data_8ZB0
# 
_entry.id   8ZB0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZB0         pdb_00008zb0 10.2210/pdb8zb0/pdb 
WWPDB D_1300047274 ?            ?                   
EMDB  EMD-39893    ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'EM metadata'     1 0 2025-03-12 ? 
3 'Half map'        1 0 2025-03-12 1 
4 'Half map'        1 0 2025-03-12 2 
5 Image             1 0 2025-03-12 ? 
6 'Primary map'     1 0 2025-03-12 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 'Half map'        repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 Image             repository 'Initial release' ? ? 
6 6 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZB0 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of human ZnT1' 
_pdbx_database_related.db_id          EMD-39893 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              fwang@zju.edu.cn 
_pdbx_contact_author.name_first         Fudi 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8730-0003 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sun, S.' 1 ? 
'Xie, E.' 2 ? 
'Xu, S.'  3 ? 
'Ji, S.'  4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Adv Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2198-3844 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            11 
_citation.language                  ? 
_citation.page_first                e2406421 
_citation.page_last                 e2406421 
_citation.title                     
'The Intestinal Transporter SLC30A1 Plays a Critical Role in Regulating Systemic Zinc Homeostasis.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/advs.202406421 
_citation.pdbx_database_id_PubMed   39422023 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sun, S.'   1  ?                   
primary 'Xie, E.'   2  ?                   
primary 'Xu, S.'    3  ?                   
primary 'Ji, S.'    4  ?                   
primary 'Wang, S.'  5  ?                   
primary 'Shen, J.'  6  ?                   
primary 'Wang, R.'  7  ?                   
primary 'Shen, X.'  8  ?                   
primary 'Su, Y.'    9  ?                   
primary 'Song, Z.'  10 ?                   
primary 'Wu, X.'    11 ?                   
primary 'Zhou, J.'  12 ?                   
primary 'Cai, Z.'   13 ?                   
primary 'Li, X.'    14 ?                   
primary 'Zhang, Y.' 15 ?                   
primary 'Min, J.'   16 ?                   
primary 'Wang, F.'  17 0000-0001-8730-0003 
# 
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     man 'Proton-coupled zinc antiporter SLC30A1' 55362.605 2 ? ? ? ? 
2 non-polymer syn 'ZINC ION'                               65.409    8 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Solute carrier family 30 member 1,Zinc transporter 1' 
# 
_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       
;MGCWGRNRGRLLCMLALTFMFMVLEVVVSRVTSSLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVM
GALVNAIFLTGLCFAILLEAIERFIEPHEMQQPLVVLGVGVAGLLVNVLGLCLFHHHSGFSQDSGHGHSHGGHGHGHGLP
KGPRVKSTRPGSSDINVAPGEQGPDQEETNTLVANTSNSNGLKLDPADPENPRSGDTVEVQVNGNLVREPDHMELEEDRA
GQLNMRGVFLHVLGDALGSVIVVVNALVFYFSWKGCSEGDFCVNPCFPDPCKAFVEIINSTHASVYEAGPCWVLYLDPTL
CVVMVCILLYTTYPLLKESALILLQTVPKQIDIRNLIKELRNVEGVEEVHELHVWQLAGSRIIATAHIKCEDPTSYMEVA
KTIKDVFHNHGIHATTIQPEFASVGSKSSVVPCELACRTQCALKQCCGTLPQAPSGKDAEKTPAVSISCLELSNNLEKKP
RRTKAENIPAVVIEIKNMPNKQPESSL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGCWGRNRGRLLCMLALTFMFMVLEVVVSRVTSSLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVM
GALVNAIFLTGLCFAILLEAIERFIEPHEMQQPLVVLGVGVAGLLVNVLGLCLFHHHSGFSQDSGHGHSHGGHGHGHGLP
KGPRVKSTRPGSSDINVAPGEQGPDQEETNTLVANTSNSNGLKLDPADPENPRSGDTVEVQVNGNLVREPDHMELEEDRA
GQLNMRGVFLHVLGDALGSVIVVVNALVFYFSWKGCSEGDFCVNPCFPDPCKAFVEIINSTHASVYEAGPCWVLYLDPTL
CVVMVCILLYTTYPLLKESALILLQTVPKQIDIRNLIKELRNVEGVEEVHELHVWQLAGSRIIATAHIKCEDPTSYMEVA
KTIKDVFHNHGIHATTIQPEFASVGSKSSVVPCELACRTQCALKQCCGTLPQAPSGKDAEKTPAVSISCLELSNNLEKKP
RRTKAENIPAVVIEIKNMPNKQPESSL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'ZINC ION' 
_pdbx_entity_nonpoly.comp_id     ZN 
# 
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   GLY n 
1 3   CYS n 
1 4   TRP n 
1 5   GLY n 
1 6   ARG n 
1 7   ASN n 
1 8   ARG n 
1 9   GLY n 
1 10  ARG n 
1 11  LEU n 
1 12  LEU n 
1 13  CYS n 
1 14  MET n 
1 15  LEU n 
1 16  ALA n 
1 17  LEU n 
1 18  THR n 
1 19  PHE n 
1 20  MET n 
1 21  PHE n 
1 22  MET n 
1 23  VAL n 
1 24  LEU n 
1 25  GLU n 
1 26  VAL n 
1 27  VAL n 
1 28  VAL n 
1 29  SER n 
1 30  ARG n 
1 31  VAL n 
1 32  THR n 
1 33  SER n 
1 34  SER n 
1 35  LEU n 
1 36  ALA n 
1 37  MET n 
1 38  LEU n 
1 39  SER n 
1 40  ASP n 
1 41  SER n 
1 42  PHE n 
1 43  HIS n 
1 44  MET n 
1 45  LEU n 
1 46  SER n 
1 47  ASP n 
1 48  VAL n 
1 49  LEU n 
1 50  ALA n 
1 51  LEU n 
1 52  VAL n 
1 53  VAL n 
1 54  ALA n 
1 55  LEU n 
1 56  VAL n 
1 57  ALA n 
1 58  GLU n 
1 59  ARG n 
1 60  PHE n 
1 61  ALA n 
1 62  ARG n 
1 63  ARG n 
1 64  THR n 
1 65  HIS n 
1 66  ALA n 
1 67  THR n 
1 68  GLN n 
1 69  LYS n 
1 70  ASN n 
1 71  THR n 
1 72  PHE n 
1 73  GLY n 
1 74  TRP n 
1 75  ILE n 
1 76  ARG n 
1 77  ALA n 
1 78  GLU n 
1 79  VAL n 
1 80  MET n 
1 81  GLY n 
1 82  ALA n 
1 83  LEU n 
1 84  VAL n 
1 85  ASN n 
1 86  ALA n 
1 87  ILE n 
1 88  PHE n 
1 89  LEU n 
1 90  THR n 
1 91  GLY n 
1 92  LEU n 
1 93  CYS n 
1 94  PHE n 
1 95  ALA n 
1 96  ILE n 
1 97  LEU n 
1 98  LEU n 
1 99  GLU n 
1 100 ALA n 
1 101 ILE n 
1 102 GLU n 
1 103 ARG n 
1 104 PHE n 
1 105 ILE n 
1 106 GLU n 
1 107 PRO n 
1 108 HIS n 
1 109 GLU n 
1 110 MET n 
1 111 GLN n 
1 112 GLN n 
1 113 PRO n 
1 114 LEU n 
1 115 VAL n 
1 116 VAL n 
1 117 LEU n 
1 118 GLY n 
1 119 VAL n 
1 120 GLY n 
1 121 VAL n 
1 122 ALA n 
1 123 GLY n 
1 124 LEU n 
1 125 LEU n 
1 126 VAL n 
1 127 ASN n 
1 128 VAL n 
1 129 LEU n 
1 130 GLY n 
1 131 LEU n 
1 132 CYS n 
1 133 LEU n 
1 134 PHE n 
1 135 HIS n 
1 136 HIS n 
1 137 HIS n 
1 138 SER n 
1 139 GLY n 
1 140 PHE n 
1 141 SER n 
1 142 GLN n 
1 143 ASP n 
1 144 SER n 
1 145 GLY n 
1 146 HIS n 
1 147 GLY n 
1 148 HIS n 
1 149 SER n 
1 150 HIS n 
1 151 GLY n 
1 152 GLY n 
1 153 HIS n 
1 154 GLY n 
1 155 HIS n 
1 156 GLY n 
1 157 HIS n 
1 158 GLY n 
1 159 LEU n 
1 160 PRO n 
1 161 LYS n 
1 162 GLY n 
1 163 PRO n 
1 164 ARG n 
1 165 VAL n 
1 166 LYS n 
1 167 SER n 
1 168 THR n 
1 169 ARG n 
1 170 PRO n 
1 171 GLY n 
1 172 SER n 
1 173 SER n 
1 174 ASP n 
1 175 ILE n 
1 176 ASN n 
1 177 VAL n 
1 178 ALA n 
1 179 PRO n 
1 180 GLY n 
1 181 GLU n 
1 182 GLN n 
1 183 GLY n 
1 184 PRO n 
1 185 ASP n 
1 186 GLN n 
1 187 GLU n 
1 188 GLU n 
1 189 THR n 
1 190 ASN n 
1 191 THR n 
1 192 LEU n 
1 193 VAL n 
1 194 ALA n 
1 195 ASN n 
1 196 THR n 
1 197 SER n 
1 198 ASN n 
1 199 SER n 
1 200 ASN n 
1 201 GLY n 
1 202 LEU n 
1 203 LYS n 
1 204 LEU n 
1 205 ASP n 
1 206 PRO n 
1 207 ALA n 
1 208 ASP n 
1 209 PRO n 
1 210 GLU n 
1 211 ASN n 
1 212 PRO n 
1 213 ARG n 
1 214 SER n 
1 215 GLY n 
1 216 ASP n 
1 217 THR n 
1 218 VAL n 
1 219 GLU n 
1 220 VAL n 
1 221 GLN n 
1 222 VAL n 
1 223 ASN n 
1 224 GLY n 
1 225 ASN n 
1 226 LEU n 
1 227 VAL n 
1 228 ARG n 
1 229 GLU n 
1 230 PRO n 
1 231 ASP n 
1 232 HIS n 
1 233 MET n 
1 234 GLU n 
1 235 LEU n 
1 236 GLU n 
1 237 GLU n 
1 238 ASP n 
1 239 ARG n 
1 240 ALA n 
1 241 GLY n 
1 242 GLN n 
1 243 LEU n 
1 244 ASN n 
1 245 MET n 
1 246 ARG n 
1 247 GLY n 
1 248 VAL n 
1 249 PHE n 
1 250 LEU n 
1 251 HIS n 
1 252 VAL n 
1 253 LEU n 
1 254 GLY n 
1 255 ASP n 
1 256 ALA n 
1 257 LEU n 
1 258 GLY n 
1 259 SER n 
1 260 VAL n 
1 261 ILE n 
1 262 VAL n 
1 263 VAL n 
1 264 VAL n 
1 265 ASN n 
1 266 ALA n 
1 267 LEU n 
1 268 VAL n 
1 269 PHE n 
1 270 TYR n 
1 271 PHE n 
1 272 SER n 
1 273 TRP n 
1 274 LYS n 
1 275 GLY n 
1 276 CYS n 
1 277 SER n 
1 278 GLU n 
1 279 GLY n 
1 280 ASP n 
1 281 PHE n 
1 282 CYS n 
1 283 VAL n 
1 284 ASN n 
1 285 PRO n 
1 286 CYS n 
1 287 PHE n 
1 288 PRO n 
1 289 ASP n 
1 290 PRO n 
1 291 CYS n 
1 292 LYS n 
1 293 ALA n 
1 294 PHE n 
1 295 VAL n 
1 296 GLU n 
1 297 ILE n 
1 298 ILE n 
1 299 ASN n 
1 300 SER n 
1 301 THR n 
1 302 HIS n 
1 303 ALA n 
1 304 SER n 
1 305 VAL n 
1 306 TYR n 
1 307 GLU n 
1 308 ALA n 
1 309 GLY n 
1 310 PRO n 
1 311 CYS n 
1 312 TRP n 
1 313 VAL n 
1 314 LEU n 
1 315 TYR n 
1 316 LEU n 
1 317 ASP n 
1 318 PRO n 
1 319 THR n 
1 320 LEU n 
1 321 CYS n 
1 322 VAL n 
1 323 VAL n 
1 324 MET n 
1 325 VAL n 
1 326 CYS n 
1 327 ILE n 
1 328 LEU n 
1 329 LEU n 
1 330 TYR n 
1 331 THR n 
1 332 THR n 
1 333 TYR n 
1 334 PRO n 
1 335 LEU n 
1 336 LEU n 
1 337 LYS n 
1 338 GLU n 
1 339 SER n 
1 340 ALA n 
1 341 LEU n 
1 342 ILE n 
1 343 LEU n 
1 344 LEU n 
1 345 GLN n 
1 346 THR n 
1 347 VAL n 
1 348 PRO n 
1 349 LYS n 
1 350 GLN n 
1 351 ILE n 
1 352 ASP n 
1 353 ILE n 
1 354 ARG n 
1 355 ASN n 
1 356 LEU n 
1 357 ILE n 
1 358 LYS n 
1 359 GLU n 
1 360 LEU n 
1 361 ARG n 
1 362 ASN n 
1 363 VAL n 
1 364 GLU n 
1 365 GLY n 
1 366 VAL n 
1 367 GLU n 
1 368 GLU n 
1 369 VAL n 
1 370 HIS n 
1 371 GLU n 
1 372 LEU n 
1 373 HIS n 
1 374 VAL n 
1 375 TRP n 
1 376 GLN n 
1 377 LEU n 
1 378 ALA n 
1 379 GLY n 
1 380 SER n 
1 381 ARG n 
1 382 ILE n 
1 383 ILE n 
1 384 ALA n 
1 385 THR n 
1 386 ALA n 
1 387 HIS n 
1 388 ILE n 
1 389 LYS n 
1 390 CYS n 
1 391 GLU n 
1 392 ASP n 
1 393 PRO n 
1 394 THR n 
1 395 SER n 
1 396 TYR n 
1 397 MET n 
1 398 GLU n 
1 399 VAL n 
1 400 ALA n 
1 401 LYS n 
1 402 THR n 
1 403 ILE n 
1 404 LYS n 
1 405 ASP n 
1 406 VAL n 
1 407 PHE n 
1 408 HIS n 
1 409 ASN n 
1 410 HIS n 
1 411 GLY n 
1 412 ILE n 
1 413 HIS n 
1 414 ALA n 
1 415 THR n 
1 416 THR n 
1 417 ILE n 
1 418 GLN n 
1 419 PRO n 
1 420 GLU n 
1 421 PHE n 
1 422 ALA n 
1 423 SER n 
1 424 VAL n 
1 425 GLY n 
1 426 SER n 
1 427 LYS n 
1 428 SER n 
1 429 SER n 
1 430 VAL n 
1 431 VAL n 
1 432 PRO n 
1 433 CYS n 
1 434 GLU n 
1 435 LEU n 
1 436 ALA n 
1 437 CYS n 
1 438 ARG n 
1 439 THR n 
1 440 GLN n 
1 441 CYS n 
1 442 ALA n 
1 443 LEU n 
1 444 LYS n 
1 445 GLN n 
1 446 CYS n 
1 447 CYS n 
1 448 GLY n 
1 449 THR n 
1 450 LEU n 
1 451 PRO n 
1 452 GLN n 
1 453 ALA n 
1 454 PRO n 
1 455 SER n 
1 456 GLY n 
1 457 LYS n 
1 458 ASP n 
1 459 ALA n 
1 460 GLU n 
1 461 LYS n 
1 462 THR n 
1 463 PRO n 
1 464 ALA n 
1 465 VAL n 
1 466 SER n 
1 467 ILE n 
1 468 SER n 
1 469 CYS n 
1 470 LEU n 
1 471 GLU n 
1 472 LEU n 
1 473 SER n 
1 474 ASN n 
1 475 ASN n 
1 476 LEU n 
1 477 GLU n 
1 478 LYS n 
1 479 LYS n 
1 480 PRO n 
1 481 ARG n 
1 482 ARG n 
1 483 THR n 
1 484 LYS n 
1 485 ALA n 
1 486 GLU n 
1 487 ASN n 
1 488 ILE n 
1 489 PRO n 
1 490 ALA n 
1 491 VAL n 
1 492 VAL n 
1 493 ILE n 
1 494 GLU n 
1 495 ILE n 
1 496 LYS n 
1 497 ASN n 
1 498 MET n 
1 499 PRO n 
1 500 ASN n 
1 501 LYS n 
1 502 GLN n 
1 503 PRO n 
1 504 GLU n 
1 505 SER n 
1 506 SER n 
1 507 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   507 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SLC30A1, ZNT1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
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 
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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   ?   ?   ?   A . n 
A 1 3   CYS 3   3   ?   ?   ?   A . n 
A 1 4   TRP 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   ?   ?   ?   A . n 
A 1 6   ARG 6   6   ?   ?   ?   A . n 
A 1 7   ASN 7   7   7   ASN ASN A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  CYS 13  13  13  CYS CYS A . n 
A 1 14  MET 14  14  14  MET MET A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  PHE 19  19  19  PHE PHE A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  MET 22  22  22  MET MET A . n 
A 1 23  VAL 23  23  23  VAL VAL A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  MET 37  37  37  MET MET A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  MET 44  44  44  MET MET A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  HIS 65  65  65  HIS HIS A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  GLN 68  68  68  GLN GLN A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  PHE 72  72  72  PHE PHE A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  TRP 74  74  74  TRP TRP A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  MET 80  80  80  MET MET A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  GLY 91  91  91  GLY GLY A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  CYS 93  93  93  CYS CYS A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 PHE 104 104 104 PHE PHE A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 HIS 108 108 108 HIS HIS A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 MET 110 110 110 MET MET A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 GLN 112 112 112 GLN ALA A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 CYS 132 132 132 CYS CYS A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 HIS 135 135 ?   ?   ?   A . n 
A 1 136 HIS 136 136 ?   ?   ?   A . n 
A 1 137 HIS 137 137 ?   ?   ?   A . n 
A 1 138 SER 138 138 ?   ?   ?   A . n 
A 1 139 GLY 139 139 ?   ?   ?   A . n 
A 1 140 PHE 140 140 ?   ?   ?   A . n 
A 1 141 SER 141 141 ?   ?   ?   A . n 
A 1 142 GLN 142 142 ?   ?   ?   A . n 
A 1 143 ASP 143 143 ?   ?   ?   A . n 
A 1 144 SER 144 144 ?   ?   ?   A . n 
A 1 145 GLY 145 145 ?   ?   ?   A . n 
A 1 146 HIS 146 146 ?   ?   ?   A . n 
A 1 147 GLY 147 147 ?   ?   ?   A . n 
A 1 148 HIS 148 148 ?   ?   ?   A . n 
A 1 149 SER 149 149 ?   ?   ?   A . n 
A 1 150 HIS 150 150 ?   ?   ?   A . n 
A 1 151 GLY 151 151 ?   ?   ?   A . n 
A 1 152 GLY 152 152 ?   ?   ?   A . n 
A 1 153 HIS 153 153 ?   ?   ?   A . n 
A 1 154 GLY 154 154 ?   ?   ?   A . n 
A 1 155 HIS 155 155 ?   ?   ?   A . n 
A 1 156 GLY 156 156 ?   ?   ?   A . n 
A 1 157 HIS 157 157 ?   ?   ?   A . n 
A 1 158 GLY 158 158 ?   ?   ?   A . n 
A 1 159 LEU 159 159 ?   ?   ?   A . n 
A 1 160 PRO 160 160 ?   ?   ?   A . n 
A 1 161 LYS 161 161 ?   ?   ?   A . n 
A 1 162 GLY 162 162 ?   ?   ?   A . n 
A 1 163 PRO 163 163 ?   ?   ?   A . n 
A 1 164 ARG 164 164 ?   ?   ?   A . n 
A 1 165 VAL 165 165 ?   ?   ?   A . n 
A 1 166 LYS 166 166 ?   ?   ?   A . n 
A 1 167 SER 167 167 ?   ?   ?   A . n 
A 1 168 THR 168 168 ?   ?   ?   A . n 
A 1 169 ARG 169 169 ?   ?   ?   A . n 
A 1 170 PRO 170 170 ?   ?   ?   A . n 
A 1 171 GLY 171 171 ?   ?   ?   A . n 
A 1 172 SER 172 172 ?   ?   ?   A . n 
A 1 173 SER 173 173 ?   ?   ?   A . n 
A 1 174 ASP 174 174 ?   ?   ?   A . n 
A 1 175 ILE 175 175 ?   ?   ?   A . n 
A 1 176 ASN 176 176 ?   ?   ?   A . n 
A 1 177 VAL 177 177 ?   ?   ?   A . n 
A 1 178 ALA 178 178 ?   ?   ?   A . n 
A 1 179 PRO 179 179 ?   ?   ?   A . n 
A 1 180 GLY 180 180 ?   ?   ?   A . n 
A 1 181 GLU 181 181 ?   ?   ?   A . n 
A 1 182 GLN 182 182 ?   ?   ?   A . n 
A 1 183 GLY 183 183 ?   ?   ?   A . n 
A 1 184 PRO 184 184 ?   ?   ?   A . n 
A 1 185 ASP 185 185 ?   ?   ?   A . n 
A 1 186 GLN 186 186 ?   ?   ?   A . n 
A 1 187 GLU 187 187 ?   ?   ?   A . n 
A 1 188 GLU 188 188 ?   ?   ?   A . n 
A 1 189 THR 189 189 ?   ?   ?   A . n 
A 1 190 ASN 190 190 ?   ?   ?   A . n 
A 1 191 THR 191 191 ?   ?   ?   A . n 
A 1 192 LEU 192 192 ?   ?   ?   A . n 
A 1 193 VAL 193 193 ?   ?   ?   A . n 
A 1 194 ALA 194 194 ?   ?   ?   A . n 
A 1 195 ASN 195 195 ?   ?   ?   A . n 
A 1 196 THR 196 196 ?   ?   ?   A . n 
A 1 197 SER 197 197 ?   ?   ?   A . n 
A 1 198 ASN 198 198 ?   ?   ?   A . n 
A 1 199 SER 199 199 ?   ?   ?   A . n 
A 1 200 ASN 200 200 ?   ?   ?   A . n 
A 1 201 GLY 201 201 ?   ?   ?   A . n 
A 1 202 LEU 202 202 ?   ?   ?   A . n 
A 1 203 LYS 203 203 ?   ?   ?   A . n 
A 1 204 LEU 204 204 ?   ?   ?   A . n 
A 1 205 ASP 205 205 ?   ?   ?   A . n 
A 1 206 PRO 206 206 ?   ?   ?   A . n 
A 1 207 ALA 207 207 ?   ?   ?   A . n 
A 1 208 ASP 208 208 ?   ?   ?   A . n 
A 1 209 PRO 209 209 ?   ?   ?   A . n 
A 1 210 GLU 210 210 ?   ?   ?   A . n 
A 1 211 ASN 211 211 ?   ?   ?   A . n 
A 1 212 PRO 212 212 ?   ?   ?   A . n 
A 1 213 ARG 213 213 ?   ?   ?   A . n 
A 1 214 SER 214 214 ?   ?   ?   A . n 
A 1 215 GLY 215 215 ?   ?   ?   A . n 
A 1 216 ASP 216 216 ?   ?   ?   A . n 
A 1 217 THR 217 217 ?   ?   ?   A . n 
A 1 218 VAL 218 218 ?   ?   ?   A . n 
A 1 219 GLU 219 219 ?   ?   ?   A . n 
A 1 220 VAL 220 220 ?   ?   ?   A . n 
A 1 221 GLN 221 221 ?   ?   ?   A . n 
A 1 222 VAL 222 222 ?   ?   ?   A . n 
A 1 223 ASN 223 223 ?   ?   ?   A . n 
A 1 224 GLY 224 224 ?   ?   ?   A . n 
A 1 225 ASN 225 225 ?   ?   ?   A . n 
A 1 226 LEU 226 226 ?   ?   ?   A . n 
A 1 227 VAL 227 227 ?   ?   ?   A . n 
A 1 228 ARG 228 228 ?   ?   ?   A . n 
A 1 229 GLU 229 229 ?   ?   ?   A . n 
A 1 230 PRO 230 230 ?   ?   ?   A . n 
A 1 231 ASP 231 231 ?   ?   ?   A . n 
A 1 232 HIS 232 232 ?   ?   ?   A . n 
A 1 233 MET 233 233 ?   ?   ?   A . n 
A 1 234 GLU 234 234 ?   ?   ?   A . n 
A 1 235 LEU 235 235 ?   ?   ?   A . n 
A 1 236 GLU 236 236 ?   ?   ?   A . n 
A 1 237 GLU 237 237 ?   ?   ?   A . n 
A 1 238 ASP 238 238 ?   ?   ?   A . n 
A 1 239 ARG 239 239 ?   ?   ?   A . n 
A 1 240 ALA 240 240 ?   ?   ?   A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 GLN 242 242 242 GLN GLN A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 MET 245 245 245 MET MET A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 VAL 248 248 248 VAL VAL A . n 
A 1 249 PHE 249 249 249 PHE PHE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 HIS 251 251 251 HIS HIS A . n 
A 1 252 VAL 252 252 252 VAL VAL A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 ASP 255 255 255 ASP ASP A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 VAL 260 260 260 VAL VAL A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 ASN 265 265 265 ASN ASN A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 PHE 269 269 269 PHE PHE A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 TRP 273 273 273 TRP TRP A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 CYS 276 276 276 CYS CYS A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 GLY 279 279 279 GLY GLY A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 PHE 281 281 281 PHE PHE A . n 
A 1 282 CYS 282 282 282 CYS CYS A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 CYS 286 286 286 CYS CYS A . n 
A 1 287 PHE 287 287 287 PHE PHE A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 PRO 290 290 290 PRO PRO A . n 
A 1 291 CYS 291 291 291 CYS CYS A . n 
A 1 292 LYS 292 292 292 LYS LYS A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 ILE 298 298 298 ILE ILE A . n 
A 1 299 ASN 299 299 299 ASN ASN A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 THR 301 301 301 THR THR A . n 
A 1 302 HIS 302 302 302 HIS HIS A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 CYS 311 311 311 CYS CYS A . n 
A 1 312 TRP 312 312 312 TRP TRP A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 LEU 314 314 314 LEU LEU A . n 
A 1 315 TYR 315 315 315 TYR TYR A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 ASP 317 317 317 ASP ASP A . n 
A 1 318 PRO 318 318 318 PRO PRO A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 CYS 321 321 321 CYS CYS A . n 
A 1 322 VAL 322 322 322 VAL VAL A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 MET 324 324 324 MET MET A . n 
A 1 325 VAL 325 325 325 VAL VAL A . n 
A 1 326 CYS 326 326 326 CYS CYS A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 THR 331 331 331 THR THR A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 TYR 333 333 333 TYR TYR A . n 
A 1 334 PRO 334 334 334 PRO PRO A . n 
A 1 335 LEU 335 335 335 LEU LEU A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 LYS 337 337 337 LYS LYS A . n 
A 1 338 GLU 338 338 338 GLU GLU A . n 
A 1 339 SER 339 339 339 SER SER A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 ILE 342 342 342 ILE ILE A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 LEU 344 344 344 LEU LEU A . n 
A 1 345 GLN 345 345 345 GLN GLN A . n 
A 1 346 THR 346 346 346 THR THR A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 GLN 350 350 350 GLN GLN A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 ILE 353 353 353 ILE ILE A . n 
A 1 354 ARG 354 354 354 ARG ARG A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 ILE 357 357 357 ILE ILE A . n 
A 1 358 LYS 358 358 358 LYS LYS A . n 
A 1 359 GLU 359 359 359 GLU GLU A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 ARG 361 361 361 ARG ARG A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 GLY 365 365 365 GLY GLY A . n 
A 1 366 VAL 366 366 366 VAL VAL A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 GLU 368 368 368 GLU GLU A . n 
A 1 369 VAL 369 369 369 VAL VAL A . n 
A 1 370 HIS 370 370 370 HIS HIS A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 HIS 373 373 373 HIS HIS A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 TRP 375 375 375 TRP TRP A . n 
A 1 376 GLN 376 376 376 GLN GLN A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 SER 380 380 380 SER SER A . n 
A 1 381 ARG 381 381 381 ARG ARG A . n 
A 1 382 ILE 382 382 382 ILE ILE A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 ALA 384 384 384 ALA ALA A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 ALA 386 386 386 ALA ALA A . n 
A 1 387 HIS 387 387 387 HIS HIS A . n 
A 1 388 ILE 388 388 388 ILE ILE A . n 
A 1 389 LYS 389 389 389 LYS LYS A . n 
A 1 390 CYS 390 390 390 CYS CYS A . n 
A 1 391 GLU 391 391 391 GLU GLU A . n 
A 1 392 ASP 392 392 392 ASP ASP A . n 
A 1 393 PRO 393 393 393 PRO PRO A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 SER 395 395 395 SER SER A . n 
A 1 396 TYR 396 396 396 TYR TYR A . n 
A 1 397 MET 397 397 397 MET MET A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 LYS 401 401 401 LYS LYS A . n 
A 1 402 THR 402 402 402 THR THR A . n 
A 1 403 ILE 403 403 403 ILE ILE A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 ASP 405 405 405 ASP ASP A . n 
A 1 406 VAL 406 406 406 VAL VAL A . n 
A 1 407 PHE 407 407 407 PHE PHE A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 ASN 409 409 409 ASN ASN A . n 
A 1 410 HIS 410 410 410 HIS HIS A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ILE 412 412 412 ILE ILE A . n 
A 1 413 HIS 413 413 413 HIS HIS A . n 
A 1 414 ALA 414 414 414 ALA ALA A . n 
A 1 415 THR 415 415 415 THR THR A . n 
A 1 416 THR 416 416 416 THR THR A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLN 418 418 418 GLN GLN A . n 
A 1 419 PRO 419 419 419 PRO PRO A . n 
A 1 420 GLU 420 420 420 GLU GLU A . n 
A 1 421 PHE 421 421 421 PHE PHE A . n 
A 1 422 ALA 422 422 422 ALA ALA A . n 
A 1 423 SER 423 423 423 SER SER A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 SER 426 426 426 SER SER A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 SER 428 428 428 SER SER A . n 
A 1 429 SER 429 429 429 SER SER A . n 
A 1 430 VAL 430 430 430 VAL VAL A . n 
A 1 431 VAL 431 431 431 VAL VAL A . n 
A 1 432 PRO 432 432 432 PRO PRO A . n 
A 1 433 CYS 433 433 433 CYS CYS A . n 
A 1 434 GLU 434 434 434 GLU GLU A . n 
A 1 435 LEU 435 435 435 LEU LEU A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 CYS 437 437 437 CYS CYS A . n 
A 1 438 ARG 438 438 438 ARG ARG A . n 
A 1 439 THR 439 439 439 THR THR A . n 
A 1 440 GLN 440 440 440 GLN GLN A . n 
A 1 441 CYS 441 441 441 CYS CYS A . n 
A 1 442 ALA 442 442 ?   ?   ?   A . n 
A 1 443 LEU 443 443 ?   ?   ?   A . n 
A 1 444 LYS 444 444 ?   ?   ?   A . n 
A 1 445 GLN 445 445 ?   ?   ?   A . n 
A 1 446 CYS 446 446 ?   ?   ?   A . n 
A 1 447 CYS 447 447 ?   ?   ?   A . n 
A 1 448 GLY 448 448 ?   ?   ?   A . n 
A 1 449 THR 449 449 ?   ?   ?   A . n 
A 1 450 LEU 450 450 ?   ?   ?   A . n 
A 1 451 PRO 451 451 ?   ?   ?   A . n 
A 1 452 GLN 452 452 ?   ?   ?   A . n 
A 1 453 ALA 453 453 ?   ?   ?   A . n 
A 1 454 PRO 454 454 ?   ?   ?   A . n 
A 1 455 SER 455 455 ?   ?   ?   A . n 
A 1 456 GLY 456 456 ?   ?   ?   A . n 
A 1 457 LYS 457 457 ?   ?   ?   A . n 
A 1 458 ASP 458 458 ?   ?   ?   A . n 
A 1 459 ALA 459 459 ?   ?   ?   A . n 
A 1 460 GLU 460 460 ?   ?   ?   A . n 
A 1 461 LYS 461 461 ?   ?   ?   A . n 
A 1 462 THR 462 462 ?   ?   ?   A . n 
A 1 463 PRO 463 463 ?   ?   ?   A . n 
A 1 464 ALA 464 464 ?   ?   ?   A . n 
A 1 465 VAL 465 465 ?   ?   ?   A . n 
A 1 466 SER 466 466 ?   ?   ?   A . n 
A 1 467 ILE 467 467 ?   ?   ?   A . n 
A 1 468 SER 468 468 ?   ?   ?   A . n 
A 1 469 CYS 469 469 ?   ?   ?   A . n 
A 1 470 LEU 470 470 ?   ?   ?   A . n 
A 1 471 GLU 471 471 ?   ?   ?   A . n 
A 1 472 LEU 472 472 ?   ?   ?   A . n 
A 1 473 SER 473 473 ?   ?   ?   A . n 
A 1 474 ASN 474 474 ?   ?   ?   A . n 
A 1 475 ASN 475 475 ?   ?   ?   A . n 
A 1 476 LEU 476 476 ?   ?   ?   A . n 
A 1 477 GLU 477 477 ?   ?   ?   A . n 
A 1 478 LYS 478 478 ?   ?   ?   A . n 
A 1 479 LYS 479 479 ?   ?   ?   A . n 
A 1 480 PRO 480 480 ?   ?   ?   A . n 
A 1 481 ARG 481 481 ?   ?   ?   A . n 
A 1 482 ARG 482 482 ?   ?   ?   A . n 
A 1 483 THR 483 483 ?   ?   ?   A . n 
A 1 484 LYS 484 484 ?   ?   ?   A . n 
A 1 485 ALA 485 485 ?   ?   ?   A . n 
A 1 486 GLU 486 486 ?   ?   ?   A . n 
A 1 487 ASN 487 487 ?   ?   ?   A . n 
A 1 488 ILE 488 488 ?   ?   ?   A . n 
A 1 489 PRO 489 489 ?   ?   ?   A . n 
A 1 490 ALA 490 490 ?   ?   ?   A . n 
A 1 491 VAL 491 491 ?   ?   ?   A . n 
A 1 492 VAL 492 492 ?   ?   ?   A . n 
A 1 493 ILE 493 493 ?   ?   ?   A . n 
A 1 494 GLU 494 494 ?   ?   ?   A . n 
A 1 495 ILE 495 495 ?   ?   ?   A . n 
A 1 496 LYS 496 496 ?   ?   ?   A . n 
A 1 497 ASN 497 497 ?   ?   ?   A . n 
A 1 498 MET 498 498 ?   ?   ?   A . n 
A 1 499 PRO 499 499 ?   ?   ?   A . n 
A 1 500 ASN 500 500 ?   ?   ?   A . n 
A 1 501 LYS 501 501 ?   ?   ?   A . n 
A 1 502 GLN 502 502 ?   ?   ?   A . n 
A 1 503 PRO 503 503 ?   ?   ?   A . n 
A 1 504 GLU 504 504 ?   ?   ?   A . n 
A 1 505 SER 505 505 ?   ?   ?   A . n 
A 1 506 SER 506 506 ?   ?   ?   A . n 
A 1 507 LEU 507 507 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLY 2   2   ?   ?   ?   B . n 
B 1 3   CYS 3   3   ?   ?   ?   B . n 
B 1 4   TRP 4   4   ?   ?   ?   B . n 
B 1 5   GLY 5   5   ?   ?   ?   B . n 
B 1 6   ARG 6   6   ?   ?   ?   B . n 
B 1 7   ASN 7   7   7   ASN ASN B . n 
B 1 8   ARG 8   8   8   ARG ARG B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  CYS 13  13  13  CYS CYS B . n 
B 1 14  MET 14  14  14  MET MET B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  ALA 16  16  16  ALA ALA B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  THR 18  18  18  THR THR B . n 
B 1 19  PHE 19  19  19  PHE PHE B . n 
B 1 20  MET 20  20  20  MET MET B . n 
B 1 21  PHE 21  21  21  PHE PHE B . n 
B 1 22  MET 22  22  22  MET MET B . n 
B 1 23  VAL 23  23  23  VAL VAL B . n 
B 1 24  LEU 24  24  24  LEU LEU B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  VAL 26  26  26  VAL VAL B . n 
B 1 27  VAL 27  27  27  VAL VAL B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  ARG 30  30  30  ARG ARG B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  MET 37  37  37  MET MET B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  SER 39  39  39  SER SER B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  SER 41  41  41  SER SER B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  MET 44  44  44  MET MET B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  ARG 59  59  59  ARG ARG B . n 
B 1 60  PHE 60  60  60  PHE PHE B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  ARG 62  62  62  ARG ARG B . n 
B 1 63  ARG 63  63  63  ARG ARG B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  HIS 65  65  65  HIS HIS B . n 
B 1 66  ALA 66  66  66  ALA ALA B . n 
B 1 67  THR 67  67  67  THR THR B . n 
B 1 68  GLN 68  68  68  GLN GLN B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  PHE 72  72  72  PHE PHE B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  TRP 74  74  74  TRP TRP B . n 
B 1 75  ILE 75  75  75  ILE ILE B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  MET 80  80  80  MET MET B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  ASN 85  85  85  ASN ASN B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  PHE 88  88  88  PHE PHE B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  GLY 91  91  91  GLY GLY B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  CYS 93  93  93  CYS CYS B . n 
B 1 94  PHE 94  94  94  PHE PHE B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  GLU 99  99  99  GLU GLU B . n 
B 1 100 ALA 100 100 100 ALA ALA B . n 
B 1 101 ILE 101 101 101 ILE ILE B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 PHE 104 104 104 PHE PHE B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 PRO 107 107 107 PRO PRO B . n 
B 1 108 HIS 108 108 108 HIS HIS B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 MET 110 110 110 MET MET B . n 
B 1 111 GLN 111 111 111 GLN GLN B . n 
B 1 112 GLN 112 112 112 GLN ALA B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 VAL 115 115 115 VAL VAL B . n 
B 1 116 VAL 116 116 116 VAL VAL B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 ALA 122 122 122 ALA ALA B . n 
B 1 123 GLY 123 123 123 GLY GLY B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 ASN 127 127 127 ASN ASN B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 LEU 131 131 131 LEU LEU B . n 
B 1 132 CYS 132 132 132 CYS CYS B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 HIS 135 135 ?   ?   ?   B . n 
B 1 136 HIS 136 136 ?   ?   ?   B . n 
B 1 137 HIS 137 137 ?   ?   ?   B . n 
B 1 138 SER 138 138 ?   ?   ?   B . n 
B 1 139 GLY 139 139 ?   ?   ?   B . n 
B 1 140 PHE 140 140 ?   ?   ?   B . n 
B 1 141 SER 141 141 ?   ?   ?   B . n 
B 1 142 GLN 142 142 ?   ?   ?   B . n 
B 1 143 ASP 143 143 ?   ?   ?   B . n 
B 1 144 SER 144 144 ?   ?   ?   B . n 
B 1 145 GLY 145 145 ?   ?   ?   B . n 
B 1 146 HIS 146 146 ?   ?   ?   B . n 
B 1 147 GLY 147 147 ?   ?   ?   B . n 
B 1 148 HIS 148 148 ?   ?   ?   B . n 
B 1 149 SER 149 149 ?   ?   ?   B . n 
B 1 150 HIS 150 150 ?   ?   ?   B . n 
B 1 151 GLY 151 151 ?   ?   ?   B . n 
B 1 152 GLY 152 152 ?   ?   ?   B . n 
B 1 153 HIS 153 153 ?   ?   ?   B . n 
B 1 154 GLY 154 154 ?   ?   ?   B . n 
B 1 155 HIS 155 155 ?   ?   ?   B . n 
B 1 156 GLY 156 156 ?   ?   ?   B . n 
B 1 157 HIS 157 157 ?   ?   ?   B . n 
B 1 158 GLY 158 158 ?   ?   ?   B . n 
B 1 159 LEU 159 159 ?   ?   ?   B . n 
B 1 160 PRO 160 160 ?   ?   ?   B . n 
B 1 161 LYS 161 161 ?   ?   ?   B . n 
B 1 162 GLY 162 162 ?   ?   ?   B . n 
B 1 163 PRO 163 163 ?   ?   ?   B . n 
B 1 164 ARG 164 164 ?   ?   ?   B . n 
B 1 165 VAL 165 165 ?   ?   ?   B . n 
B 1 166 LYS 166 166 ?   ?   ?   B . n 
B 1 167 SER 167 167 ?   ?   ?   B . n 
B 1 168 THR 168 168 ?   ?   ?   B . n 
B 1 169 ARG 169 169 ?   ?   ?   B . n 
B 1 170 PRO 170 170 ?   ?   ?   B . n 
B 1 171 GLY 171 171 ?   ?   ?   B . n 
B 1 172 SER 172 172 ?   ?   ?   B . n 
B 1 173 SER 173 173 ?   ?   ?   B . n 
B 1 174 ASP 174 174 ?   ?   ?   B . n 
B 1 175 ILE 175 175 ?   ?   ?   B . n 
B 1 176 ASN 176 176 ?   ?   ?   B . n 
B 1 177 VAL 177 177 ?   ?   ?   B . n 
B 1 178 ALA 178 178 ?   ?   ?   B . n 
B 1 179 PRO 179 179 ?   ?   ?   B . n 
B 1 180 GLY 180 180 ?   ?   ?   B . n 
B 1 181 GLU 181 181 ?   ?   ?   B . n 
B 1 182 GLN 182 182 ?   ?   ?   B . n 
B 1 183 GLY 183 183 ?   ?   ?   B . n 
B 1 184 PRO 184 184 ?   ?   ?   B . n 
B 1 185 ASP 185 185 ?   ?   ?   B . n 
B 1 186 GLN 186 186 ?   ?   ?   B . n 
B 1 187 GLU 187 187 ?   ?   ?   B . n 
B 1 188 GLU 188 188 ?   ?   ?   B . n 
B 1 189 THR 189 189 ?   ?   ?   B . n 
B 1 190 ASN 190 190 ?   ?   ?   B . n 
B 1 191 THR 191 191 ?   ?   ?   B . n 
B 1 192 LEU 192 192 ?   ?   ?   B . n 
B 1 193 VAL 193 193 ?   ?   ?   B . n 
B 1 194 ALA 194 194 ?   ?   ?   B . n 
B 1 195 ASN 195 195 ?   ?   ?   B . n 
B 1 196 THR 196 196 ?   ?   ?   B . n 
B 1 197 SER 197 197 ?   ?   ?   B . n 
B 1 198 ASN 198 198 ?   ?   ?   B . n 
B 1 199 SER 199 199 ?   ?   ?   B . n 
B 1 200 ASN 200 200 ?   ?   ?   B . n 
B 1 201 GLY 201 201 ?   ?   ?   B . n 
B 1 202 LEU 202 202 ?   ?   ?   B . n 
B 1 203 LYS 203 203 ?   ?   ?   B . n 
B 1 204 LEU 204 204 ?   ?   ?   B . n 
B 1 205 ASP 205 205 ?   ?   ?   B . n 
B 1 206 PRO 206 206 ?   ?   ?   B . n 
B 1 207 ALA 207 207 ?   ?   ?   B . n 
B 1 208 ASP 208 208 ?   ?   ?   B . n 
B 1 209 PRO 209 209 ?   ?   ?   B . n 
B 1 210 GLU 210 210 ?   ?   ?   B . n 
B 1 211 ASN 211 211 ?   ?   ?   B . n 
B 1 212 PRO 212 212 ?   ?   ?   B . n 
B 1 213 ARG 213 213 ?   ?   ?   B . n 
B 1 214 SER 214 214 ?   ?   ?   B . n 
B 1 215 GLY 215 215 ?   ?   ?   B . n 
B 1 216 ASP 216 216 ?   ?   ?   B . n 
B 1 217 THR 217 217 ?   ?   ?   B . n 
B 1 218 VAL 218 218 ?   ?   ?   B . n 
B 1 219 GLU 219 219 ?   ?   ?   B . n 
B 1 220 VAL 220 220 ?   ?   ?   B . n 
B 1 221 GLN 221 221 ?   ?   ?   B . n 
B 1 222 VAL 222 222 ?   ?   ?   B . n 
B 1 223 ASN 223 223 ?   ?   ?   B . n 
B 1 224 GLY 224 224 ?   ?   ?   B . n 
B 1 225 ASN 225 225 ?   ?   ?   B . n 
B 1 226 LEU 226 226 ?   ?   ?   B . n 
B 1 227 VAL 227 227 ?   ?   ?   B . n 
B 1 228 ARG 228 228 ?   ?   ?   B . n 
B 1 229 GLU 229 229 ?   ?   ?   B . n 
B 1 230 PRO 230 230 ?   ?   ?   B . n 
B 1 231 ASP 231 231 ?   ?   ?   B . n 
B 1 232 HIS 232 232 ?   ?   ?   B . n 
B 1 233 MET 233 233 ?   ?   ?   B . n 
B 1 234 GLU 234 234 ?   ?   ?   B . n 
B 1 235 LEU 235 235 ?   ?   ?   B . n 
B 1 236 GLU 236 236 ?   ?   ?   B . n 
B 1 237 GLU 237 237 ?   ?   ?   B . n 
B 1 238 ASP 238 238 ?   ?   ?   B . n 
B 1 239 ARG 239 239 ?   ?   ?   B . n 
B 1 240 ALA 240 240 ?   ?   ?   B . n 
B 1 241 GLY 241 241 241 GLY GLY B . n 
B 1 242 GLN 242 242 242 GLN GLN B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 MET 245 245 245 MET MET B . n 
B 1 246 ARG 246 246 246 ARG ARG B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 VAL 248 248 248 VAL VAL B . n 
B 1 249 PHE 249 249 249 PHE PHE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 HIS 251 251 251 HIS HIS B . n 
B 1 252 VAL 252 252 252 VAL VAL B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 GLY 254 254 254 GLY GLY B . n 
B 1 255 ASP 255 255 255 ASP ASP B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 SER 259 259 259 SER SER B . n 
B 1 260 VAL 260 260 260 VAL VAL B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 VAL 262 262 262 VAL VAL B . n 
B 1 263 VAL 263 263 263 VAL VAL B . n 
B 1 264 VAL 264 264 264 VAL VAL B . n 
B 1 265 ASN 265 265 265 ASN ASN B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 PHE 269 269 269 PHE PHE B . n 
B 1 270 TYR 270 270 270 TYR TYR B . n 
B 1 271 PHE 271 271 271 PHE PHE B . n 
B 1 272 SER 272 272 272 SER SER B . n 
B 1 273 TRP 273 273 273 TRP TRP B . n 
B 1 274 LYS 274 274 274 LYS LYS B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 CYS 276 276 276 CYS CYS B . n 
B 1 277 SER 277 277 277 SER SER B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 GLY 279 279 279 GLY GLY B . n 
B 1 280 ASP 280 280 280 ASP ASP B . n 
B 1 281 PHE 281 281 281 PHE PHE B . n 
B 1 282 CYS 282 282 282 CYS CYS B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 ASN 284 284 284 ASN ASN B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 CYS 286 286 286 CYS CYS B . n 
B 1 287 PHE 287 287 287 PHE PHE B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 PRO 290 290 290 PRO PRO B . n 
B 1 291 CYS 291 291 291 CYS CYS B . n 
B 1 292 LYS 292 292 292 LYS LYS B . n 
B 1 293 ALA 293 293 293 ALA ALA B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 VAL 295 295 295 VAL VAL B . n 
B 1 296 GLU 296 296 296 GLU GLU B . n 
B 1 297 ILE 297 297 297 ILE ILE B . n 
B 1 298 ILE 298 298 298 ILE ILE B . n 
B 1 299 ASN 299 299 299 ASN ASN B . n 
B 1 300 SER 300 300 300 SER SER B . n 
B 1 301 THR 301 301 301 THR THR B . n 
B 1 302 HIS 302 302 302 HIS HIS B . n 
B 1 303 ALA 303 303 303 ALA ALA B . n 
B 1 304 SER 304 304 304 SER SER B . n 
B 1 305 VAL 305 305 305 VAL VAL B . n 
B 1 306 TYR 306 306 306 TYR TYR B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 GLY 309 309 309 GLY GLY B . n 
B 1 310 PRO 310 310 310 PRO PRO B . n 
B 1 311 CYS 311 311 311 CYS CYS B . n 
B 1 312 TRP 312 312 312 TRP TRP B . n 
B 1 313 VAL 313 313 313 VAL VAL B . n 
B 1 314 LEU 314 314 314 LEU LEU B . n 
B 1 315 TYR 315 315 315 TYR TYR B . n 
B 1 316 LEU 316 316 316 LEU LEU B . n 
B 1 317 ASP 317 317 317 ASP ASP B . n 
B 1 318 PRO 318 318 318 PRO PRO B . n 
B 1 319 THR 319 319 319 THR THR B . n 
B 1 320 LEU 320 320 320 LEU LEU B . n 
B 1 321 CYS 321 321 321 CYS CYS B . n 
B 1 322 VAL 322 322 322 VAL VAL B . n 
B 1 323 VAL 323 323 323 VAL VAL B . n 
B 1 324 MET 324 324 324 MET MET B . n 
B 1 325 VAL 325 325 325 VAL VAL B . n 
B 1 326 CYS 326 326 326 CYS CYS B . n 
B 1 327 ILE 327 327 327 ILE ILE B . n 
B 1 328 LEU 328 328 328 LEU LEU B . n 
B 1 329 LEU 329 329 329 LEU LEU B . n 
B 1 330 TYR 330 330 330 TYR TYR B . n 
B 1 331 THR 331 331 331 THR THR B . n 
B 1 332 THR 332 332 332 THR THR B . n 
B 1 333 TYR 333 333 333 TYR TYR B . n 
B 1 334 PRO 334 334 334 PRO PRO B . n 
B 1 335 LEU 335 335 335 LEU LEU B . n 
B 1 336 LEU 336 336 336 LEU LEU B . n 
B 1 337 LYS 337 337 337 LYS LYS B . n 
B 1 338 GLU 338 338 338 GLU GLU B . n 
B 1 339 SER 339 339 339 SER SER B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 LEU 341 341 341 LEU LEU B . n 
B 1 342 ILE 342 342 342 ILE ILE B . n 
B 1 343 LEU 343 343 343 LEU LEU B . n 
B 1 344 LEU 344 344 344 LEU LEU B . n 
B 1 345 GLN 345 345 345 GLN GLN B . n 
B 1 346 THR 346 346 346 THR THR B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 PRO 348 348 348 PRO PRO B . n 
B 1 349 LYS 349 349 349 LYS LYS B . n 
B 1 350 GLN 350 350 350 GLN GLN B . n 
B 1 351 ILE 351 351 351 ILE ILE B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 ILE 353 353 353 ILE ILE B . n 
B 1 354 ARG 354 354 354 ARG ARG B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 ILE 357 357 357 ILE ILE B . n 
B 1 358 LYS 358 358 358 LYS LYS B . n 
B 1 359 GLU 359 359 359 GLU GLU B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 ARG 361 361 361 ARG ARG B . n 
B 1 362 ASN 362 362 362 ASN ASN B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 GLU 364 364 364 GLU GLU B . n 
B 1 365 GLY 365 365 365 GLY GLY B . n 
B 1 366 VAL 366 366 366 VAL VAL B . n 
B 1 367 GLU 367 367 367 GLU GLU B . n 
B 1 368 GLU 368 368 368 GLU GLU B . n 
B 1 369 VAL 369 369 369 VAL VAL B . n 
B 1 370 HIS 370 370 370 HIS HIS B . n 
B 1 371 GLU 371 371 371 GLU GLU B . n 
B 1 372 LEU 372 372 372 LEU LEU B . n 
B 1 373 HIS 373 373 373 HIS HIS B . n 
B 1 374 VAL 374 374 374 VAL VAL B . n 
B 1 375 TRP 375 375 375 TRP TRP B . n 
B 1 376 GLN 376 376 376 GLN GLN B . n 
B 1 377 LEU 377 377 377 LEU LEU B . n 
B 1 378 ALA 378 378 378 ALA ALA B . n 
B 1 379 GLY 379 379 379 GLY GLY B . n 
B 1 380 SER 380 380 380 SER SER B . n 
B 1 381 ARG 381 381 381 ARG ARG B . n 
B 1 382 ILE 382 382 382 ILE ILE B . n 
B 1 383 ILE 383 383 383 ILE ILE B . n 
B 1 384 ALA 384 384 384 ALA ALA B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 ALA 386 386 386 ALA ALA B . n 
B 1 387 HIS 387 387 387 HIS HIS B . n 
B 1 388 ILE 388 388 388 ILE ILE B . n 
B 1 389 LYS 389 389 389 LYS LYS B . n 
B 1 390 CYS 390 390 390 CYS CYS B . n 
B 1 391 GLU 391 391 391 GLU GLU B . n 
B 1 392 ASP 392 392 392 ASP ASP B . n 
B 1 393 PRO 393 393 393 PRO PRO B . n 
B 1 394 THR 394 394 394 THR THR B . n 
B 1 395 SER 395 395 395 SER SER B . n 
B 1 396 TYR 396 396 396 TYR TYR B . n 
B 1 397 MET 397 397 397 MET MET B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 ALA 400 400 400 ALA ALA B . n 
B 1 401 LYS 401 401 401 LYS LYS B . n 
B 1 402 THR 402 402 402 THR THR B . n 
B 1 403 ILE 403 403 403 ILE ILE B . n 
B 1 404 LYS 404 404 404 LYS LYS B . n 
B 1 405 ASP 405 405 405 ASP ASP B . n 
B 1 406 VAL 406 406 406 VAL VAL B . n 
B 1 407 PHE 407 407 407 PHE PHE B . n 
B 1 408 HIS 408 408 408 HIS HIS B . n 
B 1 409 ASN 409 409 409 ASN ASN B . n 
B 1 410 HIS 410 410 410 HIS HIS B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 ILE 412 412 412 ILE ILE B . n 
B 1 413 HIS 413 413 413 HIS HIS B . n 
B 1 414 ALA 414 414 414 ALA ALA B . n 
B 1 415 THR 415 415 415 THR THR B . n 
B 1 416 THR 416 416 416 THR THR B . n 
B 1 417 ILE 417 417 417 ILE ILE B . n 
B 1 418 GLN 418 418 418 GLN GLN B . n 
B 1 419 PRO 419 419 419 PRO PRO B . n 
B 1 420 GLU 420 420 420 GLU GLU B . n 
B 1 421 PHE 421 421 421 PHE PHE B . n 
B 1 422 ALA 422 422 422 ALA ALA B . n 
B 1 423 SER 423 423 423 SER SER B . n 
B 1 424 VAL 424 424 424 VAL VAL B . n 
B 1 425 GLY 425 425 425 GLY GLY B . n 
B 1 426 SER 426 426 426 SER SER B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 SER 428 428 428 SER SER B . n 
B 1 429 SER 429 429 429 SER SER B . n 
B 1 430 VAL 430 430 430 VAL VAL B . n 
B 1 431 VAL 431 431 431 VAL VAL B . n 
B 1 432 PRO 432 432 432 PRO PRO B . n 
B 1 433 CYS 433 433 433 CYS CYS B . n 
B 1 434 GLU 434 434 434 GLU GLU B . n 
B 1 435 LEU 435 435 435 LEU LEU B . n 
B 1 436 ALA 436 436 436 ALA ALA B . n 
B 1 437 CYS 437 437 437 CYS CYS B . n 
B 1 438 ARG 438 438 438 ARG ARG B . n 
B 1 439 THR 439 439 439 THR THR B . n 
B 1 440 GLN 440 440 440 GLN GLN B . n 
B 1 441 CYS 441 441 441 CYS CYS B . n 
B 1 442 ALA 442 442 ?   ?   ?   B . n 
B 1 443 LEU 443 443 ?   ?   ?   B . n 
B 1 444 LYS 444 444 ?   ?   ?   B . n 
B 1 445 GLN 445 445 ?   ?   ?   B . n 
B 1 446 CYS 446 446 ?   ?   ?   B . n 
B 1 447 CYS 447 447 ?   ?   ?   B . n 
B 1 448 GLY 448 448 ?   ?   ?   B . n 
B 1 449 THR 449 449 ?   ?   ?   B . n 
B 1 450 LEU 450 450 ?   ?   ?   B . n 
B 1 451 PRO 451 451 ?   ?   ?   B . n 
B 1 452 GLN 452 452 ?   ?   ?   B . n 
B 1 453 ALA 453 453 ?   ?   ?   B . n 
B 1 454 PRO 454 454 ?   ?   ?   B . n 
B 1 455 SER 455 455 ?   ?   ?   B . n 
B 1 456 GLY 456 456 ?   ?   ?   B . n 
B 1 457 LYS 457 457 ?   ?   ?   B . n 
B 1 458 ASP 458 458 ?   ?   ?   B . n 
B 1 459 ALA 459 459 ?   ?   ?   B . n 
B 1 460 GLU 460 460 ?   ?   ?   B . n 
B 1 461 LYS 461 461 ?   ?   ?   B . n 
B 1 462 THR 462 462 ?   ?   ?   B . n 
B 1 463 PRO 463 463 ?   ?   ?   B . n 
B 1 464 ALA 464 464 ?   ?   ?   B . n 
B 1 465 VAL 465 465 ?   ?   ?   B . n 
B 1 466 SER 466 466 ?   ?   ?   B . n 
B 1 467 ILE 467 467 ?   ?   ?   B . n 
B 1 468 SER 468 468 ?   ?   ?   B . n 
B 1 469 CYS 469 469 ?   ?   ?   B . n 
B 1 470 LEU 470 470 ?   ?   ?   B . n 
B 1 471 GLU 471 471 ?   ?   ?   B . n 
B 1 472 LEU 472 472 ?   ?   ?   B . n 
B 1 473 SER 473 473 ?   ?   ?   B . n 
B 1 474 ASN 474 474 ?   ?   ?   B . n 
B 1 475 ASN 475 475 ?   ?   ?   B . n 
B 1 476 LEU 476 476 ?   ?   ?   B . n 
B 1 477 GLU 477 477 ?   ?   ?   B . n 
B 1 478 LYS 478 478 ?   ?   ?   B . n 
B 1 479 LYS 479 479 ?   ?   ?   B . n 
B 1 480 PRO 480 480 ?   ?   ?   B . n 
B 1 481 ARG 481 481 ?   ?   ?   B . n 
B 1 482 ARG 482 482 ?   ?   ?   B . n 
B 1 483 THR 483 483 ?   ?   ?   B . n 
B 1 484 LYS 484 484 ?   ?   ?   B . n 
B 1 485 ALA 485 485 ?   ?   ?   B . n 
B 1 486 GLU 486 486 ?   ?   ?   B . n 
B 1 487 ASN 487 487 ?   ?   ?   B . n 
B 1 488 ILE 488 488 ?   ?   ?   B . n 
B 1 489 PRO 489 489 ?   ?   ?   B . n 
B 1 490 ALA 490 490 ?   ?   ?   B . n 
B 1 491 VAL 491 491 ?   ?   ?   B . n 
B 1 492 VAL 492 492 ?   ?   ?   B . n 
B 1 493 ILE 493 493 ?   ?   ?   B . n 
B 1 494 GLU 494 494 ?   ?   ?   B . n 
B 1 495 ILE 495 495 ?   ?   ?   B . n 
B 1 496 LYS 496 496 ?   ?   ?   B . n 
B 1 497 ASN 497 497 ?   ?   ?   B . n 
B 1 498 MET 498 498 ?   ?   ?   B . n 
B 1 499 PRO 499 499 ?   ?   ?   B . n 
B 1 500 ASN 500 500 ?   ?   ?   B . n 
B 1 501 LYS 501 501 ?   ?   ?   B . n 
B 1 502 GLN 502 502 ?   ?   ?   B . n 
B 1 503 PRO 503 503 ?   ?   ?   B . n 
B 1 504 GLU 504 504 ?   ?   ?   B . n 
B 1 505 SER 505 505 ?   ?   ?   B . n 
B 1 506 SER 506 506 ?   ?   ?   B . n 
B 1 507 LEU 507 507 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN 1 601 1 ZN ZN A . 
D 2 ZN 1 602 2 ZN ZN A . 
E 2 ZN 1 603 3 ZN ZN A . 
F 2 ZN 1 604 4 ZN ZN A . 
G 2 ZN 1 601 1 ZN ZN B . 
H 2 ZN 1 602 2 ZN ZN B . 
I 2 ZN 1 603 3 ZN ZN B . 
J 2 ZN 1 604 4 ZN ZN B . 
# 
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 GLN 112 ? CG  ? A GLN 112 CG  
2   1 Y 1 A GLN 112 ? CD  ? A GLN 112 CD  
3   1 Y 1 A GLN 112 ? OE1 ? A GLN 112 OE1 
4   1 Y 1 A GLN 112 ? NE2 ? A GLN 112 NE2 
5   1 Y 1 A VAL 268 ? CG1 ? A VAL 268 CG1 
6   1 Y 1 A VAL 268 ? CG2 ? A VAL 268 CG2 
7   1 Y 1 A TYR 270 ? CG  ? A TYR 270 CG  
8   1 Y 1 A TYR 270 ? CD1 ? A TYR 270 CD1 
9   1 Y 1 A TYR 270 ? CD2 ? A TYR 270 CD2 
10  1 Y 1 A TYR 270 ? CE1 ? A TYR 270 CE1 
11  1 Y 1 A TYR 270 ? CE2 ? A TYR 270 CE2 
12  1 Y 1 A TYR 270 ? CZ  ? A TYR 270 CZ  
13  1 Y 1 A TYR 270 ? OH  ? A TYR 270 OH  
14  1 Y 1 A SER 272 ? OG  ? A SER 272 OG  
15  1 Y 1 A TRP 273 ? CG  ? A TRP 273 CG  
16  1 Y 1 A TRP 273 ? CD1 ? A TRP 273 CD1 
17  1 Y 1 A TRP 273 ? CD2 ? A TRP 273 CD2 
18  1 Y 1 A TRP 273 ? NE1 ? A TRP 273 NE1 
19  1 Y 1 A TRP 273 ? CE2 ? A TRP 273 CE2 
20  1 Y 1 A TRP 273 ? CE3 ? A TRP 273 CE3 
21  1 Y 1 A TRP 273 ? CZ2 ? A TRP 273 CZ2 
22  1 Y 1 A TRP 273 ? CZ3 ? A TRP 273 CZ3 
23  1 Y 1 A TRP 273 ? CH2 ? A TRP 273 CH2 
24  1 Y 1 A LYS 274 ? CG  ? A LYS 274 CG  
25  1 Y 1 A LYS 274 ? CD  ? A LYS 274 CD  
26  1 Y 1 A LYS 274 ? CE  ? A LYS 274 CE  
27  1 Y 1 A LYS 274 ? NZ  ? A LYS 274 NZ  
28  1 Y 1 A SER 277 ? OG  ? A SER 277 OG  
29  1 Y 1 A GLU 278 ? CG  ? A GLU 278 CG  
30  1 Y 1 A GLU 278 ? CD  ? A GLU 278 CD  
31  1 Y 1 A GLU 278 ? OE1 ? A GLU 278 OE1 
32  1 Y 1 A GLU 278 ? OE2 ? A GLU 278 OE2 
33  1 Y 1 A PHE 281 ? CG  ? A PHE 281 CG  
34  1 Y 1 A PHE 281 ? CD1 ? A PHE 281 CD1 
35  1 Y 1 A PHE 281 ? CD2 ? A PHE 281 CD2 
36  1 Y 1 A PHE 281 ? CE1 ? A PHE 281 CE1 
37  1 Y 1 A PHE 281 ? CE2 ? A PHE 281 CE2 
38  1 Y 1 A PHE 281 ? CZ  ? A PHE 281 CZ  
39  1 Y 1 A CYS 282 ? SG  ? A CYS 282 SG  
40  1 Y 1 A VAL 283 ? CG1 ? A VAL 283 CG1 
41  1 Y 1 A VAL 283 ? CG2 ? A VAL 283 CG2 
42  1 Y 1 A ASN 284 ? CG  ? A ASN 284 CG  
43  1 Y 1 A ASN 284 ? OD1 ? A ASN 284 OD1 
44  1 Y 1 A ASN 284 ? ND2 ? A ASN 284 ND2 
45  1 Y 1 A PRO 288 ? CG  ? A PRO 288 CG  
46  1 Y 1 A PRO 288 ? CD  ? A PRO 288 CD  
47  1 Y 1 A ASP 289 ? CG  ? A ASP 289 CG  
48  1 Y 1 A ASP 289 ? OD1 ? A ASP 289 OD1 
49  1 Y 1 A ASP 289 ? OD2 ? A ASP 289 OD2 
50  1 Y 1 A PRO 290 ? CG  ? A PRO 290 CG  
51  1 Y 1 A PRO 290 ? CD  ? A PRO 290 CD  
52  1 Y 1 A LYS 292 ? CG  ? A LYS 292 CG  
53  1 Y 1 A LYS 292 ? CD  ? A LYS 292 CD  
54  1 Y 1 A LYS 292 ? CE  ? A LYS 292 CE  
55  1 Y 1 A LYS 292 ? NZ  ? A LYS 292 NZ  
56  1 Y 1 A PHE 294 ? CG  ? A PHE 294 CG  
57  1 Y 1 A PHE 294 ? CD1 ? A PHE 294 CD1 
58  1 Y 1 A PHE 294 ? CD2 ? A PHE 294 CD2 
59  1 Y 1 A PHE 294 ? CE1 ? A PHE 294 CE1 
60  1 Y 1 A PHE 294 ? CE2 ? A PHE 294 CE2 
61  1 Y 1 A PHE 294 ? CZ  ? A PHE 294 CZ  
62  1 Y 1 A VAL 295 ? CG1 ? A VAL 295 CG1 
63  1 Y 1 A VAL 295 ? CG2 ? A VAL 295 CG2 
64  1 Y 1 A GLU 296 ? CG  ? A GLU 296 CG  
65  1 Y 1 A GLU 296 ? CD  ? A GLU 296 CD  
66  1 Y 1 A GLU 296 ? OE1 ? A GLU 296 OE1 
67  1 Y 1 A GLU 296 ? OE2 ? A GLU 296 OE2 
68  1 Y 1 A ILE 297 ? CG1 ? A ILE 297 CG1 
69  1 Y 1 A ILE 297 ? CG2 ? A ILE 297 CG2 
70  1 Y 1 A ILE 297 ? CD1 ? A ILE 297 CD1 
71  1 Y 1 A ILE 298 ? CG1 ? A ILE 298 CG1 
72  1 Y 1 A ILE 298 ? CG2 ? A ILE 298 CG2 
73  1 Y 1 A ILE 298 ? CD1 ? A ILE 298 CD1 
74  1 Y 1 A SER 300 ? OG  ? A SER 300 OG  
75  1 Y 1 A THR 301 ? OG1 ? A THR 301 OG1 
76  1 Y 1 A THR 301 ? CG2 ? A THR 301 CG2 
77  1 Y 1 A HIS 302 ? CG  ? A HIS 302 CG  
78  1 Y 1 A HIS 302 ? ND1 ? A HIS 302 ND1 
79  1 Y 1 A HIS 302 ? CD2 ? A HIS 302 CD2 
80  1 Y 1 A HIS 302 ? CE1 ? A HIS 302 CE1 
81  1 Y 1 A HIS 302 ? NE2 ? A HIS 302 NE2 
82  1 Y 1 A SER 304 ? OG  ? A SER 304 OG  
83  1 Y 1 A VAL 305 ? CG1 ? A VAL 305 CG1 
84  1 Y 1 A VAL 305 ? CG2 ? A VAL 305 CG2 
85  1 Y 1 A PRO 310 ? CG  ? A PRO 310 CG  
86  1 Y 1 A PRO 310 ? CD  ? A PRO 310 CD  
87  1 Y 1 A VAL 313 ? CG1 ? A VAL 313 CG1 
88  1 Y 1 A VAL 313 ? CG2 ? A VAL 313 CG2 
89  1 Y 1 A LEU 316 ? CG  ? A LEU 316 CG  
90  1 Y 1 A LEU 316 ? CD1 ? A LEU 316 CD1 
91  1 Y 1 A LEU 316 ? CD2 ? A LEU 316 CD2 
92  1 Y 1 A ARG 354 ? CG  ? A ARG 354 CG  
93  1 Y 1 A ARG 354 ? CD  ? A ARG 354 CD  
94  1 Y 1 A ARG 354 ? NE  ? A ARG 354 NE  
95  1 Y 1 A ARG 354 ? CZ  ? A ARG 354 CZ  
96  1 Y 1 A ARG 354 ? NH1 ? A ARG 354 NH1 
97  1 Y 1 A ARG 354 ? NH2 ? A ARG 354 NH2 
98  1 Y 1 A VAL 431 ? CG1 ? A VAL 431 CG1 
99  1 Y 1 A VAL 431 ? CG2 ? A VAL 431 CG2 
100 1 Y 1 A PRO 432 ? CG  ? A PRO 432 CG  
101 1 Y 1 A PRO 432 ? CD  ? A PRO 432 CD  
102 1 Y 1 A ARG 438 ? CG  ? A ARG 438 CG  
103 1 Y 1 A ARG 438 ? CD  ? A ARG 438 CD  
104 1 Y 1 A ARG 438 ? NE  ? A ARG 438 NE  
105 1 Y 1 A ARG 438 ? CZ  ? A ARG 438 CZ  
106 1 Y 1 A ARG 438 ? NH1 ? A ARG 438 NH1 
107 1 Y 1 A ARG 438 ? NH2 ? A ARG 438 NH2 
108 1 Y 1 B GLN 112 ? CG  ? B GLN 112 CG  
109 1 Y 1 B GLN 112 ? CD  ? B GLN 112 CD  
110 1 Y 1 B GLN 112 ? OE1 ? B GLN 112 OE1 
111 1 Y 1 B GLN 112 ? NE2 ? B GLN 112 NE2 
112 1 Y 1 B VAL 268 ? CG1 ? B VAL 268 CG1 
113 1 Y 1 B VAL 268 ? CG2 ? B VAL 268 CG2 
114 1 Y 1 B TYR 270 ? CG  ? B TYR 270 CG  
115 1 Y 1 B TYR 270 ? CD1 ? B TYR 270 CD1 
116 1 Y 1 B TYR 270 ? CD2 ? B TYR 270 CD2 
117 1 Y 1 B TYR 270 ? CE1 ? B TYR 270 CE1 
118 1 Y 1 B TYR 270 ? CE2 ? B TYR 270 CE2 
119 1 Y 1 B TYR 270 ? CZ  ? B TYR 270 CZ  
120 1 Y 1 B TYR 270 ? OH  ? B TYR 270 OH  
121 1 Y 1 B SER 272 ? OG  ? B SER 272 OG  
122 1 Y 1 B TRP 273 ? CG  ? B TRP 273 CG  
123 1 Y 1 B TRP 273 ? CD1 ? B TRP 273 CD1 
124 1 Y 1 B TRP 273 ? CD2 ? B TRP 273 CD2 
125 1 Y 1 B TRP 273 ? NE1 ? B TRP 273 NE1 
126 1 Y 1 B TRP 273 ? CE2 ? B TRP 273 CE2 
127 1 Y 1 B TRP 273 ? CE3 ? B TRP 273 CE3 
128 1 Y 1 B TRP 273 ? CZ2 ? B TRP 273 CZ2 
129 1 Y 1 B TRP 273 ? CZ3 ? B TRP 273 CZ3 
130 1 Y 1 B TRP 273 ? CH2 ? B TRP 273 CH2 
131 1 Y 1 B LYS 274 ? CG  ? B LYS 274 CG  
132 1 Y 1 B LYS 274 ? CD  ? B LYS 274 CD  
133 1 Y 1 B LYS 274 ? CE  ? B LYS 274 CE  
134 1 Y 1 B LYS 274 ? NZ  ? B LYS 274 NZ  
135 1 Y 1 B SER 277 ? OG  ? B SER 277 OG  
136 1 Y 1 B GLU 278 ? CG  ? B GLU 278 CG  
137 1 Y 1 B GLU 278 ? CD  ? B GLU 278 CD  
138 1 Y 1 B GLU 278 ? OE1 ? B GLU 278 OE1 
139 1 Y 1 B GLU 278 ? OE2 ? B GLU 278 OE2 
140 1 Y 1 B PHE 281 ? CG  ? B PHE 281 CG  
141 1 Y 1 B PHE 281 ? CD1 ? B PHE 281 CD1 
142 1 Y 1 B PHE 281 ? CD2 ? B PHE 281 CD2 
143 1 Y 1 B PHE 281 ? CE1 ? B PHE 281 CE1 
144 1 Y 1 B PHE 281 ? CE2 ? B PHE 281 CE2 
145 1 Y 1 B PHE 281 ? CZ  ? B PHE 281 CZ  
146 1 Y 1 B CYS 282 ? SG  ? B CYS 282 SG  
147 1 Y 1 B VAL 283 ? CG1 ? B VAL 283 CG1 
148 1 Y 1 B VAL 283 ? CG2 ? B VAL 283 CG2 
149 1 Y 1 B ASN 284 ? CG  ? B ASN 284 CG  
150 1 Y 1 B ASN 284 ? OD1 ? B ASN 284 OD1 
151 1 Y 1 B ASN 284 ? ND2 ? B ASN 284 ND2 
152 1 Y 1 B PRO 288 ? CG  ? B PRO 288 CG  
153 1 Y 1 B PRO 288 ? CD  ? B PRO 288 CD  
154 1 Y 1 B ASP 289 ? CG  ? B ASP 289 CG  
155 1 Y 1 B ASP 289 ? OD1 ? B ASP 289 OD1 
156 1 Y 1 B ASP 289 ? OD2 ? B ASP 289 OD2 
157 1 Y 1 B PRO 290 ? CG  ? B PRO 290 CG  
158 1 Y 1 B PRO 290 ? CD  ? B PRO 290 CD  
159 1 Y 1 B LYS 292 ? CG  ? B LYS 292 CG  
160 1 Y 1 B LYS 292 ? CD  ? B LYS 292 CD  
161 1 Y 1 B LYS 292 ? CE  ? B LYS 292 CE  
162 1 Y 1 B LYS 292 ? NZ  ? B LYS 292 NZ  
163 1 Y 1 B PHE 294 ? CG  ? B PHE 294 CG  
164 1 Y 1 B PHE 294 ? CD1 ? B PHE 294 CD1 
165 1 Y 1 B PHE 294 ? CD2 ? B PHE 294 CD2 
166 1 Y 1 B PHE 294 ? CE1 ? B PHE 294 CE1 
167 1 Y 1 B PHE 294 ? CE2 ? B PHE 294 CE2 
168 1 Y 1 B PHE 294 ? CZ  ? B PHE 294 CZ  
169 1 Y 1 B VAL 295 ? CG1 ? B VAL 295 CG1 
170 1 Y 1 B VAL 295 ? CG2 ? B VAL 295 CG2 
171 1 Y 1 B GLU 296 ? CG  ? B GLU 296 CG  
172 1 Y 1 B GLU 296 ? CD  ? B GLU 296 CD  
173 1 Y 1 B GLU 296 ? OE1 ? B GLU 296 OE1 
174 1 Y 1 B GLU 296 ? OE2 ? B GLU 296 OE2 
175 1 Y 1 B ILE 297 ? CG1 ? B ILE 297 CG1 
176 1 Y 1 B ILE 297 ? CG2 ? B ILE 297 CG2 
177 1 Y 1 B ILE 297 ? CD1 ? B ILE 297 CD1 
178 1 Y 1 B ILE 298 ? CG1 ? B ILE 298 CG1 
179 1 Y 1 B ILE 298 ? CG2 ? B ILE 298 CG2 
180 1 Y 1 B ILE 298 ? CD1 ? B ILE 298 CD1 
181 1 Y 1 B SER 300 ? OG  ? B SER 300 OG  
182 1 Y 1 B THR 301 ? OG1 ? B THR 301 OG1 
183 1 Y 1 B THR 301 ? CG2 ? B THR 301 CG2 
184 1 Y 1 B HIS 302 ? CG  ? B HIS 302 CG  
185 1 Y 1 B HIS 302 ? ND1 ? B HIS 302 ND1 
186 1 Y 1 B HIS 302 ? CD2 ? B HIS 302 CD2 
187 1 Y 1 B HIS 302 ? CE1 ? B HIS 302 CE1 
188 1 Y 1 B HIS 302 ? NE2 ? B HIS 302 NE2 
189 1 Y 1 B SER 304 ? OG  ? B SER 304 OG  
190 1 Y 1 B VAL 305 ? CG1 ? B VAL 305 CG1 
191 1 Y 1 B VAL 305 ? CG2 ? B VAL 305 CG2 
192 1 Y 1 B PRO 310 ? CG  ? B PRO 310 CG  
193 1 Y 1 B PRO 310 ? CD  ? B PRO 310 CD  
194 1 Y 1 B VAL 313 ? CG1 ? B VAL 313 CG1 
195 1 Y 1 B VAL 313 ? CG2 ? B VAL 313 CG2 
196 1 Y 1 B LEU 316 ? CG  ? B LEU 316 CG  
197 1 Y 1 B LEU 316 ? CD1 ? B LEU 316 CD1 
198 1 Y 1 B LEU 316 ? CD2 ? B LEU 316 CD2 
199 1 Y 1 B ARG 354 ? CG  ? B ARG 354 CG  
200 1 Y 1 B ARG 354 ? CD  ? B ARG 354 CD  
201 1 Y 1 B ARG 354 ? NE  ? B ARG 354 NE  
202 1 Y 1 B ARG 354 ? CZ  ? B ARG 354 CZ  
203 1 Y 1 B ARG 354 ? NH1 ? B ARG 354 NH1 
204 1 Y 1 B ARG 354 ? NH2 ? B ARG 354 NH2 
205 1 Y 1 B VAL 431 ? CG1 ? B VAL 431 CG1 
206 1 Y 1 B VAL 431 ? CG2 ? B VAL 431 CG2 
207 1 Y 1 B PRO 432 ? CG  ? B PRO 432 CG  
208 1 Y 1 B PRO 432 ? CD  ? B PRO 432 CD  
209 1 Y 1 B ARG 438 ? CG  ? B ARG 438 CG  
210 1 Y 1 B ARG 438 ? CD  ? B ARG 438 CD  
211 1 Y 1 B ARG 438 ? NE  ? B ARG 438 NE  
212 1 Y 1 B ARG 438 ? CZ  ? B ARG 438 CZ  
213 1 Y 1 B ARG 438 ? NH1 ? B ARG 438 NH1 
214 1 Y 1 B ARG 438 ? NH2 ? B ARG 438 NH2 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZB0 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZB0 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZB0 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8ZB0 
_struct.title                        'Cryo-EM structure of human ZnT1' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8ZB0 
_struct_keywords.text            'Transport, ZnT1, Homodimer, Zinc, MEMBRAIN PROTEIN, PROTEIN TRANSPORT' 
_struct_keywords.pdbx_keywords   'PROTEIN TRANSPORT' 
# 
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 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ZNT1_HUMAN 
_struct_ref.pdbx_db_accession          Q9Y6M5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGCWGRNRGRLLCMLALTFMFMVLEVVVSRVTSSLAMLSDSFHMLSDVLALVVALVAERFARRTHATQKNTFGWIRAEVM
GALVNAIFLTGLCFAILLEAIERFIEPHEMQQPLVVLGVGVAGLLVNVLGLCLFHHHSGFSQDSGHGHSHGGHGHGHGLP
KGPRVKSTRPGSSDINVAPGEQGPDQEETNTLVANTSNSNGLKLDPADPENPRSGDTVEVQVNGNLVREPDHMELEEDRA
GQLNMRGVFLHVLGDALGSVIVVVNALVFYFSWKGCSEGDFCVNPCFPDPCKAFVEIINSTHASVYEAGPCWVLYLDPTL
CVVMVCILLYTTYPLLKESALILLQTVPKQIDIRNLIKELRNVEGVEEVHELHVWQLAGSRIIATAHIKCEDPTSYMEVA
KTIKDVFHNHGIHATTIQPEFASVGSKSSVVPCELACRTQCALKQCCGTLPQAPSGKDAEKTPAVSISCLELSNNLEKKP
RRTKAENIPAVVIEIKNMPNKQPESSL
;
_struct_ref.pdbx_align_begin           1 
# 
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 8ZB0 A 1 ? 507 ? Q9Y6M5 1 ? 507 ? 1 507 
2 1 8ZB0 B 1 ? 507 ? Q9Y6M5 1 ? 507 ? 1 507 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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_
_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  AA1 ASN A 7   ? THR A 32  ? ASN A 7   THR A 32  1 ? 26 
HELX_P HELX_P2  AA2 HIS A 43  ? ASP A 47  ? HIS A 43  ASP A 47  5 ? 5  
HELX_P HELX_P3  AA3 VAL A 48  ? ALA A 57  ? VAL A 48  ALA A 57  1 ? 10 
HELX_P HELX_P4  AA4 ARG A 76  ? GLU A 106 ? ARG A 76  GLU A 106 1 ? 31 
HELX_P HELX_P5  AA5 GLN A 112 ? LEU A 133 ? GLN A 112 LEU A 133 1 ? 22 
HELX_P HELX_P6  AA6 LEU A 243 ? VAL A 268 ? LEU A 243 VAL A 268 1 ? 26 
HELX_P HELX_P7  AA7 CYS A 291 ? ASN A 299 ? CYS A 291 ASN A 299 1 ? 9  
HELX_P HELX_P8  AA8 ASP A 317 ? LEU A 344 ? ASP A 317 LEU A 344 1 ? 28 
HELX_P HELX_P9  AA9 ASP A 352 ? VAL A 363 ? ASP A 352 VAL A 363 1 ? 12 
HELX_P HELX_P10 AB1 SER A 395 ? ASN A 409 ? SER A 395 ASN A 409 1 ? 15 
HELX_P HELX_P11 AB2 ARG B 8   ? THR B 32  ? ARG B 8   THR B 32  1 ? 25 
HELX_P HELX_P12 AB3 HIS B 43  ? ASP B 47  ? HIS B 43  ASP B 47  5 ? 5  
HELX_P HELX_P13 AB4 VAL B 48  ? ALA B 57  ? VAL B 48  ALA B 57  1 ? 10 
HELX_P HELX_P14 AB5 ARG B 76  ? GLU B 106 ? ARG B 76  GLU B 106 1 ? 31 
HELX_P HELX_P15 AB6 GLN B 112 ? LEU B 133 ? GLN B 112 LEU B 133 1 ? 22 
HELX_P HELX_P16 AB7 LEU B 243 ? VAL B 268 ? LEU B 243 VAL B 268 1 ? 26 
HELX_P HELX_P17 AB8 CYS B 291 ? ASN B 299 ? CYS B 291 ASN B 299 1 ? 9  
HELX_P HELX_P18 AB9 ASP B 317 ? LEU B 344 ? ASP B 317 LEU B 344 1 ? 28 
HELX_P HELX_P19 AC1 ASP B 352 ? VAL B 363 ? ASP B 352 VAL B 363 1 ? 12 
HELX_P HELX_P20 AC2 SER B 395 ? ASN B 409 ? SER B 395 ASN B 409 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 286 SG  ? ? ? 1_555 A CYS 311 SG ? ? A CYS 286 A CYS 311 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
disulf2  disulf ? ? A CYS 291 SG  ? ? ? 1_555 B CYS 291 SG ? ? A CYS 291 B CYS 291 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
disulf3  disulf ? ? B CYS 286 SG  ? ? ? 1_555 B CYS 311 SG ? ? B CYS 286 B CYS 311 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc1  metalc ? ? A ASP 47  OD2 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 47  A ZN  602 1_555 ? ? ? ? ? ? ? 1.793 ? ? 
metalc2  metalc ? ? A ASP 255 OD1 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 255 A ZN  602 1_555 ? ? ? ? ? ? ? 1.759 ? ? 
metalc3  metalc ? ? A HIS 387 ND1 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 387 A ZN  604 1_555 ? ? ? ? ? ? ? 2.263 ? ? 
metalc4  metalc ? ? A HIS 413 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 413 A ZN  603 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc5  metalc ? ? A CYS 437 SG  ? ? ? 1_555 I ZN  .   ZN ? ? A CYS 437 B ZN  603 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc6  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 B CYS 437 SG ? ? A ZN  603 B CYS 437 1_555 ? ? ? ? ? ? ? 1.979 ? ? 
metalc7  metalc ? ? B ASP 47  OD2 ? ? ? 1_555 H ZN  .   ZN ? ? B ASP 47  B ZN  602 1_555 ? ? ? ? ? ? ? 1.793 ? ? 
metalc8  metalc ? ? B ASP 255 OD1 ? ? ? 1_555 H ZN  .   ZN ? ? B ASP 255 B ZN  602 1_555 ? ? ? ? ? ? ? 1.759 ? ? 
metalc9  metalc ? ? B HIS 387 ND1 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 387 B ZN  604 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc10 metalc ? ? B HIS 413 ND1 ? ? ? 1_555 I ZN  .   ZN ? ? B HIS 413 B ZN  603 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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 OD2 ? A ASP 47  ? A ASP 47  ? 1_555 ZN ? D ZN . ? A ZN 602 ? 1_555 OD1 ? A ASP 255 ? A ASP 255 ? 1_555 142.9 ? 
