00   50.03  ? 474 LEU B C   1 
ATOM   6450 O  O   . LEU B 1 459 ? -13.109 -10.047 54.460  1.00   48.38  ? 474 LEU B O   1 
ATOM   6451 C  CB  . LEU B 1 459 ? -14.785 -12.223 53.491  1.00   49.89  ? 474 LEU B CB  1 
ATOM   6452 C  CG  . LEU B 1 459 ? -15.621 -13.029 52.493  1.00   50.21  ? 474 LEU B CG  1 
ATOM   6453 C  CD1 . LEU B 1 459 ? -16.980 -13.381 53.073  1.00   51.38  ? 474 LEU B CD1 1 
ATOM   6454 C  CD2 . LEU B 1 459 ? -15.825 -12.243 51.211  1.00   49.23  ? 474 LEU B CD2 1 
ATOM   6455 N  N   . GLN B 1 460 ? -11.328 -11.432 54.197  1.00   52.49  ? 475 GLN B N   1 
ATOM   6456 C  CA  . GLN B 1 460 ? -10.457 -10.650 55.115  1.00   54.29  ? 475 GLN B CA  1 
ATOM   6457 C  C   . GLN B 1 460 ? -10.154 -9.340  54.432  1.00   54.59  ? 475 GLN B C   1 
ATOM   6458 O  O   . GLN B 1 460 ? -10.418 -8.282  54.981  1.00   53.99  ? 475 GLN B O   1 
ATOM   6459 C  CB  . GLN B 1 460 ? -9.160  -11.367 55.531  1.00   54.46  ? 475 GLN B CB  1 
ATOM   6460 C  CG  . GLN B 1 460 ? -8.840  -11.137 57.000  1.00   57.81  ? 475 GLN B CG  1 
ATOM   6461 C  CD  . GLN B 1 460 ? -7.382  -11.402 57.426  1.00   60.55  ? 475 GLN B CD  1 
ATOM   6462 O  OE1 . GLN B 1 460 ? -7.107  -12.272 58.266  1.00   61.76  ? 475 GLN B OE1 1 
ATOM   6463 N  NE2 . GLN B 1 460 ? -6.453  -10.615 56.894  1.00   61.10  ? 475 GLN B NE2 1 
ATOM   6464 N  N   . GLY B 1 461 ? -9.654  -9.423  53.203  1.00   56.69  ? 476 GLY B N   1 
ATOM   6465 C  CA  . GLY B 1 461 ? -9.405  -8.243  52.409  1.00   57.62  ? 476 GLY B CA  1 
ATOM   6466 C  C   . GLY B 1 461 ? -8.036  -7.689  52.700  1.00   60.34  ? 476 GLY B C   1 
ATOM   6467 O  O   . GLY B 1 461 ? -7.456  -7.943  53.755  1.00   61.78  ? 476 GLY B O   1 
ATOM   6468 N  N   . ARG B 1 462 ? -7.520  -6.928  51.751  1.00   63.17  ? 477 ARG B N   1 
ATOM   6469 C  CA  . ARG B 1 462 ? -6.153  -6.443  51.797  1.00   66.24  ? 477 ARG B CA  1 
ATOM   6470 C  C   . ARG B 1 462 ? -6.207  -4.984  51.425  1.00   63.70  ? 477 ARG B C   1 
ATOM   6471 O  O   . ARG B 1 462 ? -7.160  -4.533  50.791  1.00   61.98  ? 477 ARG B O   1 
ATOM   6472 C  CB  . ARG B 1 462 ? -5.281  -7.256  50.828  1.00   71.86  ? 477 ARG B CB  1 
ATOM   6473 C  CG  . ARG B 1 462 ? -4.003  -6.581  50.333  1.00   79.50  ? 477 ARG B CG  1 
ATOM   6474 C  CD  . ARG B 1 462 ? -3.070  -7.566  49.626  1.00   85.72  ? 477 ARG B CD  1 
ATOM   6475 N  NE  . ARG B 1 462 ? -3.766  -8.361  48.604  1.00   88.49  ? 477 ARG B NE  1 
ATOM   6476 C  CZ  . ARG B 1 462 ? -3.356  -8.557  47.349  1.00   94.66  ? 477 ARG B CZ  1 
ATOM   6477 N  NH1 . ARG B 1 462 ? -2.211  -8.044  46.897  1.00   95.40  ? 477 ARG B NH1 1 
ATOM   6478 N  NH2 . ARG B 1 462 ? -4.099  -9.307  46.533  1.00   98.77  ? 477 ARG B NH2 1 
ATOM   6479 N  N   . PHE B 1 463 ? -5.200  -4.233  51.845  1.00   64.13  ? 478 PHE B N   1 
ATOM   6480 C  CA  . PHE B 1 463 ? -5.161  -2.821  51.532  1.00   63.59  ? 478 PHE B CA  1 
ATOM   6481 C  C   . PHE B 1 463 ? -4.138  -2.573  50.456  1.00   64.36  ? 478 PHE B C   1 
ATOM   6482 O  O   . PHE B 1 463 ? -2.955  -2.822  50.647  1.00   69.55  ? 478 PHE B O   1 
ATOM   6483 C  CB  . PHE B 1 463 ? -4.863  -1.961  52.764  1.00   62.73  ? 478 PHE B CB  1 
ATOM   6484 C  CG  . PHE B 1 463 ? -5.308  -0.537  52.606  1.00   61.82  ? 478 PHE B CG  1 
ATOM   6485 C  CD1 . PHE B 1 463 ? -6.617  -0.176  52.869  1.00   59.53  ? 478 PHE B CD1 1 
ATOM   6486 C  CD2 . PHE B 1 463 ? -4.424  0.438   52.163  1.00   61.50  ? 478 PHE B CD2 1 
ATOM   6487 C  CE1 . PHE B 1 463 ? -7.032  1.133   52.704  1.00   60.04  ? 478 PHE B CE1 1 
ATOM   6488 C  CE2 . PHE B 1 463 ? -4.836  1.755   51.995  1.00   60.73  ? 478 PHE B CE2 1 
ATOM   6489 C  CZ  . PHE B 1 463 ? -6.143  2.100   52.262  1.00   60.07  ? 478 PHE B CZ  1 
ATOM   6490 N  N   . GLY B 1 464 ? -4.614  -2.131  49.302  1.00   64.00  ? 479 GLY B N   1 
ATOM   6491 C  CA  . GLY B 1 464 ? -3.754  -1.523  48.314  1.00   60.92  ? 479 GLY B CA  1 
ATOM   6492 C  C   . GLY B 1 464 ? -3.874  -0.037  48.545  1.00   57.23  ? 479 GLY B C   1 
ATOM   6493 O  O   . GLY B 1 464 ? -3.370  0.503   49.523  1.00   58.99  ? 479 GLY B O   1 
ATOM   6494 N  N   . VAL B 1 465 ? -4.553  0.626   47.634  1.00   53.21  ? 480 VAL B N   1 
ATOM   6495 C  CA  . VAL B 1 465 ? -4.964  1.997   47.851  1.00   50.67  ? 480 VAL B CA  1 
ATOM   6496 C  C   . VAL B 1 465 ? -6.439  2.032   48.306  1.00   49.05  ? 480 VAL B C   1 
ATOM   6497 O  O   . VAL B 1 465 ? -6.984  3.096   48.574  1.00   49.20  ? 480 VAL B O   1 
ATOM   6498 C  CB  . VAL B 1 465 ? -4.752  2.812   46.567  1.00   51.07  ? 480 VAL B CB  1 
ATOM   6499 C  CG1 . VAL B 1 465 ? -3.357  2.542   46.013  1.00   49.80  ? 480 VAL B CG1 1 
ATOM   6500 C  CG2 . VAL B 1 465 ? -5.836  2.497   45.530  1.00   51.37  ? 480 VAL B CG2 1 
ATOM   6501 N  N   . VAL B 1 466 ? -7.076  0.859   48.355  1.00   46.17  ? 481 VAL B N   1 
ATOM   6502 C  CA  . VAL B 1 466 ? -8.378  0.682   48.957  1.00   43.89  ? 481 VAL B CA  1 
ATOM   6503 C  C   . VAL B 1 466 ? -8.439  -0.689  49.576  1.00   42.65  ? 481 VAL B C   1 
ATOM   6504 O  O   . VAL B 1 466 ? -7.611  -1.560  49.306  1.00   41.76  ? 481 VAL B O   1 
ATOM   6505 C  CB  . VAL B 1 466 ? -9.511  0.745   47.940  1.00   46.02  ? 481 VAL B CB  1 
ATOM   6506 C  CG1 . VAL B 1 466 ? -9.765  2.186   47.532  1.00   47.80  ? 481 VAL B CG1 1 
ATOM   6507 C  CG2 . VAL B 1 466 ? -9.215  -0.159  46.737  1.00   45.72  ? 481 VAL B CG2 1 
ATOM   6508 N  N   . LEU B 1 467 ? -9.449  -0.886  50.399  1.00   41.04  ? 482 LEU B N   1 
ATOM   6509 C  CA  . LEU B 1 467 ? -9.602  -2.142  51.072  1.00   41.29  ? 482 LEU B CA  1 
ATOM   6510 C  C   . LEU B 1 467 ? -10.326 -3.055  50.104  1.00   42.03  ? 482 LEU B C   1 
ATOM   6511 O  O   . LEU B 1 467 ? -11.491 -2.825  49.817  1.00   41.78  ? 482 LEU B O   1 
ATOM   6512 C  CB  . LEU B 1 467 ? -10.406 -1.937  52.372  1.00   41.14  ? 482 LEU B CB  1 
ATOM   6513 C  CG  . LEU B 1 467 ? -10.768 -3.209  53.137  1.00   40.52  ? 482 LEU B CG  1 
ATOM   6514 C  CD1 . LEU B 1 467 ? -9.543  -3.819  53.776  1.00   39.58  ? 482 LEU B CD1 1 
ATOM   6515 C  CD2 . LEU B 1 467 ? -11.833 -2.904  54.156  1.00   41.00  ? 482 LEU B CD2 1 
ATOM   6516 N  N   . GLN B 1 468 ? -9.639  -4.076  49.593  1.00   44.50  ? 483 GLN B N   1 
ATOM   6517 C  CA  . GLN B 1 468 ? -10.155 -4.881  48.459  1.00   46.55  ? 483 GLN B CA  1 
ATOM   6518 C  C   . GLN B 1 468 ? -10.011 -6.373  48.718  1.00   47.37  ? 483 GLN B C   1 
ATOM   6519 O  O   . GLN B 1 468 ? -9.101  -6.792  49.434  1.00   47.13  ? 483 GLN B O   1 
ATOM   6520 C  CB  . GLN B 1 468 ? -9.444  -4.475  47.143  1.00   47.83  ? 483 GLN B CB  1 
ATOM   6521 C  CG  . GLN B 1 468 ? -8.097  -5.147  46.877  1.00   49.85  ? 483 GLN B CG  1 
ATOM   6522 C  CD  . GLN B 1 468 ? -7.119  -4.290  46.082  1.00   52.19  ? 483 GLN B CD  1 
ATOM   6523 O  OE1 . GLN B 1 468 ? -7.472  -3.236  45.544  1.00   56.87  ? 483 GLN B OE1 1 
ATOM   6524 N  NE2 . GLN B 1 468 ? -5.878  -4.739  46.010  1.00   52.98  ? 483 GLN B NE2 1 
ATOM   6525 N  N   . PRO B 1 469 ? -10.904 -7.190  48.140  1.00   49.57  ? 484 PRO B N   1 
ATOM   6526 C  CA  . PRO B 1 469 ? -10.723 -8.626  48.344  1.00   51.65  ? 484 PRO B CA  1 
ATOM   6527 C  C   . PRO B 1 469 ? -9.438  -9.090  47.692  1.00   53.19  ? 484 PRO B C   1 
ATOM   6528 O  O   . PRO B 1 469 ? -9.034  -8.495  46.695  1.00   54.17  ? 484 PRO B O   1 
ATOM   6529 C  CB  . PRO B 1 469 ? -11.918 -9.255  47.618  1.00   50.37  ? 484 PRO B CB  1 
ATOM   6530 C  CG  . PRO B 1 469 ? -12.457 -8.209  46.715  1.00   49.57  ? 484 PRO B CG  1 
ATOM   6531 C  CD  . PRO B 1 469 ? -11.941 -6.878  47.138  1.00   49.58  ? 484 PRO B CD  1 
ATOM   6532 N  N   . GLU B 1 470 ? -8.814  -10.134 48.241  1.00   55.52  ? 485 GLU B N   1 
ATOM   6533 C  CA  . GLU B 1 470 ? -7.756  -10.862 47.523  1.00   59.00  ? 485 GLU B CA  1 
ATOM   6534 C  C   . GLU B 1 470 ? -8.358  -11.329 46.190  1.00   60.45  ? 485 GLU B C   1 
ATOM   6535 O  O   . GLU B 1 470 ? -9.571  -11.535 46.108  1.00   59.76  ? 485 GLU B O   1 
ATOM   6536 C  CB  . GLU B 1 470 ? -7.290  -12.108 48.298  1.00   62.39  ? 485 GLU B CB  1 
ATOM   6537 C  CG  . GLU B 1 470 ? -6.890  -11.924 49.761  1.00   64.27  ? 485 GLU B CG  1 
ATOM   6538 C  CD  . GLU B 1 470 ? -5.535  -11.243 49.966  1.00   67.77  ? 485 GLU B CD  1 
ATOM   6539 O  OE1 . GLU B 1 470 ? -5.192  -10.967 51.143  1.00   70.18  ? 485 GLU B OE1 1 
ATOM   6540 O  OE2 . GLU B 1 470 ? -4.803  -10.976 48.973  1.00   69.96  ? 485 GLU B OE2 1 
ATOM   6541 N  N   . ARG B 1 471 ? -7.545  -11.498 45.152  1.00   60.56  ? 486 ARG B N   1 
ATOM   6542 C  CA  . ARG B 1 471 ? -8.072  -11.990 43.869  1.00   60.96  ? 486 ARG B CA  1 
ATOM   6543 C  C   . ARG B 1 471 ? -8.768  -13.353 44.083  1.00   59.90  ? 486 ARG B C   1 
ATOM   6544 O  O   . ARG B 1 471 ? -8.369  -14.120 44.966  1.00   60.83  ? 486 ARG B O   1 
ATOM   6545 C  CB  . ARG B 1 471 ? -6.964  -12.085 42.797  1.00   62.93  ? 486 ARG B CB  1 
ATOM   6546 C  CG  . ARG B 1 471 ? -6.556  -10.741 42.199  1.00   64.08  ? 486 ARG B CG  1 
ATOM   6547 C  CD  . ARG B 1 471 ? -5.439  -10.863 41.155  1.00   67.64  ? 486 ARG B CD  1 
ATOM   6548 N  NE  . ARG B 1 471 ? -4.162  -11.368 41.691  1.00   73.19  ? 486 ARG B NE  1 
ATOM   6549 C  CZ  . ARG B 1 471 ? -3.351  -10.715 42.544  1.00   75.35  ? 486 ARG B CZ  1 
ATOM   6550 N  NH1 . ARG B 1 471 ? -3.657  -9.505  43.018  1.00   73.87  ? 486 ARG B NH1 1 
ATOM   6551 N  NH2 . ARG B 1 471 ? -2.222  -11.292 42.958  1.00   76.74  ? 486 ARG B NH2 1 
ATOM   6552 N  N   . TYR B 1 472 ? -9.812  -13.636 43.297  1.00   57.24  ? 487 TYR B N   1 
ATOM   6553 C  CA  . TYR B 1 472 ? -10.549 -14.903 43.407  1.00   56.93  ? 487 TYR B CA  1 
ATOM   6554 C  C   . TYR B 1 472 ? -11.223 -15.279 42.091  1.00   57.28  ? 487 TYR B C   1 
ATOM   6555 O  O   . TYR B 1 472 ? -11.462 -14.403 41.270  1.00   57.51  ? 487 TYR B O   1 
ATOM   6556 C  CB  . TYR B 1 472 ? -11.610 -14.785 44.485  1.00   56.18  ? 487 TYR B CB  1 
ATOM   6557 C  CG  . TYR B 1 472 ? -12.671 -13.770 44.136  1.00   54.48  ? 487 TYR B CG  1 
ATOM   6558 C  CD1 . TYR B 1 472 ? -13.750 -14.122 43.361  1.00   53.91  ? 487 TYR B CD1 1 
ATOM   6559 C  CD2 . TYR B 1 472 ? -12.575 -12.463 44.566  1.00   52.06  ? 487 TYR B CD2 1 
ATOM   6560 C  CE1 . TYR B 1 472 ? -14.708 -13.201 43.032  1.00   53.93  ? 487 TYR B CE1 1 
ATOM   6561 C  CE2 . TYR B 1 472 ? -13.539 -11.533 44.246  1.00   51.86  ? 487 TYR B CE2 1 
ATOM   6562 C  CZ  . TYR B 1 472 ? -14.606 -11.913 43.475  1.00   52.74  ? 487 TYR B CZ  1 
ATOM   6563 O  OH  . TYR B 1 472 ? -15.583 -11.004 43.141  1.00   51.89  ? 487 TYR B OH  1 
ATOM   6564 N  N   . THR B 1 473 ? -11.552 -16.565 41.919  1.00   58.38  ? 488 THR B N   1 
ATOM   6565 C  CA  . THR B 1 473 ? -12.125 -17.085 40.663  1.00   60.05  ? 488 THR B CA  1 
ATOM   6566 C  C   . THR B 1 473 ? -13.634 -17.348 40.723  1.00   62.37  ? 488 THR B C   1 
ATOM   6567 O  O   . THR B 1 473 ? -14.124 -18.026 41.626  1.00   66.69  ? 488 THR B O   1 
ATOM   6568 C  CB  . THR B 1 473 ? -11.476 -18.420 40.216  1.00   60.98  ? 488 THR B CB  1 
ATOM   6569 O  OG1 . THR B 1 473 ? -11.405 -19.334 41.321  1.00   59.41  ? 488 THR B OG1 1 
ATOM   6570 C  CG2 . THR B 1 473 ? -10.090 -18.186 39.637  1.00   60.77  ? 488 THR B CG2 1 
ATOM   6571 N  N   . VAL B 1 474 ? -14.371 -16.835 39.750  1.00   61.46  ? 489 VAL B N   1 
ATOM   6572 C  CA  . VAL B 1 474 ? -15.805 -17.092 39.682  1.00   61.78  ? 489 VAL B CA  1 
ATOM   6573 C  C   . VAL B 1 474 ? -16.189 -17.923 38.467  1.00   62.38  ? 489 VAL B C   1 
ATOM   6574 O  O   . VAL B 1 474 ? -15.597 -17.789 37.379  1.00   63.53  ? 489 VAL B O   1 
ATOM   6575 C  CB  . VAL B 1 474 ? -16.624 -15.790 39.652  1.00   60.77  ? 489 VAL B CB  1 
ATOM   6576 C  CG1 . VAL B 1 474 ? -16.534 -15.104 38.300  1.00   59.98  ? 489 VAL B CG1 1 
ATOM   6577 C  CG2 . VAL B 1 474 ? -18.078 -16.083 39.975  1.00   62.27  ? 489 VAL B CG2 1 
ATOM   6578 N  N   . THR B 1 475 ? -17.184 -18.783 38.672  1.00   62.92  ? 490 THR B N   1 
ATOM   6579 C  CA  . THR B 1 475 ? -17.832 -19.510 37.592  1.00   63.49  ? 490 THR B CA  1 
ATOM   6580 C  C   . THR B 1 475 ? -19.097 -18.756 37.226  1.00   64.38  ? 490 THR B C   1 
ATOM   6581 O  O   . THR B 1 475 ? -19.937 -18.498 38.084  1.00   66.50  ? 490 THR B O   1 
ATOM   6582 C  CB  . THR B 1 475 ? -18.177 -20.946 37.991  1.00   64.27  ? 490 THR B CB  1 
ATOM   6583 O  OG1 . THR B 1 475 ? -16.973 -21.713 38.099  1.00   63.96  ? 490 THR B OG1 1 
ATOM   6584 C  CG2 . THR B 1 475 ? -19.080 -21.591 36.944  1.00   66.97  ? 490 THR B CG2 1 
ATOM   6585 N  N   . VAL B 1 476 ? -19.208 -18.407 35.947  1.00   65.55  ? 491 VAL B N   1 
ATOM   6586 C  CA  . VAL B 1 476 ? -20.316 -17.634 35.383  1.00   66.76  ? 491 VAL B CA  1 
ATOM   6587 C  C   . VAL B 1 476 ? -21.110 -18.543 34.461  1.00   68.90  ? 491 VAL B C   1 
ATOM   6588 O  O   . VAL B 1 476 ? -20.499 -19.228 33.659  1.00   70.66  ? 491 VAL B O   1 
ATOM   6589 C  CB  . VAL B 1 476 ? -19.727 -16.465 34.572  1.00   65.35  ? 491 VAL B CB  1 
ATOM   6590 C  CG1 . VAL B 1 476 ? -20.781 -15.765 33.730  1.00   66.15  ? 491 VAL B CG1 1 
ATOM   6591 C  CG2 . VAL B 1 476 ? -19.032 -15.495 35.514  1.00   62.84  ? 491 VAL B CG2 1 
ATOM   6592 N  N   . THR B 1 477 ? -22.445 -18.554 34.531  1.00   72.53  ? 492 THR B N   1 
ATOM   6593 C  CA  . THR B 1 477 ? -23.212 -19.554 33.751  1.00   75.37  ? 492 THR B CA  1 
ATOM   6594 C  C   . THR B 1 477 ? -24.272 -19.081 32.723  1.00   79.79  ? 492 THR B C   1 
ATOM   6595 O  O   . THR B 1 477 ? -23.991 -19.044 31.505  1.00   81.32  ? 492 THR B O   1 
ATOM   6596 C  CB  . THR B 1 477 ? -23.820 -20.629 34.676  1.00   75.13  ? 492 THR B CB  1 
ATOM   6597 O  OG1 . THR B 1 477 ? -24.364 -20.003 35.828  1.00   75.98  ? 492 THR B OG1 1 
ATOM   6598 C  CG2 . THR B 1 477 ? -22.767 -21.612 35.139  1.00   74.52  ? 492 THR B CG2 1 
ATOM   6599 N  N   . PRO B 1 478 ? -25.499 -18.767 33.181  1.00   83.32  ? 493 PRO B N   1 
ATOM   6600 C  CA  . PRO B 1 478 ? -26.677 -18.852 32.288  1.00   84.03  ? 493 PRO B CA  1 
ATOM   6601 C  C   . PRO B 1 478 ? -26.816 -17.609 31.445  1.00   83.43  ? 493 PRO B C   1 
ATOM   6602 O  O   . PRO B 1 478 ? -27.569 -16.717 31.834  1.00   83.04  ? 493 PRO B O   1 
ATOM   6603 C  CB  . PRO B 1 478 ? -27.854 -18.920 33.277  1.00   85.50  ? 493 PRO B CB  1 
ATOM   6604 C  CG  . PRO B 1 478 ? -27.358 -18.107 34.471  1.00   86.56  ? 493 PRO B CG  1 
ATOM   6605 C  CD  . PRO B 1 478 ? -25.824 -17.972 34.374  1.00   82.91  ? 493 PRO B CD  1 
HETATM 6606 C  CHA . HEM C 2 .   ? 11.630  6.924   -0.957  1.00   24.95  ? 600 HEM A CHA 1 
HETATM 6607 C  CHB . HEM C 2 .   ? 14.055  3.084   -2.510  1.00   25.21  ? 600 HEM A CHB 1 
HETATM 6608 C  CHC . HEM C 2 .   ? 14.362  1.467   2.034   1.00   23.36  ? 600 HEM A CHC 1 
HETATM 6609 C  CHD . HEM C 2 .   ? 12.414  5.546   3.630   1.00   22.25  ? 600 HEM A CHD 1 
HETATM 6610 C  C1A . HEM C 2 .   ? 12.258  6.012   -1.767  1.00   25.76  ? 600 HEM A C1A 1 
HETATM 6611 C  C2A . HEM C 2 .   ? 12.160  5.960   -3.188  1.00   25.57  ? 600 HEM A C2A 1 
HETATM 6612 C  C3A . HEM C 2 .   ? 12.856  4.863   -3.594  1.00   25.81  ? 600 HEM A C3A 1 
HETATM 6613 C  C4A . HEM C 2 .   ? 13.388  4.263   -2.444  1.00   25.53  ? 600 HEM A C4A 1 
HETATM 6614 C  CMA . HEM C 2 .   ? 13.095  4.357   -4.990  1.00   24.87  ? 600 HEM A CMA 1 
HETATM 6615 C  CAA . HEM C 2 .   ? 11.404  6.869   -4.111  1.00   24.60  ? 600 HEM A CAA 1 
HETATM 6616 C  CBA . HEM C 2 .   ? 11.769  8.325   -4.090  1.00   25.51  ? 600 HEM A CBA 1 
HETATM 6617 C  CGA . HEM C 2 .   ? 10.880  8.928   -5.133  1.00   25.13  ? 600 HEM A CGA 1 
HETATM 6618 O  O1A . HEM C 2 .   ? 11.331  9.423   -6.184  1.00   26.98  ? 600 HEM A O1A 1 
HETATM 6619 O  O2A . HEM C 2 .   ? 9.667   8.924   -4.933  1.00   26.94  ? 600 HEM A O2A 1 
HETATM 6620 C  C1B . HEM C 2 .   ? 14.284  2.298   -1.391  1.00   24.32  ? 600 HEM A C1B 1 
HETATM 6621 C  C2B . HEM C 2 .   ? 14.840  1.004   -1.495  1.00   25.32  ? 600 HEM A C2B 1 
HETATM 6622 C  C3B . HEM C 2 .   ? 14.935  0.517   -0.243  1.00   25.87  ? 600 HEM A C3B 1 
HETATM 6623 C  C4B . HEM C 2 .   ? 14.405  1.564   0.648   1.00   23.96  ? 600 HEM A C4B 1 
HETATM 6624 C  CMB . HEM C 2 .   ? 15.272  0.250   -2.734  1.00   24.73  ? 600 HEM A CMB 1 
HETATM 6625 C  CAB . HEM C 2 .   ? 15.475  -0.833  -0.004  1.00   30.56  ? 600 HEM A CAB 1 
HETATM 6626 C  CBB . HEM C 2 .   ? 15.424  -1.471  1.146   1.00   32.06  ? 600 HEM A CBB 1 
HETATM 6627 C  C1C . HEM C 2 .   ? 13.901  2.463   2.892   1.00   23.16  ? 600 HEM A C1C 1 
HETATM 6628 C  C2C . HEM C 2 .   ? 13.957  2.412   4.302   1.00   22.75  ? 600 HEM A C2C 1 
HETATM 6629 C  C3C . HEM C 2 .   ? 13.388  3.585   4.766   1.00   23.18  ? 600 HEM A C3C 1 
HETATM 6630 C  C4C . HEM C 2 .   ? 13.009  4.347   3.638   1.00   21.78  ? 600 HEM A C4C 1 
HETATM 6631 C  CMC . HEM C 2 .   ? 14.525  1.305   5.181   1.00   21.23  ? 600 HEM A CMC 1 
HETATM 6632 C  CAC . HEM C 2 .   ? 13.288  3.829   6.224   1.00   27.11  ? 600 HEM A CAC 1 
HETATM 6633 C  CBC . HEM C 2 .   ? 12.729  4.880   6.818   1.00   28.43  ? 600 HEM A CBC 1 
HETATM 6634 C  C1D . HEM C 2 .   ? 12.045  6.181   2.443   1.00   23.06  ? 600 HEM A C1D 1 
HETATM 6635 C  C2D . HEM C 2 .   ? 11.250  7.404   2.505   1.00   24.20  ? 600 HEM A C2D 1 
HETATM 6636 C  C3D . HEM C 2 .   ? 11.017  7.788   1.268   1.00   23.29  ? 600 HEM A C3D 1 
HETATM 6637 C  C4D . HEM C 2 .   ? 11.671  6.791   0.422   1.00   23.62  ? 600 HEM A C4D 1 
HETATM 6638 C  CMD . HEM C 2 .   ? 10.736  8.130   3.711   1.00   25.77  ? 600 HEM A CMD 1 
HETATM 6639 C  CAD . HEM C 2 .   ? 10.218  9.003   0.895   1.00   22.39  ? 600 HEM A CAD 1 
HETATM 6640 C  CBD . HEM C 2 .   ? 11.019  10.146  0.269   1.00   21.50  ? 600 HEM A CBD 1 
HETATM 6641 C  CGD . HEM C 2 .   ? 10.013  11.061  -0.405  1.00   19.85  ? 600 HEM A CGD 1 
HETATM 6642 O  O1D . HEM C 2 .   ? 10.272  12.270  -0.414  1.00   18.05  ? 600 HEM A O1D 1 
HETATM 6643 N  NA  . HEM C 2 .   ? 12.998  4.935   -1.325  1.00   24.63  ? 600 HEM A NA  1 
HETATM 6644 N  NB  . HEM C 2 .   ? 14.088  2.609   -0.127  1.00   23.09  ? 600 HEM A NB  1 
HETATM 6645 N  NC  . HEM C 2 .   ? 13.342  3.652   2.515   1.00   22.61  ? 600 HEM A NC  1 
HETATM 6646 N  ND  . HEM C 2 .   ? 12.314  5.883   1.168   1.00   22.14  ? 600 HEM A ND  1 
HETATM 6647 FE FE  . HEM C 2 .   ? 13.168  4.353   0.546   1.00   22.70  ? 600 HEM A FE  1 
HETATM 6648 C  C1  . STR D 3 .   ? 4.088   0.207   2.108   1.00   45.69  ? 601 STR A C1  1 
HETATM 6649 C  C2  . STR D 3 .   ? 3.259   -0.310  3.266   1.00   44.77  ? 601 STR A C2  1 
HETATM 6650 C  C3  . STR D 3 .   ? 3.023   0.625   4.243   1.00   43.63  ? 601 STR A C3  1 
HETATM 6651 O  O3  . STR D 3 .   ? 2.713   0.237   5.369   1.00   47.02  ? 601 STR A O3  1 
HETATM 6652 C  C4  . STR D 3 .   ? 3.101   1.986   3.993   1.00   42.76  ? 601 STR A C4  1 
HETATM 6653 C  C5  . STR D 3 .   ? 3.502   2.514   2.760   1.00   44.16  ? 601 STR A C5  1 
HETATM 6654 C  C6  . STR D 3 .   ? 3.569   3.912   2.623   1.00   42.89  ? 601 STR A C6  1 
HETATM 6655 C  C7  . STR D 3 .   ? 4.946   4.366   2.206   1.00   42.72  ? 601 STR A C7  1 
HETATM 6656 C  C8  . STR D 3 .   ? 5.332   3.674   0.933   1.00   42.87  ? 601 STR A C8  1 
HETATM 6657 C  C9  . STR D 3 .   ? 5.203   2.162   1.085   1.00   43.28  ? 601 STR A C9  1 
HETATM 6658 C  C10 . STR D 3 .   ? 3.833   1.688   1.653   1.00   44.59  ? 601 STR A C10 1 
HETATM 6659 C  C11 . STR D 3 .   ? 5.569   1.427   -0.269  1.00   44.48  ? 601 STR A C11 1 
HETATM 6660 C  C12 . STR D 3 .   ? 7.001   1.804   -0.648  1.00   44.07  ? 601 STR A C12 1 
HETATM 6661 C  C13 . STR D 3 .   ? 7.124   3.307   -0.801  1.00   44.30  ? 601 STR A C13 1 
HETATM 6662 C  C14 . STR D 3 .   ? 6.832   3.889   0.581   1.00   43.91  ? 601 STR A C14 1 
HETATM 6663 C  C15 . STR D 3 .   ? 7.321   5.315   0.474   1.00   45.03  ? 601 STR A C15 1 
HETATM 6664 C  C16 . STR D 3 .   ? 8.540   5.230   -0.500  1.00   44.97  ? 601 STR A C16 1 
HETATM 6665 C  C17 . STR D 3 .   ? 8.571   3.793   -1.061  1.00   45.82  ? 601 STR A C17 1 
HETATM 6666 C  C18 . STR D 3 .   ? 6.166   3.798   -1.902  1.00   45.41  ? 601 STR A C18 1 
HETATM 6667 C  C19 . STR D 3 .   ? 2.724   1.742   0.582   1.00   43.24  ? 601 STR A C19 1 
HETATM 6668 C  C20 . STR D 3 .   ? 9.065   3.667   -2.561  1.00   50.75  ? 601 STR A C20 1 
HETATM 6669 O  O20 . STR D 3 .   ? 9.841   2.764   -2.884  1.00   51.96  ? 601 STR A O20 1 
HETATM 6670 C  C21 . STR D 3 .   ? 8.563   4.650   -3.667  1.00   51.91  ? 601 STR A C21 1 
HETATM 6671 C  CHA . HEM E 2 .   ? -14.107 11.318  48.334  1.00   25.87  ? 600 HEM B CHA 1 
HETATM 6672 C  CHB . HEM E 2 .   ? -16.348 7.134   48.911  1.00   26.45  ? 600 HEM B CHB 1 
HETATM 6673 C  CHC . HEM E 2 .   ? -16.623 6.618   44.173  1.00   25.06  ? 600 HEM B CHC 1 
HETATM 6674 C  CHD . HEM E 2 .   ? -14.669 10.949  43.527  1.00   25.75  ? 600 HEM B CHD 1 
HETATM 6675 C  C1A . HEM E 2 .   ? -14.675 10.223  48.914  1.00   26.33  ? 600 HEM B C1A 1 
HETATM 6676 C  C2A . HEM E 2 .   ? -14.617 9.882   50.315  1.00   27.16  ? 600 HEM B C2A 1 
HETATM 6677 C  C3A . HEM E 2 .   ? -15.261 8.699   50.436  1.00   27.02  ? 600 HEM B C3A 1 
HETATM 6678 C  C4A . HEM E 2 .   ? -15.699 8.320   49.143  1.00   27.24  ? 600 HEM B C4A 1 
HETATM 6679 C  CMA . HEM E 2 .   ? -15.510 7.905   51.696  1.00   26.29  ? 600 HEM B CMA 1 
HETATM 6680 C  CAA . HEM E 2 .   ? -13.967 10.601  51.493  1.00   26.43  ? 600 HEM B CAA 1 
HETATM 6681 C  CBA . HEM E 2 .   ? -14.402 12.042  51.716  1.00   26.87  ? 600 HEM B CBA 1 
HETATM 6682 C  CGA . HEM E 2 .   ? -13.780 12.574  52.973  1.00   26.57  ? 600 HEM B CGA 1 
HETATM 6683 O  O1A . HEM E 2 .   ? -14.493 13.169  53.807  1.00   30.06  ? 600 HEM B O1A 1 
HETATM 6684 O  O2A . HEM E 2 .   ? -12.561 12.443  53.179  1.00   27.30  ? 600 HEM B O2A 1 
HETATM 6685 C  C1B . HEM E 2 .   ? -16.586 6.630   47.670  1.00   25.15  ? 600 HEM B C1B 1 
HETATM 6686 C  C2B . HEM E 2 .   ? -17.169 5.359   47.484  1.00   26.27  ? 600 HEM B C2B 1 
HETATM 6687 C  C3B . HEM E 2 .   ? -17.272 5.176   46.150  1.00   27.84  ? 600 HEM B C3B 1 
HETATM 6688 C  C4B . HEM E 2 .   ? -16.705 6.397   45.527  1.00   25.94  ? 600 HEM B C4B 1 
HETATM 6689 C  CMB . HEM E 2 .   ? -17.647 4.343   48.488  1.00   25.53  ? 600 HEM B CMB 1 
HETATM 6690 C  CAB . HEM E 2 .   ? -17.821 3.922   45.595  1.00   30.19  ? 600 HEM B CAB 1 
HETATM 6691 C  CBB . HEM E 2 .   ? -17.765 3.573   44.320  1.00   31.39  ? 600 HEM B CBB 1 
HETATM 6692 C  C1C . HEM E 2 .   ? -16.139 7.757   43.581  1.00   24.87  ? 600 HEM B C1C 1 
HETATM 6693 C  C2C . HEM E 2 .   ? -16.136 7.977   42.214  1.00   25.86  ? 600 HEM B C2C 1 
HETATM 6694 C  C3C . HEM E 2 .   ? -15.594 9.215   41.980  1.00   26.74  ? 600 HEM B C3C 1 
HETATM 6695 C  C4C . HEM E 2 .   ? -15.265 9.754   43.262  1.00   25.92  ? 600 HEM B C4C 1 
HETATM 6696 C  CMC . HEM E 2 .   ? -16.667 7.054   41.152  1.00   26.34  ? 600 HEM B CMC 1 
HETATM 6697 C  CAC . HEM E 2 .   ? -15.456 9.736   40.596  1.00   28.89  ? 600 HEM B CAC 1 
HETATM 6698 C  CBC . HEM E 2 .   ? -14.925 10.905  40.239  1.00   30.64  ? 600 HEM B CBC 1 
HETATM 6699 C  C1D . HEM E 2 .   ? -14.354 11.339  44.821  1.00   25.57  ? 600 HEM B C1D 1 
HETATM 6700 C  C2D . HEM E 2 .   ? -13.632 12.599  45.053  1.00   25.87  ? 600 HEM B C2D 1 
HETATM 6701 C  C3D . HEM E 2 .   ? -13.479 12.696  46.392  1.00   26.02  ? 600 HEM B C3D 1 
HETATM 6702 C  C4D . HEM E 2 .   ? -14.103 11.502  46.965  1.00   25.73  ? 600 HEM B C4D 1 
HETATM 6703 C  CMD . HEM E 2 .   ? -13.149 13.587  44.018  1.00   24.74  ? 600 HEM B CMD 1 
HETATM 6704 C  CAD . HEM E 2 .   ? -12.806 13.811  47.151  1.00   26.56  ? 600 HEM B CAD 1 
HETATM 6705 C  CBD . HEM E 2 .   ? -13.854 14.688  47.853  1.00   26.98  ? 600 HEM B CBD 1 
HETATM 6706 C  CGD . HEM E 2 .   ? -13.192 15.383  49.030  1.00   27.18  ? 600 HEM B CGD 1 
HETATM 6707 O  O1D . HEM E 2 .   ? -12.925 16.607  49.004  1.00   26.09  ? 600 HEM B O1D 1 
HETATM 6708 N  NA  . HEM E 2 .   ? -15.311 9.233   48.214  1.00   25.67  ? 600 HEM B NA  1 
HETATM 6709 N  NB  . HEM E 2 .   ? -16.366 7.225   46.516  1.00   25.51  ? 600 HEM B NB  1 
HETATM 6710 N  NC  . HEM E 2 .   ? -15.621 8.834   44.198  1.00   24.62  ? 600 HEM B NC  1 
HETATM 6711 N  ND  . HEM E 2 .   ? -14.630 10.736  45.990  1.00   25.25  ? 600 HEM B ND  1 
HETATM 6712 FE FE  . HEM E 2 .   ? -15.456 9.084   46.245  1.00   25.74  ? 600 HEM B FE  1 
HETATM 6713 C  C1  . STR F 3 .   ? -5.604  5.960   44.174  1.00   41.09  ? 601 STR B C1  1 
HETATM 6714 C  C2  . STR F 3 .   ? -4.688  5.816   42.922  1.00   41.04  ? 601 STR B C2  1 
HETATM 6715 C  C3  . STR F 3 .   ? -4.577  6.965   42.139  1.00   41.32  ? 601 STR B C3  1 
HETATM 6716 O  O3  . STR F 3 .   ? -4.160  6.888   40.978  1.00   41.66  ? 601 STR B O3  1 
HETATM 6717 C  C4  . STR F 3 .   ? -4.918  8.215   42.647  1.00   41.52  ? 601 STR B C4  1 
HETATM 6718 C  C5  . STR F 3 .   ? -5.433  8.431   43.940  1.00   41.33  ? 601 STR B C5  1 
HETATM 6719 C  C6  . STR F 3 .   ? -5.698  9.770   44.324  1.00   39.03  ? 601 STR B C6  1 
HETATM 6720 C  C7  . STR F 3 .   ? -7.126  9.968   44.745  1.00   38.74  ? 601 STR B C7  1 
HETATM 6721 C  C8  . STR F 3 .   ? -7.478  8.989   45.834  1.00   38.32  ? 601 STR B C8  1 
HETATM 6722 C  C9  . STR F 3 .   ? -7.151  7.551   45.385  1.00   38.34  ? 601 STR B C9  1 
HETATM 6723 C  C10 . STR F 3 .   ? -5.660  7.371   44.870  1.00   39.81  ? 601 STR B C10 1 
HETATM 6724 C  C11 . STR F 3 .   ? -7.576  6.524   46.492  1.00   38.07  ? 601 STR B C11 1 
HETATM 6725 C  C12 . STR F 3 .   ? -9.077  6.671   46.683  1.00   37.27  ? 601 STR B C12 1 
HETATM 6726 C  C13 . STR F 3 .   ? -9.388  8.083   47.139  1.00   38.81  ? 601 STR B C13 1 
HETATM 6727 C  C14 . STR F 3 .   ? -8.976  9.041   46.040  1.00   37.05  ? 601 STR B C14 1 
HETATM 6728 C  C15 . STR F 3 .   ? -9.528  10.389  46.486  1.00   36.50  ? 601 STR B C15 1 
HETATM 6729 C  C16 . STR F 3 .   ? -10.823 9.981   47.245  1.00   37.94  ? 601 STR B C16 1 
HETATM 6730 C  C17 . STR F 3 .   ? -10.845 8.422   47.186  1.00   39.65  ? 601 STR B C17 1 
HETATM 6731 C  C18 . STR F 3 .   ? -8.723  8.326   48.522  1.00   41.25  ? 601 STR B C18 1 
HETATM 6732 C  C19 . STR F 3 .   ? -4.620  7.467   45.998  1.00   39.02  ? 601 STR B C19 1 
HETATM 6733 C  C20 . STR F 3 .   ? -11.496 7.697   48.365  1.00   41.76  ? 601 STR B C20 1 
HETATM 6734 O  O20 . STR F 3 .   ? -11.776 6.505   48.270  1.00   45.95  ? 601 STR B O20 1 
HETATM 6735 C  C21 . STR F 3 .   ? -11.772 8.458   49.653  1.00   44.46  ? 601 STR B C21 1 
HETATM 6736 O  O   . HOH G 4 .   ? 4.289   -5.299  6.724   1.00   54.18  ? 701 HOH A O   1 
HETATM 6737 O  O   . HOH G 4 .   ? 15.660  -4.796  -4.766  1.00   56.56  ? 702 HOH A O   1 
HETATM 6738 O  O   . HOH G 4 .   ? 30.920  -19.943 3.819   1.00   37.71  ? 703 HOH A O   1 
HETATM 6739 O  O   . HOH G 4 .   ? 25.026  -1.428  -1.495  1.00   40.04  ? 704 HOH A O   1 
HETATM 6740 O  O   . HOH G 4 .   ? 19.212  -9.648  -21.478 1.00   51.72  ? 705 HOH A O   1 
HETATM 6741 O  O   . HOH G 4 .   ? 20.456  13.163  -5.282  1.00   38.45  ? 706 HOH A O   1 
HETATM 6742 O  O   . HOH G 4 .   ? 14.765  0.478   -6.216  1.00   44.73  ? 707 HOH A O   1 
HETATM 6743 O  O   . HOH H 4 .   ? -6.241  1.067   56.804  1.00   62.14  ? 701 HOH B O   1 
HETATM 6744 O  O   . HOH H 4 .   ? -11.119 0.793   80.593  1.00   60.12  ? 702 HOH B O   1 
HETATM 6745 O  O   . HOH H 4 .   ? -12.775 4.557   77.711  1.00   51.26  ? 703 HOH B O   1 
HETATM 6746 O  O   . HOH H 4 .   ? -18.186 6.455   73.376  1.00   63.09  ? 704 HOH B O   1 
HETATM 6747 O  O   . HOH H 4 .   ? -10.499 -11.727 41.526  1.00   51.03  ? 705 HOH B O   1 
HETATM 6748 O  O   . HOH H 4 .   ? 8.790   2.300   44.735  1.00   51.00  ? 706 HOH B O   1 
HETATM 6749 O  O   . HOH H 4 .   ? -8.533  39.672  39.015  1.00   67.70  ? 707 HOH B O   1 
HETATM 6750 O  O   . HOH H 4 .   ? -17.586 -0.642  49.323  1.00   45.59  ? 708 HOH B O   1 
HETATM 6751 O  O   . HOH H 4 .   ? -19.430 -15.760 55.271  1.00   42.53  ? 709 HOH B O   1 
HETATM 6752 O  O   . HOH H 4 .   ? -38.418 -6.777  30.200  1.00   95.57  ? 710 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASN A 38  ? 0.7922 1.1468 0.8978 -0.0446 -0.2342 -0.0934 53  ASN A N   
2    C CA  . ASN A 38  ? 0.8025 1.1380 0.8746 -0.0354 -0.2408 -0.1065 53  ASN A CA  
3    C C   . ASN A 38  ? 0.7773 1.1071 0.8285 -0.0283 -0.2242 -0.1046 53  ASN A C   
4    O O   . ASN A 38  ? 0.8994 1.2128 0.9423 -0.0266 -0.2249 -0.1111 53  ASN A O   
5    C CB  . ASN A 38  ? 0.7983 1.1370 0.8494 -0.0275 -0.2500 -0.1122 53  ASN A CB  
6    N N   . LEU A 39  ? 0.6669 1.0098 0.7109 -0.0243 -0.2099 -0.0958 54  LEU A N   
7    C CA  . LEU A 39  ? 0.5897 0.9294 0.6129 -0.0172 -0.1953 -0.0941 54  LEU A CA  
8    C C   . LEU A 39  ? 0.5096 0.8646 0.5390 -0.0181 -0.1800 -0.0813 54  LEU A C   
9    O O   . LEU A 39  ? 0.4897 0.8558 0.5206 -0.0176 -0.1802 -0.0768 54  LEU A O   
10   C CB  . LEU A 39  ? 0.6027 0.9358 0.5923 -0.0060 -0.1986 -0.1026 54  LEU A CB  
11   C CG  . LEU A 39  ? 0.6003 0.9285 0.5664 0.0027  -0.1867 -0.1039 54  LEU A CG  
12   C CD1 . LEU A 39  ? 0.6078 0.9210 0.5762 0.0027  -0.1881 -0.1105 54  LEU A CD1 
13   C CD2 . LEU A 39  ? 0.6172 0.9428 0.5514 0.0135  -0.1898 -0.1104 54  LEU A CD2 
14   N N   . PRO A 40  ? 0.4689 0.8235 0.5011 -0.0190 -0.1673 -0.0759 55  PRO A N   
15   C CA  . PRO A 40  ? 0.4238 0.7918 0.4641 -0.0208 -0.1550 -0.0645 55  PRO A CA  
16   C C   . PRO A 40  ? 0.4052 0.7795 0.4259 -0.0143 -0.1502 -0.0621 55  PRO A C   
17   O O   . PRO A 40  ? 0.4247 0.7935 0.4224 -0.0075 -0.1504 -0.0671 55  PRO A O   
18   C CB  . PRO A 40  ? 0.4180 0.7822 0.4592 -0.0213 -0.1439 -0.0609 55  PRO A CB  
19   C CG  . PRO A 40  ? 0.4427 0.7924 0.4863 -0.0225 -0.1516 -0.0686 55  PRO A CG  
20   C CD  . PRO A 40  ? 0.4681 0.8104 0.4958 -0.0176 -0.1639 -0.0795 55  PRO A CD  
21   N N   . PRO A 41  ? 0.3748 0.7601 0.4041 -0.0160 -0.1457 -0.0540 56  PRO A N   
22   C CA  . PRO A 41  ? 0.3744 0.7632 0.3852 -0.0103 -0.1422 -0.0511 56  PRO A CA  
23   C C   . PRO A 41  ? 0.3761 0.7613 0.3661 -0.0056 -0.1324 -0.0503 56  PRO A C   
24   O O   . PRO A 41  ? 0.4026 0.7872 0.3725 -0.0001 -0.1330 -0.0511 56  PRO A O   
25   C CB  . PRO A 41  ? 0.3527 0.7518 0.3782 -0.0130 -0.1366 -0.0421 56  PRO A CB  
26   C CG  . PRO A 41  ? 0.3485 0.7523 0.3998 -0.0189 -0.1424 -0.0421 56  PRO A CG  
27   C CD  . PRO A 41  ? 0.3511 0.7461 0.4063 -0.0222 -0.1441 -0.0472 56  PRO A CD  
28   N N   . HIS A 42  ? 0.3515 0.7355 0.3463 -0.0074 -0.1237 -0.0480 57  HIS A N   
29   C CA  . HIS A 42  ? 0.3475 0.7313 0.3260 -0.0033 -0.1143 -0.0461 57  HIS A CA  
30   C C   . HIS A 42  ? 0.3661 0.7437 0.3255 0.0033  -0.1178 -0.0542 57  HIS A C   
31   O O   . HIS A 42  ? 0.3729 0.7534 0.3147 0.0082  -0.1126 -0.0523 57  HIS A O   
32   C CB  . HIS A 42  ? 0.3333 0.7182 0.3207 -0.0060 -0.1048 -0.0417 57  HIS A CB  
33   C CG  . HIS A 42  ? 0.3307 0.7084 0.3268 -0.0072 -0.1072 -0.0466 57  HIS A CG  
34   N ND1 . HIS A 42  ? 0.3270 0.7024 0.3418 -0.0127 -0.1126 -0.0470 57  HIS A ND1 
35   C CD2 . HIS A 42  ? 0.3387 0.7112 0.3285 -0.0036 -0.1043 -0.0503 57  HIS A CD2 
36   C CE1 . HIS A 42  ? 0.3303 0.6972 0.3488 -0.0130 -0.1137 -0.0507 57  HIS A CE1 
37   N NE2 . HIS A 42  ? 0.3459 0.7103 0.3490 -0.0069 -0.1090 -0.0533 57  HIS A NE2 
38   N N   . LEU A 43  ? 0.3716 0.7406 0.3342 0.0036  -0.1264 -0.0628 58  LEU A N   
39   C CA  . LEU A 43  ? 0.3977 0.7587 0.3400 0.0113  -0.1315 -0.0726 58  LEU A CA  
40   C C   . LEU A 43  ? 0.4169 0.7778 0.3443 0.0151  -0.1405 -0.0761 58  LEU A C   
41   O O   . LEU A 43  ? 0.4263 0.7858 0.3301 0.0232  -0.1396 -0.0796 58  LEU A O   
42   C CB  . LEU A 43  ? 0.4061 0.7548 0.3560 0.0104  -0.1397 -0.0816 58  LEU A CB  
43   C CG  . LEU A 43  ? 0.3899 0.7360 0.3520 0.0080  -0.1322 -0.0789 58  LEU A CG  
44   C CD1 . LEU A 43  ? 0.4045 0.7356 0.3736 0.0068  -0.1423 -0.0877 58  LEU A CD1 
45   C CD2 . LEU A 43  ? 0.3898 0.7394 0.3367 0.0154  -0.1211 -0.0778 58  LEU A CD2 
46   N N   . LEU A 44  ? 0.4183 0.7817 0.3597 0.0099  -0.1489 -0.0746 59  LEU A N   
47   C CA  . LEU A 44  ? 0.4446 0.8078 0.3736 0.0135  -0.1593 -0.0780 59  LEU A CA  
48   C C   . LEU A 44  ? 0.4364 0.8054 0.3449 0.0189  -0.1516 -0.0714 59  LEU A C   
49   O O   . LEU A 44  ? 0.4521 0.8176 0.3365 0.0264  -0.1547 -0.0758 59  LEU A O   
50   C CB  . LEU A 44  ? 0.4465 0.8150 0.3980 0.0068  -0.1681 -0.0755 59  LEU A CB  
51   C CG  . LEU A 44  ? 0.4707 0.8393 0.4160 0.0094  -0.1827 -0.0799 59  LEU A CG  
52   C CD1 . LEU A 44  ? 0.4655 0.8426 0.4045 0.0118  -0.1795 -0.0711 59  LEU A CD1 
53   C CD2 . LEU A 44  ? 0.5090 0.8664 0.4284 0.0170  -0.1917 -0.0913 59  LEU A CD2 
54   N N   . PHE A 45  ? 0.4148 0.7916 0.3319 0.0152  -0.1412 -0.0607 60  PHE A N   
55   C CA  . PHE A 45  ? 0.4088 0.7902 0.3095 0.0186  -0.1342 -0.0527 60  PHE A CA  
56   C C   . PHE A 45  ? 0.4118 0.7937 0.2954 0.0233  -0.1238 -0.0521 60  PHE A C   
57   O O   . PHE A 45  ? 0.4217 0.8061 0.2859 0.0278  -0.1196 -0.0476 60  PHE A O   
58   C CB  . PHE A 45  ? 0.3867 0.7740 0.3022 0.0130  -0.1281 -0.0423 60  PHE A CB  
59   C CG  . PHE A 45  ? 0.3897 0.7791 0.3208 0.0103  -0.1371 -0.0419 60  PHE A CG  
60   C CD1 . PHE A 45  ? 0.4125 0.8016 0.3331 0.0143  -0.1462 -0.0420 60  PHE A CD1 
61   C CD2 . PHE A 45  ? 0.3720 0.7645 0.3283 0.0043  -0.1371 -0.0414 60  PHE A CD2 
62   C CE1 . PHE A 45  ? 0.4127 0.8057 0.3496 0.0125  -0.1553 -0.0419 60  PHE A CE1 
63   C CE2 . PHE A 45  ? 0.3765 0.7738 0.3491 0.0023  -0.1448 -0.0406 60  PHE A CE2 
64   C CZ  . PHE A 45  ? 0.3991 0.7972 0.3631 0.0065  -0.1542 -0.0411 60  PHE A CZ  
65   N N   . THR A 46  ? 0.4000 0.7802 0.2910 0.0226  -0.1195 -0.0560 61  THR A N   
66   C CA  . THR A 46  ? 0.4119 0.7942 0.2879 0.0285  -0.1102 -0.0564 61  THR A CA  
67   C C   . THR A 46  ? 0.4480 0.8249 0.2990 0.0381  -0.1164 -0.0652 61  THR A C   
68   O O   . THR A 46  ? 0.4505 0.8322 0.2813 0.0440  -0.1102 -0.0615 61  THR A O   
69   C CB  . THR A 46  ? 0.3910 0.7719 0.2797 0.0272  -0.1054 -0.0592 61  THR A CB  
70   O OG1 . THR A 46  ? 0.3668 0.7533 0.2740 0.0195  -0.0988 -0.0504 61  THR A OG1 
71   C CG2 . THR A 46  ? 0.3962 0.7805 0.2697 0.0349  -0.0968 -0.0606 61  THR A CG2 
72   N N   . GLN A 47  ? 0.4701 0.8369 0.3231 0.0390  -0.1290 -0.0763 62  GLN A N   
73   C CA  . GLN A 47  ? 0.5170 0.8756 0.3469 0.0479  -0.1384 -0.0869 62  GLN A CA  
74   C C   . GLN A 47  ? 0.5287 0.8901 0.3390 0.0519  -0.1424 -0.0835 62  GLN A C   
75   O O   . GLN A 47  ? 0.5499 0.9091 0.3329 0.0617  -0.1427 -0.0878 62  GLN A O   
76   C CB  . GLN A 47  ? 0.5468 0.8941 0.3892 0.0446  -0.1536 -0.0975 62  GLN A CB  
77   C CG  . GLN A 47  ? 0.5979 0.9319 0.4235 0.0530  -0.1614 -0.1119 62  GLN A CG  
78   C CD  . GLN A 47  ? 0.6279 0.9508 0.4756 0.0465  -0.1708 -0.1191 62  GLN A CD  
79   O OE1 . GLN A 47  ? 0.6153 0.9388 0.4800 0.0423  -0.1627 -0.1156 62  GLN A OE1 
80   N NE2 . GLN A 47  ? 0.6452 0.9579 0.4939 0.0451  -0.1885 -0.1286 62  GLN A NE2 
81   N N   . LEU A 48  ? 0.5147 0.8806 0.3373 0.0454  -0.1452 -0.0755 63  LEU A N   
82   C CA  . LEU A 48  ? 0.5421 0.9093 0.3456 0.0498  -0.1499 -0.0719 63  LEU A CA  
83   C C   . LEU A 48  ? 0.5481 0.9227 0.3349 0.0530  -0.1359 -0.0607 63  LEU A C   
84   O O   . LEU A 48  ? 0.5702 0.9450 0.3363 0.0581  -0.1380 -0.0569 63  LEU A O   
85   C CB  . LEU A 48  ? 0.5319 0.9014 0.3532 0.0432  -0.1580 -0.0667 63  LEU A CB  
86   C CG  . LEU A 48  ? 0.5226 0.8883 0.3648 0.0385  -0.1725 -0.0751 63  LEU A CG  
87   C CD1 . LEU A 48  ? 0.5173 0.8883 0.3728 0.0349  -0.1797 -0.0692 63  LEU A CD1 
88   C CD2 . LEU A 48  ? 0.5484 0.9043 0.3740 0.0448  -0.1855 -0.0889 63  LEU A CD2 
89   N N   . SER A 49  ? 0.5489 0.9298 0.3454 0.0497  -0.1222 -0.0545 64  SER A N   
90   C CA  . SER A 49  ? 0.5598 0.9491 0.3469 0.0498  -0.1093 -0.0417 64  SER A CA  
91   C C   . SER A 49  ? 0.6005 0.9925 0.3590 0.0602  -0.1034 -0.0429 64  SER A C   
92   O O   . SER A 49  ? 0.5954 0.9928 0.3388 0.0621  -0.0965 -0.0327 64  SER A O   
93   C CB  . SER A 49  ? 0.5405 0.9362 0.3490 0.0423  -0.0983 -0.0349 64  SER A CB  
94   O OG  . SER A 49  ? 0.5467 0.9396 0.3783 0.0341  -0.1041 -0.0337 64  SER A OG  
95   N N   . SER A 50  ? 0.6499 1.0373 0.4002 0.0673  -0.1064 -0.0555 65  SER A N   
96   C CA  . SER A 50  ? 0.7231 1.1118 0.4430 0.0796  -0.1025 -0.0594 65  SER A CA  
97   C C   . SER A 50  ? 0.7717 1.1567 0.4665 0.0850  -0.1102 -0.0578 65  SER A C   
98   O O   . SER A 50  ? 0.8136 1.2059 0.4893 0.0891  -0.1010 -0.0476 65  SER A O   
99   C CB  . SER A 50  ? 0.7590 1.1381 0.4738 0.0870  -0.1094 -0.0762 65  SER A CB  
100  O OG  . SER A 50  ? 0.7537 1.1320 0.4963 0.0799  -0.1076 -0.0784 65  SER A OG  
101  N N   . GLN A 51  ? 0.7672 1.1415 0.4629 0.0846  -0.1273 -0.0670 66  GLN A N   
102  C CA  . GLN A 51  ? 0.7991 1.1682 0.4669 0.0925  -0.1374 -0.0692 66  GLN A CA  
103  C C   . GLN A 51  ? 0.7452 1.1175 0.4168 0.0869  -0.1386 -0.0556 66  GLN A C   
104  O O   . GLN A 51  ? 0.7415 1.1154 0.3879 0.0929  -0.1361 -0.0481 66  GLN A O   
105  C CB  . GLN A 51  ? 0.8525 1.2084 0.5169 0.0960  -0.1571 -0.0864 66  GLN A CB  
106  C CG  . GLN A 51  ? 0.8456 1.1973 0.5458 0.0848  -0.1668 -0.0917 66  GLN A CG  
107  C CD  . GLN A 51  ? 0.8723 1.2132 0.5753 0.0874  -0.1747 -0.1080 66  GLN A CD  
108  O OE1 . GLN A 51  ? 0.9652 1.2971 0.6410 0.0983  -0.1818 -0.1197 66  GLN A OE1 
109  N NE2 . GLN A 51  ? 0.8174 1.1577 0.5520 0.0777  -0.1742 -0.1089 66  GLN A NE2 
110  N N   . TYR A 52  ? 0.6808 1.0535 0.3831 0.0760  -0.1421 -0.0521 67  TYR A N   
111  C CA  . TYR A 52  ? 0.6558 1.0303 0.3648 0.0709  -0.1433 -0.0398 67  TYR A CA  
112  C C   . TYR A 52  ? 0.6258 1.0078 0.3507 0.0633  -0.1272 -0.0278 67  TYR A C   
113  O O   . TYR A 52  ? 0.6414 1.0279 0.3692 0.0634  -0.1171 -0.0299 67  TYR A O   
114  C CB  . TYR A 52  ? 0.6445 1.0150 0.3754 0.0658  -0.1589 -0.0454 67  TYR A CB  
115  C CG  . TYR A 52  ? 0.6679 1.0309 0.3869 0.0722  -0.1762 -0.0602 67  TYR A CG  
116  C CD1 . TYR A 52  ? 0.6908 1.0501 0.3843 0.0801  -0.1867 -0.0607 67  TYR A CD1 
117  C CD2 . TYR A 52  ? 0.6612 1.0198 0.3934 0.0704  -0.1827 -0.0737 67  TYR A CD2 
118  C CE1 . TYR A 52  ? 0.7172 1.0690 0.3991 0.0859  -0.2038 -0.0749 67  TYR A CE1 
119  C CE2 . TYR A 52  ? 0.6748 1.0250 0.3971 0.0753  -0.1998 -0.0876 67  TYR A CE2 
120  C CZ  . TYR A 52  ? 0.7151 1.0621 0.4120 0.0832  -0.2107 -0.0887 67  TYR A CZ  
121  O OH  . TYR A 52  ? 0.7417 1.0794 0.4270 0.0883  -0.2293 -0.1034 67  TYR A OH  
122  N N   . GLY A 53  ? 0.6046 0.9878 0.3389 0.0573  -0.1246 -0.0155 68  GLY A N   
123  C CA  . GLY A 53  ? 0.5888 0.9783 0.3344 0.0505  -0.1094 -0.0040 68  GLY A CA  
124  C C   . GLY A 53  ? 0.5507 0.9432 0.3245 0.0431  -0.1049 -0.0078 68  GLY A C   
125  O O   . GLY A 53  ? 0.5501 0.9401 0.3350 0.0432  -0.1118 -0.0193 68  GLY A O   
126  N N   . PRO A 54  ? 0.5218 0.9189 0.3073 0.0363  -0.0940 0.0024  69  PRO A N   
127  C CA  . PRO A 54  ? 0.4848 0.8839 0.2967 0.0289  -0.0906 0.0006  69  PRO A CA  
128  C C   . PRO A 54  ? 0.4582 0.8529 0.2882 0.0220  -0.0945 0.0056  69  PRO A C   
129  O O   . PRO A 54  ? 0.4344 0.8300 0.2842 0.0165  -0.0923 0.0045  69  PRO A O   
130  C CB  . PRO A 54  ? 0.4758 0.8836 0.2872 0.0267  -0.0767 0.0081  69  PRO A CB  
131  C CG  . PRO A 54  ? 0.4975 0.9066 0.2897 0.0284  -0.0725 0.0196  69  PRO A CG  
132  C CD  . PRO A 54  ? 0.5258 0.9282 0.2983 0.0359  -0.0828 0.0155  69  PRO A CD  
133  N N   . LEU A 55  ? 0.4652 0.8547 0.2867 0.0235  -0.1006 0.0108  70  LEU A N   
134  C CA  . LEU A 55  ? 0.4511 0.8356 0.2870 0.0198  -0.1056 0.0142  70  LEU A CA  
135  C C   . LEU A 55  ? 0.4741 0.8556 0.3090 0.0248  -0.1193 0.0077  70  LEU A C   
136  O O   . LEU A 55  ? 0.5051 0.8844 0.3205 0.0308  -0.1251 0.0080  70  LEU A O   
137  C CB  . LEU A 55  ? 0.4465 0.8269 0.2744 0.0173  -0.1008 0.0276  70  LEU A CB  
138  C CG  . LEU A 55  ? 0.4342 0.8069 0.2728 0.0148  -0.1053 0.0325  70  LEU A CG  
139  C CD1 . LEU A 55  ? 0.4129 0.7869 0.2741 0.0090  -0.1018 0.0296  70  LEU A CD1 
140  C CD2 . LEU A 55  ? 0.4451 0.8107 0.2711 0.0132  -0.1022 0.0459  70  LEU A CD2 
141  N N   . PHE A 56  ? 0.4769 0.8593 0.3335 0.0222  -0.1244 0.0025  71  PHE A N   
142  C CA  . PHE A 56  ? 0.4905 0.8734 0.3535 0.0254  -0.1372 -0.0044 71  PHE A CA  
143  C C   . PHE A 56  ? 0.4720 0.8550 0.3535 0.0235  -0.1399 -0.0008 71  PHE A C   
144  O O   . PHE A 56  ? 0.4638 0.8481 0.3607 0.0188  -0.1329 0.0010  71  PHE A O   
145  C CB  . PHE A 56  ? 0.5014 0.8879 0.3777 0.0235  -0.1399 -0.0152 71  PHE A CB  
146  C CG  . PHE A 56  ? 0.5451 0.9300 0.4054 0.0286  -0.1472 -0.0236 71  PHE A CG  
147  C CD1 . PHE A 56  ? 0.5781 0.9618 0.4189 0.0317  -0.1402 -0.0248 71  PHE A CD1 
148  C CD2 . PHE A 56  ? 0.5760 0.9608 0.4402 0.0311  -0.1617 -0.0306 71  PHE A CD2 
149  C CE1 . PHE A 56  ? 0.6161 0.9968 0.4387 0.0381  -0.1474 -0.0337 71  PHE A CE1 
150  C CE2 . PHE A 56  ? 0.6056 0.9867 0.4526 0.0363  -0.1704 -0.0396 71  PHE A CE2 
151  C CZ  . PHE A 56  ? 0.6256 1.0038 0.4503 0.0404  -0.1631 -0.0416 71  PHE A CZ  
152  N N   . GLY A 57  ? 0.4748 0.8571 0.3549 0.0281  -0.1503 -0.0004 72  GLY A N   
153  C CA  . GLY A 57  ? 0.4631 0.8467 0.3607 0.0286  -0.1537 0.0026  72  GLY A CA  
154  C C   . GLY A 57  ? 0.4588 0.8510 0.3754 0.0297  -0.1645 -0.0050 72  GLY A C   
155  O O   . GLY A 57  ? 0.4716 0.8650 0.3813 0.0339  -0.1759 -0.0089 72  GLY A O   
156  N N   . LEU A 58  ? 0.4404 0.8390 0.3814 0.0257  -0.1608 -0.0067 73  LEU A N   
157  C CA  . LEU A 58  ? 0.4316 0.8406 0.3958 0.0253  -0.1691 -0.0119 73  LEU A CA  
158  C C   . LEU A 58  ? 0.4496 0.8625 0.4266 0.0293  -0.1703 -0.0066 73  LEU A C   
159  O O   . LEU A 58  ? 0.4443 0.8520 0.4193 0.0297  -0.1614 -0.0008 73  LEU A O   
160  C CB  . LEU A 58  ? 0.3960 0.8100 0.3785 0.0185  -0.1626 -0.0157 73  LEU A CB  
161  C CG  . LEU A 58  ? 0.4011 0.8091 0.3691 0.0158  -0.1593 -0.0202 73  LEU A CG  
162  C CD1 . LEU A 58  ? 0.3875 0.7971 0.3690 0.0098  -0.1497 -0.0212 73  LEU A CD1 
163  C CD2 . LEU A 58  ? 0.4236 0.8318 0.3876 0.0169  -0.1716 -0.0286 73  LEU A CD2 
164  N N   . TYR A 59  ? 0.4743 0.8962 0.4644 0.0328  -0.1819 -0.0088 74  TYR A N   
165  C CA  . TYR A 59  ? 0.5028 0.9310 0.5079 0.0381  -0.1834 -0.0043 74  TYR A CA  
166  C C   . TYR A 59  ? 0.5385 0.9840 0.5768 0.0356  -0.1847 -0.0070 74  TYR A C   
167  O O   . TYR A 59  ? 0.5887 1.0423 0.6389 0.0316  -0.1924 -0.0125 74  TYR A O   
168  C CB  . TYR A 59  ? 0.5087 0.9345 0.5019 0.0459  -0.1954 -0.0023 74  TYR A CB  
169  C CG  . TYR A 59  ? 0.5237 0.9329 0.4851 0.0484  -0.1926 0.0029  74  TYR A CG  
170  C CD1 . TYR A 59  ? 0.5312 0.9339 0.4708 0.0460  -0.1931 0.0003  74  TYR A CD1 
171  C CD2 . TYR A 59  ? 0.5392 0.9388 0.4923 0.0533  -0.1890 0.0107  74  TYR A CD2 
172  C CE1 . TYR A 59  ? 0.5560 0.9455 0.4676 0.0480  -0.1891 0.0066  74  TYR A CE1 
173  C CE2 . TYR A 59  ? 0.5557 0.9400 0.4813 0.0543  -0.1862 0.0170  74  TYR A CE2 
174  C CZ  . TYR A 59  ? 0.5639 0.9445 0.4693 0.0514  -0.1858 0.0156  74  TYR A CZ  
175  O OH  . TYR A 59  ? 0.5738 0.9414 0.4532 0.0521  -0.1818 0.0233  74  TYR A OH  
176  N N   . ALA A 60  ? 0.5906 1.0413 0.6434 0.0381  -0.1769 -0.0029 75  ALA A N   
177  C CA  . ALA A 60  ? 0.6205 1.0900 0.7057 0.0369  -0.1764 -0.0034 75  ALA A CA  
178  C C   . ALA A 60  ? 0.6598 1.1331 0.7538 0.0443  -0.1693 0.0016  75  ALA A C   
179  O O   . ALA A 60  ? 0.6300 1.0958 0.7178 0.0439  -0.1577 0.0037  75  ALA A O   
180  C CB  . ALA A 60  ? 0.6091 1.0819 0.7051 0.0275  -0.1688 -0.0060 75  ALA A CB  
181  N N   . GLY A 61  ? 0.7971 1.2824 0.9057 0.0518  -0.1768 0.0031  76  GLY A N   
182  C CA  . GLY A 61  ? 0.8687 1.3568 0.9840 0.0613  -0.1710 0.0072  76  GLY A CA  
183  C C   . GLY A 61  ? 0.9272 1.3935 1.0137 0.0679  -0.1718 0.0101  76  GLY A C   
184  O O   . GLY A 61  ? 0.9223 1.3792 0.9912 0.0684  -0.1810 0.0102  76  GLY A O   
185  N N   . PRO A 62  ? 0.9677 1.4249 1.0485 0.0730  -0.1624 0.0127  77  PRO A N   
186  C CA  . PRO A 62  ? 0.9510 1.3856 1.0056 0.0781  -0.1639 0.0161  77  PRO A CA  
187  C C   . PRO A 62  ? 0.8803 1.2964 0.9112 0.0692  -0.1582 0.0166  77  PRO A C   
188  O O   . PRO A 62  ? 0.8919 1.2898 0.9005 0.0708  -0.1609 0.0203  77  PRO A O   
189  C CB  . PRO A 62  ? 0.9973 1.4296 1.0572 0.0876  -0.1572 0.0176  77  PRO A CB  
190  C CG  . PRO A 62  ? 0.9763 1.4243 1.0559 0.0836  -0.1467 0.0151  77  PRO A CG  
191  C CD  . PRO A 62  ? 0.9525 1.4183 1.0487 0.0745  -0.1506 0.0128  77  PRO A CD  
192  N N   . HIS A 63  ? 0.7883 1.2093 0.8246 0.0601  -0.1505 0.0137  78  HIS A N   
193  C CA  . HIS A 63  ? 0.7541 1.1599 0.7713 0.0525  -0.1437 0.0144  78  HIS A CA  
194  C C   . HIS A 63  ? 0.6464 1.0501 0.6513 0.0457  -0.1478 0.0131  78  HIS A C   
195  O O   . HIS A 63  ? 0.6254 1.0414 0.6413 0.0421  -0.1517 0.0089  78  HIS A O   
196  C CB  . HIS A 63  ? 0.8197 1.2302 0.8469 0.0473  -0.1327 0.0123  78  HIS A CB  
197  C CG  . HIS A 63  ? 0.9210 1.3314 0.9554 0.0544  -0.1269 0.0131  78  HIS A CG  
198  N ND1 . HIS A 63  ? 0.9961 1.3881 1.0146 0.0587  -0.1249 0.0154  78  HIS A ND1 
199  C CD2 . HIS A 63  ? 0.9494 1.3760 1.0049 0.0584  -0.1227 0.0120  78  HIS A CD2 
200  C CE1 . HIS A 63  ? 1.0111 1.4065 1.0384 0.0660  -0.1201 0.0145  78  HIS A CE1 
201  N NE2 . HIS A 63  ? 1.0058 1.4233 1.0557 0.0663  -0.1178 0.0128  78  HIS A NE2 
202  N N   . LEU A 64  ? 0.5613 0.9491 0.5433 0.0440  -0.1467 0.0168  79  LEU A N   
203  C CA  . LEU A 64  ? 0.5150 0.9007 0.4829 0.0384  -0.1479 0.0159  79  LEU A CA  
204  C C   . LEU A 64  ? 0.4670 0.8541 0.4380 0.0303  -0.1382 0.0132  79  LEU A C   
205  O O   . LEU A 64  ? 0.4592 0.8414 0.4323 0.0287  -0.1304 0.0149  79  LEU A O   
206  C CB  . LEU A 64  ? 0.5257 0.8959 0.4687 0.0400  -0.1497 0.0225  79  LEU A CB  
207  C CG  . LEU A 64  ? 0.5273 0.8934 0.4514 0.0348  -0.1472 0.0236  79  LEU A CG  
208  C CD1 . LEU A 64  ? 0.5169 0.8924 0.4395 0.0354  -0.1543 0.0177  79  LEU A CD1 
209  C CD2 . LEU A 64  ? 0.5507 0.9020 0.4532 0.0367  -0.1480 0.0326  79  LEU A CD2 
210  N N   . THR A 65  ? 0.4367 0.8300 0.4076 0.0260  -0.1394 0.0087  80  THR A N   
211  C CA  . THR A 65  ? 0.4110 0.8050 0.3831 0.0192  -0.1311 0.0063  80  THR A CA  
212  C C   . THR A 65  ? 0.4175 0.8069 0.3703 0.0168  -0.1307 0.0059  80  THR A C   
213  O O   . THR A 65  ? 0.4271 0.8202 0.3764 0.0179  -0.1375 0.0012  80  THR A O   
214  C CB  . THR A 65  ? 0.3913 0.7975 0.3852 0.0163  -0.1311 0.0007  80  THR A CB  
215  O OG1 . THR A 65  ? 0.3763 0.7884 0.3876 0.0187  -0.1284 0.0023  80  THR A OG1 
216  C CG2 . THR A 65  ? 0.3788 0.7842 0.3720 0.0101  -0.1236 -0.0016 80  THR A CG2 
217  N N   . LEU A 66  ? 0.3928 0.7746 0.3335 0.0138  -0.1229 0.0106  81  LEU A N   
218  C CA  . LEU A 66  ? 0.3929 0.7726 0.3165 0.0120  -0.1201 0.0114  81  LEU A CA  
219  C C   . LEU A 66  ? 0.3821 0.7671 0.3123 0.0076  -0.1142 0.0063  81  LEU A C   
220  O O   . LEU A 66  ? 0.3801 0.7662 0.3220 0.0041  -0.1085 0.0063  81  LEU A O   
221  C CB  . LEU A 66  ? 0.3991 0.7697 0.3092 0.0102  -0.1146 0.0204  81  LEU A CB  
222  C CG  . LEU A 66  ? 0.4249 0.7871 0.3179 0.0139  -0.1188 0.0278  81  LEU A CG  
223  C CD1 . LEU A 66  ? 0.4394 0.8030 0.3312 0.0208  -0.1298 0.0253  81  LEU A CD1 
224  C CD2 . LEU A 66  ? 0.4230 0.7744 0.3161 0.0119  -0.1161 0.0354  81  LEU A CD2 
225  N N   . VAL A 67  ? 0.3917 0.7791 0.3128 0.0085  -0.1156 0.0019  82  VAL A N   
226  C CA  . VAL A 67  ? 0.3804 0.7711 0.3057 0.0054  -0.1098 -0.0024 82  VAL A CA  
227  C C   . VAL A 67  ? 0.3921 0.7819 0.2995 0.0058  -0.1033 0.0011  82  VAL A C   
228  O O   . VAL A 67  ? 0.4124 0.8012 0.3024 0.0101  -0.1063 0.0013  82  VAL A O   
229  C CB  . VAL A 67  ? 0.3890 0.7827 0.3198 0.0068  -0.1167 -0.0118 82  VAL A CB  
230  C CG1 . VAL A 67  ? 0.3847 0.7799 0.3209 0.0040  -0.1110 -0.0160 82  VAL A CG1 
231  C CG2 . VAL A 67  ? 0.3853 0.7825 0.3355 0.0061  -0.1236 -0.0139 82  VAL A CG2 
232  N N   . VAL A 68  ? 0.3674 0.7589 0.2794 0.0016  -0.0944 0.0040  83  VAL A N   
233  C CA  . VAL A 68  ? 0.3650 0.7586 0.2647 0.0009  -0.0868 0.0094  83  VAL A CA  
234  C C   . VAL A 68  ? 0.3543 0.7539 0.2550 0.0016  -0.0817 0.0041  83  VAL A C   
235  O O   . VAL A 68  ? 0.3419 0.7434 0.2565 -0.0018 -0.0784 0.0025  83  VAL A O   
236  C CB  . VAL A 68  ? 0.3604 0.7520 0.2657 -0.0048 -0.0810 0.0178  83  VAL A CB  
237  C CG1 . VAL A 68  ? 0.3736 0.7688 0.2673 -0.0062 -0.0740 0.0252  83  VAL A CG1 
238  C CG2 . VAL A 68  ? 0.3672 0.7506 0.2730 -0.0051 -0.0859 0.0224  83  VAL A CG2 
239  N N   . SER A 69  ? 0.3604 0.7626 0.2453 0.0068  -0.0811 0.0016  84  SER A N   
240  C CA  . SER A 69  ? 0.3625 0.7690 0.2466 0.0099  -0.0774 -0.0051 84  SER A CA  
241  C C   . SER A 69  ? 0.3690 0.7837 0.2423 0.0120  -0.0674 -0.0001 84  SER A C   
242  O O   . SER A 69  ? 0.3836 0.8015 0.2488 0.0180  -0.0654 -0.0061 84  SER A O   
243  C CB  . SER A 69  ? 0.3711 0.7733 0.2475 0.0159  -0.0862 -0.0158 84  SER A CB  
244  O OG  . SER A 69  ? 0.3636 0.7612 0.2550 0.0130  -0.0947 -0.0201 84  SER A OG  
245  N N   . GLU A 70  ? 0.3703 0.7886 0.2445 0.0072  -0.0613 0.0108  85  GLU A N   
246  C CA  . GLU A 70  ? 0.3923 0.8209 0.2586 0.0083  -0.0514 0.0174  85  GLU A CA  
247  C C   . GLU A 70  ? 0.3917 0.8241 0.2715 -0.0004 -0.0459 0.0274  85  GLU A C   
248  O O   . GLU A 70  ? 0.3804 0.8049 0.2642 -0.0059 -0.0497 0.0326  85  GLU A O   
249  C CB  . GLU A 70  ? 0.4270 0.8557 0.2714 0.0130  -0.0509 0.0225  85  GLU A CB  
250  C CG  . GLU A 70  ? 0.4406 0.8819 0.2742 0.0156  -0.0396 0.0302  85  GLU A CG  
251  C CD  . GLU A 70  ? 0.4385 0.8849 0.2797 0.0066  -0.0329 0.0451  85  GLU A CD  
252  O OE1 . GLU A 70  ? 0.4347 0.8714 0.2766 0.0010  -0.0375 0.0517  85  GLU A OE1 
253  O OE2 . GLU A 70  ? 0.4435 0.9036 0.2903 0.0054  -0.0231 0.0502  85  GLU A OE2 
254  N N   . ILE A 71  ? 0.4012 0.8455 0.2873 -0.0011 -0.0375 0.0298  86  ILE A N   
255  C CA  . ILE A 71  ? 0.3853 0.8346 0.2877 -0.0097 -0.0334 0.0373  86  ILE A CA  
256  C C   . ILE A 71  ? 0.3844 0.8303 0.2857 -0.0172 -0.0330 0.0494  86  ILE A C   
257  O O   . ILE A 71  ? 0.3847 0.8232 0.2968 -0.0241 -0.0367 0.0516  86  ILE A O   
258  C CB  . ILE A 71  ? 0.3935 0.8595 0.3026 -0.0082 -0.0243 0.0388  86  ILE A CB  
259  C CG1 . ILE A 71  ? 0.3837 0.8543 0.3111 -0.0175 -0.0226 0.0456  86  ILE A CG1 
260  C CG2 . ILE A 71  ? 0.4161 0.8946 0.3121 -0.0040 -0.0158 0.0458  86  ILE A CG2 
261  C CD1 . ILE A 71  ? 0.3747 0.8356 0.3145 -0.0204 -0.0292 0.0389  86  ILE A CD1 
262  N N   . GLY A 72  ? 0.3942 0.8437 0.2812 -0.0155 -0.0291 0.0571  87  GLY A N   
263  C CA  . GLY A 72  ? 0.3995 0.8433 0.2852 -0.0232 -0.0293 0.0698  87  GLY A CA  
264  C C   . GLY A 72  ? 0.3910 0.8164 0.2757 -0.0247 -0.0393 0.0676  87  GLY A C   
265  O O   . GLY A 72  ? 0.3923 0.8089 0.2847 -0.0322 -0.0423 0.0733  87  GLY A O   
266  N N   . LEU A 73  ? 0.3881 0.8075 0.2635 -0.0173 -0.0453 0.0588  88  LEU A N   
267  C CA  . LEU A 73  ? 0.3804 0.7852 0.2569 -0.0176 -0.0544 0.0565  88  LEU A CA  
268  C C   . LEU A 73  ? 0.3582 0.7600 0.2527 -0.0219 -0.0566 0.0515  88  LEU A C   
269  O O   . LEU A 73  ? 0.3648 0.7566 0.2643 -0.0265 -0.0599 0.0555  88  LEU A O   
270  C CB  . LEU A 73  ? 0.3801 0.7815 0.2463 -0.0091 -0.0612 0.0478  88  LEU A CB  
271  C CG  . LEU A 73  ? 0.3982 0.8000 0.2432 -0.0044 -0.0605 0.0535  88  LEU A CG  
272  C CD1 . LEU A 73  ? 0.4085 0.8096 0.2432 0.0045  -0.0672 0.0428  88  LEU A CD1 
273  C CD2 . LEU A 73  ? 0.4075 0.7980 0.2472 -0.0075 -0.0641 0.0638  88  LEU A CD2 
274  N N   . VAL A 74  ? 0.3427 0.7517 0.2458 -0.0200 -0.0547 0.0432  89  VAL A N   
275  C CA  . VAL A 74  ? 0.3328 0.7379 0.2511 -0.0235 -0.0571 0.0391  89  VAL A CA  
276  C C   . VAL A 74  ? 0.3326 0.7370 0.2585 -0.0316 -0.0544 0.0470  89  VAL A C   
277  O O   . VAL A 74  ? 0.3199 0.7148 0.2520 -0.0347 -0.0585 0.0467  89  VAL A O   
278  C CB  . VAL A 74  ? 0.3265 0.7376 0.2537 -0.0207 -0.0560 0.0299  89  VAL A CB  
279  C CG1 . VAL A 74  ? 0.3305 0.7440 0.2495 -0.0135 -0.0578 0.0225  89  VAL A CG1 
280  C CG2 . VAL A 74  ? 0.3303 0.7515 0.2654 -0.0238 -0.0496 0.0323  89  VAL A CG2 
281  N N   . ARG A 75  ? 0.3461 0.7605 0.2713 -0.0348 -0.0481 0.0543  90  ARG A N   
282  C CA  . ARG A 75  ? 0.3606 0.7749 0.2949 -0.0436 -0.0468 0.0621  90  ARG A CA  
283  C C   . ARG A 75  ? 0.3653 0.7637 0.2944 -0.0475 -0.0522 0.0684  90  ARG A C   
284  O O   . ARG A 75  ? 0.3605 0.7502 0.2968 -0.0537 -0.0558 0.0707  90  ARG A O   
285  C CB  . ARG A 75  ? 0.3939 0.8246 0.3305 -0.0465 -0.0385 0.0701  90  ARG A CB  
286  C CG  . ARG A 75  ? 0.4070 0.8534 0.3514 -0.0426 -0.0334 0.0641  90  ARG A CG  
287  C CD  . ARG A 75  ? 0.4369 0.9022 0.3868 -0.0455 -0.0245 0.0732  90  ARG A CD  
288  N NE  . ARG A 75  ? 0.4611 0.9319 0.4291 -0.0532 -0.0251 0.0758  90  ARG A NE  
289  C CZ  . ARG A 75  ? 0.4677 0.9480 0.4466 -0.0508 -0.0240 0.0698  90  ARG A CZ  
290  N NH1 . ARG A 75  ? 0.4622 0.9473 0.4365 -0.0409 -0.0215 0.0609  90  ARG A NH1 
291  N NH2 . ARG A 75  ? 0.4856 0.9700 0.4800 -0.0582 -0.0261 0.0729  90  ARG A NH2 
292  N N   . GLU A 76  ? 0.3831 0.7764 0.2987 -0.0434 -0.0536 0.0710  91  GLU A N   
293  C CA  . GLU A 76  ? 0.3995 0.7763 0.3094 -0.0462 -0.0591 0.0775  91  GLU A CA  
294  C C   . GLU A 76  ? 0.3977 0.7610 0.3129 -0.0444 -0.0664 0.0699  91  GLU A C   
295  O O   . GLU A 76  ? 0.3821 0.7314 0.2989 -0.0487 -0.0709 0.0735  91  GLU A O   
296  C CB  . GLU A 76  ? 0.4174 0.7915 0.3107 -0.0405 -0.0600 0.0810  91  GLU A CB  
297  C CG  . GLU A 76  ? 0.4407 0.7980 0.3269 -0.0436 -0.0648 0.0905  91  GLU A CG  
298  C CD  . GLU A 76  ? 0.4631 0.8179 0.3312 -0.0378 -0.0657 0.0957  91  GLU A CD  
299  O OE1 . GLU A 76  ? 0.4555 0.8225 0.3145 -0.0319 -0.0619 0.0931  91  GLU A OE1 
300  O OE2 . GLU A 76  ? 0.4957 0.8348 0.3576 -0.0385 -0.0711 0.1022  91  GLU A OE2 
301  N N   . VAL A 77  ? 0.4034 0.7710 0.3213 -0.0379 -0.0676 0.0594  92  VAL A N   
302  C CA  . VAL A 77  ? 0.4029 0.7609 0.3259 -0.0347 -0.0731 0.0523  92  VAL A CA  
303  C C   . VAL A 77  ? 0.4066 0.7636 0.3404 -0.0391 -0.0725 0.0497  92  VAL A C   
304  O O   . VAL A 77  ? 0.4493 0.7943 0.3847 -0.0386 -0.0770 0.0477  92  VAL A O   
305  C CB  . VAL A 77  ? 0.3884 0.7530 0.3133 -0.0274 -0.0743 0.0431  92  VAL A CB  
306  C CG1 . VAL A 77  ? 0.3804 0.7381 0.3123 -0.0243 -0.0784 0.0374  92  VAL A CG1 
307  C CG2 . VAL A 77  ? 0.3964 0.7621 0.3100 -0.0223 -0.0766 0.0441  92  VAL A CG2 
308  N N   . LEU A 78  ? 0.3799 0.7492 0.3203 -0.0424 -0.0675 0.0494  93  LEU A N   
309  C CA  . LEU A 78  ? 0.3734 0.7429 0.3233 -0.0452 -0.0678 0.0459  93  LEU A CA  
310  C C   . LEU A 78  ? 0.4030 0.7676 0.3561 -0.0538 -0.0692 0.0527  93  LEU A C   
311  O O   . LEU A 78  ? 0.4038 0.7563 0.3582 -0.0556 -0.0741 0.0508  93  LEU A O   
312  C CB  . LEU A 78  ? 0.3539 0.7384 0.3105 -0.0434 -0.0629 0.0413  93  LEU A CB  
313  C CG  . LEU A 78  ? 0.3445 0.7326 0.3008 -0.0362 -0.0627 0.0336  93  LEU A CG  
314  C CD1 . LEU A 78  ? 0.3375 0.7376 0.3004 -0.0352 -0.0584 0.0299  93  LEU A CD1 
315  C CD2 . LEU A 78  ? 0.3387 0.7181 0.2975 -0.0330 -0.0666 0.0284  93  LEU A CD2 
316  N N   . LEU A 79  ? 0.4288 0.8035 0.3834 -0.0590 -0.0649 0.0605  94  LEU A N   
317  C CA  . LEU A 79  ? 0.4315 0.8033 0.3910 -0.0687 -0.0663 0.0690  94  LEU A CA  
318  C C   . LEU A 79  ? 0.4591 0.8157 0.4102 -0.0719 -0.0699 0.0770  94  LEU A C   
319  O O   . LEU A 79  ? 0.4804 0.8194 0.4308 -0.0747 -0.0769 0.0769  94  LEU A O   
320  C CB  . LEU A 79  ? 0.4403 0.8323 0.4074 -0.0730 -0.0591 0.0754  94  LEU A CB  
321  C CG  . LEU A 79  ? 0.4353 0.8412 0.4153 -0.0741 -0.0571 0.0714  94  LEU A CG  
322  C CD1 . LEU A 79  ? 0.4249 0.8192 0.4098 -0.0765 -0.0645 0.0659  94  LEU A CD1 
323  C CD2 . LEU A 79  ? 0.4404 0.8574 0.4180 -0.0647 -0.0521 0.0638  94  LEU A CD2 
324  N N   . GLN A 80  ? 0.4858 0.8481 0.4294 -0.0708 -0.0655 0.0840  95  GLN A N   
325  C CA  . GLN A 80  ? 0.5198 0.8704 0.4569 -0.0762 -0.0676 0.0955  95  GLN A CA  
326  C C   . GLN A 80  ? 0.5363 0.8623 0.4655 -0.0736 -0.0764 0.0935  95  GLN A C   
327  O O   . GLN A 80  ? 0.5424 0.8531 0.4714 -0.0806 -0.0812 0.1007  95  GLN A O   
328  C CB  . GLN A 80  ? 0.5431 0.9042 0.4697 -0.0730 -0.0610 0.1026  95  GLN A CB  
329  C CG  . GLN A 80  ? 0.5840 0.9372 0.5046 -0.0797 -0.0608 0.1174  95  GLN A CG  
330  C CD  . GLN A 80  ? 0.6040 0.9636 0.5087 -0.0734 -0.0556 0.1229  95  GLN A CD  
331  O OE1 . GLN A 80  ? 0.5850 0.9638 0.4878 -0.0690 -0.0479 0.1212  95  GLN A OE1 
332  N NE2 . GLN A 80  ? 0.6388 0.9812 0.5308 -0.0720 -0.0605 0.1291  95  GLN A NE2 
333  N N   . ARG A 81  ? 0.5660 0.8885 0.4894 -0.0635 -0.0787 0.0842  96  ARG A N   
334  C CA  . ARG A 81  ? 0.6042 0.9057 0.5218 -0.0588 -0.0866 0.0807  96  ARG A CA  
335  C C   . ARG A 81  ? 0.5837 0.8874 0.5070 -0.0526 -0.0878 0.0681  96  ARG A C   
336  O O   . ARG A 81  ? 0.5719 0.8711 0.4916 -0.0438 -0.0904 0.0621  96  ARG A O   
337  C CB  . ARG A 81  ? 0.6443 0.9399 0.5497 -0.0516 -0.0886 0.0834  96  ARG A CB  
338  C CG  . ARG A 81  ? 0.6974 1.0061 0.5953 -0.0513 -0.0830 0.0904  96  ARG A CG  
339  C CD  . ARG A 81  ? 0.7624 1.0587 0.6462 -0.0470 -0.0871 0.0972  96  ARG A CD  
340  N NE  . ARG A 81  ? 0.8348 1.1234 0.7139 -0.0556 -0.0861 0.1118  96  ARG A NE  
341  C CZ  . ARG A 81  ? 0.9224 1.2141 0.7895 -0.0552 -0.0829 0.1221  96  ARG A CZ  
342  N NH1 . ARG A 81  ? 0.9894 1.2906 0.8460 -0.0460 -0.0817 0.1185  96  ARG A NH1 
343  N NH2 . ARG A 81  ? 1.0010 1.2856 0.8659 -0.0641 -0.0815 0.1364  96  ARG A NH2 
344  N N   . GLY A 82  ? 0.5483 0.8600 0.4810 -0.0572 -0.0856 0.0651  97  GLY A N   
345  C CA  . GLY A 82  ? 0.5357 0.8500 0.4735 -0.0525 -0.0859 0.0549  97  GLY A CA  
346  C C   . GLY A 82  ? 0.5593 0.8554 0.4924 -0.0470 -0.0921 0.0497  97  GLY A C   
347  O O   . GLY A 82  ? 0.5747 0.8737 0.5087 -0.0391 -0.0914 0.0421  97  GLY A O   
348  N N   . ARG A 83  ? 0.5841 0.8613 0.5125 -0.0508 -0.0982 0.0539  98  ARG A N   
349  C CA  . ARG A 83  ? 0.6222 0.8798 0.5447 -0.0448 -0.1045 0.0485  98  ARG A CA  
350  C C   . ARG A 83  ? 0.6195 0.8727 0.5361 -0.0344 -0.1056 0.0470  98  ARG A C   
351  O O   . ARG A 83  ? 0.6181 0.8680 0.5338 -0.0252 -0.1066 0.0396  98  ARG A O   
352  C CB  . ARG A 83  ? 0.6885 0.9248 0.6073 -0.0522 -0.1119 0.0534  98  ARG A CB  
353  C CG  . ARG A 83  ? 0.7372 0.9771 0.6637 -0.0628 -0.1129 0.0544  98  ARG A CG  
354  C CD  . ARG A 83  ? 0.8244 1.0397 0.7476 -0.0697 -0.1226 0.0572  98  ARG A CD  
355  N NE  . ARG A 83  ? 0.9205 1.1328 0.8464 -0.0805 -0.1234 0.0700  98  ARG A NE  
356  C CZ  . ARG A 83  ? 1.0553 1.2545 0.9735 -0.0793 -0.1253 0.0772  98  ARG A CZ  
357  N NH1 . ARG A 83  ? 1.1682 1.3562 1.0763 -0.0672 -0.1273 0.0722  98  ARG A NH1 
358  N NH2 . ARG A 83  ? 1.0502 1.2488 0.9716 -0.0903 -0.1250 0.0903  98  ARG A NH2 
359  N N   . GLU A 84  ? 0.6147 0.8696 0.5274 -0.0355 -0.1051 0.0544  99  GLU A N   
360  C CA  . GLU A 84  ? 0.5997 0.8520 0.5073 -0.0259 -0.1072 0.0538  99  GLU A CA  
361  C C   . GLU A 84  ? 0.5533 0.8233 0.4673 -0.0180 -0.1033 0.0459  99  GLU A C   
362  O O   . GLU A 84  ? 0.5581 0.8258 0.4721 -0.0085 -0.1058 0.0418  99  GLU A O   
363  C CB  . GLU A 84  ? 0.6221 0.8750 0.5230 -0.0290 -0.1070 0.0639  99  GLU A CB  
364  C CG  . GLU A 84  ? 0.6587 0.8906 0.5527 -0.0353 -0.1120 0.0733  99  GLU A CG  
365  C CD  . GLU A 84  ? 0.6909 0.9274 0.5894 -0.0485 -0.1087 0.0805  99  GLU A CD  
366  O OE1 . GLU A 84  ? 0.6613 0.9025 0.5682 -0.0532 -0.1075 0.0758  99  GLU A OE1 
367  O OE2 . GLU A 84  ? 0.7556 0.9923 0.6496 -0.0539 -0.1072 0.0917  99  GLU A OE2 
368  N N   . PHE A 85  ? 0.4964 0.7842 0.4170 -0.0220 -0.0975 0.0442  100 PHE A N   
369  C CA  . PHE A 85  ? 0.4556 0.7599 0.3829 -0.0167 -0.0943 0.0383  100 PHE A CA  
370  C C   . PHE A 85  ? 0.4155 0.7252 0.3507 -0.0159 -0.0912 0.0315  100 PHE A C   
371  O O   . PHE A 85  ? 0.3698 0.6940 0.3123 -0.0148 -0.0874 0.0276  100 PHE A O   
372  C CB  . PHE A 85  ? 0.4621 0.7809 0.3893 -0.0205 -0.0903 0.0409  100 PHE A CB  
373  C CG  . PHE A 85  ? 0.4890 0.8060 0.4068 -0.0188 -0.0927 0.0466  100 PHE A CG  
374  C CD1 . PHE A 85  ? 0.4919 0.8100 0.4085 -0.0109 -0.0967 0.0440  100 PHE A CD1 
375  C CD2 . PHE A 85  ? 0.5156 0.8315 0.4262 -0.0250 -0.0908 0.0552  100 PHE A CD2 
376  C CE1 . PHE A 85  ? 0.5167 0.8331 0.4230 -0.0087 -0.0998 0.0491  100 PHE A CE1 
377  C CE2 . PHE A 85  ? 0.5276 0.8421 0.4273 -0.0228 -0.0925 0.0611  100 PHE A CE2 
378  C CZ  . PHE A 85  ? 0.5333 0.8472 0.4297 -0.0143 -0.0975 0.0577  100 PHE A CZ  
379  N N   . ALA A 86  ? 0.4196 0.7163 0.3524 -0.0162 -0.0934 0.0300  101 ALA A N   
380  C CA  . ALA A 86  ? 0.4075 0.7075 0.3448 -0.0154 -0.0908 0.0243  101 ALA A CA  
381  C C   . ALA A 86  ? 0.3944 0.6937 0.3332 -0.0053 -0.0904 0.0185  101 ALA A C   
382  O O   . ALA A 86  ? 0.3880 0.6843 0.3259 -0.0028 -0.0892 0.0142  101 ALA A O   
383  C CB  . ALA A 86  ? 0.4212 0.7081 0.3540 -0.0216 -0.0941 0.0253  101 ALA A CB  
384  N N   . GLY A 87  ? 0.3759 0.6795 0.3171 0.0010  -0.0912 0.0186  102 GLY A N   
385  C CA  . GLY A 87  ? 0.3645 0.6707 0.3098 0.0111  -0.0903 0.0143  102 GLY A CA  
386  C C   . GLY A 87  ? 0.3308 0.6569 0.2884 0.0115  -0.0849 0.0122  102 GLY A C   
387  O O   . GLY A 87  ? 0.3175 0.6529 0.2788 0.0054  -0.0837 0.0137  102 GLY A O   
388  N N   . ARG A 88  ? 0.3242 0.6567 0.2881 0.0188  -0.0816 0.0089  103 ARG A N   
389  C CA  . ARG A 88  ? 0.3045 0.6561 0.2827 0.0192  -0.0767 0.0079  103 ARG A CA  
390  C C   . ARG A 88  ? 0.3150 0.6757 0.3033 0.0279  -0.0768 0.0073  103 ARG A C   
391  O O   . ARG A 88  ? 0.3271 0.6799 0.3108 0.0360  -0.0788 0.0066  103 ARG A O   
392  C CB  . ARG A 88  ? 0.2857 0.6411 0.2651 0.0181  -0.0707 0.0062  103 ARG A CB  
393  C CG  . ARG A 88  ? 0.2731 0.6235 0.2462 0.0097  -0.0706 0.0068  103 ARG A CG  
394  C CD  . ARG A 88  ? 0.2553 0.6148 0.2344 0.0027  -0.0708 0.0085  103 ARG A CD  
395  N NE  . ARG A 88  ? 0.2417 0.6026 0.2198 -0.0032 -0.0683 0.0086  103 ARG A NE  
396  C CZ  . ARG A 88  ? 0.2291 0.5951 0.2091 -0.0090 -0.0682 0.0096  103 ARG A CZ  
397  N NH1 . ARG A 88  ? 0.2278 0.5974 0.2090 -0.0102 -0.0704 0.0105  103 ARG A NH1 
398  N NH2 . ARG A 88  ? 0.2242 0.5921 0.2042 -0.0127 -0.0658 0.0096  103 ARG A NH2 
399  N N   . PRO A 89  ? 0.3286 0.7061 0.3316 0.0263  -0.0751 0.0076  104 PRO A N   
400  C CA  . PRO A 89  ? 0.3556 0.7449 0.3717 0.0332  -0.0763 0.0078  104 PRO A CA  
401  C C   . PRO A 89  ? 0.3774 0.7776 0.4035 0.0389  -0.0688 0.0075  104 PRO A C   
402  O O   . PRO A 89  ? 0.3751 0.7793 0.4030 0.0349  -0.0629 0.0077  104 PRO A O   
403  C CB  . PRO A 89  ? 0.3444 0.7456 0.3716 0.0268  -0.0793 0.0082  104 PRO A CB  
404  C CG  . PRO A 89  ? 0.3276 0.7292 0.3536 0.0189  -0.0748 0.0078  104 PRO A CG  
405  C CD  . PRO A 89  ? 0.3244 0.7103 0.3333 0.0178  -0.0735 0.0078  104 PRO A CD  
406  N N   . LYS A 90  ? 0.4235 0.8290 0.4557 0.0490  -0.0685 0.0074  105 LYS A N   
407  C CA  . LYS A 90  ? 0.4521 0.8685 0.4920 0.0562  -0.0600 0.0077  105 LYS A CA  
408  C C   . LYS A 90  ? 0.4740 0.9151 0.5395 0.0557  -0.0577 0.0106  105 LYS A C   
409  O O   . LYS A 90  ? 0.4743 0.9256 0.5515 0.0627  -0.0600 0.0114  105 LYS A O   
410  C CB  . LYS A 90  ? 0.4723 0.8789 0.5021 0.0690  -0.0599 0.0055  105 LYS A CB  
411  C CG  . LYS A 90  ? 0.4956 0.9140 0.5309 0.0783  -0.0500 0.0056  105 LYS A CG  
412  C CD  . LYS A 90  ? 0.5198 0.9346 0.5510 0.0938  -0.0501 0.0034  105 LYS A CD  
413  C CE  . LYS A 90  ? 0.5350 0.9338 0.5454 0.1018  -0.0458 -0.0008 105 LYS A CE  
414  N NZ  . LYS A 90  ? 0.5437 0.9589 0.5602 0.1027  -0.0342 0.0013  105 LYS A NZ  
415  N N   . MET A 91  ? 0.5181 0.9684 0.5930 0.0469  -0.0538 0.0126  106 MET A N   
416  C CA  . MET A 91  ? 0.5603 1.0326 0.6607 0.0438  -0.0523 0.0159  106 MET A CA  
417  C C   . MET A 91  ? 0.5809 1.0663 0.6896 0.0500  -0.0409 0.0193  106 MET A C   
418  O O   . MET A 91  ? 0.6066 1.0818 0.6982 0.0557  -0.0351 0.0181  106 MET A O   
419  C CB  . MET A 91  ? 0.6007 1.0736 0.7061 0.0312  -0.0546 0.0163  106 MET A CB  
420  C CG  . MET A 91  ? 0.6477 1.1063 0.7401 0.0256  -0.0640 0.0128  106 MET A CG  
421  S SD  . MET A 91  ? 0.7093 1.1633 0.7996 0.0137  -0.0638 0.0122  106 MET A SD  
422  C CE  . MET A 91  ? 0.7207 1.1591 0.7922 0.0106  -0.0727 0.0084  106 MET A CE  
423  N N   . VAL A 92  ? 0.5504 1.0586 0.6850 0.0488  -0.0377 0.0239  107 VAL A N   
424  C CA  . VAL A 92  ? 0.5071 1.0309 0.6512 0.0544  -0.0253 0.0288  107 VAL A CA  
425  C C   . VAL A 92  ? 0.4575 0.9815 0.6010 0.0463  -0.0181 0.0327  107 VAL A C   
426  O O   . VAL A 92  ? 0.4619 0.9879 0.5980 0.0522  -0.0078 0.0352  107 VAL A O   
427  C CB  . VAL A 92  ? 0.5238 1.0749 0.6985 0.0575  -0.0238 0.0336  107 VAL A CB  
428  C CG1 . VAL A 92  ? 0.5138 1.0855 0.7050 0.0580  -0.0104 0.0415  107 VAL A CG1 
429  C CG2 . VAL A 92  ? 0.5730 1.1251 0.7443 0.0719  -0.0255 0.0308  107 VAL A CG2 
430  N N   . THR A 93  ? 0.4164 0.9383 0.5671 0.0337  -0.0233 0.0333  108 THR A N   
431  C CA  . THR A 93  ? 0.4283 0.9460 0.5749 0.0266  -0.0179 0.0365  108 THR A CA  
432  C C   . THR A 93  ? 0.4312 0.9288 0.5477 0.0311  -0.0157 0.0325  108 THR A C   
433  O O   . THR A 93  ? 0.4167 0.9147 0.5251 0.0351  -0.0066 0.0354  108 THR A O   
434  C CB  . THR A 93  ? 0.4473 0.9592 0.6000 0.0140  -0.0262 0.0352  108 THR A CB  
435  O OG1 . THR A 93  ? 0.5128 1.0092 0.6499 0.0137  -0.0361 0.0281  108 THR A OG1 
436  C CG2 . THR A 93  ? 0.4515 0.9812 0.6337 0.0080  -0.0297 0.0388  108 THR A CG2 
437  N N   . THR A 94  ? 0.4100 0.8905 0.5104 0.0305  -0.0244 0.0262  109 THR A N   
438  C CA  . THR A 94  ? 0.4031 0.8645 0.4777 0.0328  -0.0246 0.0223  109 THR A CA  
439  C C   . THR A 94  ? 0.4006 0.8605 0.4633 0.0447  -0.0177 0.0218  109 THR A C   
440  O O   . THR A 94  ? 0.4157 0.8675 0.4630 0.0465  -0.0132 0.0216  109 THR A O   
441  C CB  . THR A 94  ? 0.4136 0.8590 0.4753 0.0310  -0.0347 0.0169  109 THR A CB  
442  O OG1 . THR A 94  ? 0.4223 0.8693 0.4865 0.0382  -0.0386 0.0152  109 THR A OG1 
443  C CG2 . THR A 94  ? 0.4115 0.8566 0.4799 0.0206  -0.0408 0.0165  109 THR A CG2 
444  N N   . ASP A 95  ? 0.4008 0.8677 0.4694 0.0538  -0.0174 0.0211  110 ASP A N   
445  C CA  . ASP A 95  ? 0.4238 0.8904 0.4814 0.0674  -0.0102 0.0201  110 ASP A CA  
446  C C   . ASP A 95  ? 0.4307 0.9089 0.4901 0.0693  0.0020  0.0256  110 ASP A C   
447  O O   . ASP A 95  ? 0.4463 0.9144 0.4848 0.0764  0.0065  0.0235  110 ASP A O   
448  C CB  . ASP A 95  ? 0.4306 0.9091 0.5008 0.0774  -0.0102 0.0200  110 ASP A CB  
449  C CG  . ASP A 95  ? 0.4370 0.8971 0.4929 0.0826  -0.0197 0.0138  110 ASP A CG  
450  O OD1 . ASP A 95  ? 0.4585 0.8964 0.4937 0.0788  -0.0252 0.0097  110 ASP A OD1 
451  O OD2 . ASP A 95  ? 0.4381 0.9060 0.5037 0.0907  -0.0216 0.0135  110 ASP A OD2 
452  N N   . LEU A 96  ? 0.4090 0.9074 0.4927 0.0629  0.0067  0.0329  111 LEU A N   
453  C CA  . LEU A 96  ? 0.4165 0.9261 0.5031 0.0632  0.0184  0.0400  111 LEU A CA  
454  C C   . LEU A 96  ? 0.4010 0.8932 0.4671 0.0579  0.0175  0.0388  111 LEU A C   
455  O O   . LEU A 96  ? 0.4122 0.9012 0.4621 0.0643  0.0250  0.0402  111 LEU A O   
456  C CB  . LEU A 96  ? 0.4158 0.9469 0.5337 0.0536  0.0212  0.0486  111 LEU A CB  
457  C CG  . LEU A 96  ? 0.4352 0.9896 0.5797 0.0578  0.0230  0.0519  111 LEU A CG  
458  C CD1 . LEU A 96  ? 0.4250 0.9975 0.6006 0.0452  0.0235  0.0602  111 LEU A CD1 
459  C CD2 . LEU A 96  ? 0.4509 1.0183 0.5922 0.0733  0.0355  0.0546  111 LEU A CD2 
460  N N   . LEU A 97  ? 0.3843 0.8662 0.4514 0.0467  0.0083  0.0364  112 LEU A N   
461  C CA  . LEU A 97  ? 0.3902 0.8574 0.4419 0.0407  0.0060  0.0354  112 LEU A CA  
462  C C   . LEU A 97  ? 0.3826 0.8316 0.4055 0.0479  0.0044  0.0293  112 LEU A C   
463  O O   . LEU A 97  ? 0.3671 0.8100 0.3764 0.0480  0.0074  0.0307  112 LEU A O   
464  C CB  . LEU A 97  ? 0.3904 0.8501 0.4477 0.0295  -0.0042 0.0325  112 LEU A CB  
465  C CG  . LEU A 97  ? 0.4019 0.8668 0.4734 0.0191  -0.0037 0.0376  112 LEU A CG  
466  C CD1 . LEU A 97  ? 0.4084 0.8920 0.4999 0.0188  0.0053  0.0464  112 LEU A CD1 
467  C CD2 . LEU A 97  ? 0.4088 0.8710 0.4901 0.0112  -0.0137 0.0338  112 LEU A CD2 
468  N N   . THR A 98  ? 0.3653 0.8053 0.3796 0.0537  -0.0012 0.0229  113 THR A N   
469  C CA  . THR A 98  ? 0.3574 0.7766 0.3467 0.0573  -0.0067 0.0162  113 THR A CA  
470  C C   . THR A 98  ? 0.3720 0.7884 0.3484 0.0720  -0.0025 0.0129  113 THR A C   
471  O O   . THR A 98  ? 0.3884 0.7866 0.3463 0.0769  -0.0088 0.0061  113 THR A O   
472  C CB  . THR A 98  ? 0.3400 0.7467 0.3283 0.0507  -0.0182 0.0115  113 THR A CB  
473  O OG1 . THR A 98  ? 0.3229 0.7340 0.3204 0.0554  -0.0204 0.0104  113 THR A OG1 
474  C CG2 . THR A 98  ? 0.3179 0.7286 0.3184 0.0382  -0.0214 0.0143  113 THR A CG2 
475  N N   . GLN A 99  ? 0.3789 0.8138 0.3658 0.0793  0.0080  0.0179  114 GLN A N   
476  C CA  . GLN A 99  ? 0.3968 0.8319 0.3732 0.0951  0.0132  0.0148  114 GLN A CA  
477  C C   . GLN A 99  ? 0.3962 0.8166 0.3666 0.0992  0.0034  0.0074  114 GLN A C   
478  O O   . GLN A 99  ? 0.4088 0.8098 0.3562 0.1073  -0.0006 0.0003  114 GLN A O   
479  C CB  . GLN A 99  ? 0.4279 0.8507 0.3773 0.1022  0.0164  0.0120  114 GLN A CB  
480  C CG  . GLN A 99  ? 0.4578 0.8898 0.3987 0.1188  0.0279  0.0127  114 GLN A CG  
481  C CD  . GLN A 99  ? 0.4853 0.9088 0.4012 0.1232  0.0321  0.0123  114 GLN A CD  
482  O OE1 . GLN A 99  ? 0.4614 0.8911 0.3812 0.1145  0.0354  0.0190  114 GLN A OE1 
483  N NE2 . GLN A 99  ? 0.5225 0.9303 0.4113 0.1372  0.0308  0.0040  114 GLN A NE2 
484  N N   . GLY A 100 ? 0.3826 0.8109 0.3730 0.0933  -0.0014 0.0091  115 GLY A N   
485  C CA  . GLY A 100 ? 0.3915 0.8076 0.3784 0.0972  -0.0104 0.0038  115 GLY A CA  
486  C C   . GLY A 100 ? 0.3960 0.7873 0.3670 0.0891  -0.0219 -0.0010 115 GLY A C   
487  O O   . GLY A 100 ? 0.4271 0.7994 0.3823 0.0955  -0.0281 -0.0066 115 GLY A O   
488  N N   . GLY A 101 ? 0.3732 0.7645 0.3488 0.0754  -0.0250 0.0015  116 GLY A N   
489  C CA  . GLY A 101 ? 0.3770 0.7489 0.3414 0.0672  -0.0351 -0.0017 116 GLY A CA  
490  C C   . GLY A 101 ? 0.4022 0.7540 0.3432 0.0687  -0.0383 -0.0064 116 GLY A C   
491  O O   . GLY A 101 ? 0.4063 0.7394 0.3366 0.0651  -0.0474 -0.0097 116 GLY A O   
492  N N   . LYS A 102 ? 0.4094 0.7649 0.3426 0.0734  -0.0314 -0.0063 117 LYS A N   
493  C CA  . LYS A 102 ? 0.4194 0.7568 0.3300 0.0747  -0.0353 -0.0111 117 LYS A CA  
494  C C   . LYS A 102 ? 0.3840 0.7212 0.2951 0.0623  -0.0379 -0.0087 117 LYS A C   
495  O O   . LYS A 102 ? 0.3930 0.7178 0.2876 0.0623  -0.0416 -0.0120 117 LYS A O   
496  C CB  . LYS A 102 ? 0.4536 0.7936 0.3513 0.0882  -0.0270 -0.0127 117 LYS A CB  
497  C CG  . LYS A 102 ? 0.4883 0.8259 0.3819 0.1028  -0.0250 -0.0165 117 LYS A CG  
498  C CD  . LYS A 102 ? 0.5343 0.8708 0.4093 0.1174  -0.0175 -0.0196 117 LYS A CD  
499  C CE  . LYS A 102 ? 0.5704 0.8993 0.4360 0.1340  -0.0170 -0.0256 117 LYS A CE  
500  N NZ  . LYS A 102 ? 0.5724 0.9243 0.4619 0.1384  -0.0094 -0.0202 117 LYS A NZ  
501  N N   . ASP A 103 ? 0.3423 0.6925 0.2717 0.0523  -0.0368 -0.0035 118 ASP A N   
502  C CA  . ASP A 103 ? 0.3203 0.6702 0.2505 0.0419  -0.0393 -0.0016 118 ASP A CA  
503  C C   . ASP A 103 ? 0.3215 0.6586 0.2487 0.0338  -0.0494 -0.0040 118 ASP A C   
504  O O   . ASP A 103 ? 0.3302 0.6532 0.2484 0.0368  -0.0552 -0.0078 118 ASP A O   
505  C CB  . ASP A 103 ? 0.2955 0.6637 0.2455 0.0358  -0.0336 0.0045  118 ASP A CB  
506  C CG  . ASP A 103 ? 0.2787 0.6518 0.2433 0.0306  -0.0369 0.0054  118 ASP A CG  
507  O OD1 . ASP A 103 ? 0.2878 0.6540 0.2492 0.0344  -0.0408 0.0026  118 ASP A OD1 
508  O OD2 . ASP A 103 ? 0.2556 0.6379 0.2335 0.0232  -0.0363 0.0086  118 ASP A OD2 
509  N N   . ILE A 104 ? 0.3198 0.6615 0.2547 0.0238  -0.0513 -0.0013 119 ILE A N   
510  C CA  . ILE A 104 ? 0.3279 0.6627 0.2644 0.0153  -0.0588 -0.0015 119 ILE A CA  
511  C C   . ILE A 104 ? 0.3154 0.6596 0.2663 0.0108  -0.0582 0.0014  119 ILE A C   
512  O O   . ILE A 104 ? 0.3237 0.6612 0.2737 0.0089  -0.0631 0.0012  119 ILE A O   
513  C CB  . ILE A 104 ? 0.3271 0.6619 0.2624 0.0078  -0.0616 -0.0006 119 ILE A CB  
514  C CG1 . ILE A 104 ? 0.3435 0.6667 0.2629 0.0113  -0.0652 -0.0042 119 ILE A CG1 
515  C CG2 . ILE A 104 ? 0.3224 0.6553 0.2629 -0.0013 -0.0671 0.0009  119 ILE A CG2 
516  C CD1 . ILE A 104 ? 0.3627 0.6675 0.2702 0.0128  -0.0731 -0.0085 119 ILE A CD1 
517  N N   . ALA A 105 ? 0.3032 0.6617 0.2664 0.0092  -0.0530 0.0042  120 ALA A N   
518  C CA  . ALA A 105 ? 0.2994 0.6659 0.2747 0.0042  -0.0538 0.0060  120 ALA A CA  
519  C C   . ALA A 105 ? 0.3020 0.6698 0.2817 0.0084  -0.0551 0.0057  120 ALA A C   
520  O O   . ALA A 105 ? 0.2920 0.6575 0.2724 0.0053  -0.0595 0.0060  120 ALA A O   
521  C CB  . ALA A 105 ? 0.2842 0.6630 0.2711 0.0014  -0.0492 0.0083  120 ALA A CB  
522  N N   . PHE A 106 ? 0.3094 0.6814 0.2915 0.0162  -0.0510 0.0055  121 PHE A N   
523  C CA  . PHE A 106 ? 0.3239 0.6997 0.3124 0.0214  -0.0520 0.0054  121 PHE A CA  
524  C C   . PHE A 106 ? 0.3561 0.7191 0.3327 0.0296  -0.0546 0.0027  121 PHE A C   
525  O O   . PHE A 106 ? 0.3748 0.7426 0.3569 0.0371  -0.0538 0.0025  121 PHE A O   
526  C CB  . PHE A 106 ? 0.3170 0.7099 0.3211 0.0244  -0.0456 0.0078  121 PHE A CB  
527  C CG  . PHE A 106 ? 0.3039 0.7069 0.3211 0.0162  -0.0452 0.0101  121 PHE A CG  
528  C CD1 . PHE A 106 ? 0.2973 0.7032 0.3219 0.0122  -0.0505 0.0098  121 PHE A CD1 
529  C CD2 . PHE A 106 ? 0.3128 0.7202 0.3327 0.0132  -0.0402 0.0123  121 PHE A CD2 
530  C CE1 . PHE A 106 ? 0.2979 0.7105 0.3325 0.0054  -0.0512 0.0105  121 PHE A CE1 
531  C CE2 . PHE A 106 ? 0.3048 0.7184 0.3356 0.0061  -0.0407 0.0139  121 PHE A CE2 
532  C CZ  . PHE A 106 ? 0.3071 0.7231 0.3453 0.0024  -0.0463 0.0125  121 PHE A CZ  
533  N N   . ALA A 107 ? 0.3710 0.7177 0.3323 0.0283  -0.0585 0.0004  122 ALA A N   
534  C CA  . ALA A 107 ? 0.3944 0.7246 0.3430 0.0352  -0.0630 -0.0028 122 ALA A CA  
535  C C   . ALA A 107 ? 0.4167 0.7340 0.3609 0.0293  -0.0711 -0.0017 122 ALA A C   
536  O O   . ALA A 107 ? 0.3926 0.7114 0.3390 0.0195  -0.0730 0.0008  122 ALA A O   
537  C CB  . ALA A 107 ? 0.4107 0.7292 0.3443 0.0385  -0.0630 -0.0065 122 ALA A CB  
538  N N   . ASP A 108 ? 0.4555 0.7601 0.3931 0.0359  -0.0756 -0.0031 123 ASP A N   
539  C CA  . ASP A 108 ? 0.4820 0.7724 0.4143 0.0313  -0.0832 -0.0009 123 ASP A CA  
540  C C   . ASP A 108 ? 0.5192 0.7913 0.4394 0.0250  -0.0886 -0.0018 123 ASP A C   
541  O O   . ASP A 108 ? 0.5880 0.8518 0.4992 0.0291  -0.0887 -0.0064 123 ASP A O   
542  C CB  . ASP A 108 ? 0.5108 0.7914 0.4394 0.0418  -0.0868 -0.0020 123 ASP A CB  
543  C CG  . ASP A 108 ? 0.4986 0.7914 0.4385 0.0429  -0.0873 0.0018  123 ASP A CG  
544  O OD1 . ASP A 108 ? 0.4915 0.7980 0.4403 0.0351  -0.0858 0.0049  123 ASP A OD1 
545  O OD2 . ASP A 108 ? 0.5101 0.7981 0.4493 0.0523  -0.0901 0.0013  123 ASP A OD2 
546  N N   . TYR A 109 ? 0.5406 0.8068 0.4604 0.0153  -0.0933 0.0027  124 TYR A N   
547  C CA  . TYR A 109 ? 0.5549 0.8036 0.4661 0.0077  -0.0999 0.0033  124 TYR A CA  
548  C C   . TYR A 109 ? 0.5841 0.8084 0.4825 0.0146  -0.1067 -0.0004 124 TYR A C   
549  O O   . TYR A 109 ? 0.6114 0.8287 0.5082 0.0207  -0.1089 0.0008  124 TYR A O   
550  C CB  . TYR A 109 ? 0.5655 0.8148 0.4805 -0.0028 -0.1023 0.0107  124 TYR A CB  
551  C CG  . TYR A 109 ? 0.5917 0.8270 0.5024 -0.0131 -0.1086 0.0136  124 TYR A CG  
552  C CD1 . TYR A 109 ? 0.6316 0.8436 0.5339 -0.0140 -0.1166 0.0154  124 TYR A CD1 
553  C CD2 . TYR A 109 ? 0.5827 0.8285 0.4993 -0.0224 -0.1069 0.0152  124 TYR A CD2 
554  C CE1 . TYR A 109 ? 0.6493 0.8489 0.5502 -0.0250 -0.1229 0.0189  124 TYR A CE1 
555  C CE2 . TYR A 109 ? 0.6022 0.8381 0.5183 -0.0327 -0.1129 0.0187  124 TYR A CE2 
556  C CZ  . TYR A 109 ? 0.6386 0.8516 0.5474 -0.0346 -0.1209 0.0207  124 TYR A CZ  
557  O OH  . TYR A 109 ? 0.6809 0.8847 0.5916 -0.0463 -0.1273 0.0249  124 TYR A OH  
558  N N   . SER A 110 ? 0.5832 0.7933 0.4720 0.0139  -0.1111 -0.0050 125 SER A N   
559  C CA  . SER A 110 ? 0.6085 0.7941 0.4830 0.0229  -0.1176 -0.0110 125 SER A CA  
560  C C   . SER A 110 ? 0.6413 0.8127 0.5056 0.0195  -0.1236 -0.0161 125 SER A C   
561  O O   . SER A 110 ? 0.6533 0.8383 0.5215 0.0143  -0.1203 -0.0164 125 SER A O   
562  C CB  . SER A 110 ? 0.6101 0.8027 0.4821 0.0391  -0.1111 -0.0165 125 SER A CB  
563  O OG  . SER A 110 ? 0.5757 0.7853 0.4500 0.0408  -0.1036 -0.0190 125 SER A OG  
564  N N   . PRO A 111 ? 0.6541 0.7971 0.5042 0.0234  -0.1331 -0.0210 126 PRO A N   
565  C CA  . PRO A 111 ? 0.6612 0.7877 0.4989 0.0222  -0.1407 -0.0279 126 PRO A CA  
566  C C   . PRO A 111 ? 0.6441 0.7859 0.4782 0.0285  -0.1338 -0.0332 126 PRO A C   
567  O O   . PRO A 111 ? 0.6484 0.7916 0.4816 0.0209  -0.1373 -0.0342 126 PRO A O   
568  C CB  . PRO A 111 ? 0.6925 0.7890 0.5135 0.0334  -0.1487 -0.0348 126 PRO A CB  
569  C CG  . PRO A 111 ? 0.6949 0.7864 0.5224 0.0321  -0.1498 -0.0279 126 PRO A CG  
570  C CD  . PRO A 111 ? 0.6659 0.7893 0.5106 0.0292  -0.1385 -0.0203 126 PRO A CD  
571  N N   . LEU A 112 ? 0.6271 0.7814 0.4604 0.0421  -0.1241 -0.0355 127 LEU A N   
572  C CA  . LEU A 112 ? 0.6106 0.7790 0.4394 0.0493  -0.1165 -0.0393 127 LEU A CA  
573  C C   . LEU A 112 ? 0.5813 0.7745 0.4257 0.0385  -0.1102 -0.0327 127 LEU A C   
574  O O   . LEU A 112 ? 0.5925 0.7917 0.4330 0.0373  -0.1089 -0.0344 127 LEU A O   
575  C CB  . LEU A 112 ? 0.6125 0.7911 0.4403 0.0656  -0.1066 -0.0413 127 LEU A CB  
576  C CG  . LEU A 112 ? 0.6084 0.8061 0.4345 0.0741  -0.0955 -0.0426 127 LEU A CG  
577  C CD1 . LEU A 112 ? 0.6407 0.8251 0.4464 0.0778  -0.0997 -0.0497 127 LEU A CD1 
578  C CD2 . LEU A 112 ? 0.6137 0.8193 0.4401 0.0903  -0.0869 -0.0440 127 LEU A CD2 
579  N N   . TRP A 113 ? 0.5597 0.7665 0.4207 0.0313  -0.1068 -0.0253 128 TRP A N   
580  C CA  . TRP A 113 ? 0.5283 0.7587 0.4043 0.0225  -0.1004 -0.0195 128 TRP A CA  
581  C C   . TRP A 113 ? 0.5484 0.7758 0.4270 0.0088  -0.1071 -0.0171 128 TRP A C   
582  O O   . TRP A 113 ? 0.5409 0.7831 0.4259 0.0040  -0.1036 -0.0152 128 TRP A O   
583  C CB  . TRP A 113 ? 0.4856 0.7310 0.3764 0.0211  -0.0949 -0.0137 128 TRP A CB  
584  C CG  . TRP A 113 ? 0.4294 0.6962 0.3343 0.0132  -0.0891 -0.0087 128 TRP A CG  
585  C CD1 . TRP A 113 ? 0.4078 0.6934 0.3210 0.0167  -0.0805 -0.0077 128 TRP A CD1 
586  C CD2 . TRP A 113 ? 0.4084 0.6796 0.3208 0.0009  -0.0917 -0.0039 128 TRP A CD2 
587  N NE1 . TRP A 113 ? 0.3858 0.6852 0.3103 0.0076  -0.0783 -0.0034 128 TRP A NE1 
588  C CE2 . TRP A 113 ? 0.3867 0.6784 0.3106 -0.0015 -0.0846 -0.0012 128 TRP A CE2 
589  C CE3 . TRP A 113 ? 0.4058 0.6658 0.3170 -0.0084 -0.0990 -0.0010 128 TRP A CE3 
590  C CZ2 . TRP A 113 ? 0.3649 0.6661 0.2974 -0.0113 -0.0844 0.0031  128 TRP A CZ2 
591  C CZ3 . TRP A 113 ? 0.3832 0.6552 0.3046 -0.0186 -0.0979 0.0044  128 TRP A CZ3 
592  C CH2 . TRP A 113 ? 0.3615 0.6537 0.2926 -0.0193 -0.0906 0.0059  128 TRP A CH2 
593  N N   . LYS A 114 ? 0.5950 0.8037 0.4698 0.0025  -0.1168 -0.0167 129 LYS A N   
594  C CA  . LYS A 114 ? 0.6211 0.8279 0.5003 -0.0107 -0.1237 -0.0140 129 LYS A CA  
595  C C   . LYS A 114 ? 0.6340 0.8346 0.5026 -0.0090 -0.1287 -0.0205 129 LYS A C   
596  O O   . LYS A 114 ? 0.6409 0.8543 0.5168 -0.0161 -0.1286 -0.0183 129 LYS A O   
597  C CB  . LYS A 114 ? 0.6546 0.8422 0.5333 -0.0189 -0.1333 -0.0109 129 LYS A CB  
598  C CG  . LYS A 114 ? 0.6647 0.8533 0.5488 -0.0186 -0.1301 -0.0050 129 LYS A CG  
599  C CD  . LYS A 114 ? 0.6984 0.8812 0.5898 -0.0323 -0.1357 0.0032  129 LYS A CD  
600  C CE  . LYS A 114 ? 0.7733 0.9280 0.6560 -0.0371 -0.1488 0.0008  129 LYS A CE  
601  N NZ  . LYS A 114 ? 0.8296 0.9609 0.7036 -0.0324 -0.1539 0.0013  129 LYS A NZ  
602  N N   . ASN A 115 ? 0.6533 0.8348 0.5040 0.0014  -0.1332 -0.0287 130 ASN A N   
603  C CA  . ASN A 115 ? 0.6631 0.8382 0.5004 0.0048  -0.1382 -0.0355 130 ASN A CA  
604  C C   . ASN A 115 ? 0.6253 0.8230 0.4652 0.0098  -0.1274 -0.0343 130 ASN A C   
605  O O   . ASN A 115 ? 0.5919 0.7947 0.4300 0.0067  -0.1299 -0.0351 130 ASN A O   
606  C CB  . ASN A 115 ? 0.7045 0.8547 0.5193 0.0176  -0.1438 -0.0453 130 ASN A CB  
607  C CG  . ASN A 115 ? 0.7518 0.8753 0.5626 0.0130  -0.1559 -0.0469 130 ASN A CG  
608  O OD1 . ASN A 115 ? 0.7801 0.9011 0.6022 -0.0018 -0.1632 -0.0416 130 ASN A OD1 
609  N ND2 . ASN A 115 ? 0.7863 0.8899 0.5814 0.0260  -0.1579 -0.0536 130 ASN A ND2 
610  N N   . HIS A 116 ? 0.6061 0.8172 0.4512 0.0173  -0.1158 -0.0318 131 HIS A N   
611  C CA  . HIS A 116 ? 0.5703 0.8014 0.4183 0.0226  -0.1049 -0.0299 131 HIS A CA  
612  C C   . HIS A 116 ? 0.5391 0.7879 0.4032 0.0111  -0.1032 -0.0235 131 HIS A C   
