data_9GGM
# 
_entry.id   9GGM 
# 
_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   9GGM         pdb_00009ggm 10.2210/pdb9ggm/pdb 
WWPDB D_1292140728 ?            ?                   
EMDB  EMD-51337    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GGM 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-13 
_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 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of KBTBD4 P313PRR mutant-HDAC2 2:2 complex' 
_pdbx_database_related.db_id          EMD-51337 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alex.bullock@cmd.ox.ac.uk 
_pdbx_contact_author.name_first         Alex 
_pdbx_contact_author.name_last          Bullock 
_pdbx_contact_author.name_mi            N 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6757-0436 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, Z.'      1 0000-0003-4201-4649 
'Chi, G.'       2 0000-0001-9910-0965 
'Pike, A.C.W.'  3 0000-0001-9661-2607 
'Montes, B.'    4 0009-0003-3263-0883 
'Bullock, A.N.' 5 0000-0001-6757-0436 
# 
_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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3144 
_citation.page_last                 3144 
_citation.title                     
'Structural mimicry of UM171 and neomorphic cancer mutants co-opts E3 ligase KBTBD4 for HDAC1/2 recruitment.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58350-z 
_citation.pdbx_database_id_PubMed   40175372 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, Z.'         1  0000-0003-4201-4649 
primary 'Chi, G.'          2  0000-0001-9910-0965 
primary 'Balo, T.'         3  0009-0009-4013-8243 
primary 'Chen, X.'         4  0000-0003-0587-3444 
primary 'Montes, B.R.'     5  ?                   
primary 'Clifford, S.C.'   6  0000-0003-4893-2184 
primary 
;D'Angiolella, V.
;
7  0000-0001-8365-9094 
primary 'Szabo, T.'        8  0000-0003-0700-4680 
primary 'Kiss, A.'         9  ?                   
primary 'Novak, T.'        10 ?                   
primary 'Herner, A.'       11 0009-0005-1406-3971 
primary 'Kotschy, A.'      12 ?                   
primary 'Bullock, A.N.'    13 0000-0001-6757-0436 
# 
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 'Isoform 1 of Kelch repeat and BTB domain-containing protein 4' 58463.059 2 ?                
'Indel mutation R313PRR' ? 'Contains medulloblastoma cancer indel mutation R313PRR' 
2 polymer     man 'Histone deacetylase 2'                                         55443.156 2 3.5.1.98,3.5.1.- ? ? ? 
3 non-polymer syn 'ZINC ION'                                                      65.409    2 ?                ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'BTB and kelch domain-containing protein 4' 
2 'HD2,Protein deacylase HDAC2'               
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MESPEEPGASMDENYFVNYTFKDRSHSGRVAQGIMKLCLEEELFADVTISVEGREFQLHRLVLSAQSCFFRSMFTSNLKE
AHNRVIVLQDVSESVFQLLVDYIYHGTVKLRAEELQEIYEVSDMYQLTSLFEECSRFLARTVQVGNCLQVMWLADRHSDP
ELYTAAKHCAKTHLAQLQNTEEFLHLPHRLLTDIISDGVPCSQNPTEAIEAWINFNKEEREAFAESLRTSLKEIGENVHI
YLIGKESSRTHSLAVSLHCAEDDSISVSGQNSLCHQITAACKHGGDLYVVGGSIPRPRRMWKCNNATVDWEWCAPLPRDR
LQHTLVSVPGKDAIYSLGGKTLQDTLSNAVIYYRVGDNVWTETTQLEVAVSGAAGANLNGIIYLLGGEENDLDFFTKPSR
LIQCFDTETDKCHVKPYVLPFAGRMHAAVHKDLVFIVAEGDSLVCYNPLLDSFTRLCLPEAWSSAPSLWKIASCNGSIYV
FRDRYKKGDANTYKLDPATSAVTVTRGIKVLLTNLQFVLA
;
;MESPEEPGASMDENYFVNYTFKDRSHSGRVAQGIMKLCLEEELFADVTISVEGREFQLHRLVLSAQSCFFRSMFTSNLKE
AHNRVIVLQDVSESVFQLLVDYIYHGTVKLRAEELQEIYEVSDMYQLTSLFEECSRFLARTVQVGNCLQVMWLADRHSDP
ELYTAAKHCAKTHLAQLQNTEEFLHLPHRLLTDIISDGVPCSQNPTEAIEAWINFNKEEREAFAESLRTSLKEIGENVHI
YLIGKESSRTHSLAVSLHCAEDDSISVSGQNSLCHQITAACKHGGDLYVVGGSIPRPRRMWKCNNATVDWEWCAPLPRDR
LQHTLVSVPGKDAIYSLGGKTLQDTLSNAVIYYRVGDNVWTETTQLEVAVSGAAGANLNGIIYLLGGEENDLDFFTKPSR
LIQCFDTETDKCHVKPYVLPFAGRMHAAVHKDLVFIVAEGDSLVCYNPLLDSFTRLCLPEAWSSAPSLWKIASCNGSIYV
FRDRYKKGDANTYKLDPATSAVTVTRGIKVLLTNLQFVLA
;
A,C ? 
2 'polypeptide(L)' no no 
;MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSI
RPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLA
ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ
IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVA
LDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGE
DPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT
KSEQLSNP
;
;MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSI
RPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLA
ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ
IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVA
LDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGE
DPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT
KSEQLSNP
;
D,B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        'ZINC ION' 
_pdbx_entity_nonpoly.comp_id     ZN 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLU n 
1 3   SER n 
1 4   PRO n 
1 5   GLU n 
1 6   GLU n 
1 7   PRO n 
1 8   GLY n 
1 9   ALA n 
1 10  SER n 
1 11  MET n 
1 12  ASP n 
1 13  GLU n 
1 14  ASN n 
1 15  TYR n 
1 16  PHE n 
1 17  VAL n 
1 18  ASN n 
1 19  TYR n 
1 20  THR n 
1 21  PHE n 
1 22  LYS n 
1 23  ASP n 
1 24  ARG n 
1 25  SER n 
1 26  HIS n 
1 27  SER n 
1 28  GLY n 
1 29  ARG n 
1 30  VAL n 
1 31  ALA n 
1 32  GLN n 
1 33  GLY n 
1 34  ILE n 
1 35  MET n 
1 36  LYS n 
1 37  LEU n 
1 38  CYS n 
1 39  LEU n 
1 40  GLU n 
1 41  GLU n 
1 42  GLU n 
1 43  LEU n 
1 44  PHE n 
1 45  ALA n 
1 46  ASP n 
1 47  VAL n 
1 48  THR n 
1 49  ILE n 
1 50  SER n 
1 51  VAL n 
1 52  GLU n 
1 53  GLY n 
1 54  ARG n 
1 55  GLU n 
1 56  PHE n 
1 57  GLN n 
1 58  LEU n 
1 59  HIS n 
1 60  ARG n 
1 61  LEU n 
1 62  VAL n 
1 63  LEU n 
1 64  SER n 
1 65  ALA n 
1 66  GLN n 
1 67  SER n 
1 68  CYS n 
1 69  PHE n 
1 70  PHE n 
1 71  ARG n 
1 72  SER n 
1 73  MET n 
1 74  PHE n 
1 75  THR n 
1 76  SER n 
1 77  ASN n 
1 78  LEU n 
1 79  LYS n 
1 80  GLU n 
1 81  ALA n 
1 82  HIS n 
1 83  ASN n 
1 84  ARG n 
1 85  VAL n 
1 86  ILE n 
1 87  VAL n 
1 88  LEU n 
1 89  GLN n 
1 90  ASP n 
1 91  VAL n 
1 92  SER n 
1 93  GLU n 
1 94  SER n 
1 95  VAL n 
1 96  PHE n 
1 97  GLN n 
1 98  LEU n 
1 99  LEU n 
1 100 VAL n 
1 101 ASP n 
1 102 TYR n 
1 103 ILE n 
1 104 TYR n 
1 105 HIS n 
1 106 GLY n 
1 107 THR n 
1 108 VAL n 
1 109 LYS n 
1 110 LEU n 
1 111 ARG n 
1 112 ALA n 
1 113 GLU n 
1 114 GLU n 
1 115 LEU n 
1 116 GLN n 
1 117 GLU n 
1 118 ILE n 
1 119 TYR n 
1 120 GLU n 
1 121 VAL n 
1 122 SER n 
1 123 ASP n 
1 124 MET n 
1 125 TYR n 
1 126 GLN n 
1 127 LEU n 
1 128 THR n 
1 129 SER n 
1 130 LEU n 
1 131 PHE n 
1 132 GLU n 
1 133 GLU n 
1 134 CYS n 
1 135 SER n 
1 136 ARG n 
1 137 PHE n 
1 138 LEU n 
1 139 ALA n 
1 140 ARG n 
1 141 THR n 
1 142 VAL n 
1 143 GLN n 
1 144 VAL n 
1 145 GLY n 
1 146 ASN n 
1 147 CYS n 
1 148 LEU n 
1 149 GLN n 
1 150 VAL n 
1 151 MET n 
1 152 TRP n 
1 153 LEU n 
1 154 ALA n 
1 155 ASP n 
1 156 ARG n 
1 157 HIS n 
1 158 SER n 
1 159 ASP n 
1 160 PRO n 
1 161 GLU n 
1 162 LEU n 
1 163 TYR n 
1 164 THR n 
1 165 ALA n 
1 166 ALA n 
1 167 LYS n 
1 168 HIS n 
1 169 CYS n 
1 170 ALA n 
1 171 LYS n 
1 172 THR n 
1 173 HIS n 
1 174 LEU n 
1 175 ALA n 
1 176 GLN n 
1 177 LEU n 
1 178 GLN n 
1 179 ASN n 
1 180 THR n 
1 181 GLU n 
1 182 GLU n 
1 183 PHE n 
1 184 LEU n 
1 185 HIS n 
1 186 LEU n 
1 187 PRO n 
1 188 HIS n 
1 189 ARG n 
1 190 LEU n 
1 191 LEU n 
1 192 THR n 
1 193 ASP n 
1 194 ILE n 
1 195 ILE n 
1 196 SER n 
1 197 ASP n 
1 198 GLY n 
1 199 VAL n 
1 200 PRO n 
1 201 CYS n 
1 202 SER n 
1 203 GLN n 
1 204 ASN n 
1 205 PRO n 
1 206 THR n 
1 207 GLU n 
1 208 ALA n 
1 209 ILE n 
1 210 GLU n 
1 211 ALA n 
1 212 TRP n 
1 213 ILE n 
1 214 ASN n 
1 215 PHE n 
1 216 ASN n 
1 217 LYS n 
1 218 GLU n 
1 219 GLU n 
1 220 ARG n 
1 221 GLU n 
1 222 ALA n 
1 223 PHE n 
1 224 ALA n 
1 225 GLU n 
1 226 SER n 
1 227 LEU n 
1 228 ARG n 
1 229 THR n 
1 230 SER n 
1 231 LEU n 
1 232 LYS n 
1 233 GLU n 
1 234 ILE n 
1 235 GLY n 
1 236 GLU n 
1 237 ASN n 
1 238 VAL n 
1 239 HIS n 
1 240 ILE n 
1 241 TYR n 
1 242 LEU n 
1 243 ILE n 
1 244 GLY n 
1 245 LYS n 
1 246 GLU n 
1 247 SER n 
1 248 SER n 
1 249 ARG n 
1 250 THR n 
1 251 HIS n 
1 252 SER n 
1 253 LEU n 
1 254 ALA n 
1 255 VAL n 
1 256 SER n 
1 257 LEU n 
1 258 HIS n 
1 259 CYS n 
1 260 ALA n 
1 261 GLU n 
1 262 ASP n 
1 263 ASP n 
1 264 SER n 
1 265 ILE n 
1 266 SER n 
1 267 VAL n 
1 268 SER n 
1 269 GLY n 
1 270 GLN n 
1 271 ASN n 
1 272 SER n 
1 273 LEU n 
1 274 CYS n 
1 275 HIS n 
1 276 GLN n 
1 277 ILE n 
1 278 THR n 
1 279 ALA n 
1 280 ALA n 
1 281 CYS n 
1 282 LYS n 
1 283 HIS n 
1 284 GLY n 
1 285 GLY n 
1 286 ASP n 
1 287 LEU n 
1 288 TYR n 
1 289 VAL n 
1 290 VAL n 
1 291 GLY n 
1 292 GLY n 
1 293 SER n 
1 294 ILE n 
1 295 PRO n 
1 296 ARG n 
1 297 PRO n 
1 298 ARG n 
1 299 ARG n 
1 300 MET n 
1 301 TRP n 
1 302 LYS n 
1 303 CYS n 
1 304 ASN n 
1 305 ASN n 
1 306 ALA n 
1 307 THR n 
1 308 VAL n 
1 309 ASP n 
1 310 TRP n 
1 311 GLU n 
1 312 TRP n 
1 313 CYS n 
1 314 ALA n 
1 315 PRO n 
1 316 LEU n 
1 317 PRO n 
1 318 ARG n 
1 319 ASP n 
1 320 ARG n 
1 321 LEU n 
1 322 GLN n 
1 323 HIS n 
1 324 THR n 
1 325 LEU n 
1 326 VAL n 
1 327 SER n 
1 328 VAL n 
1 329 PRO n 
1 330 GLY n 
1 331 LYS n 
1 332 ASP n 
1 333 ALA n 
1 334 ILE n 
1 335 TYR n 
1 336 SER n 
1 337 LEU n 
1 338 GLY n 
1 339 GLY n 
1 340 LYS n 
1 341 THR n 
1 342 LEU n 
1 343 GLN n 
1 344 ASP n 
1 345 THR n 
1 346 LEU n 
1 347 SER n 
1 348 ASN n 
1 349 ALA n 
1 350 VAL n 
1 351 ILE n 
1 352 TYR n 
1 353 TYR n 
1 354 ARG n 
1 355 VAL n 
1 356 GLY n 
1 357 ASP n 
1 358 ASN n 
1 359 VAL n 
1 360 TRP n 
1 361 THR n 
1 362 GLU n 
1 363 THR n 
1 364 THR n 
1 365 GLN n 
1 366 LEU n 
1 367 GLU n 
1 368 VAL n 
1 369 ALA n 
1 370 VAL n 
1 371 SER n 
1 372 GLY n 
1 373 ALA n 
1 374 ALA n 
1 375 GLY n 
1 376 ALA n 
1 377 ASN n 
1 378 LEU n 
1 379 ASN n 
1 380 GLY n 
1 381 ILE n 
1 382 ILE n 
1 383 TYR n 
1 384 LEU n 
1 385 LEU n 
1 386 GLY n 
1 387 GLY n 
1 388 GLU n 
1 389 GLU n 
1 390 ASN n 
1 391 ASP n 
1 392 LEU n 
1 393 ASP n 
1 394 PHE n 
1 395 PHE n 
1 396 THR n 
1 397 LYS n 
1 398 PRO n 
1 399 SER n 
1 400 ARG n 
1 401 LEU n 
1 402 ILE n 
1 403 GLN n 
1 404 CYS n 
1 405 PHE n 
1 406 ASP n 
1 407 THR n 
1 408 GLU n 
1 409 THR n 
1 410 ASP n 
1 411 LYS n 
1 412 CYS n 
1 413 HIS n 
1 414 VAL n 
1 415 LYS n 
1 416 PRO n 
1 417 TYR n 
1 418 VAL n 
1 419 LEU n 
1 420 PRO n 
1 421 PHE n 
1 422 ALA n 
1 423 GLY n 
1 424 ARG n 
1 425 MET n 
1 426 HIS n 
1 427 ALA n 
1 428 ALA n 
1 429 VAL n 
1 430 HIS n 
1 431 LYS n 
1 432 ASP n 
1 433 LEU n 
1 434 VAL n 
1 435 PHE n 
1 436 ILE n 
1 437 VAL n 
1 438 ALA n 
1 439 GLU n 
1 440 GLY n 
1 441 ASP n 
1 442 SER n 
1 443 LEU n 
1 444 VAL n 
1 445 CYS n 
1 446 TYR n 
1 447 ASN n 
1 448 PRO n 
1 449 LEU n 
1 450 LEU n 
1 451 ASP n 
1 452 SER n 
1 453 PHE n 
1 454 THR n 
1 455 ARG n 
1 456 LEU n 
1 457 CYS n 
1 458 LEU n 
1 459 PRO n 
1 460 GLU n 
1 461 ALA n 
1 462 TRP n 
1 463 SER n 
1 464 SER n 
1 465 ALA n 
1 466 PRO n 
1 467 SER n 
1 468 LEU n 
1 469 TRP n 
1 470 LYS n 
1 471 ILE n 
1 472 ALA n 
1 473 SER n 
1 474 CYS n 
1 475 ASN n 
1 476 GLY n 
1 477 SER n 
1 478 ILE n 
1 479 TYR n 
1 480 VAL n 
1 481 PHE n 
1 482 ARG n 
1 483 ASP n 
1 484 ARG n 
1 485 TYR n 
1 486 LYS n 
1 487 LYS n 
1 488 GLY n 
1 489 ASP n 
1 490 ALA n 
1 491 ASN n 
1 492 THR n 
1 493 TYR n 
1 494 LYS n 
1 495 LEU n 
1 496 ASP n 
1 497 PRO n 
1 498 ALA n 
1 499 THR n 
1 500 SER n 
1 501 ALA n 
1 502 VAL n 
1 503 THR n 
1 504 VAL n 
1 505 THR n 
1 506 ARG n 
1 507 GLY n 
1 508 ILE n 
1 509 LYS n 
1 510 VAL n 
1 511 LEU n 
1 512 LEU n 
1 513 THR n 
1 514 ASN n 
1 515 LEU n 
1 516 GLN n 
1 517 PHE n 
1 518 VAL n 
1 519 LEU n 
1 520 ALA n 
2 1   MET n 
2 2   ALA n 
2 3   TYR n 
2 4   SER n 
2 5   GLN n 
2 6   GLY n 
2 7   GLY n 
2 8   GLY n 
2 9   LYS n 
2 10  LYS n 
2 11  LYS n 
2 12  VAL n 
2 13  CYS n 
2 14  TYR n 
2 15  TYR n 
2 16  TYR n 
2 17  ASP n 
2 18  GLY n 
2 19  ASP n 
2 20  ILE n 
2 21  GLY n 
2 22  ASN n 
2 23  TYR n 
2 24  TYR n 
2 25  TYR n 
2 26  GLY n 
2 27  GLN n 
2 28  GLY n 
2 29  HIS n 
2 30  PRO n 
2 31  MET n 
2 32  LYS n 
2 33  PRO n 
2 34  HIS n 
2 35  ARG n 
2 36  ILE n 
2 37  ARG n 
2 38  MET n 
2 39  THR n 
2 40  HIS n 
2 41  ASN n 
2 42  LEU n 
2 43  LEU n 
2 44  LEU n 
2 45  ASN n 
2 46  TYR n 
2 47  GLY n 
2 48  LEU n 
2 49  TYR n 
2 50  ARG n 
2 51  LYS n 
2 52  MET n 
2 53  GLU n 
2 54  ILE n 
2 55  TYR n 
2 56  ARG n 
2 57  PRO n 
2 58  HIS n 
2 59  LYS n 
2 60  ALA n 
2 61  THR n 
2 62  ALA n 
2 63  GLU n 
2 64  GLU n 
2 65  MET n 
2 66  THR n 
2 67  LYS n 
2 68  TYR n 
2 69  HIS n 
2 70  SER n 
2 71  ASP n 
2 72  GLU n 
2 73  TYR n 
2 74  ILE n 
2 75  LYS n 
2 76  PHE n 
2 77  LEU n 
2 78  ARG n 
2 79  SER n 
2 80  ILE n 
2 81  ARG n 
2 82  PRO n 
2 83  ASP n 
2 84  ASN n 
2 85  MET n 
2 86  SER n 
2 87  GLU n 
2 88  TYR n 
2 89  SER n 
2 90  LYS n 
2 91  GLN n 
2 92  MET n 
2 93  GLN n 
2 94  ARG n 
2 95  PHE n 
2 96  ASN n 
2 97  VAL n 
2 98  GLY n 
2 99  GLU n 
2 100 ASP n 
2 101 CYS n 
2 102 PRO n 
2 103 VAL n 
2 104 PHE n 
2 105 ASP n 
2 106 GLY n 
2 107 LEU n 
2 108 PHE n 
2 109 GLU n 
2 110 PHE n 
2 111 CYS n 
2 112 GLN n 
2 113 LEU n 
2 114 SER n 
2 115 THR n 
2 116 GLY n 
2 117 GLY n 
2 118 SER n 
2 119 VAL n 
2 120 ALA n 
2 121 GLY n 
2 122 ALA n 
2 123 VAL n 
2 124 LYS n 
2 125 LEU n 
2 126 ASN n 
2 127 ARG n 
2 128 GLN n 
2 129 GLN n 
2 130 THR n 
2 131 ASP n 
2 132 MET n 
2 133 ALA n 
2 134 VAL n 
2 135 ASN n 
2 136 TRP n 
2 137 ALA n 
2 138 GLY n 
2 139 GLY n 
2 140 LEU n 
2 141 HIS n 
2 142 HIS n 
2 143 ALA n 
2 144 LYS n 
2 145 LYS n 
2 146 SER n 
2 147 GLU n 
2 148 ALA n 
2 149 SER n 
2 150 GLY n 
2 151 PHE n 
2 152 CYS n 
2 153 TYR n 
2 154 VAL n 
2 155 ASN n 
2 156 ASP n 
2 157 ILE n 
2 158 VAL n 
2 159 LEU n 
2 160 ALA n 
2 161 ILE n 
2 162 LEU n 
2 163 GLU n 
2 164 LEU n 
2 165 LEU n 
2 166 LYS n 
2 167 TYR n 
2 168 HIS n 
2 169 GLN n 
2 170 ARG n 
2 171 VAL n 
2 172 LEU n 
2 173 TYR n 
2 174 ILE n 
2 175 ASP n 
2 176 ILE n 
2 177 ASP n 
2 178 ILE n 
2 179 HIS n 
2 180 HIS n 
2 181 GLY n 
2 182 ASP n 
2 183 GLY n 
2 184 VAL n 
2 185 GLU n 
2 186 GLU n 
2 187 ALA n 
2 188 PHE n 
2 189 TYR n 
2 190 THR n 
2 191 THR n 
2 192 ASP n 
2 193 ARG n 
2 194 VAL n 
2 195 MET n 
2 196 THR n 
2 197 VAL n 
2 198 SER n 
2 199 PHE n 
2 200 HIS n 
2 201 LYS n 
2 202 TYR n 
2 203 GLY n 
2 204 GLU n 
2 205 TYR n 
2 206 PHE n 
2 207 PRO n 
2 208 GLY n 
2 209 THR n 
2 210 GLY n 
2 211 ASP n 
2 212 LEU n 
2 213 ARG n 
2 214 ASP n 
2 215 ILE n 
2 216 GLY n 
2 217 ALA n 
2 218 GLY n 
2 219 LYS n 
2 220 GLY n 
2 221 LYS n 
2 222 TYR n 
2 223 TYR n 
2 224 ALA n 
2 225 VAL n 
2 226 ASN n 
2 227 PHE n 
2 228 PRO n 
2 229 MET n 
2 230 ARG n 
2 231 ASP n 
2 232 GLY n 
2 233 ILE n 
2 234 ASP n 
2 235 ASP n 
2 236 GLU n 
2 237 SER n 
2 238 TYR n 
2 239 GLY n 
2 240 GLN n 
2 241 ILE n 
2 242 PHE n 
2 243 LYS n 
2 244 PRO n 
2 245 ILE n 
2 246 ILE n 
2 247 SER n 
2 248 LYS n 
2 249 VAL n 
2 250 MET n 
2 251 GLU n 
2 252 MET n 
2 253 TYR n 
2 254 GLN n 
2 255 PRO n 
2 256 SER n 
2 257 ALA n 
2 258 VAL n 
2 259 VAL n 
2 260 LEU n 
2 261 GLN n 
2 262 CYS n 
2 263 GLY n 
2 264 ALA n 
2 265 ASP n 
2 266 SER n 
2 267 LEU n 
2 268 SER n 
2 269 GLY n 
2 270 ASP n 
2 271 ARG n 
2 272 LEU n 
2 273 GLY n 
2 274 CYS n 
2 275 PHE n 
2 276 ASN n 
2 277 LEU n 
2 278 THR n 
2 279 VAL n 
2 280 LYS n 
2 281 GLY n 
2 282 HIS n 
2 283 ALA n 
2 284 LYS n 
2 285 CYS n 
2 286 VAL n 
2 287 GLU n 
2 288 VAL n 
2 289 VAL n 
2 290 LYS n 
2 291 THR n 
2 292 PHE n 
2 293 ASN n 
2 294 LEU n 
2 295 PRO n 
2 296 LEU n 
2 297 LEU n 
2 298 MET n 
2 299 LEU n 
2 300 GLY n 
2 301 GLY n 
2 302 GLY n 
2 303 GLY n 
2 304 TYR n 
2 305 THR n 
2 306 ILE n 
2 307 ARG n 
2 308 ASN n 
2 309 VAL n 
2 310 ALA n 
2 311 ARG n 
2 312 CYS n 
2 313 TRP n 
2 314 THR n 
2 315 TYR n 
2 316 GLU n 
2 317 THR n 
2 318 ALA n 
2 319 VAL n 
2 320 ALA n 
2 321 LEU n 
2 322 ASP n 
2 323 CYS n 
2 324 GLU n 
2 325 ILE n 
2 326 PRO n 
2 327 ASN n 
2 328 GLU n 
2 329 LEU n 
2 330 PRO n 
2 331 TYR n 
2 332 ASN n 
2 333 ASP n 
2 334 TYR n 
2 335 PHE n 
2 336 GLU n 
2 337 TYR n 
2 338 PHE n 
2 339 GLY n 
2 340 PRO n 
2 341 ASP n 
2 342 PHE n 
2 343 LYS n 
2 344 LEU n 
2 345 HIS n 
2 346 ILE n 
2 347 SER n 
2 348 PRO n 
2 349 SER n 
2 350 ASN n 
2 351 MET n 
2 352 THR n 
2 353 ASN n 
2 354 GLN n 
2 355 ASN n 
2 356 THR n 
2 357 PRO n 
2 358 GLU n 
2 359 TYR n 
2 360 MET n 
2 361 GLU n 
2 362 LYS n 
2 363 ILE n 
2 364 LYS n 
2 365 GLN n 
2 366 ARG n 
2 367 LEU n 
2 368 PHE n 
2 369 GLU n 
2 370 ASN n 
2 371 LEU n 
2 372 ARG n 
2 373 MET n 
2 374 LEU n 
2 375 PRO n 
2 376 HIS n 
2 377 ALA n 
2 378 PRO n 
2 379 GLY n 
2 380 VAL n 
2 381 GLN n 
2 382 MET n 
2 383 GLN n 
2 384 ALA n 
2 385 ILE n 
2 386 PRO n 
2 387 GLU n 
2 388 ASP n 
2 389 ALA n 
2 390 VAL n 
2 391 HIS n 
2 392 GLU n 
2 393 ASP n 
2 394 SER n 
2 395 GLY n 
2 396 ASP n 
2 397 GLU n 
2 398 ASP n 
2 399 GLY n 
2 400 GLU n 
2 401 ASP n 
2 402 PRO n 
2 403 ASP n 
2 404 LYS n 
2 405 ARG n 
2 406 ILE n 
2 407 SER n 
2 408 ILE n 
2 409 ARG n 
2 410 ALA n 
2 411 SER n 
2 412 ASP n 
2 413 LYS n 
2 414 ARG n 
2 415 ILE n 
2 416 ALA n 
2 417 CYS n 
2 418 ASP n 
2 419 GLU n 
2 420 GLU n 
2 421 PHE n 
2 422 SER n 
2 423 ASP n 
2 424 SER n 
2 425 GLU n 
2 426 ASP n 
2 427 GLU n 
2 428 GLY n 
2 429 GLU n 
2 430 GLY n 
2 431 GLY n 
2 432 ARG n 
2 433 ARG n 
2 434 ASN n 
2 435 VAL n 
2 436 ALA n 
2 437 ASP n 
2 438 HIS n 
2 439 LYS n 
2 440 LYS n 
2 441 GLY n 
2 442 ALA n 
2 443 LYS n 
2 444 LYS n 
2 445 ALA n 
2 446 ARG n 
2 447 ILE n 
2 448 GLU n 
2 449 GLU n 
2 450 ASP n 
2 451 LYS n 
2 452 LYS n 
2 453 GLU n 
2 454 THR n 
2 455 GLU n 
2 456 ASP n 
2 457 LYS n 
2 458 LYS n 
2 459 THR n 
2 460 ASP n 
2 461 VAL n 
2 462 LYS n 
2 463 GLU n 
2 464 GLU n 
2 465 ASP n 
2 466 LYS n 
2 467 SER n 
2 468 LYS n 
2 469 ASP n 
2 470 ASN n 
2 471 SER n 
2 472 GLY n 
2 473 GLU n 
2 474 LYS n 
2 475 THR n 
2 476 ASP n 
2 477 THR n 
2 478 LYS n 
2 479 GLY n 
2 480 THR n 
2 481 LYS n 
2 482 SER n 
2 483 GLU n 
2 484 GLN n 
2 485 LEU n 
2 486 SER n 
2 487 ASN n 
2 488 PRO n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 520 human ? 'KBTBD4, BKLHD4' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? Expi293F ? ? ?        ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 488 human ? HDAC2            ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Homo sapiens' 
9606 ? ? ? ? ? ? ? ? ?        ? ? Expi293F ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   17  ?   ?   ?   A . n 
A 1 2   GLU 2   18  ?   ?   ?   A . n 
A 1 3   SER 3   19  ?   ?   ?   A . n 
A 1 4   PRO 4   20  ?   ?   ?   A . n 
A 1 5   GLU 5   21  ?   ?   ?   A . n 
A 1 6   GLU 6   22  ?   ?   ?   A . n 
A 1 7   PRO 7   23  ?   ?   ?   A . n 
A 1 8   GLY 8   24  ?   ?   ?   A . n 
A 1 9   ALA 9   25  ?   ?   ?   A . n 
A 1 10  SER 10  26  ?   ?   ?   A . n 
A 1 11  MET 11  27  ?   ?   ?   A . n 
A 1 12  ASP 12  28  ?   ?   ?   A . n 
A 1 13  GLU 13  29  ?   ?   ?   A . n 
A 1 14  ASN 14  30  ?   ?   ?   A . n 
A 1 15  TYR 15  31  ?   ?   ?   A . n 
A 1 16  PHE 16  32  32  PHE PHE A . n 
A 1 17  VAL 17  33  33  VAL VAL A . n 
A 1 18  ASN 18  34  34  ASN ASN A . n 
A 1 19  TYR 19  35  35  TYR TYR A . n 
A 1 20  THR 20  36  36  THR THR A . n 
A 1 21  PHE 21  37  37  PHE PHE A . n 
A 1 22  LYS 22  38  38  LYS LYS A . n 
A 1 23  ASP 23  39  39  ASP ASP A . n 
A 1 24  ARG 24  40  40  ARG ARG A . n 
A 1 25  SER 25  41  41  SER SER A . n 
A 1 26  HIS 26  42  42  HIS HIS A . n 
A 1 27  SER 27  43  43  SER SER A . n 
A 1 28  GLY 28  44  44  GLY GLY A . n 
A 1 29  ARG 29  45  45  ARG ARG A . n 
A 1 30  VAL 30  46  46  VAL VAL A . n 
A 1 31  ALA 31  47  47  ALA ALA A . n 
A 1 32  GLN 32  48  48  GLN GLN A . n 
A 1 33  GLY 33  49  49  GLY GLY A . n 
A 1 34  ILE 34  50  50  ILE ILE A . n 
A 1 35  MET 35  51  51  MET MET A . n 
A 1 36  LYS 36  52  52  LYS LYS A . n 
A 1 37  LEU 37  53  53  LEU LEU A . n 
A 1 38  CYS 38  54  54  CYS CYS A . n 
A 1 39  LEU 39  55  55  LEU LEU A . n 
A 1 40  GLU 40  56  56  GLU GLU A . n 
A 1 41  GLU 41  57  57  GLU GLU A . n 
A 1 42  GLU 42  58  ?   ?   ?   A . n 
A 1 43  LEU 43  59  ?   ?   ?   A . n 
A 1 44  PHE 44  60  ?   ?   ?   A . n 
A 1 45  ALA 45  61  ?   ?   ?   A . n 
A 1 46  ASP 46  62  ?   ?   ?   A . n 
A 1 47  VAL 47  63  ?   ?   ?   A . n 
A 1 48  THR 48  64  ?   ?   ?   A . n 
A 1 49  ILE 49  65  ?   ?   ?   A . n 
A 1 50  SER 50  66  ?   ?   ?   A . n 
A 1 51  VAL 51  67  ?   ?   ?   A . n 
A 1 52  GLU 52  68  ?   ?   ?   A . n 
A 1 53  GLY 53  69  ?   ?   ?   A . n 
A 1 54  ARG 54  70  ?   ?   ?   A . n 
A 1 55  GLU 55  71  ?   ?   ?   A . n 
A 1 56  PHE 56  72  ?   ?   ?   A . n 
A 1 57  GLN 57  73  ?   ?   ?   A . n 
A 1 58  LEU 58  74  ?   ?   ?   A . n 
A 1 59  HIS 59  75  ?   ?   ?   A . n 
A 1 60  ARG 60  76  76  ARG ARG A . n 
A 1 61  LEU 61  77  77  LEU LEU A . n 
A 1 62  VAL 62  78  78  VAL VAL A . n 
A 1 63  LEU 63  79  79  LEU LEU A . n 
A 1 64  SER 64  80  80  SER SER A . n 
A 1 65  ALA 65  81  81  ALA ALA A . n 
A 1 66  GLN 66  82  82  GLN GLN A . n 
A 1 67  SER 67  83  83  SER SER A . n 
A 1 68  CYS 68  84  84  CYS CYS A . n 
A 1 69  PHE 69  85  85  PHE PHE A . n 
A 1 70  PHE 70  86  86  PHE PHE A . n 
A 1 71  ARG 71  87  87  ARG ARG A . n 
A 1 72  SER 72  88  88  SER SER A . n 
A 1 73  MET 73  89  89  MET MET A . n 
A 1 74  PHE 74  90  90  PHE PHE A . n 
A 1 75  THR 75  91  ?   ?   ?   A . n 
A 1 76  SER 76  92  ?   ?   ?   A . n 
A 1 77  ASN 77  93  ?   ?   ?   A . n 
A 1 78  LEU 78  94  ?   ?   ?   A . n 
A 1 79  LYS 79  95  ?   ?   ?   A . n 
A 1 80  GLU 80  96  ?   ?   ?   A . n 
A 1 81  ALA 81  97  ?   ?   ?   A . n 
A 1 82  HIS 82  98  ?   ?   ?   A . n 
A 1 83  ASN 83  99  ?   ?   ?   A . n 
A 1 84  ARG 84  100 ?   ?   ?   A . n 
A 1 85  VAL 85  101 ?   ?   ?   A . n 
A 1 86  ILE 86  102 ?   ?   ?   A . n 
A 1 87  VAL 87  103 ?   ?   ?   A . n 
A 1 88  LEU 88  104 ?   ?   ?   A . n 
A 1 89  GLN 89  105 105 GLN GLN A . n 
A 1 90  ASP 90  106 106 ASP ASP A . n 
A 1 91  VAL 91  107 107 VAL VAL A . n 
A 1 92  SER 92  108 108 SER SER A . n 
A 1 93  GLU 93  109 109 GLU GLU A . n 
A 1 94  SER 94  110 110 SER SER A . n 
A 1 95  VAL 95  111 111 VAL VAL A . n 
A 1 96  PHE 96  112 112 PHE PHE A . n 
A 1 97  GLN 97  113 113 GLN GLN A . n 
A 1 98  LEU 98  114 114 LEU LEU A . n 
A 1 99  LEU 99  115 115 LEU LEU A . n 
A 1 100 VAL 100 116 116 VAL VAL A . n 
A 1 101 ASP 101 117 117 ASP ASP A . n 
A 1 102 TYR 102 118 118 TYR TYR A . n 
A 1 103 ILE 103 119 119 ILE ILE A . n 
A 1 104 TYR 104 120 120 TYR TYR A . n 
A 1 105 HIS 105 121 121 HIS HIS A . n 
A 1 106 GLY 106 122 122 GLY GLY A . n 
A 1 107 THR 107 123 123 THR THR A . n 
A 1 108 VAL 108 124 124 VAL VAL A . n 
A 1 109 LYS 109 125 125 LYS LYS A . n 
A 1 110 LEU 110 126 126 LEU LEU A . n 
A 1 111 ARG 111 127 127 ARG ARG A . n 
A 1 112 ALA 112 128 128 ALA ALA A . n 
A 1 113 GLU 113 129 129 GLU GLU A . n 
A 1 114 GLU 114 130 130 GLU GLU A . n 
A 1 115 LEU 115 131 131 LEU LEU A . n 
A 1 116 GLN 116 132 132 GLN GLN A . n 
A 1 117 GLU 117 133 133 GLU GLU A . n 
A 1 118 ILE 118 134 134 ILE ILE A . n 
A 1 119 TYR 119 135 135 TYR TYR A . n 
A 1 120 GLU 120 136 136 GLU GLU A . n 
A 1 121 VAL 121 137 137 VAL VAL A . n 
A 1 122 SER 122 138 138 SER SER A . n 
A 1 123 ASP 123 139 139 ASP ASP A . n 
A 1 124 MET 124 140 140 MET MET A . n 
A 1 125 TYR 125 141 141 TYR TYR A . n 
A 1 126 GLN 126 142 142 GLN GLN A . n 
A 1 127 LEU 127 143 143 LEU LEU A . n 
A 1 128 THR 128 144 144 THR THR A . n 
A 1 129 SER 129 145 145 SER SER A . n 
A 1 130 LEU 130 146 146 LEU LEU A . n 
A 1 131 PHE 131 147 147 PHE PHE A . n 
A 1 132 GLU 132 148 148 GLU GLU A . n 
A 1 133 GLU 133 149 149 GLU GLU A . n 
A 1 134 CYS 134 150 150 CYS CYS A . n 
A 1 135 SER 135 151 151 SER SER A . n 
A 1 136 ARG 136 152 152 ARG ARG A . n 
A 1 137 PHE 137 153 153 PHE PHE A . n 
A 1 138 LEU 138 154 154 LEU LEU A . n 
A 1 139 ALA 139 155 155 ALA ALA A . n 
A 1 140 ARG 140 156 ?   ?   ?   A . n 
A 1 141 THR 141 157 ?   ?   ?   A . n 
A 1 142 VAL 142 158 ?   ?   ?   A . n 
A 1 143 GLN 143 159 ?   ?   ?   A . n 
A 1 144 VAL 144 160 ?   ?   ?   A . n 
A 1 145 GLY 145 161 161 GLY GLY A . n 
A 1 146 ASN 146 162 162 ASN ASN A . n 
A 1 147 CYS 147 163 163 CYS CYS A . n 
A 1 148 LEU 148 164 164 LEU LEU A . n 
A 1 149 GLN 149 165 165 GLN GLN A . n 
A 1 150 VAL 150 166 166 VAL VAL A . n 
A 1 151 MET 151 167 167 MET MET A . n 
A 1 152 TRP 152 168 168 TRP TRP A . n 
A 1 153 LEU 153 169 169 LEU LEU A . n 
A 1 154 ALA 154 170 170 ALA ALA A . n 
A 1 155 ASP 155 171 171 ASP ASP A . n 
A 1 156 ARG 156 172 172 ARG ARG A . n 
A 1 157 HIS 157 173 173 HIS HIS A . n 
A 1 158 SER 158 174 174 SER SER A . n 
A 1 159 ASP 159 175 175 ASP ASP A . n 
A 1 160 PRO 160 176 176 PRO PRO A . n 
A 1 161 GLU 161 177 177 GLU GLU A . n 
A 1 162 LEU 162 178 178 LEU LEU A . n 
A 1 163 TYR 163 179 179 TYR TYR A . n 
A 1 164 THR 164 180 180 THR THR A . n 
A 1 165 ALA 165 181 181 ALA ALA A . n 
A 1 166 ALA 166 182 182 ALA ALA A . n 
A 1 167 LYS 167 183 183 LYS LYS A . n 
A 1 168 HIS 168 184 184 HIS HIS A . n 
A 1 169 CYS 169 185 185 CYS CYS A . n 
A 1 170 ALA 170 186 186 ALA ALA A . n 
A 1 171 LYS 171 187 187 LYS LYS A . n 
A 1 172 THR 172 188 188 THR THR A . n 
A 1 173 HIS 173 189 189 HIS HIS A . n 
A 1 174 LEU 174 190 190 LEU LEU A . n 
A 1 175 ALA 175 191 191 ALA ALA A . n 
A 1 176 GLN 176 192 192 GLN GLN A . n 
A 1 177 LEU 177 193 193 LEU LEU A . n 
A 1 178 GLN 178 194 194 GLN GLN A . n 
A 1 179 ASN 179 195 ?   ?   ?   A . n 
A 1 180 THR 180 196 ?   ?   ?   A . n 
A 1 181 GLU 181 197 ?   ?   ?   A . n 
A 1 182 GLU 182 198 ?   ?   ?   A . n 
A 1 183 PHE 183 199 ?   ?   ?   A . n 
A 1 184 LEU 184 200 ?   ?   ?   A . n 
A 1 185 HIS 185 201 ?   ?   ?   A . n 
A 1 186 LEU 186 202 ?   ?   ?   A . n 
A 1 187 PRO 187 203 ?   ?   ?   A . n 
A 1 188 HIS 188 204 204 HIS HIS A . n 
A 1 189 ARG 189 205 205 ARG ARG A . n 
A 1 190 LEU 190 206 206 LEU LEU A . n 
A 1 191 LEU 191 207 207 LEU LEU A . n 
A 1 192 THR 192 208 208 THR THR A . n 
A 1 193 ASP 193 209 209 ASP ASP A . n 
A 1 194 ILE 194 210 210 ILE ILE A . n 
A 1 195 ILE 195 211 211 ILE ILE A . n 
A 1 196 SER 196 212 212 SER SER A . n 
A 1 197 ASP 197 213 213 ASP ASP A . n 
A 1 198 GLY 198 214 214 GLY GLY A . n 
A 1 199 VAL 199 215 215 VAL VAL A . n 
A 1 200 PRO 200 216 ?   ?   ?   A . n 
A 1 201 CYS 201 217 ?   ?   ?   A . n 
A 1 202 SER 202 218 ?   ?   ?   A . n 
A 1 203 GLN 203 219 219 GLN GLN A . n 
A 1 204 ASN 204 220 220 ASN ASN A . n 
A 1 205 PRO 205 221 221 PRO PRO A . n 
A 1 206 THR 206 222 222 THR THR A . n 
A 1 207 GLU 207 223 223 GLU GLU A . n 
A 1 208 ALA 208 224 224 ALA ALA A . n 
A 1 209 ILE 209 225 225 ILE ILE A . n 
A 1 210 GLU 210 226 226 GLU GLU A . n 
A 1 211 ALA 211 227 227 ALA ALA A . n 
A 1 212 TRP 212 228 ?   ?   ?   A . n 
A 1 213 ILE 213 229 ?   ?   ?   A . n 
A 1 214 ASN 214 230 ?   ?   ?   A . n 
A 1 215 PHE 215 231 ?   ?   ?   A . n 
A 1 216 ASN 216 232 ?   ?   ?   A . n 
A 1 217 LYS 217 233 ?   ?   ?   A . n 
A 1 218 GLU 218 234 ?   ?   ?   A . n 
A 1 219 GLU 219 235 ?   ?   ?   A . n 
A 1 220 ARG 220 236 ?   ?   ?   A . n 
A 1 221 GLU 221 237 ?   ?   ?   A . n 
A 1 222 ALA 222 238 ?   ?   ?   A . n 
A 1 223 PHE 223 239 ?   ?   ?   A . n 
A 1 224 ALA 224 240 ?   ?   ?   A . n 
A 1 225 GLU 225 241 ?   ?   ?   A . n 
A 1 226 SER 226 242 ?   ?   ?   A . n 
A 1 227 LEU 227 243 243 LEU LEU A . n 
A 1 228 ARG 228 244 244 ARG ARG A . n 
A 1 229 THR 229 245 245 THR THR A . n 
A 1 230 SER 230 246 246 SER SER A . n 
A 1 231 LEU 231 247 247 LEU LEU A . n 
A 1 232 LYS 232 248 248 LYS LYS A . n 
A 1 233 GLU 233 249 249 GLU GLU A . n 
A 1 234 ILE 234 250 250 ILE ILE A . n 
A 1 235 GLY 235 251 251 GLY GLY A . n 
A 1 236 GLU 236 252 252 GLU GLU A . n 
A 1 237 ASN 237 253 253 ASN ASN A . n 
A 1 238 VAL 238 254 254 VAL VAL A . n 
A 1 239 HIS 239 255 255 HIS HIS A . n 
A 1 240 ILE 240 256 256 ILE ILE A . n 
A 1 241 TYR 241 257 257 TYR TYR A . n 
A 1 242 LEU 242 258 258 LEU LEU A . n 
A 1 243 ILE 243 259 259 ILE ILE A . n 
A 1 244 GLY 244 260 260 GLY GLY A . n 
A 1 245 LYS 245 261 261 LYS LYS A . n 
A 1 246 GLU 246 262 ?   ?   ?   A . n 
A 1 247 SER 247 263 ?   ?   ?   A . n 
A 1 248 SER 248 264 ?   ?   ?   A . n 
A 1 249 ARG 249 265 ?   ?   ?   A . n 
A 1 250 THR 250 266 ?   ?   ?   A . n 
A 1 251 HIS 251 267 ?   ?   ?   A . n 
A 1 252 SER 252 268 268 SER SER A . n 
A 1 253 LEU 253 269 269 LEU LEU A . n 
A 1 254 ALA 254 270 270 ALA ALA A . n 
A 1 255 VAL 255 271 271 VAL VAL A . n 
A 1 256 SER 256 272 272 SER SER A . n 
A 1 257 LEU 257 273 273 LEU LEU A . n 
A 1 258 HIS 258 274 274 HIS HIS A . n 
A 1 259 CYS 259 275 275 CYS CYS A . n 
A 1 260 ALA 260 276 276 ALA ALA A . n 
A 1 261 GLU 261 277 277 GLU GLU A . n 
A 1 262 ASP 262 278 ?   ?   ?   A . n 
A 1 263 ASP 263 279 ?   ?   ?   A . n 
A 1 264 SER 264 280 280 SER SER A . n 
A 1 265 ILE 265 281 281 ILE ILE A . n 
A 1 266 SER 266 282 282 SER SER A . n 
A 1 267 VAL 267 283 283 VAL VAL A . n 
A 1 268 SER 268 284 284 SER SER A . n 
A 1 269 GLY 269 285 285 GLY GLY A . n 
A 1 270 GLN 270 286 286 GLN GLN A . n 
A 1 271 ASN 271 287 287 ASN ASN A . n 
A 1 272 SER 272 288 288 SER SER A . n 
A 1 273 LEU 273 289 289 LEU LEU A . n 
A 1 274 CYS 274 290 290 CYS CYS A . n 
A 1 275 HIS 275 291 291 HIS HIS A . n 
A 1 276 GLN 276 292 292 GLN GLN A . n 
A 1 277 ILE 277 293 293 ILE ILE A . n 
A 1 278 THR 278 294 294 THR THR A . n 
A 1 279 ALA 279 295 295 ALA ALA A . n 
A 1 280 ALA 280 296 296 ALA ALA A . n 
A 1 281 CYS 281 297 297 CYS CYS A . n 
A 1 282 LYS 282 298 298 LYS LYS A . n 
A 1 283 HIS 283 299 299 HIS HIS A . n 
A 1 284 GLY 284 300 300 GLY GLY A . n 
A 1 285 GLY 285 301 301 GLY GLY A . n 
A 1 286 ASP 286 302 302 ASP ASP A . n 
A 1 287 LEU 287 303 303 LEU LEU A . n 
A 1 288 TYR 288 304 304 TYR TYR A . n 
A 1 289 VAL 289 305 305 VAL VAL A . n 
A 1 290 VAL 290 306 306 VAL VAL A . n 
A 1 291 GLY 291 307 307 GLY GLY A . n 
A 1 292 GLY 292 308 308 GLY GLY A . n 
A 1 293 SER 293 309 309 SER SER A . n 
A 1 294 ILE 294 310 310 ILE ILE A . n 
A 1 295 PRO 295 311 311 PRO PRO A . n 
A 1 296 ARG 296 312 312 ARG ARG A . n 
A 1 297 PRO 297 313 313 PRO PRO A . n 
A 1 298 ARG 298 314 314 ARG ARG A . n 
A 1 299 ARG 299 315 315 ARG ARG A . n 
A 1 300 MET 300 316 316 MET MET A . n 
A 1 301 TRP 301 317 317 TRP TRP A . n 
A 1 302 LYS 302 318 318 LYS LYS A . n 
A 1 303 CYS 303 319 319 CYS CYS A . n 
A 1 304 ASN 304 320 320 ASN ASN A . n 
A 1 305 ASN 305 321 ?   ?   ?   A . n 
A 1 306 ALA 306 322 ?   ?   ?   A . n 
A 1 307 THR 307 323 ?   ?   ?   A . n 
A 1 308 VAL 308 324 324 VAL VAL A . n 
A 1 309 ASP 309 325 325 ASP ASP A . n 
A 1 310 TRP 310 326 326 TRP TRP A . n 
A 1 311 GLU 311 327 327 GLU GLU A . n 
A 1 312 TRP 312 328 328 TRP TRP A . n 
A 1 313 CYS 313 329 329 CYS CYS A . n 
A 1 314 ALA 314 330 330 ALA ALA A . n 
A 1 315 PRO 315 331 331 PRO PRO A . n 
A 1 316 LEU 316 332 332 LEU LEU A . n 
A 1 317 PRO 317 333 333 PRO PRO A . n 
A 1 318 ARG 318 334 334 ARG ARG A . n 
A 1 319 ASP 319 335 335 ASP ASP A . n 
A 1 320 ARG 320 336 336 ARG ARG A . n 
A 1 321 LEU 321 337 337 LEU LEU A . n 
A 1 322 GLN 322 338 338 GLN GLN A . n 
A 1 323 HIS 323 339 339 HIS HIS A . n 
A 1 324 THR 324 340 340 THR THR A . n 
A 1 325 LEU 325 341 341 LEU LEU A . n 
A 1 326 VAL 326 342 342 VAL VAL A . n 
A 1 327 SER 327 343 343 SER SER A . n 
A 1 328 VAL 328 344 344 VAL VAL A . n 
A 1 329 PRO 329 345 345 PRO PRO A . n 
A 1 330 GLY 330 346 346 GLY GLY A . n 
A 1 331 LYS 331 347 347 LYS LYS A . n 
A 1 332 ASP 332 348 348 ASP ASP A . n 
A 1 333 ALA 333 349 349 ALA ALA A . n 
A 1 334 ILE 334 350 350 ILE ILE A . n 
A 1 335 TYR 335 351 351 TYR TYR A . n 
A 1 336 SER 336 352 352 SER SER A . n 
A 1 337 LEU 337 353 353 LEU LEU A . n 
A 1 338 GLY 338 354 354 GLY GLY A . n 
A 1 339 GLY 339 355 355 GLY GLY A . n 
A 1 340 LYS 340 356 356 LYS LYS A . n 
A 1 341 THR 341 357 357 THR THR A . n 
A 1 342 LEU 342 358 358 LEU LEU A . n 
A 1 343 GLN 343 359 359 GLN GLN A . n 
A 1 344 ASP 344 360 360 ASP ASP A . n 
A 1 345 THR 345 361 361 THR THR A . n 
A 1 346 LEU 346 362 362 LEU LEU A . n 
A 1 347 SER 347 363 363 SER SER A . n 
A 1 348 ASN 348 364 364 ASN ASN A . n 
A 1 349 ALA 349 365 365 ALA ALA A . n 
A 1 350 VAL 350 366 366 VAL VAL A . n 
A 1 351 ILE 351 367 367 ILE ILE A . n 
A 1 352 TYR 352 368 368 TYR TYR A . n 
A 1 353 TYR 353 369 369 TYR TYR A . n 
A 1 354 ARG 354 370 370 ARG ARG A . n 
A 1 355 VAL 355 371 371 VAL VAL A . n 
A 1 356 GLY 356 372 372 GLY GLY A . n 
A 1 357 ASP 357 373 373 ASP ASP A . n 
A 1 358 ASN 358 374 374 ASN ASN A . n 
A 1 359 VAL 359 375 375 VAL VAL A . n 
A 1 360 TRP 360 376 376 TRP TRP A . n 
A 1 361 THR 361 377 377 THR THR A . n 
A 1 362 GLU 362 378 378 GLU GLU A . n 
A 1 363 THR 363 379 379 THR THR A . n 
A 1 364 THR 364 380 380 THR THR A . n 
A 1 365 GLN 365 381 381 GLN GLN A . n 
A 1 366 LEU 366 382 382 LEU LEU A . n 
A 1 367 GLU 367 383 383 GLU GLU A . n 
A 1 368 VAL 368 384 384 VAL VAL A . n 
A 1 369 ALA 369 385 385 ALA ALA A . n 
A 1 370 VAL 370 386 386 VAL VAL A . n 
A 1 371 SER 371 387 387 SER SER A . n 
A 1 372 GLY 372 388 388 GLY GLY A . n 
A 1 373 ALA 373 389 389 ALA ALA A . n 
A 1 374 ALA 374 390 390 ALA ALA A . n 
A 1 375 GLY 375 391 391 GLY GLY A . n 
A 1 376 ALA 376 392 392 ALA ALA A . n 
A 1 377 ASN 377 393 393 ASN ASN A . n 
A 1 378 LEU 378 394 394 LEU LEU A . n 
A 1 379 ASN 379 395 395 ASN ASN A . n 
A 1 380 GLY 380 396 396 GLY GLY A . n 
A 1 381 ILE 381 397 397 ILE ILE A . n 
A 1 382 ILE 382 398 398 ILE ILE A . n 
A 1 383 TYR 383 399 399 TYR TYR A . n 
A 1 384 LEU 384 400 400 LEU LEU A . n 
A 1 385 LEU 385 401 401 LEU LEU A . n 
A 1 386 GLY 386 402 402 GLY GLY A . n 
A 1 387 GLY 387 403 403 GLY GLY A . n 
A 1 388 GLU 388 404 404 GLU GLU A . n 
A 1 389 GLU 389 405 405 GLU GLU A . n 
A 1 390 ASN 390 406 406 ASN ASN A . n 
A 1 391 ASP 391 407 407 ASP ASP A . n 
A 1 392 LEU 392 408 408 LEU LEU A . n 
A 1 393 ASP 393 409 409 ASP ASP A . n 
A 1 394 PHE 394 410 410 PHE PHE A . n 
A 1 395 PHE 395 411 411 PHE PHE A . n 
A 1 396 THR 396 412 412 THR THR A . n 
A 1 397 LYS 397 413 413 LYS LYS A . n 
A 1 398 PRO 398 414 414 PRO PRO A . n 
A 1 399 SER 399 415 415 SER SER A . n 
A 1 400 ARG 400 416 416 ARG ARG A . n 
A 1 401 LEU 401 417 417 LEU LEU A . n 
A 1 402 ILE 402 418 418 ILE ILE A . n 
A 1 403 GLN 403 419 419 GLN GLN A . n 
A 1 404 CYS 404 420 420 CYS CYS A . n 
A 1 405 PHE 405 421 421 PHE PHE A . n 
A 1 406 ASP 406 422 422 ASP ASP A . n 
A 1 407 THR 407 423 423 THR THR A . n 
A 1 408 GLU 408 424 424 GLU GLU A . n 
A 1 409 THR 409 425 425 THR THR A . n 
A 1 410 ASP 410 426 426 ASP ASP A . n 
A 1 411 LYS 411 427 427 LYS LYS A . n 
A 1 412 CYS 412 428 428 CYS CYS A . n 
A 1 413 HIS 413 429 429 HIS HIS A . n 
A 1 414 VAL 414 430 430 VAL VAL A . n 
A 1 415 LYS 415 431 431 LYS LYS A . n 
A 1 416 PRO 416 432 432 PRO PRO A . n 
A 1 417 TYR 417 433 433 TYR TYR A . n 
A 1 418 VAL 418 434 434 VAL VAL A . n 
A 1 419 LEU 419 435 435 LEU LEU A . n 
A 1 420 PRO 420 436 436 PRO PRO A . n 
A 1 421 PHE 421 437 437 PHE PHE A . n 
A 1 422 ALA 422 438 438 ALA ALA A . n 
A 1 423 GLY 423 439 439 GLY GLY A . n 
A 1 424 ARG 424 440 440 ARG ARG A . n 
A 1 425 MET 425 441 441 MET MET A . n 
A 1 426 HIS 426 442 442 HIS HIS A . n 
A 1 427 ALA 427 443 443 ALA ALA A . n 
A 1 428 ALA 428 444 444 ALA ALA A . n 
A 1 429 VAL 429 445 445 VAL VAL A . n 
A 1 430 HIS 430 446 446 HIS HIS A . n 
A 1 431 LYS 431 447 447 LYS LYS A . n 
A 1 432 ASP 432 448 448 ASP ASP A . n 
A 1 433 LEU 433 449 449 LEU LEU A . n 
A 1 434 VAL 434 450 450 VAL VAL A . n 
A 1 435 PHE 435 451 451 PHE PHE A . n 
A 1 436 ILE 436 452 452 ILE ILE A . n 
A 1 437 VAL 437 453 453 VAL VAL A . n 
A 1 438 ALA 438 454 454 ALA ALA A . n 
A 1 439 GLU 439 455 455 GLU GLU A . n 
A 1 440 GLY 440 456 456 GLY GLY A . n 
A 1 441 ASP 441 457 457 ASP ASP A . n 
A 1 442 SER 442 458 458 SER SER A . n 
A 1 443 LEU 443 459 459 LEU LEU A . n 
A 1 444 VAL 444 460 460 VAL VAL A . n 
A 1 445 CYS 445 461 461 CYS CYS A . n 
A 1 446 TYR 446 462 462 TYR TYR A . n 
A 1 447 ASN 447 463 463 ASN ASN A . n 
A 1 448 PRO 448 464 464 PRO PRO A . n 
A 1 449 LEU 449 465 465 LEU LEU A . n 
A 1 450 LEU 450 466 466 LEU LEU A . n 
A 1 451 ASP 451 467 467 ASP ASP A . n 
A 1 452 SER 452 468 468 SER SER A . n 
A 1 453 PHE 453 469 469 PHE PHE A . n 
A 1 454 THR 454 470 470 THR THR A . n 
A 1 455 ARG 455 471 471 ARG ARG A . n 
A 1 456 LEU 456 472 472 LEU LEU A . n 
A 1 457 CYS 457 473 473 CYS CYS A . n 
A 1 458 LEU 458 474 474 LEU LEU A . n 
A 1 459 PRO 459 475 475 PRO PRO A . n 
A 1 460 GLU 460 476 476 GLU GLU A . n 
A 1 461 ALA 461 477 477 ALA ALA A . n 
A 1 462 TRP 462 478 ?   ?   ?   A . n 
A 1 463 SER 463 479 ?   ?   ?   A . n 
A 1 464 SER 464 480 ?   ?   ?   A . n 
A 1 465 ALA 465 481 ?   ?   ?   A . n 
A 1 466 PRO 466 482 ?   ?   ?   A . n 
A 1 467 SER 467 483 ?   ?   ?   A . n 
A 1 468 LEU 468 484 484 LEU LEU A . n 
A 1 469 TRP 469 485 485 TRP TRP A . n 
A 1 470 LYS 470 486 486 LYS LYS A . n 
A 1 471 ILE 471 487 487 ILE ILE A . n 
A 1 472 ALA 472 488 488 ALA ALA A . n 
A 1 473 SER 473 489 489 SER SER A . n 
A 1 474 CYS 474 490 490 CYS CYS A . n 
A 1 475 ASN 475 491 491 ASN ASN A . n 
A 1 476 GLY 476 492 492 GLY GLY A . n 
A 1 477 SER 477 493 493 SER SER A . n 
A 1 478 ILE 478 494 494 ILE ILE A . n 
A 1 479 TYR 479 495 495 TYR TYR A . n 
A 1 480 VAL 480 496 496 VAL VAL A . n 
A 1 481 PHE 481 497 497 PHE PHE A . n 
A 1 482 ARG 482 498 498 ARG ARG A . n 
A 1 483 ASP 483 499 499 ASP ASP A . n 
A 1 484 ARG 484 500 500 ARG ARG A . n 
A 1 485 TYR 485 501 501 TYR TYR A . n 
A 1 486 LYS 486 502 ?   ?   ?   A . n 
A 1 487 LYS 487 503 ?   ?   ?   A . n 
A 1 488 GLY 488 504 ?   ?   ?   A . n 
A 1 489 ASP 489 505 ?   ?   ?   A . n 
A 1 490 ALA 490 506 506 ALA ALA A . n 
A 1 491 ASN 491 507 507 ASN ASN A . n 
A 1 492 THR 492 508 508 THR THR A . n 
A 1 493 TYR 493 509 509 TYR TYR A . n 
A 1 494 LYS 494 510 510 LYS LYS A . n 
A 1 495 LEU 495 511 511 LEU LEU A . n 
A 1 496 ASP 496 512 512 ASP ASP A . n 
A 1 497 PRO 497 513 513 PRO PRO A . n 
A 1 498 ALA 498 514 514 ALA ALA A . n 
A 1 499 THR 499 515 515 THR THR A . n 
A 1 500 SER 500 516 516 SER SER A . n 
A 1 501 ALA 501 517 517 ALA ALA A . n 
A 1 502 VAL 502 518 518 VAL VAL A . n 
A 1 503 THR 503 519 519 THR THR A . n 
A 1 504 VAL 504 520 520 VAL VAL A . n 
A 1 505 THR 505 521 521 THR THR A . n 
A 1 506 ARG 506 522 ?   ?   ?   A . n 
A 1 507 GLY 507 523 ?   ?   ?   A . n 
A 1 508 ILE 508 524 ?   ?   ?   A . n 
A 1 509 LYS 509 525 525 LYS LYS A . n 
A 1 510 VAL 510 526 526 VAL VAL A . n 
A 1 511 LEU 511 527 527 LEU LEU A . n 
A 1 512 LEU 512 528 528 LEU LEU A . n 
A 1 513 THR 513 529 529 THR THR A . n 
A 1 514 ASN 514 530 530 ASN ASN A . n 
A 1 515 LEU 515 531 531 LEU LEU A . n 
A 1 516 GLN 516 532 532 GLN GLN A . n 
A 1 517 PHE 517 533 533 PHE PHE A . n 
A 1 518 VAL 518 534 534 VAL VAL A . n 
A 1 519 LEU 519 535 535 LEU LEU A . n 
A 1 520 ALA 520 536 536 ALA ALA A . n 
B 2 1   MET 1   1   ?   ?   ?   D . n 
B 2 2   ALA 2   2   ?   ?   ?   D . n 
B 2 3   TYR 3   3   ?   ?   ?   D . n 
B 2 4   SER 4   4   ?   ?   ?   D . n 
B 2 5   GLN 5   5   ?   ?   ?   D . n 
B 2 6   GLY 6   6   ?   ?   ?   D . n 
B 2 7   GLY 7   7   ?   ?   ?   D . n 
B 2 8   GLY 8   8   ?   ?   ?   D . n 
B 2 9   LYS 9   9   9   LYS LYS D . n 
B 2 10  LYS 10  10  10  LYS LYS D . n 
B 2 11  LYS 11  11  11  LYS LYS D . n 
B 2 12  VAL 12  12  12  VAL VAL D . n 
B 2 13  CYS 13  13  13  CYS CYS D . n 
B 2 14  TYR 14  14  14  TYR TYR D . n 
B 2 15  TYR 15  15  15  TYR TYR D . n 
B 2 16  TYR 16  16  16  TYR TYR D . n 
B 2 17  ASP 17  17  17  ASP ASP D . n 
B 2 18  GLY 18  18  18  GLY GLY D . n 
B 2 19  ASP 19  19  19  ASP ASP D . n 
B 2 20  ILE 20  20  20  ILE ILE D . n 
B 2 21  GLY 21  21  21  GLY GLY D . n 
B 2 22  ASN 22  22  22  ASN ASN D . n 
B 2 23  TYR 23  23  23  TYR TYR D . n 
B 2 24  TYR 24  24  24  TYR TYR D . n 
B 2 25  TYR 25  25  25  TYR TYR D . n 
B 2 26  GLY 26  26  26  GLY GLY D . n 
B 2 27  GLN 27  27  27  GLN GLN D . n 
B 2 28  GLY 28  28  28  GLY GLY D . n 
B 2 29  HIS 29  29  29  HIS HIS D . n 
B 2 30  PRO 30  30  30  PRO PRO D . n 
B 2 31  MET 31  31  31  MET MET D . n 
B 2 32  LYS 32  32  32  LYS LYS D . n 
B 2 33  PRO 33  33  33  PRO PRO D . n 
B 2 34  HIS 34  34  34  HIS HIS D . n 
B 2 35  ARG 35  35  35  ARG ARG D . n 
B 2 36  ILE 36  36  36  ILE ILE D . n 
B 2 37  ARG 37  37  37  ARG ARG D . n 
B 2 38  MET 38  38  38  MET MET D . n 
B 2 39  THR 39  39  39  THR THR D . n 
B 2 40  HIS 40  40  40  HIS HIS D . n 
B 2 41  ASN 41  41  41  ASN ASN D . n 
B 2 42  LEU 42  42  42  LEU LEU D . n 
B 2 43  LEU 43  43  43  LEU LEU D . n 
B 2 44  LEU 44  44  44  LEU LEU D . n 
B 2 45  ASN 45  45  45  ASN ASN D . n 
B 2 46  TYR 46  46  46  TYR TYR D . n 
B 2 47  GLY 47  47  47  GLY GLY D . n 
B 2 48  LEU 48  48  48  LEU LEU D . n 
B 2 49  TYR 49  49  49  TYR TYR D . n 
B 2 50  ARG 50  50  50  ARG ARG D . n 
B 2 51  LYS 51  51  51  LYS LYS D . n 
B 2 52  MET 52  52  52  MET MET D . n 
B 2 53  GLU 53  53  53  GLU GLU D . n 
B 2 54  ILE 54  54  54  ILE ILE D . n 
B 2 55  TYR 55  55  55  TYR TYR D . n 
B 2 56  ARG 56  56  56  ARG ARG D . n 
B 2 57  PRO 57  57  57  PRO PRO D . n 
B 2 58  HIS 58  58  58  HIS HIS D . n 
B 2 59  LYS 59  59  59  LYS LYS D . n 
B 2 60  ALA 60  60  60  ALA ALA D . n 
B 2 61  THR 61  61  61  THR THR D . n 
B 2 62  ALA 62  62  62  ALA ALA D . n 
B 2 63  GLU 63  63  63  GLU GLU D . n 
B 2 64  GLU 64  64  64  GLU GLU D . n 
B 2 65  MET 65  65  65  MET MET D . n 
B 2 66  THR 66  66  66  THR THR D . n 
B 2 67  LYS 67  67  67  LYS LYS D . n 
B 2 68  TYR 68  68  68  TYR TYR D . n 
B 2 69  HIS 69  69  69  HIS HIS D . n 
B 2 70  SER 70  70  70  SER SER D . n 
B 2 71  ASP 71  71  71  ASP ASP D . n 
B 2 72  GLU 72  72  72  GLU GLU D . n 
B 2 73  TYR 73  73  73  TYR TYR D . n 
B 2 74  ILE 74  74  74  ILE ILE D . n 
B 2 75  LYS 75  75  75  LYS LYS D . n 
B 2 76  PHE 76  76  76  PHE PHE D . n 
B 2 77  LEU 77  77  77  LEU LEU D . n 
B 2 78  ARG 78  78  78  ARG ARG D . n 
B 2 79  SER 79  79  79  SER SER D . n 
B 2 80  ILE 80  80  80  ILE ILE D . n 
B 2 81  ARG 81  81  81  ARG ARG D . n 
B 2 82  PRO 82  82  82  PRO PRO D . n 
B 2 83  ASP 83  83  83  ASP ASP D . n 
B 2 84  ASN 84  84  84  ASN ASN D . n 
B 2 85  MET 85  85  85  MET MET D . n 
B 2 86  SER 86  86  86  SER SER D . n 
B 2 87  GLU 87  87  87  GLU GLU D . n 
B 2 88  TYR 88  88  88  TYR TYR D . n 
B 2 89  SER 89  89  89  SER SER D . n 
B 2 90  LYS 90  90  90  LYS LYS D . n 
B 2 91  GLN 91  91  91  GLN GLN D . n 
B 2 92  MET 92  92  92  MET MET D . n 
B 2 93  GLN 93  93  93  GLN GLN D . n 
B 2 94  ARG 94  94  94  ARG ARG D . n 
B 2 95  PHE 95  95  95  PHE PHE D . n 
B 2 96  ASN 96  96  96  ASN ASN D . n 
B 2 97  VAL 97  97  97  VAL VAL D . n 
B 2 98  GLY 98  98  98  GLY GLY D . n 
B 2 99  GLU 99  99  99  GLU GLU D . n 
B 2 100 ASP 100 100 100 ASP ASP D . n 
B 2 101 CYS 101 101 101 CYS CYS D . n 
B 2 102 PRO 102 102 102 PRO PRO D . n 
B 2 103 VAL 103 103 103 VAL VAL D . n 
B 2 104 PHE 104 104 104 PHE PHE D . n 
B 2 105 ASP 105 105 105 ASP ASP D . n 
B 2 106 GLY 106 106 106 GLY GLY D . n 
B 2 107 LEU 107 107 107 LEU LEU D . n 
B 2 108 PHE 108 108 108 PHE PHE D . n 
B 2 109 GLU 109 109 109 GLU GLU D . n 
B 2 110 PHE 110 110 110 PHE PHE D . n 
B 2 111 CYS 111 111 111 CYS CYS D . n 
B 2 112 GLN 112 112 112 GLN GLN D . n 
B 2 113 LEU 113 113 113 LEU LEU D . n 
B 2 114 SER 114 114 114 SER SER D . n 
B 2 115 THR 115 115 115 THR THR D . n 
B 2 116 GLY 116 116 116 GLY GLY D . n 
B 2 117 GLY 117 117 117 GLY GLY D . n 
B 2 118 SER 118 118 118 SER SER D . n 
B 2 119 VAL 119 119 119 VAL VAL D . n 
B 2 120 ALA 120 120 120 ALA ALA D . n 
B 2 121 GLY 121 121 121 GLY GLY D . n 
B 2 122 ALA 122 122 122 ALA ALA D . n 
B 2 123 VAL 123 123 123 VAL VAL D . n 
B 2 124 LYS 124 124 124 LYS LYS D . n 
B 2 125 LEU 125 125 125 LEU LEU D . n 
B 2 126 ASN 126 126 126 ASN ASN D . n 
B 2 127 ARG 127 127 127 ARG ARG D . n 
B 2 128 GLN 128 128 128 GLN GLN D . n 
B 2 129 GLN 129 129 129 GLN GLN D . n 
B 2 130 THR 130 130 130 THR THR D . n 
B 2 131 ASP 131 131 131 ASP ASP D . n 
B 2 132 MET 132 132 132 MET MET D . n 
B 2 133 ALA 133 133 133 ALA ALA D . n 
B 2 134 VAL 134 134 134 VAL VAL D . n 
B 2 135 ASN 135 135 135 ASN ASN D . n 
B 2 136 TRP 136 136 136 TRP TRP D . n 
B 2 137 ALA 137 137 137 ALA ALA D . n 
B 2 138 GLY 138 138 138 GLY GLY D . n 
B 2 139 GLY 139 139 139 GLY GLY D . n 
B 2 140 LEU 140 140 140 LEU LEU D . n 
B 2 141 HIS 141 141 141 HIS HIS D . n 
B 2 142 HIS 142 142 142 HIS HIS D . n 
B 2 143 ALA 143 143 143 ALA ALA D . n 
B 2 144 LYS 144 144 144 LYS LYS D . n 
B 2 145 LYS 145 145 145 LYS LYS D . n 
B 2 146 SER 146 146 146 SER SER D . n 
B 2 147 GLU 147 147 147 GLU GLU D . n 
B 2 148 ALA 148 148 148 ALA ALA D . n 
B 2 149 SER 149 149 149 SER SER D . n 
B 2 150 GLY 150 150 150 GLY GLY D . n 
B 2 151 PHE 151 151 151 PHE PHE D . n 
B 2 152 CYS 152 152 152 CYS CYS D . n 
B 2 153 TYR 153 153 153 TYR TYR D . n 
B 2 154 VAL 154 154 154 VAL VAL D . n 
B 2 155 ASN 155 155 155 ASN ASN D . n 
B 2 156 ASP 156 156 156 ASP ASP D . n 
B 2 157 ILE 157 157 157 ILE ILE D . n 
B 2 158 VAL 158 158 158 VAL VAL D . n 
B 2 159 LEU 159 159 159 LEU LEU D . n 
B 2 160 ALA 160 160 160 ALA ALA D . n 
B 2 161 ILE 161 161 161 ILE ILE D . n 
B 2 162 LEU 162 162 162 LEU LEU D . n 
B 2 163 GLU 163 163 163 GLU GLU D . n 
B 2 164 LEU 164 164 164 LEU LEU D . n 
B 2 165 LEU 165 165 165 LEU LEU D . n 
B 2 166 LYS 166 166 166 LYS LYS D . n 
B 2 167 TYR 167 167 167 TYR TYR D . n 
B 2 168 HIS 168 168 168 HIS HIS D . n 
B 2 169 GLN 169 169 169 GLN GLN D . n 
B 2 170 ARG 170 170 170 ARG ARG D . n 
B 2 171 VAL 171 171 171 VAL VAL D . n 
B 2 172 LEU 172 172 172 LEU LEU D . n 
B 2 173 TYR 173 173 173 TYR TYR D . n 
B 2 174 ILE 174 174 174 ILE ILE D . n 
B 2 175 ASP 175 175 175 ASP ASP D . n 
B 2 176 ILE 176 176 176 ILE ILE D . n 
B 2 177 ASP 177 177 177 ASP ASP D . n 
B 2 178 ILE 178 178 178 ILE ILE D . n 
B 2 179 HIS 179 179 179 HIS HIS D . n 
B 2 180 HIS 180 180 180 HIS HIS D . n 
B 2 181 GLY 181 181 181 GLY GLY D . n 
B 2 182 ASP 182 182 182 ASP ASP D . n 
B 2 183 GLY 183 183 183 GLY GLY D . n 
B 2 184 VAL 184 184 184 VAL VAL D . n 
B 2 185 GLU 185 185 185 GLU GLU D . n 
B 2 186 GLU 186 186 186 GLU GLU D . n 
B 2 187 ALA 187 187 187 ALA ALA D . n 
B 2 188 PHE 188 188 188 PHE PHE D . n 
B 2 189 TYR 189 189 189 TYR TYR D . n 
B 2 190 THR 190 190 190 THR THR D . n 
B 2 191 THR 191 191 191 THR THR D . n 
B 2 192 ASP 192 192 192 ASP ASP D . n 
B 2 193 ARG 193 193 193 ARG ARG D . n 
B 2 194 VAL 194 194 194 VAL VAL D . n 
B 2 195 MET 195 195 195 MET MET D . n 
B 2 196 THR 196 196 196 THR THR D . n 
B 2 197 VAL 197 197 197 VAL VAL D . n 
B 2 198 SER 198 198 198 SER SER D . n 
B 2 199 PHE 199 199 199 PHE PHE D . n 
B 2 200 HIS 200 200 200 HIS HIS D . n 
B 2 201 LYS 201 201 201 LYS LYS D . n 
B 2 202 TYR 202 202 202 TYR TYR D . n 
B 2 203 GLY 203 203 203 GLY GLY D . n 
B 2 204 GLU 204 204 204 GLU GLU D . n 
B 2 205 TYR 205 205 205 TYR TYR D . n 
B 2 206 PHE 206 206 206 PHE PHE D . n 
B 2 207 PRO 207 207 207 PRO PRO D . n 
B 2 208 GLY 208 208 208 GLY GLY D . n 
B 2 209 THR 209 209 209 THR THR D . n 
B 2 210 GLY 210 210 210 GLY GLY D . n 
B 2 211 ASP 211 211 211 ASP ASP D . n 
B 2 212 LEU 212 212 212 LEU LEU D . n 
B 2 213 ARG 213 213 213 ARG ARG D . n 
B 2 214 ASP 214 214 214 ASP ASP D . n 
B 2 215 ILE 215 215 215 ILE ILE D . n 
B 2 216 GLY 216 216 216 GLY GLY D . n 
B 2 217 ALA 217 217 217 ALA ALA D . n 
B 2 218 GLY 218 218 218 GLY GLY D . n 
B 2 219 LYS 219 219 219 LYS LYS D . n 
B 2 220 GLY 220 220 220 GLY GLY D . n 
B 2 221 LYS 221 221 221 LYS LYS D . n 
B 2 222 TYR 222 222 222 TYR TYR D . n 
B 2 223 TYR 223 223 223 TYR TYR D . n 
B 2 224 ALA 224 224 224 ALA ALA D . n 
B 2 225 VAL 225 225 225 VAL VAL D . n 
B 2 226 ASN 226 226 226 ASN ASN D . n 
B 2 227 PHE 227 227 227 PHE PHE D . n 
B 2 228 PRO 228 228 228 PRO PRO D . n 
B 2 229 MET 229 229 229 MET MET D . n 
B 2 230 ARG 230 230 230 ARG ARG D . n 
B 2 231 ASP 231 231 231 ASP ASP D . n 
B 2 232 GLY 232 232 232 GLY GLY D . n 
B 2 233 ILE 233 233 233 ILE ILE D . n 
B 2 234 ASP 234 234 234 ASP ASP D . n 
B 2 235 ASP 235 235 235 ASP ASP D . n 
B 2 236 GLU 236 236 236 GLU GLU D . n 
B 2 237 SER 237 237 237 SER SER D . n 
B 2 238 TYR 238 238 238 TYR TYR D . n 
B 2 239 GLY 239 239 239 GLY GLY D . n 
B 2 240 GLN 240 240 240 GLN GLN D . n 
B 2 241 ILE 241 241 241 ILE ILE D . n 
B 2 242 PHE 242 242 242 PHE PHE D . n 
B 2 243 LYS 243 243 243 LYS LYS D . n 
B 2 244 PRO 244 244 244 PRO PRO D . n 
B 2 245 ILE 245 245 245 ILE ILE D . n 
B 2 246 ILE 246 246 246 ILE ILE D . n 
B 2 247 SER 247 247 247 SER SER D . n 
B 2 248 LYS 248 248 248 LYS LYS D . n 
B 2 249 VAL 249 249 249 VAL VAL D . n 
B 2 250 MET 250 250 250 MET MET D . n 
B 2 251 GLU 251 251 251 GLU GLU D . n 
B 2 252 MET 252 252 252 MET MET D . n 
B 2 253 TYR 253 253 253 TYR TYR D . n 
B 2 254 GLN 254 254 254 GLN GLN D . n 
B 2 255 PRO 255 255 255 PRO PRO D . n 
B 2 256 SER 256 256 256 SER SER D . n 
B 2 257 ALA 257 257 257 ALA ALA D . n 
B 2 258 VAL 258 258 258 VAL VAL D . n 
B 2 259 VAL 259 259 259 VAL VAL D . n 
B 2 260 LEU 260 260 260 LEU LEU D . n 
B 2 261 GLN 261 261 261 GLN GLN D . n 
B 2 262 CYS 262 262 262 CYS CYS D . n 
B 2 263 GLY 263 263 263 GLY GLY D . n 
B 2 264 ALA 264 264 264 ALA ALA D . n 
B 2 265 ASP 265 265 265 ASP ASP D . n 
B 2 266 SER 266 266 266 SER SER D . n 
B 2 267 LEU 267 267 267 LEU LEU D . n 
B 2 268 SER 268 268 268 SER SER D . n 
B 2 269 GLY 269 269 269 GLY GLY D . n 
B 2 270 ASP 270 270 270 ASP ASP D . n 
B 2 271 ARG 271 271 271 ARG ARG D . n 
B 2 272 LEU 272 272 272 LEU LEU D . n 
B 2 273 GLY 273 273 273 GLY GLY D . n 
B 2 274 CYS 274 274 274 CYS CYS D . n 
B 2 275 PHE 275 275 275 PHE PHE D . n 
B 2 276 ASN 276 276 276 ASN ASN D . n 
B 2 277 LEU 277 277 277 LEU LEU D . n 
B 2 278 THR 278 278 278 THR THR D . n 
B 2 279 VAL 279 279 279 VAL VAL D . n 
B 2 280 LYS 280 280 280 LYS LYS D . n 
B 2 281 GLY 281 281 281 GLY GLY D . n 
B 2 282 HIS 282 282 282 HIS HIS D . n 
B 2 283 ALA 283 283 283 ALA ALA D . n 
B 2 284 LYS 284 284 284 LYS LYS D . n 
B 2 285 CYS 285 285 285 CYS CYS D . n 
B 2 286 VAL 286 286 286 VAL VAL D . n 
B 2 287 GLU 287 287 287 GLU GLU D . n 
B 2 288 VAL 288 288 288 VAL VAL D . n 
B 2 289 VAL 289 289 289 VAL VAL D . n 
B 2 290 LYS 290 290 290 LYS LYS D . n 
B 2 291 THR 291 291 291 THR THR D . n 
B 2 292 PHE 292 292 292 PHE PHE D . n 
B 2 293 ASN 293 293 293 ASN ASN D . n 
B 2 294 LEU 294 294 294 LEU LEU D . n 
B 2 295 PRO 295 295 295 PRO PRO D . n 
B 2 296 LEU 296 296 296 LEU LEU D . n 
B 2 297 LEU 297 297 297 LEU LEU D . n 
B 2 298 MET 298 298 298 MET MET D . n 
B 2 299 LEU 299 299 299 LEU LEU D . n 
B 2 300 GLY 300 300 300 GLY GLY D . n 
B 2 301 GLY 301 301 301 GLY GLY D . n 
B 2 302 GLY 302 302 302 GLY GLY D . n 
B 2 303 GLY 303 303 303 GLY GLY D . n 
B 2 304 TYR 304 304 304 TYR TYR D . n 
B 2 305 THR 305 305 305 THR THR D . n 
B 2 306 ILE 306 306 306 ILE ILE D . n 
B 2 307 ARG 307 307 307 ARG ARG D . n 
B 2 308 ASN 308 308 308 ASN ASN D . n 
B 2 309 VAL 309 309 309 VAL VAL D . n 
B 2 310 ALA 310 310 310 ALA ALA D . n 
B 2 311 ARG 311 311 311 ARG ARG D . n 
B 2 312 CYS 312 312 312 CYS CYS D . n 
B 2 313 TRP 313 313 313 TRP TRP D . n 
B 2 314 THR 314 314 314 THR THR D . n 
B 2 315 TYR 315 315 315 TYR TYR D . n 
B 2 316 GLU 316 316 316 GLU GLU D . n 
B 2 317 THR 317 317 317 THR THR D . n 
B 2 318 ALA 318 318 318 ALA ALA D . n 
B 2 319 VAL 319 319 319 VAL VAL D . n 
B 2 320 ALA 320 320 320 ALA ALA D . n 
B 2 321 LEU 321 321 321 LEU LEU D . n 
B 2 322 ASP 322 322 322 ASP ASP D . n 
B 2 323 CYS 323 323 323 CYS CYS D . n 
B 2 324 GLU 324 324 324 GLU GLU D . n 
B 2 325 ILE 325 325 325 ILE ILE D . n 
B 2 326 PRO 326 326 326 PRO PRO D . n 
B 2 327 ASN 327 327 327 ASN ASN D . n 
B 2 328 GLU 328 328 328 GLU GLU D . n 
B 2 329 LEU 329 329 329 LEU LEU D . n 
B 2 330 PRO 330 330 330 PRO PRO D . n 
B 2 331 TYR 331 331 331 TYR TYR D . n 
B 2 332 ASN 332 332 332 ASN ASN D . n 
B 2 333 ASP 333 333 333 ASP ASP D . n 
B 2 334 TYR 334 334 334 TYR TYR D . n 
B 2 335 PHE 335 335 335 PHE PHE D . n 
B 2 336 GLU 336 336 336 GLU GLU D . n 
B 2 337 TYR 337 337 337 TYR TYR D . n 
B 2 338 PHE 338 338 338 PHE PHE D . n 
B 2 339 GLY 339 339 339 GLY GLY D . n 
B 2 340 PRO 340 340 340 PRO PRO D . n 
B 2 341 ASP 341 341 341 ASP ASP D . n 
B 2 342 PHE 342 342 342 PHE PHE D . n 
B 2 343 LYS 343 343 343 LYS LYS D . n 
B 2 344 LEU 344 344 344 LEU LEU D . n 
B 2 345 HIS 345 345 345 HIS HIS D . n 
B 2 346 ILE 346 346 346 ILE ILE D . n 
B 2 347 SER 347 347 347 SER SER D . n 
B 2 348 PRO 348 348 348 PRO PRO D . n 
B 2 349 SER 349 349 349 SER SER D . n 
B 2 350 ASN 350 350 350 ASN ASN D . n 
B 2 351 MET 351 351 351 MET MET D . n 
B 2 352 THR 352 352 352 THR THR D . n 
B 2 353 ASN 353 353 353 ASN ASN D . n 
B 2 354 GLN 354 354 354 GLN GLN D . n 
B 2 355 ASN 355 355 355 ASN ASN D . n 
B 2 356 THR 356 356 356 THR THR D . n 
B 2 357 PRO 357 357 357 PRO PRO D . n 
B 2 358 GLU 358 358 358 GLU GLU D . n 
B 2 359 TYR 359 359 359 TYR TYR D . n 
B 2 360 MET 360 360 360 MET MET D . n 
B 2 361 GLU 361 361 361 GLU GLU D . n 
B 2 362 LYS 362 362 362 LYS LYS D . n 
B 2 363 ILE 363 363 363 ILE ILE D . n 
B 2 364 LYS 364 364 364 LYS LYS D . n 
B 2 365 GLN 365 365 365 GLN GLN D . n 
B 2 366 ARG 366 366 366 ARG ARG D . n 
B 2 367 LEU 367 367 367 LEU LEU D . n 
B 2 368 PHE 368 368 368 PHE PHE D . n 
B 2 369 GLU 369 369 369 GLU GLU D . n 
B 2 370 ASN 370 370 370 ASN ASN D . n 
B 2 371 LEU 371 371 371 LEU LEU D . n 
B 2 372 ARG 372 372 372 ARG ARG D . n 
B 2 373 MET 373 373 373 MET MET D . n 
B 2 374 LEU 374 374 374 LEU LEU D . n 
B 2 375 PRO 375 375 375 PRO PRO D . n 
B 2 376 HIS 376 376 ?   ?   ?   D . n 
B 2 377 ALA 377 377 ?   ?   ?   D . n 
B 2 378 PRO 378 378 ?   ?   ?   D . n 
B 2 379 GLY 379 379 ?   ?   ?   D . n 
B 2 380 VAL 380 380 ?   ?   ?   D . n 
B 2 381 GLN 381 381 ?   ?   ?   D . n 
B 2 382 MET 382 382 ?   ?   ?   D . n 
B 2 383 GLN 383 383 ?   ?   ?   D . n 
B 2 384 ALA 384 384 ?   ?   ?   D . n 
B 2 385 ILE 385 385 ?   ?   ?   D . n 
B 2 386 PRO 386 386 ?   ?   ?   D . n 
B 2 387 GLU 387 387 ?   ?   ?   D . n 
B 2 388 ASP 388 388 ?   ?   ?   D . n 
B 2 389 ALA 389 389 ?   ?   ?   D . n 
B 2 390 VAL 390 390 ?   ?   ?   D . n 
B 2 391 HIS 391 391 ?   ?   ?   D . n 
B 2 392 GLU 392 392 ?   ?   ?   D . n 
B 2 393 ASP 393 393 ?   ?   ?   D . n 
B 2 394 SER 394 394 ?   ?   ?   D . n 
B 2 395 GLY 395 395 ?   ?   ?   D . n 
B 2 396 ASP 396 396 ?   ?   ?   D . n 
B 2 397 GLU 397 397 ?   ?   ?   D . n 
B 2 398 ASP 398 398 ?   ?   ?   D . n 
B 2 399 GLY 399 399 ?   ?   ?   D . n 
B 2 400 GLU 400 400 ?   ?   ?   D . n 