2 ND1 ? A HIS 413 ? A HIS 413 ? 1_555 ZN ? E ZN . ? A ZN 603 ? 1_555 SG  ? B CYS 437 ? B CYS 437 ? 1_555 155.6 ? 
3 SG  ? A CYS 437 ? A CYS 437 ? 1_555 ZN ? I ZN . ? B ZN 603 ? 1_555 ND1 ? B HIS 413 ? B HIS 413 ? 1_555 153.6 ? 
4 OD2 ? B ASP 47  ? B ASP 47  ? 1_555 ZN ? H ZN . ? B ZN 602 ? 1_555 OD1 ? B ASP 255 ? B ASP 255 ? 1_555 143.0 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 286 ? CYS A 311 ? CYS A 286 ? 1_555 CYS A 311 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 291 ? CYS B 291 ? CYS A 291 ? 1_555 CYS B 291 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 286 ? CYS B 311 ? CYS B 286 ? 1_555 CYS B 311 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
# 
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 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? 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 
AA1 1 VAL A 374 ? GLN A 376 ? VAL A 374 GLN A 376 
AA1 2 ILE A 382 ? ILE A 388 ? ILE A 382 ILE A 388 
AA1 3 ALA A 414 ? PRO A 419 ? ALA A 414 PRO A 419 
AA2 1 VAL B 374 ? GLN B 376 ? VAL B 374 GLN B 376 
AA2 2 ILE B 382 ? ILE B 388 ? ILE B 382 ILE B 388 
AA2 3 ALA B 414 ? PRO B 419 ? ALA B 414 PRO B 419 
# 
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 
AA1 1 2 N TRP A 375 ? N TRP A 375 O ILE A 383 ? O ILE A 383 
AA1 2 3 N ALA A 386 ? N ALA A 386 O THR A 416 ? O THR A 416 
AA2 1 2 N TRP B 375 ? N TRP B 375 O ILE B 383 ? O ILE B 383 
AA2 2 3 N ALA B 386 ? N ALA B 386 O THR B 416 ? O THR B 416 
# 
_pdbx_entry_details.entry_id                   8ZB0 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ND1 A HIS 408 ? ? ZN A ZN 603 ? ? 1.67 
2 1 ND1 B HIS 408 ? ? ZN B ZN 603 ? ? 1.67 
3 1 OE2 B GLU 420 ? ? ZN B ZN 604 ? ? 1.68 
4 1 OE2 A GLU 420 ? ? ZN A ZN 604 ? ? 1.68 
# 
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 LEU A 45  ? ? -66.38  3.34    
2  1 ARG A 63  ? ? -85.70  48.70   
3  1 ASN A 70  ? ? -167.51 111.11  
4  1 TRP A 74  ? ? -92.77  31.06   
5  1 PHE A 269 ? ? -143.30 -29.19  
6  1 LYS A 274 ? ? -120.51 -53.01  
7  1 ALA A 303 ? ? -79.68  -163.63 
8  1 SER A 304 ? ? -78.49  -168.88 
9  1 ASP A 317 ? ? -107.08 -63.22  
10 1 PRO A 348 ? ? -62.15  -175.42 
11 1 GLU A 371 ? ? -14.99  120.20  
12 1 ALA A 386 ? ? -173.21 129.85  
13 1 PRO A 393 ? ? -82.18  41.35   
14 1 SER A 395 ? ? -97.31  36.75   
15 1 THR A 416 ? ? -161.95 103.72  
16 1 LYS A 427 ? ? -92.07  49.81   
17 1 SER A 428 ? ? -141.24 22.49   
18 1 CYS A 433 ? ? 50.21   15.62   
19 1 GLU A 434 ? ? 59.98   2.08    
20 1 LEU A 435 ? ? -162.68 108.60  
21 1 CYS A 437 ? ? -110.49 -82.59  
22 1 ARG A 438 ? ? -163.22 -67.67  
23 1 THR A 439 ? ? -135.63 -66.80  
24 1 LEU B 45  ? ? -66.39  3.32    
25 1 ARG B 63  ? ? -85.67  48.78   
26 1 ASN B 70  ? ? -167.52 111.16  
27 1 TRP B 74  ? ? -92.81  31.09   
28 1 PHE B 269 ? ? -143.33 -29.19  
29 1 LYS B 274 ? ? -120.52 -53.03  
30 1 ALA B 303 ? ? -79.67  -163.61 
31 1 SER B 304 ? ? -78.49  -168.91 
32 1 ASP B 317 ? ? -107.05 -63.25  
33 1 PRO B 348 ? ? -62.19  -175.41 
34 1 GLU B 371 ? ? -15.00  120.21  
35 1 ALA B 386 ? ? -173.24 129.83  
36 1 PRO B 393 ? ? -82.17  41.32   
37 1 SER B 395 ? ? -97.31  36.77   
38 1 THR B 416 ? ? -161.92 103.66  
39 1 LYS B 427 ? ? -92.11  49.84   
40 1 SER B 428 ? ? -141.25 22.47   
41 1 CYS B 433 ? ? 50.26   15.63   
42 1 GLU B 434 ? ? 59.90   2.10    
43 1 LEU B 435 ? ? -162.70 108.58  
44 1 CYS B 437 ? ? -110.46 -82.56  
45 1 ARG B 438 ? ? -163.24 -67.64  
46 1 THR B 439 ? ? -135.63 -66.78  
# 
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 30 ? ? 0.152 'SIDE CHAIN' 
2 1 ARG A 59 ? ? 0.260 'SIDE CHAIN' 
3 1 ARG B 30 ? ? 0.152 'SIDE CHAIN' 
4 1 ARG B 59 ? ? 0.260 'SIDE CHAIN' 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8ZB0 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    8ZB0 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.7 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               2188560 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'ZnT1 homodimer' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8ZB0 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              8ZB0 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8ZB0 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 1   ? A MET 1   
2   1 Y 1 A GLY 2   ? A GLY 2   
3   1 Y 1 A CYS 3   ? A CYS 3   
4   1 Y 1 A TRP 4   ? A TRP 4   
5   1 Y 1 A GLY 5   ? A GLY 5   
6   1 Y 1 A ARG 6   ? A ARG 6   
7   1 Y 1 A HIS 135 ? A HIS 135 
8   1 Y 1 A HIS 136 ? A HIS 136 
9   1 Y 1 A HIS 137 ? A HIS 137 
10  1 Y 1 A SER 138 ? A SER 138 
11  1 Y 1 A GLY 139 ? A GLY 139 
12  1 Y 1 A PHE 140 ? A PHE 140 
13  1 Y 1 A SER 141 ? A SER 141 
14  1 Y 1 A GLN 142 ? A GLN 142 
15  1 Y 1 A ASP 143 ? A ASP 143 
16  1 Y 1 A SER 144 ? A SER 144 
17  1 Y 1 A GLY 145 ? A GLY 145 
18  1 Y 1 A HIS 146 ? A HIS 146 
19  1 Y 1 A GLY 147 ? A GLY 147 
20  1 Y 1 A HIS 148 ? A HIS 148 
21  1 Y 1 A SER 149 ? A SER 149 
22  1 Y 1 A HIS 150 ? A HIS 150 
23  1 Y 1 A GLY 151 ? A GLY 151 
24  1 Y 1 A GLY 152 ? A GLY 152 
25  1 Y 1 A HIS 153 ? A HIS 153 
26  1 Y 1 A GLY 154 ? A GLY 154 
27  1 Y 1 A HIS 155 ? A HIS 155 
28  1 Y 1 A GLY 156 ? A GLY 156 
29  1 Y 1 A HIS 157 ? A HIS 157 
30  1 Y 1 A GLY 158 ? A GLY 158 
31  1 Y 1 A LEU 159 ? A LEU 159 
32  1 Y 1 A PRO 160 ? A PRO 160 
33  1 Y 1 A LYS 161 ? A LYS 161 
34  1 Y 1 A GLY 162 ? A GLY 162 
35  1 Y 1 A PRO 163 ? A PRO 163 
36  1 Y 1 A ARG 164 ? A ARG 164 
37  1 Y 1 A VAL 165 ? A VAL 165 
38  1 Y 1 A LYS 166 ? A LYS 166 
39  1 Y 1 A SER 167 ? A SER 167 
40  1 Y 1 A THR 168 ? A THR 168 
41  1 Y 1 A ARG 169 ? A ARG 169 
42  1 Y 1 A PRO 170 ? A PRO 170 
43  1 Y 1 A GLY 171 ? A GLY 171 
44  1 Y 1 A SER 172 ? A SER 172 
45  1 Y 1 A SER 173 ? A SER 173 
46  1 Y 1 A ASP 174 ? A ASP 174 
47  1 Y 1 A ILE 175 ? A ILE 175 
48  1 Y 1 A ASN 176 ? A ASN 176 
49  1 Y 1 A VAL 177 ? A VAL 177 
50  1 Y 1 A ALA 178 ? A ALA 178 
51  1 Y 1 A PRO 179 ? A PRO 179 
52  1 Y 1 A GLY 180 ? A GLY 180 
53  1 Y 1 A GLU 181 ? A GLU 181 
54  1 Y 1 A GLN 182 ? A GLN 182 
55  1 Y 1 A GLY 183 ? A GLY 183 
56  1 Y 1 A PRO 184 ? A PRO 184 
57  1 Y 1 A ASP 185 ? A ASP 185 
58  1 Y 1 A GLN 186 ? A GLN 186 
59  1 Y 1 A GLU 187 ? A GLU 187 
60  1 Y 1 A GLU 188 ? A GLU 188 
61  1 Y 1 A THR 189 ? A THR 189 
62  1 Y 1 A ASN 190 ? A ASN 190 
63  1 Y 1 A THR 191 ? A THR 191 
64  1 Y 1 A LEU 192 ? A LEU 192 
65  1 Y 1 A VAL 193 ? A VAL 193 
66  1 Y 1 A ALA 194 ? A ALA 194 
67  1 Y 1 A ASN 195 ? A ASN 195 
68  1 Y 1 A THR 196 ? A THR 196 
69  1 Y 1 A SER 197 ? A SER 197 
70  1 Y 1 A ASN 198 ? A ASN 198 
71  1 Y 1 A SER 199 ? A SER 199 
72  1 Y 1 A ASN 200 ? A ASN 200 
73  1 Y 1 A GLY 201 ? A GLY 201 
74  1 Y 1 A LEU 202 ? A LEU 202 
75  1 Y 1 A LYS 203 ? A LYS 203 
76  1 Y 1 A LEU 204 ? A LEU 204 
77  1 Y 1 A ASP 205 ? A ASP 205 
78  1 Y 1 A PRO 206 ? A PRO 206 
79  1 Y 1 A ALA 207 ? A ALA 207 
80  1 Y 1 A ASP 208 ? A ASP 208 
81  1 Y 1 A PRO 209 ? A PRO 209 
82  1 Y 1 A GLU 210 ? A GLU 210 
83  1 Y 1 A ASN 211 ? A ASN 211 
84  1 Y 1 A PRO 212 ? A PRO 212 
85  1 Y 1 A ARG 213 ? A ARG 213 
86  1 Y 1 A SER 214 ? A SER 214 
87  1 Y 1 A GLY 215 ? A GLY 215 
88  1 Y 1 A ASP 216 ? A ASP 216 
89  1 Y 1 A THR 217 ? A THR 217 
90  1 Y 1 A VAL 218 ? A VAL 218 
91  1 Y 1 A GLU 219 ? A GLU 219 
92  1 Y 1 A VAL 220 ? A VAL 220 
93  1 Y 1 A GLN 221 ? A GLN 221 
94  1 Y 1 A VAL 222 ? A VAL 222 
95  1 Y 1 A ASN 223 ? A ASN 223 
96  1 Y 1 A GLY 224 ? A GLY 224 
97  1 Y 1 A ASN 225 ? A ASN 225 
98  1 Y 1 A LEU 226 ? A LEU 226 
99  1 Y 1 A VAL 227 ? A VAL 227 
100 1 Y 1 A ARG 228 ? A ARG 228 
101 1 Y 1 A GLU 229 ? A GLU 229 
102 1 Y 1 A PRO 230 ? A PRO 230 
103 1 Y 1 A ASP 231 ? A ASP 231 
104 1 Y 1 A HIS 232 ? A HIS 232 
105 1 Y 1 A MET 233 ? A MET 233 
106 1 Y 1 A GLU 234 ? A GLU 234 
107 1 Y 1 A LEU 235 ? A LEU 235 
108 1 Y 1 A GLU 236 ? A GLU 236 
109 1 Y 1 A GLU 237 ? A GLU 237 
110 1 Y 1 A ASP 238 ? A ASP 238 
111 1 Y 1 A ARG 239 ? A ARG 239 
112 1 Y 1 A ALA 240 ? A ALA 240 
113 1 Y 1 A ALA 442 ? A ALA 442 
114 1 Y 1 A LEU 443 ? A LEU 443 
115 1 Y 1 A LYS 444 ? A LYS 444 
116 1 Y 1 A GLN 445 ? A GLN 445 
117 1 Y 1 A CYS 446 ? A CYS 446 
118 1 Y 1 A CYS 447 ? A CYS 447 
119 1 Y 1 A GLY 448 ? A GLY 448 
120 1 Y 1 A THR 449 ? A THR 449 
121 1 Y 1 A LEU 450 ? A LEU 450 
122 1 Y 1 A PRO 451 ? A PRO 451 
123 1 Y 1 A GLN 452 ? A GLN 452 
124 1 Y 1 A ALA 453 ? A ALA 453 
125 1 Y 1 A PRO 454 ? A PRO 454 
126 1 Y 1 A SER 455 ? A SER 455 
127 1 Y 1 A GLY 456 ? A GLY 456 
128 1 Y 1 A LYS 457 ? A LYS 457 
129 1 Y 1 A ASP 458 ? A ASP 458 
130 1 Y 1 A ALA 459 ? A ALA 459 
131 1 Y 1 A GLU 460 ? A GLU 460 
132 1 Y 1 A LYS 461 ? A LYS 461 
133 1 Y 1 A THR 462 ? A THR 462 
134 1 Y 1 A PRO 463 ? A PRO 463 
135 1 Y 1 A ALA 464 ? A ALA 464 
136 1 Y 1 A VAL 465 ? A VAL 465 
137 1 Y 1 A SER 466 ? A SER 466 
138 1 Y 1 A ILE 467 ? A ILE 467 
139 1 Y 1 A SER 468 ? A SER 468 
140 1 Y 1 A CYS 469 ? A CYS 469 
141 1 Y 1 A LEU 470 ? A LEU 470 
142 1 Y 1 A GLU 471 ? A GLU 471 
143 1 Y 1 A LEU 472 ? A LEU 472 
144 1 Y 1 A SER 473 ? A SER 473 
145 1 Y 1 A ASN 474 ? A ASN 474 
146 1 Y 1 A ASN 475 ? A ASN 475 
147 1 Y 1 A LEU 476 ? A LEU 476 
148 1 Y 1 A GLU 477 ? A GLU 477 
149 1 Y 1 A LYS 478 ? A LYS 478 
150 1 Y 1 A LYS 479 ? A LYS 479 
151 1 Y 1 A PRO 480 ? A PRO 480 
152 1 Y 1 A ARG 481 ? A ARG 481 
153 1 Y 1 A ARG 482 ? A ARG 482 
154 1 Y 1 A THR 483 ? A THR 483 
155 1 Y 1 A LYS 484 ? A LYS 484 
156 1 Y 1 A ALA 485 ? A ALA 485 
157 1 Y 1 A GLU 486 ? A GLU 486 
158 1 Y 1 A ASN 487 ? A ASN 487 
159 1 Y 1 A ILE 488 ? A ILE 488 
160 1 Y 1 A PRO 489 ? A PRO 489 
161 1 Y 1 A ALA 490 ? A ALA 490 
162 1 Y 1 A VAL 491 ? A VAL 491 
163 1 Y 1 A VAL 492 ? A VAL 492 
164 1 Y 1 A ILE 493 ? A ILE 493 
165 1 Y 1 A GLU 494 ? A GLU 494 
166 1 Y 1 A ILE 495 ? A ILE 495 
167 1 Y 1 A LYS 496 ? A LYS 496 
168 1 Y 1 A ASN 497 ? A ASN 497 
169 1 Y 1 A MET 498 ? A MET 498 
170 1 Y 1 A PRO 499 ? A PRO 499 
171 1 Y 1 A ASN 500 ? A ASN 500 
172 1 Y 1 A LYS 501 ? A LYS 501 
173 1 Y 1 A GLN 502 ? A GLN 502 
174 1 Y 1 A PRO 503 ? A PRO 503 
175 1 Y 1 A GLU 504 ? A GLU 504 
176 1 Y 1 A SER 505 ? A SER 505 
177 1 Y 1 A SER 506 ? A SER 506 
178 1 Y 1 A LEU 507 ? A LEU 507 
179 1 Y 1 B MET 1   ? B MET 1   
180 1 Y 1 B GLY 2   ? B GLY 2   
181 1 Y 1 B CYS 3   ? B CYS 3   
182 1 Y 1 B TRP 4   ? B TRP 4   
183 1 Y 1 B GLY 5   ? B GLY 5   
184 1 Y 1 B ARG 6   ? B ARG 6   
185 1 Y 1 B HIS 135 ? B HIS 135 
186 1 Y 1 B HIS 136 ? B HIS 136 
187 1 Y 1 B HIS 137 ? B HIS 137 
188 1 Y 1 B SER 138 ? B SER 138 
189 1 Y 1 B GLY 139 ? B GLY 139 
190 1 Y 1 B PHE 140 ? B PHE 140 
191 1 Y 1 B SER 141 ? B SER 141 
192 1 Y 1 B GLN 142 ? B GLN 142 
193 1 Y 1 B ASP 143 ? B ASP 143 
194 1 Y 1 B SER 144 ? B SER 144 
195 1 Y 1 B GLY 145 ? B GLY 145 
196 1 Y 1 B HIS 146 ? B HIS 146 
197 1 Y 1 B GLY 147 ? B GLY 147 
198 1 Y 1 B HIS 148 ? B HIS 148 
199 1 Y 1 B SER 149 ? B SER 149 
200 1 Y 1 B HIS 150 ? B HIS 150 
201 1 Y 1 B GLY 151 ? B GLY 151 
202 1 Y 1 B GLY 152 ? B GLY 152 
203 1 Y 1 B HIS 153 ? B HIS 153 
204 1 Y 1 B GLY 154 ? B GLY 154 
205 1 Y 1 B HIS 155 ? B HIS 155 
206 1 Y 1 B GLY 156 ? B GLY 156 
207 1 Y 1 B HIS 157 ? B HIS 157 
208 1 Y 1 B GLY 158 ? B GLY 158 
209 1 Y 1 B LEU 159 ? B LEU 159 
210 1 Y 1 B PRO 160 ? B PRO 160 
211 1 Y 1 B LYS 161 ? B LYS 161 
212 1 Y 1 B GLY 162 ? B GLY 162 
213 1 Y 1 B PRO 163 ? B PRO 163 
214 1 Y 1 B ARG 164 ? B ARG 164 
215 1 Y 1 B VAL 165 ? B VAL 165 
216 1 Y 1 B LYS 166 ? B LYS 166 
217 1 Y 1 B SER 167 ? B SER 167 
218 1 Y 1 B THR 168 ? B THR 168 
219 1 Y 1 B ARG 169 ? B ARG 169 
220 1 Y 1 B PRO 170 ? B PRO 170 
221 1 Y 1 B GLY 171 ? B GLY 171 
222 1 Y 1 B SER 172 ? B SER 172 
223 1 Y 1 B SER 173 ? B SER 173 
224 1 Y 1 B ASP 174 ? B ASP 174 
225 1 Y 1 B ILE 175 ? B ILE 175 
226 1 Y 1 B ASN 176 ? B ASN 176 
227 1 Y 1 B VAL 177 ? B VAL 177 
228 1 Y 1 B ALA 178 ? B ALA 178 
229 1 Y 1 B PRO 179 ? B PRO 179 
230 1 Y 1 B GLY 180 ? B GLY 180 
231 1 Y 1 B GLU 181 ? B GLU 181 
232 1 Y 1 B GLN 182 ? B GLN 182 
233 1 Y 1 B GLY 183 ? B GLY 183 
234 1 Y 1 B PRO 184 ? B PRO 184 
235 1 Y 1 B ASP 185 ? B ASP 185 
236 1 Y 1 B GLN 186 ? B GLN 186 
237 1 Y 1 B GLU 187 ? B GLU 187 
238 1 Y 1 B GLU 188 ? B GLU 188 
239 1 Y 1 B THR 189 ? B THR 189 
240 1 Y 1 B ASN 190 ? B ASN 190 
241 1 Y 1 B THR 191 ? B THR 191 
242 1 Y 1 B LEU 192 ? B LEU 192 
243 1 Y 1 B VAL 193 ? B VAL 193 
244 1 Y 1 B ALA 194 ? B ALA 194 
245 1 Y 1 B ASN 195 ? B ASN 195 
246 1 Y 1 B THR 196 ? B THR 196 
247 1 Y 1 B SER 197 ? B SER 197 
248 1 Y 1 B ASN 198 ? B ASN 198 
249 1 Y 1 B SER 199 ? B SER 199 
250 1 Y 1 B ASN 200 ? B ASN 200 
251 1 Y 1 B GLY 201 ? B GLY 201 
252 1 Y 1 B LEU 202 ? B LEU 202 
253 1 Y 1 B LYS 203 ? B LYS 203 
254 1 Y 1 B LEU 204 ? B LEU 204 
255 1 Y 1 B ASP 205 ? B ASP 205 
256 1 Y 1 B PRO 206 ? B PRO 206 
257 1 Y 1 B ALA 207 ? B ALA 207 
258 1 Y 1 B ASP 208 ? B ASP 208 
259 1 Y 1 B PRO 209 ? B PRO 209 
260 1 Y 1 B GLU 210 ? B GLU 210 
261 1 Y 1 B ASN 211 ? B ASN 211 
262 1 Y 1 B PRO 212 ? B PRO 212 
263 1 Y 1 B ARG 213 ? B ARG 213 
264 1 Y 1 B SER 214 ? B SER 214 
265 1 Y 1 B GLY 215 ? B GLY 215 
266 1 Y 1 B ASP 216 ? B ASP 216 
267 1 Y 1 B THR 217 ? B THR 217 
268 1 Y 1 B VAL 218 ? B VAL 218 
269 1 Y 1 B GLU 219 ? B GLU 219 
270 1 Y 1 B VAL 220 ? B VAL 220 
271 1 Y 1 B GLN 221 ? B GLN 221 
272 1 Y 1 B VAL 222 ? B VAL 222 
273 1 Y 1 B ASN 223 ? B ASN 223 
274 1 Y 1 B GLY 224 ? B GLY 224 
275 1 Y 1 B ASN 225 ? B ASN 225 
276 1 Y 1 B LEU 226 ? B LEU 226 
277 1 Y 1 B VAL 227 ? B VAL 227 
278 1 Y 1 B ARG 228 ? B ARG 228 
279 1 Y 1 B GLU 229 ? B GLU 229 
280 1 Y 1 B PRO 230 ? B PRO 230 
281 1 Y 1 B ASP 231 ? B ASP 231 
282 1 Y 1 B HIS 232 ? B HIS 232 
283 1 Y 1 B MET 233 ? B MET 233 
284 1 Y 1 B GLU 234 ? B GLU 234 
285 1 Y 1 B LEU 235 ? B LEU 235 
286 1 Y 1 B GLU 236 ? B GLU 236 
287 1 Y 1 B GLU 237 ? B GLU 237 
288 1 Y 1 B ASP 238 ? B ASP 238 
289 1 Y 1 B ARG 239 ? B ARG 239 
290 1 Y 1 B ALA 240 ? B ALA 240 
291 1 Y 1 B ALA 442 ? B ALA 442 
292 1 Y 1 B LEU 443 ? B LEU 443 
293 1 Y 1 B LYS 444 ? B LYS 444 
294 1 Y 1 B GLN 445 ? B GLN 445 
295 1 Y 1 B CYS 446 ? B CYS 446 
296 1 Y 1 B CYS 447 ? B CYS 447 
297 1 Y 1 B GLY 448 ? B GLY 448 
298 1 Y 1 B THR 449 ? B THR 449 
299 1 Y 1 B LEU 450 ? B LEU 450 
300 1 Y 1 B PRO 451 ? B PRO 451 
301 1 Y 1 B GLN 452 ? B GLN 452 
302 1 Y 1 B ALA 453 ? B ALA 453 
303 1 Y 1 B PRO 454 ? B PRO 454 
304 1 Y 1 B SER 455 ? B SER 455 
305 1 Y 1 B GLY 456 ? B GLY 456 
306 1 Y 1 B LYS 457 ? B LYS 457 
307 1 Y 1 B ASP 458 ? B ASP 458 
308 1 Y 1 B ALA 459 ? B ALA 459 
309 1 Y 1 B GLU 460 ? B GLU 460 
310 1 Y 1 B LYS 461 ? B LYS 461 
311 1 Y 1 B THR 462 ? B THR 462 
312 1 Y 1 B PRO 463 ? B PRO 463 
313 1 Y 1 B ALA 464 ? B ALA 464 
314 1 Y 1 B VAL 465 ? B VAL 465 
315 1 Y 1 B SER 466 ? B SER 466 
316 1 Y 1 B ILE 467 ? B ILE 467 
317 1 Y 1 B SER 468 ? B SER 468 
318 1 Y 1 B CYS 469 ? B CYS 469 
319 1 Y 1 B LEU 470 ? B LEU 470 
320 1 Y 1 B GLU 471 ? B GLU 471 
321 1 Y 1 B LEU 472 ? B LEU 472 
322 1 Y 1 B SER 473 ? B SER 473 
323 1 Y 1 B ASN 474 ? B ASN 474 
324 1 Y 1 B ASN 475 ? B ASN 475 
325 1 Y 1 B LEU 476 ? B LEU 476 
326 1 Y 1 B GLU 477 ? B GLU 477 
327 1 Y 1 B LYS 478 ? B LYS 478 
328 1 Y 1 B LYS 479 ? B LYS 479 
329 1 Y 1 B PRO 480 ? B PRO 480 
330 1 Y 1 B ARG 481 ? B ARG 481 
331 1 Y 1 B ARG 482 ? B ARG 482 
332 1 Y 1 B THR 483 ? B THR 483 
333 1 Y 1 B LYS 484 ? B LYS 484 
334 1 Y 1 B ALA 485 ? B ALA 485 
335 1 Y 1 B GLU 486 ? B GLU 486 
336 1 Y 1 B ASN 487 ? B ASN 487 
337 1 Y 1 B ILE 488 ? B ILE 488 
338 1 Y 1 B PRO 489 ? B PRO 489 
339 1 Y 1 B ALA 490 ? B ALA 490 
340 1 Y 1 B VAL 491 ? B VAL 491 
341 1 Y 1 B VAL 492 ? B VAL 492 
342 1 Y 1 B ILE 493 ? B ILE 493 
343 1 Y 1 B GLU 494 ? B GLU 494 
344 1 Y 1 B ILE 495 ? B ILE 495 
345 1 Y 1 B LYS 496 ? B LYS 496 
346 1 Y 1 B ASN 497 ? B ASN 497 
347 1 Y 1 B MET 498 ? B MET 498 
348 1 Y 1 B PRO 499 ? B PRO 499 
349 1 Y 1 B ASN 500 ? B ASN 500 
350 1 Y 1 B LYS 501 ? B LYS 501 
351 1 Y 1 B GLN 502 ? B GLN 502 
352 1 Y 1 B PRO 503 ? B PRO 503 
353 1 Y 1 B GLU 504 ? B GLU 504 
354 1 Y 1 B SER 505 ? B SER 505 
355 1 Y 1 B SER 506 ? B SER 506 
356 1 Y 1 B LEU 507 ? B LEU 507 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
ILE N    N  N N 158 
ILE CA   C  N S 159 
ILE C    C  N N 160 
ILE O    O  N N 161 
ILE CB   C  N S 162 
ILE CG1  C  N N 163 
ILE CG2  C  N N 164 
ILE CD1  C  N N 165 
ILE OXT  O  N N 166 
ILE H    H  N N 167 
ILE H2   H  N N 168 
ILE HA   H  N N 169 
ILE HB   H  N N 170 
ILE HG12 H  N N 171 
ILE HG13 H  N N 172 
ILE HG21 H  N N 173 
ILE HG22 H  N N 174 
ILE HG23 H  N N 175 
ILE HD11 H  N N 176 
ILE HD12 H  N N 177 
ILE HD13 H  N N 178 
ILE HXT  H  N N 179 
LEU N    N  N N 180 
LEU CA   C  N S 181 
LEU C    C  N N 182 
LEU O    O  N N 183 
LEU CB   C  N N 184 
LEU CG   C  N N 185 
LEU CD1  C  N N 186 
LEU CD2  C  N N 187 
LEU OXT  O  N N 188 
LEU H    H  N N 189 
LEU H2   H  N N 190 
LEU HA   H  N N 191 
LEU HB2  H  N N 192 
LEU HB3  H  N N 193 
LEU HG   H  N N 194 
LEU HD11 H  N N 195 
LEU HD12 H  N N 196 
LEU HD13 H  N N 197 
LEU HD21 H  N N 198 
LEU HD22 H  N N 199 
LEU HD23 H  N N 200 
LEU HXT  H  N N 201 
LYS N    N  N N 202 
LYS CA   C  N S 203 
LYS C    C  N N 204 
LYS O    O  N N 205 
LYS CB   C  N N 206 
LYS CG   C  N N 207 
LYS CD   C  N N 208 
LYS CE   C  N N 209 
LYS NZ   N  N N 210 
LYS OXT  O  N N 211 
LYS H    H  N N 212 
LYS H2   H  N N 213 
LYS HA   H  N N 214 
LYS HB2  H  N N 215 
LYS HB3  H  N N 216 
LYS HG2  H  N N 217 
LYS HG3  H  N N 218 
LYS HD2  H  N N 219 
LYS HD3  H  N N 220 
LYS HE2  H  N N 221 
LYS HE3  H  N N 222 
LYS HZ1  H  N N 223 
LYS HZ2  H  N N 224 
LYS HZ3  H  N N 225 
LYS HXT  H  N N 226 
MET N    N  N N 227 
MET CA   C  N S 228 
MET C    C  N N 229 
MET O    O  N N 230 
MET CB   C  N N 231 
MET CG   C  N N 232 
MET SD   S  N N 233 
MET CE   C  N N 234 
MET OXT  O  N N 235 
MET H    H  N N 236 
MET H2   H  N N 237 
MET HA   H  N N 238 
MET HB2  H  N N 239 
MET HB3  H  N N 240 
MET HG2  H  N N 241 
MET HG3  H  N N 242 
MET HE1  H  N N 243 
MET HE2  H  N N 244 
MET HE3  H  N N 245 
MET HXT  H  N N 246 
PHE N    N  N N 247 
PHE CA   C  N S 248 
PHE C    C  N N 249 
PHE O    O  N N 250 
PHE CB   C  N N 251 
PHE CG   C  Y N 252 
PHE CD1  C  Y N 253 
PHE CD2  C  Y N 254 
PHE CE1  C  Y N 255 
PHE CE2  C  Y N 256 
PHE CZ   C  Y N 257 
PHE OXT  O  N N 258 
PHE H    H  N N 259 
PHE H2   H  N N 260 
PHE HA   H  N N 261 
PHE HB2  H  N N 262 
PHE HB3  H  N N 263 
PHE HD1  H  N N 264 
PHE HD2  H  N N 265 
PHE HE1  H  N N 266 
PHE HE2  H  N N 267 
PHE HZ   H  N N 268 
PHE HXT  H  N N 269 
PRO N    N  N N 270 
PRO CA   C  N S 271 
PRO C    C  N N 272 
PRO O    O  N N 273 
PRO CB   C  N N 274 
PRO CG   C  N N 275 
PRO CD   C  N N 276 
PRO OXT  O  N N 277 
PRO H    H  N N 278 
PRO HA   H  N N 279 
PRO HB2  H  N N 280 
PRO HB3  H  N N 281 
PRO HG2  H  N N 282 
PRO HG3  H  N N 283 
PRO HD2  H  N N 284 
PRO HD3  H  N N 285 
PRO HXT  H  N N 286 
SER N    N  N N 287 
SER CA   C  N S 288 
SER C    C  N N 289 
SER O    O  N N 290 
SER CB   C  N N 291 
SER OG   O  N N 292 
SER OXT  O  N N 293 
SER H    H  N N 294 
SER H2   H  N N 295 
SER HA   H  N N 296 
SER HB2  H  N N 297 
SER HB3  H  N N 298 
SER HG   H  N N 299 
SER HXT  H  N N 300 
THR N    N  N N 301 
THR CA   C  N S 302 
THR C    C  N N 303 
THR O    O  N N 304 
THR CB   C  N R 305 
THR OG1  O  N N 306 
THR CG2  C  N N 307 
THR OXT  O  N N 308 
THR H    H  N N 309 
THR H2   H  N N 310 
THR HA   H  N N 311 
THR HB   H  N N 312 
THR HG1  H  N N 313 
THR HG21 H  N N 314 
THR HG22 H  N N 315 
THR HG23 H  N N 316 
THR HXT  H  N N 317 
TRP N    N  N N 318 
TRP CA   C  N S 319 
TRP C    C  N N 320 
TRP O    O  N N 321 
TRP CB   C  N N 322 
TRP CG   C  Y N 323 
TRP CD1  C  Y N 324 
TRP CD2  C  Y N 325 
TRP NE1  N  Y N 326 
TRP CE2  C  Y N 327 
TRP CE3  C  Y N 328 
TRP CZ2  C  Y N 329 
TRP CZ3  C  Y N 330 
TRP CH2  C  Y N 331 
TRP OXT  O  N N 332 
TRP H    H  N N 333 
TRP H2   H  N N 334 
TRP HA   H  N N 335 
TRP HB2  H  N N 336 
TRP HB3  H  N N 337 
TRP HD1  H  N N 338 
TRP HE1  H  N N 339 
TRP HE3  H  N N 340 
TRP HZ2  H  N N 341 
TRP HZ3  H  N N 342 
TRP HH2  H  N N 343 
TRP HXT  H  N N 344 
TYR N    N  N N 345 
TYR CA   C  N S 346 
TYR C    C  N N 347 
TYR O    O  N N 348 
TYR CB   C  N N 349 
TYR CG   C  Y N 350 
TYR CD1  C  Y N 351 
TYR CD2  C  Y N 352 
TYR CE1  C  Y N 353 
TYR CE2  C  Y N 354 
TYR CZ   C  Y N 355 
TYR OH   O  N N 356 
TYR OXT  O  N N 357 
TYR H    H  N N 358 
TYR H2   H  N N 359 
TYR HA   H  N N 360 
TYR HB2  H  N N 361 
TYR HB3  H  N N 362 
TYR HD1  H  N N 363 
TYR HD2  H  N N 364 
TYR HE1  H  N N 365 
TYR HE2  H  N N 366 
TYR HH   H  N N 367 
TYR HXT  H  N N 368 
VAL N    N  N N 369 
VAL CA   C  N S 370 
VAL C    C  N N 371 
VAL O    O  N N 372 
VAL CB   C  N N 373 
VAL CG1  C  N N 374 
VAL CG2  C  N N 375 
VAL OXT  O  N N 376 
VAL H    H  N N 377 
VAL H2   H  N N 378 
VAL HA   H  N N 379 
VAL HB   H  N N 380 
VAL HG11 H  N N 381 
VAL HG12 H  N N 382 
VAL HG13 H  N N 383 
VAL HG21 H  N N 384 
VAL HG22 H  N N 385 
VAL HG23 H  N N 386 
VAL HXT  H  N N 387 
ZN  ZN   ZN N N 388 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-25 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8ZB0 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'Cryo-EM structure of human ZnT1' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         64 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K2 SUMMIT (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8ZB0 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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 7   ? 134.089 107.295 96.603  1.00 29.28  ? 7   ASN A N   1 
ATOM   2    C  CA  . ASN A 1 7   ? 134.676 106.015 96.967  1.00 29.28  ? 7   ASN A CA  1 
ATOM   3    C  C   . ASN A 1 7   ? 133.879 105.300 98.049  1.00 29.28  ? 7   ASN A C   1 
ATOM   4    O  O   . ASN A 1 7   ? 133.331 105.922 98.940  1.00 29.28  ? 7   ASN A O   1 
ATOM   5    C  CB  . ASN A 1 7   ? 136.119 106.208 97.425  1.00 29.28  ? 7   ASN A CB  1 
ATOM   6    C  CG  . ASN A 1 7   ? 137.129 105.792 96.376  1.00 29.28  ? 7   ASN A CG  1 
ATOM   7    O  OD1 . ASN A 1 7   ? 136.935 104.800 95.676  1.00 29.28  ? 7   ASN A OD1 1 
ATOM   8    N  ND2 . ASN A 1 7   ? 138.212 106.550 96.257  1.00 29.28  ? 7   ASN A ND2 1 
ATOM   9    N  N   . ARG A 1 8   ? 133.801 103.977 97.941  1.00 32.72  ? 8   ARG A N   1 
ATOM   10   C  CA  . ARG A 1 8   ? 133.200 103.177 98.998  1.00 32.72  ? 8   ARG A CA  1 
ATOM   11   C  C   . ARG A 1 8   ? 134.149 103.026 100.174 1.00 32.72  ? 8   ARG A C   1 
ATOM   12   O  O   . ARG A 1 8   ? 133.714 102.770 101.302 1.00 32.72  ? 8   ARG A O   1 
ATOM   13   C  CB  . ARG A 1 8   ? 132.817 101.804 98.454  1.00 32.72  ? 8   ARG A CB  1 
ATOM   14   C  CG  . ARG A 1 8   ? 131.368 101.650 98.076  1.00 32.72  ? 8   ARG A CG  1 
ATOM   15   C  CD  . ARG A 1 8   ? 131.103 100.260 97.536  1.00 32.72  ? 8   ARG A CD  1 
ATOM   16   N  NE  . ARG A 1 8   ? 131.135 99.241  98.578  1.00 32.72  ? 8   ARG A NE  1 
ATOM   17   C  CZ  . ARG A 1 8   ? 130.060 98.773  99.206  1.00 32.72  ? 8   ARG A CZ  1 
ATOM   18   N  NH1 . ARG A 1 8   ? 128.855 99.230  98.899  1.00 32.72  ? 8   ARG A NH1 1 
ATOM   19   N  NH2 . ARG A 1 8   ? 130.188 97.843  100.143 1.00 32.72  ? 8   ARG A NH2 1 
ATOM   20   N  N   . GLY A 1 9   ? 135.449 103.167 99.931  1.00 32.28  ? 9   GLY A N   1 
ATOM   21   C  CA  . GLY A 1 9   ? 136.407 102.985 101.004 1.00 32.28  ? 9   GLY A CA  1 
ATOM   22   C  C   . GLY A 1 9   ? 136.249 104.018 102.098 1.00 32.28  ? 9   GLY A C   1 
ATOM   23   O  O   . GLY A 1 9   ? 136.341 103.701 103.284 1.00 32.28  ? 9   GLY A O   1 
ATOM   24   N  N   . ARG A 1 10  ? 135.982 105.260 101.721 1.00 32.41  ? 10  ARG A N   1 
ATOM   25   C  CA  . ARG A 1 10  ? 135.906 106.307 102.723 1.00 32.41  ? 10  ARG A CA  1 
ATOM   26   C  C   . ARG A 1 10  ? 134.683 106.143 103.615 1.00 32.41  ? 10  ARG A C   1 
ATOM   27   O  O   . ARG A 1 10  ? 134.802 106.172 104.845 1.00 32.41  ? 10  ARG A O   1 
ATOM   28   C  CB  . ARG A 1 10  ? 135.929 107.655 102.032 1.00 32.41  ? 10  ARG A CB  1 
ATOM   29   C  CG  . ARG A 1 10  ? 137.168 107.788 101.212 1.00 32.41  ? 10  ARG A CG  1 
ATOM   30   C  CD  . ARG A 1 10  ? 137.308 109.133 100.602 1.00 32.41  ? 10  ARG A CD  1 
ATOM   31   N  NE  . ARG A 1 10  ? 138.710 109.416 100.365 1.00 32.41  ? 10  ARG A NE  1 
ATOM   32   C  CZ  . ARG A 1 10  ? 139.156 110.542 99.837  1.00 32.41  ? 10  ARG A CZ  1 
ATOM   33   N  NH1 . ARG A 1 10  ? 138.304 111.487 99.484  1.00 32.41  ? 10  ARG A NH1 1 
ATOM   34   N  NH2 . ARG A 1 10  ? 140.452 110.722 99.660  1.00 32.41  ? 10  ARG A NH2 1 
ATOM   35   N  N   . LEU A 1 11  ? 133.501 105.959 103.025 1.00 32.29  ? 11  LEU A N   1 
ATOM   36   C  CA  . LEU A 1 11  ? 132.308 105.749 103.838 1.00 32.29  ? 11  LEU A CA  1 
ATOM   37   C  C   . LEU A 1 11  ? 132.394 104.459 104.640 1.00 32.29  ? 11  LEU A C   1 
ATOM   38   O  O   . LEU A 1 11  ? 131.859 104.391 105.747 1.00 32.29  ? 11  LEU A O   1 
ATOM   39   C  CB  . LEU A 1 11  ? 131.062 105.746 102.964 1.00 32.29  ? 11  LEU A CB  1 
ATOM   40   C  CG  . LEU A 1 11  ? 130.955 107.000 102.111 1.00 32.29  ? 11  LEU A CG  1 
ATOM   41   C  CD1 . LEU A 1 11  ? 129.692 106.998 101.289 1.00 32.29  ? 11  LEU A CD1 1 
ATOM   42   C  CD2 . LEU A 1 11  ? 131.015 108.205 102.996 1.00 32.29  ? 11  LEU A CD2 1 
ATOM   43   N  N   . LEU A 1 12  ? 133.081 103.438 104.122 1.00 31.81  ? 12  LEU A N   1 
ATOM   44   C  CA  . LEU A 1 12  ? 133.272 102.222 104.904 1.00 31.81  ? 12  LEU A CA  1 
ATOM   45   C  C   . LEU A 1 12  ? 134.142 102.479 106.124 1.00 31.81  ? 12  LEU A C   1 
ATOM   46   O  O   . LEU A 1 12  ? 133.796 102.072 107.241 1.00 31.81  ? 12  LEU A O   1 
ATOM   47   C  CB  . LEU A 1 12  ? 133.881 101.138 104.034 1.00 31.81  ? 12  LEU A CB  1 
ATOM   48   C  CG  . LEU A 1 12  ? 132.781 100.290 103.442 1.00 31.81  ? 12  LEU A CG  1 
ATOM   49   C  CD1 . LEU A 1 12  ? 133.370 99.258  102.535 1.00 31.81  ? 12  LEU A CD1 1 
ATOM   50   C  CD2 . LEU A 1 12  ? 132.014 99.648  104.558 1.00 31.81  ? 12  LEU A CD2 1 
ATOM   51   N  N   . CYS A 1 13  ? 135.274 103.157 105.937 1.00 35.25  ? 13  CYS A N   1 
ATOM   52   C  CA  . CYS A 1 13  ? 136.122 103.485 107.076 1.00 35.25  ? 13  CYS A CA  1 
ATOM   53   C  C   . CYS A 1 13  ? 135.365 104.310 108.104 1.00 35.25  ? 13  CYS A C   1 
ATOM   54   O  O   . CYS A 1 13  ? 135.446 104.042 109.308 1.00 35.25  ? 13  CYS A O   1 
ATOM   55   C  CB  . CYS A 1 13  ? 137.360 104.235 106.609 1.00 35.25  ? 13  CYS A CB  1 
ATOM   56   S  SG  . CYS A 1 13  ? 138.219 105.100 107.926 1.00 35.25  ? 13  CYS A SG  1 
ATOM   57   N  N   . MET A 1 14  ? 134.602 105.302 107.650 1.00 34.98  ? 14  MET A N   1 
ATOM   58   C  CA  . MET A 1 14  ? 133.913 106.172 108.596 1.00 34.98  ? 14  MET A CA  1 
ATOM   59   C  C   . MET A 1 14  ? 132.774 105.447 109.305 1.00 34.98  ? 14  MET A C   1 
ATOM   60   O  O   . MET A 1 14  ? 132.509 105.702 110.489 1.00 34.98  ? 14  MET A O   1 
ATOM   61   C  CB  . MET A 1 14  ? 133.399 107.417 107.893 1.00 34.98  ? 14  MET A CB  1 
ATOM   62   C  CG  . MET A 1 14  ? 132.846 108.427 108.847 1.00 34.98  ? 14  MET A CG  1 
ATOM   63   S  SD  . MET A 1 14  ? 134.001 108.809 110.153 1.00 34.98  ? 14  MET A SD  1 
ATOM   64   C  CE  . MET A 1 14  ? 132.908 109.610 111.299 1.00 34.98  ? 14  MET A CE  1 
ATOM   65   N  N   . LEU A 1 15  ? 132.086 104.541 108.610 1.00 33.61  ? 15  LEU A N   1 
ATOM   66   C  CA  . LEU A 1 15  ? 131.068 103.734 109.269 1.00 33.61  ? 15  LEU A CA  1 
ATOM   67   C  C   . LEU A 1 15  ? 131.692 102.865 110.353 1.00 33.61  ? 15  LEU A C   1 
ATOM   68   O  O   . LEU A 1 15  ? 131.149 102.733 111.462 1.00 33.61  ? 15  LEU A O   1 
ATOM   69   C  CB  . LEU A 1 15  ? 130.338 102.889 108.233 1.00 33.61  ? 15  LEU A CB  1 
ATOM   70   C  CG  . LEU A 1 15  ? 129.324 101.921 108.812 1.00 33.61  ? 15  LEU A CG  1 
ATOM   71   C  CD1 . LEU A 1 15  ? 128.397 102.696 109.679 1.00 33.61  ? 15  LEU A CD1 1 
ATOM   72   C  CD2 . LEU A 1 15  ? 128.547 101.222 107.720 1.00 33.61  ? 15  LEU A CD2 1 
ATOM   73   N  N   . ALA A 1 16  ? 132.856 102.288 110.061 1.00 34.62  ? 16  ALA A N   1 
ATOM   74   C  CA  . ALA A 1 16  ? 133.555 101.513 111.076 1.00 34.62  ? 16  ALA A CA  1 
ATOM   75   C  C   . ALA A 1 16  ? 133.939 102.380 112.264 1.00 34.62  ? 16  ALA A C   1 
ATOM   76   O  O   . ALA A 1 16  ? 133.811 101.956 113.420 1.00 34.62  ? 16  ALA A O   1 
ATOM   77   C  CB  . ALA A 1 16  ? 134.791 100.857 110.479 1.00 34.62  ? 16  ALA A CB  1 
ATOM   78   N  N   . LEU A 1 17  ? 134.398 103.603 112.010 1.00 35.19  ? 17  LEU A N   1 
ATOM   79   C  CA  . LEU A 1 17  ? 134.773 104.473 113.121 1.00 35.19  ? 17  LEU A CA  1 
ATOM   80   C  C   . LEU A 1 17  ? 133.585 104.797 114.018 1.00 35.19  ? 17  LEU A C   1 
ATOM   81   O  O   . LEU A 1 17  ? 133.703 104.752 115.249 1.00 35.19  ? 17  LEU A O   1 
ATOM   82   C  CB  . LEU A 1 17  ? 135.394 105.757 112.606 1.00 35.19  ? 17  LEU A CB  1 
ATOM   83   C  CG  . LEU A 1 17  ? 136.902 105.682 112.668 1.00 35.19  ? 17  LEU A CG  1 
ATOM   84   C  CD1 . LEU A 1 17  ? 137.497 106.997 112.274 1.00 35.19  ? 17  LEU A CD1 1 
ATOM   85   C  CD2 . LEU A 1 17  ? 137.318 105.297 114.060 1.00 35.19  ? 17  LEU A CD2 1 
ATOM   86   N  N   . THR A 1 18  ? 132.434 105.135 113.435 1.00 33.31  ? 18  THR A N   1 
ATOM   87   C  CA  . THR A 1 18  ? 131.304 105.480 114.292 1.00 33.31  ? 18  THR A CA  1 
ATOM   88   C  C   . THR A 1 18  ? 130.823 104.278 115.093 1.00 33.31  ? 18  THR A C   1 
ATOM   89   O  O   . THR A 1 18  ? 130.439 104.429 116.258 1.00 33.31  ? 18  THR A O   1 
ATOM   90   C  CB  . THR A 1 18  ? 130.159 106.068 113.494 1.00 33.31  ? 18  THR A CB  1 
ATOM   91   O  OG1 . THR A 1 18  ? 129.562 105.046 112.701 1.00 33.31  ? 18  THR A OG1 1 
ATOM   92   C  CG2 . THR A 1 18  ? 130.669 107.163 112.614 1.00 33.31  ? 18  THR A CG2 1 
ATOM   93   N  N   . PHE A 1 19  ? 130.823 103.073 114.509 1.00 38.06  ? 19  PHE A N   1 
ATOM   94   C  CA  . PHE A 1 19  ? 130.507 101.914 115.347 1.00 38.06  ? 19  PHE A CA  1 
ATOM   95   C  C   . PHE A 1 19  ? 131.493 101.776 116.496 1.00 38.06  ? 19  PHE A C   1 
ATOM   96   O  O   . PHE A 1 19  ? 131.097 101.466 117.629 1.00 38.06  ? 19  PHE A O   1 
ATOM   97   C  CB  . PHE A 1 19  ? 130.470 100.627 114.537 1.00 38.06  ? 19  PHE A CB  1 
ATOM   98   C  CG  . PHE A 1 19  ? 129.165 100.379 113.871 1.00 38.06  ? 19  PHE A CG  1 
ATOM   99   C  CD1 . PHE A 1 19  ? 128.045 101.077 114.247 1.00 38.06  ? 19  PHE A CD1 1 
ATOM   100  C  CD2 . PHE A 1 19  ? 129.047 99.425  112.884 1.00 38.06  ? 19  PHE A CD2 1 
ATOM   101  C  CE1 . PHE A 1 19  ? 126.833 100.841 113.638 1.00 38.06  ? 19  PHE A CE1 1 
ATOM   102  C  CE2 . PHE A 1 19  ? 127.837 99.186  112.271 1.00 38.06  ? 19  PHE A CE2 1 
ATOM   103  C  CZ  . PHE A 1 19  ? 126.730 99.893  112.651 1.00 38.06  ? 19  PHE A CZ  1 
ATOM   104  N  N   . MET A 1 20  ? 132.779 102.011 116.234 1.00 38.79  ? 20  MET A N   1 
ATOM   105  C  CA  . MET A 1 20  ? 133.745 101.967 117.324 1.00 38.79  ? 20  MET A CA  1 
ATOM   106  C  C   . MET A 1 20  ? 133.351 102.929 118.432 1.00 38.79  ? 20  MET A C   1 
ATOM   107  O  O   . MET A 1 20  ? 133.369 102.569 119.618 1.00 38.79  ? 20  MET A O   1 
ATOM   108  C  CB  . MET A 1 20  ? 135.145 102.301 116.820 1.00 38.79  ? 20  MET A CB  1 
ATOM   109  C  CG  . MET A 1 20  ? 136.238 102.139 117.869 1.00 38.79  ? 20  MET A CG  1 
ATOM   110  S  SD  . MET A 1 20  ? 136.414 103.495 119.059 1.00 38.79  ? 20  MET A SD  1 
ATOM   111  C  CE  . MET A 1 20  ? 137.176 104.774 118.077 1.00 38.79  ? 20  MET A CE  1 
ATOM   112  N  N   . PHE A 1 21  ? 132.981 104.154 118.073 1.00 38.10  ? 21  PHE A N   1 
ATOM   113  C  CA  . PHE A 1 21  ? 132.721 105.125 119.128 1.00 38.10  ? 21  PHE A CA  1 
ATOM   114  C  C   . PHE A 1 21  ? 131.445 104.801 119.891 1.00 38.10  ? 21  PHE A C   1 
ATOM   115  O  O   . PHE A 1 21  ? 131.365 105.046 121.098 1.00 38.10  ? 21  PHE A O   1 
ATOM   116  C  CB  . PHE A 1 21  ? 132.642 106.542 118.597 1.00 38.10  ? 21  PHE A CB  1 
ATOM   117  C  CG  . PHE A 1 21  ? 132.570 107.554 119.690 1.00 38.10  ? 21  PHE A CG  1 
ATOM   118  C  CD1 . PHE A 1 21  ? 133.709 107.929 120.371 1.00 38.10  ? 21  PHE A CD1 1 
ATOM   119  C  CD2 . PHE A 1 21  ? 131.362 108.074 120.096 1.00 38.10  ? 21  PHE A CD2 1 
ATOM   120  C  CE1 . PHE A 1 21  ? 133.651 108.837 121.398 1.00 38.10  ? 21  PHE A CE1 1 
ATOM   121  C  CE2 . PHE A 1 21  ? 131.301 108.983 121.131 1.00 38.10  ? 21  PHE A CE2 1 
ATOM   122  C  CZ  . PHE A 1 21  ? 132.447 109.360 121.778 1.00 38.10  ? 21  PHE A CZ  1 
ATOM   123  N  N   . MET A 1 22  ? 130.429 104.269 119.219 1.00 40.84  ? 22  MET A N   1 
ATOM   124  C  CA  . MET A 1 22  ? 129.231 103.878 119.956 1.00 40.84  ? 22  MET A CA  1 
ATOM   125  C  C   . MET A 1 22  ? 129.542 102.787 120.968 1.00 40.84  ? 22  MET A C   1 
ATOM   126  O  O   . MET A 1 22  ? 129.013 102.793 122.087 1.00 40.84  ? 22  MET A O   1 
ATOM   127  C  CB  . MET A 1 22  ? 128.143 103.412 119.003 1.00 40.84  ? 22  MET A CB  1 
ATOM   128  C  CG  . MET A 1 22  ? 127.249 104.506 118.541 1.00 40.84  ? 22  MET A CG  1 
ATOM   129  S  SD  . MET A 1 22  ? 126.098 103.914 117.301 1.00 40.84  ? 22  MET A SD  1 
ATOM   130  C  CE  . MET A 1 22  ? 125.785 102.268 117.923 1.00 40.84  ? 22  MET A CE  1 
ATOM   131  N  N   . VAL A 1 23  ? 130.393 101.831 120.594 1.00 41.46  ? 23  VAL A N   1 
ATOM   132  C  CA  . VAL A 1 23  ? 130.761 100.795 121.553 1.00 41.46  ? 23  VAL A CA  1 
ATOM   133  C  C   . VAL A 1 23  ? 131.502 101.398 122.734 1.00 41.46  ? 23  VAL A C   1 
ATOM   134  O  O   . VAL A 1 23  ? 131.243 101.044 123.889 1.00 41.46  ? 23  VAL A O   1 
ATOM   135  C  CB  . VAL A 1 23  ? 131.575 99.687  120.878 1.00 41.46  ? 23  VAL A CB  1 
ATOM   136  C  CG1 . VAL A 1 23  ? 132.260 98.857  121.924 1.00 41.46  ? 23  VAL A CG1 1 
ATOM   137  C  CG2 . VAL A 1 23  ? 130.643 98.804  120.068 1.00 41.46  ? 23  VAL A CG2 1 
ATOM   138  N  N   . LEU A 1 24  ? 132.429 102.322 122.472 1.00 43.66  ? 24  LEU A N   1 
ATOM   139  C  CA  . LEU A 1 24  ? 133.110 102.989 123.588 1.00 43.66  ? 24  LEU A CA  1 
ATOM   140  C  C   . LEU A 1 24  ? 132.120 103.713 124.495 1.00 43.66  ? 24  LEU A C   1 
ATOM   141  O  O   . LEU A 1 24  ? 132.274 103.721 125.725 1.00 43.66  ? 24  LEU A O   1 
ATOM   142  C  CB  . LEU A 1 24  ? 134.154 103.976 123.083 1.00 43.66  ? 24  LEU A CB  1 
ATOM   143  C  CG  . LEU A 1 24  ? 134.488 105.060 124.105 1.00 43.66  ? 24  LEU A CG  1 
ATOM   144  C  CD1 . LEU A 1 24  ? 135.392 104.509 125.166 1.00 43.66  ? 24  LEU A CD1 1 
ATOM   145  C  CD2 . LEU A 1 24  ? 135.119 106.250 123.447 1.00 43.66  ? 24  LEU A CD2 1 
ATOM   146  N  N   . GLU A 1 25  ? 131.092 104.318 123.910 1.00 44.80  ? 25  GLU A N   1 
ATOM   147  C  CA  . GLU A 1 25  ? 130.131 105.046 124.725 1.00 44.80  ? 25  GLU A CA  1 
ATOM   148  C  C   . GLU A 1 25  ? 129.318 104.106 125.602 1.00 44.80  ? 25  GLU A C   1 
ATOM   149  O  O   . GLU A 1 25  ? 129.103 104.395 126.781 1.00 44.80  ? 25  GLU A O   1 
ATOM   150  C  CB  . GLU A 1 25  ? 129.204 105.869 123.852 1.00 44.80  ? 25  GLU A CB  1 
ATOM   151  C  CG  . GLU A 1 25  ? 128.594 107.019 124.577 1.00 44.80  ? 25  GLU A CG  1 
ATOM   152  C  CD  . GLU A 1 25  ? 127.744 107.853 123.671 1.00 44.80  ? 25  GLU A CD  1 
ATOM   153  O  OE1 . GLU A 1 25  ? 126.758 107.318 123.152 1.00 44.80  ? 25  GLU A OE1 1 
ATOM   154  O  OE2 . GLU A 1 25  ? 128.074 109.029 123.444 1.00 44.80  ? 25  GLU A OE2 1 
ATOM   155  N  N   . VAL A 1 26  ? 128.836 102.989 125.055 1.00 45.44  ? 26  VAL A N   1 
ATOM   156  C  CA  . VAL A 1 26  ? 128.120 102.037 125.905 1.00 45.44  ? 26  VAL A CA  1 
ATOM   157  C  C   . VAL A 1 26  ? 129.034 101.521 127.006 1.00 45.44  ? 26  VAL A C   1 
ATOM   158  O  O   . VAL A 1 26  ? 128.606 101.333 128.151 1.00 45.44  ? 26  VAL A O   1 
ATOM   159  C  CB  . VAL A 1 26  ? 127.535 100.879 125.081 1.00 45.44  ? 26  VAL A CB  1 
ATOM   160  C  CG1 . VAL A 1 26  ? 127.316 99.680  125.965 1.00 45.44  ? 26  VAL A CG1 1 
ATOM   161  C  CG2 . VAL A 1 26  ? 126.226 101.273 124.479 1.00 45.44  ? 26  VAL A CG2 1 
ATOM   162  N  N   . VAL A 1 27  ? 130.309 101.294 126.684 1.00 46.08  ? 27  VAL A N   1 
ATOM   163  C  CA  . VAL A 1 27  ? 131.256 100.803 127.683 1.00 46.08  ? 27  VAL A CA  1 
ATOM   164  C  C   . VAL A 1 27  ? 131.385 101.788 128.835 1.00 46.08  ? 27  VAL A C   1 
ATOM   165  O  O   . VAL A 1 27  ? 131.352 101.399 130.006 1.00 46.08  ? 27  VAL A O   1 
ATOM   166  C  CB  . VAL A 1 27  ? 132.620 100.514 127.040 1.00 46.08  ? 27  VAL A CB  1 
ATOM   167  C  CG1 . VAL A 1 27  ? 133.726 100.618 128.070 1.00 46.08  ? 27  VAL A CG1 1 
ATOM   168  C  CG2 . VAL A 1 27  ? 132.603 99.137  126.416 1.00 46.08  ? 27  VAL A CG2 1 
ATOM   169  N  N   . VAL A 1 28  ? 131.536 103.076 128.532 1.00 47.14  ? 28  VAL A N   1 
ATOM   170  C  CA  . VAL A 1 28  ? 131.629 104.041 129.625 1.00 47.14  ? 28  VAL A CA  1 
ATOM   171  C  C   . VAL A 1 28  ? 130.310 104.121 130.386 1.00 47.14  ? 28  VAL A C   1 
ATOM   172  O  O   . VAL A 1 28  ? 130.291 104.172 131.622 1.00 47.14  ? 28  VAL A O   1 
ATOM   173  C  CB  . VAL A 1 28  ? 132.077 105.418 129.110 1.00 47.14  ? 28  VAL A CB  1 
ATOM   174  C  CG1 . VAL A 1 28  ? 131.651 106.490 130.063 1.00 47.14  ? 28  VAL A CG1 1 
ATOM   175  C  CG2 . VAL A 1 28  ? 133.571 105.453 128.989 1.00 47.14  ? 28  VAL A CG2 1 
ATOM   176  N  N   . SER A 1 29  ? 129.186 104.103 129.671 1.00 50.53  ? 29  SER A N   1 
ATOM   177  C  CA  . SER A 1 29  ? 127.891 104.239 130.327 1.00 50.53  ? 29  SER A CA  1 
ATOM   178  C  C   . SER A 1 29  ? 127.635 103.095 131.288 1.00 50.53  ? 29  SER A C   1 
ATOM   179  O  O   . SER A 1 29  ? 126.913 103.250 132.275 1.00 50.53  ? 29  SER A O   1 
ATOM   180  C  CB  . SER A 1 29  ? 126.777 104.306 129.290 1.00 50.53  ? 29  SER A CB  1 
ATOM   181  O  OG  . SER A 1 29  ? 126.611 105.624 128.807 1.00 50.53  ? 29  SER A OG  1 
ATOM   182  N  N   . ARG A 1 30  ? 128.193 101.929 130.997 1.00 51.47  ? 30  ARG A N   1 
ATOM   183  C  CA  . ARG A 1 30  ? 127.981 100.761 131.895 1.00 51.47  ? 30  ARG A CA  1 
ATOM   184  C  C   . ARG A 1 30  ? 129.048 100.765 132.993 1.00 51.47  ? 30  ARG A C   1 
ATOM   185  O  O   . ARG A 1 30  ? 128.721 100.346 134.115 1.00 51.47  ? 30  ARG A O   1 
ATOM   186  C  CB  . ARG A 1 30  ? 127.965 99.444  131.113 1.00 51.47  ? 30  ARG A CB  1 
ATOM   187  C  CG  . ARG A 1 30  ? 126.961 98.432  131.644 1.00 51.47  ? 30  ARG A CG  1 
ATOM   188  C  CD  . ARG A 1 30  ? 125.756 98.286  130.736 1.00 51.47  ? 30  ARG A CD  1 
ATOM   189  N  NE  . ARG A 1 30  ? 125.816 97.063  129.950 1.00 51.47  ? 30  ARG A NE  1 
ATOM   190  C  CZ  . ARG A 1 30  ? 124.934 96.722  129.019 1.00 51.47  ? 30  ARG A CZ  1 
ATOM   191  N  NH1 . ARG A 1 30  ? 124.334 97.656  128.303 1.00 51.47  ? 30  ARG A NH1 1 
ATOM   192  N  NH2 . ARG A 1 30  ? 124.656 95.449  128.807 1.00 51.47  ? 30  ARG A NH2 1 
ATOM   193  N  N   . VAL A 1 31  ? 130.266 101.204 132.704 1.00 52.83  ? 31  VAL A N   1 
ATOM   194  C  CA  . VAL A 1 31  ? 131.275 101.241 133.757 1.00 52.83  ? 31  VAL A CA  1 
ATOM   195  C  C   . VAL A 1 31  ? 130.874 102.230 134.841 1.00 52.83  ? 31  VAL A C   1 
ATOM   196  O  O   . VAL A 1 31  ? 130.793 101.881 136.023 1.00 52.83  ? 31  VAL A O   1 
ATOM   197  C  CB  . VAL A 1 31  ? 132.655 101.583 133.175 1.00 52.83  ? 31  VAL A CB  1 
ATOM   198  C  CG1 . VAL A 1 31  ? 133.554 102.147 134.251 1.00 52.83  ? 31  VAL A CG1 1 
ATOM   199  C  CG2 . VAL A 1 31  ? 133.281 100.354 132.581 1.00 52.83  ? 31  VAL A CG2 1 
ATOM   200  N  N   . THR A 1 32  ? 130.609 103.478 134.456 1.00 53.91  ? 32  THR A N   1 
ATOM   201  C  CA  . THR A 1 32  ? 130.254 104.517 135.415 1.00 53.91  ? 32  THR A CA  1 
ATOM   202  C  C   . THR A 1 32  ? 128.944 104.230 136.141 1.00 53.91  ? 32  THR A C   1 
ATOM   203  O  O   . THR A 1 32  ? 128.727 104.764 137.234 1.00 53.91  ? 32  THR A O   1 
ATOM   204  C  CB  . THR A 1 32  ? 130.198 105.855 134.674 1.00 53.91  ? 32  THR A CB  1 
ATOM   205  O  OG1 . THR A 1 32  ? 131.515 106.203 134.240 1.00 53.91  ? 32  THR A OG1 1 
ATOM   206  C  CG2 . THR A 1 32  ? 129.674 106.961 135.541 1.00 53.91  ? 32  THR A CG2 1 
ATOM   207  N  N   . SER A 1 33  ? 128.101 103.359 135.592 1.00 57.73  ? 33  SER A N   1 
ATOM   208  C  CA  . SER A 1 33  ? 126.769 103.072 136.121 1.00 57.73  ? 33  SER A CA  1 
ATOM   209  C  C   . SER A 1 33  ? 125.925 104.344 136.157 1.00 57.73  ? 33  SER A C   1 
ATOM   210  O  O   . SER A 1 33  ? 125.386 104.747 137.187 1.00 57.73  ? 33  SER A O   1 
ATOM   211  C  CB  . SER A 1 33  ? 126.848 102.413 137.499 1.00 57.73  ? 33  SER A CB  1 
ATOM   212  O  OG  . SER A 1 33  ? 127.055 101.019 137.375 1.00 57.73  ? 33  SER A OG  1 
ATOM   213  N  N   . SER A 1 34  ? 125.815 104.970 134.987 1.00 57.42  ? 34  SER A N   1 
ATOM   214  C  CA  . SER A 1 34  ? 125.080 106.222 134.826 1.00 57.42  ? 34  SER A CA  1 
ATOM   215  C  C   . SER A 1 34  ? 124.128 106.049 133.648 1.00 57.42  ? 34  SER A C   1 
ATOM   216  O  O   . SER A 1 34  ? 124.467 106.401 132.517 1.00 57.42  ? 34  SER A O   1 
ATOM   217  C  CB  . SER A 1 34  ? 126.030 107.390 134.604 1.00 57.42  ? 34  SER A CB  1 
ATOM   218  O  OG  . SER A 1 34  ? 126.392 107.500 133.244 1.00 57.42  ? 34  SER A OG  1 
ATOM   219  N  N   . LEU A 1 35  ? 122.927 105.539 133.925 1.00 59.95  ? 35  LEU A N   1 
ATOM   220  C  CA  . LEU A 1 35  ? 121.944 105.273 132.882 1.00 59.95  ? 35  LEU A CA  1 
ATOM   221  C  C   . LEU A 1 35  ? 121.466 106.527 132.179 1.00 59.95  ? 35  LEU A C   1 
ATOM   222  O  O   . LEU A 1 35  ? 120.618 106.426 131.290 1.00 59.95  ? 35  LEU A O   1 
ATOM   223  C  CB  . LEU A 1 35  ? 120.732 104.550 133.459 1.00 59.95  ? 35  LEU A CB  1 
ATOM   224  C  CG  . LEU A 1 35  ? 120.765 103.022 133.492 1.00 59.95  ? 35  LEU A CG  1 
ATOM   225  C  CD1 . LEU A 1 35  ? 119.374 102.483 133.782 1.00 59.95  ? 35  LEU A CD1 1 
ATOM   226  C  CD2 . LEU A 1 35  ? 121.320 102.435 132.199 1.00 59.95  ? 35  LEU A CD2 1 
ATOM   227  N  N   . ALA A 1 36  ? 121.950 107.699 132.569 1.00 59.71  ? 36  ALA A N   1 
ATOM   228  C  CA  . ALA A 1 36  ? 121.595 108.911 131.848 1.00 59.71  ? 36  ALA A CA  1 
ATOM   229  C  C   . ALA A 1 36  ? 122.536 109.167 130.683 1.00 59.71  ? 36  ALA A C   1 
ATOM   230  O  O   . ALA A 1 36  ? 122.293 110.076 129.885 1.00 59.71  ? 36  ALA A O   1 
ATOM   231  C  CB  . ALA A 1 36  ? 121.587 110.107 132.798 1.00 59.71  ? 36  ALA A CB  1 
ATOM   232  N  N   . MET A 1 37  ? 123.617 108.401 130.582 1.00 53.66  ? 37  MET A N   1 
ATOM   233  C  CA  . MET A 1 37  ? 124.560 108.561 129.487 1.00 53.66  ? 37  MET A CA  1 
ATOM   234  C  C   . MET A 1 37  ? 124.416 107.488 128.416 1.00 53.66  ? 37  MET A C   1 
ATOM   235  O  O   . MET A 1 37  ? 124.778 107.733 127.264 1.00 53.66  ? 37  MET A O   1 
ATOM   236  C  CB  . MET A 1 37  ? 125.986 108.562 130.027 1.00 53.66  ? 37  MET A CB  1 
ATOM   237  C  CG  . MET A 1 37  ? 127.031 108.834 128.977 1.00 53.66  ? 37  MET A CG  1 
ATOM   238  S  SD  . MET A 1 37  ? 128.685 108.972 129.650 1.00 53.66  ? 37  MET A SD  1 
ATOM   239  C  CE  . MET A 1 37  ? 129.605 108.658 128.166 1.00 53.66  ? 37  MET A CE  1 
ATOM   240  N  N   . LEU A 1 38  ? 123.898 106.311 128.760 1.00 55.60  ? 38  LEU A N   1 
ATOM   241  C  CA  . LEU A 1 38  ? 123.556 105.307 127.762 1.00 55.60  ? 38  LEU A CA  1 
ATOM   242  C  C   . LEU A 1 38  ? 122.555 105.824 126.739 1.00 55.60  ? 38  LEU A C   1 
ATOM   243  O  O   . LEU A 1 38  ? 122.348 105.170 125.718 1.00 55.60  ? 38  LEU A O   1 
ATOM   244  C  CB  . LEU A 1 38  ? 122.996 104.068 128.460 1.00 55.60  ? 38  LEU A CB  1 
ATOM   245  C  CG  . LEU A 1 38  ? 122.753 102.752 127.727 1.00 55.60  ? 38  LEU A CG  1 
ATOM   246  C  CD1 . LEU A 1 38  ? 122.973 101.608 128.684 1.00 55.60  ? 38  LEU A CD1 1 
ATOM   247  C  CD2 . LEU A 1 38  ? 121.353 102.683 127.179 1.00 55.60  ? 38  LEU A CD2 1 
ATOM   248  N  N   . SER A 1 39  ? 121.944 106.983 126.978 1.00 53.37  ? 39  SER A N   1 
ATOM   249  C  CA  . SER A 1 39  ? 121.002 107.582 126.046 1.00 53.37  ? 39  SER A CA  1 
ATOM   250  C  C   . SER A 1 39  ? 121.668 108.485 125.024 1.00 53.37  ? 39  SER A C   1 
ATOM   251  O  O   . SER A 1 39  ? 121.037 109.443 124.573 1.00 53.37  ? 39  SER A O   1 
ATOM   252  C  CB  . SER A 1 39  ? 119.937 108.356 126.811 1.00 53.37  ? 39  SER A CB  1 
ATOM   253  O  OG  . SER A 1 39  ? 119.209 107.483 127.653 1.00 53.37  ? 39  SER A OG  1 
ATOM   254  N  N   . ASP A 1 40  ? 122.929 108.234 124.687 1.00 50.85  ? 40  ASP A N   1 
ATOM   255  C  CA  . ASP A 1 40  ? 123.566 108.763 123.488 1.00 50.85  ? 40  ASP A CA  1 
ATOM   256  C  C   . ASP A 1 40  ? 124.055 107.666 122.546 1.00 50.85  ? 40  ASP A C   1 
ATOM   257  O  O   . ASP A 1 40  ? 124.173 107.894 121.330 1.00 50.85  ? 40  ASP A O   1 
ATOM   258  C  CB  . ASP A 1 40  ? 124.742 109.671 123.870 1.00 50.85  ? 40  ASP A CB  1 
ATOM   259  C  CG  . ASP A 1 40  ? 124.331 110.789 124.819 1.00 50.85  ? 40  ASP A CG  1 
ATOM   260  O  OD1 . ASP A 1 40  ? 123.119 111.027 124.969 1.00 50.85  ? 40  ASP A OD1 1 
ATOM   261  O  OD2 . ASP A 1 40  ? 125.222 111.426 125.426 1.00 50.85  ? 40  ASP A OD2 1 
ATOM   262  N  N   . SER A 1 41  ? 124.354 106.483 123.081 1.00 49.13  ? 41  SER A N   1 
ATOM   263  C  CA  . SER A 1 41  ? 124.675 105.339 122.242 1.00 49.13  ? 41  SER A CA  1 
ATOM   264  C  C   . SER A 1 41  ? 123.466 104.844 121.477 1.00 49.13  ? 41  SER A C   1 
ATOM   265  O  O   . SER A 1 41  ? 123.579 103.913 120.678 1.00 49.13  ? 41  SER A O   1 
ATOM   266  C  CB  . SER A 1 41  ? 125.241 104.218 123.090 1.00 49.13  ? 41  SER A CB  1 
ATOM   267  O  OG  . SER A 1 41  ? 124.243 103.698 123.941 1.00 49.13  ? 41  SER A OG  1 
ATOM   268  N  N   . PHE A 1 42  ? 122.296 105.387 121.754 1.00 46.08  ? 42  PHE A N   1 
ATOM   269  C  CA  . PHE A 1 42  ? 121.158 105.183 120.886 1.00 46.08  ? 42  PHE A CA  1 
ATOM   270  C  C   . PHE A 1 42  ? 120.927 106.373 119.973 1.00 46.08  ? 42  PHE A C   1 
ATOM   271  O  O   . PHE A 1 42  ? 120.166 106.262 119.013 1.00 46.08  ? 42  PHE A O   1 
ATOM   272  C  CB  . PHE A 1 42  ? 119.905 104.892 121.715 1.00 46.08  ? 42  PHE A CB  1 
ATOM   273  C  CG  . PHE A 1 42  ? 119.883 103.515 122.319 1.00 46.08  ? 42  PHE A CG  1 
ATOM   274  C  CD1 . PHE A 1 42  ? 119.535 103.330 123.644 1.00 46.08  ? 42  PHE A CD1 1 
ATOM   275  C  CD2 . PHE A 1 42  ? 120.231 102.407 121.564 1.00 46.08  ? 42  PHE A CD2 1 
ATOM   276  C  CE1 . PHE A 1 42  ? 119.526 102.065 124.202 1.00 46.08  ? 42  PHE A CE1 1 
ATOM   277  C  CE2 . PHE A 1 42  ? 120.220 101.137 122.119 1.00 46.08  ? 42  PHE A CE2 1 
ATOM   278  C  CZ  . PHE A 1 42  ? 119.870 100.968 123.439 1.00 46.08  ? 42  PHE A CZ  1 
ATOM   279  N  N   . HIS A 1 43  ? 121.574 107.502 120.243 1.00 43.49  ? 43  HIS A N   1 
ATOM   280  C  CA  . HIS A 1 43  ? 121.427 108.696 119.424 1.00 43.49  ? 43  HIS A CA  1 
ATOM   281  C  C   . HIS A 1 43  ? 122.472 108.783 118.322 1.00 43.49  ? 43  HIS A C   1 
ATOM   282  O  O   . HIS A 1 43  ? 122.391 109.673 117.471 1.00 43.49  ? 43  HIS A O   1 
ATOM   283  C  CB  . HIS A 1 43  ? 121.512 109.950 120.295 1.00 43.49  ? 43  HIS A CB  1 
ATOM   284  C  CG  . HIS A 1 43  ? 120.273 110.231 121.088 1.00 43.49  ? 43  HIS A CG  1 
ATOM   285  N  ND1 . HIS A 1 43  ? 120.147 111.339 121.898 1.00 43.49  ? 43  HIS A ND1 1 
ATOM   286  C  CD2 . HIS A 1 43  ? 119.109 109.550 121.199 1.00 43.49  ? 43  HIS A CD2 1 
ATOM   287  C  CE1 . HIS A 1 43  ? 118.960 111.327 122.475 1.00 43.49  ? 43  HIS A CE1 1 
ATOM   288  N  NE2 . HIS A 1 43  ? 118.310 110.252 122.069 1.00 43.49  ? 43  HIS A NE2 1 
ATOM   289  N  N   . MET A 1 44  ? 123.491 107.926 118.358 1.00 41.71  ? 44  MET A N   1 
ATOM   290  C  CA  . MET A 1 44  ? 124.423 107.862 117.226 1.00 41.71  ? 44  MET A CA  1 
ATOM   291  C  C   . MET A 1 44  ? 123.929 106.943 116.094 1.00 41.71  ? 44  MET A C   1 
ATOM   292  O  O   . MET A 1 44  ? 124.495 106.949 114.985 1.00 41.71  ? 44  MET A O   1 
ATOM   293  C  CB  . MET A 1 44  ? 125.799 107.436 117.725 1.00 41.71  ? 44  MET A CB  1 
ATOM   294  C  CG  . MET A 1 44  ? 126.922 107.664 116.747 1.00 41.71  ? 44  MET A CG  1 
ATOM   295  S  SD  . MET A 1 44  ? 128.549 107.621 117.509 1.00 41.71  ? 44  MET A SD  1 
ATOM   296  C  CE  . MET A 1 44  ? 128.637 109.262 118.191 1.00 41.71  ? 44  MET A CE  1 
ATOM   297  N  N   . LEU A 1 45  ? 122.873 106.168 116.334 1.00 38.90  ? 45  LEU A N   1 
ATOM   298  C  CA  . LEU A 1 45  ? 122.177 105.481 115.256 1.00 38.90  ? 45  LEU A CA  1 
ATOM   299  C  C   . LEU A 1 45  ? 121.479 106.436 114.306 1.00 38.90  ? 45  LEU A C   1 
ATOM   300  O  O   . LEU A 1 45  ? 120.750 105.978 113.424 1.00 38.90  ? 45  LEU A O   1 
ATOM   301  C  CB  . LEU A 1 45  ? 121.152 104.517 115.821 1.00 38.90  ? 45  LEU A CB  1 
ATOM   302  C  CG  . LEU A 1 45  ? 121.733 103.235 116.381 1.00 38.90  ? 45  LEU A CG  1 
ATOM   303  C  CD1 . LEU A 1 45  ? 120.689 102.508 117.202 1.00 38.90  ? 45  LEU A CD1 1 
ATOM   304  C  CD2 . LEU A 1 45  ? 122.204 102.379 115.233 1.00 38.90  ? 45  LEU A CD2 1 
ATOM   305  N  N   . SER A 1 46  ? 121.626 107.741 114.505 1.00 36.74  ? 46  SER A N   1 
ATOM   306  C  CA  . SER A 1 46  ? 121.172 108.737 113.551 1.00 36.74  ? 46  SER A CA  1 
ATOM   307  C  C   . SER A 1 46  ? 122.315 109.308 112.736 1.00 36.74  ? 46  SER A C   1 
ATOM   308  O  O   . SER A 1 46  ? 122.073 110.039 111.773 1.00 36.74  ? 46  SER A O   1 
ATOM   309  C  CB  . SER A 1 46  ? 120.446 109.868 114.277 1.00 36.74  ? 46  SER A CB  1 
ATOM   310  O  OG  . SER A 1 46  ? 121.312 110.549 115.164 1.00 36.74  ? 46  SER A OG  1 
ATOM   311  N  N   . ASP A 1 47  ? 123.547 109.020 113.129 1.00 38.96  ? 47  ASP A N   1 
ATOM   312  C  CA  . ASP A 1 47  ? 124.726 109.339 112.344 1.00 38.96  ? 47  ASP A CA  1 
ATOM   313  C  C   . ASP A 1 47  ? 125.196 108.159 111.519 1.00 38.96  ? 47  ASP A C   1 
ATOM   314  O  O   . ASP A 1 47  ? 125.960 108.349 110.573 1.00 38.96  ? 47  ASP A O   1 
ATOM   315  C  CB  . ASP A 1 47  ? 125.861 109.795 113.265 1.00 38.96  ? 47  ASP A CB  1 
ATOM   316  C  CG  . ASP A 1 47  ? 126.917 110.586 112.542 1.00 38.96  ? 47  ASP A CG  1 
ATOM   317  O  OD1 . ASP A 1 47  ? 126.735 110.850 111.340 1.00 38.96  ? 47  ASP A OD1 1 
ATOM   318  O  OD2 . ASP A 1 47  ? 127.925 110.954 113.178 1.00 38.96  ? 47  ASP A OD2 1 
ATOM   319  N  N   . VAL A 1 48  ? 124.803 106.941 111.887 1.00 30.94  ? 48  VAL A N   1 
ATOM   320  C  CA  . VAL A 1 48  ? 125.099 105.807 111.007 1.00 30.94  ? 48  VAL A CA  1 
ATOM   321  C  C   . VAL A 1 48  ? 124.136 105.743 109.815 1.00 30.94  ? 48  VAL A C   1 
ATOM   322  O  O   . VAL A 1 48  ? 124.473 105.182 108.764 1.00 30.94  ? 48  VAL A O   1 
ATOM   323  C  CB  . VAL A 1 48  ? 125.113 104.501 111.813 1.00 30.94  ? 48  VAL A CB  1 
ATOM   324  C  CG1 . VAL A 1 48  ? 124.856 103.299 110.932 1.00 30.94  ? 48  VAL A CG1 1 
ATOM   325  C  CG2 . VAL A 1 48  ? 126.450 104.354 112.483 1.00 30.94  ? 48  VAL A CG2 1 
ATOM   326  N  N   . LEU A 1 49  ? 122.951 106.337 109.926 1.00 26.79  ? 49  LEU A N   1 
ATOM   327  C  CA  . LEU A 1 49  ? 121.999 106.272 108.821 1.00 26.79  ? 49  LEU A CA  1 
ATOM   328  C  C   . LEU A 1 49  ? 122.446 107.101 107.623 1.00 26.79  ? 49  LEU A C   1 
ATOM   329  O  O   . LEU A 1 49  ? 122.270 106.684 106.474 1.00 26.79  ? 49  LEU A O   1 
ATOM   330  C  CB  . LEU A 1 49  ? 120.632 106.736 109.283 1.00 26.79  ? 49  LEU A CB  1 
ATOM   331  C  CG  . LEU A 1 49  ? 119.675 105.596 109.538 1.00 26.79  ? 49  LEU A CG  1 
ATOM   332  C  CD1 . LEU A 1 49  ? 118.327 106.156 109.908 1.00 26.79  ? 49  LEU A CD1 1 
ATOM   333  C  CD2 . LEU A 1 49  ? 119.585 104.768 108.288 1.00 26.79  ? 49  LEU A CD2 1 
ATOM   334  N  N   . ALA A 1 50  ? 122.996 108.287 107.855 1.00 24.10  ? 50  ALA A N   1 
ATOM   335  C  CA  . ALA A 1 50  ? 123.394 109.118 106.729 1.00 24.10  ? 50  ALA A CA  1 
ATOM   336  C  C   . ALA A 1 50  ? 124.620 108.572 106.031 1.00 24.10  ? 50  ALA A C   1 
ATOM   337  O  O   . ALA A 1 50  ? 124.973 109.053 104.955 1.00 24.10  ? 50  ALA A O   1 
ATOM   338  C  CB  . ALA A 1 50  ? 123.661 110.541 107.176 1.00 24.10  ? 50  ALA A CB  1 
ATOM   339  N  N   . LEU A 1 51  ? 125.319 107.619 106.641 1.00 20.26  ? 51  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 51  ? 126.381 106.934 105.917 1.00 20.26  ? 51  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 51  ? 125.853 105.695 105.209 1.00 20.26  ? 51  LEU A C   1 
ATOM   342  O  O   . LEU A 1 51  ? 126.262 105.405 104.085 1.00 20.26  ? 51  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 51  ? 127.530 106.573 106.852 1.00 20.26  ? 51  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 51  ? 128.096 107.677 107.739 1.00 20.26  ? 51  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 51  ? 129.385 107.225 108.334 1.00 20.26  ? 51  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 51  ? 128.308 108.947 106.986 1.00 20.26  ? 51  LEU A CD2 1 
ATOM   347  N  N   . VAL A 1 52  ? 124.932 104.962 105.830 1.00 23.41  ? 52  VAL A N   1 
ATOM   348  C  CA  . VAL A 1 52  ? 124.334 103.832 105.125 1.00 23.41  ? 52  VAL A CA  1 
ATOM   349  C  C   . VAL A 1 52  ? 123.639 104.277 103.847 1.00 23.41  ? 52  VAL A C   1 
ATOM   350  O  O   . VAL A 1 52  ? 123.728 103.591 102.826 1.00 23.41  ? 52  VAL A O   1 
ATOM   351  C  CB  . VAL A 1 52  ? 123.361 103.070 106.035 1.00 23.41  ? 52  VAL A CB  1 
ATOM   352  C  CG1 . VAL A 1 52  ? 122.394 102.256 105.208 1.00 23.41  ? 52  VAL A CG1 1 
ATOM   353  C  CG2 . VAL A 1 52  ? 124.125 102.162 106.968 1.00 23.41  ? 52  VAL A CG2 1 
ATOM   354  N  N   . VAL A 1 53  ? 122.953 105.421 103.857 1.00 22.08  ? 53  VAL A N   1 
ATOM   355  C  CA  . VAL A 1 53  ? 122.253 105.860 102.649 1.00 22.08  ? 53  VAL A CA  1 
ATOM   356  C  C   . VAL A 1 53  ? 123.245 106.272 101.565 1.00 22.08  ? 53  VAL A C   1 
ATOM   357  O  O   . VAL A 1 53  ? 123.155 105.824 100.417 1.00 22.08  ? 53  VAL A O   1 
ATOM   358  C  CB  . VAL A 1 53  ? 121.266 106.992 102.964 1.00 22.08  ? 53  VAL A CB  1 
ATOM   359  C  CG1 . VAL A 1 53  ? 120.950 107.737 101.708 1.00 22.08  ? 53  VAL A CG1 1 
ATOM   360  C  CG2 . VAL A 1 53  ? 120.004 106.426 103.551 1.00 22.08  ? 53  VAL A CG2 1 
ATOM   361  N  N   . ALA A 1 54  ? 124.202 107.127 101.899 1.00 24.03  ? 54  ALA A N   1 
ATOM   362  C  CA  . ALA A 1 54  ? 125.168 107.497 100.878 1.00 24.03  ? 54  ALA A CA  1 
ATOM   363  C  C   . ALA A 1 54  ? 126.103 106.372 100.521 1.00 24.03  ? 54  ALA A C   1 
ATOM   364  O  O   . ALA A 1 54  ? 126.941 106.558 99.641  1.00 24.03  ? 54  ALA A O   1 
ATOM   365  C  CB  . ALA A 1 54  ? 125.994 108.690 101.315 1.00 24.03  ? 54  ALA A CB  1 
ATOM   366  N  N   . LEU A 1 55  ? 126.024 105.237 101.204 1.00 25.55  ? 55  LEU A N   1 
ATOM   367  C  CA  . LEU A 1 55  ? 126.721 104.036 100.767 1.00 25.55  ? 55  LEU A CA  1 
ATOM   368  C  C   . LEU A 1 55  ? 125.870 103.226 99.796  1.00 25.55  ? 55  LEU A C   1 
ATOM   369  O  O   . LEU A 1 55  ? 126.382 102.687 98.814  1.00 25.55  ? 55  LEU A O   1 
ATOM   370  C  CB  . LEU A 1 55  ? 127.089 103.188 101.982 1.00 25.55  ? 55  LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 55  ? 128.073 102.062 101.750 1.00 25.55  ? 55  LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 55  ? 129.358 102.677 101.303 1.00 25.55  ? 55  LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 55  ? 128.259 101.287 103.025 1.00 25.55  ? 55  LEU A CD2 1 
ATOM   374  N  N   . VAL A 1 56  ? 124.569 103.126 100.069 1.00 19.31  ? 56  VAL A N   1 
ATOM   375  C  CA  . VAL A 1 56  ? 123.655 102.461 99.156  1.00 19.31  ? 56  VAL A CA  1 
ATOM   376  C  C   . VAL A 1 56  ? 123.593 103.180 97.830  1.00 19.31  ? 56  VAL A C   1 
ATOM   377  O  O   . VAL A 1 56  ? 123.459 102.539 96.792  1.00 19.31  ? 56  VAL A O   1 
ATOM   378  C  CB  . VAL A 1 56  ? 122.257 102.354 99.780  1.00 19.31  ? 56  VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 56  ? 121.250 102.002 98.741  1.00 19.31  ? 56  VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 56  ? 122.247 101.313 100.869 1.00 19.31  ? 56  VAL A CG2 1 
ATOM   381  N  N   . ALA A 1 57  ? 123.715 104.498 97.825  1.00 22.48  ? 57  ALA A N   1 
ATOM   382  C  CA  . ALA A 1 57  ? 123.721 105.232 96.568  1.00 22.48  ? 57  ALA A CA  1 
ATOM   383  C  C   . ALA A 1 57  ? 125.098 105.329 95.933  1.00 22.48  ? 57  ALA A C   1 
ATOM   384  O  O   . ALA A 1 57  ? 125.346 106.260 95.171  1.00 22.48  ? 57  ALA A O   1 
ATOM   385  C  CB  . ALA A 1 57  ? 123.151 106.632 96.769  1.00 22.48  ? 57  ALA A CB  1 
ATOM   386  N  N   . GLU A 1 58  ? 125.973 104.378 96.244  1.00 25.16  ? 58  GLU A N   1 
ATOM   387  C  CA  . GLU A 1 58  ? 127.337 104.326 95.654  1.00 25.16  ? 58  GLU A CA  1 
ATOM   388  C  C   . GLU A 1 58  ? 127.389 103.123 94.709  1.00 25.16  ? 58  GLU A C   1 
ATOM   389  O  O   . GLU A 1 58  ? 128.048 103.224 93.664  1.00 25.16  ? 58  GLU A O   1 
ATOM   390  C  CB  . GLU A 1 58  ? 128.411 104.269 96.739  1.00 25.16  ? 58  GLU A CB  1 
ATOM   391  C  CG  . GLU A 1 58  ? 129.524 105.279 96.530  1.00 25.16  ? 58  GLU A CG  1 
ATOM   392  C  CD  . GLU A 1 58  ? 129.072 106.681 96.159  1.00 25.16  ? 58  GLU A CD  1 
ATOM   393  O  OE1 . GLU A 1 58  ? 128.275 106.816 95.211  1.00 25.16  ? 58  GLU A OE1 1 
ATOM   394  O  OE2 . GLU A 1 58  ? 129.527 107.637 96.814  1.00 25.16  ? 58  GLU A OE2 1 
ATOM   395  N  N   . ARG A 1 59  ? 126.680 102.065 95.077  1.00 29.52  ? 59  ARG A N   1 
ATOM   396  C  CA  . ARG A 1 59  ? 126.568 100.834 94.258  1.00 29.52  ? 59  ARG A CA  1 
ATOM   397  C  C   . ARG A 1 59  ? 125.390 101.025 93.298  1.00 29.52  ? 59  ARG A C   1 
ATOM   398  O  O   . ARG A 1 59  ? 124.867 100.016 92.795  1.00 29.52  ? 59  ARG A O   1 
ATOM   399  C  CB  . ARG A 1 59  ? 126.328 99.627  95.169  1.00 29.52  ? 59  ARG A CB  1 
ATOM   400  C  CG  . ARG A 1 59  ? 126.784 98.299  94.584  1.00 29.52  ? 59  ARG A CG  1 
ATOM   401  C  CD  . ARG A 1 59  ? 126.837 97.227  95.653  1.00 29.52  ? 59  ARG A CD  1 
ATOM   402  N  NE  . ARG A 1 59  ? 127.867 96.235  95.385  1.00 29.52  ? 59  ARG A NE  1 
ATOM   403  C  CZ  . ARG A 1 59  ? 127.778 94.953  95.721  1.00 29.52  ? 59  ARG A CZ  1 
ATOM   404  N  NH1 . ARG A 1 59  ? 127.693 94.606  96.993  1.00 29.52  ? 59  ARG A NH1 1 
ATOM   405  N  NH2 . ARG A 1 59  ? 127.772 94.023  94.783  1.00 29.52  ? 59  ARG A NH2 1 
ATOM   406  N  N   . PHE A 1 60  ? 124.968 102.263 93.080  1.00 22.24  ? 60  PHE A N   1 
ATOM   407  C  CA  . PHE A 1 60  ? 123.872 102.529 92.169  1.00 22.24  ? 60  PHE A CA  1 
ATOM   408  C  C   . PHE A 1 60  ? 124.129 103.651 91.182  1.00 22.24  ? 60  PHE A C   1 
ATOM   409  O  O   . PHE A 1 60  ? 123.288 103.887 90.319  1.00 22.24  ? 60  PHE A O   1 
ATOM   410  C  CB  . PHE A 1 60  ? 122.613 102.878 92.944  1.00 22.24  ? 60  PHE A CB  1 
ATOM   411  C  CG  . PHE A 1 60  ? 121.812 101.709 93.327  1.00 22.24  ? 60  PHE A CG  1 
ATOM   412  C  CD1 . PHE A 1 60  ? 120.558 101.873 93.872  1.00 22.24  ? 60  PHE A CD1 1 
ATOM   413  C  CD2 . PHE A 1 60  ? 122.304 100.452 93.154  1.00 22.24  ? 60  PHE A CD2 1 
ATOM   414  C  CE1 . PHE A 1 60  ? 119.814 100.802 94.222  1.00 22.24  ? 60  PHE A CE1 1 
ATOM   415  C  CE2 . PHE A 1 60  ? 121.571 99.377  93.511  1.00 22.24  ? 60  PHE A CE2 1 
ATOM   416  C  CZ  . PHE A 1 60  ? 120.323 99.545  94.049  1.00 22.24  ? 60  PHE A CZ  1 
ATOM   417  N  N   . ALA A 1 61  ? 125.216 104.386 91.302  1.00 23.60  ? 61  ALA A N   1 
ATOM   418  C  CA  . ALA A 1 61  ? 125.598 105.320 90.262  1.00 23.60  ? 61  ALA A CA  1 
ATOM   419  C  C   . ALA A 1 61  ? 126.670 104.737 89.375  1.00 23.60  ? 61  ALA A C   1 
ATOM   420  O  O   . ALA A 1 61  ? 127.261 105.464 88.576  1.00 23.60  ? 61  ALA A O   1 
ATOM   421  C  CB  . ALA A 1 61  ? 126.087 106.637 90.860  1.00 23.60  ? 61  ALA A CB  1 
ATOM   422  N  N   . ARG A 1 62  ? 126.962 103.453 89.531  1.00 29.43  ? 62  ARG A N   1 
ATOM   423  C  CA  . ARG A 1 62  ? 127.897 102.743 88.681  1.00 29.43  ? 62  ARG A CA  1 
ATOM   424  C  C   . ARG A 1 62  ? 127.193 101.804 87.722  1.00 29.43  ? 62  ARG A C   1 
ATOM   425  O  O   . ARG A 1 62  ? 127.827 101.303 86.791  1.00 29.43  ? 62  ARG A O   1 
ATOM   426  C  CB  . ARG A 1 62  ? 128.897 101.948 89.527  1.00 29.43  ? 62  ARG A CB  1 
ATOM   427  C  CG  . ARG A 1 62  ? 129.378 102.661 90.771  1.00 29.43  ? 62  ARG A CG  1 
ATOM   428  C  CD  . ARG A 1 62  ? 129.991 101.689 91.767  1.00 29.43  ? 62  ARG A CD  1 
ATOM   429  N  NE  . ARG A 1 62  ? 131.003 100.836 91.156  1.00 29.43  ? 62  ARG A NE  1 
ATOM   430  C  CZ  . ARG A 1 62  ? 131.690 99.911  91.815  1.00 29.43  ? 62  ARG A CZ  1 
ATOM   431  N  NH1 . ARG A 1 62  ? 131.476 99.730  93.108  1.00 29.43  ? 62  ARG A NH1 1 
ATOM   432  N  NH2 . ARG A 1 62  ? 132.596 99.173  91.185  1.00 29.43  ? 62  ARG A NH2 1 
ATOM   433  N  N   . ARG A 1 63  ? 125.906 101.542 87.923  1.00 26.30  ? 63  ARG A N   1 
ATOM   434  C  CA  . ARG A 1 63  ? 125.190 100.703 86.981  1.00 26.30  ? 63  ARG A CA  1 
ATOM   435  C  C   . ARG A 1 63  ? 124.672 101.544 85.831  1.00 26.30  ? 63  ARG A C   1 
ATOM   436  O  O   . ARG A 1 63  ? 123.506 101.423 85.457  1.00 26.30  ? 63  ARG A O   1 
ATOM   437  C  CB  . ARG A 1 63  ? 124.026 99.988  87.654  1.00 26.30  ? 63  ARG A CB  1 
ATOM   438  C  CG  . ARG A 1 63  ? 124.389 99.153  88.847  1.00 26.30  ? 63  ARG A CG  1 
ATOM   439  C  CD  . ARG A 1 63  ? 123.133 98.548  89.433  1.00 26.30  ? 63  ARG A CD  1 
ATOM   440  N  NE  . ARG A 1 63  ? 123.406 97.536  90.443  1.00 26.30  ? 63  ARG A NE  1 
ATOM   441  C  CZ  . ARG A 1 63  ? 122.484 96.723  90.947  1.00 26.30  ? 63  ARG A CZ  1 
ATOM   442  N  NH1 . ARG A 1 63  ? 121.229 96.801  90.527  1.00 26.30  ? 63  ARG A NH1 1 
ATOM   443  N  NH2 . ARG A 1 63  ? 122.816 95.825  91.868  1.00 26.30  ? 63  ARG A NH2 1 
ATOM   444  N  N   . THR A 1 64  ? 125.526 102.377 85.243  1.00 25.62  ? 64  THR A N   1 
ATOM   445  C  CA  . THR A 1 64  ? 125.100 103.276 84.176  1.00 25.62  ? 64  THR A CA  1 
ATOM   446  C  C   . THR A 1 64  ? 125.010 102.513 82.854  1.00 25.62  ? 64  THR A C   1 
ATOM   447  O  O   . THR A 1 64  ? 125.828 102.654 81.945  1.00 25.62  ? 64  THR A O   1 
ATOM   448  C  CB  . THR A 1 64  ? 126.037 104.467 84.081  1.00 25.62  ? 64  THR A CB  1 
ATOM   449  O  OG1 . THR A 1 64  ? 125.719 105.220 82.914  1.00 25.62  ? 64  THR A OG1 1 
ATOM   450  C  CG2 . THR A 1 64  ? 127.470 104.026 84.012  1.00 25.62  ? 64  THR A CG2 1 
ATOM   451  N  N   . HIS A 1 65  ? 124.005 101.648 82.769  1.00 24.50  ? 65  HIS A N   1 
ATOM   452  C  CA  . HIS A 1 65  ? 123.744 100.854 81.538  1.00 24.50  ? 65  HIS A CA  1 
ATOM   453  C  C   . HIS A 1 65  ? 122.228 100.735 81.340  1.00 24.50  ? 65  HIS A C   1 
ATOM   454  O  O   . HIS A 1 65  ? 121.516 100.529 82.337  1.00 24.50  ? 65  HIS A O   1 
ATOM   455  C  CB  . HIS A 1 65  ? 124.516 99.525  81.539  1.00 24.50  ? 65  HIS A CB  1 
ATOM   456  C  CG  . HIS A 1 65  ? 124.210 98.625  82.687  1.00 24.50  ? 65  HIS A CG  1 
ATOM   457  N  ND1 . HIS A 1 65  ? 124.556 97.288  82.683  1.00 24.50  ? 65  HIS A ND1 1 
ATOM   458  C  CD2 . HIS A 1 65  ? 123.602 98.855  83.870  1.00 24.50  ? 65  HIS A CD2 1 
ATOM   459  C  CE1 . HIS A 1 65  ? 124.171 96.733  83.813  1.00 24.50  ? 65  HIS A CE1 1 
ATOM   460  N  NE2 . HIS A 1 65  ? 123.583 97.673  84.558  1.00 24.50  ? 65  HIS A NE2 1 
ATOM   461  N  N   . ALA A 1 66  ? 121.759 100.848 80.110  1.00 19.79  ? 66  ALA A N   1 
ATOM   462  C  CA  . ALA A 1 66  ? 120.337 100.846 79.820  1.00 19.79  ? 66  ALA A CA  1 
ATOM   463  C  C   . ALA A 1 66  ? 119.726 99.497  80.158  1.00 19.79  ? 66  ALA A C   1 
ATOM   464  O  O   . ALA A 1 66  ? 119.985 98.506  79.477  1.00 19.79  ? 66  ALA A O   1 
ATOM   465  C  CB  . ALA A 1 66  ? 120.103 101.176 78.353  1.00 19.79  ? 66  ALA A CB  1 
ATOM   466  N  N   . THR A 1 67  ? 118.899 99.464  81.192  1.00 12.53  ? 67  THR A N   1 
ATOM   467  C  CA  . THR A 1 67  ? 118.233 98.249  81.624  1.00 12.53  ? 67  THR A CA  1 
ATOM   468  C  C   . THR A 1 67  ? 116.742 98.342  81.330  1.00 12.53  ? 67  THR A C   1 
ATOM   469  O  O   . THR A 1 67  ? 116.131 99.400  81.457  1.00 12.53  ? 67  THR A O   1 
ATOM   470  C  CB  . THR A 1 67  ? 118.438 98.014  83.119  1.00 12.53  ? 67  THR A CB  1 
ATOM   471  O  OG1 . THR A 1 67  ? 119.765 98.392  83.484  1.00 12.53  ? 67  THR A OG1 1 
ATOM   472  C  CG2 . THR A 1 67  ? 118.244 96.560  83.453  1.00 12.53  ? 67  THR A CG2 1 
ATOM   473  N  N   . GLN A 1 68  ? 116.109 97.210  81.096  1.00 19.98  ? 68  GLN A N   1 
ATOM   474  C  CA  . GLN A 1 68  ? 114.688 97.230  80.664  1.00 19.98  ? 68  GLN A CA  1 
ATOM   475  C  C   . GLN A 1 68  ? 113.859 97.957  81.725  1.00 19.98  ? 68  GLN A C   1 
ATOM   476  O  O   . GLN A 1 68  ? 112.710 98.323  81.419  1.00 19.98  ? 68  GLN A O   1 
ATOM   477  C  CB  . GLN A 1 68  ? 114.185 95.808  80.410  1.00 19.98  ? 68  GLN A CB  1 
ATOM   478  C  CG  . GLN A 1 68  ? 112.724 95.741  79.994  1.00 19.98  ? 68  GLN A CG  1 
ATOM   479  C  CD  . GLN A 1 68  ? 112.351 94.376  79.471  1.00 19.98  ? 68  GLN A CD  1 
ATOM   480  O  OE1 . GLN A 1 68  ? 113.209 93.552  79.164  1.00 19.98  ? 68  GLN A OE1 1 
ATOM   481  N  NE2 . GLN A 1 68  ? 111.056 94.128  79.362  1.00 19.98  ? 68  GLN A NE2 1 
ATOM   482  N  N   . LYS A 1 69  ? 114.395 98.116  82.925  1.00 10.41  ? 69  LYS A N   1 
ATOM   483  C  CA  . LYS A 1 69  ? 113.650 98.758  84.002  1.00 10.41  ? 69  LYS A CA  1 
ATOM   484  C  C   . LYS A 1 69  ? 114.075 100.199 84.200  1.00 10.41  ? 69  LYS A C   1 
ATOM   485  O  O   . LYS A 1 69  ? 113.602 100.851 85.126  1.00 10.41  ? 69  LYS A O   1 
ATOM   486  C  CB  . LYS A 1 69  ? 113.819 97.982  85.308  1.00 10.41  ? 69  LYS A CB  1 
ATOM   487  C  CG  . LYS A 1 69  ? 112.817 98.301  86.405  1.00 10.41  ? 69  LYS A CG  1 
ATOM   488  C  CD  . LYS A 1 69  ? 111.446 98.641  85.869  1.00 10.41  ? 69  LYS A CD  1 
ATOM   489  C  CE  . LYS A 1 69  ? 110.569 99.219  86.966  1.00 10.41  ? 69  LYS A CE  1 
ATOM   490  N  NZ  . LYS A 1 69  ? 109.240 99.651  86.457  1.00 10.41  ? 69  LYS A NZ  1 
ATOM   491  N  N   . ASN A 1 70  ? 115.007 100.682 83.405  1.00 6.10   ? 70  ASN A N   1 
ATOM   492  C  CA  . ASN A 1 70  ? 115.338 102.092 83.353  1.00 6.10   ? 70  ASN A CA  1 
ATOM   493  C  C   . ASN A 1 70  ? 116.202 102.304 82.140  1.00 6.10   ? 70  ASN A C   1 