613  O O   . HIS A 116 ? 0.5296 0.7862 0.3913 0.0117  -0.1015 -0.0234 131 HIS A O   
614  C CB  . HIS A 116 ? 0.5392 0.7812 0.3928 0.0317  -0.0940 -0.0280 131 HIS A CB  
615  C CG  . HIS A 116 ? 0.5049 0.7673 0.3636 0.0361  -0.0827 -0.0248 131 HIS A CG  
616  N ND1 . HIS A 116 ? 0.4847 0.7624 0.3547 0.0408  -0.0727 -0.0211 131 HIS A ND1 
617  C CD2 . HIS A 116 ? 0.4990 0.7686 0.3540 0.0358  -0.0803 -0.0239 131 HIS A CD2 
618  C CE1 . HIS A 116 ? 0.4726 0.7657 0.3465 0.0424  -0.0644 -0.0177 131 HIS A CE1 
619  N NE2 . HIS A 116 ? 0.4843 0.7724 0.3484 0.0398  -0.0687 -0.0192 131 HIS A NE2 
620  N N   . ARG A 117 ? 0.5157 0.7698 0.3947 0.0016  -0.1039 -0.0183 132 ARG A N   
621  C CA  . ARG A 117 ? 0.4988 0.7704 0.3933 -0.0079 -0.1013 -0.0124 132 ARG A CA  
622  C C   . ARG A 117 ? 0.5032 0.7700 0.3972 -0.0162 -0.1107 -0.0129 132 ARG A C   
623  O O   . ARG A 117 ? 0.4882 0.7676 0.3881 -0.0191 -0.1094 -0.0109 132 ARG A O   
624  C CB  . ARG A 117 ? 0.5046 0.7835 0.4129 -0.0139 -0.0985 -0.0069 132 ARG A CB  
625  C CG  . ARG A 117 ? 0.4862 0.7840 0.4095 -0.0215 -0.0944 -0.0014 132 ARG A CG  
626  C CD  . ARG A 117 ? 0.4942 0.7945 0.4267 -0.0293 -0.0953 0.0038  132 ARG A CD  
627  N NE  . ARG A 117 ? 0.4877 0.8070 0.4329 -0.0333 -0.0895 0.0080  132 ARG A NE  
628  C CZ  . ARG A 117 ? 0.4894 0.8179 0.4417 -0.0394 -0.0908 0.0103  132 ARG A CZ  
629  N NH1 . ARG A 117 ? 0.4973 0.8188 0.4468 -0.0435 -0.0983 0.0092  132 ARG A NH1 
630  N NH2 . ARG A 117 ? 0.4877 0.8323 0.4500 -0.0408 -0.0850 0.0132  132 ARG A NH2 
631  N N   . ARG A 118 ? 0.5356 0.7841 0.4236 -0.0202 -0.1210 -0.0153 133 ARG A N   
632  C CA  . ARG A 118 ? 0.5694 0.8129 0.4571 -0.0280 -0.1316 -0.0164 133 ARG A CA  
633  C C   . ARG A 118 ? 0.5718 0.8169 0.4479 -0.0208 -0.1321 -0.0212 133 ARG A C   
634  O O   . ARG A 118 ? 0.5572 0.8134 0.4404 -0.0261 -0.1345 -0.0190 133 ARG A O   
635  C CB  . ARG A 118 ? 0.6142 0.8333 0.4940 -0.0321 -0.1442 -0.0198 133 ARG A CB  
636  C CG  . ARG A 118 ? 0.6612 0.8770 0.5447 -0.0423 -0.1563 -0.0201 133 ARG A CG  
637  C CD  . ARG A 118 ? 0.7292 0.9200 0.6081 -0.0489 -0.1698 -0.0224 133 ARG A CD  
638  N NE  . ARG A 118 ? 0.7675 0.9516 0.6493 -0.0493 -0.1657 -0.0183 133 ARG A NE  
639  C CZ  . ARG A 118 ? 0.8233 0.9856 0.6900 -0.0405 -0.1678 -0.0236 133 ARG A CZ  
640  N NH1 . ARG A 118 ? 0.8432 0.9865 0.6892 -0.0301 -0.1740 -0.0340 133 ARG A NH1 
641  N NH2 . ARG A 118 ? 0.8338 0.9930 0.7052 -0.0412 -0.1639 -0.0184 133 ARG A NH2 
642  N N   . LEU A 119 ? 0.5697 0.8053 0.4282 -0.0081 -0.1291 -0.0270 134 LEU A N   
643  C CA  . LEU A 119 ? 0.5724 0.8096 0.4173 0.0001  -0.1281 -0.0306 134 LEU A CA  
644  C C   . LEU A 119 ? 0.5571 0.8173 0.4140 -0.0006 -0.1183 -0.0243 134 LEU A C   
645  O O   . LEU A 119 ? 0.5611 0.8265 0.4154 -0.0009 -0.1208 -0.0241 134 LEU A O   
646  C CB  . LEU A 119 ? 0.5945 0.8214 0.4199 0.0149  -0.1233 -0.0363 134 LEU A CB  
647  C CG  . LEU A 119 ? 0.6102 0.8403 0.4196 0.0250  -0.1197 -0.0387 134 LEU A CG  
648  C CD1 . LEU A 119 ? 0.6349 0.8535 0.4323 0.0221  -0.1335 -0.0437 134 LEU A CD1 
649  C CD2 . LEU A 119 ? 0.6213 0.8431 0.4126 0.0404  -0.1132 -0.0437 134 LEU A CD2 
650  N N   . VAL A 120 ? 0.5674 0.8405 0.4372 -0.0006 -0.1077 -0.0193 135 VAL A N   
651  C CA  . VAL A 120 ? 0.5554 0.8477 0.4361 -0.0010 -0.0990 -0.0139 135 VAL A CA  
652  C C   . VAL A 120 ? 0.5679 0.8696 0.4622 -0.0114 -0.1040 -0.0103 135 VAL A C   
653  O O   . VAL A 120 ? 0.5707 0.8789 0.4642 -0.0108 -0.1051 -0.0092 135 VAL A O   
654  C CB  . VAL A 120 ? 0.5185 0.8215 0.4108 0.0005  -0.0885 -0.0100 135 VAL A CB  
655  C CG1 . VAL A 120 ? 0.4942 0.8146 0.3987 -0.0012 -0.0812 -0.0046 135 VAL A CG1 
656  C CG2 . VAL A 120 ? 0.5442 0.8417 0.4250 0.0117  -0.0828 -0.0128 135 VAL A CG2 
657  N N   . HIS A 121 ? 0.5779 0.8808 0.4845 -0.0202 -0.1069 -0.0079 136 HIS A N   
658  C CA  . HIS A 121 ? 0.5685 0.8842 0.4912 -0.0297 -0.1093 -0.0033 136 HIS A CA  
659  C C   . HIS A 121 ? 0.5576 0.8730 0.4776 -0.0320 -0.1183 -0.0048 136 HIS A C   
660  O O   . HIS A 121 ? 0.5370 0.8669 0.4668 -0.0337 -0.1169 -0.0015 136 HIS A O   
661  C CB  . HIS A 121 ? 0.5995 0.9122 0.5312 -0.0386 -0.1130 -0.0007 136 HIS A CB  
662  C CG  . HIS A 121 ? 0.5988 0.9242 0.5462 -0.0485 -0.1164 0.0041  136 HIS A CG  
663  N ND1 . HIS A 121 ? 0.5903 0.9343 0.5523 -0.0508 -0.1088 0.0093  136 HIS A ND1 
664  C CD2 . HIS A 121 ? 0.6030 0.9261 0.5547 -0.0563 -0.1268 0.0045  136 HIS A CD2 
665  C CE1 . HIS A 121 ? 0.6141 0.9683 0.5889 -0.0588 -0.1131 0.0131  136 HIS A CE1 
666  N NE2 . HIS A 121 ? 0.6214 0.9639 0.5915 -0.0629 -0.1242 0.0106  136 HIS A NE2 
667  N N   . SER A 122 ? 0.5666 0.8645 0.4729 -0.0314 -0.1284 -0.0103 137 SER A N   
668  C CA  . SER A 122 ? 0.5593 0.8542 0.4611 -0.0335 -0.1397 -0.0129 137 SER A CA  
669  C C   . SER A 122 ? 0.5591 0.8595 0.4508 -0.0243 -0.1357 -0.0136 137 SER A C   
670  O O   . SER A 122 ? 0.5737 0.8850 0.4721 -0.0264 -0.1391 -0.0113 137 SER A O   
671  C CB  . SER A 122 ? 0.5852 0.8565 0.4720 -0.0341 -0.1523 -0.0199 137 SER A CB  
672  O OG  . SER A 122 ? 0.6236 0.8828 0.4871 -0.0231 -0.1549 -0.0267 137 SER A OG  
673  N N   . SER A 123 ? 0.5793 0.8738 0.4562 -0.0138 -0.1279 -0.0159 138 SER A N   
674  C CA  . SER A 123 ? 0.5943 0.8945 0.4616 -0.0052 -0.1225 -0.0147 138 SER A CA  
675  C C   . SER A 123 ? 0.6062 0.9257 0.4917 -0.0090 -0.1175 -0.0078 138 SER A C   
676  O O   . SER A 123 ? 0.6059 0.9298 0.4889 -0.0075 -0.1215 -0.0067 138 SER A O   
677  C CB  . SER A 123 ? 0.5959 0.8931 0.4516 0.0053  -0.1111 -0.0151 138 SER A CB  
678  O OG  . SER A 123 ? 0.6056 0.8853 0.4448 0.0106  -0.1147 -0.0218 138 SER A OG  
679  N N   . PHE A 124 ? 0.6302 0.9602 0.5329 -0.0133 -0.1095 -0.0035 139 PHE A N   
680  C CA  . PHE A 124 ? 0.6377 0.9844 0.5563 -0.0153 -0.1042 0.0021  139 PHE A CA  
681  C C   . PHE A 124 ? 0.6868 1.0417 0.6168 -0.0220 -0.1129 0.0034  139 PHE A C   
682  O O   . PHE A 124 ? 0.7168 1.0809 0.6510 -0.0200 -0.1131 0.0062  139 PHE A O   
683  C CB  . PHE A 124 ? 0.6347 0.9893 0.5676 -0.0183 -0.0954 0.0051  139 PHE A CB  
684  C CG  . PHE A 124 ? 0.6122 0.9650 0.5402 -0.0119 -0.0856 0.0057  139 PHE A CG  
685  C CD1 . PHE A 124 ? 0.6168 0.9740 0.5426 -0.0064 -0.0796 0.0087  139 PHE A CD1 
686  C CD2 . PHE A 124 ? 0.5732 0.9209 0.5005 -0.0117 -0.0824 0.0041  139 PHE A CD2 
687  C CE1 . PHE A 124 ? 0.5941 0.9516 0.5185 -0.0017 -0.0705 0.0104  139 PHE A CE1 
688  C CE2 . PHE A 124 ? 0.5744 0.9232 0.5002 -0.0061 -0.0737 0.0051  139 PHE A CE2 
689  C CZ  . PHE A 124 ? 0.5592 0.9134 0.4843 -0.0015 -0.0676 0.0084  139 PHE A CZ  
690  N N   . THR A 125 ? 0.7492 1.1013 0.6854 -0.0300 -0.1201 0.0021  140 THR A N   
691  C CA  . THR A 125 ? 0.7491 1.1111 0.6997 -0.0380 -0.1286 0.0042  140 THR A CA  
692  C C   . THR A 125 ? 0.8258 1.1869 0.7685 -0.0347 -0.1377 0.0023  140 THR A C   
693  O O   . THR A 125 ? 0.9033 1.2790 0.8590 -0.0364 -0.1402 0.0057  140 THR A O   
694  C CB  . THR A 125 ? 0.7590 1.1130 0.7134 -0.0473 -0.1370 0.0029  140 THR A CB  
695  O OG1 . THR A 125 ? 0.7616 1.1150 0.7213 -0.0499 -0.1292 0.0051  140 THR A OG1 
696  C CG2 . THR A 125 ? 0.7697 1.1376 0.7431 -0.0566 -0.1451 0.0065  140 THR A CG2 
697  N N   . LEU A 126 ? 0.8733 1.2173 0.7941 -0.0291 -0.1429 -0.0032 141 LEU A N   
698  C CA  . LEU A 126 ? 0.9003 1.2401 0.8083 -0.0248 -0.1530 -0.0060 141 LEU A CA  
699  C C   . LEU A 126 ? 0.9241 1.2744 0.8309 -0.0172 -0.1467 -0.0017 141 LEU A C   
700  O O   . LEU A 126 ? 0.9335 1.2901 0.8421 -0.0165 -0.1547 -0.0007 141 LEU A O   
701  C CB  . LEU A 126 ? 0.9133 1.2312 0.7942 -0.0182 -0.1578 -0.0134 141 LEU A CB  
702  C CG  . LEU A 126 ? 0.9194 1.2303 0.7781 -0.0091 -0.1640 -0.0165 141 LEU A CG  
703  C CD1 . LEU A 126 ? 0.9185 1.2347 0.7842 -0.0145 -0.1796 -0.0172 141 LEU A CD1 
704  C CD2 . LEU A 126 ? 0.9172 1.2060 0.7484 -0.0016 -0.1670 -0.0245 141 LEU A CD2 
705  N N   . PHE A 127 ? 0.9188 1.2703 0.8232 -0.0117 -0.1331 0.0012  142 PHE A N   
706  C CA  . PHE A 127 ? 0.9442 1.3025 0.8467 -0.0047 -0.1266 0.0060  142 PHE A CA  
707  C C   . PHE A 127 ? 0.9627 1.3384 0.8881 -0.0081 -0.1237 0.0113  142 PHE A C   
708  O O   . PHE A 127 ? 0.9165 1.2978 0.8421 -0.0035 -0.1245 0.0148  142 PHE A O   
709  C CB  . PHE A 127 ? 0.9593 1.3120 0.8517 0.0017  -0.1140 0.0074  142 PHE A CB  
710  C CG  . PHE A 127 ? 1.0280 1.3660 0.8950 0.0090  -0.1155 0.0032  142 PHE A CG  
711  C CD1 . PHE A 127 ? 1.0626 1.3886 0.9211 0.0073  -0.1212 -0.0035 142 PHE A CD1 
712  C CD2 . PHE A 127 ? 1.1054 1.4408 0.9560 0.0180  -0.1116 0.0060  142 PHE A CD2 
713  C CE1 . PHE A 127 ? 1.0962 1.4078 0.9295 0.0157  -0.1228 -0.0085 142 PHE A CE1 
714  C CE2 . PHE A 127 ? 1.1722 1.4947 0.9972 0.0262  -0.1123 0.0020  142 PHE A CE2 
715  C CZ  . PHE A 127 ? 1.1314 1.4421 0.9475 0.0255  -0.1179 -0.0058 142 PHE A CZ  
716  N N   . GLY A 128 ? 0.9313 1.3148 0.8744 -0.0152 -0.1203 0.0120  143 GLY A N   
717  C CA  . GLY A 128 ? 0.8946 1.2950 0.8591 -0.0178 -0.1171 0.0162  143 GLY A CA  
718  C C   . GLY A 128 ? 0.8999 1.3128 0.8796 -0.0239 -0.1269 0.0169  143 GLY A C   
719  O O   . GLY A 128 ? 0.8567 1.2785 0.8416 -0.0208 -0.1313 0.0190  143 GLY A O   
720  N N   . GLU A 129 ? 0.9822 1.3966 0.9707 -0.0326 -0.1300 0.0160  144 GLU A N   
721  C CA  . GLU A 129 ? 1.0716 1.4992 1.0774 -0.0403 -0.1392 0.0177  144 GLU A CA  
722  C C   . GLU A 129 ? 1.0913 1.5119 1.0882 -0.0409 -0.1541 0.0145  144 GLU A C   
723  O O   . GLU A 129 ? 1.1348 1.5681 1.1421 -0.0408 -0.1614 0.0164  144 GLU A O   
724  C CB  . GLU A 129 ? 1.1384 1.5673 1.1549 -0.0503 -0.1382 0.0188  144 GLU A CB  
725  C CG  . GLU A 129 ? 1.1796 1.6182 1.2126 -0.0607 -0.1493 0.0208  144 GLU A CG  
726  C CD  . GLU A 129 ? 1.1947 1.6602 1.2532 -0.0629 -0.1461 0.0270  144 GLU A CD  
727  O OE1 . GLU A 129 ? 1.2726 1.7475 1.3381 -0.0606 -0.1339 0.0299  144 GLU A OE1 
728  O OE2 . GLU A 129 ? 1.1414 1.6194 1.2132 -0.0664 -0.1561 0.0287  144 GLU A OE2 
729  N N   . GLY A 130 ? 1.1240 1.5244 1.1014 -0.0409 -0.1591 0.0092  145 GLY A N   
730  C CA  . GLY A 130 ? 1.1918 1.5815 1.1568 -0.0413 -0.1745 0.0044  145 GLY A CA  
731  C C   . GLY A 130 ? 1.2327 1.6272 1.1913 -0.0336 -0.1802 0.0049  145 GLY A C   
732  O O   . GLY A 130 ? 1.2829 1.6794 1.2437 -0.0366 -0.1949 0.0030  145 GLY A O   
733  N N   . SER A 131 ? 1.2094 1.6051 1.1602 -0.0240 -0.1696 0.0076  146 SER A N   
734  C CA  . SER A 131 ? 1.2048 1.6048 1.1493 -0.0160 -0.1739 0.0096  146 SER A CA  
735  C C   . SER A 131 ? 1.0853 1.4927 1.0340 -0.0088 -0.1604 0.0154  146 SER A C   
736  O O   . SER A 131 ? 1.0578 1.4739 1.0225 -0.0118 -0.1503 0.0180  146 SER A O   
737  C CB  . SER A 131 ? 1.2739 1.6548 1.1881 -0.0092 -0.1817 0.0045  146 SER A CB  
738  O OG  . SER A 131 ? 1.3363 1.7088 1.2471 -0.0159 -0.1963 -0.0017 146 SER A OG  
739  N N   . ASN A 132 ? 0.9806 1.3835 0.9142 0.0006  -0.1607 0.0175  147 ASN A N   
740  C CA  . ASN A 132 ? 0.9138 1.3221 0.8521 0.0071  -0.1504 0.0236  147 ASN A CA  
741  C C   . ASN A 132 ? 0.8398 1.2336 0.7558 0.0147  -0.1413 0.0255  147 ASN A C   
742  O O   . ASN A 132 ? 0.8318 1.2262 0.7463 0.0211  -0.1361 0.0311  147 ASN A O   
743  C CB  . ASN A 132 ? 0.9289 1.3489 0.8756 0.0113  -0.1589 0.0271  147 ASN A CB  
744  C CG  . ASN A 132 ? 0.9941 1.4083 0.9249 0.0135  -0.1741 0.0243  147 ASN A CG  
745  O OD1 . ASN A 132 ? 1.0302 1.4313 0.9440 0.0116  -0.1789 0.0188  147 ASN A OD1 
746  N ND2 . ASN A 132 ? 1.0326 1.4561 0.9684 0.0183  -0.1826 0.0274  147 ASN A ND2 
747  N N   . LYS A 133 ? 0.7876 1.1685 0.6871 0.0143  -0.1391 0.0214  148 LYS A N   
748  C CA  . LYS A 133 ? 0.8145 1.1845 0.6954 0.0213  -0.1286 0.0240  148 LYS A CA  
749  C C   . LYS A 133 ? 0.7261 1.1009 0.6218 0.0198  -0.1147 0.0284  148 LYS A C   
750  O O   . LYS A 133 ? 0.6942 1.0668 0.5858 0.0250  -0.1071 0.0345  148 LYS A O   
751  C CB  . LYS A 133 ? 0.8791 1.2356 0.7398 0.0224  -0.1291 0.0181  148 LYS A CB  
752  C CG  . LYS A 133 ? 0.9647 1.3120 0.8035 0.0314  -0.1194 0.0214  148 LYS A CG  
753  C CD  . LYS A 133 ? 1.0522 1.3882 0.8747 0.0333  -0.1173 0.0152  148 LYS A CD  
754  C CE  . LYS A 133 ? 1.1030 1.4359 0.9145 0.0400  -0.1024 0.0199  148 LYS A CE  
755  N NZ  . LYS A 133 ? 1.1840 1.5100 0.9682 0.0506  -0.1020 0.0226  148 LYS A NZ  
756  N N   . LEU A 134 ? 0.6399 1.0204 0.5525 0.0124  -0.1121 0.0257  149 LEU A N   
757  C CA  . LEU A 134 ? 0.5857 0.9706 0.5121 0.0111  -0.1012 0.0288  149 LEU A CA  
758  C C   . LEU A 134 ? 0.5475 0.9407 0.4864 0.0136  -0.1010 0.0334  149 LEU A C   
759  O O   . LEU A 134 ? 0.5710 0.9617 0.5114 0.0168  -0.0933 0.0379  149 LEU A O   
760  C CB  . LEU A 134 ? 0.5820 0.9718 0.5225 0.0034  -0.0994 0.0250  149 LEU A CB  
761  C CG  . LEU A 134 ? 0.5775 0.9715 0.5313 0.0023  -0.0893 0.0272  149 LEU A CG  
762  C CD1 . LEU A 134 ? 0.5944 0.9797 0.5386 0.0058  -0.0805 0.0295  149 LEU A CD1 
763  C CD2 . LEU A 134 ? 0.5742 0.9735 0.5399 -0.0046 -0.0885 0.0239  149 LEU A CD2 
764  N N   . GLN A 135 ? 0.5104 0.9135 0.4595 0.0123  -0.1098 0.0326  150 GLN A N   
765  C CA  . GLN A 135 ? 0.4854 0.8975 0.4477 0.0159  -0.1098 0.0364  150 GLN A CA  
766  C C   . GLN A 135 ? 0.4746 0.8778 0.4235 0.0240  -0.1085 0.0420  150 GLN A C   
767  O O   . GLN A 135 ? 0.4721 0.8738 0.4265 0.0274  -0.1025 0.0461  150 GLN A O   
768  C CB  . GLN A 135 ? 0.4949 0.9206 0.4693 0.0141  -0.1206 0.0351  150 GLN A CB  
769  C CG  . GLN A 135 ? 0.4992 0.9374 0.4904 0.0184  -0.1209 0.0383  150 GLN A CG  
770  C CD  . GLN A 135 ? 0.5143 0.9699 0.5216 0.0152  -0.1307 0.0371  150 GLN A CD  
771  O OE1 . GLN A 135 ? 0.5426 1.0133 0.5697 0.0136  -0.1279 0.0373  150 GLN A OE1 
772  N NE2 . GLN A 135 ? 0.5484 1.0026 0.5472 0.0143  -0.1423 0.0360  150 GLN A NE2 
773  N N   . THR A 136 ? 0.4707 0.8666 0.4004 0.0271  -0.1143 0.0422  151 THR A N   
774  C CA  . THR A 136 ? 0.4756 0.8630 0.3897 0.0351  -0.1133 0.0485  151 THR A CA  
775  C C   . THR A 136 ? 0.4644 0.8427 0.3731 0.0357  -0.1003 0.0527  151 THR A C   
776  O O   . THR A 136 ? 0.4623 0.8374 0.3740 0.0392  -0.0953 0.0592  151 THR A O   
777  C CB  . THR A 136 ? 0.5040 0.8855 0.3960 0.0387  -0.1228 0.0468  151 THR A CB  
778  O OG1 . THR A 136 ? 0.5028 0.8938 0.4027 0.0391  -0.1360 0.0452  151 THR A OG1 
779  C CG2 . THR A 136 ? 0.5226 0.8926 0.3916 0.0471  -0.1187 0.0539  151 THR A CG2 
780  N N   . ILE A 137 ? 0.4574 0.8316 0.3594 0.0324  -0.0953 0.0492  152 ILE A N   
781  C CA  . ILE A 137 ? 0.4550 0.8233 0.3549 0.0323  -0.0831 0.0532  152 ILE A CA  
782  C C   . ILE A 137 ? 0.4416 0.8133 0.3618 0.0297  -0.0779 0.0558  152 ILE A C   
783  O O   . ILE A 137 ? 0.4464 0.8126 0.3667 0.0318  -0.0716 0.0626  152 ILE A O   
784  C CB  . ILE A 137 ? 0.4529 0.8202 0.3510 0.0281  -0.0788 0.0476  152 ILE A CB  
785  C CG1 . ILE A 137 ? 0.4810 0.8420 0.3568 0.0317  -0.0832 0.0442  152 ILE A CG1 
786  C CG2 . ILE A 137 ? 0.4467 0.8114 0.3479 0.0274  -0.0665 0.0521  152 ILE A CG2 
787  C CD1 . ILE A 137 ? 0.4807 0.8403 0.3567 0.0278  -0.0818 0.0372  152 ILE A CD1 
788  N N   . VAL A 138 ? 0.4307 0.8107 0.3675 0.0253  -0.0809 0.0504  153 VAL A N   
789  C CA  . VAL A 138 ? 0.4324 0.8145 0.3862 0.0233  -0.0757 0.0509  153 VAL A CA  
790  C C   . VAL A 138 ? 0.4561 0.8378 0.4155 0.0287  -0.0784 0.0553  153 VAL A C   
791  O O   . VAL A 138 ? 0.4503 0.8262 0.4163 0.0297  -0.0736 0.0586  153 VAL A O   
792  C CB  . VAL A 138 ? 0.4036 0.7946 0.3712 0.0175  -0.0761 0.0439  153 VAL A CB  
793  C CG1 . VAL A 138 ? 0.3850 0.7775 0.3672 0.0170  -0.0718 0.0434  153 VAL A CG1 
794  C CG2 . VAL A 138 ? 0.3979 0.7865 0.3599 0.0129  -0.0727 0.0405  153 VAL A CG2 
795  N N   . GLN A 139 ? 0.4907 0.8774 0.4476 0.0326  -0.0870 0.0554  154 GLN A N   
796  C CA  . GLN A 139 ? 0.5156 0.9013 0.4762 0.0392  -0.0902 0.0602  154 GLN A CA  
797  C C   . GLN A 139 ? 0.5398 0.9116 0.4865 0.0435  -0.0863 0.0689  154 GLN A C   
798  O O   . GLN A 139 ? 0.5261 0.8906 0.4785 0.0459  -0.0830 0.0735  154 GLN A O   
799  C CB  . GLN A 139 ? 0.5389 0.9349 0.5009 0.0426  -0.1011 0.0588  154 GLN A CB  
800  C CG  . GLN A 139 ? 0.5355 0.9472 0.5184 0.0409  -0.1037 0.0537  154 GLN A CG  
801  C CD  . GLN A 139 ? 0.5648 0.9900 0.5518 0.0413  -0.1147 0.0518  154 GLN A CD  
802  O OE1 . GLN A 139 ? 0.5687 0.9904 0.5414 0.0418  -0.1217 0.0526  154 GLN A OE1 
803  N NE2 . GLN A 139 ? 0.5711 1.0125 0.5779 0.0410  -0.1166 0.0493  154 GLN A NE2 
804  N N   . GLU A 140 ? 0.5712 0.9384 0.4991 0.0444  -0.0864 0.0715  155 GLU A N   
805  C CA  . GLU A 140 ? 0.6001 0.9557 0.5130 0.0491  -0.0824 0.0813  155 GLU A CA  
806  C C   . GLU A 140 ? 0.5859 0.9343 0.5047 0.0452  -0.0715 0.0859  155 GLU A C   
807  O O   . GLU A 140 ? 0.5818 0.9205 0.4963 0.0479  -0.0677 0.0955  155 GLU A O   
808  C CB  . GLU A 140 ? 0.6469 1.0000 0.5364 0.0519  -0.0841 0.0824  155 GLU A CB  
809  C CG  . GLU A 140 ? 0.6674 1.0212 0.5446 0.0589  -0.0955 0.0837  155 GLU A CG  
810  C CD  . GLU A 140 ? 0.7104 1.0599 0.5619 0.0623  -0.0972 0.0835  155 GLU A CD  
811  O OE1 . GLU A 140 ? 0.8143 1.1559 0.6467 0.0691  -0.0963 0.0919  155 GLU A OE1 
812  O OE2 . GLU A 140 ? 0.7073 1.0601 0.5564 0.0584  -0.0988 0.0751  155 GLU A OE2 
813  N N   . ALA A 141 ? 0.5753 0.9282 0.5044 0.0386  -0.0670 0.0795  156 ALA A N   
814  C CA  . ALA A 141 ? 0.5865 0.9346 0.5250 0.0338  -0.0581 0.0823  156 ALA A CA  
815  C C   . ALA A 141 ? 0.5854 0.9302 0.5409 0.0332  -0.0593 0.0816  156 ALA A C   
816  O O   . ALA A 141 ? 0.6368 0.9719 0.5968 0.0322  -0.0551 0.0881  156 ALA A O   
817  C CB  . ALA A 141 ? 0.5888 0.9432 0.5314 0.0278  -0.0542 0.0753  156 ALA A CB  
818  N N   . ALA A 142 ? 0.5655 0.9179 0.5304 0.0341  -0.0651 0.0740  157 ALA A N   
819  C CA  . ALA A 142 ? 0.5830 0.9319 0.5613 0.0362  -0.0667 0.0726  157 ALA A CA  
820  C C   . ALA A 142 ? 0.6060 0.9437 0.5798 0.0427  -0.0691 0.0813  157 ALA A C   
821  O O   . ALA A 142 ? 0.6106 0.9383 0.5928 0.0439  -0.0686 0.0829  157 ALA A O   
822  C CB  . ALA A 142 ? 0.5717 0.9335 0.5596 0.0378  -0.0719 0.0640  157 ALA A CB  
823  N N   . ASP A 143 ? 0.6596 0.9974 0.6193 0.0473  -0.0724 0.0869  158 ASP A N   
824  C CA  . ASP A 143 ? 0.6995 1.0254 0.6519 0.0537  -0.0743 0.0971  158 ASP A CA  
825  C C   . ASP A 143 ? 0.6769 0.9892 0.6289 0.0495  -0.0665 0.1056  158 ASP A C   
826  O O   . ASP A 143 ? 0.6549 0.9549 0.6145 0.0507  -0.0667 0.1097  158 ASP A O   
827  C CB  . ASP A 143 ? 0.7491 1.0769 0.6823 0.0587  -0.0784 0.1021  158 ASP A CB  
828  C CG  . ASP A 143 ? 0.7922 1.1308 0.7271 0.0642  -0.0887 0.0968  158 ASP A CG  
829  O OD1 . ASP A 143 ? 0.8433 1.1825 0.7911 0.0684  -0.0925 0.0952  158 ASP A OD1 
830  O OD2 . ASP A 143 ? 0.8379 1.1845 0.7621 0.0647  -0.0935 0.0941  158 ASP A OD2 
831  N N   . SER A 144 ? 0.6639 0.9786 0.6076 0.0448  -0.0598 0.1083  159 SER A N   
832  C CA  . SER A 144 ? 0.6772 0.9824 0.6214 0.0403  -0.0514 0.1181  159 SER A CA  
833  C C   . SER A 144 ? 0.6798 0.9795 0.6438 0.0348  -0.0507 0.1140  159 SER A C   
834  O O   . SER A 144 ? 0.7237 1.0094 0.6933 0.0337  -0.0496 0.1218  159 SER A O   
835  C CB  . SER A 144 ? 0.6675 0.9800 0.6031 0.0364  -0.0436 0.1194  159 SER A CB  
836  O OG  . SER A 144 ? 0.6940 1.0092 0.6082 0.0426  -0.0449 0.1228  159 SER A OG  
837  N N   . LEU A 145 ? 0.6330 0.9421 0.6068 0.0316  -0.0520 0.1020  160 LEU A N   
838  C CA  . LEU A 145 ? 0.6225 0.9265 0.6129 0.0269  -0.0519 0.0967  160 LEU A CA  
839  C C   . LEU A 145 ? 0.6487 0.9400 0.6443 0.0324  -0.0577 0.0975  160 LEU A C   
840  O O   . LEU A 145 ? 0.6545 0.9316 0.6583 0.0294  -0.0571 0.1011  160 LEU A O   
841  C CB  . LEU A 145 ? 0.5894 0.9060 0.5870 0.0243  -0.0531 0.0837  160 LEU A CB  
842  C CG  . LEU A 145 ? 0.5576 0.8683 0.5695 0.0215  -0.0546 0.0768  160 LEU A CG  
843  C CD1 . LEU A 145 ? 0.5590 0.8600 0.5783 0.0141  -0.0504 0.0825  160 LEU A CD1 
844  C CD2 . LEU A 145 ? 0.5338 0.8572 0.5504 0.0196  -0.0553 0.0651  160 LEU A CD2 
845  N N   . CYS A 146 ? 0.6517 0.9479 0.6431 0.0407  -0.0637 0.0942  161 CYS A N   
846  C CA  . CYS A 146 ? 0.6747 0.9598 0.6703 0.0482  -0.0694 0.0948  161 CYS A CA  
847  C C   . CYS A 146 ? 0.7175 0.9843 0.7076 0.0489  -0.0686 0.1085  161 CYS A C   
848  O O   . CYS A 146 ? 0.7426 0.9926 0.7402 0.0490  -0.0702 0.1103  161 CYS A O   
849  C CB  . CYS A 146 ? 0.6567 0.9535 0.6498 0.0574  -0.0759 0.0905  161 CYS A CB  
850  S SG  . CYS A 146 ? 0.5874 0.9031 0.5921 0.0579  -0.0776 0.0754  161 CYS A SG  
851  N N   . GLU A 147 ? 0.7625 1.0313 0.7387 0.0493  -0.0659 0.1183  162 GLU A N   
852  C CA  . GLU A 147 ? 0.8286 1.0808 0.7981 0.0499  -0.0639 0.1332  162 GLU A CA  
853  C C   . GLU A 147 ? 0.8118 1.0518 0.7928 0.0401  -0.0584 0.1382  162 GLU A C   
854  O O   . GLU A 147 ? 0.8021 1.0233 0.7889 0.0405  -0.0609 0.1439  162 GLU A O   
855  C CB  . GLU A 147 ? 0.8943 1.1523 0.8447 0.0519  -0.0605 0.1427  162 GLU A CB  
856  C CG  . GLU A 147 ? 0.9498 1.2149 0.8881 0.0621  -0.0685 0.1406  162 GLU A CG  
857  C CD  . GLU A 147 ? 1.0516 1.3050 0.9738 0.0689  -0.0702 0.1550  162 GLU A CD  
858  O OE1 . GLU A 147 ? 1.1016 1.3492 1.0138 0.0655  -0.0625 0.1670  162 GLU A OE1 
859  O OE2 . GLU A 147 ? 1.1107 1.3617 1.0303 0.0783  -0.0789 0.1549  162 GLU A OE2 
860  N N   . GLU A 148 ? 0.8057 1.0560 0.7911 0.0315  -0.0517 0.1357  163 GLU A N   
861  C CA  . GLU A 148 ? 0.8127 1.0551 0.8125 0.0213  -0.0474 0.1390  163 GLU A CA  
862  C C   . GLU A 148 ? 0.8131 1.0407 0.8270 0.0207  -0.0542 0.1318  163 GLU A C   
863  O O   . GLU A 148 ? 0.8136 1.0253 0.8371 0.0148  -0.0542 0.1385  163 GLU A O   
864  C CB  . GLU A 148 ? 0.8131 1.0719 0.8182 0.0140  -0.0416 0.1326  163 GLU A CB  
865  C CG  . GLU A 148 ? 0.8397 1.1103 0.8328 0.0131  -0.0331 0.1408  163 GLU A CG  
866  C CD  . GLU A 148 ? 0.8516 1.1314 0.8556 0.0038  -0.0256 0.1413  163 GLU A CD  
867  O OE1 . GLU A 148 ? 0.8324 1.1043 0.8526 -0.0041 -0.0245 0.1456  163 GLU A OE1 
868  O OE2 . GLU A 148 ? 0.9076 1.2025 0.9044 0.0046  -0.0214 0.1373  163 GLU A OE2 
869  N N   . LEU A 149 ? 0.8330 1.0661 0.8484 0.0269  -0.0601 0.1180  164 LEU A N   
870  C CA  . LEU A 149 ? 0.8606 1.0806 0.8867 0.0286  -0.0665 0.1091  164 LEU A CA  
871  C C   . LEU A 149 ? 0.9370 1.1356 0.9610 0.0361  -0.0724 0.1152  164 LEU A C   
872  O O   . LEU A 149 ? 0.9661 1.1453 0.9989 0.0345  -0.0767 0.1135  164 LEU A O   
873  C CB  . LEU A 149 ? 0.8412 1.0758 0.8684 0.0339  -0.0695 0.0934  164 LEU A CB  
874  C CG  . LEU A 149 ? 0.7891 1.0401 0.8205 0.0260  -0.0650 0.0860  164 LEU A CG  
875  C CD1 . LEU A 149 ? 0.7643 1.0345 0.7924 0.0310  -0.0659 0.0754  164 LEU A CD1 
876  C CD2 . LEU A 149 ? 0.7854 1.0262 0.8287 0.0195  -0.0668 0.0799  164 LEU A CD2 
877  N N   . GLN A 150 ? 0.9843 1.1853 0.9965 0.0445  -0.0735 0.1221  165 GLN A N   
878  C CA  . GLN A 150 ? 1.0386 1.2187 1.0477 0.0522  -0.0791 0.1299  165 GLN A CA  
879  C C   . GLN A 150 ? 1.1016 1.2599 1.1159 0.0431  -0.0770 0.1426  165 GLN A C   
880  O O   . GLN A 150 ? 1.1298 1.2660 1.1521 0.0433  -0.0825 0.1413  165 GLN A O   
881  C CB  . GLN A 150 ? 1.0181 1.2050 1.0121 0.0610  -0.0802 0.1382  165 GLN A CB  
882  C CG  . GLN A 150 ? 1.0001 1.2067 0.9916 0.0705  -0.0844 0.1270  165 GLN A CG  
883  C CD  . GLN A 150 ? 0.9997 1.1985 0.9980 0.0815  -0.0921 0.1190  165 GLN A CD  
884  O OE1 . GLN A 150 ? 0.9917 1.1674 0.9947 0.0830  -0.0952 0.1211  165 GLN A OE1 
885  N NE2 . GLN A 150 ? 0.9729 1.1912 0.9723 0.0895  -0.0954 0.1098  165 GLN A NE2 
886  N N   . ALA A 151 ? 1.1400 1.3050 1.1503 0.0349  -0.0688 0.1545  166 ALA A N   
887  C CA  . ALA A 151 ? 1.1829 1.3315 1.1995 0.0251  -0.0651 0.1692  166 ALA A CA  
888  C C   . ALA A 151 ? 1.2686 1.4065 1.3042 0.0151  -0.0676 0.1625  166 ALA A C   
889  O O   . ALA A 151 ? 1.2848 1.4015 1.3291 0.0085  -0.0692 0.1721  166 ALA A O   
890  C CB  . ALA A 151 ? 1.1514 1.3157 1.1611 0.0188  -0.0542 0.1810  166 ALA A CB  
891  N N   . CYS A 152 ? 1.3852 1.5373 1.4270 0.0136  -0.0684 0.1463  167 CYS A N   
892  C CA  . CYS A 152 ? 1.4838 1.6268 1.5419 0.0052  -0.0723 0.1378  167 CYS A CA  
893  C C   . CYS A 152 ? 1.5114 1.6302 1.5724 0.0122  -0.0831 0.1289  167 CYS A C   
894  O O   . CYS A 152 ? 1.5232 1.6262 1.5963 0.0052  -0.0882 0.1247  167 CYS A O   
895  C CB  . CYS A 152 ? 1.4968 1.6625 1.5586 0.0021  -0.0697 0.1240  167 CYS A CB  
896  S SG  . CYS A 152 ? 1.6074 1.7820 1.6626 0.0149  -0.0756 0.1041  167 CYS A SG  
897  N N   . ARG A 153 ? 1.5019 1.6178 1.5522 0.0263  -0.0873 0.1255  168 ARG A N   
898  C CA  . ARG A 153 ? 1.4866 1.5763 1.5383 0.0346  -0.0971 0.1201  168 ARG A CA  
899  C C   . ARG A 153 ? 1.5004 1.5623 1.5565 0.0277  -0.0990 0.1364  168 ARG A C   
900  O O   . ARG A 153 ? 1.5016 1.5673 1.5534 0.0233  -0.0926 0.1533  168 ARG A O   
901  C CB  . ARG A 153 ? 1.4793 1.5739 1.5199 0.0518  -0.1004 0.1156  168 ARG A CB  
902  C CG  . ARG A 153 ? 1.5015 1.5669 1.5404 0.0624  -0.1093 0.1174  168 ARG A CG  
903  C CD  . ARG A 153 ? 1.4880 1.5574 1.5236 0.0792  -0.1148 0.1024  168 ARG A CD  
904  N NE  . ARG A 153 ? 1.4936 1.5730 1.5203 0.0921  -0.1154 0.1080  168 ARG A NE  
905  C CZ  . ARG A 153 ? 1.4739 1.5328 1.4957 0.1016  -0.1210 0.1169  168 ARG A CZ  
906  N NH1 . ARG A 153 ? 1.4972 1.5220 1.5219 0.0993  -0.1264 0.1222  168 ARG A NH1 
907  N NH2 . ARG A 153 ? 1.4207 1.4928 1.4349 0.1133  -0.1221 0.1208  168 ARG A NH2 
908  N N   . GLY A 154 ? 1.5119 1.5454 1.5761 0.0264  -0.1078 0.1321  169 GLY A N   
909  C CA  . GLY A 154 ? 1.5307 1.5579 1.5981 0.0322  -0.1155 0.1118  169 GLY A CA  
910  C C   . GLY A 154 ? 1.5449 1.5693 1.6258 0.0179  -0.1171 0.1059  169 GLY A C   
911  O O   . GLY A 154 ? 1.6332 1.6327 1.7198 0.0173  -0.1267 0.0973  169 GLY A O   
912  N N   . GLN A 155 ? 1.5026 1.5519 1.5884 0.0070  -0.1085 0.1099  170 GLN A N   
913  C CA  . GLN A 155 ? 1.4258 1.4767 1.5257 -0.0067 -0.1099 0.1048  170 GLN A CA  
914  C C   . GLN A 155 ? 1.3043 1.3673 1.4014 -0.0009 -0.1131 0.0837  170 GLN A C   
915  O O   . GLN A 155 ? 1.2258 1.2999 1.3111 0.0125  -0.1122 0.0746  170 GLN A O   
916  C CB  . GLN A 155 ? 1.4380 1.5119 1.5451 -0.0197 -0.0990 0.1177  170 GLN A CB  
917  C CG  . GLN A 155 ? 1.4705 1.5425 1.5757 -0.0233 -0.0918 0.1399  170 GLN A CG  
918  C CD  . GLN A 155 ? 1.5255 1.5634 1.6342 -0.0245 -0.0987 0.1504  170 GLN A CD  
919  O OE1 . GLN A 155 ? 1.5394 1.5525 1.6554 -0.0255 -0.1097 0.1417  170 GLN A OE1 
920  N NE2 . GLN A 155 ? 1.5589 1.5941 1.6612 -0.0240 -0.0926 0.1694  170 GLN A NE2 
921  N N   . SER A 156 ? 1.2280 1.2891 1.3365 -0.0114 -0.1170 0.0769  171 SER A N   
922  C CA  . SER A 156 ? 1.1669 1.2428 1.2725 -0.0083 -0.1184 0.0593  171 SER A CA  
923  C C   . SER A 156 ? 1.1327 1.2373 1.2448 -0.0189 -0.1094 0.0646  171 SER A C   
924  O O   . SER A 156 ? 1.1563 1.2645 1.2794 -0.0288 -0.1120 0.0603  171 SER A O   
925  C CB  . SER A 156 ? 1.1726 1.2241 1.2839 -0.0105 -0.1310 0.0466  171 SER A CB  
926  O OG  . SER A 156 ? 1.1787 1.2044 1.2812 0.0023  -0.1386 0.0408  171 SER A OG  
927  N N   . SER A 157 ? 1.1005 1.2251 1.2051 -0.0156 -0.0994 0.0736  172 SER A N   
928  C CA  . SER A 157 ? 1.0344 1.1836 1.1433 -0.0242 -0.0897 0.0820  172 SER A CA  
929  C C   . SER A 157 ? 0.9955 1.1630 1.1071 -0.0270 -0.0895 0.0694  172 SER A C   
930  O O   . SER A 157 ? 0.9495 1.1169 1.0542 -0.0192 -0.0943 0.0546  172 SER A O   
931  C CB  . SER A 157 ? 1.0121 1.1775 1.1074 -0.0164 -0.0811 0.0894  172 SER A CB  
932  O OG  . SER A 157 ? 0.9684 1.1562 1.0652 -0.0230 -0.0717 0.0967  172 SER A OG  
933  N N   . ASP A 158 ? 0.9862 1.1695 1.1078 -0.0375 -0.0837 0.0760  173 ASP A N   
934  C CA  . ASP A 158 ? 0.9460 1.1524 1.0658 -0.0376 -0.0803 0.0674  173 ASP A CA  
935  C C   . ASP A 158 ? 0.8944 1.1211 1.0027 -0.0327 -0.0701 0.0736  173 ASP A C   
936  O O   . ASP A 158 ? 0.8793 1.1121 0.9896 -0.0370 -0.0627 0.0874  173 ASP A O   
937  C CB  . ASP A 158 ? 0.9719 1.1862 1.1088 -0.0502 -0.0804 0.0695  173 ASP A CB  
938  C CG  . ASP A 158 ? 0.9709 1.2089 1.1046 -0.0493 -0.0768 0.0613  173 ASP A CG  
939  O OD1 . ASP A 158 ? 0.9082 1.1648 1.0366 -0.0479 -0.0673 0.0674  173 ASP A OD1 
940  O OD2 . ASP A 158 ? 1.0009 1.2378 1.1363 -0.0495 -0.0839 0.0486  173 ASP A OD2 
941  N N   . LEU A 159 ? 0.8383 1.0752 0.9342 -0.0236 -0.0700 0.0634  174 LEU A N   
942  C CA  . LEU A 159 ? 0.7985 1.0554 0.8841 -0.0200 -0.0622 0.0663  174 LEU A CA  
943  C C   . LEU A 159 ? 0.7453 1.0183 0.8356 -0.0253 -0.0599 0.0610  174 LEU A C   
944  O O   . LEU A 159 ? 0.8682 1.1372 0.9671 -0.0294 -0.0653 0.0535  174 LEU A O   
945  C CB  . LEU A 159 ? 0.8257 1.0862 0.8982 -0.0086 -0.0638 0.0589  174 LEU A CB  
946  C CG  . LEU A 159 ? 0.8532 1.1069 0.9242 -0.0022 -0.0708 0.0452  174 LEU A CG  
947  C CD1 . LEU A 159 ? 0.8463 1.1083 0.9208 -0.0060 -0.0723 0.0347  174 LEU A CD1 
948  C CD2 . LEU A 159 ? 0.8709 1.1325 0.9312 0.0087  -0.0703 0.0417  174 LEU A CD2 
949  N N   . SER A 160 ? 0.6712 0.9613 0.7553 -0.0247 -0.0529 0.0644  175 SER A N   
950  C CA  . SER A 160 ? 0.6424 0.9475 0.7315 -0.0294 -0.0501 0.0613  175 SER A CA  
951  C C   . SER A 160 ? 0.6240 0.9395 0.7129 -0.0321 -0.0414 0.0729  175 SER A C   
952  O O   . SER A 160 ? 0.6215 0.9510 0.7035 -0.0300 -0.0370 0.0713  175 SER A O   
953  C CB  . SER A 160 ? 0.6217 0.9222 0.7266 -0.0373 -0.0551 0.0578  175 SER A CB  
954  O OG  . SER A 160 ? 0.6100 0.9266 0.7196 -0.0410 -0.0518 0.0566  175 SER A OG  
955  N N   . VAL A 161 ? 0.6059 0.9137 0.7023 -0.0364 -0.0389 0.0847  176 VAL A N   
956  C CA  . VAL A 161 ? 0.5963 0.9125 0.6894 -0.0370 -0.0294 0.0975  176 VAL A CA  
957  C C   . VAL A 161 ? 0.5809 0.8970 0.6542 -0.0279 -0.0277 0.0986  176 VAL A C   
958  O O   . VAL A 161 ? 0.5755 0.9038 0.6376 -0.0241 -0.0223 0.0994  176 VAL A O   
959  C CB  . VAL A 161 ? 0.6237 0.9297 0.7285 -0.0435 -0.0274 0.1112  176 VAL A CB  
960  C CG1 . VAL A 161 ? 0.6281 0.9433 0.7265 -0.0425 -0.0163 0.1258  176 VAL A CG1 
961  C CG2 . VAL A 161 ? 0.6272 0.9330 0.7546 -0.0539 -0.0309 0.1101  176 VAL A CG2 
962  N N   . VAL A 162 ? 0.5958 0.8975 0.6649 -0.0239 -0.0333 0.0979  177 VAL A N   
963  C CA  . VAL A 162 ? 0.6167 0.9173 0.6688 -0.0153 -0.0332 0.1001  177 VAL A CA  
964  C C   . VAL A 162 ? 0.6111 0.9251 0.6533 -0.0104 -0.0341 0.0895  177 VAL A C   
965  O O   . VAL A 162 ? 0.6451 0.9667 0.6744 -0.0065 -0.0305 0.0926  177 VAL A O   
966  C CB  . VAL A 162 ? 0.6468 0.9298 0.6980 -0.0109 -0.0400 0.1005  177 VAL A CB  
967  C CG1 . VAL A 162 ? 0.6558 0.9230 0.7188 -0.0175 -0.0401 0.1107  177 VAL A CG1 
968  C CG2 . VAL A 162 ? 0.6516 0.9318 0.7056 -0.0075 -0.0476 0.0860  177 VAL A CG2 
969  N N   . LEU A 163 ? 0.5964 0.9130 0.6442 -0.0110 -0.0389 0.0774  178 LEU A N   
970  C CA  . LEU A 163 ? 0.5880 0.9166 0.6279 -0.0074 -0.0400 0.0681  178 LEU A CA  
971  C C   . LEU A 163 ? 0.5770 0.9179 0.6141 -0.0100 -0.0346 0.0688  178 LEU A C   
972  O O   . LEU A 163 ? 0.5410 0.8895 0.5669 -0.0064 -0.0339 0.0665  178 LEU A O   
973  C CB  . LEU A 163 ? 0.5861 0.9147 0.6325 -0.0078 -0.0452 0.0564  178 LEU A CB  
974  C CG  . LEU A 163 ? 0.5917 0.9093 0.6398 -0.0031 -0.0511 0.0520  178 LEU A CG  
975  C CD1 . LEU A 163 ? 0.5831 0.9028 0.6350 -0.0029 -0.0549 0.0402  178 LEU A CD1 
976  C CD2 . LEU A 163 ? 0.5871 0.9069 0.6256 0.0047  -0.0524 0.0533  178 LEU A CD2 
977  N N   . MET A 164 ? 0.6275 0.9701 0.6761 -0.0163 -0.0316 0.0712  179 MET A N   
978  C CA  . MET A 164 ? 0.6351 0.9891 0.6831 -0.0181 -0.0254 0.0736  179 MET A CA  
979  C C   . MET A 164 ? 0.5749 0.9312 0.6088 -0.0134 -0.0200 0.0816  179 MET A C   
980  O O   . MET A 164 ? 0.5729 0.9369 0.5959 -0.0100 -0.0178 0.0790  179 MET A O   
981  C CB  . MET A 164 ? 0.7304 1.0857 0.7952 -0.0253 -0.0222 0.0795  179 MET A CB  
982  C CG  . MET A 164 ? 0.7919 1.1528 0.8684 -0.0296 -0.0256 0.0711  179 MET A CG  
983  S SD  . MET A 164 ? 0.9167 1.2929 0.9864 -0.0268 -0.0216 0.0666  179 MET A SD  
984  C CE  . MET A 164 ? 0.8907 1.2738 0.9543 -0.0242 -0.0108 0.0791  179 MET A CE  
985  N N   . ARG A 165 ? 0.5355 0.8837 0.5684 -0.0130 -0.0181 0.0915  180 ARG A N   
986  C CA  . ARG A 165 ? 0.5495 0.8991 0.5669 -0.0079 -0.0129 0.0998  180 ARG A CA  
987  C C   . ARG A 165 ? 0.5153 0.8659 0.5156 -0.0009 -0.0179 0.0930  180 ARG A C   
988  O O   . ARG A 165 ? 0.5230 0.8796 0.5094 0.0032  -0.0153 0.0923  180 ARG A O   
989  C CB  . ARG A 165 ? 0.6064 0.9450 0.6250 -0.0085 -0.0114 0.1119  180 ARG A CB  
990  C CG  . ARG A 165 ? 0.6387 0.9798 0.6425 -0.0042 -0.0036 0.1237  180 ARG A CG  
991  C CD  . ARG A 165 ? 0.6680 0.9974 0.6741 -0.0056 -0.0019 0.1372  180 ARG A CD  
992  N NE  . ARG A 165 ? 0.6961 1.0252 0.7232 -0.0150 0.0025  0.1447  180 ARG A NE  
993  C CZ  . ARG A 165 ? 0.7410 1.0574 0.7840 -0.0211 -0.0026 0.1464  180 ARG A CZ  
994  N NH1 . ARG A 165 ? 0.7491 1.0516 0.7890 -0.0177 -0.0118 0.1409  180 ARG A NH1 
995  N NH2 . ARG A 165 ? 0.7636 1.0812 0.8266 -0.0306 0.0011  0.1538  180 ARG A NH2 
996  N N   . ALA A 166 ? 0.4792 0.8239 0.4812 0.0007  -0.0254 0.0875  181 ALA A N   
997  C CA  . ALA A 166 ? 0.4450 0.7915 0.4346 0.0066  -0.0308 0.0824  181 ALA A CA  
998  C C   . ALA A 166 ? 0.4265 0.7827 0.4120 0.0063  -0.0317 0.0736  181 ALA A C   
999  O O   . ALA A 166 ? 0.4167 0.7757 0.3876 0.0104  -0.0327 0.0731  181 ALA A O   
1000 C CB  . ALA A 166 ? 0.4472 0.7884 0.4434 0.0083  -0.0378 0.0780  181 ALA A CB  
1001 N N   . VAL A 167 ? 0.4104 0.7705 0.4074 0.0016  -0.0319 0.0668  182 VAL A N   
1002 C CA  . VAL A 167 ? 0.4089 0.7767 0.4016 0.0014  -0.0334 0.0589  182 VAL A CA  
1003 C C   . VAL A 167 ? 0.4050 0.7764 0.3895 0.0023  -0.0276 0.0618  182 VAL A C   
1004 O O   . VAL A 167 ? 0.4161 0.7897 0.3885 0.0052  -0.0293 0.0580  182 VAL A O   
1005 C CB  . VAL A 167 ? 0.4024 0.7738 0.4066 -0.0027 -0.0359 0.0507  182 VAL A CB  
1006 C CG1 . VAL A 167 ? 0.4079 0.7747 0.4215 -0.0031 -0.0396 0.0487  182 VAL A CG1 
1007 C CG2 . VAL A 167 ? 0.4063 0.7809 0.4178 -0.0067 -0.0315 0.0507  182 VAL A CG2 
1008 N N   . THR A 168 ? 0.3993 0.7712 0.3904 0.0002  -0.0208 0.0687  183 THR A N   
1009 C CA  . THR A 168 ? 0.4042 0.7809 0.3871 0.0029  -0.0137 0.0728  183 THR A CA  
1010 C C   . THR A 168 ? 0.3991 0.7726 0.3610 0.0098  -0.0137 0.0761  183 THR A C   
1011 O O   . THR A 168 ? 0.3801 0.7556 0.3286 0.0140  -0.0135 0.0722  183 THR A O   
1012 C CB  . THR A 168 ? 0.4217 0.8016 0.4176 -0.0007 -0.0058 0.0819  183 THR A CB  
1013 O OG1 . THR A 168 ? 0.4158 0.7975 0.4309 -0.0073 -0.0083 0.0776  183 THR A OG1 
1014 C CG2 . THR A 168 ? 0.4326 0.8209 0.4219 0.0030  0.0027  0.0854  183 THR A CG2 
1015 N N   . ASN A 169 ? 0.4195 0.7867 0.3776 0.0115  -0.0152 0.0824  184 ASN A N   
1016 C CA  . ASN A 169 ? 0.4460 0.8098 0.3828 0.0187  -0.0162 0.0859  184 ASN A CA  
1017 C C   . ASN A 169 ? 0.4357 0.7995 0.3619 0.0214  -0.0250 0.0759  184 ASN A C   
1018 O O   . ASN A 169 ? 0.4411 0.8044 0.3491 0.0267  -0.0256 0.0743  184 ASN A O   
1019 C CB  . ASN A 169 ? 0.4734 0.8297 0.4086 0.0203  -0.0176 0.0946  184 ASN A CB  
1020 C CG  . ASN A 169 ? 0.5214 0.8751 0.4359 0.0271  -0.0129 0.1041  184 ASN A CG  
1021 O OD1 . ASN A 169 ? 0.5446 0.9012 0.4419 0.0323  -0.0111 0.1018  184 ASN A OD1 
1022 N ND2 . ASN A 169 ? 0.5365 0.8836 0.4514 0.0277  -0.0111 0.1151  184 ASN A ND2 
1023 N N   . VAL A 170 ? 0.4253 0.7900 0.3631 0.0176  -0.0320 0.0691  185 VAL A N   
1024 C CA  . VAL A 170 ? 0.4229 0.7894 0.3549 0.0184  -0.0404 0.0603  185 VAL A CA  
1025 C C   . VAL A 170 ? 0.4197 0.7876 0.3428 0.0190  -0.0392 0.0549  185 VAL A C   
1026 O O   . VAL A 170 ? 0.4262 0.7917 0.3349 0.0221  -0.0450 0.0507  185 VAL A O   
1027 C CB  . VAL A 170 ? 0.4205 0.7907 0.3691 0.0135  -0.0453 0.0543  185 VAL A CB  
1028 C CG1 . VAL A 170 ? 0.4184 0.7922 0.3638 0.0124  -0.0524 0.0463  185 VAL A CG1 
1029 C CG2 . VAL A 170 ? 0.4332 0.8015 0.3884 0.0150  -0.0485 0.0576  185 VAL A CG2 
1030 N N   . ILE A 171 ? 0.3958 0.7669 0.3281 0.0161  -0.0327 0.0545  186 ILE A N   
1031 C CA  . ILE A 171 ? 0.3723 0.7444 0.2988 0.0170  -0.0315 0.0490  186 ILE A CA  
1032 C C   . ILE A 171 ? 0.3809 0.7512 0.2893 0.0244  -0.0257 0.0528  186 ILE A C   
1033 O O   . ILE A 171 ? 0.3733 0.7401 0.2671 0.0285  -0.0285 0.0470  186 ILE A O   
1034 C CB  . ILE A 171 ? 0.3624 0.7397 0.3061 0.0121  -0.0273 0.0476  186 ILE A CB  
1035 C CG1 . ILE A 171 ? 0.3572 0.7359 0.3160 0.0061  -0.0325 0.0438  186 ILE A CG1 
1036 C CG2 . ILE A 171 ? 0.3593 0.7370 0.2973 0.0141  -0.0265 0.0422  186 ILE A CG2 
1037 C CD1 . ILE A 171 ? 0.3505 0.7291 0.3075 0.0041  -0.0395 0.0359  186 ILE A CD1 
1038 N N   . CYS A 172 ? 0.3938 0.7658 0.3024 0.0263  -0.0177 0.0624  187 CYS A N   
1039 C CA  . CYS A 172 ? 0.4403 0.8109 0.3282 0.0347  -0.0118 0.0674  187 CYS A CA  
1040 C C   . CYS A 172 ? 0.4616 0.8246 0.3273 0.0402  -0.0207 0.0631  187 CYS A C   
1041 O O   . CYS A 172 ? 0.4613 0.8209 0.3074 0.0471  -0.0209 0.0591  187 CYS A O   
1042 C CB  . CYS A 172 ? 0.4498 0.8226 0.3404 0.0353  -0.0031 0.0804  187 CYS A CB  
1043 S SG  . CYS A 172 ? 0.4644 0.8460 0.3832 0.0275  0.0060  0.0868  187 CYS A SG  
1044 N N   . ARG A 173 ? 0.4811 0.8413 0.3504 0.0376  -0.0286 0.0636  188 ARG A N   
1045 C CA  . ARG A 173 ? 0.5245 0.8788 0.3764 0.0418  -0.0391 0.0600  188 ARG A CA  
1046 C C   . ARG A 173 ? 0.5271 0.8788 0.3741 0.0408  -0.0481 0.0483  188 ARG A C   
1047 O O   . ARG A 173 ? 0.5734 0.9188 0.3990 0.0467  -0.0529 0.0441  188 ARG A O   
1048 C CB  . ARG A 173 ? 0.5315 0.8862 0.3943 0.0387  -0.0460 0.0625  188 ARG A CB  
1049 C CG  . ARG A 173 ? 0.5509 0.9024 0.4051 0.0435  -0.0435 0.0731  188 ARG A CG  
1050 C CD  . ARG A 173 ? 0.5725 0.9193 0.4066 0.0499  -0.0537 0.0717  188 ARG A CD  
1051 N NE  . ARG A 173 ? 0.5852 0.9324 0.4288 0.0491  -0.0607 0.0748  188 ARG A NE  
1052 C CZ  . ARG A 173 ? 0.6136 0.9596 0.4478 0.0529  -0.0722 0.0728  188 ARG A CZ  
1053 N NH1 . ARG A 173 ? 0.6397 0.9827 0.4540 0.0570  -0.0794 0.0669  188 ARG A NH1 
1054 N NH2 . ARG A 173 ? 0.6204 0.9680 0.4655 0.0531  -0.0776 0.0761  188 ARG A NH2 
1055 N N   . LEU A 174 ? 0.5026 0.8580 0.3686 0.0333  -0.0506 0.0434  189 LEU A N   
1056 C CA  . LEU A 174 ? 0.5024 0.8551 0.3673 0.0304  -0.0595 0.0339  189 LEU A CA  
1057 C C   . LEU A 174 ? 0.5145 0.8617 0.3660 0.0347  -0.0567 0.0289  189 LEU A C   
1058 O O   . LEU A 174 ? 0.5303 0.8695 0.3685 0.0364  -0.0654 0.0214  189 LEU A O   
1059 C CB  . LEU A 174 ? 0.4867 0.8458 0.3753 0.0218  -0.0606 0.0318  189 LEU A CB  
1060 C CG  . LEU A 174 ? 0.4887 0.8459 0.3800 0.0171  -0.0682 0.0239  189 LEU A CG  
1061 C CD1 . LEU A 174 ? 0.5171 0.8707 0.3992 0.0172  -0.0804 0.0202  189 LEU A CD1 
1062 C CD2 . LEU A 174 ? 0.4694 0.8342 0.3826 0.0098  -0.0670 0.0238  189 LEU A CD2 
1063 N N   . VAL A 175 ? 0.5033 0.8544 0.3590 0.0366  -0.0453 0.0328  190 VAL A N   
1064 C CA  . VAL A 175 ? 0.5169 0.8644 0.3606 0.0425  -0.0414 0.0286  190 VAL A CA  
1065 C C   . VAL A 175 ? 0.5466 0.8894 0.3642 0.0538  -0.0373 0.0304  190 VAL A C   
1066 O O   . VAL A 175 ? 0.5583 0.8924 0.3579 0.0598  -0.0412 0.0229  190 VAL A O   
1067 C CB  . VAL A 175 ? 0.5011 0.8569 0.3624 0.0401  -0.0315 0.0314  190 VAL A CB  
1068 C CG1 . VAL A 175 ? 0.5056 0.8588 0.3553 0.0478  -0.0270 0.0272  190 VAL A CG1 
1069 C CG2 . VAL A 175 ? 0.4619 0.8206 0.3444 0.0304  -0.0364 0.0284  190 VAL A CG2 
1070 N N   . PHE A 176 ? 0.5726 0.9201 0.3866 0.0572  -0.0293 0.0402  191 PHE A N   
1071 C CA  . PHE A 176 ? 0.6207 0.9648 0.4073 0.0691  -0.0239 0.0430  191 PHE A CA  
1072 C C   . PHE A 176 ? 0.6361 0.9742 0.4044 0.0729  -0.0306 0.0455  191 PHE A C   
1073 O O   . PHE A 176 ? 0.7086 1.0427 0.4511 0.0834  -0.0273 0.0470  191 PHE A O   
1074 C CB  . PHE A 176 ? 0.6303 0.9845 0.4200 0.0730  -0.0076 0.0547  191 PHE A CB  
1075 C CG  . PHE A 176 ? 0.6385 1.0037 0.4572 0.0654  0.0001  0.0588  191 PHE A CG  
1076 C CD1 . PHE A 176 ? 0.6603 1.0262 0.4915 0.0616  -0.0029 0.0505  191 PHE A CD1 
1077 C CD2 . PHE A 176 ? 0.6415 1.0156 0.4745 0.0620  0.0100  0.0714  191 PHE A CD2 
1078 C CE1 . PHE A 176 ? 0.6742 1.0503 0.5315 0.0549  0.0032  0.0541  191 PHE A CE1 
1079 C CE2 . PHE A 176 ? 0.6507 1.0344 0.5111 0.0544  0.0157  0.0747  191 PHE A CE2 
1080 C CZ  . PHE A 176 ? 0.6597 1.0449 0.5319 0.0512  0.0121  0.0657  191 PHE A CZ  
1081 N N   . SER A 177 ? 0.6043 0.9427 0.3851 0.0657  -0.0391 0.0466  192 SER A N   
1082 C CA  . SER A 177 ? 0.6003 0.9354 0.3679 0.0692  -0.0442 0.0519  192 SER A CA  
1083 C C   . SER A 177 ? 0.6177 0.9576 0.3834 0.0729  -0.0309 0.0657  192 SER A C   
1084 O O   . SER A 177 ? 0.6333 0.9692 0.3765 0.0809  -0.0303 0.0710  192 SER A O   
1085 C CB  . SER A 177 ? 0.6043 0.9289 0.3409 0.0779  -0.0542 0.0448  192 SER A CB  
1086 O OG  . SER A 177 ? 0.5873 0.9065 0.3270 0.0731  -0.0686 0.0332  192 SER A OG  
1087 N N   . SER A 178 ? 0.6088 0.9569 0.3981 0.0667  -0.0207 0.0719  193 SER A N   
1088 C CA  . SER A 178 ? 0.6235 0.9760 0.4169 0.0673  -0.0091 0.0863  193 SER A CA  
1089 C C   . SER A 178 ? 0.6447 0.9924 0.4366 0.0666  -0.0155 0.0927  193 SER A C   
1090 O O   . SER A 178 ? 0.6457 0.9904 0.4443 0.0629  -0.0277 0.0864  193 SER A O   
1091 C CB  . SER A 178 ? 0.6072 0.9683 0.4305 0.0584  -0.0007 0.0906  193 SER A CB  
1092 O OG  . SER A 178 ? 0.6060 0.9656 0.4491 0.0504  -0.0064 0.0926  193 SER A OG  
1093 N N   . SER A 179 ? 0.6794 1.0270 0.4637 0.0703  -0.0069 0.1061  194 SER A N   
1094 C CA  . SER A 179 ? 0.7055 1.0473 0.4874 0.0708  -0.0122 0.1139  194 SER A CA  
1095 C C   . SER A 179 ? 0.7157 1.0590 0.5145 0.0658  -0.0022 0.1283  194 SER A C   
1096 O O   . SER A 179 ? 0.7295 1.0669 0.5217 0.0682  -0.0027 0.1387  194 SER A O   
1097 C CB  . SER A 179 ? 0.7292 1.0647 0.4769 0.0821  -0.0155 0.1163  194 SER A CB  
1098 O OG  . SER A 179 ? 0.7414 1.0712 0.4883 0.0823  -0.0277 0.1167  194 SER A OG  
1099 N N   . TYR A 180 ? 0.7326 1.0830 0.5543 0.0584  0.0056  0.1286  195 TYR A N   
1100 C CA  . TYR A 180 ? 0.7538 1.1056 0.5958 0.0516  0.0142  0.1410  195 TYR A CA  
1101 C C   . TYR A 180 ? 0.7782 1.1210 0.6305 0.0480  0.0056  0.1436  195 TYR A C   
1102 O O   . TYR A 180 ? 0.8010 1.1412 0.6572 0.0471  -0.0059 0.1329  195 TYR A O   
1103 C CB  . TYR A 180 ? 0.7317 1.0918 0.6008 0.0428  0.0183  0.1365  195 TYR A CB  
1104 C CG  . TYR A 180 ? 0.7142 1.0836 0.5774 0.0464  0.0248  0.1309  195 TYR A CG  
1105 C CD1 . TYR A 180 ? 0.7152 1.0892 0.5588 0.0547  0.0355  0.1386  195 TYR A CD1 
1106 C CD2 . TYR A 180 ? 0.6827 1.0563 0.5590 0.0423  0.0206  0.1183  195 TYR A CD2 
1107 C CE1 . TYR A 180 ? 0.7237 1.1061 0.5612 0.0597  0.0417  0.1331  195 TYR A CE1 
1108 C CE2 . TYR A 180 ? 0.6855 1.0665 0.5562 0.0466  0.0262  0.1133  195 TYR A CE2 
1109 C CZ  . TYR A 180 ? 0.7127 1.0980 0.5642 0.0556  0.0366  0.1203  195 TYR A CZ  
1110 O OH  . TYR A 180 ? 0.7296 1.1219 0.5744 0.0617  0.0423  0.1150  195 TYR A OH  
1111 N N   . GLN A 181 ? 0.8414 1.1796 0.6987 0.0460  0.0116  0.1583  196 GLN A N   
1112 C CA  . GLN A 181 ? 0.8783 1.2071 0.7518 0.0411  0.0052  0.1612  196 GLN A CA  
1113 C C   . GLN A 181 ? 0.8512 1.1824 0.7532 0.0304  0.0112  0.1644  196 GLN A C   
1114 O O   . GLN A 181 ? 0.8875 1.2290 0.7952 0.0277  0.0206  0.1660  196 GLN A O   
1115 C CB  . GLN A 181 ? 0.9299 1.2483 0.7872 0.0469  0.0049  0.1749  196 GLN A CB  
1116 C CG  . GLN A 181 ? 0.9492 1.2624 0.7901 0.0547  -0.0084 0.1677  196 GLN A CG  
1117 C CD  . GLN A 181 ? 1.0516 1.3583 0.8648 0.0642  -0.0083 0.1790  196 GLN A CD  
1118 O OE1 . GLN A 181 ? 1.1092 1.4173 0.9094 0.0667  0.0031  0.1911  196 GLN A OE1 
1119 N NE2 . GLN A 181 ? 1.0816 1.3825 0.8855 0.0702  -0.0209 0.1755  196 GLN A NE2 
1120 N N   . PRO A 182 ? 0.8511 1.1732 0.7713 0.0249  0.0051  0.1641  197 PRO A N   
1121 C CA  . PRO A 182 ? 0.8492 1.1722 0.7965 0.0145  0.0079  0.1643  197 PRO A CA  
1122 C C   . PRO A 182 ? 0.8648 1.1937 0.8205 0.0092  0.0206  0.1782  197 PRO A C   
1123 O O   . PRO A 182 ? 0.8853 1.2243 0.8580 0.0029  0.0248  0.1748  197 PRO A O   
1124 C CB  . PRO A 182 ? 0.8571 1.1644 0.8145 0.0124  -0.0001 0.1663  197 PRO A CB  
1125 C CG  . PRO A 182 ? 0.8634 1.1680 0.8059 0.0209  -0.0100 0.1576  197 PRO A CG  
1126 C CD  . PRO A 182 ? 0.8662 1.1774 0.7833 0.0287  -0.0062 0.1609  197 PRO A CD  
1127 N N   . SER A 183 ? 0.8641 1.1879 0.8088 0.0119  0.0268  0.1943  198 SER A N   
1128 C CA  . SER A 183 ? 0.8637 1.1937 0.8182 0.0063  0.0397  0.2103  198 SER A CA  
1129 C C   . SER A 183 ? 0.8678 1.2171 0.8159 0.0096  0.0507  0.2095  198 SER A C   
1130 O O   . SER A 183 ? 0.8758 1.2363 0.8413 0.0032  0.0607  0.2177  198 SER A O   
1131 C CB  . SER A 183 ? 0.8885 1.2081 0.8285 0.0098  0.0439  0.2285  198 SER A CB  
1132 O OG  . SER A 183 ? 0.9204 1.2458 0.8297 0.0213  0.0489  0.2311  198 SER A OG  
1133 N N   . ASP A 184 ? 0.8555 1.2083 0.7795 0.0198  0.0480  0.1992  199 ASP A N   
1134 C CA  . ASP A 184 ? 0.8392 1.2065 0.7486 0.0268  0.0579  0.1985  199 ASP A CA  
1135 C C   . ASP A 184 ? 0.7883 1.1709 0.7222 0.0198  0.0661  0.1985  199 ASP A C   
1136 O O   . ASP A 184 ? 0.7923 1.1756 0.7472 0.0126  0.0592  0.1879  199 ASP A O   
1137 C CB  . ASP A 184 ? 0.8360 1.2026 0.7239 0.0356  0.0493  0.1816  199 ASP A CB  
1138 C CG  . ASP A 184 ? 0.8545 1.2313 0.7199 0.0458  0.0585  0.1813  199 ASP A CG  
1139 O OD1 . ASP A 184 ? 0.7957 1.1856 0.6726 0.0443  0.0662  0.1790  199 ASP A OD1 
1140 O OD2 . ASP A 184 ? 0.8979 1.2691 0.7331 0.0560  0.0572  0.1827  199 ASP A OD2 
1141 N N   . PRO A 185 ? 0.7470 1.1430 0.6780 0.0225  0.0809  0.2106  200 PRO A N   
1142 C CA  . PRO A 185 ? 0.7056 1.1192 0.6607 0.0170  0.0894  0.2118  200 PRO A CA  
1143 C C   . PRO A 185 ? 0.6558 1.0782 0.6088 0.0218  0.0865  0.1945  200 PRO A C   
1144 O O   . PRO A 185 ? 0.6420 1.0738 0.6206 0.0146  0.0863  0.1903  200 PRO A O   
1145 C CB  . PRO A 185 ? 0.7408 1.1674 0.6878 0.0219  0.1069  0.2298  200 PRO A CB  
1146 C CG  . PRO A 185 ? 0.7741 1.1864 0.7003 0.0253  0.1066  0.2416  200 PRO A CG  
1147 C CD  . PRO A 185 ? 0.7674 1.1630 0.6747 0.0304  0.0908  0.2262  200 PRO A CD  
1148 N N   . GLU A 186 ? 0.6392 1.0579 0.5622 0.0336  0.0836  0.1848  201 GLU A N   
1149 C CA  . GLU A 186 ? 0.6177 1.0430 0.5372 0.0386  0.0812  0.1694  201 GLU A CA  
1150 C C   . GLU A 186 ? 0.5830 1.0007 0.5177 0.0310  0.0669  0.1550  201 GLU A C   
1151 O O   . GLU A 186 ? 0.5662 0.9914 0.5134 0.0293  0.0656  0.1460  201 GLU A O   
1152 C CB  . GLU A 186 ? 0.6400 1.0609 0.5227 0.0530  0.0804  0.1621  201 GLU A CB  
1153 C CG  . GLU A 186 ? 0.6482 1.0756 0.5277 0.0587  0.0798  0.1482  201 GLU A CG  
1154 C CD  . GLU A 186 ? 0.6846 1.1061 0.5275 0.0732  0.0786  0.1402  201 GLU A CD  
1155 O OE1 . GLU A 186 ? 0.7021 1.1089 0.5252 0.0758  0.0672  0.1339  201 GLU A OE1 
1156 O OE2 . GLU A 186 ? 0.7081 1.1396 0.5423 0.0825  0.0883  0.1394  201 GLU A OE2 
1157 N N   . LEU A 187 ? 0.5741 0.9775 0.5068 0.0275  0.0565  0.1533  202 LEU A N   
1158 C CA  . LEU A 187 ? 0.5662 0.9629 0.5143 0.0203  0.0442  0.1418  202 LEU A CA  
1159 C C   . LEU A 187 ? 0.5575 0.9610 0.5374 0.0095  0.0467  0.1456  202 LEU A C   
1160 O O   . LEU A 187 ? 0.5065 0.9137 0.5003 0.0055  0.0419  0.1354  202 LEU A O   
1161 C CB  . LEU A 187 ? 0.5751 0.9567 0.5164 0.0196  0.0345  0.1418  202 LEU A CB  
1162 C CG  . LEU A 187 ? 0.5515 0.9253 0.5113 0.0118  0.0236  0.1344  202 LEU A CG  
1163 C CD1 . LEU A 187 ? 0.5268 0.9024 0.4864 0.0123  0.0155  0.1183  202 LEU A CD1 
1164 C CD2 . LEU A 187 ? 0.5668 0.9272 0.5189 0.0134  0.0169  0.1381  202 LEU A CD2 
1165 N N   . GLN A 188 ? 0.5970 1.0016 0.5879 0.0047  0.0539  0.1608  203 GLN A N   
1166 C CA  . GLN A 188 ? 0.6235 1.0341 0.6458 -0.0066 0.0561  0.1665  203 GLN A CA  
1167 C C   . GLN A 188 ? 0.5899 1.0194 0.6258 -0.0068 0.0626  0.1638  203 GLN A C   
1168 O O   . GLN A 188 ? 0.5532 0.9870 0.6134 -0.0150 0.0583  0.1594  203 GLN A O   
1169 C CB  . GLN A 188 ? 0.7038 1.1126 0.7331 -0.0111 0.0640  0.1857  203 GLN A CB  
1170 C CG  . GLN A 188 ? 0.7710 1.1772 0.8322 -0.0247 0.0609  0.1911  203 GLN A CG  
1171 C CD  . GLN A 188 ? 0.8187 1.2089 0.8856 -0.0289 0.0456  0.1777  203 GLN A CD  
1172 O OE1 . GLN A 188 ? 0.8529 1.2294 0.9014 -0.0233 0.0385  0.1721  203 GLN A OE1 
1173 N NE2 . GLN A 188 ? 0.8239 1.2169 0.9163 -0.0380 0.0403  0.1722  203 GLN A NE2 
1174 N N   . THR A 189 ? 0.5791 1.0195 0.5982 0.0032  0.0724  0.1658  204 THR A N   
1175 C CA  . THR A 189 ? 0.5723 1.0304 0.6006 0.0061  0.0785  0.1620  204 THR A CA  
1176 C C   . THR A 189 ? 0.5457 1.0003 0.5772 0.0054  0.0670  0.1444  204 THR A C   
1177 O O   . THR A 189 ? 0.5601 1.0253 0.6137 0.0007  0.0665  0.1415  204 THR A O   
1178 C CB  . THR A 189 ? 0.5912 1.0570 0.5933 0.0201  0.0891  0.1639  204 THR A CB  
1179 O OG1 . THR A 189 ? 0.6057 1.0787 0.6057 0.0213  0.1023  0.1820  204 THR A OG1 
1180 C CG2 . THR A 189 ? 0.5807 1.0625 0.5899 0.0253  0.0938  0.1572  204 THR A CG2 
1181 N N   . VAL A 190 ? 0.5335 0.9739 0.5429 0.0103  0.0579  0.1337  205 VAL A N   
1182 C CA  . VAL A 190 ? 0.5083 0.9438 0.5156 0.0108  0.0474  0.1177  205 VAL A CA  
1183 C C   . VAL A 190 ? 0.4906 0.9226 0.5210 0.0000  0.0386  0.1136  205 VAL A C   
1184 O O   . VAL A 190 ? 0.4746 0.9112 0.5160 -0.0021 0.0344  0.1053  205 VAL A O   
1185 C CB  . VAL A 190 ? 0.5172 0.9383 0.4981 0.0166  0.0392  0.1096  205 VAL A CB  
1186 C CG1 . VAL A 190 ? 0.4986 0.9143 0.4807 0.0148  0.0280  0.0951  205 VAL A CG1 
1187 C CG2 . VAL A 190 ? 0.5336 0.9557 0.4876 0.0285  0.0453  0.1105  205 VAL A CG2 
1188 N N   . ILE A 191 ? 0.5044 0.9268 0.5406 -0.0060 0.0352  0.1189  206 ILE A N   
1189 C CA  . ILE A 191 ? 0.5024 0.9199 0.5593 -0.0154 0.0267  0.1148  206 ILE A CA  
1190 C C   . ILE A 191 ? 0.4925 0.9235 0.5753 -0.0219 0.0310  0.1196  206 ILE A C   
1191 O O   . ILE A 191 ? 0.4738 0.9055 0.5712 -0.0271 0.0238  0.1120  206 ILE A O   
1192 C CB  . ILE A 191 ? 0.5076 0.9112 0.5671 -0.0201 0.0227  0.1206  206 ILE A CB  
1193 C CG1 . ILE A 191 ? 0.5133 0.9045 0.5536 -0.0149 0.0147  0.1125  206 ILE A CG1 
1194 C CG2 . ILE A 191 ? 0.4989 0.8987 0.5830 -0.0302 0.0161  0.1189  206 ILE A CG2 
1195 C CD1 . ILE A 191 ? 0.5423 0.9321 0.5584 -0.0062 0.0190  0.1168  206 ILE A CD1 
1196 N N   . GLN A 192 ? 0.5235 0.9659 0.6120 -0.0216 0.0425  0.1327  207 GLN A N   
1197 C CA  . GLN A 192 ? 0.5380 0.9963 0.6544 -0.0283 0.0470  0.1388  207 GLN A CA  
1198 C C   . GLN A 192 ? 0.5095 0.9818 0.6298 -0.0237 0.0476  0.1303  207 GLN A C   
1199 O O   . GLN A 192 ? 0.5005 0.9803 0.6443 -0.0305 0.0432  0.1279  207 GLN A O   
1200 C CB  . GLN A 192 ? 0.5720 1.0408 0.6963 -0.0298 0.0601  0.1568  207 GLN A CB  
1201 C CG  . GLN A 192 ? 0.6247 1.0794 0.7532 -0.0373 0.0583  0.1671  207 GLN A CG  
1202 C CD  . GLN A 192 ? 0.6480 1.0904 0.7964 -0.0485 0.0453  0.1616  207 GLN A CD  
1203 O OE1 . GLN A 192 ? 0.6532 1.0780 0.7898 -0.0474 0.0351  0.1519  207 GLN A OE1 
1204 N NE2 . GLN A 192 ? 0.6798 1.1318 0.8588 -0.0590 0.0455  0.1679  207 GLN A NE2 
1205 N N   . TYR A 193 ? 0.4828 0.9572 0.5803 -0.0123 0.0515  0.1250  208 TYR A N   
1206 C CA  . TYR A 193 ? 0.4761 0.9610 0.5773 -0.0076 0.0508  0.1165  208 TYR A CA  
1207 C C   . TYR A 193 ? 0.4520 0.9258 0.5503 -0.0096 0.0373  0.1019  208 TYR A C   
1208 O O   . TYR A 193 ? 0.4084 0.8900 0.5222 -0.0119 0.0333  0.0969  208 TYR A O   
1209 C CB  . TYR A 193 ? 0.5014 0.9938 0.5830 0.0055  0.0602  0.1165  208 TYR A CB  
1210 C CG  . TYR A 193 ? 0.5353 1.0126 0.5836 0.0144  0.0574  0.1091  208 TYR A CG  
1211 C CD1 . TYR A 193 ? 0.5309 0.9955 0.5677 0.0154  0.0458  0.0953  208 TYR A CD1 
1212 C CD2 . TYR A 193 ? 0.5620 1.0389 0.5901 0.0222  0.0663  0.1164  208 TYR A CD2 
1213 C CE1 . TYR A 193 ? 0.5408 0.9924 0.5493 0.0227  0.0424  0.0891  208 TYR A CE1 
1214 C CE2 . TYR A 193 ? 0.5689 1.0322 0.5664 0.0306  0.0625  0.1093  208 TYR A CE2 
1215 C CZ  . TYR A 193 ? 0.5605 1.0115 0.5496 0.0303  0.0503  0.0957  208 TYR A CZ  
1216 O OH  . TYR A 193 ? 0.5904 1.0289 0.5512 0.0377  0.0461  0.0896  208 TYR A OH  
1217 N N   . ASN A 194 ? 0.4474 0.9044 0.5266 -0.0085 0.0305  0.0958  209 ASN A N   
1218 C CA  . ASN A 194 ? 0.4237 0.8707 0.5025 -0.0118 0.0186  0.0842  209 ASN A CA  
1219 C C   . ASN A 194 ? 0.4253 0.8742 0.5294 -0.0220 0.0133  0.0850  209 ASN A C   
1220 O O   . ASN A 194 ? 0.4042 0.8576 0.5185 -0.0238 0.0079  0.0785  209 ASN A O   
1221 C CB  . ASN A 194 ? 0.4249 0.8562 0.4849 -0.0105 0.0130  0.0803  209 ASN A CB  
1222 C CG  . ASN A 194 ? 0.4361 0.8635 0.4709 -0.0013 0.0137  0.0754  209 ASN A CG  
1223 O OD1 . ASN A 194 ? 0.4298 0.8626 0.4598 0.0041  0.0157  0.0713  209 ASN A OD1 
1224 N ND2 . ASN A 194 ? 0.4443 0.8611 0.4631 0.0007  0.0109  0.0752  209 ASN A ND2 
1225 N N   . ASP A 195 ? 0.4421 0.8870 0.5563 -0.0283 0.0143  0.0934  210 ASP A N   
1226 C CA  . ASP A 195 ? 0.4662 0.9102 0.6044 -0.0385 0.0078  0.0939  210 ASP A CA  
1227 C C   . ASP A 195 ? 0.4803 0.9413 0.6410 -0.0417 0.0087  0.0948  210 ASP A C   
1228 O O   . ASP A 195 ? 0.4510 0.9110 0.6235 -0.0465 -0.0008 0.0874  210 ASP A O   
1229 C CB  . ASP A 195 ? 0.4935 0.9313 0.6402 -0.0447 0.0105  0.1054  210 ASP A CB  
1230 C CG  . ASP A 195 ? 0.5209 0.9514 0.6885 -0.0550 0.0012  0.1040  210 ASP A CG  
1231 O OD1 . ASP A 195 ? 0.5387 0.9569 0.7005 -0.0553 -0.0091 0.0928  210 ASP A OD1 
1232 O OD2 . ASP A 195 ? 0.5522 0.9886 0.7416 -0.0629 0.0040  0.1143  210 ASP A OD2 
1233 N N   . GLY A 196 ? 0.4887 0.9660 0.6545 -0.0382 0.0199  0.1037  211 GLY A N   
1234 C CA  . GLY A 196 ? 0.4738 0.9706 0.6621 -0.0397 0.0218  0.1055  211 GLY A CA  
1235 C C   . GLY A 196 ? 0.4529 0.9512 0.6362 -0.0348 0.0148  0.0929  211 GLY A C   
1236 O O   . GLY A 196 ? 0.4619 0.9685 0.6648 -0.0392 0.0087  0.0902  211 GLY A O   
1237 N N   . ILE A 197 ? 0.4371 0.9269 0.5940 -0.0258 0.0150  0.0858  212 ILE A N   
1238 C CA  . ILE A 197 ? 0.4229 0.9111 0.5718 -0.0209 0.0085  0.0747  212 ILE A CA  
1239 C C   . ILE A 197 ? 0.4364 0.9137 0.5890 -0.0276 -0.0044 0.0662  212 ILE A C   
1240 O O   . ILE A 197 ? 0.4494 0.9322 0.6127 -0.0289 -0.0109 0.0611  212 ILE A O   
1241 C CB  . ILE A 197 ? 0.4092 0.8881 0.5288 -0.0111 0.0110  0.0697  212 ILE A CB  
1242 C CG1 . ILE A 197 ? 0.4113 0.9021 0.5262 -0.0022 0.0231  0.0761  212 ILE A CG1 
1243 C CG2 . ILE A 197 ? 0.3993 0.8722 0.5099 -0.0080 0.0026  0.0586  212 ILE A CG2 
1244 C CD1 . ILE A 197 ? 0.4175 0.8984 0.5031 0.0078  0.0253  0.0714  212 ILE A CD1 
1245 N N   . VAL A 198 ? 0.4388 0.9011 0.5822 -0.0311 -0.0081 0.0648  213 VAL A N   
1246 C CA  . VAL A 198 ? 0.4420 0.8934 0.5876 -0.0366 -0.0192 0.0572  213 VAL A CA  
1247 C C   . VAL A 198 ? 0.4658 0.9246 0.6375 -0.0445 -0.0246 0.0587  213 VAL A C   
1248 O O   . VAL A 198 ? 0.4634 0.9226 0.6390 -0.0454 -0.0330 0.0512  213 VAL A O   
1249 C CB  . VAL A 198 ? 0.4455 0.8817 0.5816 -0.0387 -0.0210 0.0576  213 VAL A CB  
1250 C CG1 . VAL A 198 ? 0.4381 0.8639 0.5780 -0.0434 -0.0319 0.0498  213 VAL A CG1 
1251 C CG2 . VAL A 198 ? 0.4514 0.8804 0.5627 -0.0315 -0.0183 0.0550  213 VAL A CG2 
1252 N N   . GLN A 199 ? 0.4938 0.9581 0.6830 -0.0504 -0.0200 0.0688  214 GLN A N   
1253 C CA  . GLN A 199 ? 0.5027 0.9737 0.7198 -0.0597 -0.0259 0.0714  214 GLN A CA  
1254 C C   . GLN A 199 ? 0.4977 0.9853 0.7268 -0.0575 -0.0280 0.0685  214 GLN A C   
1255 O O   . GLN A 199 ? 0.4660 0.9543 0.7081 -0.0624 -0.0389 0.0629  214 GLN A O   
1256 C CB  . GLN A 199 ? 0.5420 1.0207 0.7777 -0.0659 -0.0176 0.0859  214 GLN A CB  
1257 C CG  . GLN A 199 ? 0.5869 1.0573 0.8433 -0.0780 -0.0260 0.0886  214 GLN A CG  
1258 C CD  . GLN A 199 ? 0.6265 1.1152 0.9164 -0.0870 -0.0225 0.1009  214 GLN A CD  
1259 O OE1 . GLN A 199 ? 0.6043 1.1112 0.9120 -0.0878 -0.0242 0.1003  214 GLN A OE1 
1260 N NE2 . GLN A 199 ? 0.6499 1.1338 0.9498 -0.0943 -0.0184 0.1125  214 GLN A NE2 
1261 N N   . THR A 200 ? 0.4895 0.9899 0.7132 -0.0494 -0.0181 0.0721  215 THR A N   
1262 C CA  . THR A 200 ? 0.5120 1.0307 0.7497 -0.0462 -0.0182 0.0716  215 THR A CA  
1263 C C   . THR A 200 ? 0.5047 1.0157 0.7313 -0.0430 -0.0293 0.0593  215 THR A C   
1264 O O   . THR A 200 ? 0.5150 1.0325 0.7575 -0.0465 -0.0382 0.0561  215 THR A O   
1265 C CB  . THR A 200 ? 0.5288 1.0603 0.7591 -0.0359 -0.0047 0.0771  215 THR A CB  
1266 O OG1 . THR A 200 ? 0.5356 1.0737 0.7726 -0.0380 0.0067  0.0894  215 THR A OG1 
1267 C CG2 . THR A 200 ? 0.5278 1.0798 0.7753 -0.0315 -0.0043 0.0774  215 THR A CG2 
1268 N N   . ILE A 201 ? 0.5173 1.0147 0.7165 -0.0365 -0.0289 0.0530  216 ILE A N   
1269 C CA  . ILE A 201 ? 0.5074 0.9962 0.6925 -0.0331 -0.0380 0.0427  216 ILE A CA  
1270 C C   . ILE A 201 ? 0.5122 0.9908 0.7006 -0.0402 -0.0500 0.0363  216 ILE A C   
1271 O O   . ILE A 201 ? 0.5015 0.9796 0.6888 -0.0392 -0.0588 0.0297  216 ILE A O   
1272 C CB  . ILE A 201 ? 0.4994 0.9749 0.6559 -0.0266 -0.0346 0.0389  216 ILE A CB  
1273 C CG1 . ILE A 201 ? 0.4854 0.9687 0.6352 -0.0179 -0.0251 0.0424  216 ILE A CG1 
1274 C CG2 . ILE A 201 ? 0.4852 0.9500 0.6269 -0.0251 -0.0436 0.0296  216 ILE A CG2 
1275 C CD1 . ILE A 201 ? 0.4992 0.9698 0.6236 -0.0129 -0.0213 0.0406  216 ILE A CD1 
1276 N N   . ALA A 202 ? 0.5325 1.0017 0.7230 -0.0463 -0.0506 0.0382  217 ALA A N   
1277 C CA  . ALA A 202 ? 0.5406 0.9976 0.7323 -0.0519 -0.0618 0.0315  217 ALA A CA  
1278 C C   . ALA A 202 ? 0.5694 1.0349 0.7822 -0.0570 -0.0715 0.0295  217 ALA A C   
1279 O O   . ALA A 202 ? 0.5964 1.0548 0.8030 -0.0568 -0.0822 0.0206  217 ALA A O   
1280 C CB  . ALA A 202 ? 0.5435 0.9902 0.7383 -0.0574 -0.0602 0.0357  217 ALA A CB  
1281 N N   . ARG A 203 ? 0.5987 1.0802 0.8366 -0.0613 -0.0679 0.0381  218 ARG A N   
1282 C CA  . ARG A 203 ? 0.6172 1.1099 0.8795 -0.0668 -0.0775 0.0373  218 ARG A CA  
1283 C C   . ARG A 203 ? 0.6293 1.1303 0.8858 -0.0593 -0.0813 0.0318  218 ARG A C   
1284 O O   . ARG A 203 ? 0.6144 1.1133 0.8737 -0.0610 -0.0941 0.0246  218 ARG A O   
1285 C CB  . ARG A 203 ? 0.6248 1.1366 0.9173 -0.0726 -0.0709 0.0494  218 ARG A CB  
1286 C CG  . ARG A 203 ? 0.6724 1.1762 0.9743 -0.0815 -0.0679 0.0568  218 ARG A CG  
1287 C CD  . ARG A 203 ? 0.7436 1.2686 1.0765 -0.0877 -0.0598 0.0709  218 ARG A CD  
1288 N NE  . ARG A 203 ? 0.7850 1.3267 1.1136 -0.0787 -0.0440 0.0786  218 ARG A NE  
1289 C CZ  . ARG A 203 ? 0.8117 1.3690 1.1562 -0.0807 -0.0311 0.0925  218 ARG A CZ  
1290 N NH1 . ARG A 203 ? 0.8649 1.4235 1.2328 -0.0928 -0.0318 0.1018  218 ARG A NH1 
1291 N NH2 . ARG A 203 ? 0.7871 1.3579 1.1231 -0.0704 -0.0173 0.0974  218 ARG A NH2 
1292 N N   . GLY A 204 ? 0.6382 1.1468 0.8847 -0.0506 -0.0710 0.0349  219 GLY A N   
1293 C CA  . GLY A 204 ? 0.6694 1.1889 0.9158 -0.0431 -0.0730 0.0325  219 GLY A CA  
1294 C C   . GLY A 204 ? 0.7262 1.2334 0.9434 -0.0346 -0.0741 0.0255  219 GLY A C   
1295 O O   . GLY A 204 ? 0.8175 1.3089 1.0177 -0.0358 -0.0807 0.0186  219 GLY A O   
1296 N N   . GLY A 205 ? 0.7843 1.2987 0.9958 -0.0257 -0.0672 0.0276  220 GLY A N   
1297 C CA  . GLY A 205 ? 0.8216 1.3271 1.0114 -0.0180 -0.0707 0.0218  220 GLY A CA  
1298 C C   . GLY A 205 ? 0.8480 1.3383 1.0099 -0.0129 -0.0649 0.0199  220 GLY A C   
1299 O O   . GLY A 205 ? 0.7881 1.2792 0.9453 -0.0097 -0.0549 0.0239  220 GLY A O   
1300 N N   . LEU A 206 ? 0.9005 1.3773 1.0442 -0.0127 -0.0719 0.0139  221 LEU A N   
1301 C CA  . LEU A 206 ? 0.8767 1.3430 0.9982 -0.0062 -0.0715 0.0115  221 LEU A CA  
1302 C C   . LEU A 206 ? 0.8156 1.2872 0.9406 -0.0011 -0.0786 0.0100  221 LEU A C   
1303 O O   . LEU A 206 ? 0.7671 1.2335 0.8798 0.0057  -0.0784 0.0097  221 LEU A O   
1304 C CB  . LEU A 206 ? 0.9125 1.3644 1.0160 -0.0093 -0.0761 0.0069  221 LEU A CB  
1305 C CG  . LEU A 206 ? 0.9738 1.4171 1.0687 -0.0135 -0.0716 0.0067  221 LEU A CG  
1306 C CD1 . LEU A 206 ? 1.0381 1.4722 1.1206 -0.0157 -0.0781 0.0017  221 LEU A CD1 
1307 C CD2 . LEU A 206 ? 0.9746 1.4120 1.0557 -0.0099 -0.0641 0.0088  221 LEU A CD2 
1308 N N   . VAL A 207 ? 0.7724 1.2540 0.9154 -0.0048 -0.0859 0.0093  222 VAL A N   
1309 C CA  . VAL A 207 ? 0.7302 1.2133 0.8742 -0.0031 -0.0972 0.0059  222 VAL A CA  
1310 C C   . VAL A 207 ? 0.7090 1.1773 0.8277 0.0005  -0.1021 0.0024  222 VAL A C   
1311 O O   . VAL A 207 ? 0.7149 1.1843 0.8308 0.0061  -0.1080 0.0021  222 VAL A O   
1312 C CB  . VAL A 207 ? 0.7197 1.2207 0.8848 0.0019  -0.0988 0.0090  222 VAL A CB  
1313 C CG1 . VAL A 207 ? 0.7955 1.3023 0.9710 -0.0002 -0.1126 0.0057  222 VAL A CG1 
1314 C CG2 . VAL A 207 ? 0.7071 1.2242 0.8961 -0.0009 -0.0904 0.0147  222 VAL A CG2 
1315 N N   . ASP A 208 ? 0.7065 1.1615 0.8072 -0.0027 -0.0998 0.0004  223 ASP A N   
1316 C CA  . ASP A 208 ? 0.6703 1.1144 0.7514 -0.0020 -0.1062 -0.0030 223 ASP A CA  
1317 C C   . ASP A 208 ? 0.6651 1.1137 0.7557 -0.0055 -0.1164 -0.0073 223 ASP A C   
1318 O O   . ASP A 208 ? 0.6781 1.1327 0.7856 -0.0108 -0.1163 -0.0078 223 ASP A O   
1319 C CB  . ASP A 208 ? 0.6474 1.0794 0.7102 -0.0044 -0.1005 -0.0036 223 ASP A CB  
1320 C CG  . ASP A 208 ? 0.6693 1.1000 0.7357 -0.0103 -0.1003 -0.0067 223 ASP A CG  
1321 O OD1 . ASP A 208 ? 0.6415 1.0758 0.7175 -0.0128 -0.1077 -0.0101 223 ASP A OD1 
1322 O OD2 . ASP A 208 ? 0.6541 1.0790 0.7128 -0.0122 -0.0936 -0.0059 223 ASP A OD2 
1323 N N   . ILE A 209 ? 0.6495 1.0952 0.7300 -0.0025 -0.1257 -0.0101 224 ILE A N   
1324 C CA  . ILE A 209 ? 0.6523 1.1006 0.7391 -0.0053 -0.1373 -0.0155 224 ILE A CA  
1325 C C   . ILE A 209 ? 0.6643 1.1282 0.7814 -0.0080 -0.1410 -0.0141 224 ILE A C   
1326 O O   . ILE A 209 ? 0.6871 1.1561 0.8148 -0.0100 -0.1527 -0.0178 224 ILE A O   
1327 C CB  . ILE A 209 ? 0.6450 1.0839 0.7233 -0.0102 -0.1369 -0.0204 224 ILE A CB  
1328 C CG1 . ILE A 209 ? 0.6131 1.0398 0.6626 -0.0069 -0.1344 -0.0218 224 ILE A CG1 
1329 C CG2 . ILE A 209 ? 0.6667 1.1071 0.7550 -0.0138 -0.1492 -0.0267 224 ILE A CG2 
1330 C CD1 . ILE A 209 ? 0.5726 0.9917 0.6142 -0.0100 -0.1295 -0.0247 224 ILE A CD1 
1331 N N   . LYS A 219 ? 0.6393 1.3470 1.0938 -0.0424 -0.0324 0.0955  234 LYS A N   
1332 C CA  . LYS A 219 ? 0.6602 1.3454 1.0779 -0.0367 -0.0224 0.0935  234 LYS A CA  
1333 C C   . LYS A 219 ? 0.6824 1.3836 1.0987 -0.0270 -0.0023 0.1033  234 LYS A C   
1334 O O   . LYS A 219 ? 0.7155 1.4383 1.1428 -0.0166 0.0033  0.1055  234 LYS A O   
1335 C CB  . LYS A 219 ? 0.3080 0.9700 0.6902 -0.0272 -0.0299 0.0800  234 LYS A CB  
1336 C CG  . LYS A 219 ? 0.3075 0.9815 0.6886 -0.0133 -0.0304 0.0763  234 LYS A CG  
1337 C CD  . LYS A 219 ? 0.3069 0.9569 0.6587 -0.0085 -0.0423 0.0637  234 LYS A CD  
1338 C CE  . LYS A 219 ? 0.3064 0.9417 0.6592 -0.0207 -0.0585 0.0575  234 LYS A CE  
1339 N NZ  . LYS A 219 ? 0.3074 0.9204 0.6310 -0.0162 -0.0689 0.0464  234 LYS A NZ  
1340 N N   . ASP A 220 ? 0.8154 1.5074 1.2188 -0.0295 0.0087  0.1095  235 ASP A N   
1341 C CA  . ASP A 220 ? 0.8333 1.4950 1.2116 -0.0361 0.0046  0.1051  235 ASP A CA  
1342 C C   . ASP A 220 ? 0.7568 1.3978 1.0943 -0.0236 0.0067  0.0955  235 ASP A C   
1343 O O   . ASP A 220 ? 0.6555 1.2763 0.9695 -0.0247 0.0087  0.0939  235 ASP A O   
1344 C CB  . ASP A 220 ? 0.8401 1.4880 1.2282 -0.0499 -0.0132 0.0991  235 ASP A CB  
1345 C CG  . ASP A 220 ? 0.8574 1.4735 1.2136 -0.0512 -0.0192 0.0900  235 ASP A CG  
1346 O OD1 . ASP A 220 ? 0.9048 1.5112 1.2456 -0.0508 -0.0095 0.0948  235 ASP A OD1 
1347 O OD2 . ASP A 220 ? 0.7917 1.3941 1.1387 -0.0522 -0.0334 0.0787  235 ASP A OD2 
1348 N N   . LEU A 221 ? 0.7200 1.3667 1.0504 -0.0115 0.0061  0.0897  236 LEU A N   
1349 C CA  . LEU A 221 ? 0.7038 1.3341 0.9984 0.0011  0.0109  0.0831  236 LEU A CA  
1350 C C   . LEU A 221 ? 0.6628 1.3046 0.9523 0.0098  0.0288  0.0918  236 LEU A C   
1351 O O   . LEU A 221 ? 0.6928 1.3229 0.9536 0.0211  0.0340  0.0874  236 LEU A O   
1352 C CB  . LEU A 221 ? 0.7367 1.3665 1.0240 0.0117  0.0040  0.0743  236 LEU A CB  
1353 C CG  . LEU A 221 ? 0.8101 1.4319 1.1015 0.0063  -0.0136 0.0659  236 LEU A CG  
1354 C CD1 . LEU A 221 ? 0.8055 1.4056 1.0866 -0.0058 -0.0229 0.0615  236 LEU A CD1 
1355 C CD2 . LEU A 221 ? 0.8298 1.4771 1.1576 0.0033  -0.0195 0.0695  236 LEU A CD2 
1356 N N   . LYS A 222 ? 0.6517 1.3163 0.9686 0.0046  0.0380  0.1044  237 LYS A N   
1357 C CA  . LYS A 222 ? 0.6761 1.3517 0.9868 0.0123  0.0561  0.1142  237 LYS A CA  
1358 C C   . LYS A 222 ? 0.6257 1.2840 0.9201 0.0050  0.0602  0.1190  237 LYS A C   
1359 O O   . LYS A 222 ? 0.6186 1.2732 0.8907 0.0137  0.0718  0.1221  237 LYS A O   
1360 C CB  . LYS A 222 ? 0.6925 1.4042 1.0409 0.0116  0.0663  0.1274  237 LYS A CB  
1361 C CG  . LYS A 222 ? 0.7429 1.4751 1.0973 0.0274  0.0713  0.1252  237 LYS A CG  
1362 C CD  . LYS A 222 ? 0.7628 1.4917 1.1241 0.0282  0.0549  0.1141  237 LYS A CD  
1363 C CE  . LYS A 222 ? 0.7956 1.5516 1.1738 0.0422  0.0602  0.1154  237 LYS A CE  
1364 N NZ  . LYS A 222 ? 0.8240 1.5746 1.2037 0.0457  0.0445  0.1046  237 LYS A NZ  
1365 N N   . ARG A 223 ? 0.5562 1.2029 0.8606 -0.0101 0.0498  0.1189  238 ARG A N   
1366 C CA  . ARG A 223 ? 0.5233 1.1522 0.8140 -0.0172 0.0517  0.1231  238 ARG A CA  
1367 C C   . ARG A 223 ? 0.5171 1.1198 0.7673 -0.0093 0.0494  0.1128  238 ARG A C   
1368 O O   . ARG A 223 ? 0.4897 1.0810 0.7213 -0.0087 0.0554  0.1168  238 ARG A O   
1369 C CB  . ARG A 223 ? 0.5123 1.1320 0.8217 -0.0336 0.0385  0.1224  238 ARG A CB  
1370 C CG  . ARG A 223 ? 0.5229 1.1384 0.8399 -0.0439 0.0434  0.1343  238 ARG A CG  
1371 C CD  . ARG A 223 ? 0.5512 1.1375 0.8381 -0.0444 0.0393  0.1288  238 ARG A CD  
1372 N NE  . ARG A 223 ? 0.5843 1.1698 0.8652 -0.0452 0.0515  0.1417  238 ARG A NE  
1373 C CZ  . ARG A 223 ? 0.5819 1.1465 0.8501 -0.0504 0.0487  0.1433  238 ARG A CZ  
1374 N NH1 . ARG A 223 ? 0.5706 1.1137 0.8314 -0.0555 0.0346  0.1326  238 ARG A NH1 
1375 N NH2 . ARG A 223 ? 0.6285 1.1945 0.8911 -0.0499 0.0606  0.1563  238 ARG A NH2 
1376 N N   . LEU A 224 ? 0.5123 1.1058 0.7500 -0.0037 0.0400  0.1001  239 LEU A N   
1377 C CA  . LEU A 224 ? 0.5057 1.0763 0.7085 0.0033  0.0365  0.0901  239 LEU A CA  
1378 C C   . LEU A 224 ? 0.5533 1.1268 0.7350 0.0176  0.0487  0.0915  239 LEU A C   
1379 O O   . LEU A 224 ? 0.5968 1.1556 0.7534 0.0207  0.0517  0.0909  239 LEU A O   
1380 C CB  . LEU A 224 ? 0.4638 1.0258 0.6619 0.0049  0.0237  0.0780  239 LEU A CB  
1381 C CG  . LEU A 224 ? 0.4469 0.9849 0.6125 0.0094  0.0183  0.0681  239 LEU A CG  
1382 C CD1 . LEU A 224 ? 0.4371 0.9581 0.5965 -0.0007 0.0111  0.0659  239 LEU A CD1 
1383 C CD2 . LEU A 224 ? 0.4491 0.9840 0.6113 0.0142  0.0097  0.0591  239 LEU A CD2 
1384 N N   . LYS A 225 ? 0.5846 1.1770 0.7763 0.0271  0.0548  0.0929  240 LYS A N   
1385 C CA  . LYS A 225 ? 0.5908 1.1881 0.7637 0.0429  0.0670  0.0938  240 LYS A CA  
1386 C C   . LYS A 225 ? 0.5440 1.1444 0.7092 0.0431  0.0797  0.1044  240 LYS A C   
1387 O O   . LYS A 225 ? 0.5383 1.1286 0.6743 0.0535  0.0854  0.1022  240 LYS A O   
1388 C CB  . LYS A 225 ? 0.6562 1.2801 0.8502 0.0519  0.0741  0.0972  240 LYS A CB  
1389 C CG  . LYS A 225 ? 0.7169 1.3390 0.9159 0.0556  0.0628  0.0872  240 LYS A CG  
1390 C CD  . LYS A 225 ? 0.7918 1.4353 1.0002 0.0706  0.0708  0.0883  240 LYS A CD  
1391 C CE  . LYS A 225 ? 0.8389 1.5171 1.0864 0.0667  0.0798  0.1013  240 LYS A CE  
1392 N NZ  . LYS A 225 ? 0.8507 1.5485 1.1229 0.0721  0.0755  0.0995  240 LYS A NZ  
1393 N N   . GLU A 226 ? 0.5159 1.1301 0.7076 0.0316  0.0836  0.1163  241 GLU A N   
1394 C CA  . GLU A 226 ? 0.5153 1.1332 0.7026 0.0302  0.0957  0.1288  241 GLU A CA  
1395 C C   . GLU A 226 ? 0.5061 1.0959 0.6651 0.0272  0.0891  0.1238  241 GLU A C   
1396 O O   . GLU A 226 ? 0.5441 1.1262 0.6755 0.0362  0.0963  0.1249  241 GLU A O   
1397 C CB  . GLU A 226 ? 0.5048 1.1398 0.7287 0.0158  0.0985  0.1426  241 GLU A CB  
1398 C CG  . GLU A 226 ? 0.5003 1.1684 0.7558 0.0182  0.1080  0.1516  241 GLU A CG  
1399 C CD  . GLU A 226 ? 0.5071 1.1912 0.7981 0.0028  0.1115  0.1672  241 GLU A CD  
1400 O OE1 . GLU A 226 ? 0.4913 1.2057 0.8127 0.0028  0.1203  0.1772  241 GLU A OE1 
1401 O OE2 . GLU A 226 ? 0.5185 1.1846 0.8074 -0.0093 0.1053  0.1696  241 GLU A OE2 
1402 N N   . CYS A 227 ? 0.4568 1.0316 0.6219 0.0154  0.0753  0.1181  242 CYS A N   
1403 C CA  . CYS A 227 ? 0.4246 0.9741 0.5650 0.0128  0.0683  0.1128  242 CYS A CA  
1404 C C   . CYS A 227 ? 0.4085 0.9447 0.5157 0.0255  0.0669  0.1022  242 CYS A C   
1405 O O   . CYS A 227 ? 0.4064 0.9299 0.4888 0.0296  0.0689  0.1023  242 CYS A O   
1406 C CB  . CYS A 227 ? 0.4002 0.9372 0.5511 0.0011  0.0536  0.1060  242 CYS A CB  
1407 S SG  . CYS A 227 ? 0.4038 0.9490 0.5889 -0.0147 0.0528  0.1176  242 CYS A SG  
1408 N N   . VAL A 228 ? 0.3909 0.9296 0.4981 0.0317  0.0628  0.0933  243 VAL A N   
1409 C CA  . VAL A 228 ? 0.3978 0.9212 0.4756 0.0423  0.0591  0.0824  243 VAL A CA  
1410 C C   . VAL A 228 ? 0.4154 0.9420 0.4720 0.0555  0.0712  0.0859  243 VAL A C   
1411 O O   . VAL A 228 ? 0.4378 0.9472 0.4658 0.0608  0.0687  0.0806  243 VAL A O   
1412 C CB  . VAL A 228 ? 0.3881 0.9119 0.4716 0.0456  0.0514  0.0729  243 VAL A CB  
1413 C CG1 . VAL A 228 ? 0.4103 0.9244 0.4675 0.0600  0.0518  0.0644  243 VAL A CG1 
1414 C CG2 . VAL A 228 ? 0.3643 0.8735 0.4502 0.0350  0.0372  0.0659  243 VAL A CG2 
1415 N N   . SER A 229 ? 0.4263 0.9755 0.4971 0.0607  0.0843  0.0955  244 SER A N   
1416 C CA  . SER A 229 ? 0.4360 0.9905 0.4857 0.0752  0.0977  0.0994  244 SER A CA  
1417 C C   . SER A 229 ? 0.4379 0.9816 0.4658 0.0745  0.1017  0.1054  244 SER A C   
1418 O O   . SER A 229 ? 0.4462 0.9767 0.4417 0.0853  0.1023  0.0998  244 SER A O   
1419 C CB  . SER A 229 ? 0.4392 1.0239 0.5130 0.0794  0.1123  0.1108  244 SER A CB  
1420 O OG  . SER A 229 ? 0.4686 1.0585 0.5194 0.0957  0.1254  0.1132  244 SER A OG  
1421 N N   . ILE A 230 ? 0.4246 0.9732 0.4703 0.0620  0.1037  0.1167  245 ILE A N   
1422 C CA  . ILE A 230 ? 0.4304 0.9684 0.4580 0.0603  0.1064  0.1235  245 ILE A CA  
1423 C C   . ILE A 230 ? 0.4393 0.9509 0.4406 0.0606  0.0928  0.1110  245 ILE A C   
1424 O O   . ILE A 230 ? 0.4350 0.9351 0.4073 0.0677  0.0940  0.1105  245 ILE A O   
1425 C CB  . ILE A 230 ? 0.4183 0.9632 0.4736 0.0450  0.1080  0.1369  245 ILE A CB  
1426 C CG1 . ILE A 230 ? 0.4318 1.0036 0.5057 0.0471  0.1254  0.1530  245 ILE A CG1 
1427 C CG2 . ILE A 230 ? 0.4194 0.9456 0.4574 0.0405  0.1039  0.1400  245 ILE A CG2 
1428 C CD1 . ILE A 230 ? 0.4205 1.0035 0.5302 0.0311  0.1270  0.1665  245 ILE A CD1 
1429 N N   . ARG A 231 ? 0.4320 0.9349 0.4436 0.0532  0.0795  0.1009  246 ARG A N   
1430 C CA  . ARG A 231 ? 0.4237 0.9042 0.4149 0.0524  0.0664  0.0892  246 ARG A CA  
1431 C C   . ARG A 231 ? 0.4379 0.9099 0.4005 0.0664  0.0658  0.0796  246 ARG A C   
1432 O O   . ARG A 231 ? 0.4429 0.9008 0.3788 0.0712  0.0628  0.0763  246 ARG A O   
1433 C CB  . ARG A 231 ? 0.4065 0.8825 0.4156 0.0424  0.0544  0.0817  246 ARG A CB  
1434 C CG  . ARG A 231 ? 0.4027 0.8585 0.3945 0.0408  0.0414  0.0705  246 ARG A CG  
1435 C CD  . ARG A 231 ? 0.3881 0.8413 0.3905 0.0368  0.0320  0.0615  246 ARG A CD  
1436 N NE  . ARG A 231 ? 0.3943 0.8505 0.3914 0.0464  0.0334  0.0558  246 ARG A NE  
1437 C CZ  . ARG A 231 ? 0.3894 0.8402 0.3890 0.0457  0.0249  0.0474  246 ARG A CZ  
1438 N NH1 . ARG A 231 ? 0.3695 0.8127 0.3756 0.0360  0.0152  0.0438  246 ARG A NH1 
1439 N NH2 . ARG A 231 ? 0.3949 0.8470 0.3890 0.0554  0.0262  0.0428  246 ARG A NH2 
1440 N N   . ASP A 232 ? 0.4375 0.9176 0.4056 0.0734  0.0681  0.0750  247 ASP A N   
1441 C CA  . ASP A 232 ? 0.4664 0.9360 0.4074 0.0872  0.0667  0.0651  247 ASP A CA  
1442 C C   . ASP A 232 ? 0.4933 0.9624 0.4079 0.0990  0.0764  0.0692  247 ASP A C   
1443 O O   . ASP A 232 ? 0.4988 0.9508 0.3839 0.1071  0.0709  0.0604  247 ASP A O   
1444 C CB  . ASP A 232 ? 0.4758 0.9556 0.4278 0.0946  0.0691  0.0608  247 ASP A CB  
1445 C CG  . ASP A 232 ? 0.4824 0.9556 0.4496 0.0859  0.0562  0.0532  247 ASP A CG  
1446 O OD1 . ASP A 232 ? 0.4896 0.9499 0.4562 0.0750  0.0461  0.0506  247 ASP A OD1 
1447 O OD2 . ASP A 232 ? 0.4864 0.9678 0.4660 0.0904  0.0564  0.0503  247 ASP A OD2 
1448 N N   . GLN A 233 ? 0.5007 0.9878 0.4249 0.0996  0.0903  0.0829  248 GLN A N   
1449 C CA  . GLN A 233 ? 0.5363 1.0245 0.4335 0.1127  0.1011  0.0875  248 GLN A CA  
1450 C C   . GLN A 233 ? 0.5377 1.0084 0.4127 0.1095  0.0946  0.0879  248 GLN A C   
1451 O O   . GLN A 233 ? 0.5523 1.0079 0.3951 0.1194  0.0903  0.0800  248 GLN A O   
1452 C CB  . GLN A 233 ? 0.5528 1.0673 0.4675 0.1144  0.1193  0.1039  248 GLN A CB  
1453 C CG  . GLN A 233 ? 0.5557 1.0916 0.4907 0.1210  0.1280  0.1046  248 GLN A CG  
1454 C CD  . GLN A 233 ? 0.5627 1.1266 0.5279 0.1154  0.1429  0.1225  248 GLN A CD  
1455 O OE1 . GLN A 233 ? 0.6128 1.1846 0.5680 0.1196  0.1555  0.1344  248 GLN A OE1 
1456 N NE2 . GLN A 233 ? 0.5454 1.1241 0.5475 0.1054  0.1410  0.1251  248 GLN A NE2 
1457 N N   . LEU A 234 ? 0.5338 1.0062 0.4268 0.0957  0.0928  0.0967  249 LEU A N   
1458 C CA  . LEU A 234 ? 0.5474 1.0040 0.4243 0.0913  0.0853  0.0976  249 LEU A CA  
1459 C C   . LEU A 234 ? 0.5425 0.9771 0.3972 0.0931  0.0695  0.0825  249 LEU A C   
1460 O O   . LEU A 234 ? 0.5401 0.9629 0.3691 0.0979  0.0658  0.0814  249 LEU A O   
1461 C CB  . LEU A 234 ? 0.5360 0.9949 0.4408 0.0751  0.0819  0.1055  249 LEU A CB  
1462 C CG  . LEU A 234 ? 0.5563 1.0025 0.4484 0.0711  0.0770  0.1101  249 LEU A CG  
1463 C CD1 . LEU A 234 ? 0.5602 1.0152 0.4761 0.0608  0.0836  0.1255  249 LEU A CD1 
1464 C CD2 . LEU A 234 ? 0.5500 0.9792 0.4387 0.0651  0.0601  0.0982  249 LEU A CD2 
1465 N N   . LEU A 235 ? 0.5387 0.9681 0.4041 0.0888  0.0597  0.0717  250 LEU A N   
1466 C CA  . LEU A 235 ? 0.5492 0.9589 0.3962 0.0896  0.0449  0.0583  250 LEU A CA  
1467 C C   . LEU A 235 ? 0.5788 0.9800 0.3958 0.1048  0.0454  0.0501  250 LEU A C   
1468 O O   . LEU A 235 ? 0.6085 0.9938 0.3996 0.1088  0.0368  0.0438  250 LEU A O   
1469 C CB  . LEU A 235 ? 0.5388 0.9452 0.4049 0.0807  0.0351  0.0503  250 LEU A CB  
1470 C CG  . LEU A 235 ? 0.5334 0.9374 0.4173 0.0664  0.0271  0.0521  250 LEU A CG  
1471 C CD1 . LEU A 235 ? 0.5405 0.9559 0.4391 0.0612  0.0359  0.0655  250 LEU A CD1 
1472 C CD2 . LEU A 235 ? 0.5066 0.9117 0.4112 0.0587  0.0207  0.0465  250 LEU A CD2 
1473 N N   . TYR A 236 ? 0.5758 0.9871 0.3961 0.1138  0.0545  0.0495  251 TYR A N   
1474 C CA  . TYR A 236 ? 0.6077 1.0106 0.3987 0.1305  0.0559  0.0409  251 TYR A CA  
1475 C C   . TYR A 236 ? 0.6417 1.0400 0.4026 0.1395  0.0602  0.0447  251 TYR A C   
1476 O O   . TYR A 236 ? 0.6660 1.0464 0.3957 0.1487  0.0522  0.0345  251 TYR A O   
1477 C CB  . TYR A 236 ? 0.6076 1.0273 0.4086 0.1405  0.0688  0.0431  251 TYR A CB  
1478 C CG  . TYR A 236 ? 0.6463 1.0550 0.4175 0.1588  0.0689  0.0321  251 TYR A CG  
1479 C CD1 . TYR A 236 ? 0.6598 1.0466 0.4193 0.1600  0.0539  0.0174  251 TYR A CD1 
1480 C CD2 . TYR A 236 ? 0.6924 1.1119 0.4462 0.1753  0.0840  0.0366  251 TYR A CD2 
1481 C CE1 . TYR A 236 ? 0.7075 1.0810 0.4388 0.1771  0.0526  0.0063  251 TYR A CE1 
1482 C CE2 . TYR A 236 ? 0.7273 1.1351 0.4513 0.1938  0.0838  0.0253  251 TYR A CE2 
1483 C CZ  . TYR A 236 ? 0.7488 1.1322 0.4612 0.1947  0.0674  0.0096  251 TYR A CZ  
1484 O OH  . TYR A 236 ? 0.8002 1.1687 0.4819 0.2133  0.0657  -0.0026 251 TYR A OH  
1485 N N   . LYS A 237 ? 0.6460 1.0594 0.4162 0.1364  0.0719  0.0596  252 LYS A N   
1486 C CA  . LYS A 237 ? 0.6877 1.0982 0.4303 0.1443  0.0769  0.0657  252 LYS A CA  
1487 C C   . LYS A 237 ? 0.6766 1.0660 0.4019 0.1396  0.0599  0.0583  252 LYS A C   
1488 O O   . LYS A 237 ? 0.7190 1.0935 0.4113 0.1500  0.0536  0.0499  252 LYS A O   
1489 C CB  . LYS A 237 ? 0.7056 1.1343 0.4662 0.1381  0.0905  0.0845  252 LYS A CB  
1490 C CG  . LYS A 237 ? 0.7486 1.1709 0.4833 0.1422  0.0922  0.0921  252 LYS A CG  
1491 C CD  . LYS A 237 ? 0.7649 1.2055 0.5173 0.1372  0.1076  0.1122  252 LYS A CD  
1492 C CE  . LYS A 237 ? 0.7883 1.2205 0.5195 0.1380  0.1068  0.1211  252 LYS A CE  
1493 N NZ  . LYS A 237 ? 0.7802 1.2215 0.5405 0.1238  0.1120  0.1374  252 LYS A NZ  
1494 N N   . LYS A 238 ? 0.6365 1.0248 0.3847 0.1240  0.0519  0.0608  253 LYS A N   
1495 C CA  . LYS A 238 ? 0.6251 0.9961 0.3627 0.1185  0.0351  0.0532  253 LYS A CA  
1496 C C   . LYS A 238 ? 0.6395 0.9933 0.3574 0.1247  0.0226  0.0365  253 LYS A C   
1497 O O   . LYS A 238 ? 0.6564 0.9954 0.3480 0.1296  0.0125  0.0299  253 LYS A O   
1498 C CB  . LYS A 238 ? 0.5817 0.9557 0.3507 0.1018  0.0288  0.0561  253 LYS A CB  
1499 C CG  . LYS A 238 ? 0.5870 0.9520 0.3495 0.0964  0.0187  0.0576  253 LYS A CG  
1500 C CD  . LYS A 238 ? 0.5981 0.9675 0.3509 0.0997  0.0272  0.0713  253 LYS A CD  
1501 C CE  . LYS A 238 ? 0.6140 0.9695 0.3367 0.1056  0.0166  0.0678  253 LYS A CE  
1502 N NZ  . LYS A 238 ? 0.6073 0.9620 0.3354 0.0995  0.0132  0.0772  253 LYS A NZ  
1503 N N   . LEU A 239 ? 0.6425 0.9976 0.3726 0.1249  0.0228  0.0299  254 LEU A N   
1504 C CA  . LEU A 239 ? 0.6507 0.9877 0.3637 0.1303  0.0108  0.0147  254 LEU A CA  
1505 C C   . LEU A 239 ? 0.6868 1.0131 0.3610 0.1479  0.0119  0.0086  254 LEU A C   
1506 O O   . LEU A 239 ? 0.6972 1.0035 0.3486 0.1506  -0.0025 -0.0023 254 LEU A O   
1507 C CB  . LEU A 239 ? 0.6286 0.9704 0.3623 0.1287  0.0129  0.0109  254 LEU A CB  
1508 C CG  . LEU A 239 ? 0.6394 0.9652 0.3607 0.1359  0.0047  -0.0028 254 LEU A CG  
1509 C CD1 . LEU A 239 ? 0.6627 0.9642 0.3606 0.1358  -0.0127 -0.0144 254 LEU A CD1 
1510 C CD2 . LEU A 239 ? 0.6119 0.9422 0.3628 0.1258  0.0020  -0.0036 254 LEU A CD2 
1511 N N   . LEU A 240 ? 0.7046 1.0442 0.3712 0.1600  0.0288  0.0158  255 LEU A N   
1512 C CA  . LEU A 240 ? 0.7493 1.0803 0.3758 0.1789  0.0321  0.0110  255 LEU A CA  
1513 C C   . LEU A 240 ? 0.7649 1.0850 0.3655 0.1799  0.0242  0.0119  255 LEU A C   
1514 O O   . LEU A 240 ? 0.7971 1.0977 0.3651 0.1892  0.0132  0.0002  255 LEU A O   
1515 C CB  . LEU A 240 ? 0.7551 1.1074 0.3817 0.1907  0.0542  0.0218  255 LEU A CB  
1516 C CG  . LEU A 240 ? 0.7656 1.1217 0.3909 0.2038  0.0617  0.0151  255 LEU A CG  
1517 C CD1 . LEU A 240 ? 0.7516 1.0921 0.3873 0.1981  0.0466  0.0014  255 LEU A CD1 
1518 C CD2 . LEU A 240 ? 0.7471 1.1332 0.4015 0.2033  0.0818  0.0298  255 LEU A CD2 
1519 N N   . GLU A 241 ? 0.7451 1.0772 0.3607 0.1705  0.0293  0.0257  256 GLU A N   
1520 C CA  . GLU A 241 ? 0.7646 1.0884 0.3620 0.1692  0.0211  0.0285  256 GLU A CA  
1521 C C   . GLU A 241 ? 0.7734 1.0770 0.3647 0.1623  -0.0018 0.0151  256 GLU A C   
1522 O O   . GLU A 241 ? 0.8390 1.1295 0.4023 0.1677  -0.0122 0.0106  256 GLU A O   
1523 C CB  . GLU A 241 ? 0.7364 1.0754 0.3597 0.1572  0.0286  0.0452  256 GLU A CB  
1524 C CG  . GLU A 241 ? 0.7385 1.0969 0.3654 0.1633  0.0505  0.0607  256 GLU A CG  
1525 C CD  . GLU A 241 ? 0.7260 1.0957 0.3761 0.1514  0.0567  0.0774  256 GLU A CD  
1526 O OE1 . GLU A 241 ? 0.6851 1.0551 0.3645 0.1362  0.0488  0.0774  256 GLU A OE1 
1527 O OE2 . GLU A 241 ? 0.7509 1.1290 0.3892 0.1579  0.0697  0.0909  256 GLU A OE2 
1528 N N   . HIS A 242 ? 0.7392 1.0411 0.3570 0.1504  -0.0095 0.0092  257 HIS A N   
1529 C CA  . HIS A 242 ? 0.7324 1.0179 0.3503 0.1419  -0.0302 -0.0020 257 HIS A CA  
1530 C C   . HIS A 242 ? 0.7850 1.0500 0.3768 0.1515  -0.0410 -0.0180 257 HIS A C   
1531 O O   . HIS A 242 ? 0.8037 1.0525 0.3783 0.1509  -0.0577 -0.0266 257 HIS A O   
1532 C CB  . HIS A 242 ? 0.6767 0.9692 0.3335 0.1252  -0.0333 -0.0007 257 HIS A CB  
1533 C CG  . HIS A 242 ? 0.6274 0.9308 0.3058 0.1133  -0.0330 0.0098  257 HIS A CG  
1534 N ND1 . HIS A 242 ? 0.6120 0.9310 0.3013 0.1131  -0.0182 0.0236  257 HIS A ND1 
1535 C CD2 . HIS A 242 ? 0.6022 0.9025 0.2920 0.1022  -0.0459 0.0087  257 HIS A CD2 
1536 C CE1 . HIS A 242 ? 0.5857 0.9086 0.2910 0.1028  -0.0226 0.0299  257 HIS A CE1 
1537 N NE2 . HIS A 242 ? 0.5821 0.8950 0.2883 0.0966  -0.0388 0.0209  257 HIS A NE2 
1538 N N   . LYS A 243 ? 0.8332 1.0985 0.4231 0.1602  -0.0325 -0.0221 258 LYS A N   
1539 C CA  . LYS A 243 ? 0.8959 1.1390 0.4617 0.1696  -0.0435 -0.0380 258 LYS A CA  
1540 C C   . LYS A 243 ? 0.9850 1.2134 0.5074 0.1846  -0.0490 -0.0446 258 LYS A C   
1541 O O   . LYS A 243 ? 1.0001 1.2051 0.5020 0.1872  -0.0664 -0.0587 258 LYS A O   
1542 C CB  . LYS A 243 ? 0.8960 1.1433 0.4662 0.1790  -0.0318 -0.0404 258 LYS A CB  
1543 C CG  . LYS A 243 ? 0.9133 1.1368 0.4738 0.1817  -0.0462 -0.0562 258 LYS A CG  
1544 C CD  . LYS A 243 ? 0.9354 1.1564 0.4806 0.2001  -0.0361 -0.0619 258 LYS A CD  
1545 C CE  . LYS A 243 ? 0.9184 1.1661 0.4928 0.1999  -0.0165 -0.0504 258 LYS A CE  
1546 N NZ  . LYS A 243 ? 0.9401 1.1913 0.4979 0.2209  -0.0033 -0.0536 258 LYS A NZ  
1547 N N   . LYS A 244 ? 1.0602 1.3020 0.5690 0.1940  -0.0344 -0.0341 259 LYS A N   
1548 C CA  . LYS A 244 ? 1.1493 1.3800 0.6146 0.2094  -0.0373 -0.0379 259 LYS A CA  
1549 C C   . LYS A 244 ? 1.1648 1.3823 0.6198 0.2017  -0.0576 -0.0417 259 LYS A C   
1550 O O   . LYS A 244 ? 1.1779 1.3747 0.5991 0.2109  -0.0716 -0.0542 259 LYS A O   
1551 C CB  . LYS A 244 ? 1.1747 1.4252 0.6303 0.2204  -0.0149 -0.0229 259 LYS A CB  
1552 C CG  . LYS A 244 ? 1.1612 1.4314 0.6423 0.2077  -0.0067 -0.0047 259 LYS A CG  
1553 C CD  . LYS A 244 ? 1.2067 1.4849 0.6614 0.2198  0.0061  0.0072  259 LYS A CD  
