data_8QTV
# 
_entry.id   8QTV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8QTV         pdb_00008qtv 10.2210/pdb8qtv/pdb 
WWPDB D_1292133962 ?            ?                   
EMDB  EMD-18654    ?            ?                   
# 
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 FSC               1 0 2025-03-12 ? 
4 'Half map'        1 0 2025-03-12 1 
5 'Half map'        1 0 2025-03-12 2 
6 Image             1 0 2025-03-12 ? 
7 'Primary map'     1 0 2025-03-12 ? 
8 'Structure model' 1 1 2025-04-02 ? 
# 
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 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 'Primary map'     repository 'Initial release' ? ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 8 'Structure model' 'Data collection'     
2 8 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 8 'Structure model' citation 
2 8 'Structure model' em_admin 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 8 'Structure model' '_citation.journal_volume' 
2 8 'Structure model' '_citation.page_first'     
3 8 'Structure model' '_citation.page_last'      
4 8 'Structure model' '_em_admin.last_update'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QTV 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                           8QTB      unspecified            
PDB  .                           8QSP      unspecified            
EMDB 
;MUC5AC D'D3CysD1 domains.
;
EMD-18654 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gunnar.hansson@medkem.gu.se 
_pdbx_contact_author.name_first         Gunnar 
_pdbx_contact_author.name_last          Hansson 
_pdbx_contact_author.name_mi            C 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1900-1869 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Trillo-Muyo, S.' 1 0000-0002-3135-9134 
'Hansson, G.C.'   2 0000-0002-1900-1869 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Embo Rep.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1469-3178 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            26 
_citation.language                  ? 
_citation.page_first                1457 
_citation.page_last                 1471 
_citation.title                     
'Structure of the MUC5AC VWD3 assembly responsible for the formation of net-like mucin polymers.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s44319-025-00395-8 
_citation.pdbx_database_id_PubMed   40016425 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Trillo-Muyo, S.' 1 0000-0002-3135-9134 
primary 'Ermund, A.'      2 0000-0002-3233-043X 
primary 'Hansson, G.C.'   3 0000-0002-1900-1869 
# 
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 Mucin-5AC     78246.172 2 ? ? ? ? 
2 non-polymer syn 'CALCIUM ION' 40.078    2 ? ? ? ? 
# 
_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       
;DAAQPARRAVRSSRHHHHHHGSPVCAAPMVFFDCRNATPGDTGAGCQKSCHTLDMTCYSPQCVPGCVCPDGLVADGEGGC
ITAEDCPCVHNEASYRAGQTIRVGCNTCTCDSRMWRCTDDPCLATCAVYGDGHYLTFDGQSYSFNGDCEYTLVQNHCGGK
DSTQDSFRVVTENVPCGTTGTTCSKAIKIFLGGFELKLSHGKVEVIGTDESQEVPYTIRQMGIYLVVDTDIGLVLLWDKK
TSIFINLSPEFKGRVCGLCGNFDDIAVNDFATRSRSVVGDVLEFGNSWKLSPSCPDALAPKDPCTANPFRKSWAQKQCSI
LHGPTFAACHAHVEPARYYEACVNDACACDSGGDCECFCTAVAAYAQACHEVGLCVSWRTPSICPLFCDYYNPEGQCEWH
YQPCGVPCLRTCRNPRGDCLRDVRGLEGCYPKCPPEAPIFDEDKMQCVATCPTPPLPPRCHVHGKSYRPGAVVPSDKNCQ
SCLCTERGVECTYKAEACVCTYNGQRFHPGDVIYHTTDGTGGCISARCGANGTIERRVYPCSPTTPVPPTTFSFSTPPLV
VSSTHTPSNGPSSAHTGPPSSAWPTTAGTSPRTRLPTASASLPPVCGEKCLWSPWMDVSRPGRGTDSGDFDTLENLRAHG
YRVCESPRSVECRAEDAPGVPLRALGQRVQCSPDVGLTCRNREQASGLCYNYQIRVQCCTPLPCTSEQKLISEEDLSRKL
TR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DAAQPARRAVRSSRHHHHHHGSPVCAAPMVFFDCRNATPGDTGAGCQKSCHTLDMTCYSPQCVPGCVCPDGLVADGEGGC
ITAEDCPCVHNEASYRAGQTIRVGCNTCTCDSRMWRCTDDPCLATCAVYGDGHYLTFDGQSYSFNGDCEYTLVQNHCGGK
DSTQDSFRVVTENVPCGTTGTTCSKAIKIFLGGFELKLSHGKVEVIGTDESQEVPYTIRQMGIYLVVDTDIGLVLLWDKK
TSIFINLSPEFKGRVCGLCGNFDDIAVNDFATRSRSVVGDVLEFGNSWKLSPSCPDALAPKDPCTANPFRKSWAQKQCSI
LHGPTFAACHAHVEPARYYEACVNDACACDSGGDCECFCTAVAAYAQACHEVGLCVSWRTPSICPLFCDYYNPEGQCEWH
YQPCGVPCLRTCRNPRGDCLRDVRGLEGCYPKCPPEAPIFDEDKMQCVATCPTPPLPPRCHVHGKSYRPGAVVPSDKNCQ
SCLCTERGVECTYKAEACVCTYNGQRFHPGDVIYHTTDGTGGCISARCGANGTIERRVYPCSPTTPVPPTTFSFSTPPLV
VSSTHTPSNGPSSAHTGPPSSAWPTTAGTSPRTRLPTASASLPPVCGEKCLWSPWMDVSRPGRGTDSGDFDTLENLRAHG
YRVCESPRSVECRAEDAPGVPLRALGQRVQCSPDVGLTCRNREQASGLCYNYQIRVQCCTPLPCTSEQKLISEEDLSRKL
TR
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        'CALCIUM ION' 
_pdbx_entity_nonpoly.comp_id     CA 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   ALA n 
1 3   ALA n 
1 4   GLN n 
1 5   PRO n 
1 6   ALA n 
1 7   ARG n 
1 8   ARG n 
1 9   ALA n 
1 10  VAL n 
1 11  ARG n 
1 12  SER n 
1 13  SER n 
1 14  ARG n 
1 15  HIS n 
1 16  HIS n 
1 17  HIS n 
1 18  HIS n 
1 19  HIS n 
1 20  HIS n 
1 21  GLY n 
1 22  SER n 
1 23  PRO n 
1 24  VAL n 
1 25  CYS n 
1 26  ALA n 
1 27  ALA n 
1 28  PRO n 
1 29  MET n 
1 30  VAL n 
1 31  PHE n 
1 32  PHE n 
1 33  ASP n 
1 34  CYS n 
1 35  ARG n 
1 36  ASN n 
1 37  ALA n 
1 38  THR n 
1 39  PRO n 
1 40  GLY n 
1 41  ASP n 
1 42  THR n 
1 43  GLY n 
1 44  ALA n 
1 45  GLY n 
1 46  CYS n 
1 47  GLN n 
1 48  LYS n 
1 49  SER n 
1 50  CYS n 
1 51  HIS n 
1 52  THR n 
1 53  LEU n 
1 54  ASP n 
1 55  MET n 
1 56  THR n 
1 57  CYS n 
1 58  TYR n 
1 59  SER n 
1 60  PRO n 
1 61  GLN n 
1 62  CYS n 
1 63  VAL n 
1 64  PRO n 
1 65  GLY n 
1 66  CYS n 
1 67  VAL n 
1 68  CYS n 
1 69  PRO n 
1 70  ASP n 
1 71  GLY n 
1 72  LEU n 
1 73  VAL n 
1 74  ALA n 
1 75  ASP n 
1 76  GLY n 
1 77  GLU n 
1 78  GLY n 
1 79  GLY n 
1 80  CYS n 
1 81  ILE n 
1 82  THR n 
1 83  ALA n 
1 84  GLU n 
1 85  ASP n 
1 86  CYS n 
1 87  PRO n 
1 88  CYS n 
1 89  VAL n 
1 90  HIS n 
1 91  ASN n 
1 92  GLU n 
1 93  ALA n 
1 94  SER n 
1 95  TYR n 
1 96  ARG n 
1 97  ALA n 
1 98  GLY n 
1 99  GLN n 
1 100 THR n 
1 101 ILE n 
1 102 ARG n 
1 103 VAL n 
1 104 GLY n 
1 105 CYS n 
1 106 ASN n 
1 107 THR n 
1 108 CYS n 
1 109 THR n 
1 110 CYS n 
1 111 ASP n 
1 112 SER n 
1 113 ARG n 
1 114 MET n 
1 115 TRP n 
1 116 ARG n 
1 117 CYS n 
1 118 THR n 
1 119 ASP n 
1 120 ASP n 
1 121 PRO n 
1 122 CYS n 
1 123 LEU n 
1 124 ALA n 
1 125 THR n 
1 126 CYS n 
1 127 ALA n 
1 128 VAL n 
1 129 TYR n 
1 130 GLY n 
1 131 ASP n 
1 132 GLY n 
1 133 HIS n 
1 134 TYR n 
1 135 LEU n 
1 136 THR n 
1 137 PHE n 
1 138 ASP n 
1 139 GLY n 
1 140 GLN n 
1 141 SER n 
1 142 TYR n 
1 143 SER n 
1 144 PHE n 
1 145 ASN n 
1 146 GLY n 
1 147 ASP n 
1 148 CYS n 
1 149 GLU n 
1 150 TYR n 
1 151 THR n 
1 152 LEU n 
1 153 VAL n 
1 154 GLN n 
1 155 ASN n 
1 156 HIS n 
1 157 CYS n 
1 158 GLY n 
1 159 GLY n 
1 160 LYS n 
1 161 ASP n 
1 162 SER n 
1 163 THR n 
1 164 GLN n 
1 165 ASP n 
1 166 SER n 
1 167 PHE n 
1 168 ARG n 
1 169 VAL n 
1 170 VAL n 
1 171 THR n 
1 172 GLU n 
1 173 ASN n 
1 174 VAL n 
1 175 PRO n 
1 176 CYS n 
1 177 GLY n 
1 178 THR n 
1 179 THR n 
1 180 GLY n 
1 181 THR n 
1 182 THR n 
1 183 CYS n 
1 184 SER n 
1 185 LYS n 
1 186 ALA n 
1 187 ILE n 
1 188 LYS n 
1 189 ILE n 
1 190 PHE n 
1 191 LEU n 
1 192 GLY n 
1 193 GLY n 
1 194 PHE n 
1 195 GLU n 
1 196 LEU n 
1 197 LYS n 
1 198 LEU n 
1 199 SER n 
1 200 HIS n 
1 201 GLY n 
1 202 LYS n 
1 203 VAL n 
1 204 GLU n 
1 205 VAL n 
1 206 ILE n 
1 207 GLY n 
1 208 THR n 
1 209 ASP n 
1 210 GLU n 
1 211 SER n 
1 212 GLN n 
1 213 GLU n 
1 214 VAL n 
1 215 PRO n 
1 216 TYR n 
1 217 THR n 
1 218 ILE n 
1 219 ARG n 
1 220 GLN n 
1 221 MET n 
1 222 GLY n 
1 223 ILE n 
1 224 TYR n 
1 225 LEU n 
1 226 VAL n 
1 227 VAL n 
1 228 ASP n 
1 229 THR n 
1 230 ASP n 
1 231 ILE n 
1 232 GLY n 
1 233 LEU n 
1 234 VAL n 
1 235 LEU n 
1 236 LEU n 
1 237 TRP n 
1 238 ASP n 
1 239 LYS n 
1 240 LYS n 
1 241 THR n 
1 242 SER n 
1 243 ILE n 
1 244 PHE n 
1 245 ILE n 
1 246 ASN n 
1 247 LEU n 
1 248 SER n 
1 249 PRO n 
1 250 GLU n 
1 251 PHE n 
1 252 LYS n 
1 253 GLY n 
1 254 ARG n 
1 255 VAL n 
1 256 CYS n 
1 257 GLY n 
1 258 LEU n 
1 259 CYS n 
1 260 GLY n 
1 261 ASN n 
1 262 PHE n 
1 263 ASP n 
1 264 ASP n 
1 265 ILE n 
1 266 ALA n 
1 267 VAL n 
1 268 ASN n 
1 269 ASP n 
1 270 PHE n 
1 271 ALA n 
1 272 THR n 
1 273 ARG n 
1 274 SER n 
1 275 ARG n 
1 276 SER n 
1 277 VAL n 
1 278 VAL n 
1 279 GLY n 
1 280 ASP n 
1 281 VAL n 
1 282 LEU n 
1 283 GLU n 
1 284 PHE n 
1 285 GLY n 
1 286 ASN n 
1 287 SER n 
1 288 TRP n 
1 289 LYS n 
1 290 LEU n 
1 291 SER n 
1 292 PRO n 
1 293 SER n 
1 294 CYS n 
1 295 PRO n 
1 296 ASP n 
1 297 ALA n 
1 298 LEU n 
1 299 ALA n 
1 300 PRO n 
1 301 LYS n 
1 302 ASP n 
1 303 PRO n 
1 304 CYS n 
1 305 THR n 
1 306 ALA n 
1 307 ASN n 
1 308 PRO n 
1 309 PHE n 
1 310 ARG n 
1 311 LYS n 
1 312 SER n 
1 313 TRP n 
1 314 ALA n 
1 315 GLN n 
1 316 LYS n 
1 317 GLN n 
1 318 CYS n 
1 319 SER n 
1 320 ILE n 
1 321 LEU n 
1 322 HIS n 
1 323 GLY n 
1 324 PRO n 
1 325 THR n 
1 326 PHE n 
1 327 ALA n 
1 328 ALA n 
1 329 CYS n 
1 330 HIS n 
1 331 ALA n 
1 332 HIS n 
1 333 VAL n 
1 334 GLU n 
1 335 PRO n 
1 336 ALA n 
1 337 ARG n 
1 338 TYR n 
1 339 TYR n 
1 340 GLU n 
1 341 ALA n 
1 342 CYS n 
1 343 VAL n 
1 344 ASN n 
1 345 ASP n 
1 346 ALA n 
1 347 CYS n 
1 348 ALA n 
1 349 CYS n 
1 350 ASP n 
1 351 SER n 
1 352 GLY n 
1 353 GLY n 
1 354 ASP n 
1 355 CYS n 
1 356 GLU n 
1 357 CYS n 
1 358 PHE n 
1 359 CYS n 
1 360 THR n 
1 361 ALA n 
1 362 VAL n 
1 363 ALA n 
1 364 ALA n 
1 365 TYR n 
1 366 ALA n 
1 367 GLN n 
1 368 ALA n 
1 369 CYS n 
1 370 HIS n 
1 371 GLU n 
1 372 VAL n 
1 373 GLY n 
1 374 LEU n 
1 375 CYS n 
1 376 VAL n 
1 377 SER n 
1 378 TRP n 
1 379 ARG n 
1 380 THR n 
1 381 PRO n 
1 382 SER n 
1 383 ILE n 
1 384 CYS n 
1 385 PRO n 
1 386 LEU n 
1 387 PHE n 
1 388 CYS n 
1 389 ASP n 
1 390 TYR n 
1 391 TYR n 
1 392 ASN n 
1 393 PRO n 
1 394 GLU n 
1 395 GLY n 
1 396 GLN n 
1 397 CYS n 
1 398 GLU n 
1 399 TRP n 
1 400 HIS n 
1 401 TYR n 
1 402 GLN n 
1 403 PRO n 
1 404 CYS n 
1 405 GLY n 
1 406 VAL n 
1 407 PRO n 
1 408 CYS n 
1 409 LEU n 
1 410 ARG n 
1 411 THR n 
1 412 CYS n 
1 413 ARG n 
1 414 ASN n 
1 415 PRO n 
1 416 ARG n 
1 417 GLY n 
1 418 ASP n 
1 419 CYS n 
1 420 LEU n 
1 421 ARG n 
1 422 ASP n 
1 423 VAL n 
1 424 ARG n 
1 425 GLY n 
1 426 LEU n 
1 427 GLU n 
1 428 GLY n 
1 429 CYS n 
1 430 TYR n 
1 431 PRO n 
1 432 LYS n 
1 433 CYS n 
1 434 PRO n 
1 435 PRO n 
1 436 GLU n 
1 437 ALA n 
1 438 PRO n 
1 439 ILE n 
1 440 PHE n 
1 441 ASP n 
1 442 GLU n 
1 443 ASP n 
1 444 LYS n 
1 445 MET n 
1 446 GLN n 
1 447 CYS n 
1 448 VAL n 
1 449 ALA n 
1 450 THR n 
1 451 CYS n 
1 452 PRO n 
1 453 THR n 
1 454 PRO n 
1 455 PRO n 
1 456 LEU n 
1 457 PRO n 
1 458 PRO n 
1 459 ARG n 
1 460 CYS n 
1 461 HIS n 
1 462 VAL n 
1 463 HIS n 
1 464 GLY n 
1 465 LYS n 
1 466 SER n 
1 467 TYR n 
1 468 ARG n 
1 469 PRO n 
1 470 GLY n 
1 471 ALA n 
1 472 VAL n 
1 473 VAL n 
1 474 PRO n 
1 475 SER n 
1 476 ASP n 
1 477 LYS n 
1 478 ASN n 
1 479 CYS n 
1 480 GLN n 
1 481 SER n 
1 482 CYS n 
1 483 LEU n 
1 484 CYS n 
1 485 THR n 
1 486 GLU n 
1 487 ARG n 
1 488 GLY n 
1 489 VAL n 
1 490 GLU n 
1 491 CYS n 
1 492 THR n 
1 493 TYR n 
1 494 LYS n 
1 495 ALA n 
1 496 GLU n 
1 497 ALA n 
1 498 CYS n 
1 499 VAL n 
1 500 CYS n 
1 501 THR n 
1 502 TYR n 
1 503 ASN n 
1 504 GLY n 
1 505 GLN n 
1 506 ARG n 
1 507 PHE n 
1 508 HIS n 
1 509 PRO n 
1 510 GLY n 
1 511 ASP n 
1 512 VAL n 
1 513 ILE n 
1 514 TYR n 
1 515 HIS n 
1 516 THR n 
1 517 THR n 
1 518 ASP n 
1 519 GLY n 
1 520 THR n 
1 521 GLY n 
1 522 GLY n 
1 523 CYS n 
1 524 ILE n 
1 525 SER n 
1 526 ALA n 
1 527 ARG n 
1 528 CYS n 
1 529 GLY n 
1 530 ALA n 
1 531 ASN n 
1 532 GLY n 
1 533 THR n 
1 534 ILE n 
1 535 GLU n 
1 536 ARG n 
1 537 ARG n 
1 538 VAL n 
1 539 TYR n 
1 540 PRO n 
1 541 CYS n 
1 542 SER n 
1 543 PRO n 
1 544 THR n 
1 545 THR n 
1 546 PRO n 
1 547 VAL n 
1 548 PRO n 
1 549 PRO n 
1 550 THR n 
1 551 THR n 
1 552 PHE n 
1 553 SER n 
1 554 PHE n 
1 555 SER n 
1 556 THR n 
1 557 PRO n 
1 558 PRO n 
1 559 LEU n 
1 560 VAL n 
1 561 VAL n 
1 562 SER n 
1 563 SER n 
1 564 THR n 
1 565 HIS n 
1 566 THR n 
1 567 PRO n 
1 568 SER n 
1 569 ASN n 
1 570 GLY n 
1 571 PRO n 
1 572 SER n 
1 573 SER n 
1 574 ALA n 
1 575 HIS n 
1 576 THR n 
1 577 GLY n 
1 578 PRO n 
1 579 PRO n 
1 580 SER n 
1 581 SER n 
1 582 ALA n 
1 583 TRP n 
1 584 PRO n 
1 585 THR n 
1 586 THR n 
1 587 ALA n 
1 588 GLY n 
1 589 THR n 
1 590 SER n 
1 591 PRO n 
1 592 ARG n 
1 593 THR n 
1 594 ARG n 
1 595 LEU n 
1 596 PRO n 
1 597 THR n 
1 598 ALA n 
1 599 SER n 
1 600 ALA n 
1 601 SER n 
1 602 LEU n 
1 603 PRO n 
1 604 PRO n 
1 605 VAL n 
1 606 CYS n 
1 607 GLY n 
1 608 GLU n 
1 609 LYS n 
1 610 CYS n 
1 611 LEU n 
1 612 TRP n 
1 613 SER n 
1 614 PRO n 
1 615 TRP n 
1 616 MET n 
1 617 ASP n 
1 618 VAL n 
1 619 SER n 
1 620 ARG n 
1 621 PRO n 
1 622 GLY n 
1 623 ARG n 
1 624 GLY n 
1 625 THR n 
1 626 ASP n 
1 627 SER n 
1 628 GLY n 
1 629 ASP n 
1 630 PHE n 
1 631 ASP n 
1 632 THR n 
1 633 LEU n 
1 634 GLU n 
1 635 ASN n 
1 636 LEU n 
1 637 ARG n 
1 638 ALA n 
1 639 HIS n 
1 640 GLY n 
1 641 TYR n 
1 642 ARG n 
1 643 VAL n 
1 644 CYS n 
1 645 GLU n 
1 646 SER n 
1 647 PRO n 
1 648 ARG n 
1 649 SER n 
1 650 VAL n 
1 651 GLU n 
1 652 CYS n 
1 653 ARG n 
1 654 ALA n 
1 655 GLU n 
1 656 ASP n 
1 657 ALA n 
1 658 PRO n 
1 659 GLY n 
1 660 VAL n 
1 661 PRO n 
1 662 LEU n 
1 663 ARG n 
1 664 ALA n 
1 665 LEU n 
1 666 GLY n 
1 667 GLN n 
1 668 ARG n 
1 669 VAL n 
1 670 GLN n 
1 671 CYS n 
1 672 SER n 
1 673 PRO n 
1 674 ASP n 
1 675 VAL n 
1 676 GLY n 
1 677 LEU n 
1 678 THR n 
1 679 CYS n 
1 680 ARG n 
1 681 ASN n 
1 682 ARG n 
1 683 GLU n 
1 684 GLN n 
1 685 ALA n 
1 686 SER n 
1 687 GLY n 
1 688 LEU n 
1 689 CYS n 
1 690 TYR n 
1 691 ASN n 
1 692 TYR n 
1 693 GLN n 
1 694 ILE n 
1 695 ARG n 
1 696 VAL n 
1 697 GLN n 
1 698 CYS n 
1 699 CYS n 
1 700 THR n 
1 701 PRO n 
1 702 LEU n 
1 703 PRO n 
1 704 CYS n 
1 705 THR n 
1 706 SER n 
1 707 GLU n 
1 708 GLN n 
1 709 LYS n 
1 710 LEU n 
1 711 ILE n 
1 712 SER n 
1 713 GLU n 
1 714 GLU n 
1 715 ASP n 
1 716 LEU n 
1 717 SER n 
1 718 ARG n 
1 719 LYS n 
1 720 LEU n 
1 721 THR n 
1 722 ARG 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                   722 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 MUC5AC 
_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      'Cricetulus griseus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10029 
_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               'CHO lec 3.2.8.1' 
_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 
CA  non-polymer         . 'CALCIUM ION'   ? 'Ca 2'           40.078  
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 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASP 1   778  ?    ?   ?   A . n 
A 1 2   ALA 2   779  ?    ?   ?   A . n 
A 1 3   ALA 3   780  ?    ?   ?   A . n 
A 1 4   GLN 4   781  ?    ?   ?   A . n 
A 1 5   PRO 5   782  ?    ?   ?   A . n 
A 1 6   ALA 6   783  ?    ?   ?   A . n 
A 1 7   ARG 7   784  ?    ?   ?   A . n 
A 1 8   ARG 8   785  ?    ?   ?   A . n 
A 1 9   ALA 9   786  ?    ?   ?   A . n 
A 1 10  VAL 10  787  ?    ?   ?   A . n 
A 1 11  ARG 11  788  ?    ?   ?   A . n 
A 1 12  SER 12  789  ?    ?   ?   A . n 
A 1 13  SER 13  790  ?    ?   ?   A . n 
A 1 14  ARG 14  791  ?    ?   ?   A . n 
A 1 15  HIS 15  792  ?    ?   ?   A . n 
A 1 16  HIS 16  793  ?    ?   ?   A . n 
A 1 17  HIS 17  794  ?    ?   ?   A . n 
A 1 18  HIS 18  795  ?    ?   ?   A . n 
A 1 19  HIS 19  796  ?    ?   ?   A . n 
A 1 20  HIS 20  797  ?    ?   ?   A . n 
A 1 21  GLY 21  798  ?    ?   ?   A . n 
A 1 22  SER 22  799  ?    ?   ?   A . n 
A 1 23  PRO 23  800  ?    ?   ?   A . n 
A 1 24  VAL 24  801  ?    ?   ?   A . n 
A 1 25  CYS 25  802  ?    ?   ?   A . n 
A 1 26  ALA 26  803  ?    ?   ?   A . n 
A 1 27  ALA 27  804  ?    ?   ?   A . n 
A 1 28  PRO 28  805  ?    ?   ?   A . n 
A 1 29  MET 29  806  ?    ?   ?   A . n 
A 1 30  VAL 30  807  ?    ?   ?   A . n 
A 1 31  PHE 31  808  ?    ?   ?   A . n 
A 1 32  PHE 32  809  ?    ?   ?   A . n 
A 1 33  ASP 33  810  ?    ?   ?   A . n 
A 1 34  CYS 34  811  ?    ?   ?   A . n 
A 1 35  ARG 35  812  ?    ?   ?   A . n 
A 1 36  ASN 36  813  ?    ?   ?   A . n 
A 1 37  ALA 37  814  ?    ?   ?   A . n 
A 1 38  THR 38  815  ?    ?   ?   A . n 
A 1 39  PRO 39  816  ?    ?   ?   A . n 
A 1 40  GLY 40  817  ?    ?   ?   A . n 
A 1 41  ASP 41  818  ?    ?   ?   A . n 
A 1 42  THR 42  819  ?    ?   ?   A . n 
A 1 43  GLY 43  820  ?    ?   ?   A . n 
A 1 44  ALA 44  821  ?    ?   ?   A . n 
A 1 45  GLY 45  822  ?    ?   ?   A . n 
A 1 46  CYS 46  823  ?    ?   ?   A . n 
A 1 47  GLN 47  824  ?    ?   ?   A . n 
A 1 48  LYS 48  825  ?    ?   ?   A . n 
A 1 49  SER 49  826  ?    ?   ?   A . n 
A 1 50  CYS 50  827  ?    ?   ?   A . n 
A 1 51  HIS 51  828  ?    ?   ?   A . n 
A 1 52  THR 52  829  ?    ?   ?   A . n 
A 1 53  LEU 53  830  ?    ?   ?   A . n 
A 1 54  ASP 54  831  ?    ?   ?   A . n 
A 1 55  MET 55  832  ?    ?   ?   A . n 
A 1 56  THR 56  833  ?    ?   ?   A . n 
A 1 57  CYS 57  834  ?    ?   ?   A . n 
A 1 58  TYR 58  835  ?    ?   ?   A . n 
A 1 59  SER 59  836  ?    ?   ?   A . n 
A 1 60  PRO 60  837  ?    ?   ?   A . n 
A 1 61  GLN 61  838  ?    ?   ?   A . n 
A 1 62  CYS 62  839  ?    ?   ?   A . n 
A 1 63  VAL 63  840  ?    ?   ?   A . n 
A 1 64  PRO 64  841  ?    ?   ?   A . n 
A 1 65  GLY 65  842  ?    ?   ?   A . n 
A 1 66  CYS 66  843  ?    ?   ?   A . n 
A 1 67  VAL 67  844  ?    ?   ?   A . n 
A 1 68  CYS 68  845  ?    ?   ?   A . n 
A 1 69  PRO 69  846  ?    ?   ?   A . n 
A 1 70  ASP 70  847  ?    ?   ?   A . n 
A 1 71  GLY 71  848  ?    ?   ?   A . n 
A 1 72  LEU 72  849  ?    ?   ?   A . n 
A 1 73  VAL 73  850  ?    ?   ?   A . n 
A 1 74  ALA 74  851  ?    ?   ?   A . n 
A 1 75  ASP 75  852  ?    ?   ?   A . n 
A 1 76  GLY 76  853  ?    ?   ?   A . n 
A 1 77  GLU 77  854  ?    ?   ?   A . n 
A 1 78  GLY 78  855  ?    ?   ?   A . n 
A 1 79  GLY 79  856  ?    ?   ?   A . n 
A 1 80  CYS 80  857  ?    ?   ?   A . n 
A 1 81  ILE 81  858  ?    ?   ?   A . n 
A 1 82  THR 82  859  ?    ?   ?   A . n 
A 1 83  ALA 83  860  ?    ?   ?   A . n 
A 1 84  GLU 84  861  ?    ?   ?   A . n 
A 1 85  ASP 85  862  ?    ?   ?   A . n 
A 1 86  CYS 86  863  ?    ?   ?   A . n 
A 1 87  PRO 87  864  ?    ?   ?   A . n 
A 1 88  CYS 88  865  ?    ?   ?   A . n 
A 1 89  VAL 89  866  ?    ?   ?   A . n 
A 1 90  HIS 90  867  ?    ?   ?   A . n 
A 1 91  ASN 91  868  ?    ?   ?   A . n 
A 1 92  GLU 92  869  ?    ?   ?   A . n 
A 1 93  ALA 93  870  ?    ?   ?   A . n 
A 1 94  SER 94  871  ?    ?   ?   A . n 
A 1 95  TYR 95  872  ?    ?   ?   A . n 
A 1 96  ARG 96  873  ?    ?   ?   A . n 
A 1 97  ALA 97  874  ?    ?   ?   A . n 
A 1 98  GLY 98  875  ?    ?   ?   A . n 
A 1 99  GLN 99  876  ?    ?   ?   A . n 
A 1 100 THR 100 877  ?    ?   ?   A . n 
A 1 101 ILE 101 878  ?    ?   ?   A . n 
A 1 102 ARG 102 879  ?    ?   ?   A . n 
A 1 103 VAL 103 880  ?    ?   ?   A . n 
A 1 104 GLY 104 881  ?    ?   ?   A . n 
A 1 105 CYS 105 882  ?    ?   ?   A . n 
A 1 106 ASN 106 883  ?    ?   ?   A . n 
A 1 107 THR 107 884  ?    ?   ?   A . n 
A 1 108 CYS 108 885  ?    ?   ?   A . n 
A 1 109 THR 109 886  ?    ?   ?   A . n 
A 1 110 CYS 110 887  ?    ?   ?   A . n 
A 1 111 ASP 111 888  ?    ?   ?   A . n 
A 1 112 SER 112 889  ?    ?   ?   A . n 
A 1 113 ARG 113 890  ?    ?   ?   A . n 
A 1 114 MET 114 891  ?    ?   ?   A . n 
A 1 115 TRP 115 892  ?    ?   ?   A . n 
A 1 116 ARG 116 893  ?    ?   ?   A . n 
A 1 117 CYS 117 894  ?    ?   ?   A . n 
A 1 118 THR 118 895  ?    ?   ?   A . n 
A 1 119 ASP 119 896  ?    ?   ?   A . n 
A 1 120 ASP 120 897  ?    ?   ?   A . n 
A 1 121 PRO 121 898  ?    ?   ?   A . n 
A 1 122 CYS 122 899  899  CYS CYS A . n 
A 1 123 LEU 123 900  900  LEU LEU A . n 
A 1 124 ALA 124 901  901  ALA ALA A . n 
A 1 125 THR 125 902  902  THR THR A . n 
A 1 126 CYS 126 903  903  CYS CYS A . n 
A 1 127 ALA 127 904  904  ALA ALA A . n 
A 1 128 VAL 128 905  905  VAL VAL A . n 
A 1 129 TYR 129 906  906  TYR TYR A . n 
A 1 130 GLY 130 907  907  GLY GLY A . n 
A 1 131 ASP 131 908  908  ASP ASP A . n 
A 1 132 GLY 132 909  909  GLY GLY A . n 
A 1 133 HIS 133 910  910  HIS HIS A . n 
A 1 134 TYR 134 911  911  TYR TYR A . n 
A 1 135 LEU 135 912  912  LEU LEU A . n 
A 1 136 THR 136 913  913  THR THR A . n 
A 1 137 PHE 137 914  914  PHE PHE A . n 
A 1 138 ASP 138 915  915  ASP ASP A . n 
A 1 139 GLY 139 916  916  GLY GLY A . n 
A 1 140 GLN 140 917  917  GLN GLN A . n 
A 1 141 SER 141 918  918  SER SER A . n 
A 1 142 TYR 142 919  919  TYR TYR A . n 
A 1 143 SER 143 920  920  SER SER A . n 
A 1 144 PHE 144 921  921  PHE PHE A . n 
A 1 145 ASN 145 922  922  ASN ASN A . n 
A 1 146 GLY 146 923  923  GLY GLY A . n 
A 1 147 ASP 147 924  924  ASP ASP A . n 
A 1 148 CYS 148 925  925  CYS CYS A . n 
A 1 149 GLU 149 926  926  GLU GLU A . n 
A 1 150 TYR 150 927  927  TYR TYR A . n 
A 1 151 THR 151 928  928  THR THR A . n 
A 1 152 LEU 152 929  929  LEU LEU A . n 
A 1 153 VAL 153 930  930  VAL VAL A . n 
A 1 154 GLN 154 931  931  GLN GLN A . n 
A 1 155 ASN 155 932  932  ASN ASN A . n 
A 1 156 HIS 156 933  933  HIS HIS A . n 
A 1 157 CYS 157 934  934  CYS CYS A . n 
A 1 158 GLY 158 935  935  GLY GLY A . n 
A 1 159 GLY 159 936  936  GLY GLY A . n 
A 1 160 LYS 160 937  937  LYS LYS A . n 
A 1 161 ASP 161 938  938  ASP ASP A . n 
A 1 162 SER 162 939  939  SER SER A . n 
A 1 163 THR 163 940  940  THR THR A . n 
A 1 164 GLN 164 941  941  GLN GLN A . n 
A 1 165 ASP 165 942  942  ASP ASP A . n 
A 1 166 SER 166 943  943  SER SER A . n 
A 1 167 PHE 167 944  944  PHE PHE A . n 
A 1 168 ARG 168 945  945  ARG ARG A . n 
A 1 169 VAL 169 946  946  VAL VAL A . n 
A 1 170 VAL 170 947  947  VAL VAL A . n 
A 1 171 THR 171 948  948  THR THR A . n 
A 1 172 GLU 172 949  949  GLU GLU A . n 
A 1 173 ASN 173 950  950  ASN ASN A . n 
A 1 174 VAL 174 951  951  VAL VAL A . n 
A 1 175 PRO 175 952  952  PRO PRO A . n 
A 1 176 CYS 176 953  953  CYS CYS A . n 
A 1 177 GLY 177 954  954  GLY GLY A . n 
A 1 178 THR 178 955  955  THR THR A . n 
A 1 179 THR 179 956  956  THR THR A . n 
A 1 180 GLY 180 957  957  GLY GLY A . n 
A 1 181 THR 181 958  958  THR THR A . n 
A 1 182 THR 182 959  959  THR THR A . n 
A 1 183 CYS 183 960  960  CYS CYS A . n 
A 1 184 SER 184 961  961  SER SER A . n 
A 1 185 LYS 185 962  962  LYS LYS A . n 
A 1 186 ALA 186 963  963  ALA ALA A . n 
A 1 187 ILE 187 964  964  ILE ILE A . n 
A 1 188 LYS 188 965  965  LYS LYS A . n 
A 1 189 ILE 189 966  966  ILE ILE A . n 
A 1 190 PHE 190 967  967  PHE PHE A . n 
A 1 191 LEU 191 968  968  LEU LEU A . n 
A 1 192 GLY 192 969  969  GLY GLY A . n 
A 1 193 GLY 193 970  970  GLY GLY A . n 
A 1 194 PHE 194 971  971  PHE PHE A . n 
A 1 195 GLU 195 972  972  GLU GLU A . n 
A 1 196 LEU 196 973  973  LEU LEU A . n 
A 1 197 LYS 197 974  974  LYS LYS A . n 
A 1 198 LEU 198 975  975  LEU LEU A . n 
A 1 199 SER 199 976  976  SER SER A . n 
A 1 200 HIS 200 977  977  HIS HIS A . n 
A 1 201 GLY 201 978  978  GLY GLY A . n 
A 1 202 LYS 202 979  979  LYS LYS A . n 
A 1 203 VAL 203 980  980  VAL VAL A . n 
A 1 204 GLU 204 981  981  GLU GLU A . n 
A 1 205 VAL 205 982  982  VAL VAL A . n 
A 1 206 ILE 206 983  983  ILE ILE A . n 
A 1 207 GLY 207 984  984  GLY GLY A . n 
A 1 208 THR 208 985  985  THR THR A . n 
A 1 209 ASP 209 986  986  ASP ASP A . n 
A 1 210 GLU 210 987  987  GLU GLU A . n 
A 1 211 SER 211 988  988  SER SER A . n 
A 1 212 GLN 212 989  989  GLN GLN A . n 
A 1 213 GLU 213 990  990  GLU GLU A . n 
A 1 214 VAL 214 991  991  VAL VAL A . n 
A 1 215 PRO 215 992  992  PRO PRO A . n 
A 1 216 TYR 216 993  993  TYR TYR A . n 
A 1 217 THR 217 994  994  THR THR A . n 
A 1 218 ILE 218 995  995  ILE ILE A . n 
A 1 219 ARG 219 996  996  ARG ARG A . n 
A 1 220 GLN 220 997  997  GLN GLN A . n 
A 1 221 MET 221 998  998  MET MET A . n 
A 1 222 GLY 222 999  999  GLY GLY A . n 
A 1 223 ILE 223 1000 1000 ILE ILE A . n 
A 1 224 TYR 224 1001 1001 TYR TYR A . n 
A 1 225 LEU 225 1002 1002 LEU LEU A . n 
A 1 226 VAL 226 1003 1003 VAL VAL A . n 
A 1 227 VAL 227 1004 1004 VAL VAL A . n 
A 1 228 ASP 228 1005 1005 ASP ASP A . n 
A 1 229 THR 229 1006 1006 THR THR A . n 
A 1 230 ASP 230 1007 1007 ASP ASP A . n 
A 1 231 ILE 231 1008 1008 ILE ILE A . n 
A 1 232 GLY 232 1009 1009 GLY GLY A . n 
A 1 233 LEU 233 1010 1010 LEU LEU A . n 
A 1 234 VAL 234 1011 1011 VAL VAL A . n 
A 1 235 LEU 235 1012 1012 LEU LEU A . n 
A 1 236 LEU 236 1013 1013 LEU LEU A . n 
A 1 237 TRP 237 1014 1014 TRP TRP A . n 
A 1 238 ASP 238 1015 1015 ASP ASP A . n 
A 1 239 LYS 239 1016 1016 LYS LYS A . n 
A 1 240 LYS 240 1017 1017 LYS LYS A . n 
A 1 241 THR 241 1018 1018 THR THR A . n 
A 1 242 SER 242 1019 1019 SER SER A . n 
A 1 243 ILE 243 1020 1020 ILE ILE A . n 
A 1 244 PHE 244 1021 1021 PHE PHE A . n 
A 1 245 ILE 245 1022 1022 ILE ILE A . n 
A 1 246 ASN 246 1023 1023 ASN ASN A . n 
A 1 247 LEU 247 1024 1024 LEU LEU A . n 
A 1 248 SER 248 1025 1025 SER SER A . n 
A 1 249 PRO 249 1026 1026 PRO PRO A . n 
A 1 250 GLU 250 1027 1027 GLU GLU A . n 
A 1 251 PHE 251 1028 1028 PHE PHE A . n 
A 1 252 LYS 252 1029 1029 LYS LYS A . n 
A 1 253 GLY 253 1030 1030 GLY GLY A . n 
A 1 254 ARG 254 1031 1031 ARG ARG A . n 
A 1 255 VAL 255 1032 1032 VAL VAL A . n 
A 1 256 CYS 256 1033 1033 CYS CYS A . n 
A 1 257 GLY 257 1034 1034 GLY GLY A . n 
A 1 258 LEU 258 1035 1035 LEU LEU A . n 
A 1 259 CYS 259 1036 1036 CYS CYS A . n 
A 1 260 GLY 260 1037 1037 GLY GLY A . n 
A 1 261 ASN 261 1038 1038 ASN ASN A . n 
A 1 262 PHE 262 1039 1039 PHE PHE A . n 
A 1 263 ASP 263 1040 1040 ASP ASP A . n 
A 1 264 ASP 264 1041 1041 ASP ASP A . n 
A 1 265 ILE 265 1042 1042 ILE ILE A . n 
A 1 266 ALA 266 1043 1043 ALA ALA A . n 
A 1 267 VAL 267 1044 1044 VAL VAL A . n 
A 1 268 ASN 268 1045 1045 ASN ASN A . n 
A 1 269 ASP 269 1046 1046 ASP ASP A . n 
A 1 270 PHE 270 1047 1047 PHE PHE A . n 
A 1 271 ALA 271 1048 1048 ALA ALA A . n 
A 1 272 THR 272 1049 1049 THR THR A . n 
A 1 273 ARG 273 1050 1050 ARG ARG A . n 
A 1 274 SER 274 1051 1051 SER SER A . n 
A 1 275 ARG 275 1052 1052 ARG ARG A . n 
A 1 276 SER 276 1053 1053 SER SER A . n 
A 1 277 VAL 277 1054 1054 VAL VAL A . n 
A 1 278 VAL 278 1055 1055 VAL VAL A . n 
A 1 279 GLY 279 1056 1056 GLY GLY A . n 
A 1 280 ASP 280 1057 1057 ASP ASP A . n 
A 1 281 VAL 281 1058 1058 VAL VAL A . n 
A 1 282 LEU 282 1059 1059 LEU LEU A . n 
A 1 283 GLU 283 1060 1060 GLU GLU A . n 
A 1 284 PHE 284 1061 1061 PHE PHE A . n 
A 1 285 GLY 285 1062 1062 GLY GLY A . n 
A 1 286 ASN 286 1063 1063 ASN ASN A . n 
A 1 287 SER 287 1064 1064 SER SER A . n 
A 1 288 TRP 288 1065 1065 TRP TRP A . n 
A 1 289 LYS 289 1066 1066 LYS LYS A . n 
A 1 290 LEU 290 1067 1067 LEU LEU A . n 
A 1 291 SER 291 1068 1068 SER SER A . n 
A 1 292 PRO 292 1069 1069 PRO PRO A . n 
A 1 293 SER 293 1070 1070 SER SER A . n 
A 1 294 CYS 294 1071 1071 CYS CYS A . n 
A 1 295 PRO 295 1072 1072 PRO PRO A . n 
A 1 296 ASP 296 1073 1073 ASP ASP A . n 
A 1 297 ALA 297 1074 1074 ALA ALA A . n 
A 1 298 LEU 298 1075 1075 LEU LEU A . n 
A 1 299 ALA 299 1076 1076 ALA ALA A . n 
A 1 300 PRO 300 1077 1077 PRO PRO A . n 
A 1 301 LYS 301 1078 1078 LYS LYS A . n 
A 1 302 ASP 302 1079 1079 ASP ASP A . n 
A 1 303 PRO 303 1080 1080 PRO PRO A . n 
A 1 304 CYS 304 1081 1081 CYS CYS A . n 
A 1 305 THR 305 1082 1082 THR THR A . n 
A 1 306 ALA 306 1083 1083 ALA ALA A . n 
A 1 307 ASN 307 1084 1084 ASN ASN A . n 
A 1 308 PRO 308 1085 1085 PRO PRO A . n 
A 1 309 PHE 309 1086 1086 PHE PHE A . n 
A 1 310 ARG 310 1087 1087 ARG ARG A . n 
A 1 311 LYS 311 1088 1088 LYS LYS A . n 
A 1 312 SER 312 1089 1089 SER SER A . n 
A 1 313 TRP 313 1090 1090 TRP TRP A . n 
A 1 314 ALA 314 1091 1091 ALA ALA A . n 
A 1 315 GLN 315 1092 1092 GLN GLN A . n 
A 1 316 LYS 316 1093 1093 LYS LYS A . n 
A 1 317 GLN 317 1094 1094 GLN GLN A . n 
A 1 318 CYS 318 1095 1095 CYS CYS A . n 
A 1 319 SER 319 1096 1096 SER SER A . n 
A 1 320 ILE 320 1097 1097 ILE ILE A . n 
A 1 321 LEU 321 1098 1098 LEU LEU A . n 
A 1 322 HIS 322 1099 1099 HIS HIS A . n 
A 1 323 GLY 323 1100 1100 GLY GLY A . n 
A 1 324 PRO 324 1101 1101 PRO PRO A . n 
A 1 325 THR 325 1102 1102 THR THR A . n 
A 1 326 PHE 326 1103 1103 PHE PHE A . n 
A 1 327 ALA 327 1104 1104 ALA ALA A . n 
A 1 328 ALA 328 1105 1105 ALA ALA A . n 
A 1 329 CYS 329 1106 1106 CYS CYS A . n 
A 1 330 HIS 330 1107 1107 HIS HIS A . n 
A 1 331 ALA 331 1108 1108 ALA ALA A . n 
A 1 332 HIS 332 1109 1109 HIS HIS A . n 
A 1 333 VAL 333 1110 1110 VAL VAL A . n 
A 1 334 GLU 334 1111 1111 GLU GLU A . n 
A 1 335 PRO 335 1112 1112 PRO PRO A . n 
A 1 336 ALA 336 1113 1113 ALA ALA A . n 
A 1 337 ARG 337 1114 1114 ARG ARG A . n 
A 1 338 TYR 338 1115 1115 TYR TYR A . n 
A 1 339 TYR 339 1116 1116 TYR TYR A . n 
A 1 340 GLU 340 1117 1117 GLU GLU A . n 
A 1 341 ALA 341 1118 1118 ALA ALA A . n 
A 1 342 CYS 342 1119 1119 CYS CYS A . n 
A 1 343 VAL 343 1120 1120 VAL VAL A . n 
A 1 344 ASN 344 1121 1121 ASN ASN A . n 
A 1 345 ASP 345 1122 1122 ASP ASP A . n 
A 1 346 ALA 346 1123 1123 ALA ALA A . n 
A 1 347 CYS 347 1124 1124 CYS CYS A . n 
A 1 348 ALA 348 1125 1125 ALA ALA A . n 
A 1 349 CYS 349 1126 1126 CYS CYS A . n 
A 1 350 ASP 350 1127 1127 ASP ASP A . n 
A 1 351 SER 351 1128 1128 SER SER A . n 
A 1 352 GLY 352 1129 1129 GLY GLY A . n 
A 1 353 GLY 353 1130 1130 GLY GLY A . n 
A 1 354 ASP 354 1131 1131 ASP ASP A . n 
A 1 355 CYS 355 1132 1132 CYS CYS A . n 
A 1 356 GLU 356 1133 1133 GLU GLU A . n 
A 1 357 CYS 357 1134 1134 CYS CYS A . n 
A 1 358 PHE 358 1135 1135 PHE PHE A . n 
A 1 359 CYS 359 1136 1136 CYS CYS A . n 
A 1 360 THR 360 1137 1137 THR THR A . n 
A 1 361 ALA 361 1138 1138 ALA ALA A . n 
A 1 362 VAL 362 1139 1139 VAL VAL A . n 
A 1 363 ALA 363 1140 1140 ALA ALA A . n 
A 1 364 ALA 364 1141 1141 ALA ALA A . n 
A 1 365 TYR 365 1142 1142 TYR TYR A . n 
A 1 366 ALA 366 1143 1143 ALA ALA A . n 
A 1 367 GLN 367 1144 1144 GLN GLN A . n 
A 1 368 ALA 368 1145 1145 ALA ALA A . n 
A 1 369 CYS 369 1146 1146 CYS CYS A . n 
A 1 370 HIS 370 1147 1147 HIS HIS A . n 
A 1 371 GLU 371 1148 1148 GLU GLU A . n 
A 1 372 VAL 372 1149 1149 VAL VAL A . n 
A 1 373 GLY 373 1150 1150 GLY GLY A . n 
A 1 374 LEU 374 1151 1151 LEU LEU A . n 
A 1 375 CYS 375 1152 1152 CYS CYS A . n 
A 1 376 VAL 376 1153 1153 VAL VAL A . n 
A 1 377 SER 377 1154 1154 SER SER A . n 
A 1 378 TRP 378 1155 1155 TRP TRP A . n 
A 1 379 ARG 379 1156 1156 ARG ARG A . n 
A 1 380 THR 380 1157 1157 THR THR A . n 
A 1 381 PRO 381 1158 1158 PRO PRO A . n 
A 1 382 SER 382 1159 1159 SER SER A . n 
A 1 383 ILE 383 1160 1160 ILE ILE A . n 
A 1 384 CYS 384 1161 1161 CYS CYS A . n 
A 1 385 PRO 385 1162 1162 PRO PRO A . n 
A 1 386 LEU 386 1163 1163 LEU LEU A . n 
A 1 387 PHE 387 1164 1164 PHE PHE A . n 
A 1 388 CYS 388 1165 1165 CYS CYS A . n 
A 1 389 ASP 389 1166 1166 ASP ASP A . n 
A 1 390 TYR 390 1167 1167 TYR TYR A . n 
A 1 391 TYR 391 1168 1168 TYR TYR A . n 
A 1 392 ASN 392 1169 1169 ASN ASN A . n 
A 1 393 PRO 393 1170 1170 PRO PRO A . n 
A 1 394 GLU 394 1171 1171 GLU GLU A . n 
A 1 395 GLY 395 1172 1172 GLY GLY A . n 
A 1 396 GLN 396 1173 1173 GLN GLN A . n 
A 1 397 CYS 397 1174 1174 CYS CYS A . n 
A 1 398 GLU 398 1175 1175 GLU GLU A . n 
A 1 399 TRP 399 1176 1176 TRP TRP A . n 
A 1 400 HIS 400 1177 1177 HIS HIS A . n 
A 1 401 TYR 401 1178 1178 TYR TYR A . n 
A 1 402 GLN 402 1179 1179 GLN GLN A . n 
A 1 403 PRO 403 1180 1180 PRO PRO A . n 
A 1 404 CYS 404 1181 1181 CYS CYS A . n 
A 1 405 GLY 405 1182 1182 GLY GLY A . n 
A 1 406 VAL 406 1183 1183 VAL VAL A . n 
A 1 407 PRO 407 1184 1184 PRO PRO A . n 
A 1 408 CYS 408 1185 1185 CYS CYS A . n 
A 1 409 LEU 409 1186 1186 LEU LEU A . n 
A 1 410 ARG 410 1187 1187 ARG ARG A . n 
A 1 411 THR 411 1188 1188 THR THR A . n 
A 1 412 CYS 412 1189 1189 CYS CYS A . n 
A 1 413 ARG 413 1190 1190 ARG ARG A . n 
A 1 414 ASN 414 1191 1191 ASN ASN A . n 
A 1 415 PRO 415 1192 1192 PRO PRO A . n 
A 1 416 ARG 416 1193 1193 ARG ARG A . n 
A 1 417 GLY 417 1194 1194 GLY GLY A . n 
A 1 418 ASP 418 1195 1195 ASP ASP A . n 
A 1 419 CYS 419 1196 1196 CYS CYS A . n 
A 1 420 LEU 420 1197 1197 LEU LEU A . n 
A 1 421 ARG 421 1198 1198 ARG ARG A . n 
A 1 422 ASP 422 1199 1199 ASP ASP A . n 
A 1 423 VAL 423 1200 1200 VAL VAL A . n 
A 1 424 ARG 424 1201 1201 ARG ARG A . n 
A 1 425 GLY 425 1202 1202 GLY GLY A . n 
A 1 426 LEU 426 1203 1203 LEU LEU A . n 
A 1 427 GLU 427 1204 1204 GLU GLU A . n 
A 1 428 GLY 428 1205 1205 GLY GLY A . n 
A 1 429 CYS 429 1206 1206 CYS CYS A . n 
A 1 430 TYR 430 1207 1207 TYR TYR A . n 
A 1 431 PRO 431 1208 1208 PRO PRO A . n 
A 1 432 LYS 432 1209 1209 LYS LYS A . n 
A 1 433 CYS 433 1210 1210 CYS CYS A . n 
A 1 434 PRO 434 1211 1211 PRO PRO A . n 
A 1 435 PRO 435 1212 1212 PRO PRO A . n 
A 1 436 GLU 436 1213 1213 GLU GLU A . n 
A 1 437 ALA 437 1214 1214 ALA ALA A . n 
A 1 438 PRO 438 1215 1215 PRO PRO A . n 
A 1 439 ILE 439 1216 1216 ILE ILE A . n 
A 1 440 PHE 440 1217 1217 PHE PHE A . n 
A 1 441 ASP 441 1218 1218 ASP ASP A . n 
A 1 442 GLU 442 1219 1219 GLU GLU A . n 
A 1 443 ASP 443 1220 1220 ASP ASP A . n 
A 1 444 LYS 444 1221 1221 LYS LYS A . n 
A 1 445 MET 445 1222 1222 MET MET A . n 
A 1 446 GLN 446 1223 1223 GLN GLN A . n 
A 1 447 CYS 447 1224 1224 CYS CYS A . n 
A 1 448 VAL 448 1225 1225 VAL VAL A . n 
A 1 449 ALA 449 1226 1226 ALA ALA A . n 
A 1 450 THR 450 1227 1227 THR THR A . n 
A 1 451 CYS 451 1228 1228 CYS CYS A . n 
A 1 452 PRO 452 1229 1229 PRO PRO A . n 
A 1 453 THR 453 1230 ?    ?   ?   A . n 
A 1 454 PRO 454 1231 ?    ?   ?   A . n 
A 1 455 PRO 455 1232 ?    ?   ?   A . n 
A 1 456 LEU 456 1233 ?    ?   ?   A . n 
A 1 457 PRO 457 1234 ?    ?   ?   A . n 
A 1 458 PRO 458 1235 ?    ?   ?   A . n 
A 1 459 ARG 459 1236 ?    ?   ?   A . n 
A 1 460 CYS 460 1237 ?    ?   ?   A . n 
A 1 461 HIS 461 1238 ?    ?   ?   A . n 
A 1 462 VAL 462 1239 ?    ?   ?   A . n 
A 1 463 HIS 463 1240 ?    ?   ?   A . n 
A 1 464 GLY 464 1241 ?    ?   ?   A . n 
A 1 465 LYS 465 1242 ?    ?   ?   A . n 
A 1 466 SER 466 1243 ?    ?   ?   A . n 
A 1 467 TYR 467 1244 ?    ?   ?   A . n 
A 1 468 ARG 468 1245 ?    ?   ?   A . n 
A 1 469 PRO 469 1246 ?    ?   ?   A . n 
A 1 470 GLY 470 1247 ?    ?   ?   A . n 
A 1 471 ALA 471 1248 ?    ?   ?   A . n 
A 1 472 VAL 472 1249 ?    ?   ?   A . n 
A 1 473 VAL 473 1250 ?    ?   ?   A . n 
A 1 474 PRO 474 1251 ?    ?   ?   A . n 
A 1 475 SER 475 1252 ?    ?   ?   A . n 
A 1 476 ASP 476 1253 ?    ?   ?   A . n 
A 1 477 LYS 477 1254 ?    ?   ?   A . n 
A 1 478 ASN 478 1255 ?    ?   ?   A . n 
A 1 479 CYS 479 1256 ?    ?   ?   A . n 
A 1 480 GLN 480 1257 ?    ?   ?   A . n 
A 1 481 SER 481 1258 ?    ?   ?   A . n 
A 1 482 CYS 482 1259 ?    ?   ?   A . n 
A 1 483 LEU 483 1260 ?    ?   ?   A . n 
A 1 484 CYS 484 1261 ?    ?   ?   A . n 
A 1 485 THR 485 1262 ?    ?   ?   A . n 
A 1 486 GLU 486 1263 ?    ?   ?   A . n 
A 1 487 ARG 487 1264 ?    ?   ?   A . n 
A 1 488 GLY 488 1265 ?    ?   ?   A . n 
A 1 489 VAL 489 1266 ?    ?   ?   A . n 
A 1 490 GLU 490 1267 ?    ?   ?   A . n 
A 1 491 CYS 491 1268 ?    ?   ?   A . n 
A 1 492 THR 492 1269 ?    ?   ?   A . n 
A 1 493 TYR 493 1270 ?    ?   ?   A . n 
A 1 494 LYS 494 1271 ?    ?   ?   A . n 
A 1 495 ALA 495 1272 ?    ?   ?   A . n 
A 1 496 GLU 496 1273 ?    ?   ?   A . n 
A 1 497 ALA 497 1274 ?    ?   ?   A . n 
A 1 498 CYS 498 1275 ?    ?   ?   A . n 
A 1 499 VAL 499 1276 ?    ?   ?   A . n 
A 1 500 CYS 500 1277 ?    ?   ?   A . n 
A 1 501 THR 501 1278 ?    ?   ?   A . n 
A 1 502 TYR 502 1279 ?    ?   ?   A . n 
A 1 503 ASN 503 1280 ?    ?   ?   A . n 
A 1 504 GLY 504 1281 ?    ?   ?   A . n 
A 1 505 GLN 505 1282 ?    ?   ?   A . n 
A 1 506 ARG 506 1283 ?    ?   ?   A . n 
A 1 507 PHE 507 1284 ?    ?   ?   A . n 
A 1 508 HIS 508 1285 ?    ?   ?   A . n 
A 1 509 PRO 509 1286 ?    ?   ?   A . n 
A 1 510 GLY 510 1287 ?    ?   ?   A . n 
A 1 511 ASP 511 1288 ?    ?   ?   A . n 
A 1 512 VAL 512 1289 ?    ?   ?   A . n 
A 1 513 ILE 513 1290 ?    ?   ?   A . n 
A 1 514 TYR 514 1291 ?    ?   ?   A . n 
A 1 515 HIS 515 1292 ?    ?   ?   A . n 
A 1 516 THR 516 1293 ?    ?   ?   A . n 
A 1 517 THR 517 1294 ?    ?   ?   A . n 
A 1 518 ASP 518 1295 ?    ?   ?   A . n 
A 1 519 GLY 519 1296 ?    ?   ?   A . n 
A 1 520 THR 520 1297 ?    ?   ?   A . n 
A 1 521 GLY 521 1298 ?    ?   ?   A . n 
A 1 522 GLY 522 1299 ?    ?   ?   A . n 
A 1 523 CYS 523 1300 ?    ?   ?   A . n 
A 1 524 ILE 524 1301 ?    ?   ?   A . n 
A 1 525 SER 525 1302 ?    ?   ?   A . n 
A 1 526 ALA 526 1303 ?    ?   ?   A . n 
A 1 527 ARG 527 1304 ?    ?   ?   A . n 
A 1 528 CYS 528 1305 ?    ?   ?   A . n 
A 1 529 GLY 529 1306 ?    ?   ?   A . n 
A 1 530 ALA 530 1307 ?    ?   ?   A . n 
A 1 531 ASN 531 1308 ?    ?   ?   A . n 
A 1 532 GLY 532 1309 ?    ?   ?   A . n 
A 1 533 THR 533 1310 ?    ?   ?   A . n 
A 1 534 ILE 534 1311 ?    ?   ?   A . n 
A 1 535 GLU 535 1312 ?    ?   ?   A . n 
A 1 536 ARG 536 1313 ?    ?   ?   A . n 
A 1 537 ARG 537 1314 ?    ?   ?   A . n 
A 1 538 VAL 538 1315 ?    ?   ?   A . n 
A 1 539 TYR 539 1316 ?    ?   ?   A . n 
A 1 540 PRO 540 1317 ?    ?   ?   A . n 
A 1 541 CYS 541 1318 ?    ?   ?   A . n 
A 1 542 SER 542 1319 ?    ?   ?   A . n 
A 1 543 PRO 543 1320 ?    ?   ?   A . n 
A 1 544 THR 544 1321 ?    ?   ?   A . n 
A 1 545 THR 545 1322 ?    ?   ?   A . n 
A 1 546 PRO 546 1323 ?    ?   ?   A . n 
A 1 547 VAL 547 1324 ?    ?   ?   A . n 
A 1 548 PRO 548 1325 ?    ?   ?   A . n 
A 1 549 PRO 549 1326 ?    ?   ?   A . n 
A 1 550 THR 550 1327 ?    ?   ?   A . n 
A 1 551 THR 551 1328 ?    ?   ?   A . n 
A 1 552 PHE 552 1329 ?    ?   ?   A . n 
A 1 553 SER 553 1330 ?    ?   ?   A . n 
A 1 554 PHE 554 1331 ?    ?   ?   A . n 
A 1 555 SER 555 1332 ?    ?   ?   A . n 
A 1 556 THR 556 1333 ?    ?   ?   A . n 
A 1 557 PRO 557 1334 ?    ?   ?   A . n 
A 1 558 PRO 558 1335 ?    ?   ?   A . n 
A 1 559 LEU 559 1336 ?    ?   ?   A . n 
A 1 560 VAL 560 1337 ?    ?   ?   A . n 
A 1 561 VAL 561 1338 ?    ?   ?   A . n 
A 1 562 SER 562 1339 ?    ?   ?   A . n 
A 1 563 SER 563 1340 ?    ?   ?   A . n 
A 1 564 THR 564 1341 ?    ?   ?   A . n 
A 1 565 HIS 565 1342 ?    ?   ?   A . n 
A 1 566 THR 566 1343 ?    ?   ?   A . n 
A 1 567 PRO 567 1344 ?    ?   ?   A . n 
A 1 568 SER 568 1345 ?    ?   ?   A . n 
A 1 569 ASN 569 1346 ?    ?   ?   A . n 
A 1 570 GLY 570 1347 ?    ?   ?   A . n 
A 1 571 PRO 571 1348 ?    ?   ?   A . n 
A 1 572 SER 572 1349 ?    ?   ?   A . n 
A 1 573 SER 573 1350 ?    ?   ?   A . n 
A 1 574 ALA 574 1351 ?    ?   ?   A . n 
A 1 575 HIS 575 1352 ?    ?   ?   A . n 
A 1 576 THR 576 1353 ?    ?   ?   A . n 
A 1 577 GLY 577 1354 ?    ?   ?   A . n 
A 1 578 PRO 578 1355 ?    ?   ?   A . n 
A 1 579 PRO 579 1356 ?    ?   ?   A . n 
A 1 580 SER 580 1357 ?    ?   ?   A . n 
A 1 581 SER 581 1358 ?    ?   ?   A . n 
A 1 582 ALA 582 1359 ?    ?   ?   A . n 
A 1 583 TRP 583 1360 ?    ?   ?   A . n 
A 1 584 PRO 584 1361 ?    ?   ?   A . n 
A 1 585 THR 585 1362 ?    ?   ?   A . n 
A 1 586 THR 586 1363 ?    ?   ?   A . n 
A 1 587 ALA 587 1364 ?    ?   ?   A . n 
A 1 588 GLY 588 1365 ?    ?   ?   A . n 
A 1 589 THR 589 1366 ?    ?   ?   A . n 
A 1 590 SER 590 1367 ?    ?   ?   A . n 
A 1 591 PRO 591 1368 ?    ?   ?   A . n 
A 1 592 ARG 592 1369 ?    ?   ?   A . n 
A 1 593 THR 593 1370 ?    ?   ?   A . n 
A 1 594 ARG 594 1371 ?    ?   ?   A . n 
A 1 595 LEU 595 1372 ?    ?   ?   A . n 
A 1 596 PRO 596 1373 ?    ?   ?   A . n 
A 1 597 THR 597 1374 ?    ?   ?   A . n 
A 1 598 ALA 598 1375 ?    ?   ?   A . n 
A 1 599 SER 599 1376 ?    ?   ?   A . n 
A 1 600 ALA 600 1377 ?    ?   ?   A . n 
A 1 601 SER 601 1378 ?    ?   ?   A . n 
A 1 602 LEU 602 1379 ?    ?   ?   A . n 
A 1 603 PRO 603 1380 ?    ?   ?   A . n 
A 1 604 PRO 604 1381 ?    ?   ?   A . n 
A 1 605 VAL 605 1382 ?    ?   ?   A . n 
A 1 606 CYS 606 1383 ?    ?   ?   A . n 
A 1 607 GLY 607 1384 ?    ?   ?   A . n 
A 1 608 GLU 608 1385 ?    ?   ?   A . n 
A 1 609 LYS 609 1386 ?    ?   ?   A . n 
A 1 610 CYS 610 1387 ?    ?   ?   A . n 
A 1 611 LEU 611 1388 ?    ?   ?   A . n 
A 1 612 TRP 612 1389 ?    ?   ?   A . n 
A 1 613 SER 613 1390 ?    ?   ?   A . n 
A 1 614 PRO 614 1391 ?    ?   ?   A . n 
A 1 615 TRP 615 1392 ?    ?   ?   A . n 
A 1 616 MET 616 1393 ?    ?   ?   A . n 
A 1 617 ASP 617 1394 ?    ?   ?   A . n 
A 1 618 VAL 618 1395 ?    ?   ?   A . n 
A 1 619 SER 619 1396 ?    ?   ?   A . n 
A 1 620 ARG 620 1397 ?    ?   ?   A . n 
A 1 621 PRO 621 1398 ?    ?   ?   A . n 
A 1 622 GLY 622 1399 ?    ?   ?   A . n 
A 1 623 ARG 623 1400 ?    ?   ?   A . n 
A 1 624 GLY 624 1401 ?    ?   ?   A . n 
A 1 625 THR 625 1402 ?    ?   ?   A . n 
A 1 626 ASP 626 1403 ?    ?   ?   A . n 
A 1 627 SER 627 1404 ?    ?   ?   A . n 
A 1 628 GLY 628 1405 ?    ?   ?   A . n 
A 1 629 ASP 629 1406 ?    ?   ?   A . n 
A 1 630 PHE 630 1407 ?    ?   ?   A . n 
A 1 631 ASP 631 1408 ?    ?   ?   A . n 
A 1 632 THR 632 1409 ?    ?   ?   A . n 
A 1 633 LEU 633 1410 ?    ?   ?   A . n 
A 1 634 GLU 634 1411 ?    ?   ?   A . n 
A 1 635 ASN 635 1412 ?    ?   ?   A . n 
A 1 636 LEU 636 1413 ?    ?   ?   A . n 
A 1 637 ARG 637 1414 ?    ?   ?   A . n 
A 1 638 ALA 638 1415 ?    ?   ?   A . n 
A 1 639 HIS 639 1416 ?    ?   ?   A . n 
A 1 640 GLY 640 1417 ?    ?   ?   A . n 
A 1 641 TYR 641 1418 ?    ?   ?   A . n 
A 1 642 ARG 642 1419 ?    ?   ?   A . n 
A 1 643 VAL 643 1420 ?    ?   ?   A . n 
A 1 644 CYS 644 1421 ?    ?   ?   A . n 
A 1 645 GLU 645 1422 ?    ?   ?   A . n 
A 1 646 SER 646 1423 ?    ?   ?   A . n 
A 1 647 PRO 647 1424 ?    ?   ?   A . n 
A 1 648 ARG 648 1425 ?    ?   ?   A . n 
A 1 649 SER 649 1426 ?    ?   ?   A . n 
A 1 650 VAL 650 1427 ?    ?   ?   A . n 
A 1 651 GLU 651 1428 ?    ?   ?   A . n 
A 1 652 CYS 652 1429 ?    ?   ?   A . n 
A 1 653 ARG 653 1430 ?    ?   ?   A . n 
A 1 654 ALA 654 1431 ?    ?   ?   A . n 
A 1 655 GLU 655 1432 ?    ?   ?   A . n 
A 1 656 ASP 656 1433 ?    ?   ?   A . n 
A 1 657 ALA 657 1434 ?    ?   ?   A . n 
A 1 658 PRO 658 1435 ?    ?   ?   A . n 
A 1 659 GLY 659 1436 ?    ?   ?   A . n 
A 1 660 VAL 660 1437 ?    ?   ?   A . n 
A 1 661 PRO 661 1438 ?    ?   ?   A . n 
A 1 662 LEU 662 1439 ?    ?   ?   A . n 
A 1 663 ARG 663 1440 ?    ?   ?   A . n 
A 1 664 ALA 664 1441 ?    ?   ?   A . n 
A 1 665 LEU 665 1442 ?    ?   ?   A . n 
A 1 666 GLY 666 1443 ?    ?   ?   A . n 
A 1 667 GLN 667 1444 ?    ?   ?   A . n 
A 1 668 ARG 668 1445 ?    ?   ?   A . n 
A 1 669 VAL 669 1446 ?    ?   ?   A . n 
A 1 670 GLN 670 1447 ?    ?   ?   A . n 
A 1 671 CYS 671 1448 ?    ?   ?   A . n 
A 1 672 SER 672 1449 ?    ?   ?   A . n 
A 1 673 PRO 673 1450 ?    ?   ?   A . n 
A 1 674 ASP 674 1451 ?    ?   ?   A . n 
A 1 675 VAL 675 1452 ?    ?   ?   A . n 
A 1 676 GLY 676 1453 ?    ?   ?   A . n 
A 1 677 LEU 677 1454 ?    ?   ?   A . n 
A 1 678 THR 678 1455 ?    ?   ?   A . n 
A 1 679 CYS 679 1456 ?    ?   ?   A . n 
A 1 680 ARG 680 1457 ?    ?   ?   A . n 
A 1 681 ASN 681 1458 ?    ?   ?   A . n 
A 1 682 ARG 682 1459 ?    ?   ?   A . n 
A 1 683 GLU 683 1460 ?    ?   ?   A . n 
A 1 684 GLN 684 1461 ?    ?   ?   A . n 
A 1 685 ALA 685 1462 ?    ?   ?   A . n 
A 1 686 SER 686 1463 ?    ?   ?   A . n 
A 1 687 GLY 687 1464 ?    ?   ?   A . n 
A 1 688 LEU 688 1465 ?    ?   ?   A . n 
A 1 689 CYS 689 1466 ?    ?   ?   A . n 
A 1 690 TYR 690 1467 ?    ?   ?   A . n 
A 1 691 ASN 691 1468 ?    ?   ?   A . n 
A 1 692 TYR 692 1469 ?    ?   ?   A . n 
A 1 693 GLN 693 1470 ?    ?   ?   A . n 
A 1 694 ILE 694 1471 ?    ?   ?   A . n 
A 1 695 ARG 695 1472 ?    ?   ?   A . n 
A 1 696 VAL 696 1473 ?    ?   ?   A . n 
A 1 697 GLN 697 1474 ?    ?   ?   A . n 
A 1 698 CYS 698 1475 ?    ?   ?   A . n 
A 1 699 CYS 699 1476 ?    ?   ?   A . n 
A 1 700 THR 700 1477 ?    ?   ?   A . n 
A 1 701 PRO 701 1478 ?    ?   ?   A . n 
A 1 702 LEU 702 1479 ?    ?   ?   A . n 
A 1 703 PRO 703 1480 ?    ?   ?   A . n 
A 1 704 CYS 704 1481 ?    ?   ?   A . n 
A 1 705 THR 705 1482 ?    ?   ?   A . n 
A 1 706 SER 706 1483 ?    ?   ?   A . n 
A 1 707 GLU 707 1484 ?    ?   ?   A . n 
A 1 708 GLN 708 1485 ?    ?   ?   A . n 
A 1 709 LYS 709 1486 ?    ?   ?   A . n 
A 1 710 LEU 710 1487 ?    ?   ?   A . n 
A 1 711 ILE 711 1488 ?    ?   ?   A . n 
A 1 712 SER 712 1489 ?    ?   ?   A . n 
A 1 713 GLU 713 1490 ?    ?   ?   A . n 
A 1 714 GLU 714 1491 ?    ?   ?   A . n 
A 1 715 ASP 715 1492 ?    ?   ?   A . n 
A 1 716 LEU 716 1493 ?    ?   ?   A . n 
A 1 717 SER 717 1494 ?    ?   ?   A . n 
A 1 718 ARG 718 1495 ?    ?   ?   A . n 
A 1 719 LYS 719 1496 ?    ?   ?   A . n 
A 1 720 LEU 720 1497 ?    ?   ?   A . n 
A 1 721 THR 721 1498 ?    ?   ?   A . n 
A 1 722 ARG 722 1499 ?    ?   ?   A . n 
B 1 1   ASP 1   778  ?    ?   ?   B . n 
B 1 2   ALA 2   779  ?    ?   ?   B . n 
B 1 3   ALA 3   780  ?    ?   ?   B . n 
B 1 4   GLN 4   781  ?    ?   ?   B . n 
B 1 5   PRO 5   782  ?    ?   ?   B . n 
B 1 6   ALA 6   783  ?    ?   ?   B . n 
B 1 7   ARG 7   784  ?    ?   ?   B . n 
B 1 8   ARG 8   785  ?    ?   ?   B . n 
B 1 9   ALA 9   786  ?    ?   ?   B . n 
B 1 10  VAL 10  787  ?    ?   ?   B . n 
B 1 11  ARG 11  788  ?    ?   ?   B . n 
B 1 12  SER 12  789  ?    ?   ?   B . n 
B 1 13  SER 13  790  ?    ?   ?   B . n 
B 1 14  ARG 14  791  ?    ?   ?   B . n 
B 1 15  HIS 15  792  ?    ?   ?   B . n 
B 1 16  HIS 16  793  ?    ?   ?   B . n 
B 1 17  HIS 17  794  ?    ?   ?   B . n 
B 1 18  HIS 18  795  ?    ?   ?   B . n 
B 1 19  HIS 19  796  ?    ?   ?   B . n 
B 1 20  HIS 20  797  ?    ?   ?   B . n 
B 1 21  GLY 21  798  ?    ?   ?   B . n 
B 1 22  SER 22  799  ?    ?   ?   B . n 
B 1 23  PRO 23  800  ?    ?   ?   B . n 
B 1 24  VAL 24  801  ?    ?   ?   B . n 
B 1 25  CYS 25  802  ?    ?   ?   B . n 
B 1 26  ALA 26  803  ?    ?   ?   B . n 
B 1 27  ALA 27  804  ?    ?   ?   B . n 
B 1 28  PRO 28  805  ?    ?   ?   B . n 
B 1 29  MET 29  806  ?    ?   ?   B . n 
B 1 30  VAL 30  807  ?    ?   ?   B . n 
B 1 31  PHE 31  808  ?    ?   ?   B . n 
B 1 32  PHE 32  809  ?    ?   ?   B . n 
B 1 33  ASP 33  810  ?    ?   ?   B . n 
B 1 34  CYS 34  811  ?    ?   ?   B . n 
B 1 35  ARG 35  812  ?    ?   ?   B . n 
B 1 36  ASN 36  813  ?    ?   ?   B . n 
B 1 37  ALA 37  814  ?    ?   ?   B . n 
B 1 38  THR 38  815  ?    ?   ?   B . n 
B 1 39  PRO 39  816  ?    ?   ?   B . n 
B 1 40  GLY 40  817  ?    ?   ?   B . n 
B 1 41  ASP 41  818  ?    ?   ?   B . n 
B 1 42  THR 42  819  ?    ?   ?   B . n 
B 1 43  GLY 43  820  ?    ?   ?   B . n 
B 1 44  ALA 44  821  ?    ?   ?   B . n 
B 1 45  GLY 45  822  ?    ?   ?   B . n 
B 1 46  CYS 46  823  ?    ?   ?   B . n 
B 1 47  GLN 47  824  ?    ?   ?   B . n 
B 1 48  LYS 48  825  ?    ?   ?   B . n 
B 1 49  SER 49  826  ?    ?   ?   B . n 
B 1 50  CYS 50  827  ?    ?   ?   B . n 
B 1 51  HIS 51  828  ?    ?   ?   B . n 
B 1 52  THR 52  829  ?    ?   ?   B . n 
B 1 53  LEU 53  830  ?    ?   ?   B . n 
B 1 54  ASP 54  831  ?    ?   ?   B . n 
B 1 55  MET 55  832  ?    ?   ?   B . n 
B 1 56  THR 56  833  ?    ?   ?   B . n 
B 1 57  CYS 57  834  ?    ?   ?   B . n 
B 1 58  TYR 58  835  ?    ?   ?   B . n 
B 1 59  SER 59  836  ?    ?   ?   B . n 
B 1 60  PRO 60  837  ?    ?   ?   B . n 
B 1 61  GLN 61  838  ?    ?   ?   B . n 
B 1 62  CYS 62  839  ?    ?   ?   B . n 
B 1 63  VAL 63  840  ?    ?   ?   B . n 
B 1 64  PRO 64  841  ?    ?   ?   B . n 
B 1 65  GLY 65  842  ?    ?   ?   B . n 
B 1 66  CYS 66  843  ?    ?   ?   B . n 
B 1 67  VAL 67  844  ?    ?   ?   B . n 
B 1 68  CYS 68  845  ?    ?   ?   B . n 
B 1 69  PRO 69  846  ?    ?   ?   B . n 
B 1 70  ASP 70  847  ?    ?   ?   B . n 
B 1 71  GLY 71  848  ?    ?   ?   B . n 
B 1 72  LEU 72  849  ?    ?   ?   B . n 
B 1 73  VAL 73  850  ?    ?   ?   B . n 
B 1 74  ALA 74  851  ?    ?   ?   B . n 
B 1 75  ASP 75  852  ?    ?   ?   B . n 
B 1 76  GLY 76  853  ?    ?   ?   B . n 
B 1 77  GLU 77  854  ?    ?   ?   B . n 
B 1 78  GLY 78  855  ?    ?   ?   B . n 
B 1 79  GLY 79  856  ?    ?   ?   B . n 
B 1 80  CYS 80  857  ?    ?   ?   B . n 
B 1 81  ILE 81  858  ?    ?   ?   B . n 
B 1 82  THR 82  859  ?    ?   ?   B . n 
B 1 83  ALA 83  860  ?    ?   ?   B . n 
B 1 84  GLU 84  861  ?    ?   ?   B . n 
B 1 85  ASP 85  862  ?    ?   ?   B . n 
B 1 86  CYS 86  863  ?    ?   ?   B . n 
B 1 87  PRO 87  864  ?    ?   ?   B . n 
B 1 88  CYS 88  865  ?    ?   ?   B . n 
B 1 89  VAL 89  866  ?    ?   ?   B . n 
B 1 90  HIS 90  867  ?    ?   ?   B . n 
B 1 91  ASN 91  868  ?    ?   ?   B . n 
B 1 92  GLU 92  869  ?    ?   ?   B . n 
B 1 93  ALA 93  870  ?    ?   ?   B . n 
B 1 94  SER 94  871  ?    ?   ?   B . n 
B 1 95  TYR 95  872  ?    ?   ?   B . n 
B 1 96  ARG 96  873  ?    ?   ?   B . n 
B 1 97  ALA 97  874  ?    ?   ?   B . n 
B 1 98  GLY 98  875  ?    ?   ?   B . n 
B 1 99  GLN 99  876  ?    ?   ?   B . n 
B 1 100 THR 100 877  ?    ?   ?   B . n 
B 1 101 ILE 101 878  ?    ?   ?   B . n 
B 1 102 ARG 102 879  ?    ?   ?   B . n 
B 1 103 VAL 103 880  ?    ?   ?   B . n 
B 1 104 GLY 104 881  ?    ?   ?   B . n 
B 1 105 CYS 105 882  ?    ?   ?   B . n 
B 1 106 ASN 106 883  ?    ?   ?   B . n 
B 1 107 THR 107 884  ?    ?   ?   B . n 
B 1 108 CYS 108 885  ?    ?   ?   B . n 
B 1 109 THR 109 886  ?    ?   ?   B . n 
B 1 110 CYS 110 887  ?    ?   ?   B . n 
B 1 111 ASP 111 888  ?    ?   ?   B . n 
B 1 112 SER 112 889  ?    ?   ?   B . n 
B 1 113 ARG 113 890  ?    ?   ?   B . n 
B 1 114 MET 114 891  ?    ?   ?   B . n 
B 1 115 TRP 115 892  ?    ?   ?   B . n 
B 1 116 ARG 116 893  ?    ?   ?   B . n 
B 1 117 CYS 117 894  ?    ?   ?   B . n 
B 1 118 THR 118 895  ?    ?   ?   B . n 
B 1 119 ASP 119 896  ?    ?   ?   B . n 
B 1 120 ASP 120 897  ?    ?   ?   B . n 
B 1 121 PRO 121 898  ?    ?   ?   B . n 
B 1 122 CYS 122 899  899  CYS CYS B . n 
B 1 123 LEU 123 900  900  LEU LEU B . n 
B 1 124 ALA 124 901  901  ALA ALA B . n 
B 1 125 THR 125 902  902  THR THR B . n 
B 1 126 CYS 126 903  903  CYS CYS B . n 
B 1 127 ALA 127 904  904  ALA ALA B . n 
B 1 128 VAL 128 905  905  VAL VAL B . n 
B 1 129 TYR 129 906  906  TYR TYR B . n 
B 1 130 GLY 130 907  907  GLY GLY B . n 
B 1 131 ASP 131 908  908  ASP ASP B . n 
B 1 132 GLY 132 909  909  GLY GLY B . n 
B 1 133 HIS 133 910  910  HIS HIS B . n 
B 1 134 TYR 134 911  911  TYR TYR B . n 
B 1 135 LEU 135 912  912  LEU LEU B . n 
B 1 136 THR 136 913  913  THR THR B . n 
B 1 137 PHE 137 914  914  PHE PHE B . n 
B 1 138 ASP 138 915  915  ASP ASP B . n 
B 1 139 GLY 139 916  916  GLY GLY B . n 
B 1 140 GLN 140 917  917  GLN GLN B . n 
B 1 141 SER 141 918  918  SER SER B . n 
B 1 142 TYR 142 919  919  TYR TYR B . n 
B 1 143 SER 143 920  920  SER SER B . n 
B 1 144 PHE 144 921  921  PHE PHE B . n 
B 1 145 ASN 145 922  922  ASN ASN B . n 
B 1 146 GLY 146 923  923  GLY GLY B . n 
B 1 147 ASP 147 924  924  ASP ASP B . n 
B 1 148 CYS 148 925  925  CYS CYS B . n 
B 1 149 GLU 149 926  926  GLU GLU B . n 
B 1 150 TYR 150 927  927  TYR TYR B . n 
B 1 151 THR 151 928  928  THR THR B . n 
B 1 152 LEU 152 929  929  LEU LEU B . n 
B 1 153 VAL 153 930  930  VAL VAL B . n 
B 1 154 GLN 154 931  931  GLN GLN B . n 
B 1 155 ASN 155 932  932  ASN ASN B . n 
B 1 156 HIS 156 933  933  HIS HIS B . n 
B 1 157 CYS 157 934  934  CYS CYS B . n 
B 1 158 GLY 158 935  935  GLY GLY B . n 
B 1 159 GLY 159 936  936  GLY GLY B . n 
B 1 160 LYS 160 937  937  LYS LYS B . n 
B 1 161 ASP 161 938  938  ASP ASP B . n 
B 1 162 SER 162 939  939  SER SER B . n 
B 1 163 THR 163 940  940  THR THR B . n 
B 1 164 GLN 164 941  941  GLN GLN B . n 
B 1 165 ASP 165 942  942  ASP ASP B . n 
B 1 166 SER 166 943  943  SER SER B . n 
B 1 167 PHE 167 944  944  PHE PHE B . n 
B 1 168 ARG 168 945  945  ARG ARG B . n 
B 1 169 VAL 169 946  946  VAL VAL B . n 
B 1 170 VAL 170 947  947  VAL VAL B . n 
B 1 171 THR 171 948  948  THR THR B . n 
B 1 172 GLU 172 949  949  GLU GLU B . n 
B 1 173 ASN 173 950  950  ASN ASN B . n 
B 1 174 VAL 174 951  951  VAL VAL B . n 
B 1 175 PRO 175 952  952  PRO PRO B . n 
B 1 176 CYS 176 953  953  CYS CYS B . n 
B 1 177 GLY 177 954  954  GLY GLY B . n 
B 1 178 THR 178 955  955  THR THR B . n 
B 1 179 THR 179 956  956  THR THR B . n 
B 1 180 GLY 180 957  957  GLY GLY B . n 
B 1 181 THR 181 958  958  THR THR B . n 
B 1 182 THR 182 959  959  THR THR B . n 
B 1 183 CYS 183 960  960  CYS CYS B . n 
B 1 184 SER 184 961  961  SER SER B . n 
B 1 185 LYS 185 962  962  LYS LYS B . n 
B 1 186 ALA 186 963  963  ALA ALA B . n 
B 1 187 ILE 187 964  964  ILE ILE B . n 
B 1 188 LYS 188 965  965  LYS LYS B . n 
B 1 189 ILE 189 966  966  ILE ILE B . n 
B 1 190 PHE 190 967  967  PHE PHE B . n 
B 1 191 LEU 191 968  968  LEU LEU B . n 
B 1 192 GLY 192 969  969  GLY GLY B . n 
B 1 193 GLY 193 970  970  GLY GLY B . n 
B 1 194 PHE 194 971  971  PHE PHE B . n 
B 1 195 GLU 195 972  972  GLU GLU B . n 
B 1 196 LEU 196 973  973  LEU LEU B . n 
B 1 197 LYS 197 974  974  LYS LYS B . n 
B 1 198 LEU 198 975  975  LEU LEU B . n 
B 1 199 SER 199 976  976  SER SER B . n 
B 1 200 HIS 200 977  977  HIS HIS B . n 
B 1 201 GLY 201 978  978  GLY GLY B . n 
B 1 202 LYS 202 979  979  LYS LYS B . n 
B 1 203 VAL 203 980  980  VAL VAL B . n 
B 1 204 GLU 204 981  981  GLU GLU B . n 
B 1 205 VAL 205 982  982  VAL VAL B . n 
B 1 206 ILE 206 983  983  ILE ILE B . n 
B 1 207 GLY 207 984  984  GLY GLY B . n 
B 1 208 THR 208 985  985  THR THR B . n 
B 1 209 ASP 209 986  986  ASP ASP B . n 
B 1 210 GLU 210 987  987  GLU GLU B . n 
B 1 211 SER 211 988  988  SER SER B . n 
B 1 212 GLN 212 989  989  GLN GLN B . n 
B 1 213 GLU 213 990  990  GLU GLU B . n 
B 1 214 VAL 214 991  991  VAL VAL B . n 
B 1 215 PRO 215 992  992  PRO PRO B . n 
B 1 216 TYR 216 993  993  TYR TYR B . n 
B 1 217 THR 217 994  994  THR THR B . n 
B 1 218 ILE 218 995  995  ILE ILE B . n 
B 1 219 ARG 219 996  996  ARG ARG B . n 
B 1 220 GLN 220 997  997  GLN GLN B . n 
B 1 221 MET 221 998  998  MET MET B . n 
B 1 222 GLY 222 999  999  GLY GLY B . n 
B 1 223 ILE 223 1000 1000 ILE ILE B . n 
B 1 224 TYR 224 1001 1001 TYR TYR B . n 
B 1 225 LEU 225 1002 1002 LEU LEU B . n 
B 1 226 VAL 226 1003 1003 VAL VAL B . n 
B 1 227 VAL 227 1004 1004 VAL VAL B . n 
B 1 228 ASP 228 1005 1005 ASP ASP B . n 
B 1 229 THR 229 1006 1006 THR THR B . n 
B 1 230 ASP 230 1007 1007 ASP ASP B . n 
B 1 231 ILE 231 1008 1008 ILE ILE B . n 
B 1 232 GLY 232 1009 1009 GLY GLY B . n 
B 1 233 LEU 233 1010 1010 LEU LEU B . n 
B 1 234 VAL 234 1011 1011 VAL VAL B . n 
B 1 235 LEU 235 1012 1012 LEU LEU B . n 
B 1 236 LEU 236 1013 1013 LEU LEU B . n 
B 1 237 TRP 237 1014 1014 TRP TRP B . n 
B 1 238 ASP 238 1015 1015 ASP ASP B . n 
B 1 239 LYS 239 1016 1016 LYS LYS B . n 
B 1 240 LYS 240 1017 1017 LYS LYS B . n 
B 1 241 THR 241 1018 1018 THR THR B . n 
B 1 242 SER 242 1019 1019 SER SER B . n 
B 1 243 ILE 243 1020 1020 ILE ILE B . n 
B 1 244 PHE 244 1021 1021 PHE PHE B . n 
B 1 245 ILE 245 1022 1022 ILE ILE B . n 
B 1 246 ASN 246 1023 1023 ASN ASN B . n 
B 1 247 LEU 247 1024 1024 LEU LEU B . n 
B 1 248 SER 248 1025 1025 SER SER B . n 
B 1 249 PRO 249 1026 1026 PRO PRO B . n 
B 1 250 GLU 250 1027 1027 GLU GLU B . n 
B 1 251 PHE 251 1028 1028 PHE PHE B . n 
B 1 252 LYS 252 1029 1029 LYS LYS B . n 
B 1 253 GLY 253 1030 1030 GLY GLY B . n 
B 1 254 ARG 254 1031 1031 ARG ARG B . n 
B 1 255 VAL 255 1032 1032 VAL VAL B . n 
B 1 256 CYS 256 1033 1033 CYS CYS B . n 
B 1 257 GLY 257 1034 1034 GLY GLY B . n 
B 1 258 LEU 258 1035 1035 LEU LEU B . n 
B 1 259 CYS 259 1036 1036 CYS CYS B . n 
B 1 260 GLY 260 1037 1037 GLY GLY B . n 
B 1 261 ASN 261 1038 1038 ASN ASN B . n 
B 1 262 PHE 262 1039 1039 PHE PHE B . n 
B 1 263 ASP 263 1040 1040 ASP ASP B . n 
B 1 264 ASP 264 1041 1041 ASP ASP B . n 
B 1 265 ILE 265 1042 1042 ILE ILE B . n 
B 1 266 ALA 266 1043 1043 ALA ALA B . n 
B 1 267 VAL 267 1044 1044 VAL VAL B . n 
B 1 268 ASN 268 1045 1045 ASN ASN B . n 
B 1 269 ASP 269 1046 1046 ASP ASP B . n 
B 1 270 PHE 270 1047 1047 PHE PHE B . n 
B 1 271 ALA 271 1048 1048 ALA ALA B . n 
B 1 272 THR 272 1049 1049 THR THR B . n 
B 1 273 ARG 273 1050 1050 ARG ARG B . n 
B 1 274 SER 274 1051 1051 SER SER B . n 
B 1 275 ARG 275 1052 1052 ARG ARG B . n 
B 1 276 SER 276 1053 1053 SER SER B . n 
B 1 277 VAL 277 1054 1054 VAL VAL B . n 
B 1 278 VAL 278 1055 1055 VAL VAL B . n 
B 1 279 GLY 279 1056 1056 GLY GLY B . n 
B 1 280 ASP 280 1057 1057 ASP ASP B . n 
B 1 281 VAL 281 1058 1058 VAL VAL B . n 
B 1 282 LEU 282 1059 1059 LEU LEU B . n 
B 1 283 GLU 283 1060 1060 GLU GLU B . n 
B 1 284 PHE 284 1061 1061 PHE PHE B . n 
B 1 285 GLY 285 1062 1062 GLY GLY B . n 
B 1 286 ASN 286 1063 1063 ASN ASN B . n 
B 1 287 SER 287 1064 1064 SER SER B . n 
B 1 288 TRP 288 1065 1065 TRP TRP B . n 
B 1 289 LYS 289 1066 1066 LYS LYS B . n 
B 1 290 LEU 290 1067 1067 LEU LEU B . n 
B 1 291 SER 291 1068 1068 SER SER B . n 
B 1 292 PRO 292 1069 1069 PRO PRO B . n 
B 1 293 SER 293 1070 1070 SER SER B . n 
B 1 294 CYS 294 1071 1071 CYS CYS B . n 
B 1 295 PRO 295 1072 1072 PRO PRO B . n 
B 1 296 ASP 296 1073 1073 ASP ASP B . n 
B 1 297 ALA 297 1074 1074 ALA ALA B . n 
B 1 298 LEU 298 1075 1075 LEU LEU B . n 
B 1 299 ALA 299 1076 1076 ALA ALA B . n 
B 1 300 PRO 300 1077 1077 PRO PRO B . n 
B 1 301 LYS 301 1078 1078 LYS LYS B . n 
B 1 302 ASP 302 1079 1079 ASP ASP B . n 
B 1 303 PRO 303 1080 1080 PRO PRO B . n 
B 1 304 CYS 304 1081 1081 CYS CYS B . n 
B 1 305 THR 305 1082 1082 THR THR B . n 
B 1 306 ALA 306 1083 1083 ALA ALA B . n 
B 1 307 ASN 307 1084 1084 ASN ASN B . n 
B 1 308 PRO 308 1085 1085 PRO PRO B . n 
B 1 309 PHE 309 1086 1086 PHE PHE B . n 
B 1 310 ARG 310 1087 1087 ARG ARG B . n 
B 1 311 LYS 311 1088 1088 LYS LYS B . n 
B 1 312 SER 312 1089 1089 SER SER B . n 
B 1 313 TRP 313 1090 1090 TRP TRP B . n 
B 1 314 ALA 314 1091 1091 ALA ALA B . n 
B 1 315 GLN 315 1092 1092 GLN GLN B . n 
B 1 316 LYS 316 1093 1093 LYS LYS B . n 
B 1 317 GLN 317 1094 1094 GLN GLN B . n 
B 1 318 CYS 318 1095 1095 CYS CYS B . n 
B 1 319 SER 319 1096 1096 SER SER B . n 
B 1 320 ILE 320 1097 1097 ILE ILE B . n 
B 1 321 LEU 321 1098 1098 LEU LEU B . n 
B 1 322 HIS 322 1099 1099 HIS HIS B . n 
B 1 323 GLY 323 1100 1100 GLY GLY B . n 
B 1 324 PRO 324 1101 1101 PRO PRO B . n 
B 1 325 THR 325 1102 1102 THR THR B . n 
B 1 326 PHE 326 1103 1103 PHE PHE B . n 
B 1 327 ALA 327 1104 1104 ALA ALA B . n 
B 1 328 ALA 328 1105 1105 ALA ALA B . n 
B 1 329 CYS 329 1106 1106 CYS CYS B . n 
B 1 330 HIS 330 1107 1107 HIS HIS B . n 
B 1 331 ALA 331 1108 1108 ALA ALA B . n 
B 1 332 HIS 332 1109 1109 HIS HIS B . n 
B 1 333 VAL 333 1110 1110 VAL VAL B . n 
B 1 334 GLU 334 1111 1111 GLU GLU B . n 
B 1 335 PRO 335 1112 1112 PRO PRO B . n 
B 1 336 ALA 336 1113 1113 ALA ALA B . n 
B 1 337 ARG 337 1114 1114 ARG ARG B . n 
B 1 338 TYR 338 1115 1115 TYR TYR B . n 
B 1 339 TYR 339 1116 1116 TYR TYR B . n 
B 1 340 GLU 340 1117 1117 GLU GLU B . n 
B 1 341 ALA 341 1118 1118 ALA ALA B . n 
B 1 342 CYS 342 1119 1119 CYS CYS B . n 
B 1 343 VAL 343 1120 1120 VAL VAL B . n 
B 1 344 ASN 344 1121 1121 ASN ASN B . n 
B 1 345 ASP 345 1122 1122 ASP ASP B . n 
B 1 346 ALA 346 1123 1123 ALA ALA B . n 
B 1 347 CYS 347 1124 1124 CYS CYS B . n 
B 1 348 ALA 348 1125 1125 ALA ALA B . n 
B 1 349 CYS 349 1126 1126 CYS CYS B . n 
B 1 350 ASP 350 1127 1127 ASP ASP B . n 
B 1 351 SER 351 1128 1128 SER SER B . n 
B 1 352 GLY 352 1129 1129 GLY GLY B . n 
B 1 353 GLY 353 1130 1130 GLY GLY B . n 
B 1 354 ASP 354 1131 1131 ASP ASP B . n 
B 1 355 CYS 355 1132 1132 CYS CYS B . n 
B 1 356 GLU 356 1133 1133 GLU GLU B . n 
B 1 357 CYS 357 1134 1134 CYS CYS B . n 
B 1 358 PHE 358 1135 1135 PHE PHE B . n 
B 1 359 CYS 359 1136 1136 CYS CYS B . n 
B 1 360 THR 360 1137 1137 THR THR B . n 
B 1 361 ALA 361 1138 1138 ALA ALA B . n 
B 1 362 VAL 362 1139 1139 VAL VAL B . n 
B 1 363 ALA 363 1140 1140 ALA ALA B . n 
B 1 364 ALA 364 1141 1141 ALA ALA B . n 
B 1 365 TYR 365 1142 1142 TYR TYR B . n 
B 1 366 ALA 366 1143 1143 ALA ALA B . n 
B 1 367 GLN 367 1144 1144 GLN GLN B . n 
B 1 368 ALA 368 1145 1145 ALA ALA B . n 
B 1 369 CYS 369 1146 1146 CYS CYS B . n 
B 1 370 HIS 370 1147 1147 HIS HIS B . n 
B 1 371 GLU 371 1148 1148 GLU GLU B . n 
B 1 372 VAL 372 1149 1149 VAL VAL B . n 
B 1 373 GLY 373 1150 1150 GLY GLY B . n 
B 1 374 LEU 374 1151 1151 LEU LEU B . n 
B 1 375 CYS 375 1152 1152 CYS CYS B . n 
B 1 376 VAL 376 1153 1153 VAL VAL B . n 
B 1 377 SER 377 1154 1154 SER SER B . n 
B 1 378 TRP 378 1155 1155 TRP TRP B . n 
B 1 379 ARG 379 1156 1156 ARG ARG B . n 
B 1 380 THR 380 1157 1157 THR THR B . n 
B 1 381 PRO 381 1158 1158 PRO PRO B . n 
B 1 382 SER 382 1159 1159 SER SER B . n 
B 1 383 ILE 383 1160 1160 ILE ILE B . n 
B 1 384 CYS 384 1161 1161 CYS CYS B . n 
B 1 385 PRO 385 1162 1162 PRO PRO B . n 
B 1 386 LEU 386 1163 1163 LEU LEU B . n 
B 1 387 PHE 387 1164 1164 PHE PHE B . n 
B 1 388 CYS 388 1165 1165 CYS CYS B . n 
B 1 389 ASP 389 1166 1166 ASP ASP B . n 
B 1 390 TYR 390 1167 1167 TYR TYR B . n 
B 1 391 TYR 391 1168 1168 TYR TYR B . n 
B 1 392 ASN 392 1169 1169 ASN ASN B . n 
B 1 393 PRO 393 1170 1170 PRO PRO B . n 
B 1 394 GLU 394 1171 1171 GLU GLU B . n 
B 1 395 GLY 395 1172 1172 GLY GLY B . n 
B 1 396 GLN 396 1173 1173 GLN GLN B . n 
B 1 397 CYS 397 1174 1174 CYS CYS B . n 
B 1 398 GLU 398 1175 1175 GLU GLU B . n 
B 1 399 TRP 399 1176 1176 TRP TRP B . n 
B 1 400 HIS 400 1177 1177 HIS HIS B . n 
B 1 401 TYR 401 1178 1178 TYR TYR B . n 
B 1 402 GLN 402 1179 1179 GLN GLN B . n 
B 1 403 PRO 403 1180 1180 PRO PRO B . n 
B 1 404 CYS 404 1181 1181 CYS CYS B . n 
B 1 405 GLY 405 1182 1182 GLY GLY B . n 
B 1 406 VAL 406 1183 1183 VAL VAL B . n 
B 1 407 PRO 407 1184 1184 PRO PRO B . n 
B 1 408 CYS 408 1185 1185 CYS CYS B . n 
B 1 409 LEU 409 1186 1186 LEU LEU B . n 
B 1 410 ARG 410 1187 1187 ARG ARG B . n 
B 1 411 THR 411 1188 1188 THR THR B . n 
B 1 412 CYS 412 1189 1189 CYS CYS B . n 
B 1 413 ARG 413 1190 1190 ARG ARG B . n 
B 1 414 ASN 414 1191 1191 ASN ASN B . n 
B 1 415 PRO 415 1192 1192 PRO PRO B . n 
B 1 416 ARG 416 1193 1193 ARG ARG B . n 
B 1 417 GLY 417 1194 1194 GLY GLY B . n 
B 1 418 ASP 418 1195 1195 ASP ASP B . n 
B 1 419 CYS 419 1196 1196 CYS CYS B . n 
B 1 420 LEU 420 1197 1197 LEU LEU B . n 
B 1 421 ARG 421 1198 1198 ARG ARG B . n 
B 1 422 ASP 422 1199 1199 ASP ASP B . n 
B 1 423 VAL 423 1200 1200 VAL VAL B . n 
B 1 424 ARG 424 1201 1201 ARG ARG B . n 
B 1 425 GLY 425 1202 1202 GLY GLY B . n 
B 1 426 LEU 426 1203 1203 LEU LEU B . n 
B 1 427 GLU 427 1204 1204 GLU GLU B . n 
B 1 428 GLY 428 1205 1205 GLY GLY B . n 
B 1 429 CYS 429 1206 1206 CYS CYS B . n 
B 1 430 TYR 430 1207 1207 TYR TYR B . n 
B 1 431 PRO 431 1208 1208 PRO PRO B . n 
B 1 432 LYS 432 1209 1209 LYS LYS B . n 
B 1 433 CYS 433 1210 1210 CYS CYS B . n 
B 1 434 PRO 434 1211 1211 PRO PRO B . n 
B 1 435 PRO 435 1212 1212 PRO PRO B . n 
B 1 436 GLU 436 1213 1213 GLU GLU B . n 
B 1 437 ALA 437 1214 1214 ALA ALA B . n 
B 1 438 PRO 438 1215 1215 PRO PRO B . n 
B 1 439 ILE 439 1216 1216 ILE ILE B . n 
B 1 440 PHE 440 1217 1217 PHE PHE B . n 
B 1 441 ASP 441 1218 1218 ASP ASP B . n 
B 1 442 GLU 442 1219 1219 GLU GLU B . n 
B 1 443 ASP 443 1220 1220 ASP ASP B . n 
B 1 444 LYS 444 1221 1221 LYS LYS B . n 
B 1 445 MET 445 1222 1222 MET MET B . n 
B 1 446 GLN 446 1223 1223 GLN GLN B . n 
B 1 447 CYS 447 1224 1224 CYS CYS B . n 
B 1 448 VAL 448 1225 1225 VAL VAL B . n 
B 1 449 ALA 449 1226 1226 ALA ALA B . n 
B 1 450 THR 450 1227 1227 THR THR B . n 
B 1 451 CYS 451 1228 1228 CYS CYS B . n 
B 1 452 PRO 452 1229 1229 PRO PRO B . n 
B 1 453 THR 453 1230 ?    ?   ?   B . n 
B 1 454 PRO 454 1231 ?    ?   ?   B . n 
B 1 455 PRO 455 1232 ?    ?   ?   B . n 
B 1 456 LEU 456 1233 ?    ?   ?   B . n 
B 1 457 PRO 457 1234 ?    ?   ?   B . n 
B 1 458 PRO 458 1235 ?    ?   ?   B . n 
B 1 459 ARG 459 1236 ?    ?   ?   B . n 
B 1 460 CYS 460 1237 ?    ?   ?   B . n 
B 1 461 HIS 461 1238 ?    ?   ?   B . n 
B 1 462 VAL 462 1239 ?    ?   ?   B . n 
B 1 463 HIS 463 1240 ?    ?   ?   B . n 
B 1 464 GLY 464 1241 ?    ?   ?   B . n 
B 1 465 LYS 465 1242 ?    ?   ?   B . n 
B 1 466 SER 466 1243 ?    ?   ?   B . n 
B 1 467 TYR 467 1244 ?    ?   ?   B . n 
B 1 468 ARG 468 1245 ?    ?   ?   B . n 
B 1 469 PRO 469 1246 ?    ?   ?   B . n 
B 1 470 GLY 470 1247 ?    ?   ?   B . n 
B 1 471 ALA 471 1248 ?    ?   ?   B . n 
B 1 472 VAL 472 1249 ?    ?   ?   B . n 
B 1 473 VAL 473 1250 ?    ?   ?   B . n 
B 1 474 PRO 474 1251 ?    ?   ?   B . n 
B 1 475 SER 475 1252 ?    ?   ?   B . n 
B 1 476 ASP 476 1253 ?    ?   ?   B . n 
B 1 477 LYS 477 1254 ?    ?   ?   B . n 
B 1 478 ASN 478 1255 ?    ?   ?   B . n 
B 1 479 CYS 479 1256 ?    ?   ?   B . n 
B 1 480 GLN 480 1257 ?    ?   ?   B . n 
B 1 481 SER 481 1258 ?    ?   ?   B . n 
B 1 482 CYS 482 1259 ?    ?   ?   B . n 
B 1 483 LEU 483 1260 ?    ?   ?   B . n 
B 1 484 CYS 484 1261 ?    ?   ?   B . n 
B 1 485 THR 485 1262 ?    ?   ?   B . n 
B 1 486 GLU 486 1263 ?    ?   ?   B . n 
B 1 487 ARG 487 1264 ?    ?   ?   B . n 
B 1 488 GLY 488 1265 ?    ?   ?   B . n 
B 1 489 VAL 489 1266 ?    ?   ?   B . n 
B 1 490 GLU 490 1267 ?    ?   ?   B . n 
B 1 491 CYS 491 1268 ?    ?   ?   B . n 
B 1 492 THR 492 1269 ?    ?   ?   B . n 
B 1 493 TYR 493 1270 ?    ?   ?   B . n 
B 1 494 LYS 494 1271 ?    ?   ?   B . n 
B 1 495 ALA 495 1272 ?    ?   ?   B . n 
B 1 496 GLU 496 1273 ?    ?   ?   B . n 
B 1 497 ALA 497 1274 ?    ?   ?   B . n 
B 1 498 CYS 498 1275 ?    ?   ?   B . n 
B 1 499 VAL 499 1276 ?    ?   ?   B . n 
B 1 500 CYS 500 1277 ?    ?   ?   B . n 
B 1 501 THR 501 1278 ?    ?   ?   B . n 
B 1 502 TYR 502 1279 ?    ?   ?   B . n 
B 1 503 ASN 503 1280 ?    ?   ?   B . n 
B 1 504 GLY 504 1281 ?    ?   ?   B . n 
B 1 505 GLN 505 1282 ?    ?   ?   B . n 
B 1 506 ARG 506 1283 ?    ?   ?   B . n 
B 1 507 PHE 507 1284 ?    ?   ?   B . n 
B 1 508 HIS 508 1285 ?    ?   ?   B . n 
B 1 509 PRO 509 1286 ?    ?   ?   B . n 
B 1 510 GLY 510 1287 ?    ?   ?   B . n 
B 1 511 ASP 511 1288 ?    ?   ?   B . n 
B 1 512 VAL 512 1289 ?    ?   ?   B . n 
B 1 513 ILE 513 1290 ?    ?   ?   B . n 
B 1 514 TYR 514 1291 ?    ?   ?   B . n 
B 1 515 HIS 515 1292 ?    ?   ?   B . n 
B 1 516 THR 516 1293 ?    ?   ?   B . n 
B 1 517 THR 517 1294 ?    ?   ?   B . n 
B 1 518 ASP 518 1295 ?    ?   ?   B . n 
B 1 519 GLY 519 1296 ?    ?   ?   B . n 
B 1 520 THR 520 1297 ?    ?   ?   B . n 
B 1 521 GLY 521 1298 ?    ?   ?   B . n 
B 1 522 GLY 522 1299 ?    ?   ?   B . n 
B 1 523 CYS 523 1300 ?    ?   ?   B . n 
B 1 524 ILE 524 1301 ?    ?   ?   B . n 
B 1 525 SER 525 1302 ?    ?   ?   B . n 
B 1 526 ALA 526 1303 ?    ?   ?   B . n 
B 1 527 ARG 527 1304 ?    ?   ?   B . n 
B 1 528 CYS 528 1305 ?    ?   ?   B . n 
B 1 529 GLY 529 1306 ?    ?   ?   B . n 
B 1 530 ALA 530 1307 ?    ?   ?   B . n 
B 1 531 ASN 531 1308 ?    ?   ?   B . n 
B 1 532 GLY 532 1309 ?    ?   ?   B . n 
B 1 533 THR 533 1310 ?    ?   ?   B . n 
B 1 534 ILE 534 1311 ?    ?   ?   B . n 
B 1 535 GLU 535 1312 ?    ?   ?   B . n 
B 1 536 ARG 536 1313 ?    ?   ?   B . n 
B 1 537 ARG 537 1314 ?    ?   ?   B . n 
B 1 538 VAL 538 1315 ?    ?   ?   B . n 
B 1 539 TYR 539 1316 ?    ?   ?   B . n 
B 1 540 PRO 540 1317 ?    ?   ?   B . n 
B 1 541 CYS 541 1318 ?    ?   ?   B . n 
B 1 542 SER 542 1319 ?    ?   ?   B . n 
B 1 543 PRO 543 1320 ?    ?   ?   B . n 
B 1 544 THR 544 1321 ?    ?   ?   B . n 
B 1 545 THR 545 1322 ?    ?   ?   B . n 
B 1 546 PRO 546 1323 ?    ?   ?   B . n 
B 1 547 VAL 547 1324 ?    ?   ?   B . n 
B 1 548 PRO 548 1325 ?    ?   ?   B . n 
B 1 549 PRO 549 1326 ?    ?   ?   B . n 
B 1 550 THR 550 1327 ?    ?   ?   B . n 
B 1 551 THR 551 1328 ?    ?   ?   B . n 
B 1 552 PHE 552 1329 ?    ?   ?   B . n 
B 1 553 SER 553 1330 ?    ?   ?   B . n 
B 1 554 PHE 554 1331 ?    ?   ?   B . n 
B 1 555 SER 555 1332 ?    ?   ?   B . n 
B 1 556 THR 556 1333 ?    ?   ?   B . n 
B 1 557 PRO 557 1334 ?    ?   ?   B . n 
B 1 558 PRO 558 1335 ?    ?   ?   B . n 
B 1 559 LEU 559 1336 ?    ?   ?   B . n 
B 1 560 VAL 560 1337 ?    ?   ?   B . n 
B 1 561 VAL 561 1338 ?    ?   ?   B . n 
B 1 562 SER 562 1339 ?    ?   ?   B . n 
B 1 563 SER 563 1340 ?    ?   ?   B . n 
B 1 564 THR 564 1341 ?    ?   ?   B . n 
B 1 565 HIS 565 1342 ?    ?   ?   B . n 
B 1 566 THR 566 1343 ?    ?   ?   B . n 
B 1 567 PRO 567 1344 ?    ?   ?   B . n 
B 1 568 SER 568 1345 ?    ?   ?   B . n 
B 1 569 ASN 569 1346 ?    ?   ?   B . n 
B 1 570 GLY 570 1347 ?    ?   ?   B . n 
B 1 571 PRO 571 1348 ?    ?   ?   B . n 
B 1 572 SER 572 1349 ?    ?   ?   B . n 
B 1 573 SER 573 1350 ?    ?   ?   B . n 
B 1 574 ALA 574 1351 ?    ?   ?   B . n 
B 1 575 HIS 575 1352 ?    ?   ?   B . n 
B 1 576 THR 576 1353 ?    ?   ?   B . n 
B 1 577 GLY 577 1354 ?    ?   ?   B . n 
B 1 578 PRO 578 1355 ?    ?   ?   B . n 
B 1 579 PRO 579 1356 ?    ?   ?   B . n 
B 1 580 SER 580 1357 ?    ?   ?   B . n 
B 1 581 SER 581 1358 ?    ?   ?   B . n 
B 1 582 ALA 582 1359 ?    ?   ?   B . n 
B 1 583 TRP 583 1360 ?    ?   ?   B . n 
B 1 584 PRO 584 1361 ?    ?   ?   B . n 
B 1 585 THR 585 1362 ?    ?   ?   B . n 
B 1 586 THR 586 1363 ?    ?   ?   B . n 
B 1 587 ALA 587 1364 ?    ?   ?   B . n 
B 1 588 GLY 588 1365 ?    ?   ?   B . n 
B 1 589 THR 589 1366 ?    ?   ?   B . n 
B 1 590 SER 590 1367 ?    ?   ?   B . n 
B 1 591 PRO 591 1368 ?    ?   ?   B . n 
B 1 592 ARG 592 1369 ?    ?   ?   B . n 
B 1 593 THR 593 1370 ?    ?   ?   B . n 
B 1 594 ARG 594 1371 ?    ?   ?   B . n 
B 1 595 LEU 595 1372 ?    ?   ?   B . n 
B 1 596 PRO 596 1373 ?    ?   ?   B . n 
B 1 597 THR 597 1374 ?    ?   ?   B . n 
B 1 598 ALA 598 1375 ?    ?   ?   B . n 
B 1 599 SER 599 1376 ?    ?   ?   B . n 
B 1 600 ALA 600 1377 ?    ?   ?   B . n 
B 1 601 SER 601 1378 ?    ?   ?   B . n 
B 1 602 LEU 602 1379 ?    ?   ?   B . n 
B 1 603 PRO 603 1380 ?    ?   ?   B . n 
B 1 604 PRO 604 1381 ?    ?   ?   B . n 
B 1 605 VAL 605 1382 ?    ?   ?   B . n 
B 1 606 CYS 606 1383 ?    ?   ?   B . n 
B 1 607 GLY 607 1384 ?    ?   ?   B . n 
B 1 608 GLU 608 1385 ?    ?   ?   B . n 
B 1 609 LYS 609 1386 ?    ?   ?   B . n 
B 1 610 CYS 610 1387 ?    ?   ?   B . n 
B 1 611 LEU 611 1388 ?    ?   ?   B . n 
B 1 612 TRP 612 1389 ?    ?   ?   B . n 
B 1 613 SER 613 1390 ?    ?   ?   B . n 
B 1 614 PRO 614 1391 ?    ?   ?   B . n 
B 1 615 TRP 615 1392 ?    ?   ?   B . n 
B 1 616 MET 616 1393 ?    ?   ?   B . n 
B 1 617 ASP 617 1394 ?    ?   ?   B . n 
B 1 618 VAL 618 1395 ?    ?   ?   B . n 
B 1 619 SER 619 1396 ?    ?   ?   B . n 
B 1 620 ARG 620 1397 ?    ?   ?   B . n 
B 1 621 PRO 621 1398 ?    ?   ?   B . n 
B 1 622 GLY 622 1399 ?    ?   ?   B . n 
B 1 623 ARG 623 1400 ?    ?   ?   B . n 
B 1 624 GLY 624 1401 ?    ?   ?   B . n 
B 1 625 THR 625 1402 ?    ?   ?   B . n 
B 1 626 ASP 626 1403 ?    ?   ?   B . n 
B 1 627 SER 627 1404 ?    ?   ?   B . n 
B 1 628 GLY 628 1405 ?    ?   ?   B . n 
B 1 629 ASP 629 1406 ?    ?   ?   B . n 
B 1 630 PHE 630 1407 ?    ?   ?   B . n 
B 1 631 ASP 631 1408 ?    ?   ?   B . n 
B 1 632 THR 632 1409 ?    ?   ?   B . n 
B 1 633 LEU 633 1410 ?    ?   ?   B . n 
B 1 634 GLU 634 1411 ?    ?   ?   B . n 
B 1 635 ASN 635 1412 ?    ?   ?   B . n 
B 1 636 LEU 636 1413 ?    ?   ?   B . n 
B 1 637 ARG 637 1414 ?    ?   ?   B . n 
B 1 638 ALA 638 1415 ?    ?   ?   B . n 
B 1 639 HIS 639 1416 ?    ?   ?   B . n 
B 1 640 GLY 640 1417 ?    ?   ?   B . n 
B 1 641 TYR 641 1418 ?    ?   ?   B . n 
B 1 642 ARG 642 1419 ?    ?   ?   B . n 
B 1 643 VAL 643 1420 ?    ?   ?   B . n 
B 1 644 CYS 644 1421 ?    ?   ?   B . n 
B 1 645 GLU 645 1422 ?    ?   ?   B . n 
B 1 646 SER 646 1423 ?    ?   ?   B . n 
B 1 647 PRO 647 1424 ?    ?   ?   B . n 
B 1 648 ARG 648 1425 ?    ?   ?   B . n 
B 1 649 SER 649 1426 ?    ?   ?   B . n 
B 1 650 VAL 650 1427 ?    ?   ?   B . n 
B 1 651 GLU 651 1428 ?    ?   ?   B . n 
B 1 652 CYS 652 1429 ?    ?   ?   B . n 
B 1 653 ARG 653 1430 ?    ?   ?   B . n 
B 1 654 ALA 654 1431 ?    ?   ?   B . n 
B 1 655 GLU 655 1432 ?    ?   ?   B . n 
B 1 656 ASP 656 1433 ?    ?   ?   B . n 
B 1 657 ALA 657 1434 ?    ?   ?   B . n 
B 1 658 PRO 658 1435 ?    ?   ?   B . n 
B 1 659 GLY 659 1436 ?    ?   ?   B . n 
B 1 660 VAL 660 1437 ?    ?   ?   B . n 
B 1 661 PRO 661 1438 ?    ?   ?   B . n 
B 1 662 LEU 662 1439 ?    ?   ?   B . n 
B 1 663 ARG 663 1440 ?    ?   ?   B . n 
B 1 664 ALA 664 1441 ?    ?   ?   B . n 
B 1 665 LEU 665 1442 ?    ?   ?   B . n 
B 1 666 GLY 666 1443 ?    ?   ?   B . n 
B 1 667 GLN 667 1444 ?    ?   ?   B . n 
B 1 668 ARG 668 1445 ?    ?   ?   B . n 
B 1 669 VAL 669 1446 ?    ?   ?   B . n 
B 1 670 GLN 670 1447 ?    ?   ?   B . n 
B 1 671 CYS 671 1448 ?    ?   ?   B . n 
B 1 672 SER 672 1449 ?    ?   ?   B . n 
B 1 673 PRO 673 1450 ?    ?   ?   B . n 
B 1 674 ASP 674 1451 ?    ?   ?   B . n 
B 1 675 VAL 675 1452 ?    ?   ?   B . n 
B 1 676 GLY 676 1453 ?    ?   ?   B . n 
B 1 677 LEU 677 1454 ?    ?   ?   B . n 
B 1 678 THR 678 1455 ?    ?   ?   B . n 
B 1 679 CYS 679 1456 ?    ?   ?   B . n 
B 1 680 ARG 680 1457 ?    ?   ?   B . n 
B 1 681 ASN 681 1458 ?    ?   ?   B . n 
B 1 682 ARG 682 1459 ?    ?   ?   B . n 
B 1 683 GLU 683 1460 ?    ?   ?   B . n 
B 1 684 GLN 684 1461 ?    ?   ?   B . n 
B 1 685 ALA 685 1462 ?    ?   ?   B . n 
B 1 686 SER 686 1463 ?    ?   ?   B . n 
B 1 687 GLY 687 1464 ?    ?   ?   B . n 
B 1 688 LEU 688 1465 ?    ?   ?   B . n 
B 1 689 CYS 689 1466 ?    ?   ?   B . n 
B 1 690 TYR 690 1467 ?    ?   ?   B . n 
B 1 691 ASN 691 1468 ?    ?   ?   B . n 
B 1 692 TYR 692 1469 ?    ?   ?   B . n 
B 1 693 GLN 693 1470 ?    ?   ?   B . n 
B 1 694 ILE 694 1471 ?    ?   ?   B . n 
B 1 695 ARG 695 1472 ?    ?   ?   B . n 
B 1 696 VAL 696 1473 ?    ?   ?   B . n 
B 1 697 GLN 697 1474 ?    ?   ?   B . n 
B 1 698 CYS 698 1475 ?    ?   ?   B . n 
B 1 699 CYS 699 1476 ?    ?   ?   B . n 
B 1 700 THR 700 1477 ?    ?   ?   B . n 
B 1 701 PRO 701 1478 ?    ?   ?   B . n 
B 1 702 LEU 702 1479 ?    ?   ?   B . n 
B 1 703 PRO 703 1480 ?    ?   ?   B . n 
B 1 704 CYS 704 1481 ?    ?   ?   B . n 
B 1 705 THR 705 1482 ?    ?   ?   B . n 
B 1 706 SER 706 1483 ?    ?   ?   B . n 
B 1 707 GLU 707 1484 ?    ?   ?   B . n 
B 1 708 GLN 708 1485 ?    ?   ?   B . n 
B 1 709 LYS 709 1486 ?    ?   ?   B . n 
B 1 710 LEU 710 1487 ?    ?   ?   B . n 
B 1 711 ILE 711 1488 ?    ?   ?   B . n 
B 1 712 SER 712 1489 ?    ?   ?   B . n 
B 1 713 GLU 713 1490 ?    ?   ?   B . n 
B 1 714 GLU 714 1491 ?    ?   ?   B . n 
B 1 715 ASP 715 1492 ?    ?   ?   B . n 
B 1 716 LEU 716 1493 ?    ?   ?   B . n 
B 1 717 SER 717 1494 ?    ?   ?   B . n 
B 1 718 ARG 718 1495 ?    ?   ?   B . n 
B 1 719 LYS 719 1496 ?    ?   ?   B . n 
B 1 720 LEU 720 1497 ?    ?   ?   B . n 
B 1 721 THR 721 1498 ?    ?   ?   B . n 
B 1 722 ARG 722 1499 ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 CA 1 1501 1230 CA CA A . 