ATOM   494  O  O   . ASN A 1 70  ? 117.361 101.897 82.141  1.00 6.10   ? 70  ASN A O   1 
ATOM   495  C  CB  . ASN A 1 70  ? 116.035 102.541 84.628  1.00 6.10   ? 70  ASN A CB  1 
ATOM   496  C  CG  . ASN A 1 70  ? 116.749 103.875 84.492  1.00 6.10   ? 70  ASN A CG  1 
ATOM   497  O  OD1 . ASN A 1 70  ? 117.151 104.294 83.420  1.00 6.10   ? 70  ASN A OD1 1 
ATOM   498  N  ND2 . ASN A 1 70  ? 116.867 104.577 85.603  1.00 6.10   ? 70  ASN A ND2 1 
ATOM   499  N  N   . THR A 1 71  ? 115.685 102.990 81.133  1.00 3.89   ? 71  THR A N   1 
ATOM   500  C  CA  . THR A 1 71  ? 116.387 103.124 79.873  1.00 3.89   ? 71  THR A CA  1 
ATOM   501  C  C   . THR A 1 71  ? 117.408 104.247 79.862  1.00 3.89   ? 71  THR A C   1 
ATOM   502  O  O   . THR A 1 71  ? 118.014 104.492 78.819  1.00 3.89   ? 71  THR A O   1 
ATOM   503  C  CB  . THR A 1 71  ? 115.376 103.304 78.769  1.00 3.89   ? 71  THR A CB  1 
ATOM   504  O  OG1 . THR A 1 71  ? 114.349 104.154 79.256  1.00 3.89   ? 71  THR A OG1 1 
ATOM   505  C  CG2 . THR A 1 71  ? 114.769 101.991 78.417  1.00 3.89   ? 71  THR A CG2 1 
ATOM   506  N  N   . PHE A 1 72  ? 117.615 104.924 80.992  1.00 4.96   ? 72  PHE A N   1 
ATOM   507  C  CA  . PHE A 1 72  ? 118.775 105.779 81.220  1.00 4.96   ? 72  PHE A CA  1 
ATOM   508  C  C   . PHE A 1 72  ? 119.811 105.129 82.109  1.00 4.96   ? 72  PHE A C   1 
ATOM   509  O  O   . PHE A 1 72  ? 120.951 105.596 82.144  1.00 4.96   ? 72  PHE A O   1 
ATOM   510  C  CB  . PHE A 1 72  ? 118.378 107.077 81.914  1.00 4.96   ? 72  PHE A CB  1 
ATOM   511  C  CG  . PHE A 1 72  ? 117.590 108.000 81.079  1.00 4.96   ? 72  PHE A CG  1 
ATOM   512  C  CD1 . PHE A 1 72  ? 118.206 108.883 80.255  1.00 4.96   ? 72  PHE A CD1 1 
ATOM   513  C  CD2 . PHE A 1 72  ? 116.236 107.995 81.135  1.00 4.96   ? 72  PHE A CD2 1 
ATOM   514  C  CE1 . PHE A 1 72  ? 117.490 109.729 79.497  1.00 4.96   ? 72  PHE A CE1 1 
ATOM   515  C  CE2 . PHE A 1 72  ? 115.533 108.843 80.379  1.00 4.96   ? 72  PHE A CE2 1 
ATOM   516  C  CZ  . PHE A 1 72  ? 116.159 109.709 79.554  1.00 4.96   ? 72  PHE A CZ  1 
ATOM   517  N  N   . GLY A 1 73  ? 119.428 104.090 82.845  1.00 6.17   ? 73  GLY A N   1 
ATOM   518  C  CA  . GLY A 1 73  ? 120.252 103.553 83.905  1.00 6.17   ? 73  GLY A CA  1 
ATOM   519  C  C   . GLY A 1 73  ? 119.999 104.310 85.187  1.00 6.17   ? 73  GLY A C   1 
ATOM   520  O  O   . GLY A 1 73  ? 119.190 105.234 85.243  1.00 6.17   ? 73  GLY A O   1 
ATOM   521  N  N   . TRP A 1 74  ? 120.710 103.922 86.249  1.00 9.36   ? 74  TRP A N   1 
ATOM   522  C  CA  . TRP A 1 74  ? 120.561 104.610 87.523  1.00 9.36   ? 74  TRP A CA  1 
ATOM   523  C  C   . TRP A 1 74  ? 121.565 105.723 87.694  1.00 9.36   ? 74  TRP A C   1 
ATOM   524  O  O   . TRP A 1 74  ? 121.960 106.021 88.821  1.00 9.36   ? 74  TRP A O   1 
ATOM   525  C  CB  . TRP A 1 74  ? 120.659 103.629 88.682  1.00 9.36   ? 74  TRP A CB  1 
ATOM   526  C  CG  . TRP A 1 74  ? 119.783 102.494 88.518  1.00 9.36   ? 74  TRP A CG  1 
ATOM   527  C  CD1 . TRP A 1 74  ? 120.140 101.249 88.166  1.00 9.36   ? 74  TRP A CD1 1 
ATOM   528  C  CD2 . TRP A 1 74  ? 118.374 102.479 88.681  1.00 9.36   ? 74  TRP A CD2 1 
ATOM   529  N  NE1 . TRP A 1 74  ? 119.044 100.442 88.098  1.00 9.36   ? 74  TRP A NE1 1 
ATOM   530  C  CE2 . TRP A 1 74  ? 117.940 101.181 88.414  1.00 9.36   ? 74  TRP A CE2 1 
ATOM   531  C  CE3 . TRP A 1 74  ? 117.431 103.443 89.018  1.00 9.36   ? 74  TRP A CE3 1 
ATOM   532  C  CZ2 . TRP A 1 74  ? 116.606 100.817 88.475  1.00 9.36   ? 74  TRP A CZ2 1 
ATOM   533  C  CZ3 . TRP A 1 74  ? 116.107 103.080 89.076  1.00 9.36   ? 74  TRP A CZ3 1 
ATOM   534  C  CH2 . TRP A 1 74  ? 115.707 101.782 88.809  1.00 9.36   ? 74  TRP A CH2 1 
ATOM   535  N  N   . ILE A 1 75  ? 121.976 106.361 86.600  1.00 12.18  ? 75  ILE A N   1 
ATOM   536  C  CA  . ILE A 1 75  ? 122.942 107.445 86.662  1.00 12.18  ? 75  ILE A CA  1 
ATOM   537  C  C   . ILE A 1 75  ? 122.447 108.595 87.520  1.00 12.18  ? 75  ILE A C   1 
ATOM   538  O  O   . ILE A 1 75  ? 123.227 109.484 87.871  1.00 12.18  ? 75  ILE A O   1 
ATOM   539  C  CB  . ILE A 1 75  ? 123.259 107.904 85.234  1.00 12.18  ? 75  ILE A CB  1 
ATOM   540  C  CG1 . ILE A 1 75  ? 124.449 108.841 85.203  1.00 12.18  ? 75  ILE A CG1 1 
ATOM   541  C  CG2 . ILE A 1 75  ? 122.100 108.612 84.674  1.00 12.18  ? 75  ILE A CG2 1 
ATOM   542  C  CD1 . ILE A 1 75  ? 125.744 108.175 85.605  1.00 12.18  ? 75  ILE A CD1 1 
ATOM   543  N  N   . ARG A 1 76  ? 121.166 108.600 87.881  1.00 4.96   ? 76  ARG A N   1 
ATOM   544  C  CA  . ARG A 1 76  ? 120.573 109.641 88.710  1.00 4.96   ? 76  ARG A CA  1 
ATOM   545  C  C   . ARG A 1 76  ? 120.569 109.300 90.187  1.00 4.96   ? 76  ARG A C   1 
ATOM   546  O  O   . ARG A 1 76  ? 120.446 110.209 91.006  1.00 4.96   ? 76  ARG A O   1 
ATOM   547  C  CB  . ARG A 1 76  ? 119.141 109.909 88.259  1.00 4.96   ? 76  ARG A CB  1 
ATOM   548  C  CG  . ARG A 1 76  ? 118.640 111.318 88.425  1.00 4.96   ? 76  ARG A CG  1 
ATOM   549  C  CD  . ARG A 1 76  ? 117.282 111.398 87.762  1.00 4.96   ? 76  ARG A CD  1 
ATOM   550  N  NE  . ARG A 1 76  ? 116.649 112.707 87.757  1.00 4.96   ? 76  ARG A NE  1 
ATOM   551  C  CZ  . ARG A 1 76  ? 116.949 113.665 86.904  1.00 4.96   ? 76  ARG A CZ  1 
ATOM   552  N  NH1 . ARG A 1 76  ? 117.898 113.468 86.033  1.00 4.96   ? 76  ARG A NH1 1 
ATOM   553  N  NH2 . ARG A 1 76  ? 116.326 114.820 86.942  1.00 4.96   ? 76  ARG A NH2 1 
ATOM   554  N  N   . ALA A 1 77  ? 120.727 108.028 90.553  1.00 12.92  ? 77  ALA A N   1 
ATOM   555  C  CA  . ALA A 1 77  ? 120.654 107.635 91.954  1.00 12.92  ? 77  ALA A CA  1 
ATOM   556  C  C   . ALA A 1 77  ? 121.772 108.228 92.788  1.00 12.92  ? 77  ALA A C   1 
ATOM   557  O  O   . ALA A 1 77  ? 121.832 107.974 93.988  1.00 12.92  ? 77  ALA A O   1 
ATOM   558  C  CB  . ALA A 1 77  ? 120.676 106.123 92.080  1.00 12.92  ? 77  ALA A CB  1 
ATOM   559  N  N   . GLU A 1 78  ? 122.683 108.971 92.181  1.00 19.76  ? 78  GLU A N   1 
ATOM   560  C  CA  . GLU A 1 78  ? 123.585 109.810 92.955  1.00 19.76  ? 78  GLU A CA  1 
ATOM   561  C  C   . GLU A 1 78  ? 122.857 111.048 93.448  1.00 19.76  ? 78  GLU A C   1 
ATOM   562  O  O   . GLU A 1 78  ? 122.697 111.254 94.653  1.00 19.76  ? 78  GLU A O   1 
ATOM   563  C  CB  . GLU A 1 78  ? 124.782 110.198 92.096  1.00 19.76  ? 78  GLU A CB  1 
ATOM   564  C  CG  . GLU A 1 78  ? 125.586 111.349 92.618  1.00 19.76  ? 78  GLU A CG  1 
ATOM   565  C  CD  . GLU A 1 78  ? 126.244 112.130 91.501  1.00 19.76  ? 78  GLU A CD  1 
ATOM   566  O  OE1 . GLU A 1 78  ? 125.933 111.853 90.327  1.00 19.76  ? 78  GLU A OE1 1 
ATOM   567  O  OE2 . GLU A 1 78  ? 127.079 113.010 91.789  1.00 19.76  ? 78  GLU A OE2 1 
ATOM   568  N  N   . VAL A 1 79  ? 122.352 111.857 92.516  1.00 15.46  ? 79  VAL A N   1 
ATOM   569  C  CA  . VAL A 1 79  ? 121.751 113.143 92.838  1.00 15.46  ? 79  VAL A CA  1 
ATOM   570  C  C   . VAL A 1 79  ? 120.429 112.995 93.557  1.00 15.46  ? 79  VAL A C   1 
ATOM   571  O  O   . VAL A 1 79  ? 119.795 113.995 93.883  1.00 15.46  ? 79  VAL A O   1 
ATOM   572  C  CB  . VAL A 1 79  ? 121.560 113.958 91.555  1.00 15.46  ? 79  VAL A CB  1 
ATOM   573  C  CG1 . VAL A 1 79  ? 120.294 113.545 90.885  1.00 15.46  ? 79  VAL A CG1 1 
ATOM   574  C  CG2 . VAL A 1 79  ? 121.551 115.411 91.849  1.00 15.46  ? 79  VAL A CG2 1 
ATOM   575  N  N   . MET A 1 80  ? 119.960 111.770 93.762  1.00 12.86  ? 80  MET A N   1 
ATOM   576  C  CA  . MET A 1 80  ? 118.826 111.562 94.650  1.00 12.86  ? 80  MET A CA  1 
ATOM   577  C  C   . MET A 1 80  ? 119.303 111.286 96.058  1.00 12.86  ? 80  MET A C   1 
ATOM   578  O  O   . MET A 1 80  ? 118.758 111.822 97.022  1.00 12.86  ? 80  MET A O   1 
ATOM   579  C  CB  . MET A 1 80  ? 117.962 110.417 94.163  1.00 12.86  ? 80  MET A CB  1 
ATOM   580  C  CG  . MET A 1 80  ? 117.220 109.779 95.263  1.00 12.86  ? 80  MET A CG  1 
ATOM   581  S  SD  . MET A 1 80  ? 115.755 110.716 95.579  1.00 12.86  ? 80  MET A SD  1 
ATOM   582  C  CE  . MET A 1 80  ? 114.612 109.746 94.633  1.00 12.86  ? 80  MET A CE  1 
ATOM   583  N  N   . GLY A 1 81  ? 120.334 110.458 96.191  1.00 12.69  ? 81  GLY A N   1 
ATOM   584  C  CA  . GLY A 1 81  ? 120.909 110.206 97.499  1.00 12.69  ? 81  GLY A CA  1 
ATOM   585  C  C   . GLY A 1 81  ? 121.171 111.482 98.267  1.00 12.69  ? 81  GLY A C   1 
ATOM   586  O  O   . GLY A 1 81  ? 120.709 111.641 99.395  1.00 12.69  ? 81  GLY A O   1 
ATOM   587  N  N   . ALA A 1 82  ? 121.881 112.427 97.652  1.00 16.52  ? 82  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 82  ? 122.129 113.705 98.306  1.00 16.52  ? 82  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 82  ? 120.843 114.292 98.853  1.00 16.52  ? 82  ALA A C   1 
ATOM   590  O  O   . ALA A 1 82  ? 120.763 114.634 100.037 1.00 16.52  ? 82  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 82  ? 122.789 114.684 97.343  1.00 16.52  ? 82  ALA A CB  1 
ATOM   592  N  N   . LEU A 1 83  ? 119.805 114.367 98.020  1.00 12.09  ? 83  LEU A N   1 
ATOM   593  C  CA  . LEU A 1 83  ? 118.527 114.882 98.492  1.00 12.09  ? 83  LEU A CA  1 
ATOM   594  C  C   . LEU A 1 83  ? 118.131 114.236 99.806  1.00 12.09  ? 83  LEU A C   1 
ATOM   595  O  O   . LEU A 1 83  ? 117.965 114.928 100.811 1.00 12.09  ? 83  LEU A O   1 
ATOM   596  C  CB  . LEU A 1 83  ? 117.434 114.655 97.466  1.00 12.09  ? 83  LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 83  ? 116.070 115.018 98.010  1.00 12.09  ? 83  LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 83  ? 116.039 116.488 98.224  1.00 12.09  ? 83  LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 83  ? 114.999 114.601 97.052  1.00 12.09  ? 83  LEU A CD2 1 
ATOM   600  N  N   . VAL A 1 84  ? 118.015 112.906 99.834  1.00 11.30  ? 84  VAL A N   1 
ATOM   601  C  CA  . VAL A 1 84  ? 117.547 112.255 101.053 1.00 11.30  ? 84  VAL A CA  1 
ATOM   602  C  C   . VAL A 1 84  ? 118.388 112.695 102.233 1.00 11.30  ? 84  VAL A C   1 
ATOM   603  O  O   . VAL A 1 84  ? 117.862 113.116 103.265 1.00 11.30  ? 84  VAL A O   1 
ATOM   604  C  CB  . VAL A 1 84  ? 117.550 110.734 100.902 1.00 11.30  ? 84  VAL A CB  1 
ATOM   605  C  CG1 . VAL A 1 84  ? 117.521 110.139 102.238 1.00 11.30  ? 84  VAL A CG1 1 
ATOM   606  C  CG2 . VAL A 1 84  ? 116.337 110.300 100.155 1.00 11.30  ? 84  VAL A CG2 1 
ATOM   607  N  N   . ASN A 1 85  ? 119.707 112.690 102.075 1.00 17.28  ? 85  ASN A N   1 
ATOM   608  C  CA  . ASN A 1 85  ? 120.556 113.141 103.169 1.00 17.28  ? 85  ASN A CA  1 
ATOM   609  C  C   . ASN A 1 85  ? 120.175 114.554 103.579 1.00 17.28  ? 85  ASN A C   1 
ATOM   610  O  O   . ASN A 1 85  ? 119.783 114.802 104.722 1.00 17.28  ? 85  ASN A O   1 
ATOM   611  C  CB  . ASN A 1 85  ? 122.023 113.084 102.756 1.00 17.28  ? 85  ASN A CB  1 
ATOM   612  C  CG  . ASN A 1 85  ? 122.643 111.754 103.025 1.00 17.28  ? 85  ASN A CG  1 
ATOM   613  O  OD1 . ASN A 1 85  ? 122.769 111.337 104.170 1.00 17.28  ? 85  ASN A OD1 1 
ATOM   614  N  ND2 . ASN A 1 85  ? 123.052 111.075 101.969 1.00 17.28  ? 85  ASN A ND2 1 
ATOM   615  N  N   . ALA A 1 86  ? 120.195 115.479 102.623 1.00 11.52  ? 86  ALA A N   1 
ATOM   616  C  CA  . ALA A 1 86  ? 119.949 116.870 102.947 1.00 11.52  ? 86  ALA A CA  1 
ATOM   617  C  C   . ALA A 1 86  ? 118.541 117.113 103.444 1.00 11.52  ? 86  ALA A C   1 
ATOM   618  O  O   . ALA A 1 86  ? 118.246 118.225 103.874 1.00 11.52  ? 86  ALA A O   1 
ATOM   619  C  CB  . ALA A 1 86  ? 120.221 117.747 101.742 1.00 11.52  ? 86  ALA A CB  1 
ATOM   620  N  N   . ILE A 1 87  ? 117.656 116.123 103.394 1.00 8.76   ? 87  ILE A N   1 
ATOM   621  C  CA  . ILE A 1 87  ? 116.393 116.258 104.111 1.00 8.76   ? 87  ILE A CA  1 
ATOM   622  C  C   . ILE A 1 87  ? 116.554 115.767 105.532 1.00 8.76   ? 87  ILE A C   1 
ATOM   623  O  O   . ILE A 1 87  ? 116.319 116.512 106.487 1.00 8.76   ? 87  ILE A O   1 
ATOM   624  C  CB  . ILE A 1 87  ? 115.264 115.494 103.409 1.00 8.76   ? 87  ILE A CB  1 
ATOM   625  C  CG1 . ILE A 1 87  ? 114.753 116.253 102.212 1.00 8.76   ? 87  ILE A CG1 1 
ATOM   626  C  CG2 . ILE A 1 87  ? 114.129 115.308 104.335 1.00 8.76   ? 87  ILE A CG2 1 
ATOM   627  C  CD1 . ILE A 1 87  ? 113.734 115.470 101.485 1.00 8.76   ? 87  ILE A CD1 1 
ATOM   628  N  N   . PHE A 1 88  ? 116.997 114.518 105.679 1.00 19.25  ? 88  PHE A N   1 
ATOM   629  C  CA  . PHE A 1 88  ? 117.160 113.908 106.988 1.00 19.25  ? 88  PHE A CA  1 
ATOM   630  C  C   . PHE A 1 88  ? 117.815 114.888 107.940 1.00 19.25  ? 88  PHE A C   1 
ATOM   631  O  O   . PHE A 1 88  ? 117.180 115.369 108.883 1.00 19.25  ? 88  PHE A O   1 
ATOM   632  C  CB  . PHE A 1 88  ? 117.987 112.633 106.849 1.00 19.25  ? 88  PHE A CB  1 
ATOM   633  C  CG  . PHE A 1 88  ? 118.377 112.008 108.148 1.00 19.25  ? 88  PHE A CG  1 
ATOM   634  C  CD1 . PHE A 1 88  ? 117.549 111.103 108.765 1.00 19.25  ? 88  PHE A CD1 1 
ATOM   635  C  CD2 . PHE A 1 88  ? 119.586 112.299 108.741 1.00 19.25  ? 88  PHE A CD2 1 
ATOM   636  C  CE1 . PHE A 1 88  ? 117.909 110.520 109.959 1.00 19.25  ? 88  PHE A CE1 1 
ATOM   637  C  CE2 . PHE A 1 88  ? 119.944 111.716 109.933 1.00 19.25  ? 88  PHE A CE2 1 
ATOM   638  C  CZ  . PHE A 1 88  ? 119.105 110.829 110.538 1.00 19.25  ? 88  PHE A CZ  1 
ATOM   639  N  N   . LEU A 1 89  ? 119.051 115.280 107.638 1.00 17.16  ? 89  LEU A N   1 
ATOM   640  C  CA  . LEU A 1 89  ? 119.766 116.256 108.447 1.00 17.16  ? 89  LEU A CA  1 
ATOM   641  C  C   . LEU A 1 89  ? 118.891 117.448 108.814 1.00 17.16  ? 89  LEU A C   1 
ATOM   642  O  O   . LEU A 1 89  ? 118.652 117.705 109.999 1.00 17.16  ? 89  LEU A O   1 
ATOM   643  C  CB  . LEU A 1 89  ? 121.015 116.716 107.710 1.00 17.16  ? 89  LEU A CB  1 
ATOM   644  C  CG  . LEU A 1 89  ? 121.617 118.005 108.225 1.00 17.16  ? 89  LEU A CG  1 
ATOM   645  C  CD1 . LEU A 1 89  ? 122.023 117.835 109.650 1.00 17.16  ? 89  LEU A CD1 1 
ATOM   646  C  CD2 . LEU A 1 89  ? 122.807 118.337 107.398 1.00 17.16  ? 89  LEU A CD2 1 
ATOM   647  N  N   . THR A 1 90  ? 118.366 118.166 107.817 1.00 17.82  ? 90  THR A N   1 
ATOM   648  C  CA  . THR A 1 90  ? 117.571 119.353 108.119 1.00 17.82  ? 90  THR A CA  1 
ATOM   649  C  C   . THR A 1 90  ? 116.400 119.009 109.021 1.00 17.82  ? 90  THR A C   1 
ATOM   650  O  O   . THR A 1 90  ? 116.170 119.678 110.029 1.00 17.82  ? 90  THR A O   1 
ATOM   651  C  CB  . THR A 1 90  ? 117.085 120.030 106.845 1.00 17.82  ? 90  THR A CB  1 
ATOM   652  O  OG1 . THR A 1 90  ? 118.182 120.693 106.214 1.00 17.82  ? 90  THR A OG1 1 
ATOM   653  C  CG2 . THR A 1 90  ? 116.048 121.043 107.168 1.00 17.82  ? 90  THR A CG2 1 
ATOM   654  N  N   . GLY A 1 91  ? 115.679 117.944 108.704 1.00 18.44  ? 91  GLY A N   1 
ATOM   655  C  CA  . GLY A 1 91  ? 114.608 117.515 109.576 1.00 18.44  ? 91  GLY A CA  1 
ATOM   656  C  C   . GLY A 1 91  ? 115.174 117.308 110.955 1.00 18.44  ? 91  GLY A C   1 
ATOM   657  O  O   . GLY A 1 91  ? 114.773 117.968 111.913 1.00 18.44  ? 91  GLY A O   1 
ATOM   658  N  N   . LEU A 1 92  ? 116.187 116.452 111.030 1.00 19.44  ? 92  LEU A N   1 
ATOM   659  C  CA  . LEU A 1 92  ? 116.861 116.190 112.292 1.00 19.44  ? 92  LEU A CA  1 
ATOM   660  C  C   . LEU A 1 92  ? 117.343 117.474 112.942 1.00 19.44  ? 92  LEU A C   1 
ATOM   661  O  O   . LEU A 1 92  ? 117.298 117.607 114.169 1.00 19.44  ? 92  LEU A O   1 
ATOM   662  C  CB  . LEU A 1 92  ? 118.025 115.242 112.053 1.00 19.44  ? 92  LEU A CB  1 
ATOM   663  C  CG  . LEU A 1 92  ? 118.869 114.804 113.223 1.00 19.44  ? 92  LEU A CG  1 
ATOM   664  C  CD1 . LEU A 1 92  ? 119.272 113.395 112.943 1.00 19.44  ? 92  LEU A CD1 1 
ATOM   665  C  CD2 . LEU A 1 92  ? 120.085 115.682 113.349 1.00 19.44  ? 92  LEU A CD2 1 
ATOM   666  N  N   . CYS A 1 93  ? 117.797 118.440 112.139 1.00 21.48  ? 93  CYS A N   1 
ATOM   667  C  CA  . CYS A 1 93  ? 118.306 119.678 112.718 1.00 21.48  ? 93  CYS A CA  1 
ATOM   668  C  C   . CYS A 1 93  ? 117.224 120.404 113.498 1.00 21.48  ? 93  CYS A C   1 
ATOM   669  O  O   . CYS A 1 93  ? 117.459 120.855 114.622 1.00 21.48  ? 93  CYS A O   1 
ATOM   670  C  CB  . CYS A 1 93  ? 118.882 120.588 111.648 1.00 21.48  ? 93  CYS A CB  1 
ATOM   671  S  SG  . CYS A 1 93  ? 119.526 122.078 112.349 1.00 21.48  ? 93  CYS A SG  1 
ATOM   672  N  N   . PHE A 1 94  ? 116.016 120.497 112.942 1.00 18.18  ? 94  PHE A N   1 
ATOM   673  C  CA  . PHE A 1 94  ? 114.940 121.116 113.705 1.00 18.18  ? 94  PHE A CA  1 
ATOM   674  C  C   . PHE A 1 94  ? 114.753 120.418 115.040 1.00 18.18  ? 94  PHE A C   1 
ATOM   675  O  O   . PHE A 1 94  ? 114.514 121.076 116.055 1.00 18.18  ? 94  PHE A O   1 
ATOM   676  C  CB  . PHE A 1 94  ? 113.641 121.110 112.910 1.00 18.18  ? 94  PHE A CB  1 
ATOM   677  C  CG  . PHE A 1 94  ? 113.589 122.153 111.844 1.00 18.18  ? 94  PHE A CG  1 
ATOM   678  C  CD1 . PHE A 1 94  ? 114.403 123.258 111.907 1.00 18.18  ? 94  PHE A CD1 1 
ATOM   679  C  CD2 . PHE A 1 94  ? 112.742 122.014 110.765 1.00 18.18  ? 94  PHE A CD2 1 
ATOM   680  C  CE1 . PHE A 1 94  ? 114.354 124.210 110.932 1.00 18.18  ? 94  PHE A CE1 1 
ATOM   681  C  CE2 . PHE A 1 94  ? 112.700 122.964 109.779 1.00 18.18  ? 94  PHE A CE2 1 
ATOM   682  C  CZ  . PHE A 1 94  ? 113.507 124.062 109.863 1.00 18.18  ? 94  PHE A CZ  1 
ATOM   683  N  N   . ALA A 1 95  ? 114.903 119.093 115.067 1.00 16.81  ? 95  ALA A N   1 
ATOM   684  C  CA  . ALA A 1 95  ? 114.797 118.374 116.327 1.00 16.81  ? 95  ALA A CA  1 
ATOM   685  C  C   . ALA A 1 95  ? 115.681 119.011 117.378 1.00 16.81  ? 95  ALA A C   1 
ATOM   686  O  O   . ALA A 1 95  ? 115.197 119.411 118.441 1.00 16.81  ? 95  ALA A O   1 
ATOM   687  C  CB  . ALA A 1 95  ? 115.160 116.909 116.141 1.00 16.81  ? 95  ALA A CB  1 
ATOM   688  N  N   . ILE A 1 96  ? 116.968 119.192 117.070 1.00 21.62  ? 96  ILE A N   1 
ATOM   689  C  CA  . ILE A 1 96  ? 117.864 119.828 118.034 1.00 21.62  ? 96  ILE A CA  1 
ATOM   690  C  C   . ILE A 1 96  ? 117.253 121.123 118.527 1.00 21.62  ? 96  ILE A C   1 
ATOM   691  O  O   . ILE A 1 96  ? 117.082 121.332 119.733 1.00 21.62  ? 96  ILE A O   1 
ATOM   692  C  CB  . ILE A 1 96  ? 119.246 120.083 117.420 1.00 21.62  ? 96  ILE A CB  1 
ATOM   693  C  CG1 . ILE A 1 96  ? 119.956 118.769 117.176 1.00 21.62  ? 96  ILE A CG1 1 
ATOM   694  C  CG2 . ILE A 1 96  ? 120.058 120.929 118.348 1.00 21.62  ? 96  ILE A CG2 1 
ATOM   695  C  CD1 . ILE A 1 96  ? 120.115 117.969 118.412 1.00 21.62  ? 96  ILE A CD1 1 
ATOM   696  N  N   . LEU A 1 97  ? 116.853 121.986 117.591 1.00 18.74  ? 97  LEU A N   1 
ATOM   697  C  CA  . LEU A 1 97  ? 116.291 123.275 117.965 1.00 18.74  ? 97  LEU A CA  1 
ATOM   698  C  C   . LEU A 1 97  ? 115.132 123.102 118.927 1.00 18.74  ? 97  LEU A C   1 
ATOM   699  O  O   . LEU A 1 97  ? 115.120 123.699 120.005 1.00 18.74  ? 97  LEU A O   1 
ATOM   700  C  CB  . LEU A 1 97  ? 115.849 124.033 116.728 1.00 18.74  ? 97  LEU A CB  1 
ATOM   701  C  CG  . LEU A 1 97  ? 115.397 125.436 117.051 1.00 18.74  ? 97  LEU A CG  1 
ATOM   702  C  CD1 . LEU A 1 97  ? 116.357 126.043 118.019 1.00 18.74  ? 97  LEU A CD1 1 
ATOM   703  C  CD2 . LEU A 1 97  ? 115.383 126.235 115.785 1.00 18.74  ? 97  LEU A CD2 1 
ATOM   704  N  N   . LEU A 1 98  ? 114.175 122.244 118.580 1.00 25.34  ? 98  LEU A N   1 
ATOM   705  C  CA  . LEU A 1 98  ? 113.070 121.975 119.491 1.00 25.34  ? 98  LEU A CA  1 
ATOM   706  C  C   . LEU A 1 98  ? 113.591 121.573 120.858 1.00 25.34  ? 98  LEU A C   1 
ATOM   707  O  O   . LEU A 1 98  ? 113.233 122.174 121.873 1.00 25.34  ? 98  LEU A O   1 
ATOM   708  C  CB  . LEU A 1 98  ? 112.184 120.885 118.909 1.00 25.34  ? 98  LEU A CB  1 
ATOM   709  C  CG  . LEU A 1 98  ? 111.025 120.321 119.702 1.00 25.34  ? 98  LEU A CG  1 
ATOM   710  C  CD1 . LEU A 1 98  ? 109.945 119.925 118.717 1.00 25.34  ? 98  LEU A CD1 1 
ATOM   711  C  CD2 . LEU A 1 98  ? 111.481 119.117 120.501 1.00 25.34  ? 98  LEU A CD2 1 
ATOM   712  N  N   . GLU A 1 99  ? 114.477 120.582 120.895 1.00 28.87  ? 99  GLU A N   1 
ATOM   713  C  CA  . GLU A 1 99  ? 115.037 120.131 122.158 1.00 28.87  ? 99  GLU A CA  1 
ATOM   714  C  C   . GLU A 1 99  ? 115.788 121.233 122.877 1.00 28.87  ? 99  GLU A C   1 
ATOM   715  O  O   . GLU A 1 99  ? 115.767 121.268 124.108 1.00 28.87  ? 99  GLU A O   1 
ATOM   716  C  CB  . GLU A 1 99  ? 115.950 118.939 121.917 1.00 28.87  ? 99  GLU A CB  1 
ATOM   717  C  CG  . GLU A 1 99  ? 116.572 118.351 123.147 1.00 28.87  ? 99  GLU A CG  1 
ATOM   718  C  CD  . GLU A 1 99  ? 117.382 117.111 122.824 1.00 28.87  ? 99  GLU A CD  1 
ATOM   719  O  OE1 . GLU A 1 99  ? 117.320 116.630 121.674 1.00 28.87  ? 99  GLU A OE1 1 
ATOM   720  O  OE2 . GLU A 1 99  ? 118.110 116.630 123.712 1.00 28.87  ? 99  GLU A OE2 1 
ATOM   721  N  N   . ALA A 1 100 ? 116.414 122.159 122.154 1.00 24.89  ? 100 ALA A N   1 
ATOM   722  C  CA  . ALA A 1 100 ? 117.101 123.244 122.838 1.00 24.89  ? 100 ALA A CA  1 
ATOM   723  C  C   . ALA A 1 100 ? 116.137 124.038 123.697 1.00 24.89  ? 100 ALA A C   1 
ATOM   724  O  O   . ALA A 1 100 ? 116.501 124.505 124.780 1.00 24.89  ? 100 ALA A O   1 
ATOM   725  C  CB  . ALA A 1 100 ? 117.786 124.160 121.838 1.00 24.89  ? 100 ALA A CB  1 
ATOM   726  N  N   . ILE A 1 101 ? 114.890 124.177 123.251 1.00 26.04  ? 101 ILE A N   1 
ATOM   727  C  CA  . ILE A 1 101 ? 113.915 124.916 124.043 1.00 26.04  ? 101 ILE A CA  1 
ATOM   728  C  C   . ILE A 1 101 ? 113.688 124.255 125.396 1.00 26.04  ? 101 ILE A C   1 
ATOM   729  O  O   . ILE A 1 101 ? 113.545 124.946 126.409 1.00 26.04  ? 101 ILE A O   1 
ATOM   730  C  CB  . ILE A 1 101 ? 112.607 125.074 123.252 1.00 26.04  ? 101 ILE A CB  1 
ATOM   731  C  CG1 . ILE A 1 101 ? 112.794 126.084 122.130 1.00 26.04  ? 101 ILE A CG1 1 
ATOM   732  C  CG2 . ILE A 1 101 ? 111.497 125.510 124.148 1.00 26.04  ? 101 ILE A CG2 1 
ATOM   733  C  CD1 . ILE A 1 101 ? 113.410 127.358 122.586 1.00 26.04  ? 101 ILE A CD1 1 
ATOM   734  N  N   . GLU A 1 102 ? 113.699 122.923 125.461 1.00 33.18  ? 102 GLU A N   1 
ATOM   735  C  CA  . GLU A 1 102 ? 113.528 122.291 126.761 1.00 33.18  ? 102 GLU A CA  1 
ATOM   736  C  C   . GLU A 1 102 ? 114.616 122.681 127.748 1.00 33.18  ? 102 GLU A C   1 
ATOM   737  O  O   . GLU A 1 102 ? 114.367 122.655 128.952 1.00 33.18  ? 102 GLU A O   1 
ATOM   738  C  CB  . GLU A 1 102 ? 113.517 120.776 126.637 1.00 33.18  ? 102 GLU A CB  1 
ATOM   739  C  CG  . GLU A 1 102 ? 112.666 120.252 125.544 1.00 33.18  ? 102 GLU A CG  1 
ATOM   740  C  CD  . GLU A 1 102 ? 111.228 120.579 125.746 1.00 33.18  ? 102 GLU A CD  1 
ATOM   741  O  OE1 . GLU A 1 102 ? 110.856 120.877 126.894 1.00 33.18  ? 102 GLU A OE1 1 
ATOM   742  O  OE2 . GLU A 1 102 ? 110.460 120.528 124.763 1.00 33.18  ? 102 GLU A OE2 1 
ATOM   743  N  N   . ARG A 1 103 ? 115.809 123.049 127.285 1.00 34.40  ? 103 ARG A N   1 
ATOM   744  C  CA  . ARG A 1 103 ? 116.861 123.432 128.213 1.00 34.40  ? 103 ARG A CA  1 
ATOM   745  C  C   . ARG A 1 103 ? 116.692 124.844 128.734 1.00 34.40  ? 103 ARG A C   1 
ATOM   746  O  O   . ARG A 1 103 ? 117.503 125.285 129.552 1.00 34.40  ? 103 ARG A O   1 
ATOM   747  C  CB  . ARG A 1 103 ? 118.237 123.320 127.566 1.00 34.40  ? 103 ARG A CB  1 
ATOM   748  C  CG  . ARG A 1 103 ? 118.598 121.965 127.068 1.00 34.40  ? 103 ARG A CG  1 
ATOM   749  C  CD  . ARG A 1 103 ? 118.784 121.031 128.211 1.00 34.40  ? 103 ARG A CD  1 
ATOM   750  N  NE  . ARG A 1 103 ? 117.561 120.299 128.449 1.00 34.40  ? 103 ARG A NE  1 
ATOM   751  C  CZ  . ARG A 1 103 ? 117.240 119.199 127.790 1.00 34.40  ? 103 ARG A CZ  1 
ATOM   752  N  NH1 . ARG A 1 103 ? 118.066 118.712 126.881 1.00 34.40  ? 103 ARG A NH1 1 
ATOM   753  N  NH2 . ARG A 1 103 ? 116.104 118.577 128.051 1.00 34.40  ? 103 ARG A NH2 1 
ATOM   754  N  N   . PHE A 1 104 ? 115.679 125.564 128.265 1.00 27.56  ? 104 PHE A N   1 
ATOM   755  C  CA  . PHE A 1 104 ? 115.344 126.880 128.773 1.00 27.56  ? 104 PHE A CA  1 
ATOM   756  C  C   . PHE A 1 104 ? 114.227 126.836 129.794 1.00 27.56  ? 104 PHE A C   1 
ATOM   757  O  O   . PHE A 1 104 ? 114.118 127.748 130.616 1.00 27.56  ? 104 PHE A O   1 
ATOM   758  C  CB  . PHE A 1 104 ? 114.923 127.773 127.612 1.00 27.56  ? 104 PHE A CB  1 
ATOM   759  C  CG  . PHE A 1 104 ? 116.062 128.367 126.867 1.00 27.56  ? 104 PHE A CG  1 
ATOM   760  C  CD1 . PHE A 1 104 ? 117.156 128.837 127.522 1.00 27.56  ? 104 PHE A CD1 1 
ATOM   761  C  CD2 . PHE A 1 104 ? 116.067 128.387 125.501 1.00 27.56  ? 104 PHE A CD2 1 
ATOM   762  C  CE1 . PHE A 1 104 ? 118.201 129.377 126.831 1.00 27.56  ? 104 PHE A CE1 1 
ATOM   763  C  CE2 . PHE A 1 104 ? 117.119 128.915 124.817 1.00 27.56  ? 104 PHE A CE2 1 
ATOM   764  C  CZ  . PHE A 1 104 ? 118.185 129.404 125.484 1.00 27.56  ? 104 PHE A CZ  1 
ATOM   765  N  N   . ILE A 1 105 ? 113.417 125.780 129.764 1.00 36.59  ? 105 ILE A N   1 
ATOM   766  C  CA  . ILE A 1 105 ? 112.231 125.650 130.592 1.00 36.59  ? 105 ILE A CA  1 
ATOM   767  C  C   . ILE A 1 105 ? 112.491 124.797 131.826 1.00 36.59  ? 105 ILE A C   1 
ATOM   768  O  O   . ILE A 1 105 ? 112.118 125.182 132.937 1.00 36.59  ? 105 ILE A O   1 
ATOM   769  C  CB  . ILE A 1 105 ? 111.061 125.073 129.765 1.00 36.59  ? 105 ILE A CB  1 
ATOM   770  C  CG1 . ILE A 1 105 ? 110.464 126.144 128.854 1.00 36.59  ? 105 ILE A CG1 1 
ATOM   771  C  CG2 . ILE A 1 105 ? 110.009 124.457 130.651 1.00 36.59  ? 105 ILE A CG2 1 
ATOM   772  C  CD1 . ILE A 1 105 ? 109.450 125.613 127.902 1.00 36.59  ? 105 ILE A CD1 1 
ATOM   773  N  N   . GLU A 1 106 ? 113.136 123.643 131.660 1.00 43.20  ? 106 GLU A N   1 
ATOM   774  C  CA  . GLU A 1 106 ? 113.493 122.751 132.763 1.00 43.20  ? 106 GLU A CA  1 
ATOM   775  C  C   . GLU A 1 106 ? 114.953 122.318 132.662 1.00 43.20  ? 106 GLU A C   1 
ATOM   776  O  O   . GLU A 1 106 ? 115.257 121.189 132.266 1.00 43.20  ? 106 GLU A O   1 
ATOM   777  C  CB  . GLU A 1 106 ? 112.550 121.549 132.799 1.00 43.20  ? 106 GLU A CB  1 
ATOM   778  C  CG  . GLU A 1 106 ? 112.540 120.632 131.556 1.00 43.20  ? 106 GLU A CG  1 
ATOM   779  C  CD  . GLU A 1 106 ? 111.407 119.606 131.586 1.00 43.20  ? 106 GLU A CD  1 
ATOM   780  O  OE1 . GLU A 1 106 ? 111.628 118.472 132.063 1.00 43.20  ? 106 GLU A OE1 1 
ATOM   781  O  OE2 . GLU A 1 106 ? 110.289 119.924 131.124 1.00 43.20  ? 106 GLU A OE2 1 
ATOM   782  N  N   . PRO A 1 107 ? 115.886 123.187 133.044 1.00 42.92  ? 107 PRO A N   1 
ATOM   783  C  CA  . PRO A 1 107 ? 117.301 122.894 132.807 1.00 42.92  ? 107 PRO A CA  1 
ATOM   784  C  C   . PRO A 1 107 ? 117.775 121.722 133.639 1.00 42.92  ? 107 PRO A C   1 
ATOM   785  O  O   . PRO A 1 107 ? 117.555 121.667 134.846 1.00 42.92  ? 107 PRO A O   1 
ATOM   786  C  CB  . PRO A 1 107 ? 117.999 124.183 133.237 1.00 42.92  ? 107 PRO A CB  1 
ATOM   787  C  CG  . PRO A 1 107 ? 117.119 124.734 134.265 1.00 42.92  ? 107 PRO A CG  1 
ATOM   788  C  CD  . PRO A 1 107 ? 115.718 124.408 133.843 1.00 42.92  ? 107 PRO A CD  1 
ATOM   789  N  N   . HIS A 1 108 ? 118.399 120.767 132.970 1.00 46.63  ? 108 HIS A N   1 
ATOM   790  C  CA  . HIS A 1 108 ? 118.924 119.568 133.670 1.00 46.63  ? 108 HIS A CA  1 
ATOM   791  C  C   . HIS A 1 108 ? 120.332 119.863 134.193 1.00 46.63  ? 108 HIS A C   1 
ATOM   792  O  O   . HIS A 1 108 ? 120.824 120.986 133.979 1.00 46.63  ? 108 HIS A O   1 
ATOM   793  C  CB  . HIS A 1 108 ? 118.886 118.346 132.743 1.00 46.63  ? 108 HIS A CB  1 
ATOM   794  C  CG  . HIS A 1 108 ? 117.509 117.970 132.310 1.00 46.63  ? 108 HIS A CG  1 
ATOM   795  N  ND1 . HIS A 1 108 ? 117.114 116.655 132.170 1.00 46.63  ? 108 HIS A ND1 1 
ATOM   796  C  CD2 . HIS A 1 108 ? 116.438 118.725 131.987 1.00 46.63  ? 108 HIS A CD2 1 
ATOM   797  C  CE1 . HIS A 1 108 ? 115.857 116.616 131.777 1.00 46.63  ? 108 HIS A CE1 1 
ATOM   798  N  NE2 . HIS A 1 108 ? 115.419 117.874 131.658 1.00 46.63  ? 108 HIS A NE2 1 
ATOM   799  N  N   . GLU A 1 109 ? 120.944 118.897 134.854 1.00 44.59  ? 109 GLU A N   1 
ATOM   800  C  CA  . GLU A 1 109 ? 122.284 119.043 135.392 1.00 44.59  ? 109 GLU A CA  1 
ATOM   801  C  C   . GLU A 1 109 ? 123.208 117.944 134.901 1.00 44.59  ? 109 GLU A C   1 
ATOM   802  O  O   . GLU A 1 109 ? 122.898 116.755 135.007 1.00 44.59  ? 109 GLU A O   1 
ATOM   803  C  CB  . GLU A 1 109 ? 122.271 119.066 136.900 1.00 44.59  ? 109 GLU A CB  1 
ATOM   804  C  CG  . GLU A 1 109 ? 122.043 120.437 137.390 1.00 44.59  ? 109 GLU A CG  1 
ATOM   805  C  CD  . GLU A 1 109 ? 123.184 121.334 136.997 1.00 44.59  ? 109 GLU A CD  1 
ATOM   806  O  OE1 . GLU A 1 109 ? 124.337 120.871 137.022 1.00 44.59  ? 109 GLU A OE1 1 
ATOM   807  O  OE2 . GLU A 1 109 ? 122.929 122.493 136.628 1.00 44.59  ? 109 GLU A OE2 1 
ATOM   808  N  N   . MET A 1 110 ? 124.353 118.367 134.372 1.00 38.94  ? 110 MET A N   1 
ATOM   809  C  CA  . MET A 1 110 ? 125.424 117.474 133.950 1.00 38.94  ? 110 MET A CA  1 
ATOM   810  C  C   . MET A 1 110 ? 126.142 117.013 135.210 1.00 38.94  ? 110 MET A C   1 
ATOM   811  O  O   . MET A 1 110 ? 127.047 117.668 135.726 1.00 38.94  ? 110 MET A O   1 
ATOM   812  C  CB  . MET A 1 110 ? 126.364 118.197 133.001 1.00 38.94  ? 110 MET A CB  1 
ATOM   813  C  CG  . MET A 1 110 ? 127.604 117.442 132.680 1.00 38.94  ? 110 MET A CG  1 
ATOM   814  S  SD  . MET A 1 110 ? 128.925 118.578 132.291 1.00 38.94  ? 110 MET A SD  1 
ATOM   815  C  CE  . MET A 1 110 ? 128.031 119.766 131.304 1.00 38.94  ? 110 MET A CE  1 
ATOM   816  N  N   . GLN A 1 111 ? 125.708 115.866 135.730 1.00 40.15  ? 111 GLN A N   1 
ATOM   817  C  CA  . GLN A 1 111 ? 126.199 115.419 137.026 1.00 40.15  ? 111 GLN A CA  1 
ATOM   818  C  C   . GLN A 1 111 ? 127.704 115.187 137.007 1.00 40.15  ? 111 GLN A C   1 
ATOM   819  O  O   . GLN A 1 111 ? 128.449 115.817 137.764 1.00 40.15  ? 111 GLN A O   1 
ATOM   820  C  CB  . GLN A 1 111 ? 125.464 114.152 137.451 1.00 40.15  ? 111 GLN A CB  1 
ATOM   821  C  CG  . GLN A 1 111 ? 123.971 114.333 137.568 1.00 40.15  ? 111 GLN A CG  1 
ATOM   822  C  CD  . GLN A 1 111 ? 123.543 114.714 138.965 1.00 40.15  ? 111 GLN A CD  1 
ATOM   823  O  OE1 . GLN A 1 111 ? 124.371 115.053 139.808 1.00 40.15  ? 111 GLN A OE1 1 
ATOM   824  N  NE2 . GLN A 1 111 ? 122.243 114.656 139.220 1.00 40.15  ? 111 GLN A NE2 1 
ATOM   825  N  N   . GLN A 1 112 ? 128.176 114.299 136.133 1.00 36.12  ? 112 GLN A N   1 
ATOM   826  C  CA  . GLN A 1 112 ? 129.582 113.900 136.094 1.00 36.12  ? 112 GLN A CA  1 
ATOM   827  C  C   . GLN A 1 112 ? 130.261 114.623 134.940 1.00 36.12  ? 112 GLN A C   1 
ATOM   828  O  O   . GLN A 1 112 ? 130.137 114.208 133.780 1.00 36.12  ? 112 GLN A O   1 
ATOM   829  C  CB  . GLN A 1 112 ? 129.710 112.385 135.958 1.00 36.12  ? 112 GLN A CB  1 
ATOM   830  N  N   . PRO A 1 113 ? 130.987 115.711 135.206 1.00 34.42  ? 113 PRO A N   1 
ATOM   831  C  CA  . PRO A 1 113 ? 131.548 116.498 134.104 1.00 34.42  ? 113 PRO A CA  1 
ATOM   832  C  C   . PRO A 1 113 ? 132.890 116.011 133.620 1.00 34.42  ? 113 PRO A C   1 
ATOM   833  O  O   . PRO A 1 113 ? 133.195 116.195 132.439 1.00 34.42  ? 113 PRO A O   1 
ATOM   834  C  CB  . PRO A 1 113 ? 131.666 117.888 134.708 1.00 34.42  ? 113 PRO A CB  1 
ATOM   835  C  CG  . PRO A 1 113 ? 132.003 117.594 136.112 1.00 34.42  ? 113 PRO A CG  1 
ATOM   836  C  CD  . PRO A 1 113 ? 131.276 116.327 136.503 1.00 34.42  ? 113 PRO A CD  1 
ATOM   837  N  N   . LEU A 1 114 ? 133.714 115.412 134.473 1.00 30.24  ? 114 LEU A N   1 
ATOM   838  C  CA  . LEU A 1 114 ? 134.965 114.862 133.970 1.00 30.24  ? 114 LEU A CA  1 
ATOM   839  C  C   . LEU A 1 114 ? 134.702 113.781 132.931 1.00 30.24  ? 114 LEU A C   1 
ATOM   840  O  O   . LEU A 1 114 ? 135.308 113.791 131.854 1.00 30.24  ? 114 LEU A O   1 
ATOM   841  C  CB  . LEU A 1 114 ? 135.806 114.313 135.124 1.00 30.24  ? 114 LEU A CB  1 
ATOM   842  C  CG  . LEU A 1 114 ? 136.911 113.282 134.833 1.00 30.24  ? 114 LEU A CG  1 
ATOM   843  C  CD1 . LEU A 1 114 ? 138.154 113.919 134.217 1.00 30.24  ? 114 LEU A CD1 1 
ATOM   844  C  CD2 . LEU A 1 114 ? 137.283 112.498 136.091 1.00 30.24  ? 114 LEU A CD2 1 
ATOM   845  N  N   . VAL A 1 115 ? 133.778 112.865 133.209 1.00 26.03  ? 115 VAL A N   1 
ATOM   846  C  CA  . VAL A 1 115 ? 133.562 111.769 132.278 1.00 26.03  ? 115 VAL A CA  1 
ATOM   847  C  C   . VAL A 1 115 ? 132.959 112.281 130.981 1.00 26.03  ? 115 VAL A C   1 
ATOM   848  O  O   . VAL A 1 115 ? 133.300 111.798 129.895 1.00 26.03  ? 115 VAL A O   1 
ATOM   849  C  CB  . VAL A 1 115 ? 132.697 110.674 132.918 1.00 26.03  ? 115 VAL A CB  1 
ATOM   850  C  CG1 . VAL A 1 115 ? 131.255 111.078 132.970 1.00 26.03  ? 115 VAL A CG1 1 
ATOM   851  C  CG2 . VAL A 1 115 ? 132.836 109.411 132.145 1.00 26.03  ? 115 VAL A CG2 1 
ATOM   852  N  N   . VAL A 1 116 ? 132.065 113.269 131.057 1.00 25.95  ? 116 VAL A N   1 
ATOM   853  C  CA  . VAL A 1 116 ? 131.468 113.788 129.831 1.00 25.95  ? 116 VAL A CA  1 
ATOM   854  C  C   . VAL A 1 116 ? 132.512 114.515 129.011 1.00 25.95  ? 116 VAL A C   1 
ATOM   855  O  O   . VAL A 1 116 ? 132.533 114.407 127.787 1.00 25.95  ? 116 VAL A O   1 
ATOM   856  C  CB  . VAL A 1 116 ? 130.260 114.688 130.129 1.00 25.95  ? 116 VAL A CB  1 
ATOM   857  C  CG1 . VAL A 1 116 ? 129.963 115.545 128.929 1.00 25.95  ? 116 VAL A CG1 1 
ATOM   858  C  CG2 . VAL A 1 116 ? 129.053 113.846 130.468 1.00 25.95  ? 116 VAL A CG2 1 
ATOM   859  N  N   . LEU A 1 117 ? 133.408 115.250 129.664 1.00 25.20  ? 117 LEU A N   1 
ATOM   860  C  CA  . LEU A 1 117 ? 134.508 115.849 128.923 1.00 25.20  ? 117 LEU A CA  1 
ATOM   861  C  C   . LEU A 1 117 ? 135.342 114.777 128.253 1.00 25.20  ? 117 LEU A C   1 
ATOM   862  O  O   . LEU A 1 117 ? 135.772 114.940 127.107 1.00 25.20  ? 117 LEU A O   1 
ATOM   863  C  CB  . LEU A 1 117 ? 135.376 116.693 129.841 1.00 25.20  ? 117 LEU A CB  1 
ATOM   864  C  CG  . LEU A 1 117 ? 136.712 117.103 129.249 1.00 25.20  ? 117 LEU A CG  1 
ATOM   865  C  CD1 . LEU A 1 117 ? 136.512 117.827 127.949 1.00 25.20  ? 117 LEU A CD1 1 
ATOM   866  C  CD2 . LEU A 1 117 ? 137.430 117.992 130.229 1.00 25.20  ? 117 LEU A CD2 1 
ATOM   867  N  N   . GLY A 1 118 ? 135.557 113.659 128.940 1.00 25.12  ? 118 GLY A N   1 
ATOM   868  C  CA  . GLY A 1 118 ? 136.336 112.586 128.340 1.00 25.12  ? 118 GLY A CA  1 
ATOM   869  C  C   . GLY A 1 118 ? 135.711 112.052 127.064 1.00 25.12  ? 118 GLY A C   1 
ATOM   870  O  O   . GLY A 1 118 ? 136.334 112.058 125.995 1.00 25.12  ? 118 GLY A O   1 
ATOM   871  N  N   . VAL A 1 119 ? 134.466 111.596 127.150 1.00 23.92  ? 119 VAL A N   1 
ATOM   872  C  CA  . VAL A 1 119 ? 133.885 111.001 125.956 1.00 23.92  ? 119 VAL A CA  1 
ATOM   873  C  C   . VAL A 1 119 ? 133.595 112.060 124.909 1.00 23.92  ? 119 VAL A C   1 
ATOM   874  O  O   . VAL A 1 119 ? 133.594 111.767 123.712 1.00 23.92  ? 119 VAL A O   1 
ATOM   875  C  CB  . VAL A 1 119 ? 132.634 110.191 126.287 1.00 23.92  ? 119 VAL A CB  1 
ATOM   876  C  CG1 . VAL A 1 119 ? 132.920 109.304 127.458 1.00 23.92  ? 119 VAL A CG1 1 
ATOM   877  C  CG2 . VAL A 1 119 ? 131.476 111.112 126.523 1.00 23.92  ? 119 VAL A CG2 1 
ATOM   878  N  N   . GLY A 1 120 ? 133.393 113.307 125.314 1.00 21.93  ? 120 GLY A N   1 
ATOM   879  C  CA  . GLY A 1 120 ? 133.200 114.350 124.329 1.00 21.93  ? 120 GLY A CA  1 
ATOM   880  C  C   . GLY A 1 120 ? 134.460 114.637 123.545 1.00 21.93  ? 120 GLY A C   1 
ATOM   881  O  O   . GLY A 1 120 ? 134.403 114.892 122.344 1.00 21.93  ? 120 GLY A O   1 
ATOM   882  N  N   . VAL A 1 121 ? 135.617 114.581 124.201 1.00 23.71  ? 121 VAL A N   1 
ATOM   883  C  CA  . VAL A 1 121 ? 136.847 114.819 123.464 1.00 23.71  ? 121 VAL A CA  1 
ATOM   884  C  C   . VAL A 1 121 ? 137.181 113.615 122.594 1.00 23.71  ? 121 VAL A C   1 
ATOM   885  O  O   . VAL A 1 121 ? 137.704 113.767 121.483 1.00 23.71  ? 121 VAL A O   1 
ATOM   886  C  CB  . VAL A 1 121 ? 137.997 115.191 124.413 1.00 23.71  ? 121 VAL A CB  1 
ATOM   887  C  CG1 . VAL A 1 121 ? 138.617 113.967 125.024 1.00 23.71  ? 121 VAL A CG1 1 
ATOM   888  C  CG2 . VAL A 1 121 ? 139.029 116.009 123.678 1.00 23.71  ? 121 VAL A CG2 1 
ATOM   889  N  N   . ALA A 1 122 ? 136.837 112.408 123.039 1.00 24.49  ? 122 ALA A N   1 
ATOM   890  C  CA  . ALA A 1 122 ? 137.029 111.262 122.154 1.00 24.49  ? 122 ALA A CA  1 
ATOM   891  C  C   . ALA A 1 122 ? 136.162 111.386 120.905 1.00 24.49  ? 122 ALA A C   1 
ATOM   892  O  O   . ALA A 1 122 ? 136.642 111.195 119.783 1.00 24.49  ? 122 ALA A O   1 
ATOM   893  C  CB  . ALA A 1 122 ? 136.735 109.960 122.884 1.00 24.49  ? 122 ALA A CB  1 
ATOM   894  N  N   . GLY A 1 123 ? 134.885 111.723 121.079 1.00 24.79  ? 123 GLY A N   1 
ATOM   895  C  CA  . GLY A 1 123 ? 134.013 111.899 119.929 1.00 24.79  ? 123 GLY A CA  1 
ATOM   896  C  C   . GLY A 1 123 ? 134.449 113.032 119.020 1.00 24.79  ? 123 GLY A C   1 
ATOM   897  O  O   . GLY A 1 123 ? 134.353 112.932 117.796 1.00 24.79  ? 123 GLY A O   1 
ATOM   898  N  N   . LEU A 1 124 ? 134.939 114.122 119.601 1.00 26.65  ? 124 LEU A N   1 
ATOM   899  C  CA  . LEU A 1 124 ? 135.417 115.241 118.798 1.00 26.65  ? 124 LEU A CA  1 
ATOM   900  C  C   . LEU A 1 124 ? 136.622 114.845 117.961 1.00 26.65  ? 124 LEU A C   1 
ATOM   901  O  O   . LEU A 1 124 ? 136.753 115.277 116.815 1.00 26.65  ? 124 LEU A O   1 
ATOM   902  C  CB  . LEU A 1 124 ? 135.737 116.422 119.715 1.00 26.65  ? 124 LEU A CB  1 
ATOM   903  C  CG  . LEU A 1 124 ? 136.679 117.542 119.303 1.00 26.65  ? 124 LEU A CG  1 
ATOM   904  C  CD1 . LEU A 1 124 ? 136.150 118.246 118.087 1.00 26.65  ? 124 LEU A CD1 1 
ATOM   905  C  CD2 . LEU A 1 124 ? 136.840 118.515 120.454 1.00 26.65  ? 124 LEU A CD2 1 
ATOM   906  N  N   . LEU A 1 125 ? 137.498 113.997 118.498 1.00 24.34  ? 125 LEU A N   1 
ATOM   907  C  CA  . LEU A 1 125 ? 138.626 113.537 117.695 1.00 24.34  ? 125 LEU A CA  1 
ATOM   908  C  C   . LEU A 1 125 ? 138.188 112.572 116.597 1.00 24.34  ? 125 LEU A C   1 
ATOM   909  O  O   . LEU A 1 125 ? 138.678 112.654 115.461 1.00 24.34  ? 125 LEU A O   1 
ATOM   910  C  CB  . LEU A 1 125 ? 139.679 112.895 118.584 1.00 24.34  ? 125 LEU A CB  1 
ATOM   911  C  CG  . LEU A 1 125 ? 140.290 113.854 119.601 1.00 24.34  ? 125 LEU A CG  1 
ATOM   912  C  CD1 . LEU A 1 125 ? 141.629 113.336 120.091 1.00 24.34  ? 125 LEU A CD1 1 
ATOM   913  C  CD2 . LEU A 1 125 ? 140.445 115.241 119.012 1.00 24.34  ? 125 LEU A CD2 1 
ATOM   914  N  N   . VAL A 1 126 ? 137.263 111.657 116.897 1.00 26.69  ? 126 VAL A N   1 
ATOM   915  C  CA  . VAL A 1 126 ? 136.842 110.740 115.838 1.00 26.69  ? 126 VAL A CA  1 
ATOM   916  C  C   . VAL A 1 126 ? 136.123 111.500 114.731 1.00 26.69  ? 126 VAL A C   1 
ATOM   917  O  O   . VAL A 1 126 ? 136.256 111.160 113.554 1.00 26.69  ? 126 VAL A O   1 
ATOM   918  C  CB  . VAL A 1 126 ? 135.972 109.591 116.373 1.00 26.69  ? 126 VAL A CB  1 
ATOM   919  C  CG1 . VAL A 1 126 ? 134.527 109.982 116.455 1.00 26.69  ? 126 VAL A CG1 1 
ATOM   920  C  CG2 . VAL A 1 126 ? 136.112 108.416 115.493 1.00 26.69  ? 126 VAL A CG2 1 
ATOM   921  N  N   . ASN A 1 127 ? 135.397 112.572 115.058 1.00 31.20  ? 127 ASN A N   1 
ATOM   922  C  CA  . ASN A 1 127 ? 134.746 113.330 113.993 1.00 31.20  ? 127 ASN A CA  1 
ATOM   923  C  C   . ASN A 1 127 ? 135.703 114.282 113.290 1.00 31.20  ? 127 ASN A C   1 
ATOM   924  O  O   . ASN A 1 127 ? 135.504 114.575 112.113 1.00 31.20  ? 127 ASN A O   1 
ATOM   925  C  CB  . ASN A 1 127 ? 133.531 114.079 114.524 1.00 31.20  ? 127 ASN A CB  1 
ATOM   926  C  CG  . ASN A 1 127 ? 132.399 113.147 114.875 1.00 31.20  ? 127 ASN A CG  1 
ATOM   927  O  OD1 . ASN A 1 127 ? 132.021 113.011 116.035 1.00 31.20  ? 127 ASN A OD1 1 
ATOM   928  N  ND2 . ASN A 1 127 ? 131.855 112.486 113.868 1.00 31.20  ? 127 ASN A ND2 1 
ATOM   929  N  N   . VAL A 1 128 ? 136.746 114.772 113.960 1.00 28.68  ? 128 VAL A N   1 
ATOM   930  C  CA  . VAL A 1 128 ? 137.762 115.499 113.209 1.00 28.68  ? 128 VAL A CA  1 
ATOM   931  C  C   . VAL A 1 128 ? 138.387 114.587 112.178 1.00 28.68  ? 128 VAL A C   1 
ATOM   932  O  O   . VAL A 1 128 ? 138.679 115.011 111.058 1.00 28.68  ? 128 VAL A O   1 
ATOM   933  C  CB  . VAL A 1 128 ? 138.828 116.103 114.132 1.00 28.68  ? 128 VAL A CB  1 
ATOM   934  C  CG1 . VAL A 1 128 ? 140.114 116.290 113.369 1.00 28.68  ? 128 VAL A CG1 1 
ATOM   935  C  CG2 . VAL A 1 128 ? 138.366 117.438 114.653 1.00 28.68  ? 128 VAL A CG2 1 
ATOM   936  N  N   . LEU A 1 129 ? 138.574 113.312 112.516 1.00 31.07  ? 129 LEU A N   1 
ATOM   937  C  CA  . LEU A 1 129 ? 139.061 112.380 111.499 1.00 31.07  ? 129 LEU A CA  1 
ATOM   938  C  C   . LEU A 1 129 ? 138.020 112.139 110.411 1.00 31.07  ? 129 LEU A C   1 
ATOM   939  O  O   . LEU A 1 129 ? 138.358 112.099 109.224 1.00 31.07  ? 129 LEU A O   1 
ATOM   940  C  CB  . LEU A 1 129 ? 139.477 111.059 112.125 1.00 31.07  ? 129 LEU A CB  1 
ATOM   941  C  CG  . LEU A 1 129 ? 140.263 110.182 111.160 1.00 31.07  ? 129 LEU A CG  1 
ATOM   942  C  CD1 . LEU A 1 129 ? 141.312 109.426 111.935 1.00 31.07  ? 129 LEU A CD1 1 
ATOM   943  C  CD2 . LEU A 1 129 ? 139.357 109.222 110.425 1.00 31.07  ? 129 LEU A CD2 1 
ATOM   944  N  N   . GLY A 1 130 ? 136.758 111.958 110.792 1.00 30.17  ? 130 GLY A N   1 
ATOM   945  C  CA  . GLY A 1 130 ? 135.723 111.748 109.792 1.00 30.17  ? 130 GLY A CA  1 
ATOM   946  C  C   . GLY A 1 130 ? 135.539 112.942 108.873 1.00 30.17  ? 130 GLY A C   1 
ATOM   947  O  O   . GLY A 1 130 ? 134.998 112.819 107.775 1.00 30.17  ? 130 GLY A O   1 
ATOM   948  N  N   . LEU A 1 131 ? 135.953 114.117 109.327 1.00 33.20  ? 131 LEU A N   1 
ATOM   949  C  CA  . LEU A 1 131 ? 135.890 115.310 108.496 1.00 33.20  ? 131 LEU A CA  1 
ATOM   950  C  C   . LEU A 1 131 ? 137.130 115.429 107.625 1.00 33.20  ? 131 LEU A C   1 
ATOM   951  O  O   . LEU A 1 131 ? 137.034 115.774 106.445 1.00 33.20  ? 131 LEU A O   1 
ATOM   952  C  CB  . LEU A 1 131 ? 135.730 116.531 109.397 1.00 33.20  ? 131 LEU A CB  1 
ATOM   953  C  CG  . LEU A 1 131 ? 135.644 117.983 108.952 1.00 33.20  ? 131 LEU A CG  1 
ATOM   954  C  CD1 . LEU A 1 131 ? 135.058 118.753 110.110 1.00 33.20  ? 131 LEU A CD1 1 
ATOM   955  C  CD2 . LEU A 1 131 ? 137.002 118.558 108.605 1.00 33.20  ? 131 LEU A CD2 1 
ATOM   956  N  N   . CYS A 1 132 ? 138.306 115.163 108.195 1.00 30.90  ? 132 CYS A N   1 
ATOM   957  C  CA  . CYS A 1 132 ? 139.546 115.224 107.439 1.00 30.90  ? 132 CYS A CA  1 
ATOM   958  C  C   . CYS A 1 132 ? 139.663 114.078 106.455 1.00 30.90  ? 132 CYS A C   1 
ATOM   959  O  O   . CYS A 1 132 ? 140.592 114.066 105.647 1.00 30.90  ? 132 CYS A O   1 
ATOM   960  C  CB  . CYS A 1 132 ? 140.732 115.217 108.393 1.00 30.90  ? 132 CYS A CB  1 
ATOM   961  S  SG  . CYS A 1 132 ? 142.303 115.612 107.652 1.00 30.90  ? 132 CYS A SG  1 
ATOM   962  N  N   . LEU A 1 133 ? 138.757 113.106 106.517 1.00 30.30  ? 133 LEU A N   1 
ATOM   963  C  CA  . LEU A 1 133 ? 138.733 112.058 105.505 1.00 30.30  ? 133 LEU A CA  1 
ATOM   964  C  C   . LEU A 1 133 ? 138.194 112.581 104.181 1.00 30.30  ? 133 LEU A C   1 
ATOM   965  O  O   . LEU A 1 133 ? 138.683 112.197 103.116 1.00 30.30  ? 133 LEU A O   1 
ATOM   966  C  CB  . LEU A 1 133 ? 137.899 110.887 105.997 1.00 30.30  ? 133 LEU A CB  1 
ATOM   967  C  CG  . LEU A 1 133 ? 138.029 109.599 105.221 1.00 30.30  ? 133 LEU A CG  1 
ATOM   968  C  CD1 . LEU A 1 133 ? 139.472 109.217 105.202 1.00 30.30  ? 133 LEU A CD1 1 
ATOM   969  C  CD2 . LEU A 1 133 ? 137.218 108.542 105.912 1.00 30.30  ? 133 LEU A CD2 1 
ATOM   970  N  N   . PHE A 1 134 ? 137.187 113.454 104.227 1.00 31.58  ? 134 PHE A N   1 
ATOM   971  C  CA  . PHE A 1 134 ? 136.624 114.083 103.031 1.00 31.58  ? 134 PHE A CA  1 
ATOM   972  C  C   . PHE A 1 134 ? 137.246 115.445 102.769 1.00 31.58  ? 134 PHE A C   1 
ATOM   973  O  O   . PHE A 1 134 ? 137.968 115.628 101.795 1.00 31.58  ? 134 PHE A O   1 
ATOM   974  C  CB  . PHE A 1 134 ? 135.122 114.242 103.170 1.00 31.58  ? 134 PHE A CB  1 
ATOM   975  C  CG  . PHE A 1 134 ? 134.425 112.999 103.590 1.00 31.58  ? 134 PHE A CG  1 
ATOM   976  C  CD1 . PHE A 1 134 ? 134.127 112.023 102.680 1.00 31.58  ? 134 PHE A CD1 1 
ATOM   977  C  CD2 . PHE A 1 134 ? 134.071 112.803 104.902 1.00 31.58  ? 134 PHE A CD2 1 
ATOM   978  C  CE1 . PHE A 1 134 ? 133.481 110.879 103.076 1.00 31.58  ? 134 PHE A CE1 1 
ATOM   979  C  CE2 . PHE A 1 134 ? 133.424 111.663 105.300 1.00 31.58  ? 134 PHE A CE2 1 
ATOM   980  C  CZ  . PHE A 1 134 ? 133.133 110.701 104.391 1.00 31.58  ? 134 PHE A CZ  1 
ATOM   981  N  N   . GLY A 1 241 ? 130.135 110.721 91.720  1.00 25.24  ? 241 GLY A N   1 
ATOM   982  C  CA  . GLY A 1 241 ? 129.565 111.027 93.019  1.00 25.24  ? 241 GLY A CA  1 
ATOM   983  C  C   . GLY A 1 241 ? 130.088 112.326 93.590  1.00 25.24  ? 241 GLY A C   1 
ATOM   984  O  O   . GLY A 1 241 ? 131.032 112.341 94.375  1.00 25.24  ? 241 GLY A O   1 
ATOM   985  N  N   . GLN A 1 242 ? 129.466 113.427 93.191  1.00 29.91  ? 242 GLN A N   1 
ATOM   986  C  CA  . GLN A 1 242 ? 129.906 114.742 93.628  1.00 29.91  ? 242 GLN A CA  1 
ATOM   987  C  C   . GLN A 1 242 ? 128.959 115.404 94.601  1.00 29.91  ? 242 GLN A C   1 
ATOM   988  O  O   . GLN A 1 242 ? 129.324 116.435 95.166  1.00 29.91  ? 242 GLN A O   1 
ATOM   989  C  CB  . GLN A 1 242 ? 130.096 115.668 92.420  1.00 29.91  ? 242 GLN A CB  1 
ATOM   990  C  CG  . GLN A 1 242 ? 128.801 115.967 91.681  1.00 29.91  ? 242 GLN A CG  1 
ATOM   991  C  CD  . GLN A 1 242 ? 128.983 116.920 90.519  1.00 29.91  ? 242 GLN A CD  1 
ATOM   992  O  OE1 . GLN A 1 242 ? 129.440 118.050 90.689  1.00 29.91  ? 242 GLN A OE1 1 
ATOM   993  N  NE2 . GLN A 1 242 ? 128.621 116.466 89.327  1.00 29.91  ? 242 GLN A NE2 1 
ATOM   994  N  N   . LEU A 1 243 ? 127.758 114.869 94.806  1.00 28.00  ? 243 LEU A N   1 
ATOM   995  C  CA  . LEU A 1 243 ? 126.852 115.423 95.802  1.00 28.00  ? 243 LEU A CA  1 
ATOM   996  C  C   . LEU A 1 243 ? 126.726 114.503 97.009  1.00 28.00  ? 243 LEU A C   1 
ATOM   997  O  O   . LEU A 1 243 ? 126.258 114.921 98.066  1.00 28.00  ? 243 LEU A O   1 
ATOM   998  C  CB  . LEU A 1 243 ? 125.484 115.702 95.187  1.00 28.00  ? 243 LEU A CB  1 
ATOM   999  C  CG  . LEU A 1 243 ? 125.442 116.962 94.339  1.00 28.00  ? 243 LEU A CG  1 
ATOM   1000 C  CD1 . LEU A 1 243 ? 124.051 117.200 93.867  1.00 28.00  ? 243 LEU A CD1 1 
ATOM   1001 C  CD2 . LEU A 1 243 ? 125.926 118.133 95.132  1.00 28.00  ? 243 LEU A CD2 1 
ATOM   1002 N  N   . ASN A 1 244 ? 127.129 113.242 96.881  1.00 26.97  ? 244 ASN A N   1 
ATOM   1003 C  CA  . ASN A 1 244 ? 127.231 112.435 98.087  1.00 26.97  ? 244 ASN A CA  1 
ATOM   1004 C  C   . ASN A 1 244 ? 128.348 112.919 98.994  1.00 26.97  ? 244 ASN A C   1 
ATOM   1005 O  O   . ASN A 1 244 ? 128.181 112.949 100.219 1.00 26.97  ? 244 ASN A O   1 
ATOM   1006 C  CB  . ASN A 1 244 ? 127.429 110.976 97.745  1.00 26.97  ? 244 ASN A CB  1 
ATOM   1007 C  CG  . ASN A 1 244 ? 126.144 110.295 97.486  1.00 26.97  ? 244 ASN A CG  1 
ATOM   1008 O  OD1 . ASN A 1 244 ? 125.131 110.653 98.064  1.00 26.97  ? 244 ASN A OD1 1 
ATOM   1009 N  ND2 . ASN A 1 244 ? 126.167 109.281 96.647  1.00 26.97  ? 244 ASN A ND2 1 
ATOM   1010 N  N   . MET A 1 245 ? 129.494 113.286 98.426  1.00 34.15  ? 245 MET A N   1 
ATOM   1011 C  CA  . MET A 1 245 ? 130.527 113.943 99.214  1.00 34.15  ? 245 MET A CA  1 
ATOM   1012 C  C   . MET A 1 245 ? 129.938 115.063 100.063 1.00 34.15  ? 245 MET A C   1 
ATOM   1013 O  O   . MET A 1 245 ? 130.161 115.117 101.274 1.00 34.15  ? 245 MET A O   1 
ATOM   1014 C  CB  . MET A 1 245 ? 131.620 114.496 98.303  1.00 34.15  ? 245 MET A CB  1 
ATOM   1015 C  CG  . MET A 1 245 ? 132.545 115.472 99.006  1.00 34.15  ? 245 MET A CG  1 
ATOM   1016 S  SD  . MET A 1 245 ? 133.745 116.236 97.918  1.00 34.15  ? 245 MET A SD  1 
ATOM   1017 C  CE  . MET A 1 245 ? 134.359 117.504 99.010  1.00 34.15  ? 245 MET A CE  1 
ATOM   1018 N  N   . ARG A 1 246 ? 129.175 115.952 99.442  1.00 31.40  ? 246 ARG A N   1 
ATOM   1019 C  CA  . ARG A 1 246 ? 128.600 117.106 100.181 1.00 31.40  ? 246 ARG A CA  1 
ATOM   1020 C  C   . ARG A 1 246 ? 127.534 116.634 101.173 1.00 31.40  ? 246 ARG A C   1 
ATOM   1021 O  O   . ARG A 1 246 ? 127.539 117.129 102.306 1.00 31.40  ? 246 ARG A O   1 
ATOM   1022 C  CB  . ARG A 1 246 ? 128.018 118.126 99.201  1.00 31.40  ? 246 ARG A CB  1 
ATOM   1023 C  CG  . ARG A 1 246 ? 128.774 119.445 99.172  1.00 31.40  ? 246 ARG A CG  1 
ATOM   1024 C  CD  . ARG A 1 246 ? 129.013 119.918 97.752  1.00 31.40  ? 246 ARG A CD  1 
ATOM   1025 N  NE  . ARG A 1 246 ? 127.808 120.466 97.147  1.00 31.40  ? 246 ARG A NE  1 
ATOM   1026 C  CZ  . ARG A 1 246 ? 127.805 121.332 96.142  1.00 31.40  ? 246 ARG A CZ  1 
ATOM   1027 N  NH1 . ARG A 1 246 ? 128.948 121.745 95.624  1.00 31.40  ? 246 ARG A NH1 1 
ATOM   1028 N  NH2 . ARG A 1 246 ? 126.660 121.781 95.659  1.00 31.40  ? 246 ARG A NH2 1 
ATOM   1029 N  N   . GLY A 1 247 ? 126.665 115.719 100.785 1.00 27.08  ? 247 GLY A N   1 
ATOM   1030 C  CA  . GLY A 1 247 ? 125.604 115.264 101.656 1.00 27.08  ? 247 GLY A CA  1 
ATOM   1031 C  C   . GLY A 1 247 ? 126.085 114.497 102.861 1.00 27.08  ? 247 GLY A C   1 
ATOM   1032 O  O   . GLY A 1 247 ? 125.321 114.322 103.808 1.00 27.08  ? 247 GLY A O   1 
ATOM   1033 N  N   . VAL A 1 248 ? 127.324 114.012 102.844 1.00 24.62  ? 248 VAL A N   1 
ATOM   1034 C  CA  . VAL A 1 248 ? 127.871 113.329 104.011 1.00 24.62  ? 248 VAL A CA  1 
ATOM   1035 C  C   . VAL A 1 248 ? 128.845 114.221 104.776 1.00 24.62  ? 248 VAL A C   1 
ATOM   1036 O  O   . VAL A 1 248 ? 128.949 114.136 106.008 1.00 24.62  ? 248 VAL A O   1 
ATOM   1037 C  CB  . VAL A 1 248 ? 128.525 112.007 103.603 1.00 24.62  ? 248 VAL A CB  1 
ATOM   1038 C  CG1 . VAL A 1 248 ? 129.392 111.501 104.704 1.00 24.62  ? 248 VAL A CG1 1 
ATOM   1039 C  CG2 . VAL A 1 248 ? 127.466 111.017 103.312 1.00 24.62  ? 248 VAL A CG2 1 
ATOM   1040 N  N   . PHE A 1 249 ? 129.550 115.105 104.074 1.00 27.28  ? 249 PHE A N   1 
ATOM   1041 C  CA  . PHE A 1 249 ? 130.447 116.004 104.781 1.00 27.28  ? 249 PHE A CA  1 
ATOM   1042 C  C   . PHE A 1 249 ? 129.680 116.937 105.693 1.00 27.28  ? 249 PHE A C   1 
ATOM   1043 O  O   . PHE A 1 249 ? 130.112 117.205 106.819 1.00 27.28  ? 249 PHE A O   1 
ATOM   1044 C  CB  . PHE A 1 249 ? 131.274 116.829 103.822 1.00 27.28  ? 249 PHE A CB  1 
ATOM   1045 C  CG  . PHE A 1 249 ? 131.939 117.971 104.486 1.00 27.28  ? 249 PHE A CG  1 
ATOM   1046 C  CD1 . PHE A 1 249 ? 132.872 117.754 105.463 1.00 27.28  ? 249 PHE A CD1 1 
ATOM   1047 C  CD2 . PHE A 1 249 ? 131.618 119.257 104.165 1.00 27.28  ? 249 PHE A CD2 1 
ATOM   1048 C  CE1 . PHE A 1 249 ? 133.490 118.786 106.092 1.00 27.28  ? 249 PHE A CE1 1 
ATOM   1049 C  CE2 . PHE A 1 249 ? 132.238 120.301 104.796 1.00 27.28  ? 249 PHE A CE2 1 
ATOM   1050 C  CZ  . PHE A 1 249 ? 133.175 120.061 105.763 1.00 27.28  ? 249 PHE A CZ  1 
ATOM   1051 N  N   . LEU A 1 250 ? 128.551 117.463 105.223 1.00 22.38  ? 250 LEU A N   1 
ATOM   1052 C  CA  . LEU A 1 250 ? 127.726 118.286 106.101 1.00 22.38  ? 250 LEU A CA  1 
ATOM   1053 C  C   . LEU A 1 250 ? 127.270 117.499 107.309 1.00 22.38  ? 250 LEU A C   1 
ATOM   1054 O  O   . LEU A 1 250 ? 127.242 118.014 108.432 1.00 22.38  ? 250 LEU A O   1 
ATOM   1055 C  CB  . LEU A 1 250 ? 126.528 118.820 105.343 1.00 22.38  ? 250 LEU A CB  1 
ATOM   1056 C  CG  . LEU A 1 250 ? 127.017 120.041 104.604 1.00 22.38  ? 250 LEU A CG  1 
ATOM   1057 C  CD1 . LEU A 1 250 ? 125.895 120.667 103.825 1.00 22.38  ? 250 LEU A CD1 1 
ATOM   1058 C  CD2 . LEU A 1 250 ? 127.589 120.979 105.631 1.00 22.38  ? 250 LEU A CD2 1 
ATOM   1059 N  N   . HIS A 1 251 ? 126.940 116.239 107.099 1.00 30.66  ? 251 HIS A N   1 
ATOM   1060 C  CA  . HIS A 1 251 ? 126.420 115.431 108.176 1.00 30.66  ? 251 HIS A CA  1 
ATOM   1061 C  C   . HIS A 1 251 ? 127.467 115.116 109.225 1.00 30.66  ? 251 HIS A C   1 
ATOM   1062 O  O   . HIS A 1 251 ? 127.103 114.867 110.375 1.00 30.66  ? 251 HIS A O   1 
ATOM   1063 C  CB  . HIS A 1 251 ? 125.856 114.155 107.607 1.00 30.66  ? 251 HIS A CB  1 
ATOM   1064 C  CG  . HIS A 1 251 ? 124.756 113.592 108.421 1.00 30.66  ? 251 HIS A CG  1 
ATOM   1065 N  ND1 . HIS A 1 251 ? 124.981 112.960 109.620 1.00 30.66  ? 251 HIS A ND1 1 
ATOM   1066 C  CD2 . HIS A 1 251 ? 123.420 113.589 108.229 1.00 30.66  ? 251 HIS A CD2 1 
ATOM   1067 C  CE1 . HIS A 1 251 ? 123.826 112.573 110.128 1.00 30.66  ? 251 HIS A CE1 1 
ATOM   1068 N  NE2 . HIS A 1 251 ? 122.863 112.941 109.302 1.00 30.66  ? 251 HIS A NE2 1 
ATOM   1069 N  N   . VAL A 1 252 ? 128.748 115.091 108.861 1.00 29.39  ? 252 VAL A N   1 
ATOM   1070 C  CA  . VAL A 1 252 ? 129.775 114.924 109.892 1.00 29.39  ? 252 VAL A CA  1 
ATOM   1071 C  C   . VAL A 1 252 ? 130.162 116.261 110.519 1.00 29.39  ? 252 VAL A C   1 
ATOM   1072 O  O   . VAL A 1 252 ? 130.521 116.305 111.699 1.00 29.39  ? 252 VAL A O   1 
ATOM   1073 C  CB  . VAL A 1 252 ? 131.024 114.197 109.369 1.00 29.39  ? 252 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A 1 252 ? 130.636 113.043 108.470 1.00 29.39  ? 252 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A 1 252 ? 131.978 115.154 108.697 1.00 29.39  ? 252 VAL A CG2 1 
ATOM   1076 N  N   . LEU A 1 253 ? 130.088 117.360 109.766 1.00 25.77  ? 253 LEU A N   1 
ATOM   1077 C  CA  . LEU A 1 253 ? 130.300 118.667 110.373 1.00 25.77  ? 253 LEU A CA  1 
ATOM   1078 C  C   . LEU A 1 253 ? 129.277 118.929 111.461 1.00 25.77  ? 253 LEU A C   1 
ATOM   1079 O  O   . LEU A 1 253 ? 129.588 119.562 112.476 1.00 25.77  ? 253 LEU A O   1 
ATOM   1080 C  CB  . LEU A 1 253 ? 130.222 119.755 109.313 1.00 25.77  ? 253 LEU A CB  1 
ATOM   1081 C  CG  . LEU A 1 253 ? 130.460 121.177 109.769 1.00 25.77  ? 253 LEU A CG  1 
ATOM   1082 C  CD1 . LEU A 1 253 ? 131.915 121.312 110.060 1.00 25.77  ? 253 LEU A CD1 1 
ATOM   1083 C  CD2 . LEU A 1 253 ? 130.059 122.125 108.681 1.00 25.77  ? 253 LEU A CD2 1 
ATOM   1084 N  N   . GLY A 1 254 ? 128.056 118.439 111.272 1.00 26.33  ? 254 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 254 ? 127.055 118.582 112.312 1.00 26.33  ? 254 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 254 ? 127.525 118.034 113.642 1.00 26.33  ? 254 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 254 ? 127.640 118.767 114.626 1.00 26.33  ? 254 GLY A O   1 
ATOM   1088 N  N   . ASP A 1 255 ? 127.846 116.744 113.683 1.00 35.74  ? 255 ASP A N   1 
ATOM   1089 C  CA  . ASP A 1 255 ? 128.240 116.151 114.952 1.00 35.74  ? 255 ASP A CA  1 
ATOM   1090 C  C   . ASP A 1 255 ? 129.592 116.662 115.435 1.00 35.74  ? 255 ASP A C   1 
ATOM   1091 O  O   . ASP A 1 255 ? 129.858 116.634 116.640 1.00 35.74  ? 255 ASP A O   1 
ATOM   1092 C  CB  . ASP A 1 255 ? 128.240 114.632 114.849 1.00 35.74  ? 255 ASP A CB  1 
ATOM   1093 C  CG  . ASP A 1 255 ? 126.900 114.031 115.196 1.00 35.74  ? 255 ASP A CG  1 
ATOM   1094 O  OD1 . ASP A 1 255 ? 126.172 113.612 114.275 1.00 35.74  ? 255 ASP A OD1 1 
ATOM   1095 O  OD2 . ASP A 1 255 ? 126.574 113.981 116.398 1.00 35.74  ? 255 ASP A OD2 1 
ATOM   1096 N  N   . ALA A 1 256 ? 130.450 117.160 114.541 1.00 30.65  ? 256 ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 256 ? 131.695 117.761 115.012 1.00 30.65  ? 256 ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 256 ? 131.423 119.038 115.801 1.00 30.65  ? 256 ALA A C   1 
ATOM   1099 O  O   . ALA A 1 256 ? 132.004 119.262 116.872 1.00 30.65  ? 256 ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 256 ? 132.627 118.040 113.838 1.00 30.65  ? 256 ALA A CB  1 
ATOM   1101 N  N   . LEU A 1 257 ? 130.541 119.897 115.285 1.00 26.25  ? 257 LEU A N   1 
ATOM   1102 C  CA  . LEU A 1 257 ? 130.177 121.082 116.052 1.00 26.25  ? 257 LEU A CA  1 
ATOM   1103 C  C   . LEU A 1 257 ? 129.444 120.705 117.327 1.00 26.25  ? 257 LEU A C   1 
ATOM   1104 O  O   . LEU A 1 257 ? 129.611 121.366 118.357 1.00 26.25  ? 257 LEU A O   1 
ATOM   1105 C  CB  . LEU A 1 257 ? 129.332 122.025 115.211 1.00 26.25  ? 257 LEU A CB  1 
ATOM   1106 C  CG  . LEU A 1 257 ? 130.139 122.733 114.133 1.00 26.25  ? 257 LEU A CG  1 
ATOM   1107 C  CD1 . LEU A 1 257 ? 129.288 123.740 113.411 1.00 26.25  ? 257 LEU A CD1 1 
ATOM   1108 C  CD2 . LEU A 1 257 ? 131.364 123.384 114.723 1.00 26.25  ? 257 LEU A CD2 1 
ATOM   1109 N  N   . GLY A 1 258 ? 128.645 119.642 117.288 1.00 26.73  ? 258 GLY A N   1 
ATOM   1110 C  CA  . GLY A 1 258 ? 128.054 119.143 118.520 1.00 26.73  ? 258 GLY A CA  1 
ATOM   1111 C  C   . GLY A 1 258 ? 129.104 118.761 119.545 1.00 26.73  ? 258 GLY A C   1 
ATOM   1112 O  O   . GLY A 1 258 ? 128.960 119.037 120.738 1.00 26.73  ? 258 GLY A O   1 
ATOM   1113 N  N   . SER A 1 259 ? 130.190 118.145 119.094 1.00 29.77  ? 259 SER A N   1 
ATOM   1114 C  CA  . SER A 1 259 ? 131.237 117.775 120.033 1.00 29.77  ? 259 SER A CA  1 
ATOM   1115 C  C   . SER A 1 259 ? 131.963 118.994 120.586 1.00 29.77  ? 259 SER A C   1 
ATOM   1116 O  O   . SER A 1 259 ? 132.318 119.011 121.771 1.00 29.77  ? 259 SER A O   1 
ATOM   1117 C  CB  . SER A 1 259 ? 132.217 116.822 119.368 1.00 29.77  ? 259 SER A CB  1 
ATOM   1118 O  OG  . SER A 1 259 ? 131.706 115.500 119.374 1.00 29.77  ? 259 SER A OG  1 
ATOM   1119 N  N   . VAL A 1 260 ? 132.209 120.012 119.759 1.00 24.82  ? 260 VAL A N   1 
ATOM   1120 C  CA  . VAL A 1 260 ? 132.803 121.236 120.298 1.00 24.82  ? 260 VAL A CA  1 
ATOM   1121 C  C   . VAL A 1 260 ? 131.897 121.834 121.360 1.00 24.82  ? 260 VAL A C   1 
ATOM   1122 O  O   . VAL A 1 260 ? 132.366 122.352 122.380 1.00 24.82  ? 260 VAL A O   1 
ATOM   1123 C  CB  . VAL A 1 260 ? 133.100 122.254 119.185 1.00 24.82  ? 260 VAL A CB  1 
ATOM   1124 C  CG1 . VAL A 1 260 ? 133.420 123.602 119.792 1.00 24.82  ? 260 VAL A CG1 1 
ATOM   1125 C  CG2 . VAL A 1 260 ? 134.249 121.782 118.332 1.00 24.82  ? 260 VAL A CG2 1 
ATOM   1126 N  N   . ILE A 1 261 ? 130.586 121.773 121.137 1.00 24.00  ? 261 ILE A N   1 
ATOM   1127 C  CA  . ILE A 1 261 ? 129.639 122.192 122.167 1.00 24.00  ? 261 ILE A CA  1 
ATOM   1128 C  C   . ILE A 1 261 ? 129.876 121.415 123.448 1.00 24.00  ? 261 ILE A C   1 
ATOM   1129 O  O   . ILE A 1 261 ? 129.912 121.992 124.537 1.00 24.00  ? 261 ILE A O   1 
ATOM   1130 C  CB  . ILE A 1 261 ? 128.188 122.015 121.690 1.00 24.00  ? 261 ILE A CB  1 
ATOM   1131 C  CG1 . ILE A 1 261 ? 127.763 123.150 120.773 1.00 24.00  ? 261 ILE A CG1 1 
ATOM   1132 C  CG2 . ILE A 1 261 ? 127.244 121.928 122.871 1.00 24.00  ? 261 ILE A CG2 1 
ATOM   1133 C  CD1 . ILE A 1 261 ? 126.384 122.954 120.242 1.00 24.00  ? 261 ILE A CD1 1 
ATOM   1134 N  N   . VAL A 1 262 ? 130.010 120.091 123.343 1.00 25.84  ? 262 VAL A N   1 
ATOM   1135 C  CA  . VAL A 1 262 ? 130.115 119.278 124.557 1.00 25.84  ? 262 VAL A CA  1 
ATOM   1136 C  C   . VAL A 1 262 ? 131.388 119.614 125.321 1.00 25.84  ? 262 VAL A C   1 
ATOM   1137 O  O   . VAL A 1 262 ? 131.395 119.666 126.555 1.00 25.84  ? 262 VAL A O   1 
ATOM   1138 C  CB  . VAL A 1 262 ? 130.041 117.777 124.242 1.00 25.84  ? 262 VAL A CB  1 
ATOM   1139 C  CG1 . VAL A 1 262 ? 129.971 117.020 125.531 1.00 25.84  ? 262 VAL A CG1 1 
ATOM   1140 C  CG2 . VAL A 1 262 ? 128.820 117.456 123.428 1.00 25.84  ? 262 VAL A CG2 1 
ATOM   1141 N  N   . VAL A 1 263 ? 132.480 119.866 124.606 1.00 26.31  ? 263 VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 263 ? 133.716 120.187 125.311 1.00 26.31  ? 263 VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 263 ? 133.649 121.566 125.951 1.00 26.31  ? 263 VAL A C   1 
ATOM   1144 O  O   . VAL A 1 263 ? 133.966 121.717 127.133 1.00 26.31  ? 263 VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 263 ? 134.926 120.067 124.388 1.00 26.31  ? 263 VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 263 ? 136.059 120.908 124.921 1.00 26.31  ? 263 VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 263 ? 135.331 118.636 124.342 1.00 26.31  ? 263 VAL A CG2 1 
ATOM   1148 N  N   . VAL A 1 264 ? 133.250 122.601 125.202 1.00 25.33  ? 264 VAL A N   1 
ATOM   1149 C  CA  . VAL A 1 264 ? 133.238 123.937 125.808 1.00 25.33  ? 264 VAL A CA  1 
ATOM   1150 C  C   . VAL A 1 264 ? 132.194 124.028 126.906 1.00 25.33  ? 264 VAL A C   1 
ATOM   1151 O  O   . VAL A 1 264 ? 132.376 124.771 127.866 1.00 25.33  ? 264 VAL A O   1 
ATOM   1152 C  CB  . VAL A 1 264 ? 133.047 125.033 124.747 1.00 25.33  ? 264 VAL A CB  1 
ATOM   1153 C  CG1 . VAL A 1 264 ? 132.469 126.266 125.354 1.00 25.33  ? 264 VAL A CG1 1 
ATOM   1154 C  CG2 . VAL A 1 264 ? 134.382 125.375 124.113 1.00 25.33  ? 264 VAL A CG2 1 
ATOM   1155 N  N   . ASN A 1 265 ? 131.118 123.248 126.827 1.00 29.56  ? 265 ASN A N   1 
ATOM   1156 C  CA  . ASN A 1 265 ? 130.203 123.159 127.957 1.00 29.56  ? 265 ASN A CA  1 
ATOM   1157 C  C   . ASN A 1 265 ? 130.857 122.485 129.149 1.00 29.56  ? 265 ASN A C   1 
ATOM   1158 O  O   . ASN A 1 265 ? 131.123 123.135 130.163 1.00 29.56  ? 265 ASN A O   1 
ATOM   1159 C  CB  . ASN A 1 265 ? 128.952 122.387 127.584 1.00 29.56  ? 265 ASN A CB  1 
ATOM   1160 C  CG  . ASN A 1 265 ? 127.979 122.299 128.729 1.00 29.56  ? 265 ASN A CG  1 
ATOM   1161 O  OD1 . ASN A 1 265 ? 128.139 122.957 129.746 1.00 29.56  ? 265 ASN A OD1 1 
ATOM   1162 N  ND2 . ASN A 1 265 ? 126.985 121.449 128.586 1.00 29.56  ? 265 ASN A ND2 1 
ATOM   1163 N  N   . ALA A 1 266 ? 131.116 121.178 129.063 1.00 24.19  ? 266 ALA A N   1 
ATOM   1164 C  CA  . ALA A 1 266 ? 131.577 120.458 130.246 1.00 24.19  ? 266 ALA A CA  1 
ATOM   1165 C  C   . ALA A 1 266 ? 132.950 120.925 130.697 1.00 24.19  ? 266 ALA A C   1 
ATOM   1166 O  O   . ALA A 1 266 ? 133.457 120.456 131.716 1.00 24.19  ? 266 ALA A O   1 
ATOM   1167 C  CB  . ALA A 1 266 ? 131.585 118.964 129.979 1.00 24.19  ? 266 ALA A CB  1 
ATOM   1168 N  N   . LEU A 1 267 ? 133.571 121.822 129.946 1.00 30.00  ? 267 LEU A N   1 
ATOM   1169 C  CA  . LEU A 1 267 ? 134.779 122.493 130.390 1.00 30.00  ? 267 LEU A CA  1 
ATOM   1170 C  C   . LEU A 1 267 ? 134.455 123.529 131.458 1.00 30.00  ? 267 LEU A C   1 
ATOM   1171 O  O   . LEU A 1 267 ? 134.819 123.336 132.621 1.00 30.00  ? 267 LEU A O   1 
ATOM   1172 C  CB  . LEU A 1 267 ? 135.480 123.125 129.193 1.00 30.00  ? 267 LEU A CB  1 
ATOM   1173 C  CG  . LEU A 1 267 ? 136.747 123.921 129.425 1.00 30.00  ? 267 LEU A CG  1 
ATOM   1174 C  CD1 . LEU A 1 267 ? 137.768 123.534 128.397 1.00 30.00  ? 267 LEU A CD1 1 
ATOM   1175 C  CD2 . LEU A 1 267 ? 136.419 125.388 129.284 1.00 30.00  ? 267 LEU A CD2 1 
ATOM   1176 N  N   . VAL A 1 268 ? 133.740 124.599 131.109 1.00 27.75  ? 268 VAL A N   1 
ATOM   1177 C  CA  . VAL A 1 268 ? 133.284 125.577 132.119 1.00 27.75  ? 268 VAL A CA  1 
ATOM   1178 C  C   . VAL A 1 268 ? 131.925 125.080 132.583 1.00 27.75  ? 268 VAL A C   1 
ATOM   1179 O  O   . VAL A 1 268 ? 130.871 125.630 132.269 1.00 27.75  ? 268 VAL A O   1 
ATOM   1180 C  CB  . VAL A 1 268 ? 133.233 127.002 131.562 1.00 27.75  ? 268 VAL A CB  1 
ATOM   1181 N  N   . PHE A 1 269 ? 131.954 123.995 133.304 1.00 33.53  ? 269 PHE A N   1 
ATOM   1182 C  CA  . PHE A 1 269 ? 130.895 123.450 134.133 1.00 33.53  ? 269 PHE A CA  1 
ATOM   1183 C  C   . PHE A 1 269 ? 131.427 122.818 135.405 1.00 33.53  ? 269 PHE A C   1 
ATOM   1184 O  O   . PHE A 1 269 ? 130.701 122.728 136.391 1.00 33.53  ? 269 PHE A O   1 
ATOM   1185 C  CB  . PHE A 1 269 ? 130.103 122.449 133.358 1.00 33.53  ? 269 PHE A CB  1 
ATOM   1186 C  CG  . PHE A 1 269 ? 128.719 122.262 133.854 1.00 33.53  ? 269 PHE A CG  1 
ATOM   1187 C  CD1 . PHE A 1 269 ? 127.663 122.835 133.191 1.00 33.53  ? 269 PHE A CD1 1 
ATOM   1188 C  CD2 . PHE A 1 269 ? 128.470 121.494 134.962 1.00 33.53  ? 269 PHE A CD2 1 
ATOM   1189 C  CE1 . PHE A 1 269 ? 126.391 122.647 133.625 1.00 33.53  ? 269 PHE A CE1 1 
ATOM   1190 C  CE2 . PHE A 1 269 ? 127.199 121.311 135.406 1.00 33.53  ? 269 PHE A CE2 1 
ATOM   1191 C  CZ  . PHE A 1 269 ? 126.156 121.884 134.738 1.00 33.53  ? 269 PHE A CZ  1 
ATOM   1192 N  N   . TYR A 1 270 ? 132.647 122.297 135.379 1.00 37.62  ? 270 TYR A N   1 
ATOM   1193 C  CA  . TYR A 1 270 ? 133.359 122.002 136.610 1.00 37.62  ? 270 TYR A CA  1 
ATOM   1194 C  C   . TYR A 1 270 ? 134.089 123.221 137.136 1.00 37.62  ? 270 TYR A C   1 
ATOM   1195 O  O   . TYR A 1 270 ? 134.360 123.306 138.338 1.00 37.62  ? 270 TYR A O   1 
ATOM   1196 C  CB  . TYR A 1 270 ? 134.359 120.868 136.391 1.00 37.62  ? 270 TYR A CB  1 
ATOM   1197 N  N   . PHE A 1 271 ? 134.392 124.171 136.256 1.00 36.09  ? 271 PHE A N   1 
ATOM   1198 C  CA  . PHE A 1 271 ? 135.118 125.366 136.654 1.00 36.09  ? 271 PHE A CA  1 
ATOM   1199 C  C   . PHE A 1 271 ? 134.216 126.334 137.406 1.00 36.09  ? 271 PHE A C   1 
ATOM   1200 O  O   . PHE A 1 271 ? 134.690 127.143 138.206 1.00 36.09  ? 271 PHE A O   1 
ATOM   1201 C  CB  . PHE A 1 271 ? 135.707 126.032 135.413 1.00 36.09  ? 271 PHE A CB  1 
ATOM   1202 C  CG  . PHE A 1 271 ? 136.953 125.379 134.910 1.00 36.09  ? 271 PHE A CG  1 
ATOM   1203 C  CD1 . PHE A 1 271 ? 137.922 126.123 134.276 1.00 36.09  ? 271 PHE A CD1 1 
ATOM   1204 C  CD2 . PHE A 1 271 ? 137.159 124.024 135.081 1.00 36.09  ? 271 PHE A CD2 1 
ATOM   1205 C  CE1 . PHE A 1 271 ? 139.066 125.528 133.813 1.00 36.09  ? 271 PHE A CE1 1 
ATOM   1206 C  CE2 . PHE A 1 271 ? 138.299 123.429 134.626 1.00 36.09  ? 271 PHE A CE2 1 
ATOM   1207 C  CZ  . PHE A 1 271 ? 139.257 124.181 133.991 1.00 36.09  ? 271 PHE A CZ  1 
ATOM   1208 N  N   . SER A 1 272 ? 132.910 126.276 137.154 1.00 36.82  ? 272 SER A N   1 
ATOM   1209 C  CA  . SER A 1 272 ? 132.021 127.295 137.691 1.00 36.82  ? 272 SER A CA  1 
ATOM   1210 C  C   . SER A 1 272 ? 130.995 126.751 138.674 1.00 36.82  ? 272 SER A C   1 
ATOM   1211 O  O   . SER A 1 272 ? 130.908 127.242 139.802 1.00 36.82  ? 272 SER A O   1 
ATOM   1212 C  CB  . SER A 1 272 ? 131.306 128.013 136.556 1.00 36.82  ? 272 SER A CB  1 
ATOM   1213 N  N   . TRP A 1 273 ? 130.219 125.746 138.276 1.00 39.06  ? 273 TRP A N   1 
ATOM   1214 C  CA  . TRP A 1 273 ? 129.074 125.329 139.077 1.00 39.06  ? 273 TRP A CA  1 
ATOM   1215 C  C   . TRP A 1 273 ? 129.512 124.808 140.437 1.00 39.06  ? 273 TRP A C   1 
ATOM   1216 O  O   . TRP A 1 273 ? 130.660 124.408 140.631 1.00 39.06  ? 273 TRP A O   1 
ATOM   1217 C  CB  . TRP A 1 273 ? 128.268 124.257 138.341 1.00 39.06  ? 273 TRP A CB  1 
ATOM   1218 N  N   . LYS A 1 274 ? 128.590 124.847 141.390 1.00 50.03  ? 274 LYS A N   1 
ATOM   1219 C  CA  . LYS A 1 274 ? 128.841 124.409 142.755 1.00 50.03  ? 274 LYS A CA  1 
ATOM   1220 C  C   . LYS A 1 274 ? 127.920 123.280 143.183 1.00 50.03  ? 274 LYS A C   1 
ATOM   1221 O  O   . LYS A 1 274 ? 128.396 122.246 143.660 1.00 50.03  ? 274 LYS A O   1 
ATOM   1222 C  CB  . LYS A 1 274 ? 128.698 125.592 143.719 1.00 50.03  ? 274 LYS A CB  1 