1554 C CE  . LYS A 244 ? 1.1709 1.4683 0.6528 0.2078  0.0166  0.0269  259 LYS A CE  
1555 N NZ  . LYS A 244 ? 1.1571 1.4475 0.6437 0.1963  0.0010  0.0288  259 LYS A NZ  
1556 N N   . SER A 245 ? 1.1690 1.3986 0.6533 0.1854  -0.0594 -0.0315 260 SER A N   
1557 C CA  . SER A 245 ? 1.2022 1.4233 0.6846 0.1765  -0.0785 -0.0340 260 SER A CA  
1558 C C   . SER A 245 ? 1.2020 1.4187 0.7153 0.1594  -0.0923 -0.0403 260 SER A C   
1559 O O   . SER A 245 ? 1.2088 1.4409 0.7579 0.1463  -0.0860 -0.0314 260 SER A O   
1560 C CB  . SER A 245 ? 1.2002 1.4379 0.6940 0.1712  -0.0711 -0.0177 260 SER A CB  
1561 O OG  . SER A 245 ? 1.3198 1.5557 0.7776 0.1863  -0.0658 -0.0135 260 SER A OG  
1562 N N   . LEU A 246 ? 1.2175 1.4129 0.7167 0.1595  -0.1112 -0.0553 261 LEU A N   
1563 C CA  . LEU A 246 ? 1.1846 1.3747 0.7118 0.1441  -0.1231 -0.0611 261 LEU A CA  
1564 C C   . LEU A 246 ? 1.2116 1.3817 0.7280 0.1389  -0.1482 -0.0733 261 LEU A C   
1565 O O   . LEU A 246 ? 1.2913 1.4395 0.7797 0.1483  -0.1582 -0.0864 261 LEU A O   
1566 C CB  . LEU A 246 ? 1.1759 1.3605 0.7068 0.1484  -0.1157 -0.0667 261 LEU A CB  
1567 C CG  . LEU A 246 ? 1.1003 1.2852 0.6653 0.1322  -0.1216 -0.0679 261 LEU A CG  
1568 C CD1 . LEU A 246 ? 1.0490 1.2579 0.6497 0.1188  -0.1122 -0.0540 261 LEU A CD1 
1569 C CD2 . LEU A 246 ? 1.0980 1.2767 0.6632 0.1389  -0.1141 -0.0731 261 LEU A CD2 
1570 N N   . THR A 247 ? 1.1912 1.3690 0.7313 0.1238  -0.1587 -0.0690 262 THR A N   
1571 C CA  . THR A 247 ? 1.1731 1.3364 0.7105 0.1159  -0.1831 -0.0785 262 THR A CA  
1572 C C   . THR A 247 ? 1.1218 1.2876 0.6959 0.0980  -0.1891 -0.0787 262 THR A C   
1573 O O   . THR A 247 ? 1.0722 1.2574 0.6781 0.0863  -0.1839 -0.0686 262 THR A O   
1574 C CB  . THR A 247 ? 1.1687 1.3411 0.7042 0.1138  -0.1911 -0.0728 262 THR A CB  
1575 O OG1 . THR A 247 ? 1.1782 1.3487 0.6787 0.1309  -0.1836 -0.0709 262 THR A OG1 
1576 C CG2 . THR A 247 ? 1.1756 1.3347 0.7089 0.1059  -0.2176 -0.0825 262 THR A CG2 
1577 N N   . PRO A 248 ? 1.1461 1.2914 0.7148 0.0967  -0.1994 -0.0900 263 PRO A N   
1578 C CA  . PRO A 248 ? 1.1631 1.3075 0.7628 0.0805  -0.2055 -0.0902 263 PRO A CA  
1579 C C   . PRO A 248 ? 1.2078 1.3609 0.8344 0.0629  -0.2199 -0.0869 263 PRO A C   
1580 O O   . PRO A 248 ? 1.1648 1.3320 0.8245 0.0500  -0.2148 -0.0794 263 PRO A O   
1581 C CB  . PRO A 248 ? 1.1642 1.2789 0.7421 0.0859  -0.2174 -0.1045 263 PRO A CB  
1582 C CG  . PRO A 248 ? 1.1811 1.2893 0.7252 0.1067  -0.2056 -0.1083 263 PRO A CG  
1583 C CD  . PRO A 248 ? 1.1905 1.3135 0.7226 0.1133  -0.2002 -0.1016 263 PRO A CD  
1584 N N   . GLY A 249 ? 1.3334 1.4783 0.9459 0.0628  -0.2380 -0.0925 264 GLY A N   
1585 C CA  . GLY A 249 ? 1.3891 1.5453 1.0283 0.0471  -0.2519 -0.0888 264 GLY A CA  
1586 C C   . GLY A 249 ? 1.4048 1.5901 1.0749 0.0407  -0.2357 -0.0745 264 GLY A C   
1587 O O   . GLY A 249 ? 1.3936 1.5889 1.0946 0.0280  -0.2323 -0.0695 264 GLY A O   
1588 N N   . GLU A 250 ? 1.4882 1.6855 1.1484 0.0500  -0.2261 -0.0681 265 GLU A N   
1589 C CA  . GLU A 250 ? 1.5114 1.7312 1.1917 0.0493  -0.2061 -0.0554 265 GLU A CA  
1590 C C   . GLU A 250 ? 1.4838 1.7040 1.1364 0.0653  -0.1945 -0.0520 265 GLU A C   
1591 O O   . GLU A 250 ? 1.5272 1.7327 1.1477 0.0756  -0.2036 -0.0592 265 GLU A O   
1592 C CB  . GLU A 250 ? 1.5779 1.8183 1.2888 0.0379  -0.2100 -0.0472 265 GLU A CB  
1593 C CG  . GLU A 250 ? 1.6204 1.8602 1.3504 0.0241  -0.2289 -0.0512 265 GLU A CG  
1594 C CD  . GLU A 250 ? 1.6132 1.8775 1.3801 0.0128  -0.2259 -0.0416 265 GLU A CD  
1595 O OE1 . GLU A 250 ? 1.5590 1.8344 1.3449 0.0093  -0.2105 -0.0352 265 GLU A OE1 
1596 O OE2 . GLU A 250 ? 1.6937 1.9665 1.4704 0.0081  -0.2394 -0.0408 265 GLU A OE2 
1597 N N   . PRO A 251 ? 1.3752 1.6115 1.0388 0.0676  -0.1755 -0.0411 266 PRO A N   
1598 C CA  . PRO A 251 ? 1.2481 1.5037 0.9482 0.0563  -0.1674 -0.0318 266 PRO A CA  
1599 C C   . PRO A 251 ? 1.0707 1.3311 0.7809 0.0570  -0.1489 -0.0279 266 PRO A C   
1600 O O   . PRO A 251 ? 1.0245 1.2785 0.7432 0.0515  -0.1513 -0.0332 266 PRO A O   
1601 C CB  . PRO A 251 ? 1.3019 1.5697 1.0027 0.0589  -0.1669 -0.0231 266 PRO A CB  
1602 C CG  . PRO A 251 ? 1.3556 1.6108 1.0180 0.0728  -0.1713 -0.0266 266 PRO A CG  
1603 C CD  . PRO A 251 ? 1.4017 1.6403 1.0418 0.0802  -0.1689 -0.0357 266 PRO A CD  
1604 N N   . ARG A 252 ? 0.9521 1.2232 0.6640 0.0624  -0.1320 -0.0189 267 ARG A N   
1605 C CA  . ARG A 252 ? 0.8944 1.1795 0.6154 0.0624  -0.1256 -0.0080 267 ARG A CA  
1606 C C   . ARG A 252 ? 0.7784 1.0763 0.5220 0.0587  -0.1089 0.0004  267 ARG A C   
1607 O O   . ARG A 252 ? 0.7431 1.0500 0.4919 0.0603  -0.1002 0.0099  267 ARG A O   
1608 C CB  . ARG A 252 ? 0.9683 1.2491 0.6593 0.0756  -0.1218 -0.0046 267 ARG A CB  
1609 C CG  . ARG A 252 ? 0.9954 1.2738 0.6694 0.0862  -0.1060 -0.0027 267 ARG A CG  
1610 C CD  . ARG A 252 ? 1.0386 1.2998 0.6797 0.0967  -0.1130 -0.0137 267 ARG A CD  
1611 N NE  . ARG A 252 ? 1.0635 1.3239 0.6885 0.1083  -0.0974 -0.0125 267 ARG A NE  
1612 C CZ  . ARG A 252 ? 1.0746 1.3372 0.6769 0.1204  -0.0871 -0.0060 267 ARG A CZ  
1613 N NH1 . ARG A 252 ? 1.0783 1.3421 0.6689 0.1229  -0.0913 -0.0001 267 ARG A NH1 
1614 N NH2 . ARG A 252 ? 1.0808 1.3452 0.6721 0.1305  -0.0722 -0.0048 267 ARG A NH2 
1615 N N   . ASP A 253 ? 0.7155 1.0130 0.4719 0.0538  -0.1054 -0.0031 268 ASP A N   
1616 C CA  . ASP A 253 ? 0.6676 0.9743 0.4390 0.0530  -0.0899 0.0029  268 ASP A CA  
1617 C C   . ASP A 253 ? 0.6452 0.9497 0.4300 0.0468  -0.0908 -0.0025 268 ASP A C   
1618 O O   . ASP A 253 ? 0.6477 0.9393 0.4209 0.0477  -0.0999 -0.0112 268 ASP A O   
1619 C CB  . ASP A 253 ? 0.6763 0.9809 0.4278 0.0649  -0.0778 0.0053  268 ASP A CB  
1620 C CG  . ASP A 253 ? 0.6703 0.9856 0.4265 0.0670  -0.0661 0.0170  268 ASP A CG  
1621 O OD1 . ASP A 253 ? 0.6941 1.0187 0.4740 0.0585  -0.0646 0.0226  268 ASP A OD1 
1622 O OD2 . ASP A 253 ? 0.6736 0.9876 0.4097 0.0772  -0.0583 0.0207  268 ASP A OD2 
1623 N N   . LEU A 254 ? 0.6020 0.9174 0.4093 0.0413  -0.0814 0.0027  269 LEU A N   
1624 C CA  . LEU A 254 ? 0.5934 0.9074 0.4123 0.0367  -0.0807 -0.0011 269 LEU A CA  
1625 C C   . LEU A 254 ? 0.5749 0.8800 0.3762 0.0463  -0.0761 -0.0056 269 LEU A C   
1626 O O   . LEU A 254 ? 0.5580 0.8529 0.3560 0.0459  -0.0815 -0.0125 269 LEU A O   
1627 C CB  . LEU A 254 ? 0.6069 0.9344 0.4504 0.0308  -0.0712 0.0055  269 LEU A CB  
1628 C CG  . LEU A 254 ? 0.6389 0.9665 0.4976 0.0236  -0.0731 0.0023  269 LEU A CG  
1629 C CD1 . LEU A 254 ? 0.6510 0.9911 0.5328 0.0156  -0.0701 0.0075  269 LEU A CD1 
1630 C CD2 . LEU A 254 ? 0.6416 0.9668 0.4979 0.0286  -0.0660 0.0005  269 LEU A CD2 
1631 N N   . LEU A 255 ? 0.5783 0.8874 0.3681 0.0556  -0.0657 -0.0010 270 LEU A N   
1632 C CA  . LEU A 255 ? 0.5989 0.9028 0.3720 0.0669  -0.0588 -0.0042 270 LEU A CA  
1633 C C   . LEU A 255 ? 0.6396 0.9247 0.3842 0.0744  -0.0701 -0.0146 270 LEU A C   
1634 O O   . LEU A 255 ? 0.6631 0.9374 0.3996 0.0789  -0.0724 -0.0222 270 LEU A O   
1635 C CB  . LEU A 255 ? 0.5956 0.9108 0.3649 0.0743  -0.0442 0.0051  270 LEU A CB  
1636 C CG  . LEU A 255 ? 0.6145 0.9338 0.3777 0.0846  -0.0317 0.0059  270 LEU A CG  
1637 C CD1 . LEU A 255 ? 0.5966 0.9221 0.3831 0.0792  -0.0284 0.0053  270 LEU A CD1 
1638 C CD2 . LEU A 255 ? 0.6267 0.9593 0.3895 0.0891  -0.0177 0.0177  270 LEU A CD2 
1639 N N   . ASP A 256 ? 0.6439 0.9240 0.3735 0.0758  -0.0783 -0.0153 271 ASP A N   
1640 C CA  . ASP A 256 ? 0.6783 0.9396 0.3844 0.0797  -0.0930 -0.0261 271 ASP A CA  
1641 C C   . ASP A 256 ? 0.6438 0.8949 0.3612 0.0705  -0.1048 -0.0336 271 ASP A C   
1642 O O   . ASP A 256 ? 0.6671 0.9020 0.3689 0.0764  -0.1099 -0.0425 271 ASP A O   
1643 C CB  . ASP A 256 ? 0.7221 0.9824 0.4191 0.0783  -0.1031 -0.0250 271 ASP A CB  
1644 C CG  . ASP A 256 ? 0.7690 1.0267 0.4364 0.0923  -0.0982 -0.0233 271 ASP A CG  
1645 O OD1 . ASP A 256 ? 0.7972 1.0663 0.4652 0.0980  -0.0821 -0.0145 271 ASP A OD1 
1646 O OD2 . ASP A 256 ? 0.8670 1.1111 0.5095 0.0979  -0.1106 -0.0307 271 ASP A OD2 
1647 N N   . ALA A 257 ? 0.5950 0.8552 0.3386 0.0568  -0.1089 -0.0295 272 ALA A N   
1648 C CA  . ALA A 257 ? 0.5791 0.8323 0.3372 0.0458  -0.1196 -0.0340 272 ALA A CA  
1649 C C   . ALA A 257 ? 0.5734 0.8191 0.3336 0.0476  -0.1155 -0.0375 272 ALA A C   
1650 O O   . ALA A 257 ? 0.5746 0.8044 0.3309 0.0445  -0.1265 -0.0445 272 ALA A O   
1651 C CB  . ALA A 257 ? 0.5404 0.8097 0.3277 0.0326  -0.1197 -0.0268 272 ALA A CB  
1652 N N   . LEU A 258 ? 0.5675 0.8248 0.3353 0.0522  -0.1003 -0.0322 273 LEU A N   
1653 C CA  . LEU A 258 ? 0.5864 0.8381 0.3548 0.0566  -0.0955 -0.0352 273 LEU A CA  
1654 C C   . LEU A 258 ? 0.6339 0.8684 0.3730 0.0710  -0.0975 -0.0440 273 LEU A C   
1655 O O   . LEU A 258 ? 0.6584 0.8768 0.3911 0.0732  -0.1037 -0.0512 273 LEU A O   
1656 C CB  . LEU A 258 ? 0.5737 0.8442 0.3580 0.0586  -0.0792 -0.0271 273 LEU A CB  
1657 C CG  . LEU A 258 ? 0.5355 0.8224 0.3485 0.0465  -0.0754 -0.0193 273 LEU A CG  
1658 C CD1 . LEU A 258 ? 0.5160 0.8201 0.3410 0.0497  -0.0605 -0.0117 273 LEU A CD1 
1659 C CD2 . LEU A 258 ? 0.5334 0.8149 0.3592 0.0386  -0.0813 -0.0216 273 LEU A CD2 
1660 N N   . LEU A 259 ? 0.6549 0.8921 0.3750 0.0816  -0.0920 -0.0432 274 LEU A N   
1661 C CA  . LEU A 259 ? 0.6863 0.9088 0.3759 0.0977  -0.0918 -0.0514 274 LEU A CA  
1662 C C   . LEU A 259 ? 0.7189 0.9157 0.3890 0.0978  -0.1104 -0.0633 274 LEU A C   
1663 O O   . LEU A 259 ? 0.7553 0.9345 0.4094 0.1069  -0.1138 -0.0723 274 LEU A O   
1664 C CB  . LEU A 259 ? 0.6992 0.9304 0.3710 0.1087  -0.0821 -0.0471 274 LEU A CB  
1665 C CG  . LEU A 259 ? 0.6767 0.9305 0.3637 0.1121  -0.0624 -0.0362 274 LEU A CG  
1666 C CD1 . LEU A 259 ? 0.6854 0.9483 0.3583 0.1187  -0.0544 -0.0291 274 LEU A CD1 
1667 C CD2 . LEU A 259 ? 0.6866 0.9389 0.3682 0.1241  -0.0536 -0.0399 274 LEU A CD2 
1668 N N   . ILE A 260 ? 0.7134 0.9079 0.3856 0.0879  -0.1229 -0.0634 275 ILE A N   
1669 C CA  . ILE A 260 ? 0.7371 0.9090 0.3999 0.0827  -0.1431 -0.0734 275 ILE A CA  
1670 C C   . ILE A 260 ? 0.7256 0.8873 0.4027 0.0759  -0.1471 -0.0762 275 ILE A C   
1671 O O   . ILE A 260 ? 0.7459 0.8840 0.4059 0.0815  -0.1563 -0.0862 275 ILE A O   
1672 C CB  . ILE A 260 ? 0.7307 0.9088 0.4081 0.0682  -0.1550 -0.0700 275 ILE A CB  
1673 C CG1 . ILE A 260 ? 0.7426 0.9334 0.4112 0.0728  -0.1513 -0.0649 275 ILE A CG1 
1674 C CG2 . ILE A 260 ? 0.7502 0.9053 0.4191 0.0622  -0.1765 -0.0801 275 ILE A CG2 
1675 C CD1 . ILE A 260 ? 0.7776 0.9588 0.4101 0.0906  -0.1484 -0.0701 275 ILE A CD1 
1676 N N   . GLY A 261 ? 0.6943 0.8725 0.4017 0.0642  -0.1407 -0.0673 276 GLY A N   
1677 C CA  . GLY A 261 ? 0.7109 0.8804 0.4325 0.0565  -0.1450 -0.0682 276 GLY A CA  
1678 C C   . GLY A 261 ? 0.7409 0.8980 0.4487 0.0700  -0.1395 -0.0738 276 GLY A C   
1679 O O   . GLY A 261 ? 0.7502 0.8868 0.4543 0.0690  -0.1488 -0.0798 276 GLY A O   
1680 N N   . GLN A 262 ? 0.7542 0.9244 0.4552 0.0828  -0.1242 -0.0712 277 GLN A N   
1681 C CA  . GLN A 262 ? 0.7910 0.9550 0.4807 0.0975  -0.1164 -0.0754 277 GLN A CA  
1682 C C   . GLN A 262 ? 0.8568 0.9967 0.5108 0.1123  -0.1243 -0.0878 277 GLN A C   
1683 O O   . GLN A 262 ? 0.8834 1.0060 0.5245 0.1228  -0.1262 -0.0955 277 GLN A O   
1684 C CB  . GLN A 262 ? 0.7611 0.9521 0.4617 0.1038  -0.0966 -0.0662 277 GLN A CB  
1685 C CG  . GLN A 262 ? 0.7589 0.9509 0.4567 0.1175  -0.0864 -0.0679 277 GLN A CG  
1686 C CD  . GLN A 262 ? 0.7843 0.9711 0.4529 0.1369  -0.0805 -0.0737 277 GLN A CD  
1687 O OE1 . GLN A 262 ? 0.8197 1.0072 0.4717 0.1400  -0.0808 -0.0740 277 GLN A OE1 
1688 N NE2 . GLN A 262 ? 0.7970 0.9789 0.4581 0.1511  -0.0749 -0.0783 277 GLN A NE2 
1689 N N   . GLN A 263 ? 0.9006 1.0384 0.5377 0.1139  -0.1296 -0.0900 278 GLN A N   
1690 C CA  . GLN A 263 ? 0.9978 1.1087 0.6005 0.1244  -0.1427 -0.1032 278 GLN A CA  
1691 C C   . GLN A 263 ? 1.0207 1.1028 0.6209 0.1195  -0.1598 -0.1127 278 GLN A C   
1692 O O   . GLN A 263 ? 1.0658 1.1254 0.6422 0.1333  -0.1638 -0.1234 278 GLN A O   
1693 C CB  . GLN A 263 ? 1.0415 1.1522 0.6349 0.1188  -0.1531 -0.1036 278 GLN A CB  
1694 C CG  . GLN A 263 ? 1.1006 1.2123 0.6627 0.1352  -0.1479 -0.1063 278 GLN A CG  
1695 C CD  . GLN A 263 ? 1.1582 1.2556 0.7022 0.1318  -0.1668 -0.1130 278 GLN A CD  
1696 O OE1 . GLN A 263 ? 1.2024 1.2718 0.7226 0.1368  -0.1830 -0.1264 278 GLN A OE1 
1697 N NE2 . GLN A 263 ? 1.1263 1.2422 0.6818 0.1234  -0.1657 -0.1040 278 GLN A NE2 
1698 N N   . ARG A 264 ? 1.0326 1.1154 0.6576 0.1000  -0.1695 -0.1082 279 ARG A N   
1699 C CA  . ARG A 264 ? 1.0910 1.1470 0.7173 0.0919  -0.1864 -0.1148 279 ARG A CA  
1700 C C   . ARG A 264 ? 1.0993 1.1545 0.7375 0.0949  -0.1778 -0.1122 279 ARG A C   
1701 O O   . ARG A 264 ? 1.1003 1.1658 0.7659 0.0809  -0.1763 -0.1035 279 ARG A O   
1702 C CB  . ARG A 264 ? 1.1132 1.1751 0.7651 0.0695  -0.1975 -0.1084 279 ARG A CB  
1703 C CG  . ARG A 264 ? 1.1738 1.2492 0.8257 0.0640  -0.2016 -0.1059 279 ARG A CG  
1704 C CD  . ARG A 264 ? 1.2096 1.2997 0.8939 0.0428  -0.2070 -0.0966 279 ARG A CD  
1705 N NE  . ARG A 264 ? 1.3023 1.3694 0.9889 0.0312  -0.2272 -0.1020 279 ARG A NE  
1706 C CZ  . ARG A 264 ? 1.3862 1.4538 1.0821 0.0179  -0.2421 -0.1015 279 ARG A CZ  
1707 N NH1 . ARG A 264 ? 1.3832 1.4738 1.0873 0.0148  -0.2395 -0.0960 279 ARG A NH1 
1708 N NH2 . ARG A 264 ? 1.4247 1.4698 1.1234 0.0072  -0.2604 -0.1062 279 ARG A NH2 
1709 N N   . GLY A 265 ? 1.1224 1.1667 0.7400 0.1140  -0.1719 -0.1194 280 GLY A N   
1710 C CA  . GLY A 265 ? 1.1077 1.1592 0.7378 0.1197  -0.1599 -0.1153 280 GLY A CA  
1711 C C   . GLY A 265 ? 1.1526 1.1752 0.7619 0.1348  -0.1655 -0.1265 280 GLY A C   
1712 O O   . GLY A 265 ? 1.1411 1.1701 0.7421 0.1526  -0.1526 -0.1281 280 GLY A O   
1713 N N   . SER A 266 ? 1.1861 1.1773 0.7889 0.1272  -0.1849 -0.1337 281 SER A N   
1714 C CA  . SER A 266 ? 1.2332 1.1903 0.8158 0.1398  -0.1941 -0.1452 281 SER A CA  
1715 C C   . SER A 266 ? 1.2365 1.2024 0.8191 0.1578  -0.1783 -0.1444 281 SER A C   
1716 O O   . SER A 266 ? 1.2313 1.1969 0.7907 0.1788  -0.1704 -0.1517 281 SER A O   
1717 C CB  . SER A 266 ? 1.2423 1.1747 0.8372 0.1224  -0.2120 -0.1447 281 SER A CB  
1718 O OG  . SER A 266 ? 1.1958 1.1505 0.8247 0.1062  -0.2049 -0.1302 281 SER A OG  
1719 N N   . GLY A 267 ? 1.2281 1.2035 0.8365 0.1502  -0.1734 -0.1352 282 GLY A N   
1720 C CA  . GLY A 267 ? 1.2361 1.2163 0.8463 0.1666  -0.1620 -0.1349 282 GLY A CA  
1721 C C   . GLY A 267 ? 1.2212 1.2294 0.8647 0.1573  -0.1507 -0.1210 282 GLY A C   
1722 O O   . GLY A 267 ? 1.2328 1.2480 0.8977 0.1372  -0.1548 -0.1121 282 GLY A O   
1723 N N   . GLY A 268 ? 1.2184 1.2423 0.8656 0.1731  -0.1367 -0.1194 283 GLY A N   
1724 C CA  . GLY A 268 ? 1.1865 1.2431 0.8637 0.1679  -0.1235 -0.1068 283 GLY A CA  
1725 C C   . GLY A 268 ? 1.1410 1.2023 0.8439 0.1471  -0.1284 -0.0967 283 GLY A C   
1726 O O   . GLY A 268 ? 1.1120 1.1998 0.8347 0.1341  -0.1215 -0.0872 283 GLY A O   
1727 N N   . ALA A 269 ? 1.1532 1.1886 0.8550 0.1448  -0.1400 -0.0984 284 ALA A N   
1728 C CA  . ALA A 269 ? 1.1211 1.1625 0.8466 0.1293  -0.1423 -0.0877 284 ALA A CA  
1729 C C   . ALA A 269 ? 1.0438 1.1146 0.7914 0.1110  -0.1361 -0.0769 284 ALA A C   
1730 O O   . ALA A 269 ? 1.0275 1.1269 0.7936 0.1107  -0.1243 -0.0693 284 ALA A O   
1731 C CB  . ALA A 269 ? 1.1525 1.1573 0.8707 0.1206  -0.1600 -0.0900 284 ALA A CB  
1732 N N   . ASP A 270 ? 0.9799 1.0434 0.7259 0.0963  -0.1447 -0.0768 285 ASP A N   
1733 C CA  . ASP A 270 ? 0.9100 0.9972 0.6766 0.0787  -0.1409 -0.0669 285 ASP A CA  
1734 C C   . ASP A 270 ? 0.8752 0.9757 0.6369 0.0774  -0.1373 -0.0689 285 ASP A C   
1735 O O   . ASP A 270 ? 0.8510 0.9655 0.6259 0.0628  -0.1374 -0.0627 285 ASP A O   
1736 C CB  . ASP A 270 ? 0.9093 0.9810 0.6836 0.0604  -0.1535 -0.0622 285 ASP A CB  
1737 C CG  . ASP A 270 ? 0.8899 0.9402 0.6640 0.0620  -0.1601 -0.0607 285 ASP A CG  
1738 O OD1 . ASP A 270 ? 0.8388 0.8944 0.6141 0.0746  -0.1530 -0.0604 285 ASP A OD1 
1739 O OD2 . ASP A 270 ? 0.8501 0.8786 0.6238 0.0499  -0.1727 -0.0591 285 ASP A OD2 
1740 N N   . ASP A 271 ? 0.8673 0.9636 0.6093 0.0934  -0.1339 -0.0771 286 ASP A N   
1741 C CA  . ASP A 271 ? 0.8345 0.9420 0.5681 0.0945  -0.1303 -0.0789 286 ASP A CA  
1742 C C   . ASP A 271 ? 0.8065 0.9463 0.5512 0.1002  -0.1128 -0.0724 286 ASP A C   
1743 O O   . ASP A 271 ? 0.8252 0.9744 0.5743 0.1112  -0.1033 -0.0712 286 ASP A O   
1744 C CB  . ASP A 271 ? 0.8722 0.9567 0.5748 0.1097  -0.1361 -0.0914 286 ASP A CB  
1745 C CG  . ASP A 271 ? 0.8848 0.9377 0.5745 0.1018  -0.1555 -0.0986 286 ASP A CG  
1746 O OD1 . ASP A 271 ? 0.8479 0.8993 0.5545 0.0835  -0.1635 -0.0927 286 ASP A OD1 
1747 O OD2 . ASP A 271 ? 0.9199 0.9494 0.5825 0.1143  -0.1628 -0.1103 286 ASP A OD2 
1748 N N   . ILE A 272 ? 0.7819 0.9385 0.5315 0.0930  -0.1090 -0.0681 287 ILE A N   
1749 C CA  . ILE A 272 ? 0.7616 0.9481 0.5236 0.0959  -0.0931 -0.0607 287 ILE A CA  
1750 C C   . ILE A 272 ? 0.7687 0.9577 0.5108 0.1138  -0.0845 -0.0651 287 ILE A C   
1751 O O   . ILE A 272 ? 0.8012 0.9756 0.5201 0.1193  -0.0904 -0.0721 287 ILE A O   
1752 C CB  . ILE A 272 ? 0.7460 0.9500 0.5229 0.0812  -0.0918 -0.0531 287 ILE A CB  
1753 C CG1 . ILE A 272 ? 0.7731 0.9667 0.5330 0.0793  -0.1003 -0.0576 287 ILE A CG1 
1754 C CG2 . ILE A 272 ? 0.7262 0.9321 0.5240 0.0651  -0.0975 -0.0477 287 ILE A CG2 
1755 C CD1 . ILE A 272 ? 0.7482 0.9621 0.5209 0.0698  -0.0959 -0.0499 287 ILE A CD1 
1756 N N   . THR A 273 ? 0.7680 0.9759 0.5193 0.1234  -0.0707 -0.0609 288 THR A N   
1757 C CA  . THR A 273 ? 0.7771 0.9958 0.5149 0.1386  -0.0587 -0.0614 288 THR A CA  
1758 C C   . THR A 273 ? 0.7373 0.9747 0.4814 0.1306  -0.0523 -0.0536 288 THR A C   
1759 O O   . THR A 273 ? 0.6861 0.9295 0.4466 0.1147  -0.0564 -0.0482 288 THR A O   
1760 C CB  . THR A 273 ? 0.8025 1.0413 0.5526 0.1504  -0.0441 -0.0572 288 THR A CB  
1761 O OG1 . THR A 273 ? 0.7933 1.0620 0.5622 0.1456  -0.0308 -0.0461 288 THR A OG1 
1762 C CG2 . THR A 273 ? 0.8115 1.0478 0.5792 0.1476  -0.0480 -0.0567 288 THR A CG2 
1763 N N   . GLU A 274 ? 0.7564 1.0029 0.4862 0.1433  -0.0417 -0.0527 289 GLU A N   
1764 C CA  . GLU A 274 ? 0.7278 0.9934 0.4622 0.1391  -0.0328 -0.0438 289 GLU A CA  
1765 C C   . GLU A 274 ? 0.6612 0.9542 0.4292 0.1297  -0.0220 -0.0317 289 GLU A C   
1766 O O   . GLU A 274 ? 0.6358 0.9410 0.4140 0.1203  -0.0189 -0.0240 289 GLU A O   
1767 C CB  . GLU A 274 ? 0.7645 1.0335 0.4748 0.1573  -0.0223 -0.0451 289 GLU A CB  
1768 C CG  . GLU A 274 ? 0.8089 1.0748 0.4999 0.1568  -0.0240 -0.0441 289 GLU A CG  
1769 C CD  . GLU A 274 ? 0.8783 1.1450 0.5407 0.1767  -0.0141 -0.0462 289 GLU A CD  
1770 O OE1 . GLU A 274 ? 0.9421 1.2311 0.6146 0.1842  0.0030  -0.0381 289 GLU A OE1 
1771 O OE2 . GLU A 274 ? 0.8795 1.1253 0.5097 0.1849  -0.0231 -0.0558 289 GLU A OE2 
1772 N N   . ASP A 275 ? 0.6058 0.9074 0.3902 0.1328  -0.0172 -0.0304 290 ASP A N   
1773 C CA  . ASP A 275 ? 0.5649 0.8915 0.3800 0.1249  -0.0082 -0.0201 290 ASP A CA  
1774 C C   . ASP A 275 ? 0.5236 0.8499 0.3566 0.1064  -0.0166 -0.0169 290 ASP A C   
1775 O O   . ASP A 275 ? 0.4800 0.8235 0.3320 0.0977  -0.0109 -0.0085 290 ASP A O   
1776 C CB  . ASP A 275 ? 0.5788 0.9143 0.4066 0.1334  -0.0029 -0.0203 290 ASP A CB  
1777 C CG  . ASP A 275 ? 0.6185 0.9621 0.4331 0.1528  0.0095  -0.0210 290 ASP A CG  
1778 O OD1 . ASP A 275 ? 0.6307 0.9806 0.4331 0.1571  0.0174  -0.0175 290 ASP A OD1 
1779 O OD2 . ASP A 275 ? 0.6224 0.9663 0.4381 0.1646  0.0116  -0.0248 290 ASP A OD2 
1780 N N   . HIS A 276 ? 0.5319 0.8381 0.3582 0.1006  -0.0301 -0.0236 291 HIS A N   
1781 C CA  . HIS A 276 ? 0.5077 0.8120 0.3471 0.0841  -0.0385 -0.0213 291 HIS A CA  
1782 C C   . HIS A 276 ? 0.4999 0.8071 0.3356 0.0774  -0.0393 -0.0182 291 HIS A C   
1783 O O   . HIS A 276 ? 0.4929 0.8086 0.3448 0.0655  -0.0404 -0.0131 291 HIS A O   
1784 C CB  . HIS A 276 ? 0.5234 0.8045 0.3535 0.0803  -0.0525 -0.0286 291 HIS A CB  
1785 C CG  . HIS A 276 ? 0.5505 0.8247 0.3833 0.0860  -0.0543 -0.0316 291 HIS A CG  
1786 N ND1 . HIS A 276 ? 0.5901 0.8471 0.4034 0.0992  -0.0572 -0.0396 291 HIS A ND1 
1787 C CD2 . HIS A 276 ? 0.5479 0.8289 0.3995 0.0809  -0.0543 -0.0281 291 HIS A CD2 
1788 C CE1 . HIS A 276 ? 0.6027 0.8562 0.4237 0.1021  -0.0588 -0.0403 291 HIS A CE1 
1789 N NE2 . HIS A 276 ? 0.5703 0.8387 0.4143 0.0909  -0.0571 -0.0331 291 HIS A NE2 
1790 N N   . VAL A 277 ? 0.5114 0.8103 0.3241 0.0857  -0.0396 -0.0217 292 VAL A N   
1791 C CA  . VAL A 277 ? 0.5036 0.8052 0.3113 0.0809  -0.0406 -0.0184 292 VAL A CA  
1792 C C   . VAL A 277 ? 0.4766 0.8002 0.3013 0.0788  -0.0280 -0.0080 292 VAL A C   
1793 O O   . VAL A 277 ? 0.4607 0.7919 0.2995 0.0683  -0.0289 -0.0025 292 VAL A O   
1794 C CB  . VAL A 277 ? 0.5383 0.8281 0.3157 0.0923  -0.0424 -0.0235 292 VAL A CB  
1795 C CG1 . VAL A 277 ? 0.5367 0.8303 0.3105 0.0870  -0.0441 -0.0190 292 VAL A CG1 
1796 C CG2 . VAL A 277 ? 0.5675 0.8322 0.3258 0.0950  -0.0565 -0.0350 292 VAL A CG2 
1797 N N   . LEU A 278 ? 0.4769 0.8109 0.3007 0.0893  -0.0162 -0.0050 293 LEU A N   
1798 C CA  . LEU A 278 ? 0.4564 0.8113 0.2977 0.0871  -0.0040 0.0057  293 LEU A CA  
1799 C C   . LEU A 278 ? 0.4279 0.7923 0.2983 0.0741  -0.0058 0.0095  293 LEU A C   
1800 O O   . LEU A 278 ? 0.4151 0.7872 0.2983 0.0651  -0.0046 0.0158  293 LEU A O   
1801 C CB  . LEU A 278 ? 0.4692 0.8355 0.3079 0.1003  0.0089  0.0083  293 LEU A CB  
1802 C CG  . LEU A 278 ? 0.4681 0.8562 0.3227 0.0986  0.0224  0.0208  293 LEU A CG  
1803 C CD1 . LEU A 278 ? 0.4854 0.8707 0.3213 0.1010  0.0252  0.0251  293 LEU A CD1 
1804 C CD2 . LEU A 278 ? 0.4736 0.8781 0.3358 0.1094  0.0353  0.0244  293 LEU A CD2 
1805 N N   . MET A 279 ? 0.4179 0.7798 0.2968 0.0736  -0.0095 0.0053  294 MET A N   
1806 C CA  . MET A 279 ? 0.3923 0.7629 0.2960 0.0627  -0.0115 0.0084  294 MET A CA  
1807 C C   . MET A 279 ? 0.3880 0.7521 0.2946 0.0507  -0.0202 0.0080  294 MET A C   
1808 O O   . MET A 279 ? 0.3804 0.7543 0.3044 0.0422  -0.0188 0.0131  294 MET A O   
1809 C CB  . MET A 279 ? 0.3867 0.7545 0.2962 0.0655  -0.0147 0.0041  294 MET A CB  
1810 C CG  . MET A 279 ? 0.3855 0.7653 0.2992 0.0771  -0.0049 0.0059  294 MET A CG  
1811 S SD  . MET A 279 ? 0.3638 0.7708 0.3043 0.0731  0.0072  0.0172  294 MET A SD  
1812 C CE  . MET A 279 ? 0.3825 0.7944 0.3088 0.0793  0.0176  0.0228  294 MET A CE  
1813 N N   . THR A 280 ? 0.4003 0.7485 0.2904 0.0503  -0.0293 0.0021  295 THR A N   
1814 C CA  . THR A 280 ? 0.3939 0.7388 0.2880 0.0397  -0.0368 0.0024  295 THR A CA  
1815 C C   . THR A 280 ? 0.3875 0.7405 0.2840 0.0372  -0.0327 0.0084  295 THR A C   
1816 O O   . THR A 280 ? 0.3679 0.7253 0.2766 0.0285  -0.0351 0.0111  295 THR A O   
1817 C CB  . THR A 280 ? 0.4233 0.7508 0.3012 0.0392  -0.0479 -0.0045 295 THR A CB  
1818 O OG1 . THR A 280 ? 0.4306 0.7497 0.3096 0.0394  -0.0524 -0.0087 295 THR A OG1 
1819 C CG2 . THR A 280 ? 0.4164 0.7436 0.2998 0.0286  -0.0552 -0.0033 295 THR A CG2 
1820 N N   . ALA A 281 ? 0.4014 0.7560 0.2852 0.0455  -0.0263 0.0108  296 ALA A N   
1821 C CA  . ALA A 281 ? 0.3887 0.7502 0.2739 0.0441  -0.0216 0.0180  296 ALA A CA  
1822 C C   . ALA A 281 ? 0.3708 0.7470 0.2792 0.0390  -0.0136 0.0256  296 ALA A C   
1823 O O   . ALA A 281 ? 0.3501 0.7299 0.2683 0.0325  -0.0139 0.0303  296 ALA A O   
1824 C CB  . ALA A 281 ? 0.4116 0.7715 0.2763 0.0550  -0.0156 0.0195  296 ALA A CB  
1825 N N   . ALA A 282 ? 0.3696 0.7538 0.2874 0.0422  -0.0073 0.0266  297 ALA A N   
1826 C CA  . ALA A 282 ? 0.3536 0.7519 0.2947 0.0371  -0.0009 0.0335  297 ALA A CA  
1827 C C   . ALA A 282 ? 0.3372 0.7341 0.2929 0.0269  -0.0085 0.0312  297 ALA A C   
1828 O O   . ALA A 282 ? 0.3280 0.7301 0.2975 0.0203  -0.0076 0.0359  297 ALA A O   
1829 C CB  . ALA A 282 ? 0.3560 0.7640 0.3052 0.0428  0.0056  0.0341  297 ALA A CB  
1830 N N   . GLU A 283 ? 0.3350 0.7240 0.2865 0.0261  -0.0161 0.0241  298 GLU A N   
1831 C CA  . GLU A 283 ? 0.3249 0.7130 0.2879 0.0175  -0.0228 0.0218  298 GLU A CA  
1832 C C   . GLU A 283 ? 0.3231 0.7079 0.2852 0.0117  -0.0270 0.0226  298 GLU A C   
1833 O O   . GLU A 283 ? 0.3158 0.7037 0.2902 0.0054  -0.0294 0.0230  298 GLU A O   
1834 C CB  . GLU A 283 ? 0.3285 0.7081 0.2853 0.0179  -0.0296 0.0154  298 GLU A CB  
1835 C CG  . GLU A 283 ? 0.3237 0.7047 0.2925 0.0103  -0.0345 0.0142  298 GLU A CG  
1836 C CD  . GLU A 283 ? 0.3325 0.7102 0.3014 0.0123  -0.0375 0.0109  298 GLU A CD  
1837 O OE1 . GLU A 283 ? 0.3404 0.7072 0.2996 0.0114  -0.0439 0.0073  298 GLU A OE1 
1838 O OE2 . GLU A 283 ? 0.3404 0.7264 0.3197 0.0148  -0.0338 0.0125  298 GLU A OE2 
1839 N N   . ALA A 284 ? 0.3356 0.7144 0.2829 0.0146  -0.0285 0.0226  299 ALA A N   
1840 C CA  . ALA A 284 ? 0.3345 0.7118 0.2827 0.0100  -0.0328 0.0236  299 ALA A CA  
1841 C C   . ALA A 284 ? 0.3210 0.7054 0.2832 0.0068  -0.0280 0.0297  299 ALA A C   
1842 O O   . ALA A 284 ? 0.3195 0.7043 0.2893 0.0021  -0.0315 0.0297  299 ALA A O   
1843 C CB  . ALA A 284 ? 0.3495 0.7199 0.2797 0.0143  -0.0359 0.0229  299 ALA A CB  
1844 N N   . PHE A 285 ? 0.3259 0.7160 0.2925 0.0095  -0.0201 0.0349  300 PHE A N   
1845 C CA  . PHE A 285 ? 0.3186 0.7145 0.3011 0.0054  -0.0160 0.0410  300 PHE A CA  
1846 C C   . PHE A 285 ? 0.3003 0.7008 0.2994 0.0004  -0.0179 0.0383  300 PHE A C   
1847 O O   . PHE A 285 ? 0.2913 0.6908 0.2995 -0.0047 -0.0219 0.0369  300 PHE A O   
1848 C CB  . PHE A 285 ? 0.3304 0.7325 0.3132 0.0094  -0.0064 0.0489  300 PHE A CB  
1849 C CG  . PHE A 285 ? 0.3442 0.7418 0.3085 0.0153  -0.0038 0.0525  300 PHE A CG  
1850 C CD1 . PHE A 285 ? 0.3540 0.7495 0.3187 0.0136  -0.0029 0.0592  300 PHE A CD1 
1851 C CD2 . PHE A 285 ? 0.3551 0.7495 0.3002 0.0232  -0.0032 0.0491  300 PHE A CD2 
1852 C CE1 . PHE A 285 ? 0.3693 0.7605 0.3154 0.0196  -0.0012 0.0629  300 PHE A CE1 
1853 C CE2 . PHE A 285 ? 0.3692 0.7588 0.2948 0.0294  -0.0017 0.0519  300 PHE A CE2 
1854 C CZ  . PHE A 285 ? 0.3745 0.7631 0.3005 0.0275  -0.0007 0.0591  300 PHE A CZ  
1855 N N   . GLY A 286 ? 0.3013 0.7066 0.3033 0.0029  -0.0154 0.0370  301 GLY A N   
1856 C CA  . GLY A 286 ? 0.3105 0.7206 0.3276 -0.0011 -0.0179 0.0345  301 GLY A CA  
1857 C C   . GLY A 286 ? 0.3017 0.7070 0.3206 -0.0061 -0.0256 0.0293  301 GLY A C   
1858 O O   . GLY A 286 ? 0.2991 0.7063 0.3302 -0.0107 -0.0275 0.0295  301 GLY A O   
1859 N N   . ALA A 287 ? 0.3098 0.7086 0.3160 -0.0050 -0.0300 0.0250  302 ALA A N   
1860 C CA  . ALA A 287 ? 0.3031 0.6989 0.3096 -0.0090 -0.0360 0.0210  302 ALA A CA  
1861 C C   . ALA A 287 ? 0.3052 0.6993 0.3116 -0.0110 -0.0374 0.0220  302 ALA A C   
1862 O O   . ALA A 287 ? 0.3276 0.7219 0.3384 -0.0139 -0.0407 0.0196  302 ALA A O   
1863 C CB  . ALA A 287 ? 0.3037 0.6941 0.2987 -0.0078 -0.0400 0.0172  302 ALA A CB  
1864 N N   . GLY A 288 ? 0.2969 0.6891 0.2970 -0.0084 -0.0350 0.0255  303 GLY A N   
1865 C CA  . GLY A 288 ? 0.2879 0.6778 0.2856 -0.0090 -0.0375 0.0263  303 GLY A CA  
1866 C C   . GLY A 288 ? 0.2896 0.6795 0.2960 -0.0101 -0.0356 0.0303  303 GLY A C   
1867 O O   . GLY A 288 ? 0.2995 0.6879 0.3074 -0.0105 -0.0386 0.0295  303 GLY A O   
1868 N N   . VAL A 289 ? 0.2931 0.6845 0.3061 -0.0104 -0.0307 0.0349  304 VAL A N   
1869 C CA  . VAL A 289 ? 0.2967 0.6854 0.3170 -0.0117 -0.0292 0.0401  304 VAL A CA  
1870 C C   . VAL A 289 ? 0.3133 0.7008 0.3463 -0.0158 -0.0327 0.0368  304 VAL A C   
1871 O O   . VAL A 289 ? 0.3299 0.7128 0.3637 -0.0156 -0.0361 0.0351  304 VAL A O   
1872 C CB  . VAL A 289 ? 0.2905 0.6819 0.3139 -0.0112 -0.0222 0.0480  304 VAL A CB  
1873 C CG1 . VAL A 289 ? 0.2930 0.6808 0.3278 -0.0147 -0.0211 0.0540  304 VAL A CG1 
1874 C CG2 . VAL A 289 ? 0.3003 0.6907 0.3073 -0.0057 -0.0191 0.0513  304 VAL A CG2 
1875 N N   . GLU A 290 ? 0.3130 0.7046 0.3556 -0.0186 -0.0322 0.0355  305 GLU A N   
1876 C CA  . GLU A 290 ? 0.3246 0.7140 0.3786 -0.0223 -0.0362 0.0325  305 GLU A CA  
1877 C C   . GLU A 290 ? 0.3236 0.7106 0.3724 -0.0212 -0.0416 0.0247  305 GLU A C   
1878 O O   . GLU A 290 ? 0.3381 0.7199 0.3911 -0.0218 -0.0452 0.0219  305 GLU A O   
1879 C CB  . GLU A 290 ? 0.3415 0.7372 0.4066 -0.0252 -0.0357 0.0326  305 GLU A CB  
1880 C CG  . GLU A 290 ? 0.3583 0.7508 0.4379 -0.0301 -0.0400 0.0315  305 GLU A CG  
1881 C CD  . GLU A 290 ? 0.3869 0.7790 0.4786 -0.0338 -0.0363 0.0403  305 GLU A CD  
1882 O OE1 . GLU A 290 ? 0.3956 0.7942 0.4872 -0.0326 -0.0291 0.0476  305 GLU A OE1 
1883 O OE2 . GLU A 290 ? 0.4561 0.8407 0.5575 -0.0378 -0.0408 0.0400  305 GLU A OE2 
1884 N N   . THR A 291 ? 0.3113 0.7018 0.3507 -0.0192 -0.0421 0.0217  306 THR A N   
1885 C CA  . THR A 291 ? 0.3084 0.6989 0.3430 -0.0182 -0.0457 0.0163  306 THR A CA  
1886 C C   . THR A 291 ? 0.3457 0.7334 0.3777 -0.0157 -0.0464 0.0170  306 THR A C   
1887 O O   . THR A 291 ? 0.3525 0.7392 0.3859 -0.0143 -0.0489 0.0130  306 THR A O   
1888 C CB  . THR A 291 ? 0.2970 0.6913 0.3231 -0.0177 -0.0459 0.0148  306 THR A CB  
1889 O OG1 . THR A 291 ? 0.2904 0.6841 0.3097 -0.0160 -0.0439 0.0184  306 THR A OG1 
1890 C CG2 . THR A 291 ? 0.2864 0.6828 0.3143 -0.0190 -0.0465 0.0131  306 THR A CG2 
1891 N N   . THR A 292 ? 0.3645 0.7514 0.3919 -0.0141 -0.0444 0.0218  307 THR A N   
1892 C CA  . THR A 292 ? 0.3960 0.7814 0.4210 -0.0111 -0.0458 0.0228  307 THR A CA  
1893 C C   . THR A 292 ? 0.3834 0.7615 0.4152 -0.0105 -0.0461 0.0245  307 THR A C   
1894 O O   . THR A 292 ? 0.3984 0.7744 0.4322 -0.0081 -0.0488 0.0209  307 THR A O   
1895 C CB  . THR A 292 ? 0.4457 0.8316 0.4621 -0.0090 -0.0450 0.0271  307 THR A CB  
1896 O OG1 . THR A 292 ? 0.5923 0.9761 0.6072 -0.0096 -0.0409 0.0318  307 THR A OG1 
1897 C CG2 . THR A 292 ? 0.4209 0.8118 0.4309 -0.0095 -0.0470 0.0242  307 THR A CG2 
1898 N N   . SER A 293 ? 0.3555 0.7294 0.3910 -0.0125 -0.0434 0.0302  308 SER A N   
1899 C CA  . SER A 293 ? 0.3706 0.7354 0.4140 -0.0134 -0.0444 0.0327  308 SER A CA  
1900 C C   . SER A 293 ? 0.3532 0.7143 0.4026 -0.0141 -0.0489 0.0251  308 SER A C   
1901 O O   . SER A 293 ? 0.3612 0.7141 0.4122 -0.0115 -0.0520 0.0233  308 SER A O   
1902 C CB  . SER A 293 ? 0.3914 0.7545 0.4423 -0.0177 -0.0407 0.0398  308 SER A CB  
1903 O OG  . SER A 293 ? 0.4390 0.8077 0.4831 -0.0166 -0.0355 0.0456  308 SER A OG  
1904 N N   . THR A 294 ? 0.3176 0.6838 0.3692 -0.0168 -0.0498 0.0205  309 THR A N   
1905 C CA  . THR A 294 ? 0.3221 0.6839 0.3773 -0.0169 -0.0547 0.0131  309 THR A CA  
1906 C C   . THR A 294 ? 0.3137 0.6763 0.3615 -0.0110 -0.0565 0.0070  309 THR A C   
1907 O O   . THR A 294 ? 0.3101 0.6649 0.3587 -0.0081 -0.0601 0.0021  309 THR A O   
1908 C CB  . THR A 294 ? 0.3105 0.6777 0.3685 -0.0204 -0.0560 0.0095  309 THR A CB  
1909 O OG1 . THR A 294 ? 0.3067 0.6745 0.3749 -0.0254 -0.0546 0.0150  309 THR A OG1 
1910 C CG2 . THR A 294 ? 0.3134 0.6754 0.3719 -0.0195 -0.0619 0.0012  309 THR A CG2 
1911 N N   . THR A 295 ? 0.2985 0.6707 0.3395 -0.0092 -0.0541 0.0074  310 THR A N   
1912 C CA  . THR A 295 ? 0.3030 0.6796 0.3393 -0.0040 -0.0547 0.0033  310 THR A CA  
1913 C C   . THR A 295 ? 0.3169 0.6872 0.3546 0.0011  -0.0557 0.0043  310 THR A C   
1914 O O   . THR A 295 ? 0.3359 0.7049 0.3725 0.0066  -0.0573 -0.0009 310 THR A O   
1915 C CB  . THR A 295 ? 0.3041 0.6921 0.3357 -0.0045 -0.0524 0.0052  310 THR A CB  
1916 O OG1 . THR A 295 ? 0.3084 0.6997 0.3383 -0.0088 -0.0518 0.0048  310 THR A OG1 
1917 C CG2 . THR A 295 ? 0.3120 0.7076 0.3416 -0.0001 -0.0523 0.0018  310 THR A CG2 
1918 N N   . LEU A 296 ? 0.3149 0.6808 0.3540 0.0002  -0.0548 0.0111  311 LEU A N   
1919 C CA  . LEU A 296 ? 0.3217 0.6788 0.3622 0.0050  -0.0565 0.0133  311 LEU A CA  
1920 C C   . LEU A 296 ? 0.3307 0.6733 0.3761 0.0051  -0.0600 0.0098  311 LEU A C   
1921 O O   . LEU A 296 ? 0.3419 0.6772 0.3870 0.0115  -0.0628 0.0063  311 LEU A O   
1922 C CB  . LEU A 296 ? 0.3297 0.6837 0.3691 0.0035  -0.0547 0.0225  311 LEU A CB  
1923 C CG  . LEU A 296 ? 0.3219 0.6865 0.3549 0.0042  -0.0529 0.0260  311 LEU A CG  
1924 C CD1 . LEU A 296 ? 0.3228 0.6829 0.3522 0.0028  -0.0507 0.0347  311 LEU A CD1 
1925 C CD2 . LEU A 296 ? 0.3225 0.6929 0.3543 0.0107  -0.0553 0.0241  311 LEU A CD2 
1926 N N   . LEU A 297 ? 0.3217 0.6597 0.3723 -0.0017 -0.0605 0.0109  312 LEU A N   
1927 C CA  . LEU A 297 ? 0.3223 0.6455 0.3790 -0.0031 -0.0654 0.0076  312 LEU A CA  
1928 C C   . LEU A 297 ? 0.3279 0.6490 0.3801 0.0022  -0.0694 -0.0036 312 LEU A C   
1929 O O   . LEU A 297 ? 0.3477 0.6548 0.4003 0.0062  -0.0741 -0.0078 312 LEU A O   
1930 C CB  . LEU A 297 ? 0.3121 0.6341 0.3776 -0.0120 -0.0657 0.0107  312 LEU A CB  
1931 C CG  . LEU A 297 ? 0.3130 0.6314 0.3846 -0.0165 -0.0624 0.0222  312 LEU A CG  
1932 C CD1 . LEU A 297 ? 0.3056 0.6300 0.3869 -0.0247 -0.0605 0.0261  312 LEU A CD1 
1933 C CD2 . LEU A 297 ? 0.3319 0.6322 0.4080 -0.0158 -0.0664 0.0246  312 LEU A CD2 
1934 N N   . TRP A 298 ? 0.3108 0.6447 0.3576 0.0030  -0.0676 -0.0080 313 TRP A N   
1935 C CA  . TRP A 298 ? 0.3184 0.6523 0.3584 0.0092  -0.0701 -0.0179 313 TRP A CA  
1936 C C   . TRP A 298 ? 0.3307 0.6659 0.3663 0.0192  -0.0688 -0.0200 313 TRP A C   
1937 O O   . TRP A 298 ? 0.3319 0.6576 0.3640 0.0263  -0.0722 -0.0274 313 TRP A O   
1938 C CB  . TRP A 298 ? 0.3031 0.6512 0.3379 0.0076  -0.0677 -0.0203 313 TRP A CB  
1939 C CG  . TRP A 298 ? 0.3033 0.6486 0.3402 0.0016  -0.0714 -0.0231 313 TRP A CG  
1940 C CD1 . TRP A 298 ? 0.2922 0.6460 0.3316 -0.0047 -0.0695 -0.0191 313 TRP A CD1 
1941 C CD2 . TRP A 298 ? 0.3113 0.6446 0.3483 0.0018  -0.0785 -0.0306 313 TRP A CD2 
1942 N NE1 . TRP A 298 ? 0.2883 0.6378 0.3307 -0.0083 -0.0748 -0.0231 313 TRP A NE1 
1943 C CE2 . TRP A 298 ? 0.3114 0.6481 0.3523 -0.0049 -0.0808 -0.0303 313 TRP A CE2 
1944 C CE3 . TRP A 298 ? 0.3330 0.6520 0.3668 0.0075  -0.0839 -0.0382 313 TRP A CE3 
1945 C CZ2 . TRP A 298 ? 0.3321 0.6594 0.3748 -0.0068 -0.0892 -0.0372 313 TRP A CZ2 
1946 C CZ3 . TRP A 298 ? 0.3540 0.6613 0.3881 0.0055  -0.0924 -0.0456 313 TRP A CZ3 
1947 C CH2 . TRP A 298 ? 0.3471 0.6594 0.3860 -0.0019 -0.0952 -0.0449 313 TRP A CH2 
1948 N N   . THR A 299 ? 0.3263 0.6734 0.3622 0.0202  -0.0643 -0.0137 314 THR A N   
1949 C CA  . THR A 299 ? 0.3327 0.6851 0.3670 0.0292  -0.0630 -0.0145 314 THR A CA  
1950 C C   . THR A 299 ? 0.3674 0.7022 0.4030 0.0355  -0.0672 -0.0167 314 THR A C   
1951 O O   . THR A 299 ? 0.4067 0.7391 0.4387 0.0451  -0.0684 -0.0237 314 THR A O   
1952 C CB  . THR A 299 ? 0.3176 0.6814 0.3542 0.0275  -0.0600 -0.0062 314 THR A CB  
1953 O OG1 . THR A 299 ? 0.2997 0.6780 0.3346 0.0223  -0.0569 -0.0050 314 THR A OG1 
1954 C CG2 . THR A 299 ? 0.3204 0.6907 0.3581 0.0368  -0.0596 -0.0060 314 THR A CG2 
1955 N N   . ILE A 300 ? 0.3780 0.7001 0.4181 0.0305  -0.0693 -0.0105 315 ILE A N   
1956 C CA  . ILE A 300 ? 0.4040 0.7067 0.4460 0.0349  -0.0739 -0.0106 315 ILE A CA  
1957 C C   . ILE A 300 ? 0.4239 0.7115 0.4643 0.0360  -0.0794 -0.0203 315 ILE A C   
1958 O O   . ILE A 300 ? 0.4480 0.7228 0.4856 0.0449  -0.0833 -0.0263 315 ILE A O   
1959 C CB  . ILE A 300 ? 0.4156 0.7092 0.4632 0.0272  -0.0739 0.0003  315 ILE A CB  
1960 C CG1 . ILE A 300 ? 0.4230 0.7269 0.4690 0.0302  -0.0705 0.0085  315 ILE A CG1 
1961 C CG2 . ILE A 300 ? 0.4308 0.7002 0.4820 0.0279  -0.0797 0.0007  315 ILE A CG2 
1962 C CD1 . ILE A 300 ? 0.4316 0.7342 0.4793 0.0224  -0.0680 0.0196  315 ILE A CD1 
1963 N N   . ALA A 301 ? 0.4229 0.7113 0.4649 0.0276  -0.0805 -0.0222 316 ALA A N   
1964 C CA  . ALA A 301 ? 0.4386 0.7124 0.4787 0.0279  -0.0875 -0.0320 316 ALA A CA  
1965 C C   . ALA A 301 ? 0.4475 0.7235 0.4764 0.0402  -0.0878 -0.0432 316 ALA A C   
1966 O O   . ALA A 301 ? 0.4725 0.7307 0.4971 0.0467  -0.0942 -0.0517 316 ALA A O   
1967 C CB  . ALA A 301 ? 0.4256 0.7042 0.4693 0.0177  -0.0887 -0.0324 316 ALA A CB  
1968 N N   . PHE A 302 ? 0.4365 0.7340 0.4607 0.0438  -0.0810 -0.0427 317 PHE A N   
1969 C CA  . PHE A 302 ? 0.4603 0.7643 0.4744 0.0554  -0.0793 -0.0516 317 PHE A CA  
1970 C C   . PHE A 302 ? 0.4921 0.7929 0.5056 0.0677  -0.0786 -0.0528 317 PHE A C   
1971 O O   . PHE A 302 ? 0.5451 0.8409 0.5503 0.0795  -0.0799 -0.0623 317 PHE A O   
1972 C CB  . PHE A 302 ? 0.4472 0.7759 0.4580 0.0541  -0.0720 -0.0494 317 PHE A CB  
1973 C CG  . PHE A 302 ? 0.4425 0.7722 0.4477 0.0483  -0.0739 -0.0536 317 PHE A CG  
1974 C CD1 . PHE A 302 ? 0.4626 0.7862 0.4560 0.0556  -0.0771 -0.0644 317 PHE A CD1 
1975 C CD2 . PHE A 302 ? 0.4259 0.7622 0.4366 0.0368  -0.0729 -0.0470 317 PHE A CD2 
1976 C CE1 . PHE A 302 ? 0.4646 0.7886 0.4519 0.0509  -0.0799 -0.0682 317 PHE A CE1 
1977 C CE2 . PHE A 302 ? 0.4297 0.7667 0.4358 0.0324  -0.0754 -0.0505 317 PHE A CE2 
1978 C CZ  . PHE A 302 ? 0.4501 0.7812 0.4446 0.0391  -0.0792 -0.0609 317 PHE A CZ  
1979 N N   . LEU A 303 ? 0.4940 0.7975 0.5154 0.0662  -0.0767 -0.0434 318 LEU A N   
1980 C CA  . LEU A 303 ? 0.5039 0.8050 0.5259 0.0783  -0.0767 -0.0437 318 LEU A CA  
1981 C C   . LEU A 303 ? 0.5217 0.7939 0.5417 0.0832  -0.0846 -0.0495 318 LEU A C   
1982 O O   . LEU A 303 ? 0.5334 0.7995 0.5498 0.0966  -0.0859 -0.0548 318 LEU A O   
1983 C CB  . LEU A 303 ? 0.5085 0.8188 0.5385 0.0752  -0.0741 -0.0320 318 LEU A CB  
1984 C CG  . LEU A 303 ? 0.4987 0.8368 0.5312 0.0713  -0.0674 -0.0267 318 LEU A CG  
1985 C CD1 . LEU A 303 ? 0.4973 0.8397 0.5357 0.0663  -0.0671 -0.0156 318 LEU A CD1 
1986 C CD2 . LEU A 303 ? 0.4943 0.8514 0.5257 0.0826  -0.0630 -0.0311 318 LEU A CD2 
1987 N N   . LEU A 304 ? 0.5348 0.7888 0.5576 0.0727  -0.0903 -0.0485 319 LEU A N   
1988 C CA  . LEU A 304 ? 0.5785 0.8028 0.5996 0.0761  -0.0994 -0.0549 319 LEU A CA  
1989 C C   . LEU A 304 ? 0.5997 0.8179 0.6085 0.0869  -0.1026 -0.0701 319 LEU A C   
1990 O O   . LEU A 304 ? 0.6290 0.8302 0.6324 0.0990  -0.1071 -0.0775 319 LEU A O   
1991 C CB  . LEU A 304 ? 0.5891 0.7972 0.6183 0.0611  -0.1051 -0.0502 319 LEU A CB  
1992 C CG  . LEU A 304 ? 0.6002 0.7952 0.6385 0.0565  -0.1065 -0.0383 319 LEU A CG  
1993 C CD1 . LEU A 304 ? 0.5888 0.8058 0.6292 0.0567  -0.0979 -0.0275 319 LEU A CD1 
1994 C CD2 . LEU A 304 ? 0.6095 0.7926 0.6581 0.0409  -0.1105 -0.0318 319 LEU A CD2 
1995 N N   . HIS A 305 ? 0.6030 0.8351 0.6061 0.0838  -0.1002 -0.0749 320 HIS A N   
1996 C CA  . HIS A 305 ? 0.6420 0.8697 0.6304 0.0950  -0.1027 -0.0893 320 HIS A CA  
1997 C C   . HIS A 305 ? 0.6400 0.8830 0.6213 0.1118  -0.0953 -0.0927 320 HIS A C   
1998 O O   . HIS A 305 ? 0.6598 0.8952 0.6281 0.1254  -0.0972 -0.1048 320 HIS A O   
1999 C CB  . HIS A 305 ? 0.6398 0.8789 0.6228 0.0876  -0.1020 -0.0923 320 HIS A CB  
2000 C CG  . HIS A 305 ? 0.6633 0.8847 0.6515 0.0747  -0.1116 -0.0933 320 HIS A CG  
2001 N ND1 . HIS A 305 ? 0.6842 0.8936 0.6622 0.0756  -0.1198 -0.1051 320 HIS A ND1 
2002 C CD2 . HIS A 305 ? 0.6741 0.8891 0.6773 0.0606  -0.1144 -0.0836 320 HIS A CD2 
2003 C CE1 . HIS A 305 ? 0.7090 0.9058 0.6977 0.0620  -0.1279 -0.1026 320 HIS A CE1 
2004 N NE2 . HIS A 305 ? 0.6859 0.8866 0.6903 0.0528  -0.1240 -0.0892 320 HIS A NE2 
2005 N N   . HIS A 306 ? 0.6138 0.8787 0.6039 0.1112  -0.0872 -0.0823 321 HIS A N   
2006 C CA  . HIS A 306 ? 0.6249 0.9095 0.6126 0.1255  -0.0796 -0.0836 321 HIS A CA  
2007 C C   . HIS A 306 ? 0.6197 0.9049 0.6173 0.1313  -0.0789 -0.0764 321 HIS A C   
2008 O O   . HIS A 306 ? 0.5951 0.9045 0.6011 0.1298  -0.0723 -0.0676 321 HIS A O   
2009 C CB  . HIS A 306 ? 0.6049 0.9208 0.5937 0.1202  -0.0703 -0.0783 321 HIS A CB  
2010 C CG  . HIS A 306 ? 0.6162 0.9325 0.5929 0.1175  -0.0706 -0.0854 321 HIS A CG  
2011 N ND1 . HIS A 306 ? 0.6170 0.9261 0.5949 0.1029  -0.0750 -0.0834 321 HIS A ND1 
2012 C CD2 . HIS A 306 ? 0.6278 0.9508 0.5904 0.1285  -0.0673 -0.0945 321 HIS A CD2 
2013 C CE1 . HIS A 306 ? 0.6127 0.9239 0.5779 0.1047  -0.0752 -0.0909 321 HIS A CE1 
2014 N NE2 . HIS A 306 ? 0.6218 0.9410 0.5765 0.1201  -0.0704 -0.0976 321 HIS A NE2 
2015 N N   . PRO A 307 ? 0.6470 0.9049 0.6433 0.1384  -0.0865 -0.0804 322 PRO A N   
2016 C CA  . PRO A 307 ? 0.6562 0.9123 0.6614 0.1435  -0.0870 -0.0726 322 PRO A CA  
2017 C C   . PRO A 307 ? 0.6766 0.9603 0.6849 0.1572  -0.0791 -0.0716 322 PRO A C   
2018 O O   . PRO A 307 ? 0.6523 0.9488 0.6711 0.1563  -0.0772 -0.0615 322 PRO A O   
2019 C CB  . PRO A 307 ? 0.6727 0.8931 0.6727 0.1519  -0.0967 -0.0799 322 PRO A CB  
2020 C CG  . PRO A 307 ? 0.6947 0.8961 0.6864 0.1451  -0.1029 -0.0890 322 PRO A CG  
2021 C CD  . PRO A 307 ? 0.6823 0.9095 0.6679 0.1437  -0.0956 -0.0929 322 PRO A CD  
2022 N N   . GLN A 308 ? 0.7032 0.9967 0.7026 0.1699  -0.0749 -0.0819 323 GLN A N   
2023 C CA  . GLN A 308 ? 0.7157 1.0390 0.7198 0.1833  -0.0663 -0.0808 323 GLN A CA  
2024 C C   . GLN A 308 ? 0.6688 1.0236 0.6849 0.1709  -0.0595 -0.0687 323 GLN A C   
2025 O O   . GLN A 308 ? 0.6763 1.0483 0.7047 0.1735  -0.0574 -0.0606 323 GLN A O   
2026 C CB  . GLN A 308 ? 0.7510 1.0813 0.7418 0.1984  -0.0613 -0.0933 323 GLN A CB  
2027 C CG  . GLN A 308 ? 0.7676 1.1096 0.7492 0.1901  -0.0566 -0.0960 323 GLN A CG  
2028 C CD  . GLN A 308 ? 0.7868 1.1000 0.7585 0.1782  -0.0656 -0.1014 323 GLN A CD  
2029 O OE1 . GLN A 308 ? 0.8202 1.1015 0.7855 0.1822  -0.0752 -0.1092 323 GLN A OE1 
2030 N NE2 . GLN A 308 ? 0.7492 1.0738 0.7203 0.1639  -0.0631 -0.0973 323 GLN A NE2 
2031 N N   . LEU A 309 ? 0.6534 1.0135 0.6659 0.1572  -0.0575 -0.0675 324 LEU A N   
2032 C CA  . LEU A 309 ? 0.6167 1.0031 0.6386 0.1445  -0.0519 -0.0572 324 LEU A CA  
2033 C C   . LEU A 309 ? 0.5903 0.9733 0.6229 0.1346  -0.0560 -0.0464 324 LEU A C   
2034 O O   . LEU A 309 ? 0.5760 0.9818 0.6188 0.1309  -0.0526 -0.0381 324 LEU A O   
2035 C CB  . LEU A 309 ? 0.6116 0.9973 0.6254 0.1323  -0.0508 -0.0590 324 LEU A CB  
2036 C CG  . LEU A 309 ? 0.5933 1.0016 0.6137 0.1185  -0.0459 -0.0497 324 LEU A CG  
2037 C CD1 . LEU A 309 ? 0.5981 1.0388 0.6265 0.1240  -0.0375 -0.0453 324 LEU A CD1 
2038 C CD2 . LEU A 309 ? 0.5939 0.9975 0.6041 0.1100  -0.0458 -0.0533 324 LEU A CD2 
2039 N N   . GLN A 310 ? 0.5916 0.9461 0.6216 0.1304  -0.0635 -0.0463 325 GLN A N   
2040 C CA  . GLN A 310 ? 0.5802 0.9295 0.6178 0.1226  -0.0670 -0.0358 325 GLN A CA  
2041 C C   . GLN A 310 ? 0.5822 0.9409 0.6273 0.1345  -0.0672 -0.0320 325 GLN A C   
2042 O O   . GLN A 310 ? 0.5615 0.9334 0.6144 0.1295  -0.0671 -0.0226 325 GLN A O   
2043 C CB  . GLN A 310 ? 0.5974 0.9141 0.6311 0.1170  -0.0742 -0.0359 325 GLN A CB  
2044 C CG  . GLN A 310 ? 0.5951 0.9048 0.6344 0.1111  -0.0772 -0.0244 325 GLN A CG  
2045 C CD  . GLN A 310 ? 0.6111 0.8904 0.6486 0.1041  -0.0833 -0.0221 325 GLN A CD  
2046 O OE1 . GLN A 310 ? 0.5939 0.8657 0.6344 0.0996  -0.0853 -0.0120 325 GLN A OE1 
2047 N NE2 . GLN A 310 ? 0.6207 0.8824 0.6531 0.1027  -0.0867 -0.0310 325 GLN A NE2 
2048 N N   . GLU A 311 ? 0.6134 0.9647 0.6556 0.1508  -0.0682 -0.0398 326 GLU A N   
2049 C CA  . GLU A 311 ? 0.6145 0.9772 0.6646 0.1655  -0.0682 -0.0377 326 GLU A CA  
2050 C C   . GLU A 311 ? 0.5763 0.9778 0.6366 0.1669  -0.0607 -0.0341 326 GLU A C   
2051 O O   . GLU A 311 ? 0.5458 0.9635 0.6174 0.1694  -0.0615 -0.0267 326 GLU A O   
2052 C CB  . GLU A 311 ? 0.6599 1.0056 0.7033 0.1842  -0.0704 -0.0483 326 GLU A CB  
2053 C CG  . GLU A 311 ? 0.7135 1.0222 0.7528 0.1868  -0.0798 -0.0481 326 GLU A CG  
2054 C CD  . GLU A 311 ? 0.7887 1.0726 0.8174 0.2024  -0.0837 -0.0613 326 GLU A CD  
2055 O OE1 . GLU A 311 ? 0.8195 1.1072 0.8499 0.2212  -0.0833 -0.0650 326 GLU A OE1 
2056 O OE2 . GLU A 311 ? 0.8179 1.0774 0.8365 0.1965  -0.0878 -0.0685 326 GLU A OE2 
2057 N N   . ARG A 312 ? 0.5552 0.9723 0.6122 0.1647  -0.0539 -0.0386 327 ARG A N   
2058 C CA  . ARG A 312 ? 0.5490 1.0034 0.6174 0.1646  -0.0465 -0.0339 327 ARG A CA  
2059 C C   . ARG A 312 ? 0.5309 0.9997 0.6089 0.1487  -0.0476 -0.0230 327 ARG A C   
2060 O O   . ARG A 312 ? 0.5141 1.0091 0.6060 0.1501  -0.0459 -0.0169 327 ARG A O   
2061 C CB  . ARG A 312 ? 0.5472 1.0137 0.6084 0.1660  -0.0386 -0.0401 327 ARG A CB  
2062 C CG  . ARG A 312 ? 0.5822 1.0442 0.6358 0.1860  -0.0361 -0.0506 327 ARG A CG  
2063 C CD  . ARG A 312 ? 0.6099 1.0782 0.6512 0.1874  -0.0292 -0.0575 327 ARG A CD  
2064 N NE  . ARG A 312 ? 0.6015 1.1049 0.6526 0.1802  -0.0204 -0.0496 327 ARG A NE  
2065 C CZ  . ARG A 312 ? 0.6146 1.1244 0.6579 0.1712  -0.0157 -0.0495 327 ARG A CZ  
2066 N NH1 . ARG A 312 ? 0.6218 1.1065 0.6471 0.1682  -0.0193 -0.0575 327 ARG A NH1 
2067 N NH2 . ARG A 312 ? 0.5941 1.1354 0.6482 0.1647  -0.0081 -0.0410 327 ARG A NH2 
2068 N N   . VAL A 313 ? 0.5345 0.9860 0.6054 0.1341  -0.0509 -0.0209 328 VAL A N   
2069 C CA  . VAL A 313 ? 0.5032 0.9624 0.5796 0.1198  -0.0530 -0.0116 328 VAL A CA  
2070 C C   . VAL A 313 ? 0.5035 0.9563 0.5850 0.1229  -0.0596 -0.0055 328 VAL A C   
2071 O O   . VAL A 313 ? 0.4987 0.9666 0.5880 0.1175  -0.0615 0.0017  328 VAL A O   
2072 C CB  . VAL A 313 ? 0.4869 0.9278 0.5534 0.1054  -0.0544 -0.0116 328 VAL A CB  
2073 C CG1 . VAL A 313 ? 0.4707 0.9152 0.5404 0.0929  -0.0572 -0.0028 328 VAL A CG1 
2074 C CG2 . VAL A 313 ? 0.4744 0.9234 0.5358 0.1015  -0.0487 -0.0164 328 VAL A CG2 
2075 N N   . GLN A 314 ? 0.5235 0.9518 0.5992 0.1312  -0.0638 -0.0082 329 GLN A N   
2076 C CA  . GLN A 314 ? 0.5310 0.9507 0.6096 0.1357  -0.0702 -0.0018 329 GLN A CA  
2077 C C   . GLN A 314 ? 0.5230 0.9675 0.6146 0.1482  -0.0702 -0.0001 329 GLN A C   
2078 O O   . GLN A 314 ? 0.5188 0.9681 0.6159 0.1489  -0.0754 0.0072  329 GLN A O   
2079 C CB  . GLN A 314 ? 0.5530 0.9392 0.6230 0.1419  -0.0749 -0.0047 329 GLN A CB  
2080 C CG  . GLN A 314 ? 0.5517 0.9140 0.6132 0.1282  -0.0773 -0.0014 329 GLN A CG  
2081 C CD  . GLN A 314 ? 0.5882 0.9185 0.6424 0.1320  -0.0808 -0.0069 329 GLN A CD  
2082 O OE1 . GLN A 314 ? 0.6052 0.9294 0.6578 0.1447  -0.0813 -0.0154 329 GLN A OE1 
2083 N NE2 . GLN A 314 ? 0.6048 0.9145 0.6547 0.1208  -0.0835 -0.0019 329 GLN A NE2 
2084 N N   . ALA A 315 ? 0.5285 0.9897 0.6249 0.1586  -0.0644 -0.0065 330 ALA A N   
2085 C CA  . ALA A 315 ? 0.5135 1.0035 0.6253 0.1707  -0.0629 -0.0047 330 ALA A CA  
2086 C C   . ALA A 315 ? 0.4906 1.0102 0.6146 0.1589  -0.0617 0.0026  330 ALA A C   
2087 O O   . ALA A 315 ? 0.4948 1.0327 0.6321 0.1618  -0.0657 0.0086  330 ALA A O   
2088 C CB  . ALA A 315 ? 0.5091 1.0102 0.6217 0.1850  -0.0555 -0.0132 330 ALA A CB  
2089 N N   . GLU A 316 ? 0.4762 0.9990 0.5956 0.1454  -0.0572 0.0020  331 GLU A N   
2090 C CA  . GLU A 316 ? 0.4603 1.0083 0.5903 0.1331  -0.0562 0.0083  331 GLU A CA  
2091 C C   . GLU A 316 ? 0.4598 1.0024 0.5912 0.1258  -0.0653 0.0155  331 GLU A C   
2092 O O   . GLU A 316 ? 0.4554 1.0204 0.6008 0.1246  -0.0688 0.0209  331 GLU A O   
2093 C CB  . GLU A 316 ? 0.4483 0.9944 0.5702 0.1201  -0.0509 0.0065  331 GLU A CB  
2094 C CG  . GLU A 316 ? 0.4485 1.0240 0.5832 0.1103  -0.0478 0.0119  331 GLU A CG  
2095 C CD  . GLU A 316 ? 0.4709 1.0440 0.5970 0.0989  -0.0423 0.0104  331 GLU A CD  
2096 O OE1 . GLU A 316 ? 0.4954 1.0465 0.6088 0.0889  -0.0454 0.0098  331 GLU A OE1 
2097 O OE2 . GLU A 316 ? 0.4676 1.0621 0.5999 0.1001  -0.0347 0.0106  331 GLU A OE2 
2098 N N   . LEU A 317 ? 0.4661 0.9789 0.5827 0.1213  -0.0694 0.0156  332 LEU A N   
2099 C CA  . LEU A 317 ? 0.4558 0.9601 0.5690 0.1150  -0.0772 0.0223  332 LEU A CA  
2100 C C   . LEU A 317 ? 0.4677 0.9785 0.5893 0.1266  -0.0840 0.0264  332 LEU A C   
2101 O O   . LEU A 317 ? 0.4525 0.9742 0.5790 0.1226  -0.0903 0.0321  332 LEU A O   
2102 C CB  . LEU A 317 ? 0.4460 0.9176 0.5423 0.1101  -0.0784 0.0221  332 LEU A CB  
2103 C CG  . LEU A 317 ? 0.4359 0.9032 0.5249 0.0958  -0.0745 0.0207  332 LEU A CG  
2104 C CD1 . LEU A 317 ? 0.4408 0.8785 0.5167 0.0930  -0.0741 0.0191  332 LEU A CD1 
2105 C CD2 . LEU A 317 ? 0.4212 0.8976 0.5103 0.0850  -0.0783 0.0264  332 LEU A CD2 
2106 N N   . ASP A 318 ? 0.4894 0.9924 0.6117 0.1415  -0.0833 0.0229  333 ASP A N   
2107 C CA  . ASP A 318 ? 0.5159 1.0226 0.6455 0.1551  -0.0896 0.0262  333 ASP A CA  
2108 C C   . ASP A 318 ? 0.5322 1.0766 0.6828 0.1592  -0.0905 0.0287  333 ASP A C   
2109 O O   . ASP A 318 ? 0.5759 1.1287 0.7332 0.1617  -0.0987 0.0346  333 ASP A O   
2110 C CB  . ASP A 318 ? 0.5273 1.0165 0.6530 0.1711  -0.0880 0.0205  333 ASP A CB  
2111 C CG  . ASP A 318 ? 0.5298 0.9804 0.6374 0.1672  -0.0892 0.0190  333 ASP A CG  
2112 O OD1 . ASP A 318 ? 0.5202 0.9583 0.6191 0.1547  -0.0920 0.0245  333 ASP A OD1 
2113 O OD2 . ASP A 318 ? 0.5310 0.9639 0.6334 0.1766  -0.0874 0.0123  333 ASP A OD2 
2114 N N   . GLU A 319 ? 0.5284 1.0960 0.6896 0.1599  -0.0822 0.0249  334 GLU A N   
2115 C CA  . GLU A 319 ? 0.5322 1.1387 0.7164 0.1622  -0.0815 0.0281  334 GLU A CA  
2116 C C   . GLU A 319 ? 0.5300 1.1486 0.7195 0.1457  -0.0874 0.0344  334 GLU A C   
2117 O O   . GLU A 319 ? 0.5781 1.2144 0.7812 0.1470  -0.0957 0.0397  334 GLU A O   
2118 C CB  . GLU A 319 ? 0.5454 1.1729 0.7374 0.1648  -0.0696 0.0237  334 GLU A CB  
2119 C CG  . GLU A 319 ? 0.5719 1.1884 0.7570 0.1824  -0.0632 0.0157  334 GLU A CG  
2120 C CD  . GLU A 319 ? 0.5902 1.2080 0.7674 0.1800  -0.0521 0.0096  334 GLU A CD  
2121 O OE1 . GLU A 319 ? 0.5794 1.1965 0.7515 0.1634  -0.0500 0.0112  334 GLU A OE1 
2122 O OE2 . GLU A 319 ? 0.5943 1.2127 0.7691 0.1956  -0.0459 0.0028  334 GLU A OE2 
2123 N N   . CYS A 320 ? 0.5196 1.1276 0.6979 0.1307  -0.0842 0.0333  335 CYS A N   
2124 C CA  . CYS A 320 ? 0.5383 1.1569 0.7206 0.1145  -0.0887 0.0377  335 CYS A CA  
2125 C C   . CYS A 320 ? 0.5210 1.1203 0.6909 0.1095  -0.0994 0.0413  335 CYS A C   
2126 O O   . CYS A 320 ? 0.5136 1.1267 0.6922 0.1055  -0.1083 0.0456  335 CYS A O   
2127 C CB  . CYS A 320 ? 0.5685 1.1824 0.7428 0.1020  -0.0808 0.0351  335 CYS A CB  
2128 S SG  . CYS A 320 ? 0.6770 1.3050 0.8570 0.1105  -0.0670 0.0299  335 CYS A SG  
2129 N N   . VAL A 321 ? 0.5374 1.1050 0.6867 0.1099  -0.0990 0.0396  336 VAL A N   
2130 C CA  . VAL A 321 ? 0.5587 1.1072 0.6939 0.1068  -0.1076 0.0437  336 VAL A CA  
2131 C C   . VAL A 321 ? 0.5910 1.1304 0.7252 0.1218  -0.1123 0.0460  336 VAL A C   
2132 O O   . VAL A 321 ? 0.5911 1.1321 0.7317 0.1338  -0.1080 0.0429  336 VAL A O   
2133 C CB  . VAL A 321 ? 0.5579 1.0777 0.6721 0.0983  -0.1037 0.0424  336 VAL A CB  
2134 C CG1 . VAL A 321 ? 0.5658 1.0705 0.6653 0.0939  -0.1114 0.0474  336 VAL A CG1 
2135 C CG2 . VAL A 321 ? 0.5465 1.0731 0.6616 0.0862  -0.0972 0.0390  336 VAL A CG2 
2136 N N   . GLY A 322 ? 0.6241 1.1528 0.7488 0.1222  -0.1214 0.0513  337 GLY A N   
2137 C CA  . GLY A 322 ? 0.6808 1.1950 0.8008 0.1360  -0.1259 0.0545  337 GLY A CA  
2138 C C   . GLY A 322 ? 0.6999 1.1843 0.8062 0.1385  -0.1193 0.0522  337 GLY A C   
2139 O O   . GLY A 322 ? 0.6391 1.1180 0.7422 0.1313  -0.1112 0.0474  337 GLY A O   
2140 N N   . VAL A 323 ? 0.7648 1.2297 0.8637 0.1489  -0.1234 0.0561  338 VAL A N   
2141 C CA  . VAL A 323 ? 0.8005 1.2325 0.8834 0.1474  -0.1200 0.0571  338 VAL A CA  
2142 C C   . VAL A 323 ? 0.8259 1.2421 0.8917 0.1404  -0.1245 0.0655  338 VAL A C   
2143 O O   . VAL A 323 ? 0.8933 1.2850 0.9460 0.1351  -0.1209 0.0680  338 VAL A O   
2144 C CB  . VAL A 323 ? 0.8326 1.2485 0.9170 0.1628  -0.1210 0.0561  338 VAL A CB  
2145 C CG1 . VAL A 323 ? 0.8553 1.2621 0.9349 0.1725  -0.1303 0.0648  338 VAL A CG1 
2146 C CG2 . VAL A 323 ? 0.8579 1.2441 0.9316 0.1589  -0.1154 0.0534  338 VAL A CG2 
2147 N N   . ASP A 324 ? 0.8089 1.2399 0.8748 0.1401  -0.1324 0.0699  339 ASP A N   
2148 C CA  . ASP A 324 ? 0.8308 1.2489 0.8779 0.1340  -0.1364 0.0771  339 ASP A CA  
2149 C C   . ASP A 324 ? 0.8172 1.2447 0.8597 0.1197  -0.1343 0.0744  339 ASP A C   
2150 O O   . ASP A 324 ? 0.8527 1.2638 0.8808 0.1114  -0.1290 0.0760  339 ASP A O   
2151 C CB  . ASP A 324 ? 0.8702 1.2917 0.9142 0.1438  -0.1478 0.0840  339 ASP A CB  
2152 C CG  . ASP A 324 ? 0.9256 1.3784 0.9901 0.1493  -0.1548 0.0808  339 ASP A CG  
2153 O OD1 . ASP A 324 ? 0.9474 1.4192 1.0291 0.1465  -0.1495 0.0738  339 ASP A OD1 
2154 O OD2 . ASP A 324 ? 0.8904 1.3496 0.9542 0.1566  -0.1657 0.0858  339 ASP A OD2 
2155 N N   . ARG A 325 ? 0.7629 1.2163 0.8185 0.1167  -0.1383 0.0706  340 ARG A N   
2156 C CA  . ARG A 325 ? 0.7113 1.1726 0.7629 0.1037  -0.1381 0.0678  340 ARG A CA  
2157 C C   . ARG A 325 ? 0.7124 1.1609 0.7575 0.0946  -0.1272 0.0644  340 ARG A C   
2158 O O   . ARG A 325 ? 0.7524 1.1968 0.8044 0.0969  -0.1201 0.0613  340 ARG A O   
2159 C CB  . ARG A 325 ? 0.6795 1.1708 0.7525 0.1009  -0.1414 0.0635  340 ARG A CB  
2160 C CG  . ARG A 325 ? 0.6621 1.1617 0.7321 0.0884  -0.1452 0.0614  340 ARG A CG  
2161 C CD  . ARG A 325 ? 0.6303 1.1603 0.7236 0.0859  -0.1512 0.0595  340 ARG A CD  
2162 N NE  . ARG A 325 ? 0.6004 1.1472 0.7142 0.0869  -0.1424 0.0562  340 ARG A NE  
2163 C CZ  . ARG A 325 ? 0.5628 1.1126 0.6800 0.0778  -0.1336 0.0523  340 ARG A CZ  
2164 N NH1 . ARG A 325 ? 0.5547 1.0913 0.6574 0.0667  -0.1322 0.0508  340 ARG A NH1 
2165 N NH2 . ARG A 325 ? 0.5221 1.0877 0.6560 0.0809  -0.1258 0.0500  340 ARG A NH2 
2166 N N   . PRO A 326 ? 0.6942 1.1359 0.7254 0.0849  -0.1263 0.0646  341 PRO A N   
2167 C CA  . PRO A 326 ? 0.6294 1.0645 0.6583 0.0758  -0.1168 0.0606  341 PRO A CA  
2168 C C   . PRO A 326 ? 0.6055 1.0612 0.6493 0.0691  -0.1155 0.0543  341 PRO A C   
2169 O O   . PRO A 326 ? 0.6317 1.1031 0.6813 0.0667  -0.1228 0.0539  341 PRO A O   
2170 C CB  . PRO A 326 ? 0.6389 1.0612 0.6477 0.0700  -0.1171 0.0637  341 PRO A CB  
2171 C CG  . PRO A 326 ? 0.6672 1.0977 0.6710 0.0725  -0.1281 0.0657  341 PRO A CG  
2172 C CD  . PRO A 326 ? 0.7028 1.1425 0.7190 0.0828  -0.1343 0.0680  341 PRO A CD  
2173 N N   . PRO A 327 ? 0.5827 1.0385 0.6331 0.0659  -0.1069 0.0498  342 PRO A N   
2174 C CA  . PRO A 327 ? 0.5637 1.0382 0.6264 0.0592  -0.1051 0.0453  342 PRO A CA  
2175 C C   . PRO A 327 ? 0.5721 1.0442 0.6254 0.0483  -0.1066 0.0446  342 PRO A C   
2176 O O   . PRO A 327 ? 0.6048 1.0592 0.6425 0.0452  -0.1037 0.0455  342 PRO A O   
2177 C CB  . PRO A 327 ? 0.5597 1.0304 0.6265 0.0597  -0.0956 0.0410  342 PRO A CB  
2178 C CG  . PRO A 327 ? 0.5691 1.0243 0.6321 0.0693  -0.0947 0.0425  342 PRO A CG  
2179 C CD  . PRO A 327 ? 0.5928 1.0336 0.6418 0.0696  -0.0998 0.0487  342 PRO A CD  
2180 N N   . CYS A 328 ? 0.5567 1.0465 0.6203 0.0426  -0.1110 0.0432  343 CYS A N   
2181 C CA  . CYS A 328 ? 0.5490 1.0358 0.6042 0.0328  -0.1145 0.0420  343 CYS A CA  
2182 C C   . CYS A 328 ? 0.5020 1.0031 0.5707 0.0248  -0.1112 0.0393  343 CYS A C   
2183 O O   . CYS A 328 ? 0.4571 0.9723 0.5410 0.0276  -0.1065 0.0389  343 CYS A O   
2184 C CB  . CYS A 328 ? 0.5784 1.0701 0.6312 0.0334  -0.1269 0.0439  343 CYS A CB  
2185 S SG  . CYS A 328 ? 0.6054 1.1252 0.6843 0.0375  -0.1333 0.0456  343 CYS A SG  
2186 N N   . LEU A 329 ? 0.4951 0.9919 0.5574 0.0154  -0.1134 0.0376  344 LEU A N   
2187 C CA  . LEU A 329 ? 0.4916 0.9971 0.5634 0.0074  -0.1087 0.0358  344 LEU A CA  
2188 C C   . LEU A 329 ? 0.4784 1.0096 0.5733 0.0057  -0.1113 0.0379  344 LEU A C   
2189 O O   . LEU A 329 ? 0.4369 0.9796 0.5429 0.0037  -0.1040 0.0379  344 LEU A O   
2190 C CB  . LEU A 329 ? 0.4917 0.9854 0.5516 -0.0017 -0.1115 0.0338  344 LEU A CB  
2191 C CG  . LEU A 329 ? 0.5022 0.9736 0.5412 0.0001  -0.1072 0.0322  344 LEU A CG  
2192 C CD1 . LEU A 329 ? 0.5052 0.9662 0.5327 -0.0072 -0.1111 0.0297  344 LEU A CD1 
2193 C CD2 . LEU A 329 ? 0.5049 0.9714 0.5440 0.0019  -0.0961 0.0313  344 LEU A CD2 
2194 N N   . SER A 330 ? 0.5106 1.0523 0.6131 0.0070  -0.1214 0.0399  345 SER A N   
2195 C CA  . SER A 330 ? 0.5173 1.0867 0.6451 0.0049  -0.1240 0.0428  345 SER A CA  
2196 C C   . SER A 330 ? 0.5117 1.0967 0.6535 0.0141  -0.1144 0.0439  345 SER A C   
2197 O O   . SER A 330 ? 0.5197 1.1292 0.6825 0.0120  -0.1118 0.0464  345 SER A O   
2198 C CB  . SER A 330 ? 0.5134 1.0919 0.6478 0.0055  -0.1379 0.0447  345 SER A CB  
2199 O OG  . SER A 330 ? 0.5595 1.1372 0.6917 0.0182  -0.1393 0.0458  345 SER A OG  
2200 N N   . ASP A 331 ? 0.4888 1.0596 0.6190 0.0243  -0.1091 0.0420  346 ASP A N   
2201 C CA  . ASP A 331 ? 0.4706 1.0511 0.6102 0.0344  -0.1005 0.0414  346 ASP A CA  
2202 C C   . ASP A 331 ? 0.4937 1.0754 0.6332 0.0309  -0.0894 0.0391  346 ASP A C   
2203 O O   . ASP A 331 ? 0.5011 1.0960 0.6503 0.0383  -0.0822 0.0385  346 ASP A O   
2204 C CB  . ASP A 331 ? 0.4707 1.0317 0.5970 0.0455  -0.0994 0.0400  346 ASP A CB  
2205 C CG  . ASP A 331 ? 0.4675 1.0256 0.5914 0.0510  -0.1099 0.0431  346 ASP A CG  
2206 O OD1 . ASP A 331 ? 0.4990 1.0785 0.6400 0.0551  -0.1153 0.0455  346 ASP A OD1 
2207 O OD2 . ASP A 331 ? 0.4409 0.9766 0.5462 0.0517  -0.1126 0.0436  346 ASP A OD2 
2208 N N   . ARG A 332 ? 0.5160 1.0836 0.6434 0.0209  -0.0882 0.0378  347 ARG A N   
2209 C CA  . ARG A 332 ? 0.5257 1.0907 0.6493 0.0174  -0.0787 0.0356  347 ARG A CA  
2210 C C   . ARG A 332 ? 0.5082 1.0984 0.6487 0.0184  -0.0718 0.0375  347 ARG A C   
2211 O O   . ARG A 332 ? 0.5066 1.0972 0.6448 0.0257  -0.0634 0.0347  347 ARG A O   
2212 C CB  . ARG A 332 ? 0.5716 1.1231 0.6841 0.0056  -0.0805 0.0352  347 ARG A CB  
2213 C CG  . ARG A 332 ? 0.6242 1.1494 0.7168 0.0066  -0.0819 0.0324  347 ARG A CG  
2214 C CD  . ARG A 332 ? 0.6526 1.1648 0.7340 -0.0029 -0.0821 0.0313  347 ARG A CD  
2215 N NE  . ARG A 332 ? 0.7122 1.2178 0.7883 -0.0029 -0.0737 0.0288  347 ARG A NE  
2216 C CZ  . ARG A 332 ? 0.7113 1.2008 0.7748 -0.0068 -0.0719 0.0268  347 ARG A CZ  
2217 N NH1 . ARG A 332 ? 0.6969 1.1744 0.7504 -0.0106 -0.0771 0.0268  347 ARG A NH1 
2218 N NH2 . ARG A 332 ? 0.6765 1.1626 0.7370 -0.0061 -0.0652 0.0245  347 ARG A NH2 
2219 N N   . PRO A 333 ? 0.5001 1.1115 0.6576 0.0113  -0.0755 0.0425  348 PRO A N   
2220 C CA  . PRO A 333 ? 0.4904 1.1297 0.6665 0.0120  -0.0682 0.0462  348 PRO A CA  
2221 C C   . PRO A 333 ? 0.4788 1.1319 0.6632 0.0274  -0.0629 0.0450  348 PRO A C   
2222 O O   . PRO A 333 ? 0.4782 1.1460 0.6681 0.0323  -0.0527 0.0452  348 PRO A O   
2223 C CB  . PRO A 333 ? 0.4859 1.1443 0.6812 0.0020  -0.0766 0.0523  348 PRO A CB  
2224 C CG  . PRO A 333 ? 0.4975 1.1330 0.6788 -0.0067 -0.0870 0.0505  348 PRO A CG  
2225 C CD  . PRO A 333 ? 0.4988 1.1101 0.6598 0.0025  -0.0873 0.0451  348 PRO A CD  
2226 N N   . HIS A 334 ? 0.4353 1.0825 0.6190 0.0357  -0.0696 0.0435  349 HIS A N   
2227 C CA  . HIS A 334 ? 0.4262 1.0824 0.6162 0.0516  -0.0662 0.0418  349 HIS A CA  
2228 C C   . HIS A 334 ? 0.4161 1.0485 0.5876 0.0620  -0.0610 0.0351  349 HIS A C   
2229 O O   . HIS A 334 ? 0.3901 1.0247 0.5645 0.0760  -0.0596 0.0329  349 HIS A O   
2230 C CB  . HIS A 334 ? 0.4614 1.1233 0.6607 0.0558  -0.0771 0.0444  349 HIS A CB  
2231 C CG  . HIS A 334 ? 0.4778 1.1642 0.6976 0.0459  -0.0839 0.0505  349 HIS A CG  
2232 N ND1 . HIS A 334 ? 0.4767 1.1965 0.7205 0.0457  -0.0783 0.0551  349 HIS A ND1 
2233 C CD2 . HIS A 334 ? 0.4873 1.1695 0.7071 0.0349  -0.0956 0.0527  349 HIS A CD2 
2234 C CE1 . HIS A 334 ? 0.4855 1.2208 0.7454 0.0340  -0.0870 0.0604  349 HIS A CE1 
2235 N NE2 . HIS A 334 ? 0.4986 1.2105 0.7435 0.0276  -0.0983 0.0584  349 HIS A NE2 
2236 N N   . LEU A 335 ? 0.4179 1.0279 0.5715 0.0552  -0.0585 0.0319  350 LEU A N   
2237 C CA  . LEU A 335 ? 0.4237 1.0105 0.5607 0.0629  -0.0544 0.0254  350 LEU A CA  
2238 C C   . LEU A 335 ? 0.4052 0.9894 0.5338 0.0596  -0.0458 0.0221  350 LEU A C   
2239 O O   . LEU A 335 ? 0.3931 0.9558 0.5068 0.0544  -0.0459 0.0191  350 LEU A O   
2240 C CB  . LEU A 335 ? 0.4416 1.0005 0.5639 0.0597  -0.0612 0.0247  350 LEU A CB  
2241 C CG  . LEU A 335 ? 0.4479 1.0064 0.5745 0.0643  -0.0701 0.0282  350 LEU A CG  
2242 C CD1 . LEU A 335 ? 0.4455 0.9768 0.5556 0.0611  -0.0752 0.0287  350 LEU A CD1 
2243 C CD2 . LEU A 335 ? 0.4544 1.0199 0.5891 0.0800  -0.0693 0.0270  350 LEU A CD2 
2244 N N   . PRO A 336 ? 0.4006 1.0082 0.5390 0.0638  -0.0381 0.0230  351 PRO A N   
2245 C CA  . PRO A 336 ? 0.3896 0.9997 0.5211 0.0598  -0.0301 0.0219  351 PRO A CA  
2246 C C   . PRO A 336 ? 0.4066 0.9933 0.5189 0.0659  -0.0272 0.0136  351 PRO A C   
2247 O O   . PRO A 336 ? 0.3985 0.9757 0.4995 0.0588  -0.0250 0.0123  351 PRO A O   
2248 C CB  . PRO A 336 ? 0.3945 1.0365 0.5414 0.0670  -0.0220 0.0250  351 PRO A CB  
2249 C CG  . PRO A 336 ? 0.3949 1.0461 0.5536 0.0790  -0.0250 0.0247  351 PRO A CG  
2250 C CD  . PRO A 336 ? 0.3941 1.0295 0.5518 0.0728  -0.0364 0.0262  351 PRO A CD  
2251 N N   . LEU A 337 ? 0.4079 0.9849 0.5167 0.0789  -0.0282 0.0082  352 LEU A N   
2252 C CA  . LEU A 337 ? 0.4145 0.9681 0.5064 0.0850  -0.0272 -0.0003 352 LEU A CA  
2253 C C   . LEU A 337 ? 0.4092 0.9367 0.4908 0.0746  -0.0336 -0.0008 352 LEU A C   
2254 O O   . LEU A 337 ? 0.4095 0.9265 0.4805 0.0685  -0.0323 -0.0033 352 LEU A O   
2255 C CB  . LEU A 337 ? 0.4271 0.9748 0.5191 0.1015  -0.0281 -0.0057 352 LEU A CB  
2256 C CG  . LEU A 337 ? 0.4379 0.9624 0.5134 0.1102  -0.0275 -0.0158 352 LEU A CG  
2257 C CD1 . LEU A 337 ? 0.4492 0.9853 0.5174 0.1143  -0.0191 -0.0198 352 LEU A CD1 
2258 C CD2 . LEU A 337 ? 0.4469 0.9617 0.5231 0.1258  -0.0305 -0.0205 352 LEU A CD2 
2259 N N   . LEU A 338 ? 0.4081 0.9266 0.4929 0.0728  -0.0402 0.0023  353 LEU A N   
2260 C CA  . LEU A 338 ? 0.4021 0.8992 0.4783 0.0632  -0.0452 0.0033  353 LEU A CA  
2261 C C   . LEU A 338 ? 0.3788 0.8776 0.4506 0.0512  -0.0432 0.0047  353 LEU A C   
2262 O O   . LEU A 338 ? 0.3646 0.8468 0.4264 0.0471  -0.0436 0.0016  353 LEU A O   
2263 C CB  . LEU A 338 ? 0.3887 0.8845 0.4698 0.0607  -0.0516 0.0091  353 LEU A CB  
2264 C CG  . LEU A 338 ? 0.3848 0.8610 0.4567 0.0517  -0.0556 0.0112  353 LEU A CG  
2265 C CD1 . LEU A 338 ? 0.4173 0.8711 0.4792 0.0527  -0.0547 0.0065  353 LEU A CD1 
2266 C CD2 . LEU A 338 ? 0.3926 0.8644 0.4659 0.0537  -0.0616 0.0160  353 LEU A CD2 
2267 N N   . ASP A 339 ? 0.3724 0.8914 0.4528 0.0454  -0.0416 0.0096  354 ASP A N   
2268 C CA  . ASP A 339 ? 0.3725 0.8913 0.4486 0.0340  -0.0405 0.0116  354 ASP A CA  
2269 C C   . ASP A 339 ? 0.3702 0.8855 0.4370 0.0358  -0.0350 0.0070  354 ASP A C   
2270 O O   . ASP A 339 ? 0.3583 0.8624 0.4164 0.0287  -0.0356 0.0062  354 ASP A O   
2271 C CB  . ASP A 339 ? 0.3680 0.9083 0.4561 0.0272  -0.0402 0.0181  354 ASP A CB  
2272 C CG  . ASP A 339 ? 0.3809 0.9156 0.4637 0.0150  -0.0415 0.0206  354 ASP A CG  
2273 O OD1 . ASP A 339 ? 0.4042 0.9250 0.4820 0.0095  -0.0473 0.0211  354 ASP A OD1 
2274 O OD2 . ASP A 339 ? 0.3891 0.9319 0.4712 0.0119  -0.0364 0.0219  354 ASP A OD2 
2275 N N   . ALA A 340 ? 0.3625 0.8882 0.4308 0.0462  -0.0300 0.0040  355 ALA A N   
2276 C CA  . ALA A 340 ? 0.3562 0.8782 0.4134 0.0504  -0.0253 -0.0014 355 ALA A CA  
2277 C C   . ALA A 340 ? 0.3611 0.8562 0.4062 0.0514  -0.0299 -0.0082 355 ALA A C   
2278 O O   . ALA A 340 ? 0.3740 0.8597 0.4092 0.0470  -0.0300 -0.0108 355 ALA A O   
2279 C CB  . ALA A 340 ? 0.3665 0.9038 0.4263 0.0638  -0.0192 -0.0041 355 ALA A CB  
2280 N N   . VAL A 341 ? 0.3572 0.8402 0.4040 0.0567  -0.0342 -0.0105 356 VAL A N   
2281 C CA  . VAL A 341 ? 0.3571 0.8152 0.3954 0.0571  -0.0388 -0.0160 356 VAL A CA  
2282 C C   . VAL A 341 ? 0.3546 0.8040 0.3900 0.0445  -0.0414 -0.0130 356 VAL A C   
2283 O O   . VAL A 341 ? 0.3576 0.7963 0.3851 0.0419  -0.0424 -0.0171 356 VAL A O   
2284 C CB  . VAL A 341 ? 0.3571 0.8037 0.3996 0.0628  -0.0433 -0.0158 356 VAL A CB  
2285 C CG1 . VAL A 341 ? 0.3611 0.7822 0.3978 0.0595  -0.0485 -0.0186 356 VAL A CG1 
2286 C CG2 . VAL A 341 ? 0.3768 0.8287 0.4206 0.0774  -0.0412 -0.0206 356 VAL A CG2 
2287 N N   . LEU A 342 ? 0.3508 0.8057 0.3923 0.0374  -0.0427 -0.0061 357 LEU A N   
2288 C CA  . LEU A 342 ? 0.3443 0.7920 0.3830 0.0269  -0.0447 -0.0030 357 LEU A CA  
2289 C C   . LEU A 342 ? 0.3406 0.7928 0.3741 0.0218  -0.0422 -0.0038 357 LEU A C   
2290 O O   . LEU A 342 ? 0.3284 0.7698 0.3566 0.0169  -0.0438 -0.0052 357 LEU A O   
2291 C CB  . LEU A 342 ? 0.3428 0.7979 0.3875 0.0221  -0.0466 0.0036  357 LEU A CB  
2292 C CG  . LEU A 342 ? 0.3558 0.8035 0.4031 0.0261  -0.0502 0.0056  357 LEU A CG  
2293 C CD1 . LEU A 342 ? 0.3514 0.8060 0.4022 0.0218  -0.0532 0.0114  357 LEU A CD1 
2294 C CD2 . LEU A 342 ? 0.3651 0.7926 0.4067 0.0244  -0.0520 0.0044  357 LEU A CD2 
2295 N N   . CYS A 343 ? 0.3443 0.8135 0.3800 0.0233  -0.0380 -0.0022 358 CYS A N   
2296 C CA  . CYS A 343 ? 0.3386 0.8122 0.3686 0.0187  -0.0353 -0.0016 358 CYS A CA  
2297 C C   . CYS A 343 ? 0.3529 0.8161 0.3724 0.0238  -0.0352 -0.0089 358 CYS A C   
2298 O O   . CYS A 343 ? 0.3542 0.8116 0.3666 0.0195  -0.0361 -0.0098 358 CYS A O   
2299 C CB  . CYS A 343 ? 0.3325 0.8274 0.3680 0.0191  -0.0300 0.0031  358 CYS A CB  
2300 S SG  . CYS A 343 ? 0.3287 0.8348 0.3762 0.0093  -0.0323 0.0119  358 CYS A SG  
2301 N N   . GLU A 344 ? 0.3657 0.8256 0.3837 0.0336  -0.0350 -0.0145 359 GLU A N   
2302 C CA  . GLU A 344 ? 0.3807 0.8306 0.3876 0.0394  -0.0359 -0.0225 359 GLU A CA  
2303 C C   . GLU A 344 ? 0.3899 0.8199 0.3945 0.0343  -0.0425 -0.0256 359 GLU A C   
2304 O O   . GLU A 344 ? 0.4350 0.8587 0.4314 0.0327  -0.0445 -0.0293 359 GLU A O   
2305 C CB  . GLU A 344 ? 0.3918 0.8415 0.3973 0.0521  -0.0347 -0.0284 359 GLU A CB  
2306 C CG  . GLU A 344 ? 0.4055 0.8428 0.3973 0.0594  -0.0368 -0.0383 359 GLU A CG  
2307 C CD  . GLU A 344 ? 0.3999 0.8496 0.3810 0.0625  -0.0313 -0.0390 359 GLU A CD  
2308 O OE1 . GLU A 344 ? 0.3874 0.8530 0.3722 0.0560  -0.0264 -0.0309 359 GLU A OE1 
2309 O OE2 . GLU A 344 ? 0.4024 0.8448 0.3704 0.0717  -0.0321 -0.0478 359 GLU A OE2 
2310 N N   . VAL A 345 ? 0.3844 0.8053 0.3964 0.0321  -0.0458 -0.0237 360 VAL A N   
2311 C CA  . VAL A 345 ? 0.3737 0.7780 0.3868 0.0263  -0.0511 -0.0244 360 VAL A CA  
2312 C C   . VAL A 345 ? 0.3596 0.7664 0.3714 0.0175  -0.0511 -0.0211 360 VAL A C   
2313 O O   . VAL A 345 ? 0.3848 0.7827 0.3942 0.0145  -0.0547 -0.0241 360 VAL A O   
2314 C CB  . VAL A 345 ? 0.3823 0.7813 0.4037 0.0245  -0.0525 -0.0193 360 VAL A CB  
2315 C CG1 . VAL A 345 ? 0.3822 0.7698 0.4067 0.0167  -0.0556 -0.0165 360 VAL A CG1 
2316 C CG2 . VAL A 345 ? 0.4034 0.7945 0.4259 0.0335  -0.0542 -0.0229 360 VAL A CG2 
2317 N N   . MET A 346 ? 0.3422 0.7609 0.3564 0.0134  -0.0479 -0.0149 361 MET A N   
2318 C CA  . MET A 346 ? 0.3326 0.7524 0.3450 0.0059  -0.0482 -0.0117 361 MET A CA  
2319 C C   . MET A 346 ? 0.3323 0.7544 0.3362 0.0068  -0.0478 -0.0148 361 MET A C   
2320 O O   . MET A 346 ? 0.3574 0.7750 0.3589 0.0023  -0.0501 -0.0146 361 MET A O   
2321 C CB  . MET A 346 ? 0.3295 0.7593 0.3455 0.0015  -0.0460 -0.0049 361 MET A CB  
2322 C CG  . MET A 346 ? 0.3195 0.7453 0.3408 -0.0011 -0.0476 -0.0011 361 MET A CG  
2323 S SD  . MET A 346 ? 0.3342 0.7726 0.3581 -0.0053 -0.0466 0.0049  361 MET A SD  
2324 C CE  . MET A 346 ? 0.3464 0.7776 0.3712 -0.0085 -0.0496 0.0083  361 MET A CE  
2325 N N   . ARG A 347 ? 0.3387 0.7686 0.3376 0.0131  -0.0446 -0.0172 362 ARG A N   
2326 C CA  . ARG A 347 ? 0.3373 0.7694 0.3251 0.0156  -0.0437 -0.0201 362 ARG A CA  
2327 C C   . ARG A 347 ? 0.3554 0.7736 0.3368 0.0187  -0.0495 -0.0284 362 ARG A C   
2328 O O   . ARG A 347 ? 0.3600 0.7741 0.3360 0.0158  -0.0528 -0.0296 362 ARG A O   
2329 C CB  . ARG A 347 ? 0.3460 0.7910 0.3297 0.0232  -0.0378 -0.0205 362 ARG A CB  
2330 C CG  . ARG A 347 ? 0.3549 0.8064 0.3265 0.0247  -0.0348 -0.0199 362 ARG A CG  
2331 C CD  . ARG A 347 ? 0.3696 0.8295 0.3329 0.0357  -0.0296 -0.0239 362 ARG A CD  
2332 N NE  . ARG A 347 ? 0.3901 0.8357 0.3414 0.0432  -0.0347 -0.0348 362 ARG A NE  
2333 C CZ  . ARG A 347 ? 0.4032 0.8424 0.3535 0.0522  -0.0361 -0.0424 362 ARG A CZ  
2334 N NH1 . ARG A 347 ? 0.4139 0.8610 0.3746 0.0555  -0.0323 -0.0400 362 ARG A NH1 
2335 N NH2 . ARG A 347 ? 0.4209 0.8451 0.3599 0.0581  -0.0422 -0.0525 362 ARG A NH2 
2336 N N   . ILE A 348 ? 0.3653 0.7760 0.3477 0.0248  -0.0515 -0.0342 363 ILE A N   
2337 C CA  . ILE A 348 ? 0.3783 0.7753 0.3533 0.0291  -0.0578 -0.0435 363 ILE A CA  
2338 C C   . ILE A 348 ? 0.3879 0.7724 0.3698 0.0215  -0.0650 -0.0441 363 ILE A C   
2339 O O   . ILE A 348 ? 0.4127 0.7882 0.3890 0.0221  -0.0716 -0.0506 363 ILE A O   
2340 C CB  . ILE A 348 ? 0.3849 0.7751 0.3593 0.0383  -0.0585 -0.0497 363 ILE A CB  
2341 C CG1 . ILE A 348 ? 0.4034 0.7802 0.3655 0.0449  -0.0648 -0.0609 363 ILE A CG1 
2342 C CG2 . ILE A 348 ? 0.3766 0.7577 0.3642 0.0344  -0.0611 -0.0467 363 ILE A CG2 
2343 C CD1 . ILE A 348 ? 0.4228 0.7901 0.3818 0.0556  -0.0663 -0.0685 363 ILE A CD1 
2344 N N   . ARG A 349 ? 0.3599 0.7445 0.3540 0.0148  -0.0641 -0.0374 364 ARG A N   
2345 C CA  . ARG A 349 ? 0.3447 0.7213 0.3473 0.0074  -0.0690 -0.0360 364 ARG A CA  
2346 C C   . ARG A 349 ? 0.3275 0.7121 0.3359 0.0006  -0.0655 -0.0275 364 ARG A C   
2347 O O   . ARG A 349 ? 0.3229 0.7065 0.3399 -0.0028 -0.0639 -0.0224 364 ARG A O   
2348 C CB  . ARG A 349 ? 0.3517 0.7163 0.3630 0.0072  -0.0721 -0.0369 364 ARG A CB  
2349 C CG  . ARG A 349 ? 0.3759 0.7280 0.3816 0.0134  -0.0780 -0.0464 364 ARG A CG  
2350 C CD  . ARG A 349 ? 0.3875 0.7311 0.3931 0.0099  -0.0864 -0.0520 364 ARG A CD  
2351 N NE  . ARG A 349 ? 0.4126 0.7415 0.4116 0.0160  -0.0935 -0.0623 364 ARG A NE  
2352 C CZ  . ARG A 349 ? 0.4076 0.7363 0.3904 0.0252  -0.0941 -0.0705 364 ARG A CZ  
2353 N NH1 . ARG A 349 ? 0.3995 0.7433 0.3723 0.0286  -0.0874 -0.0684 364 ARG A NH1 
2354 N NH2 . ARG A 349 ? 0.4147 0.7273 0.3908 0.0313  -0.1016 -0.0808 364 ARG A NH2 
2355 N N   . PRO A 350 ? 0.3091 0.7007 0.3115 -0.0009 -0.0645 -0.0261 365 PRO A N   
2356 C CA  . PRO A 350 ? 0.2915 0.6884 0.2976 -0.0062 -0.0619 -0.0192 365 PRO A CA  
2357 C C   . PRO A 350 ? 0.2818 0.6737 0.2978 -0.0108 -0.0644 -0.0174 365 PRO A C   
2358 O O   . PRO A 350 ? 0.2919 0.6799 0.3103 -0.0120 -0.0694 -0.0207 365 PRO A O   
2359 C CB  . PRO A 350 ? 0.2962 0.6976 0.2934 -0.0063 -0.0622 -0.0191 365 PRO A CB  
2360 C CG  . PRO A 350 ? 0.3098 0.7097 0.2973 -0.0006 -0.0643 -0.0257 365 PRO A CG  
2361 C CD  . PRO A 350 ? 0.3161 0.7070 0.3083 0.0018  -0.0679 -0.0313 365 PRO A CD  
2362 N N   . VAL A 351 ? 0.2674 0.6603 0.2893 -0.0131 -0.0611 -0.0119 366 VAL A N   
2363 C CA  . VAL A 351 ? 0.2565 0.6471 0.2877 -0.0170 -0.0614 -0.0083 366 VAL A CA  
2364 C C   . VAL A 351 ? 0.2519 0.6451 0.2851 -0.0194 -0.0634 -0.0080 366 VAL A C   
2365 O O   . VAL A 351 ? 0.2588 0.6509 0.3018 -0.0220 -0.0654 -0.0072 366 VAL A O   
2366 C CB  . VAL A 351 ? 0.2486 0.6411 0.2809 -0.0178 -0.0567 -0.0022 366 VAL A CB  
2367 C CG1 . VAL A 351 ? 0.2518 0.6402 0.2860 -0.0157 -0.0559 -0.0014 366 VAL A CG1 
2368 C CG2 . VAL A 351 ? 0.2401 0.6381 0.2645 -0.0174 -0.0546 -0.0004 366 VAL A CG2 
2369 N N   . SER A 352 ? 0.2501 0.6472 0.2752 -0.0187 -0.0631 -0.0078 367 SER A N   
2370 C CA  . SER A 352 ? 0.2543 0.6532 0.2804 -0.0196 -0.0661 -0.0081 367 SER A CA  
2371 C C   . SER A 352 ? 0.2571 0.6563 0.2727 -0.0174 -0.0691 -0.0116 367 SER A C   
2372 O O   . SER A 352 ? 0.2555 0.6568 0.2635 -0.0171 -0.0676 -0.0090 367 SER A O   
2373 C CB  . SER A 352 ? 0.2517 0.6530 0.2772 -0.0202 -0.0631 -0.0033 367 SER A CB  
2374 O OG  . SER A 352 ? 0.2769 0.6781 0.3093 -0.0212 -0.0597 -0.0001 367 SER A OG  
2375 N N   . PRO A 353 ? 0.2609 0.6570 0.2758 -0.0159 -0.0740 -0.0173 368 PRO A N   
2376 C CA  . PRO A 353 ? 0.2680 0.6639 0.2703 -0.0124 -0.0770 -0.0214 368 PRO A CA  
2377 C C   . PRO A 353 ? 0.2622 0.6606 0.2593 -0.0125 -0.0792 -0.0191 368 PRO A C   
2378 O O   . PRO A 353 ? 0.2630 0.6620 0.2473 -0.0097 -0.0799 -0.0199 368 PRO A O   
2379 C CB  . PRO A 353 ? 0.2816 0.6716 0.2871 -0.0116 -0.0842 -0.0285 368 PRO A CB  
2380 C CG  . PRO A 353 ? 0.2707 0.6601 0.2933 -0.0163 -0.0859 -0.0263 368 PRO A CG  
2381 C CD  . PRO A 353 ? 0.2595 0.6515 0.2864 -0.0179 -0.0782 -0.0199 368 PRO A CD  
2382 N N   . ILE A 354 ? 0.2560 0.6558 0.2628 -0.0150 -0.0800 -0.0160 369 ILE A N   
2383 C CA  . ILE A 354 ? 0.2603 0.6617 0.2629 -0.0144 -0.0810 -0.0126 369 ILE A CA  
2384 C C   . ILE A 354 ? 0.2645 0.6668 0.2723 -0.0161 -0.0759 -0.0073 369 ILE A C   
2385 O O   . ILE A 354 ? 0.2709 0.6748 0.2904 -0.0174 -0.0746 -0.0065 369 ILE A O   
2386 C CB  . ILE A 354 ? 0.2591 0.6618 0.2686 -0.0140 -0.0884 -0.0150 369 ILE A CB  
2387 C CG1 . ILE A 354 ? 0.2714 0.6716 0.2715 -0.0114 -0.0949 -0.0210 369 ILE A CG1 
2388 C CG2 . ILE A 354 ? 0.2579 0.6621 0.2660 -0.0126 -0.0890 -0.0108 369 ILE A CG2 
2389 C CD1 . ILE A 354 ? 0.2843 0.6859 0.2905 -0.0110 -0.1042 -0.0240 369 ILE A CD1 
2390 N N   . LEU A 355 ? 0.2746 0.6754 0.2735 -0.0159 -0.0734 -0.0035 370 LEU A N   
2391 C CA  . LEU A 355 ? 0.2825 0.6819 0.2840 -0.0168 -0.0699 0.0003  370 LEU A CA  
2392 C C   . LEU A 355 ? 0.2971 0.6970 0.3050 -0.0147 -0.0720 0.0012  370 LEU A C   
2393 O O   . LEU A 355 ? 0.3169 0.7188 0.3271 -0.0131 -0.0768 -0.0004 370 LEU A O   
2394 C CB  . LEU A 355 ? 0.2797 0.6756 0.2707 -0.0180 -0.0680 0.0041  370 LEU A CB  
2395 C CG  . LEU A 355 ? 0.2851 0.6838 0.2715 -0.0196 -0.0652 0.0044  370 LEU A CG  
2396 C CD1 . LEU A 355 ? 0.2894 0.6860 0.2690 -0.0223 -0.0636 0.0094  370 LEU A CD1 
2397 C CD2 . LEU A 355 ? 0.2810 0.6820 0.2748 -0.0201 -0.0623 0.0027  370 LEU A CD2 
2398 N N   . ILE A 356 ? 0.3104 0.7089 0.3206 -0.0141 -0.0685 0.0035  371 ILE A N   
2399 C CA  . ILE A 356 ? 0.3237 0.7229 0.3383 -0.0105 -0.0691 0.0046  371 ILE A CA  
2400 C C   . ILE A 356 ? 0.3274 0.7212 0.3320 -0.0088 -0.0734 0.0055  371 ILE A C   
2401 O O   . ILE A 356 ? 0.3494 0.7379 0.3435 -0.0111 -0.0734 0.0069  371 ILE A O   
2402 C CB  . ILE A 356 ? 0.3540 0.7499 0.3665 -0.0087 -0.0644 0.0064  371 ILE A CB  
2403 C CG1 . ILE A 356 ? 0.3579 0.7572 0.3758 -0.0106 -0.0595 0.0068  371 ILE A CG1 
2404 C CG2 . ILE A 356 ? 0.3556 0.7532 0.3725 -0.0031 -0.0639 0.0070  371 ILE A CG2 
2405 C CD1 . ILE A 356 ? 0.3548 0.7477 0.3635 -0.0098 -0.0567 0.0079  371 ILE A CD1 
2406 N N   . PRO A 357 ? 0.3174 0.7128 0.3257 -0.0048 -0.0770 0.0055  372 PRO A N   
2407 C CA  . PRO A 357 ? 0.3137 0.7025 0.3109 -0.0031 -0.0817 0.0072  372 PRO A CA  
2408 C C   . PRO A 357 ? 0.3096 0.6871 0.2956 -0.0033 -0.0803 0.0102  372 PRO A C   
2409 O O   . PRO A 357 ? 0.3097 0.6843 0.2972 -0.0018 -0.0774 0.0100  372 PRO A O   
2410 C CB  . PRO A 357 ? 0.3156 0.7087 0.3207 0.0025  -0.0859 0.0068  372 PRO A CB  
2411 C CG  . PRO A 357 ? 0.3074 0.7124 0.3294 0.0016  -0.0846 0.0046  372 PRO A CG  
2412 C CD  . PRO A 357 ? 0.3040 0.7084 0.3270 -0.0017 -0.0775 0.0049  372 PRO A CD  
2413 N N   . HIS A 358 ? 0.3206 0.6916 0.2953 -0.0054 -0.0825 0.0131  373 HIS A N   
2414 C CA  . HIS A 358 ? 0.3268 0.6852 0.2918 -0.0061 -0.0833 0.0168  373 HIS A CA  
2415 C C   . HIS A 358 ? 0.3528 0.7046 0.3135 -0.0008 -0.0886 0.0186  373 HIS A C   
2416 O O   . HIS A 358 ? 0.3751 0.7287 0.3313 -0.0002 -0.0921 0.0203  373 HIS A O   
2417 C CB  . HIS A 358 ? 0.3232 0.6791 0.2797 -0.0122 -0.0823 0.0208  373 HIS A CB  
2418 C CG  . HIS A 358 ? 0.3177 0.6765 0.2770 -0.0172 -0.0779 0.0203  373 HIS A CG  
2419 N ND1 . HIS A 358 ? 0.3100 0.6794 0.2767 -0.0178 -0.0745 0.0167  373 HIS A ND1 
2420 C CD2 . HIS A 358 ? 0.3123 0.6648 0.2688 -0.0217 -0.0772 0.0229  373 HIS A CD2 
2421 C CE1 . HIS A 358 ? 0.2946 0.6646 0.2624 -0.0217 -0.0716 0.0173  373 HIS A CE1 
2422 N NE2 . HIS A 358 ? 0.3051 0.6657 0.2672 -0.0244 -0.0733 0.0209  373 HIS A NE2 
2423 N N   . VAL A 359 ? 0.3622 0.7053 0.3222 0.0038  -0.0898 0.0183  374 VAL A N   
2424 C CA  . VAL A 359 ? 0.3816 0.7174 0.3378 0.0103  -0.0952 0.0200  374 VAL A CA  
2425 C C   . VAL A 359 ? 0.4253 0.7434 0.3681 0.0085  -0.0987 0.0252  374 VAL A C   
2426 O O   . VAL A 359 ? 0.4634 0.7712 0.4016 0.0045  -0.0976 0.0261  374 VAL A O   
2427 C CB  . VAL A 359 ? 0.3718 0.7093 0.3358 0.0189  -0.0948 0.0166  374 VAL A CB  
2428 C CG1 . VAL A 359 ? 0.3887 0.7197 0.3497 0.0267  -0.1010 0.0184  374 VAL A CG1 
2429 C CG2 . VAL A 359 ? 0.3549 0.7114 0.3346 0.0197  -0.0915 0.0132  374 VAL A CG2 
2430 N N   . ALA A 360 ? 0.4578 0.7719 0.3946 0.0114  -0.1038 0.0290  375 ALA A N   
2431 C CA  . ALA A 360 ? 0.4942 0.7909 0.4183 0.0096  -0.1077 0.0356  375 ALA A CA  
2432 C C   . ALA A 360 ? 0.5317 0.8119 0.4532 0.0159  -0.1112 0.0345  375 ALA A C   
2433 O O   . ALA A 360 ? 0.5349 0.8132 0.4574 0.0252  -0.1153 0.0336  375 ALA A O   
2434 C CB  . ALA A 360 ? 0.5104 0.8081 0.4277 0.0121  -0.1122 0.0403  375 ALA A CB  
2435 N N   . MET A 361 ? 0.5634 0.8310 0.4809 0.0110  -0.1103 0.0345  376 MET A N   
2436 C CA  . MET A 361 ? 0.6114 0.8606 0.5243 0.0168  -0.1139 0.0319  376 MET A CA  
2437 C C   . MET A 361 ? 0.6560 0.8847 0.5586 0.0210  -0.1213 0.0371  376 MET A C   
2438 O O   . MET A 361 ? 0.7085 0.9224 0.6075 0.0297  -0.1251 0.0338  376 MET A O   
2439 C CB  . MET A 361 ? 0.6527 0.8919 0.5623 0.0089  -0.1131 0.0312  376 MET A CB  
2440 C CG  . MET A 361 ? 0.6514 0.9068 0.5692 0.0060  -0.1066 0.0259  376 MET A CG  
2441 S SD  . MET A 361 ? 0.6525 0.9065 0.5717 0.0171  -0.1048 0.0170  376 MET A SD  
2442 C CE  . MET A 361 ? 0.6655 0.8902 0.5712 0.0160  -0.1117 0.0156  376 MET A CE  
2443 N N   . GLN A 362 ? 0.6547 0.8813 0.5516 0.0152  -0.1232 0.0454  377 GLN A N   
2444 C CA  . GLN A 362 ? 0.6631 0.8695 0.5493 0.0177  -0.1302 0.0524  377 GLN A CA  
2445 C C   . GLN A 362 ? 0.6474 0.8646 0.5303 0.0158  -0.1300 0.0593  377 GLN A C   
2446 O O   . GLN A 362 ? 0.6354 0.8722 0.5233 0.0111  -0.1247 0.0583  377 GLN A O   
2447 C CB  . GLN A 362 ? 0.6940 0.8789 0.5729 0.0078  -0.1328 0.0579  377 GLN A CB  
2448 C CG  . GLN A 362 ? 0.7053 0.8980 0.5834 -0.0056 -0.1288 0.0667  377 GLN A CG  
2449 C CD  . GLN A 362 ? 0.7483 0.9243 0.6243 -0.0173 -0.1309 0.0720  377 GLN A CD  
2450 O OE1 . GLN A 362 ? 0.7836 0.9456 0.6601 -0.0171 -0.1344 0.0662  377 GLN A OE1 
2451 N NE2 . GLN A 362 ? 0.7551 0.9334 0.6289 -0.0276 -0.1288 0.0831  377 GLN A NE2 
2452 N N   . ASP A 363 ? 0.6502 0.8540 0.5233 0.0199  -0.1362 0.0664  378 ASP A N   
2453 C CA  . ASP A 363 ? 0.6477 0.8609 0.5144 0.0184  -0.1362 0.0734  378 ASP A CA  
2454 C C   . ASP A 363 ? 0.6280 0.8433 0.4908 0.0050  -0.1306 0.0805  378 ASP A C   
2455 O O   . ASP A 363 ? 0.6321 0.8303 0.4908 -0.0022 -0.1317 0.0869  378 ASP A O   
2456 C CB  . ASP A 363 ? 0.6871 0.8834 0.5418 0.0251  -0.1442 0.0813  378 ASP A CB  
2457 C CG  . ASP A 363 ? 0.6973 0.8956 0.5571 0.0398  -0.1501 0.0749  378 ASP A CG  
2458 O OD1 . ASP A 363 ? 0.6725 0.8903 0.5454 0.0444  -0.1475 0.0657  378 ASP A OD1 
2459 O OD2 . ASP A 363 ? 0.7569 0.9373 0.6083 0.0470  -0.1574 0.0799  378 ASP A OD2 
2460 N N   . THR A 364 ? 0.6101 0.8466 0.4752 0.0018  -0.1250 0.0793  379 THR A N   
2461 C CA  . THR A 364 ? 0.6134 0.8558 0.4757 -0.0092 -0.1187 0.0862  379 THR A CA  
2462 C C   . THR A 364 ? 0.6016 0.8586 0.4553 -0.0080 -0.1160 0.0900  379 THR A C   
2463 O O   . THR A 364 ? 0.6137 0.8690 0.4591 -0.0001 -0.1213 0.0912  379 THR A O   
2464 C CB  . THR A 364 ? 0.6066 0.8604 0.4813 -0.0153 -0.1125 0.0793  379 THR A CB  
2465 O OG1 . THR A 364 ? 0.6403 0.9054 0.5136 -0.0241 -0.1058 0.0855  379 THR A OG1 
2466 C CG2 . THR A 364 ? 0.5780 0.8482 0.4624 -0.0086 -0.1112 0.0676  379 THR A CG2 
2467 N N   . SER A 365 ? 0.5852 0.8563 0.4400 -0.0150 -0.1083 0.0916  380 SER A N   
2468 C CA  . SER A 365 ? 0.6056 0.8895 0.4495 -0.0136 -0.1050 0.0952  380 SER A CA  
2469 C C   . SER A 365 ? 0.5914 0.8951 0.4435 -0.0162 -0.0977 0.0880  380 SER A C   
2470 O O   . SER A 365 ? 0.5702 0.8766 0.4353 -0.0208 -0.0948 0.0832  380 SER A O   
2471 C CB  . SER A 365 ? 0.6215 0.8987 0.4532 -0.0200 -0.1018 0.1104  380 SER A CB  
2472 O OG  . SER A 365 ? 0.6040 0.8958 0.4396 -0.0277 -0.0922 0.1132  380 SER A OG  
2473 N N   . LEU A 366 ? 0.6071 0.9235 0.4502 -0.0125 -0.0953 0.0867  381 LEU A N   
2474 C CA  . LEU A 366 ? 0.6101 0.9438 0.4590 -0.0135 -0.0889 0.0796  381 LEU A CA  
2475 C C   . LEU A 366 ? 0.6191 0.9608 0.4510 -0.0089 -0.0870 0.0822  381 LEU A C   
2476 O O   . LEU A 366 ? 0.6186 0.9546 0.4384 -0.0025 -0.0936 0.0834  381 LEU A O   
2477 C CB  . LEU A 366 ? 0.6074 0.9465 0.4693 -0.0092 -0.0925 0.0662  381 LEU A CB  
2478 C CG  . LEU A 366 ? 0.6164 0.9669 0.4913 -0.0130 -0.0863 0.0594  381 LEU A CG  
2479 C CD1 . LEU A 366 ? 0.6253 0.9789 0.5121 -0.0087 -0.0907 0.0481  381 LEU A CD1 
2480 C CD2 . LEU A 366 ? 0.6224 0.9860 0.4903 -0.0129 -0.0799 0.0593  381 LEU A CD2 
2481 N N   . GLY A 367 ? 0.6385 0.9930 0.4680 -0.0114 -0.0783 0.0837  382 GLY A N   
2482 C CA  . GLY A 367 ? 0.6883 1.0483 0.4978 -0.0077 -0.0745 0.0904  382 GLY A CA  
2483 C C   . GLY A 367 ? 0.7243 1.0709 0.5261 -0.0117 -0.0757 0.1051  382 GLY A C   
2484 O O   . GLY A 367 ? 0.7937 1.1320 0.6081 -0.0198 -0.0754 0.1100  382 GLY A O   
2485 N N   . GLY A 368 ? 0.6971 1.0396 0.4781 -0.0061 -0.0781 0.1118  383 GLY A N   
2486 C CA  . GLY A 368 ? 0.7148 1.0411 0.4879 -0.0088 -0.0814 0.1255  383 GLY A CA  
2487 C C   . GLY A 368 ? 0.7264 1.0385 0.4971 -0.0016 -0.0942 0.1208  383 GLY A C   
2488 O O   . GLY A 368 ? 0.7742 1.0737 0.5308 0.0011  -0.0989 0.1306  383 GLY A O   
2489 N N   . HIS A 369 ? 0.6853 1.0005 0.4703 0.0019  -0.0996 0.1064  384 HIS A N   
2490 C CA  . HIS A 369 ? 0.6610 0.9692 0.4456 0.0104  -0.1112 0.0999  384 HIS A CA  
2491 C C   . HIS A 369 ? 0.6361 0.9338 0.4385 0.0082  -0.1150 0.0971  384 HIS A C   
2492 O O   . HIS A 369 ? 0.6251 0.9267 0.4431 0.0024  -0.1102 0.0921  384 HIS A O   
2493 C CB  . HIS A 369 ? 0.6415 0.9634 0.4299 0.0165  -0.1146 0.0857  384 HIS A CB  
2494 C CG  . HIS A 369 ? 0.6631 0.9955 0.4339 0.0197  -0.1108 0.0853  384 HIS A CG  