D 2 CA 1 1501 1230 CA CA B . 
# 
_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                     8QTV 
_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                         8QTV 
_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                   8QTV 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8QTV 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.002 ? 5184 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.488 ? 7056 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 2.896 ? 712  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041 ? 760  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.003 ? 934  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8QTV 
_struct.title                        
;MUC5AC D'D3CysD1 domains.
;
_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        8QTV 
_struct_keywords.text            'gelforming glycoprotein, Mucin, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MUC5A_HUMAN 
_struct_ref.pdbx_db_accession          P98088 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APVCAAPMVFFDCRNATPGDTGAGCQKSCHTLDMTCYSPQCVPGCVCPDGLVADGEGGCITAEDCPCVHNEASYRAGQTI
RVGCNTCTCDSRMWRCTDDPCLATCAVYGDGHYLTFDGQSYSFNGDCEYTLVQNHCGGKDSTQDSFRVVTENVPCGTTGT
TCSKAIKIFLGGFELKLSHGKVEVIGTDESQEVPYTIRQMGIYLVVDTDIGLVLLWDKKTSIFINLSPEFKGRVCGLCGN
FDDIAVNDFATRSRSVVGDVLEFGNSWKLSPSCPDALAPKDPCTANPFRKSWAQKQCSILHGPTFAACHAHVEPARYYEA
CVNDACACDSGGDCECFCTAVAAYAQACHEVGLCVSWRTPSICPLFCDYYNPEGQCEWHYQPCGVPCLRTCRNPRGDCLR
DVRGLEGCYPKCPPEAPIFDEDKMQCVATCPTPPLPPRCHVHGKSYRPGAVVPSDKNCQSCLCTERGVECTYKAEACVCT
YNGQRFHPGDVIYHTTDGTGGCISARCGANGTIERRVYPCSPTTPVPPTTFSFSTPPLVVSSTHTPSNGPSSAHTGPPSS
AWPTTAGTSPRTRLPTASASLPPVCGEKCLWSPWMDVSRPGRGTDSGDFDTLENLRAHGYRVCESPRSVECRAEDAPGVP
LRALGQRVQCSPDVGLTCRNREQASGLCYNYQIRVQCCTPLPCSTSSS
;
_struct_ref.pdbx_align_begin           799 
# 
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 8QTV A 22 ? 709 ? P98088 799 ? 1486 ? 799 1486 
2 1 8QTV B 22 ? 709 ? P98088 799 ? 1486 ? 799 1486 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8QTV ASP A 1   ? UNP P98088 ?   ?    'expression tag' 778  1  
1 8QTV ALA A 2   ? UNP P98088 ?   ?    'expression tag' 779  2  
1 8QTV ALA A 3   ? UNP P98088 ?   ?    'expression tag' 780  3  
1 8QTV GLN A 4   ? UNP P98088 ?   ?    'expression tag' 781  4  
1 8QTV PRO A 5   ? UNP P98088 ?   ?    'expression tag' 782  5  
1 8QTV ALA A 6   ? UNP P98088 ?   ?    'expression tag' 783  6  
1 8QTV ARG A 7   ? UNP P98088 ?   ?    'expression tag' 784  7  
1 8QTV ARG A 8   ? UNP P98088 ?   ?    'expression tag' 785  8  
1 8QTV ALA A 9   ? UNP P98088 ?   ?    'expression tag' 786  9  
1 8QTV VAL A 10  ? UNP P98088 ?   ?    'expression tag' 787  10 
1 8QTV ARG A 11  ? UNP P98088 ?   ?    'expression tag' 788  11 
1 8QTV SER A 12  ? UNP P98088 ?   ?    'expression tag' 789  12 
1 8QTV SER A 13  ? UNP P98088 ?   ?    'expression tag' 790  13 
1 8QTV ARG A 14  ? UNP P98088 ?   ?    'expression tag' 791  14 
1 8QTV HIS A 15  ? UNP P98088 ?   ?    'expression tag' 792  15 
1 8QTV HIS A 16  ? UNP P98088 ?   ?    'expression tag' 793  16 
1 8QTV HIS A 17  ? UNP P98088 ?   ?    'expression tag' 794  17 
1 8QTV HIS A 18  ? UNP P98088 ?   ?    'expression tag' 795  18 
1 8QTV HIS A 19  ? UNP P98088 ?   ?    'expression tag' 796  19 
1 8QTV HIS A 20  ? UNP P98088 ?   ?    'expression tag' 797  20 
1 8QTV GLY A 21  ? UNP P98088 ?   ?    'expression tag' 798  21 
1 8QTV SER A 22  ? UNP P98088 ALA 799  conflict         799  22 
1 8QTV THR A 705 ? UNP P98088 SER 1482 conflict         1482 23 
1 8QTV SER A 706 ? UNP P98088 THR 1483 conflict         1483 24 
1 8QTV GLU A 707 ? UNP P98088 SER 1484 conflict         1484 25 
1 8QTV GLN A 708 ? UNP P98088 SER 1485 conflict         1485 26 
1 8QTV LYS A 709 ? UNP P98088 SER 1486 conflict         1486 27 
1 8QTV LEU A 710 ? UNP P98088 ?   ?    'expression tag' 1487 28 
1 8QTV ILE A 711 ? UNP P98088 ?   ?    'expression tag' 1488 29 
1 8QTV SER A 712 ? UNP P98088 ?   ?    'expression tag' 1489 30 
1 8QTV GLU A 713 ? UNP P98088 ?   ?    'expression tag' 1490 31 
1 8QTV GLU A 714 ? UNP P98088 ?   ?    'expression tag' 1491 32 
1 8QTV ASP A 715 ? UNP P98088 ?   ?    'expression tag' 1492 33 
1 8QTV LEU A 716 ? UNP P98088 ?   ?    'expression tag' 1493 34 
1 8QTV SER A 717 ? UNP P98088 ?   ?    'expression tag' 1494 35 
1 8QTV ARG A 718 ? UNP P98088 ?   ?    'expression tag' 1495 36 
1 8QTV LYS A 719 ? UNP P98088 ?   ?    'expression tag' 1496 37 
1 8QTV LEU A 720 ? UNP P98088 ?   ?    'expression tag' 1497 38 
1 8QTV THR A 721 ? UNP P98088 ?   ?    'expression tag' 1498 39 
1 8QTV ARG A 722 ? UNP P98088 ?   ?    'expression tag' 1499 40 
2 8QTV ASP B 1   ? UNP P98088 ?   ?    'expression tag' 778  41 
2 8QTV ALA B 2   ? UNP P98088 ?   ?    'expression tag' 779  42 
2 8QTV ALA B 3   ? UNP P98088 ?   ?    'expression tag' 780  43 
2 8QTV GLN B 4   ? UNP P98088 ?   ?    'expression tag' 781  44 
2 8QTV PRO B 5   ? UNP P98088 ?   ?    'expression tag' 782  45 
2 8QTV ALA B 6   ? UNP P98088 ?   ?    'expression tag' 783  46 
2 8QTV ARG B 7   ? UNP P98088 ?   ?    'expression tag' 784  47 
2 8QTV ARG B 8   ? UNP P98088 ?   ?    'expression tag' 785  48 
2 8QTV ALA B 9   ? UNP P98088 ?   ?    'expression tag' 786  49 
2 8QTV VAL B 10  ? UNP P98088 ?   ?    'expression tag' 787  50 
2 8QTV ARG B 11  ? UNP P98088 ?   ?    'expression tag' 788  51 
2 8QTV SER B 12  ? UNP P98088 ?   ?    'expression tag' 789  52 
2 8QTV SER B 13  ? UNP P98088 ?   ?    'expression tag' 790  53 
2 8QTV ARG B 14  ? UNP P98088 ?   ?    'expression tag' 791  54 
2 8QTV HIS B 15  ? UNP P98088 ?   ?    'expression tag' 792  55 
2 8QTV HIS B 16  ? UNP P98088 ?   ?    'expression tag' 793  56 
2 8QTV HIS B 17  ? UNP P98088 ?   ?    'expression tag' 794  57 
2 8QTV HIS B 18  ? UNP P98088 ?   ?    'expression tag' 795  58 
2 8QTV HIS B 19  ? UNP P98088 ?   ?    'expression tag' 796  59 
2 8QTV HIS B 20  ? UNP P98088 ?   ?    'expression tag' 797  60 
2 8QTV GLY B 21  ? UNP P98088 ?   ?    'expression tag' 798  61 
2 8QTV SER B 22  ? UNP P98088 ALA 799  conflict         799  62 
2 8QTV THR B 705 ? UNP P98088 SER 1482 conflict         1482 63 
2 8QTV SER B 706 ? UNP P98088 THR 1483 conflict         1483 64 
2 8QTV GLU B 707 ? UNP P98088 SER 1484 conflict         1484 65 
2 8QTV GLN B 708 ? UNP P98088 SER 1485 conflict         1485 66 
2 8QTV LYS B 709 ? UNP P98088 SER 1486 conflict         1486 67 
2 8QTV LEU B 710 ? UNP P98088 ?   ?    'expression tag' 1487 68 
2 8QTV ILE B 711 ? UNP P98088 ?   ?    'expression tag' 1488 69 
2 8QTV SER B 712 ? UNP P98088 ?   ?    'expression tag' 1489 70 
2 8QTV GLU B 713 ? UNP P98088 ?   ?    'expression tag' 1490 71 
2 8QTV GLU B 714 ? UNP P98088 ?   ?    'expression tag' 1491 72 
2 8QTV ASP B 715 ? UNP P98088 ?   ?    'expression tag' 1492 73 
2 8QTV LEU B 716 ? UNP P98088 ?   ?    'expression tag' 1493 74 
2 8QTV SER B 717 ? UNP P98088 ?   ?    'expression tag' 1494 75 
2 8QTV ARG B 718 ? UNP P98088 ?   ?    'expression tag' 1495 76 
2 8QTV LYS B 719 ? UNP P98088 ?   ?    'expression tag' 1496 77 
2 8QTV LEU B 720 ? UNP P98088 ?   ?    'expression tag' 1497 78 
2 8QTV THR B 721 ? UNP P98088 ?   ?    'expression tag' 1498 79 
2 8QTV ARG B 722 ? UNP P98088 ?   ?    'expression tag' 1499 80 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_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 
# 
_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 PRO A 249 ? LYS A 252 ? PRO A 1026 LYS A 1029 5 ? 4  
HELX_P HELX_P2  AA2 ASP A 280 ? SER A 287 ? ASP A 1057 SER A 1064 1 ? 8  
HELX_P HELX_P3  AA3 ASP A 302 ? ASN A 307 ? ASP A 1079 ASN A 1084 1 ? 6  
HELX_P HELX_P4  AA4 ARG A 310 ? SER A 319 ? ARG A 1087 SER A 1096 1 ? 10 
HELX_P HELX_P5  AA5 ILE A 320 ? THR A 325 ? ILE A 1097 THR A 1102 5 ? 6  
HELX_P HELX_P6  AA6 PHE A 326 ? ALA A 331 ? PHE A 1103 ALA A 1108 1 ? 6  
HELX_P HELX_P7  AA7 PRO A 335 ? CYS A 349 ? PRO A 1112 CYS A 1126 1 ? 15 
HELX_P HELX_P8  AA8 GLY A 353 ? GLY A 373 ? GLY A 1130 GLY A 1150 1 ? 21 
HELX_P HELX_P9  AA9 PRO B 249 ? LYS B 252 ? PRO B 1026 LYS B 1029 5 ? 4  
HELX_P HELX_P10 AB1 ASP B 280 ? SER B 287 ? ASP B 1057 SER B 1064 1 ? 8  
HELX_P HELX_P11 AB2 ASP B 302 ? ASN B 307 ? ASP B 1079 ASN B 1084 1 ? 6  
HELX_P HELX_P12 AB3 ARG B 310 ? SER B 319 ? ARG B 1087 SER B 1096 1 ? 10 
HELX_P HELX_P13 AB4 ILE B 320 ? THR B 325 ? ILE B 1097 THR B 1102 5 ? 6  
HELX_P HELX_P14 AB5 PHE B 326 ? ALA B 331 ? PHE B 1103 ALA B 1108 1 ? 6  
HELX_P HELX_P15 AB6 PRO B 335 ? CYS B 349 ? PRO B 1112 CYS B 1126 1 ? 15 
HELX_P HELX_P16 AB7 GLY B 353 ? GLY B 373 ? GLY B 1130 GLY B 1150 1 ? 21 
# 
_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 126 SG  ? ? ? 1_555 A CYS 259 SG ? ? A CYS 903  A CYS 1036 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2  disulf ? ? A CYS 148 SG  ? ? ? 1_555 A CYS 294 SG ? ? A CYS 925  A CYS 1071 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf3  disulf ? ? A CYS 157 SG  ? ? ? 1_555 A CYS 256 SG ? ? A CYS 934  A CYS 1033 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf4  disulf ? ? A CYS 176 SG  ? ? ? 1_555 A CYS 183 SG ? ? A CYS 953  A CYS 960  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf5  disulf ? ? A CYS 304 SG  ? ? ? 1_555 A CYS 347 SG ? ? A CYS 1081 A CYS 1124 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf6  disulf ? ? A CYS 318 SG  ? ? ? 1_555 A CYS 342 SG ? ? A CYS 1095 A CYS 1119 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf7  disulf ? ? A CYS 329 SG  ? ? ? 1_555 A CYS 369 SG ? ? A CYS 1106 A CYS 1146 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf8  disulf ? ? A CYS 349 SG  ? ? ? 1_555 A CYS 357 SG ? ? A CYS 1126 A CYS 1134 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf9  disulf ? ? A CYS 359 SG  ? ? ? 1_555 A CYS 384 SG ? ? A CYS 1136 A CYS 1161 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf10 disulf ? ? A CYS 375 SG  ? ? ? 1_555 A CYS 404 SG ? ? A CYS 1152 A CYS 1181 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf11 disulf ? ? A CYS 388 SG  ? ? ? 1_555 A CYS 429 SG ? ? A CYS 1165 A CYS 1206 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf12 disulf ? ? A CYS 397 SG  ? ? ? 1_555 B CYS 397 SG ? ? A CYS 1174 B CYS 1174 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf13 disulf ? ? A CYS 408 SG  ? ? ? 1_555 A CYS 419 SG ? ? A CYS 1185 A CYS 1196 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf14 disulf ? ? A CYS 412 SG  ? ? ? 1_555 A CYS 451 SG ? ? A CYS 1189 A CYS 1228 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf15 disulf ? ? A CYS 433 SG  ? ? ? 1_555 A CYS 447 SG ? ? A CYS 1210 A CYS 1224 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf16 disulf ? ? B CYS 126 SG  ? ? ? 1_555 B CYS 259 SG ? ? B CYS 903  B CYS 1036 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf17 disulf ? ? B CYS 148 SG  ? ? ? 1_555 B CYS 294 SG ? ? B CYS 925  B CYS 1071 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf18 disulf ? ? B CYS 157 SG  ? ? ? 1_555 B CYS 256 SG ? ? B CYS 934  B CYS 1033 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf19 disulf ? ? B CYS 176 SG  ? ? ? 1_555 B CYS 183 SG ? ? B CYS 953  B CYS 960  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf20 disulf ? ? B CYS 304 SG  ? ? ? 1_555 B CYS 347 SG ? ? B CYS 1081 B CYS 1124 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf21 disulf ? ? B CYS 318 SG  ? ? ? 1_555 B CYS 342 SG ? ? B CYS 1095 B CYS 1119 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf22 disulf ? ? B CYS 329 SG  ? ? ? 1_555 B CYS 369 SG ? ? B CYS 1106 B CYS 1146 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf23 disulf ? ? B CYS 349 SG  ? ? ? 1_555 B CYS 357 SG ? ? B CYS 1126 B CYS 1134 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf24 disulf ? ? B CYS 359 SG  ? ? ? 1_555 B CYS 384 SG ? ? B CYS 1136 B CYS 1161 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf25 disulf ? ? B CYS 375 SG  ? ? ? 1_555 B CYS 404 SG ? ? B CYS 1152 B CYS 1181 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf26 disulf ? ? B CYS 388 SG  ? ? ? 1_555 B CYS 429 SG ? ? B CYS 1165 B CYS 1206 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf27 disulf ? ? B CYS 408 SG  ? ? ? 1_555 B CYS 419 SG ? ? B CYS 1185 B CYS 1196 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf28 disulf ? ? B CYS 412 SG  ? ? ? 1_555 B CYS 451 SG ? ? B CYS 1189 B CYS 1228 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf29 disulf ? ? B CYS 433 SG  ? ? ? 1_555 B CYS 447 SG ? ? B CYS 1210 B CYS 1224 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc1  metalc ? ? A ASP 138 OD2 ? ? ? 1_555 C CA  .   CA ? ? A ASP 915  A CA  1501 1_555 ? ? ? ? ? ? ? 2.480 ? ? 
metalc2  metalc ? ? A ASN 261 O   ? ? ? 1_555 C CA  .   CA ? ? A ASN 1038 A CA  1501 1_555 ? ? ? ? ? ? ? 3.111 ? ? 
metalc3  metalc ? ? A ASN 261 OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASN 1038 A CA  1501 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc4  metalc ? ? A ASP 263 OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASP 1040 A CA  1501 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc5  metalc ? ? A ILE 265 O   ? ? ? 1_555 C CA  .   CA ? ? A ILE 1042 A CA  1501 1_555 ? ? ? ? ? ? ? 2.524 ? ? 
metalc6  metalc ? ? A ASN 268 OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASN 1045 A CA  1501 1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc7  metalc ? ? A ASP 269 OD1 ? ? ? 1_555 C CA  .   CA ? ? A ASP 1046 A CA  1501 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
metalc8  metalc ? ? B ASP 138 OD2 ? ? ? 1_555 D CA  .   CA ? ? B ASP 915  B CA  1501 1_555 ? ? ? ? ? ? ? 2.481 ? ? 
metalc9  metalc ? ? B ASN 261 O   ? ? ? 1_555 D CA  .   CA ? ? B ASN 1038 B CA  1501 1_555 ? ? ? ? ? ? ? 3.109 ? ? 
metalc10 metalc ? ? B ASN 261 OD1 ? ? ? 1_555 D CA  .   CA ? ? B ASN 1038 B CA  1501 1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc11 metalc ? ? B ASP 263 OD1 ? ? ? 1_555 D CA  .   CA ? ? B ASP 1040 B CA  1501 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc12 metalc ? ? B ILE 265 O   ? ? ? 1_555 D CA  .   CA ? ? B ILE 1042 B CA  1501 1_555 ? ? ? ? ? ? ? 2.525 ? ? 
metalc13 metalc ? ? B ASN 268 OD1 ? ? ? 1_555 D CA  .   CA ? ? B ASN 1045 B CA  1501 1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc14 metalc ? ? B ASP 269 OD1 ? ? ? 1_555 D CA  .   CA ? ? B ASP 1046 B CA  1501 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
# 
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 138 ? A ASP 915  ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 O   ? A ASN 261 ? A ASN 1038 ? 1_555 59.5  ? 
2  OD2 ? A ASP 138 ? A ASP 915  ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASN 261 ? A ASN 1038 ? 1_555 118.9 ? 
3  O   ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASN 261 ? A ASN 1038 ? 1_555 61.8  ? 
4  OD2 ? A ASP 138 ? A ASP 915  ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 263 ? A ASP 1040 ? 1_555 75.2  ? 
5  O   ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 263 ? A ASP 1040 ? 1_555 62.9  ? 
6  OD1 ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 263 ? A ASP 1040 ? 1_555 92.8  ? 
7  OD2 ? A ASP 138 ? A ASP 915  ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 O   ? A ILE 265 ? A ILE 1042 ? 1_555 67.5  ? 
8  O   ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 O   ? A ILE 265 ? A ILE 1042 ? 1_555 123.6 ? 
9  OD1 ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 O   ? A ILE 265 ? A ILE 1042 ? 1_555 173.4 ? 
10 OD1 ? A ASP 263 ? A ASP 1040 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 O   ? A ILE 265 ? A ILE 1042 ? 1_555 87.1  ? 
11 OD2 ? A ASP 138 ? A ASP 915  ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASN 268 ? A ASN 1045 ? 1_555 134.4 ? 
12 O   ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASN 268 ? A ASN 1045 ? 1_555 142.3 ? 
13 OD1 ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASN 268 ? A ASN 1045 ? 1_555 102.7 ? 
14 OD1 ? A ASP 263 ? A ASP 1040 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASN 268 ? A ASN 1045 ? 1_555 85.5  ? 
15 O   ? A ILE 265 ? A ILE 1042 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASN 268 ? A ASN 1045 ? 1_555 70.7  ? 
16 OD2 ? A ASP 138 ? A ASP 915  ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 269 ? A ASP 1046 ? 1_555 74.6  ? 
17 O   ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 269 ? A ASP 1046 ? 1_555 69.8  ? 
18 OD1 ? A ASN 261 ? A ASN 1038 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 269 ? A ASP 1046 ? 1_555 70.9  ? 
19 OD1 ? A ASP 263 ? A ASP 1040 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 269 ? A ASP 1046 ? 1_555 132.1 ? 
20 O   ? A ILE 265 ? A ILE 1042 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 269 ? A ASP 1046 ? 1_555 113.8 ? 
21 OD1 ? A ASN 268 ? A ASN 1045 ? 1_555 CA ? C CA . ? A CA 1501 ? 1_555 OD1 ? A ASP 269 ? A ASP 1046 ? 1_555 141.2 ? 
22 OD2 ? B ASP 138 ? B ASP 915  ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 O   ? B ASN 261 ? B ASN 1038 ? 1_555 59.5  ? 
23 OD2 ? B ASP 138 ? B ASP 915  ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASN 261 ? B ASN 1038 ? 1_555 118.9 ? 
24 O   ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASN 261 ? B ASN 1038 ? 1_555 61.8  ? 
25 OD2 ? B ASP 138 ? B ASP 915  ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 263 ? B ASP 1040 ? 1_555 75.2  ? 
26 O   ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 263 ? B ASP 1040 ? 1_555 62.9  ? 
27 OD1 ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 263 ? B ASP 1040 ? 1_555 92.9  ? 
28 OD2 ? B ASP 138 ? B ASP 915  ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 O   ? B ILE 265 ? B ILE 1042 ? 1_555 67.5  ? 
29 O   ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 O   ? B ILE 265 ? B ILE 1042 ? 1_555 123.6 ? 
30 OD1 ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 O   ? B ILE 265 ? B ILE 1042 ? 1_555 173.4 ? 
31 OD1 ? B ASP 263 ? B ASP 1040 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 O   ? B ILE 265 ? B ILE 1042 ? 1_555 87.1  ? 
32 OD2 ? B ASP 138 ? B ASP 915  ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASN 268 ? B ASN 1045 ? 1_555 134.4 ? 
33 O   ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASN 268 ? B ASN 1045 ? 1_555 142.3 ? 
34 OD1 ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASN 268 ? B ASN 1045 ? 1_555 102.7 ? 
35 OD1 ? B ASP 263 ? B ASP 1040 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASN 268 ? B ASN 1045 ? 1_555 85.5  ? 
36 O   ? B ILE 265 ? B ILE 1042 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASN 268 ? B ASN 1045 ? 1_555 70.7  ? 
37 OD2 ? B ASP 138 ? B ASP 915  ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 269 ? B ASP 1046 ? 1_555 74.6  ? 
38 O   ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 269 ? B ASP 1046 ? 1_555 69.8  ? 
39 OD1 ? B ASN 261 ? B ASN 1038 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 269 ? B ASP 1046 ? 1_555 71.0  ? 
40 OD1 ? B ASP 263 ? B ASP 1040 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 269 ? B ASP 1046 ? 1_555 132.1 ? 
41 O   ? B ILE 265 ? B ILE 1042 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 269 ? B ASP 1046 ? 1_555 113.8 ? 
42 OD1 ? B ASN 268 ? B ASN 1045 ? 1_555 CA ? D CA . ? B CA 1501 ? 1_555 OD1 ? B ASP 269 ? B ASP 1046 ? 1_555 141.2 ? 
# 
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 126 ? CYS A 259 ? CYS A 903  ? 1_555 CYS A 1036 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 148 ? CYS A 294 ? CYS A 925  ? 1_555 CYS A 1071 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 157 ? CYS A 256 ? CYS A 934  ? 1_555 CYS A 1033 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 176 ? CYS A 183 ? CYS A 953  ? 1_555 CYS A 960  ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 304 ? CYS A 347 ? CYS A 1081 ? 1_555 CYS A 1124 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS A 318 ? CYS A 342 ? CYS A 1095 ? 1_555 CYS A 1119 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS A 329 ? CYS A 369 ? CYS A 1106 ? 1_555 CYS A 1146 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS A 349 ? CYS A 357 ? CYS A 1126 ? 1_555 CYS A 1134 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS A 359 ? CYS A 384 ? CYS A 1136 ? 1_555 CYS A 1161 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS A 375 ? CYS A 404 ? CYS A 1152 ? 1_555 CYS A 1181 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS A 388 ? CYS A 429 ? CYS A 1165 ? 1_555 CYS A 1206 ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS A 397 ? CYS B 397 ? CYS A 1174 ? 1_555 CYS B 1174 ? 1_555 SG SG . . . None 'Disulfide bridge' 
13 CYS A 408 ? CYS A 419 ? CYS A 1185 ? 1_555 CYS A 1196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
14 CYS A 412 ? CYS A 451 ? CYS A 1189 ? 1_555 CYS A 1228 ? 1_555 SG SG . . . None 'Disulfide bridge' 
15 CYS A 433 ? CYS A 447 ? CYS A 1210 ? 1_555 CYS A 1224 ? 1_555 SG SG . . . None 'Disulfide bridge' 
16 CYS B 126 ? CYS B 259 ? CYS B 903  ? 1_555 CYS B 1036 ? 1_555 SG SG . . . None 'Disulfide bridge' 
17 CYS B 148 ? CYS B 294 ? CYS B 925  ? 1_555 CYS B 1071 ? 1_555 SG SG . . . None 'Disulfide bridge' 
18 CYS B 157 ? CYS B 256 ? CYS B 934  ? 1_555 CYS B 1033 ? 1_555 SG SG . . . None 'Disulfide bridge' 
19 CYS B 176 ? CYS B 183 ? CYS B 953  ? 1_555 CYS B 960  ? 1_555 SG SG . . . None 'Disulfide bridge' 
20 CYS B 304 ? CYS B 347 ? CYS B 1081 ? 1_555 CYS B 1124 ? 1_555 SG SG . . . None 'Disulfide bridge' 
21 CYS B 318 ? CYS B 342 ? CYS B 1095 ? 1_555 CYS B 1119 ? 1_555 SG SG . . . None 'Disulfide bridge' 
22 CYS B 329 ? CYS B 369 ? CYS B 1106 ? 1_555 CYS B 1146 ? 1_555 SG SG . . . None 'Disulfide bridge' 
23 CYS B 349 ? CYS B 357 ? CYS B 1126 ? 1_555 CYS B 1134 ? 1_555 SG SG . . . None 'Disulfide bridge' 
24 CYS B 359 ? CYS B 384 ? CYS B 1136 ? 1_555 CYS B 1161 ? 1_555 SG SG . . . None 'Disulfide bridge' 
25 CYS B 375 ? CYS B 404 ? CYS B 1152 ? 1_555 CYS B 1181 ? 1_555 SG SG . . . None 'Disulfide bridge' 
26 CYS B 388 ? CYS B 429 ? CYS B 1165 ? 1_555 CYS B 1206 ? 1_555 SG SG . . . None 'Disulfide bridge' 
27 CYS B 408 ? CYS B 419 ? CYS B 1185 ? 1_555 CYS B 1196 ? 1_555 SG SG . . . None 'Disulfide bridge' 
28 CYS B 412 ? CYS B 451 ? CYS B 1189 ? 1_555 CYS B 1228 ? 1_555 SG SG . . . None 'Disulfide bridge' 
29 CYS B 433 ? CYS B 447 ? CYS B 1210 ? 1_555 CYS B 1224 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 7 ? 
AA6 ? 6 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 141 ? SER A 143 ? SER A 918  SER A 920  
AA1 2 HIS A 133 ? LEU A 135 ? HIS A 910  LEU A 912  
AA1 3 ALA A 124 ? TYR A 129 ? ALA A 901  TYR A 906  
AA1 4 ILE A 243 ? LEU A 247 ? ILE A 1020 LEU A 1024 
AA1 5 LEU A 233 ? TRP A 237 ? LEU A 1010 TRP A 1014 
AA1 6 TYR A 224 ? THR A 229 ? TYR A 1001 THR A 1006 
AA1 7 TYR A 216 ? MET A 221 ? TYR A 993  MET A 998  
AA2 1 LYS A 202 ? VAL A 205 ? LYS A 979  VAL A 982  
AA2 2 PHE A 194 ? SER A 199 ? PHE A 971  SER A 976  
AA2 3 THR A 182 ? LEU A 191 ? THR A 959  LEU A 968  
AA2 4 PHE A 167 ? PRO A 175 ? PHE A 944  PRO A 952  
AA2 5 GLU A 149 ? ASN A 155 ? GLU A 926  ASN A 932  
AA2 6 VAL A 255 ? GLY A 257 ? VAL A 1032 GLY A 1034 
AA3 1 TRP A 399 ? GLN A 402 ? TRP A 1176 GLN A 1179 
AA3 2 GLY A 428 ? PRO A 431 ? GLY A 1205 PRO A 1208 
AA4 1 ILE A 439 ? PHE A 440 ? ILE A 1216 PHE A 1217 
AA4 2 CYS A 447 ? VAL A 448 ? CYS A 1224 VAL A 1225 
AA5 1 SER B 141 ? SER B 143 ? SER B 918  SER B 920  
AA5 2 HIS B 133 ? LEU B 135 ? HIS B 910  LEU B 912  
AA5 3 ALA B 124 ? TYR B 129 ? ALA B 901  TYR B 906  
AA5 4 ILE B 243 ? LEU B 247 ? ILE B 1020 LEU B 1024 
AA5 5 LEU B 233 ? TRP B 237 ? LEU B 1010 TRP B 1014 
AA5 6 TYR B 224 ? THR B 229 ? TYR B 1001 THR B 1006 
AA5 7 TYR B 216 ? MET B 221 ? TYR B 993  MET B 998  
AA6 1 LYS B 202 ? VAL B 205 ? LYS B 979  VAL B 982  
AA6 2 PHE B 194 ? SER B 199 ? PHE B 971  SER B 976  
AA6 3 THR B 182 ? LEU B 191 ? THR B 959  LEU B 968  
AA6 4 PHE B 167 ? PRO B 175 ? PHE B 944  PRO B 952  
AA6 5 GLU B 149 ? ASN B 155 ? GLU B 926  ASN B 932  
AA6 6 VAL B 255 ? GLY B 257 ? VAL B 1032 GLY B 1034 
AA7 1 TRP B 399 ? GLN B 402 ? TRP B 1176 GLN B 1179 
AA7 2 GLY B 428 ? PRO B 431 ? GLY B 1205 PRO B 1208 
AA8 1 ILE B 439 ? PHE B 440 ? ILE B 1216 PHE B 1217 
AA8 2 CYS B 447 ? VAL B 448 ? CYS B 1224 VAL B 1225 
# 
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 O TYR A 142 ? O TYR A 919  N TYR A 134 ? N TYR A 911  
AA1 2 3 O HIS A 133 ? O HIS A 910  N TYR A 129 ? N TYR A 906  
AA1 3 4 N CYS A 126 ? N CYS A 903  O ILE A 245 ? O ILE A 1022 
AA1 4 5 O PHE A 244 ? O PHE A 1021 N LEU A 236 ? N LEU A 1013 
AA1 5 6 O TRP A 237 ? O TRP A 1014 N LEU A 225 ? N LEU A 1002 
AA1 6 7 O VAL A 226 ? O VAL A 1003 N ARG A 219 ? N ARG A 996  
AA2 1 2 O GLU A 204 ? O GLU A 981  N LYS A 197 ? N LYS A 974  
AA2 2 3 O PHE A 194 ? O PHE A 971  N LEU A 191 ? N LEU A 968  
AA2 3 4 O LYS A 185 ? O LYS A 962  N GLU A 172 ? N GLU A 949  
AA2 4 5 O PHE A 167 ? O PHE A 944  N ASN A 155 ? N ASN A 932  
AA2 5 6 N GLN A 154 ? N GLN A 931  O CYS A 256 ? O CYS A 1033 
AA3 1 2 N HIS A 400 ? N HIS A 1177 O TYR A 430 ? O TYR A 1207 
AA4 1 2 N ILE A 439 ? N ILE A 1216 O VAL A 448 ? O VAL A 1225 
AA5 1 2 O TYR B 142 ? O TYR B 919  N TYR B 134 ? N TYR B 911  
AA5 2 3 O HIS B 133 ? O HIS B 910  N TYR B 129 ? N TYR B 906  
AA5 3 4 N CYS B 126 ? N CYS B 903  O ILE B 245 ? O ILE B 1022 
AA5 4 5 O PHE B 244 ? O PHE B 1021 N LEU B 236 ? N LEU B 1013 
AA5 5 6 O TRP B 237 ? O TRP B 1014 N LEU B 225 ? N LEU B 1002 
AA5 6 7 O VAL B 226 ? O VAL B 1003 N ARG B 219 ? N ARG B 996  
AA6 1 2 O GLU B 204 ? O GLU B 981  N LYS B 197 ? N LYS B 974  
AA6 2 3 O PHE B 194 ? O PHE B 971  N LEU B 191 ? N LEU B 968  
AA6 3 4 O LYS B 185 ? O LYS B 962  N GLU B 172 ? N GLU B 949  
AA6 4 5 O PHE B 167 ? O PHE B 944  N ASN B 155 ? N ASN B 932  
AA6 5 6 N GLN B 154 ? N GLN B 931  O CYS B 256 ? O CYS B 1033 
AA7 1 2 N HIS B 400 ? N HIS B 1177 O TYR B 430 ? O TYR B 1207 
AA8 1 2 N ILE B 439 ? N ILE B 1216 O VAL B 448 ? O VAL B 1225 
# 
_pdbx_entry_details.entry_id                   8QTV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 CYS A 925  ? ? -172.96 -173.26 
2  1 GLN A 989  ? ? 60.30   -129.19 
3  1 THR A 1018 ? ? -135.90 -41.73  
4  1 ARG A 1050 ? ? 65.16   -1.20   
5  1 PHE A 1103 ? ? -99.34  35.69   
6  1 CYS A 1161 ? ? 52.81   71.07   
7  1 GLU A 1219 ? ? 73.94   -6.41   
8  1 MET A 1222 ? ? 60.94   62.34   
9  1 CYS B 925  ? ? -172.93 -173.27 
10 1 GLN B 989  ? ? 60.23   -129.22 
11 1 THR B 1018 ? ? -135.94 -41.73  
12 1 ARG B 1050 ? ? 65.22   -1.27   
13 1 PHE B 1103 ? ? -99.41  35.73   
14 1 CYS B 1161 ? ? 52.73   71.08   
15 1 GLU B 1219 ? ? 73.93   -6.40   
16 1 MET B 1222 ? ? 60.95   62.38   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8QTV 
_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_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  8QTB 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                8QTB 
_em_3d_fitting_list.initial_refinement_model_id   ? 
# 
_em_3d_reconstruction.entry_id                    8QTV 
_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                  3.25 
_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               216899 
_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            7.4 
# 
_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                 
;MUC5AC D'D3CysD1 domains
;
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_image_scans.entry_id                8QTV 
_em_image_scans.id                      1 
_em_image_scans.number_digital_images   ? 
_em_image_scans.details                 ? 
_em_image_scans.scanner_model           ? 
_em_image_scans.sampling_size           ? 
_em_image_scans.od_range                ? 
_em_image_scans.quant_bit_size          ? 
_em_image_scans.citation_id             ? 
_em_image_scans.dimension_height        ? 
_em_image_scans.dimension_width         ? 
_em_image_scans.frames_per_image        40 
_em_image_scans.image_recording_id      1 
_em_image_scans.used_frames_per_image   ? 
# 
_em_imaging.entry_id                        8QTV 
_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           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_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             750 
_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_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8QTV 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8QTV 
_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 ASP 778  ? A ASP 1   
2   1 Y 1 A ALA 779  ? A ALA 2   
3   1 Y 1 A ALA 780  ? A ALA 3   
4   1 Y 1 A GLN 781  ? A GLN 4   
5   1 Y 1 A PRO 782  ? A PRO 5   
6   1 Y 1 A ALA 783  ? A ALA 6   
7   1 Y 1 A ARG 784  ? A ARG 7   
8   1 Y 1 A ARG 785  ? A ARG 8   
9   1 Y 1 A ALA 786  ? A ALA 9   
10  1 Y 1 A VAL 787  ? A VAL 10  
11  1 Y 1 A ARG 788  ? A ARG 11  
12  1 Y 1 A SER 789  ? A SER 12  
13  1 Y 1 A SER 790  ? A SER 13  
14  1 Y 1 A ARG 791  ? A ARG 14  
15  1 Y 1 A HIS 792  ? A HIS 15  
16  1 Y 1 A HIS 793  ? A HIS 16  
17  1 Y 1 A HIS 794  ? A HIS 17  
18  1 Y 1 A HIS 795  ? A HIS 18  
19  1 Y 1 A HIS 796  ? A HIS 19  
20  1 Y 1 A HIS 797  ? A HIS 20  
21  1 Y 1 A GLY 798  ? A GLY 21  
22  1 Y 1 A SER 799  ? A SER 22  
23  1 Y 1 A PRO 800  ? A PRO 23  
24  1 Y 1 A VAL 801  ? A VAL 24  
25  1 Y 1 A CYS 802  ? A CYS 25  
26  1 Y 1 A ALA 803  ? A ALA 26  
27  1 Y 1 A ALA 804  ? A ALA 27  
28  1 Y 1 A PRO 805  ? A PRO 28  
29  1 Y 1 A MET 806  ? A MET 29  
30  1 Y 1 A VAL 807  ? A VAL 30  
31  1 Y 1 A PHE 808  ? A PHE 31  
32  1 Y 1 A PHE 809  ? A PHE 32  
33  1 Y 1 A ASP 810  ? A ASP 33  
34  1 Y 1 A CYS 811  ? A CYS 34  
35  1 Y 1 A ARG 812  ? A ARG 35  
36  1 Y 1 A ASN 813  ? A ASN 36  
37  1 Y 1 A ALA 814  ? A ALA 37  
38  1 Y 1 A THR 815  ? A THR 38  
39  1 Y 1 A PRO 816  ? A PRO 39  
40  1 Y 1 A GLY 817  ? A GLY 40  
41  1 Y 1 A ASP 818  ? A ASP 41  
42  1 Y 1 A THR 819  ? A THR 42  
43  1 Y 1 A GLY 820  ? A GLY 43  
44  1 Y 1 A ALA 821  ? A ALA 44  
45  1 Y 1 A GLY 822  ? A GLY 45  
46  1 Y 1 A CYS 823  ? A CYS 46  
47  1 Y 1 A GLN 824  ? A GLN 47  
48  1 Y 1 A LYS 825  ? A LYS 48  
49  1 Y 1 A SER 826  ? A SER 49  
50  1 Y 1 A CYS 827  ? A CYS 50  
51  1 Y 1 A HIS 828  ? A HIS 51  
52  1 Y 1 A THR 829  ? A THR 52  
53  1 Y 1 A LEU 830  ? A LEU 53  
54  1 Y 1 A ASP 831  ? A ASP 54  
55  1 Y 1 A MET 832  ? A MET 55  
56  1 Y 1 A THR 833  ? A THR 56  
57  1 Y 1 A CYS 834  ? A CYS 57  
58  1 Y 1 A TYR 835  ? A TYR 58  
59  1 Y 1 A SER 836  ? A SER 59  
60  1 Y 1 A PRO 837  ? A PRO 60  
61  1 Y 1 A GLN 838  ? A GLN 61  
62  1 Y 1 A CYS 839  ? A CYS 62  
63  1 Y 1 A VAL 840  ? A VAL 63  
64  1 Y 1 A PRO 841  ? A PRO 64  
65  1 Y 1 A GLY 842  ? A GLY 65  
66  1 Y 1 A CYS 843  ? A CYS 66  
67  1 Y 1 A VAL 844  ? A VAL 67  
68  1 Y 1 A CYS 845  ? A CYS 68  
69  1 Y 1 A PRO 846  ? A PRO 69  
70  1 Y 1 A ASP 847  ? A ASP 70  
71  1 Y 1 A GLY 848  ? A GLY 71  
72  1 Y 1 A LEU 849  ? A LEU 72  
73  1 Y 1 A VAL 850  ? A VAL 73  
74  1 Y 1 A ALA 851  ? A ALA 74  
75  1 Y 1 A ASP 852  ? A ASP 75  
76  1 Y 1 A GLY 853  ? A GLY 76  
77  1 Y 1 A GLU 854  ? A GLU 77  
78  1 Y 1 A GLY 855  ? A GLY 78  
79  1 Y 1 A GLY 856  ? A GLY 79  
80  1 Y 1 A CYS 857  ? A CYS 80  
81  1 Y 1 A ILE 858  ? A ILE 81  
82  1 Y 1 A THR 859  ? A THR 82  
83  1 Y 1 A ALA 860  ? A ALA 83  
84  1 Y 1 A GLU 861  ? A GLU 84  
85  1 Y 1 A ASP 862  ? A ASP 85  
86  1 Y 1 A CYS 863  ? A CYS 86  
87  1 Y 1 A PRO 864  ? A PRO 87  
88  1 Y 1 A CYS 865  ? A CYS 88  
89  1 Y 1 A VAL 866  ? A VAL 89  
90  1 Y 1 A HIS 867  ? A HIS 90  
91  1 Y 1 A ASN 868  ? A ASN 91  
92  1 Y 1 A GLU 869  ? A GLU 92  
93  1 Y 1 A ALA 870  ? A ALA 93  
94  1 Y 1 A SER 871  ? A SER 94  
95  1 Y 1 A TYR 872  ? A TYR 95  
96  1 Y 1 A ARG 873  ? A ARG 96  
97  1 Y 1 A ALA 874  ? A ALA 97  
98  1 Y 1 A GLY 875  ? A GLY 98  
99  1 Y 1 A GLN 876  ? A GLN 99  
100 1 Y 1 A THR 877  ? A THR 100 
101 1 Y 1 A ILE 878  ? A ILE 101 
102 1 Y 1 A ARG 879  ? A ARG 102 
103 1 Y 1 A VAL 880  ? A VAL 103 
104 1 Y 1 A GLY 881  ? A GLY 104 
105 1 Y 1 A CYS 882  ? A CYS 105 
106 1 Y 1 A ASN 883  ? A ASN 106 
107 1 Y 1 A THR 884  ? A THR 107 
108 1 Y 1 A CYS 885  ? A CYS 108 
109 1 Y 1 A THR 886  ? A THR 109 
110 1 Y 1 A CYS 887  ? A CYS 110 
111 1 Y 1 A ASP 888  ? A ASP 111 
112 1 Y 1 A SER 889  ? A SER 112 
113 1 Y 1 A ARG 890  ? A ARG 113 
114 1 Y 1 A MET 891  ? A MET 114 
115 1 Y 1 A TRP 892  ? A TRP 115 
116 1 Y 1 A ARG 893  ? A ARG 116 
117 1 Y 1 A CYS 894  ? A CYS 117 
118 1 Y 1 A THR 895  ? A THR 118 
119 1 Y 1 A ASP 896  ? A ASP 119 
120 1 Y 1 A ASP 897  ? A ASP 120 
121 1 Y 1 A PRO 898  ? A PRO 121 
122 1 Y 1 A THR 1230 ? A THR 453 
123 1 Y 1 A PRO 1231 ? A PRO 454 
124 1 Y 1 A PRO 1232 ? A PRO 455 
125 1 Y 1 A LEU 1233 ? A LEU 456 
126 1 Y 1 A PRO 1234 ? A PRO 457 
127 1 Y 1 A PRO 1235 ? A PRO 458 
128 1 Y 1 A ARG 1236 ? A ARG 459 
129 1 Y 1 A CYS 1237 ? A CYS 460 
130 1 Y 1 A HIS 1238 ? A HIS 461 
131 1 Y 1 A VAL 1239 ? A VAL 462 
132 1 Y 1 A HIS 1240 ? A HIS 463 
133 1 Y 1 A GLY 1241 ? A GLY 464 
134 1 Y 1 A LYS 1242 ? A LYS 465 
135 1 Y 1 A SER 1243 ? A SER 466 
136 1 Y 1 A TYR 1244 ? A TYR 467 
137 1 Y 1 A ARG 1245 ? A ARG 468 
138 1 Y 1 A PRO 1246 ? A PRO 469 
139 1 Y 1 A GLY 1247 ? A GLY 470 
140 1 Y 1 A ALA 1248 ? A ALA 471 
141 1 Y 1 A VAL 1249 ? A VAL 472 
142 1 Y 1 A VAL 1250 ? A VAL 473 
143 1 Y 1 A PRO 1251 ? A PRO 474 
144 1 Y 1 A SER 1252 ? A SER 475 
145 1 Y 1 A ASP 1253 ? A ASP 476 
146 1 Y 1 A LYS 1254 ? A LYS 477 
147 1 Y 1 A ASN 1255 ? A ASN 478 
148 1 Y 1 A CYS 1256 ? A CYS 479 
149 1 Y 1 A GLN 1257 ? A GLN 480 
150 1 Y 1 A SER 1258 ? A SER 481 
151 1 Y 1 A CYS 1259 ? A CYS 482 
152 1 Y 1 A LEU 1260 ? A LEU 483 
153 1 Y 1 A CYS 1261 ? A CYS 484 
154 1 Y 1 A THR 1262 ? A THR 485 
155 1 Y 1 A GLU 1263 ? A GLU 486 
156 1 Y 1 A ARG 1264 ? A ARG 487 
157 1 Y 1 A GLY 1265 ? A GLY 488 
158 1 Y 1 A VAL 1266 ? A VAL 489 
159 1 Y 1 A GLU 1267 ? A GLU 490 
160 1 Y 1 A CYS 1268 ? A CYS 491 
161 1 Y 1 A THR 1269 ? A THR 492 
162 1 Y 1 A TYR 1270 ? A TYR 493 
163 1 Y 1 A LYS 1271 ? A LYS 494 
164 1 Y 1 A ALA 1272 ? A ALA 495 
165 1 Y 1 A GLU 1273 ? A GLU 496 
166 1 Y 1 A ALA 1274 ? A ALA 497 
167 1 Y 1 A CYS 1275 ? A CYS 498 
168 1 Y 1 A VAL 1276 ? A VAL 499 
169 1 Y 1 A CYS 1277 ? A CYS 500 
170 1 Y 1 A THR 1278 ? A THR 501 
171 1 Y 1 A TYR 1279 ? A TYR 502 
172 1 Y 1 A ASN 1280 ? A ASN 503 
173 1 Y 1 A GLY 1281 ? A GLY 504 
174 1 Y 1 A GLN 1282 ? A GLN 505 
175 1 Y 1 A ARG 1283 ? A ARG 506 
176 1 Y 1 A PHE 1284 ? A PHE 507 
177 1 Y 1 A HIS 1285 ? A HIS 508 
178 1 Y 1 A PRO 1286 ? A PRO 509 
179 1 Y 1 A GLY 1287 ? A GLY 510 
180 1 Y 1 A ASP 1288 ? A ASP 511 
181 1 Y 1 A VAL 1289 ? A VAL 512 
182 1 Y 1 A ILE 1290 ? A ILE 513 
183 1 Y 1 A TYR 1291 ? A TYR 514 
184 1 Y 1 A HIS 1292 ? A HIS 515 
185 1 Y 1 A THR 1293 ? A THR 516 
186 1 Y 1 A THR 1294 ? A THR 517 
187 1 Y 1 A ASP 1295 ? A ASP 518 
188 1 Y 1 A GLY 1296 ? A GLY 519 
189 1 Y 1 A THR 1297 ? A THR 520 
190 1 Y 1 A GLY 1298 ? A GLY 521 
191 1 Y 1 A GLY 1299 ? A GLY 522 
192 1 Y 1 A CYS 1300 ? A CYS 523 
193 1 Y 1 A ILE 1301 ? A ILE 524 
194 1 Y 1 A SER 1302 ? A SER 525 
195 1 Y 1 A ALA 1303 ? A ALA 526 
196 1 Y 1 A ARG 1304 ? A ARG 527 
197 1 Y 1 A CYS 1305 ? A CYS 528 
198 1 Y 1 A GLY 1306 ? A GLY 529 
199 1 Y 1 A ALA 1307 ? A ALA 530 
200 1 Y 1 A ASN 1308 ? A ASN 531 
201 1 Y 1 A GLY 1309 ? A GLY 532 
202 1 Y 1 A THR 1310 ? A THR 533 
203 1 Y 1 A ILE 1311 ? A ILE 534 
204 1 Y 1 A GLU 1312 ? A GLU 535 
205 1 Y 1 A ARG 1313 ? A ARG 536 
206 1 Y 1 A ARG 1314 ? A ARG 537 
207 1 Y 1 A VAL 1315 ? A VAL 538 
208 1 Y 1 A TYR 1316 ? A TYR 539 
209 1 Y 1 A PRO 1317 ? A PRO 540 
210 1 Y 1 A CYS 1318 ? A CYS 541 
211 1 Y 1 A SER 1319 ? A SER 542 
212 1 Y 1 A PRO 1320 ? A PRO 543 
213 1 Y 1 A THR 1321 ? A THR 544 
214 1 Y 1 A THR 1322 ? A THR 545 
215 1 Y 1 A PRO 1323 ? A PRO 546 
216 1 Y 1 A VAL 1324 ? A VAL 547 
217 1 Y 1 A PRO 1325 ? A PRO 548 
218 1 Y 1 A PRO 1326 ? A PRO 549 
219 1 Y 1 A THR 1327 ? A THR 550 
220 1 Y 1 A THR 1328 ? A THR 551 
221 1 Y 1 A PHE 1329 ? A PHE 552 
222 1 Y 1 A SER 1330 ? A SER 553 
223 1 Y 1 A PHE 1331 ? A PHE 554 
224 1 Y 1 A SER 1332 ? A SER 555 
225 1 Y 1 A THR 1333 ? A THR 556 
226 1 Y 1 A PRO 1334 ? A PRO 557 
227 1 Y 1 A PRO 1335 ? A PRO 558 
228 1 Y 1 A LEU 1336 ? A LEU 559 
229 1 Y 1 A VAL 1337 ? A VAL 560 
230 1 Y 1 A VAL 1338 ? A VAL 561 
231 1 Y 1 A SER 1339 ? A SER 562 
232 1 Y 1 A SER 1340 ? A SER 563 
233 1 Y 1 A THR 1341 ? A THR 564 
234 1 Y 1 A HIS 1342 ? A HIS 565 
235 1 Y 1 A THR 1343 ? A THR 566 
236 1 Y 1 A PRO 1344 ? A PRO 567 
237 1 Y 1 A SER 1345 ? A SER 568 
238 1 Y 1 A ASN 1346 ? A ASN 569 
239 1 Y 1 A GLY 1347 ? A GLY 570 
240 1 Y 1 A PRO 1348 ? A PRO 571 
241 1 Y 1 A SER 1349 ? A SER 572 
242 1 Y 1 A SER 1350 ? A SER 573 
243 1 Y 1 A ALA 1351 ? A ALA 574 
244 1 Y 1 A HIS 1352 ? A HIS 575 
245 1 Y 1 A THR 1353 ? A THR 576 
246 1 Y 1 A GLY 1354 ? A GLY 577 
247 1 Y 1 A PRO 1355 ? A PRO 578 
248 1 Y 1 A PRO 1356 ? A PRO 579 
249 1 Y 1 A SER 1357 ? A SER 580 
250 1 Y 1 A SER 1358 ? A SER 581 
251 1 Y 1 A ALA 1359 ? A ALA 582 
252 1 Y 1 A TRP 1360 ? A TRP 583 
253 1 Y 1 A PRO 1361 ? A PRO 584 
254 1 Y 1 A THR 1362 ? A THR 585 
255 1 Y 1 A THR 1363 ? A THR 586 
256 1 Y 1 A ALA 1364 ? A ALA 587 
257 1 Y 1 A GLY 1365 ? A GLY 588 
258 1 Y 1 A THR 1366 ? A THR 589 
259 1 Y 1 A SER 1367 ? A SER 590 
260 1 Y 1 A PRO 1368 ? A PRO 591 
261 1 Y 1 A ARG 1369 ? A ARG 592 
262 1 Y 1 A THR 1370 ? A THR 593 
263 1 Y 1 A ARG 1371 ? A ARG 594 
264 1 Y 1 A LEU 1372 ? A LEU 595 
265 1 Y 1 A PRO 1373 ? A PRO 596 
266 1 Y 1 A THR 1374 ? A THR 597 
267 1 Y 1 A ALA 1375 ? A ALA 598 
268 1 Y 1 A SER 1376 ? A SER 599 
269 1 Y 1 A ALA 1377 ? A ALA 600 
270 1 Y 1 A SER 1378 ? A SER 601 
271 1 Y 1 A LEU 1379 ? A LEU 602 
272 1 Y 1 A PRO 1380 ? A PRO 603 
273 1 Y 1 A PRO 1381 ? A PRO 604 
274 1 Y 1 A VAL 1382 ? A VAL 605 
275 1 Y 1 A CYS 1383 ? A CYS 606 
276 1 Y 1 A GLY 1384 ? A GLY 607 
277 1 Y 1 A GLU 1385 ? A GLU 608 
278 1 Y 1 A LYS 1386 ? A LYS 609 
279 1 Y 1 A CYS 1387 ? A CYS 610 
280 1 Y 1 A LEU 1388 ? A LEU 611 
281 1 Y 1 A TRP 1389 ? A TRP 612 
282 1 Y 1 A SER 1390 ? A SER 613 
283 1 Y 1 A PRO 1391 ? A PRO 614 
284 1 Y 1 A TRP 1392 ? A TRP 615 
285 1 Y 1 A MET 1393 ? A MET 616 
286 1 Y 1 A ASP 1394 ? A ASP 617 
287 1 Y 1 A VAL 1395 ? A VAL 618 
288 1 Y 1 A SER 1396 ? A SER 619 
289 1 Y 1 A ARG 1397 ? A ARG 620 
290 1 Y 1 A PRO 1398 ? A PRO 621 
291 1 Y 1 A GLY 1399 ? A GLY 622 
292 1 Y 1 A ARG 1400 ? A ARG 623 
293 1 Y 1 A GLY 1401 ? A GLY 624 
294 1 Y 1 A THR 1402 ? A THR 625 
295 1 Y 1 A ASP 1403 ? A ASP 626 
296 1 Y 1 A SER 1404 ? A SER 627 
297 1 Y 1 A GLY 1405 ? A GLY 628 
298 1 Y 1 A ASP 1406 ? A ASP 629 
299 1 Y 1 A PHE 1407 ? A PHE 630 
300 1 Y 1 A ASP 1408 ? A ASP 631 
301 1 Y 1 A THR 1409 ? A THR 632 
302 1 Y 1 A LEU 1410 ? A LEU 633 
303 1 Y 1 A GLU 1411 ? A GLU 634 
304 1 Y 1 A ASN 1412 ? A ASN 635 
305 1 Y 1 A LEU 1413 ? A LEU 636 
306 1 Y 1 A ARG 1414 ? A ARG 637 
307 1 Y 1 A ALA 1415 ? A ALA 638 
308 1 Y 1 A HIS 1416 ? A HIS 639 
309 1 Y 1 A GLY 1417 ? A GLY 640 
310 1 Y 1 A TYR 1418 ? A TYR 641 
311 1 Y 1 A ARG 1419 ? A ARG 642 
312 1 Y 1 A VAL 1420 ? A VAL 643 
313 1 Y 1 A CYS 1421 ? A CYS 644 
314 1 Y 1 A GLU 1422 ? A GLU 645 
315 1 Y 1 A SER 1423 ? A SER 646 
316 1 Y 1 A PRO 1424 ? A PRO 647 
317 1 Y 1 A ARG 1425 ? A ARG 648 
318 1 Y 1 A SER 1426 ? A SER 649 
319 1 Y 1 A VAL 1427 ? A VAL 650 
320 1 Y 1 A GLU 1428 ? A GLU 651 
321 1 Y 1 A CYS 1429 ? A CYS 652 
322 1 Y 1 A ARG 1430 ? A ARG 653 
323 1 Y 1 A ALA 1431 ? A ALA 654 
324 1 Y 1 A GLU 1432 ? A GLU 655 
325 1 Y 1 A ASP 1433 ? A ASP 656 
326 1 Y 1 A ALA 1434 ? A ALA 657 
327 1 Y 1 A PRO 1435 ? A PRO 658 
328 1 Y 1 A GLY 1436 ? A GLY 659 
329 1 Y 1 A VAL 1437 ? A VAL 660 
330 1 Y 1 A PRO 1438 ? A PRO 661 
331 1 Y 1 A LEU 1439 ? A LEU 662 
332 1 Y 1 A ARG 1440 ? A ARG 663 
333 1 Y 1 A ALA 1441 ? A ALA 664 
334 1 Y 1 A LEU 1442 ? A LEU 665 
335 1 Y 1 A GLY 1443 ? A GLY 666 
336 1 Y 1 A GLN 1444 ? A GLN 667 
337 1 Y 1 A ARG 1445 ? A ARG 668 
338 1 Y 1 A VAL 1446 ? A VAL 669 
339 1 Y 1 A GLN 1447 ? A GLN 670 
340 1 Y 1 A CYS 1448 ? A CYS 671 
341 1 Y 1 A SER 1449 ? A SER 672 
342 1 Y 1 A PRO 1450 ? A PRO 673 
343 1 Y 1 A ASP 1451 ? A ASP 674 
344 1 Y 1 A VAL 1452 ? A VAL 675 
345 1 Y 1 A GLY 1453 ? A GLY 676 
346 1 Y 1 A LEU 1454 ? A LEU 677 
347 1 Y 1 A THR 1455 ? A THR 678 
348 1 Y 1 A CYS 1456 ? A CYS 679 
349 1 Y 1 A ARG 1457 ? A ARG 680 
350 1 Y 1 A ASN 1458 ? A ASN 681 
351 1 Y 1 A ARG 1459 ? A ARG 682 
352 1 Y 1 A GLU 1460 ? A GLU 683 
353 1 Y 1 A GLN 1461 ? A GLN 684 
354 1 Y 1 A ALA 1462 ? A ALA 685 
355 1 Y 1 A SER 1463 ? A SER 686 
356 1 Y 1 A GLY 1464 ? A GLY 687 
357 1 Y 1 A LEU 1465 ? A LEU 688 
358 1 Y 1 A CYS 1466 ? A CYS 689 
359 1 Y 1 A TYR 1467 ? A TYR 690 
360 1 Y 1 A ASN 1468 ? A ASN 691 
361 1 Y 1 A TYR 1469 ? A TYR 692 
362 1 Y 1 A GLN 1470 ? A GLN 693 
363 1 Y 1 A ILE 1471 ? A ILE 694 
364 1 Y 1 A ARG 1472 ? A ARG 695 
365 1 Y 1 A VAL 1473 ? A VAL 696 
366 1 Y 1 A GLN 1474 ? A GLN 697 
367 1 Y 1 A CYS 1475 ? A CYS 698 
368 1 Y 1 A CYS 1476 ? A CYS 699 
369 1 Y 1 A THR 1477 ? A THR 700 
370 1 Y 1 A PRO 1478 ? A PRO 701 
371 1 Y 1 A LEU 1479 ? A LEU 702 
372 1 Y 1 A PRO 1480 ? A PRO 703 
373 1 Y 1 A CYS 1481 ? A CYS 704 
374 1 Y 1 A THR 1482 ? A THR 705 
375 1 Y 1 A SER 1483 ? A SER 706 
376 1 Y 1 A GLU 1484 ? A GLU 707 
377 1 Y 1 A GLN 1485 ? A GLN 708 
378 1 Y 1 A LYS 1486 ? A LYS 709 
379 1 Y 1 A LEU 1487 ? A LEU 710 
380 1 Y 1 A ILE 1488 ? A ILE 711 
381 1 Y 1 A SER 1489 ? A SER 712 
382 1 Y 1 A GLU 1490 ? A GLU 713 
383 1 Y 1 A GLU 1491 ? A GLU 714 
384 1 Y 1 A ASP 1492 ? A ASP 715 
385 1 Y 1 A LEU 1493 ? A LEU 716 
386 1 Y 1 A SER 1494 ? A SER 717 
387 1 Y 1 A ARG 1495 ? A ARG 718 
388 1 Y 1 A LYS 1496 ? A LYS 719 
389 1 Y 1 A LEU 1497 ? A LEU 720 
390 1 Y 1 A THR 1498 ? A THR 721 
391 1 Y 1 A ARG 1499 ? A ARG 722 
392 1 Y 1 B ASP 778  ? B ASP 1   
393 1 Y 1 B ALA 779  ? B ALA 2   
394 1 Y 1 B ALA 780  ? B ALA 3   
395 1 Y 1 B GLN 781  ? B GLN 4   
396 1 Y 1 B PRO 782  ? B PRO 5   
397 1 Y 1 B ALA 783  ? B ALA 6   
398 1 Y 1 B ARG 784  ? B ARG 7   
399 1 Y 1 B ARG 785  ? B ARG 8   
400 1 Y 1 B ALA 786  ? B ALA 9   
401 1 Y 1 B VAL 787  ? B VAL 10  
402 1 Y 1 B ARG 788  ? B ARG 11  
403 1 Y 1 B SER 789  ? B SER 12  
404 1 Y 1 B SER 790  ? B SER 13  
405 1 Y 1 B ARG 791  ? B ARG 14  
406 1 Y 1 B HIS 792  ? B HIS 15  
407 1 Y 1 B HIS 793  ? B HIS 16  
408 1 Y 1 B HIS 794  ? B HIS 17  
409 1 Y 1 B HIS 795  ? B HIS 18  
410 1 Y 1 B HIS 796  ? B HIS 19  
411 1 Y 1 B HIS 797  ? B HIS 20  
412 1 Y 1 B GLY 798  ? B GLY 21  
413 1 Y 1 B SER 799  ? B SER 22  
414 1 Y 1 B PRO 800  ? B PRO 23  
415 1 Y 1 B VAL 801  ? B VAL 24  
416 1 Y 1 B CYS 802  ? B CYS 25  
417 1 Y 1 B ALA 803  ? B ALA 26  
418 1 Y 1 B ALA 804  ? B ALA 27  
419 1 Y 1 B PRO 805  ? B PRO 28  
420 1 Y 1 B MET 806  ? B MET 29  
421 1 Y 1 B VAL 807  ? B VAL 30  
422 1 Y 1 B PHE 808  ? B PHE 31  
423 1 Y 1 B PHE 809  ? B PHE 32  
424 1 Y 1 B ASP 810  ? B ASP 33  
425 1 Y 1 B CYS 811  ? B CYS 34  
426 1 Y 1 B ARG 812  ? B ARG 35  
427 1 Y 1 B ASN 813  ? B ASN 36  
428 1 Y 1 B ALA 814  ? B ALA 37  
429 1 Y 1 B THR 815  ? B THR 38  
430 1 Y 1 B PRO 816  ? B PRO 39  
431 1 Y 1 B GLY 817  ? B GLY 40  
432 1 Y 1 B ASP 818  ? B ASP 41  
433 1 Y 1 B THR 819  ? B THR 42  
434 1 Y 1 B GLY 820  ? B GLY 43  
435 1 Y 1 B ALA 821  ? B ALA 44  
436 1 Y 1 B GLY 822  ? B GLY 45  
437 1 Y 1 B CYS 823  ? B CYS 46  
438 1 Y 1 B GLN 824  ? B GLN 47  
439 1 Y 1 B LYS 825  ? B LYS 48  
440 1 Y 1 B SER 826  ? B SER 49  
441 1 Y 1 B CYS 827  ? B CYS 50  
442 1 Y 1 B HIS 828  ? B HIS 51  
443 1 Y 1 B THR 829  ? B THR 52  
444 1 Y 1 B LEU 830  ? B LEU 53  
445 1 Y 1 B ASP 831  ? B ASP 54  
446 1 Y 1 B MET 832  ? B MET 55  
447 1 Y 1 B THR 833  ? B THR 56  
448 1 Y 1 B CYS 834  ? B CYS 57  
449 1 Y 1 B TYR 835  ? B TYR 58  
450 1 Y 1 B SER 836  ? B SER 59  
451 1 Y 1 B PRO 837  ? B PRO 60  
452 1 Y 1 B GLN 838  ? B GLN 61  
453 1 Y 1 B CYS 839  ? B CYS 62  
454 1 Y 1 B VAL 840  ? B VAL 63  
455 1 Y 1 B PRO 841  ? B PRO 64  
456 1 Y 1 B GLY 842  ? B GLY 65  
457 1 Y 1 B CYS 843  ? B CYS 66  
458 1 Y 1 B VAL 844  ? B VAL 67  
459 1 Y 1 B CYS 845  ? B CYS 68  
460 1 Y 1 B PRO 846  ? B PRO 69  
461 1 Y 1 B ASP 847  ? B ASP 70  
462 1 Y 1 B GLY 848  ? B GLY 71  
463 1 Y 1 B LEU 849  ? B LEU 72  
464 1 Y 1 B VAL 850  ? B VAL 73  
465 1 Y 1 B ALA 851  ? B ALA 74  
466 1 Y 1 B ASP 852  ? B ASP 75  
467 1 Y 1 B GLY 853  ? B GLY 76  
468 1 Y 1 B GLU 854  ? B GLU 77  
469 1 Y 1 B GLY 855  ? B GLY 78  
470 1 Y 1 B GLY 856  ? B GLY 79  
471 1 Y 1 B CYS 857  ? B CYS 80  
472 1 Y 1 B ILE 858  ? B ILE 81  
473 1 Y 1 B THR 859  ? B THR 82  
474 1 Y 1 B ALA 860  ? B ALA 83  
475 1 Y 1 B GLU 861  ? B GLU 84  
476 1 Y 1 B ASP 862  ? B ASP 85  
477 1 Y 1 B CYS 863  ? B CYS 86  
478 1 Y 1 B PRO 864  ? B PRO 87  
479 1 Y 1 B CYS 865  ? B CYS 88  
480 1 Y 1 B VAL 866  ? B VAL 89  
481 1 Y 1 B HIS 867  ? B HIS 90  
482 1 Y 1 B ASN 868  ? B ASN 91  
483 1 Y 1 B GLU 869  ? B GLU 92  
484 1 Y 1 B ALA 870  ? B ALA 93  
485 1 Y 1 B SER 871  ? B SER 94  
486 1 Y 1 B TYR 872  ? B TYR 95  
487 1 Y 1 B ARG 873  ? B ARG 96  
488 1 Y 1 B ALA 874  ? B ALA 97  
489 1 Y 1 B GLY 875  ? B GLY 98  
490 1 Y 1 B GLN 876  ? B GLN 99  
491 1 Y 1 B THR 877  ? B THR 100 
492 1 Y 1 B ILE 878  ? B ILE 101 
493 1 Y 1 B ARG 879  ? B ARG 102 
494 1 Y 1 B VAL 880  ? B VAL 103 
495 1 Y 1 B GLY 881  ? B GLY 104 
496 1 Y 1 B CYS 882  ? B CYS 105 
497 1 Y 1 B ASN 883  ? B ASN 106 
498 1 Y 1 B THR 884  ? B THR 107 
499 1 Y 1 B CYS 885  ? B CYS 108 
500 1 Y 1 B THR 886  ? B THR 109 
501 1 Y 1 B CYS 887  ? B CYS 110 
502 1 Y 1 B ASP 888  ? B ASP 111 
503 1 Y 1 B SER 889  ? B SER 112 
504 1 Y 1 B ARG 890  ? B ARG 113 
505 1 Y 1 B MET 891  ? B MET 114 
506 1 Y 1 B TRP 892  ? B TRP 115 
507 1 Y 1 B ARG 893  ? B ARG 116 
508 1 Y 1 B CYS 894  ? B CYS 117 
509 1 Y 1 B THR 895  ? B THR 118 
510 1 Y 1 B ASP 896  ? B ASP 119 
511 1 Y 1 B ASP 897  ? B ASP 120 
512 1 Y 1 B PRO 898  ? B PRO 121 
513 1 Y 1 B THR 1230 ? B THR 453 
514 1 Y 1 B PRO 1231 ? B PRO 454 
515 1 Y 1 B PRO 1232 ? B PRO 455 
516 1 Y 1 B LEU 1233 ? B LEU 456 
517 1 Y 1 B PRO 1234 ? B PRO 457 
518 1 Y 1 B PRO 1235 ? B PRO 458 
519 1 Y 1 B ARG 1236 ? B ARG 459 
520 1 Y 1 B CYS 1237 ? B CYS 460 
521 1 Y 1 B HIS 1238 ? B HIS 461 
522 1 Y 1 B VAL 1239 ? B VAL 462 
523 1 Y 1 B HIS 1240 ? B HIS 463 
524 1 Y 1 B GLY 1241 ? B GLY 464 
525 1 Y 1 B LYS 1242 ? B LYS 465 
526 1 Y 1 B SER 1243 ? B SER 466 
527 1 Y 1 B TYR 1244 ? B TYR 467 
528 1 Y 1 B ARG 1245 ? B ARG 468 
529 1 Y 1 B PRO 1246 ? B PRO 469 
530 1 Y 1 B GLY 1247 ? B GLY 470 
531 1 Y 1 B ALA 1248 ? B ALA 471 
532 1 Y 1 B VAL 1249 ? B VAL 472 
533 1 Y 1 B VAL 1250 ? B VAL 473 
534 1 Y 1 B PRO 1251 ? B PRO 474 
535 1 Y 1 B SER 1252 ? B SER 475 
536 1 Y 1 B ASP 1253 ? B ASP 476 
537 1 Y 1 B LYS 1254 ? B LYS 477 
538 1 Y 1 B ASN 1255 ? B ASN 478 
539 1 Y 1 B CYS 1256 ? B CYS 479 
540 1 Y 1 B GLN 1257 ? B GLN 480 
541 1 Y 1 B SER 1258 ? B SER 481 
542 1 Y 1 B CYS 1259 ? B CYS 482 
543 1 Y 1 B LEU 1260 ? B LEU 483 
544 1 Y 1 B CYS 1261 ? B CYS 484 
545 1 Y 1 B THR 1262 ? B THR 485 
546 1 Y 1 B GLU 1263 ? B GLU 486 
547 1 Y 1 B ARG 1264 ? B ARG 487 
548 1 Y 1 B GLY 1265 ? B GLY 488 
549 1 Y 1 B VAL 1266 ? B VAL 489 
550 1 Y 1 B GLU 1267 ? B GLU 490 
551 1 Y 1 B CYS 1268 ? B CYS 491 
552 1 Y 1 B THR 1269 ? B THR 492 
553 1 Y 1 B TYR 1270 ? B TYR 493 
554 1 Y 1 B LYS 1271 ? B LYS 494 
555 1 Y 1 B ALA 1272 ? B ALA 495 
556 1 Y 1 B GLU 1273 ? B GLU 496 
557 1 Y 1 B ALA 1274 ? B ALA 497 
558 1 Y 1 B CYS 1275 ? B CYS 498 
559 1 Y 1 B VAL 1276 ? B VAL 499 
560 1 Y 1 B CYS 1277 ? B CYS 500 
561 1 Y 1 B THR 1278 ? B THR 501 
562 1 Y 1 B TYR 1279 ? B TYR 502 
563 1 Y 1 B ASN 1280 ? B ASN 503 
564 1 Y 1 B GLY 1281 ? B GLY 504 
565 1 Y 1 B GLN 1282 ? B GLN 505 
566 1 Y 1 B ARG 1283 ? B ARG 506 
567 1 Y 1 B PHE 1284 ? B PHE 507 
568 1 Y 1 B HIS 1285 ? B HIS 508 
569 1 Y 1 B PRO 1286 ? B PRO 509 
570 1 Y 1 B GLY 1287 ? B GLY 510 
571 1 Y 1 B ASP 1288 ? B ASP 511 
572 1 Y 1 B VAL 1289 ? B VAL 512 
573 1 Y 1 B ILE 1290 ? B ILE 513 
574 1 Y 1 B TYR 1291 ? B TYR 514 
575 1 Y 1 B HIS 1292 ? B HIS 515 
576 1 Y 1 B THR 1293 ? B THR 516 
577 1 Y 1 B THR 1294 ? B THR 517 
578 1 Y 1 B ASP 1295 ? B ASP 518 
579 1 Y 1 B GLY 1296 ? B GLY 519 
580 1 Y 1 B THR 1297 ? B THR 520 
581 1 Y 1 B GLY 1298 ? B GLY 521 
582 1 Y 1 B GLY 1299 ? B GLY 522 
583 1 Y 1 B CYS 1300 ? B CYS 523 
584 1 Y 1 B ILE 1301 ? B ILE 524 
585 1 Y 1 B SER 1302 ? B SER 525 
586 1 Y 1 B ALA 1303 ? B ALA 526 
587 1 Y 1 B ARG 1304 ? B ARG 527 
588 1 Y 1 B CYS 1305 ? B CYS 528 
589 1 Y 1 B GLY 1306 ? B GLY 529 
590 1 Y 1 B ALA 1307 ? B ALA 530 
591 1 Y 1 B ASN 1308 ? B ASN 531 
592 1 Y 1 B GLY 1309 ? B GLY 532 
593 1 Y 1 B THR 1310 ? B THR 533 
594 1 Y 1 B ILE 1311 ? B ILE 534 
595 1 Y 1 B GLU 1312 ? B GLU 535 
596 1 Y 1 B ARG 1313 ? B ARG 536 
597 1 Y 1 B ARG 1314 ? B ARG 537 
598 1 Y 1 B VAL 1315 ? B VAL 538 
599 1 Y 1 B TYR 1316 ? B TYR 539 
600 1 Y 1 B PRO 1317 ? B PRO 540 
601 1 Y 1 B CYS 1318 ? B CYS 541 
602 1 Y 1 B SER 1319 ? B SER 542 
603 1 Y 1 B PRO 1320 ? B PRO 543 
604 1 Y 1 B THR 1321 ? B THR 544 
605 1 Y 1 B THR 1322 ? B THR 545 
606 1 Y 1 B PRO 1323 ? B PRO 546 
607 1 Y 1 B VAL 1324 ? B VAL 547 
608 1 Y 1 B PRO 1325 ? B PRO 548 
609 1 Y 1 B PRO 1326 ? B PRO 549 
610 1 Y 1 B THR 1327 ? B THR 550 
611 1 Y 1 B THR 1328 ? B THR 551 
612 1 Y 1 B PHE 1329 ? B PHE 552 
613 1 Y 1 B SER 1330 ? B SER 553 
614 1 Y 1 B PHE 1331 ? B PHE 554 
615 1 Y 1 B SER 1332 ? B SER 555 
616 1 Y 1 B THR 1333 ? B THR 556 
617 1 Y 1 B PRO 1334 ? B PRO 557 
618 1 Y 1 B PRO 1335 ? B PRO 558 
619 1 Y 1 B LEU 1336 ? B LEU 559 
620 1 Y 1 B VAL 1337 ? B VAL 560 
621 1 Y 1 B VAL 1338 ? B VAL 561 
622 1 Y 1 B SER 1339 ? B SER 562 
623 1 Y 1 B SER 1340 ? B SER 563 
624 1 Y 1 B THR 1341 ? B THR 564 
625 1 Y 1 B HIS 1342 ? B HIS 565 
626 1 Y 1 B THR 1343 ? B THR 566 
627 1 Y 1 B PRO 1344 ? B PRO 567 
628 1 Y 1 B SER 1345 ? B SER 568 
629 1 Y 1 B ASN 1346 ? B ASN 569 
630 1 Y 1 B GLY 1347 ? B GLY 570 
631 1 Y 1 B PRO 1348 ? B PRO 571 
632 1 Y 1 B SER 1349 ? B SER 572 
633 1 Y 1 B SER 1350 ? B SER 573 
634 1 Y 1 B ALA 1351 ? B ALA 574 
635 1 Y 1 B HIS 1352 ? B HIS 575 
636 1 Y 1 B THR 1353 ? B THR 576 
637 1 Y 1 B GLY 1354 ? B GLY 577 
638 1 Y 1 B PRO 1355 ? B PRO 578 
639 1 Y 1 B PRO 1356 ? B PRO 579 
640 1 Y 1 B SER 1357 ? B SER 580 
641 1 Y 1 B SER 1358 ? B SER 581 
642 1 Y 1 B ALA 1359 ? B ALA 582 
643 1 Y 1 B TRP 1360 ? B TRP 583 
644 1 Y 1 B PRO 1361 ? B PRO 584 
645 1 Y 1 B THR 1362 ? B THR 585 
646 1 Y 1 B THR 1363 ? B THR 586 
647 1 Y 1 B ALA 1364 ? B ALA 587 
648 1 Y 1 B GLY 1365 ? B GLY 588 
649 1 Y 1 B THR 1366 ? B THR 589 
650 1 Y 1 B SER 1367 ? B SER 590 
651 1 Y 1 B PRO 1368 ? B PRO 591 
652 1 Y 1 B ARG 1369 ? B ARG 592 
653 1 Y 1 B THR 1370 ? B THR 593 
654 1 Y 1 B ARG 1371 ? B ARG 594 
655 1 Y 1 B LEU 1372 ? B LEU 595 
656 1 Y 1 B PRO 1373 ? B PRO 596 
657 1 Y 1 B THR 1374 ? B THR 597 
658 1 Y 1 B ALA 1375 ? B ALA 598 
659 1 Y 1 B SER 1376 ? B SER 599 
660 1 Y 1 B ALA 1377 ? B ALA 600 
661 1 Y 1 B SER 1378 ? B SER 601 
662 1 Y 1 B LEU 1379 ? B LEU 602 
663 1 Y 1 B PRO 1380 ? B PRO 603 
664 1 Y 1 B PRO 1381 ? B PRO 604 
665 1 Y 1 B VAL 1382 ? B VAL 605 
666 1 Y 1 B CYS 1383 ? B CYS 606 
667 1 Y 1 B GLY 1384 ? B GLY 607 
668 1 Y 1 B GLU 1385 ? B GLU 608 
669 1 Y 1 B LYS 1386 ? B LYS 609 
670 1 Y 1 B CYS 1387 ? B CYS 610 
671 1 Y 1 B LEU 1388 ? B LEU 611 
672 1 Y 1 B TRP 1389 ? B TRP 612 
673 1 Y 1 B SER 1390 ? B SER 613 
674 1 Y 1 B PRO 1391 ? B PRO 614 
675 1 Y 1 B TRP 1392 ? B TRP 615 
676 1 Y 1 B MET 1393 ? B MET 616 
677 1 Y 1 B ASP 1394 ? B ASP 617 
678 1 Y 1 B VAL 1395 ? B VAL 618 
679 1 Y 1 B SER 1396 ? B SER 619 
680 1 Y 1 B ARG 1397 ? B ARG 620 
681 1 Y 1 B PRO 1398 ? B PRO 621 
682 1 Y 1 B GLY 1399 ? B GLY 622 
683 1 Y 1 B ARG 1400 ? B ARG 623 
684 1 Y 1 B GLY 1401 ? B GLY 624 
685 1 Y 1 B THR 1402 ? B THR 625 
686 1 Y 1 B ASP 1403 ? B ASP 626 
687 1 Y 1 B SER 1404 ? B SER 627 
688 1 Y 1 B GLY 1405 ? B GLY 628 
689 1 Y 1 B ASP 1406 ? B ASP 629 
690 1 Y 1 B PHE 1407 ? B PHE 630 
691 1 Y 1 B ASP 1408 ? B ASP 631 
692 1 Y 1 B THR 1409 ? B THR 632 
693 1 Y 1 B LEU 1410 ? B LEU 633 
694 1 Y 1 B GLU 1411 ? B GLU 634 
695 1 Y 1 B ASN 1412 ? B ASN 635 
696 1 Y 1 B LEU 1413 ? B LEU 636 
697 1 Y 1 B ARG 1414 ? B ARG 637 
698 1 Y 1 B ALA 1415 ? B ALA 638 
699 1 Y 1 B HIS 1416 ? B HIS 639 
700 1 Y 1 B GLY 1417 ? B GLY 640 
701 1 Y 1 B TYR 1418 ? B TYR 641 
702 1 Y 1 B ARG 1419 ? B ARG 642 
703 1 Y 1 B VAL 1420 ? B VAL 643 
704 1 Y 1 B CYS 1421 ? B CYS 644 
705 1 Y 1 B GLU 1422 ? B GLU 645 
706 1 Y 1 B SER 1423 ? B SER 646 
707 1 Y 1 B PRO 1424 ? B PRO 647 
708 1 Y 1 B ARG 1425 ? B ARG 648 
709 1 Y 1 B SER 1426 ? B SER 649 
710 1 Y 1 B VAL 1427 ? B VAL 650 
711 1 Y 1 B GLU 1428 ? B GLU 651 
712 1 Y 1 B CYS 1429 ? B CYS 652 
713 1 Y 1 B ARG 1430 ? B ARG 653 
714 1 Y 1 B ALA 1431 ? B ALA 654 
715 1 Y 1 B GLU 1432 ? B GLU 655 
716 1 Y 1 B ASP 1433 ? B ASP 656 
717 1 Y 1 B ALA 1434 ? B ALA 657 
718 1 Y 1 B PRO 1435 ? B PRO 658 
719 1 Y 1 B GLY 1436 ? B GLY 659 
720 1 Y 1 B VAL 1437 ? B VAL 660 
721 1 Y 1 B PRO 1438 ? B PRO 661 
722 1 Y 1 B LEU 1439 ? B LEU 662 
723 1 Y 1 B ARG 1440 ? B ARG 663 
724 1 Y 1 B ALA 1441 ? B ALA 664 
725 1 Y 1 B LEU 1442 ? B LEU 665 
726 1 Y 1 B GLY 1443 ? B GLY 666 
727 1 Y 1 B GLN 1444 ? B GLN 667 
728 1 Y 1 B ARG 1445 ? B ARG 668 
729 1 Y 1 B VAL 1446 ? B VAL 669 
730 1 Y 1 B GLN 1447 ? B GLN 670 
731 1 Y 1 B CYS 1448 ? B CYS 671 
732 1 Y 1 B SER 1449 ? B SER 672 
733 1 Y 1 B PRO 1450 ? B PRO 673 
734 1 Y 1 B ASP 1451 ? B ASP 674 
735 1 Y 1 B VAL 1452 ? B VAL 675 
736 1 Y 1 B GLY 1453 ? B GLY 676 
737 1 Y 1 B LEU 1454 ? B LEU 677 
738 1 Y 1 B THR 1455 ? B THR 678 
739 1 Y 1 B CYS 1456 ? B CYS 679 
740 1 Y 1 B ARG 1457 ? B ARG 680 
741 1 Y 1 B ASN 1458 ? B ASN 681 
742 1 Y 1 B ARG 1459 ? B ARG 682 
743 1 Y 1 B GLU 1460 ? B GLU 683 
744 1 Y 1 B GLN 1461 ? B GLN 684 
745 1 Y 1 B ALA 1462 ? B ALA 685 
746 1 Y 1 B SER 1463 ? B SER 686 
747 1 Y 1 B GLY 1464 ? B GLY 687 
748 1 Y 1 B LEU 1465 ? B LEU 688 
749 1 Y 1 B CYS 1466 ? B CYS 689 
750 1 Y 1 B TYR 1467 ? B TYR 690 
751 1 Y 1 B ASN 1468 ? B ASN 691 
752 1 Y 1 B TYR 1469 ? B TYR 692 
753 1 Y 1 B GLN 1470 ? B GLN 693 
754 1 Y 1 B ILE 1471 ? B ILE 694 
755 1 Y 1 B ARG 1472 ? B ARG 695 
756 1 Y 1 B VAL 1473 ? B VAL 696 
757 1 Y 1 B GLN 1474 ? B GLN 697 
758 1 Y 1 B CYS 1475 ? B CYS 698 
759 1 Y 1 B CYS 1476 ? B CYS 699 
760 1 Y 1 B THR 1477 ? B THR 700 
761 1 Y 1 B PRO 1478 ? B PRO 701 
762 1 Y 1 B LEU 1479 ? B LEU 702 
763 1 Y 1 B PRO 1480 ? B PRO 703 
764 1 Y 1 B CYS 1481 ? B CYS 704 
765 1 Y 1 B THR 1482 ? B THR 705 
766 1 Y 1 B SER 1483 ? B SER 706 
767 1 Y 1 B GLU 1484 ? B GLU 707 
768 1 Y 1 B GLN 1485 ? B GLN 708 
769 1 Y 1 B LYS 1486 ? B LYS 709 
770 1 Y 1 B LEU 1487 ? B LEU 710 
771 1 Y 1 B ILE 1488 ? B ILE 711 
772 1 Y 1 B SER 1489 ? B SER 712 
773 1 Y 1 B GLU 1490 ? B GLU 713 
774 1 Y 1 B GLU 1491 ? B GLU 714 
775 1 Y 1 B ASP 1492 ? B ASP 715 
776 1 Y 1 B LEU 1493 ? B LEU 716 
777 1 Y 1 B SER 1494 ? B SER 717 
778 1 Y 1 B ARG 1495 ? B ARG 718 
779 1 Y 1 B LYS 1496 ? B LYS 719 
780 1 Y 1 B LEU 1497 ? B LEU 720 
781 1 Y 1 B THR 1498 ? B THR 721 
782 1 Y 1 B ARG 1499 ? B ARG 722 
# 
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  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
ILE N    N  N N 159 
ILE CA   C  N S 160 
ILE C    C  N N 161 
ILE O    O  N N 162 
ILE CB   C  N S 163 
ILE CG1  C  N N 164 
ILE CG2  C  N N 165 
ILE CD1  C  N N 166 
ILE OXT  O  N N 167 
ILE H    H  N N 168 
ILE H2   H  N N 169 
ILE HA   H  N N 170 
ILE HB   H  N N 171 
ILE HG12 H  N N 172 
ILE HG13 H  N N 173 
ILE HG21 H  N N 174 
ILE HG22 H  N N 175 
ILE HG23 H  N N 176 
ILE HD11 H  N N 177 
ILE HD12 H  N N 178 
ILE HD13 H  N N 179 
ILE HXT  H  N N 180 
LEU N    N  N N 181 
LEU CA   C  N S 182 
LEU C    C  N N 183 
LEU O    O  N N 184 
LEU CB   C  N N 185 
LEU CG   C  N N 186 
LEU CD1  C  N N 187 
LEU CD2  C  N N 188 
LEU OXT  O  N N 189 
LEU H    H  N N 190 
LEU H2   H  N N 191 
LEU HA   H  N N 192 
LEU HB2  H  N N 193 
LEU HB3  H  N N 194 
LEU HG   H  N N 195 
LEU HD11 H  N N 196 
LEU HD12 H  N N 197 
LEU HD13 H  N N 198 
LEU HD21 H  N N 199 
LEU HD22 H  N N 200 
LEU HD23 H  N N 201 
LEU HXT  H  N N 202 
LYS N    N  N N 203 
LYS CA   C  N S 204 
LYS C    C  N N 205 
LYS O    O  N N 206 
LYS CB   C  N N 207 
LYS CG   C  N N 208 
LYS CD   C  N N 209 
LYS CE   C  N N 210 
LYS NZ   N  N N 211 
LYS OXT  O  N N 212 
LYS H    H  N N 213 
LYS H2   H  N N 214 
LYS HA   H  N N 215 
LYS HB2  H  N N 216 
LYS HB3  H  N N 217 
LYS HG2  H  N N 218 
LYS HG3  H  N N 219 
LYS HD2  H  N N 220 
LYS HD3  H  N N 221 
LYS HE2  H  N N 222 
LYS HE3  H  N N 223 
LYS HZ1  H  N N 224 
LYS HZ2  H  N N 225 
LYS HZ3  H  N N 226 
LYS HXT  H  N N 227 
MET N    N  N N 228 
MET CA   C  N S 229 
MET C    C  N N 230 
MET O    O  N N 231 
MET CB   C  N N 232 
MET CG   C  N N 233 
MET SD   S  N N 234 
MET CE   C  N N 235 
MET OXT  O  N N 236 
MET H    H  N N 237 
MET H2   H  N N 238 
MET HA   H  N N 239 
MET HB2  H  N N 240 
MET HB3  H  N N 241 
MET HG2  H  N N 242 
MET HG3  H  N N 243 
MET HE1  H  N N 244 
MET HE2  H  N N 245 
MET HE3  H  N N 246 
MET HXT  H  N N 247 
PHE N    N  N N 248 
PHE CA   C  N S 249 
PHE C    C  N N 250 
PHE O    O  N N 251 
PHE CB   C  N N 252 
PHE CG   C  Y N 253 
PHE CD1  C  Y N 254 
PHE CD2  C  Y N 255 
PHE CE1  C  Y N 256 
PHE CE2  C  Y N 257 
PHE CZ   C  Y N 258 
PHE OXT  O  N N 259 
PHE H    H  N N 260 
PHE H2   H  N N 261 
PHE HA   H  N N 262 
PHE HB2  H  N N 263 
PHE HB3  H  N N 264 
PHE HD1  H  N N 265 
PHE HD2  H  N N 266 
PHE HE1  H  N N 267 
PHE HE2  H  N N 268 
PHE HZ   H  N N 269 
PHE HXT  H  N N 270 
PRO N    N  N N 271 
PRO CA   C  N S 272 
PRO C    C  N N 273 
PRO O    O  N N 274 
PRO CB   C  N N 275 
PRO CG   C  N N 276 
PRO CD   C  N N 277 
PRO OXT  O  N N 278 
PRO H    H  N N 279 
PRO HA   H  N N 280 
PRO HB2  H  N N 281 
PRO HB3  H  N N 282 
PRO HG2  H  N N 283 
PRO HG3  H  N N 284 
PRO HD2  H  N N 285 
PRO HD3  H  N N 286 
PRO HXT  H  N N 287 
SER N    N  N N 288 
SER CA   C  N S 289 
SER C    C  N N 290 
SER O    O  N N 291 
SER CB   C  N N 292 
SER OG   O  N N 293 
SER OXT  O  N N 294 
SER H    H  N N 295 
SER H2   H  N N 296 
SER HA   H  N N 297 
SER HB2  H  N N 298 
SER HB3  H  N N 299 
SER HG   H  N N 300 
SER HXT  H  N N 301 
THR N    N  N N 302 
THR CA   C  N S 303 
THR C    C  N N 304 
THR O    O  N N 305 
THR CB   C  N R 306 
THR OG1  O  N N 307 
THR CG2  C  N N 308 
THR OXT  O  N N 309 
THR H    H  N N 310 
THR H2   H  N N 311 
THR HA   H  N N 312 
THR HB   H  N N 313 
THR HG1  H  N N 314 
THR HG21 H  N N 315 
THR HG22 H  N N 316 
THR HG23 H  N N 317 
THR HXT  H  N N 318 
TRP N    N  N N 319 
TRP CA   C  N S 320 
TRP C    C  N N 321 
TRP O    O  N N 322 
TRP CB   C  N N 323 
TRP CG   C  Y N 324 
TRP CD1  C  Y N 325 
TRP CD2  C  Y N 326 
TRP NE1  N  Y N 327 
TRP CE2  C  Y N 328 
TRP CE3  C  Y N 329 
TRP CZ2  C  Y N 330 
TRP CZ3  C  Y N 331 
TRP CH2  C  Y N 332 
TRP OXT  O  N N 333 
TRP H    H  N N 334 
TRP H2   H  N N 335 
TRP HA   H  N N 336 
TRP HB2  H  N N 337 
TRP HB3  H  N N 338 
TRP HD1  H  N N 339 
TRP HE1  H  N N 340 
TRP HE3  H  N N 341 
TRP HZ2  H  N N 342 
TRP HZ3  H  N N 343 
TRP HH2  H  N N 344 
TRP HXT  H  N N 345 
TYR N    N  N N 346 
TYR CA   C  N S 347 
TYR C    C  N N 348 
TYR O    O  N N 349 
TYR CB   C  N N 350 
TYR CG   C  Y N 351 
TYR CD1  C  Y N 352 
TYR CD2  C  Y N 353 
TYR CE1  C  Y N 354 
TYR CE2  C  Y N 355 
TYR CZ   C  Y N 356 
TYR OH   O  N N 357 
TYR OXT  O  N N 358 
TYR H    H  N N 359 
TYR H2   H  N N 360 
TYR HA   H  N N 361 
TYR HB2  H  N N 362 
TYR HB3  H  N N 363 
TYR HD1  H  N N 364 
TYR HD2  H  N N 365 
TYR HE1  H  N N 366 
TYR HE2  H  N N 367 
TYR HH   H  N N 368 
TYR HXT  H  N N 369 
VAL N    N  N N 370 
VAL CA   C  N S 371 
VAL C    C  N N 372 
VAL O    O  N N 373 
VAL CB   C  N N 374 
VAL CG1  C  N N 375 
VAL CG2  C  N N 376 
VAL OXT  O  N N 377 
VAL H    H  N N 378 
VAL H2   H  N N 379 
VAL HA   H  N N 380 
VAL HB   H  N N 381 
VAL HG11 H  N N 382 
VAL HG12 H  N N 383 
VAL HG13 H  N N 384 
VAL HG21 H  N N 385 
VAL HG22 H  N N 386 
VAL HG23 H  N N 387 
VAL HXT  H  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    2023-10-13 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           8QTV 
_em_admin.last_update        2025-04-02 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              
;MUC5AC D'D3CysD1 domains.
;
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20  mM 'NH2C(CH2OH)3.HCl' 1 Tris-HCl           
1 150 mM NaCl               2 'Sodium Chloride'  
1 10  mM CaCl2              3 'Calcium Chloride' 
# 
_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_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                ? 
# 
_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          10029 
_em_entity_assembly_recombinant.organism             'Cricetulus griseus' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               'CHO lec 3.2.8.1' 
# 
_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         1.29 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k 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                    1 
_em_image_recording.num_real_images                     6754 
# 
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 ? ? Topaz     0.2.3       
'IMAGE ACQUISITION'        ? 2  ? ? 1 ?         ?           
MASKING                    ? 3  ? ? ? ?         ?           
'CTF CORRECTION'           ? 4  1 ? ? cryoSPARC 4.2.1       
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ?           
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ?           
'MODEL FITTING'            ? 7  ? 1 ? ?         ?           
OTHER                      ? 8  ? ? ? ?         ?           