ATOM   1223 N  N   . GLY A 1 275 ? 126.613 123.450 143.042 1.00 63.89  ? 275 GLY A N   1 
ATOM   1224 C  CA  . GLY A 1 275 ? 125.684 122.381 143.340 1.00 63.89  ? 275 GLY A CA  1 
ATOM   1225 C  C   . GLY A 1 275 ? 125.618 122.046 144.813 1.00 63.89  ? 275 GLY A C   1 
ATOM   1226 O  O   . GLY A 1 275 ? 126.190 122.763 145.637 1.00 63.89  ? 275 GLY A O   1 
ATOM   1227 N  N   . CYS A 1 276 ? 124.956 120.939 145.150 1.00 71.42  ? 276 CYS A N   1 
ATOM   1228 C  CA  . CYS A 1 276 ? 124.690 120.589 146.543 1.00 71.42  ? 276 CYS A CA  1 
ATOM   1229 C  C   . CYS A 1 276 ? 125.913 119.938 147.177 1.00 71.42  ? 276 CYS A C   1 
ATOM   1230 O  O   . CYS A 1 276 ? 126.476 118.985 146.627 1.00 71.42  ? 276 CYS A O   1 
ATOM   1231 C  CB  . CYS A 1 276 ? 123.487 119.659 146.622 1.00 71.42  ? 276 CYS A CB  1 
ATOM   1232 S  SG  . CYS A 1 276 ? 121.971 120.386 145.985 1.00 71.42  ? 276 CYS A SG  1 
ATOM   1233 N  N   . SER A 1 277 ? 126.309 120.436 148.347 1.00 76.12  ? 277 SER A N   1 
ATOM   1234 C  CA  . SER A 1 277 ? 127.602 120.090 148.931 1.00 76.12  ? 277 SER A CA  1 
ATOM   1235 C  C   . SER A 1 277 ? 127.494 119.081 150.074 1.00 76.12  ? 277 SER A C   1 
ATOM   1236 O  O   . SER A 1 277 ? 128.130 118.022 150.037 1.00 76.12  ? 277 SER A O   1 
ATOM   1237 C  CB  . SER A 1 277 ? 128.303 121.367 149.410 1.00 76.12  ? 277 SER A CB  1 
ATOM   1238 N  N   . GLU A 1 278 ? 126.702 119.399 151.101 1.00 78.44  ? 278 GLU A N   1 
ATOM   1239 C  CA  . GLU A 1 278 ? 126.688 118.624 152.346 1.00 78.44  ? 278 GLU A CA  1 
ATOM   1240 C  C   . GLU A 1 278 ? 125.818 117.382 152.166 1.00 78.44  ? 278 GLU A C   1 
ATOM   1241 O  O   . GLU A 1 278 ? 124.647 117.333 152.550 1.00 78.44  ? 278 GLU A O   1 
ATOM   1242 C  CB  . GLU A 1 278 ? 126.202 119.484 153.506 1.00 78.44  ? 278 GLU A CB  1 
ATOM   1243 N  N   . GLY A 1 279 ? 126.422 116.348 151.584 1.00 78.00  ? 279 GLY A N   1 
ATOM   1244 C  CA  . GLY A 1 279 ? 125.729 115.095 151.359 1.00 78.00  ? 279 GLY A CA  1 
ATOM   1245 C  C   . GLY A 1 279 ? 124.603 115.217 150.356 1.00 78.00  ? 279 GLY A C   1 
ATOM   1246 O  O   . GLY A 1 279 ? 124.842 115.528 149.186 1.00 78.00  ? 279 GLY A O   1 
ATOM   1247 N  N   . ASP A 1 280 ? 123.367 114.977 150.799 1.00 75.43  ? 280 ASP A N   1 
ATOM   1248 C  CA  . ASP A 1 280 ? 122.199 115.024 149.925 1.00 75.43  ? 280 ASP A CA  1 
ATOM   1249 C  C   . ASP A 1 280 ? 121.115 115.969 150.429 1.00 75.43  ? 280 ASP A C   1 
ATOM   1250 O  O   . ASP A 1 280 ? 119.956 115.821 150.028 1.00 75.43  ? 280 ASP A O   1 
ATOM   1251 C  CB  . ASP A 1 280 ? 121.593 113.624 149.749 1.00 75.43  ? 280 ASP A CB  1 
ATOM   1252 C  CG  . ASP A 1 280 ? 122.477 112.687 148.945 1.00 75.43  ? 280 ASP A CG  1 
ATOM   1253 O  OD1 . ASP A 1 280 ? 123.712 112.842 148.976 1.00 75.43  ? 280 ASP A OD1 1 
ATOM   1254 O  OD2 . ASP A 1 280 ? 121.931 111.786 148.277 1.00 75.43  ? 280 ASP A OD2 1 
ATOM   1255 N  N   . PHE A 1 281 ? 121.445 116.926 151.295 1.00 78.25  ? 281 PHE A N   1 
ATOM   1256 C  CA  . PHE A 1 281 ? 120.445 117.783 151.938 1.00 78.25  ? 281 PHE A CA  1 
ATOM   1257 C  C   . PHE A 1 281 ? 120.887 119.241 151.861 1.00 78.25  ? 281 PHE A C   1 
ATOM   1258 O  O   . PHE A 1 281 ? 121.528 119.758 152.779 1.00 78.25  ? 281 PHE A O   1 
ATOM   1259 C  CB  . PHE A 1 281 ? 120.217 117.354 153.387 1.00 78.25  ? 281 PHE A CB  1 
ATOM   1260 N  N   . CYS A 1 282 ? 120.516 119.910 150.776 1.00 82.85  ? 282 CYS A N   1 
ATOM   1261 C  CA  . CYS A 1 282 ? 120.840 121.317 150.588 1.00 82.85  ? 282 CYS A CA  1 
ATOM   1262 C  C   . CYS A 1 282 ? 119.739 121.950 149.747 1.00 82.85  ? 282 CYS A C   1 
ATOM   1263 O  O   . CYS A 1 282 ? 118.896 121.257 149.171 1.00 82.85  ? 282 CYS A O   1 
ATOM   1264 C  CB  . CYS A 1 282 ? 122.222 121.485 149.942 1.00 82.85  ? 282 CYS A CB  1 
ATOM   1265 N  N   . VAL A 1 283 ? 119.756 123.263 149.665 1.00 90.28  ? 283 VAL A N   1 
ATOM   1266 C  CA  . VAL A 1 283 ? 118.744 123.998 148.921 1.00 90.28  ? 283 VAL A CA  1 
ATOM   1267 C  C   . VAL A 1 283 ? 119.348 124.470 147.606 1.00 90.28  ? 283 VAL A C   1 
ATOM   1268 O  O   . VAL A 1 283 ? 120.418 125.089 147.567 1.00 90.28  ? 283 VAL A O   1 
ATOM   1269 C  CB  . VAL A 1 283 ? 118.197 125.173 149.755 1.00 90.28  ? 283 VAL A CB  1 
ATOM   1270 N  N   . ASN A 1 284 ? 118.648 124.167 146.508 1.00 91.17  ? 284 ASN A N   1 
ATOM   1271 C  CA  . ASN A 1 284 ? 119.058 124.527 145.153 1.00 91.17  ? 284 ASN A CA  1 
ATOM   1272 C  C   . ASN A 1 284 ? 118.063 125.562 144.653 1.00 91.17  ? 284 ASN A C   1 
ATOM   1273 O  O   . ASN A 1 284 ? 116.993 125.212 144.135 1.00 91.17  ? 284 ASN A O   1 
ATOM   1274 C  CB  . ASN A 1 284 ? 119.101 123.314 144.226 1.00 91.17  ? 284 ASN A CB  1 
ATOM   1275 N  N   . PRO A 1 285 ? 118.368 126.848 144.819 1.00 92.07  ? 285 PRO A N   1 
ATOM   1276 C  CA  . PRO A 1 285 ? 117.398 127.874 144.413 1.00 92.07  ? 285 PRO A CA  1 
ATOM   1277 C  C   . PRO A 1 285 ? 117.319 128.058 142.911 1.00 92.07  ? 285 PRO A C   1 
ATOM   1278 O  O   . PRO A 1 285 ? 116.273 128.471 142.398 1.00 92.07  ? 285 PRO A O   1 
ATOM   1279 C  CB  . PRO A 1 285 ? 117.915 129.138 145.118 1.00 92.07  ? 285 PRO A CB  1 
ATOM   1280 C  CG  . PRO A 1 285 ? 118.908 128.646 146.146 1.00 92.07  ? 285 PRO A CG  1 
ATOM   1281 C  CD  . PRO A 1 285 ? 119.509 127.426 145.540 1.00 92.07  ? 285 PRO A CD  1 
ATOM   1282 N  N   . CYS A 1 286 ? 118.394 127.746 142.186 1.00 88.40  ? 286 CYS A N   1 
ATOM   1283 C  CA  . CYS A 1 286 ? 118.472 128.113 140.781 1.00 88.40  ? 286 CYS A CA  1 
ATOM   1284 C  C   . CYS A 1 286 ? 117.454 127.389 139.913 1.00 88.40  ? 286 CYS A C   1 
ATOM   1285 O  O   . CYS A 1 286 ? 117.165 127.859 138.811 1.00 88.40  ? 286 CYS A O   1 
ATOM   1286 C  CB  . CYS A 1 286 ? 119.873 127.854 140.247 1.00 88.40  ? 286 CYS A CB  1 
ATOM   1287 S  SG  . CYS A 1 286 ? 120.174 128.555 138.609 1.00 88.40  ? 286 CYS A SG  1 
ATOM   1288 N  N   . PHE A 1 287 ? 116.908 126.263 140.361 1.00 84.33  ? 287 PHE A N   1 
ATOM   1289 C  CA  . PHE A 1 287 ? 115.875 125.639 139.550 1.00 84.33  ? 287 PHE A CA  1 
ATOM   1290 C  C   . PHE A 1 287 ? 114.978 124.801 140.449 1.00 84.33  ? 287 PHE A C   1 
ATOM   1291 O  O   . PHE A 1 287 ? 115.329 124.582 141.618 1.00 84.33  ? 287 PHE A O   1 
ATOM   1292 C  CB  . PHE A 1 287 ? 116.444 124.785 138.410 1.00 84.33  ? 287 PHE A CB  1 
ATOM   1293 C  CG  . PHE A 1 287 ? 117.313 123.641 138.855 1.00 84.33  ? 287 PHE A CG  1 
ATOM   1294 C  CD1 . PHE A 1 287 ? 118.546 123.869 139.435 1.00 84.33  ? 287 PHE A CD1 1 
ATOM   1295 C  CD2 . PHE A 1 287 ? 116.916 122.336 138.647 1.00 84.33  ? 287 PHE A CD2 1 
ATOM   1296 C  CE1 . PHE A 1 287 ? 119.342 122.825 139.832 1.00 84.33  ? 287 PHE A CE1 1 
ATOM   1297 C  CE2 . PHE A 1 287 ? 117.713 121.291 139.037 1.00 84.33  ? 287 PHE A CE2 1 
ATOM   1298 C  CZ  . PHE A 1 287 ? 118.927 121.537 139.633 1.00 84.33  ? 287 PHE A CZ  1 
ATOM   1299 N  N   . PRO A 1 288 ? 113.827 124.349 139.961 1.00 90.20  ? 288 PRO A N   1 
ATOM   1300 C  CA  . PRO A 1 288 ? 112.873 123.666 140.862 1.00 90.20  ? 288 PRO A CA  1 
ATOM   1301 C  C   . PRO A 1 288 ? 113.361 122.292 141.310 1.00 90.20  ? 288 PRO A C   1 
ATOM   1302 O  O   . PRO A 1 288 ? 112.939 121.246 140.830 1.00 90.20  ? 288 PRO A O   1 
ATOM   1303 C  CB  . PRO A 1 288 ? 111.611 123.572 140.003 1.00 90.20  ? 288 PRO A CB  1 
ATOM   1304 N  N   . ASP A 1 289 ? 114.274 122.302 142.272 1.00 92.75  ? 289 ASP A N   1 
ATOM   1305 C  CA  . ASP A 1 289 ? 114.924 121.078 142.724 1.00 92.75  ? 289 ASP A CA  1 
ATOM   1306 C  C   . ASP A 1 289 ? 113.893 120.116 143.293 1.00 92.75  ? 289 ASP A C   1 
ATOM   1307 O  O   . ASP A 1 289 ? 113.246 120.441 144.295 1.00 92.75  ? 289 ASP A O   1 
ATOM   1308 C  CB  . ASP A 1 289 ? 115.982 121.404 143.771 1.00 92.75  ? 289 ASP A CB  1 
ATOM   1309 N  N   . PRO A 1 290 ? 113.682 118.953 142.643 1.00 96.45  ? 290 PRO A N   1 
ATOM   1310 C  CA  . PRO A 1 290 ? 112.656 117.927 142.947 1.00 96.45  ? 290 PRO A CA  1 
ATOM   1311 C  C   . PRO A 1 290 ? 112.661 117.189 144.298 1.00 96.45  ? 290 PRO A C   1 
ATOM   1312 O  O   . PRO A 1 290 ? 111.594 117.049 144.870 1.00 96.45  ? 290 PRO A O   1 
ATOM   1313 C  CB  . PRO A 1 290 ? 112.880 116.900 141.828 1.00 96.45  ? 290 PRO A CB  1 
ATOM   1314 N  N   . CYS A 1 291 ? 113.811 116.738 144.779 1.00 95.47  ? 291 CYS A N   1 
ATOM   1315 C  CA  . CYS A 1 291 ? 113.929 116.036 146.050 1.00 95.47  ? 291 CYS A CA  1 
ATOM   1316 C  C   . CYS A 1 291 ? 114.389 116.969 147.158 1.00 95.47  ? 291 CYS A C   1 
ATOM   1317 O  O   . CYS A 1 291 ? 113.880 116.907 148.284 1.00 95.47  ? 291 CYS A O   1 
ATOM   1318 C  CB  . CYS A 1 291 ? 114.891 114.860 145.927 1.00 95.47  ? 291 CYS A CB  1 
ATOM   1319 S  SG  . CYS A 1 291 ? 114.617 113.718 147.256 1.00 95.47  ? 291 CYS A SG  1 
ATOM   1320 N  N   . LYS A 1 292 ? 115.374 117.819 146.864 1.00 93.87  ? 292 LYS A N   1 
ATOM   1321 C  CA  . LYS A 1 292 ? 115.876 118.742 147.872 1.00 93.87  ? 292 LYS A CA  1 
ATOM   1322 C  C   . LYS A 1 292 ? 114.749 119.593 148.440 1.00 93.87  ? 292 LYS A C   1 
ATOM   1323 O  O   . LYS A 1 292 ? 114.535 119.622 149.657 1.00 93.87  ? 292 LYS A O   1 
ATOM   1324 C  CB  . LYS A 1 292 ? 116.977 119.618 147.270 1.00 93.87  ? 292 LYS A CB  1 
ATOM   1325 N  N   . ALA A 1 293 ? 113.993 120.262 147.568 1.00 90.80  ? 293 ALA A N   1 
ATOM   1326 C  CA  . ALA A 1 293 ? 112.908 121.111 148.042 1.00 90.80  ? 293 ALA A CA  1 
ATOM   1327 C  C   . ALA A 1 293 ? 111.811 120.291 148.705 1.00 90.80  ? 293 ALA A C   1 
ATOM   1328 O  O   . ALA A 1 293 ? 111.271 120.699 149.739 1.00 90.80  ? 293 ALA A O   1 
ATOM   1329 C  CB  . ALA A 1 293 ? 112.337 121.937 146.891 1.00 90.80  ? 293 ALA A CB  1 
ATOM   1330 N  N   . PHE A 1 294 ? 111.472 119.126 148.137 1.00 87.54  ? 294 PHE A N   1 
ATOM   1331 C  CA  . PHE A 1 294 ? 110.401 118.319 148.718 1.00 87.54  ? 294 PHE A CA  1 
ATOM   1332 C  C   . PHE A 1 294 ? 110.720 117.919 150.157 1.00 87.54  ? 294 PHE A C   1 
ATOM   1333 O  O   . PHE A 1 294 ? 109.925 118.171 151.075 1.00 87.54  ? 294 PHE A O   1 
ATOM   1334 C  CB  . PHE A 1 294 ? 110.156 117.083 147.855 1.00 87.54  ? 294 PHE A CB  1 
ATOM   1335 N  N   . VAL A 1 295 ? 111.896 117.326 150.377 1.00 85.04  ? 295 VAL A N   1 
ATOM   1336 C  CA  . VAL A 1 295 ? 112.255 116.839 151.707 1.00 85.04  ? 295 VAL A CA  1 
ATOM   1337 C  C   . VAL A 1 295 ? 112.571 117.996 152.647 1.00 85.04  ? 295 VAL A C   1 
ATOM   1338 O  O   . VAL A 1 295 ? 112.380 117.890 153.864 1.00 85.04  ? 295 VAL A O   1 
ATOM   1339 C  CB  . VAL A 1 295 ? 113.434 115.854 151.616 1.00 85.04  ? 295 VAL A CB  1 
ATOM   1340 N  N   . GLU A 1 296 ? 113.064 119.118 152.110 1.00 81.13  ? 296 GLU A N   1 
ATOM   1341 C  CA  . GLU A 1 296 ? 113.422 120.240 152.968 1.00 81.13  ? 296 GLU A CA  1 
ATOM   1342 C  C   . GLU A 1 296 ? 112.204 121.037 153.410 1.00 81.13  ? 296 GLU A C   1 
ATOM   1343 O  O   . GLU A 1 296 ? 112.227 121.649 154.483 1.00 81.13  ? 296 GLU A O   1 
ATOM   1344 C  CB  . GLU A 1 296 ? 114.412 121.151 152.243 1.00 81.13  ? 296 GLU A CB  1 
ATOM   1345 N  N   . ILE A 1 297 ? 111.142 121.050 152.606 1.00 81.39  ? 297 ILE A N   1 
ATOM   1346 C  CA  . ILE A 1 297 ? 109.916 121.723 153.006 1.00 81.39  ? 297 ILE A CA  1 
ATOM   1347 C  C   . ILE A 1 297 ? 108.989 120.803 153.791 1.00 81.39  ? 297 ILE A C   1 
ATOM   1348 O  O   . ILE A 1 297 ? 108.174 121.296 154.584 1.00 81.39  ? 297 ILE A O   1 
ATOM   1349 C  CB  . ILE A 1 297 ? 109.179 122.297 151.783 1.00 81.39  ? 297 ILE A CB  1 
ATOM   1350 N  N   . ILE A 1 298 ? 109.089 119.487 153.601 1.00 76.72  ? 298 ILE A N   1 
ATOM   1351 C  CA  . ILE A 1 298 ? 108.313 118.546 154.398 1.00 76.72  ? 298 ILE A CA  1 
ATOM   1352 C  C   . ILE A 1 298 ? 108.961 118.244 155.745 1.00 76.72  ? 298 ILE A C   1 
ATOM   1353 O  O   . ILE A 1 298 ? 108.344 117.549 156.566 1.00 76.72  ? 298 ILE A O   1 
ATOM   1354 C  CB  . ILE A 1 298 ? 108.052 117.236 153.627 1.00 76.72  ? 298 ILE A CB  1 
ATOM   1355 N  N   . ASN A 1 299 ? 110.173 118.736 156.000 1.00 71.62  ? 299 ASN A N   1 
ATOM   1356 C  CA  . ASN A 1 299 ? 110.886 118.499 157.255 1.00 71.62  ? 299 ASN A CA  1 
ATOM   1357 C  C   . ASN A 1 299 ? 111.723 119.745 157.525 1.00 71.62  ? 299 ASN A C   1 
ATOM   1358 O  O   . ASN A 1 299 ? 112.678 120.023 156.797 1.00 71.62  ? 299 ASN A O   1 
ATOM   1359 C  CB  . ASN A 1 299 ? 111.749 117.246 157.165 1.00 71.62  ? 299 ASN A CB  1 
ATOM   1360 C  CG  . ASN A 1 299 ? 112.590 117.001 158.413 1.00 71.62  ? 299 ASN A CG  1 
ATOM   1361 O  OD1 . ASN A 1 299 ? 112.812 117.892 159.231 1.00 71.62  ? 299 ASN A OD1 1 
ATOM   1362 N  ND2 . ASN A 1 299 ? 113.069 115.772 158.554 1.00 71.62  ? 299 ASN A ND2 1 
ATOM   1363 N  N   . SER A 1 300 ? 111.368 120.485 158.572 1.00 70.22  ? 300 SER A N   1 
ATOM   1364 C  CA  . SER A 1 300 ? 112.093 121.686 158.973 1.00 70.22  ? 300 SER A CA  1 
ATOM   1365 C  C   . SER A 1 300 ? 112.921 121.352 160.207 1.00 70.22  ? 300 SER A C   1 
ATOM   1366 O  O   . SER A 1 300 ? 112.393 121.309 161.322 1.00 70.22  ? 300 SER A O   1 
ATOM   1367 C  CB  . SER A 1 300 ? 111.130 122.837 159.253 1.00 70.22  ? 300 SER A CB  1 
ATOM   1368 N  N   . THR A 1 301 ? 114.218 121.122 160.007 1.00 75.79  ? 301 THR A N   1 
ATOM   1369 C  CA  . THR A 1 301 ? 115.092 120.636 161.066 1.00 75.79  ? 301 THR A CA  1 
ATOM   1370 C  C   . THR A 1 301 ? 116.303 121.530 161.311 1.00 75.79  ? 301 THR A C   1 
ATOM   1371 O  O   . THR A 1 301 ? 117.136 121.191 162.158 1.00 75.79  ? 301 THR A O   1 
ATOM   1372 C  CB  . THR A 1 301 ? 115.556 119.211 160.752 1.00 75.79  ? 301 THR A CB  1 
ATOM   1373 N  N   . HIS A 1 302 ? 116.428 122.653 160.596 1.00 82.76  ? 302 HIS A N   1 
ATOM   1374 C  CA  . HIS A 1 302 ? 117.558 123.573 160.764 1.00 82.76  ? 302 HIS A CA  1 
ATOM   1375 C  C   . HIS A 1 302 ? 118.890 122.853 160.540 1.00 82.76  ? 302 HIS A C   1 
ATOM   1376 O  O   . HIS A 1 302 ? 119.737 122.768 161.431 1.00 82.76  ? 302 HIS A O   1 
ATOM   1377 C  CB  . HIS A 1 302 ? 117.525 124.240 162.144 1.00 82.76  ? 302 HIS A CB  1 
ATOM   1378 N  N   . ALA A 1 303 ? 119.074 122.340 159.326 1.00 90.68  ? 303 ALA A N   1 
ATOM   1379 C  CA  . ALA A 1 303 ? 120.148 121.403 159.031 1.00 90.68  ? 303 ALA A CA  1 
ATOM   1380 C  C   . ALA A 1 303 ? 121.475 122.138 158.839 1.00 90.68  ? 303 ALA A C   1 
ATOM   1381 O  O   . ALA A 1 303 ? 121.633 123.300 159.222 1.00 90.68  ? 303 ALA A O   1 
ATOM   1382 C  CB  . ALA A 1 303 ? 119.787 120.556 157.812 1.00 90.68  ? 303 ALA A CB  1 
ATOM   1383 N  N   . SER A 1 304 ? 122.447 121.450 158.242 1.00 96.38  ? 304 SER A N   1 
ATOM   1384 C  CA  . SER A 1 304 ? 123.814 121.936 158.131 1.00 96.38  ? 304 SER A CA  1 
ATOM   1385 C  C   . SER A 1 304 ? 123.944 122.970 157.008 1.00 96.38  ? 304 SER A C   1 
ATOM   1386 O  O   . SER A 1 304 ? 122.958 123.461 156.450 1.00 96.38  ? 304 SER A O   1 
ATOM   1387 C  CB  . SER A 1 304 ? 124.769 120.765 157.915 1.00 96.38  ? 304 SER A CB  1 
ATOM   1388 N  N   . VAL A 1 305 ? 125.193 123.303 156.674 1.00 98.63  ? 305 VAL A N   1 
ATOM   1389 C  CA  . VAL A 1 305 ? 125.476 124.418 155.779 1.00 98.63  ? 305 VAL A CA  1 
ATOM   1390 C  C   . VAL A 1 305 ? 125.062 124.084 154.350 1.00 98.63  ? 305 VAL A C   1 
ATOM   1391 O  O   . VAL A 1 305 ? 124.943 122.911 153.968 1.00 98.63  ? 305 VAL A O   1 
ATOM   1392 C  CB  . VAL A 1 305 ? 126.965 124.793 155.854 1.00 98.63  ? 305 VAL A CB  1 
ATOM   1393 N  N   . TYR A 1 306 ? 124.818 125.129 153.560 1.00 94.23  ? 306 TYR A N   1 
ATOM   1394 C  CA  . TYR A 1 306 ? 124.414 125.033 152.165 1.00 94.23  ? 306 TYR A CA  1 
ATOM   1395 C  C   . TYR A 1 306 ? 125.286 125.960 151.314 1.00 94.23  ? 306 TYR A C   1 
ATOM   1396 O  O   . TYR A 1 306 ? 126.281 126.516 151.786 1.00 94.23  ? 306 TYR A O   1 
ATOM   1397 C  CB  . TYR A 1 306 ? 122.936 125.379 152.036 1.00 94.23  ? 306 TYR A CB  1 
ATOM   1398 C  CG  . TYR A 1 306 ? 122.547 126.582 152.863 1.00 94.23  ? 306 TYR A CG  1 
ATOM   1399 C  CD1 . TYR A 1 306 ? 122.620 127.862 152.333 1.00 94.23  ? 306 TYR A CD1 1 
ATOM   1400 C  CD2 . TYR A 1 306 ? 122.119 126.440 154.176 1.00 94.23  ? 306 TYR A CD2 1 
ATOM   1401 C  CE1 . TYR A 1 306 ? 122.278 128.962 153.080 1.00 94.23  ? 306 TYR A CE1 1 
ATOM   1402 C  CE2 . TYR A 1 306 ? 121.777 127.537 154.931 1.00 94.23  ? 306 TYR A CE2 1 
ATOM   1403 C  CZ  . TYR A 1 306 ? 121.857 128.795 154.378 1.00 94.23  ? 306 TYR A CZ  1 
ATOM   1404 O  OH  . TYR A 1 306 ? 121.514 129.894 155.128 1.00 94.23  ? 306 TYR A OH  1 
ATOM   1405 N  N   . GLU A 1 307 ? 124.909 126.144 150.046 1.00 85.78  ? 307 GLU A N   1 
ATOM   1406 C  CA  . GLU A 1 307 ? 125.556 127.107 149.160 1.00 85.78  ? 307 GLU A CA  1 
ATOM   1407 C  C   . GLU A 1 307 ? 124.723 127.287 147.895 1.00 85.78  ? 307 GLU A C   1 
ATOM   1408 O  O   . GLU A 1 307 ? 123.678 126.656 147.721 1.00 85.78  ? 307 GLU A O   1 
ATOM   1409 C  CB  . GLU A 1 307 ? 126.994 126.682 148.820 1.00 85.78  ? 307 GLU A CB  1 
ATOM   1410 C  CG  . GLU A 1 307 ? 127.121 125.319 148.173 1.00 85.78  ? 307 GLU A CG  1 
ATOM   1411 C  CD  . GLU A 1 307 ? 128.473 125.108 147.527 1.00 85.78  ? 307 GLU A CD  1 
ATOM   1412 O  OE1 . GLU A 1 307 ? 128.903 123.943 147.426 1.00 85.78  ? 307 GLU A OE1 1 
ATOM   1413 O  OE2 . GLU A 1 307 ? 129.105 126.105 147.123 1.00 85.78  ? 307 GLU A OE2 1 
ATOM   1414 N  N   . ALA A 1 308 ? 125.189 128.177 147.015 1.00 83.08  ? 308 ALA A N   1 
ATOM   1415 C  CA  . ALA A 1 308 ? 124.480 128.466 145.771 1.00 83.08  ? 308 ALA A CA  1 
ATOM   1416 C  C   . ALA A 1 308 ? 125.471 128.870 144.682 1.00 83.08  ? 308 ALA A C   1 
ATOM   1417 O  O   . ALA A 1 308 ? 126.238 129.822 144.867 1.00 83.08  ? 308 ALA A O   1 
ATOM   1418 C  CB  . ALA A 1 308 ? 123.442 129.571 145.990 1.00 83.08  ? 308 ALA A CB  1 
ATOM   1419 N  N   . GLY A 1 309 ? 125.437 128.167 143.545 1.00 62.36  ? 309 GLY A N   1 
ATOM   1420 C  CA  . GLY A 1 309 ? 126.382 128.389 142.472 1.00 62.36  ? 309 GLY A CA  1 
ATOM   1421 C  C   . GLY A 1 309 ? 125.795 129.194 141.333 1.00 62.36  ? 309 GLY A C   1 
ATOM   1422 O  O   . GLY A 1 309 ? 124.579 129.365 141.245 1.00 62.36  ? 309 GLY A O   1 
ATOM   1423 N  N   . PRO A 1 310 ? 126.644 129.689 140.427 1.00 52.48  ? 310 PRO A N   1 
ATOM   1424 C  CA  . PRO A 1 310 ? 126.158 130.614 139.391 1.00 52.48  ? 310 PRO A CA  1 
ATOM   1425 C  C   . PRO A 1 310 ? 125.172 129.940 138.450 1.00 52.48  ? 310 PRO A C   1 
ATOM   1426 O  O   . PRO A 1 310 ? 125.186 128.720 138.286 1.00 52.48  ? 310 PRO A O   1 
ATOM   1427 C  CB  . PRO A 1 310 ? 127.438 131.036 138.663 1.00 52.48  ? 310 PRO A CB  1 
ATOM   1428 N  N   . CYS A 1 311 ? 124.287 130.752 137.850 1.00 51.06  ? 311 CYS A N   1 
ATOM   1429 C  CA  . CYS A 1 311 ? 123.279 130.262 136.912 1.00 51.06  ? 311 CYS A CA  1 
ATOM   1430 C  C   . CYS A 1 311 ? 123.490 130.753 135.488 1.00 51.06  ? 311 CYS A C   1 
ATOM   1431 O  O   . CYS A 1 311 ? 122.799 130.281 134.583 1.00 51.06  ? 311 CYS A O   1 
ATOM   1432 C  CB  . CYS A 1 311 ? 121.880 130.666 137.355 1.00 51.06  ? 311 CYS A CB  1 
ATOM   1433 S  SG  . CYS A 1 311 ? 121.433 130.097 138.974 1.00 51.06  ? 311 CYS A SG  1 
ATOM   1434 N  N   . TRP A 1 312 ? 124.449 131.654 135.302 1.00 47.66  ? 312 TRP A N   1 
ATOM   1435 C  CA  . TRP A 1 312 ? 124.806 132.196 133.963 1.00 47.66  ? 312 TRP A CA  1 
ATOM   1436 C  C   . TRP A 1 312 ? 125.460 131.084 133.137 1.00 47.66  ? 312 TRP A C   1 
ATOM   1437 O  O   . TRP A 1 312 ? 125.671 131.291 131.930 1.00 47.66  ? 312 TRP A O   1 
ATOM   1438 C  CB  . TRP A 1 312 ? 125.753 133.393 134.137 1.00 47.66  ? 312 TRP A CB  1 
ATOM   1439 C  CG  . TRP A 1 312 ? 126.643 133.695 132.968 1.00 47.66  ? 312 TRP A CG  1 
ATOM   1440 C  CD1 . TRP A 1 312 ? 126.584 134.792 132.158 1.00 47.66  ? 312 TRP A CD1 1 
ATOM   1441 C  CD2 . TRP A 1 312 ? 127.754 132.913 132.494 1.00 47.66  ? 312 TRP A CD2 1 
ATOM   1442 N  NE1 . TRP A 1 312 ? 127.566 134.740 131.206 1.00 47.66  ? 312 TRP A NE1 1 
ATOM   1443 C  CE2 . TRP A 1 312 ? 128.298 133.597 131.385 1.00 47.66  ? 312 TRP A CE2 1 
ATOM   1444 C  CE3 . TRP A 1 312 ? 128.334 131.702 132.885 1.00 47.66  ? 312 TRP A CE3 1 
ATOM   1445 C  CZ2 . TRP A 1 312 ? 129.392 133.109 130.674 1.00 47.66  ? 312 TRP A CZ2 1 
ATOM   1446 C  CZ3 . TRP A 1 312 ? 129.412 131.217 132.181 1.00 47.66  ? 312 TRP A CZ3 1 
ATOM   1447 C  CH2 . TRP A 1 312 ? 129.934 131.915 131.092 1.00 47.66  ? 312 TRP A CH2 1 
ATOM   1448 N  N   . VAL A 1 313 ? 125.751 129.947 133.761 1.00 39.51  ? 313 VAL A N   1 
ATOM   1449 C  CA  . VAL A 1 313 ? 126.427 128.810 133.069 1.00 39.51  ? 313 VAL A CA  1 
ATOM   1450 C  C   . VAL A 1 313 ? 125.486 127.604 133.060 1.00 39.51  ? 313 VAL A C   1 
ATOM   1451 O  O   . VAL A 1 313 ? 125.912 126.535 132.600 1.00 39.51  ? 313 VAL A O   1 
ATOM   1452 C  CB  . VAL A 1 313 ? 127.767 128.463 133.745 1.00 39.51  ? 313 VAL A CB  1 
ATOM   1453 N  N   . LEU A 1 314 ? 124.276 127.744 133.570 1.00 34.14  ? 314 LEU A N   1 
ATOM   1454 C  CA  . LEU A 1 314 ? 123.329 126.601 133.541 1.00 34.14  ? 314 LEU A CA  1 
ATOM   1455 C  C   . LEU A 1 314 ? 122.691 126.575 132.150 1.00 34.14  ? 314 LEU A C   1 
ATOM   1456 O  O   . LEU A 1 314 ? 122.266 125.491 131.711 1.00 34.14  ? 314 LEU A O   1 
ATOM   1457 C  CB  . LEU A 1 314 ? 122.280 126.796 134.640 1.00 34.14  ? 314 LEU A CB  1 
ATOM   1458 C  CG  . LEU A 1 314 ? 121.927 125.543 135.437 1.00 34.14  ? 314 LEU A CG  1 
ATOM   1459 C  CD1 . LEU A 1 314 ? 120.632 125.738 136.207 1.00 34.14  ? 314 LEU A CD1 1 
ATOM   1460 C  CD2 . LEU A 1 314 ? 121.817 124.338 134.521 1.00 34.14  ? 314 LEU A CD2 1 
ATOM   1461 N  N   . TYR A 1 315 ? 122.644 127.729 131.490 1.00 27.29  ? 315 TYR A N   1 
ATOM   1462 C  CA  . TYR A 1 315 ? 122.074 127.860 130.123 1.00 27.29  ? 315 TYR A CA  1 
ATOM   1463 C  C   . TYR A 1 315 ? 123.189 128.269 129.157 1.00 27.29  ? 315 TYR A C   1 
ATOM   1464 O  O   . TYR A 1 315 ? 122.950 129.138 128.294 1.00 27.29  ? 315 TYR A O   1 
ATOM   1465 C  CB  . TYR A 1 315 ? 120.946 128.892 130.100 1.00 27.29  ? 315 TYR A CB  1 
ATOM   1466 C  CG  . TYR A 1 315 ? 119.760 128.529 130.953 1.00 27.29  ? 315 TYR A CG  1 
ATOM   1467 C  CD1 . TYR A 1 315 ? 119.249 127.244 130.946 1.00 27.29  ? 315 TYR A CD1 1 
ATOM   1468 C  CD2 . TYR A 1 315 ? 119.155 129.465 131.773 1.00 27.29  ? 315 TYR A CD2 1 
ATOM   1469 C  CE1 . TYR A 1 315 ? 118.161 126.897 131.728 1.00 27.29  ? 315 TYR A CE1 1 
ATOM   1470 C  CE2 . TYR A 1 315 ? 118.068 129.135 132.562 1.00 27.29  ? 315 TYR A CE2 1 
ATOM   1471 C  CZ  . TYR A 1 315 ? 117.569 127.846 132.539 1.00 27.29  ? 315 TYR A CZ  1 
ATOM   1472 O  OH  . TYR A 1 315 ? 116.500 127.511 133.315 1.00 27.29  ? 315 TYR A OH  1 
ATOM   1473 N  N   . LEU A 1 316 ? 124.373 127.687 129.324 1.00 25.41  ? 316 LEU A N   1 
ATOM   1474 C  CA  . LEU A 1 316 ? 125.527 127.961 128.426 1.00 25.41  ? 316 LEU A CA  1 
ATOM   1475 C  C   . LEU A 1 316 ? 125.562 126.882 127.343 1.00 25.41  ? 316 LEU A C   1 
ATOM   1476 O  O   . LEU A 1 316 ? 126.503 126.898 126.538 1.00 25.41  ? 316 LEU A O   1 
ATOM   1477 C  CB  . LEU A 1 316 ? 126.824 127.947 129.238 1.00 25.41  ? 316 LEU A CB  1 
ATOM   1478 N  N   . ASP A 1 317 ? 124.577 125.980 127.328 1.00 23.41  ? 317 ASP A N   1 
ATOM   1479 C  CA  . ASP A 1 317 ? 124.534 124.888 126.316 1.00 23.41  ? 317 ASP A CA  1 
ATOM   1480 C  C   . ASP A 1 317 ? 123.435 125.151 125.277 1.00 23.41  ? 317 ASP A C   1 
ATOM   1481 O  O   . ASP A 1 317 ? 123.793 125.337 124.098 1.00 23.41  ? 317 ASP A O   1 
ATOM   1482 C  CB  . ASP A 1 317 ? 124.339 123.523 126.977 1.00 23.41  ? 317 ASP A CB  1 
ATOM   1483 C  CG  . ASP A 1 317 ? 123.459 122.589 126.165 1.00 23.41  ? 317 ASP A CG  1 
ATOM   1484 O  OD1 . ASP A 1 317 ? 123.995 121.601 125.627 1.00 23.41  ? 317 ASP A OD1 1 
ATOM   1485 O  OD2 . ASP A 1 317 ? 122.245 122.859 126.075 1.00 23.41  ? 317 ASP A OD2 1 
ATOM   1486 N  N   . PRO A 1 318 ? 122.147 125.190 125.673 1.00 23.51  ? 318 PRO A N   1 
ATOM   1487 C  CA  . PRO A 1 318 ? 121.162 125.469 124.619 1.00 23.51  ? 318 PRO A CA  1 
ATOM   1488 C  C   . PRO A 1 318 ? 121.492 126.655 123.734 1.00 23.51  ? 318 PRO A C   1 
ATOM   1489 O  O   . PRO A 1 318 ? 121.141 126.621 122.552 1.00 23.51  ? 318 PRO A O   1 
ATOM   1490 C  CB  . PRO A 1 318 ? 119.867 125.698 125.400 1.00 23.51  ? 318 PRO A CB  1 
ATOM   1491 C  CG  . PRO A 1 318 ? 120.292 125.995 126.745 1.00 23.51  ? 318 PRO A CG  1 
ATOM   1492 C  CD  . PRO A 1 318 ? 121.506 125.191 126.990 1.00 23.51  ? 318 PRO A CD  1 
ATOM   1493 N  N   . THR A 1 319 ? 122.150 127.697 124.225 1.00 21.21  ? 319 THR A N   1 
ATOM   1494 C  CA  . THR A 1 319 ? 122.583 128.723 123.286 1.00 21.21  ? 319 THR A CA  1 
ATOM   1495 C  C   . THR A 1 319 ? 123.588 128.162 122.293 1.00 21.21  ? 319 THR A C   1 
ATOM   1496 O  O   . THR A 1 319 ? 123.571 128.516 121.108 1.00 21.21  ? 319 THR A O   1 
ATOM   1497 C  CB  . THR A 1 319 ? 123.174 129.909 124.016 1.00 21.21  ? 319 THR A CB  1 
ATOM   1498 O  OG1 . THR A 1 319 ? 122.177 130.467 124.870 1.00 21.21  ? 319 THR A OG1 1 
ATOM   1499 C  CG2 . THR A 1 319 ? 123.619 130.948 123.014 1.00 21.21  ? 319 THR A CG2 1 
ATOM   1500 N  N   . LEU A 1 320 ? 124.449 127.261 122.737 1.00 19.29  ? 320 LEU A N   1 
ATOM   1501 C  CA  . LEU A 1 320 ? 125.371 126.651 121.794 1.00 19.29  ? 320 LEU A CA  1 
ATOM   1502 C  C   . LEU A 1 320 ? 124.640 125.748 120.800 1.00 19.29  ? 320 LEU A C   1 
ATOM   1503 O  O   . LEU A 1 320 ? 125.009 125.699 119.624 1.00 19.29  ? 320 LEU A O   1 
ATOM   1504 C  CB  . LEU A 1 320 ? 126.457 125.901 122.548 1.00 19.29  ? 320 LEU A CB  1 
ATOM   1505 C  CG  . LEU A 1 320 ? 127.374 126.798 123.381 1.00 19.29  ? 320 LEU A CG  1 
ATOM   1506 C  CD1 . LEU A 1 320 ? 128.495 125.990 123.970 1.00 19.29  ? 320 LEU A CD1 1 
ATOM   1507 C  CD2 . LEU A 1 320 ? 127.943 127.934 122.571 1.00 19.29  ? 320 LEU A CD2 1 
ATOM   1508 N  N   . CYS A 1 321 ? 123.594 125.041 121.230 1.00 20.76  ? 321 CYS A N   1 
ATOM   1509 C  CA  . CYS A 1 321 ? 122.835 124.249 120.262 1.00 20.76  ? 321 CYS A CA  1 
ATOM   1510 C  C   . CYS A 1 321 ? 122.106 125.126 119.259 1.00 20.76  ? 321 CYS A C   1 
ATOM   1511 O  O   . CYS A 1 321 ? 122.019 124.772 118.081 1.00 20.76  ? 321 CYS A O   1 
ATOM   1512 C  CB  . CYS A 1 321 ? 121.840 123.327 120.947 1.00 20.76  ? 321 CYS A CB  1 
ATOM   1513 S  SG  . CYS A 1 321 ? 122.588 121.902 121.721 1.00 20.76  ? 321 CYS A SG  1 
ATOM   1514 N  N   . VAL A 1 322 ? 121.566 126.261 119.690 1.00 16.24  ? 322 VAL A N   1 
ATOM   1515 C  CA  . VAL A 1 322 ? 120.925 127.168 118.742 1.00 16.24  ? 322 VAL A CA  1 
ATOM   1516 C  C   . VAL A 1 322 ? 121.939 127.707 117.736 1.00 16.24  ? 322 VAL A C   1 
ATOM   1517 O  O   . VAL A 1 322 ? 121.637 127.850 116.545 1.00 16.24  ? 322 VAL A O   1 
ATOM   1518 C  CB  . VAL A 1 322 ? 120.202 128.294 119.495 1.00 16.24  ? 322 VAL A CB  1 
ATOM   1519 C  CG1 . VAL A 1 322 ? 119.986 129.472 118.590 1.00 16.24  ? 322 VAL A CG1 1 
ATOM   1520 C  CG2 . VAL A 1 322 ? 118.886 127.789 120.051 1.00 16.24  ? 322 VAL A CG2 1 
ATOM   1521 N  N   . VAL A 1 323 ? 123.164 127.987 118.178 1.00 18.03  ? 323 VAL A N   1 
ATOM   1522 C  CA  . VAL A 1 323 ? 124.164 128.413 117.206 1.00 18.03  ? 323 VAL A CA  1 
ATOM   1523 C  C   . VAL A 1 323 ? 124.537 127.284 116.246 1.00 18.03  ? 323 VAL A C   1 
ATOM   1524 O  O   . VAL A 1 323 ? 124.711 127.519 115.045 1.00 18.03  ? 323 VAL A O   1 
ATOM   1525 C  CB  . VAL A 1 323 ? 125.406 128.970 117.906 1.00 18.03  ? 323 VAL A CB  1 
ATOM   1526 C  CG1 . VAL A 1 323 ? 126.302 129.584 116.889 1.00 18.03  ? 323 VAL A CG1 1 
ATOM   1527 C  CG2 . VAL A 1 323 ? 125.017 130.018 118.896 1.00 18.03  ? 323 VAL A CG2 1 
ATOM   1528 N  N   . MET A 1 324 ? 124.669 126.051 116.732 1.00 20.51  ? 324 MET A N   1 
ATOM   1529 C  CA  . MET A 1 324 ? 124.985 124.944 115.826 1.00 20.51  ? 324 MET A CA  1 
ATOM   1530 C  C   . MET A 1 324 ? 123.870 124.711 114.814 1.00 20.51  ? 324 MET A C   1 
ATOM   1531 O  O   . MET A 1 324 ? 124.135 124.374 113.654 1.00 20.51  ? 324 MET A O   1 
ATOM   1532 C  CB  . MET A 1 324 ? 125.248 123.676 116.621 1.00 20.51  ? 324 MET A CB  1 
ATOM   1533 C  CG  . MET A 1 324 ? 125.494 122.457 115.794 1.00 20.51  ? 324 MET A CG  1 
ATOM   1534 S  SD  . MET A 1 324 ? 125.535 120.978 116.819 1.00 20.51  ? 324 MET A SD  1 
ATOM   1535 C  CE  . MET A 1 324 ? 123.860 120.395 116.666 1.00 20.51  ? 324 MET A CE  1 
ATOM   1536 N  N   . VAL A 1 325 ? 122.619 124.892 115.229 1.00 14.59  ? 325 VAL A N   1 
ATOM   1537 C  CA  . VAL A 1 325 ? 121.494 124.736 114.313 1.00 14.59  ? 325 VAL A CA  1 
ATOM   1538 C  C   . VAL A 1 325 ? 121.506 125.808 113.234 1.00 14.59  ? 325 VAL A C   1 
ATOM   1539 O  O   . VAL A 1 325 ? 121.316 125.516 112.048 1.00 14.59  ? 325 VAL A O   1 
ATOM   1540 C  CB  . VAL A 1 325 ? 120.180 124.749 115.096 1.00 14.59  ? 325 VAL A CB  1 
ATOM   1541 C  CG1 . VAL A 1 325 ? 119.066 125.137 114.197 1.00 14.59  ? 325 VAL A CG1 1 
ATOM   1542 C  CG2 . VAL A 1 325 ? 119.932 123.387 115.647 1.00 14.59  ? 325 VAL A CG2 1 
ATOM   1543 N  N   . CYS A 1 326 ? 121.703 127.064 113.612 1.00 17.16  ? 326 CYS A N   1 
ATOM   1544 C  CA  . CYS A 1 326 ? 121.771 128.087 112.574 1.00 17.16  ? 326 CYS A CA  1 
ATOM   1545 C  C   . CYS A 1 326 ? 123.020 127.960 111.712 1.00 17.16  ? 326 CYS A C   1 
ATOM   1546 O  O   . CYS A 1 326 ? 123.074 128.554 110.639 1.00 17.16  ? 326 CYS A O   1 
ATOM   1547 C  CB  . CYS A 1 326 ? 121.694 129.473 113.202 1.00 17.16  ? 326 CYS A CB  1 
ATOM   1548 S  SG  . CYS A 1 326 ? 122.050 130.849 112.102 1.00 17.16  ? 326 CYS A SG  1 
ATOM   1549 N  N   . ILE A 1 327 ? 124.027 127.211 112.145 1.00 14.65  ? 327 ILE A N   1 
ATOM   1550 C  CA  . ILE A 1 327 ? 125.153 126.959 111.251 1.00 14.65  ? 327 ILE A CA  1 
ATOM   1551 C  C   . ILE A 1 327 ? 124.813 125.876 110.229 1.00 14.65  ? 327 ILE A C   1 
ATOM   1552 O  O   . ILE A 1 327 ? 125.059 126.034 109.023 1.00 14.65  ? 327 ILE A O   1 
ATOM   1553 C  CB  . ILE A 1 327 ? 126.401 126.582 112.060 1.00 14.65  ? 327 ILE A CB  1 
ATOM   1554 C  CG1 . ILE A 1 327 ? 126.853 127.744 112.935 1.00 14.65  ? 327 ILE A CG1 1 
ATOM   1555 C  CG2 . ILE A 1 327 ? 127.512 126.180 111.131 1.00 14.65  ? 327 ILE A CG2 1 
ATOM   1556 C  CD1 . ILE A 1 327 ? 127.397 128.899 112.180 1.00 14.65  ? 327 ILE A CD1 1 
ATOM   1557 N  N   . LEU A 1 328 ? 124.252 124.755 110.684 1.00 17.68  ? 328 LEU A N   1 
ATOM   1558 C  CA  . LEU A 1 328 ? 123.933 123.674 109.757 1.00 17.68  ? 328 LEU A CA  1 
ATOM   1559 C  C   . LEU A 1 328 ? 122.852 124.067 108.761 1.00 17.68  ? 328 LEU A C   1 
ATOM   1560 O  O   . LEU A 1 328 ? 122.920 123.685 107.593 1.00 17.68  ? 328 LEU A O   1 
ATOM   1561 C  CB  . LEU A 1 328 ? 123.492 122.433 110.506 1.00 17.68  ? 328 LEU A CB  1 
ATOM   1562 C  CG  . LEU A 1 328 ? 124.644 121.531 110.856 1.00 17.68  ? 328 LEU A CG  1 
ATOM   1563 C  CD1 . LEU A 1 328 ? 124.113 120.207 111.313 1.00 17.68  ? 328 LEU A CD1 1 
ATOM   1564 C  CD2 . LEU A 1 328 ? 125.465 121.381 109.634 1.00 17.68  ? 328 LEU A CD2 1 
ATOM   1565 N  N   . LEU A 1 329 ? 121.825 124.794 109.198 1.00 9.95   ? 329 LEU A N   1 
ATOM   1566 C  CA  . LEU A 1 329 ? 120.724 125.078 108.285 1.00 9.95   ? 329 LEU A CA  1 
ATOM   1567 C  C   . LEU A 1 329 ? 121.095 126.073 107.207 1.00 9.95   ? 329 LEU A C   1 
ATOM   1568 O  O   . LEU A 1 329 ? 120.318 126.274 106.278 1.00 9.95   ? 329 LEU A O   1 
ATOM   1569 C  CB  . LEU A 1 329 ? 119.525 125.614 109.039 1.00 9.95   ? 329 LEU A CB  1 
ATOM   1570 C  CG  . LEU A 1 329 ? 118.822 124.586 109.891 1.00 9.95   ? 329 LEU A CG  1 
ATOM   1571 C  CD1 . LEU A 1 329 ? 117.485 125.138 110.288 1.00 9.95   ? 329 LEU A CD1 1 
ATOM   1572 C  CD2 . LEU A 1 329 ? 118.692 123.315 109.116 1.00 9.95   ? 329 LEU A CD2 1 
ATOM   1573 N  N   . TYR A 1 330 ? 122.226 126.735 107.322 1.00 16.50  ? 330 TYR A N   1 
ATOM   1574 C  CA  . TYR A 1 330 ? 122.663 127.558 106.215 1.00 16.50  ? 330 TYR A CA  1 
ATOM   1575 C  C   . TYR A 1 330 ? 123.727 126.869 105.399 1.00 16.50  ? 330 TYR A C   1 
ATOM   1576 O  O   . TYR A 1 330 ? 123.853 127.133 104.204 1.00 16.50  ? 330 TYR A O   1 
ATOM   1577 C  CB  . TYR A 1 330 ? 123.202 128.884 106.707 1.00 16.50  ? 330 TYR A CB  1 
ATOM   1578 C  CG  . TYR A 1 330 ? 123.991 129.601 105.665 1.00 16.50  ? 330 TYR A CG  1 
ATOM   1579 C  CD1 . TYR A 1 330 ? 123.419 129.964 104.469 1.00 16.50  ? 330 TYR A CD1 1 
ATOM   1580 C  CD2 . TYR A 1 330 ? 125.304 129.925 105.877 1.00 16.50  ? 330 TYR A CD2 1 
ATOM   1581 C  CE1 . TYR A 1 330 ? 124.137 130.620 103.511 1.00 16.50  ? 330 TYR A CE1 1 
ATOM   1582 C  CE2 . TYR A 1 330 ? 126.027 130.587 104.922 1.00 16.50  ? 330 TYR A CE2 1 
ATOM   1583 C  CZ  . TYR A 1 330 ? 125.440 130.932 103.742 1.00 16.50  ? 330 TYR A CZ  1 
ATOM   1584 O  OH  . TYR A 1 330 ? 126.168 131.594 102.787 1.00 16.50  ? 330 TYR A OH  1 
ATOM   1585 N  N   . THR A 1 331 ? 124.517 125.989 106.008 1.00 16.06  ? 331 THR A N   1 
ATOM   1586 C  CA  . THR A 1 331 ? 125.457 125.255 105.176 1.00 16.06  ? 331 THR A CA  1 
ATOM   1587 C  C   . THR A 1 331 ? 124.770 124.185 104.331 1.00 16.06  ? 331 THR A C   1 
ATOM   1588 O  O   . THR A 1 331 ? 125.259 123.867 103.247 1.00 16.06  ? 331 THR A O   1 
ATOM   1589 C  CB  . THR A 1 331 ? 126.546 124.646 106.040 1.00 16.06  ? 331 THR A CB  1 
ATOM   1590 O  OG1 . THR A 1 331 ? 126.916 125.586 107.048 1.00 16.06  ? 331 THR A OG1 1 
ATOM   1591 C  CG2 . THR A 1 331 ? 127.746 124.411 105.214 1.00 16.06  ? 331 THR A CG2 1 
ATOM   1592 N  N   . THR A 1 332 ? 123.630 123.656 104.775 1.00 14.58  ? 332 THR A N   1 
ATOM   1593 C  CA  . THR A 1 332 ? 122.910 122.626 104.037 1.00 14.58  ? 332 THR A CA  1 
ATOM   1594 C  C   . THR A 1 332 ? 122.095 123.168 102.880 1.00 14.58  ? 332 THR A C   1 
ATOM   1595 O  O   . THR A 1 332 ? 122.127 122.587 101.797 1.00 14.58  ? 332 THR A O   1 
ATOM   1596 C  CB  . THR A 1 332 ? 121.975 121.858 104.964 1.00 14.58  ? 332 THR A CB  1 
ATOM   1597 O  OG1 . THR A 1 332 ? 122.727 120.928 105.734 1.00 14.58  ? 332 THR A OG1 1 
ATOM   1598 C  CG2 . THR A 1 332 ? 120.947 121.119 104.196 1.00 14.58  ? 332 THR A CG2 1 
ATOM   1599 N  N   . TYR A 1 333 ? 121.380 124.269 103.067 1.00 12.94  ? 333 TYR A N   1 
ATOM   1600 C  CA  . TYR A 1 333 ? 120.361 124.670 102.098 1.00 12.94  ? 333 TYR A CA  1 
ATOM   1601 C  C   . TYR A 1 333 ? 120.832 124.659 100.651 1.00 12.94  ? 333 TYR A C   1 
ATOM   1602 O  O   . TYR A 1 333 ? 120.148 124.039 99.827  1.00 12.94  ? 333 TYR A O   1 
ATOM   1603 C  CB  . TYR A 1 333 ? 119.795 126.045 102.464 1.00 12.94  ? 333 TYR A CB  1 
ATOM   1604 C  CG  . TYR A 1 333 ? 119.231 126.802 101.293 1.00 12.94  ? 333 TYR A CG  1 
ATOM   1605 C  CD1 . TYR A 1 333 ? 117.934 126.597 100.865 1.00 12.94  ? 333 TYR A CD1 1 
ATOM   1606 C  CD2 . TYR A 1 333 ? 119.997 127.730 100.620 1.00 12.94  ? 333 TYR A CD2 1 
ATOM   1607 C  CE1 . TYR A 1 333 ? 117.423 127.297 99.796  1.00 12.94  ? 333 TYR A CE1 1 
ATOM   1608 C  CE2 . TYR A 1 333 ? 119.500 128.425 99.554  1.00 12.94  ? 333 TYR A CE2 1 
ATOM   1609 C  CZ  . TYR A 1 333 ? 118.217 128.208 99.144  1.00 12.94  ? 333 TYR A CZ  1 
ATOM   1610 O  OH  . TYR A 1 333 ? 117.745 128.920 98.074  1.00 12.94  ? 333 TYR A OH  1 
ATOM   1611 N  N   . PRO A 1 334 ? 121.960 125.268 100.266 1.00 13.29  ? 334 PRO A N   1 
ATOM   1612 C  CA  . PRO A 1 334 ? 122.300 125.279 98.831  1.00 13.29  ? 334 PRO A CA  1 
ATOM   1613 C  C   . PRO A 1 334 ? 122.404 123.896 98.210  1.00 13.29  ? 334 PRO A C   1 
ATOM   1614 O  O   . PRO A 1 334 ? 121.991 123.704 97.059  1.00 13.29  ? 334 PRO A O   1 
ATOM   1615 C  CB  . PRO A 1 334 ? 123.636 126.029 98.795  1.00 13.29  ? 334 PRO A CB  1 
ATOM   1616 C  CG  . PRO A 1 334 ? 124.132 126.006 100.171 1.00 13.29  ? 334 PRO A CG  1 
ATOM   1617 C  CD  . PRO A 1 334 ? 122.947 126.021 101.047 1.00 13.29  ? 334 PRO A CD  1 
ATOM   1618 N  N   . LEU A 1 335 ? 122.928 122.922 98.949  1.00 15.44  ? 335 LEU A N   1 
ATOM   1619 C  CA  . LEU A 1 335 ? 122.901 121.538 98.495  1.00 15.44  ? 335 LEU A CA  1 
ATOM   1620 C  C   . LEU A 1 335 ? 121.481 121.080 98.213  1.00 15.44  ? 335 LEU A C   1 
ATOM   1621 O  O   . LEU A 1 335 ? 121.212 120.448 97.186  1.00 15.44  ? 335 LEU A O   1 
ATOM   1622 C  CB  . LEU A 1 335 ? 123.543 120.641 99.538  1.00 15.44  ? 335 LEU A CB  1 
ATOM   1623 C  CG  . LEU A 1 335 ? 123.137 119.187 99.437  1.00 15.44  ? 335 LEU A CG  1 
ATOM   1624 C  CD1 . LEU A 1 335 ? 123.610 118.612 98.147  1.00 15.44  ? 335 LEU A CD1 1 
ATOM   1625 C  CD2 . LEU A 1 335 ? 123.693 118.411 100.600 1.00 15.44  ? 335 LEU A CD2 1 
ATOM   1626 N  N   . LEU A 1 336 ? 120.557 121.368 99.122  1.00 10.60  ? 336 LEU A N   1 
ATOM   1627 C  CA  . LEU A 1 336 ? 119.189 120.909 98.927  1.00 10.60  ? 336 LEU A CA  1 
ATOM   1628 C  C   . LEU A 1 336 ? 118.532 121.617 97.753  1.00 10.60  ? 336 LEU A C   1 
ATOM   1629 O  O   . LEU A 1 336 ? 117.769 121.004 96.997  1.00 10.60  ? 336 LEU A O   1 
ATOM   1630 C  CB  . LEU A 1 336 ? 118.389 121.109 100.198 1.00 10.60  ? 336 LEU A CB  1 
ATOM   1631 C  CG  . LEU A 1 336 ? 117.078 120.363 100.174 1.00 10.60  ? 336 LEU A CG  1 
ATOM   1632 C  CD1 . LEU A 1 336 ? 116.820 119.803 101.519 1.00 10.60  ? 336 LEU A CD1 1 
ATOM   1633 C  CD2 . LEU A 1 336 ? 115.999 121.326 99.836  1.00 10.60  ? 336 LEU A CD2 1 
ATOM   1634 N  N   . LYS A 1 337 ? 118.826 122.897 97.568  1.00 13.65  ? 337 LYS A N   1 
ATOM   1635 C  CA  . LYS A 1 337 ? 118.311 123.594 96.402  1.00 13.65  ? 337 LYS A CA  1 
ATOM   1636 C  C   . LYS A 1 337 ? 118.798 122.939 95.126  1.00 13.65  ? 337 LYS A C   1 
ATOM   1637 O  O   . LYS A 1 337 ? 118.003 122.652 94.228  1.00 13.65  ? 337 LYS A O   1 
ATOM   1638 C  CB  . LYS A 1 337 ? 118.722 125.053 96.423  1.00 13.65  ? 337 LYS A CB  1 
ATOM   1639 C  CG  . LYS A 1 337 ? 118.687 125.692 95.067  1.00 13.65  ? 337 LYS A CG  1 
ATOM   1640 C  CD  . LYS A 1 337 ? 119.386 127.019 95.096  1.00 13.65  ? 337 LYS A CD  1 
ATOM   1641 C  CE  . LYS A 1 337 ? 119.930 127.385 93.742  1.00 13.65  ? 337 LYS A CE  1 
ATOM   1642 N  NZ  . LYS A 1 337 ? 121.032 128.364 93.870  1.00 13.65  ? 337 LYS A NZ  1 
ATOM   1643 N  N   . GLU A 1 338 ? 120.101 122.677 95.026  1.00 10.86  ? 338 GLU A N   1 
ATOM   1644 C  CA  . GLU A 1 338 ? 120.630 122.117 93.784  1.00 10.86  ? 338 GLU A CA  1 
ATOM   1645 C  C   . GLU A 1 338 ? 120.081 120.727 93.505  1.00 10.86  ? 338 GLU A C   1 
ATOM   1646 O  O   . GLU A 1 338 ? 119.760 120.396 92.360  1.00 10.86  ? 338 GLU A O   1 
ATOM   1647 C  CB  . GLU A 1 338 ? 122.144 122.074 93.823  1.00 10.86  ? 338 GLU A CB  1 
ATOM   1648 C  CG  . GLU A 1 338 ? 122.720 121.658 92.525  1.00 10.86  ? 338 GLU A CG  1 
ATOM   1649 C  CD  . GLU A 1 338 ? 122.498 122.700 91.459  1.00 10.86  ? 338 GLU A CD  1 
ATOM   1650 O  OE1 . GLU A 1 338 ? 122.094 123.831 91.793  1.00 10.86  ? 338 GLU A OE1 1 
ATOM   1651 O  OE2 . GLU A 1 338 ? 122.737 122.402 90.276  1.00 10.86  ? 338 GLU A OE2 1 
ATOM   1652 N  N   . SER A 1 339 ? 119.949 119.902 94.536  1.00 9.98   ? 339 SER A N   1 
ATOM   1653 C  CA  . SER A 1 339 ? 119.414 118.566 94.326  1.00 9.98   ? 339 SER A CA  1 
ATOM   1654 C  C   . SER A 1 339 ? 117.959 118.606 93.873  1.00 9.98   ? 339 SER A C   1 
ATOM   1655 O  O   . SER A 1 339 ? 117.581 117.930 92.907  1.00 9.98   ? 339 SER A O   1 
ATOM   1656 C  CB  . SER A 1 339 ? 119.559 117.756 95.595  1.00 9.98   ? 339 SER A CB  1 
ATOM   1657 O  OG  . SER A 1 339 ? 118.564 116.773 95.629  1.00 9.98   ? 339 SER A OG  1 
ATOM   1658 N  N   . ALA A 1 340 ? 117.114 119.387 94.544  1.00 8.14   ? 340 ALA A N   1 
ATOM   1659 C  CA  . ALA A 1 340 ? 115.716 119.409 94.128  1.00 8.14   ? 340 ALA A CA  1 
ATOM   1660 C  C   . ALA A 1 340 ? 115.560 120.030 92.748  1.00 8.14   ? 340 ALA A C   1 
ATOM   1661 O  O   . ALA A 1 340 ? 114.700 119.617 91.964  1.00 8.14   ? 340 ALA A O   1 
ATOM   1662 C  CB  . ALA A 1 340 ? 114.867 120.153 95.145  1.00 8.14   ? 340 ALA A CB  1 
ATOM   1663 N  N   . LEU A 1 341 ? 116.392 121.011 92.420  1.00 7.72   ? 341 LEU A N   1 
ATOM   1664 C  CA  . LEU A 1 341 ? 116.330 121.592 91.089  1.00 7.72   ? 341 LEU A CA  1 
ATOM   1665 C  C   . LEU A 1 341 ? 116.700 120.580 90.011  1.00 7.72   ? 341 LEU A C   1 
ATOM   1666 O  O   . LEU A 1 341 ? 116.019 120.490 88.989  1.00 7.72   ? 341 LEU A O   1 
ATOM   1667 C  CB  . LEU A 1 341 ? 117.225 122.819 91.028  1.00 7.72   ? 341 LEU A CB  1 
ATOM   1668 C  CG  . LEU A 1 341 ? 116.497 124.142 91.203  1.00 7.72   ? 341 LEU A CG  1 
ATOM   1669 C  CD1 . LEU A 1 341 ? 115.906 124.552 89.903  1.00 7.72   ? 341 LEU A CD1 1 
ATOM   1670 C  CD2 . LEU A 1 341 ? 115.377 123.974 92.183  1.00 7.72   ? 341 LEU A CD2 1 
ATOM   1671 N  N   . ILE A 1 342 ? 117.762 119.800 90.209  1.00 8.86   ? 342 ILE A N   1 
ATOM   1672 C  CA  . ILE A 1 342 ? 118.064 118.756 89.232  1.00 8.86   ? 342 ILE A CA  1 
ATOM   1673 C  C   . ILE A 1 342 ? 116.898 117.795 89.097  1.00 8.86   ? 342 ILE A C   1 
ATOM   1674 O  O   . ILE A 1 342 ? 116.591 117.326 88.000  1.00 8.86   ? 342 ILE A O   1 
ATOM   1675 C  CB  . ILE A 1 342 ? 119.345 118.010 89.617  1.00 8.86   ? 342 ILE A CB  1 
ATOM   1676 C  CG1 . ILE A 1 342 ? 120.557 118.699 89.055  1.00 8.86   ? 342 ILE A CG1 1 
ATOM   1677 C  CG2 . ILE A 1 342 ? 119.326 116.638 89.105  1.00 8.86   ? 342 ILE A CG2 1 
ATOM   1678 C  CD1 . ILE A 1 342 ? 121.805 117.983 89.419  1.00 8.86   ? 342 ILE A CD1 1 
ATOM   1679 N  N   . LEU A 1 343 ? 116.230 117.479 90.204  1.00 4.92   ? 343 LEU A N   1 
ATOM   1680 C  CA  . LEU A 1 343 ? 115.179 116.472 90.131  1.00 4.92   ? 343 LEU A CA  1 
ATOM   1681 C  C   . LEU A 1 343 ? 113.840 117.025 89.669  1.00 4.92   ? 343 LEU A C   1 
ATOM   1682 O  O   . LEU A 1 343 ? 112.886 116.256 89.559  1.00 4.92   ? 343 LEU A O   1 
ATOM   1683 C  CB  . LEU A 1 343 ? 115.008 115.787 91.484  1.00 4.92   ? 343 LEU A CB  1 
ATOM   1684 C  CG  . LEU A 1 343 ? 115.812 114.519 91.730  1.00 4.92   ? 343 LEU A CG  1 
ATOM   1685 C  CD1 . LEU A 1 343 ? 117.220 114.848 92.021  1.00 4.92   ? 343 LEU A CD1 1 
ATOM   1686 C  CD2 . LEU A 1 343 ? 115.254 113.788 92.877  1.00 4.92   ? 343 LEU A CD2 1 
ATOM   1687 N  N   . LEU A 1 344 ? 113.726 118.327 89.424  1.00 7.64   ? 344 LEU A N   1 
ATOM   1688 C  CA  . LEU A 1 344 ? 112.496 118.894 88.881  1.00 7.64   ? 344 LEU A CA  1 
ATOM   1689 C  C   . LEU A 1 344 ? 112.605 119.254 87.395  1.00 7.64   ? 344 LEU A C   1 
ATOM   1690 O  O   . LEU A 1 344 ? 111.889 120.145 86.926  1.00 7.64   ? 344 LEU A O   1 
ATOM   1691 C  CB  . LEU A 1 344 ? 112.077 120.124 89.683  1.00 7.64   ? 344 LEU A CB  1 
ATOM   1692 C  CG  . LEU A 1 344 ? 111.295 119.899 90.969  1.00 7.64   ? 344 LEU A CG  1 
ATOM   1693 C  CD1 . LEU A 1 344 ? 110.866 121.214 91.510  1.00 7.64   ? 344 LEU A CD1 1 
ATOM   1694 C  CD2 . LEU A 1 344 ? 110.106 119.027 90.733  1.00 7.64   ? 344 LEU A CD2 1 
ATOM   1695 N  N   . GLN A 1 345 ? 113.487 118.582 86.653  1.00 9.26   ? 345 GLN A N   1 
ATOM   1696 C  CA  . GLN A 1 345 ? 113.595 118.721 85.202  1.00 9.26   ? 345 GLN A CA  1 
ATOM   1697 C  C   . GLN A 1 345 ? 113.910 120.144 84.787  1.00 9.26   ? 345 GLN A C   1 
ATOM   1698 O  O   . GLN A 1 345 ? 113.544 120.577 83.701  1.00 9.26   ? 345 GLN A O   1 
ATOM   1699 C  CB  . GLN A 1 345 ? 112.325 118.279 84.495  1.00 9.26   ? 345 GLN A CB  1 
ATOM   1700 C  CG  . GLN A 1 345 ? 111.779 116.977 84.895  1.00 9.26   ? 345 GLN A CG  1 
ATOM   1701 C  CD  . GLN A 1 345 ? 112.690 115.878 84.576  1.00 9.26   ? 345 GLN A CD  1 
ATOM   1702 O  OE1 . GLN A 1 345 ? 113.507 115.992 83.686  1.00 9.26   ? 345 GLN A OE1 1 
ATOM   1703 N  NE2 . GLN A 1 345 ? 112.534 114.769 85.264  1.00 9.26   ? 345 GLN A NE2 1 
ATOM   1704 N  N   . THR A 1 346 ? 114.579 120.890 85.640  1.00 9.08   ? 346 THR A N   1 
ATOM   1705 C  CA  . THR A 1 346 ? 114.786 122.288 85.329  1.00 9.08   ? 346 THR A CA  1 
ATOM   1706 C  C   . THR A 1 346 ? 116.019 122.470 84.476  1.00 9.08   ? 346 THR A C   1 
ATOM   1707 O  O   . THR A 1 346 ? 117.039 121.826 84.707  1.00 9.08   ? 346 THR A O   1 
ATOM   1708 C  CB  . THR A 1 346 ? 114.938 123.121 86.585  1.00 9.08   ? 346 THR A CB  1 
ATOM   1709 O  OG1 . THR A 1 346 ? 116.284 123.018 87.042  1.00 9.08   ? 346 THR A OG1 1 
ATOM   1710 C  CG2 . THR A 1 346 ? 114.004 122.623 87.634  1.00 9.08   ? 346 THR A CG2 1 
ATOM   1711 N  N   . VAL A 1 347 ? 115.912 123.360 83.496  1.00 9.55   ? 347 VAL A N   1 
ATOM   1712 C  CA  . VAL A 1 347 ? 117.044 123.818 82.699  1.00 9.55   ? 347 VAL A CA  1 
ATOM   1713 C  C   . VAL A 1 347 ? 118.211 124.060 83.634  1.00 9.55   ? 347 VAL A C   1 
ATOM   1714 O  O   . VAL A 1 347 ? 118.009 124.608 84.725  1.00 9.55   ? 347 VAL A O   1 
ATOM   1715 C  CB  . VAL A 1 347 ? 116.676 125.099 81.949  1.00 9.55   ? 347 VAL A CB  1 
ATOM   1716 C  CG1 . VAL A 1 347 ? 117.883 125.832 81.523  1.00 9.55   ? 347 VAL A CG1 1 
ATOM   1717 C  CG2 . VAL A 1 347 ? 115.857 124.771 80.776  1.00 9.55   ? 347 VAL A CG2 1 
ATOM   1718 N  N   . PRO A 1 348 ? 119.413 123.667 83.292  1.00 13.79  ? 348 PRO A N   1 
ATOM   1719 C  CA  . PRO A 1 348 ? 120.555 123.916 84.176  1.00 13.79  ? 348 PRO A CA  1 
ATOM   1720 C  C   . PRO A 1 348 ? 120.796 125.395 84.388  1.00 13.79  ? 348 PRO A C   1 
ATOM   1721 O  O   . PRO A 1 348 ? 120.009 126.218 83.925  1.00 13.79  ? 348 PRO A O   1 
ATOM   1722 C  CB  . PRO A 1 348 ? 121.715 123.273 83.427  1.00 13.79  ? 348 PRO A CB  1 
ATOM   1723 C  CG  . PRO A 1 348 ? 121.088 122.353 82.492  1.00 13.79  ? 348 PRO A CG  1 
ATOM   1724 C  CD  . PRO A 1 348 ? 119.805 122.933 82.096  1.00 13.79  ? 348 PRO A CD  1 
ATOM   1725 N  N   . LYS A 1 349 ? 121.844 125.778 85.086  1.00 20.40  ? 349 LYS A N   1 
ATOM   1726 C  CA  . LYS A 1 349 ? 122.069 127.204 85.218  1.00 20.40  ? 349 LYS A CA  1 
ATOM   1727 C  C   . LYS A 1 349 ? 122.848 127.791 84.049  1.00 20.40  ? 349 LYS A C   1 
ATOM   1728 O  O   . LYS A 1 349 ? 122.913 129.014 83.916  1.00 20.40  ? 349 LYS A O   1 
ATOM   1729 C  CB  . LYS A 1 349 ? 122.787 127.510 86.527  1.00 20.40  ? 349 LYS A CB  1 
ATOM   1730 C  CG  . LYS A 1 349 ? 122.322 128.799 87.166  1.00 20.40  ? 349 LYS A CG  1 
ATOM   1731 C  CD  . LYS A 1 349 ? 123.308 129.327 88.169  1.00 20.40  ? 349 LYS A CD  1 
ATOM   1732 C  CE  . LYS A 1 349 ? 122.784 130.610 88.767  1.00 20.40  ? 349 LYS A CE  1 
ATOM   1733 N  NZ  . LYS A 1 349 ? 123.779 131.234 89.679  1.00 20.40  ? 349 LYS A NZ  1 
ATOM   1734 N  N   . GLN A 1 350 ? 123.414 126.963 83.181  1.00 21.44  ? 350 GLN A N   1 
ATOM   1735 C  CA  . GLN A 1 350 ? 124.323 127.456 82.165  1.00 21.44  ? 350 GLN A CA  1 
ATOM   1736 C  C   . GLN A 1 350 ? 123.769 127.458 80.749  1.00 21.44  ? 350 GLN A C   1 
ATOM   1737 O  O   . GLN A 1 350 ? 124.556 127.620 79.816  1.00 21.44  ? 350 GLN A O   1 
ATOM   1738 C  CB  . GLN A 1 350 ? 125.622 126.634 82.165  1.00 21.44  ? 350 GLN A CB  1 
ATOM   1739 C  CG  . GLN A 1 350 ? 125.446 125.163 81.841  1.00 21.44  ? 350 GLN A CG  1 
ATOM   1740 C  CD  . GLN A 1 350 ? 125.609 124.272 83.052  1.00 21.44  ? 350 GLN A CD  1 
ATOM   1741 O  OE1 . GLN A 1 350 ? 125.536 124.736 84.185  1.00 21.44  ? 350 GLN A OE1 1 
ATOM   1742 N  NE2 . GLN A 1 350 ? 125.828 122.983 82.818  1.00 21.44  ? 350 GLN A NE2 1 
ATOM   1743 N  N   . ILE A 1 351 ? 122.468 127.260 80.550  1.00 17.26  ? 351 ILE A N   1 
ATOM   1744 C  CA  . ILE A 1 351 ? 121.876 127.189 79.217  1.00 17.26  ? 351 ILE A CA  1 
ATOM   1745 C  C   . ILE A 1 351 ? 120.659 128.089 79.171  1.00 17.26  ? 351 ILE A C   1 
ATOM   1746 O  O   . ILE A 1 351 ? 119.658 127.810 79.836  1.00 17.26  ? 351 ILE A O   1 
ATOM   1747 C  CB  . ILE A 1 351 ? 121.458 125.763 78.873  1.00 17.26  ? 351 ILE A CB  1 
ATOM   1748 C  CG1 . ILE A 1 351 ? 122.592 124.814 79.111  1.00 17.26  ? 351 ILE A CG1 1 
ATOM   1749 C  CG2 . ILE A 1 351 ? 121.088 125.688 77.461  1.00 17.26  ? 351 ILE A CG2 1 
ATOM   1750 C  CD1 . ILE A 1 351 ? 122.104 123.438 79.227  1.00 17.26  ? 351 ILE A CD1 1 
ATOM   1751 N  N   . ASP A 1 352 ? 120.700 129.131 78.356  1.00 25.33  ? 352 ASP A N   1 
ATOM   1752 C  CA  . ASP A 1 352 ? 119.611 130.106 78.311  1.00 25.33  ? 352 ASP A CA  1 
ATOM   1753 C  C   . ASP A 1 352 ? 118.704 129.771 77.133  1.00 25.33  ? 352 ASP A C   1 
ATOM   1754 O  O   . ASP A 1 352 ? 119.128 129.839 75.979  1.00 25.33  ? 352 ASP A O   1 
ATOM   1755 C  CB  . ASP A 1 352 ? 120.163 131.521 78.211  1.00 25.33  ? 352 ASP A CB  1 
ATOM   1756 C  CG  . ASP A 1 352 ? 119.287 132.527 78.910  1.00 25.33  ? 352 ASP A CG  1 
ATOM   1757 O  OD1 . ASP A 1 352 ? 118.232 132.122 79.439  1.00 25.33  ? 352 ASP A OD1 1 
ATOM   1758 O  OD2 . ASP A 1 352 ? 119.645 133.722 78.930  1.00 25.33  ? 352 ASP A OD2 1 
ATOM   1759 N  N   . ILE A 1 353 ? 117.444 129.432 77.417  1.00 15.40  ? 353 ILE A N   1 
ATOM   1760 C  CA  . ILE A 1 353 ? 116.590 128.889 76.368  1.00 15.40  ? 353 ILE A CA  1 
ATOM   1761 C  C   . ILE A 1 353 ? 116.393 129.883 75.237  1.00 15.40  ? 353 ILE A C   1 
ATOM   1762 O  O   . ILE A 1 353 ? 116.494 129.514 74.062  1.00 15.40  ? 353 ILE A O   1 
ATOM   1763 C  CB  . ILE A 1 353 ? 115.251 128.430 76.948  1.00 15.40  ? 353 ILE A CB  1 
ATOM   1764 C  CG1 . ILE A 1 353 ? 115.418 127.093 77.615  1.00 15.40  ? 353 ILE A CG1 1 
ATOM   1765 C  CG2 . ILE A 1 353 ? 114.265 128.244 75.866  1.00 15.40  ? 353 ILE A CG2 1 
ATOM   1766 C  CD1 . ILE A 1 353 ? 115.862 126.094 76.671  1.00 15.40  ? 353 ILE A CD1 1 
ATOM   1767 N  N   . ARG A 1 354 ? 116.141 131.153 75.547  1.00 20.26  ? 354 ARG A N   1 
ATOM   1768 C  CA  . ARG A 1 354 ? 115.895 132.115 74.475  1.00 20.26  ? 354 ARG A CA  1 
ATOM   1769 C  C   . ARG A 1 354 ? 117.055 132.170 73.496  1.00 20.26  ? 354 ARG A C   1 
ATOM   1770 O  O   . ARG A 1 354 ? 116.852 132.359 72.292  1.00 20.26  ? 354 ARG A O   1 
ATOM   1771 C  CB  . ARG A 1 354 ? 115.634 133.504 75.038  1.00 20.26  ? 354 ARG A CB  1 
ATOM   1772 N  N   . ASN A 1 355 ? 118.276 131.997 73.980  1.00 25.27  ? 355 ASN A N   1 
ATOM   1773 C  CA  . ASN A 1 355 ? 119.401 132.001 73.063  1.00 25.27  ? 355 ASN A CA  1 
ATOM   1774 C  C   . ASN A 1 355 ? 119.382 130.782 72.152  1.00 25.27  ? 355 ASN A C   1 
ATOM   1775 O  O   . ASN A 1 355 ? 119.647 130.900 70.951  1.00 25.27  ? 355 ASN A O   1 
ATOM   1776 C  CB  . ASN A 1 355 ? 120.695 132.086 73.844  1.00 25.27  ? 355 ASN A CB  1 
ATOM   1777 C  CG  . ASN A 1 355 ? 120.760 133.324 74.685  1.00 25.27  ? 355 ASN A CG  1 
ATOM   1778 O  OD1 . ASN A 1 355 ? 120.002 134.263 74.468  1.00 25.27  ? 355 ASN A OD1 1 
ATOM   1779 N  ND2 . ASN A 1 355 ? 121.658 133.339 75.657  1.00 25.27  ? 355 ASN A ND2 1 
ATOM   1780 N  N   . LEU A 1 356 ? 119.056 129.607 72.689  1.00 20.14  ? 356 LEU A N   1 
ATOM   1781 C  CA  . LEU A 1 356 ? 118.959 128.425 71.841  1.00 20.14  ? 356 LEU A CA  1 
ATOM   1782 C  C   . LEU A 1 356 ? 117.908 128.605 70.758  1.00 20.14  ? 356 LEU A C   1 
ATOM   1783 O  O   . LEU A 1 356 ? 118.118 128.200 69.614  1.00 20.14  ? 356 LEU A O   1 
ATOM   1784 C  CB  . LEU A 1 356 ? 118.625 127.197 72.670  1.00 20.14  ? 356 LEU A CB  1 
ATOM   1785 C  CG  . LEU A 1 356 ? 119.742 126.416 73.312  1.00 20.14  ? 356 LEU A CG  1 
ATOM   1786 C  CD1 . LEU A 1 356 ? 119.191 125.079 73.701  1.00 20.14  ? 356 LEU A CD1 1 
ATOM   1787 C  CD2 . LEU A 1 356 ? 120.860 126.275 72.348  1.00 20.14  ? 356 LEU A CD2 1 
ATOM   1788 N  N   . ILE A 1 357 ? 116.760 129.193 71.100  1.00 18.41  ? 357 ILE A N   1 
ATOM   1789 C  CA  . ILE A 1 357 ? 115.696 129.331 70.110  1.00 18.41  ? 357 ILE A CA  1 
ATOM   1790 C  C   . ILE A 1 357 ? 116.070 130.359 69.049  1.00 18.41  ? 357 ILE A C   1 
ATOM   1791 O  O   . ILE A 1 357 ? 115.847 130.145 67.851  1.00 18.41  ? 357 ILE A O   1 
ATOM   1792 C  CB  . ILE A 1 357 ? 114.372 129.689 70.787  1.00 18.41  ? 357 ILE A CB  1 
ATOM   1793 C  CG1 . ILE A 1 357 ? 113.759 128.460 71.410  1.00 18.41  ? 357 ILE A CG1 1 
ATOM   1794 C  CG2 . ILE A 1 357 ? 113.428 130.224 69.770  1.00 18.41  ? 357 ILE A CG2 1 
ATOM   1795 C  CD1 . ILE A 1 357 ? 113.160 127.575 70.422  1.00 18.41  ? 357 ILE A CD1 1 
ATOM   1796 N  N   . LYS A 1 358 ? 116.628 131.495 69.457  1.00 28.03  ? 358 LYS A N   1 
ATOM   1797 C  CA  . LYS A 1 358 ? 117.093 132.461 68.469  1.00 28.03  ? 358 LYS A CA  1 
ATOM   1798 C  C   . LYS A 1 358 ? 118.135 131.843 67.546  1.00 28.03  ? 358 LYS A C   1 
ATOM   1799 O  O   . LYS A 1 358 ? 118.123 132.079 66.331  1.00 28.03  ? 358 LYS A O   1 
ATOM   1800 C  CB  . LYS A 1 358 ? 117.648 133.688 69.180  1.00 28.03  ? 358 LYS A CB  1 
ATOM   1801 C  CG  . LYS A 1 358 ? 118.304 134.713 68.294  1.00 28.03  ? 358 LYS A CG  1 
ATOM   1802 C  CD  . LYS A 1 358 ? 118.618 135.964 69.101  1.00 28.03  ? 358 LYS A CD  1 
ATOM   1803 C  CE  . LYS A 1 358 ? 119.607 135.670 70.219  1.00 28.03  ? 358 LYS A CE  1 
ATOM   1804 N  NZ  . LYS A 1 358 ? 120.959 135.309 69.715  1.00 28.03  ? 358 LYS A NZ  1 
ATOM   1805 N  N   . GLU A 1 359 ? 119.021 131.019 68.092  1.00 28.69  ? 359 GLU A N   1 
ATOM   1806 C  CA  . GLU A 1 359 ? 120.050 130.412 67.266  1.00 28.69  ? 359 GLU A CA  1 
ATOM   1807 C  C   . GLU A 1 359 ? 119.530 129.281 66.384  1.00 28.69  ? 359 GLU A C   1 
ATOM   1808 O  O   . GLU A 1 359 ? 120.073 129.068 65.297  1.00 28.69  ? 359 GLU A O   1 
ATOM   1809 C  CB  . GLU A 1 359 ? 121.192 129.916 68.148  1.00 28.69  ? 359 GLU A CB  1 
ATOM   1810 C  CG  . GLU A 1 359 ? 121.994 131.038 68.782  1.00 28.69  ? 359 GLU A CG  1 
ATOM   1811 C  CD  . GLU A 1 359 ? 123.282 130.556 69.428  1.00 28.69  ? 359 GLU A CD  1 
ATOM   1812 O  OE1 . GLU A 1 359 ? 123.655 129.384 69.231  1.00 28.69  ? 359 GLU A OE1 1 
ATOM   1813 O  OE2 . GLU A 1 359 ? 123.928 131.355 70.133  1.00 28.69  ? 359 GLU A OE2 1 
ATOM   1814 N  N   . LEU A 1 360 ? 118.503 128.542 66.810  1.00 25.92  ? 360 LEU A N   1 
ATOM   1815 C  CA  . LEU A 1 360 ? 117.912 127.544 65.921  1.00 25.92  ? 360 LEU A CA  1 
ATOM   1816 C  C   . LEU A 1 360 ? 117.147 128.202 64.789  1.00 25.92  ? 360 LEU A C   1 
ATOM   1817 O  O   . LEU A 1 360 ? 117.132 127.694 63.668  1.00 25.92  ? 360 LEU A O   1 
ATOM   1818 C  CB  . LEU A 1 360 ? 116.974 126.608 66.671  1.00 25.92  ? 360 LEU A CB  1 
ATOM   1819 C  CG  . LEU A 1 360 ? 117.563 125.552 67.574  1.00 25.92  ? 360 LEU A CG  1 
ATOM   1820 C  CD1 . LEU A 1 360 ? 116.466 124.628 68.010  1.00 25.92  ? 360 LEU A CD1 1 
ATOM   1821 C  CD2 . LEU A 1 360 ? 118.586 124.824 66.815  1.00 25.92  ? 360 LEU A CD2 1 
ATOM   1822 N  N   . ARG A 1 361 ? 116.480 129.316 65.058  1.00 29.55  ? 361 ARG A N   1 
ATOM   1823 C  CA  . ARG A 1 361 ? 115.783 129.983 63.971  1.00 29.55  ? 361 ARG A CA  1 
ATOM   1824 C  C   . ARG A 1 361 ? 116.726 130.699 63.018  1.00 29.55  ? 361 ARG A C   1 
ATOM   1825 O  O   . ARG A 1 361 ? 116.381 130.866 61.846  1.00 29.55  ? 361 ARG A O   1 
ATOM   1826 C  CB  . ARG A 1 361 ? 114.777 130.973 64.532  1.00 29.55  ? 361 ARG A CB  1 
ATOM   1827 C  CG  . ARG A 1 361 ? 113.508 130.319 64.986  1.00 29.55  ? 361 ARG A CG  1 
ATOM   1828 C  CD  . ARG A 1 361 ? 112.719 131.209 65.899  1.00 29.55  ? 361 ARG A CD  1 
ATOM   1829 N  NE  . ARG A 1 361 ? 111.419 130.628 66.165  1.00 29.55  ? 361 ARG A NE  1 
ATOM   1830 C  CZ  . ARG A 1 361 ? 110.701 130.906 67.237  1.00 29.55  ? 361 ARG A CZ  1 
ATOM   1831 N  NH1 . ARG A 1 361 ? 111.171 131.758 68.129  1.00 29.55  ? 361 ARG A NH1 1 
ATOM   1832 N  NH2 . ARG A 1 361 ? 109.521 130.333 67.417  1.00 29.55  ? 361 ARG A NH2 1 
ATOM   1833 N  N   . ASN A 1 362 ? 117.897 131.135 63.485  1.00 32.98  ? 362 ASN A N   1 
ATOM   1834 C  CA  . ASN A 1 362 ? 118.862 131.749 62.579  1.00 32.98  ? 362 ASN A CA  1 
ATOM   1835 C  C   . ASN A 1 362 ? 119.384 130.783 61.528  1.00 32.98  ? 362 ASN A C   1 
ATOM   1836 O  O   . ASN A 1 362 ? 119.747 131.221 60.432  1.00 32.98  ? 362 ASN A O   1 
ATOM   1837 C  CB  . ASN A 1 362 ? 120.042 132.315 63.367  1.00 32.98  ? 362 ASN A CB  1 
ATOM   1838 C  CG  . ASN A 1 362 ? 119.862 133.766 63.699  1.00 32.98  ? 362 ASN A CG  1 
ATOM   1839 O  OD1 . ASN A 1 362 ? 119.479 134.556 62.845  1.00 32.98  ? 362 ASN A OD1 1 
ATOM   1840 N  ND2 . ASN A 1 362 ? 120.125 134.131 64.944  1.00 32.98  ? 362 ASN A ND2 1 
ATOM   1841 N  N   . VAL A 1 363 ? 119.427 129.486 61.839  1.00 31.95  ? 363 VAL A N   1 
ATOM   1842 C  CA  . VAL A 1 363 ? 119.999 128.493 60.941  1.00 31.95  ? 363 VAL A CA  1 
ATOM   1843 C  C   . VAL A 1 363 ? 119.208 128.454 59.646  1.00 31.95  ? 363 VAL A C   1 
ATOM   1844 O  O   . VAL A 1 363 ? 118.009 128.748 59.613  1.00 31.95  ? 363 VAL A O   1 
ATOM   1845 C  CB  . VAL A 1 363 ? 120.015 127.119 61.631  1.00 31.95  ? 363 VAL A CB  1 
ATOM   1846 C  CG1 . VAL A 1 363 ? 120.511 126.044 60.711  1.00 31.95  ? 363 VAL A CG1 1 
ATOM   1847 C  CG2 . VAL A 1 363 ? 120.880 127.182 62.848  1.00 31.95  ? 363 VAL A CG2 1 
ATOM   1848 N  N   . GLU A 1 364 ? 119.884 128.110 58.563  1.00 40.64  ? 364 GLU A N   1 
ATOM   1849 C  CA  . GLU A 1 364 ? 119.176 128.016 57.305  1.00 40.64  ? 364 GLU A CA  1 
ATOM   1850 C  C   . GLU A 1 364 ? 118.191 126.848 57.337  1.00 40.64  ? 364 GLU A C   1 
ATOM   1851 O  O   . GLU A 1 364 ? 118.131 126.067 58.288  1.00 40.64  ? 364 GLU A O   1 
ATOM   1852 C  CB  . GLU A 1 364 ? 120.162 127.861 56.155  1.00 40.64  ? 364 GLU A CB  1 
ATOM   1853 C  CG  . GLU A 1 364 ? 119.742 128.572 54.897  1.00 40.64  ? 364 GLU A CG  1 
ATOM   1854 C  CD  . GLU A 1 364 ? 120.760 128.446 53.789  1.00 40.64  ? 364 GLU A CD  1 
ATOM   1855 O  OE1 . GLU A 1 364 ? 121.650 127.577 53.892  1.00 40.64  ? 364 GLU A OE1 1 
ATOM   1856 O  OE2 . GLU A 1 364 ? 120.646 129.175 52.787  1.00 40.64  ? 364 GLU A OE2 1 
ATOM   1857 N  N   . GLY A 1 365 ? 117.367 126.772 56.299  1.00 44.70  ? 365 GLY A N   1 
ATOM   1858 C  CA  . GLY A 1 365 ? 116.514 125.629 56.068  1.00 44.70  ? 365 GLY A CA  1 
ATOM   1859 C  C   . GLY A 1 365 ? 115.374 125.421 57.039  1.00 44.70  ? 365 GLY A C   1 
ATOM   1860 O  O   . GLY A 1 365 ? 114.489 124.614 56.744  1.00 44.70  ? 365 GLY A O   1 
ATOM   1861 N  N   . VAL A 1 366 ? 115.343 126.112 58.175  1.00 43.79  ? 366 VAL A N   1 
ATOM   1862 C  CA  . VAL A 1 366 ? 114.282 125.904 59.152  1.00 43.79  ? 366 VAL A CA  1 
ATOM   1863 C  C   . VAL A 1 366 ? 113.495 127.197 59.294  1.00 43.79  ? 366 VAL A C   1 
ATOM   1864 O  O   . VAL A 1 366 ? 113.970 128.278 58.937  1.00 43.79  ? 366 VAL A O   1 
ATOM   1865 C  CB  . VAL A 1 366 ? 114.826 125.453 60.520  1.00 43.79  ? 366 VAL A CB  1 
ATOM   1866 C  CG1 . VAL A 1 366 ? 115.909 124.424 60.342  1.00 43.79  ? 366 VAL A CG1 1 
ATOM   1867 C  CG2 . VAL A 1 366 ? 115.307 126.625 61.300  1.00 43.79  ? 366 VAL A CG2 1 
ATOM   1868 N  N   . GLU A 1 367 ? 112.273 127.081 59.801  1.00 45.69  ? 367 GLU A N   1 
ATOM   1869 C  CA  . GLU A 1 367 ? 111.407 128.237 59.972  1.00 45.69  ? 367 GLU A CA  1 
ATOM   1870 C  C   . GLU A 1 367 ? 110.708 128.304 61.315  1.00 45.69  ? 367 GLU A C   1 
ATOM   1871 O  O   . GLU A 1 367 ? 110.329 129.404 61.727  1.00 45.69  ? 367 GLU A O   1 
ATOM   1872 C  CB  . GLU A 1 367 ? 110.347 128.270 58.867  1.00 45.69  ? 367 GLU A CB  1 
ATOM   1873 C  CG  . GLU A 1 367 ? 109.655 126.947 58.677  1.00 45.69  ? 367 GLU A CG  1 
ATOM   1874 C  CD  . GLU A 1 367 ? 109.149 126.759 57.268  1.00 45.69  ? 367 GLU A CD  1 
ATOM   1875 O  OE1 . GLU A 1 367 ? 107.932 126.548 57.095  1.00 45.69  ? 367 GLU A OE1 1 
ATOM   1876 O  OE2 . GLU A 1 367 ? 109.971 126.828 56.332  1.00 45.69  ? 367 GLU A OE2 1 
ATOM   1877 N  N   . GLU A 1 368 ? 110.522 127.187 62.005  1.00 33.96  ? 368 GLU A N   1 
ATOM   1878 C  CA  . GLU A 1 368 ? 109.807 127.152 63.265  1.00 33.96  ? 368 GLU A CA  1 
ATOM   1879 C  C   . GLU A 1 368 ? 110.394 126.064 64.140  1.00 33.96  ? 368 GLU A C   1 
ATOM   1880 O  O   . GLU A 1 368 ? 110.842 125.036 63.646  1.00 33.96  ? 368 GLU A O   1 
ATOM   1881 C  CB  . GLU A 1 368 ? 108.333 126.871 63.047  1.00 33.96  ? 368 GLU A CB  1 
ATOM   1882 C  CG  . GLU A 1 368 ? 107.537 126.949 64.305  1.00 33.96  ? 368 GLU A CG  1 
ATOM   1883 C  CD  . GLU A 1 368 ? 106.070 126.724 64.083  1.00 33.96  ? 368 GLU A CD  1 
ATOM   1884 O  OE1 . GLU A 1 368 ? 105.674 126.393 62.946  1.00 33.96  ? 368 GLU A OE1 1 
ATOM   1885 O  OE2 . GLU A 1 368 ? 105.311 126.905 65.052  1.00 33.96  ? 368 GLU A OE2 1 
ATOM   1886 N  N   . VAL A 1 369 ? 110.380 126.277 65.450  1.00 19.49  ? 369 VAL A N   1 
ATOM   1887 C  CA  . VAL A 1 369 ? 110.904 125.290 66.383  1.00 19.49  ? 369 VAL A CA  1 
ATOM   1888 C  C   . VAL A 1 369 ? 109.887 125.081 67.499  1.00 19.49  ? 369 VAL A C   1 
ATOM   1889 O  O   . VAL A 1 369 ? 109.825 125.877 68.438  1.00 19.49  ? 369 VAL A O   1 
ATOM   1890 C  CB  . VAL A 1 369 ? 112.253 125.713 66.956  1.00 19.49  ? 369 VAL A CB  1 
ATOM   1891 C  CG1 . VAL A 1 369 ? 112.810 124.617 67.756  1.00 19.49  ? 369 VAL A CG1 1 
ATOM   1892 C  CG2 . VAL A 1 369 ? 113.194 126.074 65.845  1.00 19.49  ? 369 VAL A CG2 1 
ATOM   1893 N  N   . HIS A 1 370 ? 109.234 123.932 67.365  1.00 21.79  ? 370 HIS A N   1 
ATOM   1894 C  CA  . HIS A 1 370 ? 108.168 123.415 68.256  1.00 21.79  ? 370 HIS A CA  1 
ATOM   1895 C  C   . HIS A 1 370 ? 108.805 122.861 69.529  1.00 21.79  ? 370 HIS A C   1 
ATOM   1896 O  O   . HIS A 1 370 ? 110.036 122.941 69.675  1.00 21.79  ? 370 HIS A O   1 
ATOM   1897 C  CB  . HIS A 1 370 ? 107.302 122.371 67.540  1.00 21.79  ? 370 HIS A CB  1 
ATOM   1898 C  CG  . HIS A 1 370 ? 106.760 122.834 66.231  1.00 21.79  ? 370 HIS A CG  1 
ATOM   1899 N  ND1 . HIS A 1 370 ? 106.685 122.004 65.131  1.00 21.79  ? 370 HIS A ND1 1 
ATOM   1900 C  CD2 . HIS A 1 370 ? 106.283 124.033 65.837  1.00 21.79  ? 370 HIS A CD2 1 
ATOM   1901 C  CE1 . HIS A 1 370 ? 106.176 122.671 64.115  1.00 21.79  ? 370 HIS A CE1 1 
ATOM   1902 N  NE2 . HIS A 1 370 ? 105.922 123.919 64.522  1.00 21.79  ? 370 HIS A NE2 1 
ATOM   1903 N  N   . GLU A 1 371 ? 107.972 122.346 70.405  1.00 15.46  ? 371 GLU A N   1 
ATOM   1904 C  CA  . GLU A 1 371 ? 108.375 121.912 71.732  1.00 15.46  ? 371 GLU A CA  1 
ATOM   1905 C  C   . GLU A 1 371 ? 109.876 121.787 71.832  1.00 15.46  ? 371 GLU A C   1 
ATOM   1906 O  O   . GLU A 1 371 ? 110.485 121.015 71.099  1.00 15.46  ? 371 GLU A O   1 
ATOM   1907 C  CB  . GLU A 1 371 ? 107.753 120.553 72.037  1.00 15.46  ? 371 GLU A CB  1 
ATOM   1908 C  CG  . GLU A 1 371 ? 106.259 120.523 72.138  1.00 15.46  ? 371 GLU A CG  1 
ATOM   1909 C  CD  . GLU A 1 371 ? 105.755 119.356 72.975  1.00 15.46  ? 371 GLU A CD  1 
ATOM   1910 O  OE1 . GLU A 1 371 ? 106.403 119.001 73.985  1.00 15.46  ? 371 GLU A OE1 1 
ATOM   1911 O  OE2 . GLU A 1 371 ? 104.707 118.788 72.618  1.00 15.46  ? 371 GLU A OE2 1 
ATOM   1912 N  N   . LEU A 1 372 ? 110.476 122.546 72.744  1.00 7.80   ? 372 LEU A N   1 
ATOM   1913 C  CA  . LEU A 1 372 ? 111.923 122.587 72.935  1.00 7.80   ? 372 LEU A CA  1 
ATOM   1914 C  C   . LEU A 1 372 ? 112.193 122.255 74.383  1.00 7.80   ? 372 LEU A C   1 
ATOM   1915 O  O   . LEU A 1 372 ? 112.278 123.167 75.194  1.00 7.80   ? 372 LEU A O   1 
ATOM   1916 C  CB  . LEU A 1 372 ? 112.490 123.932 72.614  1.00 7.80   ? 372 LEU A CB  1 
ATOM   1917 C  CG  . LEU A 1 372 ? 113.991 123.907 72.777  1.00 7.80   ? 372 LEU A CG  1 
ATOM   1918 C  CD1 . LEU A 1 372 ? 114.549 123.060 71.728  1.00 7.80   ? 372 LEU A CD1 1 
ATOM   1919 C  CD2 . LEU A 1 372 ? 114.532 125.245 72.637  1.00 7.80   ? 372 LEU A CD2 1 
ATOM   1920 N  N   . HIS A 1 373 ? 112.340 120.988 74.714  1.00 7.62   ? 373 HIS A N   1 
ATOM   1921 C  CA  . HIS A 1 373 ? 112.583 120.582 76.086  1.00 7.62   ? 373 HIS A CA  1 
ATOM   1922 C  C   . HIS A 1 373 ? 114.077 120.407 76.297  1.00 7.62   ? 373 HIS A C   1 
ATOM   1923 O  O   . HIS A 1 373 ? 114.742 119.772 75.483  1.00 7.62   ? 373 HIS A O   1 
ATOM   1924 C  CB  . HIS A 1 373 ? 111.825 119.302 76.396  1.00 7.62   ? 373 HIS A CB  1 
ATOM   1925 C  CG  . HIS A 1 373 ? 110.349 119.436 76.237  1.00 7.62   ? 373 HIS A CG  1 
ATOM   1926 N  ND1 . HIS A 1 373 ? 109.636 120.467 76.800  1.00 7.62   ? 373 HIS A ND1 1 
ATOM   1927 C  CD2 . HIS A 1 373 ? 109.450 118.680 75.568  1.00 7.62   ? 373 HIS A CD2 1 
ATOM   1928 C  CE1 . HIS A 1 373 ? 108.359 120.339 76.493  1.00 7.62   ? 373 HIS A CE1 1 
ATOM   1929 N  NE2 . HIS A 1 373 ? 108.219 119.261 75.745  1.00 7.62   ? 373 HIS A NE2 1 
ATOM   1930 N  N   . VAL A 1 374 ? 114.609 121.001 77.359  1.00 6.97   ? 374 VAL A N   1 
ATOM   1931 C  CA  . VAL A 1 374 ? 116.000 120.845 77.766  1.00 6.97   ? 374 VAL A CA  1 
ATOM   1932 C  C   . VAL A 1 374 ? 115.995 120.490 79.241  1.00 6.97   ? 374 VAL A C   1 
ATOM   1933 O  O   . VAL A 1 374 ? 115.165 121.005 79.987  1.00 6.97   ? 374 VAL A O   1 
ATOM   1934 C  CB  . VAL A 1 374 ? 116.809 122.127 77.515  1.00 6.97   ? 374 VAL A CB  1 
ATOM   1935 C  CG1 . VAL A 1 374 ? 118.178 121.976 78.023  1.00 6.97   ? 374 VAL A CG1 1 
ATOM   1936 C  CG2 . VAL A 1 374 ? 116.883 122.421 76.072  1.00 6.97   ? 374 VAL A CG2 1 
ATOM   1937 N  N   . TRP A 1 375 ? 116.885 119.603 79.669  1.00 12.18  ? 375 TRP A N   1 
ATOM   1938 C  CA  . TRP A 1 375 ? 116.921 119.309 81.092  1.00 12.18  ? 375 TRP A CA  1 
ATOM   1939 C  C   . TRP A 1 375 ? 118.270 118.754 81.501  1.00 12.18  ? 375 TRP A C   1 
ATOM   1940 O  O   . TRP A 1 375 ? 119.229 118.859 80.745  1.00 12.18  ? 375 TRP A O   1 
ATOM   1941 C  CB  . TRP A 1 375 ? 115.814 118.359 81.497  1.00 12.18  ? 375 TRP A CB  1 
ATOM   1942 C  CG  . TRP A 1 375 ? 115.561 117.268 80.604  1.00 12.18  ? 375 TRP A CG  1 
ATOM   1943 C  CD1 . TRP A 1 375 ? 114.993 117.333 79.389  1.00 12.18  ? 375 TRP A CD1 1 
ATOM   1944 C  CD2 . TRP A 1 375 ? 115.772 115.899 80.878  1.00 12.18  ? 375 TRP A CD2 1 
ATOM   1945 N  NE1 . TRP A 1 375 ? 114.870 116.084 78.861  1.00 12.18  ? 375 TRP A NE1 1 
ATOM   1946 C  CE2 . TRP A 1 375 ? 115.349 115.186 79.772  1.00 12.18  ? 375 TRP A CE2 1 
ATOM   1947 C  CE3 . TRP A 1 375 ? 116.293 115.207 81.953  1.00 12.18  ? 375 TRP A CE3 1 
ATOM   1948 C  CZ2 . TRP A 1 375 ? 115.443 113.827 79.706  1.00 12.18  ? 375 TRP A CZ2 1 
ATOM   1949 C  CZ3 . TRP A 1 375 ? 116.377 113.864 81.881  1.00 12.18  ? 375 TRP A CZ3 1 
ATOM   1950 C  CH2 . TRP A 1 375 ? 115.966 113.186 80.776  1.00 12.18  ? 375 TRP A CH2 1 
ATOM   1951 N  N   . GLN A 1 376 ? 118.360 118.240 82.724  1.00 12.20  ? 376 GLN A N   1 
ATOM   1952 C  CA  . GLN A 1 376 ? 119.634 117.761 83.245  1.00 12.20  ? 376 GLN A CA  1 
ATOM   1953 C  C   . GLN A 1 376 ? 119.480 116.366 83.802  1.00 12.20  ? 376 GLN A C   1 
ATOM   1954 O  O   . GLN A 1 376 ? 118.699 116.157 84.726  1.00 12.20  ? 376 GLN A O   1 