2495 N ND1 . HIS A 369 ? 0.7107 1.0413 0.4604 0.0279  -0.1173 0.0869  384 HIS A ND1 
2496 C CD2 . HIS A 369 ? 0.6657 1.0103 0.4357 0.0170  -0.1013 0.0828  384 HIS A CD2 
2497 C CE1 . HIS A 369 ? 0.7189 1.0596 0.4540 0.0303  -0.1118 0.0852  384 HIS A CE1 
2498 N NE2 . HIS A 369 ? 0.7022 1.0517 0.4498 0.0240  -0.1018 0.0826  384 HIS A NE2 
2499 N N   . SER A 370 ? 0.6355 0.9198 0.4346 0.0139  -0.1238 0.0998  385 SER A N   
2500 C CA  . SER A 370 ? 0.6419 0.9143 0.4551 0.0133  -0.1271 0.0974  385 SER A CA  
2501 C C   . SER A 370 ? 0.6174 0.9019 0.4486 0.0171  -0.1289 0.0829  385 SER A C   
2502 O O   . SER A 370 ? 0.6331 0.9305 0.4647 0.0222  -0.1319 0.0758  385 SER A O   
2503 C CB  . SER A 370 ? 0.6680 0.9219 0.4723 0.0197  -0.1361 0.1045  385 SER A CB  
2504 O OG  . SER A 370 ? 0.6685 0.9256 0.4809 0.0296  -0.1443 0.0955  385 SER A OG  
2505 N N   . VAL A 371 ? 0.5912 0.8713 0.4367 0.0143  -0.1271 0.0789  386 VAL A N   
2506 C CA  . VAL A 371 ? 0.5647 0.8566 0.4278 0.0168  -0.1268 0.0669  386 VAL A CA  
2507 C C   . VAL A 371 ? 0.5746 0.8554 0.4466 0.0216  -0.1307 0.0645  386 VAL A C   
2508 O O   . VAL A 371 ? 0.5661 0.8365 0.4411 0.0170  -0.1276 0.0655  386 VAL A O   
2509 C CB  . VAL A 371 ? 0.5255 0.8276 0.3973 0.0087  -0.1180 0.0627  386 VAL A CB  
2510 C CG1 . VAL A 371 ? 0.4948 0.8089 0.3836 0.0115  -0.1177 0.0515  386 VAL A CG1 
2511 C CG2 . VAL A 371 ? 0.5217 0.8340 0.3837 0.0051  -0.1133 0.0654  386 VAL A CG2 
2512 N N   . PRO A 372 ? 0.5714 0.8545 0.4476 0.0314  -0.1378 0.0610  387 PRO A N   
2513 C CA  . PRO A 372 ? 0.5692 0.8430 0.4533 0.0386  -0.1414 0.0585  387 PRO A CA  
2514 C C   . PRO A 372 ? 0.5381 0.8147 0.4351 0.0358  -0.1352 0.0518  387 PRO A C   
2515 O O   . PRO A 372 ? 0.5149 0.8073 0.4211 0.0316  -0.1300 0.0463  387 PRO A O   
2516 C CB  . PRO A 372 ? 0.5598 0.8469 0.4530 0.0485  -0.1480 0.0535  387 PRO A CB  
2517 C CG  . PRO A 372 ? 0.5758 0.8713 0.4595 0.0471  -0.1510 0.0557  387 PRO A CG  
2518 C CD  . PRO A 372 ? 0.5669 0.8628 0.4415 0.0367  -0.1433 0.0585  387 PRO A CD  
2519 N N   . LYS A 373 ? 0.5418 0.8021 0.4381 0.0388  -0.1362 0.0520  388 LYS A N   
2520 C CA  . LYS A 373 ? 0.5406 0.8034 0.4478 0.0399  -0.1317 0.0446  388 LYS A CA  
2521 C C   . LYS A 373 ? 0.5206 0.8068 0.4443 0.0448  -0.1297 0.0373  388 LYS A C   
2522 O O   . LYS A 373 ? 0.5515 0.8474 0.4795 0.0509  -0.1347 0.0372  388 LYS A O   
2523 C CB  . LYS A 373 ? 0.5674 0.8105 0.4710 0.0482  -0.1358 0.0440  388 LYS A CB  
2524 C CG  . LYS A 373 ? 0.5842 0.8295 0.4962 0.0513  -0.1310 0.0360  388 LYS A CG  
2525 C CD  . LYS A 373 ? 0.6230 0.8438 0.5268 0.0583  -0.1348 0.0348  388 LYS A CD  
2526 C CE  . LYS A 373 ? 0.6353 0.8631 0.5475 0.0669  -0.1303 0.0259  388 LYS A CE  
2527 N NZ  . LYS A 373 ? 0.6753 0.8805 0.5791 0.0776  -0.1343 0.0227  388 LYS A NZ  
2528 N N   . GLY A 374 ? 0.4825 0.7780 0.4159 0.0417  -0.1230 0.0318  389 GLY A N   
2529 C CA  . GLY A 374 ? 0.4526 0.7698 0.4032 0.0450  -0.1204 0.0261  389 GLY A CA  
2530 C C   . GLY A 374 ? 0.4357 0.7693 0.3916 0.0383  -0.1193 0.0251  389 GLY A C   
2531 O O   . GLY A 374 ? 0.4195 0.7697 0.3907 0.0385  -0.1166 0.0206  389 GLY A O   
2532 N N   . THR A 375 ? 0.4356 0.7644 0.3789 0.0326  -0.1212 0.0292  390 THR A N   
2533 C CA  . THR A 375 ? 0.4337 0.7757 0.3787 0.0277  -0.1208 0.0274  390 THR A CA  
2534 C C   . THR A 375 ? 0.4203 0.7704 0.3734 0.0211  -0.1131 0.0234  390 THR A C   
2535 O O   . THR A 375 ? 0.3836 0.7258 0.3330 0.0170  -0.1082 0.0246  390 THR A O   
2536 C CB  . THR A 375 ? 0.4482 0.7827 0.3751 0.0239  -0.1225 0.0333  390 THR A CB  
2537 O OG1 . THR A 375 ? 0.4957 0.8219 0.4136 0.0303  -0.1300 0.0379  390 THR A OG1 
2538 C CG2 . THR A 375 ? 0.4395 0.7862 0.3655 0.0209  -0.1225 0.0303  390 THR A CG2 
2539 N N   . ARG A 376 ? 0.4191 0.7841 0.3833 0.0200  -0.1133 0.0187  391 ARG A N   
2540 C CA  . ARG A 376 ? 0.4233 0.7957 0.3955 0.0143  -0.1068 0.0152  391 ARG A CA  
2541 C C   . ARG A 376 ? 0.4101 0.7831 0.3725 0.0089  -0.1058 0.0153  391 ARG A C   
2542 O O   . ARG A 376 ? 0.4356 0.8106 0.3917 0.0106  -0.1111 0.0150  391 ARG A O   
2543 C CB  . ARG A 376 ? 0.4413 0.8284 0.4326 0.0158  -0.1076 0.0105  391 ARG A CB  
2544 C CG  . ARG A 376 ? 0.4774 0.8674 0.4801 0.0218  -0.1062 0.0106  391 ARG A CG  
2545 C CD  . ARG A 376 ? 0.5233 0.9297 0.5473 0.0220  -0.1046 0.0078  391 ARG A CD  
2546 N NE  . ARG A 376 ? 0.6369 1.0462 0.6695 0.0283  -0.1004 0.0087  391 ARG A NE  
2547 C CZ  . ARG A 376 ? 0.7074 1.1315 0.7589 0.0297  -0.0964 0.0081  391 ARG A CZ  
2548 N NH1 . ARG A 376 ? 0.7258 1.1621 0.7916 0.0238  -0.0971 0.0068  391 ARG A NH1 
2549 N NH2 . ARG A 376 ? 0.6911 1.1174 0.7472 0.0371  -0.0916 0.0090  391 ARG A NH2 
2550 N N   . VAL A 377 ? 0.3889 0.7607 0.3495 0.0034  -0.0993 0.0155  392 VAL A N   
2551 C CA  . VAL A 377 ? 0.3798 0.7532 0.3309 -0.0006 -0.0971 0.0161  392 VAL A CA  
2552 C C   . VAL A 377 ? 0.3585 0.7398 0.3187 -0.0039 -0.0927 0.0113  392 VAL A C   
2553 O O   . VAL A 377 ? 0.3526 0.7331 0.3174 -0.0068 -0.0875 0.0118  392 VAL A O   
2554 C CB  . VAL A 377 ? 0.3821 0.7468 0.3212 -0.0043 -0.0936 0.0228  392 VAL A CB  
2555 C CG1 . VAL A 377 ? 0.3878 0.7579 0.3204 -0.0080 -0.0892 0.0235  392 VAL A CG1 
2556 C CG2 . VAL A 377 ? 0.3939 0.7490 0.3216 -0.0015 -0.0984 0.0286  392 VAL A CG2 
2557 N N   . LEU A 378 ? 0.3450 0.7326 0.3068 -0.0032 -0.0955 0.0066  393 LEU A N   
2558 C CA  . LEU A 378 ? 0.3256 0.7185 0.2954 -0.0058 -0.0924 0.0020  393 LEU A CA  
2559 C C   . LEU A 378 ? 0.3253 0.7181 0.2840 -0.0076 -0.0879 0.0027  393 LEU A C   
2560 O O   . LEU A 378 ? 0.3433 0.7358 0.2894 -0.0054 -0.0900 0.0027  393 LEU A O   
2561 C CB  . LEU A 378 ? 0.3238 0.7219 0.3022 -0.0043 -0.0987 -0.0039 393 LEU A CB  
2562 C CG  . LEU A 378 ? 0.3250 0.7270 0.3182 -0.0026 -0.1025 -0.0037 393 LEU A CG  
2563 C CD1 . LEU A 378 ? 0.3301 0.7386 0.3357 -0.0030 -0.1091 -0.0091 393 LEU A CD1 
2564 C CD2 . LEU A 378 ? 0.3128 0.7159 0.3164 -0.0039 -0.0957 -0.0012 393 LEU A CD2 
2565 N N   . VAL A 379 ? 0.3146 0.7083 0.2775 -0.0108 -0.0817 0.0037  394 VAL A N   
2566 C CA  . VAL A 379 ? 0.3059 0.7022 0.2614 -0.0121 -0.0769 0.0047  394 VAL A CA  
2567 C C   . VAL A 379 ? 0.3023 0.7022 0.2619 -0.0106 -0.0772 -0.0020 394 VAL A C   
2568 O O   . VAL A 379 ? 0.2796 0.6799 0.2512 -0.0119 -0.0772 -0.0047 394 VAL A O   
2569 C CB  . VAL A 379 ? 0.2947 0.6905 0.2531 -0.0162 -0.0713 0.0093  394 VAL A CB  
2570 C CG1 . VAL A 379 ? 0.2987 0.7009 0.2550 -0.0170 -0.0661 0.0093  394 VAL A CG1 
2571 C CG2 . VAL A 379 ? 0.2994 0.6894 0.2509 -0.0181 -0.0717 0.0162  394 VAL A CG2 
2572 N N   . ASN A 380 ? 0.3223 0.7238 0.2707 -0.0075 -0.0777 -0.0045 395 ASN A N   
2573 C CA  . ASN A 380 ? 0.3304 0.7325 0.2803 -0.0049 -0.0795 -0.0121 395 ASN A CA  
2574 C C   . ASN A 380 ? 0.3413 0.7473 0.2904 -0.0046 -0.0724 -0.0118 395 ASN A C   
2575 O O   . ASN A 380 ? 0.3366 0.7465 0.2744 -0.0015 -0.0688 -0.0110 395 ASN A O   
2576 C CB  . ASN A 380 ? 0.3362 0.7365 0.2730 0.0001  -0.0856 -0.0170 395 ASN A CB  
2577 C CG  . ASN A 380 ? 0.3381 0.7357 0.2768 0.0027  -0.0899 -0.0263 395 ASN A CG  
2578 O OD1 . ASN A 380 ? 0.3293 0.7265 0.2784 0.0010  -0.0872 -0.0283 395 ASN A OD1 
2579 N ND2 . ASN A 380 ? 0.3485 0.7429 0.2763 0.0070  -0.0974 -0.0322 395 ASN A ND2 
2580 N N   . MET A 381 ? 0.3698 0.7758 0.3317 -0.0074 -0.0704 -0.0120 396 MET A N   
2581 C CA  . MET A 381 ? 0.3952 0.8055 0.3595 -0.0074 -0.0643 -0.0108 396 MET A CA  
2582 C C   . MET A 381 ? 0.3820 0.7923 0.3414 -0.0018 -0.0645 -0.0176 396 MET A C   
2583 O O   . MET A 381 ? 0.4045 0.8207 0.3608 0.0008  -0.0590 -0.0167 396 MET A O   
2584 C CB  . MET A 381 ? 0.4227 0.8316 0.4004 -0.0112 -0.0631 -0.0091 396 MET A CB  
2585 C CG  . MET A 381 ? 0.4901 0.9043 0.4701 -0.0123 -0.0574 -0.0053 396 MET A CG  
2586 S SD  . MET A 381 ? 0.5755 0.9901 0.5584 -0.0179 -0.0556 0.0023  396 MET A SD  
2587 C CE  . MET A 381 ? 0.5714 0.9872 0.5430 -0.0186 -0.0556 0.0066  396 MET A CE  
2588 N N   . TRP A 382 ? 0.3724 0.7762 0.3316 0.0002  -0.0712 -0.0246 397 TRP A N   
2589 C CA  . TRP A 382 ? 0.3692 0.7695 0.3221 0.0063  -0.0730 -0.0325 397 TRP A CA  
2590 C C   . TRP A 382 ? 0.3825 0.7872 0.3169 0.0124  -0.0705 -0.0334 397 TRP A C   
2591 O O   . TRP A 382 ? 0.4002 0.8085 0.3285 0.0181  -0.0659 -0.0356 397 TRP A O   
2592 C CB  . TRP A 382 ? 0.3743 0.7653 0.3316 0.0059  -0.0826 -0.0397 397 TRP A CB  
2593 C CG  . TRP A 382 ? 0.3906 0.7746 0.3397 0.0123  -0.0865 -0.0492 397 TRP A CG  
2594 C CD1 . TRP A 382 ? 0.4052 0.7873 0.3362 0.0192  -0.0895 -0.0552 397 TRP A CD1 
2595 C CD2 . TRP A 382 ? 0.3927 0.7689 0.3497 0.0131  -0.0883 -0.0540 397 TRP A CD2 
2596 N NE1 . TRP A 382 ? 0.4227 0.7958 0.3494 0.0249  -0.0932 -0.0645 397 TRP A NE1 
2597 C CE2 . TRP A 382 ? 0.4149 0.7836 0.3581 0.0210  -0.0928 -0.0638 397 TRP A CE2 
2598 C CE3 . TRP A 382 ? 0.3865 0.7602 0.3597 0.0084  -0.0867 -0.0508 397 TRP A CE3 
2599 C CZ2 . TRP A 382 ? 0.4278 0.7855 0.3738 0.0243  -0.0963 -0.0708 397 TRP A CZ2 
2600 C CZ3 . TRP A 382 ? 0.3994 0.7629 0.3758 0.0111  -0.0898 -0.0566 397 TRP A CZ3 
2601 C CH2 . TRP A 382 ? 0.4146 0.7696 0.3778 0.0189  -0.0947 -0.0667 397 TRP A CH2 
2602 N N   . ALA A 383 ? 0.3806 0.7858 0.3062 0.0119  -0.0731 -0.0308 398 ALA A N   
2603 C CA  . ALA A 383 ? 0.3879 0.7971 0.2942 0.0177  -0.0707 -0.0301 398 ALA A CA  
2604 C C   . ALA A 383 ? 0.3870 0.8074 0.2918 0.0182  -0.0598 -0.0230 398 ALA A C   
2605 O O   . ALA A 383 ? 0.3997 0.8252 0.2945 0.0253  -0.0550 -0.0256 398 ALA A O   
2606 C CB  . ALA A 383 ? 0.3917 0.7993 0.2909 0.0158  -0.0750 -0.0258 398 ALA A CB  
2607 N N   . ILE A 384 ? 0.3833 0.8078 0.2984 0.0110  -0.0560 -0.0141 399 ILE A N   
2608 C CA  . ILE A 384 ? 0.3860 0.8222 0.3020 0.0097  -0.0467 -0.0059 399 ILE A CA  
2609 C C   . ILE A 384 ? 0.3794 0.8218 0.3038 0.0127  -0.0420 -0.0090 399 ILE A C   
2610 O O   . ILE A 384 ? 0.3799 0.8347 0.3032 0.0150  -0.0341 -0.0045 399 ILE A O   
2611 C CB  . ILE A 384 ? 0.3721 0.8093 0.2973 0.0008  -0.0453 0.0036  399 ILE A CB  
2612 C CG1 . ILE A 384 ? 0.3627 0.7931 0.3027 -0.0037 -0.0496 0.0013  399 ILE A CG1 
2613 C CG2 . ILE A 384 ? 0.3798 0.8126 0.2945 -0.0009 -0.0481 0.0087  399 ILE A CG2 
2614 C CD1 . ILE A 384 ? 0.3729 0.8050 0.3220 -0.0111 -0.0474 0.0092  399 ILE A CD1 
2615 N N   . HIS A 385 ? 0.3673 0.8015 0.3003 0.0131  -0.0469 -0.0159 400 HIS A N   
2616 C CA  . HIS A 385 ? 0.3766 0.8138 0.3157 0.0175  -0.0439 -0.0197 400 HIS A CA  
2617 C C   . HIS A 385 ? 0.3903 0.8237 0.3181 0.0276  -0.0453 -0.0293 400 HIS A C   
2618 O O   . HIS A 385 ? 0.3902 0.8266 0.3210 0.0333  -0.0421 -0.0324 400 HIS A O   
2619 C CB  . HIS A 385 ? 0.3746 0.8045 0.3287 0.0127  -0.0477 -0.0207 400 HIS A CB  
2620 C CG  . HIS A 385 ? 0.3678 0.8032 0.3325 0.0052  -0.0449 -0.0121 400 HIS A CG  
2621 N ND1 . HIS A 385 ? 0.3773 0.8064 0.3527 0.0001  -0.0480 -0.0112 400 HIS A ND1 
2622 C CD2 . HIS A 385 ? 0.3627 0.8087 0.3283 0.0019  -0.0397 -0.0041 400 HIS A CD2 
2623 C CE1 . HIS A 385 ? 0.3740 0.8084 0.3548 -0.0052 -0.0454 -0.0041 400 HIS A CE1 
2624 N NE2 . HIS A 385 ? 0.3547 0.7990 0.3308 -0.0049 -0.0410 0.0002  400 HIS A NE2 
2625 N N   . HIS A 386 ? 0.3933 0.8192 0.3074 0.0306  -0.0508 -0.0345 401 HIS A N   
2626 C CA  . HIS A 386 ? 0.4055 0.8262 0.3056 0.0410  -0.0531 -0.0446 401 HIS A CA  
2627 C C   . HIS A 386 ? 0.4290 0.8559 0.3086 0.0474  -0.0496 -0.0438 401 HIS A C   
2628 O O   . HIS A 386 ? 0.4715 0.8922 0.3349 0.0568  -0.0529 -0.0532 401 HIS A O   
2629 C CB  . HIS A 386 ? 0.4055 0.8094 0.3070 0.0402  -0.0648 -0.0539 401 HIS A CB  
2630 C CG  . HIS A 386 ? 0.3975 0.7943 0.3149 0.0379  -0.0671 -0.0566 401 HIS A CG  
2631 N ND1 . HIS A 386 ? 0.3811 0.7806 0.3162 0.0292  -0.0651 -0.0492 401 HIS A ND1 
2632 C CD2 . HIS A 386 ? 0.4104 0.7967 0.3274 0.0439  -0.0709 -0.0656 401 HIS A CD2 
2633 C CE1 . HIS A 386 ? 0.3871 0.7788 0.3321 0.0296  -0.0674 -0.0526 401 HIS A CE1 
2634 N NE2 . HIS A 386 ? 0.3995 0.7827 0.3345 0.0382  -0.0710 -0.0624 401 HIS A NE2 
2635 N N   . ASP A 387 ? 0.4249 0.8633 0.3039 0.0428  -0.0430 -0.0326 402 ASP A N   
2636 C CA  . ASP A 387 ? 0.4474 0.8921 0.3059 0.0485  -0.0389 -0.0299 402 ASP A CA  
2637 C C   . ASP A 387 ? 0.4664 0.9230 0.3146 0.0598  -0.0292 -0.0315 402 ASP A C   
2638 O O   . ASP A 387 ? 0.4419 0.9137 0.3014 0.0581  -0.0195 -0.0237 402 ASP A O   
2639 C CB  . ASP A 387 ? 0.4408 0.8933 0.3019 0.0400  -0.0346 -0.0163 402 ASP A CB  
2640 C CG  . ASP A 387 ? 0.4686 0.9245 0.3071 0.0452  -0.0319 -0.0126 402 ASP A CG  
2641 O OD1 . ASP A 387 ? 0.4915 0.9472 0.3114 0.0565  -0.0313 -0.0201 402 ASP A OD1 
2642 O OD2 . ASP A 387 ? 0.4796 0.9372 0.3172 0.0387  -0.0308 -0.0022 402 ASP A OD2 
2643 N N   . PRO A 388 ? 0.4935 0.9440 0.3200 0.0717  -0.0319 -0.0418 403 PRO A N   
2644 C CA  . PRO A 388 ? 0.5196 0.9807 0.3332 0.0852  -0.0226 -0.0451 403 PRO A CA  
2645 C C   . PRO A 388 ? 0.5337 1.0161 0.3405 0.0865  -0.0089 -0.0320 403 PRO A C   
2646 O O   . PRO A 388 ? 0.5224 1.0206 0.3270 0.0954  0.0023  -0.0304 403 PRO A O   
2647 C CB  . PRO A 388 ? 0.5395 0.9852 0.3282 0.0964  -0.0314 -0.0592 403 PRO A CB  
2648 C CG  . PRO A 388 ? 0.5379 0.9728 0.3226 0.0884  -0.0417 -0.0579 403 PRO A CG  
2649 C CD  . PRO A 388 ? 0.5026 0.9360 0.3147 0.0738  -0.0446 -0.0513 403 PRO A CD  
2650 N N   . LYS A 389 ? 0.5423 1.0251 0.3466 0.0778  -0.0097 -0.0221 404 LYS A N   
2651 C CA  . LYS A 389 ? 0.5631 1.0645 0.3669 0.0746  0.0023  -0.0068 404 LYS A CA  
2652 C C   . LYS A 389 ? 0.5338 1.0504 0.3645 0.0668  0.0100  0.0022  404 LYS A C   
2653 O O   . LYS A 389 ? 0.5225 1.0589 0.3559 0.0677  0.0219  0.0123  404 LYS A O   
2654 C CB  . LYS A 389 ? 0.5933 1.0876 0.3929 0.0650  -0.0027 0.0020  404 LYS A CB  
2655 C CG  . LYS A 389 ? 0.6329 1.1417 0.4220 0.0641  0.0081  0.0171  404 LYS A CG  
2656 C CD  . LYS A 389 ? 0.6796 1.1793 0.4394 0.0705  0.0038  0.0159  404 LYS A CD  
2657 C CE  . LYS A 389 ? 0.7171 1.2273 0.4694 0.0658  0.0126  0.0339  404 LYS A CE  
2658 N NZ  . LYS A 389 ? 0.7632 1.2712 0.4814 0.0769  0.0133  0.0339  404 LYS A NZ  
2659 N N   . HIS A 390 ? 0.5275 1.0355 0.3786 0.0587  0.0029  -0.0007 405 HIS A N   
2660 C CA  . HIS A 390 ? 0.4865 1.0081 0.3623 0.0508  0.0086  0.0078  405 HIS A CA  
2661 C C   . HIS A 390 ? 0.4671 0.9905 0.3553 0.0564  0.0085  -0.0003 405 HIS A C   
2662 O O   . HIS A 390 ? 0.4609 0.9978 0.3677 0.0522  0.0135  0.0062  405 HIS A O   
2663 C CB  . HIS A 390 ? 0.4635 0.9766 0.3534 0.0359  0.0021  0.0146  405 HIS A CB  
2664 C CG  . HIS A 390 ? 0.4867 0.9990 0.3666 0.0301  0.0029  0.0246  405 HIS A CG  
2665 N ND1 . HIS A 390 ? 0.5046 1.0334 0.3872 0.0259  0.0126  0.0386  405 HIS A ND1 
2666 C CD2 . HIS A 390 ? 0.5042 1.0014 0.3707 0.0287  -0.0048 0.0231  405 HIS A CD2 
2667 C CE1 . HIS A 390 ? 0.5107 1.0327 0.3813 0.0217  0.0107  0.0456  405 HIS A CE1 
2668 N NE2 . HIS A 390 ? 0.5094 1.0124 0.3699 0.0239  0.0000  0.0362  405 HIS A NE2 
2669 N N   . TRP A 391 ? 0.4791 0.9885 0.3572 0.0659  0.0024  -0.0142 406 TRP A N   
2670 C CA  . TRP A 391 ? 0.4763 0.9836 0.3658 0.0712  0.0010  -0.0218 406 TRP A CA  
2671 C C   . TRP A 391 ? 0.5219 1.0255 0.3933 0.0878  0.0020  -0.0338 406 TRP A C   
2672 O O   . TRP A 391 ? 0.5434 1.0324 0.3952 0.0925  -0.0045 -0.0422 406 TRP A O   
2673 C CB  . TRP A 391 ? 0.4558 0.9426 0.3549 0.0638  -0.0110 -0.0277 406 TRP A CB  
2674 C CG  . TRP A 391 ? 0.4340 0.9204 0.3489 0.0489  -0.0136 -0.0183 406 TRP A CG  
2675 C CD1 . TRP A 391 ? 0.4288 0.9063 0.3399 0.0406  -0.0190 -0.0152 406 TRP A CD1 
2676 C CD2 . TRP A 391 ? 0.4080 0.9017 0.3438 0.0417  -0.0120 -0.0120 406 TRP A CD2 
2677 N NE1 . TRP A 391 ? 0.4094 0.8878 0.3368 0.0293  -0.0202 -0.0075 406 TRP A NE1 
2678 C CE2 . TRP A 391 ? 0.3998 0.8879 0.3419 0.0295  -0.0162 -0.0056 406 TRP A CE2 
2679 C CE3 . TRP A 391 ? 0.3960 0.9004 0.3450 0.0451  -0.0079 -0.0112 406 TRP A CE3 
2680 C CZ2 . TRP A 391 ? 0.3794 0.8712 0.3388 0.0208  -0.0166 0.0008  406 TRP A CZ2 
2681 C CZ3 . TRP A 391 ? 0.3811 0.8905 0.3483 0.0358  -0.0086 -0.0041 406 TRP A CZ3 
2682 C CH2 . TRP A 391 ? 0.3658 0.8683 0.3372 0.0238  -0.0131 0.0014  406 TRP A CH2 
2683 N N   . ASP A 392 ? 0.5450 1.0610 0.4226 0.0973  0.0092  -0.0354 407 ASP A N   
2684 C CA  . ASP A 392 ? 0.5972 1.1090 0.4568 0.1149  0.0104  -0.0477 407 ASP A CA  
2685 C C   . ASP A 392 ? 0.6144 1.1023 0.4766 0.1175  -0.0013 -0.0605 407 ASP A C   
2686 O O   . ASP A 392 ? 0.5974 1.0858 0.4789 0.1144  -0.0023 -0.0591 407 ASP A O   
2687 C CB  . ASP A 392 ? 0.6182 1.1548 0.4825 0.1262  0.0239  -0.0440 407 ASP A CB  
2688 C CG  . ASP A 392 ? 0.6790 1.2109 0.5202 0.1469  0.0260  -0.0573 407 ASP A CG  
2689 O OD1 . ASP A 392 ? 0.7442 1.2823 0.5625 0.1549  0.0320  -0.0574 407 ASP A OD1 
2690 O OD2 . ASP A 392 ? 0.6750 1.1946 0.5190 0.1555  0.0209  -0.0682 407 ASP A OD2 
2691 N N   . GLN A 393 ? 0.6814 1.1483 0.5239 0.1235  -0.0105 -0.0730 408 GLN A N   
2692 C CA  . GLN A 393 ? 0.7215 1.1632 0.5668 0.1246  -0.0230 -0.0850 408 GLN A CA  
2693 C C   . GLN A 393 ? 0.6980 1.1325 0.5648 0.1076  -0.0298 -0.0786 408 GLN A C   
2694 O O   . GLN A 393 ? 0.7150 1.1442 0.5984 0.1051  -0.0322 -0.0787 408 GLN A O   
2695 C CB  . GLN A 393 ? 0.7520 1.1936 0.6015 0.1376  -0.0200 -0.0915 408 GLN A CB  
2696 C CG  . GLN A 393 ? 0.8157 1.2535 0.6397 0.1574  -0.0179 -0.1039 408 GLN A CG  
2697 C CD  . GLN A 393 ? 0.8579 1.2854 0.6852 0.1700  -0.0199 -0.1136 408 GLN A CD  
2698 O OE1 . GLN A 393 ? 0.8648 1.2939 0.7145 0.1648  -0.0201 -0.1087 408 GLN A OE1 
2699 N NE2 . GLN A 393 ? 0.9058 1.3216 0.7096 0.1874  -0.0220 -0.1277 408 GLN A NE2 
2700 N N   . PRO A 394 ? 0.6792 1.1131 0.5448 0.0966  -0.0328 -0.0729 409 PRO A N   
2701 C CA  . PRO A 394 ? 0.6259 1.0573 0.5113 0.0809  -0.0368 -0.0649 409 PRO A CA  
2702 C C   . PRO A 394 ? 0.6192 1.0294 0.5133 0.0769  -0.0483 -0.0722 409 PRO A C   
2703 O O   . PRO A 394 ? 0.5779 0.9862 0.4888 0.0660  -0.0506 -0.0662 409 PRO A O   
2704 C CB  . PRO A 394 ? 0.6178 1.0505 0.4944 0.0741  -0.0385 -0.0600 409 PRO A CB  
2705 C CG  . PRO A 394 ? 0.6442 1.0694 0.4961 0.0851  -0.0420 -0.0700 409 PRO A CG  
2706 C CD  . PRO A 394 ? 0.6565 1.0881 0.4997 0.0997  -0.0347 -0.0755 409 PRO A CD  
2707 N N   . GLU A 395 ? 0.6852 1.0789 0.5672 0.0856  -0.0557 -0.0848 410 GLU A N   
2708 C CA  . GLU A 395 ? 0.7216 1.0938 0.6117 0.0810  -0.0675 -0.0915 410 GLU A CA  
2709 C C   . GLU A 395 ? 0.6968 1.0620 0.5947 0.0875  -0.0670 -0.0953 410 GLU A C   
2710 O O   . GLU A 395 ? 0.6967 1.0433 0.6022 0.0845  -0.0760 -0.1001 410 GLU A O   
2711 C CB  . GLU A 395 ? 0.7934 1.1489 0.6662 0.0848  -0.0787 -0.1033 410 GLU A CB  
2712 C CG  . GLU A 395 ? 0.8230 1.1833 0.6891 0.0781  -0.0814 -0.0994 410 GLU A CG  
2713 C CD  . GLU A 395 ? 0.9529 1.3069 0.7920 0.0884  -0.0865 -0.1096 410 GLU A CD  
2714 O OE1 . GLU A 395 ? 1.0321 1.3920 0.8539 0.1016  -0.0793 -0.1134 410 GLU A OE1 
2715 O OE2 . GLU A 395 ? 0.9570 1.3012 0.7914 0.0841  -0.0977 -0.1137 410 GLU A OE2 
2716 N N   . GLN A 396 ? 0.6791 1.0600 0.5765 0.0963  -0.0565 -0.0924 411 GLN A N   
2717 C CA  . GLN A 396 ? 0.6966 1.0727 0.6014 0.1040  -0.0556 -0.0954 411 GLN A CA  
2718 C C   . GLN A 396 ? 0.6223 1.0134 0.5481 0.0968  -0.0491 -0.0829 411 GLN A C   
2719 O O   . GLN A 396 ? 0.5609 0.9725 0.4915 0.0913  -0.0413 -0.0731 411 GLN A O   
2720 C CB  . GLN A 396 ? 0.7692 1.1506 0.6575 0.1224  -0.0498 -0.1033 411 GLN A CB  
2721 C CG  . GLN A 396 ? 0.8361 1.2000 0.7246 0.1335  -0.0546 -0.1128 411 GLN A CG  
2722 C CD  . GLN A 396 ? 0.9099 1.2794 0.7813 0.1536  -0.0484 -0.1214 411 GLN A CD  
2723 O OE1 . GLN A 396 ? 0.9795 1.3455 0.8289 0.1616  -0.0493 -0.1297 411 GLN A OE1 
2724 N NE2 . GLN A 396 ? 0.9110 1.2894 0.7917 0.1630  -0.0422 -0.1196 411 GLN A NE2 
2725 N N   . PHE A 397 ? 0.5808 0.9601 0.5179 0.0968  -0.0532 -0.0836 412 PHE A N   
2726 C CA  . PHE A 397 ? 0.5854 0.9749 0.5408 0.0900  -0.0496 -0.0730 412 PHE A CA  
2727 C C   . PHE A 397 ? 0.6045 1.0129 0.5638 0.1007  -0.0408 -0.0704 412 PHE A C   
2728 O O   . PHE A 397 ? 0.6298 1.0307 0.5890 0.1119  -0.0420 -0.0759 412 PHE A O   
2729 C CB  . PHE A 397 ? 0.5948 0.9633 0.5599 0.0856  -0.0578 -0.0737 412 PHE A CB  
2730 C CG  . PHE A 397 ? 0.5700 0.9469 0.5514 0.0777  -0.0552 -0.0625 412 PHE A CG  
2731 C CD1 . PHE A 397 ? 0.5606 0.9476 0.5492 0.0850  -0.0509 -0.0592 412 PHE A CD1 
2732 C CD2 . PHE A 397 ? 0.5658 0.9409 0.5547 0.0640  -0.0575 -0.0557 412 PHE A CD2 
2733 C CE1 . PHE A 397 ? 0.5504 0.9442 0.5521 0.0782  -0.0499 -0.0495 412 PHE A CE1 
2734 C CE2 . PHE A 397 ? 0.5566 0.9383 0.5576 0.0578  -0.0555 -0.0462 412 PHE A CE2 
2735 C CZ  . PHE A 397 ? 0.5476 0.9380 0.5544 0.0647  -0.0522 -0.0433 412 PHE A CZ  
2736 N N   . ASN A 398 ? 0.5926 1.0255 0.5567 0.0970  -0.0324 -0.0615 413 ASN A N   
2737 C CA  . ASN A 398 ? 0.5979 1.0532 0.5657 0.1073  -0.0231 -0.0588 413 ASN A CA  
2738 C C   . ASN A 398 ? 0.5697 1.0479 0.5549 0.0983  -0.0178 -0.0459 413 ASN A C   
2739 O O   . ASN A 398 ? 0.5603 1.0577 0.5458 0.0945  -0.0110 -0.0394 413 ASN A O   
2740 C CB  . ASN A 398 ? 0.6098 1.0745 0.5606 0.1166  -0.0168 -0.0634 413 ASN A CB  
2741 C CG  . ASN A 398 ? 0.6348 1.1218 0.5881 0.1304  -0.0068 -0.0624 413 ASN A CG  
2742 O OD1 . ASN A 398 ? 0.6305 1.1368 0.6017 0.1280  -0.0022 -0.0535 413 ASN A OD1 
2743 N ND2 . ASN A 398 ? 0.6878 1.1730 0.6231 0.1455  -0.0037 -0.0718 413 ASN A ND2 
2744 N N   . PRO A 399 ? 0.5564 1.0320 0.5558 0.0950  -0.0213 -0.0419 414 PRO A N   
2745 C CA  . PRO A 399 ? 0.5533 1.0466 0.5684 0.0853  -0.0190 -0.0307 414 PRO A CA  
2746 C C   . PRO A 399 ? 0.5491 1.0722 0.5710 0.0895  -0.0096 -0.0250 414 PRO A C   
2747 O O   . PRO A 399 ? 0.5189 1.0574 0.5501 0.0792  -0.0072 -0.0159 414 PRO A O   
2748 C CB  . PRO A 399 ? 0.5680 1.0539 0.5937 0.0878  -0.0240 -0.0298 414 PRO A CB  
2749 C CG  . PRO A 399 ? 0.5846 1.0430 0.6002 0.0931  -0.0305 -0.0391 414 PRO A CG  
2750 C CD  . PRO A 399 ? 0.5812 1.0384 0.5820 0.1025  -0.0274 -0.0478 414 PRO A CD  
2751 N N   . GLU A 400 ? 0.5765 1.1069 0.5937 0.1049  -0.0044 -0.0306 415 GLU A N   
2752 C CA  . GLU A 400 ? 0.5790 1.1397 0.6018 0.1113  0.0063  -0.0256 415 GLU A CA  
2753 C C   . GLU A 400 ? 0.5162 1.0899 0.5336 0.1028  0.0126  -0.0193 415 GLU A C   
2754 O O   . GLU A 400 ? 0.4692 1.0702 0.4971 0.1022  0.0209  -0.0108 415 GLU A O   
2755 C CB  . GLU A 400 ? 0.6564 1.2185 0.6696 0.1314  0.0109  -0.0350 415 GLU A CB  
2756 C CG  . GLU A 400 ? 0.7102 1.2631 0.7311 0.1416  0.0058  -0.0397 415 GLU A CG  
2757 C CD  . GLU A 400 ? 0.7926 1.3148 0.7956 0.1528  -0.0005 -0.0535 415 GLU A CD  
2758 O OE1 . GLU A 400 ? 0.8118 1.3121 0.8001 0.1466  -0.0060 -0.0589 415 GLU A OE1 
2759 O OE2 . GLU A 400 ? 0.8530 1.3725 0.8576 0.1678  -0.0009 -0.0590 415 GLU A OE2 
2760 N N   . ARG A 401 ? 0.5031 1.0580 0.5056 0.0960  0.0082  -0.0225 416 ARG A N   
2761 C CA  . ARG A 401 ? 0.4750 1.0395 0.4720 0.0871  0.0129  -0.0154 416 ARG A CA  
2762 C C   . ARG A 401 ? 0.4605 1.0357 0.4747 0.0711  0.0120  -0.0034 416 ARG A C   
2763 O O   . ARG A 401 ? 0.4701 1.0584 0.4847 0.0643  0.0172  0.0048  416 ARG A O   
2764 C CB  . ARG A 401 ? 0.4564 0.9980 0.4338 0.0843  0.0073  -0.0219 416 ARG A CB  
2765 C CG  . ARG A 401 ? 0.4434 0.9712 0.4251 0.0684  -0.0005 -0.0179 416 ARG A CG  
2766 C CD  . ARG A 401 ? 0.4481 0.9491 0.4167 0.0687  -0.0095 -0.0277 416 ARG A CD  
2767 N NE  . ARG A 401 ? 0.4656 0.9636 0.4139 0.0768  -0.0075 -0.0339 416 ARG A NE  
2768 C CZ  . ARG A 401 ? 0.4731 0.9524 0.4074 0.0849  -0.0135 -0.0458 416 ARG A CZ  
2769 N NH1 . ARG A 401 ? 0.4672 0.9279 0.4063 0.0857  -0.0216 -0.0526 416 ARG A NH1 
2770 N NH2 . ARG A 401 ? 0.5024 0.9810 0.4170 0.0923  -0.0117 -0.0506 416 ARG A NH2 
2771 N N   . PHE A 402 ? 0.4456 1.0131 0.4723 0.0653  0.0048  -0.0025 417 PHE A N   
2772 C CA  . PHE A 402 ? 0.4394 1.0161 0.4818 0.0515  0.0027  0.0075  417 PHE A CA  
2773 C C   . PHE A 402 ? 0.4704 1.0732 0.5328 0.0543  0.0068  0.0139  417 PHE A C   
2774 O O   . PHE A 402 ? 0.4602 1.0725 0.5373 0.0437  0.0042  0.0218  417 PHE A O   
2775 C CB  . PHE A 402 ? 0.4131 0.9677 0.4562 0.0437  -0.0074 0.0054  417 PHE A CB  
2776 C CG  . PHE A 402 ? 0.3916 0.9267 0.4211 0.0368  -0.0113 0.0029  417 PHE A CG  
2777 C CD1 . PHE A 402 ? 0.3720 0.9095 0.4019 0.0253  -0.0114 0.0098  417 PHE A CD1 
2778 C CD2 . PHE A 402 ? 0.4050 0.9195 0.4221 0.0420  -0.0154 -0.0063 417 PHE A CD2 
2779 C CE1 . PHE A 402 ? 0.3611 0.8821 0.3791 0.0203  -0.0150 0.0077  417 PHE A CE1 
2780 C CE2 . PHE A 402 ? 0.3891 0.8882 0.3957 0.0359  -0.0192 -0.0083 417 PHE A CE2 
2781 C CZ  . PHE A 402 ? 0.3744 0.8774 0.3814 0.0256  -0.0188 -0.0013 417 PHE A CZ  
2782 N N   . LEU A 403 ? 0.5226 1.1368 0.5855 0.0691  0.0125  0.0099  418 LEU A N   
2783 C CA  . LEU A 403 ? 0.5502 1.1925 0.6330 0.0741  0.0174  0.0156  418 LEU A CA  
2784 C C   . LEU A 403 ? 0.6420 1.3124 0.7276 0.0776  0.0298  0.0221  418 LEU A C   
2785 O O   . LEU A 403 ? 0.6444 1.3159 0.7150 0.0901  0.0371  0.0166  418 LEU A O   
2786 C CB  . LEU A 403 ? 0.5446 1.1827 0.6276 0.0903  0.0161  0.0074  418 LEU A CB  
2787 C CG  . LEU A 403 ? 0.5321 1.1463 0.6154 0.0886  0.0050  0.0030  418 LEU A CG  
2788 C CD1 . LEU A 403 ? 0.5423 1.1499 0.6229 0.1059  0.0044  -0.0054 418 LEU A CD1 
2789 C CD2 . LEU A 403 ? 0.5146 1.1403 0.6173 0.0775  -0.0001 0.0118  418 LEU A CD2 
2790 N N   . GLU A 404 ? 0.7439 1.4370 0.8488 0.0666  0.0321  0.0340  419 GLU A N   
2791 C CA  . GLU A 404 ? 0.8455 1.5726 0.9618 0.0707  0.0444  0.0425  419 GLU A CA  
2792 C C   . GLU A 404 ? 0.8396 1.5903 0.9848 0.0582  0.0424  0.0546  419 GLU A C   
2793 O O   . GLU A 404 ? 0.8992 1.6605 1.0618 0.0624  0.0386  0.0543  419 GLU A O   
2794 C CB  . GLU A 404 ? 0.9188 1.6468 1.0185 0.0680  0.0526  0.0461  419 GLU A CB  
2795 C CG  . GLU A 404 ? 0.9820 1.7458 1.0906 0.0746  0.0675  0.0551  419 GLU A CG  
2796 C CD  . GLU A 404 ? 1.0073 1.7907 1.1328 0.0572  0.0709  0.0713  419 GLU A CD  
2797 O OE1 . GLU A 404 ? 1.1547 1.9541 1.2742 0.0584  0.0827  0.0789  419 GLU A OE1 
2798 O OE2 . GLU A 404 ? 0.9625 1.7446 1.1062 0.0425  0.0617  0.0767  419 GLU A OE2 
2799 N N   . SER A 413 ? 0.6319 1.1869 0.6364 -0.0124 0.0025  0.0496  428 SER A N   
2800 C CA  . SER A 413 ? 0.6468 1.1974 0.6424 -0.0191 0.0033  0.0576  428 SER A CA  
2801 C C   . SER A 413 ? 0.6396 1.1661 0.6208 -0.0195 -0.0046 0.0514  428 SER A C   
2802 O O   . SER A 413 ? 0.6943 1.2100 0.6770 -0.0285 -0.0097 0.0559  428 SER A O   
2803 C CB  . SER A 413 ? 0.6671 1.2330 0.6524 -0.0128 0.0137  0.0628  428 SER A CB  
2804 O OG  . SER A 413 ? 0.6572 1.2108 0.6207 -0.0038 0.0127  0.0548  428 SER A OG  
2805 N N   . SER A 414 ? 0.5636 1.0819 0.5317 -0.0097 -0.0059 0.0412  429 SER A N   
2806 C CA  . SER A 414 ? 0.5078 1.0053 0.4661 -0.0099 -0.0142 0.0347  429 SER A CA  
2807 C C   . SER A 414 ? 0.4768 0.9645 0.4422 -0.0080 -0.0202 0.0252  429 SER A C   
2808 O O   . SER A 414 ? 0.4758 0.9511 0.4336 -0.0039 -0.0252 0.0171  429 SER A O   
2809 C CB  . SER A 414 ? 0.5127 1.0059 0.4508 -0.0022 -0.0136 0.0310  429 SER A CB  
2810 O OG  . SER A 414 ? 0.5040 0.9978 0.4358 0.0084  -0.0129 0.0209  429 SER A OG  
2811 N N   . PHE A 415 ? 0.4596 0.9533 0.4400 -0.0114 -0.0200 0.0270  430 PHE A N   
2812 C CA  . PHE A 415 ? 0.4071 0.8923 0.3950 -0.0106 -0.0251 0.0205  430 PHE A CA  
2813 C C   . PHE A 415 ? 0.3638 0.8394 0.3570 -0.0195 -0.0306 0.0238  430 PHE A C   
2814 O O   . PHE A 415 ? 0.3567 0.8384 0.3580 -0.0261 -0.0303 0.0305  430 PHE A O   
2815 C CB  . PHE A 415 ? 0.3998 0.8988 0.3993 -0.0073 -0.0215 0.0209  430 PHE A CB  
2816 C CG  . PHE A 415 ? 0.3694 0.8604 0.3748 -0.0045 -0.0258 0.0147  430 PHE A CG  
2817 C CD1 . PHE A 415 ? 0.3634 0.8416 0.3618 0.0012  -0.0288 0.0064  430 PHE A CD1 
2818 C CD2 . PHE A 415 ? 0.3544 0.8511 0.3725 -0.0077 -0.0271 0.0179  430 PHE A CD2 
2819 C CE1 . PHE A 415 ? 0.3495 0.8201 0.3537 0.0032  -0.0323 0.0023  430 PHE A CE1 
2820 C CE2 . PHE A 415 ? 0.3461 0.8355 0.3682 -0.0047 -0.0307 0.0134  430 PHE A CE2 
2821 C CZ  . PHE A 415 ? 0.3496 0.8259 0.3648 0.0008  -0.0327 0.0061  430 PHE A CZ  
2822 N N   . LEU A 416 ? 0.3487 0.8094 0.3372 -0.0195 -0.0358 0.0190  431 LEU A N   
2823 C CA  . LEU A 416 ? 0.3283 0.7787 0.3199 -0.0257 -0.0408 0.0206  431 LEU A CA  
2824 C C   . LEU A 416 ? 0.3161 0.7568 0.3097 -0.0232 -0.0444 0.0145  431 LEU A C   
2825 O O   . LEU A 416 ? 0.3209 0.7519 0.3108 -0.0237 -0.0476 0.0127  431 LEU A O   
2826 C CB  . LEU A 416 ? 0.3269 0.7695 0.3103 -0.0288 -0.0429 0.0237  431 LEU A CB  
2827 C CG  . LEU A 416 ? 0.3360 0.7863 0.3174 -0.0329 -0.0395 0.0321  431 LEU A CG  
2828 C CD1 . LEU A 416 ? 0.3422 0.7844 0.3121 -0.0332 -0.0412 0.0345  431 LEU A CD1 
2829 C CD2 . LEU A 416 ? 0.3370 0.7886 0.3281 -0.0408 -0.0412 0.0378  431 LEU A CD2 
2830 N N   . PRO A 417 ? 0.3203 0.7642 0.3204 -0.0204 -0.0436 0.0121  432 PRO A N   
2831 C CA  . PRO A 417 ? 0.3138 0.7489 0.3166 -0.0186 -0.0463 0.0079  432 PRO A CA  
2832 C C   . PRO A 417 ? 0.2945 0.7214 0.2978 -0.0227 -0.0494 0.0097  432 PRO A C   
2833 O O   . PRO A 417 ? 0.3100 0.7294 0.3137 -0.0215 -0.0509 0.0071  432 PRO A O   
2834 C CB  . PRO A 417 ? 0.3143 0.7554 0.3240 -0.0156 -0.0449 0.0076  432 PRO A CB  
2835 C CG  . PRO A 417 ? 0.3261 0.7798 0.3394 -0.0180 -0.0426 0.0126  432 PRO A CG  
2836 C CD  . PRO A 417 ? 0.3271 0.7840 0.3337 -0.0189 -0.0402 0.0143  432 PRO A CD  
2837 N N   . PHE A 418 ? 0.2730 0.7011 0.2765 -0.0274 -0.0503 0.0140  433 PHE A N   
2838 C CA  . PHE A 418 ? 0.2737 0.6926 0.2753 -0.0300 -0.0534 0.0148  433 PHE A CA  
2839 C C   . PHE A 418 ? 0.2703 0.6827 0.2660 -0.0326 -0.0553 0.0165  433 PHE A C   
2840 O O   . PHE A 418 ? 0.2733 0.6781 0.2665 -0.0347 -0.0582 0.0175  433 PHE A O   
2841 C CB  . PHE A 418 ? 0.2801 0.7013 0.2853 -0.0327 -0.0553 0.0171  433 PHE A CB  
2842 C CG  . PHE A 418 ? 0.2767 0.7018 0.2866 -0.0291 -0.0545 0.0157  433 PHE A CG  
2843 C CD1 . PHE A 418 ? 0.2737 0.6913 0.2818 -0.0266 -0.0552 0.0140  433 PHE A CD1 
2844 C CD2 . PHE A 418 ? 0.2728 0.7092 0.2888 -0.0275 -0.0525 0.0165  433 PHE A CD2 
2845 C CE1 . PHE A 418 ? 0.2742 0.6939 0.2858 -0.0232 -0.0546 0.0136  433 PHE A CE1 
2846 C CE2 . PHE A 418 ? 0.2755 0.7140 0.2956 -0.0233 -0.0523 0.0153  433 PHE A CE2 
2847 C CZ  . PHE A 418 ? 0.2709 0.7002 0.2884 -0.0214 -0.0537 0.0141  433 PHE A CZ  
2848 N N   . GLY A 419 ? 0.2697 0.6836 0.2617 -0.0317 -0.0543 0.0166  434 GLY A N   
2849 C CA  . GLY A 419 ? 0.2705 0.6788 0.2566 -0.0345 -0.0563 0.0200  434 GLY A CA  
2850 C C   . GLY A 419 ? 0.2722 0.6828 0.2596 -0.0406 -0.0566 0.0259  434 GLY A C   
2851 O O   . GLY A 419 ? 0.2652 0.6868 0.2581 -0.0421 -0.0539 0.0282  434 GLY A O   
2852 N N   . ALA A 420 ? 0.2755 0.6758 0.2588 -0.0440 -0.0603 0.0287  435 ALA A N   
2853 C CA  . ALA A 420 ? 0.2719 0.6717 0.2570 -0.0511 -0.0622 0.0349  435 ALA A CA  
2854 C C   . ALA A 420 ? 0.2746 0.6580 0.2524 -0.0527 -0.0672 0.0364  435 ALA A C   
2855 O O   . ALA A 420 ? 0.2917 0.6675 0.2641 -0.0474 -0.0683 0.0325  435 ALA A O   
2856 C CB  . ALA A 420 ? 0.2772 0.6894 0.2638 -0.0532 -0.0574 0.0407  435 ALA A CB  
2857 N N   . GLY A 421 ? 0.2720 0.6498 0.2506 -0.0599 -0.0706 0.0420  436 GLY A N   
2858 C CA  . GLY A 421 ? 0.2807 0.6405 0.2520 -0.0614 -0.0762 0.0436  436 GLY A CA  
2859 C C   . GLY A 421 ? 0.2852 0.6313 0.2523 -0.0574 -0.0811 0.0369  436 GLY A C   
2860 O O   . GLY A 421 ? 0.2886 0.6395 0.2586 -0.0546 -0.0802 0.0318  436 GLY A O   
2861 N N   . PRO A 422 ? 0.2957 0.6245 0.2549 -0.0560 -0.0860 0.0367  437 PRO A N   
2862 C CA  . PRO A 422 ? 0.3089 0.6252 0.2629 -0.0511 -0.0901 0.0299  437 PRO A CA  
2863 C C   . PRO A 422 ? 0.3078 0.6324 0.2629 -0.0432 -0.0857 0.0235  437 PRO A C   
2864 O O   . PRO A 422 ? 0.3258 0.6455 0.2781 -0.0406 -0.0876 0.0190  437 PRO A O   
2865 C CB  . PRO A 422 ? 0.3200 0.6190 0.2651 -0.0473 -0.0941 0.0302  437 PRO A CB  
2866 C CG  . PRO A 422 ? 0.3212 0.6197 0.2669 -0.0541 -0.0945 0.0389  437 PRO A CG  
2867 C CD  . PRO A 422 ? 0.3071 0.6271 0.2601 -0.0559 -0.0873 0.0415  437 PRO A CD  
2868 N N   . ARG A 423 ? 0.3050 0.6420 0.2639 -0.0398 -0.0802 0.0234  438 ARG A N   
2869 C CA  . ARG A 423 ? 0.3012 0.6450 0.2626 -0.0330 -0.0763 0.0184  438 ARG A CA  
2870 C C   . ARG A 423 ? 0.2775 0.6351 0.2461 -0.0344 -0.0722 0.0178  438 ARG A C   
2871 O O   . ARG A 423 ? 0.2548 0.6188 0.2269 -0.0300 -0.0687 0.0152  438 ARG A O   
2872 C CB  . ARG A 423 ? 0.3169 0.6636 0.2787 -0.0282 -0.0745 0.0182  438 ARG A CB  
2873 C CG  . ARG A 423 ? 0.3397 0.6740 0.2955 -0.0231 -0.0780 0.0171  438 ARG A CG  
2874 C CD  . ARG A 423 ? 0.3525 0.6848 0.3077 -0.0172 -0.0766 0.0123  438 ARG A CD  
2875 N NE  . ARG A 423 ? 0.3754 0.6947 0.3236 -0.0110 -0.0797 0.0102  438 ARG A NE  
2876 C CZ  . ARG A 423 ? 0.4043 0.7240 0.3517 -0.0032 -0.0771 0.0065  438 ARG A CZ  
2877 N NH1 . ARG A 423 ? 0.4012 0.7335 0.3552 -0.0018 -0.0716 0.0054  438 ARG A NH1 
2878 N NH2 . ARG A 423 ? 0.4410 0.7483 0.3809 0.0038  -0.0799 0.0042  438 ARG A NH2 
2879 N N   . VAL A 424 ? 0.2762 0.6387 0.2482 -0.0404 -0.0727 0.0209  439 VAL A N   
2880 C CA  . VAL A 424 ? 0.2761 0.6515 0.2553 -0.0411 -0.0695 0.0205  439 VAL A CA  
2881 C C   . VAL A 424 ? 0.2751 0.6501 0.2543 -0.0370 -0.0690 0.0167  439 VAL A C   
2882 O O   . VAL A 424 ? 0.2867 0.6515 0.2596 -0.0350 -0.0719 0.0145  439 VAL A O   
2883 C CB  . VAL A 424 ? 0.2804 0.6605 0.2643 -0.0483 -0.0716 0.0247  439 VAL A CB  
2884 C CG1 . VAL A 424 ? 0.2850 0.6533 0.2653 -0.0513 -0.0784 0.0240  439 VAL A CG1 
2885 C CG2 . VAL A 424 ? 0.2687 0.6638 0.2610 -0.0479 -0.0682 0.0248  439 VAL A CG2 
2886 N N   . CYS A 425 ? 0.2755 0.6604 0.2604 -0.0352 -0.0653 0.0159  440 CYS A N   
2887 C CA  . CYS A 425 ? 0.2974 0.6816 0.2819 -0.0312 -0.0642 0.0137  440 CYS A CA  
2888 C C   . CYS A 425 ? 0.3214 0.6995 0.3008 -0.0323 -0.0687 0.0133  440 CYS A C   
2889 O O   . CYS A 425 ? 0.3363 0.7174 0.3186 -0.0370 -0.0721 0.0151  440 CYS A O   
2890 C CB  . CYS A 425 ? 0.2955 0.6898 0.2872 -0.0300 -0.0609 0.0138  440 CYS A CB  
2891 S SG  . CYS A 425 ? 0.3171 0.7098 0.3083 -0.0251 -0.0587 0.0127  440 CYS A SG  
2892 N N   . VAL A 426 ? 0.3551 0.7248 0.3268 -0.0278 -0.0691 0.0109  441 VAL A N   
2893 C CA  . VAL A 426 ? 0.3927 0.7553 0.3566 -0.0274 -0.0741 0.0094  441 VAL A CA  
2894 C C   . VAL A 426 ? 0.3696 0.7386 0.3349 -0.0255 -0.0731 0.0100  441 VAL A C   
2895 O O   . VAL A 426 ? 0.3787 0.7436 0.3382 -0.0257 -0.0783 0.0090  441 VAL A O   
2896 C CB  . VAL A 426 ? 0.4327 0.7827 0.3841 -0.0216 -0.0751 0.0061  441 VAL A CB  
2897 C CG1 . VAL A 426 ? 0.4559 0.7963 0.4042 -0.0232 -0.0783 0.0053  441 VAL A CG1 
2898 C CG2 . VAL A 426 ? 0.4378 0.7919 0.3896 -0.0149 -0.0677 0.0061  441 VAL A CG2 
2899 N N   . GLY A 427 ? 0.3425 0.7203 0.3152 -0.0235 -0.0674 0.0116  442 GLY A N   
2900 C CA  . GLY A 427 ? 0.3317 0.7144 0.3061 -0.0212 -0.0662 0.0130  442 GLY A CA  
2901 C C   . GLY A 427 ? 0.3280 0.7215 0.3136 -0.0236 -0.0657 0.0147  442 GLY A C   
2902 O O   . GLY A 427 ? 0.3016 0.6990 0.2908 -0.0207 -0.0632 0.0159  442 GLY A O   
2903 N N   . GLU A 428 ? 0.3414 0.7393 0.3322 -0.0285 -0.0678 0.0152  443 GLU A N   
2904 C CA  . GLU A 428 ? 0.3486 0.7585 0.3497 -0.0300 -0.0662 0.0168  443 GLU A CA  
2905 C C   . GLU A 428 ? 0.3643 0.7808 0.3696 -0.0293 -0.0694 0.0181  443 GLU A C   
2906 O O   . GLU A 428 ? 0.3481 0.7714 0.3592 -0.0259 -0.0668 0.0186  443 GLU A O   
2907 C CB  . GLU A 428 ? 0.3666 0.7806 0.3714 -0.0355 -0.0670 0.0184  443 GLU A CB  
2908 C CG  . GLU A 428 ? 0.3727 0.8013 0.3876 -0.0362 -0.0641 0.0206  443 GLU A CG  
2909 C CD  . GLU A 428 ? 0.3901 0.8230 0.4076 -0.0419 -0.0639 0.0238  443 GLU A CD  
2910 O OE1 . GLU A 428 ? 0.4091 0.8321 0.4211 -0.0459 -0.0672 0.0244  443 GLU A OE1 
2911 O OE2 . GLU A 428 ? 0.4101 0.8560 0.4347 -0.0419 -0.0601 0.0261  443 GLU A OE2 
2912 N N   . SER A 429 ? 0.4145 0.8285 0.4170 -0.0325 -0.0759 0.0184  444 SER A N   
2913 C CA  . SER A 429 ? 0.4740 0.8937 0.4798 -0.0318 -0.0808 0.0195  444 SER A CA  
2914 C C   . SER A 429 ? 0.4831 0.8989 0.4829 -0.0247 -0.0790 0.0192  444 SER A C   
2915 O O   . SER A 429 ? 0.5167 0.9398 0.5222 -0.0215 -0.0795 0.0208  444 SER A O   
2916 C CB  . SER A 429 ? 0.5103 0.9237 0.5110 -0.0362 -0.0898 0.0186  444 SER A CB  
2917 O OG  . SER A 429 ? 0.5745 0.9901 0.5815 -0.0437 -0.0918 0.0200  444 SER A OG  
2918 N N   . LEU A 430 ? 0.4583 0.8628 0.4470 -0.0219 -0.0766 0.0178  445 LEU A N   
2919 C CA  . LEU A 430 ? 0.4745 0.8754 0.4575 -0.0159 -0.0742 0.0191  445 LEU A CA  
2920 C C   . LEU A 430 ? 0.4218 0.8272 0.4135 -0.0135 -0.0681 0.0207  445 LEU A C   
2921 O O   . LEU A 430 ? 0.4294 0.8359 0.4224 -0.0095 -0.0678 0.0229  445 LEU A O   
2922 C CB  . LEU A 430 ? 0.5108 0.9007 0.4809 -0.0133 -0.0720 0.0181  445 LEU A CB  
2923 C CG  . LEU A 430 ? 0.5730 0.9596 0.5360 -0.0074 -0.0691 0.0210  445 LEU A CG  
2924 C CD1 . LEU A 430 ? 0.6332 1.0104 0.5798 -0.0040 -0.0700 0.0196  445 LEU A CD1 
2925 C CD2 . LEU A 430 ? 0.5957 0.9833 0.5655 -0.0062 -0.0612 0.0234  445 LEU A CD2 
2926 N N   . ALA A 431 ? 0.3864 0.7930 0.3831 -0.0156 -0.0641 0.0193  446 ALA A N   
2927 C CA  . ALA A 431 ? 0.3628 0.7717 0.3668 -0.0137 -0.0596 0.0193  446 ALA A CA  
2928 C C   . ALA A 431 ? 0.3443 0.7620 0.3565 -0.0116 -0.0608 0.0197  446 ALA A C   
2929 O O   . ALA A 431 ? 0.3291 0.7453 0.3437 -0.0073 -0.0597 0.0208  446 ALA A O   
2930 C CB  . ALA A 431 ? 0.3582 0.7677 0.3648 -0.0165 -0.0571 0.0170  446 ALA A CB  
2931 N N   . ARG A 432 ? 0.3391 0.7660 0.3562 -0.0146 -0.0629 0.0194  447 ARG A N   
2932 C CA  . ARG A 432 ? 0.3415 0.7806 0.3683 -0.0125 -0.0633 0.0201  447 ARG A CA  
2933 C C   . ARG A 432 ? 0.3383 0.7790 0.3663 -0.0081 -0.0668 0.0221  447 ARG A C   
2934 O O   . ARG A 432 ? 0.3463 0.7900 0.3795 -0.0025 -0.0655 0.0222  447 ARG A O   
2935 C CB  . ARG A 432 ? 0.3570 0.8065 0.3893 -0.0180 -0.0652 0.0211  447 ARG A CB  
2936 C CG  . ARG A 432 ? 0.3718 0.8225 0.4041 -0.0208 -0.0609 0.0201  447 ARG A CG  
2937 C CD  . ARG A 432 ? 0.4062 0.8668 0.4444 -0.0271 -0.0626 0.0230  447 ARG A CD  
2938 N NE  . ARG A 432 ? 0.4634 0.9264 0.5009 -0.0284 -0.0577 0.0230  447 ARG A NE  
2939 C CZ  . ARG A 432 ? 0.4538 0.9271 0.4957 -0.0244 -0.0525 0.0227  447 ARG A CZ  
2940 N NH1 . ARG A 432 ? 0.4719 0.9547 0.5209 -0.0185 -0.0514 0.0223  447 ARG A NH1 
2941 N NH2 . ARG A 432 ? 0.4220 0.8957 0.4599 -0.0254 -0.0487 0.0226  447 ARG A NH2 
2942 N N   . ILE A 433 ? 0.3239 0.7611 0.3458 -0.0100 -0.0721 0.0234  448 ILE A N   
2943 C CA  . ILE A 433 ? 0.3126 0.7485 0.3316 -0.0055 -0.0764 0.0255  448 ILE A CA  
2944 C C   . ILE A 433 ? 0.3117 0.7370 0.3249 0.0000  -0.0727 0.0271  448 ILE A C   
2945 O O   . ILE A 433 ? 0.3089 0.7356 0.3255 0.0054  -0.0734 0.0290  448 ILE A O   
2946 C CB  . ILE A 433 ? 0.3156 0.7460 0.3246 -0.0084 -0.0828 0.0254  448 ILE A CB  
2947 C CG1 . ILE A 433 ? 0.3101 0.7521 0.3283 -0.0137 -0.0892 0.0252  448 ILE A CG1 
2948 C CG2 . ILE A 433 ? 0.3371 0.7614 0.3367 -0.0028 -0.0861 0.0277  448 ILE A CG2 
2949 C CD1 . ILE A 433 ? 0.3215 0.7552 0.3299 -0.0186 -0.0958 0.0234  448 ILE A CD1 
2950 N N   . GLU A 434 ? 0.3178 0.7328 0.3232 -0.0013 -0.0687 0.0268  449 GLU A N   
2951 C CA  . GLU A 434 ? 0.3256 0.7317 0.3288 0.0023  -0.0645 0.0293  449 GLU A CA  
2952 C C   . GLU A 434 ? 0.3148 0.7235 0.3284 0.0053  -0.0628 0.0283  449 GLU A C   
2953 O O   . GLU A 434 ? 0.2975 0.7031 0.3122 0.0104  -0.0638 0.0309  449 GLU A O   
2954 C CB  . GLU A 434 ? 0.3339 0.7328 0.3325 -0.0006 -0.0597 0.0289  449 GLU A CB  
2955 C CG  . GLU A 434 ? 0.3600 0.7503 0.3494 0.0016  -0.0570 0.0335  449 GLU A CG  
2956 C CD  . GLU A 434 ? 0.3741 0.7608 0.3617 -0.0009 -0.0517 0.0334  449 GLU A CD  
2957 O OE1 . GLU A 434 ? 0.3603 0.7497 0.3502 -0.0043 -0.0516 0.0292  449 GLU A OE1 
2958 O OE2 . GLU A 434 ? 0.3944 0.7762 0.3788 0.0007  -0.0474 0.0383  449 GLU A OE2 
2959 N N   . LEU A 435 ? 0.3140 0.7276 0.3340 0.0032  -0.0606 0.0243  450 LEU A N   
2960 C CA  . LEU A 435 ? 0.3266 0.7398 0.3534 0.0072  -0.0587 0.0220  450 LEU A CA  
2961 C C   . LEU A 435 ? 0.3368 0.7590 0.3698 0.0130  -0.0611 0.0223  450 LEU A C   
2962 O O   . LEU A 435 ? 0.3402 0.7581 0.3762 0.0190  -0.0610 0.0218  450 LEU A O   
2963 C CB  . LEU A 435 ? 0.3209 0.7375 0.3505 0.0048  -0.0559 0.0174  450 LEU A CB  
2964 C CG  . LEU A 435 ? 0.3209 0.7304 0.3466 -0.0002 -0.0539 0.0163  450 LEU A CG  
2965 C CD1 . LEU A 435 ? 0.3213 0.7378 0.3481 -0.0027 -0.0527 0.0127  450 LEU A CD1 
2966 C CD2 . LEU A 435 ? 0.3258 0.7240 0.3531 0.0010  -0.0528 0.0160  450 LEU A CD2 
2967 N N   . PHE A 436 ? 0.3345 0.7694 0.3706 0.0113  -0.0638 0.0230  451 PHE A N   
2968 C CA  . PHE A 436 ? 0.3327 0.7789 0.3770 0.0170  -0.0663 0.0239  451 PHE A CA  
2969 C C   . PHE A 436 ? 0.3247 0.7625 0.3653 0.0224  -0.0698 0.0275  451 PHE A C   
2970 O O   . PHE A 436 ? 0.3182 0.7535 0.3625 0.0298  -0.0696 0.0274  451 PHE A O   
2971 C CB  . PHE A 436 ? 0.3431 0.8052 0.3937 0.0128  -0.0697 0.0251  451 PHE A CB  
2972 C CG  . PHE A 436 ? 0.3694 0.8448 0.4300 0.0186  -0.0734 0.0271  451 PHE A CG  
2973 C CD1 . PHE A 436 ? 0.3734 0.8616 0.4448 0.0243  -0.0699 0.0256  451 PHE A CD1 
2974 C CD2 . PHE A 436 ? 0.3748 0.8499 0.4333 0.0195  -0.0804 0.0303  451 PHE A CD2 
2975 C CE1 . PHE A 436 ? 0.3906 0.8929 0.4730 0.0308  -0.0732 0.0276  451 PHE A CE1 
2976 C CE2 . PHE A 436 ? 0.3871 0.8752 0.4557 0.0253  -0.0848 0.0323  451 PHE A CE2 
2977 C CZ  . PHE A 436 ? 0.4037 0.9062 0.4856 0.0310  -0.0810 0.0311  451 PHE A CZ  
2978 N N   . LEU A 437 ? 0.3196 0.7519 0.3514 0.0195  -0.0730 0.0307  452 LEU A N   
2979 C CA  . LEU A 437 ? 0.3227 0.7479 0.3484 0.0246  -0.0769 0.0353  452 LEU A CA  
2980 C C   . LEU A 437 ? 0.3377 0.7479 0.3606 0.0283  -0.0732 0.0372  452 LEU A C   
2981 O O   . LEU A 437 ? 0.3508 0.7572 0.3752 0.0351  -0.0753 0.0398  452 LEU A O   
2982 C CB  . LEU A 437 ? 0.3226 0.7431 0.3359 0.0211  -0.0801 0.0376  452 LEU A CB  
2983 C CG  . LEU A 437 ? 0.3271 0.7562 0.3386 0.0209  -0.0885 0.0383  452 LEU A CG  
2984 C CD1 . LEU A 437 ? 0.3265 0.7738 0.3542 0.0207  -0.0919 0.0365  452 LEU A CD1 
2985 C CD2 . LEU A 437 ? 0.3227 0.7476 0.3232 0.0149  -0.0905 0.0367  452 LEU A CD2 
2986 N N   . PHE A 438 ? 0.3580 0.7594 0.3778 0.0237  -0.0683 0.0362  453 PHE A N   
2987 C CA  . PHE A 438 ? 0.3765 0.7634 0.3955 0.0255  -0.0656 0.0386  453 PHE A CA  
2988 C C   . PHE A 438 ? 0.3937 0.7790 0.4211 0.0313  -0.0661 0.0353  453 PHE A C   
2989 O O   . PHE A 438 ? 0.4147 0.7880 0.4416 0.0355  -0.0670 0.0386  453 PHE A O   
2990 C CB  . PHE A 438 ? 0.3624 0.7425 0.3804 0.0190  -0.0607 0.0375  453 PHE A CB  
2991 C CG  . PHE A 438 ? 0.3726 0.7455 0.3818 0.0163  -0.0583 0.0437  453 PHE A CG  
2992 C CD1 . PHE A 438 ? 0.3833 0.7476 0.3870 0.0201  -0.0589 0.0511  453 PHE A CD1 
2993 C CD2 . PHE A 438 ? 0.3720 0.7467 0.3781 0.0108  -0.0550 0.0426  453 PHE A CD2 
2994 C CE1 . PHE A 438 ? 0.3902 0.7494 0.3852 0.0183  -0.0553 0.0576  453 PHE A CE1 
2995 C CE2 . PHE A 438 ? 0.3751 0.7449 0.3733 0.0097  -0.0515 0.0484  453 PHE A CE2 
2996 C CZ  . PHE A 438 ? 0.3878 0.7503 0.3801 0.0133  -0.0513 0.0560  453 PHE A CZ  
2997 N N   . VAL A 439 ? 0.3840 0.7804 0.4181 0.0319  -0.0653 0.0291  454 VAL A N   
2998 C CA  . VAL A 439 ? 0.3931 0.7860 0.4327 0.0377  -0.0646 0.0243  454 VAL A CA  
2999 C C   . VAL A 439 ? 0.4258 0.8256 0.4706 0.0473  -0.0677 0.0248  454 VAL A C   
3000 O O   . VAL A 439 ? 0.4418 0.8328 0.4886 0.0547  -0.0685 0.0227  454 VAL A O   
3001 C CB  . VAL A 439 ? 0.3977 0.7994 0.4401 0.0351  -0.0615 0.0176  454 VAL A CB  
3002 C CG1 . VAL A 439 ? 0.4111 0.8060 0.4557 0.0420  -0.0610 0.0116  454 VAL A CG1 
3003 C CG2 . VAL A 439 ? 0.3955 0.7919 0.4336 0.0261  -0.0592 0.0173  454 VAL A CG2 
3004 N N   . SER A 440 ? 0.4461 0.8614 0.4935 0.0474  -0.0701 0.0273  455 SER A N   
3005 C CA  . SER A 440 ? 0.4587 0.8832 0.5127 0.0566  -0.0738 0.0286  455 SER A CA  
3006 C C   . SER A 440 ? 0.4960 0.9047 0.5447 0.0620  -0.0776 0.0341  455 SER A C   
3007 O O   . SER A 440 ? 0.5108 0.9167 0.5637 0.0719  -0.0795 0.0337  455 SER A O   
3008 C CB  . SER A 440 ? 0.4575 0.9024 0.5169 0.0537  -0.0769 0.0306  455 SER A CB  
3009 O OG  . SER A 440 ? 0.4578 0.8977 0.5081 0.0464  -0.0795 0.0343  455 SER A OG  
3010 N N   . ARG A 441 ? 0.5269 0.9249 0.5657 0.0564  -0.0783 0.0395  456 ARG A N   
3011 C CA  . ARG A 441 ? 0.5736 0.9564 0.6058 0.0612  -0.0813 0.0464  456 ARG A CA  
3012 C C   . ARG A 441 ? 0.5602 0.9231 0.5926 0.0643  -0.0797 0.0466  456 ARG A C   
3013 O O   . ARG A 441 ? 0.5972 0.9517 0.6301 0.0729  -0.0833 0.0496  456 ARG A O   
3014 C CB  . ARG A 441 ? 0.6467 1.0241 0.6667 0.0554  -0.0815 0.0528  456 ARG A CB  
3015 C CG  . ARG A 441 ? 0.7582 1.1284 0.7705 0.0620  -0.0865 0.0609  456 ARG A CG  
3016 C CD  . ARG A 441 ? 0.8676 1.2454 0.8698 0.0591  -0.0898 0.0637  456 ARG A CD  
3017 N NE  . ARG A 441 ? 1.0027 1.3732 0.9939 0.0653  -0.0948 0.0718  456 ARG A NE  
3018 C CZ  . ARG A 441 ? 1.1079 1.4767 1.0837 0.0637  -0.0966 0.0761  456 ARG A CZ  
3019 N NH1 . ARG A 441 ? 1.1213 1.4858 1.0883 0.0567  -0.0907 0.0762  456 ARG A NH1 
3020 N NH2 . ARG A 441 ? 1.1723 1.5437 1.1408 0.0702  -0.1046 0.0800  456 ARG A NH2 
3021 N N   . PRO A 442 ? 0.5376 0.8917 0.5700 0.0577  -0.0753 0.0433  457 PRO A N   
3022 C CA  . PRO A 442 ? 0.5509 0.8844 0.5842 0.0599  -0.0756 0.0437  457 PRO A CA  
3023 C C   . PRO A 442 ? 0.5369 0.8706 0.5766 0.0698  -0.0777 0.0363  457 PRO A C   
3024 O O   . PRO A 442 ? 0.5657 0.8823 0.6055 0.0763  -0.0807 0.0375  457 PRO A O   
3025 C CB  . PRO A 442 ? 0.5531 0.8804 0.5865 0.0496  -0.0714 0.0414  457 PRO A CB  
3026 C CG  . PRO A 442 ? 0.5343 0.8781 0.5651 0.0429  -0.0686 0.0407  457 PRO A CG  
3027 C CD  . PRO A 442 ? 0.5324 0.8938 0.5653 0.0489  -0.0711 0.0385  457 PRO A CD  
3028 N N   . LEU A 443 ? 0.5112 0.8638 0.5559 0.0719  -0.0760 0.0291  458 LEU A N   
3029 C CA  . LEU A 443 ? 0.5145 0.8696 0.5645 0.0830  -0.0768 0.0220  458 LEU A CA  
3030 C C   . LEU A 443 ? 0.5173 0.8770 0.5706 0.0943  -0.0809 0.0257  458 LEU A C   
3031 O O   . LEU A 443 ? 0.5540 0.9031 0.6088 0.1051  -0.0833 0.0230  458 LEU A O   
3032 C CB  . LEU A 443 ? 0.4927 0.8683 0.5468 0.0823  -0.0725 0.0146  458 LEU A CB  
3033 C CG  . LEU A 443 ? 0.4954 0.8647 0.5456 0.0736  -0.0693 0.0096  458 LEU A CG  
3034 C CD1 . LEU A 443 ? 0.4935 0.8823 0.5465 0.0752  -0.0651 0.0030  458 LEU A CD1 
3035 C CD2 . LEU A 443 ? 0.5020 0.8458 0.5488 0.0752  -0.0716 0.0058  458 LEU A CD2 
3036 N N   . GLN A 444 ? 0.5033 0.8776 0.5573 0.0921  -0.0827 0.0317  459 GLN A N   
3037 C CA  . GLN A 444 ? 0.5027 0.8811 0.5594 0.1019  -0.0882 0.0367  459 GLN A CA  
3038 C C   . GLN A 444 ? 0.5401 0.8923 0.5893 0.1056  -0.0918 0.0432  459 GLN A C   
3039 O O   . GLN A 444 ? 0.5717 0.9182 0.6235 0.1173  -0.0957 0.0439  459 GLN A O   
3040 C CB  . GLN A 444 ? 0.4723 0.8690 0.5292 0.0969  -0.0908 0.0417  459 GLN A CB  
3041 C CG  . GLN A 444 ? 0.4769 0.8769 0.5347 0.1057  -0.0980 0.0479  459 GLN A CG  
3042 C CD  . GLN A 444 ? 0.4652 0.8769 0.5190 0.0993  -0.1020 0.0528  459 GLN A CD  
3043 O OE1 . GLN A 444 ? 0.4708 0.8717 0.5124 0.0910  -0.1010 0.0565  459 GLN A OE1 
3044 N NE2 . GLN A 444 ? 0.4585 0.8926 0.5226 0.1035  -0.1071 0.0527  459 GLN A NE2 
3045 N N   . ARG A 445 ? 0.5813 0.9178 0.6218 0.0960  -0.0903 0.0487  460 ARG A N   
3046 C CA  . ARG A 445 ? 0.6295 0.9422 0.6633 0.0985  -0.0933 0.0572  460 ARG A CA  
3047 C C   . ARG A 445 ? 0.6231 0.9112 0.6579 0.0989  -0.0929 0.0543  460 ARG A C   
3048 O O   . ARG A 445 ? 0.6546 0.9219 0.6864 0.1036  -0.0964 0.0605  460 ARG A O   
3049 C CB  . ARG A 445 ? 0.6689 0.9776 0.6924 0.0891  -0.0918 0.0668  460 ARG A CB  
3050 C CG  . ARG A 445 ? 0.7041 1.0325 0.7235 0.0891  -0.0942 0.0697  460 ARG A CG  
3051 C CD  . ARG A 445 ? 0.7640 1.0836 0.7699 0.0893  -0.0967 0.0814  460 ARG A CD  
3052 N NE  . ARG A 445 ? 0.8355 1.1314 0.8345 0.0857  -0.0935 0.0898  460 ARG A NE  
3053 C CZ  . ARG A 445 ? 0.8960 1.1834 0.8817 0.0841  -0.0928 0.1010  460 ARG A CZ  
3054 N NH1 . ARG A 445 ? 0.9134 1.2120 0.8884 0.0859  -0.0958 0.1043  460 ARG A NH1 
3055 N NH2 . ARG A 445 ? 0.9428 1.2100 0.9254 0.0801  -0.0891 0.1093  460 ARG A NH2 
3056 N N   . PHE A 446 ? 0.5996 0.8888 0.6380 0.0940  -0.0894 0.0453  461 PHE A N   
3057 C CA  . PHE A 446 ? 0.5942 0.8591 0.6332 0.0921  -0.0902 0.0419  461 PHE A CA  
3058 C C   . PHE A 446 ? 0.5757 0.8433 0.6184 0.0965  -0.0896 0.0285  461 PHE A C   
3059 O O   . PHE A 446 ? 0.5419 0.8315 0.5868 0.0954  -0.0858 0.0223  461 PHE A O   
3060 C CB  . PHE A 446 ? 0.6025 0.8597 0.6397 0.0774  -0.0868 0.0464  461 PHE A CB  
3061 C CG  . PHE A 446 ? 0.6294 0.8832 0.6609 0.0723  -0.0857 0.0599  461 PHE A CG  
3062 C CD1 . PHE A 446 ? 0.6684 0.9001 0.6975 0.0745  -0.0887 0.0693  461 PHE A CD1 
3063 C CD2 . PHE A 446 ? 0.6194 0.8908 0.6469 0.0655  -0.0815 0.0633  461 PHE A CD2 
3064 C CE1 . PHE A 446 ? 0.6827 0.9117 0.7047 0.0703  -0.0868 0.0825  461 PHE A CE1 
3065 C CE2 . PHE A 446 ? 0.6260 0.8942 0.6458 0.0620  -0.0801 0.0752  461 PHE A CE2 
3066 C CZ  . PHE A 446 ? 0.6621 0.9099 0.6788 0.0645  -0.0823 0.0852  461 PHE A CZ  
3067 N N   . SER A 447 ? 0.5919 0.8353 0.6344 0.1009  -0.0935 0.0243  462 SER A N   
3068 C CA  . SER A 447 ? 0.5908 0.8295 0.6335 0.1047  -0.0939 0.0111  462 SER A CA  
3069 C C   . SER A 447 ? 0.5874 0.8059 0.6299 0.0922  -0.0955 0.0103  462 SER A C   
3070 O O   . SER A 447 ? 0.5829 0.7789 0.6262 0.0874  -0.0991 0.0179  462 SER A O   
3071 C CB  . SER A 447 ? 0.6156 0.8406 0.6576 0.1214  -0.0988 0.0053  462 SER A CB  
3072 O OG  . SER A 447 ? 0.6128 0.8484 0.6540 0.1308  -0.0970 -0.0078 462 SER A OG  
3073 N N   . PHE A 448 ? 0.5776 0.8053 0.6198 0.0868  -0.0930 0.0019  463 PHE A N   
3074 C CA  . PHE A 448 ? 0.5711 0.7854 0.6150 0.0744  -0.0947 0.0006  463 PHE A CA  
3075 C C   . PHE A 448 ? 0.5964 0.7946 0.6372 0.0802  -0.1000 -0.0129 463 PHE A C   
3076 O O   . PHE A 448 ? 0.5891 0.8015 0.6257 0.0861  -0.0977 -0.0229 463 PHE A O   
3077 C CB  . PHE A 448 ? 0.5336 0.7702 0.5783 0.0642  -0.0889 0.0008  463 PHE A CB  
3078 C CG  . PHE A 448 ? 0.5161 0.7690 0.5615 0.0589  -0.0839 0.0121  463 PHE A CG  
3079 C CD1 . PHE A 448 ? 0.5059 0.7788 0.5497 0.0661  -0.0812 0.0131  463 PHE A CD1 
3080 C CD2 . PHE A 448 ? 0.5054 0.7542 0.5533 0.0471  -0.0822 0.0217  463 PHE A CD2 
3081 C CE1 . PHE A 448 ? 0.4904 0.7765 0.5332 0.0616  -0.0782 0.0224  463 PHE A CE1 
3082 C CE2 . PHE A 448 ? 0.5042 0.7668 0.5499 0.0438  -0.0778 0.0311  463 PHE A CE2 
3083 C CZ  . PHE A 448 ? 0.4857 0.7659 0.5280 0.0510  -0.0764 0.0310  463 PHE A CZ  
3084 N N   . SER A 449 ? 0.6326 0.8011 0.6750 0.0784  -0.1073 -0.0129 464 SER A N   
3085 C CA  . SER A 449 ? 0.6736 0.8225 0.7118 0.0837  -0.1144 -0.0267 464 SER A CA  
3086 C C   . SER A 449 ? 0.7297 0.8598 0.7736 0.0692  -0.1202 -0.0261 464 SER A C   
3087 O O   . SER A 449 ? 0.7436 0.8730 0.7960 0.0562  -0.1186 -0.0136 464 SER A O   
3088 C CB  . SER A 449 ? 0.6920 0.8185 0.7262 0.0987  -0.1204 -0.0307 464 SER A CB  
3089 O OG  . SER A 449 ? 0.7065 0.8088 0.7460 0.0933  -0.1253 -0.0197 464 SER A OG  
3090 N N   . CYS A 450 ? 0.7947 0.9104 0.8341 0.0718  -0.1272 -0.0399 465 CYS A N   
3091 C CA  . CYS A 450 ? 0.8556 0.9511 0.9016 0.0590  -0.1353 -0.0411 465 CYS A CA  
3092 C C   . CYS A 450 ? 0.8461 0.9077 0.8961 0.0596  -0.1438 -0.0368 465 CYS A C   
3093 O O   . CYS A 450 ? 0.8586 0.9070 0.9009 0.0745  -0.1466 -0.0420 465 CYS A O   
3094 C CB  . CYS A 450 ? 0.9442 1.0349 0.9813 0.0635  -0.1412 -0.0586 465 CYS A CB  
3095 S SG  . CYS A 450 ? 1.1572 1.2418 1.1773 0.0880  -0.1424 -0.0736 465 CYS A SG  
3096 N N   . PRO A 451 ? 0.8300 0.8778 0.8928 0.0437  -0.1476 -0.0267 466 PRO A N   
3097 C CA  . PRO A 451 ? 0.8484 0.8608 0.9159 0.0425  -0.1567 -0.0218 466 PRO A CA  
3098 C C   . PRO A 451 ? 0.8580 0.8386 0.9218 0.0459  -0.1709 -0.0375 466 PRO A C   
3099 O O   . PRO A 451 ? 0.8274 0.8067 0.8773 0.0608  -0.1733 -0.0536 466 PRO A O   
3100 C CB  . PRO A 451 ? 0.8427 0.8561 0.9267 0.0228  -0.1546 -0.0046 466 PRO A CB  
3101 C CG  . PRO A 451 ? 0.8140 0.8645 0.9000 0.0167  -0.1431 0.0002  466 PRO A CG  
3102 C CD  . PRO A 451 ? 0.8041 0.8710 0.8784 0.0268  -0.1419 -0.0161 466 PRO A CD  
3103 N N   . SER A 455 ? 0.9078 0.9098 0.9659 0.0279  -0.1882 -0.0801 470 SER A N   
3104 C CA  . SER A 455 ? 0.9170 0.9374 0.9647 0.0309  -0.1876 -0.0923 470 SER A CA  
3105 C C   . SER A 455 ? 0.8924 0.9526 0.9414 0.0285  -0.1722 -0.0832 470 SER A C   
3106 O O   . SER A 455 ? 0.8783 0.9519 0.9424 0.0162  -0.1656 -0.0676 470 SER A O   
3107 C CB  . SER A 455 ? 0.9284 0.9361 0.9848 0.0175  -0.2009 -0.0982 470 SER A CB  
3108 O OG  . SER A 455 ? 0.9002 0.9320 0.9509 0.0165  -0.1983 -0.1043 470 SER A OG  
3109 N N   . LEU A 456 ? 0.8953 0.9732 0.9280 0.0402  -0.1670 -0.0932 471 LEU A N   
3110 C CA  . LEU A 456 ? 0.8575 0.9707 0.8885 0.0411  -0.1527 -0.0860 471 LEU A CA  
3111 C C   . LEU A 456 ? 0.8161 0.9482 0.8572 0.0264  -0.1506 -0.0801 471 LEU A C   
3112 O O   . LEU A 456 ? 0.8068 0.9312 0.8490 0.0205  -0.1600 -0.0877 471 LEU A O   
3113 C CB  . LEU A 456 ? 0.8680 0.9936 0.8792 0.0576  -0.1481 -0.0979 471 LEU A CB  
3114 C CG  . LEU A 456 ? 0.8958 1.0134 0.8963 0.0756  -0.1461 -0.1031 471 LEU A CG  
3115 C CD1 . LEU A 456 ? 0.9042 1.0267 0.8845 0.0915  -0.1453 -0.1185 471 LEU A CD1 
3116 C CD2 . LEU A 456 ? 0.8764 1.0149 0.8830 0.0777  -0.1340 -0.0900 471 LEU A CD2 
3117 N N   . PRO A 457 ? 0.7568 0.9137 0.8045 0.0213  -0.1389 -0.0673 472 PRO A N   
3118 C CA  . PRO A 457 ? 0.7081 0.8831 0.7657 0.0087  -0.1361 -0.0610 472 PRO A CA  
3119 C C   . PRO A 457 ? 0.6938 0.8798 0.7405 0.0117  -0.1379 -0.0719 472 PRO A C   
3120 O O   . PRO A 457 ? 0.7028 0.8904 0.7328 0.0243  -0.1368 -0.0817 472 PRO A O   
3121 C CB  . PRO A 457 ? 0.6641 0.8615 0.7245 0.0078  -0.1230 -0.0481 472 PRO A CB  
3122 C CG  . PRO A 457 ? 0.6745 0.8724 0.7229 0.0219  -0.1187 -0.0512 472 PRO A CG  
3123 C CD  . PRO A 457 ? 0.7232 0.8922 0.7691 0.0279  -0.1284 -0.0586 472 PRO A CD  
3124 N N   . ASP A 458 ? 0.6656 0.8605 0.7222 0.0003  -0.1402 -0.0690 473 ASP A N   
3125 C CA  . ASP A 458 ? 0.6539 0.8565 0.7019 0.0013  -0.1442 -0.0783 473 ASP A CA  
3126 C C   . ASP A 458 ? 0.5974 0.8269 0.6393 0.0037  -0.1322 -0.0731 473 ASP A C   
3127 O O   . ASP A 458 ? 0.5936 0.8374 0.6473 -0.0044 -0.1254 -0.0615 473 ASP A O   
3128 C CB  . ASP A 458 ? 0.6713 0.8712 0.7359 -0.0125 -0.1531 -0.0765 473 ASP A CB  
3129 C CG  . ASP A 458 ? 0.7144 0.9176 0.7695 -0.0110 -0.1609 -0.0877 473 ASP A CG  
3130 O OD1 . ASP A 458 ? 0.7319 0.9307 0.7658 0.0011  -0.1627 -0.0995 473 ASP A OD1 
3131 O OD2 . ASP A 458 ? 0.7625 0.9732 0.8315 -0.0216 -0.1653 -0.0844 473 ASP A OD2 
3132 N N   . LEU A 459 ? 0.5700 0.8063 0.5935 0.0148  -0.1296 -0.0815 474 LEU A N   
3133 C CA  . LEU A 459 ? 0.5506 0.8113 0.5680 0.0173  -0.1183 -0.0763 474 LEU A CA  
3134 C C   . LEU A 459 ? 0.5536 0.8269 0.5674 0.0133  -0.1195 -0.0779 474 LEU A C   
3135 O O   . LEU A 459 ? 0.5378 0.8277 0.5423 0.0171  -0.1120 -0.0762 474 LEU A O   
3136 C CB  . LEU A 459 ? 0.5401 0.8049 0.5417 0.0314  -0.1123 -0.0813 474 LEU A CB  
3137 C CG  . LEU A 459 ? 0.5356 0.7916 0.5410 0.0367  -0.1100 -0.0785 474 LEU A CG  
3138 C CD1 . LEU A 459 ? 0.5497 0.8086 0.5400 0.0521  -0.1062 -0.0860 474 LEU A CD1 
3139 C CD2 . LEU A 459 ? 0.5070 0.7762 0.5242 0.0305  -0.1016 -0.0646 474 LEU A CD2 
3140 N N   . GLN A 460 ? 0.5956 0.8614 0.6179 0.0053  -0.1292 -0.0802 475 GLN A N   
3141 C CA  . GLN A 460 ? 0.6335 0.9109 0.6534 0.0018  -0.1315 -0.0814 475 GLN A CA  
3142 C C   . GLN A 460 ? 0.6040 0.9001 0.6353 -0.0055 -0.1226 -0.0689 475 GLN A C   
3143 O O   . GLN A 460 ? 0.6067 0.9174 0.6294 -0.0031 -0.1169 -0.0670 475 GLN A O   
3144 C CB  . GLN A 460 ? 0.6721 0.9371 0.7000 -0.0047 -0.1457 -0.0875 475 GLN A CB  
3145 C CG  . GLN A 460 ? 0.7168 0.9949 0.7459 -0.0091 -0.1488 -0.0870 475 GLN A CG  
3146 C CD  . GLN A 460 ? 0.7976 1.0704 0.8468 -0.0202 -0.1603 -0.0867 475 GLN A CD  
3147 O OE1 . GLN A 460 ? 0.8572 1.1113 0.9115 -0.0225 -0.1710 -0.0929 475 GLN A OE1 
3148 N NE2 . GLN A 460 ? 0.8004 1.0898 0.8622 -0.0271 -0.1587 -0.0794 475 GLN A NE2 
3149 N N   . GLY A 461 ? 0.5742 0.8690 0.6244 -0.0143 -0.1218 -0.0603 476 GLY A N   
3150 C CA  . GLY A 461 ? 0.5768 0.8877 0.6372 -0.0203 -0.1137 -0.0491 476 GLY A CA  
3151 C C   . GLY A 461 ? 0.6062 0.9228 0.6818 -0.0292 -0.1188 -0.0463 476 GLY A C   
3152 O O   . GLY A 461 ? 0.6529 0.9662 0.7274 -0.0299 -0.1285 -0.0538 476 GLY A O   
3153 N N   . ARG A 462 ? 0.6115 0.9382 0.7010 -0.0352 -0.1120 -0.0353 477 ARG A N   
3154 C CA  . ARG A 462 ? 0.6181 0.9535 0.7257 -0.0434 -0.1144 -0.0302 477 ARG A CA  
3155 C C   . ARG A 462 ? 0.5609 0.9133 0.6662 -0.0420 -0.1044 -0.0232 477 ARG A C   
3156 O O   . ARG A 462 ? 0.5364 0.8909 0.6329 -0.0382 -0.0958 -0.0193 477 ARG A O   
3157 C CB  . ARG A 462 ? 0.6961 1.0261 0.8229 -0.0511 -0.1139 -0.0222 477 ARG A CB  
3158 C CG  . ARG A 462 ? 0.7508 1.0916 0.9005 -0.0603 -0.1156 -0.0155 477 ARG A CG  
3159 C CD  . ARG A 462 ? 0.8401 1.1689 1.0046 -0.0675 -0.1287 -0.0198 477 ARG A CD  
3160 N NE  . ARG A 462 ? 0.9211 1.2365 1.0960 -0.0727 -0.1286 -0.0139 477 ARG A NE  
3161 C CZ  . ARG A 462 ? 0.9751 1.2978 1.1684 -0.0799 -0.1214 -0.0005 477 ARG A CZ  
3162 N NH1 . ARG A 462 ? 0.9741 1.3182 1.1771 -0.0819 -0.1133 0.0078  477 ARG A NH1 
3163 N NH2 . ARG A 462 ? 0.9842 1.2921 1.1853 -0.0845 -0.1221 0.0050  477 ARG A NH2 
3164 N N   . PHE A 463 ? 0.5424 0.9062 0.6558 -0.0449 -0.1062 -0.0217 478 PHE A N   
3165 C CA  . PHE A 463 ? 0.5095 0.8874 0.6205 -0.0429 -0.0976 -0.0155 478 PHE A CA  
3166 C C   . PHE A 463 ? 0.4811 0.8689 0.6113 -0.0483 -0.0920 -0.0053 478 PHE A C   
3167 O O   . PHE A 463 ? 0.4693 0.8641 0.6163 -0.0531 -0.0962 -0.0036 478 PHE A O   
3168 C CB  . PHE A 463 ? 0.5107 0.8951 0.6146 -0.0400 -0.1022 -0.0204 478 PHE A CB  
3169 C CG  . PHE A 463 ? 0.5213 0.9158 0.6183 -0.0366 -0.0943 -0.0156 478 PHE A CG  
3170 C CD1 . PHE A 463 ? 0.5124 0.9047 0.5921 -0.0318 -0.0884 -0.0158 478 PHE A CD1 
3171 C CD2 . PHE A 463 ? 0.5499 0.9562 0.6588 -0.0382 -0.0929 -0.0106 478 PHE A CD2 
3172 C CE1 . PHE A 463 ? 0.5180 0.9173 0.5915 -0.0293 -0.0822 -0.0116 478 PHE A CE1 
3173 C CE2 . PHE A 463 ? 0.5509 0.9639 0.6521 -0.0342 -0.0862 -0.0069 478 PHE A CE2 
3174 C CZ  . PHE A 463 ? 0.5237 0.9320 0.6068 -0.0302 -0.0813 -0.0076 478 PHE A CZ  
3175 N N   . GLY A 464 ? 0.4942 0.8833 0.6217 -0.0472 -0.0823 0.0017  479 GLY A N   
3176 C CA  . GLY A 464 ? 0.4757 0.8760 0.6163 -0.0499 -0.0746 0.0118  479 GLY A CA  
3177 C C   . GLY A 464 ? 0.4308 0.8420 0.5634 -0.0448 -0.0698 0.0124  479 GLY A C   
3178 O O   . GLY A 464 ? 0.4145 0.8313 0.5490 -0.0440 -0.0749 0.0084  479 GLY A O   
3179 N N   . VAL A 465 ? 0.3932 0.8060 0.5161 -0.0411 -0.0610 0.0170  480 VAL A N   
3180 C CA  . VAL A 465 ? 0.3615 0.7792 0.4715 -0.0355 -0.0575 0.0160  480 VAL A CA  
3181 C C   . VAL A 465 ? 0.3414 0.7503 0.4323 -0.0321 -0.0590 0.0106  480 VAL A C   
3182 O O   . VAL A 465 ? 0.3335 0.7438 0.4130 -0.0285 -0.0576 0.0092  480 VAL A O   
3183 C CB  . VAL A 465 ? 0.3599 0.7840 0.4694 -0.0330 -0.0480 0.0235  480 VAL A CB  
3184 C CG1 . VAL A 465 ? 0.3715 0.8058 0.5017 -0.0367 -0.0451 0.0303  480 VAL A CG1 
3185 C CG2 . VAL A 465 ? 0.3601 0.7767 0.4592 -0.0318 -0.0434 0.0263  480 VAL A CG2 
3186 N N   . VAL A 466 ? 0.3342 0.7343 0.4230 -0.0332 -0.0617 0.0080  481 VAL A N   
3187 C CA  . VAL A 466 ? 0.3315 0.7254 0.4057 -0.0299 -0.0637 0.0023  481 VAL A CA  
3188 C C   . VAL A 466 ? 0.3368 0.7225 0.4134 -0.0310 -0.0710 -0.0039 481 VAL A C   
3189 O O   . VAL A 466 ? 0.3420 0.7251 0.4321 -0.0352 -0.0746 -0.0031 481 VAL A O   
3190 C CB  . VAL A 466 ? 0.3483 0.7391 0.4150 -0.0277 -0.0585 0.0056  481 VAL A CB  
3191 C CG1 . VAL A 466 ? 0.3503 0.7466 0.4098 -0.0256 -0.0530 0.0095  481 VAL A CG1 
3192 C CG2 . VAL A 466 ? 0.3531 0.7390 0.4292 -0.0302 -0.0569 0.0105  481 VAL A CG2 
3193 N N   . LEU A 467 ? 0.3363 0.7181 0.4002 -0.0270 -0.0732 -0.0099 482 LEU A N   
3194 C CA  . LEU A 467 ? 0.3456 0.7176 0.4079 -0.0258 -0.0796 -0.0169 482 LEU A CA  
3195 C C   . LEU A 467 ? 0.3769 0.7406 0.4401 -0.0245 -0.0775 -0.0154 482 LEU A C   
3196 O O   . LEU A 467 ? 0.3918 0.7576 0.4470 -0.0207 -0.0724 -0.0136 482 LEU A O   
3197 C CB  . LEU A 467 ? 0.3312 0.7035 0.3781 -0.0204 -0.0817 -0.0238 482 LEU A CB  
3198 C CG  . LEU A 467 ? 0.3381 0.6997 0.3798 -0.0169 -0.0880 -0.0323 482 LEU A CG  
3199 C CD1 . LEU A 467 ? 0.3392 0.6953 0.3876 -0.0202 -0.0978 -0.0375 482 LEU A CD1 
3200 C CD2 . LEU A 467 ? 0.3447 0.7090 0.3691 -0.0099 -0.0862 -0.0369 482 LEU A CD2 
3201 N N   . GLN A 468 ? 0.4101 0.7641 0.4835 -0.0278 -0.0823 -0.0160 483 GLN A N   
3202 C CA  . GLN A 468 ? 0.4407 0.7859 0.5167 -0.0272 -0.0803 -0.0125 483 GLN A CA  
3203 C C   . GLN A 468 ? 0.4827 0.8121 0.5632 -0.0280 -0.0885 -0.0180 483 GLN A C   
3204 O O   . GLN A 468 ? 0.4976 0.8238 0.5855 -0.0322 -0.0959 -0.0219 483 GLN A O   
3205 C CB  . GLN A 468 ? 0.4497 0.7997 0.5363 -0.0321 -0.0744 -0.0016 483 GLN A CB  
3206 C CG  . GLN A 468 ? 0.4936 0.8445 0.5975 -0.0398 -0.0775 0.0019  483 GLN A CG  
3207 C CD  . GLN A 468 ? 0.5273 0.8883 0.6396 -0.0431 -0.0693 0.0130  483 GLN A CD  
3208 O OE1 . GLN A 468 ? 0.5521 0.9137 0.6574 -0.0402 -0.0626 0.0186  483 GLN A OE1 
3209 N NE2 . GLN A 468 ? 0.5216 0.8913 0.6485 -0.0485 -0.0700 0.0161  483 GLN A NE2 
3210 N N   . PRO A 469 ? 0.5156 0.8345 0.5921 -0.0237 -0.0882 -0.0184 484 PRO A N   
3211 C CA  . PRO A 469 ? 0.5508 0.8516 0.6294 -0.0230 -0.0966 -0.0245 484 PRO A CA  
3212 C C   . PRO A 469 ? 0.5977 0.8911 0.6941 -0.0325 -0.0995 -0.0175 484 PRO A C   
3213 O O   . PRO A 469 ? 0.6164 0.9179 0.7207 -0.0368 -0.0925 -0.0065 484 PRO A O   
3214 C CB  . PRO A 469 ? 0.5547 0.8487 0.6247 -0.0150 -0.0935 -0.0246 484 PRO A CB  
3215 C CG  . PRO A 469 ? 0.5379 0.8442 0.6087 -0.0159 -0.0842 -0.0141 484 PRO A CG  
3216 C CD  . PRO A 469 ? 0.5174 0.8399 0.5888 -0.0197 -0.0806 -0.0121 484 PRO A CD  
3217 N N   . GLU A 470 ? 0.6610 0.9391 0.7638 -0.0357 -0.1100 -0.0235 485 GLU A N   
3218 C CA  . GLU A 470 ? 0.7034 0.9734 0.8259 -0.0461 -0.1136 -0.0159 485 GLU A CA  
3219 C C   . GLU A 470 ? 0.7158 0.9752 0.8389 -0.0447 -0.1091 -0.0077 485 GLU A C   
3220 O O   . GLU A 470 ? 0.7075 0.9577 0.8171 -0.0355 -0.1091 -0.0128 485 GLU A O   
3221 C CB  . GLU A 470 ? 0.7487 1.0020 0.8779 -0.0502 -0.1278 -0.0250 485 GLU A CB  
3222 C CG  . GLU A 470 ? 0.7864 1.0465 0.9098 -0.0488 -0.1346 -0.0358 485 GLU A CG  
3223 C CD  . GLU A 470 ? 0.8242 1.0833 0.9670 -0.0598 -0.1451 -0.0362 485 GLU A CD  
3224 O OE1 . GLU A 470 ? 0.8126 1.0880 0.9581 -0.0615 -0.1456 -0.0372 485 GLU A OE1 
3225 O OE2 . GLU A 470 ? 0.8664 1.1088 1.0228 -0.0669 -0.1534 -0.0353 485 GLU A OE2 
3226 N N   . ARG A 471 ? 0.7144 0.9764 0.8534 -0.0534 -0.1051 0.0053  486 ARG A N   
3227 C CA  . ARG A 471 ? 0.7190 0.9705 0.8602 -0.0538 -0.1012 0.0156  486 ARG A CA  
3228 C C   . ARG A 471 ? 0.6870 0.9135 0.8212 -0.0483 -0.1100 0.0075  486 ARG A C   
3229 O O   . ARG A 471 ? 0.6508 0.8640 0.7891 -0.0508 -0.1210 -0.0016 486 ARG A O   
3230 C CB  . ARG A 471 ? 0.8150 1.0676 0.9782 -0.0664 -0.1001 0.0285  486 ARG A CB  
3231 C CG  . ARG A 471 ? 0.9578 1.2050 1.1235 -0.0678 -0.0929 0.0432  486 ARG A CG  
3232 C CD  . ARG A 471 ? 1.0730 1.3276 1.2607 -0.0802 -0.0889 0.0578  486 ARG A CD  
3233 N NE  . ARG A 471 ? 1.2409 1.4856 1.4307 -0.0821 -0.0837 0.0723  486 ARG A NE  
3234 C CZ  . ARG A 471 ? 1.3931 1.6466 1.5714 -0.0765 -0.0726 0.0816  486 ARG A CZ  
3235 N NH1 . ARG A 471 ? 1.4866 1.7585 1.6513 -0.0691 -0.0657 0.0778  486 ARG A NH1 
3236 N NH2 . ARG A 471 ? 1.4637 1.7063 1.6433 -0.0782 -0.0690 0.0950  486 ARG A NH2 
3237 N N   . TYR A 472 ? 0.6431 0.8633 0.7663 -0.0399 -0.1058 0.0101  487 TYR A N   
3238 C CA  . TYR A 472 ? 0.6504 0.8462 0.7670 -0.0330 -0.1136 0.0032  487 TYR A CA  
3239 C C   . TYR A 472 ? 0.6778 0.8632 0.7947 -0.0312 -0.1098 0.0150  487 TYR A C   
3240 O O   . TYR A 472 ? 0.6866 0.8865 0.8027 -0.0318 -0.1000 0.0263  487 TYR A O   
3241 C CB  . TYR A 472 ? 0.6326 0.8310 0.7309 -0.0196 -0.1147 -0.0109 487 TYR A CB  
3242 C CG  . TYR A 472 ? 0.6241 0.8435 0.7119 -0.0123 -0.1040 -0.0076 487 TYR A CG  
3243 C CD1 . TYR A 472 ? 0.6028 0.8449 0.6883 -0.0141 -0.0983 -0.0080 487 TYR A CD1 
3244 C CD2 . TYR A 472 ? 0.6282 0.8442 0.7088 -0.0036 -0.1006 -0.0040 487 TYR A CD2 
3245 C CE1 . TYR A 472 ? 0.5751 0.8346 0.6518 -0.0086 -0.0898 -0.0050 487 TYR A CE1 
3246 C CE2 . TYR A 472 ? 0.6007 0.8360 0.6733 0.0021  -0.0923 -0.0010 487 TYR A CE2 
3247 C CZ  . TYR A 472 ? 0.5835 0.8401 0.6544 -0.0008 -0.0871 -0.0017 487 TYR A CZ  
3248 O OH  . TYR A 472 ? 0.5433 0.8175 0.6069 0.0040  -0.0802 0.0010  487 TYR A OH  
3249 N N   . THR A 473 ? 0.6955 0.8543 0.8126 -0.0287 -0.1182 0.0122  488 THR A N   
3250 C CA  . THR A 473 ? 0.6922 0.8378 0.8060 -0.0237 -0.1162 0.0212  488 THR A CA  
3251 C C   . THR A 473 ? 0.6825 0.8267 0.7792 -0.0073 -0.1163 0.0114  488 THR A C   
3252 O O   . THR A 473 ? 0.7016 0.8405 0.7908 -0.0003 -0.1224 -0.0038 488 THR A O   
3253 C CB  . THR A 473 ? 0.7314 0.8454 0.8547 -0.0289 -0.1262 0.0241  488 THR A CB  
3254 O OG1 . THR A 473 ? 0.7408 0.8350 0.8565 -0.0211 -0.1374 0.0073  488 THR A OG1 
3255 C CG2 . THR A 473 ? 0.7416 0.8558 0.8856 -0.0464 -0.1279 0.0333  488 THR A CG2 
3256 N N   . VAL A 474 ? 0.6469 0.7959 0.7376 -0.0009 -0.1099 0.0201  489 VAL A N   
3257 C CA  . VAL A 474 ? 0.6368 0.7862 0.7146 0.0146  -0.1098 0.0132  489 VAL A CA  
3258 C C   . VAL A 474 ? 0.6530 0.7898 0.7290 0.0200  -0.1093 0.0240  489 VAL A C   
3259 O O   . VAL A 474 ? 0.6533 0.7964 0.7322 0.0143  -0.1035 0.0383  489 VAL A O   
3260 C CB  . VAL A 474 ? 0.6008 0.7802 0.6711 0.0192  -0.1016 0.0101  489 VAL A CB  
3261 C CG1 . VAL A 474 ? 0.5710 0.7689 0.6460 0.0093  -0.0936 0.0220  489 VAL A CG1 
3262 C CG2 . VAL A 474 ? 0.6024 0.7872 0.6633 0.0336  -0.0996 0.0084  489 VAL A CG2 
3263 N N   . THR A 475 ? 0.6811 0.8001 0.7510 0.0322  -0.1154 0.0169  490 THR A N   
3264 C CA  . THR A 475 ? 0.7031 0.8117 0.7694 0.0404  -0.1155 0.0257  490 THR A CA  
3265 C C   . THR A 475 ? 0.6996 0.8345 0.7583 0.0495  -0.1080 0.0280  490 THR A C   
3266 O O   . THR A 475 ? 0.6607 0.8113 0.7142 0.0584  -0.1066 0.0169  490 THR A O   
3267 C CB  . THR A 475 ? 0.7328 0.8130 0.7951 0.0519  -0.1251 0.0165  490 THR A CB  
3268 O OG1 . THR A 475 ? 0.7673 0.8196 0.8378 0.0418  -0.1333 0.0173  490 THR A OG1 
3269 C CG2 . THR A 475 ? 0.7488 0.8204 0.8066 0.0629  -0.1254 0.0249  490 THR A CG2 
3270 N N   . VAL A 476 ? 0.7219 0.8610 0.7802 0.0468  -0.1037 0.0430  491 VAL A N   
3271 C CA  . VAL A 476 ? 0.7234 0.8857 0.7752 0.0534  -0.0980 0.0475  491 VAL A CA  
3272 C C   . VAL A 476 ? 0.7403 0.8905 0.7875 0.0653  -0.1016 0.0534  491 VAL A C   
3273 O O   . VAL A 476 ? 0.7579 0.8896 0.8054 0.0620  -0.1033 0.0656  491 VAL A O   
3274 C CB  . VAL A 476 ? 0.7197 0.8970 0.7717 0.0423  -0.0907 0.0599  491 VAL A CB  
3275 C CG1 . VAL A 476 ? 0.7193 0.9221 0.7641 0.0481  -0.0862 0.0606  491 VAL A CG1 
3276 C CG2 . VAL A 476 ? 0.7008 0.8846 0.7597 0.0295  -0.0880 0.0569  491 VAL A CG2 
3277 N N   . THR A 477 ? 0.7454 0.9075 0.7888 0.0790  -0.1025 0.0458  492 THR A N   
3278 C CA  . THR A 477 ? 0.7664 0.9175 0.8064 0.0927  -0.1072 0.0494  492 THR A CA  
3279 C C   . THR A 477 ? 0.7608 0.9390 0.7982 0.1023  -0.1047 0.0493  492 THR A C   
3280 O O   . THR A 477 ? 0.7439 0.9430 0.7832 0.1059  -0.1021 0.0389  492 THR A O   
3281 C CB  . THR A 477 ? 0.7878 0.9192 0.8283 0.1039  -0.1137 0.0372  492 THR A CB  
3282 O OG1 . THR A 477 ? 0.7822 0.8976 0.8259 0.0941  -0.1160 0.0308  492 THR A OG1 
3283 C CG2 . THR A 477 ? 0.8099 0.9162 0.8483 0.1136  -0.1202 0.0441  492 THR A CG2 
3284 N N   . PRO A 478 ? 0.7959 0.9739 0.8293 0.1064  -0.1060 0.0612  493 PRO A N   
3285 C CA  . PRO A 478 ? 0.7758 0.9799 0.8080 0.1144  -0.1052 0.0618  493 PRO A CA  
3286 C C   . PRO A 478 ? 0.7754 0.9766 0.8094 0.1321  -0.1108 0.0581  493 PRO A C   
3287 O O   . PRO A 478 ? 0.7592 0.9402 0.7947 0.1387  -0.1143 0.0517  493 PRO A O   
3288 C CB  . PRO A 478 ? 0.7843 0.9873 0.8093 0.1088  -0.1044 0.0771  493 PRO A CB  
3289 C CG  . PRO A 478 ? 0.8107 0.9809 0.8337 0.1064  -0.1072 0.0858  493 PRO A CG  
3290 C CD  . PRO A 478 ? 0.8156 0.9697 0.8453 0.1032  -0.1084 0.0755  493 PRO A CD  
3291 N N   . ARG A 479 ? 0.8110 1.0310 0.8463 0.1390  -0.1114 0.0585  494 ARG A N   
3292 C CA  . ARG A 479 ? 0.8132 1.0298 0.8490 0.1553  -0.1177 0.0619  494 ARG A CA  
3293 C C   . ARG A 479 ? 0.8360 1.0300 0.8631 0.1535  -0.1216 0.0772  494 ARG A C   
3294 O O   . ARG A 479 ? 0.8387 1.0338 0.8632 0.1636  -0.1266 0.0845  494 ARG A O   
3295 C CB  . ARG A 479 ? 0.7751 1.0261 0.8164 0.1618  -0.1177 0.0604  494 ARG A CB  
3296 C CG  . ARG A 479 ? 0.6139 0.8657 0.6580 0.1792  -0.1245 0.0634  494 ARG A CG  
3297 C CD  . ARG A 479 ? 0.5966 0.8852 0.6508 0.1861  -0.1250 0.0603  494 ARG A CD  
3298 N NE  . ARG A 479 ? 0.5830 0.8898 0.6472 0.1896  -0.1198 0.0475  494 ARG A NE  
3299 C CZ  . ARG A 479 ? 0.5569 0.8877 0.6255 0.1794  -0.1139 0.0430  494 ARG A CZ  
3300 N NH1 . ARG A 479 ? 0.5416 0.8801 0.6057 0.1654  -0.1130 0.0491  494 ARG A NH1 
3301 N NH2 . ARG A 479 ? 0.5480 0.8944 0.6245 0.1838  -0.1088 0.0325  494 ARG A NH2 
3302 N N   . ASN B 38  ? 0.8675 1.1606 0.9211 -0.0051 -0.1888 0.0458  53  ASN B N   
3303 C CA  . ASN B 38  ? 0.8839 1.1503 0.9107 -0.0151 -0.1939 0.0488  53  ASN B CA  
3304 C C   . ASN B 38  ? 0.8552 1.1328 0.8603 -0.0237 -0.1758 0.0428  53  ASN B C   
3305 O O   . ASN B 38  ? 0.8549 1.1278 0.8564 -0.0268 -0.1709 0.0385  53  ASN B O   
3306 C CB  . ASN B 38  ? 0.9381 1.1737 0.9374 -0.0249 -0.2116 0.0597  53  ASN B CB  
3307 C CG  . ASN B 38  ? 0.9774 1.2181 0.9524 -0.0337 -0.2065 0.0620  53  ASN B CG  
3308 O OD1 . ASN B 38  ? 1.0087 1.2756 0.9933 -0.0291 -0.1929 0.0567  53  ASN B OD1 
3309 N ND2 . ASN B 38  ? 0.9905 1.2038 0.9316 -0.0464 -0.2171 0.0699  53  ASN B ND2 
3310 N N   . LEU B 39  ? 0.7985 1.0912 0.7898 -0.0273 -0.1664 0.0421  54  LEU B N   
3311 C CA  . LEU B 39  ? 0.7168 1.0282 0.6923 -0.0327 -0.1490 0.0355  54  LEU B CA  
3312 C C   . LEU B 39  ? 0.6667 1.0075 0.6576 -0.0220 -0.1373 0.0309  54  LEU B C   
3313 O O   . LEU B 39  ? 0.6988 1.0380 0.6930 -0.0184 -0.1420 0.0350  54  LEU B O   
3314 C CB  . LEU B 39  ? 0.7083 1.0061 0.6477 -0.0470 -0.1497 0.0394  54  LEU B CB  
3315 C CG  . LEU B 39  ? 0.7458 1.0159 0.6607 -0.0614 -0.1561 0.0425  54  LEU B CG  
3316 C CD1 . LEU B 39  ? 0.7605 1.0131 0.6388 -0.0763 -0.1590 0.0478  54  LEU B CD1 
3317 C CD2 . LEU B 39  ? 0.7570 1.0427 0.6714 -0.0658 -0.1420 0.0334  54  LEU B CD2 
3318 N N   . PRO B 40  ? 0.6022 0.9679 0.6003 -0.0176 -0.1226 0.0225  55  PRO B N   
3319 C CA  . PRO B 40  ? 0.5439 0.9334 0.5512 -0.0074 -0.1121 0.0192  55  PRO B CA  
3320 C C   . PRO B 40  ? 0.5250 0.9126 0.5089 -0.0113 -0.1101 0.0221  55  PRO B C   
3321 O O   . PRO B 40  ? 0.5435 0.9229 0.5037 -0.0223 -0.1104 0.0228  55  PRO B O   
3322 C CB  . PRO B 40  ? 0.5289 0.9429 0.5393 -0.0048 -0.0983 0.0103  55  PRO B CB  
3323 C CG  . PRO B 40  ? 0.5614 0.9646 0.5728 -0.0120 -0.1018 0.0081  55  PRO B CG  
3324 C CD  . PRO B 40  ? 0.6105 0.9831 0.6043 -0.0229 -0.1149 0.0159  55  PRO B CD  
3325 N N   . PRO B 41  ? 0.4951 0.8885 0.4837 -0.0033 -0.1076 0.0234  56  PRO B N   
3326 C CA  . PRO B 41  ? 0.4935 0.8819 0.4586 -0.0064 -0.1054 0.0255  56  PRO B CA  
3327 C C   . PRO B 41  ? 0.4903 0.8909 0.4348 -0.0109 -0.0951 0.0202  56  PRO B C   
3328 O O   . PRO B 41  ? 0.5581 0.9458 0.4794 -0.0214 -0.0976 0.0223  56  PRO B O   
3329 C CB  . PRO B 41  ? 0.4789 0.8773 0.4533 0.0051  -0.0990 0.0247  56  PRO B CB  
3330 C CG  . PRO B 41  ? 0.4611 0.8633 0.4647 0.0109  -0.1023 0.0246  56  PRO B CG  
3331 C CD  . PRO B 41  ? 0.4601 0.8637 0.4738 0.0077  -0.1052 0.0221  56  PRO B CD  
3332 N N   . HIS B 42  ? 0.4248 0.8509 0.3773 -0.0043 -0.0840 0.0130  57  HIS B N   
3333 C CA  . HIS B 42  ? 0.3994 0.8430 0.3360 -0.0077 -0.0742 0.0067  57  HIS B CA  
3334 C C   . HIS B 42  ? 0.4050 0.8360 0.3246 -0.0250 -0.0779 0.0072  57  HIS B C   
3335 O O   . HIS B 42  ? 0.4361 0.8680 0.3352 -0.0321 -0.0735 0.0053  57  HIS B O   
3336 C CB  . HIS B 42  ? 0.3817 0.8569 0.3307 0.0016  -0.0637 -0.0014 57  HIS B CB  
3337 C CG  . HIS B 42  ? 0.3668 0.8473 0.3289 -0.0032 -0.0645 -0.0048 57  HIS B CG  
3338 N ND1 . HIS B 42  ? 0.3524 0.8294 0.3350 0.0030  -0.0676 -0.0037 57  HIS B ND1 
3339 C CD2 . HIS B 42  ? 0.3637 0.8532 0.3207 -0.0141 -0.0614 -0.0103 57  HIS B CD2 
3340 C CE1 . HIS B 42  ? 0.3479 0.8290 0.3366 -0.0031 -0.0669 -0.0083 57  HIS B CE1 
3341 N NE2 . HIS B 42  ? 0.3603 0.8479 0.3329 -0.0141 -0.0635 -0.0120 57  HIS B NE2 
3342 N N   . LEU B 43  ? 0.3927 0.8094 0.3188 -0.0321 -0.0857 0.0095  58  LEU B N   
3343 C CA  . LEU B 43  ? 0.4154 0.8142 0.3212 -0.0496 -0.0898 0.0111  58  LEU B CA  
3344 C C   . LEU B 43  ? 0.4488 0.8170 0.3354 -0.0573 -0.1008 0.0198  58  LEU B C   
3345 O O   . LEU B 43  ? 0.4837 0.8381 0.3443 -0.0727 -0.1013 0.0209  58  LEU B O   
3346 C CB  . LEU B 43  ? 0.4151 0.8015 0.3305 -0.0543 -0.0959 0.0116  58  LEU B CB  
3347 C CG  . LEU B 43  ? 0.4022 0.8131 0.3313 -0.0520 -0.0862 0.0025  58  LEU B CG  
3348 C CD1 . LEU B 43  ? 0.4192 0.8063 0.3500 -0.0597 -0.0940 0.0042  58  LEU B CD1 
3349 C CD2 . LEU B 43  ? 0.4014 0.8388 0.3178 -0.0599 -0.0733 -0.0063 58  LEU B CD2 
3350 N N   . LEU B 44  ? 0.4452 0.8023 0.3431 -0.0484 -0.1096 0.0259  59  LEU B N   
3351 C CA  . LEU B 44  ? 0.4666 0.7941 0.3473 -0.0560 -0.1227 0.0346  59  LEU B CA  
3352 C C   . LEU B 44  ? 0.4645 0.7933 0.3196 -0.0611 -0.1153 0.0330  59  LEU B C   
3353 O O   . LEU B 44  ? 0.4717 0.7843 0.2996 -0.0755 -0.1171 0.0347  59  LEU B O   
3354 C CB  . LEU B 44  ? 0.4574 0.7776 0.3597 -0.0457 -0.1336 0.0401  59  LEU B CB  
3355 C CG  . LEU B 44  ? 0.4880 0.7770 0.3824 -0.0527 -0.1531 0.0498  59  LEU B CG  
3356 C CD1 . LEU B 44  ? 0.4779 0.7660 0.3840 -0.0458 -0.1594 0.0532  59  LEU B CD1 
3357 C CD2 . LEU B 44  ? 0.5188 0.7842 0.3753 -0.0695 -0.1575 0.0538  59  LEU B CD2 
3358 N N   . PHE B 45  ? 0.4647 0.8121 0.3278 -0.0489 -0.1060 0.0289  60  PHE B N   
3359 C CA  . PHE B 45  ? 0.4955 0.8449 0.3370 -0.0502 -0.0978 0.0260  60  PHE B CA  
3360 C C   . PHE B 45  ? 0.5073 0.8746 0.3344 -0.0569 -0.0848 0.0178  60  PHE B C   
3361 O O   . PHE B 45  ? 0.5345 0.9010 0.3407 -0.0611 -0.0782 0.0148  60  PHE B O   
3362 C CB  . PHE B 45  ? 0.5093 0.8728 0.3634 -0.0336 -0.0908 0.0235  60  PHE B CB  
3363 C CG  . PHE B 45  ? 0.5571 0.9050 0.4242 -0.0290 -0.1017 0.0304  60  PHE B CG  
3364 C CD1 . PHE B 45  ? 0.5951 0.9167 0.4460 -0.0377 -0.1124 0.0366  60  PHE B CD1 
3365 C CD2 . PHE B 45  ? 0.5374 0.8979 0.4324 -0.0171 -0.1011 0.0299  60  PHE B CD2 
3366 C CE1 . PHE B 45  ? 0.6098 0.9209 0.4748 -0.0346 -0.1226 0.0420  60  PHE B CE1 
3367 C CE2 . PHE B 45  ? 0.5452 0.8947 0.4536 -0.0142 -0.1098 0.0350  60  PHE B CE2 
3368 C CZ  . PHE B 45  ? 0.5728 0.8989 0.4676 -0.0230 -0.1208 0.0408  60  PHE B CZ  
3369 N N   . THR B 46  ? 0.5151 0.9000 0.3537 -0.0584 -0.0802 0.0131  61  THR B N   
3370 C CA  . THR B 46  ? 0.5465 0.9461 0.3703 -0.0701 -0.0698 0.0056  61  THR B CA  
3371 C C   . THR B 46  ? 0.6052 0.9730 0.4009 -0.0914 -0.0774 0.0112  61  THR B C   
3372 O O   . THR B 46  ? 0.6543 1.0219 0.4258 -0.1029 -0.0701 0.0074  61  THR B O   
3373 C CB  . THR B 46  ? 0.5214 0.9481 0.3643 -0.0677 -0.0634 -0.0013 61  THR B CB  
3374 O OG1 . THR B 46  ? 0.5029 0.9591 0.3651 -0.0486 -0.0556 -0.0067 61  THR B OG1 
3375 C CG2 . THR B 46  ? 0.5217 0.9638 0.3501 -0.0832 -0.0533 -0.0095 61  THR B CG2 
3376 N N   . GLN B 47  ? 0.6359 0.9763 0.4342 -0.0957 -0.0923 0.0200  62  GLN B N   
3377 C CA  . GLN B 47  ? 0.6841 0.9888 0.4546 -0.1147 -0.1029 0.0273  62  GLN B CA  
3378 C C   . GLN B 47  ? 0.6836 0.9673 0.4274 -0.1215 -0.1071 0.0319  62  GLN B C   
3379 O O   . GLN B 47  ? 0.6724 0.9387 0.3838 -0.1398 -0.1061 0.0327  62  GLN B O   
3380 C CB  . GLN B 47  ? 0.7308 1.0107 0.5143 -0.1118 -0.1204 0.0364  62  GLN B CB  
3381 C CG  . GLN B 47  ? 0.8165 1.0703 0.5809 -0.1285 -0.1268 0.0400  62  GLN B CG  
3382 C CD  . GLN B 47  ? 0.8617 1.1350 0.6413 -0.1285 -0.1173 0.0322  62  GLN B CD  
3383 O OE1 . GLN B 47  ? 0.8534 1.1525 0.6645 -0.1127 -0.1127 0.0272  62  GLN B OE1 
3384 N NE2 . GLN B 47  ? 0.9399 1.1990 0.6949 -0.1479 -0.1144 0.0309  62  GLN B NE2 
3385 N N   . LEU B 48  ? 0.6711 0.9552 0.4270 -0.1079 -0.1115 0.0347  63  LEU B N   
3386 C CA  . LEU B 48  ? 0.7109 0.9734 0.4427 -0.1136 -0.1168 0.0390  63  LEU B CA  
3387 C C   . LEU B 48  ? 0.7348 1.0111 0.4458 -0.1179 -0.0998 0.0301  63  LEU B C   
3388 O O   . LEU B 48  ? 0.7458 1.0011 0.4243 -0.1325 -0.1009 0.0318  63  LEU B O   
3389 C CB  . LEU B 48  ? 0.6944 0.9545 0.4459 -0.0990 -0.1252 0.0434  63  LEU B CB  
3390 C CG  . LEU B 48  ? 0.6903 0.9383 0.4652 -0.0936 -0.1429 0.0516  63  LEU B CG  
3391 C CD1 . LEU B 48  ? 0.6701 0.9210 0.4639 -0.0813 -0.1476 0.0537  63  LEU B CD1 
3392 C CD2 . LEU B 48  ? 0.7241 0.9372 0.4783 -0.1081 -0.1611 0.0613  63  LEU B CD2 
3393 N N   . SER B 49  ? 0.7402 1.0518 0.4697 -0.1046 -0.0844 0.0202  64  SER B N   
3394 C CA  . SER B 49  ? 0.7606 1.0912 0.4759 -0.1052 -0.0672 0.0098  64  SER B CA  
3395 C C   . SER B 49  ? 0.7678 1.0885 0.4505 -0.1278 -0.0619 0.0070  64  SER B C   
3396 O O   . SER B 49  ? 0.7687 1.0826 0.4270 -0.1342 -0.0551 0.0033  64  SER B O   
3397 C CB  . SER B 49  ? 0.7759 1.1484 0.5165 -0.0912 -0.0536 -0.0003 64  SER B CB  
3398 O OG  . SER B 49  ? 0.7899 1.1711 0.5547 -0.0703 -0.0558 0.0013  64  SER B OG  
3399 N N   . SER B 50  ? 0.7515 1.0702 0.4326 -0.1408 -0.0641 0.0081  65  SER B N   
3400 C CA  . SER B 50  ? 0.7908 1.0946 0.4379 -0.1655 -0.0601 0.0069  65  SER B CA  
3401 C C   . SER B 50  ? 0.7999 1.0667 0.4125 -0.1771 -0.0682 0.0139  65  SER B C   
3402 O O   . SER B 50  ? 0.8218 1.0892 0.4083 -0.1884 -0.0566 0.0073  65  SER B O   
3403 C CB  . SER B 50  ? 0.8175 1.1048 0.4631 -0.1779 -0.0693 0.0129  65  SER B CB  
3404 O OG  . SER B 50  ? 0.8450 1.1534 0.5278 -0.1612 -0.0712 0.0119  65  SER B OG  
3405 N N   . GLN B 51  ? 0.7883 1.0247 0.4021 -0.1738 -0.0881 0.0264  66  GLN B N   
3406 C CA  . GLN B 51  ? 0.8191 1.0131 0.3962 -0.1901 -0.1016 0.0360  66  GLN B CA  
3407 C C   . GLN B 51  ? 0.7713 0.9565 0.3437 -0.1819 -0.1055 0.0375  66  GLN B C   
3408 O O   . GLN B 51  ? 0.8052 0.9748 0.3439 -0.1945 -0.1014 0.0358  66  GLN B O   
3409 C CB  . GLN B 51  ? 0.8587 1.0210 0.4347 -0.1957 -0.1235 0.0493  66  GLN B CB  
3410 C CG  . GLN B 51  ? 0.8397 1.0165 0.4593 -0.1767 -0.1311 0.0517  66  GLN B CG  
3411 C CD  . GLN B 51  ? 0.8722 1.0208 0.4897 -0.1830 -0.1484 0.0616  66  GLN B CD  
3412 O OE1 . GLN B 51  ? 0.9617 1.0753 0.5432 -0.2014 -0.1575 0.0688  66  GLN B OE1 
3413 N NE2 . GLN B 51  ? 0.8402 1.0021 0.4949 -0.1674 -0.1529 0.0621  66  GLN B NE2 
3414 N N   . TYR B 52  ? 0.6979 0.8935 0.3029 -0.1619 -0.1116 0.0397  67  TYR B N   
3415 C CA  . TYR B 52  ? 0.6866 0.8804 0.2911 -0.1522 -0.1106 0.0383  67  TYR B CA  
3416 C C   . TYR B 52  ? 0.6674 0.8956 0.2826 -0.1400 -0.0881 0.0249  67  TYR B C   
3417 O O   . TYR B 52  ? 0.7065 0.9568 0.3252 -0.1430 -0.0760 0.0178  67  TYR B O   
3418 C CB  . TYR B 52  ? 0.6533 0.8423 0.2864 -0.1386 -0.1267 0.0464  67  TYR B CB  
3419 C CG  . TYR B 52  ? 0.6637 0.8231 0.2888 -0.1496 -0.1490 0.0585  67  TYR B CG  
3420 C CD1 . TYR B 52  ? 0.6924 0.8206 0.2891 -0.1616 -0.1629 0.0655  67  TYR B CD1 
3421 C CD2 . TYR B 52  ? 0.6557 0.8169 0.2980 -0.1488 -0.1561 0.0624  67  TYR B CD2 
3422 C CE1 . TYR B 52  ? 0.7145 0.8150 0.3022 -0.1706 -0.1849 0.0769  67  TYR B CE1 
3423 C CE2 . TYR B 52  ? 0.6766 0.8080 0.3098 -0.1573 -0.1773 0.0736  67  TYR B CE2 
3424 C CZ  . TYR B 52  ? 0.7158 0.8175 0.3219 -0.1676 -0.1922 0.0810  67  TYR B CZ  
3425 O OH  . TYR B 52  ? 0.7653 0.8363 0.3605 -0.1750 -0.2155 0.0928  67  TYR B OH  
3426 N N   . GLY B 53  ? 0.6604 0.8942 0.2807 -0.1264 -0.0821 0.0208  68  GLY B N   
3427 C CA  . GLY B 53  ? 0.6591 0.9274 0.2924 -0.1113 -0.0617 0.0081  68  GLY B CA  
3428 C C   . GLY B 53  ? 0.6103 0.9121 0.2818 -0.0939 -0.0575 0.0052  68  GLY B C   
3429 O O   . GLY B 53  ? 0.5950 0.8936 0.2869 -0.0911 -0.0696 0.0129  68  GLY B O   
3430 N N   . PRO B 54  ? 0.5932 0.9272 0.2747 -0.0808 -0.0406 -0.0062 69  PRO B N   
3431 C CA  . PRO B 54  ? 0.5526 0.9185 0.2678 -0.0617 -0.0364 -0.0095 69  PRO B CA  
3432 C C   . PRO B 54  ? 0.5364 0.8982 0.2656 -0.0418 -0.0390 -0.0065 69  PRO B C   
3433 O O   . PRO B 54  ? 0.5430 0.9277 0.2957 -0.0257 -0.0354 -0.0089 69  PRO B O   
3434 C CB  . PRO B 54  ? 0.5483 0.9484 0.2636 -0.0564 -0.0184 -0.0233 69  PRO B CB  