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? cryoSPARC 4.2.1       
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? cryoSPARC 4.2.1       
CLASSIFICATION             ? 11 1 ? ? cryoSPARC 4.2.1       
RECONSTRUCTION             ? 12 1 ? ? cryoSPARC 4.2.1       
'MODEL REFINEMENT'         ? 13 ? 1 ? PHENIX    1.20.1-4487 
# 
_em_specimen.concentration           0.16 
_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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'European Research Council (ERC)'                                                                 'European Union' 694181      1 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States'  U01AI095473 2 
'Swedish Research Council'                                                                        Sweden           2017-00958  3 
'Knut and Alice Wallenberg Foundation'                                                            Sweden           2017-0028   4 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QTV 
_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  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . CYS A 1 122 ? 122.808 77.664  122.321 1.00 222.50 ? 899  CYS A N   1 
ATOM   2    C  CA  . CYS A 1 122 ? 121.713 77.515  123.271 1.00 222.14 ? 899  CYS A CA  1 
ATOM   3    C  C   . CYS A 1 122 ? 120.374 77.398  122.550 1.00 222.57 ? 899  CYS A C   1 
ATOM   4    O  O   . CYS A 1 122 ? 119.803 76.312  122.454 1.00 222.08 ? 899  CYS A O   1 
ATOM   5    C  CB  . CYS A 1 122 ? 121.684 78.694  124.246 1.00 221.64 ? 899  CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 122 ? 122.793 78.520  125.662 1.00 223.92 ? 899  CYS A SG  1 
ATOM   7    N  N   . LEU A 1 123 ? 119.878 78.525  122.045 1.00 206.48 ? 900  LEU A N   1 
ATOM   8    C  CA  . LEU A 1 123 ? 118.605 78.578  121.339 1.00 205.61 ? 900  LEU A CA  1 
ATOM   9    C  C   . LEU A 1 123 ? 118.793 79.318  120.024 1.00 204.24 ? 900  LEU A C   1 
ATOM   10   O  O   . LEU A 1 123 ? 119.372 80.409  119.999 1.00 203.59 ? 900  LEU A O   1 
ATOM   11   C  CB  . LEU A 1 123 ? 117.528 79.266  122.185 1.00 203.90 ? 900  LEU A CB  1 
ATOM   12   C  CG  . LEU A 1 123 ? 116.853 78.413  123.262 1.00 202.69 ? 900  LEU A CG  1 
ATOM   13   C  CD1 . LEU A 1 123 ? 117.638 78.466  124.563 1.00 201.64 ? 900  LEU A CD1 1 
ATOM   14   C  CD2 . LEU A 1 123 ? 115.418 78.864  123.479 1.00 202.71 ? 900  LEU A CD2 1 
ATOM   15   N  N   . ALA A 1 124 ? 118.305 78.726  118.938 1.00 179.83 ? 901  ALA A N   1 
ATOM   16   C  CA  . ALA A 1 124 ? 118.387 79.358  117.632 1.00 178.25 ? 901  ALA A CA  1 
ATOM   17   C  C   . ALA A 1 124 ? 117.300 80.419  117.483 1.00 178.67 ? 901  ALA A C   1 
ATOM   18   O  O   . ALA A 1 124 ? 116.320 80.454  118.232 1.00 179.78 ? 901  ALA A O   1 
ATOM   19   C  CB  . ALA A 1 124 ? 118.264 78.317  116.520 1.00 178.13 ? 901  ALA A CB  1 
ATOM   20   N  N   . THR A 1 125 ? 117.487 81.294  116.498 1.00 158.62 ? 902  THR A N   1 
ATOM   21   C  CA  . THR A 1 125 ? 116.559 82.391  116.256 1.00 157.55 ? 902  THR A CA  1 
ATOM   22   C  C   . THR A 1 125 ? 116.421 82.626  114.761 1.00 155.14 ? 902  THR A C   1 
ATOM   23   O  O   . THR A 1 125 ? 117.424 82.682  114.043 1.00 157.82 ? 902  THR A O   1 
ATOM   24   C  CB  . THR A 1 125 ? 117.029 83.678  116.946 1.00 158.97 ? 902  THR A CB  1 
ATOM   25   O  OG1 . THR A 1 125 ? 117.371 83.396  118.308 1.00 161.32 ? 902  THR A OG1 1 
ATOM   26   C  CG2 . THR A 1 125 ? 115.933 84.733  116.911 1.00 158.84 ? 902  THR A CG2 1 
ATOM   27   N  N   . CYS A 1 126 ? 115.181 82.762  114.299 1.00 151.59 ? 903  CYS A N   1 
ATOM   28   C  CA  . CYS A 1 126 ? 114.878 83.123  112.920 1.00 153.15 ? 903  CYS A CA  1 
ATOM   29   C  C   . CYS A 1 126 ? 114.306 84.533  112.915 1.00 154.02 ? 903  CYS A C   1 
ATOM   30   O  O   . CYS A 1 126 ? 113.269 84.787  113.536 1.00 157.03 ? 903  CYS A O   1 
ATOM   31   C  CB  . CYS A 1 126 ? 113.892 82.135  112.294 1.00 153.71 ? 903  CYS A CB  1 
ATOM   32   S  SG  . CYS A 1 126 ? 113.578 82.405  110.534 1.00 161.22 ? 903  CYS A SG  1 
ATOM   33   N  N   . ALA A 1 127 ? 114.979 85.444  112.218 1.00 143.13 ? 904  ALA A N   1 
ATOM   34   C  CA  . ALA A 1 127 ? 114.627 86.857  112.225 1.00 142.90 ? 904  ALA A CA  1 
ATOM   35   C  C   . ALA A 1 127 ? 114.162 87.287  110.842 1.00 143.92 ? 904  ALA A C   1 
ATOM   36   O  O   . ALA A 1 127 ? 114.852 87.048  109.846 1.00 146.94 ? 904  ALA A O   1 
ATOM   37   C  CB  . ALA A 1 127 ? 115.815 87.712  112.672 1.00 142.65 ? 904  ALA A CB  1 
ATOM   38   N  N   . VAL A 1 128 ? 112.993 87.920  110.789 1.00 132.19 ? 905  VAL A N   1 
ATOM   39   C  CA  . VAL A 1 128 ? 112.453 88.507  109.568 1.00 129.96 ? 905  VAL A CA  1 
ATOM   40   C  C   . VAL A 1 128 ? 112.165 89.973  109.858 1.00 131.78 ? 905  VAL A C   1 
ATOM   41   O  O   . VAL A 1 128 ? 111.420 90.290  110.793 1.00 138.25 ? 905  VAL A O   1 
ATOM   42   C  CB  . VAL A 1 128 ? 111.184 87.783  109.092 1.00 127.22 ? 905  VAL A CB  1 
ATOM   43   C  CG1 . VAL A 1 128 ? 110.699 88.375  107.779 1.00 128.11 ? 905  VAL A CG1 1 
ATOM   44   C  CG2 . VAL A 1 128 ? 111.444 86.292  108.949 1.00 127.87 ? 905  VAL A CG2 1 
ATOM   45   N  N   . TYR A 1 129 ? 112.751 90.863  109.062 1.00 139.02 ? 906  TYR A N   1 
ATOM   46   C  CA  . TYR A 1 129 ? 112.626 92.292  109.305 1.00 138.21 ? 906  TYR A CA  1 
ATOM   47   C  C   . TYR A 1 129 ? 112.829 93.042  107.997 1.00 143.20 ? 906  TYR A C   1 
ATOM   48   O  O   . TYR A 1 129 ? 113.303 92.487  107.003 1.00 149.78 ? 906  TYR A O   1 
ATOM   49   C  CB  . TYR A 1 129 ? 113.627 92.764  110.366 1.00 138.76 ? 906  TYR A CB  1 
ATOM   50   C  CG  . TYR A 1 129 ? 115.026 92.991  109.839 1.00 140.26 ? 906  TYR A CG  1 
ATOM   51   C  CD1 . TYR A 1 129 ? 115.915 91.934  109.701 1.00 141.54 ? 906  TYR A CD1 1 
ATOM   52   C  CD2 . TYR A 1 129 ? 115.463 94.263  109.493 1.00 139.98 ? 906  TYR A CD2 1 
ATOM   53   C  CE1 . TYR A 1 129 ? 117.195 92.134  109.224 1.00 143.03 ? 906  TYR A CE1 1 
ATOM   54   C  CE2 . TYR A 1 129 ? 116.742 94.473  109.015 1.00 140.41 ? 906  TYR A CE2 1 
ATOM   55   C  CZ  . TYR A 1 129 ? 117.603 93.406  108.883 1.00 143.29 ? 906  TYR A CZ  1 
ATOM   56   O  OH  . TYR A 1 129 ? 118.877 93.610  108.408 1.00 147.34 ? 906  TYR A OH  1 
ATOM   57   N  N   . GLY A 1 130 ? 112.461 94.323  108.015 1.00 148.08 ? 907  GLY A N   1 
ATOM   58   C  CA  . GLY A 1 130 ? 112.689 95.189  106.875 1.00 149.83 ? 907  GLY A CA  1 
ATOM   59   C  C   . GLY A 1 130 ? 111.896 94.767  105.650 1.00 148.46 ? 907  GLY A C   1 
ATOM   60   O  O   . GLY A 1 130 ? 110.778 94.249  105.737 1.00 147.17 ? 907  GLY A O   1 
ATOM   61   N  N   . ASP A 1 131 ? 112.495 94.998  104.482 1.00 169.40 ? 908  ASP A N   1 
ATOM   62   C  CA  . ASP A 1 131 ? 111.871 94.670  103.201 1.00 170.90 ? 908  ASP A CA  1 
ATOM   63   C  C   . ASP A 1 131 ? 112.410 93.321  102.733 1.00 169.74 ? 908  ASP A C   1 
ATOM   64   O  O   . ASP A 1 131 ? 113.318 93.229  101.907 1.00 170.11 ? 908  ASP A O   1 
ATOM   65   C  CB  . ASP A 1 131 ? 112.130 95.774  102.181 1.00 172.46 ? 908  ASP A CB  1 
ATOM   66   C  CG  . ASP A 1 131 ? 111.312 97.021  102.453 1.00 173.60 ? 908  ASP A CG  1 
ATOM   67   O  OD1 . ASP A 1 131 ? 110.630 97.069  103.498 1.00 172.96 ? 908  ASP A OD1 1 
ATOM   68   O  OD2 . ASP A 1 131 ? 111.351 97.952  101.623 1.00 174.03 ? 908  ASP A OD2 1 
ATOM   69   N  N   . GLY A 1 132 ? 111.827 92.259  103.278 1.00 149.94 ? 909  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 132 ? 112.187 90.910  102.880 1.00 149.11 ? 909  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 132 ? 113.590 90.479  103.251 1.00 147.28 ? 909  GLY A C   1 
ATOM   72   O  O   . GLY A 1 132 ? 114.276 89.852  102.434 1.00 149.41 ? 909  GLY A O   1 
ATOM   73   N  N   . HIS A 1 133 ? 114.035 90.797  104.462 1.00 140.60 ? 910  HIS A N   1 
ATOM   74   C  CA  . HIS A 1 133 ? 115.323 90.342  104.970 1.00 139.48 ? 910  HIS A CA  1 
ATOM   75   C  C   . HIS A 1 133 ? 115.084 89.164  105.906 1.00 140.88 ? 910  HIS A C   1 
ATOM   76   O  O   . HIS A 1 133 ? 114.312 89.275  106.864 1.00 144.98 ? 910  HIS A O   1 
ATOM   77   C  CB  . HIS A 1 133 ? 116.060 91.469  105.693 1.00 140.99 ? 910  HIS A CB  1 
ATOM   78   C  CG  . HIS A 1 133 ? 116.258 92.694  104.857 1.00 142.95 ? 910  HIS A CG  1 
ATOM   79   N  ND1 . HIS A 1 133 ? 117.428 92.948  104.175 1.00 144.47 ? 910  HIS A ND1 1 
ATOM   80   C  CD2 . HIS A 1 133 ? 115.435 93.736  104.593 1.00 143.88 ? 910  HIS A CD2 1 
ATOM   81   C  CE1 . HIS A 1 133 ? 117.318 94.093  103.526 1.00 145.54 ? 910  HIS A CE1 1 
ATOM   82   N  NE2 . HIS A 1 133 ? 116.118 94.592  103.763 1.00 144.87 ? 910  HIS A NE2 1 
ATOM   83   N  N   . TYR A 1 134 ? 115.745 88.044  105.629 1.00 132.65 ? 911  TYR A N   1 
ATOM   84   C  CA  . TYR A 1 134 ? 115.526 86.807  106.362 1.00 132.31 ? 911  TYR A CA  1 
ATOM   85   C  C   . TYR A 1 134 ? 116.838 86.294  106.938 1.00 133.46 ? 911  TYR A C   1 
ATOM   86   O  O   . TYR A 1 134 ? 117.921 86.584  106.420 1.00 136.28 ? 911  TYR A O   1 
ATOM   87   C  CB  . TYR A 1 134 ? 114.901 85.732  105.463 1.00 131.16 ? 911  TYR A CB  1 
ATOM   88   C  CG  . TYR A 1 134 ? 113.510 86.069  104.974 1.00 134.35 ? 911  TYR A CG  1 
ATOM   89   C  CD1 . TYR A 1 134 ? 113.317 86.953  103.920 1.00 134.84 ? 911  TYR A CD1 1 
ATOM   90   C  CD2 . TYR A 1 134 ? 112.389 85.502  105.564 1.00 136.47 ? 911  TYR A CD2 1 
ATOM   91   C  CE1 . TYR A 1 134 ? 112.049 87.263  103.470 1.00 134.39 ? 911  TYR A CE1 1 
ATOM   92   C  CE2 . TYR A 1 134 ? 111.117 85.806  105.121 1.00 135.11 ? 911  TYR A CE2 1 
ATOM   93   C  CZ  . TYR A 1 134 ? 110.952 86.687  104.074 1.00 133.60 ? 911  TYR A CZ  1 
ATOM   94   O  OH  . TYR A 1 134 ? 109.687 86.992  103.629 1.00 133.94 ? 911  TYR A OH  1 
ATOM   95   N  N   . LEU A 1 135 ? 116.726 85.526  108.019 1.00 131.24 ? 912  LEU A N   1 
ATOM   96   C  CA  . LEU A 1 135 ? 117.877 84.908  108.673 1.00 131.40 ? 912  LEU A CA  1 
ATOM   97   C  C   . LEU A 1 135 ? 117.438 83.546  109.192 1.00 133.12 ? 912  LEU A C   1 
ATOM   98   O  O   . LEU A 1 135 ? 116.608 83.466  110.102 1.00 137.24 ? 912  LEU A O   1 
ATOM   99   C  CB  . LEU A 1 135 ? 118.409 85.782  109.808 1.00 131.38 ? 912  LEU A CB  1 
ATOM   100  C  CG  . LEU A 1 135 ? 119.624 85.241  110.564 1.00 133.27 ? 912  LEU A CG  1 
ATOM   101  C  CD1 . LEU A 1 135 ? 120.745 84.890  109.599 1.00 133.60 ? 912  LEU A CD1 1 
ATOM   102  C  CD2 . LEU A 1 135 ? 120.100 86.243  111.603 1.00 135.51 ? 912  LEU A CD2 1 
ATOM   103  N  N   . THR A 1 136 ? 117.993 82.482  108.617 1.00 151.20 ? 913  THR A N   1 
ATOM   104  C  CA  . THR A 1 136 ? 117.590 81.135  108.983 1.00 150.80 ? 913  THR A CA  1 
ATOM   105  C  C   . THR A 1 136 ? 118.086 80.784  110.385 1.00 151.60 ? 913  THR A C   1 
ATOM   106  O  O   . THR A 1 136 ? 118.900 81.491  110.987 1.00 151.89 ? 913  THR A O   1 
ATOM   107  C  CB  . THR A 1 136 ? 118.120 80.120  107.972 1.00 153.77 ? 913  THR A CB  1 
ATOM   108  O  OG1 . THR A 1 136 ? 119.538 79.984  108.129 1.00 155.69 ? 913  THR A OG1 1 
ATOM   109  C  CG2 . THR A 1 136 ? 117.811 80.571  106.552 1.00 154.89 ? 913  THR A CG2 1 
ATOM   110  N  N   . PHE A 1 137 ? 117.573 79.667  110.906 1.00 156.30 ? 914  PHE A N   1 
ATOM   111  C  CA  . PHE A 1 137 ? 117.989 79.203  112.226 1.00 157.22 ? 914  PHE A CA  1 
ATOM   112  C  C   . PHE A 1 137 ? 119.468 78.838  112.241 1.00 157.96 ? 914  PHE A C   1 
ATOM   113  O  O   . PHE A 1 137 ? 120.181 79.138  113.206 1.00 157.88 ? 914  PHE A O   1 
ATOM   114  C  CB  . PHE A 1 137 ? 117.140 78.006  112.652 1.00 156.68 ? 914  PHE A CB  1 
ATOM   115  C  CG  . PHE A 1 137 ? 115.772 78.376  113.145 1.00 156.01 ? 914  PHE A CG  1 
ATOM   116  C  CD1 . PHE A 1 137 ? 115.617 79.199  114.248 1.00 156.43 ? 914  PHE A CD1 1 
ATOM   117  C  CD2 . PHE A 1 137 ? 114.640 77.898  112.508 1.00 155.36 ? 914  PHE A CD2 1 
ATOM   118  C  CE1 . PHE A 1 137 ? 114.359 79.539  114.705 1.00 158.10 ? 914  PHE A CE1 1 
ATOM   119  C  CE2 . PHE A 1 137 ? 113.379 78.235  112.960 1.00 155.46 ? 914  PHE A CE2 1 
ATOM   120  C  CZ  . PHE A 1 137 ? 113.238 79.056  114.060 1.00 157.22 ? 914  PHE A CZ  1 
ATOM   121  N  N   . ASP A 1 138 ? 119.947 78.189  111.180 1.00 182.98 ? 915  ASP A N   1 
ATOM   122  C  CA  . ASP A 1 138 ? 121.334 77.751  111.110 1.00 183.70 ? 915  ASP A CA  1 
ATOM   123  C  C   . ASP A 1 138 ? 122.310 78.892  110.855 1.00 183.89 ? 915  ASP A C   1 
ATOM   124  O  O   . ASP A 1 138 ? 123.522 78.685  110.978 1.00 184.38 ? 915  ASP A O   1 
ATOM   125  C  CB  . ASP A 1 138 ? 121.489 76.686  110.023 1.00 184.85 ? 915  ASP A CB  1 
ATOM   126  C  CG  . ASP A 1 138 ? 120.511 75.540  110.190 1.00 184.55 ? 915  ASP A CG  1 
ATOM   127  O  OD1 . ASP A 1 138 ? 120.259 75.136  111.344 1.00 183.91 ? 915  ASP A OD1 1 
ATOM   128  O  OD2 . ASP A 1 138 ? 119.988 75.048  109.169 1.00 184.69 ? 915  ASP A OD2 1 
ATOM   129  N  N   . GLY A 1 139 ? 121.822 80.080  110.505 1.00 176.01 ? 916  GLY A N   1 
ATOM   130  C  CA  . GLY A 1 139 ? 122.666 81.238  110.291 1.00 176.17 ? 916  GLY A CA  1 
ATOM   131  C  C   . GLY A 1 139 ? 122.689 81.758  108.871 1.00 175.57 ? 916  GLY A C   1 
ATOM   132  O  O   . GLY A 1 139 ? 123.283 82.816  108.629 1.00 177.05 ? 916  GLY A O   1 
ATOM   133  N  N   . GLN A 1 140 ? 122.070 81.057  107.925 1.00 164.36 ? 917  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 140 ? 122.046 81.524  106.547 1.00 163.82 ? 917  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 140 ? 121.175 82.768  106.421 1.00 166.22 ? 917  GLN A C   1 
ATOM   136  O  O   . GLN A 1 140 ? 120.102 82.859  107.023 1.00 169.46 ? 917  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 140 ? 121.532 80.422  105.621 1.00 163.94 ? 917  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 140 ? 121.499 80.804  104.151 1.00 165.35 ? 917  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 140 ? 122.816 81.379  103.670 1.00 167.86 ? 917  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 140 ? 123.877 80.791  103.879 1.00 169.37 ? 917  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 140 ? 122.754 82.537  103.023 1.00 168.55 ? 917  GLN A NE2 1 
ATOM   142  N  N   . SER A 1 141 ? 121.647 83.733  105.635 1.00 155.63 ? 918  SER A N   1 
ATOM   143  C  CA  . SER A 1 141 ? 120.936 84.984  105.414 1.00 154.45 ? 918  SER A CA  1 
ATOM   144  C  C   . SER A 1 141 ? 120.743 85.203  103.922 1.00 155.17 ? 918  SER A C   1 
ATOM   145  O  O   . SER A 1 141 ? 121.607 84.846  103.116 1.00 159.39 ? 918  SER A O   1 
ATOM   146  C  CB  . SER A 1 141 ? 121.691 86.170  106.024 1.00 153.68 ? 918  SER A CB  1 
ATOM   147  O  OG  . SER A 1 141 ? 122.923 86.386  105.359 1.00 154.33 ? 918  SER A OG  1 
ATOM   148  N  N   . TYR A 1 142 ? 119.606 85.792  103.561 1.00 139.64 ? 919  TYR A N   1 
ATOM   149  C  CA  . TYR A 1 142 ? 119.282 86.064  102.167 1.00 140.98 ? 919  TYR A CA  1 
ATOM   150  C  C   . TYR A 1 142 ? 118.231 87.166  102.125 1.00 139.82 ? 919  TYR A C   1 
ATOM   151  O  O   . TYR A 1 142 ? 117.856 87.734  103.155 1.00 140.71 ? 919  TYR A O   1 
ATOM   152  C  CB  . TYR A 1 142 ? 118.801 84.797  101.452 1.00 141.38 ? 919  TYR A CB  1 
ATOM   153  C  CG  . TYR A 1 142 ? 117.546 84.194  102.043 1.00 141.22 ? 919  TYR A CG  1 
ATOM   154  C  CD1 . TYR A 1 142 ? 117.613 83.323  103.121 1.00 140.51 ? 919  TYR A CD1 1 
ATOM   155  C  CD2 . TYR A 1 142 ? 116.296 84.492  101.519 1.00 141.97 ? 919  TYR A CD2 1 
ATOM   156  C  CE1 . TYR A 1 142 ? 116.469 82.769  103.664 1.00 139.02 ? 919  TYR A CE1 1 
ATOM   157  C  CE2 . TYR A 1 142 ? 115.147 83.943  102.054 1.00 141.14 ? 919  TYR A CE2 1 
ATOM   158  C  CZ  . TYR A 1 142 ? 115.240 83.082  103.126 1.00 138.79 ? 919  TYR A CZ  1 
ATOM   159  O  OH  . TYR A 1 142 ? 114.099 82.533  103.662 1.00 141.32 ? 919  TYR A OH  1 
ATOM   160  N  N   . SER A 1 143 ? 117.756 87.464  100.918 1.00 131.43 ? 920  SER A N   1 
ATOM   161  C  CA  . SER A 1 143 ? 116.736 88.481  100.712 1.00 131.93 ? 920  SER A CA  1 
ATOM   162  C  C   . SER A 1 143 ? 115.760 88.008  99.647  1.00 132.61 ? 920  SER A C   1 
ATOM   163  O  O   . SER A 1 143 ? 116.168 87.452  98.624  1.00 134.68 ? 920  SER A O   1 
ATOM   164  C  CB  . SER A 1 143 ? 117.356 89.822  100.299 1.00 132.11 ? 920  SER A CB  1 
ATOM   165  O  OG  . SER A 1 143 ? 118.239 90.303  101.297 1.00 131.70 ? 920  SER A OG  1 
ATOM   166  N  N   . PHE A 1 144 ? 114.471 88.233  99.894  1.00 145.95 ? 921  PHE A N   1 
ATOM   167  C  CA  . PHE A 1 144 ? 113.430 87.817  98.965  1.00 146.02 ? 921  PHE A CA  1 
ATOM   168  C  C   . PHE A 1 144 ? 112.182 88.646  99.224  1.00 144.83 ? 921  PHE A C   1 
ATOM   169  O  O   . PHE A 1 144 ? 111.822 88.890  100.377 1.00 146.64 ? 921  PHE A O   1 
ATOM   170  C  CB  . PHE A 1 144 ? 113.121 86.321  99.110  1.00 147.01 ? 921  PHE A CB  1 
ATOM   171  C  CG  . PHE A 1 144 ? 111.710 85.954  98.749  1.00 147.07 ? 921  PHE A CG  1 
ATOM   172  C  CD1 . PHE A 1 144 ? 111.305 85.923  97.426  1.00 149.72 ? 921  PHE A CD1 1 
ATOM   173  C  CD2 . PHE A 1 144 ? 110.790 85.634  99.734  1.00 147.13 ? 921  PHE A CD2 1 
ATOM   174  C  CE1 . PHE A 1 144 ? 110.007 85.584  97.091  1.00 150.18 ? 921  PHE A CE1 1 
ATOM   175  C  CE2 . PHE A 1 144 ? 109.492 85.295  99.405  1.00 149.49 ? 921  PHE A CE2 1 
ATOM   176  C  CZ  . PHE A 1 144 ? 109.100 85.270  98.082  1.00 150.29 ? 921  PHE A CZ  1 
ATOM   177  N  N   . ASN A 1 145 ? 111.527 89.071  98.145  1.00 146.12 ? 922  ASN A N   1 
ATOM   178  C  CA  . ASN A 1 145 ? 110.318 89.877  98.226  1.00 146.39 ? 922  ASN A CA  1 
ATOM   179  C  C   . ASN A 1 145 ? 109.204 89.210  97.434  1.00 148.33 ? 922  ASN A C   1 
ATOM   180  O  O   . ASN A 1 145 ? 109.430 88.704  96.331  1.00 148.34 ? 922  ASN A O   1 
ATOM   181  C  CB  . ASN A 1 145 ? 110.558 91.296  97.698  1.00 147.18 ? 922  ASN A CB  1 
ATOM   182  C  CG  . ASN A 1 145 ? 111.223 91.306  96.337  1.00 150.99 ? 922  ASN A CG  1 
ATOM   183  O  OD1 . ASN A 1 145 ? 111.825 90.316  95.921  1.00 152.60 ? 922  ASN A OD1 1 
ATOM   184  N  ND2 . ASN A 1 145 ? 111.119 92.427  95.635  1.00 151.64 ? 922  ASN A ND2 1 
ATOM   185  N  N   . GLY A 1 146 ? 108.001 89.214  98.004  1.00 154.26 ? 923  GLY A N   1 
ATOM   186  C  CA  . GLY A 1 146 ? 106.849 88.623  97.348  1.00 153.59 ? 923  GLY A CA  1 
ATOM   187  C  C   . GLY A 1 146 ? 105.570 89.217  97.892  1.00 154.44 ? 923  GLY A C   1 
ATOM   188  O  O   . GLY A 1 146 ? 105.561 89.904  98.916  1.00 155.42 ? 923  GLY A O   1 
ATOM   189  N  N   . ASP A 1 147 ? 104.472 88.939  97.182  1.00 183.98 ? 924  ASP A N   1 
ATOM   190  C  CA  . ASP A 1 147 ? 103.144 89.447  97.538  1.00 186.10 ? 924  ASP A CA  1 
ATOM   191  C  C   . ASP A 1 147 ? 102.180 88.263  97.581  1.00 185.68 ? 924  ASP A C   1 
ATOM   192  O  O   . ASP A 1 147 ? 101.468 87.991  96.612  1.00 185.76 ? 924  ASP A O   1 
ATOM   193  C  CB  . ASP A 1 147 ? 102.690 90.520  96.545  1.00 187.46 ? 924  ASP A CB  1 
ATOM   194  C  CG  . ASP A 1 147 ? 101.417 91.222  96.982  1.00 188.25 ? 924  ASP A CG  1 
ATOM   195  O  OD1 . ASP A 1 147 ? 100.915 90.926  98.086  1.00 187.76 ? 924  ASP A OD1 1 
ATOM   196  O  OD2 . ASP A 1 147 ? 100.917 92.073  96.217  1.00 188.41 ? 924  ASP A OD2 1 
ATOM   197  N  N   . CYS A 1 148 ? 102.151 87.579  98.718  1.00 191.88 ? 925  CYS A N   1 
ATOM   198  C  CA  . CYS A 1 148 ? 101.265 86.441  98.957  1.00 192.30 ? 925  CYS A CA  1 
ATOM   199  C  C   . CYS A 1 148 ? 101.406 86.048  100.423 1.00 191.83 ? 925  CYS A C   1 
ATOM   200  O  O   . CYS A 1 148 ? 102.072 86.737  101.206 1.00 191.50 ? 925  CYS A O   1 
ATOM   201  C  CB  . CYS A 1 148 ? 101.586 85.270  98.026  1.00 193.58 ? 925  CYS A CB  1 
ATOM   202  S  SG  . CYS A 1 148 ? 100.352 83.951  98.059  1.00 200.41 ? 925  CYS A SG  1 
ATOM   203  N  N   . GLU A 1 149 ? 100.776 84.938  100.796 1.00 186.12 ? 926  GLU A N   1 
ATOM   204  C  CA  . GLU A 1 149 ? 100.922 84.376  102.131 1.00 186.00 ? 926  GLU A CA  1 
ATOM   205  C  C   . GLU A 1 149 ? 102.012 83.312  102.111 1.00 185.73 ? 926  GLU A C   1 
ATOM   206  O  O   . GLU A 1 149 ? 101.956 82.373  101.311 1.00 187.12 ? 926  GLU A O   1 
ATOM   207  C  CB  . GLU A 1 149 ? 99.602  83.777  102.615 1.00 187.67 ? 926  GLU A CB  1 
ATOM   208  C  CG  . GLU A 1 149 ? 98.431  84.747  102.597 1.00 189.17 ? 926  GLU A CG  1 
ATOM   209  C  CD  . GLU A 1 149 ? 98.496  85.768  103.716 1.00 189.48 ? 926  GLU A CD  1 
ATOM   210  O  OE1 . GLU A 1 149 ? 99.280  85.567  104.667 1.00 189.11 ? 926  GLU A OE1 1 
ATOM   211  O  OE2 . GLU A 1 149 ? 97.758  86.773  103.645 1.00 190.17 ? 926  GLU A OE2 1 
ATOM   212  N  N   . TYR A 1 150 ? 103.000 83.463  102.987 1.00 161.90 ? 927  TYR A N   1 
ATOM   213  C  CA  . TYR A 1 150 ? 104.136 82.556  103.054 1.00 161.97 ? 927  TYR A CA  1 
ATOM   214  C  C   . TYR A 1 150 ? 104.241 81.964  104.452 1.00 162.49 ? 927  TYR A C   1 
ATOM   215  O  O   . TYR A 1 150 ? 104.085 82.673  105.451 1.00 162.32 ? 927  TYR A O   1 
ATOM   216  C  CB  . TYR A 1 150 ? 105.439 83.274  102.687 1.00 161.32 ? 927  TYR A CB  1 
ATOM   217  C  CG  . TYR A 1 150 ? 105.423 83.900  101.311 1.00 161.73 ? 927  TYR A CG  1 
ATOM   218  C  CD1 . TYR A 1 150 ? 104.937 85.187  101.118 1.00 164.11 ? 927  TYR A CD1 1 
ATOM   219  C  CD2 . TYR A 1 150 ? 105.891 83.205  100.204 1.00 162.20 ? 927  TYR A CD2 1 
ATOM   220  C  CE1 . TYR A 1 150 ? 104.919 85.763  99.862  1.00 164.93 ? 927  TYR A CE1 1 
ATOM   221  C  CE2 . TYR A 1 150 ? 105.877 83.773  98.944  1.00 163.37 ? 927  TYR A CE2 1 
ATOM   222  C  CZ  . TYR A 1 150 ? 105.390 85.052  98.779  1.00 163.68 ? 927  TYR A CZ  1 
ATOM   223  O  OH  . TYR A 1 150 ? 105.374 85.623  97.528  1.00 163.86 ? 927  TYR A OH  1 
ATOM   224  N  N   . THR A 1 151 ? 104.508 80.663  104.515 1.00 157.83 ? 928  THR A N   1 
ATOM   225  C  CA  . THR A 1 151 ? 104.614 79.949  105.781 1.00 156.80 ? 928  THR A CA  1 
ATOM   226  C  C   . THR A 1 151 ? 106.050 80.025  106.285 1.00 157.81 ? 928  THR A C   1 
ATOM   227  O  O   . THR A 1 151 ? 106.978 79.573  105.605 1.00 159.63 ? 928  THR A O   1 
ATOM   228  C  CB  . THR A 1 151 ? 104.181 78.493  105.620 1.00 158.28 ? 928  THR A CB  1 
ATOM   229  O  OG1 . THR A 1 151 ? 102.822 78.443  105.171 1.00 160.78 ? 928  THR A OG1 1 
ATOM   230  C  CG2 . THR A 1 151 ? 104.300 77.754  106.944 1.00 159.21 ? 928  THR A CG2 1 
ATOM   231  N  N   . LEU A 1 152 ? 106.232 80.597  107.476 1.00 146.05 ? 929  LEU A N   1 
ATOM   232  C  CA  . LEU A 1 152 ? 107.566 80.709  108.055 1.00 145.06 ? 929  LEU A CA  1 
ATOM   233  C  C   . LEU A 1 152 ? 108.019 79.383  108.656 1.00 146.01 ? 929  LEU A C   1 
ATOM   234  O  O   . LEU A 1 152 ? 109.028 78.809  108.234 1.00 147.95 ? 929  LEU A O   1 
ATOM   235  C  CB  . LEU A 1 152 ? 107.587 81.815  109.114 1.00 142.85 ? 929  LEU A CB  1 
ATOM   236  C  CG  . LEU A 1 152 ? 107.910 83.226  108.622 1.00 142.04 ? 929  LEU A CG  1 
ATOM   237  C  CD1 . LEU A 1 152 ? 108.104 84.169  109.798 1.00 144.18 ? 929  LEU A CD1 1 
ATOM   238  C  CD2 . LEU A 1 152 ? 109.143 83.216  107.733 1.00 143.54 ? 929  LEU A CD2 1 
ATOM   239  N  N   . VAL A 1 153 ? 107.282 78.884  109.645 1.00 158.09 ? 930  VAL A N   1 
ATOM   240  C  CA  . VAL A 1 153 ? 107.604 77.635  110.324 1.00 158.96 ? 930  VAL A CA  1 
ATOM   241  C  C   . VAL A 1 153 ? 106.359 76.761  110.335 1.00 161.97 ? 930  VAL A C   1 
ATOM   242  O  O   . VAL A 1 153 ? 105.294 77.197  110.787 1.00 163.29 ? 930  VAL A O   1 
ATOM   243  C  CB  . VAL A 1 153 ? 108.110 77.880  111.758 1.00 157.91 ? 930  VAL A CB  1 
ATOM   244  C  CG1 . VAL A 1 153 ? 107.978 76.618  112.595 1.00 160.53 ? 930  VAL A CG1 1 
ATOM   245  C  CG2 . VAL A 1 153 ? 109.552 78.361  111.735 1.00 157.87 ? 930  VAL A CG2 1 
ATOM   246  N  N   . GLN A 1 154 ? 106.491 75.534  109.836 1.00 186.68 ? 931  GLN A N   1 
ATOM   247  C  CA  . GLN A 1 154 ? 105.392 74.579  109.804 1.00 187.02 ? 931  GLN A CA  1 
ATOM   248  C  C   . GLN A 1 154 ? 105.842 73.288  110.469 1.00 187.30 ? 931  GLN A C   1 
ATOM   249  O  O   . GLN A 1 154 ? 106.910 72.758  110.145 1.00 186.80 ? 931  GLN A O   1 
ATOM   250  C  CB  . GLN A 1 154 ? 104.931 74.311  108.366 1.00 186.80 ? 931  GLN A CB  1 
ATOM   251  C  CG  . GLN A 1 154 ? 103.865 73.233  108.237 1.00 188.13 ? 931  GLN A CG  1 
ATOM   252  C  CD  . GLN A 1 154 ? 104.445 71.865  107.934 1.00 191.01 ? 931  GLN A CD  1 
ATOM   253  O  OE1 . GLN A 1 154 ? 105.639 71.731  107.669 1.00 193.15 ? 931  GLN A OE1 1 
ATOM   254  N  NE2 . GLN A 1 154 ? 103.601 70.842  107.973 1.00 191.41 ? 931  GLN A NE2 1 
ATOM   255  N  N   . ASN A 1 155 ? 105.030 72.787  111.393 1.00 206.81 ? 932  ASN A N   1 
ATOM   256  C  CA  . ASN A 1 155 ? 105.335 71.559  112.109 1.00 207.52 ? 932  ASN A CA  1 
ATOM   257  C  C   . ASN A 1 155 ? 104.766 70.354  111.369 1.00 209.04 ? 932  ASN A C   1 
ATOM   258  O  O   . ASN A 1 155 ? 103.761 70.455  110.659 1.00 210.27 ? 932  ASN A O   1 
ATOM   259  C  CB  . ASN A 1 155 ? 104.772 71.609  113.531 1.00 208.73 ? 932  ASN A CB  1 
ATOM   260  C  CG  . ASN A 1 155 ? 105.239 70.446  114.385 1.00 209.14 ? 932  ASN A CG  1 
ATOM   261  O  OD1 . ASN A 1 155 ? 106.158 69.717  114.013 1.00 208.77 ? 932  ASN A OD1 1 
ATOM   262  N  ND2 . ASN A 1 155 ? 104.601 70.264  115.535 1.00 209.48 ? 932  ASN A ND2 1 
ATOM   263  N  N   . HIS A 1 156 ? 105.428 69.208  111.544 1.00 223.92 ? 933  HIS A N   1 
ATOM   264  C  CA  . HIS A 1 156 ? 105.001 67.932  110.971 1.00 224.52 ? 933  HIS A CA  1 
ATOM   265  C  C   . HIS A 1 156 ? 104.901 68.026  109.445 1.00 224.88 ? 933  HIS A C   1 
ATOM   266  O  O   . HIS A 1 156 ? 103.825 67.950  108.848 1.00 224.52 ? 933  HIS A O   1 
ATOM   267  C  CB  . HIS A 1 156 ? 103.675 67.473  111.590 1.00 224.79 ? 933  HIS A CB  1 
ATOM   268  C  CG  . HIS A 1 156 ? 103.827 66.837  112.936 1.00 225.73 ? 933  HIS A CG  1 
ATOM   269  N  ND1 . HIS A 1 156 ? 102.756 66.362  113.661 1.00 225.65 ? 933  HIS A ND1 1 
ATOM   270  C  CD2 . HIS A 1 156 ? 104.926 66.598  113.689 1.00 226.16 ? 933  HIS A CD2 1 
ATOM   271  C  CE1 . HIS A 1 156 ? 103.188 65.858  114.802 1.00 226.61 ? 933  HIS A CE1 1 
ATOM   272  N  NE2 . HIS A 1 156 ? 104.502 65.989  114.844 1.00 226.97 ? 933  HIS A NE2 1 
ATOM   273  N  N   . CYS A 1 157 ? 106.070 68.211  108.834 1.00 234.43 ? 934  CYS A N   1 
ATOM   274  C  CA  . CYS A 1 157 ? 106.157 68.283  107.382 1.00 234.89 ? 934  CYS A CA  1 
ATOM   275  C  C   . CYS A 1 157 ? 105.626 67.000  106.754 1.00 235.31 ? 934  CYS A C   1 
ATOM   276  O  O   . CYS A 1 157 ? 105.979 65.895  107.175 1.00 235.99 ? 934  CYS A O   1 
ATOM   277  C  CB  . CYS A 1 157 ? 107.604 68.523  106.953 1.00 235.09 ? 934  CYS A CB  1 
ATOM   278  S  SG  . CYS A 1 157 ? 108.424 69.877  107.824 1.00 239.14 ? 934  CYS A SG  1 
ATOM   279  N  N   . GLY A 1 158 ? 104.776 67.152  105.742 1.00 238.94 ? 935  GLY A N   1 
ATOM   280  C  CA  . GLY A 1 158 ? 104.168 65.990  105.130 1.00 239.32 ? 935  GLY A CA  1 
ATOM   281  C  C   . GLY A 1 158 ? 103.103 65.375  106.027 1.00 240.32 ? 935  GLY A C   1 
ATOM   282  O  O   . GLY A 1 158 ? 102.525 66.021  106.904 1.00 240.43 ? 935  GLY A O   1 
ATOM   283  N  N   . GLY A 1 159 ? 102.850 64.091  105.789 1.00 245.82 ? 936  GLY A N   1 
ATOM   284  C  CA  . GLY A 1 159 ? 101.868 63.346  106.544 1.00 245.74 ? 936  GLY A CA  1 
ATOM   285  C  C   . GLY A 1 159 ? 102.370 62.705  107.816 1.00 245.39 ? 936  GLY A C   1 
ATOM   286  O  O   . GLY A 1 159 ? 101.618 61.972  108.467 1.00 245.11 ? 936  GLY A O   1 
ATOM   287  N  N   . LYS A 1 160 ? 103.619 62.957  108.199 1.00 245.32 ? 937  LYS A N   1 
ATOM   288  C  CA  . LYS A 1 160 ? 104.193 62.347  109.392 1.00 245.46 ? 937  LYS A CA  1 
ATOM   289  C  C   . LYS A 1 160 ? 103.753 63.122  110.628 1.00 245.88 ? 937  LYS A C   1 
ATOM   290  O  O   . LYS A 1 160 ? 104.145 64.279  110.817 1.00 245.76 ? 937  LYS A O   1 
ATOM   291  C  CB  . LYS A 1 160 ? 105.716 62.311  109.290 1.00 245.24 ? 937  LYS A CB  1 
ATOM   292  C  CG  . LYS A 1 160 ? 106.417 61.847  110.559 1.00 245.22 ? 937  LYS A CG  1 
ATOM   293  C  CD  . LYS A 1 160 ? 105.900 60.493  111.019 1.00 244.94 ? 937  LYS A CD  1 
ATOM   294  C  CE  . LYS A 1 160 ? 106.471 60.118  112.377 1.00 245.04 ? 937  LYS A CE  1 
ATOM   295  N  NZ  . LYS A 1 160 ? 105.548 59.236  113.142 1.00 244.56 ? 937  LYS A NZ  1 
ATOM   296  N  N   . ASP A 1 161 ? 102.939 62.486  111.467 1.00 253.35 ? 938  ASP A N   1 
ATOM   297  C  CA  . ASP A 1 161 ? 102.477 63.062  112.728 1.00 253.35 ? 938  ASP A CA  1 
ATOM   298  C  C   . ASP A 1 161 ? 103.124 62.271  113.861 1.00 253.17 ? 938  ASP A C   1 
ATOM   299  O  O   . ASP A 1 161 ? 102.711 61.147  114.160 1.00 253.05 ? 938  ASP A O   1 
ATOM   300  C  CB  . ASP A 1 161 ? 100.954 63.030  112.821 1.00 253.07 ? 938  ASP A CB  1 
ATOM   301  C  CG  . ASP A 1 161 ? 100.283 63.769  111.679 1.00 253.06 ? 938  ASP A CG  1 
ATOM   302  O  OD1 . ASP A 1 161 ? 100.999 64.369  110.851 1.00 252.71 ? 938  ASP A OD1 1 
ATOM   303  O  OD2 . ASP A 1 161 ? 99.036  63.749  111.609 1.00 253.25 ? 938  ASP A OD2 1 
ATOM   304  N  N   . SER A 1 162 ? 104.138 62.862  114.491 1.00 262.60 ? 939  SER A N   1 
ATOM   305  C  CA  . SER A 1 162 ? 104.870 62.183  115.554 1.00 263.24 ? 939  SER A CA  1 
ATOM   306  C  C   . SER A 1 162 ? 104.243 62.444  116.918 1.00 263.91 ? 939  SER A C   1 
ATOM   307  O  O   . SER A 1 162 ? 104.945 62.814  117.865 1.00 264.04 ? 939  SER A O   1 
ATOM   308  C  CB  . SER A 1 162 ? 106.336 62.621  115.554 1.00 262.43 ? 939  SER A CB  1 
ATOM   309  O  OG  . SER A 1 162 ? 107.057 61.988  116.596 1.00 262.85 ? 939  SER A OG  1 
ATOM   310  N  N   . THR A 1 163 ? 102.929 62.239  117.024 1.00 258.37 ? 940  THR A N   1 
ATOM   311  C  CA  . THR A 1 163 ? 102.188 62.380  118.280 1.00 257.79 ? 940  THR A CA  1 
ATOM   312  C  C   . THR A 1 163 ? 102.432 63.745  118.925 1.00 257.74 ? 940  THR A C   1 
ATOM   313  O  O   . THR A 1 163 ? 102.619 63.865  120.138 1.00 257.25 ? 940  THR A O   1 
ATOM   314  C  CB  . THR A 1 163 ? 102.532 61.249  119.252 1.00 257.56 ? 940  THR A CB  1 
ATOM   315  O  OG1 . THR A 1 163 ? 103.876 61.409  119.724 1.00 257.87 ? 940  THR A OG1 1 
ATOM   316  C  CG2 . THR A 1 163 ? 102.399 59.897  118.564 1.00 257.19 ? 940  THR A CG2 1 
ATOM   317  N  N   . GLN A 1 164 ? 102.428 64.785  118.095 1.00 244.25 ? 941  GLN A N   1 
ATOM   318  C  CA  . GLN A 1 164 ? 102.625 66.146  118.572 1.00 243.13 ? 941  GLN A CA  1 
ATOM   319  C  C   . GLN A 1 164 ? 101.635 67.067  117.877 1.00 242.47 ? 941  GLN A C   1 
ATOM   320  O  O   . GLN A 1 164 ? 101.118 66.751  116.802 1.00 242.39 ? 941  GLN A O   1 
ATOM   321  C  CB  . GLN A 1 164 ? 104.058 66.637  118.328 1.00 243.04 ? 941  GLN A CB  1 
ATOM   322  C  CG  . GLN A 1 164 ? 105.133 65.814  119.019 1.00 243.00 ? 941  GLN A CG  1 
ATOM   323  C  CD  . GLN A 1 164 ? 106.534 66.259  118.651 1.00 242.81 ? 941  GLN A CD  1 
ATOM   324  O  OE1 . GLN A 1 164 ? 106.715 67.223  117.907 1.00 242.26 ? 941  GLN A OE1 1 
ATOM   325  N  NE2 . GLN A 1 164 ? 107.534 65.557  119.170 1.00 242.85 ? 941  GLN A NE2 1 
ATOM   326  N  N   . ASP A 1 165 ? 101.369 68.207  118.508 1.00 233.70 ? 942  ASP A N   1 
ATOM   327  C  CA  . ASP A 1 165 ? 100.502 69.207  117.903 1.00 234.30 ? 942  ASP A CA  1 
ATOM   328  C  C   . ASP A 1 165 ? 101.239 69.927  116.781 1.00 234.79 ? 942  ASP A C   1 
ATOM   329  O  O   . ASP A 1 165 ? 102.442 70.189  116.873 1.00 234.65 ? 942  ASP A O   1 
ATOM   330  C  CB  . ASP A 1 165 ? 100.029 70.210  118.956 1.00 234.07 ? 942  ASP A CB  1 
ATOM   331  C  CG  . ASP A 1 165 ? 99.099  71.265  118.386 1.00 234.70 ? 942  ASP A CG  1 
ATOM   332  O  OD1 . ASP A 1 165 ? 98.535  71.043  117.293 1.00 235.36 ? 942  ASP A OD1 1 
ATOM   333  O  OD2 . ASP A 1 165 ? 98.932  72.321  119.032 1.00 234.11 ? 942  ASP A OD2 1 
ATOM   334  N  N   . SER A 1 166 ? 100.511 70.245  115.715 1.00 217.56 ? 943  SER A N   1 
ATOM   335  C  CA  . SER A 1 166 ? 101.077 70.901  114.544 1.00 215.95 ? 943  SER A CA  1 
ATOM   336  C  C   . SER A 1 166 ? 100.799 72.396  114.623 1.00 214.99 ? 943  SER A C   1 
ATOM   337  O  O   . SER A 1 166 ? 99.639  72.811  114.730 1.00 214.23 ? 943  SER A O   1 
ATOM   338  C  CB  . SER A 1 166 ? 100.498 70.312  113.258 1.00 215.28 ? 943  SER A CB  1 
ATOM   339  O  OG  . SER A 1 166 ? 99.100  70.117  113.372 1.00 214.83 ? 943  SER A OG  1 
ATOM   340  N  N   . PHE A 1 167 ? 101.858 73.198  114.571 1.00 188.19 ? 944  PHE A N   1 
ATOM   341  C  CA  . PHE A 1 167 ? 101.751 74.649  114.581 1.00 186.63 ? 944  PHE A CA  1 
ATOM   342  C  C   . PHE A 1 167 ? 102.172 75.201  113.226 1.00 185.96 ? 944  PHE A C   1 
ATOM   343  O  O   . PHE A 1 167 ? 103.100 74.684  112.595 1.00 186.00 ? 944  PHE A O   1 
ATOM   344  C  CB  . PHE A 1 167 ? 102.609 75.264  115.692 1.00 186.58 ? 944  PHE A CB  1 
ATOM   345  C  CG  . PHE A 1 167 ? 103.990 74.679  115.791 1.00 186.45 ? 944  PHE A CG  1 
ATOM   346  C  CD1 . PHE A 1 167 ? 105.023 75.167  115.009 1.00 186.34 ? 944  PHE A CD1 1 
ATOM   347  C  CD2 . PHE A 1 167 ? 104.257 73.646  116.675 1.00 187.93 ? 944  PHE A CD2 1 
ATOM   348  C  CE1 . PHE A 1 167 ? 106.294 74.633  115.101 1.00 186.98 ? 944  PHE A CE1 1 
ATOM   349  C  CE2 . PHE A 1 167 ? 105.527 73.109  116.772 1.00 188.44 ? 944  PHE A CE2 1 
ATOM   350  C  CZ  . PHE A 1 167 ? 106.546 73.603  115.983 1.00 187.53 ? 944  PHE A CZ  1 
ATOM   351  N  N   . ARG A 1 168 ? 101.482 76.248  112.780 1.00 174.60 ? 945  ARG A N   1 
ATOM   352  C  CA  . ARG A 1 168 ? 101.745 76.857  111.482 1.00 173.24 ? 945  ARG A CA  1 
ATOM   353  C  C   . ARG A 1 168 ? 101.625 78.366  111.617 1.00 174.29 ? 945  ARG A C   1 
ATOM   354  O  O   . ARG A 1 168 ? 100.588 78.870  112.056 1.00 176.11 ? 945  ARG A O   1 
ATOM   355  C  CB  . ARG A 1 168 ? 100.773 76.332  110.421 1.00 174.12 ? 945  ARG A CB  1 
ATOM   356  C  CG  . ARG A 1 168 ? 100.896 77.015  109.070 1.00 174.62 ? 945  ARG A CG  1 
ATOM   357  C  CD  . ARG A 1 168 ? 100.099 76.276  108.009 1.00 175.17 ? 945  ARG A CD  1 
ATOM   358  N  NE  . ARG A 1 168 ? 98.806  75.830  108.513 1.00 176.64 ? 945  ARG A NE  1 
ATOM   359  C  CZ  . ARG A 1 168 ? 97.693  76.548  108.459 1.00 175.98 ? 945  ARG A CZ  1 
ATOM   360  N  NH1 . ARG A 1 168 ? 97.676  77.758  107.925 1.00 175.62 ? 945  ARG A NH1 1 
ATOM   361  N  NH2 . ARG A 1 168 ? 96.568  76.039  108.953 1.00 174.36 ? 945  ARG A NH2 1 
ATOM   362  N  N   . VAL A 1 169 ? 102.682 79.080  111.241 1.00 153.36 ? 946  VAL A N   1 
ATOM   363  C  CA  . VAL A 1 169 ? 102.714 80.537  111.281 1.00 152.67 ? 946  VAL A CA  1 
ATOM   364  C  C   . VAL A 1 169 ? 102.923 81.049  109.863 1.00 151.72 ? 946  VAL A C   1 
ATOM   365  O  O   . VAL A 1 169 ? 103.842 80.605  109.166 1.00 154.02 ? 946  VAL A O   1 
ATOM   366  C  CB  . VAL A 1 169 ? 103.816 81.059  112.221 1.00 150.46 ? 946  VAL A CB  1 
ATOM   367  C  CG1 . VAL A 1 169 ? 103.329 81.052  113.660 1.00 151.42 ? 946  VAL A CG1 1 
ATOM   368  C  CG2 . VAL A 1 169 ? 105.076 80.221  112.083 1.00 150.13 ? 946  VAL A CG2 1 
ATOM   369  N  N   . VAL A 1 170 ? 102.067 81.974  109.438 1.00 139.56 ? 947  VAL A N   1 
ATOM   370  C  CA  . VAL A 1 170 ? 102.138 82.551  108.103 1.00 139.33 ? 947  VAL A CA  1 
ATOM   371  C  C   . VAL A 1 170 ? 102.166 84.067  108.221 1.00 141.76 ? 947  VAL A C   1 
ATOM   372  O  O   . VAL A 1 170 ? 101.679 84.644  109.198 1.00 142.34 ? 947  VAL A O   1 
ATOM   373  C  CB  . VAL A 1 170 ? 100.959 82.098  107.212 1.00 140.47 ? 947  VAL A CB  1 
ATOM   374  C  CG1 . VAL A 1 170 ? 101.017 80.597  106.977 1.00 140.96 ? 947  VAL A CG1 1 
ATOM   375  C  CG2 . VAL A 1 170 ? 99.635  82.492  107.844 1.00 142.37 ? 947  VAL A CG2 1 
ATOM   376  N  N   . THR A 1 171 ? 102.750 84.712  107.214 1.00 166.69 ? 948  THR A N   1 
ATOM   377  C  CA  . THR A 1 171 ? 102.865 86.160  107.165 1.00 167.14 ? 948  THR A CA  1 
ATOM   378  C  C   . THR A 1 171 ? 102.209 86.690  105.898 1.00 168.60 ? 948  THR A C   1 
ATOM   379  O  O   . THR A 1 171 ? 102.220 86.034  104.852 1.00 171.74 ? 948  THR A O   1 
ATOM   380  C  CB  . THR A 1 171 ? 104.331 86.614  107.206 1.00 167.16 ? 948  THR A CB  1 
ATOM   381  O  OG1 . THR A 1 171 ? 104.879 86.587  105.882 1.00 166.84 ? 948  THR A OG1 1 
ATOM   382  C  CG2 . THR A 1 171 ? 105.152 85.705  108.107 1.00 168.56 ? 948  THR A CG2 1 
ATOM   383  N  N   . GLU A 1 172 ? 101.637 87.885  106.002 1.00 170.08 ? 949  GLU A N   1 
ATOM   384  C  CA  . GLU A 1 172 ? 101.006 88.562  104.877 1.00 169.40 ? 949  GLU A CA  1 
ATOM   385  C  C   . GLU A 1 172 ? 101.879 89.738  104.465 1.00 169.39 ? 949  GLU A C   1 
ATOM   386  O  O   . GLU A 1 172 ? 102.201 90.597  105.293 1.00 170.12 ? 949  GLU A O   1 
ATOM   387  C  CB  . GLU A 1 172 ? 99.598  89.036  105.240 1.00 171.07 ? 949  GLU A CB  1 
ATOM   388  C  CG  . GLU A 1 172 ? 98.901  89.804  104.130 1.00 172.94 ? 949  GLU A CG  1 
ATOM   389  C  CD  . GLU A 1 172 ? 97.488  90.211  104.500 1.00 175.31 ? 949  GLU A CD  1 
ATOM   390  O  OE1 . GLU A 1 172 ? 97.053  89.893  105.627 1.00 175.77 ? 949  GLU A OE1 1 
ATOM   391  O  OE2 . GLU A 1 172 ? 96.813  90.847  103.665 1.00 175.24 ? 949  GLU A OE2 1 
ATOM   392  N  N   . ASN A 1 173 ? 102.260 89.774  103.192 1.00 170.39 ? 950  ASN A N   1 
ATOM   393  C  CA  . ASN A 1 173 ? 103.112 90.821  102.652 1.00 172.42 ? 950  ASN A CA  1 
ATOM   394  C  C   . ASN A 1 173 ? 102.329 91.666  101.658 1.00 172.48 ? 950  ASN A C   1 
ATOM   395  O  O   . ASN A 1 173 ? 101.572 91.137  100.839 1.00 172.68 ? 950  ASN A O   1 
ATOM   396  C  CB  . ASN A 1 173 ? 104.349 90.227  101.973 1.00 172.73 ? 950  ASN A CB  1 
ATOM   397  C  CG  . ASN A 1 173 ? 105.269 89.524  102.950 1.00 172.65 ? 950  ASN A CG  1 
ATOM   398  O  OD1 . ASN A 1 173 ? 104.967 89.417  104.139 1.00 173.72 ? 950  ASN A OD1 1 
ATOM   399  N  ND2 . ASN A 1 173 ? 106.401 89.039  102.454 1.00 171.02 ? 950  ASN A ND2 1 
ATOM   400  N  N   . VAL A 1 174 ? 102.514 92.980  101.736 1.00 167.98 ? 951  VAL A N   1 
ATOM   401  C  CA  . VAL A 1 174 ? 101.846 93.916  100.836 1.00 166.60 ? 951  VAL A CA  1 
ATOM   402  C  C   . VAL A 1 174 ? 102.895 94.840  100.230 1.00 166.62 ? 951  VAL A C   1 
ATOM   403  O  O   . VAL A 1 174 ? 103.916 95.121  100.874 1.00 168.25 ? 951  VAL A O   1 
ATOM   404  C  CB  . VAL A 1 174 ? 100.755 94.713  101.568 1.00 168.06 ? 951  VAL A CB  1 
ATOM   405  C  CG1 . VAL A 1 174 ? 99.557  93.824  101.864 1.00 168.51 ? 951  VAL A CG1 1 
ATOM   406  C  CG2 . VAL A 1 174 ? 101.309 95.316  102.849 1.00 168.84 ? 951  VAL A CG2 1 
ATOM   407  N  N   . PRO A 1 175 ? 102.698 95.329  99.004  1.00 159.43 ? 952  PRO A N   1 
ATOM   408  C  CA  . PRO A 1 175 ? 103.698 96.219  98.399  1.00 160.25 ? 952  PRO A CA  1 
ATOM   409  C  C   . PRO A 1 175 ? 103.736 97.587  99.061  1.00 161.96 ? 952  PRO A C   1 
ATOM   410  O  O   . PRO A 1 175 ? 102.811 98.389  98.904  1.00 162.68 ? 952  PRO A O   1 
ATOM   411  C  CB  . PRO A 1 175 ? 103.245 96.313  96.936  1.00 159.36 ? 952  PRO A CB  1 
ATOM   412  C  CG  . PRO A 1 175 ? 101.784 96.024  96.975  1.00 158.64 ? 952  PRO A CG  1 
ATOM   413  C  CD  . PRO A 1 175 ? 101.585 95.033  98.084  1.00 159.43 ? 952  PRO A CD  1 
ATOM   414  N  N   . CYS A 1 176 ? 104.805 97.860  99.803  1.00 185.78 ? 953  CYS A N   1 
ATOM   415  C  CA  . CYS A 1 176 ? 105.001 99.140  100.472 1.00 185.13 ? 953  CYS A CA  1 
ATOM   416  C  C   . CYS A 1 176 ? 106.091 99.911  99.740  1.00 185.13 ? 953  CYS A C   1 
ATOM   417  O  O   . CYS A 1 176 ? 107.213 99.417  99.591  1.00 185.51 ? 953  CYS A O   1 
ATOM   418  C  CB  . CYS A 1 176 ? 105.371 98.941  101.942 1.00 185.88 ? 953  CYS A CB  1 
ATOM   419  S  SG  . CYS A 1 176 ? 106.507 97.570  102.254 1.00 192.60 ? 953  CYS A SG  1 
ATOM   420  N  N   . GLY A 1 177 ? 105.759 101.118 99.289  1.00 182.03 ? 954  GLY A N   1 
ATOM   421  C  CA  . GLY A 1 177 ? 106.697 101.929 98.540  1.00 181.90 ? 954  GLY A CA  1 
ATOM   422  C  C   . GLY A 1 177 ? 106.326 102.052 97.077  1.00 181.64 ? 954  GLY A C   1 
ATOM   423  O  O   . GLY A 1 177 ? 105.154 101.913 96.714  1.00 183.04 ? 954  GLY A O   1 
ATOM   424  N  N   . THR A 1 178 ? 107.316 102.314 96.226  1.00 176.12 ? 955  THR A N   1 
ATOM   425  C  CA  . THR A 1 178 ? 107.087 102.443 94.792  1.00 177.25 ? 955  THR A CA  1 
ATOM   426  C  C   . THR A 1 178 ? 108.055 101.647 93.931  1.00 177.34 ? 955  THR A C   1 
ATOM   427  O  O   . THR A 1 178 ? 107.730 101.378 92.769  1.00 177.10 ? 955  THR A O   1 
ATOM   428  C  CB  . THR A 1 178 ? 107.153 103.918 94.366  1.00 178.50 ? 955  THR A CB  1 
ATOM   429  O  OG1 . THR A 1 178 ? 106.944 104.019 92.952  1.00 179.07 ? 955  THR A OG1 1 
ATOM   430  C  CG2 . THR A 1 178 ? 108.506 104.517 94.719  1.00 177.16 ? 955  THR A CG2 1 
ATOM   431  N  N   . THR A 1 179 ? 109.225 101.265 94.448  1.00 177.70 ? 956  THR A N   1 
ATOM   432  C  CA  . THR A 1 179 ? 110.164 100.482 93.652  1.00 178.13 ? 956  THR A CA  1 
ATOM   433  C  C   . THR A 1 179 ? 109.631 99.079  93.389  1.00 177.75 ? 956  THR A C   1 
ATOM   434  O  O   . THR A 1 179 ? 109.783 98.547  92.283  1.00 178.22 ? 956  THR A O   1 
ATOM   435  C  CB  . THR A 1 179 ? 111.521 100.418 94.353  1.00 178.00 ? 956  THR A CB  1 
ATOM   436  O  OG1 . THR A 1 179 ? 111.988 101.748 94.614  1.00 177.62 ? 956  THR A OG1 1 
ATOM   437  C  CG2 . THR A 1 179 ? 112.539 99.694  93.485  1.00 177.83 ? 956  THR A CG2 1 
ATOM   438  N  N   . GLY A 1 180 ? 108.998 98.469  94.387  1.00 165.63 ? 957  GLY A N   1 
ATOM   439  C  CA  . GLY A 1 180 ? 108.465 97.130  94.238  1.00 164.84 ? 957  GLY A CA  1 
ATOM   440  C  C   . GLY A 1 180 ? 108.733 96.248  95.440  1.00 166.82 ? 957  GLY A C   1 
ATOM   441  O  O   . GLY A 1 180 ? 108.399 95.060  95.434  1.00 168.89 ? 957  GLY A O   1 
ATOM   442  N  N   . THR A 1 181 ? 109.339 96.820  96.477  1.00 174.79 ? 958  THR A N   1 
ATOM   443  C  CA  . THR A 1 181 ? 109.630 96.066  97.684  1.00 174.58 ? 958  THR A CA  1 
ATOM   444  C  C   . THR A 1 181 ? 108.346 95.765  98.453  1.00 174.59 ? 958  THR A C   1 
ATOM   445  O  O   . THR A 1 181 ? 107.337 96.467  98.336  1.00 175.89 ? 958  THR A O   1 
ATOM   446  C  CB  . THR A 1 181 ? 110.604 96.833  98.578  1.00 173.90 ? 958  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 181 ? 110.045 98.110  98.911  1.00 173.93 ? 958  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 181 ? 111.931 97.037  97.865  1.00 175.31 ? 958  THR A CG2 1 
ATOM   449  N  N   . THR A 1 182 ? 108.395 94.700  99.249  1.00 177.15 ? 959  THR A N   1 
ATOM   450  C  CA  . THR A 1 182 ? 107.256 94.262  100.041 1.00 179.08 ? 959  THR A CA  1 
ATOM   451  C  C   . THR A 1 182 ? 107.677 94.082  101.492 1.00 178.44 ? 959  THR A C   1 
ATOM   452  O  O   . THR A 1 182 ? 108.807 93.683  101.784 1.00 179.05 ? 959  THR A O   1 
ATOM   453  C  CB  . THR A 1 182 ? 106.669 92.948  99.508  1.00 179.04 ? 959  THR A CB  1 
ATOM   454  O  OG1 . THR A 1 182 ? 107.727 92.013  99.264  1.00 178.80 ? 959  THR A OG1 1 
ATOM   455  C  CG2 . THR A 1 182 ? 105.905 93.191  98.215  1.00 178.81 ? 959  THR A CG2 1 
ATOM   456  N  N   . CYS A 1 183 ? 106.751 94.383  102.399 1.00 179.76 ? 960  CYS A N   1 
ATOM   457  C  CA  . CYS A 1 183 ? 106.983 94.260  103.829 1.00 178.39 ? 960  CYS A CA  1 
ATOM   458  C  C   . CYS A 1 183 ? 105.802 93.554  104.479 1.00 179.55 ? 960  CYS A C   1 
ATOM   459  O  O   . CYS A 1 183 ? 104.670 93.627  103.993 1.00 180.76 ? 960  CYS A O   1 
ATOM   460  C  CB  . CYS A 1 183 ? 107.199 95.632  104.482 1.00 180.54 ? 960  CYS A CB  1 
ATOM   461  S  SG  . CYS A 1 183 ? 105.938 96.860  104.070 1.00 188.10 ? 960  CYS A SG  1 
ATOM   462  N  N   . SER A 1 184 ? 106.080 92.866  105.583 1.00 161.92 ? 961  SER A N   1 
ATOM   463  C  CA  . SER A 1 184 ? 105.038 92.138  106.294 1.00 161.66 ? 961  SER A CA  1 
ATOM   464  C  C   . SER A 1 184 ? 104.042 93.103  106.924 1.00 161.16 ? 961  SER A C   1 
ATOM   465  O  O   . SER A 1 184 ? 104.417 94.152  107.455 1.00 160.38 ? 961  SER A O   1 
ATOM   466  C  CB  . SER A 1 184 ? 105.655 91.244  107.368 1.00 160.18 ? 961  SER A CB  1 
ATOM   467  O  OG  . SER A 1 184 ? 104.704 90.920  108.367 1.00 160.59 ? 961  SER A OG  1 
ATOM   468  N  N   . LYS A 1 185 ? 102.762 92.740  106.864 1.00 155.67 ? 962  LYS A N   1 
ATOM   469  C  CA  . LYS A 1 185 ? 101.692 93.557  107.422 1.00 154.73 ? 962  LYS A CA  1 
ATOM   470  C  C   . LYS A 1 185 ? 100.924 92.842  108.522 1.00 155.42 ? 962  LYS A C   1 
ATOM   471  O  O   . LYS A 1 185 ? 100.697 93.422  109.590 1.00 155.55 ? 962  LYS A O   1 
ATOM   472  C  CB  . LYS A 1 185 ? 100.727 93.994  106.309 1.00 153.68 ? 962  LYS A CB  1 
ATOM   473  C  CG  . LYS A 1 185 ? 99.575  94.859  106.792 1.00 153.77 ? 962  LYS A CG  1 
ATOM   474  C  CD  . LYS A 1 185 ? 98.525  95.036  105.709 1.00 155.44 ? 962  LYS A CD  1 
ATOM   475  C  CE  . LYS A 1 185 ? 97.771  93.742  105.454 1.00 156.60 ? 962  LYS A CE  1 
ATOM   476  N  NZ  . LYS A 1 185 ? 96.339  93.990  105.132 1.00 155.75 ? 962  LYS A NZ  1 
ATOM   477  N  N   . ALA A 1 186 ? 100.517 91.596  108.293 1.00 156.65 ? 963  ALA A N   1 
ATOM   478  C  CA  . ALA A 1 186 ? 99.760  90.829  109.270 1.00 154.86 ? 963  ALA A CA  1 
ATOM   479  C  C   . ALA A 1 186 ? 100.368 89.442  109.415 1.00 154.67 ? 963  ALA A C   1 
ATOM   480  O  O   . ALA A 1 186 ? 100.960 88.903  108.476 1.00 157.12 ? 963  ALA A O   1 
ATOM   481  C  CB  . ALA A 1 186 ? 98.283  90.712  108.873 1.00 155.34 ? 963  ALA A CB  1 
ATOM   482  N  N   . ILE A 1 187 ? 100.215 88.870  110.607 1.00 139.85 ? 964  ILE A N   1 
ATOM   483  C  CA  . ILE A 1 187 ? 100.748 87.551  110.927 1.00 140.53 ? 964  ILE A CA  1 
ATOM   484  C  C   . ILE A 1 187 ? 99.626  86.710  111.518 1.00 144.22 ? 964  ILE A C   1 
ATOM   485  O  O   . ILE A 1 187 ? 98.950  87.142  112.458 1.00 145.99 ? 964  ILE A O   1 
ATOM   486  C  CB  . ILE A 1 187 ? 101.934 87.637  111.907 1.00 137.18 ? 964  ILE A CB  1 
ATOM   487  C  CG1 . ILE A 1 187 ? 103.156 88.232  111.208 1.00 138.80 ? 964  ILE A CG1 1 
ATOM   488  C  CG2 . ILE A 1 187 ? 102.260 86.265  112.476 1.00 139.44 ? 964  ILE A CG2 1 
ATOM   489  C  CD1 . ILE A 1 187 ? 104.376 88.319  112.092 1.00 139.96 ? 964  ILE A CD1 1 
ATOM   490  N  N   . LYS A 1 188 ? 99.430  85.515  110.968 1.00 155.99 ? 965  LYS A N   1 
ATOM   491  C  CA  . LYS A 1 188 ? 98.419  84.583  111.444 1.00 154.98 ? 965  LYS A CA  1 
ATOM   492  C  C   . LYS A 1 188 ? 99.092  83.354  112.040 1.00 154.85 ? 965  LYS A C   1 
ATOM   493  O  O   . LYS A 1 188 ? 100.032 82.805  111.457 1.00 155.26 ? 965  LYS A O   1 
ATOM   494  C  CB  . LYS A 1 188 ? 97.477  84.166  110.312 1.00 154.90 ? 965  LYS A CB  1 
ATOM   495  C  CG  . LYS A 1 188 ? 96.691  85.316  109.704 1.00 154.30 ? 965  LYS A CG  1 
ATOM   496  C  CD  . LYS A 1 188 ? 96.057  84.911  108.384 1.00 155.39 ? 965  LYS A CD  1 
ATOM   497  C  CE  . LYS A 1 188 ? 94.893  85.822  108.029 1.00 156.53 ? 965  LYS A CE  1 
ATOM   498  N  NZ  . LYS A 1 188 ? 95.356  87.115  107.455 1.00 156.30 ? 965  LYS A NZ  1 
ATOM   499  N  N   . ILE A 1 189 ? 98.608  82.929  113.204 1.00 164.03 ? 966  ILE A N   1 
ATOM   500  C  CA  . ILE A 1 189 ? 99.149  81.781  113.921 1.00 163.88 ? 966  ILE A CA  1 
ATOM   501  C  C   . ILE A 1 189 ? 98.070  80.712  114.002 1.00 166.23 ? 966  ILE A C   1 
ATOM   502  O  O   . ILE A 1 189 ? 96.942  80.993  114.424 1.00 168.69 ? 966  ILE A O   1 
ATOM   503  C  CB  . ILE A 1 189 ? 99.642  82.167  115.327 1.00 163.03 ? 966  ILE A CB  1 
ATOM   504  C  CG1 . ILE A 1 189 ? 100.523 83.416  115.260 1.00 164.76 ? 966  ILE A CG1 1 
ATOM   505  C  CG2 . ILE A 1 189 ? 100.393 81.009  115.965 1.00 162.64 ? 966  ILE A CG2 1 
ATOM   506  C  CD1 . ILE A 1 189 ? 101.181 83.771  116.575 1.00 166.07 ? 966  ILE A CD1 1 
ATOM   507  N  N   . PHE A 1 190 ? 98.416  79.491  113.601 1.00 173.04 ? 967  PHE A N   1 
ATOM   508  C  CA  . PHE A 1 190 ? 97.496  78.361  113.629 1.00 172.97 ? 967  PHE A CA  1 
ATOM   509  C  C   . PHE A 1 190 ? 98.109  77.251  114.467 1.00 173.76 ? 967  PHE A C   1 
ATOM   510  O  O   . PHE A 1 190 ? 99.190  76.750  114.141 1.00 174.48 ? 967  PHE A O   1 
ATOM   511  C  CB  . PHE A 1 190 ? 97.193  77.856  112.215 1.00 171.49 ? 967  PHE A CB  1 
ATOM   512  C  CG  . PHE A 1 190 ? 96.518  78.872  111.339 1.00 172.31 ? 967  PHE A CG  1 
ATOM   513  C  CD1 . PHE A 1 190 ? 95.137  78.956  111.292 1.00 172.56 ? 967  PHE A CD1 1 
ATOM   514  C  CD2 . PHE A 1 190 ? 97.265  79.740  110.560 1.00 173.33 ? 967  PHE A CD2 1 
ATOM   515  C  CE1 . PHE A 1 190 ? 94.513  79.888  110.486 1.00 174.04 ? 967  PHE A CE1 1 
ATOM   516  C  CE2 . PHE A 1 190 ? 96.646  80.674  109.752 1.00 173.45 ? 967  PHE A CE2 1 
ATOM   517  C  CZ  . PHE A 1 190 ? 95.268  80.748  109.715 1.00 173.58 ? 967  PHE A CZ  1 
ATOM   518  N  N   . LEU A 1 191 ? 97.420  76.867  115.540 1.00 176.84 ? 968  LEU A N   1 
ATOM   519  C  CA  . LEU A 1 191 ? 97.854  75.749  116.370 1.00 176.07 ? 968  LEU A CA  1 
ATOM   520  C  C   . LEU A 1 191 ? 96.675  75.268  117.203 1.00 176.80 ? 968  LEU A C   1 
ATOM   521  O  O   . LEU A 1 191 ? 95.891  76.082  117.699 1.00 176.96 ? 968  LEU A O   1 
ATOM   522  C  CB  . LEU A 1 191 ? 99.049  76.143  117.258 1.00 174.69 ? 968  LEU A CB  1 
ATOM   523  C  CG  . LEU A 1 191 ? 99.110  77.447  118.071 1.00 173.86 ? 968  LEU A CG  1 
ATOM   524  C  CD1 . LEU A 1 191 ? 98.125  77.501  119.232 1.00 174.03 ? 968  LEU A CD1 1 
ATOM   525  C  CD2 . LEU A 1 191 ? 100.530 77.685  118.570 1.00 174.61 ? 968  LEU A CD2 1 
ATOM   526  N  N   . GLY A 1 192 ? 96.540  73.948  117.326 1.00 188.93 ? 969  GLY A N   1 
ATOM   527  C  CA  . GLY A 1 192 ? 95.471  73.366  118.121 1.00 189.67 ? 969  GLY A CA  1 
ATOM   528  C  C   . GLY A 1 192 ? 94.082  73.800  117.714 1.00 189.26 ? 969  GLY A C   1 
ATOM   529  O  O   . GLY A 1 192 ? 93.177  73.833  118.555 1.00 189.74 ? 969  GLY A O   1 
ATOM   530  N  N   . GLY A 1 193 ? 93.884  74.137  116.441 1.00 192.90 ? 970  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 193 ? 92.604  74.650  116.000 1.00 193.68 ? 970  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 193 ? 92.324  76.082  116.388 1.00 193.89 ? 970  GLY A C   1 
ATOM   533  O  O   . GLY A 1 193 ? 91.195  76.547  116.210 1.00 194.59 ? 970  GLY A O   1 
ATOM   534  N  N   . PHE A 1 194 ? 93.315  76.797  116.912 1.00 200.09 ? 971  PHE A N   1 
ATOM   535  C  CA  . PHE A 1 194 ? 93.161  78.181  117.339 1.00 200.70 ? 971  PHE A CA  1 
ATOM   536  C  C   . PHE A 1 194 ? 93.826  79.099  116.325 1.00 200.71 ? 971  PHE A C   1 
ATOM   537  O  O   . PHE A 1 194 ? 94.969  78.860  115.920 1.00 200.84 ? 971  PHE A O   1 
ATOM   538  C  CB  . PHE A 1 194 ? 93.769  78.397  118.726 1.00 199.68 ? 971  PHE A CB  1 
ATOM   539  C  CG  . PHE A 1 194 ? 93.064  77.651  119.821 1.00 199.24 ? 971  PHE A CG  1 
ATOM   540  C  CD1 . PHE A 1 194 ? 91.832  78.078  120.287 1.00 200.46 ? 971  PHE A CD1 1 
ATOM   541  C  CD2 . PHE A 1 194 ? 93.634  76.522  120.386 1.00 199.22 ? 971  PHE A CD2 1 
ATOM   542  C  CE1 . PHE A 1 194 ? 91.181  77.393  121.295 1.00 201.09 ? 971  PHE A CE1 1 
ATOM   543  C  CE2 . PHE A 1 194 ? 92.988  75.833  121.394 1.00 200.07 ? 971  PHE A CE2 1 
ATOM   544  C  CZ  . PHE A 1 194 ? 91.760  76.269  121.849 1.00 201.05 ? 971  PHE A CZ  1 
ATOM   545  N  N   . GLU A 1 195 ? 93.111  80.145  115.918 1.00 204.27 ? 972  GLU A N   1 
ATOM   546  C  CA  . GLU A 1 195 ? 93.605  81.112  114.948 1.00 203.48 ? 972  GLU A CA  1 
ATOM   547  C  C   . GLU A 1 195 ? 93.765  82.466  115.623 1.00 203.28 ? 972  GLU A C   1 
ATOM   548  O  O   . GLU A 1 195 ? 92.822  82.972  116.240 1.00 204.10 ? 972  GLU A O   1 
ATOM   549  C  CB  . GLU A 1 195 ? 92.659  81.224  113.750 1.00 204.36 ? 972  GLU A CB  1 
ATOM   550  C  CG  . GLU A 1 195 ? 93.073  82.269  112.729 1.00 205.34 ? 972  GLU A CG  1 
ATOM   551  C  CD  . GLU A 1 195 ? 91.979  82.565  111.722 1.00 206.31 ? 972  GLU A CD  1 
ATOM   552  O  OE1 . GLU A 1 195 ? 90.845  82.078  111.914 1.00 206.54 ? 972  GLU A OE1 1 
ATOM   553  O  OE2 . GLU A 1 195 ? 92.253  83.285  110.739 1.00 205.86 ? 972  GLU A OE2 1 
ATOM   554  N  N   . LEU A 1 196 ? 94.956  83.047  115.502 1.00 174.36 ? 973  LEU A N   1 
ATOM   555  C  CA  . LEU A 1 196 ? 95.264  84.350  116.072 1.00 173.45 ? 973  LEU A CA  1 
ATOM   556  C  C   . LEU A 1 196 ? 95.740  85.287  114.972 1.00 173.53 ? 973  LEU A C   1 
ATOM   557  O  O   . LEU A 1 196 ? 96.510  84.887  114.093 1.00 173.47 ? 973  LEU A O   1 
ATOM   558  C  CB  . LEU A 1 196 ? 96.332  84.243  117.166 1.00 172.01 ? 973  LEU A CB  1 
ATOM   559  C  CG  . LEU A 1 196 ? 95.847  83.962  118.590 1.00 173.86 ? 973  LEU A CG  1 
ATOM   560  C  CD1 . LEU A 1 196 ? 95.409  82.513  118.744 1.00 175.41 ? 973  LEU A CD1 1 
ATOM   561  C  CD2 . LEU A 1 196 ? 96.929  84.307  119.601 1.00 173.49 ? 973  LEU A CD2 1 
ATOM   562  N  N   . LYS A 1 197 ? 95.282  86.534  115.026 1.00 170.85 ? 974  LYS A N   1 
ATOM   563  C  CA  . LYS A 1 197 ? 95.638  87.549  114.045 1.00 169.43 ? 974  LYS A CA  1 
ATOM   564  C  C   . LYS A 1 197 ? 96.310  88.723  114.743 1.00 169.36 ? 974  LYS A C   1 
ATOM   565  O  O   . LYS A 1 197 ? 95.855  89.172  115.800 1.00 172.03 ? 974  LYS A O   1 
ATOM   566  C  CB  . LYS A 1 197 ? 94.404  88.033  113.277 1.00 169.87 ? 974  LYS A CB  1 
ATOM   567  C  CG  . LYS A 1 197 ? 94.723  88.780  111.993 1.00 169.34 ? 974  LYS A CG  1 
ATOM   568  C  CD  . LYS A 1 197 ? 93.485  88.931  111.124 1.00 170.54 ? 974  LYS A CD  1 
ATOM   569  C  CE  . LYS A 1 197 ? 93.822  89.561  109.783 1.00 171.74 ? 974  LYS A CE  1 
ATOM   570  N  NZ  . LYS A 1 197 ? 94.315  90.958  109.934 1.00 172.80 ? 974  LYS A NZ  1 
ATOM   571  N  N   . LEU A 1 198 ? 97.392  89.215  114.147 1.00 145.81 ? 975  LEU A N   1 
ATOM   572  C  CA  . LEU A 1 198 ? 98.165  90.334  114.683 1.00 146.31 ? 975  LEU A CA  1 
ATOM   573  C  C   . LEU A 1 198 ? 98.210  91.425  113.618 1.00 147.59 ? 975  LEU A C   1 
ATOM   574  O  O   . LEU A 1 198 ? 99.080  91.420  112.743 1.00 150.96 ? 975  LEU A O   1 
ATOM   575  C  CB  . LEU A 1 198 ? 99.568  89.887  115.090 1.00 146.49 ? 975  LEU A CB  1 
ATOM   576  C  CG  . LEU A 1 198 ? 99.653  88.662  116.001 1.00 146.41 ? 975  LEU A CG  1 
ATOM   577  C  CD1 . LEU A 1 198 ? 101.103 88.319  116.304 1.00 146.72 ? 975  LEU A CD1 1 
ATOM   578  C  CD2 . LEU A 1 198 ? 98.875  88.896  117.285 1.00 148.10 ? 975  LEU A CD2 1 
ATOM   579  N  N   . SER A 1 199 ? 97.269  92.363  113.694 1.00 154.21 ? 976  SER A N   1 
ATOM   580  C  CA  . SER A 1 199 ? 97.186  93.469  112.753 1.00 155.87 ? 976  SER A CA  1 
ATOM   581  C  C   . SER A 1 199 ? 96.917  94.762  113.507 1.00 156.64 ? 976  SER A C   1 
ATOM   582  O  O   . SER A 1 199 ? 96.202  94.766  114.514 1.00 158.36 ? 976  SER A O   1 
ATOM   583  C  CB  . SER A 1 199 ? 96.088  93.233  111.710 1.00 156.26 ? 976  SER A CB  1 
ATOM   584  O  OG  . SER A 1 199 ? 94.800  93.364  112.287 1.00 157.58 ? 976  SER A OG  1 
ATOM   585  N  N   . HIS A 1 200 ? 97.499  95.856  113.011 1.00 154.44 ? 977  HIS A N   1 
ATOM   586  C  CA  . HIS A 1 200 ? 97.326  97.190  113.589 1.00 154.19 ? 977  HIS A CA  1 
ATOM   587  C  C   . HIS A 1 200 ? 97.753  97.239  115.054 1.00 155.05 ? 977  HIS A C   1 
ATOM   588  O  O   . HIS A 1 200 ? 97.209  98.013  115.845 1.00 156.24 ? 977  HIS A O   1 
ATOM   589  C  CB  . HIS A 1 200 ? 95.882  97.678  113.438 1.00 154.84 ? 977  HIS A CB  1 
ATOM   590  C  CG  . HIS A 1 200 ? 95.318  97.479  112.066 1.00 156.41 ? 977  HIS A CG  1 
ATOM   591  N  ND1 . HIS A 1 200 ? 94.638  96.338  111.699 1.00 156.89 ? 977  HIS A ND1 1 
ATOM   592  C  CD2 . HIS A 1 200 ? 95.334  98.276  110.971 1.00 156.57 ? 977  HIS A CD2 1 
ATOM   593  C  CE1 . HIS A 1 200 ? 94.259  96.440  110.437 1.00 155.55 ? 977  HIS A CE1 1 
ATOM   594  N  NE2 . HIS A 1 200 ? 94.668  97.607  109.973 1.00 155.94 ? 977  HIS A NE2 1 
ATOM   595  N  N   . GLY A 1 201 ? 98.728  96.414  115.428 1.00 153.52 ? 978  GLY A N   1 
ATOM   596  C  CA  . GLY A 1 201 ? 99.239  96.422  116.783 1.00 152.90 ? 978  GLY A CA  1 
ATOM   597  C  C   . GLY A 1 201 ? 98.323  95.830  117.827 1.00 153.62 ? 978  GLY A C   1 
ATOM   598  O  O   . GLY A 1 201 ? 98.573  96.012  119.022 1.00 154.97 ? 978  GLY A O   1 
ATOM   599  N  N   . LYS A 1 202 ? 97.268  95.127  117.422 1.00 164.53 ? 979  LYS A N   1 
ATOM   600  C  CA  . LYS A 1 202 ? 96.330  94.520  118.353 1.00 164.95 ? 979  LYS A CA  1 
ATOM   601  C  C   . LYS A 1 202 ? 96.208  93.032  118.059 1.00 166.10 ? 979  LYS A C   1 
ATOM   602  O  O   . LYS A 1 202 ? 96.479  92.571  116.947 1.00 167.01 ? 979  LYS A O   1 
ATOM   603  C  CB  . LYS A 1 202 ? 94.947  95.184  118.279 1.00 164.04 ? 979  LYS A CB  1 
ATOM   604  C  CG  . LYS A 1 202 ? 94.985  96.685  118.041 1.00 165.16 ? 979  LYS A CG  1 
ATOM   605  C  CD  . LYS A 1 202 ? 93.584  97.275  118.022 1.00 166.11 ? 979  LYS A CD  1 
ATOM   606  C  CE  . LYS A 1 202 ? 92.754  96.699  116.887 1.00 166.43 ? 979  LYS A CE  1 
ATOM   607  N  NZ  . LYS A 1 202 ? 93.522  96.627  115.613 1.00 165.36 ? 979  LYS A NZ  1 
ATOM   608  N  N   . VAL A 1 203 ? 95.794  92.282  119.076 1.00 164.55 ? 980  VAL A N   1 
ATOM   609  C  CA  . VAL A 1 203 ? 95.622  90.838  118.978 1.00 163.65 ? 980  VAL A CA  1 
ATOM   610  C  C   . VAL A 1 203 ? 94.138  90.533  118.842 1.00 165.02 ? 980  VAL A C   1 
ATOM   611  O  O   . VAL A 1 203 ? 93.326  90.974  119.666 1.00 166.47 ? 980  VAL A O   1 
ATOM   612  C  CB  . VAL A 1 203 ? 96.219  90.120  120.199 1.00 162.76 ? 980  VAL A CB  1 
ATOM   613  C  CG1 . VAL A 1 203 ? 96.227  88.616  119.977 1.00 162.73 ? 980  VAL A CG1 1 
ATOM   614  C  CG2 . VAL A 1 203 ? 97.620  90.631  120.480 1.00 163.12 ? 980  VAL A CG2 1 
ATOM   615  N  N   . GLU A 1 204 ? 93.782  89.780  117.804 1.00 190.15 ? 981  GLU A N   1 
ATOM   616  C  CA  . GLU A 1 204 ? 92.404  89.374  117.563 1.00 190.48 ? 981  GLU A CA  1 
ATOM   617  C  C   . GLU A 1 204 ? 92.359  87.864  117.397 1.00 190.88 ? 981  GLU A C   1 
ATOM   618  O  O   . GLU A 1 204 ? 93.110  87.302  116.594 1.00 191.50 ? 981  GLU A O   1 
ATOM   619  C  CB  . GLU A 1 204 ? 91.829  90.065  116.323 1.00 191.44 ? 981  GLU A CB  1 
ATOM   620  C  CG  . GLU A 1 204 ? 90.432  89.603  115.949 1.00 192.74 ? 981  GLU A CG  1 
ATOM   621  C  CD  . GLU A 1 204 ? 89.895  90.310  114.720 1.00 194.39 ? 981  GLU A CD  1 
ATOM   622  O  OE1 . GLU A 1 204 ? 90.602  91.188  114.182 1.00 195.04 ? 981  GLU A OE1 1 
ATOM   623  O  OE2 . GLU A 1 204 ? 88.767  89.988  114.292 1.00 194.90 ? 981  GLU A OE2 1 
ATOM   624  N  N   . VAL A 1 205 ? 91.481  87.212  118.155 1.00 186.04 ? 982  VAL A N   1 
ATOM   625  C  CA  . VAL A 1 205 ? 91.334  85.762  118.125 1.00 186.34 ? 982  VAL A CA  1 
ATOM   626  C  C   . VAL A 1 205 ? 90.095  85.414  117.312 1.00 187.42 ? 982  VAL A C   1 
ATOM   627  O  O   . VAL A 1 205 ? 89.019  85.988  117.523 1.00 188.25 ? 982  VAL A O   1 
ATOM   628  C  CB  . VAL A 1 205 ? 91.252  85.180  119.548 1.00 185.41 ? 982  VAL A CB  1 
ATOM   629  C  CG1 . VAL A 1 205 ? 90.247  85.954  120.392 1.00 185.97 ? 982  VAL A CG1 1 
ATOM   630  C  CG2 . VAL A 1 205 ? 90.893  83.702  119.502 1.00 185.45 ? 982  VAL A CG2 1 
ATOM   631  N  N   . ILE A 1 206 ? 90.249  84.485  116.370 1.00 195.94 ? 983  ILE A N   1 
ATOM   632  C  CA  . ILE A 1 206 ? 89.145  84.057  115.519 1.00 195.88 ? 983  ILE A CA  1 
ATOM   633  C  C   . ILE A 1 206 ? 88.829  82.595  115.804 1.00 196.41 ? 983  ILE A C   1 
ATOM   634  O  O   . ILE A 1 206 ? 87.706  82.255  116.191 1.00 196.30 ? 983  ILE A O   1 
ATOM   635  C  CB  . ILE A 1 206 ? 89.468  84.271  114.029 1.00 195.53 ? 983  ILE A CB  1 
ATOM   636  C  CG1 . ILE A 1 206 ? 90.108  85.644  113.811 1.00 195.12 ? 983  ILE A CG1 1 
ATOM   637  C  CG2 . ILE A 1 206 ? 88.212  84.123  113.185 1.00 195.75 ? 983  ILE A CG2 1 
ATOM   638  C  CD1 . ILE A 1 206 ? 91.599  85.592  113.553 1.00 194.91 ? 983  ILE A CD1 1 
ATOM   639  N  N   . GLY A 1 207 ? 89.817  81.724  115.615 1.00 218.38 ? 984  GLY A N   1 
ATOM   640  C  CA  . GLY A 1 207 ? 89.633  80.310  115.876 1.00 219.78 ? 984  GLY A CA  1 
ATOM   641  C  C   . GLY A 1 207 ? 89.481  80.001  117.350 1.00 219.85 ? 984  GLY A C   1 
ATOM   642  O  O   . GLY A 1 207 ? 90.448  80.088  118.113 1.00 219.45 ? 984  GLY A O   1 
ATOM   643  N  N   . THR A 1 208 ? 88.269  79.638  117.763 1.00 236.43 ? 985  THR A N   1 
ATOM   644  C  CA  . THR A 1 208 ? 87.965  79.338  119.155 1.00 236.45 ? 985  THR A CA  1 
ATOM   645  C  C   . THR A 1 208 ? 87.486  77.898  119.268 1.00 237.11 ? 985  THR A C   1 
ATOM   646  O  O   . THR A 1 208 ? 86.610  77.469  118.510 1.00 236.30 ? 985  THR A O   1 
ATOM   647  C  CB  . THR A 1 208 ? 86.900  80.290  119.707 1.00 236.51 ? 985  THR A CB  1 
ATOM   648  O  OG1 . THR A 1 208 ? 85.700  80.170  118.933 1.00 236.56 ? 985  THR A OG1 1 
ATOM   649  C  CG2 . THR A 1 208 ? 87.392  81.729  119.650 1.00 235.71 ? 985  THR A CG2 1 
ATOM   650  N  N   . ASP A 1 209 ? 88.063  77.159  120.212 1.00 269.69 ? 986  ASP A N   1 
ATOM   651  C  CA  . ASP A 1 209 ? 87.689  75.777  120.476 1.00 270.67 ? 986  ASP A CA  1 
ATOM   652  C  C   . ASP A 1 209 ? 87.227  75.656  121.920 1.00 271.52 ? 986  ASP A C   1 
ATOM   653  O  O   . ASP A 1 209 ? 87.940  76.070  122.841 1.00 271.02 ? 986  ASP A O   1 
ATOM   654  C  CB  . ASP A 1 209 ? 88.861  74.827  120.210 1.00 269.99 ? 986  ASP A CB  1 
ATOM   655  C  CG  . ASP A 1 209 ? 88.409  73.410  119.918 1.00 270.33 ? 986  ASP A CG  1 
ATOM   656  O  OD1 . ASP A 1 209 ? 87.246  73.078  120.231 1.00 270.89 ? 986  ASP A OD1 1 
ATOM   657  O  OD2 . ASP A 1 209 ? 89.217  72.627  119.376 1.00 269.92 ? 986  ASP A OD2 1 
ATOM   658  N  N   . GLU A 1 210 ? 86.039  75.091  122.114 1.00 300.36 ? 987  GLU A N   1 
ATOM   659  C  CA  . GLU A 1 210 ? 85.469  74.920  123.451 1.00 300.67 ? 987  GLU A CA  1 
ATOM   660  C  C   . GLU A 1 210 ? 85.896  73.594  124.074 1.00 300.16 ? 987  GLU A C   1 
ATOM   661  O  O   . GLU A 1 210 ? 85.073  72.806  124.539 1.00 299.97 ? 987  GLU A O   1 
ATOM   662  C  CB  . GLU A 1 210 ? 83.951  75.031  123.385 1.00 300.83 ? 987  GLU A CB  1 
ATOM   663  C  CG  . GLU A 1 210 ? 83.451  76.230  122.594 1.00 301.18 ? 987  GLU A CG  1 
ATOM   664  C  CD  . GLU A 1 210 ? 83.717  77.545  123.299 1.00 301.35 ? 987  GLU A CD  1 
ATOM   665  O  OE1 . GLU A 1 210 ? 83.736  77.559  124.548 1.00 301.47 ? 987  GLU A OE1 1 
ATOM   666  O  OE2 . GLU A 1 210 ? 83.906  78.566  122.604 1.00 301.14 ? 987  GLU A OE2 1 
ATOM   667  N  N   . SER A 1 211 ? 87.202  73.345  124.088 1.00 278.48 ? 988  SER A N   1 
ATOM   668  C  CA  . SER A 1 211 ? 87.748  72.116  124.647 1.00 277.82 ? 988  SER A CA  1 
ATOM   669  C  C   . SER A 1 211 ? 89.226  72.330  124.937 1.00 277.64 ? 988  SER A C   1 
ATOM   670  O  O   . SER A 1 211 ? 89.824  73.325  124.519 1.00 277.34 ? 988  SER A O   1 
ATOM   671  C  CB  . SER A 1 211 ? 87.541  70.929  123.700 1.00 277.66 ? 988  SER A CB  1 
ATOM   672  O  OG  . SER A 1 211 ? 88.040  69.731  124.268 1.00 277.49 ? 988  SER A OG  1 
ATOM   673  N  N   . GLN A 1 212 ? 89.803  71.377  125.666 1.00 275.68 ? 989  GLN A N   1 
ATOM   674  C  CA  . GLN A 1 212 ? 91.229  71.371  126.024 1.00 275.93 ? 989  GLN A CA  1 
ATOM   675  C  C   . GLN A 1 212 ? 91.509  72.636  126.833 1.00 275.64 ? 989  GLN A C   1 
ATOM   676  O  O   . GLN A 1 212 ? 90.781  72.909  127.801 1.00 275.43 ? 989  GLN A O   1 
ATOM   677  C  CB  . GLN A 1 212 ? 92.065  71.192  124.761 1.00 275.98 ? 989  GLN A CB  1 
ATOM   678  C  CG  . GLN A 1 212 ? 93.445  70.601  125.005 1.00 276.33 ? 989  GLN A CG  1 
ATOM   679  C  CD  . GLN A 1 212 ? 93.394  69.123  125.339 1.00 276.51 ? 989  GLN A CD  1 
ATOM   680  O  OE1 . GLN A 1 212 ? 93.596  68.727  126.487 1.00 276.82 ? 989  GLN A OE1 1 
ATOM   681  N  NE2 . GLN A 1 212 ? 93.122  68.298  124.334 1.00 276.32 ? 989  GLN A NE2 1 
ATOM   682  N  N   . GLU A 1 213 ? 92.524  73.426  126.487 1.00 257.51 ? 990  GLU A N   1 
ATOM   683  C  CA  . GLU A 1 213 ? 92.873  74.615  127.250 1.00 257.19 ? 990  GLU A CA  1 
ATOM   684  C  C   . GLU A 1 213 ? 93.666  75.549  126.348 1.00 256.10 ? 990  GLU A C   1 
ATOM   685  O  O   . GLU A 1 213 ? 94.435  75.089  125.500 1.00 256.06 ? 990  GLU A O   1 
ATOM   686  C  CB  . GLU A 1 213 ? 93.679  74.247  128.504 1.00 257.00 ? 990  GLU A CB  1 
ATOM   687  C  CG  . GLU A 1 213 ? 94.374  75.413  129.191 1.00 257.06 ? 990  GLU A CG  1 
ATOM   688  C  CD  . GLU A 1 213 ? 93.399  76.449  129.715 1.00 257.19 ? 990  GLU A CD  1 
ATOM   689  O  OE1 . GLU A 1 213 ? 92.289  76.063  130.138 1.00 257.35 ? 990  GLU A OE1 1 
ATOM   690  O  OE2 . GLU A 1 213 ? 93.742  77.650  129.704 1.00 257.05 ? 990  GLU A OE2 1 
ATOM   691  N  N   . VAL A 1 214 ? 93.467  76.852  126.529 1.00 214.52 ? 991  VAL A N   1 
ATOM   692  C  CA  . VAL A 1 214 ? 94.166  77.861  125.737 1.00 212.23 ? 991  VAL A CA  1 
ATOM   693  C  C   . VAL A 1 214 ? 95.662  77.740  126.003 1.00 212.16 ? 991  VAL A C   1 
ATOM   694  O  O   . VAL A 1 214 ? 96.099  77.853  127.158 1.00 212.25 ? 991  VAL A O   1 
ATOM   695  C  CB  . VAL A 1 214 ? 93.653  79.275  126.056 1.00 211.61 ? 991  VAL A CB  1 
ATOM   696  C  CG1 . VAL A 1 214 ? 94.688  80.321  125.668 1.00 211.42 ? 991  VAL A CG1 1 
ATOM   697  C  CG2 . VAL A 1 214 ? 92.333  79.532  125.345 1.00 211.78 ? 991  VAL A CG2 1 
ATOM   698  N  N   . PRO A 1 215 ? 96.478  77.501  124.978 1.00 199.15 ? 992  PRO A N   1 
ATOM   699  C  CA  . PRO A 1 215 ? 97.924  77.307  125.180 1.00 199.51 ? 992  PRO A CA  1 
ATOM   700  C  C   . PRO A 1 215 ? 98.788  78.546  124.978 1.00 198.51 ? 992  PRO A C   1 
ATOM   701  O  O   . PRO A 1 215 ? 100.013 78.429  125.089 1.00 198.39 ? 992  PRO A O   1 
ATOM   702  C  CB  . PRO A 1 215 ? 98.247  76.258  124.112 1.00 199.55 ? 992  PRO A CB  1 
ATOM   703  C  CG  . PRO A 1 215 ? 97.302  76.581  122.984 1.00 199.08 ? 992  PRO A CG  1 
ATOM   704  C  CD  . PRO A 1 215 ? 96.085  77.262  123.579 1.00 198.18 ? 992  PRO A CD  1 
ATOM   705  N  N   . TYR A 1 216 ? 98.203  79.704  124.691 1.00 197.35 ? 993  TYR A N   1 
ATOM   706  C  CA  . TYR A 1 216 ? 98.961  80.914  124.409 1.00 197.43 ? 993  TYR A CA  1 
ATOM   707  C  C   . TYR A 1 216 ? 98.717  81.956  125.492 1.00 197.17 ? 993  TYR A C   1 
ATOM   708  O  O   . TYR A 1 216 ? 97.603  82.081  126.010 1.00 197.70 ? 993  TYR A O   1 
ATOM   709  C  CB  . TYR A 1 216 ? 98.592  81.487  123.036 1.00 198.27 ? 993  TYR A CB  1 
ATOM   710  C  CG  . TYR A 1 216 ? 97.118  81.780  122.855 1.00 198.24 ? 993  TYR A CG  1 
ATOM   711  C  CD1 . TYR A 1 216 ? 96.587  83.016  123.202 1.00 197.61 ? 993  TYR A CD1 1 
ATOM   712  C  CD2 . TYR A 1 216 ? 96.259  80.822  122.334 1.00 199.40 ? 993  TYR A CD2 1 
ATOM   713  C  CE1 . TYR A 1 216 ? 95.243  83.287  123.037 1.00 198.68 ? 993  TYR A CE1 1 
ATOM   714  C  CE2 . TYR A 1 216 ? 94.914  81.085  122.165 1.00 199.95 ? 993  TYR A CE2 1 
ATOM   715  C  CZ  . TYR A 1 216 ? 94.411  82.319  122.519 1.00 199.96 ? 993  TYR A CZ  1 
ATOM   716  O  OH  . TYR A 1 216 ? 93.071  82.585  122.353 1.00 199.68 ? 993  TYR A OH  1 
ATOM   717  N  N   . THR A 1 217 ? 99.770  82.696  125.833 1.00 176.53 ? 994  THR A N   1 
ATOM   718  C  CA  . THR A 1 217 ? 99.698  83.782  126.801 1.00 175.63 ? 994  THR A CA  1 
ATOM   719  C  C   . THR A 1 217 ? 100.233 85.048  126.152 1.00 175.03 ? 994  THR A C   1 
ATOM   720  O  O   . THR A 1 217 ? 101.253 85.008  125.458 1.00 175.64 ? 994  THR A O   1 
ATOM   721  C  CB  . THR A 1 217 ? 100.496 83.460  128.069 1.00 175.67 ? 994  THR A CB  1 
ATOM   722  O  OG1 . THR A 1 217 ? 101.874 83.262  127.731 1.00 176.90 ? 994  THR A OG1 1 
ATOM   723  C  CG2 . THR A 1 217 ? 99.956  82.203  128.736 1.00 176.28 ? 994  THR A CG2 1 
ATOM   724  N  N   . ILE A 1 218 ? 99.549  86.166  126.379 1.00 170.84 ? 995  ILE A N   1 
ATOM   725  C  CA  . ILE A 1 218 ? 99.911  87.447  125.786 1.00 170.34 ? 995  ILE A CA  1 
ATOM   726  C  C   . ILE A 1 218 ? 100.588 88.305  126.844 1.00 171.58 ? 995  ILE A C   1 
ATOM   727  O  O   . ILE A 1 218 ? 100.035 88.518  127.931 1.00 173.51 ? 995  ILE A O   1 
ATOM   728  C  CB  . ILE A 1 218 ? 98.679  88.161  125.205 1.00 170.78 ? 995  ILE A CB  1 
ATOM   729  C  CG1 . ILE A 1 218 ? 97.788  87.167  124.458 1.00 171.53 ? 995  ILE A CG1 1 
ATOM   730  C  CG2 . ILE A 1 218 ? 99.105  89.294  124.285 1.00 170.05 ? 995  ILE A CG2 1 
ATOM   731  C  CD1 . ILE A 1 218 ? 98.453  86.533  123.255 1.00 171.30 ? 995  ILE A CD1 1 
ATOM   732  N  N   . ARG A 1 219 ? 101.784 88.797  126.530 1.00 174.95 ? 996  ARG A N   1 
ATOM   733  C  CA  . ARG A 1 219 ? 102.541 89.660  127.423 1.00 174.58 ? 996  ARG A CA  1 
ATOM   734  C  C   . ARG A 1 219 ? 103.026 90.881  126.658 1.00 174.15 ? 996  ARG A C   1 
ATOM   735  O  O   . ARG A 1 219 ? 103.248 90.827  125.445 1.00 175.73 ? 996  ARG A O   1 
ATOM   736  C  CB  . ARG A 1 219 ? 103.738 88.924  128.044 1.00 174.14 ? 996  ARG A CB  1 
ATOM   737  C  CG  . ARG A 1 219 ? 103.371 87.648  128.782 1.00 174.20 ? 996  ARG A CG  1 
ATOM   738  C  CD  . ARG A 1 219 ? 104.079 87.564  130.124 1.00 173.99 ? 996  ARG A CD  1 
ATOM   739  N  NE  . ARG A 1 219 ? 105.528 87.508  129.976 1.00 174.19 ? 996  ARG A NE  1 
ATOM   740  C  CZ  . ARG A 1 219 ? 106.230 86.385  129.900 1.00 175.48 ? 996  ARG A CZ  1 
ATOM   741  N  NH1 . ARG A 1 219 ? 105.645 85.200  129.954 1.00 175.96 ? 996  ARG A NH1 1 
ATOM   742  N  NH2 . ARG A 1 219 ? 107.551 86.454  129.766 1.00 176.11 ? 996  ARG A NH2 1 
ATOM   743  N  N   . GLN A 1 220 ? 103.188 91.987  127.379 1.00 170.09 ? 997  GLN A N   1 
ATOM   744  C  CA  . GLN A 1 220 ? 103.642 93.255  126.811 1.00 170.26 ? 997  GLN A CA  1 
ATOM   745  C  C   . GLN A 1 220 ? 104.893 93.687  127.571 1.00 171.01 ? 997  GLN A C   1 
ATOM   746  O  O   . GLN A 1 220 ? 104.806 94.337  128.616 1.00 171.98 ? 997  GLN A O   1 
ATOM   747  C  CB  . GLN A 1 220 ? 102.543 94.314  126.885 1.00 170.54 ? 997  GLN A CB  1 
ATOM   748  C  CG  . GLN A 1 220 ? 102.916 95.642  126.248 1.00 172.49 ? 997  GLN A CG  1 
ATOM   749  C  CD  . GLN A 1 220 ? 102.478 95.739  124.801 1.00 173.32 ? 997  GLN A CD  1 
ATOM   750  O  OE1 . GLN A 1 220 ? 103.056 96.487  124.013 1.00 172.46 ? 997  GLN A OE1 1 
ATOM   751  N  NE2 . GLN A 1 220 ? 101.449 94.980  124.443 1.00 173.46 ? 997  GLN A NE2 1 
ATOM   752  N  N   . MET A 1 221 ? 106.057 93.325  127.041 1.00 171.13 ? 998  MET A N   1 
ATOM   753  C  CA  . MET A 1 221 ? 107.342 93.668  127.638 1.00 171.62 ? 998  MET A CA  1 
ATOM   754  C  C   . MET A 1 221 ? 108.067 94.641  126.720 1.00 172.01 ? 998  MET A C   1 
ATOM   755  O  O   . MET A 1 221 ? 108.327 94.322  125.554 1.00 173.35 ? 998  MET A O   1 
ATOM   756  C  CB  . MET A 1 221 ? 108.189 92.418  127.874 1.00 171.45 ? 998  MET A CB  1 
ATOM   757  C  CG  . MET A 1 221 ? 107.632 91.482  128.933 1.00 173.01 ? 998  MET A CG  1 
ATOM   758  S  SD  . MET A 1 221 ? 108.779 90.159  129.360 1.00 175.05 ? 998  MET A SD  1 
ATOM   759  C  CE  . MET A 1 221 ? 108.663 89.128  127.900 1.00 174.32 ? 998  MET A CE  1 
ATOM   760  N  N   . GLY A 1 222 ? 108.398 95.817  127.248 1.00 168.32 ? 999  GLY A N   1 
ATOM   761  C  CA  . GLY A 1 222 ? 109.077 96.821  126.448 1.00 168.24 ? 999  GLY A CA  1 
ATOM   762  C  C   . GLY A 1 222 ? 108.233 97.260  125.270 1.00 167.24 ? 999  GLY A C   1 
ATOM   763  O  O   . GLY A 1 222 ? 107.039 97.551  125.400 1.00 168.21 ? 999  GLY A O   1 
ATOM   764  N  N   . ILE A 1 223 ? 108.862 97.308  124.092 1.00 147.89 ? 1000 ILE A N   1 
ATOM   765  C  CA  . ILE A 1 223 ? 108.155 97.676  122.868 1.00 147.84 ? 1000 ILE A CA  1 
ATOM   766  C  C   . ILE A 1 223 ? 107.692 96.467  122.071 1.00 149.49 ? 1000 ILE A C   1 
ATOM   767  O  O   . ILE A 1 223 ? 106.996 96.636  121.057 1.00 154.12 ? 1000 ILE A O   1 
ATOM   768  C  CB  . ILE A 1 223 ? 109.034 98.565  121.966 1.00 148.15 ? 1000 ILE A CB  1 
ATOM   769  C  CG1 . ILE A 1 223 ? 110.094 97.721  121.257 1.00 146.65 ? 1000 ILE A CG1 1 
ATOM   770  C  CG2 . ILE A 1 223 ? 109.683 99.671  122.780 1.00 149.91 ? 1000 ILE A CG2 1 
ATOM   771  C  CD1 . ILE A 1 223 ? 110.919 98.494  120.254 1.00 149.89 ? 1000 ILE A CD1 1 
ATOM   772  N  N   . TYR A 1 224 ? 108.048 95.258  122.490 1.00 151.27 ? 1001 TYR A N   1 
ATOM   773  C  CA  . TYR A 1 224 ? 107.676 94.051  121.769 1.00 152.04 ? 1001 TYR A CA  1 
ATOM   774  C  C   . TYR A 1 224 ? 106.401 93.449  122.346 1.00 152.39 ? 1001 TYR A C   1 
ATOM   775  O  O   . TYR A 1 224 ? 106.068 93.649  123.517 1.00 152.57 ? 1001 TYR A O   1 
ATOM   776  C  CB  . TYR A 1 224 ? 108.805 93.021  121.822 1.00 151.29 ? 1001 TYR A CB  1 
ATOM   777  C  CG  . TYR A 1 224 ? 110.046 93.431  121.064 1.00 151.51 ? 1001 TYR A CG  1 
ATOM   778  C  CD1 . TYR A 1 224 ? 110.079 93.398  119.677 1.00 152.59 ? 1001 TYR A CD1 1 
ATOM   779  C  CD2 . TYR A 1 224 ? 111.186 93.851  121.737 1.00 152.75 ? 1001 TYR A CD2 1 
ATOM   780  C  CE1 . TYR A 1 224 ? 111.212 93.771  118.981 1.00 155.14 ? 1001 TYR A CE1 1 
ATOM   781  C  CE2 . TYR A 1 224 ? 112.323 94.226  121.049 1.00 154.13 ? 1001 TYR A CE2 1 
ATOM   782  C  CZ  . TYR A 1 224 ? 112.331 94.185  119.671 1.00 155.56 ? 1001 TYR A CZ  1 
ATOM   783  O  OH  . TYR A 1 224 ? 113.462 94.558  118.982 1.00 156.27 ? 1001 TYR A OH  1 
ATOM   784  N  N   . LEU A 1 225 ? 105.690 92.706  121.505 1.00 152.18 ? 1002 LEU A N   1 
ATOM   785  C  CA  . LEU A 1 225 ? 104.469 92.002  121.888 1.00 150.32 ? 1002 LEU A CA  1 
ATOM   786  C  C   . LEU A 1 225 ? 104.818 90.519  121.981 1.00 150.76 ? 1002 LEU A C   1 
ATOM   787  O  O   . LEU A 1 225 ? 104.741 89.783  120.996 1.00 155.03 ? 1002 LEU A O   1 
ATOM   788  C  CB  . LEU A 1 225 ? 103.349 92.262  120.886 1.00 150.58 ? 1002 LEU A CB  1 
ATOM   789  C  CG  . LEU A 1 225 ? 101.996 91.616  121.183 1.00 151.39 ? 1002 LEU A CG  1 
ATOM   790  C  CD1 . LEU A 1 225 ? 101.538 91.954  122.592 1.00 153.58 ? 1002 LEU A CD1 1 
ATOM   791  C  CD2 . LEU A 1 225 ? 100.966 92.061  120.159 1.00 151.77 ? 1002 LEU A CD2 1 
ATOM   792  N  N   . VAL A 1 226 ? 105.204 90.086  123.175 1.00 147.56 ? 1003 VAL A N   1 
ATOM   793  C  CA  . VAL A 1 226 ? 105.702 88.733  123.392 1.00 148.03 ? 1003 VAL A CA  1 
ATOM   794  C  C   . VAL A 1 226 ? 104.529 87.801  123.655 1.00 149.07 ? 1003 VAL A C   1 
ATOM   795  O  O   . VAL A 1 226 ? 103.698 88.062  124.533 1.00 152.28 ? 1003 VAL A O   1 
ATOM   796  C  CB  . VAL A 1 226 ? 106.703 88.700  124.560 1.00 149.53 ? 1003 VAL A CB  1 
ATOM   797  C  CG1 . VAL A 1 226 ? 106.913 87.273  125.044 1.00 149.22 ? 1003 VAL A CG1 1 
ATOM   798  C  CG2 . VAL A 1 226 ? 108.021 89.330  124.144 1.00 150.67 ? 1003 VAL A CG2 1 
ATOM   799  N  N   . VAL A 1 227 ? 104.461 86.712  122.894 1.00 145.19 ? 1004 VAL A N   1 
ATOM   800  C  CA  . VAL A 1 227 ? 103.489 85.649  123.110 1.00 144.98 ? 1004 VAL A CA  1 
ATOM   801  C  C   . VAL A 1 227 ? 104.250 84.369  123.425 1.00 144.78 ? 1004 VAL A C   1 
ATOM   802  O  O   . VAL A 1 227 ? 105.334 84.128  122.881 1.00 146.01 ? 1004 VAL A O   1 
ATOM   803  C  CB  . VAL A 1 227 ? 102.556 85.459  121.895 1.00 142.79 ? 1004 VAL A CB  1 
ATOM   804  C  CG1 . VAL A 1 227 ? 101.824 86.755  121.586 1.00 143.89 ? 1004 VAL A CG1 1 
ATOM   805  C  CG2 . VAL A 1 227 ? 103.336 84.989  120.680 1.00 142.87 ? 1004 VAL A CG2 1 
ATOM   806  N  N   . ASP A 1 228 ? 103.694 83.560  124.324 1.00 187.00 ? 1005 ASP A N   1 
ATOM   807  C  CA  . ASP A 1 228 ? 104.348 82.345  124.785 1.00 188.53 ? 1005 ASP A CA  1 
ATOM   808  C  C   . ASP A 1 228 ? 103.407 81.161  124.631 1.00 189.87 ? 1005 ASP A C   1 
ATOM   809  O  O   . ASP A 1 228 ? 102.209 81.266  124.910 1.00 191.04 ? 1005 ASP A O   1 
ATOM   810  C  CB  . ASP A 1 228 ? 104.793 82.474  126.247 1.00 191.42 ? 1005 ASP A CB  1 
ATOM   811  C  CG  . ASP A 1 228 ? 105.662 81.315  126.697 1.00 191.82 ? 1005 ASP A CG  1 
ATOM   812  O  OD1 . ASP A 1 228 ? 106.135 80.551  125.829 1.00 192.16 ? 1005 ASP A OD1 1 
ATOM   813  O  OD2 . ASP A 1 228 ? 105.874 81.169  127.919 1.00 191.94 ? 1005 ASP A OD2 1 
ATOM   814  N  N   . THR A 1 229 ? 103.960 80.036  124.186 1.00 192.40 ? 1006 THR A N   1 
ATOM   815  C  CA  . THR A 1 229 ? 103.218 78.796  124.027 1.00 193.20 ? 1006 THR A CA  1 
ATOM   816  C  C   . THR A 1 229 ? 103.856 77.706  124.877 1.00 193.34 ? 1006 THR A C   1 
ATOM   817  O  O   . THR A 1 229 ? 105.066 77.713  125.121 1.00 193.43 ? 1006 THR A O   1 
ATOM   818  C  CB  . THR A 1 229 ? 103.175 78.351  122.560 1.00 193.47 ? 1006 THR A CB  1 
ATOM   819  O  OG1 . THR A 1 229 ? 104.468 77.878  122.165 1.00 193.30 ? 1006 THR A OG1 1 
ATOM   820  C  CG2 . THR A 1 229 ? 102.762 79.507  121.661 1.00 193.55 ? 1006 THR A CG2 1 
ATOM   821  N  N   . ASP A 1 230 ? 103.025 76.764  125.329 1.00 208.77 ? 1007 ASP A N   1 
ATOM   822  C  CA  . ASP A 1 230 ? 103.510 75.692  126.191 1.00 209.42 ? 1007 ASP A CA  1 
ATOM   823  C  C   . ASP A 1 230 ? 104.348 74.669  125.436 1.00 209.59 ? 1007 ASP A C   1 
ATOM   824  O  O   . ASP A 1 230 ? 105.123 73.940  126.064 1.00 209.97 ? 1007 ASP A O   1 
ATOM   825  C  CB  . ASP A 1 230 ? 102.333 74.995  126.873 1.00 209.81 ? 1007 ASP A CB  1 
ATOM   826  C  CG  . ASP A 1 230 ? 101.140 74.835  125.953 1.00 210.46 ? 1007 ASP A CG  1 
ATOM   827  O  OD1 . ASP A 1 230 ? 101.241 75.238  124.775 1.00 209.80 ? 1007 ASP A OD1 1 
ATOM   828  O  OD2 . ASP A 1 230 ? 100.103 74.307  126.406 1.00 211.32 ? 1007 ASP A OD2 1 
ATOM   829  N  N   . ILE A 1 231 ? 104.210 74.594  124.110 1.00 193.22 ? 1008 ILE A N   1 
ATOM   830  C  CA  . ILE A 1 231 ? 104.976 73.615  123.345 1.00 192.78 ? 1008 ILE A CA  1 
ATOM   831  C  C   . ILE A 1 231 ? 106.458 73.973  123.335 1.00 192.70 ? 1008 ILE A C   1 