ATOM   1955 C  CB  . GLN A 1 376 ? 120.139 118.691 84.332  1.00 12.20  ? 376 GLN A CB  1 
ATOM   1956 C  CG  . GLN A 1 376 ? 121.541 118.398 84.783  1.00 12.20  ? 376 GLN A CG  1 
ATOM   1957 C  CD  . GLN A 1 376 ? 122.085 119.447 85.721  1.00 12.20  ? 376 GLN A CD  1 
ATOM   1958 O  OE1 . GLN A 1 376 ? 121.341 120.217 86.310  1.00 12.20  ? 376 GLN A OE1 1 
ATOM   1959 N  NE2 . GLN A 1 376 ? 123.390 119.486 85.858  1.00 12.20  ? 376 GLN A NE2 1 
ATOM   1960 N  N   . LEU A 1 377 ? 120.231 115.407 83.273  1.00 2.07   ? 377 LEU A N   1 
ATOM   1961 C  CA  . LEU A 1 377 ? 120.075 114.045 83.765  1.00 2.07   ? 377 LEU A CA  1 
ATOM   1962 C  C   . LEU A 1 377 ? 120.782 113.876 85.094  1.00 2.07   ? 377 LEU A C   1 
ATOM   1963 O  O   . LEU A 1 377 ? 120.151 113.571 86.108  1.00 2.07   ? 377 LEU A O   1 
ATOM   1964 C  CB  . LEU A 1 377 ? 120.578 113.031 82.751  1.00 2.07   ? 377 LEU A CB  1 
ATOM   1965 C  CG  . LEU A 1 377 ? 120.597 111.592 83.248  1.00 2.07   ? 377 LEU A CG  1 
ATOM   1966 C  CD1 . LEU A 1 377 ? 119.374 111.235 83.985  1.00 2.07   ? 377 LEU A CD1 1 
ATOM   1967 C  CD2 . LEU A 1 377 ? 120.640 110.706 82.081  1.00 2.07   ? 377 LEU A CD2 1 
ATOM   1968 N  N   . ALA A 1 378 ? 122.091 114.063 85.110  1.00 10.92  ? 378 ALA A N   1 
ATOM   1969 C  CA  . ALA A 1 378 ? 122.850 114.136 86.345  1.00 10.92  ? 378 ALA A CA  1 
ATOM   1970 C  C   . ALA A 1 378 ? 124.169 114.778 86.014  1.00 10.92  ? 378 ALA A C   1 
ATOM   1971 O  O   . ALA A 1 378 ? 124.671 114.632 84.896  1.00 10.92  ? 378 ALA A O   1 
ATOM   1972 C  CB  . ALA A 1 378 ? 123.084 112.764 86.968  1.00 10.92  ? 378 ALA A CB  1 
ATOM   1973 N  N   . GLY A 1 379 ? 124.711 115.501 86.971  1.00 9.45   ? 379 GLY A N   1 
ATOM   1974 C  CA  . GLY A 1 379 ? 125.983 116.125 86.728  1.00 9.45   ? 379 GLY A CA  1 
ATOM   1975 C  C   . GLY A 1 379 ? 125.939 116.924 85.451  1.00 9.45   ? 379 GLY A C   1 
ATOM   1976 O  O   . GLY A 1 379 ? 125.277 117.958 85.377  1.00 9.45   ? 379 GLY A O   1 
ATOM   1977 N  N   . SER A 1 380 ? 126.605 116.433 84.424  1.00 6.35   ? 380 SER A N   1 
ATOM   1978 C  CA  . SER A 1 380 ? 126.694 117.203 83.203  1.00 6.35   ? 380 SER A CA  1 
ATOM   1979 C  C   . SER A 1 380 ? 126.338 116.380 81.982  1.00 6.35   ? 380 SER A C   1 
ATOM   1980 O  O   . SER A 1 380 ? 126.924 116.579 80.923  1.00 6.35   ? 380 SER A O   1 
ATOM   1981 C  CB  . SER A 1 380 ? 128.084 117.799 83.040  1.00 6.35   ? 380 SER A CB  1 
ATOM   1982 O  OG  . SER A 1 380 ? 128.297 118.178 81.697  1.00 6.35   ? 380 SER A OG  1 
ATOM   1983 N  N   . ARG A 1 381 ? 125.332 115.520 82.091  1.00 9.62   ? 381 ARG A N   1 
ATOM   1984 C  CA  . ARG A 1 381 ? 124.806 114.768 80.917  1.00 9.62   ? 381 ARG A CA  1 
ATOM   1985 C  C   . ARG A 1 381 ? 123.469 115.429 80.568  1.00 9.62   ? 381 ARG A C   1 
ATOM   1986 O  O   . ARG A 1 381 ? 122.435 114.911 81.018  1.00 9.62   ? 381 ARG A O   1 
ATOM   1987 C  CB  . ARG A 1 381 ? 124.589 113.293 81.263  1.00 9.62   ? 381 ARG A CB  1 
ATOM   1988 C  CG  . ARG A 1 381 ? 125.772 112.629 81.950  1.00 9.62   ? 381 ARG A CG  1 
ATOM   1989 C  CD  . ARG A 1 381 ? 125.362 111.400 82.736  1.00 9.62   ? 381 ARG A CD  1 
ATOM   1990 N  NE  . ARG A 1 381 ? 125.829 110.176 82.110  1.00 9.62   ? 381 ARG A NE  1 
ATOM   1991 C  CZ  . ARG A 1 381 ? 127.048 110.010 81.620  1.00 9.62   ? 381 ARG A CZ  1 
ATOM   1992 N  NH1 . ARG A 1 381 ? 127.378 108.873 81.033  1.00 9.62   ? 381 ARG A NH1 1 
ATOM   1993 N  NH2 . ARG A 1 381 ? 127.935 110.980 81.719  1.00 9.62   ? 381 ARG A NH2 1 
ATOM   1994 N  N   . ILE A 1 382 ? 123.484 116.507 79.791  1.00 6.71   ? 382 ILE A N   1 
ATOM   1995 C  CA  . ILE A 1 382 ? 122.290 117.299 79.525  1.00 6.71   ? 382 ILE A CA  1 
ATOM   1996 C  C   . ILE A 1 382 ? 121.663 116.836 78.223  1.00 6.71   ? 382 ILE A C   1 
ATOM   1997 O  O   . ILE A 1 382 ? 122.365 116.632 77.235  1.00 6.71   ? 382 ILE A O   1 
ATOM   1998 C  CB  . ILE A 1 382 ? 122.645 118.789 79.456  1.00 6.71   ? 382 ILE A CB  1 
ATOM   1999 C  CG1 . ILE A 1 382 ? 123.002 119.310 80.830  1.00 6.71   ? 382 ILE A CG1 1 
ATOM   2000 C  CG2 . ILE A 1 382 ? 121.530 119.561 78.895  1.00 6.71   ? 382 ILE A CG2 1 
ATOM   2001 C  CD1 . ILE A 1 382 ? 123.634 120.650 80.805  1.00 6.71   ? 382 ILE A CD1 1 
ATOM   2002 N  N   . ILE A 1 383 ? 120.349 116.675 78.214  1.00 4.76   ? 383 ILE A N   1 
ATOM   2003 C  CA  . ILE A 1 383 ? 119.618 116.163 77.066  1.00 4.76   ? 383 ILE A CA  1 
ATOM   2004 C  C   . ILE A 1 383 ? 118.899 117.321 76.404  1.00 4.76   ? 383 ILE A C   1 
ATOM   2005 O  O   . ILE A 1 383 ? 118.950 118.436 76.918  1.00 4.76   ? 383 ILE A O   1 
ATOM   2006 C  CB  . ILE A 1 383 ? 118.652 115.067 77.514  1.00 4.76   ? 383 ILE A CB  1 
ATOM   2007 C  CG1 . ILE A 1 383 ? 119.411 114.136 78.424  1.00 4.76   ? 383 ILE A CG1 1 
ATOM   2008 C  CG2 . ILE A 1 383 ? 118.142 114.293 76.367  1.00 4.76   ? 383 ILE A CG2 1 
ATOM   2009 C  CD1 . ILE A 1 383 ? 118.736 112.855 78.645  1.00 4.76   ? 383 ILE A CD1 1 
ATOM   2010 N  N   . ALA A 1 384 ? 118.307 117.095 75.235  1.00 4.19   ? 384 ALA A N   1 
ATOM   2011 C  CA  . ALA A 1 384 ? 117.531 118.129 74.557  1.00 4.19   ? 384 ALA A CA  1 
ATOM   2012 C  C   . ALA A 1 384 ? 116.704 117.549 73.431  1.00 4.19   ? 384 ALA A C   1 
ATOM   2013 O  O   . ALA A 1 384 ? 117.238 116.879 72.550  1.00 4.19   ? 384 ALA A O   1 
ATOM   2014 C  CB  . ALA A 1 384 ? 118.420 119.211 73.983  1.00 4.19   ? 384 ALA A CB  1 
ATOM   2015 N  N   . THR A 1 385 ? 115.424 117.848 73.433  1.00 6.56   ? 385 THR A N   1 
ATOM   2016 C  CA  . THR A 1 385 ? 114.503 117.450 72.388  1.00 6.56   ? 385 THR A CA  1 
ATOM   2017 C  C   . THR A 1 385 ? 114.220 118.678 71.545  1.00 6.56   ? 385 THR A C   1 
ATOM   2018 O  O   . THR A 1 385 ? 114.557 119.785 71.940  1.00 6.56   ? 385 THR A O   1 
ATOM   2019 C  CB  . THR A 1 385 ? 113.217 116.895 73.001  1.00 6.56   ? 385 THR A CB  1 
ATOM   2020 O  OG1 . THR A 1 385 ? 113.522 115.743 73.795  1.00 6.56   ? 385 THR A OG1 1 
ATOM   2021 C  CG2 . THR A 1 385 ? 112.210 116.506 71.958  1.00 6.56   ? 385 THR A CG2 1 
ATOM   2022 N  N   . ALA A 1 386 ? 113.679 118.486 70.351  1.00 9.08   ? 386 ALA A N   1 
ATOM   2023 C  CA  . ALA A 1 386 ? 113.079 119.591 69.623  1.00 9.08   ? 386 ALA A CA  1 
ATOM   2024 C  C   . ALA A 1 386 ? 112.407 119.044 68.392  1.00 9.08   ? 386 ALA A C   1 
ATOM   2025 O  O   . ALA A 1 386 ? 113.023 118.294 67.644  1.00 9.08   ? 386 ALA A O   1 
ATOM   2026 C  CB  . ALA A 1 386 ? 114.111 120.630 69.201  1.00 9.08   ? 386 ALA A CB  1 
ATOM   2027 N  N   . HIS A 1 387 ? 111.160 119.411 68.173  1.00 16.99  ? 387 HIS A N   1 
ATOM   2028 C  CA  . HIS A 1 387 ? 110.697 119.291 66.814  1.00 16.99  ? 387 HIS A CA  1 
ATOM   2029 C  C   . HIS A 1 387 ? 111.322 120.415 66.012  1.00 16.99  ? 387 HIS A C   1 
ATOM   2030 O  O   . HIS A 1 387 ? 112.000 121.285 66.548  1.00 16.99  ? 387 HIS A O   1 
ATOM   2031 C  CB  . HIS A 1 387 ? 109.185 119.354 66.734  1.00 16.99  ? 387 HIS A CB  1 
ATOM   2032 C  CG  . HIS A 1 387 ? 108.491 118.289 67.516  1.00 16.99  ? 387 HIS A CG  1 
ATOM   2033 N  ND1 . HIS A 1 387 ? 107.199 117.901 67.245  1.00 16.99  ? 387 HIS A ND1 1 
ATOM   2034 C  CD2 . HIS A 1 387 ? 108.894 117.548 68.571  1.00 16.99  ? 387 HIS A CD2 1 
ATOM   2035 C  CE1 . HIS A 1 387 ? 106.841 116.957 68.093  1.00 16.99  ? 387 HIS A CE1 1 
ATOM   2036 N  NE2 . HIS A 1 387 ? 107.850 116.727 68.910  1.00 16.99  ? 387 HIS A NE2 1 
ATOM   2037 N  N   . ILE A 1 388 ? 111.128 120.380 64.703  1.00 19.43  ? 388 ILE A N   1 
ATOM   2038 C  CA  . ILE A 1 388 ? 111.693 121.406 63.850  1.00 19.43  ? 388 ILE A CA  1 
ATOM   2039 C  C   . ILE A 1 388 ? 110.882 121.352 62.579  1.00 19.43  ? 388 ILE A C   1 
ATOM   2040 O  O   . ILE A 1 388 ? 110.129 120.406 62.364  1.00 19.43  ? 388 ILE A O   1 
ATOM   2041 C  CB  . ILE A 1 388 ? 113.195 121.150 63.607  1.00 19.43  ? 388 ILE A CB  1 
ATOM   2042 C  CG1 . ILE A 1 388 ? 113.919 122.408 63.230  1.00 19.43  ? 388 ILE A CG1 1 
ATOM   2043 C  CG2 . ILE A 1 388 ? 113.376 120.274 62.450  1.00 19.43  ? 388 ILE A CG2 1 
ATOM   2044 C  CD1 . ILE A 1 388 ? 115.388 122.199 63.250  1.00 19.43  ? 388 ILE A CD1 1 
ATOM   2045 N  N   . LYS A 1 389 ? 110.996 122.377 61.747  1.00 39.46  ? 389 LYS A N   1 
ATOM   2046 C  CA  . LYS A 1 389 ? 110.202 122.417 60.520  1.00 39.46  ? 389 LYS A CA  1 
ATOM   2047 C  C   . LYS A 1 389 ? 111.091 122.760 59.330  1.00 39.46  ? 389 LYS A C   1 
ATOM   2048 O  O   . LYS A 1 389 ? 111.274 123.932 59.002  1.00 39.46  ? 389 LYS A O   1 
ATOM   2049 C  CB  . LYS A 1 389 ? 109.067 123.391 60.651  1.00 39.46  ? 389 LYS A CB  1 
ATOM   2050 C  CG  . LYS A 1 389 ? 107.938 123.082 59.710  1.00 39.46  ? 389 LYS A CG  1 
ATOM   2051 C  CD  . LYS A 1 389 ? 106.666 123.787 60.114  1.00 39.46  ? 389 LYS A CD  1 
ATOM   2052 C  CE  . LYS A 1 389 ? 106.069 123.166 61.350  1.00 39.46  ? 389 LYS A CE  1 
ATOM   2053 N  NZ  . LYS A 1 389 ? 104.713 123.695 61.637  1.00 39.46  ? 389 LYS A NZ  1 
ATOM   2054 N  N   . CYS A 1 390 ? 111.626 121.735 58.676  1.00 51.57  ? 390 CYS A N   1 
ATOM   2055 C  CA  . CYS A 1 390 ? 112.378 121.930 57.451  1.00 51.57  ? 390 CYS A CA  1 
ATOM   2056 C  C   . CYS A 1 390 ? 111.434 122.241 56.295  1.00 51.57  ? 390 CYS A C   1 
ATOM   2057 O  O   . CYS A 1 390 ? 110.214 122.096 56.396  1.00 51.57  ? 390 CYS A O   1 
ATOM   2058 C  CB  . CYS A 1 390 ? 113.209 120.693 57.124  1.00 51.57  ? 390 CYS A CB  1 
ATOM   2059 S  SG  . CYS A 1 390 ? 114.049 119.961 58.526  1.00 51.57  ? 390 CYS A SG  1 
ATOM   2060 N  N   . GLU A 1 391 ? 112.016 122.656 55.170  1.00 66.72  ? 391 GLU A N   1 
ATOM   2061 C  CA  . GLU A 1 391 ? 111.246 123.024 53.989  1.00 66.72  ? 391 GLU A CA  1 
ATOM   2062 C  C   . GLU A 1 391 ? 111.359 122.012 52.860  1.00 66.72  ? 391 GLU A C   1 
ATOM   2063 O  O   . GLU A 1 391 ? 110.337 121.565 52.333  1.00 66.72  ? 391 GLU A O   1 
ATOM   2064 C  CB  . GLU A 1 391 ? 111.685 124.402 53.482  1.00 66.72  ? 391 GLU A CB  1 
ATOM   2065 C  CG  . GLU A 1 391 ? 110.912 124.880 52.262  1.00 66.72  ? 391 GLU A CG  1 
ATOM   2066 C  CD  . GLU A 1 391 ? 109.545 125.441 52.606  1.00 66.72  ? 391 GLU A CD  1 
ATOM   2067 O  OE1 . GLU A 1 391 ? 109.270 125.649 53.805  1.00 66.72  ? 391 GLU A OE1 1 
ATOM   2068 O  OE2 . GLU A 1 391 ? 108.745 125.678 51.676  1.00 66.72  ? 391 GLU A OE2 1 
ATOM   2069 N  N   . ASP A 1 392 ? 112.579 121.637 52.472  1.00 73.86  ? 392 ASP A N   1 
ATOM   2070 C  CA  . ASP A 1 392 ? 112.814 120.741 51.341  1.00 73.86  ? 392 ASP A CA  1 
ATOM   2071 C  C   . ASP A 1 392 ? 113.282 119.378 51.833  1.00 73.86  ? 392 ASP A C   1 
ATOM   2072 O  O   . ASP A 1 392 ? 114.412 119.264 52.334  1.00 73.86  ? 392 ASP A O   1 
ATOM   2073 C  CB  . ASP A 1 392 ? 113.844 121.341 50.383  1.00 73.86  ? 392 ASP A CB  1 
ATOM   2074 C  CG  . ASP A 1 392 ? 113.904 120.604 49.063  1.00 73.86  ? 392 ASP A CG  1 
ATOM   2075 O  OD1 . ASP A 1 392 ? 114.856 119.823 48.859  1.00 73.86  ? 392 ASP A OD1 1 
ATOM   2076 O  OD2 . ASP A 1 392 ? 113.000 120.803 48.228  1.00 73.86  ? 392 ASP A OD2 1 
ATOM   2077 N  N   . PRO A 1 393 ? 112.497 118.319 51.679  1.00 75.49  ? 393 PRO A N   1 
ATOM   2078 C  CA  . PRO A 1 393 ? 112.800 117.036 52.322  1.00 75.49  ? 393 PRO A CA  1 
ATOM   2079 C  C   . PRO A 1 393 ? 113.815 116.185 51.568  1.00 75.49  ? 393 PRO A C   1 
ATOM   2080 O  O   . PRO A 1 393 ? 113.684 114.966 51.480  1.00 75.49  ? 393 PRO A O   1 
ATOM   2081 C  CB  . PRO A 1 393 ? 111.432 116.353 52.361  1.00 75.49  ? 393 PRO A CB  1 
ATOM   2082 C  CG  . PRO A 1 393 ? 110.765 116.850 51.133  1.00 75.49  ? 393 PRO A CG  1 
ATOM   2083 C  CD  . PRO A 1 393 ? 111.233 118.268 50.927  1.00 75.49  ? 393 PRO A CD  1 
ATOM   2084 N  N   . THR A 1 394 ? 114.842 116.823 51.059  1.00 75.32  ? 394 THR A N   1 
ATOM   2085 C  CA  . THR A 1 394 ? 115.936 116.120 50.402  1.00 75.32  ? 394 THR A CA  1 
ATOM   2086 C  C   . THR A 1 394 ? 117.291 116.592 50.898  1.00 75.32  ? 394 THR A C   1 
ATOM   2087 O  O   . THR A 1 394 ? 118.246 115.813 50.913  1.00 75.32  ? 394 THR A O   1 
ATOM   2088 C  CB  . THR A 1 394 ? 115.834 116.291 48.881  1.00 75.32  ? 394 THR A CB  1 
ATOM   2089 O  OG1 . THR A 1 394 ? 114.585 115.761 48.427  1.00 75.32  ? 394 THR A OG1 1 
ATOM   2090 C  CG2 . THR A 1 394 ? 116.949 115.551 48.178  1.00 75.32  ? 394 THR A CG2 1 
ATOM   2091 N  N   . SER A 1 395 ? 117.392 117.844 51.325  1.00 63.61  ? 395 SER A N   1 
ATOM   2092 C  CA  . SER A 1 395 ? 118.598 118.373 51.950  1.00 63.61  ? 395 SER A CA  1 
ATOM   2093 C  C   . SER A 1 395 ? 118.487 118.340 53.462  1.00 63.61  ? 395 SER A C   1 
ATOM   2094 O  O   . SER A 1 395 ? 118.948 119.253 54.144  1.00 63.61  ? 395 SER A O   1 
ATOM   2095 C  CB  . SER A 1 395 ? 118.860 119.791 51.468  1.00 63.61  ? 395 SER A CB  1 
ATOM   2096 O  OG  . SER A 1 395 ? 118.137 120.714 52.261  1.00 63.61  ? 395 SER A OG  1 
ATOM   2097 N  N   . TYR A 1 396 ? 117.859 117.305 54.011  1.00 45.26  ? 396 TYR A N   1 
ATOM   2098 C  CA  . TYR A 1 396 ? 117.576 117.305 55.437  1.00 45.26  ? 396 TYR A CA  1 
ATOM   2099 C  C   . TYR A 1 396 ? 118.827 117.027 56.262  1.00 45.26  ? 396 TYR A C   1 
ATOM   2100 O  O   . TYR A 1 396 ? 119.021 117.646 57.313  1.00 45.26  ? 396 TYR A O   1 
ATOM   2101 C  CB  . TYR A 1 396 ? 116.468 116.301 55.742  1.00 45.26  ? 396 TYR A CB  1 
ATOM   2102 C  CG  . TYR A 1 396 ? 116.455 115.777 57.150  1.00 45.26  ? 396 TYR A CG  1 
ATOM   2103 C  CD1 . TYR A 1 396 ? 116.347 116.626 58.226  1.00 45.26  ? 396 TYR A CD1 1 
ATOM   2104 C  CD2 . TYR A 1 396 ? 116.510 114.426 57.395  1.00 45.26  ? 396 TYR A CD2 1 
ATOM   2105 C  CE1 . TYR A 1 396 ? 116.341 116.144 59.500  1.00 45.26  ? 396 TYR A CE1 1 
ATOM   2106 C  CE2 . TYR A 1 396 ? 116.492 113.938 58.659  1.00 45.26  ? 396 TYR A CE2 1 
ATOM   2107 C  CZ  . TYR A 1 396 ? 116.406 114.798 59.708  1.00 45.26  ? 396 TYR A CZ  1 
ATOM   2108 O  OH  . TYR A 1 396 ? 116.390 114.299 60.979  1.00 45.26  ? 396 TYR A OH  1 
ATOM   2109 N  N   . MET A 1 397 ? 119.698 116.123 55.807  1.00 48.30  ? 397 MET A N   1 
ATOM   2110 C  CA  . MET A 1 397 ? 120.805 115.705 56.664  1.00 48.30  ? 397 MET A CA  1 
ATOM   2111 C  C   . MET A 1 397 ? 121.780 116.841 56.940  1.00 48.30  ? 397 MET A C   1 
ATOM   2112 O  O   . MET A 1 397 ? 122.325 116.930 58.046  1.00 48.30  ? 397 MET A O   1 
ATOM   2113 C  CB  . MET A 1 397 ? 121.543 114.516 56.060  1.00 48.30  ? 397 MET A CB  1 
ATOM   2114 C  CG  . MET A 1 397 ? 120.825 113.181 56.232  1.00 48.30  ? 397 MET A CG  1 
ATOM   2115 S  SD  . MET A 1 397 ? 120.375 112.735 57.921  1.00 48.30  ? 397 MET A SD  1 
ATOM   2116 C  CE  . MET A 1 397 ? 121.935 112.913 58.750  1.00 48.30  ? 397 MET A CE  1 
ATOM   2117 N  N   . GLU A 1 398 ? 122.013 117.721 55.967  1.00 48.89  ? 398 GLU A N   1 
ATOM   2118 C  CA  . GLU A 1 398 ? 122.859 118.879 56.237  1.00 48.89  ? 398 GLU A CA  1 
ATOM   2119 C  C   . GLU A 1 398 ? 122.242 119.769 57.305  1.00 48.89  ? 398 GLU A C   1 
ATOM   2120 O  O   . GLU A 1 398 ? 122.942 120.254 58.204  1.00 48.89  ? 398 GLU A O   1 
ATOM   2121 C  CB  . GLU A 1 398 ? 123.095 119.680 54.962  1.00 48.89  ? 398 GLU A CB  1 
ATOM   2122 C  CG  . GLU A 1 398 ? 123.565 118.862 53.799  1.00 48.89  ? 398 GLU A CG  1 
ATOM   2123 C  CD  . GLU A 1 398 ? 123.297 119.552 52.491  1.00 48.89  ? 398 GLU A CD  1 
ATOM   2124 O  OE1 . GLU A 1 398 ? 122.824 120.706 52.523  1.00 48.89  ? 398 GLU A OE1 1 
ATOM   2125 O  OE2 . GLU A 1 398 ? 123.559 118.944 51.435  1.00 48.89  ? 398 GLU A OE2 1 
ATOM   2126 N  N   . VAL A 1 399 ? 120.935 120.005 57.218  1.00 45.38  ? 399 VAL A N   1 
ATOM   2127 C  CA  . VAL A 1 399 ? 120.269 120.808 58.232  1.00 45.38  ? 399 VAL A CA  1 
ATOM   2128 C  C   . VAL A 1 399 ? 120.413 120.161 59.597  1.00 45.38  ? 399 VAL A C   1 
ATOM   2129 O  O   . VAL A 1 399 ? 120.687 120.841 60.590  1.00 45.38  ? 399 VAL A O   1 
ATOM   2130 C  CB  . VAL A 1 399 ? 118.797 121.028 57.859  1.00 45.38  ? 399 VAL A CB  1 
ATOM   2131 C  CG1 . VAL A 1 399 ? 117.993 121.320 59.085  1.00 45.38  ? 399 VAL A CG1 1 
ATOM   2132 C  CG2 . VAL A 1 399 ? 118.690 122.178 56.902  1.00 45.38  ? 399 VAL A CG2 1 
ATOM   2133 N  N   . ALA A 1 400 ? 120.255 118.841 59.674  1.00 43.28  ? 400 ALA A N   1 
ATOM   2134 C  CA  . ALA A 1 400 ? 120.335 118.186 60.975  1.00 43.28  ? 400 ALA A CA  1 
ATOM   2135 C  C   . ALA A 1 400 ? 121.751 118.231 61.533  1.00 43.28  ? 400 ALA A C   1 
ATOM   2136 O  O   . ALA A 1 400 ? 121.941 118.361 62.747  1.00 43.28  ? 400 ALA A O   1 
ATOM   2137 C  CB  . ALA A 1 400 ? 119.831 116.753 60.886  1.00 43.28  ? 400 ALA A CB  1 
ATOM   2138 N  N   . LYS A 1 401 ? 122.761 118.151 60.667  1.00 39.50  ? 401 LYS A N   1 
ATOM   2139 C  CA  . LYS A 1 401 ? 124.134 118.310 61.139  1.00 39.50  ? 401 LYS A CA  1 
ATOM   2140 C  C   . LYS A 1 401 ? 124.372 119.718 61.675  1.00 39.50  ? 401 LYS A C   1 
ATOM   2141 O  O   . LYS A 1 401 ? 124.992 119.899 62.731  1.00 39.50  ? 401 LYS A O   1 
ATOM   2142 C  CB  . LYS A 1 401 ? 125.119 117.996 60.019  1.00 39.50  ? 401 LYS A CB  1 
ATOM   2143 C  CG  . LYS A 1 401 ? 125.610 116.569 59.999  1.00 39.50  ? 401 LYS A CG  1 
ATOM   2144 C  CD  . LYS A 1 401 ? 126.529 116.350 58.814  1.00 39.50  ? 401 LYS A CD  1 
ATOM   2145 C  CE  . LYS A 1 401 ? 126.461 114.923 58.306  1.00 39.50  ? 401 LYS A CE  1 
ATOM   2146 N  NZ  . LYS A 1 401 ? 126.485 113.938 59.413  1.00 39.50  ? 401 LYS A NZ  1 
ATOM   2147 N  N   . THR A 1 402 ? 123.886 120.733 60.959  1.00 37.81  ? 402 THR A N   1 
ATOM   2148 C  CA  . THR A 1 402 ? 124.053 122.102 61.436  1.00 37.81  ? 402 THR A CA  1 
ATOM   2149 C  C   . THR A 1 402 ? 123.361 122.306 62.775  1.00 37.81  ? 402 THR A C   1 
ATOM   2150 O  O   . THR A 1 402 ? 123.906 122.961 63.673  1.00 37.81  ? 402 THR A O   1 
ATOM   2151 C  CB  . THR A 1 402 ? 123.513 123.090 60.412  1.00 37.81  ? 402 THR A CB  1 
ATOM   2152 O  OG1 . THR A 1 402 ? 124.150 122.867 59.153  1.00 37.81  ? 402 THR A OG1 1 
ATOM   2153 C  CG2 . THR A 1 402 ? 123.810 124.485 60.849  1.00 37.81  ? 402 THR A CG2 1 
ATOM   2154 N  N   . ILE A 1 403 ? 122.166 121.741 62.935  1.00 33.39  ? 403 ILE A N   1 
ATOM   2155 C  CA  . ILE A 1 403 ? 121.446 121.890 64.191  1.00 33.39  ? 403 ILE A CA  1 
ATOM   2156 C  C   . ILE A 1 403 ? 122.178 121.174 65.311  1.00 33.39  ? 403 ILE A C   1 
ATOM   2157 O  O   . ILE A 1 403 ? 122.260 121.681 66.434  1.00 33.39  ? 403 ILE A O   1 
ATOM   2158 C  CB  . ILE A 1 403 ? 120.007 121.385 64.049  1.00 33.39  ? 403 ILE A CB  1 
ATOM   2159 C  CG1 . ILE A 1 403 ? 119.260 122.230 63.041  1.00 33.39  ? 403 ILE A CG1 1 
ATOM   2160 C  CG2 . ILE A 1 403 ? 119.305 121.498 65.340  1.00 33.39  ? 403 ILE A CG2 1 
ATOM   2161 C  CD1 . ILE A 1 403 ? 119.448 123.671 63.258  1.00 33.39  ? 403 ILE A CD1 1 
ATOM   2162 N  N   . LYS A 1 404 ? 122.730 119.993 65.037  1.00 31.52  ? 404 LYS A N   1 
ATOM   2163 C  CA  . LYS A 1 404 ? 123.504 119.320 66.073  1.00 31.52  ? 404 LYS A CA  1 
ATOM   2164 C  C   . LYS A 1 404 ? 124.729 120.130 66.460  1.00 31.52  ? 404 LYS A C   1 
ATOM   2165 O  O   . LYS A 1 404 ? 125.151 120.114 67.618  1.00 31.52  ? 404 LYS A O   1 
ATOM   2166 C  CB  . LYS A 1 404 ? 123.925 117.938 65.619  1.00 31.52  ? 404 LYS A CB  1 
ATOM   2167 C  CG  . LYS A 1 404 ? 124.672 117.199 66.684  1.00 31.52  ? 404 LYS A CG  1 
ATOM   2168 C  CD  . LYS A 1 404 ? 123.732 116.746 67.748  1.00 31.52  ? 404 LYS A CD  1 
ATOM   2169 C  CE  . LYS A 1 404 ? 124.394 115.708 68.595  1.00 31.52  ? 404 LYS A CE  1 
ATOM   2170 N  NZ  . LYS A 1 404 ? 123.444 114.611 68.882  1.00 31.52  ? 404 LYS A NZ  1 
ATOM   2171 N  N   . ASP A 1 405 ? 125.310 120.859 65.510  1.00 32.87  ? 405 ASP A N   1 
ATOM   2172 C  CA  . ASP A 1 405 ? 126.428 121.730 65.864  1.00 32.87  ? 405 ASP A CA  1 
ATOM   2173 C  C   . ASP A 1 405 ? 125.981 122.879 66.764  1.00 32.87  ? 405 ASP A C   1 
ATOM   2174 O  O   . ASP A 1 405 ? 126.676 123.231 67.727  1.00 32.87  ? 405 ASP A O   1 
ATOM   2175 C  CB  . ASP A 1 405 ? 127.091 122.272 64.603  1.00 32.87  ? 405 ASP A CB  1 
ATOM   2176 C  CG  . ASP A 1 405 ? 128.212 121.389 64.113  1.00 32.87  ? 405 ASP A CG  1 
ATOM   2177 O  OD1 . ASP A 1 405 ? 128.950 121.815 63.201  1.00 32.87  ? 405 ASP A OD1 1 
ATOM   2178 O  OD2 . ASP A 1 405 ? 128.351 120.263 64.632  1.00 32.87  ? 405 ASP A OD2 1 
ATOM   2179 N  N   . VAL A 1 406 ? 124.833 123.490 66.461  1.00 27.81  ? 406 VAL A N   1 
ATOM   2180 C  CA  . VAL A 1 406 ? 124.398 124.636 67.258  1.00 27.81  ? 406 VAL A CA  1 
ATOM   2181 C  C   . VAL A 1 406 ? 123.795 124.183 68.577  1.00 27.81  ? 406 VAL A C   1 
ATOM   2182 O  O   . VAL A 1 406 ? 123.437 125.012 69.416  1.00 27.81  ? 406 VAL A O   1 
ATOM   2183 C  CB  . VAL A 1 406 ? 123.404 125.507 66.490  1.00 27.81  ? 406 VAL A CB  1 
ATOM   2184 C  CG1 . VAL A 1 406 ? 122.085 124.836 66.472  1.00 27.81  ? 406 VAL A CG1 1 
ATOM   2185 C  CG2 . VAL A 1 406 ? 123.295 126.851 67.131  1.00 27.81  ? 406 VAL A CG2 1 
ATOM   2186 N  N   . PHE A 1 407 ? 123.602 122.879 68.765  1.00 26.07  ? 407 PHE A N   1 
ATOM   2187 C  CA  . PHE A 1 407 ? 123.432 122.383 70.129  1.00 26.07  ? 407 PHE A CA  1 
ATOM   2188 C  C   . PHE A 1 407 ? 124.760 122.066 70.788  1.00 26.07  ? 407 PHE A C   1 
ATOM   2189 O  O   . PHE A 1 407 ? 124.910 122.263 71.995  1.00 26.07  ? 407 PHE A O   1 
ATOM   2190 C  CB  . PHE A 1 407 ? 122.561 121.139 70.184  1.00 26.07  ? 407 PHE A CB  1 
ATOM   2191 C  CG  . PHE A 1 407 ? 121.117 121.426 70.214  1.00 26.07  ? 407 PHE A CG  1 
ATOM   2192 C  CD1 . PHE A 1 407 ? 120.672 122.678 70.458  1.00 26.07  ? 407 PHE A CD1 1 
ATOM   2193 C  CD2 . PHE A 1 407 ? 120.205 120.437 70.035  1.00 26.07  ? 407 PHE A CD2 1 
ATOM   2194 C  CE1 . PHE A 1 407 ? 119.348 122.934 70.497  1.00 26.07  ? 407 PHE A CE1 1 
ATOM   2195 C  CE2 . PHE A 1 407 ? 118.895 120.704 70.079  1.00 26.07  ? 407 PHE A CE2 1 
ATOM   2196 C  CZ  . PHE A 1 407 ? 118.465 121.948 70.303  1.00 26.07  ? 407 PHE A CZ  1 
ATOM   2197 N  N   . HIS A 1 408 ? 125.724 121.557 70.035  1.00 34.31  ? 408 HIS A N   1 
ATOM   2198 C  CA  . HIS A 1 408 ? 126.987 121.173 70.647  1.00 34.31  ? 408 HIS A CA  1 
ATOM   2199 C  C   . HIS A 1 408 ? 127.733 122.392 71.158  1.00 34.31  ? 408 HIS A C   1 
ATOM   2200 O  O   . HIS A 1 408 ? 128.557 122.292 72.069  1.00 34.31  ? 408 HIS A O   1 
ATOM   2201 C  CB  . HIS A 1 408 ? 127.835 120.398 69.644  1.00 34.31  ? 408 HIS A CB  1 
ATOM   2202 C  CG  . HIS A 1 408 ? 129.137 119.917 70.195  1.00 34.31  ? 408 HIS A CG  1 
ATOM   2203 N  ND1 . HIS A 1 408 ? 129.216 119.033 71.244  1.00 34.31  ? 408 HIS A ND1 1 
ATOM   2204 C  CD2 . HIS A 1 408 ? 130.411 120.194 69.835  1.00 34.31  ? 408 HIS A CD2 1 
ATOM   2205 C  CE1 . HIS A 1 408 ? 130.484 118.793 71.514  1.00 34.31  ? 408 HIS A CE1 1 
ATOM   2206 N  NE2 . HIS A 1 408 ? 131.230 119.482 70.671  1.00 34.31  ? 408 HIS A NE2 1 
ATOM   2207 N  N   . ASN A 1 409 ? 127.474 123.551 70.571  1.00 31.17  ? 409 ASN A N   1 
ATOM   2208 C  CA  . ASN A 1 409 ? 128.168 124.752 71.018  1.00 31.17  ? 409 ASN A CA  1 
ATOM   2209 C  C   . ASN A 1 409 ? 127.641 125.268 72.349  1.00 31.17  ? 409 ASN A C   1 
ATOM   2210 O  O   . ASN A 1 409 ? 128.062 126.333 72.800  1.00 31.17  ? 409 ASN A O   1 
ATOM   2211 C  CB  . ASN A 1 409 ? 128.054 125.866 69.984  1.00 31.17  ? 409 ASN A CB  1 
ATOM   2212 C  CG  . ASN A 1 409 ? 129.009 125.698 68.844  1.00 31.17  ? 409 ASN A CG  1 
ATOM   2213 O  OD1 . ASN A 1 409 ? 129.330 124.584 68.445  1.00 31.17  ? 409 ASN A OD1 1 
ATOM   2214 N  ND2 . ASN A 1 409 ? 129.471 126.810 68.302  1.00 31.17  ? 409 ASN A ND2 1 
ATOM   2215 N  N   . HIS A 1 410 ? 126.653 124.603 72.940  1.00 29.25  ? 410 HIS A N   1 
ATOM   2216 C  CA  . HIS A 1 410 ? 126.047 125.143 74.190  1.00 29.25  ? 410 HIS A CA  1 
ATOM   2217 C  C   . HIS A 1 410 ? 126.028 124.105 75.314  1.00 29.25  ? 410 HIS A C   1 
ATOM   2218 O  O   . HIS A 1 410 ? 125.056 124.108 76.083  1.00 29.25  ? 410 HIS A O   1 
ATOM   2219 C  CB  . HIS A 1 410 ? 124.624 125.653 73.928  1.00 29.25  ? 410 HIS A CB  1 
ATOM   2220 C  CG  . HIS A 1 410 ? 124.541 126.792 72.970  1.00 29.25  ? 410 HIS A CG  1 
ATOM   2221 N  ND1 . HIS A 1 410 ? 125.654 127.329 72.358  1.00 29.25  ? 410 HIS A ND1 1 
ATOM   2222 C  CD2 . HIS A 1 410 ? 123.483 127.494 72.512  1.00 29.25  ? 410 HIS A CD2 1 
ATOM   2223 C  CE1 . HIS A 1 410 ? 125.285 128.315 71.565  1.00 29.25  ? 410 HIS A CE1 1 
ATOM   2224 N  NE2 . HIS A 1 410 ? 123.958 128.435 71.641  1.00 29.25  ? 410 HIS A NE2 1 
ATOM   2225 N  N   . GLY A 1 411 ? 127.031 123.256 75.424  1.00 23.35  ? 411 GLY A N   1 
ATOM   2226 C  CA  . GLY A 1 411 ? 127.059 122.285 76.498  1.00 23.35  ? 411 GLY A CA  1 
ATOM   2227 C  C   . GLY A 1 411 ? 125.925 121.288 76.490  1.00 23.35  ? 411 GLY A C   1 
ATOM   2228 O  O   . GLY A 1 411 ? 125.690 120.636 77.503  1.00 23.35  ? 411 GLY A O   1 
ATOM   2229 N  N   . ILE A 1 412 ? 125.228 121.134 75.364  1.00 19.76  ? 412 ILE A N   1 
ATOM   2230 C  CA  . ILE A 1 412 ? 124.076 120.246 75.245  1.00 19.76  ? 412 ILE A CA  1 
ATOM   2231 C  C   . ILE A 1 412 ? 124.358 119.231 74.150  1.00 19.76  ? 412 ILE A C   1 
ATOM   2232 O  O   . ILE A 1 412 ? 124.389 119.592 72.972  1.00 19.76  ? 412 ILE A O   1 
ATOM   2233 C  CB  . ILE A 1 412 ? 122.801 121.014 74.896  1.00 19.76  ? 412 ILE A CB  1 
ATOM   2234 C  CG1 . ILE A 1 412 ? 122.401 121.929 76.030  1.00 19.76  ? 412 ILE A CG1 1 
ATOM   2235 C  CG2 . ILE A 1 412 ? 121.715 120.061 74.626  1.00 19.76  ? 412 ILE A CG2 1 
ATOM   2236 C  CD1 . ILE A 1 412 ? 121.015 122.478 75.872  1.00 19.76  ? 412 ILE A CD1 1 
ATOM   2237 N  N   . HIS A 1 413 ? 124.499 117.959 74.515  1.00 20.89  ? 413 HIS A N   1 
ATOM   2238 C  CA  . HIS A 1 413 ? 125.062 116.995 73.588  1.00 20.89  ? 413 HIS A CA  1 
ATOM   2239 C  C   . HIS A 1 413 ? 124.173 115.837 73.184  1.00 20.89  ? 413 HIS A C   1 
ATOM   2240 O  O   . HIS A 1 413 ? 124.376 115.308 72.092  1.00 20.89  ? 413 HIS A O   1 
ATOM   2241 C  CB  . HIS A 1 413 ? 126.352 116.415 74.155  1.00 20.89  ? 413 HIS A CB  1 
ATOM   2242 C  CG  . HIS A 1 413 ? 127.400 117.439 74.410  1.00 20.89  ? 413 HIS A CG  1 
ATOM   2243 N  ND1 . HIS A 1 413 ? 128.048 118.112 73.399  1.00 20.89  ? 413 HIS A ND1 1 
ATOM   2244 C  CD2 . HIS A 1 413 ? 127.921 117.903 75.566  1.00 20.89  ? 413 HIS A CD2 1 
ATOM   2245 C  CE1 . HIS A 1 413 ? 128.919 118.954 73.923  1.00 20.89  ? 413 HIS A CE1 1 
ATOM   2246 N  NE2 . HIS A 1 413 ? 128.863 118.845 75.237  1.00 20.89  ? 413 HIS A NE2 1 
ATOM   2247 N  N   . ALA A 1 414 ? 123.234 115.399 74.002  1.00 8.17   ? 414 ALA A N   1 
ATOM   2248 C  CA  . ALA A 1 414 ? 122.378 114.276 73.644  1.00 8.17   ? 414 ALA A CA  1 
ATOM   2249 C  C   . ALA A 1 414 ? 121.050 114.824 73.150  1.00 8.17   ? 414 ALA A C   1 
ATOM   2250 O  O   . ALA A 1 414 ? 120.191 115.182 73.956  1.00 8.17   ? 414 ALA A O   1 
ATOM   2251 C  CB  . ALA A 1 414 ? 122.174 113.350 74.832  1.00 8.17   ? 414 ALA A CB  1 
ATOM   2252 N  N   . THR A 1 415 ? 120.867 114.892 71.842  1.00 9.42   ? 415 THR A N   1 
ATOM   2253 C  CA  . THR A 1 415 ? 119.757 115.644 71.287  1.00 9.42   ? 415 THR A CA  1 
ATOM   2254 C  C   . THR A 1 415 ? 118.780 114.723 70.582  1.00 9.42   ? 415 THR A C   1 
ATOM   2255 O  O   . THR A 1 415 ? 118.955 113.508 70.551  1.00 9.42   ? 415 THR A O   1 
ATOM   2256 C  CB  . THR A 1 415 ? 120.241 116.697 70.315  1.00 9.42   ? 415 THR A CB  1 
ATOM   2257 O  OG1 . THR A 1 415 ? 120.585 116.067 69.082  1.00 9.42   ? 415 THR A OG1 1 
ATOM   2258 C  CG2 . THR A 1 415 ? 121.460 117.360 70.865  1.00 9.42   ? 415 THR A CG2 1 
ATOM   2259 N  N   . THR A 1 416 ? 117.701 115.320 70.080  1.00 9.41   ? 416 THR A N   1 
ATOM   2260 C  CA  . THR A 1 416 ? 116.748 114.611 69.222  1.00 9.41   ? 416 THR A CA  1 
ATOM   2261 C  C   . THR A 1 416 ? 115.912 115.642 68.468  1.00 9.41   ? 416 THR A C   1 
ATOM   2262 O  O   . THR A 1 416 ? 114.988 116.214 69.041  1.00 9.41   ? 416 THR A O   1 
ATOM   2263 C  CB  . THR A 1 416 ? 115.868 113.695 70.042  1.00 9.41   ? 416 THR A CB  1 
ATOM   2264 O  OG1 . THR A 1 416 ? 116.692 112.818 70.808  1.00 9.41   ? 416 THR A OG1 1 
ATOM   2265 C  CG2 . THR A 1 416 ? 115.035 112.894 69.146  1.00 9.41   ? 416 THR A CG2 1 
ATOM   2266 N  N   . ILE A 1 417 ? 116.204 115.847 67.190  1.00 8.51   ? 417 ILE A N   1 
ATOM   2267 C  CA  . ILE A 1 417 ? 115.614 116.920 66.398  1.00 8.51   ? 417 ILE A CA  1 
ATOM   2268 C  C   . ILE A 1 417 ? 114.688 116.329 65.347  1.00 8.51   ? 417 ILE A C   1 
ATOM   2269 O  O   . ILE A 1 417 ? 115.110 116.107 64.213  1.00 8.51   ? 417 ILE A O   1 
ATOM   2270 C  CB  . ILE A 1 417 ? 116.707 117.750 65.723  1.00 8.51   ? 417 ILE A CB  1 
ATOM   2271 C  CG1 . ILE A 1 417 ? 117.718 118.174 66.749  1.00 8.51   ? 417 ILE A CG1 1 
ATOM   2272 C  CG2 . ILE A 1 417 ? 116.134 118.973 65.100  1.00 8.51   ? 417 ILE A CG2 1 
ATOM   2273 C  CD1 . ILE A 1 417 ? 117.222 119.265 67.570  1.00 8.51   ? 417 ILE A CD1 1 
ATOM   2274 N  N   . GLN A 1 418 ? 113.415 116.153 65.676  1.00 17.72  ? 418 GLN A N   1 
ATOM   2275 C  CA  . GLN A 1 418 ? 112.493 115.529 64.731  1.00 17.72  ? 418 GLN A CA  1 
ATOM   2276 C  C   . GLN A 1 418 ? 112.071 116.527 63.681  1.00 17.72  ? 418 GLN A C   1 
ATOM   2277 O  O   . GLN A 1 418 ? 111.519 117.567 64.042  1.00 17.72  ? 418 GLN A O   1 
ATOM   2278 C  CB  . GLN A 1 418 ? 111.257 114.997 65.420  1.00 17.72  ? 418 GLN A CB  1 
ATOM   2279 C  CG  . GLN A 1 418 ? 110.200 114.588 64.430  1.00 17.72  ? 418 GLN A CG  1 
ATOM   2280 C  CD  . GLN A 1 418 ? 108.885 114.309 65.092  1.00 17.72  ? 418 GLN A CD  1 
ATOM   2281 O  OE1 . GLN A 1 418 ? 108.788 114.338 66.305  1.00 17.72  ? 418 GLN A OE1 1 
ATOM   2282 N  NE2 . GLN A 1 418 ? 107.869 114.018 64.307  1.00 17.72  ? 418 GLN A NE2 1 
ATOM   2283 N  N   . PRO A 1 419 ? 112.255 116.284 62.425  1.00 27.65  ? 419 PRO A N   1 
ATOM   2284 C  CA  . PRO A 1 419 ? 111.826 117.262 61.434  1.00 27.65  ? 419 PRO A CA  1 
ATOM   2285 C  C   . PRO A 1 419 ? 110.429 116.977 60.930  1.00 27.65  ? 419 PRO A C   1 
ATOM   2286 O  O   . PRO A 1 419 ? 110.134 115.844 60.552  1.00 27.65  ? 419 PRO A O   1 
ATOM   2287 C  CB  . PRO A 1 419 ? 112.866 117.095 60.336  1.00 27.65  ? 419 PRO A CB  1 
ATOM   2288 C  CG  . PRO A 1 419 ? 113.141 115.682 60.380  1.00 27.65  ? 419 PRO A CG  1 
ATOM   2289 C  CD  . PRO A 1 419 ? 113.062 115.240 61.810  1.00 27.65  ? 419 PRO A CD  1 
ATOM   2290 N  N   . GLU A 1 420 ? 109.563 117.988 60.916  1.00 31.82  ? 420 GLU A N   1 
ATOM   2291 C  CA  . GLU A 1 420 ? 108.170 117.862 60.514  1.00 31.82  ? 420 GLU A CA  1 
ATOM   2292 C  C   . GLU A 1 420 ? 108.055 118.445 59.112  1.00 31.82  ? 420 GLU A C   1 
ATOM   2293 O  O   . GLU A 1 420 ? 108.027 119.664 58.944  1.00 31.82  ? 420 GLU A O   1 
ATOM   2294 C  CB  . GLU A 1 420 ? 107.270 118.588 61.506  1.00 31.82  ? 420 GLU A CB  1 
ATOM   2295 C  CG  . GLU A 1 420 ? 107.026 117.839 62.800  1.00 31.82  ? 420 GLU A CG  1 
ATOM   2296 C  CD  . GLU A 1 420 ? 106.775 118.757 63.992  1.00 31.82  ? 420 GLU A CD  1 
ATOM   2297 O  OE1 . GLU A 1 420 ? 107.069 119.955 63.882  1.00 31.82  ? 420 GLU A OE1 1 
ATOM   2298 O  OE2 . GLU A 1 420 ? 106.299 118.286 65.046  1.00 31.82  ? 420 GLU A OE2 1 
ATOM   2299 N  N   . PHE A 1 421 ? 108.015 117.577 58.104  1.00 54.64  ? 421 PHE A N   1 
ATOM   2300 C  CA  . PHE A 1 421 ? 107.968 118.030 56.719  1.00 54.64  ? 421 PHE A CA  1 
ATOM   2301 C  C   . PHE A 1 421 ? 106.576 118.515 56.344  1.00 54.64  ? 421 PHE A C   1 
ATOM   2302 O  O   . PHE A 1 421 ? 105.580 117.807 56.501  1.00 54.64  ? 421 PHE A O   1 
ATOM   2303 C  CB  . PHE A 1 421 ? 108.374 116.911 55.766  1.00 54.64  ? 421 PHE A CB  1 
ATOM   2304 C  CG  . PHE A 1 421 ? 109.842 116.675 55.715  1.00 54.64  ? 421 PHE A CG  1 
ATOM   2305 C  CD1 . PHE A 1 421 ? 110.721 117.716 55.877  1.00 54.64  ? 421 PHE A CD1 1 
ATOM   2306 C  CD2 . PHE A 1 421 ? 110.342 115.409 55.537  1.00 54.64  ? 421 PHE A CD2 1 
ATOM   2307 C  CE1 . PHE A 1 421 ? 112.062 117.501 55.841  1.00 54.64  ? 421 PHE A CE1 1 
ATOM   2308 C  CE2 . PHE A 1 421 ? 111.681 115.190 55.509  1.00 54.64  ? 421 PHE A CE2 1 
ATOM   2309 C  CZ  . PHE A 1 421 ? 112.542 116.236 55.660  1.00 54.64  ? 421 PHE A CZ  1 
ATOM   2310 N  N   . ALA A 1 422 ? 106.519 119.724 55.801  1.00 71.03  ? 422 ALA A N   1 
ATOM   2311 C  CA  . ALA A 1 422 ? 105.246 120.355 55.490  1.00 71.03  ? 422 ALA A CA  1 
ATOM   2312 C  C   . ALA A 1 422 ? 104.596 119.713 54.271  1.00 71.03  ? 422 ALA A C   1 
ATOM   2313 O  O   . ALA A 1 422 ? 105.224 119.534 53.225  1.00 71.03  ? 422 ALA A O   1 
ATOM   2314 C  CB  . ALA A 1 422 ? 105.425 121.854 55.250  1.00 71.03  ? 422 ALA A CB  1 
ATOM   2315 N  N   . SER A 1 423 ? 103.317 119.380 54.420  1.00 79.17  ? 423 SER A N   1 
ATOM   2316 C  CA  . SER A 1 423 ? 102.469 118.834 53.374  1.00 79.17  ? 423 SER A CA  1 
ATOM   2317 C  C   . SER A 1 423 ? 101.890 119.983 52.555  1.00 79.17  ? 423 SER A C   1 
ATOM   2318 O  O   . SER A 1 423 ? 102.385 121.115 52.602  1.00 79.17  ? 423 SER A O   1 
ATOM   2319 C  CB  . SER A 1 423 ? 101.372 117.960 53.982  1.00 79.17  ? 423 SER A CB  1 
ATOM   2320 O  OG  . SER A 1 423 ? 101.898 117.105 54.980  1.00 79.17  ? 423 SER A OG  1 
ATOM   2321 N  N   . VAL A 1 424 ? 100.849 119.689 51.781  1.00 83.41  ? 424 VAL A N   1 
ATOM   2322 C  CA  . VAL A 1 424 ? 100.219 120.684 50.919  1.00 83.41  ? 424 VAL A CA  1 
ATOM   2323 C  C   . VAL A 1 424 ? 99.183  121.477 51.705  1.00 83.41  ? 424 VAL A C   1 
ATOM   2324 O  O   . VAL A 1 424 ? 98.211  120.921 52.229  1.00 83.41  ? 424 VAL A O   1 
ATOM   2325 C  CB  . VAL A 1 424 ? 99.589  120.016 49.684  1.00 83.41  ? 424 VAL A CB  1 
ATOM   2326 C  CG1 . VAL A 1 424 ? 99.063  121.071 48.727  1.00 83.41  ? 424 VAL A CG1 1 
ATOM   2327 C  CG2 . VAL A 1 424 ? 100.608 119.126 48.993  1.00 83.41  ? 424 VAL A CG2 1 
ATOM   2328 N  N   . GLY A 1 425 ? 99.395  122.793 51.779  1.00 80.59  ? 425 GLY A N   1 
ATOM   2329 C  CA  . GLY A 1 425 ? 98.441  123.719 52.355  1.00 80.59  ? 425 GLY A CA  1 
ATOM   2330 C  C   . GLY A 1 425 ? 98.341  123.735 53.863  1.00 80.59  ? 425 GLY A C   1 
ATOM   2331 O  O   . GLY A 1 425 ? 97.479  124.446 54.395  1.00 80.59  ? 425 GLY A O   1 
ATOM   2332 N  N   . SER A 1 426 ? 99.187  122.996 54.579  1.00 76.88  ? 426 SER A N   1 
ATOM   2333 C  CA  . SER A 1 426 ? 99.039  122.833 56.019  1.00 76.88  ? 426 SER A CA  1 
ATOM   2334 C  C   . SER A 1 426 ? 100.001 123.687 56.836  1.00 76.88  ? 426 SER A C   1 
ATOM   2335 O  O   . SER A 1 426 ? 100.302 123.329 57.979  1.00 76.88  ? 426 SER A O   1 
ATOM   2336 C  CB  . SER A 1 426 ? 99.213  121.366 56.406  1.00 76.88  ? 426 SER A CB  1 
ATOM   2337 O  OG  . SER A 1 426 ? 99.377  121.242 57.808  1.00 76.88  ? 426 SER A OG  1 
ATOM   2338 N  N   . LYS A 1 427 ? 100.488 124.800 56.291  1.00 75.89  ? 427 LYS A N   1 
ATOM   2339 C  CA  . LYS A 1 427 ? 101.351 125.705 57.054  1.00 75.89  ? 427 LYS A CA  1 
ATOM   2340 C  C   . LYS A 1 427 ? 100.517 126.790 57.738  1.00 75.89  ? 427 LYS A C   1 
ATOM   2341 O  O   . LYS A 1 427 ? 100.795 127.984 57.663  1.00 75.89  ? 427 LYS A O   1 
ATOM   2342 C  CB  . LYS A 1 427 ? 102.416 126.310 56.148  1.00 75.89  ? 427 LYS A CB  1 
ATOM   2343 C  CG  . LYS A 1 427 ? 101.876 126.881 54.853  1.00 75.89  ? 427 LYS A CG  1 
ATOM   2344 C  CD  . LYS A 1 427 ? 102.880 127.817 54.214  1.00 75.89  ? 427 LYS A CD  1 
ATOM   2345 C  CE  . LYS A 1 427 ? 102.644 127.924 52.723  1.00 75.89  ? 427 LYS A CE  1 
ATOM   2346 N  NZ  . LYS A 1 427 ? 101.194 128.032 52.411  1.00 75.89  ? 427 LYS A NZ  1 
ATOM   2347 N  N   . SER A 1 428 ? 99.472  126.333 58.427  1.00 73.26  ? 428 SER A N   1 
ATOM   2348 C  CA  . SER A 1 428 ? 98.569  127.216 59.149  1.00 73.26  ? 428 SER A CA  1 
ATOM   2349 C  C   . SER A 1 428 ? 98.118  126.644 60.483  1.00 73.26  ? 428 SER A C   1 
ATOM   2350 O  O   . SER A 1 428 ? 97.063  127.049 60.980  1.00 73.26  ? 428 SER A O   1 
ATOM   2351 C  CB  . SER A 1 428 ? 97.334  127.530 58.294  1.00 73.26  ? 428 SER A CB  1 
ATOM   2352 O  OG  . SER A 1 428 ? 96.431  126.438 58.304  1.00 73.26  ? 428 SER A OG  1 
ATOM   2353 N  N   . SER A 1 429 ? 98.864  125.713 61.070  1.00 64.98  ? 429 SER A N   1 
ATOM   2354 C  CA  . SER A 1 429 ? 98.386  124.980 62.236  1.00 64.98  ? 429 SER A CA  1 
ATOM   2355 C  C   . SER A 1 429 ? 99.598  124.448 62.991  1.00 64.98  ? 429 SER A C   1 
ATOM   2356 O  O   . SER A 1 429 ? 100.146 123.407 62.625  1.00 64.98  ? 429 SER A O   1 
ATOM   2357 C  CB  . SER A 1 429 ? 97.472  123.849 61.804  1.00 64.98  ? 429 SER A CB  1 
ATOM   2358 O  OG  . SER A 1 429 ? 98.246  122.708 61.475  1.00 64.98  ? 429 SER A OG  1 
ATOM   2359 N  N   . VAL A 1 430 ? 99.996  125.153 64.049  1.00 56.08  ? 430 VAL A N   1 
ATOM   2360 C  CA  . VAL A 1 430 ? 101.107 124.693 64.873  1.00 56.08  ? 430 VAL A CA  1 
ATOM   2361 C  C   . VAL A 1 430 ? 100.698 123.544 65.772  1.00 56.08  ? 430 VAL A C   1 
ATOM   2362 O  O   . VAL A 1 430 ? 101.420 122.546 65.855  1.00 56.08  ? 430 VAL A O   1 
ATOM   2363 C  CB  . VAL A 1 430 ? 101.641 125.846 65.735  1.00 56.08  ? 430 VAL A CB  1 
ATOM   2364 C  CG1 . VAL A 1 430 ? 102.602 125.338 66.798  1.00 56.08  ? 430 VAL A CG1 1 
ATOM   2365 C  CG2 . VAL A 1 430 ? 102.276 126.907 64.861  1.00 56.08  ? 430 VAL A CG2 1 
ATOM   2366 N  N   . VAL A 1 431 ? 99.539  123.665 66.424  1.00 57.30  ? 431 VAL A N   1 
ATOM   2367 C  CA  . VAL A 1 431 ? 99.072  122.619 67.336  1.00 57.30  ? 431 VAL A CA  1 
ATOM   2368 C  C   . VAL A 1 431 ? 99.151  121.229 66.714  1.00 57.30  ? 431 VAL A C   1 
ATOM   2369 O  O   . VAL A 1 431 ? 99.527  120.281 67.421  1.00 57.30  ? 431 VAL A O   1 
ATOM   2370 C  CB  . VAL A 1 431 ? 97.661  122.961 67.847  1.00 57.30  ? 431 VAL A CB  1 
ATOM   2371 N  N   . PRO A 1 432 ? 98.818  121.028 65.435  1.00 51.94  ? 432 PRO A N   1 
ATOM   2372 C  CA  . PRO A 1 432 ? 99.043  119.704 64.838  1.00 51.94  ? 432 PRO A CA  1 
ATOM   2373 C  C   . PRO A 1 432 ? 100.506 119.383 64.542  1.00 51.94  ? 432 PRO A C   1 
ATOM   2374 O  O   . PRO A 1 432 ? 100.794 118.225 64.213  1.00 51.94  ? 432 PRO A O   1 
ATOM   2375 C  CB  . PRO A 1 432 ? 98.208  119.752 63.545  1.00 51.94  ? 432 PRO A CB  1 
ATOM   2376 N  N   . CYS A 1 433 ? 101.431 120.344 64.613  1.00 44.13  ? 433 CYS A N   1 
ATOM   2377 C  CA  . CYS A 1 433 ? 102.833 120.098 64.272  1.00 44.13  ? 433 CYS A CA  1 
ATOM   2378 C  C   . CYS A 1 433 ? 102.997 119.413 62.924  1.00 44.13  ? 433 CYS A C   1 
ATOM   2379 O  O   . CYS A 1 433 ? 104.058 118.862 62.642  1.00 44.13  ? 433 CYS A O   1 
ATOM   2380 C  CB  . CYS A 1 433 ? 103.540 119.251 65.338  1.00 44.13  ? 433 CYS A CB  1 
ATOM   2381 S  SG  . CYS A 1 433 ? 104.164 120.094 66.789  1.00 44.13  ? 433 CYS A SG  1 
ATOM   2382 N  N   . GLU A 1 434 ? 101.959 119.406 62.095  1.00 45.65  ? 434 GLU A N   1 
ATOM   2383 C  CA  . GLU A 1 434 ? 101.829 118.498 60.962  1.00 45.65  ? 434 GLU A CA  1 
ATOM   2384 C  C   . GLU A 1 434 ? 101.835 117.049 61.401  1.00 45.65  ? 434 GLU A C   1 
ATOM   2385 O  O   . GLU A 1 434 ? 101.767 116.149 60.561  1.00 45.65  ? 434 GLU A O   1 
ATOM   2386 C  CB  . GLU A 1 434 ? 102.920 118.720 59.913  1.00 45.65  ? 434 GLU A CB  1 
ATOM   2387 C  CG  . GLU A 1 434 ? 102.764 119.986 59.119  1.00 45.65  ? 434 GLU A CG  1 
ATOM   2388 C  CD  . GLU A 1 434 ? 103.588 121.118 59.677  1.00 45.65  ? 434 GLU A CD  1 
ATOM   2389 O  OE1 . GLU A 1 434 ? 104.350 121.732 58.906  1.00 45.65  ? 434 GLU A OE1 1 
ATOM   2390 O  OE2 . GLU A 1 434 ? 103.475 121.397 60.885  1.00 45.65  ? 434 GLU A OE2 1 
ATOM   2391 N  N   . LEU A 1 435 ? 101.910 116.809 62.706  1.00 45.13  ? 435 LEU A N   1 
ATOM   2392 C  CA  . LEU A 1 435 ? 102.150 115.483 63.260  1.00 45.13  ? 435 LEU A CA  1 
ATOM   2393 C  C   . LEU A 1 435 ? 101.743 115.528 64.720  1.00 45.13  ? 435 LEU A C   1 
ATOM   2394 O  O   . LEU A 1 435 ? 102.427 116.162 65.527  1.00 45.13  ? 435 LEU A O   1 
ATOM   2395 C  CB  . LEU A 1 435 ? 103.617 115.112 63.106  1.00 45.13  ? 435 LEU A CB  1 
ATOM   2396 C  CG  . LEU A 1 435 ? 104.047 113.716 63.490  1.00 45.13  ? 435 LEU A CG  1 
ATOM   2397 C  CD1 . LEU A 1 435 ? 102.944 112.758 63.151  1.00 45.13  ? 435 LEU A CD1 1 
ATOM   2398 C  CD2 . LEU A 1 435 ? 105.270 113.393 62.695  1.00 45.13  ? 435 LEU A CD2 1 
ATOM   2399 N  N   . ALA A 1 436 ? 100.640 114.881 65.063  1.00 48.19  ? 436 ALA A N   1 
ATOM   2400 C  CA  . ALA A 1 436 ? 100.057 115.072 66.377  1.00 48.19  ? 436 ALA A CA  1 
ATOM   2401 C  C   . ALA A 1 436 ? 99.157  113.890 66.680  1.00 48.19  ? 436 ALA A C   1 
ATOM   2402 O  O   . ALA A 1 436 ? 99.260  112.832 66.055  1.00 48.19  ? 436 ALA A O   1 
ATOM   2403 C  CB  . ALA A 1 436 ? 99.298  116.399 66.448  1.00 48.19  ? 436 ALA A CB  1 
ATOM   2404 N  N   . CYS A 1 437 ? 98.346  114.013 67.726  1.00 48.93  ? 437 CYS A N   1 
ATOM   2405 C  CA  . CYS A 1 437 ? 97.474  112.885 68.157  1.00 48.93  ? 437 CYS A CA  1 
ATOM   2406 C  C   . CYS A 1 437 ? 96.003  113.206 67.877  1.00 48.93  ? 437 CYS A C   1 
ATOM   2407 O  O   . CYS A 1 437 ? 95.490  112.757 66.834  1.00 48.93  ? 437 CYS A O   1 
ATOM   2408 C  CB  . CYS A 1 437 ? 97.660  112.602 69.644  1.00 48.93  ? 437 CYS A CB  1 
ATOM   2409 S  SG  . CYS A 1 437 ? 97.863  110.845 70.040  1.00 48.93  ? 437 CYS A SG  1 
ATOM   2410 N  N   . ARG A 1 438 ? 95.367  113.950 68.774  1.00 54.94  ? 438 ARG A N   1 
ATOM   2411 C  CA  . ARG A 1 438 ? 93.943  114.347 68.625  1.00 54.94  ? 438 ARG A CA  1 
ATOM   2412 C  C   . ARG A 1 438 ? 93.661  115.512 69.580  1.00 54.94  ? 438 ARG A C   1 
ATOM   2413 O  O   . ARG A 1 438 ? 93.405  116.627 69.085  1.00 54.94  ? 438 ARG A O   1 
ATOM   2414 C  CB  . ARG A 1 438 ? 93.020  113.159 68.914  1.00 54.94  ? 438 ARG A CB  1 
ATOM   2415 N  N   . THR A 1 439 ? 93.692  115.267 70.886  1.00 58.57  ? 439 THR A N   1 
ATOM   2416 C  CA  . THR A 1 439 ? 93.444  116.344 71.882  1.00 58.57  ? 439 THR A CA  1 
ATOM   2417 C  C   . THR A 1 439 ? 94.474  116.260 73.016  1.00 58.57  ? 439 THR A C   1 
ATOM   2418 O  O   . THR A 1 439 ? 95.299  117.188 73.130  1.00 58.57  ? 439 THR A O   1 
ATOM   2419 C  CB  . THR A 1 439 ? 92.002  116.287 72.401  1.00 58.57  ? 439 THR A CB  1 
ATOM   2420 O  OG1 . THR A 1 439 ? 91.742  114.951 72.834  1.00 58.57  ? 439 THR A OG1 1 
ATOM   2421 C  CG2 . THR A 1 439 ? 90.985  116.685 71.354  1.00 58.57  ? 439 THR A CG2 1 
ATOM   2422 N  N   . GLN A 1 440 ? 94.427  115.199 73.818  1.00 53.53  ? 440 GLN A N   1 
ATOM   2423 C  CA  . GLN A 1 440 ? 95.355  115.016 74.968  1.00 53.53  ? 440 GLN A CA  1 
ATOM   2424 C  C   . GLN A 1 440 ? 96.758  114.642 74.475  1.00 53.53  ? 440 GLN A C   1 
ATOM   2425 O  O   . GLN A 1 440 ? 96.869  114.135 73.343  1.00 53.53  ? 440 GLN A O   1 
ATOM   2426 C  CB  . GLN A 1 440 ? 94.830  113.938 75.917  1.00 53.53  ? 440 GLN A CB  1 
ATOM   2427 C  CG  . GLN A 1 440 ? 94.943  112.531 75.349  1.00 53.53  ? 440 GLN A CG  1 
ATOM   2428 C  CD  . GLN A 1 440 ? 94.230  112.390 74.027  1.00 53.53  ? 440 GLN A CD  1 
ATOM   2429 O  OE1 . GLN A 1 440 ? 93.470  113.261 73.614  1.00 53.53  ? 440 GLN A OE1 1 
ATOM   2430 N  NE2 . GLN A 1 440 ? 94.472  111.280 73.349  1.00 53.53  ? 440 GLN A NE2 1 
ATOM   2431 N  N   . CYS A 1 441 ? 97.783  114.912 75.281  1.00 33.42  ? 441 CYS A N   1 
ATOM   2432 C  CA  . CYS A 1 441 ? 99.190  114.575 74.929  1.00 33.42  ? 441 CYS A CA  1 
ATOM   2433 C  C   . CYS A 1 441 ? 100.028 114.508 76.211  1.00 33.42  ? 441 CYS A C   1 
ATOM   2434 O  O   . CYS A 1 441 ? 99.701  113.717 77.096  1.00 33.42  ? 441 CYS A O   1 
ATOM   2435 C  CB  . CYS A 1 441 ? 99.796  115.621 74.002  1.00 33.42  ? 441 CYS A CB  1 
ATOM   2436 S  SG  . CYS A 1 441 ? 100.767 116.873 74.881  1.00 33.42  ? 441 CYS A SG  1 
ATOM   2437 N  N   . ASN B 1 7   ? 92.980  119.775 96.566  1.00 29.28  ? 7   ASN B N   1 
ATOM   2438 C  CA  . ASN B 1 7   ? 92.386  121.052 96.929  1.00 29.28  ? 7   ASN B CA  1 
ATOM   2439 C  C   . ASN B 1 7   ? 93.181  121.773 98.009  1.00 29.28  ? 7   ASN B C   1 
ATOM   2440 O  O   . ASN B 1 7   ? 93.733  121.156 98.900  1.00 29.28  ? 7   ASN B O   1 
ATOM   2441 C  CB  . ASN B 1 7   ? 90.945  120.852 97.389  1.00 29.28  ? 7   ASN B CB  1 
ATOM   2442 C  CG  . ASN B 1 7   ? 89.932  121.261 96.340  1.00 29.28  ? 7   ASN B CG  1 
ATOM   2443 O  OD1 . ASN B 1 7   ? 90.119  122.253 95.638  1.00 29.28  ? 7   ASN B OD1 1 
ATOM   2444 N  ND2 . ASN B 1 7   ? 88.853  120.497 96.223  1.00 29.28  ? 7   ASN B ND2 1 
ATOM   2445 N  N   . ARG B 1 8   ? 93.251  123.097 97.898  1.00 32.72  ? 8   ARG B N   1 
ATOM   2446 C  CA  . ARG B 1 8   ? 93.849  123.902 98.953  1.00 32.72  ? 8   ARG B CA  1 
ATOM   2447 C  C   . ARG B 1 8   ? 92.900  124.049 100.130 1.00 32.72  ? 8   ARG B C   1 
ATOM   2448 O  O   . ARG B 1 8   ? 93.335  124.309 101.257 1.00 32.72  ? 8   ARG B O   1 
ATOM   2449 C  CB  . ARG B 1 8   ? 94.224  125.276 98.407  1.00 32.72  ? 8   ARG B CB  1 
ATOM   2450 C  CG  . ARG B 1 8   ? 95.671  125.437 98.027  1.00 32.72  ? 8   ARG B CG  1 
ATOM   2451 C  CD  . ARG B 1 8   ? 95.928  126.828 97.484  1.00 32.72  ? 8   ARG B CD  1 
ATOM   2452 N  NE  . ARG B 1 8   ? 95.892  127.848 98.525  1.00 32.72  ? 8   ARG B NE  1 
ATOM   2453 C  CZ  . ARG B 1 8   ? 96.965  128.323 99.151  1.00 32.72  ? 8   ARG B CZ  1 
ATOM   2454 N  NH1 . ARG B 1 8   ? 98.172  127.873 98.843  1.00 32.72  ? 8   ARG B NH1 1 
ATOM   2455 N  NH2 . ARG B 1 8   ? 96.833  129.254 100.087 1.00 32.72  ? 8   ARG B NH2 1 
ATOM   2456 N  N   . GLY B 1 9   ? 91.601  123.901 99.889  1.00 32.28  ? 9   GLY B N   1 
ATOM   2457 C  CA  . GLY B 1 9   ? 90.643  124.079 100.963 1.00 32.28  ? 9   GLY B CA  1 
ATOM   2458 C  C   . GLY B 1 9   ? 90.808  123.049 102.058 1.00 32.28  ? 9   GLY B C   1 
ATOM   2459 O  O   . GLY B 1 9   ? 90.716  123.367 103.244 1.00 32.28  ? 9   GLY B O   1 
ATOM   2460 N  N   . ARG B 1 10  ? 91.082  121.808 101.683 1.00 32.41  ? 10  ARG B N   1 
ATOM   2461 C  CA  . ARG B 1 10  ? 91.165  120.763 102.686 1.00 32.41  ? 10  ARG B CA  1 
ATOM   2462 C  C   . ARG B 1 10  ? 92.388  120.935 103.577 1.00 32.41  ? 10  ARG B C   1 
ATOM   2463 O  O   . ARG B 1 10  ? 92.270  120.907 104.807 1.00 32.41  ? 10  ARG B O   1 
ATOM   2464 C  CB  . ARG B 1 10  ? 91.148  119.413 101.998 1.00 32.41  ? 10  ARG B CB  1 
ATOM   2465 C  CG  . ARG B 1 10  ? 89.909  119.272 101.179 1.00 32.41  ? 10  ARG B CG  1 
ATOM   2466 C  CD  . ARG B 1 10  ? 89.776  117.925 100.571 1.00 32.41  ? 10  ARG B CD  1 
ATOM   2467 N  NE  . ARG B 1 10  ? 88.375  117.634 100.337 1.00 32.41  ? 10  ARG B NE  1 
ATOM   2468 C  CZ  . ARG B 1 10  ? 87.935  116.505 99.811  1.00 32.41  ? 10  ARG B CZ  1 
ATOM   2469 N  NH1 . ARG B 1 10  ? 88.792  115.564 99.458  1.00 32.41  ? 10  ARG B NH1 1 
ATOM   2470 N  NH2 . ARG B 1 10  ? 86.640  116.317 99.636  1.00 32.41  ? 10  ARG B NH2 1 
ATOM   2471 N  N   . LEU B 1 11  ? 93.568  121.124 102.985 1.00 32.29  ? 11  LEU B N   1 
ATOM   2472 C  CA  . LEU B 1 11  ? 94.761  121.342 103.796 1.00 32.29  ? 11  LEU B CA  1 
ATOM   2473 C  C   . LEU B 1 11  ? 94.668  122.633 104.596 1.00 32.29  ? 11  LEU B C   1 
ATOM   2474 O  O   . LEU B 1 11  ? 95.204  122.706 105.703 1.00 32.29  ? 11  LEU B O   1 
ATOM   2475 C  CB  . LEU B 1 11  ? 96.006  121.351 102.921 1.00 32.29  ? 11  LEU B CB  1 
ATOM   2476 C  CG  . LEU B 1 11  ? 96.119  120.096 102.070 1.00 32.29  ? 11  LEU B CG  1 
ATOM   2477 C  CD1 . LEU B 1 11  ? 97.381  120.104 101.246 1.00 32.29  ? 11  LEU B CD1 1 
ATOM   2478 C  CD2 . LEU B 1 11  ? 96.066  118.892 102.957 1.00 32.29  ? 11  LEU B CD2 1 
ATOM   2479 N  N   . LEU B 1 12  ? 93.975  123.650 104.078 1.00 31.81  ? 12  LEU B N   1 
ATOM   2480 C  CA  . LEU B 1 12  ? 93.778  124.866 104.858 1.00 31.81  ? 12  LEU B CA  1 
ATOM   2481 C  C   . LEU B 1 12  ? 92.911  124.606 106.079 1.00 31.81  ? 12  LEU B C   1 
ATOM   2482 O  O   . LEU B 1 12  ? 93.256  125.016 107.195 1.00 31.81  ? 12  LEU B O   1 
ATOM   2483 C  CB  . LEU B 1 12  ? 93.162  125.945 103.987 1.00 31.81  ? 12  LEU B CB  1 
ATOM   2484 C  CG  . LEU B 1 12  ? 94.257  126.798 103.392 1.00 31.81  ? 12  LEU B CG  1 
ATOM   2485 C  CD1 . LEU B 1 12  ? 93.661  127.825 102.484 1.00 31.81  ? 12  LEU B CD1 1 
ATOM   2486 C  CD2 . LEU B 1 12  ? 95.022  127.446 104.506 1.00 31.81  ? 12  LEU B CD2 1 
ATOM   2487 N  N   . CYS B 1 13  ? 91.783  123.921 105.895 1.00 35.25  ? 13  CYS B N   1 
ATOM   2488 C  CA  . CYS B 1 13  ? 90.938  123.590 107.035 1.00 35.25  ? 13  CYS B CA  1 
ATOM   2489 C  C   . CYS B 1 13  ? 91.701  122.771 108.064 1.00 35.25  ? 13  CYS B C   1 
ATOM   2490 O  O   . CYS B 1 13  ? 91.619  123.041 109.267 1.00 35.25  ? 13  CYS B O   1 
ATOM   2491 C  CB  . CYS B 1 13  ? 89.704  122.833 106.571 1.00 35.25  ? 13  CYS B CB  1 
ATOM   2492 S  SG  . CYS B 1 13  ? 88.851  121.965 107.890 1.00 35.25  ? 13  CYS B SG  1 
ATOM   2493 N  N   . MET B 1 14  ? 92.469  121.783 107.610 1.00 34.98  ? 14  MET B N   1 
ATOM   2494 C  CA  . MET B 1 14  ? 93.164  120.918 108.557 1.00 34.98  ? 14  MET B CA  1 
ATOM   2495 C  C   . MET B 1 14  ? 94.299  121.650 109.263 1.00 34.98  ? 14  MET B C   1 
ATOM   2496 O  O   . MET B 1 14  ? 94.567  121.399 110.448 1.00 34.98  ? 14  MET B O   1 
ATOM   2497 C  CB  . MET B 1 14  ? 93.684  119.675 107.855 1.00 34.98  ? 14  MET B CB  1 
ATOM   2498 C  CG  . MET B 1 14  ? 94.243  118.669 108.810 1.00 34.98  ? 14  MET B CG  1 
ATOM   2499 S  SD  . MET B 1 14  ? 93.092  118.283 110.118 1.00 34.98  ? 14  MET B SD  1 
ATOM   2500 C  CE  . MET B 1 14  ? 94.191  117.490 111.264 1.00 34.98  ? 14  MET B CE  1 
ATOM   2501 N  N   . LEU B 1 15  ? 94.981  122.559 108.566 1.00 33.61  ? 15  LEU B N   1 
ATOM   2502 C  CA  . LEU B 1 15  ? 95.996  123.373 109.223 1.00 33.61  ? 15  LEU B CA  1 
ATOM   2503 C  C   . LEU B 1 15  ? 95.368  124.240 110.306 1.00 33.61  ? 15  LEU B C   1 
ATOM   2504 O  O   . LEU B 1 15  ? 95.912  124.377 111.414 1.00 33.61  ? 15  LEU B O   1 
ATOM   2505 C  CB  . LEU B 1 15  ? 96.720  124.220 108.185 1.00 33.61  ? 15  LEU B CB  1 
ATOM   2506 C  CG  . LEU B 1 15  ? 97.729  125.195 108.761 1.00 33.61  ? 15  LEU B CG  1 
ATOM   2507 C  CD1 . LEU B 1 15  ? 98.661  124.426 109.628 1.00 33.61  ? 15  LEU B CD1 1 
ATOM   2508 C  CD2 . LEU B 1 15  ? 98.501  125.896 107.667 1.00 33.61  ? 15  LEU B CD2 1 
ATOM   2509 N  N   . ALA B 1 16  ? 94.201  124.810 110.015 1.00 34.62  ? 16  ALA B N   1 
ATOM   2510 C  CA  . ALA B 1 16  ? 93.498  125.583 111.029 1.00 34.62  ? 16  ALA B CA  1 
ATOM   2511 C  C   . ALA B 1 16  ? 93.121  124.716 112.219 1.00 34.62  ? 16  ALA B C   1 
ATOM   2512 O  O   . ALA B 1 16  ? 93.247  125.142 113.374 1.00 34.62  ? 16  ALA B O   1 
ATOM   2513 C  CB  . ALA B 1 16  ? 92.258  126.231 110.433 1.00 34.62  ? 16  ALA B CB  1 
ATOM   2514 N  N   . LEU B 1 17  ? 92.668  123.490 111.967 1.00 35.19  ? 17  LEU B N   1 
ATOM   2515 C  CA  . LEU B 1 17  ? 92.299  122.619 113.080 1.00 35.19  ? 17  LEU B CA  1 
ATOM   2516 C  C   . LEU B 1 17  ? 93.490  122.303 113.976 1.00 35.19  ? 17  LEU B C   1 
ATOM   2517 O  O   . LEU B 1 17  ? 93.373  122.350 115.207 1.00 35.19  ? 17  LEU B O   1 
ATOM   2518 C  CB  . LEU B 1 17  ? 91.685  121.331 112.568 1.00 35.19  ? 17  LEU B CB  1 
ATOM   2519 C  CG  . LEU B 1 17  ? 90.176  121.398 112.632 1.00 35.19  ? 17  LEU B CG  1 
ATOM   2520 C  CD1 . LEU B 1 17  ? 89.588  120.079 112.240 1.00 35.19  ? 17  LEU B CD1 1 
ATOM   2521 C  CD2 . LEU B 1 17  ? 89.760  121.783 114.023 1.00 35.19  ? 17  LEU B CD2 1 
ATOM   2522 N  N   . THR B 1 18  ? 94.642  121.971 113.393 1.00 33.31  ? 18  THR B N   1 
ATOM   2523 C  CA  . THR B 1 18  ? 95.775  121.634 114.249 1.00 33.31  ? 18  THR B CA  1 
ATOM   2524 C  C   . THR B 1 18  ? 96.250  122.839 115.047 1.00 33.31  ? 18  THR B C   1 
ATOM   2525 O  O   . THR B 1 18  ? 96.636  122.692 116.212 1.00 33.31  ? 18  THR B O   1 
ATOM   2526 C  CB  . THR B 1 18  ? 96.922  121.051 113.450 1.00 33.31  ? 18  THR B CB  1 
ATOM   2527 O  OG1 . THR B 1 18  ? 97.513  122.075 112.655 1.00 33.31  ? 18  THR B OG1 1 
ATOM   2528 C  CG2 . THR B 1 18  ? 96.418  119.951 112.573 1.00 33.31  ? 18  THR B CG2 1 
ATOM   2529 N  N   . PHE B 1 19  ? 96.243  124.044 114.461 1.00 38.06  ? 19  PHE B N   1 
ATOM   2530 C  CA  . PHE B 1 19  ? 96.553  125.206 115.297 1.00 38.06  ? 19  PHE B CA  1 
ATOM   2531 C  C   . PHE B 1 19  ? 95.568  125.340 116.447 1.00 38.06  ? 19  PHE B C   1 
ATOM   2532 O  O   . PHE B 1 19  ? 95.963  125.654 117.579 1.00 38.06  ? 19  PHE B O   1 
ATOM   2533 C  CB  . PHE B 1 19  ? 96.582  126.492 114.485 1.00 38.06  ? 19  PHE B CB  1 
ATOM   2534 C  CG  . PHE B 1 19  ? 97.885  126.746 113.817 1.00 38.06  ? 19  PHE B CG  1 
ATOM   2535 C  CD1 . PHE B 1 19  ? 99.009  126.055 114.193 1.00 38.06  ? 19  PHE B CD1 1 
ATOM   2536 C  CD2 . PHE B 1 19  ? 97.997  127.699 112.829 1.00 38.06  ? 19  PHE B CD2 1 
ATOM   2537 C  CE1 . PHE B 1 19  ? 100.219 126.296 113.582 1.00 38.06  ? 19  PHE B CE1 1 
ATOM   2538 C  CE2 . PHE B 1 19  ? 99.205  127.944 112.214 1.00 38.06  ? 19  PHE B CE2 1 
ATOM   2539 C  CZ  . PHE B 1 19  ? 100.316 127.243 112.594 1.00 38.06  ? 19  PHE B CZ  1 
ATOM   2540 N  N   . MET B 1 20  ? 94.283  125.097 116.187 1.00 38.79  ? 20  MET B N   1 
ATOM   2541 C  CA  . MET B 1 20  ? 93.318  125.138 117.278 1.00 38.79  ? 20  MET B CA  1 
ATOM   2542 C  C   . MET B 1 20  ? 93.719  124.180 118.387 1.00 38.79  ? 20  MET B C   1 
ATOM   2543 O  O   . MET B 1 20  ? 93.700  124.541 119.573 1.00 38.79  ? 20  MET B O   1 
ATOM   2544 C  CB  . MET B 1 20  ? 91.919  124.795 116.776 1.00 38.79  ? 20  MET B CB  1 
ATOM   2545 C  CG  . MET B 1 20  ? 90.827  124.953 117.826 1.00 38.79  ? 20  MET B CG  1 
ATOM   2546 S  SD  . MET B 1 20  ? 90.659  123.598 119.019 1.00 38.79  ? 20  MET B SD  1 
ATOM   2547 C  CE  . MET B 1 20  ? 89.904  122.313 118.039 1.00 38.79  ? 20  MET B CE  1 
ATOM   2548 N  N   . PHE B 1 21  ? 94.095  122.956 118.030 1.00 38.10  ? 21  PHE B N   1 
ATOM   2549 C  CA  . PHE B 1 21  ? 94.362  121.988 119.086 1.00 38.10  ? 21  PHE B CA  1 
ATOM   2550 C  C   . PHE B 1 21  ? 95.637  122.321 119.847 1.00 38.10  ? 21  PHE B C   1 
ATOM   2551 O  O   . PHE B 1 21  ? 95.719  122.078 121.054 1.00 38.10  ? 21  PHE B O   1 
ATOM   2552 C  CB  . PHE B 1 21  ? 94.448  120.571 118.557 1.00 38.10  ? 21  PHE B CB  1 
ATOM   2553 C  CG  . PHE B 1 21  ? 94.527  119.561 119.652 1.00 38.10  ? 21  PHE B CG  1 
ATOM   2554 C  CD1 . PHE B 1 21  ? 93.391  119.181 120.334 1.00 38.10  ? 21  PHE B CD1 1 
ATOM   2555 C  CD2 . PHE B 1 21  ? 95.738  119.049 120.057 1.00 38.10  ? 21  PHE B CD2 1 
ATOM   2556 C  CE1 . PHE B 1 21  ? 93.455  118.275 121.363 1.00 38.10  ? 21  PHE B CE1 1 
ATOM   2557 C  CE2 . PHE B 1 21  ? 95.805  118.141 121.093 1.00 38.10  ? 21  PHE B CE2 1 
ATOM   2558 C  CZ  . PHE B 1 21  ? 94.662  117.759 121.742 1.00 38.10  ? 21  PHE B CZ  1 
ATOM   2559 N  N   . MET B 1 22  ? 96.649  122.857 119.173 1.00 40.84  ? 22  MET B N   1 
ATOM   2560 C  CA  . MET B 1 22  ? 97.846  123.256 119.908 1.00 40.84  ? 22  MET B CA  1 
ATOM   2561 C  C   . MET B 1 22  ? 97.530  124.347 120.919 1.00 40.84  ? 22  MET B C   1 
ATOM   2562 O  O   . MET B 1 22  ? 98.060  124.346 122.037 1.00 40.84  ? 22  MET B O   1 
ATOM   2563 C  CB  . MET B 1 22  ? 98.930  123.727 118.953 1.00 40.84  ? 22  MET B CB  1 
ATOM   2564 C  CG  . MET B 1 22  ? 99.829  122.637 118.492 1.00 40.84  ? 22  MET B CG  1 
ATOM   2565 S  SD  . MET B 1 22  ? 100.976 123.233 117.249 1.00 40.84  ? 22  MET B SD  1 
ATOM   2566 C  CE  . MET B 1 22  ? 101.280 124.882 117.868 1.00 40.84  ? 22  MET B CE  1 
ATOM   2567 N  N   . VAL B 1 23  ? 96.673  125.298 120.544 1.00 41.46  ? 23  VAL B N   1 
ATOM   2568 C  CA  . VAL B 1 23  ? 96.300  126.333 121.502 1.00 41.46  ? 23  VAL B CA  1 
ATOM   2569 C  C   . VAL B 1 23  ? 95.564  125.728 122.685 1.00 41.46  ? 23  VAL B C   1 
ATOM   2570 O  O   . VAL B 1 23  ? 95.822  126.085 123.839 1.00 41.46  ? 23  VAL B O   1 
ATOM   2571 C  CB  . VAL B 1 23  ? 95.479  127.435 120.826 1.00 41.46  ? 23  VAL B CB  1 
ATOM   2572 C  CG1 . VAL B 1 23  ? 94.791  128.263 121.871 1.00 41.46  ? 23  VAL B CG1 1 
ATOM   2573 C  CG2 . VAL B 1 23  ? 96.405  128.322 120.014 1.00 41.46  ? 23  VAL B CG2 1 
ATOM   2574 N  N   . LEU B 1 24  ? 94.642  124.798 122.425 1.00 43.66  ? 24  LEU B N   1 
ATOM   2575 C  CA  . LEU B 1 24  ? 93.966  124.129 123.543 1.00 43.66  ? 24  LEU B CA  1 
ATOM   2576 C  C   . LEU B 1 24  ? 94.961  123.412 124.450 1.00 43.66  ? 24  LEU B C   1 
ATOM   2577 O  O   . LEU B 1 24  ? 94.808  123.405 125.680 1.00 43.66  ? 24  LEU B O   1 
ATOM   2578 C  CB  . LEU B 1 24  ? 92.927  123.136 123.041 1.00 43.66  ? 24  LEU B CB  1 
ATOM   2579 C  CG  . LEU B 1 24  ? 92.600  122.051 124.065 1.00 43.66  ? 24  LEU B CG  1 
ATOM   2580 C  CD1 . LEU B 1 24  ? 91.694  122.599 125.126 1.00 43.66  ? 24  LEU B CD1 1 
ATOM   2581 C  CD2 . LEU B 1 24  ? 91.975  120.857 123.409 1.00 43.66  ? 24  LEU B CD2 1 
ATOM   2582 N  N   . GLU B 1 25  ? 95.991  122.812 123.865 1.00 44.80  ? 25  GLU B N   1 
ATOM   2583 C  CA  . GLU B 1 25  ? 96.957  122.091 124.680 1.00 44.80  ? 25  GLU B CA  1 
ATOM   2584 C  C   . GLU B 1 25  ? 97.766  123.037 125.554 1.00 44.80  ? 25  GLU B C   1 
ATOM   2585 O  O   . GLU B 1 25  ? 97.984  122.751 126.734 1.00 44.80  ? 25  GLU B O   1 
ATOM   2586 C  CB  . GLU B 1 25  ? 97.888  121.271 123.807 1.00 44.80  ? 25  GLU B CB  1 
ATOM   2587 C  CG  . GLU B 1 25  ? 98.505  120.126 124.533 1.00 44.80  ? 25  GLU B CG  1 
ATOM   2588 C  CD  . GLU B 1 25  ? 99.359  119.295 123.628 1.00 44.80  ? 25  GLU B CD  1 
ATOM   2589 O  OE1 . GLU B 1 25  ? 100.341 119.835 123.107 1.00 44.80  ? 25  GLU B OE1 1 
ATOM   2590 O  OE2 . GLU B 1 25  ? 99.035  118.117 123.403 1.00 44.80  ? 25  GLU B OE2 1 
ATOM   2591 N  N   . VAL B 1 26  ? 98.241  124.155 125.005 1.00 45.44  ? 26  VAL B N   1 
ATOM   2592 C  CA  . VAL B 1 26  ? 98.953  125.113 125.853 1.00 45.44  ? 26  VAL B CA  1 
ATOM   2593 C  C   . VAL B 1 26  ? 98.037  125.625 126.954 1.00 45.44  ? 26  VAL B C   1 
ATOM   2594 O  O   . VAL B 1 26  ? 98.466  125.818 128.098 1.00 45.44  ? 26  VAL B O   1 
ATOM   2595 C  CB  . VAL B 1 26  ? 99.531  126.273 125.026 1.00 45.44  ? 26  VAL B CB  1 
ATOM   2596 C  CG1 . VAL B 1 26  ? 99.744  127.474 125.908 1.00 45.44  ? 26  VAL B CG1 1 
ATOM   2597 C  CG2 . VAL B 1 26  ? 100.841 125.885 124.423 1.00 45.44  ? 26  VAL B CG2 1 
ATOM   2598 N  N   . VAL B 1 27  ? 96.761  125.845 126.633 1.00 46.08  ? 27  VAL B N   1 
ATOM   2599 C  CA  . VAL B 1 27  ? 95.812  126.332 127.632 1.00 46.08  ? 27  VAL B CA  1 
ATOM   2600 C  C   . VAL B 1 27  ? 95.690  125.348 128.786 1.00 46.08  ? 27  VAL B C   1 
ATOM   2601 O  O   . VAL B 1 27  ? 95.722  125.739 129.956 1.00 46.08  ? 27  VAL B O   1 
ATOM   2602 C  CB  . VAL B 1 27  ? 94.446  126.612 126.990 1.00 46.08  ? 27  VAL B CB  1 
ATOM   2603 C  CG1 . VAL B 1 27  ? 93.342  126.504 128.022 1.00 46.08  ? 27  VAL B CG1 1 
ATOM   2604 C  CG2 . VAL B 1 27  ? 94.454  127.988 126.364 1.00 46.08  ? 27  VAL B CG2 1 
ATOM   2605 N  N   . VAL B 1 28  ? 95.546  124.059 128.485 1.00 47.14  ? 28  VAL B N   1 
ATOM   2606 C  CA  . VAL B 1 28  ? 95.459  123.095 129.580 1.00 47.14  ? 28  VAL B CA  1 
ATOM   2607 C  C   . VAL B 1 28  ? 96.780  123.024 130.340 1.00 47.14  ? 28  VAL B C   1 
ATOM   2608 O  O   . VAL B 1 28  ? 96.800  122.975 131.576 1.00 47.14  ? 28  VAL B O   1 
ATOM   2609 C  CB  . VAL B 1 28  ? 95.019  121.715 129.068 1.00 47.14  ? 28  VAL B CB  1 
ATOM   2610 C  CG1 . VAL B 1 28  ? 95.452  120.647 130.022 1.00 47.14  ? 28  VAL B CG1 1 
ATOM   2611 C  CG2 . VAL B 1 28  ? 93.525  121.671 128.948 1.00 47.14  ? 28  VAL B CG2 1 
ATOM   2612 N  N   . SER B 1 29  ? 97.903  123.047 129.623 1.00 50.53  ? 29  SER B N   1 
ATOM   2613 C  CA  . SER B 1 29  ? 99.199  122.919 130.278 1.00 50.53  ? 29  SER B CA  1 
ATOM   2614 C  C   . SER B 1 29  ? 99.450  124.066 131.237 1.00 50.53  ? 29  SER B C   1 
ATOM   2615 O  O   . SER B 1 29  ? 100.174 123.917 132.223 1.00 50.53  ? 29  SER B O   1 
ATOM   2616 C  CB  . SER B 1 29  ? 100.312 122.857 129.240 1.00 50.53  ? 29  SER B CB  1 
ATOM   2617 O  OG  . SER B 1 29  ? 100.485 121.539 128.759 1.00 50.53  ? 29  SER B OG  1 
ATOM   2618 N  N   . ARG B 1 30  ? 98.885  125.228 130.945 1.00 51.47  ? 30  ARG B N   1 
ATOM   2619 C  CA  . ARG B 1 30  ? 99.092  126.399 131.841 1.00 51.47  ? 30  ARG B CA  1 
ATOM   2620 C  C   . ARG B 1 30  ? 98.026  126.391 132.940 1.00 51.47  ? 30  ARG B C   1 
ATOM   2621 O  O   . ARG B 1 30  ? 98.352  126.813 134.061 1.00 51.47  ? 30  ARG B O   1 
ATOM   2622 C  CB  . ARG B 1 30  ? 99.099  127.715 131.056 1.00 51.47  ? 30  ARG B CB  1 
ATOM   2623 C  CG  . ARG B 1 30  ? 100.098 128.733 131.585 1.00 51.47  ? 30  ARG B CG  1 
ATOM   2624 C  CD  . ARG B 1 30  ? 101.302 128.884 130.675 1.00 51.47  ? 30  ARG B CD  1 
ATOM   2625 N  NE  . ARG B 1 30  ? 101.234 130.106 129.887 1.00 51.47  ? 30  ARG B NE  1 
ATOM   2626 C  CZ  . ARG B 1 30  ? 102.113 130.450 128.955 1.00 51.47  ? 30  ARG B CZ  1 
ATOM   2627 N  NH1 . ARG B 1 30  ? 102.717 129.518 128.239 1.00 51.47  ? 30  ARG B NH1 1 
ATOM   2628 N  NH2 . ARG B 1 30  ? 102.384 131.724 128.740 1.00 51.47  ? 30  ARG B NH2 1 
ATOM   2629 N  N   . VAL B 1 31  ? 96.810  125.944 132.653 1.00 52.83  ? 31  VAL B N   1 
ATOM   2630 C  CA  . VAL B 1 31  ? 95.802  125.904 133.707 1.00 52.83  ? 31  VAL B CA  1 
ATOM   2631 C  C   . VAL B 1 31  ? 96.210  124.919 134.792 1.00 52.83  ? 31  VAL B C   1 
ATOM   2632 O  O   . VAL B 1 31  ? 96.291  125.270 135.974 1.00 52.83  ? 31  VAL B O   1 
ATOM   2633 C  CB  . VAL B 1 31  ? 94.424  125.553 133.127 1.00 52.83  ? 31  VAL B CB  1 
ATOM   2634 C  CG1 . VAL B 1 31  ? 93.529  124.986 134.205 1.00 52.83  ? 31  VAL B CG1 1 
ATOM   2635 C  CG2 . VAL B 1 31  ? 93.790  126.778 132.532 1.00 52.83  ? 31  VAL B CG2 1 
ATOM   2636 N  N   . THR B 1 32  ? 96.482  123.671 134.409 1.00 53.91  ? 32  THR B N   1 
ATOM   2637 C  CA  . THR B 1 32  ? 96.844  122.636 135.369 1.00 53.91  ? 32  THR B CA  1 
ATOM   2638 C  C   . THR B 1 32  ? 98.153  122.931 136.093 1.00 53.91  ? 32  THR B C   1 
ATOM   2639 O  O   . THR B 1 32  ? 98.374  122.400 137.187 1.00 53.91  ? 32  THR B O   1 
ATOM   2640 C  CB  . THR B 1 32  ? 96.906  121.297 134.630 1.00 53.91  ? 32  THR B CB  1 
ATOM   2641 O  OG1 . THR B 1 32  ? 95.591  120.941 134.198 1.00 53.91  ? 32  THR B OG1 1 
ATOM   2642 C  CG2 . THR B 1 32  ? 97.437  120.195 135.498 1.00 53.91  ? 32  THR B CG2 1 
ATOM   2643 N  N   . SER B 1 33  ? 98.990  123.806 135.542 1.00 57.73  ? 33  SER B N   1 
ATOM   2644 C  CA  . SER B 1 33  ? 100.321 124.101 136.069 1.00 57.73  ? 33  SER B CA  1 
ATOM   2645 C  C   . SER B 1 33  ? 101.172 122.834 136.106 1.00 57.73  ? 33  SER B C   1 
ATOM   2646 O  O   . SER B 1 33  ? 101.715 122.436 137.136 1.00 57.73  ? 33  SER B O   1 
ATOM   2647 C  CB  . SER B 1 33  ? 100.240 124.762 137.446 1.00 57.73  ? 33  SER B CB  1 
ATOM   2648 O  OG  . SER B 1 33  ? 100.025 126.155 137.320 1.00 57.73  ? 33  SER B OG  1 
ATOM   2649 N  N   . SER B 1 34  ? 101.285 122.207 134.937 1.00 57.42  ? 34  SER B N   1 
ATOM   2650 C  CA  . SER B 1 34  ? 102.026 120.959 134.777 1.00 57.42  ? 34  SER B CA  1 
ATOM   2651 C  C   . SER B 1 34  ? 102.976 121.135 133.598 1.00 57.42  ? 34  SER B C   1 
ATOM   2652 O  O   . SER B 1 34  ? 102.638 120.780 132.467 1.00 57.42  ? 34  SER B O   1 
ATOM   2653 C  CB  . SER B 1 34  ? 101.083 119.785 134.558 1.00 57.42  ? 34  SER B CB  1 
ATOM   2654 O  OG  . SER B 1 34  ? 100.720 119.671 133.198 1.00 57.42  ? 34  SER B OG  1 
ATOM   2655 N  N   . LEU B 1 35  ? 104.174 121.652 133.872 1.00 59.95  ? 35  LEU B N   1 
ATOM   2656 C  CA  . LEU B 1 35  ? 105.155 121.922 132.828 1.00 59.95  ? 35  LEU B CA  1 
ATOM   2657 C  C   . LEU B 1 35  ? 105.639 120.670 132.126 1.00 59.95  ? 35  LEU B C   1 
ATOM   2658 O  O   . LEU B 1 35  ? 106.485 120.774 131.236 1.00 59.95  ? 35  LEU B O   1 
ATOM   2659 C  CB  . LEU B 1 35  ? 106.363 122.653 133.402 1.00 59.95  ? 35  LEU B CB  1 
ATOM   2660 C  CG  . LEU B 1 35  ? 106.322 124.181 133.433 1.00 59.95  ? 35  LEU B CG  1 
ATOM   2661 C  CD1 . LEU B 1 35  ? 107.710 124.728 133.720 1.00 59.95  ? 35  LEU B CD1 1 
ATOM   2662 C  CD2 . LEU B 1 35  ? 105.762 124.763 132.140 1.00 59.95  ? 35  LEU B CD2 1 
ATOM   2663 N  N   . ALA B 1 36  ? 105.162 119.496 132.519 1.00 59.71  ? 36  ALA B N   1 
ATOM   2664 C  CA  . ALA B 1 36  ? 105.523 118.285 131.799 1.00 59.71  ? 36  ALA B CA  1 
ATOM   2665 C  C   . ALA B 1 36  ? 104.582 118.021 130.636 1.00 59.71  ? 36  ALA B C   1 
ATOM   2666 O  O   . ALA B 1 36  ? 104.829 117.113 129.839 1.00 59.71  ? 36  ALA B O   1 
ATOM   2667 C  CB  . ALA B 1 36  ? 105.539 117.090 132.751 1.00 59.71  ? 36  ALA B CB  1 
ATOM   2668 N  N   . MET B 1 37  ? 103.497 118.781 130.535 1.00 53.66  ? 37  MET B N   1 
ATOM   2669 C  CA  . MET B 1 37  ? 102.553 118.614 129.441 1.00 53.66  ? 37  MET B CA  1 
ATOM   2670 C  C   . MET B 1 37  ? 102.690 119.686 128.368 1.00 53.66  ? 37  MET B C   1 
ATOM   2671 O  O   . MET B 1 37  ? 102.328 119.438 127.217 1.00 53.66  ? 37  MET B O   1 
ATOM   2672 C  CB  . MET B 1 37  ? 101.128 118.606 129.983 1.00 53.66  ? 37  MET B CB  1 
ATOM   2673 C  CG  . MET B 1 37  ? 100.083 118.327 128.934 1.00 53.66  ? 37  MET B CG  1 
ATOM   2674 S  SD  . MET B 1 37  ? 98.431  118.181 129.609 1.00 53.66  ? 37  MET B SD  1 
ATOM   2675 C  CE  . MET B 1 37  ? 97.507  118.487 128.126 1.00 53.66  ? 37  MET B CE  1 
ATOM   2676 N  N   . LEU B 1 38  ? 103.202 120.867 128.710 1.00 55.60  ? 38  LEU B N   1 
ATOM   2677 C  CA  . LEU B 1 38  ? 103.537 121.871 127.710 1.00 55.60  ? 38  LEU B CA  1 
ATOM   2678 C  C   . LEU B 1 38  ? 104.540 121.358 126.686 1.00 55.60  ? 38  LEU B C   1 
ATOM   2679 O  O   . LEU B 1 38  ? 104.742 122.012 125.664 1.00 55.60  ? 38  LEU B O   1 
ATOM   2680 C  CB  . LEU B 1 38  ? 104.091 123.114 128.405 1.00 55.60  ? 38  LEU B CB  1 
ATOM   2681 C  CG  . LEU B 1 38  ? 104.326 124.430 127.670 1.00 55.60  ? 38  LEU B CG  1 
ATOM   2682 C  CD1 . LEU B 1 38  ? 104.101 125.575 128.625 1.00 55.60  ? 38  LEU B CD1 1 
ATOM   2683 C  CD2 . LEU B 1 38  ? 105.725 124.506 127.120 1.00 55.60  ? 38  LEU B CD2 1 
ATOM   2684 N  N   . SER B 1 39  ? 105.158 120.203 126.927 1.00 53.37  ? 39  SER B N   1 
ATOM   2685 C  CA  . SER B 1 39  ? 106.102 119.608 125.994 1.00 53.37  ? 39  SER B CA  1 
ATOM   2686 C  C   . SER B 1 39  ? 105.440 118.699 124.975 1.00 53.37  ? 39  SER B C   1 