3435 C CG  . PRO B 54  ? 0.5808 0.9644 0.2676 -0.0608 -0.0117 -0.0275 69  PRO B CG  
3436 C CD  . PRO B 54  ? 0.6105 0.9526 0.2719 -0.0813 -0.0250 -0.0171 69  PRO B CD  
3437 N N   . LEU B 55  ? 0.5645 0.8960 0.2775 -0.0441 -0.0453 -0.0013 70  LEU B N   
3438 C CA  . LEU B 55  ? 0.5568 0.8795 0.2780 -0.0286 -0.0469 0.0014  70  LEU B CA  
3439 C C   . LEU B 55  ? 0.5741 0.8654 0.2908 -0.0392 -0.0632 0.0120  70  LEU B C   
3440 O O   . LEU B 55  ? 0.6127 0.8793 0.3036 -0.0521 -0.0674 0.0138  70  LEU B O   
3441 C CB  . LEU B 55  ? 0.5743 0.8930 0.2758 -0.0200 -0.0346 -0.0064 70  LEU B CB  
3442 C CG  . LEU B 55  ? 0.5871 0.8813 0.2807 -0.0113 -0.0363 -0.0035 70  LEU B CG  
3443 C CD1 . LEU B 55  ? 0.5689 0.8772 0.2856 0.0091  -0.0338 -0.0029 70  LEU B CD1 
3444 C CD2 . LEU B 55  ? 0.6176 0.9000 0.2832 -0.0088 -0.0250 -0.0118 70  LEU B CD2 
3445 N N   . PHE B 56  ? 0.5593 0.8536 0.3016 -0.0338 -0.0721 0.0182  71  PHE B N   
3446 C CA  . PHE B 56  ? 0.5623 0.8345 0.3091 -0.0425 -0.0888 0.0276  71  PHE B CA  
3447 C C   . PHE B 56  ? 0.5443 0.8088 0.2995 -0.0327 -0.0895 0.0294  71  PHE B C   
3448 O O   . PHE B 56  ? 0.5346 0.8151 0.3057 -0.0175 -0.0809 0.0265  71  PHE B O   
3449 C CB  . PHE B 56  ? 0.5577 0.8416 0.3315 -0.0430 -0.0976 0.0319  71  PHE B CB  
3450 C CG  . PHE B 56  ? 0.5916 0.8609 0.3551 -0.0596 -0.1098 0.0372  71  PHE B CG  
3451 C CD1 . PHE B 56  ? 0.6155 0.8919 0.3667 -0.0678 -0.1039 0.0335  71  PHE B CD1 
3452 C CD2 . PHE B 56  ? 0.6199 0.8682 0.3859 -0.0672 -0.1278 0.0458  71  PHE B CD2 
3453 C CE1 . PHE B 56  ? 0.6406 0.8983 0.3776 -0.0842 -0.1155 0.0393  71  PHE B CE1 
3454 C CE2 . PHE B 56  ? 0.6356 0.8667 0.3894 -0.0814 -0.1410 0.0518  71  PHE B CE2 
3455 C CZ  . PHE B 56  ? 0.6433 0.8768 0.3808 -0.0901 -0.1346 0.0489  71  PHE B CZ  
3456 N N   . GLY B 57  ? 0.5457 0.7855 0.2901 -0.0425 -0.1002 0.0346  72  GLY B N   
3457 C CA  . GLY B 57  ? 0.5395 0.7707 0.2921 -0.0370 -0.1018 0.0365  72  GLY B CA  
3458 C C   . GLY B 57  ? 0.5323 0.7653 0.3117 -0.0415 -0.1169 0.0433  72  GLY B C   
3459 O O   . GLY B 57  ? 0.5300 0.7535 0.3071 -0.0539 -0.1315 0.0484  72  GLY B O   
3460 N N   . LEU B 58  ? 0.5247 0.7700 0.3292 -0.0312 -0.1137 0.0432  73  LEU B N   
3461 C CA  . LEU B 58  ? 0.5166 0.7650 0.3488 -0.0346 -0.1263 0.0479  73  LEU B CA  
3462 C C   . LEU B 58  ? 0.5452 0.7822 0.3758 -0.0355 -0.1249 0.0480  73  LEU B C   
3463 O O   . LEU B 58  ? 0.5504 0.7824 0.3672 -0.0281 -0.1118 0.0445  73  LEU B O   
3464 C CB  . LEU B 58  ? 0.4830 0.7561 0.3470 -0.0243 -0.1230 0.0468  73  LEU B CB  
3465 C CG  . LEU B 58  ? 0.4864 0.7704 0.3517 -0.0243 -0.1234 0.0460  73  LEU B CG  
3466 C CD1 . LEU B 58  ? 0.4630 0.7714 0.3540 -0.0128 -0.1157 0.0428  73  LEU B CD1 
3467 C CD2 . LEU B 58  ? 0.5044 0.7770 0.3713 -0.0363 -0.1413 0.0518  73  LEU B CD2 
3468 N N   . TYR B 59  ? 0.5998 0.8319 0.4436 -0.0452 -0.1392 0.0519  74  TYR B N   
3469 C CA  . TYR B 59  ? 0.6488 0.8725 0.4947 -0.0489 -0.1384 0.0515  74  TYR B CA  
3470 C C   . TYR B 59  ? 0.6900 0.9331 0.5758 -0.0479 -0.1449 0.0526  74  TYR B C   
3471 O O   . TYR B 59  ? 0.7515 1.0002 0.6559 -0.0542 -0.1613 0.0558  74  TYR B O   
3472 C CB  . TYR B 59  ? 0.6683 0.8684 0.4904 -0.0642 -0.1493 0.0536  74  TYR B CB  
3473 C CG  . TYR B 59  ? 0.6712 0.8513 0.4526 -0.0661 -0.1418 0.0513  74  TYR B CG  
3474 C CD1 . TYR B 59  ? 0.6695 0.8493 0.4380 -0.0685 -0.1453 0.0522  74  TYR B CD1 
3475 C CD2 . TYR B 59  ? 0.6892 0.8496 0.4443 -0.0659 -0.1306 0.0475  74  TYR B CD2 
3476 C CE1 . TYR B 59  ? 0.6974 0.8613 0.4299 -0.0709 -0.1369 0.0487  74  TYR B CE1 
3477 C CE2 . TYR B 59  ? 0.7150 0.8578 0.4342 -0.0664 -0.1228 0.0440  74  TYR B CE2 
3478 C CZ  . TYR B 59  ? 0.7224 0.8690 0.4316 -0.0691 -0.1256 0.0442  74  TYR B CZ  
3479 O OH  . TYR B 59  ? 0.7654 0.8976 0.4404 -0.0701 -0.1162 0.0394  74  TYR B OH  
3480 N N   . ALA B 60  ? 0.7529 1.0063 0.6516 -0.0392 -0.1319 0.0496  75  ALA B N   
3481 C CA  . ALA B 60  ? 0.7908 1.0625 0.7259 -0.0391 -0.1343 0.0489  75  ALA B CA  
3482 C C   . ALA B 60  ? 0.8465 1.1119 0.7742 -0.0377 -0.1198 0.0462  75  ALA B C   
3483 O O   . ALA B 60  ? 0.9543 1.2141 0.8633 -0.0277 -0.1055 0.0446  75  ALA B O   
3484 C CB  . ALA B 60  ? 0.7750 1.0700 0.7365 -0.0283 -0.1321 0.0477  75  ALA B CB  
3485 N N   . GLY B 61  ? 0.9043 1.1698 0.8454 -0.0482 -0.1239 0.0456  76  GLY B N   
3486 C CA  . GLY B 61  ? 0.9578 1.2109 0.8862 -0.0509 -0.1107 0.0434  76  GLY B CA  
3487 C C   . GLY B 61  ? 1.0323 1.2531 0.9164 -0.0536 -0.1059 0.0440  76  GLY B C   
3488 O O   . GLY B 61  ? 1.0100 1.2205 0.8767 -0.0566 -0.1144 0.0456  76  GLY B O   
3489 N N   . PRO B 62  ? 1.1169 1.3192 0.9800 -0.0524 -0.0918 0.0426  77  PRO B N   
3490 C CA  . PRO B 62  ? 1.1440 1.3122 0.9639 -0.0538 -0.0863 0.0423  77  PRO B CA  
3491 C C   . PRO B 62  ? 1.0491 1.2126 0.8474 -0.0371 -0.0790 0.0418  77  PRO B C   
3492 O O   . PRO B 62  ? 1.0784 1.2157 0.8420 -0.0359 -0.0745 0.0406  77  PRO B O   
3493 C CB  . PRO B 62  ? 1.2039 1.3540 1.0109 -0.0564 -0.0733 0.0411  77  PRO B CB  
3494 C CG  . PRO B 62  ? 1.1964 1.3716 1.0314 -0.0477 -0.0666 0.0409  77  PRO B CG  
3495 C CD  . PRO B 62  ? 1.1424 1.3522 1.0178 -0.0486 -0.0794 0.0411  77  PRO B CD  
3496 N N   . HIS B 63  ? 0.9312 1.1209 0.7504 -0.0247 -0.0775 0.0420  78  HIS B N   
3497 C CA  . HIS B 63  ? 0.8981 1.0897 0.7014 -0.0091 -0.0702 0.0405  78  HIS B CA  
3498 C C   . HIS B 63  ? 0.8067 1.0113 0.6148 -0.0103 -0.0792 0.0406  78  HIS B C   
3499 O O   . HIS B 63  ? 0.7873 1.0132 0.6233 -0.0139 -0.0886 0.0422  78  HIS B O   
3500 C CB  . HIS B 63  ? 0.8973 1.1067 0.7140 0.0058  -0.0605 0.0399  78  HIS B CB  
3501 C CG  . HIS B 63  ? 0.9649 1.1575 0.7702 0.0076  -0.0503 0.0403  78  HIS B CG  
3502 N ND1 . HIS B 63  ? 1.0119 1.1726 0.7807 0.0122  -0.0421 0.0399  78  HIS B ND1 
3503 C CD2 . HIS B 63  ? 0.9587 1.1591 0.7820 0.0044  -0.0465 0.0409  78  HIS B CD2 
3504 C CE1 . HIS B 63  ? 1.0446 1.1921 0.8074 0.0115  -0.0341 0.0411  78  HIS B CE1 
3505 N NE2 . HIS B 63  ? 1.0265 1.1987 0.8220 0.0061  -0.0361 0.0416  78  HIS B NE2 
3506 N N   . LEU B 64  ? 0.7281 0.9182 0.5070 -0.0072 -0.0754 0.0384  79  LEU B N   
3507 C CA  . LEU B 64  ? 0.6784 0.8802 0.4558 -0.0066 -0.0791 0.0374  79  LEU B CA  
3508 C C   . LEU B 64  ? 0.6211 0.8502 0.4163 0.0081  -0.0723 0.0356  79  LEU B C   
3509 O O   . LEU B 64  ? 0.6146 0.8452 0.4054 0.0219  -0.0613 0.0337  79  LEU B O   
3510 C CB  . LEU B 64  ? 0.7053 0.8864 0.4465 -0.0055 -0.0728 0.0336  79  LEU B CB  
3511 C CG  . LEU B 64  ? 0.6975 0.8863 0.4294 -0.0081 -0.0745 0.0313  79  LEU B CG  
3512 C CD1 . LEU B 64  ? 0.7015 0.8889 0.4395 -0.0260 -0.0907 0.0357  79  LEU B CD1 
3513 C CD2 . LEU B 64  ? 0.7170 0.8841 0.4133 -0.0054 -0.0651 0.0259  79  LEU B CD2 
3514 N N   . THR B 65  ? 0.5830 0.8318 0.3970 0.0046  -0.0797 0.0365  80  THR B N   
3515 C CA  . THR B 65  ? 0.5403 0.8148 0.3674 0.0158  -0.0739 0.0338  80  THR B CA  
3516 C C   . THR B 65  ? 0.5332 0.8122 0.3469 0.0124  -0.0744 0.0312  80  THR B C   
3517 O O   . THR B 65  ? 0.5128 0.7894 0.3291 -0.0003 -0.0852 0.0340  80  THR B O   
3518 C CB  . THR B 65  ? 0.5130 0.8065 0.3736 0.0141  -0.0804 0.0360  80  THR B CB  
3519 O OG1 . THR B 65  ? 0.5216 0.8134 0.3942 0.0166  -0.0775 0.0372  80  THR B OG1 
3520 C CG2 . THR B 65  ? 0.5016 0.8201 0.3734 0.0236  -0.0746 0.0327  80  THR B CG2 
3521 N N   . LEU B 66  ? 0.5099 0.7950 0.3084 0.0237  -0.0627 0.0257  81  LEU B N   
3522 C CA  . LEU B 66  ? 0.4987 0.7917 0.2845 0.0203  -0.0601 0.0214  81  LEU B CA  
3523 C C   . LEU B 66  ? 0.4546 0.7782 0.2602 0.0249  -0.0579 0.0188  81  LEU B C   
3524 O O   . LEU B 66  ? 0.4273 0.7676 0.2452 0.0384  -0.0517 0.0167  81  LEU B O   
3525 C CB  . LEU B 66  ? 0.5289 0.8151 0.2898 0.0304  -0.0483 0.0151  81  LEU B CB  
3526 C CG  . LEU B 66  ? 0.5711 0.8329 0.3029 0.0190  -0.0489 0.0136  81  LEU B CG  
3527 C CD1 . LEU B 66  ? 0.5916 0.8242 0.3160 0.0059  -0.0593 0.0199  81  LEU B CD1 
3528 C CD2 . LEU B 66  ? 0.5912 0.8472 0.3021 0.0331  -0.0356 0.0063  81  LEU B CD2 
3529 N N   . VAL B 67  ? 0.4445 0.7737 0.2506 0.0128  -0.0630 0.0188  82  VAL B N   
3530 C CA  . VAL B 67  ? 0.4236 0.7808 0.2447 0.0155  -0.0594 0.0150  82  VAL B CA  
3531 C C   . VAL B 67  ? 0.4226 0.7932 0.2280 0.0141  -0.0501 0.0073  82  VAL B C   
3532 O O   . VAL B 67  ? 0.4471 0.8063 0.2356 -0.0002 -0.0527 0.0073  82  VAL B O   
3533 C CB  . VAL B 67  ? 0.4168 0.7728 0.2527 0.0030  -0.0710 0.0199  82  VAL B CB  
3534 C CG1 . VAL B 67  ? 0.4034 0.7872 0.2546 0.0058  -0.0662 0.0152  82  VAL B CG1 
3535 C CG2 . VAL B 67  ? 0.4042 0.7494 0.2579 0.0038  -0.0802 0.0262  82  VAL B CG2 
3536 N N   . VAL B 68  ? 0.4097 0.8066 0.2218 0.0284  -0.0397 0.0003  83  VAL B N   
3537 C CA  . VAL B 68  ? 0.4218 0.8384 0.2241 0.0285  -0.0298 -0.0088 83  VAL B CA  
3538 C C   . VAL B 68  ? 0.3941 0.8401 0.2111 0.0223  -0.0282 -0.0131 83  VAL B C   
3539 O O   . VAL B 68  ? 0.3684 0.8357 0.2053 0.0319  -0.0274 -0.0143 83  VAL B O   
3540 C CB  . VAL B 68  ? 0.4368 0.8667 0.2365 0.0497  -0.0193 -0.0154 83  VAL B CB  
3541 C CG1 . VAL B 68  ? 0.4492 0.8967 0.2372 0.0489  -0.0089 -0.0259 83  VAL B CG1 
3542 C CG2 . VAL B 68  ? 0.4569 0.8548 0.2418 0.0570  -0.0204 -0.0110 83  VAL B CG2 
3543 N N   . SER B 69  ? 0.3896 0.8354 0.1941 0.0051  -0.0272 -0.0158 84  SER B N   
3544 C CA  . SER B 69  ? 0.3782 0.8458 0.1925 -0.0054 -0.0261 -0.0194 84  SER B CA  
3545 C C   . SER B 69  ? 0.3789 0.8730 0.1846 -0.0104 -0.0135 -0.0311 84  SER B C   
3546 O O   . SER B 69  ? 0.3809 0.8855 0.1861 -0.0261 -0.0122 -0.0340 84  SER B O   
3547 C CB  . SER B 69  ? 0.3911 0.8314 0.1984 -0.0255 -0.0378 -0.0111 84  SER B CB  
3548 O OG  . SER B 69  ? 0.3730 0.8007 0.1975 -0.0210 -0.0487 -0.0028 84  SER B OG  
3549 N N   . GLU B 70  ? 0.3755 0.8808 0.1748 0.0025  -0.0039 -0.0383 85  GLU B N   
3550 C CA  . GLU B 70  ? 0.3795 0.9138 0.1740 -0.0015 0.0088  -0.0507 85  GLU B CA  
3551 C C   . GLU B 70  ? 0.3708 0.9358 0.1780 0.0237  0.0174  -0.0596 85  GLU B C   
3552 O O   . GLU B 70  ? 0.3703 0.9199 0.1752 0.0416  0.0156  -0.0560 85  GLU B O   
3553 C CB  . GLU B 70  ? 0.4113 0.9214 0.1764 -0.0167 0.0124  -0.0519 85  GLU B CB  
3554 C CG  . GLU B 70  ? 0.4161 0.9533 0.1728 -0.0272 0.0266  -0.0652 85  GLU B CG  
3555 C CD  . GLU B 70  ? 0.4138 0.9751 0.1731 -0.0074 0.0394  -0.0773 85  GLU B CD  
3556 O OE1 . GLU B 70  ? 0.4100 0.9554 0.1674 0.0119  0.0375  -0.0744 85  GLU B OE1 
3557 O OE2 . GLU B 70  ? 0.4137 1.0105 0.1770 -0.0113 0.0518  -0.0904 85  GLU B OE2 
3558 N N   . ILE B 71  ? 0.3624 0.9707 0.1823 0.0244  0.0262  -0.0712 86  ILE B N   
3559 C CA  . ILE B 71  ? 0.3492 0.9942 0.1852 0.0492  0.0328  -0.0805 86  ILE B CA  
3560 C C   . ILE B 71  ? 0.3706 1.0055 0.1943 0.0680  0.0388  -0.0844 86  ILE B C   
3561 O O   . ILE B 71  ? 0.3674 1.0047 0.1979 0.0925  0.0373  -0.0834 86  ILE B O   
3562 C CB  . ILE B 71  ? 0.3392 1.0361 0.1906 0.0435  0.0418  -0.0944 86  ILE B CB  
3563 C CG1 . ILE B 71  ? 0.3301 1.0662 0.2011 0.0717  0.0452  -0.1028 86  ILE B CG1 
3564 C CG2 . ILE B 71  ? 0.3559 1.0598 0.1925 0.0264  0.0533  -0.1042 86  ILE B CG2 
3565 C CD1 . ILE B 71  ? 0.3152 1.0459 0.1984 0.0879  0.0348  -0.0938 86  ILE B CD1 
3566 N N   . GLY B 72  ? 0.4026 1.0247 0.2061 0.0565  0.0462  -0.0891 87  GLY B N   
3567 C CA  . GLY B 72  ? 0.4261 1.0346 0.2154 0.0732  0.0527  -0.0937 87  GLY B CA  
3568 C C   . GLY B 72  ? 0.4297 0.9963 0.2102 0.0845  0.0431  -0.0810 87  GLY B C   
3569 O O   . GLY B 72  ? 0.4357 1.0005 0.2181 0.1094  0.0441  -0.0819 87  GLY B O   
3570 N N   . LEU B 73  ? 0.4333 0.9663 0.2045 0.0660  0.0333  -0.0692 88  LEU B N   
3571 C CA  . LEU B 73  ? 0.4448 0.9381 0.2075 0.0723  0.0244  -0.0577 88  LEU B CA  
3572 C C   . LEU B 73  ? 0.4354 0.9384 0.2171 0.0915  0.0195  -0.0531 88  LEU B C   
3573 O O   . LEU B 73  ? 0.4500 0.9306 0.2236 0.1070  0.0186  -0.0494 88  LEU B O   
3574 C CB  . LEU B 73  ? 0.4437 0.9048 0.1968 0.0487  0.0137  -0.0468 88  LEU B CB  
3575 C CG  . LEU B 73  ? 0.4714 0.9070 0.1961 0.0317  0.0164  -0.0484 88  LEU B CG  
3576 C CD1 . LEU B 73  ? 0.4787 0.8903 0.1964 0.0073  0.0043  -0.0382 88  LEU B CD1 
3577 C CD2 . LEU B 73  ? 0.4906 0.8948 0.1957 0.0428  0.0184  -0.0478 88  LEU B CD2 
3578 N N   . VAL B 74  ? 0.4255 0.9597 0.2296 0.0899  0.0170  -0.0537 89  VAL B N   
3579 C CA  . VAL B 74  ? 0.4259 0.9693 0.2462 0.1073  0.0124  -0.0495 89  VAL B CA  
3580 C C   . VAL B 74  ? 0.4430 1.0115 0.2679 0.1339  0.0187  -0.0576 89  VAL B C   
3581 O O   . VAL B 74  ? 0.4550 1.0155 0.2814 0.1517  0.0154  -0.0528 89  VAL B O   
3582 C CB  . VAL B 74  ? 0.4126 0.9769 0.2540 0.0981  0.0067  -0.0470 89  VAL B CB  
3583 C CG1 . VAL B 74  ? 0.4155 0.9751 0.2552 0.0711  0.0041  -0.0457 89  VAL B CG1 
3584 C CG2 . VAL B 74  ? 0.3965 1.0066 0.2560 0.1117  0.0108  -0.0558 89  VAL B CG2 
3585 N N   . ARG B 75  ? 0.4651 1.0635 0.2920 0.1368  0.0277  -0.0700 90  ARG B N   
3586 C CA  . ARG B 75  ? 0.4902 1.1121 0.3218 0.1648  0.0330  -0.0784 90  ARG B CA  
3587 C C   . ARG B 75  ? 0.5101 1.0921 0.3188 0.1793  0.0350  -0.0758 90  ARG B C   
3588 O O   . ARG B 75  ? 0.5249 1.1063 0.3323 0.2052  0.0348  -0.0762 90  ARG B O   
3589 C CB  . ARG B 75  ? 0.5117 1.1802 0.3544 0.1649  0.0430  -0.0943 90  ARG B CB  
3590 C CG  . ARG B 75  ? 0.5059 1.2199 0.3720 0.1530  0.0423  -0.0995 90  ARG B CG  
3591 C CD  . ARG B 75  ? 0.5410 1.3065 0.4208 0.1574  0.0527  -0.1166 90  ARG B CD  
3592 N NE  . ARG B 75  ? 0.5805 1.3852 0.4806 0.1843  0.0502  -0.1223 90  ARG B NE  
3593 C CZ  . ARG B 75  ? 0.5964 1.4392 0.5180 0.1822  0.0457  -0.1246 90  ARG B CZ  
3594 N NH1 . ARG B 75  ? 0.5973 1.4446 0.5236 0.1544  0.0443  -0.1225 90  ARG B NH1 
3595 N NH2 . ARG B 75  ? 0.6117 1.4870 0.5487 0.2083  0.0420  -0.1290 90  ARG B NH2 
3596 N N   . GLU B 76  ? 0.5141 1.0607 0.3023 0.1626  0.0366  -0.0729 91  GLU B N   
3597 C CA  . GLU B 76  ? 0.5331 1.0379 0.2972 0.1738  0.0383  -0.0703 91  GLU B CA  
3598 C C   . GLU B 76  ? 0.5144 0.9868 0.2739 0.1797  0.0295  -0.0572 91  GLU B C   
3599 O O   . GLU B 76  ? 0.5293 0.9765 0.2739 0.1979  0.0307  -0.0555 91  GLU B O   
3600 C CB  . GLU B 76  ? 0.5666 1.0417 0.3085 0.1528  0.0415  -0.0707 91  GLU B CB  
3601 C CG  . GLU B 76  ? 0.6056 1.0352 0.3202 0.1624  0.0439  -0.0690 91  GLU B CG  
3602 C CD  . GLU B 76  ? 0.6228 1.0223 0.3139 0.1393  0.0456  -0.0690 91  GLU B CD  
3603 O OE1 . GLU B 76  ? 0.6125 1.0287 0.3077 0.1180  0.0459  -0.0712 91  GLU B OE1 
3604 O OE2 . GLU B 76  ? 0.6530 1.0108 0.3198 0.1419  0.0462  -0.0665 91  GLU B OE2 
3605 N N   . VAL B 77  ? 0.4902 0.9629 0.2619 0.1643  0.0213  -0.0485 92  VAL B N   
3606 C CA  . VAL B 77  ? 0.4902 0.9371 0.2607 0.1679  0.0139  -0.0371 92  VAL B CA  
3607 C C   . VAL B 77  ? 0.4932 0.9589 0.2732 0.1920  0.0133  -0.0372 92  VAL B C   
3608 O O   . VAL B 77  ? 0.5260 0.9652 0.2913 0.2080  0.0131  -0.0328 92  VAL B O   
3609 C CB  . VAL B 77  ? 0.4716 0.9179 0.2557 0.1457  0.0059  -0.0294 92  VAL B CB  
3610 C CG1 . VAL B 77  ? 0.4710 0.8995 0.2586 0.1502  0.0000  -0.0196 92  VAL B CG1 
3611 C CG2 . VAL B 77  ? 0.4929 0.9122 0.2637 0.1230  0.0034  -0.0265 92  VAL B CG2 
3612 N N   . LEU B 78  ? 0.4620 0.9717 0.2645 0.1936  0.0126  -0.0421 93  LEU B N   
3613 C CA  . LEU B 78  ? 0.4535 0.9833 0.2651 0.2143  0.0103  -0.0420 93  LEU B CA  
3614 C C   . LEU B 78  ? 0.4855 1.0221 0.2882 0.2421  0.0149  -0.0492 93  LEU B C   
3615 O O   . LEU B 78  ? 0.5139 1.0268 0.3026 0.2609  0.0129  -0.0440 93  LEU B O   
3616 C CB  . LEU B 78  ? 0.4238 0.9995 0.2611 0.2064  0.0081  -0.0463 93  LEU B CB  
3617 C CG  . LEU B 78  ? 0.4034 0.9725 0.2505 0.1815  0.0032  -0.0397 93  LEU B CG  
3618 C CD1 . LEU B 78  ? 0.3746 0.9868 0.2444 0.1741  0.0019  -0.0451 93  LEU B CD1 
3619 C CD2 . LEU B 78  ? 0.4101 0.9469 0.2513 0.1828  -0.0019 -0.0284 93  LEU B CD2 
3620 N N   . LEU B 79  ? 0.4881 1.0552 0.2980 0.2447  0.0214  -0.0615 94  LEU B N   
3621 C CA  . LEU B 79  ? 0.5088 1.0884 0.3148 0.2733  0.0259  -0.0703 94  LEU B CA  
3622 C C   . LEU B 79  ? 0.5518 1.0895 0.3311 0.2812  0.0320  -0.0716 94  LEU B C   
3623 O O   . LEU B 79  ? 0.5810 1.0843 0.3416 0.3002  0.0297  -0.0656 94  LEU B O   
3624 C CB  . LEU B 79  ? 0.4946 1.1325 0.3235 0.2748  0.0314  -0.0853 94  LEU B CB  
3625 C CG  . LEU B 79  ? 0.4664 1.1571 0.3217 0.2830  0.0266  -0.0897 94  LEU B CG  
3626 C CD1 . LEU B 79  ? 0.4669 1.1445 0.3169 0.3048  0.0174  -0.0805 94  LEU B CD1 
3627 C CD2 . LEU B 79  ? 0.4355 1.1468 0.3066 0.2531  0.0252  -0.0889 94  LEU B CD2 
3628 N N   . GLN B 80  ? 0.5449 1.0836 0.3199 0.2666  0.0399  -0.0795 95  GLN B N   
3629 C CA  . GLN B 80  ? 0.5807 1.0857 0.3311 0.2750  0.0473  -0.0840 95  GLN B CA  
3630 C C   . GLN B 80  ? 0.6266 1.0716 0.3495 0.2803  0.0433  -0.0722 95  GLN B C   
3631 O O   . GLN B 80  ? 0.6622 1.0846 0.3681 0.3043  0.0462  -0.0744 95  GLN B O   
3632 C CB  . GLN B 80  ? 0.5755 1.0762 0.3183 0.2492  0.0547  -0.0899 95  GLN B CB  
3633 C CG  . GLN B 80  ? 0.5978 1.0697 0.3159 0.2582  0.0643  -0.0978 95  GLN B CG  
3634 C CD  . GLN B 80  ? 0.5958 1.0594 0.3016 0.2311  0.0714  -0.1030 95  GLN B CD  
3635 O OE1 . GLN B 80  ? 0.5694 1.0576 0.2877 0.2077  0.0706  -0.1035 95  GLN B OE1 
3636 N NE2 . GLN B 80  ? 0.6247 1.0507 0.3030 0.2340  0.0782  -0.1069 95  GLN B NE2 
3637 N N   . ARG B 81  ? 0.6374 1.0563 0.3557 0.2579  0.0370  -0.0603 96  ARG B N   
3638 C CA  . ARG B 81  ? 0.6745 1.0400 0.3690 0.2599  0.0332  -0.0491 96  ARG B CA  
3639 C C   . ARG B 81  ? 0.6742 1.0401 0.3795 0.2556  0.0245  -0.0375 96  ARG B C   
3640 O O   . ARG B 81  ? 0.6873 1.0208 0.3836 0.2394  0.0206  -0.0280 96  ARG B O   
3641 C CB  . ARG B 81  ? 0.6907 1.0148 0.3630 0.2383  0.0355  -0.0471 96  ARG B CB  
3642 C CG  . ARG B 81  ? 0.6712 1.0155 0.3515 0.2145  0.0380  -0.0530 96  ARG B CG  
3643 C CD  . ARG B 81  ? 0.6890 0.9916 0.3417 0.1988  0.0412  -0.0534 96  ARG B CD  
3644 N NE  . ARG B 81  ? 0.7118 1.0188 0.3529 0.2103  0.0523  -0.0667 96  ARG B NE  
3645 C CZ  . ARG B 81  ? 0.7321 1.0169 0.3517 0.1964  0.0581  -0.0721 96  ARG B CZ  
3646 N NH1 . ARG B 81  ? 0.7422 0.9970 0.3481 0.1703  0.0523  -0.0645 96  ARG B NH1 
3647 N NH2 . ARG B 81  ? 0.7558 1.0492 0.3674 0.2092  0.0697  -0.0858 96  ARG B NH2 
3648 N N   . GLY B 82  ? 0.6808 1.0846 0.4050 0.2711  0.0217  -0.0395 97  GLY B N   
3649 C CA  . GLY B 82  ? 0.6755 1.0860 0.4106 0.2693  0.0146  -0.0306 97  GLY B CA  
3650 C C   . GLY B 82  ? 0.7165 1.0817 0.4290 0.2769  0.0120  -0.0199 97  GLY B C   
3651 O O   . GLY B 82  ? 0.7104 1.0680 0.4277 0.2641  0.0077  -0.0113 97  GLY B O   
3652 N N   . ARG B 83  ? 0.7549 1.0896 0.4423 0.2975  0.0152  -0.0208 98  ARG B N   
3653 C CA  . ARG B 83  ? 0.8122 1.0973 0.4721 0.3039  0.0138  -0.0107 98  ARG B CA  
3654 C C   . ARG B 83  ? 0.8030 1.0469 0.4488 0.2785  0.0152  -0.0047 98  ARG B C   
3655 O O   . ARG B 83  ? 0.8351 1.0522 0.4713 0.2703  0.0130  0.0047  98  ARG B O   
3656 C CB  . ARG B 83  ? 0.8897 1.1483 0.5236 0.3327  0.0168  -0.0137 98  ARG B CB  
3657 C CG  . ARG B 83  ? 0.9616 1.1615 0.5609 0.3383  0.0163  -0.0032 98  ARG B CG  
3658 C CD  . ARG B 83  ? 1.0517 1.2266 0.6254 0.3706  0.0182  -0.0064 98  ARG B CD  
3659 N NE  . ARG B 83  ? 1.0785 1.2407 0.6427 0.3735  0.0256  -0.0163 98  ARG B NE  
3660 C CZ  . ARG B 83  ? 1.1311 1.2397 0.6656 0.3635  0.0307  -0.0146 98  ARG B CZ  
3661 N NH1 . ARG B 83  ? 1.1729 1.2367 0.6857 0.3486  0.0294  -0.0035 98  ARG B NH1 
3662 N NH2 . ARG B 83  ? 1.1634 1.2638 0.6895 0.3670  0.0377  -0.0249 98  ARG B NH2 
3663 N N   . GLU B 84  ? 0.7752 1.0149 0.4191 0.2658  0.0189  -0.0106 99  GLU B N   
3664 C CA  . GLU B 84  ? 0.7641 0.9669 0.3943 0.2415  0.0191  -0.0061 99  GLU B CA  
3665 C C   . GLU B 84  ? 0.7118 0.9325 0.3659 0.2164  0.0132  -0.0006 99  GLU B C   
3666 O O   . GLU B 84  ? 0.7278 0.9196 0.3743 0.1986  0.0111  0.0058  99  GLU B O   
3667 C CB  . GLU B 84  ? 0.7820 0.9780 0.4026 0.2345  0.0241  -0.0146 99  GLU B CB  
3668 C CG  . GLU B 84  ? 0.8283 1.0002 0.4230 0.2578  0.0313  -0.0214 99  GLU B CG  
3669 C CD  . GLU B 84  ? 0.8159 1.0311 0.4262 0.2759  0.0356  -0.0335 99  GLU B CD  
3670 O OE1 . GLU B 84  ? 0.7671 1.0253 0.4020 0.2867  0.0323  -0.0344 99  GLU B OE1 
3671 O OE2 . GLU B 84  ? 0.8433 1.0501 0.4410 0.2784  0.0428  -0.0428 99  GLU B OE2 
3672 N N   . PHE B 85  ? 0.6564 0.9243 0.3394 0.2145  0.0105  -0.0039 100 PHE B N   
3673 C CA  . PHE B 85  ? 0.6175 0.9034 0.3243 0.1941  0.0047  0.0009  100 PHE B CA  
3674 C C   . PHE B 85  ? 0.6013 0.9045 0.3214 0.2027  0.0021  0.0054  100 PHE B C   
3675 O O   . PHE B 85  ? 0.5616 0.8921 0.3059 0.1915  -0.0016 0.0060  100 PHE B O   
3676 C CB  . PHE B 85  ? 0.5841 0.9065 0.3119 0.1823  0.0035  -0.0054 100 PHE B CB  
3677 C CG  . PHE B 85  ? 0.6094 0.9144 0.3253 0.1668  0.0046  -0.0081 100 PHE B CG  
3678 C CD1 . PHE B 85  ? 0.6208 0.9015 0.3341 0.1446  -0.0008 -0.0018 100 PHE B CD1 
3679 C CD2 . PHE B 85  ? 0.6312 0.9457 0.3387 0.1735  0.0109  -0.0176 100 PHE B CD2 
3680 C CE1 . PHE B 85  ? 0.6182 0.8818 0.3179 0.1294  -0.0012 -0.0040 100 PHE B CE1 
3681 C CE2 . PHE B 85  ? 0.6411 0.9379 0.3345 0.1574  0.0123  -0.0203 100 PHE B CE2 
3682 C CZ  . PHE B 85  ? 0.6347 0.9049 0.3228 0.1353  0.0056  -0.0130 100 PHE B CZ  
3683 N N   . ALA B 86  ? 0.6317 0.9161 0.3335 0.2218  0.0039  0.0085  101 ALA B N   
3684 C CA  . ALA B 86  ? 0.6448 0.9434 0.3541 0.2306  0.0015  0.0127  101 ALA B CA  
3685 C C   . ALA B 86  ? 0.6520 0.9224 0.3551 0.2169  0.0012  0.0216  101 ALA B C   
3686 O O   . ALA B 86  ? 0.6481 0.9166 0.3465 0.2248  0.0009  0.0261  101 ALA B O   
3687 C CB  . ALA B 86  ? 0.6665 0.9630 0.3588 0.2601  0.0024  0.0117  101 ALA B CB  
3688 N N   . GLY B 87  ? 0.6493 0.8989 0.3520 0.1959  0.0011  0.0236  102 GLY B N   
3689 C CA  . GLY B 87  ? 0.6493 0.8759 0.3498 0.1807  0.0013  0.0304  102 GLY B CA  
3690 C C   . GLY B 87  ? 0.6050 0.8650 0.3381 0.1678  -0.0022 0.0305  102 GLY B C   
3691 O O   . GLY B 87  ? 0.5704 0.8647 0.3252 0.1665  -0.0052 0.0257  102 GLY B O   
3692 N N   . ARG B 88  ? 0.6135 0.8624 0.3488 0.1581  -0.0008 0.0353  103 ARG B N   
3693 C CA  . ARG B 88  ? 0.5940 0.8709 0.3599 0.1460  -0.0030 0.0350  103 ARG B CA  
3694 C C   . ARG B 88  ? 0.6038 0.8624 0.3757 0.1258  -0.0026 0.0382  103 ARG B C   
3695 O O   . ARG B 88  ? 0.6600 0.8848 0.4088 0.1235  0.0017  0.0420  103 ARG B O   
3696 C CB  . ARG B 88  ? 0.5997 0.8907 0.3654 0.1576  -0.0005 0.0359  103 ARG B CB  
3697 C CG  . ARG B 88  ? 0.5886 0.9089 0.3570 0.1759  -0.0025 0.0316  103 ARG B CG  
3698 C CD  . ARG B 88  ? 0.5648 0.9215 0.3625 0.1681  -0.0068 0.0256  103 ARG B CD  
3699 N NE  . ARG B 88  ? 0.5609 0.9531 0.3682 0.1803  -0.0081 0.0209  103 ARG B NE  
3700 C CZ  . ARG B 88  ? 0.5474 0.9709 0.3715 0.1793  -0.0106 0.0145  103 ARG B CZ  
3701 N NH1 . ARG B 88  ? 0.5375 0.9600 0.3688 0.1671  -0.0122 0.0125  103 ARG B NH1 
3702 N NH2 . ARG B 88  ? 0.5508 1.0068 0.3828 0.1895  -0.0115 0.0100  103 ARG B NH2 
3703 N N   . PRO B 89  ? 0.5710 0.8516 0.3739 0.1113  -0.0072 0.0364  104 PRO B N   
3704 C CA  . PRO B 89  ? 0.5763 0.8479 0.3927 0.0921  -0.0085 0.0380  104 PRO B CA  
3705 C C   . PRO B 89  ? 0.5892 0.8614 0.4131 0.0869  -0.0025 0.0393  104 PRO B C   
3706 O O   . PRO B 89  ? 0.5510 0.8446 0.3853 0.0938  0.0000  0.0378  104 PRO B O   
3707 C CB  . PRO B 89  ? 0.5403 0.8390 0.3879 0.0833  -0.0168 0.0351  104 PRO B CB  
3708 C CG  . PRO B 89  ? 0.5162 0.8433 0.3726 0.0954  -0.0163 0.0320  104 PRO B CG  
3709 C CD  . PRO B 89  ? 0.5345 0.8510 0.3620 0.1126  -0.0120 0.0321  104 PRO B CD  
3710 N N   . LYS B 90  ? 0.6323 0.8826 0.4511 0.0733  0.0003  0.0414  105 LYS B N   
3711 C CA  . LYS B 90  ? 0.6822 0.9341 0.5102 0.0643  0.0074  0.0415  105 LYS B CA  
3712 C C   . LYS B 90  ? 0.6800 0.9586 0.5499 0.0497  0.0029  0.0376  105 LYS B C   
3713 O O   . LYS B 90  ? 0.6286 0.9016 0.5089 0.0355  -0.0013 0.0373  105 LYS B O   
3714 C CB  . LYS B 90  ? 0.7231 0.9369 0.5213 0.0566  0.0147  0.0450  105 LYS B CB  
3715 C CG  . LYS B 90  ? 0.7591 0.9758 0.5704 0.0412  0.0223  0.0438  105 LYS B CG  
3716 C CD  . LYS B 90  ? 0.8231 0.9997 0.5976 0.0348  0.0321  0.0476  105 LYS B CD  
3717 C CE  . LYS B 90  ? 0.8468 1.0071 0.5884 0.0506  0.0391  0.0516  105 LYS B CE  
3718 N NZ  . LYS B 90  ? 0.8227 1.0105 0.5832 0.0512  0.0438  0.0492  105 LYS B NZ  
3719 N N   . MET B 91  ? 0.7497 1.0573 0.6430 0.0540  0.0034  0.0344  106 MET B N   
3720 C CA  . MET B 91  ? 0.7719 1.1051 0.7056 0.0434  0.0004  0.0299  106 MET B CA  
3721 C C   . MET B 91  ? 0.7309 1.0693 0.6703 0.0391  0.0120  0.0275  106 MET B C   
3722 O O   . MET B 91  ? 0.6938 1.0186 0.6057 0.0456  0.0208  0.0297  106 MET B O   
3723 C CB  . MET B 91  ? 0.8488 1.2093 0.8047 0.0505  -0.0070 0.0269  106 MET B CB  
3724 C CG  . MET B 91  ? 1.0014 1.3582 0.9403 0.0598  -0.0135 0.0288  106 MET B CG  
3725 S SD  . MET B 91  ? 1.2393 1.6261 1.1992 0.0658  -0.0198 0.0248  106 MET B SD  
3726 C CE  . MET B 91  ? 1.1716 1.5523 1.1023 0.0777  -0.0215 0.0263  106 MET B CE  
3727 N N   . VAL B 92  ? 0.6547 1.0130 0.6295 0.0285  0.0118  0.0226  107 VAL B N   
3728 C CA  . VAL B 92  ? 0.6267 0.9931 0.6104 0.0227  0.0237  0.0186  107 VAL B CA  
3729 C C   . VAL B 92  ? 0.5692 0.9535 0.5561 0.0338  0.0274  0.0156  107 VAL B C   
3730 O O   . VAL B 92  ? 0.5681 0.9469 0.5366 0.0355  0.0385  0.0154  107 VAL B O   
3731 C CB  . VAL B 92  ? 0.6666 1.0514 0.6905 0.0083  0.0225  0.0128  107 VAL B CB  
3732 C CG1 . VAL B 92  ? 0.6770 1.0932 0.7373 0.0107  0.0241  0.0052  107 VAL B CG1 
3733 C CG2 . VAL B 92  ? 0.6972 1.0685 0.7110 -0.0058 0.0345  0.0120  107 VAL B CG2 
3734 N N   . THR B 93  ? 0.4975 0.9016 0.5055 0.0400  0.0182  0.0132  108 THR B N   
3735 C CA  . THR B 93  ? 0.4902 0.9120 0.5022 0.0490  0.0208  0.0095  108 THR B CA  
3736 C C   . THR B 93  ? 0.5091 0.9180 0.4825 0.0604  0.0252  0.0138  108 THR B C   
3737 O O   . THR B 93  ? 0.5366 0.9495 0.5006 0.0631  0.0338  0.0118  108 THR B O   
3738 C CB  . THR B 93  ? 0.4772 0.9159 0.5101 0.0534  0.0094  0.0074  108 THR B CB  
3739 O OG1 . THR B 93  ? 0.5380 0.9646 0.5656 0.0518  -0.0011 0.0122  108 THR B OG1 
3740 C CG2 . THR B 93  ? 0.4687 0.9273 0.5412 0.0474  0.0082  0.0006  108 THR B CG2 
3741 N N   . THR B 94  ? 0.4877 0.8808 0.4381 0.0672  0.0191  0.0193  109 THR B N   
3742 C CA  . THR B 94  ? 0.4959 0.8787 0.4122 0.0809  0.0211  0.0230  109 THR B CA  
3743 C C   . THR B 94  ? 0.5177 0.8756 0.4049 0.0795  0.0310  0.0269  109 THR B C   
3744 O O   . THR B 94  ? 0.5342 0.8863 0.3956 0.0904  0.0341  0.0291  109 THR B O   
3745 C CB  . THR B 94  ? 0.5128 0.8832 0.4115 0.0891  0.0134  0.0270  109 THR B CB  
3746 O OG1 . THR B 94  ? 0.5344 0.8783 0.4223 0.0809  0.0134  0.0308  109 THR B OG1 
3747 C CG2 . THR B 94  ? 0.4969 0.8895 0.4186 0.0898  0.0041  0.0236  109 THR B CG2 
3748 N N   . ASP B 95  ? 0.5261 0.8684 0.4158 0.0657  0.0353  0.0277  110 ASP B N   
3749 C CA  . ASP B 95  ? 0.5613 0.8764 0.4210 0.0610  0.0459  0.0314  110 ASP B CA  
3750 C C   . ASP B 95  ? 0.5726 0.9004 0.4348 0.0591  0.0554  0.0277  110 ASP B C   
3751 O O   . ASP B 95  ? 0.6070 0.9179 0.4352 0.0657  0.0609  0.0317  110 ASP B O   
3752 C CB  . ASP B 95  ? 0.5759 0.8752 0.4408 0.0434  0.0493  0.0316  110 ASP B CB  
3753 C CG  . ASP B 95  ? 0.5999 0.8706 0.4413 0.0453  0.0434  0.0370  110 ASP B CG  
3754 O OD1 . ASP B 95  ? 0.6168 0.8831 0.4418 0.0614  0.0369  0.0399  110 ASP B OD1 
3755 O OD2 . ASP B 95  ? 0.5890 0.8426 0.4285 0.0305  0.0458  0.0376  110 ASP B OD2 
3756 N N   . LEU B 96  ? 0.5442 0.9009 0.4454 0.0509  0.0569  0.0201  111 LEU B N   
3757 C CA  . LEU B 96  ? 0.5556 0.9255 0.4606 0.0479  0.0671  0.0150  111 LEU B CA  
3758 C C   . LEU B 96  ? 0.5643 0.9424 0.4521 0.0637  0.0640  0.0159  111 LEU B C   
3759 O O   . LEU B 96  ? 0.6321 1.0062 0.4990 0.0648  0.0721  0.0157  111 LEU B O   
3760 C CB  . LEU B 96  ? 0.5245 0.9249 0.4774 0.0383  0.0687  0.0054  111 LEU B CB  
3761 C CG  . LEU B 96  ? 0.5163 0.9179 0.4954 0.0231  0.0700  0.0026  111 LEU B CG  
3762 C CD1 . LEU B 96  ? 0.4925 0.9265 0.5199 0.0182  0.0703  -0.0075 111 LEU B CD1 
3763 C CD2 . LEU B 96  ? 0.5519 0.9316 0.5081 0.0101  0.0834  0.0043  111 LEU B CD2 
3764 N N   . LEU B 97  ? 0.5343 0.9245 0.4296 0.0749  0.0524  0.0164  112 LEU B N   
3765 C CA  . LEU B 97  ? 0.5164 0.9191 0.3988 0.0889  0.0486  0.0161  112 LEU B CA  
3766 C C   . LEU B 97  ? 0.5360 0.9150 0.3740 0.1012  0.0487  0.0237  112 LEU B C   
3767 O O   . LEU B 97  ? 0.5419 0.9297 0.3654 0.1106  0.0482  0.0232  112 LEU B O   
3768 C CB  . LEU B 97  ? 0.4875 0.9099 0.3895 0.0958  0.0371  0.0140  112 LEU B CB  
3769 C CG  . LEU B 97  ? 0.4641 0.9153 0.4029 0.0902  0.0353  0.0057  112 LEU B CG  
3770 C CD1 . LEU B 97  ? 0.4629 0.9190 0.4222 0.0778  0.0449  0.0000  112 LEU B CD1 
3771 C CD2 . LEU B 97  ? 0.4595 0.9164 0.4202 0.0883  0.0252  0.0056  112 LEU B CD2 
3772 N N   . THR B 98  ? 0.5573 0.9056 0.3732 0.1013  0.0487  0.0304  113 THR B N   
3773 C CA  . THR B 98  ? 0.5922 0.9155 0.3671 0.1169  0.0455  0.0380  113 THR B CA  
3774 C C   . THR B 98  ? 0.6332 0.9135 0.3713 0.1119  0.0532  0.0451  113 THR B C   
3775 O O   . THR B 98  ? 0.6578 0.9109 0.3614 0.1248  0.0501  0.0518  113 THR B O   
3776 C CB  . THR B 98  ? 0.5794 0.9035 0.3577 0.1272  0.0354  0.0393  113 THR B CB  
3777 O OG1 . THR B 98  ? 0.5813 0.8863 0.3650 0.1153  0.0363  0.0408  113 THR B OG1 
3778 C CG2 . THR B 98  ? 0.5272 0.8909 0.3392 0.1302  0.0280  0.0325  113 THR B CG2 
3779 N N   . GLN B 99  ? 0.6693 0.9429 0.4145 0.0930  0.0636  0.0431  114 GLN B N   
3780 C CA  . GLN B 99  ? 0.7405 0.9724 0.4504 0.0842  0.0724  0.0492  114 GLN B CA  
3781 C C   . GLN B 99  ? 0.7650 0.9686 0.4598 0.0876  0.0670  0.0543  114 GLN B C   
3782 O O   . GLN B 99  ? 0.8128 0.9776 0.4642 0.0958  0.0676  0.0618  114 GLN B O   
3783 C CB  . GLN B 99  ? 0.7928 1.0033 0.4583 0.0938  0.0760  0.0550  114 GLN B CB  
3784 C CG  . GLN B 99  ? 0.8392 1.0187 0.4758 0.0772  0.0901  0.0579  114 GLN B CG  
3785 C CD  . GLN B 99  ? 0.8836 1.0568 0.4880 0.0838  0.0936  0.0607  114 GLN B CD  
3786 O OE1 . GLN B 99  ? 0.8857 1.0879 0.5096 0.0779  0.0984  0.0540  114 GLN B OE1 
3787 N NE2 . GLN B 99  ? 0.9305 1.0646 0.4844 0.0966  0.0907  0.0706  114 GLN B NE2 
3788 N N   . GLY B 100 ? 0.7308 0.9526 0.4599 0.0818  0.0612  0.0501  115 GLY B N   
3789 C CA  . GLY B 100 ? 0.7340 0.9320 0.4519 0.0832  0.0560  0.0534  115 GLY B CA  
3790 C C   . GLY B 100 ? 0.7416 0.9329 0.4388 0.1065  0.0471  0.0569  115 GLY B C   
3791 O O   . GLY B 100 ? 0.7984 0.9534 0.4625 0.1130  0.0467  0.0621  115 GLY B O   
3792 N N   . GLY B 101 ? 0.6879 0.9142 0.4050 0.1190  0.0403  0.0533  116 GLY B N   
3793 C CA  . GLY B 101 ? 0.6898 0.9163 0.3921 0.1409  0.0324  0.0549  116 GLY B CA  
3794 C C   . GLY B 101 ? 0.7266 0.9256 0.3853 0.1580  0.0335  0.0613  116 GLY B C   
3795 O O   . GLY B 101 ? 0.7325 0.9089 0.3665 0.1731  0.0297  0.0646  116 GLY B O   
3796 N N   . LYS B 102 ? 0.7621 0.9615 0.4101 0.1559  0.0385  0.0628  117 LYS B N   
3797 C CA  . LYS B 102 ? 0.8171 0.9997 0.4267 0.1752  0.0362  0.0686  117 LYS B CA  
3798 C C   . LYS B 102 ? 0.7767 1.0028 0.4040 0.1906  0.0281  0.0641  117 LYS B C   
3799 O O   . LYS B 102 ? 0.7859 1.0091 0.3889 0.2040  0.0255  0.0675  117 LYS B O   
3800 C CB  . LYS B 102 ? 0.8668 1.0219 0.4475 0.1642  0.0460  0.0735  117 LYS B CB  
3801 C CG  . LYS B 102 ? 0.9280 1.0345 0.4818 0.1504  0.0542  0.0787  117 LYS B CG  
3802 C CD  . LYS B 102 ? 0.9867 1.0638 0.5069 0.1390  0.0647  0.0836  117 LYS B CD  
3803 C CE  . LYS B 102 ? 1.0521 1.0807 0.5448 0.1221  0.0741  0.0881  117 LYS B CE  
3804 N NZ  . LYS B 102 ? 1.0441 1.0905 0.5758 0.0971  0.0804  0.0810  117 LYS B NZ  
3805 N N   . ASP B 103 ? 0.7064 0.9712 0.3744 0.1874  0.0238  0.0566  118 ASP B N   
3806 C CA  . ASP B 103 ? 0.6455 0.9535 0.3339 0.1991  0.0162  0.0508  118 ASP B CA  
3807 C C   . ASP B 103 ? 0.6452 0.9568 0.3302 0.2177  0.0084  0.0503  118 ASP B C   
3808 O O   . ASP B 103 ? 0.6898 0.9655 0.3459 0.2272  0.0084  0.0558  118 ASP B O   
3809 C CB  . ASP B 103 ? 0.5862 0.9301 0.3183 0.1823  0.0174  0.0428  118 ASP B CB  
3810 C CG  . ASP B 103 ? 0.5536 0.9033 0.3093 0.1762  0.0144  0.0398  118 ASP B CG  
3811 O OD1 . ASP B 103 ? 0.5700 0.8895 0.3115 0.1748  0.0155  0.0439  118 ASP B OD1 
3812 O OD2 . ASP B 103 ? 0.4986 0.8816 0.2848 0.1720  0.0109  0.0334  118 ASP B OD2 
3813 N N   . ILE B 104 ? 0.6071 0.9605 0.3201 0.2223  0.0025  0.0430  119 ILE B N   
3814 C CA  . ILE B 104 ? 0.5985 0.9616 0.3154 0.2360  -0.0031 0.0401  119 ILE B CA  
3815 C C   . ILE B 104 ? 0.5694 0.9487 0.3171 0.2214  -0.0028 0.0345  119 ILE B C   
3816 O O   . ILE B 104 ? 0.5978 0.9640 0.3409 0.2248  -0.0035 0.0343  119 ILE B O   
3817 C CB  . ILE B 104 ? 0.5966 0.9986 0.3202 0.2536  -0.0103 0.0351  119 ILE B CB  
3818 C CG1 . ILE B 104 ? 0.6349 1.0204 0.3243 0.2736  -0.0138 0.0411  119 ILE B CG1 
3819 C CG2 . ILE B 104 ? 0.5840 1.0064 0.3208 0.2636  -0.0143 0.0291  119 ILE B CG2 
3820 C CD1 . ILE B 104 ? 0.6690 1.0261 0.3305 0.2958  -0.0171 0.0453  119 ILE B CD1 
3821 N N   . ALA B 105 ? 0.5260 0.9327 0.3033 0.2058  -0.0022 0.0298  120 ALA B N   
3822 C CA  . ALA B 105 ? 0.4929 0.9160 0.2979 0.1931  -0.0038 0.0248  120 ALA B CA  
3823 C C   . ALA B 105 ? 0.4925 0.8843 0.2945 0.1811  -0.0016 0.0283  120 ALA B C   
3824 O O   . ALA B 105 ? 0.4890 0.8805 0.2945 0.1805  -0.0041 0.0263  120 ALA B O   
3825 C CB  . ALA B 105 ? 0.4534 0.9056 0.2877 0.1791  -0.0037 0.0196  120 ALA B CB  
3826 N N   . PHE B 106 ? 0.4984 0.8647 0.2927 0.1710  0.0032  0.0329  121 PHE B N   
3827 C CA  . PHE B 106 ? 0.5054 0.8451 0.2993 0.1570  0.0050  0.0356  121 PHE B CA  
3828 C C   . PHE B 106 ? 0.5451 0.8423 0.3034 0.1619  0.0092  0.0419  121 PHE B C   
3829 O O   . PHE B 106 ? 0.5314 0.8042 0.2859 0.1477  0.0128  0.0446  121 PHE B O   
3830 C CB  . PHE B 106 ? 0.4916 0.8396 0.3112 0.1379  0.0074  0.0341  121 PHE B CB  
3831 C CG  . PHE B 106 ? 0.4687 0.8540 0.3197 0.1341  0.0038  0.0281  121 PHE B CG  
3832 C CD1 . PHE B 106 ? 0.4569 0.8544 0.3286 0.1266  -0.0021 0.0252  121 PHE B CD1 
3833 C CD2 . PHE B 106 ? 0.4597 0.8657 0.3161 0.1379  0.0060  0.0253  121 PHE B CD2 
3834 C CE1 . PHE B 106 ? 0.4317 0.8592 0.3285 0.1228  -0.0053 0.0198  121 PHE B CE1 
3835 C CE2 . PHE B 106 ? 0.4285 0.8660 0.3113 0.1339  0.0030  0.0191  121 PHE B CE2 
3836 C CZ  . PHE B 106 ? 0.4113 0.8586 0.3140 0.1264  -0.0025 0.0165  121 PHE B CZ  
3837 N N   . ALA B 107 ? 0.5862 0.8746 0.3183 0.1823  0.0083  0.0440  122 ALA B N   
3838 C CA  . ALA B 107 ? 0.6579 0.9013 0.3514 0.1905  0.0113  0.0500  122 ALA B CA  
3839 C C   . ALA B 107 ? 0.6985 0.9303 0.3830 0.1994  0.0085  0.0483  122 ALA B C   
3840 O O   . ALA B 107 ? 0.6914 0.9530 0.3913 0.2087  0.0041  0.0428  122 ALA B O   
3841 C CB  . ALA B 107 ? 0.6822 0.9185 0.3492 0.2097  0.0109  0.0539  122 ALA B CB  
3842 N N   . ASP B 108 ? 0.7423 0.9305 0.4007 0.1956  0.0120  0.0522  123 ASP B N   
3843 C CA  . ASP B 108 ? 0.7618 0.9339 0.4070 0.2045  0.0106  0.0500  123 ASP B CA  
3844 C C   . ASP B 108 ? 0.8035 0.9737 0.4283 0.2333  0.0085  0.0496  123 ASP B C   
3845 O O   . ASP B 108 ? 0.8639 1.0232 0.4691 0.2461  0.0085  0.0544  123 ASP B O   
3846 C CB  . ASP B 108 ? 0.8012 0.9236 0.4200 0.1927  0.0152  0.0539  123 ASP B CB  
3847 C CG  . ASP B 108 ? 0.7867 0.9144 0.4265 0.1702  0.0140  0.0508  123 ASP B CG  
3848 O OD1 . ASP B 108 ? 0.7502 0.9104 0.4148 0.1698  0.0094  0.0454  123 ASP B OD1 
3849 O OD2 . ASP B 108 ? 0.7909 0.8903 0.4213 0.1524  0.0174  0.0537  123 ASP B OD2 
3850 N N   . TYR B 109 ? 0.7998 0.9805 0.4285 0.2437  0.0065  0.0438  124 TYR B N   
3851 C CA  . TYR B 109 ? 0.8316 1.0092 0.4418 0.2727  0.0046  0.0421  124 TYR B CA  
3852 C C   . TYR B 109 ? 0.8994 1.0169 0.4657 0.2810  0.0081  0.0487  124 TYR B C   
3853 O O   . TYR B 109 ? 0.9346 1.0170 0.4873 0.2656  0.0124  0.0502  124 TYR B O   
3854 C CB  . TYR B 109 ? 0.8129 1.0122 0.4372 0.2778  0.0041  0.0331  124 TYR B CB  
3855 C CG  . TYR B 109 ? 0.8230 1.0301 0.4373 0.3078  0.0024  0.0283  124 TYR B CG  
3856 C CD1 . TYR B 109 ? 0.8758 1.0384 0.4563 0.3241  0.0050  0.0295  124 TYR B CD1 
3857 C CD2 . TYR B 109 ? 0.8054 1.0656 0.4457 0.3196  -0.0016 0.0216  124 TYR B CD2 
3858 C CE1 . TYR B 109 ? 0.9048 1.0769 0.4790 0.3540  0.0032  0.0240  124 TYR B CE1 
3859 C CE2 . TYR B 109 ? 0.8317 1.1052 0.4674 0.3479  -0.0035 0.0158  124 TYR B CE2 
3860 C CZ  . TYR B 109 ? 0.8820 1.1123 0.4858 0.3662  -0.0013 0.0169  124 TYR B CZ  
3861 O OH  . TYR B 109 ? 0.9243 1.1715 0.5272 0.3965  -0.0036 0.0101  124 TYR B OH  
3862 N N   . SER B 110 ? 0.9381 1.0427 0.4808 0.3048  0.0055  0.0528  125 SER B N   
3863 C CA  . SER B 110 ? 0.9845 1.0276 0.4808 0.3125  0.0084  0.0609  125 SER B CA  
3864 C C   . SER B 110 ? 1.0087 1.0466 0.4827 0.3449  0.0025  0.0642  125 SER B C   
3865 O O   . SER B 110 ? 0.9757 1.0591 0.4710 0.3559  -0.0037 0.0619  125 SER B O   
3866 C CB  . SER B 110 ? 0.9984 1.0178 0.4852 0.2875  0.0132  0.0685  125 SER B CB  
3867 O OG  . SER B 110 ? 0.9804 1.0263 0.4766 0.2890  0.0104  0.0715  125 SER B OG  
3868 N N   . PRO B 111 ? 1.0568 1.0375 0.4863 0.3601  0.0036  0.0699  126 PRO B N   
3869 C CA  . PRO B 111 ? 1.0877 1.0586 0.4926 0.3892  -0.0035 0.0753  126 PRO B CA  
3870 C C   . PRO B 111 ? 1.0725 1.0642 0.4829 0.3807  -0.0064 0.0812  126 PRO B C   
3871 O O   . PRO B 111 ? 1.0731 1.1006 0.4937 0.4003  -0.0150 0.0801  126 PRO B O   
3872 C CB  . PRO B 111 ? 1.1543 1.0471 0.5043 0.3965  0.0001  0.0833  126 PRO B CB  
3873 C CG  . PRO B 111 ? 1.1563 1.0207 0.5038 0.3683  0.0098  0.0815  126 PRO B CG  
3874 C CD  . PRO B 111 ? 1.0907 1.0131 0.4891 0.3522  0.0104  0.0716  126 PRO B CD  
3875 N N   . LEU B 112 ? 1.0454 1.0179 0.4504 0.3514  0.0008  0.0863  127 LEU B N   
3876 C CA  . LEU B 112 ? 1.0341 1.0280 0.4458 0.3417  -0.0002 0.0901  127 LEU B CA  
3877 C C   . LEU B 112 ? 0.9692 1.0356 0.4295 0.3438  -0.0059 0.0814  127 LEU B C   
3878 O O   . LEU B 112 ? 0.9681 1.0609 0.4304 0.3587  -0.0131 0.0820  127 LEU B O   
3879 C CB  . LEU B 112 ? 1.0374 1.0114 0.4473 0.3071  0.0100  0.0936  127 LEU B CB  
3880 C CG  . LEU B 112 ? 1.0361 1.0249 0.4482 0.2942  0.0119  0.0972  127 LEU B CG  
3881 C CD1 . LEU B 112 ? 1.0821 1.0490 0.4547 0.3167  0.0058  0.1054  127 LEU B CD1 
3882 C CD2 . LEU B 112 ? 1.0377 0.9995 0.4427 0.2617  0.0236  0.1003  127 LEU B CD2 
3883 N N   . TRP B 113 ? 0.9290 1.0257 0.4261 0.3289  -0.0031 0.0732  128 TRP B N   
3884 C CA  . TRP B 113 ? 0.8713 1.0327 0.4137 0.3254  -0.0069 0.0648  128 TRP B CA  
3885 C C   . TRP B 113 ? 0.8665 1.0638 0.4181 0.3543  -0.0157 0.0593  128 TRP B C   
3886 O O   . TRP B 113 ? 0.8291 1.0730 0.4041 0.3564  -0.0206 0.0554  128 TRP B O   
3887 C CB  . TRP B 113 ? 0.8312 1.0099 0.4052 0.3038  -0.0025 0.0580  128 TRP B CB  
3888 C CG  . TRP B 113 ? 0.7752 1.0138 0.3929 0.2955  -0.0054 0.0502  128 TRP B CG  
3889 C CD1 . TRP B 113 ? 0.7520 1.0136 0.3911 0.2768  -0.0040 0.0499  128 TRP B CD1 
3890 C CD2 . TRP B 113 ? 0.7438 1.0253 0.3874 0.3052  -0.0094 0.0410  128 TRP B CD2 
3891 N NE1 . TRP B 113 ? 0.7091 1.0218 0.3840 0.2742  -0.0074 0.0417  128 TRP B NE1 
3892 C CE2 . TRP B 113 ? 0.6973 1.0236 0.3754 0.2903  -0.0105 0.0362  128 TRP B CE2 
3893 C CE3 . TRP B 113 ? 0.7529 1.0391 0.3935 0.3246  -0.0112 0.0356  128 TRP B CE3 
3894 C CZ2 . TRP B 113 ? 0.6551 1.0286 0.3625 0.2922  -0.0134 0.0268  128 TRP B CZ2 
3895 C CZ3 . TRP B 113 ? 0.7078 1.0444 0.3799 0.3265  -0.0134 0.0257  128 TRP B CZ3 
3896 C CH2 . TRP B 113 ? 0.6607 1.0395 0.3647 0.3095  -0.0145 0.0217  128 TRP B CH2 
3897 N N   . LYS B 114 ? 0.9110 1.0881 0.4454 0.3761  -0.0175 0.0579  129 LYS B N   
3898 C CA  . LYS B 114 ? 0.9139 1.1281 0.4602 0.4046  -0.0255 0.0512  129 LYS B CA  
3899 C C   . LYS B 114 ? 0.9492 1.1702 0.4802 0.4232  -0.0345 0.0567  129 LYS B C   
3900 O O   . LYS B 114 ? 0.9203 1.1951 0.4772 0.4323  -0.0415 0.0505  129 LYS B O   
3901 C CB  . LYS B 114 ? 0.9530 1.1387 0.4803 0.4266  -0.0250 0.0487  129 LYS B CB  
3902 C CG  . LYS B 114 ? 0.9489 1.1266 0.4875 0.4097  -0.0165 0.0427  129 LYS B CG  
3903 C CD  . LYS B 114 ? 0.9550 1.1604 0.5094 0.4294  -0.0172 0.0312  129 LYS B CD  
3904 C CE  . LYS B 114 ? 1.0216 1.1914 0.5434 0.4636  -0.0202 0.0324  129 LYS B CE  
3905 N NZ  . LYS B 114 ? 1.0653 1.1691 0.5528 0.4576  -0.0126 0.0362  129 LYS B NZ  
3906 N N   . ASN B 115 ? 1.0117 1.1775 0.4990 0.4274  -0.0345 0.0682  130 ASN B N   
3907 C CA  . ASN B 115 ? 1.0431 1.2071 0.5080 0.4437  -0.0436 0.0753  130 ASN B CA  
3908 C C   . ASN B 115 ? 0.9856 1.1898 0.4746 0.4228  -0.0433 0.0738  130 ASN B C   
3909 O O   . ASN B 115 ? 0.9643 1.2074 0.4630 0.4348  -0.0524 0.0717  130 ASN B O   
3910 C CB  . ASN B 115 ? 1.1143 1.2043 0.5232 0.4457  -0.0415 0.0888  130 ASN B CB  
3911 C CG  . ASN B 115 ? 1.1794 1.2223 0.5554 0.4724  -0.0440 0.0915  130 ASN B CG  
3912 O OD1 . ASN B 115 ? 1.1764 1.2456 0.5668 0.4992  -0.0510 0.0844  130 ASN B OD1 
3913 N ND2 . ASN B 115 ? 1.2302 1.2026 0.5616 0.4646  -0.0375 0.1011  130 ASN B ND2 
3914 N N   . HIS B 116 ? 0.9465 1.1415 0.4456 0.3911  -0.0327 0.0743  131 HIS B N   
3915 C CA  . HIS B 116 ? 0.9039 1.1327 0.4263 0.3696  -0.0305 0.0721  131 HIS B CA  
3916 C C   . HIS B 116 ? 0.8703 1.1681 0.4368 0.3734  -0.0364 0.0608  131 HIS B C   
3917 O O   . HIS B 116 ? 0.8564 1.1864 0.4306 0.3750  -0.0418 0.0592  131 HIS B O   
3918 C CB  . HIS B 116 ? 0.8670 1.0781 0.3988 0.3373  -0.0186 0.0726  131 HIS B CB  
3919 C CG  . HIS B 116 ? 0.8358 1.0706 0.3849 0.3157  -0.0148 0.0713  131 HIS B CG  
3920 N ND1 . HIS B 116 ? 0.8088 1.0464 0.3805 0.2876  -0.0057 0.0686  131 HIS B ND1 
3921 C CD2 . HIS B 116 ? 0.8374 1.0955 0.3853 0.3187  -0.0190 0.0715  131 HIS B CD2 
3922 C CE1 . HIS B 116 ? 0.7986 1.0589 0.3826 0.2748  -0.0035 0.0668  131 HIS B CE1 
3923 N NE2 . HIS B 116 ? 0.8192 1.0916 0.3880 0.2924  -0.0111 0.0685  131 HIS B NE2 
3924 N N   . ARG B 117 ? 0.8673 1.1861 0.4595 0.3749  -0.0353 0.0526  132 ARG B N   
3925 C CA  . ARG B 117 ? 0.8313 1.2137 0.4646 0.3751  -0.0392 0.0413  132 ARG B CA  
3926 C C   . ARG B 117 ? 0.8538 1.2695 0.4873 0.4040  -0.0507 0.0377  132 ARG B C   
3927 O O   . ARG B 117 ? 0.8306 1.2967 0.4890 0.4013  -0.0553 0.0311  132 ARG B O   
3928 C CB  . ARG B 117 ? 0.8043 1.1973 0.4610 0.3675  -0.0341 0.0337  132 ARG B CB  
3929 C CG  . ARG B 117 ? 0.7562 1.2085 0.4550 0.3561  -0.0348 0.0227  132 ARG B CG  
3930 C CD  . ARG B 117 ? 0.7416 1.2017 0.4583 0.3496  -0.0300 0.0155  132 ARG B CD  
3931 N NE  . ARG B 117 ? 0.6971 1.2106 0.4504 0.3369  -0.0302 0.0054  132 ARG B NE  
3932 C CZ  . ARG B 117 ? 0.6874 1.2491 0.4578 0.3503  -0.0354 -0.0031 132 ARG B CZ  
3933 N NH1 . ARG B 117 ? 0.6981 1.2644 0.4550 0.3791  -0.0421 -0.0031 132 ARG B NH1 
3934 N NH2 . ARG B 117 ? 0.6708 1.2764 0.4718 0.3346  -0.0343 -0.0120 132 ARG B NH2 
3935 N N   . ARG B 118 ? 0.9194 1.3077 0.5260 0.4316  -0.0557 0.0415  133 ARG B N   
3936 C CA  . ARG B 118 ? 0.9469 1.3660 0.5539 0.4631  -0.0682 0.0381  133 ARG B CA  
3937 C C   . ARG B 118 ? 0.9813 1.4108 0.5759 0.4650  -0.0765 0.0434  133 ARG B C   
3938 O O   . ARG B 118 ? 0.9940 1.4743 0.6071 0.4769  -0.0862 0.0369  133 ARG B O   
3939 C CB  . ARG B 118 ? 0.9959 1.3717 0.5699 0.4931  -0.0721 0.0431  133 ARG B CB  
3940 C CG  . ARG B 118 ? 1.0200 1.4355 0.6066 0.5272  -0.0834 0.0353  133 ARG B CG  
3941 C CD  . ARG B 118 ? 1.1080 1.4717 0.6572 0.5581  -0.0873 0.0415  133 ARG B CD  
3942 N NE  . ARG B 118 ? 1.1588 1.4822 0.7005 0.5492  -0.0751 0.0406  133 ARG B NE  
3943 C CZ  . ARG B 118 ? 1.2223 1.4741 0.7210 0.5550  -0.0715 0.0502  133 ARG B CZ  
3944 N NH1 . ARG B 118 ? 1.2768 1.4833 0.7322 0.5697  -0.0788 0.0628  133 ARG B NH1 
3945 N NH2 . ARG B 118 ? 1.2155 1.4384 0.7119 0.5443  -0.0604 0.0473  133 ARG B NH2 
3946 N N   . LEU B 119 ? 0.9868 1.3687 0.5496 0.4518  -0.0722 0.0545  134 LEU B N   
3947 C CA  . LEU B 119 ? 0.9971 1.3843 0.5451 0.4489  -0.0777 0.0594  134 LEU B CA  
3948 C C   . LEU B 119 ? 0.9400 1.3867 0.5289 0.4286  -0.0764 0.0493  134 LEU B C   
3949 O O   . LEU B 119 ? 0.9432 1.4304 0.5400 0.4377  -0.0865 0.0454  134 LEU B O   
3950 C CB  . LEU B 119 ? 1.0400 1.3663 0.5503 0.4320  -0.0692 0.0713  134 LEU B CB  
3951 C CG  . LEU B 119 ? 1.0745 1.3947 0.5602 0.4267  -0.0727 0.0778  134 LEU B CG  
3952 C CD1 . LEU B 119 ? 1.0956 1.4194 0.5557 0.4588  -0.0895 0.0822  134 LEU B CD1 
3953 C CD2 . LEU B 119 ? 1.1034 1.3610 0.5525 0.4079  -0.0613 0.0884  134 LEU B CD2 
3954 N N   . VAL B 120 ? 0.8910 1.3424 0.5052 0.4014  -0.0648 0.0448  135 VAL B N   
3955 C CA  . VAL B 120 ? 0.8383 1.3374 0.4884 0.3798  -0.0622 0.0358  135 VAL B CA  
3956 C C   . VAL B 120 ? 0.8178 1.3786 0.5012 0.3907  -0.0698 0.0238  135 VAL B C   
3957 O O   . VAL B 120 ? 0.7837 1.3848 0.4798 0.3884  -0.0754 0.0184  135 VAL B O   
3958 C CB  . VAL B 120 ? 0.7909 1.2798 0.4614 0.3510  -0.0494 0.0336  135 VAL B CB  
3959 C CG1 . VAL B 120 ? 0.7380 1.2745 0.4450 0.3312  -0.0476 0.0239  135 VAL B CG1 
3960 C CG2 . VAL B 120 ? 0.8113 1.2476 0.4542 0.3366  -0.0411 0.0436  135 VAL B CG2 
3961 N N   . HIS B 121 ? 0.8468 1.4155 0.5437 0.4013  -0.0691 0.0187  136 HIS B N   
3962 C CA  . HIS B 121 ? 0.8486 1.4776 0.5783 0.4101  -0.0745 0.0060  136 HIS B CA  
3963 C C   . HIS B 121 ? 0.8829 1.5385 0.6037 0.4361  -0.0888 0.0055  136 HIS B C   
3964 O O   . HIS B 121 ? 0.8819 1.5923 0.6271 0.4339  -0.0945 -0.0038 136 HIS B O   
3965 C CB  . HIS B 121 ? 0.8655 1.4944 0.6063 0.4194  -0.0706 0.0007  136 HIS B CB  
3966 C CG  . HIS B 121 ? 0.8583 1.5503 0.6326 0.4278  -0.0745 -0.0133 136 HIS B CG  
3967 N ND1 . HIS B 121 ? 0.7937 1.5202 0.6008 0.4060  -0.0674 -0.0237 136 HIS B ND1 
3968 C CD2 . HIS B 121 ? 0.8913 1.6195 0.6712 0.4551  -0.0850 -0.0191 136 HIS B CD2 
3969 C CE1 . HIS B 121 ? 0.8077 1.5891 0.6389 0.4176  -0.0719 -0.0356 136 HIS B CE1 
3970 N NE2 . HIS B 121 ? 0.8744 1.6604 0.6919 0.4479  -0.0829 -0.0336 136 HIS B NE2 
3971 N N   . SER B 122 ? 0.9388 1.5541 0.6234 0.4604  -0.0952 0.0155  137 SER B N   
3972 C CA  . SER B 122 ? 0.9490 1.5809 0.6186 0.4875  -0.1110 0.0174  137 SER B CA  
3973 C C   . SER B 122 ? 0.9442 1.5971 0.6116 0.4735  -0.1156 0.0181  137 SER B C   
3974 O O   . SER B 122 ? 0.9456 1.6472 0.6256 0.4848  -0.1275 0.0117  137 SER B O   
3975 C CB  . SER B 122 ? 1.0070 1.5763 0.6290 0.5109  -0.1157 0.0311  137 SER B CB  
3976 O OG  . SER B 122 ? 1.0665 1.6331 0.6616 0.5250  -0.1290 0.0381  137 SER B OG  
3977 N N   . SER B 123 ? 0.9334 1.5502 0.5845 0.4489  -0.1062 0.0252  138 SER B N   
3978 C CA  . SER B 123 ? 0.9141 1.5465 0.5611 0.4339  -0.1084 0.0252  138 SER B CA  
3979 C C   . SER B 123 ? 0.8566 1.5524 0.5482 0.4168  -0.1070 0.0106  138 SER B C   
3980 O O   . SER B 123 ? 0.8448 1.5849 0.5450 0.4242  -0.1179 0.0045  138 SER B O   
3981 C CB  . SER B 123 ? 0.9386 1.5198 0.5614 0.4109  -0.0965 0.0343  138 SER B CB  
3982 O OG  . SER B 123 ? 0.9872 1.5089 0.5655 0.4258  -0.0978 0.0476  138 SER B OG  
3983 N N   . PHE B 124 ? 0.8219 1.5222 0.5410 0.3948  -0.0946 0.0048  139 PHE B N   
3984 C CA  . PHE B 124 ? 0.7848 1.5404 0.5439 0.3773  -0.0925 -0.0089 139 PHE B CA  
3985 C C   . PHE B 124 ? 0.7767 1.5903 0.5582 0.3951  -0.1032 -0.0196 139 PHE B C   
3986 O O   . PHE B 124 ? 0.7055 1.5677 0.5097 0.3837  -0.1059 -0.0300 139 PHE B O   
3987 C CB  . PHE B 124 ? 0.7679 1.5168 0.5508 0.3566  -0.0796 -0.0128 139 PHE B CB  
3988 C CG  . PHE B 124 ? 0.7973 1.5089 0.5735 0.3320  -0.0687 -0.0073 139 PHE B CG  
3989 C CD1 . PHE B 124 ? 0.7851 1.4973 0.5542 0.3182  -0.0677 -0.0068 139 PHE B CD1 
3990 C CD2 . PHE B 124 ? 0.7814 1.4595 0.5601 0.3220  -0.0591 -0.0037 139 PHE B CD2 
3991 C CE1 . PHE B 124 ? 0.8056 1.4864 0.5719 0.2965  -0.0568 -0.0031 139 PHE B CE1 
3992 C CE2 . PHE B 124 ? 0.7918 1.4395 0.5680 0.3002  -0.0496 0.0005  139 PHE B CE2 
3993 C CZ  . PHE B 124 ? 0.7948 1.4445 0.5659 0.2879  -0.0481 0.0006  139 PHE B CZ  
3994 N N   . THR B 125 ? 0.8182 1.6271 0.5948 0.4218  -0.1083 -0.0182 140 THR B N   
3995 C CA  . THR B 125 ? 0.8331 1.6986 0.6326 0.4420  -0.1184 -0.0291 140 THR B CA  
3996 C C   . THR B 125 ? 0.8817 1.7719 0.6684 0.4599  -0.1350 -0.0282 140 THR B C   
3997 O O   . THR B 125 ? 0.9093 1.8608 0.7226 0.4655  -0.1430 -0.0401 140 THR B O   
3998 C CB  . THR B 125 ? 0.8457 1.6995 0.6442 0.4678  -0.1188 -0.0291 140 THR B CB  
3999 O OG1 . THR B 125 ? 0.8408 1.6658 0.6455 0.4510  -0.1041 -0.0288 140 THR B OG1 
4000 C CG2 . THR B 125 ? 0.8147 1.7364 0.6465 0.4841  -0.1261 -0.0439 140 THR B CG2 
4001 N N   . LEU B 126 ? 0.9230 1.7685 0.6693 0.4676  -0.1405 -0.0148 141 LEU B N   
4002 C CA  . LEU B 126 ? 0.9597 1.8275 0.6906 0.4806  -0.1569 -0.0134 141 LEU B CA  
4003 C C   . LEU B 126 ? 0.9759 1.8845 0.7268 0.4519  -0.1545 -0.0228 141 LEU B C   
4004 O O   . LEU B 126 ? 0.9907 1.8869 0.7185 0.4427  -0.1576 -0.0180 141 LEU B O   
4005 C CB  . LEU B 126 ? 0.9867 1.7921 0.6648 0.4930  -0.1623 0.0037  141 LEU B CB  
4006 C CG  . LEU B 126 ? 1.0011 1.8202 0.6546 0.5074  -0.1804 0.0075  141 LEU B CG  
4007 C CD1 . LEU B 126 ? 1.0460 1.8396 0.6676 0.5465  -0.1964 0.0176  141 LEU B CD1 
4008 C CD2 . LEU B 126 ? 0.9998 1.7861 0.6233 0.4833  -0.1748 0.0149  141 LEU B CD2 
4009 N N   . PHE B 127 ? 0.9943 1.9495 0.7869 0.4371  -0.1480 -0.0369 142 PHE B N   
4010 C CA  . PHE B 127 ? 0.9622 1.9592 0.7795 0.4085  -0.1440 -0.0484 142 PHE B CA  
4011 C C   . PHE B 127 ? 0.9287 1.9876 0.7900 0.4061  -0.1430 -0.0647 142 PHE B C   
4012 O O   . PHE B 127 ? 0.8987 2.0051 0.7830 0.3879  -0.1434 -0.0768 142 PHE B O   
4013 C CB  . PHE B 127 ? 0.8911 1.8486 0.7032 0.3774  -0.1279 -0.0446 142 PHE B CB  
4014 C CG  . PHE B 127 ? 0.9266 1.8274 0.6974 0.3778  -0.1270 -0.0304 142 PHE B CG  
4015 C CD1 . PHE B 127 ? 0.9666 1.8712 0.7203 0.3685  -0.1313 -0.0300 142 PHE B CD1 
4016 C CD2 . PHE B 127 ? 0.9495 1.7927 0.6968 0.3863  -0.1213 -0.0180 142 PHE B CD2 
4017 C CE1 . PHE B 127 ? 1.0081 1.8601 0.7221 0.3670  -0.1288 -0.0175 142 PHE B CE1 
4018 C CE2 . PHE B 127 ? 0.9831 1.7741 0.6912 0.3846  -0.1192 -0.0054 142 PHE B CE2 
4019 C CZ  . PHE B 127 ? 0.9806 1.7761 0.6721 0.3747  -0.1225 -0.0052 142 PHE B CZ  
4020 N N   . GLY B 128 ? 0.9456 2.0022 0.8167 0.4234  -0.1408 -0.0654 143 GLY B N   
4021 C CA  . GLY B 128 ? 0.9461 2.0646 0.8504 0.4363  -0.1459 -0.0795 143 GLY B CA  
4022 C C   . GLY B 128 ? 1.0063 2.1563 0.9038 0.4663  -0.1659 -0.0799 143 GLY B C   
4023 O O   . GLY B 128 ? 1.0131 2.2283 0.9402 0.4747  -0.1736 -0.0935 143 GLY B O   
4024 N N   . GLU B 129 ? 1.0789 2.1817 0.9364 0.4832  -0.1746 -0.0649 144 GLU B N   
4025 C CA  . GLU B 129 ? 1.1402 2.2647 0.9820 0.5003  -0.1940 -0.0629 144 GLU B CA  
4026 C C   . GLU B 129 ? 1.1788 2.2639 0.9891 0.4781  -0.1910 -0.0534 144 GLU B C   
4027 O O   . GLU B 129 ? 1.1994 2.2997 1.0245 0.4462  -0.1813 -0.0606 144 GLU B O   
4028 C CB  . GLU B 129 ? 1.1774 2.2823 0.9966 0.5430  -0.2091 -0.0539 144 GLU B CB  
4029 C CG  . GLU B 129 ? 1.2385 2.3603 1.0364 0.5642  -0.2318 -0.0498 144 GLU B CG  
4030 C CD  . GLU B 129 ? 1.2571 2.4622 1.0895 0.5571  -0.2422 -0.0661 144 GLU B CD  
4031 O OE1 . GLU B 129 ? 1.2419 2.4812 1.1058 0.5257  -0.2295 -0.0786 144 GLU B OE1 
4032 O OE2 . GLU B 129 ? 1.2327 2.4683 1.0593 0.5825  -0.2637 -0.0664 144 GLU B OE2 
4033 N N   . GLY B 130 ? 1.2135 2.2459 0.9793 0.4938  -0.1981 -0.0378 145 GLY B N   
4034 C CA  . GLY B 130 ? 1.1630 2.1559 0.8962 0.4736  -0.1939 -0.0289 145 GLY B CA  
4035 C C   . GLY B 130 ? 1.1032 2.1292 0.8350 0.4560  -0.2001 -0.0350 145 GLY B C   
4036 O O   . GLY B 130 ? 1.1135 2.1150 0.8360 0.4282  -0.1878 -0.0337 145 GLY B O   
4037 N N   . SER B 131 ? 1.0626 2.1475 0.8078 0.4681  -0.2174 -0.0439 146 SER B N   
4038 C CA  . SER B 131 ? 0.9903 2.1440 0.7816 0.4756  -0.2222 -0.0594 146 SER B CA  
4039 C C   . SER B 131 ? 0.8994 2.0793 0.7200 0.4364  -0.2068 -0.0722 146 SER B C   
4040 O O   . SER B 131 ? 0.8580 2.0647 0.7142 0.4265  -0.1968 -0.0826 146 SER B O   
4041 C CB  . SER B 131 ? 1.0151 2.2252 0.8097 0.4961  -0.2460 -0.0654 146 SER B CB  
4042 O OG  . SER B 131 ? 1.0571 2.2305 0.8083 0.5249  -0.2624 -0.0503 146 SER B OG  
4043 N N   . ASN B 132 ? 0.8946 2.0646 0.6968 0.4143  -0.2054 -0.0714 147 ASN B N   
4044 C CA  . ASN B 132 ? 0.8520 2.0340 0.6731 0.3772  -0.1908 -0.0816 147 ASN B CA  
4045 C C   . ASN B 132 ? 0.8910 2.0115 0.6796 0.3583  -0.1789 -0.0714 147 ASN B C   
4046 O O   . ASN B 132 ? 0.8992 2.0271 0.6899 0.3313  -0.1724 -0.0785 147 ASN B O   
4047 C CB  . ASN B 132 ? 0.5648 1.8126 0.4037 0.3659  -0.2011 -0.0966 147 ASN B CB  
4048 C CG  . ASN B 132 ? 0.5455 1.8611 0.4264 0.3753  -0.2074 -0.1108 147 ASN B CG  
4049 O OD1 . ASN B 132 ? 0.5265 1.8411 0.4291 0.3802  -0.1985 -0.1124 147 ASN B OD1 
4050 N ND2 . ASN B 132 ? 0.5517 1.9279 0.4442 0.3770  -0.2226 -0.1218 147 ASN B ND2 
4051 N N   . LYS B 133 ? 0.9512 2.0111 0.7097 0.3716  -0.1755 -0.0558 148 LYS B N   
4052 C CA  . LYS B 133 ? 0.9831 1.9851 0.7134 0.3530  -0.1620 -0.0468 148 LYS B CA  
4053 C C   . LYS B 133 ? 0.8774 1.8781 0.6357 0.3227  -0.1433 -0.0549 148 LYS B C   
4054 O O   . LYS B 133 ? 0.8438 1.8350 0.5962 0.2991  -0.1349 -0.0581 148 LYS B O   
4055 C CB  . LYS B 133 ? 1.0861 2.0243 0.7848 0.3694  -0.1587 -0.0300 148 LYS B CB  
4056 C CG  . LYS B 133 ? 1.2646 2.1810 0.9191 0.3940  -0.1747 -0.0181 148 LYS B CG  
4057 C CD  . LYS B 133 ? 1.3747 2.2331 1.0021 0.4143  -0.1731 -0.0029 148 LYS B CD  
4058 C CE  . LYS B 133 ? 1.4269 2.2763 1.0195 0.4478  -0.1938 0.0070  148 LYS B CE  
4059 N NZ  . LYS B 133 ? 1.4636 2.3032 1.0179 0.4426  -0.2021 0.0118  148 LYS B NZ  
4060 N N   . LEU B 134 ? 0.8336 1.8439 0.6214 0.3242  -0.1373 -0.0585 149 LEU B N   
4061 C CA  . LEU B 134 ? 0.7878 1.7909 0.6003 0.2980  -0.1206 -0.0642 149 LEU B CA  
4062 C C   . LEU B 134 ? 0.7256 1.7786 0.5646 0.2766  -0.1200 -0.0800 149 LEU B C   
4063 O O   . LEU B 134 ? 0.7122 1.7542 0.5562 0.2509  -0.1089 -0.0845 149 LEU B O   
4064 C CB  . LEU B 134 ? 0.8009 1.7986 0.6330 0.3062  -0.1154 -0.0631 149 LEU B CB  
4065 C CG  . LEU B 134 ? 0.8050 1.7846 0.6566 0.2812  -0.0991 -0.0659 149 LEU B CG  
4066 C CD1 . LEU B 134 ? 0.8407 1.7591 0.6694 0.2746  -0.0891 -0.0540 149 LEU B CD1 
4067 C CD2 . LEU B 134 ? 0.7916 1.7832 0.6665 0.2875  -0.0964 -0.0689 149 LEU B CD2 
4068 N N   . GLN B 135 ? 0.6691 1.7773 0.5256 0.2873  -0.1320 -0.0892 150 GLN B N   
4069 C CA  . GLN B 135 ? 0.6273 1.7860 0.5075 0.2664  -0.1323 -0.1051 150 GLN B CA  
4070 C C   . GLN B 135 ? 0.6391 1.7887 0.5003 0.2476  -0.1311 -0.1072 150 GLN B C   
4071 O O   . GLN B 135 ? 0.6505 1.8032 0.5243 0.2204  -0.1207 -0.1161 150 GLN B O   
4072 C CB  . GLN B 135 ? 0.6204 1.8415 0.5167 0.2835  -0.1481 -0.1139 150 GLN B CB  
4073 C CG  . GLN B 135 ? 0.5859 1.8640 0.5090 0.2603  -0.1481 -0.1318 150 GLN B CG  
4074 C CD  . GLN B 135 ? 0.5712 1.9138 0.5217 0.2755  -0.1592 -0.1423 150 GLN B CD  
4075 O OE1 . GLN B 135 ? 0.5381 1.8972 0.5151 0.2726  -0.1515 -0.1483 150 GLN B OE1 
4076 N NE2 . GLN B 135 ? 0.5921 1.9720 0.5361 0.2924  -0.1775 -0.1448 150 GLN B NE2 
4077 N N   . THR B 136 ? 0.6579 1.7928 0.4865 0.2622  -0.1413 -0.0990 151 THR B N   
4078 C CA  . THR B 136 ? 0.6659 1.7943 0.4719 0.2464  -0.1415 -0.1014 151 THR B CA  
4079 C C   . THR B 136 ? 0.6511 1.7300 0.4493 0.2243  -0.1228 -0.0985 151 THR B C   
4080 O O   . THR B 136 ? 0.6170 1.7028 0.4240 0.1988  -0.1142 -0.1088 151 THR B O   
4081 C CB  . THR B 136 ? 0.7150 1.8277 0.4815 0.2685  -0.1558 -0.0903 151 THR B CB  
4082 O OG1 . THR B 136 ? 0.7149 1.8763 0.4895 0.2912  -0.1753 -0.0935 151 THR B OG1 
4083 C CG2 . THR B 136 ? 0.7485 1.8515 0.4882 0.2511  -0.1548 -0.0928 151 THR B CG2 
4084 N N   . ILE B 137 ? 0.6552 1.6841 0.4371 0.2348  -0.1166 -0.0847 152 ILE B N   
4085 C CA  . ILE B 137 ? 0.6346 1.6181 0.4131 0.2171  -0.0991 -0.0814 152 ILE B CA  
4086 C C   . ILE B 137 ? 0.6115 1.6139 0.4251 0.1938  -0.0890 -0.0939 152 ILE B C   
4087 O O   . ILE B 137 ? 0.6115 1.6066 0.4253 0.1719  -0.0798 -0.1010 152 ILE B O   
4088 C CB  . ILE B 137 ? 0.6412 1.5793 0.4106 0.2316  -0.0941 -0.0672 152 ILE B CB  
4089 C CG1 . ILE B 137 ? 0.6771 1.5842 0.4042 0.2495  -0.1012 -0.0542 152 ILE B CG1 
4090 C CG2 . ILE B 137 ? 0.6241 1.5248 0.4032 0.2123  -0.0760 -0.0661 152 ILE B CG2 
4091 C CD1 . ILE B 137 ? 0.6863 1.5578 0.4026 0.2695  -0.1014 -0.0409 152 ILE B CD1 
4092 N N   . VAL B 138 ? 0.5800 1.6062 0.4212 0.1983  -0.0907 -0.0972 153 VAL B N   
4093 C CA  . VAL B 138 ? 0.5540 1.5874 0.4245 0.1763  -0.0800 -0.1064 153 VAL B CA  
4094 C C   . VAL B 138 ? 0.5380 1.6135 0.4202 0.1573  -0.0823 -0.1219 153 VAL B C   
4095 O O   . VAL B 138 ? 0.4943 1.5651 0.3901 0.1342  -0.0722 -0.1299 153 VAL B O   
4096 C CB  . VAL B 138 ? 0.5402 1.5817 0.4335 0.1844  -0.0794 -0.1050 153 VAL B CB  
4097 C CG1 . VAL B 138 ? 0.5142 1.5584 0.4326 0.1602  -0.0687 -0.1136 153 VAL B CG1 
4098 C CG2 . VAL B 138 ? 0.5429 1.5385 0.4232 0.2005  -0.0760 -0.0903 153 VAL B CG2 
4099 N N   . GLN B 139 ? 0.5728 1.6880 0.4484 0.1673  -0.0961 -0.1263 154 GLN B N   
4100 C CA  . GLN B 139 ? 0.5784 1.7366 0.4629 0.1491  -0.0996 -0.1416 154 GLN B CA  
4101 C C   . GLN B 139 ? 0.5789 1.7130 0.4420 0.1317  -0.0934 -0.1444 154 GLN B C   
4102 O O   . GLN B 139 ? 0.5372 1.6761 0.4104 0.1070  -0.0852 -0.1558 154 GLN B O   
4103 C CB  . GLN B 139 ? 0.6078 1.8204 0.4943 0.1659  -0.1178 -0.1461 154 GLN B CB  
4104 C CG  . GLN B 139 ? 0.6028 1.8540 0.5202 0.1742  -0.1209 -0.1509 154 GLN B CG  
4105 C CD  . GLN B 139 ? 0.6676 1.9826 0.5944 0.1871  -0.1382 -0.1594 154 GLN B CD  
4106 O OE1 . GLN B 139 ? 0.7160 2.0379 0.6217 0.2044  -0.1522 -0.1549 154 GLN B OE1 
4107 N NE2 . GLN B 139 ? 0.6850 2.0479 0.6437 0.1787  -0.1375 -0.1721 154 GLN B NE2 
4108 N N   . GLU B 140 ? 0.6165 1.7213 0.4488 0.1440  -0.0960 -0.1341 155 GLU B N   
4109 C CA  . GLU B 140 ? 0.6561 1.7341 0.4655 0.1282  -0.0881 -0.1364 155 GLU B CA  
4110 C C   . GLU B 140 ? 0.6448 1.6799 0.4635 0.1127  -0.0694 -0.1357 155 GLU B C   
4111 O O   . GLU B 140 ? 0.6452 1.6707 0.4621 0.0920  -0.0599 -0.1447 155 GLU B O   
4112 C CB  . GLU B 140 ? 0.7014 1.7545 0.4728 0.1447  -0.0943 -0.1246 155 GLU B CB  
4113 C CG  . GLU B 140 ? 0.7247 1.8146 0.4797 0.1606  -0.1144 -0.1246 155 GLU B CG  
4114 C CD  . GLU B 140 ? 0.7745 1.8301 0.4892 0.1793  -0.1204 -0.1097 155 GLU B CD  
4115 O OE1 . GLU B 140 ? 0.8077 1.8171 0.5017 0.1708  -0.1072 -0.1043 155 GLU B OE1 
4116 O OE2 . GLU B 140 ? 0.8027 1.8769 0.5058 0.2025  -0.1379 -0.1036 155 GLU B OE2 
4117 N N   . ALA B 141 ? 0.6242 1.6333 0.4524 0.1233  -0.0646 -0.1253 156 ALA B N   
4118 C CA  . ALA B 141 ? 0.6178 1.5916 0.4593 0.1101  -0.0492 -0.1247 156 ALA B CA  
4119 C C   . ALA B 141 ? 0.5935 1.5871 0.4617 0.0897  -0.0447 -0.1376 156 ALA B C   
4120 O O   . ALA B 141 ? 0.6201 1.5923 0.4936 0.0722  -0.0333 -0.1433 156 ALA B O   
4121 C CB  . ALA B 141 ? 0.6205 1.5678 0.4677 0.1249  -0.0471 -0.1117 156 ALA B CB  
4122 N N   . ALA B 142 ? 0.5718 1.6059 0.4561 0.0915  -0.0533 -0.1429 157 ALA B N   
4123 C CA  . ALA B 142 ? 0.5760 1.6280 0.4822 0.0702  -0.0488 -0.1552 157 ALA B CA  
4124 C C   . ALA B 142 ? 0.6065 1.6691 0.5043 0.0498  -0.0465 -0.1686 157 ALA B C   
4125 O O   . ALA B 142 ? 0.6224 1.6745 0.5304 0.0290  -0.0374 -0.1771 157 ALA B O   
4126 C CB  . ALA B 142 ? 0.5675 1.6636 0.4919 0.0754  -0.0574 -0.1591 157 ALA B CB  
4127 N N   . ASP B 143 ? 0.6617 1.7418 0.5386 0.0555  -0.0548 -0.1702 158 ASP B N   
4128 C CA  . ASP B 143 ? 0.6694 1.7588 0.5343 0.0360  -0.0530 -0.1832 158 ASP B CA  
4129 C C   . ASP B 143 ? 0.6681 1.7113 0.5221 0.0232  -0.0380 -0.1847 158 ASP B C   
4130 O O   . ASP B 143 ? 0.6526 1.6937 0.5100 0.0015  -0.0306 -0.1973 158 ASP B O   
4131 C CB  . ASP B 143 ? 0.6949 1.8161 0.5384 0.0458  -0.0674 -0.1843 158 ASP B CB  
4132 C CG  . ASP B 143 ? 0.7443 1.9248 0.6035 0.0422  -0.0797 -0.1949 158 ASP B CG  
4133 O OD1 . ASP B 143 ? 0.7617 1.9566 0.6350 0.0187  -0.0742 -0.2083 158 ASP B OD1 
4134 O OD2 . ASP B 143 ? 0.7701 1.9827 0.6279 0.0624  -0.0947 -0.1904 158 ASP B OD2 
4135 N N   . SER B 144 ? 0.6596 1.6660 0.5012 0.0361  -0.0328 -0.1727 159 SER B N   
4136 C CA  . SER B 144 ? 0.6617 1.6266 0.4972 0.0254  -0.0174 -0.1747 159 SER B CA  
4137 C C   . SER B 144 ? 0.6694 1.6197 0.5319 0.0115  -0.0079 -0.1801 159 SER B C   
4138 O O   . SER B 144 ? 0.6494 1.5874 0.5132 -0.0063 0.0014  -0.1914 159 SER B O   
4139 C CB  . SER B 144 ? 0.6501 1.5795 0.4727 0.0409  -0.0126 -0.1605 159 SER B CB  
4140 O OG  . SER B 144 ? 0.6355 1.5765 0.4410 0.0611  -0.0250 -0.1495 159 SER B OG  
4141 N N   . LEU B 145 ? 0.6730 1.6236 0.5550 0.0204  -0.0107 -0.1719 160 LEU B N   
4142 C CA  . LEU B 145 ? 0.6433 1.5807 0.5489 0.0091  -0.0045 -0.1748 160 LEU B CA  
4143 C C   . LEU B 145 ? 0.6336 1.5931 0.5442 -0.0120 -0.0047 -0.1899 160 LEU B C   
4144 O O   . LEU B 145 ? 0.5946 1.5318 0.5105 -0.0281 0.0044  -0.1977 160 LEU B O   
4145 C CB  . LEU B 145 ? 0.6417 1.5856 0.5625 0.0218  -0.0103 -0.1646 160 LEU B CB  
4146 C CG  . LEU B 145 ? 0.6201 1.5530 0.5626 0.0115  -0.0063 -0.1657 160 LEU B CG  
4147 C CD1 . LEU B 145 ? 0.6365 1.5256 0.5850 0.0042  0.0047  -0.1650 160 LEU B CD1 
4148 C CD2 . LEU B 145 ? 0.5901 1.5277 0.5418 0.0266  -0.0118 -0.1546 160 LEU B CD2 
4149 N N   . CYS B 146 ? 0.6526 1.6561 0.5611 -0.0119 -0.0154 -0.1945 161 CYS B N   
4150 C CA  . CYS B 146 ? 0.6641 1.6933 0.5761 -0.0336 -0.0161 -0.2097 161 CYS B CA  
4151 C C   . CYS B 146 ? 0.7096 1.7226 0.6059 -0.0498 -0.0085 -0.2210 161 CYS B C   
4152 O O   . CYS B 146 ? 0.7246 1.7277 0.6256 -0.0705 -0.0017 -0.2318 161 CYS B O   
4153 C CB  . CYS B 146 ? 0.6530 1.7374 0.5658 -0.0294 -0.0295 -0.2137 161 CYS B CB  
4154 S SG  . CYS B 146 ? 0.6192 1.7289 0.5579 -0.0273 -0.0333 -0.2114 161 CYS B SG  
4155 N N   . GLU B 147 ? 0.7494 1.7560 0.6252 -0.0410 -0.0090 -0.2185 162 GLU B N   
4156 C CA  . GLU B 147 ? 0.8029 1.7925 0.6616 -0.0559 -0.0004 -0.2296 162 GLU B CA  
4157 C C   . GLU B 147 ? 0.8061 1.7500 0.6746 -0.0639 0.0145  -0.2316 162 GLU B C   
4158 O O   . GLU B 147 ? 0.8134 1.7475 0.6826 -0.0834 0.0213  -0.2445 162 GLU B O   
4159 C CB  . GLU B 147 ? 0.8447 1.8302 0.6774 -0.0443 -0.0022 -0.2249 162 GLU B CB  
4160 C CG  . GLU B 147 ? 0.8890 1.9187 0.7053 -0.0417 -0.0172 -0.2279 162 GLU B CG  
4161 C CD  . GLU B 147 ? 0.9276 1.9494 0.7119 -0.0445 -0.0156 -0.2318 162 GLU B CD  
4162 O OE1 . GLU B 147 ? 0.9432 1.9300 0.7156 -0.0359 -0.0070 -0.2238 162 GLU B OE1 
4163 O OE2 . GLU B 147 ? 0.9551 2.0058 0.7256 -0.0565 -0.0226 -0.2431 162 GLU B OE2 
4164 N N   . GLU B 148 ? 0.8068 1.7226 0.6829 -0.0486 0.0190  -0.2190 163 GLU B N   
4165 C CA  . GLU B 148 ? 0.8400 1.7140 0.7284 -0.0528 0.0318  -0.2199 163 GLU B CA  
4166 C C   . GLU B 148 ? 0.8367 1.7049 0.7412 -0.0683 0.0334  -0.2271 163 GLU B C   
4167 O O   . GLU B 148 ? 0.8260 1.6631 0.7354 -0.0777 0.0433  -0.2339 163 GLU B O   
4168 C CB  . GLU B 148 ? 0.8577 1.7101 0.7574 -0.0345 0.0334  -0.2044 163 GLU B CB  
4169 C CG  . GLU B 148 ? 0.9303 1.7720 0.8128 -0.0228 0.0373  -0.1984 163 GLU B CG  
4170 C CD  . GLU B 148 ? 1.0059 1.8172 0.9013 -0.0112 0.0440  -0.1874 163 GLU B CD  
4171 O OE1 . GLU B 148 ? 1.0166 1.8055 0.9328 -0.0157 0.0506  -0.1895 163 GLU B OE1 
4172 O OE2 . GLU B 148 ? 1.1087 1.9176 0.9924 0.0023  0.0423  -0.1768 163 GLU B OE2 
4173 N N   . LEU B 149 ? 0.8605 1.7578 0.7722 -0.0710 0.0240  -0.2259 164 LEU B N   
4174 C CA  . LEU B 149 ? 0.8824 1.7718 0.8074 -0.0857 0.0254  -0.2303 164 LEU B CA  
4175 C C   . LEU B 149 ? 0.9284 1.8239 0.8435 -0.1100 0.0285  -0.2475 164 LEU B C   
4176 O O   . LEU B 149 ? 0.9129 1.7758 0.8308 -0.1230 0.0364  -0.2538 164 LEU B O   
4177 C CB  . LEU B 149 ? 0.8465 1.7631 0.7834 -0.0796 0.0160  -0.2224 164 LEU B CB  
4178 C CG  . LEU B 149 ? 0.7975 1.6956 0.7453 -0.0590 0.0151  -0.2060 164 LEU B CG  
4179 C CD1 . LEU B 149 ? 0.7632 1.6945 0.7167 -0.0468 0.0052  -0.1981 164 LEU B CD1 
4180 C CD2 . LEU B 149 ? 0.8050 1.6634 0.7657 -0.0644 0.0211  -0.2031 164 LEU B CD2 
4181 N N   . GLN B 150 ? 0.9568 1.8925 0.8599 -0.1161 0.0219  -0.2553 165 GLN B N   
4182 C CA  . GLN B 150 ? 1.0286 1.9720 0.9201 -0.1410 0.0247  -0.2726 165 GLN B CA  
4183 C C   . GLN B 150 ? 1.0624 1.9702 0.9397 -0.1474 0.0360  -0.2814 165 GLN B C   
4184 O O   . GLN B 150 ? 1.0805 1.9769 0.9493 -0.1686 0.0418  -0.2956 165 GLN B O   
4185 C CB  . GLN B 150 ? 1.0531 2.0519 0.9360 -0.1461 0.0136  -0.2795 165 GLN B CB  
4186 C CG  . GLN B 150 ? 1.0624 2.0778 0.9285 -0.1319 0.0081  -0.2768 165 GLN B CG  
4187 C CD  . GLN B 150 ? 1.0520 2.1256 0.9165 -0.1277 -0.0071 -0.2778 165 GLN B CD  
4188 O OE1 . GLN B 150 ? 0.9902 2.0952 0.8705 -0.1323 -0.0132 -0.2793 165 GLN B OE1 
4189 N NE2 . GLN B 150 ? 1.0674 2.1560 0.9126 -0.1183 -0.0137 -0.2770 165 GLN B NE2 
4190 N N   . ALA B 151 ? 1.0538 1.9431 0.9280 -0.1298 0.0400  -0.2735 166 ALA B N   
4191 C CA  . ALA B 151 ? 1.1005 1.9540 0.9647 -0.1335 0.0530  -0.2814 166 ALA B CA  
4192 C C   . ALA B 151 ? 1.1684 1.9767 1.0470 -0.1385 0.0631  -0.2839 166 ALA B C   
4193 O O   . ALA B 151 ? 1.2047 1.9850 1.0759 -0.1467 0.0742  -0.2953 166 ALA B O   
4194 C CB  . ALA B 151 ? 1.0536 1.9008 0.9116 -0.1142 0.0554  -0.2720 166 ALA B CB  
4195 N N   . CYS B 152 ? 1.2272 2.0275 1.1252 -0.1326 0.0592  -0.2734 167 CYS B N   
4196 C CA  . CYS B 152 ? 1.2672 2.0246 1.1781 -0.1360 0.0658  -0.2740 167 CYS B CA  
4197 C C   . CYS B 152 ? 1.3515 2.1101 1.2645 -0.1529 0.0613  -0.2769 167 CYS B C   
4198 O O   . CYS B 152 ? 1.4416 2.1742 1.3675 -0.1506 0.0608  -0.2698 167 CYS B O   
4199 C CB  . CYS B 152 ? 1.2473 1.9865 1.1776 -0.1148 0.0656  -0.2585 167 CYS B CB  
4200 S SG  . CYS B 152 ? 1.2927 2.0667 1.2311 -0.1005 0.0526  -0.2413 167 CYS B SG  
4201 N N   . ARG B 153 ? 1.4068 2.1959 1.3063 -0.1709 0.0578  -0.2874 168 ARG B N   
4202 C CA  . ARG B 153 ? 1.3870 2.1754 1.2854 -0.1918 0.0559  -0.2928 168 ARG B CA  
4203 C C   . ARG B 153 ? 1.3737 2.1111 1.2647 -0.2052 0.0660  -0.3032 168 ARG B C   
4204 O O   . ARG B 153 ? 1.3408 2.0597 1.2236 -0.2041 0.0741  -0.3118 168 ARG B O   
4205 C CB  . ARG B 153 ? 1.4139 2.2534 1.3020 -0.2081 0.0494  -0.3023 168 ARG B CB  
4206 C CG  . ARG B 153 ? 1.4749 2.3134 1.3431 -0.2336 0.0545  -0.3215 168 ARG B CG  
4207 C CD  . ARG B 153 ? 1.4891 2.3206 1.3532 -0.2602 0.0558  -0.3297 168 ARG B CD  
4208 N NE  . ARG B 153 ? 1.4757 2.3122 1.3195 -0.2866 0.0598  -0.3488 168 ARG B NE  
4209 C CZ  . ARG B 153 ? 1.4689 2.2586 1.2979 -0.3026 0.0697  -0.3601 168 ARG B CZ  
4210 N NH1 . ARG B 153 ? 1.4470 2.1802 1.2805 -0.2941 0.0764  -0.3544 168 ARG B NH1 
4211 N NH2 . ARG B 153 ? 1.4830 2.2821 1.2922 -0.3273 0.0726  -0.3778 168 ARG B NH2 
4212 N N   . GLY B 154 ? 1.3454 2.0576 1.2385 -0.2167 0.0659  -0.3019 169 GLY B N   
4213 C CA  . GLY B 154 ? 1.3350 1.9910 1.2225 -0.2249 0.0739  -0.3084 169 GLY B CA  
4214 C C   . GLY B 154 ? 1.2570 1.8748 1.1614 -0.2019 0.0761  -0.2977 169 GLY B C   
4215 O O   . GLY B 154 ? 1.2622 1.8331 1.1649 -0.2034 0.0824  -0.3029 169 GLY B O   
4216 N N   . GLN B 155 ? 1.1706 1.8084 1.0914 -0.1807 0.0707  -0.2833 170 GLN B N   
4217 C CA  . GLN B 155 ? 1.1324 1.7419 1.0716 -0.1586 0.0722  -0.2731 170 GLN B CA  
4218 C C   . GLN B 155 ? 1.0576 1.6668 1.0104 -0.1496 0.0632  -0.2565 170 GLN B C   
4219 O O   . GLN B 155 ? 1.0029 1.6492 0.9571 -0.1475 0.0565  -0.2491 170 GLN B O   
4220 C CB  . GLN B 155 ? 1.1354 1.7653 1.0803 -0.1409 0.0755  -0.2709 170 GLN B CB  
4221 C CG  . GLN B 155 ? 1.1611 1.7996 1.0896 -0.1487 0.0838  -0.2862 170 GLN B CG  
4222 C CD  . GLN B 155 ? 1.1708 1.7740 1.1050 -0.1406 0.0954  -0.2934 170 GLN B CD  
4223 O OE1 . GLN B 155 ? 1.1724 1.7363 1.1106 -0.1442 0.0995  -0.2986 170 GLN B OE1 
4224 N NE2 . GLN B 155 ? 1.1591 1.7755 1.0930 -0.1294 0.1011  -0.2940 170 GLN B NE2 
4225 N N   . SER B 156 ? 1.0294 1.5963 0.9921 -0.1434 0.0629  -0.2508 171 SER B N   
4226 C CA  . SER B 156 ? 0.9861 1.5468 0.9618 -0.1328 0.0545  -0.2347 171 SER B CA  
4227 C C   . SER B 156 ? 0.9362 1.5156 0.9289 -0.1098 0.0533  -0.2246 171 SER B C   
4228 O O   . SER B 156 ? 0.9973 1.5529 1.0056 -0.0950 0.0550  -0.2205 171 SER B O   
4229 C CB  . SER B 156 ? 0.9985 1.5063 0.9785 -0.1319 0.0533  -0.2321 171 SER B CB  
4230 O OG  . SER B 156 ? 1.0219 1.5054 0.9826 -0.1534 0.0561  -0.2427 171 SER B OG  
4231 N N   . SER B 157 ? 0.8621 1.4842 0.8517 -0.1069 0.0502  -0.2208 172 SER B N   
4232 C CA  . SER B 157 ? 0.7752 1.4139 0.7756 -0.0870 0.0494  -0.2116 172 SER B CA  
4233 C C   . SER B 157 ? 0.7624 1.3966 0.7760 -0.0749 0.0417  -0.1955 172 SER B C   
4234 O O   . SER B 157 ? 0.7648 1.3941 0.7767 -0.0824 0.0358  -0.1906 172 SER B O   
4235 C CB  . SER B 157 ? 0.7381 1.4206 0.7270 -0.0870 0.0484  -0.2140 172 SER B CB  
4236 O OG  . SER B 157 ? 0.6758 1.3704 0.6714 -0.0683 0.0471  -0.2036 172 SER B OG  
4237 N N   . ASP B 158 ? 0.7230 1.3586 0.7480 -0.0574 0.0427  -0.1878 173 ASP B N   
4238 C CA  . ASP B 158 ? 0.6414 1.2754 0.6777 -0.0450 0.0360  -0.1731 173 ASP B CA  
4239 C C   . ASP B 158 ? 0.5874 1.2560 0.6175 -0.0358 0.0343  -0.1677 173 ASP B C   
4240 O O   . ASP B 158 ? 0.5335 1.2075 0.5636 -0.0263 0.0393  -0.1679 173 ASP B O   
4241 C CB  . ASP B 158 ? 0.6409 1.2470 0.6957 -0.0328 0.0389  -0.1696 173 ASP B CB  
4242 C CG  . ASP B 158 ? 0.6124 1.2113 0.6795 -0.0221 0.0313  -0.1550 173 ASP B CG  
4243 O OD1 . ASP B 158 ? 0.5935 1.2134 0.6569 -0.0154 0.0280  -0.1467 173 ASP B OD1 
4244 O OD2 . ASP B 158 ? 0.6285 1.1990 0.7085 -0.0196 0.0283  -0.1520 173 ASP B OD2 
4245 N N   . LEU B 159 ? 0.5757 1.2676 0.5992 -0.0388 0.0277  -0.1636 174 LEU B N   
4246 C CA  . LEU B 159 ? 0.5579 1.2811 0.5753 -0.0278 0.0247  -0.1582 174 LEU B CA  
4247 C C   . LEU B 159 ? 0.5557 1.2651 0.5823 -0.0113 0.0239  -0.1460 174 LEU B C   
4248 O O   . LEU B 159 ? 0.6263 1.3069 0.6656 -0.0095 0.0255  -0.1430 174 LEU B O   
4249 C CB  . LEU B 159 ? 0.5623 1.3118 0.5750 -0.0330 0.0180  -0.1567 174 LEU B CB  
4250 C CG  . LEU B 159 ? 0.5644 1.3364 0.5675 -0.0502 0.0185  -0.1696 174 LEU B CG  
4251 C CD1 . LEU B 159 ? 0.5792 1.3700 0.5823 -0.0586 0.0135  -0.1686 174 LEU B CD1 
4252 C CD2 . LEU B 159 ? 0.5688 1.3723 0.5615 -0.0456 0.0185  -0.1749 174 LEU B CD2 
4253 N N   . SER B 160 ? 0.5191 1.2477 0.5395 0.0008  0.0212  -0.1389 175 SER B N   
4254 C CA  . SER B 160 ? 0.5016 1.2156 0.5285 0.0151  0.0207  -0.1271 175 SER B CA  
4255 C C   . SER B 160 ? 0.4876 1.1949 0.5116 0.0215  0.0281  -0.1283 175 SER B C   
4256 O O   . SER B 160 ? 0.4868 1.1983 0.5030 0.0327  0.0278  -0.1209 175 SER B O   
4257 C CB  . SER B 160 ? 0.5010 1.1857 0.5444 0.0139  0.0191  -0.1217 175 SER B CB  
4258 O OG  . SER B 160 ? 0.4879 1.1507 0.5422 0.0116  0.0254  -0.1272 175 SER B OG  
4259 N N   . VAL B 161 ? 0.4691 1.1640 0.4979 0.0139  0.0353  -0.1381 176 VAL B N   
4260 C CA  . VAL B 161 ? 0.5066 1.1990 0.5296 0.0173  0.0441  -0.1419 176 VAL B CA  
4261 C C   . VAL B 161 ? 0.5072 1.2262 0.5073 0.0187  0.0418  -0.1433 176 VAL B C   
4262 O O   . VAL B 161 ? 0.5723 1.2942 0.5605 0.0282  0.0430  -0.1371 176 VAL B O   
4263 C CB  . VAL B 161 ? 0.5428 1.2201 0.5730 0.0085  0.0534  -0.1548 176 VAL B CB  
4264 C CG1 . VAL B 161 ? 0.5313 1.2009 0.5617 0.0139  0.0640  -0.1564 176 VAL B CG1 
4265 C CG2 . VAL B 161 ? 0.5464 1.2001 0.5977 0.0053  0.0517  -0.1553 176 VAL B CG2 
4266 N N   . VAL B 162 ? 0.4837 1.2214 0.4767 0.0091  0.0380  -0.1511 177 VAL B N   
4267 C CA  . VAL B 162 ? 0.4781 1.2460 0.4512 0.0104  0.0332  -0.1531 177 VAL B CA  
4268 C C   . VAL B 162 ? 0.4619 1.2470 0.4304 0.0236  0.0238  -0.1417 177 VAL B C   
4269 O O   . VAL B 162 ? 0.4640 1.2639 0.4154 0.0326  0.0206  -0.1387 177 VAL B O   
4270 C CB  . VAL B 162 ? 0.4934 1.2806 0.4621 -0.0051 0.0311  -0.1657 177 VAL B CB  
4271 C CG1 . VAL B 162 ? 0.4985 1.2679 0.4670 -0.0178 0.0408  -0.1783 177 VAL B CG1 
4272 C CG2 . VAL B 162 ? 0.4964 1.2883 0.4773 -0.0116 0.0253  -0.1645 177 VAL B CG2 
4273 N N   . LEU B 163 ? 0.4628 1.2448 0.4446 0.0251  0.0191  -0.1357 178 LEU B N   
4274 C CA  . LEU B 163 ? 0.4528 1.2521 0.4307 0.0375  0.0107  -0.1266 178 LEU B CA  
4275 C C   . LEU B 163 ? 0.4735 1.2550 0.4466 0.0530  0.0115  -0.1145 178 LEU B C   
4276 O O   . LEU B 163 ? 0.4726 1.2670 0.4345 0.0660  0.0055  -0.1079 178 LEU B O   
4277 C CB  . LEU B 163 ? 0.4228 1.2253 0.4137 0.0326  0.0064  -0.1251 178 LEU B CB  
4278 C CG  . LEU B 163 ? 0.4123 1.2343 0.4061 0.0159  0.0052  -0.1363 178 LEU B CG  
4279 C CD1 . LEU B 163 ? 0.3960 1.2135 0.4002 0.0105  0.0025  -0.1331 178 LEU B CD1 
4280 C CD2 . LEU B 163 ? 0.4143 1.2770 0.3979 0.0176  -0.0001 -0.1422 178 LEU B CD2 
4281 N N   . MET B 164 ? 0.4702 1.2222 0.4519 0.0518  0.0186  -0.1119 179 MET B N   
4282 C CA  . MET B 164 ? 0.4950 1.2295 0.4706 0.0633  0.0210  -0.1019 179 MET B CA  
4283 C C   . MET B 164 ? 0.4921 1.2354 0.4437 0.0694  0.0220  -0.1020 179 MET B C   
4284 O O   . MET B 164 ? 0.4634 1.2104 0.3995 0.0822  0.0168  -0.0935 179 MET B O   
4285 C CB  . MET B 164 ? 0.5632 1.2705 0.5540 0.0588  0.0294  -0.1021 179 MET B CB  
4286 C CG  . MET B 164 ? 0.6195 1.3115 0.6294 0.0589  0.0261  -0.0961 179 MET B CG  
4287 S SD  . MET B 164 ? 0.7380 1.4227 0.7396 0.0727  0.0210  -0.0815 179 MET B SD  
4288 C CE  . MET B 164 ? 0.7860 1.4533 0.7781 0.0768  0.0306  -0.0784 179 MET B CE  
4289 N N   . ARG B 165 ? 0.5049 1.2497 0.4515 0.0603  0.0285  -0.1117 180 ARG B N   
4290 C CA  . ARG B 165 ? 0.5305 1.2824 0.4512 0.0633  0.0298  -0.1130 180 ARG B CA  
4291 C C   . ARG B 165 ? 0.4915 1.2694 0.3958 0.0737  0.0176  -0.1091 180 ARG B C   
4292 O O   . ARG B 165 ? 0.4607 1.2345 0.3435 0.0858  0.0146  -0.1008 180 ARG B O   
4293 C CB  . ARG B 165 ? 0.5989 1.3555 0.5174 0.0494  0.0366  -0.1269 180 ARG B CB  
4294 C CG  . ARG B 165 ? 0.6912 1.4547 0.5797 0.0506  0.0377  -0.1290 180 ARG B CG  
4295 C CD  . ARG B 165 ? 0.7541 1.5125 0.6388 0.0366  0.0486  -0.1424 180 ARG B CD  
4296 N NE  . ARG B 165 ? 0.8048 1.5390 0.7121 0.0311  0.0605  -0.1458 180 ARG B NE  
4297 C CZ  . ARG B 165 ? 0.8371 1.5673 0.7639 0.0204  0.0651  -0.1566 180 ARG B CZ  
4298 N NH1 . ARG B 165 ? 0.8274 1.5747 0.7520 0.0110  0.0603  -0.1659 180 ARG B NH1 
4299 N NH2 . ARG B 165 ? 0.8475 1.5558 0.7957 0.0188  0.0744  -0.1585 180 ARG B NH2 
4300 N N   . ALA B 166 ? 0.4633 1.2671 0.3781 0.0688  0.0107  -0.1154 181 ALA B N   
4301 C CA  . ALA B 166 ? 0.4413 1.2770 0.3476 0.0785  -0.0013 -0.1139 181 ALA B CA  
4302 C C   . ALA B 166 ? 0.4313 1.2599 0.3336 0.0967  -0.0069 -0.1009 181 ALA B C   
4303 O O   . ALA B 166 ? 0.4115 1.2457 0.2928 0.1106  -0.0131 -0.0952 181 ALA B O   
4304 C CB  . ALA B 166 ? 0.4171 1.2797 0.3405 0.0676  -0.0054 -0.1232 181 ALA B CB  
4305 N N   . VAL B 167 ? 0.4349 1.2481 0.3546 0.0969  -0.0049 -0.0959 182 VAL B N   
4306 C CA  . VAL B 167 ? 0.4478 1.2521 0.3618 0.1139  -0.0096 -0.0841 182 VAL B CA  
4307 C C   . VAL B 167 ? 0.4646 1.2387 0.3579 0.1219  -0.0051 -0.0751 182 VAL B C   
4308 O O   . VAL B 167 ? 0.4650 1.2384 0.3371 0.1374  -0.0110 -0.0678 182 VAL B O   
4309 C CB  . VAL B 167 ? 0.4256 1.2226 0.3593 0.1132  -0.0100 -0.0806 182 VAL B CB  
4310 C CG1 . VAL B 167 ? 0.4087 1.2263 0.3614 0.0987  -0.0108 -0.0903 182 VAL B CG1 
4311 C CG2 . VAL B 167 ? 0.4493 1.2093 0.3892 0.1100  -0.0027 -0.0741 182 VAL B CG2 
4312 N N   . THR B 168 ? 0.4703 1.2202 0.3682 0.1113  0.0054  -0.0763 183 THR B N   
4313 C CA  . THR B 168 ? 0.4934 1.2158 0.3715 0.1156  0.0116  -0.0691 183 THR B CA  
4314 C C   . THR B 168 ? 0.5370 1.2650 0.3824 0.1241  0.0075  -0.0669 183 THR B C   
4315 O O   . THR B 168 ? 0.5578 1.2661 0.3808 0.1355  0.0063  -0.0565 183 THR B O   
4316 C CB  . THR B 168 ? 0.4916 1.1965 0.3805 0.1016  0.0243  -0.0746 183 THR B CB  
4317 O OG1 . THR B 168 ? 0.4992 1.2045 0.4185 0.0930  0.0255  -0.0790 183 THR B OG1 
4318 C CG2 . THR B 168 ? 0.5084 1.1830 0.3862 0.1045  0.0318  -0.0661 183 THR B CG2 
4319 N N   . ASN B 169 ? 0.5577 1.3102 0.3985 0.1180  0.0049  -0.0765 184 ASN B N   
4320 C CA  . ASN B 169 ? 0.5769 1.3391 0.3859 0.1260  -0.0018 -0.0750 184 ASN B CA  
4321 C C   . ASN B 169 ? 0.5520 1.3250 0.3511 0.1462  -0.0153 -0.0664 184 ASN B C   
4322 O O   . ASN B 169 ? 0.5501 1.3037 0.3218 0.1594  -0.0184 -0.0561 184 ASN B O   
4323 C CB  . ASN B 169 ? 0.6079 1.4009 0.4178 0.1153  -0.0046 -0.0881 184 ASN B CB  
4324 C CG  . ASN B 169 ? 0.6908 1.4777 0.4682 0.1120  -0.0023 -0.0899 184 ASN B CG  
4325 O OD1 . ASN B 169 ? 0.7173 1.4759 0.4691 0.1168  0.0022  -0.0813 184 ASN B OD1 
4326 N ND2 . ASN B 169 ? 0.7204 1.5330 0.4971 0.1016  -0.0047 -0.1018 184 ASN B ND2 
4327 N N   . VAL B 170 ? 0.5311 1.3340 0.3523 0.1484  -0.0228 -0.0711 185 VAL B N   
4328 C CA  . VAL B 170 ? 0.5394 1.3594 0.3555 0.1684  -0.0356 -0.0656 185 VAL B CA  
4329 C C   . VAL B 170 ? 0.5599 1.3435 0.3592 0.1832  -0.0347 -0.0517 185 VAL B C   
4330 O O   . VAL B 170 ? 0.6061 1.3857 0.3803 0.2010  -0.0434 -0.0442 185 VAL B O   
4331 C CB  . VAL B 170 ? 0.5185 1.3691 0.3655 0.1662  -0.0393 -0.0723 185 VAL B CB  
4332 C CG1 . VAL B 170 ? 0.5185 1.3813 0.3633 0.1881  -0.0497 -0.0664 185 VAL B CG1 
4333 C CG2 . VAL B 170 ? 0.5198 1.4097 0.3780 0.1532  -0.0424 -0.0861 185 VAL B CG2 
4334 N N   . ILE B 171 ? 0.5634 1.3189 0.3751 0.1756  -0.0247 -0.0482 186 ILE B N   
4335 C CA  . ILE B 171 ? 0.5992 1.3182 0.3956 0.1863  -0.0226 -0.0358 186 ILE B CA  
4336 C C   . ILE B 171 ? 0.6350 1.3242 0.3962 0.1878  -0.0186 -0.0289 186 ILE B C   
4337 O O   . ILE B 171 ? 0.6369 1.3061 0.3706 0.2037  -0.0238 -0.0187 186 ILE B O   
4338 C CB  . ILE B 171 ? 0.5956 1.2938 0.4152 0.1750  -0.0130 -0.0349 186 ILE B CB  
4339 C CG1 . ILE B 171 ? 0.5778 1.3016 0.4275 0.1722  -0.0167 -0.0411 186 ILE B CG1 
4340 C CG2 . ILE B 171 ? 0.6221 1.2827 0.4253 0.1842  -0.0107 -0.0229 186 ILE B CG2 
4341 C CD1 . ILE B 171 ? 0.5812 1.3275 0.4274 0.1901  -0.0279 -0.0398 186 ILE B CD1 
4342 N N   . CYS B 172 ? 0.6320 1.3162 0.3930 0.1709  -0.0087 -0.0347 187 CYS B N   
4343 C CA  . CYS B 172 ? 0.6924 1.3521 0.4186 0.1693  -0.0037 -0.0301 187 CYS B CA  
4344 C C   . CYS B 172 ? 0.7366 1.4044 0.4293 0.1858  -0.0172 -0.0252 187 CYS B C   
4345 O O   . CYS B 172 ? 0.7423 1.3793 0.3983 0.1943  -0.0179 -0.0147 187 CYS B O   
4346 C CB  . CYS B 172 ? 0.6995 1.3656 0.4319 0.1497  0.0068  -0.0410 187 CYS B CB  
4347 S SG  . CYS B 172 ? 0.6649 1.3122 0.4275 0.1315  0.0242  -0.0456 187 CYS B SG  
4348 N N   . ARG B 173 ? 0.7375 1.4464 0.4421 0.1894  -0.0280 -0.0332 188 ARG B N   
4349 C CA  . ARG B 173 ? 0.7871 1.5116 0.4650 0.2052  -0.0429 -0.0303 188 ARG B CA  
4350 C C   . ARG B 173 ? 0.7567 1.4721 0.4269 0.2290  -0.0531 -0.0198 188 ARG B C   
4351 O O   . ARG B 173 ? 0.7752 1.4647 0.4089 0.2436  -0.0589 -0.0089 188 ARG B O   
4352 C CB  . ARG B 173 ? 0.8561 1.6309 0.5534 0.2006  -0.0512 -0.0433 188 ARG B CB  
4353 C CG  . ARG B 173 ? 0.9390 1.7184 0.6385 0.1776  -0.0411 -0.0540 188 ARG B CG  
4354 C CD  . ARG B 173 ? 1.0304 1.8562 0.7415 0.1713  -0.0494 -0.0669 188 ARG B CD  
4355 N NE  . ARG B 173 ? 1.2348 2.0550 0.9349 0.1516  -0.0398 -0.0753 188 ARG B NE  
4356 C CZ  . ARG B 173 ? 1.3783 2.2303 1.0837 0.1395  -0.0428 -0.0883 188 ARG B CZ  
4357 N NH1 . ARG B 173 ? 1.4414 2.3365 1.1649 0.1437  -0.0553 -0.0947 188 ARG B NH1 
4358 N NH2 . ARG B 173 ? 1.3896 2.2303 1.0821 0.1221  -0.0322 -0.0957 188 ARG B NH2 
4359 N N   . LEU B 174 ? 0.6965 1.4288 0.3994 0.2322  -0.0541 -0.0229 189 LEU B N   
4360 C CA  . LEU B 174 ? 0.6823 1.4095 0.3814 0.2550  -0.0629 -0.0152 189 LEU B CA  
4361 C C   . LEU B 174 ? 0.7037 1.3762 0.3729 0.2616  -0.0575 -0.0015 189 LEU B C   
4362 O O   . LEU B 174 ? 0.7127 1.3699 0.3613 0.2832  -0.0662 0.0073  189 LEU B O   
4363 C CB  . LEU B 174 ? 0.6395 1.3895 0.3782 0.2520  -0.0611 -0.0218 189 LEU B CB  
4364 C CG  . LEU B 174 ? 0.6495 1.4052 0.3924 0.2743  -0.0696 -0.0180 189 LEU B CG  
4365 C CD1 . LEU B 174 ? 0.6716 1.4630 0.4070 0.2949  -0.0860 -0.0203 189 LEU B CD1 
4366 C CD2 . LEU B 174 ? 0.6136 1.3892 0.3948 0.2640  -0.0642 -0.0258 189 LEU B CD2 
4367 N N   . VAL B 175 ? 0.7223 1.3652 0.3881 0.2428  -0.0430 -0.0002 190 VAL B N   
4368 C CA  . VAL B 175 ? 0.7791 1.3718 0.4217 0.2441  -0.0354 0.0111  190 VAL B CA  
4369 C C   . VAL B 175 ? 0.8423 1.4029 0.4394 0.2426  -0.0330 0.0185  190 VAL B C   
4370 O O   . VAL B 175 ? 0.8702 1.3968 0.4326 0.2573  -0.0375 0.0302  190 VAL B O   
4371 C CB  . VAL B 175 ? 0.7633 1.3441 0.4351 0.2245  -0.0207 0.0077  190 VAL B CB  
4372 C CG1 . VAL B 175 ? 0.7986 1.3291 0.4477 0.2223  -0.0118 0.0183  190 VAL B CG1 
4373 C CG2 . VAL B 175 ? 0.7177 1.3240 0.4268 0.2275  -0.0245 0.0025  190 VAL B CG2 
4374 N N   . PHE B 176 ? 0.8624 1.4311 0.4577 0.2245  -0.0254 0.0117  191 PHE B N   
4375 C CA  . PHE B 176 ? 0.9251 1.4647 0.4752 0.2198  -0.0215 0.0175  191 PHE B CA  