ATOM   832  O  O   . ILE A 1 231 ? 107.318 73.084  123.291 1.00 193.28 ? 1008 ILE A O   1 
ATOM   833  C  CB  . ILE A 1 231 ? 104.405 73.486  121.919 1.00 191.49 ? 1008 ILE A CB  1 
ATOM   834  C  CG1 . ILE A 1 231 ? 105.126 72.379  121.146 1.00 192.19 ? 1008 ILE A CG1 1 
ATOM   835  C  CG2 . ILE A 1 231 ? 104.490 74.809  121.174 1.00 190.23 ? 1008 ILE A CG2 1 
ATOM   836  C  CD1 . ILE A 1 231 ? 104.915 70.996  121.721 1.00 192.55 ? 1008 ILE A CD1 1 
ATOM   837  N  N   . GLY A 1 232 ? 106.786 75.262  123.391 1.00 182.30 ? 1009 GLY A N   1 
ATOM   838  C  CA  . GLY A 1 232 ? 108.172 75.684  123.410 1.00 181.92 ? 1009 GLY A CA  1 
ATOM   839  C  C   . GLY A 1 232 ? 108.534 76.619  122.275 1.00 180.92 ? 1009 GLY A C   1 
ATOM   840  O  O   . GLY A 1 232 ? 109.703 76.719  121.892 1.00 182.02 ? 1009 GLY A O   1 
ATOM   841  N  N   . LEU A 1 233 ? 107.537 77.309  121.729 1.00 163.43 ? 1010 LEU A N   1 
ATOM   842  C  CA  . LEU A 1 233 ? 107.729 78.250  120.634 1.00 162.93 ? 1010 LEU A CA  1 
ATOM   843  C  C   . LEU A 1 233 ? 107.190 79.611  121.050 1.00 163.82 ? 1010 LEU A C   1 
ATOM   844  O  O   . LEU A 1 233 ? 106.047 79.717  121.505 1.00 166.87 ? 1010 LEU A O   1 
ATOM   845  C  CB  . LEU A 1 233 ? 107.037 77.751  119.359 1.00 163.21 ? 1010 LEU A CB  1 
ATOM   846  C  CG  . LEU A 1 233 ? 106.807 78.711  118.190 1.00 161.62 ? 1010 LEU A CG  1 
ATOM   847  C  CD1 . LEU A 1 233 ? 107.001 77.979  116.875 1.00 163.48 ? 1010 LEU A CD1 1 
ATOM   848  C  CD2 . LEU A 1 233 ? 105.410 79.305  118.247 1.00 160.95 ? 1010 LEU A CD2 1 
ATOM   849  N  N   . VAL A 1 234 ? 108.016 80.646  120.898 1.00 146.23 ? 1011 VAL A N   1 
ATOM   850  C  CA  . VAL A 1 234 ? 107.646 82.005  121.268 1.00 145.86 ? 1011 VAL A CA  1 
ATOM   851  C  C   . VAL A 1 234 ? 107.859 82.918  120.068 1.00 145.21 ? 1011 VAL A C   1 
ATOM   852  O  O   . VAL A 1 234 ? 108.557 82.578  119.109 1.00 147.77 ? 1011 VAL A O   1 
ATOM   853  C  CB  . VAL A 1 234 ? 108.438 82.520  122.488 1.00 144.80 ? 1011 VAL A CB  1 
ATOM   854  C  CG1 . VAL A 1 234 ? 108.516 81.453  123.570 1.00 146.67 ? 1011 VAL A CG1 1 
ATOM   855  C  CG2 . VAL A 1 234 ? 109.831 82.964  122.070 1.00 142.63 ? 1011 VAL A CG2 1 
ATOM   856  N  N   . LEU A 1 235 ? 107.239 84.094  120.132 1.00 138.16 ? 1012 LEU A N   1 
ATOM   857  C  CA  . LEU A 1 235 ? 107.339 85.092  119.079 1.00 138.21 ? 1012 LEU A CA  1 
ATOM   858  C  C   . LEU A 1 235 ? 107.595 86.461  119.691 1.00 137.87 ? 1012 LEU A C   1 
ATOM   859  O  O   . LEU A 1 235 ? 107.102 86.776  120.778 1.00 140.75 ? 1012 LEU A O   1 
ATOM   860  C  CB  . LEU A 1 235 ? 106.067 85.142  118.221 1.00 137.97 ? 1012 LEU A CB  1 
ATOM   861  C  CG  . LEU A 1 235 ? 105.784 83.948  117.308 1.00 139.50 ? 1012 LEU A CG  1 
ATOM   862  C  CD1 . LEU A 1 235 ? 104.940 82.912  118.028 1.00 141.26 ? 1012 LEU A CD1 1 
ATOM   863  C  CD2 . LEU A 1 235 ? 105.098 84.405  116.031 1.00 139.49 ? 1012 LEU A CD2 1 
ATOM   864  N  N   . LEU A 1 236 ? 108.372 87.274  118.979 1.00 138.78 ? 1013 LEU A N   1 
ATOM   865  C  CA  . LEU A 1 236 ? 108.673 88.644  119.380 1.00 137.43 ? 1013 LEU A CA  1 
ATOM   866  C  C   . LEU A 1 236 ? 108.238 89.570  118.253 1.00 138.59 ? 1013 LEU A C   1 
ATOM   867  O  O   . LEU A 1 236 ? 108.908 89.653  117.218 1.00 143.55 ? 1013 LEU A O   1 
ATOM   868  C  CB  . LEU A 1 236 ? 110.159 88.816  119.691 1.00 140.00 ? 1013 LEU A CB  1 
ATOM   869  C  CG  . LEU A 1 236 ? 110.844 87.682  120.457 1.00 142.38 ? 1013 LEU A CG  1 
ATOM   870  C  CD1 . LEU A 1 236 ? 112.334 87.951  120.593 1.00 142.20 ? 1013 LEU A CD1 1 
ATOM   871  C  CD2 . LEU A 1 236 ? 110.207 87.491  121.822 1.00 139.38 ? 1013 LEU A CD2 1 
ATOM   872  N  N   . TRP A 1 237 ? 107.122 90.264  118.453 1.00 140.32 ? 1014 TRP A N   1 
ATOM   873  C  CA  . TRP A 1 237 ? 106.539 91.137  117.444 1.00 140.89 ? 1014 TRP A CA  1 
ATOM   874  C  C   . TRP A 1 237 ? 106.660 92.586  117.893 1.00 143.31 ? 1014 TRP A C   1 
ATOM   875  O  O   . TRP A 1 237 ? 106.257 92.929  119.009 1.00 147.95 ? 1014 TRP A O   1 
ATOM   876  C  CB  . TRP A 1 237 ? 105.072 90.779  117.199 1.00 140.20 ? 1014 TRP A CB  1 
ATOM   877  C  CG  . TRP A 1 237 ? 104.494 91.395  115.963 1.00 141.71 ? 1014 TRP A CG  1 
ATOM   878  C  CD1 . TRP A 1 237 ? 105.075 91.460  114.732 1.00 144.08 ? 1014 TRP A CD1 1 
ATOM   879  C  CD2 . TRP A 1 237 ? 103.217 92.031  115.838 1.00 142.81 ? 1014 TRP A CD2 1 
ATOM   880  N  NE1 . TRP A 1 237 ? 104.241 92.098  113.847 1.00 144.33 ? 1014 TRP A NE1 1 
ATOM   881  C  CE2 . TRP A 1 237 ? 103.093 92.458  114.501 1.00 143.15 ? 1014 TRP A CE2 1 
ATOM   882  C  CE3 . TRP A 1 237 ? 102.167 92.281  116.726 1.00 143.24 ? 1014 TRP A CE3 1 
ATOM   883  C  CZ2 . TRP A 1 237 ? 101.962 93.122  114.032 1.00 143.02 ? 1014 TRP A CZ2 1 
ATOM   884  C  CZ3 . TRP A 1 237 ? 101.045 92.940  116.258 1.00 144.65 ? 1014 TRP A CZ3 1 
ATOM   885  C  CH2 . TRP A 1 237 ? 100.951 93.352  114.924 1.00 145.03 ? 1014 TRP A CH2 1 
ATOM   886  N  N   . ASP A 1 238 ? 107.212 93.430  117.024 1.00 158.06 ? 1015 ASP A N   1 
ATOM   887  C  CA  . ASP A 1 238 ? 107.343 94.854  117.301 1.00 158.76 ? 1015 ASP A CA  1 
ATOM   888  C  C   . ASP A 1 238 ? 106.101 95.644  116.916 1.00 158.40 ? 1015 ASP A C   1 
ATOM   889  O  O   . ASP A 1 238 ? 106.101 96.873  117.049 1.00 158.49 ? 1015 ASP A O   1 
ATOM   890  C  CB  . ASP A 1 238 ? 108.562 95.429  116.572 1.00 161.42 ? 1015 ASP A CB  1 
ATOM   891  C  CG  . ASP A 1 238 ? 108.485 95.244  115.068 1.00 164.64 ? 1015 ASP A CG  1 
ATOM   892  O  OD1 . ASP A 1 238 ? 107.519 94.618  114.583 1.00 164.92 ? 1015 ASP A OD1 1 
ATOM   893  O  OD2 . ASP A 1 238 ? 109.398 95.728  114.366 1.00 167.03 ? 1015 ASP A OD2 1 
ATOM   894  N  N   . LYS A 1 239 ? 105.062 94.971  116.423 1.00 142.61 ? 1016 LYS A N   1 
ATOM   895  C  CA  . LYS A 1 239 ? 103.780 95.532  116.007 1.00 143.37 ? 1016 LYS A CA  1 
ATOM   896  C  C   . LYS A 1 239 ? 103.879 96.394  114.755 1.00 141.93 ? 1016 LYS A C   1 
ATOM   897  O  O   . LYS A 1 239 ? 102.857 96.942  114.324 1.00 141.87 ? 1016 LYS A O   1 
ATOM   898  C  CB  . LYS A 1 239 ? 103.109 96.354  117.118 1.00 141.81 ? 1016 LYS A CB  1 
ATOM   899  C  CG  . LYS A 1 239 ? 102.937 95.606  118.429 1.00 142.38 ? 1016 LYS A CG  1 
ATOM   900  C  CD  . LYS A 1 239 ? 102.391 96.518  119.515 1.00 140.55 ? 1016 LYS A CD  1 
ATOM   901  C  CE  . LYS A 1 239 ? 103.513 97.173  120.302 1.00 140.99 ? 1016 LYS A CE  1 
ATOM   902  N  NZ  . LYS A 1 239 ? 103.017 97.795  121.561 1.00 143.63 ? 1016 LYS A NZ  1 
ATOM   903  N  N   . LYS A 1 240 ? 105.061 96.541  114.154 1.00 152.40 ? 1017 LYS A N   1 
ATOM   904  C  CA  . LYS A 1 240 ? 105.194 97.354  112.950 1.00 153.70 ? 1017 LYS A CA  1 
ATOM   905  C  C   . LYS A 1 240 ? 105.599 96.537  111.731 1.00 154.50 ? 1017 LYS A C   1 
ATOM   906  O  O   . LYS A 1 240 ? 104.821 96.448  110.775 1.00 155.73 ? 1017 LYS A O   1 
ATOM   907  C  CB  . LYS A 1 240 ? 106.203 98.484  113.194 1.00 152.83 ? 1017 LYS A CB  1 
ATOM   908  C  CG  . LYS A 1 240 ? 106.063 99.166  114.544 1.00 154.63 ? 1017 LYS A CG  1 
ATOM   909  C  CD  . LYS A 1 240 ? 105.395 100.523 114.407 1.00 154.24 ? 1017 LYS A CD  1 
ATOM   910  C  CE  . LYS A 1 240 ? 105.831 101.466 115.517 1.00 155.38 ? 1017 LYS A CE  1 
ATOM   911  N  NZ  . LYS A 1 240 ? 107.314 101.572 115.600 1.00 154.12 ? 1017 LYS A NZ  1 
ATOM   912  N  N   . THR A 1 241 ? 106.788 95.933  111.725 1.00 149.10 ? 1018 THR A N   1 
ATOM   913  C  CA  . THR A 1 241 ? 107.233 95.215  110.536 1.00 146.75 ? 1018 THR A CA  1 
ATOM   914  C  C   . THR A 1 241 ? 107.862 93.862  110.852 1.00 147.89 ? 1018 THR A C   1 
ATOM   915  O  O   . THR A 1 241 ? 107.587 92.870  110.168 1.00 148.25 ? 1018 THR A O   1 
ATOM   916  C  CB  . THR A 1 241 ? 108.223 96.081  109.749 1.00 148.47 ? 1018 THR A CB  1 
ATOM   917  O  OG1 . THR A 1 241 ? 107.519 97.157  109.117 1.00 151.47 ? 1018 THR A OG1 1 
ATOM   918  C  CG2 . THR A 1 241 ? 108.938 95.261  108.684 1.00 148.57 ? 1018 THR A CG2 1 
ATOM   919  N  N   . SER A 1 242 ? 108.682 93.801  111.896 1.00 150.49 ? 1019 SER A N   1 
ATOM   920  C  CA  . SER A 1 242 ? 109.547 92.650  112.105 1.00 150.16 ? 1019 SER A CA  1 
ATOM   921  C  C   . SER A 1 242 ? 108.915 91.637  113.056 1.00 148.54 ? 1019 SER A C   1 
ATOM   922  O  O   . SER A 1 242 ? 107.946 91.919  113.763 1.00 151.14 ? 1019 SER A O   1 
ATOM   923  C  CB  . SER A 1 242 ? 110.910 93.094  112.636 1.00 148.83 ? 1019 SER A CB  1 
ATOM   924  O  OG  . SER A 1 242 ? 110.780 93.875  113.808 1.00 150.49 ? 1019 SER A OG  1 
ATOM   925  N  N   . ILE A 1 243 ? 109.489 90.437  113.061 1.00 128.52 ? 1020 ILE A N   1 
ATOM   926  C  CA  . ILE A 1 243 ? 109.031 89.343  113.912 1.00 127.79 ? 1020 ILE A CA  1 
ATOM   927  C  C   . ILE A 1 243 ? 110.208 88.409  114.160 1.00 128.58 ? 1020 ILE A C   1 
ATOM   928  O  O   . ILE A 1 243 ? 110.937 88.054  113.229 1.00 132.64 ? 1020 ILE A O   1 
ATOM   929  C  CB  . ILE A 1 243 ? 107.844 88.586  113.281 1.00 125.47 ? 1020 ILE A CB  1 
ATOM   930  C  CG1 . ILE A 1 243 ? 107.527 87.315  114.071 1.00 131.02 ? 1020 ILE A CG1 1 
ATOM   931  C  CG2 . ILE A 1 243 ? 108.122 88.268  111.818 1.00 124.32 ? 1020 ILE A CG2 1 
ATOM   932  C  CD1 . ILE A 1 243 ? 107.025 87.578  115.474 1.00 134.76 ? 1020 ILE A CD1 1 
ATOM   933  N  N   . PHE A 1 244 ? 110.401 88.022  115.418 1.00 129.59 ? 1021 PHE A N   1 
ATOM   934  C  CA  . PHE A 1 244 ? 111.479 87.127  115.812 1.00 126.26 ? 1021 PHE A CA  1 
ATOM   935  C  C   . PHE A 1 244 ? 110.899 85.816  116.322 1.00 130.22 ? 1021 PHE A C   1 
ATOM   936  O  O   . PHE A 1 244 ? 109.936 85.811  117.096 1.00 137.33 ? 1021 PHE A O   1 
ATOM   937  C  CB  . PHE A 1 244 ? 112.359 87.766  116.889 1.00 127.13 ? 1021 PHE A CB  1 
ATOM   938  C  CG  . PHE A 1 244 ? 113.122 88.969  116.414 1.00 130.90 ? 1021 PHE A CG  1 
ATOM   939  C  CD1 . PHE A 1 244 ? 112.542 90.226  116.431 1.00 132.94 ? 1021 PHE A CD1 1 
ATOM   940  C  CD2 . PHE A 1 244 ? 114.420 88.842  115.950 1.00 133.08 ? 1021 PHE A CD2 1 
ATOM   941  C  CE1 . PHE A 1 244 ? 113.242 91.334  115.995 1.00 131.24 ? 1021 PHE A CE1 1 
ATOM   942  C  CE2 . PHE A 1 244 ? 115.125 89.947  115.512 1.00 132.59 ? 1021 PHE A CE2 1 
ATOM   943  C  CZ  . PHE A 1 244 ? 114.535 91.194  115.535 1.00 130.80 ? 1021 PHE A CZ  1 
ATOM   944  N  N   . ILE A 1 245 ? 111.489 84.706  115.888 1.00 137.52 ? 1022 ILE A N   1 
ATOM   945  C  CA  . ILE A 1 245 ? 111.019 83.369  116.230 1.00 137.62 ? 1022 ILE A CA  1 
ATOM   946  C  C   . ILE A 1 245 ? 112.118 82.649  116.996 1.00 140.79 ? 1022 ILE A C   1 
ATOM   947  O  O   . ILE A 1 245 ? 113.277 82.635  116.565 1.00 145.99 ? 1022 ILE A O   1 
ATOM   948  C  CB  . ILE A 1 245 ? 110.618 82.569  114.977 1.00 136.93 ? 1022 ILE A CB  1 
ATOM   949  C  CG1 . ILE A 1 245 ? 109.783 83.436  114.032 1.00 138.30 ? 1022 ILE A CG1 1 
ATOM   950  C  CG2 . ILE A 1 245 ? 109.866 81.306  115.369 1.00 136.55 ? 1022 ILE A CG2 1 
ATOM   951  C  CD1 . ILE A 1 245 ? 108.326 83.539  114.420 1.00 138.21 ? 1022 ILE A CD1 1 
ATOM   952  N  N   . ASN A 1 246 ? 111.754 82.053  118.129 1.00 161.75 ? 1023 ASN A N   1 
ATOM   953  C  CA  . ASN A 1 246 ? 112.664 81.255  118.938 1.00 162.79 ? 1023 ASN A CA  1 
ATOM   954  C  C   . ASN A 1 246 ? 112.085 79.857  119.092 1.00 164.09 ? 1023 ASN A C   1 
ATOM   955  O  O   . ASN A 1 246 ? 110.910 79.704  119.444 1.00 167.16 ? 1023 ASN A O   1 
ATOM   956  C  CB  . ASN A 1 246 ? 112.893 81.893  120.310 1.00 163.95 ? 1023 ASN A CB  1 
ATOM   957  C  CG  . ASN A 1 246 ? 114.231 82.597  120.409 1.00 165.18 ? 1023 ASN A CG  1 
ATOM   958  O  OD1 . ASN A 1 246 ? 114.906 82.814  119.403 1.00 166.22 ? 1023 ASN A OD1 1 
ATOM   959  N  ND2 . ASN A 1 246 ? 114.621 82.958  121.625 1.00 165.97 ? 1023 ASN A ND2 1 
ATOM   960  N  N   . LEU A 1 247 ? 112.906 78.843  118.833 1.00 175.26 ? 1024 LEU A N   1 
ATOM   961  C  CA  . LEU A 1 247 ? 112.471 77.455  118.858 1.00 176.76 ? 1024 LEU A CA  1 
ATOM   962  C  C   . LEU A 1 247 ? 113.315 76.661  119.845 1.00 179.16 ? 1024 LEU A C   1 
ATOM   963  O  O   . LEU A 1 247 ? 114.515 76.910  119.993 1.00 179.52 ? 1024 LEU A O   1 
ATOM   964  C  CB  . LEU A 1 247 ? 112.565 76.824  117.464 1.00 177.07 ? 1024 LEU A CB  1 
ATOM   965  C  CG  . LEU A 1 247 ? 111.859 75.481  117.275 1.00 177.65 ? 1024 LEU A CG  1 
ATOM   966  C  CD1 . LEU A 1 247 ? 110.405 75.578  117.708 1.00 177.17 ? 1024 LEU A CD1 1 
ATOM   967  C  CD2 . LEU A 1 247 ? 111.962 75.019  115.831 1.00 179.51 ? 1024 LEU A CD2 1 
ATOM   968  N  N   . SER A 1 248 ? 112.678 75.707  120.518 1.00 194.47 ? 1025 SER A N   1 
ATOM   969  C  CA  . SER A 1 248 ? 113.382 74.863  121.467 1.00 193.63 ? 1025 SER A CA  1 
ATOM   970  C  C   . SER A 1 248 ? 114.283 73.871  120.731 1.00 193.77 ? 1025 SER A C   1 
ATOM   971  O  O   . SER A 1 248 ? 114.000 73.489  119.593 1.00 194.00 ? 1025 SER A O   1 
ATOM   972  C  CB  . SER A 1 248 ? 112.390 74.110  122.349 1.00 192.97 ? 1025 SER A CB  1 
ATOM   973  O  OG  . SER A 1 248 ? 111.390 74.980  122.849 1.00 194.08 ? 1025 SER A OG  1 
ATOM   974  N  N   . PRO A 1 249 ? 115.381 73.442  121.361 1.00 197.24 ? 1026 PRO A N   1 
ATOM   975  C  CA  . PRO A 1 249 ? 116.266 72.464  120.706 1.00 198.08 ? 1026 PRO A CA  1 
ATOM   976  C  C   . PRO A 1 249 ? 115.618 71.109  120.476 1.00 197.97 ? 1026 PRO A C   1 
ATOM   977  O  O   . PRO A 1 249 ? 116.142 70.323  119.677 1.00 197.35 ? 1026 PRO A O   1 
ATOM   978  C  CB  . PRO A 1 249 ? 117.452 72.352  121.675 1.00 197.74 ? 1026 PRO A CB  1 
ATOM   979  C  CG  . PRO A 1 249 ? 117.379 73.582  122.527 1.00 197.05 ? 1026 PRO A CG  1 
ATOM   980  C  CD  . PRO A 1 249 ? 115.925 73.903  122.649 1.00 196.45 ? 1026 PRO A CD  1 
ATOM   981  N  N   . GLU A 1 250 ? 114.503 70.809  121.148 1.00 211.00 ? 1027 GLU A N   1 
ATOM   982  C  CA  . GLU A 1 250 ? 113.856 69.512  120.973 1.00 211.84 ? 1027 GLU A CA  1 
ATOM   983  C  C   . GLU A 1 250 ? 113.313 69.334  119.560 1.00 211.77 ? 1027 GLU A C   1 
ATOM   984  O  O   . GLU A 1 250 ? 113.169 68.199  119.092 1.00 212.91 ? 1027 GLU A O   1 
ATOM   985  C  CB  . GLU A 1 250 ? 112.734 69.346  121.997 1.00 212.54 ? 1027 GLU A CB  1 
ATOM   986  C  CG  . GLU A 1 250 ? 112.249 67.915  122.164 1.00 213.26 ? 1027 GLU A CG  1 
ATOM   987  C  CD  . GLU A 1 250 ? 110.750 67.783  121.983 1.00 213.03 ? 1027 GLU A CD  1 
ATOM   988  O  OE1 . GLU A 1 250 ? 110.156 68.640  121.296 1.00 213.03 ? 1027 GLU A OE1 1 
ATOM   989  O  OE2 . GLU A 1 250 ? 110.166 66.824  122.529 1.00 212.17 ? 1027 GLU A OE2 1 
ATOM   990  N  N   . PHE A 1 251 ? 113.013 70.434  118.865 1.00 193.49 ? 1028 PHE A N   1 
ATOM   991  C  CA  . PHE A 1 251 ? 112.481 70.385  117.509 1.00 192.52 ? 1028 PHE A CA  1 
ATOM   992  C  C   . PHE A 1 251 ? 113.575 70.368  116.448 1.00 192.26 ? 1028 PHE A C   1 
ATOM   993  O  O   . PHE A 1 251 ? 113.337 70.791  115.309 1.00 192.83 ? 1028 PHE A O   1 
ATOM   994  C  CB  . PHE A 1 251 ? 111.534 71.563  117.276 1.00 192.29 ? 1028 PHE A CB  1 
ATOM   995  C  CG  . PHE A 1 251 ? 110.167 71.366  117.862 1.00 192.41 ? 1028 PHE A CG  1 
ATOM   996  C  CD1 . PHE A 1 251 ? 109.364 70.319  117.442 1.00 193.21 ? 1028 PHE A CD1 1 
ATOM   997  C  CD2 . PHE A 1 251 ? 109.686 72.225  118.835 1.00 192.28 ? 1028 PHE A CD2 1 
ATOM   998  C  CE1 . PHE A 1 251 ? 108.105 70.134  117.980 1.00 193.86 ? 1028 PHE A CE1 1 
ATOM   999  C  CE2 . PHE A 1 251 ? 108.428 72.045  119.377 1.00 192.85 ? 1028 PHE A CE2 1 
ATOM   1000 C  CZ  . PHE A 1 251 ? 107.637 70.998  118.949 1.00 193.65 ? 1028 PHE A CZ  1 
ATOM   1001 N  N   . LYS A 1 252 ? 114.769 69.891  116.792 1.00 186.05 ? 1029 LYS A N   1 
ATOM   1002 C  CA  . LYS A 1 252 ? 115.871 69.867  115.840 1.00 186.42 ? 1029 LYS A CA  1 
ATOM   1003 C  C   . LYS A 1 252 ? 115.625 68.814  114.767 1.00 186.03 ? 1029 LYS A C   1 
ATOM   1004 O  O   . LYS A 1 252 ? 115.309 67.660  115.072 1.00 185.05 ? 1029 LYS A O   1 
ATOM   1005 C  CB  . LYS A 1 252 ? 117.186 69.589  116.566 1.00 186.25 ? 1029 LYS A CB  1 
ATOM   1006 C  CG  . LYS A 1 252 ? 118.423 69.745  115.700 1.00 186.16 ? 1029 LYS A CG  1 
ATOM   1007 C  CD  . LYS A 1 252 ? 119.664 69.978  116.547 1.00 186.86 ? 1029 LYS A CD  1 
ATOM   1008 C  CE  . LYS A 1 252 ? 119.514 71.213  117.420 1.00 186.39 ? 1029 LYS A CE  1 
ATOM   1009 N  NZ  . LYS A 1 252 ? 120.728 71.460  118.245 1.00 186.11 ? 1029 LYS A NZ  1 
ATOM   1010 N  N   . GLY A 1 253 ? 115.772 69.215  113.506 1.00 176.39 ? 1030 GLY A N   1 
ATOM   1011 C  CA  . GLY A 1 253 ? 115.617 68.288  112.402 1.00 175.46 ? 1030 GLY A CA  1 
ATOM   1012 C  C   . GLY A 1 253 ? 114.202 67.833  112.136 1.00 175.37 ? 1030 GLY A C   1 
ATOM   1013 O  O   . GLY A 1 253 ? 114.007 66.791  111.505 1.00 174.99 ? 1030 GLY A O   1 
ATOM   1014 N  N   . ARG A 1 254 ? 113.198 68.586  112.598 1.00 185.38 ? 1031 ARG A N   1 
ATOM   1015 C  CA  . ARG A 1 254 ? 111.809 68.200  112.381 1.00 185.71 ? 1031 ARG A CA  1 
ATOM   1016 C  C   . ARG A 1 254 ? 110.930 69.385  111.992 1.00 186.66 ? 1031 ARG A C   1 
ATOM   1017 O  O   . ARG A 1 254 ? 109.700 69.285  112.077 1.00 186.82 ? 1031 ARG A O   1 
ATOM   1018 C  CB  . ARG A 1 254 ? 111.231 67.523  113.629 1.00 185.52 ? 1031 ARG A CB  1 
ATOM   1019 C  CG  . ARG A 1 254 ? 111.801 66.143  113.914 1.00 185.51 ? 1031 ARG A CG  1 
ATOM   1020 C  CD  . ARG A 1 254 ? 110.944 65.388  114.917 1.00 185.75 ? 1031 ARG A CD  1 
ATOM   1021 N  NE  . ARG A 1 254 ? 110.583 66.216  116.062 1.00 186.57 ? 1031 ARG A NE  1 
ATOM   1022 C  CZ  . ARG A 1 254 ? 111.404 66.516  117.059 1.00 187.23 ? 1031 ARG A CZ  1 
ATOM   1023 N  NH1 . ARG A 1 254 ? 112.648 66.066  117.092 1.00 186.94 ? 1031 ARG A NH1 1 
ATOM   1024 N  NH2 . ARG A 1 254 ? 110.966 67.287  118.050 1.00 188.47 ? 1031 ARG A NH2 1 
ATOM   1025 N  N   . VAL A 1 255 ? 111.522 70.500  111.571 1.00 178.62 ? 1032 VAL A N   1 
ATOM   1026 C  CA  . VAL A 1 255 ? 110.782 71.702  111.211 1.00 177.43 ? 1032 VAL A CA  1 
ATOM   1027 C  C   . VAL A 1 255 ? 111.251 72.167  109.841 1.00 176.95 ? 1032 VAL A C   1 
ATOM   1028 O  O   . VAL A 1 255 ? 112.457 72.300  109.606 1.00 176.86 ? 1032 VAL A O   1 
ATOM   1029 C  CB  . VAL A 1 255 ? 110.968 72.820  112.256 1.00 177.17 ? 1032 VAL A CB  1 
ATOM   1030 C  CG1 . VAL A 1 255 ? 110.566 74.167  111.677 1.00 177.26 ? 1032 VAL A CG1 1 
ATOM   1031 C  CG2 . VAL A 1 255 ? 110.164 72.511  113.509 1.00 177.62 ? 1032 VAL A CG2 1 
ATOM   1032 N  N   . CYS A 1 256 ? 110.302 72.411  108.939 1.00 183.22 ? 1033 CYS A N   1 
ATOM   1033 C  CA  . CYS A 1 256 ? 110.599 72.912  107.606 1.00 182.30 ? 1033 CYS A CA  1 
ATOM   1034 C  C   . CYS A 1 256 ? 109.773 74.160  107.336 1.00 181.10 ? 1033 CYS A C   1 
ATOM   1035 O  O   . CYS A 1 256 ? 108.671 74.322  107.867 1.00 181.78 ? 1033 CYS A O   1 
ATOM   1036 C  CB  . CYS A 1 256 ? 110.317 71.857  106.528 1.00 184.24 ? 1033 CYS A CB  1 
ATOM   1037 S  SG  . CYS A 1 256 ? 108.590 71.338  106.425 1.00 191.68 ? 1033 CYS A SG  1 
ATOM   1038 N  N   . GLY A 1 257 ? 110.317 75.040  106.506 1.00 156.37 ? 1034 GLY A N   1 
ATOM   1039 C  CA  . GLY A 1 257 ? 109.634 76.274  106.169 1.00 158.53 ? 1034 GLY A CA  1 
ATOM   1040 C  C   . GLY A 1 257 ? 110.617 77.286  105.607 1.00 158.01 ? 1034 GLY A C   1 
ATOM   1041 O  O   . GLY A 1 257 ? 111.712 76.933  105.174 1.00 158.32 ? 1034 GLY A O   1 
ATOM   1042 N  N   . LEU A 1 258 ? 110.192 78.552  105.627 1.00 143.02 ? 1035 LEU A N   1 
ATOM   1043 C  CA  . LEU A 1 258 ? 111.041 79.628  105.132 1.00 140.06 ? 1035 LEU A CA  1 
ATOM   1044 C  C   . LEU A 1 258 ? 112.265 79.852  106.009 1.00 140.89 ? 1035 LEU A C   1 
ATOM   1045 O  O   . LEU A 1 258 ? 113.254 80.420  105.536 1.00 144.35 ? 1035 LEU A O   1 
ATOM   1046 C  CB  . LEU A 1 258 ? 110.238 80.925  105.020 1.00 141.01 ? 1035 LEU A CB  1 
ATOM   1047 C  CG  . LEU A 1 258 ? 109.849 81.354  103.604 1.00 140.51 ? 1035 LEU A CG  1 
ATOM   1048 C  CD1 . LEU A 1 258 ? 109.296 82.770  103.604 1.00 141.56 ? 1035 LEU A CD1 1 
ATOM   1049 C  CD2 . LEU A 1 258 ? 111.037 81.241  102.663 1.00 142.63 ? 1035 LEU A CD2 1 
ATOM   1050 N  N   . CYS A 1 259 ? 112.223 79.421  107.268 1.00 149.33 ? 1036 CYS A N   1 
ATOM   1051 C  CA  . CYS A 1 259 ? 113.365 79.547  108.163 1.00 150.59 ? 1036 CYS A CA  1 
ATOM   1052 C  C   . CYS A 1 259 ? 114.378 78.424  107.991 1.00 150.88 ? 1036 CYS A C   1 
ATOM   1053 O  O   . CYS A 1 259 ? 115.414 78.439  108.663 1.00 150.72 ? 1036 CYS A O   1 
ATOM   1054 C  CB  . CYS A 1 259 ? 112.892 79.594  109.619 1.00 151.21 ? 1036 CYS A CB  1 
ATOM   1055 S  SG  . CYS A 1 259 ? 112.062 81.129  110.091 1.00 155.00 ? 1036 CYS A SG  1 
ATOM   1056 N  N   . GLY A 1 260 ? 114.107 77.458  107.123 1.00 173.92 ? 1037 GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 260 ? 115.027 76.371  106.875 1.00 175.42 ? 1037 GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 260 ? 114.914 75.261  107.905 1.00 176.46 ? 1037 GLY A C   1 
ATOM   1059 O  O   . GLY A 1 260 ? 114.353 75.422  108.988 1.00 177.21 ? 1037 GLY A O   1 
ATOM   1060 N  N   . ASN A 1 261 ? 115.466 74.105  107.547 1.00 182.07 ? 1038 ASN A N   1 
ATOM   1061 C  CA  . ASN A 1 261 ? 115.448 72.960  108.448 1.00 181.69 ? 1038 ASN A CA  1 
ATOM   1062 C  C   . ASN A 1 261 ? 116.448 73.166  109.578 1.00 181.55 ? 1038 ASN A C   1 
ATOM   1063 O  O   . ASN A 1 261 ? 117.599 73.545  109.344 1.00 180.78 ? 1038 ASN A O   1 
ATOM   1064 C  CB  . ASN A 1 261 ? 115.758 71.674  107.683 1.00 180.83 ? 1038 ASN A CB  1 
ATOM   1065 C  CG  . ASN A 1 261 ? 117.113 71.710  107.003 1.00 181.65 ? 1038 ASN A CG  1 
ATOM   1066 O  OD1 . ASN A 1 261 ? 117.561 72.758  106.540 1.00 181.71 ? 1038 ASN A OD1 1 
ATOM   1067 N  ND2 . ASN A 1 261 ? 117.773 70.560  106.939 1.00 182.00 ? 1038 ASN A ND2 1 
ATOM   1068 N  N   . PHE A 1 262 ? 116.003 72.919  110.810 1.00 174.54 ? 1039 PHE A N   1 
ATOM   1069 C  CA  . PHE A 1 262 ? 116.843 73.098  111.993 1.00 172.86 ? 1039 PHE A CA  1 
ATOM   1070 C  C   . PHE A 1 262 ? 117.766 71.889  112.117 1.00 173.59 ? 1039 PHE A C   1 
ATOM   1071 O  O   . PHE A 1 262 ? 117.499 70.924  112.837 1.00 173.52 ? 1039 PHE A O   1 
ATOM   1072 C  CB  . PHE A 1 262 ? 115.983 73.285  113.237 1.00 172.66 ? 1039 PHE A CB  1 
ATOM   1073 C  CG  . PHE A 1 262 ? 116.748 73.759  114.438 1.00 171.59 ? 1039 PHE A CG  1 
ATOM   1074 C  CD1 . PHE A 1 262 ? 117.935 74.457  114.291 1.00 172.69 ? 1039 PHE A CD1 1 
ATOM   1075 C  CD2 . PHE A 1 262 ? 116.279 73.508  115.716 1.00 171.41 ? 1039 PHE A CD2 1 
ATOM   1076 C  CE1 . PHE A 1 262 ? 118.640 74.894  115.396 1.00 174.53 ? 1039 PHE A CE1 1 
ATOM   1077 C  CE2 . PHE A 1 262 ? 116.979 73.943  116.825 1.00 172.53 ? 1039 PHE A CE2 1 
ATOM   1078 C  CZ  . PHE A 1 262 ? 118.161 74.637  116.664 1.00 173.95 ? 1039 PHE A CZ  1 
ATOM   1079 N  N   . ASP A 1 263 ? 118.884 71.950  111.390 1.00 186.46 ? 1040 ASP A N   1 
ATOM   1080 C  CA  . ASP A 1 263 ? 119.863 70.871  111.386 1.00 187.14 ? 1040 ASP A CA  1 
ATOM   1081 C  C   . ASP A 1 263 ? 121.287 71.368  111.604 1.00 188.17 ? 1040 ASP A C   1 
ATOM   1082 O  O   . ASP A 1 263 ? 122.235 70.604  111.384 1.00 187.10 ? 1040 ASP A O   1 
ATOM   1083 C  CB  . ASP A 1 263 ? 119.784 70.079  110.075 1.00 187.40 ? 1040 ASP A CB  1 
ATOM   1084 C  CG  . ASP A 1 263 ? 120.301 70.866  108.887 1.00 187.31 ? 1040 ASP A CG  1 
ATOM   1085 O  OD1 . ASP A 1 263 ? 120.105 72.099  108.856 1.00 186.09 ? 1040 ASP A OD1 1 
ATOM   1086 O  OD2 . ASP A 1 263 ? 120.903 70.249  107.984 1.00 187.89 ? 1040 ASP A OD2 1 
ATOM   1087 N  N   . ASP A 1 264 ? 121.461 72.624  112.019 1.00 201.64 ? 1041 ASP A N   1 
ATOM   1088 C  CA  . ASP A 1 264 ? 122.767 73.221  112.296 1.00 201.54 ? 1041 ASP A CA  1 
ATOM   1089 C  C   . ASP A 1 264 ? 123.680 73.231  111.073 1.00 201.37 ? 1041 ASP A C   1 
ATOM   1090 O  O   . ASP A 1 264 ? 124.906 73.288  111.211 1.00 201.70 ? 1041 ASP A O   1 
ATOM   1091 C  CB  . ASP A 1 264 ? 123.464 72.518  113.468 1.00 200.92 ? 1041 ASP A CB  1 
ATOM   1092 C  CG  . ASP A 1 264 ? 122.725 72.699  114.779 1.00 200.73 ? 1041 ASP A CG  1 
ATOM   1093 O  OD1 . ASP A 1 264 ? 122.078 73.752  114.957 1.00 200.94 ? 1041 ASP A OD1 1 
ATOM   1094 O  OD2 . ASP A 1 264 ? 122.792 71.789  115.631 1.00 200.64 ? 1041 ASP A OD2 1 
ATOM   1095 N  N   . ILE A 1 265 ? 123.107 73.176  109.874 1.00 193.64 ? 1042 ILE A N   1 
ATOM   1096 C  CA  . ILE A 1 265 ? 123.863 73.225  108.627 1.00 192.99 ? 1042 ILE A CA  1 
ATOM   1097 C  C   . ILE A 1 265 ? 123.331 74.391  107.807 1.00 192.67 ? 1042 ILE A C   1 
ATOM   1098 O  O   . ILE A 1 265 ? 122.132 74.448  107.505 1.00 193.40 ? 1042 ILE A O   1 
ATOM   1099 C  CB  . ILE A 1 265 ? 123.764 71.908  107.842 1.00 193.06 ? 1042 ILE A CB  1 
ATOM   1100 C  CG1 . ILE A 1 265 ? 124.154 70.724  108.729 1.00 192.47 ? 1042 ILE A CG1 1 
ATOM   1101 C  CG2 . ILE A 1 265 ? 124.644 71.959  106.606 1.00 192.02 ? 1042 ILE A CG2 1 
ATOM   1102 C  CD1 . ILE A 1 265 ? 125.598 70.746  109.176 1.00 192.59 ? 1042 ILE A CD1 1 
ATOM   1103 N  N   . ALA A 1 266 ? 124.218 75.312  107.441 1.00 185.67 ? 1043 ALA A N   1 
ATOM   1104 C  CA  . ALA A 1 266 ? 123.830 76.533  106.749 1.00 185.98 ? 1043 ALA A CA  1 
ATOM   1105 C  C   . ALA A 1 266 ? 123.867 76.405  105.232 1.00 186.59 ? 1043 ALA A C   1 
ATOM   1106 O  O   . ALA A 1 266 ? 123.619 77.397  104.538 1.00 187.23 ? 1043 ALA A O   1 
ATOM   1107 C  CB  . ALA A 1 266 ? 124.730 77.693  107.186 1.00 184.71 ? 1043 ALA A CB  1 
ATOM   1108 N  N   . VAL A 1 267 ? 124.165 75.222  104.698 1.00 189.53 ? 1044 VAL A N   1 
ATOM   1109 C  CA  . VAL A 1 267 ? 124.242 75.026  103.253 1.00 190.54 ? 1044 VAL A CA  1 
ATOM   1110 C  C   . VAL A 1 267 ? 123.065 74.241  102.696 1.00 189.98 ? 1044 VAL A C   1 
ATOM   1111 O  O   . VAL A 1 267 ? 122.891 74.210  101.467 1.00 190.13 ? 1044 VAL A O   1 
ATOM   1112 C  CB  . VAL A 1 267 ? 125.566 74.346  102.843 1.00 190.54 ? 1044 VAL A CB  1 
ATOM   1113 C  CG1 . VAL A 1 267 ? 126.745 75.032  103.516 1.00 190.30 ? 1044 VAL A CG1 1 
ATOM   1114 C  CG2 . VAL A 1 267 ? 125.533 72.865  103.181 1.00 188.82 ? 1044 VAL A CG2 1 
ATOM   1115 N  N   . ASN A 1 268 ? 122.255 73.609  103.545 1.00 179.63 ? 1045 ASN A N   1 
ATOM   1116 C  CA  . ASN A 1 268 ? 121.098 72.840  103.103 1.00 179.23 ? 1045 ASN A CA  1 
ATOM   1117 C  C   . ASN A 1 268 ? 119.785 73.476  103.552 1.00 179.65 ? 1045 ASN A C   1 
ATOM   1118 O  O   . ASN A 1 268 ? 118.791 72.779  103.767 1.00 179.74 ? 1045 ASN A O   1 
ATOM   1119 C  CB  . ASN A 1 268 ? 121.191 71.398  103.602 1.00 178.86 ? 1045 ASN A CB  1 
ATOM   1120 C  CG  . ASN A 1 268 ? 121.377 71.308  105.105 1.00 179.46 ? 1045 ASN A CG  1 
ATOM   1121 O  OD1 . ASN A 1 268 ? 121.266 72.304  105.819 1.00 179.30 ? 1045 ASN A OD1 1 
ATOM   1122 N  ND2 . ASN A 1 268 ? 121.664 70.107  105.593 1.00 179.95 ? 1045 ASN A ND2 1 
ATOM   1123 N  N   . ASP A 1 269 ? 119.770 74.803  103.698 1.00 188.95 ? 1046 ASP A N   1 
ATOM   1124 C  CA  . ASP A 1 269 ? 118.589 75.534  104.140 1.00 189.99 ? 1046 ASP A CA  1 
ATOM   1125 C  C   . ASP A 1 269 ? 117.713 75.992  102.980 1.00 189.64 ? 1046 ASP A C   1 
ATOM   1126 O  O   . ASP A 1 269 ? 117.002 76.997  103.104 1.00 190.77 ? 1046 ASP A O   1 
ATOM   1127 C  CB  . ASP A 1 269 ? 119.004 76.731  104.996 1.00 189.72 ? 1046 ASP A CB  1 
ATOM   1128 C  CG  . ASP A 1 269 ? 118.891 76.453  106.481 1.00 189.55 ? 1046 ASP A CG  1 
ATOM   1129 O  OD1 . ASP A 1 269 ? 118.177 75.500  106.857 1.00 188.79 ? 1046 ASP A OD1 1 
ATOM   1130 O  OD2 . ASP A 1 269 ? 119.516 77.187  107.274 1.00 190.74 ? 1046 ASP A OD2 1 
ATOM   1131 N  N   . PHE A 1 270 ? 117.746 75.282  101.852 1.00 184.79 ? 1047 PHE A N   1 
ATOM   1132 C  CA  . PHE A 1 270 ? 116.970 75.681  100.685 1.00 184.50 ? 1047 PHE A CA  1 
ATOM   1133 C  C   . PHE A 1 270 ? 116.044 74.561  100.227 1.00 186.38 ? 1047 PHE A C   1 
ATOM   1134 O  O   . PHE A 1 270 ? 115.957 74.270  99.030  1.00 186.83 ? 1047 PHE A O   1 
ATOM   1135 C  CB  . PHE A 1 270 ? 117.901 76.099  99.545  1.00 184.00 ? 1047 PHE A CB  1 
ATOM   1136 C  CG  . PHE A 1 270 ? 118.425 77.500  99.675  1.00 185.51 ? 1047 PHE A CG  1 
ATOM   1137 C  CD1 . PHE A 1 270 ? 119.396 77.807  100.613 1.00 185.62 ? 1047 PHE A CD1 1 
ATOM   1138 C  CD2 . PHE A 1 270 ? 117.944 78.511  98.860  1.00 186.58 ? 1047 PHE A CD2 1 
ATOM   1139 C  CE1 . PHE A 1 270 ? 119.879 79.096  100.735 1.00 185.67 ? 1047 PHE A CE1 1 
ATOM   1140 C  CE2 . PHE A 1 270 ? 118.423 79.802  98.978  1.00 185.69 ? 1047 PHE A CE2 1 
ATOM   1141 C  CZ  . PHE A 1 270 ? 119.392 80.094  99.916  1.00 184.63 ? 1047 PHE A CZ  1 
ATOM   1142 N  N   . ALA A 1 271 ? 115.351 73.927  101.171 1.00 217.42 ? 1048 ALA A N   1 
ATOM   1143 C  CA  . ALA A 1 271 ? 114.394 72.875  100.848 1.00 218.80 ? 1048 ALA A CA  1 
ATOM   1144 C  C   . ALA A 1 271 ? 113.134 73.517  100.280 1.00 220.22 ? 1048 ALA A C   1 
ATOM   1145 O  O   . ALA A 1 271 ? 112.355 74.131  101.016 1.00 220.66 ? 1048 ALA A O   1 
ATOM   1146 C  CB  . ALA A 1 271 ? 114.079 72.039  102.084 1.00 218.73 ? 1048 ALA A CB  1 
ATOM   1147 N  N   . THR A 1 272 ? 112.929 73.372  98.971  1.00 239.10 ? 1049 THR A N   1 
ATOM   1148 C  CA  . THR A 1 272 ? 111.811 74.023  98.298  1.00 238.52 ? 1049 THR A CA  1 
ATOM   1149 C  C   . THR A 1 272 ? 110.534 73.197  98.402  1.00 238.71 ? 1049 THR A C   1 
ATOM   1150 O  O   . THR A 1 272 ? 109.910 72.883  97.383  1.00 239.01 ? 1049 THR A O   1 
ATOM   1151 C  CB  . THR A 1 272 ? 112.147 74.279  96.828  1.00 239.04 ? 1049 THR A CB  1 
ATOM   1152 O  OG1 . THR A 1 272 ? 111.803 73.127  96.048  1.00 239.68 ? 1049 THR A OG1 1 
ATOM   1153 C  CG2 . THR A 1 272 ? 113.630 74.572  96.663  1.00 238.99 ? 1049 THR A CG2 1 
ATOM   1154 N  N   . ARG A 1 273 ? 110.150 72.830  99.625  1.00 239.77 ? 1050 ARG A N   1 
ATOM   1155 C  CA  . ARG A 1 273 ? 108.906 72.140  99.959  1.00 239.90 ? 1050 ARG A CA  1 
ATOM   1156 C  C   . ARG A 1 273 ? 108.829 70.734  99.370  1.00 241.03 ? 1050 ARG A C   1 
ATOM   1157 O  O   . ARG A 1 273 ? 107.841 70.030  99.611  1.00 240.52 ? 1050 ARG A O   1 
ATOM   1158 C  CB  . ARG A 1 273 ? 107.669 72.942  99.522  1.00 239.82 ? 1050 ARG A CB  1 
ATOM   1159 C  CG  . ARG A 1 273 ? 106.399 72.646  100.308 1.00 239.71 ? 1050 ARG A CG  1 
ATOM   1160 C  CD  . ARG A 1 273 ? 105.218 73.452  99.784  1.00 239.80 ? 1050 ARG A CD  1 
ATOM   1161 N  NE  . ARG A 1 273 ? 105.404 73.876  98.401  1.00 240.51 ? 1050 ARG A NE  1 
ATOM   1162 C  CZ  . ARG A 1 273 ? 105.057 73.156  97.342  1.00 240.71 ? 1050 ARG A CZ  1 
ATOM   1163 N  NH1 . ARG A 1 273 ? 104.500 71.963  97.470  1.00 240.55 ? 1050 ARG A NH1 1 
ATOM   1164 N  NH2 . ARG A 1 273 ? 105.275 73.645  96.125  1.00 240.17 ? 1050 ARG A NH2 1 
ATOM   1165 N  N   . SER A 1 274 ? 109.840 70.291  98.620  1.00 265.21 ? 1051 SER A N   1 
ATOM   1166 C  CA  . SER A 1 274 ? 109.846 68.962  98.020  1.00 265.32 ? 1051 SER A CA  1 
ATOM   1167 C  C   . SER A 1 274 ? 111.084 68.164  98.413  1.00 265.97 ? 1051 SER A C   1 
ATOM   1168 O  O   . SER A 1 274 ? 111.462 67.226  97.702  1.00 266.04 ? 1051 SER A O   1 
ATOM   1169 C  CB  . SER A 1 274 ? 109.740 69.062  96.497  1.00 264.59 ? 1051 SER A CB  1 
ATOM   1170 O  OG  . SER A 1 274 ? 110.850 69.755  95.954  1.00 264.92 ? 1051 SER A OG  1 
ATOM   1171 N  N   . ARG A 1 275 ? 111.720 68.521  99.531  1.00 278.75 ? 1052 ARG A N   1 
ATOM   1172 C  CA  . ARG A 1 275 ? 112.929 67.849  100.012 1.00 278.79 ? 1052 ARG A CA  1 
ATOM   1173 C  C   . ARG A 1 275 ? 114.034 67.871  98.957  1.00 278.83 ? 1052 ARG A C   1 
ATOM   1174 O  O   . ARG A 1 275 ? 114.792 66.911  98.803  1.00 279.46 ? 1052 ARG A O   1 
ATOM   1175 C  CB  . ARG A 1 275 ? 112.629 66.415  100.458 1.00 278.77 ? 1052 ARG A CB  1 
ATOM   1176 C  CG  . ARG A 1 275 ? 112.095 66.303  101.879 1.00 278.32 ? 1052 ARG A CG  1 
ATOM   1177 C  CD  . ARG A 1 275 ? 110.597 66.555  101.933 1.00 277.94 ? 1052 ARG A CD  1 
ATOM   1178 N  NE  . ARG A 1 275 ? 110.119 66.708  103.302 1.00 278.51 ? 1052 ARG A NE  1 
ATOM   1179 C  CZ  . ARG A 1 275 ? 109.647 65.717  104.046 1.00 279.02 ? 1052 ARG A CZ  1 
ATOM   1180 N  NH1 . ARG A 1 275 ? 109.575 64.479  103.583 1.00 279.32 ? 1052 ARG A NH1 1 
ATOM   1181 N  NH2 . ARG A 1 275 ? 109.238 65.973  105.285 1.00 278.49 ? 1052 ARG A NH2 1 
ATOM   1182 N  N   . SER A 1 276 ? 114.124 68.978  98.224  1.00 256.53 ? 1053 SER A N   1 
ATOM   1183 C  CA  . SER A 1 276 ? 115.132 69.158  97.185  1.00 255.96 ? 1053 SER A CA  1 
ATOM   1184 C  C   . SER A 1 276 ? 115.791 70.514  97.379  1.00 255.01 ? 1053 SER A C   1 
ATOM   1185 O  O   . SER A 1 276 ? 115.116 71.547  97.331  1.00 254.90 ? 1053 SER A O   1 
ATOM   1186 C  CB  . SER A 1 276 ? 114.512 69.055  95.789  1.00 255.23 ? 1053 SER A CB  1 
ATOM   1187 O  OG  . SER A 1 276 ? 113.386 69.907  95.666  1.00 254.92 ? 1053 SER A OG  1 
ATOM   1188 N  N   . VAL A 1 277 ? 117.103 70.509  97.598  1.00 229.11 ? 1054 VAL A N   1 
ATOM   1189 C  CA  . VAL A 1 277 ? 117.849 71.744  97.813  1.00 227.82 ? 1054 VAL A CA  1 
ATOM   1190 C  C   . VAL A 1 277 ? 118.147 72.378  96.460  1.00 227.70 ? 1054 VAL A C   1 
ATOM   1191 O  O   . VAL A 1 277 ? 118.765 71.753  95.592  1.00 227.70 ? 1054 VAL A O   1 
ATOM   1192 C  CB  . VAL A 1 277 ? 119.141 71.482  98.598  1.00 227.78 ? 1054 VAL A CB  1 
ATOM   1193 C  CG1 . VAL A 1 277 ? 119.753 72.794  99.064  1.00 226.35 ? 1054 VAL A CG1 1 
ATOM   1194 C  CG2 . VAL A 1 277 ? 118.864 70.566  99.781  1.00 227.53 ? 1054 VAL A CG2 1 
ATOM   1195 N  N   . VAL A 1 278 ? 117.709 73.621  96.280  1.00 226.25 ? 1055 VAL A N   1 
ATOM   1196 C  CA  . VAL A 1 278 ? 117.913 74.368  95.046  1.00 226.76 ? 1055 VAL A CA  1 
ATOM   1197 C  C   . VAL A 1 278 ? 118.608 75.677  95.390  1.00 226.67 ? 1055 VAL A C   1 
ATOM   1198 O  O   . VAL A 1 278 ? 118.171 76.398  96.295  1.00 227.09 ? 1055 VAL A O   1 
ATOM   1199 C  CB  . VAL A 1 278 ? 116.584 74.630  94.313  1.00 225.71 ? 1055 VAL A CB  1 
ATOM   1200 C  CG1 . VAL A 1 278 ? 116.808 75.525  93.103  1.00 225.22 ? 1055 VAL A CG1 1 
ATOM   1201 C  CG2 . VAL A 1 278 ? 115.938 73.317  93.899  1.00 225.87 ? 1055 VAL A CG2 1 
ATOM   1202 N  N   . GLY A 1 279 ? 119.688 75.981  94.670  1.00 215.87 ? 1056 GLY A N   1 
ATOM   1203 C  CA  . GLY A 1 279 ? 120.432 77.203  94.912  1.00 214.84 ? 1056 GLY A CA  1 
ATOM   1204 C  C   . GLY A 1 279 ? 119.702 78.474  94.531  1.00 215.29 ? 1056 GLY A C   1 
ATOM   1205 O  O   . GLY A 1 279 ? 120.112 79.555  94.968  1.00 214.48 ? 1056 GLY A O   1 
ATOM   1206 N  N   . ASP A 1 280 ? 118.640 78.373  93.736  1.00 216.44 ? 1057 ASP A N   1 
ATOM   1207 C  CA  . ASP A 1 280 ? 117.879 79.548  93.323  1.00 216.04 ? 1057 ASP A CA  1 
ATOM   1208 C  C   . ASP A 1 280 ? 117.074 80.071  94.507  1.00 215.33 ? 1057 ASP A C   1 
ATOM   1209 O  O   . ASP A 1 280 ? 116.086 79.454  94.918  1.00 215.25 ? 1057 ASP A O   1 
ATOM   1210 C  CB  . ASP A 1 280 ? 116.966 79.199  92.151  1.00 216.10 ? 1057 ASP A CB  1 
ATOM   1211 C  CG  . ASP A 1 280 ? 116.483 80.427  91.402  1.00 215.91 ? 1057 ASP A CG  1 
ATOM   1212 O  OD1 . ASP A 1 280 ? 116.749 81.555  91.868  1.00 215.46 ? 1057 ASP A OD1 1 
ATOM   1213 O  OD2 . ASP A 1 280 ? 115.838 80.263  90.346  1.00 215.92 ? 1057 ASP A OD2 1 
ATOM   1214 N  N   . VAL A 1 281 ? 117.499 81.212  95.055  1.00 199.28 ? 1058 VAL A N   1 
ATOM   1215 C  CA  . VAL A 1 281 ? 116.799 81.799  96.195  1.00 198.69 ? 1058 VAL A CA  1 
ATOM   1216 C  C   . VAL A 1 281 ? 115.390 82.216  95.797  1.00 198.77 ? 1058 VAL A C   1 
ATOM   1217 O  O   . VAL A 1 281 ? 114.435 82.043  96.564  1.00 198.84 ? 1058 VAL A O   1 
ATOM   1218 C  CB  . VAL A 1 281 ? 117.602 82.984  96.761  1.00 198.37 ? 1058 VAL A CB  1 
ATOM   1219 C  CG1 . VAL A 1 281 ? 117.043 83.407  98.111  1.00 196.78 ? 1058 VAL A CG1 1 
ATOM   1220 C  CG2 . VAL A 1 281 ? 119.074 82.623  96.873  1.00 198.71 ? 1058 VAL A CG2 1 
ATOM   1221 N  N   . LEU A 1 282 ? 115.238 82.777  94.594  1.00 200.10 ? 1059 LEU A N   1 
ATOM   1222 C  CA  . LEU A 1 282 ? 113.918 83.192  94.132  1.00 199.87 ? 1059 LEU A CA  1 
ATOM   1223 C  C   . LEU A 1 282 ? 112.978 82.001  93.998  1.00 201.05 ? 1059 LEU A C   1 
ATOM   1224 O  O   . LEU A 1 282 ? 111.818 82.065  94.423  1.00 201.37 ? 1059 LEU A O   1 
ATOM   1225 C  CB  . LEU A 1 282 ? 114.040 83.933  92.801  1.00 199.89 ? 1059 LEU A CB  1 
ATOM   1226 C  CG  . LEU A 1 282 ? 112.846 84.792  92.383  1.00 199.03 ? 1059 LEU A CG  1 
ATOM   1227 C  CD1 . LEU A 1 282 ? 113.312 86.164  91.928  1.00 198.67 ? 1059 LEU A CD1 1 
ATOM   1228 C  CD2 . LEU A 1 282 ? 112.050 84.104  91.286  1.00 198.52 ? 1059 LEU A CD2 1 
ATOM   1229 N  N   . GLU A 1 283 ? 113.460 80.902  93.412  1.00 205.97 ? 1060 GLU A N   1 
ATOM   1230 C  CA  . GLU A 1 283 ? 112.629 79.710  93.281  1.00 204.23 ? 1060 GLU A CA  1 
ATOM   1231 C  C   . GLU A 1 283 ? 112.298 79.115  94.644  1.00 203.81 ? 1060 GLU A C   1 
ATOM   1232 O  O   . GLU A 1 283 ? 111.168 78.668  94.874  1.00 204.28 ? 1060 GLU A O   1 
ATOM   1233 C  CB  . GLU A 1 283 ? 113.327 78.676  92.399  1.00 204.44 ? 1060 GLU A CB  1 
ATOM   1234 C  CG  . GLU A 1 283 ? 112.946 78.757  90.930  1.00 205.14 ? 1060 GLU A CG  1 
ATOM   1235 C  CD  . GLU A 1 283 ? 113.687 77.744  90.080  1.00 206.13 ? 1060 GLU A CD  1 
ATOM   1236 O  OE1 . GLU A 1 283 ? 113.770 76.568  90.493  1.00 206.53 ? 1060 GLU A OE1 1 
ATOM   1237 O  OE2 . GLU A 1 283 ? 114.186 78.123  89.001  1.00 206.64 ? 1060 GLU A OE2 1 
ATOM   1238 N  N   . PHE A 1 284 ? 113.271 79.100  95.559  1.00 188.23 ? 1061 PHE A N   1 
ATOM   1239 C  CA  . PHE A 1 284 ? 113.017 78.583  96.900  1.00 187.78 ? 1061 PHE A CA  1 
ATOM   1240 C  C   . PHE A 1 284 ? 111.957 79.409  97.616  1.00 187.84 ? 1061 PHE A C   1 
ATOM   1241 O  O   . PHE A 1 284 ? 111.091 78.859  98.307  1.00 187.29 ? 1061 PHE A O   1 
ATOM   1242 C  CB  . PHE A 1 284 ? 114.317 78.559  97.704  1.00 188.36 ? 1061 PHE A CB  1 
ATOM   1243 C  CG  . PHE A 1 284 ? 114.114 78.414  99.184  1.00 187.44 ? 1061 PHE A CG  1 
ATOM   1244 C  CD1 . PHE A 1 284 ? 113.709 77.206  99.726  1.00 188.67 ? 1061 PHE A CD1 1 
ATOM   1245 C  CD2 . PHE A 1 284 ? 114.334 79.484  100.035 1.00 186.69 ? 1061 PHE A CD2 1 
ATOM   1246 C  CE1 . PHE A 1 284 ? 113.523 77.070  101.089 1.00 188.48 ? 1061 PHE A CE1 1 
ATOM   1247 C  CE2 . PHE A 1 284 ? 114.149 79.354  101.398 1.00 186.33 ? 1061 PHE A CE2 1 
ATOM   1248 C  CZ  . PHE A 1 284 ? 113.744 78.145  101.925 1.00 186.77 ? 1061 PHE A CZ  1 
ATOM   1249 N  N   . GLY A 1 285 ? 112.009 80.733  97.464  1.00 201.09 ? 1062 GLY A N   1 
ATOM   1250 C  CA  . GLY A 1 285 ? 110.994 81.577  98.071  1.00 200.92 ? 1062 GLY A CA  1 
ATOM   1251 C  C   . GLY A 1 285 ? 109.630 81.410  97.430  1.00 201.19 ? 1062 GLY A C   1 
ATOM   1252 O  O   . GLY A 1 285 ? 108.606 81.419  98.119  1.00 202.69 ? 1062 GLY A O   1 
ATOM   1253 N  N   . ASN A 1 286 ? 109.593 81.257  96.104  1.00 194.60 ? 1063 ASN A N   1 
ATOM   1254 C  CA  . ASN A 1 286 ? 108.315 81.128  95.412  1.00 193.73 ? 1063 ASN A CA  1 
ATOM   1255 C  C   . ASN A 1 286 ? 107.672 79.769  95.654  1.00 194.41 ? 1063 ASN A C   1 
ATOM   1256 O  O   . ASN A 1 286 ? 106.445 79.643  95.565  1.00 193.74 ? 1063 ASN A O   1 
ATOM   1257 C  CB  . ASN A 1 286 ? 108.503 81.364  93.914  1.00 193.16 ? 1063 ASN A CB  1 
ATOM   1258 C  CG  . ASN A 1 286 ? 108.164 82.783  93.501  1.00 193.29 ? 1063 ASN A CG  1 
ATOM   1259 O  OD1 . ASN A 1 286 ? 107.086 83.291  93.810  1.00 192.52 ? 1063 ASN A OD1 1 
ATOM   1260 N  ND2 . ASN A 1 286 ? 109.085 83.429  92.797  1.00 194.67 ? 1063 ASN A ND2 1 
ATOM   1261 N  N   . SER A 1 287 ? 108.472 78.745  95.957  1.00 203.47 ? 1064 SER A N   1 
ATOM   1262 C  CA  . SER A 1 287 ? 107.922 77.414  96.185  1.00 202.67 ? 1064 SER A CA  1 
ATOM   1263 C  C   . SER A 1 287 ? 107.154 77.300  97.495  1.00 202.54 ? 1064 SER A C   1 
ATOM   1264 O  O   . SER A 1 287 ? 106.491 76.280  97.713  1.00 203.14 ? 1064 SER A O   1 
ATOM   1265 C  CB  . SER A 1 287 ? 109.042 76.374  96.156  1.00 203.66 ? 1064 SER A CB  1 
ATOM   1266 O  OG  . SER A 1 287 ? 108.661 75.197  96.847  1.00 204.65 ? 1064 SER A OG  1 
ATOM   1267 N  N   . TRP A 1 288 ? 107.223 78.306  98.366  1.00 183.08 ? 1065 TRP A N   1 
ATOM   1268 C  CA  . TRP A 1 288 ? 106.561 78.266  99.663  1.00 181.07 ? 1065 TRP A CA  1 
ATOM   1269 C  C   . TRP A 1 288 ? 105.287 79.103  99.700  1.00 180.73 ? 1065 TRP A C   1 
ATOM   1270 O  O   . TRP A 1 288 ? 104.780 79.398  100.787 1.00 179.13 ? 1065 TRP A O   1 
ATOM   1271 C  CB  . TRP A 1 288 ? 107.524 78.723  100.760 1.00 178.84 ? 1065 TRP A CB  1 
ATOM   1272 C  CG  . TRP A 1 288 ? 108.336 77.610  101.345 1.00 178.79 ? 1065 TRP A CG  1 
ATOM   1273 C  CD1 . TRP A 1 288 ? 109.693 77.476  101.302 1.00 181.39 ? 1065 TRP A CD1 1 
ATOM   1274 C  CD2 . TRP A 1 288 ? 107.843 76.472  102.063 1.00 179.72 ? 1065 TRP A CD2 1 
ATOM   1275 N  NE1 . TRP A 1 288 ? 110.076 76.326  101.948 1.00 182.96 ? 1065 TRP A NE1 1 
ATOM   1276 C  CE2 . TRP A 1 288 ? 108.959 75.692  102.424 1.00 181.24 ? 1065 TRP A CE2 1 
ATOM   1277 C  CE3 . TRP A 1 288 ? 106.567 76.038  102.435 1.00 180.49 ? 1065 TRP A CE3 1 
ATOM   1278 C  CZ2 . TRP A 1 288 ? 108.837 74.502  103.139 1.00 180.86 ? 1065 TRP A CZ2 1 
ATOM   1279 C  CZ3 . TRP A 1 288 ? 106.449 74.857  103.144 1.00 182.35 ? 1065 TRP A CZ3 1 
ATOM   1280 C  CH2 . TRP A 1 288 ? 107.577 74.103  103.488 1.00 181.79 ? 1065 TRP A CH2 1 
ATOM   1281 N  N   . LYS A 1 289 ? 104.763 79.495  98.541  1.00 187.74 ? 1066 LYS A N   1 
ATOM   1282 C  CA  . LYS A 1 289 ? 103.538 80.281  98.508  1.00 186.26 ? 1066 LYS A CA  1 
ATOM   1283 C  C   . LYS A 1 289 ? 102.346 79.429  98.928  1.00 187.76 ? 1066 LYS A C   1 
ATOM   1284 O  O   . LYS A 1 289 ? 102.283 78.231  98.637  1.00 188.92 ? 1066 LYS A O   1 
ATOM   1285 C  CB  . LYS A 1 289 ? 103.309 80.858  97.111  1.00 186.66 ? 1066 LYS A CB  1 
ATOM   1286 C  CG  . LYS A 1 289 ? 103.201 79.815  96.010  1.00 188.25 ? 1066 LYS A CG  1 
ATOM   1287 C  CD  . LYS A 1 289 ? 102.609 80.410  94.743  1.00 188.39 ? 1066 LYS A CD  1 
ATOM   1288 C  CE  . LYS A 1 289 ? 103.404 81.618  94.277  1.00 189.04 ? 1066 LYS A CE  1 
ATOM   1289 N  NZ  . LYS A 1 289 ? 102.797 82.254  93.075  1.00 189.95 ? 1066 LYS A NZ  1 
ATOM   1290 N  N   . LEU A 1 290 ? 101.398 80.055  99.627  1.00 184.10 ? 1067 LEU A N   1 
ATOM   1291 C  CA  . LEU A 1 290 ? 100.220 79.334  100.096 1.00 184.04 ? 1067 LEU A CA  1 
ATOM   1292 C  C   . LEU A 1 290 ? 99.158  79.250  99.004  1.00 185.43 ? 1067 LEU A C   1 
ATOM   1293 O  O   . LEU A 1 290 ? 98.778  78.155  98.575  1.00 185.10 ? 1067 LEU A O   1 
ATOM   1294 C  CB  . LEU A 1 290 ? 99.663  80.007  101.356 1.00 182.78 ? 1067 LEU A CB  1 
ATOM   1295 C  CG  . LEU A 1 290 ? 98.777  79.191  102.307 1.00 182.88 ? 1067 LEU A CG  1 
ATOM   1296 C  CD1 . LEU A 1 290 ? 98.687  79.886  103.656 1.00 183.71 ? 1067 LEU A CD1 1 
ATOM   1297 C  CD2 . LEU A 1 290 ? 97.380  78.959  101.746 1.00 183.08 ? 1067 LEU A CD2 1 
ATOM   1298 N  N   . SER A 1 291 ? 98.671  80.396  98.544  1.00 198.07 ? 1068 SER A N   1 
ATOM   1299 C  CA  . SER A 1 291 ? 97.636  80.417  97.518  1.00 196.99 ? 1068 SER A CA  1 
ATOM   1300 C  C   . SER A 1 291 ? 98.256  80.183  96.146  1.00 197.21 ? 1068 SER A C   1 
ATOM   1301 O  O   . SER A 1 291 ? 99.151  80.937  95.747  1.00 197.61 ? 1068 SER A O   1 
ATOM   1302 C  CB  . SER A 1 291 ? 96.892  81.745  97.536  1.00 197.19 ? 1068 SER A CB  1 
ATOM   1303 O  OG  . SER A 1 291 ? 96.320  82.024  96.271  1.00 197.59 ? 1068 SER A OG  1 
ATOM   1304 N  N   . PRO A 1 292 ? 97.822  79.165  95.400  1.00 200.38 ? 1069 PRO A N   1 
ATOM   1305 C  CA  . PRO A 1 292 ? 98.397  78.935  94.064  1.00 201.27 ? 1069 PRO A CA  1 
ATOM   1306 C  C   . PRO A 1 292 ? 98.114  80.053  93.077  1.00 201.42 ? 1069 PRO A C   1 
ATOM   1307 O  O   . PRO A 1 292 ? 98.831  80.169  92.075  1.00 200.92 ? 1069 PRO A O   1 
ATOM   1308 C  CB  . PRO A 1 292 ? 97.742  77.618  93.619  1.00 200.52 ? 1069 PRO A CB  1 
ATOM   1309 C  CG  . PRO A 1 292 ? 97.227  76.987  94.881  1.00 199.84 ? 1069 PRO A CG  1 
ATOM   1310 C  CD  . PRO A 1 292 ? 96.846  78.127  95.770  1.00 199.56 ? 1069 PRO A CD  1 
ATOM   1311 N  N   . SER A 1 293 ? 97.096  80.877  93.320  1.00 204.33 ? 1070 SER A N   1 
ATOM   1312 C  CA  . SER A 1 293 ? 96.738  81.954  92.406  1.00 204.25 ? 1070 SER A CA  1 
ATOM   1313 C  C   . SER A 1 293 ? 97.612  83.191  92.566  1.00 203.71 ? 1070 SER A C   1 
ATOM   1314 O  O   . SER A 1 293 ? 97.459  84.139  91.789  1.00 203.58 ? 1070 SER A O   1 
ATOM   1315 C  CB  . SER A 1 293 ? 95.268  82.336  92.596  1.00 203.52 ? 1070 SER A CB  1 
ATOM   1316 O  OG  . SER A 1 293 ? 94.905  83.407  91.742  1.00 203.38 ? 1070 SER A OG  1 
ATOM   1317 N  N   . CYS A 1 294 ? 98.509  83.209  93.546  1.00 206.70 ? 1071 CYS A N   1 
ATOM   1318 C  CA  . CYS A 1 294 ? 99.364  84.369  93.745  1.00 206.52 ? 1071 CYS A CA  1 
ATOM   1319 C  C   . CYS A 1 294 ? 100.357 84.498  92.591  1.00 206.80 ? 1071 CYS A C   1 
ATOM   1320 O  O   . CYS A 1 294 ? 100.855 83.489  92.083  1.00 207.07 ? 1071 CYS A O   1 
ATOM   1321 C  CB  . CYS A 1 294 ? 100.120 84.259  95.067  1.00 207.04 ? 1071 CYS A CB  1 
ATOM   1322 S  SG  . CYS A 1 294 ? 99.092  84.423  96.539  1.00 211.75 ? 1071 CYS A SG  1 
ATOM   1323 N  N   . PRO A 1 295 ? 100.657 85.718  92.153  1.00 205.87 ? 1072 PRO A N   1 
ATOM   1324 C  CA  . PRO A 1 295 ? 101.663 85.894  91.100  1.00 206.29 ? 1072 PRO A CA  1 
ATOM   1325 C  C   . PRO A 1 295 ? 103.048 85.497  91.584  1.00 206.30 ? 1072 PRO A C   1 
ATOM   1326 O  O   . PRO A 1 295 ? 103.385 85.633  92.763  1.00 206.12 ? 1072 PRO A O   1 
ATOM   1327 C  CB  . PRO A 1 295 ? 101.594 87.394  90.784  1.00 206.48 ? 1072 PRO A CB  1 
ATOM   1328 C  CG  . PRO A 1 295 ? 100.282 87.855  91.346  1.00 206.14 ? 1072 PRO A CG  1 
ATOM   1329 C  CD  . PRO A 1 295 ? 100.033 86.993  92.540  1.00 205.77 ? 1072 PRO A CD  1 
ATOM   1330 N  N   . ASP A 1 296 ? 103.853 84.998  90.651  1.00 203.03 ? 1073 ASP A N   1 
ATOM   1331 C  CA  . ASP A 1 296 ? 105.208 84.582  90.983  1.00 202.48 ? 1073 ASP A CA  1 
ATOM   1332 C  C   . ASP A 1 296 ? 106.097 85.798  91.214  1.00 201.76 ? 1073 ASP A C   1 
ATOM   1333 O  O   . ASP A 1 296 ? 105.998 86.805  90.508  1.00 201.70 ? 1073 ASP A O   1 
ATOM   1334 C  CB  . ASP A 1 296 ? 105.784 83.711  89.867  1.00 203.47 ? 1073 ASP A CB  1 
ATOM   1335 C  CG  . ASP A 1 296 ? 106.972 82.889  90.324  1.00 203.68 ? 1073 ASP A CG  1 
ATOM   1336 O  OD1 . ASP A 1 296 ? 108.079 83.455  90.443  1.00 204.51 ? 1073 ASP A OD1 1 
ATOM   1337 O  OD2 . ASP A 1 296 ? 106.800 81.676  90.567  1.00 202.79 ? 1073 ASP A OD2 1 
ATOM   1338 N  N   . ALA A 1 297 ? 106.970 85.698  92.212  1.00 180.98 ? 1074 ALA A N   1 
ATOM   1339 C  CA  . ALA A 1 297 ? 107.861 86.801  92.540  1.00 179.71 ? 1074 ALA A CA  1 
ATOM   1340 C  C   . ALA A 1 297 ? 108.954 86.946  91.488  1.00 180.66 ? 1074 ALA A C   1 
ATOM   1341 O  O   . ALA A 1 297 ? 109.339 85.983  90.819  1.00 181.15 ? 1074 ALA A O   1 
ATOM   1342 C  CB  . ALA A 1 297 ? 108.485 86.592  93.919  1.00 178.28 ? 1074 ALA A CB  1 
ATOM   1343 N  N   . LEU A 1 298 ? 109.455 88.168  91.346  1.00 181.61 ? 1075 LEU A N   1 
ATOM   1344 C  CA  . LEU A 1 298 ? 110.504 88.489  90.392  1.00 181.01 ? 1075 LEU A CA  1 
ATOM   1345 C  C   . LEU A 1 298 ? 111.677 89.142  91.112  1.00 180.86 ? 1075 LEU A C   1 
ATOM   1346 O  O   . LEU A 1 298 ? 111.585 89.533  92.279  1.00 181.01 ? 1075 LEU A O   1 
ATOM   1347 C  CB  . LEU A 1 298 ? 109.981 89.410  89.282  1.00 181.22 ? 1075 LEU A CB  1 
ATOM   1348 C  CG  . LEU A 1 298 ? 109.605 88.738  87.960  1.00 181.61 ? 1075 LEU A CG  1 
ATOM   1349 C  CD1 . LEU A 1 298 ? 108.376 87.858  88.129  1.00 182.17 ? 1075 LEU A CD1 1 
ATOM   1350 C  CD2 . LEU A 1 298 ? 109.379 89.779  86.874  1.00 181.77 ? 1075 LEU A CD2 1 
ATOM   1351 N  N   . ALA A 1 299 ? 112.793 89.249  90.398  1.00 183.46 ? 1076 ALA A N   1 
ATOM   1352 C  CA  . ALA A 1 299 ? 113.987 89.847  90.974  1.00 184.73 ? 1076 ALA A CA  1 
ATOM   1353 C  C   . ALA A 1 299 ? 113.767 91.340  91.211  1.00 185.89 ? 1076 ALA A C   1 
ATOM   1354 O  O   . ALA A 1 299 ? 113.177 92.024  90.369  1.00 185.74 ? 1076 ALA A O   1 
ATOM   1355 C  CB  . ALA A 1 299 ? 115.191 89.635  90.058  1.00 184.11 ? 1076 ALA A CB  1 
ATOM   1356 N  N   . PRO A 1 300 ? 114.225 91.872  92.339  1.00 188.70 ? 1077 PRO A N   1 
ATOM   1357 C  CA  . PRO A 1 300 ? 114.045 93.295  92.627  1.00 188.14 ? 1077 PRO A CA  1 
ATOM   1358 C  C   . PRO A 1 300 ? 115.164 94.136  92.022  1.00 188.38 ? 1077 PRO A C   1 
ATOM   1359 O  O   . PRO A 1 300 ? 116.194 93.628  91.573  1.00 187.47 ? 1077 PRO A O   1 
ATOM   1360 C  CB  . PRO A 1 300 ? 114.086 93.352  94.164  1.00 186.51 ? 1077 PRO A CB  1 
ATOM   1361 C  CG  . PRO A 1 300 ? 114.574 91.986  94.628  1.00 186.84 ? 1077 PRO A CG  1 
ATOM   1362 C  CD  . PRO A 1 300 ? 114.939 91.179  93.421  1.00 187.81 ? 1077 PRO A CD  1 
ATOM   1363 N  N   . LYS A 1 301 ? 114.937 95.445  92.020  1.00 188.72 ? 1078 LYS A N   1 
ATOM   1364 C  CA  . LYS A 1 301 ? 115.887 96.408  91.494  1.00 188.26 ? 1078 LYS A CA  1 
ATOM   1365 C  C   . LYS A 1 301 ? 116.658 97.052  92.645  1.00 187.80 ? 1078 LYS A C   1 
ATOM   1366 O  O   . LYS A 1 301 ? 116.527 96.660  93.809  1.00 187.89 ? 1078 LYS A O   1 
ATOM   1367 C  CB  . LYS A 1 301 ? 115.158 97.449  90.642  1.00 186.71 ? 1078 LYS A CB  1 
ATOM   1368 C  CG  . LYS A 1 301 ? 113.963 96.900  89.883  1.00 185.86 ? 1078 LYS A CG  1 
ATOM   1369 C  CD  . LYS A 1 301 ? 113.383 97.941  88.941  1.00 186.96 ? 1078 LYS A CD  1 
ATOM   1370 C  CE  . LYS A 1 301 ? 112.890 99.160  89.702  1.00 186.65 ? 1078 LYS A CE  1 
ATOM   1371 N  NZ  . LYS A 1 301 ? 112.236 100.149 88.803  1.00 187.80 ? 1078 LYS A NZ  1 
ATOM   1372 N  N   . ASP A 1 302 ? 117.474 98.054  92.322  1.00 181.12 ? 1079 ASP A N   1 
ATOM   1373 C  CA  . ASP A 1 302 ? 118.241 98.765  93.332  1.00 180.14 ? 1079 ASP A CA  1 
ATOM   1374 C  C   . ASP A 1 302 ? 117.485 100.020 93.736  1.00 180.47 ? 1079 ASP A C   1 
ATOM   1375 O  O   . ASP A 1 302 ? 117.334 100.933 92.908  1.00 182.31 ? 1079 ASP A O   1 
ATOM   1376 C  CB  . ASP A 1 302 ? 119.628 99.125  92.804  1.00 180.70 ? 1079 ASP A CB  1 
ATOM   1377 C  CG  . ASP A 1 302 ? 120.480 99.836  93.839  1.00 181.86 ? 1079 ASP A CG  1 
ATOM   1378 O  OD1 . ASP A 1 302 ? 120.179 99.719  95.045  1.00 180.85 ? 1079 ASP A OD1 1 
ATOM   1379 O  OD2 . ASP A 1 302 ? 121.453 100.513 93.446  1.00 183.66 ? 1079 ASP A OD2 1 
ATOM   1380 N  N   . PRO A 1 303 ? 116.984 100.113 94.971  1.00 167.33 ? 1080 PRO A N   1 
ATOM   1381 C  CA  . PRO A 1 303 ? 116.259 101.331 95.370  1.00 168.41 ? 1080 PRO A CA  1 
ATOM   1382 C  C   . PRO A 1 303 ? 117.124 102.578 95.349  1.00 168.94 ? 1080 PRO A C   1 
ATOM   1383 O  O   . PRO A 1 303 ? 116.631 103.663 95.016  1.00 168.46 ? 1080 PRO A O   1 
ATOM   1384 C  CB  . PRO A 1 303 ? 115.772 100.995 96.787  1.00 168.67 ? 1080 PRO A CB  1 
ATOM   1385 C  CG  . PRO A 1 303 ? 116.708 99.935  97.270  1.00 167.87 ? 1080 PRO A CG  1 
ATOM   1386 C  CD  . PRO A 1 303 ? 117.061 99.126  96.060  1.00 167.25 ? 1080 PRO A CD  1 
ATOM   1387 N  N   . CYS A 1 304 ? 118.407 102.455 95.696  1.00 190.34 ? 1081 CYS A N   1 
ATOM   1388 C  CA  . CYS A 1 304 ? 119.287 103.618 95.684  1.00 191.30 ? 1081 CYS A CA  1 
ATOM   1389 C  C   . CYS A 1 304 ? 119.513 104.123 94.264  1.00 191.47 ? 1081 CYS A C   1 
ATOM   1390 O  O   . CYS A 1 304 ? 119.560 105.336 94.030  1.00 193.26 ? 1081 CYS A O   1 
ATOM   1391 C  CB  . CYS A 1 304 ? 120.615 103.277 96.357  1.00 190.90 ? 1081 CYS A CB  1 
ATOM   1392 S  SG  . CYS A 1 304 ? 120.524 103.161 98.162  1.00 200.00 ? 1081 CYS A SG  1 
ATOM   1393 N  N   . THR A 1 305 ? 119.658 103.208 93.304  1.00 175.97 ? 1082 THR A N   1 
ATOM   1394 C  CA  . THR A 1 305 ? 119.779 103.618 91.909  1.00 175.29 ? 1082 THR A CA  1 
ATOM   1395 C  C   . THR A 1 305 ? 118.467 104.198 91.393  1.00 174.91 ? 1082 THR A C   1 
ATOM   1396 O  O   . THR A 1 305 ? 118.470 105.156 90.610  1.00 173.16 ? 1082 THR A O   1 
ATOM   1397 C  CB  . THR A 1 305 ? 120.219 102.434 91.047  1.00 174.60 ? 1082 THR A CB  1 
ATOM   1398 O  OG1 . THR A 1 305 ? 121.418 101.867 91.589  1.00 175.54 ? 1082 THR A OG1 1 
ATOM   1399 C  CG2 . THR A 1 305 ? 120.481 102.879 89.617  1.00 172.84 ? 1082 THR A CG2 1 
ATOM   1400 N  N   . ALA A 1 306 ? 117.337 103.634 91.824  1.00 170.72 ? 1083 ALA A N   1 
ATOM   1401 C  CA  . ALA A 1 306 ? 116.041 104.147 91.391  1.00 169.22 ? 1083 ALA A CA  1 
ATOM   1402 C  C   . ALA A 1 306 ? 115.797 105.556 91.916  1.00 169.28 ? 1083 ALA A C   1 
ATOM   1403 O  O   . ALA A 1 306 ? 115.212 106.392 91.217  1.00 169.67 ? 1083 ALA A O   1 
ATOM   1404 C  CB  . ALA A 1 306 ? 114.926 103.204 91.842  1.00 169.78 ? 1083 ALA A CB  1 
ATOM   1405 N  N   . ASN A 1 307 ? 116.235 105.839 93.141  1.00 169.09 ? 1084 ASN A N   1 
ATOM   1406 C  CA  . ASN A 1 307 ? 116.068 107.150 93.768  1.00 168.58 ? 1084 ASN A CA  1 
ATOM   1407 C  C   . ASN A 1 307 ? 117.437 107.645 94.214  1.00 170.29 ? 1084 ASN A C   1 
ATOM   1408 O  O   . ASN A 1 307 ? 117.813 107.502 95.385  1.00 172.13 ? 1084 ASN A O   1 
ATOM   1409 C  CB  . ASN A 1 307 ? 115.091 107.082 94.941  1.00 167.68 ? 1084 ASN A CB  1 
ATOM   1410 C  CG  . ASN A 1 307 ? 113.670 106.797 94.499  1.00 168.26 ? 1084 ASN A CG  1 
ATOM   1411 O  OD1 . ASN A 1 307 ? 113.294 107.076 93.360  1.00 169.63 ? 1084 ASN A OD1 1 
ATOM   1412 N  ND2 . ASN A 1 307 ? 112.870 106.238 95.399  1.00 168.75 ? 1084 ASN A ND2 1 
ATOM   1413 N  N   . PRO A 1 308 ? 118.213 108.237 93.301  1.00 149.87 ? 1085 PRO A N   1 
ATOM   1414 C  CA  . PRO A 1 308 ? 119.569 108.677 93.654  1.00 148.81 ? 1085 PRO A CA  1 
ATOM   1415 C  C   . PRO A 1 308 ? 119.620 109.941 94.496  1.00 148.99 ? 1085 PRO A C   1 
ATOM   1416 O  O   . PRO A 1 308 ? 120.711 110.315 94.947  1.00 149.74 ? 1085 PRO A O   1 
ATOM   1417 C  CB  . PRO A 1 308 ? 120.223 108.906 92.287  1.00 146.09 ? 1085 PRO A CB  1 
ATOM   1418 C  CG  . PRO A 1 308 ? 119.087 109.282 91.399  1.00 145.95 ? 1085 PRO A CG  1 
ATOM   1419 C  CD  . PRO A 1 308 ? 117.884 108.520 91.893  1.00 147.29 ? 1085 PRO A CD  1 
ATOM   1420 N  N   . PHE A 1 309 ? 118.492 110.609 94.723  1.00 153.15 ? 1086 PHE A N   1 
ATOM   1421 C  CA  . PHE A 1 309 ? 118.470 111.843 95.496  1.00 153.52 ? 1086 PHE A CA  1 
ATOM   1422 C  C   . PHE A 1 309 ? 118.345 111.605 96.996  1.00 152.96 ? 1086 PHE A C   1 
ATOM   1423 O  O   . PHE A 1 309 ? 118.297 112.574 97.759  1.00 153.80 ? 1086 PHE A O   1 
ATOM   1424 C  CB  . PHE A 1 309 ? 117.329 112.750 95.018  1.00 152.73 ? 1086 PHE A CB  1 
ATOM   1425 C  CG  . PHE A 1 309 ? 116.077 112.009 94.647  1.00 153.45 ? 1086 PHE A CG  1 
ATOM   1426 C  CD1 . PHE A 1 309 ? 115.145 111.670 95.612  1.00 154.29 ? 1086 PHE A CD1 1 
ATOM   1427 C  CD2 . PHE A 1 309 ? 115.827 111.659 93.330  1.00 152.63 ? 1086 PHE A CD2 1 
ATOM   1428 C  CE1 . PHE A 1 309 ? 113.991 110.990 95.274  1.00 154.73 ? 1086 PHE A CE1 1 
ATOM   1429 C  CE2 . PHE A 1 309 ? 114.675 110.979 92.985  1.00 154.04 ? 1086 PHE A CE2 1 
ATOM   1430 C  CZ  . PHE A 1 309 ? 113.756 110.644 93.958  1.00 154.99 ? 1086 PHE A CZ  1 
ATOM   1431 N  N   . ARG A 1 310 ? 118.291 110.348 97.435  1.00 135.44 ? 1087 ARG A N   1 
ATOM   1432 C  CA  . ARG A 1 310 ? 118.241 110.022 98.853  1.00 135.39 ? 1087 ARG A CA  1 
ATOM   1433 C  C   . ARG A 1 310 ? 119.467 109.260 99.335  1.00 136.69 ? 1087 ARG A C   1 
ATOM   1434 O  O   . ARG A 1 310 ? 119.516 108.878 100.510 1.00 138.56 ? 1087 ARG A O   1 
ATOM   1435 C  CB  . ARG A 1 310 ? 116.982 109.204 99.171  1.00 136.25 ? 1087 ARG A CB  1 
ATOM   1436 C  CG  . ARG A 1 310 ? 115.739 109.657 98.429  1.00 137.17 ? 1087 ARG A CG  1 
ATOM   1437 C  CD  . ARG A 1 310 ? 114.619 108.637 98.559  1.00 137.68 ? 1087 ARG A CD  1 
ATOM   1438 N  NE  . ARG A 1 310 ? 114.445 108.189 99.935  1.00 136.63 ? 1087 ARG A NE  1 
ATOM   1439 C  CZ  . ARG A 1 310 ? 113.449 108.564 100.725 1.00 135.67 ? 1087 ARG A CZ  1 
ATOM   1440 N  NH1 . ARG A 1 310 ? 112.512 109.399 100.306 1.00 135.83 ? 1087 ARG A NH1 1 
ATOM   1441 N  NH2 . ARG A 1 310 ? 113.390 108.090 101.966 1.00 136.25 ? 1087 ARG A NH2 1 
ATOM   1442 N  N   . LYS A 1 311 ? 120.454 109.026 98.466  1.00 146.00 ? 1088 LYS A N   1 
ATOM   1443 C  CA  . LYS A 1 311 ? 121.613 108.228 98.854  1.00 147.36 ? 1088 LYS A CA  1 
ATOM   1444 C  C   . LYS A 1 311 ? 122.428 108.913 99.944  1.00 149.24 ? 1088 LYS A C   1 
ATOM   1445 O  O   . LYS A 1 311 ? 122.872 108.259 100.895 1.00 150.21 ? 1088 LYS A O   1 
ATOM   1446 C  CB  . LYS A 1 311 ? 122.486 107.946 97.631  1.00 147.49 ? 1088 LYS A CB  1 
ATOM   1447 C  CG  . LYS A 1 311 ? 123.477 106.811 97.826  1.00 147.91 ? 1088 LYS A CG  1 
ATOM   1448 C  CD  . LYS A 1 311 ? 124.163 106.449 96.519  1.00 148.83 ? 1088 LYS A CD  1 
ATOM   1449 C  CE  . LYS A 1 311 ? 125.132 105.293 96.707  1.00 149.59 ? 1088 LYS A CE  1 
ATOM   1450 N  NZ  . LYS A 1 311 ? 125.630 104.772 95.404  1.00 151.64 ? 1088 LYS A NZ  1 
ATOM   1451 N  N   . SER A 1 312 ? 122.639 110.225 99.824  1.00 153.41 ? 1089 SER A N   1 
ATOM   1452 C  CA  . SER A 1 312 ? 123.434 110.942 100.816 1.00 154.21 ? 1089 SER A CA  1 
ATOM   1453 C  C   . SER A 1 312 ? 122.758 110.921 102.181 1.00 154.21 ? 1089 SER A C   1 
ATOM   1454 O  O   . SER A 1 312 ? 123.403 110.658 103.204 1.00 155.44 ? 1089 SER A O   1 
ATOM   1455 C  CB  . SER A 1 312 ? 123.674 112.379 100.354 1.00 153.55 ? 1089 SER A CB  1 
ATOM   1456 O  OG  . SER A 1 312 ? 122.454 113.017 100.021 1.00 154.76 ? 1089 SER A OG  1 
ATOM   1457 N  N   . TRP A 1 313 ? 121.453 111.198 102.215 1.00 136.56 ? 1090 TRP A N   1 
ATOM   1458 C  CA  . TRP A 1 313 ? 120.720 111.167 103.477 1.00 135.71 ? 1090 TRP A CA  1 
ATOM   1459 C  C   . TRP A 1 313 ? 120.711 109.766 104.073 1.00 135.28 ? 1090 TRP A C   1 
ATOM   1460 O  O   . TRP A 1 313 ? 120.882 109.596 105.287 1.00 137.26 ? 1090 TRP A O   1 
ATOM   1461 C  CB  . TRP A 1 313 ? 119.294 111.673 103.262 1.00 134.86 ? 1090 TRP A CB  1 
ATOM   1462 C  CG  . TRP A 1 313 ? 118.449 111.669 104.498 1.00 138.29 ? 1090 TRP A CG  1 
ATOM   1463 C  CD1 . TRP A 1 313 ? 118.306 112.686 105.395 1.00 140.78 ? 1090 TRP A CD1 1 
ATOM   1464 C  CD2 . TRP A 1 313 ? 117.618 110.601 104.966 1.00 137.56 ? 1090 TRP A CD2 1 
ATOM   1465 N  NE1 . TRP A 1 313 ? 117.442 112.315 106.397 1.00 138.81 ? 1090 TRP A NE1 1 
ATOM   1466 C  CE2 . TRP A 1 313 ? 117.005 111.039 106.157 1.00 137.63 ? 1090 TRP A CE2 1 
ATOM   1467 C  CE3 . TRP A 1 313 ? 117.334 109.315 104.496 1.00 137.58 ? 1090 TRP A CE3 1 
ATOM   1468 C  CZ2 . TRP A 1 313 ? 116.127 110.239 106.883 1.00 137.49 ? 1090 TRP A CZ2 1 
ATOM   1469 C  CZ3 . TRP A 1 313 ? 116.463 108.522 105.219 1.00 139.90 ? 1090 TRP A CZ3 1 
ATOM   1470 C  CH2 . TRP A 1 313 ? 115.870 108.986 106.399 1.00 139.81 ? 1090 TRP A CH2 1 
ATOM   1471 N  N   . ALA A 1 314 ? 120.518 108.747 103.231 1.00 139.15 ? 1091 ALA A N   1 
ATOM   1472 C  CA  . ALA A 1 314 ? 120.522 107.372 103.716 1.00 141.22 ? 1091 ALA A CA  1 
ATOM   1473 C  C   . ALA A 1 314 ? 121.868 107.005 104.325 1.00 145.41 ? 1091 ALA A C   1 
ATOM   1474 O  O   . ALA A 1 314 ? 121.926 106.394 105.399 1.00 148.61 ? 1091 ALA A O   1 
ATOM   1475 C  CB  . ALA A 1 314 ? 120.172 106.416 102.577 1.00 143.73 ? 1091 ALA A CB  1 
ATOM   1476 N  N   . GLN A 1 315 ? 122.963 107.367 103.652 1.00 149.74 ? 1092 GLN A N   1 
ATOM   1477 C  CA  . GLN A 1 315 ? 124.289 107.066 104.179 1.00 148.66 ? 1092 GLN A CA  1 
ATOM   1478 C  C   . GLN A 1 315 ? 124.548 107.816 105.478 1.00 149.16 ? 1092 GLN A C   1 
ATOM   1479 O  O   . GLN A 1 315 ? 125.085 107.247 106.435 1.00 150.81 ? 1092 GLN A O   1 
ATOM   1480 C  CB  . GLN A 1 315 ? 125.356 107.407 103.139 1.00 146.00 ? 1092 GLN A CB  1 
ATOM   1481 C  CG  . GLN A 1 315 ? 126.016 106.193 102.508 1.00 147.80 ? 1092 GLN A CG  1 
ATOM   1482 C  CD  . GLN A 1 315 ? 126.690 106.516 101.191 1.00 150.57 ? 1092 GLN A CD  1 
ATOM   1483 O  OE1 . GLN A 1 315 ? 126.784 107.678 100.796 1.00 151.50 ? 1092 GLN A OE1 1 
ATOM   1484 N  NE2 . GLN A 1 315 ? 127.165 105.485 100.501 1.00 151.43 ? 1092 GLN A NE2 1 
ATOM   1485 N  N   . LYS A 1 316 ? 124.162 109.093 105.536 1.00 149.35 ? 1093 LYS A N   1 
ATOM   1486 C  CA  . LYS A 1 316 ? 124.375 109.873 106.750 1.00 149.83 ? 1093 LYS A CA  1 
ATOM   1487 C  C   . LYS A 1 316 ? 123.593 109.294 107.922 1.00 149.54 ? 1093 LYS A C   1 
ATOM   1488 O  O   . LYS A 1 316 ? 124.077 109.291 109.059 1.00 150.65 ? 1093 LYS A O   1 
ATOM   1489 C  CB  . LYS A 1 316 ? 123.985 111.332 106.511 1.00 149.44 ? 1093 LYS A CB  1 
ATOM   1490 C  CG  . LYS A 1 316 ? 124.265 112.251 107.689 1.00 150.20 ? 1093 LYS A CG  1 
ATOM   1491 C  CD  . LYS A 1 316 ? 123.564 113.591 107.530 1.00 150.83 ? 1093 LYS A CD  1 
ATOM   1492 C  CE  . LYS A 1 316 ? 123.755 114.156 106.131 1.00 151.65 ? 1093 LYS A CE  1 
ATOM   1493 N  NZ  . LYS A 1 316 ? 122.907 115.358 105.897 1.00 151.97 ? 1093 LYS A NZ  1 
ATOM   1494 N  N   . GLN A 1 317 ? 122.382 108.796 107.665 1.00 143.40 ? 1094 GLN A N   1 
ATOM   1495 C  CA  . GLN A 1 317 ? 121.584 108.233 108.749 1.00 142.93 ? 1094 GLN A CA  1 
ATOM   1496 C  C   . GLN A 1 317 ? 122.105 106.867 109.179 1.00 142.64 ? 1094 GLN A C   1 
ATOM   1497 O  O   . GLN A 1 317 ? 122.171 106.574 110.378 1.00 142.49 ? 1094 GLN A O   1 
ATOM   1498 C  CB  . GLN A 1 317 ? 120.116 108.146 108.332 1.00 146.20 ? 1094 GLN A CB  1 
ATOM   1499 C  CG  . GLN A 1 317 ? 119.430 109.498 108.209 1.00 146.72 ? 1094 GLN A CG  1 
ATOM   1500 C  CD  . GLN A 1 317 ? 118.903 110.013 109.535 1.00 147.63 ? 1094 GLN A CD  1 
ATOM   1501 O  OE1 . GLN A 1 317 ? 119.365 109.607 110.602 1.00 146.73 ? 1094 GLN A OE1 1 
ATOM   1502 N  NE2 . GLN A 1 317 ? 117.932 110.916 109.474 1.00 146.69 ? 1094 GLN A NE2 1 
ATOM   1503 N  N   . CYS A 1 318 ? 122.488 106.019 108.224 1.00 153.81 ? 1095 CYS A N   1 
ATOM   1504 C  CA  . CYS A 1 318 ? 122.934 104.669 108.550 1.00 155.02 ? 1095 CYS A CA  1 
ATOM   1505 C  C   . CYS A 1 318 ? 124.401 104.602 108.955 1.00 155.14 ? 1095 CYS A C   1 
ATOM   1506 O  O   . CYS A 1 318 ? 124.874 103.518 109.315 1.00 156.66 ? 1095 CYS A O   1 
ATOM   1507 C  CB  . CYS A 1 318 ? 122.684 103.729 107.367 1.00 156.44 ? 1095 CYS A CB  1 
ATOM   1508 S  SG  . CYS A 1 318 ? 120.944 103.544 106.899 1.00 162.87 ? 1095 CYS A SG  1 
ATOM   1509 N  N   . SER A 1 319 ? 125.132 105.718 108.906 1.00 149.24 ? 1096 SER A N   1 
ATOM   1510 C  CA  . SER A 1 319 ? 126.515 105.720 109.368 1.00 149.93 ? 1096 SER A CA  1 
ATOM   1511 C  C   . SER A 1 319 ? 126.645 105.470 110.865 1.00 149.22 ? 1096 SER A C   1 
ATOM   1512 O  O   . SER A 1 319 ? 127.758 105.208 111.333 1.00 149.29 ? 1096 SER A O   1 
ATOM   1513 C  CB  . SER A 1 319 ? 127.183 107.049 109.012 1.00 148.77 ? 1096 SER A CB  1 
ATOM   1514 O  OG  . SER A 1 319 ? 126.550 108.130 109.674 1.00 149.52 ? 1096 SER A OG  1 
ATOM   1515 N  N   . ILE A 1 320 ? 125.548 105.547 111.622 1.00 135.15 ? 1097 ILE A N   1 
ATOM   1516 C  CA  . ILE A 1 320 ? 125.603 105.293 113.057 1.00 134.31 ? 1097 ILE A CA  1 
ATOM   1517 C  C   . ILE A 1 320 ? 126.008 103.857 113.358 1.00 135.71 ? 1097 ILE A C   1 
ATOM   1518 O  O   . ILE A 1 320 ? 126.538 103.577 114.438 1.00 137.28 ? 1097 ILE A O   1 
ATOM   1519 C  CB  . ILE A 1 320 ? 124.246 105.642 113.708 1.00 133.24 ? 1097 ILE A CB  1 
ATOM   1520 C  CG1 . ILE A 1 320 ? 124.373 105.694 115.233 1.00 134.28 ? 1097 ILE A CG1 1 
ATOM   1521 C  CG2 . ILE A 1 320 ? 123.172 104.650 113.288 1.00 131.80 ? 1097 ILE A CG2 1 
ATOM   1522 C  CD1 . ILE A 1 320 ? 125.508 106.566 115.723 1.00 136.31 ? 1097 ILE A CD1 1 
ATOM   1523 N  N   . LEU A 1 321 ? 125.779 102.933 112.421 1.00 139.15 ? 1098 LEU A N   1 
ATOM   1524 C  CA  . LEU A 1 321 ? 126.172 101.545 112.639 1.00 137.68 ? 1098 LEU A CA  1 
ATOM   1525 C  C   . LEU A 1 321 ? 127.688 101.402 112.700 1.00 137.24 ? 1098 LEU A C   1 
ATOM   1526 O  O   . LEU A 1 321 ? 128.210 100.588 113.471 1.00 140.02 ? 1098 LEU A O   1 
ATOM   1527 C  CB  . LEU A 1 321 ? 125.593 100.656 111.540 1.00 137.06 ? 1098 LEU A CB  1 
ATOM   1528 C  CG  . LEU A 1 321 ? 124.101 100.329 111.637 1.00 137.48 ? 1098 LEU A CG  1 
ATOM   1529 C  CD1 . LEU A 1 321 ? 123.761 99.123  110.776 1.00 137.98 ? 1098 LEU A CD1 1 
ATOM   1530 C  CD2 . LEU A 1 321 ? 123.691 100.091 113.082 1.00 138.83 ? 1098 LEU A CD2 1 
ATOM   1531 N  N   . HIS A 1 322 ? 128.409 102.180 111.897 1.00 139.41 ? 1099 HIS A N   1 
ATOM   1532 C  CA  . HIS A 1 322 ? 129.864 102.138 111.871 1.00 140.46 ? 1099 HIS A CA  1 
ATOM   1533 C  C   . HIS A 1 322 ? 130.503 103.087 112.875 1.00 143.86 ? 1099 HIS A C   1 
ATOM   1534 O  O   . HIS A 1 322 ? 131.734 103.184 112.916 1.00 143.31 ? 1099 HIS A O   1 
ATOM   1535 C  CB  . HIS A 1 322 ? 130.374 102.460 110.463 1.00 142.40 ? 1099 HIS A CB  1 
ATOM   1536 C  CG  . HIS A 1 322 ? 130.391 101.281 109.542 1.00 144.80 ? 1099 HIS A CG  1 
ATOM   1537 N  ND1 . HIS A 1 322 ? 130.136 101.387 108.192 1.00 146.69 ? 1099 HIS A ND1 1 
ATOM   1538 C  CD2 . HIS A 1 322 ? 130.632 99.970  109.777 1.00 144.12 ? 1099 HIS A CD2 1 
ATOM   1539 C  CE1 . HIS A 1 322 ? 130.219 100.193 107.634 1.00 145.63 ? 1099 HIS A CE1 1 
ATOM   1540 N  NE2 . HIS A 1 322 ? 130.520 99.315  108.574 1.00 145.90 ? 1099 HIS A NE2 1 
ATOM   1541 N  N   . GLY A 1 323 ? 129.706 103.786 113.681 1.00 157.37 ? 1100 GLY A N   1 
ATOM   1542 C  CA  . GLY A 1 323 ? 130.239 104.718 114.643 1.00 156.92 ? 1100 GLY A CA  1 
ATOM   1543 C  C   . GLY A 1 323 ? 130.781 104.026 115.874 1.00 157.45 ? 1100 GLY A C   1 
ATOM   1544 O  O   . GLY A 1 323 ? 130.744 102.796 116.013 1.00 157.77 ? 1100 GLY A O   1 
ATOM   1545 N  N   . PRO A 1 324 ? 131.303 104.833 116.803 1.00 155.05 ? 1101 PRO A N   1 
ATOM   1546 C  CA  . PRO A 1 324 ? 131.875 104.267 118.034 1.00 154.38 ? 1101 PRO A CA  1 
ATOM   1547 C  C   . PRO A 1 324 ? 130.837 103.743 119.012 1.00 153.36 ? 1101 PRO A C   1 
ATOM   1548 O  O   . PRO A 1 324 ? 131.220 103.128 120.016 1.00 154.07 ? 1101 PRO A O   1 
ATOM   1549 C  CB  . PRO A 1 324 ? 132.648 105.447 118.632 1.00 154.12 ? 1101 PRO A CB  1 
ATOM   1550 C  CG  . PRO A 1 324 ? 131.912 106.648 118.142 1.00 154.51 ? 1101 PRO A CG  1 
ATOM   1551 C  CD  . PRO A 1 324 ? 131.414 106.301 116.762 1.00 154.54 ? 1101 PRO A CD  1 
ATOM   1552 N  N   . THR A 1 325 ? 129.545 103.969 118.759 1.00 144.14 ? 1102 THR A N   1 
ATOM   1553 C  CA  . THR A 1 325 ? 128.517 103.491 119.679 1.00 144.86 ? 1102 THR A CA  1 
ATOM   1554 C  C   . THR A 1 325 ? 128.482 101.969 119.729 1.00 146.17 ? 1102 THR A C   1 
ATOM   1555 O  O   . THR A 1 325 ? 128.343 101.378 120.806 1.00 145.20 ? 1102 THR A O   1 
ATOM   1556 C  CB  . THR A 1 325 ? 127.151 104.045 119.272 1.00 144.52 ? 1102 THR A CB  1 
ATOM   1557 O  OG1 . THR A 1 325 ? 127.221 105.473 119.183 1.00 144.63 ? 1102 THR A OG1 1 
ATOM   1558 C  CG2 . THR A 1 325 ? 126.094 103.660 120.295 1.00 144.18 ? 1102 THR A CG2 1 
ATOM   1559 N  N   . PHE A 1 326 ? 128.615 101.316 118.576 1.00 149.55 ? 1103 PHE A N   1 
ATOM   1560 C  CA  . PHE A 1 326 ? 128.557 99.859  118.478 1.00 149.23 ? 1103 PHE A CA  1 
ATOM   1561 C  C   . PHE A 1 326 ? 129.945 99.236  118.411 1.00 150.75 ? 1103 PHE A C   1 
ATOM   1562 O  O   . PHE A 1 326 ? 130.155 98.238  117.715 1.00 152.87 ? 1103 PHE A O   1 
ATOM   1563 C  CB  . PHE A 1 326 ? 127.723 99.445  117.270 1.00 150.10 ? 1103 PHE A CB  1 
ATOM   1564 C  CG  . PHE A 1 326 ? 126.270 99.805  117.386 1.00 149.13 ? 1103 PHE A CG  1 
ATOM   1565 C  CD1 . PHE A 1 326 ? 125.812 101.041 116.962 1.00 149.89 ? 1103 PHE A CD1 1 
ATOM   1566 C  CD2 . PHE A 1 326 ? 125.361 98.907  117.919 1.00 148.57 ? 1103 PHE A CD2 1 
ATOM   1567 C  CE1 . PHE A 1 326 ? 124.476 101.374 117.067 1.00 149.40 ? 1103 PHE A CE1 1 
ATOM   1568 C  CE2 . PHE A 1 326 ? 124.023 99.235  118.027 1.00 147.30 ? 1103 PHE A CE2 1 
ATOM   1569 C  CZ  . PHE A 1 326 ? 123.581 100.470 117.600 1.00 146.47 ? 1103 PHE A CZ  1 
ATOM   1570 N  N   . ALA A 1 327 ? 130.914 99.813  119.126 1.00 160.19 ? 1104 ALA A N   1 
ATOM   1571 C  CA  . ALA A 1 327 ? 132.265 99.260  119.125 1.00 161.48 ? 1104 ALA A CA  1 
ATOM   1572 C  C   . ALA A 1 327 ? 132.288 97.857  119.718 1.00 161.47 ? 1104 ALA A C   1 
ATOM   1573 O  O   . ALA A 1 327 ? 132.989 96.973  119.213 1.00 161.24 ? 1104 ALA A O   1 
ATOM   1574 C  CB  . ALA A 1 327 ? 133.212 100.183 119.890 1.00 160.89 ? 1104 ALA A CB  1 
ATOM   1575 N  N   . ALA A 1 328 ? 131.531 97.636  120.795 1.00 156.87 ? 1105 ALA A N   1 
ATOM   1576 C  CA  . ALA A 1 328 ? 131.464 96.304  121.388 1.00 158.03 ? 1105 ALA A CA  1 
ATOM   1577 C  C   . ALA A 1 328 ? 130.802 95.310  120.442 1.00 157.85 ? 1105 ALA A C   1 
ATOM   1578 O  O   . ALA A 1 328 ? 131.239 94.158  120.339 1.00 157.49 ? 1105 ALA A O   1 
ATOM   1579 C  CB  . ALA A 1 328 ? 130.716 96.360  122.720 1.00 158.02 ? 1105 ALA A CB  1 
ATOM   1580 N  N   . CYS A 1 329 ? 129.746 95.736  119.745 1.00 171.57 ? 1106 CYS A N   1 
ATOM   1581 C  CA  . CYS A 1 329 ? 129.071 94.844  118.808 1.00 171.23 ? 1106 CYS A CA  1 
ATOM   1582 C  C   . CYS A 1 329 ? 129.943 94.532  117.598 1.00 172.21 ? 1106 CYS A C   1 
ATOM   1583 O  O   . CYS A 1 329 ? 129.800 93.463  116.994 1.00 173.13 ? 1106 CYS A O   1 
ATOM   1584 C  CB  . CYS A 1 329 ? 127.745 95.457  118.358 1.00 173.25 ? 1106 CYS A CB  1 
ATOM   1585 S  SG  . CYS A 1 329 ? 126.599 95.848  119.699 1.00 180.18 ? 1106 CYS A SG  1 
ATOM   1586 N  N   . HIS A 1 330 ? 130.841 95.449  117.228 1.00 160.98 ? 1107 HIS A N   1 
ATOM   1587 C  CA  . HIS A 1 330 ? 131.703 95.216  116.073 1.00 159.55 ? 1107 HIS A CA  1 
ATOM   1588 C  C   . HIS A 1 330 ? 132.615 94.013  116.277 1.00 159.63 ? 1107 HIS A C   1 
ATOM   1589 O  O   . HIS A 1 330 ? 133.022 93.372  115.302 1.00 160.03 ? 1107 HIS A O   1 
ATOM   1590 C  CB  . HIS A 1 330 ? 132.540 96.462  115.779 1.00 157.47 ? 1107 HIS A CB  1 
ATOM   1591 C  CG  . HIS A 1 330 ? 131.743 97.618  115.262 1.00 158.35 ? 1107 HIS A CG  1 
ATOM   1592 N  ND1 . HIS A 1 330 ? 132.057 98.927  115.554 1.00 159.26 ? 1107 HIS A ND1 1 
ATOM   1593 C  CD2 . HIS A 1 330 ? 130.643 97.661  114.474 1.00 160.54 ? 1107 HIS A CD2 1 
ATOM   1594 C  CE1 . HIS A 1 330 ? 131.186 99.728  114.967 1.00 161.39 ? 1107 HIS A CE1 1 
ATOM   1595 N  NE2 . HIS A 1 330 ? 130.318 98.985  114.305 1.00 163.04 ? 1107 HIS A NE2 1 
ATOM   1596 N  N   . ALA A 1 331 ? 132.946 93.690  117.527 1.00 147.89 ? 1108 ALA A N   1 
ATOM   1597 C  CA  . ALA A 1 331 ? 133.848 92.582  117.811 1.00 147.65 ? 1108 ALA A CA  1 
ATOM   1598 C  C   . ALA A 1 331 ? 133.153 91.228  117.819 1.00 148.53 ? 1108 ALA A C   1 
ATOM   1599 O  O   . ALA A 1 331 ? 133.835 90.204  117.929 1.00 147.05 ? 1108 ALA A O   1 
ATOM   1600 C  CB  . ALA A 1 331 ? 134.547 92.805  119.154 1.00 147.24 ? 1108 ALA A CB  1 
ATOM   1601 N  N   . HIS A 1 332 ? 131.829 91.191  117.706 1.00 166.34 ? 1109 HIS A N   1 
ATOM   1602 C  CA  . HIS A 1 332 ? 131.084 89.939  117.743 1.00 166.64 ? 1109 HIS A CA  1 
ATOM   1603 C  C   . HIS A 1 332 ? 130.223 89.709  116.513 1.00 167.30 ? 1109 HIS A C   1 
ATOM   1604 O  O   . HIS A 1 332 ? 130.159 88.581  116.016 1.00 167.53 ? 1109 HIS A O   1 
ATOM   1605 C  CB  . HIS A 1 332 ? 130.200 89.888  118.997 1.00 167.55 ? 1109 HIS A CB  1 
ATOM   1606 C  CG  . HIS A 1 332 ? 130.971 89.899  120.279 1.00 168.92 ? 1109 HIS A CG  1 
ATOM   1607 N  ND1 . HIS A 1 332 ? 131.727 88.828  120.702 1.00 168.20 ? 1109 HIS A ND1 1 
ATOM   1608 C  CD2 . HIS A 1 332 ? 131.103 90.852  121.232 1.00 169.75 ? 1109 HIS A CD2 1 
ATOM   1609 C  CE1 . HIS A 1 332 ? 132.291 89.119  121.861 1.00 168.01 ? 1109 HIS A CE1 1 
ATOM   1610 N  NE2 . HIS A 1 332 ? 131.929 90.342  122.204 1.00 168.97 ? 1109 HIS A NE2 1 
ATOM   1611 N  N   . VAL A 1 333 ? 129.557 90.743  116.005 1.00 168.93 ? 1110 VAL A N   1 
ATOM   1612 C  CA  . VAL A 1 333 ? 128.658 90.625  114.864 1.00 169.53 ? 1110 VAL A CA  1 
ATOM   1613 C  C   . VAL A 1 333 ? 129.135 91.573  113.773 1.00 170.52 ? 1110 VAL A C   1 
ATOM   1614 O  O   . VAL A 1 333 ? 129.354 92.762  114.030 1.00 172.70 ? 1110 VAL A O   1 
ATOM   1615 C  CB  . VAL A 1 333 ? 127.201 90.931  115.255 1.00 167.14 ? 1110 VAL A CB  1 
ATOM   1616 C  CG1 . VAL A 1 333 ? 126.303 90.896  114.029 1.00 167.60 ? 1110 VAL A CG1 1 
ATOM   1617 C  CG2 . VAL A 1 333 ? 126.716 89.946  116.307 1.00 166.93 ? 1110 VAL A CG2 1 
ATOM   1618 N  N   . GLU A 1 334 ? 129.294 91.048  112.566 1.00 165.30 ? 1111 GLU A N   1 
ATOM   1619 C  CA  . GLU A 1 334 ? 129.708 91.868  111.434 1.00 163.45 ? 1111 GLU A CA  1 
ATOM   1620 C  C   . GLU A 1 334 ? 128.571 92.798  111.029 1.00 163.96 ? 1111 GLU A C   1 
ATOM   1621 O  O   . GLU A 1 334 ? 127.462 92.321  110.757 1.00 166.16 ? 1111 GLU A O   1 
ATOM   1622 C  CB  . GLU A 1 334 ? 130.118 90.985  110.260 1.00 164.67 ? 1111 GLU A CB  1 
ATOM   1623 C  CG  . GLU A 1 334 ? 131.454 90.286  110.446 1.00 165.85 ? 1111 GLU A CG  1 
ATOM   1624 C  CD  . GLU A 1 334 ? 132.635 91.214  110.233 1.00 168.96 ? 1111 GLU A CD  1 
ATOM   1625 O  OE1 . GLU A 1 334 ? 132.431 92.329  109.709 1.00 168.40 ? 1111 GLU A OE1 1 
ATOM   1626 O  OE2 . GLU A 1 334 ? 133.767 90.827  110.591 1.00 170.59 ? 1111 GLU A OE2 1 
ATOM   1627 N  N   . PRO A 1 335 ? 128.790 94.110  110.974 1.00 153.97 ? 1112 PRO A N   1 
ATOM   1628 C  CA  . PRO A 1 335 ? 127.709 95.047  110.641 1.00 156.56 ? 1112 PRO A CA  1 
ATOM   1629 C  C   . PRO A 1 335 ? 127.589 95.402  109.166 1.00 157.10 ? 1112 PRO A C   1 
ATOM   1630 O  O   . PRO A 1 335 ? 126.786 96.279  108.833 1.00 157.81 ? 1112 PRO A O   1 
ATOM   1631 C  CB  . PRO A 1 335 ? 128.103 96.287  111.453 1.00 156.63 ? 1112 PRO A CB  1 
ATOM   1632 C  CG  . PRO A 1 335 ? 129.607 96.252  111.470 1.00 155.97 ? 1112 PRO A CG  1 
ATOM   1633 C  CD  . PRO A 1 335 ? 130.043 94.810  111.305 1.00 153.97 ? 1112 PRO A CD  1 
ATOM   1634 N  N   . ALA A 1 336 ? 128.356 94.761  108.281 1.00 154.05 ? 1113 ALA A N   1 
ATOM   1635 C  CA  . ALA A 1 336 ? 128.294 95.101  106.863 1.00 154.08 ? 1113 ALA A CA  1 
ATOM   1636 C  C   . ALA A 1 336 ? 126.928 94.770  106.275 1.00 154.03 ? 1113 ALA A C   1 
ATOM   1637 O  O   . ALA A 1 336 ? 126.331 95.585  105.560 1.00 156.58 ? 1113 ALA A O   1 
ATOM   1638 C  CB  . ALA A 1 336 ? 129.401 94.372  106.101 1.00 154.22 ? 1113 ALA A CB  1 
ATOM   1639 N  N   . ARG A 1 337 ? 126.416 93.573  106.569 1.00 154.01 ? 1114 ARG A N   1 
ATOM   1640 C  CA  . ARG A 1 337 ? 125.104 93.185  106.061 1.00 156.63 ? 1114 ARG A CA  1 
ATOM   1641 C  C   . ARG A 1 337 ? 124.011 94.090  106.613 1.00 157.12 ? 1114 ARG A C   1 
ATOM   1642 O  O   . ARG A 1 337 ? 123.112 94.513  105.876 1.00 159.49 ? 1114 ARG A O   1 
ATOM   1643 C  CB  . ARG A 1 337 ? 124.818 91.724  106.408 1.00 155.56 ? 1114 ARG A CB  1 
ATOM   1644 C  CG  . ARG A 1 337 ? 123.438 91.245  105.990 1.00 157.26 ? 1114 ARG A CG  1 
ATOM   1645 C  CD  . ARG A 1 337 ? 123.253 89.766  106.287 1.00 157.70 ? 1114 ARG A CD  1 
ATOM   1646 N  NE  . ARG A 1 337 ? 123.099 89.509  107.714 1.00 159.77 ? 1114 ARG A NE  1 
ATOM   1647 C  CZ  . ARG A 1 337 ? 124.033 88.966  108.483 1.00 159.03 ? 1114 ARG A CZ  1 
ATOM   1648 N  NH1 . ARG A 1 337 ? 125.209 88.608  107.994 1.00 158.50 ? 1114 ARG A NH1 1 
ATOM   1649 N  NH2 . ARG A 1 337 ? 123.780 88.777  109.775 1.00 156.97 ? 1114 ARG A NH2 1 
ATOM   1650 N  N   . TYR A 1 338 ? 124.077 94.407  107.907 1.00 143.31 ? 1115 TYR A N   1 
ATOM   1651 C  CA  . TYR A 1 338 ? 123.073 95.281  108.504 1.00 143.61 ? 1115 TYR A CA  1 
ATOM   1652 C  C   . TYR A 1 338 ? 123.179 96.700  107.959 1.00 144.66 ? 1115 TYR A C   1 
ATOM   1653 O  O   . TYR A 1 338 ? 122.161 97.374  107.771 1.00 144.82 ? 1115 TYR A O   1 
ATOM   1654 C  CB  . TYR A 1 338 ? 123.206 95.269  110.025 1.00 143.26 ? 1115 TYR A CB  1 
ATOM   1655 C  CG  . TYR A 1 338 ? 122.931 93.917  110.646 1.00 145.68 ? 1115 TYR A CG  1 
ATOM   1656 C  CD1 . TYR A 1 338 ? 123.928 92.954  110.731 1.00 146.91 ? 1115 TYR A CD1 1 
ATOM   1657 C  CD2 . TYR A 1 338 ? 121.674 93.603  111.144 1.00 145.76 ? 1115 TYR A CD2 1 
ATOM   1658 C  CE1 . TYR A 1 338 ? 123.681 91.717  111.296 1.00 146.06 ? 1115 TYR A CE1 1 
ATOM   1659 C  CE2 . TYR A 1 338 ? 121.418 92.369  111.711 1.00 144.45 ? 1115 TYR A CE2 1 
ATOM   1660 C  CZ  . TYR A 1 338 ? 122.425 91.431  111.784 1.00 144.06 ? 1115 TYR A CZ  1 
ATOM   1661 O  OH  . TYR A 1 338 ? 122.174 90.201  112.348 1.00 143.15 ? 1115 TYR A OH  1 
ATOM   1662 N  N   . TYR A 1 339 ? 124.401 97.170  107.693 1.00 150.77 ? 1116 TYR A N   1 
ATOM   1663 C  CA  . TYR A 1 339 ? 124.565 98.490  107.091 1.00 151.38 ? 1116 TYR A CA  1 
ATOM   1664 C  C   . TYR A 1 339 ? 123.974 98.531  105.687 1.00 152.86 ? 1116 TYR A C   1 
ATOM   1665 O  O   . TYR A 1 339 ? 123.299 99.500  105.314 1.00 155.17 ? 1116 TYR A O   1 
ATOM   1666 C  CB  . TYR A 1 339 ? 126.044 98.873  107.064 1.00 151.12 ? 1116 TYR A CB  1 
ATOM   1667 C  CG  . TYR A 1 339 ? 126.325 100.204 106.407 1.00 151.80 ? 1116 TYR A CG  1 
ATOM   1668 C  CD1 . TYR A 1 339 ? 125.998 101.395 107.040 1.00 152.15 ? 1116 TYR A CD1 1 
ATOM   1669 C  CD2 . TYR A 1 339 ? 126.920 100.270 105.155 1.00 152.79 ? 1116 TYR A CD2 1 
ATOM   1670 C  CE1 . TYR A 1 339 ? 126.253 102.615 106.445 1.00 152.07 ? 1116 TYR A CE1 1 
ATOM   1671 C  CE2 . TYR A 1 339 ? 127.179 101.485 104.551 1.00 154.08 ? 1116 TYR A CE2 1 
ATOM   1672 C  CZ  . TYR A 1 339 ? 126.844 102.654 105.200 1.00 154.26 ? 1116 TYR A CZ  1 
ATOM   1673 O  OH  . TYR A 1 339 ? 127.101 103.866 104.603 1.00 155.99 ? 1116 TYR A OH  1 
ATOM   1674 N  N   . GLU A 1 340 ? 124.217 97.484  104.893 1.00 160.38 ? 1117 GLU A N   1 
ATOM   1675 C  CA  . GLU A 1 340 ? 123.630 97.419  103.559 1.00 159.62 ? 1117 GLU A CA  1 