ATOM   2687 O  O   . SER B 1 39  ? 106.076 117.744 124.524 1.00 53.37  ? 39  SER B O   1 
ATOM   2688 C  CB  . SER B 1 39  ? 107.172 118.841 126.759 1.00 53.37  ? 39  SER B CB  1 
ATOM   2689 O  OG  . SER B 1 39  ? 107.896 119.719 127.599 1.00 53.37  ? 39  SER B OG  1 
ATOM   2690 N  N   . ASP B 1 40  ? 104.177 118.943 124.639 1.00 50.85  ? 40  ASP B N   1 
ATOM   2691 C  CA  . ASP B 1 40  ? 103.542 118.408 123.441 1.00 50.85  ? 40  ASP B CA  1 
ATOM   2692 C  C   . ASP B 1 40  ? 103.045 119.501 122.498 1.00 50.85  ? 40  ASP B C   1 
ATOM   2693 O  O   . ASP B 1 40  ? 102.927 119.270 121.283 1.00 50.85  ? 40  ASP B O   1 
ATOM   2694 C  CB  . ASP B 1 40  ? 102.371 117.494 123.826 1.00 50.85  ? 40  ASP B CB  1 
ATOM   2695 C  CG  . ASP B 1 40  ? 102.789 116.380 124.776 1.00 50.85  ? 40  ASP B CG  1 
ATOM   2696 O  OD1 . ASP B 1 40  ? 104.003 116.149 124.925 1.00 50.85  ? 40  ASP B OD1 1 
ATOM   2697 O  OD2 . ASP B 1 40  ? 101.903 115.739 125.385 1.00 50.85  ? 40  ASP B OD2 1 
ATOM   2698 N  N   . SER B 1 41  ? 102.740 120.683 123.031 1.00 49.13  ? 41  SER B N   1 
ATOM   2699 C  CA  . SER B 1 41  ? 102.412 121.824 122.191 1.00 49.13  ? 41  SER B CA  1 
ATOM   2700 C  C   . SER B 1 41  ? 103.618 122.325 121.424 1.00 49.13  ? 41  SER B C   1 
ATOM   2701 O  O   . SER B 1 41  ? 103.498 123.254 120.624 1.00 49.13  ? 41  SER B O   1 
ATOM   2702 C  CB  . SER B 1 41  ? 101.841 122.943 123.038 1.00 49.13  ? 41  SER B CB  1 
ATOM   2703 O  OG  . SER B 1 41  ? 102.837 123.470 123.887 1.00 49.13  ? 41  SER B OG  1 
ATOM   2704 N  N   . PHE B 1 42  ? 104.791 121.789 121.700 1.00 46.08  ? 42  PHE B N   1 
ATOM   2705 C  CA  . PHE B 1 42  ? 105.927 121.998 120.831 1.00 46.08  ? 42  PHE B CA  1 
ATOM   2706 C  C   . PHE B 1 42  ? 106.163 120.807 119.919 1.00 46.08  ? 42  PHE B C   1 
ATOM   2707 O  O   . PHE B 1 42  ? 106.923 120.921 118.958 1.00 46.08  ? 42  PHE B O   1 
ATOM   2708 C  CB  . PHE B 1 42  ? 107.179 122.297 121.658 1.00 46.08  ? 42  PHE B CB  1 
ATOM   2709 C  CG  . PHE B 1 42  ? 107.194 123.675 122.260 1.00 46.08  ? 42  PHE B CG  1 
ATOM   2710 C  CD1 . PHE B 1 42  ? 107.542 123.864 123.584 1.00 46.08  ? 42  PHE B CD1 1 
ATOM   2711 C  CD2 . PHE B 1 42  ? 106.839 124.780 121.503 1.00 46.08  ? 42  PHE B CD2 1 
ATOM   2712 C  CE1 . PHE B 1 42  ? 107.545 125.130 124.140 1.00 46.08  ? 42  PHE B CE1 1 
ATOM   2713 C  CE2 . PHE B 1 42  ? 106.844 126.051 122.056 1.00 46.08  ? 42  PHE B CE2 1 
ATOM   2714 C  CZ  . PHE B 1 42  ? 107.194 126.224 123.376 1.00 46.08  ? 42  PHE B CZ  1 
ATOM   2715 N  N   . HIS B 1 43  ? 105.523 119.675 120.192 1.00 43.49  ? 43  HIS B N   1 
ATOM   2716 C  CA  . HIS B 1 43  ? 105.676 118.481 119.375 1.00 43.49  ? 43  HIS B CA  1 
ATOM   2717 C  C   . HIS B 1 43  ? 104.630 118.386 118.274 1.00 43.49  ? 43  HIS B C   1 
ATOM   2718 O  O   . HIS B 1 43  ? 104.715 117.495 117.424 1.00 43.49  ? 43  HIS B O   1 
ATOM   2719 C  CB  . HIS B 1 43  ? 105.599 117.228 120.248 1.00 43.49  ? 43  HIS B CB  1 
ATOM   2720 C  CG  . HIS B 1 43  ? 106.840 116.955 121.040 1.00 43.49  ? 43  HIS B CG  1 
ATOM   2721 N  ND1 . HIS B 1 43  ? 106.973 115.849 121.851 1.00 43.49  ? 43  HIS B ND1 1 
ATOM   2722 C  CD2 . HIS B 1 43  ? 108.000 117.643 121.148 1.00 43.49  ? 43  HIS B CD2 1 
ATOM   2723 C  CE1 . HIS B 1 43  ? 108.161 115.868 122.427 1.00 43.49  ? 43  HIS B CE1 1 
ATOM   2724 N  NE2 . HIS B 1 43  ? 108.804 116.946 122.019 1.00 43.49  ? 43  HIS B NE2 1 
ATOM   2725 N  N   . MET B 1 44  ? 103.606 119.238 118.310 1.00 41.71  ? 44  MET B N   1 
ATOM   2726 C  CA  . MET B 1 44  ? 102.673 119.295 117.179 1.00 41.71  ? 44  MET B CA  1 
ATOM   2727 C  C   . MET B 1 44  ? 103.160 120.215 116.045 1.00 41.71  ? 44  MET B C   1 
ATOM   2728 O  O   . MET B 1 44  ? 102.593 120.204 114.936 1.00 41.71  ? 44  MET B O   1 
ATOM   2729 C  CB  . MET B 1 44  ? 101.295 119.714 117.679 1.00 41.71  ? 44  MET B CB  1 
ATOM   2730 C  CG  . MET B 1 44  ? 100.172 119.478 116.702 1.00 41.71  ? 44  MET B CG  1 
ATOM   2731 S  SD  . MET B 1 44  ? 98.546  119.513 117.466 1.00 41.71  ? 44  MET B SD  1 
ATOM   2732 C  CE  . MET B 1 44  ? 98.468  117.873 118.151 1.00 41.71  ? 44  MET B CE  1 
ATOM   2733 N  N   . LEU B 1 45  ? 104.212 120.996 116.282 1.00 38.90  ? 45  LEU B N   1 
ATOM   2734 C  CA  . LEU B 1 45  ? 104.903 121.685 115.202 1.00 38.90  ? 45  LEU B CA  1 
ATOM   2735 C  C   . LEU B 1 45  ? 105.605 120.732 114.253 1.00 38.90  ? 45  LEU B C   1 
ATOM   2736 O  O   . LEU B 1 45  ? 106.331 121.193 113.370 1.00 38.90  ? 45  LEU B O   1 
ATOM   2737 C  CB  . LEU B 1 45  ? 105.923 122.656 115.765 1.00 38.90  ? 45  LEU B CB  1 
ATOM   2738 C  CG  . LEU B 1 45  ? 105.336 123.935 116.323 1.00 38.90  ? 45  LEU B CG  1 
ATOM   2739 C  CD1 . LEU B 1 45  ? 106.377 124.669 117.142 1.00 38.90  ? 45  LEU B CD1 1 
ATOM   2740 C  CD2 . LEU B 1 45  ? 104.859 124.787 115.175 1.00 38.90  ? 45  LEU B CD2 1 
ATOM   2741 N  N   . SER B 1 46  ? 105.466 119.427 114.454 1.00 36.74  ? 46  SER B N   1 
ATOM   2742 C  CA  . SER B 1 46  ? 105.924 118.432 113.501 1.00 36.74  ? 46  SER B CA  1 
ATOM   2743 C  C   . SER B 1 46  ? 104.783 117.853 112.689 1.00 36.74  ? 46  SER B C   1 
ATOM   2744 O  O   . SER B 1 46  ? 105.028 117.122 111.727 1.00 36.74  ? 46  SER B O   1 
ATOM   2745 C  CB  . SER B 1 46  ? 106.657 117.306 114.228 1.00 36.74  ? 46  SER B CB  1 
ATOM   2746 O  OG  . SER B 1 46  ? 105.796 116.622 115.117 1.00 36.74  ? 46  SER B OG  1 
ATOM   2747 N  N   . ASP B 1 47  ? 103.550 118.135 113.083 1.00 38.96  ? 47  ASP B N   1 
ATOM   2748 C  CA  . ASP B 1 47  ? 102.372 117.808 112.299 1.00 38.96  ? 47  ASP B CA  1 
ATOM   2749 C  C   . ASP B 1 47  ? 101.895 118.984 111.473 1.00 38.96  ? 47  ASP B C   1 
ATOM   2750 O  O   . ASP B 1 47  ? 101.131 118.788 110.528 1.00 38.96  ? 47  ASP B O   1 
ATOM   2751 C  CB  . ASP B 1 47  ? 101.241 117.347 113.222 1.00 38.96  ? 47  ASP B CB  1 
ATOM   2752 C  CG  . ASP B 1 47  ? 100.188 116.549 112.502 1.00 38.96  ? 47  ASP B CG  1 
ATOM   2753 O  OD1 . ASP B 1 47  ? 100.371 116.284 111.300 1.00 38.96  ? 47  ASP B OD1 1 
ATOM   2754 O  OD2 . ASP B 1 47  ? 99.183  116.177 113.140 1.00 38.96  ? 47  ASP B OD2 1 
ATOM   2755 N  N   . VAL B 1 48  ? 102.281 120.205 111.839 1.00 30.94  ? 48  VAL B N   1 
ATOM   2756 C  CA  . VAL B 1 48  ? 101.978 121.336 110.957 1.00 30.94  ? 48  VAL B CA  1 
ATOM   2757 C  C   . VAL B 1 48  ? 102.939 121.403 109.764 1.00 30.94  ? 48  VAL B C   1 
ATOM   2758 O  O   . VAL B 1 48  ? 102.598 121.961 108.713 1.00 30.94  ? 48  VAL B O   1 
ATOM   2759 C  CB  . VAL B 1 48  ? 101.958 122.643 111.761 1.00 30.94  ? 48  VAL B CB  1 
ATOM   2760 C  CG1 . VAL B 1 48  ? 102.207 123.845 110.878 1.00 30.94  ? 48  VAL B CG1 1 
ATOM   2761 C  CG2 . VAL B 1 48  ? 100.621 122.784 112.433 1.00 30.94  ? 48  VAL B CG2 1 
ATOM   2762 N  N   . LEU B 1 49  ? 104.128 120.816 109.875 1.00 26.79  ? 49  LEU B N   1 
ATOM   2763 C  CA  . LEU B 1 49  ? 105.078 120.885 108.768 1.00 26.79  ? 49  LEU B CA  1 
ATOM   2764 C  C   . LEU B 1 49  ? 104.634 120.051 107.572 1.00 26.79  ? 49  LEU B C   1 
ATOM   2765 O  O   . LEU B 1 49  ? 104.807 120.467 106.422 1.00 26.79  ? 49  LEU B O   1 
ATOM   2766 C  CB  . LEU B 1 49  ? 106.448 120.429 109.230 1.00 26.79  ? 49  LEU B CB  1 
ATOM   2767 C  CG  . LEU B 1 49  ? 107.399 121.575 109.482 1.00 26.79  ? 49  LEU B CG  1 
ATOM   2768 C  CD1 . LEU B 1 49  ? 108.751 121.023 109.851 1.00 26.79  ? 49  LEU B CD1 1 
ATOM   2769 C  CD2 . LEU B 1 49  ? 107.483 122.401 108.230 1.00 26.79  ? 49  LEU B CD2 1 
ATOM   2770 N  N   . ALA B 1 50  ? 104.091 118.863 107.807 1.00 24.10  ? 50  ALA B N   1 
ATOM   2771 C  CA  . ALA B 1 50  ? 103.697 118.028 106.683 1.00 24.10  ? 50  ALA B CA  1 
ATOM   2772 C  C   . ALA B 1 50  ? 102.467 118.566 105.985 1.00 24.10  ? 50  ALA B C   1 
ATOM   2773 O  O   . ALA B 1 50  ? 102.115 118.081 104.910 1.00 24.10  ? 50  ALA B O   1 
ATOM   2774 C  CB  . ALA B 1 50  ? 103.438 116.604 107.132 1.00 24.10  ? 50  ALA B CB  1 
ATOM   2775 N  N   . LEU B 1 51  ? 101.763 119.516 106.594 1.00 20.26  ? 51  LEU B N   1 
ATOM   2776 C  CA  . LEU B 1 51  ? 100.697 120.194 105.871 1.00 20.26  ? 51  LEU B CA  1 
ATOM   2777 C  C   . LEU B 1 51  ? 101.217 121.435 105.160 1.00 20.26  ? 51  LEU B C   1 
ATOM   2778 O  O   . LEU B 1 51  ? 100.805 121.720 104.036 1.00 20.26  ? 51  LEU B O   1 
ATOM   2779 C  CB  . LEU B 1 51  ? 99.547  120.550 106.806 1.00 20.26  ? 51  LEU B CB  1 
ATOM   2780 C  CG  . LEU B 1 51  ? 98.988  119.444 107.696 1.00 20.26  ? 51  LEU B CG  1 
ATOM   2781 C  CD1 . LEU B 1 51  ? 97.697  119.890 108.291 1.00 20.26  ? 51  LEU B CD1 1 
ATOM   2782 C  CD2 . LEU B 1 51  ? 98.782  118.172 106.945 1.00 20.26  ? 51  LEU B CD2 1 
ATOM   2783 N  N   . VAL B 1 52  ? 102.135 122.174 105.779 1.00 23.41  ? 52  VAL B N   1 
ATOM   2784 C  CA  . VAL B 1 52  ? 102.725 123.306 105.071 1.00 23.41  ? 52  VAL B CA  1 
ATOM   2785 C  C   . VAL B 1 52  ? 103.421 122.863 103.793 1.00 23.41  ? 52  VAL B C   1 
ATOM   2786 O  O   . VAL B 1 52  ? 103.327 123.547 102.771 1.00 23.41  ? 52  VAL B O   1 
ATOM   2787 C  CB  . VAL B 1 52  ? 103.695 124.075 105.979 1.00 23.41  ? 52  VAL B CB  1 
ATOM   2788 C  CG1 . VAL B 1 52  ? 104.657 124.893 105.150 1.00 23.41  ? 52  VAL B CG1 1 
ATOM   2789 C  CG2 . VAL B 1 52  ? 102.927 124.980 106.911 1.00 23.41  ? 52  VAL B CG2 1 
ATOM   2790 N  N   . VAL B 1 53  ? 104.114 121.723 103.804 1.00 22.08  ? 53  VAL B N   1 
ATOM   2791 C  CA  . VAL B 1 53  ? 104.815 121.285 102.596 1.00 22.08  ? 53  VAL B CA  1 
ATOM   2792 C  C   . VAL B 1 53  ? 103.824 120.866 101.514 1.00 22.08  ? 53  VAL B C   1 
ATOM   2793 O  O   . VAL B 1 53  ? 103.910 121.313 100.365 1.00 22.08  ? 53  VAL B O   1 
ATOM   2794 C  CB  . VAL B 1 53  ? 105.809 120.160 102.912 1.00 22.08  ? 53  VAL B CB  1 
ATOM   2795 C  CG1 . VAL B 1 53  ? 106.127 119.414 101.657 1.00 22.08  ? 53  VAL B CG1 1 
ATOM   2796 C  CG2 . VAL B 1 53  ? 107.068 120.733 103.496 1.00 22.08  ? 53  VAL B CG2 1 
ATOM   2797 N  N   . ALA B 1 54  ? 102.872 120.006 101.850 1.00 24.03  ? 54  ALA B N   1 
ATOM   2798 C  CA  . ALA B 1 54  ? 101.907 119.629 100.831 1.00 24.03  ? 54  ALA B CA  1 
ATOM   2799 C  C   . ALA B 1 54  ? 100.965 120.749 100.473 1.00 24.03  ? 54  ALA B C   1 
ATOM   2800 O  O   . ALA B 1 54  ? 100.127 120.557 99.595  1.00 24.03  ? 54  ALA B O   1 
ATOM   2801 C  CB  . ALA B 1 54  ? 101.088 118.433 101.271 1.00 24.03  ? 54  ALA B CB  1 
ATOM   2802 N  N   . LEU B 1 55  ? 101.039 121.885 101.154 1.00 25.55  ? 55  LEU B N   1 
ATOM   2803 C  CA  . LEU B 1 55  ? 100.335 123.082 100.716 1.00 25.55  ? 55  LEU B CA  1 
ATOM   2804 C  C   . LEU B 1 55  ? 101.180 123.895 99.743  1.00 25.55  ? 55  LEU B C   1 
ATOM   2805 O  O   . LEU B 1 55  ? 100.664 124.429 98.761  1.00 25.55  ? 55  LEU B O   1 
ATOM   2806 C  CB  . LEU B 1 55  ? 99.963  123.929 101.930 1.00 25.55  ? 55  LEU B CB  1 
ATOM   2807 C  CG  . LEU B 1 55  ? 98.973  125.050 101.698 1.00 25.55  ? 55  LEU B CG  1 
ATOM   2808 C  CD1 . LEU B 1 55  ? 97.691  124.427 101.253 1.00 25.55  ? 55  LEU B CD1 1 
ATOM   2809 C  CD2 . LEU B 1 55  ? 98.784  125.826 102.972 1.00 25.55  ? 55  LEU B CD2 1 
ATOM   2810 N  N   . VAL B 1 56  ? 102.481 124.002 100.014 1.00 19.31  ? 56  VAL B N   1 
ATOM   2811 C  CA  . VAL B 1 56  ? 103.390 124.671 99.099  1.00 19.31  ? 56  VAL B CA  1 
ATOM   2812 C  C   . VAL B 1 56  ? 103.455 123.950 97.774  1.00 19.31  ? 56  VAL B C   1 
ATOM   2813 O  O   . VAL B 1 56  ? 103.584 124.590 96.735  1.00 19.31  ? 56  VAL B O   1 
ATOM   2814 C  CB  . VAL B 1 56  ? 104.788 124.787 99.722  1.00 19.31  ? 56  VAL B CB  1 
ATOM   2815 C  CG1 . VAL B 1 56  ? 105.792 125.143 98.681  1.00 19.31  ? 56  VAL B CG1 1 
ATOM   2816 C  CG2 . VAL B 1 56  ? 104.794 125.830 100.809 1.00 19.31  ? 56  VAL B CG2 1 
ATOM   2817 N  N   . ALA B 1 57  ? 103.340 122.632 97.772  1.00 22.48  ? 57  ALA B N   1 
ATOM   2818 C  CA  . ALA B 1 57  ? 103.337 121.896 96.516  1.00 22.48  ? 57  ALA B CA  1 
ATOM   2819 C  C   . ALA B 1 57  ? 101.959 121.790 95.883  1.00 22.48  ? 57  ALA B C   1 
ATOM   2820 O  O   . ALA B 1 57  ? 101.716 120.856 95.122  1.00 22.48  ? 57  ALA B O   1 
ATOM   2821 C  CB  . ALA B 1 57  ? 103.915 120.499 96.718  1.00 22.48  ? 57  ALA B CB  1 
ATOM   2822 N  N   . GLU B 1 58  ? 101.079 122.737 96.193  1.00 25.16  ? 58  GLU B N   1 
ATOM   2823 C  CA  . GLU B 1 58  ? 99.714  122.780 95.605  1.00 25.16  ? 58  GLU B CA  1 
ATOM   2824 C  C   . GLU B 1 58  ? 99.655  123.981 94.658  1.00 25.16  ? 58  GLU B C   1 
ATOM   2825 O  O   . GLU B 1 58  ? 98.995  123.875 93.614  1.00 25.16  ? 58  GLU B O   1 
ATOM   2826 C  CB  . GLU B 1 58  ? 98.641  122.833 96.691  1.00 25.16  ? 58  GLU B CB  1 
ATOM   2827 C  CG  . GLU B 1 58  ? 97.534  121.816 96.485  1.00 25.16  ? 58  GLU B CG  1 
ATOM   2828 C  CD  . GLU B 1 58  ? 97.993  120.416 96.115  1.00 25.16  ? 58  GLU B CD  1 
ATOM   2829 O  OE1 . GLU B 1 58  ? 98.790  120.284 95.167  1.00 25.16  ? 58  GLU B OE1 1 
ATOM   2830 O  OE2 . GLU B 1 58  ? 97.544  119.459 96.772  1.00 25.16  ? 58  GLU B OE2 1 
ATOM   2831 N  N   . ARG B 1 59  ? 100.358 125.044 95.023  1.00 29.52  ? 59  ARG B N   1 
ATOM   2832 C  CA  . ARG B 1 59  ? 100.462 126.274 94.202  1.00 29.52  ? 59  ARG B CA  1 
ATOM   2833 C  C   . ARG B 1 59  ? 101.640 126.088 93.241  1.00 29.52  ? 59  ARG B C   1 
ATOM   2834 O  O   . ARG B 1 59  ? 102.157 127.099 92.736  1.00 29.52  ? 59  ARG B O   1 
ATOM   2835 C  CB  . ARG B 1 59  ? 100.697 127.484 95.111  1.00 29.52  ? 59  ARG B CB  1 
ATOM   2836 C  CG  . ARG B 1 59  ? 100.233 128.808 94.524  1.00 29.52  ? 59  ARG B CG  1 
ATOM   2837 C  CD  . ARG B 1 59  ? 100.175 129.882 95.592  1.00 29.52  ? 59  ARG B CD  1 
ATOM   2838 N  NE  . ARG B 1 59  ? 99.139  130.868 95.323  1.00 29.52  ? 59  ARG B NE  1 
ATOM   2839 C  CZ  . ARG B 1 59  ? 99.221  132.151 95.657  1.00 29.52  ? 59  ARG B CZ  1 
ATOM   2840 N  NH1 . ARG B 1 59  ? 99.306  132.500 96.929  1.00 29.52  ? 59  ARG B NH1 1 
ATOM   2841 N  NH2 . ARG B 1 59  ? 99.221  133.079 94.718  1.00 29.52  ? 59  ARG B NH2 1 
ATOM   2842 N  N   . PHE B 1 60  ? 102.069 124.852 93.025  1.00 22.24  ? 60  PHE B N   1 
ATOM   2843 C  CA  . PHE B 1 60  ? 103.165 124.591 92.113  1.00 22.24  ? 60  PHE B CA  1 
ATOM   2844 C  C   . PHE B 1 60  ? 102.914 123.466 91.128  1.00 22.24  ? 60  PHE B C   1 
ATOM   2845 O  O   . PHE B 1 60  ? 103.755 123.233 90.264  1.00 22.24  ? 60  PHE B O   1 
ATOM   2846 C  CB  . PHE B 1 60  ? 104.427 124.250 92.887  1.00 22.24  ? 60  PHE B CB  1 
ATOM   2847 C  CG  . PHE B 1 60  ? 105.222 125.424 93.267  1.00 22.24  ? 60  PHE B CG  1 
ATOM   2848 C  CD1 . PHE B 1 60  ? 106.478 125.268 93.811  1.00 22.24  ? 60  PHE B CD1 1 
ATOM   2849 C  CD2 . PHE B 1 60  ? 104.723 126.678 93.093  1.00 22.24  ? 60  PHE B CD2 1 
ATOM   2850 C  CE1 . PHE B 1 60  ? 107.216 126.344 94.158  1.00 22.24  ? 60  PHE B CE1 1 
ATOM   2851 C  CE2 . PHE B 1 60  ? 105.450 127.758 93.447  1.00 22.24  ? 60  PHE B CE2 1 
ATOM   2852 C  CZ  . PHE B 1 60  ? 106.700 127.597 93.984  1.00 22.24  ? 60  PHE B CZ  1 
ATOM   2853 N  N   . ALA B 1 61  ? 101.831 122.725 91.250  1.00 23.60  ? 61  ALA B N   1 
ATOM   2854 C  CA  . ALA B 1 61  ? 101.453 121.787 90.212  1.00 23.60  ? 61  ALA B CA  1 
ATOM   2855 C  C   . ALA B 1 61  ? 100.377 122.363 89.325  1.00 23.60  ? 61  ALA B C   1 
ATOM   2856 O  O   . ALA B 1 61  ? 99.789  121.631 88.528  1.00 23.60  ? 61  ALA B O   1 
ATOM   2857 C  CB  . ALA B 1 61  ? 100.972 120.468 90.813  1.00 23.60  ? 61  ALA B CB  1 
ATOM   2858 N  N   . ARG B 1 62  ? 100.078 123.645 89.480  1.00 29.43  ? 62  ARG B N   1 
ATOM   2859 C  CA  . ARG B 1 62  ? 99.138  124.349 88.630  1.00 29.43  ? 62  ARG B CA  1 
ATOM   2860 C  C   . ARG B 1 62  ? 99.835  125.290 87.668  1.00 29.43  ? 62  ARG B C   1 
ATOM   2861 O  O   . ARG B 1 62  ? 99.198  125.786 86.737  1.00 29.43  ? 62  ARG B O   1 
ATOM   2862 C  CB  . ARG B 1 62  ? 98.134  125.140 89.476  1.00 29.43  ? 62  ARG B CB  1 
ATOM   2863 C  CG  . ARG B 1 62  ? 97.659  124.426 90.721  1.00 29.43  ? 62  ARG B CG  1 
ATOM   2864 C  CD  . ARG B 1 62  ? 97.041  125.396 91.716  1.00 29.43  ? 62  ARG B CD  1 
ATOM   2865 N  NE  . ARG B 1 62  ? 96.024  126.242 91.105  1.00 29.43  ? 62  ARG B NE  1 
ATOM   2866 C  CZ  . ARG B 1 62  ? 95.333  127.165 91.764  1.00 29.43  ? 62  ARG B CZ  1 
ATOM   2867 N  NH1 . ARG B 1 62  ? 95.547  127.349 93.056  1.00 29.43  ? 62  ARG B NH1 1 
ATOM   2868 N  NH2 . ARG B 1 62  ? 94.422  127.897 91.133  1.00 29.43  ? 62  ARG B NH2 1 
ATOM   2869 N  N   . ARG B 1 63  ? 101.121 125.560 87.868  1.00 26.30  ? 63  ARG B N   1 
ATOM   2870 C  CA  . ARG B 1 63  ? 101.831 126.401 86.923  1.00 26.30  ? 63  ARG B CA  1 
ATOM   2871 C  C   . ARG B 1 63  ? 102.353 125.561 85.774  1.00 26.30  ? 63  ARG B C   1 
ATOM   2872 O  O   . ARG B 1 63  ? 103.518 125.688 85.399  1.00 26.30  ? 63  ARG B O   1 
ATOM   2873 C  CB  . ARG B 1 63  ? 102.992 127.124 87.594  1.00 26.30  ? 63  ARG B CB  1 
ATOM   2874 C  CG  . ARG B 1 63  ? 102.626 127.959 88.786  1.00 26.30  ? 63  ARG B CG  1 
ATOM   2875 C  CD  . ARG B 1 63  ? 103.879 128.572 89.370  1.00 26.30  ? 63  ARG B CD  1 
ATOM   2876 N  NE  . ARG B 1 63  ? 103.602 129.584 90.378  1.00 26.30  ? 63  ARG B NE  1 
ATOM   2877 C  CZ  . ARG B 1 63  ? 104.520 130.402 90.880  1.00 26.30  ? 63  ARG B CZ  1 
ATOM   2878 N  NH1 . ARG B 1 63  ? 105.775 130.331 90.459  1.00 26.30  ? 63  ARG B NH1 1 
ATOM   2879 N  NH2 . ARG B 1 63  ? 104.184 131.300 91.800  1.00 26.30  ? 63  ARG B NH2 1 
ATOM   2880 N  N   . THR B 1 64  ? 101.503 124.723 85.188  1.00 25.62  ? 64  THR B N   1 
ATOM   2881 C  CA  . THR B 1 64  ? 101.933 123.824 84.122  1.00 25.62  ? 64  THR B CA  1 
ATOM   2882 C  C   . THR B 1 64  ? 102.017 124.586 82.799  1.00 25.62  ? 64  THR B C   1 
ATOM   2883 O  O   . THR B 1 64  ? 101.199 124.439 81.891  1.00 25.62  ? 64  THR B O   1 
ATOM   2884 C  CB  . THR B 1 64  ? 101.002 122.628 84.030  1.00 25.62  ? 64  THR B CB  1 
ATOM   2885 O  OG1 . THR B 1 64  ? 101.323 121.875 82.864  1.00 25.62  ? 64  THR B OG1 1 
ATOM   2886 C  CG2 . THR B 1 64  ? 99.567  123.061 83.962  1.00 25.62  ? 64  THR B CG2 1 
ATOM   2887 N  N   . HIS B 1 65  ? 103.017 125.456 82.712  1.00 24.50  ? 65  HIS B N   1 
ATOM   2888 C  CA  . HIS B 1 65  ? 103.272 126.250 81.479  1.00 24.50  ? 65  HIS B CA  1 
ATOM   2889 C  C   . HIS B 1 65  ? 104.787 126.377 81.279  1.00 24.50  ? 65  HIS B C   1 
ATOM   2890 O  O   . HIS B 1 65  ? 105.499 126.588 82.275  1.00 24.50  ? 65  HIS B O   1 
ATOM   2891 C  CB  . HIS B 1 65  ? 102.493 127.574 81.479  1.00 24.50  ? 65  HIS B CB  1 
ATOM   2892 C  CG  . HIS B 1 65  ? 102.795 128.478 82.625  1.00 24.50  ? 65  HIS B CG  1 
ATOM   2893 N  ND1 . HIS B 1 65  ? 102.442 129.813 82.619  1.00 24.50  ? 65  HIS B ND1 1 
ATOM   2894 C  CD2 . HIS B 1 65  ? 103.406 128.253 83.808  1.00 24.50  ? 65  HIS B CD2 1 
ATOM   2895 C  CE1 . HIS B 1 65  ? 102.825 130.372 83.748  1.00 24.50  ? 65  HIS B CE1 1 
ATOM   2896 N  NE2 . HIS B 1 65  ? 103.419 129.436 84.494  1.00 24.50  ? 65  HIS B NE2 1 
ATOM   2897 N  N   . ALA B 1 66  ? 105.255 126.264 80.049  1.00 19.79  ? 66  ALA B N   1 
ATOM   2898 C  CA  . ALA B 1 66  ? 106.677 126.274 79.757  1.00 19.79  ? 66  ALA B CA  1 
ATOM   2899 C  C   . ALA B 1 66  ? 107.281 127.627 80.092  1.00 19.79  ? 66  ALA B C   1 
ATOM   2900 O  O   . ALA B 1 66  ? 107.016 128.615 79.410  1.00 19.79  ? 66  ALA B O   1 
ATOM   2901 C  CB  . ALA B 1 66  ? 106.911 125.943 78.290  1.00 19.79  ? 66  ALA B CB  1 
ATOM   2902 N  N   . THR B 1 67  ? 108.109 127.666 81.125  1.00 12.53  ? 67  THR B N   1 
ATOM   2903 C  CA  . THR B 1 67  ? 108.769 128.885 81.555  1.00 12.53  ? 67  THR B CA  1 
ATOM   2904 C  C   . THR B 1 67  ? 110.260 128.800 81.259  1.00 12.53  ? 67  THR B C   1 
ATOM   2905 O  O   . THR B 1 67  ? 110.877 127.746 81.387  1.00 12.53  ? 67  THR B O   1 
ATOM   2906 C  CB  . THR B 1 67  ? 108.564 129.122 83.049  1.00 12.53  ? 67  THR B CB  1 
ATOM   2907 O  OG1 . THR B 1 67  ? 107.240 128.737 83.417  1.00 12.53  ? 67  THR B OG1 1 
ATOM   2908 C  CG2 . THR B 1 67  ? 108.750 130.577 83.381  1.00 12.53  ? 67  THR B CG2 1 
ATOM   2909 N  N   . GLN B 1 68  ? 110.886 129.935 81.022  1.00 19.98  ? 68  GLN B N   1 
ATOM   2910 C  CA  . GLN B 1 68  ? 112.307 129.923 80.589  1.00 19.98  ? 68  GLN B CA  1 
ATOM   2911 C  C   . GLN B 1 68  ? 113.141 129.202 81.650  1.00 19.98  ? 68  GLN B C   1 
ATOM   2912 O  O   . GLN B 1 68  ? 114.292 128.842 81.343  1.00 19.98  ? 68  GLN B O   1 
ATOM   2913 C  CB  . GLN B 1 68  ? 112.802 131.347 80.332  1.00 19.98  ? 68  GLN B CB  1 
ATOM   2914 C  CG  . GLN B 1 68  ? 114.262 131.421 79.914  1.00 19.98  ? 68  GLN B CG  1 
ATOM   2915 C  CD  . GLN B 1 68  ? 114.627 132.788 79.389  1.00 19.98  ? 68  GLN B CD  1 
ATOM   2916 O  OE1 . GLN B 1 68  ? 113.764 133.606 79.081  1.00 19.98  ? 68  GLN B OE1 1 
ATOM   2917 N  NE2 . GLN B 1 68  ? 115.920 133.043 79.278  1.00 19.98  ? 68  GLN B NE2 1 
ATOM   2918 N  N   . LYS B 1 69  ? 112.607 129.042 82.851  1.00 10.41  ? 69  LYS B N   1 
ATOM   2919 C  CA  . LYS B 1 69  ? 113.357 128.406 83.928  1.00 10.41  ? 69  LYS B CA  1 
ATOM   2920 C  C   . LYS B 1 69  ? 112.940 126.963 84.129  1.00 10.41  ? 69  LYS B C   1 
ATOM   2921 O  O   . LYS B 1 69  ? 113.418 126.315 85.055  1.00 10.41  ? 69  LYS B O   1 
ATOM   2922 C  CB  . LYS B 1 69  ? 113.185 129.183 85.233  1.00 10.41  ? 69  LYS B CB  1 
ATOM   2923 C  CG  . LYS B 1 69  ? 114.190 128.871 86.329  1.00 10.41  ? 69  LYS B CG  1 
ATOM   2924 C  CD  . LYS B 1 69  ? 115.562 128.538 85.792  1.00 10.41  ? 69  LYS B CD  1 
ATOM   2925 C  CE  . LYS B 1 69  ? 116.444 127.967 86.889  1.00 10.41  ? 69  LYS B CE  1 
ATOM   2926 N  NZ  . LYS B 1 69  ? 117.775 127.541 86.380  1.00 10.41  ? 69  LYS B NZ  1 
ATOM   2927 N  N   . ASN B 1 70  ? 112.010 126.473 83.336  1.00 6.10   ? 70  ASN B N   1 
ATOM   2928 C  CA  . ASN B 1 70  ? 111.687 125.061 83.286  1.00 6.10   ? 70  ASN B CA  1 
ATOM   2929 C  C   . ASN B 1 70  ? 110.823 124.843 82.075  1.00 6.10   ? 70  ASN B C   1 
ATOM   2930 O  O   . ASN B 1 70  ? 109.662 125.243 82.076  1.00 6.10   ? 70  ASN B O   1 
ATOM   2931 C  CB  . ASN B 1 70  ? 110.994 124.610 84.563  1.00 6.10   ? 70  ASN B CB  1 
ATOM   2932 C  CG  . ASN B 1 70  ? 110.287 123.272 84.430  1.00 6.10   ? 70  ASN B CG  1 
ATOM   2933 O  OD1 . ASN B 1 70  ? 109.886 122.849 83.359  1.00 6.10   ? 70  ASN B OD1 1 
ATOM   2934 N  ND2 . ASN B 1 70  ? 110.174 122.571 85.542  1.00 6.10   ? 70  ASN B ND2 1 
ATOM   2935 N  N   . THR B 1 71  ? 111.342 124.158 81.068  1.00 3.89   ? 71  THR B N   1 
ATOM   2936 C  CA  . THR B 1 71  ? 110.640 124.018 79.809  1.00 3.89   ? 71  THR B CA  1 
ATOM   2937 C  C   . THR B 1 71  ? 109.625 122.889 79.801  1.00 3.89   ? 71  THR B C   1 
ATOM   2938 O  O   . THR B 1 71  ? 109.019 122.639 78.759  1.00 3.89   ? 71  THR B O   1 
ATOM   2939 C  CB  . THR B 1 71  ? 111.650 123.842 78.704  1.00 3.89   ? 71  THR B CB  1 
ATOM   2940 O  OG1 . THR B 1 71  ? 112.683 122.998 79.191  1.00 3.89   ? 71  THR B OG1 1 
ATOM   2941 C  CG2 . THR B 1 71  ? 112.250 125.158 78.350  1.00 3.89   ? 71  THR B CG2 1 
ATOM   2942 N  N   . PHE B 1 72  ? 109.423 122.213 80.932  1.00 4.96   ? 72  PHE B N   1 
ATOM   2943 C  CA  . PHE B 1 72  ? 108.268 121.352 81.163  1.00 4.96   ? 72  PHE B CA  1 
ATOM   2944 C  C   . PHE B 1 72  ? 107.230 121.997 82.052  1.00 4.96   ? 72  PHE B C   1 
ATOM   2945 O  O   . PHE B 1 72  ? 106.092 121.524 82.089  1.00 4.96   ? 72  PHE B O   1 
ATOM   2946 C  CB  . PHE B 1 72  ? 108.673 120.057 81.859  1.00 4.96   ? 72  PHE B CB  1 
ATOM   2947 C  CG  . PHE B 1 72  ? 109.465 119.137 81.024  1.00 4.96   ? 72  PHE B CG  1 
ATOM   2948 C  CD1 . PHE B 1 72  ? 108.853 118.250 80.202  1.00 4.96   ? 72  PHE B CD1 1 
ATOM   2949 C  CD2 . PHE B 1 72  ? 110.819 119.150 81.079  1.00 4.96   ? 72  PHE B CD2 1 
ATOM   2950 C  CE1 . PHE B 1 72  ? 109.573 117.406 79.445  1.00 4.96   ? 72  PHE B CE1 1 
ATOM   2951 C  CE2 . PHE B 1 72  ? 111.526 118.305 80.323  1.00 4.96   ? 72  PHE B CE2 1 
ATOM   2952 C  CZ  . PHE B 1 72  ? 110.904 117.434 79.500  1.00 4.96   ? 72  PHE B CZ  1 
ATOM   2953 N  N   . GLY B 1 73  ? 107.608 123.040 82.786  1.00 6.17   ? 73  GLY B N   1 
ATOM   2954 C  CA  . GLY B 1 73  ? 106.782 123.574 83.846  1.00 6.17   ? 73  GLY B CA  1 
ATOM   2955 C  C   . GLY B 1 73  ? 107.040 122.820 85.129  1.00 6.17   ? 73  GLY B C   1 
ATOM   2956 O  O   . GLY B 1 73  ? 107.855 121.901 85.186  1.00 6.17   ? 73  GLY B O   1 
ATOM   2957 N  N   . TRP B 1 74  ? 106.328 123.206 86.191  1.00 9.36   ? 74  TRP B N   1 
ATOM   2958 C  CA  . TRP B 1 74  ? 106.483 122.521 87.466  1.00 9.36   ? 74  TRP B CA  1 
ATOM   2959 C  C   . TRP B 1 74  ? 105.485 121.403 87.640  1.00 9.36   ? 74  TRP B C   1 
ATOM   2960 O  O   . TRP B 1 74  ? 105.093 121.104 88.768  1.00 9.36   ? 74  TRP B O   1 
ATOM   2961 C  CB  . TRP B 1 74  ? 106.381 123.503 88.624  1.00 9.36   ? 74  TRP B CB  1 
ATOM   2962 C  CG  . TRP B 1 74  ? 107.250 124.643 88.457  1.00 9.36   ? 74  TRP B CG  1 
ATOM   2963 C  CD1 . TRP B 1 74  ? 106.886 125.885 88.103  1.00 9.36   ? 74  TRP B CD1 1 
ATOM   2964 C  CD2 . TRP B 1 74  ? 108.659 124.666 88.618  1.00 9.36   ? 74  TRP B CD2 1 
ATOM   2965 N  NE1 . TRP B 1 74  ? 107.977 126.698 88.033  1.00 9.36   ? 74  TRP B NE1 1 
ATOM   2966 C  CE2 . TRP B 1 74  ? 109.086 125.966 88.349  1.00 9.36   ? 74  TRP B CE2 1 
ATOM   2967 C  CE3 . TRP B 1 74  ? 109.608 123.708 88.956  1.00 9.36   ? 74  TRP B CE3 1 
ATOM   2968 C  CZ2 . TRP B 1 74  ? 110.418 126.337 88.408  1.00 9.36   ? 74  TRP B CZ2 1 
ATOM   2969 C  CZ3 . TRP B 1 74  ? 110.930 124.078 89.012  1.00 9.36   ? 74  TRP B CZ3 1 
ATOM   2970 C  CH2 . TRP B 1 74  ? 111.322 125.378 88.742  1.00 9.36   ? 74  TRP B CH2 1 
ATOM   2971 N  N   . ILE B 1 75  ? 105.076 120.761 86.548  1.00 12.18  ? 75  ILE B N   1 
ATOM   2972 C  CA  . ILE B 1 75  ? 104.117 119.671 86.612  1.00 12.18  ? 75  ILE B CA  1 
ATOM   2973 C  C   . ILE B 1 75  ? 104.619 118.525 87.472  1.00 12.18  ? 75  ILE B C   1 
ATOM   2974 O  O   . ILE B 1 75  ? 103.844 117.633 87.825  1.00 12.18  ? 75  ILE B O   1 
ATOM   2975 C  CB  . ILE B 1 75  ? 103.801 119.208 85.186  1.00 12.18  ? 75  ILE B CB  1 
ATOM   2976 C  CG1 . ILE B 1 75  ? 102.616 118.265 85.157  1.00 12.18  ? 75  ILE B CG1 1 
ATOM   2977 C  CG2 . ILE B 1 75  ? 104.963 118.506 84.625  1.00 12.18  ? 75  ILE B CG2 1 
ATOM   2978 C  CD1 . ILE B 1 75  ? 101.318 118.924 85.560  1.00 12.18  ? 75  ILE B CD1 1 
ATOM   2979 N  N   . ARG B 1 76  ? 105.900 118.528 87.831  1.00 4.96   ? 76  ARG B N   1 
ATOM   2980 C  CA  . ARG B 1 76  ? 106.500 117.492 88.661  1.00 4.96   ? 76  ARG B CA  1 
ATOM   2981 C  C   . ARG B 1 76  ? 106.504 117.835 90.138  1.00 4.96   ? 76  ARG B C   1 
ATOM   2982 O  O   . ARG B 1 76  ? 106.633 116.928 90.958  1.00 4.96   ? 76  ARG B O   1 
ATOM   2983 C  CB  . ARG B 1 76  ? 107.933 117.231 88.209  1.00 4.96   ? 76  ARG B CB  1 
ATOM   2984 C  CG  . ARG B 1 76  ? 108.442 115.825 88.377  1.00 4.96   ? 76  ARG B CG  1 
ATOM   2985 C  CD  . ARG B 1 76  ? 109.800 115.752 87.712  1.00 4.96   ? 76  ARG B CD  1 
ATOM   2986 N  NE  . ARG B 1 76  ? 110.440 114.446 87.709  1.00 4.96   ? 76  ARG B NE  1 
ATOM   2987 C  CZ  . ARG B 1 76  ? 110.144 113.485 86.857  1.00 4.96   ? 76  ARG B CZ  1 
ATOM   2988 N  NH1 . ARG B 1 76  ? 109.193 113.676 85.987  1.00 4.96   ? 76  ARG B NH1 1 
ATOM   2989 N  NH2 . ARG B 1 76  ? 110.774 112.334 86.897  1.00 4.96   ? 76  ARG B NH2 1 
ATOM   2990 N  N   . ALA B 1 77  ? 106.339 119.107 90.502  1.00 12.92  ? 77  ALA B N   1 
ATOM   2991 C  CA  . ALA B 1 77  ? 106.412 119.502 91.902  1.00 12.92  ? 77  ALA B CA  1 
ATOM   2992 C  C   . ALA B 1 77  ? 105.298 118.905 92.738  1.00 12.92  ? 77  ALA B C   1 
ATOM   2993 O  O   . ALA B 1 77  ? 105.238 119.160 93.938  1.00 12.92  ? 77  ALA B O   1 
ATOM   2994 C  CB  . ALA B 1 77  ? 106.381 121.015 92.026  1.00 12.92  ? 77  ALA B CB  1 
ATOM   2995 N  N   . GLU B 1 78  ? 104.390 118.156 92.134  1.00 19.76  ? 78  GLU B N   1 
ATOM   2996 C  CA  . GLU B 1 78  ? 103.494 117.313 92.910  1.00 19.76  ? 78  GLU B CA  1 
ATOM   2997 C  C   . GLU B 1 78  ? 104.229 116.080 93.404  1.00 19.76  ? 78  GLU B C   1 
ATOM   2998 O  O   . GLU B 1 78  ? 104.392 115.876 94.609  1.00 19.76  ? 78  GLU B O   1 
ATOM   2999 C  CB  . GLU B 1 78  ? 102.298 116.917 92.053  1.00 19.76  ? 78  GLU B CB  1 
ATOM   3000 C  CG  . GLU B 1 78  ? 101.501 115.762 92.578  1.00 19.76  ? 78  GLU B CG  1 
ATOM   3001 C  CD  . GLU B 1 78  ? 100.846 114.976 91.463  1.00 19.76  ? 78  GLU B CD  1 
ATOM   3002 O  OE1 . GLU B 1 78  ? 101.154 115.253 90.288  1.00 19.76  ? 78  GLU B OE1 1 
ATOM   3003 O  OE2 . GLU B 1 78  ? 100.016 114.092 91.753  1.00 19.76  ? 78  GLU B OE2 1 
ATOM   3004 N  N   . VAL B 1 79  ? 104.738 115.272 92.473  1.00 15.46  ? 79  VAL B N   1 
ATOM   3005 C  CA  . VAL B 1 79  ? 105.346 113.990 92.796  1.00 15.46  ? 79  VAL B CA  1 
ATOM   3006 C  C   . VAL B 1 79  ? 106.668 114.146 93.513  1.00 15.46  ? 79  VAL B C   1 
ATOM   3007 O  O   . VAL B 1 79  ? 107.308 113.150 93.840  1.00 15.46  ? 79  VAL B O   1 
ATOM   3008 C  CB  . VAL B 1 79  ? 105.540 113.174 91.514  1.00 15.46  ? 79  VAL B CB  1 
ATOM   3009 C  CG1 . VAL B 1 79  ? 106.803 113.593 90.842  1.00 15.46  ? 79  VAL B CG1 1 
ATOM   3010 C  CG2 . VAL B 1 79  ? 105.558 111.721 91.810  1.00 15.46  ? 79  VAL B CG2 1 
ATOM   3011 N  N   . MET B 1 80  ? 107.131 115.374 93.716  1.00 12.86  ? 80  MET B N   1 
ATOM   3012 C  CA  . MET B 1 80  ? 108.265 115.590 94.602  1.00 12.86  ? 80  MET B CA  1 
ATOM   3013 C  C   . MET B 1 80  ? 107.788 115.866 96.010  1.00 12.86  ? 80  MET B C   1 
ATOM   3014 O  O   . MET B 1 80  ? 108.337 115.334 96.975  1.00 12.86  ? 80  MET B O   1 
ATOM   3015 C  CB  . MET B 1 80  ? 109.122 116.739 94.112  1.00 12.86  ? 80  MET B CB  1 
ATOM   3016 C  CG  . MET B 1 80  ? 109.861 117.383 95.211  1.00 12.86  ? 80  MET B CG  1 
ATOM   3017 S  SD  . MET B 1 80  ? 111.332 116.455 95.526  1.00 12.86  ? 80  MET B SD  1 
ATOM   3018 C  CE  . MET B 1 80  ? 112.468 117.429 94.578  1.00 12.86  ? 80  MET B CE  1 
ATOM   3019 N  N   . GLY B 1 81  ? 106.752 116.688 96.143  1.00 12.69  ? 81  GLY B N   1 
ATOM   3020 C  CA  . GLY B 1 81  ? 106.177 116.939 97.451  1.00 12.69  ? 81  GLY B CA  1 
ATOM   3021 C  C   . GLY B 1 81  ? 105.923 115.663 98.222  1.00 12.69  ? 81  GLY B C   1 
ATOM   3022 O  O   . GLY B 1 81  ? 106.387 115.508 99.350  1.00 12.69  ? 81  GLY B O   1 
ATOM   3023 N  N   . ALA B 1 82  ? 105.218 114.713 97.609  1.00 16.52  ? 82  ALA B N   1 
ATOM   3024 C  CA  . ALA B 1 82  ? 104.978 113.434 98.265  1.00 16.52  ? 82  ALA B CA  1 
ATOM   3025 C  C   . ALA B 1 82  ? 106.268 112.855 98.812  1.00 16.52  ? 82  ALA B C   1 
ATOM   3026 O  O   . ALA B 1 82  ? 106.351 112.516 99.996  1.00 16.52  ? 82  ALA B O   1 
ATOM   3027 C  CB  . ALA B 1 82  ? 104.322 112.450 97.305  1.00 16.52  ? 82  ALA B CB  1 
ATOM   3028 N  N   . LEU B 1 83  ? 107.305 112.785 97.978  1.00 12.09  ? 83  LEU B N   1 
ATOM   3029 C  CA  . LEU B 1 83  ? 108.586 112.278 98.449  1.00 12.09  ? 83  LEU B CA  1 
ATOM   3030 C  C   . LEU B 1 83  ? 108.980 112.928 99.762  1.00 12.09  ? 83  LEU B C   1 
ATOM   3031 O  O   . LEU B 1 83  ? 109.151 112.239 100.768 1.00 12.09  ? 83  LEU B O   1 
ATOM   3032 C  CB  . LEU B 1 83  ? 109.677 112.509 97.422  1.00 12.09  ? 83  LEU B CB  1 
ATOM   3033 C  CG  . LEU B 1 83  ? 111.044 112.155 97.965  1.00 12.09  ? 83  LEU B CG  1 
ATOM   3034 C  CD1 . LEU B 1 83  ? 111.083 110.685 98.181  1.00 12.09  ? 83  LEU B CD1 1 
ATOM   3035 C  CD2 . LEU B 1 83  ? 112.111 112.576 97.005  1.00 12.09  ? 83  LEU B CD2 1 
ATOM   3036 N  N   . VAL B 1 84  ? 109.089 114.259 99.787  1.00 11.30  ? 84  VAL B N   1 
ATOM   3037 C  CA  . VAL B 1 84  ? 109.555 114.914 101.005 1.00 11.30  ? 84  VAL B CA  1 
ATOM   3038 C  C   . VAL B 1 84  ? 108.717 114.471 102.187 1.00 11.30  ? 84  VAL B C   1 
ATOM   3039 O  O   . VAL B 1 84  ? 109.247 114.055 103.219 1.00 11.30  ? 84  VAL B O   1 
ATOM   3040 C  CB  . VAL B 1 84  ? 109.543 116.435 100.851 1.00 11.30  ? 84  VAL B CB  1 
ATOM   3041 C  CG1 . VAL B 1 84  ? 109.570 117.032 102.187 1.00 11.30  ? 84  VAL B CG1 1 
ATOM   3042 C  CG2 . VAL B 1 84  ? 110.753 116.875 100.102 1.00 11.30  ? 84  VAL B CG2 1 
ATOM   3043 N  N   . ASN B 1 85  ? 107.398 114.469 102.030 1.00 17.28  ? 85  ASN B N   1 
ATOM   3044 C  CA  . ASN B 1 85  ? 106.553 114.015 103.126 1.00 17.28  ? 85  ASN B CA  1 
ATOM   3045 C  C   . ASN B 1 85  ? 106.942 112.605 103.538 1.00 17.28  ? 85  ASN B C   1 
ATOM   3046 O  O   . ASN B 1 85  ? 107.337 112.361 104.680 1.00 17.28  ? 85  ASN B O   1 
ATOM   3047 C  CB  . ASN B 1 85  ? 105.085 114.063 102.714 1.00 17.28  ? 85  ASN B CB  1 
ATOM   3048 C  CG  . ASN B 1 85  ? 104.458 115.390 102.982 1.00 17.28  ? 85  ASN B CG  1 
ATOM   3049 O  OD1 . ASN B 1 85  ? 104.331 115.808 104.126 1.00 17.28  ? 85  ASN B OD1 1 
ATOM   3050 N  ND2 . ASN B 1 85  ? 104.044 116.065 101.925 1.00 17.28  ? 85  ASN B ND2 1 
ATOM   3051 N  N   . ALA B 1 86  ? 106.926 111.678 102.583 1.00 11.52  ? 86  ALA B N   1 
ATOM   3052 C  CA  . ALA B 1 86  ? 107.180 110.289 102.909 1.00 11.52  ? 86  ALA B CA  1 
ATOM   3053 C  C   . ALA B 1 86  ? 108.590 110.055 103.405 1.00 11.52  ? 86  ALA B C   1 
ATOM   3054 O  O   . ALA B 1 86  ? 108.892 108.945 103.836 1.00 11.52  ? 86  ALA B O   1 
ATOM   3055 C  CB  . ALA B 1 86  ? 106.912 109.409 101.706 1.00 11.52  ? 86  ALA B CB  1 
ATOM   3056 N  N   . ILE B 1 87  ? 109.470 111.049 103.352 1.00 8.76   ? 87  ILE B N   1 
ATOM   3057 C  CA  . ILE B 1 87  ? 110.734 110.923 104.068 1.00 8.76   ? 87  ILE B CA  1 
ATOM   3058 C  C   . ILE B 1 87  ? 110.572 111.415 105.488 1.00 8.76   ? 87  ILE B C   1 
ATOM   3059 O  O   . ILE B 1 87  ? 110.812 110.673 106.444 1.00 8.76   ? 87  ILE B O   1 
ATOM   3060 C  CB  . ILE B 1 87  ? 111.858 111.692 103.363 1.00 8.76   ? 87  ILE B CB  1 
ATOM   3061 C  CG1 . ILE B 1 87  ? 112.372 110.934 102.167 1.00 8.76   ? 87  ILE B CG1 1 
ATOM   3062 C  CG2 . ILE B 1 87  ? 112.993 111.886 104.288 1.00 8.76   ? 87  ILE B CG2 1 
ATOM   3063 C  CD1 . ILE B 1 87  ? 113.386 111.721 101.438 1.00 8.76   ? 87  ILE B CD1 1 
ATOM   3064 N  N   . PHE B 1 88  ? 110.122 112.662 105.634 1.00 19.25  ? 88  PHE B N   1 
ATOM   3065 C  CA  . PHE B 1 88  ? 109.958 113.273 106.942 1.00 19.25  ? 88  PHE B CA  1 
ATOM   3066 C  C   . PHE B 1 88  ? 109.309 112.291 107.896 1.00 19.25  ? 88  PHE B C   1 
ATOM   3067 O  O   . PHE B 1 88  ? 109.948 111.815 108.839 1.00 19.25  ? 88  PHE B O   1 
ATOM   3068 C  CB  . PHE B 1 88  ? 109.123 114.543 106.802 1.00 19.25  ? 88  PHE B CB  1 
ATOM   3069 C  CG  . PHE B 1 88  ? 108.731 115.168 108.100 1.00 19.25  ? 88  PHE B CG  1 
ATOM   3070 C  CD1 . PHE B 1 88  ? 109.555 116.078 108.715 1.00 19.25  ? 88  PHE B CD1 1 
ATOM   3071 C  CD2 . PHE B 1 88  ? 107.525 114.871 108.695 1.00 19.25  ? 88  PHE B CD2 1 
ATOM   3072 C  CE1 . PHE B 1 88  ? 109.193 116.661 109.909 1.00 19.25  ? 88  PHE B CE1 1 
ATOM   3073 C  CE2 . PHE B 1 88  ? 107.165 115.454 109.887 1.00 19.25  ? 88  PHE B CE2 1 
ATOM   3074 C  CZ  . PHE B 1 88  ? 107.999 116.347 110.489 1.00 19.25  ? 88  PHE B CZ  1 
ATOM   3075 N  N   . LEU B 1 89  ? 108.075 111.891 107.596 1.00 17.16  ? 89  LEU B N   1 
ATOM   3076 C  CA  . LEU B 1 89  ? 107.366 110.913 108.408 1.00 17.16  ? 89  LEU B CA  1 
ATOM   3077 C  C   . LEU B 1 89  ? 108.248 109.726 108.776 1.00 17.16  ? 89  LEU B C   1 
ATOM   3078 O  O   . LEU B 1 89  ? 108.490 109.472 109.961 1.00 17.16  ? 89  LEU B O   1 
ATOM   3079 C  CB  . LEU B 1 89  ? 106.119 110.445 107.673 1.00 17.16  ? 89  LEU B CB  1 
ATOM   3080 C  CG  . LEU B 1 89  ? 105.525 109.153 108.191 1.00 17.16  ? 89  LEU B CG  1 
ATOM   3081 C  CD1 . LEU B 1 89  ? 105.119 109.323 109.616 1.00 17.16  ? 89  LEU B CD1 1 
ATOM   3082 C  CD2 . LEU B 1 89  ? 104.336 108.813 107.365 1.00 17.16  ? 89  LEU B CD2 1 
ATOM   3083 N  N   . THR B 1 90  ? 108.776 109.010 107.779 1.00 17.82  ? 90  THR B N   1 
ATOM   3084 C  CA  . THR B 1 90  ? 109.578 107.827 108.082 1.00 17.82  ? 90  THR B CA  1 
ATOM   3085 C  C   . THR B 1 90  ? 110.748 108.179 108.982 1.00 17.82  ? 90  THR B C   1 
ATOM   3086 O  O   . THR B 1 90  ? 110.983 107.513 109.991 1.00 17.82  ? 90  THR B O   1 
ATOM   3087 C  CB  . THR B 1 90  ? 110.066 107.151 106.809 1.00 17.82  ? 90  THR B CB  1 
ATOM   3088 O  OG1 . THR B 1 90  ? 108.972 106.481 106.180 1.00 17.82  ? 90  THR B OG1 1 
ATOM   3089 C  CG2 . THR B 1 90  ? 111.109 106.144 107.132 1.00 17.82  ? 90  THR B CG2 1 
ATOM   3090 N  N   . GLY B 1 91  ? 111.463 109.248 108.663 1.00 18.44  ? 91  GLY B N   1 
ATOM   3091 C  CA  . GLY B 1 91  ? 112.533 109.684 109.533 1.00 18.44  ? 91  GLY B CA  1 
ATOM   3092 C  C   . GLY B 1 91  ? 111.967 109.890 110.912 1.00 18.44  ? 91  GLY B C   1 
ATOM   3093 O  O   . GLY B 1 91  ? 112.373 109.234 111.871 1.00 18.44  ? 91  GLY B O   1 
ATOM   3094 N  N   . LEU B 1 92  ? 110.949 110.741 110.987 1.00 19.44  ? 92  LEU B N   1 
ATOM   3095 C  CA  . LEU B 1 92  ? 110.275 111.001 112.249 1.00 19.44  ? 92  LEU B CA  1 
ATOM   3096 C  C   . LEU B 1 92  ? 109.801 109.715 112.902 1.00 19.44  ? 92  LEU B C   1 
ATOM   3097 O  O   . LEU B 1 92  ? 109.848 109.585 114.129 1.00 19.44  ? 92  LEU B O   1 
ATOM   3098 C  CB  . LEU B 1 92  ? 109.106 111.942 112.010 1.00 19.44  ? 92  LEU B CB  1 
ATOM   3099 C  CG  . LEU B 1 92  ? 108.261 112.377 113.180 1.00 19.44  ? 92  LEU B CG  1 
ATOM   3100 C  CD1 . LEU B 1 92  ? 107.849 113.784 112.899 1.00 19.44  ? 92  LEU B CD1 1 
ATOM   3101 C  CD2 . LEU B 1 92  ? 107.050 111.493 113.309 1.00 19.44  ? 92  LEU B CD2 1 
ATOM   3102 N  N   . CYS B 1 93  ? 109.352 108.746 112.101 1.00 21.48  ? 93  CYS B N   1 
ATOM   3103 C  CA  . CYS B 1 93  ? 108.850 107.506 112.682 1.00 21.48  ? 93  CYS B CA  1 
ATOM   3104 C  C   . CYS B 1 93  ? 109.937 106.787 113.462 1.00 21.48  ? 93  CYS B C   1 
ATOM   3105 O  O   . CYS B 1 93  ? 109.706 106.336 114.587 1.00 21.48  ? 93  CYS B O   1 
ATOM   3106 C  CB  . CYS B 1 93  ? 108.278 106.591 111.615 1.00 21.48  ? 93  CYS B CB  1 
ATOM   3107 S  SG  . CYS B 1 93  ? 107.643 105.098 112.319 1.00 21.48  ? 93  CYS B SG  1 
ATOM   3108 N  N   . PHE B 1 94  ? 111.145 106.700 112.905 1.00 18.18  ? 94  PHE B N   1 
ATOM   3109 C  CA  . PHE B 1 94  ? 112.225 106.088 113.668 1.00 18.18  ? 94  PHE B CA  1 
ATOM   3110 C  C   . PHE B 1 94  ? 112.410 106.789 115.002 1.00 18.18  ? 94  PHE B C   1 
ATOM   3111 O  O   . PHE B 1 94  ? 112.654 106.134 116.017 1.00 18.18  ? 94  PHE B O   1 
ATOM   3112 C  CB  . PHE B 1 94  ? 113.523 106.100 112.871 1.00 18.18  ? 94  PHE B CB  1 
ATOM   3113 C  CG  . PHE B 1 94  ? 113.580 105.056 111.807 1.00 18.18  ? 94  PHE B CG  1 
ATOM   3114 C  CD1 . PHE B 1 94  ? 112.772 103.946 111.873 1.00 18.18  ? 94  PHE B CD1 1 
ATOM   3115 C  CD2 . PHE B 1 94  ? 114.425 105.198 110.727 1.00 18.18  ? 94  PHE B CD2 1 
ATOM   3116 C  CE1 . PHE B 1 94  ? 112.825 102.993 110.899 1.00 18.18  ? 94  PHE B CE1 1 
ATOM   3117 C  CE2 . PHE B 1 94  ? 114.471 104.246 109.742 1.00 18.18  ? 94  PHE B CE2 1 
ATOM   3118 C  CZ  . PHE B 1 94  ? 113.670 103.144 109.829 1.00 18.18  ? 94  PHE B CZ  1 
ATOM   3119 N  N   . ALA B 1 95  ? 112.253 108.113 115.027 1.00 16.81  ? 95  ALA B N   1 
ATOM   3120 C  CA  . ALA B 1 95  ? 112.356 108.835 116.285 1.00 16.81  ? 95  ALA B CA  1 
ATOM   3121 C  C   . ALA B 1 95  ? 111.477 108.195 117.338 1.00 16.81  ? 95  ALA B C   1 
ATOM   3122 O  O   . ALA B 1 95  ? 111.964 107.799 118.401 1.00 16.81  ? 95  ALA B O   1 
ATOM   3123 C  CB  . ALA B 1 95  ? 111.985 110.298 116.097 1.00 16.81  ? 95  ALA B CB  1 
ATOM   3124 N  N   . ILE B 1 96  ? 110.190 108.006 117.032 1.00 21.62  ? 96  ILE B N   1 
ATOM   3125 C  CA  . ILE B 1 96  ? 109.299 107.367 117.998 1.00 21.62  ? 96  ILE B CA  1 
ATOM   3126 C  C   . ILE B 1 96  ? 109.918 106.076 118.493 1.00 21.62  ? 96  ILE B C   1 
ATOM   3127 O  O   . ILE B 1 96  ? 110.091 105.870 119.699 1.00 21.62  ? 96  ILE B O   1 
ATOM   3128 C  CB  . ILE B 1 96  ? 107.918 107.103 117.386 1.00 21.62  ? 96  ILE B CB  1 
ATOM   3129 C  CG1 . ILE B 1 96  ? 107.200 108.413 117.141 1.00 21.62  ? 96  ILE B CG1 1 
ATOM   3130 C  CG2 . ILE B 1 96  ? 107.112 106.254 118.316 1.00 21.62  ? 96  ILE B CG2 1 
ATOM   3131 C  CD1 . ILE B 1 96  ? 107.038 109.214 118.376 1.00 21.62  ? 96  ILE B CD1 1 
ATOM   3132 N  N   . LEU B 1 97  ? 110.322 105.214 117.557 1.00 18.74  ? 97  LEU B N   1 
ATOM   3133 C  CA  . LEU B 1 97  ? 110.891 103.928 117.933 1.00 18.74  ? 97  LEU B CA  1 
ATOM   3134 C  C   . LEU B 1 97  ? 112.050 104.109 118.893 1.00 18.74  ? 97  LEU B C   1 
ATOM   3135 O  O   . LEU B 1 97  ? 112.067 103.514 119.972 1.00 18.74  ? 97  LEU B O   1 
ATOM   3136 C  CB  . LEU B 1 97  ? 111.336 103.171 116.697 1.00 18.74  ? 97  LEU B CB  1 
ATOM   3137 C  CG  . LEU B 1 97  ? 111.796 101.771 117.021 1.00 18.74  ? 97  LEU B CG  1 
ATOM   3138 C  CD1 . LEU B 1 97  ? 110.841 101.160 117.991 1.00 18.74  ? 97  LEU B CD1 1 
ATOM   3139 C  CD2 . LEU B 1 97  ? 111.813 100.970 115.756 1.00 18.74  ? 97  LEU B CD2 1 
ATOM   3140 N  N   . LEU B 1 98  ? 113.002 104.972 118.544 1.00 25.34  ? 98  LEU B N   1 
ATOM   3141 C  CA  . LEU B 1 98  ? 114.107 105.249 119.453 1.00 25.34  ? 98  LEU B CA  1 
ATOM   3142 C  C   . LEU B 1 98  ? 113.585 105.650 120.820 1.00 25.34  ? 98  LEU B C   1 
ATOM   3143 O  O   . LEU B 1 98  ? 113.947 105.053 121.836 1.00 25.34  ? 98  LEU B O   1 
ATOM   3144 C  CB  . LEU B 1 98  ? 114.986 106.343 118.868 1.00 25.34  ? 98  LEU B CB  1 
ATOM   3145 C  CG  . LEU B 1 98  ? 116.143 106.914 119.659 1.00 25.34  ? 98  LEU B CG  1 
ATOM   3146 C  CD1 . LEU B 1 98  ? 117.219 107.315 118.672 1.00 25.34  ? 98  LEU B CD1 1 
ATOM   3147 C  CD2 . LEU B 1 98  ? 115.681 108.117 120.457 1.00 25.34  ? 98  LEU B CD2 1 
ATOM   3148 N  N   . GLU B 1 99  ? 112.693 106.636 120.856 1.00 28.87  ? 99  GLU B N   1 
ATOM   3149 C  CA  . GLU B 1 99  ? 112.132 107.086 122.119 1.00 28.87  ? 99  GLU B CA  1 
ATOM   3150 C  C   . GLU B 1 99  ? 111.388 105.981 122.841 1.00 28.87  ? 99  GLU B C   1 
ATOM   3151 O  O   . GLU B 1 99  ? 111.411 105.948 124.072 1.00 28.87  ? 99  GLU B O   1 
ATOM   3152 C  CB  . GLU B 1 99  ? 111.212 108.272 121.878 1.00 28.87  ? 99  GLU B CB  1 
ATOM   3153 C  CG  . GLU B 1 99  ? 110.589 108.859 123.107 1.00 28.87  ? 99  GLU B CG  1 
ATOM   3154 C  CD  . GLU B 1 99  ? 109.771 110.094 122.783 1.00 28.87  ? 99  GLU B CD  1 
ATOM   3155 O  OE1 . GLU B 1 99  ? 109.829 110.573 121.632 1.00 28.87  ? 99  GLU B OE1 1 
ATOM   3156 O  OE2 . GLU B 1 99  ? 109.042 110.572 123.671 1.00 28.87  ? 99  GLU B OE2 1 
ATOM   3157 N  N   . ALA B 1 100 ? 110.767 105.050 122.120 1.00 24.89  ? 100 ALA B N   1 
ATOM   3158 C  CA  . ALA B 1 100 ? 110.086 103.963 122.807 1.00 24.89  ? 100 ALA B CA  1 
ATOM   3159 C  C   . ALA B 1 100 ? 111.056 103.175 123.666 1.00 24.89  ? 100 ALA B C   1 
ATOM   3160 O  O   . ALA B 1 100 ? 110.696 102.708 124.750 1.00 24.89  ? 100 ALA B O   1 
ATOM   3161 C  CB  . ALA B 1 100 ? 109.405 103.041 121.809 1.00 24.89  ? 100 ALA B CB  1 
ATOM   3162 N  N   . ILE B 1 101 ? 112.303 103.042 123.219 1.00 26.04  ? 101 ILE B N   1 
ATOM   3163 C  CA  . ILE B 1 101 ? 113.283 102.310 124.011 1.00 26.04  ? 101 ILE B CA  1 
ATOM   3164 C  C   . ILE B 1 101 ? 113.508 102.975 125.362 1.00 26.04  ? 101 ILE B C   1 
ATOM   3165 O  O   . ILE B 1 101 ? 113.656 102.286 126.376 1.00 26.04  ? 101 ILE B O   1 
ATOM   3166 C  CB  . ILE B 1 101 ? 114.591 102.158 123.218 1.00 26.04  ? 101 ILE B CB  1 
ATOM   3167 C  CG1 . ILE B 1 101 ? 114.408 101.145 122.098 1.00 26.04  ? 101 ILE B CG1 1 
ATOM   3168 C  CG2 . ILE B 1 101 ? 115.704 101.730 124.114 1.00 26.04  ? 101 ILE B CG2 1 
ATOM   3169 C  CD1 . ILE B 1 101 ? 113.800 99.869  122.557 1.00 26.04  ? 101 ILE B CD1 1 
ATOM   3170 N  N   . GLU B 1 102 ? 113.490 104.307 125.425 1.00 33.18  ? 102 GLU B N   1 
ATOM   3171 C  CA  . GLU B 1 102 ? 113.659 104.942 126.724 1.00 33.18  ? 102 GLU B CA  1 
ATOM   3172 C  C   . GLU B 1 102 ? 112.574 104.547 127.713 1.00 33.18  ? 102 GLU B C   1 
ATOM   3173 O  O   . GLU B 1 102 ? 112.824 104.576 128.917 1.00 33.18  ? 102 GLU B O   1 
ATOM   3174 C  CB  . GLU B 1 102 ? 113.661 106.456 126.598 1.00 33.18  ? 102 GLU B CB  1 
ATOM   3175 C  CG  . GLU B 1 102 ? 114.508 106.983 125.503 1.00 33.18  ? 102 GLU B CG  1 
ATOM   3176 C  CD  . GLU B 1 102 ? 115.948 106.665 125.704 1.00 33.18  ? 102 GLU B CD  1 
ATOM   3177 O  OE1 . GLU B 1 102 ? 116.323 106.371 126.852 1.00 33.18  ? 102 GLU B OE1 1 
ATOM   3178 O  OE2 . GLU B 1 102 ? 116.714 106.719 124.720 1.00 33.18  ? 102 GLU B OE2 1 
ATOM   3179 N  N   . ARG B 1 103 ? 111.382 104.172 127.252 1.00 34.40  ? 103 ARG B N   1 
ATOM   3180 C  CA  . ARG B 1 103 ? 110.334 103.784 128.182 1.00 34.40  ? 103 ARG B CA  1 
ATOM   3181 C  C   . ARG B 1 103 ? 110.511 102.374 128.705 1.00 34.40  ? 103 ARG B C   1 
ATOM   3182 O  O   . ARG B 1 103 ? 109.703 101.930 129.524 1.00 34.40  ? 103 ARG B O   1 
ATOM   3183 C  CB  . ARG B 1 103 ? 108.956 103.888 127.536 1.00 34.40  ? 103 ARG B CB  1 
ATOM   3184 C  CG  . ARG B 1 103 ? 108.587 105.240 127.036 1.00 34.40  ? 103 ARG B CG  1 
ATOM   3185 C  CD  . ARG B 1 103 ? 108.397 106.175 128.178 1.00 34.40  ? 103 ARG B CD  1 
ATOM   3186 N  NE  . ARG B 1 103 ? 109.616 106.914 128.414 1.00 34.40  ? 103 ARG B NE  1 
ATOM   3187 C  CZ  . ARG B 1 103 ? 109.931 108.015 127.752 1.00 34.40  ? 103 ARG B CZ  1 
ATOM   3188 N  NH1 . ARG B 1 103 ? 109.101 108.495 126.844 1.00 34.40  ? 103 ARG B NH1 1 
ATOM   3189 N  NH2 . ARG B 1 103 ? 111.063 108.643 128.011 1.00 34.40  ? 103 ARG B NH2 1 
ATOM   3190 N  N   . PHE B 1 104 ? 111.528 101.659 128.236 1.00 27.56  ? 104 PHE B N   1 
ATOM   3191 C  CA  . PHE B 1 104 ? 111.870 100.346 128.745 1.00 27.56  ? 104 PHE B CA  1 
ATOM   3192 C  C   . PHE B 1 104 ? 112.988 100.398 129.765 1.00 27.56  ? 104 PHE B C   1 
ATOM   3193 O  O   . PHE B 1 104 ? 113.103 99.488  130.588 1.00 27.56  ? 104 PHE B O   1 
ATOM   3194 C  CB  . PHE B 1 104 ? 112.295 99.453  127.585 1.00 27.56  ? 104 PHE B CB  1 
ATOM   3195 C  CG  . PHE B 1 104 ? 111.159 98.852  126.843 1.00 27.56  ? 104 PHE B CG  1 
ATOM   3196 C  CD1 . PHE B 1 104 ? 110.068 98.377  127.500 1.00 27.56  ? 104 PHE B CD1 1 
ATOM   3197 C  CD2 . PHE B 1 104 ? 111.152 98.830  125.477 1.00 27.56  ? 104 PHE B CD2 1 
ATOM   3198 C  CE1 . PHE B 1 104 ? 109.025 97.830  126.811 1.00 27.56  ? 104 PHE B CE1 1 
ATOM   3199 C  CE2 . PHE B 1 104 ? 110.102 98.295  124.795 1.00 27.56  ? 104 PHE B CE2 1 
ATOM   3200 C  CZ  . PHE B 1 104 ? 109.040 97.801  125.464 1.00 27.56  ? 104 PHE B CZ  1 
ATOM   3201 N  N   . ILE B 1 105 ? 113.792 101.458 129.732 1.00 36.59  ? 105 ILE B N   1 
ATOM   3202 C  CA  . ILE B 1 105 ? 114.979 101.596 130.559 1.00 36.59  ? 105 ILE B CA  1 
ATOM   3203 C  C   . ILE B 1 105 ? 114.715 102.449 131.792 1.00 36.59  ? 105 ILE B C   1 
ATOM   3204 O  O   . ILE B 1 105 ? 115.092 102.068 132.903 1.00 36.59  ? 105 ILE B O   1 
ATOM   3205 C  CB  . ILE B 1 105 ? 116.144 102.178 129.730 1.00 36.59  ? 105 ILE B CB  1 
ATOM   3206 C  CG1 . ILE B 1 105 ? 116.746 101.109 128.820 1.00 36.59  ? 105 ILE B CG1 1 
ATOM   3207 C  CG2 . ILE B 1 105 ? 117.194 102.801 130.614 1.00 36.59  ? 105 ILE B CG2 1 
ATOM   3208 C  CD1 . ILE B 1 105 ? 117.756 101.644 127.866 1.00 36.59  ? 105 ILE B CD1 1 
ATOM   3209 N  N   . GLU B 1 106 ? 114.064 103.600 131.625 1.00 43.20  ? 106 GLU B N   1 
ATOM   3210 C  CA  . GLU B 1 106 ? 113.703 104.491 132.727 1.00 43.20  ? 106 GLU B CA  1 
ATOM   3211 C  C   . GLU B 1 106 ? 112.240 104.916 132.627 1.00 43.20  ? 106 GLU B C   1 
ATOM   3212 O  O   . GLU B 1 106 ? 111.930 106.043 132.229 1.00 43.20  ? 106 GLU B O   1 
ATOM   3213 C  CB  . GLU B 1 106 ? 114.639 105.699 132.760 1.00 43.20  ? 106 GLU B CB  1 
ATOM   3214 C  CG  . GLU B 1 106 ? 114.643 106.614 131.515 1.00 43.20  ? 106 GLU B CG  1 
ATOM   3215 C  CD  . GLU B 1 106 ? 115.770 107.646 131.542 1.00 43.20  ? 106 GLU B CD  1 
ATOM   3216 O  OE1 . GLU B 1 106 ? 115.543 108.780 132.018 1.00 43.20  ? 106 GLU B OE1 1 
ATOM   3217 O  OE2 . GLU B 1 106 ? 116.889 107.334 131.080 1.00 43.20  ? 106 GLU B OE2 1 
ATOM   3218 N  N   . PRO B 1 107 ? 111.313 104.042 133.011 1.00 42.92  ? 107 PRO B N   1 
ATOM   3219 C  CA  . PRO B 1 107 ? 109.896 104.327 132.775 1.00 42.92  ? 107 PRO B CA  1 
ATOM   3220 C  C   . PRO B 1 107 ? 109.416 105.498 133.606 1.00 42.92  ? 107 PRO B C   1 
ATOM   3221 O  O   . PRO B 1 107 ? 109.637 105.556 134.813 1.00 42.92  ? 107 PRO B O   1 
ATOM   3222 C  CB  . PRO B 1 107 ? 109.205 103.035 133.208 1.00 42.92  ? 107 PRO B CB  1 
ATOM   3223 C  CG  . PRO B 1 107 ? 110.090 102.491 134.236 1.00 42.92  ? 107 PRO B CG  1 
ATOM   3224 C  CD  . PRO B 1 107 ? 111.488 102.824 133.812 1.00 42.92  ? 107 PRO B CD  1 
ATOM   3225 N  N   . HIS B 1 108 ? 108.786 106.448 132.936 1.00 46.63  ? 108 HIS B N   1 
ATOM   3226 C  CA  . HIS B 1 108 ? 108.255 107.645 133.635 1.00 46.63  ? 108 HIS B CA  1 
ATOM   3227 C  C   . HIS B 1 108 ? 106.850 107.343 134.160 1.00 46.63  ? 108 HIS B C   1 
ATOM   3228 O  O   . HIS B 1 108 ? 106.364 106.217 133.948 1.00 46.63  ? 108 HIS B O   1 
ATOM   3229 C  CB  . HIS B 1 108 ? 108.285 108.866 132.706 1.00 46.63  ? 108 HIS B CB  1 
ATOM   3230 C  CG  . HIS B 1 108 ? 109.660 109.249 132.271 1.00 46.63  ? 108 HIS B CG  1 
ATOM   3231 N  ND1 . HIS B 1 108 ? 110.047 110.566 132.128 1.00 46.63  ? 108 HIS B ND1 1 
ATOM   3232 C  CD2 . HIS B 1 108 ? 110.735 108.500 131.948 1.00 46.63  ? 108 HIS B CD2 1 
ATOM   3233 C  CE1 . HIS B 1 108 ? 111.304 110.612 131.734 1.00 46.63  ? 108 HIS B CE1 1 
ATOM   3234 N  NE2 . HIS B 1 108 ? 111.749 109.356 131.616 1.00 46.63  ? 108 HIS B NE2 1 
ATOM   3235 N  N   . GLU B 1 109 ? 106.233 108.307 134.820 1.00 44.59  ? 109 GLU B N   1 
ATOM   3236 C  CA  . GLU B 1 109 ? 104.894 108.155 135.360 1.00 44.59  ? 109 GLU B CA  1 
ATOM   3237 C  C   . GLU B 1 109 ? 103.964 109.248 134.868 1.00 44.59  ? 109 GLU B C   1 
ATOM   3238 O  O   . GLU B 1 109 ? 104.267 110.438 134.972 1.00 44.59  ? 109 GLU B O   1 
ATOM   3239 C  CB  . GLU B 1 109 ? 104.909 108.134 136.868 1.00 44.59  ? 109 GLU B CB  1 
ATOM   3240 C  CG  . GLU B 1 109 ? 105.145 106.765 137.360 1.00 44.59  ? 109 GLU B CG  1 
ATOM   3241 C  CD  . GLU B 1 109 ? 104.009 105.861 136.970 1.00 44.59  ? 109 GLU B CD  1 
ATOM   3242 O  OE1 . GLU B 1 109 ? 102.853 106.318 136.995 1.00 44.59  ? 109 GLU B OE1 1 
ATOM   3243 O  OE2 . GLU B 1 109 ? 104.270 104.703 136.602 1.00 44.59  ? 109 GLU B OE2 1 
ATOM   3244 N  N   . MET B 1 110 ? 102.820 108.817 134.341 1.00 38.94  ? 110 MET B N   1 
ATOM   3245 C  CA  . MET B 1 110 ? 101.744 109.704 133.919 1.00 38.94  ? 110 MET B CA  1 
ATOM   3246 C  C   . MET B 1 110 ? 101.025 110.163 135.179 1.00 38.94  ? 110 MET B C   1 
ATOM   3247 O  O   . MET B 1 110 ? 100.124 109.503 135.697 1.00 38.94  ? 110 MET B O   1 
ATOM   3248 C  CB  . MET B 1 110 ? 100.807 108.974 132.972 1.00 38.94  ? 110 MET B CB  1 
ATOM   3249 C  CG  . MET B 1 110 ? 99.562  109.722 132.651 1.00 38.94  ? 110 MET B CG  1 
ATOM   3250 S  SD  . MET B 1 110 ? 98.247  108.578 132.266 1.00 38.94  ? 110 MET B SD  1 
ATOM   3251 C  CE  . MET B 1 110 ? 99.147  107.393 131.280 1.00 38.94  ? 110 MET B CE  1 
ATOM   3252 N  N   . GLN B 1 111 ? 101.453 111.313 135.697 1.00 40.15  ? 111 GLN B N   1 
ATOM   3253 C  CA  . GLN B 1 111 ? 100.961 111.759 136.993 1.00 40.15  ? 111 GLN B CA  1 
ATOM   3254 C  C   . GLN B 1 111 ? 99.455  111.983 136.975 1.00 40.15  ? 111 GLN B C   1 
ATOM   3255 O  O   . GLN B 1 111 ? 98.714  111.350 137.734 1.00 40.15  ? 111 GLN B O   1 
ATOM   3256 C  CB  . GLN B 1 111 ? 101.689 113.031 137.415 1.00 40.15  ? 111 GLN B CB  1 
ATOM   3257 C  CG  . GLN B 1 111 ? 103.184 112.858 137.530 1.00 40.15  ? 111 GLN B CG  1 
ATOM   3258 C  CD  . GLN B 1 111 ? 103.615 112.482 138.928 1.00 40.15  ? 111 GLN B CD  1 
ATOM   3259 O  OE1 . GLN B 1 111 ? 102.790 112.140 139.772 1.00 40.15  ? 111 GLN B OE1 1 
ATOM   3260 N  NE2 . GLN B 1 111 ? 104.915 112.548 139.181 1.00 40.15  ? 111 GLN B NE2 1 
ATOM   3261 N  N   . GLN B 1 112 ? 98.977  112.867 136.100 1.00 36.12  ? 112 GLN B N   1 
ATOM   3262 C  CA  . GLN B 1 112 ? 97.569  113.258 136.062 1.00 36.12  ? 112 GLN B CA  1 
ATOM   3263 C  C   . GLN B 1 112 ? 96.892  112.529 134.910 1.00 36.12  ? 112 GLN B C   1 
ATOM   3264 O  O   . GLN B 1 112 ? 97.013  112.943 133.749 1.00 36.12  ? 112 GLN B O   1 
ATOM   3265 C  CB  . GLN B 1 112 ? 97.432  114.772 135.924 1.00 36.12  ? 112 GLN B CB  1 
ATOM   3266 N  N   . PRO B 1 113 ? 96.173  111.438 135.179 1.00 34.42  ? 113 PRO B N   1 
ATOM   3267 C  CA  . PRO B 1 113 ? 95.615  110.646 134.078 1.00 34.42  ? 113 PRO B CA  1 
ATOM   3268 C  C   . PRO B 1 113 ? 94.270  111.125 133.595 1.00 34.42  ? 113 PRO B C   1 
ATOM   3269 O  O   . PRO B 1 113 ? 93.964  110.937 132.415 1.00 34.42  ? 113 PRO B O   1 
ATOM   3270 C  CB  . PRO B 1 113 ? 95.505  109.256 134.685 1.00 34.42  ? 113 PRO B CB  1 
ATOM   3271 C  CG  . PRO B 1 113 ? 95.168  109.551 136.089 1.00 34.42  ? 113 PRO B CG  1 
ATOM   3272 C  CD  . PRO B 1 113 ? 95.889  110.822 136.477 1.00 34.42  ? 113 PRO B CD  1 
ATOM   3273 N  N   . LEU B 1 114 ? 93.443  111.720 134.448 1.00 30.24  ? 114 LEU B N   1 
ATOM   3274 C  CA  . LEU B 1 114 ? 92.189  112.263 133.946 1.00 30.24  ? 114 LEU B CA  1 
ATOM   3275 C  C   . LEU B 1 114 ? 92.444  113.343 132.905 1.00 30.24  ? 114 LEU B C   1 
ATOM   3276 O  O   . LEU B 1 114 ? 91.837  113.328 131.829 1.00 30.24  ? 114 LEU B O   1 
ATOM   3277 C  CB  . LEU B 1 114 ? 91.346  112.809 135.100 1.00 30.24  ? 114 LEU B CB  1 
ATOM   3278 C  CG  . LEU B 1 114 ? 90.235  113.833 134.809 1.00 30.24  ? 114 LEU B CG  1 
ATOM   3279 C  CD1 . LEU B 1 114 ? 88.995  113.188 134.195 1.00 30.24  ? 114 LEU B CD1 1 
ATOM   3280 C  CD2 . LEU B 1 114 ? 89.860  114.617 136.066 1.00 30.24  ? 114 LEU B CD2 1 
ATOM   3281 N  N   . VAL B 1 115 ? 93.364  114.265 133.180 1.00 26.03  ? 115 VAL B N   1 
ATOM   3282 C  CA  . VAL B 1 115 ? 93.572  115.361 132.247 1.00 26.03  ? 115 VAL B CA  1 
ATOM   3283 C  C   . VAL B 1 115 ? 94.177  114.850 130.950 1.00 26.03  ? 115 VAL B C   1 
ATOM   3284 O  O   . VAL B 1 115 ? 93.832  115.329 129.864 1.00 26.03  ? 115 VAL B O   1 
ATOM   3285 C  CB  . VAL B 1 115 ? 94.432  116.461 132.885 1.00 26.03  ? 115 VAL B CB  1 
ATOM   3286 C  CG1 . VAL B 1 115 ? 95.876  116.066 132.936 1.00 26.03  ? 115 VAL B CG1 1 
ATOM   3287 C  CG2 . VAL B 1 115 ? 94.285  117.722 132.110 1.00 26.03  ? 115 VAL B CG2 1 
ATOM   3288 N  N   . VAL B 1 116 ? 95.076  113.867 131.027 1.00 25.95  ? 116 VAL B N   1 
ATOM   3289 C  CA  . VAL B 1 116 ? 95.675  113.349 129.801 1.00 25.95  ? 116 VAL B CA  1 
ATOM   3290 C  C   . VAL B 1 116 ? 94.634  112.615 128.983 1.00 25.95  ? 116 VAL B C   1 
ATOM   3291 O  O   . VAL B 1 116 ? 94.611  112.721 127.759 1.00 25.95  ? 116 VAL B O   1 
ATOM   3292 C  CB  . VAL B 1 116 ? 96.888  112.457 130.099 1.00 25.95  ? 116 VAL B CB  1 
ATOM   3293 C  CG1 . VAL B 1 116 ? 97.189  111.599 128.900 1.00 25.95  ? 116 VAL B CG1 1 
ATOM   3294 C  CG2 . VAL B 1 116 ? 98.091  113.306 130.435 1.00 25.95  ? 116 VAL B CG2 1 
ATOM   3295 N  N   . LEU B 1 117 ? 93.743  111.876 129.639 1.00 25.20  ? 117 LEU B N   1 
ATOM   3296 C  CA  . LEU B 1 117 ? 92.645  111.270 128.900 1.00 25.20  ? 117 LEU B CA  1 
ATOM   3297 C  C   . LEU B 1 117 ? 91.805  112.336 128.229 1.00 25.20  ? 117 LEU B C   1 
ATOM   3298 O  O   . LEU B 1 117 ? 91.374  112.169 127.084 1.00 25.20  ? 117 LEU B O   1 
ATOM   3299 C  CB  . LEU B 1 117 ? 91.783  110.423 129.820 1.00 25.20  ? 117 LEU B CB  1 
ATOM   3300 C  CG  . LEU B 1 117 ? 90.449  110.004 129.230 1.00 25.20  ? 117 LEU B CG  1 
ATOM   3301 C  CD1 . LEU B 1 117 ? 90.651  109.279 127.931 1.00 25.20  ? 117 LEU B CD1 1 
ATOM   3302 C  CD2 . LEU B 1 117 ? 89.737  109.113 130.213 1.00 25.20  ? 117 LEU B CD2 1 
ATOM   3303 N  N   . GLY B 1 118 ? 91.584  113.454 128.915 1.00 25.12  ? 118 GLY B N   1 
ATOM   3304 C  CA  . GLY B 1 118 ? 90.799  114.522 128.314 1.00 25.12  ? 118 GLY B CA  1 
ATOM   3305 C  C   . GLY B 1 118 ? 91.419  115.057 127.036 1.00 25.12  ? 118 GLY B C   1 
ATOM   3306 O  O   . GLY B 1 118 ? 90.795  115.046 125.968 1.00 25.12  ? 118 GLY B O   1 
ATOM   3307 N  N   . VAL B 1 119 ? 92.662  115.520 127.120 1.00 23.92  ? 119 VAL B N   1 
ATOM   3308 C  CA  . VAL B 1 119 ? 93.238  116.117 125.924 1.00 23.92  ? 119 VAL B CA  1 
ATOM   3309 C  C   . VAL B 1 119 ? 93.533  115.058 124.879 1.00 23.92  ? 119 VAL B C   1 
ATOM   3310 O  O   . VAL B 1 119 ? 93.531  115.349 123.681 1.00 23.92  ? 119 VAL B O   1 
ATOM   3311 C  CB  . VAL B 1 119 ? 94.485  116.934 126.253 1.00 23.92  ? 119 VAL B CB  1 
ATOM   3312 C  CG1 . VAL B 1 119 ? 94.195  117.822 127.423 1.00 23.92  ? 119 VAL B CG1 1 
ATOM   3313 C  CG2 . VAL B 1 119 ? 95.648  116.020 126.489 1.00 23.92  ? 119 VAL B CG2 1 
ATOM   3314 N  N   . GLY B 1 120 ? 93.742  113.813 125.286 1.00 21.93  ? 120 GLY B N   1 
ATOM   3315 C  CA  . GLY B 1 120 ? 93.940  112.769 124.302 1.00 21.93  ? 120 GLY B CA  1 
ATOM   3316 C  C   . GLY B 1 120 ? 92.681  112.474 123.520 1.00 21.93  ? 120 GLY B C   1 
ATOM   3317 O  O   . GLY B 1 120 ? 92.738  112.217 122.319 1.00 21.93  ? 120 GLY B O   1 
ATOM   3318 N  N   . VAL B 1 121 ? 91.524  112.524 124.177 1.00 23.71  ? 121 VAL B N   1 
ATOM   3319 C  CA  . VAL B 1 121 ? 90.295  112.278 123.442 1.00 23.71  ? 121 VAL B CA  1 
ATOM   3320 C  C   . VAL B 1 121 ? 89.953  113.479 122.570 1.00 23.71  ? 121 VAL B C   1 
ATOM   3321 O  O   . VAL B 1 121 ? 89.429  113.322 121.460 1.00 23.71  ? 121 VAL B O   1 
ATOM   3322 C  CB  . VAL B 1 121 ? 89.148  111.902 124.393 1.00 23.71  ? 121 VAL B CB  1 
ATOM   3323 C  CG1 . VAL B 1 121 ? 88.522  113.123 125.003 1.00 23.71  ? 121 VAL B CG1 1 
ATOM   3324 C  CG2 . VAL B 1 121 ? 88.119  111.077 123.660 1.00 23.71  ? 121 VAL B CG2 1 
ATOM   3325 N  N   . ALA B 1 122 ? 90.291  114.689 123.013 1.00 24.49  ? 122 ALA B N   1 
ATOM   3326 C  CA  . ALA B 1 122 ? 90.091  115.832 122.126 1.00 24.49  ? 122 ALA B CA  1 
ATOM   3327 C  C   . ALA B 1 122 ? 90.958  115.711 120.877 1.00 24.49  ? 122 ALA B C   1 
ATOM   3328 O  O   . ALA B 1 122 ? 90.475  115.898 119.755 1.00 24.49  ? 122 ALA B O   1 
ATOM   3329 C  CB  . ALA B 1 122 ? 90.379  117.137 122.854 1.00 24.49  ? 122 ALA B CB  1 
ATOM   3330 N  N   . GLY B 1 123 ? 92.237  115.382 121.050 1.00 24.79  ? 123 GLY B N   1 
ATOM   3331 C  CA  . GLY B 1 123 ? 93.108  115.209 119.899 1.00 24.79  ? 123 GLY B CA  1 
ATOM   3332 C  C   . GLY B 1 123 ? 92.678  114.072 118.992 1.00 24.79  ? 123 GLY B C   1 
ATOM   3333 O  O   . GLY B 1 123 ? 92.772  114.170 117.768 1.00 24.79  ? 123 GLY B O   1 
ATOM   3334 N  N   . LEU B 1 124 ? 92.194  112.980 119.576 1.00 26.65  ? 124 LEU B N   1 
ATOM   3335 C  CA  . LEU B 1 124 ? 91.722  111.857 118.775 1.00 26.65  ? 124 LEU B CA  1 
ATOM   3336 C  C   . LEU B 1 124 ? 90.513  112.245 117.939 1.00 26.65  ? 124 LEU B C   1 
ATOM   3337 O  O   . LEU B 1 124 ? 90.384  111.810 116.794 1.00 26.65  ? 124 LEU B O   1 
ATOM   3338 C  CB  . LEU B 1 124 ? 91.409  110.676 119.694 1.00 26.65  ? 124 LEU B CB  1 
ATOM   3339 C  CG  . LEU B 1 124 ? 90.473  109.550 119.285 1.00 26.65  ? 124 LEU B CG  1 
ATOM   3340 C  CD1 . LEU B 1 124 ? 91.005  108.847 118.070 1.00 26.65  ? 124 LEU B CD1 1 
ATOM   3341 C  CD2 . LEU B 1 124 ? 90.319  108.578 120.438 1.00 26.65  ? 124 LEU B CD2 1 
ATOM   3342 N  N   . LEU B 1 125 ? 89.633  113.089 118.475 1.00 24.34  ? 125 LEU B N   1 
ATOM   3343 C  CA  . LEU B 1 125 ? 88.502  113.541 117.673 1.00 24.34  ? 125 LEU B CA  1 
ATOM   3344 C  C   . LEU B 1 125 ? 88.933  114.507 116.573 1.00 24.34  ? 125 LEU B C   1 
ATOM   3345 O  O   . LEU B 1 125 ? 88.442  114.420 115.438 1.00 24.34  ? 125 LEU B O   1 
ATOM   3346 C  CB  . LEU B 1 125 ? 87.446  114.179 118.562 1.00 24.34  ? 125 LEU B CB  1 
ATOM   3347 C  CG  . LEU B 1 125 ? 86.842  113.218 119.581 1.00 24.34  ? 125 LEU B CG  1 
ATOM   3348 C  CD1 . LEU B 1 125 ? 85.501  113.729 120.072 1.00 24.34  ? 125 LEU B CD1 1 
ATOM   3349 C  CD2 . LEU B 1 125 ? 86.694  111.829 118.995 1.00 24.34  ? 125 LEU B CD2 1 
ATOM   3350 N  N   . VAL B 1 126 ? 89.854  115.428 116.870 1.00 26.69  ? 126 VAL B N   1 
ATOM   3351 C  CA  . VAL B 1 126 ? 90.268  116.345 115.809 1.00 26.69  ? 126 VAL B CA  1 
ATOM   3352 C  C   . VAL B 1 126 ? 90.990  115.588 114.703 1.00 26.69  ? 126 VAL B C   1 
ATOM   3353 O  O   . VAL B 1 126 ? 90.854  115.925 113.525 1.00 26.69  ? 126 VAL B O   1 
ATOM   3354 C  CB  . VAL B 1 126 ? 91.132  117.500 116.342 1.00 26.69  ? 126 VAL B CB  1 
ATOM   3355 C  CG1 . VAL B 1 126 ? 92.580  117.117 116.423 1.00 26.69  ? 126 VAL B CG1 1 
ATOM   3356 C  CG2 . VAL B 1 126 ? 90.985  118.673 115.460 1.00 26.69  ? 126 VAL B CG2 1 
ATOM   3357 N  N   . ASN B 1 127 ? 91.723  114.520 115.031 1.00 31.20  ? 127 ASN B N   1 
ATOM   3358 C  CA  . ASN B 1 127 ? 92.377  113.764 113.966 1.00 31.20  ? 127 ASN B CA  1 
ATOM   3359 C  C   . ASN B 1 127 ? 91.424  112.806 113.266 1.00 31.20  ? 127 ASN B C   1 
ATOM   3360 O  O   . ASN B 1 127 ? 91.623  112.512 112.089 1.00 31.20  ? 127 ASN B O   1 
ATOM   3361 C  CB  . ASN B 1 127 ? 93.596  113.023 114.497 1.00 31.20  ? 127 ASN B CB  1 
ATOM   3362 C  CG  . ASN B 1 127 ? 94.723  113.962 114.845 1.00 31.20  ? 127 ASN B CG  1 
ATOM   3363 O  OD1 . ASN B 1 127 ? 95.102  114.101 116.005 1.00 31.20  ? 127 ASN B OD1 1 
ATOM   3364 N  ND2 . ASN B 1 127 ? 95.263  114.624 113.837 1.00 31.20  ? 127 ASN B ND2 1 
ATOM   3365 N  N   . VAL B 1 128 ? 90.385  112.311 113.938 1.00 28.68  ? 128 VAL B N   1 
ATOM   3366 C  CA  . VAL B 1 128 ? 89.372  111.577 113.189 1.00 28.68  ? 128 VAL B CA  1 
ATOM   3367 C  C   . VAL B 1 128 ? 88.741  112.484 112.157 1.00 28.68  ? 128 VAL B C   1 
ATOM   3368 O  O   . VAL B 1 128 ? 88.450  112.057 111.038 1.00 28.68  ? 128 VAL B O   1 
ATOM   3369 C  CB  . VAL B 1 128 ? 88.310  110.969 114.114 1.00 28.68  ? 128 VAL B CB  1 
ATOM   3370 C  CG1 . VAL B 1 128 ? 87.024  110.773 113.353 1.00 28.68  ? 128 VAL B CG1 1 
ATOM   3371 C  CG2 . VAL B 1 128 ? 88.780  109.637 114.637 1.00 28.68  ? 128 VAL B CG2 1 
ATOM   3372 N  N   . LEU B 1 129 ? 88.547  113.758 112.494 1.00 31.07  ? 129 LEU B N   1 
ATOM   3373 C  CA  . LEU B 1 129 ? 88.053  114.686 111.476 1.00 31.07  ? 129 LEU B CA  1 
ATOM   3374 C  C   . LEU B 1 129 ? 89.092  114.931 110.386 1.00 31.07  ? 129 LEU B C   1 
ATOM   3375 O  O   . LEU B 1 129 ? 88.752  114.967 109.199 1.00 31.07  ? 129 LEU B O   1 
ATOM   3376 C  CB  . LEU B 1 129 ? 87.631  116.006 112.100 1.00 31.07  ? 129 LEU B CB  1 
ATOM   3377 C  CG  . LEU B 1 129 ? 86.839  116.877 111.134 1.00 31.07  ? 129 LEU B CG  1 
ATOM   3378 C  CD1 . LEU B 1 129 ? 85.787  117.628 111.909 1.00 31.07  ? 129 LEU B CD1 1 
ATOM   3379 C  CD2 . LEU B 1 129 ? 87.739  117.841 110.397 1.00 31.07  ? 129 LEU B CD2 1 
ATOM   3380 N  N   . GLY B 1 130 ? 90.353  115.120 110.765 1.00 30.17  ? 130 GLY B N   1 
ATOM   3381 C  CA  . GLY B 1 130 ? 91.386  115.334 109.764 1.00 30.17  ? 130 GLY B CA  1 
ATOM   3382 C  C   . GLY B 1 130 ? 91.576  114.140 108.846 1.00 30.17  ? 130 GLY B C   1 
ATOM   3383 O  O   . GLY B 1 130 ? 92.115  114.264 107.748 1.00 30.17  ? 130 GLY B O   1 
ATOM   3384 N  N   . LEU B 1 131 ? 91.169  112.963 109.303 1.00 33.20  ? 131 LEU B N   1 
ATOM   3385 C  CA  . LEU B 1 131 ? 91.237  111.769 108.474 1.00 33.20  ? 131 LEU B CA  1 
ATOM   3386 C  C   . LEU B 1 131 ? 89.997  111.642 107.604 1.00 33.20  ? 131 LEU B C   1 
ATOM   3387 O  O   . LEU B 1 131 ? 90.094  111.295 106.425 1.00 33.20  ? 131 LEU B O   1 
ATOM   3388 C  CB  . LEU B 1 131 ? 91.405  110.550 109.376 1.00 33.20  ? 131 LEU B CB  1 
ATOM   3389 C  CG  . LEU B 1 131 ? 91.499  109.098 108.934 1.00 33.20  ? 131 LEU B CG  1 
ATOM   3390 C  CD1 . LEU B 1 131 ? 92.090  108.333 110.092 1.00 33.20  ? 131 LEU B CD1 1 
ATOM   3391 C  CD2 . LEU B 1 131 ? 90.144  108.515 108.589 1.00 33.20  ? 131 LEU B CD2 1 
ATOM   3392 N  N   . CYS B 1 132 ? 88.820  111.902 108.175 1.00 30.90  ? 132 CYS B N   1 
ATOM   3393 C  CA  . CYS B 1 132 ? 87.580  111.833 107.421 1.00 30.90  ? 132 CYS B CA  1 
ATOM   3394 C  C   . CYS B 1 132 ? 87.455  112.977 106.435 1.00 30.90  ? 132 CYS B C   1 
ATOM   3395 O  O   . CYS B 1 132 ? 86.525  112.982 105.628 1.00 30.90  ? 132 CYS B O   1 
ATOM   3396 C  CB  . CYS B 1 132 ? 86.395  111.835 108.376 1.00 30.90  ? 132 CYS B CB  1 
ATOM   3397 S  SG  . CYS B 1 132 ? 84.825  111.430 107.637 1.00 30.90  ? 132 CYS B SG  1 
ATOM   3398 N  N   . LEU B 1 133 ? 88.356  113.954 106.494 1.00 30.30  ? 133 LEU B N   1 
ATOM   3399 C  CA  . LEU B 1 133 ? 88.373  115.000 105.481 1.00 30.30  ? 133 LEU B CA  1 
ATOM   3400 C  C   . LEU B 1 133 ? 88.913  114.478 104.157 1.00 30.30  ? 133 LEU B C   1 
ATOM   3401 O  O   . LEU B 1 133 ? 88.421  114.858 103.092 1.00 30.30  ? 133 LEU B O   1 
ATOM   3402 C  CB  . LEU B 1 133 ? 89.201  116.177 105.970 1.00 30.30  ? 133 LEU B CB  1 
ATOM   3403 C  CG  . LEU B 1 133 ? 89.063  117.463 105.192 1.00 30.30  ? 133 LEU B CG  1 
ATOM   3404 C  CD1 . LEU B 1 133 ? 87.618  117.837 105.174 1.00 30.30  ? 133 LEU B CD1 1 
ATOM   3405 C  CD2 . LEU B 1 133 ? 89.869  118.525 105.880 1.00 30.30  ? 133 LEU B CD2 1 
ATOM   3406 N  N   . PHE B 1 134 ? 89.925  113.611 104.203 1.00 31.58  ? 134 PHE B N   1 
ATOM   3407 C  CA  . PHE B 1 134 ? 90.490  112.983 103.008 1.00 31.58  ? 134 PHE B CA  1 
ATOM   3408 C  C   . PHE B 1 134 ? 89.876  111.617 102.748 1.00 31.58  ? 134 PHE B C   1 
ATOM   3409 O  O   . PHE B 1 134 ? 89.154  111.429 101.775 1.00 31.58  ? 134 PHE B O   1 
ATOM   3410 C  CB  . PHE B 1 134 ? 91.993  112.833 103.145 1.00 31.58  ? 134 PHE B CB  1 
ATOM   3411 C  CG  . PHE B 1 134 ? 92.684  114.080 103.562 1.00 31.58  ? 134 PHE B CG  1 
ATOM   3412 C  CD1 . PHE B 1 134 ? 92.975  115.057 102.650 1.00 31.58  ? 134 PHE B CD1 1 
ATOM   3413 C  CD2 . PHE B 1 134 ? 93.038  114.280 104.874 1.00 31.58  ? 134 PHE B CD2 1 
ATOM   3414 C  CE1 . PHE B 1 134 ? 93.615  116.205 103.044 1.00 31.58  ? 134 PHE B CE1 1 
ATOM   3415 C  CE2 . PHE B 1 134 ? 93.679  115.425 105.269 1.00 31.58  ? 134 PHE B CE2 1 
ATOM   3416 C  CZ  . PHE B 1 134 ? 93.964  116.387 104.358 1.00 31.58  ? 134 PHE B CZ  1 
ATOM   3417 N  N   . GLY B 1 241 ? 96.948  116.363 91.684  1.00 25.24  ? 241 GLY B N   1 