B 2 401 ASP 401 401 ?   ?   ?   D . n 
B 2 402 PRO 402 402 ?   ?   ?   D . n 
B 2 403 ASP 403 403 ?   ?   ?   D . n 
B 2 404 LYS 404 404 ?   ?   ?   D . n 
B 2 405 ARG 405 405 ?   ?   ?   D . n 
B 2 406 ILE 406 406 ?   ?   ?   D . n 
B 2 407 SER 407 407 ?   ?   ?   D . n 
B 2 408 ILE 408 408 ?   ?   ?   D . n 
B 2 409 ARG 409 409 ?   ?   ?   D . n 
B 2 410 ALA 410 410 ?   ?   ?   D . n 
B 2 411 SER 411 411 ?   ?   ?   D . n 
B 2 412 ASP 412 412 ?   ?   ?   D . n 
B 2 413 LYS 413 413 ?   ?   ?   D . n 
B 2 414 ARG 414 414 ?   ?   ?   D . n 
B 2 415 ILE 415 415 ?   ?   ?   D . n 
B 2 416 ALA 416 416 ?   ?   ?   D . n 
B 2 417 CYS 417 417 ?   ?   ?   D . n 
B 2 418 ASP 418 418 ?   ?   ?   D . n 
B 2 419 GLU 419 419 ?   ?   ?   D . n 
B 2 420 GLU 420 420 ?   ?   ?   D . n 
B 2 421 PHE 421 421 ?   ?   ?   D . n 
B 2 422 SER 422 422 ?   ?   ?   D . n 
B 2 423 ASP 423 423 ?   ?   ?   D . n 
B 2 424 SER 424 424 ?   ?   ?   D . n 
B 2 425 GLU 425 425 ?   ?   ?   D . n 
B 2 426 ASP 426 426 ?   ?   ?   D . n 
B 2 427 GLU 427 427 ?   ?   ?   D . n 
B 2 428 GLY 428 428 ?   ?   ?   D . n 
B 2 429 GLU 429 429 ?   ?   ?   D . n 
B 2 430 GLY 430 430 ?   ?   ?   D . n 
B 2 431 GLY 431 431 ?   ?   ?   D . n 
B 2 432 ARG 432 432 ?   ?   ?   D . n 
B 2 433 ARG 433 433 ?   ?   ?   D . n 
B 2 434 ASN 434 434 ?   ?   ?   D . n 
B 2 435 VAL 435 435 ?   ?   ?   D . n 
B 2 436 ALA 436 436 ?   ?   ?   D . n 
B 2 437 ASP 437 437 ?   ?   ?   D . n 
B 2 438 HIS 438 438 ?   ?   ?   D . n 
B 2 439 LYS 439 439 ?   ?   ?   D . n 
B 2 440 LYS 440 440 ?   ?   ?   D . n 
B 2 441 GLY 441 441 ?   ?   ?   D . n 
B 2 442 ALA 442 442 ?   ?   ?   D . n 
B 2 443 LYS 443 443 ?   ?   ?   D . n 
B 2 444 LYS 444 444 ?   ?   ?   D . n 
B 2 445 ALA 445 445 ?   ?   ?   D . n 
B 2 446 ARG 446 446 ?   ?   ?   D . n 
B 2 447 ILE 447 447 ?   ?   ?   D . n 
B 2 448 GLU 448 448 ?   ?   ?   D . n 
B 2 449 GLU 449 449 ?   ?   ?   D . n 
B 2 450 ASP 450 450 ?   ?   ?   D . n 
B 2 451 LYS 451 451 ?   ?   ?   D . n 
B 2 452 LYS 452 452 ?   ?   ?   D . n 
B 2 453 GLU 453 453 ?   ?   ?   D . n 
B 2 454 THR 454 454 ?   ?   ?   D . n 
B 2 455 GLU 455 455 ?   ?   ?   D . n 
B 2 456 ASP 456 456 ?   ?   ?   D . n 
B 2 457 LYS 457 457 ?   ?   ?   D . n 
B 2 458 LYS 458 458 ?   ?   ?   D . n 
B 2 459 THR 459 459 ?   ?   ?   D . n 
B 2 460 ASP 460 460 ?   ?   ?   D . n 
B 2 461 VAL 461 461 ?   ?   ?   D . n 
B 2 462 LYS 462 462 ?   ?   ?   D . n 
B 2 463 GLU 463 463 ?   ?   ?   D . n 
B 2 464 GLU 464 464 ?   ?   ?   D . n 
B 2 465 ASP 465 465 ?   ?   ?   D . n 
B 2 466 LYS 466 466 ?   ?   ?   D . n 
B 2 467 SER 467 467 ?   ?   ?   D . n 
B 2 468 LYS 468 468 ?   ?   ?   D . n 
B 2 469 ASP 469 469 ?   ?   ?   D . n 
B 2 470 ASN 470 470 ?   ?   ?   D . n 
B 2 471 SER 471 471 ?   ?   ?   D . n 
B 2 472 GLY 472 472 ?   ?   ?   D . n 
B 2 473 GLU 473 473 ?   ?   ?   D . n 
B 2 474 LYS 474 474 ?   ?   ?   D . n 
B 2 475 THR 475 475 ?   ?   ?   D . n 
B 2 476 ASP 476 476 ?   ?   ?   D . n 
B 2 477 THR 477 477 ?   ?   ?   D . n 
B 2 478 LYS 478 478 ?   ?   ?   D . n 
B 2 479 GLY 479 479 ?   ?   ?   D . n 
B 2 480 THR 480 480 ?   ?   ?   D . n 
B 2 481 LYS 481 481 ?   ?   ?   D . n 
B 2 482 SER 482 482 ?   ?   ?   D . n 
B 2 483 GLU 483 483 ?   ?   ?   D . n 
B 2 484 GLN 484 484 ?   ?   ?   D . n 
B 2 485 LEU 485 485 ?   ?   ?   D . n 
B 2 486 SER 486 486 ?   ?   ?   D . n 
B 2 487 ASN 487 487 ?   ?   ?   D . n 
B 2 488 PRO 488 488 ?   ?   ?   D . n 
C 1 1   MET 1   17  ?   ?   ?   C . n 
C 1 2   GLU 2   18  ?   ?   ?   C . n 
C 1 3   SER 3   19  ?   ?   ?   C . n 
C 1 4   PRO 4   20  ?   ?   ?   C . n 
C 1 5   GLU 5   21  ?   ?   ?   C . n 
C 1 6   GLU 6   22  ?   ?   ?   C . n 
C 1 7   PRO 7   23  ?   ?   ?   C . n 
C 1 8   GLY 8   24  ?   ?   ?   C . n 
C 1 9   ALA 9   25  ?   ?   ?   C . n 
C 1 10  SER 10  26  ?   ?   ?   C . n 
C 1 11  MET 11  27  ?   ?   ?   C . n 
C 1 12  ASP 12  28  ?   ?   ?   C . n 
C 1 13  GLU 13  29  ?   ?   ?   C . n 
C 1 14  ASN 14  30  ?   ?   ?   C . n 
C 1 15  TYR 15  31  ?   ?   ?   C . n 
C 1 16  PHE 16  32  32  PHE PHE C . n 
C 1 17  VAL 17  33  33  VAL VAL C . n 
C 1 18  ASN 18  34  34  ASN ASN C . n 
C 1 19  TYR 19  35  35  TYR TYR C . n 
C 1 20  THR 20  36  36  THR THR C . n 
C 1 21  PHE 21  37  37  PHE PHE C . n 
C 1 22  LYS 22  38  38  LYS LYS C . n 
C 1 23  ASP 23  39  39  ASP ASP C . n 
C 1 24  ARG 24  40  40  ARG ARG C . n 
C 1 25  SER 25  41  41  SER SER C . n 
C 1 26  HIS 26  42  42  HIS HIS C . n 
C 1 27  SER 27  43  43  SER SER C . n 
C 1 28  GLY 28  44  44  GLY GLY C . n 
C 1 29  ARG 29  45  45  ARG ARG C . n 
C 1 30  VAL 30  46  46  VAL VAL C . n 
C 1 31  ALA 31  47  47  ALA ALA C . n 
C 1 32  GLN 32  48  48  GLN GLN C . n 
C 1 33  GLY 33  49  49  GLY GLY C . n 
C 1 34  ILE 34  50  50  ILE ILE C . n 
C 1 35  MET 35  51  51  MET MET C . n 
C 1 36  LYS 36  52  52  LYS LYS C . n 
C 1 37  LEU 37  53  53  LEU LEU C . n 
C 1 38  CYS 38  54  54  CYS CYS C . n 
C 1 39  LEU 39  55  55  LEU LEU C . n 
C 1 40  GLU 40  56  56  GLU GLU C . n 
C 1 41  GLU 41  57  57  GLU GLU C . n 
C 1 42  GLU 42  58  ?   ?   ?   C . n 
C 1 43  LEU 43  59  ?   ?   ?   C . n 
C 1 44  PHE 44  60  ?   ?   ?   C . n 
C 1 45  ALA 45  61  ?   ?   ?   C . n 
C 1 46  ASP 46  62  ?   ?   ?   C . n 
C 1 47  VAL 47  63  ?   ?   ?   C . n 
C 1 48  THR 48  64  ?   ?   ?   C . n 
C 1 49  ILE 49  65  ?   ?   ?   C . n 
C 1 50  SER 50  66  ?   ?   ?   C . n 
C 1 51  VAL 51  67  ?   ?   ?   C . n 
C 1 52  GLU 52  68  ?   ?   ?   C . n 
C 1 53  GLY 53  69  ?   ?   ?   C . n 
C 1 54  ARG 54  70  ?   ?   ?   C . n 
C 1 55  GLU 55  71  ?   ?   ?   C . n 
C 1 56  PHE 56  72  ?   ?   ?   C . n 
C 1 57  GLN 57  73  ?   ?   ?   C . n 
C 1 58  LEU 58  74  ?   ?   ?   C . n 
C 1 59  HIS 59  75  ?   ?   ?   C . n 
C 1 60  ARG 60  76  76  ARG ARG C . n 
C 1 61  LEU 61  77  77  LEU LEU C . n 
C 1 62  VAL 62  78  78  VAL VAL C . n 
C 1 63  LEU 63  79  79  LEU LEU C . n 
C 1 64  SER 64  80  80  SER SER C . n 
C 1 65  ALA 65  81  81  ALA ALA C . n 
C 1 66  GLN 66  82  82  GLN GLN C . n 
C 1 67  SER 67  83  83  SER SER C . n 
C 1 68  CYS 68  84  84  CYS CYS C . n 
C 1 69  PHE 69  85  85  PHE PHE C . n 
C 1 70  PHE 70  86  86  PHE PHE C . n 
C 1 71  ARG 71  87  87  ARG ARG C . n 
C 1 72  SER 72  88  88  SER SER C . n 
C 1 73  MET 73  89  89  MET MET C . n 
C 1 74  PHE 74  90  90  PHE PHE C . n 
C 1 75  THR 75  91  ?   ?   ?   C . n 
C 1 76  SER 76  92  ?   ?   ?   C . n 
C 1 77  ASN 77  93  ?   ?   ?   C . n 
C 1 78  LEU 78  94  ?   ?   ?   C . n 
C 1 79  LYS 79  95  ?   ?   ?   C . n 
C 1 80  GLU 80  96  ?   ?   ?   C . n 
C 1 81  ALA 81  97  ?   ?   ?   C . n 
C 1 82  HIS 82  98  ?   ?   ?   C . n 
C 1 83  ASN 83  99  ?   ?   ?   C . n 
C 1 84  ARG 84  100 ?   ?   ?   C . n 
C 1 85  VAL 85  101 ?   ?   ?   C . n 
C 1 86  ILE 86  102 ?   ?   ?   C . n 
C 1 87  VAL 87  103 ?   ?   ?   C . n 
C 1 88  LEU 88  104 ?   ?   ?   C . n 
C 1 89  GLN 89  105 105 GLN GLN C . n 
C 1 90  ASP 90  106 106 ASP ASP C . n 
C 1 91  VAL 91  107 107 VAL VAL C . n 
C 1 92  SER 92  108 108 SER SER C . n 
C 1 93  GLU 93  109 109 GLU GLU C . n 
C 1 94  SER 94  110 110 SER SER C . n 
C 1 95  VAL 95  111 111 VAL VAL C . n 
C 1 96  PHE 96  112 112 PHE PHE C . n 
C 1 97  GLN 97  113 113 GLN GLN C . n 
C 1 98  LEU 98  114 114 LEU LEU C . n 
C 1 99  LEU 99  115 115 LEU LEU C . n 
C 1 100 VAL 100 116 116 VAL VAL C . n 
C 1 101 ASP 101 117 117 ASP ASP C . n 
C 1 102 TYR 102 118 118 TYR TYR C . n 
C 1 103 ILE 103 119 119 ILE ILE C . n 
C 1 104 TYR 104 120 120 TYR TYR C . n 
C 1 105 HIS 105 121 121 HIS HIS C . n 
C 1 106 GLY 106 122 122 GLY GLY C . n 
C 1 107 THR 107 123 123 THR THR C . n 
C 1 108 VAL 108 124 124 VAL VAL C . n 
C 1 109 LYS 109 125 125 LYS LYS C . n 
C 1 110 LEU 110 126 126 LEU LEU C . n 
C 1 111 ARG 111 127 127 ARG ARG C . n 
C 1 112 ALA 112 128 128 ALA ALA C . n 
C 1 113 GLU 113 129 129 GLU GLU C . n 
C 1 114 GLU 114 130 130 GLU GLU C . n 
C 1 115 LEU 115 131 131 LEU LEU C . n 
C 1 116 GLN 116 132 132 GLN GLN C . n 
C 1 117 GLU 117 133 133 GLU GLU C . n 
C 1 118 ILE 118 134 134 ILE ILE C . n 
C 1 119 TYR 119 135 135 TYR TYR C . n 
C 1 120 GLU 120 136 136 GLU GLU C . n 
C 1 121 VAL 121 137 137 VAL VAL C . n 
C 1 122 SER 122 138 138 SER SER C . n 
C 1 123 ASP 123 139 139 ASP ASP C . n 
C 1 124 MET 124 140 140 MET MET C . n 
C 1 125 TYR 125 141 141 TYR TYR C . n 
C 1 126 GLN 126 142 142 GLN GLN C . n 
C 1 127 LEU 127 143 143 LEU LEU C . n 
C 1 128 THR 128 144 144 THR THR C . n 
C 1 129 SER 129 145 145 SER SER C . n 
C 1 130 LEU 130 146 146 LEU LEU C . n 
C 1 131 PHE 131 147 147 PHE PHE C . n 
C 1 132 GLU 132 148 148 GLU GLU C . n 
C 1 133 GLU 133 149 149 GLU GLU C . n 
C 1 134 CYS 134 150 150 CYS CYS C . n 
C 1 135 SER 135 151 151 SER SER C . n 
C 1 136 ARG 136 152 152 ARG ARG C . n 
C 1 137 PHE 137 153 153 PHE PHE C . n 
C 1 138 LEU 138 154 154 LEU LEU C . n 
C 1 139 ALA 139 155 155 ALA ALA C . n 
C 1 140 ARG 140 156 ?   ?   ?   C . n 
C 1 141 THR 141 157 ?   ?   ?   C . n 
C 1 142 VAL 142 158 ?   ?   ?   C . n 
C 1 143 GLN 143 159 ?   ?   ?   C . n 
C 1 144 VAL 144 160 ?   ?   ?   C . n 
C 1 145 GLY 145 161 161 GLY GLY C . n 
C 1 146 ASN 146 162 162 ASN ASN C . n 
C 1 147 CYS 147 163 163 CYS CYS C . n 
C 1 148 LEU 148 164 164 LEU LEU C . n 
C 1 149 GLN 149 165 165 GLN GLN C . n 
C 1 150 VAL 150 166 166 VAL VAL C . n 
C 1 151 MET 151 167 167 MET MET C . n 
C 1 152 TRP 152 168 168 TRP TRP C . n 
C 1 153 LEU 153 169 169 LEU LEU C . n 
C 1 154 ALA 154 170 170 ALA ALA C . n 
C 1 155 ASP 155 171 171 ASP ASP C . n 
C 1 156 ARG 156 172 172 ARG ARG C . n 
C 1 157 HIS 157 173 173 HIS HIS C . n 
C 1 158 SER 158 174 174 SER SER C . n 
C 1 159 ASP 159 175 175 ASP ASP C . n 
C 1 160 PRO 160 176 176 PRO PRO C . n 
C 1 161 GLU 161 177 177 GLU GLU C . n 
C 1 162 LEU 162 178 178 LEU LEU C . n 
C 1 163 TYR 163 179 179 TYR TYR C . n 
C 1 164 THR 164 180 180 THR THR C . n 
C 1 165 ALA 165 181 181 ALA ALA C . n 
C 1 166 ALA 166 182 182 ALA ALA C . n 
C 1 167 LYS 167 183 183 LYS LYS C . n 
C 1 168 HIS 168 184 184 HIS HIS C . n 
C 1 169 CYS 169 185 185 CYS CYS C . n 
C 1 170 ALA 170 186 186 ALA ALA C . n 
C 1 171 LYS 171 187 187 LYS LYS C . n 
C 1 172 THR 172 188 188 THR THR C . n 
C 1 173 HIS 173 189 189 HIS HIS C . n 
C 1 174 LEU 174 190 190 LEU LEU C . n 
C 1 175 ALA 175 191 191 ALA ALA C . n 
C 1 176 GLN 176 192 192 GLN GLN C . n 
C 1 177 LEU 177 193 193 LEU LEU C . n 
C 1 178 GLN 178 194 194 GLN GLN C . n 
C 1 179 ASN 179 195 ?   ?   ?   C . n 
C 1 180 THR 180 196 ?   ?   ?   C . n 
C 1 181 GLU 181 197 ?   ?   ?   C . n 
C 1 182 GLU 182 198 ?   ?   ?   C . n 
C 1 183 PHE 183 199 ?   ?   ?   C . n 
C 1 184 LEU 184 200 ?   ?   ?   C . n 
C 1 185 HIS 185 201 ?   ?   ?   C . n 
C 1 186 LEU 186 202 ?   ?   ?   C . n 
C 1 187 PRO 187 203 ?   ?   ?   C . n 
C 1 188 HIS 188 204 204 HIS HIS C . n 
C 1 189 ARG 189 205 205 ARG ARG C . n 
C 1 190 LEU 190 206 206 LEU LEU C . n 
C 1 191 LEU 191 207 207 LEU LEU C . n 
C 1 192 THR 192 208 208 THR THR C . n 
C 1 193 ASP 193 209 209 ASP ASP C . n 
C 1 194 ILE 194 210 210 ILE ILE C . n 
C 1 195 ILE 195 211 211 ILE ILE C . n 
C 1 196 SER 196 212 212 SER SER C . n 
C 1 197 ASP 197 213 213 ASP ASP C . n 
C 1 198 GLY 198 214 214 GLY GLY C . n 
C 1 199 VAL 199 215 215 VAL VAL C . n 
C 1 200 PRO 200 216 ?   ?   ?   C . n 
C 1 201 CYS 201 217 ?   ?   ?   C . n 
C 1 202 SER 202 218 ?   ?   ?   C . n 
C 1 203 GLN 203 219 219 GLN GLN C . n 
C 1 204 ASN 204 220 220 ASN ASN C . n 
C 1 205 PRO 205 221 221 PRO PRO C . n 
C 1 206 THR 206 222 222 THR THR C . n 
C 1 207 GLU 207 223 223 GLU GLU C . n 
C 1 208 ALA 208 224 224 ALA ALA C . n 
C 1 209 ILE 209 225 225 ILE ILE C . n 
C 1 210 GLU 210 226 226 GLU GLU C . n 
C 1 211 ALA 211 227 227 ALA ALA C . n 
C 1 212 TRP 212 228 ?   ?   ?   C . n 
C 1 213 ILE 213 229 ?   ?   ?   C . n 
C 1 214 ASN 214 230 ?   ?   ?   C . n 
C 1 215 PHE 215 231 ?   ?   ?   C . n 
C 1 216 ASN 216 232 ?   ?   ?   C . n 
C 1 217 LYS 217 233 ?   ?   ?   C . n 
C 1 218 GLU 218 234 ?   ?   ?   C . n 
C 1 219 GLU 219 235 ?   ?   ?   C . n 
C 1 220 ARG 220 236 ?   ?   ?   C . n 
C 1 221 GLU 221 237 ?   ?   ?   C . n 
C 1 222 ALA 222 238 ?   ?   ?   C . n 
C 1 223 PHE 223 239 ?   ?   ?   C . n 
C 1 224 ALA 224 240 ?   ?   ?   C . n 
C 1 225 GLU 225 241 ?   ?   ?   C . n 
C 1 226 SER 226 242 ?   ?   ?   C . n 
C 1 227 LEU 227 243 243 LEU LEU C . n 
C 1 228 ARG 228 244 244 ARG ARG C . n 
C 1 229 THR 229 245 245 THR THR C . n 
C 1 230 SER 230 246 246 SER SER C . n 
C 1 231 LEU 231 247 247 LEU LEU C . n 
C 1 232 LYS 232 248 248 LYS LYS C . n 
C 1 233 GLU 233 249 249 GLU GLU C . n 
C 1 234 ILE 234 250 250 ILE ILE C . n 
C 1 235 GLY 235 251 251 GLY GLY C . n 
C 1 236 GLU 236 252 252 GLU GLU C . n 
C 1 237 ASN 237 253 253 ASN ASN C . n 
C 1 238 VAL 238 254 254 VAL VAL C . n 
C 1 239 HIS 239 255 255 HIS HIS C . n 
C 1 240 ILE 240 256 256 ILE ILE C . n 
C 1 241 TYR 241 257 257 TYR TYR C . n 
C 1 242 LEU 242 258 258 LEU LEU C . n 
C 1 243 ILE 243 259 259 ILE ILE C . n 
C 1 244 GLY 244 260 260 GLY GLY C . n 
C 1 245 LYS 245 261 261 LYS LYS C . n 
C 1 246 GLU 246 262 ?   ?   ?   C . n 
C 1 247 SER 247 263 ?   ?   ?   C . n 
C 1 248 SER 248 264 ?   ?   ?   C . n 
C 1 249 ARG 249 265 ?   ?   ?   C . n 
C 1 250 THR 250 266 ?   ?   ?   C . n 
C 1 251 HIS 251 267 ?   ?   ?   C . n 
C 1 252 SER 252 268 268 SER SER C . n 
C 1 253 LEU 253 269 269 LEU LEU C . n 
C 1 254 ALA 254 270 270 ALA ALA C . n 
C 1 255 VAL 255 271 271 VAL VAL C . n 
C 1 256 SER 256 272 272 SER SER C . n 
C 1 257 LEU 257 273 273 LEU LEU C . n 
C 1 258 HIS 258 274 274 HIS HIS C . n 
C 1 259 CYS 259 275 275 CYS CYS C . n 
C 1 260 ALA 260 276 276 ALA ALA C . n 
C 1 261 GLU 261 277 277 GLU GLU C . n 
C 1 262 ASP 262 278 ?   ?   ?   C . n 
C 1 263 ASP 263 279 ?   ?   ?   C . n 
C 1 264 SER 264 280 280 SER SER C . n 
C 1 265 ILE 265 281 281 ILE ILE C . n 
C 1 266 SER 266 282 282 SER SER C . n 
C 1 267 VAL 267 283 283 VAL VAL C . n 
C 1 268 SER 268 284 284 SER SER C . n 
C 1 269 GLY 269 285 285 GLY GLY C . n 
C 1 270 GLN 270 286 286 GLN GLN C . n 
C 1 271 ASN 271 287 287 ASN ASN C . n 
C 1 272 SER 272 288 288 SER SER C . n 
C 1 273 LEU 273 289 289 LEU LEU C . n 
C 1 274 CYS 274 290 290 CYS CYS C . n 
C 1 275 HIS 275 291 291 HIS HIS C . n 
C 1 276 GLN 276 292 292 GLN GLN C . n 
C 1 277 ILE 277 293 293 ILE ILE C . n 
C 1 278 THR 278 294 294 THR THR C . n 
C 1 279 ALA 279 295 295 ALA ALA C . n 
C 1 280 ALA 280 296 296 ALA ALA C . n 
C 1 281 CYS 281 297 297 CYS CYS C . n 
C 1 282 LYS 282 298 298 LYS LYS C . n 
C 1 283 HIS 283 299 299 HIS HIS C . n 
C 1 284 GLY 284 300 300 GLY GLY C . n 
C 1 285 GLY 285 301 301 GLY GLY C . n 
C 1 286 ASP 286 302 302 ASP ASP C . n 
C 1 287 LEU 287 303 303 LEU LEU C . n 
C 1 288 TYR 288 304 304 TYR TYR C . n 
C 1 289 VAL 289 305 305 VAL VAL C . n 
C 1 290 VAL 290 306 306 VAL VAL C . n 
C 1 291 GLY 291 307 307 GLY GLY C . n 
C 1 292 GLY 292 308 308 GLY GLY C . n 
C 1 293 SER 293 309 309 SER SER C . n 
C 1 294 ILE 294 310 310 ILE ILE C . n 
C 1 295 PRO 295 311 311 PRO PRO C . n 
C 1 296 ARG 296 312 312 ARG ARG C . n 
C 1 297 PRO 297 313 313 PRO PRO C . n 
C 1 298 ARG 298 314 314 ARG ARG C . n 
C 1 299 ARG 299 315 315 ARG ARG C . n 
C 1 300 MET 300 316 316 MET MET C . n 
C 1 301 TRP 301 317 317 TRP TRP C . n 
C 1 302 LYS 302 318 318 LYS LYS C . n 
C 1 303 CYS 303 319 319 CYS CYS C . n 
C 1 304 ASN 304 320 320 ASN ASN C . n 
C 1 305 ASN 305 321 ?   ?   ?   C . n 
C 1 306 ALA 306 322 ?   ?   ?   C . n 
C 1 307 THR 307 323 ?   ?   ?   C . n 
C 1 308 VAL 308 324 324 VAL VAL C . n 
C 1 309 ASP 309 325 325 ASP ASP C . n 
C 1 310 TRP 310 326 326 TRP TRP C . n 
C 1 311 GLU 311 327 327 GLU GLU C . n 
C 1 312 TRP 312 328 328 TRP TRP C . n 
C 1 313 CYS 313 329 329 CYS CYS C . n 
C 1 314 ALA 314 330 330 ALA ALA C . n 
C 1 315 PRO 315 331 331 PRO PRO C . n 
C 1 316 LEU 316 332 332 LEU LEU C . n 
C 1 317 PRO 317 333 333 PRO PRO C . n 
C 1 318 ARG 318 334 334 ARG ARG C . n 
C 1 319 ASP 319 335 335 ASP ASP C . n 
C 1 320 ARG 320 336 336 ARG ARG C . n 
C 1 321 LEU 321 337 337 LEU LEU C . n 
C 1 322 GLN 322 338 338 GLN GLN C . n 
C 1 323 HIS 323 339 339 HIS HIS C . n 
C 1 324 THR 324 340 340 THR THR C . n 
C 1 325 LEU 325 341 341 LEU LEU C . n 
C 1 326 VAL 326 342 342 VAL VAL C . n 
C 1 327 SER 327 343 343 SER SER C . n 
C 1 328 VAL 328 344 344 VAL VAL C . n 
C 1 329 PRO 329 345 345 PRO PRO C . n 
C 1 330 GLY 330 346 346 GLY GLY C . n 
C 1 331 LYS 331 347 347 LYS LYS C . n 
C 1 332 ASP 332 348 348 ASP ASP C . n 
C 1 333 ALA 333 349 349 ALA ALA C . n 
C 1 334 ILE 334 350 350 ILE ILE C . n 
C 1 335 TYR 335 351 351 TYR TYR C . n 
C 1 336 SER 336 352 352 SER SER C . n 
C 1 337 LEU 337 353 353 LEU LEU C . n 
C 1 338 GLY 338 354 354 GLY GLY C . n 
C 1 339 GLY 339 355 355 GLY GLY C . n 
C 1 340 LYS 340 356 356 LYS LYS C . n 
C 1 341 THR 341 357 357 THR THR C . n 
C 1 342 LEU 342 358 358 LEU LEU C . n 
C 1 343 GLN 343 359 359 GLN GLN C . n 
C 1 344 ASP 344 360 360 ASP ASP C . n 
C 1 345 THR 345 361 361 THR THR C . n 
C 1 346 LEU 346 362 362 LEU LEU C . n 
C 1 347 SER 347 363 363 SER SER C . n 
C 1 348 ASN 348 364 364 ASN ASN C . n 
C 1 349 ALA 349 365 365 ALA ALA C . n 
C 1 350 VAL 350 366 366 VAL VAL C . n 
C 1 351 ILE 351 367 367 ILE ILE C . n 
C 1 352 TYR 352 368 368 TYR TYR C . n 
C 1 353 TYR 353 369 369 TYR TYR C . n 
C 1 354 ARG 354 370 370 ARG ARG C . n 
C 1 355 VAL 355 371 371 VAL VAL C . n 
C 1 356 GLY 356 372 372 GLY GLY C . n 
C 1 357 ASP 357 373 373 ASP ASP C . n 
C 1 358 ASN 358 374 374 ASN ASN C . n 
C 1 359 VAL 359 375 375 VAL VAL C . n 
C 1 360 TRP 360 376 376 TRP TRP C . n 
C 1 361 THR 361 377 377 THR THR C . n 
C 1 362 GLU 362 378 378 GLU GLU C . n 
C 1 363 THR 363 379 379 THR THR C . n 
C 1 364 THR 364 380 380 THR THR C . n 
C 1 365 GLN 365 381 381 GLN GLN C . n 
C 1 366 LEU 366 382 382 LEU LEU C . n 
C 1 367 GLU 367 383 383 GLU GLU C . n 
C 1 368 VAL 368 384 384 VAL VAL C . n 
C 1 369 ALA 369 385 385 ALA ALA C . n 
C 1 370 VAL 370 386 386 VAL VAL C . n 
C 1 371 SER 371 387 387 SER SER C . n 
C 1 372 GLY 372 388 388 GLY GLY C . n 
C 1 373 ALA 373 389 389 ALA ALA C . n 
C 1 374 ALA 374 390 390 ALA ALA C . n 
C 1 375 GLY 375 391 391 GLY GLY C . n 
C 1 376 ALA 376 392 392 ALA ALA C . n 
C 1 377 ASN 377 393 393 ASN ASN C . n 
C 1 378 LEU 378 394 394 LEU LEU C . n 
C 1 379 ASN 379 395 395 ASN ASN C . n 
C 1 380 GLY 380 396 396 GLY GLY C . n 
C 1 381 ILE 381 397 397 ILE ILE C . n 
C 1 382 ILE 382 398 398 ILE ILE C . n 
C 1 383 TYR 383 399 399 TYR TYR C . n 
C 1 384 LEU 384 400 400 LEU LEU C . n 
C 1 385 LEU 385 401 401 LEU LEU C . n 
C 1 386 GLY 386 402 402 GLY GLY C . n 
C 1 387 GLY 387 403 403 GLY GLY C . n 
C 1 388 GLU 388 404 404 GLU GLU C . n 
C 1 389 GLU 389 405 405 GLU GLU C . n 
C 1 390 ASN 390 406 406 ASN ASN C . n 
C 1 391 ASP 391 407 407 ASP ASP C . n 
C 1 392 LEU 392 408 408 LEU LEU C . n 
C 1 393 ASP 393 409 409 ASP ASP C . n 
C 1 394 PHE 394 410 410 PHE PHE C . n 
C 1 395 PHE 395 411 411 PHE PHE C . n 
C 1 396 THR 396 412 412 THR THR C . n 
C 1 397 LYS 397 413 413 LYS LYS C . n 
C 1 398 PRO 398 414 414 PRO PRO C . n 
C 1 399 SER 399 415 415 SER SER C . n 
C 1 400 ARG 400 416 416 ARG ARG C . n 
C 1 401 LEU 401 417 417 LEU LEU C . n 
C 1 402 ILE 402 418 418 ILE ILE C . n 
C 1 403 GLN 403 419 419 GLN GLN C . n 
C 1 404 CYS 404 420 420 CYS CYS C . n 
C 1 405 PHE 405 421 421 PHE PHE C . n 
C 1 406 ASP 406 422 422 ASP ASP C . n 
C 1 407 THR 407 423 423 THR THR C . n 
C 1 408 GLU 408 424 424 GLU GLU C . n 
C 1 409 THR 409 425 425 THR THR C . n 
C 1 410 ASP 410 426 426 ASP ASP C . n 
C 1 411 LYS 411 427 427 LYS LYS C . n 
C 1 412 CYS 412 428 428 CYS CYS C . n 
C 1 413 HIS 413 429 429 HIS HIS C . n 
C 1 414 VAL 414 430 430 VAL VAL C . n 
C 1 415 LYS 415 431 431 LYS LYS C . n 
C 1 416 PRO 416 432 432 PRO PRO C . n 
C 1 417 TYR 417 433 433 TYR TYR C . n 
C 1 418 VAL 418 434 434 VAL VAL C . n 
C 1 419 LEU 419 435 435 LEU LEU C . n 
C 1 420 PRO 420 436 436 PRO PRO C . n 
C 1 421 PHE 421 437 437 PHE PHE C . n 
C 1 422 ALA 422 438 438 ALA ALA C . n 
C 1 423 GLY 423 439 439 GLY GLY C . n 
C 1 424 ARG 424 440 440 ARG ARG C . n 
C 1 425 MET 425 441 441 MET MET C . n 
C 1 426 HIS 426 442 442 HIS HIS C . n 
C 1 427 ALA 427 443 443 ALA ALA C . n 
C 1 428 ALA 428 444 444 ALA ALA C . n 
C 1 429 VAL 429 445 445 VAL VAL C . n 
C 1 430 HIS 430 446 446 HIS HIS C . n 
C 1 431 LYS 431 447 447 LYS LYS C . n 
C 1 432 ASP 432 448 448 ASP ASP C . n 
C 1 433 LEU 433 449 449 LEU LEU C . n 
C 1 434 VAL 434 450 450 VAL VAL C . n 
C 1 435 PHE 435 451 451 PHE PHE C . n 
C 1 436 ILE 436 452 452 ILE ILE C . n 
C 1 437 VAL 437 453 453 VAL VAL C . n 
C 1 438 ALA 438 454 454 ALA ALA C . n 
C 1 439 GLU 439 455 455 GLU GLU C . n 
C 1 440 GLY 440 456 456 GLY GLY C . n 
C 1 441 ASP 441 457 457 ASP ASP C . n 
C 1 442 SER 442 458 458 SER SER C . n 
C 1 443 LEU 443 459 459 LEU LEU C . n 
C 1 444 VAL 444 460 460 VAL VAL C . n 
C 1 445 CYS 445 461 461 CYS CYS C . n 
C 1 446 TYR 446 462 462 TYR TYR C . n 
C 1 447 ASN 447 463 463 ASN ASN C . n 
C 1 448 PRO 448 464 464 PRO PRO C . n 
C 1 449 LEU 449 465 465 LEU LEU C . n 
C 1 450 LEU 450 466 466 LEU LEU C . n 
C 1 451 ASP 451 467 467 ASP ASP C . n 
C 1 452 SER 452 468 468 SER SER C . n 
C 1 453 PHE 453 469 469 PHE PHE C . n 
C 1 454 THR 454 470 470 THR THR C . n 
C 1 455 ARG 455 471 471 ARG ARG C . n 
C 1 456 LEU 456 472 472 LEU LEU C . n 
C 1 457 CYS 457 473 473 CYS CYS C . n 
C 1 458 LEU 458 474 474 LEU LEU C . n 
C 1 459 PRO 459 475 475 PRO PRO C . n 
C 1 460 GLU 460 476 476 GLU GLU C . n 
C 1 461 ALA 461 477 477 ALA ALA C . n 
C 1 462 TRP 462 478 ?   ?   ?   C . n 
C 1 463 SER 463 479 ?   ?   ?   C . n 
C 1 464 SER 464 480 ?   ?   ?   C . n 
C 1 465 ALA 465 481 ?   ?   ?   C . n 
C 1 466 PRO 466 482 ?   ?   ?   C . n 
C 1 467 SER 467 483 ?   ?   ?   C . n 
C 1 468 LEU 468 484 484 LEU LEU C . n 
C 1 469 TRP 469 485 485 TRP TRP C . n 
C 1 470 LYS 470 486 486 LYS LYS C . n 
C 1 471 ILE 471 487 487 ILE ILE C . n 
C 1 472 ALA 472 488 488 ALA ALA C . n 
C 1 473 SER 473 489 489 SER SER C . n 
C 1 474 CYS 474 490 490 CYS CYS C . n 
C 1 475 ASN 475 491 491 ASN ASN C . n 
C 1 476 GLY 476 492 492 GLY GLY C . n 
C 1 477 SER 477 493 493 SER SER C . n 
C 1 478 ILE 478 494 494 ILE ILE C . n 
C 1 479 TYR 479 495 495 TYR TYR C . n 
C 1 480 VAL 480 496 496 VAL VAL C . n 
C 1 481 PHE 481 497 497 PHE PHE C . n 
C 1 482 ARG 482 498 498 ARG ARG C . n 
C 1 483 ASP 483 499 499 ASP ASP C . n 
C 1 484 ARG 484 500 500 ARG ARG C . n 
C 1 485 TYR 485 501 501 TYR TYR C . n 
C 1 486 LYS 486 502 ?   ?   ?   C . n 
C 1 487 LYS 487 503 ?   ?   ?   C . n 
C 1 488 GLY 488 504 ?   ?   ?   C . n 
C 1 489 ASP 489 505 ?   ?   ?   C . n 
C 1 490 ALA 490 506 506 ALA ALA C . n 
C 1 491 ASN 491 507 507 ASN ASN C . n 
C 1 492 THR 492 508 508 THR THR C . n 
C 1 493 TYR 493 509 509 TYR TYR C . n 
C 1 494 LYS 494 510 510 LYS LYS C . n 
C 1 495 LEU 495 511 511 LEU LEU C . n 
C 1 496 ASP 496 512 512 ASP ASP C . n 
C 1 497 PRO 497 513 513 PRO PRO C . n 
C 1 498 ALA 498 514 514 ALA ALA C . n 
C 1 499 THR 499 515 515 THR THR C . n 
C 1 500 SER 500 516 516 SER SER C . n 
C 1 501 ALA 501 517 517 ALA ALA C . n 
C 1 502 VAL 502 518 518 VAL VAL C . n 
C 1 503 THR 503 519 519 THR THR C . n 
C 1 504 VAL 504 520 520 VAL VAL C . n 
C 1 505 THR 505 521 521 THR THR C . n 
C 1 506 ARG 506 522 ?   ?   ?   C . n 
C 1 507 GLY 507 523 ?   ?   ?   C . n 
C 1 508 ILE 508 524 ?   ?   ?   C . n 
C 1 509 LYS 509 525 525 LYS LYS C . n 
C 1 510 VAL 510 526 526 VAL VAL C . n 
C 1 511 LEU 511 527 527 LEU LEU C . n 
C 1 512 LEU 512 528 528 LEU LEU C . n 
C 1 513 THR 513 529 529 THR THR C . n 
C 1 514 ASN 514 530 530 ASN ASN C . n 
C 1 515 LEU 515 531 531 LEU LEU C . n 
C 1 516 GLN 516 532 532 GLN GLN C . n 
C 1 517 PHE 517 533 533 PHE PHE C . n 
C 1 518 VAL 518 534 534 VAL VAL C . n 
C 1 519 LEU 519 535 535 LEU LEU C . n 
C 1 520 ALA 520 536 536 ALA ALA C . n 
D 2 1   MET 1   1   ?   ?   ?   B . n 
D 2 2   ALA 2   2   ?   ?   ?   B . n 
D 2 3   TYR 3   3   ?   ?   ?   B . n 
D 2 4   SER 4   4   ?   ?   ?   B . n 
D 2 5   GLN 5   5   ?   ?   ?   B . n 
D 2 6   GLY 6   6   ?   ?   ?   B . n 
D 2 7   GLY 7   7   ?   ?   ?   B . n 
D 2 8   GLY 8   8   ?   ?   ?   B . n 
D 2 9   LYS 9   9   9   LYS LYS B . n 
D 2 10  LYS 10  10  10  LYS LYS B . n 
D 2 11  LYS 11  11  11  LYS LYS B . n 
D 2 12  VAL 12  12  12  VAL VAL B . n 
D 2 13  CYS 13  13  13  CYS CYS B . n 
D 2 14  TYR 14  14  14  TYR TYR B . n 
D 2 15  TYR 15  15  15  TYR TYR B . n 
D 2 16  TYR 16  16  16  TYR TYR B . n 
D 2 17  ASP 17  17  17  ASP ASP B . n 
D 2 18  GLY 18  18  18  GLY GLY B . n 
D 2 19  ASP 19  19  19  ASP ASP B . n 
D 2 20  ILE 20  20  20  ILE ILE B . n 
D 2 21  GLY 21  21  21  GLY GLY B . n 
D 2 22  ASN 22  22  22  ASN ASN B . n 
D 2 23  TYR 23  23  23  TYR TYR B . n 
D 2 24  TYR 24  24  24  TYR TYR B . n 
D 2 25  TYR 25  25  25  TYR TYR B . n 
D 2 26  GLY 26  26  26  GLY GLY B . n 
D 2 27  GLN 27  27  27  GLN GLN B . n 
D 2 28  GLY 28  28  28  GLY GLY B . n 
D 2 29  HIS 29  29  29  HIS HIS B . n 
D 2 30  PRO 30  30  30  PRO PRO B . n 
D 2 31  MET 31  31  31  MET MET B . n 
D 2 32  LYS 32  32  32  LYS LYS B . n 
D 2 33  PRO 33  33  33  PRO PRO B . n 
D 2 34  HIS 34  34  34  HIS HIS B . n 
D 2 35  ARG 35  35  35  ARG ARG B . n 
D 2 36  ILE 36  36  36  ILE ILE B . n 
D 2 37  ARG 37  37  37  ARG ARG B . n 
D 2 38  MET 38  38  38  MET MET B . n 
D 2 39  THR 39  39  39  THR THR B . n 
D 2 40  HIS 40  40  40  HIS HIS B . n 
D 2 41  ASN 41  41  41  ASN ASN B . n 
D 2 42  LEU 42  42  42  LEU LEU B . n 
D 2 43  LEU 43  43  43  LEU LEU B . n 
D 2 44  LEU 44  44  44  LEU LEU B . n 
D 2 45  ASN 45  45  45  ASN ASN B . n 
D 2 46  TYR 46  46  46  TYR TYR B . n 
D 2 47  GLY 47  47  47  GLY GLY B . n 
D 2 48  LEU 48  48  48  LEU LEU B . n 
D 2 49  TYR 49  49  49  TYR TYR B . n 
D 2 50  ARG 50  50  50  ARG ARG B . n 
D 2 51  LYS 51  51  51  LYS LYS B . n 
D 2 52  MET 52  52  52  MET MET B . n 
D 2 53  GLU 53  53  53  GLU GLU B . n 
D 2 54  ILE 54  54  54  ILE ILE B . n 
D 2 55  TYR 55  55  55  TYR TYR B . n 
D 2 56  ARG 56  56  56  ARG ARG B . n 
D 2 57  PRO 57  57  57  PRO PRO B . n 
D 2 58  HIS 58  58  58  HIS HIS B . n 
D 2 59  LYS 59  59  59  LYS LYS B . n 
D 2 60  ALA 60  60  60  ALA ALA B . n 
D 2 61  THR 61  61  61  THR THR B . n 
D 2 62  ALA 62  62  62  ALA ALA B . n 
D 2 63  GLU 63  63  63  GLU GLU B . n 
D 2 64  GLU 64  64  64  GLU GLU B . n 
D 2 65  MET 65  65  65  MET MET B . n 
D 2 66  THR 66  66  66  THR THR B . n 
D 2 67  LYS 67  67  67  LYS LYS B . n 
D 2 68  TYR 68  68  68  TYR TYR B . n 
D 2 69  HIS 69  69  69  HIS HIS B . n 
D 2 70  SER 70  70  70  SER SER B . n 
D 2 71  ASP 71  71  71  ASP ASP B . n 
D 2 72  GLU 72  72  72  GLU GLU B . n 
D 2 73  TYR 73  73  73  TYR TYR B . n 
D 2 74  ILE 74  74  74  ILE ILE B . n 
D 2 75  LYS 75  75  75  LYS LYS B . n 
D 2 76  PHE 76  76  76  PHE PHE B . n 
D 2 77  LEU 77  77  77  LEU LEU B . n 
D 2 78  ARG 78  78  78  ARG ARG B . n 
D 2 79  SER 79  79  79  SER SER B . n 
D 2 80  ILE 80  80  80  ILE ILE B . n 
D 2 81  ARG 81  81  81  ARG ARG B . n 
D 2 82  PRO 82  82  82  PRO PRO B . n 
D 2 83  ASP 83  83  83  ASP ASP B . n 
D 2 84  ASN 84  84  84  ASN ASN B . n 
D 2 85  MET 85  85  85  MET MET B . n 
D 2 86  SER 86  86  86  SER SER B . n 
D 2 87  GLU 87  87  87  GLU GLU B . n 
D 2 88  TYR 88  88  88  TYR TYR B . n 
D 2 89  SER 89  89  89  SER SER B . n 
D 2 90  LYS 90  90  90  LYS LYS B . n 
D 2 91  GLN 91  91  91  GLN GLN B . n 
D 2 92  MET 92  92  92  MET MET B . n 
D 2 93  GLN 93  93  93  GLN GLN B . n 
D 2 94  ARG 94  94  94  ARG ARG B . n 
D 2 95  PHE 95  95  95  PHE PHE B . n 
D 2 96  ASN 96  96  96  ASN ASN B . n 
D 2 97  VAL 97  97  97  VAL VAL B . n 
D 2 98  GLY 98  98  98  GLY GLY B . n 
D 2 99  GLU 99  99  99  GLU GLU B . n 
D 2 100 ASP 100 100 100 ASP ASP B . n 
D 2 101 CYS 101 101 101 CYS CYS B . n 
D 2 102 PRO 102 102 102 PRO PRO B . n 
D 2 103 VAL 103 103 103 VAL VAL B . n 
D 2 104 PHE 104 104 104 PHE PHE B . n 
D 2 105 ASP 105 105 105 ASP ASP B . n 
D 2 106 GLY 106 106 106 GLY GLY B . n 
D 2 107 LEU 107 107 107 LEU LEU B . n 
D 2 108 PHE 108 108 108 PHE PHE B . n 
D 2 109 GLU 109 109 109 GLU GLU B . n 
D 2 110 PHE 110 110 110 PHE PHE B . n 
D 2 111 CYS 111 111 111 CYS CYS B . n 
D 2 112 GLN 112 112 112 GLN GLN B . n 
D 2 113 LEU 113 113 113 LEU LEU B . n 
D 2 114 SER 114 114 114 SER SER B . n 
D 2 115 THR 115 115 115 THR THR B . n 
D 2 116 GLY 116 116 116 GLY GLY B . n 
D 2 117 GLY 117 117 117 GLY GLY B . n 
D 2 118 SER 118 118 118 SER SER B . n 
D 2 119 VAL 119 119 119 VAL VAL B . n 
D 2 120 ALA 120 120 120 ALA ALA B . n 
D 2 121 GLY 121 121 121 GLY GLY B . n 
D 2 122 ALA 122 122 122 ALA ALA B . n 
D 2 123 VAL 123 123 123 VAL VAL B . n 
D 2 124 LYS 124 124 124 LYS LYS B . n 
D 2 125 LEU 125 125 125 LEU LEU B . n 
D 2 126 ASN 126 126 126 ASN ASN B . n 
D 2 127 ARG 127 127 127 ARG ARG B . n 
D 2 128 GLN 128 128 128 GLN GLN B . n 
D 2 129 GLN 129 129 129 GLN GLN B . n 
D 2 130 THR 130 130 130 THR THR B . n 
D 2 131 ASP 131 131 131 ASP ASP B . n 
D 2 132 MET 132 132 132 MET MET B . n 
D 2 133 ALA 133 133 133 ALA ALA B . n 
D 2 134 VAL 134 134 134 VAL VAL B . n 
D 2 135 ASN 135 135 135 ASN ASN B . n 
D 2 136 TRP 136 136 136 TRP TRP B . n 
D 2 137 ALA 137 137 137 ALA ALA B . n 
D 2 138 GLY 138 138 138 GLY GLY B . n 
D 2 139 GLY 139 139 139 GLY GLY B . n 
D 2 140 LEU 140 140 140 LEU LEU B . n 
D 2 141 HIS 141 141 141 HIS HIS B . n 
D 2 142 HIS 142 142 142 HIS HIS B . n 
D 2 143 ALA 143 143 143 ALA ALA B . n 
D 2 144 LYS 144 144 144 LYS LYS B . n 
D 2 145 LYS 145 145 145 LYS LYS B . n 
D 2 146 SER 146 146 146 SER SER B . n 
D 2 147 GLU 147 147 147 GLU GLU B . n 
D 2 148 ALA 148 148 148 ALA ALA B . n 
D 2 149 SER 149 149 149 SER SER B . n 
D 2 150 GLY 150 150 150 GLY GLY B . n 
D 2 151 PHE 151 151 151 PHE PHE B . n 
D 2 152 CYS 152 152 152 CYS CYS B . n 
D 2 153 TYR 153 153 153 TYR TYR B . n 
D 2 154 VAL 154 154 154 VAL VAL B . n 
D 2 155 ASN 155 155 155 ASN ASN B . n 
D 2 156 ASP 156 156 156 ASP ASP B . n 
D 2 157 ILE 157 157 157 ILE ILE B . n 
D 2 158 VAL 158 158 158 VAL VAL B . n 
D 2 159 LEU 159 159 159 LEU LEU B . n 
D 2 160 ALA 160 160 160 ALA ALA B . n 
D 2 161 ILE 161 161 161 ILE ILE B . n 
D 2 162 LEU 162 162 162 LEU LEU B . n 
D 2 163 GLU 163 163 163 GLU GLU B . n 
D 2 164 LEU 164 164 164 LEU LEU B . n 
D 2 165 LEU 165 165 165 LEU LEU B . n 
D 2 166 LYS 166 166 166 LYS LYS B . n 
D 2 167 TYR 167 167 167 TYR TYR B . n 
D 2 168 HIS 168 168 168 HIS HIS B . n 
D 2 169 GLN 169 169 169 GLN GLN B . n 
D 2 170 ARG 170 170 170 ARG ARG B . n 
D 2 171 VAL 171 171 171 VAL VAL B . n 
D 2 172 LEU 172 172 172 LEU LEU B . n 
D 2 173 TYR 173 173 173 TYR TYR B . n 
D 2 174 ILE 174 174 174 ILE ILE B . n 
D 2 175 ASP 175 175 175 ASP ASP B . n 
D 2 176 ILE 176 176 176 ILE ILE B . n 
D 2 177 ASP 177 177 177 ASP ASP B . n 
D 2 178 ILE 178 178 178 ILE ILE B . n 
D 2 179 HIS 179 179 179 HIS HIS B . n 
D 2 180 HIS 180 180 180 HIS HIS B . n 
D 2 181 GLY 181 181 181 GLY GLY B . n 
D 2 182 ASP 182 182 182 ASP ASP B . n 
D 2 183 GLY 183 183 183 GLY GLY B . n 
D 2 184 VAL 184 184 184 VAL VAL B . n 
D 2 185 GLU 185 185 185 GLU GLU B . n 
D 2 186 GLU 186 186 186 GLU GLU B . n 
D 2 187 ALA 187 187 187 ALA ALA B . n 
D 2 188 PHE 188 188 188 PHE PHE B . n 
D 2 189 TYR 189 189 189 TYR TYR B . n 
D 2 190 THR 190 190 190 THR THR B . n 
D 2 191 THR 191 191 191 THR THR B . n 
D 2 192 ASP 192 192 192 ASP ASP B . n 
D 2 193 ARG 193 193 193 ARG ARG B . n 
D 2 194 VAL 194 194 194 VAL VAL B . n 
D 2 195 MET 195 195 195 MET MET B . n 
D 2 196 THR 196 196 196 THR THR B . n 
D 2 197 VAL 197 197 197 VAL VAL B . n 
D 2 198 SER 198 198 198 SER SER B . n 
D 2 199 PHE 199 199 199 PHE PHE B . n 
D 2 200 HIS 200 200 200 HIS HIS B . n 
D 2 201 LYS 201 201 201 LYS LYS B . n 
D 2 202 TYR 202 202 202 TYR TYR B . n 
D 2 203 GLY 203 203 203 GLY GLY B . n 
D 2 204 GLU 204 204 204 GLU GLU B . n 
D 2 205 TYR 205 205 205 TYR TYR B . n 
D 2 206 PHE 206 206 206 PHE PHE B . n 
D 2 207 PRO 207 207 207 PRO PRO B . n 
D 2 208 GLY 208 208 208 GLY GLY B . n 
D 2 209 THR 209 209 209 THR THR B . n 
D 2 210 GLY 210 210 210 GLY GLY B . n 
D 2 211 ASP 211 211 211 ASP ASP B . n 
D 2 212 LEU 212 212 212 LEU LEU B . n 
D 2 213 ARG 213 213 213 ARG ARG B . n 
D 2 214 ASP 214 214 214 ASP ASP B . n 
D 2 215 ILE 215 215 215 ILE ILE B . n 
D 2 216 GLY 216 216 216 GLY GLY B . n 
D 2 217 ALA 217 217 217 ALA ALA B . n 
D 2 218 GLY 218 218 218 GLY GLY B . n 
D 2 219 LYS 219 219 219 LYS LYS B . n 
D 2 220 GLY 220 220 220 GLY GLY B . n 
D 2 221 LYS 221 221 221 LYS LYS B . n 
D 2 222 TYR 222 222 222 TYR TYR B . n 
D 2 223 TYR 223 223 223 TYR TYR B . n 
D 2 224 ALA 224 224 224 ALA ALA B . n 
D 2 225 VAL 225 225 225 VAL VAL B . n 
D 2 226 ASN 226 226 226 ASN ASN B . n 
D 2 227 PHE 227 227 227 PHE PHE B . n 
D 2 228 PRO 228 228 228 PRO PRO B . n 
D 2 229 MET 229 229 229 MET MET B . n 
D 2 230 ARG 230 230 230 ARG ARG B . n 
D 2 231 ASP 231 231 231 ASP ASP B . n 
D 2 232 GLY 232 232 232 GLY GLY B . n 
D 2 233 ILE 233 233 233 ILE ILE B . n 
D 2 234 ASP 234 234 234 ASP ASP B . n 
D 2 235 ASP 235 235 235 ASP ASP B . n 
D 2 236 GLU 236 236 236 GLU GLU B . n 
D 2 237 SER 237 237 237 SER SER B . n 
D 2 238 TYR 238 238 238 TYR TYR B . n 
D 2 239 GLY 239 239 239 GLY GLY B . n 
D 2 240 GLN 240 240 240 GLN GLN B . n 
D 2 241 ILE 241 241 241 ILE ILE B . n 
D 2 242 PHE 242 242 242 PHE PHE B . n 
D 2 243 LYS 243 243 243 LYS LYS B . n 
D 2 244 PRO 244 244 244 PRO PRO B . n 
D 2 245 ILE 245 245 245 ILE ILE B . n 
D 2 246 ILE 246 246 246 ILE ILE B . n 
D 2 247 SER 247 247 247 SER SER B . n 
D 2 248 LYS 248 248 248 LYS LYS B . n 
D 2 249 VAL 249 249 249 VAL VAL B . n 
D 2 250 MET 250 250 250 MET MET B . n 
D 2 251 GLU 251 251 251 GLU GLU B . n 
D 2 252 MET 252 252 252 MET MET B . n 
D 2 253 TYR 253 253 253 TYR TYR B . n 
D 2 254 GLN 254 254 254 GLN GLN B . n 
D 2 255 PRO 255 255 255 PRO PRO B . n 
D 2 256 SER 256 256 256 SER SER B . n 
D 2 257 ALA 257 257 257 ALA ALA B . n 
D 2 258 VAL 258 258 258 VAL VAL B . n 
D 2 259 VAL 259 259 259 VAL VAL B . n 
D 2 260 LEU 260 260 260 LEU LEU B . n 
D 2 261 GLN 261 261 261 GLN GLN B . n 
D 2 262 CYS 262 262 262 CYS CYS B . n 
D 2 263 GLY 263 263 263 GLY GLY B . n 
D 2 264 ALA 264 264 264 ALA ALA B . n 
D 2 265 ASP 265 265 265 ASP ASP B . n 
D 2 266 SER 266 266 266 SER SER B . n 
D 2 267 LEU 267 267 267 LEU LEU B . n 
D 2 268 SER 268 268 268 SER SER B . n 
D 2 269 GLY 269 269 269 GLY GLY B . n 
D 2 270 ASP 270 270 270 ASP ASP B . n 
D 2 271 ARG 271 271 271 ARG ARG B . n 
D 2 272 LEU 272 272 272 LEU LEU B . n 
D 2 273 GLY 273 273 273 GLY GLY B . n 
D 2 274 CYS 274 274 274 CYS CYS B . n 
D 2 275 PHE 275 275 275 PHE PHE B . n 
D 2 276 ASN 276 276 276 ASN ASN B . n 
D 2 277 LEU 277 277 277 LEU LEU B . n 
D 2 278 THR 278 278 278 THR THR B . n 
D 2 279 VAL 279 279 279 VAL VAL B . n 
D 2 280 LYS 280 280 280 LYS LYS B . n 
D 2 281 GLY 281 281 281 GLY GLY B . n 
D 2 282 HIS 282 282 282 HIS HIS B . n 
D 2 283 ALA 283 283 283 ALA ALA B . n 
D 2 284 LYS 284 284 284 LYS LYS B . n 
D 2 285 CYS 285 285 285 CYS CYS B . n 
D 2 286 VAL 286 286 286 VAL VAL B . n 
D 2 287 GLU 287 287 287 GLU GLU B . n 
D 2 288 VAL 288 288 288 VAL VAL B . n 
D 2 289 VAL 289 289 289 VAL VAL B . n 
D 2 290 LYS 290 290 290 LYS LYS B . n 
D 2 291 THR 291 291 291 THR THR B . n 
D 2 292 PHE 292 292 292 PHE PHE B . n 
D 2 293 ASN 293 293 293 ASN ASN B . n 
D 2 294 LEU 294 294 294 LEU LEU B . n 
D 2 295 PRO 295 295 295 PRO PRO B . n 
D 2 296 LEU 296 296 296 LEU LEU B . n 
D 2 297 LEU 297 297 297 LEU LEU B . n 
D 2 298 MET 298 298 298 MET MET B . n 
D 2 299 LEU 299 299 299 LEU LEU B . n 
D 2 300 GLY 300 300 300 GLY GLY B . n 
D 2 301 GLY 301 301 301 GLY GLY B . n 
D 2 302 GLY 302 302 302 GLY GLY B . n 
D 2 303 GLY 303 303 303 GLY GLY B . n 
D 2 304 TYR 304 304 304 TYR TYR B . n 
D 2 305 THR 305 305 305 THR THR B . n 
D 2 306 ILE 306 306 306 ILE ILE B . n 
D 2 307 ARG 307 307 307 ARG ARG B . n 
D 2 308 ASN 308 308 308 ASN ASN B . n 
D 2 309 VAL 309 309 309 VAL VAL B . n 
D 2 310 ALA 310 310 310 ALA ALA B . n 
D 2 311 ARG 311 311 311 ARG ARG B . n 
D 2 312 CYS 312 312 312 CYS CYS B . n 
D 2 313 TRP 313 313 313 TRP TRP B . n 
D 2 314 THR 314 314 314 THR THR B . n 
D 2 315 TYR 315 315 315 TYR TYR B . n 
D 2 316 GLU 316 316 316 GLU GLU B . n 
D 2 317 THR 317 317 317 THR THR B . n 
D 2 318 ALA 318 318 318 ALA ALA B . n 
D 2 319 VAL 319 319 319 VAL VAL B . n 
D 2 320 ALA 320 320 320 ALA ALA B . n 
D 2 321 LEU 321 321 321 LEU LEU B . n 
D 2 322 ASP 322 322 322 ASP ASP B . n 
D 2 323 CYS 323 323 323 CYS CYS B . n 
D 2 324 GLU 324 324 324 GLU GLU B . n 
D 2 325 ILE 325 325 325 ILE ILE B . n 
D 2 326 PRO 326 326 326 PRO PRO B . n 
D 2 327 ASN 327 327 327 ASN ASN B . n 
D 2 328 GLU 328 328 328 GLU GLU B . n 
D 2 329 LEU 329 329 329 LEU LEU B . n 
D 2 330 PRO 330 330 330 PRO PRO B . n 
D 2 331 TYR 331 331 331 TYR TYR B . n 
D 2 332 ASN 332 332 332 ASN ASN B . n 
D 2 333 ASP 333 333 333 ASP ASP B . n 
D 2 334 TYR 334 334 334 TYR TYR B . n 
D 2 335 PHE 335 335 335 PHE PHE B . n 
D 2 336 GLU 336 336 336 GLU GLU B . n 
D 2 337 TYR 337 337 337 TYR TYR B . n 
D 2 338 PHE 338 338 338 PHE PHE B . n 
D 2 339 GLY 339 339 339 GLY GLY B . n 
D 2 340 PRO 340 340 340 PRO PRO B . n 
D 2 341 ASP 341 341 341 ASP ASP B . n 
D 2 342 PHE 342 342 342 PHE PHE B . n 
D 2 343 LYS 343 343 343 LYS LYS B . n 
D 2 344 LEU 344 344 344 LEU LEU B . n 
D 2 345 HIS 345 345 345 HIS HIS B . n 
D 2 346 ILE 346 346 346 ILE ILE B . n 
D 2 347 SER 347 347 347 SER SER B . n 
D 2 348 PRO 348 348 348 PRO PRO B . n 
D 2 349 SER 349 349 349 SER SER B . n 
D 2 350 ASN 350 350 350 ASN ASN B . n 
D 2 351 MET 351 351 351 MET MET B . n 
D 2 352 THR 352 352 352 THR THR B . n 
D 2 353 ASN 353 353 353 ASN ASN B . n 
D 2 354 GLN 354 354 354 GLN GLN B . n 
D 2 355 ASN 355 355 355 ASN ASN B . n 
D 2 356 THR 356 356 356 THR THR B . n 
D 2 357 PRO 357 357 357 PRO PRO B . n 
D 2 358 GLU 358 358 358 GLU GLU B . n 
D 2 359 TYR 359 359 359 TYR TYR B . n 
D 2 360 MET 360 360 360 MET MET B . n 
D 2 361 GLU 361 361 361 GLU GLU B . n 
D 2 362 LYS 362 362 362 LYS LYS B . n 
D 2 363 ILE 363 363 363 ILE ILE B . n 
D 2 364 LYS 364 364 364 LYS LYS B . n 
D 2 365 GLN 365 365 365 GLN GLN B . n 
D 2 366 ARG 366 366 366 ARG ARG B . n 
D 2 367 LEU 367 367 367 LEU LEU B . n 
D 2 368 PHE 368 368 368 PHE PHE B . n 
D 2 369 GLU 369 369 369 GLU GLU B . n 
D 2 370 ASN 370 370 370 ASN ASN B . n 
D 2 371 LEU 371 371 371 LEU LEU B . n 
D 2 372 ARG 372 372 372 ARG ARG B . n 
D 2 373 MET 373 373 373 MET MET B . n 
D 2 374 LEU 374 374 374 LEU LEU B . n 
D 2 375 PRO 375 375 375 PRO PRO B . n 
D 2 376 HIS 376 376 ?   ?   ?   B . n 
D 2 377 ALA 377 377 ?   ?   ?   B . n 
D 2 378 PRO 378 378 ?   ?   ?   B . n 
D 2 379 GLY 379 379 ?   ?   ?   B . n 
D 2 380 VAL 380 380 ?   ?   ?   B . n 
D 2 381 GLN 381 381 ?   ?   ?   B . n 
D 2 382 MET 382 382 ?   ?   ?   B . n 
D 2 383 GLN 383 383 ?   ?   ?   B . n 
D 2 384 ALA 384 384 ?   ?   ?   B . n 
D 2 385 ILE 385 385 ?   ?   ?   B . n 
D 2 386 PRO 386 386 ?   ?   ?   B . n 
D 2 387 GLU 387 387 ?   ?   ?   B . n 
D 2 388 ASP 388 388 ?   ?   ?   B . n 
D 2 389 ALA 389 389 ?   ?   ?   B . n 
D 2 390 VAL 390 390 ?   ?   ?   B . n 
D 2 391 HIS 391 391 ?   ?   ?   B . n 
D 2 392 GLU 392 392 ?   ?   ?   B . n 
D 2 393 ASP 393 393 ?   ?   ?   B . n 
D 2 394 SER 394 394 ?   ?   ?   B . n 
D 2 395 GLY 395 395 ?   ?   ?   B . n 
D 2 396 ASP 396 396 ?   ?   ?   B . n 
D 2 397 GLU 397 397 ?   ?   ?   B . n 
D 2 398 ASP 398 398 ?   ?   ?   B . n 
D 2 399 GLY 399 399 ?   ?   ?   B . n 
D 2 400 GLU 400 400 ?   ?   ?   B . n 
D 2 401 ASP 401 401 ?   ?   ?   B . n 
D 2 402 PRO 402 402 ?   ?   ?   B . n 
D 2 403 ASP 403 403 ?   ?   ?   B . n 
D 2 404 LYS 404 404 ?   ?   ?   B . n 
D 2 405 ARG 405 405 ?   ?   ?   B . n 
D 2 406 ILE 406 406 ?   ?   ?   B . n 
D 2 407 SER 407 407 ?   ?   ?   B . n 
D 2 408 ILE 408 408 ?   ?   ?   B . n 
D 2 409 ARG 409 409 ?   ?   ?   B . n 
D 2 410 ALA 410 410 ?   ?   ?   B . n 
D 2 411 SER 411 411 ?   ?   ?   B . n 
D 2 412 ASP 412 412 ?   ?   ?   B . n 
D 2 413 LYS 413 413 ?   ?   ?   B . n 
D 2 414 ARG 414 414 ?   ?   ?   B . n 
D 2 415 ILE 415 415 ?   ?   ?   B . n 
D 2 416 ALA 416 416 ?   ?   ?   B . n 
D 2 417 CYS 417 417 ?   ?   ?   B . n 
D 2 418 ASP 418 418 ?   ?   ?   B . n 
D 2 419 GLU 419 419 ?   ?   ?   B . n 
D 2 420 GLU 420 420 ?   ?   ?   B . n 
D 2 421 PHE 421 421 ?   ?   ?   B . n 
D 2 422 SER 422 422 ?   ?   ?   B . n 
D 2 423 ASP 423 423 ?   ?   ?   B . n 
D 2 424 SER 424 424 ?   ?   ?   B . n 
D 2 425 GLU 425 425 ?   ?   ?   B . n 
D 2 426 ASP 426 426 ?   ?   ?   B . n 
D 2 427 GLU 427 427 ?   ?   ?   B . n 
D 2 428 GLY 428 428 ?   ?   ?   B . n 
D 2 429 GLU 429 429 ?   ?   ?   B . n 
D 2 430 GLY 430 430 ?   ?   ?   B . n 
D 2 431 GLY 431 431 ?   ?   ?   B . n 
D 2 432 ARG 432 432 ?   ?   ?   B . n 
D 2 433 ARG 433 433 ?   ?   ?   B . n 
D 2 434 ASN 434 434 ?   ?   ?   B . n 
D 2 435 VAL 435 435 ?   ?   ?   B . n 
D 2 436 ALA 436 436 ?   ?   ?   B . n 
D 2 437 ASP 437 437 ?   ?   ?   B . n 
D 2 438 HIS 438 438 ?   ?   ?   B . n 
D 2 439 LYS 439 439 ?   ?   ?   B . n 
D 2 440 LYS 440 440 ?   ?   ?   B . n 
D 2 441 GLY 441 441 ?   ?   ?   B . n 
D 2 442 ALA 442 442 ?   ?   ?   B . n 
D 2 443 LYS 443 443 ?   ?   ?   B . n 
D 2 444 LYS 444 444 ?   ?   ?   B . n 
D 2 445 ALA 445 445 ?   ?   ?   B . n 
D 2 446 ARG 446 446 ?   ?   ?   B . n 
D 2 447 ILE 447 447 ?   ?   ?   B . n 
D 2 448 GLU 448 448 ?   ?   ?   B . n 
D 2 449 GLU 449 449 ?   ?   ?   B . n 
D 2 450 ASP 450 450 ?   ?   ?   B . n 
D 2 451 LYS 451 451 ?   ?   ?   B . n 
D 2 452 LYS 452 452 ?   ?   ?   B . n 
D 2 453 GLU 453 453 ?   ?   ?   B . n 
D 2 454 THR 454 454 ?   ?   ?   B . n 
D 2 455 GLU 455 455 ?   ?   ?   B . n 
D 2 456 ASP 456 456 ?   ?   ?   B . n 
D 2 457 LYS 457 457 ?   ?   ?   B . n 
D 2 458 LYS 458 458 ?   ?   ?   B . n 
D 2 459 THR 459 459 ?   ?   ?   B . n 
D 2 460 ASP 460 460 ?   ?   ?   B . n 
D 2 461 VAL 461 461 ?   ?   ?   B . n 
D 2 462 LYS 462 462 ?   ?   ?   B . n 
D 2 463 GLU 463 463 ?   ?   ?   B . n 
D 2 464 GLU 464 464 ?   ?   ?   B . n 
D 2 465 ASP 465 465 ?   ?   ?   B . n 
D 2 466 LYS 466 466 ?   ?   ?   B . n 
D 2 467 SER 467 467 ?   ?   ?   B . n 
D 2 468 LYS 468 468 ?   ?   ?   B . n 
D 2 469 ASP 469 469 ?   ?   ?   B . n 
D 2 470 ASN 470 470 ?   ?   ?   B . n 
D 2 471 SER 471 471 ?   ?   ?   B . n 
D 2 472 GLY 472 472 ?   ?   ?   B . n 
D 2 473 GLU 473 473 ?   ?   ?   B . n 
D 2 474 LYS 474 474 ?   ?   ?   B . n 
D 2 475 THR 475 475 ?   ?   ?   B . n 
D 2 476 ASP 476 476 ?   ?   ?   B . n 
D 2 477 THR 477 477 ?   ?   ?   B . n 
D 2 478 LYS 478 478 ?   ?   ?   B . n 
D 2 479 GLY 479 479 ?   ?   ?   B . n 
D 2 480 THR 480 480 ?   ?   ?   B . n 
D 2 481 LYS 481 481 ?   ?   ?   B . n 
D 2 482 SER 482 482 ?   ?   ?   B . n 
D 2 483 GLU 483 483 ?   ?   ?   B . n 
D 2 484 GLN 484 484 ?   ?   ?   B . n 
D 2 485 LEU 485 485 ?   ?   ?   B . n 
D 2 486 SER 486 486 ?   ?   ?   B . n 
D 2 487 ASN 487 487 ?   ?   ?   B . n 
D 2 488 PRO 488 488 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 ZN 1 501 401 ZN ZN D . 
F 3 ZN 1 501 401 ZN ZN B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1    1 Y 1 A THR 36  ? OG1 ? A THR 20  OG1 
2    1 Y 1 A THR 36  ? CG2 ? A THR 20  CG2 
3    1 Y 1 A LYS 38  ? CG  ? A LYS 22  CG  
4    1 Y 1 A LYS 38  ? CD  ? A LYS 22  CD  
5    1 Y 1 A LYS 38  ? CE  ? A LYS 22  CE  
6    1 Y 1 A LYS 38  ? NZ  ? A LYS 22  NZ  
7    1 Y 1 A ARG 40  ? CG  ? A ARG 24  CG  
8    1 Y 1 A ARG 40  ? CD  ? A ARG 24  CD  
9    1 Y 1 A ARG 40  ? NE  ? A ARG 24  NE  
10   1 Y 1 A ARG 40  ? CZ  ? A ARG 24  CZ  
11   1 Y 1 A ARG 40  ? NH1 ? A ARG 24  NH1 
12   1 Y 1 A ARG 40  ? NH2 ? A ARG 24  NH2 
13   1 Y 1 A GLN 48  ? CG  ? A GLN 32  CG  
14   1 Y 1 A GLN 48  ? CD  ? A GLN 32  CD  
15   1 Y 1 A GLN 48  ? OE1 ? A GLN 32  OE1 
16   1 Y 1 A GLN 48  ? NE2 ? A GLN 32  NE2 
17   1 Y 1 A LYS 52  ? CG  ? A LYS 36  CG  
18   1 Y 1 A LYS 52  ? CD  ? A LYS 36  CD  
19   1 Y 1 A LYS 52  ? CE  ? A LYS 36  CE  
20   1 Y 1 A LYS 52  ? NZ  ? A LYS 36  NZ  
21   1 Y 1 A LEU 55  ? CG  ? A LEU 39  CG  
22   1 Y 1 A LEU 55  ? CD1 ? A LEU 39  CD1 
23   1 Y 1 A LEU 55  ? CD2 ? A LEU 39  CD2 
24   1 Y 1 A GLU 57  ? CG  ? A GLU 41  CG  
25   1 Y 1 A GLU 57  ? CD  ? A GLU 41  CD  
26   1 Y 1 A GLU 57  ? OE1 ? A GLU 41  OE1 
27   1 Y 1 A GLU 57  ? OE2 ? A GLU 41  OE2 
28   1 Y 1 A LEU 77  ? CG  ? A LEU 61  CG  
29   1 Y 1 A LEU 77  ? CD1 ? A LEU 61  CD1 
30   1 Y 1 A LEU 77  ? CD2 ? A LEU 61  CD2 
31   1 Y 1 A VAL 78  ? CG1 ? A VAL 62  CG1 
32   1 Y 1 A VAL 78  ? CG2 ? A VAL 62  CG2 
33   1 Y 1 A LEU 79  ? CG  ? A LEU 63  CG  
34   1 Y 1 A LEU 79  ? CD1 ? A LEU 63  CD1 
35   1 Y 1 A LEU 79  ? CD2 ? A LEU 63  CD2 
36   1 Y 1 A SER 88  ? OG  ? A SER 72  OG  
37   1 Y 1 A GLN 105 ? CG  ? A GLN 89  CG  
38   1 Y 1 A GLN 105 ? CD  ? A GLN 89  CD  
39   1 Y 1 A GLN 105 ? OE1 ? A GLN 89  OE1 
40   1 Y 1 A GLN 105 ? NE2 ? A GLN 89  NE2 
41   1 Y 1 A ASP 106 ? CG  ? A ASP 90  CG  
42   1 Y 1 A ASP 106 ? OD1 ? A ASP 90  OD1 
43   1 Y 1 A ASP 106 ? OD2 ? A ASP 90  OD2 
44   1 Y 1 A GLU 109 ? CG  ? A GLU 93  CG  
45   1 Y 1 A GLU 109 ? CD  ? A GLU 93  CD  
46   1 Y 1 A GLU 109 ? OE1 ? A GLU 93  OE1 
47   1 Y 1 A GLU 109 ? OE2 ? A GLU 93  OE2 
48   1 Y 1 A GLN 113 ? CG  ? A GLN 97  CG  
49   1 Y 1 A GLN 113 ? CD  ? A GLN 97  CD  
50   1 Y 1 A GLN 113 ? OE1 ? A GLN 97  OE1 
51   1 Y 1 A GLN 113 ? NE2 ? A GLN 97  NE2 
52   1 Y 1 A LEU 115 ? CG  ? A LEU 99  CG  
53   1 Y 1 A LEU 115 ? CD1 ? A LEU 99  CD1 
54   1 Y 1 A LEU 115 ? CD2 ? A LEU 99  CD2 
55   1 Y 1 A ASP 117 ? CG  ? A ASP 101 CG  
56   1 Y 1 A ASP 117 ? OD1 ? A ASP 101 OD1 
57   1 Y 1 A ASP 117 ? OD2 ? A ASP 101 OD2 
58   1 Y 1 A THR 123 ? OG1 ? A THR 107 OG1 
59   1 Y 1 A THR 123 ? CG2 ? A THR 107 CG2 
60   1 Y 1 A LYS 125 ? CG  ? A LYS 109 CG  
61   1 Y 1 A LYS 125 ? CD  ? A LYS 109 CD  
62   1 Y 1 A LYS 125 ? CE  ? A LYS 109 CE  
63   1 Y 1 A LYS 125 ? NZ  ? A LYS 109 NZ  
64   1 Y 1 A GLU 129 ? CG  ? A GLU 113 CG  
65   1 Y 1 A GLU 129 ? CD  ? A GLU 113 CD  
66   1 Y 1 A GLU 129 ? OE1 ? A GLU 113 OE1 
67   1 Y 1 A GLU 129 ? OE2 ? A GLU 113 OE2 
68   1 Y 1 A VAL 137 ? CG1 ? A VAL 121 CG1 
69   1 Y 1 A VAL 137 ? CG2 ? A VAL 121 CG2 
70   1 Y 1 A MET 140 ? CG  ? A MET 124 CG  
71   1 Y 1 A MET 140 ? SD  ? A MET 124 SD  
72   1 Y 1 A MET 140 ? CE  ? A MET 124 CE  
73   1 Y 1 A LEU 143 ? CG  ? A LEU 127 CG  
74   1 Y 1 A LEU 143 ? CD1 ? A LEU 127 CD1 
75   1 Y 1 A LEU 143 ? CD2 ? A LEU 127 CD2 
76   1 Y 1 A THR 144 ? OG1 ? A THR 128 OG1 
77   1 Y 1 A THR 144 ? CG2 ? A THR 128 CG2 
78   1 Y 1 A SER 145 ? OG  ? A SER 129 OG  
79   1 Y 1 A PHE 147 ? CG  ? A PHE 131 CG  
80   1 Y 1 A PHE 147 ? CD1 ? A PHE 131 CD1 
81   1 Y 1 A PHE 147 ? CD2 ? A PHE 131 CD2 
82   1 Y 1 A PHE 147 ? CE1 ? A PHE 131 CE1 
83   1 Y 1 A PHE 147 ? CE2 ? A PHE 131 CE2 
84   1 Y 1 A PHE 147 ? CZ  ? A PHE 131 CZ  
85   1 Y 1 A GLU 148 ? CG  ? A GLU 132 CG  
86   1 Y 1 A GLU 148 ? CD  ? A GLU 132 CD  
87   1 Y 1 A GLU 148 ? OE1 ? A GLU 132 OE1 
88   1 Y 1 A GLU 148 ? OE2 ? A GLU 132 OE2 
89   1 Y 1 A SER 151 ? OG  ? A SER 135 OG  
90   1 Y 1 A GLN 165 ? CG  ? A GLN 149 CG  
91   1 Y 1 A GLN 165 ? CD  ? A GLN 149 CD  
92   1 Y 1 A GLN 165 ? OE1 ? A GLN 149 OE1 
93   1 Y 1 A GLN 165 ? NE2 ? A GLN 149 NE2 
94   1 Y 1 A TRP 168 ? CG  ? A TRP 152 CG  
95   1 Y 1 A TRP 168 ? CD1 ? A TRP 152 CD1 
96   1 Y 1 A TRP 168 ? CD2 ? A TRP 152 CD2 
97   1 Y 1 A TRP 168 ? NE1 ? A TRP 152 NE1 
98   1 Y 1 A TRP 168 ? CE2 ? A TRP 152 CE2 
99   1 Y 1 A TRP 168 ? CE3 ? A TRP 152 CE3 
100  1 Y 1 A TRP 168 ? CZ2 ? A TRP 152 CZ2 
101  1 Y 1 A TRP 168 ? CZ3 ? A TRP 152 CZ3 
102  1 Y 1 A TRP 168 ? CH2 ? A TRP 152 CH2 
103  1 Y 1 A LEU 169 ? CG  ? A LEU 153 CG  
104  1 Y 1 A LEU 169 ? CD1 ? A LEU 153 CD1 
105  1 Y 1 A LEU 169 ? CD2 ? A LEU 153 CD2 
106  1 Y 1 A ASP 171 ? CG  ? A ASP 155 CG  
107  1 Y 1 A ASP 171 ? OD1 ? A ASP 155 OD1 
108  1 Y 1 A ASP 171 ? OD2 ? A ASP 155 OD2 
109  1 Y 1 A ARG 172 ? CG  ? A ARG 156 CG  
110  1 Y 1 A ARG 172 ? CD  ? A ARG 156 CD  
111  1 Y 1 A ARG 172 ? NE  ? A ARG 156 NE  
112  1 Y 1 A ARG 172 ? CZ  ? A ARG 156 CZ  
113  1 Y 1 A ARG 172 ? NH1 ? A ARG 156 NH1 
114  1 Y 1 A ARG 172 ? NH2 ? A ARG 156 NH2 
115  1 Y 1 A SER 174 ? OG  ? A SER 158 OG  
116  1 Y 1 A GLU 177 ? CG  ? A GLU 161 CG  
117  1 Y 1 A GLU 177 ? CD  ? A GLU 161 CD  
118  1 Y 1 A GLU 177 ? OE1 ? A GLU 161 OE1 
119  1 Y 1 A GLU 177 ? OE2 ? A GLU 161 OE2 
120  1 Y 1 A LYS 183 ? CG  ? A LYS 167 CG  
121  1 Y 1 A LYS 183 ? CD  ? A LYS 167 CD  
122  1 Y 1 A LYS 183 ? CE  ? A LYS 167 CE  
123  1 Y 1 A LYS 183 ? NZ  ? A LYS 167 NZ  
124  1 Y 1 A LYS 187 ? CG  ? A LYS 171 CG  
125  1 Y 1 A LYS 187 ? CD  ? A LYS 171 CD  
126  1 Y 1 A LYS 187 ? CE  ? A LYS 171 CE  
127  1 Y 1 A LYS 187 ? NZ  ? A LYS 171 NZ  
128  1 Y 1 A GLN 192 ? CG  ? A GLN 176 CG  
129  1 Y 1 A GLN 192 ? CD  ? A GLN 176 CD  
130  1 Y 1 A GLN 192 ? OE1 ? A GLN 176 OE1 
131  1 Y 1 A GLN 192 ? NE2 ? A GLN 176 NE2 
132  1 Y 1 A LEU 193 ? CG  ? A LEU 177 CG  
133  1 Y 1 A LEU 193 ? CD1 ? A LEU 177 CD1 
134  1 Y 1 A LEU 193 ? CD2 ? A LEU 177 CD2 
135  1 Y 1 A GLN 194 ? CG  ? A GLN 178 CG  
136  1 Y 1 A GLN 194 ? CD  ? A GLN 178 CD  
137  1 Y 1 A GLN 194 ? OE1 ? A GLN 178 OE1 
138  1 Y 1 A GLN 194 ? NE2 ? A GLN 178 NE2 
139  1 Y 1 A ARG 205 ? CG  ? A ARG 189 CG  
140  1 Y 1 A ARG 205 ? CD  ? A ARG 189 CD  
141  1 Y 1 A ARG 205 ? NE  ? A ARG 189 NE  
142  1 Y 1 A ARG 205 ? CZ  ? A ARG 189 CZ  
143  1 Y 1 A ARG 205 ? NH1 ? A ARG 189 NH1 
144  1 Y 1 A ARG 205 ? NH2 ? A ARG 189 NH2 
145  1 Y 1 A LEU 206 ? CG  ? A LEU 190 CG  
146  1 Y 1 A LEU 206 ? CD1 ? A LEU 190 CD1 
147  1 Y 1 A LEU 206 ? CD2 ? A LEU 190 CD2 
148  1 Y 1 A LEU 207 ? CG  ? A LEU 191 CG  
149  1 Y 1 A LEU 207 ? CD1 ? A LEU 191 CD1 
150  1 Y 1 A LEU 207 ? CD2 ? A LEU 191 CD2 
151  1 Y 1 A ASP 209 ? CG  ? A ASP 193 CG  
152  1 Y 1 A ASP 209 ? OD1 ? A ASP 193 OD1 
153  1 Y 1 A ASP 209 ? OD2 ? A ASP 193 OD2 
154  1 Y 1 A ILE 211 ? CG1 ? A ILE 195 CG1 
155  1 Y 1 A ILE 211 ? CG2 ? A ILE 195 CG2 
156  1 Y 1 A ILE 211 ? CD1 ? A ILE 195 CD1 
157  1 Y 1 A ASP 213 ? CG  ? A ASP 197 CG  
158  1 Y 1 A ASP 213 ? OD1 ? A ASP 197 OD1 
159  1 Y 1 A ASP 213 ? OD2 ? A ASP 197 OD2 
160  1 Y 1 A GLN 219 ? CG  ? A GLN 203 CG  
161  1 Y 1 A GLN 219 ? CD  ? A GLN 203 CD  
162  1 Y 1 A GLN 219 ? OE1 ? A GLN 203 OE1 
163  1 Y 1 A GLN 219 ? NE2 ? A GLN 203 NE2 
164  1 Y 1 A ASN 220 ? CG  ? A ASN 204 CG  
165  1 Y 1 A ASN 220 ? OD1 ? A ASN 204 OD1 
166  1 Y 1 A ASN 220 ? ND2 ? A ASN 204 ND2 
167  1 Y 1 A THR 222 ? OG1 ? A THR 206 OG1 
168  1 Y 1 A THR 222 ? CG2 ? A THR 206 CG2 
169  1 Y 1 A GLU 223 ? CG  ? A GLU 207 CG  
170  1 Y 1 A GLU 223 ? CD  ? A GLU 207 CD  
171  1 Y 1 A GLU 223 ? OE1 ? A GLU 207 OE1 
172  1 Y 1 A GLU 223 ? OE2 ? A GLU 207 OE2 
173  1 Y 1 A ILE 225 ? CG1 ? A ILE 209 CG1 
174  1 Y 1 A ILE 225 ? CG2 ? A ILE 209 CG2 
175  1 Y 1 A ILE 225 ? CD1 ? A ILE 209 CD1 
176  1 Y 1 A GLU 226 ? CG  ? A GLU 210 CG  
177  1 Y 1 A GLU 226 ? CD  ? A GLU 210 CD  
178  1 Y 1 A GLU 226 ? OE1 ? A GLU 210 OE1 
179  1 Y 1 A GLU 226 ? OE2 ? A GLU 210 OE2 
180  1 Y 1 A LEU 243 ? CG  ? A LEU 227 CG  
181  1 Y 1 A LEU 243 ? CD1 ? A LEU 227 CD1 
182  1 Y 1 A LEU 243 ? CD2 ? A LEU 227 CD2 
183  1 Y 1 A ARG 244 ? CG  ? A ARG 228 CG  
184  1 Y 1 A ARG 244 ? CD  ? A ARG 228 CD  
185  1 Y 1 A ARG 244 ? NE  ? A ARG 228 NE  
186  1 Y 1 A ARG 244 ? CZ  ? A ARG 228 CZ  
187  1 Y 1 A ARG 244 ? NH1 ? A ARG 228 NH1 
188  1 Y 1 A ARG 244 ? NH2 ? A ARG 228 NH2 
189  1 Y 1 A THR 245 ? OG1 ? A THR 229 OG1 
190  1 Y 1 A THR 245 ? CG2 ? A THR 229 CG2 
191  1 Y 1 A SER 246 ? OG  ? A SER 230 OG  
192  1 Y 1 A LYS 248 ? CG  ? A LYS 232 CG  
193  1 Y 1 A LYS 248 ? CD  ? A LYS 232 CD  
194  1 Y 1 A LYS 248 ? CE  ? A LYS 232 CE  
195  1 Y 1 A LYS 248 ? NZ  ? A LYS 232 NZ  
196  1 Y 1 A GLU 249 ? CG  ? A GLU 233 CG  
197  1 Y 1 A GLU 249 ? CD  ? A GLU 233 CD  
198  1 Y 1 A GLU 249 ? OE1 ? A GLU 233 OE1 
199  1 Y 1 A GLU 249 ? OE2 ? A GLU 233 OE2 
200  1 Y 1 A ILE 250 ? CG1 ? A ILE 234 CG1 
201  1 Y 1 A ILE 250 ? CG2 ? A ILE 234 CG2 
202  1 Y 1 A ILE 250 ? CD1 ? A ILE 234 CD1 
203  1 Y 1 A GLU 252 ? CG  ? A GLU 236 CG  
204  1 Y 1 A GLU 252 ? CD  ? A GLU 236 CD  
205  1 Y 1 A GLU 252 ? OE1 ? A GLU 236 OE1 
206  1 Y 1 A GLU 252 ? OE2 ? A GLU 236 OE2 
207  1 Y 1 A ASN 253 ? CG  ? A ASN 237 CG  
208  1 Y 1 A ASN 253 ? OD1 ? A ASN 237 OD1 
209  1 Y 1 A ASN 253 ? ND2 ? A ASN 237 ND2 
210  1 Y 1 A HIS 255 ? CG  ? A HIS 239 CG  
211  1 Y 1 A HIS 255 ? ND1 ? A HIS 239 ND1 
212  1 Y 1 A HIS 255 ? CD2 ? A HIS 239 CD2 
213  1 Y 1 A HIS 255 ? CE1 ? A HIS 239 CE1 
214  1 Y 1 A HIS 255 ? NE2 ? A HIS 239 NE2 
215  1 Y 1 A LEU 258 ? CG  ? A LEU 242 CG  
216  1 Y 1 A LEU 258 ? CD1 ? A LEU 242 CD1 
217  1 Y 1 A LEU 258 ? CD2 ? A LEU 242 CD2 
218  1 Y 1 A CYS 275 ? SG  ? A CYS 259 SG  
219  1 Y 1 A GLU 277 ? CG  ? A GLU 261 CG  
220  1 Y 1 A GLU 277 ? CD  ? A GLU 261 CD  
221  1 Y 1 A GLU 277 ? OE1 ? A GLU 261 OE1 
222  1 Y 1 A GLU 277 ? OE2 ? A GLU 261 OE2 
223  1 Y 1 A ASN 287 ? CG  ? A ASN 271 CG  
224  1 Y 1 A ASN 287 ? OD1 ? A ASN 271 OD1 
225  1 Y 1 A ASN 287 ? ND2 ? A ASN 271 ND2 
226  1 Y 1 A CYS 290 ? SG  ? A CYS 274 SG  
227  1 Y 1 A HIS 299 ? CG  ? A HIS 283 CG  
228  1 Y 1 A HIS 299 ? ND1 ? A HIS 283 ND1 
229  1 Y 1 A HIS 299 ? CD2 ? A HIS 283 CD2 
230  1 Y 1 A HIS 299 ? CE1 ? A HIS 283 CE1 
231  1 Y 1 A HIS 299 ? NE2 ? A HIS 283 NE2 
232  1 Y 1 A ASP 302 ? CG  ? A ASP 286 CG  
233  1 Y 1 A ASP 302 ? OD1 ? A ASP 286 OD1 
234  1 Y 1 A ASP 302 ? OD2 ? A ASP 286 OD2 
235  1 Y 1 A VAL 324 ? CG1 ? A VAL 308 CG1 
236  1 Y 1 A VAL 324 ? CG2 ? A VAL 308 CG2 
237  1 Y 1 A ASP 325 ? CG  ? A ASP 309 CG  
238  1 Y 1 A ASP 325 ? OD1 ? A ASP 309 OD1 
239  1 Y 1 A ASP 325 ? OD2 ? A ASP 309 OD2 
240  1 Y 1 A TRP 326 ? CG  ? A TRP 310 CG  
241  1 Y 1 A TRP 326 ? CD1 ? A TRP 310 CD1 
242  1 Y 1 A TRP 326 ? CD2 ? A TRP 310 CD2 
243  1 Y 1 A TRP 326 ? NE1 ? A TRP 310 NE1 
244  1 Y 1 A TRP 326 ? CE2 ? A TRP 310 CE2 
245  1 Y 1 A TRP 326 ? CE3 ? A TRP 310 CE3 
246  1 Y 1 A TRP 326 ? CZ2 ? A TRP 310 CZ2 
247  1 Y 1 A TRP 326 ? CZ3 ? A TRP 310 CZ3 
248  1 Y 1 A TRP 326 ? CH2 ? A TRP 310 CH2 
249  1 Y 1 A ASP 360 ? CG  ? A ASP 344 CG  
250  1 Y 1 A ASP 360 ? OD1 ? A ASP 344 OD1 
251  1 Y 1 A ASP 360 ? OD2 ? A ASP 344 OD2 
252  1 Y 1 A ASP 373 ? CG  ? A ASP 357 CG  
253  1 Y 1 A ASP 373 ? OD1 ? A ASP 357 OD1 
254  1 Y 1 A ASP 373 ? OD2 ? A ASP 357 OD2 
255  1 Y 1 A ASN 395 ? CG  ? A ASN 379 CG  
256  1 Y 1 A ASN 395 ? OD1 ? A ASN 379 OD1 
257  1 Y 1 A ASN 395 ? ND2 ? A ASN 379 ND2 