ATOM   1676 C  C   . GLU A 1 340 ? 122.110 97.363  103.632 1.00 160.08 ? 1117 GLU A C   1 
ATOM   1677 O  O   . GLU A 1 340 ? 121.418 97.991  102.821 1.00 162.85 ? 1117 GLU A O   1 
ATOM   1678 C  CB  . GLU A 1 340 ? 124.177 96.209  102.803 1.00 159.85 ? 1117 GLU A CB  1 
ATOM   1679 C  CG  . GLU A 1 340 ? 125.280 96.543  101.814 1.00 162.22 ? 1117 GLU A CG  1 
ATOM   1680 C  CD  . GLU A 1 340 ? 125.565 95.405  100.855 1.00 164.76 ? 1117 GLU A CD  1 
ATOM   1681 O  OE1 . GLU A 1 340 ? 124.654 94.585  100.615 1.00 165.96 ? 1117 GLU A OE1 1 
ATOM   1682 O  OE2 . GLU A 1 340 ? 126.701 95.329  100.341 1.00 165.04 ? 1117 GLU A OE2 1 
ATOM   1683 N  N   . ALA A 1 341 ? 121.573 96.613  104.598 1.00 147.24 ? 1118 ALA A N   1 
ATOM   1684 C  CA  . ALA A 1 341 ? 120.126 96.554  104.771 1.00 147.78 ? 1118 ALA A CA  1 
ATOM   1685 C  C   . ALA A 1 341 ? 119.559 97.917  105.147 1.00 147.42 ? 1118 ALA A C   1 
ATOM   1686 O  O   . ALA A 1 341 ? 118.506 98.319  104.642 1.00 149.55 ? 1118 ALA A O   1 
ATOM   1687 C  CB  . ALA A 1 341 ? 119.766 95.511  105.828 1.00 148.09 ? 1118 ALA A CB  1 
ATOM   1688 N  N   . CYS A 1 342 ? 120.246 98.641  106.035 1.00 146.62 ? 1119 CYS A N   1 
ATOM   1689 C  CA  . CYS A 1 342 ? 119.810 99.986  106.399 1.00 146.49 ? 1119 CYS A CA  1 
ATOM   1690 C  C   . CYS A 1 342 ? 119.803 100.905 105.187 1.00 148.25 ? 1119 CYS A C   1 
ATOM   1691 O  O   . CYS A 1 342 ? 118.845 101.660 104.974 1.00 149.33 ? 1119 CYS A O   1 
ATOM   1692 C  CB  . CYS A 1 342 ? 120.717 100.553 107.491 1.00 149.63 ? 1119 CYS A CB  1 
ATOM   1693 S  SG  . CYS A 1 342 ? 120.197 102.150 108.178 1.00 155.91 ? 1119 CYS A SG  1 
ATOM   1694 N  N   . VAL A 1 343 ? 120.865 100.855 104.380 1.00 140.30 ? 1120 VAL A N   1 
ATOM   1695 C  CA  . VAL A 1 343 ? 120.949 101.717 103.203 1.00 137.90 ? 1120 VAL A CA  1 
ATOM   1696 C  C   . VAL A 1 343 ? 119.828 101.389 102.224 1.00 140.04 ? 1120 VAL A C   1 
ATOM   1697 O  O   . VAL A 1 343 ? 119.154 102.285 101.699 1.00 138.40 ? 1120 VAL A O   1 
ATOM   1698 C  CB  . VAL A 1 343 ? 122.334 101.589 102.544 1.00 136.04 ? 1120 VAL A CB  1 
ATOM   1699 C  CG1 . VAL A 1 343 ? 122.333 102.237 101.171 1.00 137.32 ? 1120 VAL A CG1 1 
ATOM   1700 C  CG2 . VAL A 1 343 ? 123.400 102.212 103.430 1.00 135.97 ? 1120 VAL A CG2 1 
ATOM   1701 N  N   . ASN A 1 344 ? 119.602 100.096 101.975 1.00 152.43 ? 1121 ASN A N   1 
ATOM   1702 C  CA  . ASN A 1 344 ? 118.560 99.694  101.035 1.00 149.57 ? 1121 ASN A CA  1 
ATOM   1703 C  C   . ASN A 1 344 ? 117.176 100.090 101.536 1.00 150.76 ? 1121 ASN A C   1 
ATOM   1704 O  O   . ASN A 1 344 ? 116.341 100.567 100.759 1.00 152.57 ? 1121 ASN A O   1 
ATOM   1705 C  CB  . ASN A 1 344 ? 118.630 98.188  100.788 1.00 150.19 ? 1121 ASN A CB  1 
ATOM   1706 C  CG  . ASN A 1 344 ? 119.620 97.822  99.701  1.00 152.25 ? 1121 ASN A CG  1 
ATOM   1707 O  OD1 . ASN A 1 344 ? 120.470 98.628  99.323  1.00 151.14 ? 1121 ASN A OD1 1 
ATOM   1708 N  ND2 . ASN A 1 344 ? 119.517 96.600  99.193  1.00 152.83 ? 1121 ASN A ND2 1 
ATOM   1709 N  N   . ASP A 1 345 ? 116.915 99.902  102.832 1.00 166.96 ? 1122 ASP A N   1 
ATOM   1710 C  CA  . ASP A 1 345 ? 115.616 100.270 103.384 1.00 167.65 ? 1122 ASP A CA  1 
ATOM   1711 C  C   . ASP A 1 345 ? 115.392 101.774 103.313 1.00 167.29 ? 1122 ASP A C   1 
ATOM   1712 O  O   . ASP A 1 345 ? 114.299 102.226 102.953 1.00 169.00 ? 1122 ASP A O   1 
ATOM   1713 C  CB  . ASP A 1 345 ? 115.500 99.776  104.825 1.00 167.89 ? 1122 ASP A CB  1 
ATOM   1714 C  CG  . ASP A 1 345 ? 115.147 98.305  104.909 1.00 169.02 ? 1122 ASP A CG  1 
ATOM   1715 O  OD1 . ASP A 1 345 ? 115.631 97.527  104.061 1.00 168.12 ? 1122 ASP A OD1 1 
ATOM   1716 O  OD2 . ASP A 1 345 ? 114.385 97.926  105.824 1.00 170.44 ? 1122 ASP A OD2 1 
ATOM   1717 N  N   . ALA A 1 346 ? 116.414 102.567 103.645 1.00 149.10 ? 1123 ALA A N   1 
ATOM   1718 C  CA  . ALA A 1 346 ? 116.269 104.016 103.565 1.00 147.22 ? 1123 ALA A CA  1 
ATOM   1719 C  C   . ALA A 1 346 ? 116.089 104.482 102.126 1.00 148.39 ? 1123 ALA A C   1 
ATOM   1720 O  O   . ALA A 1 346 ? 115.379 105.465 101.881 1.00 149.40 ? 1123 ALA A O   1 
ATOM   1721 C  CB  . ALA A 1 346 ? 117.475 104.701 104.204 1.00 148.36 ? 1123 ALA A CB  1 
ATOM   1722 N  N   . CYS A 1 347 ? 116.716 103.798 101.166 1.00 157.48 ? 1124 CYS A N   1 
ATOM   1723 C  CA  . CYS A 1 347 ? 116.513 104.152 99.766  1.00 156.97 ? 1124 CYS A CA  1 
ATOM   1724 C  C   . CYS A 1 347 ? 115.129 103.743 99.275  1.00 156.81 ? 1124 CYS A C   1 
ATOM   1725 O  O   . CYS A 1 347 ? 114.569 104.399 98.390  1.00 154.29 ? 1124 CYS A O   1 
ATOM   1726 C  CB  . CYS A 1 347 ? 117.594 103.509 98.897  1.00 160.42 ? 1124 CYS A CB  1 
ATOM   1727 S  SG  . CYS A 1 347 ? 119.093 104.503 98.694  1.00 169.23 ? 1124 CYS A SG  1 
ATOM   1728 N  N   . ALA A 1 348 ? 114.563 102.671 99.831  1.00 161.16 ? 1125 ALA A N   1 
ATOM   1729 C  CA  . ALA A 1 348 ? 113.278 102.164 99.366  1.00 160.40 ? 1125 ALA A CA  1 
ATOM   1730 C  C   . ALA A 1 348 ? 112.093 102.734 100.132 1.00 161.74 ? 1125 ALA A C   1 
ATOM   1731 O  O   . ALA A 1 348 ? 111.016 102.905 99.548  1.00 162.65 ? 1125 ALA A O   1 
ATOM   1732 C  CB  . ALA A 1 348 ? 113.250 100.636 99.457  1.00 161.41 ? 1125 ALA A CB  1 
ATOM   1733 N  N   . CYS A 1 349 ? 112.259 103.034 101.419 1.00 183.58 ? 1126 CYS A N   1 
ATOM   1734 C  CA  . CYS A 1 349 ? 111.156 103.533 102.234 1.00 183.54 ? 1126 CYS A CA  1 
ATOM   1735 C  C   . CYS A 1 349 ? 110.837 104.979 101.875 1.00 181.80 ? 1126 CYS A C   1 
ATOM   1736 O  O   . CYS A 1 349 ? 111.094 105.892 102.665 1.00 183.98 ? 1126 CYS A O   1 
ATOM   1737 C  CB  . CYS A 1 349 ? 111.497 103.408 103.723 1.00 185.19 ? 1126 CYS A CB  1 
ATOM   1738 S  SG  . CYS A 1 349 ? 110.100 103.581 104.858 1.00 189.07 ? 1126 CYS A SG  1 
ATOM   1739 N  N   . ASP A 1 350 ? 110.274 105.195 100.686 1.00 153.67 ? 1127 ASP A N   1 
ATOM   1740 C  CA  . ASP A 1 350 ? 109.982 106.532 100.185 1.00 154.50 ? 1127 ASP A CA  1 
ATOM   1741 C  C   . ASP A 1 350 ? 108.489 106.807 100.059 1.00 153.68 ? 1127 ASP A C   1 
ATOM   1742 O  O   . ASP A 1 350 ? 108.103 107.812 99.454  1.00 153.24 ? 1127 ASP A O   1 
ATOM   1743 C  CB  . ASP A 1 350 ? 110.670 106.751 98.835  1.00 155.89 ? 1127 ASP A CB  1 
ATOM   1744 C  CG  . ASP A 1 350 ? 110.447 105.600 97.869  1.00 156.43 ? 1127 ASP A CG  1 
ATOM   1745 O  OD1 . ASP A 1 350 ? 109.411 104.911 97.982  1.00 155.16 ? 1127 ASP A OD1 1 
ATOM   1746 O  OD2 . ASP A 1 350 ? 111.311 105.384 96.994  1.00 158.04 ? 1127 ASP A OD2 1 
ATOM   1747 N  N   . SER A 1 351 ? 107.641 105.942 100.608 1.00 148.30 ? 1128 SER A N   1 
ATOM   1748 C  CA  . SER A 1 351 ? 106.198 106.125 100.541 1.00 148.76 ? 1128 SER A CA  1 
ATOM   1749 C  C   . SER A 1 351 ? 105.653 106.962 101.689 1.00 149.11 ? 1128 SER A C   1 
ATOM   1750 O  O   . SER A 1 351 ? 104.436 107.153 101.774 1.00 147.45 ? 1128 SER A O   1 
ATOM   1751 C  CB  . SER A 1 351 ? 105.494 104.765 100.518 1.00 150.98 ? 1128 SER A CB  1 
ATOM   1752 O  OG  . SER A 1 351 ? 104.202 104.871 99.945  1.00 150.67 ? 1128 SER A OG  1 
ATOM   1753 N  N   . GLY A 1 352 ? 106.516 107.463 102.568 1.00 151.35 ? 1129 GLY A N   1 
ATOM   1754 C  CA  . GLY A 1 352 ? 106.071 108.249 103.701 1.00 149.81 ? 1129 GLY A CA  1 
ATOM   1755 C  C   . GLY A 1 352 ? 106.320 107.555 105.023 1.00 150.12 ? 1129 GLY A C   1 
ATOM   1756 O  O   . GLY A 1 352 ? 105.668 106.555 105.339 1.00 150.39 ? 1129 GLY A O   1 
ATOM   1757 N  N   . GLY A 1 353 ? 107.260 108.077 105.806 1.00 174.50 ? 1130 GLY A N   1 
ATOM   1758 C  CA  . GLY A 1 353 ? 107.590 107.476 107.083 1.00 176.33 ? 1130 GLY A CA  1 
ATOM   1759 C  C   . GLY A 1 353 ? 108.901 106.718 107.068 1.00 176.95 ? 1130 GLY A C   1 
ATOM   1760 O  O   . GLY A 1 353 ? 109.001 105.628 107.639 1.00 177.95 ? 1130 GLY A O   1 
ATOM   1761 N  N   . ASP A 1 354 ? 109.916 107.285 106.410 1.00 179.88 ? 1131 ASP A N   1 
ATOM   1762 C  CA  . ASP A 1 354 ? 111.227 106.649 106.371 1.00 180.14 ? 1131 ASP A CA  1 
ATOM   1763 C  C   . ASP A 1 354 ? 111.873 106.573 107.748 1.00 180.19 ? 1131 ASP A C   1 
ATOM   1764 O  O   . ASP A 1 354 ? 112.760 105.737 107.961 1.00 179.68 ? 1131 ASP A O   1 
ATOM   1765 C  CB  . ASP A 1 354 ? 112.145 107.398 105.404 1.00 180.68 ? 1131 ASP A CB  1 
ATOM   1766 C  CG  . ASP A 1 354 ? 112.120 108.898 105.622 1.00 181.47 ? 1131 ASP A CG  1 
ATOM   1767 O  OD1 . ASP A 1 354 ? 111.420 109.355 106.550 1.00 181.35 ? 1131 ASP A OD1 1 
ATOM   1768 O  OD2 . ASP A 1 354 ? 112.801 109.621 104.865 1.00 180.58 ? 1131 ASP A OD2 1 
ATOM   1769 N  N   . CYS A 1 355 ? 111.449 107.425 108.684 1.00 178.65 ? 1132 CYS A N   1 
ATOM   1770 C  CA  . CYS A 1 355 ? 111.995 107.372 110.036 1.00 178.05 ? 1132 CYS A CA  1 
ATOM   1771 C  C   . CYS A 1 355 ? 111.687 106.038 110.700 1.00 177.74 ? 1132 CYS A C   1 
ATOM   1772 O  O   . CYS A 1 355 ? 112.547 105.459 111.373 1.00 179.01 ? 1132 CYS A O   1 
ATOM   1773 C  CB  . CYS A 1 355 ? 111.445 108.528 110.870 1.00 178.04 ? 1132 CYS A CB  1 
ATOM   1774 S  SG  . CYS A 1 355 ? 111.885 108.458 112.621 1.00 182.54 ? 1132 CYS A SG  1 
ATOM   1775 N  N   . GLU A 1 356 ? 110.464 105.531 110.520 1.00 180.24 ? 1133 GLU A N   1 
ATOM   1776 C  CA  . GLU A 1 356 ? 110.111 104.235 111.091 1.00 181.60 ? 1133 GLU A CA  1 
ATOM   1777 C  C   . GLU A 1 356 ? 110.937 103.116 110.470 1.00 181.78 ? 1133 GLU A C   1 
ATOM   1778 O  O   . GLU A 1 356 ? 111.389 102.204 111.174 1.00 183.99 ? 1133 GLU A O   1 
ATOM   1779 C  CB  . GLU A 1 356 ? 108.618 103.969 110.903 1.00 182.82 ? 1133 GLU A CB  1 
ATOM   1780 C  CG  . GLU A 1 356 ? 107.718 105.028 111.514 1.00 183.59 ? 1133 GLU A CG  1 
ATOM   1781 C  CD  . GLU A 1 356 ? 106.248 104.677 111.402 1.00 185.70 ? 1133 GLU A CD  1 
ATOM   1782 O  OE1 . GLU A 1 356 ? 105.933 103.599 110.856 1.00 186.81 ? 1133 GLU A OE1 1 
ATOM   1783 O  OE2 . GLU A 1 356 ? 105.407 105.479 111.860 1.00 185.37 ? 1133 GLU A OE2 1 
ATOM   1784 N  N   . CYS A 1 357 ? 111.144 103.166 109.152 1.00 173.34 ? 1134 CYS A N   1 
ATOM   1785 C  CA  . CYS A 1 357 ? 111.963 102.155 108.491 1.00 172.91 ? 1134 CYS A CA  1 
ATOM   1786 C  C   . CYS A 1 357 ? 113.392 102.174 109.020 1.00 172.17 ? 1134 CYS A C   1 
ATOM   1787 O  O   . CYS A 1 357 ? 113.971 101.118 109.307 1.00 173.17 ? 1134 CYS A O   1 
ATOM   1788 C  CB  . CYS A 1 357 ? 111.943 102.374 106.977 1.00 173.73 ? 1134 CYS A CB  1 
ATOM   1789 S  SG  . CYS A 1 357 ? 110.337 102.064 106.192 1.00 184.04 ? 1134 CYS A SG  1 
ATOM   1790 N  N   . PHE A 1 358 ? 113.971 103.368 109.170 1.00 146.68 ? 1135 PHE A N   1 
ATOM   1791 C  CA  . PHE A 1 358 ? 115.329 103.473 109.695 1.00 146.07 ? 1135 PHE A CA  1 
ATOM   1792 C  C   . PHE A 1 358 ? 115.405 102.980 111.135 1.00 148.58 ? 1135 PHE A C   1 
ATOM   1793 O  O   . PHE A 1 358 ? 116.361 102.290 111.516 1.00 150.44 ? 1135 PHE A O   1 
ATOM   1794 C  CB  . PHE A 1 358 ? 115.813 104.920 109.589 1.00 144.10 ? 1135 PHE A CB  1 
ATOM   1795 C  CG  . PHE A 1 358 ? 117.047 105.209 110.392 1.00 144.29 ? 1135 PHE A CG  1 
ATOM   1796 C  CD1 . PHE A 1 358 ? 118.290 104.793 109.947 1.00 144.66 ? 1135 PHE A CD1 1 
ATOM   1797 C  CD2 . PHE A 1 358 ? 116.967 105.906 111.586 1.00 146.01 ? 1135 PHE A CD2 1 
ATOM   1798 C  CE1 . PHE A 1 358 ? 119.429 105.061 110.681 1.00 146.83 ? 1135 PHE A CE1 1 
ATOM   1799 C  CE2 . PHE A 1 358 ? 118.102 106.176 112.324 1.00 146.45 ? 1135 PHE A CE2 1 
ATOM   1800 C  CZ  . PHE A 1 358 ? 119.335 105.753 111.871 1.00 147.18 ? 1135 PHE A CZ  1 
ATOM   1801 N  N   . CYS A 1 359 ? 114.405 103.325 111.952 1.00 170.65 ? 1136 CYS A N   1 
ATOM   1802 C  CA  . CYS A 1 359 ? 114.396 102.878 113.341 1.00 170.28 ? 1136 CYS A CA  1 
ATOM   1803 C  C   . CYS A 1 359 ? 114.310 101.361 113.431 1.00 169.34 ? 1136 CYS A C   1 
ATOM   1804 O  O   . CYS A 1 359 ? 115.007 100.743 114.241 1.00 170.72 ? 1136 CYS A O   1 
ATOM   1805 C  CB  . CYS A 1 359 ? 113.235 103.527 114.096 1.00 172.19 ? 1136 CYS A CB  1 
ATOM   1806 S  SG  . CYS A 1 359 ? 113.443 105.293 114.436 1.00 182.19 ? 1136 CYS A SG  1 
ATOM   1807 N  N   . THR A 1 360 ? 113.463 100.741 112.605 1.00 155.67 ? 1137 THR A N   1 
ATOM   1808 C  CA  . THR A 1 360 ? 113.373 99.284  112.603 1.00 155.12 ? 1137 THR A CA  1 
ATOM   1809 C  C   . THR A 1 360 ? 114.674 98.649  112.128 1.00 154.17 ? 1137 THR A C   1 
ATOM   1810 O  O   . THR A 1 360 ? 115.120 97.637  112.686 1.00 155.20 ? 1137 THR A O   1 
ATOM   1811 C  CB  . THR A 1 360 ? 112.206 98.824  111.730 1.00 155.27 ? 1137 THR A CB  1 
ATOM   1812 O  OG1 . THR A 1 360 ? 112.331 99.392  110.421 1.00 157.55 ? 1137 THR A OG1 1 
ATOM   1813 C  CG2 . THR A 1 360 ? 110.880 99.247  112.344 1.00 156.18 ? 1137 THR A CG2 1 
ATOM   1814 N  N   . ALA A 1 361 ? 115.300 99.231  111.101 1.00 144.55 ? 1138 ALA A N   1 
ATOM   1815 C  CA  . ALA A 1 361 ? 116.562 98.691  110.606 1.00 143.85 ? 1138 ALA A CA  1 
ATOM   1816 C  C   . ALA A 1 361 ? 117.643 98.743  111.678 1.00 144.67 ? 1138 ALA A C   1 
ATOM   1817 O  O   . ALA A 1 361 ? 118.431 97.801  111.822 1.00 144.95 ? 1138 ALA A O   1 
ATOM   1818 C  CB  . ALA A 1 361 ? 117.005 99.452  109.357 1.00 146.42 ? 1138 ALA A CB  1 
ATOM   1819 N  N   . VAL A 1 362 ? 117.698 99.837  112.440 1.00 140.26 ? 1139 VAL A N   1 
ATOM   1820 C  CA  . VAL A 1 362 ? 118.690 99.937  113.507 1.00 138.17 ? 1139 VAL A CA  1 
ATOM   1821 C  C   . VAL A 1 362 ? 118.348 98.989  114.652 1.00 139.49 ? 1139 VAL A C   1 
ATOM   1822 O  O   . VAL A 1 362 ? 119.232 98.337  115.224 1.00 139.92 ? 1139 VAL A O   1 
ATOM   1823 C  CB  . VAL A 1 362 ? 118.809 101.394 113.991 1.00 138.56 ? 1139 VAL A CB  1 
ATOM   1824 C  CG1 . VAL A 1 362 ? 119.708 101.476 115.212 1.00 140.09 ? 1139 VAL A CG1 1 
ATOM   1825 C  CG2 . VAL A 1 362 ? 119.344 102.274 112.877 1.00 137.00 ? 1139 VAL A CG2 1 
ATOM   1826 N  N   . ALA A 1 363 ? 117.062 98.891  115.002 1.00 138.78 ? 1140 ALA A N   1 
ATOM   1827 C  CA  . ALA A 1 363 ? 116.653 98.038  116.112 1.00 136.51 ? 1140 ALA A CA  1 
ATOM   1828 C  C   . ALA A 1 363 ? 116.893 96.567  115.812 1.00 138.09 ? 1140 ALA A C   1 
ATOM   1829 O  O   . ALA A 1 363 ? 117.101 95.778  116.739 1.00 140.60 ? 1140 ALA A O   1 
ATOM   1830 C  CB  . ALA A 1 363 ? 115.181 98.279  116.445 1.00 138.42 ? 1140 ALA A CB  1 
ATOM   1831 N  N   . ALA A 1 364 ? 116.867 96.178  114.536 1.00 144.00 ? 1141 ALA A N   1 
ATOM   1832 C  CA  . ALA A 1 364 ? 117.200 94.800  114.186 1.00 144.35 ? 1141 ALA A CA  1 
ATOM   1833 C  C   . ALA A 1 364 ? 118.614 94.450  114.637 1.00 144.14 ? 1141 ALA A C   1 
ATOM   1834 O  O   . ALA A 1 364 ? 118.828 93.454  115.341 1.00 146.85 ? 1141 ALA A O   1 
ATOM   1835 C  CB  . ALA A 1 364 ? 117.043 94.589  112.681 1.00 146.56 ? 1141 ALA A CB  1 
ATOM   1836 N  N   . TYR A 1 365 ? 119.593 95.273  114.255 1.00 146.71 ? 1142 TYR A N   1 
ATOM   1837 C  CA  . TYR A 1 365 ? 120.968 95.037  114.684 1.00 148.50 ? 1142 TYR A CA  1 
ATOM   1838 C  C   . TYR A 1 365 ? 121.125 95.215  116.187 1.00 148.10 ? 1142 TYR A C   1 
ATOM   1839 O  O   . TYR A 1 365 ? 121.938 94.521  116.809 1.00 148.38 ? 1142 TYR A O   1 
ATOM   1840 C  CB  . TYR A 1 365 ? 121.920 95.970  113.937 1.00 151.35 ? 1142 TYR A CB  1 
ATOM   1841 C  CG  . TYR A 1 365 ? 123.380 95.747  114.264 1.00 151.40 ? 1142 TYR A CG  1 
ATOM   1842 C  CD1 . TYR A 1 365 ? 124.092 94.712  113.676 1.00 152.09 ? 1142 TYR A CD1 1 
ATOM   1843 C  CD2 . TYR A 1 365 ? 124.046 96.576  115.157 1.00 149.72 ? 1142 TYR A CD2 1 
ATOM   1844 C  CE1 . TYR A 1 365 ? 125.424 94.504  113.969 1.00 150.62 ? 1142 TYR A CE1 1 
ATOM   1845 C  CE2 . TYR A 1 365 ? 125.380 96.376  115.456 1.00 149.72 ? 1142 TYR A CE2 1 
ATOM   1846 C  CZ  . TYR A 1 365 ? 126.064 95.338  114.859 1.00 149.96 ? 1142 TYR A CZ  1 
ATOM   1847 O  OH  . TYR A 1 365 ? 127.392 95.133  115.151 1.00 152.75 ? 1142 TYR A OH  1 
ATOM   1848 N  N   . ALA A 1 366 ? 120.362 96.132  116.786 1.00 153.73 ? 1143 ALA A N   1 
ATOM   1849 C  CA  . ALA A 1 366 ? 120.420 96.306  118.234 1.00 155.55 ? 1143 ALA A CA  1 
ATOM   1850 C  C   . ALA A 1 366 ? 120.006 95.029  118.954 1.00 155.31 ? 1143 ALA A C   1 
ATOM   1851 O  O   . ALA A 1 366 ? 120.684 94.576  119.883 1.00 157.15 ? 1143 ALA A O   1 
ATOM   1852 C  CB  . ALA A 1 366 ? 119.534 97.478  118.657 1.00 157.13 ? 1143 ALA A CB  1 
ATOM   1853 N  N   . GLN A 1 367 ? 118.896 94.424  118.525 1.00 162.06 ? 1144 GLN A N   1 
ATOM   1854 C  CA  . GLN A 1 367 ? 118.446 93.175  119.131 1.00 161.49 ? 1144 GLN A CA  1 
ATOM   1855 C  C   . GLN A 1 367 ? 119.410 92.037  118.825 1.00 161.88 ? 1144 GLN A C   1 
ATOM   1856 O  O   . GLN A 1 367 ? 119.634 91.162  119.670 1.00 163.96 ? 1144 GLN A O   1 
ATOM   1857 C  CB  . GLN A 1 367 ? 117.036 92.837  118.645 1.00 161.74 ? 1144 GLN A CB  1 
ATOM   1858 C  CG  . GLN A 1 367 ? 116.234 91.961  119.597 1.00 162.46 ? 1144 GLN A CG  1 
ATOM   1859 C  CD  . GLN A 1 367 ? 116.635 90.501  119.533 1.00 165.01 ? 1144 GLN A CD  1 
ATOM   1860 O  OE1 . GLN A 1 367 ? 117.099 90.017  118.501 1.00 165.29 ? 1144 GLN A OE1 1 
ATOM   1861 N  NE2 . GLN A 1 367 ? 116.458 89.790  120.640 1.00 166.53 ? 1144 GLN A NE2 1 
ATOM   1862 N  N   . ALA A 1 368 ? 119.991 92.030  117.621 1.00 154.64 ? 1145 ALA A N   1 
ATOM   1863 C  CA  . ALA A 1 368 ? 120.969 91.001  117.283 1.00 154.82 ? 1145 ALA A CA  1 
ATOM   1864 C  C   . ALA A 1 368 ? 122.178 91.067  118.207 1.00 156.12 ? 1145 ALA A C   1 
ATOM   1865 O  O   . ALA A 1 368 ? 122.689 90.031  118.649 1.00 156.58 ? 1145 ALA A O   1 
ATOM   1866 C  CB  . ALA A 1 368 ? 121.398 91.143  115.824 1.00 156.42 ? 1145 ALA A CB  1 
ATOM   1867 N  N   . CYS A 1 369 ? 122.651 92.277  118.511 1.00 174.77 ? 1146 CYS A N   1 
ATOM   1868 C  CA  . CYS A 1 369 ? 123.769 92.419  119.437 1.00 175.50 ? 1146 CYS A CA  1 
ATOM   1869 C  C   . CYS A 1 369 ? 123.346 92.105  120.868 1.00 175.64 ? 1146 CYS A C   1 
ATOM   1870 O  O   . CYS A 1 369 ? 124.133 91.552  121.646 1.00 176.08 ? 1146 CYS A O   1 
ATOM   1871 C  CB  . CYS A 1 369 ? 124.356 93.827  119.348 1.00 176.25 ? 1146 CYS A CB  1 
ATOM   1872 S  SG  . CYS A 1 369 ? 125.886 94.041  120.289 1.00 182.26 ? 1146 CYS A SG  1 
ATOM   1873 N  N   . HIS A 1 370 ? 122.110 92.453  121.234 1.00 172.70 ? 1147 HIS A N   1 
ATOM   1874 C  CA  . HIS A 1 370 ? 121.622 92.161  122.578 1.00 171.42 ? 1147 HIS A CA  1 
ATOM   1875 C  C   . HIS A 1 370 ? 121.493 90.663  122.816 1.00 172.67 ? 1147 HIS A C   1 
ATOM   1876 O  O   . HIS A 1 370 ? 121.644 90.203  123.954 1.00 171.64 ? 1147 HIS A O   1 
ATOM   1877 C  CB  . HIS A 1 370 ? 120.276 92.847  122.809 1.00 172.82 ? 1147 HIS A CB  1 
ATOM   1878 C  CG  . HIS A 1 370 ? 120.390 94.245  123.330 1.00 173.60 ? 1147 HIS A CG  1 
ATOM   1879 N  ND1 . HIS A 1 370 ? 120.795 95.301  122.543 1.00 174.50 ? 1147 HIS A ND1 1 
ATOM   1880 C  CD2 . HIS A 1 370 ? 120.147 94.762  124.558 1.00 173.14 ? 1147 HIS A CD2 1 
ATOM   1881 C  CE1 . HIS A 1 370 ? 120.799 96.408  123.264 1.00 173.90 ? 1147 HIS A CE1 1 
ATOM   1882 N  NE2 . HIS A 1 370 ? 120.409 96.109  124.490 1.00 174.14 ? 1147 HIS A NE2 1 
ATOM   1883 N  N   . GLU A 1 371 ? 121.209 89.892  121.764 1.00 197.82 ? 1148 GLU A N   1 
ATOM   1884 C  CA  . GLU A 1 371 ? 121.076 88.447  121.916 1.00 198.58 ? 1148 GLU A CA  1 
ATOM   1885 C  C   . GLU A 1 371 ? 122.392 87.801  122.335 1.00 198.47 ? 1148 GLU A C   1 
ATOM   1886 O  O   . GLU A 1 371 ? 122.385 86.743  122.974 1.00 198.62 ? 1148 GLU A O   1 
ATOM   1887 C  CB  . GLU A 1 371 ? 120.563 87.834  120.610 1.00 198.54 ? 1148 GLU A CB  1 
ATOM   1888 C  CG  . GLU A 1 371 ? 120.349 86.327  120.648 1.00 199.44 ? 1148 GLU A CG  1 
ATOM   1889 C  CD  . GLU A 1 371 ? 121.556 85.552  120.156 1.00 200.90 ? 1148 GLU A CD  1 
ATOM   1890 O  OE1 . GLU A 1 371 ? 122.391 86.143  119.439 1.00 200.98 ? 1148 GLU A OE1 1 
ATOM   1891 O  OE2 . GLU A 1 371 ? 121.670 84.353  120.487 1.00 201.48 ? 1148 GLU A OE2 1 
ATOM   1892 N  N   . VAL A 1 372 ? 123.523 88.422  121.994 1.00 180.88 ? 1149 VAL A N   1 
ATOM   1893 C  CA  . VAL A 1 372 ? 124.823 87.858  122.351 1.00 179.72 ? 1149 VAL A CA  1 
ATOM   1894 C  C   . VAL A 1 372 ? 124.994 87.821  123.864 1.00 180.13 ? 1149 VAL A C   1 
ATOM   1895 O  O   . VAL A 1 372 ? 125.506 86.842  124.423 1.00 179.22 ? 1149 VAL A O   1 
ATOM   1896 C  CB  . VAL A 1 372 ? 125.954 88.652  121.673 1.00 179.37 ? 1149 VAL A CB  1 
ATOM   1897 C  CG1 . VAL A 1 372 ? 127.297 87.987  121.930 1.00 178.34 ? 1149 VAL A CG1 1 
ATOM   1898 C  CG2 . VAL A 1 372 ? 125.691 88.778  120.181 1.00 179.93 ? 1149 VAL A CG2 1 
ATOM   1899 N  N   . GLY A 1 373 ? 124.569 88.878  124.551 1.00 187.48 ? 1150 GLY A N   1 
ATOM   1900 C  CA  . GLY A 1 373 ? 124.678 88.925  125.996 1.00 187.66 ? 1150 GLY A CA  1 
ATOM   1901 C  C   . GLY A 1 373 ? 125.031 90.295  126.536 1.00 188.76 ? 1150 GLY A C   1 
ATOM   1902 O  O   . GLY A 1 373 ? 124.760 90.597  127.702 1.00 190.22 ? 1150 GLY A O   1 
ATOM   1903 N  N   . LEU A 1 374 ? 125.636 91.134  125.700 1.00 172.83 ? 1151 LEU A N   1 
ATOM   1904 C  CA  . LEU A 1 374 ? 126.011 92.486  126.086 1.00 171.78 ? 1151 LEU A CA  1 
ATOM   1905 C  C   . LEU A 1 374 ? 125.019 93.486  125.506 1.00 171.55 ? 1151 LEU A C   1 
ATOM   1906 O  O   . LEU A 1 374 ? 124.540 93.321  124.380 1.00 171.86 ? 1151 LEU A O   1 
ATOM   1907 C  CB  . LEU A 1 374 ? 127.431 92.813  125.619 1.00 170.43 ? 1151 LEU A CB  1 
ATOM   1908 C  CG  . LEU A 1 374 ? 127.732 92.713  124.121 1.00 170.13 ? 1151 LEU A CG  1 
ATOM   1909 C  CD1 . LEU A 1 374 ? 127.696 94.084  123.464 1.00 170.70 ? 1151 LEU A CD1 1 
ATOM   1910 C  CD2 . LEU A 1 374 ? 129.075 92.038  123.890 1.00 170.30 ? 1151 LEU A CD2 1 
ATOM   1911 N  N   . CYS A 1 375 ? 124.710 94.519  126.284 1.00 179.64 ? 1152 CYS A N   1 
ATOM   1912 C  CA  . CYS A 1 375 ? 123.748 95.539  125.895 1.00 181.33 ? 1152 CYS A CA  1 
ATOM   1913 C  C   . CYS A 1 375 ? 124.452 96.876  125.710 1.00 180.15 ? 1152 CYS A C   1 
ATOM   1914 O  O   . CYS A 1 375 ? 125.379 97.211  126.454 1.00 179.58 ? 1152 CYS A O   1 
ATOM   1915 C  CB  . CYS A 1 375 ? 122.638 95.673  126.940 1.00 183.40 ? 1152 CYS A CB  1 
ATOM   1916 S  SG  . CYS A 1 375 ? 123.203 96.179  128.580 1.00 188.76 ? 1152 CYS A SG  1 
ATOM   1917 N  N   . VAL A 1 376 ? 124.008 97.636  124.711 1.00 161.60 ? 1153 VAL A N   1 
ATOM   1918 C  CA  . VAL A 1 376 ? 124.568 98.944  124.399 1.00 161.21 ? 1153 VAL A CA  1 
ATOM   1919 C  C   . VAL A 1 376 ? 123.419 99.921  124.191 1.00 161.41 ? 1153 VAL A C   1 
ATOM   1920 O  O   . VAL A 1 376 ? 122.436 99.597  123.515 1.00 161.70 ? 1153 VAL A O   1 
ATOM   1921 C  CB  . VAL A 1 376 ? 125.480 98.893  123.157 1.00 161.97 ? 1153 VAL A CB  1 
ATOM   1922 C  CG1 . VAL A 1 376 ? 124.781 98.192  122.000 1.00 160.68 ? 1153 VAL A CG1 1 
ATOM   1923 C  CG2 . VAL A 1 376 ? 125.920 100.292 122.754 1.00 161.77 ? 1153 VAL A CG2 1 
ATOM   1924 N  N   . SER A 1 377 ? 123.535 101.107 124.782 1.00 156.62 ? 1154 SER A N   1 
ATOM   1925 C  CA  . SER A 1 377 ? 122.523 102.146 124.647 1.00 156.55 ? 1154 SER A CA  1 
ATOM   1926 C  C   . SER A 1 377 ? 122.813 102.968 123.397 1.00 157.72 ? 1154 SER A C   1 
ATOM   1927 O  O   . SER A 1 377 ? 123.885 103.571 123.279 1.00 158.84 ? 1154 SER A O   1 
ATOM   1928 C  CB  . SER A 1 377 ? 122.495 103.039 125.886 1.00 156.20 ? 1154 SER A CB  1 
ATOM   1929 O  OG  . SER A 1 377 ? 121.607 104.129 125.708 1.00 155.63 ? 1154 SER A OG  1 
ATOM   1930 N  N   . TRP A 1 378 ? 121.857 102.991 122.467 1.00 137.10 ? 1155 TRP A N   1 
ATOM   1931 C  CA  . TRP A 1 378 ? 122.015 103.710 121.213 1.00 133.16 ? 1155 TRP A CA  1 
ATOM   1932 C  C   . TRP A 1 378 ? 120.953 104.772 120.973 1.00 132.79 ? 1155 TRP A C   1 
ATOM   1933 O  O   . TRP A 1 378 ? 121.109 105.573 120.045 1.00 134.05 ? 1155 TRP A O   1 
ATOM   1934 C  CB  . TRP A 1 378 ? 122.002 102.730 120.029 1.00 131.81 ? 1155 TRP A CB  1 
ATOM   1935 C  CG  . TRP A 1 378 ? 120.702 102.005 119.877 1.00 132.35 ? 1155 TRP A CG  1 
ATOM   1936 C  CD1 . TRP A 1 378 ? 120.339 100.838 120.481 1.00 134.71 ? 1155 TRP A CD1 1 
ATOM   1937 C  CD2 . TRP A 1 378 ? 119.584 102.405 119.075 1.00 132.61 ? 1155 TRP A CD2 1 
ATOM   1938 N  NE1 . TRP A 1 378 ? 119.067 100.483 120.102 1.00 135.38 ? 1155 TRP A NE1 1 
ATOM   1939 C  CE2 . TRP A 1 378 ? 118.582 101.430 119.239 1.00 133.07 ? 1155 TRP A CE2 1 
ATOM   1940 C  CE3 . TRP A 1 378 ? 119.335 103.493 118.233 1.00 135.17 ? 1155 TRP A CE3 1 
ATOM   1941 C  CZ2 . TRP A 1 378 ? 117.351 101.508 118.592 1.00 132.83 ? 1155 TRP A CZ2 1 
ATOM   1942 C  CZ3 . TRP A 1 378 ? 118.112 103.570 117.592 1.00 134.81 ? 1155 TRP A CZ3 1 
ATOM   1943 C  CH2 . TRP A 1 378 ? 117.136 102.583 117.775 1.00 133.83 ? 1155 TRP A CH2 1 
ATOM   1944 N  N   . ARG A 1 379 ? 119.887 104.804 121.767 1.00 133.03 ? 1156 ARG A N   1 
ATOM   1945 C  CA  . ARG A 1 379 ? 118.814 105.758 121.535 1.00 133.79 ? 1156 ARG A CA  1 
ATOM   1946 C  C   . ARG A 1 379 ? 119.262 107.174 121.876 1.00 136.51 ? 1156 ARG A C   1 
ATOM   1947 O  O   . ARG A 1 379 ? 120.167 107.390 122.686 1.00 138.80 ? 1156 ARG A O   1 
ATOM   1948 C  CB  . ARG A 1 379 ? 117.579 105.381 122.351 1.00 133.21 ? 1156 ARG A CB  1 
ATOM   1949 C  CG  . ARG A 1 379 ? 116.983 104.039 121.962 1.00 132.38 ? 1156 ARG A CG  1 
ATOM   1950 C  CD  . ARG A 1 379 ? 115.497 103.978 122.266 1.00 135.04 ? 1156 ARG A CD  1 
ATOM   1951 N  NE  . ARG A 1 379 ? 114.869 102.806 121.668 1.00 133.90 ? 1156 ARG A NE  1 
ATOM   1952 C  CZ  . ARG A 1 379 ? 114.293 102.793 120.474 1.00 131.56 ? 1156 ARG A CZ  1 
ATOM   1953 N  NH1 . ARG A 1 379 ? 114.241 103.878 119.719 1.00 132.49 ? 1156 ARG A NH1 1 
ATOM   1954 N  NH2 . ARG A 1 379 ? 113.753 101.663 120.026 1.00 130.18 ? 1156 ARG A NH2 1 
ATOM   1955 N  N   . THR A 1 380 ? 118.609 108.147 121.239 1.00 151.80 ? 1157 THR A N   1 
ATOM   1956 C  CA  . THR A 1 380 ? 118.959 109.551 121.341 1.00 151.06 ? 1157 THR A CA  1 
ATOM   1957 C  C   . THR A 1 380 ? 117.680 110.348 121.140 1.00 152.59 ? 1157 THR A C   1 
ATOM   1958 O  O   . THR A 1 380 ? 116.863 109.977 120.285 1.00 156.60 ? 1157 THR A O   1 
ATOM   1959 C  CB  . THR A 1 380 ? 120.012 109.941 120.293 1.00 150.89 ? 1157 THR A CB  1 
ATOM   1960 O  OG1 . THR A 1 380 ? 121.289 109.418 120.680 1.00 154.28 ? 1157 THR A OG1 1 
ATOM   1961 C  CG2 . THR A 1 380 ? 120.119 111.452 120.137 1.00 149.43 ? 1157 THR A CG2 1 
ATOM   1962 N  N   . PRO A 1 381 ? 117.464 111.421 121.909 1.00 139.64 ? 1158 PRO A N   1 
ATOM   1963 C  CA  . PRO A 1 381 ? 116.246 112.228 121.717 1.00 139.68 ? 1158 PRO A CA  1 
ATOM   1964 C  C   . PRO A 1 381 ? 116.059 112.736 120.297 1.00 139.70 ? 1158 PRO A C   1 
ATOM   1965 O  O   . PRO A 1 381 ? 114.943 113.137 119.943 1.00 139.37 ? 1158 PRO A O   1 
ATOM   1966 C  CB  . PRO A 1 381 ? 116.429 113.390 122.708 1.00 137.34 ? 1158 PRO A CB  1 
ATOM   1967 C  CG  . PRO A 1 381 ? 117.860 113.311 123.174 1.00 137.63 ? 1158 PRO A CG  1 
ATOM   1968 C  CD  . PRO A 1 381 ? 118.244 111.875 123.070 1.00 137.39 ? 1158 PRO A CD  1 
ATOM   1969 N  N   . SER A 1 382 ? 117.107 112.737 119.475 1.00 147.03 ? 1159 SER A N   1 
ATOM   1970 C  CA  . SER A 1 382 ? 116.993 113.095 118.070 1.00 147.17 ? 1159 SER A CA  1 
ATOM   1971 C  C   . SER A 1 382 ? 117.055 111.891 117.139 1.00 146.30 ? 1159 SER A C   1 
ATOM   1972 O  O   . SER A 1 382 ? 116.826 112.049 115.935 1.00 147.44 ? 1159 SER A O   1 
ATOM   1973 C  CB  . SER A 1 382 ? 118.095 114.090 117.685 1.00 148.62 ? 1159 SER A CB  1 
ATOM   1974 O  OG  . SER A 1 382 ? 117.850 115.365 118.251 1.00 151.52 ? 1159 SER A OG  1 
ATOM   1975 N  N   . ILE A 1 383 ? 117.352 110.701 117.659 1.00 140.35 ? 1160 ILE A N   1 
ATOM   1976 C  CA  . ILE A 1 383 ? 117.485 109.488 116.855 1.00 140.29 ? 1160 ILE A CA  1 
ATOM   1977 C  C   . ILE A 1 383 ? 116.577 108.431 117.474 1.00 141.14 ? 1160 ILE A C   1 
ATOM   1978 O  O   . ILE A 1 383 ? 116.934 107.812 118.483 1.00 142.71 ? 1160 ILE A O   1 
ATOM   1979 C  CB  . ILE A 1 383 ? 118.934 108.992 116.780 1.00 138.63 ? 1160 ILE A CB  1 
ATOM   1980 C  CG1 . ILE A 1 383 ? 119.836 110.059 116.159 1.00 140.22 ? 1160 ILE A CG1 1 
ATOM   1981 C  CG2 . ILE A 1 383 ? 119.013 107.701 115.981 1.00 139.29 ? 1160 ILE A CG2 1 
ATOM   1982 C  CD1 . ILE A 1 383 ? 119.425 110.470 114.763 1.00 139.77 ? 1160 ILE A CD1 1 
ATOM   1983 N  N   . CYS A 1 384 ? 115.408 108.215 116.865 1.00 153.61 ? 1161 CYS A N   1 
ATOM   1984 C  CA  . CYS A 1 384 ? 114.431 107.217 117.292 1.00 153.79 ? 1161 CYS A CA  1 
ATOM   1985 C  C   . CYS A 1 384 ? 114.084 107.371 118.769 1.00 153.86 ? 1161 CYS A C   1 
ATOM   1986 O  O   . CYS A 1 384 ? 114.478 106.530 119.588 1.00 155.32 ? 1161 CYS A O   1 
ATOM   1987 C  CB  . CYS A 1 384 ? 114.953 105.804 117.020 1.00 155.89 ? 1161 CYS A CB  1 
ATOM   1988 S  SG  . CYS A 1 384 ? 115.285 105.437 115.280 1.00 161.81 ? 1161 CYS A SG  1 
ATOM   1989 N  N   . PRO A 1 385 ? 113.357 108.417 119.152 1.00 136.89 ? 1162 PRO A N   1 
ATOM   1990 C  CA  . PRO A 1 385 ? 113.022 108.618 120.562 1.00 137.20 ? 1162 PRO A CA  1 
ATOM   1991 C  C   . PRO A 1 385 ? 111.774 107.853 120.981 1.00 138.41 ? 1162 PRO A C   1 
ATOM   1992 O  O   . PRO A 1 385 ? 110.931 107.474 120.166 1.00 140.32 ? 1162 PRO A O   1 
ATOM   1993 C  CB  . PRO A 1 385 ? 112.782 110.131 120.638 1.00 136.09 ? 1162 PRO A CB  1 
ATOM   1994 C  CG  . PRO A 1 385 ? 112.209 110.461 119.300 1.00 136.79 ? 1162 PRO A CG  1 
ATOM   1995 C  CD  . PRO A 1 385 ? 112.833 109.503 118.304 1.00 137.51 ? 1162 PRO A CD  1 
ATOM   1996 N  N   . LEU A 1 386 ? 111.674 107.632 122.291 1.00 142.72 ? 1163 LEU A N   1 
ATOM   1997 C  CA  . LEU A 1 386 ? 110.519 106.989 122.900 1.00 140.68 ? 1163 LEU A CA  1 
ATOM   1998 C  C   . LEU A 1 386 ? 109.967 107.885 123.998 1.00 145.09 ? 1163 LEU A C   1 
ATOM   1999 O  O   . LEU A 1 386 ? 110.728 108.522 124.732 1.00 148.16 ? 1163 LEU A O   1 
ATOM   2000 C  CB  . LEU A 1 386 ? 110.877 105.616 123.481 1.00 139.58 ? 1163 LEU A CB  1 
ATOM   2001 C  CG  . LEU A 1 386 ? 111.656 104.659 122.579 1.00 143.95 ? 1163 LEU A CG  1 
ATOM   2002 C  CD1 . LEU A 1 386 ? 112.007 103.389 123.336 1.00 143.35 ? 1163 LEU A CD1 1 
ATOM   2003 C  CD2 . LEU A 1 386 ? 110.861 104.338 121.325 1.00 145.34 ? 1163 LEU A CD2 1 
ATOM   2004 N  N   . PHE A 1 387 ? 108.639 107.930 124.106 1.00 159.72 ? 1164 PHE A N   1 
ATOM   2005 C  CA  . PHE A 1 387 ? 107.964 108.776 125.088 1.00 159.58 ? 1164 PHE A CA  1 
ATOM   2006 C  C   . PHE A 1 387 ? 107.597 107.917 126.295 1.00 159.71 ? 1164 PHE A C   1 
ATOM   2007 O  O   . PHE A 1 387 ? 106.450 107.512 126.485 1.00 163.91 ? 1164 PHE A O   1 
ATOM   2008 C  CB  . PHE A 1 387 ? 106.739 109.440 124.468 1.00 159.96 ? 1164 PHE A CB  1 
ATOM   2009 C  CG  . PHE A 1 387 ? 106.426 110.791 125.043 1.00 159.64 ? 1164 PHE A CG  1 
ATOM   2010 C  CD1 . PHE A 1 387 ? 105.864 110.911 126.301 1.00 161.44 ? 1164 PHE A CD1 1 
ATOM   2011 C  CD2 . PHE A 1 387 ? 106.689 111.942 124.320 1.00 159.06 ? 1164 PHE A CD2 1 
ATOM   2012 C  CE1 . PHE A 1 387 ? 105.574 112.154 126.831 1.00 162.73 ? 1164 PHE A CE1 1 
ATOM   2013 C  CE2 . PHE A 1 387 ? 106.402 113.187 124.843 1.00 161.64 ? 1164 PHE A CE2 1 
ATOM   2014 C  CZ  . PHE A 1 387 ? 105.843 113.293 126.100 1.00 162.61 ? 1164 PHE A CZ  1 
ATOM   2015 N  N   . CYS A 1 388 ? 108.603 107.639 127.127 1.00 167.11 ? 1165 CYS A N   1 
ATOM   2016 C  CA  . CYS A 1 388 ? 108.379 106.838 128.325 1.00 169.21 ? 1165 CYS A CA  1 
ATOM   2017 C  C   . CYS A 1 388 ? 107.554 107.575 129.372 1.00 168.87 ? 1165 CYS A C   1 
ATOM   2018 O  O   . CYS A 1 388 ? 106.961 106.929 130.242 1.00 169.53 ? 1165 CYS A O   1 
ATOM   2019 C  CB  . CYS A 1 388 ? 109.715 106.407 128.933 1.00 169.71 ? 1165 CYS A CB  1 
ATOM   2020 S  SG  . CYS A 1 388 ? 110.518 105.010 128.105 1.00 178.76 ? 1165 CYS A SG  1 
ATOM   2021 N  N   . ASP A 1 389 ? 107.503 108.906 129.311 1.00 167.42 ? 1166 ASP A N   1 
ATOM   2022 C  CA  . ASP A 1 389 ? 106.760 109.690 130.290 1.00 168.66 ? 1166 ASP A CA  1 
ATOM   2023 C  C   . ASP A 1 389 ? 105.257 109.680 130.042 1.00 168.77 ? 1166 ASP A C   1 
ATOM   2024 O  O   . ASP A 1 389 ? 104.498 110.098 130.923 1.00 168.83 ? 1166 ASP A O   1 
ATOM   2025 C  CB  . ASP A 1 389 ? 107.273 111.133 130.296 1.00 170.57 ? 1166 ASP A CB  1 
ATOM   2026 C  CG  . ASP A 1 389 ? 106.817 111.911 131.516 1.00 172.06 ? 1166 ASP A CG  1 
ATOM   2027 O  OD1 . ASP A 1 389 ? 106.448 111.276 132.526 1.00 171.70 ? 1166 ASP A OD1 1 
ATOM   2028 O  OD2 . ASP A 1 389 ? 106.827 113.159 131.463 1.00 171.57 ? 1166 ASP A OD2 1 
ATOM   2029 N  N   . TYR A 1 390 ? 104.810 109.215 128.873 1.00 160.48 ? 1167 TYR A N   1 
ATOM   2030 C  CA  . TYR A 1 390 ? 103.381 109.211 128.575 1.00 159.67 ? 1167 TYR A CA  1 
ATOM   2031 C  C   . TYR A 1 390 ? 102.623 108.277 129.509 1.00 158.67 ? 1167 TYR A C   1 
ATOM   2032 O  O   . TYR A 1 390 ? 101.509 108.592 129.945 1.00 158.35 ? 1167 TYR A O   1 
ATOM   2033 C  CB  . TYR A 1 390 ? 103.152 108.813 127.117 1.00 160.23 ? 1167 TYR A CB  1 
ATOM   2034 C  CG  . TYR A 1 390 ? 101.747 109.065 126.623 1.00 159.31 ? 1167 TYR A CG  1 
ATOM   2035 C  CD1 . TYR A 1 390 ? 101.349 110.332 126.219 1.00 159.01 ? 1167 TYR A CD1 1 
ATOM   2036 C  CD2 . TYR A 1 390 ? 100.818 108.035 126.556 1.00 160.73 ? 1167 TYR A CD2 1 
ATOM   2037 C  CE1 . TYR A 1 390 ? 100.066 110.568 125.765 1.00 160.59 ? 1167 TYR A CE1 1 
ATOM   2038 C  CE2 . TYR A 1 390 ? 99.533  108.261 126.104 1.00 161.54 ? 1167 TYR A CE2 1 
ATOM   2039 C  CZ  . TYR A 1 390 ? 99.162  109.529 125.710 1.00 162.00 ? 1167 TYR A CZ  1 
ATOM   2040 O  OH  . TYR A 1 390 ? 97.883  109.758 125.259 1.00 163.14 ? 1167 TYR A OH  1 
ATOM   2041 N  N   . TYR A 1 391 ? 103.210 107.123 129.830 1.00 165.28 ? 1168 TYR A N   1 
ATOM   2042 C  CA  . TYR A 1 391 ? 102.540 106.162 130.697 1.00 167.72 ? 1168 TYR A CA  1 
ATOM   2043 C  C   . TYR A 1 391 ? 102.552 106.590 132.159 1.00 169.80 ? 1168 TYR A C   1 
ATOM   2044 O  O   . TYR A 1 391 ? 101.795 106.031 132.960 1.00 170.00 ? 1168 TYR A O   1 
ATOM   2045 C  CB  . TYR A 1 391 ? 103.188 104.786 130.553 1.00 167.79 ? 1168 TYR A CB  1 
ATOM   2046 C  CG  . TYR A 1 391 ? 103.442 104.379 129.120 1.00 166.72 ? 1168 TYR A CG  1 
ATOM   2047 C  CD1 . TYR A 1 391 ? 102.416 104.385 128.184 1.00 166.55 ? 1168 TYR A CD1 1 
ATOM   2048 C  CD2 . TYR A 1 391 ? 104.707 103.990 128.701 1.00 167.53 ? 1168 TYR A CD2 1 
ATOM   2049 C  CE1 . TYR A 1 391 ? 102.643 104.014 126.873 1.00 167.74 ? 1168 TYR A CE1 1 
ATOM   2050 C  CE2 . TYR A 1 391 ? 104.944 103.618 127.392 1.00 167.95 ? 1168 TYR A CE2 1 
ATOM   2051 C  CZ  . TYR A 1 391 ? 103.908 103.632 126.482 1.00 168.03 ? 1168 TYR A CZ  1 
ATOM   2052 O  OH  . TYR A 1 391 ? 104.139 103.262 125.178 1.00 169.31 ? 1168 TYR A OH  1 
ATOM   2053 N  N   . ASN A 1 392 ? 103.385 107.555 132.523 1.00 178.13 ? 1169 ASN A N   1 
ATOM   2054 C  CA  . ASN A 1 392 ? 103.444 108.005 133.908 1.00 177.60 ? 1169 ASN A CA  1 
ATOM   2055 C  C   . ASN A 1 392 ? 102.178 108.780 134.259 1.00 177.19 ? 1169 ASN A C   1 
ATOM   2056 O  O   . ASN A 1 392 ? 101.808 109.713 133.537 1.00 177.72 ? 1169 ASN A O   1 
ATOM   2057 C  CB  . ASN A 1 392 ? 104.675 108.879 134.135 1.00 175.97 ? 1169 ASN A CB  1 
ATOM   2058 C  CG  . ASN A 1 392 ? 105.829 108.111 134.749 1.00 176.10 ? 1169 ASN A CG  1 
ATOM   2059 O  OD1 . ASN A 1 392 ? 105.635 107.067 135.371 1.00 176.42 ? 1169 ASN A OD1 1 
ATOM   2060 N  ND2 . ASN A 1 392 ? 107.040 108.628 134.579 1.00 176.03 ? 1169 ASN A ND2 1 
ATOM   2061 N  N   . PRO A 1 393 ? 101.491 108.430 135.342 1.00 175.13 ? 1170 PRO A N   1 
ATOM   2062 C  CA  . PRO A 1 393 ? 100.304 109.191 135.745 1.00 175.49 ? 1170 PRO A CA  1 
ATOM   2063 C  C   . PRO A 1 393 ? 100.691 110.547 136.315 1.00 178.03 ? 1170 PRO A C   1 
ATOM   2064 O  O   . PRO A 1 393 ? 101.861 110.849 136.558 1.00 179.32 ? 1170 PRO A O   1 
ATOM   2065 C  CB  . PRO A 1 393 ? 99.652  108.301 136.805 1.00 174.70 ? 1170 PRO A CB  1 
ATOM   2066 C  CG  . PRO A 1 393 ? 100.781 107.507 137.367 1.00 174.86 ? 1170 PRO A CG  1 
ATOM   2067 C  CD  . PRO A 1 393 ? 101.751 107.288 136.237 1.00 174.55 ? 1170 PRO A CD  1 
ATOM   2068 N  N   . GLU A 1 394 ? 99.672  111.377 136.526 1.00 207.12 ? 1171 GLU A N   1 
ATOM   2069 C  CA  . GLU A 1 394 ? 99.895  112.723 137.036 1.00 208.10 ? 1171 GLU A CA  1 
ATOM   2070 C  C   . GLU A 1 394 ? 100.425 112.672 138.463 1.00 207.77 ? 1171 GLU A C   1 
ATOM   2071 O  O   . GLU A 1 394 ? 99.857  111.995 139.326 1.00 207.40 ? 1171 GLU A O   1 
ATOM   2072 C  CB  . GLU A 1 394 ? 98.599  113.531 136.980 1.00 208.45 ? 1171 GLU A CB  1 
ATOM   2073 C  CG  . GLU A 1 394 ? 98.775  115.004 137.307 1.00 209.12 ? 1171 GLU A CG  1 
ATOM   2074 C  CD  . GLU A 1 394 ? 99.757  115.694 136.380 1.00 209.45 ? 1171 GLU A CD  1 
ATOM   2075 O  OE1 . GLU A 1 394 ? 99.700  115.443 135.157 1.00 209.14 ? 1171 GLU A OE1 1 
ATOM   2076 O  OE2 . GLU A 1 394 ? 100.586 116.487 136.873 1.00 209.41 ? 1171 GLU A OE2 1 
ATOM   2077 N  N   . GLY A 1 395 ? 101.519 113.390 138.709 1.00 202.48 ? 1172 GLY A N   1 
ATOM   2078 C  CA  . GLY A 1 395 ? 102.119 113.449 140.024 1.00 202.47 ? 1172 GLY A CA  1 
ATOM   2079 C  C   . GLY A 1 395 ? 102.997 112.274 140.390 1.00 202.02 ? 1172 GLY A C   1 
ATOM   2080 O  O   . GLY A 1 395 ? 103.538 112.252 141.503 1.00 201.29 ? 1172 GLY A O   1 
ATOM   2081 N  N   . GLN A 1 396 ? 103.163 111.301 139.498 1.00 199.96 ? 1173 GLN A N   1 
ATOM   2082 C  CA  . GLN A 1 396 ? 103.965 110.118 139.769 1.00 198.99 ? 1173 GLN A CA  1 
ATOM   2083 C  C   . GLN A 1 396 ? 104.996 109.933 138.664 1.00 199.43 ? 1173 GLN A C   1 
ATOM   2084 O  O   . GLN A 1 396 ? 104.842 110.436 137.549 1.00 199.71 ? 1173 GLN A O   1 
ATOM   2085 C  CB  . GLN A 1 396 ? 103.094 108.859 139.886 1.00 199.44 ? 1173 GLN A CB  1 
ATOM   2086 C  CG  . GLN A 1 396 ? 101.949 108.976 140.880 1.00 199.64 ? 1173 GLN A CG  1 
ATOM   2087 C  CD  . GLN A 1 396 ? 102.402 109.481 142.235 1.00 200.18 ? 1173 GLN A CD  1 
ATOM   2088 O  OE1 . GLN A 1 396 ? 103.354 108.961 142.818 1.00 200.45 ? 1173 GLN A OE1 1 
ATOM   2089 N  NE2 . GLN A 1 396 ? 101.720 110.499 142.746 1.00 199.89 ? 1173 GLN A NE2 1 
ATOM   2090 N  N   . CYS A 1 397 ? 106.059 109.198 138.994 1.00 204.23 ? 1174 CYS A N   1 
ATOM   2091 C  CA  . CYS A 1 397 ? 107.122 108.907 138.033 1.00 204.91 ? 1174 CYS A CA  1 
ATOM   2092 C  C   . CYS A 1 397 ? 107.689 107.534 138.381 1.00 204.98 ? 1174 CYS A C   1 
ATOM   2093 O  O   . CYS A 1 397 ? 108.425 107.395 139.362 1.00 205.49 ? 1174 CYS A O   1 
ATOM   2094 C  CB  . CYS A 1 397 ? 108.201 109.982 138.060 1.00 204.35 ? 1174 CYS A CB  1 
ATOM   2095 S  SG  . CYS A 1 397 ? 109.757 109.491 137.285 1.00 205.88 ? 1174 CYS A SG  1 
ATOM   2096 N  N   . GLU A 1 398 ? 107.341 106.530 137.577 1.00 195.76 ? 1175 GLU A N   1 
ATOM   2097 C  CA  . GLU A 1 398 ? 107.799 105.168 137.823 1.00 195.59 ? 1175 GLU A CA  1 
ATOM   2098 C  C   . GLU A 1 398 ? 108.382 104.548 136.561 1.00 194.63 ? 1175 GLU A C   1 
ATOM   2099 O  O   . GLU A 1 398 ? 109.230 103.652 136.636 1.00 195.94 ? 1175 GLU A O   1 
ATOM   2100 C  CB  . GLU A 1 398 ? 106.652 104.305 138.354 1.00 196.69 ? 1175 GLU A CB  1 
ATOM   2101 C  CG  . GLU A 1 398 ? 106.214 104.647 139.768 1.00 197.86 ? 1175 GLU A CG  1 
ATOM   2102 C  CD  . GLU A 1 398 ? 105.204 105.777 139.808 1.00 197.58 ? 1175 GLU A CD  1 
ATOM   2103 O  OE1 . GLU A 1 398 ? 104.699 106.162 138.733 1.00 198.07 ? 1175 GLU A OE1 1 
ATOM   2104 O  OE2 . GLU A 1 398 ? 104.916 106.280 140.914 1.00 197.09 ? 1175 GLU A OE2 1 
ATOM   2105 N  N   . TRP A 1 399 ? 107.936 105.014 135.398 1.00 170.29 ? 1176 TRP A N   1 
ATOM   2106 C  CA  . TRP A 1 399 ? 108.388 104.452 134.134 1.00 170.82 ? 1176 TRP A CA  1 
ATOM   2107 C  C   . TRP A 1 399 ? 109.785 104.951 133.788 1.00 170.66 ? 1176 TRP A C   1 
ATOM   2108 O  O   . TRP A 1 399 ? 110.114 106.121 134.000 1.00 171.25 ? 1176 TRP A O   1 
ATOM   2109 C  CB  . TRP A 1 399 ? 107.411 104.806 133.014 1.00 169.90 ? 1176 TRP A CB  1 
ATOM   2110 C  CG  . TRP A 1 399 ? 106.103 104.084 133.117 1.00 169.75 ? 1176 TRP A CG  1 
ATOM   2111 C  CD1 . TRP A 1 399 ? 104.989 104.498 133.786 1.00 170.76 ? 1176 TRP A CD1 1 
ATOM   2112 C  CD2 . TRP A 1 399 ? 105.774 102.818 132.534 1.00 169.28 ? 1176 TRP A CD2 1 
ATOM   2113 N  NE1 . TRP A 1 399 ? 103.986 103.569 133.655 1.00 170.27 ? 1176 TRP A NE1 1 
ATOM   2114 C  CE2 . TRP A 1 399 ? 104.442 102.527 132.891 1.00 169.85 ? 1176 TRP A CE2 1 
ATOM   2115 C  CE3 . TRP A 1 399 ? 106.475 101.902 131.745 1.00 170.07 ? 1176 TRP A CE3 1 
ATOM   2116 C  CZ2 . TRP A 1 399 ? 103.798 101.361 132.486 1.00 171.57 ? 1176 TRP A CZ2 1 
ATOM   2117 C  CZ3 . TRP A 1 399 ? 105.834 100.744 131.343 1.00 170.98 ? 1176 TRP A CZ3 1 
ATOM   2118 C  CH2 . TRP A 1 399 ? 104.509 100.484 131.715 1.00 171.76 ? 1176 TRP A CH2 1 
ATOM   2119 N  N   . HIS A 1 400 ? 110.606 104.050 133.252 1.00 177.96 ? 1177 HIS A N   1 
ATOM   2120 C  CA  . HIS A 1 400 ? 111.967 104.380 132.859 1.00 176.28 ? 1177 HIS A CA  1 
ATOM   2121 C  C   . HIS A 1 400 ? 112.339 103.558 131.635 1.00 176.88 ? 1177 HIS A C   1 
ATOM   2122 O  O   . HIS A 1 400 ? 111.698 102.551 131.321 1.00 180.20 ? 1177 HIS A O   1 
ATOM   2123 C  CB  . HIS A 1 400 ? 112.964 104.127 133.997 1.00 177.35 ? 1177 HIS A CB  1 
ATOM   2124 C  CG  . HIS A 1 400 ? 112.868 105.115 135.117 1.00 179.24 ? 1177 HIS A CG  1 
ATOM   2125 N  ND1 . HIS A 1 400 ? 111.931 105.012 136.122 1.00 180.27 ? 1177 HIS A ND1 1 
ATOM   2126 C  CD2 . HIS A 1 400 ? 113.593 106.225 135.391 1.00 180.46 ? 1177 HIS A CD2 1 
ATOM   2127 C  CE1 . HIS A 1 400 ? 112.083 106.016 136.967 1.00 180.97 ? 1177 HIS A CE1 1 
ATOM   2128 N  NE2 . HIS A 1 400 ? 113.084 106.767 136.546 1.00 181.50 ? 1177 HIS A NE2 1 
ATOM   2129 N  N   . TYR A 1 401 ? 113.387 103.999 130.946 1.00 151.46 ? 1178 TYR A N   1 
ATOM   2130 C  CA  . TYR A 1 401 ? 113.873 103.333 129.745 1.00 153.33 ? 1178 TYR A CA  1 
ATOM   2131 C  C   . TYR A 1 401 ? 115.071 102.463 130.105 1.00 152.74 ? 1178 TYR A C   1 
ATOM   2132 O  O   . TYR A 1 401 ? 116.075 102.964 130.621 1.00 153.38 ? 1178 TYR A O   1 
ATOM   2133 C  CB  . TYR A 1 401 ? 114.253 104.353 128.672 1.00 153.16 ? 1178 TYR A CB  1 
ATOM   2134 C  CG  . TYR A 1 401 ? 115.150 103.796 127.590 1.00 153.03 ? 1178 TYR A CG  1 
ATOM   2135 C  CD1 . TYR A 1 401 ? 114.706 102.790 126.743 1.00 152.58 ? 1178 TYR A CD1 1 
ATOM   2136 C  CD2 . TYR A 1 401 ? 116.440 104.278 127.416 1.00 153.84 ? 1178 TYR A CD2 1 
ATOM   2137 C  CE1 . TYR A 1 401 ? 115.523 102.278 125.754 1.00 153.16 ? 1178 TYR A CE1 1 
ATOM   2138 C  CE2 . TYR A 1 401 ? 117.263 103.772 126.429 1.00 154.30 ? 1178 TYR A CE2 1 
ATOM   2139 C  CZ  . TYR A 1 401 ? 116.800 102.772 125.601 1.00 154.21 ? 1178 TYR A CZ  1 
ATOM   2140 O  OH  . TYR A 1 401 ? 117.617 102.265 124.618 1.00 154.15 ? 1178 TYR A OH  1 
ATOM   2141 N  N   . GLN A 1 402 ? 114.961 101.165 129.832 1.00 158.40 ? 1179 GLN A N   1 
ATOM   2142 C  CA  . GLN A 1 402 ? 116.037 100.220 130.110 1.00 156.97 ? 1179 GLN A CA  1 
ATOM   2143 C  C   . GLN A 1 402 ? 116.587 99.672  128.802 1.00 157.91 ? 1179 GLN A C   1 
ATOM   2144 O  O   . GLN A 1 402 ? 115.910 98.866  128.143 1.00 159.45 ? 1179 GLN A O   1 
ATOM   2145 C  CB  . GLN A 1 402 ? 115.538 99.080  130.998 1.00 159.20 ? 1179 GLN A CB  1 
ATOM   2146 C  CG  . GLN A 1 402 ? 114.751 99.541  132.212 1.00 161.30 ? 1179 GLN A CG  1 
ATOM   2147 C  CD  . GLN A 1 402 ? 115.639 100.133 133.288 1.00 162.20 ? 1179 GLN A CD  1 
ATOM   2148 O  OE1 . GLN A 1 402 ? 116.842 99.877  133.327 1.00 162.14 ? 1179 GLN A OE1 1 
ATOM   2149 N  NE2 . GLN A 1 402 ? 115.047 100.931 134.170 1.00 161.90 ? 1179 GLN A NE2 1 
ATOM   2150 N  N   . PRO A 1 403 ? 117.786 100.078 128.378 1.00 161.43 ? 1180 PRO A N   1 
ATOM   2151 C  CA  . PRO A 1 403 ? 118.336 99.545  127.121 1.00 162.82 ? 1180 PRO A CA  1 
ATOM   2152 C  C   . PRO A 1 403 ? 118.549 98.042  127.142 1.00 162.53 ? 1180 PRO A C   1 
ATOM   2153 O  O   . PRO A 1 403 ? 118.388 97.388  126.104 1.00 161.45 ? 1180 PRO A O   1 
ATOM   2154 C  CB  . PRO A 1 403 ? 119.665 100.299 126.969 1.00 163.63 ? 1180 PRO A CB  1 
ATOM   2155 C  CG  . PRO A 1 403 ? 119.556 101.484 127.879 1.00 164.25 ? 1180 PRO A CG  1 
ATOM   2156 C  CD  . PRO A 1 403 ? 118.692 101.046 129.015 1.00 162.76 ? 1180 PRO A CD  1 
ATOM   2157 N  N   . CYS A 1 404 ? 118.906 97.474  128.291 1.00 191.35 ? 1181 CYS A N   1 
ATOM   2158 C  CA  . CYS A 1 404 ? 119.162 96.045  128.399 1.00 192.55 ? 1181 CYS A CA  1 
ATOM   2159 C  C   . CYS A 1 404 ? 117.939 95.248  128.832 1.00 193.13 ? 1181 CYS A C   1 
ATOM   2160 O  O   . CYS A 1 404 ? 117.933 94.022  128.678 1.00 193.43 ? 1181 CYS A O   1 
ATOM   2161 C  CB  . CYS A 1 404 ? 120.307 95.787  129.385 1.00 194.52 ? 1181 CYS A CB  1 
ATOM   2162 S  SG  . CYS A 1 404 ? 121.578 97.072  129.407 1.00 198.73 ? 1181 CYS A SG  1 
ATOM   2163 N  N   . GLY A 1 405 ? 116.911 95.904  129.363 1.00 195.77 ? 1182 GLY A N   1 
ATOM   2164 C  CA  . GLY A 1 405 ? 115.733 95.204  129.835 1.00 195.63 ? 1182 GLY A CA  1 
ATOM   2165 C  C   . GLY A 1 405 ? 115.921 94.608  131.214 1.00 197.06 ? 1182 GLY A C   1 
ATOM   2166 O  O   . GLY A 1 405 ? 116.994 94.085  131.530 1.00 198.81 ? 1182 GLY A O   1 
ATOM   2167 N  N   . VAL A 1 406 ? 114.887 94.683  132.045 1.00 194.73 ? 1183 VAL A N   1 
ATOM   2168 C  CA  . VAL A 1 406 ? 114.948 94.160  133.408 1.00 195.45 ? 1183 VAL A CA  1 
ATOM   2169 C  C   . VAL A 1 406 ? 115.026 92.639  133.358 1.00 196.05 ? 1183 VAL A C   1 
ATOM   2170 O  O   . VAL A 1 406 ? 114.413 92.015  132.480 1.00 195.06 ? 1183 VAL A O   1 
ATOM   2171 C  CB  . VAL A 1 406 ? 113.745 94.631  134.240 1.00 194.17 ? 1183 VAL A CB  1 
ATOM   2172 C  CG1 . VAL A 1 406 ? 113.824 96.130  134.481 1.00 193.68 ? 1183 VAL A CG1 1 
ATOM   2173 C  CG2 . VAL A 1 406 ? 112.441 94.270  133.545 1.00 194.23 ? 1183 VAL A CG2 1 
ATOM   2174 N  N   . PRO A 1 407 ? 115.775 92.001  134.261 1.00 224.50 ? 1184 PRO A N   1 
ATOM   2175 C  CA  . PRO A 1 407 ? 115.833 90.533  134.266 1.00 224.57 ? 1184 PRO A CA  1 
ATOM   2176 C  C   . PRO A 1 407 ? 114.506 89.908  134.664 1.00 224.18 ? 1184 PRO A C   1 
ATOM   2177 O  O   . PRO A 1 407 ? 114.003 89.011  133.981 1.00 224.12 ? 1184 PRO A O   1 
ATOM   2178 C  CB  . PRO A 1 407 ? 116.934 90.226  135.290 1.00 225.18 ? 1184 PRO A CB  1 
ATOM   2179 C  CG  . PRO A 1 407 ? 116.993 91.434  136.165 1.00 224.79 ? 1184 PRO A CG  1 
ATOM   2180 C  CD  . PRO A 1 407 ? 116.642 92.601  135.290 1.00 225.10 ? 1184 PRO A CD  1 
ATOM   2181 N  N   . CYS A 1 408 ? 113.931 90.379  135.768 1.00 232.64 ? 1185 CYS A N   1 
ATOM   2182 C  CA  . CYS A 1 408 ? 112.640 89.891  136.229 1.00 233.48 ? 1185 CYS A CA  1 
ATOM   2183 C  C   . CYS A 1 408 ? 112.004 90.952  137.113 1.00 232.76 ? 1185 CYS A C   1 
ATOM   2184 O  O   . CYS A 1 408 ? 112.696 91.663  137.847 1.00 232.06 ? 1185 CYS A O   1 
ATOM   2185 C  CB  . CYS A 1 408 ? 112.774 88.565  136.989 1.00 234.86 ? 1185 CYS A CB  1 
ATOM   2186 S  SG  . CYS A 1 408 ? 113.583 88.696  138.600 1.00 236.61 ? 1185 CYS A SG  1 
ATOM   2187 N  N   . LEU A 1 409 ? 110.680 91.052  137.030 1.00 219.55 ? 1186 LEU A N   1 
ATOM   2188 C  CA  . LEU A 1 409 ? 109.926 92.017  137.814 1.00 218.66 ? 1186 LEU A CA  1 
ATOM   2189 C  C   . LEU A 1 409 ? 108.699 91.334  138.400 1.00 219.60 ? 1186 LEU A C   1 
ATOM   2190 O  O   . LEU A 1 409 ? 108.223 90.317  137.887 1.00 221.15 ? 1186 LEU A O   1 
ATOM   2191 C  CB  . LEU A 1 409 ? 109.515 93.235  136.974 1.00 218.45 ? 1186 LEU A CB  1 
ATOM   2192 C  CG  . LEU A 1 409 ? 108.201 93.145  136.196 1.00 219.04 ? 1186 LEU A CG  1 
ATOM   2193 C  CD1 . LEU A 1 409 ? 107.742 94.529  135.766 1.00 219.46 ? 1186 LEU A CD1 1 
ATOM   2194 C  CD2 . LEU A 1 409 ? 108.344 92.230  134.990 1.00 219.42 ? 1186 LEU A CD2 1 
ATOM   2195 N  N   . ARG A 1 410 ? 108.192 91.906  139.488 1.00 235.41 ? 1187 ARG A N   1 
ATOM   2196 C  CA  . ARG A 1 410 ? 107.053 91.345  140.202 1.00 236.78 ? 1187 ARG A CA  1 
ATOM   2197 C  C   . ARG A 1 410 ? 105.763 91.943  139.653 1.00 237.25 ? 1187 ARG A C   1 
ATOM   2198 O  O   . ARG A 1 410 ? 105.553 93.159  139.731 1.00 237.19 ? 1187 ARG A O   1 
ATOM   2199 C  CB  . ARG A 1 410 ? 107.177 91.612  141.701 1.00 236.66 ? 1187 ARG A CB  1 
ATOM   2200 C  CG  . ARG A 1 410 ? 108.598 91.522  142.230 1.00 236.05 ? 1187 ARG A CG  1 
ATOM   2201 C  CD  . ARG A 1 410 ? 108.770 92.345  143.495 1.00 236.01 ? 1187 ARG A CD  1 
ATOM   2202 N  NE  . ARG A 1 410 ? 107.616 92.231  144.380 1.00 236.09 ? 1187 ARG A NE  1 
ATOM   2203 C  CZ  . ARG A 1 410 ? 107.562 92.727  145.608 1.00 236.43 ? 1187 ARG A CZ  1 
ATOM   2204 N  NH1 . ARG A 1 410 ? 108.584 93.383  146.134 1.00 236.68 ? 1187 ARG A NH1 1 
ATOM   2205 N  NH2 . ARG A 1 410 ? 106.456 92.560  146.328 1.00 236.45 ? 1187 ARG A NH2 1 
ATOM   2206 N  N   . THR A 1 411 ? 104.906 91.092  139.102 1.00 256.51 ? 1188 THR A N   1 
ATOM   2207 C  CA  . THR A 1 411 ? 103.613 91.493  138.566 1.00 256.54 ? 1188 THR A CA  1 
ATOM   2208 C  C   . THR A 1 411 ? 102.505 90.738  139.301 1.00 256.92 ? 1188 THR A C   1 
ATOM   2209 O  O   . THR A 1 411 ? 102.752 90.026  140.279 1.00 257.27 ? 1188 THR A O   1 
ATOM   2210 C  CB  . THR A 1 411 ? 103.550 91.246  137.056 1.00 256.70 ? 1188 THR A CB  1 
ATOM   2211 O  OG1 . THR A 1 411 ? 103.624 89.838  136.797 1.00 257.42 ? 1188 THR A OG1 1 
ATOM   2212 C  CG2 . THR A 1 411 ? 104.698 91.949  136.350 1.00 256.72 ? 1188 THR A CG2 1 
ATOM   2213 N  N   . CYS A 1 412 ? 101.271 90.906  138.822 1.00 264.73 ? 1189 CYS A N   1 
ATOM   2214 C  CA  . CYS A 1 412 ? 100.145 90.200  139.426 1.00 265.19 ? 1189 CYS A CA  1 
ATOM   2215 C  C   . CYS A 1 412 ? 100.264 88.694  139.227 1.00 264.92 ? 1189 CYS A C   1 
ATOM   2216 O  O   . CYS A 1 412 ? 100.025 87.919  140.160 1.00 264.88 ? 1189 CYS A O   1 
ATOM   2217 C  CB  . CYS A 1 412 ? 98.829  90.717  138.846 1.00 265.44 ? 1189 CYS A CB  1 
ATOM   2218 S  SG  . CYS A 1 412 ? 98.005  91.960  139.868 1.00 268.80 ? 1189 CYS A SG  1 
ATOM   2219 N  N   . ARG A 1 413 ? 100.632 88.262  138.021 1.00 251.70 ? 1190 ARG A N   1 
ATOM   2220 C  CA  . ARG A 1 413 ? 100.791 86.841  137.740 1.00 251.73 ? 1190 ARG A CA  1 
ATOM   2221 C  C   . ARG A 1 413 ? 102.175 86.316  138.095 1.00 251.66 ? 1190 ARG A C   1 
ATOM   2222 O  O   . ARG A 1 413 ? 102.372 85.096  138.103 1.00 250.92 ? 1190 ARG A O   1 
ATOM   2223 C  CB  . ARG A 1 413 ? 100.501 86.562  136.263 1.00 251.80 ? 1190 ARG A CB  1 
ATOM   2224 C  CG  . ARG A 1 413 ? 99.185  87.143  135.770 1.00 251.34 ? 1190 ARG A CG  1 
ATOM   2225 C  CD  . ARG A 1 413 ? 99.150  87.222  134.253 1.00 251.95 ? 1190 ARG A CD  1 
ATOM   2226 N  NE  . ARG A 1 413 ? 100.303 87.935  133.716 1.00 252.76 ? 1190 ARG A NE  1 
ATOM   2227 C  CZ  . ARG A 1 413 ? 100.522 88.139  132.424 1.00 252.02 ? 1190 ARG A CZ  1 
ATOM   2228 N  NH1 . ARG A 1 413 ? 99.682  87.698  131.502 1.00 251.68 ? 1190 ARG A NH1 1 
ATOM   2229 N  NH2 . ARG A 1 413 ? 101.612 88.802  132.048 1.00 251.23 ? 1190 ARG A NH2 1 
ATOM   2230 N  N   . ASN A 1 414 ? 103.130 87.195  138.386 1.00 262.62 ? 1191 ASN A N   1 
ATOM   2231 C  CA  . ASN A 1 414 ? 104.487 86.792  138.755 1.00 262.92 ? 1191 ASN A CA  1 
ATOM   2232 C  C   . ASN A 1 414 ? 104.808 87.331  140.142 1.00 263.26 ? 1191 ASN A C   1 
ATOM   2233 O  O   . ASN A 1 414 ? 105.178 88.510  140.282 1.00 263.57 ? 1191 ASN A O   1 
ATOM   2234 C  CB  . ASN A 1 414 ? 105.504 87.297  137.733 1.00 262.95 ? 1191 ASN A CB  1 
ATOM   2235 C  CG  . ASN A 1 414 ? 106.927 86.902  138.081 1.00 263.10 ? 1191 ASN A CG  1 
ATOM   2236 O  OD1 . ASN A 1 414 ? 107.155 85.939  138.813 1.00 263.12 ? 1191 ASN A OD1 1 
ATOM   2237 N  ND2 . ASN A 1 414 ? 107.892 87.647  137.557 1.00 263.42 ? 1191 ASN A ND2 1 
ATOM   2238 N  N   . PRO A 1 415 ? 104.680 86.520  141.189 1.00 257.76 ? 1192 PRO A N   1 
ATOM   2239 C  CA  . PRO A 1 415 ? 104.977 87.001  142.543 1.00 257.03 ? 1192 PRO A CA  1 
ATOM   2240 C  C   . PRO A 1 415 ? 106.451 87.345  142.707 1.00 258.06 ? 1192 PRO A C   1 
ATOM   2241 O  O   . PRO A 1 415 ? 107.287 87.104  141.834 1.00 258.61 ? 1192 PRO A O   1 
ATOM   2242 C  CB  . PRO A 1 415 ? 104.577 85.824  143.439 1.00 256.65 ? 1192 PRO A CB  1 
ATOM   2243 C  CG  . PRO A 1 415 ? 103.637 85.008  142.605 1.00 256.56 ? 1192 PRO A CG  1 
ATOM   2244 C  CD  . PRO A 1 415 ? 104.119 85.160  141.196 1.00 257.38 ? 1192 PRO A CD  1 
ATOM   2245 N  N   . ARG A 1 416 ? 106.759 87.927  143.869 1.00 270.78 ? 1193 ARG A N   1 
ATOM   2246 C  CA  . ARG A 1 416 ? 108.129 88.342  144.154 1.00 270.93 ? 1193 ARG A CA  1 
ATOM   2247 C  C   . ARG A 1 416 ? 109.070 87.146  144.230 1.00 271.54 ? 1193 ARG A C   1 
ATOM   2248 O  O   . ARG A 1 416 ? 110.208 87.212  143.750 1.00 271.06 ? 1193 ARG A O   1 
ATOM   2249 C  CB  . ARG A 1 416 ? 108.170 89.142  145.456 1.00 271.15 ? 1193 ARG A CB  1 
ATOM   2250 C  CG  . ARG A 1 416 ? 109.569 89.518  145.917 1.00 271.49 ? 1193 ARG A CG  1 
ATOM   2251 C  CD  . ARG A 1 416 ? 109.549 90.083  147.327 1.00 272.22 ? 1193 ARG A CD  1 
ATOM   2252 N  NE  . ARG A 1 416 ? 108.971 89.146  148.283 1.00 272.51 ? 1193 ARG A NE  1 
ATOM   2253 C  CZ  . ARG A 1 416 ? 108.843 89.383  149.581 1.00 271.99 ? 1193 ARG A CZ  1 
ATOM   2254 N  NH1 . ARG A 1 416 ? 109.245 90.524  150.119 1.00 271.99 ? 1193 ARG A NH1 1 
ATOM   2255 N  NH2 . ARG A 1 416 ? 108.298 88.453  150.360 1.00 271.80 ? 1193 ARG A NH2 1 
ATOM   2256 N  N   . GLY A 1 417 ? 108.613 86.042  144.820 1.00 286.15 ? 1194 GLY A N   1 
ATOM   2257 C  CA  . GLY A 1 417 ? 109.452 84.867  144.973 1.00 286.32 ? 1194 GLY A CA  1 
ATOM   2258 C  C   . GLY A 1 417 ? 109.746 84.126  143.686 1.00 286.95 ? 1194 GLY A C   1 
ATOM   2259 O  O   . GLY A 1 417 ? 110.578 83.212  143.698 1.00 287.06 ? 1194 GLY A O   1 
ATOM   2260 N  N   . ASP A 1 418 ? 109.092 84.490  142.587 1.00 289.38 ? 1195 ASP A N   1 
ATOM   2261 C  CA  . ASP A 1 418 ? 109.296 83.850  141.297 1.00 289.34 ? 1195 ASP A CA  1 
ATOM   2262 C  C   . ASP A 1 418 ? 109.935 84.832  140.324 1.00 288.57 ? 1195 ASP A C   1 
ATOM   2263 O  O   . ASP A 1 418 ? 109.597 86.020  140.312 1.00 288.15 ? 1195 ASP A O   1 
ATOM   2264 C  CB  . ASP A 1 418 ? 107.973 83.332  140.727 1.00 289.27 ? 1195 ASP A CB  1 
ATOM   2265 C  CG  . ASP A 1 418 ? 107.171 82.542  141.742 1.00 289.06 ? 1195 ASP A CG  1 
ATOM   2266 O  OD1 . ASP A 1 418 ? 107.345 81.307  141.809 1.00 289.09 ? 1195 ASP A OD1 1 
ATOM   2267 O  OD2 . ASP A 1 418 ? 106.370 83.156  142.477 1.00 288.60 ? 1195 ASP A OD2 1 
ATOM   2268 N  N   . CYS A 1 419 ? 110.862 84.328  139.511 1.00 286.28 ? 1196 CYS A N   1 
ATOM   2269 C  CA  . CYS A 1 419 ? 111.554 85.152  138.523 1.00 286.20 ? 1196 CYS A CA  1 
ATOM   2270 C  C   . CYS A 1 419 ? 111.932 84.258  137.351 1.00 286.04 ? 1196 CYS A C   1 
ATOM   2271 O  O   . CYS A 1 419 ? 112.850 83.440  137.466 1.00 285.94 ? 1196 CYS A O   1 
ATOM   2272 C  CB  . CYS A 1 419 ? 112.788 85.818  139.127 1.00 286.16 ? 1196 CYS A CB  1 
ATOM   2273 S  SG  . CYS A 1 419 ? 112.495 87.470  139.801 1.00 287.46 ? 1196 CYS A SG  1 
ATOM   2274 N  N   . LEU A 1 420 ? 111.229 84.413  136.232 1.00 266.56 ? 1197 LEU A N   1 
ATOM   2275 C  CA  . LEU A 1 420 ? 111.467 83.601  135.040 1.00 265.89 ? 1197 LEU A CA  1 
ATOM   2276 C  C   . LEU A 1 420 ? 112.482 84.320  134.160 1.00 265.88 ? 1197 LEU A C   1 
ATOM   2277 O  O   . LEU A 1 420 ? 112.147 85.277  133.458 1.00 265.09 ? 1197 LEU A O   1 
ATOM   2278 C  CB  . LEU A 1 420 ? 110.162 83.345  134.294 1.00 265.08 ? 1197 LEU A CB  1 
ATOM   2279 C  CG  . LEU A 1 420 ? 109.067 82.618  135.077 1.00 265.02 ? 1197 LEU A CG  1 
ATOM   2280 C  CD1 . LEU A 1 420 ? 107.859 82.353  134.192 1.00 265.09 ? 1197 LEU A CD1 1 
ATOM   2281 C  CD2 . LEU A 1 420 ? 109.600 81.321  135.667 1.00 265.17 ? 1197 LEU A CD2 1 
ATOM   2282 N  N   . ARG A 1 421 ? 113.731 83.856  134.197 1.00 264.71 ? 1198 ARG A N   1 
ATOM   2283 C  CA  . ARG A 1 421 ? 114.805 84.426  133.386 1.00 264.43 ? 1198 ARG A CA  1 
ATOM   2284 C  C   . ARG A 1 421 ? 115.001 83.536  132.161 1.00 264.37 ? 1198 ARG A C   1 
ATOM   2285 O  O   . ARG A 1 421 ? 115.947 82.755  132.063 1.00 263.67 ? 1198 ARG A O   1 
ATOM   2286 C  CB  . ARG A 1 421 ? 116.084 84.561  134.206 1.00 263.80 ? 1198 ARG A CB  1 
ATOM   2287 C  CG  . ARG A 1 421 ? 116.268 83.473  135.251 1.00 263.68 ? 1198 ARG A CG  1 
ATOM   2288 C  CD  . ARG A 1 421 ? 117.315 83.866  136.280 1.00 263.67 ? 1198 ARG A CD  1 
ATOM   2289 N  NE  . ARG A 1 421 ? 117.001 85.139  136.918 1.00 263.37 ? 1198 ARG A NE  1 
ATOM   2290 C  CZ  . ARG A 1 421 ? 116.278 85.266  138.022 1.00 263.01 ? 1198 ARG A CZ  1 
ATOM   2291 N  NH1 . ARG A 1 421 ? 115.773 84.212  138.642 1.00 262.44 ? 1198 ARG A NH1 1 
ATOM   2292 N  NH2 . ARG A 1 421 ? 116.056 86.481  138.516 1.00 263.10 ? 1198 ARG A NH2 1 
ATOM   2293 N  N   . ASP A 1 422 ? 114.079 83.667  131.208 1.00 267.85 ? 1199 ASP A N   1 
ATOM   2294 C  CA  . ASP A 1 422 ? 114.098 82.868  129.991 1.00 267.44 ? 1199 ASP A CA  1 
ATOM   2295 C  C   . ASP A 1 422 ? 114.332 83.680  128.727 1.00 267.18 ? 1199 ASP A C   1 
ATOM   2296 O  O   . ASP A 1 422 ? 114.907 83.155  127.772 1.00 266.87 ? 1199 ASP A O   1 
ATOM   2297 C  CB  . ASP A 1 422 ? 112.783 82.092  129.842 1.00 267.72 ? 1199 ASP A CB  1 
ATOM   2298 C  CG  . ASP A 1 422 ? 112.475 81.230  131.051 1.00 267.63 ? 1199 ASP A CG  1 
ATOM   2299 O  OD1 . ASP A 1 422 ? 113.420 80.872  131.785 1.00 267.80 ? 1199 ASP A OD1 1 
ATOM   2300 O  OD2 . ASP A 1 422 ? 111.287 80.911  131.267 1.00 267.20 ? 1199 ASP A OD2 1 
ATOM   2301 N  N   . VAL A 1 423 ? 113.903 84.939  128.695 1.00 251.12 ? 1200 VAL A N   1 
ATOM   2302 C  CA  . VAL A 1 423 ? 114.048 85.797  127.527 1.00 250.25 ? 1200 VAL A CA  1 
ATOM   2303 C  C   . VAL A 1 423 ? 114.937 86.976  127.893 1.00 249.86 ? 1200 VAL A C   1 
ATOM   2304 O  O   . VAL A 1 423 ? 114.797 87.563  128.971 1.00 250.23 ? 1200 VAL A O   1 
ATOM   2305 C  CB  . VAL A 1 423 ? 112.680 86.285  127.004 1.00 250.33 ? 1200 VAL A CB  1 
ATOM   2306 C  CG1 . VAL A 1 423 ? 112.021 85.205  126.162 1.00 250.54 ? 1200 VAL A CG1 1 
ATOM   2307 C  CG2 . VAL A 1 423 ? 111.780 86.685  128.163 1.00 249.62 ? 1200 VAL A CG2 1 
ATOM   2308 N  N   . ARG A 1 424 ? 115.857 87.316  126.993 1.00 218.95 ? 1201 ARG A N   1 
ATOM   2309 C  CA  . ARG A 1 424 ? 116.783 88.419  127.196 1.00 217.80 ? 1201 ARG A CA  1 
ATOM   2310 C  C   . ARG A 1 424 ? 116.847 89.272  125.937 1.00 217.68 ? 1201 ARG A C   1 
ATOM   2311 O  O   . ARG A 1 424 ? 116.615 88.788  124.826 1.00 217.16 ? 1201 ARG A O   1 
ATOM   2312 C  CB  . ARG A 1 424 ? 118.187 87.915  127.557 1.00 216.54 ? 1201 ARG A CB  1 
ATOM   2313 C  CG  . ARG A 1 424 ? 118.764 86.924  126.560 1.00 216.83 ? 1201 ARG A CG  1 
ATOM   2314 C  CD  . ARG A 1 424 ? 119.998 86.236  127.117 1.00 217.41 ? 1201 ARG A CD  1 
ATOM   2315 N  NE  . ARG A 1 424 ? 119.718 85.542  128.368 1.00 218.58 ? 1201 ARG A NE  1 
ATOM   2316 C  CZ  . ARG A 1 424 ? 120.617 84.863  129.066 1.00 218.95 ? 1201 ARG A CZ  1 
ATOM   2317 N  NH1 . ARG A 1 424 ? 121.873 84.763  128.662 1.00 219.04 ? 1201 ARG A NH1 1 
ATOM   2318 N  NH2 . ARG A 1 424 ? 120.247 84.268  130.196 1.00 218.60 ? 1201 ARG A NH2 1 
ATOM   2319 N  N   . GLY A 1 425 ? 117.166 90.550  126.124 1.00 191.91 ? 1202 GLY A N   1 
ATOM   2320 C  CA  . GLY A 1 425 ? 117.282 91.470  125.010 1.00 190.75 ? 1202 GLY A CA  1 
ATOM   2321 C  C   . GLY A 1 425 ? 115.960 92.081  124.595 1.00 189.90 ? 1202 GLY A C   1 
ATOM   2322 O  O   . GLY A 1 425 ? 115.554 91.970  123.434 1.00 189.69 ? 1202 GLY A O   1 
ATOM   2323 N  N   . LEU A 1 426 ? 115.276 92.729  125.536 1.00 173.10 ? 1203 LEU A N   1 
ATOM   2324 C  CA  . LEU A 1 426 ? 113.988 93.373  125.282 1.00 172.02 ? 1203 LEU A CA  1 
ATOM   2325 C  C   . LEU A 1 426 ? 114.060 94.799  125.817 1.00 173.98 ? 1203 LEU A C   1 
ATOM   2326 O  O   . LEU A 1 426 ? 114.007 95.017  127.031 1.00 175.73 ? 1203 LEU A O   1 
ATOM   2327 C  CB  . LEU A 1 426 ? 112.846 92.594  125.927 1.00 171.99 ? 1203 LEU A CB  1 
ATOM   2328 C  CG  . LEU A 1 426 ? 112.683 91.137  125.490 1.00 173.40 ? 1203 LEU A CG  1 
ATOM   2329 C  CD1 . LEU A 1 426 ? 113.307 90.195  126.509 1.00 176.11 ? 1203 LEU A CD1 1 
ATOM   2330 C  CD2 . LEU A 1 426 ? 111.217 90.805  125.276 1.00 173.28 ? 1203 LEU A CD2 1 
ATOM   2331 N  N   . GLU A 1 427 ? 114.177 95.766  124.913 1.00 167.06 ? 1204 GLU A N   1 
ATOM   2332 C  CA  . GLU A 1 427 ? 114.271 97.166  125.291 1.00 166.25 ? 1204 GLU A CA  1 
ATOM   2333 C  C   . GLU A 1 427 ? 112.900 97.833  125.239 1.00 166.50 ? 1204 GLU A C   1 
ATOM   2334 O  O   . GLU A 1 427 ? 111.964 97.341  124.605 1.00 166.89 ? 1204 GLU A O   1 
ATOM   2335 C  CB  . GLU A 1 427 ? 115.249 97.906  124.378 1.00 166.75 ? 1204 GLU A CB  1 
ATOM   2336 C  CG  . GLU A 1 427 ? 114.820 97.957  122.922 1.00 167.94 ? 1204 GLU A CG  1 
ATOM   2337 C  CD  . GLU A 1 427 ? 115.707 98.856  122.085 1.00 170.23 ? 1204 GLU A CD  1 
ATOM   2338 O  OE1 . GLU A 1 427 ? 116.196 99.875  122.618 1.00 171.13 ? 1204 GLU A OE1 1 
ATOM   2339 O  OE2 . GLU A 1 427 ? 115.916 98.546  120.894 1.00 170.47 ? 1204 GLU A OE2 1 
ATOM   2340 N  N   . GLY A 1 428 ? 112.794 98.970  125.921 1.00 175.61 ? 1205 GLY A N   1 
ATOM   2341 C  CA  . GLY A 1 428 ? 111.553 99.718  125.958 1.00 177.06 ? 1205 GLY A CA  1 
ATOM   2342 C  C   . GLY A 1 428 ? 111.290 100.369 127.300 1.00 176.42 ? 1205 GLY A C   1 
ATOM   2343 O  O   . GLY A 1 428 ? 112.126 100.298 128.206 1.00 177.40 ? 1205 GLY A O   1 
ATOM   2344 N  N   . CYS A 1 429 ? 110.133 101.010 127.438 1.00 176.04 ? 1206 CYS A N   1 
ATOM   2345 C  CA  . CYS A 1 429 ? 109.776 101.643 128.700 1.00 175.89 ? 1206 CYS A CA  1 
ATOM   2346 C  C   . CYS A 1 429 ? 109.365 100.587 129.718 1.00 174.23 ? 1206 CYS A C   1 
ATOM   2347 O  O   . CYS A 1 429 ? 108.547 99.710  129.424 1.00 175.72 ? 1206 CYS A O   1 
ATOM   2348 C  CB  . CYS A 1 429 ? 108.642 102.646 128.491 1.00 177.95 ? 1206 CYS A CB  1 
ATOM   2349 S  SG  . CYS A 1 429 ? 108.990 103.952 127.286 1.00 187.25 ? 1206 CYS A SG  1 
ATOM   2350 N  N   . TYR A 1 430 ? 109.936 100.670 130.919 1.00 160.59 ? 1207 TYR A N   1 
ATOM   2351 C  CA  . TYR A 1 430 ? 109.615 99.746  131.992 1.00 159.53 ? 1207 TYR A CA  1 
ATOM   2352 C  C   . TYR A 1 430 ? 109.319 100.518 133.270 1.00 160.03 ? 1207 TYR A C   1 
ATOM   2353 O  O   . TYR A 1 430 ? 109.946 101.552 133.533 1.00 163.36 ? 1207 TYR A O   1 
ATOM   2354 C  CB  . TYR A 1 430 ? 110.766 98.760  132.237 1.00 158.82 ? 1207 TYR A CB  1 
ATOM   2355 C  CG  . TYR A 1 430 ? 110.862 97.660  131.205 1.00 159.84 ? 1207 TYR A CG  1 
ATOM   2356 C  CD1 . TYR A 1 430 ? 110.157 96.474  131.359 1.00 160.38 ? 1207 TYR A CD1 1 
ATOM   2357 C  CD2 . TYR A 1 430 ? 111.657 97.807  130.077 1.00 161.57 ? 1207 TYR A CD2 1 
ATOM   2358 C  CE1 . TYR A 1 430 ? 110.241 95.466  130.419 1.00 160.99 ? 1207 TYR A CE1 1 
ATOM   2359 C  CE2 . TYR A 1 430 ? 111.747 96.805  129.131 1.00 162.62 ? 1207 TYR A CE2 1 
ATOM   2360 C  CZ  . TYR A 1 430 ? 111.037 95.636  129.307 1.00 161.77 ? 1207 TYR A CZ  1 
ATOM   2361 O  OH  . TYR A 1 430 ? 111.125 94.635  128.368 1.00 162.61 ? 1207 TYR A OH  1 
ATOM   2362 N  N   . PRO A 1 431 ? 108.376 100.047 134.081 1.00 148.20 ? 1208 PRO A N   1 
ATOM   2363 C  CA  . PRO A 1 431 ? 108.045 100.743 135.325 1.00 149.79 ? 1208 PRO A CA  1 
ATOM   2364 C  C   . PRO A 1 431 ? 108.922 100.309 136.487 1.00 151.23 ? 1208 PRO A C   1 
ATOM   2365 O  O   . PRO A 1 431 ? 109.379 99.168  136.576 1.00 150.79 ? 1208 PRO A O   1 
ATOM   2366 C  CB  . PRO A 1 431 ? 106.584 100.337 135.561 1.00 150.91 ? 1208 PRO A CB  1 
ATOM   2367 C  CG  . PRO A 1 431 ? 106.482 98.971  134.959 1.00 151.71 ? 1208 PRO A CG  1 
ATOM   2368 C  CD  . PRO A 1 431 ? 107.520 98.868  133.861 1.00 149.96 ? 1208 PRO A CD  1 
ATOM   2369 N  N   . LYS A 1 432 ? 109.154 101.256 137.391 1.00 185.80 ? 1209 LYS A N   1 
ATOM   2370 C  CA  . LYS A 1 432 ? 109.933 101.033 138.607 1.00 186.57 ? 1209 LYS A CA  1 
ATOM   2371 C  C   . LYS A 1 432 ? 109.015 101.316 139.792 1.00 186.39 ? 1209 LYS A C   1 
ATOM   2372 O  O   . LYS A 1 432 ? 108.892 102.459 140.239 1.00 186.16 ? 1209 LYS A O   1 
ATOM   2373 C  CB  . LYS A 1 432 ? 111.182 101.913 138.635 1.00 187.54 ? 1209 LYS A CB  1 
ATOM   2374 C  CG  . LYS A 1 432 ? 112.150 101.580 139.758 1.00 187.96 ? 1209 LYS A CG  1 
ATOM   2375 C  CD  . LYS A 1 432 ? 113.591 101.781 139.320 1.00 188.66 ? 1209 LYS A CD  1 
ATOM   2376 C  CE  . LYS A 1 432 ? 113.867 103.236 138.980 1.00 188.13 ? 1209 LYS A CE  1 
ATOM   2377 N  NZ  . LYS A 1 432 ? 115.303 103.586 139.159 1.00 188.25 ? 1209 LYS A NZ  1 
ATOM   2378 N  N   . CYS A 1 433 ? 108.369 100.270 140.295 1.00 210.30 ? 1210 CYS A N   1 
ATOM   2379 C  CA  . CYS A 1 433 ? 107.431 100.437 141.393 1.00 211.66 ? 1210 CYS A CA  1 
ATOM   2380 C  C   . CYS A 1 433 ? 108.174 100.818 142.672 1.00 212.27 ? 1210 CYS A C   1 
ATOM   2381 O  O   . CYS A 1 433 ? 109.279 100.326 142.921 1.00 213.11 ? 1210 CYS A O   1 
ATOM   2382 C  CB  . CYS A 1 433 ? 106.632 99.154  141.616 1.00 212.84 ? 1210 CYS A CB  1 
ATOM   2383 S  SG  . CYS A 1 433 ? 105.560 98.693  140.235 1.00 216.91 ? 1210 CYS A SG  1 
ATOM   2384 N  N   . PRO A 1 434 ? 107.600 101.688 143.496 1.00 209.63 ? 1211 PRO A N   1 
ATOM   2385 C  CA  . PRO A 1 434 ? 108.240 102.055 144.763 1.00 209.81 ? 1211 PRO A CA  1 
ATOM   2386 C  C   . PRO A 1 434 ? 108.205 100.894 145.739 1.00 211.12 ? 1211 PRO A C   1 
ATOM   2387 O  O   . PRO A 1 434 ? 107.470 99.918  145.524 1.00 212.13 ? 1211 PRO A O   1 
ATOM   2388 C  CB  . PRO A 1 434 ? 107.387 103.234 145.265 1.00 209.63 ? 1211 PRO A CB  1 
ATOM   2389 C  CG  . PRO A 1 434 ? 106.555 103.662 144.091 1.00 209.78 ? 1211 PRO A CG  1 
ATOM   2390 C  CD  . PRO A 1 434 ? 106.353 102.435 143.269 1.00 209.66 ? 1211 PRO A CD  1 
ATOM   2391 N  N   . PRO A 1 435 ? 108.996 100.950 146.817 1.00 225.06 ? 1212 PRO A N   1 
ATOM   2392 C  CA  . PRO A 1 435 ? 108.926 99.873  147.820 1.00 226.00 ? 1212 PRO A CA  1 
ATOM   2393 C  C   . PRO A 1 435 ? 107.534 99.685  148.395 1.00 225.78 ? 1212 PRO A C   1 
ATOM   2394 O  O   . PRO A 1 435 ? 107.127 98.549  148.668 1.00 226.06 ? 1212 PRO A O   1 
ATOM   2395 C  CB  . PRO A 1 435 ? 109.934 100.320 148.891 1.00 225.65 ? 1212 PRO A CB  1 
ATOM   2396 C  CG  . PRO A 1 435 ? 110.199 101.770 148.616 1.00 225.55 ? 1212 PRO A CG  1 
ATOM   2397 C  CD  . PRO A 1 435 ? 110.031 101.944 147.144 1.00 224.97 ? 1212 PRO A CD  1 
ATOM   2398 N  N   . GLU A 1 436 ? 106.790 100.771 148.586 1.00 223.87 ? 1213 GLU A N   1 
ATOM   2399 C  CA  . GLU A 1 436 ? 105.395 100.671 148.988 1.00 223.61 ? 1213 GLU A CA  1 
ATOM   2400 C  C   . GLU A 1 436 ? 104.545 100.303 147.779 1.00 224.25 ? 1213 GLU A C   1 
ATOM   2401 O  O   . GLU A 1 436 ? 104.617 100.961 146.736 1.00 223.63 ? 1213 GLU A O   1 
ATOM   2402 C  CB  . GLU A 1 436 ? 104.914 101.986 149.606 1.00 223.64 ? 1213 GLU A CB  1 
ATOM   2403 C  CG  . GLU A 1 436 ? 105.293 103.240 148.826 1.00 224.46 ? 1213 GLU A CG  1 
ATOM   2404 C  CD  . GLU A 1 436 ? 106.688 103.741 149.151 1.00 224.99 ? 1213 GLU A CD  1 
ATOM   2405 O  OE1 . GLU A 1 436 ? 107.399 103.068 149.927 1.00 225.21 ? 1213 GLU A OE1 1 
ATOM   2406 O  OE2 . GLU A 1 436 ? 107.073 104.809 148.630 1.00 225.15 ? 1213 GLU A OE2 1 
ATOM   2407 N  N   . ALA A 1 437 ? 103.745 99.244  147.923 1.00 237.07 ? 1214 ALA A N   1 
ATOM   2408 C  CA  . ALA A 1 437 ? 102.940 98.685  146.842 1.00 237.60 ? 1214 ALA A CA  1 
ATOM   2409 C  C   . ALA A 1 437 ? 103.812 98.384  145.627 1.00 237.40 ? 1214 ALA A C   1 
ATOM   2410 O  O   . ALA A 1 437 ? 103.668 99.035  144.584 1.00 236.72 ? 1214 ALA A O   1 
ATOM   2411 C  CB  . ALA A 1 437 ? 101.804 99.637  146.462 1.00 238.16 ? 1214 ALA A CB  1 
ATOM   2412 N  N   . PRO A 1 438 ? 104.721 97.414  145.716 1.00 237.56 ? 1215 PRO A N   1 
ATOM   2413 C  CA  . PRO A 1 438 ? 105.640 97.133  144.605 1.00 237.24 ? 1215 PRO A CA  1 
ATOM   2414 C  C   . PRO A 1 438 ? 105.148 96.096  143.604 1.00 237.47 ? 1215 PRO A C   1 
ATOM   2415 O  O   . PRO A 1 438 ? 105.943 95.661  142.765 1.00 237.03 ? 1215 PRO A O   1 
ATOM   2416 C  CB  . PRO A 1 438 ? 106.880 96.612  145.342 1.00 237.51 ? 1215 PRO A CB  1 
ATOM   2417 C  CG  . PRO A 1 438 ? 106.325 95.928  146.566 1.00 237.56 ? 1215 PRO A CG  1 
ATOM   2418 C  CD  . PRO A 1 438 ? 104.956 96.511  146.856 1.00 237.30 ? 1215 PRO A CD  1 
ATOM   2419 N  N   . ILE A 1 439 ? 103.884 95.693  143.664 1.00 254.54 ? 1216 ILE A N   1 
ATOM   2420 C  CA  . ILE A 1 439 ? 103.347 94.682  142.761 1.00 254.88 ? 1216 ILE A CA  1 
ATOM   2421 C  C   . ILE A 1 439 ? 102.725 95.385  141.562 1.00 255.17 ? 1216 ILE A C   1 
ATOM   2422 O  O   . ILE A 1 439 ? 101.828 96.221  141.717 1.00 256.05 ? 1216 ILE A O   1 
ATOM   2423 C  CB  . ILE A 1 439 ? 102.318 93.790  143.473 1.00 254.97 ? 1216 ILE A CB  1 
ATOM   2424 C  CG1 . ILE A 1 439 ? 103.019 92.822  144.428 1.00 254.70 ? 1216 ILE A CG1 1 
ATOM   2425 C  CG2 . ILE A 1 439 ? 101.482 93.024  142.458 1.00 255.10 ? 1216 ILE A CG2 1 
ATOM   2426 C  CD1 . ILE A 1 439 ? 104.199 92.101  143.814 1.00 254.14 ? 1216 ILE A CD1 1 
ATOM   2427 N  N   . PHE A 1 440 ? 103.201 95.049  140.366 1.00 241.85 ? 1217 PHE A N   1 
ATOM   2428 C  CA  . PHE A 1 440 ? 102.646 95.628  139.151 1.00 241.61 ? 1217 PHE A CA  1 
ATOM   2429 C  C   . PHE A 1 440 ? 101.276 95.026  138.868 1.00 242.60 ? 1217 PHE A C   1 
ATOM   2430 O  O   . PHE A 1 440 ? 101.112 93.802  138.859 1.00 242.46 ? 1217 PHE A O   1 
ATOM   2431 C  CB  . PHE A 1 440 ? 103.588 95.392  137.972 1.00 240.66 ? 1217 PHE A CB  1 
ATOM   2432 C  CG  . PHE A 1 440 ? 103.282 96.242  136.772 1.00 240.40 ? 1217 PHE A CG  1 
ATOM   2433 C  CD1 . PHE A 1 440 ? 103.182 97.618  136.890 1.00 240.54 ? 1217 PHE A CD1 1 
ATOM   2434 C  CD2 . PHE A 1 440 ? 103.098 95.666  135.527 1.00 240.51 ? 1217 PHE A CD2 1 
ATOM   2435 C  CE1 . PHE A 1 440 ? 102.901 98.403  135.788 1.00 240.19 ? 1217 PHE A CE1 1 
ATOM   2436 C  CE2 . PHE A 1 440 ? 102.818 96.446  134.421 1.00 240.49 ? 1217 PHE A CE2 1 
ATOM   2437 C  CZ  . PHE A 1 440 ? 102.719 97.816  134.552 1.00 240.15 ? 1217 PHE A CZ  1 
ATOM   2438 N  N   . ASP A 1 441 ? 100.287 95.893  138.634 1.00 275.45 ? 1218 ASP A N   1 
ATOM   2439 C  CA  . ASP A 1 441 ? 98.921  95.416  138.445 1.00 276.26 ? 1218 ASP A CA  1 
ATOM   2440 C  C   . ASP A 1 441 ? 98.746  94.748  137.085 1.00 276.10 ? 1218 ASP A C   1 
ATOM   2441 O  O   . ASP A 1 441 ? 97.885  93.873  136.932 1.00 276.41 ? 1218 ASP A O   1 
ATOM   2442 C  CB  . ASP A 1 441 ? 97.942  96.576  138.627 1.00 276.51 ? 1218 ASP A CB  1 
ATOM   2443 C  CG  . ASP A 1 441 ? 96.501  96.119  138.696 1.00 276.51 ? 1218 ASP A CG  1 
ATOM   2444 O  OD1 . ASP A 1 441 ? 96.245  95.035  139.260 1.00 277.21 ? 1218 ASP A OD1 1 
ATOM   2445 O  OD2 . ASP A 1 441 ? 95.620  96.858  138.211 1.00 276.05 ? 1218 ASP A OD2 1 
ATOM   2446 N  N   . GLU A 1 442 ? 99.541  95.151  136.095 1.00 267.39 ? 1219 GLU A N   1 
ATOM   2447 C  CA  . GLU A 1 442 ? 99.776  94.499  134.811 1.00 267.03 ? 1219 GLU A CA  1 
ATOM   2448 C  C   . GLU A 1 442 ? 98.609  94.632  133.829 1.00 267.24 ? 1219 GLU A C   1 
ATOM   2449 O  O   . GLU A 1 442 ? 98.756  94.226  132.676 1.00 267.32 ? 1219 GLU A O   1 
ATOM   2450 C  CB  . GLU A 1 442 ? 100.129 93.004  134.951 1.00 266.93 ? 1219 GLU A CB  1 
ATOM   2451 C  CG  . GLU A 1 442 ? 101.142 92.504  133.934 1.00 266.94 ? 1219 GLU A CG  1 
ATOM   2452 C  CD  . GLU A 1 442 ? 100.506 91.677  132.835 1.00 267.59 ? 1219 GLU A CD  1 
ATOM   2453 O  OE1 . GLU A 1 442 ? 99.328  91.290  132.987 1.00 267.98 ? 1219 GLU A OE1 1 
ATOM   2454 O  OE2 . GLU A 1 442 ? 101.183 91.416  131.819 1.00 267.57 ? 1219 GLU A OE2 1 
ATOM   2455 N  N   . ASP A 1 443 ? 97.463  95.185  134.227 1.00 265.59 ? 1220 ASP A N   1 
ATOM   2456 C  CA  . ASP A 1 443 ? 96.346  95.343  133.306 1.00 265.17 ? 1220 ASP A CA  1 
ATOM   2457 C  C   . ASP A 1 443 ? 95.945  96.791  133.065 1.00 265.25 ? 1220 ASP A C   1 
ATOM   2458 O  O   . ASP A 1 443 ? 95.321  97.072  132.036 1.00 265.39 ? 1220 ASP A O   1 
ATOM   2459 C  CB  . ASP A 1 443 ? 95.119  94.560  133.801 1.00 265.01 ? 1220 ASP A CB  1 
ATOM   2460 C  CG  . ASP A 1 443 ? 94.868  94.749  135.277 1.00 264.86 ? 1220 ASP A CG  1 
ATOM   2461 O  OD1 . ASP A 1 443 ? 95.700  95.408  135.930 1.00 265.23 ? 1220 ASP A OD1 1 
ATOM   2462 O  OD2 . ASP A 1 443 ? 93.845  94.243  135.783 1.00 264.55 ? 1220 ASP A OD2 1 
ATOM   2463 N  N   . LYS A 1 444 ? 96.278  97.715  133.972 1.00 263.64 ? 1221 LYS A N   1 
ATOM   2464 C  CA  . LYS A 1 444 ? 95.995  99.125  133.732 1.00 263.58 ? 1221 LYS A CA  1 
ATOM   2465 C  C   . LYS A 1 444 ? 97.199  100.014 134.034 1.00 263.17 ? 1221 LYS A C   1 
ATOM   2466 O  O   . LYS A 1 444 ? 97.022  101.206 134.315 1.00 263.61 ? 1221 LYS A O   1 
ATOM   2467 C  CB  . LYS A 1 444 ? 94.772  99.586  134.536 1.00 263.69 ? 1221 LYS A CB  1 
ATOM   2468 C  CG  . LYS A 1 444 ? 94.483  98.775  135.786 1.00 263.19 ? 1221 LYS A CG  1 
ATOM   2469 C  CD  . LYS A 1 444 ? 93.350  99.403  136.585 1.00 263.09 ? 1221 LYS A CD  1 
ATOM   2470 C  CE  . LYS A 1 444 ? 92.927  98.516  137.745 1.00 262.78 ? 1221 LYS A CE  1 
ATOM   2471 N  NZ  . LYS A 1 444 ? 92.286  97.257  137.275 1.00 263.32 ? 1221 LYS A NZ  1 
ATOM   2472 N  N   . MET A 1 445 ? 98.412  99.459  133.987 1.00 248.51 ? 1222 MET A N   1 
ATOM   2473 C  CA  . MET A 1 445 ? 99.658  100.225 134.003 1.00 248.28 ? 1222 MET A CA  1 
ATOM   2474 C  C   . MET A 1 445 ? 99.806  101.052 135.283 1.00 248.67 ? 1222 MET A C   1 
ATOM   2475 O  O   . MET A 1 445 ? 99.867  102.284 135.259 1.00 248.29 ? 1222 MET A O   1 
ATOM   2476 C  CB  . MET A 1 445 ? 99.762  101.114 132.758 1.00 247.21 ? 1222 MET A CB  1 
ATOM   2477 C  CG  . MET A 1 445 ? 99.622  100.370 131.437 1.00 247.07 ? 1222 MET A CG  1 
ATOM   2478 S  SD  . MET A 1 445 ? 100.589 98.849  131.364 1.00 246.79 ? 1222 MET A SD  1 
ATOM   2479 C  CE  . MET A 1 445 ? 99.294  97.611  131.394 1.00 247.57 ? 1222 MET A CE  1 
ATOM   2480 N  N   . GLN A 1 446 ? 99.866  100.348 136.411 1.00 265.49 ? 1223 GLN A N   1 
ATOM   2481 C  CA  . GLN A 1 446 ? 100.182 100.976 137.687 1.00 265.22 ? 1223 GLN A CA  1 
ATOM   2482 C  C   . GLN A 1 446 ? 100.622 99.893  138.662 1.00 265.57 ? 1223 GLN A C   1 
ATOM   2483 O  O   . GLN A 1 446 ? 100.451 98.697  138.414 1.00 266.03 ? 1223 GLN A O   1 
ATOM   2484 C  CB  . GLN A 1 446 ? 98.993  101.765 138.248 1.00 264.90 ? 1223 GLN A CB  1 
ATOM   2485 C  CG  . GLN A 1 446 ? 98.005  100.930 139.043 1.00 265.68 ? 1223 GLN A CG  1 
ATOM   2486 C  CD  . GLN A 1 446 ? 96.958  100.273 138.172 1.00 266.31 ? 1223 GLN A CD  1 
ATOM   2487 O  OE1 . GLN A 1 446 ? 97.279  99.590  137.199 1.00 266.71 ? 1223 GLN A OE1 1 
ATOM   2488 N  NE2 . GLN A 1 446 ? 95.694  100.477 138.518 1.00 266.11 ? 1223 GLN A NE2 1 
ATOM   2489 N  N   . CYS A 1 447 ? 101.194 100.332 139.779 1.00 262.56 ? 1224 CYS A N   1 
ATOM   2490 C  CA  . CYS A 1 447 ? 101.637 99.439  140.840 1.00 262.60 ? 1224 CYS A CA  1 
ATOM   2491 C  C   . CYS A 1 447 ? 100.607 99.435  141.961 1.00 262.44 ? 1224 CYS A C   1 
ATOM   2492 O  O   . CYS A 1 447 ? 100.142 100.497 142.387 1.00 262.51 ? 1224 CYS A O   1 
ATOM   2493 C  CB  . CYS A 1 447 ? 103.005 99.863  141.378 1.00 262.18 ? 1224 CYS A CB  1 
ATOM   2494 S  SG  . CYS A 1 447 ? 104.233 100.224 140.101 1.00 263.71 ? 1224 CYS A SG  1 
ATOM   2495 N  N   . VAL A 1 448 ? 100.253 98.240  142.434 1.00 262.47 ? 1225 VAL A N   1 
ATOM   2496 C  CA  . VAL A 1 448 ? 99.263  98.073  143.487 1.00 262.51 ? 1225 VAL A CA  1 
ATOM   2497 C  C   . VAL A 1 448 ? 99.882  97.274  144.625 1.00 262.42 ? 1225 VAL A C   1 
ATOM   2498 O  O   . VAL A 1 448 ? 100.902 96.601  144.462 1.00 262.59 ? 1225 VAL A O   1 
ATOM   2499 C  CB  . VAL A 1 448 ? 97.979  97.381  142.980 1.00 262.11 ? 1225 VAL A CB  1 
ATOM   2500 C  CG1 . VAL A 1 448 ? 97.256  98.271  141.982 1.00 261.89 ? 1225 VAL A CG1 1 
ATOM   2501 C  CG2 . VAL A 1 448 ? 98.314  96.034  142.360 1.00 262.52 ? 1225 VAL A CG2 1 
ATOM   2502 N  N   . ALA A 1 449 ? 99.247  97.363  145.795 1.00 257.34 ? 1226 ALA A N   1 
ATOM   2503 C  CA  . ALA A 1 449 ? 99.744  96.643  146.964 1.00 257.11 ? 1226 ALA A CA  1 
ATOM   2504 C  C   . ALA A 1 449 ? 99.614  95.137  146.778 1.00 257.73 ? 1226 ALA A C   1 
ATOM   2505 O  O   . ALA A 1 449 ? 100.580 94.391  146.977 1.00 257.63 ? 1226 ALA A O   1 
ATOM   2506 C  CB  . ALA A 1 449 ? 98.998  97.100  148.217 1.00 257.02 ? 1226 ALA A CB  1 
ATOM   2507 N  N   . THR A 1 450 ? 98.429  94.671  146.391 1.00 273.82 ? 1227 THR A N   1 
ATOM   2508 C  CA  . THR A 1 450 ? 98.197  93.249  146.187 1.00 274.15 ? 1227 THR A CA  1 
ATOM   2509 C  C   . THR A 1 450 ? 96.990  93.072  145.279 1.00 274.45 ? 1227 THR A C   1 
ATOM   2510 O  O   . THR A 1 450 ? 96.135  93.954  145.172 1.00 274.19 ? 1227 THR A O   1 
ATOM   2511 C  CB  . THR A 1 450 ? 97.981  92.514  147.515 1.00 274.35 ? 1227 THR A CB  1 
ATOM   2512 O  OG1 . THR A 1 450 ? 97.572  91.165  147.256 1.00 274.24 ? 1227 THR A OG1 1 
ATOM   2513 C  CG2 . THR A 1 450 ? 96.913  93.213  148.343 1.00 274.46 ? 1227 THR A CG2 1 
ATOM   2514 N  N   . CYS A 1 451 ? 96.936  91.916  144.627 1.00 292.54 ? 1228 CYS A N   1 
ATOM   2515 C  CA  . CYS A 1 451 ? 95.841  91.557  143.741 1.00 292.88 ? 1228 CYS A CA  1 
ATOM   2516 C  C   . CYS A 1 451 ? 95.555  90.070  143.880 1.00 292.94 ? 1228 CYS A C   1 
ATOM   2517 O  O   . CYS A 1 451 ? 96.475  89.278  144.117 1.00 292.81 ? 1228 CYS A O   1 
ATOM   2518 C  CB  . CYS A 1 451 ? 96.164  91.891  142.276 1.00 293.21 ? 1228 CYS A CB  1 
ATOM   2519 S  SG  . CYS A 1 451 ? 97.560  90.972  141.585 1.00 295.25 ? 1228 CYS A SG  1 
ATOM   2520 N  N   . PRO A 1 452 ? 94.284  89.660  143.744 1.00 282.88 ? 1229 PRO A N   1 