ATOM   3418 C  CA  . GLY B 1 241 ? 97.521  116.063 92.983  1.00 25.24  ? 241 GLY B CA  1 
ATOM   3419 C  C   . GLY B 1 241 ? 97.006  114.762 93.556  1.00 25.24  ? 241 GLY B C   1 
ATOM   3420 O  O   . GLY B 1 241 ? 96.063  114.743 94.342  1.00 25.24  ? 241 GLY B O   1 
ATOM   3421 N  N   . GLN B 1 242 ? 97.633  113.663 93.158  1.00 29.91  ? 242 GLN B N   1 
ATOM   3422 C  CA  . GLN B 1 242 ? 97.201  112.347 93.598  1.00 29.91  ? 242 GLN B CA  1 
ATOM   3423 C  C   . GLN B 1 242 ? 98.153  111.692 94.571  1.00 29.91  ? 242 GLN B C   1 
ATOM   3424 O  O   . GLN B 1 242 ? 97.794  110.659 95.138  1.00 29.91  ? 242 GLN B O   1 
ATOM   3425 C  CB  . GLN B 1 242 ? 97.015  111.418 92.392  1.00 29.91  ? 242 GLN B CB  1 
ATOM   3426 C  CG  . GLN B 1 242 ? 98.311  111.125 91.652  1.00 29.91  ? 242 GLN B CG  1 
ATOM   3427 C  CD  . GLN B 1 242 ? 98.133  110.169 90.491  1.00 29.91  ? 242 GLN B CD  1 
ATOM   3428 O  OE1 . GLN B 1 242 ? 97.682  109.037 90.664  1.00 29.91  ? 242 GLN B OE1 1 
ATOM   3429 N  NE2 . GLN B 1 242 ? 98.491  110.623 89.298  1.00 29.91  ? 242 GLN B NE2 1 
ATOM   3430 N  N   . LEU B 1 243 ? 99.351  112.234 94.774  1.00 28.00  ? 243 LEU B N   1 
ATOM   3431 C  CA  . LEU B 1 243 ? 100.261 111.686 95.770  1.00 28.00  ? 243 LEU B CA  1 
ATOM   3432 C  C   . LEU B 1 243 ? 100.384 112.609 96.975  1.00 28.00  ? 243 LEU B C   1 
ATOM   3433 O  O   . LEU B 1 243 ? 100.855 112.195 98.032  1.00 28.00  ? 243 LEU B O   1 
ATOM   3434 C  CB  . LEU B 1 243 ? 101.630 111.414 95.153  1.00 28.00  ? 243 LEU B CB  1 
ATOM   3435 C  CG  . LEU B 1 243 ? 101.678 110.153 94.307  1.00 28.00  ? 243 LEU B CG  1 
ATOM   3436 C  CD1 . LEU B 1 243 ? 103.070 109.922 93.834  1.00 28.00  ? 243 LEU B CD1 1 
ATOM   3437 C  CD2 . LEU B 1 243 ? 101.202 108.980 95.103  1.00 28.00  ? 243 LEU B CD2 1 
ATOM   3438 N  N   . ASN B 1 244 ? 99.974  113.867 96.845  1.00 26.97  ? 244 ASN B N   1 
ATOM   3439 C  CA  . ASN B 1 244 ? 99.868  114.676 98.050  1.00 26.97  ? 244 ASN B CA  1 
ATOM   3440 C  C   . ASN B 1 244 ? 98.755  114.187 98.959  1.00 26.97  ? 244 ASN B C   1 
ATOM   3441 O  O   . ASN B 1 244 ? 98.924  114.160 100.184 1.00 26.97  ? 244 ASN B O   1 
ATOM   3442 C  CB  . ASN B 1 244 ? 99.662  116.133 97.706  1.00 26.97  ? 244 ASN B CB  1 
ATOM   3443 C  CG  . ASN B 1 244 ? 100.943 116.821 97.445  1.00 26.97  ? 244 ASN B CG  1 
ATOM   3444 O  OD1 . ASN B 1 244 ? 101.958 116.469 98.022  1.00 26.97  ? 244 ASN B OD1 1 
ATOM   3445 N  ND2 . ASN B 1 244 ? 100.913 117.833 96.604  1.00 26.97  ? 244 ASN B ND2 1 
ATOM   3446 N  N   . MET B 1 245 ? 97.611  113.813 98.393  1.00 34.15  ? 245 MET B N   1 
ATOM   3447 C  CA  . MET B 1 245 ? 96.582  113.151 99.183  1.00 34.15  ? 245 MET B CA  1 
ATOM   3448 C  C   . MET B 1 245 ? 97.178  112.036 100.033 1.00 34.15  ? 245 MET B C   1 
ATOM   3449 O  O   . MET B 1 245 ? 96.957  111.982 101.245 1.00 34.15  ? 245 MET B O   1 
ATOM   3450 C  CB  . MET B 1 245 ? 95.491  112.591 98.274  1.00 34.15  ? 245 MET B CB  1 
ATOM   3451 C  CG  . MET B 1 245 ? 94.572  111.611 98.980  1.00 34.15  ? 245 MET B CG  1 
ATOM   3452 S  SD  . MET B 1 245 ? 93.375  110.838 97.895  1.00 34.15  ? 245 MET B SD  1 
ATOM   3453 C  CE  . MET B 1 245 ? 92.770  109.569 98.989  1.00 34.15  ? 245 MET B CE  1 
ATOM   3454 N  N   . ARG B 1 246 ? 97.946  111.150 99.413  1.00 31.40  ? 246 ARG B N   1 
ATOM   3455 C  CA  . ARG B 1 246 ? 98.528  110.000 100.153 1.00 31.40  ? 246 ARG B CA  1 
ATOM   3456 C  C   . ARG B 1 246 ? 99.592  110.480 101.143 1.00 31.40  ? 246 ARG B C   1 
ATOM   3457 O  O   . ARG B 1 246 ? 99.591  109.987 102.277 1.00 31.40  ? 246 ARG B O   1 
ATOM   3458 C  CB  . ARG B 1 246 ? 99.114  108.982 99.174  1.00 31.40  ? 246 ARG B CB  1 
ATOM   3459 C  CG  . ARG B 1 246 ? 98.366  107.659 99.148  1.00 31.40  ? 246 ARG B CG  1 
ATOM   3460 C  CD  . ARG B 1 246 ? 98.128  107.182 97.729  1.00 31.40  ? 246 ARG B CD  1 
ATOM   3461 N  NE  . ARG B 1 246 ? 99.335  106.640 97.124  1.00 31.40  ? 246 ARG B NE  1 
ATOM   3462 C  CZ  . ARG B 1 246 ? 99.342  105.773 96.120  1.00 31.40  ? 246 ARG B CZ  1 
ATOM   3463 N  NH1 . ARG B 1 246 ? 98.201  105.352 95.604  1.00 31.40  ? 246 ARG B NH1 1 
ATOM   3464 N  NH2 . ARG B 1 246 ? 100.489 105.329 95.636  1.00 31.40  ? 246 ARG B NH2 1 
ATOM   3465 N  N   . GLY B 1 247 ? 100.456 111.399 100.753 1.00 27.08  ? 247 GLY B N   1 
ATOM   3466 C  CA  . GLY B 1 247 ? 101.515 111.861 101.622 1.00 27.08  ? 247 GLY B CA  1 
ATOM   3467 C  C   . GLY B 1 247 ? 101.031 112.628 102.826 1.00 27.08  ? 247 GLY B C   1 
ATOM   3468 O  O   . GLY B 1 247 ? 101.795 112.808 103.772 1.00 27.08  ? 247 GLY B O   1 
ATOM   3469 N  N   . VAL B 1 248 ? 99.790  113.106 102.810 1.00 24.62  ? 248 VAL B N   1 
ATOM   3470 C  CA  . VAL B 1 248 ? 99.240  113.788 103.976 1.00 24.62  ? 248 VAL B CA  1 
ATOM   3471 C  C   . VAL B 1 248 ? 98.272  112.891 104.744 1.00 24.62  ? 248 VAL B C   1 
ATOM   3472 O  O   . VAL B 1 248 ? 98.169  112.978 105.976 1.00 24.62  ? 248 VAL B O   1 
ATOM   3473 C  CB  . VAL B 1 248 ? 98.578  115.105 103.567 1.00 24.62  ? 248 VAL B CB  1 
ATOM   3474 C  CG1 . VAL B 1 248 ? 97.710  115.608 104.668 1.00 24.62  ? 248 VAL B CG1 1 
ATOM   3475 C  CG2 . VAL B 1 248 ? 99.631  116.101 103.273 1.00 24.62  ? 248 VAL B CG2 1 
ATOM   3476 N  N   . PHE B 1 249 ? 97.571  112.002 104.044 1.00 27.28  ? 249 PHE B N   1 
ATOM   3477 C  CA  . PHE B 1 249 ? 96.680  111.099 104.754 1.00 27.28  ? 249 PHE B CA  1 
ATOM   3478 C  C   . PHE B 1 249 ? 97.453  110.172 105.666 1.00 27.28  ? 249 PHE B C   1 
ATOM   3479 O  O   . PHE B 1 249 ? 97.024  109.904 106.793 1.00 27.28  ? 249 PHE B O   1 
ATOM   3480 C  CB  . PHE B 1 249 ? 95.856  110.268 103.797 1.00 27.28  ? 249 PHE B CB  1 
ATOM   3481 C  CG  . PHE B 1 249 ? 95.199  109.124 104.463 1.00 27.28  ? 249 PHE B CG  1 
ATOM   3482 C  CD1 . PHE B 1 249 ? 94.265  109.337 105.441 1.00 27.28  ? 249 PHE B CD1 1 
ATOM   3483 C  CD2 . PHE B 1 249 ? 95.526  107.839 104.144 1.00 27.28  ? 249 PHE B CD2 1 
ATOM   3484 C  CE1 . PHE B 1 249 ? 93.654  108.303 106.072 1.00 27.28  ? 249 PHE B CE1 1 
ATOM   3485 C  CE2 . PHE B 1 249 ? 94.913  106.793 104.777 1.00 27.28  ? 249 PHE B CE2 1 
ATOM   3486 C  CZ  . PHE B 1 249 ? 93.976  107.029 105.745 1.00 27.28  ? 249 PHE B CZ  1 
ATOM   3487 N  N   . LEU B 1 250 ? 98.585  109.652 105.196 1.00 22.38  ? 250 LEU B N   1 
ATOM   3488 C  CA  . LEU B 1 250 ? 99.415  108.835 106.074 1.00 22.38  ? 250 LEU B CA  1 
ATOM   3489 C  C   . LEU B 1 250 ? 99.868  109.626 107.280 1.00 22.38  ? 250 LEU B C   1 
ATOM   3490 O  O   . LEU B 1 250 ? 99.900  109.113 108.404 1.00 22.38  ? 250 LEU B O   1 
ATOM   3491 C  CB  . LEU B 1 250 ? 100.615 108.306 105.315 1.00 22.38  ? 250 LEU B CB  1 
ATOM   3492 C  CG  . LEU B 1 250 ? 100.132 107.081 104.579 1.00 22.38  ? 250 LEU B CG  1 
ATOM   3493 C  CD1 . LEU B 1 250 ? 101.257 106.460 103.800 1.00 22.38  ? 250 LEU B CD1 1 
ATOM   3494 C  CD2 . LEU B 1 250 ? 99.567  106.142 105.608 1.00 22.38  ? 250 LEU B CD2 1 
ATOM   3495 N  N   . HIS B 1 251 ? 100.191 110.888 107.068 1.00 30.66  ? 251 HIS B N   1 
ATOM   3496 C  CA  . HIS B 1 251 ? 100.707 111.700 108.143 1.00 30.66  ? 251 HIS B CA  1 
ATOM   3497 C  C   . HIS B 1 251 ? 99.660  112.011 109.193 1.00 30.66  ? 251 HIS B C   1 
ATOM   3498 O  O   . HIS B 1 251 ? 100.024 112.264 110.342 1.00 30.66  ? 251 HIS B O   1 
ATOM   3499 C  CB  . HIS B 1 251 ? 101.264 112.978 107.571 1.00 30.66  ? 251 HIS B CB  1 
ATOM   3500 C  CG  . HIS B 1 251 ? 102.362 113.549 108.383 1.00 30.66  ? 251 HIS B CG  1 
ATOM   3501 N  ND1 . HIS B 1 251 ? 102.134 114.181 109.581 1.00 30.66  ? 251 HIS B ND1 1 
ATOM   3502 C  CD2 . HIS B 1 251 ? 103.697 113.559 108.190 1.00 30.66  ? 251 HIS B CD2 1 
ATOM   3503 C  CE1 . HIS B 1 251 ? 103.288 114.576 110.088 1.00 30.66  ? 251 HIS B CE1 1 
ATOM   3504 N  NE2 . HIS B 1 251 ? 104.252 114.212 109.261 1.00 30.66  ? 251 HIS B NE2 1 
ATOM   3505 N  N   . VAL B 1 252 ? 98.378  112.028 108.830 1.00 29.39  ? 252 VAL B N   1 
ATOM   3506 C  CA  . VAL B 1 252 ? 97.352  112.191 109.862 1.00 29.39  ? 252 VAL B CA  1 
ATOM   3507 C  C   . VAL B 1 252 ? 96.973  110.853 110.492 1.00 29.39  ? 252 VAL B C   1 
ATOM   3508 O  O   . VAL B 1 252 ? 96.615  110.809 111.672 1.00 29.39  ? 252 VAL B O   1 
ATOM   3509 C  CB  . VAL B 1 252 ? 96.098  112.910 109.339 1.00 29.39  ? 252 VAL B CB  1 
ATOM   3510 C  CG1 . VAL B 1 252 ? 96.479  114.065 108.438 1.00 29.39  ? 252 VAL B CG1 1 
ATOM   3511 C  CG2 . VAL B 1 252 ? 95.149  111.947 108.670 1.00 29.39  ? 252 VAL B CG2 1 
ATOM   3512 N  N   . LEU B 1 253 ? 97.052  109.753 109.740 1.00 25.77  ? 253 LEU B N   1 
ATOM   3513 C  CA  . LEU B 1 253 ? 96.848  108.446 110.350 1.00 25.77  ? 253 LEU B CA  1 
ATOM   3514 C  C   . LEU B 1 253 ? 97.874  108.192 111.437 1.00 25.77  ? 253 LEU B C   1 
ATOM   3515 O  O   . LEU B 1 253 ? 97.567  107.558 112.453 1.00 25.77  ? 253 LEU B O   1 
ATOM   3516 C  CB  . LEU B 1 253 ? 96.931  107.357 109.291 1.00 25.77  ? 253 LEU B CB  1 
ATOM   3517 C  CG  . LEU B 1 253 ? 96.701  105.934 109.750 1.00 25.77  ? 253 LEU B CG  1 
ATOM   3518 C  CD1 . LEU B 1 253 ? 95.247  105.792 110.043 1.00 25.77  ? 253 LEU B CD1 1 
ATOM   3519 C  CD2 . LEU B 1 253 ? 97.106  104.987 108.663 1.00 25.77  ? 253 LEU B CD2 1 
ATOM   3520 N  N   . GLY B 1 254 ? 99.092  108.688 111.246 1.00 26.33  ? 254 GLY B N   1 
ATOM   3521 C  CA  . GLY B 1 254 ? 100.095 108.552 112.285 1.00 26.33  ? 254 GLY B CA  1 
ATOM   3522 C  C   . GLY B 1 254 ? 99.623  109.100 113.614 1.00 26.33  ? 254 GLY B C   1 
ATOM   3523 O  O   . GLY B 1 254 ? 99.513  108.368 114.600 1.00 26.33  ? 254 GLY B O   1 
ATOM   3524 N  N   . ASP B 1 255 ? 99.295  110.388 113.654 1.00 35.74  ? 255 ASP B N   1 
ATOM   3525 C  CA  . ASP B 1 255 ? 98.899  110.981 114.922 1.00 35.74  ? 255 ASP B CA  1 
ATOM   3526 C  C   . ASP B 1 255 ? 97.551  110.463 115.408 1.00 35.74  ? 255 ASP B C   1 
ATOM   3527 O  O   . ASP B 1 255 ? 97.286  110.492 116.613 1.00 35.74  ? 255 ASP B O   1 
ATOM   3528 C  CB  . ASP B 1 255 ? 98.891  112.500 114.817 1.00 35.74  ? 255 ASP B CB  1 
ATOM   3529 C  CG  . ASP B 1 255 ? 100.228 113.109 115.161 1.00 35.74  ? 255 ASP B CG  1 
ATOM   3530 O  OD1 . ASP B 1 255 ? 100.952 113.530 114.239 1.00 35.74  ? 255 ASP B OD1 1 
ATOM   3531 O  OD2 . ASP B 1 255 ? 100.555 113.162 116.363 1.00 35.74  ? 255 ASP B OD2 1 
ATOM   3532 N  N   . ALA B 1 256 ? 96.694  109.959 114.515 1.00 30.65  ? 256 ALA B N   1 
ATOM   3533 C  CA  . ALA B 1 256 ? 95.453  109.352 114.989 1.00 30.65  ? 256 ALA B CA  1 
ATOM   3534 C  C   . ALA B 1 256 ? 95.733  108.078 115.779 1.00 30.65  ? 256 ALA B C   1 
ATOM   3535 O  O   . ALA B 1 256 ? 95.155  107.852 116.851 1.00 30.65  ? 256 ALA B O   1 
ATOM   3536 C  CB  . ALA B 1 256 ? 94.522  109.066 113.816 1.00 30.65  ? 256 ALA B CB  1 
ATOM   3537 N  N   . LEU B 1 257 ? 96.619  107.223 115.264 1.00 26.25  ? 257 LEU B N   1 
ATOM   3538 C  CA  . LEU B 1 257 ? 96.991  106.041 116.032 1.00 26.25  ? 257 LEU B CA  1 
ATOM   3539 C  C   . LEU B 1 257 ? 97.723  106.424 117.306 1.00 26.25  ? 257 LEU B C   1 
ATOM   3540 O  O   . LEU B 1 257 ? 97.561  105.764 118.337 1.00 26.25  ? 257 LEU B O   1 
ATOM   3541 C  CB  . LEU B 1 257 ? 97.840  105.101 115.192 1.00 26.25  ? 257 LEU B CB  1 
ATOM   3542 C  CG  . LEU B 1 257 ? 97.036  104.387 114.116 1.00 26.25  ? 257 LEU B CG  1 
ATOM   3543 C  CD1 . LEU B 1 257 ? 97.892  103.384 113.394 1.00 26.25  ? 257 LEU B CD1 1 
ATOM   3544 C  CD2 . LEU B 1 257 ? 95.815  103.730 114.708 1.00 26.25  ? 257 LEU B CD2 1 
ATOM   3545 N  N   . GLY B 1 258 ? 98.516  107.491 117.264 1.00 26.73  ? 258 GLY B N   1 
ATOM   3546 C  CA  . GLY B 1 258 ? 99.106  107.996 118.495 1.00 26.73  ? 258 GLY B CA  1 
ATOM   3547 C  C   . GLY B 1 258 ? 98.055  108.373 119.520 1.00 26.73  ? 258 GLY B C   1 
ATOM   3548 O  O   . GLY B 1 258 ? 98.202  108.100 120.714 1.00 26.73  ? 258 GLY B O   1 
ATOM   3549 N  N   . SER B 1 259 ? 96.965  108.983 119.070 1.00 29.77  ? 259 SER B N   1 
ATOM   3550 C  CA  . SER B 1 259 ? 95.917  109.348 120.009 1.00 29.77  ? 259 SER B CA  1 
ATOM   3551 C  C   . SER B 1 259 ? 95.198  108.126 120.565 1.00 29.77  ? 259 SER B C   1 
ATOM   3552 O  O   . SER B 1 259 ? 94.845  108.109 121.750 1.00 29.77  ? 259 SER B O   1 
ATOM   3553 C  CB  . SER B 1 259 ? 94.931  110.295 119.344 1.00 29.77  ? 259 SER B CB  1 
ATOM   3554 O  OG  . SER B 1 259 ? 95.435  111.620 119.347 1.00 29.77  ? 259 SER B OG  1 
ATOM   3555 N  N   . VAL B 1 260 ? 94.957  107.105 119.740 1.00 24.82  ? 260 VAL B N   1 
ATOM   3556 C  CA  . VAL B 1 260 ? 94.371  105.879 120.281 1.00 24.82  ? 260 VAL B CA  1 
ATOM   3557 C  C   . VAL B 1 260 ? 95.281  105.288 121.343 1.00 24.82  ? 260 VAL B C   1 
ATOM   3558 O  O   . VAL B 1 260 ? 94.816  104.769 122.365 1.00 24.82  ? 260 VAL B O   1 
ATOM   3559 C  CB  . VAL B 1 260 ? 94.078  104.858 119.170 1.00 24.82  ? 260 VAL B CB  1 
ATOM   3560 C  CG1 . VAL B 1 260 ? 93.766  103.509 119.780 1.00 24.82  ? 260 VAL B CG1 1 
ATOM   3561 C  CG2 . VAL B 1 260 ? 92.925  105.322 118.318 1.00 24.82  ? 260 VAL B CG2 1 
ATOM   3562 N  N   . ILE B 1 261 ? 96.592  105.356 121.119 1.00 24.00  ? 261 ILE B N   1 
ATOM   3563 C  CA  . ILE B 1 261 ? 97.542  104.944 122.148 1.00 24.00  ? 261 ILE B CA  1 
ATOM   3564 C  C   . ILE B 1 261 ? 97.302  105.721 123.428 1.00 24.00  ? 261 ILE B C   1 
ATOM   3565 O  O   . ILE B 1 261 ? 97.271  105.146 124.518 1.00 24.00  ? 261 ILE B O   1 
ATOM   3566 C  CB  . ILE B 1 261 ? 98.991  105.128 121.669 1.00 24.00  ? 261 ILE B CB  1 
ATOM   3567 C  CG1 . ILE B 1 261 ? 99.422  103.994 120.754 1.00 24.00  ? 261 ILE B CG1 1 
ATOM   3568 C  CG2 . ILE B 1 261 ? 99.936  105.222 122.849 1.00 24.00  ? 261 ILE B CG2 1 
ATOM   3569 C  CD1 . ILE B 1 261 ? 100.799 104.197 120.221 1.00 24.00  ? 261 ILE B CD1 1 
ATOM   3570 N  N   . VAL B 1 262 ? 97.161  107.044 123.321 1.00 25.84  ? 262 VAL B N   1 
ATOM   3571 C  CA  . VAL B 1 262 ? 97.053  107.859 124.534 1.00 25.84  ? 262 VAL B CA  1 
ATOM   3572 C  C   . VAL B 1 262 ? 95.782  107.517 125.300 1.00 25.84  ? 262 VAL B C   1 
ATOM   3573 O  O   . VAL B 1 262 ? 95.777  107.467 126.534 1.00 25.84  ? 262 VAL B O   1 
ATOM   3574 C  CB  . VAL B 1 262 ? 97.118  109.360 124.217 1.00 25.84  ? 262 VAL B CB  1 
ATOM   3575 C  CG1 . VAL B 1 262 ? 97.185  110.119 125.505 1.00 25.84  ? 262 VAL B CG1 1 
ATOM   3576 C  CG2 . VAL B 1 262 ? 98.336  109.686 123.401 1.00 25.84  ? 262 VAL B CG2 1 
ATOM   3577 N  N   . VAL B 1 263 ? 94.691  107.258 124.587 1.00 26.31  ? 263 VAL B N   1 
ATOM   3578 C  CA  . VAL B 1 263 ? 93.457  106.931 125.294 1.00 26.31  ? 263 VAL B CA  1 
ATOM   3579 C  C   . VAL B 1 263 ? 93.533  105.553 125.936 1.00 26.31  ? 263 VAL B C   1 
ATOM   3580 O  O   . VAL B 1 263 ? 93.218  105.402 127.119 1.00 26.31  ? 263 VAL B O   1 
ATOM   3581 C  CB  . VAL B 1 263 ? 92.246  107.043 124.372 1.00 26.31  ? 263 VAL B CB  1 
ATOM   3582 C  CG1 . VAL B 1 263 ? 91.118  106.196 124.908 1.00 26.31  ? 263 VAL B CG1 1 
ATOM   3583 C  CG2 . VAL B 1 263 ? 91.833  108.471 124.324 1.00 26.31  ? 263 VAL B CG2 1 
ATOM   3584 N  N   . VAL B 1 264 ? 93.937  104.519 125.188 1.00 25.33  ? 264 VAL B N   1 
ATOM   3585 C  CA  . VAL B 1 264 ? 93.957  103.184 125.796 1.00 25.33  ? 264 VAL B CA  1 
ATOM   3586 C  C   . VAL B 1 264 ? 95.003  103.101 126.893 1.00 25.33  ? 264 VAL B C   1 
ATOM   3587 O  O   . VAL B 1 264 ? 94.826  102.358 127.855 1.00 25.33  ? 264 VAL B O   1 
ATOM   3588 C  CB  . VAL B 1 264 ? 94.153  102.088 124.737 1.00 25.33  ? 264 VAL B CB  1 
ATOM   3589 C  CG1 . VAL B 1 264 ? 94.738  100.859 125.345 1.00 25.33  ? 264 VAL B CG1 1 
ATOM   3590 C  CG2 . VAL B 1 264 ? 92.819  101.737 124.105 1.00 25.33  ? 264 VAL B CG2 1 
ATOM   3591 N  N   . ASN B 1 265 ? 96.074  103.887 126.812 1.00 29.56  ? 265 ASN B N   1 
ATOM   3592 C  CA  . ASN B 1 265 ? 96.990  103.983 127.940 1.00 29.56  ? 265 ASN B CA  1 
ATOM   3593 C  C   . ASN B 1 265 ? 96.334  104.655 129.132 1.00 29.56  ? 265 ASN B C   1 
ATOM   3594 O  O   . ASN B 1 265 ? 96.072  104.005 130.148 1.00 29.56  ? 265 ASN B O   1 
ATOM   3595 C  CB  . ASN B 1 265 ? 98.236  104.761 127.565 1.00 29.56  ? 265 ASN B CB  1 
ATOM   3596 C  CG  . ASN B 1 265 ? 99.210  104.856 128.709 1.00 29.56  ? 265 ASN B CG  1 
ATOM   3597 O  OD1 . ASN B 1 265 ? 99.055  104.199 129.727 1.00 29.56  ? 265 ASN B OD1 1 
ATOM   3598 N  ND2 . ASN B 1 265 ? 100.199 105.712 128.563 1.00 29.56  ? 265 ASN B ND2 1 
ATOM   3599 N  N   . ALA B 1 266 ? 96.067  105.960 129.044 1.00 24.19  ? 266 ALA B N   1 
ATOM   3600 C  CA  . ALA B 1 266 ? 95.604  106.680 130.227 1.00 24.19  ? 266 ALA B CA  1 
ATOM   3601 C  C   . ALA B 1 266 ? 94.234  106.206 130.680 1.00 24.19  ? 266 ALA B C   1 
ATOM   3602 O  O   . ALA B 1 266 ? 93.725  106.673 131.699 1.00 24.19  ? 266 ALA B O   1 
ATOM   3603 C  CB  . ALA B 1 266 ? 95.587  108.173 129.957 1.00 24.19  ? 266 ALA B CB  1 
ATOM   3604 N  N   . LEU B 1 267 ? 93.617  105.304 129.931 1.00 30.00  ? 267 LEU B N   1 
ATOM   3605 C  CA  . LEU B 1 267 ? 92.413  104.627 130.378 1.00 30.00  ? 267 LEU B CA  1 
ATOM   3606 C  C   . LEU B 1 267 ? 92.744  103.595 131.447 1.00 30.00  ? 267 LEU B C   1 
ATOM   3607 O  O   . LEU B 1 267 ? 92.380  103.787 132.610 1.00 30.00  ? 267 LEU B O   1 
ATOM   3608 C  CB  . LEU B 1 267 ? 91.714  103.989 129.182 1.00 30.00  ? 267 LEU B CB  1 
ATOM   3609 C  CG  . LEU B 1 267 ? 90.452  103.187 129.417 1.00 30.00  ? 267 LEU B CG  1 
ATOM   3610 C  CD1 . LEU B 1 267 ? 89.428  103.566 128.390 1.00 30.00  ? 267 LEU B CD1 1 
ATOM   3611 C  CD2 . LEU B 1 267 ? 90.788  101.721 129.278 1.00 30.00  ? 267 LEU B CD2 1 
ATOM   3612 N  N   . VAL B 1 268 ? 93.465  102.528 131.099 1.00 27.75  ? 268 VAL B N   1 
ATOM   3613 C  CA  . VAL B 1 268 ? 93.927  101.554 132.110 1.00 27.75  ? 268 VAL B CA  1 
ATOM   3614 C  C   . VAL B 1 268 ? 95.284  102.059 132.571 1.00 27.75  ? 268 VAL B C   1 
ATOM   3615 O  O   . VAL B 1 268 ? 96.341  101.515 132.257 1.00 27.75  ? 268 VAL B O   1 
ATOM   3616 C  CB  . VAL B 1 268 ? 93.986  100.129 131.555 1.00 27.75  ? 268 VAL B CB  1 
ATOM   3617 N  N   . PHE B 1 269 ? 95.250  103.145 133.291 1.00 33.53  ? 269 PHE B N   1 
ATOM   3618 C  CA  . PHE B 1 269 ? 96.307  103.698 134.118 1.00 33.53  ? 269 PHE B CA  1 
ATOM   3619 C  C   . PHE B 1 269 ? 95.773  104.329 135.389 1.00 33.53  ? 269 PHE B C   1 
ATOM   3620 O  O   . PHE B 1 269 ? 96.499  104.424 136.374 1.00 33.53  ? 269 PHE B O   1 
ATOM   3621 C  CB  . PHE B 1 269 ? 97.092  104.702 133.340 1.00 33.53  ? 269 PHE B CB  1 
ATOM   3622 C  CG  . PHE B 1 269 ? 98.476  104.897 133.834 1.00 33.53  ? 269 PHE B CG  1 
ATOM   3623 C  CD1 . PHE B 1 269 ? 99.534  104.329 133.171 1.00 33.53  ? 269 PHE B CD1 1 
ATOM   3624 C  CD2 . PHE B 1 269 ? 98.722  105.668 134.941 1.00 33.53  ? 269 PHE B CD2 1 
ATOM   3625 C  CE1 . PHE B 1 269 ? 100.805 104.525 133.603 1.00 33.53  ? 269 PHE B CE1 1 
ATOM   3626 C  CE2 . PHE B 1 269 ? 99.992  105.859 135.383 1.00 33.53  ? 269 PHE B CE2 1 
ATOM   3627 C  CZ  . PHE B 1 269 ? 101.037 105.291 134.715 1.00 33.53  ? 269 PHE B CZ  1 
ATOM   3628 N  N   . TYR B 1 270 ? 94.550  104.843 135.364 1.00 37.62  ? 270 TYR B N   1 
ATOM   3629 C  CA  . TYR B 1 270 ? 93.837  105.136 136.595 1.00 37.62  ? 270 TYR B CA  1 
ATOM   3630 C  C   . TYR B 1 270 ? 93.115  103.914 137.124 1.00 37.62  ? 270 TYR B C   1 
ATOM   3631 O  O   . TYR B 1 270 ? 92.846  103.829 138.326 1.00 37.62  ? 270 TYR B O   1 
ATOM   3632 C  CB  . TYR B 1 270 ? 92.831  106.264 136.376 1.00 37.62  ? 270 TYR B CB  1 
ATOM   3633 N  N   . PHE B 1 271 ? 92.816  102.961 136.246 1.00 36.09  ? 271 PHE B N   1 
ATOM   3634 C  CA  . PHE B 1 271 ? 92.097  101.762 136.647 1.00 36.09  ? 271 PHE B CA  1 
ATOM   3635 C  C   . PHE B 1 271 ? 93.005  100.800 137.399 1.00 36.09  ? 271 PHE B C   1 
ATOM   3636 O  O   . PHE B 1 271 ? 92.537  99.990  138.201 1.00 36.09  ? 271 PHE B O   1 
ATOM   3637 C  CB  . PHE B 1 271 ? 91.511  101.091 135.407 1.00 36.09  ? 271 PHE B CB  1 
ATOM   3638 C  CG  . PHE B 1 271 ? 90.260  101.736 134.905 1.00 36.09  ? 271 PHE B CG  1 
ATOM   3639 C  CD1 . PHE B 1 271 ? 89.295  100.986 134.273 1.00 36.09  ? 271 PHE B CD1 1 
ATOM   3640 C  CD2 . PHE B 1 271 ? 90.047  103.090 135.074 1.00 36.09  ? 271 PHE B CD2 1 
ATOM   3641 C  CE1 . PHE B 1 271 ? 88.147  101.574 133.810 1.00 36.09  ? 271 PHE B CE1 1 
ATOM   3642 C  CE2 . PHE B 1 271 ? 88.903  103.678 134.619 1.00 36.09  ? 271 PHE B CE2 1 
ATOM   3643 C  CZ  . PHE B 1 271 ? 87.949  102.920 133.986 1.00 36.09  ? 271 PHE B CZ  1 
ATOM   3644 N  N   . SER B 1 272 ? 94.311  100.865 137.145 1.00 36.82  ? 272 SER B N   1 
ATOM   3645 C  CA  . SER B 1 272 ? 95.206  99.852  137.683 1.00 36.82  ? 272 SER B CA  1 
ATOM   3646 C  C   . SER B 1 272 ? 96.230  100.403 138.664 1.00 36.82  ? 272 SER B C   1 
ATOM   3647 O  O   . SER B 1 272 ? 96.321  99.915  139.793 1.00 36.82  ? 272 SER B O   1 
ATOM   3648 C  CB  . SER B 1 272 ? 95.924  99.136  136.548 1.00 36.82  ? 272 SER B CB  1 
ATOM   3649 N  N   . TRP B 1 273 ? 97.000  101.412 138.264 1.00 39.06  ? 273 TRP B N   1 
ATOM   3650 C  CA  . TRP B 1 273 ? 98.144  101.837 139.063 1.00 39.06  ? 273 TRP B CA  1 
ATOM   3651 C  C   . TRP B 1 273 ? 97.704  102.357 140.422 1.00 39.06  ? 273 TRP B C   1 
ATOM   3652 O  O   . TRP B 1 273 ? 96.554  102.751 140.617 1.00 39.06  ? 273 TRP B O   1 
ATOM   3653 C  CB  . TRP B 1 273 ? 98.943  102.912 138.324 1.00 39.06  ? 273 TRP B CB  1 
ATOM   3654 N  N   . LYS B 1 274 ? 98.628  102.325 141.374 1.00 50.03  ? 274 LYS B N   1 
ATOM   3655 C  CA  . LYS B 1 274 ? 98.376  102.764 142.739 1.00 50.03  ? 274 LYS B CA  1 
ATOM   3656 C  C   . LYS B 1 274 ? 99.291  103.899 143.164 1.00 50.03  ? 274 LYS B C   1 
ATOM   3657 O  O   . LYS B 1 274 ? 98.810  104.931 143.640 1.00 50.03  ? 274 LYS B O   1 
ATOM   3658 C  CB  . LYS B 1 274 ? 98.526  101.583 143.705 1.00 50.03  ? 274 LYS B CB  1 
ATOM   3659 N  N   . GLY B 1 275 ? 100.599 103.736 143.022 1.00 63.89  ? 275 GLY B N   1 
ATOM   3660 C  CA  . GLY B 1 275 ? 101.522 104.810 143.317 1.00 63.89  ? 275 GLY B CA  1 
ATOM   3661 C  C   . GLY B 1 275 ? 101.588 105.148 144.789 1.00 63.89  ? 275 GLY B C   1 
ATOM   3662 O  O   . GLY B 1 275 ? 101.021 104.429 145.615 1.00 63.89  ? 275 GLY B O   1 
ATOM   3663 N  N   . CYS B 1 276 ? 102.244 106.259 145.124 1.00 71.42  ? 276 CYS B N   1 
ATOM   3664 C  CA  . CYS B 1 276 ? 102.510 106.613 146.516 1.00 71.42  ? 276 CYS B CA  1 
ATOM   3665 C  C   . CYS B 1 276 ? 101.284 107.258 147.150 1.00 71.42  ? 276 CYS B C   1 
ATOM   3666 O  O   . CYS B 1 276 ? 100.715 108.207 146.600 1.00 71.42  ? 276 CYS B O   1 
ATOM   3667 C  CB  . CYS B 1 276 ? 103.708 107.550 146.592 1.00 71.42  ? 276 CYS B CB  1 
ATOM   3668 S  SG  . CYS B 1 276 ? 105.227 106.830 145.955 1.00 71.42  ? 276 CYS B SG  1 
ATOM   3669 N  N   . SER B 1 277 ? 100.892 106.760 148.322 1.00 76.12  ? 277 SER B N   1 
ATOM   3670 C  CA  . SER B 1 277 ? 99.598  107.099 148.907 1.00 76.12  ? 277 SER B CA  1 
ATOM   3671 C  C   . SER B 1 277 ? 99.701  108.111 150.048 1.00 76.12  ? 277 SER B C   1 
ATOM   3672 O  O   . SER B 1 277 ? 99.059  109.166 150.010 1.00 76.12  ? 277 SER B O   1 
ATOM   3673 C  CB  . SER B 1 277 ? 98.904  105.819 149.388 1.00 76.12  ? 277 SER B CB  1 
ATOM   3674 N  N   . GLU B 1 278 ? 100.496 107.799 151.075 1.00 78.44  ? 278 GLU B N   1 
ATOM   3675 C  CA  . GLU B 1 278 ? 100.507 108.576 152.318 1.00 78.44  ? 278 GLU B CA  1 
ATOM   3676 C  C   . GLU B 1 278 ? 101.370 109.822 152.135 1.00 78.44  ? 278 GLU B C   1 
ATOM   3677 O  O   . GLU B 1 278 ? 102.541 109.879 152.518 1.00 78.44  ? 278 GLU B O   1 
ATOM   3678 C  CB  . GLU B 1 278 ? 100.999 107.720 153.479 1.00 78.44  ? 278 GLU B CB  1 
ATOM   3679 N  N   . GLY B 1 279 ? 100.760 110.852 151.552 1.00 78.00  ? 279 GLY B N   1 
ATOM   3680 C  CA  . GLY B 1 279 ? 101.445 112.109 151.325 1.00 78.00  ? 279 GLY B CA  1 
ATOM   3681 C  C   . GLY B 1 279 ? 102.571 111.991 150.321 1.00 78.00  ? 279 GLY B C   1 
ATOM   3682 O  O   . GLY B 1 279 ? 102.332 111.677 149.151 1.00 78.00  ? 279 GLY B O   1 
ATOM   3683 N  N   . ASP B 1 280 ? 103.806 112.239 150.762 1.00 75.43  ? 280 ASP B N   1 
ATOM   3684 C  CA  . ASP B 1 280 ? 104.973 112.197 149.886 1.00 75.43  ? 280 ASP B CA  1 
ATOM   3685 C  C   . ASP B 1 280 ? 106.063 111.259 150.391 1.00 75.43  ? 280 ASP B C   1 
ATOM   3686 O  O   . ASP B 1 280 ? 107.221 111.413 149.988 1.00 75.43  ? 280 ASP B O   1 
ATOM   3687 C  CB  . ASP B 1 280 ? 105.571 113.600 149.708 1.00 75.43  ? 280 ASP B CB  1 
ATOM   3688 C  CG  . ASP B 1 280 ? 104.681 114.531 148.903 1.00 75.43  ? 280 ASP B CG  1 
ATOM   3689 O  OD1 . ASP B 1 280 ? 103.447 114.369 148.936 1.00 75.43  ? 280 ASP B OD1 1 
ATOM   3690 O  OD2 . ASP B 1 280 ? 105.222 115.434 148.233 1.00 75.43  ? 280 ASP B OD2 1 
ATOM   3691 N  N   . PHE B 1 281 ? 105.740 110.301 151.259 1.00 78.25  ? 281 PHE B N   1 
ATOM   3692 C  CA  . PHE B 1 281 ? 106.745 109.451 151.902 1.00 78.25  ? 281 PHE B CA  1 
ATOM   3693 C  C   . PHE B 1 281 ? 106.311 107.990 151.828 1.00 78.25  ? 281 PHE B C   1 
ATOM   3694 O  O   . PHE B 1 281 ? 105.674 107.471 152.747 1.00 78.25  ? 281 PHE B O   1 
ATOM   3695 C  CB  . PHE B 1 281 ? 106.972 109.884 153.350 1.00 78.25  ? 281 PHE B CB  1 
ATOM   3696 N  N   . CYS B 1 282 ? 106.685 107.322 150.743 1.00 82.85  ? 282 CYS B N   1 
ATOM   3697 C  CA  . CYS B 1 282 ? 106.368 105.913 150.558 1.00 82.85  ? 282 CYS B CA  1 
ATOM   3698 C  C   . CYS B 1 282 ? 107.472 105.285 149.717 1.00 82.85  ? 282 CYS B C   1 
ATOM   3699 O  O   . CYS B 1 282 ? 108.310 105.981 149.139 1.00 82.85  ? 282 CYS B O   1 
ATOM   3700 C  CB  . CYS B 1 282 ? 104.986 105.736 149.914 1.00 82.85  ? 282 CYS B CB  1 
ATOM   3701 N  N   . VAL B 1 283 ? 107.462 103.971 149.637 1.00 90.28  ? 283 VAL B N   1 
ATOM   3702 C  CA  . VAL B 1 283 ? 108.477 103.241 148.893 1.00 90.28  ? 283 VAL B CA  1 
ATOM   3703 C  C   . VAL B 1 283 ? 107.874 102.763 147.579 1.00 90.28  ? 283 VAL B C   1 
ATOM   3704 O  O   . VAL B 1 283 ? 106.808 102.138 147.542 1.00 90.28  ? 283 VAL B O   1 
ATOM   3705 C  CB  . VAL B 1 283 ? 109.032 102.070 149.728 1.00 90.28  ? 283 VAL B CB  1 
ATOM   3706 N  N   . ASN B 1 284 ? 108.571 103.068 146.480 1.00 91.17  ? 284 ASN B N   1 
ATOM   3707 C  CA  . ASN B 1 284 ? 108.162 102.704 145.126 1.00 91.17  ? 284 ASN B CA  1 
ATOM   3708 C  C   . ASN B 1 284 ? 109.162 101.674 144.626 1.00 91.17  ? 284 ASN B C   1 
ATOM   3709 O  O   . ASN B 1 284 ? 110.230 102.029 144.107 1.00 91.17  ? 284 ASN B O   1 
ATOM   3710 C  CB  . ASN B 1 284 ? 108.111 103.915 144.197 1.00 91.17  ? 284 ASN B CB  1 
ATOM   3711 N  N   . PRO B 1 285 ? 108.864 100.386 144.795 1.00 92.07  ? 285 PRO B N   1 
ATOM   3712 C  CA  . PRO B 1 285 ? 109.840 99.365  144.389 1.00 92.07  ? 285 PRO B CA  1 
ATOM   3713 C  C   . PRO B 1 285 ? 109.918 99.179  142.888 1.00 92.07  ? 285 PRO B C   1 
ATOM   3714 O  O   . PRO B 1 285 ? 110.966 98.771  142.374 1.00 92.07  ? 285 PRO B O   1 
ATOM   3715 C  CB  . PRO B 1 285 ? 109.331 98.099  145.097 1.00 92.07  ? 285 PRO B CB  1 
ATOM   3716 C  CG  . PRO B 1 285 ? 108.336 98.588  146.125 1.00 92.07  ? 285 PRO B CG  1 
ATOM   3717 C  CD  . PRO B 1 285 ? 107.727 99.803  145.518 1.00 92.07  ? 285 PRO B CD  1 
ATOM   3718 N  N   . CYS B 1 286 ? 108.840 99.484  142.163 1.00 88.40  ? 286 CYS B N   1 
ATOM   3719 C  CA  . CYS B 1 286 ? 108.763 99.114  140.759 1.00 88.40  ? 286 CYS B CA  1 
ATOM   3720 C  C   . CYS B 1 286 ? 109.776 99.843  139.889 1.00 88.40  ? 286 CYS B C   1 
ATOM   3721 O  O   . CYS B 1 286 ? 110.066 99.373  138.787 1.00 88.40  ? 286 CYS B O   1 
ATOM   3722 C  CB  . CYS B 1 286 ? 107.360 99.365  140.226 1.00 88.40  ? 286 CYS B CB  1 
ATOM   3723 S  SG  . CYS B 1 286 ? 107.061 98.660  138.590 1.00 88.40  ? 286 CYS B SG  1 
ATOM   3724 N  N   . PHE B 1 287 ? 110.316 100.972 140.334 1.00 84.33  ? 287 PHE B N   1 
ATOM   3725 C  CA  . PHE B 1 287 ? 111.345 101.601 139.521 1.00 84.33  ? 287 PHE B CA  1 
ATOM   3726 C  C   . PHE B 1 287 ? 112.238 102.445 140.418 1.00 84.33  ? 287 PHE B C   1 
ATOM   3727 O  O   . PHE B 1 287 ? 111.887 102.664 141.587 1.00 84.33  ? 287 PHE B O   1 
ATOM   3728 C  CB  . PHE B 1 287 ? 110.770 102.450 138.380 1.00 84.33  ? 287 PHE B CB  1 
ATOM   3729 C  CG  . PHE B 1 287 ? 109.895 103.590 138.825 1.00 84.33  ? 287 PHE B CG  1 
ATOM   3730 C  CD1 . PHE B 1 287 ? 108.664 103.356 139.406 1.00 84.33  ? 287 PHE B CD1 1 
ATOM   3731 C  CD2 . PHE B 1 287 ? 110.284 104.897 138.614 1.00 84.33  ? 287 PHE B CD2 1 
ATOM   3732 C  CE1 . PHE B 1 287 ? 107.862 104.396 139.803 1.00 84.33  ? 287 PHE B CE1 1 
ATOM   3733 C  CE2 . PHE B 1 287 ? 109.482 105.938 139.003 1.00 84.33  ? 287 PHE B CE2 1 
ATOM   3734 C  CZ  . PHE B 1 287 ? 108.270 105.686 139.601 1.00 84.33  ? 287 PHE B CZ  1 
ATOM   3735 N  N   . PRO B 1 288 ? 113.386 102.903 139.928 1.00 90.20  ? 288 PRO B N   1 
ATOM   3736 C  CA  . PRO B 1 288 ? 114.337 103.593 140.827 1.00 90.20  ? 288 PRO B CA  1 
ATOM   3737 C  C   . PRO B 1 288 ? 113.842 104.965 141.273 1.00 90.20  ? 288 PRO B C   1 
ATOM   3738 O  O   . PRO B 1 288 ? 114.258 106.012 140.791 1.00 90.20  ? 288 PRO B O   1 
ATOM   3739 C  CB  . PRO B 1 288 ? 115.598 103.692 139.966 1.00 90.20  ? 288 PRO B CB  1 
ATOM   3740 N  N   . ASP B 1 289 ? 112.930 104.951 142.236 1.00 92.75  ? 289 ASP B N   1 
ATOM   3741 C  CA  . ASP B 1 289 ? 112.274 106.172 142.687 1.00 92.75  ? 289 ASP B CA  1 
ATOM   3742 C  C   . ASP B 1 289 ? 113.300 107.141 143.253 1.00 92.75  ? 289 ASP B C   1 
ATOM   3743 O  O   . ASP B 1 289 ? 113.950 106.821 144.255 1.00 92.75  ? 289 ASP B O   1 
ATOM   3744 C  CB  . ASP B 1 289 ? 111.219 105.842 143.735 1.00 92.75  ? 289 ASP B CB  1 
ATOM   3745 N  N   . PRO B 1 290 ? 113.504 108.304 142.601 1.00 96.45  ? 290 PRO B N   1 
ATOM   3746 C  CA  . PRO B 1 290 ? 114.525 109.336 142.902 1.00 96.45  ? 290 PRO B CA  1 
ATOM   3747 C  C   . PRO B 1 290 ? 114.517 110.076 144.252 1.00 96.45  ? 290 PRO B C   1 
ATOM   3748 O  O   . PRO B 1 290 ? 115.584 110.223 144.823 1.00 96.45  ? 290 PRO B O   1 
ATOM   3749 C  CB  . PRO B 1 290 ? 114.294 110.360 141.782 1.00 96.45  ? 290 PRO B CB  1 
ATOM   3750 N  N   . CYS B 1 291 ? 113.365 110.522 144.734 1.00 95.47  ? 291 CYS B N   1 
ATOM   3751 C  CA  . CYS B 1 291 ? 113.245 111.225 146.004 1.00 95.47  ? 291 CYS B CA  1 
ATOM   3752 C  C   . CYS B 1 291 ? 112.791 110.291 147.114 1.00 95.47  ? 291 CYS B C   1 
ATOM   3753 O  O   . CYS B 1 291 ? 113.301 110.358 148.239 1.00 95.47  ? 291 CYS B O   1 
ATOM   3754 C  CB  . CYS B 1 291 ? 112.276 112.395 145.880 1.00 95.47  ? 291 CYS B CB  1 
ATOM   3755 S  SG  . CYS B 1 291 ? 112.545 113.541 147.207 1.00 95.47  ? 291 CYS B SG  1 
ATOM   3756 N  N   . LYS B 1 292 ? 111.810 109.435 146.822 1.00 93.87  ? 292 LYS B N   1 
ATOM   3757 C  CA  . LYS B 1 292 ? 111.315 108.511 147.832 1.00 93.87  ? 292 LYS B CA  1 
ATOM   3758 C  C   . LYS B 1 292 ? 112.447 107.667 148.400 1.00 93.87  ? 292 LYS B C   1 
ATOM   3759 O  O   . LYS B 1 292 ? 112.663 107.641 149.617 1.00 93.87  ? 292 LYS B O   1 
ATOM   3760 C  CB  . LYS B 1 292 ? 110.218 107.628 147.233 1.00 93.87  ? 292 LYS B CB  1 
ATOM   3761 N  N   . ALA B 1 293 ? 113.206 107.001 147.528 1.00 90.80  ? 293 ALA B N   1 
ATOM   3762 C  CA  . ALA B 1 293 ? 114.296 106.159 148.002 1.00 90.80  ? 293 ALA B CA  1 
ATOM   3763 C  C   . ALA B 1 293 ? 115.389 106.986 148.663 1.00 90.80  ? 293 ALA B C   1 
ATOM   3764 O  O   . ALA B 1 293 ? 115.933 106.583 149.697 1.00 90.80  ? 293 ALA B O   1 
ATOM   3765 C  CB  . ALA B 1 293 ? 114.870 105.334 146.852 1.00 90.80  ? 293 ALA B CB  1 
ATOM   3766 N  N   . PHE B 1 294 ? 115.721 108.152 148.093 1.00 87.54  ? 294 PHE B N   1 
ATOM   3767 C  CA  . PHE B 1 294 ? 116.788 108.966 148.671 1.00 87.54  ? 294 PHE B CA  1 
ATOM   3768 C  C   . PHE B 1 294 ? 116.469 109.366 150.110 1.00 87.54  ? 294 PHE B C   1 
ATOM   3769 O  O   . PHE B 1 294 ? 117.266 109.120 151.027 1.00 87.54  ? 294 PHE B O   1 
ATOM   3770 C  CB  . PHE B 1 294 ? 117.025 110.202 147.806 1.00 87.54  ? 294 PHE B CB  1 
ATOM   3771 N  N   . VAL B 1 295 ? 115.290 109.953 150.330 1.00 85.04  ? 295 VAL B N   1 
ATOM   3772 C  CA  . VAL B 1 295 ? 114.929 110.440 151.660 1.00 85.04  ? 295 VAL B CA  1 
ATOM   3773 C  C   . VAL B 1 295 ? 114.621 109.283 152.602 1.00 85.04  ? 295 VAL B C   1 
ATOM   3774 O  O   . VAL B 1 295 ? 114.813 109.392 153.819 1.00 85.04  ? 295 VAL B O   1 
ATOM   3775 C  CB  . VAL B 1 295 ? 113.745 111.418 151.569 1.00 85.04  ? 295 VAL B CB  1 
ATOM   3776 N  N   . GLU B 1 296 ? 114.134 108.157 152.068 1.00 81.13  ? 296 GLU B N   1 
ATOM   3777 C  CA  . GLU B 1 296 ? 113.783 107.035 152.928 1.00 81.13  ? 296 GLU B CA  1 
ATOM   3778 C  C   . GLU B 1 296 ? 115.006 106.245 153.370 1.00 81.13  ? 296 GLU B C   1 
ATOM   3779 O  O   . GLU B 1 296 ? 114.987 105.635 154.444 1.00 81.13  ? 296 GLU B O   1 
ATOM   3780 C  CB  . GLU B 1 296 ? 112.797 106.117 152.205 1.00 81.13  ? 296 GLU B CB  1 
ATOM   3781 N  N   . ILE B 1 297 ? 116.067 106.237 152.564 1.00 81.39  ? 297 ILE B N   1 
ATOM   3782 C  CA  . ILE B 1 297 ? 117.297 105.571 152.964 1.00 81.39  ? 297 ILE B CA  1 
ATOM   3783 C  C   . ILE B 1 297 ? 118.220 106.498 153.747 1.00 81.39  ? 297 ILE B C   1 
ATOM   3784 O  O   . ILE B 1 297 ? 119.038 106.011 154.539 1.00 81.39  ? 297 ILE B O   1 
ATOM   3785 C  CB  . ILE B 1 297 ? 118.036 105.000 151.741 1.00 81.39  ? 297 ILE B CB  1 
ATOM   3786 N  N   . ILE B 1 298 ? 118.112 107.813 153.555 1.00 76.72  ? 298 ILE B N   1 
ATOM   3787 C  CA  . ILE B 1 298 ? 118.884 108.759 154.349 1.00 76.72  ? 298 ILE B CA  1 
ATOM   3788 C  C   . ILE B 1 298 ? 118.236 109.060 155.696 1.00 76.72  ? 298 ILE B C   1 
ATOM   3789 O  O   . ILE B 1 298 ? 118.850 109.760 156.516 1.00 76.72  ? 298 ILE B O   1 
ATOM   3790 C  CB  . ILE B 1 298 ? 119.137 110.070 153.576 1.00 76.72  ? 298 ILE B CB  1 
ATOM   3791 N  N   . ASN B 1 299 ? 117.027 108.562 155.954 1.00 71.62  ? 299 ASN B N   1 
ATOM   3792 C  CA  . ASN B 1 299 ? 116.314 108.797 157.209 1.00 71.62  ? 299 ASN B CA  1 
ATOM   3793 C  C   . ASN B 1 299 ? 115.484 107.546 157.482 1.00 71.62  ? 299 ASN B C   1 
ATOM   3794 O  O   . ASN B 1 299 ? 114.530 107.262 156.755 1.00 71.62  ? 299 ASN B O   1 
ATOM   3795 C  CB  . ASN B 1 299 ? 115.444 110.045 157.118 1.00 71.62  ? 299 ASN B CB  1 
ATOM   3796 C  CG  . ASN B 1 299 ? 114.603 110.287 158.367 1.00 71.62  ? 299 ASN B CG  1 
ATOM   3797 O  OD1 . ASN B 1 299 ? 114.387 109.396 159.186 1.00 71.62  ? 299 ASN B OD1 1 
ATOM   3798 N  ND2 . ASN B 1 299 ? 114.117 111.514 158.506 1.00 71.62  ? 299 ASN B ND2 1 
ATOM   3799 N  N   . SER B 1 300 ? 115.844 106.810 158.530 1.00 70.22  ? 300 SER B N   1 
ATOM   3800 C  CA  . SER B 1 300 ? 115.127 105.606 158.933 1.00 70.22  ? 300 SER B CA  1 
ATOM   3801 C  C   . SER B 1 300 ? 114.298 105.937 160.168 1.00 70.22  ? 300 SER B C   1 
ATOM   3802 O  O   . SER B 1 300 ? 114.827 105.985 161.282 1.00 70.22  ? 300 SER B O   1 
ATOM   3803 C  CB  . SER B 1 300 ? 116.096 104.461 159.214 1.00 70.22  ? 300 SER B CB  1 
ATOM   3804 N  N   . THR B 1 301 ? 113.000 106.160 159.969 1.00 75.79  ? 301 THR B N   1 
ATOM   3805 C  CA  . THR B 1 301 ? 112.124 106.642 161.028 1.00 75.79  ? 301 THR B CA  1 
ATOM   3806 C  C   . THR B 1 301 ? 110.918 105.742 161.276 1.00 75.79  ? 301 THR B C   1 
ATOM   3807 O  O   . THR B 1 301 ? 110.085 106.078 162.123 1.00 75.79  ? 301 THR B O   1 
ATOM   3808 C  CB  . THR B 1 301 ? 111.652 108.064 160.712 1.00 75.79  ? 301 THR B CB  1 
ATOM   3809 N  N   . HIS B 1 302 ? 110.799 104.617 160.563 1.00 82.76  ? 302 HIS B N   1 
ATOM   3810 C  CA  . HIS B 1 302 ? 109.674 103.691 160.734 1.00 82.76  ? 302 HIS B CA  1 
ATOM   3811 C  C   . HIS B 1 302 ? 108.338 104.403 160.510 1.00 82.76  ? 302 HIS B C   1 
ATOM   3812 O  O   . HIS B 1 302 ? 107.492 104.485 161.402 1.00 82.76  ? 302 HIS B O   1 
ATOM   3813 C  CB  . HIS B 1 302 ? 109.712 103.027 162.115 1.00 82.76  ? 302 HIS B CB  1 
ATOM   3814 N  N   . ALA B 1 303 ? 108.150 104.913 159.295 1.00 90.68  ? 303 ALA B N   1 
ATOM   3815 C  CA  . ALA B 1 303 ? 107.070 105.844 159.000 1.00 90.68  ? 303 ALA B CA  1 
ATOM   3816 C  C   . ALA B 1 303 ? 105.747 105.101 158.811 1.00 90.68  ? 303 ALA B C   1 
ATOM   3817 O  O   . ALA B 1 303 ? 105.596 103.939 159.196 1.00 90.68  ? 303 ALA B O   1 
ATOM   3818 C  CB  . ALA B 1 303 ? 107.425 106.691 157.779 1.00 90.68  ? 303 ALA B CB  1 
ATOM   3819 N  N   . SER B 1 304 ? 104.771 105.783 158.214 1.00 96.38  ? 304 SER B N   1 
ATOM   3820 C  CA  . SER B 1 304 ? 103.406 105.289 158.105 1.00 96.38  ? 304 SER B CA  1 
ATOM   3821 C  C   . SER B 1 304 ? 103.281 104.253 156.984 1.00 96.38  ? 304 SER B C   1 
ATOM   3822 O  O   . SER B 1 304 ? 104.269 103.766 156.426 1.00 96.38  ? 304 SER B O   1 
ATOM   3823 C  CB  . SER B 1 304 ? 102.444 106.454 157.888 1.00 96.38  ? 304 SER B CB  1 
ATOM   3824 N  N   . VAL B 1 305 ? 102.033 103.912 156.652 1.00 98.63  ? 305 VAL B N   1 
ATOM   3825 C  CA  . VAL B 1 305 ? 101.755 102.794 155.759 1.00 98.63  ? 305 VAL B CA  1 
ATOM   3826 C  C   . VAL B 1 305 ? 102.166 103.128 154.329 1.00 98.63  ? 305 VAL B C   1 
ATOM   3827 O  O   . VAL B 1 305 ? 102.278 104.301 153.945 1.00 98.63  ? 305 VAL B O   1 
ATOM   3828 C  CB  . VAL B 1 305 ? 100.269 102.411 155.836 1.00 98.63  ? 305 VAL B CB  1 
ATOM   3829 N  N   . TYR B 1 306 ? 102.415 102.083 153.540 1.00 94.23  ? 306 TYR B N   1 
ATOM   3830 C  CA  . TYR B 1 306 ? 102.817 102.179 152.145 1.00 94.23  ? 306 TYR B CA  1 
ATOM   3831 C  C   . TYR B 1 306 ? 101.949 101.246 151.296 1.00 94.23  ? 306 TYR B C   1 
ATOM   3832 O  O   . TYR B 1 306 ? 100.958 100.685 151.770 1.00 94.23  ? 306 TYR B O   1 
ATOM   3833 C  CB  . TYR B 1 306 ? 104.296 101.841 152.015 1.00 94.23  ? 306 TYR B CB  1 
ATOM   3834 C  CG  . TYR B 1 306 ? 104.693 100.642 152.843 1.00 94.23  ? 306 TYR B CG  1 
ATOM   3835 C  CD1 . TYR B 1 306 ? 104.627 99.361  152.315 1.00 94.23  ? 306 TYR B CD1 1 
ATOM   3836 C  CD2 . TYR B 1 306 ? 105.122 100.788 154.155 1.00 94.23  ? 306 TYR B CD2 1 
ATOM   3837 C  CE1 . TYR B 1 306 ? 104.976 98.264  153.064 1.00 94.23  ? 306 TYR B CE1 1 
ATOM   3838 C  CE2 . TYR B 1 306 ? 105.471 99.694  154.912 1.00 94.23  ? 306 TYR B CE2 1 
ATOM   3839 C  CZ  . TYR B 1 306 ? 105.397 98.435  154.361 1.00 94.23  ? 306 TYR B CZ  1 
ATOM   3840 O  OH  . TYR B 1 306 ? 105.747 97.339  155.112 1.00 94.23  ? 306 TYR B OH  1 
ATOM   3841 N  N   . GLU B 1 307 ? 102.326 101.062 150.028 1.00 85.78  ? 307 GLU B N   1 
ATOM   3842 C  CA  . GLU B 1 307 ? 101.683 100.094 149.144 1.00 85.78  ? 307 GLU B CA  1 
ATOM   3843 C  C   . GLU B 1 307 ? 102.515 99.917  147.879 1.00 85.78  ? 307 GLU B C   1 
ATOM   3844 O  O   . GLU B 1 307 ? 103.557 100.553 147.703 1.00 85.78  ? 307 GLU B O   1 
ATOM   3845 C  CB  . GLU B 1 307 ? 100.242 100.511 148.805 1.00 85.78  ? 307 GLU B CB  1 
ATOM   3846 C  CG  . GLU B 1 307 ? 100.107 101.872 148.156 1.00 85.78  ? 307 GLU B CG  1 
ATOM   3847 C  CD  . GLU B 1 307 ? 98.753  102.074 147.512 1.00 85.78  ? 307 GLU B CD  1 
ATOM   3848 O  OE1 . GLU B 1 307 ? 98.316  103.237 147.409 1.00 85.78  ? 307 GLU B OE1 1 
ATOM   3849 O  OE2 . GLU B 1 307 ? 98.126  101.073 147.110 1.00 85.78  ? 307 GLU B OE2 1 
ATOM   3850 N  N   . ALA B 1 308 ? 102.053 99.023  147.001 1.00 83.08  ? 308 ALA B N   1 
ATOM   3851 C  CA  . ALA B 1 308 ? 102.763 98.736  145.756 1.00 83.08  ? 308 ALA B CA  1 
ATOM   3852 C  C   . ALA B 1 308 ? 101.773 98.325  144.669 1.00 83.08  ? 308 ALA B C   1 
ATOM   3853 O  O   . ALA B 1 308 ? 101.011 97.369  144.856 1.00 83.08  ? 308 ALA B O   1 
ATOM   3854 C  CB  . ALA B 1 308 ? 103.807 97.637  145.976 1.00 83.08  ? 308 ALA B CB  1 
ATOM   3855 N  N   . GLY B 1 309 ? 101.801 99.026  143.531 1.00 62.36  ? 309 GLY B N   1 
ATOM   3856 C  CA  . GLY B 1 309 ? 100.856 98.797  142.459 1.00 62.36  ? 309 GLY B CA  1 
ATOM   3857 C  C   . GLY B 1 309 ? 101.447 97.994  141.321 1.00 62.36  ? 309 GLY B C   1 
ATOM   3858 O  O   . GLY B 1 309 ? 102.664 97.829  141.232 1.00 62.36  ? 309 GLY B O   1 
ATOM   3859 N  N   . PRO B 1 310 ? 100.599 97.492  140.417 1.00 52.48  ? 310 PRO B N   1 
ATOM   3860 C  CA  . PRO B 1 310 ? 101.089 96.568  139.382 1.00 52.48  ? 310 PRO B CA  1 
ATOM   3861 C  C   . PRO B 1 310 ? 102.071 97.246  138.438 1.00 52.48  ? 310 PRO B C   1 
ATOM   3862 O  O   . PRO B 1 310 ? 102.050 98.466  138.273 1.00 52.48  ? 310 PRO B O   1 
ATOM   3863 C  CB  . PRO B 1 310 ? 99.811  96.138  138.656 1.00 52.48  ? 310 PRO B CB  1 
ATOM   3864 N  N   . CYS B 1 311 ? 102.959 96.438  137.839 1.00 51.06  ? 311 CYS B N   1 
ATOM   3865 C  CA  . CYS B 1 311 ? 103.964 96.933  136.899 1.00 51.06  ? 311 CYS B CA  1 
ATOM   3866 C  C   . CYS B 1 311 ? 103.754 96.438  135.476 1.00 51.06  ? 311 CYS B C   1 
ATOM   3867 O  O   . CYS B 1 311 ? 104.441 96.913  134.569 1.00 51.06  ? 311 CYS B O   1 
ATOM   3868 C  CB  . CYS B 1 311 ? 105.365 96.537  137.341 1.00 51.06  ? 311 CYS B CB  1 
ATOM   3869 S  SG  . CYS B 1 311 ? 105.811 97.111  138.958 1.00 51.06  ? 311 CYS B SG  1 
ATOM   3870 N  N   . TRP B 1 312 ? 102.800 95.532  135.292 1.00 47.66  ? 312 TRP B N   1 
ATOM   3871 C  CA  . TRP B 1 312 ? 102.444 94.985  133.955 1.00 47.66  ? 312 TRP B CA  1 
ATOM   3872 C  C   . TRP B 1 312 ? 101.783 96.092  133.128 1.00 47.66  ? 312 TRP B C   1 
ATOM   3873 O  O   . TRP B 1 312 ? 101.572 95.882  131.921 1.00 47.66  ? 312 TRP B O   1 
ATOM   3874 C  CB  . TRP B 1 312 ? 101.504 93.783  134.132 1.00 47.66  ? 312 TRP B CB  1 
ATOM   3875 C  CG  . TRP B 1 312 ? 100.614 93.475  132.964 1.00 47.66  ? 312 TRP B CG  1 
ATOM   3876 C  CD1 . TRP B 1 312 ? 100.678 92.377  132.156 1.00 47.66  ? 312 TRP B CD1 1 
ATOM   3877 C  CD2 . TRP B 1 312 ? 99.498  94.250  132.490 1.00 47.66  ? 312 TRP B CD2 1 
ATOM   3878 N  NE1 . TRP B 1 312 ? 99.695  92.422  131.205 1.00 47.66  ? 312 TRP B NE1 1 
ATOM   3879 C  CE2 . TRP B 1 312 ? 98.957  93.561  131.383 1.00 47.66  ? 312 TRP B CE2 1 
ATOM   3880 C  CE3 . TRP B 1 312 ? 98.912  95.458  132.880 1.00 47.66  ? 312 TRP B CE3 1 
ATOM   3881 C  CZ2 . TRP B 1 312 ? 97.859  94.042  130.672 1.00 47.66  ? 312 TRP B CZ2 1 
ATOM   3882 C  CZ3 . TRP B 1 312 ? 97.831  95.936  132.176 1.00 47.66  ? 312 TRP B CZ3 1 
ATOM   3883 C  CH2 . TRP B 1 312 ? 97.311  95.233  131.089 1.00 47.66  ? 312 TRP B CH2 1 
ATOM   3884 N  N   . VAL B 1 313 ? 101.486 97.229  133.750 1.00 39.51  ? 313 VAL B N   1 
ATOM   3885 C  CA  . VAL B 1 313 ? 100.803 98.361  133.057 1.00 39.51  ? 313 VAL B CA  1 
ATOM   3886 C  C   . VAL B 1 313 ? 101.737 99.572  133.045 1.00 39.51  ? 313 VAL B C   1 
ATOM   3887 O  O   . VAL B 1 313 ? 101.305 100.638 132.584 1.00 39.51  ? 313 VAL B O   1 
ATOM   3888 C  CB  . VAL B 1 313 ? 99.462  98.702  133.734 1.00 39.51  ? 313 VAL B CB  1 
ATOM   3889 N  N   . LEU B 1 314 ? 102.949 99.440  133.554 1.00 34.14  ? 314 LEU B N   1 
ATOM   3890 C  CA  . LEU B 1 314 ? 103.889 100.588 133.522 1.00 34.14  ? 314 LEU B CA  1 
ATOM   3891 C  C   . LEU B 1 314 ? 104.526 100.615 132.130 1.00 34.14  ? 314 LEU B C   1 
ATOM   3892 O  O   . LEU B 1 314 ? 104.944 101.701 131.689 1.00 34.14  ? 314 LEU B O   1 
ATOM   3893 C  CB  . LEU B 1 314 ? 104.941 100.400 134.620 1.00 34.14  ? 314 LEU B CB  1 
ATOM   3894 C  CG  . LEU B 1 314 ? 105.288 101.657 135.415 1.00 34.14  ? 314 LEU B CG  1 
ATOM   3895 C  CD1 . LEU B 1 314 ? 106.585 101.470 136.184 1.00 34.14  ? 314 LEU B CD1 1 
ATOM   3896 C  CD2 . LEU B 1 314 ? 105.390 102.861 134.497 1.00 34.14  ? 314 LEU B CD2 1 
ATOM   3897 N  N   . TYR B 1 315 ? 104.578 99.460  131.472 1.00 27.29  ? 315 TYR B N   1 
ATOM   3898 C  CA  . TYR B 1 315 ? 105.147 99.330  130.105 1.00 27.29  ? 315 TYR B CA  1 
ATOM   3899 C  C   . TYR B 1 315 ? 104.034 98.914  129.141 1.00 27.29  ? 315 TYR B C   1 
ATOM   3900 O  O   . TYR B 1 315 ? 104.277 98.045  128.279 1.00 27.29  ? 315 TYR B O   1 
ATOM   3901 C  CB  . TYR B 1 315 ? 106.281 98.305  130.082 1.00 27.29  ? 315 TYR B CB  1 
ATOM   3902 C  CG  . TYR B 1 315 ? 107.466 98.676  130.933 1.00 27.29  ? 315 TYR B CG  1 
ATOM   3903 C  CD1 . TYR B 1 315 ? 107.970 99.963  130.923 1.00 27.29  ? 315 TYR B CD1 1 
ATOM   3904 C  CD2 . TYR B 1 315 ? 108.077 97.744  131.754 1.00 27.29  ? 315 TYR B CD2 1 
ATOM   3905 C  CE1 . TYR B 1 315 ? 109.057 100.318 131.704 1.00 27.29  ? 315 TYR B CE1 1 
ATOM   3906 C  CE2 . TYR B 1 315 ? 109.163 98.082  132.541 1.00 27.29  ? 315 TYR B CE2 1 
ATOM   3907 C  CZ  . TYR B 1 315 ? 109.655 99.373  132.515 1.00 27.29  ? 315 TYR B CZ  1 
ATOM   3908 O  OH  . TYR B 1 315 ? 110.723 99.716  133.290 1.00 27.29  ? 315 TYR B OH  1 
ATOM   3909 N  N   . LEU B 1 316 ? 102.847 99.489  129.308 1.00 25.41  ? 316 LEU B N   1 
ATOM   3910 C  CA  . LEU B 1 316 ? 101.693 99.208  128.412 1.00 25.41  ? 316 LEU B CA  1 
ATOM   3911 C  C   . LEU B 1 316 ? 101.651 100.285 127.327 1.00 25.41  ? 316 LEU B C   1 
ATOM   3912 O  O   . LEU B 1 316 ? 100.709 100.262 126.523 1.00 25.41  ? 316 LEU B O   1 
ATOM   3913 C  CB  . LEU B 1 316 ? 100.397 99.216  129.225 1.00 25.41  ? 316 LEU B CB  1 
ATOM   3914 N  N   . ASP B 1 317 ? 102.631 101.192 127.310 1.00 23.41  ? 317 ASP B N   1 
ATOM   3915 C  CA  . ASP B 1 317 ? 102.667 102.283 126.296 1.00 23.41  ? 317 ASP B CA  1 
ATOM   3916 C  C   . ASP B 1 317 ? 103.766 102.024 125.256 1.00 23.41  ? 317 ASP B C   1 
ATOM   3917 O  O   . ASP B 1 317 ? 103.408 101.834 124.078 1.00 23.41  ? 317 ASP B O   1 
ATOM   3918 C  CB  . ASP B 1 317 ? 102.855 103.650 126.954 1.00 23.41  ? 317 ASP B CB  1 
ATOM   3919 C  CG  . ASP B 1 317 ? 103.729 104.587 126.140 1.00 23.41  ? 317 ASP B CG  1 
ATOM   3920 O  OD1 . ASP B 1 317 ? 103.187 105.572 125.601 1.00 23.41  ? 317 ASP B OD1 1 
ATOM   3921 O  OD2 . ASP B 1 317 ? 104.944 104.324 126.049 1.00 23.41  ? 317 ASP B OD2 1 
ATOM   3922 N  N   . PRO B 1 318 ? 105.055 101.993 125.651 1.00 23.51  ? 318 PRO B N   1 
ATOM   3923 C  CA  . PRO B 1 318 ? 106.040 101.718 124.596 1.00 23.51  ? 318 PRO B CA  1 
ATOM   3924 C  C   . PRO B 1 318 ? 105.716 100.529 123.713 1.00 23.51  ? 318 PRO B C   1 
ATOM   3925 O  O   . PRO B 1 318 ? 106.065 100.563 122.531 1.00 23.51  ? 318 PRO B O   1 
ATOM   3926 C  CB  . PRO B 1 318 ? 107.337 101.497 125.376 1.00 23.51  ? 318 PRO B CB  1 
ATOM   3927 C  CG  . PRO B 1 318 ? 106.915 101.200 126.722 1.00 23.51  ? 318 PRO B CG  1 
ATOM   3928 C  CD  . PRO B 1 318 ? 105.697 101.998 126.967 1.00 23.51  ? 318 PRO B CD  1 
ATOM   3929 N  N   . THR B 1 319 ? 105.064 99.484  124.206 1.00 21.21  ? 319 THR B N   1 
ATOM   3930 C  CA  . THR B 1 319 ? 104.636 98.454  123.270 1.00 21.21  ? 319 THR B CA  1 
ATOM   3931 C  C   . THR B 1 319 ? 103.626 99.008  122.277 1.00 21.21  ? 319 THR B C   1 
ATOM   3932 O  O   . THR B 1 319 ? 103.644 98.652  121.092 1.00 21.21  ? 319 THR B O   1 
ATOM   3933 C  CB  . THR B 1 319 ? 104.052 97.266  124.002 1.00 21.21  ? 319 THR B CB  1 
ATOM   3934 O  OG1 . THR B 1 319 ? 105.053 96.715  124.856 1.00 21.21  ? 319 THR B OG1 1 
ATOM   3935 C  CG2 . THR B 1 319 ? 103.612 96.223  123.002 1.00 21.21  ? 319 THR B CG2 1 
ATOM   3936 N  N   . LEU B 1 320 ? 102.761 99.905  122.720 1.00 19.29  ? 320 LEU B N   1 
ATOM   3937 C  CA  . LEU B 1 320 ? 101.834 100.508 121.778 1.00 19.29  ? 320 LEU B CA  1 
ATOM   3938 C  C   . LEU B 1 320 ? 102.559 101.413 120.781 1.00 19.29  ? 320 LEU B C   1 
ATOM   3939 O  O   . LEU B 1 320 ? 102.189 101.458 119.606 1.00 19.29  ? 320 LEU B O   1 
ATOM   3940 C  CB  . LEU B 1 320 ? 100.745 101.253 122.532 1.00 19.29  ? 320 LEU B CB  1 
ATOM   3941 C  CG  . LEU B 1 320 ? 99.834  100.352 123.367 1.00 19.29  ? 320 LEU B CG  1 
ATOM   3942 C  CD1 . LEU B 1 320 ? 98.709  101.155 123.956 1.00 19.29  ? 320 LEU B CD1 1 
ATOM   3943 C  CD2 . LEU B 1 320 ? 99.270  99.212  122.559 1.00 19.29  ? 320 LEU B CD2 1 
ATOM   3944 N  N   . CYS B 1 321 ? 103.602 102.127 121.209 1.00 20.76  ? 321 CYS B N   1 
ATOM   3945 C  CA  . CYS B 1 321 ? 104.355 102.922 120.239 1.00 20.76  ? 321 CYS B CA  1 
ATOM   3946 C  C   . CYS B 1 321 ? 105.088 102.047 119.236 1.00 20.76  ? 321 CYS B C   1 
ATOM   3947 O  O   . CYS B 1 321 ? 105.172 102.400 118.058 1.00 20.76  ? 321 CYS B O   1 
ATOM   3948 C  CB  . CYS B 1 321 ? 105.346 103.850 120.921 1.00 20.76  ? 321 CYS B CB  1 
ATOM   3949 S  SG  . CYS B 1 321 ? 104.591 105.272 121.694 1.00 20.76  ? 321 CYS B SG  1 
ATOM   3950 N  N   . VAL B 1 322 ? 105.635 100.916 119.669 1.00 16.24  ? 322 VAL B N   1 
ATOM   3951 C  CA  . VAL B 1 322 ? 106.280 100.011 118.721 1.00 16.24  ? 322 VAL B CA  1 
ATOM   3952 C  C   . VAL B 1 322 ? 105.268 99.465  117.717 1.00 16.24  ? 322 VAL B C   1 
ATOM   3953 O  O   . VAL B 1 322 ? 105.569 99.321  116.526 1.00 16.24  ? 322 VAL B O   1 
ATOM   3954 C  CB  . VAL B 1 322 ? 107.010 98.890  119.475 1.00 16.24  ? 322 VAL B CB  1 
ATOM   3955 C  CG1 . VAL B 1 322 ? 107.231 97.712  118.572 1.00 16.24  ? 322 VAL B CG1 1 
ATOM   3956 C  CG2 . VAL B 1 322 ? 108.324 99.403  120.029 1.00 16.24  ? 322 VAL B CG2 1 
ATOM   3957 N  N   . VAL B 1 323 ? 104.045 99.178  118.161 1.00 18.03  ? 323 VAL B N   1 
ATOM   3958 C  CA  . VAL B 1 323 ? 103.046 98.745  117.191 1.00 18.03  ? 323 VAL B CA  1 
ATOM   3959 C  C   . VAL B 1 323 ? 102.666 99.871  116.230 1.00 18.03  ? 323 VAL B C   1 
ATOM   3960 O  O   . VAL B 1 323 ? 102.492 99.633  115.029 1.00 18.03  ? 323 VAL B O   1 
ATOM   3961 C  CB  . VAL B 1 323 ? 101.808 98.183  117.893 1.00 18.03  ? 323 VAL B CB  1 
ATOM   3962 C  CG1 . VAL B 1 323 ? 100.914 97.562  116.878 1.00 18.03  ? 323 VAL B CG1 1 
ATOM   3963 C  CG2 . VAL B 1 323 ? 102.204 97.138  118.884 1.00 18.03  ? 323 VAL B CG2 1 
ATOM   3964 N  N   . MET B 1 324 ? 102.527 101.104 116.714 1.00 20.51  ? 324 MET B N   1 
ATOM   3965 C  CA  . MET B 1 324 ? 102.204 102.208 115.806 1.00 20.51  ? 324 MET B CA  1 
ATOM   3966 C  C   . MET B 1 324 ? 103.317 102.445 114.793 1.00 20.51  ? 324 MET B C   1 
ATOM   3967 O  O   . MET B 1 324 ? 103.048 102.779 113.633 1.00 20.51  ? 324 MET B O   1 
ATOM   3968 C  CB  . MET B 1 324 ? 101.935 103.475 116.600 1.00 20.51  ? 324 MET B CB  1 
ATOM   3969 C  CG  . MET B 1 324 ? 101.681 104.692 115.771 1.00 20.51  ? 324 MET B CG  1 
ATOM   3970 S  SD  . MET B 1 324 ? 101.633 106.172 116.794 1.00 20.51  ? 324 MET B SD  1 
ATOM   3971 C  CE  . MET B 1 324 ? 103.305 106.764 116.638 1.00 20.51  ? 324 MET B CE  1 
ATOM   3972 N  N   . VAL B 1 325 ? 104.569 102.272 115.207 1.00 14.59  ? 325 VAL B N   1 
ATOM   3973 C  CA  . VAL B 1 325 ? 105.692 102.433 114.289 1.00 14.59  ? 325 VAL B CA  1 
ATOM   3974 C  C   . VAL B 1 325 ? 105.685 101.359 113.212 1.00 14.59  ? 325 VAL B C   1 
ATOM   3975 O  O   . VAL B 1 325 ? 105.872 101.650 112.025 1.00 14.59  ? 325 VAL B O   1 
ATOM   3976 C  CB  . VAL B 1 325 ? 107.007 102.428 115.071 1.00 14.59  ? 325 VAL B CB  1 
ATOM   3977 C  CG1 . VAL B 1 325 ? 108.122 102.045 114.171 1.00 14.59  ? 325 VAL B CG1 1 
ATOM   3978 C  CG2 . VAL B 1 325 ? 107.248 103.792 115.619 1.00 14.59  ? 325 VAL B CG2 1 
ATOM   3979 N  N   . CYS B 1 326 ? 105.495 100.102 113.592 1.00 17.16  ? 326 CYS B N   1 
ATOM   3980 C  CA  . CYS B 1 326 ? 105.432 99.077  112.556 1.00 17.16  ? 326 CYS B CA  1 
ATOM   3981 C  C   . CYS B 1 326 ? 104.181 99.196  111.695 1.00 17.16  ? 326 CYS B C   1 
ATOM   3982 O  O   . CYS B 1 326 ? 104.129 98.600  110.623 1.00 17.16  ? 326 CYS B O   1 
ATOM   3983 C  CB  . CYS B 1 326 ? 105.517 97.693  113.186 1.00 17.16  ? 326 CYS B CB  1 
ATOM   3984 S  SG  . CYS B 1 326 ? 105.168 96.313  112.088 1.00 17.16  ? 326 CYS B SG  1 
ATOM   3985 N  N   . ILE B 1 327 ? 103.171 99.940  112.128 1.00 14.65  ? 327 ILE B N   1 
ATOM   3986 C  CA  . ILE B 1 327 ? 102.042 100.184 111.235 1.00 14.65  ? 327 ILE B CA  1 
ATOM   3987 C  C   . ILE B 1 327 ? 102.375 101.268 110.211 1.00 14.65  ? 327 ILE B C   1 
ATOM   3988 O  O   . ILE B 1 327 ? 102.128 101.106 109.005 1.00 14.65  ? 327 ILE B O   1 
ATOM   3989 C  CB  . ILE B 1 327 ? 100.793 100.556 112.045 1.00 14.65  ? 327 ILE B CB  1 
ATOM   3990 C  CG1 . ILE B 1 327 ? 100.348 99.393  112.922 1.00 14.65  ? 327 ILE B CG1 1 
ATOM   3991 C  CG2 . ILE B 1 327 ? 99.679  100.950 111.116 1.00 14.65  ? 327 ILE B CG2 1 
ATOM   3992 C  CD1 . ILE B 1 327 ? 99.810  98.233  112.169 1.00 14.65  ? 327 ILE B CD1 1 
ATOM   3993 N  N   . LEU B 1 328 ? 102.930 102.392 110.663 1.00 17.68  ? 328 LEU B N   1 
ATOM   3994 C  CA  . LEU B 1 328 ? 103.242 103.474 109.734 1.00 17.68  ? 328 LEU B CA  1 
ATOM   3995 C  C   . LEU B 1 328 ? 104.324 103.085 108.738 1.00 17.68  ? 328 LEU B C   1 
ATOM   3996 O  O   . LEU B 1 328 ? 104.253 103.465 107.569 1.00 17.68  ? 328 LEU B O   1 
ATOM   3997 C  CB  . LEU B 1 328 ? 103.677 104.718 110.481 1.00 17.68  ? 328 LEU B CB  1 
ATOM   3998 C  CG  . LEU B 1 328 ? 102.520 105.614 110.831 1.00 17.68  ? 328 LEU B CG  1 
ATOM   3999 C  CD1 . LEU B 1 328 ? 103.045 106.942 111.285 1.00 17.68  ? 328 LEU B CD1 1 
ATOM   4000 C  CD2 . LEU B 1 328 ? 101.697 105.758 109.609 1.00 17.68  ? 328 LEU B CD2 1 
ATOM   4001 N  N   . LEU B 1 329 ? 105.356 102.365 109.175 1.00 9.95   ? 329 LEU B N   1 
ATOM   4002 C  CA  . LEU B 1 329 ? 106.457 102.085 108.261 1.00 9.95   ? 329 LEU B CA  1 
ATOM   4003 C  C   . LEU B 1 329 ? 106.091 101.087 107.185 1.00 9.95   ? 329 LEU B C   1 
ATOM   4004 O  O   . LEU B 1 329 ? 106.868 100.888 106.255 1.00 9.95   ? 329 LEU B O   1 
ATOM   4005 C  CB  . LEU B 1 329 ? 107.660 101.557 109.014 1.00 9.95   ? 329 LEU B CB  1 
ATOM   4006 C  CG  . LEU B 1 329 ? 108.358 102.590 109.864 1.00 9.95   ? 329 LEU B CG  1 
ATOM   4007 C  CD1 . LEU B 1 329 ? 109.699 102.046 110.260 1.00 9.95   ? 329 LEU B CD1 1 
ATOM   4008 C  CD2 . LEU B 1 329 ? 108.480 103.861 109.087 1.00 9.95   ? 329 LEU B CD2 1 
ATOM   4009 N  N   . TYR B 1 330 ? 104.963 100.418 107.302 1.00 16.50  ? 330 TYR B N   1 
ATOM   4010 C  CA  . TYR B 1 330 ? 104.530 99.591  106.197 1.00 16.50  ? 330 TYR B CA  1 
ATOM   4011 C  C   . TYR B 1 330 ? 103.461 100.273 105.381 1.00 16.50  ? 330 TYR B C   1 
ATOM   4012 O  O   . TYR B 1 330 ? 103.335 100.006 104.187 1.00 16.50  ? 330 TYR B O   1 
ATOM   4013 C  CB  . TYR B 1 330 ? 103.999 98.263  106.692 1.00 16.50  ? 330 TYR B CB  1 
ATOM   4014 C  CG  . TYR B 1 330 ? 103.213 97.540  105.652 1.00 16.50  ? 330 TYR B CG  1 
ATOM   4015 C  CD1 . TYR B 1 330 ? 103.785 97.178  104.456 1.00 16.50  ? 330 TYR B CD1 1 
ATOM   4016 C  CD2 . TYR B 1 330 ? 101.902 97.209  105.866 1.00 16.50  ? 330 TYR B CD2 1 
ATOM   4017 C  CE1 . TYR B 1 330 ? 103.070 96.517  103.499 1.00 16.50  ? 330 TYR B CE1 1 
ATOM   4018 C  CE2 . TYR B 1 330 ? 101.181 96.542  104.913 1.00 16.50  ? 330 TYR B CE2 1 
ATOM   4019 C  CZ  . TYR B 1 330 ? 101.769 96.198  103.732 1.00 16.50  ? 330 TYR B CZ  1 
ATOM   4020 O  OH  . TYR B 1 330 ? 101.043 95.530  102.779 1.00 16.50  ? 330 TYR B OH  1 
ATOM   4021 N  N   . THR B 1 331 ? 102.667 101.150 105.990 1.00 16.06  ? 331 THR B N   1 
ATOM   4022 C  CA  . THR B 1 331 ? 101.722 101.877 105.157 1.00 16.06  ? 331 THR B CA  1 
ATOM   4023 C  C   . THR B 1 331 ? 102.402 102.949 104.310 1.00 16.06  ? 331 THR B C   1 
ATOM   4024 O  O   . THR B 1 331 ? 101.910 103.263 103.226 1.00 16.06  ? 331 THR B O   1 
ATOM   4025 C  CB  . THR B 1 331 ? 100.630 102.481 106.022 1.00 16.06  ? 331 THR B CB  1 
ATOM   4026 O  OG1 . THR B 1 331 ? 100.267 101.541 107.032 1.00 16.06  ? 331 THR B OG1 1 
ATOM   4027 C  CG2 . THR B 1 331 ? 99.428  102.708 105.197 1.00 16.06  ? 331 THR B CG2 1 
ATOM   4028 N  N   . THR B 1 332 ? 103.539 103.486 104.752 1.00 14.58  ? 332 THR B N   1 
ATOM   4029 C  CA  . THR B 1 332 ? 104.253 104.518 104.011 1.00 14.58  ? 332 THR B CA  1 
ATOM   4030 C  C   . THR B 1 332 ? 105.070 103.979 102.854 1.00 14.58  ? 332 THR B C   1 
ATOM   4031 O  O   . THR B 1 332 ? 105.033 104.558 101.770 1.00 14.58  ? 332 THR B O   1 
ATOM   4032 C  CB  . THR B 1 332 ? 105.185 105.293 104.936 1.00 14.58  ? 332 THR B CB  1 
ATOM   4033 O  OG1 . THR B 1 332 ? 104.428 106.220 105.705 1.00 14.58  ? 332 THR B OG1 1 
ATOM   4034 C  CG2 . THR B 1 332 ? 106.208 106.036 104.166 1.00 14.58  ? 332 THR B CG2 1 
ATOM   4035 N  N   . TYR B 1 333 ? 105.791 102.882 103.042 1.00 12.94  ? 333 TYR B N   1 
ATOM   4036 C  CA  . TYR B 1 333 ? 106.811 102.485 102.073 1.00 12.94  ? 333 TYR B CA  1 
ATOM   4037 C  C   . TYR B 1 333 ? 106.338 102.492 100.626 1.00 12.94  ? 333 TYR B C   1 
ATOM   4038 O  O   . TYR B 1 333 ? 107.018 103.114 99.800  1.00 12.94  ? 333 TYR B O   1 
ATOM   4039 C  CB  . TYR B 1 333 ? 107.385 101.114 102.440 1.00 12.94  ? 333 TYR B CB  1 
ATOM   4040 C  CG  . TYR B 1 333 ? 107.952 100.359 101.270 1.00 12.94  ? 333 TYR B CG  1 
ATOM   4041 C  CD1 . TYR B 1 333 ? 109.247 100.570 100.840 1.00 12.94  ? 333 TYR B CD1 1 
ATOM   4042 C  CD2 . TYR B 1 333 ? 107.190 99.425  100.599 1.00 12.94  ? 333 TYR B CD2 1 
ATOM   4043 C  CE1 . TYR B 1 333 ? 109.761 99.871  99.772  1.00 12.94  ? 333 TYR B CE1 1 
ATOM   4044 C  CE2 . TYR B 1 333 ? 107.690 98.731  99.534  1.00 12.94  ? 333 TYR B CE2 1 
ATOM   4045 C  CZ  . TYR B 1 333 ? 108.971 98.955  99.122  1.00 12.94  ? 333 TYR B CZ  1 
ATOM   4046 O  OH  . TYR B 1 333 ? 109.446 98.244  98.052  1.00 12.94  ? 333 TYR B OH  1 
ATOM   4047 N  N   . PRO B 1 334 ? 105.213 101.876 100.243 1.00 13.29  ? 334 PRO B N   1 
ATOM   4048 C  CA  . PRO B 1 334 ? 104.872 101.861 98.809  1.00 13.29  ? 334 PRO B CA  1 
ATOM   4049 C  C   . PRO B 1 334 ? 104.759 103.242 98.186  1.00 13.29  ? 334 PRO B C   1 
ATOM   4050 O  O   . PRO B 1 334 ? 105.170 103.434 97.034  1.00 13.29  ? 334 PRO B O   1 
ATOM   4051 C  CB  . PRO B 1 334 ? 103.540 101.103 98.776  1.00 13.29  ? 334 PRO B CB  1 
ATOM   4052 C  CG  . PRO B 1 334 ? 103.045 101.125 100.152 1.00 13.29  ? 334 PRO B CG  1 
ATOM   4053 C  CD  . PRO B 1 334 ? 104.231 101.118 101.027 1.00 13.29  ? 334 PRO B CD  1 
ATOM   4054 N  N   . LEU B 1 335 ? 104.231 104.214 98.924  1.00 15.44  ? 335 LEU B N   1 
ATOM   4055 C  CA  . LEU B 1 335 ? 104.250 105.598 98.468  1.00 15.44  ? 335 LEU B CA  1 
ATOM   4056 C  C   . LEU B 1 335 ? 105.667 106.063 98.183  1.00 15.44  ? 335 LEU B C   1 
ATOM   4057 O  O   . LEU B 1 335 ? 105.931 106.695 97.155  1.00 15.44  ? 335 LEU B O   1 
ATOM   4058 C  CB  . LEU B 1 335 ? 103.604 106.493 99.510  1.00 15.44  ? 335 LEU B CB  1 
ATOM   4059 C  CG  . LEU B 1 335 ? 104.001 107.949 99.406  1.00 15.44  ? 335 LEU B CG  1 
ATOM   4060 C  CD1 . LEU B 1 335 ? 103.524 108.519 98.116  1.00 15.44  ? 335 LEU B CD1 1 
ATOM   4061 C  CD2 . LEU B 1 335 ? 103.442 108.723 100.569 1.00 15.44  ? 335 LEU B CD2 1 
ATOM   4062 N  N   . LEU B 1 336 ? 106.593 105.782 99.092  1.00 10.60  ? 336 LEU B N   1 
ATOM   4063 C  CA  . LEU B 1 336 ? 107.958 106.248 98.894  1.00 10.60  ? 336 LEU B CA  1 
ATOM   4064 C  C   . LEU B 1 336 ? 108.618 105.542 97.721  1.00 10.60  ? 336 LEU B C   1 
ATOM   4065 O  O   . LEU B 1 336 ? 109.377 106.158 96.963  1.00 10.60  ? 336 LEU B O   1 
ATOM   4066 C  CB  . LEU B 1 336 ? 108.761 106.054 100.165 1.00 10.60  ? 336 LEU B CB  1 
ATOM   4067 C  CG  . LEU B 1 336 ? 110.068 106.808 100.138 1.00 10.60  ? 336 LEU B CG  1 
ATOM   4068 C  CD1 . LEU B 1 336 ? 110.324 107.371 101.482 1.00 10.60  ? 336 LEU B CD1 1 
ATOM   4069 C  CD2 . LEU B 1 336 ? 111.152 105.850 99.800  1.00 10.60  ? 336 LEU B CD2 1 
ATOM   4070 N  N   . LYS B 1 337 ? 108.331 104.260 97.538  1.00 13.65  ? 337 LYS B N   1 
ATOM   4071 C  CA  . LYS B 1 337 ? 108.849 103.564 96.373  1.00 13.65  ? 337 LYS B CA  1 
ATOM   4072 C  C   . LYS B 1 337 ? 108.356 104.214 95.096  1.00 13.65  ? 337 LYS B C   1 
ATOM   4073 O  O   . LYS B 1 337 ? 109.149 104.504 94.197  1.00 13.65  ? 337 LYS B O   1 
ATOM   4074 C  CB  . LYS B 1 337 ? 108.446 102.103 96.396  1.00 13.65  ? 337 LYS B CB  1 
ATOM   4075 C  CG  . LYS B 1 337 ? 108.483 101.462 95.041  1.00 13.65  ? 337 LYS B CG  1 
ATOM   4076 C  CD  . LYS B 1 337 ? 107.791 100.131 95.073  1.00 13.65  ? 337 LYS B CD  1 
ATOM   4077 C  CE  . LYS B 1 337 ? 107.248 99.760  93.721  1.00 13.65  ? 337 LYS B CE  1 
ATOM   4078 N  NZ  . LYS B 1 337 ? 106.151 98.775  93.851  1.00 13.65  ? 337 LYS B NZ  1 
ATOM   4079 N  N   . GLU B 1 338 ? 107.052 104.469 94.997  1.00 10.86  ? 338 GLU B N   1 
ATOM   4080 C  CA  . GLU B 1 338 ? 106.518 105.024 93.755  1.00 10.86  ? 338 GLU B CA  1 
ATOM   4081 C  C   . GLU B 1 338 ? 107.059 106.416 93.473  1.00 10.86  ? 338 GLU B C   1 
ATOM   4082 O  O   . GLU B 1 338 ? 107.377 106.747 92.327  1.00 10.86  ? 338 GLU B O   1 
ATOM   4083 C  CB  . GLU B 1 338 ? 105.004 105.058 93.796  1.00 10.86  ? 338 GLU B CB  1 
ATOM   4084 C  CG  . GLU B 1 338 ? 104.424 105.469 92.498  1.00 10.86  ? 338 GLU B CG  1 
ATOM   4085 C  CD  . GLU B 1 338 ? 104.651 104.427 91.433  1.00 10.86  ? 338 GLU B CD  1 
ATOM   4086 O  OE1 . GLU B 1 338 ? 105.062 103.298 91.768  1.00 10.86  ? 338 GLU B OE1 1 
ATOM   4087 O  OE2 . GLU B 1 338 ? 104.409 104.721 90.250  1.00 10.86  ? 338 GLU B OE2 1 
ATOM   4088 N  N   . SER B 1 339 ? 107.188 107.244 94.503  1.00 9.98   ? 339 SER B N   1 
ATOM   4089 C  CA  . SER B 1 339 ? 107.715 108.582 94.290  1.00 9.98   ? 339 SER B CA  1 
ATOM   4090 C  C   . SER B 1 339 ? 109.170 108.550 93.835  1.00 9.98   ? 339 SER B C   1 
ATOM   4091 O  O   . SER B 1 339 ? 109.543 109.226 92.868  1.00 9.98   ? 339 SER B O   1 
ATOM   4092 C  CB  . SER B 1 339 ? 107.567 109.394 95.558  1.00 9.98   ? 339 SER B CB  1 
ATOM   4093 O  OG  . SER B 1 339 ? 108.557 110.382 95.589  1.00 9.98   ? 339 SER B OG  1 
ATOM   4094 N  N   . ALA B 1 340 ? 110.020 107.774 94.507  1.00 8.14   ? 340 ALA B N   1 
ATOM   4095 C  CA  . ALA B 1 340 ? 111.418 107.760 94.089  1.00 8.14   ? 340 ALA B CA  1 
ATOM   4096 C  C   . ALA B 1 340 ? 111.575 107.137 92.710  1.00 8.14   ? 340 ALA B C   1 
ATOM   4097 O  O   . ALA B 1 340 ? 112.432 107.554 91.924  1.00 8.14   ? 340 ALA B O   1 
ATOM   4098 C  CB  . ALA B 1 340 ? 112.272 107.022 95.106  1.00 8.14   ? 340 ALA B CB  1 
ATOM   4099 N  N   . LEU B 1 341 ? 110.749 106.151 92.384  1.00 7.72   ? 341 LEU B N   1 
ATOM   4100 C  CA  . LEU B 1 341 ? 110.812 105.568 91.054  1.00 7.72   ? 341 LEU B CA  1 
ATOM   4101 C  C   . LEU B 1 341 ? 110.435 106.577 89.975  1.00 7.72   ? 341 LEU B C   1 
ATOM   4102 O  O   . LEU B 1 341 ? 111.115 106.669 88.952  1.00 7.72   ? 341 LEU B O   1 
ATOM   4103 C  CB  . LEU B 1 341 ? 109.924 104.336 90.996  1.00 7.72   ? 341 LEU B CB  1 
ATOM   4104 C  CG  . LEU B 1 341 ? 110.660 103.018 91.172  1.00 7.72   ? 341 LEU B CG  1 
ATOM   4105 C  CD1 . LEU B 1 341 ? 111.251 102.609 89.872  1.00 7.72   ? 341 LEU B CD1 1 
ATOM   4106 C  CD2 . LEU B 1 341 ? 111.780 103.193 92.151  1.00 7.72   ? 341 LEU B CD2 1 
ATOM   4107 N  N   . ILE B 1 342 ? 109.369 107.351 90.173  1.00 8.86   ? 342 ILE B N   1 
ATOM   4108 C  CA  . ILE B 1 342 ? 109.060 108.392 89.195  1.00 8.86   ? 342 ILE B CA  1 
ATOM   4109 C  C   . ILE B 1 342 ? 110.221 109.359 89.057  1.00 8.86   ? 342 ILE B C   1 
ATOM   4110 O  O   . ILE B 1 342 ? 110.524 109.828 87.959  1.00 8.86   ? 342 ILE B O   1 
ATOM   4111 C  CB  . ILE B 1 342 ? 107.776 109.131 89.580  1.00 8.86   ? 342 ILE B CB  1 
ATOM   4112 C  CG1 . ILE B 1 342 ? 106.567 108.435 89.021  1.00 8.86   ? 342 ILE B CG1 1 
ATOM   4113 C  CG2 . ILE B 1 342 ? 107.787 110.502 89.066  1.00 8.86   ? 342 ILE B CG2 1 
ATOM   4114 C  CD1 . ILE B 1 342 ? 105.315 109.144 89.385  1.00 8.86   ? 342 ILE B CD1 1 
ATOM   4115 N  N   . LEU B 1 343 ? 110.888 109.680 90.163  1.00 4.92   ? 343 LEU B N   1 
ATOM   4116 C  CA  . LEU B 1 343 ? 111.934 110.693 90.087  1.00 4.92   ? 343 LEU B CA  1 
ATOM   4117 C  C   . LEU B 1 343 ? 113.275 110.147 89.624  1.00 4.92   ? 343 LEU B C   1 
ATOM   4118 O  O   . LEU B 1 343 ? 114.225 110.921 89.512  1.00 4.92   ? 343 LEU B O   1 
ATOM   4119 C  CB  . LEU B 1 343 ? 112.102 111.381 91.439  1.00 4.92   ? 343 LEU B CB  1 
ATOM   4120 C  CG  . LEU B 1 343 ? 111.292 112.645 91.683  1.00 4.92   ? 343 LEU B CG  1 
ATOM   4121 C  CD1 . LEU B 1 343 ? 109.886 112.309 91.977  1.00 4.92   ? 343 LEU B CD1 1 
ATOM   4122 C  CD2 . LEU B 1 343 ? 111.847 113.381 92.829  1.00 4.92   ? 343 LEU B CD2 1 
ATOM   4123 N  N   . LEU B 1 344 ? 113.396 108.845 89.381  1.00 7.64   ? 344 LEU B N   1 
ATOM   4124 C  CA  . LEU B 1 344 ? 114.629 108.284 88.838  1.00 7.64   ? 344 LEU B CA  1 
ATOM   4125 C  C   . LEU B 1 344 ? 114.520 107.921 87.352  1.00 7.64   ? 344 LEU B C   1 
ATOM   4126 O  O   . LEU B 1 344 ? 115.240 107.033 86.884  1.00 7.64   ? 344 LEU B O   1 
ATOM   4127 C  CB  . LEU B 1 344 ? 115.055 107.058 89.641  1.00 7.64   ? 344 LEU B CB  1 
ATOM   4128 C  CG  . LEU B 1 344 ? 115.838 107.289 90.926  1.00 7.64   ? 344 LEU B CG  1 
ATOM   4129 C  CD1 . LEU B 1 344 ? 116.275 105.977 91.468  1.00 7.64   ? 344 LEU B CD1 1 
ATOM   4130 C  CD2 . LEU B 1 344 ? 117.022 108.167 90.687  1.00 7.64   ? 344 LEU B CD2 1 
ATOM   4131 N  N   . GLN B 1 345 ? 113.633 108.587 86.610  1.00 9.26   ? 345 GLN B N   1 
ATOM   4132 C  CA  . GLN B 1 345 ? 113.525 108.445 85.160  1.00 9.26   ? 345 GLN B CA  1 
ATOM   4133 C  C   . GLN B 1 345 ? 113.217 107.020 84.747  1.00 9.26   ? 345 GLN B C   1 
ATOM   4134 O  O   . GLN B 1 345 ? 113.584 106.587 83.661  1.00 9.26   ? 345 GLN B O   1 
ATOM   4135 C  CB  . GLN B 1 345 ? 114.791 108.893 84.450  1.00 9.26   ? 345 GLN B CB  1 
ATOM   4136 C  CG  . GLN B 1 345 ? 115.331 110.199 84.848  1.00 9.26   ? 345 GLN B CG  1 
ATOM   4137 C  CD  . GLN B 1 345 ? 114.413 111.292 84.528  1.00 9.26   ? 345 GLN B CD  1 
ATOM   4138 O  OE1 . GLN B 1 345 ? 113.596 111.172 83.639  1.00 9.26   ? 345 GLN B OE1 1 
ATOM   4139 N  NE2 . GLN B 1 345 ? 114.564 112.403 85.214  1.00 9.26   ? 345 GLN B NE2 1 
ATOM   4140 N  N   . THR B 1 346 ? 112.553 106.271 85.602  1.00 9.08   ? 346 THR B N   1 
ATOM   4141 C  CA  . THR B 1 346 ? 112.354 104.872 85.294  1.00 9.08   ? 346 THR B CA  1 
ATOM   4142 C  C   . THR B 1 346 ? 111.121 104.682 84.442  1.00 9.08   ? 346 THR B C   1 
ATOM   4143 O  O   . THR B 1 346 ? 110.097 105.320 84.673  1.00 9.08   ? 346 THR B O   1 
ATOM   4144 C  CB  . THR B 1 346 ? 112.208 104.040 86.551  1.00 9.08   ? 346 THR B CB  1 
ATOM   4145 O  OG1 . THR B 1 346 ? 110.862 104.136 87.009  1.00 9.08   ? 346 THR B OG1 1 
ATOM   4146 C  CG2 . THR B 1 346 ? 113.140 104.545 87.598  1.00 9.08   ? 346 THR B CG2 1 
ATOM   4147 N  N   . VAL B 1 347 ? 111.232 103.791 83.464  1.00 9.55   ? 347 VAL B N   1 
ATOM   4148 C  CA  . VAL B 1 347 ? 110.101 103.325 82.669  1.00 9.55   ? 347 VAL B CA  1 
ATOM   4149 C  C   . VAL B 1 347 ? 108.937 103.078 83.605  1.00 9.55   ? 347 VAL B C   1 