258  1 Y 1 A GLU 424 ? CG  ? A GLU 408 CG  
259  1 Y 1 A GLU 424 ? CD  ? A GLU 408 CD  
260  1 Y 1 A GLU 424 ? OE1 ? A GLU 408 OE1 
261  1 Y 1 A GLU 424 ? OE2 ? A GLU 408 OE2 
262  1 Y 1 A ASP 426 ? CG  ? A ASP 410 CG  
263  1 Y 1 A ASP 426 ? OD1 ? A ASP 410 OD1 
264  1 Y 1 A ASP 426 ? OD2 ? A ASP 410 OD2 
265  1 Y 1 A ARG 440 ? CG  ? A ARG 424 CG  
266  1 Y 1 A ARG 440 ? CD  ? A ARG 424 CD  
267  1 Y 1 A ARG 440 ? NE  ? A ARG 424 NE  
268  1 Y 1 A ARG 440 ? CZ  ? A ARG 424 CZ  
269  1 Y 1 A ARG 440 ? NH1 ? A ARG 424 NH1 
270  1 Y 1 A ARG 440 ? NH2 ? A ARG 424 NH2 
271  1 Y 1 A LYS 447 ? CG  ? A LYS 431 CG  
272  1 Y 1 A LYS 447 ? CD  ? A LYS 431 CD  
273  1 Y 1 A LYS 447 ? CE  ? A LYS 431 CE  
274  1 Y 1 A LYS 447 ? NZ  ? A LYS 431 NZ  
275  1 Y 1 A GLU 455 ? CG  ? A GLU 439 CG  
276  1 Y 1 A GLU 455 ? CD  ? A GLU 439 CD  
277  1 Y 1 A GLU 455 ? OE1 ? A GLU 439 OE1 
278  1 Y 1 A GLU 455 ? OE2 ? A GLU 439 OE2 
279  1 Y 1 A ASP 457 ? CG  ? A ASP 441 CG  
280  1 Y 1 A ASP 457 ? OD1 ? A ASP 441 OD1 
281  1 Y 1 A ASP 457 ? OD2 ? A ASP 441 OD2 
282  1 Y 1 A SER 458 ? OG  ? A SER 442 OG  
283  1 Y 1 A ASP 467 ? CG  ? A ASP 451 CG  
284  1 Y 1 A ASP 467 ? OD1 ? A ASP 451 OD1 
285  1 Y 1 A ASP 467 ? OD2 ? A ASP 451 OD2 
286  1 Y 1 A CYS 473 ? SG  ? A CYS 457 SG  
287  1 Y 1 A GLU 476 ? CG  ? A GLU 460 CG  
288  1 Y 1 A GLU 476 ? CD  ? A GLU 460 CD  
289  1 Y 1 A GLU 476 ? OE1 ? A GLU 460 OE1 
290  1 Y 1 A GLU 476 ? OE2 ? A GLU 460 OE2 
291  1 Y 1 A LEU 484 ? CG  ? A LEU 468 CG  
292  1 Y 1 A LEU 484 ? CD1 ? A LEU 468 CD1 
293  1 Y 1 A LEU 484 ? CD2 ? A LEU 468 CD2 
294  1 Y 1 A ASN 491 ? CG  ? A ASN 475 CG  
295  1 Y 1 A ASN 491 ? OD1 ? A ASN 475 OD1 
296  1 Y 1 A ASN 491 ? ND2 ? A ASN 475 ND2 
297  1 Y 1 A ARG 498 ? CG  ? A ARG 482 CG  
298  1 Y 1 A ARG 498 ? CD  ? A ARG 482 CD  
299  1 Y 1 A ARG 498 ? NE  ? A ARG 482 NE  
300  1 Y 1 A ARG 498 ? CZ  ? A ARG 482 CZ  
301  1 Y 1 A ARG 498 ? NH1 ? A ARG 482 NH1 
302  1 Y 1 A ARG 498 ? NH2 ? A ARG 482 NH2 
303  1 Y 1 A ASP 499 ? CG  ? A ASP 483 CG  
304  1 Y 1 A ASP 499 ? OD1 ? A ASP 483 OD1 
305  1 Y 1 A ASP 499 ? OD2 ? A ASP 483 OD2 
306  1 Y 1 A ARG 500 ? CG  ? A ARG 484 CG  
307  1 Y 1 A ARG 500 ? CD  ? A ARG 484 CD  
308  1 Y 1 A ARG 500 ? NE  ? A ARG 484 NE  
309  1 Y 1 A ARG 500 ? CZ  ? A ARG 484 CZ  
310  1 Y 1 A ARG 500 ? NH1 ? A ARG 484 NH1 
311  1 Y 1 A ARG 500 ? NH2 ? A ARG 484 NH2 
312  1 Y 1 A TYR 501 ? CG  ? A TYR 485 CG  
313  1 Y 1 A TYR 501 ? CD1 ? A TYR 485 CD1 
314  1 Y 1 A TYR 501 ? CD2 ? A TYR 485 CD2 
315  1 Y 1 A TYR 501 ? CE1 ? A TYR 485 CE1 
316  1 Y 1 A TYR 501 ? CE2 ? A TYR 485 CE2 
317  1 Y 1 A TYR 501 ? CZ  ? A TYR 485 CZ  
318  1 Y 1 A TYR 501 ? OH  ? A TYR 485 OH  
319  1 Y 1 A ASN 507 ? CG  ? A ASN 491 CG  
320  1 Y 1 A ASN 507 ? OD1 ? A ASN 491 OD1 
321  1 Y 1 A ASN 507 ? ND2 ? A ASN 491 ND2 
322  1 Y 1 A THR 515 ? OG1 ? A THR 499 OG1 
323  1 Y 1 A THR 515 ? CG2 ? A THR 499 CG2 
324  1 Y 1 A LYS 525 ? CG  ? A LYS 509 CG  
325  1 Y 1 A LYS 525 ? CD  ? A LYS 509 CD  
326  1 Y 1 A LYS 525 ? CE  ? A LYS 509 CE  
327  1 Y 1 A LYS 525 ? NZ  ? A LYS 509 NZ  
328  1 Y 1 A VAL 526 ? CG1 ? A VAL 510 CG1 
329  1 Y 1 A VAL 526 ? CG2 ? A VAL 510 CG2 
330  1 Y 1 D LYS 9   ? CG  ? B LYS 9   CG  
331  1 Y 1 D LYS 9   ? CD  ? B LYS 9   CD  
332  1 Y 1 D LYS 9   ? CE  ? B LYS 9   CE  
333  1 Y 1 D LYS 9   ? NZ  ? B LYS 9   NZ  
334  1 Y 1 D LYS 10  ? CG  ? B LYS 10  CG  
335  1 Y 1 D LYS 10  ? CD  ? B LYS 10  CD  
336  1 Y 1 D LYS 10  ? CE  ? B LYS 10  CE  
337  1 Y 1 D LYS 10  ? NZ  ? B LYS 10  NZ  
338  1 Y 1 D ASP 19  ? CG  ? B ASP 19  CG  
339  1 Y 1 D ASP 19  ? OD1 ? B ASP 19  OD1 
340  1 Y 1 D ASP 19  ? OD2 ? B ASP 19  OD2 
341  1 Y 1 D GLN 27  ? CG  ? B GLN 27  CG  
342  1 Y 1 D GLN 27  ? CD  ? B GLN 27  CD  
343  1 Y 1 D GLN 27  ? OE1 ? B GLN 27  OE1 
344  1 Y 1 D GLN 27  ? NE2 ? B GLN 27  NE2 
345  1 Y 1 D ARG 35  ? CG  ? B ARG 35  CG  
346  1 Y 1 D ARG 35  ? CD  ? B ARG 35  CD  
347  1 Y 1 D ARG 35  ? NE  ? B ARG 35  NE  
348  1 Y 1 D ARG 35  ? CZ  ? B ARG 35  CZ  
349  1 Y 1 D ARG 35  ? NH1 ? B ARG 35  NH1 
350  1 Y 1 D ARG 35  ? NH2 ? B ARG 35  NH2 
351  1 Y 1 D LEU 43  ? CG  ? B LEU 43  CG  
352  1 Y 1 D LEU 43  ? CD1 ? B LEU 43  CD1 
353  1 Y 1 D LEU 43  ? CD2 ? B LEU 43  CD2 
354  1 Y 1 D LEU 44  ? CG  ? B LEU 44  CG  
355  1 Y 1 D LEU 44  ? CD1 ? B LEU 44  CD1 
356  1 Y 1 D LEU 44  ? CD2 ? B LEU 44  CD2 
357  1 Y 1 D TYR 49  ? CG  ? B TYR 49  CG  
358  1 Y 1 D TYR 49  ? CD1 ? B TYR 49  CD1 
359  1 Y 1 D TYR 49  ? CD2 ? B TYR 49  CD2 
360  1 Y 1 D TYR 49  ? CE1 ? B TYR 49  CE1 
361  1 Y 1 D TYR 49  ? CE2 ? B TYR 49  CE2 
362  1 Y 1 D TYR 49  ? CZ  ? B TYR 49  CZ  
363  1 Y 1 D TYR 49  ? OH  ? B TYR 49  OH  
364  1 Y 1 D ARG 50  ? CG  ? B ARG 50  CG  
365  1 Y 1 D ARG 50  ? CD  ? B ARG 50  CD  
366  1 Y 1 D ARG 50  ? NE  ? B ARG 50  NE  
367  1 Y 1 D ARG 50  ? CZ  ? B ARG 50  CZ  
368  1 Y 1 D ARG 50  ? NH1 ? B ARG 50  NH1 
369  1 Y 1 D ARG 50  ? NH2 ? B ARG 50  NH2 
370  1 Y 1 D LYS 51  ? CG  ? B LYS 51  CG  
371  1 Y 1 D LYS 51  ? CD  ? B LYS 51  CD  
372  1 Y 1 D LYS 51  ? CE  ? B LYS 51  CE  
373  1 Y 1 D LYS 51  ? NZ  ? B LYS 51  NZ  
374  1 Y 1 D ARG 56  ? CG  ? B ARG 56  CG  
375  1 Y 1 D ARG 56  ? CD  ? B ARG 56  CD  
376  1 Y 1 D ARG 56  ? NE  ? B ARG 56  NE  
377  1 Y 1 D ARG 56  ? CZ  ? B ARG 56  CZ  
378  1 Y 1 D ARG 56  ? NH1 ? B ARG 56  NH1 
379  1 Y 1 D ARG 56  ? NH2 ? B ARG 56  NH2 
380  1 Y 1 D LYS 59  ? CG  ? B LYS 59  CG  
381  1 Y 1 D LYS 59  ? CD  ? B LYS 59  CD  
382  1 Y 1 D LYS 59  ? CE  ? B LYS 59  CE  
383  1 Y 1 D LYS 59  ? NZ  ? B LYS 59  NZ  
384  1 Y 1 D GLU 63  ? CG  ? B GLU 63  CG  
385  1 Y 1 D GLU 63  ? CD  ? B GLU 63  CD  
386  1 Y 1 D GLU 63  ? OE1 ? B GLU 63  OE1 
387  1 Y 1 D GLU 63  ? OE2 ? B GLU 63  OE2 
388  1 Y 1 D GLU 64  ? CG  ? B GLU 64  CG  
389  1 Y 1 D GLU 64  ? CD  ? B GLU 64  CD  
390  1 Y 1 D GLU 64  ? OE1 ? B GLU 64  OE1 
391  1 Y 1 D GLU 64  ? OE2 ? B GLU 64  OE2 
392  1 Y 1 D LYS 67  ? CG  ? B LYS 67  CG  
393  1 Y 1 D LYS 67  ? CD  ? B LYS 67  CD  
394  1 Y 1 D LYS 67  ? CE  ? B LYS 67  CE  
395  1 Y 1 D LYS 67  ? NZ  ? B LYS 67  NZ  
396  1 Y 1 D ASP 71  ? CG  ? B ASP 71  CG  
397  1 Y 1 D ASP 71  ? OD1 ? B ASP 71  OD1 
398  1 Y 1 D ASP 71  ? OD2 ? B ASP 71  OD2 
399  1 Y 1 D GLU 72  ? CG  ? B GLU 72  CG  
400  1 Y 1 D GLU 72  ? CD  ? B GLU 72  CD  
401  1 Y 1 D GLU 72  ? OE1 ? B GLU 72  OE1 
402  1 Y 1 D GLU 72  ? OE2 ? B GLU 72  OE2 
403  1 Y 1 D LYS 75  ? CG  ? B LYS 75  CG  
404  1 Y 1 D LYS 75  ? CD  ? B LYS 75  CD  
405  1 Y 1 D LYS 75  ? CE  ? B LYS 75  CE  
406  1 Y 1 D LYS 75  ? NZ  ? B LYS 75  NZ  
407  1 Y 1 D ARG 78  ? CG  ? B ARG 78  CG  
408  1 Y 1 D ARG 78  ? CD  ? B ARG 78  CD  
409  1 Y 1 D ARG 78  ? NE  ? B ARG 78  NE  
410  1 Y 1 D ARG 78  ? CZ  ? B ARG 78  CZ  
411  1 Y 1 D ARG 78  ? NH1 ? B ARG 78  NH1 
412  1 Y 1 D ARG 78  ? NH2 ? B ARG 78  NH2 
413  1 Y 1 D ARG 81  ? CG  ? B ARG 81  CG  
414  1 Y 1 D ARG 81  ? CD  ? B ARG 81  CD  
415  1 Y 1 D ARG 81  ? NE  ? B ARG 81  NE  
416  1 Y 1 D ARG 81  ? CZ  ? B ARG 81  CZ  
417  1 Y 1 D ARG 81  ? NH1 ? B ARG 81  NH1 
418  1 Y 1 D ARG 81  ? NH2 ? B ARG 81  NH2 
419  1 Y 1 D ASP 83  ? CG  ? B ASP 83  CG  
420  1 Y 1 D ASP 83  ? OD1 ? B ASP 83  OD1 
421  1 Y 1 D ASP 83  ? OD2 ? B ASP 83  OD2 
422  1 Y 1 D SER 86  ? OG  ? B SER 86  OG  
423  1 Y 1 D GLU 87  ? CG  ? B GLU 87  CG  
424  1 Y 1 D GLU 87  ? CD  ? B GLU 87  CD  
425  1 Y 1 D GLU 87  ? OE1 ? B GLU 87  OE1 
426  1 Y 1 D GLU 87  ? OE2 ? B GLU 87  OE2 
427  1 Y 1 D SER 89  ? OG  ? B SER 89  OG  
428  1 Y 1 D LYS 90  ? CG  ? B LYS 90  CG  
429  1 Y 1 D LYS 90  ? CD  ? B LYS 90  CD  
430  1 Y 1 D LYS 90  ? CE  ? B LYS 90  CE  
431  1 Y 1 D LYS 90  ? NZ  ? B LYS 90  NZ  
432  1 Y 1 D GLN 93  ? CG  ? B GLN 93  CG  
433  1 Y 1 D GLN 93  ? CD  ? B GLN 93  CD  
434  1 Y 1 D GLN 93  ? OE1 ? B GLN 93  OE1 
435  1 Y 1 D GLN 93  ? NE2 ? B GLN 93  NE2 
436  1 Y 1 D GLU 99  ? CG  ? B GLU 99  CG  
437  1 Y 1 D GLU 99  ? CD  ? B GLU 99  CD  
438  1 Y 1 D GLU 99  ? OE1 ? B GLU 99  OE1 
439  1 Y 1 D GLU 99  ? OE2 ? B GLU 99  OE2 
440  1 Y 1 D ASP 100 ? CG  ? B ASP 100 CG  
441  1 Y 1 D ASP 100 ? OD1 ? B ASP 100 OD1 
442  1 Y 1 D ASP 100 ? OD2 ? B ASP 100 OD2 
443  1 Y 1 D ASP 105 ? CG  ? B ASP 105 CG  
444  1 Y 1 D ASP 105 ? OD1 ? B ASP 105 OD1 
445  1 Y 1 D ASP 105 ? OD2 ? B ASP 105 OD2 
446  1 Y 1 D GLU 109 ? CG  ? B GLU 109 CG  
447  1 Y 1 D GLU 109 ? CD  ? B GLU 109 CD  
448  1 Y 1 D GLU 109 ? OE1 ? B GLU 109 OE1 
449  1 Y 1 D GLU 109 ? OE2 ? B GLU 109 OE2 
450  1 Y 1 D ARG 127 ? CG  ? B ARG 127 CG  
451  1 Y 1 D ARG 127 ? CD  ? B ARG 127 CD  
452  1 Y 1 D ARG 127 ? NE  ? B ARG 127 NE  
453  1 Y 1 D ARG 127 ? CZ  ? B ARG 127 CZ  
454  1 Y 1 D ARG 127 ? NH1 ? B ARG 127 NH1 
455  1 Y 1 D ARG 127 ? NH2 ? B ARG 127 NH2 
456  1 Y 1 D GLN 128 ? CG  ? B GLN 128 CG  
457  1 Y 1 D GLN 128 ? CD  ? B GLN 128 CD  
458  1 Y 1 D GLN 128 ? OE1 ? B GLN 128 OE1 
459  1 Y 1 D GLN 128 ? NE2 ? B GLN 128 NE2 
460  1 Y 1 D SER 149 ? OG  ? B SER 149 OG  
461  1 Y 1 D LYS 219 ? CG  ? B LYS 219 CG  
462  1 Y 1 D LYS 219 ? CD  ? B LYS 219 CD  
463  1 Y 1 D LYS 219 ? CE  ? B LYS 219 CE  
464  1 Y 1 D LYS 219 ? NZ  ? B LYS 219 NZ  
465  1 Y 1 D GLU 236 ? CG  ? B GLU 236 CG  
466  1 Y 1 D GLU 236 ? CD  ? B GLU 236 CD  
467  1 Y 1 D GLU 236 ? OE1 ? B GLU 236 OE1 
468  1 Y 1 D GLU 236 ? OE2 ? B GLU 236 OE2 
469  1 Y 1 D GLU 251 ? CG  ? B GLU 251 CG  
470  1 Y 1 D GLU 251 ? CD  ? B GLU 251 CD  
471  1 Y 1 D GLU 251 ? OE1 ? B GLU 251 OE1 
472  1 Y 1 D GLU 251 ? OE2 ? B GLU 251 OE2 
473  1 Y 1 D ASN 293 ? CG  ? B ASN 293 CG  
474  1 Y 1 D ASN 293 ? OD1 ? B ASN 293 OD1 
475  1 Y 1 D ASN 293 ? ND2 ? B ASN 293 ND2 
476  1 Y 1 D ASP 322 ? CG  ? B ASP 322 CG  
477  1 Y 1 D ASP 322 ? OD1 ? B ASP 322 OD1 
478  1 Y 1 D ASP 322 ? OD2 ? B ASP 322 OD2 
479  1 Y 1 D GLU 324 ? CG  ? B GLU 324 CG  
480  1 Y 1 D GLU 324 ? CD  ? B GLU 324 CD  
481  1 Y 1 D GLU 324 ? OE1 ? B GLU 324 OE1 
482  1 Y 1 D GLU 324 ? OE2 ? B GLU 324 OE2 
483  1 Y 1 D GLU 336 ? CG  ? B GLU 336 CG  
484  1 Y 1 D GLU 336 ? CD  ? B GLU 336 CD  
485  1 Y 1 D GLU 336 ? OE1 ? B GLU 336 OE1 
486  1 Y 1 D GLU 336 ? OE2 ? B GLU 336 OE2 
487  1 Y 1 D TYR 337 ? CG  ? B TYR 337 CG  
488  1 Y 1 D TYR 337 ? CD1 ? B TYR 337 CD1 
489  1 Y 1 D TYR 337 ? CD2 ? B TYR 337 CD2 
490  1 Y 1 D TYR 337 ? CE1 ? B TYR 337 CE1 
491  1 Y 1 D TYR 337 ? CE2 ? B TYR 337 CE2 
492  1 Y 1 D TYR 337 ? CZ  ? B TYR 337 CZ  
493  1 Y 1 D TYR 337 ? OH  ? B TYR 337 OH  
494  1 Y 1 D ASP 341 ? CG  ? B ASP 341 CG  
495  1 Y 1 D ASP 341 ? OD1 ? B ASP 341 OD1 
496  1 Y 1 D ASP 341 ? OD2 ? B ASP 341 OD2 
497  1 Y 1 D PHE 342 ? CG  ? B PHE 342 CG  
498  1 Y 1 D PHE 342 ? CD1 ? B PHE 342 CD1 
499  1 Y 1 D PHE 342 ? CD2 ? B PHE 342 CD2 
500  1 Y 1 D PHE 342 ? CE1 ? B PHE 342 CE1 
501  1 Y 1 D PHE 342 ? CE2 ? B PHE 342 CE2 
502  1 Y 1 D PHE 342 ? CZ  ? B PHE 342 CZ  
503  1 Y 1 D LYS 343 ? CG  ? B LYS 343 CG  
504  1 Y 1 D LYS 343 ? CD  ? B LYS 343 CD  
505  1 Y 1 D LYS 343 ? CE  ? B LYS 343 CE  
506  1 Y 1 D LYS 343 ? NZ  ? B LYS 343 NZ  
507  1 Y 1 D ASN 350 ? CG  ? B ASN 350 CG  
508  1 Y 1 D ASN 350 ? OD1 ? B ASN 350 OD1 
509  1 Y 1 D ASN 350 ? ND2 ? B ASN 350 ND2 
510  1 Y 1 D GLU 358 ? CG  ? B GLU 358 CG  
511  1 Y 1 D GLU 358 ? CD  ? B GLU 358 CD  
512  1 Y 1 D GLU 358 ? OE1 ? B GLU 358 OE1 
513  1 Y 1 D GLU 358 ? OE2 ? B GLU 358 OE2 
514  1 Y 1 C THR 36  ? OG1 ? C THR 20  OG1 
515  1 Y 1 C THR 36  ? CG2 ? C THR 20  CG2 
516  1 Y 1 C LYS 38  ? CG  ? C LYS 22  CG  
517  1 Y 1 C LYS 38  ? CD  ? C LYS 22  CD  
518  1 Y 1 C LYS 38  ? CE  ? C LYS 22  CE  
519  1 Y 1 C LYS 38  ? NZ  ? C LYS 22  NZ  
520  1 Y 1 C ARG 40  ? CG  ? C ARG 24  CG  
521  1 Y 1 C ARG 40  ? CD  ? C ARG 24  CD  
522  1 Y 1 C ARG 40  ? NE  ? C ARG 24  NE  
523  1 Y 1 C ARG 40  ? CZ  ? C ARG 24  CZ  
524  1 Y 1 C ARG 40  ? NH1 ? C ARG 24  NH1 
525  1 Y 1 C ARG 40  ? NH2 ? C ARG 24  NH2 
526  1 Y 1 C GLN 48  ? CG  ? C GLN 32  CG  
527  1 Y 1 C GLN 48  ? CD  ? C GLN 32  CD  
528  1 Y 1 C GLN 48  ? OE1 ? C GLN 32  OE1 
529  1 Y 1 C GLN 48  ? NE2 ? C GLN 32  NE2 
530  1 Y 1 C LYS 52  ? CG  ? C LYS 36  CG  
531  1 Y 1 C LYS 52  ? CD  ? C LYS 36  CD  
532  1 Y 1 C LYS 52  ? CE  ? C LYS 36  CE  
533  1 Y 1 C LYS 52  ? NZ  ? C LYS 36  NZ  
534  1 Y 1 C LEU 55  ? CG  ? C LEU 39  CG  
535  1 Y 1 C LEU 55  ? CD1 ? C LEU 39  CD1 
536  1 Y 1 C LEU 55  ? CD2 ? C LEU 39  CD2 
537  1 Y 1 C GLU 57  ? CG  ? C GLU 41  CG  
538  1 Y 1 C GLU 57  ? CD  ? C GLU 41  CD  
539  1 Y 1 C GLU 57  ? OE1 ? C GLU 41  OE1 
540  1 Y 1 C GLU 57  ? OE2 ? C GLU 41  OE2 
541  1 Y 1 C LEU 77  ? CG  ? C LEU 61  CG  
542  1 Y 1 C LEU 77  ? CD1 ? C LEU 61  CD1 
543  1 Y 1 C LEU 77  ? CD2 ? C LEU 61  CD2 
544  1 Y 1 C VAL 78  ? CG1 ? C VAL 62  CG1 
545  1 Y 1 C VAL 78  ? CG2 ? C VAL 62  CG2 
546  1 Y 1 C LEU 79  ? CG  ? C LEU 63  CG  
547  1 Y 1 C LEU 79  ? CD1 ? C LEU 63  CD1 
548  1 Y 1 C LEU 79  ? CD2 ? C LEU 63  CD2 
549  1 Y 1 C SER 88  ? OG  ? C SER 72  OG  
550  1 Y 1 C GLN 105 ? CG  ? C GLN 89  CG  
551  1 Y 1 C GLN 105 ? CD  ? C GLN 89  CD  
552  1 Y 1 C GLN 105 ? OE1 ? C GLN 89  OE1 
553  1 Y 1 C GLN 105 ? NE2 ? C GLN 89  NE2 
554  1 Y 1 C ASP 106 ? CG  ? C ASP 90  CG  
555  1 Y 1 C ASP 106 ? OD1 ? C ASP 90  OD1 
556  1 Y 1 C ASP 106 ? OD2 ? C ASP 90  OD2 
557  1 Y 1 C GLU 109 ? CG  ? C GLU 93  CG  
558  1 Y 1 C GLU 109 ? CD  ? C GLU 93  CD  
559  1 Y 1 C GLU 109 ? OE1 ? C GLU 93  OE1 
560  1 Y 1 C GLU 109 ? OE2 ? C GLU 93  OE2 
561  1 Y 1 C GLN 113 ? CG  ? C GLN 97  CG  
562  1 Y 1 C GLN 113 ? CD  ? C GLN 97  CD  
563  1 Y 1 C GLN 113 ? OE1 ? C GLN 97  OE1 
564  1 Y 1 C GLN 113 ? NE2 ? C GLN 97  NE2 
565  1 Y 1 C LEU 115 ? CG  ? C LEU 99  CG  
566  1 Y 1 C LEU 115 ? CD1 ? C LEU 99  CD1 
567  1 Y 1 C LEU 115 ? CD2 ? C LEU 99  CD2 
568  1 Y 1 C ASP 117 ? CG  ? C ASP 101 CG  
569  1 Y 1 C ASP 117 ? OD1 ? C ASP 101 OD1 
570  1 Y 1 C ASP 117 ? OD2 ? C ASP 101 OD2 
571  1 Y 1 C THR 123 ? OG1 ? C THR 107 OG1 
572  1 Y 1 C THR 123 ? CG2 ? C THR 107 CG2 
573  1 Y 1 C LYS 125 ? CG  ? C LYS 109 CG  
574  1 Y 1 C LYS 125 ? CD  ? C LYS 109 CD  
575  1 Y 1 C LYS 125 ? CE  ? C LYS 109 CE  
576  1 Y 1 C LYS 125 ? NZ  ? C LYS 109 NZ  
577  1 Y 1 C GLU 129 ? CG  ? C GLU 113 CG  
578  1 Y 1 C GLU 129 ? CD  ? C GLU 113 CD  
579  1 Y 1 C GLU 129 ? OE1 ? C GLU 113 OE1 
580  1 Y 1 C GLU 129 ? OE2 ? C GLU 113 OE2 
581  1 Y 1 C VAL 137 ? CG1 ? C VAL 121 CG1 
582  1 Y 1 C VAL 137 ? CG2 ? C VAL 121 CG2 
583  1 Y 1 C MET 140 ? CG  ? C MET 124 CG  
584  1 Y 1 C MET 140 ? SD  ? C MET 124 SD  
585  1 Y 1 C MET 140 ? CE  ? C MET 124 CE  
586  1 Y 1 C LEU 143 ? CG  ? C LEU 127 CG  
587  1 Y 1 C LEU 143 ? CD1 ? C LEU 127 CD1 
588  1 Y 1 C LEU 143 ? CD2 ? C LEU 127 CD2 
589  1 Y 1 C THR 144 ? OG1 ? C THR 128 OG1 
590  1 Y 1 C THR 144 ? CG2 ? C THR 128 CG2 
591  1 Y 1 C SER 145 ? OG  ? C SER 129 OG  
592  1 Y 1 C PHE 147 ? CG  ? C PHE 131 CG  
593  1 Y 1 C PHE 147 ? CD1 ? C PHE 131 CD1 
594  1 Y 1 C PHE 147 ? CD2 ? C PHE 131 CD2 
595  1 Y 1 C PHE 147 ? CE1 ? C PHE 131 CE1 
596  1 Y 1 C PHE 147 ? CE2 ? C PHE 131 CE2 
597  1 Y 1 C PHE 147 ? CZ  ? C PHE 131 CZ  
598  1 Y 1 C GLU 148 ? CG  ? C GLU 132 CG  
599  1 Y 1 C GLU 148 ? CD  ? C GLU 132 CD  
600  1 Y 1 C GLU 148 ? OE1 ? C GLU 132 OE1 
601  1 Y 1 C GLU 148 ? OE2 ? C GLU 132 OE2 
602  1 Y 1 C SER 151 ? OG  ? C SER 135 OG  
603  1 Y 1 C GLN 165 ? CG  ? C GLN 149 CG  
604  1 Y 1 C GLN 165 ? CD  ? C GLN 149 CD  
605  1 Y 1 C GLN 165 ? OE1 ? C GLN 149 OE1 
606  1 Y 1 C GLN 165 ? NE2 ? C GLN 149 NE2 
607  1 Y 1 C TRP 168 ? CG  ? C TRP 152 CG  
608  1 Y 1 C TRP 168 ? CD1 ? C TRP 152 CD1 
609  1 Y 1 C TRP 168 ? CD2 ? C TRP 152 CD2 
610  1 Y 1 C TRP 168 ? NE1 ? C TRP 152 NE1 
611  1 Y 1 C TRP 168 ? CE2 ? C TRP 152 CE2 
612  1 Y 1 C TRP 168 ? CE3 ? C TRP 152 CE3 
613  1 Y 1 C TRP 168 ? CZ2 ? C TRP 152 CZ2 
614  1 Y 1 C TRP 168 ? CZ3 ? C TRP 152 CZ3 
615  1 Y 1 C TRP 168 ? CH2 ? C TRP 152 CH2 
616  1 Y 1 C LEU 169 ? CG  ? C LEU 153 CG  
617  1 Y 1 C LEU 169 ? CD1 ? C LEU 153 CD1 
618  1 Y 1 C LEU 169 ? CD2 ? C LEU 153 CD2 
619  1 Y 1 C ASP 171 ? CG  ? C ASP 155 CG  
620  1 Y 1 C ASP 171 ? OD1 ? C ASP 155 OD1 
621  1 Y 1 C ASP 171 ? OD2 ? C ASP 155 OD2 
622  1 Y 1 C ARG 172 ? CG  ? C ARG 156 CG  
623  1 Y 1 C ARG 172 ? CD  ? C ARG 156 CD  
624  1 Y 1 C ARG 172 ? NE  ? C ARG 156 NE  
625  1 Y 1 C ARG 172 ? CZ  ? C ARG 156 CZ  
626  1 Y 1 C ARG 172 ? NH1 ? C ARG 156 NH1 
627  1 Y 1 C ARG 172 ? NH2 ? C ARG 156 NH2 
628  1 Y 1 C SER 174 ? OG  ? C SER 158 OG  
629  1 Y 1 C GLU 177 ? CG  ? C GLU 161 CG  
630  1 Y 1 C GLU 177 ? CD  ? C GLU 161 CD  
631  1 Y 1 C GLU 177 ? OE1 ? C GLU 161 OE1 
632  1 Y 1 C GLU 177 ? OE2 ? C GLU 161 OE2 
633  1 Y 1 C LYS 183 ? CG  ? C LYS 167 CG  
634  1 Y 1 C LYS 183 ? CD  ? C LYS 167 CD  
635  1 Y 1 C LYS 183 ? CE  ? C LYS 167 CE  
636  1 Y 1 C LYS 183 ? NZ  ? C LYS 167 NZ  
637  1 Y 1 C LYS 187 ? CG  ? C LYS 171 CG  
638  1 Y 1 C LYS 187 ? CD  ? C LYS 171 CD  
639  1 Y 1 C LYS 187 ? CE  ? C LYS 171 CE  
640  1 Y 1 C LYS 187 ? NZ  ? C LYS 171 NZ  
641  1 Y 1 C GLN 192 ? CG  ? C GLN 176 CG  
642  1 Y 1 C GLN 192 ? CD  ? C GLN 176 CD  
643  1 Y 1 C GLN 192 ? OE1 ? C GLN 176 OE1 
644  1 Y 1 C GLN 192 ? NE2 ? C GLN 176 NE2 
645  1 Y 1 C LEU 193 ? CG  ? C LEU 177 CG  
646  1 Y 1 C LEU 193 ? CD1 ? C LEU 177 CD1 
647  1 Y 1 C LEU 193 ? CD2 ? C LEU 177 CD2 
648  1 Y 1 C GLN 194 ? CG  ? C GLN 178 CG  
649  1 Y 1 C GLN 194 ? CD  ? C GLN 178 CD  
650  1 Y 1 C GLN 194 ? OE1 ? C GLN 178 OE1 
651  1 Y 1 C GLN 194 ? NE2 ? C GLN 178 NE2 
652  1 Y 1 C ARG 205 ? CG  ? C ARG 189 CG  
653  1 Y 1 C ARG 205 ? CD  ? C ARG 189 CD  
654  1 Y 1 C ARG 205 ? NE  ? C ARG 189 NE  
655  1 Y 1 C ARG 205 ? CZ  ? C ARG 189 CZ  
656  1 Y 1 C ARG 205 ? NH1 ? C ARG 189 NH1 
657  1 Y 1 C ARG 205 ? NH2 ? C ARG 189 NH2 
658  1 Y 1 C LEU 206 ? CG  ? C LEU 190 CG  
659  1 Y 1 C LEU 206 ? CD1 ? C LEU 190 CD1 
660  1 Y 1 C LEU 206 ? CD2 ? C LEU 190 CD2 
661  1 Y 1 C LEU 207 ? CG  ? C LEU 191 CG  
662  1 Y 1 C LEU 207 ? CD1 ? C LEU 191 CD1 
663  1 Y 1 C LEU 207 ? CD2 ? C LEU 191 CD2 
664  1 Y 1 C ASP 209 ? CG  ? C ASP 193 CG  
665  1 Y 1 C ASP 209 ? OD1 ? C ASP 193 OD1 
666  1 Y 1 C ASP 209 ? OD2 ? C ASP 193 OD2 
667  1 Y 1 C ILE 211 ? CG1 ? C ILE 195 CG1 
668  1 Y 1 C ILE 211 ? CG2 ? C ILE 195 CG2 
669  1 Y 1 C ILE 211 ? CD1 ? C ILE 195 CD1 
670  1 Y 1 C ASP 213 ? CG  ? C ASP 197 CG  
671  1 Y 1 C ASP 213 ? OD1 ? C ASP 197 OD1 
672  1 Y 1 C ASP 213 ? OD2 ? C ASP 197 OD2 
673  1 Y 1 C GLN 219 ? CG  ? C GLN 203 CG  
674  1 Y 1 C GLN 219 ? CD  ? C GLN 203 CD  
675  1 Y 1 C GLN 219 ? OE1 ? C GLN 203 OE1 
676  1 Y 1 C GLN 219 ? NE2 ? C GLN 203 NE2 
677  1 Y 1 C ASN 220 ? CG  ? C ASN 204 CG  
678  1 Y 1 C ASN 220 ? OD1 ? C ASN 204 OD1 
679  1 Y 1 C ASN 220 ? ND2 ? C ASN 204 ND2 
680  1 Y 1 C THR 222 ? OG1 ? C THR 206 OG1 
681  1 Y 1 C THR 222 ? CG2 ? C THR 206 CG2 
682  1 Y 1 C GLU 223 ? CG  ? C GLU 207 CG  
683  1 Y 1 C GLU 223 ? CD  ? C GLU 207 CD  
684  1 Y 1 C GLU 223 ? OE1 ? C GLU 207 OE1 
685  1 Y 1 C GLU 223 ? OE2 ? C GLU 207 OE2 
686  1 Y 1 C ILE 225 ? CG1 ? C ILE 209 CG1 
687  1 Y 1 C ILE 225 ? CG2 ? C ILE 209 CG2 
688  1 Y 1 C ILE 225 ? CD1 ? C ILE 209 CD1 
689  1 Y 1 C GLU 226 ? CG  ? C GLU 210 CG  
690  1 Y 1 C GLU 226 ? CD  ? C GLU 210 CD  
691  1 Y 1 C GLU 226 ? OE1 ? C GLU 210 OE1 
692  1 Y 1 C GLU 226 ? OE2 ? C GLU 210 OE2 
693  1 Y 1 C LEU 243 ? CG  ? C LEU 227 CG  
694  1 Y 1 C LEU 243 ? CD1 ? C LEU 227 CD1 
695  1 Y 1 C LEU 243 ? CD2 ? C LEU 227 CD2 
696  1 Y 1 C ARG 244 ? CG  ? C ARG 228 CG  
697  1 Y 1 C ARG 244 ? CD  ? C ARG 228 CD  
698  1 Y 1 C ARG 244 ? NE  ? C ARG 228 NE  
699  1 Y 1 C ARG 244 ? CZ  ? C ARG 228 CZ  
700  1 Y 1 C ARG 244 ? NH1 ? C ARG 228 NH1 
701  1 Y 1 C ARG 244 ? NH2 ? C ARG 228 NH2 
702  1 Y 1 C THR 245 ? OG1 ? C THR 229 OG1 
703  1 Y 1 C THR 245 ? CG2 ? C THR 229 CG2 
704  1 Y 1 C SER 246 ? OG  ? C SER 230 OG  
705  1 Y 1 C LYS 248 ? CG  ? C LYS 232 CG  
706  1 Y 1 C LYS 248 ? CD  ? C LYS 232 CD  
707  1 Y 1 C LYS 248 ? CE  ? C LYS 232 CE  
708  1 Y 1 C LYS 248 ? NZ  ? C LYS 232 NZ  
709  1 Y 1 C GLU 249 ? CG  ? C GLU 233 CG  
710  1 Y 1 C GLU 249 ? CD  ? C GLU 233 CD  
711  1 Y 1 C GLU 249 ? OE1 ? C GLU 233 OE1 
712  1 Y 1 C GLU 249 ? OE2 ? C GLU 233 OE2 
713  1 Y 1 C ILE 250 ? CG1 ? C ILE 234 CG1 
714  1 Y 1 C ILE 250 ? CG2 ? C ILE 234 CG2 
715  1 Y 1 C ILE 250 ? CD1 ? C ILE 234 CD1 
716  1 Y 1 C GLU 252 ? CG  ? C GLU 236 CG  
717  1 Y 1 C GLU 252 ? CD  ? C GLU 236 CD  
718  1 Y 1 C GLU 252 ? OE1 ? C GLU 236 OE1 
719  1 Y 1 C GLU 252 ? OE2 ? C GLU 236 OE2 
720  1 Y 1 C ASN 253 ? CG  ? C ASN 237 CG  
721  1 Y 1 C ASN 253 ? OD1 ? C ASN 237 OD1 
722  1 Y 1 C ASN 253 ? ND2 ? C ASN 237 ND2 
723  1 Y 1 C HIS 255 ? CG  ? C HIS 239 CG  
724  1 Y 1 C HIS 255 ? ND1 ? C HIS 239 ND1 
725  1 Y 1 C HIS 255 ? CD2 ? C HIS 239 CD2 
726  1 Y 1 C HIS 255 ? CE1 ? C HIS 239 CE1 
727  1 Y 1 C HIS 255 ? NE2 ? C HIS 239 NE2 
728  1 Y 1 C LEU 258 ? CG  ? C LEU 242 CG  
729  1 Y 1 C LEU 258 ? CD1 ? C LEU 242 CD1 
730  1 Y 1 C LEU 258 ? CD2 ? C LEU 242 CD2 
731  1 Y 1 C CYS 275 ? SG  ? C CYS 259 SG  
732  1 Y 1 C GLU 277 ? CG  ? C GLU 261 CG  
733  1 Y 1 C GLU 277 ? CD  ? C GLU 261 CD  
734  1 Y 1 C GLU 277 ? OE1 ? C GLU 261 OE1 
735  1 Y 1 C GLU 277 ? OE2 ? C GLU 261 OE2 
736  1 Y 1 C ASN 287 ? CG  ? C ASN 271 CG  
737  1 Y 1 C ASN 287 ? OD1 ? C ASN 271 OD1 
738  1 Y 1 C ASN 287 ? ND2 ? C ASN 271 ND2 
739  1 Y 1 C CYS 290 ? SG  ? C CYS 274 SG  
740  1 Y 1 C HIS 299 ? CG  ? C HIS 283 CG  
741  1 Y 1 C HIS 299 ? ND1 ? C HIS 283 ND1 
742  1 Y 1 C HIS 299 ? CD2 ? C HIS 283 CD2 
743  1 Y 1 C HIS 299 ? CE1 ? C HIS 283 CE1 
744  1 Y 1 C HIS 299 ? NE2 ? C HIS 283 NE2 
745  1 Y 1 C ASP 302 ? CG  ? C ASP 286 CG  
746  1 Y 1 C ASP 302 ? OD1 ? C ASP 286 OD1 
747  1 Y 1 C ASP 302 ? OD2 ? C ASP 286 OD2 
748  1 Y 1 C VAL 324 ? CG1 ? C VAL 308 CG1 
749  1 Y 1 C VAL 324 ? CG2 ? C VAL 308 CG2 
750  1 Y 1 C ASP 325 ? CG  ? C ASP 309 CG  
751  1 Y 1 C ASP 325 ? OD1 ? C ASP 309 OD1 
752  1 Y 1 C ASP 325 ? OD2 ? C ASP 309 OD2 
753  1 Y 1 C TRP 326 ? CG  ? C TRP 310 CG  
754  1 Y 1 C TRP 326 ? CD1 ? C TRP 310 CD1 
755  1 Y 1 C TRP 326 ? CD2 ? C TRP 310 CD2 
756  1 Y 1 C TRP 326 ? NE1 ? C TRP 310 NE1 
757  1 Y 1 C TRP 326 ? CE2 ? C TRP 310 CE2 
758  1 Y 1 C TRP 326 ? CE3 ? C TRP 310 CE3 
759  1 Y 1 C TRP 326 ? CZ2 ? C TRP 310 CZ2 
760  1 Y 1 C TRP 326 ? CZ3 ? C TRP 310 CZ3 
761  1 Y 1 C TRP 326 ? CH2 ? C TRP 310 CH2 
762  1 Y 1 C ASP 360 ? CG  ? C ASP 344 CG  
763  1 Y 1 C ASP 360 ? OD1 ? C ASP 344 OD1 
764  1 Y 1 C ASP 360 ? OD2 ? C ASP 344 OD2 
765  1 Y 1 C ASP 373 ? CG  ? C ASP 357 CG  
766  1 Y 1 C ASP 373 ? OD1 ? C ASP 357 OD1 
767  1 Y 1 C ASP 373 ? OD2 ? C ASP 357 OD2 
768  1 Y 1 C ASN 395 ? CG  ? C ASN 379 CG  
769  1 Y 1 C ASN 395 ? OD1 ? C ASN 379 OD1 
770  1 Y 1 C ASN 395 ? ND2 ? C ASN 379 ND2 
771  1 Y 1 C GLU 424 ? CG  ? C GLU 408 CG  
772  1 Y 1 C GLU 424 ? CD  ? C GLU 408 CD  
773  1 Y 1 C GLU 424 ? OE1 ? C GLU 408 OE1 
774  1 Y 1 C GLU 424 ? OE2 ? C GLU 408 OE2 
775  1 Y 1 C ASP 426 ? CG  ? C ASP 410 CG  
776  1 Y 1 C ASP 426 ? OD1 ? C ASP 410 OD1 
777  1 Y 1 C ASP 426 ? OD2 ? C ASP 410 OD2 
778  1 Y 1 C ARG 440 ? CG  ? C ARG 424 CG  
779  1 Y 1 C ARG 440 ? CD  ? C ARG 424 CD  
780  1 Y 1 C ARG 440 ? NE  ? C ARG 424 NE  
781  1 Y 1 C ARG 440 ? CZ  ? C ARG 424 CZ  
782  1 Y 1 C ARG 440 ? NH1 ? C ARG 424 NH1 
783  1 Y 1 C ARG 440 ? NH2 ? C ARG 424 NH2 
784  1 Y 1 C LYS 447 ? CG  ? C LYS 431 CG  
785  1 Y 1 C LYS 447 ? CD  ? C LYS 431 CD  
786  1 Y 1 C LYS 447 ? CE  ? C LYS 431 CE  
787  1 Y 1 C LYS 447 ? NZ  ? C LYS 431 NZ  
788  1 Y 1 C GLU 455 ? CG  ? C GLU 439 CG  
789  1 Y 1 C GLU 455 ? CD  ? C GLU 439 CD  
790  1 Y 1 C GLU 455 ? OE1 ? C GLU 439 OE1 
791  1 Y 1 C GLU 455 ? OE2 ? C GLU 439 OE2 
792  1 Y 1 C ASP 457 ? CG  ? C ASP 441 CG  
793  1 Y 1 C ASP 457 ? OD1 ? C ASP 441 OD1 
794  1 Y 1 C ASP 457 ? OD2 ? C ASP 441 OD2 
795  1 Y 1 C SER 458 ? OG  ? C SER 442 OG  
796  1 Y 1 C ASP 467 ? CG  ? C ASP 451 CG  
797  1 Y 1 C ASP 467 ? OD1 ? C ASP 451 OD1 
798  1 Y 1 C ASP 467 ? OD2 ? C ASP 451 OD2 
799  1 Y 1 C CYS 473 ? SG  ? C CYS 457 SG  
800  1 Y 1 C GLU 476 ? CG  ? C GLU 460 CG  
801  1 Y 1 C GLU 476 ? CD  ? C GLU 460 CD  
802  1 Y 1 C GLU 476 ? OE1 ? C GLU 460 OE1 
803  1 Y 1 C GLU 476 ? OE2 ? C GLU 460 OE2 
804  1 Y 1 C LEU 484 ? CG  ? C LEU 468 CG  
805  1 Y 1 C LEU 484 ? CD1 ? C LEU 468 CD1 
806  1 Y 1 C LEU 484 ? CD2 ? C LEU 468 CD2 
807  1 Y 1 C ASN 491 ? CG  ? C ASN 475 CG  
808  1 Y 1 C ASN 491 ? OD1 ? C ASN 475 OD1 
809  1 Y 1 C ASN 491 ? ND2 ? C ASN 475 ND2 
810  1 Y 1 C ARG 498 ? CG  ? C ARG 482 CG  
811  1 Y 1 C ARG 498 ? CD  ? C ARG 482 CD  
812  1 Y 1 C ARG 498 ? NE  ? C ARG 482 NE  
813  1 Y 1 C ARG 498 ? CZ  ? C ARG 482 CZ  
814  1 Y 1 C ARG 498 ? NH1 ? C ARG 482 NH1 
815  1 Y 1 C ARG 498 ? NH2 ? C ARG 482 NH2 
816  1 Y 1 C ASP 499 ? CG  ? C ASP 483 CG  
817  1 Y 1 C ASP 499 ? OD1 ? C ASP 483 OD1 
818  1 Y 1 C ASP 499 ? OD2 ? C ASP 483 OD2 
819  1 Y 1 C ARG 500 ? CG  ? C ARG 484 CG  
820  1 Y 1 C ARG 500 ? CD  ? C ARG 484 CD  
821  1 Y 1 C ARG 500 ? NE  ? C ARG 484 NE  
822  1 Y 1 C ARG 500 ? CZ  ? C ARG 484 CZ  
823  1 Y 1 C ARG 500 ? NH1 ? C ARG 484 NH1 
824  1 Y 1 C ARG 500 ? NH2 ? C ARG 484 NH2 
825  1 Y 1 C TYR 501 ? CG  ? C TYR 485 CG  
826  1 Y 1 C TYR 501 ? CD1 ? C TYR 485 CD1 
827  1 Y 1 C TYR 501 ? CD2 ? C TYR 485 CD2 
828  1 Y 1 C TYR 501 ? CE1 ? C TYR 485 CE1 
829  1 Y 1 C TYR 501 ? CE2 ? C TYR 485 CE2 
830  1 Y 1 C TYR 501 ? CZ  ? C TYR 485 CZ  
831  1 Y 1 C TYR 501 ? OH  ? C TYR 485 OH  
832  1 Y 1 C ASN 507 ? CG  ? C ASN 491 CG  
833  1 Y 1 C ASN 507 ? OD1 ? C ASN 491 OD1 
834  1 Y 1 C ASN 507 ? ND2 ? C ASN 491 ND2 
835  1 Y 1 C THR 515 ? OG1 ? C THR 499 OG1 
836  1 Y 1 C THR 515 ? CG2 ? C THR 499 CG2 
837  1 Y 1 C LYS 525 ? CG  ? C LYS 509 CG  
838  1 Y 1 C LYS 525 ? CD  ? C LYS 509 CD  
839  1 Y 1 C LYS 525 ? CE  ? C LYS 509 CE  
840  1 Y 1 C LYS 525 ? NZ  ? C LYS 509 NZ  
841  1 Y 1 C VAL 526 ? CG1 ? C VAL 510 CG1 
842  1 Y 1 C VAL 526 ? CG2 ? C VAL 510 CG2 
843  1 Y 1 B LYS 9   ? CG  ? D LYS 9   CG  
844  1 Y 1 B LYS 9   ? CD  ? D LYS 9   CD  
845  1 Y 1 B LYS 9   ? CE  ? D LYS 9   CE  
846  1 Y 1 B LYS 9   ? NZ  ? D LYS 9   NZ  
847  1 Y 1 B LYS 10  ? CG  ? D LYS 10  CG  
848  1 Y 1 B LYS 10  ? CD  ? D LYS 10  CD  
849  1 Y 1 B LYS 10  ? CE  ? D LYS 10  CE  
850  1 Y 1 B LYS 10  ? NZ  ? D LYS 10  NZ  
851  1 Y 1 B ASP 19  ? CG  ? D ASP 19  CG  
852  1 Y 1 B ASP 19  ? OD1 ? D ASP 19  OD1 
853  1 Y 1 B ASP 19  ? OD2 ? D ASP 19  OD2 
854  1 Y 1 B GLN 27  ? CG  ? D GLN 27  CG  
855  1 Y 1 B GLN 27  ? CD  ? D GLN 27  CD  
856  1 Y 1 B GLN 27  ? OE1 ? D GLN 27  OE1 
857  1 Y 1 B GLN 27  ? NE2 ? D GLN 27  NE2 
858  1 Y 1 B ARG 35  ? CG  ? D ARG 35  CG  
859  1 Y 1 B ARG 35  ? CD  ? D ARG 35  CD  
860  1 Y 1 B ARG 35  ? NE  ? D ARG 35  NE  
861  1 Y 1 B ARG 35  ? CZ  ? D ARG 35  CZ  
862  1 Y 1 B ARG 35  ? NH1 ? D ARG 35  NH1 
863  1 Y 1 B ARG 35  ? NH2 ? D ARG 35  NH2 
864  1 Y 1 B LEU 43  ? CG  ? D LEU 43  CG  
865  1 Y 1 B LEU 43  ? CD1 ? D LEU 43  CD1 
866  1 Y 1 B LEU 43  ? CD2 ? D LEU 43  CD2 
867  1 Y 1 B LEU 44  ? CG  ? D LEU 44  CG  
868  1 Y 1 B LEU 44  ? CD1 ? D LEU 44  CD1 
869  1 Y 1 B LEU 44  ? CD2 ? D LEU 44  CD2 
870  1 Y 1 B TYR 49  ? CG  ? D TYR 49  CG  
871  1 Y 1 B TYR 49  ? CD1 ? D TYR 49  CD1 
872  1 Y 1 B TYR 49  ? CD2 ? D TYR 49  CD2 
873  1 Y 1 B TYR 49  ? CE1 ? D TYR 49  CE1 
874  1 Y 1 B TYR 49  ? CE2 ? D TYR 49  CE2 
875  1 Y 1 B TYR 49  ? CZ  ? D TYR 49  CZ  
876  1 Y 1 B TYR 49  ? OH  ? D TYR 49  OH  
877  1 Y 1 B ARG 50  ? CG  ? D ARG 50  CG  
878  1 Y 1 B ARG 50  ? CD  ? D ARG 50  CD  
879  1 Y 1 B ARG 50  ? NE  ? D ARG 50  NE  
880  1 Y 1 B ARG 50  ? CZ  ? D ARG 50  CZ  
881  1 Y 1 B ARG 50  ? NH1 ? D ARG 50  NH1 
882  1 Y 1 B ARG 50  ? NH2 ? D ARG 50  NH2 
883  1 Y 1 B LYS 51  ? CG  ? D LYS 51  CG  
884  1 Y 1 B LYS 51  ? CD  ? D LYS 51  CD  
885  1 Y 1 B LYS 51  ? CE  ? D LYS 51  CE  
886  1 Y 1 B LYS 51  ? NZ  ? D LYS 51  NZ  
887  1 Y 1 B ARG 56  ? CG  ? D ARG 56  CG  
888  1 Y 1 B ARG 56  ? CD  ? D ARG 56  CD  
889  1 Y 1 B ARG 56  ? NE  ? D ARG 56  NE  
890  1 Y 1 B ARG 56  ? CZ  ? D ARG 56  CZ  
891  1 Y 1 B ARG 56  ? NH1 ? D ARG 56  NH1 
892  1 Y 1 B ARG 56  ? NH2 ? D ARG 56  NH2 
893  1 Y 1 B LYS 59  ? CG  ? D LYS 59  CG  
894  1 Y 1 B LYS 59  ? CD  ? D LYS 59  CD  
895  1 Y 1 B LYS 59  ? CE  ? D LYS 59  CE  
896  1 Y 1 B LYS 59  ? NZ  ? D LYS 59  NZ  
897  1 Y 1 B GLU 63  ? CG  ? D GLU 63  CG  
898  1 Y 1 B GLU 63  ? CD  ? D GLU 63  CD  
899  1 Y 1 B GLU 63  ? OE1 ? D GLU 63  OE1 
900  1 Y 1 B GLU 63  ? OE2 ? D GLU 63  OE2 
901  1 Y 1 B GLU 64  ? CG  ? D GLU 64  CG  
902  1 Y 1 B GLU 64  ? CD  ? D GLU 64  CD  
903  1 Y 1 B GLU 64  ? OE1 ? D GLU 64  OE1 
904  1 Y 1 B GLU 64  ? OE2 ? D GLU 64  OE2 
905  1 Y 1 B LYS 67  ? CG  ? D LYS 67  CG  
906  1 Y 1 B LYS 67  ? CD  ? D LYS 67  CD  
907  1 Y 1 B LYS 67  ? CE  ? D LYS 67  CE  
908  1 Y 1 B LYS 67  ? NZ  ? D LYS 67  NZ  
909  1 Y 1 B ASP 71  ? CG  ? D ASP 71  CG  
910  1 Y 1 B ASP 71  ? OD1 ? D ASP 71  OD1 
911  1 Y 1 B ASP 71  ? OD2 ? D ASP 71  OD2 
912  1 Y 1 B GLU 72  ? CG  ? D GLU 72  CG  
913  1 Y 1 B GLU 72  ? CD  ? D GLU 72  CD  
914  1 Y 1 B GLU 72  ? OE1 ? D GLU 72  OE1 
915  1 Y 1 B GLU 72  ? OE2 ? D GLU 72  OE2 
916  1 Y 1 B LYS 75  ? CG  ? D LYS 75  CG  
917  1 Y 1 B LYS 75  ? CD  ? D LYS 75  CD  
918  1 Y 1 B LYS 75  ? CE  ? D LYS 75  CE  
919  1 Y 1 B LYS 75  ? NZ  ? D LYS 75  NZ  
920  1 Y 1 B ARG 78  ? CG  ? D ARG 78  CG  
921  1 Y 1 B ARG 78  ? CD  ? D ARG 78  CD  
922  1 Y 1 B ARG 78  ? NE  ? D ARG 78  NE  
923  1 Y 1 B ARG 78  ? CZ  ? D ARG 78  CZ  
924  1 Y 1 B ARG 78  ? NH1 ? D ARG 78  NH1 
925  1 Y 1 B ARG 78  ? NH2 ? D ARG 78  NH2 
926  1 Y 1 B ARG 81  ? CG  ? D ARG 81  CG  
927  1 Y 1 B ARG 81  ? CD  ? D ARG 81  CD  
928  1 Y 1 B ARG 81  ? NE  ? D ARG 81  NE  
929  1 Y 1 B ARG 81  ? CZ  ? D ARG 81  CZ  
930  1 Y 1 B ARG 81  ? NH1 ? D ARG 81  NH1 
931  1 Y 1 B ARG 81  ? NH2 ? D ARG 81  NH2 
932  1 Y 1 B ASP 83  ? CG  ? D ASP 83  CG  
933  1 Y 1 B ASP 83  ? OD1 ? D ASP 83  OD1 
934  1 Y 1 B ASP 83  ? OD2 ? D ASP 83  OD2 
935  1 Y 1 B SER 86  ? OG  ? D SER 86  OG  
936  1 Y 1 B GLU 87  ? CG  ? D GLU 87  CG  
937  1 Y 1 B GLU 87  ? CD  ? D GLU 87  CD  
938  1 Y 1 B GLU 87  ? OE1 ? D GLU 87  OE1 
939  1 Y 1 B GLU 87  ? OE2 ? D GLU 87  OE2 
940  1 Y 1 B SER 89  ? OG  ? D SER 89  OG  
941  1 Y 1 B LYS 90  ? CG  ? D LYS 90  CG  
942  1 Y 1 B LYS 90  ? CD  ? D LYS 90  CD  
943  1 Y 1 B LYS 90  ? CE  ? D LYS 90  CE  
944  1 Y 1 B LYS 90  ? NZ  ? D LYS 90  NZ  
945  1 Y 1 B GLN 93  ? CG  ? D GLN 93  CG  
946  1 Y 1 B GLN 93  ? CD  ? D GLN 93  CD  
947  1 Y 1 B GLN 93  ? OE1 ? D GLN 93  OE1 
948  1 Y 1 B GLN 93  ? NE2 ? D GLN 93  NE2 
949  1 Y 1 B GLU 99  ? CG  ? D GLU 99  CG  
950  1 Y 1 B GLU 99  ? CD  ? D GLU 99  CD  
951  1 Y 1 B GLU 99  ? OE1 ? D GLU 99  OE1 
952  1 Y 1 B GLU 99  ? OE2 ? D GLU 99  OE2 
953  1 Y 1 B ASP 100 ? CG  ? D ASP 100 CG  
954  1 Y 1 B ASP 100 ? OD1 ? D ASP 100 OD1 
955  1 Y 1 B ASP 100 ? OD2 ? D ASP 100 OD2 
956  1 Y 1 B ASP 105 ? CG  ? D ASP 105 CG  
957  1 Y 1 B ASP 105 ? OD1 ? D ASP 105 OD1 
958  1 Y 1 B ASP 105 ? OD2 ? D ASP 105 OD2 
959  1 Y 1 B GLU 109 ? CG  ? D GLU 109 CG  
960  1 Y 1 B GLU 109 ? CD  ? D GLU 109 CD  
961  1 Y 1 B GLU 109 ? OE1 ? D GLU 109 OE1 
962  1 Y 1 B GLU 109 ? OE2 ? D GLU 109 OE2 
963  1 Y 1 B ARG 127 ? CG  ? D ARG 127 CG  
964  1 Y 1 B ARG 127 ? CD  ? D ARG 127 CD  
965  1 Y 1 B ARG 127 ? NE  ? D ARG 127 NE  
966  1 Y 1 B ARG 127 ? CZ  ? D ARG 127 CZ  
967  1 Y 1 B ARG 127 ? NH1 ? D ARG 127 NH1 
968  1 Y 1 B ARG 127 ? NH2 ? D ARG 127 NH2 
969  1 Y 1 B GLN 128 ? CG  ? D GLN 128 CG  
970  1 Y 1 B GLN 128 ? CD  ? D GLN 128 CD  
971  1 Y 1 B GLN 128 ? OE1 ? D GLN 128 OE1 
972  1 Y 1 B GLN 128 ? NE2 ? D GLN 128 NE2 
973  1 Y 1 B SER 149 ? OG  ? D SER 149 OG  
974  1 Y 1 B LYS 219 ? CG  ? D LYS 219 CG  
975  1 Y 1 B LYS 219 ? CD  ? D LYS 219 CD  
976  1 Y 1 B LYS 219 ? CE  ? D LYS 219 CE  
977  1 Y 1 B LYS 219 ? NZ  ? D LYS 219 NZ  
978  1 Y 1 B GLU 236 ? CG  ? D GLU 236 CG  
979  1 Y 1 B GLU 236 ? CD  ? D GLU 236 CD  
980  1 Y 1 B GLU 236 ? OE1 ? D GLU 236 OE1 
981  1 Y 1 B GLU 236 ? OE2 ? D GLU 236 OE2 
982  1 Y 1 B GLU 251 ? CG  ? D GLU 251 CG  
983  1 Y 1 B GLU 251 ? CD  ? D GLU 251 CD  
984  1 Y 1 B GLU 251 ? OE1 ? D GLU 251 OE1 
985  1 Y 1 B GLU 251 ? OE2 ? D GLU 251 OE2 
986  1 Y 1 B ASN 293 ? CG  ? D ASN 293 CG  
987  1 Y 1 B ASN 293 ? OD1 ? D ASN 293 OD1 
988  1 Y 1 B ASN 293 ? ND2 ? D ASN 293 ND2 
989  1 Y 1 B ASP 322 ? CG  ? D ASP 322 CG  
990  1 Y 1 B ASP 322 ? OD1 ? D ASP 322 OD1 
991  1 Y 1 B ASP 322 ? OD2 ? D ASP 322 OD2 
992  1 Y 1 B GLU 324 ? CG  ? D GLU 324 CG  
993  1 Y 1 B GLU 324 ? CD  ? D GLU 324 CD  
994  1 Y 1 B GLU 324 ? OE1 ? D GLU 324 OE1 
995  1 Y 1 B GLU 324 ? OE2 ? D GLU 324 OE2 
996  1 Y 1 B GLU 336 ? CG  ? D GLU 336 CG  
997  1 Y 1 B GLU 336 ? CD  ? D GLU 336 CD  
998  1 Y 1 B GLU 336 ? OE1 ? D GLU 336 OE1 
999  1 Y 1 B GLU 336 ? OE2 ? D GLU 336 OE2 
1000 1 Y 1 B TYR 337 ? CG  ? D TYR 337 CG  
1001 1 Y 1 B TYR 337 ? CD1 ? D TYR 337 CD1 
1002 1 Y 1 B TYR 337 ? CD2 ? D TYR 337 CD2 
1003 1 Y 1 B TYR 337 ? CE1 ? D TYR 337 CE1 
1004 1 Y 1 B TYR 337 ? CE2 ? D TYR 337 CE2 
1005 1 Y 1 B TYR 337 ? CZ  ? D TYR 337 CZ  
1006 1 Y 1 B TYR 337 ? OH  ? D TYR 337 OH  
1007 1 Y 1 B ASP 341 ? CG  ? D ASP 341 CG  
1008 1 Y 1 B ASP 341 ? OD1 ? D ASP 341 OD1 
1009 1 Y 1 B ASP 341 ? OD2 ? D ASP 341 OD2 
1010 1 Y 1 B PHE 342 ? CG  ? D PHE 342 CG  
1011 1 Y 1 B PHE 342 ? CD1 ? D PHE 342 CD1 
1012 1 Y 1 B PHE 342 ? CD2 ? D PHE 342 CD2 
1013 1 Y 1 B PHE 342 ? CE1 ? D PHE 342 CE1 
1014 1 Y 1 B PHE 342 ? CE2 ? D PHE 342 CE2 
1015 1 Y 1 B PHE 342 ? CZ  ? D PHE 342 CZ  
1016 1 Y 1 B LYS 343 ? CG  ? D LYS 343 CG  
1017 1 Y 1 B LYS 343 ? CD  ? D LYS 343 CD  
1018 1 Y 1 B LYS 343 ? CE  ? D LYS 343 CE  
1019 1 Y 1 B LYS 343 ? NZ  ? D LYS 343 NZ  
1020 1 Y 1 B ASN 350 ? CG  ? D ASN 350 CG  
1021 1 Y 1 B ASN 350 ? OD1 ? D ASN 350 OD1 
1022 1 Y 1 B ASN 350 ? ND2 ? D ASN 350 ND2 
1023 1 Y 1 B GLU 358 ? CG  ? D GLU 358 CG  
1024 1 Y 1 B GLU 358 ? CD  ? D GLU 358 CD  
1025 1 Y 1 B GLU 358 ? OE1 ? D GLU 358 OE1 
1026 1 Y 1 B GLU 358 ? OE2 ? D GLU 358 OE2 
# 
_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                     9GGM 
_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                         9GGM 
_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                   9GGM 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9GGM 
_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' ? 0.004 ? 11698 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.774 ? 15918 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 3.928 ? 1672  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.048 ? 1828  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.006 ? 2034  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9GGM 
_struct.title                        'Cryo-EM structure of KBTBD4 P313PRR mutant-HDAC2 2:2 complex' 
_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        9GGM 
_struct_keywords.text            'E3 ligase, deacetylase, transcription, cancer mutation, protein complex, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP KBTB4_HUMAN Q9NVX7 Q9NVX7-2 1 
;MESPEEPGASMDENYFVNYTFKDRSHSGRVAQGIMKLCLEEELFADVTISVEGREFQLHRLVLSAQSCFFRSMFTSNLKE
AHNRVIVLQDVSESVFQLLVDYIYHGTVKLRAEELQEIYEVSDMYQLTSLFEECSRFLARTVQVGNCLQVMWLADRHSDP
ELYTAAKHCAKTHLAQLQNTEEFLHLPHRLLTDIISDGVPCSQNPTEAIEAWINFNKEEREAFAESLRTSLKEIGENVHI
YLIGKESSRTHSLAVSLHCAEDDSISVSGQNSLCHQITAACKHGGDLYVVGGSIPRRMWKCNNATVDWEWCAPLPRDRLQ
HTLVSVPGKDAIYSLGGKTLQDTLSNAVIYYRVGDNVWTETTQLEVAVSGAAGANLNGIIYLLGGEENDLDFFTKPSRLI
QCFDTETDKCHVKPYVLPFAGRMHAAVHKDLVFIVAEGDSLVCYNPLLDSFTRLCLPEAWSSAPSLWKIASCNGSIYVFR
DRYKKGDANTYKLDPATSAVTVTRGIKVLLTNLQFVLA
;
17 
2 UNP HDAC2_HUMAN Q92769 ?        2 
;MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSI
RPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLA
ILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQ
IFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVA
LDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGE
DPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGT
KSEQLSNP
;
1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GGM A 1 ? 520 ? Q9NVX7 17 ? 534 ? 17 536 
2 2 9GGM D 1 ? 488 ? Q92769 1  ? 488 ? 1  488 
3 1 9GGM C 1 ? 520 ? Q9NVX7 17 ? 534 ? 17 536 
4 2 9GGM B 1 ? 488 ? Q92769 1  ? 488 ? 1  488 
# 
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 9GGM PRO A 295 ? UNP Q9NVX7 ? ? insertion 311 1 
1 9GGM ARG A 296 ? UNP Q9NVX7 ? ? insertion 312 2 
3 9GGM PRO C 295 ? UNP Q9NVX7 ? ? insertion 311 3 
3 9GGM ARG C 296 ? UNP Q9NVX7 ? ? insertion 312 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 SER A 25  ? GLU A 41  ? SER A 41  GLU A 57  1 ? 17 
HELX_P HELX_P2  AA2 LEU A 61  ? ALA A 65  ? LEU A 77  ALA A 81  1 ? 5  
HELX_P HELX_P3  AA3 SER A 67  ? PHE A 74  ? SER A 83  PHE A 90  1 ? 8  
HELX_P HELX_P4  AA4 SER A 92  ? HIS A 105 ? SER A 108 HIS A 121 1 ? 14 
HELX_P HELX_P5  AA5 ARG A 111 ? GLU A 113 ? ARG A 127 GLU A 129 5 ? 3  
HELX_P HELX_P6  AA6 GLU A 114 ? TYR A 125 ? GLU A 130 TYR A 141 1 ? 12 
HELX_P HELX_P7  AA7 THR A 128 ? ALA A 139 ? THR A 144 ALA A 155 1 ? 12 
HELX_P HELX_P8  AA8 ASN A 146 ? SER A 158 ? ASN A 162 SER A 174 1 ? 13 
HELX_P HELX_P9  AA9 GLU A 161 ? HIS A 173 ? GLU A 177 HIS A 189 1 ? 13 
HELX_P HELX_P10 AB1 ARG A 189 ? GLY A 198 ? ARG A 205 GLY A 214 1 ? 10 
HELX_P HELX_P11 AB2 ASN A 204 ? ALA A 211 ? ASN A 220 ALA A 227 1 ? 8  
HELX_P HELX_P12 AB3 ASP B 17  ? TYR B 23  ? ASP D 17  TYR D 23  5 ? 7  
HELX_P HELX_P13 AB4 HIS B 34  ? TYR B 46  ? HIS D 34  TYR D 46  1 ? 13 
HELX_P HELX_P14 AB5 GLY B 47  ? MET B 52  ? GLY D 47  MET D 52  1 ? 6  
HELX_P HELX_P15 AB6 THR B 61  ? THR B 66  ? THR D 61  THR D 66  1 ? 6  
HELX_P HELX_P16 AB7 SER B 70  ? ILE B 80  ? SER D 70  ILE D 80  1 ? 11 
HELX_P HELX_P17 AB8 LYS B 90  ? PHE B 95  ? LYS D 90  PHE D 95  1 ? 6  
HELX_P HELX_P18 AB9 GLY B 106 ? THR B 115 ? GLY D 106 THR D 115 1 ? 10 
HELX_P HELX_P19 AC1 THR B 115 ? ARG B 127 ? THR D 115 ARG D 127 1 ? 13 
HELX_P HELX_P20 AC2 ASN B 155 ? LYS B 166 ? ASN D 155 LYS D 166 1 ? 12 
HELX_P HELX_P21 AC3 GLY B 181 ? PHE B 188 ? GLY D 181 PHE D 188 1 ? 8  
HELX_P HELX_P22 AC4 ALA B 217 ? LYS B 221 ? ALA D 217 LYS D 221 5 ? 5  
HELX_P HELX_P23 AC5 ASP B 234 ? GLN B 254 ? ASP D 234 GLN D 254 1 ? 21 
HELX_P HELX_P24 AC6 ASP B 265 ? LEU B 267 ? ASP D 265 LEU D 267 5 ? 3  
HELX_P HELX_P25 AC7 THR B 278 ? PHE B 292 ? THR D 278 PHE D 292 1 ? 15 
HELX_P HELX_P26 AC8 THR B 305 ? ASP B 322 ? THR D 305 ASP D 322 1 ? 18 
HELX_P HELX_P27 AC9 TYR B 334 ? GLY B 339 ? TYR D 334 GLY D 339 1 ? 6  
HELX_P HELX_P28 AD1 THR B 356 ? ARG B 372 ? THR D 356 ARG D 372 1 ? 17 
HELX_P HELX_P29 AD2 SER C 25  ? GLU C 41  ? SER C 41  GLU C 57  1 ? 17 
HELX_P HELX_P30 AD3 LEU C 61  ? ALA C 65  ? LEU C 77  ALA C 81  1 ? 5  
HELX_P HELX_P31 AD4 SER C 67  ? PHE C 74  ? SER C 83  PHE C 90  1 ? 8  
HELX_P HELX_P32 AD5 SER C 92  ? HIS C 105 ? SER C 108 HIS C 121 1 ? 14 
HELX_P HELX_P33 AD6 ARG C 111 ? GLU C 113 ? ARG C 127 GLU C 129 5 ? 3  
HELX_P HELX_P34 AD7 GLU C 114 ? TYR C 125 ? GLU C 130 TYR C 141 1 ? 12 
HELX_P HELX_P35 AD8 THR C 128 ? ALA C 139 ? THR C 144 ALA C 155 1 ? 12 
HELX_P HELX_P36 AD9 ASN C 146 ? SER C 158 ? ASN C 162 SER C 174 1 ? 13 
HELX_P HELX_P37 AE1 GLU C 161 ? HIS C 173 ? GLU C 177 HIS C 189 1 ? 13 
HELX_P HELX_P38 AE2 ARG C 189 ? GLY C 198 ? ARG C 205 GLY C 214 1 ? 10 
HELX_P HELX_P39 AE3 ASN C 204 ? ALA C 211 ? ASN C 220 ALA C 227 1 ? 8  
HELX_P HELX_P40 AE4 ASP D 17  ? TYR D 23  ? ASP B 17  TYR B 23  5 ? 7  
HELX_P HELX_P41 AE5 HIS D 34  ? TYR D 46  ? HIS B 34  TYR B 46  1 ? 13 
HELX_P HELX_P42 AE6 GLY D 47  ? MET D 52  ? GLY B 47  MET B 52  1 ? 6  
HELX_P HELX_P43 AE7 THR D 61  ? THR D 66  ? THR B 61  THR B 66  1 ? 6  
HELX_P HELX_P44 AE8 SER D 70  ? ILE D 80  ? SER B 70  ILE B 80  1 ? 11 
HELX_P HELX_P45 AE9 LYS D 90  ? PHE D 95  ? LYS B 90  PHE B 95  1 ? 6  
HELX_P HELX_P46 AF1 GLY D 106 ? THR D 115 ? GLY B 106 THR B 115 1 ? 10 
HELX_P HELX_P47 AF2 THR D 115 ? ARG D 127 ? THR B 115 ARG B 127 1 ? 13 
HELX_P HELX_P48 AF3 ASN D 155 ? LYS D 166 ? ASN B 155 LYS B 166 1 ? 12 
HELX_P HELX_P49 AF4 GLY D 181 ? PHE D 188 ? GLY B 181 PHE B 188 1 ? 8  
HELX_P HELX_P50 AF5 ALA D 217 ? LYS D 221 ? ALA B 217 LYS B 221 5 ? 5  
HELX_P HELX_P51 AF6 ASP D 234 ? GLN D 254 ? ASP B 234 GLN B 254 1 ? 21 
HELX_P HELX_P52 AF7 ASP D 265 ? LEU D 267 ? ASP B 265 LEU B 267 5 ? 3  
HELX_P HELX_P53 AF8 THR D 278 ? PHE D 292 ? THR B 278 PHE B 292 1 ? 15 
HELX_P HELX_P54 AF9 THR D 305 ? ASP D 322 ? THR B 305 ASP B 322 1 ? 18 
HELX_P HELX_P55 AG1 TYR D 334 ? GLY D 339 ? TYR B 334 GLY B 339 1 ? 6  
HELX_P HELX_P56 AG2 THR D 356 ? ARG D 372 ? THR B 356 ARG B 372 1 ? 17 
# 
_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 
metalc1 metalc ? ? B ASP 177 OD1 ? ? ? 1_555 E ZN . ZN ? ? D ASP 177 D ZN 501 1_555 ? ? ? ? ? ? ? 2.204 ? ? 
metalc2 metalc ? ? B ASP 177 OD2 ? ? ? 1_555 E ZN . ZN ? ? D ASP 177 D ZN 501 1_555 ? ? ? ? ? ? ? 2.503 ? ? 
metalc3 metalc ? ? B HIS 179 ND1 ? ? ? 1_555 E ZN . ZN ? ? D HIS 179 D ZN 501 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc4 metalc ? ? B ASP 265 OD2 ? ? ? 1_555 E ZN . ZN ? ? D ASP 265 D ZN 501 1_555 ? ? ? ? ? ? ? 2.128 ? ? 
metalc5 metalc ? ? D ASP 177 OD1 ? ? ? 1_555 F ZN . ZN ? ? B ASP 177 B ZN 501 1_555 ? ? ? ? ? ? ? 2.204 ? ? 
metalc6 metalc ? ? D ASP 177 OD2 ? ? ? 1_555 F ZN . ZN ? ? B ASP 177 B ZN 501 1_555 ? ? ? ? ? ? ? 2.504 ? ? 
metalc7 metalc ? ? D HIS 179 ND1 ? ? ? 1_555 F ZN . ZN ? ? B HIS 179 B ZN 501 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc8 metalc ? ? D ASP 265 OD2 ? ? ? 1_555 F ZN . ZN ? ? B ASP 265 B ZN 501 1_555 ? ? ? ? ? ? ? 2.127 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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  OD1 ? B ASP 177 ? D ASP 177 ? 1_555 ZN ? E ZN . ? D ZN 501 ? 1_555 OD2 ? B ASP 177 ? D ASP 177 ? 1_555 55.2  ? 
2  OD1 ? B ASP 177 ? D ASP 177 ? 1_555 ZN ? E ZN . ? D ZN 501 ? 1_555 ND1 ? B HIS 179 ? D HIS 179 ? 1_555 105.3 ? 
3  OD2 ? B ASP 177 ? D ASP 177 ? 1_555 ZN ? E ZN . ? D ZN 501 ? 1_555 ND1 ? B HIS 179 ? D HIS 179 ? 1_555 135.6 ? 
4  OD1 ? B ASP 177 ? D ASP 177 ? 1_555 ZN ? E ZN . ? D ZN 501 ? 1_555 OD2 ? B ASP 265 ? D ASP 265 ? 1_555 86.0  ? 
5  OD2 ? B ASP 177 ? D ASP 177 ? 1_555 ZN ? E ZN . ? D ZN 501 ? 1_555 OD2 ? B ASP 265 ? D ASP 265 ? 1_555 121.3 ? 
6  ND1 ? B HIS 179 ? D HIS 179 ? 1_555 ZN ? E ZN . ? D ZN 501 ? 1_555 OD2 ? B ASP 265 ? D ASP 265 ? 1_555 92.5  ? 
7  OD1 ? D ASP 177 ? B ASP 177 ? 1_555 ZN ? F ZN . ? B ZN 501 ? 1_555 OD2 ? D ASP 177 ? B ASP 177 ? 1_555 55.1  ? 
8  OD1 ? D ASP 177 ? B ASP 177 ? 1_555 ZN ? F ZN . ? B ZN 501 ? 1_555 ND1 ? D HIS 179 ? B HIS 179 ? 1_555 105.3 ? 
9  OD2 ? D ASP 177 ? B ASP 177 ? 1_555 ZN ? F ZN . ? B ZN 501 ? 1_555 ND1 ? D HIS 179 ? B HIS 179 ? 1_555 135.6 ? 
10 OD1 ? D ASP 177 ? B ASP 177 ? 1_555 ZN ? F ZN . ? B ZN 501 ? 1_555 OD2 ? D ASP 265 ? B ASP 265 ? 1_555 86.0  ? 
11 OD2 ? D ASP 177 ? B ASP 177 ? 1_555 ZN ? F ZN . ? B ZN 501 ? 1_555 OD2 ? D ASP 265 ? B ASP 265 ? 1_555 121.4 ? 
12 ND1 ? D HIS 179 ? B HIS 179 ? 1_555 ZN ? F ZN . ? B ZN 501 ? 1_555 OD2 ? D ASP 265 ? B ASP 265 ? 1_555 92.5  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 2 ? 
AA9 ? 3 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 8 ? 
AB4 ? 4 ? 
AB5 ? 4 ? 
AB6 ? 2 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 2 ? 
AC1 ? 3 ? 
AC2 ? 4 ? 
AC3 ? 4 ? 
AC4 ? 8 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? parallel      
AB3 5 6 ? parallel      
AB3 6 7 ? parallel      
AB3 7 8 ? parallel      
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC1 2 3 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? parallel      
AC4 2 3 ? parallel      
AC4 3 4 ? parallel      
AC4 4 5 ? parallel      
AC4 5 6 ? parallel      
AC4 6 7 ? parallel      
AC4 7 8 ? 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 THR A 20  ? LYS A 22  ? THR A 36  LYS A 38  
AA1 2 THR C 107 ? LYS C 109 ? THR C 123 LYS C 125 
AA2 1 THR A 107 ? LYS A 109 ? THR A 123 LYS A 125 
AA2 2 THR C 20  ? LYS C 22  ? THR C 36  LYS C 38  
AA3 1 ILE A 265 ? ASN A 271 ? ILE A 281 ASN A 287 
AA3 2 ALA A 254 ? CYS A 259 ? ALA A 270 CYS A 275 
AA3 3 LEU A 242 ? GLY A 244 ? LEU A 258 GLY A 260 
AA3 4 LEU A 515 ? VAL A 518 ? LEU A 531 VAL A 534 
AA4 1 ILE A 277 ? ALA A 280 ? ILE A 293 ALA A 296 
AA4 2 TYR A 288 ? GLY A 291 ? TYR A 304 GLY A 307 
AA4 3 ARG A 299 ? LYS A 302 ? ARG A 315 LYS A 318 
AA4 4 GLU A 311 ? TRP A 312 ? GLU A 327 TRP A 328 
AA5 1 ARG A 320 ? LEU A 321 ? ARG A 336 LEU A 337 
AA5 2 LYS A 340 ? THR A 341 ? LYS A 356 THR A 357 
AA6 1 THR A 324 ? VAL A 328 ? THR A 340 VAL A 344 
AA6 2 ALA A 333 ? LEU A 337 ? ALA A 349 LEU A 353 
AA6 3 VAL A 350 ? ARG A 354 ? VAL A 366 ARG A 370 
AA6 4 VAL A 359 ? THR A 363 ? VAL A 375 THR A 379 
AA7 1 ALA A 374 ? LEU A 378 ? ALA A 390 LEU A 394 
AA7 2 ILE A 381 ? LEU A 385 ? ILE A 397 LEU A 401 
AA7 3 ILE A 402 ? ASP A 406 ? ILE A 418 ASP A 422 
AA7 4 LYS A 411 ? VAL A 414 ? LYS A 427 VAL A 430 
AA8 1 GLU A 388 ? ASP A 391 ? GLU A 404 ASP A 407 
AA8 2 PHE A 395 ? PRO A 398 ? PHE A 411 PRO A 414 
AA9 1 MET A 425 ? HIS A 426 ? MET A 441 HIS A 442 
AA9 2 LEU A 433 ? ALA A 438 ? LEU A 449 ALA A 454 
AA9 3 VAL A 429 ? HIS A 430 ? VAL A 445 HIS A 446 
AB1 1 MET A 425 ? HIS A 426 ? MET A 441 HIS A 442 
AB1 2 LEU A 433 ? ALA A 438 ? LEU A 449 ALA A 454 
AB1 3 LEU A 443 ? TYR A 446 ? LEU A 459 TYR A 462 
AB1 4 PHE A 453 ? ARG A 455 ? PHE A 469 ARG A 471 
AB2 1 LYS A 470 ? SER A 473 ? LYS A 486 SER A 489 
AB2 2 ILE A 478 ? PHE A 481 ? ILE A 494 PHE A 497 
AB2 3 THR A 492 ? LEU A 495 ? THR A 508 LEU A 511 
AB2 4 VAL A 502 ? VAL A 504 ? VAL A 518 VAL A 520 
AB3 1 GLU B 53  ? TYR B 55  ? GLU D 53  TYR D 55  
AB3 2 VAL B 12  ? TYR B 15  ? VAL D 12  TYR D 15  
AB3 3 MET B 132 ? ASN B 135 ? MET D 132 ASN D 135 
AB3 4 LEU B 296 ? GLY B 301 ? LEU D 296 GLY D 301 
AB3 5 VAL B 258 ? GLY B 263 ? VAL D 258 GLY D 263 
AB3 6 VAL B 171 ? ILE B 176 ? VAL D 171 ILE D 176 
AB3 7 VAL B 194 ? LYS B 201 ? VAL D 194 LYS D 201 
AB3 8 ASN B 226 ? MET B 229 ? ASN D 226 MET D 229 
AB4 1 ILE C 265 ? ASN C 271 ? ILE C 281 ASN C 287 
AB4 2 ALA C 254 ? CYS C 259 ? ALA C 270 CYS C 275 
AB4 3 LEU C 242 ? GLY C 244 ? LEU C 258 GLY C 260 
AB4 4 LEU C 515 ? VAL C 518 ? LEU C 531 VAL C 534 
AB5 1 ILE C 277 ? HIS C 283 ? ILE C 293 HIS C 299 
AB5 2 ASP C 286 ? GLY C 291 ? ASP C 302 GLY C 307 
AB5 3 ARG C 299 ? LYS C 302 ? ARG C 315 LYS C 318 
AB5 4 GLU C 311 ? TRP C 312 ? GLU C 327 TRP C 328 
AB6 1 ARG C 320 ? LEU C 321 ? ARG C 336 LEU C 337 
AB6 2 LYS C 340 ? THR C 341 ? LYS C 356 THR C 357 
AB7 1 THR C 324 ? VAL C 328 ? THR C 340 VAL C 344 
AB7 2 ALA C 333 ? LEU C 337 ? ALA C 349 LEU C 353 
AB7 3 VAL C 350 ? ARG C 354 ? VAL C 366 ARG C 370 
AB7 4 VAL C 359 ? THR C 363 ? VAL C 375 THR C 379 
AB8 1 ALA C 374 ? LEU C 378 ? ALA C 390 LEU C 394 
AB8 2 ILE C 381 ? LEU C 385 ? ILE C 397 LEU C 401 
AB8 3 ILE C 402 ? ASP C 406 ? ILE C 418 ASP C 422 
AB8 4 LYS C 411 ? VAL C 414 ? LYS C 427 VAL C 430 
AB9 1 GLU C 388 ? ASP C 391 ? GLU C 404 ASP C 407 
AB9 2 PHE C 395 ? PRO C 398 ? PHE C 411 PRO C 414 
AC1 1 MET C 425 ? HIS C 426 ? MET C 441 HIS C 442 
AC1 2 LEU C 433 ? ALA C 438 ? LEU C 449 ALA C 454 
AC1 3 VAL C 429 ? HIS C 430 ? VAL C 445 HIS C 446 
AC2 1 MET C 425 ? HIS C 426 ? MET C 441 HIS C 442 
AC2 2 LEU C 433 ? ALA C 438 ? LEU C 449 ALA C 454 
AC2 3 LEU C 443 ? TYR C 446 ? LEU C 459 TYR C 462 
AC2 4 PHE C 453 ? ARG C 455 ? PHE C 469 ARG C 471 
AC3 1 LYS C 470 ? SER C 473 ? LYS C 486 SER C 489 
AC3 2 ILE C 478 ? PHE C 481 ? ILE C 494 PHE C 497 
AC3 3 THR C 492 ? LEU C 495 ? THR C 508 LEU C 511 
AC3 4 VAL C 502 ? VAL C 504 ? VAL C 518 VAL C 520 
AC4 1 GLU D 53  ? TYR D 55  ? GLU B 53  TYR B 55  
AC4 2 VAL D 12  ? TYR D 15  ? VAL B 12  TYR B 15  
AC4 3 MET D 132 ? ASN D 135 ? MET B 132 ASN B 135 
AC4 4 LEU D 296 ? GLY D 301 ? LEU B 296 GLY B 301 
AC4 5 VAL D 258 ? GLY D 263 ? VAL B 258 GLY B 263 
AC4 6 VAL D 171 ? ILE D 176 ? VAL B 171 ILE B 176 
AC4 7 VAL D 194 ? LYS D 201 ? VAL B 194 LYS B 201 
AC4 8 ASN D 226 ? MET D 229 ? ASN B 226 MET B 229 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 21  ? N PHE A 37  O VAL C 108 ? O VAL C 124 
AA2 1 2 N VAL A 108 ? N VAL A 124 O PHE C 21  ? O PHE C 37  
AA3 1 2 O SER A 266 ? O SER A 282 N HIS A 258 ? N HIS A 274 
AA3 2 3 O VAL A 255 ? O VAL A 271 N LEU A 242 ? N LEU A 258 
AA3 3 4 N ILE A 243 ? N ILE A 259 O PHE A 517 ? O PHE A 533 
AA4 1 2 N ALA A 279 ? N ALA A 295 O VAL A 290 ? O VAL A 306 
AA4 2 3 N VAL A 289 ? N VAL A 305 O TRP A 301 ? O TRP A 317 
AA4 3 4 N LYS A 302 ? N LYS A 318 O GLU A 311 ? O GLU A 327 
AA5 1 2 N LEU A 321 ? N LEU A 337 O LYS A 340 ? O LYS A 356 
AA6 1 2 N VAL A 326 ? N VAL A 342 O TYR A 335 ? O TYR A 351 
AA6 2 3 N SER A 336 ? N SER A 352 O ILE A 351 ? O ILE A 367 
AA6 3 4 N TYR A 352 ? N TYR A 368 O THR A 361 ? O THR A 377 
AA7 1 2 N LEU A 378 ? N LEU A 394 O ILE A 381 ? O ILE A 397 
AA7 2 3 N ILE A 382 ? N ILE A 398 O PHE A 405 ? O PHE A 421 
AA7 3 4 N ASP A 406 ? N ASP A 422 O LYS A 411 ? O LYS A 427 
AA8 1 2 N GLU A 389 ? N GLU A 405 O LYS A 397 ? O LYS A 413 
AA9 1 2 N HIS A 426 ? N HIS A 442 O VAL A 437 ? O VAL A 453 
AA9 2 3 O LEU A 433 ? O LEU A 449 N HIS A 430 ? N HIS A 446 
AB1 1 2 N HIS A 426 ? N HIS A 442 O VAL A 437 ? O VAL A 453 
AB1 2 3 N VAL A 434 ? N VAL A 450 O TYR A 446 ? O TYR A 462 
AB1 3 4 N CYS A 445 ? N CYS A 461 O THR A 454 ? O THR A 470 
AB2 1 2 N ALA A 472 ? N ALA A 488 O TYR A 479 ? O TYR A 495 
AB2 2 3 N ILE A 478 ? N ILE A 494 O LEU A 495 ? O LEU A 511 
AB2 3 4 N LYS A 494 ? N LYS A 510 O THR A 503 ? O THR A 519 
AB3 1 2 O GLU B 53  ? O GLU D 53  N TYR B 14  ? N TYR D 14  
AB3 2 3 N CYS B 13  ? N CYS D 13  O VAL B 134 ? O VAL D 134 
AB3 3 4 N ASN B 135 ? N ASN D 135 O GLY B 300 ? O GLY D 300 
AB3 4 5 O LEU B 297 ? O LEU D 297 N LEU B 260 ? N LEU D 260 
AB3 5 6 O GLN B 261 ? O GLN D 261 N ILE B 174 ? N ILE D 174 
AB3 6 7 N TYR B 173 ? N TYR D 173 O MET B 195 ? O MET D 195 
AB3 7 8 N SER B 198 ? N SER D 198 O PHE B 227 ? O PHE D 227 
AB4 1 2 O SER C 266 ? O SER C 282 N HIS C 258 ? N HIS C 274 
AB4 2 3 O VAL C 255 ? O VAL C 271 N LEU C 242 ? N LEU C 258 
AB4 3 4 N ILE C 243 ? N ILE C 259 O PHE C 517 ? O PHE C 533 
AB5 1 2 N HIS C 283 ? N HIS C 299 O ASP C 286 ? O ASP C 302 
AB5 2 3 N GLY C 291 ? N GLY C 307 O ARG C 299 ? O ARG C 315 
AB5 3 4 N LYS C 302 ? N LYS C 318 O GLU C 311 ? O GLU C 327 
AB6 1 2 N LEU C 321 ? N LEU C 337 O LYS C 340 ? O LYS C 356 
AB7 1 2 N VAL C 326 ? N VAL C 342 O TYR C 335 ? O TYR C 351 
AB7 2 3 N SER C 336 ? N SER C 352 O ILE C 351 ? O ILE C 367 
AB7 3 4 N TYR C 352 ? N TYR C 368 O THR C 361 ? O THR C 377 
AB8 1 2 N LEU C 378 ? N LEU C 394 O ILE C 381 ? O ILE C 397 
AB8 2 3 N ILE C 382 ? N ILE C 398 O PHE C 405 ? O PHE C 421 
AB8 3 4 N ASP C 406 ? N ASP C 422 O LYS C 411 ? O LYS C 427 
AB9 1 2 N GLU C 389 ? N GLU C 405 O LYS C 397 ? O LYS C 413 
AC1 1 2 N HIS C 426 ? N HIS C 442 O VAL C 437 ? O VAL C 453 
AC1 2 3 O LEU C 433 ? O LEU C 449 N HIS C 430 ? N HIS C 446 
AC2 1 2 N HIS C 426 ? N HIS C 442 O VAL C 437 ? O VAL C 453 
AC2 2 3 N ILE C 436 ? N ILE C 452 O VAL C 444 ? O VAL C 460 
AC2 3 4 N CYS C 445 ? N CYS C 461 O THR C 454 ? O THR C 470 
AC3 1 2 N ALA C 472 ? N ALA C 488 O TYR C 479 ? O TYR C 495 
AC3 2 3 N ILE C 478 ? N ILE C 494 O LEU C 495 ? O LEU C 511 
AC3 3 4 N LYS C 494 ? N LYS C 510 O THR C 503 ? O THR C 519 
AC4 1 2 O GLU D 53  ? O GLU B 53  N TYR D 14  ? N TYR B 14  
AC4 2 3 N CYS D 13  ? N CYS B 13  O VAL D 134 ? O VAL B 134 
AC4 3 4 N ASN D 135 ? N ASN B 135 O GLY D 300 ? O GLY B 300 
AC4 4 5 O LEU D 297 ? O LEU B 297 N LEU D 260 ? N LEU B 260 
AC4 5 6 O GLN D 261 ? O GLN B 261 N ILE D 174 ? N ILE B 174 
AC4 6 7 N TYR D 173 ? N TYR B 173 O MET D 195 ? O MET B 195 
AC4 7 8 N SER D 198 ? N SER B 198 O PHE D 227 ? O PHE B 227 
# 
_pdbx_entry_details.entry_id                   9GGM 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG  D SER 118 ? ? OD2 D ASP 156 ? ? 2.09 
2 1 OG  B SER 118 ? ? OD2 B ASP 156 ? ? 2.09 
3 1 OD2 B ASP 235 ? ? OG1 B THR 278 ? ? 2.15 
4 1 OD2 D ASP 235 ? ? OG1 D THR 278 ? ? 2.15 
5 1 OG1 C THR 340 ? ? O   C ALA 389 ? ? 2.17 
6 1 OG1 A THR 340 ? ? O   A ALA 389 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A PRO 464 ? ? N  A PRO 464 ? ? CD A PRO 464 ? ? 94.62  111.70 -17.08 1.40 N 
2 1 CA D LEU 344 ? ? CB D LEU 344 ? ? CG D LEU 344 ? ? 129.89 115.30 14.59  2.30 N 
3 1 CA B LEU 344 ? ? CB B LEU 344 ? ? CG B LEU 344 ? ? 129.89 115.30 14.59  2.30 N 
# 
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 TRP A 326 ? ? 71.98   32.14   
2  1 ASP A 409 ? ? 73.28   -5.77   
3  1 LYS A 447 ? ? 56.40   -118.32 
4  1 GLU A 455 ? ? 58.83   -129.05 
5  1 CYS A 490 ? ? -117.67 -169.96 
6  1 ASN D 84  ? ? -93.22  32.74   
7  1 GLU D 99  ? ? -110.96 -75.27  
8  1 GLU D 204 ? ? -94.72  58.06   
9  1 ASN D 350 ? ? -99.83  31.74   
10 1 TRP C 326 ? ? 71.95   32.30   
11 1 ASP C 409 ? ? 73.28   -5.67   
12 1 LYS C 447 ? ? 56.64   -118.19 
13 1 GLU C 455 ? ? 58.70   -128.98 
14 1 CYS C 490 ? ? -117.68 -169.96 
15 1 ASN B 84  ? ? -93.26  32.77   
16 1 GLU B 99  ? ? -110.93 -75.28  
17 1 GLU B 204 ? ? -94.72  58.01   
18 1 ASN B 350 ? ? -99.87  31.75   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9GGM 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   107.7 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
loop_
_em_3d_fitting_list.id 
_em_3d_fitting_list.3d_fitting_id 
_em_3d_fitting_list.pdb_entry_id 
_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 
_em_3d_fitting_list.type 
_em_3d_fitting_list.accession_code 
_em_3d_fitting_list.initial_refinement_model_id 
1 1 7ZZT ? ? ? ? ? PDB       'experimental model' 7ZZT         1 
2 1 .    . . ? ? ? AlphaFold 'in silico model'    AF-Q9N010-F1 2 
# 
_em_3d_reconstruction.entry_id                    9GGM 
_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                  2.71 
_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               295217 
_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            7.5 
# 
_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                 'KBTBD4 R313PRR cancer mutant in complex with HDAC2 at 2:2 stoichiometry' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       '1, 2' 
# 
_em_image_scans.entry_id                9GGM 
_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        4092 
_em_image_scans.dimension_width         5760 
_em_image_scans.frames_per_image        ? 
_em_image_scans.image_recording_id      1 
_em_image_scans.used_frames_per_image   ? 