4376 C C   . PHE B 176 ? 0.9568 1.5200 0.4850 0.2280  -0.0349 0.0154  191 PHE B C   
4377 O O   . PHE B 176 ? 1.0262 1.5639 0.5099 0.2291  -0.0360 0.0223  191 PHE B O   
4378 C CB  . PHE B 176 ? 0.9384 1.4694 0.4940 0.1933  -0.0029 0.0103  191 PHE B CB  
4379 C CG  . PHE B 176 ? 0.9051 1.4413 0.5048 0.1786  0.0096  0.0033  191 PHE B CG  
4380 C CD1 . PHE B 176 ? 0.9059 1.4243 0.5184 0.1835  0.0111  0.0093  191 PHE B CD1 
4381 C CD2 . PHE B 176 ? 0.8837 1.4396 0.5094 0.1595  0.0201  -0.0095 191 PHE B CD2 
4382 C CE1 . PHE B 176 ? 0.8928 1.4158 0.5447 0.1698  0.0211  0.0032  191 PHE B CE1 
4383 C CE2 . PHE B 176 ? 0.8481 1.4073 0.5136 0.1473  0.0303  -0.0156 191 PHE B CE2 
4384 C CZ  . PHE B 176 ? 0.8455 1.3888 0.5241 0.1524  0.0303  -0.0089 191 PHE B CZ  
4385 N N   . SER B 177 ? 0.9404 1.5523 0.4988 0.2310  -0.0443 0.0052  192 SER B N   
4386 C CA  . SER B 177 ? 0.9528 1.5948 0.5001 0.2294  -0.0532 -0.0015 192 SER B CA  
4387 C C   . SER B 177 ? 0.9518 1.5844 0.4927 0.2036  -0.0372 -0.0089 192 SER B C   
4388 O O   . SER B 177 ? 1.0107 1.6282 0.5121 0.2000  -0.0373 -0.0062 192 SER B O   
4389 C CB  . SER B 177 ? 1.0153 1.6476 0.5185 0.2517  -0.0706 0.0091  192 SER B CB  
4390 O OG  . SER B 177 ? 1.1136 1.7827 0.6112 0.2512  -0.0820 0.0015  192 SER B OG  
4391 N N   . SER B 178 ? 0.9026 1.5435 0.4824 0.1863  -0.0233 -0.0183 193 SER B N   
4392 C CA  . SER B 178 ? 0.8973 1.5407 0.4836 0.1628  -0.0087 -0.0295 193 SER B CA  
4393 C C   . SER B 178 ? 0.9071 1.5863 0.4892 0.1594  -0.0177 -0.0396 193 SER B C   
4394 O O   . SER B 178 ? 0.8978 1.6079 0.4839 0.1731  -0.0346 -0.0401 193 SER B O   
4395 C CB  . SER B 178 ? 0.8388 1.4911 0.4731 0.1490  0.0035  -0.0387 193 SER B CB  
4396 O OG  . SER B 178 ? 0.7770 1.4709 0.4418 0.1458  -0.0032 -0.0503 193 SER B OG  
4397 N N   . SER B 179 ? 0.9440 1.6200 0.5190 0.1403  -0.0055 -0.0487 194 SER B N   
4398 C CA  . SER B 179 ? 0.9632 1.6691 0.5308 0.1335  -0.0120 -0.0593 194 SER B CA  
4399 C C   . SER B 179 ? 0.9569 1.6748 0.5567 0.1117  0.0029  -0.0753 194 SER B C   
4400 O O   . SER B 179 ? 0.9749 1.7090 0.5669 0.0997  0.0039  -0.0865 194 SER B O   
4401 C CB  . SER B 179 ? 1.0108 1.6939 0.5242 0.1322  -0.0125 -0.0538 194 SER B CB  
4402 O OG  . SER B 179 ? 1.0231 1.7327 0.5158 0.1426  -0.0323 -0.0538 194 SER B OG  
4403 N N   . TYR B 180 ? 0.9533 1.6628 0.5890 0.1071  0.0137  -0.0767 195 TYR B N   
4404 C CA  . TYR B 180 ? 0.9591 1.6664 0.6194 0.0875  0.0307  -0.0898 195 TYR B CA  
4405 C C   . TYR B 180 ? 0.9946 1.7362 0.6738 0.0780  0.0266  -0.1045 195 TYR B C   
4406 O O   . TYR B 180 ? 0.9948 1.7654 0.6859 0.0859  0.0119  -0.1049 195 TYR B O   
4407 C CB  . TYR B 180 ? 0.8942 1.5885 0.5913 0.0863  0.0398  -0.0880 195 TYR B CB  
4408 C CG  . TYR B 180 ? 0.8885 1.5490 0.5731 0.0925  0.0458  -0.0751 195 TYR B CG  
4409 C CD1 . TYR B 180 ? 0.9101 1.5437 0.5585 0.0877  0.0553  -0.0711 195 TYR B CD1 
4410 C CD2 . TYR B 180 ? 0.8607 1.5148 0.5689 0.1009  0.0430  -0.0675 195 TYR B CD2 
4411 C CE1 . TYR B 180 ? 0.9281 1.5295 0.5639 0.0910  0.0617  -0.0597 195 TYR B CE1 
4412 C CE2 . TYR B 180 ? 0.8715 1.4940 0.5680 0.1049  0.0487  -0.0564 195 TYR B CE2 
4413 C CZ  . TYR B 180 ? 0.9234 1.5196 0.5840 0.0995  0.0582  -0.0526 195 TYR B CZ  
4414 O OH  . TYR B 180 ? 0.9451 1.5086 0.5926 0.1012  0.0647  -0.0420 195 TYR B OH  
4415 N N   . GLN B 181 ? 1.0405 1.7779 0.7219 0.0604  0.0405  -0.1174 196 GLN B N   
4416 C CA  . GLN B 181 ? 1.0580 1.8194 0.7628 0.0480  0.0410  -0.1328 196 GLN B CA  
4417 C C   . GLN B 181 ? 1.0478 1.7923 0.7853 0.0378  0.0576  -0.1398 196 GLN B C   
4418 O O   . GLN B 181 ? 1.0968 1.8150 0.8310 0.0364  0.0706  -0.1365 196 GLN B O   
4419 C CB  . GLN B 181 ? 1.1157 1.8867 0.7916 0.0366  0.0417  -0.1434 196 GLN B CB  
4420 C CG  . GLN B 181 ? 1.1131 1.9216 0.7973 0.0326  0.0285  -0.1529 196 GLN B CG  
4421 C CD  . GLN B 181 ? 1.1454 1.9716 0.7919 0.0357  0.0149  -0.1520 196 GLN B CD  
4422 O OE1 . GLN B 181 ? 1.1520 1.9705 0.7720 0.0505  0.0060  -0.1386 196 GLN B OE1 
4423 N NE2 . GLN B 181 ? 1.1875 2.0363 0.8299 0.0218  0.0125  -0.1663 196 GLN B NE2 
4424 N N   . PRO B 182 ? 1.0275 1.7866 0.7962 0.0306  0.0569  -0.1496 197 PRO B N   
4425 C CA  . PRO B 182 ? 0.9859 1.7282 0.7880 0.0247  0.0693  -0.1541 197 PRO B CA  
4426 C C   . PRO B 182 ? 1.0180 1.7351 0.8152 0.0176  0.0879  -0.1587 197 PRO B C   
4427 O O   . PRO B 182 ? 1.1344 1.8343 0.9529 0.0200  0.0960  -0.1550 197 PRO B O   
4428 C CB  . PRO B 182 ? 0.9799 1.7382 0.7998 0.0129  0.0681  -0.1681 197 PRO B CB  
4429 C CG  . PRO B 182 ? 0.9829 1.7717 0.7927 0.0174  0.0508  -0.1656 197 PRO B CG  
4430 C CD  . PRO B 182 ? 1.0227 1.8132 0.7956 0.0256  0.0456  -0.1581 197 PRO B CD  
4431 N N   . SER B 183 ? 1.0203 1.7363 0.7896 0.0087  0.0949  -0.1670 198 SER B N   
4432 C CA  . SER B 183 ? 0.9853 1.6794 0.7491 0.0006  0.1146  -0.1732 198 SER B CA  
4433 C C   . SER B 183 ? 0.9347 1.6084 0.6905 0.0078  0.1202  -0.1601 198 SER B C   
4434 O O   . SER B 183 ? 0.9451 1.6032 0.7160 0.0027  0.1364  -0.1645 198 SER B O   
4435 C CB  . SER B 183 ? 1.0109 1.7071 0.7386 -0.0105 0.1201  -0.1834 198 SER B CB  
4436 O OG  . SER B 183 ? 1.0420 1.7457 0.7315 -0.0037 0.1064  -0.1730 198 SER B OG  
4437 N N   . ASP B 184 ? 0.8863 1.5599 0.6182 0.0194  0.1073  -0.1449 199 ASP B N   
4438 C CA  . ASP B 184 ? 0.8723 1.5227 0.5879 0.0249  0.1123  -0.1321 199 ASP B CA  
4439 C C   . ASP B 184 ? 0.8529 1.4910 0.6062 0.0250  0.1220  -0.1308 199 ASP B C   
4440 O O   . ASP B 184 ? 0.8293 1.4761 0.6152 0.0310  0.1138  -0.1286 199 ASP B O   
4441 C CB  . ASP B 184 ? 0.8703 1.5219 0.5614 0.0406  0.0940  -0.1155 199 ASP B CB  
4442 C CG  . ASP B 184 ? 0.9074 1.5601 0.5490 0.0414  0.0870  -0.1130 199 ASP B CG  
4443 O OD1 . ASP B 184 ? 0.9264 1.5870 0.5556 0.0295  0.0925  -0.1253 199 ASP B OD1 
4444 O OD2 . ASP B 184 ? 0.8976 1.5419 0.5110 0.0544  0.0754  -0.0987 199 ASP B OD2 
4445 N N   . PRO B 185 ? 0.8570 1.4762 0.6063 0.0171  0.1399  -0.1329 200 PRO B N   
4446 C CA  . PRO B 185 ? 0.8187 1.4275 0.6014 0.0175  0.1482  -0.1306 200 PRO B CA  
4447 C C   . PRO B 185 ? 0.7742 1.3730 0.5541 0.0292  0.1372  -0.1134 200 PRO B C   
4448 O O   . PRO B 185 ? 0.7372 1.3353 0.5515 0.0320  0.1366  -0.1113 200 PRO B O   
4449 C CB  . PRO B 185 ? 0.8526 1.4460 0.6222 0.0052  0.1698  -0.1369 200 PRO B CB  
4450 C CG  . PRO B 185 ? 0.8716 1.4715 0.6187 -0.0039 0.1757  -0.1494 200 PRO B CG  
4451 C CD  . PRO B 185 ? 0.8949 1.5053 0.6145 0.0045  0.1554  -0.1418 200 PRO B CD  
4452 N N   . GLU B 186 ? 0.7752 1.3647 0.5136 0.0361  0.1287  -0.1013 201 GLU B N   
4453 C CA  . GLU B 186 ? 0.7853 1.3640 0.5186 0.0488  0.1173  -0.0854 201 GLU B CA  
4454 C C   . GLU B 186 ? 0.7765 1.3752 0.5406 0.0592  0.1014  -0.0839 201 GLU B C   
4455 O O   . GLU B 186 ? 0.7218 1.3142 0.5059 0.0651  0.0976  -0.0767 201 GLU B O   
4456 C CB  . GLU B 186 ? 0.8225 1.3860 0.5033 0.0567  0.1093  -0.0730 201 GLU B CB  
4457 C CG  . GLU B 186 ? 0.8630 1.3938 0.5140 0.0500  0.1227  -0.0660 201 GLU B CG  
4458 C CD  . GLU B 186 ? 0.8961 1.4035 0.4973 0.0615  0.1119  -0.0496 201 GLU B CD  
4459 O OE1 . GLU B 186 ? 0.8711 1.3886 0.4657 0.0781  0.0928  -0.0423 201 GLU B OE1 
4460 O OE2 . GLU B 186 ? 0.9171 1.3948 0.4851 0.0539  0.1231  -0.0441 201 GLU B OE2 
4461 N N   . LEU B 187 ? 0.7731 1.3955 0.5403 0.0598  0.0929  -0.0914 202 LEU B N   
4462 C CA  . LEU B 187 ? 0.7567 1.3990 0.5542 0.0656  0.0807  -0.0924 202 LEU B CA  
4463 C C   . LEU B 187 ? 0.7099 1.3499 0.5505 0.0588  0.0886  -0.0989 202 LEU B C   
4464 O O   . LEU B 187 ? 0.6370 1.2775 0.4998 0.0646  0.0816  -0.0934 202 LEU B O   
4465 C CB  . LEU B 187 ? 0.7731 1.4418 0.5663 0.0635  0.0724  -0.1015 202 LEU B CB  
4466 C CG  . LEU B 187 ? 0.7382 1.4282 0.5612 0.0665  0.0613  -0.1039 202 LEU B CG  
4467 C CD1 . LEU B 187 ? 0.7212 1.4167 0.5383 0.0821  0.0468  -0.0913 202 LEU B CD1 
4468 C CD2 . LEU B 187 ? 0.7481 1.4623 0.5704 0.0584  0.0578  -0.1165 202 LEU B CD2 
4469 N N   . GLN B 188 ? 0.7290 1.3660 0.5802 0.0471  0.1029  -0.1108 203 GLN B N   
4470 C CA  . GLN B 188 ? 0.7183 1.3531 0.6103 0.0422  0.1098  -0.1176 203 GLN B CA  
4471 C C   . GLN B 188 ? 0.6713 1.2904 0.5767 0.0456  0.1126  -0.1084 203 GLN B C   
4472 O O   . GLN B 188 ? 0.6424 1.2617 0.5812 0.0467  0.1099  -0.1085 203 GLN B O   
4473 C CB  . GLN B 188 ? 0.7962 1.4298 0.6951 0.0306  0.1261  -0.1329 203 GLN B CB  
4474 C CG  . GLN B 188 ? 0.8401 1.4750 0.7824 0.0276  0.1301  -0.1424 203 GLN B CG  
4475 C CD  . GLN B 188 ? 0.8489 1.4958 0.8034 0.0290  0.1173  -0.1452 203 GLN B CD  
4476 O OE1 . GLN B 188 ? 0.8117 1.4694 0.7490 0.0248  0.1148  -0.1518 203 GLN B OE1 
4477 N NE2 . GLN B 188 ? 0.8495 1.4945 0.8320 0.0337  0.1091  -0.1401 203 GLN B NE2 
4478 N N   . THR B 189 ? 0.6621 1.2663 0.5392 0.0463  0.1177  -0.1003 204 THR B N   
4479 C CA  . THR B 189 ? 0.6597 1.2470 0.5444 0.0466  0.1224  -0.0923 204 THR B CA  
4480 C C   . THR B 189 ? 0.6264 1.2104 0.5127 0.0579  0.1073  -0.0794 204 THR B C   
4481 O O   . THR B 189 ? 0.5891 1.1659 0.4981 0.0583  0.1070  -0.0753 204 THR B O   
4482 C CB  . THR B 189 ? 0.7114 1.2799 0.5577 0.0421  0.1330  -0.0875 204 THR B CB  
4483 O OG1 . THR B 189 ? 0.7529 1.3251 0.5882 0.0317  0.1462  -0.0994 204 THR B OG1 
4484 C CG2 . THR B 189 ? 0.7135 1.2658 0.5712 0.0374  0.1422  -0.0830 204 THR B CG2 
4485 N N   . VAL B 190 ? 0.6377 1.2281 0.4991 0.0672  0.0948  -0.0734 205 VAL B N   
4486 C CA  . VAL B 190 ? 0.5947 1.1866 0.4578 0.0791  0.0802  -0.0634 205 VAL B CA  
4487 C C   . VAL B 190 ? 0.5567 1.1612 0.4604 0.0765  0.0763  -0.0692 205 VAL B C   
4488 O O   . VAL B 190 ? 0.5642 1.1599 0.4864 0.0779  0.0743  -0.0641 205 VAL B O   
4489 C CB  . VAL B 190 ? 0.6045 1.2091 0.4404 0.0897  0.0674  -0.0598 205 VAL B CB  
4490 C CG1 . VAL B 190 ? 0.5928 1.2036 0.4369 0.1015  0.0538  -0.0524 205 VAL B CG1 
4491 C CG2 . VAL B 190 ? 0.6402 1.2278 0.4318 0.0941  0.0690  -0.0521 205 VAL B CG2 
4492 N N   . ILE B 191 ? 0.5315 1.1539 0.4475 0.0716  0.0758  -0.0801 206 ILE B N   
4493 C CA  . ILE B 191 ? 0.5271 1.1572 0.4784 0.0684  0.0720  -0.0854 206 ILE B CA  
4494 C C   . ILE B 191 ? 0.5310 1.1484 0.5116 0.0634  0.0798  -0.0872 206 ILE B C   
4495 O O   . ILE B 191 ? 0.4994 1.1146 0.5023 0.0650  0.0731  -0.0841 206 ILE B O   
4496 C CB  . ILE B 191 ? 0.5283 1.1749 0.4868 0.0617  0.0721  -0.0981 206 ILE B CB  
4497 C CG1 . ILE B 191 ? 0.5225 1.1886 0.4678 0.0662  0.0594  -0.0967 206 ILE B CG1 
4498 C CG2 . ILE B 191 ? 0.5085 1.1529 0.5027 0.0562  0.0727  -0.1046 206 ILE B CG2 
4499 C CD1 . ILE B 191 ? 0.5356 1.2104 0.4463 0.0706  0.0571  -0.0951 206 ILE B CD1 
4500 N N   . GLN B 192 ? 0.5809 1.1911 0.5615 0.0570  0.0937  -0.0926 207 GLN B N   
4501 C CA  . GLN B 192 ? 0.6103 1.2148 0.6243 0.0523  0.1010  -0.0972 207 GLN B CA  
4502 C C   . GLN B 192 ? 0.5939 1.1866 0.6143 0.0552  0.0977  -0.0864 207 GLN B C   
4503 O O   . GLN B 192 ? 0.5674 1.1592 0.6192 0.0546  0.0948  -0.0871 207 GLN B O   
4504 C CB  . GLN B 192 ? 0.7093 1.3129 0.7250 0.0440  0.1185  -0.1080 207 GLN B CB  
4505 C CG  . GLN B 192 ? 0.7964 1.4099 0.8248 0.0395  0.1232  -0.1226 207 GLN B CG  
4506 C CD  . GLN B 192 ? 0.8654 1.4820 0.9278 0.0418  0.1142  -0.1259 207 GLN B CD  
4507 O OE1 . GLN B 192 ? 0.8296 1.4505 0.8876 0.0448  0.1015  -0.1223 207 GLN B OE1 
4508 N NE2 . GLN B 192 ? 0.9429 1.5573 1.0392 0.0402  0.1207  -0.1331 207 GLN B NE2 
4509 N N   . TYR B 193 ? 0.5942 1.1763 0.5835 0.0586  0.0971  -0.0763 208 TYR B N   
4510 C CA  . TYR B 193 ? 0.5862 1.1541 0.5780 0.0600  0.0950  -0.0666 208 TYR B CA  
4511 C C   . TYR B 193 ? 0.5628 1.1284 0.5505 0.0690  0.0797  -0.0566 208 TYR B C   
4512 O O   . TYR B 193 ? 0.5698 1.1262 0.5704 0.0688  0.0763  -0.0511 208 TYR B O   
4513 C CB  . TYR B 193 ? 0.6268 1.1786 0.5892 0.0562  0.1058  -0.0621 208 TYR B CB  
4514 C CG  . TYR B 193 ? 0.6487 1.2033 0.6274 0.0446  0.1226  -0.0729 208 TYR B CG  
4515 C CD1 . TYR B 193 ? 0.6376 1.1940 0.6520 0.0390  0.1270  -0.0766 208 TYR B CD1 
4516 C CD2 . TYR B 193 ? 0.6820 1.2398 0.6422 0.0394  0.1338  -0.0808 208 TYR B CD2 
4517 C CE1 . TYR B 193 ? 0.6421 1.2052 0.6758 0.0293  0.1428  -0.0881 208 TYR B CE1 
4518 C CE2 . TYR B 193 ? 0.6818 1.2439 0.6585 0.0286  0.1507  -0.0924 208 TYR B CE2 
4519 C CZ  . TYR B 193 ? 0.6678 1.2336 0.6829 0.0242  0.1553  -0.0963 208 TYR B CZ  
4520 O OH  . TYR B 193 ? 0.6900 1.2634 0.7253 0.0144  0.1725  -0.1089 208 TYR B OH  
4521 N N   . ASN B 194 ? 0.5541 1.1298 0.5257 0.0760  0.0709  -0.0554 209 ASN B N   
4522 C CA  . ASN B 194 ? 0.5296 1.1091 0.5048 0.0833  0.0573  -0.0495 209 ASN B CA  
4523 C C   . ASN B 194 ? 0.5055 1.0905 0.5167 0.0781  0.0538  -0.0546 209 ASN B C   
4524 O O   . ASN B 194 ? 0.4909 1.0678 0.5145 0.0788  0.0480  -0.0491 209 ASN B O   
4525 C CB  . ASN B 194 ? 0.5347 1.1312 0.4934 0.0899  0.0495  -0.0507 209 ASN B CB  
4526 C CG  . ASN B 194 ? 0.5485 1.1400 0.4703 0.0994  0.0477  -0.0435 209 ASN B CG  
4527 O OD1 . ASN B 194 ? 0.5234 1.0937 0.4280 0.1020  0.0510  -0.0355 209 ASN B OD1 
4528 N ND2 . ASN B 194 ? 0.5370 1.1474 0.4455 0.1047  0.0415  -0.0463 209 ASN B ND2 
4529 N N   . ASP B 195 ? 0.4931 1.0894 0.5191 0.0728  0.0572  -0.0651 210 ASP B N   
4530 C CA  . ASP B 195 ? 0.4966 1.0942 0.5546 0.0685  0.0540  -0.0702 210 ASP B CA  
4531 C C   . ASP B 195 ? 0.5236 1.1102 0.6058 0.0655  0.0576  -0.0692 210 ASP B C   
4532 O O   . ASP B 195 ? 0.5378 1.1203 0.6409 0.0653  0.0495  -0.0669 210 ASP B O   
4533 C CB  . ASP B 195 ? 0.5001 1.1074 0.5671 0.0633  0.0588  -0.0825 210 ASP B CB  
4534 C CG  . ASP B 195 ? 0.5239 1.1281 0.6208 0.0603  0.0541  -0.0870 210 ASP B CG  
4535 O OD1 . ASP B 195 ? 0.5591 1.1656 0.6551 0.0602  0.0441  -0.0851 210 ASP B OD1 
4536 O OD2 . ASP B 195 ? 0.4775 1.0766 0.5983 0.0582  0.0600  -0.0922 210 ASP B OD2 
4537 N N   . GLY B 196 ? 0.5217 1.1046 0.6011 0.0624  0.0696  -0.0713 211 GLY B N   
4538 C CA  . GLY B 196 ? 0.4954 1.0715 0.5965 0.0588  0.0733  -0.0704 211 GLY B CA  
4539 C C   . GLY B 196 ? 0.5019 1.0671 0.5978 0.0618  0.0629  -0.0586 211 GLY B C   
4540 O O   . GLY B 196 ? 0.4775 1.0408 0.5977 0.0611  0.0551  -0.0571 211 GLY B O   
4541 N N   . ILE B 197 ? 0.4953 1.0522 0.5581 0.0658  0.0621  -0.0502 212 ILE B N   
4542 C CA  . ILE B 197 ? 0.4848 1.0291 0.5392 0.0689  0.0536  -0.0398 212 ILE B CA  
4543 C C   . ILE B 197 ? 0.5136 1.0624 0.5852 0.0709  0.0407  -0.0389 212 ILE B C   
4544 O O   . ILE B 197 ? 0.5737 1.1153 0.6605 0.0686  0.0347  -0.0352 212 ILE B O   
4545 C CB  . ILE B 197 ? 0.4699 1.0058 0.4856 0.0764  0.0522  -0.0320 212 ILE B CB  
4546 C CG1 . ILE B 197 ? 0.4813 1.0045 0.4751 0.0732  0.0640  -0.0303 212 ILE B CG1 
4547 C CG2 . ILE B 197 ? 0.4519 0.9762 0.4600 0.0811  0.0421  -0.0229 212 ILE B CG2 
4548 C CD1 . ILE B 197 ? 0.4982 1.0164 0.4528 0.0814  0.0639  -0.0257 212 ILE B CD1 
4549 N N   . VAL B 198 ? 0.5216 1.0818 0.5893 0.0738  0.0365  -0.0424 213 VAL B N   
4550 C CA  . VAL B 198 ? 0.5034 1.0665 0.5825 0.0739  0.0253  -0.0417 213 VAL B CA  
4551 C C   . VAL B 198 ? 0.5134 1.0731 0.6251 0.0688  0.0221  -0.0449 213 VAL B C   
4552 O O   . VAL B 198 ? 0.4708 1.0212 0.5905 0.0678  0.0145  -0.0391 213 VAL B O   
4553 C CB  . VAL B 198 ? 0.4836 1.0615 0.5547 0.0750  0.0236  -0.0472 213 VAL B CB  
4554 C CG1 . VAL B 198 ? 0.4752 1.0544 0.5634 0.0707  0.0152  -0.0499 213 VAL B CG1 
4555 C CG2 . VAL B 198 ? 0.4813 1.0644 0.5240 0.0822  0.0206  -0.0421 213 VAL B CG2 
4556 N N   . GLN B 199 ? 0.5741 1.1408 0.7037 0.0661  0.0277  -0.0545 214 GLN B N   
4557 C CA  . GLN B 199 ? 0.6206 1.1849 0.7819 0.0637  0.0232  -0.0587 214 GLN B CA  
4558 C C   . GLN B 199 ? 0.6303 1.1874 0.8065 0.0627  0.0202  -0.0535 214 GLN B C   
4559 O O   . GLN B 199 ? 0.6697 1.2195 0.8573 0.0624  0.0085  -0.0489 214 GLN B O   
4560 C CB  . GLN B 199 ? 0.6981 1.2700 0.8764 0.0622  0.0334  -0.0709 214 GLN B CB  
4561 C CG  . GLN B 199 ? 0.8017 1.3698 1.0091 0.0623  0.0269  -0.0763 214 GLN B CG  
4562 C CD  . GLN B 199 ? 0.8320 1.4040 1.0724 0.0631  0.0335  -0.0842 214 GLN B CD  
4563 O OE1 . GLN B 199 ? 0.7762 1.3450 1.0393 0.0644  0.0260  -0.0811 214 GLN B OE1 
4564 N NE2 . GLN B 199 ? 0.8640 1.4443 1.1075 0.0620  0.0475  -0.0951 214 GLN B NE2 
4565 N N   . THR B 200 ? 0.6411 1.1995 0.8141 0.0611  0.0306  -0.0539 215 THR B N   
4566 C CA  . THR B 200 ? 0.6251 1.1778 0.8087 0.0581  0.0292  -0.0493 215 THR B CA  
4567 C C   . THR B 200 ? 0.5944 1.1354 0.7670 0.0591  0.0155  -0.0390 215 THR B C   
4568 O O   . THR B 200 ? 0.5971 1.1350 0.7897 0.0578  0.0051  -0.0374 215 THR B O   
4569 C CB  . THR B 200 ? 0.6597 1.2102 0.8255 0.0548  0.0426  -0.0486 215 THR B CB  
4570 O OG1 . THR B 200 ? 0.6716 1.2331 0.8487 0.0522  0.0562  -0.0592 215 THR B OG1 
4571 C CG2 . THR B 200 ? 0.6730 1.2168 0.8475 0.0493  0.0418  -0.0442 215 THR B CG2 
4572 N N   . ILE B 201 ? 0.6226 1.1572 0.7630 0.0619  0.0151  -0.0326 216 ILE B N   
4573 C CA  . ILE B 201 ? 0.6358 1.1588 0.7633 0.0627  0.0042  -0.0237 216 ILE B CA  
4574 C C   . ILE B 201 ? 0.6697 1.1925 0.8113 0.0620  -0.0083 -0.0237 216 ILE B C   
4575 O O   . ILE B 201 ? 0.7122 1.2250 0.8543 0.0598  -0.0184 -0.0178 216 ILE B O   
4576 C CB  . ILE B 201 ? 0.6096 1.1291 0.7020 0.0686  0.0053  -0.0189 216 ILE B CB  
4577 C CG1 . ILE B 201 ? 0.5942 1.1067 0.6655 0.0701  0.0157  -0.0166 216 ILE B CG1 
4578 C CG2 . ILE B 201 ? 0.6227 1.1311 0.7035 0.0693  -0.0049 -0.0115 216 ILE B CG2 
4579 C CD1 . ILE B 201 ? 0.5744 1.0847 0.6126 0.0787  0.0162  -0.0126 216 ILE B CD1 
4580 N N   . ALA B 202 ? 0.6960 1.2277 0.8461 0.0629  -0.0077 -0.0302 217 ALA B N   
4581 C CA  . ALA B 202 ? 0.7175 1.2451 0.8742 0.0613  -0.0188 -0.0298 217 ALA B CA  
4582 C C   . ALA B 202 ? 0.7208 1.2385 0.8986 0.0587  -0.0299 -0.0264 217 ALA B C   
4583 O O   . ALA B 202 ? 0.6759 1.1832 0.8477 0.0564  -0.0413 -0.0211 217 ALA B O   
4584 C CB  . ALA B 202 ? 0.6897 1.2250 0.8555 0.0612  -0.0154 -0.0386 217 ALA B CB  
4585 N N   . ARG B 203 ? 0.7192 1.2412 0.9212 0.0586  -0.0265 -0.0298 218 ARG B N   
4586 C CA  . ARG B 203 ? 0.7429 1.2596 0.9688 0.0570  -0.0377 -0.0274 218 ARG B CA  
4587 C C   . ARG B 203 ? 0.7225 1.2337 0.9410 0.0531  -0.0398 -0.0207 218 ARG B C   
4588 O O   . ARG B 203 ? 0.6651 1.1827 0.9032 0.0508  -0.0366 -0.0231 218 ARG B O   
4589 C CB  . ARG B 203 ? 0.7667 1.2946 1.0280 0.0593  -0.0337 -0.0367 218 ARG B CB  
4590 C CG  . ARG B 203 ? 0.8158 1.3439 1.0831 0.0628  -0.0332 -0.0435 218 ARG B CG  
4591 C CD  . ARG B 203 ? 0.8896 1.4313 1.1843 0.0658  -0.0221 -0.0551 218 ARG B CD  
4592 N NE  . ARG B 203 ? 0.9412 1.4927 1.2195 0.0639  -0.0049 -0.0594 218 ARG B NE  
4593 C CZ  . ARG B 203 ? 1.0384 1.6025 1.3312 0.0629  0.0086  -0.0668 218 ARG B CZ  
4594 N NH1 . ARG B 203 ? 1.0538 1.6266 1.3823 0.0638  0.0079  -0.0720 218 ARG B NH1 
4595 N NH2 . ARG B 203 ? 1.0638 1.6325 1.3345 0.0606  0.0229  -0.0692 218 ARG B NH2 
4596 N N   . GLY B 204 ? 0.7538 1.2532 0.9438 0.0518  -0.0447 -0.0130 219 GLY B N   
4597 C CA  . GLY B 204 ? 0.7579 1.2475 0.9348 0.0478  -0.0471 -0.0064 219 GLY B CA  
4598 C C   . GLY B 204 ? 0.7719 1.2603 0.9247 0.0491  -0.0338 -0.0056 219 GLY B C   
4599 O O   . GLY B 204 ? 0.8298 1.3268 0.9775 0.0529  -0.0230 -0.0101 219 GLY B O   
4600 N N   . GLY B 205 ? 0.7465 1.2217 0.8821 0.0457  -0.0350 0.0003  220 GLY B N   
4601 C CA  . GLY B 205 ? 0.7293 1.1972 0.8377 0.0476  -0.0237 0.0023  220 GLY B CA  
4602 C C   . GLY B 205 ? 0.7007 1.1695 0.7831 0.0561  -0.0200 0.0030  220 GLY B C   
4603 O O   . GLY B 205 ? 0.7225 1.1923 0.7995 0.0583  -0.0274 0.0042  220 GLY B O   
4604 N N   . ASN B 218 ? 0.5751 1.0981 0.8423 0.0132  -0.0242 -0.0203 233 ASN B N   
4605 C CA  . ASN B 218 ? 0.6073 1.1555 0.9189 0.0098  -0.0211 -0.0301 233 ASN B CA  
4606 C C   . ASN B 218 ? 0.6537 1.2136 0.9684 0.0072  0.0007  -0.0387 233 ASN B C   
4607 O O   . ASN B 218 ? 0.6454 1.2001 0.9397 0.0133  0.0099  -0.0392 233 ASN B O   
4608 C CB  . ASN B 218 ? 0.6612 1.2220 1.0065 0.0194  -0.0346 -0.0337 233 ASN B CB  
4609 C CG  . ASN B 218 ? 0.6809 1.2399 1.0176 0.0296  -0.0293 -0.0361 233 ASN B CG  
4610 O OD1 . ASN B 218 ? 0.7371 1.2981 1.0600 0.0295  -0.0125 -0.0400 233 ASN B OD1 
4611 N ND2 . ASN B 218 ? 0.6882 1.2420 1.0307 0.0372  -0.0439 -0.0337 233 ASN B ND2 
4612 N N   . LYS B 219 ? 0.7764 1.3467 1.1029 -0.0027 0.0117  -0.0441 234 LYS B N   
4613 C CA  . LYS B 219 ? 0.7714 1.3478 1.0913 -0.0068 0.0339  -0.0512 234 LYS B CA  
4614 C C   . LYS B 219 ? 0.7320 1.3194 1.0648 0.0051  0.0368  -0.0577 234 LYS B C   
4615 O O   . LYS B 219 ? 0.7550 1.3498 1.1122 0.0142  0.0228  -0.0588 234 LYS B O   
4616 C CB  . LYS B 219 ? 0.8224 1.4199 1.1722 -0.0201 0.0452  -0.0609 234 LYS B CB  
4617 C CG  . LYS B 219 ? 0.8492 1.4443 1.2033 -0.0327 0.0374  -0.0572 234 LYS B CG  
4618 C CD  . LYS B 219 ? 0.8670 1.4266 1.1703 -0.0363 0.0333  -0.0442 234 LYS B CD  
4619 C CE  . LYS B 219 ? 0.8641 1.4204 1.1741 -0.0460 0.0196  -0.0403 234 LYS B CE  
4620 N NZ  . LYS B 219 ? 0.8475 1.4175 1.1898 -0.0374 -0.0024 -0.0398 234 LYS B NZ  
4621 N N   . ASP B 220 ? 0.6672 1.2528 0.9800 0.0048  0.0543  -0.0615 235 ASP B N   
4622 C CA  . ASP B 220 ? 0.6274 1.2106 0.9275 0.0158  0.0560  -0.0629 235 ASP B CA  
4623 C C   . ASP B 220 ? 0.5934 1.1513 0.8451 0.0203  0.0502  -0.0506 235 ASP B C   
4624 O O   . ASP B 220 ? 0.5469 1.1017 0.7852 0.0290  0.0473  -0.0496 235 ASP B O   
4625 C CB  . ASP B 220 ? 0.6089 1.2058 0.9451 0.0258  0.0447  -0.0688 235 ASP B CB  
4626 C CG  . ASP B 220 ? 0.6220 1.2446 1.0101 0.0239  0.0464  -0.0803 235 ASP B CG  
4627 O OD1 . ASP B 220 ? 0.6141 1.2473 1.0120 0.0131  0.0575  -0.0848 235 ASP B OD1 
4628 O OD2 . ASP B 220 ? 0.6327 1.2647 1.0523 0.0332  0.0360  -0.0851 235 ASP B OD2 
4629 N N   . LEU B 221 ? 0.5633 1.1043 0.7916 0.0141  0.0482  -0.0420 236 LEU B N   
4630 C CA  . LEU B 221 ? 0.5735 1.0921 0.7539 0.0138  0.0552  -0.0344 236 LEU B CA  
4631 C C   . LEU B 221 ? 0.6301 1.1503 0.7976 0.0081  0.0750  -0.0399 236 LEU B C   
4632 O O   . LEU B 221 ? 0.6536 1.1583 0.7823 0.0115  0.0809  -0.0352 236 LEU B O   
4633 C CB  . LEU B 221 ? 0.5628 1.0624 0.7253 0.0055  0.0526  -0.0268 236 LEU B CB  
4634 C CG  . LEU B 221 ? 0.5570 1.0414 0.7081 0.0084  0.0362  -0.0178 236 LEU B CG  
4635 C CD1 . LEU B 221 ? 0.5318 1.0185 0.6821 0.0209  0.0237  -0.0152 236 LEU B CD1 
4636 C CD2 . LEU B 221 ? 0.5673 1.0599 0.7491 -0.0013 0.0283  -0.0197 236 LEU B CD2 
4637 N N   . LYS B 222 ? 0.6620 1.2002 0.8605 -0.0011 0.0851  -0.0498 237 LYS B N   
4638 C CA  . LYS B 222 ? 0.7125 1.2525 0.8992 -0.0089 0.1053  -0.0561 237 LYS B CA  
4639 C C   . LYS B 222 ? 0.6773 1.2229 0.8551 0.0002  0.1101  -0.0604 237 LYS B C   
4640 O O   . LYS B 222 ? 0.6889 1.2227 0.8315 -0.0017 0.1216  -0.0591 237 LYS B O   
4641 C CB  . LYS B 222 ? 0.7706 1.3339 0.9979 -0.0211 0.1159  -0.0678 237 LYS B CB  
4642 C CG  . LYS B 222 ? 0.8501 1.4037 1.0690 -0.0373 0.1218  -0.0650 237 LYS B CG  
4643 C CD  . LYS B 222 ? 0.8951 1.4280 1.0972 -0.0357 0.1051  -0.0528 237 LYS B CD  
4644 C CE  . LYS B 222 ? 0.9165 1.4536 1.1366 -0.0511 0.1046  -0.0542 237 LYS B CE  
4645 N NZ  . LYS B 222 ? 0.8892 1.4189 1.1138 -0.0461 0.0835  -0.0463 237 LYS B NZ  
4646 N N   . ARG B 223 ? 0.6199 1.1812 0.8266 0.0097  0.1005  -0.0653 238 ARG B N   
4647 C CA  . ARG B 223 ? 0.6084 1.1746 0.8071 0.0173  0.1039  -0.0701 238 ARG B CA  
4648 C C   . ARG B 223 ? 0.6337 1.1814 0.7879 0.0246  0.0974  -0.0594 238 ARG B C   
4649 O O   . ARG B 223 ? 0.7107 1.2588 0.8447 0.0282  0.1031  -0.0618 238 ARG B O   
4650 C CB  . ARG B 223 ? 0.5757 1.1582 0.8127 0.0252  0.0942  -0.0771 238 ARG B CB  
4651 C CG  . ARG B 223 ? 0.5812 1.1737 0.8211 0.0284  0.1039  -0.0877 238 ARG B CG  
4652 C CD  . ARG B 223 ? 0.5915 1.1775 0.8117 0.0373  0.0939  -0.0838 238 ARG B CD  
4653 N NE  . ARG B 223 ? 0.6589 1.2507 0.8692 0.0378  0.1049  -0.0928 238 ARG B NE  
4654 C CZ  . ARG B 223 ? 0.7107 1.3015 0.9080 0.0437  0.0988  -0.0931 238 ARG B CZ  
4655 N NH1 . ARG B 223 ? 0.7074 1.2923 0.9009 0.0495  0.0825  -0.0852 238 ARG B NH1 
4656 N NH2 . ARG B 223 ? 0.6982 1.2943 0.8854 0.0425  0.1095  -0.1022 238 ARG B NH2 
4657 N N   . LEU B 224 ? 0.5900 1.1229 0.7297 0.0270  0.0855  -0.0485 239 LEU B N   
4658 C CA  . LEU B 224 ? 0.5433 1.0589 0.6415 0.0346  0.0799  -0.0385 239 LEU B CA  
4659 C C   . LEU B 224 ? 0.5517 1.0485 0.6116 0.0300  0.0913  -0.0338 239 LEU B C   
4660 O O   . LEU B 224 ? 0.5553 1.0438 0.5817 0.0365  0.0926  -0.0300 239 LEU B O   
4661 C CB  . LEU B 224 ? 0.5249 1.0300 0.6208 0.0384  0.0647  -0.0296 239 LEU B CB  
4662 C CG  . LEU B 224 ? 0.5331 1.0261 0.5934 0.0487  0.0577  -0.0215 239 LEU B CG  
4663 C CD1 . LEU B 224 ? 0.5149 1.0239 0.5865 0.0562  0.0503  -0.0254 239 LEU B CD1 
4664 C CD2 . LEU B 224 ? 0.5510 1.0267 0.5995 0.0496  0.0481  -0.0125 239 LEU B CD2 
4665 N N   . LYS B 225 ? 0.5710 1.0602 0.6344 0.0185  0.0988  -0.0336 240 LYS B N   
4666 C CA  . LYS B 225 ? 0.6157 1.0851 0.6427 0.0108  0.1125  -0.0304 240 LYS B CA  
4667 C C   . LYS B 225 ? 0.5943 1.0716 0.6108 0.0099  0.1253  -0.0374 240 LYS B C   
4668 O O   . LYS B 225 ? 0.5883 1.0480 0.5625 0.0131  0.1291  -0.0318 240 LYS B O   
4669 C CB  . LYS B 225 ? 0.6431 1.1085 0.6819 -0.0053 0.1213  -0.0325 240 LYS B CB  
4670 C CG  . LYS B 225 ? 0.6812 1.1265 0.7091 -0.0068 0.1115  -0.0231 240 LYS B CG  
4671 C CD  . LYS B 225 ? 0.7440 1.1798 0.7717 -0.0253 0.1223  -0.0244 240 LYS B CD  
4672 C CE  . LYS B 225 ? 0.7577 1.2247 0.8314 -0.0372 0.1327  -0.0379 240 LYS B CE  
4673 N NZ  . LYS B 225 ? 0.7890 1.2567 0.8778 -0.0549 0.1377  -0.0405 240 LYS B NZ  
4674 N N   . GLU B 226 ? 0.5633 1.0661 0.6170 0.0066  0.1312  -0.0496 241 GLU B N   
4675 C CA  . GLU B 226 ? 0.5960 1.1065 0.6397 0.0059  0.1429  -0.0573 241 GLU B CA  
4676 C C   . GLU B 226 ? 0.6100 1.1151 0.6232 0.0188  0.1341  -0.0519 241 GLU B C   
4677 O O   . GLU B 226 ? 0.6815 1.1712 0.6530 0.0191  0.1396  -0.0474 241 GLU B O   
4678 C CB  . GLU B 226 ? 0.5650 1.1038 0.6560 0.0037  0.1482  -0.0720 241 GLU B CB  
4679 C CG  . GLU B 226 ? 0.5715 1.1204 0.6880 -0.0105 0.1630  -0.0808 241 GLU B CG  
4680 C CD  . GLU B 226 ? 0.5599 1.1366 0.7343 -0.0085 0.1602  -0.0927 241 GLU B CD  
4681 O OE1 . GLU B 226 ? 0.5898 1.1761 0.7939 -0.0161 0.1617  -0.0957 241 GLU B OE1 
4682 O OE2 . GLU B 226 ? 0.5295 1.1178 0.7193 0.0006  0.1561  -0.0990 241 GLU B OE2 
4683 N N   . CYS B 227 ? 0.5667 1.0847 0.5997 0.0290  0.1204  -0.0526 242 CYS B N   
4684 C CA  . CYS B 227 ? 0.5538 1.0745 0.5653 0.0392  0.1135  -0.0510 242 CYS B CA  
4685 C C   . CYS B 227 ? 0.5479 1.0476 0.5133 0.0460  0.1086  -0.0388 242 CYS B C   
4686 O O   . CYS B 227 ? 0.5931 1.0909 0.5289 0.0506  0.1098  -0.0378 242 CYS B O   
4687 C CB  . CYS B 227 ? 0.5478 1.0821 0.5855 0.0471  0.0989  -0.0522 242 CYS B CB  
4688 S SG  . CYS B 227 ? 0.5514 1.1072 0.6406 0.0429  0.1020  -0.0665 242 CYS B SG  
4689 N N   . VAL B 228 ? 0.5280 1.0116 0.4874 0.0471  0.1026  -0.0298 243 VAL B N   
4690 C CA  . VAL B 228 ? 0.5302 0.9896 0.4464 0.0545  0.0982  -0.0181 243 VAL B CA  
4691 C C   . VAL B 228 ? 0.5491 0.9895 0.4281 0.0485  0.1112  -0.0160 243 VAL B C   
4692 O O   . VAL B 228 ? 0.5695 0.9977 0.4102 0.0574  0.1082  -0.0098 243 VAL B O   
4693 C CB  . VAL B 228 ? 0.5198 0.9627 0.4384 0.0540  0.0918  -0.0105 243 VAL B CB  
4694 C CG1 . VAL B 228 ? 0.5538 0.9643 0.4255 0.0587  0.0917  0.0006  243 VAL B CG1 
4695 C CG2 . VAL B 228 ? 0.4898 0.9461 0.4303 0.0627  0.0769  -0.0099 243 VAL B CG2 
4696 N N   . SER B 229 ? 0.5529 0.9914 0.4431 0.0332  0.1254  -0.0214 244 SER B N   
4697 C CA  . SER B 229 ? 0.5954 1.0136 0.4492 0.0238  0.1399  -0.0199 244 SER B CA  
4698 C C   . SER B 229 ? 0.5992 1.0236 0.4301 0.0286  0.1423  -0.0228 244 SER B C   
4699 O O   . SER B 229 ? 0.6155 1.0177 0.3993 0.0338  0.1412  -0.0144 244 SER B O   
4700 C CB  . SER B 229 ? 0.6016 1.0265 0.4802 0.0048  0.1565  -0.0290 244 SER B CB  
4701 O OG  . SER B 229 ? 0.6621 1.0708 0.5054 -0.0058 0.1723  -0.0295 244 SER B OG  
4702 N N   . ILE B 230 ? 0.5754 1.0289 0.4386 0.0277  0.1441  -0.0345 245 ILE B N   
4703 C CA  . ILE B 230 ? 0.5945 1.0568 0.4389 0.0312  0.1456  -0.0389 245 ILE B CA  
4704 C C   . ILE B 230 ? 0.6035 1.0635 0.4226 0.0482  0.1288  -0.0302 245 ILE B C   
4705 O O   . ILE B 230 ? 0.6392 1.0945 0.4231 0.0520  0.1285  -0.0284 245 ILE B O   
4706 C CB  . ILE B 230 ? 0.5671 1.0594 0.4523 0.0273  0.1503  -0.0540 245 ILE B CB  
4707 C CG1 . ILE B 230 ? 0.5686 1.0646 0.4742 0.0111  0.1693  -0.0641 245 ILE B CG1 
4708 C CG2 . ILE B 230 ? 0.5738 1.0754 0.4382 0.0314  0.1493  -0.0585 245 ILE B CG2 
4709 C CD1 . ILE B 230 ? 0.5437 1.0674 0.4996 0.0094  0.1722  -0.0785 245 ILE B CD1 
4710 N N   . ARG B 231 ? 0.5736 1.0379 0.4096 0.0582  0.1149  -0.0253 246 ARG B N   
4711 C CA  . ARG B 231 ? 0.5794 1.0449 0.3947 0.0745  0.0997  -0.0183 246 ARG B CA  
4712 C C   . ARG B 231 ? 0.6148 1.0489 0.3805 0.0810  0.0983  -0.0060 246 ARG B C   
4713 O O   . ARG B 231 ? 0.6229 1.0559 0.3581 0.0912  0.0920  -0.0024 246 ARG B O   
4714 C CB  . ARG B 231 ? 0.5663 1.0422 0.4098 0.0821  0.0870  -0.0164 246 ARG B CB  
4715 C CG  . ARG B 231 ? 0.5657 1.0483 0.3935 0.0989  0.0719  -0.0110 246 ARG B CG  
4716 C CD  . ARG B 231 ? 0.5465 1.0265 0.3890 0.1052  0.0622  -0.0060 246 ARG B CD  
4717 N NE  . ARG B 231 ? 0.5722 1.0206 0.3953 0.1043  0.0651  0.0029  246 ARG B NE  
4718 C CZ  . ARG B 231 ? 0.5583 0.9966 0.3888 0.1071  0.0592  0.0078  246 ARG B CZ  
4719 N NH1 . ARG B 231 ? 0.5011 0.9583 0.3577 0.1109  0.0499  0.0050  246 ARG B NH1 
4720 N NH2 . ARG B 231 ? 0.5888 0.9957 0.3977 0.1048  0.0629  0.0153  246 ARG B NH2 
4721 N N   . ASP B 232 ? 0.6413 1.0491 0.3984 0.0751  0.1037  0.0003  247 ASP B N   
4722 C CA  . ASP B 232 ? 0.6919 1.0634 0.4007 0.0819  0.1016  0.0129  247 ASP B CA  
4723 C C   . ASP B 232 ? 0.7291 1.0812 0.3950 0.0758  0.1115  0.0149  247 ASP B C   
4724 O O   . ASP B 232 ? 0.7786 1.1116 0.4018 0.0881  0.1043  0.0238  247 ASP B O   
4725 C CB  . ASP B 232 ? 0.7118 1.0579 0.4221 0.0737  0.1062  0.0180  247 ASP B CB  
4726 C CG  . ASP B 232 ? 0.7090 1.0644 0.4485 0.0813  0.0946  0.0192  247 ASP B CG  
4727 O OD1 . ASP B 232 ? 0.6799 1.0583 0.4349 0.0943  0.0823  0.0175  247 ASP B OD1 
4728 O OD2 . ASP B 232 ? 0.7529 1.0914 0.4983 0.0724  0.0983  0.0216  247 ASP B OD2 
4729 N N   . GLN B 233 ? 0.7107 1.0668 0.3873 0.0571  0.1280  0.0066  248 GLN B N   
4730 C CA  . GLN B 233 ? 0.7513 1.0883 0.3870 0.0477  0.1400  0.0074  248 GLN B CA  
4731 C C   . GLN B 233 ? 0.7528 1.0998 0.3643 0.0604  0.1304  0.0081  248 GLN B C   
4732 O O   . GLN B 233 ? 0.7861 1.1067 0.3473 0.0679  0.1259  0.0181  248 GLN B O   
4733 C CB  . GLN B 233 ? 0.7432 1.0957 0.4052 0.0265  0.1594  -0.0059 248 GLN B CB  
4734 C CG  . GLN B 233 ? 0.7483 1.0860 0.4214 0.0094  0.1730  -0.0066 248 GLN B CG  
4735 C CD  . GLN B 233 ? 0.7518 1.1120 0.4579 -0.0096 0.1919  -0.0219 248 GLN B CD  
4736 O OE1 . GLN B 233 ? 0.7890 1.1461 0.4725 -0.0196 0.2052  -0.0270 248 GLN B OE1 
4737 N NE2 . GLN B 233 ? 0.7278 1.1107 0.4871 -0.0143 0.1931  -0.0296 248 GLN B NE2 
4738 N N   . LEU B 234 ? 0.7085 1.0934 0.3563 0.0627  0.1264  -0.0026 249 LEU B N   
4739 C CA  . LEU B 234 ? 0.7099 1.1117 0.3424 0.0720  0.1177  -0.0048 249 LEU B CA  
4740 C C   . LEU B 234 ? 0.7516 1.1419 0.3530 0.0931  0.0994  0.0077  249 LEU B C   
4741 O O   . LEU B 234 ? 0.8040 1.1793 0.3602 0.0994  0.0951  0.0139  249 LEU B O   
4742 C CB  . LEU B 234 ? 0.6506 1.0927 0.3319 0.0716  0.1146  -0.0176 249 LEU B CB  
4743 C CG  . LEU B 234 ? 0.6468 1.1128 0.3211 0.0801  0.1042  -0.0219 249 LEU B CG  
4744 C CD1 . LEU B 234 ? 0.6144 1.1117 0.3314 0.0713  0.1093  -0.0373 249 LEU B CD1 
4745 C CD2 . LEU B 234 ? 0.6375 1.1116 0.3092 0.1000  0.0843  -0.0141 249 LEU B CD2 
4746 N N   . LEU B 235 ? 0.7426 1.1395 0.3675 0.1045  0.0885  0.0110  250 LEU B N   
4747 C CA  . LEU B 235 ? 0.7751 1.1599 0.3739 0.1254  0.0726  0.0222  250 LEU B CA  
4748 C C   . LEU B 235 ? 0.8526 1.1904 0.3963 0.1275  0.0755  0.0347  250 LEU B C   
4749 O O   . LEU B 235 ? 0.9134 1.2410 0.4188 0.1420  0.0650  0.0419  250 LEU B O   
4750 C CB  . LEU B 235 ? 0.7394 1.1313 0.3696 0.1337  0.0647  0.0237  250 LEU B CB  
4751 C CG  . LEU B 235 ? 0.7158 1.1467 0.3765 0.1458  0.0511  0.0181  250 LEU B CG  
4752 C CD1 . LEU B 235 ? 0.7058 1.1714 0.3838 0.1395  0.0518  0.0067  250 LEU B CD1 
4753 C CD2 . LEU B 235 ? 0.6858 1.1260 0.3868 0.1436  0.0497  0.0156  250 LEU B CD2 
4754 N N   . TYR B 236 ? 0.8730 1.1823 0.4116 0.1124  0.0892  0.0371  251 TYR B N   
4755 C CA  . TYR B 236 ? 0.9417 1.2013 0.4261 0.1120  0.0930  0.0493  251 TYR B CA  
4756 C C   . TYR B 236 ? 1.0052 1.2515 0.4427 0.1100  0.0954  0.0520  251 TYR B C   
4757 O O   . TYR B 236 ? 1.0378 1.2518 0.4249 0.1231  0.0867  0.0639  251 TYR B O   
4758 C CB  . TYR B 236 ? 0.9470 1.1842 0.4382 0.0909  0.1100  0.0486  251 TYR B CB  
4759 C CG  . TYR B 236 ? 1.0189 1.2007 0.4569 0.0899  0.1132  0.0617  251 TYR B CG  
4760 C CD1 . TYR B 236 ? 1.0412 1.1983 0.4615 0.1083  0.1004  0.0722  251 TYR B CD1 
4761 C CD2 . TYR B 236 ? 1.0735 1.2256 0.4774 0.0697  0.1302  0.0631  251 TYR B CD2 
4762 C CE1 . TYR B 236 ? 1.1058 1.2071 0.4746 0.1073  0.1036  0.0842  251 TYR B CE1 
4763 C CE2 . TYR B 236 ? 1.1352 1.2324 0.4867 0.0668  0.1339  0.0753  251 TYR B CE2 
4764 C CZ  . TYR B 236 ? 1.1650 1.2355 0.4985 0.0858  0.1203  0.0861  251 TYR B CZ  
4765 O OH  . TYR B 236 ? 1.2311 1.2427 0.5100 0.0823  0.1245  0.0980  251 TYR B OH  
4766 N N   . LYS B 237 ? 1.0174 1.2876 0.4704 0.0944  0.1064  0.0406  252 LYS B N   
4767 C CA  . LYS B 237 ? 1.0701 1.3335 0.4817 0.0915  0.1082  0.0411  252 LYS B CA  
4768 C C   . LYS B 237 ? 1.0757 1.3533 0.4730 0.1159  0.0861  0.0459  252 LYS B C   
4769 O O   . LYS B 237 ? 1.1577 1.4073 0.5026 0.1267  0.0775  0.0569  252 LYS B O   
4770 C CB  . LYS B 237 ? 1.0614 1.3564 0.5013 0.0729  0.1223  0.0252  252 LYS B CB  
4771 C CG  . LYS B 237 ? 1.1142 1.4131 0.5187 0.0715  0.1212  0.0229  252 LYS B CG  
4772 C CD  . LYS B 237 ? 1.0921 1.4335 0.5363 0.0612  0.1281  0.0055  252 LYS B CD  
4773 C CE  . LYS B 237 ? 1.1191 1.4817 0.5462 0.0708  0.1147  0.0029  252 LYS B CE  
4774 N NZ  . LYS B 237 ? 1.0861 1.4899 0.5549 0.0625  0.1194  -0.0144 252 LYS B NZ  
4775 N N   . LYS B 238 ? 1.0192 1.3404 0.4632 0.1246  0.0765  0.0377  253 LYS B N   
4776 C CA  . LYS B 238 ? 1.0196 1.3636 0.4577 0.1460  0.0562  0.0395  253 LYS B CA  
4777 C C   . LYS B 238 ? 1.0450 1.3599 0.4506 0.1693  0.0413  0.0544  253 LYS B C   
4778 O O   . LYS B 238 ? 1.0652 1.3840 0.4448 0.1881  0.0249  0.0597  253 LYS B O   
4779 C CB  . LYS B 238 ? 0.9611 1.3551 0.4576 0.1478  0.0511  0.0273  253 LYS B CB  
4780 C CG  . LYS B 238 ? 0.9625 1.3935 0.4613 0.1575  0.0373  0.0215  253 LYS B CG  
4781 C CD  . LYS B 238 ? 0.9872 1.4252 0.4681 0.1429  0.0450  0.0140  253 LYS B CD  
4782 C CE  . LYS B 238 ? 1.0249 1.4729 0.4707 0.1576  0.0276  0.0177  253 LYS B CE  
4783 N NZ  . LYS B 238 ? 0.9972 1.4863 0.4600 0.1506  0.0250  0.0041  253 LYS B NZ  
4784 N N   . LEU B 239 ? 1.0454 1.3302 0.4514 0.1679  0.0469  0.0607  254 LEU B N   
4785 C CA  . LEU B 239 ? 1.0788 1.3265 0.4493 0.1880  0.0359  0.0747  254 LEU B CA  
4786 C C   . LEU B 239 ? 1.1251 1.3244 0.4280 0.1891  0.0364  0.0867  254 LEU B C   
4787 O O   . LEU B 239 ? 1.1355 1.3246 0.4046 0.2116  0.0196  0.0953  254 LEU B O   
4788 C CB  . LEU B 239 ? 1.0836 1.3107 0.4725 0.1830  0.0433  0.0769  254 LEU B CB  
4789 C CG  . LEU B 239 ? 1.1424 1.3137 0.4890 0.1919  0.0418  0.0907  254 LEU B CG  
4790 C CD1 . LEU B 239 ? 1.1990 1.3583 0.5130 0.2228  0.0220  0.1003  254 LEU B CD1 
4791 C CD2 . LEU B 239 ? 1.1222 1.2924 0.5037 0.1875  0.0464  0.0884  254 LEU B CD2 
4792 N N   . LEU B 240 ? 1.1297 1.2986 0.4125 0.1650  0.0554  0.0873  255 LEU B N   
4793 C CA  . LEU B 240 ? 1.1837 1.3022 0.3983 0.1613  0.0586  0.0986  255 LEU B CA  
4794 C C   . LEU B 240 ? 1.2021 1.3364 0.3904 0.1730  0.0450  0.0995  255 LEU B C   
4795 O O   . LEU B 240 ? 1.2352 1.3389 0.3731 0.1916  0.0307  0.1122  255 LEU B O   
4796 C CB  . LEU B 240 ? 1.1914 1.2891 0.3975 0.1287  0.0838  0.0946  255 LEU B CB  
4797 C CG  . LEU B 240 ? 1.2157 1.2640 0.4018 0.1164  0.0966  0.1021  255 LEU B CG  
4798 C CD1 . LEU B 240 ? 1.2032 1.2454 0.4090 0.1342  0.0857  0.1069  255 LEU B CD1 
4799 C CD2 . LEU B 240 ? 1.1867 1.2455 0.4034 0.0846  0.1210  0.0906  255 LEU B CD2 
4800 N N   . GLU B 241 ? 1.1682 1.3509 0.3919 0.1630  0.0483  0.0857  256 GLU B N   
4801 C CA  . GLU B 241 ? 1.1792 1.3882 0.3886 0.1725  0.0348  0.0832  256 GLU B CA  
4802 C C   . GLU B 241 ? 1.1881 1.4097 0.3922 0.2052  0.0084  0.0901  256 GLU B C   
4803 O O   . GLU B 241 ? 1.2262 1.4506 0.3974 0.2169  -0.0058 0.0941  256 GLU B O   
4804 C CB  . GLU B 241 ? 1.1266 1.3903 0.3880 0.1582  0.0419  0.0652  256 GLU B CB  
4805 C CG  . GLU B 241 ? 1.1461 1.4011 0.4036 0.1280  0.0661  0.0570  256 GLU B CG  
4806 C CD  . GLU B 241 ? 1.1019 1.4065 0.4077 0.1147  0.0736  0.0387  256 GLU B CD  
4807 O OE1 . GLU B 241 ? 1.0636 1.4103 0.4056 0.1265  0.0603  0.0320  256 GLU B OE1 
4808 O OE2 . GLU B 241 ? 1.1051 1.4051 0.4117 0.0913  0.0941  0.0303  256 GLU B OE2 
4809 N N   . HIS B 242 ? 1.1926 1.4250 0.4313 0.2197  0.0019  0.0905  257 HIS B N   
4810 C CA  . HIS B 242 ? 1.1888 1.4353 0.4269 0.2517  -0.0216 0.0957  257 HIS B CA  
4811 C C   . HIS B 242 ? 1.2610 1.4507 0.4411 0.2705  -0.0309 0.1129  257 HIS B C   
4812 O O   . HIS B 242 ? 1.2854 1.4780 0.4423 0.2965  -0.0516 0.1193  257 HIS B O   
4813 C CB  . HIS B 242 ? 1.1056 1.3870 0.4031 0.2593  -0.0240 0.0882  257 HIS B CB  
4814 C CG  . HIS B 242 ? 1.0490 1.3945 0.3942 0.2583  -0.0298 0.0740  257 HIS B CG  
4815 N ND1 . HIS B 242 ? 1.0263 1.3959 0.3864 0.2359  -0.0193 0.0631  257 HIS B ND1 
4816 C CD2 . HIS B 242 ? 1.0206 1.4102 0.4000 0.2761  -0.0444 0.0684  257 HIS B CD2 
4817 C CE1 . HIS B 242 ? 0.9885 1.4117 0.3882 0.2394  -0.0275 0.0519  257 HIS B CE1 
4818 N NE2 . HIS B 242 ? 0.9885 1.4261 0.4012 0.2628  -0.0425 0.0547  257 HIS B NE2 
4819 N N   . LYS B 243 ? 1.2990 1.4372 0.4560 0.2574  -0.0158 0.1200  258 LYS B N   
4820 C CA  . LYS B 243 ? 1.3852 1.4623 0.4865 0.2733  -0.0225 0.1364  258 LYS B CA  
4821 C C   . LYS B 243 ? 1.4887 1.5356 0.5244 0.2804  -0.0326 0.1470  258 LYS B C   
4822 O O   . LYS B 243 ? 1.5297 1.5418 0.5235 0.3059  -0.0488 0.1600  258 LYS B O   
4823 C CB  . LYS B 243 ? 1.3875 1.4156 0.4763 0.2529  -0.0025 0.1406  258 LYS B CB  
4824 C CG  . LYS B 243 ? 1.4428 1.4137 0.4891 0.2735  -0.0110 0.1552  258 LYS B CG  
4825 C CD  . LYS B 243 ? 1.4573 1.3743 0.4820 0.2509  0.0088  0.1601  258 LYS B CD  
4826 C CE  . LYS B 243 ? 1.3762 1.3200 0.4615 0.2388  0.0199  0.1496  258 LYS B CE  
4827 N NZ  . LYS B 243 ? 1.4030 1.2919 0.4625 0.2182  0.0370  0.1551  258 LYS B NZ  
4828 N N   . LYS B 244 ? 1.5459 1.6050 0.5717 0.2588  -0.0237 0.1415  259 LYS B N   
4829 C CA  . LYS B 244 ? 1.6347 1.6787 0.6050 0.2670  -0.0367 0.1494  259 LYS B CA  
4830 C C   . LYS B 244 ? 1.6441 1.7330 0.6323 0.2996  -0.0645 0.1481  259 LYS B C   
4831 O O   . LYS B 244 ? 1.6838 1.7495 0.6484 0.3290  -0.0823 0.1593  259 LYS B O   
4832 C CB  . LYS B 244 ? 1.6744 1.7264 0.6326 0.2364  -0.0208 0.1418  259 LYS B CB  
4833 C CG  . LYS B 244 ? 1.6439 1.7637 0.6663 0.2216  -0.0134 0.1223  259 LYS B CG  
4834 C CD  . LYS B 244 ? 1.7141 1.8354 0.7160 0.1938  0.0018  0.1152  259 LYS B CD  
4835 C CE  . LYS B 244 ? 1.7063 1.8898 0.7417 0.1931  -0.0059 0.1008  259 LYS B CE  
4836 N NZ  . LYS B 244 ? 1.7448 1.9257 0.7293 0.2037  -0.0242 0.1067  259 LYS B NZ  
4837 N N   . SER B 245 ? 1.6224 1.7762 0.6555 0.2952  -0.0680 0.1337  260 SER B N   
4838 C CA  . SER B 245 ? 1.6517 1.8485 0.6916 0.3216  -0.0942 0.1320  260 SER B CA  
4839 C C   . SER B 245 ? 1.6126 1.8333 0.6926 0.3491  -0.1072 0.1310  260 SER B C   
4840 O O   . SER B 245 ? 1.5695 1.8428 0.7114 0.3453  -0.1040 0.1174  260 SER B O   
4841 C CB  . SER B 245 ? 1.6330 1.8913 0.7085 0.3054  -0.0925 0.1157  260 SER B CB  
4842 O OG  . SER B 245 ? 1.6768 1.9191 0.7023 0.2930  -0.0927 0.1184  260 SER B OG  
4843 N N   . LEU B 246 ? 1.6452 1.8253 0.6882 0.3766  -0.1213 0.1452  261 LEU B N   
4844 C CA  . LEU B 246 ? 1.6372 1.8248 0.7130 0.3993  -0.1274 0.1449  261 LEU B CA  
4845 C C   . LEU B 246 ? 1.6695 1.8733 0.7378 0.4399  -0.1557 0.1497  261 LEU B C   
4846 O O   . LEU B 246 ? 1.7373 1.8910 0.7495 0.4602  -0.1681 0.1646  261 LEU B O   
4847 C CB  . LEU B 246 ? 1.6728 1.7920 0.7210 0.3933  -0.1127 0.1553  261 LEU B CB  
4848 C CG  . LEU B 246 ? 1.6375 1.7630 0.7287 0.4019  -0.1081 0.1511  261 LEU B CG  
4849 C CD1 . LEU B 246 ? 1.5401 1.7382 0.7063 0.3933  -0.1040 0.1335  261 LEU B CD1 
4850 C CD2 . LEU B 246 ? 1.6439 1.7102 0.7153 0.3811  -0.0870 0.1572  261 LEU B CD2 
4851 N N   . THR B 247 ? 1.6276 1.9012 0.7537 0.4514  -0.1653 0.1365  262 THR B N   
4852 C CA  . THR B 247 ? 1.6121 1.9176 0.7430 0.4888  -0.1921 0.1371  262 THR B CA  
4853 C C   . THR B 247 ? 1.5806 1.9021 0.7534 0.5095  -0.1936 0.1324  262 THR B C   
4854 O O   . THR B 247 ? 1.5201 1.9031 0.7536 0.5049  -0.1908 0.1174  262 THR B O   
4855 C CB  . THR B 247 ? 1.5645 1.9443 0.7268 0.4849  -0.2033 0.1240  262 THR B CB  
4856 O OG1 . THR B 247 ? 1.5582 1.9270 0.6941 0.4554  -0.1934 0.1238  262 THR B OG1 
4857 C CG2 . THR B 247 ? 1.5908 1.9945 0.7391 0.5217  -0.2337 0.1277  262 THR B CG2 
4858 N N   . PRO B 248 ? 1.6053 1.8685 0.7436 0.5308  -0.1967 0.1450  263 PRO B N   
4859 C CA  . PRO B 248 ? 1.5936 1.8658 0.7645 0.5529  -0.1986 0.1411  263 PRO B CA  
4860 C C   . PRO B 248 ? 1.6083 1.9523 0.8232 0.5815  -0.2182 0.1301  263 PRO B C   
4861 O O   . PRO B 248 ? 1.5901 1.9630 0.8503 0.5890  -0.2141 0.1206  263 PRO B O   
4862 C CB  . PRO B 248 ? 1.6436 1.8351 0.7538 0.5747  -0.2037 0.1585  263 PRO B CB  
4863 C CG  . PRO B 248 ? 1.6751 1.8076 0.7312 0.5479  -0.1916 0.1697  263 PRO B CG  
4864 C CD  . PRO B 248 ? 1.6567 1.8353 0.7244 0.5261  -0.1916 0.1624  263 PRO B CD  
4865 N N   . GLY B 249 ? 1.6404 2.0137 0.8420 0.5962  -0.2388 0.1309  264 GLY B N   
4866 C CA  . GLY B 249 ? 1.6317 2.0767 0.8738 0.6236  -0.2590 0.1201  264 GLY B CA  
4867 C C   . GLY B 249 ? 1.5576 2.0826 0.8646 0.6011  -0.2516 0.1008  264 GLY B C   
4868 O O   . GLY B 249 ? 1.5134 2.0790 0.8710 0.6066  -0.2477 0.0890  264 GLY B O   
4869 N N   . GLU B 250 ? 1.5644 2.1097 0.8672 0.5756  -0.2495 0.0973  265 GLU B N   
4870 C CA  . GLU B 250 ? 1.5204 2.1330 0.8780 0.5496  -0.2408 0.0796  265 GLU B CA  
4871 C C   . GLU B 250 ? 1.5136 2.0947 0.8735 0.5107  -0.2135 0.0788  265 GLU B C   
4872 O O   . GLU B 250 ? 1.6127 2.1651 0.9387 0.4902  -0.2070 0.0841  265 GLU B O   
4873 C CB  . GLU B 250 ? 1.5163 2.1753 0.8701 0.5455  -0.2561 0.0741  265 GLU B CB  
4874 C CG  . GLU B 250 ? 1.5935 2.2494 0.9083 0.5789  -0.2844 0.0836  265 GLU B CG  
4875 C CD  . GLU B 250 ? 1.5754 2.2800 0.9231 0.6162  -0.3041 0.0774  265 GLU B CD  
4876 O OE1 . GLU B 250 ? 1.5425 2.3028 0.9494 0.6120  -0.2977 0.0619  265 GLU B OE1 
4877 O OE2 . GLU B 250 ? 1.5875 2.2740 0.9007 0.6500  -0.3263 0.0880  265 GLU B OE2 
4878 N N   . PRO B 251 ? 1.4202 2.0063 0.8193 0.5006  -0.1975 0.0721  266 PRO B N   
4879 C CA  . PRO B 251 ? 1.3749 1.9355 0.7806 0.4653  -0.1732 0.0707  266 PRO B CA  
4880 C C   . PRO B 251 ? 1.2938 1.9074 0.7389 0.4368  -0.1652 0.0557  266 PRO B C   
4881 O O   . PRO B 251 ? 1.2330 1.9065 0.7230 0.4395  -0.1705 0.0427  266 PRO B O   
4882 C CB  . PRO B 251 ? 1.3758 1.9225 0.8065 0.4694  -0.1628 0.0697  266 PRO B CB  
4883 C CG  . PRO B 251 ? 1.3778 1.9754 0.8409 0.4968  -0.1779 0.0616  266 PRO B CG  
4884 C CD  . PRO B 251 ? 1.4046 2.0204 0.8433 0.5210  -0.2010 0.0651  266 PRO B CD  
4885 N N   . ARG B 252 ? 1.2722 1.8615 0.6999 0.4089  -0.1514 0.0569  267 ARG B N   
4886 C CA  . ARG B 252 ? 1.1984 1.8293 0.6534 0.3820  -0.1442 0.0436  267 ARG B CA  
4887 C C   . ARG B 252 ? 1.1104 1.7466 0.6069 0.3574  -0.1241 0.0350  267 ARG B C   
4888 O O   . ARG B 252 ? 1.0469 1.7244 0.5775 0.3391  -0.1192 0.0219  267 ARG B O   
4889 C CB  . ARG B 252 ? 1.2566 1.8621 0.6686 0.3663  -0.1412 0.0480  267 ARG B CB  
4890 C CG  . ARG B 252 ? 1.3140 1.8479 0.6806 0.3586  -0.1284 0.0617  267 ARG B CG  
4891 C CD  . ARG B 252 ? 1.3697 1.8784 0.6833 0.3517  -0.1312 0.0681  267 ARG B CD  
4892 N NE  . ARG B 252 ? 1.4334 1.8721 0.7003 0.3449  -0.1191 0.0816  267 ARG B NE  
4893 C CZ  . ARG B 252 ? 1.4634 1.8768 0.7320 0.3166  -0.0959 0.0795  267 ARG B CZ  
4894 N NH1 . ARG B 252 ? 1.4504 1.8928 0.7721 0.2987  -0.0818 0.0671  267 ARG B NH1 
4895 N NH2 . ARG B 252 ? 1.5179 1.8766 0.7346 0.3059  -0.0868 0.0897  267 ARG B NH2 
4896 N N   . ASP B 253 ? 1.0927 1.6859 0.5849 0.3576  -0.1133 0.0425  268 ASP B N   
4897 C CA  . ASP B 253 ? 1.0340 1.6203 0.5564 0.3333  -0.0941 0.0372  268 ASP B CA  
4898 C C   . ASP B 253 ? 1.0211 1.5853 0.5544 0.3434  -0.0905 0.0417  268 ASP B C   
4899 O O   . ASP B 253 ? 1.0295 1.5676 0.5367 0.3672  -0.0994 0.0512  268 ASP B O   
4900 C CB  . ASP B 253 ? 1.0519 1.5961 0.5468 0.3108  -0.0788 0.0419  268 ASP B CB  
4901 C CG  . ASP B 253 ? 1.0582 1.6299 0.5586 0.2913  -0.0753 0.0322  268 ASP B CG  
4902 O OD1 . ASP B 253 ? 1.0645 1.6768 0.6085 0.2792  -0.0716 0.0196  268 ASP B OD1 
4903 O OD2 . ASP B 253 ? 1.0464 1.5986 0.5066 0.2878  -0.0763 0.0370  268 ASP B OD2 
4904 N N   . LEU B 254 ? 0.9744 1.5468 0.5445 0.3250  -0.0774 0.0347  269 LEU B N   
4905 C CA  . LEU B 254 ? 0.9565 1.5042 0.5360 0.3291  -0.0716 0.0385  269 LEU B CA  
4906 C C   . LEU B 254 ? 0.9620 1.4470 0.5035 0.3241  -0.0623 0.0506  269 LEU B C   
4907 O O   . LEU B 254 ? 0.9372 1.3871 0.4591 0.3387  -0.0641 0.0590  269 LEU B O   
4908 C CB  . LEU B 254 ? 0.9424 1.5130 0.5678 0.3084  -0.0607 0.0284  269 LEU B CB  
4909 C CG  . LEU B 254 ? 0.9802 1.5381 0.6192 0.3163  -0.0588 0.0302  269 LEU B CG  
4910 C CD1 . LEU B 254 ? 0.9665 1.5741 0.6502 0.3129  -0.0606 0.0181  269 LEU B CD1 
4911 C CD2 . LEU B 254 ? 0.9903 1.5035 0.6242 0.2996  -0.0447 0.0357  269 LEU B CD2 
4912 N N   . LEU B 255 ? 0.9835 1.4547 0.5142 0.3022  -0.0516 0.0505  270 LEU B N   
4913 C CA  . LEU B 255 ? 1.0362 1.4506 0.5280 0.2939  -0.0416 0.0610  270 LEU B CA  
4914 C C   . LEU B 255 ? 1.1114 1.4913 0.5521 0.3181  -0.0537 0.0737  270 LEU B C   
4915 O O   . LEU B 255 ? 1.1736 1.5035 0.5850 0.3233  -0.0503 0.0839  270 LEU B O   
4916 C CB  . LEU B 255 ? 1.0301 1.4448 0.5166 0.2694  -0.0301 0.0570  270 LEU B CB  
4917 C CG  . LEU B 255 ? 1.0666 1.4293 0.5182 0.2536  -0.0157 0.0648  270 LEU B CG  
4918 C CD1 . LEU B 255 ? 1.0578 1.3932 0.5227 0.2456  -0.0050 0.0674  270 LEU B CD1 
4919 C CD2 . LEU B 255 ? 1.0470 1.4245 0.5063 0.2293  -0.0037 0.0563  270 LEU B CD2 
4920 N N   . ASP B 256 ? 1.1301 1.5368 0.5600 0.3329  -0.0686 0.0727  271 ASP B N   
4921 C CA  . ASP B 256 ? 1.1653 1.5469 0.5502 0.3606  -0.0844 0.0840  271 ASP B CA  
4922 C C   . ASP B 256 ? 1.1235 1.4914 0.5123 0.3843  -0.0908 0.0881  271 ASP B C   
4923 O O   . ASP B 256 ? 1.1364 1.4479 0.4876 0.3920  -0.0888 0.0996  271 ASP B O   
4924 C CB  . ASP B 256 ? 1.1710 1.5999 0.5585 0.3742  -0.1019 0.0790  271 ASP B CB  
4925 C CG  . ASP B 256 ? 1.2316 1.6314 0.5640 0.3776  -0.1089 0.0887  271 ASP B CG  
4926 O OD1 . ASP B 256 ? 1.2628 1.6116 0.5595 0.3615  -0.0960 0.0966  271 ASP B OD1 
4927 O OD2 . ASP B 256 ? 1.2797 1.7088 0.6042 0.3954  -0.1274 0.0878  271 ASP B OD2 
4928 N N   . ALA B 257 ? 1.0586 1.4773 0.4925 0.3944  -0.0973 0.0778  272 ALA B N   
4929 C CA  . ALA B 257 ? 1.0743 1.4876 0.5156 0.4182  -0.1035 0.0792  272 ALA B CA  
4930 C C   . ALA B 257 ? 1.0892 1.4463 0.5158 0.4093  -0.0897 0.0862  272 ALA B C   
4931 O O   . ALA B 257 ? 1.1431 1.4585 0.5397 0.4294  -0.0942 0.0951  272 ALA B O   
4932 C CB  . ALA B 257 ? 1.0164 1.4931 0.5142 0.4200  -0.1060 0.0648  272 ALA B CB  
4933 N N   . LEU B 258 ? 1.0473 1.4027 0.4947 0.3791  -0.0733 0.0819  273 LEU B N   
4934 C CA  . LEU B 258 ? 1.0577 1.3658 0.4959 0.3673  -0.0601 0.0871  273 LEU B CA  
4935 C C   . LEU B 258 ? 1.1376 1.3796 0.5161 0.3710  -0.0586 0.1013  273 LEU B C   
4936 O O   . LEU B 258 ? 1.1711 1.3691 0.5268 0.3813  -0.0578 0.1084  273 LEU B O   
4937 C CB  . LEU B 258 ? 1.0266 1.3487 0.4985 0.3344  -0.0443 0.0796  273 LEU B CB  
4938 C CG  . LEU B 258 ? 0.9677 1.3418 0.4958 0.3293  -0.0440 0.0669  273 LEU B CG  
4939 C CD1 . LEU B 258 ? 0.9272 1.3088 0.4835 0.2983  -0.0297 0.0610  273 LEU B CD1 
4940 C CD2 . LEU B 258 ? 0.9566 1.3232 0.4942 0.3441  -0.0466 0.0669  273 LEU B CD2 
4941 N N   . LEU B 259 ? 1.1923 1.4252 0.5423 0.3628  -0.0585 0.1055  274 LEU B N   
4942 C CA  . LEU B 259 ? 1.2884 1.4571 0.5755 0.3668  -0.0582 0.1197  274 LEU B CA  
4943 C C   . LEU B 259 ? 1.3606 1.5078 0.6143 0.4040  -0.0767 0.1286  274 LEU B C   
4944 O O   . LEU B 259 ? 1.3946 1.4824 0.6089 0.4123  -0.0753 0.1390  274 LEU B O   
4945 C CB  . LEU B 259 ? 1.3145 1.4815 0.5774 0.3497  -0.0543 0.1213  274 LEU B CB  
4946 C CG  . LEU B 259 ? 1.2815 1.4477 0.5635 0.3130  -0.0328 0.1154  274 LEU B CG  
4947 C CD1 . LEU B 259 ? 1.2583 1.4540 0.5441 0.2964  -0.0293 0.1091  274 LEU B CD1 
4948 C CD2 . LEU B 259 ? 1.3338 1.4323 0.5731 0.3000  -0.0197 0.1258  274 LEU B CD2 
4949 N N   . ILE B 260 ? 1.3816 1.5773 0.6523 0.4262  -0.0939 0.1237  275 ILE B N   
4950 C CA  . ILE B 260 ? 1.4516 1.6359 0.6975 0.4648  -0.1133 0.1303  275 ILE B CA  
4951 C C   . ILE B 260 ? 1.4988 1.6510 0.7450 0.4788  -0.1105 0.1324  275 ILE B C   
4952 O O   . ILE B 260 ? 1.5843 1.6792 0.7831 0.4980  -0.1161 0.1442  275 ILE B O   
4953 C CB  . ILE B 260 ? 1.4168 1.6740 0.7013 0.4858  -0.1306 0.1199  275 ILE B CB  
4954 C CG1 . ILE B 260 ? 1.3919 1.6900 0.6826 0.4713  -0.1342 0.1150  275 ILE B CG1 
4955 C CG2 . ILE B 260 ? 1.4626 1.7066 0.7209 0.5274  -0.1511 0.1268  275 ILE B CG2 
4956 C CD1 . ILE B 260 ? 1.4558 1.7068 0.6867 0.4650  -0.1354 0.1274  275 ILE B CD1 
4957 N N   . GLY B 261 ? 1.4495 1.6376 0.7476 0.4692  -0.1021 0.1208  276 GLY B N   
4958 C CA  . GLY B 261 ? 1.4782 1.6387 0.7803 0.4772  -0.0969 0.1209  276 GLY B CA  
4959 C C   . GLY B 261 ? 1.5065 1.5965 0.7717 0.4574  -0.0819 0.1303  276 GLY B C   
4960 O O   . GLY B 261 ? 1.5566 1.5943 0.7897 0.4723  -0.0826 0.1376  276 GLY B O   
4961 N N   . GLN B 262 ? 1.4767 1.5653 0.7465 0.4236  -0.0679 0.1295  277 GLN B N   
4962 C CA  . GLN B 262 ? 1.5219 1.5506 0.7617 0.4006  -0.0522 0.1367  277 GLN B CA  
4963 C C   . GLN B 262 ? 1.6195 1.5797 0.7887 0.4105  -0.0559 0.1520  277 GLN B C   
4964 O O   . GLN B 262 ? 1.6877 1.5873 0.8230 0.4015  -0.0463 0.1594  277 GLN B O   
4965 C CB  . GLN B 262 ? 1.4889 1.5399 0.7551 0.3636  -0.0369 0.1304  277 GLN B CB  
4966 C CG  . GLN B 262 ? 1.5185 1.5192 0.7651 0.3365  -0.0194 0.1349  277 GLN B CG  
4967 C CD  . GLN B 262 ? 1.6136 1.5670 0.8053 0.3253  -0.0139 0.1453  277 GLN B CD  
4968 O OE1 . GLN B 262 ? 1.6492 1.6190 0.8284 0.3281  -0.0197 0.1465  277 GLN B OE1 
4969 N NE2 . GLN B 262 ? 1.6698 1.5630 0.8261 0.3112  -0.0024 0.1526  277 GLN B NE2 
4970 N N   . GLN B 263 ? 1.6484 1.6169 0.7938 0.4282  -0.0701 0.1568  278 GLN B N   
4971 C CA  . GLN B 263 ? 1.7332 1.6368 0.8081 0.4446  -0.0783 0.1724  278 GLN B CA  
4972 C C   . GLN B 263 ? 1.7415 1.5949 0.7902 0.4698  -0.0834 0.1789  278 GLN B C   
4973 O O   . GLN B 263 ? 1.8227 1.6020 0.8148 0.4674  -0.0788 0.1910  278 GLN B O   
4974 C CB  . GLN B 263 ? 1.7856 1.7176 0.8483 0.4692  -0.0988 0.1749  278 GLN B CB  
4975 C CG  . GLN B 263 ? 1.8495 1.7678 0.8749 0.4513  -0.0968 0.1812  278 GLN B CG  
4976 C CD  . GLN B 263 ? 1.8836 1.8111 0.8799 0.4803  -0.1202 0.1875  278 GLN B CD  
4977 O OE1 . GLN B 263 ? 1.9373 1.8385 0.9063 0.5147  -0.1367 0.1954  278 GLN B OE1 
4978 N NE2 . GLN B 263 ? 1.8502 1.8142 0.8514 0.4668  -0.1220 0.1838  278 GLN B NE2 
4979 N N   . ARG B 264 ? 1.6678 1.5617 0.7577 0.4928  -0.0920 0.1700  279 ARG B N   
4980 C CA  . ARG B 264 ? 1.7037 1.5614 0.7725 0.5257  -0.1011 0.1742  279 ARG B CA  
4981 C C   . ARG B 264 ? 1.7051 1.5240 0.7752 0.5079  -0.0841 0.1727  279 ARG B C   
4982 O O   . ARG B 264 ? 1.6439 1.4893 0.7532 0.5142  -0.0822 0.1628  279 ARG B O   
4983 C CB  . ARG B 264 ? 1.6594 1.5842 0.7753 0.5566  -0.1163 0.1632  279 ARG B CB  
4984 C CG  . ARG B 264 ? 1.6236 1.6177 0.7685 0.5564  -0.1266 0.1572  279 ARG B CG  
4985 C CD  . ARG B 264 ? 1.5944 1.6555 0.7852 0.5856  -0.1411 0.1457  279 ARG B CD  
4986 N NE  . ARG B 264 ? 1.6684 1.7108 0.8254 0.6270  -0.1618 0.1533  279 ARG B NE  
4987 C CZ  . ARG B 264 ? 1.6842 1.7641 0.8683 0.6612  -0.1750 0.1455  279 ARG B CZ  
4988 N NH1 . ARG B 264 ? 1.6364 1.7736 0.8800 0.6572  -0.1686 0.1299  279 ARG B NH1 
4989 N NH2 . ARG B 264 ? 1.7579 1.8172 0.9086 0.6998  -0.1948 0.1533  279 ARG B NH2 
4990 N N   . GLY B 265 ? 1.7615 1.5177 0.7873 0.4836  -0.0713 0.1822  280 GLY B N   
4991 C CA  . GLY B 265 ? 1.7734 1.4982 0.8030 0.4587  -0.0538 0.1799  280 GLY B CA  
4992 C C   . GLY B 265 ? 1.8761 1.5141 0.8383 0.4447  -0.0446 0.1933  280 GLY B C   
4993 O O   . GLY B 265 ? 1.8723 1.4854 0.7949 0.4357  -0.0444 0.2024  280 GLY B O   
4994 N N   . SER B 266 ? 1.9428 1.5332 0.8896 0.4425  -0.0369 0.1941  281 SER B N   
4995 C CA  . SER B 266 ? 2.0248 1.5349 0.9150 0.4207  -0.0239 0.2041  281 SER B CA  
4996 C C   . SER B 266 ? 1.9852 1.5140 0.9120 0.3786  -0.0045 0.1953  281 SER B C   
4997 O O   . SER B 266 ? 1.8684 1.4683 0.8588 0.3693  -0.0029 0.1833  281 SER B O   
4998 C CB  . SER B 266 ? 2.0735 1.5165 0.9213 0.4458  -0.0285 0.2100  281 SER B CB  
4999 O OG  . SER B 266 ? 1.9862 1.4623 0.8808 0.4559  -0.0287 0.1980  281 SER B OG  
5000 N N   . GLY B 267 ? 2.0559 1.5208 0.9416 0.3528  0.0099  0.2013  282 GLY B N   
5001 C CA  . GLY B 267 ? 2.0135 1.4859 0.9298 0.3183  0.0265  0.1930  282 GLY B CA  
5002 C C   . GLY B 267 ? 2.0015 1.4651 0.9311 0.3347  0.0231  0.1876  282 GLY B C   
5003 O O   . GLY B 267 ? 2.0729 1.4664 0.9550 0.3382  0.0262  0.1937  282 GLY B O   
5004 N N   . GLY B 268 ? 1.8967 1.4296 0.8884 0.3447  0.0172  0.1760  283 GLY B N   
5005 C CA  . GLY B 268 ? 1.8789 1.4111 0.8856 0.3638  0.0130  0.1696  283 GLY B CA  
5006 C C   . GLY B 268 ? 1.7943 1.3722 0.8576 0.3401  0.0211  0.1572  283 GLY B C   
5007 O O   . GLY B 268 ? 1.7406 1.3563 0.8370 0.3114  0.0286  0.1530  283 GLY B O   
5008 N N   . ALA B 269 ? 1.7756 1.3487 0.8490 0.3527  0.0195  0.1511  284 ALA B N   
5009 C CA  . ALA B 269 ? 1.7109 1.3224 0.8332 0.3314  0.0258  0.1400  284 ALA B CA  
5010 C C   . ALA B 269 ? 1.6001 1.2977 0.7858 0.3344  0.0196  0.1307  284 ALA B C   
5011 O O   . ALA B 269 ? 1.5309 1.2666 0.7578 0.3083  0.0254  0.1239  284 ALA B O   
5012 C CB  . ALA B 269 ? 1.7472 1.3286 0.8590 0.3449  0.0257  0.1357  284 ALA B CB  
5013 N N   . ASP B 270 ? 1.5810 1.3076 0.7730 0.3661  0.0075  0.1304  285 ASP B N   
5014 C CA  . ASP B 270 ? 1.4887 1.2939 0.7379 0.3728  0.0010  0.1204  285 ASP B CA  
5015 C C   . ASP B 270 ? 1.4632 1.3055 0.7203 0.3795  -0.0063 0.1230  285 ASP B C   
5016 O O   . ASP B 270 ? 1.4030 1.3062 0.6990 0.3918  -0.0141 0.1156  285 ASP B O   
5017 C CB  . ASP B 270 ? 1.5027 1.3209 0.7612 0.4049  -0.0071 0.1139  285 ASP B CB  
5018 C CG  . ASP B 270 ? 1.5711 1.3298 0.7982 0.4082  -0.0016 0.1144  285 ASP B CG  
5019 O OD1 . ASP B 270 ? 1.5679 1.3049 0.7948 0.3788  0.0089  0.1133  285 ASP B OD1 
5020 O OD2 . ASP B 270 ? 1.6155 1.3498 0.8185 0.4410  -0.0081 0.1152  285 ASP B OD2 
5021 N N   . ASP B 271 ? 1.4928 1.2980 0.7113 0.3702  -0.0033 0.1330  286 ASP B N   
5022 C CA  . ASP B 271 ? 1.4650 1.2995 0.6845 0.3743  -0.0095 0.1359  286 ASP B CA  
5023 C C   . ASP B 271 ? 1.4024 1.2807 0.6618 0.3417  -0.0007 0.1299  286 ASP B C   
5024 O O   . ASP B 271 ? 1.3906 1.2502 0.6522 0.3126  0.0118  0.1295  286 ASP B O   
5025 C CB  . ASP B 271 ? 1.5222 1.2936 0.6771 0.3795  -0.0102 0.1497  286 ASP B CB  
5026 C CG  . ASP B 271 ? 1.5710 1.2979 0.6847 0.4155  -0.0209 0.1561  286 ASP B CG  
5027 O OD1 . ASP B 271 ? 1.5232 1.2868 0.6626 0.4436  -0.0320 0.1497  286 ASP B OD1 
5028 O OD2 . ASP B 271 ? 1.6684 1.3231 0.7238 0.4159  -0.0181 0.1672  286 ASP B OD2 
5029 N N   . ILE B 272 ? 1.3396 1.2765 0.6312 0.3466  -0.0074 0.1247  287 ILE B N   
5030 C CA  . ILE B 272 ? 1.2794 1.2577 0.6089 0.3179  0.0005  0.1184  287 ILE B CA  
5031 C C   . ILE B 272 ? 1.2968 1.2504 0.5949 0.3011  0.0075  0.1254  287 ILE B C   
5032 O O   . ILE B 272 ? 1.3566 1.3012 0.6238 0.3161  0.0001  0.1316  287 ILE B O   
5033 C CB  . ILE B 272 ? 1.2118 1.2638 0.5925 0.3247  -0.0072 0.1081  287 ILE B CB  
5034 C CG1 . ILE B 272 ? 1.2222 1.2928 0.5894 0.3513  -0.0208 0.1103  287 ILE B CG1 
5035 C CG2 . ILE B 272 ? 1.1861 1.2633 0.6016 0.3317  -0.0097 0.0998  287 ILE B CG2 
5036 C CD1 . ILE B 272 ? 1.1680 1.3102 0.5835 0.3511  -0.0263 0.0997  287 ILE B CD1 
5037 N N   . THR B 273 ? 1.2579 1.1994 0.5629 0.2696  0.0218  0.1239  288 THR B N   
5038 C CA  . THR B 273 ? 1.2494 1.1782 0.5360 0.2475  0.0320  0.1271  288 THR B CA  
5039 C C   . THR B 273 ? 1.1923 1.1792 0.5107 0.2457  0.0288  0.1204  288 THR B C   
5040 O O   . THR B 273 ? 1.1434 1.1776 0.4954 0.2618  0.0182  0.1140  288 THR B O   
5041 C CB  . THR B 273 ? 1.2470 1.1562 0.5413 0.2142  0.0483  0.1248  288 THR B CB  
5042 O OG1 . THR B 273 ? 1.3476 1.2272 0.6083 0.1944  0.0597  0.1298  288 THR B OG1 
5043 C CG2 . THR B 273 ? 1.1853 1.1500 0.5430 0.1970  0.0522  0.1129  288 THR B CG2 
5044 N N   . GLU B 274 ? 1.2010 1.1819 0.5054 0.2262  0.0385  0.1215  289 GLU B N   
5045 C CA  . GLU B 274 ? 1.1556 1.1857 0.4854 0.2220  0.0373  0.1147  289 GLU B CA  
5046 C C   . GLU B 274 ? 1.0652 1.1440 0.4564 0.2016  0.0449  0.1020  289 GLU B C   
5047 O O   . GLU B 274 ? 1.0182 1.1452 0.4414 0.2017  0.0417  0.0941  289 GLU B O   
5048 C CB  . GLU B 274 ? 1.2026 1.2054 0.4904 0.2086  0.0457  0.1201  289 GLU B CB  
5049 C CG  . GLU B 274 ? 1.2624 1.2347 0.4953 0.2324  0.0335  0.1313  289 GLU B CG  
5050 C CD  . GLU B 274 ? 1.3086 1.2565 0.4990 0.2173  0.0417  0.1362  289 GLU B CD  
5051 O OE1 . GLU B 274 ? 1.3075 1.2428 0.4980 0.1876  0.0599  0.1335  289 GLU B OE1 
5052 O OE2 . GLU B 274 ? 1.3210 1.2635 0.4779 0.2348  0.0300  0.1424  289 GLU B OE2 
5053 N N   . ASP B 275 ? 1.0336 1.0976 0.4389 0.1838  0.0546  0.1002  290 ASP B N   
5054 C CA  . ASP B 275 ? 0.9742 1.0802 0.4371 0.1681  0.0590  0.0893  290 ASP B CA  
5055 C C   . ASP B 275 ? 0.9351 1.0841 0.4340 0.1868  0.0455  0.0837  290 ASP B C   
5056 O O   . ASP B 275 ? 0.8956 1.0903 0.4371 0.1799  0.0453  0.0746  290 ASP B O   
5057 C CB  . ASP B 275 ? 0.9740 1.0549 0.4429 0.1501  0.0678  0.0894  290 ASP B CB  
5058 C CG  . ASP B 275 ? 1.0265 1.0715 0.4675 0.1260  0.0837  0.0924  290 ASP B CG  
5059 O OD1 . ASP B 275 ? 1.0538 1.1103 0.4937 0.1136  0.0922  0.0895  290 ASP B OD1 
5060 O OD2 . ASP B 275 ? 1.0487 1.0543 0.4697 0.1173  0.0887  0.0967  290 ASP B OD2 
5061 N N   . HIS B 276 ? 0.9418 1.0755 0.4224 0.2100  0.0350  0.0886  291 HIS B N   
5062 C CA  . HIS B 276 ? 0.9179 1.0914 0.4289 0.2282  0.0230  0.0830  291 HIS B CA  
5063 C C   . HIS B 276 ? 0.9054 1.1205 0.4267 0.2401  0.0147  0.0790  291 HIS B C   
5064 O O   . HIS B 276 ? 0.8652 1.1253 0.4235 0.2450  0.0086  0.0710  291 HIS B O   
5065 C CB  . HIS B 276 ? 0.9725 1.1182 0.4570 0.2522  0.0148  0.0887  291 HIS B CB  
5066 C CG  . HIS B 276 ? 1.0096 1.1189 0.4873 0.2436  0.0207  0.0909  291 HIS B CG  
5067 N ND1 . HIS B 276 ? 1.0631 1.1142 0.4962 0.2382  0.0273  0.0996  291 HIS B ND1 
5068 C CD2 . HIS B 276 ? 0.9875 1.1088 0.4947 0.2383  0.0208  0.0855  291 HIS B CD2 
5069 C CE1 . HIS B 276 ? 1.0848 1.1147 0.5216 0.2299  0.0312  0.0989  291 HIS B CE1 
5070 N NE2 . HIS B 276 ? 1.0280 1.0999 0.5091 0.2302  0.0270  0.0905  291 HIS B NE2 
5071 N N   . VAL B 277 ? 0.9493 1.1468 0.4342 0.2446  0.0142  0.0849  292 VAL B N   
5072 C CA  . VAL B 277 ? 0.9394 1.1726 0.4279 0.2537  0.0064  0.0816  292 VAL B CA  
5073 C C   . VAL B 277 ? 0.8655 1.1373 0.3933 0.2315  0.0143  0.0714  292 VAL B C   
5074 O O   . VAL B 277 ? 0.8350 1.1534 0.3954 0.2347  0.0083  0.0629  292 VAL B O   
5075 C CB  . VAL B 277 ? 1.0218 1.2201 0.4569 0.2592  0.0054  0.0911  292 VAL B CB  
5076 C CG1 . VAL B 277 ? 1.0300 1.2668 0.4681 0.2668  -0.0032 0.0870  292 VAL B CG1 
5077 C CG2 . VAL B 277 ? 1.0762 1.2278 0.4670 0.2821  -0.0024 0.1022  292 VAL B CG2 
5078 N N   . LEU B 278 ? 0.8410 1.0917 0.3647 0.2086  0.0283  0.0718  293 LEU B N   
5079 C CA  . LEU B 278 ? 0.7907 1.0712 0.3490 0.1873  0.0376  0.0621  293 LEU B CA  
5080 C C   . LEU B 278 ? 0.7371 1.0521 0.3479 0.1819  0.0362  0.0533  293 LEU B C   
5081 O O   . LEU B 278 ? 0.7000 1.0549 0.3422 0.1781  0.0346  0.0444  293 LEU B O   
5082 C CB  . LEU B 278 ? 0.8153 1.0634 0.3585 0.1653  0.0534  0.0643  293 LEU B CB  
5083 C CG  . LEU B 278 ? 0.7908 1.0640 0.3635 0.1433  0.0654  0.0543  293 LEU B CG  
5084 C CD1 . LEU B 278 ? 0.7990 1.0949 0.3633 0.1468  0.0631  0.0504  293 LEU B CD1 
5085 C CD2 . LEU B 278 ? 0.8256 1.0640 0.3791 0.1230  0.0813  0.0570  293 LEU B CD2 
5086 N N   . MET B 279 ? 0.7303 1.0270 0.3477 0.1807  0.0368  0.0560  294 MET B N   
5087 C CA  . MET B 279 ? 0.6857 1.0089 0.3474 0.1761  0.0341  0.0492  294 MET B CA  
5088 C C   . MET B 279 ? 0.6517 1.0109 0.3314 0.1923  0.0222  0.0448  294 MET B C   
5089 O O   . MET B 279 ? 0.5944 0.9856 0.3121 0.1852  0.0208  0.0370  294 MET B O   
5090 C CB  . MET B 279 ? 0.6960 0.9886 0.3528 0.1737  0.0355  0.0538  294 MET B CB  
5091 C CG  . MET B 279 ? 0.7044 0.9678 0.3538 0.1530  0.0479  0.0560  294 MET B CG  
5092 S SD  . MET B 279 ? 0.6602 0.9559 0.3508 0.1302  0.0576  0.0459  294 MET B SD  
5093 C CE  . MET B 279 ? 0.6995 0.9901 0.3590 0.1291  0.0645  0.0469  294 MET B CE  
5094 N N   . THR B 280 ? 0.6828 1.0366 0.3351 0.2137  0.0135  0.0495  295 THR B N   
5095 C CA  . THR B 280 ? 0.6808 1.0734 0.3495 0.2292  0.0025  0.0442  295 THR B CA  
5096 C C   . THR B 280 ? 0.6531 1.0821 0.3348 0.2245  0.0013  0.0373  295 THR B C   
5097 O O   . THR B 280 ? 0.5888 1.0575 0.3019 0.2230  -0.0028 0.0287  295 THR B O   
5098 C CB  . THR B 280 ? 0.7311 1.1090 0.3686 0.2557  -0.0071 0.0505  295 THR B CB  
5099 O OG1 . THR B 280 ? 0.7640 1.0984 0.3814 0.2583  -0.0040 0.0575  295 THR B OG1 
5100 C CG2 . THR B 280 ? 0.7131 1.1336 0.3750 0.2705  -0.0172 0.0434  295 THR B CG2 
5101 N N   . ALA B 281 ? 0.6878 1.1012 0.3430 0.2207  0.0054  0.0407  296 ALA B N   
5102 C CA  . ALA B 281 ? 0.6888 1.1318 0.3527 0.2133  0.0061  0.0337  296 ALA B CA  
5103 C C   . ALA B 281 ? 0.6406 1.1063 0.3466 0.1930  0.0139  0.0240  296 ALA B C   
5104 O O   . ALA B 281 ? 0.6215 1.1239 0.3515 0.1904  0.0105  0.0152  296 ALA B O   
5105 C CB  . ALA B 281 ? 0.7230 1.1388 0.3488 0.2086  0.0121  0.0391  296 ALA B CB  
5106 N N   . ALA B 282 ? 0.6258 1.0689 0.3400 0.1787  0.0237  0.0255  297 ALA B N   
5107 C CA  . ALA B 282 ? 0.6053 1.0666 0.3602 0.1619  0.0294  0.0171  297 ALA B CA  
5108 C C   . ALA B 282 ? 0.5774 1.0647 0.3625 0.1665  0.0209  0.0128  297 ALA B C   
5109 O O   . ALA B 282 ? 0.5502 1.0668 0.3628 0.1598  0.0199  0.0042  297 ALA B O   
5110 C CB  . ALA B 282 ? 0.6109 1.0441 0.3690 0.1480  0.0395  0.0201  297 ALA B CB  
5111 N N   . GLU B 283 ? 0.5876 1.0623 0.3651 0.1775  0.0152  0.0182  298 GLU B N   
5112 C CA  . GLU B 283 ? 0.5827 1.0794 0.3856 0.1803  0.0085  0.0141  298 GLU B CA  
5113 C C   . GLU B 283 ? 0.5858 1.1226 0.4008 0.1869  0.0013  0.0068  298 GLU B C   
5114 O O   . GLU B 283 ? 0.5505 1.1091 0.3907 0.1831  -0.0020 0.0012  298 GLU B O   
5115 C CB  . GLU B 283 ? 0.5898 1.0663 0.3764 0.1935  0.0041  0.0205  298 GLU B CB  
5116 C CG  . GLU B 283 ? 0.5525 1.0412 0.3635 0.1909  0.0006  0.0170  298 GLU B CG  
5117 C CD  . GLU B 283 ? 0.5649 1.0191 0.3636 0.1913  0.0024  0.0233  298 GLU B CD  
5118 O OE1 . GLU B 283 ? 0.6053 1.0381 0.3751 0.2066  0.0004  0.0290  298 GLU B OE1 
5119 O OE2 . GLU B 283 ? 0.5313 0.9781 0.3478 0.1765  0.0053  0.0227  298 GLU B OE2 
5120 N N   . ALA B 284 ? 0.5944 1.1399 0.3896 0.1959  -0.0016 0.0069  299 ALA B N   
5121 C CA  . ALA B 284 ? 0.5856 1.1706 0.3904 0.2012  -0.0087 -0.0005 299 ALA B CA  
5122 C C   . ALA B 284 ? 0.5560 1.1620 0.3866 0.1831  -0.0041 -0.0098 299 ALA B C   
5123 O O   . ALA B 284 ? 0.5298 1.1689 0.3777 0.1812  -0.0085 -0.0178 299 ALA B O   
5124 C CB  . ALA B 284 ? 0.6297 1.2156 0.4037 0.2156  -0.0141 0.0028  299 ALA B CB  
5125 N N   . PHE B 285 ? 0.5658 1.1528 0.3985 0.1695  0.0053  -0.0095 300 PHE B N   
5126 C CA  . PHE B 285 ? 0.5785 1.1809 0.4387 0.1530  0.0103  -0.0186 300 PHE B CA  
5127 C C   . PHE B 285 ? 0.5617 1.1600 0.4492 0.1449  0.0108  -0.0193 300 PHE B C   
5128 O O   . PHE B 285 ? 0.5543 1.1732 0.4641 0.1385  0.0080  -0.0261 300 PHE B O   
5129 C CB  . PHE B 285 ? 0.6046 1.1920 0.4584 0.1424  0.0208  -0.0198 300 PHE B CB  
5130 C CG  . PHE B 285 ? 0.6363 1.2301 0.4641 0.1468  0.0205  -0.0208 300 PHE B CG  
5131 C CD1 . PHE B 285 ? 0.6326 1.2546 0.4689 0.1417  0.0190  -0.0306 300 PHE B CD1 
5132 C CD2 . PHE B 285 ? 0.6758 1.2454 0.4680 0.1553  0.0211  -0.0120 300 PHE B CD2 
5133 C CE1 . PHE B 285 ? 0.6529 1.2813 0.4635 0.1450  0.0177  -0.0317 300 PHE B CE1 
5134 C CE2 . PHE B 285 ? 0.6965 1.2704 0.4614 0.1594  0.0194  -0.0122 300 PHE B CE2 
5135 C CZ  . PHE B 285 ? 0.6916 1.2961 0.4662 0.1543  0.0174  -0.0222 300 PHE B CZ  
5136 N N   . GLY B 286 ? 0.5693 1.1395 0.4529 0.1441  0.0140  -0.0123 301 GLY B N   
5137 C CA  . GLY B 286 ? 0.5501 1.1134 0.4562 0.1367  0.0132  -0.0118 301 GLY B CA  
5138 C C   . GLY B 286 ? 0.5194 1.1023 0.4359 0.1405  0.0051  -0.0144 301 GLY B C   
5139 O O   . GLY B 286 ? 0.5085 1.1055 0.4478 0.1308  0.0039  -0.0203 301 GLY B O   
5140 N N   . ALA B 287 ? 0.5110 1.0945 0.4097 0.1547  0.0001  -0.0104 302 ALA B N   
5141 C CA  . ALA B 287 ? 0.4994 1.1023 0.4067 0.1588  -0.0062 -0.0134 302 ALA B CA  
5142 C C   . ALA B 287 ? 0.4886 1.1284 0.4023 0.1602  -0.0098 -0.0217 302 ALA B C   
5143 O O   . ALA B 287 ? 0.5184 1.1779 0.4436 0.1587  -0.0133 -0.0263 302 ALA B O   
5144 C CB  . ALA B 287 ? 0.5022 1.0923 0.3898 0.1745  -0.0093 -0.0074 302 ALA B CB  
5145 N N   . GLY B 288 ? 0.4592 1.1088 0.3644 0.1618  -0.0088 -0.0242 303 GLY B N   
5146 C CA  . GLY B 288 ? 0.4434 1.1292 0.3510 0.1646  -0.0134 -0.0320 303 GLY B CA  
5147 C C   . GLY B 288 ? 0.4240 1.1262 0.3505 0.1477  -0.0107 -0.0411 303 GLY B C   
5148 O O   . GLY B 288 ? 0.4076 1.1360 0.3468 0.1424  -0.0137 -0.0484 303 GLY B O   
5149 N N   . VAL B 289 ? 0.4498 1.1356 0.3771 0.1389  -0.0042 -0.0413 304 VAL B N   
5150 C CA  . VAL B 289 ? 0.4304 1.1253 0.3747 0.1234  -0.0005 -0.0501 304 VAL B CA  
5151 C C   . VAL B 289 ? 0.4198 1.1045 0.3841 0.1149  -0.0007 -0.0495 304 VAL B C   
5152 O O   . VAL B 289 ? 0.4775 1.1423 0.4405 0.1190  -0.0012 -0.0419 304 VAL B O   
5153 C CB  . VAL B 289 ? 0.4232 1.1006 0.3638 0.1176  0.0079  -0.0506 304 VAL B CB  
5154 C CG1 . VAL B 289 ? 0.4155 1.1009 0.3738 0.1030  0.0122  -0.0609 304 VAL B CG1 
5155 C CG2 . VAL B 289 ? 0.4470 1.1266 0.3605 0.1267  0.0081  -0.0485 304 VAL B CG2 
5156 N N   . GLU B 290 ? 0.3989 1.0945 0.3795 0.1025  -0.0007 -0.0571 305 GLU B N   
5157 C CA  . GLU B 290 ? 0.3890 1.0698 0.3862 0.0937  -0.0017 -0.0556 305 GLU B CA  
5158 C C   . GLU B 290 ? 0.3328 1.0264 0.3304 0.0940  -0.0073 -0.0554 305 GLU B C   
5159 O O   . GLU B 290 ? 0.2896 0.9901 0.2971 0.0826  -0.0086 -0.0607 305 GLU B O   
5160 C CB  . GLU B 290 ? 0.4150 1.0666 0.4145 0.0962  0.0005  -0.0473 305 GLU B CB  
5161 C CG  . GLU B 290 ? 0.4417 1.0778 0.4620 0.0852  0.0007  -0.0483 305 GLU B CG  
5162 C CD  . GLU B 290 ? 0.4461 1.0775 0.4765 0.0798  0.0072  -0.0538 305 GLU B CD  
5163 O OE1 . GLU B 290 ? 0.4932 1.1250 0.5125 0.0847  0.0127  -0.0537 305 GLU B OE1 
5164 O OE2 . GLU B 290 ? 0.4916 1.1170 0.5396 0.0712  0.0069  -0.0582 305 GLU B OE2 
5165 N N   . THR B 291 ? 0.3209 1.0171 0.3064 0.1068  -0.0099 -0.0501 306 THR B N   
5166 C CA  . THR B 291 ? 0.3205 1.0361 0.3054 0.1086  -0.0139 -0.0523 306 THR B CA  
5167 C C   . THR B 291 ? 0.3200 1.0716 0.3080 0.1039  -0.0150 -0.0626 306 THR B C   
5168 O O   . THR B 291 ? 0.3152 1.0807 0.3113 0.0927  -0.0157 -0.0683 306 THR B O   
5169 C CB  . THR B 291 ? 0.3337 1.0485 0.3038 0.1265  -0.0160 -0.0464 306 THR B CB  
5170 O OG1 . THR B 291 ? 0.3433 1.0514 0.2999 0.1369  -0.0148 -0.0430 306 THR B OG1 
5171 C CG2 . THR B 291 ? 0.3318 1.0172 0.3001 0.1272  -0.0159 -0.0385 306 THR B CG2 
5172 N N   . THR B 292 ? 0.3224 1.0882 0.3022 0.1109  -0.0152 -0.0651 307 THR B N   
5173 C CA  . THR B 292 ? 0.3317 1.1339 0.3131 0.1074  -0.0173 -0.0749 307 THR B CA  
5174 C C   . THR B 292 ? 0.3263 1.1272 0.3173 0.0883  -0.0137 -0.0826 307 THR B C   
5175 O O   . THR B 292 ? 0.3350 1.1575 0.3331 0.0761  -0.0143 -0.0912 307 THR B O   
5176 C CB  . THR B 292 ? 0.3480 1.1651 0.3144 0.1226  -0.0205 -0.0743 307 THR B CB  
5177 O OG1 . THR B 292 ? 0.4381 1.2326 0.3968 0.1208  -0.0163 -0.0716 307 THR B OG1 
5178 C CG2 . THR B 292 ? 0.3420 1.1538 0.2970 0.1426  -0.0242 -0.0662 307 THR B CG2 
5179 N N   . SER B 293 ? 0.3110 1.0862 0.3021 0.0853  -0.0093 -0.0803 308 SER B N   
5180 C CA  . SER B 293 ? 0.3031 1.0726 0.3027 0.0695  -0.0053 -0.0879 308 SER B CA  
5181 C C   . SER B 293 ? 0.2776 1.0390 0.2890 0.0568  -0.0061 -0.0891 308 SER B C   
5182 O O   . SER B 293 ? 0.2643 1.0367 0.2795 0.0430  -0.0056 -0.0976 308 SER B O   
5183 C CB  . SER B 293 ? 0.3147 1.0555 0.3159 0.0702  0.0004  -0.0845 308 SER B CB  
5184 O OG  . SER B 293 ? 0.3290 1.0617 0.3177 0.0847  0.0006  -0.0762 308 SER B OG  
5185 N N   . THR B 294 ? 0.2669 1.0072 0.2813 0.0609  -0.0076 -0.0804 309 THR B N   
5186 C CA  . THR B 294 ? 0.2622 0.9887 0.2844 0.0494  -0.0093 -0.0796 309 THR B CA  
5187 C C   . THR B 294 ? 0.2416 0.9941 0.2611 0.0422  -0.0111 -0.0853 309 THR B C   
5188 O O   . THR B 294 ? 0.2192 0.9697 0.2419 0.0261  -0.0106 -0.0906 309 THR B O   
5189 C CB  . THR B 294 ? 0.2626 0.9623 0.2864 0.0555  -0.0114 -0.0688 309 THR B CB  
5190 O OG1 . THR B 294 ? 0.2847 0.9624 0.3141 0.0593  -0.0089 -0.0653 309 THR B OG1 
5191 C CG2 . THR B 294 ? 0.2579 0.9416 0.2862 0.0433  -0.0145 -0.0673 309 THR B CG2 
5192 N N   . THR B 295 ? 0.2416 1.0180 0.2551 0.0541  -0.0129 -0.0845 310 THR B N   
5193 C CA  . THR B 295 ? 0.2626 1.0708 0.2761 0.0488  -0.0138 -0.0914 310 THR B CA  
5194 C C   . THR B 295 ? 0.2720 1.1058 0.2876 0.0359  -0.0125 -0.1032 310 THR B C   
5195 O O   . THR B 295 ? 0.2931 1.1405 0.3112 0.0200  -0.0113 -0.1103 310 THR B O   
5196 C CB  . THR B 295 ? 0.2795 1.1117 0.2879 0.0676  -0.0163 -0.0898 310 THR B CB  
5197 O OG1 . THR B 295 ? 0.2906 1.0956 0.2943 0.0789  -0.0169 -0.0792 310 THR B OG1 
5198 C CG2 . THR B 295 ? 0.2896 1.1593 0.3018 0.0624  -0.0164 -0.0984 310 THR B CG2 
5199 N N   . LEU B 296 ? 0.2632 1.1023 0.2760 0.0414  -0.0122 -0.1054 311 LEU B N   
5200 C CA  . LEU B 296 ? 0.2692 1.1290 0.2822 0.0289  -0.0110 -0.1166 311 LEU B CA  
5201 C C   . LEU B 296 ? 0.2703 1.1054 0.2870 0.0089  -0.0073 -0.1205 311 LEU B C   
5202 O O   . LEU B 296 ? 0.2848 1.1358 0.3017 -0.0078 -0.0061 -0.1301 311 LEU B O   
5203 C CB  . LEU B 296 ? 0.2766 1.1417 0.2824 0.0389  -0.0113 -0.1175 311 LEU B CB  
5204 C CG  . LEU B 296 ? 0.2804 1.1762 0.2795 0.0573  -0.0168 -0.1159 311 LEU B CG  
5205 C CD1 . LEU B 296 ? 0.2992 1.1902 0.2862 0.0677  -0.0173 -0.1138 311 LEU B CD1 
5206 C CD2 . LEU B 296 ? 0.2809 1.2235 0.2841 0.0514  -0.0202 -0.1267 311 LEU B CD2 
5207 N N   . LEU B 297 ? 0.2656 1.0619 0.2851 0.0105  -0.0058 -0.1135 312 LEU B N   
5208 C CA  . LEU B 297 ? 0.2657 1.0333 0.2889 -0.0054 -0.0038 -0.1158 312 LEU B CA  
5209 C C   . LEU B 297 ? 0.2585 1.0222 0.2804 -0.0182 -0.0054 -0.1152 312 LEU B C   
5210 O O   . LEU B 297 ? 0.2644 1.0243 0.2835 -0.0361 -0.0037 -0.1222 312 LEU B O   
5211 C CB  . LEU B 297 ? 0.2710 1.0016 0.3006 0.0017  -0.0032 -0.1079 312 LEU B CB  
5212 C CG  . LEU B 297 ? 0.2823 1.0054 0.3141 0.0053  0.0014  -0.1118 312 LEU B CG  
5213 C CD1 . LEU B 297 ? 0.2779 0.9828 0.3147 0.0199  0.0021  -0.1027 312 LEU B CD1 
5214 C CD2 . LEU B 297 ? 0.3020 1.0029 0.3380 -0.0089 0.0040  -0.1187 312 LEU B CD2 
5215 N N   . TRP B 298 ? 0.2492 1.0110 0.2707 -0.0105 -0.0081 -0.1071 313 TRP B N   
5216 C CA  . TRP B 298 ? 0.2694 1.0296 0.2867 -0.0242 -0.0086 -0.1073 313 TRP B CA  
5217 C C   . TRP B 298 ? 0.2774 1.0743 0.2917 -0.0385 -0.0058 -0.1193 313 TRP B C   
5218 O O   . TRP B 298 ? 0.2912 1.0791 0.3002 -0.0590 -0.0039 -0.1241 313 TRP B O   
5219 C CB  . TRP B 298 ? 0.2592 1.0201 0.2747 -0.0132 -0.0108 -0.0991 313 TRP B CB  
5220 C CG  . TRP B 298 ? 0.2604 0.9813 0.2766 -0.0078 -0.0142 -0.0877 313 TRP B CG  
5221 C CD1 . TRP B 298 ? 0.2480 0.9605 0.2659 0.0095  -0.0161 -0.0792 313 TRP B CD1 
5222 C CD2 . TRP B 298 ? 0.2722 0.9562 0.2869 -0.0199 -0.0169 -0.0835 313 TRP B CD2 
5223 N NE1 . TRP B 298 ? 0.2552 0.9316 0.2745 0.0081  -0.0196 -0.0708 313 TRP B NE1 
5224 C CE2 . TRP B 298 ? 0.2746 0.9330 0.2923 -0.0088 -0.0210 -0.0729 313 TRP B CE2 
5225 C CE3 . TRP B 298 ? 0.2961 0.9646 0.3056 -0.0390 -0.0168 -0.0875 313 TRP B CE3 
5226 C CZ2 . TRP B 298 ? 0.2900 0.9106 0.3081 -0.0151 -0.0263 -0.0662 313 TRP B CZ2 
5227 C CZ3 . TRP B 298 ? 0.3138 0.9404 0.3210 -0.0446 -0.0221 -0.0801 313 TRP B CZ3 
5228 C CH2 . TRP B 298 ? 0.3050 0.9100 0.3177 -0.0320 -0.0273 -0.0696 313 TRP B CH2 
5229 N N   . THR B 299 ? 0.2660 1.1037 0.2831 -0.0281 -0.0060 -0.1243 314 THR B N   
5230 C CA  . THR B 299 ? 0.2839 1.1630 0.3014 -0.0408 -0.0040 -0.1367 314 THR B CA  
5231 C C   . THR B 299 ? 0.3058 1.1764 0.3194 -0.0630 -0.0010 -0.1457 314 THR B C   
5232 O O   . THR B 299 ? 0.3190 1.1929 0.3282 -0.0839 0.0021  -0.1519 314 THR B O   
5233 C CB  . THR B 299 ? 0.2775 1.2006 0.2993 -0.0249 -0.0066 -0.1414 314 THR B CB  
5234 O OG1 . THR B 299 ? 0.2651 1.1899 0.2880 -0.0021 -0.0096 -0.1324 314 THR B OG1 
5235 C CG2 . THR B 299 ? 0.2782 1.2502 0.3040 -0.0378 -0.0053 -0.1547 314 THR B CG2 
5236 N N   . ILE B 300 ? 0.3203 1.1776 0.3338 -0.0589 -0.0010 -0.1465 315 ILE B N   
5237 C CA  . ILE B 300 ? 0.3456 1.1922 0.3542 -0.0781 0.0023  -0.1558 315 ILE B CA  
5238 C C   . ILE B 300 ? 0.3603 1.1618 0.3632 -0.0933 0.0037  -0.1524 315 ILE B C   
5239 O O   . ILE B 300 ? 0.3873 1.1848 0.3824 -0.1155 0.0068  -0.1606 315 ILE B O   
5240 C CB  . ILE B 300 ? 0.3603 1.1997 0.3692 -0.0690 0.0028  -0.1575 315 ILE B CB  
5241 C CG1 . ILE B 300 ? 0.3676 1.2553 0.3767 -0.0614 0.0007  -0.1643 315 ILE B CG1 
5242 C CG2 . ILE B 300 ? 0.3802 1.1934 0.3835 -0.0873 0.0070  -0.1654 315 ILE B CG2 
5243 C CD1 . ILE B 300 ? 0.3797 1.2626 0.3860 -0.0483 0.0008  -0.1635 315 ILE B CD1 
5244 N N   . ALA B 301 ? 0.3530 1.1201 0.3584 -0.0821 0.0010  -0.1402 316 ALA B N   
5245 C CA  . ALA B 301 ? 0.3656 1.0887 0.3647 -0.0943 0.0000  -0.1354 316 ALA B CA  
5246 C C   . ALA B 301 ? 0.3829 1.1151 0.3716 -0.1139 0.0017  -0.1387 316 ALA B C   
5247 O O   . ALA B 301 ? 0.4003 1.1061 0.3778 -0.1334 0.0031  -0.1417 316 ALA B O   
5248 C CB  . ALA B 301 ? 0.3540 1.0465 0.3585 -0.0784 -0.0048 -0.1217 316 ALA B CB  
5249 N N   . PHE B 302 ? 0.3817 1.1498 0.3730 -0.1091 0.0020  -0.1388 317 PHE B N   
5250 C CA  . PHE B 302 ? 0.4010 1.1821 0.3833 -0.1284 0.0054  -0.1431 317 PHE B CA  
5251 C C   . PHE B 302 ? 0.4190 1.2324 0.3986 -0.1489 0.0106  -0.1584 317 PHE B C   
5252 O O   . PHE B 302 ? 0.4386 1.2448 0.4059 -0.1738 0.0147  -0.1637 317 PHE B O   
5253 C CB  . PHE B 302 ? 0.3805 1.1899 0.3679 -0.1161 0.0051  -0.1396 317 PHE B CB  
5254 C CG  . PHE B 302 ? 0.3855 1.1580 0.3684 -0.1075 0.0013  -0.1261 317 PHE B CG  
5255 C CD1 . PHE B 302 ? 0.4082 1.1477 0.3760 -0.1254 0.0015  -0.1221 317 PHE B CD1 
5256 C CD2 . PHE B 302 ? 0.3826 1.1505 0.3739 -0.0827 -0.0028 -0.1171 317 PHE B CD2 
5257 C CE1 . PHE B 302 ? 0.3999 1.1050 0.3623 -0.1181 -0.0033 -0.1096 317 PHE B CE1 
5258 C CE2 . PHE B 302 ? 0.3700 1.1038 0.3569 -0.0763 -0.0068 -0.1051 317 PHE B CE2 
5259 C CZ  . PHE B 302 ? 0.3820 1.0858 0.3550 -0.0937 -0.0075 -0.1015 317 PHE B CZ  
5260 N N   . LEU B 303 ? 0.4172 1.2645 0.4063 -0.1400 0.0103  -0.1656 318 LEU B N   
5261 C CA  . LEU B 303 ? 0.4349 1.3152 0.4220 -0.1598 0.0143  -0.1807 318 LEU B CA  
5262 C C   . LEU B 303 ? 0.4666 1.3074 0.4409 -0.1795 0.0169  -0.1849 318 LEU B C   
5263 O O   . LEU B 303 ? 0.5106 1.3646 0.4770 -0.2041 0.0215  -0.1966 318 LEU B O   
5264 C CB  . LEU B 303 ? 0.4114 1.3420 0.4104 -0.1451 0.0119  -0.1875 318 LEU B CB  
5265 C CG  . LEU B 303 ? 0.3995 1.3746 0.4100 -0.1290 0.0098  -0.1864 318 LEU B CG  
5266 C CD1 . LEU B 303 ? 0.3991 1.4190 0.4195 -0.1115 0.0052  -0.1914 318 LEU B CD1 
5267 C CD2 . LEU B 303 ? 0.4071 1.4126 0.4180 -0.1488 0.0149  -0.1951 318 LEU B CD2 
5268 N N   . LEU B 304 ? 0.4516 1.2440 0.4240 -0.1694 0.0143  -0.1761 319 LEU B N   
5269 C CA  . LEU B 304 ? 0.4813 1.2285 0.4408 -0.1861 0.0163  -0.1790 319 LEU B CA  
5270 C C   . LEU B 304 ? 0.5085 1.2268 0.4513 -0.2081 0.0179  -0.1767 319 LEU B C   
5271 O O   . LEU B 304 ? 0.5435 1.2466 0.4713 -0.2326 0.0221  -0.1852 319 LEU B O   
5272 C CB  . LEU B 304 ? 0.4950 1.1995 0.4595 -0.1683 0.0131  -0.1707 319 LEU B CB  
5273 C CG  . LEU B 304 ? 0.5078 1.2190 0.4770 -0.1623 0.0154  -0.1789 319 LEU B CG  
5274 C CD1 . LEU B 304 ? 0.4980 1.2615 0.4780 -0.1472 0.0144  -0.1813 319 LEU B CD1 
5275 C CD2 . LEU B 304 ? 0.5101 1.1781 0.4848 -0.1477 0.0140  -0.1728 319 LEU B CD2 
5276 N N   . HIS B 305 ? 0.4945 1.2044 0.4375 -0.2006 0.0149  -0.1656 320 HIS B N   
5277 C CA  . HIS B 305 ? 0.5246 1.2059 0.4487 -0.2209 0.0160  -0.1617 320 HIS B CA  
5278 C C   . HIS B 305 ? 0.5479 1.2701 0.4656 -0.2440 0.0233  -0.1727 320 HIS B C   
5279 O O   . HIS B 305 ? 0.5832 1.2821 0.4803 -0.2695 0.0270  -0.1742 320 HIS B O   
5280 C CB  . HIS B 305 ? 0.5143 1.1741 0.4392 -0.2058 0.0102  -0.1466 320 HIS B CB  
5281 C CG  . HIS B 305 ? 0.5158 1.1212 0.4401 -0.1933 0.0028  -0.1353 320 HIS B CG  
5282 N ND1 . HIS B 305 ? 0.5479 1.0991 0.4527 -0.2068 -0.0006 -0.1293 320 HIS B ND1 
5283 C CD2 . HIS B 305 ? 0.4903 1.0882 0.4314 -0.1688 -0.0019 -0.1296 320 HIS B CD2 
5284 C CE1 . HIS B 305 ? 0.5496 1.0647 0.4620 -0.1895 -0.0080 -0.1207 320 HIS B CE1 
5285 N NE2 . HIS B 305 ? 0.5181 1.0618 0.4532 -0.1672 -0.0081 -0.1212 320 HIS B NE2 
5286 N N   . HIS B 306 ? 0.5337 1.3169 0.4686 -0.2354 0.0253  -0.1806 321 HIS B N   
5287 C CA  . HIS B 306 ? 0.5434 1.3740 0.4780 -0.2545 0.0321  -0.1923 321 HIS B CA  
5288 C C   . HIS B 306 ? 0.5774 1.4546 0.5212 -0.2619 0.0346  -0.2079 321 HIS B C   
5289 O O   . HIS B 306 ? 0.5638 1.4979 0.5260 -0.2486 0.0336  -0.2139 321 HIS B O   
5290 C CB  . HIS B 306 ? 0.5062 1.3684 0.4526 -0.2377 0.0315  -0.1875 321 HIS B CB  
5291 C CG  . HIS B 306 ? 0.5172 1.3346 0.4491 -0.2391 0.0303  -0.1747 321 HIS B CG  
5292 N ND1 . HIS B 306 ? 0.4912 1.2917 0.4295 -0.2134 0.0241  -0.1613 321 HIS B ND1 
5293 C CD2 . HIS B 306 ? 0.5514 1.3345 0.4600 -0.2645 0.0341  -0.1729 321 HIS B CD2 
5294 C CE1 . HIS B 306 ? 0.5038 1.2644 0.4246 -0.2224 0.0235  -0.1523 321 HIS B CE1 
5295 N NE2 . HIS B 306 ? 0.5358 1.2840 0.4375 -0.2530 0.0293  -0.1586 321 HIS B NE2 
5296 N N   . PRO B 307 ? 0.6265 1.4778 0.5558 -0.2837 0.0375  -0.2150 322 PRO B N   
5297 C CA  . PRO B 307 ? 0.6304 1.5201 0.5660 -0.2915 0.0391  -0.2298 322 PRO B CA  
5298 C C   . PRO B 307 ? 0.6626 1.6195 0.6071 -0.3070 0.0439  -0.2439 322 PRO B C   
5299 O O   . PRO B 307 ? 0.6971 1.7062 0.6576 -0.2984 0.0413  -0.2529 322 PRO B O   
5300 C CB  . PRO B 307 ? 0.6594 1.4990 0.5725 -0.3163 0.0427  -0.2344 322 PRO B CB  
5301 C CG  . PRO B 307 ? 0.6814 1.4539 0.5786 -0.3157 0.0410  -0.2202 322 PRO B CG  
5302 C CD  . PRO B 307 ? 0.6631 1.4492 0.5671 -0.3042 0.0393  -0.2105 322 PRO B CD  
5303 N N   . GLN B 308 ? 0.6892 1.6459 0.6231 -0.3306 0.0507  -0.2466 323 GLN B N   
5304 C CA  . GLN B 308 ? 0.7058 1.7311 0.6512 -0.3463 0.0566  -0.2613 323 GLN B CA  
5305 C C   . GLN B 308 ? 0.6571 1.7424 0.6311 -0.3152 0.0514  -0.2610 323 GLN B C   
5306 O O   . GLN B 308 ? 0.6497 1.7999 0.6415 -0.3152 0.0508  -0.2742 323 GLN B O   
5307 C CB  . GLN B 308 ? 0.7355 1.7469 0.6636 -0.3750 0.0660  -0.2626 323 GLN B CB  
5308 C CG  . GLN B 308 ? 0.7580 1.7519 0.6851 -0.3600 0.0656  -0.2491 323 GLN B CG  
5309 C CD  . GLN B 308 ? 0.7686 1.6906 0.6833 -0.3410 0.0579  -0.2298 323 GLN B CD  
5310 O OE1 . GLN B 308 ? 0.8012 1.6748 0.7029 -0.3445 0.0547  -0.2260 323 GLN B OE1 
5311 N NE2 . GLN B 308 ? 0.7668 1.6833 0.6866 -0.3206 0.0551  -0.2184 323 GLN B NE2 
5312 N N   . LEU B 309 ? 0.6359 1.6963 0.6131 -0.2879 0.0466  -0.2456 324 LEU B N   
5313 C CA  . LEU B 309 ? 0.6162 1.7195 0.6158 -0.2563 0.0415  -0.2427 324 LEU B CA  
5314 C C   . LEU B 309 ? 0.5935 1.7177 0.6061 -0.2319 0.0327  -0.2430 324 LEU B C   
5315 O O   . LEU B 309 ? 0.5697 1.7482 0.6012 -0.2130 0.0285  -0.2474 324 LEU B O   
5316 C CB  . LEU B 309 ? 0.6287 1.6885 0.6227 -0.2379 0.0394  -0.2257 324 LEU B CB  