ATOM   2521 C  CA  . PRO A 1 452 ? 93.901  88.246  143.839 1.00 282.39 ? 1229 PRO A CA  1 
ATOM   2522 C  C   . PRO A 1 452 ? 94.519  87.394  142.734 1.00 282.13 ? 1229 PRO A C   1 
ATOM   2523 O  O   . PRO A 1 452 ? 94.216  87.624  141.563 1.00 282.35 ? 1229 PRO A O   1 
ATOM   2524 C  CB  . PRO A 1 452 ? 92.373  88.284  143.703 1.00 281.96 ? 1229 PRO A CB  1 
ATOM   2525 C  CG  . PRO A 1 452 ? 91.987  89.680  144.063 1.00 281.98 ? 1229 PRO A CG  1 
ATOM   2526 C  CD  . PRO A 1 452 ? 93.113  90.537  143.583 1.00 282.44 ? 1229 PRO A CD  1 
ATOM   2527 N  N   . CYS B 1 122 ? 97.799  142.974 122.294 1.00 222.50 ? 899  CYS B N   1 
ATOM   2528 C  CA  . CYS B 1 122 ? 98.896  143.126 123.242 1.00 222.14 ? 899  CYS B CA  1 
ATOM   2529 C  C   . CYS B 1 122 ? 100.233 143.241 122.519 1.00 222.57 ? 899  CYS B C   1 
ATOM   2530 O  O   . CYS B 1 122 ? 100.804 144.327 122.419 1.00 222.08 ? 899  CYS B O   1 
ATOM   2531 C  CB  . CYS B 1 122 ? 98.926  141.949 124.220 1.00 221.64 ? 899  CYS B CB  1 
ATOM   2532 S  SG  . CYS B 1 122 ? 97.818  142.128 125.637 1.00 223.92 ? 899  CYS B SG  1 
ATOM   2533 N  N   . LEU B 1 123 ? 100.729 142.112 122.017 1.00 206.48 ? 900  LEU B N   1 
ATOM   2534 C  CA  . LEU B 1 123 ? 102.000 142.058 121.309 1.00 205.61 ? 900  LEU B CA  1 
ATOM   2535 C  C   . LEU B 1 123 ? 101.811 141.314 119.996 1.00 204.24 ? 900  LEU B C   1 
ATOM   2536 O  O   . LEU B 1 123 ? 101.232 140.223 119.976 1.00 203.59 ? 900  LEU B O   1 
ATOM   2537 C  CB  . LEU B 1 123 ? 103.078 141.372 122.156 1.00 203.90 ? 900  LEU B CB  1 
ATOM   2538 C  CG  . LEU B 1 123 ? 103.755 142.228 123.229 1.00 202.69 ? 900  LEU B CG  1 
ATOM   2539 C  CD1 . LEU B 1 123 ? 102.971 142.179 124.532 1.00 201.64 ? 900  LEU B CD1 1 
ATOM   2540 C  CD2 . LEU B 1 123 ? 105.191 141.777 123.446 1.00 202.71 ? 900  LEU B CD2 1 
ATOM   2541 N  N   . ALA B 1 124 ? 102.298 141.903 118.908 1.00 179.83 ? 901  ALA B N   1 
ATOM   2542 C  CA  . ALA B 1 124 ? 102.215 141.267 117.605 1.00 178.25 ? 901  ALA B CA  1 
ATOM   2543 C  C   . ALA B 1 124 ? 103.301 140.206 117.457 1.00 178.67 ? 901  ALA B C   1 
ATOM   2544 O  O   . ALA B 1 124 ? 104.282 140.173 118.205 1.00 179.78 ? 901  ALA B O   1 
ATOM   2545 C  CB  . ALA B 1 124 ? 102.336 142.305 116.489 1.00 178.13 ? 901  ALA B CB  1 
ATOM   2546 N  N   . THR B 1 125 ? 103.113 139.328 116.474 1.00 158.62 ? 902  THR B N   1 
ATOM   2547 C  CA  . THR B 1 125 ? 104.040 138.230 116.234 1.00 157.55 ? 902  THR B CA  1 
ATOM   2548 C  C   . THR B 1 125 ? 104.177 137.991 114.739 1.00 155.14 ? 902  THR B C   1 
ATOM   2549 O  O   . THR B 1 125 ? 103.173 137.933 114.023 1.00 157.82 ? 902  THR B O   1 
ATOM   2550 C  CB  . THR B 1 125 ? 103.572 136.945 116.928 1.00 158.97 ? 902  THR B CB  1 
ATOM   2551 O  OG1 . THR B 1 125 ? 103.231 137.231 118.290 1.00 161.32 ? 902  THR B OG1 1 
ATOM   2552 C  CG2 . THR B 1 125 ? 104.668 135.891 116.895 1.00 158.84 ? 902  THR B CG2 1 
ATOM   2553 N  N   . CYS B 1 126 ? 105.416 137.853 114.277 1.00 151.59 ? 903  CYS B N   1 
ATOM   2554 C  CA  . CYS B 1 126 ? 105.718 137.489 112.898 1.00 153.15 ? 903  CYS B CA  1 
ATOM   2555 C  C   . CYS B 1 126 ? 106.290 136.079 112.896 1.00 154.02 ? 903  CYS B C   1 
ATOM   2556 O  O   . CYS B 1 126 ? 107.328 135.826 113.517 1.00 157.03 ? 903  CYS B O   1 
ATOM   2557 C  CB  . CYS B 1 126 ? 106.703 138.475 112.269 1.00 153.71 ? 903  CYS B CB  1 
ATOM   2558 S  SG  . CYS B 1 126 ? 107.014 138.200 110.509 1.00 161.22 ? 903  CYS B SG  1 
ATOM   2559 N  N   . ALA B 1 127 ? 105.616 135.166 112.204 1.00 143.13 ? 904  ALA B N   1 
ATOM   2560 C  CA  . ALA B 1 127 ? 105.968 133.753 112.214 1.00 142.90 ? 904  ALA B CA  1 
ATOM   2561 C  C   . ALA B 1 127 ? 106.432 133.319 110.831 1.00 143.92 ? 904  ALA B C   1 
ATOM   2562 O  O   . ALA B 1 127 ? 105.740 133.555 109.835 1.00 146.94 ? 904  ALA B O   1 
ATOM   2563 C  CB  . ALA B 1 127 ? 104.781 132.899 112.664 1.00 142.65 ? 904  ALA B CB  1 
ATOM   2564 N  N   . VAL B 1 128 ? 107.601 132.686 110.778 1.00 132.19 ? 905  VAL B N   1 
ATOM   2565 C  CA  . VAL B 1 128 ? 108.139 132.095 109.559 1.00 129.96 ? 905  VAL B CA  1 
ATOM   2566 C  C   . VAL B 1 128 ? 108.427 130.631 109.852 1.00 131.78 ? 905  VAL B C   1 
ATOM   2567 O  O   . VAL B 1 128 ? 109.173 130.316 110.788 1.00 138.25 ? 905  VAL B O   1 
ATOM   2568 C  CB  . VAL B 1 128 ? 109.407 132.818 109.079 1.00 127.22 ? 905  VAL B CB  1 
ATOM   2569 C  CG1 . VAL B 1 128 ? 109.891 132.223 107.767 1.00 128.11 ? 905  VAL B CG1 1 
ATOM   2570 C  CG2 . VAL B 1 128 ? 109.147 134.309 108.932 1.00 127.87 ? 905  VAL B CG2 1 
ATOM   2571 N  N   . TYR B 1 129 ? 107.840 129.738 109.059 1.00 139.02 ? 906  TYR B N   1 
ATOM   2572 C  CA  . TYR B 1 129 ? 107.965 128.309 109.306 1.00 138.21 ? 906  TYR B CA  1 
ATOM   2573 C  C   . TYR B 1 129 ? 107.761 127.556 108.001 1.00 143.20 ? 906  TYR B C   1 
ATOM   2574 O  O   . TYR B 1 129 ? 107.285 128.109 107.006 1.00 149.78 ? 906  TYR B O   1 
ATOM   2575 C  CB  . TYR B 1 129 ? 106.966 127.841 110.370 1.00 138.76 ? 906  TYR B CB  1 
ATOM   2576 C  CG  . TYR B 1 129 ? 105.566 127.612 109.846 1.00 140.26 ? 906  TYR B CG  1 
ATOM   2577 C  CD1 . TYR B 1 129 ? 104.677 128.669 109.705 1.00 141.54 ? 906  TYR B CD1 1 
ATOM   2578 C  CD2 . TYR B 1 129 ? 105.129 126.339 109.504 1.00 139.98 ? 906  TYR B CD2 1 
ATOM   2579 C  CE1 . TYR B 1 129 ? 103.397 128.467 109.230 1.00 143.03 ? 906  TYR B CE1 1 
ATOM   2580 C  CE2 . TYR B 1 129 ? 103.850 126.128 109.028 1.00 140.41 ? 906  TYR B CE2 1 
ATOM   2581 C  CZ  . TYR B 1 129 ? 102.988 127.195 108.894 1.00 143.29 ? 906  TYR B CZ  1 
ATOM   2582 O  OH  . TYR B 1 129 ? 101.713 126.989 108.421 1.00 147.34 ? 906  TYR B OH  1 
ATOM   2583 N  N   . GLY B 1 130 ? 108.129 126.275 108.021 1.00 148.08 ? 907  GLY B N   1 
ATOM   2584 C  CA  . GLY B 1 130 ? 107.900 125.406 106.885 1.00 149.83 ? 907  GLY B CA  1 
ATOM   2585 C  C   . GLY B 1 130 ? 108.691 125.825 105.657 1.00 148.46 ? 907  GLY B C   1 
ATOM   2586 O  O   . GLY B 1 130 ? 109.809 126.343 105.742 1.00 147.17 ? 907  GLY B O   1 
ATOM   2587 N  N   . ASP B 1 131 ? 108.091 125.591 104.490 1.00 169.40 ? 908  ASP B N   1 
ATOM   2588 C  CA  . ASP B 1 131 ? 108.713 125.915 103.209 1.00 170.90 ? 908  ASP B CA  1 
ATOM   2589 C  C   . ASP B 1 131 ? 108.174 127.262 102.737 1.00 169.74 ? 908  ASP B C   1 
ATOM   2590 O  O   . ASP B 1 131 ? 107.264 127.352 101.912 1.00 170.11 ? 908  ASP B O   1 
ATOM   2591 C  CB  . ASP B 1 131 ? 108.453 124.808 102.192 1.00 172.46 ? 908  ASP B CB  1 
ATOM   2592 C  CG  . ASP B 1 131 ? 109.271 123.562 102.466 1.00 173.60 ? 908  ASP B CG  1 
ATOM   2593 O  OD1 . ASP B 1 131 ? 109.954 123.517 103.511 1.00 172.96 ? 908  ASP B OD1 1 
ATOM   2594 O  OD2 . ASP B 1 131 ? 109.231 122.628 101.638 1.00 174.03 ? 908  ASP B OD2 1 
ATOM   2595 N  N   . GLY B 1 132 ? 108.757 128.326 103.278 1.00 149.94 ? 909  GLY B N   1 
ATOM   2596 C  CA  . GLY B 1 132 ? 108.396 129.674 102.877 1.00 149.11 ? 909  GLY B CA  1 
ATOM   2597 C  C   . GLY B 1 132 ? 106.994 130.106 103.248 1.00 147.28 ? 909  GLY B C   1 
ATOM   2598 O  O   . GLY B 1 132 ? 106.307 130.731 102.431 1.00 149.41 ? 909  GLY B O   1 
ATOM   2599 N  N   . HIS B 1 133 ? 106.550 129.791 104.461 1.00 140.60 ? 910  HIS B N   1 
ATOM   2600 C  CA  . HIS B 1 133 ? 105.263 130.248 104.969 1.00 139.48 ? 910  HIS B CA  1 
ATOM   2601 C  C   . HIS B 1 133 ? 105.503 131.428 105.901 1.00 140.88 ? 910  HIS B C   1 
ATOM   2602 O  O   . HIS B 1 133 ? 106.277 131.320 106.859 1.00 144.98 ? 910  HIS B O   1 
ATOM   2603 C  CB  . HIS B 1 133 ? 104.528 129.123 105.696 1.00 140.99 ? 910  HIS B CB  1 
ATOM   2604 C  CG  . HIS B 1 133 ? 104.328 127.895 104.864 1.00 142.95 ? 910  HIS B CG  1 
ATOM   2605 N  ND1 . HIS B 1 133 ? 103.157 127.640 104.184 1.00 144.47 ? 910  HIS B ND1 1 
ATOM   2606 C  CD2 . HIS B 1 133 ? 105.151 126.852 104.602 1.00 143.88 ? 910  HIS B CD2 1 
ATOM   2607 C  CE1 . HIS B 1 133 ? 103.267 126.492 103.539 1.00 145.54 ? 910  HIS B CE1 1 
ATOM   2608 N  NE2 . HIS B 1 133 ? 104.467 125.994 103.776 1.00 144.87 ? 910  HIS B NE2 1 
ATOM   2609 N  N   . TYR B 1 134 ? 104.842 132.548 105.622 1.00 132.65 ? 911  TYR B N   1 
ATOM   2610 C  CA  . TYR B 1 134 ? 105.061 133.786 106.351 1.00 132.31 ? 911  TYR B CA  1 
ATOM   2611 C  C   . TYR B 1 134 ? 103.750 134.301 106.927 1.00 133.46 ? 911  TYR B C   1 
ATOM   2612 O  O   . TYR B 1 134 ? 102.667 134.010 106.412 1.00 136.28 ? 911  TYR B O   1 
ATOM   2613 C  CB  . TYR B 1 134 ? 105.686 134.859 105.449 1.00 131.16 ? 911  TYR B CB  1 
ATOM   2614 C  CG  . TYR B 1 134 ? 107.076 134.520 104.959 1.00 134.35 ? 911  TYR B CG  1 
ATOM   2615 C  CD1 . TYR B 1 134 ? 107.267 133.634 103.907 1.00 134.84 ? 911  TYR B CD1 1 
ATOM   2616 C  CD2 . TYR B 1 134 ? 108.197 135.089 105.546 1.00 136.47 ? 911  TYR B CD2 1 
ATOM   2617 C  CE1 . TYR B 1 134 ? 108.536 133.323 103.456 1.00 134.39 ? 911  TYR B CE1 1 
ATOM   2618 C  CE2 . TYR B 1 134 ? 109.469 134.784 105.103 1.00 135.11 ? 911  TYR B CE2 1 
ATOM   2619 C  CZ  . TYR B 1 134 ? 109.632 133.901 104.058 1.00 133.60 ? 911  TYR B CZ  1 
ATOM   2620 O  OH  . TYR B 1 134 ? 110.897 133.594 103.612 1.00 133.94 ? 911  TYR B OH  1 
ATOM   2621 N  N   . LEU B 1 135 ? 103.864 135.072 108.007 1.00 131.24 ? 912  LEU B N   1 
ATOM   2622 C  CA  . LEU B 1 135 ? 102.714 135.692 108.660 1.00 131.40 ? 912  LEU B CA  1 
ATOM   2623 C  C   . LEU B 1 135 ? 103.153 137.055 109.174 1.00 133.12 ? 912  LEU B C   1 
ATOM   2624 O  O   . LEU B 1 135 ? 103.984 137.138 110.084 1.00 137.24 ? 912  LEU B O   1 
ATOM   2625 C  CB  . LEU B 1 135 ? 102.183 134.821 109.798 1.00 131.38 ? 912  LEU B CB  1 
ATOM   2626 C  CG  . LEU B 1 135 ? 100.969 135.364 110.554 1.00 133.27 ? 912  LEU B CG  1 
ATOM   2627 C  CD1 . LEU B 1 135 ? 99.847  135.712 109.589 1.00 133.60 ? 912  LEU B CD1 1 
ATOM   2628 C  CD2 . LEU B 1 135 ? 100.494 134.365 111.597 1.00 135.51 ? 912  LEU B CD2 1 
ATOM   2629 N  N   . THR B 1 136 ? 102.598 138.118 108.597 1.00 151.20 ? 913  THR B N   1 
ATOM   2630 C  CA  . THR B 1 136 ? 103.001 139.466 108.960 1.00 150.80 ? 913  THR B CA  1 
ATOM   2631 C  C   . THR B 1 136 ? 102.506 139.820 110.361 1.00 151.60 ? 913  THR B C   1 
ATOM   2632 O  O   . THR B 1 136 ? 101.693 139.116 110.966 1.00 151.89 ? 913  THR B O   1 
ATOM   2633 C  CB  . THR B 1 136 ? 102.469 140.478 107.946 1.00 153.77 ? 913  THR B CB  1 
ATOM   2634 O  OG1 . THR B 1 136 ? 101.052 140.615 108.105 1.00 155.69 ? 913  THR B OG1 1 
ATOM   2635 C  CG2 . THR B 1 136 ? 102.776 140.023 106.527 1.00 154.89 ? 913  THR B CG2 1 
ATOM   2636 N  N   . PHE B 1 137 ? 103.020 140.939 110.878 1.00 156.30 ? 914  PHE B N   1 
ATOM   2637 C  CA  . PHE B 1 137 ? 102.605 141.407 112.197 1.00 157.22 ? 914  PHE B CA  1 
ATOM   2638 C  C   . PHE B 1 137 ? 101.127 141.772 112.213 1.00 157.96 ? 914  PHE B C   1 
ATOM   2639 O  O   . PHE B 1 137 ? 100.415 141.474 113.179 1.00 157.88 ? 914  PHE B O   1 
ATOM   2640 C  CB  . PHE B 1 137 ? 103.455 142.605 112.619 1.00 156.68 ? 914  PHE B CB  1 
ATOM   2641 C  CG  . PHE B 1 137 ? 104.824 142.237 113.112 1.00 156.01 ? 914  PHE B CG  1 
ATOM   2642 C  CD1 . PHE B 1 137 ? 104.980 141.417 114.216 1.00 156.43 ? 914  PHE B CD1 1 
ATOM   2643 C  CD2 . PHE B 1 137 ? 105.955 142.713 112.472 1.00 155.36 ? 914  PHE B CD2 1 
ATOM   2644 C  CE1 . PHE B 1 137 ? 106.239 141.078 114.673 1.00 158.10 ? 914  PHE B CE1 1 
ATOM   2645 C  CE2 . PHE B 1 137 ? 107.217 142.377 112.923 1.00 155.46 ? 914  PHE B CE2 1 
ATOM   2646 C  CZ  . PHE B 1 137 ? 107.359 141.559 114.025 1.00 157.22 ? 914  PHE B CZ  1 
ATOM   2647 N  N   . ASP B 1 138 ? 100.647 142.418 111.151 1.00 182.98 ? 915  ASP B N   1 
ATOM   2648 C  CA  . ASP B 1 138 ? 99.259  142.855 111.082 1.00 183.70 ? 915  ASP B CA  1 
ATOM   2649 C  C   . ASP B 1 138 ? 98.283  141.714 110.830 1.00 183.89 ? 915  ASP B C   1 
ATOM   2650 O  O   . ASP B 1 138 ? 97.071  141.921 110.954 1.00 184.38 ? 915  ASP B O   1 
ATOM   2651 C  CB  . ASP B 1 138 ? 99.103  143.917 109.991 1.00 184.85 ? 915  ASP B CB  1 
ATOM   2652 C  CG  . ASP B 1 138 ? 100.081 145.064 110.154 1.00 184.55 ? 915  ASP B CG  1 
ATOM   2653 O  OD1 . ASP B 1 138 ? 100.334 145.471 111.307 1.00 183.91 ? 915  ASP B OD1 1 
ATOM   2654 O  OD2 . ASP B 1 138 ? 100.603 145.553 109.131 1.00 184.69 ? 915  ASP B OD2 1 
ATOM   2655 N  N   . GLY B 1 139 ? 98.771  140.525 110.484 1.00 176.01 ? 916  GLY B N   1 
ATOM   2656 C  CA  . GLY B 1 139 ? 97.926  139.366 110.274 1.00 176.17 ? 916  GLY B CA  1 
ATOM   2657 C  C   . GLY B 1 139 ? 97.902  138.843 108.855 1.00 175.57 ? 916  GLY B C   1 
ATOM   2658 O  O   . GLY B 1 139 ? 97.307  137.784 108.617 1.00 177.05 ? 916  GLY B O   1 
ATOM   2659 N  N   . GLN B 1 140 ? 98.520  139.541 107.907 1.00 164.36 ? 917  GLN B N   1 
ATOM   2660 C  CA  . GLN B 1 140 ? 98.541  139.070 106.529 1.00 163.82 ? 917  GLN B CA  1 
ATOM   2661 C  C   . GLN B 1 140 ? 99.412  137.826 106.406 1.00 166.22 ? 917  GLN B C   1 
ATOM   2662 O  O   . GLN B 1 140 ? 100.486 137.736 107.007 1.00 169.46 ? 917  GLN B O   1 
ATOM   2663 C  CB  . GLN B 1 140 ? 99.055  140.170 105.600 1.00 163.94 ? 917  GLN B CB  1 
ATOM   2664 C  CG  . GLN B 1 140 ? 99.086  139.783 104.131 1.00 165.35 ? 917  GLN B CG  1 
ATOM   2665 C  CD  . GLN B 1 140 ? 97.768  139.207 103.654 1.00 167.86 ? 917  GLN B CD  1 
ATOM   2666 O  OE1 . GLN B 1 140 ? 96.708  139.796 103.862 1.00 169.37 ? 917  GLN B OE1 1 
ATOM   2667 N  NE2 . GLN B 1 140 ? 97.829  138.047 103.009 1.00 168.55 ? 917  GLN B NE2 1 
ATOM   2668 N  N   . SER B 1 141 ? 98.940  136.858 105.624 1.00 155.63 ? 918  SER B N   1 
ATOM   2669 C  CA  . SER B 1 141 ? 99.651  135.607 105.405 1.00 154.45 ? 918  SER B CA  1 
ATOM   2670 C  C   . SER B 1 141 ? 99.842  135.383 103.913 1.00 155.17 ? 918  SER B C   1 
ATOM   2671 O  O   . SER B 1 141 ? 98.977  135.738 103.107 1.00 159.39 ? 918  SER B O   1 
ATOM   2672 C  CB  . SER B 1 141 ? 98.896  134.422 106.020 1.00 153.68 ? 918  SER B CB  1 
ATOM   2673 O  OG  . SER B 1 141 ? 97.664  134.204 105.356 1.00 154.33 ? 918  SER B OG  1 
ATOM   2674 N  N   . TYR B 1 142 ? 100.978 134.793 103.553 1.00 139.64 ? 919  TYR B N   1 
ATOM   2675 C  CA  . TYR B 1 142 ? 101.300 134.518 102.159 1.00 140.98 ? 919  TYR B CA  1 
ATOM   2676 C  C   . TYR B 1 142 ? 102.352 133.416 102.119 1.00 139.82 ? 919  TYR B C   1 
ATOM   2677 O  O   . TYR B 1 142 ? 102.728 132.851 103.150 1.00 140.71 ? 919  TYR B O   1 
ATOM   2678 C  CB  . TYR B 1 142 ? 101.781 135.782 101.440 1.00 141.38 ? 919  TYR B CB  1 
ATOM   2679 C  CG  . TYR B 1 142 ? 103.036 136.387 102.027 1.00 141.22 ? 919  TYR B CG  1 
ATOM   2680 C  CD1 . TYR B 1 142 ? 102.971 137.262 103.104 1.00 140.51 ? 919  TYR B CD1 1 
ATOM   2681 C  CD2 . TYR B 1 142 ? 104.286 136.087 101.503 1.00 141.97 ? 919  TYR B CD2 1 
ATOM   2682 C  CE1 . TYR B 1 142 ? 104.115 137.817 103.643 1.00 139.02 ? 919  TYR B CE1 1 
ATOM   2683 C  CE2 . TYR B 1 142 ? 105.435 136.638 102.035 1.00 141.14 ? 919  TYR B CE2 1 
ATOM   2684 C  CZ  . TYR B 1 142 ? 105.344 137.502 103.105 1.00 138.79 ? 919  TYR B CZ  1 
ATOM   2685 O  OH  . TYR B 1 142 ? 106.485 138.053 103.638 1.00 141.32 ? 919  TYR B OH  1 
ATOM   2686 N  N   . SER B 1 143 ? 102.825 133.114 100.912 1.00 131.43 ? 920  SER B N   1 
ATOM   2687 C  CA  . SER B 1 143 ? 103.845 132.096 100.708 1.00 131.93 ? 920  SER B CA  1 
ATOM   2688 C  C   . SER B 1 143 ? 104.820 132.567 99.641  1.00 132.61 ? 920  SER B C   1 
ATOM   2689 O  O   . SER B 1 143 ? 104.410 133.120 98.616  1.00 134.68 ? 920  SER B O   1 
ATOM   2690 C  CB  . SER B 1 143 ? 103.224 130.755 100.299 1.00 132.11 ? 920  SER B CB  1 
ATOM   2691 O  OG  . SER B 1 143 ? 102.342 130.277 101.299 1.00 131.70 ? 920  SER B OG  1 
ATOM   2692 N  N   . PHE B 1 144 ? 106.109 132.343 99.886  1.00 145.95 ? 921  PHE B N   1 
ATOM   2693 C  CA  . PHE B 1 144 ? 107.148 132.756 98.955  1.00 146.02 ? 921  PHE B CA  1 
ATOM   2694 C  C   . PHE B 1 144 ? 108.397 131.927 99.214  1.00 144.83 ? 921  PHE B C   1 
ATOM   2695 O  O   . PHE B 1 144 ? 108.759 131.687 100.368 1.00 146.64 ? 921  PHE B O   1 
ATOM   2696 C  CB  . PHE B 1 144 ? 107.457 134.252 99.095  1.00 147.01 ? 921  PHE B CB  1 
ATOM   2697 C  CG  . PHE B 1 144 ? 108.868 134.619 98.732  1.00 147.07 ? 921  PHE B CG  1 
ATOM   2698 C  CD1 . PHE B 1 144 ? 109.272 134.646 97.408  1.00 149.72 ? 921  PHE B CD1 1 
ATOM   2699 C  CD2 . PHE B 1 144 ? 109.789 134.941 99.714  1.00 147.13 ? 921  PHE B CD2 1 
ATOM   2700 C  CE1 . PHE B 1 144 ? 110.569 134.983 97.071  1.00 150.18 ? 921  PHE B CE1 1 
ATOM   2701 C  CE2 . PHE B 1 144 ? 111.087 135.279 99.383  1.00 149.49 ? 921  PHE B CE2 1 
ATOM   2702 C  CZ  . PHE B 1 144 ? 111.477 135.301 98.060  1.00 150.29 ? 921  PHE B CZ  1 
ATOM   2703 N  N   . ASN B 1 145 ? 109.050 131.499 98.136  1.00 146.12 ? 922  ASN B N   1 
ATOM   2704 C  CA  . ASN B 1 145 ? 110.260 130.694 98.218  1.00 146.39 ? 922  ASN B CA  1 
ATOM   2705 C  C   . ASN B 1 145 ? 111.373 131.359 97.423  1.00 148.33 ? 922  ASN B C   1 
ATOM   2706 O  O   . ASN B 1 145 ? 111.145 131.862 96.319  1.00 148.34 ? 922  ASN B O   1 
ATOM   2707 C  CB  . ASN B 1 145 ? 110.020 129.273 97.694  1.00 147.18 ? 922  ASN B CB  1 
ATOM   2708 C  CG  . ASN B 1 145 ? 109.352 129.260 96.334  1.00 150.99 ? 922  ASN B CG  1 
ATOM   2709 O  OD1 . ASN B 1 145 ? 108.750 130.249 95.916  1.00 152.60 ? 922  ASN B OD1 1 
ATOM   2710 N  ND2 . ASN B 1 145 ? 109.456 128.136 95.635  1.00 151.64 ? 922  ASN B ND2 1 
ATOM   2711 N  N   . GLY B 1 146 ? 112.576 131.356 97.991  1.00 154.26 ? 923  GLY B N   1 
ATOM   2712 C  CA  . GLY B 1 146 ? 113.728 131.945 97.332  1.00 153.59 ? 923  GLY B CA  1 
ATOM   2713 C  C   . GLY B 1 146 ? 115.007 131.353 97.876  1.00 154.44 ? 923  GLY B C   1 
ATOM   2714 O  O   . GLY B 1 146 ? 115.018 130.669 98.902  1.00 155.42 ? 923  GLY B O   1 
ATOM   2715 N  N   . ASP B 1 147 ? 116.104 131.630 97.164  1.00 183.98 ? 924  ASP B N   1 
ATOM   2716 C  CA  . ASP B 1 147 ? 117.433 131.122 97.520  1.00 186.10 ? 924  ASP B CA  1 
ATOM   2717 C  C   . ASP B 1 147 ? 118.397 132.306 97.558  1.00 185.68 ? 924  ASP B C   1 
ATOM   2718 O  O   . ASP B 1 147 ? 119.108 132.575 96.587  1.00 185.76 ? 924  ASP B O   1 
ATOM   2719 C  CB  . ASP B 1 147 ? 117.886 130.046 96.529  1.00 187.46 ? 924  ASP B CB  1 
ATOM   2720 C  CG  . ASP B 1 147 ? 119.159 129.346 96.966  1.00 188.25 ? 924  ASP B CG  1 
ATOM   2721 O  OD1 . ASP B 1 147 ? 119.663 129.645 98.069  1.00 187.76 ? 924  ASP B OD1 1 
ATOM   2722 O  OD2 . ASP B 1 147 ? 119.659 128.492 96.203  1.00 188.41 ? 924  ASP B OD2 1 
ATOM   2723 N  N   . CYS B 1 148 ? 118.427 132.994 98.693  1.00 191.88 ? 925  CYS B N   1 
ATOM   2724 C  CA  . CYS B 1 148 ? 119.313 134.132 98.928  1.00 192.30 ? 925  CYS B CA  1 
ATOM   2725 C  C   . CYS B 1 148 ? 119.174 134.530 100.393 1.00 191.83 ? 925  CYS B C   1 
ATOM   2726 O  O   . CYS B 1 148 ? 118.510 133.843 101.179 1.00 191.50 ? 925  CYS B O   1 
ATOM   2727 C  CB  . CYS B 1 148 ? 118.991 135.301 97.994  1.00 193.58 ? 925  CYS B CB  1 
ATOM   2728 S  SG  . CYS B 1 148 ? 120.225 136.620 98.022  1.00 200.41 ? 925  CYS B SG  1 
ATOM   2729 N  N   . GLU B 1 149 ? 119.804 135.640 100.763 1.00 186.12 ? 926  GLU B N   1 
ATOM   2730 C  CA  . GLU B 1 149 ? 119.660 136.206 102.096 1.00 186.00 ? 926  GLU B CA  1 
ATOM   2731 C  C   . GLU B 1 149 ? 118.571 137.270 102.074 1.00 185.73 ? 926  GLU B C   1 
ATOM   2732 O  O   . GLU B 1 149 ? 118.625 138.207 101.271 1.00 187.12 ? 926  GLU B O   1 
ATOM   2733 C  CB  . GLU B 1 149 ? 120.981 136.807 102.577 1.00 187.67 ? 926  GLU B CB  1 
ATOM   2734 C  CG  . GLU B 1 149 ? 122.152 135.837 102.559 1.00 189.17 ? 926  GLU B CG  1 
ATOM   2735 C  CD  . GLU B 1 149 ? 122.089 134.819 103.682 1.00 189.48 ? 926  GLU B CD  1 
ATOM   2736 O  OE1 . GLU B 1 149 ? 121.306 135.023 104.633 1.00 189.11 ? 926  GLU B OE1 1 
ATOM   2737 O  OE2 . GLU B 1 149 ? 122.827 133.814 103.613 1.00 190.17 ? 926  GLU B OE2 1 
ATOM   2738 N  N   . TYR B 1 150 ? 117.583 137.121 102.952 1.00 161.90 ? 927  TYR B N   1 
ATOM   2739 C  CA  . TYR B 1 150 ? 116.447 138.029 103.018 1.00 161.97 ? 927  TYR B CA  1 
ATOM   2740 C  C   . TYR B 1 150 ? 116.344 138.625 104.414 1.00 162.49 ? 927  TYR B C   1 
ATOM   2741 O  O   . TYR B 1 150 ? 116.502 137.919 105.415 1.00 162.32 ? 927  TYR B O   1 
ATOM   2742 C  CB  . TYR B 1 150 ? 115.144 137.310 102.654 1.00 161.32 ? 927  TYR B CB  1 
ATOM   2743 C  CG  . TYR B 1 150 ? 115.158 136.679 101.280 1.00 161.73 ? 927  TYR B CG  1 
ATOM   2744 C  CD1 . TYR B 1 150 ? 115.644 135.393 101.090 1.00 164.11 ? 927  TYR B CD1 1 
ATOM   2745 C  CD2 . TYR B 1 150 ? 114.689 137.372 100.172 1.00 162.20 ? 927  TYR B CD2 1 
ATOM   2746 C  CE1 . TYR B 1 150 ? 115.660 134.813 99.836  1.00 164.93 ? 927  TYR B CE1 1 
ATOM   2747 C  CE2 . TYR B 1 150 ? 114.701 136.800 98.913  1.00 163.37 ? 927  TYR B CE2 1 
ATOM   2748 C  CZ  . TYR B 1 150 ? 115.188 135.520 98.752  1.00 163.68 ? 927  TYR B CZ  1 
ATOM   2749 O  OH  . TYR B 1 150 ? 115.203 134.946 97.501  1.00 163.86 ? 927  TYR B OH  1 
ATOM   2750 N  N   . THR B 1 151 ? 116.077 139.926 104.474 1.00 157.83 ? 928  THR B N   1 
ATOM   2751 C  CA  . THR B 1 151 ? 115.972 140.643 105.738 1.00 156.80 ? 928  THR B CA  1 
ATOM   2752 C  C   . THR B 1 151 ? 114.537 140.568 106.243 1.00 157.81 ? 928  THR B C   1 
ATOM   2753 O  O   . THR B 1 151 ? 113.609 141.019 105.563 1.00 159.63 ? 928  THR B O   1 
ATOM   2754 C  CB  . THR B 1 151 ? 116.405 142.099 105.572 1.00 158.28 ? 928  THR B CB  1 
ATOM   2755 O  OG1 . THR B 1 151 ? 117.764 142.148 105.121 1.00 160.78 ? 928  THR B OG1 1 
ATOM   2756 C  CG2 . THR B 1 151 ? 116.288 142.842 106.894 1.00 159.21 ? 928  THR B CG2 1 
ATOM   2757 N  N   . LEU B 1 152 ? 114.357 140.000 107.436 1.00 146.05 ? 929  LEU B N   1 
ATOM   2758 C  CA  . LEU B 1 152 ? 113.024 139.889 108.018 1.00 145.06 ? 929  LEU B CA  1 
ATOM   2759 C  C   . LEU B 1 152 ? 112.571 141.217 108.616 1.00 146.01 ? 929  LEU B C   1 
ATOM   2760 O  O   . LEU B 1 152 ? 111.562 141.790 108.193 1.00 147.95 ? 929  LEU B O   1 
ATOM   2761 C  CB  . LEU B 1 152 ? 113.004 138.787 109.080 1.00 142.85 ? 929  LEU B CB  1 
ATOM   2762 C  CG  . LEU B 1 152 ? 112.680 137.374 108.592 1.00 142.04 ? 929  LEU B CG  1 
ATOM   2763 C  CD1 . LEU B 1 152 ? 112.488 136.434 109.771 1.00 144.18 ? 929  LEU B CD1 1 
ATOM   2764 C  CD2 . LEU B 1 152 ? 111.447 137.382 107.704 1.00 143.54 ? 929  LEU B CD2 1 
ATOM   2765 N  N   . VAL B 1 153 ? 113.310 141.719 109.602 1.00 158.09 ? 930  VAL B N   1 
ATOM   2766 C  CA  . VAL B 1 153 ? 112.988 142.970 110.278 1.00 158.96 ? 930  VAL B CA  1 
ATOM   2767 C  C   . VAL B 1 153 ? 114.234 143.844 110.285 1.00 161.97 ? 930  VAL B C   1 
ATOM   2768 O  O   . VAL B 1 153 ? 115.299 143.410 110.737 1.00 163.29 ? 930  VAL B O   1 
ATOM   2769 C  CB  . VAL B 1 153 ? 112.484 142.729 111.713 1.00 157.91 ? 930  VAL B CB  1 
ATOM   2770 C  CG1 . VAL B 1 153 ? 112.617 143.993 112.547 1.00 160.53 ? 930  VAL B CG1 1 
ATOM   2771 C  CG2 . VAL B 1 153 ? 111.042 142.248 111.693 1.00 157.87 ? 930  VAL B CG2 1 
ATOM   2772 N  N   . GLN B 1 154 ? 114.101 145.069 109.783 1.00 186.68 ? 931  GLN B N   1 
ATOM   2773 C  CA  . GLN B 1 154 ? 115.199 146.025 109.747 1.00 187.02 ? 931  GLN B CA  1 
ATOM   2774 C  C   . GLN B 1 154 ? 114.750 147.318 110.408 1.00 187.30 ? 931  GLN B C   1 
ATOM   2775 O  O   . GLN B 1 154 ? 113.682 147.846 110.084 1.00 186.80 ? 931  GLN B O   1 
ATOM   2776 C  CB  . GLN B 1 154 ? 115.659 146.289 108.307 1.00 186.80 ? 931  GLN B CB  1 
ATOM   2777 C  CG  . GLN B 1 154 ? 116.725 147.366 108.174 1.00 188.13 ? 931  GLN B CG  1 
ATOM   2778 C  CD  . GLN B 1 154 ? 116.144 148.733 107.868 1.00 191.01 ? 931  GLN B CD  1 
ATOM   2779 O  OE1 . GLN B 1 154 ? 114.949 148.867 107.604 1.00 193.15 ? 931  GLN B OE1 1 
ATOM   2780 N  NE2 . GLN B 1 154 ? 116.988 149.757 107.903 1.00 191.41 ? 931  GLN B NE2 1 
ATOM   2781 N  N   . ASN B 1 155 ? 115.563 147.821 111.330 1.00 206.81 ? 932  ASN B N   1 
ATOM   2782 C  CA  . ASN B 1 155 ? 115.259 149.051 112.043 1.00 207.52 ? 932  ASN B CA  1 
ATOM   2783 C  C   . ASN B 1 155 ? 115.827 150.253 111.299 1.00 209.04 ? 932  ASN B C   1 
ATOM   2784 O  O   . ASN B 1 155 ? 116.831 150.151 110.589 1.00 210.27 ? 932  ASN B O   1 
ATOM   2785 C  CB  . ASN B 1 155 ? 115.824 149.005 113.464 1.00 208.73 ? 932  ASN B CB  1 
ATOM   2786 C  CG  . ASN B 1 155 ? 115.358 150.170 114.316 1.00 209.14 ? 932  ASN B CG  1 
ATOM   2787 O  OD1 . ASN B 1 155 ? 114.439 150.899 113.943 1.00 208.77 ? 932  ASN B OD1 1 
ATOM   2788 N  ND2 . ASN B 1 155 ? 115.997 150.355 115.465 1.00 209.48 ? 932  ASN B ND2 1 
ATOM   2789 N  N   . HIS B 1 156 ? 115.165 151.400 111.472 1.00 223.92 ? 933  HIS B N   1 
ATOM   2790 C  CA  . HIS B 1 156 ? 115.592 152.675 110.895 1.00 224.52 ? 933  HIS B CA  1 
ATOM   2791 C  C   . HIS B 1 156 ? 115.689 152.577 109.369 1.00 224.88 ? 933  HIS B C   1 
ATOM   2792 O  O   . HIS B 1 156 ? 116.764 152.651 108.770 1.00 224.52 ? 933  HIS B O   1 
ATOM   2793 C  CB  . HIS B 1 156 ? 116.919 153.136 111.510 1.00 224.79 ? 933  HIS B CB  1 
ATOM   2794 C  CG  . HIS B 1 156 ? 116.768 153.775 112.855 1.00 225.73 ? 933  HIS B CG  1 
ATOM   2795 N  ND1 . HIS B 1 156 ? 117.840 154.252 113.577 1.00 225.65 ? 933  HIS B ND1 1 
ATOM   2796 C  CD2 . HIS B 1 156 ? 115.669 154.016 113.609 1.00 226.16 ? 933  HIS B CD2 1 
ATOM   2797 C  CE1 . HIS B 1 156 ? 117.409 154.760 114.718 1.00 226.61 ? 933  HIS B CE1 1 
ATOM   2798 N  NE2 . HIS B 1 156 ? 116.095 154.629 114.762 1.00 226.97 ? 933  HIS B NE2 1 
ATOM   2799 N  N   . CYS B 1 157 ? 114.520 152.390 108.760 1.00 234.43 ? 934  CYS B N   1 
ATOM   2800 C  CA  . CYS B 1 157 ? 114.431 152.314 107.308 1.00 234.89 ? 934  CYS B CA  1 
ATOM   2801 C  C   . CYS B 1 157 ? 114.961 153.595 106.676 1.00 235.31 ? 934  CYS B C   1 
ATOM   2802 O  O   . CYS B 1 157 ? 114.609 154.701 107.094 1.00 235.99 ? 934  CYS B O   1 
ATOM   2803 C  CB  . CYS B 1 157 ? 112.984 152.072 106.881 1.00 235.09 ? 934  CYS B CB  1 
ATOM   2804 S  SG  . CYS B 1 157 ? 112.165 150.721 107.758 1.00 239.14 ? 934  CYS B SG  1 
ATOM   2805 N  N   . GLY B 1 158 ? 115.810 153.440 105.664 1.00 238.94 ? 935  GLY B N   1 
ATOM   2806 C  CA  . GLY B 1 158 ? 116.417 154.600 105.047 1.00 239.32 ? 935  GLY B CA  1 
ATOM   2807 C  C   . GLY B 1 158 ? 117.483 155.218 105.941 1.00 240.32 ? 935  GLY B C   1 
ATOM   2808 O  O   . GLY B 1 158 ? 118.062 154.574 106.819 1.00 240.43 ? 935  GLY B O   1 
ATOM   2809 N  N   . GLY B 1 159 ? 117.736 156.501 105.699 1.00 245.82 ? 936  GLY B N   1 
ATOM   2810 C  CA  . GLY B 1 159 ? 118.719 157.249 106.451 1.00 245.74 ? 936  GLY B CA  1 
ATOM   2811 C  C   . GLY B 1 159 ? 118.218 157.893 107.722 1.00 245.39 ? 936  GLY B C   1 
ATOM   2812 O  O   . GLY B 1 159 ? 118.971 158.627 108.369 1.00 245.11 ? 936  GLY B O   1 
ATOM   2813 N  N   . LYS B 1 160 ? 116.970 157.642 108.107 1.00 245.32 ? 937  LYS B N   1 
ATOM   2814 C  CA  . LYS B 1 160 ? 116.398 158.255 109.299 1.00 245.46 ? 937  LYS B CA  1 
ATOM   2815 C  C   . LYS B 1 160 ? 116.839 157.484 110.537 1.00 245.88 ? 937  LYS B C   1 
ATOM   2816 O  O   . LYS B 1 160 ? 116.447 156.328 110.729 1.00 245.76 ? 937  LYS B O   1 
ATOM   2817 C  CB  . LYS B 1 160 ? 114.874 158.291 109.199 1.00 245.24 ? 937  LYS B CB  1 
ATOM   2818 C  CG  . LYS B 1 160 ? 114.175 158.758 110.467 1.00 245.22 ? 937  LYS B CG  1 
ATOM   2819 C  CD  . LYS B 1 160 ? 114.692 160.114 110.923 1.00 244.94 ? 937  LYS B CD  1 
ATOM   2820 C  CE  . LYS B 1 160 ? 114.123 160.492 112.280 1.00 245.04 ? 937  LYS B CE  1 
ATOM   2821 N  NZ  . LYS B 1 160 ? 115.047 161.377 113.042 1.00 244.56 ? 937  LYS B NZ  1 
ATOM   2822 N  N   . ASP B 1 161 ? 117.654 158.122 111.373 1.00 253.35 ? 938  ASP B N   1 
ATOM   2823 C  CA  . ASP B 1 161 ? 118.117 157.550 112.635 1.00 253.35 ? 938  ASP B CA  1 
ATOM   2824 C  C   . ASP B 1 161 ? 117.472 158.344 113.767 1.00 253.17 ? 938  ASP B C   1 
ATOM   2825 O  O   . ASP B 1 161 ? 117.885 159.469 114.062 1.00 253.05 ? 938  ASP B O   1 
ATOM   2826 C  CB  . ASP B 1 161 ? 119.641 157.582 112.726 1.00 253.07 ? 938  ASP B CB  1 
ATOM   2827 C  CG  . ASP B 1 161 ? 120.310 156.840 111.585 1.00 253.06 ? 938  ASP B CG  1 
ATOM   2828 O  OD1 . ASP B 1 161 ? 119.593 156.237 110.759 1.00 252.71 ? 938  ASP B OD1 1 
ATOM   2829 O  OD2 . ASP B 1 161 ? 121.557 156.860 111.513 1.00 253.25 ? 938  ASP B OD2 1 
ATOM   2830 N  N   . SER B 1 162 ? 116.458 157.754 114.399 1.00 262.60 ? 939  SER B N   1 
ATOM   2831 C  CA  . SER B 1 162 ? 115.728 158.436 115.461 1.00 263.24 ? 939  SER B CA  1 
ATOM   2832 C  C   . SER B 1 162 ? 116.357 158.179 116.825 1.00 263.91 ? 939  SER B C   1 
ATOM   2833 O  O   . SER B 1 162 ? 115.656 157.812 117.774 1.00 264.04 ? 939  SER B O   1 
ATOM   2834 C  CB  . SER B 1 162 ? 114.262 157.998 115.464 1.00 262.43 ? 939  SER B CB  1 
ATOM   2835 O  OG  . SER B 1 162 ? 113.542 158.635 116.506 1.00 262.85 ? 939  SER B OG  1 
ATOM   2836 N  N   . THR B 1 163 ? 117.671 158.384 116.929 1.00 258.37 ? 940  THR B N   1 
ATOM   2837 C  CA  . THR B 1 163 ? 118.413 158.247 118.184 1.00 257.79 ? 940  THR B CA  1 
ATOM   2838 C  C   . THR B 1 163 ? 118.171 156.885 118.834 1.00 257.74 ? 940  THR B C   1 
ATOM   2839 O  O   . THR B 1 163 ? 117.984 156.767 120.047 1.00 257.25 ? 940  THR B O   1 
ATOM   2840 C  CB  . THR B 1 163 ? 118.070 159.381 119.153 1.00 257.56 ? 940  THR B CB  1 
ATOM   2841 O  OG1 . THR B 1 163 ? 116.727 159.222 119.628 1.00 257.87 ? 940  THR B OG1 1 
ATOM   2842 C  CG2 . THR B 1 163 ? 118.202 160.731 118.462 1.00 257.19 ? 940  THR B CG2 1 
ATOM   2843 N  N   . GLN B 1 164 ? 118.173 155.842 118.006 1.00 244.25 ? 941  GLN B N   1 
ATOM   2844 C  CA  . GLN B 1 164 ? 117.977 154.482 118.487 1.00 243.13 ? 941  GLN B CA  1 
ATOM   2845 C  C   . GLN B 1 164 ? 118.967 153.559 117.794 1.00 242.47 ? 941  GLN B C   1 
ATOM   2846 O  O   . GLN B 1 164 ? 119.482 153.872 116.717 1.00 242.39 ? 941  GLN B O   1 
ATOM   2847 C  CB  . GLN B 1 164 ? 116.543 153.990 118.247 1.00 243.04 ? 941  GLN B CB  1 
ATOM   2848 C  CG  . GLN B 1 164 ? 115.470 154.816 118.937 1.00 243.00 ? 941  GLN B CG  1 
ATOM   2849 C  CD  . GLN B 1 164 ? 114.068 154.369 118.571 1.00 242.81 ? 941  GLN B CD  1 
ATOM   2850 O  OE1 . GLN B 1 164 ? 113.886 153.403 117.831 1.00 242.26 ? 941  GLN B OE1 1 
ATOM   2851 N  NE2 . GLN B 1 164 ? 113.069 155.073 119.090 1.00 242.85 ? 941  GLN B NE2 1 
ATOM   2852 N  N   . ASP B 1 165 ? 119.233 152.421 118.427 1.00 233.70 ? 942  ASP B N   1 
ATOM   2853 C  CA  . ASP B 1 165 ? 120.099 151.419 117.825 1.00 234.30 ? 942  ASP B CA  1 
ATOM   2854 C  C   . ASP B 1 165 ? 119.360 150.697 116.705 1.00 234.79 ? 942  ASP B C   1 
ATOM   2855 O  O   . ASP B 1 165 ? 118.158 150.434 116.799 1.00 234.65 ? 942  ASP B O   1 
ATOM   2856 C  CB  . ASP B 1 165 ? 120.573 150.420 118.880 1.00 234.07 ? 942  ASP B CB  1 
ATOM   2857 C  CG  . ASP B 1 165 ? 121.503 149.362 118.311 1.00 234.70 ? 942  ASP B CG  1 
ATOM   2858 O  OD1 . ASP B 1 165 ? 122.066 149.582 117.218 1.00 235.36 ? 942  ASP B OD1 1 
ATOM   2859 O  OD2 . ASP B 1 165 ? 121.671 148.309 118.960 1.00 234.11 ? 942  ASP B OD2 1 
ATOM   2860 N  N   . SER B 1 166 ? 120.087 150.375 115.640 1.00 217.56 ? 943  SER B N   1 
ATOM   2861 C  CA  . SER B 1 166 ? 119.520 149.716 114.471 1.00 215.95 ? 943  SER B CA  1 
ATOM   2862 C  C   . SER B 1 166 ? 119.799 148.221 114.554 1.00 214.99 ? 943  SER B C   1 
ATOM   2863 O  O   . SER B 1 166 ? 120.958 147.806 114.660 1.00 214.23 ? 943  SER B O   1 
ATOM   2864 C  CB  . SER B 1 166 ? 120.097 150.301 113.183 1.00 215.28 ? 943  SER B CB  1 
ATOM   2865 O  OG  . SER B 1 166 ? 121.496 150.497 113.295 1.00 214.83 ? 943  SER B OG  1 
ATOM   2866 N  N   . PHE B 1 167 ? 118.739 147.419 114.506 1.00 188.19 ? 944  PHE B N   1 
ATOM   2867 C  CA  . PHE B 1 167 ? 118.846 145.968 114.519 1.00 186.63 ? 944  PHE B CA  1 
ATOM   2868 C  C   . PHE B 1 167 ? 118.423 145.412 113.167 1.00 185.96 ? 944  PHE B C   1 
ATOM   2869 O  O   . PHE B 1 167 ? 117.495 145.927 112.535 1.00 186.00 ? 944  PHE B O   1 
ATOM   2870 C  CB  . PHE B 1 167 ? 117.989 145.356 115.633 1.00 186.58 ? 944  PHE B CB  1 
ATOM   2871 C  CG  . PHE B 1 167 ? 116.609 145.942 115.733 1.00 186.45 ? 944  PHE B CG  1 
ATOM   2872 C  CD1 . PHE B 1 167 ? 115.574 145.451 114.953 1.00 186.34 ? 944  PHE B CD1 1 
ATOM   2873 C  CD2 . PHE B 1 167 ? 116.342 146.976 116.614 1.00 187.93 ? 944  PHE B CD2 1 
ATOM   2874 C  CE1 . PHE B 1 167 ? 114.304 145.985 115.045 1.00 186.98 ? 944  PHE B CE1 1 
ATOM   2875 C  CE2 . PHE B 1 167 ? 115.073 147.514 116.710 1.00 188.44 ? 944  PHE B CE2 1 
ATOM   2876 C  CZ  . PHE B 1 167 ? 114.053 147.018 115.925 1.00 187.53 ? 944  PHE B CZ  1 
ATOM   2877 N  N   . ARG B 1 168 ? 119.113 144.364 112.723 1.00 174.60 ? 945  ARG B N   1 
ATOM   2878 C  CA  . ARG B 1 168 ? 118.849 143.751 111.427 1.00 173.24 ? 945  ARG B CA  1 
ATOM   2879 C  C   . ARG B 1 168 ? 118.969 142.243 111.566 1.00 174.29 ? 945  ARG B C   1 
ATOM   2880 O  O   . ARG B 1 168 ? 120.007 141.740 112.005 1.00 176.11 ? 945  ARG B O   1 
ATOM   2881 C  CB  . ARG B 1 168 ? 119.819 144.274 110.363 1.00 174.12 ? 945  ARG B CB  1 
ATOM   2882 C  CG  . ARG B 1 168 ? 119.695 143.587 109.014 1.00 174.62 ? 945  ARG B CG  1 
ATOM   2883 C  CD  . ARG B 1 168 ? 120.490 144.323 107.950 1.00 175.17 ? 945  ARG B CD  1 
ATOM   2884 N  NE  . ARG B 1 168 ? 121.784 144.771 108.451 1.00 176.64 ? 945  ARG B NE  1 
ATOM   2885 C  CZ  . ARG B 1 168 ? 122.897 144.052 108.398 1.00 175.98 ? 945  ARG B CZ  1 
ATOM   2886 N  NH1 . ARG B 1 168 ? 122.913 142.841 107.867 1.00 175.62 ? 945  ARG B NH1 1 
ATOM   2887 N  NH2 . ARG B 1 168 ? 124.023 144.563 108.889 1.00 174.36 ? 945  ARG B NH2 1 
ATOM   2888 N  N   . VAL B 1 169 ? 117.911 141.527 111.193 1.00 153.36 ? 946  VAL B N   1 
ATOM   2889 C  CA  . VAL B 1 169 ? 117.879 140.071 111.237 1.00 152.67 ? 946  VAL B CA  1 
ATOM   2890 C  C   . VAL B 1 169 ? 117.669 139.555 109.821 1.00 151.72 ? 946  VAL B C   1 
ATOM   2891 O  O   . VAL B 1 169 ? 116.749 139.997 109.124 1.00 154.02 ? 946  VAL B O   1 
ATOM   2892 C  CB  . VAL B 1 169 ? 116.779 139.551 112.180 1.00 150.46 ? 946  VAL B CB  1 
ATOM   2893 C  CG1 . VAL B 1 169 ? 117.268 139.563 113.618 1.00 151.42 ? 946  VAL B CG1 1 
ATOM   2894 C  CG2 . VAL B 1 169 ? 115.518 140.389 112.041 1.00 150.13 ? 946  VAL B CG2 1 
ATOM   2895 N  N   . VAL B 1 170 ? 118.525 138.628 109.397 1.00 139.56 ? 947  VAL B N   1 
ATOM   2896 C  CA  . VAL B 1 170 ? 118.452 138.048 108.064 1.00 139.33 ? 947  VAL B CA  1 
ATOM   2897 C  C   . VAL B 1 170 ? 118.423 136.532 108.187 1.00 141.76 ? 947  VAL B C   1 
ATOM   2898 O  O   . VAL B 1 170 ? 118.912 135.958 109.164 1.00 142.34 ? 947  VAL B O   1 
ATOM   2899 C  CB  . VAL B 1 170 ? 119.629 138.498 107.171 1.00 140.47 ? 947  VAL B CB  1 
ATOM   2900 C  CG1 . VAL B 1 170 ? 119.571 139.998 106.931 1.00 140.96 ? 947  VAL B CG1 1 
ATOM   2901 C  CG2 . VAL B 1 170 ? 120.954 138.107 107.802 1.00 142.37 ? 947  VAL B CG2 1 
ATOM   2902 N  N   . THR B 1 171 ? 117.839 135.885 107.182 1.00 166.69 ? 948  THR B N   1 
ATOM   2903 C  CA  . THR B 1 171 ? 117.723 134.436 107.137 1.00 167.14 ? 948  THR B CA  1 
ATOM   2904 C  C   . THR B 1 171 ? 118.378 133.903 105.871 1.00 168.60 ? 948  THR B C   1 
ATOM   2905 O  O   . THR B 1 171 ? 118.365 134.555 104.823 1.00 171.74 ? 948  THR B O   1 
ATOM   2906 C  CB  . THR B 1 171 ? 116.257 133.982 107.182 1.00 167.16 ? 948  THR B CB  1 
ATOM   2907 O  OG1 . THR B 1 171 ? 115.708 134.005 105.858 1.00 166.84 ? 948  THR B OG1 1 
ATOM   2908 C  CG2 . THR B 1 171 ? 115.438 134.894 108.080 1.00 168.56 ? 948  THR B CG2 1 
ATOM   2909 N  N   . GLU B 1 172 ? 118.950 132.708 105.978 1.00 170.08 ? 949  GLU B N   1 
ATOM   2910 C  CA  . GLU B 1 172 ? 119.580 132.028 104.854 1.00 169.40 ? 949  GLU B CA  1 
ATOM   2911 C  C   . GLU B 1 172 ? 118.706 130.850 104.446 1.00 169.39 ? 949  GLU B C   1 
ATOM   2912 O  O   . GLU B 1 172 ? 118.385 129.994 105.277 1.00 170.12 ? 949  GLU B O   1 
ATOM   2913 C  CB  . GLU B 1 172 ? 120.988 131.555 105.216 1.00 171.07 ? 949  GLU B CB  1 
ATOM   2914 C  CG  . GLU B 1 172 ? 121.685 130.784 104.107 1.00 172.94 ? 949  GLU B CG  1 
ATOM   2915 C  CD  . GLU B 1 172 ? 123.097 130.378 104.477 1.00 175.31 ? 949  GLU B CD  1 
ATOM   2916 O  OE1 . GLU B 1 172 ? 123.534 130.699 105.603 1.00 175.77 ? 949  GLU B OE1 1 
ATOM   2917 O  OE2 . GLU B 1 172 ? 123.772 129.740 103.643 1.00 175.24 ? 949  GLU B OE2 1 
ATOM   2918 N  N   . ASN B 1 173 ? 118.324 130.811 103.174 1.00 170.39 ? 950  ASN B N   1 
ATOM   2919 C  CA  . ASN B 1 173 ? 117.471 129.762 102.638 1.00 172.42 ? 950  ASN B CA  1 
ATOM   2920 C  C   . ASN B 1 173 ? 118.253 128.915 101.645 1.00 172.48 ? 950  ASN B C   1 
ATOM   2921 O  O   . ASN B 1 173 ? 119.009 129.442 100.823 1.00 172.68 ? 950  ASN B O   1 
ATOM   2922 C  CB  . ASN B 1 173 ? 116.233 130.354 101.958 1.00 172.73 ? 950  ASN B CB  1 
ATOM   2923 C  CG  . ASN B 1 173 ? 115.315 131.061 102.935 1.00 172.65 ? 950  ASN B CG  1 
ATOM   2924 O  OD1 . ASN B 1 173 ? 115.619 131.171 104.122 1.00 173.72 ? 950  ASN B OD1 1 
ATOM   2925 N  ND2 . ASN B 1 173 ? 114.182 131.544 102.438 1.00 171.02 ? 950  ASN B ND2 1 
ATOM   2926 N  N   . VAL B 1 174 ? 118.068 127.601 101.727 1.00 167.98 ? 951  VAL B N   1 
ATOM   2927 C  CA  . VAL B 1 174 ? 118.735 126.663 100.828 1.00 166.60 ? 951  VAL B CA  1 
ATOM   2928 C  C   . VAL B 1 174 ? 117.685 125.737 100.226 1.00 166.62 ? 951  VAL B C   1 
ATOM   2929 O  O   . VAL B 1 174 ? 116.665 125.457 100.872 1.00 168.25 ? 951  VAL B O   1 
ATOM   2930 C  CB  . VAL B 1 174 ? 119.827 125.868 101.561 1.00 168.06 ? 951  VAL B CB  1 
ATOM   2931 C  CG1 . VAL B 1 174 ? 121.025 126.758 101.854 1.00 168.51 ? 951  VAL B CG1 1 
ATOM   2932 C  CG2 . VAL B 1 174 ? 119.275 125.268 102.845 1.00 168.84 ? 951  VAL B CG2 1 
ATOM   2933 N  N   . PRO B 1 175 ? 117.881 125.244 99.001  1.00 159.43 ? 952  PRO B N   1 
ATOM   2934 C  CA  . PRO B 1 175 ? 116.880 124.353 98.400  1.00 160.25 ? 952  PRO B CA  1 
ATOM   2935 C  C   . PRO B 1 175 ? 116.843 122.987 99.066  1.00 161.96 ? 952  PRO B C   1 
ATOM   2936 O  O   . PRO B 1 175 ? 117.768 122.184 98.911  1.00 162.68 ? 952  PRO B O   1 
ATOM   2937 C  CB  . PRO B 1 175 ? 117.331 124.255 96.937  1.00 159.36 ? 952  PRO B CB  1 
ATOM   2938 C  CG  . PRO B 1 175 ? 118.793 124.544 96.973  1.00 158.64 ? 952  PRO B CG  1 
ATOM   2939 C  CD  . PRO B 1 175 ? 118.993 125.538 98.080  1.00 159.43 ? 952  PRO B CD  1 
ATOM   2940 N  N   . CYS B 1 176 ? 115.775 122.715 99.810  1.00 185.78 ? 953  CYS B N   1 
ATOM   2941 C  CA  . CYS B 1 176 ? 115.580 121.437 100.483 1.00 185.13 ? 953  CYS B CA  1 
ATOM   2942 C  C   . CYS B 1 176 ? 114.489 120.664 99.755  1.00 185.13 ? 953  CYS B C   1 
ATOM   2943 O  O   . CYS B 1 176 ? 113.367 121.158 99.606  1.00 185.51 ? 953  CYS B O   1 
ATOM   2944 C  CB  . CYS B 1 176 ? 115.212 121.640 101.953 1.00 185.88 ? 953  CYS B CB  1 
ATOM   2945 S  SG  . CYS B 1 176 ? 114.077 123.013 102.263 1.00 192.60 ? 953  CYS B SG  1 
ATOM   2946 N  N   . GLY B 1 177 ? 114.821 119.457 99.306  1.00 182.03 ? 954  GLY B N   1 
ATOM   2947 C  CA  . GLY B 1 177 ? 113.882 118.643 98.561  1.00 181.90 ? 954  GLY B CA  1 
ATOM   2948 C  C   . GLY B 1 177 ? 114.251 118.516 97.098  1.00 181.64 ? 954  GLY B C   1 
ATOM   2949 O  O   . GLY B 1 177 ? 115.422 118.654 96.733  1.00 183.04 ? 954  GLY B O   1 
ATOM   2950 N  N   . THR B 1 178 ? 113.260 118.252 96.249  1.00 176.12 ? 955  THR B N   1 
ATOM   2951 C  CA  . THR B 1 178 ? 113.487 118.118 94.815  1.00 177.25 ? 955  THR B CA  1 
ATOM   2952 C  C   . THR B 1 178 ? 112.518 118.912 93.953  1.00 177.34 ? 955  THR B C   1 
ATOM   2953 O  O   . THR B 1 178 ? 112.841 119.178 92.790  1.00 177.10 ? 955  THR B O   1 
ATOM   2954 C  CB  . THR B 1 178 ? 113.421 116.642 94.393  1.00 178.50 ? 955  THR B CB  1 
ATOM   2955 O  OG1 . THR B 1 178 ? 113.628 116.537 92.979  1.00 179.07 ? 955  THR B OG1 1 
ATOM   2956 C  CG2 . THR B 1 178 ? 112.068 116.044 94.750  1.00 177.16 ? 955  THR B CG2 1 
ATOM   2957 N  N   . THR B 1 179 ? 111.348 119.296 94.471  1.00 177.70 ? 956  THR B N   1 
ATOM   2958 C  CA  . THR B 1 179 ? 110.408 120.076 93.673  1.00 178.13 ? 956  THR B CA  1 
ATOM   2959 C  C   . THR B 1 179 ? 110.941 121.478 93.406  1.00 177.75 ? 956  THR B C   1 
ATOM   2960 O  O   . THR B 1 179 ? 110.788 122.007 92.298  1.00 178.22 ? 956  THR B O   1 
ATOM   2961 C  CB  . THR B 1 179 ? 109.052 120.142 94.376  1.00 178.00 ? 956  THR B CB  1 
ATOM   2962 O  OG1 . THR B 1 179 ? 108.586 118.813 94.641  1.00 177.62 ? 956  THR B OG1 1 
ATOM   2963 C  CG2 . THR B 1 179 ? 108.033 120.864 93.507  1.00 177.83 ? 956  THR B CG2 1 
ATOM   2964 N  N   . GLY B 1 180 ? 111.575 122.091 94.402  1.00 165.63 ? 957  GLY B N   1 
ATOM   2965 C  CA  . GLY B 1 180 ? 112.108 123.430 94.248  1.00 164.84 ? 957  GLY B CA  1 
ATOM   2966 C  C   . GLY B 1 180 ? 111.841 124.315 95.447  1.00 166.82 ? 957  GLY B C   1 
ATOM   2967 O  O   . GLY B 1 180 ? 112.175 125.503 95.438  1.00 168.89 ? 957  GLY B O   1 
ATOM   2968 N  N   . THR B 1 181 ? 111.237 123.746 96.487  1.00 174.79 ? 958  THR B N   1 
ATOM   2969 C  CA  . THR B 1 181 ? 110.948 124.504 97.693  1.00 174.58 ? 958  THR B CA  1 
ATOM   2970 C  C   . THR B 1 181 ? 112.233 124.806 98.459  1.00 174.59 ? 958  THR B C   1 
ATOM   2971 O  O   . THR B 1 181 ? 113.241 124.104 98.343  1.00 175.89 ? 958  THR B O   1 
ATOM   2972 C  CB  . THR B 1 181 ? 109.975 123.739 98.590  1.00 173.90 ? 958  THR B CB  1 
ATOM   2973 O  OG1 . THR B 1 181 ? 110.534 122.463 98.926  1.00 173.93 ? 958  THR B OG1 1 
ATOM   2974 C  CG2 . THR B 1 181 ? 108.646 123.533 97.879  1.00 175.31 ? 958  THR B CG2 1 
ATOM   2975 N  N   . THR B 1 182 ? 112.184 125.873 99.252  1.00 177.15 ? 959  THR B N   1 
ATOM   2976 C  CA  . THR B 1 182 ? 113.324 126.314 100.041 1.00 179.08 ? 959  THR B CA  1 
ATOM   2977 C  C   . THR B 1 182 ? 112.905 126.498 101.492 1.00 178.44 ? 959  THR B C   1 
ATOM   2978 O  O   . THR B 1 182 ? 111.775 126.898 101.785 1.00 179.05 ? 959  THR B O   1 
ATOM   2979 C  CB  . THR B 1 182 ? 113.911 127.627 99.504  1.00 179.04 ? 959  THR B CB  1 
ATOM   2980 O  OG1 . THR B 1 182 ? 112.852 128.561 99.258  1.00 178.80 ? 959  THR B OG1 1 
ATOM   2981 C  CG2 . THR B 1 182 ? 114.672 127.380 98.211  1.00 178.81 ? 959  THR B CG2 1 
ATOM   2982 N  N   . CYS B 1 183 ? 113.832 126.200 102.399 1.00 179.76 ? 960  CYS B N   1 
ATOM   2983 C  CA  . CYS B 1 183 ? 113.602 126.326 103.829 1.00 178.39 ? 960  CYS B CA  1 
ATOM   2984 C  C   . CYS B 1 183 ? 114.784 127.034 104.475 1.00 179.55 ? 960  CYS B C   1 
ATOM   2985 O  O   . CYS B 1 183 ? 115.915 126.960 103.988 1.00 180.76 ? 960  CYS B O   1 
ATOM   2986 C  CB  . CYS B 1 183 ? 113.387 124.957 104.487 1.00 180.54 ? 960  CYS B CB  1 
ATOM   2987 S  SG  . CYS B 1 183 ? 114.647 123.728 104.076 1.00 188.10 ? 960  CYS B SG  1 
ATOM   2988 N  N   . SER B 1 184 ? 114.507 127.726 105.578 1.00 161.92 ? 961  SER B N   1 
ATOM   2989 C  CA  . SER B 1 184 ? 115.550 128.456 106.285 1.00 161.66 ? 961  SER B CA  1 
ATOM   2990 C  C   . SER B 1 184 ? 116.547 127.493 106.917 1.00 161.16 ? 961  SER B C   1 
ATOM   2991 O  O   . SER B 1 184 ? 116.172 126.445 107.451 1.00 160.38 ? 961  SER B O   1 
ATOM   2992 C  CB  . SER B 1 184 ? 114.934 129.353 107.358 1.00 160.18 ? 961  SER B CB  1 
ATOM   2993 O  OG  . SER B 1 184 ? 115.886 129.679 108.355 1.00 160.59 ? 961  SER B OG  1 
ATOM   2994 N  N   . LYS B 1 185 ? 117.826 127.856 106.855 1.00 155.67 ? 962  LYS B N   1 
ATOM   2995 C  CA  . LYS B 1 185 ? 118.897 127.040 107.414 1.00 154.73 ? 962  LYS B CA  1 
ATOM   2996 C  C   . LYS B 1 185 ? 119.666 127.758 108.510 1.00 155.42 ? 962  LYS B C   1 
ATOM   2997 O  O   . LYS B 1 185 ? 119.895 127.181 109.580 1.00 155.55 ? 962  LYS B O   1 
ATOM   2998 C  CB  . LYS B 1 185 ? 119.860 126.600 106.300 1.00 153.68 ? 962  LYS B CB  1 
ATOM   2999 C  CG  . LYS B 1 185 ? 121.013 125.737 106.785 1.00 153.77 ? 962  LYS B CG  1 
ATOM   3000 C  CD  . LYS B 1 185 ? 122.062 125.556 105.700 1.00 155.44 ? 962  LYS B CD  1 
ATOM   3001 C  CE  . LYS B 1 185 ? 122.816 126.850 105.441 1.00 156.60 ? 962  LYS B CE  1 
ATOM   3002 N  NZ  . LYS B 1 185 ? 124.248 126.601 105.118 1.00 155.75 ? 962  LYS B NZ  1 
ATOM   3003 N  N   . ALA B 1 186 ? 120.074 129.004 108.277 1.00 156.65 ? 963  ALA B N   1 
ATOM   3004 C  CA  . ALA B 1 186 ? 120.831 129.774 109.251 1.00 154.86 ? 963  ALA B CA  1 
ATOM   3005 C  C   . ALA B 1 186 ? 120.224 131.161 109.394 1.00 154.67 ? 963  ALA B C   1 
ATOM   3006 O  O   . ALA B 1 186 ? 119.631 131.697 108.454 1.00 157.12 ? 963  ALA B O   1 
ATOM   3007 C  CB  . ALA B 1 186 ? 122.308 129.889 108.852 1.00 155.34 ? 963  ALA B CB  1 
ATOM   3008 N  N   . ILE B 1 187 ? 120.378 131.736 110.583 1.00 139.85 ? 964  ILE B N   1 
ATOM   3009 C  CA  . ILE B 1 187 ? 119.846 133.056 110.901 1.00 140.53 ? 964  ILE B CA  1 
ATOM   3010 C  C   . ILE B 1 187 ? 120.968 133.899 111.487 1.00 144.22 ? 964  ILE B C   1 
ATOM   3011 O  O   . ILE B 1 187 ? 121.645 133.469 112.428 1.00 145.99 ? 964  ILE B O   1 
ATOM   3012 C  CB  . ILE B 1 187 ? 118.661 132.973 111.882 1.00 137.18 ? 964  ILE B CB  1 
ATOM   3013 C  CG1 . ILE B 1 187 ? 117.437 132.375 111.187 1.00 138.80 ? 964  ILE B CG1 1 
ATOM   3014 C  CG2 . ILE B 1 187 ? 118.336 134.346 112.448 1.00 139.44 ? 964  ILE B CG2 1 
ATOM   3015 C  CD1 . ILE B 1 187 ? 116.218 132.291 112.072 1.00 139.96 ? 964  ILE B CD1 1 
ATOM   3016 N  N   . LYS B 1 188 ? 121.163 135.092 110.934 1.00 155.99 ? 965  LYS B N   1 
ATOM   3017 C  CA  . LYS B 1 188 ? 122.175 136.026 111.406 1.00 154.98 ? 965  LYS B CA  1 
ATOM   3018 C  C   . LYS B 1 188 ? 121.502 137.256 112.000 1.00 154.85 ? 965  LYS B C   1 
ATOM   3019 O  O   . LYS B 1 188 ? 120.562 137.804 111.416 1.00 155.26 ? 965  LYS B O   1 
ATOM   3020 C  CB  . LYS B 1 188 ? 123.116 136.439 110.272 1.00 154.90 ? 965  LYS B CB  1 
ATOM   3021 C  CG  . LYS B 1 188 ? 123.900 135.288 109.666 1.00 154.30 ? 965  LYS B CG  1 
ATOM   3022 C  CD  . LYS B 1 188 ? 124.533 135.689 108.344 1.00 155.39 ? 965  LYS B CD  1 
ATOM   3023 C  CE  . LYS B 1 188 ? 125.696 134.777 107.990 1.00 156.53 ? 965  LYS B CE  1 
ATOM   3024 N  NZ  . LYS B 1 188 ? 125.233 133.482 107.421 1.00 156.30 ? 965  LYS B NZ  1 
ATOM   3025 N  N   . ILE B 1 189 ? 121.988 137.684 113.162 1.00 164.03 ? 966  ILE B N   1 
ATOM   3026 C  CA  . ILE B 1 189 ? 121.447 138.835 113.876 1.00 163.88 ? 966  ILE B CA  1 
ATOM   3027 C  C   . ILE B 1 189 ? 122.527 139.903 113.953 1.00 166.23 ? 966  ILE B C   1 
ATOM   3028 O  O   . ILE B 1 189 ? 123.656 139.624 114.374 1.00 168.69 ? 966  ILE B O   1 
ATOM   3029 C  CB  . ILE B 1 189 ? 120.957 138.452 115.284 1.00 163.03 ? 966  ILE B CB  1 
ATOM   3030 C  CG1 . ILE B 1 189 ? 120.075 137.204 115.221 1.00 164.76 ? 966  ILE B CG1 1 
ATOM   3031 C  CG2 . ILE B 1 189 ? 120.207 139.612 115.919 1.00 162.64 ? 966  ILE B CG2 1 
ATOM   3032 C  CD1 . ILE B 1 189 ? 119.419 136.852 116.538 1.00 166.07 ? 966  ILE B CD1 1 
ATOM   3033 N  N   . PHE B 1 190 ? 122.180 141.124 113.549 1.00 173.04 ? 967  PHE B N   1 
ATOM   3034 C  CA  . PHE B 1 190 ? 123.100 142.254 113.573 1.00 172.97 ? 967  PHE B CA  1 
ATOM   3035 C  C   . PHE B 1 190 ? 122.488 143.366 114.408 1.00 173.76 ? 967  PHE B C   1 
ATOM   3036 O  O   . PHE B 1 190 ? 121.407 143.866 114.082 1.00 174.48 ? 967  PHE B O   1 
ATOM   3037 C  CB  . PHE B 1 190 ? 123.401 142.754 112.157 1.00 171.49 ? 967  PHE B CB  1 
ATOM   3038 C  CG  . PHE B 1 190 ? 124.075 141.737 111.283 1.00 172.31 ? 967  PHE B CG  1 
ATOM   3039 C  CD1 . PHE B 1 190 ? 125.456 141.652 111.234 1.00 172.56 ? 967  PHE B CD1 1 
ATOM   3040 C  CD2 . PHE B 1 190 ? 123.328 140.866 110.507 1.00 173.33 ? 967  PHE B CD2 1 
ATOM   3041 C  CE1 . PHE B 1 190 ? 126.080 140.718 110.430 1.00 174.04 ? 967  PHE B CE1 1 
ATOM   3042 C  CE2 . PHE B 1 190 ? 123.946 139.929 109.701 1.00 173.45 ? 967  PHE B CE2 1 
ATOM   3043 C  CZ  . PHE B 1 190 ? 125.323 139.855 109.663 1.00 173.58 ? 967  PHE B CZ  1 
ATOM   3044 N  N   . LEU B 1 191 ? 123.179 143.753 115.479 1.00 176.84 ? 968  LEU B N   1 
ATOM   3045 C  CA  . LEU B 1 191 ? 122.746 144.873 116.307 1.00 176.07 ? 968  LEU B CA  1 
ATOM   3046 C  C   . LEU B 1 191 ? 123.925 145.357 117.137 1.00 176.80 ? 968  LEU B C   1 
ATOM   3047 O  O   . LEU B 1 191 ? 124.710 144.544 117.634 1.00 176.96 ? 968  LEU B O   1 
ATOM   3048 C  CB  . LEU B 1 191 ? 121.552 144.482 117.197 1.00 174.69 ? 968  LEU B CB  1 
ATOM   3049 C  CG  . LEU B 1 191 ? 121.491 143.180 118.014 1.00 173.86 ? 968  LEU B CG  1 
ATOM   3050 C  CD1 . LEU B 1 191 ? 122.479 143.130 119.174 1.00 174.03 ? 968  LEU B CD1 1 
ATOM   3051 C  CD2 . LEU B 1 191 ? 120.072 142.944 118.516 1.00 174.61 ? 968  LEU B CD2 1 
ATOM   3052 N  N   . GLY B 1 192 ? 124.061 146.676 117.255 1.00 188.93 ? 969  GLY B N   1 
ATOM   3053 C  CA  . GLY B 1 192 ? 125.131 147.261 118.048 1.00 189.67 ? 969  GLY B CA  1 
ATOM   3054 C  C   . GLY B 1 192 ? 126.520 146.826 117.640 1.00 189.26 ? 969  GLY B C   1 
ATOM   3055 O  O   . GLY B 1 192 ? 127.425 146.796 118.481 1.00 189.74 ? 969  GLY B O   1 
ATOM   3056 N  N   . GLY B 1 193 ? 126.716 146.485 116.369 1.00 192.90 ? 970  GLY B N   1 
ATOM   3057 C  CA  . GLY B 1 193 ? 127.995 145.972 115.927 1.00 193.68 ? 970  GLY B CA  1 
ATOM   3058 C  C   . GLY B 1 193 ? 128.275 144.540 116.319 1.00 193.89 ? 970  GLY B C   1 
ATOM   3059 O  O   . GLY B 1 193 ? 129.405 144.075 116.141 1.00 194.59 ? 970  GLY B O   1 
ATOM   3060 N  N   . PHE B 1 194 ? 127.285 143.827 116.846 1.00 200.09 ? 971  PHE B N   1 
ATOM   3061 C  CA  . PHE B 1 194 ? 127.440 142.444 117.277 1.00 200.70 ? 971  PHE B CA  1 
ATOM   3062 C  C   . PHE B 1 194 ? 126.774 141.523 116.266 1.00 200.71 ? 971  PHE B C   1 
ATOM   3063 O  O   . PHE B 1 194 ? 125.631 141.761 115.862 1.00 200.84 ? 971  PHE B O   1 
ATOM   3064 C  CB  . PHE B 1 194 ? 126.833 142.232 118.665 1.00 199.68 ? 971  PHE B CB  1 
ATOM   3065 C  CG  . PHE B 1 194 ? 127.540 142.981 119.757 1.00 199.24 ? 971  PHE B CG  1 
ATOM   3066 C  CD1 . PHE B 1 194 ? 128.772 142.555 120.222 1.00 200.46 ? 971  PHE B CD1 1 
ATOM   3067 C  CD2 . PHE B 1 194 ? 126.970 144.111 120.319 1.00 199.22 ? 971  PHE B CD2 1 
ATOM   3068 C  CE1 . PHE B 1 194 ? 129.424 143.243 121.228 1.00 201.09 ? 971  PHE B CE1 1 
ATOM   3069 C  CE2 . PHE B 1 194 ? 127.618 144.804 121.325 1.00 200.07 ? 971  PHE B CE2 1 
ATOM   3070 C  CZ  . PHE B 1 194 ? 128.846 144.369 121.780 1.00 201.05 ? 971  PHE B CZ  1 
ATOM   3071 N  N   . GLU B 1 195 ? 127.488 140.476 115.861 1.00 204.27 ? 972  GLU B N   1 
ATOM   3072 C  CA  . GLU B 1 195 ? 126.993 139.506 114.894 1.00 203.48 ? 972  GLU B CA  1 
ATOM   3073 C  C   . GLU B 1 195 ? 126.834 138.154 115.573 1.00 203.28 ? 972  GLU B C   1 
ATOM   3074 O  O   . GLU B 1 195 ? 127.778 137.650 116.191 1.00 204.10 ? 972  GLU B O   1 
ATOM   3075 C  CB  . GLU B 1 195 ? 127.938 139.391 113.696 1.00 204.36 ? 972  GLU B CB  1 
ATOM   3076 C  CG  . GLU B 1 195 ? 127.522 138.343 112.678 1.00 205.34 ? 972  GLU B CG  1 
ATOM   3077 C  CD  . GLU B 1 195 ? 128.615 138.044 111.671 1.00 206.31 ? 972  GLU B CD  1 
ATOM   3078 O  OE1 . GLU B 1 195 ? 129.749 138.532 111.860 1.00 206.54 ? 972  GLU B OE1 1 
ATOM   3079 O  OE2 . GLU B 1 195 ? 128.340 137.322 110.690 1.00 205.86 ? 972  GLU B OE2 1 
ATOM   3080 N  N   . LEU B 1 196 ? 125.643 137.573 115.456 1.00 174.36 ? 973  LEU B N   1 
ATOM   3081 C  CA  . LEU B 1 196 ? 125.336 136.271 116.030 1.00 173.45 ? 973  LEU B CA  1 
ATOM   3082 C  C   . LEU B 1 196 ? 124.858 135.331 114.933 1.00 173.53 ? 973  LEU B C   1 
ATOM   3083 O  O   . LEU B 1 196 ? 124.087 135.729 114.054 1.00 173.47 ? 973  LEU B O   1 
ATOM   3084 C  CB  . LEU B 1 196 ? 124.269 136.382 117.125 1.00 172.01 ? 973  LEU B CB  1 
ATOM   3085 C  CG  . LEU B 1 196 ? 124.756 136.667 118.547 1.00 173.86 ? 973  LEU B CG  1 
ATOM   3086 C  CD1 . LEU B 1 196 ? 125.193 138.116 118.697 1.00 175.41 ? 973  LEU B CD1 1 
ATOM   3087 C  CD2 . LEU B 1 196 ? 123.675 136.324 119.560 1.00 173.49 ? 973  LEU B CD2 1 
ATOM   3088 N  N   . LYS B 1 197 ? 125.317 134.084 114.989 1.00 170.85 ? 974  LYS B N   1 
ATOM   3089 C  CA  . LYS B 1 197 ? 124.960 133.067 114.012 1.00 169.43 ? 974  LYS B CA  1 
ATOM   3090 C  C   . LYS B 1 197 ? 124.289 131.895 114.714 1.00 169.36 ? 974  LYS B C   1 
ATOM   3091 O  O   . LYS B 1 197 ? 124.744 131.449 115.772 1.00 172.03 ? 974  LYS B O   1 
ATOM   3092 C  CB  . LYS B 1 197 ? 126.193 132.581 113.244 1.00 169.87 ? 974  LYS B CB  1 
ATOM   3093 C  CG  . LYS B 1 197 ? 125.872 131.830 111.962 1.00 169.34 ? 974  LYS B CG  1 
ATOM   3094 C  CD  . LYS B 1 197 ? 127.109 131.676 111.092 1.00 170.54 ? 974  LYS B CD  1 
ATOM   3095 C  CE  . LYS B 1 197 ? 126.770 131.042 109.754 1.00 171.74 ? 974  LYS B CE  1 
ATOM   3096 N  NZ  . LYS B 1 197 ? 126.277 129.646 109.909 1.00 172.80 ? 974  LYS B NZ  1 
ATOM   3097 N  N   . LEU B 1 198 ? 123.205 131.401 114.121 1.00 145.81 ? 975  LEU B N   1 
ATOM   3098 C  CA  . LEU B 1 198 ? 122.433 130.284 114.661 1.00 146.31 ? 975  LEU B CA  1 
ATOM   3099 C  C   . LEU B 1 198 ? 122.387 129.189 113.599 1.00 147.59 ? 975  LEU B C   1 
ATOM   3100 O  O   . LEU B 1 198 ? 121.516 129.192 112.725 1.00 150.96 ? 975  LEU B O   1 
ATOM   3101 C  CB  . LEU B 1 198 ? 121.031 130.732 115.068 1.00 146.49 ? 975  LEU B CB  1 
ATOM   3102 C  CG  . LEU B 1 198 ? 120.947 131.959 115.976 1.00 146.41 ? 975  LEU B CG  1 
ATOM   3103 C  CD1 . LEU B 1 198 ? 119.497 132.303 116.280 1.00 146.72 ? 975  LEU B CD1 1 
ATOM   3104 C  CD2 . LEU B 1 198 ? 121.727 131.729 117.260 1.00 148.10 ? 975  LEU B CD2 1 
ATOM   3105 N  N   . SER B 1 199 ? 123.328 128.252 113.677 1.00 154.21 ? 976  SER B N   1 
ATOM   3106 C  CA  . SER B 1 199 ? 123.410 127.143 112.739 1.00 155.87 ? 976  SER B CA  1 
ATOM   3107 C  C   . SER B 1 199 ? 123.680 125.852 113.496 1.00 156.64 ? 976  SER B C   1 
ATOM   3108 O  O   . SER B 1 199 ? 124.396 125.851 114.502 1.00 158.36 ? 976  SER B O   1 
ATOM   3109 C  CB  . SER B 1 199 ? 124.507 127.376 111.693 1.00 156.26 ? 976  SER B CB  1 
ATOM   3110 O  OG  . SER B 1 199 ? 125.795 127.247 112.269 1.00 157.58 ? 976  SER B OG  1 
ATOM   3111 N  N   . HIS B 1 200 ? 123.097 124.757 113.004 1.00 154.44 ? 977  HIS B N   1 
ATOM   3112 C  CA  . HIS B 1 200 ? 123.271 123.425 113.585 1.00 154.19 ? 977  HIS B CA  1 
ATOM   3113 C  C   . HIS B 1 200 ? 122.846 123.380 115.051 1.00 155.05 ? 977  HIS B C   1 
ATOM   3114 O  O   . HIS B 1 200 ? 123.391 122.607 115.843 1.00 156.24 ? 977  HIS B O   1 
ATOM   3115 C  CB  . HIS B 1 200 ? 124.715 122.936 113.434 1.00 154.84 ? 977  HIS B CB  1 
ATOM   3116 C  CG  . HIS B 1 200 ? 125.277 123.131 112.060 1.00 156.41 ? 977  HIS B CG  1 
ATOM   3117 N  ND1 . HIS B 1 200 ? 125.956 124.272 111.689 1.00 156.89 ? 977  HIS B ND1 1 
ATOM   3118 C  CD2 . HIS B 1 200 ? 125.260 122.331 110.968 1.00 156.57 ? 977  HIS B CD2 1 
ATOM   3119 C  CE1 . HIS B 1 200 ? 126.334 124.166 110.428 1.00 155.55 ? 977  HIS B CE1 1 
ATOM   3120 N  NE2 . HIS B 1 200 ? 125.924 122.998 109.967 1.00 155.94 ? 977  HIS B NE2 1 
ATOM   3121 N  N   . GLY B 1 201 ? 121.871 124.206 115.423 1.00 153.52 ? 978  GLY B N   1 
ATOM   3122 C  CA  . GLY B 1 201 ? 121.362 124.201 116.780 1.00 152.90 ? 978  GLY B CA  1 
ATOM   3123 C  C   . GLY B 1 201 ? 122.280 124.797 117.821 1.00 153.62 ? 978  GLY B C   1 
ATOM   3124 O  O   . GLY B 1 201 ? 122.030 124.617 119.017 1.00 154.97 ? 978  GLY B O   1 
ATOM   3125 N  N   . LYS B 1 202 ? 123.333 125.499 117.412 1.00 164.53 ? 979  LYS B N   1 
ATOM   3126 C  CA  . LYS B 1 202 ? 124.273 126.108 118.340 1.00 164.95 ? 979  LYS B CA  1 
ATOM   3127 C  C   . LYS B 1 202 ? 124.394 127.595 118.042 1.00 166.10 ? 979  LYS B C   1 
ATOM   3128 O  O   . LYS B 1 202 ? 124.122 128.053 116.929 1.00 167.01 ? 979  LYS B O   1 
ATOM   3129 C  CB  . LYS B 1 202 ? 125.656 125.444 118.267 1.00 164.04 ? 979  LYS B CB  1 
ATOM   3130 C  CG  . LYS B 1 202 ? 125.618 123.943 118.033 1.00 165.16 ? 979  LYS B CG  1 
ATOM   3131 C  CD  . LYS B 1 202 ? 127.018 123.352 118.014 1.00 166.11 ? 979  LYS B CD  1 
ATOM   3132 C  CE  . LYS B 1 202 ? 127.847 123.925 116.876 1.00 166.43 ? 979  LYS B CE  1 
ATOM   3133 N  NZ  . LYS B 1 202 ? 127.077 123.993 115.603 1.00 165.36 ? 979  LYS B NZ  1 
ATOM   3134 N  N   . VAL B 1 203 ? 124.810 128.347 119.057 1.00 164.55 ? 980  VAL B N   1 
ATOM   3135 C  CA  . VAL B 1 203 ? 124.982 129.792 118.954 1.00 163.65 ? 980  VAL B CA  1 
ATOM   3136 C  C   . VAL B 1 203 ? 126.465 130.096 118.816 1.00 165.02 ? 980  VAL B C   1 
ATOM   3137 O  O   . VAL B 1 203 ? 127.278 129.657 119.640 1.00 166.47 ? 980  VAL B O   1 
ATOM   3138 C  CB  . VAL B 1 203 ? 124.386 130.513 120.174 1.00 162.76 ? 980  VAL B CB  1 
ATOM   3139 C  CG1 . VAL B 1 203 ? 124.377 132.017 119.947 1.00 162.73 ? 980  VAL B CG1 1 
ATOM   3140 C  CG2 . VAL B 1 203 ? 122.985 130.003 120.458 1.00 163.12 ? 980  VAL B CG2 1 
ATOM   3141 N  N   . GLU B 1 204 ? 126.820 130.846 117.775 1.00 190.15 ? 981  GLU B N   1 
ATOM   3142 C  CA  . GLU B 1 204 ? 128.197 131.252 117.532 1.00 190.48 ? 981  GLU B CA  1 
ATOM   3143 C  C   . GLU B 1 204 ? 128.243 132.762 117.361 1.00 190.88 ? 981  GLU B C   1 
ATOM   3144 O  O   . GLU B 1 204 ? 127.491 133.321 116.557 1.00 191.50 ? 981  GLU B O   1 
ATOM   3145 C  CB  . GLU B 1 204 ? 128.771 130.557 116.293 1.00 191.44 ? 981  GLU B CB  1 
ATOM   3146 C  CG  . GLU B 1 204 ? 130.168 131.018 115.915 1.00 192.74 ? 981  GLU B CG  1 
ATOM   3147 C  CD  . GLU B 1 204 ? 130.703 130.308 114.688 1.00 194.39 ? 981  GLU B CD  1 
ATOM   3148 O  OE1 . GLU B 1 204 ? 129.996 129.428 114.153 1.00 195.04 ? 981  GLU B OE1 1 
ATOM   3149 O  OE2 . GLU B 1 204 ? 131.830 130.629 114.258 1.00 194.90 ? 981  GLU B OE2 1 
ATOM   3150 N  N   . VAL B 1 205 ? 129.121 133.415 118.116 1.00 186.04 ? 982  VAL B N   1 
ATOM   3151 C  CA  . VAL B 1 205 ? 129.269 134.866 118.082 1.00 186.34 ? 982  VAL B CA  1 
ATOM   3152 C  C   . VAL B 1 205 ? 130.506 135.212 117.266 1.00 187.42 ? 982  VAL B C   1 
ATOM   3153 O  O   . VAL B 1 205 ? 131.583 134.638 117.478 1.00 188.25 ? 982  VAL B O   1 
ATOM   3154 C  CB  . VAL B 1 205 ? 129.352 135.451 119.503 1.00 185.41 ? 982  VAL B CB  1 
ATOM   3155 C  CG1 . VAL B 1 205 ? 130.358 134.679 120.348 1.00 185.97 ? 982  VAL B CG1 1 
ATOM   3156 C  CG2 . VAL B 1 205 ? 129.711 136.929 119.453 1.00 185.45 ? 982  VAL B CG2 1 
ATOM   3157 N  N   . ILE B 1 206 ? 130.351 136.138 116.321 1.00 195.94 ? 983  ILE B N   1 
ATOM   3158 C  CA  . ILE B 1 206 ? 131.454 136.563 115.468 1.00 195.88 ? 983  ILE B CA  1 
ATOM   3159 C  C   . ILE B 1 206 ? 131.770 138.026 115.749 1.00 196.41 ? 983  ILE B C   1 
ATOM   3160 O  O   . ILE B 1 206 ? 132.894 138.367 116.133 1.00 196.30 ? 983  ILE B O   1 
ATOM   3161 C  CB  . ILE B 1 206 ? 131.129 136.345 113.979 1.00 195.53 ? 983  ILE B CB  1 
ATOM   3162 C  CG1 . ILE B 1 206 ? 130.488 134.971 113.766 1.00 195.12 ? 983  ILE B CG1 1 
ATOM   3163 C  CG2 . ILE B 1 206 ? 132.384 136.491 113.133 1.00 195.75 ? 983  ILE B CG2 1 
ATOM   3164 C  CD1 . ILE B 1 206 ? 128.998 135.023 113.509 1.00 194.91 ? 983  ILE B CD1 1 
ATOM   3165 N  N   . GLY B 1 207 ? 130.782 138.897 115.559 1.00 218.38 ? 984  GLY B N   1 
ATOM   3166 C  CA  . GLY B 1 207 ? 130.967 140.311 115.815 1.00 219.78 ? 984  GLY B CA  1 
ATOM   3167 C  C   . GLY B 1 207 ? 131.120 140.625 117.288 1.00 219.85 ? 984  GLY B C   1 
ATOM   3168 O  O   . GLY B 1 207 ? 130.154 140.540 118.052 1.00 219.45 ? 984  GLY B O   1 
ATOM   3169 N  N   . THR B 1 208 ? 132.332 140.989 117.699 1.00 236.43 ? 985  THR B N   1 
ATOM   3170 C  CA  . THR B 1 208 ? 132.639 141.293 119.089 1.00 236.45 ? 985  THR B CA  1 
ATOM   3171 C  C   . THR B 1 208 ? 133.117 142.732 119.198 1.00 237.11 ? 985  THR B C   1 
ATOM   3172 O  O   . THR B 1 208 ? 133.992 143.159 118.437 1.00 236.30 ? 985  THR B O   1 
ATOM   3173 C  CB  . THR B 1 208 ? 133.704 140.342 119.643 1.00 236.51 ? 985  THR B CB  1 
ATOM   3174 O  OG1 . THR B 1 208 ? 134.903 140.460 118.867 1.00 236.56 ? 985  THR B OG1 1 
ATOM   3175 C  CG2 . THR B 1 208 ? 133.212 138.903 119.590 1.00 235.71 ? 985  THR B CG2 1 
ATOM   3176 N  N   . ASP B 1 209 ? 132.542 143.474 120.140 1.00 269.69 ? 986  ASP B N   1 
ATOM   3177 C  CA  . ASP B 1 209 ? 132.915 144.857 120.400 1.00 270.67 ? 986  ASP B CA  1 
ATOM   3178 C  C   . ASP B 1 209 ? 133.380 144.982 121.843 1.00 271.52 ? 986  ASP B C   1 
ATOM   3179 O  O   . ASP B 1 209 ? 132.668 144.571 122.766 1.00 271.02 ? 986  ASP B O   1 
ATOM   3180 C  CB  . ASP B 1 209 ? 131.743 145.806 120.133 1.00 269.99 ? 986  ASP B CB  1 
ATOM   3181 C  CG  . ASP B 1 209 ? 132.195 147.223 119.837 1.00 270.33 ? 986  ASP B CG  1 
ATOM   3182 O  OD1 . ASP B 1 209 ? 133.358 147.556 120.147 1.00 270.89 ? 986  ASP B OD1 1 
ATOM   3183 O  OD2 . ASP B 1 209 ? 131.386 148.004 119.294 1.00 269.92 ? 986  ASP B OD2 1 
ATOM   3184 N  N   . GLU B 1 210 ? 134.568 145.548 122.035 1.00 300.36 ? 987  GLU B N   1 
ATOM   3185 C  CA  . GLU B 1 210 ? 135.139 145.723 123.370 1.00 300.67 ? 987  GLU B CA  1 
ATOM   3186 C  C   . GLU B 1 210 ? 134.713 147.050 123.990 1.00 300.16 ? 987  GLU B C   1 
ATOM   3187 O  O   . GLU B 1 210 ? 135.536 147.840 124.451 1.00 299.97 ? 987  GLU B O   1 
ATOM   3188 C  CB  . GLU B 1 210 ? 136.657 145.611 123.302 1.00 300.83 ? 987  GLU B CB  1 
ATOM   3189 C  CG  . GLU B 1 210 ? 137.156 144.411 122.515 1.00 301.18 ? 987  GLU B CG  1 
ATOM   3190 C  CD  . GLU B 1 210 ? 136.892 143.097 123.223 1.00 301.35 ? 987  GLU B CD  1 
ATOM   3191 O  OE1 . GLU B 1 210 ? 136.874 143.086 124.472 1.00 301.47 ? 987  GLU B OE1 1 
ATOM   3192 O  OE2 . GLU B 1 210 ? 136.701 142.075 122.532 1.00 301.14 ? 987  GLU B OE2 1 
ATOM   3193 N  N   . SER B 1 211 ? 133.407 147.299 124.005 1.00 278.48 ? 988  SER B N   1 
ATOM   3194 C  CA  . SER B 1 211 ? 132.862 148.530 124.561 1.00 277.82 ? 988  SER B CA  1 
ATOM   3195 C  C   . SER B 1 211 ? 131.384 148.317 124.854 1.00 277.64 ? 988  SER B C   1 
ATOM   3196 O  O   . SER B 1 211 ? 130.786 147.321 124.439 1.00 277.34 ? 988  SER B O   1 
ATOM   3197 C  CB  . SER B 1 211 ? 133.068 149.714 123.610 1.00 277.66 ? 988  SER B CB  1 
ATOM   3198 O  OG  . SER B 1 211 ? 132.569 150.914 124.176 1.00 277.49 ? 988  SER B OG  1 
ATOM   3199 N  N   . GLN B 1 212 ? 130.808 149.272 125.580 1.00 275.68 ? 989  GLN B N   1 
ATOM   3200 C  CA  . GLN B 1 212 ? 129.382 149.279 125.940 1.00 275.93 ? 989  GLN B CA  1 
ATOM   3201 C  C   . GLN B 1 212 ? 129.103 148.015 126.753 1.00 275.64 ? 989  GLN B C   1 
ATOM   3202 O  O   . GLN B 1 212 ? 129.832 147.746 127.721 1.00 275.43 ? 989  GLN B O   1 
ATOM   3203 C  CB  . GLN B 1 212 ? 128.544 149.454 124.678 1.00 275.98 ? 989  GLN B CB  1 
ATOM   3204 C  CG  . GLN B 1 212 ? 127.165 150.046 124.922 1.00 276.33 ? 989  GLN B CG  1 
ATOM   3205 C  CD  . GLN B 1 212 ? 127.217 151.524 125.252 1.00 276.51 ? 989  GLN B CD  1 
ATOM   3206 O  OE1 . GLN B 1 212 ? 127.015 151.923 126.398 1.00 276.82 ? 989  GLN B OE1 1 
ATOM   3207 N  NE2 . GLN B 1 212 ? 127.487 152.346 124.244 1.00 276.32 ? 989  GLN B NE2 1 
ATOM   3208 N  N   . GLU B 1 213 ? 128.088 147.225 126.411 1.00 257.51 ? 990  GLU B N   1 
ATOM   3209 C  CA  . GLU B 1 213 ? 127.740 146.038 127.178 1.00 257.19 ? 990  GLU B CA  1 
ATOM   3210 C  C   . GLU B 1 213 ? 126.946 145.101 126.279 1.00 256.10 ? 990  GLU B C   1 
ATOM   3211 O  O   . GLU B 1 213 ? 126.176 145.559 125.431 1.00 256.06 ? 990  GLU B O   1 
ATOM   3212 C  CB  . GLU B 1 213 ? 126.935 146.410 128.431 1.00 257.00 ? 990  GLU B CB  1 
ATOM   3213 C  CG  . GLU B 1 213 ? 126.241 145.245 129.122 1.00 257.06 ? 990  GLU B CG  1 
ATOM   3214 C  CD  . GLU B 1 213 ? 127.217 144.211 129.648 1.00 257.19 ? 990  GLU B CD  1 
ATOM   3215 O  OE1 . GLU B 1 213 ? 128.328 144.598 130.069 1.00 257.35 ? 990  GLU B OE1 1 
ATOM   3216 O  OE2 . GLU B 1 213 ? 126.874 143.010 129.640 1.00 257.05 ? 990  GLU B OE2 1 
ATOM   3217 N  N   . VAL B 1 214 ? 127.145 143.799 126.463 1.00 214.52 ? 991  VAL B N   1 
ATOM   3218 C  CA  . VAL B 1 214 ? 126.445 142.787 125.675 1.00 212.23 ? 991  VAL B CA  1 
ATOM   3219 C  C   . VAL B 1 214 ? 124.950 142.910 125.943 1.00 212.16 ? 991  VAL B C   1 
ATOM   3220 O  O   . VAL B 1 214 ? 124.514 142.800 127.098 1.00 212.25 ? 991  VAL B O   1 
ATOM   3221 C  CB  . VAL B 1 214 ? 126.959 141.375 125.997 1.00 211.61 ? 991  VAL B CB  1 
ATOM   3222 C  CG1 . VAL B 1 214 ? 125.923 140.327 125.613 1.00 211.42 ? 991  VAL B CG1 1 
ATOM   3223 C  CG2 . VAL B 1 214 ? 128.277 141.116 125.285 1.00 211.78 ? 991  VAL B CG2 1 
ATOM   3224 N  N   . PRO B 1 215 ? 124.132 143.145 124.918 1.00 199.15 ? 992  PRO B N   1 
ATOM   3225 C  CA  . PRO B 1 215 ? 122.687 143.340 125.121 1.00 199.51 ? 992  PRO B CA  1 
ATOM   3226 C  C   . PRO B 1 215 ? 121.822 142.101 124.924 1.00 198.51 ? 992  PRO B C   1 
ATOM   3227 O  O   . PRO B 1 215 ? 120.597 142.218 125.035 1.00 198.39 ? 992  PRO B O   1 
ATOM   3228 C  CB  . PRO B 1 215 ? 122.362 144.386 124.051 1.00 199.55 ? 992  PRO B CB  1 
ATOM   3229 C  CG  . PRO B 1 215 ? 123.306 144.060 122.922 1.00 199.08 ? 992  PRO B CG  1 
ATOM   3230 C  CD  . PRO B 1 215 ? 124.523 143.381 123.517 1.00 198.18 ? 992  PRO B CD  1 
ATOM   3231 N  N   . TYR B 1 216 ? 122.407 140.941 124.639 1.00 197.35 ? 993  TYR B N   1 
ATOM   3232 C  CA  . TYR B 1 216 ? 121.649 139.730 124.361 1.00 197.43 ? 993  TYR B CA  1 
ATOM   3233 C  C   . TYR B 1 216 ? 121.894 138.692 125.447 1.00 197.17 ? 993  TYR B C   1 
ATOM   3234 O  O   . TYR B 1 216 ? 123.008 138.568 125.964 1.00 197.70 ? 993  TYR B O   1 
ATOM   3235 C  CB  . TYR B 1 216 ? 122.016 139.154 122.990 1.00 198.27 ? 993  TYR B CB  1 
ATOM   3236 C  CG  . TYR B 1 216 ? 123.490 138.860 122.808 1.00 198.24 ? 993  TYR B CG  1 
ATOM   3237 C  CD1 . TYR B 1 216 ? 124.021 137.626 123.157 1.00 197.61 ? 993  TYR B CD1 1 
ATOM   3238 C  CD2 . TYR B 1 216 ? 124.348 139.817 122.282 1.00 199.40 ? 993  TYR B CD2 1 
ATOM   3239 C  CE1 . TYR B 1 216 ? 125.365 137.354 122.992 1.00 198.68 ? 993  TYR B CE1 1 
ATOM   3240 C  CE2 . TYR B 1 216 ? 125.693 139.554 122.113 1.00 199.95 ? 993  TYR B CE2 1 
ATOM   3241 C  CZ  . TYR B 1 216 ? 126.197 138.321 122.469 1.00 199.96 ? 993  TYR B CZ  1 
ATOM   3242 O  OH  . TYR B 1 216 ? 127.536 138.054 122.303 1.00 199.68 ? 993  TYR B OH  1 
ATOM   3243 N  N   . THR B 1 217 ? 120.841 137.953 125.792 1.00 176.53 ? 994  THR B N   1 
ATOM   3244 C  CA  . THR B 1 217 ? 120.915 136.869 126.763 1.00 175.63 ? 994  THR B CA  1 
ATOM   3245 C  C   . THR B 1 217 ? 120.379 135.601 126.118 1.00 175.03 ? 994  THR B C   1 
ATOM   3246 O  O   . THR B 1 217 ? 119.358 135.639 125.424 1.00 175.64 ? 994  THR B O   1 
ATOM   3247 C  CB  . THR B 1 217 ? 120.118 137.195 128.031 1.00 175.67 ? 994  THR B CB  1 
ATOM   3248 O  OG1 . THR B 1 217 ? 118.740 137.392 127.694 1.00 176.90 ? 994  THR B OG1 1 
ATOM   3249 C  CG2 . THR B 1 217 ? 120.659 138.454 128.693 1.00 176.28 ? 994  THR B CG2 1 
ATOM   3250 N  N   . ILE B 1 218 ? 121.063 134.485 126.347 1.00 170.84 ? 995  ILE B N   1 
ATOM   3251 C  CA  . ILE B 1 218 ? 120.700 133.201 125.758 1.00 170.34 ? 995  ILE B CA  1 
ATOM   3252 C  C   . ILE B 1 218 ? 120.025 132.347 126.820 1.00 171.58 ? 995  ILE B C   1 
ATOM   3253 O  O   . ILE B 1 218 ? 120.580 132.137 127.906 1.00 173.51 ? 995  ILE B O   1 
ATOM   3254 C  CB  . ILE B 1 218 ? 121.932 132.486 125.178 1.00 170.78 ? 995  ILE B CB  1 
ATOM   3255 C  CG1 . ILE B 1 218 ? 122.822 133.478 124.427 1.00 171.53 ? 995  ILE B CG1 1 
ATOM   3256 C  CG2 . ILE B 1 218 ? 121.505 131.350 124.262 1.00 170.05 ? 995  ILE B CG2 1 
ATOM   3257 C  CD1 . ILE B 1 218 ? 122.156 134.108 123.223 1.00 171.30 ? 995  ILE B CD1 1 
ATOM   3258 N  N   . ARG B 1 219 ? 118.828 131.854 126.508 1.00 174.95 ? 996  ARG B N   1 
ATOM   3259 C  CA  . ARG B 1 219 ? 118.073 130.993 127.404 1.00 174.58 ? 996  ARG B CA  1 
ATOM   3260 C  C   . ARG B 1 219 ? 117.586 129.770 126.643 1.00 174.15 ? 996  ARG B C   1 
ATOM   3261 O  O   . ARG B 1 219 ? 117.363 129.820 125.431 1.00 175.73 ? 996  ARG B O   1 
ATOM   3262 C  CB  . ARG B 1 219 ? 116.877 131.730 128.025 1.00 174.14 ? 996  ARG B CB  1 
ATOM   3263 C  CG  . ARG B 1 219 ? 117.244 133.009 128.759 1.00 174.20 ? 996  ARG B CG  1 
ATOM   3264 C  CD  . ARG B 1 219 ? 116.538 133.096 130.102 1.00 173.99 ? 996  ARG B CD  1 
ATOM   3265 N  NE  . ARG B 1 219 ? 115.088 133.152 129.955 1.00 174.19 ? 996  ARG B NE  1 
ATOM   3266 C  CZ  . ARG B 1 219 ? 114.387 134.275 129.876 1.00 175.48 ? 996  ARG B CZ  1 
ATOM   3267 N  NH1 . ARG B 1 219 ? 114.972 135.460 129.927 1.00 175.96 ? 996  ARG B NH1 1 
ATOM   3268 N  NH2 . ARG B 1 219 ? 113.065 134.206 129.745 1.00 176.11 ? 996  ARG B NH2 1 
ATOM   3269 N  N   . GLN B 1 220 ? 117.425 128.666 127.368 1.00 170.09 ? 997  GLN B N   1 
ATOM   3270 C  CA  . GLN B 1 220 ? 116.971 127.397 126.804 1.00 170.26 ? 997  GLN B CA  1 
ATOM   3271 C  C   . GLN B 1 220 ? 115.721 126.966 127.566 1.00 171.01 ? 997  GLN B C   1 
ATOM   3272 O  O   . GLN B 1 220 ? 115.809 126.320 128.613 1.00 171.98 ? 997  GLN B O   1 
ATOM   3273 C  CB  . GLN B 1 220 ? 118.071 126.338 126.879 1.00 170.54 ? 997  GLN B CB  1 
ATOM   3274 C  CG  . GLN B 1 220 ? 117.696 125.008 126.247 1.00 172.49 ? 997  GLN B CG  1 
ATOM   3275 C  CD  . GLN B 1 220 ? 118.133 124.907 124.799 1.00 173.32 ? 997  GLN B CD  1 
ATOM   3276 O  OE1 . GLN B 1 220 ? 117.554 124.157 124.014 1.00 172.46 ? 997  GLN B OE1 1 
ATOM   3277 N  NE2 . GLN B 1 220 ? 119.162 125.665 124.438 1.00 173.46 ? 997  GLN B NE2 1 
ATOM   3278 N  N   . MET B 1 221 ? 114.556 127.327 127.037 1.00 171.13 ? 998  MET B N   1 
ATOM   3279 C  CA  . MET B 1 221 ? 113.273 126.986 127.637 1.00 171.62 ? 998  MET B CA  1 
ATOM   3280 C  C   . MET B 1 221 ? 112.546 126.010 126.722 1.00 172.01 ? 998  MET B C   1 
ATOM   3281 O  O   . MET B 1 221 ? 112.284 126.325 125.556 1.00 173.35 ? 998  MET B O   1 
ATOM   3282 C  CB  . MET B 1 221 ? 112.426 128.236 127.871 1.00 171.45 ? 998  MET B CB  1 
ATOM   3283 C  CG  . MET B 1 221 ? 112.984 129.175 128.926 1.00 173.01 ? 998  MET B CG  1 
ATOM   3284 S  SD  . MET B 1 221 ? 111.837 130.499 129.350 1.00 175.05 ? 998  MET B SD  1 
ATOM   3285 C  CE  . MET B 1 221 ? 111.951 131.526 127.888 1.00 174.32 ? 998  MET B CE  1 
ATOM   3286 N  N   . GLY B 1 222 ? 112.216 124.835 127.254 1.00 168.32 ? 999  GLY B N   1 
ATOM   3287 C  CA  . GLY B 1 222 ? 111.535 123.829 126.458 1.00 168.24 ? 999  GLY B CA  1 
ATOM   3288 C  C   . GLY B 1 222 ? 112.379 123.387 125.280 1.00 167.24 ? 999  GLY B C   1 
ATOM   3289 O  O   . GLY B 1 222 ? 113.573 123.096 125.409 1.00 168.21 ? 999  GLY B O   1 
ATOM   3290 N  N   . ILE B 1 223 ? 111.748 123.336 124.103 1.00 147.89 ? 1000 ILE B N   1 
ATOM   3291 C  CA  . ILE B 1 223 ? 112.453 122.964 122.879 1.00 147.84 ? 1000 ILE B CA  1 
ATOM   3292 C  C   . ILE B 1 223 ? 112.915 124.171 122.078 1.00 149.49 ? 1000 ILE B C   1 
ATOM   3293 O  O   . ILE B 1 223 ? 113.610 123.999 121.064 1.00 154.12 ? 1000 ILE B O   1 
ATOM   3294 C  CB  . ILE B 1 223 ? 111.574 122.073 121.981 1.00 148.15 ? 1000 ILE B CB  1 
ATOM   3295 C  CG1 . ILE B 1 223 ? 110.513 122.915 121.270 1.00 146.65 ? 1000 ILE B CG1 1 
ATOM   3296 C  CG2 . ILE B 1 223 ? 110.925 120.969 122.799 1.00 149.91 ? 1000 ILE B CG2 1 
ATOM   3297 C  CD1 . ILE B 1 223 ? 109.686 122.138 120.271 1.00 149.89 ? 1000 ILE B CD1 1 
ATOM   3298 N  N   . TYR B 1 224 ? 112.560 125.381 122.494 1.00 151.27 ? 1001 TYR B N   1 
ATOM   3299 C  CA  . TYR B 1 224 ? 112.931 126.586 121.770 1.00 152.04 ? 1001 TYR B CA  1 
ATOM   3300 C  C   . TYR B 1 224 ? 114.206 127.189 122.343 1.00 152.39 ? 1001 TYR B C   1 
ATOM   3301 O  O   . TYR B 1 224 ? 114.541 126.993 123.514 1.00 152.57 ? 1001 TYR B O   1 
ATOM   3302 C  CB  . TYR B 1 224 ? 111.802 127.617 121.820 1.00 151.29 ? 1001 TYR B CB  1 
ATOM   3303 C  CG  . TYR B 1 224 ? 110.560 127.204 121.066 1.00 151.51 ? 1001 TYR B CG  1 
ATOM   3304 C  CD1 . TYR B 1 224 ? 110.525 127.234 119.678 1.00 152.59 ? 1001 TYR B CD1 1 
ATOM   3305 C  CD2 . TYR B 1 224 ? 109.421 126.786 121.741 1.00 152.75 ? 1001 TYR B CD2 1 
ATOM   3306 C  CE1 . TYR B 1 224 ? 109.391 126.858 118.984 1.00 155.14 ? 1001 TYR B CE1 1 
ATOM   3307 C  CE2 . TYR B 1 224 ? 108.283 126.409 121.055 1.00 154.13 ? 1001 TYR B CE2 1 
ATOM   3308 C  CZ  . TYR B 1 224 ? 108.274 126.446 119.678 1.00 155.56 ? 1001 TYR B CZ  1 
ATOM   3309 O  OH  . TYR B 1 224 ? 107.142 126.071 118.991 1.00 156.27 ? 1001 TYR B OH  1 
ATOM   3310 N  N   . LEU B 1 225 ? 114.916 127.931 121.499 1.00 152.18 ? 1002 LEU B N   1 
ATOM   3311 C  CA  . LEU B 1 225 ? 116.138 128.636 121.879 1.00 150.32 ? 1002 LEU B CA  1 
ATOM   3312 C  C   . LEU B 1 225 ? 115.789 130.119 121.967 1.00 150.76 ? 1002 LEU B C   1 
ATOM   3313 O  O   . LEU B 1 225 ? 115.865 130.852 120.980 1.00 155.03 ? 1002 LEU B O   1 
ATOM   3314 C  CB  . LEU B 1 225 ? 117.257 128.373 120.876 1.00 150.58 ? 1002 LEU B CB  1 
ATOM   3315 C  CG  . LEU B 1 225 ? 118.610 129.020 121.169 1.00 151.39 ? 1002 LEU B CG  1 
ATOM   3316 C  CD1 . LEU B 1 225 ? 119.070 128.686 122.578 1.00 153.58 ? 1002 LEU B CD1 1 
ATOM   3317 C  CD2 . LEU B 1 225 ? 119.639 128.572 120.145 1.00 151.77 ? 1002 LEU B CD2 1 
ATOM   3318 N  N   . VAL B 1 226 ? 115.405 130.555 123.161 1.00 147.56 ? 1003 VAL B N   1 
ATOM   3319 C  CA  . VAL B 1 226 ? 114.906 131.908 123.375 1.00 148.03 ? 1003 VAL B CA  1 
ATOM   3320 C  C   . VAL B 1 226 ? 116.080 132.842 123.634 1.00 149.07 ? 1003 VAL B C   1 
ATOM   3321 O  O   . VAL B 1 226 ? 116.912 132.583 124.512 1.00 152.28 ? 1003 VAL B O   1 
ATOM   3322 C  CB  . VAL B 1 226 ? 113.908 131.945 124.543 1.00 149.53 ? 1003 VAL B CB  1 
ATOM   3323 C  CG1 . VAL B 1 226 ? 113.698 133.373 125.024 1.00 149.22 ? 1003 VAL B CG1 1 
ATOM   3324 C  CG2 . VAL B 1 226 ? 112.589 131.314 124.131 1.00 150.67 ? 1003 VAL B CG2 1 
ATOM   3325 N  N   . VAL B 1 227 ? 116.147 133.928 122.869 1.00 145.19 ? 1004 VAL B N   1 
ATOM   3326 C  CA  . VAL B 1 227 ? 117.119 134.992 123.082 1.00 144.98 ? 1004 VAL B CA  1 
ATOM   3327 C  C   . VAL B 1 227 ? 116.359 136.273 123.394 1.00 144.78 ? 1004 VAL B C   1 
ATOM   3328 O  O   . VAL B 1 227 ? 115.274 136.512 122.851 1.00 146.01 ? 1004 VAL B O   1 
ATOM   3329 C  CB  . VAL B 1 227 ? 118.051 135.178 121.865 1.00 142.79 ? 1004 VAL B CB  1 
ATOM   3330 C  CG1 . VAL B 1 227 ? 118.782 133.882 121.558 1.00 143.89 ? 1004 VAL B CG1 1 
ATOM   3331 C  CG2 . VAL B 1 227 ? 117.270 135.645 120.649 1.00 142.87 ? 1004 VAL B CG2 1 
ATOM   3332 N  N   . ASP B 1 228 ? 116.916 137.084 124.289 1.00 187.00 ? 1005 ASP B N   1 
ATOM   3333 C  CA  . ASP B 1 228 ? 116.262 138.300 124.748 1.00 188.53 ? 1005 ASP B CA  1 
ATOM   3334 C  C   . ASP B 1 228 ? 117.203 139.484 124.590 1.00 189.87 ? 1005 ASP B C   1 
ATOM   3335 O  O   . ASP B 1 228 ? 118.401 139.380 124.867 1.00 191.04 ? 1005 ASP B O   1 
ATOM   3336 C  CB  . ASP B 1 228 ? 115.819 138.176 126.211 1.00 191.42 ? 1005 ASP B CB  1 
ATOM   3337 C  CG  . ASP B 1 228 ? 114.950 139.336 126.658 1.00 191.82 ? 1005 ASP B CG  1 
ATOM   3338 O  OD1 . ASP B 1 228 ? 114.476 140.098 125.789 1.00 192.16 ? 1005 ASP B OD1 1 
ATOM   3339 O  OD2 . ASP B 1 228 ? 114.741 139.486 127.880 1.00 191.94 ? 1005 ASP B OD2 1 
ATOM   3340 N  N   . THR B 1 229 ? 116.650 140.608 124.142 1.00 192.40 ? 1006 THR B N   1 
ATOM   3341 C  CA  . THR B 1 229 ? 117.391 141.848 123.979 1.00 193.20 ? 1006 THR B CA  1 
ATOM   3342 C  C   . THR B 1 229 ? 116.754 142.940 124.827 1.00 193.34 ? 1006 THR B C   1 
ATOM   3343 O  O   . THR B 1 229 ? 115.544 142.934 125.072 1.00 193.43 ? 1006 THR B O   1 
ATOM   3344 C  CB  . THR B 1 229 ? 117.433 142.289 122.511 1.00 193.47 ? 1006 THR B CB  1 
ATOM   3345 O  OG1 . THR B 1 229 ? 116.139 142.760 122.115 1.00 193.30 ? 1006 THR B OG1 1 
ATOM   3346 C  CG2 . THR B 1 229 ? 117.844 141.130 121.614 1.00 193.55 ? 1006 THR B CG2 1 
ATOM   3347 N  N   . ASP B 1 230 ? 117.586 143.883 125.275 1.00 208.77 ? 1007 ASP B N   1 
ATOM   3348 C  CA  . ASP B 1 230 ? 117.102 144.957 126.134 1.00 209.42 ? 1007 ASP B CA  1 
ATOM   3349 C  C   . ASP B 1 230 ? 116.263 145.978 125.377 1.00 209.59 ? 1007 ASP B C   1 
ATOM   3350 O  O   . ASP B 1 230 ? 115.489 146.709 126.004 1.00 209.97 ? 1007 ASP B O   1 
ATOM   3351 C  CB  . ASP B 1 230 ? 118.280 145.657 126.813 1.00 209.81 ? 1007 ASP B CB  1 
ATOM   3352 C  CG  . ASP B 1 230 ? 119.471 145.814 125.891 1.00 210.46 ? 1007 ASP B CG  1 
ATOM   3353 O  OD1 . ASP B 1 230 ? 119.369 145.408 124.714 1.00 209.80 ? 1007 ASP B OD1 1 
ATOM   3354 O  OD2 . ASP B 1 230 ? 120.509 146.343 126.341 1.00 211.32 ? 1007 ASP B OD2 1 
ATOM   3355 N  N   . ILE B 1 231 ? 116.399 146.050 124.051 1.00 193.22 ? 1008 ILE B N   1 
ATOM   3356 C  CA  . ILE B 1 231 ? 115.632 147.027 123.284 1.00 192.78 ? 1008 ILE B CA  1 
ATOM   3357 C  C   . ILE B 1 231 ? 114.150 146.669 123.278 1.00 192.70 ? 1008 ILE B C   1 
ATOM   3358 O  O   . ILE B 1 231 ? 113.291 147.557 123.232 1.00 193.28 ? 1008 ILE B O   1 
ATOM   3359 C  CB  . ILE B 1 231 ? 116.202 147.152 121.857 1.00 191.49 ? 1008 ILE B CB  1 
ATOM   3360 C  CG1 . ILE B 1 231 ? 115.480 148.256 121.082 1.00 192.19 ? 1008 ILE B CG1 1 
ATOM   3361 C  CG2 . ILE B 1 231 ? 116.115 145.826 121.116 1.00 190.23 ? 1008 ILE B CG2 1 
ATOM   3362 C  CD1 . ILE B 1 231 ? 115.691 149.641 121.653 1.00 192.55 ? 1008 ILE B CD1 1 
ATOM   3363 N  N   . GLY B 1 232 ? 113.822 145.380 123.337 1.00 182.30 ? 1009 GLY B N   1 
ATOM   3364 C  CA  . GLY B 1 232 ? 112.436 144.958 123.359 1.00 181.92 ? 1009 GLY B CA  1 
ATOM   3365 C  C   . GLY B 1 232 ? 112.073 144.020 122.227 1.00 180.92 ? 1009 GLY B C   1 