# 
_em_imaging.entry_id                        9GGM 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2800 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           105000 
_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                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'UltrAuFoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9GGM 
_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   277.15 
_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                9GGM 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9GGM 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 17  ? A MET 1   
2   1 Y 1 A GLU 18  ? A GLU 2   
3   1 Y 1 A SER 19  ? A SER 3   
4   1 Y 1 A PRO 20  ? A PRO 4   
5   1 Y 1 A GLU 21  ? A GLU 5   
6   1 Y 1 A GLU 22  ? A GLU 6   
7   1 Y 1 A PRO 23  ? A PRO 7   
8   1 Y 1 A GLY 24  ? A GLY 8   
9   1 Y 1 A ALA 25  ? A ALA 9   
10  1 Y 1 A SER 26  ? A SER 10  
11  1 Y 1 A MET 27  ? A MET 11  
12  1 Y 1 A ASP 28  ? A ASP 12  
13  1 Y 1 A GLU 29  ? A GLU 13  
14  1 Y 1 A ASN 30  ? A ASN 14  
15  1 Y 1 A TYR 31  ? A TYR 15  
16  1 Y 1 A GLU 58  ? A GLU 42  
17  1 Y 1 A LEU 59  ? A LEU 43  
18  1 Y 1 A PHE 60  ? A PHE 44  
19  1 Y 1 A ALA 61  ? A ALA 45  
20  1 Y 1 A ASP 62  ? A ASP 46  
21  1 Y 1 A VAL 63  ? A VAL 47  
22  1 Y 1 A THR 64  ? A THR 48  
23  1 Y 1 A ILE 65  ? A ILE 49  
24  1 Y 1 A SER 66  ? A SER 50  
25  1 Y 1 A VAL 67  ? A VAL 51  
26  1 Y 1 A GLU 68  ? A GLU 52  
27  1 Y 1 A GLY 69  ? A GLY 53  
28  1 Y 1 A ARG 70  ? A ARG 54  
29  1 Y 1 A GLU 71  ? A GLU 55  
30  1 Y 1 A PHE 72  ? A PHE 56  
31  1 Y 1 A GLN 73  ? A GLN 57  
32  1 Y 1 A LEU 74  ? A LEU 58  
33  1 Y 1 A HIS 75  ? A HIS 59  
34  1 Y 1 A THR 91  ? A THR 75  
35  1 Y 1 A SER 92  ? A SER 76  
36  1 Y 1 A ASN 93  ? A ASN 77  
37  1 Y 1 A LEU 94  ? A LEU 78  
38  1 Y 1 A LYS 95  ? A LYS 79  
39  1 Y 1 A GLU 96  ? A GLU 80  
40  1 Y 1 A ALA 97  ? A ALA 81  
41  1 Y 1 A HIS 98  ? A HIS 82  
42  1 Y 1 A ASN 99  ? A ASN 83  
43  1 Y 1 A ARG 100 ? A ARG 84  
44  1 Y 1 A VAL 101 ? A VAL 85  
45  1 Y 1 A ILE 102 ? A ILE 86  
46  1 Y 1 A VAL 103 ? A VAL 87  
47  1 Y 1 A LEU 104 ? A LEU 88  
48  1 Y 1 A ARG 156 ? A ARG 140 
49  1 Y 1 A THR 157 ? A THR 141 
50  1 Y 1 A VAL 158 ? A VAL 142 
51  1 Y 1 A GLN 159 ? A GLN 143 
52  1 Y 1 A VAL 160 ? A VAL 144 
53  1 Y 1 A ASN 195 ? A ASN 179 
54  1 Y 1 A THR 196 ? A THR 180 
55  1 Y 1 A GLU 197 ? A GLU 181 
56  1 Y 1 A GLU 198 ? A GLU 182 
57  1 Y 1 A PHE 199 ? A PHE 183 
58  1 Y 1 A LEU 200 ? A LEU 184 
59  1 Y 1 A HIS 201 ? A HIS 185 
60  1 Y 1 A LEU 202 ? A LEU 186 
61  1 Y 1 A PRO 203 ? A PRO 187 
62  1 Y 1 A PRO 216 ? A PRO 200 
63  1 Y 1 A CYS 217 ? A CYS 201 
64  1 Y 1 A SER 218 ? A SER 202 
65  1 Y 1 A TRP 228 ? A TRP 212 
66  1 Y 1 A ILE 229 ? A ILE 213 
67  1 Y 1 A ASN 230 ? A ASN 214 
68  1 Y 1 A PHE 231 ? A PHE 215 
69  1 Y 1 A ASN 232 ? A ASN 216 
70  1 Y 1 A LYS 233 ? A LYS 217 
71  1 Y 1 A GLU 234 ? A GLU 218 
72  1 Y 1 A GLU 235 ? A GLU 219 
73  1 Y 1 A ARG 236 ? A ARG 220 
74  1 Y 1 A GLU 237 ? A GLU 221 
75  1 Y 1 A ALA 238 ? A ALA 222 
76  1 Y 1 A PHE 239 ? A PHE 223 
77  1 Y 1 A ALA 240 ? A ALA 224 
78  1 Y 1 A GLU 241 ? A GLU 225 
79  1 Y 1 A SER 242 ? A SER 226 
80  1 Y 1 A GLU 262 ? A GLU 246 
81  1 Y 1 A SER 263 ? A SER 247 
82  1 Y 1 A SER 264 ? A SER 248 
83  1 Y 1 A ARG 265 ? A ARG 249 
84  1 Y 1 A THR 266 ? A THR 250 
85  1 Y 1 A HIS 267 ? A HIS 251 
86  1 Y 1 A ASP 278 ? A ASP 262 
87  1 Y 1 A ASP 279 ? A ASP 263 
88  1 Y 1 A ASN 321 ? A ASN 305 
89  1 Y 1 A ALA 322 ? A ALA 306 
90  1 Y 1 A THR 323 ? A THR 307 
91  1 Y 1 A TRP 478 ? A TRP 462 
92  1 Y 1 A SER 479 ? A SER 463 
93  1 Y 1 A SER 480 ? A SER 464 
94  1 Y 1 A ALA 481 ? A ALA 465 
95  1 Y 1 A PRO 482 ? A PRO 466 
96  1 Y 1 A SER 483 ? A SER 467 
97  1 Y 1 A LYS 502 ? A LYS 486 
98  1 Y 1 A LYS 503 ? A LYS 487 
99  1 Y 1 A GLY 504 ? A GLY 488 
100 1 Y 1 A ASP 505 ? A ASP 489 
101 1 Y 1 A ARG 522 ? A ARG 506 
102 1 Y 1 A GLY 523 ? A GLY 507 
103 1 Y 1 A ILE 524 ? A ILE 508 
104 1 Y 1 D MET 1   ? B MET 1   
105 1 Y 1 D ALA 2   ? B ALA 2   
106 1 Y 1 D TYR 3   ? B TYR 3   
107 1 Y 1 D SER 4   ? B SER 4   
108 1 Y 1 D GLN 5   ? B GLN 5   
109 1 Y 1 D GLY 6   ? B GLY 6   
110 1 Y 1 D GLY 7   ? B GLY 7   
111 1 Y 1 D GLY 8   ? B GLY 8   
112 1 Y 1 D HIS 376 ? B HIS 376 
113 1 Y 1 D ALA 377 ? B ALA 377 
114 1 Y 1 D PRO 378 ? B PRO 378 
115 1 Y 1 D GLY 379 ? B GLY 379 
116 1 Y 1 D VAL 380 ? B VAL 380 
117 1 Y 1 D GLN 381 ? B GLN 381 
118 1 Y 1 D MET 382 ? B MET 382 
119 1 Y 1 D GLN 383 ? B GLN 383 
120 1 Y 1 D ALA 384 ? B ALA 384 
121 1 Y 1 D ILE 385 ? B ILE 385 
122 1 Y 1 D PRO 386 ? B PRO 386 
123 1 Y 1 D GLU 387 ? B GLU 387 
124 1 Y 1 D ASP 388 ? B ASP 388 
125 1 Y 1 D ALA 389 ? B ALA 389 
126 1 Y 1 D VAL 390 ? B VAL 390 
127 1 Y 1 D HIS 391 ? B HIS 391 
128 1 Y 1 D GLU 392 ? B GLU 392 
129 1 Y 1 D ASP 393 ? B ASP 393 
130 1 Y 1 D SER 394 ? B SER 394 
131 1 Y 1 D GLY 395 ? B GLY 395 
132 1 Y 1 D ASP 396 ? B ASP 396 
133 1 Y 1 D GLU 397 ? B GLU 397 
134 1 Y 1 D ASP 398 ? B ASP 398 
135 1 Y 1 D GLY 399 ? B GLY 399 
136 1 Y 1 D GLU 400 ? B GLU 400 
137 1 Y 1 D ASP 401 ? B ASP 401 
138 1 Y 1 D PRO 402 ? B PRO 402 
139 1 Y 1 D ASP 403 ? B ASP 403 
140 1 Y 1 D LYS 404 ? B LYS 404 
141 1 Y 1 D ARG 405 ? B ARG 405 
142 1 Y 1 D ILE 406 ? B ILE 406 
143 1 Y 1 D SER 407 ? B SER 407 
144 1 Y 1 D ILE 408 ? B ILE 408 
145 1 Y 1 D ARG 409 ? B ARG 409 
146 1 Y 1 D ALA 410 ? B ALA 410 
147 1 Y 1 D SER 411 ? B SER 411 
148 1 Y 1 D ASP 412 ? B ASP 412 
149 1 Y 1 D LYS 413 ? B LYS 413 
150 1 Y 1 D ARG 414 ? B ARG 414 
151 1 Y 1 D ILE 415 ? B ILE 415 
152 1 Y 1 D ALA 416 ? B ALA 416 
153 1 Y 1 D CYS 417 ? B CYS 417 
154 1 Y 1 D ASP 418 ? B ASP 418 
155 1 Y 1 D GLU 419 ? B GLU 419 
156 1 Y 1 D GLU 420 ? B GLU 420 
157 1 Y 1 D PHE 421 ? B PHE 421 
158 1 Y 1 D SER 422 ? B SER 422 
159 1 Y 1 D ASP 423 ? B ASP 423 
160 1 Y 1 D SER 424 ? B SER 424 
161 1 Y 1 D GLU 425 ? B GLU 425 
162 1 Y 1 D ASP 426 ? B ASP 426 
163 1 Y 1 D GLU 427 ? B GLU 427 
164 1 Y 1 D GLY 428 ? B GLY 428 
165 1 Y 1 D GLU 429 ? B GLU 429 
166 1 Y 1 D GLY 430 ? B GLY 430 
167 1 Y 1 D GLY 431 ? B GLY 431 
168 1 Y 1 D ARG 432 ? B ARG 432 
169 1 Y 1 D ARG 433 ? B ARG 433 
170 1 Y 1 D ASN 434 ? B ASN 434 
171 1 Y 1 D VAL 435 ? B VAL 435 
172 1 Y 1 D ALA 436 ? B ALA 436 
173 1 Y 1 D ASP 437 ? B ASP 437 
174 1 Y 1 D HIS 438 ? B HIS 438 
175 1 Y 1 D LYS 439 ? B LYS 439 
176 1 Y 1 D LYS 440 ? B LYS 440 
177 1 Y 1 D GLY 441 ? B GLY 441 
178 1 Y 1 D ALA 442 ? B ALA 442 
179 1 Y 1 D LYS 443 ? B LYS 443 
180 1 Y 1 D LYS 444 ? B LYS 444 
181 1 Y 1 D ALA 445 ? B ALA 445 
182 1 Y 1 D ARG 446 ? B ARG 446 
183 1 Y 1 D ILE 447 ? B ILE 447 
184 1 Y 1 D GLU 448 ? B GLU 448 
185 1 Y 1 D GLU 449 ? B GLU 449 
186 1 Y 1 D ASP 450 ? B ASP 450 
187 1 Y 1 D LYS 451 ? B LYS 451 
188 1 Y 1 D LYS 452 ? B LYS 452 
189 1 Y 1 D GLU 453 ? B GLU 453 
190 1 Y 1 D THR 454 ? B THR 454 
191 1 Y 1 D GLU 455 ? B GLU 455 
192 1 Y 1 D ASP 456 ? B ASP 456 
193 1 Y 1 D LYS 457 ? B LYS 457 
194 1 Y 1 D LYS 458 ? B LYS 458 
195 1 Y 1 D THR 459 ? B THR 459 
196 1 Y 1 D ASP 460 ? B ASP 460 
197 1 Y 1 D VAL 461 ? B VAL 461 
198 1 Y 1 D LYS 462 ? B LYS 462 
199 1 Y 1 D GLU 463 ? B GLU 463 
200 1 Y 1 D GLU 464 ? B GLU 464 
201 1 Y 1 D ASP 465 ? B ASP 465 
202 1 Y 1 D LYS 466 ? B LYS 466 
203 1 Y 1 D SER 467 ? B SER 467 
204 1 Y 1 D LYS 468 ? B LYS 468 
205 1 Y 1 D ASP 469 ? B ASP 469 
206 1 Y 1 D ASN 470 ? B ASN 470 
207 1 Y 1 D SER 471 ? B SER 471 
208 1 Y 1 D GLY 472 ? B GLY 472 
209 1 Y 1 D GLU 473 ? B GLU 473 
210 1 Y 1 D LYS 474 ? B LYS 474 
211 1 Y 1 D THR 475 ? B THR 475 
212 1 Y 1 D ASP 476 ? B ASP 476 
213 1 Y 1 D THR 477 ? B THR 477 
214 1 Y 1 D LYS 478 ? B LYS 478 
215 1 Y 1 D GLY 479 ? B GLY 479 
216 1 Y 1 D THR 480 ? B THR 480 
217 1 Y 1 D LYS 481 ? B LYS 481 
218 1 Y 1 D SER 482 ? B SER 482 
219 1 Y 1 D GLU 483 ? B GLU 483 
220 1 Y 1 D GLN 484 ? B GLN 484 
221 1 Y 1 D LEU 485 ? B LEU 485 
222 1 Y 1 D SER 486 ? B SER 486 
223 1 Y 1 D ASN 487 ? B ASN 487 
224 1 Y 1 D PRO 488 ? B PRO 488 
225 1 Y 1 C MET 17  ? C MET 1   
226 1 Y 1 C GLU 18  ? C GLU 2   
227 1 Y 1 C SER 19  ? C SER 3   
228 1 Y 1 C PRO 20  ? C PRO 4   
229 1 Y 1 C GLU 21  ? C GLU 5   
230 1 Y 1 C GLU 22  ? C GLU 6   
231 1 Y 1 C PRO 23  ? C PRO 7   
232 1 Y 1 C GLY 24  ? C GLY 8   
233 1 Y 1 C ALA 25  ? C ALA 9   
234 1 Y 1 C SER 26  ? C SER 10  
235 1 Y 1 C MET 27  ? C MET 11  
236 1 Y 1 C ASP 28  ? C ASP 12  
237 1 Y 1 C GLU 29  ? C GLU 13  
238 1 Y 1 C ASN 30  ? C ASN 14  
239 1 Y 1 C TYR 31  ? C TYR 15  
240 1 Y 1 C GLU 58  ? C GLU 42  
241 1 Y 1 C LEU 59  ? C LEU 43  
242 1 Y 1 C PHE 60  ? C PHE 44  
243 1 Y 1 C ALA 61  ? C ALA 45  
244 1 Y 1 C ASP 62  ? C ASP 46  
245 1 Y 1 C VAL 63  ? C VAL 47  
246 1 Y 1 C THR 64  ? C THR 48  
247 1 Y 1 C ILE 65  ? C ILE 49  
248 1 Y 1 C SER 66  ? C SER 50  
249 1 Y 1 C VAL 67  ? C VAL 51  
250 1 Y 1 C GLU 68  ? C GLU 52  
251 1 Y 1 C GLY 69  ? C GLY 53  
252 1 Y 1 C ARG 70  ? C ARG 54  
253 1 Y 1 C GLU 71  ? C GLU 55  
254 1 Y 1 C PHE 72  ? C PHE 56  
255 1 Y 1 C GLN 73  ? C GLN 57  
256 1 Y 1 C LEU 74  ? C LEU 58  
257 1 Y 1 C HIS 75  ? C HIS 59  
258 1 Y 1 C THR 91  ? C THR 75  
259 1 Y 1 C SER 92  ? C SER 76  
260 1 Y 1 C ASN 93  ? C ASN 77  
261 1 Y 1 C LEU 94  ? C LEU 78  
262 1 Y 1 C LYS 95  ? C LYS 79  
263 1 Y 1 C GLU 96  ? C GLU 80  
264 1 Y 1 C ALA 97  ? C ALA 81  
265 1 Y 1 C HIS 98  ? C HIS 82  
266 1 Y 1 C ASN 99  ? C ASN 83  
267 1 Y 1 C ARG 100 ? C ARG 84  
268 1 Y 1 C VAL 101 ? C VAL 85  
269 1 Y 1 C ILE 102 ? C ILE 86  
270 1 Y 1 C VAL 103 ? C VAL 87  
271 1 Y 1 C LEU 104 ? C LEU 88  
272 1 Y 1 C ARG 156 ? C ARG 140 
273 1 Y 1 C THR 157 ? C THR 141 
274 1 Y 1 C VAL 158 ? C VAL 142 
275 1 Y 1 C GLN 159 ? C GLN 143 
276 1 Y 1 C VAL 160 ? C VAL 144 
277 1 Y 1 C ASN 195 ? C ASN 179 
278 1 Y 1 C THR 196 ? C THR 180 
279 1 Y 1 C GLU 197 ? C GLU 181 
280 1 Y 1 C GLU 198 ? C GLU 182 
281 1 Y 1 C PHE 199 ? C PHE 183 
282 1 Y 1 C LEU 200 ? C LEU 184 
283 1 Y 1 C HIS 201 ? C HIS 185 
284 1 Y 1 C LEU 202 ? C LEU 186 
285 1 Y 1 C PRO 203 ? C PRO 187 
286 1 Y 1 C PRO 216 ? C PRO 200 
287 1 Y 1 C CYS 217 ? C CYS 201 
288 1 Y 1 C SER 218 ? C SER 202 
289 1 Y 1 C TRP 228 ? C TRP 212 
290 1 Y 1 C ILE 229 ? C ILE 213 
291 1 Y 1 C ASN 230 ? C ASN 214 
292 1 Y 1 C PHE 231 ? C PHE 215 
293 1 Y 1 C ASN 232 ? C ASN 216 
294 1 Y 1 C LYS 233 ? C LYS 217 
295 1 Y 1 C GLU 234 ? C GLU 218 
296 1 Y 1 C GLU 235 ? C GLU 219 
297 1 Y 1 C ARG 236 ? C ARG 220 
298 1 Y 1 C GLU 237 ? C GLU 221 
299 1 Y 1 C ALA 238 ? C ALA 222 
300 1 Y 1 C PHE 239 ? C PHE 223 
301 1 Y 1 C ALA 240 ? C ALA 224 
302 1 Y 1 C GLU 241 ? C GLU 225 
303 1 Y 1 C SER 242 ? C SER 226 
304 1 Y 1 C GLU 262 ? C GLU 246 
305 1 Y 1 C SER 263 ? C SER 247 
306 1 Y 1 C SER 264 ? C SER 248 
307 1 Y 1 C ARG 265 ? C ARG 249 
308 1 Y 1 C THR 266 ? C THR 250 
309 1 Y 1 C HIS 267 ? C HIS 251 
310 1 Y 1 C ASP 278 ? C ASP 262 
311 1 Y 1 C ASP 279 ? C ASP 263 
312 1 Y 1 C ASN 321 ? C ASN 305 
313 1 Y 1 C ALA 322 ? C ALA 306 
314 1 Y 1 C THR 323 ? C THR 307 
315 1 Y 1 C TRP 478 ? C TRP 462 
316 1 Y 1 C SER 479 ? C SER 463 
317 1 Y 1 C SER 480 ? C SER 464 
318 1 Y 1 C ALA 481 ? C ALA 465 
319 1 Y 1 C PRO 482 ? C PRO 466 
320 1 Y 1 C SER 483 ? C SER 467 
321 1 Y 1 C LYS 502 ? C LYS 486 
322 1 Y 1 C LYS 503 ? C LYS 487 
323 1 Y 1 C GLY 504 ? C GLY 488 
324 1 Y 1 C ASP 505 ? C ASP 489 
325 1 Y 1 C ARG 522 ? C ARG 506 
326 1 Y 1 C GLY 523 ? C GLY 507 
327 1 Y 1 C ILE 524 ? C ILE 508 
328 1 Y 1 B MET 1   ? D MET 1   
329 1 Y 1 B ALA 2   ? D ALA 2   
330 1 Y 1 B TYR 3   ? D TYR 3   
331 1 Y 1 B SER 4   ? D SER 4   
332 1 Y 1 B GLN 5   ? D GLN 5   
333 1 Y 1 B GLY 6   ? D GLY 6   
334 1 Y 1 B GLY 7   ? D GLY 7   
335 1 Y 1 B GLY 8   ? D GLY 8   
336 1 Y 1 B HIS 376 ? D HIS 376 
337 1 Y 1 B ALA 377 ? D ALA 377 
338 1 Y 1 B PRO 378 ? D PRO 378 
339 1 Y 1 B GLY 379 ? D GLY 379 
340 1 Y 1 B VAL 380 ? D VAL 380 
341 1 Y 1 B GLN 381 ? D GLN 381 
342 1 Y 1 B MET 382 ? D MET 382 
343 1 Y 1 B GLN 383 ? D GLN 383 
344 1 Y 1 B ALA 384 ? D ALA 384 
345 1 Y 1 B ILE 385 ? D ILE 385 
346 1 Y 1 B PRO 386 ? D PRO 386 
347 1 Y 1 B GLU 387 ? D GLU 387 
348 1 Y 1 B ASP 388 ? D ASP 388 
349 1 Y 1 B ALA 389 ? D ALA 389 
350 1 Y 1 B VAL 390 ? D VAL 390 
351 1 Y 1 B HIS 391 ? D HIS 391 
352 1 Y 1 B GLU 392 ? D GLU 392 
353 1 Y 1 B ASP 393 ? D ASP 393 
354 1 Y 1 B SER 394 ? D SER 394 
355 1 Y 1 B GLY 395 ? D GLY 395 
356 1 Y 1 B ASP 396 ? D ASP 396 
357 1 Y 1 B GLU 397 ? D GLU 397 
358 1 Y 1 B ASP 398 ? D ASP 398 
359 1 Y 1 B GLY 399 ? D GLY 399 
360 1 Y 1 B GLU 400 ? D GLU 400 
361 1 Y 1 B ASP 401 ? D ASP 401 
362 1 Y 1 B PRO 402 ? D PRO 402 
363 1 Y 1 B ASP 403 ? D ASP 403 
364 1 Y 1 B LYS 404 ? D LYS 404 
365 1 Y 1 B ARG 405 ? D ARG 405 
366 1 Y 1 B ILE 406 ? D ILE 406 
367 1 Y 1 B SER 407 ? D SER 407 
368 1 Y 1 B ILE 408 ? D ILE 408 
369 1 Y 1 B ARG 409 ? D ARG 409 
370 1 Y 1 B ALA 410 ? D ALA 410 
371 1 Y 1 B SER 411 ? D SER 411 
372 1 Y 1 B ASP 412 ? D ASP 412 
373 1 Y 1 B LYS 413 ? D LYS 413 
374 1 Y 1 B ARG 414 ? D ARG 414 
375 1 Y 1 B ILE 415 ? D ILE 415 
376 1 Y 1 B ALA 416 ? D ALA 416 
377 1 Y 1 B CYS 417 ? D CYS 417 
378 1 Y 1 B ASP 418 ? D ASP 418 
379 1 Y 1 B GLU 419 ? D GLU 419 
380 1 Y 1 B GLU 420 ? D GLU 420 
381 1 Y 1 B PHE 421 ? D PHE 421 
382 1 Y 1 B SER 422 ? D SER 422 
383 1 Y 1 B ASP 423 ? D ASP 423 
384 1 Y 1 B SER 424 ? D SER 424 
385 1 Y 1 B GLU 425 ? D GLU 425 
386 1 Y 1 B ASP 426 ? D ASP 426 
387 1 Y 1 B GLU 427 ? D GLU 427 
388 1 Y 1 B GLY 428 ? D GLY 428 
389 1 Y 1 B GLU 429 ? D GLU 429 
390 1 Y 1 B GLY 430 ? D GLY 430 
391 1 Y 1 B GLY 431 ? D GLY 431 
392 1 Y 1 B ARG 432 ? D ARG 432 
393 1 Y 1 B ARG 433 ? D ARG 433 
394 1 Y 1 B ASN 434 ? D ASN 434 
395 1 Y 1 B VAL 435 ? D VAL 435 
396 1 Y 1 B ALA 436 ? D ALA 436 
397 1 Y 1 B ASP 437 ? D ASP 437 
398 1 Y 1 B HIS 438 ? D HIS 438 
399 1 Y 1 B LYS 439 ? D LYS 439 
400 1 Y 1 B LYS 440 ? D LYS 440 
401 1 Y 1 B GLY 441 ? D GLY 441 
402 1 Y 1 B ALA 442 ? D ALA 442 
403 1 Y 1 B LYS 443 ? D LYS 443 
404 1 Y 1 B LYS 444 ? D LYS 444 
405 1 Y 1 B ALA 445 ? D ALA 445 
406 1 Y 1 B ARG 446 ? D ARG 446 
407 1 Y 1 B ILE 447 ? D ILE 447 
408 1 Y 1 B GLU 448 ? D GLU 448 
409 1 Y 1 B GLU 449 ? D GLU 449 
410 1 Y 1 B ASP 450 ? D ASP 450 
411 1 Y 1 B LYS 451 ? D LYS 451 
412 1 Y 1 B LYS 452 ? D LYS 452 
413 1 Y 1 B GLU 453 ? D GLU 453 
414 1 Y 1 B THR 454 ? D THR 454 
415 1 Y 1 B GLU 455 ? D GLU 455 
416 1 Y 1 B ASP 456 ? D ASP 456 
417 1 Y 1 B LYS 457 ? D LYS 457 
418 1 Y 1 B LYS 458 ? D LYS 458 
419 1 Y 1 B THR 459 ? D THR 459 
420 1 Y 1 B ASP 460 ? D ASP 460 
421 1 Y 1 B VAL 461 ? D VAL 461 
422 1 Y 1 B LYS 462 ? D LYS 462 
423 1 Y 1 B GLU 463 ? D GLU 463 
424 1 Y 1 B GLU 464 ? D GLU 464 
425 1 Y 1 B ASP 465 ? D ASP 465 
426 1 Y 1 B LYS 466 ? D LYS 466 
427 1 Y 1 B SER 467 ? D SER 467 
428 1 Y 1 B LYS 468 ? D LYS 468 
429 1 Y 1 B ASP 469 ? D ASP 469 
430 1 Y 1 B ASN 470 ? D ASN 470 
431 1 Y 1 B SER 471 ? D SER 471 
432 1 Y 1 B GLY 472 ? D GLY 472 
433 1 Y 1 B GLU 473 ? D GLU 473 
434 1 Y 1 B LYS 474 ? D LYS 474 
435 1 Y 1 B THR 475 ? D THR 475 
436 1 Y 1 B ASP 476 ? D ASP 476 
437 1 Y 1 B THR 477 ? D THR 477 
438 1 Y 1 B LYS 478 ? D LYS 478 
439 1 Y 1 B GLY 479 ? D GLY 479 
440 1 Y 1 B THR 480 ? D THR 480 
441 1 Y 1 B LYS 481 ? D LYS 481 
442 1 Y 1 B SER 482 ? D SER 482 
443 1 Y 1 B GLU 483 ? D GLU 483 
444 1 Y 1 B GLN 484 ? D GLN 484 
445 1 Y 1 B LEU 485 ? D LEU 485 
446 1 Y 1 B SER 486 ? D SER 486 
447 1 Y 1 B ASN 487 ? D ASN 487 
448 1 Y 1 B PRO 488 ? D PRO 488 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
ILE N    N  N N 158 
ILE CA   C  N S 159 
ILE C    C  N N 160 
ILE O    O  N N 161 
ILE CB   C  N S 162 
ILE CG1  C  N N 163 
ILE CG2  C  N N 164 
ILE CD1  C  N N 165 
ILE OXT  O  N N 166 
ILE H    H  N N 167 
ILE H2   H  N N 168 
ILE HA   H  N N 169 
ILE HB   H  N N 170 
ILE HG12 H  N N 171 
ILE HG13 H  N N 172 
ILE HG21 H  N N 173 
ILE HG22 H  N N 174 
ILE HG23 H  N N 175 
ILE HD11 H  N N 176 
ILE HD12 H  N N 177 
ILE HD13 H  N N 178 
ILE HXT  H  N N 179 
LEU N    N  N N 180 
LEU CA   C  N S 181 
LEU C    C  N N 182 
LEU O    O  N N 183 
LEU CB   C  N N 184 
LEU CG   C  N N 185 
LEU CD1  C  N N 186 
LEU CD2  C  N N 187 
LEU OXT  O  N N 188 
LEU H    H  N N 189 
LEU H2   H  N N 190 
LEU HA   H  N N 191 
LEU HB2  H  N N 192 
LEU HB3  H  N N 193 
LEU HG   H  N N 194 
LEU HD11 H  N N 195 
LEU HD12 H  N N 196 
LEU HD13 H  N N 197 
LEU HD21 H  N N 198 
LEU HD22 H  N N 199 
LEU HD23 H  N N 200 
LEU HXT  H  N N 201 
LYS N    N  N N 202 
LYS CA   C  N S 203 
LYS C    C  N N 204 
LYS O    O  N N 205 
LYS CB   C  N N 206 
LYS CG   C  N N 207 
LYS CD   C  N N 208 
LYS CE   C  N N 209 
LYS NZ   N  N N 210 
LYS OXT  O  N N 211 
LYS H    H  N N 212 
LYS H2   H  N N 213 
LYS HA   H  N N 214 
LYS HB2  H  N N 215 
LYS HB3  H  N N 216 
LYS HG2  H  N N 217 
LYS HG3  H  N N 218 
LYS HD2  H  N N 219 
LYS HD3  H  N N 220 
LYS HE2  H  N N 221 
LYS HE3  H  N N 222 
LYS HZ1  H  N N 223 
LYS HZ2  H  N N 224 
LYS HZ3  H  N N 225 
LYS HXT  H  N N 226 
MET N    N  N N 227 
MET CA   C  N S 228 
MET C    C  N N 229 
MET O    O  N N 230 
MET CB   C  N N 231 
MET CG   C  N N 232 
MET SD   S  N N 233 
MET CE   C  N N 234 
MET OXT  O  N N 235 
MET H    H  N N 236 
MET H2   H  N N 237 
MET HA   H  N N 238 
MET HB2  H  N N 239 
MET HB3  H  N N 240 
MET HG2  H  N N 241 
MET HG3  H  N N 242 
MET HE1  H  N N 243 
MET HE2  H  N N 244 
MET HE3  H  N N 245 
MET HXT  H  N N 246 
PHE N    N  N N 247 
PHE CA   C  N S 248 
PHE C    C  N N 249 
PHE O    O  N N 250 
PHE CB   C  N N 251 
PHE CG   C  Y N 252 
PHE CD1  C  Y N 253 
PHE CD2  C  Y N 254 
PHE CE1  C  Y N 255 
PHE CE2  C  Y N 256 
PHE CZ   C  Y N 257 
PHE OXT  O  N N 258 
PHE H    H  N N 259 
PHE H2   H  N N 260 
PHE HA   H  N N 261 
PHE HB2  H  N N 262 
PHE HB3  H  N N 263 
PHE HD1  H  N N 264 
PHE HD2  H  N N 265 
PHE HE1  H  N N 266 
PHE HE2  H  N N 267 
PHE HZ   H  N N 268 
PHE HXT  H  N N 269 
PRO N    N  N N 270 
PRO CA   C  N S 271 
PRO C    C  N N 272 
PRO O    O  N N 273 
PRO CB   C  N N 274 
PRO CG   C  N N 275 
PRO CD   C  N N 276 
PRO OXT  O  N N 277 
PRO H    H  N N 278 
PRO HA   H  N N 279 
PRO HB2  H  N N 280 
PRO HB3  H  N N 281 
PRO HG2  H  N N 282 
PRO HG3  H  N N 283 
PRO HD2  H  N N 284 
PRO HD3  H  N N 285 
PRO HXT  H  N N 286 
SER N    N  N N 287 
SER CA   C  N S 288 
SER C    C  N N 289 
SER O    O  N N 290 
SER CB   C  N N 291 
SER OG   O  N N 292 
SER OXT  O  N N 293 
SER H    H  N N 294 
SER H2   H  N N 295 
SER HA   H  N N 296 
SER HB2  H  N N 297 
SER HB3  H  N N 298 
SER HG   H  N N 299 
SER HXT  H  N N 300 
THR N    N  N N 301 
THR CA   C  N S 302 
THR C    C  N N 303 
THR O    O  N N 304 
THR CB   C  N R 305 
THR OG1  O  N N 306 
THR CG2  C  N N 307 
THR OXT  O  N N 308 
THR H    H  N N 309 
THR H2   H  N N 310 
THR HA   H  N N 311 
THR HB   H  N N 312 
THR HG1  H  N N 313 
THR HG21 H  N N 314 
THR HG22 H  N N 315 
THR HG23 H  N N 316 
THR HXT  H  N N 317 
TRP N    N  N N 318 
TRP CA   C  N S 319 
TRP C    C  N N 320 
TRP O    O  N N 321 
TRP CB   C  N N 322 
TRP CG   C  Y N 323 
TRP CD1  C  Y N 324 
TRP CD2  C  Y N 325 
TRP NE1  N  Y N 326 
TRP CE2  C  Y N 327 
TRP CE3  C  Y N 328 
TRP CZ2  C  Y N 329 
TRP CZ3  C  Y N 330 
TRP CH2  C  Y N 331 
TRP OXT  O  N N 332 
TRP H    H  N N 333 
TRP H2   H  N N 334 
TRP HA   H  N N 335 
TRP HB2  H  N N 336 
TRP HB3  H  N N 337 
TRP HD1  H  N N 338 
TRP HE1  H  N N 339 
TRP HE3  H  N N 340 
TRP HZ2  H  N N 341 
TRP HZ3  H  N N 342 
TRP HH2  H  N N 343 
TRP HXT  H  N N 344 
TYR N    N  N N 345 
TYR CA   C  N S 346 
TYR C    C  N N 347 
TYR O    O  N N 348 
TYR CB   C  N N 349 
TYR CG   C  Y N 350 
TYR CD1  C  Y N 351 
TYR CD2  C  Y N 352 
TYR CE1  C  Y N 353 
TYR CE2  C  Y N 354 
TYR CZ   C  Y N 355 
TYR OH   O  N N 356 
TYR OXT  O  N N 357 
TYR H    H  N N 358 
TYR H2   H  N N 359 
TYR HA   H  N N 360 
TYR HB2  H  N N 361 
TYR HB3  H  N N 362 
TYR HD1  H  N N 363 
TYR HD2  H  N N 364 
TYR HE1  H  N N 365 
TYR HE2  H  N N 366 
TYR HH   H  N N 367 
TYR HXT  H  N N 368 
VAL N    N  N N 369 
VAL CA   C  N S 370 
VAL C    C  N N 371 
VAL O    O  N N 372 
VAL CB   C  N N 373 
VAL CG1  C  N N 374 
VAL CG2  C  N N 375 
VAL OXT  O  N N 376 
VAL H    H  N N 377 
VAL H2   H  N N 378 
VAL HA   H  N N 379 
VAL HB   H  N N 380 
VAL HG11 H  N N 381 
VAL HG12 H  N N 382 
VAL HG13 H  N N 383 
VAL HG21 H  N N 384 
VAL HG22 H  N N 385 
VAL HG23 H  N N 386 
VAL HXT  H  N N 387 
ZN  ZN   ZN N N 388 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-13 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9GGM 
_em_admin.last_update        2025-04-09 
_em_admin.map_release_date   2025-04-09 
_em_admin.title              'Cryo-EM structure of KBTBD4 P313PRR mutant-HDAC2 2:2 complex' 
# 
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 50  mM C8H18N2O4S  1 HEPES                  
1 150 mM NaCl        2 'sodium chloride'      
1 5   mM MgCl2       3 'magnesium dichloride' 
1 10  %  'C3H5(OH)3' 4 glycerol               
1 0.5 mM C9H15O6P    5 TCEP                   
# 
_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                ? 
_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          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         38.6 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (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                     13131 
# 
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 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           0.4 
_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 
'Cancer Research UK'              'United Kingdom' DRCNPG-May21/100002 1 
'Innovative Medicines Initiative' Switzerland      875510              2 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB       7ZZT         ? 
2 ? 'in silico model'    AlphaFold AF-Q9N010-F1 ? 
# 
_atom_sites.entry_id                    9GGM 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . PHE A 1 16  ? 133.190 171.863 126.588 1.00 117.54 ? 32  PHE A N   1 
ATOM   2     C  CA  . PHE A 1 16  ? 132.064 172.082 125.688 1.00 117.54 ? 32  PHE A CA  1 
ATOM   3     C  C   . PHE A 1 16  ? 132.469 172.825 124.420 1.00 117.54 ? 32  PHE A C   1 
ATOM   4     O  O   . PHE A 1 16  ? 131.701 172.885 123.460 1.00 117.54 ? 32  PHE A O   1 
ATOM   5     C  CB  . PHE A 1 16  ? 130.946 172.835 126.408 1.00 117.54 ? 32  PHE A CB  1 
ATOM   6     C  CG  . PHE A 1 16  ? 130.013 171.941 127.173 1.00 117.54 ? 32  PHE A CG  1 
ATOM   7     C  CD1 . PHE A 1 16  ? 130.335 171.499 128.444 1.00 117.54 ? 32  PHE A CD1 1 
ATOM   8     C  CD2 . PHE A 1 16  ? 128.808 171.546 126.617 1.00 117.54 ? 32  PHE A CD2 1 
ATOM   9     C  CE1 . PHE A 1 16  ? 129.472 170.675 129.143 1.00 117.54 ? 32  PHE A CE1 1 
ATOM   10    C  CE2 . PHE A 1 16  ? 127.943 170.724 127.311 1.00 117.54 ? 32  PHE A CE2 1 
ATOM   11    C  CZ  . PHE A 1 16  ? 128.275 170.289 128.576 1.00 117.54 ? 32  PHE A CZ  1 
ATOM   12    N  N   . VAL A 1 17  ? 133.677 173.391 124.413 1.00 139.07 ? 33  VAL A N   1 
ATOM   13    C  CA  . VAL A 1 17  ? 134.170 174.151 123.275 1.00 139.07 ? 33  VAL A CA  1 
ATOM   14    C  C   . VAL A 1 17  ? 135.479 173.588 122.734 1.00 139.07 ? 33  VAL A C   1 
ATOM   15    O  O   . VAL A 1 17  ? 135.639 173.453 121.517 1.00 139.07 ? 33  VAL A O   1 
ATOM   16    C  CB  . VAL A 1 17  ? 134.331 175.646 123.632 1.00 139.07 ? 33  VAL A CB  1 
ATOM   17    C  CG1 . VAL A 1 17  ? 132.996 176.363 123.518 1.00 139.07 ? 33  VAL A CG1 1 
ATOM   18    C  CG2 . VAL A 1 17  ? 134.901 175.802 125.032 1.00 139.07 ? 33  VAL A CG2 1 
ATOM   19    N  N   . ASN A 1 18  ? 136.431 173.264 123.608 1.00 143.87 ? 34  ASN A N   1 
ATOM   20    C  CA  . ASN A 1 18  ? 137.741 172.814 123.155 1.00 143.87 ? 34  ASN A CA  1 
ATOM   21    C  C   . ASN A 1 18  ? 138.317 171.779 124.109 1.00 143.87 ? 34  ASN A C   1 
ATOM   22    O  O   . ASN A 1 18  ? 138.267 171.973 125.325 1.00 143.87 ? 34  ASN A O   1 
ATOM   23    C  CB  . ASN A 1 18  ? 138.702 174.002 123.025 1.00 143.87 ? 34  ASN A CB  1 
ATOM   24    C  CG  . ASN A 1 18  ? 140.158 173.588 123.116 1.00 143.87 ? 34  ASN A CG  1 
ATOM   25    O  OD1 . ASN A 1 18  ? 140.720 173.039 122.170 1.00 143.87 ? 34  ASN A OD1 1 
ATOM   26    N  ND2 . ASN A 1 18  ? 140.776 173.854 124.260 1.00 143.87 ? 34  ASN A ND2 1 
ATOM   27    N  N   . TYR A 1 19  ? 138.835 170.679 123.559 1.00 137.63 ? 35  TYR A N   1 
ATOM   28    C  CA  . TYR A 1 19  ? 139.503 169.633 124.329 1.00 137.63 ? 35  TYR A CA  1 
ATOM   29    C  C   . TYR A 1 19  ? 140.268 168.793 123.317 1.00 137.63 ? 35  TYR A C   1 
ATOM   30    O  O   . TYR A 1 19  ? 139.875 168.711 122.150 1.00 137.63 ? 35  TYR A O   1 
ATOM   31    C  CB  . TYR A 1 19  ? 138.591 168.714 125.151 1.00 137.63 ? 35  TYR A CB  1 
ATOM   32    C  CG  . TYR A 1 19  ? 137.653 167.856 124.352 1.00 137.63 ? 35  TYR A CG  1 
ATOM   33    C  CD1 . TYR A 1 19  ? 136.749 168.400 123.468 1.00 137.63 ? 35  TYR A CD1 1 
ATOM   34    C  CD2 . TYR A 1 19  ? 137.717 166.472 124.459 1.00 137.63 ? 35  TYR A CD2 1 
ATOM   35    C  CE1 . TYR A 1 19  ? 135.920 167.596 122.736 1.00 137.63 ? 35  TYR A CE1 1 
ATOM   36    C  CE2 . TYR A 1 19  ? 136.886 165.659 123.727 1.00 137.63 ? 35  TYR A CE2 1 
ATOM   37    C  CZ  . TYR A 1 19  ? 135.986 166.228 122.862 1.00 137.63 ? 35  TYR A CZ  1 
ATOM   38    O  OH  . TYR A 1 19  ? 135.141 165.430 122.124 1.00 137.63 ? 35  TYR A OH  1 
ATOM   39    N  N   . THR A 1 20  ? 141.350 168.166 123.761 1.00 136.74 ? 36  THR A N   1 
ATOM   40    C  CA  . THR A 1 20  ? 142.094 167.246 122.910 1.00 136.74 ? 36  THR A CA  1 
ATOM   41    C  C   . THR A 1 20  ? 141.666 165.812 123.201 1.00 136.74 ? 36  THR A C   1 
ATOM   42    O  O   . THR A 1 20  ? 141.597 165.399 124.363 1.00 136.74 ? 36  THR A O   1 
ATOM   43    C  CB  . THR A 1 20  ? 143.600 167.397 123.124 1.00 136.74 ? 36  THR A CB  1 
ATOM   44    N  N   . PHE A 1 21  ? 141.376 165.064 122.132 1.00 143.32 ? 37  PHE A N   1 
ATOM   45    C  CA  . PHE A 1 21  ? 140.946 163.668 122.191 1.00 143.32 ? 37  PHE A CA  1 
ATOM   46    C  C   . PHE A 1 21  ? 142.096 162.779 121.730 1.00 143.32 ? 37  PHE A C   1 
ATOM   47    O  O   . PHE A 1 21  ? 142.464 162.784 120.550 1.00 143.32 ? 37  PHE A O   1 
ATOM   48    C  CB  . PHE A 1 21  ? 139.685 163.477 121.339 1.00 143.32 ? 37  PHE A CB  1 
ATOM   49    C  CG  . PHE A 1 21  ? 139.347 162.038 121.006 1.00 143.32 ? 37  PHE A CG  1 
ATOM   50    C  CD1 . PHE A 1 21  ? 139.482 161.021 121.933 1.00 143.32 ? 37  PHE A CD1 1 
ATOM   51    C  CD2 . PHE A 1 21  ? 138.840 161.721 119.758 1.00 143.32 ? 37  PHE A CD2 1 
ATOM   52    C  CE1 . PHE A 1 21  ? 139.152 159.717 121.612 1.00 143.32 ? 37  PHE A CE1 1 
ATOM   53    C  CE2 . PHE A 1 21  ? 138.507 160.424 119.433 1.00 143.32 ? 37  PHE A CE2 1 
ATOM   54    C  CZ  . PHE A 1 21  ? 138.664 159.420 120.360 1.00 143.32 ? 37  PHE A CZ  1 
ATOM   55    N  N   . LYS A 1 22  ? 142.655 162.019 122.670 1.00 132.77 ? 38  LYS A N   1 
ATOM   56    C  CA  . LYS A 1 22  ? 143.720 161.054 122.416 1.00 132.77 ? 38  LYS A CA  1 
ATOM   57    C  C   . LYS A 1 22  ? 143.166 159.654 122.655 1.00 132.77 ? 38  LYS A C   1 
ATOM   58    O  O   . LYS A 1 22  ? 142.850 159.293 123.794 1.00 132.77 ? 38  LYS A O   1 
ATOM   59    C  CB  . LYS A 1 22  ? 144.929 161.324 123.309 1.00 132.77 ? 38  LYS A CB  1 
ATOM   60    N  N   . ASP A 1 23  ? 143.061 158.864 121.590 1.00 149.57 ? 39  ASP A N   1 
ATOM   61    C  CA  . ASP A 1 23  ? 142.529 157.511 121.690 1.00 149.57 ? 39  ASP A CA  1 
ATOM   62    C  C   . ASP A 1 23  ? 143.684 156.552 121.946 1.00 149.57 ? 39  ASP A C   1 
ATOM   63    O  O   . ASP A 1 23  ? 144.475 156.265 121.042 1.00 149.57 ? 39  ASP A O   1 
ATOM   64    C  CB  . ASP A 1 23  ? 141.797 157.123 120.409 1.00 149.57 ? 39  ASP A CB  1 
ATOM   65    C  CG  . ASP A 1 23  ? 142.504 157.623 119.165 1.00 149.57 ? 39  ASP A CG  1 
ATOM   66    O  OD1 . ASP A 1 23  ? 143.561 158.274 119.300 1.00 149.57 ? 39  ASP A OD1 1 
ATOM   67    O  OD2 . ASP A 1 23  ? 141.999 157.379 118.053 1.00 149.57 ? 39  ASP A OD2 1 
ATOM   68    N  N   . ARG A 1 24  ? 143.783 156.056 123.182 1.00 142.69 ? 40  ARG A N   1 
ATOM   69    C  CA  . ARG A 1 24  ? 144.881 155.164 123.526 1.00 142.69 ? 40  ARG A CA  1 
ATOM   70    C  C   . ARG A 1 24  ? 144.809 153.837 122.784 1.00 142.69 ? 40  ARG A C   1 
ATOM   71    O  O   . ARG A 1 24  ? 145.798 153.096 122.778 1.00 142.69 ? 40  ARG A O   1 
ATOM   72    C  CB  . ARG A 1 24  ? 144.899 154.916 125.036 1.00 142.69 ? 40  ARG A CB  1 
ATOM   73    N  N   . SER A 1 25  ? 143.670 153.517 122.172 1.00 150.53 ? 41  SER A N   1 
ATOM   74    C  CA  . SER A 1 25  ? 143.472 152.256 121.473 1.00 150.53 ? 41  SER A CA  1 
ATOM   75    C  C   . SER A 1 25  ? 143.677 152.376 119.967 1.00 150.53 ? 41  SER A C   1 
ATOM   76    O  O   . SER A 1 25  ? 143.424 151.409 119.243 1.00 150.53 ? 41  SER A O   1 
ATOM   77    C  CB  . SER A 1 25  ? 142.076 151.704 121.767 1.00 150.53 ? 41  SER A CB  1 
ATOM   78    O  OG  . SER A 1 25  ? 141.700 151.956 123.109 1.00 150.53 ? 41  SER A OG  1 
ATOM   79    N  N   . HIS A 1 26  ? 144.113 153.540 119.478 1.00 140.84 ? 42  HIS A N   1 
ATOM   80    C  CA  . HIS A 1 26  ? 144.349 153.698 118.046 1.00 140.84 ? 42  HIS A CA  1 
ATOM   81    C  C   . HIS A 1 26  ? 145.418 152.730 117.554 1.00 140.84 ? 42  HIS A C   1 
ATOM   82    O  O   . HIS A 1 26  ? 145.244 152.061 116.528 1.00 140.84 ? 42  HIS A O   1 
ATOM   83    C  CB  . HIS A 1 26  ? 144.748 155.141 117.736 1.00 140.84 ? 42  HIS A CB  1 
ATOM   84    C  CG  . HIS A 1 26  ? 145.506 155.293 116.454 1.00 140.84 ? 42  HIS A CG  1 
ATOM   85    N  ND1 . HIS A 1 26  ? 144.939 155.044 115.223 1.00 140.84 ? 42  HIS A ND1 1 
ATOM   86    C  CD2 . HIS A 1 26  ? 146.786 155.661 116.211 1.00 140.84 ? 42  HIS A CD2 1 
ATOM   87    C  CE1 . HIS A 1 26  ? 145.834 155.257 114.277 1.00 140.84 ? 42  HIS A CE1 1 
ATOM   88    N  NE2 . HIS A 1 26  ? 146.964 155.632 114.849 1.00 140.84 ? 42  HIS A NE2 1 
ATOM   89    N  N   . SER A 1 27  ? 146.539 152.649 118.277 1.00 141.34 ? 43  SER A N   1 
ATOM   90    C  CA  . SER A 1 27  ? 147.624 151.763 117.869 1.00 141.34 ? 43  SER A CA  1 
ATOM   91    C  C   . SER A 1 27  ? 147.179 150.307 117.876 1.00 141.34 ? 43  SER A C   1 
ATOM   92    O  O   . SER A 1 27  ? 147.478 149.556 116.941 1.00 141.34 ? 43  SER A O   1 
ATOM   93    C  CB  . SER A 1 27  ? 148.835 151.961 118.781 1.00 141.34 ? 43  SER A CB  1 
ATOM   94    O  OG  . SER A 1 27  ? 148.518 151.654 120.128 1.00 141.34 ? 43  SER A OG  1 
ATOM   95    N  N   . GLY A 1 28  ? 146.463 149.890 118.922 1.00 141.04 ? 44  GLY A N   1 
ATOM   96    C  CA  . GLY A 1 28  ? 145.982 148.518 118.971 1.00 141.04 ? 44  GLY A CA  1 
ATOM   97    C  C   . GLY A 1 28  ? 145.046 148.194 117.823 1.00 141.04 ? 44  GLY A C   1 
ATOM   98    O  O   . GLY A 1 28  ? 145.175 147.151 117.173 1.00 141.04 ? 44  GLY A O   1 
ATOM   99    N  N   . ARG A 1 29  ? 144.090 149.088 117.557 1.00 133.40 ? 45  ARG A N   1 
ATOM   100   C  CA  . ARG A 1 29  ? 143.137 148.856 116.475 1.00 133.40 ? 45  ARG A CA  1 
ATOM   101   C  C   . ARG A 1 29  ? 143.848 148.766 115.132 1.00 133.40 ? 45  ARG A C   1 
ATOM   102   O  O   . ARG A 1 29  ? 143.587 147.853 114.339 1.00 133.40 ? 45  ARG A O   1 
ATOM   103   C  CB  . ARG A 1 29  ? 142.082 149.964 116.446 1.00 133.40 ? 45  ARG A CB  1 
ATOM   104   C  CG  . ARG A 1 29  ? 141.042 149.889 117.552 1.00 133.40 ? 45  ARG A CG  1 
ATOM   105   C  CD  . ARG A 1 29  ? 139.868 150.811 117.254 1.00 133.40 ? 45  ARG A CD  1 
ATOM   106   N  NE  . ARG A 1 29  ? 140.287 152.193 117.053 1.00 133.40 ? 45  ARG A NE  1 
ATOM   107   C  CZ  . ARG A 1 29  ? 140.418 153.087 118.023 1.00 133.40 ? 45  ARG A CZ  1 
ATOM   108   N  NH1 . ARG A 1 29  ? 140.167 152.781 119.285 1.00 133.40 ? 45  ARG A NH1 1 
ATOM   109   N  NH2 . ARG A 1 29  ? 140.809 154.321 117.719 1.00 133.40 ? 45  ARG A NH2 1 
ATOM   110   N  N   . VAL A 1 30  ? 144.753 149.710 114.856 1.00 128.80 ? 46  VAL A N   1 
ATOM   111   C  CA  . VAL A 1 30  ? 145.422 149.717 113.559 1.00 128.80 ? 46  VAL A CA  1 
ATOM   112   C  C   . VAL A 1 30  ? 146.312 148.487 113.409 1.00 128.80 ? 46  VAL A C   1 
ATOM   113   O  O   . VAL A 1 30  ? 146.372 147.883 112.332 1.00 128.80 ? 46  VAL A O   1 
ATOM   114   C  CB  . VAL A 1 30  ? 146.197 151.032 113.337 1.00 128.80 ? 46  VAL A CB  1 
ATOM   115   C  CG1 . VAL A 1 30  ? 147.360 151.176 114.302 1.00 128.80 ? 46  VAL A CG1 1 
ATOM   116   C  CG2 . VAL A 1 30  ? 146.681 151.123 111.896 1.00 128.80 ? 46  VAL A CG2 1 
ATOM   117   N  N   . ALA A 1 31  ? 147.006 148.085 114.480 1.00 125.31 ? 47  ALA A N   1 
ATOM   118   C  CA  . ALA A 1 31  ? 147.866 146.908 114.407 1.00 125.31 ? 47  ALA A CA  1 
ATOM   119   C  C   . ALA A 1 31  ? 147.048 145.647 114.159 1.00 125.31 ? 47  ALA A C   1 
ATOM   120   O  O   . ALA A 1 31  ? 147.398 144.819 113.307 1.00 125.31 ? 47  ALA A O   1 
ATOM   121   C  CB  . ALA A 1 31  ? 148.686 146.777 115.690 1.00 125.31 ? 47  ALA A CB  1 
ATOM   122   N  N   . GLN A 1 32  ? 145.948 145.480 114.896 1.00 122.90 ? 48  GLN A N   1 
ATOM   123   C  CA  . GLN A 1 32  ? 145.117 144.300 114.698 1.00 122.90 ? 48  GLN A CA  1 
ATOM   124   C  C   . GLN A 1 32  ? 144.543 144.269 113.287 1.00 122.90 ? 48  GLN A C   1 
ATOM   125   O  O   . GLN A 1 32  ? 144.527 143.216 112.637 1.00 122.90 ? 48  GLN A O   1 
ATOM   126   C  CB  . GLN A 1 32  ? 143.997 144.264 115.738 1.00 122.90 ? 48  GLN A CB  1 
ATOM   127   N  N   . GLY A 1 33  ? 144.063 145.415 112.798 1.00 133.00 ? 49  GLY A N   1 
ATOM   128   C  CA  . GLY A 1 33  ? 143.517 145.454 111.453 1.00 133.00 ? 49  GLY A CA  1 
ATOM   129   C  C   . GLY A 1 33  ? 144.540 145.176 110.367 1.00 133.00 ? 49  GLY A C   1 
ATOM   130   O  O   . GLY A 1 33  ? 144.253 144.449 109.413 1.00 133.00 ? 49  GLY A O   1 
ATOM   131   N  N   . ILE A 1 34  ? 145.747 145.739 110.490 1.00 125.59 ? 50  ILE A N   1 
ATOM   132   C  CA  . ILE A 1 34  ? 146.774 145.449 109.489 1.00 125.59 ? 50  ILE A CA  1 
ATOM   133   C  C   . ILE A 1 34  ? 147.120 143.965 109.516 1.00 125.59 ? 50  ILE A C   1 
ATOM   134   O  O   . ILE A 1 34  ? 147.227 143.321 108.467 1.00 125.59 ? 50  ILE A O   1 
ATOM   135   C  CB  . ILE A 1 34  ? 148.009 146.367 109.642 1.00 125.59 ? 50  ILE A CB  1 
ATOM   136   C  CG1 . ILE A 1 34  ? 148.690 146.312 111.015 1.00 125.59 ? 50  ILE A CG1 1 
ATOM   137   C  CG2 . ILE A 1 34  ? 147.641 147.808 109.304 1.00 125.59 ? 50  ILE A CG2 1 
ATOM   138   C  CD1 . ILE A 1 34  ? 149.722 145.203 111.191 1.00 125.59 ? 50  ILE A CD1 1 
ATOM   139   N  N   . MET A 1 35  ? 147.300 143.402 110.716 1.00 130.01 ? 51  MET A N   1 
ATOM   140   C  CA  . MET A 1 35  ? 147.556 141.971 110.833 1.00 130.01 ? 51  MET A CA  1 
ATOM   141   C  C   . MET A 1 35  ? 146.487 141.166 110.103 1.00 130.01 ? 51  MET A C   1 
ATOM   142   O  O   . MET A 1 35  ? 146.796 140.331 109.244 1.00 130.01 ? 51  MET A O   1 
ATOM   143   C  CB  . MET A 1 35  ? 147.621 141.570 112.308 1.00 130.01 ? 51  MET A CB  1 
ATOM   144   C  CG  . MET A 1 35  ? 147.383 140.089 112.563 1.00 130.01 ? 51  MET A CG  1 
ATOM   145   S  SD  . MET A 1 35  ? 147.332 139.659 114.315 1.00 130.01 ? 51  MET A SD  1 
ATOM   146   C  CE  . MET A 1 35  ? 148.163 141.067 115.048 1.00 130.01 ? 51  MET A CE  1 
ATOM   147   N  N   . LYS A 1 36  ? 145.215 141.425 110.425 1.00 121.61 ? 52  LYS A N   1 
ATOM   148   C  CA  . LYS A 1 36  ? 144.125 140.638 109.856 1.00 121.61 ? 52  LYS A CA  1 
ATOM   149   C  C   . LYS A 1 36  ? 144.082 140.772 108.338 1.00 121.61 ? 52  LYS A C   1 
ATOM   150   O  O   . LYS A 1 36  ? 144.070 139.768 107.616 1.00 121.61 ? 52  LYS A O   1 
ATOM   151   C  CB  . LYS A 1 36  ? 142.794 141.063 110.475 1.00 121.61 ? 52  LYS A CB  1 
ATOM   152   N  N   . LEU A 1 37  ? 144.059 142.007 107.831 1.00 116.67 ? 53  LEU A N   1 
ATOM   153   C  CA  . LEU A 1 37  ? 143.915 142.189 106.390 1.00 116.67 ? 53  LEU A CA  1 
ATOM   154   C  C   . LEU A 1 37  ? 145.116 141.635 105.634 1.00 116.67 ? 53  LEU A C   1 
ATOM   155   O  O   . LEU A 1 37  ? 144.947 140.976 104.603 1.00 116.67 ? 53  LEU A O   1 
ATOM   156   C  CB  . LEU A 1 37  ? 143.678 143.660 106.044 1.00 116.67 ? 53  LEU A CB  1 
ATOM   157   C  CG  . LEU A 1 37  ? 142.232 144.160 106.157 1.00 116.67 ? 53  LEU A CG  1 
ATOM   158   C  CD1 . LEU A 1 37  ? 141.859 144.627 107.553 1.00 116.67 ? 53  LEU A CD1 1 
ATOM   159   C  CD2 . LEU A 1 37  ? 141.983 145.265 105.138 1.00 116.67 ? 53  LEU A CD2 1 
ATOM   160   N  N   . CYS A 1 38  ? 146.335 141.878 106.123 1.00 124.17 ? 54  CYS A N   1 
ATOM   161   C  CA  . CYS A 1 38  ? 147.515 141.390 105.419 1.00 124.17 ? 54  CYS A CA  1 
ATOM   162   C  C   . CYS A 1 38  ? 147.567 139.866 105.415 1.00 124.17 ? 54  CYS A C   1 
ATOM   163   O  O   . CYS A 1 38  ? 147.798 139.249 104.368 1.00 124.17 ? 54  CYS A O   1 
ATOM   164   C  CB  . CYS A 1 38  ? 148.783 141.974 106.045 1.00 124.17 ? 54  CYS A CB  1 
ATOM   165   S  SG  . CYS A 1 38  ? 148.936 143.770 105.890 1.00 124.17 ? 54  CYS A SG  1 
ATOM   166   N  N   . LEU A 1 39  ? 147.363 139.236 106.577 1.00 133.88 ? 55  LEU A N   1 
ATOM   167   C  CA  . LEU A 1 39  ? 147.434 137.779 106.642 1.00 133.88 ? 55  LEU A CA  1 
ATOM   168   C  C   . LEU A 1 39  ? 146.329 137.121 105.820 1.00 133.88 ? 55  LEU A C   1 
ATOM   169   O  O   . LEU A 1 39  ? 146.572 136.119 105.137 1.00 133.88 ? 55  LEU A O   1 
ATOM   170   C  CB  . LEU A 1 39  ? 147.382 137.316 108.098 1.00 133.88 ? 55  LEU A CB  1 
ATOM   171   N  N   . GLU A 1 40  ? 145.110 137.662 105.866 1.00 136.92 ? 56  GLU A N   1 
ATOM   172   C  CA  . GLU A 1 40  ? 143.977 137.040 105.188 1.00 136.92 ? 56  GLU A CA  1 
ATOM   173   C  C   . GLU A 1 40  ? 143.819 137.461 103.730 1.00 136.92 ? 56  GLU A C   1 
ATOM   174   O  O   . GLU A 1 40  ? 142.934 136.935 103.048 1.00 136.92 ? 56  GLU A O   1 
ATOM   175   C  CB  . GLU A 1 40  ? 142.669 137.323 105.943 1.00 136.92 ? 56  GLU A CB  1 
ATOM   176   C  CG  . GLU A 1 40  ? 142.353 136.398 107.134 1.00 136.92 ? 56  GLU A CG  1 
ATOM   177   C  CD  . GLU A 1 40  ? 143.399 136.380 108.237 1.00 136.92 ? 56  GLU A CD  1 
ATOM   178   O  OE1 . GLU A 1 40  ? 144.342 137.189 108.207 1.00 136.92 ? 56  GLU A OE1 1 
ATOM   179   O  OE2 . GLU A 1 40  ? 143.272 135.537 109.150 1.00 136.92 ? 56  GLU A OE2 1 
ATOM   180   N  N   . GLU A 1 41  ? 144.634 138.385 103.231 1.00 134.58 ? 57  GLU A N   1 
ATOM   181   C  CA  . GLU A 1 41  ? 144.532 138.779 101.826 1.00 134.58 ? 57  GLU A CA  1 
ATOM   182   C  C   . GLU A 1 41  ? 145.558 138.038 100.976 1.00 134.58 ? 57  GLU A C   1 
ATOM   183   O  O   . GLU A 1 41  ? 145.476 138.038 99.748  1.00 134.58 ? 57  GLU A O   1 
ATOM   184   C  CB  . GLU A 1 41  ? 144.715 140.288 101.661 1.00 134.58 ? 57  GLU A CB  1 
ATOM   185   N  N   . ARG A 1 60  ? 154.439 147.041 102.376 1.00 117.02 ? 76  ARG A N   1 
ATOM   186   C  CA  . ARG A 1 60  ? 155.688 147.765 102.581 1.00 117.02 ? 76  ARG A CA  1 
ATOM   187   C  C   . ARG A 1 60  ? 155.646 148.600 103.856 1.00 117.02 ? 76  ARG A C   1 
ATOM   188   O  O   . ARG A 1 60  ? 156.667 148.784 104.517 1.00 117.02 ? 76  ARG A O   1 
ATOM   189   C  CB  . ARG A 1 60  ? 155.997 148.660 101.378 1.00 117.02 ? 76  ARG A CB  1 
ATOM   190   C  CG  . ARG A 1 60  ? 154.917 149.680 101.062 1.00 117.02 ? 76  ARG A CG  1 
ATOM   191   C  CD  . ARG A 1 60  ? 155.335 150.589 99.919  1.00 117.02 ? 76  ARG A CD  1 
ATOM   192   N  NE  . ARG A 1 60  ? 156.501 151.393 100.263 1.00 117.02 ? 76  ARG A NE  1 
ATOM   193   C  CZ  . ARG A 1 60  ? 156.465 152.481 101.020 1.00 117.02 ? 76  ARG A CZ  1 
ATOM   194   N  NH1 . ARG A 1 60  ? 155.334 152.918 101.549 1.00 117.02 ? 76  ARG A NH1 1 
ATOM   195   N  NH2 . ARG A 1 60  ? 157.593 153.144 101.258 1.00 117.02 ? 76  ARG A NH2 1 
ATOM   196   N  N   . LEU A 1 61  ? 154.458 149.107 104.192 1.00 122.64 ? 77  LEU A N   1 
ATOM   197   C  CA  . LEU A 1 61  ? 154.324 149.960 105.369 1.00 122.64 ? 77  LEU A CA  1 
ATOM   198   C  C   . LEU A 1 61  ? 154.636 149.196 106.649 1.00 122.64 ? 77  LEU A C   1 
ATOM   199   O  O   . LEU A 1 61  ? 155.282 149.733 107.557 1.00 122.64 ? 77  LEU A O   1 
ATOM   200   C  CB  . LEU A 1 61  ? 152.917 150.554 105.428 1.00 122.64 ? 77  LEU A CB  1 
ATOM   201   N  N   . VAL A 1 62  ? 154.180 147.945 106.743 1.00 116.40 ? 78  VAL A N   1 
ATOM   202   C  CA  . VAL A 1 62  ? 154.381 147.165 107.963 1.00 116.40 ? 78  VAL A CA  1 
ATOM   203   C  C   . VAL A 1 62  ? 155.866 146.946 108.224 1.00 116.40 ? 78  VAL A C   1 
ATOM   204   O  O   . VAL A 1 62  ? 156.341 147.096 109.356 1.00 116.40 ? 78  VAL A O   1 
ATOM   205   C  CB  . VAL A 1 62  ? 153.618 145.831 107.875 1.00 116.40 ? 78  VAL A CB  1 
ATOM   206   N  N   . LEU A 1 63  ? 156.621 146.586 107.184 1.00 132.52 ? 79  LEU A N   1 
ATOM   207   C  CA  . LEU A 1 63  ? 158.053 146.358 107.356 1.00 132.52 ? 79  LEU A CA  1 
ATOM   208   C  C   . LEU A 1 63  ? 158.801 147.668 107.562 1.00 132.52 ? 79  LEU A C   1 
ATOM   209   O  O   . LEU A 1 63  ? 159.674 147.760 108.434 1.00 132.52 ? 79  LEU A O   1 
ATOM   210   C  CB  . LEU A 1 63  ? 158.611 145.601 106.151 1.00 132.52 ? 79  LEU A CB  1 
ATOM   211   N  N   . SER A 1 64  ? 158.481 148.690 106.763 1.00 127.55 ? 80  SER A N   1 
ATOM   212   C  CA  . SER A 1 64  ? 159.172 149.969 106.882 1.00 127.55 ? 80  SER A CA  1 
ATOM   213   C  C   . SER A 1 64  ? 158.937 150.612 108.242 1.00 127.55 ? 80  SER A C   1 
ATOM   214   O  O   . SER A 1 64  ? 159.769 151.400 108.706 1.00 127.55 ? 80  SER A O   1 
ATOM   215   C  CB  . SER A 1 64  ? 158.728 150.912 105.764 1.00 127.55 ? 80  SER A CB  1 
ATOM   216   O  OG  . SER A 1 64  ? 158.988 150.348 104.491 1.00 127.55 ? 80  SER A OG  1 
ATOM   217   N  N   . ALA A 1 65  ? 157.817 150.296 108.893 1.00 125.85 ? 81  ALA A N   1 
ATOM   218   C  CA  . ALA A 1 65  ? 157.536 150.841 110.214 1.00 125.85 ? 81  ALA A CA  1 
ATOM   219   C  C   . ALA A 1 65  ? 158.311 150.143 111.322 1.00 125.85 ? 81  ALA A C   1 
ATOM   220   O  O   . ALA A 1 65  ? 158.284 150.613 112.465 1.00 125.85 ? 81  ALA A O   1 
ATOM   221   C  CB  . ALA A 1 65  ? 156.038 150.747 110.508 1.00 125.85 ? 81  ALA A CB  1 
ATOM   222   N  N   . GLN A 1 66  ? 158.992 149.044 111.017 1.00 127.88 ? 82  GLN A N   1 
ATOM   223   C  CA  . GLN A 1 66  ? 159.789 148.314 111.991 1.00 127.88 ? 82  GLN A CA  1 
ATOM   224   C  C   . GLN A 1 66  ? 161.275 148.305 111.678 1.00 127.88 ? 82  GLN A C   1 
ATOM   225   O  O   . GLN A 1 66  ? 162.088 148.297 112.604 1.00 127.88 ? 82  GLN A O   1 
ATOM   226   C  CB  . GLN A 1 66  ? 159.310 146.856 112.088 1.00 127.88 ? 82  GLN A CB  1 
ATOM   227   C  CG  . GLN A 1 66  ? 157.902 146.680 112.623 1.00 127.88 ? 82  GLN A CG  1 
ATOM   228   C  CD  . GLN A 1 66  ? 157.888 146.152 114.042 1.00 127.88 ? 82  GLN A CD  1 
ATOM   229   O  OE1 . GLN A 1 66  ? 158.376 146.803 114.964 1.00 127.88 ? 82  GLN A OE1 1 
ATOM   230   N  NE2 . GLN A 1 66  ? 157.337 144.958 114.222 1.00 127.88 ? 82  GLN A NE2 1 
ATOM   231   N  N   . SER A 1 67  ? 161.645 148.307 110.401 1.00 141.68 ? 83  SER A N   1 
ATOM   232   C  CA  . SER A 1 67  ? 163.027 148.178 109.965 1.00 141.68 ? 83  SER A CA  1 
ATOM   233   C  C   . SER A 1 67  ? 163.425 149.358 109.090 1.00 141.68 ? 83  SER A C   1 
ATOM   234   O  O   . SER A 1 67  ? 162.731 149.681 108.120 1.00 141.68 ? 83  SER A O   1 
ATOM   235   C  CB  . SER A 1 67  ? 163.218 146.867 109.213 1.00 141.68 ? 83  SER A CB  1 
ATOM   236   O  OG  . SER A 1 67  ? 162.755 146.990 107.895 1.00 141.68 ? 83  SER A OG  1 
ATOM   237   N  N   . CYS A 1 68  ? 164.544 149.994 109.438 1.00 148.40 ? 84  CYS A N   1 
ATOM   238   C  CA  . CYS A 1 68  ? 165.053 151.112 108.649 1.00 148.40 ? 84  CYS A CA  1 
ATOM   239   C  C   . CYS A 1 68  ? 165.582 150.663 107.289 1.00 148.40 ? 84  CYS A C   1 
ATOM   240   O  O   . CYS A 1 68  ? 165.417 151.374 106.292 1.00 148.40 ? 84  CYS A O   1 
ATOM   241   C  CB  . CYS A 1 68  ? 166.144 151.845 109.428 1.00 148.40 ? 84  CYS A CB  1 
ATOM   242   S  SG  . CYS A 1 68  ? 165.720 152.208 111.148 1.00 148.40 ? 84  CYS A SG  1 
ATOM   243   N  N   . PHE A 1 69  ? 166.242 149.503 107.229 1.00 146.53 ? 85  PHE A N   1 
ATOM   244   C  CA  . PHE A 1 69  ? 166.811 149.043 105.962 1.00 146.53 ? 85  PHE A CA  1 
ATOM   245   C  C   . PHE A 1 69  ? 165.736 148.720 104.927 1.00 146.53 ? 85  PHE A C   1 
ATOM   246   O  O   . PHE A 1 69  ? 165.884 149.067 103.746 1.00 146.53 ? 85  PHE A O   1 
ATOM   247   C  CB  . PHE A 1 69  ? 167.705 147.829 106.215 1.00 146.53 ? 85  PHE A CB  1 
ATOM   248   C  CG  . PHE A 1 69  ? 167.975 147.005 104.991 1.00 146.53 ? 85  PHE A CG  1 
ATOM   249   C  CD1 . PHE A 1 69  ? 168.773 147.496 103.971 1.00 146.53 ? 85  PHE A CD1 1 
ATOM   250   C  CD2 . PHE A 1 69  ? 167.445 145.732 104.867 1.00 146.53 ? 85  PHE A CD2 1 
ATOM   251   C  CE1 . PHE A 1 69  ? 169.029 146.736 102.846 1.00 146.53 ? 85  PHE A CE1 1 
ATOM   252   C  CE2 . PHE A 1 69  ? 167.698 144.968 103.745 1.00 146.53 ? 85  PHE A CE2 1 
ATOM   253   C  CZ  . PHE A 1 69  ? 168.492 145.470 102.735 1.00 146.53 ? 85  PHE A CZ  1 
ATOM   254   N  N   . PHE A 1 70  ? 164.649 148.059 105.338 1.00 146.54 ? 86  PHE A N   1 
ATOM   255   C  CA  . PHE A 1 70  ? 163.541 147.845 104.410 1.00 146.54 ? 86  PHE A CA  1 
ATOM   256   C  C   . PHE A 1 70  ? 162.975 149.177 103.939 1.00 146.54 ? 86  PHE A C   1 
ATOM   257   O  O   . PHE A 1 70  ? 162.642 149.338 102.760 1.00 146.54 ? 86  PHE A O   1 
ATOM   258   C  CB  . PHE A 1 70  ? 162.447 146.992 105.047 1.00 146.54 ? 86  PHE A CB  1 
ATOM   259   C  CG  . PHE A 1 70  ? 162.630 145.513 104.848 1.00 146.54 ? 86  PHE A CG  1 
ATOM   260   C  CD1 . PHE A 1 70  ? 163.086 145.012 103.641 1.00 146.54 ? 86  PHE A CD1 1 
ATOM   261   C  CD2 . PHE A 1 70  ? 162.345 144.624 105.872 1.00 146.54 ? 86  PHE A CD2 1 
ATOM   262   C  CE1 . PHE A 1 70  ? 163.254 143.653 103.458 1.00 146.54 ? 86  PHE A CE1 1 
ATOM   263   C  CE2 . PHE A 1 70  ? 162.511 143.263 105.695 1.00 146.54 ? 86  PHE A CE2 1 
ATOM   264   C  CZ  . PHE A 1 70  ? 162.967 142.778 104.486 1.00 146.54 ? 86  PHE A CZ  1 
ATOM   265   N  N   . ARG A 1 71  ? 162.864 150.145 104.853 1.00 149.41 ? 87  ARG A N   1 
ATOM   266   C  CA  . ARG A 1 71  ? 162.412 151.479 104.475 1.00 149.41 ? 87  ARG A CA  1 
ATOM   267   C  C   . ARG A 1 71  ? 163.320 152.069 103.406 1.00 149.41 ? 87  ARG A C   1 
ATOM   268   O  O   . ARG A 1 71  ? 162.845 152.687 102.446 1.00 149.41 ? 87  ARG A O   1 
ATOM   269   C  CB  . ARG A 1 71  ? 162.374 152.384 105.706 1.00 149.41 ? 87  ARG A CB  1 
ATOM   270   C  CG  . ARG A 1 71  ? 161.799 153.766 105.455 1.00 149.41 ? 87  ARG A CG  1 
ATOM   271   C  CD  . ARG A 1 71  ? 161.980 154.662 106.673 1.00 149.41 ? 87  ARG A CD  1 
ATOM   272   N  NE  . ARG A 1 71  ? 161.676 153.967 107.919 1.00 149.41 ? 87  ARG A NE  1 
ATOM   273   C  CZ  . ARG A 1 71  ? 161.992 154.416 109.126 1.00 149.41 ? 87  ARG A CZ  1 
ATOM   274   N  NH1 . ARG A 1 71  ? 162.618 155.570 109.293 1.00 149.41 ? 87  ARG A NH1 1 
ATOM   275   N  NH2 . ARG A 1 71  ? 161.668 153.692 110.193 1.00 149.41 ? 87  ARG A NH2 1 
ATOM   276   N  N   . SER A 1 72  ? 164.634 151.896 103.565 1.00 138.94 ? 88  SER A N   1 
ATOM   277   C  CA  . SER A 1 72  ? 165.575 152.430 102.588 1.00 138.94 ? 88  SER A CA  1 
ATOM   278   C  C   . SER A 1 72  ? 165.385 151.767 101.230 1.00 138.94 ? 88  SER A C   1 
ATOM   279   O  O   . SER A 1 72  ? 165.367 152.447 100.198 1.00 138.94 ? 88  SER A O   1 
ATOM   280   C  CB  . SER A 1 72  ? 167.009 152.245 103.084 1.00 138.94 ? 88  SER A CB  1 
ATOM   281   N  N   . MET A 1 73  ? 165.243 150.437 101.207 1.00 145.10 ? 89  MET A N   1 
ATOM   282   C  CA  . MET A 1 73  ? 165.099 149.761 99.921  1.00 145.10 ? 89  MET A CA  1 
ATOM   283   C  C   . MET A 1 73  ? 163.690 149.898 99.353  1.00 145.10 ? 89  MET A C   1 
ATOM   284   O  O   . MET A 1 73  ? 163.529 149.964 98.129  1.00 145.10 ? 89  MET A O   1 
ATOM   285   C  CB  . MET A 1 73  ? 165.478 148.281 100.024 1.00 145.10 ? 89  MET A CB  1 
ATOM   286   C  CG  . MET A 1 73  ? 164.757 147.496 101.097 1.00 145.10 ? 89  MET A CG  1 
ATOM   287   S  SD  . MET A 1 73  ? 164.867 145.718 100.810 1.00 145.10 ? 89  MET A SD  1 
ATOM   288   C  CE  . MET A 1 73  ? 166.430 145.603 99.944  1.00 145.10 ? 89  MET A CE  1 
ATOM   289   N  N   . PHE A 1 74  ? 162.668 149.937 100.203 1.00 142.29 ? 90  PHE A N   1 
ATOM   290   C  CA  . PHE A 1 74  ? 161.299 150.112 99.724  1.00 142.29 ? 90  PHE A CA  1 
ATOM   291   C  C   . PHE A 1 74  ? 161.088 151.530 99.200  1.00 142.29 ? 90  PHE A C   1 
ATOM   292   O  O   . PHE A 1 74  ? 160.579 151.726 98.096  1.00 142.29 ? 90  PHE A O   1 
ATOM   293   C  CB  . PHE A 1 74  ? 160.285 149.812 100.831 1.00 142.29 ? 90  PHE A CB  1 
ATOM   294   C  CG  . PHE A 1 74  ? 160.207 148.360 101.210 1.00 142.29 ? 90  PHE A CG  1 
ATOM   295   C  CD1 . PHE A 1 74  ? 160.578 147.375 100.312 1.00 142.29 ? 90  PHE A CD1 1 
ATOM   296   C  CD2 . PHE A 1 74  ? 159.754 147.982 102.463 1.00 142.29 ? 90  PHE A CD2 1 
ATOM   297   C  CE1 . PHE A 1 74  ? 160.505 146.040 100.660 1.00 142.29 ? 90  PHE A CE1 1 
ATOM   298   C  CE2 . PHE A 1 74  ? 159.677 146.649 102.816 1.00 142.29 ? 90  PHE A CE2 1 
ATOM   299   C  CZ  . PHE A 1 74  ? 160.053 145.677 101.914 1.00 142.29 ? 90  PHE A CZ  1 
ATOM   300   N  N   . GLN A 1 89  ? 168.824 136.682 99.794  1.00 146.96 ? 105 GLN A N   1 
ATOM   301   C  CA  . GLN A 1 89  ? 169.994 135.870 99.485  1.00 146.96 ? 105 GLN A CA  1 
ATOM   302   C  C   . GLN A 1 89  ? 170.647 135.345 100.759 1.00 146.96 ? 105 GLN A C   1 
ATOM   303   O  O   . GLN A 1 89  ? 170.810 134.137 100.932 1.00 146.96 ? 105 GLN A O   1 
ATOM   304   C  CB  . GLN A 1 89  ? 171.006 136.677 98.669  1.00 146.96 ? 105 GLN A CB  1 
ATOM   305   N  N   . ASP A 1 90  ? 171.023 136.269 101.646 1.00 151.08 ? 106 ASP A N   1 
ATOM   306   C  CA  . ASP A 1 90  ? 171.667 135.880 102.897 1.00 151.08 ? 106 ASP A CA  1 
ATOM   307   C  C   . ASP A 1 90  ? 170.733 135.051 103.768 1.00 151.08 ? 106 ASP A C   1 
ATOM   308   O  O   . ASP A 1 90  ? 171.158 134.072 104.392 1.00 151.08 ? 106 ASP A O   1 
ATOM   309   C  CB  . ASP A 1 90  ? 172.142 137.122 103.651 1.00 151.08 ? 106 ASP A CB  1 
ATOM   310   N  N   . VAL A 1 91  ? 169.463 135.426 103.825 1.00 140.33 ? 107 VAL A N   1 
ATOM   311   C  CA  . VAL A 1 91  ? 168.486 134.761 104.678 1.00 140.33 ? 107 VAL A CA  1 
ATOM   312   C  C   . VAL A 1 91  ? 167.855 133.607 103.912 1.00 140.33 ? 107 VAL A C   1 
ATOM   313   O  O   . VAL A 1 91  ? 167.714 133.647 102.686 1.00 140.33 ? 107 VAL A O   1 
ATOM   314   C  CB  . VAL A 1 91  ? 167.421 135.767 105.160 1.00 140.33 ? 107 VAL A CB  1 
ATOM   315   C  CG1 . VAL A 1 91  ? 166.629 135.201 106.331 1.00 140.33 ? 107 VAL A CG1 1 
ATOM   316   C  CG2 . VAL A 1 91  ? 168.072 137.093 105.519 1.00 140.33 ? 107 VAL A CG2 1 
ATOM   317   N  N   . SER A 1 92  ? 167.472 132.565 104.643 1.00 138.47 ? 108 SER A N   1 
ATOM   318   C  CA  . SER A 1 92  ? 166.815 131.407 104.059 1.00 138.47 ? 108 SER A CA  1 
ATOM   319   C  C   . SER A 1 92  ? 165.300 131.590 104.075 1.00 138.47 ? 108 SER A C   1 
ATOM   320   O  O   . SER A 1 92  ? 164.759 132.438 104.788 1.00 138.47 ? 108 SER A O   1 
ATOM   321   C  CB  . SER A 1 92  ? 167.198 130.131 104.809 1.00 138.47 ? 108 SER A CB  1 
ATOM   322   O  OG  . SER A 1 92  ? 166.520 129.006 104.277 1.00 138.47 ? 108 SER A OG  1 
ATOM   323   N  N   . GLU A 1 93  ? 164.616 130.777 103.265 1.00 140.97 ? 109 GLU A N   1 
ATOM   324   C  CA  . GLU A 1 93  ? 163.160 130.853 103.197 1.00 140.97 ? 109 GLU A CA  1 
ATOM   325   C  C   . GLU A 1 93  ? 162.523 130.522 104.542 1.00 140.97 ? 109 GLU A C   1 
ATOM   326   O  O   . GLU A 1 93  ? 161.585 131.199 104.977 1.00 140.97 ? 109 GLU A O   1 
ATOM   327   C  CB  . GLU A 1 93  ? 162.636 129.916 102.109 1.00 140.97 ? 109 GLU A CB  1 
ATOM   328   N  N   . SER A 1 94  ? 163.025 129.483 105.215 1.00 141.94 ? 110 SER A N   1 
ATOM   329   C  CA  . SER A 1 94  ? 162.492 129.122 106.525 1.00 141.94 ? 110 SER A CA  1 
ATOM   330   C  C   . SER A 1 94  ? 162.707 130.243 107.534 1.00 141.94 ? 110 SER A C   1 
ATOM   331   O  O   . SER A 1 94  ? 161.812 130.557 108.326 1.00 141.94 ? 110 SER A O   1 
ATOM   332   C  CB  . SER A 1 94  ? 163.137 127.826 107.015 1.00 141.94 ? 110 SER A CB  1 
ATOM   333   O  OG  . SER A 1 94  ? 162.956 127.662 108.411 1.00 141.94 ? 110 SER A OG  1 
ATOM   334   N  N   . VAL A 1 95  ? 163.893 130.854 107.523 1.00 145.73 ? 111 VAL A N   1 
ATOM   335   C  CA  . VAL A 1 95  ? 164.167 131.956 108.437 1.00 145.73 ? 111 VAL A CA  1 
ATOM   336   C  C   . VAL A 1 95  ? 163.365 133.190 108.039 1.00 145.73 ? 111 VAL A C   1 
ATOM   337   O  O   . VAL A 1 95  ? 162.870 133.931 108.898 1.00 145.73 ? 111 VAL A O   1 
ATOM   338   C  CB  . VAL A 1 95  ? 165.678 132.248 108.484 1.00 145.73 ? 111 VAL A CB  1 
ATOM   339   C  CG1 . VAL A 1 95  ? 165.983 133.318 109.521 1.00 145.73 ? 111 VAL A CG1 1 
ATOM   340   C  CG2 . VAL A 1 95  ? 166.452 130.973 108.779 1.00 145.73 ? 111 VAL A CG2 1 
ATOM   341   N  N   . PHE A 1 96  ? 163.229 133.438 106.733 1.00 135.57 ? 112 PHE A N   1 
ATOM   342   C  CA  . PHE A 1 96  ? 162.446 134.585 106.284 1.00 135.57 ? 112 PHE A CA  1 
ATOM   343   C  C   . PHE A 1 96  ? 160.972 134.438 106.638 1.00 135.57 ? 112 PHE A C   1 
ATOM   344   O  O   . PHE A 1 96  ? 160.270 135.444 106.780 1.00 135.57 ? 112 PHE A O   1 
ATOM   345   C  CB  . PHE A 1 96  ? 162.613 134.782 104.778 1.00 135.57 ? 112 PHE A CB  1 
ATOM   346   C  CG  . PHE A 1 96  ? 162.073 136.089 104.279 1.00 135.57 ? 112 PHE A CG  1 
ATOM   347   C  CD1 . PHE A 1 96  ? 162.536 137.287 104.796 1.00 135.57 ? 112 PHE A CD1 1 
ATOM   348   C  CD2 . PHE A 1 96  ? 161.104 136.122 103.290 1.00 135.57 ? 112 PHE A CD2 1 
ATOM   349   C  CE1 . PHE A 1 96  ? 162.041 138.493 104.340 1.00 135.57 ? 112 PHE A CE1 1 
ATOM   350   C  CE2 . PHE A 1 96  ? 160.606 137.325 102.828 1.00 135.57 ? 112 PHE A CE2 1 
ATOM   351   C  CZ  . PHE A 1 96  ? 161.075 138.512 103.354 1.00 135.57 ? 112 PHE A CZ  1 
ATOM   352   N  N   . GLN A 1 97  ? 160.483 133.204 106.781 1.00 136.27 ? 113 GLN A N   1 
ATOM   353   C  CA  . GLN A 1 97  ? 159.114 133.006 107.249 1.00 136.27 ? 113 GLN A CA  1 
ATOM   354   C  C   . GLN A 1 97  ? 158.935 133.570 108.654 1.00 136.27 ? 113 GLN A C   1 
ATOM   355   O  O   . GLN A 1 97  ? 157.977 134.302 108.929 1.00 136.27 ? 113 GLN A O   1 
ATOM   356   C  CB  . GLN A 1 97  ? 158.756 131.520 107.212 1.00 136.27 ? 113 GLN A CB  1 
ATOM   357   N  N   . LEU A 1 98  ? 159.858 133.247 109.559 1.00 130.24 ? 114 LEU A N   1 
ATOM   358   C  CA  . LEU A 1 98  ? 159.795 133.823 110.896 1.00 130.24 ? 114 LEU A CA  1 
ATOM   359   C  C   . LEU A 1 98  ? 160.046 135.326 110.856 1.00 130.24 ? 114 LEU A C   1 
ATOM   360   O  O   . LEU A 1 98  ? 159.479 136.073 111.662 1.00 130.24 ? 114 LEU A O   1 
ATOM   361   C  CB  . LEU A 1 98  ? 160.800 133.125 111.811 1.00 130.24 ? 114 LEU A CB  1 
ATOM   362   C  CG  . LEU A 1 98  ? 160.859 133.581 113.267 1.00 130.24 ? 114 LEU A CG  1 
ATOM   363   C  CD1 . LEU A 1 98  ? 159.446 133.731 113.812 1.00 130.24 ? 114 LEU A CD1 1 
ATOM   364   C  CD2 . LEU A 1 98  ? 161.657 132.594 114.101 1.00 130.24 ? 114 LEU A CD2 1 
ATOM   365   N  N   . LEU A 1 99  ? 160.886 135.785 109.925 1.00 133.21 ? 115 LEU A N   1 
ATOM   366   C  CA  . LEU A 1 99  ? 161.119 137.219 109.771 1.00 133.21 ? 115 LEU A CA  1 
ATOM   367   C  C   . LEU A 1 99  ? 159.825 137.957 109.441 1.00 133.21 ? 115 LEU A C   1 
ATOM   368   O  O   . LEU A 1 99  ? 159.492 138.965 110.074 1.00 133.21 ? 115 LEU A O   1 
ATOM   369   C  CB  . LEU A 1 99  ? 162.172 137.465 108.689 1.00 133.21 ? 115 LEU A CB  1 
ATOM   370   N  N   . VAL A 1 100 ? 159.080 137.469 108.446 1.00 126.87 ? 116 VAL A N   1 
ATOM   371   C  CA  . VAL A 1 100 ? 157.821 138.116 108.083 1.00 126.87 ? 116 VAL A CA  1 
ATOM   372   C  C   . VAL A 1 100 ? 156.794 137.952 109.199 1.00 126.87 ? 116 VAL A C   1 
ATOM   373   O  O   . VAL A 1 100 ? 155.964 138.843 109.421 1.00 126.87 ? 116 VAL A O   1 
ATOM   374   C  CB  . VAL A 1 100 ? 157.294 137.611 106.724 1.00 126.87 ? 116 VAL A CB  1 
ATOM   375   C  CG1 . VAL A 1 100 ? 158.268 137.975 105.613 1.00 126.87 ? 116 VAL A CG1 1 
ATOM   376   C  CG2 . VAL A 1 100 ? 157.035 136.122 106.740 1.00 126.87 ? 116 VAL A CG2 1 
ATOM   377   N  N   . ASP A 1 101 ? 156.811 136.815 109.905 1.00 124.26 ? 117 ASP A N   1 
ATOM   378   C  CA  . ASP A 1 101 ? 155.919 136.646 111.049 1.00 124.26 ? 117 ASP A CA  1 
ATOM   379   C  C   . ASP A 1 101 ? 156.197 137.702 112.112 1.00 124.26 ? 117 ASP A C   1 
ATOM   380   O  O   . ASP A 1 101 ? 155.272 138.196 112.767 1.00 124.26 ? 117 ASP A O   1 
ATOM   381   C  CB  . ASP A 1 101 ? 156.068 135.241 111.631 1.00 124.26 ? 117 ASP A CB  1 
ATOM   382   N  N   . TYR A 1 102 ? 157.470 138.054 112.299 1.00 125.59 ? 118 TYR A N   1 
ATOM   383   C  CA  . TYR A 1 102 ? 157.823 139.122 113.229 1.00 125.59 ? 118 TYR A CA  1 
ATOM   384   C  C   . TYR A 1 102 ? 157.419 140.483 112.680 1.00 125.59 ? 118 TYR A C   1 
ATOM   385   O  O   . TYR A 1 102 ? 157.010 141.370 113.438 1.00 125.59 ? 118 TYR A O   1 
ATOM   386   C  CB  . TYR A 1 102 ? 159.327 139.089 113.501 1.00 125.59 ? 118 TYR A CB  1 
ATOM   387   C  CG  . TYR A 1 102 ? 159.829 140.169 114.434 1.00 125.59 ? 118 TYR A CG  1 
ATOM   388   C  CD1 . TYR A 1 102 ? 159.629 140.092 115.804 1.00 125.59 ? 118 TYR A CD1 1 
ATOM   389   C  CD2 . TYR A 1 102 ? 160.507 141.273 113.934 1.00 125.59 ? 118 TYR A CD2 1 
ATOM   390   C  CE1 . TYR A 1 102 ? 160.096 141.081 116.649 1.00 125.59 ? 118 TYR A CE1 1 
ATOM   391   C  CE2 . TYR A 1 102 ? 160.972 142.267 114.770 1.00 125.59 ? 118 TYR A CE2 1 
ATOM   392   C  CZ  . TYR A 1 102 ? 160.762 142.167 116.127 1.00 125.59 ? 118 TYR A CZ  1 
ATOM   393   O  OH  . TYR A 1 102 ? 161.225 143.155 116.966 1.00 125.59 ? 118 TYR A OH  1 
ATOM   394   N  N   . ILE A 1 103 ? 157.540 140.665 111.365 1.00 117.36 ? 119 ILE A N   1 
ATOM   395   C  CA  . ILE A 1 103 ? 157.181 141.941 110.750 1.00 117.36 ? 119 ILE A CA  1 
ATOM   396   C  C   . ILE A 1 103 ? 155.696 142.227 110.940 1.00 117.36 ? 119 ILE A C   1 
ATOM   397   O  O   . ILE A 1 103 ? 155.306 143.313 111.383 1.00 117.36 ? 119 ILE A O   1 
ATOM   398   C  CB  . ILE A 1 103 ? 157.570 141.950 109.261 1.00 117.36 ? 119 ILE A CB  1 
ATOM   399   C  CG1 . ILE A 1 103 ? 159.091 141.928 109.103 1.00 117.36 ? 119 ILE A CG1 1 
ATOM   400   C  CG2 . ILE A 1 103 ? 156.964 143.150 108.557 1.00 117.36 ? 119 ILE A CG2 1 
ATOM   401   C  CD1 . ILE A 1 103 ? 159.554 141.914 107.662 1.00 117.36 ? 119 ILE A CD1 1 
ATOM   402   N  N   . TYR A 1 104 ? 154.846 141.253 110.614 1.00 107.77 ? 120 TYR A N   1 
ATOM   403   C  CA  . TYR A 1 104 ? 153.406 141.479 110.641 1.00 107.77 ? 120 TYR A CA  1 
ATOM   404   C  C   . TYR A 1 104 ? 152.772 141.141 111.988 1.00 107.77 ? 120 TYR A C   1 
ATOM   405   O  O   . TYR A 1 104 ? 152.014 141.947 112.535 1.00 107.77 ? 120 TYR A O   1 
ATOM   406   C  CB  . TYR A 1 104 ? 152.734 140.665 109.532 1.00 107.77 ? 120 TYR A CB  1 
ATOM   407   C  CG  . TYR A 1 104 ? 153.060 141.144 108.137 1.00 107.77 ? 120 TYR A CG  1 
ATOM   408   C  CD1 . TYR A 1 104 ? 152.462 142.282 107.615 1.00 107.77 ? 120 TYR A CD1 1 
ATOM   409   C  CD2 . TYR A 1 104 ? 153.966 140.457 107.342 1.00 107.77 ? 120 TYR A CD2 1 
ATOM   410   C  CE1 . TYR A 1 104 ? 152.757 142.723 106.339 1.00 107.77 ? 120 TYR A CE1 1 
ATOM   411   C  CE2 . TYR A 1 104 ? 154.267 140.890 106.065 1.00 107.77 ? 120 TYR A CE2 1 
ATOM   412   C  CZ  . TYR A 1 104 ? 153.661 142.023 105.569 1.00 107.77 ? 120 TYR A CZ  1 
ATOM   413   O  OH  . TYR A 1 104 ? 153.957 142.457 104.298 1.00 107.77 ? 120 TYR A OH  1 
ATOM   414   N  N   . HIS A 1 105 ? 153.070 139.965 112.539 1.00 122.87 ? 121 HIS A N   1 
ATOM   415   C  CA  . HIS A 1 105 ? 152.389 139.504 113.743 1.00 122.87 ? 121 HIS A CA  1 
ATOM   416   C  C   . HIS A 1 105 ? 153.217 139.654 115.010 1.00 122.87 ? 121 HIS A C   1 
ATOM   417   O  O   . HIS A 1 105 ? 152.645 139.797 116.095 1.00 122.87 ? 121 HIS A O   1 
ATOM   418   C  CB  . HIS A 1 105 ? 151.982 138.034 113.590 1.00 122.87 ? 121 HIS A CB  1 
ATOM   419   C  CG  . HIS A 1 105 ? 151.442 137.692 112.236 1.00 122.87 ? 121 HIS A CG  1 
ATOM   420   N  ND1 . HIS A 1 105 ? 151.789 136.539 111.567 1.00 122.87 ? 121 HIS A ND1 1 
ATOM   421   C  CD2 . HIS A 1 105 ? 150.580 138.352 111.427 1.00 122.87 ? 121 HIS A CD2 1 
ATOM   422   C  CE1 . HIS A 1 105 ? 151.165 136.503 110.403 1.00 122.87 ? 121 HIS A CE1 1 
ATOM   423   N  NE2 . HIS A 1 105 ? 150.425 137.591 110.294 1.00 122.87 ? 121 HIS A NE2 1 
ATOM   424   N  N   . GLY A 1 106 ? 154.543 139.628 114.902 1.00 136.23 ? 122 GLY A N   1 
ATOM   425   C  CA  . GLY A 1 106 ? 155.390 139.708 116.074 1.00 136.23 ? 122 GLY A CA  1 
ATOM   426   C  C   . GLY A 1 106 ? 155.403 138.465 116.935 1.00 136.23 ? 122 GLY A C   1 
ATOM   427   O  O   . GLY A 1 106 ? 155.723 138.551 118.123 1.00 136.23 ? 122 GLY A O   1 
ATOM   428   N  N   . THR A 1 107 ? 155.063 137.308 116.370 1.00 126.17 ? 123 THR A N   1 
ATOM   429   C  CA  . THR A 1 107 ? 155.042 136.044 117.099 1.00 126.17 ? 123 THR A CA  1 
ATOM   430   C  C   . THR A 1 107 ? 156.289 135.260 116.710 1.00 126.17 ? 123 THR A C   1 
ATOM   431   O  O   . THR A 1 107 ? 156.413 134.806 115.569 1.00 126.17 ? 123 THR A O   1 
ATOM   432   C  CB  . THR A 1 107 ? 153.774 135.250 116.792 1.00 126.17 ? 123 THR A CB  1 
ATOM   433   N  N   . VAL A 1 108 ? 157.211 135.104 117.657 1.00 127.50 ? 124 VAL A N   1 
ATOM   434   C  CA  . VAL A 1 108 ? 158.521 134.514 117.401 1.00 127.50 ? 124 VAL A CA  1 
ATOM   435   C  C   . VAL A 1 108 ? 158.772 133.404 118.409 1.00 127.50 ? 124 VAL A C   1 
ATOM   436   O  O   . VAL A 1 108 ? 158.900 133.668 119.611 1.00 127.50 ? 124 VAL A O   1 
ATOM   437   C  CB  . VAL A 1 108 ? 159.646 135.557 117.465 1.00 127.50 ? 124 VAL A CB  1 
ATOM   438   C  CG1 . VAL A 1 108 ? 160.868 135.080 116.704 1.00 127.50 ? 124 VAL A CG1 1 
ATOM   439   C  CG2 . VAL A 1 108 ? 159.169 136.879 116.897 1.00 127.50 ? 124 VAL A CG2 1 
ATOM   440   N  N   . LYS A 1 109 ? 158.835 132.165 117.931 1.00 120.07 ? 125 LYS A N   1 
ATOM   441   C  CA  . LYS A 1 109 ? 159.408 131.079 118.705 1.00 120.07 ? 125 LYS A CA  1 
ATOM   442   C  C   . LYS A 1 109 ? 160.608 130.525 117.951 1.00 120.07 ? 125 LYS A C   1 
ATOM   443   O  O   . LYS A 1 109 ? 160.617 130.472 116.717 1.00 120.07 ? 125 LYS A O   1 
ATOM   444   C  CB  . LYS A 1 109 ? 158.384 129.967 118.958 1.00 120.07 ? 125 LYS A CB  1 
ATOM   445   N  N   . LEU A 1 110 ? 161.622 130.118 118.704 1.00 144.54 ? 126 LEU A N   1 
ATOM   446   C  CA  . LEU A 1 110 ? 162.861 129.596 118.147 1.00 144.54 ? 126 LEU A CA  1 
ATOM   447   C  C   . LEU A 1 110 ? 163.095 128.147 118.546 1.00 144.54 ? 126 LEU A C   1 
ATOM   448   O  O   . LEU A 1 110 ? 162.657 127.689 119.606 1.00 144.54 ? 126 LEU A O   1 
ATOM   449   C  CB  . LEU A 1 110 ? 164.088 130.437 118.515 1.00 144.54 ? 126 LEU A CB  1 
ATOM   450   C  CG  . LEU A 1 110 ? 164.764 130.359 119.875 1.00 144.54 ? 126 LEU A CG  1 
ATOM   451   C  CD1 . LEU A 1 110 ? 165.747 129.214 119.970 1.00 144.54 ? 126 LEU A CD1 1 
ATOM   452   C  CD2 . LEU A 1 110 ? 165.522 131.663 119.986 1.00 144.54 ? 126 LEU A CD2 1 
ATOM   453   N  N   . ARG A 1 111 ? 163.796 127.443 117.669 1.00 138.57 ? 127 ARG A N   1 
ATOM   454   C  CA  . ARG A 1 111 ? 164.441 126.179 117.979 1.00 138.57 ? 127 ARG A CA  1 