5317 C CG  . LEU B 309 ? 0.6346 1.7260 0.6457 -0.2081 0.0361  -0.2209 324 LEU B CG  
5318 C CD1 . LEU B 309 ? 0.6487 1.8044 0.6734 -0.2165 0.0423  -0.2348 324 LEU B CD1 
5319 C CD2 . LEU B 309 ? 0.6742 1.7124 0.6734 -0.1989 0.0353  -0.2049 324 LEU B CD2 
5320 N N   . GLN B 310 ? 0.5834 1.6630 0.5848 -0.2317 0.0299  -0.2382 325 GLN B N   
5321 C CA  . GLN B 310 ? 0.5540 1.6510 0.5624 -0.2158 0.0235  -0.2408 325 GLN B CA  
5322 C C   . GLN B 310 ? 0.5593 1.7214 0.5770 -0.2305 0.0238  -0.2590 325 GLN B C   
5323 O O   . GLN B 310 ? 0.5497 1.7625 0.5834 -0.2111 0.0174  -0.2624 325 GLN B O   
5324 C CB  . GLN B 310 ? 0.5583 1.5968 0.5514 -0.2207 0.0235  -0.2365 325 GLN B CB  
5325 C CG  . GLN B 310 ? 0.5564 1.6055 0.5537 -0.2038 0.0180  -0.2380 325 GLN B CG  
5326 C CD  . GLN B 310 ? 0.5733 1.5638 0.5583 -0.2030 0.0188  -0.2329 325 GLN B CD  
5327 O OE1 . GLN B 310 ? 0.5627 1.5569 0.5488 -0.1900 0.0157  -0.2338 325 GLN B OE1 
5328 N NE2 . GLN B 310 ? 0.5895 1.5261 0.5624 -0.2165 0.0229  -0.2279 325 GLN B NE2 
5329 N N   . GLU B 311 ? 0.5722 1.7327 0.5793 -0.2651 0.0308  -0.2706 326 GLU B N   
5330 C CA  . GLU B 311 ? 0.5712 1.7945 0.5871 -0.2842 0.0319  -0.2893 326 GLU B CA  
5331 C C   . GLU B 311 ? 0.5252 1.8210 0.5658 -0.2708 0.0294  -0.2953 326 GLU B C   
5332 O O   . GLU B 311 ? 0.4895 1.8431 0.5451 -0.2645 0.0232  -0.3056 326 GLU B O   
5333 C CB  . GLU B 311 ? 0.6219 1.8300 0.6214 -0.3260 0.0422  -0.2998 326 GLU B CB  
5334 C CG  . GLU B 311 ? 0.6638 1.8111 0.6396 -0.3425 0.0444  -0.2993 326 GLU B CG  
5335 C CD  . GLU B 311 ? 0.7274 1.8246 0.6796 -0.3742 0.0538  -0.2991 326 GLU B CD  
5336 O OE1 . GLU B 311 ? 0.7739 1.8928 0.7191 -0.4080 0.0610  -0.3137 326 GLU B OE1 
5337 O OE2 . GLU B 311 ? 0.7526 1.7882 0.6925 -0.3656 0.0537  -0.2841 326 GLU B OE2 
5338 N N   . ARG B 312 ? 0.5122 1.8047 0.5568 -0.2659 0.0337  -0.2892 327 ARG B N   
5339 C CA  . ARG B 312 ? 0.5066 1.8667 0.5750 -0.2546 0.0332  -0.2965 327 ARG B CA  
5340 C C   . ARG B 312 ? 0.4580 1.8458 0.5430 -0.2141 0.0213  -0.2904 327 ARG B C   
5341 O O   . ARG B 312 ? 0.4589 1.9138 0.5642 -0.2051 0.0160  -0.3012 327 ARG B O   
5342 C CB  . ARG B 312 ? 0.5428 1.8874 0.6085 -0.2593 0.0418  -0.2914 327 ARG B CB  
5343 C CG  . ARG B 312 ? 0.5956 1.9199 0.6436 -0.3012 0.0541  -0.2986 327 ARG B CG  
5344 C CD  . ARG B 312 ? 0.6422 1.9260 0.6779 -0.3024 0.0607  -0.2877 327 ARG B CD  
5345 N NE  . ARG B 312 ? 0.6538 1.9890 0.7105 -0.2863 0.0629  -0.2916 327 ARG B NE  
5346 C CZ  . ARG B 312 ? 0.7017 2.0138 0.7530 -0.2777 0.0669  -0.2823 327 ARG B CZ  
5347 N NH1 . ARG B 312 ? 0.7094 1.9475 0.7349 -0.2835 0.0679  -0.2675 327 ARG B NH1 
5348 N NH2 . ARG B 312 ? 0.7255 2.0898 0.7976 -0.2629 0.0697  -0.2887 327 ARG B NH2 
5349 N N   . VAL B 313 ? 0.4305 1.7669 0.5061 -0.1898 0.0166  -0.2733 328 VAL B N   
5350 C CA  . VAL B 313 ? 0.3999 1.7538 0.4860 -0.1522 0.0058  -0.2660 328 VAL B CA  
5351 C C   . VAL B 313 ? 0.3973 1.7833 0.4858 -0.1523 -0.0020 -0.2748 328 VAL B C   
5352 O O   . VAL B 313 ? 0.3851 1.8268 0.4894 -0.1345 -0.0105 -0.2806 328 VAL B O   
5353 C CB  . VAL B 313 ? 0.3941 1.6827 0.4671 -0.1305 0.0032  -0.2465 328 VAL B CB  
5354 C CG1 . VAL B 313 ? 0.3710 1.6781 0.4528 -0.0927 -0.0067 -0.2390 328 VAL B CG1 
5355 C CG2 . VAL B 313 ? 0.3987 1.6443 0.4637 -0.1371 0.0109  -0.2376 328 VAL B CG2 
5356 N N   . GLN B 314 ? 0.4040 1.7539 0.4758 -0.1726 0.0005  -0.2763 329 GLN B N   
5357 C CA  . GLN B 314 ? 0.4134 1.7893 0.4833 -0.1782 -0.0056 -0.2862 329 GLN B CA  
5358 C C   . GLN B 314 ? 0.4195 1.8751 0.5082 -0.1893 -0.0082 -0.3043 329 GLN B C   
5359 O O   . GLN B 314 ? 0.3974 1.8972 0.4944 -0.1752 -0.0190 -0.3094 329 GLN B O   
5360 C CB  . GLN B 314 ? 0.4290 1.7552 0.4780 -0.2051 0.0006  -0.2887 329 GLN B CB  
5361 C CG  . GLN B 314 ? 0.4338 1.7040 0.4686 -0.1872 -0.0022 -0.2756 329 GLN B CG  
5362 C CD  . GLN B 314 ? 0.4622 1.6689 0.4779 -0.2090 0.0060  -0.2744 329 GLN B CD  
5363 O OE1 . GLN B 314 ? 0.4916 1.6751 0.5017 -0.2305 0.0138  -0.2756 329 GLN B OE1 
5364 N NE2 . GLN B 314 ? 0.4746 1.6507 0.4791 -0.2027 0.0043  -0.2719 329 GLN B NE2 
5365 N N   . ALA B 315 ? 0.4322 1.9063 0.5270 -0.2147 0.0013  -0.3138 330 ALA B N   
5366 C CA  . ALA B 315 ? 0.4497 2.0029 0.5654 -0.2281 0.0007  -0.3326 330 ALA B CA  
5367 C C   . ALA B 315 ? 0.4246 2.0330 0.5659 -0.1952 -0.0071 -0.3320 330 ALA B C   
5368 O O   . ALA B 315 ? 0.4137 2.0917 0.5747 -0.1907 -0.0149 -0.3447 330 ALA B O   
5369 C CB  . ALA B 315 ? 0.4698 2.0243 0.5831 -0.2661 0.0150  -0.3429 330 ALA B CB  
5370 N N   . GLU B 316 ? 0.4110 1.9885 0.5520 -0.1722 -0.0053 -0.3178 331 GLU B N   
5371 C CA  . GLU B 316 ? 0.3904 2.0119 0.5528 -0.1382 -0.0127 -0.3163 331 GLU B CA  
5372 C C   . GLU B 316 ? 0.3824 2.0210 0.5458 -0.1105 -0.0288 -0.3127 331 GLU B C   
5373 O O   . GLU B 316 ? 0.3694 2.0729 0.5533 -0.0943 -0.0386 -0.3215 331 GLU B O   
5374 C CB  . GLU B 316 ? 0.3823 1.9557 0.5383 -0.1183 -0.0083 -0.3001 331 GLU B CB  
5375 C CG  . GLU B 316 ? 0.3790 1.9971 0.5568 -0.0869 -0.0129 -0.3009 331 GLU B CG  
5376 C CD  . GLU B 316 ? 0.3777 1.9448 0.5463 -0.0657 -0.0096 -0.2844 331 GLU B CD  
5377 O OE1 . GLU B 316 ? 0.4001 1.9128 0.5511 -0.0493 -0.0149 -0.2684 331 GLU B OE1 
5378 O OE2 . GLU B 316 ? 0.3550 1.9376 0.5337 -0.0663 -0.0014 -0.2883 331 GLU B OE2 
5379 N N   . LEU B 317 ? 0.3926 1.9716 0.5328 -0.1052 -0.0315 -0.2999 332 LEU B N   
5380 C CA  . LEU B 317 ? 0.3916 1.9762 0.5260 -0.0818 -0.0454 -0.2950 332 LEU B CA  
5381 C C   . LEU B 317 ? 0.4056 2.0482 0.5475 -0.0986 -0.0521 -0.3124 332 LEU B C   
5382 O O   . LEU B 317 ? 0.4125 2.1059 0.5662 -0.0775 -0.0657 -0.3162 332 LEU B O   
5383 C CB  . LEU B 317 ? 0.3994 1.9089 0.5071 -0.0800 -0.0438 -0.2806 332 LEU B CB  
5384 C CG  . LEU B 317 ? 0.4012 1.8645 0.5014 -0.0486 -0.0454 -0.2613 332 LEU B CG  
5385 C CD1 . LEU B 317 ? 0.4087 1.7949 0.4899 -0.0582 -0.0361 -0.2494 332 LEU B CD1 
5386 C CD2 . LEU B 317 ? 0.3841 1.8586 0.4792 -0.0172 -0.0595 -0.2546 332 LEU B CD2 
5387 N N   . ASP B 318 ? 0.4126 2.0472 0.5468 -0.1365 -0.0432 -0.3230 333 ASP B N   
5388 C CA  . ASP B 318 ? 0.4343 2.1169 0.5713 -0.1566 -0.0489 -0.3397 333 ASP B CA  
5389 C C   . ASP B 318 ? 0.4533 2.2255 0.6210 -0.1495 -0.0571 -0.3540 333 ASP B C   
5390 O O   . ASP B 318 ? 0.4409 2.2590 0.6145 -0.1394 -0.0712 -0.3604 333 ASP B O   
5391 C CB  . ASP B 318 ? 0.4411 2.1000 0.5652 -0.2011 -0.0358 -0.3501 333 ASP B CB  
5392 C CG  . ASP B 318 ? 0.4534 2.0388 0.5475 -0.2084 -0.0328 -0.3414 333 ASP B CG  
5393 O OD1 . ASP B 318 ? 0.4203 1.9760 0.5036 -0.1812 -0.0402 -0.3282 333 ASP B OD1 
5394 O OD2 . ASP B 318 ? 0.4799 2.0370 0.5605 -0.2422 -0.0223 -0.3485 333 ASP B OD2 
5395 N N   . GLU B 319 ? 0.4934 2.2903 0.6805 -0.1536 -0.0484 -0.3589 334 GLU B N   
5396 C CA  . GLU B 319 ? 0.5339 2.4170 0.7542 -0.1446 -0.0544 -0.3729 334 GLU B CA  
5397 C C   . GLU B 319 ? 0.5596 2.4666 0.7917 -0.0967 -0.0705 -0.3641 334 GLU B C   
5398 O O   . GLU B 319 ? 0.5756 2.5521 0.8285 -0.0838 -0.0839 -0.3746 334 GLU B O   
5399 C CB  . GLU B 319 ? 0.5503 2.4443 0.7850 -0.1608 -0.0384 -0.3793 334 GLU B CB  
5400 C CG  . GLU B 319 ? 0.5540 2.5359 0.8265 -0.1495 -0.0414 -0.3941 334 GLU B CG  
5401 C CD  . GLU B 319 ? 0.5861 2.5856 0.8692 -0.1822 -0.0227 -0.4067 334 GLU B CD  
5402 O OE1 . GLU B 319 ? 0.6071 2.5390 0.8650 -0.2052 -0.0090 -0.3988 334 GLU B OE1 
5403 O OE2 . GLU B 319 ? 0.6173 2.6968 0.9331 -0.1851 -0.0216 -0.4245 334 GLU B OE2 
5404 N N   . CYS B 320 ? 0.6280 2.4770 0.8466 -0.0704 -0.0695 -0.3449 335 CYS B N   
5405 C CA  . CYS B 320 ? 0.6817 2.5473 0.9098 -0.0255 -0.0825 -0.3360 335 CYS B CA  
5406 C C   . CYS B 320 ? 0.6936 2.5442 0.9032 -0.0037 -0.0991 -0.3264 335 CYS B C   
5407 O O   . CYS B 320 ? 0.7288 2.6164 0.9485 0.0286  -0.1147 -0.3251 335 CYS B O   
5408 C CB  . CYS B 320 ? 0.7019 2.5139 0.9234 -0.0084 -0.0733 -0.3208 335 CYS B CB  
5409 S SG  . CYS B 320 ? 0.7922 2.6384 1.0388 -0.0270 -0.0563 -0.3339 335 CYS B SG  
5410 N N   . VAL B 321 ? 0.7063 2.5011 0.8878 -0.0211 -0.0956 -0.3197 336 VAL B N   
5411 C CA  . VAL B 321 ? 0.7173 2.4944 0.8767 -0.0083 -0.1088 -0.3125 336 VAL B CA  
5412 C C   . VAL B 321 ? 0.7292 2.5143 0.8799 -0.0463 -0.1055 -0.3258 336 VAL B C   
5413 O O   . VAL B 321 ? 0.7294 2.5068 0.8832 -0.0791 -0.0912 -0.3344 336 VAL B O   
5414 C CB  . VAL B 321 ? 0.7063 2.3990 0.8376 0.0068  -0.1045 -0.2912 336 VAL B CB  
5415 C CG1 . VAL B 321 ? 0.7258 2.4011 0.8326 0.0211  -0.1173 -0.2837 336 VAL B CG1 
5416 C CG2 . VAL B 321 ? 0.6723 2.3495 0.8109 0.0379  -0.1038 -0.2789 336 VAL B CG2 
5417 N N   . GLY B 322 ? 0.7569 2.5554 0.8944 -0.0436 -0.1185 -0.3281 337 GLY B N   
5418 C CA  . GLY B 322 ? 0.8264 2.6237 0.9516 -0.0805 -0.1141 -0.3405 337 GLY B CA  
5419 C C   . GLY B 322 ? 0.8830 2.5955 0.9804 -0.0955 -0.1000 -0.3304 337 GLY B C   
5420 O O   . GLY B 322 ? 0.8221 2.4807 0.9088 -0.0745 -0.0966 -0.3132 337 GLY B O   
5421 N N   . VAL B 323 ? 0.9890 2.6902 1.0750 -0.1318 -0.0919 -0.3420 338 VAL B N   
5422 C CA  . VAL B 323 ? 1.0468 2.6716 1.1043 -0.1450 -0.0813 -0.3349 338 VAL B CA  
5423 C C   . VAL B 323 ? 1.1113 2.7219 1.1454 -0.1300 -0.0921 -0.3295 338 VAL B C   
5424 O O   . VAL B 323 ? 1.1780 2.7536 1.1896 -0.1481 -0.0871 -0.3329 338 VAL B O   
5425 C CB  . VAL B 323 ? 1.0548 2.6675 1.1062 -0.1890 -0.0682 -0.3495 338 VAL B CB  
5426 C CG1 . VAL B 323 ? 1.0664 2.7329 1.1170 -0.2108 -0.0760 -0.3684 338 VAL B CG1 
5427 C CG2 . VAL B 323 ? 1.0380 2.5676 1.0638 -0.1986 -0.0562 -0.3412 338 VAL B CG2 
5428 N N   . ASP B 324 ? 1.1009 2.7374 1.1395 -0.0959 -0.1067 -0.3209 339 ASP B N   
5429 C CA  . ASP B 324 ? 1.0557 2.6843 1.0720 -0.0765 -0.1193 -0.3139 339 ASP B CA  
5430 C C   . ASP B 324 ? 1.0316 2.6764 1.0593 -0.0372 -0.1302 -0.3010 339 ASP B C   
5431 O O   . ASP B 324 ? 1.0343 2.7211 1.0900 -0.0315 -0.1314 -0.3055 339 ASP B O   
5432 C CB  . ASP B 324 ? 1.0509 2.7371 1.0654 -0.0897 -0.1323 -0.3297 339 ASP B CB  
5433 C CG  . ASP B 324 ? 1.0517 2.8195 1.0983 -0.0827 -0.1442 -0.3400 339 ASP B CG  
5434 O OD1 . ASP B 324 ? 1.0289 2.8163 1.1000 -0.0972 -0.1343 -0.3476 339 ASP B OD1 
5435 O OD2 . ASP B 324 ? 1.0992 2.9112 1.1464 -0.0621 -0.1635 -0.3405 339 ASP B OD2 
5436 N N   . ARG B 325 ? 1.0017 2.6120 1.0071 -0.0108 -0.1371 -0.2857 340 ARG B N   
5437 C CA  . ARG B 325 ? 0.9201 2.5364 0.9307 0.0281  -0.1476 -0.2721 340 ARG B CA  
5438 C C   . ARG B 325 ? 0.8467 2.4063 0.8584 0.0386  -0.1341 -0.2575 340 ARG B C   
5439 O O   . ARG B 325 ? 0.8179 2.3659 0.8442 0.0196  -0.1198 -0.2616 340 ARG B O   
5440 C CB  . ARG B 325 ? 0.8606 2.5559 0.9028 0.0392  -0.1602 -0.2824 340 ARG B CB  
5441 C CG  . ARG B 325 ? 0.8135 2.5142 0.8714 0.0734  -0.1642 -0.2720 340 ARG B CG  
5442 C CD  . ARG B 325 ? 0.7586 2.5345 0.8550 0.0734  -0.1682 -0.2867 340 ARG B CD  
5443 N NE  . ARG B 325 ? 0.7282 2.5075 0.8401 0.1054  -0.1700 -0.2782 340 ARG B NE  
5444 C CZ  . ARG B 325 ? 0.7060 2.5003 0.8156 0.1434  -0.1871 -0.2701 340 ARG B CZ  
5445 N NH1 . ARG B 325 ? 0.7235 2.5312 0.8148 0.1547  -0.2049 -0.2684 340 ARG B NH1 
5446 N NH2 . ARG B 325 ? 0.6950 2.4889 0.8185 0.1705  -0.1866 -0.2637 340 ARG B NH2 
5447 N N   . PRO B 326 ? 0.7807 2.3049 0.7754 0.0685  -0.1391 -0.2404 341 PRO B N   
5448 C CA  . PRO B 326 ? 0.7538 2.2248 0.7480 0.0777  -0.1273 -0.2268 341 PRO B CA  
5449 C C   . PRO B 326 ? 0.6959 2.1965 0.7161 0.0963  -0.1296 -0.2259 341 PRO B C   
5450 O O   . PRO B 326 ? 0.7048 2.2491 0.7325 0.1198  -0.1446 -0.2268 341 PRO B O   
5451 C CB  . PRO B 326 ? 0.7665 2.1932 0.7298 0.1001  -0.1327 -0.2108 341 PRO B CB  
5452 C CG  . PRO B 326 ? 0.7874 2.2597 0.7440 0.1181  -0.1527 -0.2132 341 PRO B CG  
5453 C CD  . PRO B 326 ? 0.8034 2.3411 0.7813 0.0973  -0.1576 -0.2328 341 PRO B CD  
5454 N N   . PRO B 327 ? 0.6152 2.0932 0.6491 0.0859  -0.1151 -0.2247 342 PRO B N   
5455 C CA  . PRO B 327 ? 0.5615 2.0594 0.6163 0.1041  -0.1153 -0.2229 342 PRO B CA  
5456 C C   . PRO B 327 ? 0.5511 2.0138 0.5914 0.1387  -0.1208 -0.2055 342 PRO B C   
5457 O O   . PRO B 327 ? 0.6032 2.0051 0.6228 0.1398  -0.1142 -0.1927 342 PRO B O   
5458 C CB  . PRO B 327 ? 0.5354 2.0056 0.5998 0.0802  -0.0977 -0.2246 342 PRO B CB  
5459 C CG  . PRO B 327 ? 0.5479 2.0015 0.6027 0.0474  -0.0904 -0.2319 342 PRO B CG  
5460 C CD  . PRO B 327 ? 0.5970 2.0322 0.6275 0.0566  -0.0985 -0.2261 342 PRO B CD  
5461 N N   . CYS B 328 ? 0.5290 2.0296 0.5802 0.1666  -0.1327 -0.2055 343 CYS B N   
5462 C CA  . CYS B 328 ? 0.5233 1.9915 0.5594 0.2008  -0.1388 -0.1897 343 CYS B CA  
5463 C C   . CYS B 328 ? 0.5007 1.9760 0.5578 0.2124  -0.1326 -0.1899 343 CYS B C   
5464 O O   . CYS B 328 ? 0.4825 1.9927 0.5650 0.1945  -0.1250 -0.2027 343 CYS B O   
5465 C CB  . CYS B 328 ? 0.5432 2.0478 0.5726 0.2270  -0.1592 -0.1896 343 CYS B CB  
5466 S SG  . CYS B 328 ? 0.5092 2.1091 0.5793 0.2303  -0.1685 -0.2096 343 CYS B SG  
5467 N N   . LEU B 329 ? 0.5131 1.9548 0.5576 0.2418  -0.1357 -0.1763 344 LEU B N   
5468 C CA  . LEU B 329 ? 0.5037 1.9380 0.5619 0.2533  -0.1281 -0.1745 344 LEU B CA  
5469 C C   . LEU B 329 ? 0.4953 1.9987 0.5861 0.2629  -0.1320 -0.1892 344 LEU B C   
5470 O O   . LEU B 329 ? 0.4414 1.9488 0.5489 0.2597  -0.1213 -0.1934 344 LEU B O   
5471 C CB  . LEU B 329 ? 0.5303 1.9134 0.5641 0.2839  -0.1321 -0.1571 344 LEU B CB  
5472 C CG  . LEU B 329 ? 0.5583 1.8688 0.5655 0.2715  -0.1225 -0.1431 344 LEU B CG  
5473 C CD1 . LEU B 329 ? 0.5947 1.8555 0.5740 0.2998  -0.1273 -0.1263 344 LEU B CD1 
5474 C CD2 . LEU B 329 ? 0.5452 1.8332 0.5645 0.2488  -0.1057 -0.1447 344 LEU B CD2 
5475 N N   . SER B 330 ? 0.5259 2.0852 0.6260 0.2747  -0.1474 -0.1976 345 SER B N   
5476 C CA  . SER B 330 ? 0.5182 2.1516 0.6533 0.2840  -0.1519 -0.2137 345 SER B CA  
5477 C C   . SER B 330 ? 0.4734 2.1462 0.6348 0.2466  -0.1387 -0.2310 345 SER B C   
5478 O O   . SER B 330 ? 0.4400 2.1691 0.6319 0.2485  -0.1368 -0.2451 345 SER B O   
5479 C CB  . SER B 330 ? 0.5539 2.2365 0.6913 0.3058  -0.1737 -0.2178 345 SER B CB  
5480 O OG  . SER B 330 ? 0.5981 2.2430 0.7025 0.3011  -0.1808 -0.2072 345 SER B OG  
5481 N N   . ASP B 331 ? 0.4668 2.1079 0.6151 0.2128  -0.1291 -0.2300 346 ASP B N   
5482 C CA  . ASP B 331 ? 0.4469 2.1104 0.6125 0.1745  -0.1152 -0.2441 346 ASP B CA  
5483 C C   . ASP B 331 ? 0.4390 2.0691 0.6080 0.1626  -0.0976 -0.2416 346 ASP B C   
5484 O O   . ASP B 331 ? 0.4126 2.0624 0.5953 0.1323  -0.0860 -0.2535 346 ASP B O   
5485 C CB  . ASP B 331 ? 0.4445 2.0805 0.5916 0.1439  -0.1120 -0.2437 346 ASP B CB  
5486 C CG  . ASP B 331 ? 0.4297 2.1087 0.5761 0.1438  -0.1268 -0.2514 346 ASP B CG  
5487 O OD1 . ASP B 331 ? 0.4505 2.1989 0.6210 0.1531  -0.1364 -0.2641 346 ASP B OD1 
5488 O OD2 . ASP B 331 ? 0.4311 2.0763 0.5534 0.1339  -0.1288 -0.2457 346 ASP B OD2 
5489 N N   . ARG B 332 ? 0.4617 2.0395 0.6157 0.1843  -0.0956 -0.2263 347 ARG B N   
5490 C CA  . ARG B 332 ? 0.4733 2.0109 0.6253 0.1723  -0.0798 -0.2220 347 ARG B CA  
5491 C C   . ARG B 332 ? 0.4679 2.0561 0.6477 0.1639  -0.0712 -0.2375 347 ARG B C   
5492 O O   . ARG B 332 ? 0.4811 2.0622 0.6640 0.1329  -0.0577 -0.2431 347 ARG B O   
5493 C CB  . ARG B 332 ? 0.4996 1.9806 0.6329 0.2000  -0.0804 -0.2046 347 ARG B CB  
5494 C CG  . ARG B 332 ? 0.5257 1.9464 0.6293 0.2046  -0.0847 -0.1882 347 ARG B CG  
5495 C CD  . ARG B 332 ? 0.5653 1.9336 0.6521 0.2292  -0.0838 -0.1728 347 ARG B CD  
5496 N NE  . ARG B 332 ? 0.5803 1.9021 0.6619 0.2097  -0.0697 -0.1674 347 ARG B NE  
5497 C CZ  . ARG B 332 ? 0.6146 1.8727 0.6751 0.2142  -0.0663 -0.1523 347 ARG B CZ  
5498 N NH1 . ARG B 332 ? 0.6269 1.8554 0.6671 0.2372  -0.0744 -0.1402 347 ARG B NH1 
5499 N NH2 . ARG B 332 ? 0.6481 1.8713 0.7067 0.1945  -0.0549 -0.1492 347 ARG B NH2 
5500 N N   . PRO B 333 ? 0.4718 2.1106 0.6713 0.1916  -0.0787 -0.2448 348 PRO B N   
5501 C CA  . PRO B 333 ? 0.4544 2.1435 0.6819 0.1839  -0.0685 -0.2610 348 PRO B CA  
5502 C C   . PRO B 333 ? 0.4283 2.1635 0.6726 0.1438  -0.0606 -0.2785 348 PRO B C   
5503 O O   . PRO B 333 ? 0.3923 2.1391 0.6473 0.1225  -0.0457 -0.2877 348 PRO B O   
5504 C CB  . PRO B 333 ? 0.4778 2.2220 0.7258 0.2224  -0.0816 -0.2675 348 PRO B CB  
5505 C CG  . PRO B 333 ? 0.4884 2.1843 0.7101 0.2540  -0.0954 -0.2488 348 PRO B CG  
5506 C CD  . PRO B 333 ? 0.4681 2.1220 0.6655 0.2305  -0.0963 -0.2397 348 PRO B CD  
5507 N N   . HIS B 334 ? 0.4149 2.1720 0.6581 0.1324  -0.0699 -0.2827 349 HIS B N   
5508 C CA  . HIS B 334 ? 0.4081 2.2035 0.6627 0.0926  -0.0634 -0.2989 349 HIS B CA  
5509 C C   . HIS B 334 ? 0.4135 2.1471 0.6436 0.0570  -0.0518 -0.2921 349 HIS B C   
5510 O O   . HIS B 334 ? 0.3863 2.1390 0.6183 0.0240  -0.0479 -0.3031 349 HIS B O   
5511 C CB  . HIS B 334 ? 0.4153 2.2641 0.6791 0.0953  -0.0793 -0.3078 349 HIS B CB  
5512 C CG  . HIS B 334 ? 0.4044 2.3097 0.6895 0.1340  -0.0948 -0.3124 349 HIS B CG  
5513 N ND1 . HIS B 334 ? 0.4027 2.3718 0.7213 0.1425  -0.0913 -0.3276 349 HIS B ND1 
5514 C CD2 . HIS B 334 ? 0.3948 2.2998 0.6712 0.1676  -0.1137 -0.3035 349 HIS B CD2 
5515 C CE1 . HIS B 334 ? 0.4090 2.4159 0.7406 0.1814  -0.1084 -0.3281 349 HIS B CE1 
5516 N NE2 . HIS B 334 ? 0.4143 2.3813 0.7190 0.1971  -0.1227 -0.3128 349 HIS B NE2 
5517 N N   . LEU B 335 ? 0.4364 2.0963 0.6436 0.0638  -0.0469 -0.2746 350 LEU B N   
5518 C CA  . LEU B 335 ? 0.4259 2.0216 0.6096 0.0359  -0.0378 -0.2661 350 LEU B CA  
5519 C C   . LEU B 335 ? 0.4258 1.9737 0.6009 0.0354  -0.0263 -0.2568 350 LEU B C   
5520 O O   . LEU B 335 ? 0.4487 1.9339 0.6039 0.0469  -0.0270 -0.2400 350 LEU B O   
5521 C CB  . LEU B 335 ? 0.4339 1.9848 0.5954 0.0466  -0.0473 -0.2525 350 LEU B CB  
5522 C CG  . LEU B 335 ? 0.4519 2.0443 0.6167 0.0432  -0.0585 -0.2615 350 LEU B CG  
5523 C CD1 . LEU B 335 ? 0.4509 2.0026 0.5928 0.0600  -0.0684 -0.2478 350 LEU B CD1 
5524 C CD2 . LEU B 335 ? 0.4674 2.0727 0.6335 0.0017  -0.0505 -0.2748 350 LEU B CD2 
5525 N N   . PRO B 336 ? 0.4095 1.9887 0.5994 0.0215  -0.0155 -0.2684 351 PRO B N   
5526 C CA  . PRO B 336 ? 0.4010 1.9420 0.5829 0.0201  -0.0045 -0.2617 351 PRO B CA  
5527 C C   . PRO B 336 ? 0.3990 1.8732 0.5567 -0.0083 0.0039  -0.2522 351 PRO B C   
5528 O O   . PRO B 336 ? 0.4241 1.8460 0.5672 -0.0018 0.0076  -0.2394 351 PRO B O   
5529 C CB  . PRO B 336 ? 0.3998 2.0026 0.6048 0.0074  0.0053  -0.2803 351 PRO B CB  
5530 C CG  . PRO B 336 ? 0.4025 2.0572 0.6205 -0.0160 0.0036  -0.2959 351 PRO B CG  
5531 C CD  . PRO B 336 ? 0.4064 2.0639 0.6224 0.0069  -0.0131 -0.2897 351 PRO B CD  
5532 N N   . LEU B 337 ? 0.3670 1.8433 0.5204 -0.0391 0.0063  -0.2589 352 LEU B N   
5533 C CA  . LEU B 337 ? 0.3557 1.7695 0.4863 -0.0663 0.0131  -0.2510 352 LEU B CA  
5534 C C   . LEU B 337 ? 0.3419 1.6958 0.4553 -0.0501 0.0056  -0.2336 352 LEU B C   
5535 O O   . LEU B 337 ? 0.3360 1.6348 0.4349 -0.0487 0.0087  -0.2208 352 LEU B O   
5536 C CB  . LEU B 337 ? 0.3517 1.7829 0.4810 -0.1028 0.0176  -0.2639 352 LEU B CB  
5537 C CG  . LEU B 337 ? 0.3583 1.7310 0.4645 -0.1353 0.0258  -0.2592 352 LEU B CG  
5538 C CD1 . LEU B 337 ? 0.3623 1.7009 0.4578 -0.1429 0.0350  -0.2529 352 LEU B CD1 
5539 C CD2 . LEU B 337 ? 0.3656 1.7679 0.4728 -0.1712 0.0316  -0.2755 352 LEU B CD2 
5540 N N   . LEU B 338 ? 0.3606 1.7271 0.4756 -0.0379 -0.0042 -0.2334 353 LEU B N   
5541 C CA  . LEU B 338 ? 0.3720 1.6857 0.4712 -0.0223 -0.0103 -0.2180 353 LEU B CA  
5542 C C   . LEU B 338 ? 0.3630 1.6446 0.4575 0.0035  -0.0111 -0.2042 353 LEU B C   
5543 O O   . LEU B 338 ? 0.3779 1.6021 0.4582 0.0006  -0.0083 -0.1921 353 LEU B O   
5544 C CB  . LEU B 338 ? 0.3755 1.7148 0.4768 -0.0072 -0.0213 -0.2201 353 LEU B CB  
5545 C CG  . LEU B 338 ? 0.3667 1.6573 0.4519 0.0120  -0.0272 -0.2048 353 LEU B CG  
5546 C CD1 . LEU B 338 ? 0.3861 1.6181 0.4563 -0.0080 -0.0210 -0.1983 353 LEU B CD1 
5547 C CD2 . LEU B 338 ? 0.3760 1.6963 0.4608 0.0239  -0.0377 -0.2084 353 LEU B CD2 
5548 N N   . ASP B 339 ? 0.3556 1.6746 0.4624 0.0281  -0.0150 -0.2068 354 ASP B N   
5549 C CA  . ASP B 339 ? 0.3609 1.6516 0.4625 0.0521  -0.0149 -0.1955 354 ASP B CA  
5550 C C   . ASP B 339 ? 0.3505 1.5981 0.4423 0.0345  -0.0048 -0.1901 354 ASP B C   
5551 O O   . ASP B 339 ? 0.3104 1.5042 0.3880 0.0419  -0.0052 -0.1761 354 ASP B O   
5552 C CB  . ASP B 339 ? 0.3723 1.7155 0.4911 0.0744  -0.0172 -0.2037 354 ASP B CB  
5553 C CG  . ASP B 339 ? 0.3898 1.7022 0.5012 0.1002  -0.0172 -0.1928 354 ASP B CG  
5554 O OD1 . ASP B 339 ? 0.4326 1.7050 0.5340 0.0895  -0.0091 -0.1867 354 ASP B OD1 
5555 O OD2 . ASP B 339 ? 0.4101 1.7360 0.5239 0.1312  -0.0256 -0.1900 354 ASP B OD2 
5556 N N   . ALA B 340 ? 0.3574 1.6310 0.4563 0.0102  0.0039  -0.2019 355 ALA B N   
5557 C CA  . ALA B 340 ? 0.3568 1.5948 0.4445 -0.0094 0.0134  -0.1985 355 ALA B CA  
5558 C C   . ALA B 340 ? 0.3654 1.5400 0.4344 -0.0234 0.0127  -0.1864 355 ALA B C   
5559 O O   . ALA B 340 ? 0.3814 1.5091 0.4374 -0.0239 0.0148  -0.1756 355 ALA B O   
5560 C CB  . ALA B 340 ? 0.3680 1.6453 0.4635 -0.0379 0.0231  -0.2143 355 ALA B CB  
5561 N N   . VAL B 341 ? 0.3592 1.5325 0.4271 -0.0337 0.0092  -0.1885 356 VAL B N   
5562 C CA  . VAL B 341 ? 0.3709 1.4858 0.4236 -0.0439 0.0081  -0.1780 356 VAL B CA  
5563 C C   . VAL B 341 ? 0.3706 1.4449 0.4170 -0.0180 0.0022  -0.1624 356 VAL B C   
5564 O O   . VAL B 341 ? 0.3942 1.4194 0.4298 -0.0211 0.0033  -0.1517 356 VAL B O   
5565 C CB  . VAL B 341 ? 0.3621 1.4851 0.4147 -0.0597 0.0065  -0.1852 356 VAL B CB  
5566 C CG1 . VAL B 341 ? 0.3569 1.4200 0.3961 -0.0643 0.0049  -0.1746 356 VAL B CG1 
5567 C CG2 . VAL B 341 ? 0.3599 1.5116 0.4143 -0.0909 0.0137  -0.1997 356 VAL B CG2 
5568 N N   . LEU B 342 ? 0.3721 1.4662 0.4239 0.0067  -0.0044 -0.1610 357 LEU B N   
5569 C CA  . LEU B 342 ? 0.3548 1.4135 0.3993 0.0313  -0.0090 -0.1470 357 LEU B CA  
5570 C C   . LEU B 342 ? 0.3489 1.3847 0.3887 0.0384  -0.0059 -0.1398 357 LEU B C   
5571 O O   . LEU B 342 ? 0.3537 1.3450 0.3842 0.0463  -0.0074 -0.1275 357 LEU B O   
5572 C CB  . LEU B 342 ? 0.3460 1.4353 0.3947 0.0576  -0.0163 -0.1477 357 LEU B CB  
5573 C CG  . LEU B 342 ? 0.3529 1.4555 0.4011 0.0547  -0.0209 -0.1517 357 LEU B CG  
5574 C CD1 . LEU B 342 ? 0.3495 1.4969 0.4030 0.0769  -0.0289 -0.1562 357 LEU B CD1 
5575 C CD2 . LEU B 342 ? 0.3539 1.4047 0.3897 0.0567  -0.0216 -0.1402 357 LEU B CD2 
5576 N N   . CYS B 343 ? 0.3260 1.3938 0.3724 0.0350  -0.0013 -0.1483 358 CYS B N   
5577 C CA  . CYS B 343 ? 0.3338 1.3811 0.3741 0.0405  0.0024  -0.1430 358 CYS B CA  
5578 C C   . CYS B 343 ? 0.3452 1.3470 0.3729 0.0163  0.0065  -0.1371 358 CYS B C   
5579 O O   . CYS B 343 ? 0.3278 1.2844 0.3447 0.0217  0.0050  -0.1251 358 CYS B O   
5580 C CB  . CYS B 343 ? 0.3406 1.4369 0.3919 0.0441  0.0074  -0.1552 358 CYS B CB  
5581 S SG  . CYS B 343 ? 0.3611 1.4977 0.4239 0.0815  0.0002  -0.1580 358 CYS B SG  
5582 N N   . GLU B 344 ? 0.3314 1.3445 0.3597 -0.0105 0.0109  -0.1454 359 GLU B N   
5583 C CA  . GLU B 344 ? 0.3230 1.2940 0.3375 -0.0343 0.0137  -0.1405 359 GLU B CA  
5584 C C   . GLU B 344 ? 0.3354 1.2565 0.3432 -0.0301 0.0073  -0.1278 359 GLU B C   
5585 O O   . GLU B 344 ? 0.3292 1.2056 0.3254 -0.0354 0.0062  -0.1180 359 GLU B O   
5586 C CB  . GLU B 344 ? 0.3230 1.3128 0.3370 -0.0637 0.0192  -0.1518 359 GLU B CB  
5587 C CG  . GLU B 344 ? 0.3483 1.2900 0.3442 -0.0890 0.0212  -0.1462 359 GLU B CG  
5588 C CD  . GLU B 344 ? 0.3697 1.2969 0.3528 -0.0976 0.0264  -0.1438 359 GLU B CD  
5589 O OE1 . GLU B 344 ? 0.3594 1.3052 0.3472 -0.0809 0.0285  -0.1445 359 GLU B OE1 
5590 O OE2 . GLU B 344 ? 0.3862 1.2798 0.3518 -0.1217 0.0286  -0.1411 359 GLU B OE2 
5591 N N   . VAL B 345 ? 0.3257 1.2546 0.3405 -0.0207 0.0030  -0.1283 360 VAL B N   
5592 C CA  . VAL B 345 ? 0.3282 1.2127 0.3388 -0.0175 -0.0016 -0.1179 360 VAL B CA  
5593 C C   . VAL B 345 ? 0.3192 1.1758 0.3261 0.0023  -0.0048 -0.1058 360 VAL B C   
5594 O O   . VAL B 345 ? 0.3262 1.1415 0.3260 -0.0033 -0.0064 -0.0970 360 VAL B O   
5595 C CB  . VAL B 345 ? 0.3118 1.2087 0.3286 -0.0118 -0.0042 -0.1213 360 VAL B CB  
5596 C CG1 . VAL B 345 ? 0.3014 1.1539 0.3155 -0.0062 -0.0074 -0.1111 360 VAL B CG1 
5597 C CG2 . VAL B 345 ? 0.3195 1.2357 0.3376 -0.0346 -0.0012 -0.1330 360 VAL B CG2 
5598 N N   . MET B 346 ? 0.3068 1.1857 0.3173 0.0248  -0.0061 -0.1056 361 MET B N   
5599 C CA  . MET B 346 ? 0.3068 1.1612 0.3114 0.0433  -0.0081 -0.0953 361 MET B CA  
5600 C C   . MET B 346 ? 0.3099 1.1395 0.3056 0.0343  -0.0059 -0.0910 361 MET B C   
5601 O O   . MET B 346 ? 0.2934 1.0877 0.2820 0.0414  -0.0084 -0.0809 361 MET B O   
5602 C CB  . MET B 346 ? 0.3128 1.1990 0.3203 0.0672  -0.0091 -0.0981 361 MET B CB  
5603 C CG  . MET B 346 ? 0.3117 1.2117 0.3220 0.0815  -0.0134 -0.0983 361 MET B CG  
5604 S SD  . MET B 346 ? 0.3245 1.2640 0.3366 0.1102  -0.0167 -0.1021 361 MET B SD  
5605 C CE  . MET B 346 ? 0.3660 1.3037 0.3746 0.1188  -0.0221 -0.0990 361 MET B CE  
5606 N N   . ARG B 347 ? 0.3214 1.1696 0.3161 0.0176  -0.0010 -0.0992 362 ARG B N   
5607 C CA  . ARG B 347 ? 0.3389 1.1657 0.3220 0.0071  0.0018  -0.0962 362 ARG B CA  
5608 C C   . ARG B 347 ? 0.3372 1.1186 0.3105 -0.0118 -0.0015 -0.0883 362 ARG B C   
5609 O O   . ARG B 347 ? 0.3400 1.0866 0.3031 -0.0115 -0.0043 -0.0793 362 ARG B O   
5610 C CB  . ARG B 347 ? 0.3663 1.2306 0.3507 -0.0056 0.0093  -0.1086 362 ARG B CB  
5611 C CG  . ARG B 347 ? 0.4042 1.2544 0.3753 -0.0140 0.0142  -0.1078 362 ARG B CG  
5612 C CD  . ARG B 347 ? 0.4337 1.3004 0.4000 -0.0416 0.0217  -0.1175 362 ARG B CD  
5613 N NE  . ARG B 347 ? 0.4640 1.2830 0.4128 -0.0635 0.0189  -0.1093 362 ARG B NE  
5614 C CZ  . ARG B 347 ? 0.4768 1.2908 0.4196 -0.0884 0.0207  -0.1129 362 ARG B CZ  
5615 N NH1 . ARG B 347 ? 0.4771 1.3332 0.4289 -0.0993 0.0270  -0.1260 362 ARG B NH1 
5616 N NH2 . ARG B 347 ? 0.5176 1.2827 0.4447 -0.1026 0.0155  -0.1033 362 ARG B NH2 
5617 N N   . ILE B 348 ? 0.3263 1.1077 0.3022 -0.0276 -0.0018 -0.0920 363 ILE B N   
5618 C CA  . ILE B 348 ? 0.3332 1.0750 0.2987 -0.0471 -0.0047 -0.0867 363 ILE B CA  
5619 C C   . ILE B 348 ? 0.3339 1.0378 0.3028 -0.0389 -0.0124 -0.0762 363 ILE B C   
5620 O O   . ILE B 348 ? 0.3534 1.0194 0.3142 -0.0502 -0.0171 -0.0695 363 ILE B O   
5621 C CB  . ILE B 348 ? 0.3433 1.0990 0.3080 -0.0689 -0.0009 -0.0962 363 ILE B CB  
5622 C CG1 . ILE B 348 ? 0.3752 1.0929 0.3217 -0.0925 -0.0018 -0.0922 363 ILE B CG1 
5623 C CG2 . ILE B 348 ? 0.3405 1.0981 0.3161 -0.0646 -0.0036 -0.0981 363 ILE B CG2 
5624 C CD1 . ILE B 348 ? 0.3931 1.1178 0.3342 -0.1166 0.0026  -0.1013 363 ILE B CD1 
5625 N N   . ARG B 349 ? 0.3093 1.0231 0.2896 -0.0196 -0.0139 -0.0749 364 ARG B N   
5626 C CA  . ARG B 349 ? 0.3049 0.9866 0.2903 -0.0110 -0.0196 -0.0658 364 ARG B CA  
5627 C C   . ARG B 349 ? 0.2936 0.9831 0.2837 0.0118  -0.0199 -0.0620 364 ARG B C   
5628 O O   . ARG B 349 ? 0.2875 0.9864 0.2854 0.0219  -0.0195 -0.0633 364 ARG B O   
5629 C CB  . ARG B 349 ? 0.3023 0.9807 0.2958 -0.0170 -0.0201 -0.0696 364 ARG B CB  
5630 C CG  . ARG B 349 ? 0.3192 0.9774 0.3060 -0.0388 -0.0212 -0.0715 364 ARG B CG  
5631 C CD  . ARG B 349 ? 0.3318 0.9458 0.3120 -0.0433 -0.0283 -0.0610 364 ARG B CD  
5632 N NE  . ARG B 349 ? 0.3571 0.9485 0.3272 -0.0637 -0.0299 -0.0625 364 ARG B NE  
5633 C CZ  . ARG B 349 ? 0.3524 0.9421 0.3055 -0.0818 -0.0276 -0.0646 364 ARG B CZ  
5634 N NH1 . ARG B 349 ? 0.3381 0.9501 0.2843 -0.0824 -0.0229 -0.0666 364 ARG B NH1 
5635 N NH2 . ARG B 349 ? 0.3673 0.9308 0.3090 -0.0998 -0.0295 -0.0651 364 ARG B NH2 
5636 N N   . PRO B 350 ? 0.2921 0.9751 0.2745 0.0194  -0.0201 -0.0573 365 PRO B N   
5637 C CA  . PRO B 350 ? 0.2835 0.9710 0.2666 0.0405  -0.0198 -0.0539 365 PRO B CA  
5638 C C   . PRO B 350 ? 0.2917 0.9585 0.2816 0.0475  -0.0228 -0.0478 365 PRO B C   
5639 O O   . PRO B 350 ? 0.2832 0.9238 0.2769 0.0386  -0.0265 -0.0434 365 PRO B O   
5640 C CB  . PRO B 350 ? 0.2951 0.9654 0.2668 0.0432  -0.0203 -0.0487 365 PRO B CB  
5641 C CG  . PRO B 350 ? 0.2997 0.9583 0.2639 0.0230  -0.0208 -0.0494 365 PRO B CG  
5642 C CD  . PRO B 350 ? 0.2935 0.9608 0.2637 0.0079  -0.0204 -0.0549 365 PRO B CD  
5643 N N   . VAL B 351 ? 0.3264 1.0058 0.3178 0.0631  -0.0212 -0.0481 366 VAL B N   
5644 C CA  . VAL B 351 ? 0.3269 0.9889 0.3240 0.0684  -0.0222 -0.0435 366 VAL B CA  
5645 C C   . VAL B 351 ? 0.3266 0.9571 0.3200 0.0732  -0.0245 -0.0339 366 VAL B C   
5646 O O   . VAL B 351 ? 0.3365 0.9487 0.3373 0.0725  -0.0254 -0.0301 366 VAL B O   
5647 C CB  . VAL B 351 ? 0.3227 1.0052 0.3187 0.0818  -0.0196 -0.0464 366 VAL B CB  
5648 C CG1 . VAL B 351 ? 0.3200 1.0326 0.3214 0.0748  -0.0182 -0.0563 366 VAL B CG1 
5649 C CG2 . VAL B 351 ? 0.3260 1.0171 0.3103 0.0990  -0.0192 -0.0442 366 VAL B CG2 
5650 N N   . SER B 352 ? 0.3288 0.9547 0.3111 0.0778  -0.0247 -0.0311 367 SER B N   
5651 C CA  . SER B 352 ? 0.3404 0.9357 0.3173 0.0787  -0.0274 -0.0229 367 SER B CA  
5652 C C   . SER B 352 ? 0.3348 0.9236 0.3040 0.0686  -0.0294 -0.0228 367 SER B C   
5653 O O   . SER B 352 ? 0.3382 0.9296 0.2952 0.0747  -0.0272 -0.0233 367 SER B O   
5654 C CB  . SER B 352 ? 0.3711 0.9612 0.3364 0.0952  -0.0249 -0.0194 367 SER B CB  
5655 O OG  . SER B 352 ? 0.4046 1.0054 0.3725 0.1044  -0.0223 -0.0206 367 SER B OG  
5656 N N   . PRO B 353 ? 0.3136 0.8924 0.2882 0.0530  -0.0335 -0.0225 368 PRO B N   
5657 C CA  . PRO B 353 ? 0.3187 0.8874 0.2823 0.0412  -0.0357 -0.0217 368 PRO B CA  
5658 C C   . PRO B 353 ? 0.3150 0.8605 0.2662 0.0450  -0.0379 -0.0152 368 PRO B C   
5659 O O   . PRO B 353 ? 0.3244 0.8657 0.2615 0.0388  -0.0373 -0.0158 368 PRO B O   
5660 C CB  . PRO B 353 ? 0.3344 0.8850 0.3049 0.0264  -0.0422 -0.0193 368 PRO B CB  
5661 C CG  . PRO B 353 ? 0.3207 0.8680 0.3081 0.0325  -0.0435 -0.0180 368 PRO B CG  
5662 C CD  . PRO B 353 ? 0.3024 0.8689 0.2915 0.0477  -0.0372 -0.0206 368 PRO B CD  
5663 N N   . ILE B 354 ? 0.2875 0.8175 0.2429 0.0534  -0.0399 -0.0096 369 ILE B N   
5664 C CA  . ILE B 354 ? 0.2938 0.8060 0.2363 0.0600  -0.0397 -0.0050 369 ILE B CA  
5665 C C   . ILE B 354 ? 0.2879 0.8061 0.2299 0.0766  -0.0346 -0.0050 369 ILE B C   
5666 O O   . ILE B 354 ? 0.2806 0.8024 0.2348 0.0794  -0.0342 -0.0045 369 ILE B O   
5667 C CB  . ILE B 354 ? 0.3084 0.7910 0.2537 0.0519  -0.0478 0.0025  369 ILE B CB  
5668 C CG1 . ILE B 354 ? 0.3221 0.7926 0.2624 0.0362  -0.0548 0.0042  369 ILE B CG1 
5669 C CG2 . ILE B 354 ? 0.3223 0.7861 0.2538 0.0582  -0.0469 0.0067  369 ILE B CG2 
5670 C CD1 . ILE B 354 ? 0.3378 0.7824 0.2832 0.0293  -0.0649 0.0114  369 ILE B CD1 
5671 N N   . LEU B 355 ? 0.2946 0.8114 0.2208 0.0876  -0.0305 -0.0055 370 LEU B N   
5672 C CA  . LEU B 355 ? 0.2955 0.8146 0.2163 0.1044  -0.0262 -0.0048 370 LEU B CA  
5673 C C   . LEU B 355 ? 0.3170 0.8074 0.2344 0.1054  -0.0272 0.0024  370 LEU B C   
5674 O O   . LEU B 355 ? 0.3210 0.7913 0.2417 0.0940  -0.0318 0.0066  370 LEU B O   
5675 C CB  . LEU B 355 ? 0.2918 0.8188 0.1966 0.1181  -0.0218 -0.0085 370 LEU B CB  
5676 C CG  . LEU B 355 ? 0.2838 0.8443 0.1933 0.1175  -0.0194 -0.0172 370 LEU B CG  
5677 C CD1 . LEU B 355 ? 0.2929 0.8678 0.1915 0.1360  -0.0148 -0.0222 370 LEU B CD1 
5678 C CD2 . LEU B 355 ? 0.2633 0.8505 0.1900 0.1128  -0.0202 -0.0213 370 LEU B CD2 
5679 N N   . ILE B 356 ? 0.3385 0.8271 0.2481 0.1188  -0.0232 0.0037  371 ILE B N   
5680 C CA  . ILE B 356 ? 0.3651 0.8254 0.2665 0.1193  -0.0223 0.0099  371 ILE B CA  
5681 C C   . ILE B 356 ? 0.3810 0.8175 0.2643 0.1187  -0.0229 0.0122  371 ILE B C   
5682 O O   . ILE B 356 ? 0.4152 0.8540 0.2832 0.1301  -0.0201 0.0096  371 ILE B O   
5683 C CB  . ILE B 356 ? 0.3920 0.8507 0.2804 0.1346  -0.0174 0.0112  371 ILE B CB  
5684 C CG1 . ILE B 356 ? 0.3840 0.8664 0.2867 0.1356  -0.0162 0.0083  371 ILE B CG1 
5685 C CG2 . ILE B 356 ? 0.4130 0.8389 0.2889 0.1329  -0.0151 0.0175  371 ILE B CG2 
5686 C CD1 . ILE B 356 ? 0.3907 0.8789 0.2778 0.1525  -0.0130 0.0084  371 ILE B CD1 
5687 N N   . PRO B 357 ? 0.3951 0.8092 0.2797 0.1061  -0.0266 0.0163  372 PRO B N   
5688 C CA  . PRO B 357 ? 0.4165 0.8043 0.2799 0.1051  -0.0266 0.0183  372 PRO B CA  
5689 C C   . PRO B 357 ? 0.4487 0.8272 0.2874 0.1228  -0.0203 0.0173  372 PRO B C   
5690 O O   . PRO B 357 ? 0.4495 0.8290 0.2834 0.1348  -0.0165 0.0185  372 PRO B O   
5691 C CB  . PRO B 357 ? 0.4169 0.7812 0.2829 0.0949  -0.0288 0.0236  372 PRO B CB  
5692 C CG  . PRO B 357 ? 0.3948 0.7762 0.2894 0.0855  -0.0331 0.0234  372 PRO B CG  
5693 C CD  . PRO B 357 ? 0.3821 0.7928 0.2868 0.0934  -0.0306 0.0190  372 PRO B CD  
5694 N N   . HIS B 358 ? 0.4746 0.8432 0.2970 0.1246  -0.0194 0.0150  373 HIS B N   
5695 C CA  . HIS B 358 ? 0.5098 0.8636 0.3075 0.1416  -0.0138 0.0136  373 HIS B CA  
5696 C C   . HIS B 358 ? 0.5525 0.8679 0.3301 0.1339  -0.0137 0.0168  373 HIS B C   
5697 O O   . HIS B 358 ? 0.6183 0.9285 0.3926 0.1229  -0.0160 0.0149  373 HIS B O   
5698 C CB  . HIS B 358 ? 0.5031 0.8785 0.2986 0.1499  -0.0113 0.0060  373 HIS B CB  
5699 C CG  . HIS B 358 ? 0.4919 0.9033 0.2996 0.1638  -0.0098 0.0014  373 HIS B CG  
5700 N ND1 . HIS B 358 ? 0.4684 0.9071 0.2992 0.1564  -0.0128 0.0009  373 HIS B ND1 
5701 C CD2 . HIS B 358 ? 0.5069 0.9322 0.3073 0.1851  -0.0063 -0.0032 373 HIS B CD2 
5702 C CE1 . HIS B 358 ? 0.4616 0.9302 0.2980 0.1708  -0.0111 -0.0040 373 HIS B CE1 
5703 N NE2 . HIS B 358 ? 0.4795 0.9419 0.2987 0.1890  -0.0078 -0.0064 373 HIS B NE2 
5704 N N   . VAL B 359 ? 0.5651 0.8519 0.3265 0.1382  -0.0110 0.0214  374 VAL B N   
5705 C CA  . VAL B 359 ? 0.5695 0.8184 0.3117 0.1279  -0.0110 0.0243  374 VAL B CA  
5706 C C   . VAL B 359 ? 0.6082 0.8348 0.3208 0.1409  -0.0058 0.0209  374 VAL B C   
5707 O O   . VAL B 359 ? 0.6092 0.8388 0.3113 0.1618  -0.0014 0.0188  374 VAL B O   
5708 C CB  . VAL B 359 ? 0.5755 0.8015 0.3125 0.1230  -0.0094 0.0303  374 VAL B CB  
5709 C CG1 . VAL B 359 ? 0.5923 0.7837 0.3145 0.1069  -0.0106 0.0326  374 VAL B CG1 
5710 C CG2 . VAL B 359 ? 0.5525 0.8046 0.3200 0.1144  -0.0126 0.0319  374 VAL B CG2 
5711 N N   . ALA B 360 ? 0.6368 0.8406 0.3357 0.1288  -0.0068 0.0199  375 ALA B N   
5712 C CA  . ALA B 360 ? 0.6932 0.8717 0.3629 0.1396  -0.0010 0.0160  375 ALA B CA  
5713 C C   . ALA B 360 ? 0.7433 0.8842 0.3896 0.1465  0.0029  0.0208  375 ALA B C   
5714 O O   . ALA B 360 ? 0.7651 0.8835 0.4076 0.1299  0.0010  0.0256  375 ALA B O   
5715 C CB  . ALA B 360 ? 0.7129 0.8752 0.3721 0.1221  -0.0032 0.0136  375 ALA B CB  
5716 N N   . MET B 361 ? 0.7856 0.9202 0.4161 0.1707  0.0081  0.0196  376 MET B N   
5717 C CA  . MET B 361 ? 0.8312 0.9230 0.4320 0.1790  0.0122  0.0244  376 MET B CA  
5718 C C   . MET B 361 ? 0.8583 0.9045 0.4259 0.1761  0.0164  0.0222  376 MET B C   
5719 O O   . MET B 361 ? 0.8788 0.8819 0.4178 0.1781  0.0200  0.0263  376 MET B O   
5720 C CB  . MET B 361 ? 0.8750 0.9729 0.4677 0.2078  0.0146  0.0243  376 MET B CB  
5721 C CG  . MET B 361 ? 0.8786 1.0202 0.4997 0.2130  0.0109  0.0257  376 MET B CG  
5722 S SD  . MET B 361 ? 0.9259 1.0537 0.5390 0.2160  0.0112  0.0349  376 MET B SD  
5723 C CE  . MET B 361 ? 0.9883 1.0511 0.5512 0.2287  0.0165  0.0394  376 MET B CE  
5724 N N   . GLN B 362 ? 0.8526 0.9060 0.4210 0.1711  0.0164  0.0154  377 GLN B N   
5725 C CA  . GLN B 362 ? 0.8865 0.8974 0.4241 0.1637  0.0201  0.0124  377 GLN B CA  
5726 C C   . GLN B 362 ? 0.8462 0.8723 0.3918 0.1481  0.0178  0.0064  377 GLN B C   
5727 O O   . GLN B 362 ? 0.7962 0.8642 0.3701 0.1435  0.0135  0.0049  377 GLN B O   
5728 C CB  . GLN B 362 ? 0.9500 0.9337 0.4576 0.1904  0.0277  0.0080  377 GLN B CB  
5729 C CG  . GLN B 362 ? 0.9563 0.9747 0.4753 0.2100  0.0304  -0.0013 377 GLN B CG  
5730 C CD  . GLN B 362 ? 1.0023 1.0113 0.5059 0.2435  0.0348  -0.0035 377 GLN B CD  
5731 O OE1 . GLN B 362 ? 1.0361 1.0466 0.5416 0.2558  0.0323  0.0029  377 GLN B OE1 
5732 N NE2 . GLN B 362 ? 1.0286 1.0288 0.5170 0.2589  0.0412  -0.0131 377 GLN B NE2 
5733 N N   . ASP B 363 ? 0.8655 0.8550 0.3832 0.1390  0.0206  0.0031  378 ASP B N   
5734 C CA  . ASP B 363 ? 0.8528 0.8526 0.3711 0.1260  0.0195  -0.0032 378 ASP B CA  
5735 C C   . ASP B 363 ? 0.8346 0.8654 0.3608 0.1464  0.0252  -0.0116 378 ASP B C   
5736 O O   . ASP B 363 ? 0.8578 0.8833 0.3739 0.1721  0.0319  -0.0152 378 ASP B O   
5737 C CB  . ASP B 363 ? 0.8997 0.8523 0.3821 0.1150  0.0229  -0.0066 378 ASP B CB  
5738 C CG  . ASP B 363 ? 0.9120 0.8411 0.3906 0.0895  0.0159  0.0004  378 ASP B CG  
5739 O OD1 . ASP B 363 ? 0.8855 0.8372 0.3917 0.0812  0.0088  0.0074  378 ASP B OD1 
5740 O OD2 . ASP B 363 ? 0.9522 0.8413 0.4009 0.0777  0.0178  -0.0020 378 ASP B OD2 
5741 N N   . THR B 364 ? 0.7941 0.8581 0.3388 0.1346  0.0221  -0.0149 379 THR B N   
5742 C CA  . THR B 364 ? 0.7769 0.8818 0.3380 0.1497  0.0266  -0.0224 379 THR B CA  
5743 C C   . THR B 364 ? 0.7684 0.8916 0.3359 0.1283  0.0242  -0.0260 379 THR B C   
5744 O O   . THR B 364 ? 0.7729 0.8783 0.3343 0.1045  0.0171  -0.0212 379 THR B O   
5745 C CB  . THR B 364 ? 0.7404 0.8815 0.3316 0.1621  0.0229  -0.0177 379 THR B CB  
5746 O OG1 . THR B 364 ? 0.7214 0.9056 0.3300 0.1761  0.0270  -0.0259 379 THR B OG1 
5747 C CG2 . THR B 364 ? 0.7087 0.8648 0.3232 0.1411  0.0130  -0.0095 379 THR B CG2 
5748 N N   . SER B 365 ? 0.7479 0.9056 0.3258 0.1360  0.0300  -0.0348 380 SER B N   
5749 C CA  . SER B 365 ? 0.7340 0.9098 0.3173 0.1147  0.0278  -0.0374 380 SER B CA  
5750 C C   . SER B 365 ? 0.6691 0.8913 0.2856 0.1152  0.0240  -0.0359 380 SER B C   
5751 O O   . SER B 365 ? 0.6359 0.8786 0.2689 0.1342  0.0252  -0.0356 380 SER B O   
5752 C CB  . SER B 365 ? 0.7843 0.9590 0.3478 0.1175  0.0395  -0.0503 380 SER B CB  
5753 O OG  . SER B 365 ? 0.7834 1.0025 0.3650 0.1158  0.0437  -0.0576 380 SER B OG  
5754 N N   . LEU B 366 ? 0.6482 0.8840 0.2720 0.0933  0.0188  -0.0345 381 LEU B N   
5755 C CA  . LEU B 366 ? 0.6196 0.8990 0.2703 0.0916  0.0176  -0.0360 381 LEU B CA  
5756 C C   . LEU B 366 ? 0.6296 0.9145 0.2709 0.0701  0.0188  -0.0403 381 LEU B C   
5757 O O   . LEU B 366 ? 0.6411 0.8975 0.2655 0.0503  0.0120  -0.0352 381 LEU B O   
5758 C CB  . LEU B 366 ? 0.5934 0.8779 0.2662 0.0852  0.0060  -0.0250 381 LEU B CB  
5759 C CG  . LEU B 366 ? 0.5614 0.8875 0.2638 0.0877  0.0042  -0.0252 381 LEU B CG  
5760 C CD1 . LEU B 366 ? 0.5420 0.8626 0.2607 0.0757  -0.0080 -0.0144 381 LEU B CD1 
5761 C CD2 . LEU B 366 ? 0.5540 0.9069 0.2597 0.0765  0.0082  -0.0325 381 LEU B CD2 
5762 N N   . GLY B 367 ? 0.6150 0.9358 0.2656 0.0727  0.0272  -0.0499 382 GLY B N   
5763 C CA  . GLY B 367 ? 0.6414 0.9632 0.2767 0.0520  0.0310  -0.0551 382 GLY B CA  
5764 C C   . GLY B 367 ? 0.6879 0.9727 0.2904 0.0512  0.0366  -0.0592 382 GLY B C   
5765 O O   . GLY B 367 ? 0.7274 0.9998 0.3247 0.0717  0.0417  -0.0620 382 GLY B O   
5766 N N   . GLY B 368 ? 0.7021 0.9656 0.2801 0.0280  0.0353  -0.0592 383 GLY B N   
5767 C CA  . GLY B 368 ? 0.7562 0.9819 0.3007 0.0261  0.0405  -0.0635 383 GLY B CA  
5768 C C   . GLY B 368 ? 0.7710 0.9555 0.3037 0.0276  0.0314  -0.0545 383 GLY B C   
5769 O O   . GLY B 368 ? 0.8165 0.9685 0.3209 0.0278  0.0366  -0.0589 383 GLY B O   
5770 N N   . HIS B 369 ? 0.7358 0.9221 0.2900 0.0285  0.0190  -0.0429 384 HIS B N   
5771 C CA  . HIS B 369 ? 0.7352 0.8863 0.2799 0.0177  0.0069  -0.0329 384 HIS B CA  
5772 C C   . HIS B 369 ? 0.7304 0.8701 0.2834 0.0355  0.0065  -0.0288 384 HIS B C   
5773 O O   . HIS B 369 ? 0.7265 0.8916 0.3034 0.0534  0.0089  -0.0283 384 HIS B O   
5774 C CB  . HIS B 369 ? 0.7150 0.8757 0.2771 -0.0007 -0.0085 -0.0225 384 HIS B CB  
5775 C CG  . HIS B 369 ? 0.7209 0.8959 0.2771 -0.0169 -0.0082 -0.0254 384 HIS B CG  
5776 N ND1 . HIS B 369 ? 0.7504 0.9006 0.2789 -0.0397 -0.0141 -0.0238 384 HIS B ND1 
5777 C CD2 . HIS B 369 ? 0.7060 0.9161 0.2773 -0.0147 -0.0021 -0.0302 384 HIS B CD2 
5778 C CE1 . HIS B 369 ? 0.7515 0.9189 0.2771 -0.0511 -0.0115 -0.0268 384 HIS B CE1 
5779 N NE2 . HIS B 369 ? 0.7159 0.9201 0.2678 -0.0368 -0.0037 -0.0311 384 HIS B NE2 
5780 N N   . SER B 370 ? 0.7461 0.8464 0.2774 0.0292  0.0034  -0.0258 385 SER B N   
5781 C CA  . SER B 370 ? 0.7485 0.8311 0.2813 0.0424  0.0037  -0.0218 385 SER B CA  
5782 C C   . SER B 370 ? 0.7243 0.8260 0.2891 0.0399  -0.0072 -0.0117 385 SER B C   
5783 O O   . SER B 370 ? 0.7209 0.8365 0.3006 0.0236  -0.0177 -0.0066 385 SER B O   
5784 C CB  . SER B 370 ? 0.7845 0.8205 0.2867 0.0307  0.0019  -0.0208 385 SER B CB  
5785 O OG  . SER B 370 ? 0.7848 0.8048 0.2919 0.0368  -0.0006 -0.0144 385 SER B OG  
5786 N N   . VAL B 371 ? 0.7211 0.8226 0.2953 0.0570  -0.0041 -0.0092 386 VAL B N   
5787 C CA  . VAL B 371 ? 0.6820 0.8046 0.2867 0.0580  -0.0114 -0.0014 386 VAL B CA  
5788 C C   . VAL B 371 ? 0.6997 0.7941 0.2946 0.0653  -0.0091 0.0024  386 VAL B C   
5789 O O   . VAL B 371 ? 0.7070 0.7950 0.2919 0.0862  -0.0001 -0.0007 386 VAL B O   
5790 C CB  . VAL B 371 ? 0.6524 0.8158 0.2802 0.0744  -0.0069 -0.0046 386 VAL B CB  
5791 C CG1 . VAL B 371 ? 0.6277 0.8061 0.2801 0.0823  -0.0104 0.0018  386 VAL B CG1 
5792 C CG2 . VAL B 371 ? 0.6320 0.8215 0.2714 0.0606  -0.0111 -0.0065 386 VAL B CG2 
5793 N N   . PRO B 372 ? 0.7087 0.7842 0.3040 0.0474  -0.0175 0.0087  387 PRO B N   
5794 C CA  . PRO B 372 ? 0.7230 0.7679 0.3051 0.0495  -0.0146 0.0120  387 PRO B CA  
5795 C C   . PRO B 372 ? 0.6924 0.7538 0.2932 0.0648  -0.0118 0.0157  387 PRO B C   
5796 O O   . PRO B 372 ? 0.6430 0.7402 0.2733 0.0667  -0.0158 0.0175  387 PRO B O   
5797 C CB  . PRO B 372 ? 0.7246 0.7598 0.3134 0.0242  -0.0258 0.0172  387 PRO B CB  
5798 C CG  . PRO B 372 ? 0.7129 0.7648 0.3098 0.0099  -0.0351 0.0166  387 PRO B CG  
5799 C CD  . PRO B 372 ? 0.6938 0.7772 0.3029 0.0242  -0.0306 0.0131  387 PRO B CD  
5800 N N   . LYS B 373 ? 0.7249 0.7572 0.3057 0.0747  -0.0049 0.0169  388 LYS B N   
5801 C CA  . LYS B 373 ? 0.7331 0.7735 0.3262 0.0855  -0.0028 0.0217  388 LYS B CA  
5802 C C   . LYS B 373 ? 0.7104 0.7701 0.3341 0.0676  -0.0109 0.0274  388 LYS B C   
5803 O O   . LYS B 373 ? 0.7230 0.7709 0.3480 0.0463  -0.0170 0.0292  388 LYS B O   
5804 C CB  . LYS B 373 ? 0.7874 0.7827 0.3470 0.0929  0.0048  0.0231  388 LYS B CB  
5805 C CG  . LYS B 373 ? 0.7954 0.7913 0.3586 0.1047  0.0082  0.0284  388 LYS B CG  
5806 C CD  . LYS B 373 ? 0.8422 0.7869 0.3709 0.1016  0.0140  0.0313  388 LYS B CD  
5807 C CE  . LYS B 373 ? 0.8596 0.7976 0.3815 0.1173  0.0187  0.0363  388 LYS B CE  
5808 N NZ  . LYS B 373 ? 0.9251 0.8074 0.4081 0.1126  0.0250  0.0392  388 LYS B NZ  
5809 N N   . GLY B 374 ? 0.6685 0.7592 0.3174 0.0766  -0.0113 0.0295  389 GLY B N   
5810 C CA  . GLY B 374 ? 0.6339 0.7453 0.3136 0.0626  -0.0176 0.0334  389 GLY B CA  
5811 C C   . GLY B 374 ? 0.5945 0.7436 0.3035 0.0589  -0.0253 0.0321  389 GLY B C   
5812 O O   . GLY B 374 ? 0.5738 0.7466 0.3114 0.0541  -0.0295 0.0342  389 GLY B O   
5813 N N   . THR B 375 ? 0.6073 0.7610 0.3080 0.0611  -0.0262 0.0281  390 THR B N   
5814 C CA  . THR B 375 ? 0.5925 0.7774 0.3159 0.0557  -0.0331 0.0269  390 THR B CA  
5815 C C   . THR B 375 ? 0.5866 0.8047 0.3315 0.0693  -0.0304 0.0260  390 THR B C   
5816 O O   . THR B 375 ? 0.5875 0.8073 0.3236 0.0871  -0.0225 0.0242  390 THR B O   
5817 C CB  . THR B 375 ? 0.5963 0.7784 0.3016 0.0557  -0.0318 0.0218  390 THR B CB  
5818 O OG1 . THR B 375 ? 0.6495 0.7983 0.3304 0.0433  -0.0337 0.0218  390 THR B OG1 
5819 C CG2 . THR B 375 ? 0.5637 0.7728 0.2880 0.0467  -0.0390 0.0213  390 THR B CG2 
5820 N N   . ARG B 376 ? 0.5922 0.8357 0.3639 0.0608  -0.0377 0.0270  391 ARG B N   
5821 C CA  . ARG B 376 ? 0.5850 0.8605 0.3785 0.0702  -0.0360 0.0257  391 ARG B CA  
5822 C C   . ARG B 376 ? 0.5466 0.8437 0.3455 0.0682  -0.0381 0.0217  391 ARG B C   
5823 O O   . ARG B 376 ? 0.5831 0.8742 0.3803 0.0537  -0.0451 0.0226  391 ARG B O   
5824 C CB  . ARG B 376 ? 0.5894 0.8748 0.4102 0.0613  -0.0417 0.0294  391 ARG B CB  
5825 C CG  . ARG B 376 ? 0.6429 0.9080 0.4575 0.0609  -0.0381 0.0325  391 ARG B CG  
5826 C CD  . ARG B 376 ? 0.7036 0.9749 0.5442 0.0477  -0.0444 0.0351  391 ARG B CD  
5827 N NE  . ARG B 376 ? 0.7890 1.0438 0.6233 0.0467  -0.0383 0.0371  391 ARG B NE  
5828 C CZ  . ARG B 376 ? 0.8604 1.1235 0.7174 0.0388  -0.0392 0.0380  391 ARG B CZ  
5829 N NH1 . ARG B 376 ? 0.8584 1.1458 0.7474 0.0329  -0.0468 0.0371  391 ARG B NH1 
5830 N NH2 . ARG B 376 ? 0.9233 1.1695 0.7700 0.0366  -0.0318 0.0393  391 ARG B NH2 
5831 N N   . VAL B 377 ? 0.4902 0.8122 0.2946 0.0816  -0.0323 0.0175  392 VAL B N   
5832 C CA  . VAL B 377 ? 0.4576 0.8016 0.2655 0.0792  -0.0322 0.0124  392 VAL B CA  
5833 C C   . VAL B 377 ? 0.4235 0.7988 0.2563 0.0812  -0.0331 0.0112  392 VAL B C   
5834 O O   . VAL B 377 ? 0.4540 0.8443 0.2926 0.0952  -0.0284 0.0096  392 VAL B O   
5835 C CB  . VAL B 377 ? 0.4711 0.8179 0.2598 0.0928  -0.0232 0.0057  392 VAL B CB  
5836 C CG1 . VAL B 377 ? 0.4646 0.8369 0.2575 0.0878  -0.0215 -0.0007 392 VAL B CG1 
5837 C CG2 . VAL B 377 ? 0.4998 0.8118 0.2616 0.0901  -0.0216 0.0062  392 VAL B CG2 
5838 N N   . LEU B 378 ? 0.3924 0.7757 0.2380 0.0670  -0.0397 0.0120  393 LEU B N   
5839 C CA  . LEU B 378 ? 0.3586 0.7685 0.2256 0.0667  -0.0406 0.0101  393 LEU B CA  
5840 C C   . LEU B 378 ? 0.3495 0.7822 0.2132 0.0659  -0.0364 0.0031  393 LEU B C   
5841 O O   . LEU B 378 ? 0.3419 0.7694 0.1981 0.0526  -0.0392 0.0026  393 LEU B O   
5842 C CB  . LEU B 378 ? 0.3449 0.7479 0.2282 0.0521  -0.0507 0.0149  393 LEU B CB  
5843 C CG  . LEU B 378 ? 0.3504 0.7351 0.2408 0.0506  -0.0550 0.0205  393 LEU B CG  
5844 C CD1 . LEU B 378 ? 0.3462 0.7298 0.2569 0.0387  -0.0655 0.0238  393 LEU B CD1 
5845 C CD2 . LEU B 378 ? 0.3482 0.7398 0.2452 0.0633  -0.0481 0.0201  393 LEU B CD2 
5846 N N   . VAL B 379 ? 0.3401 0.7995 0.2096 0.0792  -0.0298 -0.0024 394 VAL B N   
5847 C CA  . VAL B 379 ? 0.3256 0.8120 0.1952 0.0779  -0.0251 -0.0104 394 VAL B CA  
5848 C C   . VAL B 379 ? 0.3148 0.8149 0.2001 0.0646  -0.0291 -0.0110 394 VAL B C   
5849 O O   . VAL B 379 ? 0.3082 0.8183 0.2091 0.0683  -0.0305 -0.0101 394 VAL B O   
5850 C CB  . VAL B 379 ? 0.3170 0.8294 0.1883 0.0974  -0.0180 -0.0167 394 VAL B CB  
5851 C CG1 . VAL B 379 ? 0.3141 0.8631 0.1934 0.0941  -0.0138 -0.0260 394 VAL B CG1 
5852 C CG2 . VAL B 379 ? 0.3337 0.8298 0.1856 0.1112  -0.0134 -0.0173 394 VAL B CG2 
5853 N N   . ASN B 380 ? 0.3353 0.8321 0.2141 0.0482  -0.0309 -0.0122 395 ASN B N   
5854 C CA  . ASN B 380 ? 0.3391 0.8445 0.2287 0.0342  -0.0345 -0.0129 395 ASN B CA  
5855 C C   . ASN B 380 ? 0.3429 0.8855 0.2379 0.0362  -0.0265 -0.0229 395 ASN B C   
5856 O O   . ASN B 380 ? 0.3601 0.9136 0.2457 0.0265  -0.0217 -0.0288 395 ASN B O   
5857 C CB  . ASN B 380 ? 0.3489 0.8300 0.2254 0.0143  -0.0411 -0.0088 395 ASN B CB  
5858 C CG  . ASN B 380 ? 0.3371 0.8180 0.2234 0.0010  -0.0468 -0.0075 395 ASN B CG  
5859 O OD1 . ASN B 380 ? 0.3235 0.8252 0.2258 0.0051  -0.0443 -0.0114 395 ASN B OD1 
5860 N ND2 . ASN B 380 ? 0.3520 0.8074 0.2267 -0.0148 -0.0549 -0.0022 395 ASN B ND2 
5861 N N   . MET B 381 ? 0.3395 0.9024 0.2497 0.0479  -0.0250 -0.0251 396 MET B N   
5862 C CA  . MET B 381 ? 0.3477 0.9490 0.2669 0.0508  -0.0191 -0.0345 396 MET B CA  
5863 C C   . MET B 381 ? 0.3308 0.9380 0.2535 0.0305  -0.0202 -0.0376 396 MET B C   
5864 O O   . MET B 381 ? 0.3284 0.9667 0.2542 0.0259  -0.0144 -0.0468 396 MET B O   
5865 C CB  . MET B 381 ? 0.3697 0.9837 0.3022 0.0655  -0.0197 -0.0341 396 MET B CB  
5866 C CG  . MET B 381 ? 0.4139 1.0692 0.3555 0.0721  -0.0151 -0.0436 396 MET B CG  
5867 S SD  . MET B 381 ? 0.5291 1.1985 0.4660 0.0996  -0.0119 -0.0453 396 MET B SD  
5868 C CE  . MET B 381 ? 0.4931 1.1491 0.4135 0.0989  -0.0078 -0.0465 396 MET B CE  
5869 N N   . TRP B 382 ? 0.3151 0.8933 0.2378 0.0183  -0.0277 -0.0303 397 TRP B N   
5870 C CA  . TRP B 382 ? 0.3191 0.8964 0.2408 -0.0009 -0.0291 -0.0325 397 TRP B CA  
5871 C C   . TRP B 382 ? 0.3437 0.9209 0.2466 -0.0144 -0.0247 -0.0360 397 TRP B C   
5872 O O   . TRP B 382 ? 0.3571 0.9580 0.2582 -0.0246 -0.0181 -0.0445 397 TRP B O   
5873 C CB  . TRP B 382 ? 0.3165 0.8602 0.2411 -0.0092 -0.0393 -0.0238 397 TRP B CB  
5874 C CG  . TRP B 382 ? 0.3311 0.8686 0.2503 -0.0286 -0.0410 -0.0257 397 TRP B CG  
5875 C CD1 . TRP B 382 ? 0.3550 0.8721 0.2545 -0.0458 -0.0434 -0.0233 397 TRP B CD1 
5876 C CD2 . TRP B 382 ? 0.3294 0.8794 0.2596 -0.0339 -0.0396 -0.0309 397 TRP B CD2 
5877 N NE1 . TRP B 382 ? 0.3643 0.8781 0.2610 -0.0617 -0.0438 -0.0259 397 TRP B NE1 
5878 C CE2 . TRP B 382 ? 0.3498 0.8832 0.2657 -0.0547 -0.0415 -0.0309 397 TRP B CE2 
5879 C CE3 . TRP B 382 ? 0.3124 0.8834 0.2608 -0.0240 -0.0369 -0.0355 397 TRP B CE3 
5880 C CZ2 . TRP B 382 ? 0.3537 0.8901 0.2731 -0.0658 -0.0405 -0.0357 397 TRP B CZ2 
5881 C CZ3 . TRP B 382 ? 0.3135 0.8892 0.2663 -0.0349 -0.0360 -0.0407 397 TRP B CZ3 
5882 C CH2 . TRP B 382 ? 0.3317 0.8897 0.2702 -0.0557 -0.0376 -0.0409 397 TRP B CH2 
5883 N N   . ALA B 383 ? 0.3581 0.9094 0.2462 -0.0148 -0.0277 -0.0300 398 ALA B N   
5884 C CA  . ALA B 383 ? 0.3714 0.9142 0.2380 -0.0292 -0.0244 -0.0319 398 ALA B CA  
5885 C C   . ALA B 383 ? 0.3648 0.9468 0.2317 -0.0264 -0.0116 -0.0444 398 ALA B C   
5886 O O   . ALA B 383 ? 0.3691 0.9643 0.2294 -0.0432 -0.0060 -0.0509 398 ALA B O   
5887 C CB  . ALA B 383 ? 0.3906 0.9035 0.2427 -0.0254 -0.0288 -0.0247 398 ALA B CB  
5888 N N   . ILE B 384 ? 0.3499 0.9515 0.2251 -0.0051 -0.0070 -0.0480 399 ILE B N   
5889 C CA  . ILE B 384 ? 0.3592 0.9994 0.2368 0.0005  0.0041  -0.0603 399 ILE B CA  
5890 C C   . ILE B 384 ? 0.3461 1.0250 0.2391 -0.0060 0.0082  -0.0695 399 ILE B C   
5891 O O   . ILE B 384 ? 0.3488 1.0594 0.2421 -0.0118 0.0175  -0.0807 399 ILE B O   
5892 C CB  . ILE B 384 ? 0.3608 1.0124 0.2432 0.0272  0.0071  -0.0623 399 ILE B CB  
5893 C CG1 . ILE B 384 ? 0.3560 1.0227 0.2573 0.0439  0.0030  -0.0607 399 ILE B CG1 
5894 C CG2 . ILE B 384 ? 0.3716 0.9827 0.2367 0.0314  0.0036  -0.0539 399 ILE B CG2 
5895 C CD1 . ILE B 384 ? 0.3634 1.0369 0.2660 0.0706  0.0048  -0.0614 399 ILE B CD1 
5896 N N   . HIS B 385 ? 0.3363 1.0134 0.2418 -0.0066 0.0020  -0.0658 400 HIS B N   
5897 C CA  . HIS B 385 ? 0.3311 1.0442 0.2499 -0.0139 0.0058  -0.0751 400 HIS B CA  
5898 C C   . HIS B 385 ? 0.3339 1.0369 0.2427 -0.0422 0.0067  -0.0767 400 HIS B C   
5899 O O   . HIS B 385 ? 0.3229 1.0570 0.2394 -0.0526 0.0118  -0.0863 400 HIS B O   
5900 C CB  . HIS B 385 ? 0.3218 1.0393 0.2571 -0.0025 -0.0001 -0.0722 400 HIS B CB  
5901 C CG  . HIS B 385 ? 0.3127 1.0577 0.2595 0.0228  0.0013  -0.0756 400 HIS B CG  
5902 N ND1 . HIS B 385 ? 0.3057 1.0621 0.2655 0.0333  -0.0023 -0.0751 400 HIS B ND1 
5903 C CD2 . HIS B 385 ? 0.3148 1.0756 0.2600 0.0400  0.0054  -0.0791 400 HIS B CD2 
5904 C CE1 . HIS B 385 ? 0.3043 1.0809 0.2684 0.0558  -0.0014 -0.0772 400 HIS B CE1 
5905 N NE2 . HIS B 385 ? 0.3102 1.0898 0.2664 0.0612  0.0031  -0.0798 400 HIS B NE2 
5906 N N   . HIS B 386 ? 0.3386 0.9973 0.2297 -0.0545 0.0010  -0.0669 401 HIS B N   
5907 C CA  . HIS B 386 ? 0.3610 0.9993 0.2374 -0.0810 -0.0002 -0.0658 401 HIS B CA  
5908 C C   . HIS B 386 ? 0.3910 1.0142 0.2417 -0.0983 0.0045  -0.0663 401 HIS B C   
5909 O O   . HIS B 386 ? 0.4155 1.0159 0.2476 -0.1219 0.0035  -0.0642 401 HIS B O   
5910 C CB  . HIS B 386 ? 0.3612 0.9584 0.2375 -0.0825 -0.0127 -0.0539 401 HIS B CB  
5911 C CG  . HIS B 386 ? 0.3514 0.9603 0.2459 -0.0797 -0.0147 -0.0564 401 HIS B CG  
5912 N ND1 . HIS B 386 ? 0.3326 0.9601 0.2478 -0.0583 -0.0157 -0.0571 401 HIS B ND1 
5913 C CD2 . HIS B 386 ? 0.3630 0.9644 0.2556 -0.0961 -0.0157 -0.0584 401 HIS B CD2 
5914 C CE1 . HIS B 386 ? 0.3264 0.9591 0.2524 -0.0619 -0.0169 -0.0599 401 HIS B CE1 
5915 N NE2 . HIS B 386 ? 0.3545 0.9719 0.2677 -0.0844 -0.0169 -0.0611 401 HIS B NE2 
5916 N N   . ASP B 387 ? 0.3957 1.0314 0.2439 -0.0865 0.0103  -0.0696 402 ASP B N   
5917 C CA  . ASP B 387 ? 0.4183 1.0377 0.2412 -0.0993 0.0152  -0.0700 402 ASP B CA  
5918 C C   . ASP B 387 ? 0.4326 1.0755 0.2452 -0.1227 0.0276  -0.0816 402 ASP B C   
5919 O O   . ASP B 387 ? 0.4244 1.1153 0.2519 -0.1170 0.0388  -0.0951 402 ASP B O   
5920 C CB  . ASP B 387 ? 0.4102 1.0431 0.2373 -0.0770 0.0199  -0.0732 402 ASP B CB  
5921 C CG  . ASP B 387 ? 0.4369 1.0492 0.2379 -0.0865 0.0244  -0.0731 402 ASP B CG  
5922 O OD1 . ASP B 387 ? 0.4572 1.0643 0.2388 -0.1111 0.0299  -0.0765 402 ASP B OD1 
5923 O OD2 . ASP B 387 ? 0.4375 1.0384 0.2359 -0.0695 0.0230  -0.0701 402 ASP B OD2 
5924 N N   . PRO B 388 ? 0.4606 1.0702 0.2468 -0.1494 0.0257  -0.0769 403 PRO B N   
5925 C CA  . PRO B 388 ? 0.4769 1.1081 0.2518 -0.1749 0.0386  -0.0884 403 PRO B CA  
5926 C C   . PRO B 388 ? 0.4857 1.1438 0.2533 -0.1771 0.0534  -0.1000 403 PRO B C   
5927 O O   . PRO B 388 ? 0.5021 1.1870 0.2650 -0.1965 0.0663  -0.1119 403 PRO B O   
5928 C CB  . PRO B 388 ? 0.5052 1.0844 0.2479 -0.2017 0.0314  -0.0781 403 PRO B CB  
5929 C CG  . PRO B 388 ? 0.5111 1.0446 0.2451 -0.1902 0.0162  -0.0626 403 PRO B CG  
5930 C CD  . PRO B 388 ? 0.4790 1.0313 0.2429 -0.1581 0.0121  -0.0616 403 PRO B CD  
5931 N N   . LYS B 389 ? 0.4880 1.1403 0.2551 -0.1578 0.0527  -0.0977 404 LYS B N   
5932 C CA  . LYS B 389 ? 0.5116 1.1911 0.2738 -0.1571 0.0678  -0.1104 404 LYS B CA  
5933 C C   . LYS B 389 ? 0.4791 1.2208 0.2758 -0.1360 0.0767  -0.1249 404 LYS B C   
5934 O O   . LYS B 389 ? 0.4918 1.2689 0.2909 -0.1375 0.0912  -0.1393 404 LYS B O   
5935 C CB  . LYS B 389 ? 0.5413 1.1859 0.2848 -0.1468 0.0643  -0.1031 404 LYS B CB  
5936 C CG  . LYS B 389 ? 0.5723 1.2388 0.3069 -0.1463 0.0806  -0.1165 404 LYS B CG  
5937 C CD  . LYS B 389 ? 0.5940 1.2205 0.3039 -0.1411 0.0779  -0.1098 404 LYS B CD  
5938 C CE  . LYS B 389 ? 0.6173 1.2698 0.3198 -0.1407 0.0966  -0.1260 404 LYS B CE  
5939 N NZ  . LYS B 389 ? 0.6691 1.2841 0.3297 -0.1665 0.1010  -0.1240 404 LYS B NZ  
5940 N N   . HIS B 390 ? 0.4481 1.2034 0.2708 -0.1164 0.0679  -0.1216 405 HIS B N   
5941 C CA  . HIS B 390 ? 0.4150 1.2281 0.2697 -0.0945 0.0734  -0.1341 405 HIS B CA  
5942 C C   . HIS B 390 ? 0.4032 1.2460 0.2782 -0.1000 0.0711  -0.1383 405 HIS B C   
5943 O O   . HIS B 390 ? 0.3781 1.2716 0.2788 -0.0848 0.0748  -0.1492 405 HIS B O   
5944 C CB  . HIS B 390 ? 0.3885 1.1957 0.2550 -0.0602 0.0660  -0.1280 405 HIS B CB  
5945 C CG  . HIS B 390 ? 0.4075 1.1885 0.2553 -0.0526 0.0690  -0.1257 405 HIS B CG  
5946 N ND1 . HIS B 390 ? 0.4216 1.2299 0.2676 -0.0495 0.0830  -0.1393 405 HIS B ND1 
5947 C CD2 . HIS B 390 ? 0.4096 1.1394 0.2387 -0.0490 0.0604  -0.1122 405 HIS B CD2 
5948 C CE1 . HIS B 390 ? 0.4309 1.2040 0.2567 -0.0434 0.0829  -0.1343 405 HIS B CE1 
5949 N NE2 . HIS B 390 ? 0.4324 1.1581 0.2477 -0.0434 0.0689  -0.1177 405 HIS B NE2 
5950 N N   . TRP B 391 ? 0.4235 1.2353 0.2863 -0.1217 0.0648  -0.1303 406 TRP B N   
5951 C CA  . TRP B 391 ? 0.4275 1.2627 0.3063 -0.1294 0.0631  -0.1347 406 TRP B CA  
5952 C C   . TRP B 391 ? 0.4752 1.2918 0.3325 -0.1654 0.0671  -0.1357 406 TRP B C   
5953 O O   . TRP B 391 ? 0.4976 1.2608 0.3282 -0.1787 0.0614  -0.1237 406 TRP B O   
5954 C CB  . TRP B 391 ? 0.4032 1.2110 0.2904 -0.1146 0.0485  -0.1220 406 TRP B CB  
5955 C CG  . TRP B 391 ? 0.3809 1.1988 0.2855 -0.0812 0.0433  -0.1188 406 TRP B CG  
5956 C CD1 . TRP B 391 ? 0.3859 1.1665 0.2830 -0.0650 0.0357  -0.1067 406 TRP B CD1 
5957 C CD2 . TRP B 391 ? 0.3666 1.2325 0.2971 -0.0604 0.0441  -0.1273 406 TRP B CD2 
5958 N NE1 . TRP B 391 ? 0.3695 1.1697 0.2845 -0.0360 0.0330  -0.1070 406 TRP B NE1 
5959 C CE2 . TRP B 391 ? 0.3624 1.2140 0.2974 -0.0318 0.0374  -0.1191 406 TRP B CE2 
5960 C CE3 . TRP B 391 ? 0.3579 1.2771 0.3071 -0.0637 0.0494  -0.1410 406 TRP B CE3 
5961 C CZ2 . TRP B 391 ? 0.3529 1.2384 0.3079 -0.0060 0.0353  -0.1232 406 TRP B CZ2 
5962 C CZ3 . TRP B 391 ? 0.3512 1.3072 0.3223 -0.0376 0.0465  -0.1455 406 TRP B CZ3 
5963 C CH2 . TRP B 391 ? 0.3472 1.2847 0.3200 -0.0084 0.0393  -0.1361 406 TRP B CH2 
5964 N N   . ASP B 392 ? 0.5081 1.3665 0.3756 -0.1814 0.0759  -0.1493 407 ASP B N   
5965 C CA  . ASP B 392 ? 0.5858 1.4247 0.4308 -0.2177 0.0804  -0.1506 407 ASP B CA  
5966 C C   . ASP B 392 ? 0.5992 1.4063 0.4430 -0.2222 0.0687  -0.1413 407 ASP B C   
5967 O O   . ASP B 392 ? 0.6047 1.4406 0.4729 -0.2098 0.0655  -0.1456 407 ASP B O   
5968 C CB  . ASP B 392 ? 0.6207 1.5168 0.4760 -0.2366 0.0956  -0.1700 407 ASP B CB  
5969 C CG  . ASP B 392 ? 0.6902 1.5610 0.5146 -0.2772 0.1029  -0.1715 407 ASP B CG  
5970 O OD1 . ASP B 392 ? 0.7854 1.6314 0.5826 -0.2914 0.1091  -0.1693 407 ASP B OD1 
5971 O OD2 . ASP B 392 ? 0.6935 1.5660 0.5178 -0.2955 0.1026  -0.1748 407 ASP B OD2 
5972 N N   . GLN B 393 ? 0.6564 1.4043 0.4708 -0.2403 0.0624  -0.1292 408 GLN B N   
5973 C CA  . GLN B 393 ? 0.6797 1.3899 0.4916 -0.2426 0.0504  -0.1194 408 GLN B CA  
5974 C C   . GLN B 393 ? 0.6305 1.3497 0.4713 -0.2099 0.0402  -0.1146 408 GLN B C   
5975 O O   . GLN B 393 ? 0.6106 1.3474 0.4685 -0.2067 0.0383  -0.1190 408 GLN B O   
5976 C CB  . GLN B 393 ? 0.7342 1.4567 0.5416 -0.2699 0.0572  -0.1292 408 GLN B CB  
5977 C CG  . GLN B 393 ? 0.8249 1.5219 0.5961 -0.3059 0.0655  -0.1306 408 GLN B CG  
5978 C CD  . GLN B 393 ? 0.8775 1.5568 0.6343 -0.3338 0.0669  -0.1336 408 GLN B CD  
5979 O OE1 . GLN B 393 ? 0.9205 1.5967 0.6920 -0.3256 0.0597  -0.1325 408 GLN B OE1 
5980 N NE2 . GLN B 393 ? 0.9068 1.5726 0.6327 -0.3680 0.0770  -0.1378 408 GLN B NE2 
5981 N N   . PRO B 394 ? 0.5805 1.2852 0.4241 -0.1870 0.0340  -0.1056 409 PRO B N   
5982 C CA  . PRO B 394 ? 0.5398 1.2498 0.4069 -0.1568 0.0254  -0.1004 409 PRO B CA  
5983 C C   . PRO B 394 ? 0.5282 1.2080 0.3999 -0.1555 0.0148  -0.0924 409 PRO B C   
5984 O O   . PRO B 394 ? 0.4822 1.1723 0.3742 -0.1344 0.0099  -0.0908 409 PRO B O   
5985 C CB  . PRO B 394 ? 0.5344 1.2172 0.3925 -0.1424 0.0205  -0.0902 409 PRO B CB  
5986 C CG  . PRO B 394 ? 0.5659 1.2134 0.3927 -0.1666 0.0217  -0.0859 409 PRO B CG  
5987 C CD  . PRO B 394 ? 0.5880 1.2623 0.4077 -0.1919 0.0340  -0.0987 409 PRO B CD  
5988 N N   . GLU B 395 ? 0.5705 1.2112 0.4216 -0.1779 0.0115  -0.0877 410 GLU B N   
5989 C CA  . GLU B 395 ? 0.5863 1.1934 0.4398 -0.1769 0.0016  -0.0804 410 GLU B CA  
5990 C C   . GLU B 395 ? 0.5791 1.2072 0.4399 -0.1893 0.0067  -0.0910 410 GLU B C   
5991 O O   . GLU B 395 ? 0.5639 1.1778 0.4343 -0.1831 0.0006  -0.0887 410 GLU B O   
5992 C CB  . GLU B 395 ? 0.6320 1.1784 0.4588 -0.1900 -0.0078 -0.0676 410 GLU B CB  
5993 C CG  . GLU B 395 ? 0.6956 1.2226 0.4923 -0.2221 -0.0026 -0.0703 410 GLU B CG  
5994 C CD  . GLU B 395 ? 0.7278 1.2928 0.5163 -0.2364 0.0122  -0.0817 410 GLU B CD  
5995 O OE1 . GLU B 395 ? 0.7052 1.2842 0.4952 -0.2255 0.0149  -0.0812 410 GLU B OE1 
5996 O OE2 . GLU B 395 ? 0.7924 1.3746 0.5735 -0.2592 0.0220  -0.0922 410 GLU B OE2 
5997 N N   . GLN B 396 ? 0.6098 1.2733 0.4669 -0.2073 0.0183  -0.1038 411 GLN B N   
5998 C CA  . GLN B 396 ? 0.6044 1.2933 0.4706 -0.2183 0.0230  -0.1151 411 GLN B CA  
5999 C C   . GLN B 396 ? 0.5448 1.2917 0.4417 -0.1966 0.0257  -0.1244 411 GLN B C   
6000 O O   . GLN B 396 ? 0.5111 1.2898 0.4186 -0.1811 0.0287  -0.1267 411 GLN B O   
6001 C CB  . GLN B 396 ? 0.6454 1.3414 0.4917 -0.2520 0.0337  -0.1247 411 GLN B CB  
6002 C CG  . GLN B 396 ? 0.6888 1.3885 0.5356 -0.2687 0.0359  -0.1331 411 GLN B CG  
6003 C CD  . GLN B 396 ? 0.7491 1.4274 0.5661 -0.3061 0.0433  -0.1376 411 GLN B CD  
6004 O OE1 . GLN B 396 ? 0.7992 1.4629 0.5940 -0.3213 0.0479  -0.1350 411 GLN B OE1 
6005 N NE2 . GLN B 396 ? 0.7397 1.4139 0.5534 -0.3225 0.0451  -0.1446 411 GLN B NE2 
6006 N N   . PHE B 397 ? 0.5236 1.2811 0.4328 -0.1946 0.0238  -0.1292 412 PHE B N   
6007 C CA  . PHE B 397 ? 0.5259 1.3338 0.4609 -0.1737 0.0243  -0.1366 412 PHE B CA  
6008 C C   . PHE B 397 ? 0.5269 1.3955 0.4706 -0.1868 0.0341  -0.1538 412 PHE B C   
6009 O O   . PHE B 397 ? 0.5322 1.4121 0.4746 -0.2061 0.0374  -0.1632 412 PHE B O   
6010 C CB  . PHE B 397 ? 0.5453 1.3380 0.4889 -0.1647 0.0178  -0.1343 412 PHE B CB  
6011 C CG  . PHE B 397 ? 0.5350 1.3738 0.5006 -0.1442 0.0170  -0.1407 412 PHE B CG  
6012 C CD1 . PHE B 397 ? 0.5447 1.3845 0.5211 -0.1156 0.0118  -0.1329 412 PHE B CD1 
6013 C CD2 . PHE B 397 ? 0.5281 1.4072 0.5014 -0.1544 0.0210  -0.1543 412 PHE B CD2 
6014 C CE1 . PHE B 397 ? 0.5246 1.4022 0.5169 -0.0967 0.0103  -0.1376 412 PHE B CE1 
6015 C CE2 . PHE B 397 ? 0.5373 1.4576 0.5283 -0.1352 0.0188  -0.1595 412 PHE B CE2 
6016 C CZ  . PHE B 397 ? 0.5221 1.4403 0.5216 -0.1060 0.0132  -0.1507 412 PHE B CZ  
6017 N N   . ASN B 398 ? 0.5023 1.4105 0.4559 -0.1758 0.0386  -0.1587 413 ASN B N   
6018 C CA  . ASN B 398 ? 0.4918 1.4607 0.4561 -0.1874 0.0482  -0.1756 413 ASN B CA  
6019 C C   . ASN B 398 ? 0.4735 1.5006 0.4634 -0.1596 0.0478  -0.1826 413 ASN B C   
6020 O O   . ASN B 398 ? 0.4701 1.5149 0.4629 -0.1509 0.0525  -0.1845 413 ASN B O   
6021 C CB  . ASN B 398 ? 0.5024 1.4644 0.4482 -0.2125 0.0582  -0.1789 413 ASN B CB  
6022 C CG  . ASN B 398 ? 0.5067 1.5246 0.4602 -0.2351 0.0695  -0.1977 413 ASN B CG  
6023 O OD1 . ASN B 398 ? 0.4960 1.5557 0.4680 -0.2332 0.0686  -0.2079 413 ASN B OD1 
6024 N ND2 . ASN B 398 ? 0.5102 1.5305 0.4491 -0.2576 0.0805  -0.2030 413 ASN B ND2 
6025 N N   . PRO B 399 ? 0.4627 1.5198 0.4700 -0.1463 0.0424  -0.1872 414 PRO B N   
6026 C CA  . PRO B 399 ? 0.4421 1.5552 0.4726 -0.1194 0.0400  -0.1940 414 PRO B CA  
6027 C C   . PRO B 399 ? 0.4285 1.6007 0.4721 -0.1245 0.0491  -0.2093 414 PRO B C   
6028 O O   . PRO B 399 ? 0.3935 1.6024 0.4536 -0.0986 0.0475  -0.2126 414 PRO B O   
6029 C CB  . PRO B 399 ? 0.4277 1.5633 0.4686 -0.1182 0.0343  -0.1996 414 PRO B CB  
6030 C CG  . PRO B 399 ? 0.4420 1.5241 0.4659 -0.1359 0.0325  -0.1925 414 PRO B CG  
6031 C CD  . PRO B 399 ? 0.4673 1.5047 0.4707 -0.1568 0.0380  -0.1865 414 PRO B CD  
6032 N N   . GLU B 400 ? 0.4465 1.6275 0.4826 -0.1575 0.0590  -0.2189 415 GLU B N   
6033 C CA  . GLU B 400 ? 0.4764 1.7156 0.5260 -0.1652 0.0694  -0.2350 415 GLU B CA  
6034 C C   . GLU B 400 ? 0.4600 1.6919 0.5068 -0.1498 0.0739  -0.2310 415 GLU B C   
6035 O O   . GLU B 400 ? 0.4588 1.7441 0.5233 -0.1420 0.0804  -0.2436 415 GLU B O   
6036 C CB  . GLU B 400 ? 0.5236 1.7698 0.5622 -0.2079 0.0806  -0.2462 415 GLU B CB  
6037 C CG  . GLU B 400 ? 0.5438 1.8461 0.6006 -0.2205 0.0810  -0.2623 415 GLU B CG  
6038 C CD  . GLU B 400 ? 0.6028 1.8730 0.6391 -0.2565 0.0836  -0.2634 415 GLU B CD  
6039 O OE1 . GLU B 400 ? 0.6638 1.8740 0.6829 -0.2541 0.0760  -0.2494 415 GLU B OE1 
6040 O OE2 . GLU B 400 ? 0.6212 1.9273 0.6594 -0.2867 0.0935  -0.2791 415 GLU B OE2 
6041 N N   . ARG B 401 ? 0.4555 1.6232 0.4811 -0.1441 0.0700  -0.2142 416 ARG B N   
6042 C CA  . ARG B 401 ? 0.4314 1.5858 0.4513 -0.1291 0.0734  -0.2094 416 ARG B CA  
6043 C C   . ARG B 401 ? 0.4117 1.6050 0.4546 -0.0910 0.0690  -0.2124 416 ARG B C   
6044 O O   . ARG B 401 ? 0.3993 1.6039 0.4441 -0.0787 0.0747  -0.2156 416 ARG B O   
6045 C CB  . ARG B 401 ? 0.4243 1.5030 0.4188 -0.1284 0.0671  -0.1902 416 ARG B CB  
6046 C CG  . ARG B 401 ? 0.4074 1.4630 0.4075 -0.0964 0.0546  -0.1773 416 ARG B CG  
6047 C CD  . ARG B 401 ? 0.4091 1.3956 0.3892 -0.1012 0.0468  -0.1602 416 ARG B CD  
6048 N NE  . ARG B 401 ? 0.4334 1.3798 0.3886 -0.1248 0.0514  -0.1554 416 ARG B NE  
6049 C CZ  . ARG B 401 ? 0.4397 1.3471 0.3769 -0.1498 0.0497  -0.1502 416 ARG B CZ  
6050 N NH1 . ARG B 401 ? 0.4390 1.3410 0.3813 -0.1547 0.0446  -0.1498 416 ARG B NH1 
6051 N NH2 . ARG B 401 ? 0.4486 1.3193 0.3606 -0.1695 0.0529  -0.1453 416 ARG B NH2 
6052 N N   . PHE B 402 ? 0.4060 1.6163 0.4637 -0.0726 0.0587  -0.2112 417 PHE B N   
6053 C CA  . PHE B 402 ? 0.4015 1.6511 0.4798 -0.0370 0.0530  -0.2146 417 PHE B CA  
6054 C C   . PHE B 402 ? 0.4375 1.7654 0.5425 -0.0385 0.0561  -0.2341 417 PHE B C   
6055 O O   . PHE B 402 ? 0.4074 1.7759 0.5316 -0.0094 0.0512  -0.2392 417 PHE B O   
6056 C CB  . PHE B 402 ? 0.3740 1.5977 0.4508 -0.0158 0.0397  -0.2020 417 PHE B CB  
6057 C CG  . PHE B 402 ? 0.3756 1.5306 0.4317 -0.0087 0.0357  -0.1839 417 PHE B CG  
6058 C CD1 . PHE B 402 ? 0.3731 1.4785 0.4121 -0.0306 0.0347  -0.1747 417 PHE B CD1 
6059 C CD2 . PHE B 402 ? 0.3693 1.5090 0.4229 0.0200  0.0328  -0.1764 417 PHE B CD2 
6060 C CE1 . PHE B 402 ? 0.3710 1.4174 0.3938 -0.0240 0.0304  -0.1589 417 PHE B CE1 
6061 C CE2 . PHE B 402 ? 0.3652 1.4440 0.4004 0.0246  0.0293  -0.1605 417 PHE B CE2 
6062 C CZ  . PHE B 402 ? 0.3718 1.4061 0.3931 0.0027  0.0278  -0.1520 417 PHE B CZ  
6063 N N   . LEU B 403 ? 0.5009 1.8489 0.6063 -0.0726 0.0637  -0.2449 418 LEU B N   
6064 C CA  . LEU B 403 ? 0.5501 1.9752 0.6807 -0.0807 0.0698  -0.2657 418 LEU B CA  
6065 C C   . LEU B 403 ? 0.6516 2.1014 0.7851 -0.0929 0.0852  -0.2776 418 LEU B C   
6066 O O   . LEU B 403 ? 0.6810 2.1169 0.7991 -0.1281 0.0969  -0.2815 418 LEU B O   
6067 C CB  . LEU B 403 ? 0.5175 1.9581 0.6485 -0.1119 0.0702  -0.2736 418 LEU B CB  
6068 C CG  . LEU B 403 ? 0.4831 1.9148 0.6161 -0.0977 0.0557  -0.2663 418 LEU B CG  
6069 C CD1 . LEU B 403 ? 0.4834 1.9278 0.6145 -0.1311 0.0576  -0.2753 418 LEU B CD1 
6070 C CD2 . LEU B 403 ? 0.4618 1.9447 0.6198 -0.0608 0.0457  -0.2707 418 LEU B CD2 
6071 N N   . GLU B 404 ? 0.7411 2.2204 0.8911 -0.0617 0.0851  -0.2817 419 GLU B N   
6072 C CA  . GLU B 404 ? 0.7669 2.3152 0.9411 -0.0624 0.0965  -0.3022 419 GLU B CA  
6073 C C   . GLU B 404 ? 0.7638 2.3711 0.9701 -0.0260 0.0850  -0.3095 419 GLU B C   
6074 O O   . GLU B 404 ? 0.8045 2.4861 1.0396 -0.0297 0.0884  -0.3287 419 GLU B O   
6075 C CB  . GLU B 404 ? 0.7782 2.3052 0.9411 -0.0574 0.1080  -0.3015 419 GLU B CB  
6076 C CG  . GLU B 404 ? 0.7869 2.3765 0.9682 -0.0721 0.1251  -0.3240 419 GLU B CG  
6077 C CD  . GLU B 404 ? 0.8035 2.3521 0.9572 -0.0950 0.1405  -0.3221 419 GLU B CD  
6078 O OE1 . GLU B 404 ? 0.8026 2.3100 0.9295 -0.1309 0.1449  -0.3159 419 GLU B OE1 
6079 O OE2 . GLU B 404 ? 0.8372 2.3925 0.9938 -0.0772 0.1481  -0.3267 419 GLU B OE2 
6080 N N   . PRO B 405 ? 0.7413 2.3140 0.9412 0.0083  0.0712  -0.2940 420 PRO B N   
6081 C CA  . PRO B 405 ? 0.7123 2.3244 0.9338 0.0432  0.0565  -0.2958 420 PRO B CA  
6082 C C   . PRO B 405 ? 0.7418 2.3460 0.9589 0.0343  0.0445  -0.2897 420 PRO B C   
6083 O O   . PRO B 405 ? 0.7261 2.2652 0.9176 0.0263  0.0407  -0.2732 420 PRO B O   
6084 C CB  . PRO B 405 ? 0.6932 2.2657 0.9047 0.0827  0.0489  -0.2817 420 PRO B CB  
6085 N N   . GLN B 412 ? 0.8219 1.8347 0.7992 0.0030  0.0666  -0.1657 427 GLN B N   
6086 C CA  . GLN B 412 ? 0.8087 1.8591 0.8096 0.0279  0.0601  -0.1692 427 GLN B CA  
6087 C C   . GLN B 412 ? 0.7824 1.8400 0.7883 0.0630  0.0591  -0.1700 427 GLN B C   
6088 O O   . GLN B 412 ? 0.8244 1.9185 0.8490 0.0865  0.0545  -0.1750 427 GLN B O   
6089 C CB  . GLN B 412 ? 0.8164 1.9311 0.8394 0.0169  0.0654  -0.1860 427 GLN B CB  
6090 C CG  . GLN B 412 ? 0.8394 1.9479 0.8574 -0.0166 0.0657  -0.1860 427 GLN B CG  
6091 C CD  . GLN B 412 ? 0.8963 1.9850 0.8943 -0.0495 0.0764  -0.1883 427 GLN B CD  
6092 O OE1 . GLN B 412 ? 0.9566 2.0363 0.9437 -0.0485 0.0841  -0.1902 427 GLN B OE1 
6093 N NE2 . GLN B 412 ? 0.9125 1.9916 0.9028 -0.0793 0.0770  -0.1883 427 GLN B NE2 
6094 N N   . SER B 413 ? 0.7399 1.7621 0.7273 0.0660  0.0634  -0.1656 428 SER B N   
6095 C CA  . SER B 413 ? 0.7263 1.7314 0.7095 0.0979  0.0603  -0.1610 428 SER B CA  
6096 C C   . SER B 413 ? 0.7123 1.6496 0.6720 0.0962  0.0529  -0.1428 428 SER B C   
6097 O O   . SER B 413 ? 0.7591 1.6725 0.7129 0.1202  0.0476  -0.1353 428 SER B O   
6098 C CB  . SER B 413 ? 0.7593 1.7821 0.7410 0.1051  0.0725  -0.1733 428 SER B CB  
6099 O OG  . SER B 413 ? 0.7427 1.7182 0.6977 0.0887  0.0775  -0.1674 428 SER B OG  
6100 N N   . SER B 414 ? 0.6258 1.5315 0.5713 0.0676  0.0525  -0.1361 429 SER B N   
6101 C CA  . SER B 414 ? 0.5549 1.4036 0.4839 0.0644  0.0436  -0.1195 429 SER B CA  
6102 C C   . SER B 414 ? 0.5108 1.3618 0.4520 0.0625  0.0344  -0.1135 429 SER B C   
6103 O O   . SER B 414 ? 0.4819 1.3129 0.4184 0.0408  0.0310  -0.1080 429 SER B O   
6104 C CB  . SER B 414 ? 0.5622 1.3750 0.4692 0.0367  0.0463  -0.1152 429 SER B CB  
6105 O OG  . SER B 414 ? 0.5525 1.3768 0.4613 0.0101  0.0479  -0.1184 429 SER B OG  
6106 N N   . PHE B 415 ? 0.4902 1.3655 0.4458 0.0863  0.0305  -0.1152 430 PHE B N   
6107 C CA  . PHE B 415 ? 0.4681 1.3535 0.4359 0.0867  0.0232  -0.1122 430 PHE B CA  
6108 C C   . PHE B 415 ? 0.4611 1.3384 0.4296 0.1161  0.0168  -0.1059 430 PHE B C   
6109 O O   . PHE B 415 ? 0.4418 1.3501 0.4182 0.1381  0.0178  -0.1128 430 PHE B O   
6110 C CB  . PHE B 415 ? 0.4684 1.4105 0.4549 0.0795  0.0269  -0.1263 430 PHE B CB  
6111 C CG  . PHE B 415 ? 0.4571 1.4143 0.4555 0.0832  0.0196  -0.1250 430 PHE B CG  
6112 C CD1 . PHE B 415 ? 0.4726 1.4040 0.4674 0.0643  0.0157  -0.1183 430 PHE B CD1 
6113 C CD2 . PHE B 415 ? 0.4451 1.4411 0.4575 0.1062  0.0161  -0.1307 430 PHE B CD2 
6114 C CE1 . PHE B 415 ? 0.4584 1.4023 0.4626 0.0671  0.0099  -0.1180 430 PHE B CE1 
6115 C CE2 . PHE B 415 ? 0.4470 1.4551 0.4672 0.1086  0.0091  -0.1295 430 PHE B CE2 
6116 C CZ  . PHE B 415 ? 0.4288 1.4112 0.4448 0.0883  0.0068  -0.1237 430 PHE B CZ  
6117 N N   . LEU B 416 ? 0.4480 1.2814 0.4068 0.1161  0.0105  -0.0926 431 LEU B N   
6118 C CA  . LEU B 416 ? 0.4469 1.2628 0.4014 0.1399  0.0050  -0.0847 431 LEU B CA  
6119 C C   . LEU B 416 ? 0.4416 1.2379 0.3981 0.1336  -0.0015 -0.0759 431 LEU B C   
6120 O O   . LEU B 416 ? 0.4443 1.1989 0.3914 0.1286  -0.0041 -0.0656 431 LEU B O   
6121 C CB  . LEU B 416 ? 0.4559 1.2309 0.3921 0.1477  0.0062  -0.0777 431 LEU B CB  
6122 C CG  . LEU B 416 ? 0.4769 1.2655 0.4086 0.1541  0.0138  -0.0866 431 LEU B CG  
6123 C CD1 . LEU B 416 ? 0.5165 1.2572 0.4272 0.1508  0.0153  -0.0794 431 LEU B CD1 
6124 C CD2 . LEU B 416 ? 0.4720 1.2897 0.4098 0.1834  0.0139  -0.0930 431 LEU B CD2 
6125 N N   . PRO B 417 ? 0.4284 1.2566 0.3978 0.1341  -0.0038 -0.0809 432 PRO B N   
6126 C CA  . PRO B 417 ? 0.3962 1.2089 0.3682 0.1266  -0.0084 -0.0748 432 PRO B CA  
6127 C C   . PRO B 417 ? 0.3897 1.1768 0.3531 0.1450  -0.0125 -0.0651 432 PRO B C   
6128 O O   . PRO B 417 ? 0.4132 1.1734 0.3753 0.1378  -0.0148 -0.0579 432 PRO B O   
6129 C CB  . PRO B 417 ? 0.3915 1.2494 0.3777 0.1219  -0.0087 -0.0850 432 PRO B CB  
6130 C CG  . PRO B 417 ? 0.4081 1.3062 0.3996 0.1386  -0.0071 -0.0941 432 PRO B CG  
6131 C CD  . PRO B 417 ? 0.4233 1.3052 0.4059 0.1419  -0.0023 -0.0933 432 PRO B CD  
6132 N N   . PHE B 418 ? 0.3789 1.1734 0.3358 0.1683  -0.0133 -0.0654 433 PHE B N   
6133 C CA  . PHE B 418 ? 0.3777 1.1472 0.3222 0.1859  -0.0168 -0.0564 433 PHE B CA  
6134 C C   . PHE B 418 ? 0.3815 1.1148 0.3094 0.1961  -0.0151 -0.0498 433 PHE B C   
6135 O O   . PHE B 418 ? 0.3997 1.1090 0.3131 0.2119  -0.0172 -0.0426 433 PHE B O   
6136 C CB  . PHE B 418 ? 0.3903 1.1927 0.3361 0.2071  -0.0208 -0.0608 433 PHE B CB  
6137 C CG  . PHE B 418 ? 0.3774 1.2142 0.3368 0.1982  -0.0233 -0.0671 433 PHE B CG  
6138 C CD1 . PHE B 418 ? 0.3742 1.1961 0.3296 0.1945  -0.0259 -0.0615 433 PHE B CD1 
6139 C CD2 . PHE B 418 ? 0.3562 1.2408 0.3317 0.1923  -0.0224 -0.0795 433 PHE B CD2 
6140 C CE1 . PHE B 418 ? 0.3578 1.2094 0.3236 0.1855  -0.0278 -0.0681 433 PHE B CE1 
6141 C CE2 . PHE B 418 ? 0.3404 1.2556 0.3269 0.1823  -0.0246 -0.0859 433 PHE B CE2 
6142 C CZ  . PHE B 418 ? 0.3537 1.2512 0.3346 0.1792  -0.0275 -0.0801 433 PHE B CZ  
6143 N N   . GLY B 419 ? 0.3627 1.0902 0.2898 0.1862  -0.0111 -0.0526 434 GLY B N   
6144 C CA  . GLY B 419 ? 0.3714 1.0636 0.2813 0.1933  -0.0089 -0.0475 434 GLY B CA  
6145 C C   . GLY B 419 ? 0.3884 1.0997 0.2942 0.2154  -0.0066 -0.0545 434 GLY B C   
6146 O O   . GLY B 419 ? 0.3918 1.1483 0.3117 0.2210  -0.0061 -0.0644 434 GLY B O   
6147 N N   . ALA B 420 ? 0.3917 1.0693 0.2787 0.2278  -0.0050 -0.0499 435 ALA B N   
6148 C CA  . ALA B 420 ? 0.3914 1.0803 0.2727 0.2501  -0.0022 -0.0566 435 ALA B CA  
6149 C C   . ALA B 420 ? 0.4210 1.0615 0.2766 0.2651  -0.0018 -0.0489 435 ALA B C   
6150 O O   . ALA B 420 ? 0.4338 1.0310 0.2760 0.2529  -0.0021 -0.0393 435 ALA B O   
6151 C CB  . ALA B 420 ? 0.3793 1.0907 0.2687 0.2392  0.0047  -0.0673 435 ALA B CB  
6152 N N   . GLY B 421 ? 0.4269 1.0749 0.2760 0.2916  -0.0012 -0.0536 436 GLY B N   
6153 C CA  . GLY B 421 ? 0.4496 1.0507 0.2717 0.3081  -0.0003 -0.0476 436 GLY B CA  
6154 C C   . GLY B 421 ? 0.4466 1.0187 0.2544 0.3146  -0.0063 -0.0355 436 GLY B C   
6155 O O   . GLY B 421 ? 0.4165 1.0131 0.2364 0.3136  -0.0113 -0.0344 436 GLY B O   
6156 N N   . PRO B 422 ? 0.4757 0.9942 0.2564 0.3185  -0.0052 -0.0269 437 PRO B N   
6157 C CA  . PRO B 422 ? 0.5061 0.9940 0.2669 0.3298  -0.0097 -0.0164 437 PRO B CA  
6158 C C   . PRO B 422 ? 0.5002 0.9912 0.2697 0.3119  -0.0128 -0.0097 437 PRO B C   
6159 O O   . PRO B 422 ? 0.5279 1.0116 0.2865 0.3228  -0.0168 -0.0038 437 PRO B O   
6160 C CB  . PRO B 422 ? 0.5310 0.9593 0.2621 0.3284  -0.0056 -0.0099 437 PRO B CB  
6161 C CG  . PRO B 422 ? 0.5284 0.9597 0.2626 0.3241  0.0002  -0.0183 437 PRO B CG  
6162 C CD  . PRO B 422 ? 0.4905 0.9717 0.2562 0.3075  0.0006  -0.0261 437 PRO B CD  
6163 N N   . ARG B 423 ? 0.4794 0.9796 0.2668 0.2855  -0.0108 -0.0108 438 ARG B N   
6164 C CA  . ARG B 423 ? 0.4611 0.9634 0.2595 0.2669  -0.0125 -0.0060 438 ARG B CA  
6165 C C   . ARG B 423 ? 0.4346 0.9872 0.2598 0.2608  -0.0149 -0.0131 438 ARG B C   
6166 O O   . ARG B 423 ? 0.4247 0.9838 0.2643 0.2414  -0.0153 -0.0119 438 ARG B O   
6167 C CB  . ARG B 423 ? 0.4606 0.9373 0.2612 0.2423  -0.0098 -0.0026 438 ARG B CB  
6168 C CG  . ARG B 423 ? 0.5021 0.9274 0.2762 0.2440  -0.0075 0.0049  438 ARG B CG  
6169 C CD  . ARG B 423 ? 0.5374 0.9459 0.2987 0.2505  -0.0087 0.0124  438 ARG B CD  
6170 N NE  . ARG B 423 ? 0.5711 0.9310 0.3098 0.2444  -0.0059 0.0204  438 ARG B NE  
6171 C CZ  . ARG B 423 ? 0.5945 0.9386 0.3303 0.2339  -0.0048 0.0266  438 ARG B CZ  
6172 N NH1 . ARG B 423 ? 0.5732 0.9447 0.3268 0.2288  -0.0063 0.0260  438 ARG B NH1 
6173 N NH2 . ARG B 423 ? 0.6587 0.9592 0.3732 0.2273  -0.0014 0.0328  438 ARG B NH2 
6174 N N   . VAL B 424 ? 0.4337 1.0223 0.2658 0.2775  -0.0167 -0.0209 439 VAL B N   
6175 C CA  . VAL B 424 ? 0.4140 1.0524 0.2704 0.2713  -0.0190 -0.0286 439 VAL B CA  
6176 C C   . VAL B 424 ? 0.4142 1.0541 0.2704 0.2695  -0.0230 -0.0235 439 VAL B C   
6177 O O   . VAL B 424 ? 0.4318 1.0408 0.2670 0.2799  -0.0247 -0.0149 439 VAL B O   
6178 C CB  . VAL B 424 ? 0.4117 1.0926 0.2771 0.2909  -0.0203 -0.0391 439 VAL B CB  
6179 C CG1 . VAL B 424 ? 0.4238 1.1078 0.2771 0.3175  -0.0270 -0.0362 439 VAL B CG1 
6180 C CG2 . VAL B 424 ? 0.3815 1.1132 0.2740 0.2760  -0.0196 -0.0497 439 VAL B CG2 
6181 N N   . CYS B 425 ? 0.3958 1.0690 0.2729 0.2547  -0.0238 -0.0290 440 CYS B N   
6182 C CA  . CYS B 425 ? 0.4122 1.0909 0.2903 0.2512  -0.0268 -0.0263 440 CYS B CA  
6183 C C   . CYS B 425 ? 0.4523 1.1383 0.3155 0.2760  -0.0326 -0.0246 440 CYS B C   
6184 O O   . CYS B 425 ? 0.4914 1.2133 0.3618 0.2907  -0.0364 -0.0319 440 CYS B O   
6185 C CB  . CYS B 425 ? 0.3870 1.1055 0.2891 0.2344  -0.0269 -0.0350 440 CYS B CB  
6186 S SG  . CYS B 425 ? 0.4144 1.1336 0.3179 0.2247  -0.0285 -0.0326 440 CYS B SG  
6187 N N   . VAL B 426 ? 0.4814 1.1340 0.3234 0.2808  -0.0334 -0.0151 441 VAL B N   
6188 C CA  . VAL B 426 ? 0.5175 1.1752 0.3421 0.3030  -0.0403 -0.0124 441 VAL B CA  
6189 C C   . VAL B 426 ? 0.4972 1.1964 0.3350 0.2987  -0.0450 -0.0184 441 VAL B C   
6190 O O   . VAL B 426 ? 0.5014 1.2185 0.3304 0.3176  -0.0528 -0.0190 441 VAL B O   
6191 C CB  . VAL B 426 ? 0.5543 1.1622 0.3471 0.3081  -0.0396 -0.0002 441 VAL B CB  
6192 C CG1 . VAL B 426 ? 0.5924 1.1634 0.3608 0.3269  -0.0397 0.0056  441 VAL B CG1 
6193 C CG2 . VAL B 426 ? 0.5442 1.1269 0.3404 0.2829  -0.0322 0.0038  441 VAL B CG2 
6194 N N   . GLY B 427 ? 0.4688 1.1810 0.3259 0.2745  -0.0408 -0.0227 442 GLY B N   
6195 C CA  . GLY B 427 ? 0.4596 1.2101 0.3296 0.2670  -0.0440 -0.0298 442 GLY B CA  
6196 C C   . GLY B 427 ? 0.4463 1.2485 0.3415 0.2639  -0.0461 -0.0423 442 GLY B C   
6197 O O   . GLY B 427 ? 0.4336 1.2689 0.3407 0.2546  -0.0483 -0.0495 442 GLY B O   
6198 N N   . GLU B 428 ? 0.4509 1.2610 0.3538 0.2700  -0.0446 -0.0459 443 GLU B N   
6199 C CA  . GLU B 428 ? 0.4436 1.3001 0.3711 0.2608  -0.0437 -0.0584 443 GLU B CA  
6200 C C   . GLU B 428 ? 0.4374 1.3428 0.3730 0.2689  -0.0513 -0.0665 443 GLU B C   
6201 O O   . GLU B 428 ? 0.4022 1.3371 0.3538 0.2505  -0.0504 -0.0747 443 GLU B O   
6202 C CB  . GLU B 428 ? 0.4588 1.3192 0.3907 0.2695  -0.0406 -0.0620 443 GLU B CB  
6203 C CG  . GLU B 428 ? 0.4563 1.3634 0.4125 0.2568  -0.0375 -0.0755 443 GLU B CG  
6204 C CD  . GLU B 428 ? 0.4886 1.4012 0.4479 0.2660  -0.0333 -0.0802 443 GLU B CD  
6205 O OE1 . GLU B 428 ? 0.5587 1.4433 0.5015 0.2867  -0.0346 -0.0738 443 GLU B OE1 
6206 O OE2 . GLU B 428 ? 0.4833 1.4266 0.4597 0.2523  -0.0282 -0.0907 443 GLU B OE2 
6207 N N   . SER B 429 ? 0.4761 1.3887 0.3997 0.2957  -0.0595 -0.0643 444 SER B N   
6208 C CA  . SER B 429 ? 0.5060 1.4652 0.4358 0.3048  -0.0691 -0.0712 444 SER B CA  
6209 C C   . SER B 429 ? 0.5198 1.4769 0.4459 0.2863  -0.0694 -0.0704 444 SER B C   
6210 O O   . SER B 429 ? 0.5287 1.5263 0.4719 0.2720  -0.0705 -0.0807 444 SER B O   
6211 C CB  . SER B 429 ? 0.5270 1.4801 0.4364 0.3371  -0.0797 -0.0650 444 SER B CB  
6212 O OG  . SER B 429 ? 0.5497 1.5383 0.4725 0.3576  -0.0840 -0.0729 444 SER B OG  
6213 N N   . LEU B 430 ? 0.5186 1.4279 0.4215 0.2861  -0.0677 -0.0587 445 LEU B N   
6214 C CA  . LEU B 430 ? 0.5195 1.4225 0.4168 0.2698  -0.0665 -0.0579 445 LEU B CA  
6215 C C   . LEU B 430 ? 0.4590 1.3826 0.3807 0.2420  -0.0598 -0.0677 445 LEU B C   
6216 O O   . LEU B 430 ? 0.4437 1.4020 0.3744 0.2324  -0.0627 -0.0766 445 LEU B O   
6217 C CB  . LEU B 430 ? 0.5534 1.3993 0.4274 0.2680  -0.0613 -0.0452 445 LEU B CB  
6218 C CG  . LEU B 430 ? 0.5777 1.4094 0.4483 0.2478  -0.0559 -0.0448 445 LEU B CG  
6219 C CD1 . LEU B 430 ? 0.5988 1.4642 0.4662 0.2479  -0.0630 -0.0511 445 LEU B CD1 
6220 C CD2 . LEU B 430 ? 0.6058 1.3847 0.4512 0.2504  -0.0513 -0.0325 445 LEU B CD2 
6221 N N   . ALA B 431 ? 0.4206 1.3224 0.3515 0.2293  -0.0516 -0.0663 446 ALA B N   
6222 C CA  . ALA B 431 ? 0.3890 1.2977 0.3378 0.2024  -0.0452 -0.0732 446 ALA B CA  
6223 C C   . ALA B 431 ? 0.3725 1.3334 0.3412 0.1947  -0.0470 -0.0867 446 ALA B C   
6224 O O   . ALA B 431 ? 0.3278 1.3065 0.3059 0.1755  -0.0453 -0.0946 446 ALA B O   
6225 C CB  . ALA B 431 ? 0.3725 1.2452 0.3243 0.1924  -0.0380 -0.0678 446 ALA B CB  
6226 N N   . ARG B 432 ? 0.4112 1.3969 0.3862 0.2091  -0.0497 -0.0903 447 ARG B N   
6227 C CA  . ARG B 432 ? 0.4267 1.4654 0.4222 0.2014  -0.0502 -0.1042 447 ARG B CA  
6228 C C   . ARG B 432 ? 0.4455 1.5216 0.4437 0.1995  -0.0571 -0.1117 447 ARG B C   
6229 O O   . ARG B 432 ? 0.4825 1.5805 0.4921 0.1770  -0.0544 -0.1211 447 ARG B O   
6230 C CB  . ARG B 432 ? 0.4323 1.4939 0.4340 0.2219  -0.0523 -0.1074 447 ARG B CB  
6231 C CG  . ARG B 432 ? 0.4290 1.4601 0.4301 0.2174  -0.0440 -0.1035 447 ARG B CG  
6232 C CD  . ARG B 432 ? 0.4363 1.4894 0.4431 0.2379  -0.0445 -0.1081 447 ARG B CD  
6233 N NE  . ARG B 432 ? 0.4367 1.4727 0.4464 0.2258  -0.0351 -0.1089 447 ARG B NE  
6234 C CZ  . ARG B 432 ? 0.4193 1.4769 0.4433 0.2019  -0.0283 -0.1183 447 ARG B CZ  
6235 N NH1 . ARG B 432 ? 0.4079 1.5066 0.4462 0.1867  -0.0292 -0.1286 447 ARG B NH1 
6236 N NH2 . ARG B 432 ? 0.4012 1.4372 0.4227 0.1920  -0.0204 -0.1174 447 ARG B NH2 
6237 N N   . ILE B 433 ? 0.4481 1.5275 0.4328 0.2225  -0.0664 -0.1070 448 ILE B N   
6238 C CA  . ILE B 433 ? 0.4391 1.5508 0.4217 0.2232  -0.0749 -0.1126 448 ILE B CA  
6239 C C   . ILE B 433 ? 0.4417 1.5341 0.4192 0.1983  -0.0695 -0.1132 448 ILE B C   
6240 O O   . ILE B 433 ? 0.4450 1.5697 0.4331 0.1808  -0.0698 -0.1243 448 ILE B O   
6241 C CB  . ILE B 433 ? 0.4461 1.5448 0.4058 0.2515  -0.0853 -0.1029 448 ILE B CB  
6242 C CG1 . ILE B 433 ? 0.4558 1.5857 0.4230 0.2788  -0.0935 -0.1056 448 ILE B CG1 
6243 C CG2 . ILE B 433 ? 0.4442 1.5563 0.3924 0.2475  -0.0925 -0.1050 448 ILE B CG2 
6244 C CD1 . ILE B 433 ? 0.4900 1.5859 0.4309 0.3086  -0.1009 -0.0924 448 ILE B CD1 
6245 N N   . GLU B 434 ? 0.4399 1.4792 0.4012 0.1972  -0.0643 -0.1017 449 GLU B N   
6246 C CA  . GLU B 434 ? 0.4392 1.4547 0.3942 0.1778  -0.0587 -0.1013 449 GLU B CA  
6247 C C   . GLU B 434 ? 0.4106 1.4428 0.3851 0.1507  -0.0524 -0.1125 449 GLU B C   
6248 O O   . GLU B 434 ? 0.4127 1.4583 0.3878 0.1354  -0.0520 -0.1202 449 GLU B O   
6249 C CB  . GLU B 434 ? 0.4623 1.4212 0.4047 0.1795  -0.0520 -0.0886 449 GLU B CB  
6250 C CG  . GLU B 434 ? 0.4790 1.4077 0.4091 0.1684  -0.0470 -0.0855 449 GLU B CG  
6251 C CD  . GLU B 434 ? 0.5037 1.3823 0.4200 0.1754  -0.0420 -0.0726 449 GLU B CD  
6252 O OE1 . GLU B 434 ? 0.4820 1.3372 0.4085 0.1673  -0.0357 -0.0696 449 GLU B OE1 
6253 O OE2 . GLU B 434 ? 0.5354 1.3974 0.4290 0.1886  -0.0447 -0.0653 449 GLU B OE2 
6254 N N   . LEU B 435 ? 0.3813 1.4120 0.3692 0.1448  -0.0475 -0.1135 450 LEU B N   
6255 C CA  . LEU B 435 ? 0.3575 1.3928 0.3591 0.1186  -0.0408 -0.1217 450 LEU B CA  
6256 C C   . LEU B 435 ? 0.3495 1.4381 0.3637 0.1083  -0.0435 -0.1361 450 LEU B C   
6257 O O   . LEU B 435 ? 0.3322 1.4252 0.3508 0.0852  -0.0395 -0.1441 450 LEU B O   