ATOM   3366 O  O   . GLY B 1 232 ? 110.904 143.918 121.846 1.00 182.02 ? 1009 GLY B O   1 
ATOM   3367 N  N   . LEU B 1 233 ? 113.070 143.328 121.682 1.00 163.43 ? 1010 LEU B N   1 
ATOM   3368 C  CA  . LEU B 1 233 ? 112.876 142.384 120.590 1.00 162.93 ? 1010 LEU B CA  1 
ATOM   3369 C  C   . LEU B 1 233 ? 113.415 141.024 121.009 1.00 163.82 ? 1010 LEU B C   1 
ATOM   3370 O  O   . LEU B 1 233 ? 114.559 140.919 121.463 1.00 166.87 ? 1010 LEU B O   1 
ATOM   3371 C  CB  . LEU B 1 233 ? 113.566 142.879 119.313 1.00 163.21 ? 1010 LEU B CB  1 
ATOM   3372 C  CG  . LEU B 1 233 ? 113.795 141.916 118.146 1.00 161.62 ? 1010 LEU B CG  1 
ATOM   3373 C  CD1 . LEU B 1 233 ? 113.599 142.644 116.829 1.00 163.48 ? 1010 LEU B CD1 1 
ATOM   3374 C  CD2 . LEU B 1 233 ? 115.192 141.322 118.203 1.00 160.95 ? 1010 LEU B CD2 1 
ATOM   3375 N  N   . VAL B 1 234 ? 112.590 139.989 120.861 1.00 146.23 ? 1011 VAL B N   1 
ATOM   3376 C  CA  . VAL B 1 234 ? 112.960 138.631 121.234 1.00 145.86 ? 1011 VAL B CA  1 
ATOM   3377 C  C   . VAL B 1 234 ? 112.745 137.714 120.037 1.00 145.21 ? 1011 VAL B C   1 
ATOM   3378 O  O   . VAL B 1 234 ? 112.047 138.052 119.078 1.00 147.77 ? 1011 VAL B O   1 
ATOM   3379 C  CB  . VAL B 1 234 ? 112.169 138.119 122.457 1.00 144.80 ? 1011 VAL B CB  1 
ATOM   3380 C  CG1 . VAL B 1 234 ? 112.093 139.189 123.536 1.00 146.67 ? 1011 VAL B CG1 1 
ATOM   3381 C  CG2 . VAL B 1 234 ? 110.776 137.674 122.042 1.00 142.63 ? 1011 VAL B CG2 1 
ATOM   3382 N  N   . LEU B 1 235 ? 113.366 136.539 120.104 1.00 138.16 ? 1012 LEU B N   1 
ATOM   3383 C  CA  . LEU B 1 235 ? 113.264 135.537 119.054 1.00 138.21 ? 1012 LEU B CA  1 
ATOM   3384 C  C   . LEU B 1 235 ? 113.009 134.170 119.670 1.00 137.87 ? 1012 LEU B C   1 
ATOM   3385 O  O   . LEU B 1 235 ? 113.503 133.859 120.757 1.00 140.75 ? 1012 LEU B O   1 
ATOM   3386 C  CB  . LEU B 1 235 ? 114.535 135.485 118.194 1.00 137.97 ? 1012 LEU B CB  1 
ATOM   3387 C  CG  . LEU B 1 235 ? 114.817 136.676 117.278 1.00 139.50 ? 1012 LEU B CG  1 
ATOM   3388 C  CD1 . LEU B 1 235 ? 115.662 137.714 117.993 1.00 141.26 ? 1012 LEU B CD1 1 
ATOM   3389 C  CD2 . LEU B 1 235 ? 115.501 136.216 116.001 1.00 139.49 ? 1012 LEU B CD2 1 
ATOM   3390 N  N   . LEU B 1 236 ? 112.231 133.356 118.961 1.00 138.78 ? 1013 LEU B N   1 
ATOM   3391 C  CA  . LEU B 1 236 ? 111.931 131.986 119.366 1.00 137.43 ? 1013 LEU B CA  1 
ATOM   3392 C  C   . LEU B 1 236 ? 112.365 131.057 118.241 1.00 138.59 ? 1013 LEU B C   1 
ATOM   3393 O  O   . LEU B 1 236 ? 111.693 130.971 117.207 1.00 143.55 ? 1013 LEU B O   1 
ATOM   3394 C  CB  . LEU B 1 236 ? 110.445 131.815 119.680 1.00 140.00 ? 1013 LEU B CB  1 
ATOM   3395 C  CG  . LEU B 1 236 ? 109.761 132.952 120.443 1.00 142.38 ? 1013 LEU B CG  1 
ATOM   3396 C  CD1 . LEU B 1 236 ? 108.272 132.683 120.582 1.00 142.20 ? 1013 LEU B CD1 1 
ATOM   3397 C  CD2 . LEU B 1 236 ? 110.399 133.146 121.807 1.00 139.38 ? 1013 LEU B CD2 1 
ATOM   3398 N  N   . TRP B 1 237 ? 113.481 130.364 118.441 1.00 140.32 ? 1014 TRP B N   1 
ATOM   3399 C  CA  . TRP B 1 237 ? 114.062 129.488 117.434 1.00 140.89 ? 1014 TRP B CA  1 
ATOM   3400 C  C   . TRP B 1 237 ? 113.942 128.040 117.888 1.00 143.31 ? 1014 TRP B C   1 
ATOM   3401 O  O   . TRP B 1 237 ? 114.347 127.700 119.004 1.00 147.95 ? 1014 TRP B O   1 
ATOM   3402 C  CB  . TRP B 1 237 ? 115.530 129.845 117.186 1.00 140.20 ? 1014 TRP B CB  1 
ATOM   3403 C  CG  . TRP B 1 237 ? 116.106 129.226 115.952 1.00 141.71 ? 1014 TRP B CG  1 
ATOM   3404 C  CD1 . TRP B 1 237 ? 115.523 129.157 114.721 1.00 144.08 ? 1014 TRP B CD1 1 
ATOM   3405 C  CD2 . TRP B 1 237 ? 117.383 128.590 115.827 1.00 142.81 ? 1014 TRP B CD2 1 
ATOM   3406 N  NE1 . TRP B 1 237 ? 116.357 128.517 113.837 1.00 144.33 ? 1014 TRP B NE1 1 
ATOM   3407 C  CE2 . TRP B 1 237 ? 117.505 128.159 114.492 1.00 143.15 ? 1014 TRP B CE2 1 
ATOM   3408 C  CE3 . TRP B 1 237 ? 118.434 128.342 116.714 1.00 143.24 ? 1014 TRP B CE3 1 
ATOM   3409 C  CZ2 . TRP B 1 237 ? 118.636 127.494 114.023 1.00 143.02 ? 1014 TRP B CZ2 1 
ATOM   3410 C  CZ3 . TRP B 1 237 ? 119.555 127.682 116.247 1.00 144.65 ? 1014 TRP B CZ3 1 
ATOM   3411 C  CH2 . TRP B 1 237 ? 119.647 127.266 114.914 1.00 145.03 ? 1014 TRP B CH2 1 
ATOM   3412 N  N   . ASP B 1 238 ? 113.389 127.194 117.022 1.00 158.06 ? 1015 ASP B N   1 
ATOM   3413 C  CA  . ASP B 1 238 ? 113.259 125.771 117.303 1.00 158.76 ? 1015 ASP B CA  1 
ATOM   3414 C  C   . ASP B 1 238 ? 114.500 124.979 116.919 1.00 158.40 ? 1015 ASP B C   1 
ATOM   3415 O  O   . ASP B 1 238 ? 114.500 123.751 117.055 1.00 158.49 ? 1015 ASP B O   1 
ATOM   3416 C  CB  . ASP B 1 238 ? 112.039 125.194 116.577 1.00 161.42 ? 1015 ASP B CB  1 
ATOM   3417 C  CG  . ASP B 1 238 ? 112.114 125.374 115.072 1.00 164.64 ? 1015 ASP B CG  1 
ATOM   3418 O  OD1 . ASP B 1 238 ? 113.079 125.998 114.585 1.00 164.92 ? 1015 ASP B OD1 1 
ATOM   3419 O  OD2 . ASP B 1 238 ? 111.200 124.889 114.373 1.00 167.03 ? 1015 ASP B OD2 1 
ATOM   3420 N  N   . LYS B 1 239 ? 115.538 125.651 116.422 1.00 142.61 ? 1016 LYS B N   1 
ATOM   3421 C  CA  . LYS B 1 239 ? 116.820 125.089 116.007 1.00 143.37 ? 1016 LYS B CA  1 
ATOM   3422 C  C   . LYS B 1 239 ? 116.719 124.223 114.757 1.00 141.93 ? 1016 LYS B C   1 
ATOM   3423 O  O   . LYS B 1 239 ? 117.740 123.675 114.326 1.00 141.87 ? 1016 LYS B O   1 
ATOM   3424 C  CB  . LYS B 1 239 ? 117.493 124.270 117.119 1.00 141.81 ? 1016 LYS B CB  1 
ATOM   3425 C  CG  . LYS B 1 239 ? 117.665 125.021 118.428 1.00 142.38 ? 1016 LYS B CG  1 
ATOM   3426 C  CD  . LYS B 1 239 ? 118.214 124.113 119.515 1.00 140.55 ? 1016 LYS B CD  1 
ATOM   3427 C  CE  . LYS B 1 239 ? 117.092 123.460 120.306 1.00 140.99 ? 1016 LYS B CE  1 
ATOM   3428 N  NZ  . LYS B 1 239 ? 117.589 122.842 121.566 1.00 143.63 ? 1016 LYS B NZ  1 
ATOM   3429 N  N   . LYS B 1 240 ? 115.537 124.075 114.158 1.00 152.40 ? 1017 LYS B N   1 
ATOM   3430 C  CA  . LYS B 1 240 ? 115.402 123.258 112.956 1.00 153.70 ? 1017 LYS B CA  1 
ATOM   3431 C  C   . LYS B 1 240 ? 114.996 124.072 111.735 1.00 154.50 ? 1017 LYS B C   1 
ATOM   3432 O  O   . LYS B 1 240 ? 115.773 124.158 110.779 1.00 155.73 ? 1017 LYS B O   1 
ATOM   3433 C  CB  . LYS B 1 240 ? 114.393 122.129 113.204 1.00 152.83 ? 1017 LYS B CB  1 
ATOM   3434 C  CG  . LYS B 1 240 ? 114.535 121.451 114.556 1.00 154.63 ? 1017 LYS B CG  1 
ATOM   3435 C  CD  . LYS B 1 240 ? 115.204 120.093 114.423 1.00 154.24 ? 1017 LYS B CD  1 
ATOM   3436 C  CE  . LYS B 1 240 ? 114.769 119.154 115.535 1.00 155.38 ? 1017 LYS B CE  1 
ATOM   3437 N  NZ  . LYS B 1 240 ? 113.286 119.048 115.621 1.00 154.12 ? 1017 LYS B NZ  1 
ATOM   3438 N  N   . THR B 1 241 ? 113.807 124.676 111.729 1.00 149.10 ? 1018 THR B N   1 
ATOM   3439 C  CA  . THR B 1 241 ? 113.361 125.390 110.538 1.00 146.75 ? 1018 THR B CA  1 
ATOM   3440 C  C   . THR B 1 241 ? 112.732 126.744 110.852 1.00 147.89 ? 1018 THR B C   1 
ATOM   3441 O  O   . THR B 1 241 ? 113.006 127.734 110.165 1.00 148.25 ? 1018 THR B O   1 
ATOM   3442 C  CB  . THR B 1 241 ? 112.369 124.522 109.756 1.00 148.47 ? 1018 THR B CB  1 
ATOM   3443 O  OG1 . THR B 1 241 ? 113.072 123.444 109.126 1.00 151.47 ? 1018 THR B OG1 1 
ATOM   3444 C  CG2 . THR B 1 241 ? 111.653 125.339 108.690 1.00 148.57 ? 1018 THR B CG2 1 
ATOM   3445 N  N   . SER B 1 242 ? 111.913 126.808 111.897 1.00 150.49 ? 1019 SER B N   1 
ATOM   3446 C  CA  . SER B 1 242 ? 111.048 127.960 112.103 1.00 150.16 ? 1019 SER B CA  1 
ATOM   3447 C  C   . SER B 1 242 ? 111.681 128.975 113.051 1.00 148.54 ? 1019 SER B C   1 
ATOM   3448 O  O   . SER B 1 242 ? 112.651 128.695 113.758 1.00 151.14 ? 1019 SER B O   1 
ATOM   3449 C  CB  . SER B 1 242 ? 109.685 127.517 112.637 1.00 148.83 ? 1019 SER B CB  1 
ATOM   3450 O  OG  . SER B 1 242 ? 109.817 126.740 113.812 1.00 150.49 ? 1019 SER B OG  1 
ATOM   3451 N  N   . ILE B 1 243 ? 111.107 130.176 113.054 1.00 128.52 ? 1020 ILE B N   1 
ATOM   3452 C  CA  . ILE B 1 243 ? 111.566 131.272 113.901 1.00 127.79 ? 1020 ILE B CA  1 
ATOM   3453 C  C   . ILE B 1 243 ? 110.389 132.206 114.148 1.00 128.58 ? 1020 ILE B C   1 
ATOM   3454 O  O   . ILE B 1 243 ? 109.659 132.559 113.216 1.00 132.64 ? 1020 ILE B O   1 
ATOM   3455 C  CB  . ILE B 1 243 ? 112.752 132.027 113.266 1.00 125.47 ? 1020 ILE B CB  1 
ATOM   3456 C  CG1 . ILE B 1 243 ? 113.070 133.300 114.053 1.00 131.02 ? 1020 ILE B CG1 1 
ATOM   3457 C  CG2 . ILE B 1 243 ? 112.473 132.342 111.802 1.00 124.32 ? 1020 ILE B CG2 1 
ATOM   3458 C  CD1 . ILE B 1 243 ? 113.574 133.041 115.456 1.00 134.76 ? 1020 ILE B CD1 1 
ATOM   3459 N  N   . PHE B 1 244 ? 110.198 132.597 115.404 1.00 129.59 ? 1021 PHE B N   1 
ATOM   3460 C  CA  . PHE B 1 244 ? 109.120 133.493 115.797 1.00 126.26 ? 1021 PHE B CA  1 
ATOM   3461 C  C   . PHE B 1 244 ? 109.701 134.806 116.303 1.00 130.22 ? 1021 PHE B C   1 
ATOM   3462 O  O   . PHE B 1 244 ? 110.665 134.813 117.076 1.00 137.33 ? 1021 PHE B O   1 
ATOM   3463 C  CB  . PHE B 1 244 ? 108.242 132.857 116.877 1.00 127.13 ? 1021 PHE B CB  1 
ATOM   3464 C  CG  . PHE B 1 244 ? 107.478 131.653 116.406 1.00 130.90 ? 1021 PHE B CG  1 
ATOM   3465 C  CD1 . PHE B 1 244 ? 108.058 130.396 116.427 1.00 132.94 ? 1021 PHE B CD1 1 
ATOM   3466 C  CD2 . PHE B 1 244 ? 106.180 131.778 115.943 1.00 133.08 ? 1021 PHE B CD2 1 
ATOM   3467 C  CE1 . PHE B 1 244 ? 107.358 129.287 115.994 1.00 131.24 ? 1021 PHE B CE1 1 
ATOM   3468 C  CE2 . PHE B 1 244 ? 105.474 130.672 115.510 1.00 132.59 ? 1021 PHE B CE2 1 
ATOM   3469 C  CZ  . PHE B 1 244 ? 106.065 129.425 115.535 1.00 130.80 ? 1021 PHE B CZ  1 
ATOM   3470 N  N   . ILE B 1 245 ? 109.110 135.915 115.867 1.00 137.52 ? 1022 ILE B N   1 
ATOM   3471 C  CA  . ILE B 1 245 ? 109.581 137.252 116.204 1.00 137.62 ? 1022 ILE B CA  1 
ATOM   3472 C  C   . ILE B 1 245 ? 108.482 137.975 116.970 1.00 140.79 ? 1022 ILE B C   1 
ATOM   3473 O  O   . ILE B 1 245 ? 107.323 137.987 116.540 1.00 145.99 ? 1022 ILE B O   1 
ATOM   3474 C  CB  . ILE B 1 245 ? 109.980 138.049 114.949 1.00 136.93 ? 1022 ILE B CB  1 
ATOM   3475 C  CG1 . ILE B 1 245 ? 110.814 137.179 114.005 1.00 138.30 ? 1022 ILE B CG1 1 
ATOM   3476 C  CG2 . ILE B 1 245 ? 110.733 139.313 115.337 1.00 136.55 ? 1022 ILE B CG2 1 
ATOM   3477 C  CD1 . ILE B 1 245 ? 112.272 137.077 114.391 1.00 138.21 ? 1022 ILE B CD1 1 
ATOM   3478 N  N   . ASN B 1 246 ? 108.848 138.573 118.100 1.00 161.75 ? 1023 ASN B N   1 
ATOM   3479 C  CA  . ASN B 1 246 ? 107.939 139.374 118.908 1.00 162.79 ? 1023 ASN B CA  1 
ATOM   3480 C  C   . ASN B 1 246 ? 108.519 140.772 119.058 1.00 164.09 ? 1023 ASN B C   1 
ATOM   3481 O  O   . ASN B 1 246 ? 109.693 140.926 119.408 1.00 167.16 ? 1023 ASN B O   1 
ATOM   3482 C  CB  . ASN B 1 246 ? 107.712 138.739 120.282 1.00 163.95 ? 1023 ASN B CB  1 
ATOM   3483 C  CG  . ASN B 1 246 ? 106.374 138.036 120.385 1.00 165.18 ? 1023 ASN B CG  1 
ATOM   3484 O  OD1 . ASN B 1 246 ? 105.697 137.816 119.381 1.00 166.22 ? 1023 ASN B OD1 1 
ATOM   3485 N  ND2 . ASN B 1 246 ? 105.985 137.678 121.603 1.00 165.97 ? 1023 ASN B ND2 1 
ATOM   3486 N  N   . LEU B 1 247 ? 107.697 141.785 118.797 1.00 175.26 ? 1024 LEU B N   1 
ATOM   3487 C  CA  . LEU B 1 247 ? 108.131 143.174 118.817 1.00 176.76 ? 1024 LEU B CA  1 
ATOM   3488 C  C   . LEU B 1 247 ? 107.289 143.970 119.803 1.00 179.16 ? 1024 LEU B C   1 
ATOM   3489 O  O   . LEU B 1 247 ? 106.089 143.722 119.954 1.00 179.52 ? 1024 LEU B O   1 
ATOM   3490 C  CB  . LEU B 1 247 ? 108.036 143.800 117.422 1.00 177.07 ? 1024 LEU B CB  1 
ATOM   3491 C  CG  . LEU B 1 247 ? 108.742 145.143 117.228 1.00 177.65 ? 1024 LEU B CG  1 
ATOM   3492 C  CD1 . LEU B 1 247 ? 110.196 145.047 117.660 1.00 177.17 ? 1024 LEU B CD1 1 
ATOM   3493 C  CD2 . LEU B 1 247 ? 108.637 145.601 115.783 1.00 179.51 ? 1024 LEU B CD2 1 
ATOM   3494 N  N   . SER B 1 248 ? 107.927 144.927 120.472 1.00 194.47 ? 1025 SER B N   1 
ATOM   3495 C  CA  . SER B 1 248 ? 107.224 145.773 121.420 1.00 193.63 ? 1025 SER B CA  1 
ATOM   3496 C  C   . SER B 1 248 ? 106.322 146.763 120.683 1.00 193.77 ? 1025 SER B C   1 
ATOM   3497 O  O   . SER B 1 248 ? 106.604 147.142 119.543 1.00 194.00 ? 1025 SER B O   1 
ATOM   3498 C  CB  . SER B 1 248 ? 108.217 146.529 122.299 1.00 192.97 ? 1025 SER B CB  1 
ATOM   3499 O  OG  . SER B 1 248 ? 109.218 145.660 122.800 1.00 194.08 ? 1025 SER B OG  1 
ATOM   3500 N  N   . PRO B 1 249 ? 105.225 147.194 121.313 1.00 197.24 ? 1026 PRO B N   1 
ATOM   3501 C  CA  . PRO B 1 249 ? 104.339 148.170 120.656 1.00 198.08 ? 1026 PRO B CA  1 
ATOM   3502 C  C   . PRO B 1 249 ? 104.987 149.524 120.421 1.00 197.97 ? 1026 PRO B C   1 
ATOM   3503 O  O   . PRO B 1 249 ? 104.461 150.308 119.621 1.00 197.35 ? 1026 PRO B O   1 
ATOM   3504 C  CB  . PRO B 1 249 ? 103.154 148.284 121.626 1.00 197.74 ? 1026 PRO B CB  1 
ATOM   3505 C  CG  . PRO B 1 249 ? 103.228 147.057 122.482 1.00 197.05 ? 1026 PRO B CG  1 
ATOM   3506 C  CD  . PRO B 1 249 ? 104.683 146.736 122.602 1.00 196.45 ? 1026 PRO B CD  1 
ATOM   3507 N  N   . GLU B 1 250 ? 106.102 149.826 121.092 1.00 211.00 ? 1027 GLU B N   1 
ATOM   3508 C  CA  . GLU B 1 250 ? 106.749 151.122 120.912 1.00 211.84 ? 1027 GLU B CA  1 
ATOM   3509 C  C   . GLU B 1 250 ? 107.290 151.296 119.498 1.00 211.77 ? 1027 GLU B C   1 
ATOM   3510 O  O   . GLU B 1 250 ? 107.434 152.430 119.027 1.00 212.91 ? 1027 GLU B O   1 
ATOM   3511 C  CB  . GLU B 1 250 ? 107.873 151.292 121.934 1.00 212.54 ? 1027 GLU B CB  1 
ATOM   3512 C  CG  . GLU B 1 250 ? 108.357 152.723 122.096 1.00 213.26 ? 1027 GLU B CG  1 
ATOM   3513 C  CD  . GLU B 1 250 ? 109.856 152.854 121.914 1.00 213.03 ? 1027 GLU B CD  1 
ATOM   3514 O  OE1 . GLU B 1 250 ? 110.450 151.996 121.228 1.00 213.03 ? 1027 GLU B OE1 1 
ATOM   3515 O  OE2 . GLU B 1 250 ? 110.441 153.815 122.456 1.00 212.17 ? 1027 GLU B OE2 1 
ATOM   3516 N  N   . PHE B 1 251 ? 107.589 150.195 118.806 1.00 193.49 ? 1028 PHE B N   1 
ATOM   3517 C  CA  . PHE B 1 251 ? 108.120 150.239 117.448 1.00 192.52 ? 1028 PHE B CA  1 
ATOM   3518 C  C   . PHE B 1 251 ? 107.024 150.254 116.389 1.00 192.26 ? 1028 PHE B C   1 
ATOM   3519 O  O   . PHE B 1 251 ? 107.261 149.827 115.251 1.00 192.83 ? 1028 PHE B O   1 
ATOM   3520 C  CB  . PHE B 1 251 ? 109.066 149.061 117.218 1.00 192.29 ? 1028 PHE B CB  1 
ATOM   3521 C  CG  . PHE B 1 251 ? 110.434 149.260 117.802 1.00 192.41 ? 1028 PHE B CG  1 
ATOM   3522 C  CD1 . PHE B 1 251 ? 111.236 150.306 117.378 1.00 193.21 ? 1028 PHE B CD1 1 
ATOM   3523 C  CD2 . PHE B 1 251 ? 110.917 148.404 118.777 1.00 192.28 ? 1028 PHE B CD2 1 
ATOM   3524 C  CE1 . PHE B 1 251 ? 112.496 150.492 117.914 1.00 193.86 ? 1028 PHE B CE1 1 
ATOM   3525 C  CE2 . PHE B 1 251 ? 112.175 148.585 119.317 1.00 192.85 ? 1028 PHE B CE2 1 
ATOM   3526 C  CZ  . PHE B 1 251 ? 112.966 149.631 118.885 1.00 193.65 ? 1028 PHE B CZ  1 
ATOM   3527 N  N   . LYS B 1 252 ? 105.831 150.732 116.733 1.00 186.05 ? 1029 LYS B N   1 
ATOM   3528 C  CA  . LYS B 1 252 ? 104.728 150.753 115.783 1.00 186.42 ? 1029 LYS B CA  1 
ATOM   3529 C  C   . LYS B 1 252 ? 104.972 151.803 114.706 1.00 186.03 ? 1029 LYS B C   1 
ATOM   3530 O  O   . LYS B 1 252 ? 105.289 152.958 115.008 1.00 185.05 ? 1029 LYS B O   1 
ATOM   3531 C  CB  . LYS B 1 252 ? 103.414 151.033 116.510 1.00 186.25 ? 1029 LYS B CB  1 
ATOM   3532 C  CG  . LYS B 1 252 ? 102.175 150.875 115.645 1.00 186.16 ? 1029 LYS B CG  1 
ATOM   3533 C  CD  . LYS B 1 252 ? 100.936 150.644 116.494 1.00 186.86 ? 1029 LYS B CD  1 
ATOM   3534 C  CE  . LYS B 1 252 ? 101.087 149.411 117.370 1.00 186.39 ? 1029 LYS B CE  1 
ATOM   3535 N  NZ  . LYS B 1 252 ? 99.874  149.166 118.198 1.00 186.11 ? 1029 LYS B NZ  1 
ATOM   3536 N  N   . GLY B 1 253 ? 104.824 151.398 113.446 1.00 176.39 ? 1030 GLY B N   1 
ATOM   3537 C  CA  . GLY B 1 253 ? 104.977 152.322 112.340 1.00 175.46 ? 1030 GLY B CA  1 
ATOM   3538 C  C   . GLY B 1 253 ? 106.392 152.776 112.070 1.00 175.37 ? 1030 GLY B C   1 
ATOM   3539 O  O   . GLY B 1 253 ? 106.586 153.817 111.436 1.00 174.99 ? 1030 GLY B O   1 
ATOM   3540 N  N   . ARG B 1 254 ? 107.396 152.025 112.533 1.00 185.38 ? 1031 ARG B N   1 
ATOM   3541 C  CA  . ARG B 1 254 ? 108.785 152.411 112.314 1.00 185.71 ? 1031 ARG B CA  1 
ATOM   3542 C  C   . ARG B 1 254 ? 109.664 151.224 111.927 1.00 186.66 ? 1031 ARG B C   1 
ATOM   3543 O  O   . ARG B 1 254 ? 110.894 151.325 112.010 1.00 186.82 ? 1031 ARG B O   1 
ATOM   3544 C  CB  . ARG B 1 254 ? 109.365 153.091 113.559 1.00 185.52 ? 1031 ARG B CB  1 
ATOM   3545 C  CG  . ARG B 1 254 ? 108.795 154.472 113.841 1.00 185.51 ? 1031 ARG B CG  1 
ATOM   3546 C  CD  . ARG B 1 254 ? 109.654 155.230 114.841 1.00 185.75 ? 1031 ARG B CD  1 
ATOM   3547 N  NE  . ARG B 1 254 ? 110.015 154.405 115.988 1.00 186.57 ? 1031 ARG B NE  1 
ATOM   3548 C  CZ  . ARG B 1 254 ? 109.196 154.107 116.987 1.00 187.23 ? 1031 ARG B CZ  1 
ATOM   3549 N  NH1 . ARG B 1 254 ? 107.952 154.558 117.020 1.00 186.94 ? 1031 ARG B NH1 1 
ATOM   3550 N  NH2 . ARG B 1 254 ? 109.636 153.339 117.980 1.00 188.47 ? 1031 ARG B NH2 1 
ATOM   3551 N  N   . VAL B 1 255 ? 109.071 150.108 111.510 1.00 178.62 ? 1032 VAL B N   1 
ATOM   3552 C  CA  . VAL B 1 255 ? 109.811 148.905 111.152 1.00 177.43 ? 1032 VAL B CA  1 
ATOM   3553 C  C   . VAL B 1 255 ? 109.340 148.437 109.784 1.00 176.95 ? 1032 VAL B C   1 
ATOM   3554 O  O   . VAL B 1 255 ? 108.134 148.303 109.551 1.00 176.86 ? 1032 VAL B O   1 
ATOM   3555 C  CB  . VAL B 1 255 ? 109.627 147.790 112.201 1.00 177.17 ? 1032 VAL B CB  1 
ATOM   3556 C  CG1 . VAL B 1 255 ? 110.028 146.442 111.625 1.00 177.26 ? 1032 VAL B CG1 1 
ATOM   3557 C  CG2 . VAL B 1 255 ? 110.432 148.102 113.452 1.00 177.62 ? 1032 VAL B CG2 1 
ATOM   3558 N  N   . CYS B 1 256 ? 110.288 148.189 108.882 1.00 183.22 ? 1033 CYS B N   1 
ATOM   3559 C  CA  . CYS B 1 256 ? 109.989 147.686 107.551 1.00 182.30 ? 1033 CYS B CA  1 
ATOM   3560 C  C   . CYS B 1 256 ? 110.815 146.437 107.283 1.00 181.10 ? 1033 CYS B C   1 
ATOM   3561 O  O   . CYS B 1 256 ? 111.918 146.276 107.813 1.00 181.78 ? 1033 CYS B O   1 
ATOM   3562 C  CB  . CYS B 1 256 ? 110.270 148.737 106.469 1.00 184.24 ? 1033 CYS B CB  1 
ATOM   3563 S  SG  . CYS B 1 256 ? 111.997 149.255 106.362 1.00 191.68 ? 1033 CYS B SG  1 
ATOM   3564 N  N   . GLY B 1 257 ? 110.270 145.554 106.456 1.00 156.37 ? 1034 GLY B N   1 
ATOM   3565 C  CA  . GLY B 1 257 ? 110.953 144.319 106.122 1.00 158.53 ? 1034 GLY B CA  1 
ATOM   3566 C  C   . GLY B 1 257 ? 109.969 143.305 105.564 1.00 158.01 ? 1034 GLY B C   1 
ATOM   3567 O  O   . GLY B 1 257 ? 108.874 143.657 105.131 1.00 158.32 ? 1034 GLY B O   1 
ATOM   3568 N  N   . LEU B 1 258 ? 110.394 142.040 105.587 1.00 143.02 ? 1035 LEU B N   1 
ATOM   3569 C  CA  . LEU B 1 258 ? 109.545 140.962 105.096 1.00 140.06 ? 1035 LEU B CA  1 
ATOM   3570 C  C   . LEU B 1 258 ? 108.322 140.741 105.975 1.00 140.89 ? 1035 LEU B C   1 
ATOM   3571 O  O   . LEU B 1 258 ? 107.332 140.171 105.505 1.00 144.35 ? 1035 LEU B O   1 
ATOM   3572 C  CB  . LEU B 1 258 ? 110.348 139.665 104.987 1.00 141.01 ? 1035 LEU B CB  1 
ATOM   3573 C  CG  . LEU B 1 258 ? 110.735 139.232 103.571 1.00 140.51 ? 1035 LEU B CG  1 
ATOM   3574 C  CD1 . LEU B 1 258 ? 111.288 137.816 103.575 1.00 141.56 ? 1035 LEU B CD1 1 
ATOM   3575 C  CD2 . LEU B 1 258 ? 109.546 139.343 102.631 1.00 142.63 ? 1035 LEU B CD2 1 
ATOM   3576 N  N   . CYS B 1 259 ? 108.366 141.175 107.233 1.00 149.33 ? 1036 CYS B N   1 
ATOM   3577 C  CA  . CYS B 1 259 ? 107.225 141.051 108.130 1.00 150.59 ? 1036 CYS B CA  1 
ATOM   3578 C  C   . CYS B 1 259 ? 106.211 142.174 107.955 1.00 150.88 ? 1036 CYS B C   1 
ATOM   3579 O  O   . CYS B 1 259 ? 105.176 142.161 108.629 1.00 150.72 ? 1036 CYS B O   1 
ATOM   3580 C  CB  . CYS B 1 259 ? 107.700 141.009 109.585 1.00 151.21 ? 1036 CYS B CB  1 
ATOM   3581 S  SG  . CYS B 1 259 ? 108.530 139.475 110.060 1.00 155.00 ? 1036 CYS B SG  1 
ATOM   3582 N  N   . GLY B 1 260 ? 106.481 143.138 107.085 1.00 173.92 ? 1037 GLY B N   1 
ATOM   3583 C  CA  . GLY B 1 260 ? 105.561 144.224 106.834 1.00 175.42 ? 1037 GLY B CA  1 
ATOM   3584 C  C   . GLY B 1 260 ? 105.675 145.337 107.862 1.00 176.46 ? 1037 GLY B C   1 
ATOM   3585 O  O   . GLY B 1 260 ? 106.238 145.179 108.944 1.00 177.21 ? 1037 GLY B O   1 
ATOM   3586 N  N   . ASN B 1 261 ? 105.122 146.492 107.501 1.00 182.07 ? 1038 ASN B N   1 
ATOM   3587 C  CA  . ASN B 1 261 ? 105.142 147.639 108.398 1.00 181.69 ? 1038 ASN B CA  1 
ATOM   3588 C  C   . ASN B 1 261 ? 104.143 147.437 109.530 1.00 181.55 ? 1038 ASN B C   1 
ATOM   3589 O  O   . ASN B 1 261 ? 102.991 147.056 109.299 1.00 180.78 ? 1038 ASN B O   1 
ATOM   3590 C  CB  . ASN B 1 261 ? 104.830 148.923 107.630 1.00 180.83 ? 1038 ASN B CB  1 
ATOM   3591 C  CG  . ASN B 1 261 ? 103.475 148.885 106.952 1.00 181.65 ? 1038 ASN B CG  1 
ATOM   3592 O  OD1 . ASN B 1 261 ? 103.027 147.836 106.493 1.00 181.71 ? 1038 ASN B OD1 1 
ATOM   3593 N  ND2 . ASN B 1 261 ? 102.814 150.035 106.886 1.00 182.00 ? 1038 ASN B ND2 1 
ATOM   3594 N  N   . PHE B 1 262 ? 104.590 147.687 110.761 1.00 174.54 ? 1039 PHE B N   1 
ATOM   3595 C  CA  . PHE B 1 262 ? 103.751 147.512 111.946 1.00 172.86 ? 1039 PHE B CA  1 
ATOM   3596 C  C   . PHE B 1 262 ? 102.828 148.721 112.068 1.00 173.59 ? 1039 PHE B C   1 
ATOM   3597 O  O   . PHE B 1 262 ? 103.097 149.688 112.785 1.00 173.52 ? 1039 PHE B O   1 
ATOM   3598 C  CB  . PHE B 1 262 ? 104.612 147.328 113.189 1.00 172.66 ? 1039 PHE B CB  1 
ATOM   3599 C  CG  . PHE B 1 262 ? 103.849 146.857 114.393 1.00 171.59 ? 1039 PHE B CG  1 
ATOM   3600 C  CD1 . PHE B 1 262 ? 102.662 146.158 114.249 1.00 172.69 ? 1039 PHE B CD1 1 
ATOM   3601 C  CD2 . PHE B 1 262 ? 104.320 147.111 115.670 1.00 171.41 ? 1039 PHE B CD2 1 
ATOM   3602 C  CE1 . PHE B 1 262 ? 101.959 145.724 115.355 1.00 174.53 ? 1039 PHE B CE1 1 
ATOM   3603 C  CE2 . PHE B 1 262 ? 103.621 146.680 116.780 1.00 172.53 ? 1039 PHE B CE2 1 
ATOM   3604 C  CZ  . PHE B 1 262 ? 102.439 145.985 116.623 1.00 173.95 ? 1039 PHE B CZ  1 
ATOM   3605 N  N   . ASP B 1 263 ? 101.710 148.657 111.342 1.00 186.46 ? 1040 ASP B N   1 
ATOM   3606 C  CA  . ASP B 1 263 ? 100.730 149.736 111.336 1.00 187.14 ? 1040 ASP B CA  1 
ATOM   3607 C  C   . ASP B 1 263 ? 99.307  149.239 111.557 1.00 188.17 ? 1040 ASP B C   1 
ATOM   3608 O  O   . ASP B 1 263 ? 98.359  150.003 111.337 1.00 187.10 ? 1040 ASP B O   1 
ATOM   3609 C  CB  . ASP B 1 263 ? 100.808 150.524 110.023 1.00 187.40 ? 1040 ASP B CB  1 
ATOM   3610 C  CG  . ASP B 1 263 ? 100.289 149.735 108.838 1.00 187.31 ? 1040 ASP B CG  1 
ATOM   3611 O  OD1 . ASP B 1 263 ? 100.485 148.501 108.810 1.00 186.09 ? 1040 ASP B OD1 1 
ATOM   3612 O  OD2 . ASP B 1 263 ? 99.686  150.348 107.934 1.00 187.89 ? 1040 ASP B OD2 1 
ATOM   3613 N  N   . ASP B 1 264 ? 99.133  147.985 111.976 1.00 201.64 ? 1041 ASP B N   1 
ATOM   3614 C  CA  . ASP B 1 264 ? 97.827  147.389 112.257 1.00 201.54 ? 1041 ASP B CA  1 
ATOM   3615 C  C   . ASP B 1 264 ? 96.913  147.376 111.035 1.00 201.37 ? 1041 ASP B C   1 
ATOM   3616 O  O   . ASP B 1 264 ? 95.688  147.319 111.175 1.00 201.70 ? 1041 ASP B O   1 
ATOM   3617 C  CB  . ASP B 1 264 ? 97.132  148.095 113.427 1.00 200.92 ? 1041 ASP B CB  1 
ATOM   3618 C  CG  . ASP B 1 264 ? 97.872  147.918 114.737 1.00 200.73 ? 1041 ASP B CG  1 
ATOM   3619 O  OD1 . ASP B 1 264 ? 98.520  146.865 114.918 1.00 200.94 ? 1041 ASP B OD1 1 
ATOM   3620 O  OD2 . ASP B 1 264 ? 97.807  148.830 115.587 1.00 200.64 ? 1041 ASP B OD2 1 
ATOM   3621 N  N   . ILE B 1 265 ? 97.484  147.427 109.834 1.00 193.64 ? 1042 ILE B N   1 
ATOM   3622 C  CA  . ILE B 1 265 ? 96.727  147.375 108.589 1.00 192.99 ? 1042 ILE B CA  1 
ATOM   3623 C  C   . ILE B 1 265 ? 97.258  146.207 107.771 1.00 192.67 ? 1042 ILE B C   1 
ATOM   3624 O  O   . ILE B 1 265 ? 98.456  146.149 107.468 1.00 193.40 ? 1042 ILE B O   1 
ATOM   3625 C  CB  . ILE B 1 265 ? 96.825  148.689 107.800 1.00 193.06 ? 1042 ILE B CB  1 
ATOM   3626 C  CG1 . ILE B 1 265 ? 96.436  149.876 108.684 1.00 192.47 ? 1042 ILE B CG1 1 
ATOM   3627 C  CG2 . ILE B 1 265 ? 95.943  148.635 106.565 1.00 192.02 ? 1042 ILE B CG2 1 
ATOM   3628 C  CD1 . ILE B 1 265 ? 94.992  149.855 109.133 1.00 192.59 ? 1042 ILE B CD1 1 
ATOM   3629 N  N   . ALA B 1 266 ? 96.370  145.284 107.409 1.00 185.67 ? 1043 ALA B N   1 
ATOM   3630 C  CA  . ALA B 1 266 ? 96.757  144.061 106.720 1.00 185.98 ? 1043 ALA B CA  1 
ATOM   3631 C  C   . ALA B 1 266 ? 96.719  144.185 105.202 1.00 186.59 ? 1043 ALA B C   1 
ATOM   3632 O  O   . ALA B 1 266 ? 96.966  143.191 104.511 1.00 187.23 ? 1043 ALA B O   1 
ATOM   3633 C  CB  . ALA B 1 266 ? 95.858  142.902 107.161 1.00 184.71 ? 1043 ALA B CB  1 
ATOM   3634 N  N   . VAL B 1 267 ? 96.420  145.366 104.665 1.00 189.53 ? 1044 VAL B N   1 
ATOM   3635 C  CA  . VAL B 1 267 ? 96.341  145.558 103.220 1.00 190.54 ? 1044 VAL B CA  1 
ATOM   3636 C  C   . VAL B 1 267 ? 97.517  146.342 102.660 1.00 189.98 ? 1044 VAL B C   1 
ATOM   3637 O  O   . VAL B 1 267 ? 97.690  146.370 101.430 1.00 190.13 ? 1044 VAL B O   1 
ATOM   3638 C  CB  . VAL B 1 267 ? 95.017  146.237 102.810 1.00 190.54 ? 1044 VAL B CB  1 
ATOM   3639 C  CG1 . VAL B 1 267 ? 93.838  145.553 103.487 1.00 190.30 ? 1044 VAL B CG1 1 
ATOM   3640 C  CG2 . VAL B 1 267 ? 95.051  147.719 103.144 1.00 188.82 ? 1044 VAL B CG2 1 
ATOM   3641 N  N   . ASN B 1 268 ? 98.329  146.977 103.506 1.00 179.63 ? 1045 ASN B N   1 
ATOM   3642 C  CA  . ASN B 1 268 ? 99.485  147.744 103.061 1.00 179.23 ? 1045 ASN B CA  1 
ATOM   3643 C  C   . ASN B 1 268 ? 100.799 147.109 103.509 1.00 179.65 ? 1045 ASN B C   1 
ATOM   3644 O  O   . ASN B 1 268 ? 101.793 147.807 103.721 1.00 179.74 ? 1045 ASN B O   1 
ATOM   3645 C  CB  . ASN B 1 268 ? 99.392  149.187 103.555 1.00 178.86 ? 1045 ASN B CB  1 
ATOM   3646 C  CG  . ASN B 1 268 ? 99.208  149.281 105.058 1.00 179.46 ? 1045 ASN B CG  1 
ATOM   3647 O  OD1 . ASN B 1 268 ? 99.321  148.287 105.775 1.00 179.30 ? 1045 ASN B OD1 1 
ATOM   3648 N  ND2 . ASN B 1 268 ? 98.923  150.484 105.543 1.00 179.95 ? 1045 ASN B ND2 1 
ATOM   3649 N  N   . ASP B 1 269 ? 100.814 145.783 103.659 1.00 188.95 ? 1046 ASP B N   1 
ATOM   3650 C  CA  . ASP B 1 269 ? 101.996 145.054 104.101 1.00 189.99 ? 1046 ASP B CA  1 
ATOM   3651 C  C   . ASP B 1 269 ? 102.870 144.592 102.941 1.00 189.64 ? 1046 ASP B C   1 
ATOM   3652 O  O   . ASP B 1 269 ? 103.582 143.587 103.068 1.00 190.77 ? 1046 ASP B O   1 
ATOM   3653 C  CB  . ASP B 1 269 ? 101.581 143.859 104.961 1.00 189.72 ? 1046 ASP B CB  1 
ATOM   3654 C  CG  . ASP B 1 269 ? 101.697 144.141 106.446 1.00 189.55 ? 1046 ASP B CG  1 
ATOM   3655 O  OD1 . ASP B 1 269 ? 102.411 145.094 106.818 1.00 188.79 ? 1046 ASP B OD1 1 
ATOM   3656 O  OD2 . ASP B 1 269 ? 101.072 143.409 107.242 1.00 190.74 ? 1046 ASP B OD2 1 
ATOM   3657 N  N   . PHE B 1 270 ? 102.836 145.298 101.812 1.00 184.79 ? 1047 PHE B N   1 
ATOM   3658 C  CA  . PHE B 1 270 ? 103.610 144.897 100.645 1.00 184.50 ? 1047 PHE B CA  1 
ATOM   3659 C  C   . PHE B 1 270 ? 104.535 146.016 100.183 1.00 186.38 ? 1047 PHE B C   1 
ATOM   3660 O  O   . PHE B 1 270 ? 104.621 146.303 98.985  1.00 186.83 ? 1047 PHE B O   1 
ATOM   3661 C  CB  . PHE B 1 270 ? 102.678 144.476 99.507  1.00 184.00 ? 1047 PHE B CB  1 
ATOM   3662 C  CG  . PHE B 1 270 ? 102.154 143.075 99.642  1.00 185.51 ? 1047 PHE B CG  1 
ATOM   3663 C  CD1 . PHE B 1 270 ? 101.184 142.770 100.582 1.00 185.62 ? 1047 PHE B CD1 1 
ATOM   3664 C  CD2 . PHE B 1 270 ? 102.634 142.061 98.829  1.00 186.58 ? 1047 PHE B CD2 1 
ATOM   3665 C  CE1 . PHE B 1 270 ? 100.701 141.481 100.708 1.00 185.67 ? 1047 PHE B CE1 1 
ATOM   3666 C  CE2 . PHE B 1 270 ? 102.155 140.771 98.951  1.00 185.69 ? 1047 PHE B CE2 1 
ATOM   3667 C  CZ  . PHE B 1 270 ? 101.188 140.481 99.892  1.00 184.63 ? 1047 PHE B CZ  1 
ATOM   3668 N  N   . ALA B 1 271 ? 105.229 146.652 101.124 1.00 217.42 ? 1048 ALA B N   1 
ATOM   3669 C  CA  . ALA B 1 271 ? 106.187 147.703 100.797 1.00 218.80 ? 1048 ALA B CA  1 
ATOM   3670 C  C   . ALA B 1 271 ? 107.445 147.060 100.229 1.00 220.22 ? 1048 ALA B C   1 
ATOM   3671 O  O   . ALA B 1 271 ? 108.225 146.447 100.966 1.00 220.66 ? 1048 ALA B O   1 
ATOM   3672 C  CB  . ALA B 1 271 ? 106.503 148.543 102.031 1.00 218.73 ? 1048 ALA B CB  1 
ATOM   3673 N  N   . THR B 1 272 ? 107.649 147.201 98.920  1.00 239.10 ? 1049 THR B N   1 
ATOM   3674 C  CA  . THR B 1 272 ? 108.767 146.548 98.248  1.00 238.52 ? 1049 THR B CA  1 
ATOM   3675 C  C   . THR B 1 272 ? 110.043 147.374 98.347  1.00 238.71 ? 1049 THR B C   1 
ATOM   3676 O  O   . THR B 1 272 ? 110.666 147.685 97.327  1.00 239.01 ? 1049 THR B O   1 
ATOM   3677 C  CB  . THR B 1 272 ? 108.428 146.287 96.778  1.00 239.04 ? 1049 THR B CB  1 
ATOM   3678 O  OG1 . THR B 1 272 ? 108.771 147.438 95.995  1.00 239.68 ? 1049 THR B OG1 1 
ATOM   3679 C  CG2 . THR B 1 272 ? 106.945 145.994 96.616  1.00 238.99 ? 1049 THR B CG2 1 
ATOM   3680 N  N   . ARG B 1 273 ? 110.429 147.745 99.569  1.00 239.77 ? 1050 ARG B N   1 
ATOM   3681 C  CA  . ARG B 1 273 ? 111.673 148.436 99.899  1.00 239.90 ? 1050 ARG B CA  1 
ATOM   3682 C  C   . ARG B 1 273 ? 111.749 149.841 99.307  1.00 241.03 ? 1050 ARG B C   1 
ATOM   3683 O  O   . ARG B 1 273 ? 112.738 150.545 99.544  1.00 240.52 ? 1050 ARG B O   1 
ATOM   3684 C  CB  . ARG B 1 273 ? 112.909 147.633 99.463  1.00 239.82 ? 1050 ARG B CB  1 
ATOM   3685 C  CG  . ARG B 1 273 ? 114.181 147.931 100.246 1.00 239.71 ? 1050 ARG B CG  1 
ATOM   3686 C  CD  . ARG B 1 273 ? 115.361 147.123 99.723  1.00 239.80 ? 1050 ARG B CD  1 
ATOM   3687 N  NE  . ARG B 1 273 ? 115.173 146.696 98.342  1.00 240.51 ? 1050 ARG B NE  1 
ATOM   3688 C  CZ  . ARG B 1 273 ? 115.519 147.413 97.281  1.00 240.71 ? 1050 ARG B CZ  1 
ATOM   3689 N  NH1 . ARG B 1 273 ? 116.076 148.606 97.405  1.00 240.55 ? 1050 ARG B NH1 1 
ATOM   3690 N  NH2 . ARG B 1 273 ? 115.299 146.920 96.065  1.00 240.17 ? 1050 ARG B NH2 1 
ATOM   3691 N  N   . SER B 1 274 ? 110.737 150.281 98.557  1.00 265.21 ? 1051 SER B N   1 
ATOM   3692 C  CA  . SER B 1 274 ? 110.731 151.609 97.953  1.00 265.32 ? 1051 SER B CA  1 
ATOM   3693 C  C   . SER B 1 274 ? 109.493 152.407 98.344  1.00 265.97 ? 1051 SER B C   1 
ATOM   3694 O  O   . SER B 1 274 ? 109.114 153.343 97.632  1.00 266.04 ? 1051 SER B O   1 
ATOM   3695 C  CB  . SER B 1 274 ? 110.835 151.504 96.430  1.00 264.59 ? 1051 SER B CB  1 
ATOM   3696 O  OG  . SER B 1 274 ? 109.724 150.810 95.890  1.00 264.92 ? 1051 SER B OG  1 
ATOM   3697 N  N   . ARG B 1 275 ? 108.858 152.053 99.465  1.00 278.75 ? 1052 ARG B N   1 
ATOM   3698 C  CA  . ARG B 1 275 ? 107.650 152.727 99.945  1.00 278.79 ? 1052 ARG B CA  1 
ATOM   3699 C  C   . ARG B 1 275 ? 106.544 152.702 98.892  1.00 278.83 ? 1052 ARG B C   1 
ATOM   3700 O  O   . ARG B 1 275 ? 105.786 153.661 98.736  1.00 279.46 ? 1052 ARG B O   1 
ATOM   3701 C  CB  . ARG B 1 275 ? 107.951 154.162 100.387 1.00 278.77 ? 1052 ARG B CB  1 
ATOM   3702 C  CG  . ARG B 1 275 ? 108.486 154.278 101.806 1.00 278.32 ? 1052 ARG B CG  1 
ATOM   3703 C  CD  . ARG B 1 275 ? 109.984 154.026 101.860 1.00 277.94 ? 1052 ARG B CD  1 
ATOM   3704 N  NE  . ARG B 1 275 ? 110.464 153.877 103.229 1.00 278.51 ? 1052 ARG B NE  1 
ATOM   3705 C  CZ  . ARG B 1 275 ? 110.937 154.871 103.969 1.00 279.02 ? 1052 ARG B CZ  1 
ATOM   3706 N  NH1 . ARG B 1 275 ? 111.008 156.107 103.503 1.00 279.32 ? 1052 ARG B NH1 1 
ATOM   3707 N  NH2 . ARG B 1 275 ? 111.347 154.618 105.208 1.00 278.49 ? 1052 ARG B NH2 1 
ATOM   3708 N  N   . SER B 1 276 ? 106.452 151.593 98.161  1.00 256.53 ? 1053 SER B N   1 
ATOM   3709 C  CA  . SER B 1 276 ? 105.444 151.410 97.125  1.00 255.96 ? 1053 SER B CA  1 
ATOM   3710 C  C   . SER B 1 276 ? 104.784 150.055 97.324  1.00 255.01 ? 1053 SER B C   1 
ATOM   3711 O  O   . SER B 1 276 ? 105.460 149.021 97.277  1.00 254.90 ? 1053 SER B O   1 
ATOM   3712 C  CB  . SER B 1 276 ? 106.062 151.509 95.727  1.00 255.23 ? 1053 SER B CB  1 
ATOM   3713 O  OG  . SER B 1 276 ? 107.187 150.657 95.605  1.00 254.92 ? 1053 SER B OG  1 
ATOM   3714 N  N   . VAL B 1 277 ? 103.474 150.060 97.543  1.00 229.11 ? 1054 VAL B N   1 
ATOM   3715 C  CA  . VAL B 1 277 ? 102.728 148.825 97.763  1.00 227.82 ? 1054 VAL B CA  1 
ATOM   3716 C  C   . VAL B 1 277 ? 102.428 148.187 96.413  1.00 227.70 ? 1054 VAL B C   1 
ATOM   3717 O  O   . VAL B 1 277 ? 101.809 148.810 95.544  1.00 227.70 ? 1054 VAL B O   1 
ATOM   3718 C  CB  . VAL B 1 277 ? 101.437 149.090 98.549  1.00 227.78 ? 1054 VAL B CB  1 
ATOM   3719 C  CG1 . VAL B 1 277 ? 100.826 147.779 99.019  1.00 226.35 ? 1054 VAL B CG1 1 
ATOM   3720 C  CG2 . VAL B 1 277 ? 101.715 150.009 99.729  1.00 227.53 ? 1054 VAL B CG2 1 
ATOM   3721 N  N   . VAL B 1 278 ? 102.866 146.944 96.236  1.00 226.25 ? 1055 VAL B N   1 
ATOM   3722 C  CA  . VAL B 1 278 ? 102.661 146.193 95.003  1.00 226.76 ? 1055 VAL B CA  1 
ATOM   3723 C  C   . VAL B 1 278 ? 101.965 144.886 95.353  1.00 226.67 ? 1055 VAL B C   1 
ATOM   3724 O  O   . VAL B 1 278 ? 102.403 144.167 96.258  1.00 227.09 ? 1055 VAL B O   1 
ATOM   3725 C  CB  . VAL B 1 278 ? 103.989 145.929 94.270  1.00 225.71 ? 1055 VAL B CB  1 
ATOM   3726 C  CG1 . VAL B 1 278 ? 103.763 145.031 93.063  1.00 225.22 ? 1055 VAL B CG1 1 
ATOM   3727 C  CG2 . VAL B 1 278 ? 104.634 147.242 93.851  1.00 225.87 ? 1055 VAL B CG2 1 
ATOM   3728 N  N   . GLY B 1 279 ? 100.885 144.580 94.634  1.00 215.87 ? 1056 GLY B N   1 
ATOM   3729 C  CA  . GLY B 1 279 ? 100.141 143.358 94.880  1.00 214.84 ? 1056 GLY B CA  1 
ATOM   3730 C  C   . GLY B 1 279 ? 100.871 142.086 94.503  1.00 215.29 ? 1056 GLY B C   1 
ATOM   3731 O  O   . GLY B 1 279 ? 100.461 141.007 94.943  1.00 214.48 ? 1056 GLY B O   1 
ATOM   3732 N  N   . ASP B 1 280 ? 101.932 142.185 93.706  1.00 216.44 ? 1057 ASP B N   1 
ATOM   3733 C  CA  . ASP B 1 280 ? 102.693 141.009 93.295  1.00 216.04 ? 1057 ASP B CA  1 
ATOM   3734 C  C   . ASP B 1 280 ? 103.498 140.489 94.479  1.00 215.33 ? 1057 ASP B C   1 
ATOM   3735 O  O   . ASP B 1 280 ? 104.487 141.107 94.888  1.00 215.25 ? 1057 ASP B O   1 
ATOM   3736 C  CB  . ASP B 1 280 ? 103.604 141.354 92.121  1.00 216.10 ? 1057 ASP B CB  1 
ATOM   3737 C  CG  . ASP B 1 280 ? 104.086 140.125 91.375  1.00 215.91 ? 1057 ASP B CG  1 
ATOM   3738 O  OD1 . ASP B 1 280 ? 103.821 138.998 91.844  1.00 215.46 ? 1057 ASP B OD1 1 
ATOM   3739 O  OD2 . ASP B 1 280 ? 104.730 140.285 90.317  1.00 215.92 ? 1057 ASP B OD2 1 
ATOM   3740 N  N   . VAL B 1 281 ? 103.075 139.350 95.032  1.00 199.28 ? 1058 VAL B N   1 
ATOM   3741 C  CA  . VAL B 1 281 ? 103.776 138.766 96.172  1.00 198.69 ? 1058 VAL B CA  1 
ATOM   3742 C  C   . VAL B 1 281 ? 105.185 138.347 95.773  1.00 198.77 ? 1058 VAL B C   1 
ATOM   3743 O  O   . VAL B 1 281 ? 106.141 138.523 96.539  1.00 198.84 ? 1058 VAL B O   1 
ATOM   3744 C  CB  . VAL B 1 281 ? 102.974 137.582 96.743  1.00 198.37 ? 1058 VAL B CB  1 
ATOM   3745 C  CG1 . VAL B 1 281 ? 103.534 137.163 98.093  1.00 196.78 ? 1058 VAL B CG1 1 
ATOM   3746 C  CG2 . VAL B 1 281 ? 101.501 137.944 96.856  1.00 198.71 ? 1058 VAL B CG2 1 
ATOM   3747 N  N   . LEU B 1 282 ? 105.335 137.784 94.572  1.00 200.10 ? 1059 LEU B N   1 
ATOM   3748 C  CA  . LEU B 1 282 ? 106.655 137.367 94.109  1.00 199.87 ? 1059 LEU B CA  1 
ATOM   3749 C  C   . LEU B 1 282 ? 107.595 138.558 93.971  1.00 201.05 ? 1059 LEU B C   1 
ATOM   3750 O  O   . LEU B 1 282 ? 108.755 138.495 94.395  1.00 201.37 ? 1059 LEU B O   1 
ATOM   3751 C  CB  . LEU B 1 282 ? 106.531 136.622 92.781  1.00 199.89 ? 1059 LEU B CB  1 
ATOM   3752 C  CG  . LEU B 1 282 ? 107.724 135.762 92.363  1.00 199.03 ? 1059 LEU B CG  1 
ATOM   3753 C  CD1 . LEU B 1 282 ? 107.258 134.389 91.913  1.00 198.67 ? 1059 LEU B CD1 1 
ATOM   3754 C  CD2 . LEU B 1 282 ? 108.519 136.448 91.264  1.00 198.52 ? 1059 LEU B CD2 1 
ATOM   3755 N  N   . GLU B 1 283 ? 107.111 139.655 93.382  1.00 205.97 ? 1060 GLU B N   1 
ATOM   3756 C  CA  . GLU B 1 283 ? 107.942 140.847 93.247  1.00 204.23 ? 1060 GLU B CA  1 
ATOM   3757 C  C   . GLU B 1 283 ? 108.275 141.446 94.608  1.00 203.81 ? 1060 GLU B C   1 
ATOM   3758 O  O   . GLU B 1 283 ? 109.405 141.893 94.835  1.00 204.28 ? 1060 GLU B O   1 
ATOM   3759 C  CB  . GLU B 1 283 ? 107.243 141.878 92.363  1.00 204.44 ? 1060 GLU B CB  1 
ATOM   3760 C  CG  . GLU B 1 283 ? 107.622 141.794 90.894  1.00 205.14 ? 1060 GLU B CG  1 
ATOM   3761 C  CD  . GLU B 1 283 ? 106.880 142.804 90.042  1.00 206.13 ? 1060 GLU B CD  1 
ATOM   3762 O  OE1 . GLU B 1 283 ? 106.797 143.981 90.451  1.00 206.53 ? 1060 GLU B OE1 1 
ATOM   3763 O  OE2 . GLU B 1 283 ? 106.380 142.421 88.964  1.00 206.64 ? 1060 GLU B OE2 1 
ATOM   3764 N  N   . PHE B 1 284 ? 107.303 141.464 95.524  1.00 188.23 ? 1061 PHE B N   1 
ATOM   3765 C  CA  . PHE B 1 284 ? 107.558 141.984 96.863  1.00 187.78 ? 1061 PHE B CA  1 
ATOM   3766 C  C   . PHE B 1 284 ? 108.620 141.160 97.580  1.00 187.84 ? 1061 PHE B C   1 
ATOM   3767 O  O   . PHE B 1 284 ? 109.486 141.712 98.268  1.00 187.29 ? 1061 PHE B O   1 
ATOM   3768 C  CB  . PHE B 1 284 ? 106.259 142.010 97.669  1.00 188.36 ? 1061 PHE B CB  1 
ATOM   3769 C  CG  . PHE B 1 284 ? 106.464 142.159 99.148  1.00 187.44 ? 1061 PHE B CG  1 
ATOM   3770 C  CD1 . PHE B 1 284 ? 106.870 143.369 99.687  1.00 188.67 ? 1061 PHE B CD1 1 
ATOM   3771 C  CD2 . PHE B 1 284 ? 106.246 141.091 100.003 1.00 186.69 ? 1061 PHE B CD2 1 
ATOM   3772 C  CE1 . PHE B 1 284 ? 107.057 143.509 101.048 1.00 188.48 ? 1061 PHE B CE1 1 
ATOM   3773 C  CE2 . PHE B 1 284 ? 106.432 141.226 101.365 1.00 186.33 ? 1061 PHE B CE2 1 
ATOM   3774 C  CZ  . PHE B 1 284 ? 106.838 142.436 101.888 1.00 186.77 ? 1061 PHE B CZ  1 
ATOM   3775 N  N   . GLY B 1 285 ? 108.567 139.835 97.432  1.00 201.09 ? 1062 GLY B N   1 
ATOM   3776 C  CA  . GLY B 1 285 ? 109.583 138.993 98.040  1.00 200.92 ? 1062 GLY B CA  1 
ATOM   3777 C  C   . GLY B 1 285 ? 110.947 139.158 97.397  1.00 201.19 ? 1062 GLY B C   1 
ATOM   3778 O  O   . GLY B 1 285 ? 111.972 139.152 98.085  1.00 202.69 ? 1062 GLY B O   1 
ATOM   3779 N  N   . ASN B 1 286 ? 110.981 139.308 96.071  1.00 194.60 ? 1063 ASN B N   1 
ATOM   3780 C  CA  . ASN B 1 286 ? 112.259 139.435 95.377  1.00 193.73 ? 1063 ASN B CA  1 
ATOM   3781 C  C   . ASN B 1 286 ? 112.902 140.795 95.614  1.00 194.41 ? 1063 ASN B C   1 
ATOM   3782 O  O   . ASN B 1 286 ? 114.129 140.921 95.524  1.00 193.74 ? 1063 ASN B O   1 
ATOM   3783 C  CB  . ASN B 1 286 ? 112.069 139.195 93.879  1.00 193.16 ? 1063 ASN B CB  1 
ATOM   3784 C  CG  . ASN B 1 286 ? 112.408 137.775 93.470  1.00 193.29 ? 1063 ASN B CG  1 
ATOM   3785 O  OD1 . ASN B 1 286 ? 113.486 137.268 93.779  1.00 192.52 ? 1063 ASN B OD1 1 
ATOM   3786 N  ND2 . ASN B 1 286 ? 111.486 137.126 92.769  1.00 194.67 ? 1063 ASN B ND2 1 
ATOM   3787 N  N   . SER B 1 287 ? 112.103 141.820 95.915  1.00 203.47 ? 1064 SER B N   1 
ATOM   3788 C  CA  . SER B 1 287 ? 112.653 143.151 96.138  1.00 202.67 ? 1064 SER B CA  1 
ATOM   3789 C  C   . SER B 1 287 ? 113.422 143.269 97.448  1.00 202.54 ? 1064 SER B C   1 
ATOM   3790 O  O   . SER B 1 287 ? 114.086 144.289 97.662  1.00 203.14 ? 1064 SER B O   1 
ATOM   3791 C  CB  . SER B 1 287 ? 111.533 144.191 96.108  1.00 203.66 ? 1064 SER B CB  1 
ATOM   3792 O  OG  . SER B 1 287 ? 111.914 145.370 96.796  1.00 204.65 ? 1064 SER B OG  1 
ATOM   3793 N  N   . TRP B 1 288 ? 113.354 142.265 98.322  1.00 183.08 ? 1065 TRP B N   1 
ATOM   3794 C  CA  . TRP B 1 288 ? 114.018 142.309 99.617  1.00 181.07 ? 1065 TRP B CA  1 
ATOM   3795 C  C   . TRP B 1 288 ? 115.292 141.472 99.655  1.00 180.73 ? 1065 TRP B C   1 
ATOM   3796 O  O   . TRP B 1 288 ? 115.801 141.180 100.743 1.00 179.13 ? 1065 TRP B O   1 
ATOM   3797 C  CB  . TRP B 1 288 ? 113.057 141.855 100.717 1.00 178.84 ? 1065 TRP B CB  1 
ATOM   3798 C  CG  . TRP B 1 288 ? 112.245 142.970 101.300 1.00 178.79 ? 1065 TRP B CG  1 
ATOM   3799 C  CD1 . TRP B 1 288 ? 110.888 143.103 101.259 1.00 181.39 ? 1065 TRP B CD1 1 
ATOM   3800 C  CD2 . TRP B 1 288 ? 112.739 144.109 102.014 1.00 179.72 ? 1065 TRP B CD2 1 
ATOM   3801 N  NE1 . TRP B 1 288 ? 110.506 144.255 101.902 1.00 182.96 ? 1065 TRP B NE1 1 
ATOM   3802 C  CE2 . TRP B 1 288 ? 111.624 144.891 102.375 1.00 181.24 ? 1065 TRP B CE2 1 
ATOM   3803 C  CE3 . TRP B 1 288 ? 114.015 144.545 102.383 1.00 180.49 ? 1065 TRP B CE3 1 
ATOM   3804 C  CZ2 . TRP B 1 288 ? 111.746 146.083 103.086 1.00 180.86 ? 1065 TRP B CZ2 1 
ATOM   3805 C  CZ3 . TRP B 1 288 ? 114.134 145.728 103.089 1.00 182.35 ? 1065 TRP B CZ3 1 
ATOM   3806 C  CH2 . TRP B 1 288 ? 113.007 146.483 103.433 1.00 181.79 ? 1065 TRP B CH2 1 
ATOM   3807 N  N   . LYS B 1 289 ? 115.815 141.077 98.497  1.00 187.74 ? 1066 LYS B N   1 
ATOM   3808 C  CA  . LYS B 1 289 ? 117.040 140.291 98.465  1.00 186.26 ? 1066 LYS B CA  1 
ATOM   3809 C  C   . LYS B 1 289 ? 118.232 141.144 98.880  1.00 187.76 ? 1066 LYS B C   1 
ATOM   3810 O  O   . LYS B 1 289 ? 118.295 142.341 98.586  1.00 188.92 ? 1066 LYS B O   1 
ATOM   3811 C  CB  . LYS B 1 289 ? 117.267 139.710 97.069  1.00 186.66 ? 1066 LYS B CB  1 
ATOM   3812 C  CG  . LYS B 1 289 ? 117.374 140.750 95.965  1.00 188.25 ? 1066 LYS B CG  1 
ATOM   3813 C  CD  . LYS B 1 289 ? 117.964 140.152 94.699  1.00 188.39 ? 1066 LYS B CD  1 
ATOM   3814 C  CE  . LYS B 1 289 ? 117.169 138.942 94.237  1.00 189.04 ? 1066 LYS B CE  1 
ATOM   3815 N  NZ  . LYS B 1 289 ? 117.774 138.303 93.037  1.00 189.95 ? 1066 LYS B NZ  1 
ATOM   3816 N  N   . LEU B 1 290 ? 119.181 140.520 99.580  1.00 184.10 ? 1067 LEU B N   1 
ATOM   3817 C  CA  . LEU B 1 290 ? 120.360 141.243 100.046 1.00 184.04 ? 1067 LEU B CA  1 
ATOM   3818 C  C   . LEU B 1 290 ? 121.420 141.324 98.952  1.00 185.43 ? 1067 LEU B C   1 
ATOM   3819 O  O   . LEU B 1 290 ? 121.800 142.417 98.519  1.00 185.10 ? 1067 LEU B O   1 
ATOM   3820 C  CB  . LEU B 1 290 ? 120.919 140.573 101.307 1.00 182.78 ? 1067 LEU B CB  1 
ATOM   3821 C  CG  . LEU B 1 290 ? 121.805 141.391 102.254 1.00 182.88 ? 1067 LEU B CG  1 
ATOM   3822 C  CD1 . LEU B 1 290 ? 121.897 140.700 103.605 1.00 183.71 ? 1067 LEU B CD1 1 
ATOM   3823 C  CD2 . LEU B 1 290 ? 123.202 141.622 101.691 1.00 183.08 ? 1067 LEU B CD2 1 
ATOM   3824 N  N   . SER B 1 291 ? 121.907 140.176 98.495  1.00 198.07 ? 1068 SER B N   1 
ATOM   3825 C  CA  . SER B 1 291 ? 122.941 140.152 97.468  1.00 196.99 ? 1068 SER B CA  1 
ATOM   3826 C  C   . SER B 1 291 ? 122.319 140.382 96.096  1.00 197.21 ? 1068 SER B C   1 
ATOM   3827 O  O   . SER B 1 291 ? 121.423 139.627 95.700  1.00 197.61 ? 1068 SER B O   1 
ATOM   3828 C  CB  . SER B 1 291 ? 123.684 138.824 97.489  1.00 197.19 ? 1068 SER B CB  1 
ATOM   3829 O  OG  . SER B 1 291 ? 124.255 138.542 96.223  1.00 197.59 ? 1068 SER B OG  1 
ATOM   3830 N  N   . PRO B 1 292 ? 122.752 141.399 95.347  1.00 200.38 ? 1069 PRO B N   1 
ATOM   3831 C  CA  . PRO B 1 292 ? 122.175 141.625 94.011  1.00 201.27 ? 1069 PRO B CA  1 
ATOM   3832 C  C   . PRO B 1 292 ? 122.457 140.504 93.026  1.00 201.42 ? 1069 PRO B C   1 
ATOM   3833 O  O   . PRO B 1 292 ? 121.738 140.385 92.026  1.00 200.92 ? 1069 PRO B O   1 
ATOM   3834 C  CB  . PRO B 1 292 ? 122.830 142.940 93.561  1.00 200.52 ? 1069 PRO B CB  1 
ATOM   3835 C  CG  . PRO B 1 292 ? 123.346 143.574 94.821  1.00 199.84 ? 1069 PRO B CG  1 
ATOM   3836 C  CD  . PRO B 1 292 ? 123.728 142.437 95.712  1.00 199.56 ? 1069 PRO B CD  1 
ATOM   3837 N  N   . SER B 1 293 ? 123.475 139.680 93.271  1.00 204.33 ? 1070 SER B N   1 
ATOM   3838 C  CA  . SER B 1 293 ? 123.832 138.601 92.359  1.00 204.25 ? 1070 SER B CA  1 
ATOM   3839 C  C   . SER B 1 293 ? 122.959 137.365 92.524  1.00 203.71 ? 1070 SER B C   1 
ATOM   3840 O  O   . SER B 1 293 ? 123.111 136.414 91.749  1.00 203.58 ? 1070 SER B O   1 
ATOM   3841 C  CB  . SER B 1 293 ? 125.303 138.219 92.548  1.00 203.52 ? 1070 SER B CB  1 
ATOM   3842 O  OG  . SER B 1 293 ? 125.664 137.146 91.697  1.00 203.38 ? 1070 SER B OG  1 
ATOM   3843 N  N   . CYS B 1 294 ? 122.062 137.349 93.505  1.00 206.70 ? 1071 CYS B N   1 
ATOM   3844 C  CA  . CYS B 1 294 ? 121.208 136.190 93.708  1.00 206.52 ? 1071 CYS B CA  1 
ATOM   3845 C  C   . CYS B 1 294 ? 120.214 136.057 92.555  1.00 206.80 ? 1071 CYS B C   1 
ATOM   3846 O  O   . CYS B 1 294 ? 119.715 137.065 92.045  1.00 207.07 ? 1071 CYS B O   1 
ATOM   3847 C  CB  . CYS B 1 294 ? 120.453 136.304 95.030  1.00 207.04 ? 1071 CYS B CB  1 
ATOM   3848 S  SG  . CYS B 1 294 ? 121.483 136.144 96.502  1.00 211.75 ? 1071 CYS B SG  1 
ATOM   3849 N  N   . PRO B 1 295 ? 119.913 134.836 92.121  1.00 205.87 ? 1072 PRO B N   1 
ATOM   3850 C  CA  . PRO B 1 295 ? 118.906 134.658 91.070  1.00 206.29 ? 1072 PRO B CA  1 
ATOM   3851 C  C   . PRO B 1 295 ? 117.522 135.056 91.555  1.00 206.30 ? 1072 PRO B C   1 
ATOM   3852 O  O   . PRO B 1 295 ? 117.186 134.923 92.734  1.00 206.12 ? 1072 PRO B O   1 
ATOM   3853 C  CB  . PRO B 1 295 ? 118.974 133.157 90.758  1.00 206.48 ? 1072 PRO B CB  1 
ATOM   3854 C  CG  . PRO B 1 295 ? 120.287 132.697 91.320  1.00 206.14 ? 1072 PRO B CG  1 
ATOM   3855 C  CD  . PRO B 1 295 ? 120.538 133.563 92.511  1.00 205.77 ? 1072 PRO B CD  1 
ATOM   3856 N  N   . ASP B 1 296 ? 116.715 135.552 90.621  1.00 203.03 ? 1073 ASP B N   1 
ATOM   3857 C  CA  . ASP B 1 296 ? 115.360 135.969 90.953  1.00 202.48 ? 1073 ASP B CA  1 
ATOM   3858 C  C   . ASP B 1 296 ? 114.472 134.754 91.189  1.00 201.76 ? 1073 ASP B C   1 
ATOM   3859 O  O   . ASP B 1 296 ? 114.570 133.744 90.486  1.00 201.70 ? 1073 ASP B O   1 
ATOM   3860 C  CB  . ASP B 1 296 ? 114.783 136.837 89.836  1.00 203.47 ? 1073 ASP B CB  1 
ATOM   3861 C  CG  . ASP B 1 296 ? 113.595 137.660 90.292  1.00 203.68 ? 1073 ASP B CG  1 
ATOM   3862 O  OD1 . ASP B 1 296 ? 112.489 137.094 90.414  1.00 204.51 ? 1073 ASP B OD1 1 
ATOM   3863 O  OD2 . ASP B 1 296 ? 113.768 138.874 90.531  1.00 202.79 ? 1073 ASP B OD2 1 
ATOM   3864 N  N   . ALA B 1 297 ? 113.600 134.856 92.188  1.00 180.98 ? 1074 ALA B N   1 
ATOM   3865 C  CA  . ALA B 1 297 ? 112.710 133.754 92.520  1.00 179.71 ? 1074 ALA B CA  1 
ATOM   3866 C  C   . ALA B 1 297 ? 111.615 133.606 91.470  1.00 180.66 ? 1074 ALA B C   1 
ATOM   3867 O  O   . ALA B 1 297 ? 111.230 134.567 90.799  1.00 181.15 ? 1074 ALA B O   1 
ATOM   3868 C  CB  . ALA B 1 297 ? 112.087 133.967 93.899  1.00 178.28 ? 1074 ALA B CB  1 
ATOM   3869 N  N   . LEU B 1 298 ? 111.114 132.383 91.332  1.00 181.61 ? 1075 LEU B N   1 
ATOM   3870 C  CA  . LEU B 1 298 ? 110.064 132.060 90.380  1.00 181.01 ? 1075 LEU B CA  1 
ATOM   3871 C  C   . LEU B 1 298 ? 108.892 131.409 91.104  1.00 180.86 ? 1075 LEU B C   1 
ATOM   3872 O  O   . LEU B 1 298 ? 108.986 131.021 92.271  1.00 181.01 ? 1075 LEU B O   1 
ATOM   3873 C  CB  . LEU B 1 298 ? 110.586 131.135 89.272  1.00 181.22 ? 1075 LEU B CB  1 
ATOM   3874 C  CG  . LEU B 1 298 ? 110.960 131.804 87.948  1.00 181.61 ? 1075 LEU B CG  1 
ATOM   3875 C  CD1 . LEU B 1 298 ? 112.189 132.684 88.113  1.00 182.17 ? 1075 LEU B CD1 1 
ATOM   3876 C  CD2 . LEU B 1 298 ? 111.185 130.760 86.865  1.00 181.77 ? 1075 LEU B CD2 1 
ATOM   3877 N  N   . ALA B 1 299 ? 107.775 131.300 90.391  1.00 183.46 ? 1076 ALA B N   1 
ATOM   3878 C  CA  . ALA B 1 299 ? 106.582 130.703 90.971  1.00 184.73 ? 1076 ALA B CA  1 
ATOM   3879 C  C   . ALA B 1 299 ? 106.802 129.211 91.211  1.00 185.89 ? 1076 ALA B C   1 
ATOM   3880 O  O   . ALA B 1 299 ? 107.391 128.525 90.370  1.00 185.74 ? 1076 ALA B O   1 
ATOM   3881 C  CB  . ALA B 1 299 ? 105.377 130.913 90.055  1.00 184.11 ? 1076 ALA B CB  1 
ATOM   3882 N  N   . PRO B 1 300 ? 106.346 128.682 92.341  1.00 188.70 ? 1077 PRO B N   1 
ATOM   3883 C  CA  . PRO B 1 300 ? 106.526 127.260 92.633  1.00 188.14 ? 1077 PRO B CA  1 
ATOM   3884 C  C   . PRO B 1 300 ? 105.406 126.417 92.032  1.00 188.38 ? 1077 PRO B C   1 
ATOM   3885 O  O   . PRO B 1 300 ? 104.376 126.924 91.583  1.00 187.47 ? 1077 PRO B O   1 
ATOM   3886 C  CB  . PRO B 1 300 ? 106.487 127.207 94.171  1.00 186.51 ? 1077 PRO B CB  1 
ATOM   3887 C  CG  . PRO B 1 300 ? 105.999 128.575 94.631  1.00 186.84 ? 1077 PRO B CG  1 
ATOM   3888 C  CD  . PRO B 1 300 ? 105.633 129.378 93.422  1.00 187.81 ? 1077 PRO B CD  1 
ATOM   3889 N  N   . LYS B 1 301 ? 105.633 125.109 92.033  1.00 188.72 ? 1078 LYS B N   1 
ATOM   3890 C  CA  . LYS B 1 301 ? 104.682 124.144 91.511  1.00 188.26 ? 1078 LYS B CA  1 
ATOM   3891 C  C   . LYS B 1 301 ? 103.913 123.503 92.665  1.00 187.80 ? 1078 LYS B C   1 
ATOM   3892 O  O   . LYS B 1 301 ? 104.045 123.898 93.827  1.00 187.89 ? 1078 LYS B O   1 
ATOM   3893 C  CB  . LYS B 1 301 ? 105.410 123.101 90.662  1.00 186.71 ? 1078 LYS B CB  1 
ATOM   3894 C  CG  . LYS B 1 301 ? 106.605 123.648 89.899  1.00 185.86 ? 1078 LYS B CG  1 
ATOM   3895 C  CD  . LYS B 1 301 ? 107.184 122.604 88.959  1.00 186.96 ? 1078 LYS B CD  1 
ATOM   3896 C  CE  . LYS B 1 301 ? 107.678 121.387 89.723  1.00 186.65 ? 1078 LYS B CE  1 
ATOM   3897 N  NZ  . LYS B 1 301 ? 108.331 120.395 88.826  1.00 187.80 ? 1078 LYS B NZ  1 
ATOM   3898 N  N   . ASP B 1 302 ? 103.096 122.500 92.346  1.00 181.12 ? 1079 ASP B N   1 
ATOM   3899 C  CA  . ASP B 1 302 ? 102.331 121.792 93.359  1.00 180.14 ? 1079 ASP B CA  1 
ATOM   3900 C  C   . ASP B 1 302 ? 103.088 120.538 93.765  1.00 180.47 ? 1079 ASP B C   1 
ATOM   3901 O  O   . ASP B 1 302 ? 103.237 119.623 92.940  1.00 182.31 ? 1079 ASP B O   1 
ATOM   3902 C  CB  . ASP B 1 302 ? 100.943 121.430 92.834  1.00 180.70 ? 1079 ASP B CB  1 
ATOM   3903 C  CG  . ASP B 1 302 ? 100.093 120.722 93.871  1.00 181.86 ? 1079 ASP B CG  1 
ATOM   3904 O  OD1 . ASP B 1 302 ? 100.395 120.843 95.077  1.00 180.85 ? 1079 ASP B OD1 1 
ATOM   3905 O  OD2 . ASP B 1 302 ? 99.119  120.044 93.481  1.00 183.66 ? 1079 ASP B OD2 1 
ATOM   3906 N  N   . PRO B 1 303 ? 103.591 120.449 94.999  1.00 167.33 ? 1080 PRO B N   1 
ATOM   3907 C  CA  . PRO B 1 303 ? 104.315 119.232 95.402  1.00 168.41 ? 1080 PRO B CA  1 
ATOM   3908 C  C   . PRO B 1 303 ? 103.451 117.984 95.385  1.00 168.94 ? 1080 PRO B C   1 
ATOM   3909 O  O   . PRO B 1 303 ? 103.944 116.898 95.055  1.00 168.46 ? 1080 PRO B O   1 
ATOM   3910 C  CB  . PRO B 1 303 ? 104.804 119.571 96.817  1.00 168.67 ? 1080 PRO B CB  1 
ATOM   3911 C  CG  . PRO B 1 303 ? 103.869 120.633 97.298  1.00 167.87 ? 1080 PRO B CG  1 
ATOM   3912 C  CD  . PRO B 1 303 ? 103.514 121.438 96.086  1.00 167.25 ? 1080 PRO B CD  1 
ATOM   3913 N  N   . CYS B 1 304 ? 102.169 118.109 95.733  1.00 190.34 ? 1081 CYS B N   1 
ATOM   3914 C  CA  . CYS B 1 304 ? 101.288 116.945 95.725  1.00 191.30 ? 1081 CYS B CA  1 
ATOM   3915 C  C   . CYS B 1 304 ? 101.060 116.437 94.307  1.00 191.47 ? 1081 CYS B C   1 
ATOM   3916 O  O   . CYS B 1 304 ? 101.014 115.223 94.077  1.00 193.26 ? 1081 CYS B O   1 
ATOM   3917 C  CB  . CYS B 1 304 ? 99.961  117.288 96.399  1.00 190.90 ? 1081 CYS B CB  1 
ATOM   3918 S  SG  . CYS B 1 304 ? 100.054 117.409 98.204  1.00 200.00 ? 1081 CYS B SG  1 
ATOM   3919 N  N   . THR B 1 305 ? 100.914 117.349 93.344  1.00 175.97 ? 1082 THR B N   1 
ATOM   3920 C  CA  . THR B 1 305 ? 100.792 116.935 91.951  1.00 175.29 ? 1082 THR B CA  1 
ATOM   3921 C  C   . THR B 1 305 ? 102.103 116.353 91.435  1.00 174.91 ? 1082 THR B C   1 
ATOM   3922 O  O   . THR B 1 305 ? 102.099 115.393 90.655  1.00 173.16 ? 1082 THR B O   1 
ATOM   3923 C  CB  . THR B 1 305 ? 100.351 118.117 91.087  1.00 174.60 ? 1082 THR B CB  1 
ATOM   3924 O  OG1 . THR B 1 305 ? 99.152  118.685 91.629  1.00 175.54 ? 1082 THR B OG1 1 
ATOM   3925 C  CG2 . THR B 1 305 ? 100.086 117.667 89.657  1.00 172.84 ? 1082 THR B CG2 1 
ATOM   3926 N  N   . ALA B 1 306 ? 103.234 116.919 91.863  1.00 170.72 ? 1083 ALA B N   1 
ATOM   3927 C  CA  . ALA B 1 306 ? 104.529 116.405 91.430  1.00 169.22 ? 1083 ALA B CA  1 
ATOM   3928 C  C   . ALA B 1 306 ? 104.774 114.997 91.959  1.00 169.28 ? 1083 ALA B C   1 
ATOM   3929 O  O   . ALA B 1 306 ? 105.358 114.159 91.262  1.00 169.67 ? 1083 ALA B O   1 
ATOM   3930 C  CB  . ALA B 1 306 ? 105.645 117.348 91.877  1.00 169.78 ? 1083 ALA B CB  1 
ATOM   3931 N  N   . ASN B 1 307 ? 104.337 114.717 93.185  1.00 169.09 ? 1084 ASN B N   1 
ATOM   3932 C  CA  . ASN B 1 307 ? 104.505 113.408 93.815  1.00 168.58 ? 1084 ASN B CA  1 
ATOM   3933 C  C   . ASN B 1 307 ? 103.137 112.915 94.264  1.00 170.29 ? 1084 ASN B C   1 
ATOM   3934 O  O   . ASN B 1 307 ? 102.762 113.061 95.436  1.00 172.13 ? 1084 ASN B O   1 
ATOM   3935 C  CB  . ASN B 1 307 ? 105.484 113.479 94.987  1.00 167.68 ? 1084 ASN B CB  1 
ATOM   3936 C  CG  . ASN B 1 307 ? 106.904 113.763 94.542  1.00 168.26 ? 1084 ASN B CG  1 
ATOM   3937 O  OD1 . ASN B 1 307 ? 107.278 113.481 93.404  1.00 169.63 ? 1084 ASN B OD1 1 
ATOM   3938 N  ND2 . ASN B 1 307 ? 107.705 114.325 95.440  1.00 168.75 ? 1084 ASN B ND2 1 
ATOM   3939 N  N   . PRO B 1 308 ? 102.360 112.320 93.354  1.00 149.87 ? 1085 PRO B N   1 
ATOM   3940 C  CA  . PRO B 1 308 ? 101.004 111.881 93.711  1.00 148.81 ? 1085 PRO B CA  1 
ATOM   3941 C  C   . PRO B 1 308 ? 100.954 110.619 94.555  1.00 148.99 ? 1085 PRO B C   1 
ATOM   3942 O  O   . PRO B 1 308 ? 99.864  110.247 95.009  1.00 149.74 ? 1085 PRO B O   1 
ATOM   3943 C  CB  . PRO B 1 308 ? 100.348 111.647 92.344  1.00 146.09 ? 1085 PRO B CB  1 
ATOM   3944 C  CG  . PRO B 1 308 ? 101.483 111.269 91.456  1.00 145.95 ? 1085 PRO B CG  1 
ATOM   3945 C  CD  . PRO B 1 308 ? 102.687 112.033 91.946  1.00 147.29 ? 1085 PRO B CD  1 
ATOM   3946 N  N   . PHE B 1 309 ? 102.082 109.952 94.783  1.00 153.15 ? 1086 PHE B N   1 
ATOM   3947 C  CA  . PHE B 1 309 ? 102.105 108.720 95.560  1.00 153.52 ? 1086 PHE B CA  1 
ATOM   3948 C  C   . PHE B 1 309 ? 102.232 108.962 97.058  1.00 152.96 ? 1086 PHE B C   1 
ATOM   3949 O  O   . PHE B 1 309 ? 102.282 107.995 97.824  1.00 153.80 ? 1086 PHE B O   1 
ATOM   3950 C  CB  . PHE B 1 309 ? 103.246 107.812 95.083  1.00 152.73 ? 1086 PHE B CB  1 
ATOM   3951 C  CG  . PHE B 1 309 ? 104.497 108.552 94.708  1.00 153.45 ? 1086 PHE B CG  1 
ATOM   3952 C  CD1 . PHE B 1 309 ? 105.430 108.894 95.671  1.00 154.29 ? 1086 PHE B CD1 1 
ATOM   3953 C  CD2 . PHE B 1 309 ? 104.745 108.898 93.390  1.00 152.63 ? 1086 PHE B CD2 1 
ATOM   3954 C  CE1 . PHE B 1 309 ? 106.584 109.573 95.329  1.00 154.73 ? 1086 PHE B CE1 1 
ATOM   3955 C  CE2 . PHE B 1 309 ? 105.897 109.577 93.042  1.00 154.04 ? 1086 PHE B CE2 1 
ATOM   3956 C  CZ  . PHE B 1 309 ? 106.818 109.914 94.013  1.00 154.99 ? 1086 PHE B CZ  1 
ATOM   3957 N  N   . ARG B 1 310 ? 102.286 110.221 97.495  1.00 135.44 ? 1087 ARG B N   1 
ATOM   3958 C  CA  . ARG B 1 310 ? 102.338 110.551 98.911  1.00 135.39 ? 1087 ARG B CA  1 
ATOM   3959 C  C   . ARG B 1 310 ? 101.113 111.314 99.392  1.00 136.69 ? 1087 ARG B C   1 
ATOM   3960 O  O   . ARG B 1 310 ? 101.066 111.699 100.566 1.00 138.56 ? 1087 ARG B O   1 
ATOM   3961 C  CB  . ARG B 1 310 ? 103.598 111.369 99.226  1.00 136.25 ? 1087 ARG B CB  1 
ATOM   3962 C  CG  . ARG B 1 310 ? 104.840 110.915 98.483  1.00 137.17 ? 1087 ARG B CG  1 
ATOM   3963 C  CD  . ARG B 1 310 ? 105.960 111.934 98.609  1.00 137.68 ? 1087 ARG B CD  1 
ATOM   3964 N  NE  . ARG B 1 310 ? 106.135 112.387 99.983  1.00 136.63 ? 1087 ARG B NE  1 
ATOM   3965 C  CZ  . ARG B 1 310 ? 107.133 112.014 100.773 1.00 135.67 ? 1087 ARG B CZ  1 
ATOM   3966 N  NH1 . ARG B 1 310 ? 108.069 111.178 100.355 1.00 135.83 ? 1087 ARG B NH1 1 
ATOM   3967 N  NH2 . ARG B 1 310 ? 107.193 112.491 102.013 1.00 136.25 ? 1087 ARG B NH2 1 
ATOM   3968 N  N   . LYS B 1 311 ? 100.124 111.545 98.524  1.00 146.00 ? 1088 LYS B N   1 
ATOM   3969 C  CA  . LYS B 1 311 ? 98.966  112.344 98.911  1.00 147.36 ? 1088 LYS B CA  1 
ATOM   3970 C  C   . LYS B 1 311 ? 98.153  111.663 100.004 1.00 149.24 ? 1088 LYS B C   1 
ATOM   3971 O  O   . LYS B 1 311 ? 97.710  112.319 100.954 1.00 150.21 ? 1088 LYS B O   1 
ATOM   3972 C  CB  . LYS B 1 311 ? 98.092  112.623 97.689  1.00 147.49 ? 1088 LYS B CB  1 
ATOM   3973 C  CG  . LYS B 1 311 ? 97.101  113.758 97.881  1.00 147.91 ? 1088 LYS B CG  1 
ATOM   3974 C  CD  . LYS B 1 311 ? 96.414  114.117 96.575  1.00 148.83 ? 1088 LYS B CD  1 
ATOM   3975 C  CE  . LYS B 1 311 ? 95.445  115.273 96.760  1.00 149.59 ? 1088 LYS B CE  1 
ATOM   3976 N  NZ  . LYS B 1 311 ? 94.944  115.790 95.457  1.00 151.64 ? 1088 LYS B NZ  1 
ATOM   3977 N  N   . SER B 1 312 ? 97.942  110.350 99.888  1.00 153.41 ? 1089 SER B N   1 
ATOM   3978 C  CA  . SER B 1 312 ? 97.147  109.636 100.883 1.00 154.21 ? 1089 SER B CA  1 
ATOM   3979 C  C   . SER B 1 312 ? 97.825  109.660 102.248 1.00 154.21 ? 1089 SER B C   1 
ATOM   3980 O  O   . SER B 1 312 ? 97.182  109.926 103.270 1.00 155.44 ? 1089 SER B O   1 
ATOM   3981 C  CB  . SER B 1 312 ? 96.907  108.197 100.426 1.00 153.55 ? 1089 SER B CB  1 
ATOM   3982 O  OG  . SER B 1 312 ? 98.127  107.559 100.093 1.00 154.76 ? 1089 SER B OG  1 
ATOM   3983 N  N   . TRP B 1 313 ? 99.131  109.384 102.281 1.00 136.56 ? 1090 TRP B N   1 
ATOM   3984 C  CA  . TRP B 1 313 ? 99.865  109.418 103.541 1.00 135.71 ? 1090 TRP B CA  1 
ATOM   3985 C  C   . TRP B 1 313 ? 99.875  110.821 104.134 1.00 135.28 ? 1090 TRP B C   1 
ATOM   3986 O  O   . TRP B 1 313 ? 99.705  110.994 105.347 1.00 137.26 ? 1090 TRP B O   1 
ATOM   3987 C  CB  . TRP B 1 313 ? 101.291 108.911 103.326 1.00 134.86 ? 1090 TRP B CB  1 
ATOM   3988 C  CG  . TRP B 1 313 ? 102.138 108.919 104.561 1.00 138.29 ? 1090 TRP B CG  1 
ATOM   3989 C  CD1 . TRP B 1 313 ? 102.282 107.905 105.461 1.00 140.78 ? 1090 TRP B CD1 1 
ATOM   3990 C  CD2 . TRP B 1 313 ? 102.969 109.989 105.025 1.00 137.56 ? 1090 TRP B CD2 1 
ATOM   3991 N  NE1 . TRP B 1 313 ? 103.147 108.278 106.461 1.00 138.81 ? 1090 TRP B NE1 1 
ATOM   3992 C  CE2 . TRP B 1 313 ? 103.583 109.554 106.216 1.00 137.63 ? 1090 TRP B CE2 1 
ATOM   3993 C  CE3 . TRP B 1 313 ? 103.252 111.273 104.551 1.00 137.58 ? 1090 TRP B CE3 1 
ATOM   3994 C  CZ2 . TRP B 1 313 ? 104.462 110.357 106.939 1.00 137.49 ? 1090 TRP B CZ2 1 
ATOM   3995 C  CZ3 . TRP B 1 313 ? 104.125 112.069 105.271 1.00 139.90 ? 1090 TRP B CZ3 1 
ATOM   3996 C  CH2 . TRP B 1 313 ? 104.719 111.608 106.451 1.00 139.81 ? 1090 TRP B CH2 1 
ATOM   3997 N  N   . ALA B 1 314 ? 100.067 111.838 103.289 1.00 139.15 ? 1091 ALA B N   1 
ATOM   3998 C  CA  . ALA B 1 314 ? 100.063 113.214 103.770 1.00 141.22 ? 1091 ALA B CA  1 
ATOM   3999 C  C   . ALA B 1 314 ? 98.718  113.583 104.379 1.00 145.41 ? 1091 ALA B C   1 
ATOM   4000 O  O   . ALA B 1 314 ? 98.661  114.197 105.451 1.00 148.61 ? 1091 ALA B O   1 
ATOM   4001 C  CB  . ALA B 1 314 ? 100.412 114.167 102.627 1.00 143.73 ? 1091 ALA B CB  1 
ATOM   4002 N  N   . GLN B 1 315 ? 97.622  113.218 103.708 1.00 149.74 ? 1092 GLN B N   1 
ATOM   4003 C  CA  . GLN B 1 315 ? 96.297  113.521 104.236 1.00 148.66 ? 1092 GLN B CA  1 
ATOM   4004 C  C   . GLN B 1 315 ? 96.040  112.775 105.538 1.00 149.16 ? 1092 GLN B C   1 
ATOM   4005 O  O   . GLN B 1 315 ? 95.503  113.347 106.494 1.00 150.81 ? 1092 GLN B O   1 
ATOM   4006 C  CB  . GLN B 1 315 ? 95.228  113.177 103.199 1.00 146.00 ? 1092 GLN B CB  1 
ATOM   4007 C  CG  . GLN B 1 315 ? 94.568  114.389 102.565 1.00 147.80 ? 1092 GLN B CG  1 
ATOM   4008 C  CD  . GLN B 1 315 ? 93.892  114.063 101.249 1.00 150.57 ? 1092 GLN B CD  1 
ATOM   4009 O  OE1 . GLN B 1 315 ? 93.798  112.900 100.858 1.00 151.50 ? 1092 GLN B OE1 1 
ATOM   4010 N  NE2 . GLN B 1 315 ? 93.416  115.091 100.558 1.00 151.43 ? 1092 GLN B NE2 1 
ATOM   4011 N  N   . LYS B 1 316 ? 96.426  111.498 105.599 1.00 149.35 ? 1093 LYS B N   1 
ATOM   4012 C  CA  . LYS B 1 316 ? 96.215  110.721 106.815 1.00 149.83 ? 1093 LYS B CA  1 
ATOM   4013 C  C   . LYS B 1 316 ? 96.998  111.303 107.984 1.00 149.54 ? 1093 LYS B C   1 
ATOM   4014 O  O   . LYS B 1 316 ? 96.515  111.310 109.123 1.00 150.65 ? 1093 LYS B O   1 
ATOM   4015 C  CB  . LYS B 1 316 ? 96.604  109.262 106.580 1.00 149.44 ? 1093 LYS B CB  1 
ATOM   4016 C  CG  . LYS B 1 316 ? 96.326  108.346 107.761 1.00 150.20 ? 1093 LYS B CG  1 
ATOM   4017 C  CD  . LYS B 1 316 ? 97.027  107.006 107.604 1.00 150.83 ? 1093 LYS B CD  1 
ATOM   4018 C  CE  . LYS B 1 316 ? 96.834  106.436 106.208 1.00 151.65 ? 1093 LYS B CE  1 
ATOM   4019 N  NZ  . LYS B 1 316 ? 97.681  105.234 105.976 1.00 151.97 ? 1093 LYS B NZ  1 
ATOM   4020 N  N   . GLN B 1 317 ? 98.209  111.801 107.725 1.00 143.40 ? 1094 GLN B N   1 
ATOM   4021 C  CA  . GLN B 1 317 ? 99.008  112.367 108.806 1.00 142.93 ? 1094 GLN B CA  1 
ATOM   4022 C  C   . GLN B 1 317 ? 98.487  113.735 109.233 1.00 142.64 ? 1094 GLN B C   1 
ATOM   4023 O  O   . GLN B 1 317 ? 98.423  114.030 110.432 1.00 142.49 ? 1094 GLN B O   1 
ATOM   4024 C  CB  . GLN B 1 317 ? 100.475 112.453 108.387 1.00 146.20 ? 1094 GLN B CB  1 
ATOM   4025 C  CG  . GLN B 1 317 ? 101.161 111.101 108.267 1.00 146.72 ? 1094 GLN B CG  1 
ATOM   4026 C  CD  . GLN B 1 317 ? 101.689 110.590 109.594 1.00 147.63 ? 1094 GLN B CD  1 
ATOM   4027 O  OE1 . GLN B 1 317 ? 101.229 110.998 110.660 1.00 146.73 ? 1094 GLN B OE1 1 
ATOM   4028 N  NE2 . GLN B 1 317 ? 102.661 109.686 109.534 1.00 146.69 ? 1094 GLN B NE2 1 
ATOM   4029 N  N   . CYS B 1 318 ? 98.102  114.580 108.276 1.00 153.81 ? 1095 CYS B N   1 
ATOM   4030 C  CA  . CYS B 1 318 ? 97.657  115.930 108.599 1.00 155.02 ? 1095 CYS B CA  1 
ATOM   4031 C  C   . CYS B 1 318 ? 96.191  115.999 109.006 1.00 155.14 ? 1095 CYS B C   1 
ATOM   4032 O  O   . CYS B 1 318 ? 95.718  117.083 109.363 1.00 156.66 ? 1095 CYS B O   1 
ATOM   4033 C  CB  . CYS B 1 318 ? 97.905  116.868 107.413 1.00 156.44 ? 1095 CYS B CB  1 
ATOM   4034 S  SG  . CYS B 1 318 ? 99.645  117.051 106.942 1.00 162.87 ? 1095 CYS B SG  1 
ATOM   4035 N  N   . SER B 1 319 ? 95.459  114.882 108.960 1.00 149.24 ? 1096 SER B N   1 
ATOM   4036 C  CA  . SER B 1 319 ? 94.077  114.881 109.424 1.00 149.93 ? 1096 SER B CA  1 
ATOM   4037 C  C   . SER B 1 319 ? 93.949  115.136 110.921 1.00 149.22 ? 1096 SER B C   1 
ATOM   4038 O  O   . SER B 1 319 ? 92.836  115.399 111.390 1.00 149.29 ? 1096 SER B O   1 
ATOM   4039 C  CB  . SER B 1 319 ? 93.409  113.551 109.073 1.00 148.77 ? 1096 SER B CB  1 
ATOM   4040 O  OG  . SER B 1 319 ? 94.042  112.472 109.737 1.00 149.52 ? 1096 SER B OG  1 
ATOM   4041 N  N   . ILE B 1 320 ? 95.047  115.061 111.677 1.00 135.15 ? 1097 ILE B N   1 
ATOM   4042 C  CA  . ILE B 1 320 ? 94.994  115.319 113.111 1.00 134.31 ? 1097 ILE B CA  1 
ATOM   4043 C  C   . ILE B 1 320 ? 94.589  116.756 113.408 1.00 135.71 ? 1097 ILE B C   1 
ATOM   4044 O  O   . ILE B 1 320 ? 94.061  117.039 114.489 1.00 137.28 ? 1097 ILE B O   1 
ATOM   4045 C  CB  . ILE B 1 320 ? 96.352  114.971 113.762 1.00 133.24 ? 1097 ILE B CB  1 
ATOM   4046 C  CG1 . ILE B 1 320 ? 96.227  114.924 115.286 1.00 134.28 ? 1097 ILE B CG1 1 
ATOM   4047 C  CG2 . ILE B 1 320 ? 97.425  115.963 113.337 1.00 131.80 ? 1097 ILE B CG2 1 
ATOM   4048 C  CD1 . ILE B 1 320 ? 95.092  114.054 115.780 1.00 136.31 ? 1097 ILE B CD1 1 
ATOM   4049 N  N   . LEU B 1 321 ? 94.817  117.677 112.468 1.00 139.15 ? 1098 LEU B N   1 
ATOM   4050 C  CA  . LEU B 1 321 ? 94.424  119.066 112.683 1.00 137.68 ? 1098 LEU B CA  1 
ATOM   4051 C  C   . LEU B 1 321 ? 92.908  119.209 112.745 1.00 137.24 ? 1098 LEU B C   1 
ATOM   4052 O  O   . LEU B 1 321 ? 92.387  120.025 113.515 1.00 140.02 ? 1098 LEU B O   1 
ATOM   4053 C  CB  . LEU B 1 321 ? 95.002  119.952 111.581 1.00 137.06 ? 1098 LEU B CB  1 
ATOM   4054 C  CG  . LEU B 1 321 ? 96.494  120.279 111.675 1.00 137.48 ? 1098 LEU B CG  1 
ATOM   4055 C  CD1 . LEU B 1 321 ? 96.832  121.482 110.810 1.00 137.98 ? 1098 LEU B CD1 1 
ATOM   4056 C  CD2 . LEU B 1 321 ? 96.906  120.521 113.118 1.00 138.83 ? 1098 LEU B CD2 1 
ATOM   4057 N  N   . HIS B 1 322 ? 92.187  118.429 111.946 1.00 139.41 ? 1099 HIS B N   1 
ATOM   4058 C  CA  . HIS B 1 322 ? 90.731  118.471 111.921 1.00 140.46 ? 1099 HIS B CA  1 
ATOM   4059 C  C   . HIS B 1 322 ? 90.093  117.524 112.929 1.00 143.86 ? 1099 HIS B C   1 
ATOM   4060 O  O   . HIS B 1 322 ? 88.862  117.428 112.972 1.00 143.31 ? 1099 HIS B O   1 
ATOM   4061 C  CB  . HIS B 1 322 ? 90.219  118.144 110.515 1.00 142.40 ? 1099 HIS B CB  1 
ATOM   4062 C  CG  . HIS B 1 322 ? 90.202  119.321 109.591 1.00 144.80 ? 1099 HIS B CG  1 
ATOM   4063 N  ND1 . HIS B 1 322 ? 90.455  119.211 108.240 1.00 146.69 ? 1099 HIS B ND1 1 
ATOM   4064 C  CD2 . HIS B 1 322 ? 89.960  120.633 109.822 1.00 144.12 ? 1099 HIS B CD2 1 
ATOM   4065 C  CE1 . HIS B 1 322 ? 90.371  120.404 107.680 1.00 145.63 ? 1099 HIS B CE1 1 
ATOM   4066 N  NE2 . HIS B 1 322 ? 90.071  121.285 108.618 1.00 145.90 ? 1099 HIS B NE2 1 
ATOM   4067 N  N   . GLY B 1 323 ? 90.892  116.828 113.736 1.00 157.37 ? 1100 GLY B N   1 
ATOM   4068 C  CA  . GLY B 1 323 ? 90.360  115.898 114.701 1.00 156.92 ? 1100 GLY B CA  1 
ATOM   4069 C  C   . GLY B 1 323 ? 89.819  116.594 115.930 1.00 157.45 ? 1100 GLY B C   1 
ATOM   4070 O  O   . GLY B 1 323 ? 89.856  117.824 116.066 1.00 157.77 ? 1100 GLY B O   1 
ATOM   4071 N  N   . PRO B 1 324 ? 89.298  115.790 116.862 1.00 155.05 ? 1101 PRO B N   1 
ATOM   4072 C  CA  . PRO B 1 324 ? 88.728  116.359 118.093 1.00 154.38 ? 1101 PRO B CA  1 
ATOM   4073 C  C   . PRO B 1 324 ? 89.767  116.886 119.067 1.00 153.36 ? 1101 PRO B C   1 
ATOM   4074 O  O   . PRO B 1 324 ? 89.386  117.503 120.070 1.00 154.07 ? 1101 PRO B O   1 
ATOM   4075 C  CB  . PRO B 1 324 ? 87.955  115.181 118.695 1.00 154.12 ? 1101 PRO B CB  1 
ATOM   4076 C  CG  . PRO B 1 324 ? 88.691  113.978 118.207 1.00 154.51 ? 1101 PRO B CG  1 
ATOM   4077 C  CD  . PRO B 1 324 ? 89.187  114.321 116.826 1.00 154.54 ? 1101 PRO B CD  1 
ATOM   4078 N  N   . THR B 1 325 ? 91.058  116.659 118.814 1.00 144.14 ? 1102 THR B N   1 
ATOM   4079 C  CA  . THR B 1 325 ? 92.088  117.139 119.731 1.00 144.86 ? 1102 THR B CA  1 
ATOM   4080 C  C   . THR B 1 325 ? 92.123  118.662 119.777 1.00 146.17 ? 1102 THR B C   1 
ATOM   4081 O  O   . THR B 1 325 ? 92.263  119.255 120.852 1.00 145.20 ? 1102 THR B O   1 
ATOM   4082 C  CB  . THR B 1 325 ? 93.453  116.584 119.325 1.00 144.52 ? 1102 THR B CB  1 
ATOM   4083 O  OG1 . THR B 1 325 ? 93.383  115.156 119.239 1.00 144.63 ? 1102 THR B OG1 1 
ATOM   4084 C  CG2 . THR B 1 325 ? 94.512  116.972 120.345 1.00 144.18 ? 1102 THR B CG2 1 
ATOM   4085 N  N   . PHE B 1 326 ? 91.988  119.311 118.623 1.00 149.55 ? 1103 PHE B N   1 
ATOM   4086 C  CA  . PHE B 1 326 ? 92.046  120.768 118.521 1.00 149.23 ? 1103 PHE B CA  1 
ATOM   4087 C  C   . PHE B 1 326 ? 90.658  121.391 118.453 1.00 150.75 ? 1103 PHE B C   1 
ATOM   4088 O  O   . PHE B 1 326 ? 90.447  122.387 117.755 1.00 152.87 ? 1103 PHE B O   1 
ATOM   4089 C  CB  . PHE B 1 326 ? 92.878  121.179 117.310 1.00 150.10 ? 1103 PHE B CB  1 
ATOM   4090 C  CG  . PHE B 1 326 ? 94.332  120.819 117.425 1.00 149.13 ? 1103 PHE B CG  1 
ATOM   4091 C  CD1 . PHE B 1 326 ? 94.789  119.582 117.004 1.00 149.89 ? 1103 PHE B CD1 1 
ATOM   4092 C  CD2 . PHE B 1 326 ? 95.242  121.718 117.955 1.00 148.57 ? 1103 PHE B CD2 1 
ATOM   4093 C  CE1 . PHE B 1 326 ? 96.126  119.249 117.109 1.00 149.40 ? 1103 PHE B CE1 1 
ATOM   4094 C  CE2 . PHE B 1 326 ? 96.579  121.391 118.062 1.00 147.30 ? 1103 PHE B CE2 1 
ATOM   4095 C  CZ  . PHE B 1 326 ? 97.022  120.155 117.638 1.00 146.47 ? 1103 PHE B CZ  1 
ATOM   4096 N  N   . ALA B 1 327 ? 89.690  120.816 119.171 1.00 160.19 ? 1104 ALA B N   1 
ATOM   4097 C  CA  . ALA B 1 327 ? 88.339  121.369 119.170 1.00 161.48 ? 1104 ALA B CA  1 
ATOM   4098 C  C   . ALA B 1 327 ? 88.317  122.773 119.759 1.00 161.47 ? 1104 ALA B C   1 
ATOM   4099 O  O   . ALA B 1 327 ? 87.615  123.656 119.252 1.00 161.24 ? 1104 ALA B O   1 
ATOM   4100 C  CB  . ALA B 1 327 ? 87.393  120.447 119.939 1.00 160.89 ? 1104 ALA B CB  1 
ATOM   4101 N  N   . ALA B 1 328 ? 89.075  122.998 120.835 1.00 156.87 ? 1105 ALA B N   1 
ATOM   4102 C  CA  . ALA B 1 328 ? 89.143  124.331 121.424 1.00 158.03 ? 1105 ALA B CA  1 
ATOM   4103 C  C   . ALA B 1 328 ? 89.804  125.322 120.475 1.00 157.85 ? 1105 ALA B C   1 
ATOM   4104 O  O   . ALA B 1 328 ? 89.366  126.474 120.368 1.00 157.49 ? 1105 ALA B O   1 
ATOM   4105 C  CB  . ALA B 1 328 ? 89.892  124.279 122.755 1.00 158.02 ? 1105 ALA B CB  1 
ATOM   4106 N  N   . CYS B 1 329 ? 90.859  124.895 119.777 1.00 171.57 ? 1106 CYS B N   1 
ATOM   4107 C  CA  . CYS B 1 329 ? 91.532  125.784 118.837 1.00 171.23 ? 1106 CYS B CA  1 
ATOM   4108 C  C   . CYS B 1 329 ? 90.659  126.093 117.627 1.00 172.21 ? 1106 CYS B C   1 
ATOM   4109 O  O   . CYS B 1 329 ? 90.801  127.160 117.020 1.00 173.13 ? 1106 CYS B O   1 
ATOM   4110 C  CB  . CYS B 1 329 ? 92.858  125.170 118.387 1.00 173.25 ? 1106 CYS B CB  1 
ATOM   4111 S  SG  . CYS B 1 329 ? 94.006  124.782 119.728 1.00 180.18 ? 1106 CYS B SG  1 
ATOM   4112 N  N   . HIS B 1 330 ? 89.761  125.174 117.261 1.00 160.98 ? 1107 HIS B N   1 
ATOM   4113 C  CA  . HIS B 1 330 ? 88.897  125.404 116.106 1.00 159.55 ? 1107 HIS B CA  1 
ATOM   4114 C  C   . HIS B 1 330 ? 87.986  126.608 116.308 1.00 159.63 ? 1107 HIS B C   1 
ATOM   4115 O  O   . HIS B 1 330 ? 87.577  127.246 115.332 1.00 160.03 ? 1107 HIS B O   1 
ATOM   4116 C  CB  . HIS B 1 330 ? 88.060  124.158 115.817 1.00 157.47 ? 1107 HIS B CB  1 
ATOM   4117 C  CG  . HIS B 1 330 ? 88.856  123.000 115.302 1.00 158.35 ? 1107 HIS B CG  1 
ATOM   4118 N  ND1 . HIS B 1 330 ? 88.543  121.691 115.598 1.00 159.26 ? 1107 HIS B ND1 1 
ATOM   4119 C  CD2 . HIS B 1 330 ? 89.955  122.954 114.512 1.00 160.54 ? 1107 HIS B CD2 1 
ATOM   4120 C  CE1 . HIS B 1 330 ? 89.413  120.889 115.012 1.00 161.39 ? 1107 HIS B CE1 1 
ATOM   4121 N  NE2 . HIS B 1 330 ? 90.280  121.630 114.347 1.00 163.04 ? 1107 HIS B NE2 1 
ATOM   4122 N  N   . ALA B 1 331 ? 87.656  126.934 117.558 1.00 147.89 ? 1108 ALA B N   1 
ATOM   4123 C  CA  . ALA B 1 331 ? 86.754  128.043 117.839 1.00 147.65 ? 1108 ALA B CA  1 
ATOM   4124 C  C   . ALA B 1 331 ? 87.449  129.397 117.842 1.00 148.53 ? 1108 ALA B C   1 
ATOM   4125 O  O   . ALA B 1 331 ? 86.767  130.422 117.951 1.00 147.05 ? 1108 ALA B O   1 
ATOM   4126 C  CB  . ALA B 1 331 ? 86.057  127.824 119.184 1.00 147.24 ? 1108 ALA B CB  1 
ATOM   4127 N  N   . HIS B 1 332 ? 88.773  129.433 117.728 1.00 166.34 ? 1109 HIS B N   1 
ATOM   4128 C  CA  . HIS B 1 332 ? 89.517  130.686 117.760 1.00 166.64 ? 1109 HIS B CA  1 
ATOM   4129 C  C   . HIS B 1 332 ? 90.377  130.913 116.528 1.00 167.30 ? 1109 HIS B C   1 
ATOM   4130 O  O   . HIS B 1 332 ? 90.441  132.039 116.029 1.00 167.53 ? 1109 HIS B O   1 
ATOM   4131 C  CB  . HIS B 1 332 ? 90.404  130.740 119.013 1.00 167.55 ? 1109 HIS B CB  1 
ATOM   4132 C  CG  . HIS B 1 332 ? 89.634  130.733 120.297 1.00 168.92 ? 1109 HIS B CG  1 
ATOM   4133 N  ND1 . HIS B 1 332 ? 88.878  131.806 120.718 1.00 168.20 ? 1109 HIS B ND1 1 
ATOM   4134 C  CD2 . HIS B 1 332 ? 89.503  129.783 121.252 1.00 169.75 ? 1109 HIS B CD2 1 
ATOM   4135 C  CE1 . HIS B 1 332 ? 88.316  131.517 121.877 1.00 168.01 ? 1109 HIS B CE1 1 
ATOM   4136 N  NE2 . HIS B 1 332 ? 88.679  130.295 122.224 1.00 168.97 ? 1109 HIS B NE2 1 
ATOM   4137 N  N   . VAL B 1 333 ? 91.042  129.878 116.023 1.00 168.93 ? 1110 VAL B N   1 
ATOM   4138 C  CA  . VAL B 1 333 ? 91.940  129.992 114.880 1.00 169.53 ? 1110 VAL B CA  1 
ATOM   4139 C  C   . VAL B 1 333 ? 91.462  129.041 113.793 1.00 170.52 ? 1110 VAL B C   1 
ATOM   4140 O  O   . VAL B 1 333 ? 91.243  127.852 114.053 1.00 172.70 ? 1110 VAL B O   1 
ATOM   4141 C  CB  . VAL B 1 333 ? 93.398  129.687 115.270 1.00 167.14 ? 1110 VAL B CB  1 
ATOM   4142 C  CG1 . VAL B 1 333 ? 94.295  129.718 114.043 1.00 167.60 ? 1110 VAL B CG1 1 
ATOM   4143 C  CG2 . VAL B 1 333 ? 93.884  130.675 116.319 1.00 166.93 ? 1110 VAL B CG2 1 
ATOM   4144 N  N   . GLU B 1 334 ? 91.302  129.563 112.584 1.00 165.30 ? 1111 GLU B N   1 
ATOM   4145 C  CA  . GLU B 1 334 ? 90.886  128.739 111.455 1.00 163.45 ? 1111 GLU B CA  1 
ATOM   4146 C  C   . GLU B 1 334 ? 92.022  127.809 111.051 1.00 163.96 ? 1111 GLU B C   1 
ATOM   4147 O  O   . GLU B 1 334 ? 93.132  128.284 110.776 1.00 166.16 ? 1111 GLU B O   1 
ATOM   4148 C  CB  . GLU B 1 334 ? 90.474  129.618 110.279 1.00 164.67 ? 1111 GLU B CB  1 
ATOM   4149 C  CG  . GLU B 1 334 ? 89.139  130.319 110.465 1.00 165.85 ? 1111 GLU B CG  1 
ATOM   4150 C  CD  . GLU B 1 334 ? 87.958  129.390 110.256 1.00 168.96 ? 1111 GLU B CD  1 
ATOM   4151 O  OE1 . GLU B 1 334 ? 88.161  128.273 109.735 1.00 168.40 ? 1111 GLU B OE1 1 
ATOM   4152 O  OE2 . GLU B 1 334 ? 86.826  129.778 110.615 1.00 170.59 ? 1111 GLU B OE2 1 
ATOM   4153 N  N   . PRO B 1 335 ? 91.803  126.496 111.000 1.00 153.97 ? 1112 PRO B N   1 
ATOM   4154 C  CA  . PRO B 1 335 ? 92.884  125.558 110.669 1.00 156.56 ? 1112 PRO B CA  1 
ATOM   4155 C  C   . PRO B 1 335 ? 93.002  125.199 109.194 1.00 157.10 ? 1112 PRO B C   1 
ATOM   4156 O  O   . PRO B 1 335 ? 93.805  124.321 108.863 1.00 157.81 ? 1112 PRO B O   1 
ATOM   4157 C  CB  . PRO B 1 335 ? 92.491  124.320 111.485 1.00 156.63 ? 1112 PRO B CB  1 
ATOM   4158 C  CG  . PRO B 1 335 ? 90.988  124.355 111.503 1.00 155.97 ? 1112 PRO B CG  1 
ATOM   4159 C  CD  . PRO B 1 335 ? 90.552  125.796 111.335 1.00 153.97 ? 1112 PRO B CD  1 
ATOM   4160 N  N   . ALA B 1 336 ? 92.235  125.838 108.309 1.00 154.05 ? 1113 ALA B N   1 
ATOM   4161 C  CA  . ALA B 1 336 ? 92.295  125.493 106.891 1.00 154.08 ? 1113 ALA B CA  1 
ATOM   4162 C  C   . ALA B 1 336 ? 93.660  125.823 106.301 1.00 154.03 ? 1113 ALA B C   1 
ATOM   4163 O  O   . ALA B 1 336 ? 94.257  125.006 105.588 1.00 156.58 ? 1113 ALA B O   1 
ATOM   4164 C  CB  . ALA B 1 336 ? 91.187  126.220 106.129 1.00 154.22 ? 1113 ALA B CB  1 
ATOM   4165 N  N   . ARG B 1 337 ? 94.173  127.021 106.591 1.00 154.01 ? 1114 ARG B N   1 
ATOM   4166 C  CA  . ARG B 1 337 ? 95.484  127.407 106.080 1.00 156.63 ? 1114 ARG B CA  1 
ATOM   4167 C  C   . ARG B 1 337 ? 96.577  126.504 106.633 1.00 157.12 ? 1114 ARG B C   1 
ATOM   4168 O  O   . ARG B 1 337 ? 97.475  126.079 105.897 1.00 159.49 ? 1114 ARG B O   1 
ATOM   4169 C  CB  . ARG B 1 337 ? 95.770  128.869 106.423 1.00 155.56 ? 1114 ARG B CB  1 
ATOM   4170 C  CG  . ARG B 1 337 ? 97.149  129.347 106.002 1.00 157.26 ? 1114 ARG B CG  1 
ATOM   4171 C  CD  . ARG B 1 337 ? 97.335  130.827 106.295 1.00 157.70 ? 1114 ARG B CD  1 
ATOM   4172 N  NE  . ARG B 1 337 ? 97.491  131.088 107.721 1.00 159.77 ? 1114 ARG B NE  1 
ATOM   4173 C  CZ  . ARG B 1 337 ? 96.558  131.633 108.489 1.00 159.03 ? 1114 ARG B CZ  1 
ATOM   4174 N  NH1 . ARG B 1 337 ? 95.381  131.989 108.001 1.00 158.50 ? 1114 ARG B NH1 1 
ATOM   4175 N  NH2 . ARG B 1 337 ? 96.812  131.826 109.780 1.00 156.97 ? 1114 ARG B NH2 1 
ATOM   4176 N  N   . TYR B 1 338 ? 96.513  126.191 107.929 1.00 143.31 ? 1115 TYR B N   1 
ATOM   4177 C  CA  . TYR B 1 338 ? 97.518  125.318 108.526 1.00 143.61 ? 1115 TYR B CA  1 
ATOM   4178 C  C   . TYR B 1 338 ? 97.411  123.898 107.986 1.00 144.66 ? 1115 TYR B C   1 
ATOM   4179 O  O   . TYR B 1 338 ? 98.428  123.223 107.798 1.00 144.82 ? 1115 TYR B O   1 
ATOM   4180 C  CB  . TYR B 1 338 ? 97.387  125.335 110.048 1.00 143.26 ? 1115 TYR B CB  1 
ATOM   4181 C  CG  . TYR B 1 338 ? 97.662  126.689 110.665 1.00 145.68 ? 1115 TYR B CG  1 
ATOM   4182 C  CD1 . TYR B 1 338 ? 96.665  127.652 110.748 1.00 146.91 ? 1115 TYR B CD1 1 
ATOM   4183 C  CD2 . TYR B 1 338 ? 98.920  127.004 111.161 1.00 145.76 ? 1115 TYR B CD2 1 
ATOM   4184 C  CE1 . TYR B 1 338 ? 96.913  128.890 111.310 1.00 146.06 ? 1115 TYR B CE1 1 
ATOM   4185 C  CE2 . TYR B 1 338 ? 99.177  128.239 111.724 1.00 144.45 ? 1115 TYR B CE2 1 
ATOM   4186 C  CZ  . TYR B 1 338 ? 98.170  129.178 111.795 1.00 144.06 ? 1115 TYR B CZ  1 
ATOM   4187 O  OH  . TYR B 1 338 ? 98.421  130.409 112.355 1.00 143.15 ? 1115 TYR B OH  1 
ATOM   4188 N  N   . TYR B 1 339 ? 96.189  123.427 107.723 1.00 150.77 ? 1116 TYR B N   1 
ATOM   4189 C  CA  . TYR B 1 339 ? 96.024  122.105 107.124 1.00 151.38 ? 1116 TYR B CA  1 
ATOM   4190 C  C   . TYR B 1 339 ? 96.613  122.061 105.720 1.00 152.86 ? 1116 TYR B C   1 
ATOM   4191 O  O   . TYR B 1 339 ? 97.288  121.091 105.348 1.00 155.17 ? 1116 TYR B O   1 
ATOM   4192 C  CB  . TYR B 1 339 ? 94.545  121.723 107.100 1.00 151.12 ? 1116 TYR B CB  1 
ATOM   4193 C  CG  . TYR B 1 339 ? 94.264  120.389 106.447 1.00 151.80 ? 1116 TYR B CG  1 
ATOM   4194 C  CD1 . TYR B 1 339 ? 94.592  119.200 107.084 1.00 152.15 ? 1116 TYR B CD1 1 
ATOM   4195 C  CD2 . TYR B 1 339 ? 93.667  120.319 105.196 1.00 152.79 ? 1116 TYR B CD2 1 
ATOM   4196 C  CE1 . TYR B 1 339 ? 94.335  117.979 106.492 1.00 152.07 ? 1116 TYR B CE1 1 
ATOM   4197 C  CE2 . TYR B 1 339 ? 93.407  119.103 104.596 1.00 154.08 ? 1116 TYR B CE2 1 
ATOM   4198 C  CZ  . TYR B 1 339 ? 93.743  117.936 105.248 1.00 154.26 ? 1116 TYR B CZ  1 
ATOM   4199 O  OH  . TYR B 1 339 ? 93.486  116.722 104.655 1.00 155.99 ? 1116 TYR B OH  1 
ATOM   4200 N  N   . GLU B 1 340 ? 96.369  123.105 104.923 1.00 160.38 ? 1117 GLU B N   1 
ATOM   4201 C  CA  . GLU B 1 340 ? 96.955  123.166 103.588 1.00 159.62 ? 1117 GLU B CA  1 
ATOM   4202 C  C   . GLU B 1 340 ? 98.475  123.222 103.659 1.00 160.08 ? 1117 GLU B C   1 
ATOM   4203 O  O   . GLU B 1 340 ? 99.166  122.592 102.850 1.00 162.85 ? 1117 GLU B O   1 
ATOM   4204 C  CB  . GLU B 1 340 ? 96.407  124.374 102.829 1.00 159.85 ? 1117 GLU B CB  1 
ATOM   4205 C  CG  . GLU B 1 340 ? 95.303  124.037 101.843 1.00 162.22 ? 1117 GLU B CG  1 
ATOM   4206 C  CD  . GLU B 1 340 ? 95.016  125.173 100.881 1.00 164.76 ? 1117 GLU B CD  1 
ATOM   4207 O  OE1 . GLU B 1 340 ? 95.927  125.992 100.638 1.00 165.96 ? 1117 GLU B OE1 1 
ATOM   4208 O  OE2 . GLU B 1 340 ? 93.880  125.247 100.368 1.00 165.04 ? 1117 GLU B OE2 1 
ATOM   4209 N  N   . ALA B 1 341 ? 99.013  123.975 104.622 1.00 147.24 ? 1118 ALA B N   1 
ATOM   4210 C  CA  . ALA B 1 341 ? 100.460 124.035 104.794 1.00 147.78 ? 1118 ALA B CA  1 