ATOM   455   C  C   . ARG A 1 111 ? 165.949 126.388 117.909 1.00 138.57 ? 127 ARG A C   1 
ATOM   456   O  O   . ARG A 1 111 ? 166.437 127.239 117.164 1.00 138.57 ? 127 ARG A O   1 
ATOM   457   C  CB  . ARG A 1 111 ? 163.997 125.078 117.012 1.00 138.57 ? 127 ARG A CB  1 
ATOM   458   C  CG  . ARG A 1 111 ? 162.888 124.187 117.554 1.00 138.57 ? 127 ARG A CG  1 
ATOM   459   C  CD  . ARG A 1 111 ? 161.676 125.005 117.983 1.00 138.57 ? 127 ARG A CD  1 
ATOM   460   N  NE  . ARG A 1 111 ? 161.089 125.749 116.874 1.00 138.57 ? 127 ARG A NE  1 
ATOM   461   C  CZ  . ARG A 1 111 ? 159.958 126.437 116.950 1.00 138.57 ? 127 ARG A CZ  1 
ATOM   462   N  NH1 . ARG A 1 111 ? 159.262 126.503 118.073 1.00 138.57 ? 127 ARG A NH1 1 
ATOM   463   N  NH2 . ARG A 1 111 ? 159.513 127.076 115.871 1.00 138.57 ? 127 ARG A NH2 1 
ATOM   464   N  N   . ALA A 1 112 ? 166.683 125.632 118.729 1.00 147.84 ? 128 ALA A N   1 
ATOM   465   C  CA  . ALA A 1 112 ? 168.075 125.964 119.032 1.00 147.84 ? 128 ALA A CA  1 
ATOM   466   C  C   . ALA A 1 112 ? 168.950 126.083 117.786 1.00 147.84 ? 128 ALA A C   1 
ATOM   467   O  O   . ALA A 1 112 ? 169.964 126.789 117.812 1.00 147.84 ? 128 ALA A O   1 
ATOM   468   C  CB  . ALA A 1 112 ? 168.662 124.921 119.984 1.00 147.84 ? 128 ALA A CB  1 
ATOM   469   N  N   . GLU A 1 113 ? 168.585 125.416 116.693 1.00 140.01 ? 129 GLU A N   1 
ATOM   470   C  CA  . GLU A 1 113 ? 169.462 125.307 115.531 1.00 140.01 ? 129 GLU A CA  1 
ATOM   471   C  C   . GLU A 1 113 ? 169.424 126.508 114.588 1.00 140.01 ? 129 GLU A C   1 
ATOM   472   O  O   . GLU A 1 113 ? 170.158 126.501 113.594 1.00 140.01 ? 129 GLU A O   1 
ATOM   473   C  CB  . GLU A 1 113 ? 169.118 124.040 114.742 1.00 140.01 ? 129 GLU A CB  1 
ATOM   474   N  N   . GLU A 1 114 ? 168.616 127.537 114.851 1.00 131.22 ? 130 GLU A N   1 
ATOM   475   C  CA  . GLU A 1 114 ? 168.490 128.650 113.914 1.00 131.22 ? 130 GLU A CA  1 
ATOM   476   C  C   . GLU A 1 114 ? 169.049 129.969 114.432 1.00 131.22 ? 130 GLU A C   1 
ATOM   477   O  O   . GLU A 1 114 ? 169.087 130.939 113.661 1.00 131.22 ? 130 GLU A O   1 
ATOM   478   C  CB  . GLU A 1 114 ? 167.024 128.869 113.500 1.00 131.22 ? 130 GLU A CB  1 
ATOM   479   C  CG  . GLU A 1 114 ? 165.996 128.610 114.576 1.00 131.22 ? 130 GLU A CG  1 
ATOM   480   C  CD  . GLU A 1 114 ? 164.639 128.231 114.017 1.00 131.22 ? 130 GLU A CD  1 
ATOM   481   O  OE1 . GLU A 1 114 ? 164.445 127.048 113.667 1.00 131.22 ? 130 GLU A OE1 1 
ATOM   482   O  OE2 . GLU A 1 114 ? 163.763 129.118 113.933 1.00 131.22 ? 130 GLU A OE2 1 
ATOM   483   N  N   . LEU A 1 115 ? 169.505 130.024 115.691 1.00 122.33 ? 131 LEU A N   1 
ATOM   484   C  CA  . LEU A 1 115 ? 169.982 131.277 116.279 1.00 122.33 ? 131 LEU A CA  1 
ATOM   485   C  C   . LEU A 1 115 ? 170.919 132.016 115.339 1.00 122.33 ? 131 LEU A C   1 
ATOM   486   O  O   . LEU A 1 115 ? 170.772 133.227 115.128 1.00 122.33 ? 131 LEU A O   1 
ATOM   487   C  CB  . LEU A 1 115 ? 170.712 131.002 117.596 1.00 122.33 ? 131 LEU A CB  1 
ATOM   488   C  CG  . LEU A 1 115 ? 169.990 131.173 118.929 1.00 122.33 ? 131 LEU A CG  1 
ATOM   489   C  CD1 . LEU A 1 115 ? 169.707 132.638 119.219 1.00 122.33 ? 131 LEU A CD1 1 
ATOM   490   C  CD2 . LEU A 1 115 ? 168.729 130.374 118.907 1.00 122.33 ? 131 LEU A CD2 1 
ATOM   491   N  N   . GLN A 1 116 ? 171.868 131.289 114.740 1.00 143.50 ? 132 GLN A N   1 
ATOM   492   C  CA  . GLN A 1 116 ? 172.806 131.863 113.784 1.00 143.50 ? 132 GLN A CA  1 
ATOM   493   C  C   . GLN A 1 116 ? 172.100 132.830 112.845 1.00 143.50 ? 132 GLN A C   1 
ATOM   494   O  O   . GLN A 1 116 ? 172.349 134.042 112.875 1.00 143.50 ? 132 GLN A O   1 
ATOM   495   C  CB  . GLN A 1 116 ? 173.496 130.744 112.997 1.00 143.50 ? 132 GLN A CB  1 
ATOM   496   C  CG  . GLN A 1 116 ? 174.500 131.232 111.964 1.00 143.50 ? 132 GLN A CG  1 
ATOM   497   C  CD  . GLN A 1 116 ? 175.770 131.773 112.592 1.00 143.50 ? 132 GLN A CD  1 
ATOM   498   O  OE1 . GLN A 1 116 ? 176.044 131.537 113.769 1.00 143.50 ? 132 GLN A OE1 1 
ATOM   499   N  NE2 . GLN A 1 116 ? 176.555 132.500 111.806 1.00 143.50 ? 132 GLN A NE2 1 
ATOM   500   N  N   . GLU A 1 117 ? 171.162 132.315 112.047 1.00 141.85 ? 133 GLU A N   1 
ATOM   501   C  CA  . GLU A 1 117 ? 170.470 133.188 111.108 1.00 141.85 ? 133 GLU A CA  1 
ATOM   502   C  C   . GLU A 1 117 ? 169.633 134.219 111.847 1.00 141.85 ? 133 GLU A C   1 
ATOM   503   O  O   . GLU A 1 117 ? 169.678 135.411 111.517 1.00 141.85 ? 133 GLU A O   1 
ATOM   504   C  CB  . GLU A 1 117 ? 169.605 132.364 110.153 1.00 141.85 ? 133 GLU A CB  1 
ATOM   505   C  CG  . GLU A 1 117 ? 170.324 131.754 108.937 1.00 141.85 ? 133 GLU A CG  1 
ATOM   506   C  CD  . GLU A 1 117 ? 171.493 132.576 108.389 1.00 141.85 ? 133 GLU A CD  1 
ATOM   507   O  OE1 . GLU A 1 117 ? 172.389 131.964 107.773 1.00 141.85 ? 133 GLU A OE1 1 
ATOM   508   O  OE2 . GLU A 1 117 ? 171.491 133.823 108.479 1.00 141.85 ? 133 GLU A OE2 1 
ATOM   509   N  N   . ILE A 1 118 ? 168.917 133.787 112.892 1.00 136.74 ? 134 ILE A N   1 
ATOM   510   C  CA  . ILE A 1 118 ? 168.118 134.708 113.691 1.00 136.74 ? 134 ILE A CA  1 
ATOM   511   C  C   . ILE A 1 118 ? 168.985 135.836 114.222 1.00 136.74 ? 134 ILE A C   1 
ATOM   512   O  O   . ILE A 1 118 ? 168.477 136.911 114.554 1.00 136.74 ? 134 ILE A O   1 
ATOM   513   C  CB  . ILE A 1 118 ? 167.403 133.942 114.828 1.00 136.74 ? 134 ILE A CB  1 
ATOM   514   C  CG1 . ILE A 1 118 ? 166.482 132.871 114.244 1.00 136.74 ? 134 ILE A CG1 1 
ATOM   515   C  CG2 . ILE A 1 118 ? 166.574 134.875 115.697 1.00 136.74 ? 134 ILE A CG2 1 
ATOM   516   C  CD1 . ILE A 1 118 ? 165.712 132.099 115.291 1.00 136.74 ? 134 ILE A CD1 1 
ATOM   517   N  N   . TYR A 1 119 ? 170.298 135.620 114.303 1.00 127.65 ? 135 TYR A N   1 
ATOM   518   C  CA  . TYR A 1 119 ? 171.205 136.719 114.599 1.00 127.65 ? 135 TYR A CA  1 
ATOM   519   C  C   . TYR A 1 119 ? 171.515 137.517 113.337 1.00 127.65 ? 135 TYR A C   1 
ATOM   520   O  O   . TYR A 1 119 ? 171.129 138.687 113.213 1.00 127.65 ? 135 TYR A O   1 
ATOM   521   C  CB  . TYR A 1 119 ? 172.488 136.174 115.231 1.00 127.65 ? 135 TYR A CB  1 
ATOM   522   C  CG  . TYR A 1 119 ? 173.393 137.229 115.817 1.00 127.65 ? 135 TYR A CG  1 
ATOM   523   C  CD1 . TYR A 1 119 ? 173.261 137.629 117.139 1.00 127.65 ? 135 TYR A CD1 1 
ATOM   524   C  CD2 . TYR A 1 119 ? 174.391 137.815 115.051 1.00 127.65 ? 135 TYR A CD2 1 
ATOM   525   C  CE1 . TYR A 1 119 ? 174.093 138.588 117.679 1.00 127.65 ? 135 TYR A CE1 1 
ATOM   526   C  CE2 . TYR A 1 119 ? 175.225 138.776 115.582 1.00 127.65 ? 135 TYR A CE2 1 
ATOM   527   C  CZ  . TYR A 1 119 ? 175.072 139.157 116.896 1.00 127.65 ? 135 TYR A CZ  1 
ATOM   528   O  OH  . TYR A 1 119 ? 175.900 140.115 117.427 1.00 127.65 ? 135 TYR A OH  1 
ATOM   529   N  N   . GLU A 1 120 ? 172.136 136.854 112.356 1.00 133.68 ? 136 GLU A N   1 
ATOM   530   C  CA  . GLU A 1 120 ? 172.660 137.528 111.171 1.00 133.68 ? 136 GLU A CA  1 
ATOM   531   C  C   . GLU A 1 120 ? 171.601 138.389 110.500 1.00 133.68 ? 136 GLU A C   1 
ATOM   532   O  O   . GLU A 1 120 ? 171.754 139.610 110.379 1.00 133.68 ? 136 GLU A O   1 
ATOM   533   C  CB  . GLU A 1 120 ? 173.214 136.490 110.194 1.00 133.68 ? 136 GLU A CB  1 
ATOM   534   C  CG  . GLU A 1 120 ? 174.622 136.029 110.520 1.00 133.68 ? 136 GLU A CG  1 
ATOM   535   C  CD  . GLU A 1 120 ? 175.355 135.497 109.307 1.00 133.68 ? 136 GLU A CD  1 
ATOM   536   O  OE1 . GLU A 1 120 ? 174.773 134.665 108.580 1.00 133.68 ? 136 GLU A OE1 1 
ATOM   537   O  OE2 . GLU A 1 120 ? 176.510 135.911 109.080 1.00 133.68 ? 136 GLU A OE2 1 
ATOM   538   N  N   . VAL A 1 121 ? 170.504 137.760 110.077 1.00 132.82 ? 137 VAL A N   1 
ATOM   539   C  CA  . VAL A 1 121 ? 169.433 138.491 109.409 1.00 132.82 ? 137 VAL A CA  1 
ATOM   540   C  C   . VAL A 1 121 ? 168.949 139.633 110.288 1.00 132.82 ? 137 VAL A C   1 
ATOM   541   O  O   . VAL A 1 121 ? 168.802 140.774 109.832 1.00 132.82 ? 137 VAL A O   1 
ATOM   542   C  CB  . VAL A 1 121 ? 168.282 137.537 109.044 1.00 132.82 ? 137 VAL A CB  1 
ATOM   543   N  N   . SER A 1 122 ? 168.724 139.350 111.572 1.00 125.40 ? 138 SER A N   1 
ATOM   544   C  CA  . SER A 1 122 ? 168.178 140.371 112.453 1.00 125.40 ? 138 SER A CA  1 
ATOM   545   C  C   . SER A 1 122 ? 169.154 141.511 112.703 1.00 125.40 ? 138 SER A C   1 
ATOM   546   O  O   . SER A 1 122 ? 168.745 142.534 113.257 1.00 125.40 ? 138 SER A O   1 
ATOM   547   C  CB  . SER A 1 122 ? 167.732 139.758 113.776 1.00 125.40 ? 138 SER A CB  1 
ATOM   548   O  OG  . SER A 1 122 ? 166.902 140.663 114.478 1.00 125.40 ? 138 SER A OG  1 
ATOM   549   N  N   . ASP A 1 123 ? 170.426 141.358 112.332 1.00 130.54 ? 139 ASP A N   1 
ATOM   550   C  CA  . ASP A 1 123 ? 171.362 142.472 112.373 1.00 130.54 ? 139 ASP A CA  1 
ATOM   551   C  C   . ASP A 1 123 ? 171.559 143.135 111.018 1.00 130.54 ? 139 ASP A C   1 
ATOM   552   O  O   . ASP A 1 123 ? 172.050 144.268 110.967 1.00 130.54 ? 139 ASP A O   1 
ATOM   553   C  CB  . ASP A 1 123 ? 172.726 142.012 112.904 1.00 130.54 ? 139 ASP A CB  1 
ATOM   554   C  CG  . ASP A 1 123 ? 172.795 142.015 114.416 1.00 130.54 ? 139 ASP A CG  1 
ATOM   555   O  OD1 . ASP A 1 123 ? 171.738 142.165 115.060 1.00 130.54 ? 139 ASP A OD1 1 
ATOM   556   O  OD2 . ASP A 1 123 ? 173.909 141.872 114.962 1.00 130.54 ? 139 ASP A OD2 1 
ATOM   557   N  N   . MET A 1 124 ? 171.186 142.466 109.928 1.00 121.63 ? 140 MET A N   1 
ATOM   558   C  CA  . MET A 1 124 ? 171.350 143.007 108.584 1.00 121.63 ? 140 MET A CA  1 
ATOM   559   C  C   . MET A 1 124 ? 170.061 143.615 108.048 1.00 121.63 ? 140 MET A C   1 
ATOM   560   O  O   . MET A 1 124 ? 170.070 144.732 107.521 1.00 121.63 ? 140 MET A O   1 
ATOM   561   C  CB  . MET A 1 124 ? 171.849 141.913 107.632 1.00 121.63 ? 140 MET A CB  1 
ATOM   562   N  N   . TYR A 1 125 ? 168.947 142.893 108.174 1.00 124.48 ? 141 TYR A N   1 
ATOM   563   C  CA  . TYR A 1 125 ? 167.671 143.386 107.669 1.00 124.48 ? 141 TYR A CA  1 
ATOM   564   C  C   . TYR A 1 125 ? 167.123 144.531 108.510 1.00 124.48 ? 141 TYR A C   1 
ATOM   565   O  O   . TYR A 1 125 ? 166.462 145.427 107.973 1.00 124.48 ? 141 TYR A O   1 
ATOM   566   C  CB  . TYR A 1 125 ? 166.654 142.246 107.609 1.00 124.48 ? 141 TYR A CB  1 
ATOM   567   C  CG  . TYR A 1 125 ? 166.690 141.457 106.320 1.00 124.48 ? 141 TYR A CG  1 
ATOM   568   C  CD1 . TYR A 1 125 ? 167.666 141.697 105.363 1.00 124.48 ? 141 TYR A CD1 1 
ATOM   569   C  CD2 . TYR A 1 125 ? 165.743 140.475 106.059 1.00 124.48 ? 141 TYR A CD2 1 
ATOM   570   C  CE1 . TYR A 1 125 ? 167.700 140.979 104.183 1.00 124.48 ? 141 TYR A CE1 1 
ATOM   571   C  CE2 . TYR A 1 125 ? 165.769 139.753 104.881 1.00 124.48 ? 141 TYR A CE2 1 
ATOM   572   C  CZ  . TYR A 1 125 ? 166.749 140.009 103.948 1.00 124.48 ? 141 TYR A CZ  1 
ATOM   573   O  OH  . TYR A 1 125 ? 166.779 139.292 102.774 1.00 124.48 ? 141 TYR A OH  1 
ATOM   574   N  N   . GLN A 1 126 ? 167.375 144.526 109.817 1.00 119.67 ? 142 GLN A N   1 
ATOM   575   C  CA  . GLN A 1 126 ? 166.729 145.485 110.702 1.00 119.67 ? 142 GLN A CA  1 
ATOM   576   C  C   . GLN A 1 126 ? 167.551 145.656 111.969 1.00 119.67 ? 142 GLN A C   1 
ATOM   577   O  O   . GLN A 1 126 ? 168.498 144.912 112.227 1.00 119.67 ? 142 GLN A O   1 
ATOM   578   C  CB  . GLN A 1 126 ? 165.314 145.028 111.062 1.00 119.67 ? 142 GLN A CB  1 
ATOM   579   C  CG  . GLN A 1 126 ? 165.261 143.748 111.878 1.00 119.67 ? 142 GLN A CG  1 
ATOM   580   C  CD  . GLN A 1 126 ? 164.047 142.902 111.551 1.00 119.67 ? 142 GLN A CD  1 
ATOM   581   O  OE1 . GLN A 1 126 ? 163.405 143.090 110.518 1.00 119.67 ? 142 GLN A OE1 1 
ATOM   582   N  NE2 . GLN A 1 126 ? 163.725 141.963 112.433 1.00 119.67 ? 142 GLN A NE2 1 
ATOM   583   N  N   . LEU A 1 127 ? 167.201 146.689 112.734 1.00 112.23 ? 143 LEU A N   1 
ATOM   584   C  CA  . LEU A 1 127 ? 167.752 146.908 114.065 1.00 112.23 ? 143 LEU A CA  1 
ATOM   585   C  C   . LEU A 1 127 ? 166.676 146.714 115.129 1.00 112.23 ? 143 LEU A C   1 
ATOM   586   O  O   . LEU A 1 127 ? 166.707 147.352 116.184 1.00 112.23 ? 143 LEU A O   1 
ATOM   587   C  CB  . LEU A 1 127 ? 168.372 148.300 114.171 1.00 112.23 ? 143 LEU A CB  1 
ATOM   588   N  N   . THR A 1 128 ? 165.719 145.832 114.851 1.00 113.63 ? 144 THR A N   1 
ATOM   589   C  CA  . THR A 1 128 ? 164.556 145.633 115.702 1.00 113.63 ? 144 THR A CA  1 
ATOM   590   C  C   . THR A 1 128 ? 164.953 144.986 117.027 1.00 113.63 ? 144 THR A C   1 
ATOM   591   O  O   . THR A 1 128 ? 166.107 144.614 117.257 1.00 113.63 ? 144 THR A O   1 
ATOM   592   C  CB  . THR A 1 128 ? 163.514 144.782 114.981 1.00 113.63 ? 144 THR A CB  1 
ATOM   593   N  N   . SER A 1 129 ? 163.963 144.852 117.914 1.00 126.84 ? 145 SER A N   1 
ATOM   594   C  CA  . SER A 1 129 ? 164.148 144.128 119.165 1.00 126.84 ? 145 SER A CA  1 
ATOM   595   C  C   . SER A 1 129 ? 164.409 142.646 118.938 1.00 126.84 ? 145 SER A C   1 
ATOM   596   O  O   . SER A 1 129 ? 164.839 141.959 119.872 1.00 126.84 ? 145 SER A O   1 
ATOM   597   C  CB  . SER A 1 129 ? 162.926 144.309 120.066 1.00 126.84 ? 145 SER A CB  1 
ATOM   598   N  N   . LEU A 1 130 ? 164.155 142.144 117.726 1.00 121.94 ? 146 LEU A N   1 
ATOM   599   C  CA  . LEU A 1 130 ? 164.482 140.760 117.404 1.00 121.94 ? 146 LEU A CA  1 
ATOM   600   C  C   . LEU A 1 130 ? 165.981 140.521 117.524 1.00 121.94 ? 146 LEU A C   1 
ATOM   601   O  O   . LEU A 1 130 ? 166.413 139.494 118.058 1.00 121.94 ? 146 LEU A O   1 
ATOM   602   C  CB  . LEU A 1 130 ? 163.986 140.416 116.000 1.00 121.94 ? 146 LEU A CB  1 
ATOM   603   C  CG  . LEU A 1 130 ? 164.218 138.980 115.530 1.00 121.94 ? 146 LEU A CG  1 
ATOM   604   C  CD1 . LEU A 1 130 ? 163.373 138.017 116.348 1.00 121.94 ? 146 LEU A CD1 1 
ATOM   605   C  CD2 . LEU A 1 130 ? 163.912 138.843 114.047 1.00 121.94 ? 146 LEU A CD2 1 
ATOM   606   N  N   . PHE A 1 131 ? 166.788 141.448 117.003 1.00 119.39 ? 147 PHE A N   1 
ATOM   607   C  CA  . PHE A 1 131 ? 168.238 141.319 117.103 1.00 119.39 ? 147 PHE A CA  1 
ATOM   608   C  C   . PHE A 1 131 ? 168.683 141.326 118.556 1.00 119.39 ? 147 PHE A C   1 
ATOM   609   O  O   . PHE A 1 131 ? 169.538 140.530 118.958 1.00 119.39 ? 147 PHE A O   1 
ATOM   610   C  CB  . PHE A 1 131 ? 168.917 142.450 116.335 1.00 119.39 ? 147 PHE A CB  1 
ATOM   611   N  N   . GLU A 1 132 ? 168.119 142.229 119.356 1.00 123.84 ? 148 GLU A N   1 
ATOM   612   C  CA  . GLU A 1 132 ? 168.472 142.284 120.767 1.00 123.84 ? 148 GLU A CA  1 
ATOM   613   C  C   . GLU A 1 132 ? 168.122 140.974 121.465 1.00 123.84 ? 148 GLU A C   1 
ATOM   614   O  O   . GLU A 1 132 ? 168.926 140.441 122.238 1.00 123.84 ? 148 GLU A O   1 
ATOM   615   C  CB  . GLU A 1 132 ? 167.775 143.470 121.428 1.00 123.84 ? 148 GLU A CB  1 
ATOM   616   N  N   . GLU A 1 133 ? 166.931 140.430 121.191 1.00 135.18 ? 149 GLU A N   1 
ATOM   617   C  CA  . GLU A 1 133 ? 166.527 139.180 121.832 1.00 135.18 ? 149 GLU A CA  1 
ATOM   618   C  C   . GLU A 1 133 ? 167.397 138.011 121.395 1.00 135.18 ? 149 GLU A C   1 
ATOM   619   O  O   . GLU A 1 133 ? 167.818 137.202 122.230 1.00 135.18 ? 149 GLU A O   1 
ATOM   620   C  CB  . GLU A 1 133 ? 165.062 138.872 121.519 1.00 135.18 ? 149 GLU A CB  1 
ATOM   621   C  CG  . GLU A 1 133 ? 164.420 137.851 122.455 1.00 135.18 ? 149 GLU A CG  1 
ATOM   622   C  CD  . GLU A 1 133 ? 164.315 138.328 123.883 1.00 135.18 ? 149 GLU A CD  1 
ATOM   623   O  OE1 . GLU A 1 133 ? 164.515 139.531 124.120 1.00 135.18 ? 149 GLU A OE1 1 
ATOM   624   O  OE2 . GLU A 1 133 ? 164.043 137.494 124.771 1.00 135.18 ? 149 GLU A OE2 1 
ATOM   625   N  N   . CYS A 1 134 ? 167.682 137.902 120.098 1.00 115.86 ? 150 CYS A N   1 
ATOM   626   C  CA  . CYS A 1 134 ? 168.510 136.801 119.624 1.00 115.86 ? 150 CYS A CA  1 
ATOM   627   C  C   . CYS A 1 134 ? 169.924 136.891 120.182 1.00 115.86 ? 150 CYS A C   1 
ATOM   628   O  O   . CYS A 1 134 ? 170.510 135.873 120.567 1.00 115.86 ? 150 CYS A O   1 
ATOM   629   C  CB  . CYS A 1 134 ? 168.533 136.777 118.097 1.00 115.86 ? 150 CYS A CB  1 
ATOM   630   S  SG  . CYS A 1 134 ? 169.634 137.990 117.362 1.00 115.86 ? 150 CYS A SG  1 
ATOM   631   N  N   . SER A 1 135 ? 170.495 138.098 120.226 1.00 119.06 ? 151 SER A N   1 
ATOM   632   C  CA  . SER A 1 135 ? 171.832 138.253 120.787 1.00 119.06 ? 151 SER A CA  1 
ATOM   633   C  C   . SER A 1 135 ? 171.861 137.953 122.281 1.00 119.06 ? 151 SER A C   1 
ATOM   634   O  O   . SER A 1 135 ? 172.797 137.307 122.766 1.00 119.06 ? 151 SER A O   1 
ATOM   635   C  CB  . SER A 1 135 ? 172.345 139.666 120.520 1.00 119.06 ? 151 SER A CB  1 
ATOM   636   N  N   . ARG A 1 136 ? 170.857 138.417 123.031 1.00 130.38 ? 152 ARG A N   1 
ATOM   637   C  CA  . ARG A 1 136 ? 170.783 138.070 124.447 1.00 130.38 ? 152 ARG A CA  1 
ATOM   638   C  C   . ARG A 1 136 ? 170.658 136.566 124.649 1.00 130.38 ? 152 ARG A C   1 
ATOM   639   O  O   . ARG A 1 136 ? 171.279 136.000 125.556 1.00 130.38 ? 152 ARG A O   1 
ATOM   640   C  CB  . ARG A 1 136 ? 169.628 138.804 125.129 1.00 130.38 ? 152 ARG A CB  1 
ATOM   641   C  CG  . ARG A 1 136 ? 169.941 140.255 125.454 1.00 130.38 ? 152 ARG A CG  1 
ATOM   642   C  CD  . ARG A 1 136 ? 168.718 141.005 125.952 1.00 130.38 ? 152 ARG A CD  1 
ATOM   643   N  NE  . ARG A 1 136 ? 167.878 141.552 124.895 1.00 130.38 ? 152 ARG A NE  1 
ATOM   644   C  CZ  . ARG A 1 136 ? 167.064 142.585 125.063 1.00 130.38 ? 152 ARG A CZ  1 
ATOM   645   N  NH1 . ARG A 1 136 ? 167.001 143.234 126.214 1.00 130.38 ? 152 ARG A NH1 1 
ATOM   646   N  NH2 . ARG A 1 136 ? 166.279 142.964 124.060 1.00 130.38 ? 152 ARG A NH2 1 
ATOM   647   N  N   . PHE A 1 137 ? 169.865 135.902 123.807 1.00 118.93 ? 153 PHE A N   1 
ATOM   648   C  CA  . PHE A 1 137 ? 169.721 134.454 123.903 1.00 118.93 ? 153 PHE A CA  1 
ATOM   649   C  C   . PHE A 1 137 ? 171.030 133.741 123.589 1.00 118.93 ? 153 PHE A C   1 
ATOM   650   O  O   . PHE A 1 137 ? 171.387 132.765 124.258 1.00 118.93 ? 153 PHE A O   1 
ATOM   651   C  CB  . PHE A 1 137 ? 168.624 133.986 122.953 1.00 118.93 ? 153 PHE A CB  1 
ATOM   652   C  CG  . PHE A 1 137 ? 168.066 132.644 123.293 1.00 118.93 ? 153 PHE A CG  1 
ATOM   653   C  CD1 . PHE A 1 137 ? 167.618 132.371 124.572 1.00 118.93 ? 153 PHE A CD1 1 
ATOM   654   C  CD2 . PHE A 1 137 ? 168.010 131.646 122.341 1.00 118.93 ? 153 PHE A CD2 1 
ATOM   655   C  CE1 . PHE A 1 137 ? 167.104 131.134 124.886 1.00 118.93 ? 153 PHE A CE1 1 
ATOM   656   C  CE2 . PHE A 1 137 ? 167.502 130.408 122.652 1.00 118.93 ? 153 PHE A CE2 1 
ATOM   657   C  CZ  . PHE A 1 137 ? 167.045 130.154 123.921 1.00 118.93 ? 153 PHE A CZ  1 
ATOM   658   N  N   . LEU A 1 138 ? 171.751 134.208 122.568 1.00 101.04 ? 154 LEU A N   1 
ATOM   659   C  CA  . LEU A 1 138 ? 173.053 133.630 122.256 1.00 101.04 ? 154 LEU A CA  1 
ATOM   660   C  C   . LEU A 1 138 ? 174.031 133.833 123.406 1.00 101.04 ? 154 LEU A C   1 
ATOM   661   O  O   . LEU A 1 138 ? 174.846 132.951 123.701 1.00 101.04 ? 154 LEU A O   1 
ATOM   662   C  CB  . LEU A 1 138 ? 173.600 134.236 120.965 1.00 101.04 ? 154 LEU A CB  1 
ATOM   663   C  CG  . LEU A 1 138 ? 173.467 133.360 119.718 1.00 101.04 ? 154 LEU A CG  1 
ATOM   664   C  CD1 . LEU A 1 138 ? 173.622 134.192 118.457 1.00 101.04 ? 154 LEU A CD1 1 
ATOM   665   C  CD2 . LEU A 1 138 ? 174.485 132.232 119.747 1.00 101.04 ? 154 LEU A CD2 1 
ATOM   666   N  N   . ALA A 1 139 ? 173.971 134.992 124.057 1.00 102.43 ? 155 ALA A N   1 
ATOM   667   C  CA  . ALA A 1 139 ? 174.816 135.295 125.210 1.00 102.43 ? 155 ALA A CA  1 
ATOM   668   C  C   . ALA A 1 139 ? 174.683 134.248 126.312 1.00 102.43 ? 155 ALA A C   1 
ATOM   669   O  O   . ALA A 1 139 ? 173.760 133.434 126.304 1.00 102.43 ? 155 ALA A O   1 
ATOM   670   C  CB  . ALA A 1 139 ? 174.484 136.677 125.753 1.00 102.43 ? 155 ALA A CB  1 
ATOM   671   N  N   . GLY A 1 145 ? 183.317 125.730 124.258 1.00 118.26 ? 161 GLY A N   1 
ATOM   672   C  CA  . GLY A 1 145 ? 182.998 124.942 123.083 1.00 118.26 ? 161 GLY A CA  1 
ATOM   673   C  C   . GLY A 1 145 ? 182.607 125.785 121.885 1.00 118.26 ? 161 GLY A C   1 
ATOM   674   O  O   . GLY A 1 145 ? 183.127 125.600 120.786 1.00 118.26 ? 161 GLY A O   1 
ATOM   675   N  N   . ASN A 1 146 ? 181.680 126.717 122.102 1.00 128.85 ? 162 ASN A N   1 
ATOM   676   C  CA  . ASN A 1 146 ? 181.215 127.618 121.058 1.00 128.85 ? 162 ASN A CA  1 
ATOM   677   C  C   . ASN A 1 146 ? 181.669 129.055 121.270 1.00 128.85 ? 162 ASN A C   1 
ATOM   678   O  O   . ASN A 1 146 ? 181.317 129.926 120.467 1.00 128.85 ? 162 ASN A O   1 
ATOM   679   C  CB  . ASN A 1 146 ? 179.686 127.569 120.962 1.00 128.85 ? 162 ASN A CB  1 
ATOM   680   C  CG  . ASN A 1 146 ? 179.008 128.060 122.226 1.00 128.85 ? 162 ASN A CG  1 
ATOM   681   O  OD1 . ASN A 1 146 ? 179.537 127.907 123.327 1.00 128.85 ? 162 ASN A OD1 1 
ATOM   682   N  ND2 . ASN A 1 146 ? 177.829 128.652 122.074 1.00 128.85 ? 162 ASN A ND2 1 
ATOM   683   N  N   . CYS A 1 147 ? 182.429 129.326 122.334 1.00 145.15 ? 163 CYS A N   1 
ATOM   684   C  CA  . CYS A 1 147 ? 182.857 130.692 122.621 1.00 145.15 ? 163 CYS A CA  1 
ATOM   685   C  C   . CYS A 1 147 ? 183.724 131.260 121.503 1.00 145.15 ? 163 CYS A C   1 
ATOM   686   O  O   . CYS A 1 147 ? 183.566 132.424 121.120 1.00 145.15 ? 163 CYS A O   1 
ATOM   687   C  CB  . CYS A 1 147 ? 183.601 130.737 123.956 1.00 145.15 ? 163 CYS A CB  1 
ATOM   688   S  SG  . CYS A 1 147 ? 185.000 129.601 124.070 1.00 145.15 ? 163 CYS A SG  1 
ATOM   689   N  N   . LEU A 1 148 ? 184.640 130.453 120.961 1.00 138.99 ? 164 LEU A N   1 
ATOM   690   C  CA  . LEU A 1 148 ? 185.575 130.953 119.954 1.00 138.99 ? 164 LEU A CA  1 
ATOM   691   C  C   . LEU A 1 148 ? 184.865 131.421 118.688 1.00 138.99 ? 164 LEU A C   1 
ATOM   692   O  O   . LEU A 1 148 ? 185.392 132.271 117.961 1.00 138.99 ? 164 LEU A O   1 
ATOM   693   C  CB  . LEU A 1 148 ? 186.607 129.876 119.618 1.00 138.99 ? 164 LEU A CB  1 
ATOM   694   C  CG  . LEU A 1 148 ? 187.461 129.388 120.790 1.00 138.99 ? 164 LEU A CG  1 
ATOM   695   C  CD1 . LEU A 1 148 ? 188.561 128.457 120.305 1.00 138.99 ? 164 LEU A CD1 1 
ATOM   696   C  CD2 . LEU A 1 148 ? 188.050 130.568 121.548 1.00 138.99 ? 164 LEU A CD2 1 
ATOM   697   N  N   . GLN A 1 149 ? 183.680 130.885 118.404 1.00 123.15 ? 165 GLN A N   1 
ATOM   698   C  CA  . GLN A 1 149 ? 182.926 131.259 117.213 1.00 123.15 ? 165 GLN A CA  1 
ATOM   699   C  C   . GLN A 1 149 ? 182.028 132.459 117.480 1.00 123.15 ? 165 GLN A C   1 
ATOM   700   O  O   . GLN A 1 149 ? 181.907 133.356 116.635 1.00 123.15 ? 165 GLN A O   1 
ATOM   701   C  CB  . GLN A 1 149 ? 182.090 130.075 116.720 1.00 123.15 ? 165 GLN A CB  1 
ATOM   702   N  N   . VAL A 1 150 ? 181.394 132.483 118.653 1.00 131.98 ? 166 VAL A N   1 
ATOM   703   C  CA  . VAL A 1 150 ? 180.542 133.603 119.028 1.00 131.98 ? 166 VAL A CA  1 
ATOM   704   C  C   . VAL A 1 150 ? 181.370 134.873 119.220 1.00 131.98 ? 166 VAL A C   1 
ATOM   705   O  O   . VAL A 1 150 ? 180.874 135.977 118.975 1.00 131.98 ? 166 VAL A O   1 
ATOM   706   C  CB  . VAL A 1 150 ? 179.699 133.225 120.261 1.00 131.98 ? 166 VAL A CB  1 
ATOM   707   C  CG1 . VAL A 1 150 ? 180.468 133.430 121.527 1.00 131.98 ? 166 VAL A CG1 1 
ATOM   708   C  CG2 . VAL A 1 150 ? 178.412 134.039 120.288 1.00 131.98 ? 166 VAL A CG2 1 
ATOM   709   N  N   . MET A 1 151 ? 182.630 134.748 119.653 1.00 137.90 ? 167 MET A N   1 
ATOM   710   C  CA  . MET A 1 151 ? 183.525 135.904 119.668 1.00 137.90 ? 167 MET A CA  1 
ATOM   711   C  C   . MET A 1 151 ? 183.635 136.526 118.283 1.00 137.90 ? 167 MET A C   1 
ATOM   712   O  O   . MET A 1 151 ? 183.478 137.742 118.120 1.00 137.90 ? 167 MET A O   1 
ATOM   713   C  CB  . MET A 1 151 ? 184.919 135.504 120.158 1.00 137.90 ? 167 MET A CB  1 
ATOM   714   C  CG  . MET A 1 151 ? 185.029 135.061 121.597 1.00 137.90 ? 167 MET A CG  1 
ATOM   715   S  SD  . MET A 1 151 ? 184.910 136.467 122.717 1.00 137.90 ? 167 MET A SD  1 
ATOM   716   C  CE  . MET A 1 151 ? 186.618 136.624 123.233 1.00 137.90 ? 167 MET A CE  1 
ATOM   717   N  N   . TRP A 1 152 ? 183.920 135.702 117.273 1.00 127.39 ? 168 TRP A N   1 
ATOM   718   C  CA  . TRP A 1 152 ? 184.059 136.217 115.916 1.00 127.39 ? 168 TRP A CA  1 
ATOM   719   C  C   . TRP A 1 152 ? 182.745 136.794 115.407 1.00 127.39 ? 168 TRP A C   1 
ATOM   720   O  O   . TRP A 1 152 ? 182.734 137.829 114.733 1.00 127.39 ? 168 TRP A O   1 
ATOM   721   C  CB  . TRP A 1 152 ? 184.555 135.110 114.988 1.00 127.39 ? 168 TRP A CB  1 
ATOM   722   N  N   . LEU A 1 153 ? 181.627 136.137 115.720 1.00 138.70 ? 169 LEU A N   1 
ATOM   723   C  CA  . LEU A 1 153 ? 180.330 136.649 115.286 1.00 138.70 ? 169 LEU A CA  1 
ATOM   724   C  C   . LEU A 1 153 ? 180.041 138.020 115.892 1.00 138.70 ? 169 LEU A C   1 
ATOM   725   O  O   . LEU A 1 153 ? 179.646 138.957 115.184 1.00 138.70 ? 169 LEU A O   1 
ATOM   726   C  CB  . LEU A 1 153 ? 179.230 135.653 115.654 1.00 138.70 ? 169 LEU A CB  1 
ATOM   727   N  N   . ALA A 1 154 ? 180.242 138.159 117.207 1.00 130.91 ? 170 ALA A N   1 
ATOM   728   C  CA  . ALA A 1 154 ? 180.016 139.440 117.868 1.00 130.91 ? 170 ALA A CA  1 
ATOM   729   C  C   . ALA A 1 154 ? 180.958 140.515 117.343 1.00 130.91 ? 170 ALA A C   1 
ATOM   730   O  O   . ALA A 1 154 ? 180.552 141.667 117.154 1.00 130.91 ? 170 ALA A O   1 
ATOM   731   C  CB  . ALA A 1 154 ? 180.165 139.285 119.381 1.00 130.91 ? 170 ALA A CB  1 
ATOM   732   N  N   . ASP A 1 155 ? 182.226 140.161 117.111 1.00 133.42 ? 171 ASP A N   1 
ATOM   733   C  CA  . ASP A 1 155 ? 183.174 141.128 116.569 1.00 133.42 ? 171 ASP A CA  1 
ATOM   734   C  C   . ASP A 1 155 ? 182.758 141.589 115.179 1.00 133.42 ? 171 ASP A C   1 
ATOM   735   O  O   . ASP A 1 155 ? 182.843 142.780 114.860 1.00 133.42 ? 171 ASP A O   1 
ATOM   736   C  CB  . ASP A 1 155 ? 184.577 140.523 116.537 1.00 133.42 ? 171 ASP A CB  1 
ATOM   737   N  N   . ARG A 1 156 ? 182.308 140.658 114.335 1.00 132.09 ? 172 ARG A N   1 
ATOM   738   C  CA  . ARG A 1 156 ? 181.955 141.013 112.968 1.00 132.09 ? 172 ARG A CA  1 
ATOM   739   C  C   . ARG A 1 156 ? 180.652 141.798 112.908 1.00 132.09 ? 172 ARG A C   1 
ATOM   740   O  O   . ARG A 1 156 ? 180.459 142.600 111.988 1.00 132.09 ? 172 ARG A O   1 
ATOM   741   C  CB  . ARG A 1 156 ? 181.857 139.756 112.104 1.00 132.09 ? 172 ARG A CB  1 
ATOM   742   N  N   . HIS A 1 157 ? 179.752 141.591 113.870 1.00 136.66 ? 173 HIS A N   1 
ATOM   743   C  CA  . HIS A 1 157 ? 178.469 142.283 113.872 1.00 136.66 ? 173 HIS A CA  1 
ATOM   744   C  C   . HIS A 1 157 ? 178.389 143.394 114.914 1.00 136.66 ? 173 HIS A C   1 
ATOM   745   O  O   . HIS A 1 157 ? 177.307 143.952 115.121 1.00 136.66 ? 173 HIS A O   1 
ATOM   746   C  CB  . HIS A 1 157 ? 177.337 141.277 114.087 1.00 136.66 ? 173 HIS A CB  1 
ATOM   747   C  CG  . HIS A 1 157 ? 177.214 140.267 112.990 1.00 136.66 ? 173 HIS A CG  1 
ATOM   748   N  ND1 . HIS A 1 157 ? 177.641 138.964 113.128 1.00 136.66 ? 173 HIS A ND1 1 
ATOM   749   C  CD2 . HIS A 1 157 ? 176.725 140.370 111.731 1.00 136.66 ? 173 HIS A CD2 1 
ATOM   750   C  CE1 . HIS A 1 157 ? 177.414 138.306 112.006 1.00 136.66 ? 173 HIS A CE1 1 
ATOM   751   N  NE2 . HIS A 1 157 ? 176.859 139.137 111.142 1.00 136.66 ? 173 HIS A NE2 1 
ATOM   752   N  N   . SER A 1 158 ? 179.506 143.738 115.556 1.00 140.13 ? 174 SER A N   1 
ATOM   753   C  CA  . SER A 1 158 ? 179.604 144.898 116.444 1.00 140.13 ? 174 SER A CA  1 
ATOM   754   C  C   . SER A 1 158 ? 178.523 144.872 117.526 1.00 140.13 ? 174 SER A C   1 
ATOM   755   O  O   . SER A 1 158 ? 177.677 145.762 117.626 1.00 140.13 ? 174 SER A O   1 
ATOM   756   C  CB  . SER A 1 158 ? 179.546 146.200 115.640 1.00 140.13 ? 174 SER A CB  1 
ATOM   757   N  N   . ASP A 1 159 ? 178.560 143.820 118.342 1.00 140.66 ? 175 ASP A N   1 
ATOM   758   C  CA  . ASP A 1 159 ? 177.636 143.693 119.465 1.00 140.66 ? 175 ASP A CA  1 
ATOM   759   C  C   . ASP A 1 159 ? 178.415 143.846 120.765 1.00 140.66 ? 175 ASP A C   1 
ATOM   760   O  O   . ASP A 1 159 ? 179.130 142.919 121.173 1.00 140.66 ? 175 ASP A O   1 
ATOM   761   C  CB  . ASP A 1 159 ? 176.913 142.342 119.412 1.00 140.66 ? 175 ASP A CB  1 
ATOM   762   C  CG  . ASP A 1 159 ? 175.962 142.111 120.588 1.00 140.66 ? 175 ASP A CG  1 
ATOM   763   O  OD1 . ASP A 1 159 ? 176.208 142.581 121.718 1.00 140.66 ? 175 ASP A OD1 1 
ATOM   764   O  OD2 . ASP A 1 159 ? 174.940 141.433 120.371 1.00 140.66 ? 175 ASP A OD2 1 
ATOM   765   N  N   . PRO A 1 160 ? 178.317 144.987 121.448 1.00 147.37 ? 176 PRO A N   1 
ATOM   766   C  CA  . PRO A 1 160 ? 179.061 145.188 122.697 1.00 147.37 ? 176 PRO A CA  1 
ATOM   767   C  C   . PRO A 1 160 ? 178.483 144.472 123.908 1.00 147.37 ? 176 PRO A C   1 
ATOM   768   O  O   . PRO A 1 160 ? 178.960 144.706 125.021 1.00 147.37 ? 176 PRO A O   1 
ATOM   769   C  CB  . PRO A 1 160 ? 178.989 146.711 122.885 1.00 147.37 ? 176 PRO A CB  1 
ATOM   770   C  CG  . PRO A 1 160 ? 177.707 147.096 122.238 1.00 147.37 ? 176 PRO A CG  1 
ATOM   771   C  CD  . PRO A 1 160 ? 177.546 146.180 121.058 1.00 147.37 ? 176 PRO A CD  1 
ATOM   772   N  N   . GLU A 1 161 ? 177.470 143.626 123.737 1.00 146.59 ? 177 GLU A N   1 
ATOM   773   C  CA  . GLU A 1 161 ? 176.895 142.844 124.828 1.00 146.59 ? 177 GLU A CA  1 
ATOM   774   C  C   . GLU A 1 161 ? 177.193 141.359 124.714 1.00 146.59 ? 177 GLU A C   1 
ATOM   775   O  O   . GLU A 1 161 ? 177.543 140.725 125.712 1.00 146.59 ? 177 GLU A O   1 
ATOM   776   C  CB  . GLU A 1 161 ? 175.378 143.053 124.888 1.00 146.59 ? 177 GLU A CB  1 
ATOM   777   N  N   . LEU A 1 162 ? 177.046 140.789 123.517 1.00 134.00 ? 178 LEU A N   1 
ATOM   778   C  CA  . LEU A 1 162 ? 177.456 139.408 123.287 1.00 134.00 ? 178 LEU A CA  1 
ATOM   779   C  C   . LEU A 1 162 ? 178.965 139.255 123.409 1.00 134.00 ? 178 LEU A C   1 
ATOM   780   O  O   . LEU A 1 162 ? 179.451 138.211 123.866 1.00 134.00 ? 178 LEU A O   1 
ATOM   781   C  CB  . LEU A 1 162 ? 176.986 138.958 121.903 1.00 134.00 ? 178 LEU A CB  1 
ATOM   782   C  CG  . LEU A 1 162 ? 177.234 137.518 121.453 1.00 134.00 ? 178 LEU A CG  1 
ATOM   783   C  CD1 . LEU A 1 162 ? 176.525 136.535 122.357 1.00 134.00 ? 178 LEU A CD1 1 
ATOM   784   C  CD2 . LEU A 1 162 ? 176.783 137.339 120.011 1.00 134.00 ? 178 LEU A CD2 1 
ATOM   785   N  N   . TYR A 1 163 ? 179.713 140.286 123.012 1.00 135.40 ? 179 TYR A N   1 
ATOM   786   C  CA  . TYR A 1 163 ? 181.169 140.217 123.033 1.00 135.40 ? 179 TYR A CA  1 
ATOM   787   C  C   . TYR A 1 163 ? 181.706 140.011 124.444 1.00 135.40 ? 179 TYR A C   1 
ATOM   788   O  O   . TYR A 1 163 ? 182.617 139.204 124.649 1.00 135.40 ? 179 TYR A O   1 
ATOM   789   C  CB  . TYR A 1 163 ? 181.767 141.475 122.407 1.00 135.40 ? 179 TYR A CB  1 
ATOM   790   C  CG  . TYR A 1 163 ? 183.149 141.258 121.837 1.00 135.40 ? 179 TYR A CG  1 
ATOM   791   C  CD1 . TYR A 1 163 ? 183.327 140.601 120.627 1.00 135.40 ? 179 TYR A CD1 1 
ATOM   792   C  CD2 . TYR A 1 163 ? 184.277 141.710 122.508 1.00 135.40 ? 179 TYR A CD2 1 
ATOM   793   C  CE1 . TYR A 1 163 ? 184.589 140.399 120.103 1.00 135.40 ? 179 TYR A CE1 1 
ATOM   794   C  CE2 . TYR A 1 163 ? 185.542 141.514 121.992 1.00 135.40 ? 179 TYR A CE2 1 
ATOM   795   C  CZ  . TYR A 1 163 ? 185.693 140.858 120.789 1.00 135.40 ? 179 TYR A CZ  1 
ATOM   796   O  OH  . TYR A 1 163 ? 186.952 140.660 120.272 1.00 135.40 ? 179 TYR A OH  1 
ATOM   797   N  N   . THR A 1 164 ? 181.173 140.738 125.431 1.00 134.94 ? 180 THR A N   1 
ATOM   798   C  CA  . THR A 1 164 ? 181.694 140.594 126.789 1.00 134.94 ? 180 THR A CA  1 
ATOM   799   C  C   . THR A 1 164 ? 181.329 139.241 127.389 1.00 134.94 ? 180 THR A C   1 
ATOM   800   O  O   . THR A 1 164 ? 182.144 138.632 128.090 1.00 134.94 ? 180 THR A O   1 
ATOM   801   C  CB  . THR A 1 164 ? 181.178 141.721 127.683 1.00 134.94 ? 180 THR A CB  1 
ATOM   802   O  OG1 . THR A 1 164 ? 180.766 141.178 128.944 1.00 134.94 ? 180 THR A OG1 1 
ATOM   803   C  CG2 . THR A 1 164 ? 179.997 142.417 127.036 1.00 134.94 ? 180 THR A CG2 1 
ATOM   804   N  N   . ALA A 1 165 ? 180.112 138.757 127.134 1.00 129.34 ? 181 ALA A N   1 
ATOM   805   C  CA  . ALA A 1 165 ? 179.728 137.433 127.617 1.00 129.34 ? 181 ALA A CA  1 
ATOM   806   C  C   . ALA A 1 165 ? 180.623 136.360 127.013 1.00 129.34 ? 181 ALA A C   1 
ATOM   807   O  O   . ALA A 1 165 ? 181.078 135.436 127.708 1.00 129.34 ? 181 ALA A O   1 
ATOM   808   C  CB  . ALA A 1 165 ? 178.261 137.157 127.292 1.00 129.34 ? 181 ALA A CB  1 
ATOM   809   N  N   . ALA A 1 166 ? 180.941 136.507 125.727 1.00 126.33 ? 182 ALA A N   1 
ATOM   810   C  CA  . ALA A 1 166 ? 181.802 135.538 125.068 1.00 126.33 ? 182 ALA A CA  1 
ATOM   811   C  C   . ALA A 1 166 ? 183.232 135.642 125.575 1.00 126.33 ? 182 ALA A C   1 
ATOM   812   O  O   . ALA A 1 166 ? 183.920 134.625 125.708 1.00 126.33 ? 182 ALA A O   1 
ATOM   813   C  CB  . ALA A 1 166 ? 181.742 135.753 123.562 1.00 126.33 ? 182 ALA A CB  1 
ATOM   814   N  N   . LYS A 1 167 ? 183.709 136.860 125.844 1.00 138.66 ? 183 LYS A N   1 
ATOM   815   C  CA  . LYS A 1 167 ? 185.056 137.009 126.378 1.00 138.66 ? 183 LYS A CA  1 
ATOM   816   C  C   . LYS A 1 167 ? 185.145 136.386 127.762 1.00 138.66 ? 183 LYS A C   1 
ATOM   817   O  O   . LYS A 1 167 ? 186.148 135.752 128.104 1.00 138.66 ? 183 LYS A O   1 
ATOM   818   C  CB  . LYS A 1 167 ? 185.450 138.486 126.417 1.00 138.66 ? 183 LYS A CB  1 
ATOM   819   N  N   . HIS A 1 168 ? 184.098 136.561 128.572 1.00 144.83 ? 184 HIS A N   1 
ATOM   820   C  CA  . HIS A 1 168 ? 184.037 135.917 129.879 1.00 144.83 ? 184 HIS A CA  1 
ATOM   821   C  C   . HIS A 1 168 ? 184.143 134.404 129.742 1.00 144.83 ? 184 HIS A C   1 
ATOM   822   O  O   . HIS A 1 168 ? 184.949 133.759 130.426 1.00 144.83 ? 184 HIS A O   1 
ATOM   823   C  CB  . HIS A 1 168 ? 182.746 136.316 130.595 1.00 144.83 ? 184 HIS A CB  1 
ATOM   824   C  CG  . HIS A 1 168 ? 182.602 135.726 131.963 1.00 144.83 ? 184 HIS A CG  1 
ATOM   825   N  ND1 . HIS A 1 168 ? 182.342 134.389 132.174 1.00 144.83 ? 184 HIS A ND1 1 
ATOM   826   C  CD2 . HIS A 1 168 ? 182.683 136.290 133.191 1.00 144.83 ? 184 HIS A CD2 1 
ATOM   827   C  CE1 . HIS A 1 168 ? 182.266 134.155 133.472 1.00 144.83 ? 184 HIS A CE1 1 
ATOM   828   N  NE2 . HIS A 1 168 ? 182.470 135.293 134.112 1.00 144.83 ? 184 HIS A NE2 1 
ATOM   829   N  N   . CYS A 1 169 ? 183.334 133.818 128.852 1.00 148.34 ? 185 CYS A N   1 
ATOM   830   C  CA  . CYS A 1 169 ? 183.371 132.367 128.682 1.00 148.34 ? 185 CYS A CA  1 
ATOM   831   C  C   . CYS A 1 169 ? 184.731 131.898 128.176 1.00 148.34 ? 185 CYS A C   1 
ATOM   832   O  O   . CYS A 1 169 ? 185.265 130.891 128.658 1.00 148.34 ? 185 CYS A O   1 
ATOM   833   C  CB  . CYS A 1 169 ? 182.263 131.920 127.728 1.00 148.34 ? 185 CYS A CB  1 
ATOM   834   S  SG  . CYS A 1 169 ? 182.073 130.126 127.594 1.00 148.34 ? 185 CYS A SG  1 
ATOM   835   N  N   . ALA A 1 170 ? 185.303 132.607 127.200 1.00 145.85 ? 186 ALA A N   1 
ATOM   836   C  CA  . ALA A 1 170 ? 186.590 132.210 126.637 1.00 145.85 ? 186 ALA A CA  1 
ATOM   837   C  C   . ALA A 1 170 ? 187.706 132.301 127.671 1.00 145.85 ? 186 ALA A C   1 
ATOM   838   O  O   . ALA A 1 170 ? 188.565 131.415 127.748 1.00 145.85 ? 186 ALA A O   1 
ATOM   839   C  CB  . ALA A 1 170 ? 186.919 133.070 125.417 1.00 145.85 ? 186 ALA A CB  1 
ATOM   840   N  N   . LYS A 1 171 ? 187.711 133.370 128.471 1.00 143.73 ? 187 LYS A N   1 
ATOM   841   C  CA  . LYS A 1 171 ? 188.723 133.527 129.510 1.00 143.73 ? 187 LYS A CA  1 
ATOM   842   C  C   . LYS A 1 171 ? 188.581 132.469 130.594 1.00 143.73 ? 187 LYS A C   1 
ATOM   843   O  O   . LYS A 1 171 ? 189.586 131.946 131.088 1.00 143.73 ? 187 LYS A O   1 
ATOM   844   C  CB  . LYS A 1 171 ? 188.640 134.929 130.113 1.00 143.73 ? 187 LYS A CB  1 
ATOM   845   N  N   . THR A 1 172 ? 187.347 132.146 130.988 1.00 152.39 ? 188 THR A N   1 
ATOM   846   C  CA  . THR A 1 172 ? 187.163 131.137 132.025 1.00 152.39 ? 188 THR A CA  1 
ATOM   847   C  C   . THR A 1 172 ? 187.648 129.770 131.554 1.00 152.39 ? 188 THR A C   1 
ATOM   848   O  O   . THR A 1 172 ? 188.242 129.011 132.329 1.00 152.39 ? 188 THR A O   1 
ATOM   849   C  CB  . THR A 1 172 ? 185.693 131.074 132.442 1.00 152.39 ? 188 THR A CB  1 
ATOM   850   O  OG1 . THR A 1 172 ? 185.297 132.337 132.990 1.00 152.39 ? 188 THR A OG1 1 
ATOM   851   C  CG2 . THR A 1 172 ? 185.479 129.992 133.489 1.00 152.39 ? 188 THR A CG2 1 
ATOM   852   N  N   . HIS A 1 173 ? 187.418 129.445 130.281 1.00 146.72 ? 189 HIS A N   1 
ATOM   853   C  CA  . HIS A 1 173 ? 187.785 128.152 129.714 1.00 146.72 ? 189 HIS A CA  1 
ATOM   854   C  C   . HIS A 1 173 ? 189.035 128.227 128.842 1.00 146.72 ? 189 HIS A C   1 
ATOM   855   O  O   . HIS A 1 173 ? 189.183 127.435 127.904 1.00 146.72 ? 189 HIS A O   1 
ATOM   856   C  CB  . HIS A 1 173 ? 186.613 127.570 128.924 1.00 146.72 ? 189 HIS A CB  1 
ATOM   857   C  CG  . HIS A 1 173 ? 185.459 127.149 129.781 1.00 146.72 ? 189 HIS A CG  1 
ATOM   858   N  ND1 . HIS A 1 173 ? 184.887 127.980 130.719 1.00 146.72 ? 189 HIS A ND1 1 
ATOM   859   C  CD2 . HIS A 1 173 ? 184.776 125.982 129.845 1.00 146.72 ? 189 HIS A CD2 1 
ATOM   860   C  CE1 . HIS A 1 173 ? 183.898 127.344 131.323 1.00 146.72 ? 189 HIS A CE1 1 
ATOM   861   N  NE2 . HIS A 1 173 ? 183.810 126.130 130.811 1.00 146.72 ? 189 HIS A NE2 1 
ATOM   862   N  N   . LEU A 1 174 ? 189.937 129.171 129.124 1.00 129.78 ? 190 LEU A N   1 
ATOM   863   C  CA  . LEU A 1 174 ? 191.154 129.292 128.325 1.00 129.78 ? 190 LEU A CA  1 
ATOM   864   C  C   . LEU A 1 174 ? 192.049 128.068 128.480 1.00 129.78 ? 190 LEU A C   1 
ATOM   865   O  O   . LEU A 1 174 ? 192.685 127.632 127.514 1.00 129.78 ? 190 LEU A O   1 
ATOM   866   C  CB  . LEU A 1 174 ? 191.914 130.561 128.711 1.00 129.78 ? 190 LEU A CB  1 
ATOM   867   C  CG  . LEU A 1 174 ? 192.932 131.087 127.696 1.00 129.78 ? 190 LEU A CG  1 
ATOM   868   C  CD1 . LEU A 1 174 ? 192.431 130.906 126.270 1.00 129.78 ? 190 LEU A CD1 1 
ATOM   869   C  CD2 . LEU A 1 174 ? 193.261 132.546 127.970 1.00 129.78 ? 190 LEU A CD2 1 
ATOM   870   N  N   . ALA A 1 175 ? 192.115 127.505 129.689 1.00 137.20 ? 191 ALA A N   1 
ATOM   871   C  CA  . ALA A 1 175 ? 192.909 126.299 129.905 1.00 137.20 ? 191 ALA A CA  1 
ATOM   872   C  C   . ALA A 1 175 ? 192.375 125.128 129.089 1.00 137.20 ? 191 ALA A C   1 
ATOM   873   O  O   . ALA A 1 175 ? 193.151 124.366 128.500 1.00 137.20 ? 191 ALA A O   1 
ATOM   874   C  CB  . ALA A 1 175 ? 192.937 125.949 131.392 1.00 137.20 ? 191 ALA A CB  1 
ATOM   875   N  N   . GLN A 1 176 ? 191.051 124.970 129.039 1.00 147.94 ? 192 GLN A N   1 
ATOM   876   C  CA  . GLN A 1 176 ? 190.457 123.854 128.312 1.00 147.94 ? 192 GLN A CA  1 
ATOM   877   C  C   . GLN A 1 176 ? 190.537 124.031 126.802 1.00 147.94 ? 192 GLN A C   1 
ATOM   878   O  O   . GLN A 1 176 ? 190.403 123.045 126.069 1.00 147.94 ? 192 GLN A O   1 
ATOM   879   C  CB  . GLN A 1 176 ? 188.999 123.669 128.736 1.00 147.94 ? 192 GLN A CB  1 
ATOM   880   N  N   . LEU A 1 177 ? 190.752 125.255 126.320 1.00 144.79 ? 193 LEU A N   1 
ATOM   881   C  CA  . LEU A 1 177 ? 190.844 125.528 124.891 1.00 144.79 ? 193 LEU A CA  1 
ATOM   882   C  C   . LEU A 1 177 ? 192.251 125.937 124.469 1.00 144.79 ? 193 LEU A C   1 
ATOM   883   O  O   . LEU A 1 177 ? 192.430 126.495 123.382 1.00 144.79 ? 193 LEU A O   1 
ATOM   884   C  CB  . LEU A 1 177 ? 189.837 126.608 124.493 1.00 144.79 ? 193 LEU A CB  1 
ATOM   885   N  N   . GLN A 1 178 ? 193.248 125.675 125.309 1.00 137.62 ? 194 GLN A N   1 
ATOM   886   C  CA  . GLN A 1 178 ? 194.631 126.020 124.998 1.00 137.62 ? 194 GLN A CA  1 
ATOM   887   C  C   . GLN A 1 178 ? 195.142 125.234 123.794 1.00 137.62 ? 194 GLN A C   1 
ATOM   888   O  O   . GLN A 1 178 ? 195.602 125.815 122.811 1.00 137.62 ? 194 GLN A O   1 
ATOM   889   C  CB  . GLN A 1 178 ? 195.530 125.768 126.209 1.00 137.62 ? 194 GLN A CB  1 
ATOM   890   N  N   . HIS A 1 188 ? 193.421 137.476 116.667 1.00 136.83 ? 204 HIS A N   1 
ATOM   891   C  CA  . HIS A 1 188 ? 194.640 138.128 117.131 1.00 136.83 ? 204 HIS A CA  1 
ATOM   892   C  C   . HIS A 1 188 ? 194.299 139.146 118.214 1.00 136.83 ? 204 HIS A C   1 
ATOM   893   O  O   . HIS A 1 188 ? 194.665 138.973 119.377 1.00 136.83 ? 204 HIS A O   1 
ATOM   894   C  CB  . HIS A 1 188 ? 195.371 138.800 115.963 1.00 136.83 ? 204 HIS A CB  1 
ATOM   895   C  CG  . HIS A 1 188 ? 196.762 139.251 116.290 1.00 136.83 ? 204 HIS A CG  1 
ATOM   896   N  ND1 . HIS A 1 188 ? 197.123 139.734 117.530 1.00 136.83 ? 204 HIS A ND1 1 
ATOM   897   C  CD2 . HIS A 1 188 ? 197.886 139.285 115.534 1.00 136.83 ? 204 HIS A CD2 1 
ATOM   898   C  CE1 . HIS A 1 188 ? 198.406 140.049 117.523 1.00 136.83 ? 204 HIS A CE1 1 
ATOM   899   N  NE2 . HIS A 1 188 ? 198.892 139.786 116.323 1.00 136.83 ? 204 HIS A NE2 1 
ATOM   900   N  N   . ARG A 1 189 ? 193.603 140.216 117.820 1.00 131.33 ? 205 ARG A N   1 
ATOM   901   C  CA  . ARG A 1 189 ? 193.156 141.208 118.792 1.00 131.33 ? 205 ARG A CA  1 
ATOM   902   C  C   . ARG A 1 189 ? 192.225 140.600 119.833 1.00 131.33 ? 205 ARG A C   1 
ATOM   903   O  O   . ARG A 1 189 ? 192.228 141.024 120.996 1.00 131.33 ? 205 ARG A O   1 
ATOM   904   C  CB  . ARG A 1 189 ? 192.466 142.371 118.078 1.00 131.33 ? 205 ARG A CB  1 
ATOM   905   N  N   . LEU A 1 190 ? 191.426 139.605 119.439 1.00 138.70 ? 206 LEU A N   1 
ATOM   906   C  CA  . LEU A 1 190 ? 190.562 138.933 120.403 1.00 138.70 ? 206 LEU A CA  1 
ATOM   907   C  C   . LEU A 1 190 ? 191.377 138.237 121.486 1.00 138.70 ? 206 LEU A C   1 
ATOM   908   O  O   . LEU A 1 190 ? 190.995 138.253 122.661 1.00 138.70 ? 206 LEU A O   1 
ATOM   909   C  CB  . LEU A 1 190 ? 189.655 137.933 119.686 1.00 138.70 ? 206 LEU A CB  1 
ATOM   910   N  N   . LEU A 1 191 ? 192.518 137.649 121.114 1.00 128.58 ? 207 LEU A N   1 
ATOM   911   C  CA  . LEU A 1 191 ? 193.381 137.014 122.107 1.00 128.58 ? 207 LEU A CA  1 
ATOM   912   C  C   . LEU A 1 191 ? 193.906 138.035 123.105 1.00 128.58 ? 207 LEU A C   1 
ATOM   913   O  O   . LEU A 1 191 ? 193.962 137.769 124.313 1.00 128.58 ? 207 LEU A O   1 
ATOM   914   C  CB  . LEU A 1 191 ? 194.537 136.293 121.415 1.00 128.58 ? 207 LEU A CB  1 
ATOM   915   N  N   . THR A 1 192 ? 194.296 139.212 122.615 1.00 131.41 ? 208 THR A N   1 
ATOM   916   C  CA  . THR A 1 192 ? 194.751 140.268 123.509 1.00 131.41 ? 208 THR A CA  1 
ATOM   917   C  C   . THR A 1 192 ? 193.631 140.709 124.440 1.00 131.41 ? 208 THR A C   1 
ATOM   918   O  O   . THR A 1 192 ? 193.873 140.991 125.617 1.00 131.41 ? 208 THR A O   1 
ATOM   919   C  CB  . THR A 1 192 ? 195.282 141.458 122.711 1.00 131.41 ? 208 THR A CB  1 
ATOM   920   O  OG1 . THR A 1 192 ? 194.421 141.712 121.597 1.00 131.41 ? 208 THR A OG1 1 
ATOM   921   C  CG2 . THR A 1 192 ? 196.686 141.172 122.202 1.00 131.41 ? 208 THR A CG2 1 
ATOM   922   N  N   . ASP A 1 193 ? 192.401 140.804 123.925 1.00 137.87 ? 209 ASP A N   1 
ATOM   923   C  CA  . ASP A 1 193 ? 191.277 141.161 124.788 1.00 137.87 ? 209 ASP A CA  1 
ATOM   924   C  C   . ASP A 1 193 ? 191.043 140.115 125.878 1.00 137.87 ? 209 ASP A C   1 
ATOM   925   O  O   . ASP A 1 193 ? 190.814 140.467 127.043 1.00 137.87 ? 209 ASP A O   1 
ATOM   926   C  CB  . ASP A 1 193 ? 190.014 141.350 123.949 1.00 137.87 ? 209 ASP A CB  1 
ATOM   927   N  N   . ILE A 1 194 ? 191.097 138.826 125.522 1.00 140.45 ? 210 ILE A N   1 
ATOM   928   C  CA  . ILE A 1 194 ? 190.988 137.773 126.536 1.00 140.45 ? 210 ILE A CA  1 
ATOM   929   C  C   . ILE A 1 194 ? 192.073 137.931 127.593 1.00 140.45 ? 210 ILE A C   1 
ATOM   930   O  O   . ILE A 1 194 ? 191.801 137.879 128.799 1.00 140.45 ? 210 ILE A O   1 
ATOM   931   C  CB  . ILE A 1 194 ? 191.014 136.365 125.908 1.00 140.45 ? 210 ILE A CB  1 
ATOM   932   C  CG1 . ILE A 1 194 ? 190.091 136.262 124.695 1.00 140.45 ? 210 ILE A CG1 1 
ATOM   933   C  CG2 . ILE A 1 194 ? 190.637 135.318 126.943 1.00 140.45 ? 210 ILE A CG2 1 
ATOM   934   C  CD1 . ILE A 1 194 ? 190.609 135.337 123.614 1.00 140.45 ? 210 ILE A CD1 1 
ATOM   935   N  N   . ILE A 1 195 ? 193.322 138.111 127.157 1.00 143.68 ? 211 ILE A N   1 
ATOM   936   C  CA  . ILE A 1 195 ? 194.430 138.206 128.105 1.00 143.68 ? 211 ILE A CA  1 
ATOM   937   C  C   . ILE A 1 195 ? 194.260 139.423 129.007 1.00 143.68 ? 211 ILE A C   1 
ATOM   938   O  O   . ILE A 1 195 ? 194.492 139.352 130.220 1.00 143.68 ? 211 ILE A O   1 
ATOM   939   C  CB  . ILE A 1 195 ? 195.774 138.238 127.355 1.00 143.68 ? 211 ILE A CB  1 
ATOM   940   N  N   . SER A 1 196 ? 193.859 140.558 128.430 1.00 151.84 ? 212 SER A N   1 
ATOM   941   C  CA  . SER A 1 196 ? 193.709 141.783 129.208 1.00 151.84 ? 212 SER A CA  1 
ATOM   942   C  C   . SER A 1 196 ? 192.580 141.653 130.222 1.00 151.84 ? 212 SER A C   1 
ATOM   943   O  O   . SER A 1 196 ? 192.671 142.190 131.332 1.00 151.84 ? 212 SER A O   1 
ATOM   944   C  CB  . SER A 1 196 ? 193.461 142.969 128.278 1.00 151.84 ? 212 SER A CB  1 
ATOM   945   O  OG  . SER A 1 196 ? 194.108 142.783 127.031 1.00 151.84 ? 212 SER A OG  1 
ATOM   946   N  N   . ASP A 1 197 ? 191.499 140.959 129.851 1.00 150.87 ? 213 ASP A N   1 
ATOM   947   C  CA  . ASP A 1 197 ? 190.370 140.805 130.763 1.00 150.87 ? 213 ASP A CA  1 
ATOM   948   C  C   . ASP A 1 197 ? 190.787 140.085 132.040 1.00 150.87 ? 213 ASP A C   1 
ATOM   949   O  O   . ASP A 1 197 ? 190.389 140.478 133.142 1.00 150.87 ? 213 ASP A O   1 
ATOM   950   C  CB  . ASP A 1 197 ? 189.234 140.056 130.069 1.00 150.87 ? 213 ASP A CB  1 
ATOM   951   N  N   . GLY A 1 198 ? 191.580 139.032 131.911 1.00 139.48 ? 214 GLY A N   1 
ATOM   952   C  CA  . GLY A 1 198 ? 192.082 138.281 133.038 1.00 139.48 ? 214 GLY A CA  1 
ATOM   953   C  C   . GLY A 1 198 ? 192.008 136.798 132.757 1.00 139.48 ? 214 GLY A C   1 
ATOM   954   O  O   . GLY A 1 198 ? 191.741 136.373 131.635 1.00 139.48 ? 214 GLY A O   1 
ATOM   955   N  N   . VAL A 1 199 ? 192.213 136.011 133.810 1.00 118.98 ? 215 VAL A N   1 
ATOM   956   C  CA  . VAL A 1 199 ? 192.157 134.552 133.748 1.00 118.98 ? 215 VAL A CA  1 
ATOM   957   C  C   . VAL A 1 199 ? 191.806 134.008 135.126 1.00 118.98 ? 215 VAL A C   1 
ATOM   958   O  O   . VAL A 1 199 ? 190.812 133.301 135.291 1.00 118.98 ? 215 VAL A O   1 
ATOM   959   C  CB  . VAL A 1 199 ? 193.490 133.932 133.259 1.00 118.98 ? 215 VAL A CB  1 
ATOM   960   C  CG1 . VAL A 1 199 ? 193.579 132.479 133.693 1.00 118.98 ? 215 VAL A CG1 1 
ATOM   961   C  CG2 . VAL A 1 199 ? 193.620 134.014 131.747 1.00 118.98 ? 215 VAL A CG2 1 
ATOM   962   N  N   . GLN A 1 203 ? 193.924 127.673 134.388 1.00 140.39 ? 219 GLN A N   1 
ATOM   963   C  CA  . GLN A 1 203 ? 194.529 128.940 134.780 1.00 140.39 ? 219 GLN A CA  1 
ATOM   964   C  C   . GLN A 1 203 ? 196.011 128.973 134.422 1.00 140.39 ? 219 GLN A C   1 
ATOM   965   O  O   . GLN A 1 203 ? 196.871 128.991 135.303 1.00 140.39 ? 219 GLN A O   1 
ATOM   966   C  CB  . GLN A 1 203 ? 194.343 129.181 136.279 1.00 140.39 ? 219 GLN A CB  1 
ATOM   967   N  N   . ASN A 1 204 ? 196.302 128.980 133.123 1.00 143.91 ? 220 ASN A N   1 
ATOM   968   C  CA  . ASN A 1 204 ? 197.672 129.011 132.611 1.00 143.91 ? 220 ASN A CA  1 
ATOM   969   C  C   . ASN A 1 204 ? 197.787 130.097 131.548 1.00 143.91 ? 220 ASN A C   1 
ATOM   970   O  O   . ASN A 1 204 ? 197.872 129.806 130.349 1.00 143.91 ? 220 ASN A O   1 
ATOM   971   C  CB  . ASN A 1 204 ? 198.077 127.647 132.050 1.00 143.91 ? 220 ASN A CB  1 
ATOM   972   N  N   . PRO A 1 205 ? 197.781 131.370 131.957 1.00 137.10 ? 221 PRO A N   1 
ATOM   973   C  CA  . PRO A 1 205 ? 197.896 132.450 130.958 1.00 137.10 ? 221 PRO A CA  1 
ATOM   974   C  C   . PRO A 1 205 ? 199.205 132.417 130.187 1.00 137.10 ? 221 PRO A C   1 
ATOM   975   O  O   . PRO A 1 205 ? 199.198 132.502 128.951 1.00 137.10 ? 221 PRO A O   1 
ATOM   976   C  CB  . PRO A 1 205 ? 197.761 133.725 131.806 1.00 137.10 ? 221 PRO A CB  1 
ATOM   977   C  CG  . PRO A 1 205 ? 197.139 133.286 133.092 1.00 137.10 ? 221 PRO A CG  1 
ATOM   978   C  CD  . PRO A 1 205 ? 197.621 131.892 133.324 1.00 137.10 ? 221 PRO A CD  1 
ATOM   979   N  N   . THR A 1 206 ? 200.336 132.307 130.889 1.00 133.73 ? 222 THR A N   1 
ATOM   980   C  CA  . THR A 1 206 ? 201.631 132.293 130.214 1.00 133.73 ? 222 THR A CA  1 
ATOM   981   C  C   . THR A 1 206 ? 201.768 131.081 129.301 1.00 133.73 ? 222 THR A C   1 
ATOM   982   O  O   . THR A 1 206 ? 202.294 131.190 128.187 1.00 133.73 ? 222 THR A O   1 
ATOM   983   C  CB  . THR A 1 206 ? 202.761 132.317 131.243 1.00 133.73 ? 222 THR A CB  1 
ATOM   984   N  N   . GLU A 1 207 ? 201.313 129.912 129.761 1.00 134.93 ? 223 GLU A N   1 
ATOM   985   C  CA  . GLU A 1 207 ? 201.390 128.713 128.934 1.00 134.93 ? 223 GLU A CA  1 
ATOM   986   C  C   . GLU A 1 207 ? 200.558 128.862 127.666 1.00 134.93 ? 223 GLU A C   1 
ATOM   987   O  O   . GLU A 1 207 ? 200.996 128.475 126.577 1.00 134.93 ? 223 GLU A O   1 
ATOM   988   C  CB  . GLU A 1 207 ? 200.936 127.493 129.735 1.00 134.93 ? 223 GLU A CB  1 
ATOM   989   N  N   . ALA A 1 208 ? 199.349 129.416 127.790 1.00 134.05 ? 224 ALA A N   1 
ATOM   990   C  CA  . ALA A 1 208 ? 198.515 129.639 126.614 1.00 134.05 ? 224 ALA A CA  1 
ATOM   991   C  C   . ALA A 1 208 ? 199.158 130.642 125.666 1.00 134.05 ? 224 ALA A C   1 
ATOM   992   O  O   . ALA A 1 208 ? 199.108 130.472 124.442 1.00 134.05 ? 224 ALA A O   1 
ATOM   993   C  CB  . ALA A 1 208 ? 197.125 130.113 127.037 1.00 134.05 ? 224 ALA A CB  1 
ATOM   994   N  N   . ILE A 1 209 ? 199.757 131.702 126.215 1.00 127.93 ? 225 ILE A N   1 
ATOM   995   C  CA  . ILE A 1 209 ? 200.429 132.699 125.385 1.00 127.93 ? 225 ILE A CA  1 
ATOM   996   C  C   . ILE A 1 209 ? 201.571 132.058 124.606 1.00 127.93 ? 225 ILE A C   1 
ATOM   997   O  O   . ILE A 1 209 ? 201.742 132.299 123.405 1.00 127.93 ? 225 ILE A O   1 
ATOM   998   C  CB  . ILE A 1 209 ? 200.924 133.873 126.249 1.00 127.93 ? 225 ILE A CB  1 
ATOM   999   N  N   . GLU A 1 210 ? 202.376 131.236 125.284 1.00 136.42 ? 226 GLU A N   1 
ATOM   1000  C  CA  . GLU A 1 210 ? 203.456 130.529 124.604 1.00 136.42 ? 226 GLU A CA  1 
ATOM   1001  C  C   . GLU A 1 210 ? 202.914 129.568 123.554 1.00 136.42 ? 226 GLU A C   1 
ATOM   1002  O  O   . GLU A 1 210 ? 203.472 129.456 122.456 1.00 136.42 ? 226 GLU A O   1 
ATOM   1003  C  CB  . GLU A 1 210 ? 204.317 129.781 125.623 1.00 136.42 ? 226 GLU A CB  1 
ATOM   1004  N  N   . ALA A 1 211 ? 201.832 128.864 123.873 1.00 142.38 ? 227 ALA A N   1 
ATOM   1005  C  CA  . ALA A 1 211 ? 201.222 127.926 122.938 1.00 142.38 ? 227 ALA A CA  1 
ATOM   1006  C  C   . ALA A 1 211 ? 200.591 128.659 121.758 1.00 142.38 ? 227 ALA A C   1 
ATOM   1007  O  O   . ALA A 1 211 ? 201.242 128.897 120.741 1.00 142.38 ? 227 ALA A O   1 
ATOM   1008  C  CB  . ALA A 1 211 ? 200.184 127.071 123.647 1.00 142.38 ? 227 ALA A CB  1 
ATOM   1009  N  N   . LEU A 1 227 ? 202.342 142.690 124.547 1.00 151.11 ? 243 LEU A N   1 
ATOM   1010  C  CA  . LEU A 1 227 ? 202.419 141.235 124.568 1.00 151.11 ? 243 LEU A CA  1 
ATOM   1011  C  C   . LEU A 1 227 ? 202.431 140.708 125.999 1.00 151.11 ? 243 LEU A C   1 
ATOM   1012  O  O   . LEU A 1 227 ? 201.385 140.370 126.553 1.00 151.11 ? 243 LEU A O   1 
ATOM   1013  C  CB  . LEU A 1 227 ? 203.663 140.752 123.819 1.00 151.11 ? 243 LEU A CB  1 
ATOM   1014  N  N   . ARG A 1 228 ? 203.627 140.635 126.588 1.00 148.18 ? 244 ARG A N   1 
ATOM   1015  C  CA  . ARG A 1 228 ? 203.749 140.151 127.960 1.00 148.18 ? 244 ARG A CA  1 
ATOM   1016  C  C   . ARG A 1 228 ? 203.024 141.068 128.937 1.00 148.18 ? 244 ARG A C   1 
ATOM   1017  O  O   . ARG A 1 228 ? 202.356 140.595 129.865 1.00 148.18 ? 244 ARG A O   1 
ATOM   1018  C  CB  . ARG A 1 228 ? 205.223 140.020 128.340 1.00 148.18 ? 244 ARG A CB  1 
ATOM   1019  N  N   . THR A 1 229 ? 203.146 142.385 128.749 1.00 159.52 ? 245 THR A N   1 
ATOM   1020  C  CA  . THR A 1 229 ? 202.483 143.330 129.640 1.00 159.52 ? 245 THR A CA  1 
ATOM   1021  C  C   . THR A 1 229 ? 200.968 143.300 129.497 1.00 159.52 ? 245 THR A C   1 
ATOM   1022  O  O   . THR A 1 229 ? 200.263 143.738 130.412 1.00 159.52 ? 245 THR A O   1 
ATOM   1023  C  CB  . THR A 1 229 ? 202.997 144.748 129.384 1.00 159.52 ? 245 THR A CB  1 
ATOM   1024  N  N   . SER A 1 230 ? 200.453 142.797 128.376 1.00 164.03 ? 246 SER A N   1 
ATOM   1025  C  CA  . SER A 1 230 ? 199.010 142.701 128.156 1.00 164.03 ? 246 SER A CA  1 
ATOM   1026  C  C   . SER A 1 230 ? 198.466 141.403 128.757 1.00 164.03 ? 246 SER A C   1 
ATOM   1027  O  O   . SER A 1 230 ? 197.876 140.561 128.082 1.00 164.03 ? 246 SER A O   1 
ATOM   1028  C  CB  . SER A 1 230 ? 198.695 142.800 126.667 1.00 164.03 ? 246 SER A CB  1 
ATOM   1029  N  N   . LEU A 1 231 ? 198.682 141.255 130.062 1.00 151.73 ? 247 LEU A N   1 
ATOM   1030  C  CA  . LEU A 1 231 ? 198.249 140.070 130.784 1.00 151.73 ? 247 LEU A CA  1 
ATOM   1031  C  C   . LEU A 1 231 ? 197.854 140.467 132.198 1.00 151.73 ? 247 LEU A C   1 
ATOM   1032  O  O   . LEU A 1 231 ? 198.353 141.455 132.742 1.00 151.73 ? 247 LEU A O   1 
ATOM   1033  C  CB  . LEU A 1 231 ? 199.349 139.000 130.810 1.00 151.73 ? 247 LEU A CB  1 
ATOM   1034  C  CG  . LEU A 1 231 ? 198.929 137.548 131.051 1.00 151.73 ? 247 LEU A CG  1 
ATOM   1035  C  CD1 . LEU A 1 231 ? 199.761 136.609 130.193 1.00 151.73 ? 247 LEU A CD1 1 
ATOM   1036  C  CD2 . LEU A 1 231 ? 199.061 137.181 132.521 1.00 151.73 ? 247 LEU A CD2 1 
ATOM   1037  N  N   . LYS A 1 232 ? 196.950 139.687 132.786 1.00 171.18 ? 248 LYS A N   1 
ATOM   1038  C  CA  . LYS A 1 232 ? 196.486 139.944 134.140 1.00 171.18 ? 248 LYS A CA  1 
ATOM   1039  C  C   . LYS A 1 232 ? 196.117 138.622 134.795 1.00 171.18 ? 248 LYS A C   1 
ATOM   1040  O  O   . LYS A 1 232 ? 195.922 137.605 134.123 1.00 171.18 ? 248 LYS A O   1 
ATOM   1041  C  CB  . LYS A 1 232 ? 195.290 140.904 134.155 1.00 171.18 ? 248 LYS A CB  1 
ATOM   1042  N  N   . GLU A 1 233 ? 196.025 138.648 136.122 1.00 164.34 ? 249 GLU A N   1 
ATOM   1043  C  CA  . GLU A 1 233 ? 195.703 137.457 136.890 1.00 164.34 ? 249 GLU A CA  1 
ATOM   1044  C  C   . GLU A 1 233 ? 194.862 137.850 138.095 1.00 164.34 ? 249 GLU A C   1 
ATOM   1045  O  O   . GLU A 1 233 ? 195.028 138.935 138.659 1.00 164.34 ? 249 GLU A O   1 
ATOM   1046  C  CB  . GLU A 1 233 ? 196.968 136.718 137.343 1.00 164.34 ? 249 GLU A CB  1 
ATOM   1047  N  N   . ILE A 1 234 ? 193.956 136.954 138.480 1.00 147.29 ? 250 ILE A N   1 
ATOM   1048  C  CA  . ILE A 1 234 ? 193.093 137.171 139.635 1.00 147.29 ? 250 ILE A CA  1 
ATOM   1049  C  C   . ILE A 1 234 ? 193.192 135.963 140.556 1.00 147.29 ? 250 ILE A C   1 
ATOM   1050  O  O   . ILE A 1 234 ? 192.279 135.692 141.345 1.00 147.29 ? 250 ILE A O   1 
ATOM   1051  C  CB  . ILE A 1 234 ? 191.637 137.426 139.208 1.00 147.29 ? 250 ILE A CB  1 
ATOM   1052  N  N   . GLY A 1 235 ? 194.304 135.242 140.469 1.00 147.47 ? 251 GLY A N   1 
ATOM   1053  C  CA  . GLY A 1 235 ? 194.483 134.055 141.289 1.00 147.47 ? 251 GLY A CA  1 
ATOM   1054  C  C   . GLY A 1 235 ? 193.436 133.012 140.953 1.00 147.47 ? 251 GLY A C   1 
ATOM   1055  O  O   . GLY A 1 235 ? 193.323 132.557 139.809 1.00 147.47 ? 251 GLY A O   1 
ATOM   1056  N  N   . GLU A 1 236 ? 192.652 132.621 141.957 1.00 141.21 ? 252 GLU A N   1 
ATOM   1057  C  CA  . GLU A 1 236 ? 191.582 131.635 141.784 1.00 141.21 ? 252 GLU A CA  1 
ATOM   1058  C  C   . GLU A 1 236 ? 190.358 132.162 142.529 1.00 141.21 ? 252 GLU A C   1 
ATOM   1059  O  O   . GLU A 1 236 ? 190.177 131.896 143.720 1.00 141.21 ? 252 GLU A O   1 
ATOM   1060  C  CB  . GLU A 1 236 ? 192.004 130.260 142.286 1.00 141.21 ? 252 GLU A CB  1 
ATOM   1061  N  N   . ASN A 1 237 ? 189.521 132.912 141.817 1.00 138.91 ? 253 ASN A N   1 
ATOM   1062  C  CA  . ASN A 1 237 ? 188.280 133.403 142.396 1.00 138.91 ? 253 ASN A CA  1 
ATOM   1063  C  C   . ASN A 1 237 ? 187.300 132.256 142.604 1.00 138.91 ? 253 ASN A C   1 
ATOM   1064  O  O   . ASN A 1 237 ? 187.199 131.344 141.778 1.00 138.91 ? 253 ASN A O   1 
ATOM   1065  C  CB  . ASN A 1 237 ? 187.658 134.470 141.497 1.00 138.91 ? 253 ASN A CB  1 
ATOM   1066  N  N   . VAL A 1 238 ? 186.575 132.305 143.721 1.00 126.06 ? 254 VAL A N   1 
ATOM   1067  C  CA  . VAL A 1 238 ? 185.621 131.251 144.044 1.00 126.06 ? 254 VAL A CA  1 
ATOM   1068  C  C   . VAL A 1 238 ? 184.446 131.323 143.080 1.00 126.06 ? 254 VAL A C   1 
ATOM   1069  O  O   . VAL A 1 238 ? 183.817 132.376 142.917 1.00 126.06 ? 254 VAL A O   1 
ATOM   1070  C  CB  . VAL A 1 238 ? 185.163 131.374 145.504 1.00 126.06 ? 254 VAL A CB  1 
ATOM   1071  C  CG1 . VAL A 1 238 ? 184.262 130.213 145.877 1.00 126.06 ? 254 VAL A CG1 1 
ATOM   1072  C  CG2 . VAL A 1 238 ? 186.368 131.430 146.427 1.00 126.06 ? 254 VAL A CG2 1 
ATOM   1073  N  N   . HIS A 1 239 ? 184.148 130.197 142.429 1.00 112.86 ? 255 HIS A N   1 
ATOM   1074  C  CA  . HIS A 1 239 ? 183.056 130.176 141.462 1.00 112.86 ? 255 HIS A CA  1 
ATOM   1075  C  C   . HIS A 1 239 ? 181.697 130.234 142.148 1.00 112.86 ? 255 HIS A C   1 
ATOM   1076  O  O   . HIS A 1 239 ? 180.818 130.995 141.728 1.00 112.86 ? 255 HIS A O   1 
ATOM   1077  C  CB  . HIS A 1 239 ? 183.161 128.929 140.584 1.00 112.86 ? 255 HIS A CB  1 
ATOM   1078  N  N   . ILE A 1 240 ? 181.506 129.448 143.205 1.00 108.92 ? 256 ILE A N   1 
ATOM   1079  C  CA  . ILE A 1 240 ? 180.215 129.357 143.880 1.00 108.92 ? 256 ILE A CA  1 
ATOM   1080  C  C   . ILE A 1 240 ? 180.464 129.162 145.369 1.00 108.92 ? 256 ILE A C   1 
ATOM   1081  O  O   . ILE A 1 240 ? 181.366 128.421 145.768 1.00 108.92 ? 256 ILE A O   1 
ATOM   1082  C  CB  . ILE A 1 240 ? 179.363 128.202 143.301 1.00 108.92 ? 256 ILE A CB  1 
ATOM   1083  C  CG1 . ILE A 1 240 ? 178.782 128.576 141.935 1.00 108.92 ? 256 ILE A CG1 1 
ATOM   1084  C  CG2 . ILE A 1 240 ? 178.244 127.807 144.254 1.00 108.92 ? 256 ILE A CG2 1 
ATOM   1085  C  CD1 . ILE A 1 240 ? 178.210 127.398 141.172 1.00 108.92 ? 256 ILE A CD1 1 
ATOM   1086  N  N   . TYR A 1 241 ? 179.662 129.827 146.192 1.00 110.71 ? 257 TYR A N   1 
ATOM   1087  C  CA  . TYR A 1 241 ? 179.678 129.626 147.632 1.00 110.71 ? 257 TYR A CA  1 
ATOM   1088  C  C   . TYR A 1 241 ? 178.422 128.883 148.061 1.00 110.71 ? 257 TYR A C   1 
ATOM   1089  O  O   . TYR A 1 241 ? 177.458 128.750 147.303 1.00 110.71 ? 257 TYR A O   1 
ATOM   1090  C  CB  . TYR A 1 241 ? 179.765 130.963 148.377 1.00 110.71 ? 257 TYR A CB  1 
ATOM   1091  C  CG  . TYR A 1 241 ? 181.093 131.675 148.273 1.00 110.71 ? 257 TYR A CG  1 
ATOM   1092  C  CD1 . TYR A 1 241 ? 181.373 132.515 147.205 1.00 110.71 ? 257 TYR A CD1 1 
ATOM   1093  C  CD2 . TYR A 1 241 ? 182.057 131.527 149.261 1.00 110.71 ? 257 TYR A CD2 1 
ATOM   1094  C  CE1 . TYR A 1 241 ? 182.582 133.178 147.119 1.00 110.71 ? 257 TYR A CE1 1 
ATOM   1095  C  CE2 . TYR A 1 241 ? 183.267 132.182 149.181 1.00 110.71 ? 257 TYR A CE2 1 
ATOM   1096  C  CZ  . TYR A 1 241 ? 183.525 133.006 148.110 1.00 110.71 ? 257 TYR A CZ  1 
ATOM   1097  O  OH  . TYR A 1 241 ? 184.734 133.656 148.029 1.00 110.71 ? 257 TYR A OH  1 
ATOM   1098  N  N   . LEU A 1 242 ? 178.438 128.399 149.301 1.00 100.74 ? 258 LEU A N   1 
ATOM   1099  C  CA  . LEU A 1 242 ? 177.285 127.683 149.828 1.00 100.74 ? 258 LEU A CA  1 
ATOM   1100  C  C   . LEU A 1 242 ? 177.387 127.603 151.342 1.00 100.74 ? 258 LEU A C   1 
ATOM   1101  O  O   . LEU A 1 242 ? 178.416 127.178 151.874 1.00 100.74 ? 258 LEU A O   1 
ATOM   1102  C  CB  . LEU A 1 242 ? 177.190 126.273 149.233 1.00 100.74 ? 258 LEU A CB  1 
ATOM   1103  N  N   . ILE A 1 243 ? 176.320 128.000 152.023 1.00 96.23  ? 259 ILE A N   1 
ATOM   1104  C  CA  . ILE A 1 243 ? 176.239 127.922 153.475 1.00 96.23  ? 259 ILE A CA  1 
ATOM   1105  C  C   . ILE A 1 243 ? 175.481 126.654 153.827 1.00 96.23  ? 259 ILE A C   1 
ATOM   1106  O  O   . ILE A 1 243 ? 174.371 126.427 153.324 1.00 96.23  ? 259 ILE A O   1 
ATOM   1107  C  CB  . ILE A 1 243 ? 175.566 129.165 154.084 1.00 96.23  ? 259 ILE A CB  1 
ATOM   1108  C  CG1 . ILE A 1 243 ? 176.501 130.378 154.041 1.00 96.23  ? 259 ILE A CG1 1 
ATOM   1109  C  CG2 . ILE A 1 243 ? 175.126 128.885 155.513 1.00 96.23  ? 259 ILE A CG2 1 
ATOM   1110  C  CD1 . ILE A 1 243 ? 176.672 131.009 152.686 1.00 96.23  ? 259 ILE A CD1 1 
ATOM   1111  N  N   . GLY A 1 244 ? 176.066 125.853 154.712 1.00 121.17 ? 260 GLY A N   1 
ATOM   1112  C  CA  . GLY A 1 244 ? 175.497 124.600 155.159 1.00 121.17 ? 260 GLY A CA  1 
ATOM   1113  C  C   . GLY A 1 244 ? 175.521 124.446 156.664 1.00 121.17 ? 260 GLY A C   1 
ATOM   1114  O  O   . GLY A 1 244 ? 175.662 125.428 157.398 1.00 121.17 ? 260 GLY A O   1 
ATOM   1115  N  N   . LYS A 1 245 ? 175.423 123.204 157.125 1.00 135.23 ? 261 LYS A N   1 
ATOM   1116  C  CA  . LYS A 1 245 ? 175.476 122.864 158.543 1.00 135.23 ? 261 LYS A CA  1 
ATOM   1117  C  C   . LYS A 1 245 ? 176.110 121.487 158.687 1.00 135.23 ? 261 LYS A C   1 
ATOM   1118  O  O   . LYS A 1 245 ? 177.041 121.145 157.954 1.00 135.23 ? 261 LYS A O   1 
ATOM   1119  C  CB  . LYS A 1 245 ? 174.078 122.848 159.182 1.00 135.23 ? 261 LYS A CB  1 
ATOM   1120  C  CG  . LYS A 1 245 ? 173.201 124.099 159.019 1.00 135.23 ? 261 LYS A CG  1 
ATOM   1121  C  CD  . LYS A 1 245 ? 173.712 125.309 159.805 1.00 135.23 ? 261 LYS A CD  1 
ATOM   1122  C  CE  . LYS A 1 245 ? 173.905 125.024 161.295 1.00 135.23 ? 261 LYS A CE  1 
ATOM   1123  N  NZ  . LYS A 1 245 ? 173.028 123.951 161.852 1.00 135.23 ? 261 LYS A NZ  1 
ATOM   1124  N  N   . SER A 1 252 ? 177.294 125.376 160.537 1.00 131.36 ? 268 SER A N   1 
ATOM   1125  C  CA  . SER A 1 252 ? 177.039 126.769 160.195 1.00 131.36 ? 268 SER A CA  1 
ATOM   1126  C  C   . SER A 1 252 ? 178.097 127.300 159.235 1.00 131.36 ? 268 SER A C   1 
ATOM   1127  O  O   . SER A 1 252 ? 177.930 128.364 158.641 1.00 131.36 ? 268 SER A O   1 
ATOM   1128  C  CB  . SER A 1 252 ? 176.991 127.629 161.459 1.00 131.36 ? 268 SER A CB  1 
ATOM   1129  O  OG  . SER A 1 252 ? 178.239 127.618 162.130 1.00 131.36 ? 268 SER A OG  1 
ATOM   1130  N  N   . LEU A 1 253 ? 179.184 126.548 159.092 1.00 120.94 ? 269 LEU A N   1 
ATOM   1131  C  CA  . LEU A 1 253 ? 180.307 126.975 158.270 1.00 120.94 ? 269 LEU A CA  1 
ATOM   1132  C  C   . LEU A 1 253 ? 179.917 127.057 156.796 1.00 120.94 ? 269 LEU A C   1 
ATOM   1133  O  O   . LEU A 1 253 ? 179.092 126.285 156.301 1.00 120.94 ? 269 LEU A O   1 
ATOM   1134  C  CB  . LEU A 1 253 ? 181.491 126.025 158.465 1.00 120.94 ? 269 LEU A CB  1 
ATOM   1135  C  CG  . LEU A 1 253 ? 181.430 124.616 157.869 1.00 120.94 ? 269 LEU A CG  1 
ATOM   1136  C  CD1 . LEU A 1 253 ? 182.142 124.553 156.529 1.00 120.94 ? 269 LEU A CD1 1 
ATOM   1137  C  CD2 . LEU A 1 253 ? 182.016 123.602 158.840 1.00 120.94 ? 269 LEU A CD2 1 
ATOM   1138  N  N   . ALA A 1 254 ? 180.523 128.014 156.097 1.00 105.30 ? 270 ALA A N   1 
ATOM   1139  C  CA  . ALA A 1 254 ? 180.286 128.237 154.676 1.00 105.30 ? 270 ALA A CA  1 
ATOM   1140  C  C   . ALA A 1 254 ? 181.462 127.697 153.873 1.00 105.30 ? 270 ALA A C   1 
ATOM   1141  O  O   . ALA A 1 254 ? 182.615 128.045 154.146 1.00 105.30 ? 270 ALA A O   1 
ATOM   1142  C  CB  . ALA A 1 254 ? 180.084 129.724 154.382 1.00 105.30 ? 270 ALA A CB  1 
ATOM   1143  N  N   . VAL A 1 255 ? 181.168 126.854 152.885 1.00 110.44 ? 271 VAL A N   1 
ATOM   1144  C  CA  . VAL A 1 255 ? 182.189 126.219 152.059 1.00 110.44 ? 271 VAL A CA  1 
ATOM   1145  C  C   . VAL A 1 255 ? 182.327 126.980 150.748 1.00 110.44 ? 271 VAL A C   1 
ATOM   1146  O  O   . VAL A 1 255 ? 181.329 127.246 150.065 1.00 110.44 ? 271 VAL A O   1 
ATOM   1147  C  CB  . VAL A 1 255 ? 181.846 124.744 151.794 1.00 110.44 ? 271 VAL A CB  1 
ATOM   1148  C  CG1 . VAL A 1 255 ? 183.065 124.006 151.285 1.00 110.44 ? 271 VAL A CG1 1 