ATOM   4150 O  O   . VAL B 1 347 ? 109.143 102.533 84.697  1.00 9.55   ? 347 VAL B O   1 
ATOM   4151 C  CB  . VAL B 1 347 ? 110.476 102.045 81.920  1.00 9.55   ? 347 VAL B CB  1 
ATOM   4152 C  CG1 . VAL B 1 347 ? 109.272 101.305 81.497  1.00 9.55   ? 347 VAL B CG1 1 
ATOM   4153 C  CG2 . VAL B 1 347 ? 111.291 102.376 80.746  1.00 9.55   ? 347 VAL B CG2 1 
ATOM   4154 N  N   . PRO B 1 348 ? 107.732 103.464 83.264  1.00 13.79  ? 348 PRO B N   1 
ATOM   4155 C  CA  . PRO B 1 348 ? 106.593 103.210 84.150  1.00 13.79  ? 348 PRO B CA  1 
ATOM   4156 C  C   . PRO B 1 348 ? 106.360 101.730 84.364  1.00 13.79  ? 348 PRO B C   1 
ATOM   4157 O  O   . PRO B 1 348 ? 107.151 100.911 83.902  1.00 13.79  ? 348 PRO B O   1 
ATOM   4158 C  CB  . PRO B 1 348 ? 105.428 103.845 83.401  1.00 13.79  ? 348 PRO B CB  1 
ATOM   4159 C  CG  . PRO B 1 348 ? 106.049 104.767 82.464  1.00 13.79  ? 348 PRO B CG  1 
ATOM   4160 C  CD  . PRO B 1 348 ? 107.335 104.194 82.067  1.00 13.79  ? 348 PRO B CD  1 
ATOM   4161 N  N   . LYS B 1 349 ? 105.315 101.342 85.064  1.00 20.40  ? 349 LYS B N   1 
ATOM   4162 C  CA  . LYS B 1 349 ? 105.098 99.915  85.199  1.00 20.40  ? 349 LYS B CA  1 
ATOM   4163 C  C   . LYS B 1 349 ? 104.321 99.322  84.032  1.00 20.40  ? 349 LYS B C   1 
ATOM   4164 O  O   . LYS B 1 349 ? 104.263 98.098  83.901  1.00 20.40  ? 349 LYS B O   1 
ATOM   4165 C  CB  . LYS B 1 349 ? 104.383 99.607  86.509  1.00 20.40  ? 349 LYS B CB  1 
ATOM   4166 C  CG  . LYS B 1 349 ? 104.856 98.322  87.149  1.00 20.40  ? 349 LYS B CG  1 
ATOM   4167 C  CD  . LYS B 1 349 ? 103.874 97.790  88.154  1.00 20.40  ? 349 LYS B CD  1 
ATOM   4168 C  CE  . LYS B 1 349 ? 104.406 96.511  88.754  1.00 20.40  ? 349 LYS B CE  1 
ATOM   4169 N  NZ  . LYS B 1 349 ? 103.416 95.883  89.668  1.00 20.40  ? 349 LYS B NZ  1 
ATOM   4170 N  N   . GLN B 1 350 ? 103.749 100.145 83.163  1.00 21.44  ? 350 GLN B N   1 
ATOM   4171 C  CA  . GLN B 1 350 ? 102.842 99.646  82.149  1.00 21.44  ? 350 GLN B CA  1 
ATOM   4172 C  C   . GLN B 1 350 ? 103.394 99.645  80.732  1.00 21.44  ? 350 GLN B C   1 
ATOM   4173 O  O   . GLN B 1 350 ? 102.607 99.477  79.800  1.00 21.44  ? 350 GLN B O   1 
ATOM   4174 C  CB  . GLN B 1 350 ? 101.538 100.461 82.149  1.00 21.44  ? 350 GLN B CB  1 
ATOM   4175 C  CG  . GLN B 1 350 ? 101.706 101.932 81.822  1.00 21.44  ? 350 GLN B CG  1 
ATOM   4176 C  CD  . GLN B 1 350 ? 101.539 102.824 83.032  1.00 21.44  ? 350 GLN B CD  1 
ATOM   4177 O  OE1 . GLN B 1 350 ? 101.616 102.362 84.166  1.00 21.44  ? 350 GLN B OE1 1 
ATOM   4178 N  NE2 . GLN B 1 350 ? 101.313 104.111 82.796  1.00 21.44  ? 350 GLN B NE2 1 
ATOM   4179 N  N   . ILE B 1 351 ? 104.694 99.850  80.531  1.00 17.26  ? 351 ILE B N   1 
ATOM   4180 C  CA  . ILE B 1 351 ? 105.284 99.922  79.197  1.00 17.26  ? 351 ILE B CA  1 
ATOM   4181 C  C   . ILE B 1 351 ? 106.506 99.028  79.151  1.00 17.26  ? 351 ILE B C   1 
ATOM   4182 O  O   . ILE B 1 351 ? 107.506 99.314  79.815  1.00 17.26  ? 351 ILE B O   1 
ATOM   4183 C  CB  . ILE B 1 351 ? 105.694 101.350 78.851  1.00 17.26  ? 351 ILE B CB  1 
ATOM   4184 C  CG1 . ILE B 1 351 ? 104.555 102.293 79.089  1.00 17.26  ? 351 ILE B CG1 1 
ATOM   4185 C  CG2 . ILE B 1 351 ? 106.062 101.424 77.438  1.00 17.26  ? 351 ILE B CG2 1 
ATOM   4186 C  CD1 . ILE B 1 351 ? 105.035 103.671 79.202  1.00 17.26  ? 351 ILE B CD1 1 
ATOM   4187 N  N   . ASP B 1 352 ? 106.470 97.985  78.338  1.00 25.33  ? 352 ASP B N   1 
ATOM   4188 C  CA  . ASP B 1 352 ? 107.564 97.016  78.293  1.00 25.33  ? 352 ASP B CA  1 
ATOM   4189 C  C   . ASP B 1 352 ? 108.468 97.354  77.114  1.00 25.33  ? 352 ASP B C   1 
ATOM   4190 O  O   . ASP B 1 352 ? 108.043 97.282  75.961  1.00 25.33  ? 352 ASP B O   1 
ATOM   4191 C  CB  . ASP B 1 352 ? 107.020 95.598  78.196  1.00 25.33  ? 352 ASP B CB  1 
ATOM   4192 C  CG  . ASP B 1 352 ? 107.902 94.598  78.896  1.00 25.33  ? 352 ASP B CG  1 
ATOM   4193 O  OD1 . ASP B 1 352 ? 108.956 95.009  79.423  1.00 25.33  ? 352 ASP B OD1 1 
ATOM   4194 O  OD2 . ASP B 1 352 ? 107.551 93.401  78.918  1.00 25.33  ? 352 ASP B OD2 1 
ATOM   4195 N  N   . ILE B 1 353 ? 109.727 97.701  77.396  1.00 15.40  ? 353 ILE B N   1 
ATOM   4196 C  CA  . ILE B 1 353 ? 110.576 98.247  76.345  1.00 15.40  ? 353 ILE B CA  1 
ATOM   4197 C  C   . ILE B 1 353 ? 110.778 97.252  75.215  1.00 15.40  ? 353 ILE B C   1 
ATOM   4198 O  O   . ILE B 1 353 ? 110.673 97.619  74.040  1.00 15.40  ? 353 ILE B O   1 
ATOM   4199 C  CB  . ILE B 1 353 ? 111.913 98.714  76.923  1.00 15.40  ? 353 ILE B CB  1 
ATOM   4200 C  CG1 . ILE B 1 353 ? 111.740 100.051 77.588  1.00 15.40  ? 353 ILE B CG1 1 
ATOM   4201 C  CG2 . ILE B 1 353 ? 112.897 98.904  75.839  1.00 15.40  ? 353 ILE B CG2 1 
ATOM   4202 C  CD1 . ILE B 1 353 ? 111.289 101.046 76.643  1.00 15.40  ? 353 ILE B CD1 1 
ATOM   4203 N  N   . ARG B 1 354 ? 111.037 95.984  75.527  1.00 20.26  ? 354 ARG B N   1 
ATOM   4204 C  CA  . ARG B 1 354 ? 111.287 95.022  74.456  1.00 20.26  ? 354 ARG B CA  1 
ATOM   4205 C  C   . ARG B 1 354 ? 110.126 94.959  73.479  1.00 20.26  ? 354 ARG B C   1 
ATOM   4206 O  O   . ARG B 1 354 ? 110.329 94.769  72.275  1.00 20.26  ? 354 ARG B O   1 
ATOM   4207 C  CB  . ARG B 1 354 ? 111.556 93.635  75.021  1.00 20.26  ? 354 ARG B CB  1 
ATOM   4208 N  N   . ASN B 1 355 ? 108.905 95.126  73.964  1.00 25.27  ? 355 ASN B N   1 
ATOM   4209 C  CA  . ASN B 1 355 ? 107.779 95.114  73.048  1.00 25.27  ? 355 ASN B CA  1 
ATOM   4210 C  C   . ASN B 1 355 ? 107.790 96.332  72.135  1.00 25.27  ? 355 ASN B C   1 
ATOM   4211 O  O   . ASN B 1 355 ? 107.524 96.210  70.935  1.00 25.27  ? 355 ASN B O   1 
ATOM   4212 C  CB  . ASN B 1 355 ? 106.486 95.023  73.831  1.00 25.27  ? 355 ASN B CB  1 
ATOM   4213 C  CG  . ASN B 1 355 ? 106.429 93.786  74.674  1.00 25.27  ? 355 ASN B CG  1 
ATOM   4214 O  OD1 . ASN B 1 355 ? 107.192 92.851  74.458  1.00 25.27  ? 355 ASN B OD1 1 
ATOM   4215 N  ND2 . ASN B 1 355 ? 105.532 93.767  75.647  1.00 25.27  ? 355 ASN B ND2 1 
ATOM   4216 N  N   . LEU B 1 356 ? 108.110 97.509  72.670  1.00 20.14  ? 356 LEU B N   1 
ATOM   4217 C  CA  . LEU B 1 356 ? 108.200 98.690  71.820  1.00 20.14  ? 356 LEU B CA  1 
ATOM   4218 C  C   . LEU B 1 356 ? 109.250 98.514  70.736  1.00 20.14  ? 356 LEU B C   1 
ATOM   4219 O  O   . LEU B 1 356 ? 109.037 98.916  69.592  1.00 20.14  ? 356 LEU B O   1 
ATOM   4220 C  CB  . LEU B 1 356 ? 108.528 99.921  72.647  1.00 20.14  ? 356 LEU B CB  1 
ATOM   4221 C  CG  . LEU B 1 356 ? 107.407 100.697 73.289  1.00 20.14  ? 356 LEU B CG  1 
ATOM   4222 C  CD1 . LEU B 1 356 ? 107.951 102.038 73.675  1.00 20.14  ? 356 LEU B CD1 1 
ATOM   4223 C  CD2 . LEU B 1 356 ? 106.287 100.831 72.326  1.00 20.14  ? 356 LEU B CD2 1 
ATOM   4224 N  N   . ILE B 1 357 ? 110.402 97.933  71.078  1.00 18.41  ? 357 ILE B N   1 
ATOM   4225 C  CA  . ILE B 1 357 ? 111.466 97.800  70.087  1.00 18.41  ? 357 ILE B CA  1 
ATOM   4226 C  C   . ILE B 1 357 ? 111.096 96.768  69.028  1.00 18.41  ? 357 ILE B C   1 
ATOM   4227 O  O   . ILE B 1 357 ? 111.317 96.981  67.829  1.00 18.41  ? 357 ILE B O   1 
ATOM   4228 C  CB  . ILE B 1 357 ? 112.792 97.450  70.763  1.00 18.41  ? 357 ILE B CB  1 
ATOM   4229 C  CG1 . ILE B 1 357 ? 113.399 98.684  71.383  1.00 18.41  ? 357 ILE B CG1 1 
ATOM   4230 C  CG2 . ILE B 1 357 ? 113.738 96.919  69.746  1.00 18.41  ? 357 ILE B CG2 1 
ATOM   4231 C  CD1 . ILE B 1 357 ? 113.992 99.570  70.393  1.00 18.41  ? 357 ILE B CD1 1 
ATOM   4232 N  N   . LYS B 1 358 ? 110.545 95.630  69.438  1.00 28.03  ? 358 LYS B N   1 
ATOM   4233 C  CA  . LYS B 1 358 ? 110.084 94.659  68.452  1.00 28.03  ? 358 LYS B CA  1 
ATOM   4234 C  C   . LYS B 1 358 ? 109.038 95.270  67.530  1.00 28.03  ? 358 LYS B C   1 
ATOM   4235 O  O   . LYS B 1 358 ? 109.050 95.032  66.315  1.00 28.03  ? 358 LYS B O   1 
ATOM   4236 C  CB  . LYS B 1 358 ? 109.537 93.430  69.166  1.00 28.03  ? 358 LYS B CB  1 
ATOM   4237 C  CG  . LYS B 1 358 ? 108.886 92.400  68.282  1.00 28.03  ? 358 LYS B CG  1 
ATOM   4238 C  CD  . LYS B 1 358 ? 108.580 91.149  69.092  1.00 28.03  ? 358 LYS B CD  1 
ATOM   4239 C  CE  . LYS B 1 358 ? 107.590 91.439  70.210  1.00 28.03  ? 358 LYS B CE  1 
ATOM   4240 N  NZ  . LYS B 1 358 ? 106.236 91.792  69.707  1.00 28.03  ? 358 LYS B NZ  1 
ATOM   4241 N  N   . GLU B 1 359 ? 108.148 96.090  68.075  1.00 28.69  ? 359 GLU B N   1 
ATOM   4242 C  CA  . GLU B 1 359 ? 107.115 96.690  67.249  1.00 28.69  ? 359 GLU B CA  1 
ATOM   4243 C  C   . GLU B 1 359 ? 107.627 97.823  66.365  1.00 28.69  ? 359 GLU B C   1 
ATOM   4244 O  O   . GLU B 1 359 ? 107.082 98.031  65.278  1.00 28.69  ? 359 GLU B O   1 
ATOM   4245 C  CB  . GLU B 1 359 ? 105.971 97.181  68.132  1.00 28.69  ? 359 GLU B CB  1 
ATOM   4246 C  CG  . GLU B 1 359 ? 105.176 96.056  68.769  1.00 28.69  ? 359 GLU B CG  1 
ATOM   4247 C  CD  . GLU B 1 359 ? 103.886 96.531  69.415  1.00 28.69  ? 359 GLU B CD  1 
ATOM   4248 O  OE1 . GLU B 1 359 ? 103.506 97.701  69.217  1.00 28.69  ? 359 GLU B OE1 1 
ATOM   4249 O  OE2 . GLU B 1 359 ? 103.245 95.730  70.122  1.00 28.69  ? 359 GLU B OE2 1 
ATOM   4250 N  N   . LEU B 1 360 ? 108.651 98.568  66.789  1.00 25.92  ? 360 LEU B N   1 
ATOM   4251 C  CA  . LEU B 1 360 ? 109.235 99.568  65.898  1.00 25.92  ? 360 LEU B CA  1 
ATOM   4252 C  C   . LEU B 1 360 ? 110.002 98.912  64.766  1.00 25.92  ? 360 LEU B C   1 
ATOM   4253 O  O   . LEU B 1 360 ? 110.013 99.419  63.644  1.00 25.92  ? 360 LEU B O   1 
ATOM   4254 C  CB  . LEU B 1 360 ? 110.169 100.510 66.645  1.00 25.92  ? 360 LEU B CB  1 
ATOM   4255 C  CG  . LEU B 1 360 ? 109.575 101.564 67.547  1.00 25.92  ? 360 LEU B CG  1 
ATOM   4256 C  CD1 . LEU B 1 360 ? 110.667 102.495 67.980  1.00 25.92  ? 360 LEU B CD1 1 
ATOM   4257 C  CD2 . LEU B 1 360 ? 108.547 102.285 66.788  1.00 25.92  ? 360 LEU B CD2 1 
ATOM   4258 N  N   . ARG B 1 361 ? 110.676 97.802  65.036  1.00 29.55  ? 361 ARG B N   1 
ATOM   4259 C  CA  . ARG B 1 361 ? 111.375 97.138  63.949  1.00 29.55  ? 361 ARG B CA  1 
ATOM   4260 C  C   . ARG B 1 361 ? 110.435 96.415  62.998  1.00 29.55  ? 361 ARG B C   1 
ATOM   4261 O  O   . ARG B 1 361 ? 110.780 96.248  61.826  1.00 29.55  ? 361 ARG B O   1 
ATOM   4262 C  CB  . ARG B 1 361 ? 112.387 96.154  64.510  1.00 29.55  ? 361 ARG B CB  1 
ATOM   4263 C  CG  . ARG B 1 361 ? 113.653 96.816  64.962  1.00 29.55  ? 361 ARG B CG  1 
ATOM   4264 C  CD  . ARG B 1 361 ? 114.448 95.932  65.875  1.00 29.55  ? 361 ARG B CD  1 
ATOM   4265 N  NE  . ARG B 1 361 ? 115.745 96.520  66.139  1.00 29.55  ? 361 ARG B NE  1 
ATOM   4266 C  CZ  . ARG B 1 361 ? 116.466 96.248  67.211  1.00 29.55  ? 361 ARG B CZ  1 
ATOM   4267 N  NH1 . ARG B 1 361 ? 116.002 95.395  68.104  1.00 29.55  ? 361 ARG B NH1 1 
ATOM   4268 N  NH2 . ARG B 1 361 ? 117.643 96.828  67.388  1.00 29.55  ? 361 ARG B NH2 1 
ATOM   4269 N  N   . ASN B 1 362 ? 109.267 95.973  63.467  1.00 32.98  ? 362 ASN B N   1 
ATOM   4270 C  CA  . ASN B 1 362 ? 108.305 95.352  62.563  1.00 32.98  ? 362 ASN B CA  1 
ATOM   4271 C  C   . ASN B 1 362 ? 107.776 96.314  61.511  1.00 32.98  ? 362 ASN B C   1 
ATOM   4272 O  O   . ASN B 1 362 ? 107.414 95.872  60.416  1.00 32.98  ? 362 ASN B O   1 
ATOM   4273 C  CB  . ASN B 1 362 ? 107.129 94.781  63.354  1.00 32.98  ? 362 ASN B CB  1 
ATOM   4274 C  CG  . ASN B 1 362 ? 107.317 93.331  63.688  1.00 32.98  ? 362 ASN B CG  1 
ATOM   4275 O  OD1 . ASN B 1 362 ? 107.704 92.542  62.834  1.00 32.98  ? 362 ASN B OD1 1 
ATOM   4276 N  ND2 . ASN B 1 362 ? 107.058 92.967  64.933  1.00 32.98  ? 362 ASN B ND2 1 
ATOM   4277 N  N   . VAL B 1 363 ? 107.726 97.611  61.820  1.00 31.95  ? 363 VAL B N   1 
ATOM   4278 C  CA  . VAL B 1 363 ? 107.148 98.599  60.921  1.00 31.95  ? 363 VAL B CA  1 
ATOM   4279 C  C   . VAL B 1 363 ? 107.937 98.641  59.625  1.00 31.95  ? 363 VAL B C   1 
ATOM   4280 O  O   . VAL B 1 363 ? 109.138 98.353  59.592  1.00 31.95  ? 363 VAL B O   1 
ATOM   4281 C  CB  . VAL B 1 363 ? 107.125 99.974  61.609  1.00 31.95  ? 363 VAL B CB  1 
ATOM   4282 C  CG1 . VAL B 1 363 ? 106.622 101.045 60.688  1.00 31.95  ? 363 VAL B CG1 1 
ATOM   4283 C  CG2 . VAL B 1 363 ? 106.262 99.908  62.827  1.00 31.95  ? 363 VAL B CG2 1 
ATOM   4284 N  N   . GLU B 1 364 ? 107.258 98.979  58.543  1.00 40.64  ? 364 GLU B N   1 
ATOM   4285 C  CA  . GLU B 1 364 ? 107.964 99.075  57.284  1.00 40.64  ? 364 GLU B CA  1 
ATOM   4286 C  C   . GLU B 1 364 ? 108.942 100.249 57.313  1.00 40.64  ? 364 GLU B C   1 
ATOM   4287 O  O   . GLU B 1 364 ? 108.999 101.031 58.262  1.00 40.64  ? 364 GLU B O   1 
ATOM   4288 C  CB  . GLU B 1 364 ? 106.976 99.223  56.135  1.00 40.64  ? 364 GLU B CB  1 
ATOM   4289 C  CG  . GLU B 1 364 ? 107.398 98.512  54.877  1.00 40.64  ? 364 GLU B CG  1 
ATOM   4290 C  CD  . GLU B 1 364 ? 106.378 98.631  53.770  1.00 40.64  ? 364 GLU B CD  1 
ATOM   4291 O  OE1 . GLU B 1 364 ? 105.484 99.495  53.873  1.00 40.64  ? 364 GLU B OE1 1 
ATOM   4292 O  OE2 . GLU B 1 364 ? 106.495 97.901  52.769  1.00 40.64  ? 364 GLU B OE2 1 
ATOM   4293 N  N   . GLY B 1 365 ? 109.765 100.327 56.274  1.00 44.70  ? 365 GLY B N   1 
ATOM   4294 C  CA  . GLY B 1 365 ? 110.611 101.475 56.040  1.00 44.70  ? 365 GLY B CA  1 
ATOM   4295 C  C   . GLY B 1 365 ? 111.751 101.691 57.009  1.00 44.70  ? 365 GLY B C   1 
ATOM   4296 O  O   . GLY B 1 365 ? 112.631 102.502 56.712  1.00 44.70  ? 365 GLY B O   1 
ATOM   4297 N  N   . VAL B 1 366 ? 111.787 101.002 58.146  1.00 43.79  ? 366 VAL B N   1 
ATOM   4298 C  CA  . VAL B 1 366 ? 112.848 101.217 59.122  1.00 43.79  ? 366 VAL B CA  1 
ATOM   4299 C  C   . VAL B 1 366 ? 113.643 99.929  59.265  1.00 43.79  ? 366 VAL B C   1 
ATOM   4300 O  O   . VAL B 1 366 ? 113.173 98.845  58.910  1.00 43.79  ? 366 VAL B O   1 
ATOM   4301 C  CB  . VAL B 1 366 ? 112.303 101.667 60.490  1.00 43.79  ? 366 VAL B CB  1 
ATOM   4302 C  CG1 . VAL B 1 366 ? 111.214 102.690 60.311  1.00 43.79  ? 366 VAL B CG1 1 
ATOM   4303 C  CG2 . VAL B 1 366 ? 111.830 100.494 61.272  1.00 43.79  ? 366 VAL B CG2 1 
ATOM   4304 N  N   . GLU B 1 367 ? 114.864 100.052 59.770  1.00 45.69  ? 367 GLU B N   1 
ATOM   4305 C  CA  . GLU B 1 367 ? 115.737 98.902  59.942  1.00 45.69  ? 367 GLU B CA  1 
ATOM   4306 C  C   . GLU B 1 367 ? 116.438 98.841  61.285  1.00 45.69  ? 367 GLU B C   1 
ATOM   4307 O  O   . GLU B 1 367 ? 116.824 97.743  61.698  1.00 45.69  ? 367 GLU B O   1 
ATOM   4308 C  CB  . GLU B 1 367 ? 116.796 98.873  58.836  1.00 45.69  ? 367 GLU B CB  1 
ATOM   4309 C  CG  . GLU B 1 367 ? 117.480 100.199 58.643  1.00 45.69  ? 367 GLU B CG  1 
ATOM   4310 C  CD  . GLU B 1 367 ? 117.984 100.388 57.233  1.00 45.69  ? 367 GLU B CD  1 
ATOM   4311 O  OE1 . GLU B 1 367 ? 119.199 100.605 57.059  1.00 45.69  ? 367 GLU B OE1 1 
ATOM   4312 O  OE2 . GLU B 1 367 ? 117.161 100.313 56.298  1.00 45.69  ? 367 GLU B OE2 1 
ATOM   4313 N  N   . GLU B 1 368 ? 116.618 99.960  61.973  1.00 33.96  ? 368 GLU B N   1 
ATOM   4314 C  CA  . GLU B 1 368 ? 117.335 100.001 63.232  1.00 33.96  ? 368 GLU B CA  1 
ATOM   4315 C  C   . GLU B 1 368 ? 116.743 101.087 64.106  1.00 33.96  ? 368 GLU B C   1 
ATOM   4316 O  O   . GLU B 1 368 ? 116.288 102.111 63.611  1.00 33.96  ? 368 GLU B O   1 
ATOM   4317 C  CB  . GLU B 1 368 ? 118.807 100.290 63.012  1.00 33.96  ? 368 GLU B CB  1 
ATOM   4318 C  CG  . GLU B 1 368 ? 119.605 100.218 64.269  1.00 33.96  ? 368 GLU B CG  1 
ATOM   4319 C  CD  . GLU B 1 368 ? 121.070 100.451 64.045  1.00 33.96  ? 368 GLU B CD  1 
ATOM   4320 O  OE1 . GLU B 1 368 ? 121.463 100.782 62.907  1.00 33.96  ? 368 GLU B OE1 1 
ATOM   4321 O  OE2 . GLU B 1 368 ? 121.831 100.276 65.013  1.00 33.96  ? 368 GLU B OE2 1 
ATOM   4322 N  N   . VAL B 1 369 ? 116.759 100.876 65.416  1.00 19.49  ? 369 VAL B N   1 
ATOM   4323 C  CA  . VAL B 1 369 ? 116.231 101.861 66.348  1.00 19.49  ? 369 VAL B CA  1 
ATOM   4324 C  C   . VAL B 1 369 ? 117.248 102.078 67.462  1.00 19.49  ? 369 VAL B C   1 
ATOM   4325 O  O   . VAL B 1 369 ? 117.315 101.284 68.403  1.00 19.49  ? 369 VAL B O   1 
ATOM   4326 C  CB  . VAL B 1 369 ? 114.885 101.432 66.923  1.00 19.49  ? 369 VAL B CB  1 
ATOM   4327 C  CG1 . VAL B 1 369 ? 114.323 102.526 67.722  1.00 19.49  ? 369 VAL B CG1 1 
ATOM   4328 C  CG2 . VAL B 1 369 ? 113.945 101.064 65.814  1.00 19.49  ? 369 VAL B CG2 1 
ATOM   4329 N  N   . HIS B 1 370 ? 117.894 103.230 67.326  1.00 21.79  ? 370 HIS B N   1 
ATOM   4330 C  CA  . HIS B 1 370 ? 118.958 103.755 68.215  1.00 21.79  ? 370 HIS B CA  1 
ATOM   4331 C  C   . HIS B 1 370 ? 118.320 104.307 69.488  1.00 21.79  ? 370 HIS B C   1 
ATOM   4332 O  O   . HIS B 1 370 ? 117.089 104.220 69.635  1.00 21.79  ? 370 HIS B O   1 
ATOM   4333 C  CB  . HIS B 1 370 ? 119.818 104.802 67.496  1.00 21.79  ? 370 HIS B CB  1 
ATOM   4334 C  CG  . HIS B 1 370 ? 120.361 104.340 66.187  1.00 21.79  ? 370 HIS B CG  1 
ATOM   4335 N  ND1 . HIS B 1 370 ? 120.430 105.169 65.086  1.00 21.79  ? 370 HIS B ND1 1 
ATOM   4336 C  CD2 . HIS B 1 370 ? 120.844 103.143 65.795  1.00 21.79  ? 370 HIS B CD2 1 
ATOM   4337 C  CE1 . HIS B 1 370 ? 120.942 104.503 64.070  1.00 21.79  ? 370 HIS B CE1 1 
ATOM   4338 N  NE2 . HIS B 1 370 ? 121.203 103.257 64.479  1.00 21.79  ? 370 HIS B NE2 1 
ATOM   4339 N  N   . GLU B 1 371 ? 119.151 104.828 70.362  1.00 15.46  ? 371 GLU B N   1 
ATOM   4340 C  CA  . GLU B 1 371 ? 118.747 105.262 71.689  1.00 15.46  ? 371 GLU B CA  1 
ATOM   4341 C  C   . GLU B 1 371 ? 117.246 105.379 71.790  1.00 15.46  ? 371 GLU B C   1 
ATOM   4342 O  O   . GLU B 1 371 ? 116.631 106.146 71.057  1.00 15.46  ? 371 GLU B O   1 
ATOM   4343 C  CB  . GLU B 1 371 ? 119.362 106.625 71.991  1.00 15.46  ? 371 GLU B CB  1 
ATOM   4344 C  CG  . GLU B 1 371 ? 120.856 106.663 72.090  1.00 15.46  ? 371 GLU B CG  1 
ATOM   4345 C  CD  . GLU B 1 371 ? 121.354 107.834 72.925  1.00 15.46  ? 371 GLU B CD  1 
ATOM   4346 O  OE1 . GLU B 1 371 ? 120.705 108.187 73.935  1.00 15.46  ? 371 GLU B OE1 1 
ATOM   4347 O  OE2 . GLU B 1 371 ? 122.399 108.408 72.566  1.00 15.46  ? 371 GLU B OE2 1 
ATOM   4348 N  N   . LEU B 1 372 ? 116.651 104.618 72.704  1.00 7.80   ? 372 LEU B N   1 
ATOM   4349 C  CA  . LEU B 1 372 ? 115.204 104.569 72.897  1.00 7.80   ? 372 LEU B CA  1 
ATOM   4350 C  C   . LEU B 1 372 ? 114.934 104.902 74.345  1.00 7.80   ? 372 LEU B C   1 
ATOM   4351 O  O   . LEU B 1 372 ? 114.855 103.991 75.157  1.00 7.80   ? 372 LEU B O   1 
ATOM   4352 C  CB  . LEU B 1 372 ? 114.644 103.221 72.579  1.00 7.80   ? 372 LEU B CB  1 
ATOM   4353 C  CG  . LEU B 1 372 ? 113.143 103.237 72.743  1.00 7.80   ? 372 LEU B CG  1 
ATOM   4354 C  CD1 . LEU B 1 372 ? 112.580 104.080 71.694  1.00 7.80   ? 372 LEU B CD1 1 
ATOM   4355 C  CD2 . LEU B 1 372 ? 112.610 101.896 72.606  1.00 7.80   ? 372 LEU B CD2 1 
ATOM   4356 N  N   . HIS B 1 373 ? 114.780 106.169 74.674  1.00 7.62   ? 373 HIS B N   1 
ATOM   4357 C  CA  . HIS B 1 373 ? 114.537 106.575 76.045  1.00 7.62   ? 373 HIS B CA  1 
ATOM   4358 C  C   . HIS B 1 373 ? 113.042 106.742 76.258  1.00 7.62   ? 373 HIS B C   1 
ATOM   4359 O  O   . HIS B 1 373 ? 112.372 107.372 75.444  1.00 7.62   ? 373 HIS B O   1 
ATOM   4360 C  CB  . HIS B 1 373 ? 115.288 107.860 76.353  1.00 7.62   ? 373 HIS B CB  1 
ATOM   4361 C  CG  . HIS B 1 373 ? 116.764 107.734 76.192  1.00 7.62   ? 373 HIS B CG  1 
ATOM   4362 N  ND1 . HIS B 1 373 ? 117.484 106.708 76.756  1.00 7.62   ? 373 HIS B ND1 1 
ATOM   4363 C  CD2 . HIS B 1 373 ? 117.658 108.494 75.521  1.00 7.62   ? 373 HIS B CD2 1 
ATOM   4364 C  CE1 . HIS B 1 373 ? 118.760 106.843 76.447  1.00 7.62   ? 373 HIS B CE1 1 
ATOM   4365 N  NE2 . HIS B 1 373 ? 118.893 107.920 75.697  1.00 7.62   ? 373 HIS B NE2 1 
ATOM   4366 N  N   . VAL B 1 374 ? 112.514 106.147 77.321  1.00 6.97   ? 374 VAL B N   1 
ATOM   4367 C  CA  . VAL B 1 374 ? 111.123 106.296 77.730  1.00 6.97   ? 374 VAL B CA  1 
ATOM   4368 C  C   . VAL B 1 374 ? 111.128 106.653 79.204  1.00 6.97   ? 374 VAL B C   1 
ATOM   4369 O  O   . VAL B 1 374 ? 111.961 106.144 79.950  1.00 6.97   ? 374 VAL B O   1 
ATOM   4370 C  CB  . VAL B 1 374 ? 110.321 105.009 77.482  1.00 6.97   ? 374 VAL B CB  1 
ATOM   4371 C  CG1 . VAL B 1 374 ? 108.952 105.153 77.991  1.00 6.97   ? 374 VAL B CG1 1 
ATOM   4372 C  CG2 . VAL B 1 374 ? 110.247 104.713 76.039  1.00 6.97   ? 374 VAL B CG2 1 
ATOM   4373 N  N   . TRP B 1 375 ? 110.233 107.536 79.632  1.00 12.18  ? 375 TRP B N   1 
ATOM   4374 C  CA  . TRP B 1 375 ? 110.197 107.832 81.054  1.00 12.18  ? 375 TRP B CA  1 
ATOM   4375 C  C   . TRP B 1 375 ? 108.846 108.380 81.464  1.00 12.18  ? 375 TRP B C   1 
ATOM   4376 O  O   . TRP B 1 375 ? 107.886 108.269 80.709  1.00 12.18  ? 375 TRP B O   1 
ATOM   4377 C  CB  . TRP B 1 375 ? 111.299 108.789 81.457  1.00 12.18  ? 375 TRP B CB  1 
ATOM   4378 C  CG  . TRP B 1 375 ? 111.545 109.880 80.562  1.00 12.18  ? 375 TRP B CG  1 
ATOM   4379 C  CD1 . TRP B 1 375 ? 112.112 109.816 79.346  1.00 12.18  ? 375 TRP B CD1 1 
ATOM   4380 C  CD2 . TRP B 1 375 ? 111.327 111.248 80.834  1.00 12.18  ? 375 TRP B CD2 1 
ATOM   4381 N  NE1 . TRP B 1 375 ? 112.228 111.065 78.816  1.00 12.18  ? 375 TRP B NE1 1 
ATOM   4382 C  CE2 . TRP B 1 375 ? 111.745 111.962 79.726  1.00 12.18  ? 375 TRP B CE2 1 
ATOM   4383 C  CE3 . TRP B 1 375 ? 110.803 111.939 81.908  1.00 12.18  ? 375 TRP B CE3 1 
ATOM   4384 C  CZ2 . TRP B 1 375 ? 111.643 113.320 79.658  1.00 12.18  ? 375 TRP B CZ2 1 
ATOM   4385 C  CZ3 . TRP B 1 375 ? 110.712 113.281 81.834  1.00 12.18  ? 375 TRP B CZ3 1 
ATOM   4386 C  CH2 . TRP B 1 375 ? 111.118 113.960 80.728  1.00 12.18  ? 375 TRP B CH2 1 
ATOM   4387 N  N   . GLN B 1 376 ? 108.754 108.896 82.686  1.00 12.20  ? 376 GLN B N   1 
ATOM   4388 C  CA  . GLN B 1 376 ? 107.478 109.368 83.208  1.00 12.20  ? 376 GLN B CA  1 
ATOM   4389 C  C   . GLN B 1 376 ? 107.625 110.765 83.763  1.00 12.20  ? 376 GLN B C   1 
ATOM   4390 O  O   . GLN B 1 376 ? 108.406 110.980 84.685  1.00 12.20  ? 376 GLN B O   1 
ATOM   4391 C  CB  . GLN B 1 376 ? 106.980 108.437 84.297  1.00 12.20  ? 376 GLN B CB  1 
ATOM   4392 C  CG  . GLN B 1 376 ? 105.576 108.723 84.749  1.00 12.20  ? 376 GLN B CG  1 
ATOM   4393 C  CD  . GLN B 1 376 ? 105.039 107.673 85.689  1.00 12.20  ? 376 GLN B CD  1 
ATOM   4394 O  OE1 . GLN B 1 376 ? 105.788 106.908 86.279  1.00 12.20  ? 376 GLN B OE1 1 
ATOM   4395 N  NE2 . GLN B 1 376 ? 103.735 107.627 85.828  1.00 12.20  ? 376 GLN B NE2 1 
ATOM   4396 N  N   . LEU B 1 377 ? 106.868 111.719 83.233  1.00 2.07   ? 377 LEU B N   1 
ATOM   4397 C  CA  . LEU B 1 377 ? 107.017 113.083 83.723  1.00 2.07   ? 377 LEU B CA  1 
ATOM   4398 C  C   . LEU B 1 377 ? 106.311 113.250 85.052  1.00 2.07   ? 377 LEU B C   1 
ATOM   4399 O  O   . LEU B 1 377 ? 106.941 113.560 86.065  1.00 2.07   ? 377 LEU B O   1 
ATOM   4400 C  CB  . LEU B 1 377 ? 106.507 114.092 82.708  1.00 2.07   ? 377 LEU B CB  1 
ATOM   4401 C  CG  . LEU B 1 377 ? 106.481 115.532 83.202  1.00 2.07   ? 377 LEU B CG  1 
ATOM   4402 C  CD1 . LEU B 1 377 ? 107.703 115.897 83.937  1.00 2.07   ? 377 LEU B CD1 1 
ATOM   4403 C  CD2 . LEU B 1 377 ? 106.432 116.416 82.034  1.00 2.07   ? 377 LEU B CD2 1 
ATOM   4404 N  N   . ALA B 1 378 ? 105.003 113.056 85.070  1.00 10.92  ? 378 ALA B N   1 
ATOM   4405 C  CA  . ALA B 1 378 ? 104.246 112.980 86.306  1.00 10.92  ? 378 ALA B CA  1 
ATOM   4406 C  C   . ALA B 1 378 ? 102.930 112.331 85.977  1.00 10.92  ? 378 ALA B C   1 
ATOM   4407 O  O   . ALA B 1 378 ? 102.426 112.472 84.860  1.00 10.92  ? 378 ALA B O   1 
ATOM   4408 C  CB  . ALA B 1 378 ? 104.005 114.352 86.927  1.00 10.92  ? 378 ALA B CB  1 
ATOM   4409 N  N   . GLY B 1 379 ? 102.393 111.606 86.936  1.00 9.45   ? 379 GLY B N   1 
ATOM   4410 C  CA  . GLY B 1 379 ? 101.124 110.975 86.696  1.00 9.45   ? 379 GLY B CA  1 
ATOM   4411 C  C   . GLY B 1 379 ? 101.171 110.174 85.420  1.00 9.45   ? 379 GLY B C   1 
ATOM   4412 O  O   . GLY B 1 379 ? 101.839 109.143 85.347  1.00 9.45   ? 379 GLY B O   1 
ATOM   4413 N  N   . SER B 1 380 ? 100.501 110.660 84.393  1.00 6.35   ? 380 SER B N   1 
ATOM   4414 C  CA  . SER B 1 380 ? 100.415 109.887 83.173  1.00 6.35   ? 380 SER B CA  1 
ATOM   4415 C  C   . SER B 1 380 ? 100.765 110.710 81.950  1.00 6.35   ? 380 SER B C   1 
ATOM   4416 O  O   . SER B 1 380 ? 100.179 110.506 80.892  1.00 6.35   ? 380 SER B O   1 
ATOM   4417 C  CB  . SER B 1 380 ? 99.028  109.283 83.013  1.00 6.35   ? 380 SER B CB  1 
ATOM   4418 O  OG  . SER B 1 380 ? 98.816  108.901 81.671  1.00 6.35   ? 380 SER B OG  1 
ATOM   4419 N  N   . ARG B 1 381 ? 101.766 111.576 82.057  1.00 9.62   ? 381 ARG B N   1 
ATOM   4420 C  CA  . ARG B 1 381 ? 102.287 112.329 80.881  1.00 9.62   ? 381 ARG B CA  1 
ATOM   4421 C  C   . ARG B 1 381 ? 103.627 111.675 80.532  1.00 9.62   ? 381 ARG B C   1 
ATOM   4422 O  O   . ARG B 1 381 ? 104.659 112.199 80.980  1.00 9.62   ? 381 ARG B O   1 
ATOM   4423 C  CB  . ARG B 1 381 ? 102.496 113.806 81.225  1.00 9.62   ? 381 ARG B CB  1 
ATOM   4424 C  CG  . ARG B 1 381 ? 101.310 114.464 81.912  1.00 9.62   ? 381 ARG B CG  1 
ATOM   4425 C  CD  . ARG B 1 381 ? 101.714 115.697 82.695  1.00 9.62   ? 381 ARG B CD  1 
ATOM   4426 N  NE  . ARG B 1 381 ? 101.240 116.917 82.068  1.00 9.62   ? 381 ARG B NE  1 
ATOM   4427 C  CZ  . ARG B 1 381 ? 100.019 117.075 81.579  1.00 9.62   ? 381 ARG B CZ  1 
ATOM   4428 N  NH1 . ARG B 1 381 ? 99.682  118.210 80.991  1.00 9.62   ? 381 ARG B NH1 1 
ATOM   4429 N  NH2 . ARG B 1 381 ? 99.138  116.101 81.681  1.00 9.62   ? 381 ARG B NH2 1 
ATOM   4430 N  N   . ILE B 1 382 ? 103.617 110.596 79.756  1.00 6.71   ? 382 ILE B N   1 
ATOM   4431 C  CA  . ILE B 1 382 ? 104.815 109.810 79.490  1.00 6.71   ? 382 ILE B CA  1 
ATOM   4432 C  C   . ILE B 1 382 ? 105.438 110.274 78.187  1.00 6.71   ? 382 ILE B C   1 
ATOM   4433 O  O   . ILE B 1 382 ? 104.734 110.473 77.199  1.00 6.71   ? 382 ILE B O   1 
ATOM   4434 C  CB  . ILE B 1 382 ? 104.469 108.318 79.424  1.00 6.71   ? 382 ILE B CB  1 
ATOM   4435 C  CG1 . ILE B 1 382 ? 104.116 107.797 80.799  1.00 6.71   ? 382 ILE B CG1 1 
ATOM   4436 C  CG2 . ILE B 1 382 ? 105.587 107.551 78.863  1.00 6.71   ? 382 ILE B CG2 1 
ATOM   4437 C  CD1 . ILE B 1 382 ? 103.492 106.453 80.777  1.00 6.71   ? 382 ILE B CD1 1 
ATOM   4438 N  N   . ILE B 1 383 ? 106.751 110.443 78.176  1.00 4.76   ? 383 ILE B N   1 
ATOM   4439 C  CA  . ILE B 1 383 ? 107.478 110.957 77.026  1.00 4.76   ? 383 ILE B CA  1 
ATOM   4440 C  C   . ILE B 1 383 ? 108.203 109.802 76.365  1.00 4.76   ? 383 ILE B C   1 
ATOM   4441 O  O   . ILE B 1 383 ? 108.159 108.687 76.881  1.00 4.76   ? 383 ILE B O   1 
ATOM   4442 C  CB  . ILE B 1 383 ? 108.439 112.059 77.472  1.00 4.76   ? 383 ILE B CB  1 
ATOM   4443 C  CG1 . ILE B 1 383 ? 107.676 112.987 78.381  1.00 4.76   ? 383 ILE B CG1 1 
ATOM   4444 C  CG2 . ILE B 1 383 ? 108.943 112.834 76.323  1.00 4.76   ? 383 ILE B CG2 1 
ATOM   4445 C  CD1 . ILE B 1 383 ? 108.344 114.272 78.599  1.00 4.76   ? 383 ILE B CD1 1 
ATOM   4446 N  N   . ALA B 1 384 ? 108.792 110.029 75.195  1.00 4.19   ? 384 ALA B N   1 
ATOM   4447 C  CA  . ALA B 1 384 ? 109.573 108.998 74.518  1.00 4.19   ? 384 ALA B CA  1 
ATOM   4448 C  C   . ALA B 1 384 ? 110.396 109.581 73.390  1.00 4.19   ? 384 ALA B C   1 
ATOM   4449 O  O   . ALA B 1 384 ? 109.857 110.247 72.509  1.00 4.19   ? 384 ALA B O   1 
ATOM   4450 C  CB  . ALA B 1 384 ? 108.690 107.911 73.947  1.00 4.19   ? 384 ALA B CB  1 
ATOM   4451 N  N   . THR B 1 385 ? 111.677 109.289 73.391  1.00 6.56   ? 385 THR B N   1 
ATOM   4452 C  CA  . THR B 1 385 ? 112.595 109.691 72.345  1.00 6.56   ? 385 THR B CA  1 
ATOM   4453 C  C   . THR B 1 385 ? 112.884 108.463 71.503  1.00 6.56   ? 385 THR B C   1 
ATOM   4454 O  O   . THR B 1 385 ? 112.554 107.355 71.900  1.00 6.56   ? 385 THR B O   1 
ATOM   4455 C  CB  . THR B 1 385 ? 113.879 110.254 72.955  1.00 6.56   ? 385 THR B CB  1 
ATOM   4456 O  OG1 . THR B 1 385 ? 113.568 111.405 73.748  1.00 6.56   ? 385 THR B OG1 1 
ATOM   4457 C  CG2 . THR B 1 385 ? 114.882 110.647 71.911  1.00 6.56   ? 385 THR B CG2 1 
ATOM   4458 N  N   . ALA B 1 386 ? 113.423 108.656 70.308  1.00 9.08   ? 386 ALA B N   1 
ATOM   4459 C  CA  . ALA B 1 386 ? 114.028 107.553 69.581  1.00 9.08   ? 386 ALA B CA  1 
ATOM   4460 C  C   . ALA B 1 386 ? 114.695 108.102 68.349  1.00 9.08   ? 386 ALA B C   1 
ATOM   4461 O  O   . ALA B 1 386 ? 114.074 108.848 67.600  1.00 9.08   ? 386 ALA B O   1 
ATOM   4462 C  CB  . ALA B 1 386 ? 113.001 106.508 69.162  1.00 9.08   ? 386 ALA B CB  1 
ATOM   4463 N  N   . HIS B 1 387 ? 115.944 107.742 68.129  1.00 16.99  ? 387 HIS B N   1 
ATOM   4464 C  CA  . HIS B 1 387 ? 116.405 107.862 66.769  1.00 16.99  ? 387 HIS B CA  1 
ATOM   4465 C  C   . HIS B 1 387 ? 115.785 106.733 65.970  1.00 16.99  ? 387 HIS B C   1 
ATOM   4466 O  O   . HIS B 1 387 ? 115.113 105.861 66.508  1.00 16.99  ? 387 HIS B O   1 
ATOM   4467 C  CB  . HIS B 1 387 ? 117.917 107.807 66.688  1.00 16.99  ? 387 HIS B CB  1 
ATOM   4468 C  CG  . HIS B 1 387 ? 118.606 108.878 67.467  1.00 16.99  ? 387 HIS B CG  1 
ATOM   4469 N  ND1 . HIS B 1 387 ? 119.896 109.272 67.194  1.00 16.99  ? 387 HIS B ND1 1 
ATOM   4470 C  CD2 . HIS B 1 387 ? 118.200 109.618 68.521  1.00 16.99  ? 387 HIS B CD2 1 
ATOM   4471 C  CE1 . HIS B 1 387 ? 120.249 110.220 68.040  1.00 16.99  ? 387 HIS B CE1 1 
ATOM   4472 N  NE2 . HIS B 1 387 ? 119.240 110.445 68.858  1.00 16.99  ? 387 HIS B NE2 1 
ATOM   4473 N  N   . ILE B 1 388 ? 115.978 106.767 64.660  1.00 19.43  ? 388 ILE B N   1 
ATOM   4474 C  CA  . ILE B 1 388 ? 115.417 105.737 63.810  1.00 19.43  ? 388 ILE B CA  1 
ATOM   4475 C  C   . ILE B 1 388 ? 116.227 105.793 62.538  1.00 19.43  ? 388 ILE B C   1 
ATOM   4476 O  O   . ILE B 1 388 ? 116.974 106.743 62.320  1.00 19.43  ? 388 ILE B O   1 
ATOM   4477 C  CB  . ILE B 1 388 ? 113.914 105.984 63.568  1.00 19.43  ? 388 ILE B CB  1 
ATOM   4478 C  CG1 . ILE B 1 388 ? 113.196 104.722 63.194  1.00 19.43  ? 388 ILE B CG1 1 
ATOM   4479 C  CG2 . ILE B 1 388 ? 113.727 106.857 62.410  1.00 19.43  ? 388 ILE B CG2 1 
ATOM   4480 C  CD1 . ILE B 1 388 ? 111.726 104.922 63.215  1.00 19.43  ? 388 ILE B CD1 1 
ATOM   4481 N  N   . LYS B 1 389 ? 116.117 104.767 61.707  1.00 39.46  ? 389 LYS B N   1 
ATOM   4482 C  CA  . LYS B 1 389 ? 116.910 104.729 60.480  1.00 39.46  ? 389 LYS B CA  1 
ATOM   4483 C  C   . LYS B 1 389 ? 116.022 104.379 59.291  1.00 39.46  ? 389 LYS B C   1 
ATOM   4484 O  O   . LYS B 1 389 ? 115.845 103.206 58.965  1.00 39.46  ? 389 LYS B O   1 
ATOM   4485 C  CB  . LYS B 1 389 ? 118.051 103.762 60.611  1.00 39.46  ? 389 LYS B CB  1 
ATOM   4486 C  CG  . LYS B 1 389 ? 119.177 104.075 59.668  1.00 39.46  ? 389 LYS B CG  1 
ATOM   4487 C  CD  . LYS B 1 389 ? 120.453 103.378 60.072  1.00 39.46  ? 389 LYS B CD  1 
ATOM   4488 C  CE  . LYS B 1 389 ? 121.048 104.004 61.306  1.00 39.46  ? 389 LYS B CE  1 
ATOM   4489 N  NZ  . LYS B 1 389 ? 122.408 103.483 61.592  1.00 39.46  ? 389 LYS B NZ  1 
ATOM   4490 N  N   . CYS B 1 390 ? 115.480 105.400 58.636  1.00 51.57  ? 390 CYS B N   1 
ATOM   4491 C  CA  . CYS B 1 390 ? 114.728 105.199 57.412  1.00 51.57  ? 390 CYS B CA  1 
ATOM   4492 C  C   . CYS B 1 390 ? 115.672 104.891 56.256  1.00 51.57  ? 390 CYS B C   1 
ATOM   4493 O  O   . CYS B 1 390 ? 116.892 105.043 56.355  1.00 51.57  ? 390 CYS B O   1 
ATOM   4494 C  CB  . CYS B 1 390 ? 113.890 106.431 57.084  1.00 51.57  ? 390 CYS B CB  1 
ATOM   4495 S  SG  . CYS B 1 390 ? 113.047 107.160 58.486  1.00 51.57  ? 390 CYS B SG  1 
ATOM   4496 N  N   . GLU B 1 391 ? 115.092 104.471 55.132  1.00 66.72  ? 391 GLU B N   1 
ATOM   4497 C  CA  . GLU B 1 391 ? 115.862 104.106 53.951  1.00 66.72  ? 391 GLU B CA  1 
ATOM   4498 C  C   . GLU B 1 391 ? 115.742 105.115 52.820  1.00 66.72  ? 391 GLU B C   1 
ATOM   4499 O  O   . GLU B 1 391 ? 116.761 105.567 52.291  1.00 66.72  ? 391 GLU B O   1 
ATOM   4500 C  CB  . GLU B 1 391 ? 115.430 102.725 53.446  1.00 66.72  ? 391 GLU B CB  1 
ATOM   4501 C  CG  . GLU B 1 391 ? 116.205 102.249 52.226  1.00 66.72  ? 391 GLU B CG  1 
ATOM   4502 C  CD  . GLU B 1 391 ? 117.575 101.696 52.570  1.00 66.72  ? 391 GLU B CD  1 
ATOM   4503 O  OE1 . GLU B 1 391 ? 117.853 101.492 53.769  1.00 66.72  ? 391 GLU B OE1 1 
ATOM   4504 O  OE2 . GLU B 1 391 ? 118.375 101.462 51.639  1.00 66.72  ? 391 GLU B OE2 1 
ATOM   4505 N  N   . ASP B 1 392 ? 114.520 105.483 52.433  1.00 73.86  ? 392 ASP B N   1 
ATOM   4506 C  CA  . ASP B 1 392 ? 114.279 106.376 51.301  1.00 73.86  ? 392 ASP B CA  1 
ATOM   4507 C  C   . ASP B 1 392 ? 113.804 107.737 51.791  1.00 73.86  ? 392 ASP B C   1 
ATOM   4508 O  O   . ASP B 1 392 ? 112.673 107.846 52.293  1.00 73.86  ? 392 ASP B O   1 
ATOM   4509 C  CB  . ASP B 1 392 ? 113.251 105.769 50.345  1.00 73.86  ? 392 ASP B CB  1 
ATOM   4510 C  CG  . ASP B 1 392 ? 113.185 106.503 49.024  1.00 73.86  ? 392 ASP B CG  1 
ATOM   4511 O  OD1 . ASP B 1 392 ? 112.229 107.279 48.820  1.00 73.86  ? 392 ASP B OD1 1 
ATOM   4512 O  OD2 . ASP B 1 392 ? 114.089 106.308 48.188  1.00 73.86  ? 392 ASP B OD2 1 
ATOM   4513 N  N   . PRO B 1 393 ? 114.582 108.800 51.635  1.00 75.49  ? 393 PRO B N   1 
ATOM   4514 C  CA  . PRO B 1 393 ? 114.273 110.082 52.276  1.00 75.49  ? 393 PRO B CA  1 
ATOM   4515 C  C   . PRO B 1 393 ? 113.252 110.927 51.522  1.00 75.49  ? 393 PRO B C   1 
ATOM   4516 O  O   . PRO B 1 393 ? 113.377 112.146 51.432  1.00 75.49  ? 393 PRO B O   1 
ATOM   4517 C  CB  . PRO B 1 393 ? 115.637 110.773 52.312  1.00 75.49  ? 393 PRO B CB  1 
ATOM   4518 C  CG  . PRO B 1 393 ? 116.306 110.278 51.084  1.00 75.49  ? 393 PRO B CG  1 
ATOM   4519 C  CD  . PRO B 1 393 ? 115.845 108.857 50.881  1.00 75.49  ? 393 PRO B CD  1 
ATOM   4520 N  N   . THR B 1 394 ? 112.228 110.282 51.015  1.00 75.32  ? 394 THR B N   1 
ATOM   4521 C  CA  . THR B 1 394 ? 111.130 110.978 50.358  1.00 75.32  ? 394 THR B CA  1 
ATOM   4522 C  C   . THR B 1 394 ? 109.778 110.499 50.857  1.00 75.32  ? 394 THR B C   1 
ATOM   4523 O  O   . THR B 1 394 ? 108.819 111.273 50.871  1.00 75.32  ? 394 THR B O   1 
ATOM   4524 C  CB  . THR B 1 394 ? 111.231 110.805 48.837  1.00 75.32  ? 394 THR B CB  1 
ATOM   4525 O  OG1 . THR B 1 394 ? 112.477 111.341 48.381  1.00 75.32  ? 394 THR B OG1 1 
ATOM   4526 C  CG2 . THR B 1 394 ? 110.111 111.538 48.135  1.00 75.32  ? 394 THR B CG2 1 
ATOM   4527 N  N   . SER B 1 395 ? 109.684 109.247 51.286  1.00 63.61  ? 395 SER B N   1 
ATOM   4528 C  CA  . SER B 1 395 ? 108.482 108.713 51.913  1.00 63.61  ? 395 SER B CA  1 
ATOM   4529 C  C   . SER B 1 395 ? 108.595 108.749 53.425  1.00 63.61  ? 395 SER B C   1 
ATOM   4530 O  O   . SER B 1 395 ? 108.140 107.834 54.109  1.00 63.61  ? 395 SER B O   1 
ATOM   4531 C  CB  . SER B 1 395 ? 108.227 107.292 51.433  1.00 63.61  ? 395 SER B CB  1 
ATOM   4532 O  OG  . SER B 1 395 ? 108.957 106.375 52.227  1.00 63.61  ? 395 SER B OG  1 
ATOM   4533 N  N   . TYR B 1 396 ? 109.218 109.788 53.971  1.00 45.26  ? 396 TYR B N   1 
ATOM   4534 C  CA  . TYR B 1 396 ? 109.502 109.792 55.397  1.00 45.26  ? 396 TYR B CA  1 
ATOM   4535 C  C   . TYR B 1 396 ? 108.251 110.064 56.223  1.00 45.26  ? 396 TYR B C   1 
ATOM   4536 O  O   . TYR B 1 396 ? 108.061 109.446 57.275  1.00 45.26  ? 396 TYR B O   1 
ATOM   4537 C  CB  . TYR B 1 396 ? 110.605 110.802 55.699  1.00 45.26  ? 396 TYR B CB  1 
ATOM   4538 C  CG  . TYR B 1 396 ? 110.617 111.329 57.106  1.00 45.26  ? 396 TYR B CG  1 
ATOM   4539 C  CD1 . TYR B 1 396 ? 110.730 110.482 58.183  1.00 45.26  ? 396 TYR B CD1 1 
ATOM   4540 C  CD2 . TYR B 1 396 ? 110.554 112.680 57.349  1.00 45.26  ? 396 TYR B CD2 1 
ATOM   4541 C  CE1 . TYR B 1 396 ? 110.735 110.966 59.457  1.00 45.26  ? 396 TYR B CE1 1 
ATOM   4542 C  CE2 . TYR B 1 396 ? 110.571 113.170 58.612  1.00 45.26  ? 396 TYR B CE2 1 
ATOM   4543 C  CZ  . TYR B 1 396 ? 110.663 112.312 59.663  1.00 45.26  ? 396 TYR B CZ  1 
ATOM   4544 O  OH  . TYR B 1 396 ? 110.678 112.813 60.933  1.00 45.26  ? 396 TYR B OH  1 
ATOM   4545 N  N   . MET B 1 397 ? 107.374 110.963 55.768  1.00 48.30  ? 397 MET B N   1 
ATOM   4546 C  CA  . MET B 1 397 ? 106.266 111.376 56.625  1.00 48.30  ? 397 MET B CA  1 
ATOM   4547 C  C   . MET B 1 397 ? 105.297 110.235 56.904  1.00 48.30  ? 397 MET B C   1 
ATOM   4548 O  O   . MET B 1 397 ? 104.754 110.144 58.011  1.00 48.30  ? 397 MET B O   1 
ATOM   4549 C  CB  . MET B 1 397 ? 105.520 112.560 56.020  1.00 48.30  ? 397 MET B CB  1 
ATOM   4550 C  CG  . MET B 1 397 ? 106.231 113.899 56.189  1.00 48.30  ? 397 MET B CG  1 
ATOM   4551 S  SD  . MET B 1 397 ? 106.681 114.350 57.877  1.00 48.30  ? 397 MET B SD  1 
ATOM   4552 C  CE  . MET B 1 397 ? 105.122 114.165 58.708  1.00 48.30  ? 397 MET B CE  1 
ATOM   4553 N  N   . GLU B 1 398 ? 105.068 109.352 55.933  1.00 48.89  ? 398 GLU B N   1 
ATOM   4554 C  CA  . GLU B 1 398 ? 104.229 108.190 56.205  1.00 48.89  ? 398 GLU B CA  1 
ATOM   4555 C  C   . GLU B 1 398 ? 104.852 107.305 57.274  1.00 48.89  ? 398 GLU B C   1 
ATOM   4556 O  O   . GLU B 1 398 ? 104.156 106.817 58.175  1.00 48.89  ? 398 GLU B O   1 
ATOM   4557 C  CB  . GLU B 1 398 ? 103.996 107.385 54.932  1.00 48.89  ? 398 GLU B CB  1 
ATOM   4558 C  CG  . GLU B 1 398 ? 103.520 108.199 53.768  1.00 48.89  ? 398 GLU B CG  1 
ATOM   4559 C  CD  . GLU B 1 398 ? 103.790 107.508 52.461  1.00 48.89  ? 398 GLU B CD  1 
ATOM   4560 O  OE1 . GLU B 1 398 ? 104.270 106.357 52.494  1.00 48.89  ? 398 GLU B OE1 1 
ATOM   4561 O  OE2 . GLU B 1 398 ? 103.524 108.113 51.404  1.00 48.89  ? 398 GLU B OE2 1 
ATOM   4562 N  N   . VAL B 1 399 ? 106.160 107.076 57.186  1.00 45.38  ? 399 VAL B N   1 
ATOM   4563 C  CA  . VAL B 1 399 ? 106.832 106.278 58.201  1.00 45.38  ? 399 VAL B CA  1 
ATOM   4564 C  C   . VAL B 1 399 ? 106.686 106.927 59.565  1.00 45.38  ? 399 VAL B C   1 
ATOM   4565 O  O   . VAL B 1 399 ? 106.417 106.247 60.559  1.00 45.38  ? 399 VAL B O   1 
ATOM   4566 C  CB  . VAL B 1 399 ? 108.305 106.066 57.826  1.00 45.38  ? 399 VAL B CB  1 
ATOM   4567 C  CG1 . VAL B 1 399 ? 109.112 105.780 59.052  1.00 45.38  ? 399 VAL B CG1 1 
ATOM   4568 C  CG2 . VAL B 1 399 ? 108.417 104.915 56.871  1.00 45.38  ? 399 VAL B CG2 1 
ATOM   4569 N  N   . ALA B 1 400 ? 106.837 108.248 59.639  1.00 43.28  ? 400 ALA B N   1 
ATOM   4570 C  CA  . ALA B 1 400 ? 106.754 108.904 60.940  1.00 43.28  ? 400 ALA B CA  1 
ATOM   4571 C  C   . ALA B 1 400 ? 105.339 108.852 61.499  1.00 43.28  ? 400 ALA B C   1 
ATOM   4572 O  O   . ALA B 1 400 ? 105.151 108.723 62.714  1.00 43.28  ? 400 ALA B O   1 
ATOM   4573 C  CB  . ALA B 1 400 ? 107.250 110.340 60.848  1.00 43.28  ? 400 ALA B CB  1 
ATOM   4574 N  N   . LYS B 1 401 ? 104.328 108.925 60.634  1.00 39.50  ? 401 LYS B N   1 
ATOM   4575 C  CA  . LYS B 1 401 ? 102.956 108.759 61.108  1.00 39.50  ? 401 LYS B CA  1 
ATOM   4576 C  C   . LYS B 1 401 ? 102.727 107.351 61.647  1.00 39.50  ? 401 LYS B C   1 
ATOM   4577 O  O   . LYS B 1 401 ? 102.109 107.168 62.704  1.00 39.50  ? 401 LYS B O   1 
ATOM   4578 C  CB  . LYS B 1 401 ? 101.968 109.066 59.989  1.00 39.50  ? 401 LYS B CB  1 
ATOM   4579 C  CG  . LYS B 1 401 ? 101.469 110.490 59.967  1.00 39.50  ? 401 LYS B CG  1 
ATOM   4580 C  CD  . LYS B 1 401 ? 100.548 110.702 58.783  1.00 39.50  ? 401 LYS B CD  1 
ATOM   4581 C  CE  . LYS B 1 401 ? 100.607 112.129 58.272  1.00 39.50  ? 401 LYS B CE  1 
ATOM   4582 N  NZ  . LYS B 1 401 ? 100.579 113.115 59.378  1.00 39.50  ? 401 LYS B NZ  1 
ATOM   4583 N  N   . THR B 1 402 ? 103.218 106.337 60.932  1.00 37.81  ? 402 THR B N   1 
ATOM   4584 C  CA  . THR B 1 402 ? 103.059 104.968 61.411  1.00 37.81  ? 402 THR B CA  1 
ATOM   4585 C  C   . THR B 1 402 ? 103.753 104.770 62.749  1.00 37.81  ? 402 THR B C   1 
ATOM   4586 O  O   . THR B 1 402 ? 103.213 104.114 63.649  1.00 37.81  ? 402 THR B O   1 
ATOM   4587 C  CB  . THR B 1 402 ? 103.603 103.982 60.388  1.00 37.81  ? 402 THR B CB  1 
ATOM   4588 O  OG1 . THR B 1 402 ? 102.963 104.199 59.129  1.00 37.81  ? 402 THR B OG1 1 
ATOM   4589 C  CG2 . THR B 1 402 ? 103.314 102.586 60.827  1.00 37.81  ? 402 THR B CG2 1 
ATOM   4590 N  N   . ILE B 1 403 ? 104.945 105.342 62.907  1.00 33.39  ? 403 ILE B N   1 
ATOM   4591 C  CA  . ILE B 1 403 ? 105.668 105.199 64.163  1.00 33.39  ? 403 ILE B CA  1 
ATOM   4592 C  C   . ILE B 1 403 ? 104.933 105.913 65.282  1.00 33.39  ? 403 ILE B C   1 
ATOM   4593 O  O   . ILE B 1 403 ? 104.855 105.407 66.406  1.00 33.39  ? 403 ILE B O   1 
ATOM   4594 C  CB  . ILE B 1 403 ? 107.104 105.712 64.018  1.00 33.39  ? 403 ILE B CB  1 
ATOM   4595 C  CG1 . ILE B 1 403 ? 107.854 104.870 63.011  1.00 33.39  ? 403 ILE B CG1 1 
ATOM   4596 C  CG2 . ILE B 1 403 ? 107.808 105.605 65.309  1.00 33.39  ? 403 ILE B CG2 1 
ATOM   4597 C  CD1 . ILE B 1 403 ? 107.674 103.428 63.230  1.00 33.39  ? 403 ILE B CD1 1 
ATOM   4598 N  N   . LYS B 1 404 ? 104.374 107.090 65.007  1.00 31.52  ? 404 LYS B N   1 
ATOM   4599 C  CA  . LYS B 1 404 ? 103.597 107.761 66.043  1.00 31.52  ? 404 LYS B CA  1 
ATOM   4600 C  C   . LYS B 1 404 ? 102.377 106.945 66.433  1.00 31.52  ? 404 LYS B C   1 
ATOM   4601 O  O   . LYS B 1 404 ? 101.957 106.960 67.591  1.00 31.52  ? 404 LYS B O   1 
ATOM   4602 C  CB  . LYS B 1 404 ? 103.168 109.140 65.587  1.00 31.52  ? 404 LYS B CB  1 
ATOM   4603 C  CG  . LYS B 1 404 ? 102.418 109.876 66.652  1.00 31.52  ? 404 LYS B CG  1 
ATOM   4604 C  CD  . LYS B 1 404 ? 103.357 110.336 67.714  1.00 31.52  ? 404 LYS B CD  1 
ATOM   4605 C  CE  . LYS B 1 404 ? 102.690 111.372 68.560  1.00 31.52  ? 404 LYS B CE  1 
ATOM   4606 N  NZ  . LYS B 1 404 ? 103.634 112.474 68.844  1.00 31.52  ? 404 LYS B NZ  1 
ATOM   4607 N  N   . ASP B 1 405 ? 101.799 106.211 65.484  1.00 32.87  ? 405 ASP B N   1 
ATOM   4608 C  CA  . ASP B 1 405 ? 100.687 105.334 65.841  1.00 32.87  ? 405 ASP B CA  1 
ATOM   4609 C  C   . ASP B 1 405 ? 101.141 104.189 66.742  1.00 32.87  ? 405 ASP B C   1 
ATOM   4610 O  O   . ASP B 1 405 ? 100.449 103.835 67.707  1.00 32.87  ? 405 ASP B O   1 
ATOM   4611 C  CB  . ASP B 1 405 ? 100.025 104.786 64.582  1.00 32.87  ? 405 ASP B CB  1 
ATOM   4612 C  CG  . ASP B 1 405 ? 98.899  105.662 64.092  1.00 32.87  ? 405 ASP B CG  1 
ATOM   4613 O  OD1 . ASP B 1 405 ? 98.162  105.231 63.181  1.00 32.87  ? 405 ASP B OD1 1 
ATOM   4614 O  OD2 . ASP B 1 405 ? 98.754  106.788 64.609  1.00 32.87  ? 405 ASP B OD2 1 
ATOM   4615 N  N   . VAL B 1 406 ? 102.292 103.584 66.439  1.00 27.81  ? 406 VAL B N   1 
ATOM   4616 C  CA  . VAL B 1 406 ? 102.734 102.442 67.237  1.00 27.81  ? 406 VAL B CA  1 
ATOM   4617 C  C   . VAL B 1 406 ? 103.336 102.900 68.555  1.00 27.81  ? 406 VAL B C   1 
ATOM   4618 O  O   . VAL B 1 406 ? 103.700 102.074 69.395  1.00 27.81  ? 406 VAL B O   1 
ATOM   4619 C  CB  . VAL B 1 406 ? 103.732 101.575 66.470  1.00 27.81  ? 406 VAL B CB  1 
ATOM   4620 C  CG1 . VAL B 1 406 ? 105.048 102.253 66.449  1.00 27.81  ? 406 VAL B CG1 1 
ATOM   4621 C  CG2 . VAL B 1 406 ? 103.850 100.233 67.113  1.00 27.81  ? 406 VAL B CG2 1 
ATOM   4622 N  N   . PHE B 1 407 ? 103.522 104.205 68.741  1.00 26.07  ? 407 PHE B N   1 
ATOM   4623 C  CA  . PHE B 1 407 ? 103.691 104.705 70.104  1.00 26.07  ? 407 PHE B CA  1 
ATOM   4624 C  C   . PHE B 1 407 ? 102.362 105.015 70.764  1.00 26.07  ? 407 PHE B C   1 
ATOM   4625 O  O   . PHE B 1 407 ? 102.215 104.819 71.971  1.00 26.07  ? 407 PHE B O   1 
ATOM   4626 C  CB  . PHE B 1 407 ? 104.555 105.954 70.156  1.00 26.07  ? 407 PHE B CB  1 
ATOM   4627 C  CG  . PHE B 1 407 ? 106.001 105.675 70.185  1.00 26.07  ? 407 PHE B CG  1 
ATOM   4628 C  CD1 . PHE B 1 407 ? 106.453 104.425 70.430  1.00 26.07  ? 407 PHE B CD1 1 
ATOM   4629 C  CD2 . PHE B 1 407 ? 106.907 106.668 70.003  1.00 26.07  ? 407 PHE B CD2 1 
ATOM   4630 C  CE1 . PHE B 1 407 ? 107.779 104.177 70.468  1.00 26.07  ? 407 PHE B CE1 1 
ATOM   4631 C  CE2 . PHE B 1 407 ? 108.219 106.409 70.046  1.00 26.07  ? 407 PHE B CE2 1 
ATOM   4632 C  CZ  . PHE B 1 407 ? 108.656 105.168 70.271  1.00 26.07  ? 407 PHE B CZ  1 
ATOM   4633 N  N   . HIS B 1 408 ? 101.394 105.518 70.011  1.00 34.31  ? 408 HIS B N   1 
ATOM   4634 C  CA  . HIS B 1 408 ? 100.130 105.896 70.624  1.00 34.31  ? 408 HIS B CA  1 
ATOM   4635 C  C   . HIS B 1 408 ? 99.391  104.673 71.138  1.00 34.31  ? 408 HIS B C   1 
ATOM   4636 O  O   . HIS B 1 408 ? 98.568  104.770 72.049  1.00 34.31  ? 408 HIS B O   1 
ATOM   4637 C  CB  . HIS B 1 408 ? 99.277  106.664 69.621  1.00 34.31  ? 408 HIS B CB  1 
ATOM   4638 C  CG  . HIS B 1 408 ? 97.973  107.139 70.172  1.00 34.31  ? 408 HIS B CG  1 
ATOM   4639 N  ND1 . HIS B 1 408 ? 97.890  108.024 71.220  1.00 34.31  ? 408 HIS B ND1 1 
ATOM   4640 C  CD2 . HIS B 1 408 ? 96.700  106.854 69.814  1.00 34.31  ? 408 HIS B CD2 1 
ATOM   4641 C  CE1 . HIS B 1 408 ? 96.621  108.257 71.491  1.00 34.31  ? 408 HIS B CE1 1 
ATOM   4642 N  NE2 . HIS B 1 408 ? 95.878  107.563 70.650  1.00 34.31  ? 408 HIS B NE2 1 
ATOM   4643 N  N   . ASN B 1 409 ? 99.656  103.515 70.552  1.00 31.17  ? 409 ASN B N   1 
ATOM   4644 C  CA  . ASN B 1 409 ? 98.969  102.311 71.002  1.00 31.17  ? 409 ASN B CA  1 
ATOM   4645 C  C   . ASN B 1 409 ? 99.501  101.800 72.333  1.00 31.17  ? 409 ASN B C   1 
ATOM   4646 O  O   . ASN B 1 409 ? 99.086  100.733 72.786  1.00 31.17  ? 409 ASN B O   1 
ATOM   4647 C  CB  . ASN B 1 409 ? 99.088  101.196 69.969  1.00 31.17  ? 409 ASN B CB  1 
ATOM   4648 C  CG  . ASN B 1 409 ? 98.131  101.357 68.830  1.00 31.17  ? 409 ASN B CG  1 
ATOM   4649 O  OD1 . ASN B 1 409 ? 97.804  102.468 68.430  1.00 31.17  ? 409 ASN B OD1 1 
ATOM   4650 N  ND2 . ASN B 1 409 ? 97.675  100.241 68.291  1.00 31.17  ? 409 ASN B ND2 1 
ATOM   4651 N  N   . HIS B 1 410 ? 100.486 102.471 72.922  1.00 29.25  ? 410 HIS B N   1 
ATOM   4652 C  CA  . HIS B 1 410 ? 101.096 101.937 74.172  1.00 29.25  ? 410 HIS B CA  1 
ATOM   4653 C  C   . HIS B 1 410 ? 101.111 102.976 75.294  1.00 29.25  ? 410 HIS B C   1 
ATOM   4654 O  O   . HIS B 1 410 ? 102.083 102.980 76.062  1.00 29.25  ? 410 HIS B O   1 
ATOM   4655 C  CB  . HIS B 1 410 ? 102.522 101.434 73.909  1.00 29.25  ? 410 HIS B CB  1 
ATOM   4656 C  CG  . HIS B 1 410 ? 102.610 100.294 72.953  1.00 29.25  ? 410 HIS B CG  1 
ATOM   4657 N  ND1 . HIS B 1 410 ? 101.499 99.750  72.343  1.00 29.25  ? 410 HIS B ND1 1 
ATOM   4658 C  CD2 . HIS B 1 410 ? 103.671 99.597  72.495  1.00 29.25  ? 410 HIS B CD2 1 
ATOM   4659 C  CE1 . HIS B 1 410 ? 101.873 98.765  71.551  1.00 29.25  ? 410 HIS B CE1 1 
ATOM   4660 N  NE2 . HIS B 1 410 ? 103.201 98.652  71.626  1.00 29.25  ? 410 HIS B NE2 1 
ATOM   4661 N  N   . GLY B 1 411 ? 100.103 103.820 75.404  1.00 23.35  ? 411 GLY B N   1 
ATOM   4662 C  CA  . GLY B 1 411 ? 100.071 104.793 76.477  1.00 23.35  ? 411 GLY B CA  1 
ATOM   4663 C  C   . GLY B 1 411 ? 101.199 105.796 76.466  1.00 23.35  ? 411 GLY B C   1 
ATOM   4664 O  O   . GLY B 1 411 ? 101.432 106.451 77.477  1.00 23.35  ? 411 GLY B O   1 
ATOM   4665 N  N   . ILE B 1 412 ? 101.894 105.952 75.339  1.00 19.76  ? 412 ILE B N   1 
ATOM   4666 C  CA  . ILE B 1 412 ? 103.041 106.846 75.217  1.00 19.76  ? 412 ILE B CA  1 
ATOM   4667 C  C   . ILE B 1 412 ? 102.752 107.858 74.121  1.00 19.76  ? 412 ILE B C   1 
ATOM   4668 O  O   . ILE B 1 412 ? 102.722 107.495 72.943  1.00 19.76  ? 412 ILE B O   1 
ATOM   4669 C  CB  . ILE B 1 412 ? 104.320 106.085 74.868  1.00 19.76  ? 412 ILE B CB  1 
ATOM   4670 C  CG1 . ILE B 1 412 ? 104.726 105.174 76.003  1.00 19.76  ? 412 ILE B CG1 1 
ATOM   4671 C  CG2 . ILE B 1 412 ? 105.400 107.043 74.595  1.00 19.76  ? 412 ILE B CG2 1 
ATOM   4672 C  CD1 . ILE B 1 412 ? 106.115 104.632 75.844  1.00 19.76  ? 412 ILE B CD1 1 
ATOM   4673 N  N   . HIS B 1 413 ? 102.604 109.130 74.484  1.00 20.89  ? 413 HIS B N   1 
ATOM   4674 C  CA  . HIS B 1 413 ? 102.035 110.089 73.556  1.00 20.89  ? 413 HIS B CA  1 
ATOM   4675 C  C   . HIS B 1 413 ? 102.917 111.251 73.149  1.00 20.89  ? 413 HIS B C   1 
ATOM   4676 O  O   . HIS B 1 413 ? 102.710 111.777 72.057  1.00 20.89  ? 413 HIS B O   1 
ATOM   4677 C  CB  . HIS B 1 413 ? 100.742 110.663 74.124  1.00 20.89  ? 413 HIS B CB  1 
ATOM   4678 C  CG  . HIS B 1 413 ? 99.700  109.633 74.381  1.00 20.89  ? 413 HIS B CG  1 
ATOM   4679 N  ND1 . HIS B 1 413 ? 99.055  108.955 73.372  1.00 20.89  ? 413 HIS B ND1 1 
ATOM   4680 C  CD2 . HIS B 1 413 ? 99.183  109.168 75.539  1.00 20.89  ? 413 HIS B CD2 1 
ATOM   4681 C  CE1 . HIS B 1 413 ? 98.189  108.109 73.898  1.00 20.89  ? 413 HIS B CE1 1 
ATOM   4682 N  NE2 . HIS B 1 413 ? 98.246  108.220 75.212  1.00 20.89  ? 413 HIS B NE2 1 
ATOM   4683 N  N   . ALA B 1 414 ? 103.855 111.696 73.965  1.00 8.17   ? 414 ALA B N   1 
ATOM   4684 C  CA  . ALA B 1 414 ? 104.704 112.823 73.605  1.00 8.17   ? 414 ALA B CA  1 
ATOM   4685 C  C   . ALA B 1 414 ? 106.034 112.282 73.110  1.00 8.17   ? 414 ALA B C   1 
ATOM   4686 O  O   . ALA B 1 414 ? 106.896 111.930 73.916  1.00 8.17   ? 414 ALA B O   1 
ATOM   4687 C  CB  . ALA B 1 414 ? 104.904 113.752 74.791  1.00 8.17   ? 414 ALA B CB  1 
ATOM   4688 N  N   . THR B 1 415 ? 106.216 112.212 71.802  1.00 9.42   ? 415 THR B N   1 
ATOM   4689 C  CA  . THR B 1 415 ? 107.330 111.466 71.247  1.00 9.42   ? 415 THR B CA  1 
ATOM   4690 C  C   . THR B 1 415 ? 108.301 112.391 70.539  1.00 9.42   ? 415 THR B C   1 
ATOM   4691 O  O   . THR B 1 415 ? 108.119 113.605 70.507  1.00 9.42   ? 415 THR B O   1 
ATOM   4692 C  CB  . THR B 1 415 ? 106.851 110.409 70.277  1.00 9.42   ? 415 THR B CB  1 
ATOM   4693 O  OG1 . THR B 1 415 ? 106.502 111.035 69.043  1.00 9.42   ? 415 THR B OG1 1 
ATOM   4694 C  CG2 . THR B 1 415 ? 105.636 109.740 70.829  1.00 9.42   ? 415 THR B CG2 1 
ATOM   4695 N  N   . THR B 1 416 ? 109.383 111.799 70.037  1.00 9.41   ? 416 THR B N   1 
ATOM   4696 C  CA  . THR B 1 416 ? 110.331 112.512 69.177  1.00 9.41   ? 416 THR B CA  1 
ATOM   4697 C  C   . THR B 1 416 ? 111.172 111.485 68.423  1.00 9.41   ? 416 THR B C   1 
ATOM   4698 O  O   . THR B 1 416 ? 112.099 110.919 68.996  1.00 9.41   ? 416 THR B O   1 
ATOM   4699 C  CB  . THR B 1 416 ? 111.207 113.434 69.994  1.00 9.41   ? 416 THR B CB  1 
ATOM   4700 O  OG1 . THR B 1 416 ? 110.378 114.308 70.760  1.00 9.41   ? 416 THR B OG1 1 
ATOM   4701 C  CG2 . THR B 1 416 ? 112.034 114.239 69.096  1.00 9.41   ? 416 THR B CG2 1 
ATOM   4702 N  N   . ILE B 1 417 ? 110.879 111.276 67.146  1.00 8.51   ? 417 ILE B N   1 
ATOM   4703 C  CA  . ILE B 1 417 ? 111.474 110.205 66.355  1.00 8.51   ? 417 ILE B CA  1 
ATOM   4704 C  C   . ILE B 1 417 ? 112.396 110.800 65.302  1.00 8.51   ? 417 ILE B C   1 
ATOM   4705 O  O   . ILE B 1 417 ? 111.971 111.017 64.168  1.00 8.51   ? 417 ILE B O   1 
ATOM   4706 C  CB  . ILE B 1 417 ? 110.385 109.368 65.683  1.00 8.51   ? 417 ILE B CB  1 
ATOM   4707 C  CG1 . ILE B 1 417 ? 109.378 108.940 66.710  1.00 8.51   ? 417 ILE B CG1 1 
ATOM   4708 C  CG2 . ILE B 1 417 ? 110.964 108.147 65.061  1.00 8.51   ? 417 ILE B CG2 1 
ATOM   4709 C  CD1 . ILE B 1 417 ? 109.881 107.853 67.533  1.00 8.51   ? 417 ILE B CD1 1 
ATOM   4710 N  N   . GLN B 1 418 ? 113.668 110.983 65.629  1.00 17.72  ? 418 GLN B N   1 
ATOM   4711 C  CA  . GLN B 1 418 ? 114.586 111.611 64.682  1.00 17.72  ? 418 GLN B CA  1 
ATOM   4712 C  C   . GLN B 1 418 ? 115.012 110.614 63.633  1.00 17.72  ? 418 GLN B C   1 
ATOM   4713 O  O   . GLN B 1 418 ? 115.570 109.577 63.995  1.00 17.72  ? 418 GLN B O   1 
ATOM   4714 C  CB  . GLN B 1 418 ? 115.819 112.151 65.369  1.00 17.72  ? 418 GLN B CB  1 
ATOM   4715 C  CG  . GLN B 1 418 ? 116.873 112.564 64.377  1.00 17.72  ? 418 GLN B CG  1 
ATOM   4716 C  CD  . GLN B 1 418 ? 118.187 112.851 65.037  1.00 17.72  ? 418 GLN B CD  1 
ATOM   4717 O  OE1 . GLN B 1 418 ? 118.286 112.825 66.250  1.00 17.72  ? 418 GLN B OE1 1 
ATOM   4718 N  NE2 . GLN B 1 418 ? 119.201 113.147 64.251  1.00 17.72  ? 418 GLN B NE2 1 
ATOM   4719 N  N   . PRO B 1 419 ? 114.825 110.854 62.377  1.00 27.65  ? 419 PRO B N   1 
ATOM   4720 C  CA  . PRO B 1 419 ? 115.259 109.876 61.387  1.00 27.65  ? 419 PRO B CA  1 
ATOM   4721 C  C   . PRO B 1 419 ? 116.653 110.168 60.881  1.00 27.65  ? 419 PRO B C   1 
ATOM   4722 O  O   . PRO B 1 419 ? 116.942 111.302 60.501  1.00 27.65  ? 419 PRO B O   1 
ATOM   4723 C  CB  . PRO B 1 419 ? 114.216 110.036 60.290  1.00 27.65  ? 419 PRO B CB  1 
ATOM   4724 C  CG  . PRO B 1 419 ? 113.934 111.447 60.332  1.00 27.65  ? 419 PRO B CG  1 
ATOM   4725 C  CD  . PRO B 1 419 ? 114.012 111.892 61.762  1.00 27.65  ? 419 PRO B CD  1 
ATOM   4726 N  N   . GLU B 1 420 ? 117.525 109.162 60.868  1.00 31.82  ? 420 GLU B N   1 
ATOM   4727 C  CA  . GLU B 1 420 ? 118.917 109.295 60.464  1.00 31.82  ? 420 GLU B CA  1 
ATOM   4728 C  C   . GLU B 1 420 ? 119.033 108.711 59.063  1.00 31.82  ? 420 GLU B C   1 
ATOM   4729 O  O   . GLU B 1 420 ? 119.068 107.492 58.897  1.00 31.82  ? 420 GLU B O   1 
ATOM   4730 C  CB  . GLU B 1 420 ? 119.822 108.576 61.456  1.00 31.82  ? 420 GLU B CB  1 
ATOM   4731 C  CG  . GLU B 1 420 ? 120.063 109.328 62.749  1.00 31.82  ? 420 GLU B CG  1 
ATOM   4732 C  CD  . GLU B 1 420 ? 120.321 108.414 63.942  1.00 31.82  ? 420 GLU B CD  1 
ATOM   4733 O  OE1 . GLU B 1 420 ? 120.033 107.214 63.834  1.00 31.82  ? 420 GLU B OE1 1 
ATOM   4734 O  OE2 . GLU B 1 420 ? 120.795 108.889 64.995  1.00 31.82  ? 420 GLU B OE2 1 
ATOM   4735 N  N   . PHE B 1 421 ? 119.067 109.577 58.053  1.00 54.64  ? 421 PHE B N   1 
ATOM   4736 C  CA  . PHE B 1 421 ? 119.115 109.122 56.669  1.00 54.64  ? 421 PHE B CA  1 
ATOM   4737 C  C   . PHE B 1 421 ? 120.510 108.645 56.293  1.00 54.64  ? 421 PHE B C   1 
ATOM   4738 O  O   . PHE B 1 421 ? 121.502 109.358 56.448  1.00 54.64  ? 421 PHE B O   1 
ATOM   4739 C  CB  . PHE B 1 421 ? 118.702 110.238 55.715  1.00 54.64  ? 421 PHE B CB  1 
ATOM   4740 C  CG  . PHE B 1 421 ? 117.233 110.465 55.665  1.00 54.64  ? 421 PHE B CG  1 
ATOM   4741 C  CD1 . PHE B 1 421 ? 116.360 109.420 55.830  1.00 54.64  ? 421 PHE B CD1 1 
ATOM   4742 C  CD2 . PHE B 1 421 ? 116.726 111.728 55.486  1.00 54.64  ? 421 PHE B CD2 1 
ATOM   4743 C  CE1 . PHE B 1 421 ? 115.018 109.627 55.795  1.00 54.64  ? 421 PHE B CE1 1 
ATOM   4744 C  CE2 . PHE B 1 421 ? 115.385 111.940 55.459  1.00 54.64  ? 421 PHE B CE2 1 
ATOM   4745 C  CZ  . PHE B 1 421 ? 114.530 110.889 55.613  1.00 54.64  ? 421 PHE B CZ  1 
ATOM   4746 N  N   . ALA B 1 422 ? 120.573 107.435 55.752  1.00 71.03  ? 422 ALA B N   1 
ATOM   4747 C  CA  . ALA B 1 422 ? 121.849 106.811 55.441  1.00 71.03  ? 422 ALA B CA  1 
ATOM   4748 C  C   . ALA B 1 422 ? 122.494 107.454 54.220  1.00 71.03  ? 422 ALA B C   1 
ATOM   4749 O  O   . ALA B 1 422 ? 121.864 107.628 53.174  1.00 71.03  ? 422 ALA B O   1 
ATOM   4750 C  CB  . ALA B 1 422 ? 121.678 105.310 55.203  1.00 71.03  ? 422 ALA B CB  1 
ATOM   4751 N  N   . SER B 1 423 ? 123.771 107.795 54.367  1.00 79.17  ? 423 SER B N   1 
ATOM   4752 C  CA  . SER B 1 423 ? 124.615 108.344 53.319  1.00 79.17  ? 423 SER B CA  1 
ATOM   4753 C  C   . SER B 1 423 ? 125.200 107.197 52.501  1.00 79.17  ? 423 SER B C   1 
ATOM   4754 O  O   . SER B 1 423 ? 124.711 106.062 52.551  1.00 79.17  ? 423 SER B O   1 
ATOM   4755 C  CB  . SER B 1 423 ? 125.708 109.225 53.925  1.00 79.17  ? 423 SER B CB  1 
ATOM   4756 O  OG  . SER B 1 423 ? 125.178 110.078 54.922  1.00 79.17  ? 423 SER B OG  1 
ATOM   4757 N  N   . VAL B 1 424 ? 126.238 107.495 51.726  1.00 83.41  ? 424 VAL B N   1 
ATOM   4758 C  CA  . VAL B 1 424 ? 126.873 106.502 50.865  1.00 83.41  ? 424 VAL B CA  1 
ATOM   4759 C  C   . VAL B 1 424 ? 127.914 105.716 51.651  1.00 83.41  ? 424 VAL B C   1 
ATOM   4760 O  O   . VAL B 1 424 ? 128.883 106.279 52.173  1.00 83.41  ? 424 VAL B O   1 
ATOM   4761 C  CB  . VAL B 1 424 ? 127.497 107.172 49.628  1.00 83.41  ? 424 VAL B CB  1 
ATOM   4762 C  CG1 . VAL B 1 424 ? 128.028 106.118 48.672  1.00 83.41  ? 424 VAL B CG1 1 
ATOM   4763 C  CG2 . VAL B 1 424 ? 126.473 108.055 48.937  1.00 83.41  ? 424 VAL B CG2 1 
ATOM   4764 N  N   . GLY B 1 425 ? 127.709 104.399 51.727  1.00 80.59  ? 425 GLY B N   1 
ATOM   4765 C  CA  . GLY B 1 425 ? 128.669 103.480 52.303  1.00 80.59  ? 425 GLY B CA  1 
ATOM   4766 C  C   . GLY B 1 425 ? 128.771 103.467 53.811  1.00 80.59  ? 425 GLY B C   1 
ATOM   4767 O  O   . GLY B 1 425 ? 129.637 102.761 54.343  1.00 80.59  ? 425 GLY B O   1 
ATOM   4768 N  N   . SER B 1 426 ? 127.922 104.202 54.527  1.00 76.88  ? 426 SER B N   1 
ATOM   4769 C  CA  . SER B 1 426 ? 128.070 104.368 55.967  1.00 76.88  ? 426 SER B CA  1 
ATOM   4770 C  C   . SER B 1 426 ? 127.114 103.510 56.786  1.00 76.88  ? 426 SER B C   1 
ATOM   4771 O  O   . SER B 1 426 ? 126.812 103.868 57.929  1.00 76.88  ? 426 SER B O   1 
ATOM   4772 C  CB  . SER B 1 426 ? 127.889 105.835 56.351  1.00 76.88  ? 426 SER B CB  1 
ATOM   4773 O  OG  . SER B 1 426 ? 127.725 105.960 57.753  1.00 76.88  ? 426 SER B OG  1 
ATOM   4774 N  N   . LYS B 1 427 ? 126.633 102.393 56.243  1.00 75.89  ? 427 LYS B N   1 
ATOM   4775 C  CA  . LYS B 1 427 ? 125.775 101.485 57.009  1.00 75.89  ? 427 LYS B CA  1 
ATOM   4776 C  C   . LYS B 1 427 ? 126.616 100.406 57.694  1.00 75.89  ? 427 LYS B C   1 
ATOM   4777 O  O   . LYS B 1 427 ? 126.345 99.210  57.621  1.00 75.89  ? 427 LYS B O   1 
ATOM   4778 C  CB  . LYS B 1 427 ? 124.713 100.873 56.105  1.00 75.89  ? 427 LYS B CB  1 
ATOM   4779 C  CG  . LYS B 1 427 ? 125.255 100.302 54.810  1.00 75.89  ? 427 LYS B CG  1 
ATOM   4780 C  CD  . LYS B 1 427 ? 124.255 99.360  54.174  1.00 75.89  ? 427 LYS B CD  1 
ATOM   4781 C  CE  . LYS B 1 427 ? 124.490 99.252  52.683  1.00 75.89  ? 427 LYS B CE  1 
ATOM   4782 N  NZ  . LYS B 1 427 ? 125.940 99.151  52.369  1.00 75.89  ? 427 LYS B NZ  1 
ATOM   4783 N  N   . SER B 1 428 ? 127.659 100.870 58.381  1.00 73.26  ? 428 SER B N   1 
ATOM   4784 C  CA  . SER B 1 428 ? 128.568 99.993  59.103  1.00 73.26  ? 428 SER B CA  1 
ATOM   4785 C  C   . SER B 1 428 ? 129.018 100.569 60.436  1.00 73.26  ? 428 SER B C   1 
ATOM   4786 O  O   . SER B 1 428 ? 130.075 100.171 60.932  1.00 73.26  ? 428 SER B O   1 
ATOM   4787 C  CB  . SER B 1 428 ? 129.804 99.684  58.247  1.00 73.26  ? 428 SER B CB  1 
ATOM   4788 O  OG  . SER B 1 428 ? 130.701 100.781 58.254  1.00 73.26  ? 428 SER B OG  1 
ATOM   4789 N  N   . SER B 1 429 ? 128.267 101.497 61.022  1.00 64.98  ? 429 SER B N   1 
ATOM   4790 C  CA  . SER B 1 429 ? 128.742 102.235 62.186  1.00 64.98  ? 429 SER B CA  1 
ATOM   4791 C  C   . SER B 1 429 ? 127.528 102.761 62.942  1.00 64.98  ? 429 SER B C   1 
ATOM   4792 O  O   . SER B 1 429 ? 126.974 103.798 62.575  1.00 64.98  ? 429 SER B O   1 
ATOM   4793 C  CB  . SER B 1 429 ? 129.649 103.370 61.751  1.00 64.98  ? 429 SER B CB  1 
ATOM   4794 O  OG  . SER B 1 429 ? 128.869 104.506 61.421  1.00 64.98  ? 429 SER B OG  1 
ATOM   4795 N  N   . VAL B 1 430 ? 127.135 102.055 64.001  1.00 56.08  ? 430 VAL B N   1 
ATOM   4796 C  CA  . VAL B 1 430 ? 126.023 102.511 64.826  1.00 56.08  ? 430 VAL B CA  1 
ATOM   4797 C  C   . VAL B 1 430 ? 126.426 103.663 65.723  1.00 56.08  ? 430 VAL B C   1 
ATOM   4798 O  O   . VAL B 1 430 ? 125.699 104.657 65.805  1.00 56.08  ? 430 VAL B O   1 
ATOM   4799 C  CB  . VAL B 1 430 ? 125.496 101.356 65.690  1.00 56.08  ? 430 VAL B CB  1 
ATOM   4800 C  CG1 . VAL B 1 430 ? 124.533 101.860 66.754  1.00 56.08  ? 430 VAL B CG1 1 
ATOM   4801 C  CG2 . VAL B 1 430 ? 124.866 100.290 64.819  1.00 56.08  ? 430 VAL B CG2 1 
ATOM   4802 N  N   . VAL B 1 431 ? 127.587 103.550 66.373  1.00 57.30  ? 431 VAL B N   1 
ATOM   4803 C  CA  . VAL B 1 431 ? 128.049 104.600 67.283  1.00 57.30  ? 431 VAL B CA  1 
ATOM   4804 C  C   . VAL B 1 431 ? 127.961 105.988 66.659  1.00 57.30  ? 431 VAL B C   1 
ATOM   4805 O  O   . VAL B 1 431 ? 127.581 106.935 67.365  1.00 57.30  ? 431 VAL B O   1 
ATOM   4806 C  CB  . VAL B 1 431 ? 129.462 104.266 67.793  1.00 57.30  ? 431 VAL B CB  1 
ATOM   4807 N  N   . PRO B 1 432 ? 128.292 106.189 65.379  1.00 51.94  ? 432 PRO B N   1 
ATOM   4808 C  CA  . PRO B 1 432 ? 128.059 107.511 64.781  1.00 51.94  ? 432 PRO B CA  1 
ATOM   4809 C  C   . PRO B 1 432 ? 126.594 107.823 64.486  1.00 51.94  ? 432 PRO B C   1 
ATOM   4810 O  O   . PRO B 1 432 ? 126.299 108.979 64.155  1.00 51.94  ? 432 PRO B O   1 
ATOM   4811 C  CB  . PRO B 1 432 ? 128.893 107.466 63.487  1.00 51.94  ? 432 PRO B CB  1 
ATOM   4812 N  N   . CYS B 1 433 ? 125.674 106.857 64.559  1.00 44.13  ? 433 CYS B N   1 
ATOM   4813 C  CA  . CYS B 1 433 ? 124.270 107.095 64.220  1.00 44.13  ? 433 CYS B CA  1 
ATOM   4814 C  C   . CYS B 1 433 ? 124.101 107.777 62.871  1.00 44.13  ? 433 CYS B C   1 
ATOM   4815 O  O   . CYS B 1 433 ? 123.037 108.322 62.589  1.00 44.13  ? 433 CYS B O   1 
ATOM   4816 C  CB  . CYS B 1 433 ? 123.560 107.940 65.285  1.00 44.13  ? 433 CYS B CB  1 
ATOM   4817 S  SG  . CYS B 1 433 ? 122.942 107.096 66.738  1.00 44.13  ? 433 CYS B SG  1 
ATOM   4818 N  N   . GLU B 1 434 ? 125.138 107.788 62.040  1.00 45.65  ? 434 GLU B N   1 
ATOM   4819 C  CA  . GLU B 1 434 ? 125.262 108.695 60.906  1.00 45.65  ? 434 GLU B CA  1 
ATOM   4820 C  C   . GLU B 1 434 ? 125.248 110.145 61.343  1.00 45.65  ? 434 GLU B C   1 
ATOM   4821 O  O   . GLU B 1 434 ? 125.310 111.044 60.501  1.00 45.65  ? 434 GLU B O   1 
ATOM   4822 C  CB  . GLU B 1 434 ? 124.171 108.466 59.858  1.00 45.65  ? 434 GLU B CB  1 
ATOM   4823 C  CG  . GLU B 1 434 ? 124.333 107.199 59.066  1.00 45.65  ? 434 GLU B CG  1 
ATOM   4824 C  CD  . GLU B 1 434 ? 123.516 106.063 59.627  1.00 45.65  ? 434 GLU B CD  1 
ATOM   4825 O  OE1 . GLU B 1 434 ? 122.756 105.444 58.858  1.00 45.65  ? 434 GLU B OE1 1 
ATOM   4826 O  OE2 . GLU B 1 434 ? 123.632 105.787 60.835  1.00 45.65  ? 434 GLU B OE2 1 
ATOM   4827 N  N   . LEU B 1 435 ? 125.173 110.387 62.647  1.00 45.13  ? 435 LEU B N   1 
ATOM   4828 C  CA  . LEU B 1 435 ? 124.927 111.712 63.199  1.00 45.13  ? 435 LEU B CA  1 
ATOM   4829 C  C   . LEU B 1 435 ? 125.335 111.672 64.659  1.00 45.13  ? 435 LEU B C   1 
ATOM   4830 O  O   . LEU B 1 435 ? 124.656 111.035 65.468  1.00 45.13  ? 435 LEU B O   1 
ATOM   4831 C  CB  . LEU B 1 435 ? 123.457 112.075 63.047  1.00 45.13  ? 435 LEU B CB  1 
ATOM   4832 C  CG  . LEU B 1 435 ? 123.020 113.469 63.429  1.00 45.13  ? 435 LEU B CG  1 
ATOM   4833 C  CD1 . LEU B 1 435 ? 124.117 114.432 63.087  1.00 45.13  ? 435 LEU B CD1 1 
ATOM   4834 C  CD2 . LEU B 1 435 ? 121.794 113.784 62.635  1.00 45.13  ? 435 LEU B CD2 1 
ATOM   4835 N  N   . ALA B 1 436 ? 126.435 112.325 65.000  1.00 48.19  ? 436 ALA B N   1 
ATOM   4836 C  CA  . ALA B 1 436 ? 127.021 112.140 66.313  1.00 48.19  ? 436 ALA B CA  1 
ATOM   4837 C  C   . ALA B 1 436 ? 127.915 113.327 66.614  1.00 48.19  ? 436 ALA B C   1 
ATOM   4838 O  O   . ALA B 1 436 ? 127.805 114.384 65.987  1.00 48.19  ? 436 ALA B O   1 
ATOM   4839 C  CB  . ALA B 1 436 ? 127.787 110.817 66.386  1.00 48.19  ? 436 ALA B CB  1 
ATOM   4840 N  N   . CYS B 1 437 ? 128.727 113.210 67.659  1.00 48.93  ? 437 CYS B N   1 
ATOM   4841 C  CA  . CYS B 1 437 ? 129.594 114.344 68.087  1.00 48.93  ? 437 CYS B CA  1 
ATOM   4842 C  C   . CYS B 1 437 ? 131.066 114.031 67.806  1.00 48.93  ? 437 CYS B C   1 
ATOM   4843 O  O   . CYS B 1 437 ? 131.575 114.481 66.762  1.00 48.93  ? 437 CYS B O   1 
ATOM   4844 C  CB  . CYS B 1 437 ? 129.408 114.628 69.574  1.00 48.93  ? 437 CYS B CB  1 
ATOM   4845 S  SG  . CYS B 1 437 ? 129.195 116.385 69.967  1.00 48.93  ? 437 CYS B SG  1 
ATOM   4846 N  N   . ARG B 1 438 ? 131.707 113.292 68.703  1.00 54.94  ? 438 ARG B N   1 
ATOM   4847 C  CA  . ARG B 1 438 ? 133.133 112.902 68.553  1.00 54.94  ? 438 ARG B CA  1 
ATOM   4848 C  C   . ARG B 1 438 ? 133.423 111.740 69.510  1.00 54.94  ? 438 ARG B C   1 
ATOM   4849 O  O   . ARG B 1 438 ? 133.684 110.626 69.016  1.00 54.94  ? 438 ARG B O   1 
ATOM   4850 C  CB  . ARG B 1 438 ? 134.050 114.096 68.839  1.00 54.94  ? 438 ARG B CB  1 
ATOM   4851 N  N   . THR B 1 439 ? 133.392 111.987 70.815  1.00 58.57  ? 439 THR B N   1 
ATOM   4852 C  CA  . THR B 1 439 ? 133.647 110.913 71.813  1.00 58.57  ? 439 THR B CA  1 
ATOM   4853 C  C   . THR B 1 439 ? 132.618 110.993 72.948  1.00 58.57  ? 439 THR B C   1 
ATOM   4854 O  O   . THR B 1 439 ? 131.798 110.061 73.064  1.00 58.57  ? 439 THR B O   1 
ATOM   4855 C  CB  . THR B 1 439 ? 135.089 110.979 72.330  1.00 58.57  ? 439 THR B CB  1 
ATOM   4856 O  OG1 . THR B 1 439 ? 135.342 112.317 72.761  1.00 58.57  ? 439 THR B OG1 1 
ATOM   4857 C  CG2 . THR B 1 439 ? 136.107 110.585 71.283  1.00 58.57  ? 439 THR B CG2 1 
ATOM   4858 N  N   . GLN B 1 440 ? 132.660 112.056 73.748  1.00 53.53  ? 440 GLN B N   1 
ATOM   4859 C  CA  . GLN B 1 440 ? 131.732 112.235 74.899  1.00 53.53  ? 440 GLN B CA  1 
ATOM   4860 C  C   . GLN B 1 440 ? 130.326 112.601 74.407  1.00 53.53  ? 440 GLN B C   1 
ATOM   4861 O  O   . GLN B 1 440 ? 130.211 113.105 73.274  1.00 53.53  ? 440 GLN B O   1 
ATOM   4862 C  CB  . GLN B 1 440 ? 132.252 113.318 75.846  1.00 53.53  ? 440 GLN B CB  1 
ATOM   4863 C  CG  . GLN B 1 440 ? 132.131 114.723 75.276  1.00 53.53  ? 440 GLN B CG  1 
ATOM   4864 C  CD  . GLN B 1 440 ? 132.841 114.866 73.953  1.00 53.53  ? 440 GLN B CD  1 
ATOM   4865 O  OE1 . GLN B 1 440 ? 133.606 113.999 73.540  1.00 53.53  ? 440 GLN B OE1 1 
ATOM   4866 N  NE2 . GLN B 1 440 ? 132.592 115.974 73.273  1.00 53.53  ? 440 GLN B NE2 1 
ATOM   4867 N  N   . CYS B 1 441 ? 129.304 112.326 75.215  1.00 33.42  ? 441 CYS B N   1 
ATOM   4868 C  CA  . CYS B 1 441 ? 127.895 112.655 74.864  1.00 33.42  ? 441 CYS B CA  1 
ATOM   4869 C  C   . CYS B 1 441 ? 127.058 112.719 76.147  1.00 33.42  ? 441 CYS B C   1 
ATOM   4870 O  O   . CYS B 1 441 ? 127.381 113.514 77.030  1.00 33.42  ? 441 CYS B O   1 
ATOM   4871 C  CB  . CYS B 1 441 ? 127.293 111.604 73.939  1.00 33.42  ? 441 CYS B CB  1 
ATOM   4872 S  SG  . CYS B 1 441 ? 126.330 110.348 74.821  1.00 33.42  ? 441 CYS B SG  1 
HETATM 4873 ZN ZN  . ZN  C 2 .   ? 121.357 119.896 123.671 1.00 93.20  ? 601 ZN  A ZN  1 
HETATM 4874 ZN ZN  . ZN  D 2 .   ? 126.865 111.998 114.178 1.00 110.34 ? 602 ZN  A ZN  1 
HETATM 4875 ZN ZN  . ZN  E 2 .   ? 129.024 117.421 71.645  1.00 62.80  ? 603 ZN  A ZN  1 
HETATM 4876 ZN ZN  . ZN  F 2 .   ? 105.769 119.341 66.244  1.00 43.25  ? 604 ZN  A ZN  1 
HETATM 4877 ZN ZN  . ZN  G 2 .   ? 105.813 107.288 123.639 1.00 93.20  ? 601 ZN  B ZN  1 
HETATM 4878 ZN ZN  . ZN  H 2 .   ? 100.250 115.140 114.140 1.00 110.34 ? 602 ZN  B ZN  1 
HETATM 4879 ZN ZN  . ZN  I 2 .   ? 98.073  109.638 71.618  1.00 62.80  ? 603 ZN  B ZN  1 
HETATM 4880 ZN ZN  . ZN  J 2 .   ? 121.332 107.839 66.194  1.00 43.25  ? 604 ZN  B ZN  1 
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