ATOM   4211 C  C   . ALA B 1 341 ? 101.027 122.673 105.173 1.00 147.42 ? 1118 ALA B C   1 
ATOM   4212 O  O   . ALA B 1 341 ? 102.080 122.270 104.668 1.00 149.55 ? 1118 ALA B O   1 
ATOM   4213 C  CB  . ALA B 1 341 ? 100.822 125.081 105.848 1.00 148.09 ? 1118 ALA B CB  1 
ATOM   4214 N  N   . CYS B 1 342 ? 100.342 121.951 106.064 1.00 146.62 ? 1119 CYS B N   1 
ATOM   4215 C  CA  . CYS B 1 342 ? 100.779 120.608 106.430 1.00 146.49 ? 1119 CYS B CA  1 
ATOM   4216 C  C   . CYS B 1 342 ? 100.784 119.685 105.221 1.00 148.25 ? 1119 CYS B C   1 
ATOM   4217 O  O   . CYS B 1 342 ? 101.741 118.930 105.010 1.00 149.33 ? 1119 CYS B O   1 
ATOM   4218 C  CB  . CYS B 1 342 ? 99.873  120.043 107.526 1.00 149.63 ? 1119 CYS B CB  1 
ATOM   4219 S  SG  . CYS B 1 342 ? 100.394 118.448 108.216 1.00 155.91 ? 1119 CYS B SG  1 
ATOM   4220 N  N   . VAL B 1 343 ? 99.721  119.733 104.416 1.00 140.30 ? 1120 VAL B N   1 
ATOM   4221 C  CA  . VAL B 1 343 ? 99.635  118.868 103.241 1.00 137.90 ? 1120 VAL B CA  1 
ATOM   4222 C  C   . VAL B 1 343 ? 100.755 119.193 102.260 1.00 140.04 ? 1120 VAL B C   1 
ATOM   4223 O  O   . VAL B 1 343 ? 101.428 118.295 101.736 1.00 138.40 ? 1120 VAL B O   1 
ATOM   4224 C  CB  . VAL B 1 343 ? 98.250  118.994 102.583 1.00 136.04 ? 1120 VAL B CB  1 
ATOM   4225 C  CG1 . VAL B 1 343 ? 98.249  118.341 101.212 1.00 137.32 ? 1120 VAL B CG1 1 
ATOM   4226 C  CG2 . VAL B 1 343 ? 97.185  118.373 103.473 1.00 135.97 ? 1120 VAL B CG2 1 
ATOM   4227 N  N   . ASN B 1 344 ? 100.981 120.485 102.007 1.00 152.43 ? 1121 ASN B N   1 
ATOM   4228 C  CA  . ASN B 1 344 ? 102.022 120.884 101.064 1.00 149.57 ? 1121 ASN B CA  1 
ATOM   4229 C  C   . ASN B 1 344 ? 103.406 120.490 101.565 1.00 150.76 ? 1121 ASN B C   1 
ATOM   4230 O  O   . ASN B 1 344 ? 104.241 120.011 100.788 1.00 152.57 ? 1121 ASN B O   1 
ATOM   4231 C  CB  . ASN B 1 344 ? 101.952 122.390 100.813 1.00 150.19 ? 1121 ASN B CB  1 
ATOM   4232 C  CG  . ASN B 1 344 ? 100.959 122.753 99.727  1.00 152.25 ? 1121 ASN B CG  1 
ATOM   4233 O  OD1 . ASN B 1 344 ? 100.110 121.945 99.351  1.00 151.14 ? 1121 ASN B OD1 1 
ATOM   4234 N  ND2 . ASN B 1 344 ? 101.062 123.974 99.215  1.00 152.83 ? 1121 ASN B ND2 1 
ATOM   4235 N  N   . ASP B 1 345 ? 103.669 120.681 102.860 1.00 166.96 ? 1122 ASP B N   1 
ATOM   4236 C  CA  . ASP B 1 345 ? 104.968 120.315 103.411 1.00 167.65 ? 1122 ASP B CA  1 
ATOM   4237 C  C   . ASP B 1 345 ? 105.192 118.811 103.344 1.00 167.29 ? 1122 ASP B C   1 
ATOM   4238 O  O   . ASP B 1 345 ? 106.285 118.358 102.984 1.00 169.00 ? 1122 ASP B O   1 
ATOM   4239 C  CB  . ASP B 1 345 ? 105.087 120.813 104.851 1.00 167.89 ? 1122 ASP B CB  1 
ATOM   4240 C  CG  . ASP B 1 345 ? 105.439 122.284 104.931 1.00 169.02 ? 1122 ASP B CG  1 
ATOM   4241 O  OD1 . ASP B 1 345 ? 104.954 123.060 104.080 1.00 168.12 ? 1122 ASP B OD1 1 
ATOM   4242 O  OD2 . ASP B 1 345 ? 106.202 122.666 105.843 1.00 170.44 ? 1122 ASP B OD2 1 
ATOM   4243 N  N   . ALA B 1 346 ? 104.171 118.019 103.680 1.00 149.10 ? 1123 ALA B N   1 
ATOM   4244 C  CA  . ALA B 1 346 ? 104.316 116.570 103.603 1.00 147.22 ? 1123 ALA B CA  1 
ATOM   4245 C  C   . ALA B 1 346 ? 104.494 116.099 102.166 1.00 148.39 ? 1123 ALA B C   1 
ATOM   4246 O  O   . ALA B 1 346 ? 105.204 115.116 101.923 1.00 149.40 ? 1123 ALA B O   1 
ATOM   4247 C  CB  . ALA B 1 346 ? 103.111 115.886 104.246 1.00 148.36 ? 1123 ALA B CB  1 
ATOM   4248 N  N   . CYS B 1 347 ? 103.866 116.781 101.205 1.00 157.48 ? 1124 CYS B N   1 
ATOM   4249 C  CA  . CYS B 1 347 ? 104.068 116.423 99.805  1.00 156.97 ? 1124 CYS B CA  1 
ATOM   4250 C  C   . CYS B 1 347 ? 105.450 116.831 99.311  1.00 156.81 ? 1124 CYS B C   1 
ATOM   4251 O  O   . CYS B 1 347 ? 106.009 116.172 98.428  1.00 154.29 ? 1124 CYS B O   1 
ATOM   4252 C  CB  . CYS B 1 347 ? 102.985 117.064 98.936  1.00 160.42 ? 1124 CYS B CB  1 
ATOM   4253 S  SG  . CYS B 1 347 ? 101.486 116.069 98.738  1.00 169.23 ? 1124 CYS B SG  1 
ATOM   4254 N  N   . ALA B 1 348 ? 106.017 117.904 99.864  1.00 161.16 ? 1125 ALA B N   1 
ATOM   4255 C  CA  . ALA B 1 348 ? 107.301 118.410 99.396  1.00 160.40 ? 1125 ALA B CA  1 
ATOM   4256 C  C   . ALA B 1 348 ? 108.488 117.842 100.162 1.00 161.74 ? 1125 ALA B C   1 
ATOM   4257 O  O   . ALA B 1 348 ? 109.564 117.669 99.577  1.00 162.65 ? 1125 ALA B O   1 
ATOM   4258 C  CB  . ALA B 1 348 ? 107.330 119.938 99.482  1.00 161.41 ? 1125 ALA B CB  1 
ATOM   4259 N  N   . CYS B 1 349 ? 108.324 117.546 101.451 1.00 183.58 ? 1126 CYS B N   1 
ATOM   4260 C  CA  . CYS B 1 349 ? 109.427 117.050 102.265 1.00 183.54 ? 1126 CYS B CA  1 
ATOM   4261 C  C   . CYS B 1 349 ? 109.746 115.603 101.910 1.00 181.80 ? 1126 CYS B C   1 
ATOM   4262 O  O   . CYS B 1 349 ? 109.490 114.691 102.702 1.00 183.98 ? 1126 CYS B O   1 
ATOM   4263 C  CB  . CYS B 1 349 ? 109.088 117.178 103.754 1.00 185.19 ? 1126 CYS B CB  1 
ATOM   4264 S  SG  . CYS B 1 349 ? 110.487 117.009 104.887 1.00 189.07 ? 1126 CYS B SG  1 
ATOM   4265 N  N   . ASP B 1 350 ? 110.308 115.383 100.720 1.00 153.67 ? 1127 ASP B N   1 
ATOM   4266 C  CA  . ASP B 1 350 ? 110.599 114.044 100.223 1.00 154.50 ? 1127 ASP B CA  1 
ATOM   4267 C  C   . ASP B 1 350 ? 112.092 113.770 100.096 1.00 153.68 ? 1127 ASP B C   1 
ATOM   4268 O  O   . ASP B 1 350 ? 112.477 112.762 99.493  1.00 153.24 ? 1127 ASP B O   1 
ATOM   4269 C  CB  . ASP B 1 350 ? 109.909 113.822 98.874  1.00 155.89 ? 1127 ASP B CB  1 
ATOM   4270 C  CG  . ASP B 1 350 ? 110.131 114.970 97.906  1.00 156.43 ? 1127 ASP B CG  1 
ATOM   4271 O  OD1 . ASP B 1 350 ? 111.167 115.660 98.015  1.00 155.16 ? 1127 ASP B OD1 1 
ATOM   4272 O  OD2 . ASP B 1 350 ? 109.266 115.183 97.031  1.00 158.04 ? 1127 ASP B OD2 1 
ATOM   4273 N  N   . SER B 1 351 ? 112.940 114.636 100.641 1.00 148.30 ? 1128 SER B N   1 
ATOM   4274 C  CA  . SER B 1 351 ? 114.383 114.453 100.573 1.00 148.76 ? 1128 SER B CA  1 
ATOM   4275 C  C   . SER B 1 351 ? 114.930 113.619 101.723 1.00 149.11 ? 1128 SER B C   1 
ATOM   4276 O  O   . SER B 1 351 ? 116.147 113.428 101.807 1.00 147.45 ? 1128 SER B O   1 
ATOM   4277 C  CB  . SER B 1 351 ? 115.087 115.812 100.546 1.00 150.98 ? 1128 SER B CB  1 
ATOM   4278 O  OG  . SER B 1 351 ? 116.378 115.705 99.972  1.00 150.67 ? 1128 SER B OG  1 
ATOM   4279 N  N   . GLY B 1 352 ? 114.068 113.120 102.605 1.00 151.35 ? 1129 GLY B N   1 
ATOM   4280 C  CA  . GLY B 1 352 ? 114.514 112.338 103.739 1.00 149.81 ? 1129 GLY B CA  1 
ATOM   4281 C  C   . GLY B 1 352 ? 114.267 113.035 105.060 1.00 150.12 ? 1129 GLY B C   1 
ATOM   4282 O  O   . GLY B 1 352 ? 114.919 114.036 105.372 1.00 150.39 ? 1129 GLY B O   1 
ATOM   4283 N  N   . GLY B 1 353 ? 113.328 112.516 105.845 1.00 174.50 ? 1130 GLY B N   1 
ATOM   4284 C  CA  . GLY B 1 353 ? 112.999 113.119 107.120 1.00 176.33 ? 1130 GLY B CA  1 
ATOM   4285 C  C   . GLY B 1 353 ? 111.689 113.878 107.105 1.00 176.95 ? 1130 GLY B C   1 
ATOM   4286 O  O   . GLY B 1 353 ? 111.589 114.969 107.673 1.00 177.95 ? 1130 GLY B O   1 
ATOM   4287 N  N   . ASP B 1 354 ? 110.673 113.309 106.450 1.00 179.88 ? 1131 ASP B N   1 
ATOM   4288 C  CA  . ASP B 1 354 ? 109.361 113.945 106.411 1.00 180.14 ? 1131 ASP B CA  1 
ATOM   4289 C  C   . ASP B 1 354 ? 108.718 114.025 107.789 1.00 180.19 ? 1131 ASP B C   1 
ATOM   4290 O  O   . ASP B 1 354 ? 107.831 114.861 108.000 1.00 179.68 ? 1131 ASP B O   1 
ATOM   4291 C  CB  . ASP B 1 354 ? 108.442 113.193 105.448 1.00 180.68 ? 1131 ASP B CB  1 
ATOM   4292 C  CG  . ASP B 1 354 ? 108.467 111.693 105.669 1.00 181.47 ? 1131 ASP B CG  1 
ATOM   4293 O  OD1 . ASP B 1 354 ? 109.169 111.239 106.597 1.00 181.35 ? 1131 ASP B OD1 1 
ATOM   4294 O  OD2 . ASP B 1 354 ? 107.785 110.969 104.915 1.00 180.58 ? 1131 ASP B OD2 1 
ATOM   4295 N  N   . CYS B 1 355 ? 109.143 113.175 108.727 1.00 178.65 ? 1132 CYS B N   1 
ATOM   4296 C  CA  . CYS B 1 355 ? 108.598 113.232 110.078 1.00 178.05 ? 1132 CYS B CA  1 
ATOM   4297 C  C   . CYS B 1 355 ? 108.907 114.568 110.739 1.00 177.74 ? 1132 CYS B C   1 
ATOM   4298 O  O   . CYS B 1 355 ? 108.048 115.149 111.411 1.00 179.01 ? 1132 CYS B O   1 
ATOM   4299 C  CB  . CYS B 1 355 ? 109.150 112.078 110.915 1.00 178.04 ? 1132 CYS B CB  1 
ATOM   4300 S  SG  . CYS B 1 355 ? 108.711 112.153 112.667 1.00 182.54 ? 1132 CYS B SG  1 
ATOM   4301 N  N   . GLU B 1 356 ? 110.129 115.074 110.556 1.00 180.24 ? 1133 GLU B N   1 
ATOM   4302 C  CA  . GLU B 1 356 ? 110.483 116.372 111.122 1.00 181.60 ? 1133 GLU B CA  1 
ATOM   4303 C  C   . GLU B 1 356 ? 109.656 117.490 110.500 1.00 181.78 ? 1133 GLU B C   1 
ATOM   4304 O  O   . GLU B 1 356 ? 109.205 118.403 111.202 1.00 183.99 ? 1133 GLU B O   1 
ATOM   4305 C  CB  . GLU B 1 356 ? 111.976 116.638 110.932 1.00 182.82 ? 1133 GLU B CB  1 
ATOM   4306 C  CG  . GLU B 1 356 ? 112.877 115.580 111.545 1.00 183.59 ? 1133 GLU B CG  1 
ATOM   4307 C  CD  . GLU B 1 356 ? 114.347 115.931 111.430 1.00 185.70 ? 1133 GLU B CD  1 
ATOM   4308 O  OE1 . GLU B 1 356 ? 114.661 117.007 110.881 1.00 186.81 ? 1133 GLU B OE1 1 
ATOM   4309 O  OE2 . GLU B 1 356 ? 115.189 115.130 111.890 1.00 185.37 ? 1133 GLU B OE2 1 
ATOM   4310 N  N   . CYS B 1 357 ? 109.448 117.435 109.182 1.00 173.34 ? 1134 CYS B N   1 
ATOM   4311 C  CA  . CYS B 1 357 ? 108.628 118.444 108.519 1.00 172.91 ? 1134 CYS B CA  1 
ATOM   4312 C  C   . CYS B 1 357 ? 107.200 118.427 109.050 1.00 172.17 ? 1134 CYS B C   1 
ATOM   4313 O  O   . CYS B 1 357 ? 106.621 119.483 109.335 1.00 173.17 ? 1134 CYS B O   1 
ATOM   4314 C  CB  . CYS B 1 357 ? 108.646 118.221 107.006 1.00 173.73 ? 1134 CYS B CB  1 
ATOM   4315 S  SG  . CYS B 1 357 ? 110.251 118.529 106.218 1.00 184.04 ? 1134 CYS B SG  1 
ATOM   4316 N  N   . PHE B 1 358 ? 106.621 117.234 109.204 1.00 146.68 ? 1135 PHE B N   1 
ATOM   4317 C  CA  . PHE B 1 358 ? 105.264 117.130 109.731 1.00 146.07 ? 1135 PHE B CA  1 
ATOM   4318 C  C   . PHE B 1 358 ? 105.189 117.626 111.170 1.00 148.58 ? 1135 PHE B C   1 
ATOM   4319 O  O   . PHE B 1 358 ? 104.234 118.318 111.550 1.00 150.44 ? 1135 PHE B O   1 
ATOM   4320 C  CB  . PHE B 1 358 ? 104.780 115.683 109.630 1.00 144.10 ? 1135 PHE B CB  1 
ATOM   4321 C  CG  . PHE B 1 358 ? 103.546 115.396 110.435 1.00 144.29 ? 1135 PHE B CG  1 
ATOM   4322 C  CD1 . PHE B 1 358 ? 102.303 115.810 109.991 1.00 144.66 ? 1135 PHE B CD1 1 
ATOM   4323 C  CD2 . PHE B 1 358 ? 103.628 114.702 111.631 1.00 146.01 ? 1135 PHE B CD2 1 
ATOM   4324 C  CE1 . PHE B 1 358 ? 101.165 115.544 110.726 1.00 146.83 ? 1135 PHE B CE1 1 
ATOM   4325 C  CE2 . PHE B 1 358 ? 102.494 114.434 112.372 1.00 146.45 ? 1135 PHE B CE2 1 
ATOM   4326 C  CZ  . PHE B 1 358 ? 101.261 114.855 111.919 1.00 147.18 ? 1135 PHE B CZ  1 
ATOM   4327 N  N   . CYS B 1 359 ? 106.190 117.285 111.987 1.00 170.65 ? 1136 CYS B N   1 
ATOM   4328 C  CA  . CYS B 1 359 ? 106.201 117.735 113.374 1.00 170.28 ? 1136 CYS B CA  1 
ATOM   4329 C  C   . CYS B 1 359 ? 106.287 119.252 113.459 1.00 169.34 ? 1136 CYS B C   1 
ATOM   4330 O  O   . CYS B 1 359 ? 105.591 119.872 114.269 1.00 170.72 ? 1136 CYS B O   1 
ATOM   4331 C  CB  . CYS B 1 359 ? 107.363 117.088 114.129 1.00 172.19 ? 1136 CYS B CB  1 
ATOM   4332 S  SG  . CYS B 1 359 ? 107.156 115.323 114.475 1.00 182.19 ? 1136 CYS B SG  1 
ATOM   4333 N  N   . THR B 1 360 ? 107.133 119.870 112.631 1.00 155.67 ? 1137 THR B N   1 
ATOM   4334 C  CA  . THR B 1 360 ? 107.223 121.328 112.625 1.00 155.12 ? 1137 THR B CA  1 
ATOM   4335 C  C   . THR B 1 360 ? 105.921 121.961 112.150 1.00 154.17 ? 1137 THR B C   1 
ATOM   4336 O  O   . THR B 1 360 ? 105.476 122.974 112.706 1.00 155.20 ? 1137 THR B O   1 
ATOM   4337 C  CB  . THR B 1 360 ? 108.389 121.785 111.749 1.00 155.27 ? 1137 THR B CB  1 
ATOM   4338 O  OG1 . THR B 1 360 ? 108.262 121.213 110.442 1.00 157.55 ? 1137 THR B OG1 1 
ATOM   4339 C  CG2 . THR B 1 360 ? 109.716 121.364 112.363 1.00 156.18 ? 1137 THR B CG2 1 
ATOM   4340 N  N   . ALA B 1 361 ? 105.294 121.376 111.125 1.00 144.55 ? 1138 ALA B N   1 
ATOM   4341 C  CA  . ALA B 1 361 ? 104.031 121.915 110.630 1.00 143.85 ? 1138 ALA B CA  1 
ATOM   4342 C  C   . ALA B 1 361 ? 102.952 121.865 111.704 1.00 144.67 ? 1138 ALA B C   1 
ATOM   4343 O  O   . ALA B 1 361 ? 102.164 122.808 111.846 1.00 144.95 ? 1138 ALA B O   1 
ATOM   4344 C  CB  . ALA B 1 361 ? 103.587 121.150 109.384 1.00 146.42 ? 1138 ALA B CB  1 
ATOM   4345 N  N   . VAL B 1 362 ? 102.898 120.773 112.469 1.00 140.26 ? 1139 VAL B N   1 
ATOM   4346 C  CA  . VAL B 1 362 ? 101.907 120.676 113.538 1.00 138.17 ? 1139 VAL B CA  1 
ATOM   4347 C  C   . VAL B 1 362 ? 102.251 121.628 114.679 1.00 139.49 ? 1139 VAL B C   1 
ATOM   4348 O  O   . VAL B 1 362 ? 101.367 122.281 115.250 1.00 139.92 ? 1139 VAL B O   1 
ATOM   4349 C  CB  . VAL B 1 362 ? 101.789 119.221 114.025 1.00 138.56 ? 1139 VAL B CB  1 
ATOM   4350 C  CG1 . VAL B 1 362 ? 100.891 119.142 115.248 1.00 140.09 ? 1139 VAL B CG1 1 
ATOM   4351 C  CG2 . VAL B 1 362 ? 101.252 118.338 112.914 1.00 137.00 ? 1139 VAL B CG2 1 
ATOM   4352 N  N   . ALA B 1 363 ? 103.537 121.727 115.027 1.00 138.78 ? 1140 ALA B N   1 
ATOM   4353 C  CA  . ALA B 1 363 ? 103.947 122.582 116.134 1.00 136.51 ? 1140 ALA B CA  1 
ATOM   4354 C  C   . ALA B 1 363 ? 103.707 124.053 115.831 1.00 138.09 ? 1140 ALA B C   1 
ATOM   4355 O  O   . ALA B 1 363 ? 103.500 124.845 116.755 1.00 140.60 ? 1140 ALA B O   1 
ATOM   4356 C  CB  . ALA B 1 363 ? 105.419 122.343 116.466 1.00 138.42 ? 1140 ALA B CB  1 
ATOM   4357 N  N   . ALA B 1 364 ? 103.731 124.439 114.554 1.00 144.00 ? 1141 ALA B N   1 
ATOM   4358 C  CA  . ALA B 1 364 ? 103.397 125.815 114.200 1.00 144.35 ? 1141 ALA B CA  1 
ATOM   4359 C  C   . ALA B 1 364 ? 101.984 126.167 114.652 1.00 144.14 ? 1141 ALA B C   1 
ATOM   4360 O  O   . ALA B 1 364 ? 101.771 127.164 115.353 1.00 146.85 ? 1141 ALA B O   1 
ATOM   4361 C  CB  . ALA B 1 364 ? 103.553 126.022 112.694 1.00 146.56 ? 1141 ALA B CB  1 
ATOM   4362 N  N   . TYR B 1 365 ? 101.004 125.342 114.274 1.00 146.71 ? 1142 TYR B N   1 
ATOM   4363 C  CA  . TYR B 1 365 ? 99.631  125.580 114.703 1.00 148.50 ? 1142 TYR B CA  1 
ATOM   4364 C  C   . TYR B 1 365 ? 99.475  125.406 116.207 1.00 148.10 ? 1142 TYR B C   1 
ATOM   4365 O  O   . TYR B 1 365 ? 98.663  126.102 116.829 1.00 148.38 ? 1142 TYR B O   1 
ATOM   4366 C  CB  . TYR B 1 365 ? 98.677  124.645 113.960 1.00 151.35 ? 1142 TYR B CB  1 
ATOM   4367 C  CG  . TYR B 1 365 ? 97.218  124.868 114.289 1.00 151.40 ? 1142 TYR B CG  1 
ATOM   4368 C  CD1 . TYR B 1 365 ? 96.505  125.902 113.699 1.00 152.09 ? 1142 TYR B CD1 1 
ATOM   4369 C  CD2 . TYR B 1 365 ? 96.553  124.042 115.184 1.00 149.72 ? 1142 TYR B CD2 1 
ATOM   4370 C  CE1 . TYR B 1 365 ? 95.173  126.110 113.992 1.00 150.62 ? 1142 TYR B CE1 1 
ATOM   4371 C  CE2 . TYR B 1 365 ? 95.219  124.243 115.485 1.00 149.72 ? 1142 TYR B CE2 1 
ATOM   4372 C  CZ  . TYR B 1 365 ? 94.535  125.279 114.885 1.00 149.96 ? 1142 TYR B CZ  1 
ATOM   4373 O  OH  . TYR B 1 365 ? 93.207  125.485 115.178 1.00 152.75 ? 1142 TYR B OH  1 
ATOM   4374 N  N   . ALA B 1 366 ? 100.239 124.490 116.807 1.00 153.73 ? 1143 ALA B N   1 
ATOM   4375 C  CA  . ALA B 1 366 ? 100.183 124.320 118.256 1.00 155.55 ? 1143 ALA B CA  1 
ATOM   4376 C  C   . ALA B 1 366 ? 100.598 125.600 118.972 1.00 155.31 ? 1143 ALA B C   1 
ATOM   4377 O  O   . ALA B 1 366 ? 99.921  126.055 119.901 1.00 157.15 ? 1143 ALA B O   1 
ATOM   4378 C  CB  . ALA B 1 366 ? 101.070 123.150 118.681 1.00 157.13 ? 1143 ALA B CB  1 
ATOM   4379 N  N   . GLN B 1 367 ? 101.707 126.204 118.540 1.00 162.06 ? 1144 GLN B N   1 
ATOM   4380 C  CA  . GLN B 1 367 ? 102.158 127.454 119.142 1.00 161.49 ? 1144 GLN B CA  1 
ATOM   4381 C  C   . GLN B 1 367 ? 101.193 128.591 118.834 1.00 161.88 ? 1144 GLN B C   1 
ATOM   4382 O  O   . GLN B 1 367 ? 100.970 129.469 119.677 1.00 163.96 ? 1144 GLN B O   1 
ATOM   4383 C  CB  . GLN B 1 367 ? 103.567 127.791 118.653 1.00 161.74 ? 1144 GLN B CB  1 
ATOM   4384 C  CG  . GLN B 1 367 ? 104.370 128.669 119.602 1.00 162.46 ? 1144 GLN B CG  1 
ATOM   4385 C  CD  . GLN B 1 367 ? 103.969 130.129 119.534 1.00 165.01 ? 1144 GLN B CD  1 
ATOM   4386 O  OE1 . GLN B 1 367 ? 103.504 130.610 118.501 1.00 165.29 ? 1144 GLN B OE1 1 
ATOM   4387 N  NE2 . GLN B 1 367 ? 104.148 130.844 120.639 1.00 166.53 ? 1144 GLN B NE2 1 
ATOM   4388 N  N   . ALA B 1 368 ? 100.611 128.595 117.631 1.00 154.64 ? 1145 ALA B N   1 
ATOM   4389 C  CA  . ALA B 1 368 ? 99.633  129.623 117.291 1.00 154.82 ? 1145 ALA B CA  1 
ATOM   4390 C  C   . ALA B 1 368 ? 98.425  129.560 118.217 1.00 156.12 ? 1145 ALA B C   1 
ATOM   4391 O  O   . ALA B 1 368 ? 97.914  130.597 118.656 1.00 156.58 ? 1145 ALA B O   1 
ATOM   4392 C  CB  . ALA B 1 368 ? 99.202  129.477 115.833 1.00 156.42 ? 1145 ALA B CB  1 
ATOM   4393 N  N   . CYS B 1 369 ? 97.952  128.350 118.524 1.00 174.77 ? 1146 CYS B N   1 
ATOM   4394 C  CA  . CYS B 1 369 ? 96.835  128.211 119.453 1.00 175.50 ? 1146 CYS B CA  1 
ATOM   4395 C  C   . CYS B 1 369 ? 97.259  128.529 120.882 1.00 175.64 ? 1146 CYS B C   1 
ATOM   4396 O  O   . CYS B 1 369 ? 96.474  129.084 121.659 1.00 176.08 ? 1146 CYS B O   1 
ATOM   4397 C  CB  . CYS B 1 369 ? 96.248  126.803 119.369 1.00 176.25 ? 1146 CYS B CB  1 
ATOM   4398 S  SG  . CYS B 1 369 ? 94.719  126.592 120.311 1.00 182.26 ? 1146 CYS B SG  1 
ATOM   4399 N  N   . HIS B 1 370 ? 98.497  128.182 121.247 1.00 172.70 ? 1147 HIS B N   1 
ATOM   4400 C  CA  . HIS B 1 370 ? 98.986  128.478 122.590 1.00 171.42 ? 1147 HIS B CA  1 
ATOM   4401 C  C   . HIS B 1 370 ? 99.115  129.977 122.824 1.00 172.67 ? 1147 HIS B C   1 
ATOM   4402 O  O   . HIS B 1 370 ? 98.966  130.440 123.960 1.00 171.64 ? 1147 HIS B O   1 
ATOM   4403 C  CB  . HIS B 1 370 ? 100.332 127.793 122.821 1.00 172.82 ? 1147 HIS B CB  1 
ATOM   4404 C  CG  . HIS B 1 370 ? 100.219 126.396 123.346 1.00 173.60 ? 1147 HIS B CG  1 
ATOM   4405 N  ND1 . HIS B 1 370 ? 99.813  125.337 122.563 1.00 174.50 ? 1147 HIS B ND1 1 
ATOM   4406 C  CD2 . HIS B 1 370 ? 100.464 125.882 124.575 1.00 173.14 ? 1147 HIS B CD2 1 
ATOM   4407 C  CE1 . HIS B 1 370 ? 99.809  124.232 123.287 1.00 173.90 ? 1147 HIS B CE1 1 
ATOM   4408 N  NE2 . HIS B 1 370 ? 100.201 124.536 124.512 1.00 174.14 ? 1147 HIS B NE2 1 
ATOM   4409 N  N   . GLU B 1 371 ? 99.398  130.745 121.769 1.00 197.82 ? 1148 GLU B N   1 
ATOM   4410 C  CA  . GLU B 1 371 ? 99.531  132.190 121.917 1.00 198.58 ? 1148 GLU B CA  1 
ATOM   4411 C  C   . GLU B 1 371 ? 98.216  132.837 122.335 1.00 198.47 ? 1148 GLU B C   1 
ATOM   4412 O  O   . GLU B 1 371 ? 98.223  133.897 122.972 1.00 198.62 ? 1148 GLU B O   1 
ATOM   4413 C  CB  . GLU B 1 371 ? 100.043 132.800 120.609 1.00 198.54 ? 1148 GLU B CB  1 
ATOM   4414 C  CG  . GLU B 1 371 ? 100.257 134.306 120.642 1.00 199.44 ? 1148 GLU B CG  1 
ATOM   4415 C  CD  . GLU B 1 371 ? 99.049  135.080 120.150 1.00 200.90 ? 1148 GLU B CD  1 
ATOM   4416 O  OE1 . GLU B 1 371 ? 98.213  134.487 119.436 1.00 200.98 ? 1148 GLU B OE1 1 
ATOM   4417 O  OE2 . GLU B 1 371 ? 98.935  136.280 120.477 1.00 201.48 ? 1148 GLU B OE2 1 
ATOM   4418 N  N   . VAL B 1 372 ? 97.084  132.215 121.998 1.00 180.88 ? 1149 VAL B N   1 
ATOM   4419 C  CA  . VAL B 1 372 ? 95.785  132.780 122.355 1.00 179.72 ? 1149 VAL B CA  1 
ATOM   4420 C  C   . VAL B 1 372 ? 95.616  132.822 123.868 1.00 180.13 ? 1149 VAL B C   1 
ATOM   4421 O  O   . VAL B 1 372 ? 95.104  133.801 124.424 1.00 179.22 ? 1149 VAL B O   1 
ATOM   4422 C  CB  . VAL B 1 372 ? 94.653  131.984 121.680 1.00 179.37 ? 1149 VAL B CB  1 
ATOM   4423 C  CG1 . VAL B 1 372 ? 93.310  132.649 121.938 1.00 178.34 ? 1149 VAL B CG1 1 
ATOM   4424 C  CG2 . VAL B 1 372 ? 94.914  131.854 120.188 1.00 179.93 ? 1149 VAL B CG2 1 
ATOM   4425 N  N   . GLY B 1 373 ? 96.041  131.766 124.558 1.00 187.48 ? 1150 GLY B N   1 
ATOM   4426 C  CA  . GLY B 1 373 ? 95.934  131.723 126.003 1.00 187.66 ? 1150 GLY B CA  1 
ATOM   4427 C  C   . GLY B 1 373 ? 95.582  130.355 126.547 1.00 188.76 ? 1150 GLY B C   1 
ATOM   4428 O  O   . GLY B 1 373 ? 95.854  130.056 127.713 1.00 190.22 ? 1150 GLY B O   1 
ATOM   4429 N  N   . LEU B 1 374 ? 94.976  129.514 125.714 1.00 172.83 ? 1151 LEU B N   1 
ATOM   4430 C  CA  . LEU B 1 374 ? 94.602  128.162 126.104 1.00 171.78 ? 1151 LEU B CA  1 
ATOM   4431 C  C   . LEU B 1 374 ? 95.593  127.161 125.526 1.00 171.55 ? 1151 LEU B C   1 
ATOM   4432 O  O   . LEU B 1 374 ? 96.070  127.323 124.399 1.00 171.86 ? 1151 LEU B O   1 
ATOM   4433 C  CB  . LEU B 1 374 ? 93.180  127.834 125.640 1.00 170.43 ? 1151 LEU B CB  1 
ATOM   4434 C  CG  . LEU B 1 374 ? 92.878  127.930 124.143 1.00 170.13 ? 1151 LEU B CG  1 
ATOM   4435 C  CD1 . LEU B 1 374 ? 92.913  126.557 123.489 1.00 170.70 ? 1151 LEU B CD1 1 
ATOM   4436 C  CD2 . LEU B 1 374 ? 91.535  128.604 123.911 1.00 170.30 ? 1151 LEU B CD2 1 
ATOM   4437 N  N   . CYS B 1 375 ? 95.903  126.131 126.306 1.00 179.64 ? 1152 CYS B N   1 
ATOM   4438 C  CA  . CYS B 1 375 ? 96.864  125.109 125.919 1.00 181.33 ? 1152 CYS B CA  1 
ATOM   4439 C  C   . CYS B 1 375 ? 96.160  123.771 125.739 1.00 180.15 ? 1152 CYS B C   1 
ATOM   4440 O  O   . CYS B 1 375 ? 95.234  123.439 126.485 1.00 179.58 ? 1152 CYS B O   1 
ATOM   4441 C  CB  . CYS B 1 375 ? 97.976  124.978 126.964 1.00 183.40 ? 1152 CYS B CB  1 
ATOM   4442 S  SG  . CYS B 1 375 ? 97.412  124.476 128.605 1.00 188.76 ? 1152 CYS B SG  1 
ATOM   4443 N  N   . VAL B 1 376 ? 96.603  123.009 124.742 1.00 161.60 ? 1153 VAL B N   1 
ATOM   4444 C  CA  . VAL B 1 376 ? 96.043  121.700 124.433 1.00 161.21 ? 1153 VAL B CA  1 
ATOM   4445 C  C   . VAL B 1 376 ? 97.191  120.722 124.227 1.00 161.41 ? 1153 VAL B C   1 
ATOM   4446 O  O   . VAL B 1 376 ? 98.174  121.045 123.549 1.00 161.70 ? 1153 VAL B O   1 
ATOM   4447 C  CB  . VAL B 1 376 ? 95.128  121.747 123.192 1.00 161.97 ? 1153 VAL B CB  1 
ATOM   4448 C  CG1 . VAL B 1 376 ? 95.827  122.445 122.033 1.00 160.68 ? 1153 VAL B CG1 1 
ATOM   4449 C  CG2 . VAL B 1 376 ? 94.688  120.347 122.795 1.00 161.77 ? 1153 VAL B CG2 1 
ATOM   4450 N  N   . SER B 1 377 ? 97.076  119.538 124.821 1.00 156.62 ? 1154 SER B N   1 
ATOM   4451 C  CA  . SER B 1 377 ? 98.088  118.499 124.688 1.00 156.55 ? 1154 SER B CA  1 
ATOM   4452 C  C   . SER B 1 377 ? 97.797  117.673 123.441 1.00 157.72 ? 1154 SER B C   1 
ATOM   4453 O  O   . SER B 1 377 ? 96.725  117.070 123.326 1.00 158.84 ? 1154 SER B O   1 
ATOM   4454 C  CB  . SER B 1 377 ? 98.118  117.609 125.929 1.00 156.20 ? 1154 SER B CB  1 
ATOM   4455 O  OG  . SER B 1 377 ? 99.005  116.519 125.753 1.00 155.63 ? 1154 SER B OG  1 
ATOM   4456 N  N   . TRP B 1 378 ? 98.751  117.647 122.510 1.00 137.10 ? 1155 TRP B N   1 
ATOM   4457 C  CA  . TRP B 1 378 ? 98.592  116.925 121.258 1.00 133.16 ? 1155 TRP B CA  1 
ATOM   4458 C  C   . TRP B 1 378 ? 99.653  115.863 121.020 1.00 132.79 ? 1155 TRP B C   1 
ATOM   4459 O  O   . TRP B 1 378 ? 99.496  115.059 120.094 1.00 134.05 ? 1155 TRP B O   1 
ATOM   4460 C  CB  . TRP B 1 378 ? 98.603  117.902 120.071 1.00 131.81 ? 1155 TRP B CB  1 
ATOM   4461 C  CG  . TRP B 1 378 ? 99.903  118.626 119.915 1.00 132.35 ? 1155 TRP B CG  1 
ATOM   4462 C  CD1 . TRP B 1 378 ? 100.267 119.795 120.516 1.00 134.71 ? 1155 TRP B CD1 1 
ATOM   4463 C  CD2 . TRP B 1 378 ? 101.020 118.224 119.113 1.00 132.61 ? 1155 TRP B CD2 1 
ATOM   4464 N  NE1 . TRP B 1 378 ? 101.538 120.149 120.134 1.00 135.38 ? 1155 TRP B NE1 1 
ATOM   4465 C  CE2 . TRP B 1 378 ? 102.022 119.200 119.273 1.00 133.07 ? 1155 TRP B CE2 1 
ATOM   4466 C  CE3 . TRP B 1 378 ? 101.268 117.134 118.274 1.00 135.17 ? 1155 TRP B CE3 1 
ATOM   4467 C  CZ2 . TRP B 1 378 ? 103.252 119.119 118.625 1.00 132.83 ? 1155 TRP B CZ2 1 
ATOM   4468 C  CZ3 . TRP B 1 378 ? 102.490 117.055 117.632 1.00 134.81 ? 1155 TRP B CZ3 1 
ATOM   4469 C  CH2 . TRP B 1 378 ? 103.466 118.042 117.811 1.00 133.83 ? 1155 TRP B CH2 1 
ATOM   4470 N  N   . ARG B 1 379 ? 100.720 115.833 121.813 1.00 133.03 ? 1156 ARG B N   1 
ATOM   4471 C  CA  . ARG B 1 379 ? 101.793 114.879 121.581 1.00 133.79 ? 1156 ARG B CA  1 
ATOM   4472 C  C   . ARG B 1 379 ? 101.346 113.463 121.927 1.00 136.51 ? 1156 ARG B C   1 
ATOM   4473 O  O   . ARG B 1 379 ? 100.442 113.249 122.739 1.00 138.80 ? 1156 ARG B O   1 
ATOM   4474 C  CB  . ARG B 1 379 ? 103.030 115.257 122.395 1.00 133.21 ? 1156 ARG B CB  1 
ATOM   4475 C  CG  . ARG B 1 379 ? 103.625 116.599 122.002 1.00 132.38 ? 1156 ARG B CG  1 
ATOM   4476 C  CD  . ARG B 1 379 ? 105.111 116.660 122.304 1.00 135.04 ? 1156 ARG B CD  1 
ATOM   4477 N  NE  . ARG B 1 379 ? 105.738 117.830 121.701 1.00 133.90 ? 1156 ARG B NE  1 
ATOM   4478 C  CZ  . ARG B 1 379 ? 106.313 117.840 120.507 1.00 131.56 ? 1156 ARG B CZ  1 
ATOM   4479 N  NH1 . ARG B 1 379 ? 106.364 116.753 119.755 1.00 132.49 ? 1156 ARG B NH1 1 
ATOM   4480 N  NH2 . ARG B 1 379 ? 106.852 118.969 120.055 1.00 130.18 ? 1156 ARG B NH2 1 
ATOM   4481 N  N   . THR B 1 380 ? 101.998 112.488 121.292 1.00 151.80 ? 1157 THR B N   1 
ATOM   4482 C  CA  . THR B 1 380 ? 101.648 111.085 121.399 1.00 151.06 ? 1157 THR B CA  1 
ATOM   4483 C  C   . THR B 1 380 ? 102.927 110.287 121.198 1.00 152.59 ? 1157 THR B C   1 
ATOM   4484 O  O   . THR B 1 380 ? 103.743 110.655 120.341 1.00 156.60 ? 1157 THR B O   1 
ATOM   4485 C  CB  . THR B 1 380 ? 100.594 110.692 120.353 1.00 150.89 ? 1157 THR B CB  1 
ATOM   4486 O  OG1 . THR B 1 380 ? 99.317  111.216 120.740 1.00 154.28 ? 1157 THR B OG1 1 
ATOM   4487 C  CG2 . THR B 1 380 ? 100.487 109.180 120.202 1.00 149.43 ? 1157 THR B CG2 1 
ATOM   4488 N  N   . PRO B 1 381 ? 103.144 109.216 121.970 1.00 139.64 ? 1158 PRO B N   1 
ATOM   4489 C  CA  . PRO B 1 381 ? 104.362 108.408 121.779 1.00 139.68 ? 1158 PRO B CA  1 
ATOM   4490 C  C   . PRO B 1 381 ? 104.547 107.896 120.360 1.00 139.70 ? 1158 PRO B C   1 
ATOM   4491 O  O   . PRO B 1 381 ? 105.662 107.495 120.006 1.00 139.37 ? 1158 PRO B O   1 
ATOM   4492 C  CB  . PRO B 1 381 ? 104.180 107.250 122.773 1.00 137.34 ? 1158 PRO B CB  1 
ATOM   4493 C  CG  . PRO B 1 381 ? 102.750 107.330 123.240 1.00 137.63 ? 1158 PRO B CG  1 
ATOM   4494 C  CD  . PRO B 1 381 ? 102.365 108.766 123.133 1.00 137.39 ? 1158 PRO B CD  1 
ATOM   4495 N  N   . SER B 1 382 ? 103.498 107.894 119.540 1.00 147.03 ? 1159 SER B N   1 
ATOM   4496 C  CA  . SER B 1 382 ? 103.611 107.532 118.135 1.00 147.17 ? 1159 SER B CA  1 
ATOM   4497 C  C   . SER B 1 382 ? 103.547 108.733 117.201 1.00 146.30 ? 1159 SER B C   1 
ATOM   4498 O  O   . SER B 1 382 ? 103.775 108.572 115.997 1.00 147.44 ? 1159 SER B O   1 
ATOM   4499 C  CB  . SER B 1 382 ? 102.508 106.536 117.755 1.00 148.62 ? 1159 SER B CB  1 
ATOM   4500 O  OG  . SER B 1 382 ? 102.754 105.262 118.323 1.00 151.52 ? 1159 SER B OG  1 
ATOM   4501 N  N   . ILE B 1 383 ? 103.251 109.924 117.717 1.00 140.35 ? 1160 ILE B N   1 
ATOM   4502 C  CA  . ILE B 1 383 ? 103.116 111.135 116.911 1.00 140.29 ? 1160 ILE B CA  1 
ATOM   4503 C  C   . ILE B 1 383 ? 104.025 112.193 117.526 1.00 141.14 ? 1160 ILE B C   1 
ATOM   4504 O  O   . ILE B 1 383 ? 103.670 112.816 118.533 1.00 142.71 ? 1160 ILE B O   1 
ATOM   4505 C  CB  . ILE B 1 383 ? 101.668 111.631 116.836 1.00 138.63 ? 1160 ILE B CB  1 
ATOM   4506 C  CG1 . ILE B 1 383 ? 100.765 110.561 116.219 1.00 140.22 ? 1160 ILE B CG1 1 
ATOM   4507 C  CG2 . ILE B 1 383 ? 101.587 112.920 116.033 1.00 139.29 ? 1160 ILE B CG2 1 
ATOM   4508 C  CD1 . ILE B 1 383 ? 101.174 110.147 114.824 1.00 139.77 ? 1160 ILE B CD1 1 
ATOM   4509 N  N   . CYS B 1 384 ? 105.194 112.409 116.915 1.00 153.61 ? 1161 CYS B N   1 
ATOM   4510 C  CA  . CYS B 1 384 ? 106.171 113.407 117.337 1.00 153.79 ? 1161 CYS B CA  1 
ATOM   4511 C  C   . CYS B 1 384 ? 106.520 113.258 118.815 1.00 153.86 ? 1161 CYS B C   1 
ATOM   4512 O  O   . CYS B 1 384 ? 106.127 114.101 119.631 1.00 155.32 ? 1161 CYS B O   1 
ATOM   4513 C  CB  . CYS B 1 384 ? 105.648 114.819 117.063 1.00 155.89 ? 1161 CYS B CB  1 
ATOM   4514 S  SG  . CYS B 1 384 ? 105.315 115.181 115.321 1.00 161.81 ? 1161 CYS B SG  1 
ATOM   4515 N  N   . PRO B 1 385 ? 107.247 112.213 119.199 1.00 136.89 ? 1162 PRO B N   1 
ATOM   4516 C  CA  . PRO B 1 385 ? 107.584 112.015 120.610 1.00 137.20 ? 1162 PRO B CA  1 
ATOM   4517 C  C   . PRO B 1 385 ? 108.833 112.782 121.025 1.00 138.41 ? 1162 PRO B C   1 
ATOM   4518 O  O   . PRO B 1 385 ? 109.674 113.159 120.208 1.00 140.32 ? 1162 PRO B O   1 
ATOM   4519 C  CB  . PRO B 1 385 ? 107.824 110.502 120.690 1.00 136.09 ? 1162 PRO B CB  1 
ATOM   4520 C  CG  . PRO B 1 385 ? 108.396 110.169 119.352 1.00 136.79 ? 1162 PRO B CG  1 
ATOM   4521 C  CD  . PRO B 1 385 ? 107.771 111.124 118.354 1.00 137.51 ? 1162 PRO B CD  1 
ATOM   4522 N  N   . LEU B 1 386 ? 108.934 113.007 122.334 1.00 142.72 ? 1163 LEU B N   1 
ATOM   4523 C  CA  . LEU B 1 386 ? 110.090 113.652 122.940 1.00 140.68 ? 1163 LEU B CA  1 
ATOM   4524 C  C   . LEU B 1 386 ? 110.643 112.758 124.039 1.00 145.09 ? 1163 LEU B C   1 
ATOM   4525 O  O   . LEU B 1 386 ? 109.883 112.123 124.776 1.00 148.16 ? 1163 LEU B O   1 
ATOM   4526 C  CB  . LEU B 1 386 ? 109.733 115.026 123.518 1.00 139.58 ? 1163 LEU B CB  1 
ATOM   4527 C  CG  . LEU B 1 386 ? 108.952 115.980 122.614 1.00 143.95 ? 1163 LEU B CG  1 
ATOM   4528 C  CD1 . LEU B 1 386 ? 108.602 117.252 123.368 1.00 143.35 ? 1163 LEU B CD1 1 
ATOM   4529 C  CD2 . LEU B 1 386 ? 109.746 116.298 121.358 1.00 145.34 ? 1163 LEU B CD2 1 
ATOM   4530 N  N   . PHE B 1 387 ? 111.971 112.714 124.146 1.00 159.72 ? 1164 PHE B N   1 
ATOM   4531 C  CA  . PHE B 1 387 ? 112.648 111.871 125.130 1.00 159.58 ? 1164 PHE B CA  1 
ATOM   4532 C  C   . PHE B 1 387 ? 113.016 112.733 126.334 1.00 159.71 ? 1164 PHE B C   1 
ATOM   4533 O  O   . PHE B 1 387 ? 114.163 113.139 126.521 1.00 163.91 ? 1164 PHE B O   1 
ATOM   4534 C  CB  . PHE B 1 387 ? 113.872 111.204 124.511 1.00 159.96 ? 1164 PHE B CB  1 
ATOM   4535 C  CG  . PHE B 1 387 ? 114.186 109.855 125.088 1.00 159.64 ? 1164 PHE B CG  1 
ATOM   4536 C  CD1 . PHE B 1 387 ? 114.749 109.739 126.346 1.00 161.44 ? 1164 PHE B CD1 1 
ATOM   4537 C  CD2 . PHE B 1 387 ? 113.922 108.703 124.369 1.00 159.06 ? 1164 PHE B CD2 1 
ATOM   4538 C  CE1 . PHE B 1 387 ? 115.040 108.498 126.879 1.00 162.73 ? 1164 PHE B CE1 1 
ATOM   4539 C  CE2 . PHE B 1 387 ? 114.210 107.459 124.896 1.00 161.64 ? 1164 PHE B CE2 1 
ATOM   4540 C  CZ  . PHE B 1 387 ? 114.770 107.356 126.152 1.00 162.61 ? 1164 PHE B CZ  1 
ATOM   4541 N  N   . CYS B 1 388 ? 112.011 113.013 127.167 1.00 167.11 ? 1165 CYS B N   1 
ATOM   4542 C  CA  . CYS B 1 388 ? 112.237 113.817 128.362 1.00 169.21 ? 1165 CYS B CA  1 
ATOM   4543 C  C   . CYS B 1 388 ? 113.063 113.083 129.410 1.00 168.87 ? 1165 CYS B C   1 
ATOM   4544 O  O   . CYS B 1 388 ? 113.657 113.732 130.278 1.00 169.53 ? 1165 CYS B O   1 
ATOM   4545 C  CB  . CYS B 1 388 ? 110.902 114.251 128.970 1.00 169.71 ? 1165 CYS B CB  1 
ATOM   4546 S  SG  . CYS B 1 388 ? 110.098 115.645 128.140 1.00 178.76 ? 1165 CYS B SG  1 
ATOM   4547 N  N   . ASP B 1 389 ? 113.114 111.752 129.353 1.00 167.42 ? 1166 ASP B N   1 
ATOM   4548 C  CA  . ASP B 1 389 ? 113.858 110.971 130.333 1.00 168.66 ? 1166 ASP B CA  1 
ATOM   4549 C  C   . ASP B 1 389 ? 115.361 110.980 130.083 1.00 168.77 ? 1166 ASP B C   1 
ATOM   4550 O  O   . ASP B 1 389 ? 116.121 110.565 130.964 1.00 168.83 ? 1166 ASP B O   1 
ATOM   4551 C  CB  . ASP B 1 389 ? 113.346 109.528 130.344 1.00 170.57 ? 1166 ASP B CB  1 
ATOM   4552 C  CG  . ASP B 1 389 ? 113.803 108.753 131.565 1.00 172.06 ? 1166 ASP B CG  1 
ATOM   4553 O  OD1 . ASP B 1 389 ? 114.173 109.391 132.573 1.00 171.70 ? 1166 ASP B OD1 1 
ATOM   4554 O  OD2 . ASP B 1 389 ? 113.793 107.506 131.516 1.00 171.57 ? 1166 ASP B OD2 1 
ATOM   4555 N  N   . TYR B 1 390 ? 115.807 111.442 128.912 1.00 160.48 ? 1167 TYR B N   1 
ATOM   4556 C  CA  . TYR B 1 390 ? 117.235 111.446 128.612 1.00 159.67 ? 1167 TYR B CA  1 
ATOM   4557 C  C   . TYR B 1 390 ? 117.994 112.382 129.543 1.00 158.67 ? 1167 TYR B C   1 
ATOM   4558 O  O   . TYR B 1 390 ? 119.109 112.068 129.978 1.00 158.35 ? 1167 TYR B O   1 
ATOM   4559 C  CB  . TYR B 1 390 ? 117.462 111.839 127.153 1.00 160.23 ? 1167 TYR B CB  1 
ATOM   4560 C  CG  . TYR B 1 390 ? 118.867 111.586 126.658 1.00 159.31 ? 1167 TYR B CG  1 
ATOM   4561 C  CD1 . TYR B 1 390 ? 119.264 110.317 126.257 1.00 159.01 ? 1167 TYR B CD1 1 
ATOM   4562 C  CD2 . TYR B 1 390 ? 119.795 112.616 126.587 1.00 160.73 ? 1167 TYR B CD2 1 
ATOM   4563 C  CE1 . TYR B 1 390 ? 120.547 110.081 125.803 1.00 160.59 ? 1167 TYR B CE1 1 
ATOM   4564 C  CE2 . TYR B 1 390 ? 121.080 112.389 126.134 1.00 161.54 ? 1167 TYR B CE2 1 
ATOM   4565 C  CZ  . TYR B 1 390 ? 121.451 111.120 125.743 1.00 162.00 ? 1167 TYR B CZ  1 
ATOM   4566 O  OH  . TYR B 1 390 ? 122.729 110.889 125.291 1.00 163.14 ? 1167 TYR B OH  1 
ATOM   4567 N  N   . TYR B 1 391 ? 117.408 113.537 129.861 1.00 165.28 ? 1168 TYR B N   1 
ATOM   4568 C  CA  . TYR B 1 391 ? 118.079 114.500 130.725 1.00 167.72 ? 1168 TYR B CA  1 
ATOM   4569 C  C   . TYR B 1 391 ? 118.068 114.077 132.188 1.00 169.80 ? 1168 TYR B C   1 
ATOM   4570 O  O   . TYR B 1 391 ? 118.826 114.638 132.986 1.00 170.00 ? 1168 TYR B O   1 
ATOM   4571 C  CB  . TYR B 1 391 ? 117.430 115.876 130.578 1.00 167.79 ? 1168 TYR B CB  1 
ATOM   4572 C  CG  . TYR B 1 391 ? 117.175 116.279 129.143 1.00 166.72 ? 1168 TYR B CG  1 
ATOM   4573 C  CD1 . TYR B 1 391 ? 118.200 116.271 128.207 1.00 166.55 ? 1168 TYR B CD1 1 
ATOM   4574 C  CD2 . TYR B 1 391 ? 115.909 116.667 128.726 1.00 167.53 ? 1168 TYR B CD2 1 
ATOM   4575 C  CE1 . TYR B 1 391 ? 117.971 116.637 126.895 1.00 167.74 ? 1168 TYR B CE1 1 
ATOM   4576 C  CE2 . TYR B 1 391 ? 115.671 117.035 127.416 1.00 167.95 ? 1168 TYR B CE2 1 
ATOM   4577 C  CZ  . TYR B 1 391 ? 116.705 117.019 126.505 1.00 168.03 ? 1168 TYR B CZ  1 
ATOM   4578 O  OH  . TYR B 1 391 ? 116.473 117.385 125.199 1.00 169.31 ? 1168 TYR B OH  1 
ATOM   4579 N  N   . ASN B 1 392 ? 117.235 113.113 132.555 1.00 178.13 ? 1169 ASN B N   1 
ATOM   4580 C  CA  . ASN B 1 392 ? 117.179 112.666 133.942 1.00 177.60 ? 1169 ASN B CA  1 
ATOM   4581 C  C   . ASN B 1 392 ? 118.445 111.893 134.293 1.00 177.19 ? 1169 ASN B C   1 
ATOM   4582 O  O   . ASN B 1 392 ? 118.814 110.957 133.574 1.00 177.72 ? 1169 ASN B O   1 
ATOM   4583 C  CB  . ASN B 1 392 ? 115.948 111.793 134.173 1.00 175.97 ? 1169 ASN B CB  1 
ATOM   4584 C  CG  . ASN B 1 392 ? 114.794 112.563 134.787 1.00 176.10 ? 1169 ASN B CG  1 
ATOM   4585 O  OD1 . ASN B 1 392 ? 114.989 113.609 135.405 1.00 176.42 ? 1169 ASN B OD1 1 
ATOM   4586 N  ND2 . ASN B 1 392 ? 113.583 112.046 134.619 1.00 176.03 ? 1169 ASN B ND2 1 
ATOM   4587 N  N   . PRO B 1 393 ? 119.133 112.246 135.375 1.00 175.13 ? 1170 PRO B N   1 
ATOM   4588 C  CA  . PRO B 1 393 ? 120.321 111.486 135.778 1.00 175.49 ? 1170 PRO B CA  1 
ATOM   4589 C  C   . PRO B 1 393 ? 119.935 110.131 136.353 1.00 178.03 ? 1170 PRO B C   1 
ATOM   4590 O  O   . PRO B 1 393 ? 118.765 109.830 136.598 1.00 179.32 ? 1170 PRO B O   1 
ATOM   4591 C  CB  . PRO B 1 393 ? 120.975 112.379 136.835 1.00 174.70 ? 1170 PRO B CB  1 
ATOM   4592 C  CG  . PRO B 1 393 ? 119.846 113.174 137.396 1.00 174.86 ? 1170 PRO B CG  1 
ATOM   4593 C  CD  . PRO B 1 393 ? 118.875 113.390 136.267 1.00 174.55 ? 1170 PRO B CD  1 
ATOM   4594 N  N   . GLU B 1 394 ? 120.954 109.302 136.564 1.00 207.12 ? 1171 GLU B N   1 
ATOM   4595 C  CA  . GLU B 1 394 ? 120.732 107.957 137.078 1.00 208.10 ? 1171 GLU B CA  1 
ATOM   4596 C  C   . GLU B 1 394 ? 120.203 108.013 138.506 1.00 207.77 ? 1171 GLU B C   1 
ATOM   4597 O  O   . GLU B 1 394 ? 120.772 108.692 139.366 1.00 207.40 ? 1171 GLU B O   1 
ATOM   4598 C  CB  . GLU B 1 394 ? 122.027 107.150 137.024 1.00 208.45 ? 1171 GLU B CB  1 
ATOM   4599 C  CG  . GLU B 1 394 ? 121.852 105.677 137.355 1.00 209.12 ? 1171 GLU B CG  1 
ATOM   4600 C  CD  . GLU B 1 394 ? 120.869 104.985 136.431 1.00 209.45 ? 1171 GLU B CD  1 
ATOM   4601 O  OE1 . GLU B 1 394 ? 120.925 105.232 135.208 1.00 209.14 ? 1171 GLU B OE1 1 
ATOM   4602 O  OE2 . GLU B 1 394 ? 120.041 104.193 136.928 1.00 209.41 ? 1171 GLU B OE2 1 
ATOM   4603 N  N   . GLY B 1 395 ? 119.110 107.295 138.756 1.00 202.48 ? 1172 GLY B N   1 
ATOM   4604 C  CA  . GLY B 1 395 ? 118.512 107.240 140.072 1.00 202.47 ? 1172 GLY B CA  1 
ATOM   4605 C  C   . GLY B 1 395 ? 117.634 108.416 140.436 1.00 202.02 ? 1172 GLY B C   1 
ATOM   4606 O  O   . GLY B 1 395 ? 117.094 108.441 141.549 1.00 201.29 ? 1172 GLY B O   1 
ATOM   4607 N  N   . GLN B 1 396 ? 117.466 109.387 139.541 1.00 199.96 ? 1173 GLN B N   1 
ATOM   4608 C  CA  . GLN B 1 396 ? 116.665 110.570 139.809 1.00 198.99 ? 1173 GLN B CA  1 
ATOM   4609 C  C   . GLN B 1 396 ? 115.632 110.751 138.706 1.00 199.43 ? 1173 GLN B C   1 
ATOM   4610 O  O   . GLN B 1 396 ? 115.785 110.245 137.591 1.00 199.71 ? 1173 GLN B O   1 
ATOM   4611 C  CB  . GLN B 1 396 ? 117.536 111.829 139.922 1.00 199.44 ? 1173 GLN B CB  1 
ATOM   4612 C  CG  . GLN B 1 396 ? 118.682 111.715 140.915 1.00 199.64 ? 1173 GLN B CG  1 
ATOM   4613 C  CD  . GLN B 1 396 ? 118.231 111.214 142.272 1.00 200.18 ? 1173 GLN B CD  1 
ATOM   4614 O  OE1 . GLN B 1 396 ? 117.280 111.735 142.855 1.00 200.45 ? 1173 GLN B OE1 1 
ATOM   4615 N  NE2 . GLN B 1 396 ? 118.914 110.197 142.784 1.00 199.89 ? 1173 GLN B NE2 1 
ATOM   4616 N  N   . CYS B 1 397 ? 114.570 111.487 139.034 1.00 204.23 ? 1174 CYS B N   1 
ATOM   4617 C  CA  . CYS B 1 397 ? 113.505 111.776 138.074 1.00 204.91 ? 1174 CYS B CA  1 
ATOM   4618 C  C   . CYS B 1 397 ? 112.939 113.150 138.419 1.00 204.98 ? 1174 CYS B C   1 
ATOM   4619 O  O   . CYS B 1 397 ? 112.204 113.292 139.401 1.00 205.49 ? 1174 CYS B O   1 
ATOM   4620 C  CB  . CYS B 1 397 ? 112.427 110.701 138.106 1.00 204.35 ? 1174 CYS B CB  1 
ATOM   4621 S  SG  . CYS B 1 397 ? 110.869 111.189 137.331 1.00 205.88 ? 1174 CYS B SG  1 
ATOM   4622 N  N   . GLU B 1 398 ? 113.286 114.152 137.612 1.00 195.76 ? 1175 GLU B N   1 
ATOM   4623 C  CA  . GLU B 1 398 ? 112.828 115.514 137.855 1.00 195.59 ? 1175 GLU B CA  1 
ATOM   4624 C  C   . GLU B 1 398 ? 112.243 116.131 136.591 1.00 194.63 ? 1175 GLU B C   1 
ATOM   4625 O  O   . GLU B 1 398 ? 111.396 117.027 136.665 1.00 195.94 ? 1175 GLU B O   1 
ATOM   4626 C  CB  . GLU B 1 398 ? 113.976 116.379 138.381 1.00 196.69 ? 1175 GLU B CB  1 
ATOM   4627 C  CG  . GLU B 1 398 ? 114.415 116.040 139.796 1.00 197.86 ? 1175 GLU B CG  1 
ATOM   4628 C  CD  . GLU B 1 398 ? 115.425 114.911 139.838 1.00 197.58 ? 1175 GLU B CD  1 
ATOM   4629 O  OE1 . GLU B 1 398 ? 115.929 114.523 138.763 1.00 198.07 ? 1175 GLU B OE1 1 
ATOM   4630 O  OE2 . GLU B 1 398 ? 115.716 114.411 140.945 1.00 197.09 ? 1175 GLU B OE2 1 
ATOM   4631 N  N   . TRP B 1 399 ? 112.688 115.662 135.429 1.00 170.29 ? 1176 TRP B N   1 
ATOM   4632 C  CA  . TRP B 1 399 ? 112.235 116.220 134.164 1.00 170.82 ? 1176 TRP B CA  1 
ATOM   4633 C  C   . TRP B 1 399 ? 110.838 115.720 133.822 1.00 170.66 ? 1176 TRP B C   1 
ATOM   4634 O  O   . TRP B 1 399 ? 110.508 114.550 134.037 1.00 171.25 ? 1176 TRP B O   1 
ATOM   4635 C  CB  . TRP B 1 399 ? 113.211 115.863 133.044 1.00 169.90 ? 1176 TRP B CB  1 
ATOM   4636 C  CG  . TRP B 1 399 ? 114.518 116.585 133.144 1.00 169.75 ? 1176 TRP B CG  1 
ATOM   4637 C  CD1 . TRP B 1 399 ? 115.633 116.173 133.812 1.00 170.76 ? 1176 TRP B CD1 1 
ATOM   4638 C  CD2 . TRP B 1 399 ? 114.847 117.850 132.557 1.00 169.28 ? 1176 TRP B CD2 1 
ATOM   4639 N  NE1 . TRP B 1 399 ? 116.636 117.102 133.678 1.00 170.27 ? 1176 TRP B NE1 1 
ATOM   4640 C  CE2 . TRP B 1 399 ? 116.179 118.141 132.911 1.00 169.85 ? 1176 TRP B CE2 1 
ATOM   4641 C  CE3 . TRP B 1 399 ? 114.145 118.764 131.765 1.00 170.07 ? 1176 TRP B CE3 1 
ATOM   4642 C  CZ2 . TRP B 1 399 ? 116.822 119.306 132.502 1.00 171.57 ? 1176 TRP B CZ2 1 
ATOM   4643 C  CZ3 . TRP B 1 399 ? 114.785 119.920 131.360 1.00 170.98 ? 1176 TRP B CZ3 1 
ATOM   4644 C  CH2 . TRP B 1 399 ? 116.110 120.181 131.729 1.00 171.76 ? 1176 TRP B CH2 1 
ATOM   4645 N  N   . HIS B 1 400 ? 110.016 116.619 133.284 1.00 177.96 ? 1177 HIS B N   1 
ATOM   4646 C  CA  . HIS B 1 400 ? 108.654 116.288 132.894 1.00 176.28 ? 1177 HIS B CA  1 
ATOM   4647 C  C   . HIS B 1 400 ? 108.281 117.107 131.668 1.00 176.88 ? 1177 HIS B C   1 
ATOM   4648 O  O   . HIS B 1 400 ? 108.921 118.112 131.350 1.00 180.20 ? 1177 HIS B O   1 
ATOM   4649 C  CB  . HIS B 1 400 ? 107.659 116.544 134.032 1.00 177.35 ? 1177 HIS B CB  1 
ATOM   4650 C  CG  . HIS B 1 400 ? 107.756 115.559 135.155 1.00 179.24 ? 1177 HIS B CG  1 
ATOM   4651 N  ND1 . HIS B 1 400 ? 108.694 115.665 136.158 1.00 180.27 ? 1177 HIS B ND1 1 
ATOM   4652 C  CD2 . HIS B 1 400 ? 107.031 114.450 135.433 1.00 180.46 ? 1177 HIS B CD2 1 
ATOM   4653 C  CE1 . HIS B 1 400 ? 108.544 114.664 137.006 1.00 180.97 ? 1177 HIS B CE1 1 
ATOM   4654 N  NE2 . HIS B 1 400 ? 107.541 113.912 136.589 1.00 181.50 ? 1177 HIS B NE2 1 
ATOM   4655 N  N   . TYR B 1 401 ? 107.232 116.664 130.981 1.00 151.46 ? 1178 TYR B N   1 
ATOM   4656 C  CA  . TYR B 1 401 ? 106.744 117.326 129.778 1.00 153.33 ? 1178 TYR B CA  1 
ATOM   4657 C  C   . TYR B 1 401 ? 105.547 118.198 130.138 1.00 152.74 ? 1178 TYR B C   1 
ATOM   4658 O  O   . TYR B 1 401 ? 104.543 117.698 130.656 1.00 153.38 ? 1178 TYR B O   1 
ATOM   4659 C  CB  . TYR B 1 401 ? 106.363 116.303 128.709 1.00 153.16 ? 1178 TYR B CB  1 
ATOM   4660 C  CG  . TYR B 1 401 ? 105.465 116.857 127.627 1.00 153.03 ? 1178 TYR B CG  1 
ATOM   4661 C  CD1 . TYR B 1 401 ? 105.907 117.861 126.776 1.00 152.58 ? 1178 TYR B CD1 1 
ATOM   4662 C  CD2 . TYR B 1 401 ? 104.175 116.375 127.456 1.00 153.84 ? 1178 TYR B CD2 1 
ATOM   4663 C  CE1 . TYR B 1 401 ? 105.090 118.370 125.787 1.00 153.16 ? 1178 TYR B CE1 1 
ATOM   4664 C  CE2 . TYR B 1 401 ? 103.350 116.878 126.468 1.00 154.30 ? 1178 TYR B CE2 1 
ATOM   4665 C  CZ  . TYR B 1 401 ? 103.812 117.875 125.637 1.00 154.21 ? 1178 TYR B CZ  1 
ATOM   4666 O  OH  . TYR B 1 401 ? 102.994 118.379 124.653 1.00 154.15 ? 1178 TYR B OH  1 
ATOM   4667 N  N   . GLN B 1 402 ? 105.656 119.494 129.861 1.00 158.40 ? 1179 GLN B N   1 
ATOM   4668 C  CA  . GLN B 1 402 ? 104.581 120.440 130.137 1.00 156.97 ? 1179 GLN B CA  1 
ATOM   4669 C  C   . GLN B 1 402 ? 104.029 120.985 128.829 1.00 157.91 ? 1179 GLN B C   1 
ATOM   4670 O  O   . GLN B 1 402 ? 104.705 121.788 128.167 1.00 159.45 ? 1179 GLN B O   1 
ATOM   4671 C  CB  . GLN B 1 402 ? 105.081 121.583 131.022 1.00 159.20 ? 1179 GLN B CB  1 
ATOM   4672 C  CG  . GLN B 1 402 ? 105.869 121.125 132.237 1.00 161.30 ? 1179 GLN B CG  1 
ATOM   4673 C  CD  . GLN B 1 402 ? 104.983 120.536 133.315 1.00 162.20 ? 1179 GLN B CD  1 
ATOM   4674 O  OE1 . GLN B 1 402 ? 103.780 120.792 133.355 1.00 162.14 ? 1179 GLN B OE1 1 
ATOM   4675 N  NE2 . GLN B 1 402 ? 105.575 119.741 134.199 1.00 161.90 ? 1179 GLN B NE2 1 
ATOM   4676 N  N   . PRO B 1 403 ? 102.829 120.578 128.408 1.00 161.43 ? 1180 PRO B N   1 
ATOM   4677 C  CA  . PRO B 1 403 ? 102.278 121.107 127.149 1.00 162.82 ? 1180 PRO B CA  1 
ATOM   4678 C  C   . PRO B 1 403 ? 102.065 122.609 127.166 1.00 162.53 ? 1180 PRO B C   1 
ATOM   4679 O  O   . PRO B 1 403 ? 102.224 123.261 126.127 1.00 161.45 ? 1180 PRO B O   1 
ATOM   4680 C  CB  . PRO B 1 403 ? 100.948 120.352 127.001 1.00 163.63 ? 1180 PRO B CB  1 
ATOM   4681 C  CG  . PRO B 1 403 ? 101.059 119.169 127.914 1.00 164.25 ? 1180 PRO B CG  1 
ATOM   4682 C  CD  . PRO B 1 403 ? 101.924 119.611 129.049 1.00 162.76 ? 1180 PRO B CD  1 
ATOM   4683 N  N   . CYS B 1 404 ? 101.709 123.181 128.315 1.00 191.35 ? 1181 CYS B N   1 
ATOM   4684 C  CA  . CYS B 1 404 ? 101.454 124.611 128.419 1.00 192.55 ? 1181 CYS B CA  1 
ATOM   4685 C  C   . CYS B 1 404 ? 102.677 125.409 128.848 1.00 193.13 ? 1181 CYS B C   1 
ATOM   4686 O  O   . CYS B 1 404 ? 102.682 126.634 128.691 1.00 193.43 ? 1181 CYS B O   1 
ATOM   4687 C  CB  . CYS B 1 404 ? 100.310 124.871 129.405 1.00 194.52 ? 1181 CYS B CB  1 
ATOM   4688 S  SG  . CYS B 1 404 ? 99.038  123.586 129.433 1.00 198.73 ? 1181 CYS B SG  1 
ATOM   4689 N  N   . GLY B 1 405 ? 103.705 124.754 129.380 1.00 195.77 ? 1182 GLY B N   1 
ATOM   4690 C  CA  . GLY B 1 405 ? 104.884 125.455 129.848 1.00 195.63 ? 1182 GLY B CA  1 
ATOM   4691 C  C   . GLY B 1 405 ? 104.697 126.055 131.226 1.00 197.06 ? 1182 GLY B C   1 
ATOM   4692 O  O   . GLY B 1 405 ? 103.625 126.579 131.541 1.00 198.81 ? 1182 GLY B O   1 
ATOM   4693 N  N   . VAL B 1 406 ? 105.733 125.983 132.056 1.00 194.73 ? 1183 VAL B N   1 
ATOM   4694 C  CA  . VAL B 1 406 ? 105.673 126.509 133.417 1.00 195.45 ? 1183 VAL B CA  1 
ATOM   4695 C  C   . VAL B 1 406 ? 105.595 128.031 133.363 1.00 196.05 ? 1183 VAL B C   1 
ATOM   4696 O  O   . VAL B 1 406 ? 106.208 128.652 132.482 1.00 195.06 ? 1183 VAL B O   1 
ATOM   4697 C  CB  . VAL B 1 406 ? 106.877 126.041 134.250 1.00 194.17 ? 1183 VAL B CB  1 
ATOM   4698 C  CG1 . VAL B 1 406 ? 106.798 124.543 134.495 1.00 193.68 ? 1183 VAL B CG1 1 
ATOM   4699 C  CG2 . VAL B 1 406 ? 108.181 126.400 133.552 1.00 194.23 ? 1183 VAL B CG2 1 
ATOM   4700 N  N   . PRO B 1 407 ? 104.847 128.670 134.266 1.00 224.50 ? 1184 PRO B N   1 
ATOM   4701 C  CA  . PRO B 1 407 ? 104.789 130.139 134.267 1.00 224.57 ? 1184 PRO B CA  1 
ATOM   4702 C  C   . PRO B 1 407 ? 106.117 130.765 134.661 1.00 224.18 ? 1184 PRO B C   1 
ATOM   4703 O  O   . PRO B 1 407 ? 106.619 131.660 133.975 1.00 224.12 ? 1184 PRO B O   1 
ATOM   4704 C  CB  . PRO B 1 407 ? 103.690 130.449 135.291 1.00 225.18 ? 1184 PRO B CB  1 
ATOM   4705 C  CG  . PRO B 1 407 ? 103.632 129.243 136.169 1.00 224.79 ? 1184 PRO B CG  1 
ATOM   4706 C  CD  . PRO B 1 407 ? 103.982 128.074 135.298 1.00 225.10 ? 1184 PRO B CD  1 
ATOM   4707 N  N   . CYS B 1 408 ? 106.693 130.297 135.766 1.00 232.64 ? 1185 CYS B N   1 
ATOM   4708 C  CA  . CYS B 1 408 ? 107.985 130.787 136.224 1.00 233.48 ? 1185 CYS B CA  1 
ATOM   4709 C  C   . CYS B 1 408 ? 108.622 129.728 137.110 1.00 232.76 ? 1185 CYS B C   1 
ATOM   4710 O  O   . CYS B 1 408 ? 107.931 129.019 137.847 1.00 232.06 ? 1185 CYS B O   1 
ATOM   4711 C  CB  . CYS B 1 408 ? 107.852 132.114 136.980 1.00 234.86 ? 1185 CYS B CB  1 
ATOM   4712 S  SG  . CYS B 1 408 ? 107.045 131.989 138.592 1.00 236.61 ? 1185 CYS B SG  1 
ATOM   4713 N  N   . LEU B 1 409 ? 109.946 129.628 137.025 1.00 219.55 ? 1186 LEU B N   1 
ATOM   4714 C  CA  . LEU B 1 409 ? 110.701 128.665 137.811 1.00 218.66 ? 1186 LEU B CA  1 
ATOM   4715 C  C   . LEU B 1 409 ? 111.928 129.350 138.393 1.00 219.60 ? 1186 LEU B C   1 
ATOM   4716 O  O   . LEU B 1 409 ? 112.404 130.365 137.878 1.00 221.15 ? 1186 LEU B O   1 
ATOM   4717 C  CB  . LEU B 1 409 ? 111.110 127.445 136.974 1.00 218.45 ? 1186 LEU B CB  1 
ATOM   4718 C  CG  . LEU B 1 409 ? 112.424 127.533 136.194 1.00 219.04 ? 1186 LEU B CG  1 
ATOM   4719 C  CD1 . LEU B 1 409 ? 112.883 126.147 135.768 1.00 219.46 ? 1186 LEU B CD1 1 
ATOM   4720 C  CD2 . LEU B 1 409 ? 112.279 128.444 134.985 1.00 219.42 ? 1186 LEU B CD2 1 
ATOM   4721 N  N   . ARG B 1 410 ? 112.436 128.781 139.482 1.00 235.41 ? 1187 ARG B N   1 
ATOM   4722 C  CA  . ARG B 1 410 ? 113.577 129.343 140.194 1.00 236.78 ? 1187 ARG B CA  1 
ATOM   4723 C  C   . ARG B 1 410 ? 114.866 128.744 139.645 1.00 237.25 ? 1187 ARG B C   1 
ATOM   4724 O  O   . ARG B 1 410 ? 115.076 127.529 139.726 1.00 237.19 ? 1187 ARG B O   1 
ATOM   4725 C  CB  . ARG B 1 410 ? 113.455 129.081 141.694 1.00 236.66 ? 1187 ARG B CB  1 
ATOM   4726 C  CG  . ARG B 1 410 ? 112.034 129.172 142.224 1.00 236.05 ? 1187 ARG B CG  1 
ATOM   4727 C  CD  . ARG B 1 410 ? 111.864 128.353 143.492 1.00 236.01 ? 1187 ARG B CD  1 
ATOM   4728 N  NE  . ARG B 1 410 ? 113.019 128.469 144.375 1.00 236.09 ? 1187 ARG B NE  1 
ATOM   4729 C  CZ  . ARG B 1 410 ? 113.074 127.977 145.604 1.00 236.43 ? 1187 ARG B CZ  1 
ATOM   4730 N  NH1 . ARG B 1 410 ? 112.053 127.322 146.133 1.00 236.68 ? 1187 ARG B NH1 1 
ATOM   4731 N  NH2 . ARG B 1 410 ? 114.181 128.146 146.322 1.00 236.45 ? 1187 ARG B NH2 1 
ATOM   4732 N  N   . THR B 1 411 ? 115.722 129.594 139.090 1.00 256.51 ? 1188 THR B N   1 
ATOM   4733 C  CA  . THR B 1 411 ? 117.015 129.192 138.554 1.00 256.54 ? 1188 THR B CA  1 
ATOM   4734 C  C   . THR B 1 411 ? 118.123 129.949 139.286 1.00 256.92 ? 1188 THR B C   1 
ATOM   4735 O  O   . THR B 1 411 ? 117.878 130.663 140.262 1.00 257.27 ? 1188 THR B O   1 
ATOM   4736 C  CB  . THR B 1 411 ? 117.076 129.434 137.043 1.00 256.70 ? 1188 THR B CB  1 
ATOM   4737 O  OG1 . THR B 1 411 ? 117.001 130.841 136.780 1.00 257.42 ? 1188 THR B OG1 1 
ATOM   4738 C  CG2 . THR B 1 411 ? 115.927 128.729 136.340 1.00 256.72 ? 1188 THR B CG2 1 
ATOM   4739 N  N   . CYS B 1 412 ? 119.357 129.779 138.806 1.00 264.73 ? 1189 CYS B N   1 
ATOM   4740 C  CA  . CYS B 1 412 ? 120.484 130.487 139.406 1.00 265.19 ? 1189 CYS B CA  1 
ATOM   4741 C  C   . CYS B 1 412 ? 120.365 131.992 139.203 1.00 264.92 ? 1189 CYS B C   1 
ATOM   4742 O  O   . CYS B 1 412 ? 120.605 132.770 140.134 1.00 264.88 ? 1189 CYS B O   1 
ATOM   4743 C  CB  . CYS B 1 412 ? 121.799 129.968 138.826 1.00 265.44 ? 1189 CYS B CB  1 
ATOM   4744 S  SG  . CYS B 1 412 ? 122.624 128.728 139.850 1.00 268.80 ? 1189 CYS B SG  1 
ATOM   4745 N  N   . ARG B 1 413 ? 119.995 132.421 137.997 1.00 251.70 ? 1190 ARG B N   1 
ATOM   4746 C  CA  . ARG B 1 413 ? 119.835 133.841 137.711 1.00 251.73 ? 1190 ARG B CA  1 
ATOM   4747 C  C   . ARG B 1 413 ? 118.452 134.367 138.067 1.00 251.66 ? 1190 ARG B C   1 
ATOM   4748 O  O   . ARG B 1 413 ? 118.255 135.587 138.072 1.00 250.92 ? 1190 ARG B O   1 
ATOM   4749 C  CB  . ARG B 1 413 ? 120.124 134.116 136.233 1.00 251.80 ? 1190 ARG B CB  1 
ATOM   4750 C  CG  . ARG B 1 413 ? 121.439 133.534 135.740 1.00 251.34 ? 1190 ARG B CG  1 
ATOM   4751 C  CD  . ARG B 1 413 ? 121.472 133.450 134.223 1.00 251.95 ? 1190 ARG B CD  1 
ATOM   4752 N  NE  . ARG B 1 413 ? 120.318 132.736 133.690 1.00 252.76 ? 1190 ARG B NE  1 
ATOM   4753 C  CZ  . ARG B 1 413 ? 120.098 132.528 132.399 1.00 252.02 ? 1190 ARG B CZ  1 
ATOM   4754 N  NH1 . ARG B 1 413 ? 120.937 132.967 131.475 1.00 251.68 ? 1190 ARG B NH1 1 
ATOM   4755 N  NH2 . ARG B 1 413 ? 119.007 131.864 132.026 1.00 251.23 ? 1190 ARG B NH2 1 
ATOM   4756 N  N   . ASN B 1 414 ? 117.497 133.489 138.361 1.00 262.62 ? 1191 ASN B N   1 
ATOM   4757 C  CA  . ASN B 1 414 ? 116.140 133.893 138.731 1.00 262.92 ? 1191 ASN B CA  1 
ATOM   4758 C  C   . ASN B 1 414 ? 115.822 133.358 140.119 1.00 263.26 ? 1191 ASN B C   1 
ATOM   4759 O  O   . ASN B 1 414 ? 115.452 132.179 140.263 1.00 263.57 ? 1191 ASN B O   1 
ATOM   4760 C  CB  . ASN B 1 414 ? 115.122 133.385 137.712 1.00 262.95 ? 1191 ASN B CB  1 
ATOM   4761 C  CG  . ASN B 1 414 ? 113.700 133.781 138.060 1.00 263.10 ? 1191 ASN B CG  1 
ATOM   4762 O  OD1 . ASN B 1 414 ? 113.473 134.746 138.789 1.00 263.12 ? 1191 ASN B OD1 1 
ATOM   4763 N  ND2 . ASN B 1 414 ? 112.734 133.034 137.539 1.00 263.42 ? 1191 ASN B ND2 1 
ATOM   4764 N  N   . PRO B 1 415 ? 115.950 134.171 141.164 1.00 257.76 ? 1192 PRO B N   1 
ATOM   4765 C  CA  . PRO B 1 415 ? 115.656 133.694 142.520 1.00 257.03 ? 1192 PRO B CA  1 
ATOM   4766 C  C   . PRO B 1 415 ? 114.182 133.350 142.687 1.00 258.06 ? 1192 PRO B C   1 
ATOM   4767 O  O   . PRO B 1 415 ? 113.345 133.589 141.814 1.00 258.61 ? 1192 PRO B O   1 
ATOM   4768 C  CB  . PRO B 1 415 ? 116.057 134.874 143.412 1.00 256.65 ? 1192 PRO B CB  1 
ATOM   4769 C  CG  . PRO B 1 415 ? 116.995 135.688 142.575 1.00 256.56 ? 1192 PRO B CG  1 
ATOM   4770 C  CD  . PRO B 1 415 ? 116.511 135.532 141.167 1.00 257.38 ? 1192 PRO B CD  1 
ATOM   4771 N  N   . ARG B 1 416 ? 113.875 132.772 143.850 1.00 270.78 ? 1193 ARG B N   1 
ATOM   4772 C  CA  . ARG B 1 416 ? 112.505 132.358 144.139 1.00 270.93 ? 1193 ARG B CA  1 
ATOM   4773 C  C   . ARG B 1 416 ? 111.565 133.554 144.212 1.00 271.54 ? 1193 ARG B C   1 
ATOM   4774 O  O   . ARG B 1 416 ? 110.426 133.486 143.733 1.00 271.06 ? 1193 ARG B O   1 
ATOM   4775 C  CB  . ARG B 1 416 ? 112.466 131.562 145.443 1.00 271.15 ? 1193 ARG B CB  1 
ATOM   4776 C  CG  . ARG B 1 416 ? 111.068 131.187 145.906 1.00 271.49 ? 1193 ARG B CG  1 
ATOM   4777 C  CD  . ARG B 1 416 ? 111.089 130.626 147.319 1.00 272.22 ? 1193 ARG B CD  1 
ATOM   4778 N  NE  . ARG B 1 416 ? 111.669 131.565 148.271 1.00 272.51 ? 1193 ARG B NE  1 
ATOM   4779 C  CZ  . ARG B 1 416 ? 111.798 131.332 149.570 1.00 271.99 ? 1193 ARG B CZ  1 
ATOM   4780 N  NH1 . ARG B 1 416 ? 111.397 130.193 150.111 1.00 271.99 ? 1193 ARG B NH1 1 
ATOM   4781 N  NH2 . ARG B 1 416 ? 112.344 132.264 150.345 1.00 271.80 ? 1193 ARG B NH2 1 
ATOM   4782 N  N   . GLY B 1 417 ? 112.022 134.660 144.799 1.00 286.15 ? 1194 GLY B N   1 
ATOM   4783 C  CA  . GLY B 1 417 ? 111.183 135.835 144.949 1.00 286.32 ? 1194 GLY B CA  1 
ATOM   4784 C  C   . GLY B 1 417 ? 110.887 136.573 143.660 1.00 286.95 ? 1194 GLY B C   1 
ATOM   4785 O  O   . GLY B 1 417 ? 110.055 137.487 143.671 1.00 287.06 ? 1194 GLY B O   1 
ATOM   4786 N  N   . ASP B 1 418 ? 111.540 136.205 142.562 1.00 289.38 ? 1195 ASP B N   1 
ATOM   4787 C  CA  . ASP B 1 418 ? 111.335 136.842 141.270 1.00 289.34 ? 1195 ASP B CA  1 
ATOM   4788 C  C   . ASP B 1 418 ? 110.694 135.857 140.301 1.00 288.57 ? 1195 ASP B C   1 
ATOM   4789 O  O   . ASP B 1 418 ? 111.032 134.669 140.292 1.00 288.15 ? 1195 ASP B O   1 
ATOM   4790 C  CB  . ASP B 1 418 ? 112.657 137.358 140.697 1.00 289.27 ? 1195 ASP B CB  1 
ATOM   4791 C  CG  . ASP B 1 418 ? 113.460 138.151 141.710 1.00 289.06 ? 1195 ASP B CG  1 
ATOM   4792 O  OD1 . ASP B 1 418 ? 113.286 139.386 141.773 1.00 289.09 ? 1195 ASP B OD1 1 
ATOM   4793 O  OD2 . ASP B 1 418 ? 114.262 137.539 142.445 1.00 288.60 ? 1195 ASP B OD2 1 
ATOM   4794 N  N   . CYS B 1 419 ? 109.766 136.359 139.488 1.00 286.28 ? 1196 CYS B N   1 
ATOM   4795 C  CA  . CYS B 1 419 ? 109.073 135.532 138.503 1.00 286.20 ? 1196 CYS B CA  1 
ATOM   4796 C  C   . CYS B 1 419 ? 108.694 136.423 137.329 1.00 286.04 ? 1196 CYS B C   1 
ATOM   4797 O  O   . CYS B 1 419 ? 107.776 137.241 137.443 1.00 285.94 ? 1196 CYS B O   1 
ATOM   4798 C  CB  . CYS B 1 419 ? 107.841 134.867 139.110 1.00 286.16 ? 1196 CYS B CB  1 
ATOM   4799 S  SG  . CYS B 1 419 ? 108.134 133.217 139.788 1.00 287.46 ? 1196 CYS B SG  1 
ATOM   4800 N  N   . LEU B 1 420 ? 109.396 136.265 136.209 1.00 266.56 ? 1197 LEU B N   1 
ATOM   4801 C  CA  . LEU B 1 420 ? 109.156 137.073 135.015 1.00 265.89 ? 1197 LEU B CA  1 
ATOM   4802 C  C   . LEU B 1 420 ? 108.140 136.352 134.138 1.00 265.88 ? 1197 LEU B C   1 
ATOM   4803 O  O   . LEU B 1 420 ? 108.474 135.392 133.439 1.00 265.09 ? 1197 LEU B O   1 
ATOM   4804 C  CB  . LEU B 1 420 ? 110.460 137.328 134.267 1.00 265.08 ? 1197 LEU B CB  1 
ATOM   4805 C  CG  . LEU B 1 420 ? 111.556 138.057 135.047 1.00 265.02 ? 1197 LEU B CG  1 
ATOM   4806 C  CD1 . LEU B 1 420 ? 112.763 138.319 134.160 1.00 265.09 ? 1197 LEU B CD1 1 
ATOM   4807 C  CD2 . LEU B 1 420 ? 111.024 139.355 135.634 1.00 265.17 ? 1197 LEU B CD2 1 
ATOM   4808 N  N   . ARG B 1 421 ? 106.891 136.816 134.176 1.00 264.71 ? 1198 ARG B N   1 
ATOM   4809 C  CA  . ARG B 1 421 ? 105.816 136.243 133.368 1.00 264.43 ? 1198 ARG B CA  1 
ATOM   4810 C  C   . ARG B 1 421 ? 105.618 137.129 132.140 1.00 264.37 ? 1198 ARG B C   1 
ATOM   4811 O  O   . ARG B 1 421 ? 104.672 137.911 132.042 1.00 263.67 ? 1198 ARG B O   1 
ATOM   4812 C  CB  . ARG B 1 421 ? 104.538 136.110 134.190 1.00 263.80 ? 1198 ARG B CB  1 
ATOM   4813 C  CG  . ARG B 1 421 ? 104.355 137.202 135.232 1.00 263.68 ? 1198 ARG B CG  1 
ATOM   4814 C  CD  . ARG B 1 421 ? 103.310 136.811 136.263 1.00 263.67 ? 1198 ARG B CD  1 
ATOM   4815 N  NE  . ARG B 1 421 ? 103.624 135.540 136.904 1.00 263.37 ? 1198 ARG B NE  1 
ATOM   4816 C  CZ  . ARG B 1 421 ? 104.349 135.416 138.008 1.00 263.01 ? 1198 ARG B CZ  1 
ATOM   4817 N  NH1 . ARG B 1 421 ? 104.855 136.472 138.624 1.00 262.44 ? 1198 ARG B NH1 1 
ATOM   4818 N  NH2 . ARG B 1 421 ? 104.572 134.203 138.505 1.00 263.10 ? 1198 ARG B NH2 1 
ATOM   4819 N  N   . ASP B 1 422 ? 106.540 136.996 131.187 1.00 267.85 ? 1199 ASP B N   1 
ATOM   4820 C  CA  . ASP B 1 422 ? 106.518 137.792 129.967 1.00 267.44 ? 1199 ASP B CA  1 
ATOM   4821 C  C   . ASP B 1 422 ? 106.284 136.977 128.706 1.00 267.18 ? 1199 ASP B C   1 
ATOM   4822 O  O   . ASP B 1 422 ? 105.707 137.499 127.750 1.00 266.87 ? 1199 ASP B O   1 
ATOM   4823 C  CB  . ASP B 1 422 ? 107.833 138.567 129.815 1.00 267.72 ? 1199 ASP B CB  1 
ATOM   4824 C  CG  . ASP B 1 422 ? 108.143 139.432 131.021 1.00 267.63 ? 1199 ASP B CG  1 
ATOM   4825 O  OD1 . ASP B 1 422 ? 107.199 139.793 131.755 1.00 267.80 ? 1199 ASP B OD1 1 
ATOM   4826 O  OD2 . ASP B 1 422 ? 109.331 139.752 131.235 1.00 267.20 ? 1199 ASP B OD2 1 
ATOM   4827 N  N   . VAL B 1 423 ? 106.712 135.718 128.678 1.00 251.12 ? 1200 VAL B N   1 
ATOM   4828 C  CA  . VAL B 1 423 ? 106.566 134.856 127.512 1.00 250.25 ? 1200 VAL B CA  1 
ATOM   4829 C  C   . VAL B 1 423 ? 105.677 133.678 127.882 1.00 249.86 ? 1200 VAL B C   1 
ATOM   4830 O  O   . VAL B 1 423 ? 105.819 133.094 128.962 1.00 250.23 ? 1200 VAL B O   1 
ATOM   4831 C  CB  . VAL B 1 423 ? 107.933 134.367 126.989 1.00 250.33 ? 1200 VAL B CB  1 
ATOM   4832 C  CG1 . VAL B 1 423 ? 108.591 135.444 126.142 1.00 250.54 ? 1200 VAL B CG1 1 
ATOM   4833 C  CG2 . VAL B 1 423 ? 108.835 133.970 128.148 1.00 249.62 ? 1200 VAL B CG2 1 
ATOM   4834 N  N   . ARG B 1 424 ? 104.756 133.335 126.984 1.00 218.95 ? 1201 ARG B N   1 
ATOM   4835 C  CA  . ARG B 1 424 ? 103.830 132.233 127.191 1.00 217.80 ? 1201 ARG B CA  1 
ATOM   4836 C  C   . ARG B 1 424 ? 103.765 131.376 125.935 1.00 217.68 ? 1201 ARG B C   1 
ATOM   4837 O  O   . ARG B 1 424 ? 103.996 131.857 124.823 1.00 217.16 ? 1201 ARG B O   1 
ATOM   4838 C  CB  . ARG B 1 424 ? 102.427 132.737 127.553 1.00 216.54 ? 1201 ARG B CB  1 
ATOM   4839 C  CG  . ARG B 1 424 ? 101.849 133.726 126.554 1.00 216.83 ? 1201 ARG B CG  1 
ATOM   4840 C  CD  . ARG B 1 424 ? 100.615 134.415 127.110 1.00 217.41 ? 1201 ARG B CD  1 
ATOM   4841 N  NE  . ARG B 1 424 ? 100.897 135.113 128.359 1.00 218.58 ? 1201 ARG B NE  1 
ATOM   4842 C  CZ  . ARG B 1 424 ? 99.999  135.794 129.056 1.00 218.95 ? 1201 ARG B CZ  1 
ATOM   4843 N  NH1 . ARG B 1 424 ? 98.742  135.893 128.654 1.00 219.04 ? 1201 ARG B NH1 1 
ATOM   4844 N  NH2 . ARG B 1 424 ? 100.370 136.392 130.185 1.00 218.60 ? 1201 ARG B NH2 1 
ATOM   4845 N  N   . GLY B 1 425 ? 103.446 130.099 126.126 1.00 191.91 ? 1202 GLY B N   1 
ATOM   4846 C  CA  . GLY B 1 425 ? 103.329 129.176 125.015 1.00 190.75 ? 1202 GLY B CA  1 
ATOM   4847 C  C   . GLY B 1 425 ? 104.651 128.564 124.599 1.00 189.90 ? 1202 GLY B C   1 
ATOM   4848 O  O   . GLY B 1 425 ? 105.055 128.672 123.438 1.00 189.69 ? 1202 GLY B O   1 
ATOM   4849 N  N   . LEU B 1 426 ? 105.335 127.919 125.542 1.00 173.10 ? 1203 LEU B N   1 
ATOM   4850 C  CA  . LEU B 1 426 ? 106.623 127.274 125.288 1.00 172.02 ? 1203 LEU B CA  1 
ATOM   4851 C  C   . LEU B 1 426 ? 106.552 125.849 125.827 1.00 173.98 ? 1203 LEU B C   1 
ATOM   4852 O  O   . LEU B 1 426 ? 106.606 125.635 127.042 1.00 175.73 ? 1203 LEU B O   1 
ATOM   4853 C  CB  . LEU B 1 426 ? 107.766 128.054 125.930 1.00 171.99 ? 1203 LEU B CB  1 
ATOM   4854 C  CG  . LEU B 1 426 ? 107.928 129.510 125.489 1.00 173.40 ? 1203 LEU B CG  1 
ATOM   4855 C  CD1 . LEU B 1 426 ? 107.306 130.455 126.505 1.00 176.11 ? 1203 LEU B CD1 1 
ATOM   4856 C  CD2 . LEU B 1 426 ? 109.395 129.842 125.271 1.00 173.28 ? 1203 LEU B CD2 1 
ATOM   4857 N  N   . GLU B 1 427 ? 106.434 124.880 124.926 1.00 167.06 ? 1204 GLU B N   1 
ATOM   4858 C  CA  . GLU B 1 427 ? 106.340 123.480 125.308 1.00 166.25 ? 1204 GLU B CA  1 
ATOM   4859 C  C   . GLU B 1 427 ? 107.711 122.814 125.256 1.00 166.50 ? 1204 GLU B C   1 
ATOM   4860 O  O   . GLU B 1 427 ? 108.647 123.304 124.619 1.00 166.89 ? 1204 GLU B O   1 
ATOM   4861 C  CB  . GLU B 1 427 ? 105.361 122.738 124.399 1.00 166.75 ? 1204 GLU B CB  1 
ATOM   4862 C  CG  . GLU B 1 427 ? 105.789 122.683 122.942 1.00 167.94 ? 1204 GLU B CG  1 
ATOM   4863 C  CD  . GLU B 1 427 ? 104.901 121.781 122.108 1.00 170.23 ? 1204 GLU B CD  1 
ATOM   4864 O  OE1 . GLU B 1 427 ? 104.413 120.765 122.645 1.00 171.13 ? 1204 GLU B OE1 1 
ATOM   4865 O  OE2 . GLU B 1 427 ? 104.690 122.089 120.917 1.00 170.47 ? 1204 GLU B OE2 1 
ATOM   4866 N  N   . GLY B 1 428 ? 107.818 121.679 125.942 1.00 175.61 ? 1205 GLY B N   1 
ATOM   4867 C  CA  . GLY B 1 428 ? 109.059 120.931 125.979 1.00 177.06 ? 1205 GLY B CA  1 
ATOM   4868 C  C   . GLY B 1 428 ? 109.324 120.284 127.322 1.00 176.42 ? 1205 GLY B C   1 
ATOM   4869 O  O   . GLY B 1 428 ? 108.490 120.357 128.229 1.00 177.40 ? 1205 GLY B O   1 
ATOM   4870 N  N   . CYS B 1 429 ? 110.482 119.643 127.461 1.00 176.04 ? 1206 CYS B N   1 
ATOM   4871 C  CA  . CYS B 1 429 ? 110.840 119.013 128.724 1.00 175.89 ? 1206 CYS B CA  1 
ATOM   4872 C  C   . CYS B 1 429 ? 111.252 120.072 129.739 1.00 174.23 ? 1206 CYS B C   1 
ATOM   4873 O  O   . CYS B 1 429 ? 112.069 120.948 129.441 1.00 175.72 ? 1206 CYS B O   1 
ATOM   4874 C  CB  . CYS B 1 429 ? 111.973 118.010 128.517 1.00 177.95 ? 1206 CYS B CB  1 
ATOM   4875 S  SG  . CYS B 1 429 ? 111.625 116.701 127.316 1.00 187.25 ? 1206 CYS B SG  1 
ATOM   4876 N  N   . TYR B 1 430 ? 110.683 119.992 130.940 1.00 160.59 ? 1207 TYR B N   1 
ATOM   4877 C  CA  . TYR B 1 430 ? 111.005 120.920 132.011 1.00 159.53 ? 1207 TYR B CA  1 
ATOM   4878 C  C   . TYR B 1 430 ? 111.303 120.151 133.290 1.00 160.03 ? 1207 TYR B C   1 
ATOM   4879 O  O   . TYR B 1 430 ? 110.676 119.118 133.557 1.00 163.36 ? 1207 TYR B O   1 
ATOM   4880 C  CB  . TYR B 1 430 ? 109.854 121.906 132.254 1.00 158.82 ? 1207 TYR B CB  1 
ATOM   4881 C  CG  . TYR B 1 430 ? 109.757 123.003 131.219 1.00 159.84 ? 1207 TYR B CG  1 
ATOM   4882 C  CD1 . TYR B 1 430 ? 110.462 124.190 131.369 1.00 160.38 ? 1207 TYR B CD1 1 
ATOM   4883 C  CD2 . TYR B 1 430 ? 108.961 122.853 130.093 1.00 161.57 ? 1207 TYR B CD2 1 
ATOM   4884 C  CE1 . TYR B 1 430 ? 110.377 125.195 130.426 1.00 160.99 ? 1207 TYR B CE1 1 
ATOM   4885 C  CE2 . TYR B 1 430 ? 108.869 123.853 129.144 1.00 162.62 ? 1207 TYR B CE2 1 
ATOM   4886 C  CZ  . TYR B 1 430 ? 109.579 125.022 129.316 1.00 161.77 ? 1207 TYR B CZ  1 
ATOM   4887 O  OH  . TYR B 1 430 ? 109.490 126.020 128.374 1.00 162.61 ? 1207 TYR B OH  1 
ATOM   4888 N  N   . PRO B 1 431 ? 112.247 120.625 134.098 1.00 148.20 ? 1208 PRO B N   1 
ATOM   4889 C  CA  . PRO B 1 431 ? 112.579 119.932 135.344 1.00 149.79 ? 1208 PRO B CA  1 
ATOM   4890 C  C   . PRO B 1 431 ? 111.703 120.369 136.506 1.00 151.23 ? 1208 PRO B C   1 
ATOM   4891 O  O   . PRO B 1 431 ? 111.247 121.511 136.592 1.00 150.79 ? 1208 PRO B O   1 
ATOM   4892 C  CB  . PRO B 1 431 ? 114.041 120.339 135.577 1.00 150.91 ? 1208 PRO B CB  1 
ATOM   4893 C  CG  . PRO B 1 431 ? 114.142 121.703 134.971 1.00 151.71 ? 1208 PRO B CG  1 
ATOM   4894 C  CD  . PRO B 1 431 ? 113.103 121.803 133.875 1.00 149.96 ? 1208 PRO B CD  1 
ATOM   4895 N  N   . LYS B 1 432 ? 111.472 119.425 137.414 1.00 185.80 ? 1209 LYS B N   1 
ATOM   4896 C  CA  . LYS B 1 432 ? 110.695 119.651 138.630 1.00 186.57 ? 1209 LYS B CA  1 
ATOM   4897 C  C   . LYS B 1 432 ? 111.614 119.372 139.814 1.00 186.39 ? 1209 LYS B C   1 
ATOM   4898 O  O   . LYS B 1 432 ? 111.738 118.230 140.264 1.00 186.16 ? 1209 LYS B O   1 
ATOM   4899 C  CB  . LYS B 1 432 ? 109.447 118.771 138.662 1.00 187.54 ? 1209 LYS B CB  1 
ATOM   4900 C  CG  . LYS B 1 432 ? 108.480 119.108 139.784 1.00 187.96 ? 1209 LYS B CG  1 
ATOM   4901 C  CD  . LYS B 1 432 ? 107.038 118.905 139.350 1.00 188.66 ? 1209 LYS B CD  1 
ATOM   4902 C  CE  . LYS B 1 432 ? 106.762 117.449 139.013 1.00 188.13 ? 1209 LYS B CE  1 
ATOM   4903 N  NZ  . LYS B 1 432 ? 105.326 117.100 139.195 1.00 188.25 ? 1209 LYS B NZ  1 
ATOM   4904 N  N   . CYS B 1 433 ? 112.261 120.420 140.314 1.00 210.30 ? 1210 CYS B N   1 
ATOM   4905 C  CA  . CYS B 1 433 ? 113.200 120.256 141.411 1.00 211.66 ? 1210 CYS B CA  1 
ATOM   4906 C  C   . CYS B 1 433 ? 112.459 119.878 142.692 1.00 212.27 ? 1210 CYS B C   1 
ATOM   4907 O  O   . CYS B 1 433 ? 111.354 120.371 142.941 1.00 213.11 ? 1210 CYS B O   1 
ATOM   4908 C  CB  . CYS B 1 433 ? 114.000 121.539 141.629 1.00 212.84 ? 1210 CYS B CB  1 
ATOM   4909 S  SG  . CYS B 1 433 ? 115.070 121.996 140.245 1.00 216.91 ? 1210 CYS B SG  1 
ATOM   4910 N  N   . PRO B 1 434 ? 113.035 119.010 143.518 1.00 209.63 ? 1211 PRO B N   1 
ATOM   4911 C  CA  . PRO B 1 434 ? 112.396 118.646 144.786 1.00 209.81 ? 1211 PRO B CA  1 
ATOM   4912 C  C   . PRO B 1 434 ? 112.432 119.810 145.759 1.00 211.12 ? 1211 PRO B C   1 
ATOM   4913 O  O   . PRO B 1 434 ? 113.167 120.786 145.540 1.00 212.13 ? 1211 PRO B O   1 
ATOM   4914 C  CB  . PRO B 1 434 ? 113.249 117.469 145.291 1.00 209.63 ? 1211 PRO B CB  1 
ATOM   4915 C  CG  . PRO B 1 434 ? 114.080 117.038 144.117 1.00 209.78 ? 1211 PRO B CG  1 
ATOM   4916 C  CD  . PRO B 1 434 ? 114.281 118.263 143.291 1.00 209.66 ? 1211 PRO B CD  1 
ATOM   4917 N  N   . PRO B 1 435 ? 111.642 119.757 146.838 1.00 225.06 ? 1212 PRO B N   1 
ATOM   4918 C  CA  . PRO B 1 435 ? 111.713 120.837 147.838 1.00 226.00 ? 1212 PRO B CA  1 
ATOM   4919 C  C   . PRO B 1 435 ? 113.106 121.027 148.411 1.00 225.78 ? 1212 PRO B C   1 
ATOM   4920 O  O   . PRO B 1 435 ? 113.513 122.163 148.680 1.00 226.06 ? 1212 PRO B O   1 
ATOM   4921 C  CB  . PRO B 1 435 ? 110.707 120.393 148.912 1.00 225.65 ? 1212 PRO B CB  1 
ATOM   4922 C  CG  . PRO B 1 435 ? 110.442 118.942 148.641 1.00 225.55 ? 1212 PRO B CG  1 
ATOM   4923 C  CD  . PRO B 1 435 ? 110.608 118.764 147.169 1.00 224.97 ? 1212 PRO B CD  1 
ATOM   4924 N  N   . GLU B 1 436 ? 113.851 119.942 148.604 1.00 223.87 ? 1213 GLU B N   1 
ATOM   4925 C  CA  . GLU B 1 436 ? 115.246 120.042 149.004 1.00 223.61 ? 1213 GLU B CA  1 
ATOM   4926 C  C   . GLU B 1 436 ? 116.094 120.407 147.793 1.00 224.25 ? 1213 GLU B C   1 
ATOM   4927 O  O   . GLU B 1 436 ? 116.021 119.746 146.752 1.00 223.63 ? 1213 GLU B O   1 
ATOM   4928 C  CB  . GLU B 1 436 ? 115.728 118.729 149.625 1.00 223.64 ? 1213 GLU B CB  1 
ATOM   4929 C  CG  . GLU B 1 436 ? 115.348 117.473 148.848 1.00 224.46 ? 1213 GLU B CG  1 
ATOM   4930 C  CD  . GLU B 1 436 ? 113.953 116.973 149.177 1.00 224.99 ? 1213 GLU B CD  1 
ATOM   4931 O  OE1 . GLU B 1 436 ? 113.243 117.648 149.951 1.00 225.21 ? 1213 GLU B OE1 1 
ATOM   4932 O  OE2 . GLU B 1 436 ? 113.567 115.904 148.660 1.00 225.15 ? 1213 GLU B OE2 1 
ATOM   4933 N  N   . ALA B 1 437 ? 116.895 121.467 147.933 1.00 237.07 ? 1214 ALA B N   1 
ATOM   4934 C  CA  . ALA B 1 437 ? 117.698 122.023 146.849 1.00 237.60 ? 1214 ALA B CA  1 
ATOM   4935 C  C   . ALA B 1 437 ? 116.825 122.321 145.634 1.00 237.40 ? 1214 ALA B C   1 
ATOM   4936 O  O   . ALA B 1 437 ? 116.968 121.667 144.593 1.00 236.72 ? 1214 ALA B O   1 
ATOM   4937 C  CB  . ALA B 1 437 ? 118.834 121.069 146.471 1.00 238.16 ? 1214 ALA B CB  1 
ATOM   4938 N  N   . PRO B 1 438 ? 115.916 123.290 145.722 1.00 237.56 ? 1215 PRO B N   1 
ATOM   4939 C  CA  . PRO B 1 438 ? 114.995 123.568 144.611 1.00 237.24 ? 1215 PRO B CA  1 
ATOM   4940 C  C   . PRO B 1 438 ? 115.486 124.602 143.607 1.00 237.47 ? 1215 PRO B C   1 
ATOM   4941 O  O   . PRO B 1 438 ? 114.690 125.035 142.768 1.00 237.03 ? 1215 PRO B O   1 
ATOM   4942 C  CB  . PRO B 1 438 ? 113.756 124.091 145.348 1.00 237.51 ? 1215 PRO B CB  1 
ATOM   4943 C  CG  . PRO B 1 438 ? 114.313 124.779 146.570 1.00 237.56 ? 1215 PRO B CG  1 
ATOM   4944 C  CD  . PRO B 1 438 ? 115.682 124.197 146.859 1.00 237.30 ? 1215 PRO B CD  1 
ATOM   4945 N  N   . ILE B 1 439 ? 116.750 125.006 143.664 1.00 254.54 ? 1216 ILE B N   1 
ATOM   4946 C  CA  . ILE B 1 439 ? 117.286 126.014 142.757 1.00 254.88 ? 1216 ILE B CA  1 
ATOM   4947 C  C   . ILE B 1 439 ? 117.907 125.308 141.559 1.00 255.17 ? 1216 ILE B C   1 
ATOM   4948 O  O   . ILE B 1 439 ? 118.804 124.472 141.716 1.00 256.05 ? 1216 ILE B O   1 
ATOM   4949 C  CB  . ILE B 1 439 ? 118.315 126.908 143.466 1.00 254.97 ? 1216 ILE B CB  1 
ATOM   4950 C  CG1 . ILE B 1 439 ? 117.616 127.879 144.419 1.00 254.70 ? 1216 ILE B CG1 1 
ATOM   4951 C  CG2 . ILE B 1 439 ? 119.150 127.671 142.448 1.00 255.10 ? 1216 ILE B CG2 1 
ATOM   4952 C  CD1 . ILE B 1 439 ? 116.435 128.598 143.804 1.00 254.14 ? 1216 ILE B CD1 1 
ATOM   4953 N  N   . PHE B 1 440 ? 117.429 125.641 140.363 1.00 241.85 ? 1217 PHE B N   1 
ATOM   4954 C  CA  . PHE B 1 440 ? 117.982 125.058 139.149 1.00 241.61 ? 1217 PHE B CA  1 
ATOM   4955 C  C   . PHE B 1 440 ? 119.353 125.659 138.862 1.00 242.60 ? 1217 PHE B C   1 
ATOM   4956 O  O   . PHE B 1 440 ? 119.516 126.883 138.851 1.00 242.46 ? 1217 PHE B O   1 
ATOM   4957 C  CB  . PHE B 1 440 ? 117.039 125.291 137.970 1.00 240.66 ? 1217 PHE B CB  1 
ATOM   4958 C  CG  . PHE B 1 440 ? 117.344 124.438 136.773 1.00 240.40 ? 1217 PHE B CG  1 
ATOM   4959 C  CD1 . PHE B 1 440 ? 117.444 123.062 136.894 1.00 240.54 ? 1217 PHE B CD1 1 
ATOM   4960 C  CD2 . PHE B 1 440 ? 117.526 125.010 135.526 1.00 240.51 ? 1217 PHE B CD2 1 
ATOM   4961 C  CE1 . PHE B 1 440 ? 117.723 122.273 135.794 1.00 240.19 ? 1217 PHE B CE1 1 
ATOM   4962 C  CE2 . PHE B 1 440 ? 117.805 124.227 134.422 1.00 240.49 ? 1217 PHE B CE2 1 
ATOM   4963 C  CZ  . PHE B 1 440 ? 117.904 122.857 134.557 1.00 240.15 ? 1217 PHE B CZ  1 
ATOM   4964 N  N   . ASP B 1 441 ? 120.341 124.792 138.630 1.00 275.45 ? 1218 ASP B N   1 
ATOM   4965 C  CA  . ASP B 1 441 ? 121.707 125.268 138.438 1.00 276.26 ? 1218 ASP B CA  1 
ATOM   4966 C  C   . ASP B 1 441 ? 121.880 125.933 137.076 1.00 276.10 ? 1218 ASP B C   1 
ATOM   4967 O  O   . ASP B 1 441 ? 122.741 126.807 136.920 1.00 276.41 ? 1218 ASP B O   1 
ATOM   4968 C  CB  . ASP B 1 441 ? 122.686 124.109 138.622 1.00 276.51 ? 1218 ASP B CB  1 
ATOM   4969 C  CG  . ASP B 1 441 ? 124.127 124.566 138.688 1.00 276.51 ? 1218 ASP B CG  1 
ATOM   4970 O  OD1 . ASP B 1 441 ? 124.384 125.652 139.249 1.00 277.21 ? 1218 ASP B OD1 1 
ATOM   4971 O  OD2 . ASP B 1 441 ? 125.008 123.826 138.204 1.00 276.05 ? 1218 ASP B OD2 1 
ATOM   4972 N  N   . GLU B 1 442 ? 121.084 125.527 136.088 1.00 267.39 ? 1219 GLU B N   1 
ATOM   4973 C  CA  . GLU B 1 442 ? 120.847 126.175 134.802 1.00 267.03 ? 1219 GLU B CA  1 
ATOM   4974 C  C   . GLU B 1 442 ? 122.013 126.039 133.820 1.00 267.24 ? 1219 GLU B C   1 
ATOM   4975 O  O   . GLU B 1 442 ? 121.865 126.442 132.665 1.00 267.32 ? 1219 GLU B O   1 
ATOM   4976 C  CB  . GLU B 1 442 ? 120.494 127.670 134.939 1.00 266.93 ? 1219 GLU B CB  1 
ATOM   4977 C  CG  . GLU B 1 442 ? 119.480 128.168 133.922 1.00 266.94 ? 1219 GLU B CG  1 
ATOM   4978 C  CD  . GLU B 1 442 ? 120.115 128.991 132.820 1.00 267.59 ? 1219 GLU B CD  1 
ATOM   4979 O  OE1 . GLU B 1 442 ? 121.293 129.379 132.969 1.00 267.98 ? 1219 GLU B OE1 1 
ATOM   4980 O  OE2 . GLU B 1 442 ? 119.437 129.250 131.803 1.00 267.57 ? 1219 GLU B OE2 1 
ATOM   4981 N  N   . ASP B 1 443 ? 123.159 125.488 134.218 1.00 265.59 ? 1220 ASP B N   1 
ATOM   4982 C  CA  . ASP B 1 443 ? 124.275 125.327 133.296 1.00 265.17 ? 1220 ASP B CA  1 
ATOM   4983 C  C   . ASP B 1 443 ? 124.676 123.879 133.058 1.00 265.25 ? 1220 ASP B C   1 
ATOM   4984 O  O   . ASP B 1 443 ? 125.299 123.594 132.029 1.00 265.39 ? 1220 ASP B O   1 
ATOM   4985 C  CB  . ASP B 1 443 ? 125.502 126.111 133.787 1.00 265.01 ? 1220 ASP B CB  1 
ATOM   4986 C  CG  . ASP B 1 443 ? 125.755 125.926 135.263 1.00 264.86 ? 1220 ASP B CG  1 
ATOM   4987 O  OD1 . ASP B 1 443 ? 124.924 125.270 135.919 1.00 265.23 ? 1220 ASP B OD1 1 
ATOM   4988 O  OD2 . ASP B 1 443 ? 126.779 126.434 135.767 1.00 264.55 ? 1220 ASP B OD2 1 
ATOM   4989 N  N   . LYS B 1 444 ? 124.344 122.957 133.968 1.00 263.64 ? 1221 LYS B N   1 
ATOM   4990 C  CA  . LYS B 1 444 ? 124.627 121.546 133.731 1.00 263.58 ? 1221 LYS B CA  1 
ATOM   4991 C  C   . LYS B 1 444 ? 123.423 120.658 134.038 1.00 263.17 ? 1221 LYS B C   1 
ATOM   4992 O  O   . LYS B 1 444 ? 123.601 119.467 134.322 1.00 263.61 ? 1221 LYS B O   1 
ATOM   4993 C  CB  . LYS B 1 444 ? 125.851 121.088 134.535 1.00 263.69 ? 1221 LYS B CB  1 
ATOM   4994 C  CG  . LYS B 1 444 ? 126.141 121.902 135.783 1.00 263.19 ? 1221 LYS B CG  1 
ATOM   4995 C  CD  . LYS B 1 444 ? 127.275 121.276 136.583 1.00 263.09 ? 1221 LYS B CD  1 
ATOM   4996 C  CE  . LYS B 1 444 ? 127.699 122.166 137.739 1.00 262.78 ? 1221 LYS B CE  1 
ATOM   4997 N  NZ  . LYS B 1 444 ? 128.340 123.424 137.266 1.00 263.32 ? 1221 LYS B NZ  1 
ATOM   4998 N  N   . MET B 1 445 ? 122.211 121.213 133.991 1.00 248.51 ? 1222 MET B N   1 
ATOM   4999 C  CA  . MET B 1 445 ? 120.964 120.447 134.010 1.00 248.28 ? 1222 MET B CA  1 
ATOM   5000 C  C   . MET B 1 445 ? 120.818 119.623 135.293 1.00 248.67 ? 1222 MET B C   1 
ATOM   5001 O  O   . MET B 1 445 ? 120.757 118.392 135.273 1.00 248.29 ? 1222 MET B O   1 
ATOM   5002 C  CB  . MET B 1 445 ? 120.859 119.554 132.768 1.00 247.21 ? 1222 MET B CB  1 
ATOM   5003 C  CG  . MET B 1 445 ? 120.998 120.294 131.444 1.00 247.07 ? 1222 MET B CG  1 
ATOM   5004 S  SD  . MET B 1 445 ? 120.030 121.815 131.369 1.00 246.79 ? 1222 MET B SD  1 
ATOM   5005 C  CE  . MET B 1 445 ? 121.325 123.053 131.393 1.00 247.57 ? 1222 MET B CE  1 
ATOM   5006 N  N   . GLN B 1 446 ? 120.759 120.330 136.419 1.00 265.49 ? 1223 GLN B N   1 
ATOM   5007 C  CA  . GLN B 1 446 ? 120.445 119.706 137.698 1.00 265.22 ? 1223 GLN B CA  1 
ATOM   5008 C  C   . GLN B 1 446 ? 120.006 120.791 138.670 1.00 265.57 ? 1223 GLN B C   1 
ATOM   5009 O  O   . GLN B 1 446 ? 120.176 121.987 138.418 1.00 266.03 ? 1223 GLN B O   1 
ATOM   5010 C  CB  . GLN B 1 446 ? 121.634 118.919 138.259 1.00 264.90 ? 1223 GLN B CB  1 
ATOM   5011 C  CG  . GLN B 1 446 ? 122.623 119.756 139.051 1.00 265.68 ? 1223 GLN B CG  1 
ATOM   5012 C  CD  . GLN B 1 446 ? 123.669 120.411 138.176 1.00 266.31 ? 1223 GLN B CD  1 
ATOM   5013 O  OE1 . GLN B 1 446 ? 123.347 121.091 137.202 1.00 266.71 ? 1223 GLN B OE1 1 
ATOM   5014 N  NE2 . GLN B 1 446 ? 124.934 120.208 138.521 1.00 266.11 ? 1223 GLN B NE2 1 
ATOM   5015 N  N   . CYS B 1 447 ? 119.435 120.356 139.789 1.00 262.56 ? 1224 CYS B N   1 
ATOM   5016 C  CA  . CYS B 1 447 ? 118.993 121.252 140.848 1.00 262.60 ? 1224 CYS B CA  1 
ATOM   5017 C  C   . CYS B 1 447 ? 120.025 121.259 141.968 1.00 262.44 ? 1224 CYS B C   1 
ATOM   5018 O  O   . CYS B 1 447 ? 120.491 120.198 142.396 1.00 262.51 ? 1224 CYS B O   1 
ATOM   5019 C  CB  . CYS B 1 447 ? 117.626 120.829 141.388 1.00 262.18 ? 1224 CYS B CB  1 
ATOM   5020 S  SG  . CYS B 1 447 ? 116.397 120.464 140.114 1.00 263.71 ? 1224 CYS B SG  1 
ATOM   5021 N  N   . VAL B 1 448 ? 120.380 122.456 142.437 1.00 262.47 ? 1225 VAL B N   1 
ATOM   5022 C  CA  . VAL B 1 448 ? 121.371 122.625 143.488 1.00 262.51 ? 1225 VAL B CA  1 
ATOM   5023 C  C   . VAL B 1 448 ? 120.753 123.428 144.624 1.00 262.42 ? 1225 VAL B C   1 
ATOM   5024 O  O   . VAL B 1 448 ? 119.733 124.100 144.461 1.00 262.59 ? 1225 VAL B O   1 
ATOM   5025 C  CB  . VAL B 1 448 ? 122.654 123.316 142.978 1.00 262.11 ? 1225 VAL B CB  1 
ATOM   5026 C  CG1 . VAL B 1 448 ? 123.377 122.423 141.981 1.00 261.89 ? 1225 VAL B CG1 1 
ATOM   5027 C  CG2 . VAL B 1 448 ? 122.318 124.661 142.354 1.00 262.52 ? 1225 VAL B CG2 1 
ATOM   5028 N  N   . ALA B 1 449 ? 121.389 123.341 145.794 1.00 257.34 ? 1226 ALA B N   1 
ATOM   5029 C  CA  . ALA B 1 449 ? 120.894 124.065 146.961 1.00 257.11 ? 1226 ALA B CA  1 
ATOM   5030 C  C   . ALA B 1 449 ? 121.024 125.571 146.771 1.00 257.73 ? 1226 ALA B C   1 
ATOM   5031 O  O   . ALA B 1 449 ? 120.058 126.317 146.969 1.00 257.63 ? 1226 ALA B O   1 
ATOM   5032 C  CB  . ALA B 1 449 ? 121.642 123.612 148.215 1.00 257.02 ? 1226 ALA B CB  1 
ATOM   5033 N  N   . THR B 1 450 ? 122.209 126.035 146.382 1.00 273.82 ? 1227 THR B N   1 
ATOM   5034 C  CA  . THR B 1 450 ? 122.440 127.457 146.173 1.00 274.15 ? 1227 THR B CA  1 
ATOM   5035 C  C   . THR B 1 450 ? 123.646 127.632 145.263 1.00 274.45 ? 1227 THR B C   1 
ATOM   5036 O  O   . THR B 1 450 ? 124.501 126.749 145.157 1.00 274.19 ? 1227 THR B O   1 
ATOM   5037 C  CB  . THR B 1 450 ? 122.658 128.196 147.499 1.00 274.35 ? 1227 THR B CB  1 
ATOM   5038 O  OG1 . THR B 1 450 ? 123.067 129.544 147.236 1.00 274.24 ? 1227 THR B OG1 1 
ATOM   5039 C  CG2 . THR B 1 450 ? 123.727 127.499 148.327 1.00 274.46 ? 1227 THR B CG2 1 
ATOM   5040 N  N   . CYS B 1 451 ? 123.699 128.786 144.607 1.00 292.54 ? 1228 CYS B N   1 
ATOM   5041 C  CA  . CYS B 1 451 ? 124.793 129.142 143.720 1.00 292.88 ? 1228 CYS B CA  1 
ATOM   5042 C  C   . CYS B 1 451 ? 125.079 130.630 143.854 1.00 292.94 ? 1228 CYS B C   1 
ATOM   5043 O  O   . CYS B 1 451 ? 124.159 131.422 144.090 1.00 292.81 ? 1228 CYS B O   1 
ATOM   5044 C  CB  . CYS B 1 451 ? 124.468 128.805 142.256 1.00 293.21 ? 1228 CYS B CB  1 
ATOM   5045 S  SG  . CYS B 1 451 ? 123.072 129.721 141.564 1.00 295.25 ? 1228 CYS B SG  1 
ATOM   5046 N  N   . PRO B 1 452 ? 126.350 131.040 143.715 1.00 282.88 ? 1229 PRO B N   1 
ATOM   5047 C  CA  . PRO B 1 452 ? 126.733 132.453 143.805 1.00 282.39 ? 1229 PRO B CA  1 
ATOM   5048 C  C   . PRO B 1 452 ? 126.114 133.302 142.699 1.00 282.13 ? 1229 PRO B C   1 
ATOM   5049 O  O   . PRO B 1 452 ? 126.415 133.069 141.529 1.00 282.35 ? 1229 PRO B O   1 
ATOM   5050 C  CB  . PRO B 1 452 ? 128.260 132.415 143.668 1.00 281.96 ? 1229 PRO B CB  1 
ATOM   5051 C  CG  . PRO B 1 452 ? 128.647 131.020 144.031 1.00 281.98 ? 1229 PRO B CG  1 
ATOM   5052 C  CD  . PRO B 1 452 ? 127.521 130.162 143.555 1.00 282.44 ? 1229 PRO B CD  1 
HETATM 5053 CA CA  . CA  C 2 .   ? 119.759 73.684  107.110 1.00 253.47 ? 1501 CA  A CA  1 
HETATM 5054 CA CA  . CA  D 2 .   ? 100.830 146.912 107.068 1.00 253.47 ? 1501 CA  B CA  1 
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