ATOM   1149  C  CG2 . VAL A 1 255 ? 181.298 124.090 153.052 1.00 110.44 ? 271 VAL A CG2 1 
ATOM   1150  N  N   . SER A 1 256 ? 183.565 127.338 150.399 1.00 122.10 ? 272 SER A N   1 
ATOM   1151  C  CA  . SER A 1 256 ? 183.858 128.051 149.155 1.00 122.10 ? 272 SER A CA  1 
ATOM   1152  C  C   . SER A 1 256 ? 184.137 127.041 148.042 1.00 122.10 ? 272 SER A C   1 
ATOM   1153  O  O   . SER A 1 256 ? 185.282 126.737 147.705 1.00 122.10 ? 272 SER A O   1 
ATOM   1154  C  CB  . SER A 1 256 ? 185.027 129.008 149.353 1.00 122.10 ? 272 SER A CB  1 
ATOM   1155  O  OG  . SER A 1 256 ? 186.234 128.448 148.867 1.00 122.10 ? 272 SER A OG  1 
ATOM   1156  N  N   . LEU A 1 257 ? 183.059 126.508 147.469 1.00 124.38 ? 273 LEU A N   1 
ATOM   1157  C  CA  . LEU A 1 257 ? 183.183 125.533 146.390 1.00 124.38 ? 273 LEU A CA  1 
ATOM   1158  C  C   . LEU A 1 257 ? 183.878 126.146 145.178 1.00 124.38 ? 273 LEU A C   1 
ATOM   1159  O  O   . LEU A 1 257 ? 183.632 127.298 144.816 1.00 124.38 ? 273 LEU A O   1 
ATOM   1160  C  CB  . LEU A 1 257 ? 181.808 124.992 145.995 1.00 124.38 ? 273 LEU A CB  1 
ATOM   1161  C  CG  . LEU A 1 257 ? 181.088 124.097 147.009 1.00 124.38 ? 273 LEU A CG  1 
ATOM   1162  C  CD1 . LEU A 1 257 ? 182.078 123.193 147.727 1.00 124.38 ? 273 LEU A CD1 1 
ATOM   1163  C  CD2 . LEU A 1 257 ? 180.287 124.917 148.005 1.00 124.38 ? 273 LEU A CD2 1 
ATOM   1164  N  N   . HIS A 1 258 ? 184.749 125.365 144.543 1.00 143.08 ? 274 HIS A N   1 
ATOM   1165  C  CA  . HIS A 1 258 ? 185.530 125.817 143.399 1.00 143.08 ? 274 HIS A CA  1 
ATOM   1166  C  C   . HIS A 1 258 ? 185.233 124.924 142.202 1.00 143.08 ? 274 HIS A C   1 
ATOM   1167  O  O   . HIS A 1 258 ? 185.251 123.695 142.317 1.00 143.08 ? 274 HIS A O   1 
ATOM   1168  C  CB  . HIS A 1 258 ? 187.028 125.807 143.714 1.00 143.08 ? 274 HIS A CB  1 
ATOM   1169  C  CG  . HIS A 1 258 ? 187.776 126.960 143.122 1.00 143.08 ? 274 HIS A CG  1 
ATOM   1170  N  ND1 . HIS A 1 258 ? 188.193 128.040 143.871 1.00 143.08 ? 274 HIS A ND1 1 
ATOM   1171  C  CD2 . HIS A 1 258 ? 188.181 127.204 141.853 1.00 143.08 ? 274 HIS A CD2 1 
ATOM   1172  C  CE1 . HIS A 1 258 ? 188.824 128.898 143.089 1.00 143.08 ? 274 HIS A CE1 1 
ATOM   1173  N  NE2 . HIS A 1 258 ? 188.830 128.415 141.860 1.00 143.08 ? 274 HIS A NE2 1 
ATOM   1174  N  N   . CYS A 1 259 ? 184.953 125.534 141.056 1.00 165.39 ? 275 CYS A N   1 
ATOM   1175  C  CA  . CYS A 1 259 ? 184.630 124.778 139.854 1.00 165.39 ? 275 CYS A CA  1 
ATOM   1176  C  C   . CYS A 1 259 ? 185.863 124.684 138.966 1.00 165.39 ? 275 CYS A C   1 
ATOM   1177  O  O   . CYS A 1 259 ? 186.466 125.705 138.619 1.00 165.39 ? 275 CYS A O   1 
ATOM   1178  C  CB  . CYS A 1 259 ? 183.477 125.432 139.092 1.00 165.39 ? 275 CYS A CB  1 
ATOM   1179  N  N   . ALA A 1 260 ? 186.228 123.456 138.606 1.00 169.55 ? 276 ALA A N   1 
ATOM   1180  C  CA  . ALA A 1 260 ? 187.371 123.175 137.748 1.00 169.55 ? 276 ALA A CA  1 
ATOM   1181  C  C   . ALA A 1 260 ? 186.913 122.354 136.552 1.00 169.55 ? 276 ALA A C   1 
ATOM   1182  O  O   . ALA A 1 260 ? 186.209 121.352 136.716 1.00 169.55 ? 276 ALA A O   1 
ATOM   1183  C  CB  . ALA A 1 260 ? 188.468 122.432 138.515 1.00 169.55 ? 276 ALA A CB  1 
ATOM   1184  N  N   . GLU A 1 261 ? 187.312 122.776 135.357 1.00 167.99 ? 277 GLU A N   1 
ATOM   1185  C  CA  . GLU A 1 261 ? 186.932 122.073 134.137 1.00 167.99 ? 277 GLU A CA  1 
ATOM   1186  C  C   . GLU A 1 261 ? 188.008 121.074 133.725 1.00 167.99 ? 277 GLU A C   1 
ATOM   1187  O  O   . GLU A 1 261 ? 187.718 119.908 133.459 1.00 167.99 ? 277 GLU A O   1 
ATOM   1188  C  CB  . GLU A 1 261 ? 186.674 123.067 133.003 1.00 167.99 ? 277 GLU A CB  1 
ATOM   1189  N  N   . SER A 1 264 ? 183.200 118.971 136.913 1.00 154.11 ? 280 SER A N   1 
ATOM   1190  C  CA  . SER A 1 264 ? 183.514 118.460 138.243 1.00 154.11 ? 280 SER A CA  1 
ATOM   1191  C  C   . SER A 1 264 ? 183.512 119.581 139.277 1.00 154.11 ? 280 SER A C   1 
ATOM   1192  O  O   . SER A 1 264 ? 183.414 120.758 138.930 1.00 154.11 ? 280 SER A O   1 
ATOM   1193  C  CB  . SER A 1 264 ? 184.869 117.750 138.238 1.00 154.11 ? 280 SER A CB  1 
ATOM   1194  O  OG  . SER A 1 264 ? 185.869 118.561 137.647 1.00 154.11 ? 280 SER A OG  1 
ATOM   1195  N  N   . ILE A 1 265 ? 183.622 119.207 140.550 1.00 154.45 ? 281 ILE A N   1 
ATOM   1196  C  CA  . ILE A 1 265 ? 183.578 120.154 141.655 1.00 154.45 ? 281 ILE A CA  1 
ATOM   1197  C  C   . ILE A 1 265 ? 184.795 119.915 142.539 1.00 154.45 ? 281 ILE A C   1 
ATOM   1198  O  O   . ILE A 1 265 ? 185.335 118.806 142.599 1.00 154.45 ? 281 ILE A O   1 
ATOM   1199  C  CB  . ILE A 1 265 ? 182.260 120.022 142.458 1.00 154.45 ? 281 ILE A CB  1 
ATOM   1200  C  CG1 . ILE A 1 265 ? 182.138 121.121 143.516 1.00 154.45 ? 281 ILE A CG1 1 
ATOM   1201  C  CG2 . ILE A 1 265 ? 182.155 118.644 143.094 1.00 154.45 ? 281 ILE A CG2 1 
ATOM   1202  C  CD1 . ILE A 1 265 ? 180.822 121.106 144.262 1.00 154.45 ? 281 ILE A CD1 1 
ATOM   1203  N  N   . SER A 1 266 ? 185.234 120.970 143.224 1.00 150.12 ? 282 SER A N   1 
ATOM   1204  C  CA  . SER A 1 266 ? 186.357 120.912 144.141 1.00 150.12 ? 282 SER A CA  1 
ATOM   1205  C  C   . SER A 1 266 ? 186.007 121.704 145.391 1.00 150.12 ? 282 SER A C   1 
ATOM   1206  O  O   . SER A 1 266 ? 185.160 122.601 145.367 1.00 150.12 ? 282 SER A O   1 
ATOM   1207  C  CB  . SER A 1 266 ? 187.642 121.456 143.501 1.00 150.12 ? 282 SER A CB  1 
ATOM   1208  O  OG  . SER A 1 266 ? 187.869 120.864 142.234 1.00 150.12 ? 282 SER A OG  1 
ATOM   1209  N  N   . VAL A 1 267 ? 186.696 121.390 146.477 1.00 142.41 ? 283 VAL A N   1 
ATOM   1210  C  CA  . VAL A 1 267 ? 186.483 122.054 147.760 1.00 142.41 ? 283 VAL A CA  1 
ATOM   1211  C  C   . VAL A 1 267 ? 187.832 122.625 148.178 1.00 142.41 ? 283 VAL A C   1 
ATOM   1212  O  O   . VAL A 1 267 ? 188.650 121.958 148.817 1.00 142.41 ? 283 VAL A O   1 
ATOM   1213  C  CB  . VAL A 1 267 ? 185.924 121.104 148.821 1.00 142.41 ? 283 VAL A CB  1 
ATOM   1214  C  CG1 . VAL A 1 267 ? 185.621 121.858 150.101 1.00 142.41 ? 283 VAL A CG1 1 
ATOM   1215  C  CG2 . VAL A 1 267 ? 184.677 120.403 148.303 1.00 142.41 ? 283 VAL A CG2 1 
ATOM   1216  N  N   . SER A 1 268 ? 188.068 123.881 147.807 1.00 138.65 ? 284 SER A N   1 
ATOM   1217  C  CA  . SER A 1 268 ? 189.263 124.628 148.186 1.00 138.65 ? 284 SER A CA  1 
ATOM   1218  C  C   . SER A 1 268 ? 188.803 125.873 148.935 1.00 138.65 ? 284 SER A C   1 
ATOM   1219  O  O   . SER A 1 268 ? 188.370 126.852 148.319 1.00 138.65 ? 284 SER A O   1 
ATOM   1220  C  CB  . SER A 1 268 ? 190.097 124.989 146.961 1.00 138.65 ? 284 SER A CB  1 
ATOM   1221  O  OG  . SER A 1 268 ? 189.363 125.818 146.077 1.00 138.65 ? 284 SER A OG  1 
ATOM   1222  N  N   . GLY A 1 269 ? 188.888 125.834 150.260 1.00 130.65 ? 285 GLY A N   1 
ATOM   1223  C  CA  . GLY A 1 269 ? 188.435 126.940 151.078 1.00 130.65 ? 285 GLY A CA  1 
ATOM   1224  C  C   . GLY A 1 269 ? 187.365 126.540 152.070 1.00 130.65 ? 285 GLY A C   1 
ATOM   1225  O  O   . GLY A 1 269 ? 186.447 125.785 151.734 1.00 130.65 ? 285 GLY A O   1 
ATOM   1226  N  N   . GLN A 1 270 ? 187.470 127.045 153.296 1.00 127.34 ? 286 GLN A N   1 
ATOM   1227  C  CA  . GLN A 1 270 ? 186.514 126.718 154.343 1.00 127.34 ? 286 GLN A CA  1 
ATOM   1228  C  C   . GLN A 1 270 ? 186.671 127.719 155.477 1.00 127.34 ? 286 GLN A C   1 
ATOM   1229  O  O   . GLN A 1 270 ? 187.793 128.081 155.839 1.00 127.34 ? 286 GLN A O   1 
ATOM   1230  C  CB  . GLN A 1 270 ? 186.713 125.288 154.858 1.00 127.34 ? 286 GLN A CB  1 
ATOM   1231  C  CG  . GLN A 1 270 ? 185.705 124.863 155.908 1.00 127.34 ? 286 GLN A CG  1 
ATOM   1232  C  CD  . GLN A 1 270 ? 185.950 123.458 156.415 1.00 127.34 ? 286 GLN A CD  1 
ATOM   1233  O  OE1 . GLN A 1 270 ? 186.754 122.714 155.852 1.00 127.34 ? 286 GLN A OE1 1 
ATOM   1234  N  NE2 . GLN A 1 270 ? 185.257 123.085 157.483 1.00 127.34 ? 286 GLN A NE2 1 
ATOM   1235  N  N   . ASN A 1 271 ? 185.543 128.160 156.031 1.00 115.79 ? 287 ASN A N   1 
ATOM   1236  C  CA  . ASN A 1 271 ? 185.560 129.134 157.114 1.00 115.79 ? 287 ASN A CA  1 
ATOM   1237  C  C   . ASN A 1 271 ? 184.250 129.032 157.877 1.00 115.79 ? 287 ASN A C   1 
ATOM   1238  O  O   . ASN A 1 271 ? 183.177 129.010 157.266 1.00 115.79 ? 287 ASN A O   1 
ATOM   1239  C  CB  . ASN A 1 271 ? 185.761 130.555 156.578 1.00 115.79 ? 287 ASN A CB  1 
ATOM   1240  N  N   . SER A 1 272 ? 184.339 128.968 159.199 1.00 120.51 ? 288 SER A N   1 
ATOM   1241  C  CA  . SER A 1 272 ? 183.155 128.861 160.033 1.00 120.51 ? 288 SER A CA  1 
ATOM   1242  C  C   . SER A 1 272 ? 182.662 130.242 160.447 1.00 120.51 ? 288 SER A C   1 
ATOM   1243  O  O   . SER A 1 272 ? 183.405 131.226 160.442 1.00 120.51 ? 288 SER A O   1 
ATOM   1244  C  CB  . SER A 1 272 ? 183.442 128.014 161.274 1.00 120.51 ? 288 SER A CB  1 
ATOM   1245  O  OG  . SER A 1 272 ? 182.367 128.079 162.195 1.00 120.51 ? 288 SER A OG  1 
ATOM   1246  N  N   . LEU A 1 273 ? 181.383 130.302 160.807 1.00 127.18 ? 289 LEU A N   1 
ATOM   1247  C  CA  . LEU A 1 273 ? 180.760 131.523 161.291 1.00 127.18 ? 289 LEU A CA  1 
ATOM   1248  C  C   . LEU A 1 273 ? 180.094 131.245 162.629 1.00 127.18 ? 289 LEU A C   1 
ATOM   1249  O  O   . LEU A 1 273 ? 179.548 130.159 162.847 1.00 127.18 ? 289 LEU A O   1 
ATOM   1250  C  CB  . LEU A 1 273 ? 179.728 132.075 160.291 1.00 127.18 ? 289 LEU A CB  1 
ATOM   1251  C  CG  . LEU A 1 273 ? 180.111 132.165 158.808 1.00 127.18 ? 289 LEU A CG  1 
ATOM   1252  C  CD1 . LEU A 1 273 ? 179.872 130.853 158.072 1.00 127.18 ? 289 LEU A CD1 1 
ATOM   1253  C  CD2 . LEU A 1 273 ? 179.360 133.302 158.131 1.00 127.18 ? 289 LEU A CD2 1 
ATOM   1254  N  N   . CYS A 1 274 ? 180.142 132.229 163.521 1.00 130.10 ? 290 CYS A N   1 
ATOM   1255  C  CA  . CYS A 1 274 ? 179.457 132.156 164.803 1.00 130.10 ? 290 CYS A CA  1 
ATOM   1256  C  C   . CYS A 1 274 ? 178.082 132.807 164.765 1.00 130.10 ? 290 CYS A C   1 
ATOM   1257  O  O   . CYS A 1 274 ? 177.426 132.903 165.807 1.00 130.10 ? 290 CYS A O   1 
ATOM   1258  C  CB  . CYS A 1 274 ? 180.312 132.805 165.895 1.00 130.10 ? 290 CYS A CB  1 
ATOM   1259  N  N   . HIS A 1 275 ? 177.638 133.255 163.596 1.00 122.28 ? 291 HIS A N   1 
ATOM   1260  C  CA  . HIS A 1 275 ? 176.416 134.029 163.460 1.00 122.28 ? 291 HIS A CA  1 
ATOM   1261  C  C   . HIS A 1 275 ? 175.406 133.293 162.590 1.00 122.28 ? 291 HIS A C   1 
ATOM   1262  O  O   . HIS A 1 275 ? 175.771 132.522 161.698 1.00 122.28 ? 291 HIS A O   1 
ATOM   1263  C  CB  . HIS A 1 275 ? 176.708 135.402 162.852 1.00 122.28 ? 291 HIS A CB  1 
ATOM   1264  C  CG  . HIS A 1 275 ? 178.072 135.928 163.177 1.00 122.28 ? 291 HIS A CG  1 
ATOM   1265  N  ND1 . HIS A 1 275 ? 179.121 135.871 162.285 1.00 122.28 ? 291 HIS A ND1 1 
ATOM   1266  C  CD2 . HIS A 1 275 ? 178.560 136.515 164.295 1.00 122.28 ? 291 HIS A CD2 1 
ATOM   1267  C  CE1 . HIS A 1 275 ? 180.195 136.404 162.838 1.00 122.28 ? 291 HIS A CE1 1 
ATOM   1268  N  NE2 . HIS A 1 275 ? 179.882 136.802 164.057 1.00 122.28 ? 291 HIS A NE2 1 
ATOM   1269  N  N   . GLN A 1 276 ? 174.128 133.544 162.862 1.00 124.48 ? 292 GLN A N   1 
ATOM   1270  C  CA  . GLN A 1 276 ? 173.056 133.076 161.997 1.00 124.48 ? 292 GLN A CA  1 
ATOM   1271  C  C   . GLN A 1 276 ? 172.976 133.965 160.764 1.00 124.48 ? 292 GLN A C   1 
ATOM   1272  O  O   . GLN A 1 276 ? 173.117 135.188 160.853 1.00 124.48 ? 292 GLN A O   1 
ATOM   1273  C  CB  . GLN A 1 276 ? 171.720 133.077 162.741 1.00 124.48 ? 292 GLN A CB  1 
ATOM   1274  C  CG  . GLN A 1 276 ? 171.830 132.723 164.216 1.00 124.48 ? 292 GLN A CG  1 
ATOM   1275  C  CD  . GLN A 1 276 ? 170.502 132.302 164.820 1.00 124.48 ? 292 GLN A CD  1 
ATOM   1276  O  OE1 . GLN A 1 276 ? 169.902 133.035 165.606 1.00 124.48 ? 292 GLN A OE1 1 
ATOM   1277  N  NE2 . GLN A 1 276 ? 170.034 131.116 164.449 1.00 124.48 ? 292 GLN A NE2 1 
ATOM   1278  N  N   . ILE A 1 277 ? 172.752 133.348 159.609 1.00 101.75 ? 293 ILE A N   1 
ATOM   1279  C  CA  . ILE A 1 277 ? 172.769 134.047 158.331 1.00 101.75 ? 293 ILE A CA  1 
ATOM   1280  C  C   . ILE A 1 277 ? 171.333 134.185 157.852 1.00 101.75 ? 293 ILE A C   1 
ATOM   1281  O  O   . ILE A 1 277 ? 170.689 133.193 157.488 1.00 101.75 ? 293 ILE A O   1 
ATOM   1282  C  CB  . ILE A 1 277 ? 173.626 133.311 157.294 1.00 101.75 ? 293 ILE A CB  1 
ATOM   1283  C  CG1 . ILE A 1 277 ? 175.062 133.158 157.797 1.00 101.75 ? 293 ILE A CG1 1 
ATOM   1284  C  CG2 . ILE A 1 277 ? 173.595 134.038 155.962 1.00 101.75 ? 293 ILE A CG2 1 
ATOM   1285  C  CD1 . ILE A 1 277 ? 175.669 134.442 158.308 1.00 101.75 ? 293 ILE A CD1 1 
ATOM   1286  N  N   . THR A 1 278 ? 170.827 135.420 157.855 1.00 97.00  ? 294 THR A N   1 
ATOM   1287  C  CA  . THR A 1 278 ? 169.516 135.688 157.278 1.00 97.00  ? 294 THR A CA  1 
ATOM   1288  C  C   . THR A 1 278 ? 169.579 135.732 155.756 1.00 97.00  ? 294 THR A C   1 
ATOM   1289  O  O   . THR A 1 278 ? 168.667 135.244 155.080 1.00 97.00  ? 294 THR A O   1 
ATOM   1290  C  CB  . THR A 1 278 ? 168.962 137.002 157.835 1.00 97.00  ? 294 THR A CB  1 
ATOM   1291  O  OG1 . THR A 1 278 ? 168.570 136.817 159.201 1.00 97.00  ? 294 THR A OG1 1 
ATOM   1292  C  CG2 . THR A 1 278 ? 167.755 137.469 157.033 1.00 97.00  ? 294 THR A CG2 1 
ATOM   1293  N  N   . ALA A 1 279 ? 170.656 136.284 155.200 1.00 90.67  ? 295 ALA A N   1 
ATOM   1294  C  CA  . ALA A 1 279 ? 170.805 136.360 153.754 1.00 90.67  ? 295 ALA A CA  1 
ATOM   1295  C  C   . ALA A 1 279 ? 172.284 136.419 153.404 1.00 90.67  ? 295 ALA A C   1 
ATOM   1296  O  O   . ALA A 1 279 ? 173.128 136.748 154.240 1.00 90.67  ? 295 ALA A O   1 
ATOM   1297  C  CB  . ALA A 1 279 ? 170.059 137.563 153.166 1.00 90.67  ? 295 ALA A CB  1 
ATOM   1298  N  N   . ALA A 1 280 ? 172.591 136.096 152.150 1.00 104.61 ? 296 ALA A N   1 
ATOM   1299  C  CA  . ALA A 1 280 ? 173.965 136.111 151.675 1.00 104.61 ? 296 ALA A CA  1 
ATOM   1300  C  C   . ALA A 1 280 ? 173.978 136.474 150.198 1.00 104.61 ? 296 ALA A C   1 
ATOM   1301  O  O   . ALA A 1 280 ? 172.997 136.257 149.482 1.00 104.61 ? 296 ALA A O   1 
ATOM   1302  C  CB  . ALA A 1 280 ? 174.656 134.761 151.899 1.00 104.61 ? 296 ALA A CB  1 
ATOM   1303  N  N   . CYS A 1 281 ? 175.047 137.157 149.808 1.00 111.61 ? 297 CYS A N   1 
ATOM   1304  C  CA  . CYS A 1 281 ? 175.159 137.576 148.399 1.00 111.61 ? 297 CYS A CA  1 
ATOM   1305  C  C   . CYS A 1 281 ? 176.617 137.562 147.989 1.00 111.61 ? 297 CYS A C   1 
ATOM   1306  O  O   . CYS A 1 281 ? 177.276 138.566 148.187 1.00 111.61 ? 297 CYS A O   1 
ATOM   1307  C  CB  . CYS A 1 281 ? 174.653 138.994 148.199 1.00 111.61 ? 297 CYS A CB  1 
ATOM   1308  S  SG  . CYS A 1 281 ? 174.114 139.314 146.499 1.00 111.61 ? 297 CYS A SG  1 
ATOM   1309  N  N   . LYS A 1 282 ? 177.078 136.458 147.432 1.00 102.95 ? 298 LYS A N   1 
ATOM   1310  C  CA  . LYS A 1 282 ? 178.463 136.452 146.939 1.00 102.95 ? 298 LYS A CA  1 
ATOM   1311  C  C   . LYS A 1 282 ? 178.568 137.551 145.877 1.00 102.95 ? 298 LYS A C   1 
ATOM   1312  O  O   . LYS A 1 282 ? 177.928 137.405 144.828 1.00 102.95 ? 298 LYS A O   1 
ATOM   1313  C  CB  . LYS A 1 282 ? 178.801 135.081 146.366 1.00 102.95 ? 298 LYS A CB  1 
ATOM   1314  C  CG  . LYS A 1 282 ? 180.229 134.927 145.889 1.00 102.95 ? 298 LYS A CG  1 
ATOM   1315  C  CD  . LYS A 1 282 ? 180.499 133.569 145.341 1.00 102.95 ? 298 LYS A CD  1 
ATOM   1316  C  CE  . LYS A 1 282 ? 179.729 133.395 144.063 1.00 102.95 ? 298 LYS A CE  1 
ATOM   1317  N  NZ  . LYS A 1 282 ? 180.237 134.339 143.045 1.00 102.95 ? 298 LYS A NZ  1 
ATOM   1318  N  N   . HIS A 1 283 ? 179.336 138.608 146.163 1.00 30.00  ? 299 HIS A N   1 
ATOM   1319  C  CA  . HIS A 1 283 ? 179.515 139.784 145.282 1.00 30.00  ? 299 HIS A CA  1 
ATOM   1320  C  C   . HIS A 1 283 ? 180.911 139.814 144.664 1.00 30.00  ? 299 HIS A C   1 
ATOM   1321  O  O   . HIS A 1 283 ? 181.886 139.818 145.400 1.00 30.00  ? 299 HIS A O   1 
ATOM   1322  C  CB  . HIS A 1 283 ? 179.258 141.076 146.058 1.00 30.00  ? 299 HIS A CB  1 
ATOM   1323  N  N   . GLY A 1 284 ? 180.987 139.765 143.337 1.00 100.41 ? 300 GLY A N   1 
ATOM   1324  C  CA  . GLY A 1 284 ? 182.265 139.898 142.609 1.00 100.41 ? 300 GLY A CA  1 
ATOM   1325  C  C   . GLY A 1 284 ? 183.364 138.990 143.130 1.00 100.41 ? 300 GLY A C   1 
ATOM   1326  O  O   . GLY A 1 284 ? 184.496 139.469 143.281 1.00 100.41 ? 300 GLY A O   1 
ATOM   1327  N  N   . GLY A 1 285 ? 183.058 137.732 143.430 1.00 113.18 ? 301 GLY A N   1 
ATOM   1328  C  CA  . GLY A 1 285 ? 184.090 136.826 143.957 1.00 113.18 ? 301 GLY A CA  1 
ATOM   1329  C  C   . GLY A 1 285 ? 184.294 136.972 145.455 1.00 113.18 ? 301 GLY A C   1 
ATOM   1330  O  O   . GLY A 1 285 ? 185.217 136.322 145.979 1.00 113.18 ? 301 GLY A O   1 
ATOM   1331  N  N   . ASP A 1 286 ? 183.489 137.793 146.131 1.00 112.88 ? 302 ASP A N   1 
ATOM   1332  C  CA  . ASP A 1 286 ? 183.618 137.931 147.604 1.00 112.88 ? 302 ASP A CA  1 
ATOM   1333  C  C   . ASP A 1 286 ? 182.265 137.591 148.222 1.00 112.88 ? 302 ASP A C   1 
ATOM   1334  O  O   . ASP A 1 286 ? 181.293 137.792 147.571 1.00 112.88 ? 302 ASP A O   1 
ATOM   1335  C  CB  . ASP A 1 286 ? 184.108 139.322 147.996 1.00 112.88 ? 302 ASP A CB  1 
ATOM   1336  N  N   . LEU A 1 287 ? 182.238 137.088 149.442 1.00 110.62 ? 303 LEU A N   1 
ATOM   1337  C  CA  . LEU A 1 287 ? 181.046 136.672 150.172 1.00 110.62 ? 303 LEU A CA  1 
ATOM   1338  C  C   . LEU A 1 287 ? 180.619 137.757 151.151 1.00 110.62 ? 303 LEU A C   1 
ATOM   1339  O  O   . LEU A 1 287 ? 181.410 138.177 152.003 1.00 110.62 ? 303 LEU A O   1 
ATOM   1340  C  CB  . LEU A 1 287 ? 181.295 135.359 150.911 1.00 110.62 ? 303 LEU A CB  1 
ATOM   1341  C  CG  . LEU A 1 287 ? 180.044 134.554 151.264 1.00 110.62 ? 303 LEU A CG  1 
ATOM   1342  C  CD1 . LEU A 1 287 ? 179.324 134.109 150.008 1.00 110.62 ? 303 LEU A CD1 1 
ATOM   1343  C  CD2 . LEU A 1 287 ? 180.409 133.359 152.129 1.00 110.62 ? 303 LEU A CD2 1 
ATOM   1344  N  N   . TYR A 1 288 ? 179.373 138.209 151.022 1.00 107.85 ? 304 TYR A N   1 
ATOM   1345  C  CA  . TYR A 1 288 ? 178.740 139.116 151.968 1.00 107.85 ? 304 TYR A CA  1 
ATOM   1346  C  C   . TYR A 1 288 ? 177.611 138.360 152.654 1.00 107.85 ? 304 TYR A C   1 
ATOM   1347  O  O   . TYR A 1 288 ? 176.808 137.705 151.983 1.00 107.85 ? 304 TYR A O   1 
ATOM   1348  C  CB  . TYR A 1 288 ? 178.195 140.357 151.259 1.00 107.85 ? 304 TYR A CB  1 
ATOM   1349  C  CG  . TYR A 1 288 ? 179.263 141.284 150.723 1.00 107.85 ? 304 TYR A CG  1 
ATOM   1350  C  CD1 . TYR A 1 288 ? 179.779 142.306 151.505 1.00 107.85 ? 304 TYR A CD1 1 
ATOM   1351  C  CD2 . TYR A 1 288 ? 179.743 141.145 149.429 1.00 107.85 ? 304 TYR A CD2 1 
ATOM   1352  C  CE1 . TYR A 1 288 ? 180.748 143.159 151.018 1.00 107.85 ? 304 TYR A CE1 1 
ATOM   1353  C  CE2 . TYR A 1 288 ? 180.714 141.992 148.932 1.00 107.85 ? 304 TYR A CE2 1 
ATOM   1354  C  CZ  . TYR A 1 288 ? 181.212 142.997 149.731 1.00 107.85 ? 304 TYR A CZ  1 
ATOM   1355  O  OH  . TYR A 1 288 ? 182.179 143.844 149.242 1.00 107.85 ? 304 TYR A OH  1 
ATOM   1356  N  N   . VAL A 1 289 ? 177.548 138.438 153.982 1.00 100.06 ? 305 VAL A N   1 
ATOM   1357  C  CA  . VAL A 1 289 ? 176.523 137.738 154.752 1.00 100.06 ? 305 VAL A CA  1 
ATOM   1358  C  C   . VAL A 1 289 ? 175.884 138.713 155.735 1.00 100.06 ? 305 VAL A C   1 
ATOM   1359  O  O   . VAL A 1 289 ? 176.582 139.447 156.439 1.00 100.06 ? 305 VAL A O   1 
ATOM   1360  C  CB  . VAL A 1 289 ? 177.085 136.488 155.470 1.00 100.06 ? 305 VAL A CB  1 
ATOM   1361  C  CG1 . VAL A 1 289 ? 177.992 135.695 154.541 1.00 100.06 ? 305 VAL A CG1 1 
ATOM   1362  C  CG2 . VAL A 1 289 ? 177.857 136.849 156.730 1.00 100.06 ? 305 VAL A CG2 1 
ATOM   1363  N  N   . VAL A 1 290 ? 174.554 138.768 155.733 1.00 94.89  ? 306 VAL A N   1 
ATOM   1364  C  CA  . VAL A 1 290 ? 173.798 139.636 156.626 1.00 94.89  ? 306 VAL A CA  1 
ATOM   1365  C  C   . VAL A 1 290 ? 172.941 138.778 157.548 1.00 94.89  ? 306 VAL A C   1 
ATOM   1366  O  O   . VAL A 1 290 ? 172.296 137.819 157.103 1.00 94.89  ? 306 VAL A O   1 
ATOM   1367  C  CB  . VAL A 1 290 ? 172.944 140.656 155.849 1.00 94.89  ? 306 VAL A CB  1 
ATOM   1368  C  CG1 . VAL A 1 290 ? 171.914 139.964 154.984 1.00 94.89  ? 306 VAL A CG1 1 
ATOM   1369  C  CG2 . VAL A 1 290 ? 172.259 141.597 156.817 1.00 94.89  ? 306 VAL A CG2 1 
ATOM   1370  N  N   . GLY A 1 291 ? 172.966 139.110 158.837 1.00 97.01  ? 307 GLY A N   1 
ATOM   1371  C  CA  . GLY A 1 291 ? 172.220 138.389 159.843 1.00 97.01  ? 307 GLY A CA  1 
ATOM   1372  C  C   . GLY A 1 291 ? 172.487 138.850 161.263 1.00 97.01  ? 307 GLY A C   1 
ATOM   1373  O  O   . GLY A 1 291 ? 172.556 140.056 161.555 1.00 97.01  ? 307 GLY A O   1 
ATOM   1374  N  N   . GLY A 1 292 ? 172.709 137.864 162.133 1.00 110.08 ? 308 GLY A N   1 
ATOM   1375  C  CA  . GLY A 1 292 ? 172.859 138.029 163.566 1.00 110.08 ? 308 GLY A CA  1 
ATOM   1376  C  C   . GLY A 1 292 ? 171.603 137.622 164.311 1.00 110.08 ? 308 GLY A C   1 
ATOM   1377  O  O   . GLY A 1 292 ? 170.860 136.757 163.838 1.00 110.08 ? 308 GLY A O   1 
ATOM   1378  N  N   . SER A 1 293 ? 171.352 138.221 165.472 1.00 120.98 ? 309 SER A N   1 
ATOM   1379  C  CA  . SER A 1 293 ? 170.160 137.889 166.240 1.00 120.98 ? 309 SER A CA  1 
ATOM   1380  C  C   . SER A 1 293 ? 168.908 138.301 165.474 1.00 120.98 ? 309 SER A C   1 
ATOM   1381  O  O   . SER A 1 293 ? 168.926 139.244 164.680 1.00 120.98 ? 309 SER A O   1 
ATOM   1382  C  CB  . SER A 1 293 ? 170.195 138.574 167.606 1.00 120.98 ? 309 SER A CB  1 
ATOM   1383  O  OG  . SER A 1 293 ? 170.076 139.979 167.473 1.00 120.98 ? 309 SER A OG  1 
ATOM   1384  N  N   . ILE A 1 294 ? 167.812 137.584 165.709 1.00 118.70 ? 310 ILE A N   1 
ATOM   1385  C  CA  . ILE A 1 294 ? 166.615 137.811 164.898 1.00 118.70 ? 310 ILE A CA  1 
ATOM   1386  C  C   . ILE A 1 294 ? 165.928 139.148 165.201 1.00 118.70 ? 310 ILE A C   1 
ATOM   1387  O  O   . ILE A 1 294 ? 165.284 139.686 164.289 1.00 118.70 ? 310 ILE A O   1 
ATOM   1388  C  CB  . ILE A 1 294 ? 165.661 136.591 164.948 1.00 118.70 ? 310 ILE A CB  1 
ATOM   1389  C  CG1 . ILE A 1 294 ? 165.168 136.131 166.340 1.00 118.70 ? 310 ILE A CG1 1 
ATOM   1390  C  CG2 . ILE A 1 294 ? 166.298 135.401 164.235 1.00 118.70 ? 310 ILE A CG2 1 
ATOM   1391  C  CD1 . ILE A 1 294 ? 164.438 137.111 167.215 1.00 118.70 ? 310 ILE A CD1 1 
ATOM   1392  N  N   . PRO A 1 295 ? 166.005 139.749 166.405 1.00 118.02 ? 311 PRO A N   1 
ATOM   1393  C  CA  . PRO A 1 295 ? 165.347 141.054 166.570 1.00 118.02 ? 311 PRO A CA  1 
ATOM   1394  C  C   . PRO A 1 295 ? 166.157 142.182 165.964 1.00 118.02 ? 311 PRO A C   1 
ATOM   1395  O  O   . PRO A 1 295 ? 165.587 143.224 165.614 1.00 118.02 ? 311 PRO A O   1 
ATOM   1396  C  CB  . PRO A 1 295 ? 165.235 141.206 168.090 1.00 118.02 ? 311 PRO A CB  1 
ATOM   1397  C  CG  . PRO A 1 295 ? 166.430 140.539 168.587 1.00 118.02 ? 311 PRO A CG  1 
ATOM   1398  C  CD  . PRO A 1 295 ? 166.723 139.394 167.650 1.00 118.02 ? 311 PRO A CD  1 
ATOM   1399  N  N   . ARG A 1 296 ? 167.469 141.993 165.837 1.00 103.00 ? 312 ARG A N   1 
ATOM   1400  C  CA  . ARG A 1 296 ? 168.383 142.944 165.207 1.00 103.00 ? 312 ARG A CA  1 
ATOM   1401  C  C   . ARG A 1 296 ? 169.221 142.196 164.178 1.00 103.00 ? 312 ARG A C   1 
ATOM   1402  O  O   . ARG A 1 296 ? 170.425 141.988 164.372 1.00 103.00 ? 312 ARG A O   1 
ATOM   1403  C  CB  . ARG A 1 296 ? 169.270 143.616 166.254 1.00 103.00 ? 312 ARG A CB  1 
ATOM   1404  C  CG  . ARG A 1 296 ? 168.646 144.827 166.909 1.00 103.00 ? 312 ARG A CG  1 
ATOM   1405  C  CD  . ARG A 1 296 ? 169.615 145.498 167.864 1.00 103.00 ? 312 ARG A CD  1 
ATOM   1406  N  NE  . ARG A 1 296 ? 169.147 145.449 169.242 1.00 103.00 ? 312 ARG A NE  1 
ATOM   1407  C  CZ  . ARG A 1 296 ? 169.677 146.150 170.235 1.00 103.00 ? 312 ARG A CZ  1 
ATOM   1408  N  NH1 . ARG A 1 296 ? 170.698 146.966 170.035 1.00 103.00 ? 312 ARG A NH1 1 
ATOM   1409  N  NH2 . ARG A 1 296 ? 169.164 146.035 171.456 1.00 103.00 ? 312 ARG A NH2 1 
ATOM   1410  N  N   . PRO A 1 297 ? 168.609 141.765 163.058 1.00 105.02 ? 313 PRO A N   1 
ATOM   1411  C  CA  . PRO A 1 297 ? 169.344 141.045 162.012 1.00 105.02 ? 313 PRO A CA  1 
ATOM   1412  C  C   . PRO A 1 297 ? 169.983 141.978 160.988 1.00 105.02 ? 313 PRO A C   1 
ATOM   1413  O  O   . PRO A 1 297 ? 169.764 141.853 159.777 1.00 105.02 ? 313 PRO A O   1 
ATOM   1414  C  CB  . PRO A 1 297 ? 168.257 140.173 161.380 1.00 105.02 ? 313 PRO A CB  1 
ATOM   1415  C  CG  . PRO A 1 297 ? 167.035 141.027 161.478 1.00 105.02 ? 313 PRO A CG  1 
ATOM   1416  C  CD  . PRO A 1 297 ? 167.173 141.860 162.736 1.00 105.02 ? 313 PRO A CD  1 
ATOM   1417  N  N   . ARG A 1 298 ? 170.780 142.929 161.472 1.00 102.11 ? 314 ARG A N   1 
ATOM   1418  C  CA  . ARG A 1 298 ? 171.441 143.899 160.617 1.00 102.11 ? 314 ARG A CA  1 
ATOM   1419  C  C   . ARG A 1 298 ? 172.925 143.651 160.439 1.00 102.11 ? 314 ARG A C   1 
ATOM   1420  O  O   . ARG A 1 298 ? 173.504 144.179 159.484 1.00 102.11 ? 314 ARG A O   1 
ATOM   1421  C  CB  . ARG A 1 298 ? 171.301 145.319 161.178 1.00 102.11 ? 314 ARG A CB  1 
ATOM   1422  C  CG  . ARG A 1 298 ? 170.902 145.386 162.627 1.00 102.11 ? 314 ARG A CG  1 
ATOM   1423  C  CD  . ARG A 1 298 ? 170.093 146.626 162.870 1.00 102.11 ? 314 ARG A CD  1 
ATOM   1424  N  NE  . ARG A 1 298 ? 169.816 146.832 164.283 1.00 102.11 ? 314 ARG A NE  1 
ATOM   1425  C  CZ  . ARG A 1 298 ? 169.627 148.024 164.824 1.00 102.11 ? 314 ARG A CZ  1 
ATOM   1426  N  NH1 . ARG A 1 298 ? 169.685 149.125 164.098 1.00 102.11 ? 314 ARG A NH1 1 
ATOM   1427  N  NH2 . ARG A 1 298 ? 169.359 148.114 166.122 1.00 102.11 ? 314 ARG A NH2 1 
ATOM   1428  N  N   . ARG A 1 299 ? 173.559 142.900 161.342 1.00 101.30 ? 315 ARG A N   1 
ATOM   1429  C  CA  . ARG A 1 299 ? 175.004 142.739 161.256 1.00 101.30 ? 315 ARG A CA  1 
ATOM   1430  C  C   . ARG A 1 299 ? 175.397 142.193 159.893 1.00 101.30 ? 315 ARG A C   1 
ATOM   1431  O  O   . ARG A 1 299 ? 174.787 141.251 159.384 1.00 101.30 ? 315 ARG A O   1 
ATOM   1432  C  CB  . ARG A 1 299 ? 175.474 141.805 162.369 1.00 101.30 ? 315 ARG A CB  1 
ATOM   1433  C  CG  . ARG A 1 299 ? 175.674 142.475 163.718 1.00 101.30 ? 315 ARG A CG  1 
ATOM   1434  C  CD  . ARG A 1 299 ? 177.112 142.920 163.896 1.00 101.30 ? 315 ARG A CD  1 
ATOM   1435  N  NE  . ARG A 1 299 ? 177.903 141.879 164.544 1.00 101.30 ? 315 ARG A NE  1 
ATOM   1436  C  CZ  . ARG A 1 299 ? 179.223 141.900 164.661 1.00 101.30 ? 315 ARG A CZ  1 
ATOM   1437  N  NH1 . ARG A 1 299 ? 179.947 142.874 164.136 1.00 101.30 ? 315 ARG A NH1 1 
ATOM   1438  N  NH2 . ARG A 1 299 ? 179.833 140.913 165.309 1.00 101.30 ? 315 ARG A NH2 1 
ATOM   1439  N  N   . MET A 1 300 ? 176.424 142.786 159.293 1.00 110.15 ? 316 MET A N   1 
ATOM   1440  C  CA  . MET A 1 300 ? 176.871 142.332 157.988 1.00 110.15 ? 316 MET A CA  1 
ATOM   1441  C  C   . MET A 1 300 ? 178.371 142.075 158.041 1.00 110.15 ? 316 MET A C   1 
ATOM   1442  O  O   . MET A 1 300 ? 179.141 142.896 158.558 1.00 110.15 ? 316 MET A O   1 
ATOM   1443  C  CB  . MET A 1 300 ? 176.470 143.340 156.898 1.00 110.15 ? 316 MET A CB  1 
ATOM   1444  C  CG  . MET A 1 300 ? 176.132 142.682 155.561 1.00 110.15 ? 316 MET A CG  1 
ATOM   1445  S  SD  . MET A 1 300 ? 176.045 143.788 154.143 1.00 110.15 ? 316 MET A SD  1 
ATOM   1446  C  CE  . MET A 1 300 ? 177.762 143.914 153.694 1.00 110.15 ? 316 MET A CE  1 
ATOM   1447  N  N   . TRP A 1 301 ? 178.785 140.985 157.401 1.00 101.18 ? 317 TRP A N   1 
ATOM   1448  C  CA  . TRP A 1 301 ? 180.169 140.547 157.400 1.00 101.18 ? 317 TRP A CA  1 
ATOM   1449  C  C   . TRP A 1 301 ? 180.641 140.214 155.995 1.00 101.18 ? 317 TRP A C   1 
ATOM   1450  O  O   . TRP A 1 301 ? 179.869 139.796 155.126 1.00 101.18 ? 317 TRP A O   1 
ATOM   1451  C  CB  . TRP A 1 301 ? 180.385 139.314 158.287 1.00 101.18 ? 317 TRP A CB  1 
ATOM   1452  C  CG  . TRP A 1 301 ? 180.017 139.501 159.719 1.00 101.18 ? 317 TRP A CG  1 
ATOM   1453  C  CD1 . TRP A 1 301 ? 180.806 140.003 160.711 1.00 101.18 ? 317 TRP A CD1 1 
ATOM   1454  C  CD2 . TRP A 1 301 ? 178.775 139.147 160.334 1.00 101.18 ? 317 TRP A CD2 1 
ATOM   1455  N  NE1 . TRP A 1 301 ? 180.125 140.003 161.903 1.00 101.18 ? 317 TRP A NE1 1 
ATOM   1456  C  CE2 . TRP A 1 301 ? 178.875 139.480 161.698 1.00 101.18 ? 317 TRP A CE2 1 
ATOM   1457  C  CE3 . TRP A 1 301 ? 177.585 138.589 159.860 1.00 101.18 ? 317 TRP A CE3 1 
ATOM   1458  C  CZ2 . TRP A 1 301 ? 177.830 139.273 162.592 1.00 101.18 ? 317 TRP A CZ2 1 
ATOM   1459  C  CZ3 . TRP A 1 301 ? 176.550 138.385 160.749 1.00 101.18 ? 317 TRP A CZ3 1 
ATOM   1460  C  CH2 . TRP A 1 301 ? 176.679 138.725 162.099 1.00 101.18 ? 317 TRP A CH2 1 
ATOM   1461  N  N   . LYS A 1 302 ? 181.939 140.418 155.810 1.00 110.01 ? 318 LYS A N   1 
ATOM   1462  C  CA  . LYS A 1 302 ? 182.712 140.185 154.601 1.00 110.01 ? 318 LYS A CA  1 
ATOM   1463  C  C   . LYS A 1 302 ? 183.805 139.215 155.029 1.00 110.01 ? 318 LYS A C   1 
ATOM   1464  O  O   . LYS A 1 302 ? 184.876 139.621 155.500 1.00 110.01 ? 318 LYS A O   1 
ATOM   1465  C  CB  . LYS A 1 302 ? 183.273 141.518 154.081 1.00 110.01 ? 318 LYS A CB  1 
ATOM   1466  C  CG  . LYS A 1 302 ? 184.166 141.452 152.860 1.00 110.01 ? 318 LYS A CG  1 
ATOM   1467  C  CD  . LYS A 1 302 ? 183.408 140.996 151.633 1.00 110.01 ? 318 LYS A CD  1 
ATOM   1468  C  CE  . LYS A 1 302 ? 184.199 141.321 150.382 1.00 110.01 ? 318 LYS A CE  1 
ATOM   1469  N  NZ  . LYS A 1 302 ? 184.509 142.773 150.288 1.00 110.01 ? 318 LYS A NZ  1 
ATOM   1470  N  N   . CYS A 1 303 ? 183.467 137.927 155.004 1.00 116.75 ? 319 CYS A N   1 
ATOM   1471  C  CA  . CYS A 1 303 ? 184.349 136.862 155.464 1.00 116.75 ? 319 CYS A CA  1 
ATOM   1472  C  C   . CYS A 1 303 ? 184.986 136.203 154.245 1.00 116.75 ? 319 CYS A C   1 
ATOM   1473  O  O   . CYS A 1 303 ? 184.323 135.458 153.516 1.00 116.75 ? 319 CYS A O   1 
ATOM   1474  C  CB  . CYS A 1 303 ? 183.576 135.850 156.310 1.00 116.75 ? 319 CYS A CB  1 
ATOM   1475  S  SG  . CYS A 1 303 ? 182.048 135.226 155.571 1.00 116.75 ? 319 CYS A SG  1 
ATOM   1476  N  N   . ASN A 1 304 ? 186.267 136.475 154.027 1.00 134.30 ? 320 ASN A N   1 
ATOM   1477  C  CA  . ASN A 1 304 ? 186.991 135.897 152.898 1.00 134.30 ? 320 ASN A CA  1 
ATOM   1478  C  C   . ASN A 1 304 ? 188.455 135.672 153.255 1.00 134.30 ? 320 ASN A C   1 
ATOM   1479  O  O   . ASN A 1 304 ? 189.239 136.620 153.324 1.00 134.30 ? 320 ASN A O   1 
ATOM   1480  C  CB  . ASN A 1 304 ? 186.887 136.789 151.654 1.00 134.30 ? 320 ASN A CB  1 
ATOM   1481  C  CG  . ASN A 1 304 ? 185.467 136.903 151.126 1.00 134.30 ? 320 ASN A CG  1 
ATOM   1482  O  OD1 . ASN A 1 304 ? 185.095 136.227 150.167 1.00 134.30 ? 320 ASN A OD1 1 
ATOM   1483  N  ND2 . ASN A 1 304 ? 184.677 137.784 151.729 1.00 134.30 ? 320 ASN A ND2 1 
ATOM   1484  N  N   . VAL A 1 308 ? 192.098 136.251 156.661 1.00 149.86 ? 324 VAL A N   1 
ATOM   1485  C  CA  . VAL A 1 308 ? 191.339 136.617 157.849 1.00 149.86 ? 324 VAL A CA  1 
ATOM   1486  C  C   . VAL A 1 308 ? 189.926 137.039 157.464 1.00 149.86 ? 324 VAL A C   1 
ATOM   1487  O  O   . VAL A 1 308 ? 189.734 138.004 156.726 1.00 149.86 ? 324 VAL A O   1 
ATOM   1488  C  CB  . VAL A 1 308 ? 192.043 137.734 158.637 1.00 149.86 ? 324 VAL A CB  1 
ATOM   1489  N  N   . ASP A 1 309 ? 188.940 136.307 157.971 1.00 146.71 ? 325 ASP A N   1 
ATOM   1490  C  CA  . ASP A 1 309 ? 187.541 136.573 157.681 1.00 146.71 ? 325 ASP A CA  1 
ATOM   1491  C  C   . ASP A 1 309 ? 186.970 137.514 158.742 1.00 146.71 ? 325 ASP A C   1 
ATOM   1492  O  O   . ASP A 1 309 ? 187.711 138.116 159.525 1.00 146.71 ? 325 ASP A O   1 
ATOM   1493  C  CB  . ASP A 1 309 ? 186.772 135.256 157.607 1.00 146.71 ? 325 ASP A CB  1 
ATOM   1494  N  N   . TRP A 1 310 ? 185.641 137.681 158.746 1.00 131.96 ? 326 TRP A N   1 
ATOM   1495  C  CA  . TRP A 1 310 ? 184.929 138.481 159.747 1.00 131.96 ? 326 TRP A CA  1 
ATOM   1496  C  C   . TRP A 1 310 ? 185.149 139.984 159.581 1.00 131.96 ? 326 TRP A C   1 
ATOM   1497  O  O   . TRP A 1 310 ? 185.164 140.720 160.571 1.00 131.96 ? 326 TRP A O   1 
ATOM   1498  C  CB  . TRP A 1 310 ? 185.280 138.048 161.176 1.00 131.96 ? 326 TRP A CB  1 
ATOM   1499  N  N   . GLU A 1 311 ? 185.330 140.468 158.353 1.00 129.96 ? 327 GLU A N   1 
ATOM   1500  C  CA  . GLU A 1 311 ? 185.477 141.905 158.140 1.00 129.96 ? 327 GLU A CA  1 
ATOM   1501  C  C   . GLU A 1 311 ? 184.108 142.574 158.249 1.00 129.96 ? 327 GLU A C   1 
ATOM   1502  O  O   . GLU A 1 311 ? 183.197 142.256 157.487 1.00 129.96 ? 327 GLU A O   1 
ATOM   1503  C  CB  . GLU A 1 311 ? 186.115 142.177 156.779 1.00 129.96 ? 327 GLU A CB  1 
ATOM   1504  C  CG  . GLU A 1 311 ? 187.620 142.437 156.829 1.00 129.96 ? 327 GLU A CG  1 
ATOM   1505  C  CD  . GLU A 1 311 ? 188.438 141.196 157.176 1.00 129.96 ? 327 GLU A CD  1 
ATOM   1506  O  OE1 . GLU A 1 311 ? 187.847 140.128 157.441 1.00 129.96 ? 327 GLU A OE1 1 
ATOM   1507  O  OE2 . GLU A 1 311 ? 189.683 141.289 157.182 1.00 129.96 ? 327 GLU A OE2 1 
ATOM   1508  N  N   . TRP A 1 312 ? 183.958 143.510 159.181 1.00 115.74 ? 328 TRP A N   1 
ATOM   1509  C  CA  . TRP A 1 312 ? 182.644 144.088 159.432 1.00 115.74 ? 328 TRP A CA  1 
ATOM   1510  C  C   . TRP A 1 312 ? 182.290 145.128 158.374 1.00 115.74 ? 328 TRP A C   1 
ATOM   1511  O  O   . TRP A 1 312 ? 183.155 145.842 157.860 1.00 115.74 ? 328 TRP A O   1 
ATOM   1512  C  CB  . TRP A 1 312 ? 182.623 144.676 160.853 1.00 115.74 ? 328 TRP A CB  1 
ATOM   1513  C  CG  . TRP A 1 312 ? 183.253 146.059 161.059 1.00 115.74 ? 328 TRP A CG  1 
ATOM   1514  C  CD1 . TRP A 1 312 ? 184.389 146.322 161.774 1.00 115.74 ? 328 TRP A CD1 1 
ATOM   1515  C  CD2 . TRP A 1 312 ? 182.722 147.343 160.682 1.00 115.74 ? 328 TRP A CD2 1 
ATOM   1516  N  NE1 . TRP A 1 312 ? 184.641 147.670 161.795 1.00 115.74 ? 328 TRP A NE1 1 
ATOM   1517  C  CE2 . TRP A 1 312 ? 183.629 148.322 161.141 1.00 115.74 ? 328 TRP A CE2 1 
ATOM   1518  C  CE3 . TRP A 1 312 ? 181.588 147.759 159.979 1.00 115.74 ? 328 TRP A CE3 1 
ATOM   1519  C  CZ2 . TRP A 1 312 ? 183.436 149.684 160.916 1.00 115.74 ? 328 TRP A CZ2 1 
ATOM   1520  C  CZ3 . TRP A 1 312 ? 181.403 149.112 159.753 1.00 115.74 ? 328 TRP A CZ3 1 
ATOM   1521  C  CH2 . TRP A 1 312 ? 182.320 150.057 160.222 1.00 115.74 ? 328 TRP A CH2 1 
ATOM   1522  N  N   . CYS A 1 313 ? 180.994 145.207 158.045 1.00 106.92 ? 329 CYS A N   1 
ATOM   1523  C  CA  . CYS A 1 313 ? 180.515 146.163 157.053 1.00 106.92 ? 329 CYS A CA  1 
ATOM   1524  C  C   . CYS A 1 313 ? 179.375 147.002 157.618 1.00 106.92 ? 329 CYS A C   1 
ATOM   1525  O  O   . CYS A 1 313 ? 178.896 146.776 158.732 1.00 106.92 ? 329 CYS A O   1 
ATOM   1526  C  CB  . CYS A 1 313 ? 180.059 145.455 155.773 1.00 106.92 ? 329 CYS A CB  1 
ATOM   1527  S  SG  . CYS A 1 313 ? 181.394 144.752 154.783 1.00 106.92 ? 329 CYS A SG  1 
ATOM   1528  N  N   . ALA A 1 314 ? 178.949 147.988 156.827 1.00 97.73  ? 330 ALA A N   1 
ATOM   1529  C  CA  . ALA A 1 314 ? 177.932 148.925 157.285 1.00 97.73  ? 330 ALA A CA  1 
ATOM   1530  C  C   . ALA A 1 314 ? 176.615 148.195 157.527 1.00 97.73  ? 330 ALA A C   1 
ATOM   1531  O  O   . ALA A 1 314 ? 176.145 147.463 156.645 1.00 97.73  ? 330 ALA A O   1 
ATOM   1532  C  CB  . ALA A 1 314 ? 177.729 150.043 156.265 1.00 97.73  ? 330 ALA A CB  1 
ATOM   1533  N  N   . PRO A 1 315 ? 175.996 148.362 158.689 1.00 90.35  ? 331 PRO A N   1 
ATOM   1534  C  CA  . PRO A 1 315 ? 174.690 147.742 158.931 1.00 90.35  ? 331 PRO A CA  1 
ATOM   1535  C  C   . PRO A 1 315 ? 173.581 148.379 158.112 1.00 90.35  ? 331 PRO A C   1 
ATOM   1536  O  O   . PRO A 1 315 ? 173.657 149.543 157.712 1.00 90.35  ? 331 PRO A O   1 
ATOM   1537  C  CB  . PRO A 1 315 ? 174.460 147.978 160.427 1.00 90.35  ? 331 PRO A CB  1 
ATOM   1538  C  CG  . PRO A 1 315 ? 175.804 148.293 160.976 1.00 90.35  ? 331 PRO A CG  1 
ATOM   1539  C  CD  . PRO A 1 315 ? 176.541 148.994 159.898 1.00 90.35  ? 331 PRO A CD  1 
ATOM   1540  N  N   . LEU A 1 316 ? 172.540 147.596 157.865 1.00 88.77  ? 332 LEU A N   1 
ATOM   1541  C  CA  . LEU A 1 316 ? 171.341 148.111 157.225 1.00 88.77  ? 332 LEU A CA  1 
ATOM   1542  C  C   . LEU A 1 316 ? 170.473 148.849 158.244 1.00 88.77  ? 332 LEU A C   1 
ATOM   1543  O  O   . LEU A 1 316 ? 170.416 148.464 159.415 1.00 88.77  ? 332 LEU A O   1 
ATOM   1544  C  CB  . LEU A 1 316 ? 170.544 146.985 156.575 1.00 88.77  ? 332 LEU A CB  1 
ATOM   1545  C  CG  . LEU A 1 316 ? 171.270 146.171 155.501 1.00 88.77  ? 332 LEU A CG  1 
ATOM   1546  C  CD1 . LEU A 1 316 ? 172.061 145.023 156.093 1.00 88.77  ? 332 LEU A CD1 1 
ATOM   1547  C  CD2 . LEU A 1 316 ? 170.275 145.661 154.471 1.00 88.77  ? 332 LEU A CD2 1 
ATOM   1548  N  N   . PRO A 1 317 ? 169.783 149.912 157.824 1.00 89.86  ? 333 PRO A N   1 
ATOM   1549  C  CA  . PRO A 1 317 ? 168.918 150.655 158.748 1.00 89.86  ? 333 PRO A CA  1 
ATOM   1550  C  C   . PRO A 1 317 ? 167.567 150.007 159.014 1.00 89.86  ? 333 PRO A C   1 
ATOM   1551  O  O   . PRO A 1 317 ? 166.754 150.596 159.735 1.00 89.86  ? 333 PRO A O   1 
ATOM   1552  C  CB  . PRO A 1 317 ? 168.754 152.006 158.041 1.00 89.86  ? 333 PRO A CB  1 
ATOM   1553  C  CG  . PRO A 1 317 ? 168.863 151.680 156.607 1.00 89.86  ? 333 PRO A CG  1 
ATOM   1554  C  CD  . PRO A 1 317 ? 169.856 150.552 156.499 1.00 89.86  ? 333 PRO A CD  1 
ATOM   1555  N  N   . ARG A 1 318 ? 167.296 148.829 158.457 1.00 101.11 ? 334 ARG A N   1 
ATOM   1556  C  CA  . ARG A 1 318 ? 166.032 148.133 158.651 1.00 101.11 ? 334 ARG A CA  1 
ATOM   1557  C  C   . ARG A 1 318 ? 166.277 146.775 159.292 1.00 101.11 ? 334 ARG A C   1 
ATOM   1558  O  O   . ARG A 1 318 ? 167.358 146.193 159.164 1.00 101.11 ? 334 ARG A O   1 
ATOM   1559  C  CB  . ARG A 1 318 ? 165.282 147.926 157.329 1.00 101.11 ? 334 ARG A CB  1 
ATOM   1560  C  CG  . ARG A 1 318 ? 164.973 149.183 156.547 1.00 101.11 ? 334 ARG A CG  1 
ATOM   1561  C  CD  . ARG A 1 318 ? 163.638 149.790 156.921 1.00 101.11 ? 334 ARG A CD  1 
ATOM   1562  N  NE  . ARG A 1 318 ? 163.183 150.719 155.894 1.00 101.11 ? 334 ARG A NE  1 
ATOM   1563  C  CZ  . ARG A 1 318 ? 162.115 151.497 156.000 1.00 101.11 ? 334 ARG A CZ  1 
ATOM   1564  N  NH1 . ARG A 1 318 ? 161.368 151.500 157.092 1.00 101.11 ? 334 ARG A NH1 1 
ATOM   1565  N  NH2 . ARG A 1 318 ? 161.790 152.294 154.986 1.00 101.11 ? 334 ARG A NH2 1 
ATOM   1566  N  N   . ASP A 1 319 ? 165.258 146.278 159.986 1.00 97.29  ? 335 ASP A N   1 
ATOM   1567  C  CA  . ASP A 1 319 ? 165.271 144.952 160.596 1.00 97.29  ? 335 ASP A CA  1 
ATOM   1568  C  C   . ASP A 1 319 ? 164.217 144.102 159.900 1.00 97.29  ? 335 ASP A C   1 
ATOM   1569  O  O   . ASP A 1 319 ? 163.026 144.193 160.211 1.00 97.29  ? 335 ASP A O   1 
ATOM   1570  C  CB  . ASP A 1 319 ? 165.029 145.038 162.098 1.00 97.29  ? 335 ASP A CB  1 
ATOM   1571  C  CG  . ASP A 1 319 ? 166.235 145.554 162.839 1.00 97.29  ? 335 ASP A CG  1 
ATOM   1572  O  OD1 . ASP A 1 319 ? 167.336 145.492 162.260 1.00 97.29  ? 335 ASP A OD1 1 
ATOM   1573  O  OD2 . ASP A 1 319 ? 166.093 146.016 163.987 1.00 97.29  ? 335 ASP A OD2 1 
ATOM   1574  N  N   . ARG A 1 320 ? 164.659 143.273 158.958 1.00 88.11  ? 336 ARG A N   1 
ATOM   1575  C  CA  . ARG A 1 320 ? 163.760 142.447 158.172 1.00 88.11  ? 336 ARG A CA  1 
ATOM   1576  C  C   . ARG A 1 320 ? 164.343 141.049 158.048 1.00 88.11  ? 336 ARG A C   1 
ATOM   1577  O  O   . ARG A 1 320 ? 165.562 140.870 157.986 1.00 88.11  ? 336 ARG A O   1 
ATOM   1578  C  CB  . ARG A 1 320 ? 163.529 143.043 156.776 1.00 88.11  ? 336 ARG A CB  1 
ATOM   1579  C  CG  . ARG A 1 320 ? 162.977 144.459 156.785 1.00 88.11  ? 336 ARG A CG  1 
ATOM   1580  C  CD  . ARG A 1 320 ? 163.003 145.072 155.397 1.00 88.11  ? 336 ARG A CD  1 
ATOM   1581  N  NE  . ARG A 1 320 ? 164.354 145.128 154.851 1.00 88.11  ? 336 ARG A NE  1 
ATOM   1582  C  CZ  . ARG A 1 320 ? 164.648 145.515 153.618 1.00 88.11  ? 336 ARG A CZ  1 
ATOM   1583  N  NH1 . ARG A 1 320 ? 163.706 145.897 152.771 1.00 88.11  ? 336 ARG A NH1 1 
ATOM   1584  N  NH2 . ARG A 1 320 ? 165.918 145.522 153.226 1.00 88.11  ? 336 ARG A NH2 1 
ATOM   1585  N  N   . LEU A 1 321 ? 163.456 140.061 158.013 1.00 82.65  ? 337 LEU A N   1 
ATOM   1586  C  CA  . LEU A 1 321 ? 163.828 138.667 157.837 1.00 82.65  ? 337 LEU A CA  1 
ATOM   1587  C  C   . LEU A 1 321 ? 163.409 138.201 156.450 1.00 82.65  ? 337 LEU A C   1 
ATOM   1588  O  O   . LEU A 1 321 ? 162.389 138.641 155.912 1.00 82.65  ? 337 LEU A O   1 
ATOM   1589  C  CB  . LEU A 1 321 ? 163.187 137.781 158.908 1.00 82.65  ? 337 LEU A CB  1 
ATOM   1590  C  CG  . LEU A 1 321 ? 163.754 137.919 160.322 1.00 82.65  ? 337 LEU A CG  1 
ATOM   1591  C  CD1 . LEU A 1 321 ? 162.839 137.255 161.338 1.00 82.65  ? 337 LEU A CD1 1 
ATOM   1592  C  CD2 . LEU A 1 321 ? 165.155 137.332 160.396 1.00 82.65  ? 337 LEU A CD2 1 
ATOM   1593  N  N   . GLN A 1 322 ? 164.211 137.302 155.878 1.00 93.80  ? 338 GLN A N   1 
ATOM   1594  C  CA  . GLN A 1 322 ? 163.975 136.772 154.535 1.00 93.80  ? 338 GLN A CA  1 
ATOM   1595  C  C   . GLN A 1 322 ? 163.892 137.895 153.503 1.00 93.80  ? 338 GLN A C   1 
ATOM   1596  O  O   . GLN A 1 322 ? 163.103 137.838 152.558 1.00 93.80  ? 338 GLN A O   1 
ATOM   1597  C  CB  . GLN A 1 322 ? 162.717 135.901 154.492 1.00 93.80  ? 338 GLN A CB  1 
ATOM   1598  C  CG  . GLN A 1 322 ? 162.871 134.549 155.167 1.00 93.80  ? 338 GLN A CG  1 
ATOM   1599  C  CD  . GLN A 1 322 ? 161.630 134.134 155.931 1.00 93.80  ? 338 GLN A CD  1 
ATOM   1600  O  OE1 . GLN A 1 322 ? 160.525 134.133 155.390 1.00 93.80  ? 338 GLN A OE1 1 
ATOM   1601  N  NE2 . GLN A 1 322 ? 161.807 133.778 157.198 1.00 93.80  ? 338 GLN A NE2 1 
ATOM   1602  N  N   . HIS A 1 323 ? 164.713 138.927 153.685 1.00 87.58  ? 339 HIS A N   1 
ATOM   1603  C  CA  . HIS A 1 323 ? 164.789 140.011 152.716 1.00 87.58  ? 339 HIS A CA  1 
ATOM   1604  C  C   . HIS A 1 323 ? 165.710 139.603 151.574 1.00 87.58  ? 339 HIS A C   1 
ATOM   1605  O  O   . HIS A 1 323 ? 166.791 139.053 151.803 1.00 87.58  ? 339 HIS A O   1 
ATOM   1606  C  CB  . HIS A 1 323 ? 165.287 141.296 153.379 1.00 87.58  ? 339 HIS A CB  1 
ATOM   1607  C  CG  . HIS A 1 323 ? 166.687 141.207 153.900 1.00 87.58  ? 339 HIS A CG  1 
ATOM   1608  N  ND1 . HIS A 1 323 ? 167.792 141.393 153.099 1.00 87.58  ? 339 HIS A ND1 1 
ATOM   1609  C  CD2 . HIS A 1 323 ? 167.162 140.954 155.143 1.00 87.58  ? 339 HIS A CD2 1 
ATOM   1610  C  CE1 . HIS A 1 323 ? 168.888 141.258 153.825 1.00 87.58  ? 339 HIS A CE1 1 
ATOM   1611  N  NE2 . HIS A 1 323 ? 168.533 140.991 155.068 1.00 87.58  ? 339 HIS A NE2 1 
ATOM   1612  N  N   . THR A 1 324 ? 165.275 139.864 150.346 1.00 90.30  ? 340 THR A N   1 
ATOM   1613  C  CA  . THR A 1 324 ? 166.024 139.430 149.173 1.00 90.30  ? 340 THR A CA  1 
ATOM   1614  C  C   . THR A 1 324 ? 167.286 140.266 148.991 1.00 90.30  ? 340 THR A C   1 
ATOM   1615  O  O   . THR A 1 324 ? 167.212 141.490 148.843 1.00 90.30  ? 340 THR A O   1 
ATOM   1616  C  CB  . THR A 1 324 ? 165.151 139.520 147.929 1.00 90.30  ? 340 THR A CB  1 
ATOM   1617  O  OG1 . THR A 1 324 ? 164.149 138.499 147.974 1.00 90.30  ? 340 THR A OG1 1 
ATOM   1618  C  CG2 . THR A 1 324 ? 165.999 139.323 146.695 1.00 90.30  ? 340 THR A CG2 1 
ATOM   1619  N  N   . LEU A 1 325 ? 168.441 139.605 149.003 1.00 98.96  ? 341 LEU A N   1 
ATOM   1620  C  CA  . LEU A 1 325 ? 169.726 140.266 148.818 1.00 98.96  ? 341 LEU A CA  1 
ATOM   1621  C  C   . LEU A 1 325 ? 170.246 139.970 147.416 1.00 98.96  ? 341 LEU A C   1 
ATOM   1622  O  O   . LEU A 1 325 ? 170.344 138.804 147.018 1.00 98.96  ? 341 LEU A O   1 
ATOM   1623  C  CB  . LEU A 1 325 ? 170.731 139.801 149.873 1.00 98.96  ? 341 LEU A CB  1 
ATOM   1624  C  CG  . LEU A 1 325 ? 171.926 140.717 150.135 1.00 98.96  ? 341 LEU A CG  1 
ATOM   1625  C  CD1 . LEU A 1 325 ? 171.464 142.023 150.756 1.00 98.96  ? 341 LEU A CD1 1 
ATOM   1626  C  CD2 . LEU A 1 325 ? 172.938 140.028 151.034 1.00 98.96  ? 341 LEU A CD2 1 
ATOM   1627  N  N   . VAL A 1 326 ? 170.575 141.026 146.675 1.00 97.76  ? 342 VAL A N   1 
ATOM   1628  C  CA  . VAL A 1 326 ? 170.991 140.937 145.281 1.00 97.76  ? 342 VAL A CA  1 
ATOM   1629  C  C   . VAL A 1 326 ? 172.273 141.743 145.105 1.00 97.76  ? 342 VAL A C   1 
ATOM   1630  O  O   . VAL A 1 326 ? 172.510 142.718 145.820 1.00 97.76  ? 342 VAL A O   1 
ATOM   1631  C  CB  . VAL A 1 326 ? 169.873 141.445 144.336 1.00 97.76  ? 342 VAL A CB  1 
ATOM   1632  C  CG1 . VAL A 1 326 ? 170.324 141.454 142.889 1.00 97.76  ? 342 VAL A CG1 1 
ATOM   1633  C  CG2 . VAL A 1 326 ? 168.620 140.600 144.491 1.00 97.76  ? 342 VAL A CG2 1 
ATOM   1634  N  N   . SER A 1 327 ? 173.113 141.327 144.159 1.00 108.25 ? 343 SER A N   1 
ATOM   1635  C  CA  . SER A 1 327 ? 174.350 142.031 143.847 1.00 108.25 ? 343 SER A CA  1 
ATOM   1636  C  C   . SER A 1 327 ? 174.269 142.629 142.449 1.00 108.25 ? 343 SER A C   1 
ATOM   1637  O  O   . SER A 1 327 ? 173.807 141.973 141.511 1.00 108.25 ? 343 SER A O   1 
ATOM   1638  C  CB  . SER A 1 327 ? 175.559 141.097 143.937 1.00 108.25 ? 343 SER A CB  1 
ATOM   1639  O  OG  . SER A 1 327 ? 176.713 141.698 143.376 1.00 108.25 ? 343 SER A OG  1 
ATOM   1640  N  N   . VAL A 1 328 ? 174.718 143.875 142.311 1.00 109.15 ? 344 VAL A N   1 
ATOM   1641  C  CA  . VAL A 1 328 ? 174.761 144.559 141.022 1.00 109.15 ? 344 VAL A CA  1 
ATOM   1642  C  C   . VAL A 1 328 ? 176.148 145.169 140.856 1.00 109.15 ? 344 VAL A C   1 
ATOM   1643  O  O   . VAL A 1 328 ? 176.369 146.322 141.259 1.00 109.15 ? 344 VAL A O   1 
ATOM   1644  C  CB  . VAL A 1 328 ? 173.669 145.637 140.911 1.00 109.15 ? 344 VAL A CB  1 
ATOM   1645  C  CG1 . VAL A 1 328 ? 173.547 146.121 139.474 1.00 109.15 ? 344 VAL A CG1 1 
ATOM   1646  C  CG2 . VAL A 1 328 ? 172.330 145.114 141.415 1.00 109.15 ? 344 VAL A CG2 1 
ATOM   1647  N  N   . PRO A 1 329 ? 177.116 144.431 140.310 1.00 105.50 ? 345 PRO A N   1 
ATOM   1648  C  CA  . PRO A 1 329 ? 178.429 145.036 140.031 1.00 105.50 ? 345 PRO A CA  1 
ATOM   1649  C  C   . PRO A 1 329 ? 178.378 146.151 139.003 1.00 105.50 ? 345 PRO A C   1 
ATOM   1650  O  O   . PRO A 1 329 ? 179.318 146.953 138.938 1.00 105.50 ? 345 PRO A O   1 
ATOM   1651  C  CB  . PRO A 1 329 ? 179.267 143.850 139.531 1.00 105.50 ? 345 PRO A CB  1 
ATOM   1652  C  CG  . PRO A 1 329 ? 178.267 142.836 139.074 1.00 105.50 ? 345 PRO A CG  1 
ATOM   1653  C  CD  . PRO A 1 329 ? 177.078 143.000 139.967 1.00 105.50 ? 345 PRO A CD  1 
ATOM   1654  N  N   . GLY A 1 330 ? 177.322 146.218 138.187 1.00 118.70 ? 346 GLY A N   1 
ATOM   1655  C  CA  . GLY A 1 330 ? 177.207 147.305 137.226 1.00 118.70 ? 346 GLY A CA  1 
ATOM   1656  C  C   . GLY A 1 330 ? 177.224 148.668 137.890 1.00 118.70 ? 346 GLY A C   1 
ATOM   1657  O  O   . GLY A 1 330 ? 177.908 149.588 137.435 1.00 118.70 ? 346 GLY A O   1 
ATOM   1658  N  N   . LYS A 1 331 ? 176.467 148.816 138.973 1.00 109.72 ? 347 LYS A N   1 
ATOM   1659  C  CA  . LYS A 1 331 ? 176.487 150.024 139.781 1.00 109.72 ? 347 LYS A CA  1 
ATOM   1660  C  C   . LYS A 1 331 ? 177.267 149.837 141.074 1.00 109.72 ? 347 LYS A C   1 
ATOM   1661  O  O   . LYS A 1 331 ? 177.250 150.726 141.931 1.00 109.72 ? 347 LYS A O   1 
ATOM   1662  C  CB  . LYS A 1 331 ? 175.061 150.487 140.082 1.00 109.72 ? 347 LYS A CB  1 
ATOM   1663  C  CG  . LYS A 1 331 ? 174.160 150.526 138.858 1.00 109.72 ? 347 LYS A CG  1 
ATOM   1664  C  CD  . LYS A 1 331 ? 172.861 151.253 139.148 1.00 109.72 ? 347 LYS A CD  1 
ATOM   1665  C  CE  . LYS A 1 331 ? 171.956 151.260 137.928 1.00 109.72 ? 347 LYS A CE  1 
ATOM   1666  N  NZ  . LYS A 1 331 ? 171.641 149.883 137.461 1.00 109.72 ? 347 LYS A NZ  1 
ATOM   1667  N  N   . ASP A 1 332 ? 177.949 148.698 141.228 1.00 124.37 ? 348 ASP A N   1 
ATOM   1668  C  CA  . ASP A 1 332 ? 178.774 148.415 142.403 1.00 124.37 ? 348 ASP A CA  1 
ATOM   1669  C  C   . ASP A 1 332 ? 177.945 148.519 143.682 1.00 124.37 ? 348 ASP A C   1 
ATOM   1670  O  O   . ASP A 1 332 ? 178.398 149.043 144.702 1.00 124.37 ? 348 ASP A O   1 
ATOM   1671  C  CB  . ASP A 1 332 ? 179.996 149.338 142.452 1.00 124.37 ? 348 ASP A CB  1 
ATOM   1672  C  CG  . ASP A 1 332 ? 181.131 148.768 143.283 1.00 124.37 ? 348 ASP A CG  1 
ATOM   1673  O  OD1 . ASP A 1 332 ? 180.860 148.054 144.269 1.00 124.37 ? 348 ASP A OD1 1 
ATOM   1674  O  OD2 . ASP A 1 332 ? 182.302 149.037 142.945 1.00 124.37 ? 348 ASP A OD2 1 
ATOM   1675  N  N   . ALA A 1 333 ? 176.709 148.028 143.622 1.00 113.49 ? 349 ALA A N   1 
ATOM   1676  C  CA  . ALA A 1 333 ? 175.752 148.206 144.703 1.00 113.49 ? 349 ALA A CA  1 
ATOM   1677  C  C   . ALA A 1 333 ? 175.099 146.879 145.056 1.00 113.49 ? 349 ALA A C   1 
ATOM   1678  O  O   . ALA A 1 333 ? 174.766 146.081 144.175 1.00 113.49 ? 349 ALA A O   1 
ATOM   1679  C  CB  . ALA A 1 333 ? 174.676 149.230 144.324 1.00 113.49 ? 349 ALA A CB  1 
ATOM   1680  N  N   . ILE A 1 334 ? 174.887 146.658 146.348 1.00 103.58 ? 350 ILE A N   1 
ATOM   1681  C  CA  . ILE A 1 334 ? 174.206 145.454 146.824 1.00 103.58 ? 350 ILE A CA  1 
ATOM   1682  C  C   . ILE A 1 334 ? 172.835 145.842 147.357 1.00 103.58 ? 350 ILE A C   1 
ATOM   1683  O  O   . ILE A 1 334 ? 172.733 146.569 148.347 1.00 103.58 ? 350 ILE A O   1 
ATOM   1684  C  CB  . ILE A 1 334 ? 175.025 144.728 147.902 1.00 103.58 ? 350 ILE A CB  1 
ATOM   1685  C  CG1 . ILE A 1 334 ? 176.370 144.271 147.335 1.00 103.58 ? 350 ILE A CG1 1 
ATOM   1686  C  CG2 . ILE A 1 334 ? 174.242 143.552 148.467 1.00 103.58 ? 350 ILE A CG2 1 
ATOM   1687  C  CD1 . ILE A 1 334 ? 177.227 143.522 148.330 1.00 103.58 ? 350 ILE A CD1 1 
ATOM   1688  N  N   . TYR A 1 335 ? 171.784 145.303 146.757 1.00 98.46  ? 351 TYR A N   1 
ATOM   1689  C  CA  . TYR A 1 335 ? 170.431 145.695 147.117 1.00 98.46  ? 351 TYR A CA  1 
ATOM   1690  C  C   . TYR A 1 335 ? 169.796 144.707 148.087 1.00 98.46  ? 351 TYR A C   1 
ATOM   1691  O  O   . TYR A 1 335 ? 170.069 143.506 148.062 1.00 98.46  ? 351 TYR A O   1 
ATOM   1692  C  CB  . TYR A 1 335 ? 169.551 145.832 145.874 1.00 98.46  ? 351 TYR A CB  1 
ATOM   1693  C  CG  . TYR A 1 335 ? 169.636 147.192 145.224 1.00 98.46  ? 351 TYR A CG  1 
ATOM   1694  C  CD1 . TYR A 1 335 ? 170.754 147.571 144.492 1.00 98.46  ? 351 TYR A CD1 1 
ATOM   1695  C  CD2 . TYR A 1 335 ? 168.605 148.109 145.368 1.00 98.46  ? 351 TYR A CD2 1 
ATOM   1696  C  CE1 . TYR A 1 335 ? 170.831 148.822 143.906 1.00 98.46  ? 351 TYR A CE1 1 
ATOM   1697  C  CE2 . TYR A 1 335 ? 168.672 149.357 144.789 1.00 98.46  ? 351 TYR A CE2 1 
ATOM   1698  C  CZ  . TYR A 1 335 ? 169.786 149.711 144.061 1.00 98.46  ? 351 TYR A CZ  1 
ATOM   1699  O  OH  . TYR A 1 335 ? 169.849 150.960 143.489 1.00 98.46  ? 351 TYR A OH  1 
ATOM   1700  N  N   . SER A 1 336 ? 168.942 145.248 148.952 1.00 90.53  ? 352 SER A N   1 
ATOM   1701  C  CA  . SER A 1 336 ? 168.151 144.495 149.919 1.00 90.53  ? 352 SER A CA  1 
ATOM   1702  C  C   . SER A 1 336 ? 166.706 144.937 149.713 1.00 90.53  ? 352 SER A C   1 
ATOM   1703  O  O   . SER A 1 336 ? 166.338 146.063 150.075 1.00 90.53  ? 352 SER A O   1 
ATOM   1704  C  CB  . SER A 1 336 ? 168.621 144.746 151.346 1.00 90.53  ? 352 SER A CB  1 
ATOM   1705  O  OG  . SER A 1 336 ? 167.677 144.262 152.284 1.00 90.53  ? 352 SER A OG  1 
ATOM   1706  N  N   . LEU A 1 337 ? 165.924 144.085 149.058 1.00 80.84  ? 353 LEU A N   1 
ATOM   1707  C  CA  . LEU A 1 337 ? 164.541 144.371 148.716 1.00 80.84  ? 353 LEU A CA  1 
ATOM   1708  C  C   . LEU A 1 337 ? 163.598 143.528 149.565 1.00 80.84  ? 353 LEU A C   1 
ATOM   1709  O  O   . LEU A 1 337 ? 163.964 142.463 150.073 1.00 80.84  ? 353 LEU A O   1 
ATOM   1710  C  CB  . LEU A 1 337 ? 164.272 144.105 147.230 1.00 80.84  ? 353 LEU A CB  1 
ATOM   1711  C  CG  . LEU A 1 337 ? 165.137 144.837 146.204 1.00 80.84  ? 353 LEU A CG  1 
ATOM   1712  C  CD1 . LEU A 1 337 ? 166.380 144.028 145.869 1.00 80.84  ? 353 LEU A CD1 1 
ATOM   1713  C  CD2 . LEU A 1 337 ? 164.338 145.142 144.947 1.00 80.84  ? 353 LEU A CD2 1 
ATOM   1714  N  N   . GLY A 1 338 ? 162.368 144.017 149.699 1.00 88.27  ? 354 GLY A N   1 
ATOM   1715  C  CA  . GLY A 1 338 ? 161.306 143.306 150.381 1.00 88.27  ? 354 GLY A CA  1 
ATOM   1716  C  C   . GLY A 1 338 ? 161.633 143.024 151.834 1.00 88.27  ? 354 GLY A C   1 
ATOM   1717  O  O   . GLY A 1 338 ? 162.318 143.791 152.517 1.00 88.27  ? 354 GLY A O   1 
ATOM   1718  N  N   . GLY A 1 339 ? 161.131 141.895 152.312 1.00 92.22  ? 355 GLY A N   1 
ATOM   1719  C  CA  . GLY A 1 339 ? 161.396 141.418 153.652 1.00 92.22  ? 355 GLY A CA  1 
ATOM   1720  C  C   . GLY A 1 339 ? 160.142 141.390 154.510 1.00 92.22  ? 355 GLY A C   1 
ATOM   1721  O  O   . GLY A 1 339 ? 159.107 141.976 154.189 1.00 92.22  ? 355 GLY A O   1 
ATOM   1722  N  N   . LYS A 1 340 ? 160.264 140.681 155.629 1.00 93.87  ? 356 LYS A N   1 
ATOM   1723  C  CA  . LYS A 1 340 ? 159.202 140.566 156.618 1.00 93.87  ? 356 LYS A CA  1 
ATOM   1724  C  C   . LYS A 1 340 ? 159.695 141.162 157.928 1.00 93.87  ? 356 LYS A C   1 
ATOM   1725  O  O   . LYS A 1 340 ? 160.759 140.780 158.425 1.00 93.87  ? 356 LYS A O   1 
ATOM   1726  C  CB  . LYS A 1 340 ? 158.774 139.107 156.806 1.00 93.87  ? 356 LYS A CB  1 
ATOM   1727  C  CG  . LYS A 1 340 ? 158.421 138.724 158.233 1.00 93.87  ? 356 LYS A CG  1 
ATOM   1728  C  CD  . LYS A 1 340 ? 157.976 137.273 158.322 1.00 93.87  ? 356 LYS A CD  1 
ATOM   1729  C  CE  . LYS A 1 340 ? 156.943 136.943 157.256 1.00 93.87  ? 356 LYS A CE  1 
ATOM   1730  N  NZ  . LYS A 1 340 ? 156.349 135.594 157.463 1.00 93.87  ? 356 LYS A NZ  1 
ATOM   1731  N  N   . THR A 1 341 ? 158.935 142.107 158.472 1.00 98.70  ? 357 THR A N   1 
ATOM   1732  C  CA  . THR A 1 341 ? 159.320 142.746 159.719 1.00 98.70  ? 357 THR A CA  1 
ATOM   1733  C  C   . THR A 1 341 ? 159.131 141.795 160.897 1.00 98.70  ? 357 THR A C   1 
ATOM   1734  O  O   . THR A 1 341 ? 158.460 140.763 160.802 1.00 98.70  ? 357 THR A O   1 
ATOM   1735  C  CB  . THR A 1 341 ? 158.508 144.020 159.944 1.00 98.70  ? 357 THR A CB  1 
ATOM   1736  O  OG1 . THR A 1 341 ? 157.141 143.679 160.202 1.00 98.70  ? 357 THR A OG1 1 
ATOM   1737  C  CG2 . THR A 1 341 ? 158.576 144.909 158.716 1.00 98.70  ? 357 THR A CG2 1 
ATOM   1738  N  N   . LEU A 1 342 ? 159.739 142.160 162.028 1.00 103.29 ? 358 LEU A N   1 
ATOM   1739  C  CA  . LEU A 1 342 ? 159.628 141.355 163.240 1.00 103.29 ? 358 LEU A CA  1 
ATOM   1740  C  C   . LEU A 1 342 ? 158.235 141.401 163.851 1.00 103.29 ? 358 LEU A C   1 
ATOM   1741  O  O   . LEU A 1 342 ? 157.963 140.636 164.782 1.00 103.29 ? 358 LEU A O   1 
ATOM   1742  C  CB  . LEU A 1 342 ? 160.658 141.811 164.276 1.00 103.29 ? 358 LEU A CB  1 
ATOM   1743  C  CG  . LEU A 1 342 ? 162.063 141.199 164.238 1.00 103.29 ? 358 LEU A CG  1 
ATOM   1744  C  CD1 . LEU A 1 342 ? 162.021 139.756 164.718 1.00 103.29 ? 358 LEU A CD1 1 
ATOM   1745  C  CD2 . LEU A 1 342 ? 162.700 141.291 162.858 1.00 103.29 ? 358 LEU A CD2 1 
ATOM   1746  N  N   . GLN A 1 343 ? 157.385 142.239 163.261 1.00 125.06 ? 359 GLN A N   1 
ATOM   1747  C  CA  . GLN A 1 343 ? 155.977 142.424 163.685 1.00 125.06 ? 359 GLN A CA  1 
ATOM   1748  C  C   . GLN A 1 343 ? 155.072 141.590 162.776 1.00 125.06 ? 359 GLN A C   1 
ATOM   1749  O  O   . GLN A 1 343 ? 153.925 141.973 162.582 1.00 125.06 ? 359 GLN A O   1 
ATOM   1750  C  CB  . GLN A 1 343 ? 155.591 143.888 163.505 1.00 125.06 ? 359 GLN A CB  1 
ATOM   1751  C  CG  . GLN A 1 343 ? 155.949 144.767 164.686 1.00 125.06 ? 359 GLN A CG  1 
ATOM   1752  C  CD  . GLN A 1 343 ? 157.416 144.717 165.010 1.00 125.06 ? 359 GLN A CD  1 
ATOM   1753  O  OE1 . GLN A 1 343 ? 158.218 145.461 164.460 1.00 125.06 ? 359 GLN A OE1 1 
ATOM   1754  N  NE2 . GLN A 1 343 ? 157.773 143.845 165.931 1.00 125.06 ? 359 GLN A NE2 1 
ATOM   1755  N  N   . ASP A 1 344 ? 155.593 140.501 162.225 1.00 123.05 ? 360 ASP A N   1 
ATOM   1756  C  CA  . ASP A 1 344 ? 154.824 139.621 161.343 1.00 123.05 ? 360 ASP A CA  1 
ATOM   1757  C  C   . ASP A 1 344 ? 154.136 140.401 160.227 1.00 123.05 ? 360 ASP A C   1 
ATOM   1758  O  O   . ASP A 1 344 ? 153.075 140.005 159.739 1.00 123.05 ? 360 ASP A O   1 
ATOM   1759  C  CB  . ASP A 1 344 ? 153.802 138.792 162.129 1.00 123.05 ? 360 ASP A CB  1 
ATOM   1760  N  N   . THR A 1 345 ? 154.735 141.515 159.815 1.00 110.40 ? 361 THR A N   1 
ATOM   1761  C  CA  . THR A 1 345 ? 154.190 142.370 158.771 1.00 110.40 ? 361 THR A CA  1 
ATOM   1762  C  C   . THR A 1 345 ? 155.173 142.421 157.610 1.00 110.40 ? 361 THR A C   1 
ATOM   1763  O  O   . THR A 1 345 ? 156.373 142.626 157.817 1.00 110.40 ? 361 THR A O   1 
ATOM   1764  C  CB  . THR A 1 345 ? 153.916 143.781 159.303 1.00 110.40 ? 361 THR A CB  1 
ATOM   1765  O  OG1 . THR A 1 345 ? 152.777 143.752 160.171 1.00 110.40 ? 361 THR A OG1 1 
ATOM   1766  C  CG2 . THR A 1 345 ? 153.645 144.748 158.161 1.00 110.40 ? 361 THR A CG2 1 
ATOM   1767  N  N   . LEU A 1 346 ? 154.663 142.232 156.396 1.00 102.59 ? 362 LEU A N   1 
ATOM   1768  C  CA  . LEU A 1 346 ? 155.500 142.288 155.207 1.00 102.59 ? 362 LEU A CA  1 
ATOM   1769  C  C   . LEU A 1 346 ? 155.957 143.716 154.936 1.00 102.59 ? 362 LEU A C   1 
ATOM   1770  O  O   . LEU A 1 346 ? 155.297 144.688 155.314 1.00 102.59 ? 362 LEU A O   1 
ATOM   1771  C  CB  . LEU A 1 346 ? 154.746 141.739 153.999 1.00 102.59 ? 362 LEU A CB  1 
ATOM   1772  C  CG  . LEU A 1 346 ? 154.124 140.356 154.183 1.00 102.59 ? 362 LEU A CG  1 
ATOM   1773  C  CD1 . LEU A 1 346 ? 153.592 139.850 152.863 1.00 102.59 ? 362 LEU A CD1 1 
ATOM   1774  C  CD2 . LEU A 1 346 ? 155.137 139.381 154.759 1.00 102.59 ? 362 LEU A CD2 1 
ATOM   1775  N  N   . SER A 1 347 ? 157.103 143.838 154.273 1.00 102.64 ? 363 SER A N   1 
ATOM   1776  C  CA  . SER A 1 347 ? 157.707 145.130 153.994 1.00 102.64 ? 363 SER A CA  1 
ATOM   1777  C  C   . SER A 1 347 ? 157.923 145.310 152.499 1.00 102.64 ? 363 SER A C   1 
ATOM   1778  O  O   . SER A 1 347 ? 158.128 144.342 151.761 1.00 102.64 ? 363 SER A O   1 
ATOM   1779  C  CB  . SER A 1 347 ? 159.049 145.270 154.714 1.00 102.64 ? 363 SER A CB  1 
ATOM   1780  O  OG  . SER A 1 347 ? 160.048 144.494 154.077 1.00 102.64 ? 363 SER A OG  1 
ATOM   1781  N  N   . ASN A 1 348 ? 157.871 146.569 152.057 1.00 101.34 ? 364 ASN A N   1 
ATOM   1782  C  CA  . ASN A 1 348 ? 158.114 146.913 150.661 1.00 101.34 ? 364 ASN A CA  1 
ATOM   1783  C  C   . ASN A 1 348 ? 159.252 147.916 150.510 1.00 101.34 ? 364 ASN A C   1 
ATOM   1784  O  O   . ASN A 1 348 ? 159.346 148.588 149.480 1.00 101.34 ? 364 ASN A O   1 
ATOM   1785  C  CB  . ASN A 1 348 ? 156.839 147.462 150.020 1.00 101.34 ? 364 ASN A CB  1 
ATOM   1786  C  CG  . ASN A 1 348 ? 156.218 148.582 150.829 1.00 101.34 ? 364 ASN A CG  1 
ATOM   1787  O  OD1 . ASN A 1 348 ? 156.498 148.732 152.019 1.00 101.34 ? 364 ASN A OD1 1 
ATOM   1788  N  ND2 . ASN A 1 348 ? 155.368 149.375 150.188 1.00 101.34 ? 364 ASN A ND2 1 
ATOM   1789  N  N   . ALA A 1 349 ? 160.122 148.026 151.509 1.00 92.71  ? 365 ALA A N   1 
ATOM   1790  C  CA  . ALA A 1 349 ? 161.237 148.958 151.444 1.00 92.71  ? 365 ALA A CA  1 
ATOM   1791  C  C   . ALA A 1 349 ? 162.409 148.358 150.679 1.00 92.71  ? 365 ALA A C   1 
ATOM   1792  O  O   . ALA A 1 349 ? 162.608 147.140 150.661 1.00 92.71  ? 365 ALA A O   1 
ATOM   1793  C  CB  . ALA A 1 349 ? 161.684 149.358 152.849 1.00 92.71  ? 365 ALA A CB  1 
ATOM   1794  N  N   . VAL A 1 350 ? 163.192 149.229 150.044 1.00 88.05  ? 366 VAL A N   1 
ATOM   1795  C  CA  . VAL A 1 350 ? 164.353 148.818 149.264 1.00 88.05  ? 366 VAL A CA  1 
ATOM   1796  C  C   . VAL A 1 350 ? 165.534 149.678 149.691 1.00 88.05  ? 366 VAL A C   1 
ATOM   1797  O  O   . VAL A 1 350 ? 165.415 150.906 149.786 1.00 88.05  ? 366 VAL A O   1 
ATOM   1798  C  CB  . VAL A 1 350 ? 164.109 148.948 147.747 1.00 88.05  ? 366 VAL A CB  1 
ATOM   1799  C  CG1 . VAL A 1 350 ? 165.311 148.434 146.973 1.00 88.05  ? 366 VAL A CG1 1 
ATOM   1800  C  CG2 . VAL A 1 350 ? 162.850 148.199 147.338 1.00 88.05  ? 366 VAL A CG2 1 
ATOM   1801  N  N   . ILE A 1 351 ? 166.674 149.033 149.948 1.00 94.87  ? 367 ILE A N   1 
ATOM   1802  C  CA  . ILE A 1 351 ? 167.893 149.736 150.323 1.00 94.87  ? 367 ILE A CA  1 
ATOM   1803  C  C   . ILE A 1 351 ? 169.031 149.183 149.474 1.00 94.87  ? 367 ILE A C   1 
ATOM   1804  O  O   . ILE A 1 351 ? 168.945 148.080 148.937 1.00 94.87  ? 367 ILE A O   1 
ATOM   1805  C  CB  . ILE A 1 351 ? 168.181 149.593 151.833 1.00 94.87  ? 367 ILE A CB  1 
ATOM   1806  C  CG1 . ILE A 1 351 ? 167.082 150.281 152.627 1.00 94.87  ? 367 ILE A CG1 1 
ATOM   1807  C  CG2 . ILE A 1 351 ? 169.461 150.287 152.235 1.00 94.87  ? 367 ILE A CG2 1 
ATOM   1808  C  CD1 . ILE A 1 351 ? 167.142 149.970 154.071 1.00 94.87  ? 367 ILE A CD1 1 
ATOM   1809  N  N   . TYR A 1 352 ? 170.093 149.972 149.317 1.00 99.14  ? 368 TYR A N   1 
ATOM   1810  C  CA  . TYR A 1 352 ? 171.253 149.492 148.581 1.00 99.14  ? 368 TYR A CA  1 
ATOM   1811  C  C   . TYR A 1 352 ? 172.556 149.953 149.217 1.00 99.14  ? 368 TYR A C   1 
ATOM   1812  O  O   . TYR A 1 352 ? 172.660 151.073 149.715 1.00 99.14  ? 368 TYR A O   1 
ATOM   1813  C  CB  . TYR A 1 352 ? 171.186 149.945 147.116 1.00 99.14  ? 368 TYR A CB  1 
ATOM   1814  C  CG  . TYR A 1 352 ? 171.461 151.415 146.875 1.00 99.14  ? 368 TYR A CG  1 
ATOM   1815  C  CD1 . TYR A 1 352 ? 172.752 151.882 146.660 1.00 99.14  ? 368 TYR A CD1 1 
ATOM   1816  C  CD2 . TYR A 1 352 ? 170.421 152.334 146.849 1.00 99.14  ? 368 TYR A CD2 1 
ATOM   1817  C  CE1 . TYR A 1 352 ? 172.997 153.222 146.436 1.00 99.14  ? 368 TYR A CE1 1 
ATOM   1818  C  CE2 . TYR A 1 352 ? 170.657 153.675 146.624 1.00 99.14  ? 368 TYR A CE2 1 
ATOM   1819  C  CZ  . TYR A 1 352 ? 171.946 154.114 146.419 1.00 99.14  ? 368 TYR A CZ  1 
ATOM   1820  O  OH  . TYR A 1 352 ? 172.184 155.450 146.196 1.00 99.14  ? 368 TYR A OH  1 
ATOM   1821  N  N   . TYR A 1 353 ? 173.551 149.078 149.157 1.00 95.78  ? 369 TYR A N   1 
ATOM   1822  C  CA  . TYR A 1 353 ? 174.883 149.255 149.705 1.00 95.78  ? 369 TYR A CA  1 
ATOM   1823  C  C   . TYR A 1 353 ? 175.830 149.673 148.595 1.00 95.78  ? 369 TYR A C   1 
ATOM   1824  O  O   . TYR A 1 353 ? 175.612 149.356 147.423 1.00 95.78  ? 369 TYR A O   1 
ATOM   1825  C  CB  . TYR A 1 353 ? 175.361 147.944 150.340 1.00 95.78  ? 369 TYR A CB  1 
ATOM   1826  C  CG  . TYR A 1 353 ? 176.728 147.974 150.986 1.00 95.78  ? 369 TYR A CG  1 
ATOM   1827  C  CD1 . TYR A 1 353 ? 176.925 148.542 152.235 1.00 95.78  ? 369 TYR A CD1 1 
ATOM   1828  C  CD2 . TYR A 1 353 ? 177.821 147.401 150.349 1.00 95.78  ? 369 TYR A CD2 1 
ATOM   1829  C  CE1 . TYR A 1 353 ? 178.176 148.553 152.823 1.00 95.78  ? 369 TYR A CE1 1 
ATOM   1830  C  CE2 . TYR A 1 353 ? 179.072 147.408 150.926 1.00 95.78  ? 369 TYR A CE2 1 
ATOM   1831  C  CZ  . TYR A 1 353 ? 179.245 147.985 152.163 1.00 95.78  ? 369 TYR A CZ  1 
ATOM   1832  O  OH  . TYR A 1 353 ? 180.493 147.993 152.741 1.00 95.78  ? 369 TYR A OH  1 
ATOM   1833  N  N   . ARG A 1 354 ? 176.965 150.232 149.006 1.00 111.28 ? 370 ARG A N   1 
ATOM   1834  C  CA  . ARG A 1 354 ? 178.028 150.634 148.093 1.00 111.28 ? 370 ARG A CA  1 
ATOM   1835  C  C   . ARG A 1 354 ? 179.349 150.095 148.614 1.00 111.28 ? 370 ARG A C   1 
ATOM   1836  O  O   . ARG A 1 354 ? 179.788 150.477 149.702 1.00 111.28 ? 370 ARG A O   1 
ATOM   1837  C  CB  . ARG A 1 354 ? 178.100 152.160 147.978 1.00 111.28 ? 370 ARG A CB  1 
ATOM   1838  C  CG  . ARG A 1 354 ? 177.860 152.728 146.591 1.00 111.28 ? 370 ARG A CG  1 
ATOM   1839  C  CD  . ARG A 1 354 ? 176.444 152.463 146.121 1.00 111.28 ? 370 ARG A CD  1 
ATOM   1840  N  NE  . ARG A 1 354 ? 176.215 152.984 144.779 1.00 111.28 ? 370 ARG A NE  1 
ATOM   1841  C  CZ  . ARG A 1 354 ? 175.802 154.217 144.518 1.00 111.28 ? 370 ARG A CZ  1 