6258 C CB  . LEU B 435 ? 0.3509 1.3684 0.3594 0.1154  -0.0355 -0.1181 450 LEU B CB  
6259 C CG  . LEU B 435 ? 0.3551 1.3184 0.3549 0.1174  -0.0315 -0.1056 450 LEU B CG  
6260 C CD1 . LEU B 435 ? 0.3599 1.3144 0.3648 0.1171  -0.0284 -0.1031 450 LEU B CD1 
6261 C CD2 . LEU B 435 ? 0.3509 1.2867 0.3512 0.0974  -0.0266 -0.1058 450 LEU B CD2 
6262 N N   . PHE B 436 ? 0.3648 1.4936 0.3854 0.1252  -0.0500 -0.1400 451 PHE B N   
6263 C CA  . PHE B 436 ? 0.3791 1.5671 0.4135 0.1181  -0.0542 -0.1546 451 PHE B CA  
6264 C C   . PHE B 436 ? 0.3807 1.5785 0.4069 0.1094  -0.0586 -0.1593 451 PHE B C   
6265 O O   . PHE B 436 ? 0.3660 1.5767 0.3977 0.0841  -0.0546 -0.1697 451 PHE B O   
6266 C CB  . PHE B 436 ? 0.3854 1.6128 0.4268 0.1447  -0.0628 -0.1564 451 PHE B CB  
6267 C CG  . PHE B 436 ? 0.3964 1.6904 0.4552 0.1397  -0.0682 -0.1721 451 PHE B CG  
6268 C CD1 . PHE B 436 ? 0.3974 1.7243 0.4759 0.1208  -0.0613 -0.1844 451 PHE B CD1 
6269 C CD2 . PHE B 436 ? 0.4143 1.7397 0.4693 0.1537  -0.0806 -0.1747 451 PHE B CD2 
6270 C CE1 . PHE B 436 ? 0.3888 1.7816 0.4855 0.1150  -0.0659 -0.2001 451 PHE B CE1 
6271 C CE2 . PHE B 436 ? 0.4085 1.7997 0.4817 0.1494  -0.0869 -0.1899 451 PHE B CE2 
6272 C CZ  . PHE B 436 ? 0.3961 1.8223 0.4915 0.1296  -0.0791 -0.2031 451 PHE B CZ  
6273 N N   . LEU B 437 ? 0.3851 1.5722 0.3950 0.1296  -0.0662 -0.1514 452 LEU B N   
6274 C CA  . LEU B 437 ? 0.3950 1.5902 0.3929 0.1241  -0.0712 -0.1552 452 LEU B CA  
6275 C C   . LEU B 437 ? 0.3909 1.5539 0.3845 0.0977  -0.0612 -0.1575 452 LEU B C   
6276 O O   . LEU B 437 ? 0.3715 1.5545 0.3652 0.0798  -0.0614 -0.1682 452 LEU B O   
6277 C CB  . LEU B 437 ? 0.4137 1.5880 0.3889 0.1491  -0.0790 -0.1434 452 LEU B CB  
6278 C CG  . LEU B 437 ? 0.4401 1.6574 0.4123 0.1722  -0.0943 -0.1453 452 LEU B CG  
6279 C CD1 . LEU B 437 ? 0.4239 1.7064 0.4218 0.1702  -0.0997 -0.1596 452 LEU B CD1 
6280 C CD2 . LEU B 437 ? 0.4628 1.6540 0.4210 0.2027  -0.0993 -0.1312 452 LEU B CD2 
6281 N N   . PHE B 438 ? 0.3950 1.5085 0.3853 0.0951  -0.0526 -0.1481 453 PHE B N   
6282 C CA  . PHE B 438 ? 0.4021 1.4842 0.3903 0.0727  -0.0437 -0.1504 453 PHE B CA  
6283 C C   . PHE B 438 ? 0.3979 1.4986 0.4001 0.0474  -0.0389 -0.1625 453 PHE B C   
6284 O O   . PHE B 438 ? 0.4104 1.5159 0.4096 0.0297  -0.0369 -0.1715 453 PHE B O   
6285 C CB  . PHE B 438 ? 0.4069 1.4339 0.3907 0.0758  -0.0366 -0.1382 453 PHE B CB  
6286 C CG  . PHE B 438 ? 0.4143 1.4133 0.3803 0.0871  -0.0366 -0.1301 453 PHE B CG  
6287 C CD1 . PHE B 438 ? 0.4186 1.4204 0.3741 0.0783  -0.0361 -0.1363 453 PHE B CD1 
6288 C CD2 . PHE B 438 ? 0.4284 1.3985 0.3861 0.1052  -0.0367 -0.1171 453 PHE B CD2 
6289 C CE1 . PHE B 438 ? 0.4452 1.4217 0.3823 0.0870  -0.0349 -0.1296 453 PHE B CE1 
6290 C CE2 . PHE B 438 ? 0.4463 1.3903 0.3855 0.1134  -0.0357 -0.1101 453 PHE B CE2 
6291 C CZ  . PHE B 438 ? 0.4591 1.4068 0.3879 0.1042  -0.0345 -0.1163 453 PHE B CZ  
6292 N N   . VAL B 439 ? 0.3923 1.5029 0.4074 0.0445  -0.0367 -0.1634 454 VAL B N   
6293 C CA  . VAL B 439 ? 0.4048 1.5231 0.4290 0.0172  -0.0305 -0.1736 454 VAL B CA  
6294 C C   . VAL B 439 ? 0.4134 1.5862 0.4443 0.0035  -0.0337 -0.1894 454 VAL B C   
6295 O O   . VAL B 439 ? 0.4063 1.5780 0.4362 -0.0221 -0.0289 -0.1990 454 VAL B O   
6296 C CB  . VAL B 439 ? 0.4104 1.5231 0.4437 0.0159  -0.0264 -0.1703 454 VAL B CB  
6297 C CG1 . VAL B 439 ? 0.4106 1.5186 0.4474 -0.0141 -0.0190 -0.1785 454 VAL B CG1 
6298 C CG2 . VAL B 439 ? 0.4115 1.4745 0.4384 0.0302  -0.0247 -0.1550 454 VAL B CG2 
6299 N N   . SER B 440 ? 0.4199 1.6404 0.4578 0.0203  -0.0422 -0.1927 455 SER B N   
6300 C CA  . SER B 440 ? 0.4221 1.7000 0.4687 0.0086  -0.0468 -0.2083 455 SER B CA  
6301 C C   . SER B 440 ? 0.4464 1.7176 0.4802 -0.0066 -0.0474 -0.2143 455 SER B C   
6302 O O   . SER B 440 ? 0.4541 1.7386 0.4905 -0.0335 -0.0430 -0.2266 455 SER B O   
6303 C CB  . SER B 440 ? 0.4141 1.7425 0.4694 0.0343  -0.0585 -0.2097 455 SER B CB  
6304 O OG  . SER B 440 ? 0.4155 1.7195 0.4564 0.0622  -0.0654 -0.1964 455 SER B OG  
6305 N N   . ARG B 441 ? 0.4837 1.7301 0.5016 0.0093  -0.0516 -0.2056 456 ARG B N   
6306 C CA  . ARG B 441 ? 0.5299 1.7707 0.5329 -0.0024 -0.0523 -0.2114 456 ARG B CA  
6307 C C   . ARG B 441 ? 0.5359 1.7399 0.5334 -0.0298 -0.0411 -0.2167 456 ARG B C   
6308 O O   . ARG B 441 ? 0.5674 1.7895 0.5612 -0.0503 -0.0406 -0.2297 456 ARG B O   
6309 C CB  . ARG B 441 ? 0.5630 1.7798 0.5477 0.0202  -0.0574 -0.2000 456 ARG B CB  
6310 C CG  . ARG B 441 ? 0.6090 1.8706 0.5923 0.0418  -0.0718 -0.2000 456 ARG B CG  
6311 C CD  . ARG B 441 ? 0.6712 1.9604 0.6425 0.0325  -0.0789 -0.2102 456 ARG B CD  
6312 N NE  . ARG B 441 ? 0.7246 1.9855 0.6707 0.0489  -0.0830 -0.2000 456 ARG B NE  
6313 C CZ  . ARG B 441 ? 0.7865 2.0506 0.7242 0.0778  -0.0933 -0.1890 456 ARG B CZ  
6314 N NH1 . ARG B 441 ? 0.7831 2.0798 0.7376 0.0954  -0.1009 -0.1876 456 ARG B NH1 
6315 N NH2 . ARG B 441 ? 0.8493 2.0823 0.7602 0.0890  -0.0955 -0.1797 456 ARG B NH2 
6316 N N   . PRO B 442 ? 0.5299 1.6818 0.5261 -0.0300 -0.0326 -0.2071 457 PRO B N   
6317 C CA  . PRO B 442 ? 0.5456 1.6628 0.5380 -0.0542 -0.0230 -0.2124 457 PRO B CA  
6318 C C   . PRO B 442 ? 0.5360 1.6741 0.5372 -0.0788 -0.0195 -0.2236 457 PRO B C   
6319 O O   . PRO B 442 ? 0.5563 1.6839 0.5510 -0.1023 -0.0144 -0.2336 457 PRO B O   
6320 C CB  . PRO B 442 ? 0.5688 1.6325 0.5618 -0.0447 -0.0173 -0.1985 457 PRO B CB  
6321 C CG  . PRO B 442 ? 0.5508 1.6132 0.5396 -0.0167 -0.0229 -0.1868 457 PRO B CG  
6322 C CD  . PRO B 442 ? 0.5478 1.6665 0.5433 -0.0078 -0.0321 -0.1912 457 PRO B CD  
6323 N N   . LEU B 443 ? 0.5304 1.6968 0.5450 -0.0745 -0.0216 -0.2228 458 LEU B N   
6324 C CA  . LEU B 443 ? 0.5119 1.7044 0.5344 -0.0995 -0.0176 -0.2347 458 LEU B CA  
6325 C C   . LEU B 443 ? 0.5291 1.7772 0.5538 -0.1101 -0.0230 -0.2501 458 LEU B C   
6326 O O   . LEU B 443 ? 0.5682 1.8215 0.5893 -0.1383 -0.0183 -0.2625 458 LEU B O   
6327 C CB  . LEU B 443 ? 0.4933 1.6999 0.5288 -0.0923 -0.0168 -0.2303 458 LEU B CB  
6328 C CG  . LEU B 443 ? 0.5032 1.6508 0.5340 -0.0895 -0.0109 -0.2168 458 LEU B CG  
6329 C CD1 . LEU B 443 ? 0.4939 1.6530 0.5345 -0.0848 -0.0091 -0.2131 458 LEU B CD1 
6330 C CD2 . LEU B 443 ? 0.5169 1.6193 0.5370 -0.1154 -0.0031 -0.2193 458 LEU B CD2 
6331 N N   . GLN B 444 ? 0.5330 1.8203 0.5620 -0.0877 -0.0336 -0.2491 459 GLN B N   
6332 C CA  . GLN B 444 ? 0.5692 1.9084 0.5987 -0.0945 -0.0414 -0.2626 459 GLN B CA  
6333 C C   . GLN B 444 ? 0.6004 1.9137 0.6119 -0.1162 -0.0372 -0.2700 459 GLN B C   
6334 O O   . GLN B 444 ? 0.6132 1.9447 0.6248 -0.1443 -0.0337 -0.2844 459 GLN B O   
6335 C CB  . GLN B 444 ? 0.5507 1.9184 0.5801 -0.0627 -0.0549 -0.2564 459 GLN B CB  
6336 C CG  . GLN B 444 ? 0.5500 1.9847 0.5863 -0.0656 -0.0660 -0.2701 459 GLN B CG  
6337 C CD  . GLN B 444 ? 0.5679 2.0190 0.5962 -0.0349 -0.0806 -0.2628 459 GLN B CD  
6338 O OE1 . GLN B 444 ? 0.5679 1.9780 0.5746 -0.0257 -0.0812 -0.2535 459 GLN B OE1 
6339 N NE2 . GLN B 444 ? 0.5558 2.0672 0.6007 -0.0193 -0.0924 -0.2674 459 GLN B NE2 
6340 N N   . ARG B 445 ? 0.6185 1.8872 0.6142 -0.1039 -0.0364 -0.2605 460 ARG B N   
6341 C CA  . ARG B 445 ? 0.6494 1.8922 0.6269 -0.1202 -0.0321 -0.2674 460 ARG B CA  
6342 C C   . ARG B 445 ? 0.6261 1.8219 0.5991 -0.1454 -0.0192 -0.2712 460 ARG B C   
6343 O O   . ARG B 445 ? 0.6350 1.8259 0.5971 -0.1687 -0.0151 -0.2837 460 ARG B O   
6344 C CB  . ARG B 445 ? 0.6881 1.8970 0.6503 -0.0988 -0.0335 -0.2562 460 ARG B CB  
6345 C CG  . ARG B 445 ? 0.7214 1.9631 0.6812 -0.0715 -0.0466 -0.2495 460 ARG B CG  
6346 C CD  . ARG B 445 ? 0.7756 2.0329 0.7159 -0.0731 -0.0533 -0.2562 460 ARG B CD  
6347 N NE  . ARG B 445 ? 0.8171 2.0241 0.7379 -0.0813 -0.0436 -0.2561 460 ARG B NE  
6348 C CZ  . ARG B 445 ? 0.8493 2.0498 0.7480 -0.0752 -0.0468 -0.2557 460 ARG B CZ  
6349 N NH1 . ARG B 445 ? 0.8965 2.1344 0.7869 -0.0598 -0.0610 -0.2538 460 ARG B NH1 
6350 N NH2 . ARG B 445 ? 0.8312 1.9862 0.7148 -0.0840 -0.0356 -0.2571 460 ARG B NH2 
6351 N N   . PHE B 446 ? 0.5775 1.7368 0.5569 -0.1404 -0.0134 -0.2605 461 PHE B N   
6352 C CA  . PHE B 446 ? 0.5598 1.6633 0.5324 -0.1574 -0.0028 -0.2604 461 PHE B CA  
6353 C C   . PHE B 446 ? 0.5244 1.6161 0.5043 -0.1715 0.0022  -0.2591 461 PHE B C   
6354 O O   . PHE B 446 ? 0.4756 1.5937 0.4679 -0.1635 -0.0008 -0.2547 461 PHE B O   
6355 C CB  . PHE B 446 ? 0.5579 1.6097 0.5261 -0.1382 0.0002  -0.2470 461 PHE B CB  
6356 C CG  . PHE B 446 ? 0.5854 1.6356 0.5420 -0.1276 -0.0016 -0.2479 461 PHE B CG  
6357 C CD1 . PHE B 446 ? 0.6427 1.6800 0.5855 -0.1454 0.0035  -0.2600 461 PHE B CD1 
6358 C CD2 . PHE B 446 ? 0.5849 1.6419 0.5415 -0.1006 -0.0074 -0.2366 461 PHE B CD2 
6359 C CE1 . PHE B 446 ? 0.6588 1.6927 0.5883 -0.1369 0.0029  -0.2613 461 PHE B CE1 
6360 C CE2 . PHE B 446 ? 0.6265 1.6787 0.5686 -0.0924 -0.0083 -0.2371 461 PHE B CE2 
6361 C CZ  . PHE B 446 ? 0.6517 1.6934 0.5803 -0.1108 -0.0029 -0.2496 461 PHE B CZ  
6362 N N   . SER B 447 ? 0.5274 1.5731 0.4973 -0.1913 0.0103  -0.2622 462 SER B N   
6363 C CA  . SER B 447 ? 0.5080 1.5266 0.4775 -0.2071 0.0157  -0.2601 462 SER B CA  
6364 C C   . SER B 447 ? 0.5083 1.4591 0.4712 -0.2010 0.0200  -0.2503 462 SER B C   
6365 O O   . SER B 447 ? 0.4793 1.4045 0.4340 -0.2004 0.0227  -0.2538 462 SER B O   
6366 C CB  . SER B 447 ? 0.5319 1.5608 0.4921 -0.2413 0.0206  -0.2759 462 SER B CB  
6367 O OG  . SER B 447 ? 0.5464 1.5556 0.5041 -0.2578 0.0254  -0.2739 462 SER B OG  
6368 N N   . PHE B 448 ? 0.4907 1.4142 0.4575 -0.1963 0.0206  -0.2390 463 PHE B N   
6369 C CA  . PHE B 448 ? 0.4886 1.3548 0.4542 -0.1848 0.0220  -0.2277 463 PHE B CA  
6370 C C   . PHE B 448 ? 0.5171 1.3391 0.4731 -0.2040 0.0257  -0.2264 463 PHE B C   
6371 O O   . PHE B 448 ? 0.5298 1.3582 0.4861 -0.2110 0.0251  -0.2225 463 PHE B O   
6372 C CB  . PHE B 448 ? 0.4589 1.3286 0.4368 -0.1578 0.0172  -0.2128 463 PHE B CB  
6373 C CG  . PHE B 448 ? 0.4283 1.3336 0.4123 -0.1366 0.0129  -0.2116 463 PHE B CG  
6374 C CD1 . PHE B 448 ? 0.4015 1.3610 0.3915 -0.1319 0.0082  -0.2146 463 PHE B CD1 
6375 C CD2 . PHE B 448 ? 0.4215 1.3050 0.4048 -0.1207 0.0135  -0.2072 463 PHE B CD2 
6376 C CE1 . PHE B 448 ? 0.3854 1.3734 0.3781 -0.1109 0.0028  -0.2122 463 PHE B CE1 
6377 C CE2 . PHE B 448 ? 0.4078 1.3194 0.3920 -0.1021 0.0095  -0.2050 463 PHE B CE2 
6378 C CZ  . PHE B 448 ? 0.3881 1.3503 0.3759 -0.0968 0.0034  -0.2070 463 PHE B CZ  
6379 N N   . SER B 449 ? 0.5362 1.3119 0.4821 -0.2124 0.0296  -0.2297 464 SER B N   
6380 C CA  . SER B 449 ? 0.5778 1.3048 0.5115 -0.2289 0.0317  -0.2273 464 SER B CA  
6381 C C   . SER B 449 ? 0.6184 1.2897 0.5547 -0.2132 0.0305  -0.2177 464 SER B C   
6382 O O   . SER B 449 ? 0.5903 1.2599 0.5366 -0.1939 0.0305  -0.2162 464 SER B O   
6383 C CB  . SER B 449 ? 0.6030 1.3220 0.5186 -0.2590 0.0374  -0.2422 464 SER B CB  
6384 O OG  . SER B 449 ? 0.6039 1.3183 0.5170 -0.2572 0.0404  -0.2516 464 SER B OG  
6385 N N   . CYS B 450 ? 0.6698 1.2959 0.5964 -0.2218 0.0294  -0.2113 465 CYS B N   
6386 C CA  . CYS B 450 ? 0.6968 1.2710 0.6276 -0.2066 0.0264  -0.2017 465 CYS B CA  
6387 C C   . CYS B 450 ? 0.7344 1.2657 0.6542 -0.2156 0.0308  -0.2110 465 CYS B C   
6388 O O   . CYS B 450 ? 0.7695 1.2699 0.6695 -0.2375 0.0326  -0.2151 465 CYS B O   
6389 C CB  . CYS B 450 ? 0.7176 1.2621 0.6424 -0.2091 0.0210  -0.1891 465 CYS B CB  
6390 S SG  . CYS B 450 ? 0.7210 1.2105 0.6560 -0.1863 0.0145  -0.1764 465 CYS B SG  
6391 N N   . PRO B 451 ? 0.7391 1.2658 0.6705 -0.1988 0.0332  -0.2143 466 PRO B N   
6392 C CA  . PRO B 451 ? 0.7875 1.2790 0.7107 -0.2046 0.0389  -0.2252 466 PRO B CA  
6393 C C   . PRO B 451 ? 0.8406 1.2756 0.7455 -0.2199 0.0380  -0.2250 466 PRO B C   
6394 O O   . PRO B 451 ? 0.8409 1.2469 0.7470 -0.2134 0.0312  -0.2124 466 PRO B O   
6395 C CB  . PRO B 451 ? 0.7643 1.2425 0.7081 -0.1772 0.0385  -0.2203 466 PRO B CB  
6396 C CG  . PRO B 451 ? 0.7161 1.2425 0.6751 -0.1618 0.0360  -0.2132 466 PRO B CG  
6397 C CD  . PRO B 451 ? 0.7147 1.2631 0.6677 -0.1719 0.0309  -0.2064 466 PRO B CD  
6398 N N   . SER B 452 ? 0.9188 1.3360 0.8047 -0.2401 0.0445  -0.2390 467 SER B N   
6399 C CA  . SER B 452 ? 0.9847 1.3405 0.8490 -0.2547 0.0446  -0.2404 467 SER B CA  
6400 C C   . SER B 452 ? 0.9748 1.2839 0.8468 -0.2358 0.0361  -0.2254 467 SER B C   
6401 O O   . SER B 452 ? 1.0113 1.2854 0.8659 -0.2471 0.0310  -0.2177 467 SER B O   
6402 C CB  . SER B 452 ? 1.0369 1.3678 0.8906 -0.2620 0.0530  -0.2567 467 SER B CB  
6403 O OG  . SER B 452 ? 1.1164 1.3816 0.9482 -0.2734 0.0529  -0.2579 467 SER B OG  
6404 N N   . GLU B 453 ? 0.9437 1.2534 0.8411 -0.2078 0.0343  -0.2213 468 GLU B N   
6405 C CA  . GLU B 453 ? 0.9583 1.2250 0.8659 -0.1889 0.0256  -0.2090 468 GLU B CA  
6406 C C   . GLU B 453 ? 0.8624 1.1556 0.8009 -0.1613 0.0205  -0.1980 468 GLU B C   
6407 O O   . GLU B 453 ? 0.8322 1.1019 0.7889 -0.1407 0.0174  -0.1948 468 GLU B O   
6408 C CB  . GLU B 453 ? 1.0615 1.2745 0.9640 -0.1853 0.0285  -0.2176 468 GLU B CB  
6409 C CG  . GLU B 453 ? 1.1534 1.3244 1.0203 -0.2130 0.0307  -0.2242 468 GLU B CG  
6410 C CD  . GLU B 453 ? 1.2473 1.3610 1.1061 -0.2095 0.0339  -0.2336 468 GLU B CD  
6411 O OE1 . GLU B 453 ? 1.3032 1.3592 1.1401 -0.2169 0.0279  -0.2286 468 GLU B OE1 
6412 O OE2 . GLU B 453 ? 1.2440 1.3688 1.1159 -0.2000 0.0425  -0.2462 468 GLU B OE2 
6413 N N   . ALA B 454 ? 0.7895 1.1315 0.7337 -0.1615 0.0196  -0.1926 469 ALA B N   
6414 C CA  . ALA B 454 ? 0.7379 1.0965 0.7031 -0.1410 0.0124  -0.1787 469 ALA B CA  
6415 C C   . ALA B 454 ? 0.7246 1.0819 0.6767 -0.1513 0.0048  -0.1668 469 ALA B C   
6416 O O   . ALA B 454 ? 0.7255 1.0834 0.6548 -0.1749 0.0070  -0.1707 469 ALA B O   
6417 C CB  . ALA B 454 ? 0.6969 1.1090 0.6783 -0.1300 0.0174  -0.1812 469 ALA B CB  
6418 N N   . SER B 455 ? 0.6793 1.0340 0.6453 -0.1349 -0.0038 -0.1530 470 SER B N   
6419 C CA  . SER B 455 ? 0.6543 1.0051 0.6076 -0.1431 -0.0109 -0.1415 470 SER B CA  
6420 C C   . SER B 455 ? 0.6288 1.0335 0.5822 -0.1486 -0.0067 -0.1424 470 SER B C   
6421 O O   . SER B 455 ? 0.6005 1.0441 0.5701 -0.1367 -0.0025 -0.1461 470 SER B O   
6422 C CB  . SER B 455 ? 0.6352 0.9658 0.6029 -0.1238 -0.0219 -0.1271 470 SER B CB  
6423 O OG  . SER B 455 ? 0.6659 0.9418 0.6279 -0.1220 -0.0287 -0.1244 470 SER B OG  
6424 N N   . LEU B 456 ? 0.6564 1.0631 0.5907 -0.1667 -0.0078 -0.1394 471 LEU B N   
6425 C CA  . LEU B 456 ? 0.6336 1.0899 0.5712 -0.1677 -0.0056 -0.1383 471 LEU B CA  
6426 C C   . LEU B 456 ? 0.5995 1.0646 0.5578 -0.1424 -0.0113 -0.1273 471 LEU B C   
6427 O O   . LEU B 456 ? 0.6142 1.0429 0.5763 -0.1325 -0.0191 -0.1176 471 LEU B O   
6428 C CB  . LEU B 456 ? 0.6543 1.1047 0.5696 -0.1890 -0.0064 -0.1349 471 LEU B CB  
6429 C CG  . LEU B 456 ? 0.6905 1.1420 0.5851 -0.2174 0.0013  -0.1476 471 LEU B CG  
6430 C CD1 . LEU B 456 ? 0.7140 1.1484 0.5835 -0.2401 0.0009  -0.1433 471 LEU B CD1 
6431 C CD2 . LEU B 456 ? 0.6681 1.1803 0.5727 -0.2207 0.0092  -0.1603 471 LEU B CD2 
6432 N N   . PRO B 457 ? 0.5702 1.0823 0.5417 -0.1314 -0.0080 -0.1289 472 PRO B N   
6433 C CA  . PRO B 457 ? 0.5459 1.0631 0.5349 -0.1086 -0.0127 -0.1188 472 PRO B CA  
6434 C C   . PRO B 457 ? 0.5798 1.0785 0.5626 -0.1083 -0.0205 -0.1060 472 PRO B C   
6435 O O   . PRO B 457 ? 0.6183 1.1211 0.5842 -0.1244 -0.0200 -0.1056 472 PRO B O   
6436 C CB  . PRO B 457 ? 0.5220 1.0911 0.5184 -0.1009 -0.0079 -0.1229 472 PRO B CB  
6437 C CG  . PRO B 457 ? 0.5260 1.1217 0.5094 -0.1207 -0.0025 -0.1336 472 PRO B CG  
6438 C CD  . PRO B 457 ? 0.5582 1.1189 0.5285 -0.1388 -0.0009 -0.1398 472 PRO B CD  
6439 N N   . ASP B 458 ? 0.5501 1.0296 0.5463 -0.0913 -0.0272 -0.0965 473 ASP B N   
6440 C CA  . ASP B 458 ? 0.5340 0.9954 0.5247 -0.0897 -0.0356 -0.0842 473 ASP B CA  
6441 C C   . ASP B 458 ? 0.4894 0.9866 0.4823 -0.0830 -0.0337 -0.0808 473 ASP B C   
6442 O O   . ASP B 458 ? 0.4397 0.9604 0.4481 -0.0668 -0.0314 -0.0808 473 ASP B O   
6443 C CB  . ASP B 458 ? 0.5568 0.9876 0.5628 -0.0740 -0.0444 -0.0759 473 ASP B CB  
6444 C CG  . ASP B 458 ? 0.5669 0.9617 0.5600 -0.0789 -0.0556 -0.0646 473 ASP B CG  
6445 O OD1 . ASP B 458 ? 0.5452 0.9466 0.5221 -0.0882 -0.0563 -0.0601 473 ASP B OD1 
6446 O OD2 . ASP B 458 ? 0.6070 0.9667 0.6061 -0.0731 -0.0638 -0.0608 473 ASP B OD2 
6447 N N   . LEU B 459 ? 0.4914 0.9888 0.4670 -0.0957 -0.0346 -0.0778 474 LEU B N   
6448 C CA  . LEU B 459 ? 0.4656 0.9949 0.4409 -0.0908 -0.0321 -0.0758 474 LEU B CA  
6449 C C   . LEU B 459 ? 0.4715 0.9818 0.4475 -0.0806 -0.0401 -0.0633 474 LEU B C   
6450 O O   . LEU B 459 ? 0.4455 0.9752 0.4174 -0.0777 -0.0384 -0.0611 474 LEU B O   
6451 C CB  . LEU B 459 ? 0.4641 1.0100 0.4213 -0.1113 -0.0265 -0.0820 474 LEU B CB  
6452 C CG  . LEU B 459 ? 0.4611 1.0287 0.4179 -0.1231 -0.0189 -0.0954 474 LEU B CG  
6453 C CD1 . LEU B 459 ? 0.4749 1.0618 0.4154 -0.1454 -0.0127 -0.1025 474 LEU B CD1 
6454 C CD2 . LEU B 459 ? 0.4292 1.0376 0.4037 -0.1070 -0.0148 -0.1014 474 LEU B CD2 
6455 N N   . GLN B 460 ? 0.5131 0.9867 0.4947 -0.0749 -0.0489 -0.0560 475 GLN B N   
6456 C CA  . GLN B 460 ? 0.5411 0.9972 0.5246 -0.0656 -0.0578 -0.0443 475 GLN B CA  
6457 C C   . GLN B 460 ? 0.5299 1.0132 0.5309 -0.0473 -0.0544 -0.0440 475 GLN B C   
6458 O O   . GLN B 460 ? 0.5202 1.0149 0.5163 -0.0433 -0.0542 -0.0399 475 GLN B O   
6459 C CB  . GLN B 460 ? 0.5555 0.9698 0.5439 -0.0625 -0.0695 -0.0371 475 GLN B CB  
6460 C CG  . GLN B 460 ? 0.6119 0.9998 0.5849 -0.0671 -0.0800 -0.0258 475 GLN B CG  
6461 C CD  . GLN B 460 ? 0.6541 1.0085 0.6379 -0.0578 -0.0942 -0.0170 475 GLN B CD  
6462 O OE1 . GLN B 460 ? 0.6868 1.0045 0.6554 -0.0662 -0.1044 -0.0112 475 GLN B OE1 
6463 N NE2 . GLN B 460 ? 0.6485 1.0154 0.6575 -0.0408 -0.0955 -0.0158 475 GLN B NE2 
6464 N N   . GLY B 461 ? 0.5475 1.0401 0.5664 -0.0372 -0.0509 -0.0489 476 GLY B N   
6465 C CA  . GLY B 461 ? 0.5469 1.0634 0.5789 -0.0215 -0.0465 -0.0491 476 GLY B CA  
6466 C C   . GLY B 461 ? 0.5831 1.0813 0.6284 -0.0102 -0.0534 -0.0408 476 GLY B C   
6467 O O   . GLY B 461 ? 0.6112 1.0828 0.6533 -0.0137 -0.0628 -0.0335 476 GLY B O   
6468 N N   . ARG B 462 ? 0.6093 1.1220 0.6687 0.0026  -0.0487 -0.0421 477 ARG B N   
6469 C CA  . ARG B 462 ? 0.6470 1.1468 0.7229 0.0125  -0.0533 -0.0365 477 ARG B CA  
6470 C C   . ARG B 462 ? 0.6091 1.1271 0.6842 0.0224  -0.0482 -0.0343 477 ARG B C   
6471 O O   . ARG B 462 ? 0.5826 1.1234 0.6487 0.0244  -0.0409 -0.0385 477 ARG B O   
6472 C CB  . ARG B 462 ? 0.7134 1.2080 0.8091 0.0164  -0.0511 -0.0425 477 ARG B CB  
6473 C CG  . ARG B 462 ? 0.8028 1.2985 0.9195 0.0279  -0.0502 -0.0410 477 ARG B CG  
6474 C CD  . ARG B 462 ? 0.8773 1.3645 1.0152 0.0310  -0.0490 -0.0476 477 ARG B CD  
6475 N NE  . ARG B 462 ? 0.9109 1.4074 1.0439 0.0269  -0.0401 -0.0578 477 ARG B NE  
6476 C CZ  . ARG B 462 ? 0.9817 1.4878 1.1270 0.0315  -0.0308 -0.0664 477 ARG B CZ  
6477 N NH1 . ARG B 462 ? 0.9835 1.4926 1.1489 0.0403  -0.0279 -0.0667 477 ARG B NH1 
6478 N NH2 . ARG B 462 ? 1.0343 1.5474 1.1711 0.0258  -0.0238 -0.0757 477 ARG B NH2 
6479 N N   . PHE B 463 ? 0.6155 1.1225 0.6986 0.0283  -0.0528 -0.0275 478 PHE B N   
6480 C CA  . PHE B 463 ? 0.6061 1.1244 0.6857 0.0369  -0.0480 -0.0248 478 PHE B CA  
6481 C C   . PHE B 463 ? 0.6087 1.1305 0.7062 0.0442  -0.0428 -0.0273 478 PHE B C   
6482 O O   . PHE B 463 ? 0.6726 1.1821 0.7880 0.0449  -0.0475 -0.0256 478 PHE B O   
6483 C CB  . PHE B 463 ? 0.6026 1.1068 0.6741 0.0365  -0.0551 -0.0161 478 PHE B CB  
6484 C CG  . PHE B 463 ? 0.5921 1.1063 0.6507 0.0437  -0.0494 -0.0139 478 PHE B CG  
6485 C CD1 . PHE B 463 ? 0.5651 1.0916 0.6051 0.0437  -0.0463 -0.0153 478 PHE B CD1 
6486 C CD2 . PHE B 463 ? 0.5869 1.0980 0.6517 0.0507  -0.0469 -0.0111 478 PHE B CD2 
6487 C CE1 . PHE B 463 ? 0.5733 1.1069 0.6011 0.0528  -0.0416 -0.0136 478 PHE B CE1 
6488 C CE2 . PHE B 463 ? 0.5809 1.0961 0.6303 0.0578  -0.0418 -0.0088 478 PHE B CE2 
6489 C CZ  . PHE B 463 ? 0.5753 1.1009 0.6062 0.0600  -0.0396 -0.0099 478 PHE B CZ  
6490 N N   . GLY B 464 ? 0.5998 1.1395 0.6922 0.0494  -0.0333 -0.0318 479 GLY B N   
6491 C CA  . GLY B 464 ? 0.5566 1.0996 0.6586 0.0558  -0.0265 -0.0330 479 GLY B CA  
6492 C C   . GLY B 464 ? 0.5150 1.0571 0.6024 0.0613  -0.0253 -0.0264 479 GLY B C   
6493 O O   . GLY B 464 ? 0.5418 1.0703 0.6293 0.0603  -0.0313 -0.0199 479 GLY B O   
6494 N N   . VAL B 465 ? 0.4645 1.0196 0.5377 0.0673  -0.0181 -0.0281 480 VAL B N   
6495 C CA  . VAL B 465 ? 0.4394 0.9923 0.4934 0.0740  -0.0172 -0.0222 480 VAL B CA  
6496 C C   . VAL B 465 ? 0.4201 0.9855 0.4580 0.0758  -0.0195 -0.0230 480 VAL B C   
6497 O O   . VAL B 465 ? 0.4276 0.9927 0.4491 0.0828  -0.0193 -0.0192 480 VAL B O   
6498 C CB  . VAL B 465 ? 0.4461 1.0025 0.4919 0.0808  -0.0086 -0.0227 480 VAL B CB  
6499 C CG1 . VAL B 465 ? 0.4259 0.9754 0.4908 0.0768  -0.0041 -0.0249 480 VAL B CG1 
6500 C CG2 . VAL B 465 ? 0.4466 1.0232 0.4820 0.0846  -0.0046 -0.0286 480 VAL B CG2 
6501 N N   . VAL B 466 ? 0.3783 0.9551 0.4211 0.0692  -0.0211 -0.0288 481 VAL B N   
6502 C CA  . VAL B 466 ? 0.3485 0.9386 0.3804 0.0671  -0.0232 -0.0308 481 VAL B CA  
6503 C C   . VAL B 466 ? 0.3314 0.9174 0.3715 0.0543  -0.0273 -0.0341 481 VAL B C   
6504 O O   . VAL B 466 ? 0.3190 0.8947 0.3730 0.0495  -0.0281 -0.0359 481 VAL B O   
6505 C CB  . VAL B 466 ? 0.3693 0.9862 0.3929 0.0726  -0.0187 -0.0370 481 VAL B CB  
6506 C CG1 . VAL B 466 ? 0.3957 1.0155 0.4051 0.0867  -0.0165 -0.0329 481 VAL B CG1 
6507 C CG2 . VAL B 466 ? 0.3600 0.9840 0.3931 0.0691  -0.0147 -0.0437 481 VAL B CG2 
6508 N N   . LEU B 467 ? 0.3119 0.9053 0.3422 0.0488  -0.0293 -0.0352 482 LEU B N   
6509 C CA  . LEU B 467 ? 0.3169 0.9028 0.3492 0.0350  -0.0329 -0.0376 482 LEU B CA  
6510 C C   . LEU B 467 ? 0.3188 0.9247 0.3534 0.0303  -0.0283 -0.0470 482 LEU B C   
6511 O O   . LEU B 467 ? 0.3095 0.9414 0.3364 0.0315  -0.0248 -0.0520 482 LEU B O   
6512 C CB  . LEU B 467 ? 0.3198 0.9053 0.3381 0.0287  -0.0354 -0.0355 482 LEU B CB  
6513 C CG  . LEU B 467 ? 0.3163 0.8931 0.3303 0.0121  -0.0384 -0.0378 482 LEU B CG  
6514 C CD1 . LEU B 467 ? 0.3136 0.8568 0.3333 0.0069  -0.0466 -0.0314 482 LEU B CD1 
6515 C CD2 . LEU B 467 ? 0.3246 0.9103 0.3229 0.0058  -0.0371 -0.0385 482 LEU B CD2 
6516 N N   . GLN B 468 ? 0.3502 0.9450 0.3957 0.0254  -0.0284 -0.0502 483 GLN B N   
6517 C CA  . GLN B 468 ? 0.3699 0.9816 0.4173 0.0216  -0.0231 -0.0600 483 GLN B CA  
6518 C C   . GLN B 468 ? 0.3847 0.9798 0.4351 0.0080  -0.0251 -0.0641 483 GLN B C   
6519 O O   . GLN B 468 ? 0.3890 0.9564 0.4453 0.0057  -0.0309 -0.0590 483 GLN B O   
6520 C CB  . GLN B 468 ? 0.3819 0.9978 0.4375 0.0319  -0.0180 -0.0617 483 GLN B CB  
6521 C CG  . GLN B 468 ? 0.4095 1.0033 0.4812 0.0313  -0.0181 -0.0621 483 GLN B CG  
6522 C CD  . GLN B 468 ? 0.4369 1.0295 0.5165 0.0420  -0.0138 -0.0600 483 GLN B CD  
6523 O OE1 . GLN B 468 ? 0.4950 1.1011 0.5648 0.0498  -0.0102 -0.0582 483 GLN B OE1 
6524 N NE2 . GLN B 468 ? 0.4467 1.0225 0.5437 0.0424  -0.0140 -0.0603 483 GLN B NE2 
6525 N N   . PRO B 469 ? 0.4091 1.0198 0.4545 -0.0011 -0.0210 -0.0735 484 PRO B N   
6526 C CA  . PRO B 469 ? 0.4425 1.0320 0.4880 -0.0144 -0.0225 -0.0775 484 PRO B CA  
6527 C C   . PRO B 469 ? 0.4636 1.0332 0.5242 -0.0083 -0.0221 -0.0785 484 PRO B C   
6528 O O   . PRO B 469 ? 0.4693 1.0511 0.5378 0.0021  -0.0173 -0.0804 484 PRO B O   
6529 C CB  . PRO B 469 ? 0.4208 1.0350 0.4581 -0.0248 -0.0168 -0.0888 484 PRO B CB  
6530 C CG  . PRO B 469 ? 0.3992 1.0475 0.4367 -0.0136 -0.0128 -0.0911 484 PRO B CG  
6531 C CD  . PRO B 469 ? 0.3994 1.0449 0.4397 0.0011  -0.0155 -0.0810 484 PRO B CD  
6532 N N   . GLU B 470 ? 0.5023 1.0411 0.5660 -0.0146 -0.0270 -0.0776 485 GLU B N   
6533 C CA  . GLU B 470 ? 0.5469 1.0689 0.6259 -0.0101 -0.0255 -0.0821 485 GLU B CA  
6534 C C   . GLU B 470 ? 0.5601 1.1009 0.6358 -0.0141 -0.0159 -0.0944 485 GLU B C   
6535 O O   . GLU B 470 ? 0.5505 1.1086 0.6114 -0.0247 -0.0133 -0.0992 485 GLU B O   
6536 C CB  . GLU B 470 ? 0.6023 1.0878 0.6806 -0.0174 -0.0327 -0.0808 485 GLU B CB  
6537 C CG  . GLU B 470 ? 0.6348 1.0975 0.7097 -0.0178 -0.0442 -0.0689 485 GLU B CG  
6538 C CD  . GLU B 470 ? 0.6747 1.1299 0.7702 -0.0032 -0.0499 -0.0619 485 GLU B CD  
6539 O OE1 . GLU B 470 ? 0.7118 1.1509 0.8040 -0.0033 -0.0600 -0.0521 485 GLU B OE1 
6540 O OE2 . GLU B 470 ? 0.6927 1.1584 0.8070 0.0072  -0.0441 -0.0666 485 GLU B OE2 
6541 N N   . ARG B 471 ? 0.5576 1.0968 0.6466 -0.0068 -0.0103 -0.1001 486 ARG B N   
6542 C CA  . ARG B 471 ? 0.5593 1.1140 0.6429 -0.0117 -0.0012 -0.1123 486 ARG B CA  
6543 C C   . ARG B 471 ? 0.5547 1.0956 0.6258 -0.0281 -0.0016 -0.1195 486 ARG B C   
6544 O O   . ARG B 471 ? 0.5766 1.0866 0.6481 -0.0323 -0.0078 -0.1161 486 ARG B O   
6545 C CB  . ARG B 471 ? 0.5806 1.1306 0.6799 -0.0026 0.0058  -0.1183 486 ARG B CB  
6546 C CG  . ARG B 471 ? 0.5868 1.1562 0.6916 0.0095  0.0099  -0.1143 486 ARG B CG  
6547 C CD  . ARG B 471 ? 0.6283 1.1935 0.7482 0.0163  0.0186  -0.1212 486 ARG B CD  
6548 N NE  . ARG B 471 ? 0.6992 1.2400 0.8416 0.0217  0.0154  -0.1200 486 ARG B NE  
6549 C CZ  . ARG B 471 ? 0.7244 1.2579 0.8807 0.0294  0.0086  -0.1101 486 ARG B CZ  
6550 N NH1 . ARG B 471 ? 0.7043 1.2497 0.8528 0.0322  0.0051  -0.1002 486 ARG B NH1 
6551 N NH2 . ARG B 471 ? 0.7413 1.2551 0.9194 0.0346  0.0047  -0.1105 486 ARG B NH2 
6552 N N   . TYR B 472 ? 0.5179 1.0808 0.5764 -0.0378 0.0042  -0.1291 487 TYR B N   
6553 C CA  . TYR B 472 ? 0.5222 1.0740 0.5668 -0.0560 0.0052  -0.1372 487 TYR B CA  
6554 C C   . TYR B 472 ? 0.5220 1.0956 0.5587 -0.0635 0.0134  -0.1508 487 TYR B C   
6555 O O   . TYR B 472 ? 0.5143 1.1184 0.5523 -0.0558 0.0166  -0.1520 487 TYR B O   
6556 C CB  . TYR B 472 ? 0.5144 1.0749 0.5454 -0.0677 0.0004  -0.1325 487 TYR B CB  
6557 C CG  . TYR B 472 ? 0.4792 1.0849 0.5060 -0.0660 0.0024  -0.1336 487 TYR B CG  
6558 C CD1 . TYR B 472 ? 0.4659 1.0992 0.4833 -0.0774 0.0071  -0.1449 487 TYR B CD1 
6559 C CD2 . TYR B 472 ? 0.4418 1.0621 0.4741 -0.0524 -0.0010 -0.1238 487 TYR B CD2 
6560 C CE1 . TYR B 472 ? 0.4527 1.1286 0.4680 -0.0738 0.0074  -0.1460 487 TYR B CE1 
6561 C CE2 . TYR B 472 ? 0.4275 1.0871 0.4560 -0.0485 0.0000  -0.1248 487 TYR B CE2 
6562 C CZ  . TYR B 472 ? 0.4316 1.1199 0.4524 -0.0585 0.0037  -0.1359 487 TYR B CZ  
6563 O OH  . TYR B 472 ? 0.4079 1.1372 0.4264 -0.0528 0.0033  -0.1373 487 TYR B OH  
6564 N N   . THR B 473 ? 0.5452 1.1017 0.5714 -0.0792 0.0163  -0.1605 488 THR B N   
6565 C CA  . THR B 473 ? 0.5638 1.1366 0.5810 -0.0886 0.0240  -0.1748 488 THR B CA  
6566 C C   . THR B 473 ? 0.5900 1.1895 0.5904 -0.1078 0.0242  -0.1812 488 THR B C   
6567 O O   . THR B 473 ? 0.6532 1.2375 0.6434 -0.1229 0.0216  -0.1807 488 THR B O   
6568 C CB  . THR B 473 ? 0.5886 1.1242 0.6041 -0.0945 0.0290  -0.1846 488 THR B CB  
6569 O OG1 . THR B 473 ? 0.5836 1.0816 0.5922 -0.1041 0.0239  -0.1811 488 THR B OG1 
6570 C CG2 . THR B 473 ? 0.5844 1.1062 0.6184 -0.0760 0.0325  -0.1843 488 THR B CG2 
6571 N N   . VAL B 474 ? 0.5662 1.2058 0.5631 -0.1079 0.0270  -0.1877 489 VAL B N   
6572 C CA  . VAL B 474 ? 0.5639 1.2351 0.5482 -0.1259 0.0270  -0.1958 489 VAL B CA  
6573 C C   . VAL B 474 ? 0.5728 1.2509 0.5463 -0.1391 0.0332  -0.2115 489 VAL B C   
6574 O O   . VAL B 474 ? 0.5869 1.2645 0.5625 -0.1298 0.0374  -0.2157 489 VAL B O   
6575 C CB  . VAL B 474 ? 0.5338 1.2533 0.5218 -0.1164 0.0229  -0.1913 489 VAL B CB  
6576 C CG1 . VAL B 474 ? 0.5154 1.2596 0.5042 -0.1039 0.0247  -0.1946 489 VAL B CG1 
6577 C CG2 . VAL B 474 ? 0.5448 1.2966 0.5244 -0.1353 0.0219  -0.1985 489 VAL B CG2 
6578 N N   . THR B 475 ? 0.5821 1.2661 0.5426 -0.1624 0.0343  -0.2206 490 THR B N   
6579 C CA  . THR B 475 ? 0.5886 1.2873 0.5366 -0.1788 0.0391  -0.2365 490 THR B CA  
6580 C C   . THR B 475 ? 0.5799 1.3386 0.5277 -0.1813 0.0355  -0.2401 490 THR B C   
6581 O O   . THR B 475 ? 0.5986 1.3799 0.5483 -0.1881 0.0318  -0.2373 490 THR B O   
6582 C CB  . THR B 475 ? 0.6137 1.2822 0.5460 -0.2049 0.0428  -0.2455 490 THR B CB  
6583 O OG1 . THR B 475 ? 0.6288 1.2407 0.5605 -0.2003 0.0459  -0.2442 490 THR B OG1 
6584 C CG2 . THR B 475 ? 0.6446 1.3370 0.5630 -0.2251 0.0472  -0.2628 490 THR B CG2 
6585 N N   . VAL B 476 ? 0.5871 1.3710 0.5326 -0.1754 0.0363  -0.2466 491 VAL B N   
6586 C CA  . VAL B 476 ? 0.5831 1.4247 0.5285 -0.1737 0.0311  -0.2501 491 VAL B CA  
6587 C C   . VAL B 476 ? 0.6093 1.4683 0.5405 -0.1962 0.0338  -0.2675 491 VAL B C   
6588 O O   . VAL B 476 ? 0.6438 1.4756 0.5654 -0.2008 0.0398  -0.2750 491 VAL B O   
6589 C CB  . VAL B 476 ? 0.5603 1.4126 0.5100 -0.1483 0.0287  -0.2426 491 VAL B CB  
6590 C CG1 . VAL B 476 ? 0.5537 1.4604 0.4992 -0.1452 0.0224  -0.2472 491 VAL B CG1 
6591 C CG2 . VAL B 476 ? 0.5287 1.3670 0.4919 -0.1276 0.0257  -0.2259 491 VAL B CG2 
6592 N N   . THR B 477 ? 0.6401 1.5454 0.5703 -0.2105 0.0297  -0.2751 492 THR B N   
6593 C CA  . THR B 477 ? 0.6759 1.5959 0.5918 -0.2363 0.0325  -0.2929 492 THR B CA  
6594 C C   . THR B 477 ? 0.7123 1.6932 0.6262 -0.2377 0.0257  -0.3020 492 THR B C   
6595 O O   . THR B 477 ? 0.7347 1.7167 0.6383 -0.2332 0.0259  -0.3070 492 THR B O   
6596 C CB  . THR B 477 ? 0.6787 1.5870 0.5888 -0.2649 0.0365  -0.2999 492 THR B CB  
6597 O OG1 . THR B 477 ? 0.6775 1.6088 0.6004 -0.2613 0.0324  -0.2915 492 THR B OG1 
6598 C CG2 . THR B 477 ? 0.6971 1.5361 0.5983 -0.2710 0.0439  -0.2977 492 THR B CG2 
6599 N N   . PRO B 478 ? 0.7368 1.7690 0.6598 -0.2447 0.0197  -0.3051 493 PRO B N   
6600 C CA  . PRO B 478 ? 0.7285 1.8166 0.6477 -0.2575 0.0141  -0.3193 493 PRO B CA  
6601 C C   . PRO B 478 ? 0.7070 1.8327 0.6304 -0.2313 0.0038  -0.3136 493 PRO B C   
6602 O O   . PRO B 478 ? 0.6819 1.8529 0.6202 -0.2191 -0.0045 -0.3094 493 PRO B O   
6603 C CB  . PRO B 478 ? 0.7296 1.8580 0.6612 -0.2727 0.0122  -0.3239 493 PRO B CB  
6604 C CG  . PRO B 478 ? 0.7440 1.8554 0.6896 -0.2522 0.0120  -0.3069 493 PRO B CG  
6605 C CD  . PRO B 478 ? 0.7201 1.7701 0.6599 -0.2336 0.0159  -0.2943 493 PRO B CD  
# 
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   MET 1   16  ?   ?   ?   A . n 
A 1 2   ALA 2   17  ?   ?   ?   A . n 
A 1 3   LYS 3   18  ?   ?   ?   A . n 
A 1 4   LYS 4   19  ?   ?   ?   A . n 
A 1 5   THR 5   20  ?   ?   ?   A . n 
A 1 6   SER 6   21  ?   ?   ?   A . n 
A 1 7   SER 7   22  ?   ?   ?   A . n 
A 1 8   LYS 8   23  ?   ?   ?   A . n 
A 1 9   GLY 9   24  ?   ?   ?   A . n 
A 1 10  LYS 10  25  ?   ?   ?   A . n 
A 1 11  GLU 11  26  ?   ?   ?   A . n 
A 1 12  GLY 12  27  ?   ?   ?   A . n 
A 1 13  VAL 13  28  ?   ?   ?   A . n 
A 1 14  GLY 14  29  ?   ?   ?   A . n 
A 1 15  SER 15  30  ?   ?   ?   A . n 
A 1 16  SER 16  31  ?   ?   ?   A . n 
A 1 17  SER 17  32  ?   ?   ?   A . n 
A 1 18  VAL 18  33  ?   ?   ?   A . n 
A 1 19  SER 19  34  ?   ?   ?   A . n 
A 1 20  PHE 20  35  ?   ?   ?   A . n 
A 1 21  PRO 21  36  ?   ?   ?   A . n 
A 1 22  CYS 22  37  ?   ?   ?   A . n 
A 1 23  LEU 23  38  ?   ?   ?   A . n 
A 1 24  PRO 24  39  ?   ?   ?   A . n 
A 1 25  ARG 25  40  ?   ?   ?   A . n 
A 1 26  LEU 26  41  ?   ?   ?   A . n 
A 1 27  PRO 27  42  ?   ?   ?   A . n 
A 1 28  LEU 28  43  ?   ?   ?   A . n 
A 1 29  LEU 29  44  ?   ?   ?   A . n 
A 1 30  GLY 30  45  ?   ?   ?   A . n 
A 1 31  SER 31  46  ?   ?   ?   A . n 
A 1 32  LEU 32  47  ?   ?   ?   A . n 
A 1 33  LEU 33  48  ?   ?   ?   A . n 
A 1 34  HIS 34  49  ?   ?   ?   A . n 
A 1 35  LEU 35  50  ?   ?   ?   A . n 
A 1 36  ARG 36  51  ?   ?   ?   A . n 
A 1 37  SER 37  52  ?   ?   ?   A . n 
A 1 38  ASN 38  53  53  ASN ASN A . n 
A 1 39  LEU 39  54  54  LEU LEU A . n 
A 1 40  PRO 40  55  55  PRO PRO A . n 
A 1 41  PRO 41  56  56  PRO PRO A . n 
A 1 42  HIS 42  57  57  HIS HIS A . n 
A 1 43  LEU 43  58  58  LEU LEU A . n 
A 1 44  LEU 44  59  59  LEU LEU A . n 
A 1 45  PHE 45  60  60  PHE PHE A . n 
A 1 46  THR 46  61  61  THR THR A . n 
A 1 47  GLN 47  62  62  GLN GLN A . n 
A 1 48  LEU 48  63  63  LEU LEU A . n 
A 1 49  SER 49  64  64  SER SER A . n 
A 1 50  SER 50  65  65  SER SER A . n 
A 1 51  GLN 51  66  66  GLN GLN A . n 
A 1 52  TYR 52  67  67  TYR TYR A . n 
A 1 53  GLY 53  68  68  GLY GLY A . n 
A 1 54  PRO 54  69  69  PRO PRO A . n 
A 1 55  LEU 55  70  70  LEU LEU A . n 
A 1 56  PHE 56  71  71  PHE PHE A . n 
A 1 57  GLY 57  72  72  GLY GLY A . n 
A 1 58  LEU 58  73  73  LEU LEU A . n 
A 1 59  TYR 59  74  74  TYR TYR A . n 
A 1 60  ALA 60  75  75  ALA ALA A . n 
A 1 61  GLY 61  76  76  GLY GLY A . n 
A 1 62  PRO 62  77  77  PRO PRO A . n 
A 1 63  HIS 63  78  78  HIS HIS A . n 
A 1 64  LEU 64  79  79  LEU LEU A . n 
A 1 65  THR 65  80  80  THR THR A . n 
A 1 66  LEU 66  81  81  LEU LEU A . n 
A 1 67  VAL 67  82  82  VAL VAL A . n 
A 1 68  VAL 68  83  83  VAL VAL A . n 
A 1 69  SER 69  84  84  SER SER A . n 
A 1 70  GLU 70  85  85  GLU GLU A . n 
A 1 71  ILE 71  86  86  ILE ILE A . n 
A 1 72  GLY 72  87  87  GLY GLY A . n 
A 1 73  LEU 73  88  88  LEU LEU A . n 
A 1 74  VAL 74  89  89  VAL VAL A . n 
A 1 75  ARG 75  90  90  ARG ARG A . n 
A 1 76  GLU 76  91  91  GLU GLU A . n 
A 1 77  VAL 77  92  92  VAL VAL A . n 
A 1 78  LEU 78  93  93  LEU LEU A . n 
A 1 79  LEU 79  94  94  LEU LEU A . n 
A 1 80  GLN 80  95  95  GLN GLN A . n 
A 1 81  ARG 81  96  96  ARG ARG A . n 
A 1 82  GLY 82  97  97  GLY GLY A . n 
A 1 83  ARG 83  98  98  ARG ARG A . n 
A 1 84  GLU 84  99  99  GLU GLU A . n 
A 1 85  PHE 85  100 100 PHE PHE A . n 
A 1 86  ALA 86  101 101 ALA ALA A . n 
A 1 87  GLY 87  102 102 GLY GLY A . n 
A 1 88  ARG 88  103 103 ARG ARG A . n 
A 1 89  PRO 89  104 104 PRO PRO A . n 
A 1 90  LYS 90  105 105 LYS LYS A . n 
A 1 91  MET 91  106 106 MET MET A . n 
A 1 92  VAL 92  107 107 VAL VAL A . n 
A 1 93  THR 93  108 108 THR THR A . n 
A 1 94  THR 94  109 109 THR THR A . n 
A 1 95  ASP 95  110 110 ASP ASP A . n 
A 1 96  LEU 96  111 111 LEU LEU A . n 
A 1 97  LEU 97  112 112 LEU LEU A . n 
A 1 98  THR 98  113 113 THR THR A . n 
A 1 99  GLN 99  114 114 GLN GLN A . n 
A 1 100 GLY 100 115 115 GLY GLY A . n 
A 1 101 GLY 101 116 116 GLY GLY A . n 
A 1 102 LYS 102 117 117 LYS LYS A . n 
A 1 103 ASP 103 118 118 ASP ASP A . n 
A 1 104 ILE 104 119 119 ILE ILE A . n 
A 1 105 ALA 105 120 120 ALA ALA A . n 
A 1 106 PHE 106 121 121 PHE PHE A . n 
A 1 107 ALA 107 122 122 ALA ALA A . n 
A 1 108 ASP 108 123 123 ASP ASP A . n 
A 1 109 TYR 109 124 124 TYR TYR A . n 
A 1 110 SER 110 125 125 SER SER A . n 
A 1 111 PRO 111 126 126 PRO PRO A . n 
A 1 112 LEU 112 127 127 LEU LEU A . n 
A 1 113 TRP 113 128 128 TRP TRP A . n 
A 1 114 LYS 114 129 129 LYS LYS A . n 
A 1 115 ASN 115 130 130 ASN ASN A . n 
A 1 116 HIS 116 131 131 HIS HIS A . n 
A 1 117 ARG 117 132 132 ARG ARG A . n 
A 1 118 ARG 118 133 133 ARG ARG A . n 
A 1 119 LEU 119 134 134 LEU LEU A . n 
A 1 120 VAL 120 135 135 VAL VAL A . n 
A 1 121 HIS 121 136 136 HIS HIS A . n 
A 1 122 SER 122 137 137 SER SER A . n 
A 1 123 SER 123 138 138 SER SER A . n 
A 1 124 PHE 124 139 139 PHE PHE A . n 
A 1 125 THR 125 140 140 THR THR A . n 
A 1 126 LEU 126 141 141 LEU LEU A . n 
A 1 127 PHE 127 142 142 PHE PHE A . n 
A 1 128 GLY 128 143 143 GLY GLY A . n 
A 1 129 GLU 129 144 144 GLU GLU A . n 
A 1 130 GLY 130 145 145 GLY GLY A . n 
A 1 131 SER 131 146 146 SER SER A . n 
A 1 132 ASN 132 147 147 ASN ASN A . n 
A 1 133 LYS 133 148 148 LYS LYS A . n 
A 1 134 LEU 134 149 149 LEU LEU A . n 
A 1 135 GLN 135 150 150 GLN GLN A . n 
A 1 136 THR 136 151 151 THR THR A . n 
A 1 137 ILE 137 152 152 ILE ILE A . n 
A 1 138 VAL 138 153 153 VAL VAL A . n 
A 1 139 GLN 139 154 154 GLN GLN A . n 
A 1 140 GLU 140 155 155 GLU GLU A . n 
A 1 141 ALA 141 156 156 ALA ALA A . n 
A 1 142 ALA 142 157 157 ALA ALA A . n 
A 1 143 ASP 143 158 158 ASP ASP A . n 
A 1 144 SER 144 159 159 SER SER A . n 
A 1 145 LEU 145 160 160 LEU LEU A . n 
A 1 146 CYS 146 161 161 CYS CYS A . n 
A 1 147 GLU 147 162 162 GLU GLU A . n 
A 1 148 GLU 148 163 163 GLU GLU A . n 
A 1 149 LEU 149 164 164 LEU LEU A . n 
A 1 150 GLN 150 165 165 GLN GLN A . n 
A 1 151 ALA 151 166 166 ALA ALA A . n 
A 1 152 CYS 152 167 167 CYS CYS A . n 
A 1 153 ARG 153 168 168 ARG ARG A . n 
A 1 154 GLY 154 169 169 GLY GLY A . n 
A 1 155 GLN 155 170 170 GLN GLN A . n 
A 1 156 SER 156 171 171 SER SER A . n 
A 1 157 SER 157 172 172 SER SER A . n 
A 1 158 ASP 158 173 173 ASP ASP A . n 
A 1 159 LEU 159 174 174 LEU LEU A . n 
A 1 160 SER 160 175 175 SER SER A . n 
A 1 161 VAL 161 176 176 VAL VAL A . n 
A 1 162 VAL 162 177 177 VAL VAL A . n 
A 1 163 LEU 163 178 178 LEU LEU A . n 
A 1 164 MET 164 179 179 MET MET A . n 
A 1 165 ARG 165 180 180 ARG ARG A . n 
A 1 166 ALA 166 181 181 ALA ALA A . n 
A 1 167 VAL 167 182 182 VAL VAL A . n 
A 1 168 THR 168 183 183 THR THR A . n 
A 1 169 ASN 169 184 184 ASN ASN A . n 
A 1 170 VAL 170 185 185 VAL VAL A . n 
A 1 171 ILE 171 186 186 ILE ILE A . n 
A 1 172 CYS 172 187 187 CYS CYS A . n 
A 1 173 ARG 173 188 188 ARG ARG A . n 
A 1 174 LEU 174 189 189 LEU LEU A . n 
A 1 175 VAL 175 190 190 VAL VAL A . n 
A 1 176 PHE 176 191 191 PHE PHE A . n 
A 1 177 SER 177 192 192 SER SER A . n 
A 1 178 SER 178 193 193 SER SER A . n 
A 1 179 SER 179 194 194 SER SER A . n 
A 1 180 TYR 180 195 195 TYR TYR A . n 
A 1 181 GLN 181 196 196 GLN GLN A . n 
A 1 182 PRO 182 197 197 PRO PRO A . n 
A 1 183 SER 183 198 198 SER SER A . n 
A 1 184 ASP 184 199 199 ASP ASP A . n 
A 1 185 PRO 185 200 200 PRO PRO A . n 
A 1 186 GLU 186 201 201 GLU GLU A . n 
A 1 187 LEU 187 202 202 LEU LEU A . n 
A 1 188 GLN 188 203 203 GLN GLN A . n 
A 1 189 THR 189 204 204 THR THR A . n 
A 1 190 VAL 190 205 205 VAL VAL A . n 
A 1 191 ILE 191 206 206 ILE ILE A . n 
A 1 192 GLN 192 207 207 GLN GLN A . n 
A 1 193 TYR 193 208 208 TYR TYR A . n 
A 1 194 ASN 194 209 209 ASN ASN A . n 
A 1 195 ASP 195 210 210 ASP ASP A . n 
A 1 196 GLY 196 211 211 GLY GLY A . n 
A 1 197 ILE 197 212 212 ILE ILE A . n 
A 1 198 VAL 198 213 213 VAL VAL A . n 
A 1 199 GLN 199 214 214 GLN GLN A . n 
A 1 200 THR 200 215 215 THR THR A . n 
A 1 201 ILE 201 216 216 ILE ILE A . n 
A 1 202 ALA 202 217 217 ALA ALA A . n 
A 1 203 ARG 203 218 218 ARG ARG A . n 
A 1 204 GLY 204 219 219 GLY GLY A . n 
A 1 205 GLY 205 220 220 GLY GLY A . n 
A 1 206 LEU 206 221 221 LEU LEU A . n 
A 1 207 VAL 207 222 222 VAL VAL A . n 
A 1 208 ASP 208 223 223 ASP ASP A . n 
A 1 209 ILE 209 224 224 ILE ILE A . n 
A 1 210 PHE 210 225 ?   ?   ?   A . n 
A 1 211 PRO 211 226 ?   ?   ?   A . n 
A 1 212 TRP 212 227 ?   ?   ?   A . n 
A 1 213 LEU 213 228 ?   ?   ?   A . n 
A 1 214 ARG 214 229 ?   ?   ?   A . n 
A 1 215 ILE 215 230 ?   ?   ?   A . n 
A 1 216 PHE 216 231 ?   ?   ?   A . n 
A 1 217 PRO 217 232 ?   ?   ?   A . n 
A 1 218 ASN 218 233 ?   ?   ?   A . n 
A 1 219 LYS 219 234 234 LYS LYS A . n 
A 1 220 ASP 220 235 235 ASP ASP A . n 
A 1 221 LEU 221 236 236 LEU LEU A . n 
A 1 222 LYS 222 237 237 LYS LYS A . n 
A 1 223 ARG 223 238 238 ARG ARG A . n 
A 1 224 LEU 224 239 239 LEU LEU A . n 
A 1 225 LYS 225 240 240 LYS LYS A . n 
A 1 226 GLU 226 241 241 GLU GLU A . n 
A 1 227 CYS 227 242 242 CYS CYS A . n 
A 1 228 VAL 228 243 243 VAL VAL A . n 
A 1 229 SER 229 244 244 SER SER A . n 
A 1 230 ILE 230 245 245 ILE ILE A . n 
A 1 231 ARG 231 246 246 ARG ARG A . n 
A 1 232 ASP 232 247 247 ASP ASP A . n 
A 1 233 GLN 233 248 248 GLN GLN A . n 
A 1 234 LEU 234 249 249 LEU LEU A . n 
A 1 235 LEU 235 250 250 LEU LEU A . n 
A 1 236 TYR 236 251 251 TYR TYR A . n 
A 1 237 LYS 237 252 252 LYS LYS A . n 
A 1 238 LYS 238 253 253 LYS LYS A . n 
A 1 239 LEU 239 254 254 LEU LEU A . n 
A 1 240 LEU 240 255 255 LEU LEU A . n 
A 1 241 GLU 241 256 256 GLU GLU A . n 
A 1 242 HIS 242 257 257 HIS HIS A . n 
A 1 243 LYS 243 258 258 LYS LYS A . n 
A 1 244 LYS 244 259 259 LYS LYS A . n 
A 1 245 SER 245 260 260 SER SER A . n 
A 1 246 LEU 246 261 261 LEU LEU A . n 
A 1 247 THR 247 262 262 THR THR A . n 
A 1 248 PRO 248 263 263 PRO PRO A . n 
A 1 249 GLY 249 264 264 GLY GLY A . n 
A 1 250 GLU 250 265 265 GLU GLU A . n 
A 1 251 PRO 251 266 266 PRO PRO A . n 
A 1 252 ARG 252 267 267 ARG ARG A . n 
A 1 253 ASP 253 268 268 ASP ASP A . n 
A 1 254 LEU 254 269 269 LEU LEU A . n 
A 1 255 LEU 255 270 270 LEU LEU A . n 
A 1 256 ASP 256 271 271 ASP ASP A . n 
A 1 257 ALA 257 272 272 ALA ALA A . n 
A 1 258 LEU 258 273 273 LEU LEU A . n 
A 1 259 LEU 259 274 274 LEU LEU A . n 
A 1 260 ILE 260 275 275 ILE ILE A . n 
A 1 261 GLY 261 276 276 GLY GLY A . n 
A 1 262 GLN 262 277 277 GLN GLN A . n 
A 1 263 GLN 263 278 278 GLN GLN A . n 
A 1 264 ARG 264 279 279 ARG ARG A . n 
A 1 265 GLY 265 280 280 GLY GLY A . n 
A 1 266 SER 266 281 281 SER SER A . n 
A 1 267 GLY 267 282 282 GLY GLY A . n 
A 1 268 GLY 268 283 283 GLY GLY A . n 
A 1 269 ALA 269 284 284 ALA ALA A . n 
A 1 270 ASP 270 285 285 ASP ASP A . n 
A 1 271 ASP 271 286 286 ASP ASP A . n 
A 1 272 ILE 272 287 287 ILE ILE A . n 
A 1 273 THR 273 288 288 THR THR A . n 
A 1 274 GLU 274 289 289 GLU GLU A . n 
A 1 275 ASP 275 290 290 ASP ASP A . n 
A 1 276 HIS 276 291 291 HIS HIS A . n 
A 1 277 VAL 277 292 292 VAL VAL A . n 
A 1 278 LEU 278 293 293 LEU LEU A . n 
A 1 279 MET 279 294 294 MET MET A . n 
A 1 280 THR 280 295 295 THR THR A . n 
A 1 281 ALA 281 296 296 ALA ALA A . n 
A 1 282 ALA 282 297 297 ALA ALA A . n 
A 1 283 GLU 283 298 298 GLU GLU A . n 
A 1 284 ALA 284 299 299 ALA ALA A . n 
A 1 285 PHE 285 300 300 PHE PHE A . n 
A 1 286 GLY 286 301 301 GLY GLY A . n 
A 1 287 ALA 287 302 302 ALA ALA A . n 
A 1 288 GLY 288 303 303 GLY GLY A . n 
A 1 289 VAL 289 304 304 VAL VAL A . n 
A 1 290 GLU 290 305 305 GLU GLU A . n 
A 1 291 THR 291 306 306 THR THR A . n 
A 1 292 THR 292 307 307 THR THR A . n 
A 1 293 SER 293 308 308 SER SER A . n 
A 1 294 THR 294 309 309 THR THR A . n 
A 1 295 THR 295 310 310 THR THR A . n 
A 1 296 LEU 296 311 311 LEU LEU A . n 
A 1 297 LEU 297 312 312 LEU LEU A . n 
A 1 298 TRP 298 313 313 TRP TRP A . n 
A 1 299 THR 299 314 314 THR THR A . n 
A 1 300 ILE 300 315 315 ILE ILE A . n 
A 1 301 ALA 301 316 316 ALA ALA A . n 
A 1 302 PHE 302 317 317 PHE PHE A . n 
A 1 303 LEU 303 318 318 LEU LEU A . n 
A 1 304 LEU 304 319 319 LEU LEU A . n 
A 1 305 HIS 305 320 320 HIS HIS A . n 
A 1 306 HIS 306 321 321 HIS HIS A . n 
A 1 307 PRO 307 322 322 PRO PRO A . n 
A 1 308 GLN 308 323 323 GLN GLN A . n 
A 1 309 LEU 309 324 324 LEU LEU A . n 
A 1 310 GLN 310 325 325 GLN GLN A . n 
A 1 311 GLU 311 326 326 GLU GLU A . n 
A 1 312 ARG 312 327 327 ARG ARG A . n 
A 1 313 VAL 313 328 328 VAL VAL A . n 
A 1 314 GLN 314 329 329 GLN GLN A . n 
A 1 315 ALA 315 330 330 ALA ALA A . n 
A 1 316 GLU 316 331 331 GLU GLU A . n 
A 1 317 LEU 317 332 332 LEU LEU A . n 
A 1 318 ASP 318 333 333 ASP ASP A . n 
A 1 319 GLU 319 334 334 GLU GLU A . n 
A 1 320 CYS 320 335 335 CYS CYS A . n 
A 1 321 VAL 321 336 336 VAL VAL A . n 
A 1 322 GLY 322 337 337 GLY GLY A . n 
A 1 323 VAL 323 338 338 VAL VAL A . n 
A 1 324 ASP 324 339 339 ASP ASP A . n 
A 1 325 ARG 325 340 340 ARG ARG A . n 
A 1 326 PRO 326 341 341 PRO PRO A . n 
A 1 327 PRO 327 342 342 PRO PRO A . n 
A 1 328 CYS 328 343 343 CYS CYS A . n 
A 1 329 LEU 329 344 344 LEU LEU A . n 
A 1 330 SER 330 345 345 SER SER A . n 
A 1 331 ASP 331 346 346 ASP ASP A . n 
A 1 332 ARG 332 347 347 ARG ARG A . n 
A 1 333 PRO 333 348 348 PRO PRO A . n 
A 1 334 HIS 334 349 349 HIS HIS A . n 
A 1 335 LEU 335 350 350 LEU LEU A . n 
A 1 336 PRO 336 351 351 PRO PRO A . n 
A 1 337 LEU 337 352 352 LEU LEU A . n 
A 1 338 LEU 338 353 353 LEU LEU A . n 
A 1 339 ASP 339 354 354 ASP ASP A . n 
A 1 340 ALA 340 355 355 ALA ALA A . n 
A 1 341 VAL 341 356 356 VAL VAL A . n 
A 1 342 LEU 342 357 357 LEU LEU A . n 
A 1 343 CYS 343 358 358 CYS CYS A . n 
A 1 344 GLU 344 359 359 GLU GLU A . n 
A 1 345 VAL 345 360 360 VAL VAL A . n 
A 1 346 MET 346 361 361 MET MET A . n 
A 1 347 ARG 347 362 362 ARG ARG A . n 
A 1 348 ILE 348 363 363 ILE ILE A . n 
A 1 349 ARG 349 364 364 ARG ARG A . n 
A 1 350 PRO 350 365 365 PRO PRO A . n 
A 1 351 VAL 351 366 366 VAL VAL A . n 
A 1 352 SER 352 367 367 SER SER A . n 
A 1 353 PRO 353 368 368 PRO PRO A . n 
A 1 354 ILE 354 369 369 ILE ILE A . n 
A 1 355 LEU 355 370 370 LEU LEU A . n 
A 1 356 ILE 356 371 371 ILE ILE A . n 
A 1 357 PRO 357 372 372 PRO PRO A . n 
A 1 358 HIS 358 373 373 HIS HIS A . n 
A 1 359 VAL 359 374 374 VAL VAL A . n 
A 1 360 ALA 360 375 375 ALA ALA A . n 
A 1 361 MET 361 376 376 MET MET A . n 
A 1 362 GLN 362 377 377 GLN GLN A . n 
A 1 363 ASP 363 378 378 ASP ASP A . n 
A 1 364 THR 364 379 379 THR THR A . n 
A 1 365 SER 365 380 380 SER SER A . n 
A 1 366 LEU 366 381 381 LEU LEU A . n 
A 1 367 GLY 367 382 382 GLY GLY A . n 
A 1 368 GLY 368 383 383 GLY GLY A . n 
A 1 369 HIS 369 384 384 HIS HIS A . n 
A 1 370 SER 370 385 385 SER SER A . n 
A 1 371 VAL 371 386 386 VAL VAL A . n 
A 1 372 PRO 372 387 387 PRO PRO A . n 
A 1 373 LYS 373 388 388 LYS LYS A . n 
A 1 374 GLY 374 389 389 GLY GLY A . n 
A 1 375 THR 375 390 390 THR THR A . n 
A 1 376 ARG 376 391 391 ARG ARG A . n 
A 1 377 VAL 377 392 392 VAL VAL A . n 
A 1 378 LEU 378 393 393 LEU LEU A . n 
A 1 379 VAL 379 394 394 VAL VAL A . n 
A 1 380 ASN 380 395 395 ASN ASN A . n 
A 1 381 MET 381 396 396 MET MET A . n 
A 1 382 TRP 382 397 397 TRP TRP A . n 
A 1 383 ALA 383 398 398 ALA ALA A . n 
A 1 384 ILE 384 399 399 ILE ILE A . n 
A 1 385 HIS 385 400 400 HIS HIS A . n 
A 1 386 HIS 386 401 401 HIS HIS A . n 
A 1 387 ASP 387 402 402 ASP ASP A . n 
A 1 388 PRO 388 403 403 PRO PRO A . n 
A 1 389 LYS 389 404 404 LYS LYS A . n 
A 1 390 HIS 390 405 405 HIS HIS A . n 
A 1 391 TRP 391 406 406 TRP TRP A . n 
A 1 392 ASP 392 407 407 ASP ASP A . n 
A 1 393 GLN 393 408 408 GLN GLN A . n 
A 1 394 PRO 394 409 409 PRO PRO A . n 
A 1 395 GLU 395 410 410 GLU GLU A . n 
A 1 396 GLN 396 411 411 GLN GLN A . n 
A 1 397 PHE 397 412 412 PHE PHE A . n 
A 1 398 ASN 398 413 413 ASN ASN A . n 
A 1 399 PRO 399 414 414 PRO PRO A . n 
A 1 400 GLU 400 415 415 GLU GLU A . n 
A 1 401 ARG 401 416 416 ARG ARG A . n 
A 1 402 PHE 402 417 417 PHE PHE A . n 
A 1 403 LEU 403 418 418 LEU LEU A . n 
A 1 404 GLU 404 419 419 GLU GLU A . n 
A 1 405 PRO 405 420 ?   ?   ?   A . n 
A 1 406 SER 406 421 ?   ?   ?   A . n 
A 1 407 GLY 407 422 ?   ?   ?   A . n 
A 1 408 LYS 408 423 ?   ?   ?   A . n 
A 1 409 LYS 409 424 ?   ?   ?   A . n 
A 1 410 LYS 410 425 ?   ?   ?   A . n 
A 1 411 THR 411 426 ?   ?   ?   A . n 
A 1 412 GLN 412 427 ?   ?   ?   A . n 
A 1 413 SER 413 428 428 SER SER A . n 
A 1 414 SER 414 429 429 SER SER A . n 
A 1 415 PHE 415 430 430 PHE PHE A . n 
A 1 416 LEU 416 431 431 LEU LEU A . n 
A 1 417 PRO 417 432 432 PRO PRO A . n 
A 1 418 PHE 418 433 433 PHE PHE A . n 
A 1 419 GLY 419 434 434 GLY GLY A . n 
A 1 420 ALA 420 435 435 ALA ALA A . n 
A 1 421 GLY 421 436 436 GLY GLY A . n 
A 1 422 PRO 422 437 437 PRO PRO A . n 
A 1 423 ARG 423 438 438 ARG ARG A . n 
A 1 424 VAL 424 439 439 VAL VAL A . n 
A 1 425 CYS 425 440 440 CYS CYS A . n 
A 1 426 VAL 426 441 441 VAL VAL A . n 
A 1 427 GLY 427 442 442 GLY GLY A . n 
A 1 428 GLU 428 443 443 GLU GLU A . n 
A 1 429 SER 429 444 444 SER SER A . n 
A 1 430 LEU 430 445 445 LEU LEU A . n 
A 1 431 ALA 431 446 446 ALA ALA A . n 
A 1 432 ARG 432 447 447 ARG ARG A . n 
A 1 433 ILE 433 448 448 ILE ILE A . n 
A 1 434 GLU 434 449 449 GLU GLU A . n 
A 1 435 LEU 435 450 450 LEU LEU A . n 
A 1 436 PHE 436 451 451 PHE PHE A . n 
A 1 437 LEU 437 452 452 LEU LEU A . n 
A 1 438 PHE 438 453 453 PHE PHE A . n 
A 1 439 VAL 439 454 454 VAL VAL A . n 
A 1 440 SER 440 455 455 SER SER A . n 
A 1 441 ARG 441 456 456 ARG ARG A . n 
A 1 442 PRO 442 457 457 PRO PRO A . n 
A 1 443 LEU 443 458 458 LEU LEU A . n 
A 1 444 GLN 444 459 459 GLN GLN A . n 
A 1 445 ARG 445 460 460 ARG ARG A . n 
A 1 446 PHE 446 461 461 PHE PHE A . n 
A 1 447 SER 447 462 462 SER SER A . n 
A 1 448 PHE 448 463 463 PHE PHE A . n 
A 1 449 SER 449 464 464 SER SER A . n 
A 1 450 CYS 450 465 465 CYS CYS A . n 
A 1 451 PRO 451 466 466 PRO PRO A . n 
A 1 452 SER 452 467 ?   ?   ?   A . n 
A 1 453 GLU 453 468 ?   ?   ?   A . n 
A 1 454 ALA 454 469 ?   ?   ?   A . n 
A 1 455 SER 455 470 470 SER SER A . n 
A 1 456 LEU 456 471 471 LEU LEU A . n 
A 1 457 PRO 457 472 472 PRO PRO A . n 
A 1 458 ASP 458 473 473 ASP ASP A . n 
A 1 459 LEU 459 474 474 LEU LEU A . n 
A 1 460 GLN 460 475 475 GLN GLN A . n 
A 1 461 GLY 461 476 476 GLY GLY A . n 
A 1 462 ARG 462 477 477 ARG ARG A . n 
A 1 463 PHE 463 478 478 PHE PHE A . n 
A 1 464 GLY 464 479 479 GLY GLY A . n 
A 1 465 VAL 465 480 480 VAL VAL A . n 
A 1 466 VAL 466 481 481 VAL VAL A . n 
A 1 467 LEU 467 482 482 LEU LEU A . n 
A 1 468 GLN 468 483 483 GLN GLN A . n 
A 1 469 PRO 469 484 484 PRO PRO A . n 
A 1 470 GLU 470 485 485 GLU GLU A . n 
A 1 471 ARG 471 486 486 ARG ARG A . n 
A 1 472 TYR 472 487 487 TYR TYR A . n 
A 1 473 THR 473 488 488 THR THR A . n 
A 1 474 VAL 474 489 489 VAL VAL A . n 
A 1 475 THR 475 490 490 THR THR A . n 
A 1 476 VAL 476 491 491 VAL VAL A . n 
A 1 477 THR 477 492 492 THR THR A . n 
A 1 478 PRO 478 493 493 PRO PRO A . n 
A 1 479 ARG 479 494 494 ARG ARG A . n 
A 1 480 HIS 480 495 ?   ?   ?   A . n 
A 1 481 HIS 481 496 ?   ?   ?   A . n 
A 1 482 HIS 482 497 ?   ?   ?   A . n 
A 1 483 HIS 483 498 ?   ?   ?   A . n 
A 1 484 HIS 484 499 ?   ?   ?   A . n 
A 1 485 HIS 485 500 ?   ?   ?   A . n 
A 1 486 HIS 486 501 ?   ?   ?   A . n 
B 1 1   MET 1   16  ?   ?   ?   B . n 
B 1 2   ALA 2   17  ?   ?   ?   B . n 
B 1 3   LYS 3   18  ?   ?   ?   B . n 
B 1 4   LYS 4   19  ?   ?   ?   B . n 
B 1 5   THR 5   20  ?   ?   ?   B . n 
B 1 6   SER 6   21  ?   ?   ?   B . n 
B 1 7   SER 7   22  ?   ?   ?   B . n 
B 1 8   LYS 8   23  ?   ?   ?   B . n 
B 1 9   GLY 9   24  ?   ?   ?   B . n 
B 1 10  LYS 10  25  ?   ?   ?   B . n 
B 1 11  GLU 11  26  ?   ?   ?   B . n 
B 1 12  GLY 12  27  ?   ?   ?   B . n 
B 1 13  VAL 13  28  ?   ?   ?   B . n 
B 1 14  GLY 14  29  ?   ?   ?   B . n 
B 1 15  SER 15  30  ?   ?   ?   B . n 
B 1 16  SER 16  31  ?   ?   ?   B . n 
B 1 17  SER 17  32  ?   ?   ?   B . n 
B 1 18  VAL 18  33  ?   ?   ?   B . n 
B 1 19  SER 19  34  ?   ?   ?   B . n 
B 1 20  PHE 20  35  ?   ?   ?   B . n 
B 1 21  PRO 21  36  ?   ?   ?   B . n 
B 1 22  CYS 22  37  ?   ?   ?   B . n 
B 1 23  LEU 23  38  ?   ?   ?   B . n 
B 1 24  PRO 24  39  ?   ?   ?   B . n 
B 1 25  ARG 25  40  ?   ?   ?   B . n 
B 1 26  LEU 26  41  ?   ?   ?   B . n 
B 1 27  PRO 27  42  ?   ?   ?   B . n 
B 1 28  LEU 28  43  ?   ?   ?   B . n 
B 1 29  LEU 29  44  ?   ?   ?   B . n 
B 1 30  GLY 30  45  ?   ?   ?   B . n 
B 1 31  SER 31  46  ?   ?   ?   B . n 
B 1 32  LEU 32  47  ?   ?   ?   B . n 
B 1 33  LEU 33  48  ?   ?   ?   B . n 
B 1 34  HIS 34  49  ?   ?   ?   B . n 
B 1 35  LEU 35  50  ?   ?   ?   B . n 
B 1 36  ARG 36  51  ?   ?   ?   B . n 
B 1 37  SER 37  52  ?   ?   ?   B . n 
B 1 38  ASN 38  53  53  ASN ASN B . n 
B 1 39  LEU 39  54  54  LEU LEU B . n 
B 1 40  PRO 40  55  55  PRO PRO B . n 
B 1 41  PRO 41  56  56  PRO PRO B . n 
B 1 42  HIS 42  57  57  HIS HIS B . n 
B 1 43  LEU 43  58  58  LEU LEU B . n 
B 1 44  LEU 44  59  59  LEU LEU B . n 
B 1 45  PHE 45  60  60  PHE PHE B . n 
B 1 46  THR 46  61  61  THR THR B . n 
B 1 47  GLN 47  62  62  GLN GLN B . n 
B 1 48  LEU 48  63  63  LEU LEU B . n 
B 1 49  SER 49  64  64  SER SER B . n 
B 1 50  SER 50  65  65  SER SER B . n 
B 1 51  GLN 51  66  66  GLN GLN B . n 
B 1 52  TYR 52  67  67  TYR TYR B . n 
B 1 53  GLY 53  68  68  GLY GLY B . n 
B 1 54  PRO 54  69  69  PRO PRO B . n 
B 1 55  LEU 55  70  70  LEU LEU B . n 
B 1 56  PHE 56  71  71  PHE PHE B . n 
B 1 57  GLY 57  72  72  GLY GLY B . n 
B 1 58  LEU 58  73  73  LEU LEU B . n 
B 1 59  TYR 59  74  74  TYR TYR B . n 
B 1 60  ALA 60  75  75  ALA ALA B . n 
B 1 61  GLY 61  76  76  GLY GLY B . n 
B 1 62  PRO 62  77  77  PRO PRO B . n 
B 1 63  HIS 63  78  78  HIS HIS B . n 
B 1 64  LEU 64  79  79  LEU LEU B . n 
B 1 65  THR 65  80  80  THR THR B . n 
B 1 66  LEU 66  81  81  LEU LEU B . n 
B 1 67  VAL 67  82  82  VAL VAL B . n 
B 1 68  VAL 68  83  83  VAL VAL B . n 
B 1 69  SER 69  84  84  SER SER B . n 
B 1 70  GLU 70  85  85  GLU GLU B . n 
B 1 71  ILE 71  86  86  ILE ILE B . n 
B 1 72  GLY 72  87  87  GLY GLY B . n 
B 1 73  LEU 73  88  88  LEU LEU B . n 
B 1 74  VAL 74  89  89  VAL VAL B . n 
B 1 75  ARG 75  90  90  ARG ARG B . n 
B 1 76  GLU 76  91  91  GLU GLU B . n 
B 1 77  VAL 77  92  92  VAL VAL B . n 
B 1 78  LEU 78  93  93  LEU LEU B . n 
B 1 79  LEU 79  94  94  LEU LEU B . n 
B 1 80  GLN 80  95  95  GLN GLN B . n 
B 1 81  ARG 81  96  96  ARG ARG B . n 
B 1 82  GLY 82  97  97  GLY GLY B . n 
B 1 83  ARG 83  98  98  ARG ARG B . n 
B 1 84  GLU 84  99  99  GLU GLU B . n 
B 1 85  PHE 85  100 100 PHE PHE B . n 
B 1 86  ALA 86  101 101 ALA ALA B . n 
B 1 87  GLY 87  102 102 GLY GLY B . n 
B 1 88  ARG 88  103 103 ARG ARG B . n 
B 1 89  PRO 89  104 104 PRO PRO B . n 
B 1 90  LYS 90  105 105 LYS LYS B . n 
B 1 91  MET 91  106 106 MET MET B . n 
B 1 92  VAL 92  107 107 VAL VAL B . n 
B 1 93  THR 93  108 108 THR THR B . n 
B 1 94  THR 94  109 109 THR THR B . n 
B 1 95  ASP 95  110 110 ASP ASP B . n 
B 1 96  LEU 96  111 111 LEU LEU B . n 
B 1 97  LEU 97  112 112 LEU LEU B . n 
B 1 98  THR 98  113 113 THR THR B . n 
B 1 99  GLN 99  114 114 GLN GLN B . n 
B 1 100 GLY 100 115 115 GLY GLY B . n 
B 1 101 GLY 101 116 116 GLY GLY B . n 
B 1 102 LYS 102 117 117 LYS LYS B . n 
B 1 103 ASP 103 118 118 ASP ASP B . n 
B 1 104 ILE 104 119 119 ILE ILE B . n 
B 1 105 ALA 105 120 120 ALA ALA B . n 
B 1 106 PHE 106 121 121 PHE PHE B . n 
B 1 107 ALA 107 122 122 ALA ALA B . n 
B 1 108 ASP 108 123 123 ASP ASP B . n 
B 1 109 TYR 109 124 124 TYR TYR B . n 
B 1 110 SER 110 125 125 SER SER B . n 
B 1 111 PRO 111 126 126 PRO PRO B . n 
B 1 112 LEU 112 127 127 LEU LEU B . n 
B 1 113 TRP 113 128 128 TRP TRP B . n 
B 1 114 LYS 114 129 129 LYS LYS B . n 
B 1 115 ASN 115 130 130 ASN ASN B . n 
B 1 116 HIS 116 131 131 HIS HIS B . n 
B 1 117 ARG 117 132 132 ARG ARG B . n 
B 1 118 ARG 118 133 133 ARG ARG B . n 
B 1 119 LEU 119 134 134 LEU LEU B . n 
B 1 120 VAL 120 135 135 VAL VAL B . n 
B 1 121 HIS 121 136 136 HIS HIS B . n 
B 1 122 SER 122 137 137 SER SER B . n 
B 1 123 SER 123 138 138 SER SER B . n 
B 1 124 PHE 124 139 139 PHE PHE B . n 
B 1 125 THR 125 140 140 THR THR B . n 
B 1 126 LEU 126 141 141 LEU LEU B . n 
B 1 127 PHE 127 142 142 PHE PHE B . n 
B 1 128 GLY 128 143 143 GLY GLY B . n 
B 1 129 GLU 129 144 144 GLU GLU B . n 
B 1 130 GLY 130 145 145 GLY GLY B . n 
B 1 131 SER 131 146 146 SER SER B . n 
B 1 132 ASN 132 147 147 ASN ASN B . n 
B 1 133 LYS 133 148 148 LYS LYS B . n 
B 1 134 LEU 134 149 149 LEU LEU B . n 
B 1 135 GLN 135 150 150 GLN GLN B . n 
B 1 136 THR 136 151 151 THR THR B . n 
B 1 137 ILE 137 152 152 ILE ILE B . n 
B 1 138 VAL 138 153 153 VAL VAL B . n 
B 1 139 GLN 139 154 154 GLN GLN B . n 
B 1 140 GLU 140 155 155 GLU GLU B . n 
B 1 141 ALA 141 156 156 ALA ALA B . n 
B 1 142 ALA 142 157 157 ALA ALA B . n 
B 1 143 ASP 143 158 158 ASP ASP B . n 
B 1 144 SER 144 159 159 SER SER B . n 
B 1 145 LEU 145 160 160 LEU LEU B . n 
B 1 146 CYS 146 161 161 CYS CYS B . n 
B 1 147 GLU 147 162 162 GLU GLU B . n 
B 1 148 GLU 148 163 163 GLU GLU B . n 
B 1 149 LEU 149 164 164 LEU LEU B . n 
B 1 150 GLN 150 165 165 GLN GLN B . n 
B 1 151 ALA 151 166 166 ALA ALA B . n 
B 1 152 CYS 152 167 167 CYS CYS B . n 
B 1 153 ARG 153 168 168 ARG ARG B . n 
B 1 154 GLY 154 169 169 GLY GLY B . n 
B 1 155 GLN 155 170 170 GLN GLN B . n 
B 1 156 SER 156 171 171 SER SER B . n 
B 1 157 SER 157 172 172 SER SER B . n 
B 1 158 ASP 158 173 173 ASP ASP B . n 
B 1 159 LEU 159 174 174 LEU LEU B . n 
B 1 160 SER 160 175 175 SER SER B . n 
B 1 161 VAL 161 176 176 VAL VAL B . n 
B 1 162 VAL 162 177 177 VAL VAL B . n 
B 1 163 LEU 163 178 178 LEU LEU B . n 
B 1 164 MET 164 179 179 MET MET B . n 
B 1 165 ARG 165 180 180 ARG ARG B . n 
B 1 166 ALA 166 181 181 ALA ALA B . n 
B 1 167 VAL 167 182 182 VAL VAL B . n 
B 1 168 THR 168 183 183 THR THR B . n 
B 1 169 ASN 169 184 184 ASN ASN B . n 
B 1 170 VAL 170 185 185 VAL VAL B . n 
B 1 171 ILE 171 186 186 ILE ILE B . n 
B 1 172 CYS 172 187 187 CYS CYS B . n 
B 1 173 ARG 173 188 188 ARG ARG B . n 
B 1 174 LEU 174 189 189 LEU LEU B . n 
B 1 175 VAL 175 190 190 VAL VAL B . n 
B 1 176 PHE 176 191 191 PHE PHE B . n 
B 1 177 SER 177 192 192 SER SER B . n 
B 1 178 SER 178 193 193 SER SER B . n 
B 1 179 SER 179 194 194 SER SER B . n 
B 1 180 TYR 180 195 195 TYR TYR B . n 
B 1 181 GLN 181 196 196 GLN GLN B . n 
B 1 182 PRO 182 197 197 PRO PRO B . n 
B 1 183 SER 183 198 198 SER SER B . n 
B 1 184 ASP 184 199 199 ASP ASP B . n 
B 1 185 PRO 185 200 200 PRO PRO B . n 
B 1 186 GLU 186 201 201 GLU GLU B . n 
B 1 187 LEU 187 202 202 LEU LEU B . n 
B 1 188 GLN 188 203 203 GLN GLN B . n 
B 1 189 THR 189 204 204 THR THR B . n 
B 1 190 VAL 190 205 205 VAL VAL B . n 
B 1 191 ILE 191 206 206 ILE ILE B . n 
B 1 192 GLN 192 207 207 GLN GLN B . n 
B 1 193 TYR 193 208 208 TYR TYR B . n 
B 1 194 ASN 194 209 209 ASN ASN B . n 
B 1 195 ASP 195 210 210 ASP ASP B . n 
B 1 196 GLY 196 211 211 GLY GLY B . n 
B 1 197 ILE 197 212 212 ILE ILE B . n 
B 1 198 VAL 198 213 213 VAL VAL B . n 
B 1 199 GLN 199 214 214 GLN GLN B . n 
B 1 200 THR 200 215 215 THR THR B . n 
B 1 201 ILE 201 216 216 ILE ILE B . n 
B 1 202 ALA 202 217 217 ALA ALA B . n 
B 1 203 ARG 203 218 218 ARG ARG B . n 
B 1 204 GLY 204 219 219 GLY GLY B . n 
B 1 205 GLY 205 220 220 GLY GLY B . n 
B 1 206 LEU 206 221 ?   ?   ?   B . n 
B 1 207 VAL 207 222 ?   ?   ?   B . n 
B 1 208 ASP 208 223 ?   ?   ?   B . n 
B 1 209 ILE 209 224 ?   ?   ?   B . n 
B 1 210 PHE 210 225 ?   ?   ?   B . n 
B 1 211 PRO 211 226 ?   ?   ?   B . n 
B 1 212 TRP 212 227 ?   ?   ?   B . n 
B 1 213 LEU 213 228 ?   ?   ?   B . n 
B 1 214 ARG 214 229 ?   ?   ?   B . n 
B 1 215 ILE 215 230 ?   ?   ?   B . n 
B 1 216 PHE 216 231 ?   ?   ?   B . n 
B 1 217 PRO 217 232 ?   ?   ?   B . n 
B 1 218 ASN 218 233 233 ASN ASN B . n 
B 1 219 LYS 219 234 234 LYS LYS B . n 
B 1 220 ASP 220 235 235 ASP ASP B . n 
B 1 221 LEU 221 236 236 LEU LEU B . n 
B 1 222 LYS 222 237 237 LYS LYS B . n 
B 1 223 ARG 223 238 238 ARG ARG B . n 
B 1 224 LEU 224 239 239 LEU LEU B . n 
B 1 225 LYS 225 240 240 LYS LYS B . n 
B 1 226 GLU 226 241 241 GLU GLU B . n 
B 1 227 CYS 227 242 242 CYS CYS B . n 
B 1 228 VAL 228 243 243 VAL VAL B . n 
B 1 229 SER 229 244 244 SER SER B . n 
B 1 230 ILE 230 245 245 ILE ILE B . n 
B 1 231 ARG 231 246 246 ARG ARG B . n 
B 1 232 ASP 232 247 247 ASP ASP B . n 
B 1 233 GLN 233 248 248 GLN GLN B . n 
B 1 234 LEU 234 249 249 LEU LEU B . n 
B 1 235 LEU 235 250 250 LEU LEU B . n 
B 1 236 TYR 236 251 251 TYR TYR B . n 
B 1 237 LYS 237 252 252 LYS LYS B . n 
B 1 238 LYS 238 253 253 LYS LYS B . n 
B 1 239 LEU 239 254 254 LEU LEU B . n 
B 1 240 LEU 240 255 255 LEU LEU B . n 
B 1 241 GLU 241 256 256 GLU GLU B . n 
B 1 242 HIS 242 257 257 HIS HIS B . n 
B 1 243 LYS 243 258 258 LYS LYS B . n 
B 1 244 LYS 244 259 259 LYS LYS B . n 
B 1 245 SER 245 260 260 SER SER B . n 
B 1 246 LEU 246 261 261 LEU LEU B . n 
B 1 247 THR 247 262 262 THR THR B . n 
B 1 248 PRO 248 263 263 PRO PRO B . n 
B 1 249 GLY 249 264 264 GLY GLY B . n 
B 1 250 GLU 250 265 265 GLU GLU B . n 
B 1 251 PRO 251 266 266 PRO PRO B . n 
B 1 252 ARG 252 267 267 ARG ARG B . n 
B 1 253 ASP 253 268 268 ASP ASP B . n 
B 1 254 LEU 254 269 269 LEU LEU B . n 
B 1 255 LEU 255 270 270 LEU LEU B . n 
B 1 256 ASP 256 271 271 ASP ASP B . n 
B 1 257 ALA 257 272 272 ALA ALA B . n 
B 1 258 LEU 258 273 273 LEU LEU B . n 
B 1 259 LEU 259 274 274 LEU LEU B . n 
B 1 260 ILE 260 275 275 ILE ILE B . n 
B 1 261 GLY 261 276 276 GLY GLY B . n 
B 1 262 GLN 262 277 277 GLN GLN B . n 
B 1 263 GLN 263 278 278 GLN GLN B . n 
B 1 264 ARG 264 279 279 ARG ARG B . n 
B 1 265 GLY 265 280 280 GLY GLY B . n 
B 1 266 SER 266 281 281 SER SER B . n 
B 1 267 GLY 267 282 282 GLY GLY B . n 
B 1 268 GLY 268 283 283 GLY GLY B . n 
B 1 269 ALA 269 284 284 ALA ALA B . n 
B 1 270 ASP 270 285 285 ASP ASP B . n 
B 1 271 ASP 271 286 286 ASP ASP B . n 
B 1 272 ILE 272 287 287 ILE ILE B . n 
B 1 273 THR 273 288 288 THR THR B . n 
B 1 274 GLU 274 289 289 GLU GLU B . n 
B 1 275 ASP 275 290 290 ASP ASP B . n 
B 1 276 HIS 276 291 291 HIS HIS B . n 
B 1 277 VAL 277 292 292 VAL VAL B . n 
B 1 278 LEU 278 293 293 LEU LEU B . n 
B 1 279 MET 279 294 294 MET MET B . n 
B 1 280 THR 280 295 295 THR THR B . n 
B 1 281 ALA 281 296 296 ALA ALA B . n 
B 1 282 ALA 282 297 297 ALA ALA B . n 
B 1 283 GLU 283 298 298 GLU GLU B . n 
B 1 284 ALA 284 299 299 ALA ALA B . n 
B 1 285 PHE 285 300 300 PHE PHE B . n 
B 1 286 GLY 286 301 301 GLY GLY B . n 
B 1 287 ALA 287 302 302 ALA ALA B . n 
B 1 288 GLY 288 303 303 GLY GLY B . n 
B 1 289 VAL 289 304 304 VAL VAL B . n 
B 1 290 GLU 290 305 305 GLU GLU B . n 
B 1 291 THR 291 306 306 THR THR B . n 
B 1 292 THR 292 307 307 THR THR B . n 
B 1 293 SER 293 308 308 SER SER B . n 
B 1 294 THR 294 309 309 THR THR B . n 
B 1 295 THR 295 310 310 THR THR B . n 
B 1 296 LEU 296 311 311 LEU LEU B . n 
B 1 297 LEU 297 312 312 LEU LEU B . n 
B 1 298 TRP 298 313 313 TRP TRP B . n 
B 1 299 THR 299 314 314 THR THR B . n 
B 1 300 ILE 300 315 315 ILE ILE B . n 
B 1 301 ALA 301 316 316 ALA ALA B . n 
B 1 302 PHE 302 317 317 PHE PHE B . n 
B 1 303 LEU 303 318 318 LEU LEU B . n 
B 1 304 LEU 304 319 319 LEU LEU B . n 
B 1 305 HIS 305 320 320 HIS HIS B . n 
B 1 306 HIS 306 321 321 HIS HIS B . n 
B 1 307 PRO 307 322 322 PRO PRO B . n 
B 1 308 GLN 308 323 323 GLN GLN B . n 
B 1 309 LEU 309 324 324 LEU LEU B . n 
B 1 310 GLN 310 325 325 GLN GLN B . n 
B 1 311 GLU 311 326 326 GLU GLU B . n 
B 1 312 ARG 312 327 327 ARG ARG B . n 
B 1 313 VAL 313 328 328 VAL VAL B . n 
B 1 314 GLN 314 329 329 GLN GLN B . n 
B 1 315 ALA 315 330 330 ALA ALA B . n 
B 1 316 GLU 316 331 331 GLU GLU B . n 
B 1 317 LEU 317 332 332 LEU LEU B . n 
B 1 318 ASP 318 333 333 ASP ASP B . n 
B 1 319 GLU 319 334 334 GLU GLU B . n 
B 1 320 CYS 320 335 335 CYS CYS B . n 
B 1 321 VAL 321 336 336 VAL VAL B . n 
B 1 322 GLY 322 337 337 GLY GLY B . n 
B 1 323 VAL 323 338 338 VAL VAL B . n 
B 1 324 ASP 324 339 339 ASP ASP B . n 
B 1 325 ARG 325 340 340 ARG ARG B . n 
B 1 326 PRO 326 341 341 PRO PRO B . n 
B 1 327 PRO 327 342 342 PRO PRO B . n 
B 1 328 CYS 328 343 343 CYS CYS B . n 
B 1 329 LEU 329 344 344 LEU LEU B . n 
B 1 330 SER 330 345 345 SER SER B . n 
B 1 331 ASP 331 346 346 ASP ASP B . n 
B 1 332 ARG 332 347 347 ARG ARG B . n 
B 1 333 PRO 333 348 348 PRO PRO B . n 
B 1 334 HIS 334 349 349 HIS HIS B . n 
B 1 335 LEU 335 350 350 LEU LEU B . n 
B 1 336 PRO 336 351 351 PRO PRO B . n 
B 1 337 LEU 337 352 352 LEU LEU B . n 
B 1 338 LEU 338 353 353 LEU LEU B . n 
B 1 339 ASP 339 354 354 ASP ASP B . n 
B 1 340 ALA 340 355 355 ALA ALA B . n 
B 1 341 VAL 341 356 356 VAL VAL B . n 
B 1 342 LEU 342 357 357 LEU LEU B . n 
B 1 343 CYS 343 358 358 CYS CYS B . n 
B 1 344 GLU 344 359 359 GLU GLU B . n 
B 1 345 VAL 345 360 360 VAL VAL B . n 
B 1 346 MET 346 361 361 MET MET B . n 
B 1 347 ARG 347 362 362 ARG ARG B . n 
B 1 348 ILE 348 363 363 ILE ILE B . n 
B 1 349 ARG 349 364 364 ARG ARG B . n 
B 1 350 PRO 350 365 365 PRO PRO B . n 
B 1 351 VAL 351 366 366 VAL VAL B . n 
B 1 352 SER 352 367 367 SER SER B . n 
B 1 353 PRO 353 368 368 PRO PRO B . n 
B 1 354 ILE 354 369 369 ILE ILE B . n 
B 1 355 LEU 355 370 370 LEU LEU B . n 
B 1 356 ILE 356 371 371 ILE ILE B . n 
B 1 357 PRO 357 372 372 PRO PRO B . n 
B 1 358 HIS 358 373 373 HIS HIS B . n 
B 1 359 VAL 359 374 374 VAL VAL B . n 
B 1 360 ALA 360 375 375 ALA ALA B . n 
B 1 361 MET 361 376 376 MET MET B . n 
B 1 362 GLN 362 377 377 GLN GLN B . n 
B 1 363 ASP 363 378 378 ASP ASP B . n 
B 1 364 THR 364 379 379 THR THR B . n 
B 1 365 SER 365 380 380 SER SER B . n 
B 1 366 LEU 366 381 381 LEU LEU B . n 
B 1 367 GLY 367 382 382 GLY GLY B . n 
B 1 368 GLY 368 383 383 GLY GLY B . n 
B 1 369 HIS 369 384 384 HIS HIS B . n 
B 1 370 SER 370 385 385 SER SER B . n 
B 1 371 VAL 371 386 386 VAL VAL B . n 
B 1 372 PRO 372 387 387 PRO PRO B . n 
B 1 373 LYS 373 388 388 LYS LYS B . n 
B 1 374 GLY 374 389 389 GLY GLY B . n 
B 1 375 THR 375 390 390 THR THR B . n 
B 1 376 ARG 376 391 391 ARG ARG B . n 
B 1 377 VAL 377 392 392 VAL VAL B . n 
B 1 378 LEU 378 393 393 LEU LEU B . n 
B 1 379 VAL 379 394 394 VAL VAL B . n 
B 1 380 ASN 380 395 395 ASN ASN B . n 
B 1 381 MET 381 396 396 MET MET B . n 
B 1 382 TRP 382 397 397 TRP TRP B . n 
B 1 383 ALA 383 398 398 ALA ALA B . n 
B 1 384 ILE 384 399 399 ILE ILE B . n 
B 1 385 HIS 385 400 400 HIS HIS B . n 
B 1 386 HIS 386 401 401 HIS HIS B . n 
B 1 387 ASP 387 402 402 ASP ASP B . n 
B 1 388 PRO 388 403 403 PRO PRO B . n 
B 1 389 LYS 389 404 404 LYS LYS B . n 
B 1 390 HIS 390 405 405 HIS HIS B . n 
B 1 391 TRP 391 406 406 TRP TRP B . n 
B 1 392 ASP 392 407 407 ASP ASP B . n 
B 1 393 GLN 393 408 408 GLN GLN B . n 
B 1 394 PRO 394 409 409 PRO PRO B . n 
B 1 395 GLU 395 410 410 GLU GLU B . n 
B 1 396 GLN 396 411 411 GLN GLN B . n 
B 1 397 PHE 397 412 412 PHE PHE B . n 
B 1 398 ASN 398 413 413 ASN ASN B . n 
B 1 399 PRO 399 414 414 PRO PRO B . n 
B 1 400 GLU 400 415 415 GLU GLU B . n 
B 1 401 ARG 401 416 416 ARG ARG B . n 
B 1 402 PHE 402 417 417 PHE PHE B . n 
B 1 403 LEU 403 418 418 LEU LEU B . n 
B 1 404 GLU 404 419 419 GLU GLU B . n 
B 1 405 PRO 405 420 420 PRO PRO B . n 
B 1 406 SER 406 421 ?   ?   ?   B . n 
B 1 407 GLY 407 422 ?   ?   ?   B . n 
B 1 408 LYS 408 423 ?   ?   ?   B . n 
B 1 409 LYS 409 424 ?   ?   ?   B . n 
B 1 410 LYS 410 425 ?   ?   ?   B . n 
B 1 411 THR 411 426 ?   ?   ?   B . n 
B 1 412 GLN 412 427 427 GLN GLN B . n 
B 1 413 SER 413 428 428 SER SER B . n 
B 1 414 SER 414 429 429 SER SER B . n 
B 1 415 PHE 415 430 430 PHE PHE B . n 
B 1 416 LEU 416 431 431 LEU LEU B . n 
B 1 417 PRO 417 432 432 PRO PRO B . n 
B 1 418 PHE 418 433 433 PHE PHE B . n 
B 1 419 GLY 419 434 434 GLY GLY B . n 
B 1 420 ALA 420 435 435 ALA ALA B . n 
B 1 421 GLY 421 436 436 GLY GLY B . n 
B 1 422 PRO 422 437 437 PRO PRO B . n 
B 1 423 ARG 423 438 438 ARG ARG B . n 
B 1 424 VAL 424 439 439 VAL VAL B . n 
B 1 425 CYS 425 440 440 CYS CYS B . n 
B 1 426 VAL 426 441 441 VAL VAL B . n 
B 1 427 GLY 427 442 442 GLY GLY B . n 
B 1 428 GLU 428 443 443 GLU GLU B . n 
B 1 429 SER 429 444 444 SER SER B . n 
B 1 430 LEU 430 445 445 LEU LEU B . n 
B 1 431 ALA 431 446 446 ALA ALA B . n 
B 1 432 ARG 432 447 447 ARG ARG B . n 
B 1 433 ILE 433 448 448 ILE ILE B . n 
B 1 434 GLU 434 449 449 GLU GLU B . n 
B 1 435 LEU 435 450 450 LEU LEU B . n 
B 1 436 PHE 436 451 451 PHE PHE B . n 
B 1 437 LEU 437 452 452 LEU LEU B . n 
B 1 438 PHE 438 453 453 PHE PHE B . n 
B 1 439 VAL 439 454 454 VAL VAL B . n 
B 1 440 SER 440 455 455 SER SER B . n 
B 1 441 ARG 441 456 456 ARG ARG B . n 
B 1 442 PRO 442 457 457 PRO PRO B . n 
B 1 443 LEU 443 458 458 LEU LEU B . n 
B 1 444 GLN 444 459 459 GLN GLN B . n 
B 1 445 ARG 445 460 460 ARG ARG B . n 
B 1 446 PHE 446 461 461 PHE PHE B . n 
B 1 447 SER 447 462 462 SER SER B . n 
B 1 448 PHE 448 463 463 PHE PHE B . n 
B 1 449 SER 449 464 464 SER SER B . n 
B 1 450 CYS 450 465 465 CYS CYS B . n 
B 1 451 PRO 451 466 466 PRO PRO B . n 
B 1 452 SER 452 467 467 SER SER B . n 
B 1 453 GLU 453 468 468 GLU GLU B . n 
B 1 454 ALA 454 469 469 ALA ALA B . n 
B 1 455 SER 455 470 470 SER SER B . n 
B 1 456 LEU 456 471 471 LEU LEU B . n 
B 1 457 PRO 457 472 472 PRO PRO B . n 
B 1 458 ASP 458 473 473 ASP ASP B . n 
B 1 459 LEU 459 474 474 LEU LEU B . n 
B 1 460 GLN 460 475 475 GLN GLN B . n 
B 1 461 GLY 461 476 476 GLY GLY B . n 
B 1 462 ARG 462 477 477 ARG ARG B . n 
B 1 463 PHE 463 478 478 PHE PHE B . n 
B 1 464 GLY 464 479 479 GLY GLY B . n 
B 1 465 VAL 465 480 480 VAL VAL B . n 
B 1 466 VAL 466 481 481 VAL VAL B . n 
B 1 467 LEU 467 482 482 LEU LEU B . n 
B 1 468 GLN 468 483 483 GLN GLN B . n 
B 1 469 PRO 469 484 484 PRO PRO B . n 
B 1 470 GLU 470 485 485 GLU GLU B . n 
B 1 471 ARG 471 486 486 ARG ARG B . n 
B 1 472 TYR 472 487 487 TYR TYR B . n 
B 1 473 THR 473 488 488 THR THR B . n 
B 1 474 VAL 474 489 489 VAL VAL B . n 
B 1 475 THR 475 490 490 THR THR B . n 
B 1 476 VAL 476 491 491 VAL VAL B . n 
B 1 477 THR 477 492 492 THR THR B . n 
B 1 478 PRO 478 493 493 PRO PRO B . n 
B 1 479 ARG 479 494 ?   ?   ?   B . n 
B 1 480 HIS 480 495 ?   ?   ?   B . n 
B 1 481 HIS 481 496 ?   ?   ?   B . n 
B 1 482 HIS 482 497 ?   ?   ?   B . n 
B 1 483 HIS 483 498 ?   ?   ?   B . n 
B 1 484 HIS 484 499 ?   ?   ?   B . n 
B 1 485 HIS 485 500 ?   ?   ?   B . n 
B 1 486 HIS 486 501 ?   ?   ?   B . n 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_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  SG ? B CYS 425 ? B CYS 440 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 NA ? E HEM . ? B HEM 600 ? 1_555 93.5  ? 
2  SG ? B CYS 425 ? B CYS 440 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 NB ? E HEM . ? B HEM 600 ? 1_555 91.7  ? 
3  NA ? E HEM .   ? B HEM 600 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 NB ? E HEM . ? B HEM 600 ? 1_555 88.3  ? 
4  SG ? B CYS 425 ? B CYS 440 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 NC ? E HEM . ? B HEM 600 ? 1_555 87.3  ? 
5  NA ? E HEM .   ? B HEM 600 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 NC ? E HEM . ? B HEM 600 ? 1_555 177.3 ? 
6  NB ? E HEM .   ? B HEM 600 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 NC ? E HEM . ? B HEM 600 ? 1_555 89.2  ? 
7  SG ? B CYS 425 ? B CYS 440 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 ND ? E HEM . ? B HEM 600 ? 1_555 88.8  ? 
8  NA ? E HEM .   ? B HEM 600 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 ND ? E HEM . ? B HEM 600 ? 1_555 92.1  ? 
9  NB ? E HEM .   ? B HEM 600 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 ND ? E HEM . ? B HEM 600 ? 1_555 179.4 ? 
10 NC ? E HEM .   ? B HEM 600 ? 1_555 FE ? E HEM . ? B HEM 600 ? 1_555 ND ? E HEM . ? B HEM 600 ? 1_555 90.4  ? 
11 SG ? A CYS 425 ? A CYS 440 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 NA ? C HEM . ? A HEM 600 ? 1_555 93.4  ? 
12 SG ? A CYS 425 ? A CYS 440 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 NB ? C HEM . ? A HEM 600 ? 1_555 94.4  ? 
13 NA ? C HEM .   ? A HEM 600 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 NB ? C HEM . ? A HEM 600 ? 1_555 88.8  ? 
14 SG ? A CYS 425 ? A CYS 440 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 NC ? C HEM . ? A HEM 600 ? 1_555 88.0  ? 
15 NA ? C HEM .   ? A HEM 600 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 NC ? C HEM . ? A HEM 600 ? 1_555 177.7 ? 
16 NB ? C HEM .   ? A HEM 600 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 NC ? C HEM . ? A HEM 600 ? 1_555 89.2  ? 
17 SG ? A CYS 425 ? A CYS 440 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 ND ? C HEM . ? A HEM 600 ? 1_555 86.8  ? 
18 NA ? C HEM .   ? A HEM 600 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 ND ? C HEM . ? A HEM 600 ? 1_555 92.0  ? 
19 NB ? C HEM .   ? A HEM 600 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 ND ? C HEM . ? A HEM 600 ? 1_555 178.5 ? 
20 NC ? C HEM .   ? A HEM 600 ? 1_555 FE ? C HEM . ? A HEM 600 ? 1_555 ND ? C HEM . ? A HEM 600 ? 1_555 89.9  ? 
# 
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 2014-12-31 
2 'Structure model' 1 1 2015-03-04 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 12.4716  0.4396 1.0003  0.0570 0.4534 0.0717 -0.0174 -0.0472 0.0139  1.2834 1.4371 1.4289 -0.5178 
0.4602  -0.3047 -0.0328 -0.0299 -0.1409 0.0719  0.0284  0.0760  0.0098  0.0224  0.0044 
'X-RAY DIFFRACTION' 2 ? refined -14.6262 5.2246 45.0225 0.0535 0.7688 0.0090 0.1454  -0.0188 -0.0415 0.9274 1.7298 2.4282 0.5818  
-0.0563 0.6500  0.0585  0.2871  -0.0417 -0.1268 -0.1594 -0.0037 -0.2878 -0.6988 0.1010 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 53 ? ? A 601 ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 53 ? ? B 601 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MD2      'data collection' 'diffractometer software from EMBL (with LS-CAT developed extensions)' ? 1 
PHASER   phasing           .                                                                      ? 2 
REFMAC   refinement        5.8.0073                                                               ? 3 
HKL-2000 'data reduction'  .                                                                      ? 4 
HKL-2000 'data scaling'    .                                                                      ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 CD A LYS 234 ? ? CD2 A LEU 236 ? ? 2.03 
2 1 CG A LYS 234 ? ? CD2 A LEU 236 ? ? 2.12 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             O 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_1              233 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             C 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_2              233 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             N 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              234 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                111.69 
_pdbx_validate_rmsd_angle.angle_target_value         122.70 
_pdbx_validate_rmsd_angle.angle_deviation            -11.01 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
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 ALA A 75  ? ? -163.85 109.27  
2  1 LEU A 94  ? ? -83.27  -71.41  
3  1 ASP A 118 ? ? -85.64  -155.31 
4  1 SER A 146 ? ? -155.03 -152.37 
5  1 SER A 171 ? ? -105.34 63.58   
6  1 SER A 175 ? ? 134.16  -50.86  
7  1 VAL A 222 ? ? 28.01   42.47   
8  1 ASP A 235 ? ? 85.59   -19.93  
9  1 PRO A 266 ? ? -122.72 -97.45  
10 1 SER A 281 ? ? -24.47  -81.19  
11 1 ALA A 284 ? ? -23.93  -74.80  
12 1 THR A 379 ? ? -136.97 -153.49 
13 1 ALA A 435 ? ? 174.12  177.49  
14 1 ARG A 486 ? ? -39.85  133.76  
15 1 PRO A 493 ? ? -97.98  -157.29 
16 1 LEU B 94  ? ? -85.00  -76.13  
17 1 ASP B 118 ? ? -97.26  -154.95 
18 1 LEU B 141 ? ? -65.75  48.77   
19 1 PHE B 142 ? ? -157.08 -17.23  
20 1 GLU B 144 ? ? -117.33 -113.45 
21 1 LEU B 174 ? ? -63.65  -178.43 
22 1 SER B 175 ? ? 94.03   -49.14  
23 1 LYS B 234 ? ? -40.29  157.70  
24 1 ASP B 235 ? ? 85.62   9.16    
25 1 LYS B 259 ? ? -59.11  -84.40  
26 1 GLU B 305 ? ? 92.64   -57.86  
27 1 VAL B 338 ? ? -76.94  35.81   
28 1 ARG B 340 ? ? 90.11   137.07  
29 1 PRO B 372 ? ? -28.12  142.27  
30 1 PRO B 466 ? ? -33.00  137.13  
31 1 SER B 467 ? ? -23.33  -47.74  
32 1 THR B 492 ? ? -122.00 -82.69  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 GLY A 220 ? ? LEU A 221 ? ? 136.95  
2 1 PRO A 266 ? ? ARG A 267 ? ? -35.69  
3 1 PHE B 142 ? ? GLY B 143 ? ? 149.62  
4 1 GLY B 145 ? ? SER B 146 ? ? -51.65  
5 1 LYS B 234 ? ? ASP B 235 ? ? -148.58 
6 1 ASP B 235 ? ? LEU B 236 ? ? 134.12  
7 1 LEU B 418 ? ? GLU B 419 ? ? 139.04  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 456 ? ? 0.176 'SIDE CHAIN' 
2 1 ARG B 267 ? ? 0.143 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASN 53  ? CG  ? A ASN 38  CG  
2  1 Y 1 A ASN 53  ? OD1 ? A ASN 38  OD1 
3  1 Y 1 A ASN 53  ? ND2 ? A ASN 38  ND2 
4  1 Y 0 A LYS 234 ? CB  ? A LYS 219 CB  
5  1 Y 0 A LYS 234 ? CG  ? A LYS 219 CG  
6  1 Y 0 A LYS 234 ? CD  ? A LYS 219 CD  
7  1 Y 0 A LYS 234 ? CE  ? A LYS 219 CE  
8  1 Y 0 A LYS 234 ? NZ  ? A LYS 219 NZ  
9  1 Y 0 B ASN 147 ? CB  ? B ASN 132 CB  
10 1 Y 0 B ASN 147 ? CG  ? B ASN 132 CG  
11 1 Y 0 B ASN 147 ? OD1 ? B ASN 132 OD1 
12 1 Y 0 B ASN 147 ? ND2 ? B ASN 132 ND2 
13 1 Y 0 B LYS 234 ? CB  ? B LYS 219 CB  
14 1 Y 0 B LYS 234 ? CG  ? B LYS 219 CG  
15 1 Y 0 B LYS 234 ? CD  ? B LYS 219 CD  
16 1 Y 0 B LYS 234 ? CE  ? B LYS 219 CE  
17 1 Y 0 B LYS 234 ? NZ  ? B LYS 219 NZ  
18 1 Y 1 B PRO 420 ? CG  ? B PRO 405 CG  
19 1 Y 1 B PRO 420 ? CD  ? B PRO 405 CD  
20 1 N 1 A HEM 600 ? O2D ? C HEM 1   O2D 
21 1 N 1 B HEM 600 ? O2D ? E HEM 1   O2D 
# 
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 MET 16  ? A MET 1   
2   1 Y 1 A ALA 17  ? A ALA 2   
3   1 Y 1 A LYS 18  ? A LYS 3   
4   1 Y 1 A LYS 19  ? A LYS 4   
5   1 Y 1 A THR 20  ? A THR 5   
6   1 Y 1 A SER 21  ? A SER 6   
7   1 Y 1 A SER 22  ? A SER 7   
8   1 Y 1 A LYS 23  ? A LYS 8   
9   1 Y 1 A GLY 24  ? A GLY 9   
10  1 Y 1 A LYS 25  ? A LYS 10  
11  1 Y 1 A GLU 26  ? A GLU 11  
12  1 Y 1 A GLY 27  ? A GLY 12  
13  1 Y 1 A VAL 28  ? A VAL 13  
14  1 Y 1 A GLY 29  ? A GLY 14  
15  1 Y 1 A SER 30  ? A SER 15  
16  1 Y 1 A SER 31  ? A SER 16  
17  1 Y 1 A SER 32  ? A SER 17  
18  1 Y 1 A VAL 33  ? A VAL 18  
19  1 Y 1 A SER 34  ? A SER 19  
20  1 Y 1 A PHE 35  ? A PHE 20  
21  1 Y 1 A PRO 36  ? A PRO 21  
22  1 Y 1 A CYS 37  ? A CYS 22  
23  1 Y 1 A LEU 38  ? A LEU 23  
24  1 Y 1 A PRO 39  ? A PRO 24  
25  1 Y 1 A ARG 40  ? A ARG 25  
26  1 Y 1 A LEU 41  ? A LEU 26  
27  1 Y 1 A PRO 42  ? A PRO 27  
28  1 Y 1 A LEU 43  ? A LEU 28  
29  1 Y 1 A LEU 44  ? A LEU 29  
30  1 Y 1 A GLY 45  ? A GLY 30  
31  1 Y 1 A SER 46  ? A SER 31  
32  1 Y 1 A LEU 47  ? A LEU 32  
33  1 Y 1 A LEU 48  ? A LEU 33  
34  1 Y 1 A HIS 49  ? A HIS 34  
35  1 Y 1 A LEU 50  ? A LEU 35  
36  1 Y 1 A ARG 51  ? A ARG 36  
37  1 Y 1 A SER 52  ? A SER 37  
38  1 Y 1 A PHE 225 ? A PHE 210 
39  1 Y 1 A PRO 226 ? A PRO 211 
40  1 Y 1 A TRP 227 ? A TRP 212 
41  1 Y 1 A LEU 228 ? A LEU 213 
42  1 Y 1 A ARG 229 ? A ARG 214 
43  1 Y 1 A ILE 230 ? A ILE 215 
44  1 Y 1 A PHE 231 ? A PHE 216 
45  1 Y 1 A PRO 232 ? A PRO 217 
46  1 Y 1 A ASN 233 ? A ASN 218 
47  1 Y 1 A PRO 420 ? A PRO 405 
48  1 Y 1 A SER 421 ? A SER 406 
49  1 Y 1 A GLY 422 ? A GLY 407 
50  1 Y 1 A LYS 423 ? A LYS 408 
51  1 Y 1 A LYS 424 ? A LYS 409 
52  1 Y 1 A LYS 425 ? A LYS 410 
53  1 Y 1 A THR 426 ? A THR 411 
54  1 Y 1 A GLN 427 ? A GLN 412 
55  1 Y 1 A SER 467 ? A SER 452 
56  1 Y 1 A GLU 468 ? A GLU 453 
57  1 Y 1 A ALA 469 ? A ALA 454 
58  1 Y 1 A HIS 495 ? A HIS 480 
59  1 Y 1 A HIS 496 ? A HIS 481 
60  1 Y 1 A HIS 497 ? A HIS 482 
61  1 Y 1 A HIS 498 ? A HIS 483 
62  1 Y 1 A HIS 499 ? A HIS 484 
63  1 Y 1 A HIS 500 ? A HIS 485 
64  1 Y 1 A HIS 501 ? A HIS 486 
65  1 Y 1 B MET 16  ? B MET 1   
66  1 Y 1 B ALA 17  ? B ALA 2   
67  1 Y 1 B LYS 18  ? B LYS 3   
68  1 Y 1 B LYS 19  ? B LYS 4   
69  1 Y 1 B THR 20  ? B THR 5   
70  1 Y 1 B SER 21  ? B SER 6   
71  1 Y 1 B SER 22  ? B SER 7   
72  1 Y 1 B LYS 23  ? B LYS 8   
73  1 Y 1 B GLY 24  ? B GLY 9   
74  1 Y 1 B LYS 25  ? B LYS 10  
75  1 Y 1 B GLU 26  ? B GLU 11  
76  1 Y 1 B GLY 27  ? B GLY 12  
77  1 Y 1 B VAL 28  ? B VAL 13  
78  1 Y 1 B GLY 29  ? B GLY 14  
79  1 Y 1 B SER 30  ? B SER 15  
80  1 Y 1 B SER 31  ? B SER 16  
81  1 Y 1 B SER 32  ? B SER 17  
82  1 Y 1 B VAL 33  ? B VAL 18  
83  1 Y 1 B SER 34  ? B SER 19  
84  1 Y 1 B PHE 35  ? B PHE 20  
85  1 Y 1 B PRO 36  ? B PRO 21  
86  1 Y 1 B CYS 37  ? B CYS 22  
87  1 Y 1 B LEU 38  ? B LEU 23  
88  1 Y 1 B PRO 39  ? B PRO 24  
89  1 Y 1 B ARG 40  ? B ARG 25  
90  1 Y 1 B LEU 41  ? B LEU 26  
91  1 Y 1 B PRO 42  ? B PRO 27  
92  1 Y 1 B LEU 43  ? B LEU 28  
93  1 Y 1 B LEU 44  ? B LEU 29  
94  1 Y 1 B GLY 45  ? B GLY 30  
95  1 Y 1 B SER 46  ? B SER 31  
96  1 Y 1 B LEU 47  ? B LEU 32  
97  1 Y 1 B LEU 48  ? B LEU 33  
98  1 Y 1 B HIS 49  ? B HIS 34  
99  1 Y 1 B LEU 50  ? B LEU 35  
100 1 Y 1 B ARG 51  ? B ARG 36  
101 1 Y 1 B SER 52  ? B SER 37  
102 1 Y 1 B LEU 221 ? B LEU 206 
103 1 Y 1 B VAL 222 ? B VAL 207 
104 1 Y 1 B ASP 223 ? B ASP 208 
105 1 Y 1 B ILE 224 ? B ILE 209 
106 1 Y 1 B PHE 225 ? B PHE 210 
107 1 Y 1 B PRO 226 ? B PRO 211 
108 1 Y 1 B TRP 227 ? B TRP 212 
109 1 Y 1 B LEU 228 ? B LEU 213 
110 1 Y 1 B ARG 229 ? B ARG 214 
111 1 Y 1 B ILE 230 ? B ILE 215 
112 1 Y 1 B PHE 231 ? B PHE 216 
113 1 Y 1 B PRO 232 ? B PRO 217 
114 1 Y 1 B SER 421 ? B SER 406 
115 1 Y 1 B GLY 422 ? B GLY 407 
116 1 Y 1 B LYS 423 ? B LYS 408 
117 1 Y 1 B LYS 424 ? B LYS 409 
118 1 Y 1 B LYS 425 ? B LYS 410 
119 1 Y 1 B THR 426 ? B THR 411 
120 1 Y 1 B ARG 494 ? B ARG 479 
121 1 Y 1 B HIS 495 ? B HIS 480 
122 1 Y 1 B HIS 496 ? B HIS 481 
123 1 Y 1 B HIS 497 ? B HIS 482 
124 1 Y 1 B HIS 498 ? B HIS 483 
125 1 Y 1 B HIS 499 ? B HIS 484 
126 1 Y 1 B HIS 500 ? B HIS 485 
127 1 Y 1 B HIS 501 ? B HIS 486 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
3 PROGESTERONE                      STR 
4 water                             HOH 
# 
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 
C 2 HEM 1  600 600 HEM HEM A . 
D 3 STR 1  601 601 STR STR A . 
E 2 HEM 1  600 600 HEM HEM B . 
F 3 STR 1  601 601 STR STR B . 
G 4 HOH 1  701 1   HOH HOH A . 
G 4 HOH 2  702 2   HOH HOH A . 
G 4 HOH 3  703 3   HOH HOH A . 
G 4 HOH 4  704 4   HOH HOH A . 
G 4 HOH 5  705 5   HOH HOH A . 
G 4 HOH 6  706 6   HOH HOH A . 
G 4 HOH 7  707 17  HOH HOH A . 
H 4 HOH 1  701 7   HOH HOH B . 
H 4 HOH 2  702 8   HOH HOH B . 
H 4 HOH 3  703 9   HOH HOH B . 
H 4 HOH 4  704 10  HOH HOH B . 
H 4 HOH 5  705 11  HOH HOH B . 
H 4 HOH 6  706 12  HOH HOH B . 
H 4 HOH 7  707 13  HOH HOH B . 
H 4 HOH 8  708 14  HOH HOH B . 
H 4 HOH 9  709 15  HOH HOH B . 
H 4 HOH 10 710 16  HOH HOH B . 
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