ATOM   1842  N  NH1 . ARG A 1 354 ? 175.588 155.093 145.486 1.00 111.28 ? 370 ARG A NH1 1 
ATOM   1843  N  NH2 . ARG A 1 354 ? 175.608 154.583 143.255 1.00 111.28 ? 370 ARG A NH2 1 
ATOM   1844  N  N   . VAL A 1 355 ? 179.977 149.202 147.846 1.00 116.91 ? 371 VAL A N   1 
ATOM   1845  C  CA  . VAL A 1 355 ? 181.251 148.628 148.270 1.00 116.91 ? 371 VAL A CA  1 
ATOM   1846  C  C   . VAL A 1 355 ? 182.323 149.707 148.350 1.00 116.91 ? 371 VAL A C   1 
ATOM   1847  O  O   . VAL A 1 355 ? 183.112 149.751 149.302 1.00 116.91 ? 371 VAL A O   1 
ATOM   1848  C  CB  . VAL A 1 355 ? 181.667 147.484 147.329 1.00 116.91 ? 371 VAL A CB  1 
ATOM   1849  C  CG1 . VAL A 1 355 ? 182.860 146.737 147.901 1.00 116.91 ? 371 VAL A CG1 1 
ATOM   1850  C  CG2 . VAL A 1 355 ? 180.502 146.533 147.106 1.00 116.91 ? 371 VAL A CG2 1 
ATOM   1851  N  N   . GLY A 1 356 ? 182.371 150.592 147.353 1.00 118.07 ? 372 GLY A N   1 
ATOM   1852  C  CA  . GLY A 1 356 ? 183.386 151.633 147.349 1.00 118.07 ? 372 GLY A CA  1 
ATOM   1853  C  C   . GLY A 1 356 ? 183.218 152.634 148.477 1.00 118.07 ? 372 GLY A C   1 
ATOM   1854  O  O   . GLY A 1 356 ? 184.195 153.024 149.123 1.00 118.07 ? 372 GLY A O   1 
ATOM   1855  N  N   . ASP A 1 357 ? 181.983 153.062 148.734 1.00 109.18 ? 373 ASP A N   1 
ATOM   1856  C  CA  . ASP A 1 357 ? 181.726 154.083 149.741 1.00 109.18 ? 373 ASP A CA  1 
ATOM   1857  C  C   . ASP A 1 357 ? 181.394 153.502 151.108 1.00 109.18 ? 373 ASP A C   1 
ATOM   1858  O  O   . ASP A 1 357 ? 181.499 154.220 152.110 1.00 109.18 ? 373 ASP A O   1 
ATOM   1859  C  CB  . ASP A 1 357 ? 180.583 154.997 149.288 1.00 109.18 ? 373 ASP A CB  1 
ATOM   1860  N  N   . ASN A 1 358 ? 180.991 152.233 151.166 1.00 100.52 ? 374 ASN A N   1 
ATOM   1861  C  CA  . ASN A 1 358 ? 180.650 151.547 152.412 1.00 100.52 ? 374 ASN A CA  1 
ATOM   1862  C  C   . ASN A 1 358 ? 179.510 152.282 153.122 1.00 100.52 ? 374 ASN A C   1 
ATOM   1863  O  O   . ASN A 1 358 ? 179.613 152.688 154.281 1.00 100.52 ? 374 ASN A O   1 
ATOM   1864  C  CB  . ASN A 1 358 ? 181.891 151.406 153.305 1.00 100.52 ? 374 ASN A CB  1 
ATOM   1865  C  CG  . ASN A 1 358 ? 181.682 150.457 154.476 1.00 100.52 ? 374 ASN A CG  1 
ATOM   1866  O  OD1 . ASN A 1 358 ? 180.575 150.292 154.979 1.00 100.52 ? 374 ASN A OD1 1 
ATOM   1867  N  ND2 . ASN A 1 358 ? 182.765 149.826 154.914 1.00 100.52 ? 374 ASN A ND2 1 
ATOM   1868  N  N   . VAL A 1 359 ? 178.414 152.467 152.384 1.00 99.23  ? 375 VAL A N   1 
ATOM   1869  C  CA  . VAL A 1 359 ? 177.227 153.141 152.897 1.00 99.23  ? 375 VAL A CA  1 
ATOM   1870  C  C   . VAL A 1 359 ? 175.982 152.431 152.384 1.00 99.23  ? 375 VAL A C   1 
ATOM   1871  O  O   . VAL A 1 359 ? 175.996 151.790 151.327 1.00 99.23  ? 375 VAL A O   1 
ATOM   1872  C  CB  . VAL A 1 359 ? 177.182 154.637 152.502 1.00 99.23  ? 375 VAL A CB  1 
ATOM   1873  C  CG1 . VAL A 1 359 ? 178.344 155.403 153.117 1.00 99.23  ? 375 VAL A CG1 1 
ATOM   1874  C  CG2 . VAL A 1 359 ? 177.179 154.788 150.988 1.00 99.23  ? 375 VAL A CG2 1 
ATOM   1875  N  N   . TRP A 1 360 ? 174.901 152.551 153.154 1.00 93.94  ? 376 TRP A N   1 
ATOM   1876  C  CA  . TRP A 1 360 ? 173.588 152.029 152.797 1.00 93.94  ? 376 TRP A CA  1 
ATOM   1877  C  C   . TRP A 1 360 ? 172.644 153.204 152.569 1.00 93.94  ? 376 TRP A C   1 
ATOM   1878  O  O   . TRP A 1 360 ? 172.587 154.124 153.393 1.00 93.94  ? 376 TRP A O   1 
ATOM   1879  C  CB  . TRP A 1 360 ? 173.030 151.125 153.899 1.00 93.94  ? 376 TRP A CB  1 
ATOM   1880  C  CG  . TRP A 1 360 ? 173.615 149.740 153.952 1.00 93.94  ? 376 TRP A CG  1 
ATOM   1881  C  CD1 . TRP A 1 360 ? 174.659 149.329 154.727 1.00 93.94  ? 376 TRP A CD1 1 
ATOM   1882  C  CD2 . TRP A 1 360 ? 173.202 148.592 153.198 1.00 93.94  ? 376 TRP A CD2 1 
ATOM   1883  N  NE1 . TRP A 1 360 ? 174.912 147.997 154.516 1.00 93.94  ? 376 TRP A NE1 1 
ATOM   1884  C  CE2 . TRP A 1 360 ? 174.035 147.522 153.578 1.00 93.94  ? 376 TRP A CE2 1 
ATOM   1885  C  CE3 . TRP A 1 360 ? 172.210 148.364 152.242 1.00 93.94  ? 376 TRP A CE3 1 
ATOM   1886  C  CZ2 . TRP A 1 360 ? 173.905 146.247 153.035 1.00 93.94  ? 376 TRP A CZ2 1 
ATOM   1887  C  CZ3 . TRP A 1 360 ? 172.082 147.097 151.705 1.00 93.94  ? 376 TRP A CZ3 1 
ATOM   1888  C  CH2 . TRP A 1 360 ? 172.925 146.055 152.102 1.00 93.94  ? 376 TRP A CH2 1 
ATOM   1889  N  N   . THR A 1 361 ? 171.905 153.176 151.462 1.00 91.03  ? 377 THR A N   1 
ATOM   1890  C  CA  . THR A 1 361 ? 171.005 154.258 151.085 1.00 91.03  ? 377 THR A CA  1 
ATOM   1891  C  C   . THR A 1 361 ? 169.629 153.690 150.763 1.00 91.03  ? 377 THR A C   1 
ATOM   1892  O  O   . THR A 1 361 ? 169.519 152.711 150.020 1.00 91.03  ? 377 THR A O   1 
ATOM   1893  C  CB  . THR A 1 361 ? 171.557 155.035 149.883 1.00 91.03  ? 377 THR A CB  1 
ATOM   1894  O  OG1 . THR A 1 361 ? 172.737 155.747 150.276 1.00 91.03  ? 377 THR A OG1 1 
ATOM   1895  C  CG2 . THR A 1 361 ? 170.531 156.027 149.363 1.00 91.03  ? 377 THR A CG2 1 
ATOM   1896  N  N   . GLU A 1 362 ? 168.587 154.309 151.314 1.00 103.79 ? 378 GLU A N   1 
ATOM   1897  C  CA  . GLU A 1 362 ? 167.214 153.925 151.019 1.00 103.79 ? 378 GLU A CA  1 
ATOM   1898  C  C   . GLU A 1 362 ? 166.808 154.406 149.628 1.00 103.79 ? 378 GLU A C   1 
ATOM   1899  O  O   . GLU A 1 362 ? 167.378 155.353 149.080 1.00 103.79 ? 378 GLU A O   1 
ATOM   1900  C  CB  . GLU A 1 362 ? 166.259 154.506 152.063 1.00 103.79 ? 378 GLU A CB  1 
ATOM   1901  C  CG  . GLU A 1 362 ? 166.385 153.896 153.447 1.00 103.79 ? 378 GLU A CG  1 
ATOM   1902  C  CD  . GLU A 1 362 ? 165.213 153.001 153.794 1.00 103.79 ? 378 GLU A CD  1 
ATOM   1903  O  OE1 . GLU A 1 362 ? 164.411 152.694 152.888 1.00 103.79 ? 378 GLU A OE1 1 
ATOM   1904  O  OE2 . GLU A 1 362 ? 165.091 152.607 154.973 1.00 103.79 ? 378 GLU A OE2 1 
ATOM   1905  N  N   . THR A 1 363 ? 165.808 153.747 149.053 1.00 92.73  ? 379 THR A N   1 
ATOM   1906  C  CA  . THR A 1 363 ? 165.352 154.125 147.718 1.00 92.73  ? 379 THR A CA  1 
ATOM   1907  C  C   . THR A 1 363 ? 163.856 153.837 147.621 1.00 92.73  ? 379 THR A C   1 
ATOM   1908  O  O   . THR A 1 363 ? 163.179 153.664 148.640 1.00 92.73  ? 379 THR A O   1 
ATOM   1909  C  CB  . THR A 1 363 ? 166.178 153.410 146.635 1.00 92.73  ? 379 THR A CB  1 
ATOM   1910  O  OG1 . THR A 1 363 ? 165.613 153.680 145.346 1.00 92.73  ? 379 THR A OG1 1 
ATOM   1911  C  CG2 . THR A 1 363 ? 166.193 151.916 146.870 1.00 92.73  ? 379 THR A CG2 1 
ATOM   1912  N  N   . THR A 1 364 ? 163.339 153.796 146.394 1.00 98.87  ? 380 THR A N   1 
ATOM   1913  C  CA  . THR A 1 364 ? 161.903 153.680 146.176 1.00 98.87  ? 380 THR A CA  1 
ATOM   1914  C  C   . THR A 1 364 ? 161.370 152.370 146.745 1.00 98.87  ? 380 THR A C   1 
ATOM   1915  O  O   . THR A 1 364 ? 162.067 151.354 146.790 1.00 98.87  ? 380 THR A O   1 
ATOM   1916  C  CB  . THR A 1 364 ? 161.587 153.767 144.682 1.00 98.87  ? 380 THR A CB  1 
ATOM   1917  O  OG1 . THR A 1 364 ? 162.380 154.799 144.084 1.00 98.87  ? 380 THR A OG1 1 
ATOM   1918  C  CG2 . THR A 1 364 ? 160.116 154.084 144.457 1.00 98.87  ? 380 THR A CG2 1 
ATOM   1919  N  N   . GLN A 1 365 ? 160.116 152.404 147.182 1.00 105.75 ? 381 GLN A N   1 
ATOM   1920  C  CA  . GLN A 1 365 ? 159.473 151.251 147.789 1.00 105.75 ? 381 GLN A CA  1 
ATOM   1921  C  C   . GLN A 1 365 ? 158.861 150.342 146.728 1.00 105.75 ? 381 GLN A C   1 
ATOM   1922  O  O   . GLN A 1 365 ? 158.680 150.725 145.569 1.00 105.75 ? 381 GLN A O   1 
ATOM   1923  C  CB  . GLN A 1 365 ? 158.390 151.697 148.771 1.00 105.75 ? 381 GLN A CB  1 
ATOM   1924  C  CG  . GLN A 1 365 ? 158.920 152.270 150.072 1.00 105.75 ? 381 GLN A CG  1 
ATOM   1925  C  CD  . GLN A 1 365 ? 157.812 152.615 151.046 1.00 105.75 ? 381 GLN A CD  1 
ATOM   1926  O  OE1 . GLN A 1 365 ? 156.751 153.098 150.650 1.00 105.75 ? 381 GLN A OE1 1 
ATOM   1927  N  NE2 . GLN A 1 365 ? 158.051 152.366 152.328 1.00 105.75 ? 381 GLN A NE2 1 
ATOM   1928  N  N   . LEU A 1 366 ? 158.541 149.122 147.147 1.00 100.89 ? 382 LEU A N   1 
ATOM   1929  C  CA  . LEU A 1 366 ? 157.907 148.153 146.268 1.00 100.89 ? 382 LEU A CA  1 
ATOM   1930  C  C   . LEU A 1 366 ? 156.400 148.373 146.234 1.00 100.89 ? 382 LEU A C   1 
ATOM   1931  O  O   . LEU A 1 366 ? 155.795 148.824 147.210 1.00 100.89 ? 382 LEU A O   1 
ATOM   1932  C  CB  . LEU A 1 366 ? 158.211 146.728 146.733 1.00 100.89 ? 382 LEU A CB  1 
ATOM   1933  C  CG  . LEU A 1 366 ? 159.670 146.268 146.703 1.00 100.89 ? 382 LEU A CG  1 
ATOM   1934  C  CD1 . LEU A 1 366 ? 159.819 144.947 147.438 1.00 100.89 ? 382 LEU A CD1 1 
ATOM   1935  C  CD2 . LEU A 1 366 ? 160.185 146.148 145.280 1.00 100.89 ? 382 LEU A CD2 1 
ATOM   1936  N  N   . GLU A 1 367 ? 155.795 148.059 145.087 1.00 105.67 ? 383 GLU A N   1 
ATOM   1937  C  CA  . GLU A 1 367 ? 154.350 148.216 144.957 1.00 105.67 ? 383 GLU A CA  1 
ATOM   1938  C  C   . GLU A 1 367 ? 153.608 147.278 145.901 1.00 105.67 ? 383 GLU A C   1 
ATOM   1939  O  O   . GLU A 1 367 ? 152.655 147.688 146.573 1.00 105.67 ? 383 GLU A O   1 
ATOM   1940  C  CB  . GLU A 1 367 ? 153.924 147.973 143.510 1.00 105.67 ? 383 GLU A CB  1 
ATOM   1941  C  CG  . GLU A 1 367 ? 154.460 148.996 142.523 1.00 105.67 ? 383 GLU A CG  1 
ATOM   1942  C  CD  . GLU A 1 367 ? 153.475 150.117 142.255 1.00 105.67 ? 383 GLU A CD  1 
ATOM   1943  O  OE1 . GLU A 1 367 ? 152.289 149.817 142.001 1.00 105.67 ? 383 GLU A OE1 1 
ATOM   1944  O  OE2 . GLU A 1 367 ? 153.884 151.296 142.298 1.00 105.67 ? 383 GLU A OE2 1 
ATOM   1945  N  N   . VAL A 1 368 ? 154.032 146.018 145.969 1.00 92.96  ? 384 VAL A N   1 
ATOM   1946  C  CA  . VAL A 1 368 ? 153.410 145.013 146.823 1.00 92.96  ? 384 VAL A CA  1 
ATOM   1947  C  C   . VAL A 1 368 ? 154.474 144.457 147.757 1.00 92.96  ? 384 VAL A C   1 
ATOM   1948  O  O   . VAL A 1 368 ? 155.550 144.047 147.305 1.00 92.96  ? 384 VAL A O   1 
ATOM   1949  C  CB  . VAL A 1 368 ? 152.764 143.885 145.997 1.00 92.96  ? 384 VAL A CB  1 
ATOM   1950  C  CG1 . VAL A 1 368 ? 151.996 142.936 146.903 1.00 92.96  ? 384 VAL A CG1 1 
ATOM   1951  C  CG2 . VAL A 1 368 ? 151.853 144.461 144.926 1.00 92.96  ? 384 VAL A CG2 1 
ATOM   1952  N  N   . ALA A 1 369 ? 154.174 144.441 149.053 1.00 92.55  ? 385 ALA A N   1 
ATOM   1953  C  CA  . ALA A 1 369 ? 155.110 143.900 150.030 1.00 92.55  ? 385 ALA A CA  1 
ATOM   1954  C  C   . ALA A 1 369 ? 155.155 142.380 149.944 1.00 92.55  ? 385 ALA A C   1 
ATOM   1955  O  O   . ALA A 1 369 ? 154.113 141.717 149.922 1.00 92.55  ? 385 ALA A O   1 
ATOM   1956  C  CB  . ALA A 1 369 ? 154.717 144.341 151.438 1.00 92.55  ? 385 ALA A CB  1 
ATOM   1957  N  N   . VAL A 1 370 ? 156.368 141.824 149.896 1.00 88.11  ? 386 VAL A N   1 
ATOM   1958  C  CA  . VAL A 1 370 ? 156.573 140.383 149.820 1.00 88.11  ? 386 VAL A CA  1 
ATOM   1959  C  C   . VAL A 1 370 ? 157.709 139.993 150.756 1.00 88.11  ? 386 VAL A C   1 
ATOM   1960  O  O   . VAL A 1 370 ? 158.510 140.827 151.182 1.00 88.11  ? 386 VAL A O   1 
ATOM   1961  C  CB  . VAL A 1 370 ? 156.881 139.900 148.385 1.00 88.11  ? 386 VAL A CB  1 
ATOM   1962  C  CG1 . VAL A 1 370 ? 155.675 140.097 147.481 1.00 88.11  ? 386 VAL A CG1 1 
ATOM   1963  C  CG2 . VAL A 1 370 ? 158.089 140.628 147.834 1.00 88.11  ? 386 VAL A CG2 1 
ATOM   1964  N  N   . SER A 1 371 ? 157.766 138.702 151.074 1.00 93.14  ? 387 SER A N   1 
ATOM   1965  C  CA  . SER A 1 371 ? 158.791 138.156 151.952 1.00 93.14  ? 387 SER A CA  1 
ATOM   1966  C  C   . SER A 1 371 ? 159.278 136.830 151.390 1.00 93.14  ? 387 SER A C   1 
ATOM   1967  O  O   . SER A 1 371 ? 158.477 136.014 150.928 1.00 93.14  ? 387 SER A O   1 
ATOM   1968  C  CB  . SER A 1 371 ? 158.262 137.958 153.376 1.00 93.14  ? 387 SER A CB  1 
ATOM   1969  O  OG  . SER A 1 371 ? 159.180 137.215 154.158 1.00 93.14  ? 387 SER A OG  1 
ATOM   1970  N  N   . GLY A 1 372 ? 160.591 136.617 151.438 1.00 83.64  ? 388 GLY A N   1 
ATOM   1971  C  CA  . GLY A 1 372 ? 161.164 135.374 150.966 1.00 83.64  ? 388 GLY A CA  1 
ATOM   1972  C  C   . GLY A 1 372 ? 161.248 135.233 149.464 1.00 83.64  ? 388 GLY A C   1 
ATOM   1973  O  O   . GLY A 1 372 ? 161.565 134.141 148.979 1.00 83.64  ? 388 GLY A O   1 
ATOM   1974  N  N   . ALA A 1 373 ? 160.974 136.295 148.714 1.00 90.01  ? 389 ALA A N   1 
ATOM   1975  C  CA  . ALA A 1 373 ? 161.010 136.230 147.261 1.00 90.01  ? 389 ALA A CA  1 
ATOM   1976  C  C   . ALA A 1 373 ? 162.438 136.060 146.753 1.00 90.01  ? 389 ALA A C   1 
ATOM   1977  O  O   . ALA A 1 373 ? 163.399 136.550 147.350 1.00 90.01  ? 389 ALA A O   1 
ATOM   1978  C  CB  . ALA A 1 373 ? 160.390 137.490 146.658 1.00 90.01  ? 389 ALA A CB  1 
ATOM   1979  N  N   . ALA A 1 374 ? 162.569 135.341 145.641 1.00 99.91  ? 390 ALA A N   1 
ATOM   1980  C  CA  . ALA A 1 374 ? 163.868 135.131 145.016 1.00 99.91  ? 390 ALA A CA  1 
ATOM   1981  C  C   . ALA A 1 374 ? 164.225 136.320 144.132 1.00 99.91  ? 390 ALA A C   1 
ATOM   1982  O  O   . ALA A 1 374 ? 163.393 136.800 143.357 1.00 99.91  ? 390 ALA A O   1 
ATOM   1983  C  CB  . ALA A 1 374 ? 163.865 133.841 144.198 1.00 99.91  ? 390 ALA A CB  1 
ATOM   1984  N  N   . GLY A 1 375 ? 165.458 136.800 144.258 1.00 92.99  ? 391 GLY A N   1 
ATOM   1985  C  CA  . GLY A 1 375 ? 165.936 137.935 143.484 1.00 92.99  ? 391 GLY A CA  1 
ATOM   1986  C  C   . GLY A 1 375 ? 166.738 137.504 142.269 1.00 92.99  ? 391 GLY A C   1 
ATOM   1987  O  O   . GLY A 1 375 ? 167.460 136.509 142.307 1.00 92.99  ? 391 GLY A O   1 
ATOM   1988  N  N   . ALA A 1 376 ? 166.600 138.271 141.188 1.00 107.23 ? 392 ALA A N   1 
ATOM   1989  C  CA  . ALA A 1 376 ? 167.341 138.017 139.954 1.00 107.23 ? 392 ALA A CA  1 
ATOM   1990  C  C   . ALA A 1 376 ? 167.714 139.356 139.333 1.00 107.23 ? 392 ALA A C   1 
ATOM   1991  O  O   . ALA A 1 376 ? 166.833 140.118 138.927 1.00 107.23 ? 392 ALA A O   1 
ATOM   1992  C  CB  . ALA A 1 376 ? 166.522 137.172 138.979 1.00 107.23 ? 392 ALA A CB  1 
ATOM   1993  N  N   . ASN A 1 377 ? 169.009 139.649 139.264 1.00 109.66 ? 393 ASN A N   1 
ATOM   1994  C  CA  . ASN A 1 377 ? 169.493 140.885 138.658 1.00 109.66 ? 393 ASN A CA  1 
ATOM   1995  C  C   . ASN A 1 377 ? 169.778 140.629 137.183 1.00 109.66 ? 393 ASN A C   1 
ATOM   1996  O  O   . ASN A 1 377 ? 170.728 139.917 136.841 1.00 109.66 ? 393 ASN A O   1 
ATOM   1997  C  CB  . ASN A 1 377 ? 170.741 141.382 139.384 1.00 109.66 ? 393 ASN A CB  1 
ATOM   1998  C  CG  . ASN A 1 377 ? 171.526 142.399 138.578 1.00 109.66 ? 393 ASN A CG  1 
ATOM   1999  O  OD1 . ASN A 1 377 ? 170.954 143.221 137.863 1.00 109.66 ? 393 ASN A OD1 1 
ATOM   2000  N  ND2 . ASN A 1 377 ? 172.848 142.349 138.693 1.00 109.66 ? 393 ASN A ND2 1 
ATOM   2001  N  N   . LEU A 1 378 ? 168.956 141.208 136.308 1.00 111.83 ? 394 LEU A N   1 
ATOM   2002  C  CA  . LEU A 1 378 ? 169.125 141.098 134.862 1.00 111.83 ? 394 LEU A CA  1 
ATOM   2003  C  C   . LEU A 1 378 ? 169.375 142.490 134.298 1.00 111.83 ? 394 LEU A C   1 
ATOM   2004  O  O   . LEU A 1 378 ? 168.482 143.344 134.332 1.00 111.83 ? 394 LEU A O   1 
ATOM   2005  C  CB  . LEU A 1 378 ? 167.897 140.459 134.214 1.00 111.83 ? 394 LEU A CB  1 
ATOM   2006  C  CG  . LEU A 1 378 ? 167.968 138.971 133.871 1.00 111.83 ? 394 LEU A CG  1 
ATOM   2007  C  CD1 . LEU A 1 378 ? 167.022 138.655 132.727 1.00 111.83 ? 394 LEU A CD1 1 
ATOM   2008  C  CD2 . LEU A 1 378 ? 169.387 138.581 133.502 1.00 111.83 ? 394 LEU A CD2 1 
ATOM   2009  N  N   . ASN A 1 379 ? 170.584 142.712 133.778 1.00 107.33 ? 395 ASN A N   1 
ATOM   2010  C  CA  . ASN A 1 379 ? 170.952 143.979 133.139 1.00 107.33 ? 395 ASN A CA  1 
ATOM   2011  C  C   . ASN A 1 379 ? 170.696 145.170 134.059 1.00 107.33 ? 395 ASN A C   1 
ATOM   2012  O  O   . ASN A 1 379 ? 170.371 146.269 133.603 1.00 107.33 ? 395 ASN A O   1 
ATOM   2013  C  CB  . ASN A 1 379 ? 170.217 144.159 131.808 1.00 107.33 ? 395 ASN A CB  1 
ATOM   2014  N  N   . GLY A 1 380 ? 170.839 144.958 135.366 1.00 102.46 ? 396 GLY A N   1 
ATOM   2015  C  CA  . GLY A 1 380 ? 170.658 146.002 136.345 1.00 102.46 ? 396 GLY A CA  1 
ATOM   2016  C  C   . GLY A 1 380 ? 169.260 146.100 136.918 1.00 102.46 ? 396 GLY A C   1 
ATOM   2017  O  O   . GLY A 1 380 ? 169.078 146.727 137.966 1.00 102.46 ? 396 GLY A O   1 
ATOM   2018  N  N   . ILE A 1 381 ? 168.273 145.492 136.270 1.00 107.10 ? 397 ILE A N   1 
ATOM   2019  C  CA  . ILE A 1 381 ? 166.899 145.497 136.759 1.00 107.10 ? 397 ILE A CA  1 
ATOM   2020  C  C   . ILE A 1 381 ? 166.724 144.302 137.686 1.00 107.10 ? 397 ILE A C   1 
ATOM   2021  O  O   . ILE A 1 381 ? 167.091 143.174 137.337 1.00 107.10 ? 397 ILE A O   1 
ATOM   2022  C  CB  . ILE A 1 381 ? 165.886 145.454 135.599 1.00 107.10 ? 397 ILE A CB  1 
ATOM   2023  C  CG1 . ILE A 1 381 ? 165.836 146.782 134.826 1.00 107.10 ? 397 ILE A CG1 1 
ATOM   2024  C  CG2 . ILE A 1 381 ? 164.497 145.130 136.121 1.00 107.10 ? 397 ILE A CG2 1 
ATOM   2025  C  CD1 . ILE A 1 381 ? 167.053 147.103 133.976 1.00 107.10 ? 397 ILE A CD1 1 
ATOM   2026  N  N   . ILE A 1 382 ? 166.175 144.545 138.870 1.00 91.42  ? 398 ILE A N   1 
ATOM   2027  C  CA  . ILE A 1 382 ? 165.970 143.493 139.858 1.00 91.42  ? 398 ILE A CA  1 
ATOM   2028  C  C   . ILE A 1 382 ? 164.568 142.925 139.691 1.00 91.42  ? 398 ILE A C   1 
ATOM   2029  O  O   . ILE A 1 382 ? 163.587 143.673 139.644 1.00 91.42  ? 398 ILE A O   1 
ATOM   2030  C  CB  . ILE A 1 382 ? 166.179 144.034 141.280 1.00 91.42  ? 398 ILE A CB  1 
ATOM   2031  C  CG1 . ILE A 1 382 ? 167.575 144.644 141.412 1.00 91.42  ? 398 ILE A CG1 1 
ATOM   2032  C  CG2 . ILE A 1 382 ? 165.973 142.932 142.306 1.00 91.42  ? 398 ILE A CG2 1 
ATOM   2033  C  CD1 . ILE A 1 382 ? 167.835 145.281 142.753 1.00 91.42  ? 398 ILE A CD1 1 
ATOM   2034  N  N   . TYR A 1 383 ? 164.470 141.605 139.585 1.00 102.38 ? 399 TYR A N   1 
ATOM   2035  C  CA  . TYR A 1 383 ? 163.190 140.914 139.521 1.00 102.38 ? 399 TYR A CA  1 
ATOM   2036  C  C   . TYR A 1 383 ? 163.000 140.113 140.801 1.00 102.38 ? 399 TYR A C   1 
ATOM   2037  O  O   . TYR A 1 383 ? 163.846 139.282 141.153 1.00 102.38 ? 399 TYR A O   1 
ATOM   2038  C  CB  . TYR A 1 383 ? 163.108 140.021 138.284 1.00 102.38 ? 399 TYR A CB  1 
ATOM   2039  C  CG  . TYR A 1 383 ? 163.191 140.805 136.996 1.00 102.38 ? 399 TYR A CG  1 
ATOM   2040  C  CD1 . TYR A 1 383 ? 162.057 141.377 136.437 1.00 102.38 ? 399 TYR A CD1 1 
ATOM   2041  C  CD2 . TYR A 1 383 ? 164.403 140.980 136.342 1.00 102.38 ? 399 TYR A CD2 1 
ATOM   2042  C  CE1 . TYR A 1 383 ? 162.127 142.103 135.264 1.00 102.38 ? 399 TYR A CE1 1 
ATOM   2043  C  CE2 . TYR A 1 383 ? 164.482 141.701 135.165 1.00 102.38 ? 399 TYR A CE2 1 
ATOM   2044  C  CZ  . TYR A 1 383 ? 163.341 142.260 134.631 1.00 102.38 ? 399 TYR A CZ  1 
ATOM   2045  O  OH  . TYR A 1 383 ? 163.413 142.978 133.460 1.00 102.38 ? 399 TYR A OH  1 
ATOM   2046  N  N   . LEU A 1 384 ? 161.901 140.388 141.496 1.00 89.03  ? 400 LEU A N   1 
ATOM   2047  C  CA  . LEU A 1 384 ? 161.536 139.738 142.747 1.00 89.03  ? 400 LEU A CA  1 
ATOM   2048  C  C   . LEU A 1 384 ? 160.407 138.759 142.458 1.00 89.03  ? 400 LEU A C   1 
ATOM   2049  O  O   . LEU A 1 384 ? 159.330 139.168 142.008 1.00 89.03  ? 400 LEU A O   1 
ATOM   2050  C  CB  . LEU A 1 384 ? 161.107 140.778 143.781 1.00 89.03  ? 400 LEU A CB  1 
ATOM   2051  C  CG  . LEU A 1 384 ? 161.678 140.633 145.186 1.00 89.03  ? 400 LEU A CG  1 
ATOM   2052  C  CD1 . LEU A 1 384 ? 163.178 140.793 145.118 1.00 89.03  ? 400 LEU A CD1 1 
ATOM   2053  C  CD2 . LEU A 1 384 ? 161.080 141.671 146.114 1.00 89.03  ? 400 LEU A CD2 1 
ATOM   2054  N  N   . LEU A 1 385 ? 160.652 137.474 142.707 1.00 87.34  ? 401 LEU A N   1 
ATOM   2055  C  CA  . LEU A 1 385 ? 159.769 136.405 142.262 1.00 87.34  ? 401 LEU A CA  1 
ATOM   2056  C  C   . LEU A 1 385 ? 159.207 135.650 143.457 1.00 87.34  ? 401 LEU A C   1 
ATOM   2057  O  O   . LEU A 1 385 ? 159.956 135.273 144.365 1.00 87.34  ? 401 LEU A O   1 
ATOM   2058  C  CB  . LEU A 1 385 ? 160.524 135.435 141.351 1.00 87.34  ? 401 LEU A CB  1 
ATOM   2059  C  CG  . LEU A 1 385 ? 161.187 136.026 140.108 1.00 87.34  ? 401 LEU A CG  1 
ATOM   2060  C  CD1 . LEU A 1 385 ? 162.521 135.350 139.845 1.00 87.34  ? 401 LEU A CD1 1 
ATOM   2061  C  CD2 . LEU A 1 385 ? 160.274 135.884 138.906 1.00 87.34  ? 401 LEU A CD2 1 
ATOM   2062  N  N   . GLY A 1 386 ? 157.895 135.414 143.442 1.00 94.54  ? 402 GLY A N   1 
ATOM   2063  C  CA  . GLY A 1 386 ? 157.274 134.578 144.451 1.00 94.54  ? 402 GLY A CA  1 
ATOM   2064  C  C   . GLY A 1 386 ? 157.328 135.168 145.849 1.00 94.54  ? 402 GLY A C   1 
ATOM   2065  O  O   . GLY A 1 386 ? 157.282 136.385 146.052 1.00 94.54  ? 402 GLY A O   1 
ATOM   2066  N  N   . GLY A 1 387 ? 157.423 134.278 146.832 1.00 101.87 ? 403 GLY A N   1 
ATOM   2067  C  CA  . GLY A 1 387 ? 157.470 134.686 148.220 1.00 101.87 ? 403 GLY A CA  1 
ATOM   2068  C  C   . GLY A 1 387 ? 156.137 134.528 148.916 1.00 101.87 ? 403 GLY A C   1 
ATOM   2069  O  O   . GLY A 1 387 ? 155.400 133.575 148.648 1.00 101.87 ? 403 GLY A O   1 
ATOM   2070  N  N   . GLU A 1 388 ? 155.820 135.449 149.819 1.00 109.46 ? 404 GLU A N   1 
ATOM   2071  C  CA  . GLU A 1 388 ? 154.567 135.430 150.555 1.00 109.46 ? 404 GLU A CA  1 
ATOM   2072  C  C   . GLU A 1 388 ? 153.936 136.808 150.466 1.00 109.46 ? 404 GLU A C   1 
ATOM   2073  O  O   . GLU A 1 388 ? 154.639 137.823 150.468 1.00 109.46 ? 404 GLU A O   1 
ATOM   2074  C  CB  . GLU A 1 388 ? 154.781 135.031 152.020 1.00 109.46 ? 404 GLU A CB  1 
ATOM   2075  C  CG  . GLU A 1 388 ? 155.507 133.708 152.196 1.00 109.46 ? 404 GLU A CG  1 
ATOM   2076  C  CD  . GLU A 1 388 ? 154.837 132.810 153.216 1.00 109.46 ? 404 GLU A CD  1 
ATOM   2077  O  OE1 . GLU A 1 388 ? 154.658 131.608 152.925 1.00 109.46 ? 404 GLU A OE1 1 
ATOM   2078  O  OE2 . GLU A 1 388 ? 154.490 133.302 154.307 1.00 109.46 ? 404 GLU A OE2 1 
ATOM   2079  N  N   . GLU A 1 389 ? 152.610 136.842 150.391 1.00 113.67 ? 405 GLU A N   1 
ATOM   2080  C  CA  . GLU A 1 389 ? 151.888 138.098 150.277 1.00 113.67 ? 405 GLU A CA  1 
ATOM   2081  C  C   . GLU A 1 389 ? 150.745 138.124 151.282 1.00 113.67 ? 405 GLU A C   1 
ATOM   2082  O  O   . GLU A 1 389 ? 150.261 137.081 151.731 1.00 113.67 ? 405 GLU A O   1 
ATOM   2083  C  CB  . GLU A 1 389 ? 151.363 138.314 148.852 1.00 113.67 ? 405 GLU A CB  1 
ATOM   2084  C  CG  . GLU A 1 389 ? 150.384 137.261 148.371 1.00 113.67 ? 405 GLU A CG  1 
ATOM   2085  C  CD  . GLU A 1 389 ? 149.783 137.611 147.024 1.00 113.67 ? 405 GLU A CD  1 
ATOM   2086  O  OE1 . GLU A 1 389 ? 150.219 138.614 146.427 1.00 113.67 ? 405 GLU A OE1 1 
ATOM   2087  O  OE2 . GLU A 1 389 ? 148.867 136.897 146.567 1.00 113.67 ? 405 GLU A OE2 1 
ATOM   2088  N  N   . ASN A 1 390 ? 150.318 139.338 151.629 1.00 124.02 ? 406 ASN A N   1 
ATOM   2089  C  CA  . ASN A 1 390 ? 149.293 139.516 152.651 1.00 124.02 ? 406 ASN A CA  1 
ATOM   2090  C  C   . ASN A 1 390 ? 147.996 138.829 152.244 1.00 124.02 ? 406 ASN A C   1 
ATOM   2091  O  O   . ASN A 1 390 ? 147.615 138.830 151.071 1.00 124.02 ? 406 ASN A O   1 
ATOM   2092  C  CB  . ASN A 1 390 ? 149.048 141.004 152.897 1.00 124.02 ? 406 ASN A CB  1 
ATOM   2093  C  CG  . ASN A 1 390 ? 149.840 141.535 154.071 1.00 124.02 ? 406 ASN A CG  1 
ATOM   2094  O  OD1 . ASN A 1 390 ? 150.566 142.521 153.948 1.00 124.02 ? 406 ASN A OD1 1 
ATOM   2095  N  ND2 . ASN A 1 390 ? 149.707 140.882 155.219 1.00 124.02 ? 406 ASN A ND2 1 
ATOM   2096  N  N   . ASP A 1 391 ? 147.313 138.242 153.225 1.00 123.27 ? 407 ASP A N   1 
ATOM   2097  C  CA  . ASP A 1 391 ? 146.050 137.569 152.971 1.00 123.27 ? 407 ASP A CA  1 
ATOM   2098  C  C   . ASP A 1 391 ? 145.283 137.510 154.285 1.00 123.27 ? 407 ASP A C   1 
ATOM   2099  O  O   . ASP A 1 391 ? 145.881 137.322 155.350 1.00 123.27 ? 407 ASP A O   1 
ATOM   2100  C  CB  . ASP A 1 391 ? 146.281 136.159 152.408 1.00 123.27 ? 407 ASP A CB  1 
ATOM   2101  C  CG  . ASP A 1 391 ? 144.999 135.364 152.261 1.00 123.27 ? 407 ASP A CG  1 
ATOM   2102  O  OD1 . ASP A 1 391 ? 143.914 135.979 152.196 1.00 123.27 ? 407 ASP A OD1 1 
ATOM   2103  O  OD2 . ASP A 1 391 ? 145.085 134.122 152.148 1.00 123.27 ? 407 ASP A OD2 1 
ATOM   2104  N  N   . LEU A 1 392 ? 143.965 137.700 154.198 1.00 113.51 ? 408 LEU A N   1 
ATOM   2105  C  CA  . LEU A 1 392 ? 143.042 137.597 155.327 1.00 113.51 ? 408 LEU A CA  1 
ATOM   2106  C  C   . LEU A 1 392 ? 143.302 138.654 156.395 1.00 113.51 ? 408 LEU A C   1 
ATOM   2107  O  O   . LEU A 1 392 ? 142.861 138.500 157.540 1.00 113.51 ? 408 LEU A O   1 
ATOM   2108  C  CB  . LEU A 1 392 ? 143.067 136.194 155.948 1.00 113.51 ? 408 LEU A CB  1 
ATOM   2109  C  CG  . LEU A 1 392 ? 142.714 135.048 154.996 1.00 113.51 ? 408 LEU A CG  1 
ATOM   2110  C  CD1 . LEU A 1 392 ? 142.882 133.704 155.678 1.00 113.51 ? 408 LEU A CD1 1 
ATOM   2111  C  CD2 . LEU A 1 392 ? 141.306 135.207 154.450 1.00 113.51 ? 408 LEU A CD2 1 
ATOM   2112  N  N   . ASP A 1 393 ? 144.058 139.702 156.051 1.00 108.26 ? 409 ASP A N   1 
ATOM   2113  C  CA  . ASP A 1 393 ? 144.267 140.883 156.889 1.00 108.26 ? 409 ASP A CA  1 
ATOM   2114  C  C   . ASP A 1 393 ? 145.187 140.594 158.069 1.00 108.26 ? 409 ASP A C   1 
ATOM   2115  O  O   . ASP A 1 393 ? 145.557 141.510 158.810 1.00 108.26 ? 409 ASP A O   1 
ATOM   2116  C  CB  . ASP A 1 393 ? 142.935 141.463 157.384 1.00 108.26 ? 409 ASP A CB  1 
ATOM   2117  C  CG  . ASP A 1 393 ? 141.831 141.370 156.346 1.00 108.26 ? 409 ASP A CG  1 
ATOM   2118  O  OD1 . ASP A 1 393 ? 142.020 141.895 155.229 1.00 108.26 ? 409 ASP A OD1 1 
ATOM   2119  O  OD2 . ASP A 1 393 ? 140.780 140.767 156.645 1.00 108.26 ? 409 ASP A OD2 1 
ATOM   2120  N  N   . PHE A 1 394 ? 145.570 139.331 158.252 1.00 100.49 ? 410 PHE A N   1 
ATOM   2121  C  CA  . PHE A 1 394 ? 146.454 138.971 159.353 1.00 100.49 ? 410 PHE A CA  1 
ATOM   2122  C  C   . PHE A 1 394 ? 147.514 137.947 158.988 1.00 100.49 ? 410 PHE A C   1 
ATOM   2123  O  O   . PHE A 1 394 ? 148.464 137.786 159.760 1.00 100.49 ? 410 PHE A O   1 
ATOM   2124  C  CB  . PHE A 1 394 ? 145.642 138.435 160.542 1.00 100.49 ? 410 PHE A CB  1 
ATOM   2125  C  CG  . PHE A 1 394 ? 144.569 139.371 161.018 1.00 100.49 ? 410 PHE A CG  1 
ATOM   2126  C  CD1 . PHE A 1 394 ? 144.872 140.418 161.871 1.00 100.49 ? 410 PHE A CD1 1 
ATOM   2127  C  CD2 . PHE A 1 394 ? 143.255 139.198 160.620 1.00 100.49 ? 410 PHE A CD2 1 
ATOM   2128  C  CE1 . PHE A 1 394 ? 143.884 141.278 162.311 1.00 100.49 ? 410 PHE A CE1 1 
ATOM   2129  C  CE2 . PHE A 1 394 ? 142.264 140.054 161.057 1.00 100.49 ? 410 PHE A CE2 1 
ATOM   2130  C  CZ  . PHE A 1 394 ? 142.579 141.095 161.904 1.00 100.49 ? 410 PHE A CZ  1 
ATOM   2131  N  N   . PHE A 1 395 ? 147.400 137.251 157.859 1.00 97.94  ? 411 PHE A N   1 
ATOM   2132  C  CA  . PHE A 1 395 ? 148.309 136.150 157.572 1.00 97.94  ? 411 PHE A CA  1 
ATOM   2133  C  C   . PHE A 1 395 ? 148.963 136.322 156.210 1.00 97.94  ? 411 PHE A C   1 
ATOM   2134  O  O   . PHE A 1 395 ? 148.784 137.350 155.550 1.00 97.94  ? 411 PHE A O   1 
ATOM   2135  C  CB  . PHE A 1 395 ? 147.574 134.810 157.635 1.00 97.94  ? 411 PHE A CB  1 
ATOM   2136  C  CG  . PHE A 1 395 ? 146.755 134.626 158.876 1.00 97.94  ? 411 PHE A CG  1 
ATOM   2137  C  CD1 . PHE A 1 395 ? 147.338 134.156 160.040 1.00 97.94  ? 411 PHE A CD1 1 
ATOM   2138  C  CD2 . PHE A 1 395 ? 145.402 134.917 158.880 1.00 97.94  ? 411 PHE A CD2 1 
ATOM   2139  C  CE1 . PHE A 1 395 ? 146.589 133.982 161.184 1.00 97.94  ? 411 PHE A CE1 1 
ATOM   2140  C  CE2 . PHE A 1 395 ? 144.649 134.746 160.023 1.00 97.94  ? 411 PHE A CE2 1 
ATOM   2141  C  CZ  . PHE A 1 395 ? 145.243 134.277 161.176 1.00 97.94  ? 411 PHE A CZ  1 
ATOM   2142  N  N   . THR A 1 396 ? 149.706 135.312 155.775 1.00 99.63  ? 412 THR A N   1 
ATOM   2143  C  CA  . THR A 1 396 ? 150.403 135.356 154.503 1.00 99.63  ? 412 THR A CA  1 
ATOM   2144  C  C   . THR A 1 396 ? 150.076 134.105 153.705 1.00 99.63  ? 412 THR A C   1 
ATOM   2145  O  O   . THR A 1 396 ? 149.898 133.018 154.262 1.00 99.63  ? 412 THR A O   1 
ATOM   2146  C  CB  . THR A 1 396 ? 151.925 135.467 154.688 1.00 99.63  ? 412 THR A CB  1 
ATOM   2147  O  OG1 . THR A 1 396 ? 152.382 134.416 155.548 1.00 99.63  ? 412 THR A OG1 1 
ATOM   2148  C  CG2 . THR A 1 396 ? 152.295 136.812 155.297 1.00 99.63  ? 412 THR A CG2 1 
ATOM   2149  N  N   . LYS A 1 397 ? 149.997 134.275 152.392 1.00 101.36 ? 413 LYS A N   1 
ATOM   2150  C  CA  . LYS A 1 397 ? 149.772 133.184 151.466 1.00 101.36 ? 413 LYS A CA  1 
ATOM   2151  C  C   . LYS A 1 397 ? 150.924 133.108 150.473 1.00 101.36 ? 413 LYS A C   1 
ATOM   2152  O  O   . LYS A 1 397 ? 151.568 134.124 150.188 1.00 101.36 ? 413 LYS A O   1 
ATOM   2153  C  CB  . LYS A 1 397 ? 148.447 133.355 150.711 1.00 101.36 ? 413 LYS A CB  1 
ATOM   2154  C  CG  . LYS A 1 397 ? 148.368 134.601 149.848 1.00 101.36 ? 413 LYS A CG  1 
ATOM   2155  C  CD  . LYS A 1 397 ? 147.118 134.584 148.984 1.00 101.36 ? 413 LYS A CD  1 
ATOM   2156  C  CE  . LYS A 1 397 ? 146.624 135.991 148.695 1.00 101.36 ? 413 LYS A CE  1 
ATOM   2157  N  NZ  . LYS A 1 397 ? 145.545 135.995 147.670 1.00 101.36 ? 413 LYS A NZ  1 
ATOM   2158  N  N   . PRO A 1 398 ? 151.223 131.913 149.947 1.00 99.91  ? 414 PRO A N   1 
ATOM   2159  C  CA  . PRO A 1 398 ? 152.264 131.799 148.917 1.00 99.91  ? 414 PRO A CA  1 
ATOM   2160  C  C   . PRO A 1 398 ? 152.024 132.742 147.752 1.00 99.91  ? 414 PRO A C   1 
ATOM   2161  O  O   . PRO A 1 398 ? 151.036 132.605 147.024 1.00 99.91  ? 414 PRO A O   1 
ATOM   2162  C  CB  . PRO A 1 398 ? 152.165 130.332 148.481 1.00 99.91  ? 414 PRO A CB  1 
ATOM   2163  C  CG  . PRO A 1 398 ? 151.603 129.630 149.664 1.00 99.91  ? 414 PRO A CG  1 
ATOM   2164  C  CD  . PRO A 1 398 ? 150.662 130.602 150.316 1.00 99.91  ? 414 PRO A CD  1 
ATOM   2165  N  N   . SER A 1 399 ? 152.921 133.705 147.569 1.00 105.85 ? 415 SER A N   1 
ATOM   2166  C  CA  . SER A 1 399 ? 152.756 134.674 146.502 1.00 105.85 ? 415 SER A CA  1 
ATOM   2167  C  C   . SER A 1 399 ? 153.249 134.101 145.181 1.00 105.85 ? 415 SER A C   1 
ATOM   2168  O  O   . SER A 1 399 ? 154.153 133.263 145.138 1.00 105.85 ? 415 SER A O   1 
ATOM   2169  C  CB  . SER A 1 399 ? 153.513 135.962 146.823 1.00 105.85 ? 415 SER A CB  1 
ATOM   2170  O  OG  . SER A 1 399 ? 153.386 136.903 145.771 1.00 105.85 ? 415 SER A OG  1 
ATOM   2171  N  N   . ARG A 1 400 ? 152.640 134.570 144.096 1.00 111.58 ? 416 ARG A N   1 
ATOM   2172  C  CA  . ARG A 1 400 ? 153.030 134.189 142.747 1.00 111.58 ? 416 ARG A CA  1 
ATOM   2173  C  C   . ARG A 1 400 ? 153.176 135.415 141.851 1.00 111.58 ? 416 ARG A C   1 
ATOM   2174  O  O   . ARG A 1 400 ? 152.921 135.349 140.645 1.00 111.58 ? 416 ARG A O   1 
ATOM   2175  C  CB  . ARG A 1 400 ? 152.034 133.181 142.174 1.00 111.58 ? 416 ARG A CB  1 
ATOM   2176  C  CG  . ARG A 1 400 ? 150.599 133.676 142.148 1.00 111.58 ? 416 ARG A CG  1 
ATOM   2177  C  CD  . ARG A 1 400 ? 149.640 132.622 141.606 1.00 111.58 ? 416 ARG A CD  1 
ATOM   2178  N  NE  . ARG A 1 400 ? 149.532 131.458 142.477 1.00 111.58 ? 416 ARG A NE  1 
ATOM   2179  C  CZ  . ARG A 1 400 ? 149.686 130.204 142.073 1.00 111.58 ? 416 ARG A CZ  1 
ATOM   2180  N  NH1 . ARG A 1 400 ? 149.927 129.912 140.805 1.00 111.58 ? 416 ARG A NH1 1 
ATOM   2181  N  NH2 . ARG A 1 400 ? 149.584 129.219 142.960 1.00 111.58 ? 416 ARG A NH2 1 
ATOM   2182  N  N   . LEU A 1 401 ? 153.587 136.538 142.432 1.00 104.14 ? 417 LEU A N   1 
ATOM   2183  C  CA  . LEU A 1 401 ? 153.766 137.794 141.721 1.00 104.14 ? 417 LEU A CA  1 
ATOM   2184  C  C   . LEU A 1 401 ? 155.208 137.945 141.243 1.00 104.14 ? 417 LEU A C   1 
ATOM   2185  O  O   . LEU A 1 401 ? 156.127 137.293 141.743 1.00 104.14 ? 417 LEU A O   1 
ATOM   2186  C  CB  . LEU A 1 401 ? 153.389 138.980 142.609 1.00 104.14 ? 417 LEU A CB  1 
ATOM   2187  C  CG  . LEU A 1 401 ? 151.910 139.163 142.949 1.00 104.14 ? 417 LEU A CG  1 
ATOM   2188  C  CD1 . LEU A 1 401 ? 151.751 140.172 144.073 1.00 104.14 ? 417 LEU A CD1 1 
ATOM   2189  C  CD2 . LEU A 1 401 ? 151.125 139.595 141.723 1.00 104.14 ? 417 LEU A CD2 1 
ATOM   2190  N  N   . ILE A 1 402 ? 155.395 138.821 140.258 1.00 101.48 ? 418 ILE A N   1 
ATOM   2191  C  CA  . ILE A 1 402 ? 156.718 139.206 139.780 1.00 101.48 ? 418 ILE A CA  1 
ATOM   2192  C  C   . ILE A 1 402 ? 156.819 140.722 139.856 1.00 101.48 ? 418 ILE A C   1 
ATOM   2193  O  O   . ILE A 1 402 ? 156.083 141.430 139.157 1.00 101.48 ? 418 ILE A O   1 
ATOM   2194  C  CB  . ILE A 1 402 ? 156.983 138.723 138.344 1.00 101.48 ? 418 ILE A CB  1 
ATOM   2195  C  CG1 . ILE A 1 402 ? 156.621 137.247 138.194 1.00 101.48 ? 418 ILE A CG1 1 
ATOM   2196  C  CG2 . ILE A 1 402 ? 158.437 138.953 137.967 1.00 101.48 ? 418 ILE A CG2 1 
ATOM   2197  C  CD1 . ILE A 1 402 ? 155.495 136.993 137.218 1.00 101.48 ? 418 ILE A CD1 1 
ATOM   2198  N  N   . GLN A 1 403 ? 157.720 141.220 140.698 1.00 95.73  ? 419 GLN A N   1 
ATOM   2199  C  CA  . GLN A 1 403 ? 157.960 142.649 140.823 1.00 95.73  ? 419 GLN A CA  1 
ATOM   2200  C  C   . GLN A 1 403 ? 159.259 143.030 140.121 1.00 95.73  ? 419 GLN A C   1 
ATOM   2201  O  O   . GLN A 1 403 ? 160.208 142.245 140.071 1.00 95.73  ? 419 GLN A O   1 
ATOM   2202  C  CB  . GLN A 1 403 ? 158.020 143.062 142.294 1.00 95.73  ? 419 GLN A CB  1 
ATOM   2203  C  CG  . GLN A 1 403 ? 156.831 142.590 143.111 1.00 95.73  ? 419 GLN A CG  1 
ATOM   2204  C  CD  . GLN A 1 403 ? 156.568 143.464 144.318 1.00 95.73  ? 419 GLN A CD  1 
ATOM   2205  O  OE1 . GLN A 1 403 ? 156.452 144.683 144.202 1.00 95.73  ? 419 GLN A OE1 1 
ATOM   2206  N  NE2 . GLN A 1 403 ? 156.475 142.844 145.488 1.00 95.73  ? 419 GLN A NE2 1 
ATOM   2207  N  N   . CYS A 1 404 ? 159.296 144.249 139.586 1.00 114.98 ? 420 CYS A N   1 
ATOM   2208  C  CA  . CYS A 1 404 ? 160.430 144.742 138.815 1.00 114.98 ? 420 CYS A CA  1 
ATOM   2209  C  C   . CYS A 1 404 ? 160.883 146.073 139.389 1.00 114.98 ? 420 CYS A C   1 
ATOM   2210  O  O   . CYS A 1 404 ? 160.099 147.028 139.443 1.00 114.98 ? 420 CYS A O   1 
ATOM   2211  C  CB  . CYS A 1 404 ? 160.066 144.894 137.337 1.00 114.98 ? 420 CYS A CB  1 
ATOM   2212  S  SG  . CYS A 1 404 ? 159.199 143.476 136.657 1.00 114.98 ? 420 CYS A SG  1 
ATOM   2213  N  N   . PHE A 1 405 ? 162.140 146.128 139.818 1.00 105.76 ? 421 PHE A N   1 
ATOM   2214  C  CA  . PHE A 1 405 ? 162.783 147.337 140.316 1.00 105.76 ? 421 PHE A CA  1 
ATOM   2215  C  C   . PHE A 1 405 ? 163.807 147.771 139.274 1.00 105.76 ? 421 PHE A C   1 
ATOM   2216  O  O   . PHE A 1 405 ? 164.848 147.125 139.112 1.00 105.76 ? 421 PHE A O   1 
ATOM   2217  C  CB  . PHE A 1 405 ? 163.439 147.082 141.672 1.00 105.76 ? 421 PHE A CB  1 
ATOM   2218  C  CG  . PHE A 1 405 ? 163.840 148.331 142.402 1.00 105.76 ? 421 PHE A CG  1 
ATOM   2219  C  CD1 . PHE A 1 405 ? 165.022 148.983 142.094 1.00 105.76 ? 421 PHE A CD1 1 
ATOM   2220  C  CD2 . PHE A 1 405 ? 163.041 148.847 143.408 1.00 105.76 ? 421 PHE A CD2 1 
ATOM   2221  C  CE1 . PHE A 1 405 ? 165.395 150.129 142.767 1.00 105.76 ? 421 PHE A CE1 1 
ATOM   2222  C  CE2 . PHE A 1 405 ? 163.409 149.992 144.086 1.00 105.76 ? 421 PHE A CE2 1 
ATOM   2223  C  CZ  . PHE A 1 405 ? 164.588 150.634 143.765 1.00 105.76 ? 421 PHE A CZ  1 
ATOM   2224  N  N   . ASP A 1 406 ? 163.499 148.849 138.558 1.00 113.78 ? 422 ASP A N   1 
ATOM   2225  C  CA  . ASP A 1 406 ? 164.430 149.468 137.624 1.00 113.78 ? 422 ASP A CA  1 
ATOM   2226  C  C   . ASP A 1 406 ? 165.415 150.295 138.438 1.00 113.78 ? 422 ASP A C   1 
ATOM   2227  O  O   . ASP A 1 406 ? 165.034 151.286 139.074 1.00 113.78 ? 422 ASP A O   1 
ATOM   2228  C  CB  . ASP A 1 406 ? 163.674 150.325 136.612 1.00 113.78 ? 422 ASP A CB  1 
ATOM   2229  C  CG  . ASP A 1 406 ? 164.572 150.895 135.521 1.00 113.78 ? 422 ASP A CG  1 
ATOM   2230  O  OD1 . ASP A 1 406 ? 165.788 151.071 135.748 1.00 113.78 ? 422 ASP A OD1 1 
ATOM   2231  O  OD2 . ASP A 1 406 ? 164.050 151.173 134.421 1.00 113.78 ? 422 ASP A OD2 1 
ATOM   2232  N  N   . THR A 1 407 ? 166.681 149.872 138.426 1.00 104.67 ? 423 THR A N   1 
ATOM   2233  C  CA  . THR A 1 407 ? 167.711 150.513 139.234 1.00 104.67 ? 423 THR A CA  1 
ATOM   2234  C  C   . THR A 1 407 ? 168.168 151.834 138.628 1.00 104.67 ? 423 THR A C   1 
ATOM   2235  O  O   . THR A 1 407 ? 168.462 152.784 139.362 1.00 104.67 ? 423 THR A O   1 
ATOM   2236  C  CB  . THR A 1 407 ? 168.901 149.567 139.400 1.00 104.67 ? 423 THR A CB  1 
ATOM   2237  O  OG1 . THR A 1 407 ? 168.426 148.232 139.614 1.00 104.67 ? 423 THR A OG1 1 
ATOM   2238  C  CG2 . THR A 1 407 ? 169.754 149.984 140.573 1.00 104.67 ? 423 THR A CG2 1 
ATOM   2239  N  N   . GLU A 1 408 ? 168.248 151.909 137.297 1.00 111.80 ? 424 GLU A N   1 
ATOM   2240  C  CA  . GLU A 1 408 ? 168.659 153.155 136.658 1.00 111.80 ? 424 GLU A CA  1 
ATOM   2241  C  C   . GLU A 1 408 ? 167.673 154.276 136.961 1.00 111.80 ? 424 GLU A C   1 
ATOM   2242  O  O   . GLU A 1 408 ? 168.077 155.406 137.257 1.00 111.80 ? 424 GLU A O   1 
ATOM   2243  C  CB  . GLU A 1 408 ? 168.796 152.952 135.149 1.00 111.80 ? 424 GLU A CB  1 
ATOM   2244  N  N   . THR A 1 409 ? 166.376 153.981 136.893 1.00 112.73 ? 425 THR A N   1 
ATOM   2245  C  CA  . THR A 1 409 ? 165.340 154.949 137.222 1.00 112.73 ? 425 THR A CA  1 
ATOM   2246  C  C   . THR A 1 409 ? 164.854 154.818 138.660 1.00 112.73 ? 425 THR A C   1 
ATOM   2247  O  O   . THR A 1 409 ? 164.172 155.724 139.153 1.00 112.73 ? 425 THR A O   1 
ATOM   2248  C  CB  . THR A 1 409 ? 164.156 154.794 136.255 1.00 112.73 ? 425 THR A CB  1 
ATOM   2249  O  OG1 . THR A 1 409 ? 164.651 154.632 134.921 1.00 112.73 ? 425 THR A OG1 1 
ATOM   2250  C  CG2 . THR A 1 409 ? 163.257 156.023 136.287 1.00 112.73 ? 425 THR A CG2 1 
ATOM   2251  N  N   . ASP A 1 410 ? 165.215 153.733 139.350 1.00 106.74 ? 426 ASP A N   1 
ATOM   2252  C  CA  . ASP A 1 410 ? 164.802 153.494 140.734 1.00 106.74 ? 426 ASP A CA  1 
ATOM   2253  C  C   . ASP A 1 410 ? 163.279 153.514 140.862 1.00 106.74 ? 426 ASP A C   1 
ATOM   2254  O  O   . ASP A 1 410 ? 162.710 154.251 141.669 1.00 106.74 ? 426 ASP A O   1 
ATOM   2255  C  CB  . ASP A 1 410 ? 165.450 154.504 141.686 1.00 106.74 ? 426 ASP A CB  1 
ATOM   2256  N  N   . LYS A 1 411 ? 162.616 152.694 140.048 1.00 113.51 ? 427 LYS A N   1 
ATOM   2257  C  CA  . LYS A 1 411 ? 161.159 152.658 140.009 1.00 113.51 ? 427 LYS A CA  1 
ATOM   2258  C  C   . LYS A 1 411 ? 160.673 151.217 140.061 1.00 113.51 ? 427 LYS A C   1 
ATOM   2259  O  O   . LYS A 1 411 ? 161.252 150.340 139.423 1.00 113.51 ? 427 LYS A O   1 
ATOM   2260  C  CB  . LYS A 1 411 ? 160.630 153.352 138.745 1.00 113.51 ? 427 LYS A CB  1 
ATOM   2261  C  CG  . LYS A 1 411 ? 159.128 153.220 138.526 1.00 113.51 ? 427 LYS A CG  1 
ATOM   2262  C  CD  . LYS A 1 411 ? 158.634 153.982 137.293 1.00 113.51 ? 427 LYS A CD  1 
ATOM   2263  C  CE  . LYS A 1 411 ? 159.508 155.175 136.907 1.00 113.51 ? 427 LYS A CE  1 
ATOM   2264  N  NZ  . LYS A 1 411 ? 159.671 156.190 137.994 1.00 113.51 ? 427 LYS A NZ  1 
ATOM   2265  N  N   . CYS A 1 412 ? 159.592 150.977 140.797 1.00 112.52 ? 428 CYS A N   1 
ATOM   2266  C  CA  . CYS A 1 412 ? 159.059 149.634 140.981 1.00 112.52 ? 428 CYS A CA  1 
ATOM   2267  C  C   . CYS A 1 412 ? 157.705 149.490 140.301 1.00 112.52 ? 428 CYS A C   1 
ATOM   2268  O  O   . CYS A 1 412 ? 156.886 150.414 140.323 1.00 112.52 ? 428 CYS A O   1 
ATOM   2269  C  CB  . CYS A 1 412 ? 158.922 149.292 142.465 1.00 112.52 ? 428 CYS A CB  1 
ATOM   2270  S  SG  . CYS A 1 412 ? 158.227 147.653 142.759 1.00 112.52 ? 428 CYS A SG  1 
ATOM   2271  N  N   . HIS A 1 413 ? 157.477 148.323 139.700 1.00 109.03 ? 429 HIS A N   1 
ATOM   2272  C  CA  . HIS A 1 413 ? 156.186 148.017 139.095 1.00 109.03 ? 429 HIS A CA  1 
ATOM   2273  C  C   . HIS A 1 413 ? 155.969 146.510 139.065 1.00 109.03 ? 429 HIS A C   1 
ATOM   2274  O  O   . HIS A 1 413 ? 156.919 145.732 138.964 1.00 109.03 ? 429 HIS A O   1 
ATOM   2275  C  CB  . HIS A 1 413 ? 156.080 148.603 137.681 1.00 109.03 ? 429 HIS A CB  1 
ATOM   2276  C  CG  . HIS A 1 413 ? 156.616 147.705 136.609 1.00 109.03 ? 429 HIS A CG  1 
ATOM   2277  N  ND1 . HIS A 1 413 ? 157.932 147.735 136.203 1.00 109.03 ? 429 HIS A ND1 1 
ATOM   2278  C  CD2 . HIS A 1 413 ? 156.010 146.761 135.850 1.00 109.03 ? 429 HIS A CD2 1 
ATOM   2279  C  CE1 . HIS A 1 413 ? 158.117 146.844 135.245 1.00 109.03 ? 429 HIS A CE1 1 
ATOM   2280  N  NE2 . HIS A 1 413 ? 156.966 146.239 135.013 1.00 109.03 ? 429 HIS A NE2 1 
ATOM   2281  N  N   . VAL A 1 414 ? 154.703 146.107 139.141 1.00 104.01 ? 430 VAL A N   1 
ATOM   2282  C  CA  . VAL A 1 414 ? 154.314 144.700 139.171 1.00 104.01 ? 430 VAL A CA  1 
ATOM   2283  C  C   . VAL A 1 414 ? 153.907 144.261 137.773 1.00 104.01 ? 430 VAL A C   1 
ATOM   2284  O  O   . VAL A 1 414 ? 153.186 144.978 137.069 1.00 104.01 ? 430 VAL A O   1 
ATOM   2285  C  CB  . VAL A 1 414 ? 153.174 144.455 140.178 1.00 104.01 ? 430 VAL A CB  1 
ATOM   2286  C  CG1 . VAL A 1 414 ? 152.888 142.969 140.304 1.00 104.01 ? 430 VAL A CG1 1 
ATOM   2287  C  CG2 . VAL A 1 414 ? 153.532 145.037 141.528 1.00 104.01 ? 430 VAL A CG2 1 
ATOM   2288  N  N   . LYS A 1 415 ? 154.376 143.082 137.366 1.00 102.52 ? 431 LYS A N   1 
ATOM   2289  C  CA  . LYS A 1 415 ? 154.034 142.555 136.055 1.00 102.52 ? 431 LYS A CA  1 
ATOM   2290  C  C   . LYS A 1 415 ? 152.533 142.280 135.968 1.00 102.52 ? 431 LYS A C   1 
ATOM   2291  O  O   . LYS A 1 415 ? 151.888 141.975 136.976 1.00 102.52 ? 431 LYS A O   1 
ATOM   2292  C  CB  . LYS A 1 415 ? 154.814 141.273 135.771 1.00 102.52 ? 431 LYS A CB  1 
ATOM   2293  C  CG  . LYS A 1 415 ? 156.319 141.449 135.712 1.00 102.52 ? 431 LYS A CG  1 
ATOM   2294  C  CD  . LYS A 1 415 ? 156.720 142.232 134.473 1.00 102.52 ? 431 LYS A CD  1 
ATOM   2295  C  CE  . LYS A 1 415 ? 158.030 141.721 133.895 1.00 102.52 ? 431 LYS A CE  1 
ATOM   2296  N  NZ  . LYS A 1 415 ? 158.553 142.612 132.825 1.00 102.52 ? 431 LYS A NZ  1 
ATOM   2297  N  N   . PRO A 1 416 ? 151.950 142.380 134.771 1.00 105.86 ? 432 PRO A N   1 
ATOM   2298  C  CA  . PRO A 1 416 ? 150.514 142.122 134.614 1.00 105.86 ? 432 PRO A CA  1 
ATOM   2299  C  C   . PRO A 1 416 ? 150.146 140.649 134.534 1.00 105.86 ? 432 PRO A C   1 
ATOM   2300  O  O   . PRO A 1 416 ? 148.952 140.335 134.480 1.00 105.86 ? 432 PRO A O   1 
ATOM   2301  C  CB  . PRO A 1 416 ? 150.174 142.839 133.293 1.00 105.86 ? 432 PRO A CB  1 
ATOM   2302  C  CG  . PRO A 1 416 ? 151.424 143.593 132.891 1.00 105.86 ? 432 PRO A CG  1 
ATOM   2303  C  CD  . PRO A 1 416 ? 152.554 142.866 133.523 1.00 105.86 ? 432 PRO A CD  1 
ATOM   2304  N  N   . TYR A 1 417 ? 151.117 139.743 134.527 1.00 113.87 ? 433 TYR A N   1 
ATOM   2305  C  CA  . TYR A 1 417 ? 150.852 138.313 134.448 1.00 113.87 ? 433 TYR A CA  1 
ATOM   2306  C  C   . TYR A 1 417 ? 151.336 137.635 135.727 1.00 113.87 ? 433 TYR A C   1 
ATOM   2307  O  O   . TYR A 1 417 ? 151.817 138.284 136.659 1.00 113.87 ? 433 TYR A O   1 
ATOM   2308  C  CB  . TYR A 1 417 ? 151.508 137.693 133.211 1.00 113.87 ? 433 TYR A CB  1 
ATOM   2309  C  CG  . TYR A 1 417 ? 152.921 138.155 132.938 1.00 113.87 ? 433 TYR A CG  1 
ATOM   2310  C  CD1 . TYR A 1 417 ? 154.007 137.486 133.485 1.00 113.87 ? 433 TYR A CD1 1 
ATOM   2311  C  CD2 . TYR A 1 417 ? 153.169 139.253 132.127 1.00 113.87 ? 433 TYR A CD2 1 
ATOM   2312  C  CE1 . TYR A 1 417 ? 155.300 137.898 133.234 1.00 113.87 ? 433 TYR A CE1 1 
ATOM   2313  C  CE2 . TYR A 1 417 ? 154.459 139.676 131.874 1.00 113.87 ? 433 TYR A CE2 1 
ATOM   2314  C  CZ  . TYR A 1 417 ? 155.519 138.993 132.428 1.00 113.87 ? 433 TYR A CZ  1 
ATOM   2315  O  OH  . TYR A 1 417 ? 156.805 139.406 132.175 1.00 113.87 ? 433 TYR A OH  1 
ATOM   2316  N  N   . VAL A 1 418 ? 151.199 136.310 135.766 1.00 112.70 ? 434 VAL A N   1 
ATOM   2317  C  CA  . VAL A 1 418 ? 151.342 135.557 137.002 1.00 112.70 ? 434 VAL A CA  1 
ATOM   2318  C  C   . VAL A 1 418 ? 152.354 134.433 136.810 1.00 112.70 ? 434 VAL A C   1 
ATOM   2319  O  O   . VAL A 1 418 ? 152.618 133.982 135.693 1.00 112.70 ? 434 VAL A O   1 
ATOM   2320  C  CB  . VAL A 1 418 ? 149.982 134.997 137.471 1.00 112.70 ? 434 VAL A CB  1 
ATOM   2321  C  CG1 . VAL A 1 418 ? 149.671 133.666 136.792 1.00 112.70 ? 434 VAL A CG1 1 
ATOM   2322  C  CG2 . VAL A 1 418 ? 149.940 134.890 138.972 1.00 112.70 ? 434 VAL A CG2 1 
ATOM   2323  N  N   . LEU A 1 419 ? 152.940 133.991 137.934 1.00 100.84 ? 435 LEU A N   1 
ATOM   2324  C  CA  . LEU A 1 419 ? 153.906 132.903 137.935 1.00 100.84 ? 435 LEU A CA  1 
ATOM   2325  C  C   . LEU A 1 419 ? 153.197 131.551 137.854 1.00 100.84 ? 435 LEU A C   1 
ATOM   2326  O  O   . LEU A 1 419 ? 152.048 131.420 138.284 1.00 100.84 ? 435 LEU A O   1 
ATOM   2327  C  CB  . LEU A 1 419 ? 154.763 132.952 139.196 1.00 100.84 ? 435 LEU A CB  1 
ATOM   2328  C  CG  . LEU A 1 419 ? 156.015 133.828 139.164 1.00 100.84 ? 435 LEU A CG  1 
ATOM   2329  C  CD1 . LEU A 1 419 ? 156.537 134.064 140.572 1.00 100.84 ? 435 LEU A CD1 1 
ATOM   2330  C  CD2 . LEU A 1 419 ? 157.088 133.202 138.291 1.00 100.84 ? 435 LEU A CD2 1 
ATOM   2331  N  N   . PRO A 1 420 ? 153.857 130.534 137.289 1.00 102.74 ? 436 PRO A N   1 
ATOM   2332  C  CA  . PRO A 1 420 ? 153.226 129.203 137.242 1.00 102.74 ? 436 PRO A CA  1 
ATOM   2333  C  C   . PRO A 1 420 ? 152.882 128.635 138.609 1.00 102.74 ? 436 PRO A C   1 
ATOM   2334  O  O   . PRO A 1 420 ? 151.842 127.982 138.756 1.00 102.74 ? 436 PRO A O   1 
ATOM   2335  C  CB  . PRO A 1 420 ? 154.278 128.348 136.521 1.00 102.74 ? 436 PRO A CB  1 
ATOM   2336  C  CG  . PRO A 1 420 ? 155.090 129.323 135.738 1.00 102.74 ? 436 PRO A CG  1 
ATOM   2337  C  CD  . PRO A 1 420 ? 155.144 130.563 136.574 1.00 102.74 ? 436 PRO A CD  1 
ATOM   2338  N  N   . PHE A 1 421 ? 153.723 128.863 139.618 1.00 99.64  ? 437 PHE A N   1 
ATOM   2339  C  CA  . PHE A 1 421 ? 153.513 128.301 140.946 1.00 99.64  ? 437 PHE A CA  1 
ATOM   2340  C  C   . PHE A 1 421 ? 153.772 129.374 141.998 1.00 99.64  ? 437 PHE A C   1 
ATOM   2341  O  O   . PHE A 1 421 ? 154.062 130.532 141.679 1.00 99.64  ? 437 PHE A O   1 
ATOM   2342  C  CB  . PHE A 1 421 ? 154.376 127.051 141.168 1.00 99.64  ? 437 PHE A CB  1 
ATOM   2343  C  CG  . PHE A 1 421 ? 155.757 127.143 140.584 1.00 99.64  ? 437 PHE A CG  1 
ATOM   2344  C  CD1 . PHE A 1 421 ? 156.626 128.152 140.957 1.00 99.64  ? 437 PHE A CD1 1 
ATOM   2345  C  CD2 . PHE A 1 421 ? 156.188 126.204 139.662 1.00 99.64  ? 437 PHE A CD2 1 
ATOM   2346  C  CE1 . PHE A 1 421 ? 157.893 128.225 140.415 1.00 99.64  ? 437 PHE A CE1 1 
ATOM   2347  C  CE2 . PHE A 1 421 ? 157.454 126.274 139.120 1.00 99.64  ? 437 PHE A CE2 1 
ATOM   2348  C  CZ  . PHE A 1 421 ? 158.306 127.284 139.500 1.00 99.64  ? 437 PHE A CZ  1 
ATOM   2349  N  N   . ALA A 1 422 ? 153.663 128.979 143.266 1.00 93.96  ? 438 ALA A N   1 
ATOM   2350  C  CA  . ALA A 1 422 ? 153.811 129.903 144.380 1.00 93.96  ? 438 ALA A CA  1 
ATOM   2351  C  C   . ALA A 1 422 ? 154.458 129.191 145.560 1.00 93.96  ? 438 ALA A C   1 
ATOM   2352  O  O   . ALA A 1 422 ? 154.329 127.975 145.718 1.00 93.96  ? 438 ALA A O   1 
ATOM   2353  C  CB  . ALA A 1 422 ? 152.460 130.495 144.798 1.00 93.96  ? 438 ALA A CB  1 
ATOM   2354  N  N   . GLY A 1 423 ? 155.157 129.968 146.387 1.00 101.43 ? 439 GLY A N   1 
ATOM   2355  C  CA  . GLY A 1 423 ? 155.730 129.475 147.628 1.00 101.43 ? 439 GLY A CA  1 
ATOM   2356  C  C   . GLY A 1 423 ? 157.226 129.695 147.737 1.00 101.43 ? 439 GLY A C   1 
ATOM   2357  O  O   . GLY A 1 423 ? 157.770 130.571 147.057 1.00 101.43 ? 439 GLY A O   1 
ATOM   2358  N  N   . ARG A 1 424 ? 157.901 128.928 148.597 1.00 104.55 ? 440 ARG A N   1 
ATOM   2359  C  CA  . ARG A 1 424 ? 159.347 129.059 148.728 1.00 104.55 ? 440 ARG A CA  1 
ATOM   2360  C  C   . ARG A 1 424 ? 160.012 128.820 147.380 1.00 104.55 ? 440 ARG A C   1 
ATOM   2361  O  O   . ARG A 1 424 ? 159.676 127.874 146.663 1.00 104.55 ? 440 ARG A O   1 
ATOM   2362  C  CB  . ARG A 1 424 ? 159.879 128.072 149.767 1.00 104.55 ? 440 ARG A CB  1 
ATOM   2363  N  N   . MET A 1 425 ? 160.963 129.681 147.032 1.00 107.36 ? 441 MET A N   1 
ATOM   2364  C  CA  . MET A 1 425 ? 161.480 129.689 145.674 1.00 107.36 ? 441 MET A CA  1 
ATOM   2365  C  C   . MET A 1 425 ? 162.971 130.006 145.667 1.00 107.36 ? 441 MET A C   1 
ATOM   2366  O  O   . MET A 1 425 ? 163.486 130.663 146.575 1.00 107.36 ? 441 MET A O   1 
ATOM   2367  C  CB  . MET A 1 425 ? 160.664 130.673 144.835 1.00 107.36 ? 441 MET A CB  1 
ATOM   2368  C  CG  . MET A 1 425 ? 160.977 130.664 143.377 1.00 107.36 ? 441 MET A CG  1 
ATOM   2369  S  SD  . MET A 1 425 ? 159.478 130.435 142.402 1.00 107.36 ? 441 MET A SD  1 
ATOM   2370  C  CE  . MET A 1 425 ? 158.350 131.549 143.213 1.00 107.36 ? 441 MET A CE  1 
ATOM   2371  N  N   . HIS A 1 426 ? 163.660 129.525 144.629 1.00 111.73 ? 442 HIS A N   1 
ATOM   2372  C  CA  . HIS A 1 426 ? 165.077 129.790 144.417 1.00 111.73 ? 442 HIS A CA  1 
ATOM   2373  C  C   . HIS A 1 426 ? 165.318 130.120 142.950 1.00 111.73 ? 442 HIS A C   1 
ATOM   2374  O  O   . HIS A 1 426 ? 164.722 129.504 142.063 1.00 111.73 ? 442 HIS A O   1 
ATOM   2375  C  CB  . HIS A 1 426 ? 165.938 128.591 144.829 1.00 111.73 ? 442 HIS A CB  1 
ATOM   2376  C  CG  . HIS A 1 426 ? 167.329 128.959 145.240 1.00 111.73 ? 442 HIS A CG  1 
ATOM   2377  N  ND1 . HIS A 1 426 ? 168.374 129.031 144.345 1.00 111.73 ? 442 HIS A ND1 1 
ATOM   2378  C  CD2 . HIS A 1 426 ? 167.848 129.271 146.451 1.00 111.73 ? 442 HIS A CD2 1 
ATOM   2379  C  CE1 . HIS A 1 426 ? 169.477 129.375 144.987 1.00 111.73 ? 442 HIS A CE1 1 
ATOM   2380  N  NE2 . HIS A 1 426 ? 169.184 129.526 146.266 1.00 111.73 ? 442 HIS A NE2 1 
ATOM   2381  N  N   . ALA A 1 427 ? 166.193 131.095 142.702 1.00 90.37  ? 443 ALA A N   1 
ATOM   2382  C  CA  . ALA A 1 427 ? 166.462 131.594 141.359 1.00 90.37  ? 443 ALA A CA  1 
ATOM   2383  C  C   . ALA A 1 427 ? 167.964 131.710 141.131 1.00 90.37  ? 443 ALA A C   1 
ATOM   2384  O  O   . ALA A 1 427 ? 168.749 131.833 142.074 1.00 90.37  ? 443 ALA A O   1 
ATOM   2385  C  CB  . ALA A 1 427 ? 165.792 132.954 141.119 1.00 90.37  ? 443 ALA A CB  1 
ATOM   2386  N  N   . ALA A 1 428 ? 168.353 131.672 139.857 1.00 94.45  ? 444 ALA A N   1 
ATOM   2387  C  CA  . ALA A 1 428 ? 169.755 131.796 139.464 1.00 94.45  ? 444 ALA A CA  1 
ATOM   2388  C  C   . ALA A 1 428 ? 169.822 132.353 138.051 1.00 94.45  ? 444 ALA A C   1 
ATOM   2389  O  O   . ALA A 1 428 ? 169.235 131.778 137.130 1.00 94.45  ? 444 ALA A O   1 
ATOM   2390  C  CB  . ALA A 1 428 ? 170.474 130.449 139.547 1.00 94.45  ? 444 ALA A CB  1 
ATOM   2391  N  N   . VAL A 1 429 ? 170.534 133.463 137.883 1.00 98.17  ? 445 VAL A N   1 
ATOM   2392  C  CA  . VAL A 1 429 ? 170.614 134.146 136.596 1.00 98.17  ? 445 VAL A CA  1 
ATOM   2393  C  C   . VAL A 1 429 ? 171.585 133.413 135.679 1.00 98.17  ? 445 VAL A C   1 
ATOM   2394  O  O   . VAL A 1 429 ? 172.722 133.119 136.064 1.00 98.17  ? 445 VAL A O   1 
ATOM   2395  C  CB  . VAL A 1 429 ? 171.044 135.608 136.789 1.00 98.17  ? 445 VAL A CB  1 
ATOM   2396  C  CG1 . VAL A 1 429 ? 171.291 136.271 135.446 1.00 98.17  ? 445 VAL A CG1 1 
ATOM   2397  C  CG2 . VAL A 1 429 ? 169.996 136.370 137.586 1.00 98.17  ? 445 VAL A CG2 1 
ATOM   2398  N  N   . HIS A 1 430 ? 171.138 133.125 134.457 1.00 116.86 ? 446 HIS A N   1 
ATOM   2399  C  CA  . HIS A 1 430 ? 171.972 132.492 133.440 1.00 116.86 ? 446 HIS A CA  1 
ATOM   2400  C  C   . HIS A 1 430 ? 171.711 133.182 132.111 1.00 116.86 ? 446 HIS A C   1 
ATOM   2401  O  O   . HIS A 1 430 ? 170.589 133.130 131.598 1.00 116.86 ? 446 HIS A O   1 
ATOM   2402  C  CB  . HIS A 1 430 ? 171.683 130.991 133.334 1.00 116.86 ? 446 HIS A CB  1 
ATOM   2403  C  CG  . HIS A 1 430 ? 172.637 130.248 132.448 1.00 116.86 ? 446 HIS A CG  1 
ATOM   2404  N  ND1 . HIS A 1 430 ? 173.023 128.950 132.698 1.00 116.86 ? 446 HIS A ND1 1 
ATOM   2405  C  CD2 . HIS A 1 430 ? 173.275 130.617 131.311 1.00 116.86 ? 446 HIS A CD2 1 
ATOM   2406  C  CE1 . HIS A 1 430 ? 173.861 128.551 131.757 1.00 116.86 ? 446 HIS A CE1 1 
ATOM   2407  N  NE2 . HIS A 1 430 ? 174.031 129.545 130.904 1.00 116.86 ? 446 HIS A NE2 1 
ATOM   2408  N  N   . LYS A 1 431 ? 172.745 133.819 131.558 1.00 117.22 ? 447 LYS A N   1 
ATOM   2409  C  CA  . LYS A 1 431 ? 172.653 134.586 130.311 1.00 117.22 ? 447 LYS A CA  1 
ATOM   2410  C  C   . LYS A 1 431 ? 171.569 135.641 130.494 1.00 117.22 ? 447 LYS A C   1 
ATOM   2411  O  O   . LYS A 1 431 ? 171.718 136.503 131.377 1.00 117.22 ? 447 LYS A O   1 
ATOM   2412  C  CB  . LYS A 1 431 ? 172.453 133.617 129.145 1.00 117.22 ? 447 LYS A CB  1 
ATOM   2413  N  N   . ASP A 1 432 ? 170.488 135.628 129.713 1.00 116.17 ? 448 ASP A N   1 
ATOM   2414  C  CA  . ASP A 1 432 ? 169.395 136.576 129.876 1.00 116.17 ? 448 ASP A CA  1 
ATOM   2415  C  C   . ASP A 1 432 ? 168.151 135.907 130.445 1.00 116.17 ? 448 ASP A C   1 
ATOM   2416  O  O   . ASP A 1 432 ? 167.041 136.425 130.285 1.00 116.17 ? 448 ASP A O   1 
ATOM   2417  C  CB  . ASP A 1 432 ? 169.061 137.248 128.545 1.00 116.17 ? 448 ASP A CB  1 
ATOM   2418  C  CG  . ASP A 1 432 ? 168.786 136.247 127.444 1.00 116.17 ? 448 ASP A CG  1 
ATOM   2419  O  OD1 . ASP A 1 432 ? 169.433 135.180 127.437 1.00 116.17 ? 448 ASP A OD1 1 
ATOM   2420  O  OD2 . ASP A 1 432 ? 167.916 136.522 126.592 1.00 116.17 ? 448 ASP A OD2 1 
ATOM   2421  N  N   . LEU A 1 433 ? 168.314 134.765 131.104 1.00 105.71 ? 449 LEU A N   1 
ATOM   2422  C  CA  . LEU A 1 433 ? 167.198 133.984 131.609 1.00 105.71 ? 449 LEU A CA  1 
ATOM   2423  C  C   . LEU A 1 433 ? 167.309 133.853 133.120 1.00 105.71 ? 449 LEU A C   1 
ATOM   2424  O  O   . LEU A 1 433 ? 168.354 134.116 133.720 1.00 105.71 ? 449 LEU A O   1 
ATOM   2425  C  CB  . LEU A 1 433 ? 167.153 132.585 130.976 1.00 105.71 ? 449 LEU A CB  1 
ATOM   2426  C  CG  . LEU A 1 433 ? 167.126 132.405 129.455 1.00 105.71 ? 449 LEU A CG  1 
ATOM   2427  C  CD1 . LEU A 1 433 ? 166.205 133.417 128.798 1.00 105.71 ? 449 LEU A CD1 1 
ATOM   2428  C  CD2 . LEU A 1 433 ? 168.523 132.446 128.852 1.00 105.71 ? 449 LEU A CD2 1 
ATOM   2429  N  N   . VAL A 1 434 ? 166.208 133.436 133.734 1.00 92.73  ? 450 VAL A N   1 
ATOM   2430  C  CA  . VAL A 1 434 ? 166.172 133.108 135.152 1.00 92.73  ? 450 VAL A CA  1 
ATOM   2431  C  C   . VAL A 1 434 ? 165.645 131.687 135.275 1.00 92.73  ? 450 VAL A C   1 
ATOM   2432  O  O   . VAL A 1 434 ? 164.523 131.395 134.840 1.00 92.73  ? 450 VAL A O   1 
ATOM   2433  C  CB  . VAL A 1 434 ? 165.304 134.092 135.953 1.00 92.73  ? 450 VAL A CB  1 
ATOM   2434  C  CG1 . VAL A 1 434 ? 165.438 133.819 137.441 1.00 92.73  ? 450 VAL A CG1 1 
ATOM   2435  C  CG2 . VAL A 1 434 ? 165.695 135.527 135.639 1.00 92.73  ? 450 VAL A CG2 1 
ATOM   2436  N  N   . PHE A 1 435 ? 166.462 130.799 135.835 1.00 99.28  ? 451 PHE A N   1 
ATOM   2437  C  CA  . PHE A 1 435 ? 166.063 129.410 136.044 1.00 99.28  ? 451 PHE A CA  1 
ATOM   2438  C  C   . PHE A 1 435 ? 165.523 129.300 137.462 1.00 99.28  ? 451 PHE A C   1 
ATOM   2439  O  O   . PHE A 1 435 ? 166.284 129.187 138.425 1.00 99.28  ? 451 PHE A O   1 
ATOM   2440  C  CB  . PHE A 1 435 ? 167.230 128.463 135.799 1.00 99.28  ? 451 PHE A CB  1 
ATOM   2441  C  CG  . PHE A 1 435 ? 167.547 128.262 134.350 1.00 99.28  ? 451 PHE A CG  1 
ATOM   2442  C  CD1 . PHE A 1 435 ? 168.428 129.103 133.697 1.00 99.28  ? 451 PHE A CD1 1 
ATOM   2443  C  CD2 . PHE A 1 435 ? 166.952 127.236 133.637 1.00 99.28  ? 451 PHE A CD2 1 
ATOM   2444  C  CE1 . PHE A 1 435 ? 168.716 128.918 132.362 1.00 99.28  ? 451 PHE A CE1 1 
ATOM   2445  C  CE2 . PHE A 1 435 ? 167.236 127.048 132.302 1.00 99.28  ? 451 PHE A CE2 1 
ATOM   2446  C  CZ  . PHE A 1 435 ? 168.118 127.890 131.665 1.00 99.28  ? 451 PHE A CZ  1 
ATOM   2447  N  N   . ILE A 1 436 ? 164.202 129.330 137.588 1.00 100.29 ? 452 ILE A N   1 
ATOM   2448  C  CA  . ILE A 1 436 ? 163.528 129.403 138.875 1.00 100.29 ? 452 ILE A CA  1 
ATOM   2449  C  C   . ILE A 1 436 ? 163.085 128.003 139.274 1.00 100.29 ? 452 ILE A C   1 
ATOM   2450  O  O   . ILE A 1 436 ? 162.474 127.282 138.474 1.00 100.29 ? 452 ILE A O   1 
ATOM   2451  C  CB  . ILE A 1 436 ? 162.335 130.369 138.812 1.00 100.29 ? 452 ILE A CB  1 
ATOM   2452  C  CG1 . ILE A 1 436 ? 162.691 131.591 137.971 1.00 100.29 ? 452 ILE A CG1 1 
ATOM   2453  C  CG2 . ILE A 1 436 ? 162.013 130.867 140.173 1.00 100.29 ? 452 ILE A CG2 1 
ATOM   2454  C  CD1 . ILE A 1 436 ? 161.491 132.401 137.552 1.00 100.29 ? 452 ILE A CD1 1 
ATOM   2455  N  N   . VAL A 1 437 ? 163.387 127.616 140.511 1.00 104.45 ? 453 VAL A N   1 
ATOM   2456  C  CA  . VAL A 1 437 ? 163.093 126.283 141.024 1.00 104.45 ? 453 VAL A CA  1 
ATOM   2457  C  C   . VAL A 1 437 ? 162.269 126.423 142.296 1.00 104.45 ? 453 VAL A C   1 
ATOM   2458  O  O   . VAL A 1 437 ? 162.604 127.228 143.173 1.00 104.45 ? 453 VAL A O   1 
ATOM   2459  C  CB  . VAL A 1 437 ? 164.383 125.488 141.295 1.00 104.45 ? 453 VAL A CB  1 
ATOM   2460  C  CG1 . VAL A 1 437 ? 164.079 124.213 142.062 1.00 104.45 ? 453 VAL A CG1 1 
ATOM   2461  C  CG2 . VAL A 1 437 ? 165.096 125.176 139.993 1.00 104.45 ? 453 VAL A CG2 1 
ATOM   2462  N  N   . ALA A 1 438 ? 161.195 125.640 142.395 1.00 111.52 ? 454 ALA A N   1 
ATOM   2463  C  CA  . ALA A 1 438 ? 160.320 125.677 143.558 1.00 111.52 ? 454 ALA A CA  1 
ATOM   2464  C  C   . ALA A 1 438 ? 159.570 124.357 143.652 1.00 111.52 ? 454 ALA A C   1 
ATOM   2465  O  O   . ALA A 1 438 ? 159.474 123.606 142.678 1.00 111.52 ? 454 ALA A O   1 
ATOM   2466  C  CB  . ALA A 1 438 ? 159.338 126.851 143.490 1.00 111.52 ? 454 ALA A CB  1 
ATOM   2467  N  N   . GLU A 1 439 ? 159.039 124.090 144.845 1.00 128.73 ? 455 GLU A N   1 
ATOM   2468  C  CA  . GLU A 1 439 ? 158.233 122.893 145.137 1.00 128.73 ? 455 GLU A CA  1 
ATOM   2469  C  C   . GLU A 1 439 ? 159.094 121.666 144.839 1.00 128.73 ? 455 GLU A C   1 
ATOM   2470  O  O   . GLU A 1 439 ? 160.232 121.591 145.330 1.00 128.73 ? 455 GLU A O   1 
ATOM   2471  C  CB  . GLU A 1 439 ? 156.916 122.978 144.376 1.00 128.73 ? 455 GLU A CB  1 
ATOM   2472  N  N   . GLY A 1 440 ? 158.613 120.699 144.061 1.00 133.30 ? 456 GLY A N   1 
ATOM   2473  C  CA  . GLY A 1 440 ? 159.397 119.526 143.734 1.00 133.30 ? 456 GLY A CA  1 
ATOM   2474  C  C   . GLY A 1 440 ? 159.195 119.089 142.299 1.00 133.30 ? 456 GLY A C   1 
ATOM   2475  O  O   . GLY A 1 440 ? 158.064 119.080 141.801 1.00 133.30 ? 456 GLY A O   1 
ATOM   2476  N  N   . ASP A 1 441 ? 160.292 118.732 141.626 1.00 137.43 ? 457 ASP A N   1 
ATOM   2477  C  CA  . ASP A 1 441 ? 160.273 118.343 140.215 1.00 137.43 ? 457 ASP A CA  1 
ATOM   2478  C  C   . ASP A 1 441 ? 159.690 119.451 139.346 1.00 137.43 ? 457 ASP A C   1 
ATOM   2479  O  O   . ASP A 1 441 ? 159.071 119.188 138.312 1.00 137.43 ? 457 ASP A O   1 
ATOM   2480  C  CB  . ASP A 1 441 ? 159.509 117.032 140.003 1.00 137.43 ? 457 ASP A CB  1 
ATOM   2481  N  N   . SER A 1 442 ? 159.890 120.698 139.767 1.00 122.26 ? 458 SER A N   1 
ATOM   2482  C  CA  . SER A 1 442 ? 159.389 121.867 139.058 1.00 122.26 ? 458 SER A CA  1 
ATOM   2483  C  C   . SER A 1 442 ? 160.546 122.817 138.794 1.00 122.26 ? 458 SER A C   1 
ATOM   2484  O  O   . SER A 1 442 ? 161.319 123.129 139.708 1.00 122.26 ? 458 SER A O   1 
ATOM   2485  C  CB  . SER A 1 442 ? 158.288 122.574 139.860 1.00 122.26 ? 458 SER A CB  1 
ATOM   2486  N  N   . LEU A 1 443 ? 160.660 123.269 137.551 1.00 123.49 ? 459 LEU A N   1 
ATOM   2487  C  CA  . LEU A 1 443 ? 161.714 124.188 137.151 1.00 123.49 ? 459 LEU A CA  1 
ATOM   2488  C  C   . LEU A 1 443 ? 161.210 124.962 135.949 1.00 123.49 ? 459 LEU A C   1 
ATOM   2489  O  O   . LEU A 1 443 ? 160.719 124.360 134.991 1.00 123.49 ? 459 LEU A O   1 
ATOM   2490  C  CB  . LEU A 1 443 ? 163.012 123.439 136.823 1.00 123.49 ? 459 LEU A CB  1 
ATOM   2491  C  CG  . LEU A 1 443 ? 164.256 124.228 136.407 1.00 123.49 ? 459 LEU A CG  1 
ATOM   2492  C  CD1 . LEU A 1 443 ? 165.493 123.457 136.807 1.00 123.49 ? 459 LEU A CD1 1 
ATOM   2493  C  CD2 . LEU A 1 443 ? 164.289 124.513 134.913 1.00 123.49 ? 459 LEU A CD2 1 
ATOM   2494  N  N   . VAL A 1 444 ? 161.326 126.286 135.999 1.00 112.17 ? 460 VAL A N   1 
ATOM   2495  C  CA  . VAL A 1 444 ? 160.814 127.141 134.940 1.00 112.17 ? 460 VAL A CA  1 
ATOM   2496  C  C   . VAL A 1 444 ? 161.919 128.075 134.475 1.00 112.17 ? 460 VAL A C   1 
ATOM   2497  O  O   . VAL A 1 444 ? 162.583 128.718 135.294 1.00 112.17 ? 460 VAL A O   1 
ATOM   2498  C  CB  . VAL A 1 444 ? 159.591 127.959 135.406 1.00 112.17 ? 460 VAL A CB  1 
ATOM   2499  C  CG1 . VAL A 1 444 ? 158.354 127.094 135.475 1.00 112.17 ? 460 VAL A CG1 1 
ATOM   2500  C  CG2 . VAL A 1 444 ? 159.859 128.610 136.754 1.00 112.17 ? 460 VAL A CG2 1 
ATOM   2501  N  N   . CYS A 1 445 ? 162.115 128.151 133.166 1.00 115.19 ? 461 CYS A N   1 
ATOM   2502  C  CA  . CYS A 1 445 ? 163.019 129.137 132.587 1.00 115.19 ? 461 CYS A CA  1 
ATOM   2503  C  C   . CYS A 1 445 ? 162.165 130.330 132.186 1.00 115.19 ? 461 CYS A C   1 
ATOM   2504  O  O   . CYS A 1 445 ? 161.308 130.220 131.298 1.00 115.19 ? 461 CYS A O   1 
ATOM   2505  C  CB  . CYS A 1 445 ? 163.776 128.555 131.394 1.00 115.19 ? 461 CYS A CB  1 
ATOM   2506  S  SG  . CYS A 1 445 ? 164.825 129.726 130.514 1.00 115.19 ? 461 CYS A SG  1 
ATOM   2507  N  N   . TYR A 1 446 ? 162.335 131.435 132.905 1.00 115.31 ? 462 TYR A N   1 
ATOM   2508  C  CA  . TYR A 1 446 ? 161.504 132.617 132.749 1.00 115.31 ? 462 TYR A CA  1 
ATOM   2509  C  C   . TYR A 1 446 ? 162.434 133.703 132.216 1.00 115.31 ? 462 TYR A C   1 
ATOM   2510  O  O   . TYR A 1 446 ? 163.514 133.927 132.772 1.00 115.31 ? 462 TYR A O   1 
ATOM   2511  C  CB  . TYR A 1 446 ? 160.860 133.006 134.091 1.00 115.31 ? 462 TYR A CB  1 
ATOM   2512  C  CG  . TYR A 1 446 ? 160.168 134.361 134.199 1.00 115.31 ? 462 TYR A CG  1 
ATOM   2513  C  CD1 . TYR A 1 446 ? 159.764 135.061 133.067 1.00 115.31 ? 462 TYR A CD1 1 
ATOM   2514  C  CD2 . TYR A 1 446 ? 159.907 134.931 135.444 1.00 115.31 ? 462 TYR A CD2 1 
ATOM   2515  C  CE1 . TYR A 1 446 ? 159.120 136.276 133.172 1.00 115.31 ? 462 TYR A CE1 1 
ATOM   2516  C  CE2 . TYR A 1 446 ? 159.268 136.153 135.554 1.00 115.31 ? 462 TYR A CE2 1 
ATOM   2517  C  CZ  . TYR A 1 446 ? 158.883 136.824 134.418 1.00 115.31 ? 462 TYR A CZ  1 
ATOM   2518  O  OH  . TYR A 1 446 ? 158.245 138.041 134.536 1.00 115.31 ? 462 TYR A OH  1 
ATOM   2519  N  N   . ASN A 1 447 ? 162.027 134.360 131.139 1.00 122.62 ? 463 ASN A N   1 
ATOM   2520  C  CA  . ASN A 1 447 ? 162.743 135.500 130.569 1.00 122.62 ? 463 ASN A CA  1 
ATOM   2521  C  C   . ASN A 1 447 ? 162.024 136.835 130.808 1.00 122.62 ? 463 ASN A C   1 
ATOM   2522  O  O   . ASN A 1 447 ? 161.140 137.240 130.049 1.00 122.62 ? 463 ASN A O   1 
ATOM   2523  C  CB  . ASN A 1 447 ? 163.094 135.228 129.097 1.00 122.62 ? 463 ASN A CB  1 
ATOM   2524  C  CG  . ASN A 1 447 ? 161.960 135.438 128.089 1.00 122.62 ? 463 ASN A CG  1 
ATOM   2525  O  OD1 . ASN A 1 447 ? 160.789 135.642 128.406 1.00 122.62 ? 463 ASN A OD1 1 
ATOM   2526  N  ND2 . ASN A 1 447 ? 162.334 135.341 126.829 1.00 122.62 ? 463 ASN A ND2 1 
ATOM   2527  N  N   . PRO A 1 448 ? 162.394 137.563 131.873 1.00 114.99 ? 464 PRO A N   1 
ATOM   2528  C  CA  . PRO A 1 448 ? 161.600 138.681 132.322 1.00 114.99 ? 464 PRO A CA  1 
ATOM   2529  C  C   . PRO A 1 448 ? 161.366 139.801 131.339 1.00 114.99 ? 464 PRO A C   1 
ATOM   2530  O  O   . PRO A 1 448 ? 160.351 140.490 131.479 1.00 114.99 ? 464 PRO A O   1 
ATOM   2531  C  CB  . PRO A 1 448 ? 162.525 139.201 133.433 1.00 114.99 ? 464 PRO A CB  1 
ATOM   2532  C  CG  . PRO A 1 448 ? 163.303 137.822 133.840 1.00 114.99 ? 464 PRO A CG  1 
ATOM   2533  C  CD  . PRO A 1 448 ? 162.428 136.891 133.217 1.00 114.99 ? 464 PRO A CD  1 
ATOM   2534  N  N   . LEU A 1 449 ? 162.250 140.030 130.365 1.00 126.91 ? 465 LEU A N   1 
ATOM   2535  C  CA  . LEU A 1 449 ? 161.949 141.040 129.354 1.00 126.91 ? 465 LEU A CA  1 
ATOM   2536  C  C   . LEU A 1 449 ? 160.666 140.710 128.595 1.00 126.91 ? 465 LEU A C   1 
ATOM   2537  O  O   . LEU A 1 449 ? 159.985 141.617 128.101 1.00 126.91 ? 465 LEU A O   1 
ATOM   2538  C  CB  . LEU A 1 449 ? 163.138 141.221 128.409 1.00 126.91 ? 465 LEU A CB  1 
ATOM   2539  C  CG  . LEU A 1 449 ? 162.845 141.785 127.025 1.00 126.91 ? 465 LEU A CG  1 
ATOM   2540  C  CD1 . LEU A 1 449 ? 162.501 143.254 127.136 1.00 126.91 ? 465 LEU A CD1 1 
ATOM   2541  C  CD2 . LEU A 1 449 ? 164.062 141.631 126.175 1.00 126.91 ? 465 LEU A CD2 1 
ATOM   2542  N  N   . LEU A 1 450 ? 160.297 139.435 128.532 1.00 114.13 ? 466 LEU A N   1 
ATOM   2543  C  CA  . LEU A 1 450 ? 159.097 138.969 127.844 1.00 114.13 ? 466 LEU A CA  1 
ATOM   2544  C  C   . LEU A 1 450 ? 158.132 138.326 128.834 1.00 114.13 ? 466 LEU A C   1 
ATOM   2545  O  O   . LEU A 1 450 ? 158.339 138.348 130.049 1.00 114.13 ? 466 LEU A O   1 
ATOM   2546  C  CB  . LEU A 1 450 ? 159.445 137.996 126.718 1.00 114.13 ? 466 LEU A CB  1 
ATOM   2547  C  CG  . LEU A 1 450 ? 160.700 138.288 125.911 1.00 114.13 ? 466 LEU A CG  1 
ATOM   2548  C  CD1 . LEU A 1 450 ? 160.870 137.203 124.885 1.00 114.13 ? 466 LEU A CD1 1 
ATOM   2549  C  CD2 . LEU A 1 450 ? 160.568 139.641 125.230 1.00 114.13 ? 466 LEU A CD2 1 
ATOM   2550  N  N   . ASP A 1 451 ? 157.070 137.734 128.289 1.00 128.41 ? 467 ASP A N   1 
ATOM   2551  C  CA  . ASP A 1 451 ? 156.009 137.097 129.066 1.00 128.41 ? 467 ASP A CA  1 
ATOM   2552  C  C   . ASP A 1 451 ? 155.816 135.677 128.548 1.00 128.41 ? 467 ASP A C   1 
ATOM   2553  O  O   . ASP A 1 451 ? 154.973 135.425 127.683 1.00 128.41 ? 467 ASP A O   1 
ATOM   2554  C  CB  . ASP A 1 451 ? 154.717 137.903 128.978 1.00 128.41 ? 467 ASP A CB  1 
ATOM   2555  N  N   . SER A 1 452 ? 156.612 134.756 129.084 1.00 116.73 ? 468 SER A N   1 
ATOM   2556  C  CA  . SER A 1 452 ? 156.504 133.332 128.800 1.00 116.73 ? 468 SER A CA  1 
ATOM   2557  C  C   . SER A 1 452 ? 157.401 132.588 129.775 1.00 116.73 ? 468 SER A C   1 
ATOM   2558  O  O   . SER A 1 452 ? 158.494 133.056 130.101 1.00 116.73 ? 468 SER A O   1 
ATOM   2559  C  CB  . SER A 1 452 ? 156.908 133.008 127.353 1.00 116.73 ? 468 SER A CB  1 
ATOM   2560  O  OG  . SER A 1 452 ? 158.288 133.246 127.140 1.00 116.73 ? 468 SER A OG  1 
ATOM   2561  N  N   . PHE A 1 453 ? 156.930 131.433 130.234 1.00 114.34 ? 469 PHE A N   1 
ATOM   2562  C  CA  . PHE A 1 453 ? 157.665 130.584 131.162 1.00 114.34 ? 469 PHE A CA  1 
ATOM   2563  C  C   . PHE A 1 453 ? 157.738 129.194 130.557 1.00 114.34 ? 469 PHE A C   1 
ATOM   2564  O  O   . PHE A 1 453 ? 156.708 128.637 130.165 1.00 114.34 ? 469 PHE A O   1 
ATOM   2565  C  CB  . PHE A 1 453 ? 156.993 130.527 132.544 1.00 114.34 ? 469 PHE A CB  1 
ATOM   2566  C  CG  . PHE A 1 453 ? 156.577 131.870 133.086 1.00 114.34 ? 469 PHE A CG  1 
ATOM   2567  C  CD1 . PHE A 1 453 ? 155.432 132.498 132.626 1.00 114.34 ? 469 PHE A CD1 1 
ATOM   2568  C  CD2 . PHE A 1 453 ? 157.322 132.493 134.070 1.00 114.34 ? 469 PHE A CD2 1 
ATOM   2569  C  CE1 . PHE A 1 453 ? 155.050 133.727 133.125 1.00 114.34 ? 469 PHE A CE1 1 
ATOM   2570  C  CE2 . PHE A 1 453 ? 156.939 133.720 134.575 1.00 114.34 ? 469 PHE A CE2 1 
ATOM   2571  C  CZ  . PHE A 1 453 ? 155.805 134.338 134.101 1.00 114.34 ? 469 PHE A CZ  1 
ATOM   2572  N  N   . THR A 1 454 ? 158.936 128.629 130.477 1.00 117.64 ? 470 THR A N   1 
ATOM   2573  C  CA  . THR A 1 454 ? 159.058 127.247 130.041 1.00 117.64 ? 470 THR A CA  1 
ATOM   2574  C  C   . THR A 1 454 ? 159.339 126.331 131.224 1.00 117.64 ? 470 THR A C   1 
ATOM   2575  O  O   . THR A 1 454 ? 159.746 126.777 132.296 1.00 117.64 ? 470 THR A O   1 
ATOM   2576  C  CB  . THR A 1 454 ? 160.157 127.113 128.992 1.00 117.64 ? 470 THR A CB  1 
ATOM   2577  O  OG1 . THR A 1 454 ? 161.417 127.468 129.573 1.00 117.64 ? 470 THR A OG1 1 
ATOM   2578  C  CG2 . THR A 1 454 ? 159.868 128.060 127.856 1.00 117.64 ? 470 THR A CG2 1 
ATOM   2579  N  N   . ARG A 1 455 ? 159.154 125.031 131.003 1.00 125.37 ? 471 ARG A N   1 
ATOM   2580  C  CA  . ARG A 1 455 ? 159.386 124.031 132.037 1.00 125.37 ? 471 ARG A CA  1 
ATOM   2581  C  C   . ARG A 1 455 ? 160.275 122.913 131.514 1.00 125.37 ? 471 ARG A C   1 
ATOM   2582  O  O   . ARG A 1 455 ? 160.129 122.471 130.370 1.00 125.37 ? 471 ARG A O   1 
ATOM   2583  C  CB  . ARG A 1 455 ? 158.062 123.431 132.531 1.00 125.37 ? 471 ARG A CB  1 
ATOM   2584  C  CG  . ARG A 1 455 ? 157.507 124.069 133.792 1.00 125.37 ? 471 ARG A CG  1 
ATOM   2585  C  CD  . ARG A 1 455 ? 157.076 123.013 134.798 1.00 125.37 ? 471 ARG A CD  1 
ATOM   2586  N  NE  . ARG A 1 455 ? 156.471 123.595 135.990 1.00 125.37 ? 471 ARG A NE  1 
ATOM   2587  C  CZ  . ARG A 1 455 ? 155.223 124.039 136.060 1.00 125.37 ? 471 ARG A CZ  1 
ATOM   2588  N  NH1 . ARG A 1 455 ? 154.421 124.015 135.009 1.00 125.37 ? 471 ARG A NH1 1 
ATOM   2589  N  NH2 . ARG A 1 455 ? 154.770 124.522 137.213 1.00 125.37 ? 471 ARG A NH2 1 
ATOM   2590  N  N   . LEU A 1 456 ? 161.192 122.457 132.364 1.00 142.96 ? 472 LEU A N   1 
ATOM   2591  C  CA  . LEU A 1 456 ? 162.099 121.359 132.056 1.00 142.96 ? 472 LEU A CA  1 
ATOM   2592  C  C   . LEU A 1 456 ? 161.885 120.234 133.059 1.00 142.96 ? 472 LEU A C   1 
ATOM   2593  O  O   . LEU A 1 456 ? 161.729 120.482 134.259 1.00 142.96 ? 472 LEU A O   1 
ATOM   2594  C  CB  . LEU A 1 456 ? 163.572 121.802 132.079 1.00 142.96 ? 472 LEU A CB  1 
ATOM   2595  C  CG  . LEU A 1 456 ? 164.027 123.107 131.418 1.00 142.96 ? 472 LEU A CG  1 
ATOM   2596  C  CD1 . LEU A 1 456 ? 165.526 123.056 131.177 1.00 142.96 ? 472 LEU A CD1 1 
ATOM   2597  C  CD2 . LEU A 1 456 ? 163.304 123.360 130.103 1.00 142.96 ? 472 LEU A CD2 1 
ATOM   2598  N  N   . CYS A 1 457 ? 161.877 119.000 132.564 1.00 150.97 ? 473 CYS A N   1 
ATOM   2599  C  CA  . CYS A 1 457 ? 161.673 117.849 133.433 1.00 150.97 ? 473 CYS A CA  1 
ATOM   2600  C  C   . CYS A 1 457 ? 162.891 117.627 134.320 1.00 150.97 ? 473 CYS A C   1 
ATOM   2601  O  O   . CYS A 1 457 ? 164.035 117.692 133.862 1.00 150.97 ? 473 CYS A O   1 
ATOM   2602  C  CB  . CYS A 1 457 ? 161.394 116.597 132.602 1.00 150.97 ? 473 CYS A CB  1 
ATOM   2603  N  N   . LEU A 1 458 ? 162.641 117.362 135.592 1.00 158.46 ? 474 LEU A N   1 
ATOM   2604  C  CA  . LEU A 1 458 ? 163.674 117.040 136.562 1.00 158.46 ? 474 LEU A CA  1 
ATOM   2605  C  C   . LEU A 1 458 ? 163.774 115.528 136.727 1.00 158.46 ? 474 LEU A C   1 
ATOM   2606  O  O   . LEU A 1 458 ? 162.921 114.782 136.240 1.00 158.46 ? 474 LEU A O   1 
ATOM   2607  C  CB  . LEU A 1 458 ? 163.346 117.721 137.896 1.00 158.46 ? 474 LEU A CB  1 
ATOM   2608  C  CG  . LEU A 1 458 ? 163.890 119.140 138.093 1.00 158.46 ? 474 LEU A CG  1 
ATOM   2609  C  CD1 . LEU A 1 458 ? 163.638 119.624 139.515 1.00 158.46 ? 474 LEU A CD1 1 
ATOM   2610  C  CD2 . LEU A 1 458 ? 165.368 119.234 137.743 1.00 158.46 ? 474 LEU A CD2 1 
ATOM   2611  N  N   . PRO A 1 459 ? 164.820 115.019 137.421 1.00 172.99 ? 475 PRO A N   1 
ATOM   2612  C  CA  . PRO A 1 459 ? 165.000 113.560 137.474 1.00 172.99 ? 475 PRO A CA  1 
ATOM   2613  C  C   . PRO A 1 459 ? 164.009 112.853 138.388 1.00 172.99 ? 475 PRO A C   1 
ATOM   2614  O  O   . PRO A 1 459 ? 164.173 111.661 138.671 1.00 172.99 ? 475 PRO A O   1 
ATOM   2615  C  CB  . PRO A 1 459 ? 166.439 113.399 137.979 1.00 172.99 ? 475 PRO A CB  1 
ATOM   2616  C  CG  . PRO A 1 459 ? 166.715 114.633 138.736 1.00 172.99 ? 475 PRO A CG  1 
ATOM   2617  C  CD  . PRO A 1 459 ? 165.956 115.726 138.044 1.00 172.99 ? 475 PRO A CD  1 
ATOM   2618  N  N   . GLU A 1 460 ? 162.987 113.572 138.855 1.00 184.20 ? 476 GLU A N   1 
ATOM   2619  C  CA  . GLU A 1 460 ? 161.895 112.998 139.641 1.00 184.20 ? 476 GLU A CA  1 
ATOM   2620  C  C   . GLU A 1 460 ? 162.424 112.336 140.916 1.00 184.20 ? 476 GLU A C   1 
ATOM   2621  O  O   . GLU A 1 460 ? 162.308 111.126 141.120 1.00 184.20 ? 476 GLU A O   1 
ATOM   2622  C  CB  . GLU A 1 460 ? 161.075 112.011 138.802 1.00 184.20 ? 476 GLU A CB  1 
ATOM   2623  N  N   . ALA A 1 461 ? 163.017 113.160 141.774 1.00 176.39 ? 477 ALA A N   1 
ATOM   2624  C  CA  . ALA A 1 461 ? 163.539 112.690 143.051 1.00 176.39 ? 477 ALA A CA  1 
ATOM   2625  C  C   . ALA A 1 461 ? 162.413 112.221 143.967 1.00 176.39 ? 477 ALA A C   1 
ATOM   2626  O  O   . ALA A 1 461 ? 161.437 112.939 144.184 1.00 176.39 ? 477 ALA A O   1 
ATOM   2627  C  CB  . ALA A 1 461 ? 164.351 113.783 143.726 1.00 176.39 ? 477 ALA A CB  1 
ATOM   2628  N  N   . LEU A 1 468 ? 163.500 119.770 147.864 1.00 127.81 ? 484 LEU A N   1 
ATOM   2629  C  CA  . LEU A 1 468 ? 163.753 121.206 147.897 1.00 127.81 ? 484 LEU A CA  1 
ATOM   2630  C  C   . LEU A 1 468 ? 165.081 121.542 147.229 1.00 127.81 ? 484 LEU A C   1 
ATOM   2631  O  O   . LEU A 1 468 ? 166.091 121.746 147.902 1.00 127.81 ? 484 LEU A O   1 
ATOM   2632  C  CB  . LEU A 1 468 ? 163.741 121.720 149.337 1.00 127.81 ? 484 LEU A CB  1 
ATOM   2633  N  N   . TRP A 1 469 ? 165.071 121.599 145.901 1.00 131.97 ? 485 TRP A N   1 
ATOM   2634  C  CA  . TRP A 1 469 ? 166.282 121.897 145.151 1.00 131.97 ? 485 TRP A CA  1 
ATOM   2635  C  C   . TRP A 1 469 ? 166.693 123.354 145.325 1.00 131.97 ? 485 TRP A C   1 
ATOM   2636  O  O   . TRP A 1 469 ? 165.870 124.232 145.595 1.00 131.97 ? 485 TRP A O   1 
ATOM   2637  C  CB  . TRP A 1 469 ? 166.082 121.597 143.666 1.00 131.97 ? 485 TRP A CB  1 
ATOM   2638  C  CG  . TRP A 1 469 ? 165.747 120.172 143.371 1.00 131.97 ? 485 TRP A CG  1 
ATOM   2639  C  CD1 . TRP A 1 469 ? 164.535 119.676 142.988 1.00 131.97 ? 485 TRP A CD1 1 
ATOM   2640  C  CD2 . TRP A 1 469 ? 166.639 119.054 143.426 1.00 131.97 ? 485 TRP A CD2 1 
ATOM   2641  N  NE1 . TRP A 1 469 ? 164.617 118.318 142.804 1.00 131.97 ? 485 TRP A NE1 1 
ATOM   2642  C  CE2 . TRP A 1 469 ? 165.899 117.911 143.067 1.00 131.97 ? 485 TRP A CE2 1 
ATOM   2643  C  CE3 . TRP A 1 469 ? 167.992 118.908 143.745 1.00 131.97 ? 485 TRP A CE3 1 
ATOM   2644  C  CZ2 . TRP A 1 469 ? 166.465 116.640 143.019 1.00 131.97 ? 485 TRP A CZ2 1 
ATOM   2645  C  CZ3 . TRP A 1 469 ? 168.552 117.647 143.697 1.00 131.97 ? 485 TRP A CZ3 1 
ATOM   2646  C  CH2 . TRP A 1 469 ? 167.790 116.529 143.337 1.00 131.97 ? 485 TRP A CH2 1 
ATOM   2647  N  N   . LYS A 1 470 ? 167.991 123.603 145.164 1.00 105.68 ? 486 LYS A N   1 
ATOM   2648  C  CA  . LYS A 1 470 ? 168.540 124.950 145.109 1.00 105.68 ? 486 LYS A CA  1 
ATOM   2649  C  C   . LYS A 1 470 ? 169.489 125.023 143.924 1.00 105.68 ? 486 LYS A C   1 
ATOM   2650  O  O   . LYS A 1 470 ? 170.386 124.187 143.790 1.00 105.68 ? 486 LYS A O   1 
ATOM   2651  C  CB  . LYS A 1 470 ? 169.260 125.318 146.410 1.00 105.68 ? 486 LYS A CB  1 
ATOM   2652  C  CG  . LYS A 1 470 ? 168.331 125.477 147.602 1.00 105.68 ? 486 LYS A CG  1 
ATOM   2653  C  CD  . LYS A 1 470 ? 169.100 125.796 148.871 1.00 105.68 ? 486 LYS A CD  1 
ATOM   2654  C  CE  . LYS A 1 470 ? 168.188 125.776 150.085 1.00 105.68 ? 486 LYS A CE  1 
ATOM   2655  N  NZ  . LYS A 1 470 ? 167.517 127.088 150.294 1.00 105.68 ? 486 LYS A NZ  1 
ATOM   2656  N  N   . ILE A 1 471 ? 169.292 126.014 143.073 1.00 105.19 ? 487 ILE A N   1 
ATOM   2657  C  CA  . ILE A 1 471 ? 170.005 126.108 141.807 1.00 105.19 ? 487 ILE A CA  1 
ATOM   2658  C  C   . ILE A 1 471 ? 171.108 127.150 141.925 1.00 105.19 ? 487 ILE A C   1 
ATOM   2659  O  O   . ILE A 1 471 ? 171.029 128.080 142.736 1.00 105.19 ? 487 ILE A O   1 
ATOM   2660  C  CB  . ILE A 1 471 ? 169.015 126.433 140.667 1.00 105.19 ? 487 ILE A CB  1 
ATOM   2661  C  CG1 . ILE A 1 471 ? 169.702 126.396 139.304 1.00 105.19 ? 487 ILE A CG1 1 
ATOM   2662  C  CG2 . ILE A 1 471 ? 168.349 127.780 140.906 1.00 105.19 ? 487 ILE A CG2 1 
ATOM   2663  C  CD1 . ILE A 1 471 ? 168.732 126.379 138.160 1.00 105.19 ? 487 ILE A CD1 1 
ATOM   2664  N  N   . ALA A 1 472 ? 172.155 126.991 141.116 1.00 108.28 ? 488 ALA A N   1 
ATOM   2665  C  CA  . ALA A 1 472 ? 173.248 127.953 141.095 1.00 108.28 ? 488 ALA A CA  1 
ATOM   2666  C  C   . ALA A 1 472 ? 173.914 127.934 139.729 1.00 108.28 ? 488 ALA A C   1 
ATOM   2667  O  O   . ALA A 1 472 ? 174.268 126.867 139.218 1.00 108.28 ? 488 ALA A O   1 
ATOM   2668  C  CB  . ALA A 1 472 ? 174.276 127.648 142.188 1.00 108.28 ? 488 ALA A CB  1 
ATOM   2669  N  N   . SER A 1 473 ? 174.081 129.113 139.144 1.00 120.54 ? 489 SER A N   1 
ATOM   2670  C  CA  . SER A 1 473 ? 174.691 129.227 137.831 1.00 120.54 ? 489 SER A CA  1 
ATOM   2671  C  C   . SER A 1 473 ? 176.184 129.494 137.958 1.00 120.54 ? 489 SER A C   1 
ATOM   2672  O  O   . SER A 1 473 ? 176.645 130.147 138.898 1.00 120.54 ? 489 SER A O   1 
ATOM   2673  C  CB  . SER A 1 473 ? 174.028 130.343 137.022 1.00 120.54 ? 489 SER A CB  1 
ATOM   2674  O  OG  . SER A 1 473 ? 174.584 130.429 135.722 1.00 120.54 ? 489 SER A OG  1 
ATOM   2675  N  N   . CYS A 1 474 ? 176.937 128.977 136.997 1.00 135.49 ? 490 CYS A N   1 
ATOM   2676  C  CA  . CYS A 1 474 ? 178.376 129.169 136.904 1.00 135.49 ? 490 CYS A CA  1 
ATOM   2677  C  C   . CYS A 1 474 ? 178.682 129.908 135.605 1.00 135.49 ? 490 CYS A C   1 
ATOM   2678  O  O   . CYS A 1 474 ? 177.782 130.431 134.942 1.00 135.49 ? 490 CYS A O   1 
ATOM   2679  C  CB  . CYS A 1 474 ? 179.109 127.829 136.986 1.00 135.49 ? 490 CYS A CB  1 
ATOM   2680  S  SG  . CYS A 1 474 ? 180.911 127.968 136.985 1.00 135.49 ? 490 CYS A SG  1 
ATOM   2681  N  N   . ASN A 1 475 ? 179.973 129.980 135.266 1.00 147.01 ? 491 ASN A N   1 
ATOM   2682  C  CA  . ASN A 1 475 ? 180.391 130.694 134.062 1.00 147.01 ? 491 ASN A CA  1 
ATOM   2683  C  C   . ASN A 1 475 ? 179.602 130.236 132.842 1.00 147.01 ? 491 ASN A C   1 
ATOM   2684  O  O   . ASN A 1 475 ? 179.182 131.057 132.019 1.00 147.01 ? 491 ASN A O   1 
ATOM   2685  C  CB  . ASN A 1 475 ? 181.891 130.502 133.834 1.00 147.01 ? 491 ASN A CB  1 
ATOM   2686  N  N   . GLY A 1 476 ? 179.392 128.928 132.708 1.00 140.06 ? 492 GLY A N   1 
ATOM   2687  C  CA  . GLY A 1 476 ? 178.600 128.400 131.616 1.00 140.06 ? 492 GLY A CA  1 
ATOM   2688  C  C   . GLY A 1 476 ? 177.805 127.161 131.978 1.00 140.06 ? 492 GLY A C   1 
ATOM   2689  O  O   . GLY A 1 476 ? 177.238 126.507 131.098 1.00 140.06 ? 492 GLY A O   1 
ATOM   2690  N  N   . SER A 1 477 ? 177.750 126.825 133.266 1.00 127.66 ? 493 SER A N   1 
ATOM   2691  C  CA  . SER A 1 477 ? 177.140 125.584 133.720 1.00 127.66 ? 493 SER A CA  1 
ATOM   2692  C  C   . SER A 1 477 ? 176.114 125.860 134.810 1.00 127.66 ? 493 SER A C   1 
ATOM   2693  O  O   . SER A 1 477 ? 176.218 126.841 135.552 1.00 127.66 ? 493 SER A O   1 
ATOM   2694  C  CB  . SER A 1 477 ? 178.198 124.602 134.243 1.00 127.66 ? 493 SER A CB  1 
ATOM   2695  O  OG  . SER A 1 477 ? 179.279 124.488 133.335 1.00 127.66 ? 493 SER A OG  1 
ATOM   2696  N  N   . ILE A 1 478 ? 175.119 124.980 134.895 1.00 118.47 ? 494 ILE A N   1 
ATOM   2697  C  CA  . ILE A 1 478 ? 174.056 125.061 135.891 1.00 118.47 ? 494 ILE A CA  1 
ATOM   2698  C  C   . ILE A 1 478 ? 174.199 123.881 136.840 1.00 118.47 ? 494 ILE A C   1 
ATOM   2699  O  O   . ILE A 1 478 ? 174.213 122.724 136.401 1.00 118.47 ? 494 ILE A O   1 
ATOM   2700  C  CB  . ILE A 1 478 ? 172.665 125.058 135.234 1.00 118.47 ? 494 ILE A CB  1 
ATOM   2701  C  CG1 . ILE A 1 478 ? 172.605 126.082 134.102 1.00 118.47 ? 494 ILE A CG1 1 
ATOM   2702  C  CG2 . ILE A 1 478 ? 171.595 125.342 136.267 1.00 118.47 ? 494 ILE A CG2 1 
ATOM   2703  C  CD1 . ILE A 1 478 ? 171.260 126.145 133.411 1.00 118.47 ? 494 ILE A CD1 1 
ATOM   2704  N  N   . TYR A 1 479 ? 174.283 124.166 138.139 1.00 115.07 ? 495 TYR A N   1 
ATOM   2705  C  CA  . TYR A 1 479 ? 174.431 123.140 139.161 1.00 115.07 ? 495 TYR A CA  1 
ATOM   2706  C  C   . TYR A 1 479 ? 173.212 123.168 140.072 1.00 115.07 ? 495 TYR A C   1 
ATOM   2707  O  O   . TYR A 1 479 ? 172.899 124.206 140.667 1.00 115.07 ? 495 TYR A O   1 
ATOM   2708  C  CB  . TYR A 1 479 ? 175.710 123.357 139.971 1.00 115.07 ? 495 TYR A CB  1 
ATOM   2709  C  CG  . TYR A 1 479 ? 176.982 123.025 139.226 1.00 115.07 ? 495 TYR A CG  1 
ATOM   2710  C  CD1 . TYR A 1 479 ? 177.482 121.730 139.208 1.00 115.07 ? 495 TYR A CD1 1 
ATOM   2711  C  CD2 . TYR A 1 479 ? 177.690 124.009 138.550 1.00 115.07 ? 495 TYR A CD2 1 
ATOM   2712  C  CE1 . TYR A 1 479 ? 178.647 121.424 138.532 1.00 115.07 ? 495 TYR A CE1 1 
ATOM   2713  C  CE2 . TYR A 1 479 ? 178.855 123.713 137.872 1.00 115.07 ? 495 TYR A CE2 1 
ATOM   2714  C  CZ  . TYR A 1 479 ? 179.329 122.420 137.866 1.00 115.07 ? 495 TYR A CZ  1 
ATOM   2715  O  OH  . TYR A 1 479 ? 180.490 122.120 137.191 1.00 115.07 ? 495 TYR A OH  1 
ATOM   2716  N  N   . VAL A 1 480 ? 172.530 122.034 140.179 1.00 116.11 ? 496 VAL A N   1 
ATOM   2717  C  CA  . VAL A 1 480 ? 171.402 121.872 141.088 1.00 116.11 ? 496 VAL A CA  1 
ATOM   2718  C  C   . VAL A 1 480 ? 171.875 121.094 142.306 1.00 116.11 ? 496 VAL A C   1 
ATOM   2719  O  O   . VAL A 1 480 ? 172.619 120.113 142.182 1.00 116.11 ? 496 VAL A O   1 
ATOM   2720  C  CB  . VAL A 1 480 ? 170.224 121.160 140.398 1.00 116.11 ? 496 VAL A CB  1 
ATOM   2721  C  CG1 . VAL A 1 480 ? 168.970 121.264 141.249 1.00 116.11 ? 496 VAL A CG1 1 
ATOM   2722  C  CG2 . VAL A 1 480 ? 169.987 121.744 139.014 1.00 116.11 ? 496 VAL A CG2 1 
ATOM   2723  N  N   . PHE A 1 481 ? 171.457 121.532 143.489 1.00 115.15 ? 497 PHE A N   1 
ATOM   2724  C  CA  . PHE A 1 481 ? 171.887 120.920 144.734 1.00 115.15 ? 497 PHE A CA  1 
ATOM   2725  C  C   . PHE A 1 481 ? 170.668 120.532 145.554 1.00 115.15 ? 497 PHE A C   1 
ATOM   2726  O  O   . PHE A 1 481 ? 169.678 121.269 145.597 1.00 115.15 ? 497 PHE A O   1 
ATOM   2727  C  CB  . PHE A 1 481 ? 172.773 121.868 145.548 1.00 115.15 ? 497 PHE A CB  1 
ATOM   2728  C  CG  . PHE A 1 481 ? 174.029 122.293 144.842 1.00 115.15 ? 497 PHE A CG  1 
ATOM   2729  C  CD1 . PHE A 1 481 ? 174.018 123.369 143.971 1.00 115.15 ? 497 PHE A CD1 1 
ATOM   2730  C  CD2 . PHE A 1 481 ? 175.221 121.623 145.055 1.00 115.15 ? 497 PHE A CD2 1 
ATOM   2731  C  CE1 . PHE A 1 481 ? 175.170 123.767 143.327 1.00 115.15 ? 497 PHE A CE1 1 
ATOM   2732  C  CE2 . PHE A 1 481 ? 176.377 122.016 144.409 1.00 115.15 ? 497 PHE A CE2 1 
ATOM   2733  C  CZ  . PHE A 1 481 ? 176.351 123.089 143.544 1.00 115.15 ? 497 PHE A CZ  1 
ATOM   2734  N  N   . ARG A 1 482 ? 170.745 119.375 146.203 1.00 131.68 ? 498 ARG A N   1 
ATOM   2735  C  CA  . ARG A 1 482 ? 169.674 118.922 147.076 1.00 131.68 ? 498 ARG A CA  1 
ATOM   2736  C  C   . ARG A 1 482 ? 169.798 119.591 148.438 1.00 131.68 ? 498 ARG A C   1 
ATOM   2737  O  O   . ARG A 1 482 ? 170.906 119.832 148.926 1.00 131.68 ? 498 ARG A O   1 
ATOM   2738  C  CB  . ARG A 1 482 ? 169.713 117.402 147.230 1.00 131.68 ? 498 ARG A CB  1 
ATOM   2739  N  N   . ASP A 1 483 ? 168.650 119.899 149.047 1.00 130.66 ? 499 ASP A N   1 
ATOM   2740  C  CA  . ASP A 1 483 ? 168.660 120.524 150.366 1.00 130.66 ? 499 ASP A CA  1 
ATOM   2741  C  C   . ASP A 1 483 ? 169.362 119.640 151.389 1.00 130.66 ? 499 ASP A C   1 
ATOM   2742  O  O   . ASP A 1 483 ? 170.085 120.138 152.260 1.00 130.66 ? 499 ASP A O   1 
ATOM   2743  C  CB  . ASP A 1 483 ? 167.232 120.833 150.813 1.00 130.66 ? 499 ASP A CB  1 
ATOM   2744  N  N   . ARG A 1 484 ? 169.162 118.329 151.299 1.00 136.31 ? 500 ARG A N   1 
ATOM   2745  C  CA  . ARG A 1 484 ? 169.821 117.365 152.168 1.00 136.31 ? 500 ARG A CA  1 
ATOM   2746  C  C   . ARG A 1 484 ? 170.701 116.450 151.329 1.00 136.31 ? 500 ARG A C   1 
ATOM   2747  O  O   . ARG A 1 484 ? 170.294 116.002 150.252 1.00 136.31 ? 500 ARG A O   1 
ATOM   2748  C  CB  . ARG A 1 484 ? 168.801 116.538 152.957 1.00 136.31 ? 500 ARG A CB  1 
ATOM   2749  N  N   . TYR A 1 485 ? 171.909 116.191 151.821 1.00 138.03 ? 501 TYR A N   1 
ATOM   2750  C  CA  . TYR A 1 485 ? 172.875 115.353 151.116 1.00 138.03 ? 501 TYR A CA  1 
ATOM   2751  C  C   . TYR A 1 485 ? 172.312 113.968 150.809 1.00 138.03 ? 501 TYR A C   1 
ATOM   2752  O  O   . TYR A 1 485 ? 172.015 113.650 149.657 1.00 138.03 ? 501 TYR A O   1 
ATOM   2753  C  CB  . TYR A 1 485 ? 174.162 115.222 151.934 1.00 138.03 ? 501 TYR A CB  1 
ATOM   2754  N  N   . ALA A 1 490 ? 172.765 111.221 145.141 1.00 138.64 ? 506 ALA A N   1 
ATOM   2755  C  CA  . ALA A 1 490 ? 173.797 112.216 144.872 1.00 138.64 ? 506 ALA A CA  1 
ATOM   2756  C  C   . ALA A 1 490 ? 173.419 113.568 145.468 1.00 138.64 ? 506 ALA A C   1 
ATOM   2757  O  O   . ALA A 1 490 ? 172.240 113.917 145.540 1.00 138.64 ? 506 ALA A O   1 
ATOM   2758  C  CB  . ALA A 1 490 ? 174.033 112.343 143.377 1.00 138.64 ? 506 ALA A CB  1 
ATOM   2759  N  N   . ASN A 1 491 ? 174.427 114.326 145.897 1.00 130.95 ? 507 ASN A N   1 
ATOM   2760  C  CA  . ASN A 1 491 ? 174.198 115.631 146.499 1.00 130.95 ? 507 ASN A CA  1 
ATOM   2761  C  C   . ASN A 1 491 ? 174.214 116.774 145.493 1.00 130.95 ? 507 ASN A C   1 
ATOM   2762  O  O   . ASN A 1 491 ? 173.623 117.825 145.766 1.00 130.95 ? 507 ASN A O   1 
ATOM   2763  C  CB  . ASN A 1 491 ? 175.244 115.902 147.585 1.00 130.95 ? 507 ASN A CB  1 
ATOM   2764  N  N   . THR A 1 492 ? 174.866 116.602 144.345 1.00 138.84 ? 508 THR A N   1 
ATOM   2765  C  CA  . THR A 1 492 ? 174.944 117.651 143.340 1.00 138.84 ? 508 THR A CA  1 
ATOM   2766  C  C   . THR A 1 492 ? 174.681 117.061 141.962 1.00 138.84 ? 508 THR A C   1 
ATOM   2767  O  O   . THR A 1 492 ? 174.992 115.897 141.697 1.00 138.84 ? 508 THR A O   1 
ATOM   2768  C  CB  . THR A 1 492 ? 176.312 118.350 143.362 1.00 138.84 ? 508 THR A CB  1 
ATOM   2769  O  OG1 . THR A 1 492 ? 176.406 119.261 142.260 1.00 138.84 ? 508 THR A OG1 1 
ATOM   2770  C  CG2 . THR A 1 492 ? 177.439 117.333 143.278 1.00 138.84 ? 508 THR A CG2 1 
ATOM   2771  N  N   . TYR A 1 493 ? 174.095 117.878 141.087 1.00 126.86 ? 509 TYR A N   1 
ATOM   2772  C  CA  . TYR A 1 493 ? 173.786 117.479 139.723 1.00 126.86 ? 509 TYR A CA  1 
ATOM   2773  C  C   . TYR A 1 493 ? 174.106 118.632 138.784 1.00 126.86 ? 509 TYR A C   1 
ATOM   2774  O  O   . TYR A 1 493 ? 174.085 119.797 139.186 1.00 126.86 ? 509 TYR A O   1 
ATOM   2775  C  CB  . TYR A 1 493 ? 172.311 117.073 139.577 1.00 126.86 ? 509 TYR A CB  1 
ATOM   2776  C  CG  . TYR A 1 493 ? 171.845 116.043 140.586 1.00 126.86 ? 509 TYR A CG  1 
ATOM   2777  C  CD1 . TYR A 1 493 ? 171.451 116.421 141.864 1.00 126.86 ? 509 TYR A CD1 1 
ATOM   2778  C  CD2 . TYR A 1 493 ? 171.810 114.693 140.265 1.00 126.86 ? 509 TYR A CD2 1 
ATOM   2779  C  CE1 . TYR A 1 493 ? 171.030 115.486 142.788 1.00 126.86 ? 509 TYR A CE1 1 
ATOM   2780  C  CE2 . TYR A 1 493 ? 171.387 113.751 141.183 1.00 126.86 ? 509 TYR A CE2 1 
ATOM   2781  C  CZ  . TYR A 1 493 ? 170.999 114.153 142.443 1.00 126.86 ? 509 TYR A CZ  1 
ATOM   2782  O  OH  . TYR A 1 493 ? 170.579 113.219 143.362 1.00 126.86 ? 509 TYR A OH  1 
ATOM   2783  N  N   . LYS A 1 494 ? 174.378 118.305 137.525 1.00 125.45 ? 510 LYS A N   1 
ATOM   2784  C  CA  . LYS A 1 494 ? 174.649 119.291 136.489 1.00 125.45 ? 510 LYS A CA  1 
ATOM   2785  C  C   . LYS A 1 494 ? 173.541 119.241 135.449 1.00 125.45 ? 510 LYS A C   1 
ATOM   2786  O  O   . LYS A 1 494 ? 173.241 118.172 134.904 1.00 125.45 ? 510 LYS A O   1 
ATOM   2787  C  CB  . LYS A 1 494 ? 176.006 119.040 135.827 1.00 125.45 ? 510 LYS A CB  1 
ATOM   2788  C  CG  . LYS A 1 494 ? 176.268 119.903 134.605 1.00 125.45 ? 510 LYS A CG  1 
ATOM   2789  C  CD  . LYS A 1 494 ? 177.752 119.972 134.283 1.00 125.45 ? 510 LYS A CD  1 
ATOM   2790  C  CE  . LYS A 1 494 ? 178.006 120.772 133.014 1.00 125.45 ? 510 LYS A CE  1 
ATOM   2791  N  NZ  . LYS A 1 494 ? 176.763 121.400 132.487 1.00 125.45 ? 510 LYS A NZ  1 
ATOM   2792  N  N   . LEU A 1 495 ? 172.923 120.391 135.198 1.00 121.62 ? 511 LEU A N   1 
ATOM   2793  C  CA  . LEU A 1 495 ? 171.784 120.499 134.299 1.00 121.62 ? 511 LEU A CA  1 
ATOM   2794  C  C   . LEU A 1 495 ? 172.269 121.017 132.951 1.00 121.62 ? 511 LEU A C   1 
ATOM   2795  O  O   . LEU A 1 495 ? 172.861 122.098 132.875 1.00 121.62 ? 511 LEU A O   1 
ATOM   2796  C  CB  . LEU A 1 495 ? 170.722 121.430 134.889 1.00 121.62 ? 511 LEU A CB  1 
ATOM   2797  C  CG  . LEU A 1 495 ? 169.262 121.397 134.420 1.00 121.62 ? 511 LEU A CG  1 
ATOM   2798  C  CD1 . LEU A 1 495 ? 168.481 122.454 135.175 1.00 121.62 ? 511 LEU A CD1 1 
ATOM   2799  C  CD2 . LEU A 1 495 ? 169.091 121.600 132.920 1.00 121.62 ? 511 LEU A CD2 1 
ATOM   2800  N  N   . ASP A 1 496 ? 172.016 120.247 131.893 1.00 147.09 ? 512 ASP A N   1 
ATOM   2801  C  CA  . ASP A 1 496 ? 172.332 120.686 130.541 1.00 147.09 ? 512 ASP A CA  1 
ATOM   2802  C  C   . ASP A 1 496 ? 171.105 121.390 129.981 1.00 147.09 ? 512 ASP A C   1 
ATOM   2803  O  O   . ASP A 1 496 ? 170.074 120.736 129.773 1.00 147.09 ? 512 ASP A O   1 
ATOM   2804  C  CB  . ASP A 1 496 ? 172.722 119.506 129.663 1.00 147.09 ? 512 ASP A CB  1 
ATOM   2805  C  CG  . ASP A 1 496 ? 173.136 119.932 128.269 1.00 147.09 ? 512 ASP A CG  1 
ATOM   2806  O  OD1 . ASP A 1 496 ? 173.724 121.026 128.132 1.00 147.09 ? 512 ASP A OD1 1 
ATOM   2807  O  OD2 . ASP A 1 496 ? 172.875 119.176 127.310 1.00 147.09 ? 512 ASP A OD2 1 
ATOM   2808  N  N   . PRO A 1 497 ? 171.157 122.701 129.729 1.00 131.94 ? 513 PRO A N   1 
ATOM   2809  C  CA  . PRO A 1 497 ? 169.950 123.398 129.249 1.00 131.94 ? 513 PRO A CA  1 
ATOM   2810  C  C   . PRO A 1 497 ? 169.413 122.866 127.932 1.00 131.94 ? 513 PRO A C   1 
ATOM   2811  O  O   . PRO A 1 497 ? 168.191 122.818 127.740 1.00 131.94 ? 513 PRO A O   1 
ATOM   2812  C  CB  . PRO A 1 497 ? 170.419 124.855 129.122 1.00 131.94 ? 513 PRO A CB  1 
ATOM   2813  C  CG  . PRO A 1 497 ? 171.677 124.945 129.931 1.00 131.94 ? 513 PRO A CG  1 
ATOM   2814  C  CD  . PRO A 1 497 ? 172.315 123.601 129.843 1.00 131.94 ? 513 PRO A CD  1 
ATOM   2815  N  N   . ALA A 1 498 ? 170.294 122.469 127.013 1.00 146.27 ? 514 ALA A N   1 
ATOM   2816  C  CA  . ALA A 1 498 ? 169.850 122.043 125.690 1.00 146.27 ? 514 ALA A CA  1 
ATOM   2817  C  C   . ALA A 1 498 ? 169.115 120.709 125.751 1.00 146.27 ? 514 ALA A C   1 
ATOM   2818  O  O   . ALA A 1 498 ? 168.028 120.560 125.181 1.00 146.27 ? 514 ALA A O   1 
ATOM   2819  C  CB  . ALA A 1 498 ? 171.045 121.958 124.740 1.00 146.27 ? 514 ALA A CB  1 
ATOM   2820  N  N   . THR A 1 499 ? 169.696 119.726 126.438 1.00 142.59 ? 515 THR A N   1 
ATOM   2821  C  CA  . THR A 1 499 ? 169.139 118.382 126.512 1.00 142.59 ? 515 THR A CA  1 
ATOM   2822  C  C   . THR A 1 499 ? 168.316 118.123 127.767 1.00 142.59 ? 515 THR A C   1 
ATOM   2823  O  O   . THR A 1 499 ? 167.664 117.075 127.846 1.00 142.59 ? 515 THR A O   1 
ATOM   2824  C  CB  . THR A 1 499 ? 170.262 117.339 126.428 1.00 142.59 ? 515 THR A CB  1 
ATOM   2825  N  N   . SER A 1 500 ? 168.329 119.033 128.742 1.00 130.64 ? 516 SER A N   1 
ATOM   2826  C  CA  . SER A 1 500 ? 167.624 118.863 130.013 1.00 130.64 ? 516 SER A CA  1 
ATOM   2827  C  C   . SER A 1 500 ? 168.060 117.602 130.753 1.00 130.64 ? 516 SER A C   1 
ATOM   2828  O  O   . SER A 1 500 ? 167.317 117.078 131.588 1.00 130.64 ? 516 SER A O   1 
ATOM   2829  C  CB  . SER A 1 500 ? 166.103 118.859 129.815 1.00 130.64 ? 516 SER A CB  1 
ATOM   2830  O  OG  . SER A 1 500 ? 165.428 118.913 131.060 1.00 130.64 ? 516 SER A OG  1 
ATOM   2831  N  N   . ALA A 1 501 ? 169.260 117.107 130.458 1.00 127.40 ? 517 ALA A N   1 
ATOM   2832  C  CA  . ALA A 1 501 ? 169.764 115.870 131.039 1.00 127.40 ? 517 ALA A CA  1 
ATOM   2833  C  C   . ALA A 1 501 ? 170.525 116.181 132.322 1.00 127.40 ? 517 ALA A C   1 
ATOM   2834  O  O   . ALA A 1 501 ? 171.520 116.914 132.301 1.00 127.40 ? 517 ALA A O   1 
ATOM   2835  C  CB  . ALA A 1 501 ? 170.662 115.134 130.046 1.00 127.40 ? 517 ALA A CB  1 
ATOM   2836  N  N   . VAL A 1 502 ? 170.056 115.622 133.433 1.00 128.20 ? 518 VAL A N   1 
ATOM   2837  C  CA  . VAL A 1 502 ? 170.699 115.789 134.733 1.00 128.20 ? 518 VAL A CA  1 
ATOM   2838  C  C   . VAL A 1 502 ? 171.826 114.764 134.828 1.00 128.20 ? 518 VAL A C   1 
ATOM   2839  O  O   . VAL A 1 502 ? 171.581 113.556 134.845 1.00 128.20 ? 518 VAL A O   1 
ATOM   2840  C  CB  . VAL A 1 502 ? 169.693 115.629 135.879 1.00 128.20 ? 518 VAL A CB  1 
ATOM   2841  C  CG1 . VAL A 1 502 ? 170.398 115.252 137.167 1.00 128.20 ? 518 VAL A CG1 1 
ATOM   2842  C  CG2 . VAL A 1 502 ? 168.894 116.911 136.062 1.00 128.20 ? 518 VAL A CG2 1 
ATOM   2843  N  N   . THR A 1 503 ? 173.068 115.244 134.861 1.00 127.73 ? 519 THR A N   1 
ATOM   2844  C  CA  . THR A 1 503 ? 174.246 114.386 134.938 1.00 127.73 ? 519 THR A CA  1 
ATOM   2845  C  C   . THR A 1 503 ? 174.941 114.570 136.282 1.00 127.73 ? 519 THR A C   1 
ATOM   2846  O  O   . THR A 1 503 ? 175.270 115.697 136.666 1.00 127.73 ? 519 THR A O   1 
ATOM   2847  C  CB  . THR A 1 503 ? 175.215 114.690 133.796 1.00 127.73 ? 519 THR A CB  1 
ATOM   2848  O  OG1 . THR A 1 503 ? 176.038 115.808 134.152 1.00 127.73 ? 519 THR A OG1 1 
ATOM   2849  C  CG2 . THR A 1 503 ? 174.451 115.020 132.524 1.00 127.73 ? 519 THR A CG2 1 
ATOM   2850  N  N   . VAL A 1 504 ? 175.133 113.468 137.005 1.00 133.74 ? 520 VAL A N   1 
ATOM   2851  C  CA  . VAL A 1 504 ? 175.787 113.527 138.307 1.00 133.74 ? 520 VAL A CA  1 
ATOM   2852  C  C   . VAL A 1 504 ? 177.258 113.872 138.117 1.00 133.74 ? 520 VAL A C   1 
ATOM   2853  O  O   . VAL A 1 504 ? 177.960 113.250 137.309 1.00 133.74 ? 520 VAL A O   1 
ATOM   2854  C  CB  . VAL A 1 504 ? 175.618 112.197 139.056 1.00 133.74 ? 520 VAL A CB  1 
ATOM   2855  C  CG1 . VAL A 1 504 ? 174.265 112.146 139.741 1.00 133.74 ? 520 VAL A CG1 1 
ATOM   2856  C  CG2 . VAL A 1 504 ? 175.780 111.023 138.103 1.00 133.74 ? 520 VAL A CG2 1 
ATOM   2857  N  N   . THR A 1 505 ? 177.731 114.868 138.858 1.00 129.51 ? 521 THR A N   1 
ATOM   2858  C  CA  . THR A 1 505 ? 179.124 115.292 138.759 1.00 129.51 ? 521 THR A CA  1 
ATOM   2859  C  C   . THR A 1 505 ? 180.000 114.535 139.750 1.00 129.51 ? 521 THR A C   1 
ATOM   2860  O  O   . THR A 1 505 ? 181.073 115.004 140.129 1.00 129.51 ? 521 THR A O   1 
ATOM   2861  C  CB  . THR A 1 505 ? 179.277 116.804 139.007 1.00 129.51 ? 521 THR A CB  1 
ATOM   2862  O  OG1 . THR A 1 505 ? 178.773 117.132 140.307 1.00 129.51 ? 521 THR A OG1 1 
ATOM   2863  C  CG2 . THR A 1 505 ? 178.518 117.594 137.958 1.00 129.51 ? 521 THR A CG2 1 
ATOM   2864  N  N   . LYS A 1 509 ? 182.342 116.475 145.621 1.00 143.67 ? 525 LYS A N   1 
ATOM   2865  C  CA  . LYS A 1 509 ? 182.742 116.423 147.022 1.00 143.67 ? 525 LYS A CA  1 
ATOM   2866  C  C   . LYS A 1 509 ? 181.840 117.298 147.885 1.00 143.67 ? 525 LYS A C   1 
ATOM   2867  O  O   . LYS A 1 509 ? 181.811 118.518 147.731 1.00 143.67 ? 525 LYS A O   1 
ATOM   2868  C  CB  . LYS A 1 509 ? 184.200 116.860 147.177 1.00 143.67 ? 525 LYS A CB  1 
ATOM   2869  N  N   . VAL A 1 510 ? 181.098 116.664 148.790 1.00 162.28 ? 526 VAL A N   1 
ATOM   2870  C  CA  . VAL A 1 510 ? 180.192 117.356 149.699 1.00 162.28 ? 526 VAL A CA  1 
ATOM   2871  C  C   . VAL A 1 510 ? 180.467 116.864 151.112 1.00 162.28 ? 526 VAL A C   1 
ATOM   2872  O  O   . VAL A 1 510 ? 180.494 115.653 151.356 1.00 162.28 ? 526 VAL A O   1 
ATOM   2873  C  CB  . VAL A 1 510 ? 178.715 117.127 149.324 1.00 162.28 ? 526 VAL A CB  1 
ATOM   2874  N  N   . LEU A 1 511 ? 180.661 117.801 152.042 1.00 153.72 ? 527 LEU A N   1 
ATOM   2875  C  CA  . LEU A 1 511 ? 180.928 117.470 153.437 1.00 153.72 ? 527 LEU A CA  1 
ATOM   2876  C  C   . LEU A 1 511 ? 179.936 118.119 154.393 1.00 153.72 ? 527 LEU A C   1 
ATOM   2877  O  O   . LEU A 1 511 ? 180.187 118.146 155.604 1.00 153.72 ? 527 LEU A O   1 
ATOM   2878  C  CB  . LEU A 1 511 ? 182.352 117.883 153.823 1.00 153.72 ? 527 LEU A CB  1 
ATOM   2879  C  CG  . LEU A 1 511 ? 183.450 117.699 152.777 1.00 153.72 ? 527 LEU A CG  1 
ATOM   2880  C  CD1 . LEU A 1 511 ? 184.757 118.289 153.279 1.00 153.72 ? 527 LEU A CD1 1 
ATOM   2881  C  CD2 . LEU A 1 511 ? 183.621 116.228 152.432 1.00 153.72 ? 527 LEU A CD2 1 
ATOM   2882  N  N   . LEU A 1 512 ? 178.826 118.645 153.889 1.00 146.50 ? 528 LEU A N   1 
ATOM   2883  C  CA  . LEU A 1 512 ? 177.845 119.343 154.708 1.00 146.50 ? 528 LEU A CA  1 
ATOM   2884  C  C   . LEU A 1 512 ? 176.525 118.580 154.728 1.00 146.50 ? 528 LEU A C   1 
ATOM   2885  O  O   . LEU A 1 512 ? 176.009 118.183 153.678 1.00 146.50 ? 528 LEU A O   1 
ATOM   2886  C  CB  . LEU A 1 512 ? 177.676 120.791 154.222 1.00 146.50 ? 528 LEU A CB  1 
ATOM   2887  C  CG  . LEU A 1 512 ? 177.473 121.246 152.763 1.00 146.50 ? 528 LEU A CG  1 
ATOM   2888  C  CD1 . LEU A 1 512 ? 176.288 120.636 152.033 1.00 146.50 ? 528 LEU A CD1 1 
ATOM   2889  C  CD2 . LEU A 1 512 ? 177.410 122.766 152.689 1.00 146.50 ? 528 LEU A CD2 1 
ATOM   2890  N  N   . THR A 1 513 ? 176.020 118.318 155.936 1.00 145.04 ? 529 THR A N   1 
ATOM   2891  C  CA  . THR A 1 513 ? 174.753 117.605 156.068 1.00 145.04 ? 529 THR A CA  1 
ATOM   2892  C  C   . THR A 1 513 ? 173.592 118.430 155.525 1.00 145.04 ? 529 THR A C   1 
ATOM   2893  O  O   . THR A 1 513 ? 172.687 117.888 154.879 1.00 145.04 ? 529 THR A O   1 
ATOM   2894  C  CB  . THR A 1 513 ? 174.512 117.210 157.527 1.00 145.04 ? 529 THR A CB  1 
ATOM   2895  O  OG1 . THR A 1 513 ? 173.185 116.691 157.672 1.00 145.04 ? 529 THR A OG1 1 
ATOM   2896  C  CG2 . THR A 1 513 ? 174.699 118.398 158.460 1.00 145.04 ? 529 THR A CG2 1 
ATOM   2897  N  N   . ASN A 1 514 ? 173.603 119.739 155.766 1.00 142.32 ? 530 ASN A N   1 
ATOM   2898  C  CA  . ASN A 1 514 ? 172.510 120.620 155.390 1.00 142.32 ? 530 ASN A CA  1 
ATOM   2899  C  C   . ASN A 1 514 ? 173.007 121.643 154.376 1.00 142.32 ? 530 ASN A C   1 
ATOM   2900  O  O   . ASN A 1 514 ? 174.212 121.850 154.209 1.00 142.32 ? 530 ASN A O   1 
ATOM   2901  C  CB  . ASN A 1 514 ? 171.921 121.330 156.617 1.00 142.32 ? 530 ASN A CB  1 
ATOM   2902  C  CG  . ASN A 1 514 ? 170.514 121.844 156.377 1.00 142.32 ? 530 ASN A CG  1 
ATOM   2903  O  OD1 . ASN A 1 514 ? 170.181 122.296 155.281 1.00 142.32 ? 530 ASN A OD1 1 
ATOM   2904  N  ND2 . ASN A 1 514 ? 169.679 121.779 157.408 1.00 142.32 ? 530 ASN A ND2 1 
ATOM   2905  N  N   . LEU A 1 515 ? 172.057 122.274 153.685 1.00 123.10 ? 531 LEU A N   1 
ATOM   2906  C  CA  . LEU A 1 515 ? 172.358 123.246 152.630 1.00 123.10 ? 531 LEU A CA  1 
ATOM   2907  C  C   . LEU A 1 515 ? 171.409 124.433 152.781 1.00 123.10 ? 531 LEU A C   1 
ATOM   2908  O  O   . LEU A 1 515 ? 170.298 124.422 152.245 1.00 123.10 ? 531 LEU A O   1 
ATOM   2909  C  CB  . LEU A 1 515 ? 172.231 122.595 151.262 1.00 123.10 ? 531 LEU A CB  1 
ATOM   2910  C  CG  . LEU A 1 515 ? 172.873 123.291 150.069 1.00 123.10 ? 531 LEU A CG  1 
ATOM   2911  C  CD1 . LEU A 1 515 ? 174.364 123.015 150.008 1.00 123.10 ? 531 LEU A CD1 1 
ATOM   2912  C  CD2 . LEU A 1 515 ? 172.185 122.808 148.818 1.00 123.10 ? 531 LEU A CD2 1 
ATOM   2913  N  N   . GLN A 1 516 ? 171.851 125.455 153.512 1.00 105.58 ? 532 GLN A N   1 
ATOM   2914  C  CA  . GLN A 1 516 ? 170.984 126.603 153.754 1.00 105.58 ? 532 GLN A CA  1 
ATOM   2915  C  C   . GLN A 1 516 ? 170.977 127.566 152.572 1.00 105.58 ? 532 GLN A C   1 
ATOM   2916  O  O   . GLN A 1 516 ? 169.908 127.960 152.093 1.00 105.58 ? 532 GLN A O   1 
ATOM   2917  C  CB  . GLN A 1 516 ? 171.406 127.325 155.035 1.00 105.58 ? 532 GLN A CB  1 
ATOM   2918  C  CG  . GLN A 1 516 ? 170.457 128.441 155.447 1.00 105.58 ? 532 GLN A CG  1 
ATOM   2919  C  CD  . GLN A 1 516 ? 170.925 129.184 156.683 1.00 105.58 ? 532 GLN A CD  1 
ATOM   2920  O  OE1 . GLN A 1 516 ? 172.095 129.549 156.796 1.00 105.58 ? 532 GLN A OE1 1 
ATOM   2921  N  NE2 . GLN A 1 516 ? 170.011 129.409 157.620 1.00 105.58 ? 532 GLN A NE2 1 
ATOM   2922  N  N   . PHE A 1 517 ? 172.154 127.957 152.085 1.00 94.33  ? 533 PHE A N   1 
ATOM   2923  C  CA  . PHE A 1 517 ? 172.247 128.912 150.986 1.00 94.33  ? 533 PHE A CA  1 
ATOM   2924  C  C   . PHE A 1 517 ? 173.157 128.388 149.887 1.00 94.33  ? 533 PHE A C   1 
ATOM   2925  O  O   . PHE A 1 517 ? 174.168 127.745 150.169 1.00 94.33  ? 533 PHE A O   1 
ATOM   2926  C  CB  . PHE A 1 517 ? 172.774 130.268 151.474 1.00 94.33  ? 533 PHE A CB  1 
ATOM   2927  C  CG  . PHE A 1 517 ? 171.758 131.086 152.215 1.00 94.33  ? 533 PHE A CG  1 
ATOM   2928  C  CD1 . PHE A 1 517 ? 170.802 131.813 151.529 1.00 94.33  ? 533 PHE A CD1 1 
ATOM   2929  C  CD2 . PHE A 1 517 ? 171.764 131.136 153.599 1.00 94.33  ? 533 PHE A CD2 1 
ATOM   2930  C  CE1 . PHE A 1 517 ? 169.866 132.569 152.207 1.00 94.33  ? 533 PHE A CE1 1 
ATOM   2931  C  CE2 . PHE A 1 517 ? 170.830 131.890 154.283 1.00 94.33  ? 533 PHE A CE2 1 
ATOM   2932  C  CZ  . PHE A 1 517 ? 169.880 132.608 153.586 1.00 94.33  ? 533 PHE A CZ  1 
ATOM   2933  N  N   . VAL A 1 518 ? 172.796 128.666 148.634 1.00 105.13 ? 534 VAL A N   1 
ATOM   2934  C  CA  . VAL A 1 518 ? 173.632 128.338 147.478 1.00 105.13 ? 534 VAL A CA  1 
ATOM   2935  C  C   . VAL A 1 518 ? 173.748 129.608 146.638 1.00 105.13 ? 534 VAL A C   1 
ATOM   2936  O  O   . VAL A 1 518 ? 172.907 129.880 145.775 1.00 105.13 ? 534 VAL A O   1 
ATOM   2937  C  CB  . VAL A 1 518 ? 173.073 127.180 146.648 1.00 105.13 ? 534 VAL A CB  1 
ATOM   2938  C  CG1 . VAL A 1 518 ? 174.117 126.693 145.656 1.00 105.13 ? 534 VAL A CG1 1 
ATOM   2939  C  CG2 . VAL A 1 518 ? 172.623 126.053 147.547 1.00 105.13 ? 534 VAL A CG2 1 
ATOM   2940  N  N   . LEU A 1 519 ? 174.793 130.393 146.881 1.00 103.77 ? 535 LEU A N   1 
ATOM   2941  C  CA  . LEU A 1 519 ? 174.951 131.656 146.179 1.00 103.77 ? 535 LEU A CA  1 
ATOM   2942  C  C   . LEU A 1 519 ? 175.518 131.428 144.782 1.00 103.77 ? 535 LEU A C   1 
ATOM   2943  O  O   . LEU A 1 519 ? 176.036 130.357 144.458 1.00 103.77 ? 535 LEU A O   1 
ATOM   2944  C  CB  . LEU A 1 519 ? 175.851 132.615 146.960 1.00 103.77 ? 535 LEU A CB  1 
ATOM   2945  C  CG  . LEU A 1 519 ? 175.395 133.051 148.355 1.00 103.77 ? 535 LEU A CG  1 
ATOM   2946  C  CD1 . LEU A 1 519 ? 173.906 133.368 148.358 1.00 103.77 ? 535 LEU A CD1 1 
ATOM   2947  C  CD2 . LEU A 1 519 ? 175.735 132.025 149.419 1.00 103.77 ? 535 LEU A CD2 1 
ATOM   2948  N  N   . ALA A 1 520 ? 175.396 132.457 143.947 1.00 128.35 ? 536 ALA A N   1 
ATOM   2949  C  CA  . ALA A 1 520 ? 175.837 132.407 142.554 1.00 128.35 ? 536 ALA A CA  1 
ATOM   2950  C  C   . ALA A 1 520 ? 177.298 131.984 142.416 1.00 128.35 ? 536 ALA A C   1 
ATOM   2951  O  O   . ALA A 1 520 ? 177.739 131.596 141.335 1.00 128.35 ? 536 ALA A O   1 
ATOM   2952  C  CB  . ALA A 1 520 ? 175.622 133.757 141.890 1.00 128.35 ? 536 ALA A CB  1 
ATOM   2953  O  OXT . ALA A 1 520 ? 178.072 132.019 143.372 1.00 128.35 ? 536 ALA A OXT 1 
ATOM   2954  N  N   . LYS B 2 9   ? 116.236 124.733 190.461 1.00 151.05 ? 9   LYS D N   1 
ATOM   2955  C  CA  . LYS B 2 9   ? 116.949 124.755 189.190 1.00 151.05 ? 9   LYS D CA  1 
ATOM   2956  C  C   . LYS B 2 9   ? 118.106 125.749 189.228 1.00 151.05 ? 9   LYS D C   1 
ATOM   2957  O  O   . LYS B 2 9   ? 118.891 125.769 190.176 1.00 151.05 ? 9   LYS D O   1 
ATOM   2958  C  CB  . LYS B 2 9   ? 115.994 125.099 188.045 1.00 151.05 ? 9   LYS D CB  1 
ATOM   2959  N  N   . LYS B 2 10  ? 118.203 126.573 188.188 1.00 149.35 ? 10  LYS D N   1 
ATOM   2960  C  CA  . LYS B 2 10  ? 119.259 127.575 188.056 1.00 149.35 ? 10  LYS D CA  1 
ATOM   2961  C  C   . LYS B 2 10  ? 118.724 128.908 188.568 1.00 149.35 ? 10  LYS D C   1 
ATOM   2962  O  O   . LYS B 2 10  ? 117.935 129.572 187.891 1.00 149.35 ? 10  LYS D O   1 
ATOM   2963  C  CB  . LYS B 2 10  ? 119.728 127.680 186.609 1.00 149.35 ? 10  LYS D CB  1 
ATOM   2964  N  N   . LYS B 2 11  ? 119.143 129.291 189.774 1.00 140.29 ? 11  LYS D N   1 
ATOM   2965  C  CA  . LYS B 2 11  ? 118.686 130.542 190.366 1.00 140.29 ? 11  LYS D CA  1 
ATOM   2966  C  C   . LYS B 2 11  ? 119.147 131.719 189.514 1.00 140.29 ? 11  LYS D C   1 
ATOM   2967  O  O   . LYS B 2 11  ? 120.322 131.808 189.146 1.00 140.29 ? 11  LYS D O   1 
ATOM   2968  C  CB  . LYS B 2 11  ? 119.259 130.659 191.779 1.00 140.29 ? 11  LYS D CB  1 
ATOM   2969  C  CG  . LYS B 2 11  ? 118.653 131.721 192.674 1.00 140.29 ? 11  LYS D CG  1 
ATOM   2970  C  CD  . LYS B 2 11  ? 117.210 131.417 193.012 1.00 140.29 ? 11  LYS D CD  1 
ATOM   2971  C  CE  . LYS B 2 11  ? 116.744 132.279 194.174 1.00 140.29 ? 11  LYS D CE  1 
ATOM   2972  N  NZ  . LYS B 2 11  ? 115.484 131.763 194.779 1.00 140.29 ? 11  LYS D NZ  1 
ATOM   2973  N  N   . VAL B 2 12  ? 118.226 132.631 189.203 1.00 131.67 ? 12  VAL D N   1 
ATOM   2974  C  CA  . VAL B 2 12  ? 118.532 133.787 188.368 1.00 131.67 ? 12  VAL D CA  1 
ATOM   2975  C  C   . VAL B 2 12  ? 118.144 135.068 189.096 1.00 131.67 ? 12  VAL D C   1 
ATOM   2976  O  O   . VAL B 2 12  ? 117.140 135.105 189.816 1.00 131.67 ? 12  VAL D O   1 
ATOM   2977  C  CB  . VAL B 2 12  ? 117.812 133.692 187.004 1.00 131.67 ? 12  VAL D CB  1 
ATOM   2978  C  CG1 . VAL B 2 12  ? 118.138 134.891 186.128 1.00 131.67 ? 12  VAL D CG1 1 
ATOM   2979  C  CG2 . VAL B 2 12  ? 118.187 132.404 186.295 1.00 131.67 ? 12  VAL D CG2 1 
ATOM   2980  N  N   . CYS B 2 13  ? 118.942 136.117 188.901 1.00 123.10 ? 13  CYS D N   1 
ATOM   2981  C  CA  . CYS B 2 13  ? 118.743 137.410 189.541 1.00 123.10 ? 13  CYS D CA  1 
ATOM   2982  C  C   . CYS B 2 13  ? 118.549 138.484 188.480 1.00 123.10 ? 13  CYS D C   1 
ATOM   2983  O  O   . CYS B 2 13  ? 119.277 138.520 187.483 1.00 123.10 ? 13  CYS D O   1 
ATOM   2984  C  CB  . CYS B 2 13  ? 119.912 137.781 190.455 1.00 123.10 ? 13  CYS D CB  1 
ATOM   2985  S  SG  . CYS B 2 13  ? 120.176 136.633 191.816 1.00 123.10 ? 13  CYS D SG  1 
ATOM   2986  N  N   . TYR B 2 14  ? 117.567 139.355 188.692 1.00 116.74 ? 14  TYR D N   1 
ATOM   2987  C  CA  . TYR B 2 14  ? 117.230 140.410 187.746 1.00 116.74 ? 14  TYR D CA  1 
ATOM   2988  C  C   . TYR B 2 14  ? 117.434 141.759 188.416 1.00 116.74 ? 14  TYR D C   1 
ATOM   2989  O  O   . TYR B 2 14  ? 117.183 141.911 189.615 1.00 116.74 ? 14  TYR D O   1 
ATOM   2990  C  CB  . TYR B 2 14  ? 115.793 140.291 187.244 1.00 116.74 ? 14  TYR D CB  1 
ATOM   2991  C  CG  . TYR B 2 14  ? 115.542 141.008 185.932 1.00 116.74 ? 14  TYR D CG  1 
ATOM   2992  C  CD1 . TYR B 2 14  ? 116.142 140.579 184.755 1.00 116.74 ? 14  TYR D CD1 1 
ATOM   2993  C  CD2 . TYR B 2 14  ? 114.691 142.104 185.870 1.00 116.74 ? 14  TYR D CD2 1 
ATOM   2994  C  CE1 . TYR B 2 14  ? 115.910 141.228 183.556 1.00 116.74 ? 14  TYR D CE1 1 
ATOM   2995  C  CE2 . TYR B 2 14  ? 114.451 142.757 184.676 1.00 116.74 ? 14  TYR D CE2 1 
ATOM   2996  C  CZ  . TYR B 2 14  ? 115.063 142.316 183.522 1.00 116.74 ? 14  TYR D CZ  1 
ATOM   2997  O  OH  . TYR B 2 14  ? 114.827 142.965 182.332 1.00 116.74 ? 14  TYR D OH  1 
ATOM   2998  N  N   . TYR B 2 15  ? 117.893 142.735 187.639 1.00 117.33 ? 15  TYR D N   1 
ATOM   2999  C  CA  . TYR B 2 15  ? 118.186 144.065 188.157 1.00 117.33 ? 15  TYR D CA  1 
ATOM   3000  C  C   . TYR B 2 15  ? 117.565 145.093 187.227 1.00 117.33 ? 15  TYR D C   1 
ATOM   3001  O  O   . TYR B 2 15  ? 117.918 145.151 186.044 1.00 117.33 ? 15  TYR D O   1 
ATOM   3002  C  CB  . TYR B 2 15  ? 119.696 144.279 188.278 1.00 117.33 ? 15  TYR D CB  1 
ATOM   3003  C  CG  . TYR B 2 15  ? 120.299 143.596 189.481 1.00 117.33 ? 15  TYR D CG  1 
ATOM   3004  C  CD1 . TYR B 2 15  ? 120.276 144.197 190.731 1.00 117.33 ? 15  TYR D CD1 1 
ATOM   3005  C  CD2 . TYR B 2 15  ? 120.871 142.336 189.371 1.00 117.33 ? 15  TYR D CD2 1 
ATOM   3006  C  CE1 . TYR B 2 15  ? 120.821 143.570 191.835 1.00 117.33 ? 15  TYR D CE1 1 
ATOM   3007  C  CE2 . TYR B 2 15  ? 121.415 141.701 190.467 1.00 117.33 ? 15  TYR D CE2 1 
ATOM   3008  C  CZ  . TYR B 2 15  ? 121.389 142.321 191.696 1.00 117.33 ? 15  TYR D CZ  1 
ATOM   3009  O  OH  . TYR B 2 15  ? 121.935 141.689 192.790 1.00 117.33 ? 15  TYR D OH  1 
ATOM   3010  N  N   . TYR B 2 16  ? 116.652 145.904 187.760 1.00 129.83 ? 16  TYR D N   1 
ATOM   3011  C  CA  . TYR B 2 16  ? 115.988 146.905 186.941 1.00 129.83 ? 16  TYR D CA  1 
ATOM   3012  C  C   . TYR B 2 16  ? 115.278 147.944 187.796 1.00 129.83 ? 16  TYR D C   1 
ATOM   3013  O  O   . TYR B 2 16  ? 114.577 147.601 188.750 1.00 129.83 ? 16  TYR D O   1 
ATOM   3014  C  CB  . TYR B 2 16  ? 114.979 146.256 185.986 1.00 129.83 ? 16  TYR D CB  1 
ATOM   3015  C  CG  . TYR B 2 16  ? 114.516 147.234 184.954 1.00 129.83 ? 16  TYR D CG  1 
ATOM   3016  C  CD1 . TYR B 2 16  ? 113.491 148.128 185.233 1.00 129.83 ? 16  TYR D CD1 1 
ATOM   3017  C  CD2 . TYR B 2 16  ? 115.153 147.325 183.734 1.00 129.83 ? 16  TYR D CD2 1 
ATOM   3018  C  CE1 . TYR B 2 16  ? 113.091 149.050 184.315 1.00 129.83 ? 16  TYR D CE1 1 
ATOM   3019  C  CE2 . TYR B 2 16  ? 114.754 148.238 182.810 1.00 129.83 ? 16  TYR D CE2 1 
ATOM   3020  C  CZ  . TYR B 2 16  ? 113.727 149.103 183.106 1.00 129.83 ? 16  TYR D CZ  1 
ATOM   3021  O  OH  . TYR B 2 16  ? 113.327 150.030 182.190 1.00 129.83 ? 16  TYR D OH  1 
ATOM   3022  N  N   . ASP B 2 17  ? 115.420 149.211 187.397 1.00 136.59 ? 17  ASP D N   1 
ATOM   3023  C  CA  . ASP B 2 17  ? 114.697 150.333 187.979 1.00 136.59 ? 17  ASP D CA  1 
ATOM   3024  C  C   . ASP B 2 17  ? 113.978 151.084 186.866 1.00 136.59 ? 17  ASP D C   1 
ATOM   3025  O  O   . ASP B 2 17  ? 114.532 151.279 185.780 1.00 136.59 ? 17  ASP D O   1 
ATOM   3026  C  CB  . ASP B 2 17  ? 115.639 151.283 188.731 1.00 136.59 ? 17  ASP D CB  1 
ATOM   3027  C  CG  . ASP B 2 17  ? 114.895 152.382 189.471 1.00 136.59 ? 17  ASP D CG  1 
ATOM   3028  O  OD1 . ASP B 2 17  ? 113.648 152.337 189.523 1.00 136.59 ? 17  ASP D OD1 1 
ATOM   3029  O  OD2 . ASP B 2 17  ? 115.562 153.299 189.995 1.00 136.59 ? 17  ASP D OD2 1 
ATOM   3030  N  N   . GLY B 2 18  ? 112.748 151.517 187.151 1.00 134.88 ? 18  GLY D N   1 
ATOM   3031  C  CA  . GLY B 2 18  ? 111.932 152.157 186.128 1.00 134.88 ? 18  GLY D CA  1 
ATOM   3032  C  C   . GLY B 2 18  ? 112.472 153.493 185.651 1.00 134.88 ? 18  GLY D C   1 
ATOM   3033  O  O   . GLY B 2 18  ? 112.500 153.768 184.445 1.00 134.88 ? 18  GLY D O   1 
ATOM   3034  N  N   . ASP B 2 19  ? 112.944 154.327 186.584 1.00 139.26 ? 19  ASP D N   1 
ATOM   3035  C  CA  . ASP B 2 19  ? 113.335 155.694 186.254 1.00 139.26 ? 19  ASP D CA  1 
ATOM   3036  C  C   . ASP B 2 19  ? 114.417 155.758 185.186 1.00 139.26 ? 19  ASP D C   1 
ATOM   3037  O  O   . ASP B 2 19  ? 114.558 156.799 184.530 1.00 139.26 ? 19  ASP D O   1 
ATOM   3038  C  CB  . ASP B 2 19  ? 113.808 156.420 187.514 1.00 139.26 ? 19  ASP D CB  1 
ATOM   3039  N  N   . ILE B 2 20  ? 115.168 154.672 184.982 1.00 132.61 ? 20  ILE D N   1 
ATOM   3040  C  CA  . ILE B 2 20  ? 116.221 154.665 183.976 1.00 132.61 ? 20  ILE D CA  1 
ATOM   3041  C  C   . ILE B 2 20  ? 115.659 155.036 182.610 1.00 132.61 ? 20  ILE D C   1 
ATOM   3042  O  O   . ILE B 2 20  ? 116.401 155.497 181.735 1.00 132.61 ? 20  ILE D O   1 
ATOM   3043  C  CB  . ILE B 2 20  ? 116.923 153.291 183.932 1.00 132.61 ? 20  ILE D CB  1 
ATOM   3044  C  CG1 . ILE B 2 20  ? 117.442 152.913 185.314 1.00 132.61 ? 20  ILE D CG1 1 
ATOM   3045  C  CG2 . ILE B 2 20  ? 118.121 153.337 183.000 1.00 132.61 ? 20  ILE D CG2 1 
ATOM   3046  C  CD1 . ILE B 2 20  ? 117.808 151.452 185.446 1.00 132.61 ? 20  ILE D CD1 1 
ATOM   3047  N  N   . GLY B 2 21  ? 114.349 154.878 182.414 1.00 124.90 ? 21  GLY D N   1 
ATOM   3048  C  CA  . GLY B 2 21  ? 113.761 155.176 181.124 1.00 124.90 ? 21  GLY D CA  1 
ATOM   3049  C  C   . GLY B 2 21  ? 113.592 156.649 180.815 1.00 124.90 ? 21  GLY D C   1 
ATOM   3050  O  O   . GLY B 2 21  ? 113.184 156.988 179.700 1.00 124.90 ? 21  GLY D O   1 
ATOM   3051  N  N   . ASN B 2 22  ? 113.888 157.534 181.765 1.00 131.60 ? 22  ASN D N   1 
ATOM   3052  C  CA  . ASN B 2 22  ? 113.675 158.963 181.579 1.00 131.60 ? 22  ASN D CA  1 
ATOM   3053  C  C   . ASN B 2 22  ? 114.964 159.720 181.278 1.00 131.60 ? 22  ASN D C   1 
ATOM   3054  O  O   . ASN B 2 22  ? 114.954 160.954 181.253 1.00 131.60 ? 22  ASN D O   1 
ATOM   3055  C  CB  . ASN B 2 22  ? 112.993 159.557 182.812 1.00 131.60 ? 22  ASN D CB  1 
ATOM   3056  C  CG  . ASN B 2 22  ? 111.798 158.742 183.265 1.00 131.60 ? 22  ASN D CG  1 
ATOM   3057  O  OD1 . ASN B 2 22  ? 110.955 158.354 182.457 1.00 131.60 ? 22  ASN D OD1 1 
ATOM   3058  N  ND2 . ASN B 2 22  ? 111.721 158.476 184.563 1.00 131.60 ? 22  ASN D ND2 1 
ATOM   3059  N  N   . TYR B 2 23  ? 116.070 159.010 181.047 1.00 116.93 ? 23  TYR D N   1 
ATOM   3060  C  CA  . TYR B 2 23  ? 117.365 159.636 180.771 1.00 116.93 ? 23  TYR D CA  1 
ATOM   3061  C  C   . TYR B 2 23  ? 117.507 159.859 179.267 1.00 116.93 ? 23  TYR D C   1 
ATOM   3062  O  O   . TYR B 2 23  ? 118.177 159.112 178.553 1.00 116.93 ? 23  TYR D O   1 
ATOM   3063  C  CB  . TYR B 2 23  ? 118.498 158.777 181.319 1.00 116.93 ? 23  TYR D CB  1 
ATOM   3064  C  CG  . TYR B 2 23  ? 118.522 158.690 182.827 1.00 116.93 ? 23  TYR D CG  1 
ATOM   3065  C  CD1 . TYR B 2 23  ? 118.797 159.805 183.606 1.00 116.93 ? 23  TYR D CD1 1 
ATOM   3066  C  CD2 . TYR B 2 23  ? 118.267 157.489 183.471 1.00 116.93 ? 23  TYR D CD2 1 
ATOM   3067  C  CE1 . TYR B 2 23  ? 118.818 159.723 184.987 1.00 116.93 ? 23  TYR D CE1 1 
ATOM   3068  C  CE2 . TYR B 2 23  ? 118.285 157.398 184.848 1.00 116.93 ? 23  TYR D CE2 1 
ATOM   3069  C  CZ  . TYR B 2 23  ? 118.561 158.516 185.601 1.00 116.93 ? 23  TYR D CZ  1 
ATOM   3070  O  OH  . TYR B 2 23  ? 118.578 158.422 186.973 1.00 116.93 ? 23  TYR D OH  1 
ATOM   3071  N  N   . TYR B 2 24  ? 116.858 160.914 178.782 1.00 122.64 ? 24  TYR D N   1 
ATOM   3072  C  CA  . TYR B 2 24  ? 116.928 161.254 177.365 1.00 122.64 ? 24  TYR D CA  1 
ATOM   3073  C  C   . TYR B 2 24  ? 118.345 161.675 176.987 1.00 122.64 ? 24  TYR D C   1 
ATOM   3074  O  O   . TYR B 2 24  ? 118.856 162.684 177.483 1.00 122.64 ? 24  TYR D O   1 
ATOM   3075  C  CB  . TYR B 2 24  ? 115.935 162.363 177.032 1.00 122.64 ? 24  TYR D CB  1 
ATOM   3076  C  CG  . TYR B 2 24  ? 115.800 162.623 175.548 1.00 122.64 ? 24  TYR D CG  1 
ATOM   3077  C  CD1 . TYR B 2 24  ? 115.382 161.622 174.682 1.00 122.64 ? 24  TYR D CD1 1 
ATOM   3078  C  CD2 . TYR B 2 24  ? 116.093 163.870 175.014 1.00 122.64 ? 24  TYR D CD2 1 
ATOM   3079  C  CE1 . TYR B 2 24  ? 115.261 161.855 173.324 1.00 122.64 ? 24  TYR D CE1 1 
ATOM   3080  C  CE2 . TYR B 2 24  ? 115.973 164.114 173.659 1.00 122.64 ? 24  TYR D CE2 1 
ATOM   3081  C  CZ  . TYR B 2 24  ? 115.558 163.103 172.819 1.00 122.64 ? 24  TYR D CZ  1 
ATOM   3082  O  OH  . TYR B 2 24  ? 115.437 163.343 171.470 1.00 122.64 ? 24  TYR D OH  1 
ATOM   3083  N  N   . TYR B 2 25  ? 118.977 160.890 176.110 1.00 128.40 ? 25  TYR D N   1 
ATOM   3084  C  CA  . TYR B 2 25  ? 120.345 161.174 175.687 1.00 128.40 ? 25  TYR D CA  1 
ATOM   3085  C  C   . TYR B 2 25  ? 120.441 162.513 174.965 1.00 128.40 ? 25  TYR D C   1 
ATOM   3086  O  O   . TYR B 2 25  ? 121.376 163.288 175.200 1.00 128.40 ? 25  TYR D O   1 
ATOM   3087  C  CB  . TYR B 2 25  ? 120.844 160.046 174.785 1.00 128.40 ? 25  TYR D CB  1 
ATOM   3088  C  CG  . TYR B 2 25  ? 122.311 159.697 174.900 1.00 128.40 ? 25  TYR D CG  1 
ATOM   3089  C  CD1 . TYR B 2 25  ? 122.832 159.154 176.067 1.00 128.40 ? 25  TYR D CD1 1 
ATOM   3090  C  CD2 . TYR B 2 25  ? 123.170 159.886 173.824 1.00 128.40 ? 25  TYR D CD2 1 
ATOM   3091  C  CE1 . TYR B 2 25  ? 124.172 158.826 176.163 1.00 128.40 ? 25  TYR D CE1 1 
ATOM   3092  C  CE2 . TYR B 2 25  ? 124.509 159.562 173.911 1.00 128.40 ? 25  TYR D CE2 1 
ATOM   3093  C  CZ  . TYR B 2 25  ? 125.005 159.032 175.082 1.00 128.40 ? 25  TYR D CZ  1 
ATOM   3094  O  OH  . TYR B 2 25  ? 126.339 158.708 175.173 1.00 128.40 ? 25  TYR D OH  1 
ATOM   3095  N  N   . GLY B 2 26  ? 119.493 162.802 174.090 1.00 126.15 ? 26  GLY D N   1 
ATOM   3096  C  CA  . GLY B 2 26  ? 119.514 164.035 173.325 1.00 126.15 ? 26  GLY D CA  1 
ATOM   3097  C  C   . GLY B 2 26  ? 118.905 163.826 171.956 1.00 126.15 ? 26  GLY D C   1 
ATOM   3098  O  O   . GLY B 2 26  ? 118.659 162.706 171.520 1.00 126.15 ? 26  GLY D O   1 
ATOM   3099  N  N   . GLN B 2 27  ? 118.613 164.943 171.294 1.00 127.29 ? 27  GLN D N   1 
ATOM   3100  C  CA  . GLN B 2 27  ? 118.028 164.881 169.960 1.00 127.29 ? 27  GLN D CA  1 
ATOM   3101  C  C   . GLN B 2 27  ? 118.951 164.116 169.018 1.00 127.29 ? 27  GLN D C   1 
ATOM   3102  O  O   . GLN B 2 27  ? 120.165 164.343 169.001 1.00 127.29 ? 27  GLN D O   1 
ATOM   3103  C  CB  . GLN B 2 27  ? 117.774 166.291 169.428 1.00 127.29 ? 27  GLN D CB  1 
ATOM   3104  N  N   . GLY B 2 28  ? 118.374 163.216 168.228 1.00 129.51 ? 28  GLY D N   1 
ATOM   3105  C  CA  . GLY B 2 28  ? 119.180 162.431 167.303 1.00 129.51 ? 28  GLY D CA  1 
ATOM   3106  C  C   . GLY B 2 28  ? 120.166 161.514 167.993 1.00 129.51 ? 28  GLY D C   1 
ATOM   3107  O  O   . GLY B 2 28  ? 121.332 161.435 167.585 1.00 129.51 ? 28  GLY D O   1 
ATOM   3108  N  N   . HIS B 2 29  ? 119.720 160.809 169.034 1.00 127.43 ? 29  HIS D N   1 
ATOM   3109  C  CA  . HIS B 2 29  ? 120.601 159.985 169.849 1.00 127.43 ? 29  HIS D CA  1 
ATOM   3110  C  C   . HIS B 2 29  ? 120.507 158.522 169.451 1.00 127.43 ? 29  HIS D C   1 
ATOM   3111  O  O   . HIS B 2 29  ? 119.419 157.929 169.537 1.00 127.43 ? 29  HIS D O   1 
ATOM   3112  C  CB  . HIS B 2 29  ? 120.248 160.148 171.324 1.00 127.43 ? 29  HIS D CB  1 
ATOM   3113  C  CG  . HIS B 2 29  ? 118.858 159.701 171.674 1.00 127.43 ? 29  HIS D CG  1 
ATOM   3114  N  ND1 . HIS B 2 29  ? 117.819 159.720 170.768 1.00 127.43 ? 29  HIS D ND1 1 
ATOM   3115  C  CD2 . HIS B 2 29  ? 118.335 159.231 172.831 1.00 127.43 ? 29  HIS D CD2 1 
ATOM   3116  C  CE1 . HIS B 2 29  ? 116.719 159.278 171.350 1.00 127.43 ? 29  HIS D CE1 1 
ATOM   3117  N  NE2 . HIS B 2 29  ? 117.005 158.973 172.603 1.00 127.43 ? 29  HIS D NE2 1 
ATOM   3118  N  N   . PRO B 2 30  ? 121.598 157.914 168.978 1.00 113.92 ? 30  PRO D N   1 
ATOM   3119  C  CA  . PRO B 2 30  ? 121.572 156.463 168.729 1.00 113.92 ? 30  PRO D CA  1 
ATOM   3120  C  C   . PRO B 2 30  ? 121.280 155.654 169.982 1.00 113.92 ? 30  PRO D C   1 
ATOM   3121  O  O   . PRO B 2 30  ? 120.596 154.625 169.912 1.00 113.92 ? 30  PRO D O   1 
ATOM   3122  C  CB  . PRO B 2 30  ? 122.974 156.177 168.172 1.00 113.92 ? 30  PRO D CB  1 
ATOM   3123  C  CG  . PRO B 2 30  ? 123.487 157.503 167.699 1.00 113.92 ? 30  PRO D CG  1 
ATOM   3124  C  CD  . PRO B 2 30  ? 122.886 158.522 168.611 1.00 113.92 ? 30  PRO D CD  1 
ATOM   3125  N  N   . MET B 2 31  ? 121.786 156.097 171.131 1.00 114.06 ? 31  MET D N   1 
ATOM   3126  C  CA  . MET B 2 31  ? 121.640 155.377 172.390 1.00 114.06 ? 31  MET D CA  1 
ATOM   3127  C  C   . MET B 2 31  ? 120.375 155.841 173.102 1.00 114.06 ? 31  MET D C   1 
ATOM   3128  O  O   . MET B 2 31  ? 120.251 157.020 173.449 1.00 114.06 ? 31  MET D O   1 
ATOM   3129  C  CB  . MET B 2 31  ? 122.865 155.602 173.275 1.00 114.06 ? 31  MET D CB  1 
ATOM   3130  C  CG  . MET B 2 31  ? 123.396 154.352 173.953 1.00 114.06 ? 31  MET D CG  1 
ATOM   3131  S  SD  . MET B 2 31  ? 122.580 154.017 175.524 1.00 114.06 ? 31  MET D SD  1 
ATOM   3132  C  CE  . MET B 2 31  ? 123.412 155.191 176.591 1.00 114.06 ? 31  MET D CE  1 
ATOM   3133  N  N   . LYS B 2 32  ? 119.446 154.914 173.331 1.00 113.92 ? 32  LYS D N   1 
ATOM   3134  C  CA  . LYS B 2 32  ? 118.156 155.222 173.946 1.00 113.92 ? 32  LYS D CA  1 
ATOM   3135  C  C   . LYS B 2 32  ? 117.941 154.284 175.124 1.00 113.92 ? 32  LYS D C   1 
ATOM   3136  O  O   . LYS B 2 32  ? 117.407 153.178 174.964 1.00 113.92 ? 32  LYS D O   1 
ATOM   3137  C  CB  . LYS B 2 32  ? 117.017 155.106 172.935 1.00 101.97 ? 32  LYS D CB  1 
ATOM   3138  C  CG  . LYS B 2 32  ? 117.388 155.519 171.518 1.00 101.97 ? 32  LYS D CG  1 
ATOM   3139  C  CD  . LYS B 2 32  ? 116.149 155.800 170.683 1.00 101.97 ? 32  LYS D CD  1 
ATOM   3140  C  CE  . LYS B 2 32  ? 116.509 156.457 169.361 1.00 101.97 ? 32  LYS D CE  1 
ATOM   3141  N  NZ  . LYS B 2 32  ? 117.405 155.599 168.541 1.00 101.97 ? 32  LYS D NZ  1 
ATOM   3142  N  N   . PRO B 2 33  ? 118.360 154.688 176.326 1.00 110.73 ? 33  PRO D N   1 
ATOM   3143  C  CA  . PRO B 2 33  ? 118.259 153.787 177.489 1.00 110.73 ? 33  PRO D CA  1 
ATOM   3144  C  C   . PRO B 2 33  ? 116.844 153.326 177.790 1.00 110.73 ? 33  PRO D C   1 
ATOM   3145  O  O   . PRO B 2 33  ? 116.656 152.186 178.239 1.00 110.73 ? 33  PRO D O   1 
ATOM   3146  C  CB  . PRO B 2 33  ? 118.836 154.629 178.636 1.00 110.73 ? 33  PRO D CB  1 
ATOM   3147  C  CG  . PRO B 2 33  ? 118.763 156.040 178.161 1.00 110.73 ? 33  PRO D CG  1 
ATOM   3148  C  CD  . PRO B 2 33  ? 118.947 155.989 176.681 1.00 110.73 ? 33  PRO D CD  1 
ATOM   3149  N  N   . HIS B 2 34  ? 115.838 154.166 177.531 1.00 113.45 ? 34  HIS D N   1 
ATOM   3150  C  CA  . HIS B 2 34  ? 114.441 153.827 177.787 1.00 113.45 ? 34  HIS D CA  1 
ATOM   3151  C  C   . HIS B 2 34  ? 114.040 152.526 177.100 1.00 113.45 ? 34  HIS D C   1 
ATOM   3152  O  O   . HIS B 2 34  ? 113.016 151.925 177.445 1.00 113.45 ? 34  HIS D O   1 
ATOM   3153  C  CB  . HIS B 2 34  ? 113.538 154.979 177.328 1.00 113.45 ? 34  HIS D CB  1 
ATOM   3154  C  CG  . HIS B 2 34  ? 112.109 154.587 177.104 1.00 113.45 ? 34  HIS D CG  1 
ATOM   3155  N  ND1 . HIS B 2 34  ? 111.345 153.975 178.074 1.00 113.45 ? 34  HIS D ND1 1 
ATOM   3156  C  CD2 . HIS B 2 34  ? 111.307 154.716 176.020 1.00 113.45 ? 34  HIS D CD2 1 
ATOM   3157  C  CE1 . HIS B 2 34  ? 110.134 153.746 177.599 1.00 113.45 ? 34  HIS D CE1 1 
ATOM   3158  N  NE2 . HIS B 2 34  ? 110.085 154.186 176.355 1.00 113.45 ? 34  HIS D NE2 1 
ATOM   3159  N  N   . ARG B 2 35  ? 114.863 152.060 176.155 1.00 123.72 ? 35  ARG D N   1 
ATOM   3160  C  CA  . ARG B 2 35  ? 114.575 150.802 175.479 1.00 123.72 ? 35  ARG D CA  1 
ATOM   3161  C  C   . ARG B 2 35  ? 114.442 149.661 176.468 1.00 123.72 ? 35  ARG D C   1 
ATOM   3162  O  O   . ARG B 2 35  ? 113.592 148.779 176.291 1.00 123.72 ? 35  ARG D O   1 
ATOM   3163  C  CB  . ARG B 2 35  ? 115.687 150.474 174.488 1.00 123.72 ? 35  ARG D CB  1 
ATOM   3164  N  N   . ILE B 2 36  ? 115.226 149.701 177.547 1.00 115.40 ? 36  ILE D N   1 
ATOM   3165  C  CA  . ILE B 2 36  ? 115.160 148.638 178.542 1.00 115.40 ? 36  ILE D CA  1 
ATOM   3166  C  C   . ILE B 2 36  ? 113.764 148.522 179.142 1.00 115.40 ? 36  ILE D C   1 
ATOM   3167  O  O   . ILE B 2 36  ? 113.314 147.412 179.454 1.00 115.40 ? 36  ILE D O   1 
ATOM   3168  C  CB  . ILE B 2 36  ? 116.263 148.851 179.597 1.00 115.40 ? 36  ILE D CB  1 
ATOM   3169  C  CG1 . ILE B 2 36  ? 115.979 150.083 180.450 1.00 115.40 ? 36  ILE D CG1 1 
ATOM   3170  C  CG2 . ILE B 2 36  ? 117.622 148.970 178.922 1.00 115.40 ? 36  ILE D CG2 1 
ATOM   3171  C  CD1 . ILE B 2 36  ? 117.113 150.427 181.373 1.00 115.40 ? 36  ILE D CD1 1 
ATOM   3172  N  N   . ARG B 2 37  ? 113.018 149.630 179.238 1.00 129.28 ? 37  ARG D N   1 
ATOM   3173  C  CA  . ARG B 2 37  ? 111.693 149.482 179.828 1.00 129.28 ? 37  ARG D CA  1 
ATOM   3174  C  C   . ARG B 2 37  ? 110.766 148.815 178.838 1.00 129.28 ? 37  ARG D C   1 
ATOM   3175  O  O   . ARG B 2 37  ? 109.945 147.972 179.223 1.00 129.28 ? 37  ARG D O   1 
ATOM   3176  C  CB  . ARG B 2 37  ? 111.130 150.844 180.246 1.00 129.28 ? 37  ARG D CB  1 
ATOM   3177  C  CG  . ARG B 2 37  ? 109.608 150.921 180.220 1.00 129.28 ? 37  ARG D CG  1 
ATOM   3178  C  CD  . ARG B 2 37  ? 109.055 151.792 181.337 1.00 129.28 ? 37  ARG D CD  1 
ATOM   3179  N  NE  . ARG B 2 37  ? 109.122 153.214 181.017 1.00 129.28 ? 37  ARG D NE  1 
ATOM   3180  C  CZ  . ARG B 2 37  ? 110.036 154.047 181.494 1.00 129.28 ? 37  ARG D CZ  1 
ATOM   3181  N  NH1 . ARG B 2 37  ? 110.982 153.635 182.321 1.00 129.28 ? 37  ARG D NH1 1 
ATOM   3182  N  NH2 . ARG B 2 37  ? 109.995 155.327 181.136 1.00 129.28 ? 37  ARG D NH2 1 
ATOM   3183  N  N   . MET B 2 38  ? 110.946 149.120 177.555 1.00 128.99 ? 38  MET D N   1 
ATOM   3184  C  CA  . MET B 2 38  ? 110.170 148.458 176.522 1.00 128.99 ? 38  MET D CA  1 
ATOM   3185  C  C   . MET B 2 38  ? 110.504 146.972 176.516 1.00 128.99 ? 38  MET D C   1 
ATOM   3186  O  O   . MET B 2 38  ? 109.750 146.165 175.962 1.00 128.99 ? 38  MET D O   1 
ATOM   3187  C  CB  . MET B 2 38  ? 110.377 149.174 175.184 1.00 128.99 ? 38  MET D CB  1 
ATOM   3188  C  CG  . MET B 2 38  ? 110.338 148.346 173.933 1.00 128.99 ? 38  MET D CG  1 
ATOM   3189  S  SD  . MET B 2 38  ? 110.343 149.499 172.548 1.00 128.99 ? 38  MET D SD  1 
ATOM   3190  C  CE  . MET B 2 38  ? 110.763 148.417 171.203 1.00 128.99 ? 38  MET D CE  1 
ATOM   3191  N  N   . THR B 2 39  ? 111.615 146.604 177.164 1.00 113.92 ? 39  THR D N   1 
ATOM   3192  C  CA  . THR B 2 39  ? 112.015 145.224 177.391 1.00 113.92 ? 39  THR D CA  1 
ATOM   3193  C  C   . THR B 2 39  ? 111.369 144.680 178.658 1.00 113.92 ? 39  THR D C   1 
ATOM   3194  O  O   . THR B 2 39  ? 110.850 143.559 178.656 1.00 113.92 ? 39  THR D O   1 
ATOM   3195  C  CB  . THR B 2 39  ? 113.542 145.135 177.525 1.00 113.92 ? 39  THR D CB  1 
ATOM   3196  O  OG1 . THR B 2 39  ? 114.149 145.118 176.234 1.00 113.92 ? 39  THR D OG1 1 
ATOM   3197  C  CG2 . THR B 2 39  ? 113.952 143.880 178.278 1.00 113.92 ? 39  THR D CG2 1 
ATOM   3198  N  N   . HIS B 2 40  ? 111.397 145.464 179.743 1.00 118.62 ? 40  HIS D N   1 
ATOM   3199  C  CA  . HIS B 2 40  ? 110.871 144.984 181.018 1.00 118.62 ? 40  HIS D CA  1 
ATOM   3200  C  C   . HIS B 2 40  ? 109.439 144.485 180.878 1.00 118.62 ? 40  HIS D C   1 
ATOM   3201  O  O   . HIS B 2 40  ? 109.079 143.444 181.441 1.00 118.62 ? 40  HIS D O   1 
ATOM   3202  C  CB  . HIS B 2 40  ? 110.946 146.091 182.070 1.00 118.62 ? 40  HIS D CB  1 
ATOM   3203  C  CG  . HIS B 2 40  ? 110.657 145.618 183.460 1.00 118.62 ? 40  HIS D CG  1 
ATOM   3204  N  ND1 . HIS B 2 40  ? 111.584 144.948 184.228 1.00 118.62 ? 40  HIS D ND1 1 
ATOM   3205  C  CD2 . HIS B 2 40  ? 109.538 145.709 184.216 1.00 118.62 ? 40  HIS D CD2 1 
ATOM   3206  C  CE1 . HIS B 2 40  ? 111.050 144.650 185.399 1.00 118.62 ? 40  HIS D CE1 1 
ATOM   3207  N  NE2 . HIS B 2 40  ? 109.809 145.101 185.418 1.00 118.62 ? 40  HIS D NE2 1 
ATOM   3208  N  N   . ASN B 2 41  ? 108.616 145.197 180.103 1.00 128.16 ? 41  ASN D N   1 
ATOM   3209  C  CA  . ASN B 2 41  ? 107.218 144.804 179.968 1.00 128.16 ? 41  ASN D CA  1 
ATOM   3210  C  C   . ASN B 2 41  ? 107.096 143.442 179.304 1.00 128.16 ? 41  ASN D C   1 
ATOM   3211  O  O   . ASN B 2 41  ? 106.241 142.634 179.691 1.00 128.16 ? 41  ASN D O   1 
ATOM   3212  C  CB  . ASN B 2 41  ? 106.447 145.858 179.174 1.00 128.16 ? 41  ASN D CB  1 
ATOM   3213  C  CG  . ASN B 2 41  ? 105.127 146.226 179.824 1.00 128.16 ? 41  ASN D CG  1 
ATOM   3214  O  OD1 . ASN B 2 41  ? 104.155 145.476 179.749 1.00 128.16 ? 41  ASN D OD1 1 
ATOM   3215  N  ND2 . ASN B 2 41  ? 105.089 147.385 180.470 1.00 128.16 ? 41  ASN D ND2 1 
ATOM   3216  N  N   . LEU B 2 42  ? 107.994 143.137 178.363 1.00 115.35 ? 42  LEU D N   1 
ATOM   3217  C  CA  . LEU B 2 42  ? 107.966 141.839 177.704 1.00 115.35 ? 42  LEU D CA  1 
ATOM   3218  C  C   . LEU B 2 42  ? 108.297 140.726 178.683 1.00 115.35 ? 42  LEU D C   1 
ATOM   3219  O  O   . LEU B 2 42  ? 107.901 139.578 178.460 1.00 115.35 ? 42  LEU D O   1 
ATOM   3220  C  CB  . LEU B 2 42  ? 108.936 141.820 176.523 1.00 115.35 ? 42  LEU D CB  1 
ATOM   3221  C  CG  . LEU B 2 42  ? 108.382 142.348 175.198 1.00 115.35 ? 42  LEU D CG  1 
ATOM   3222  C  CD1 . LEU B 2 42  ? 109.448 143.109 174.427 1.00 115.35 ? 42  LEU D CD1 1 
ATOM   3223  C  CD2 . LEU B 2 42  ? 107.822 141.212 174.360 1.00 115.35 ? 42  LEU D CD2 1 
ATOM   3224  N  N   . LEU B 2 43  ? 109.014 141.046 179.761 1.00 118.21 ? 43  LEU D N   1 
ATOM   3225  C  CA  . LEU B 2 43  ? 109.200 140.078 180.833 1.00 118.21 ? 43  LEU D CA  1 
ATOM   3226  C  C   . LEU B 2 43  ? 107.912 139.897 181.625 1.00 118.21 ? 43  LEU D C   1 
ATOM   3227  O  O   . LEU B 2 43  ? 107.532 138.767 181.953 1.00 118.21 ? 43  LEU D O   1 
ATOM   3228  C  CB  . LEU B 2 43  ? 110.342 140.519 181.749 1.00 118.21 ? 43  LEU D CB  1 
ATOM   3229  N  N   . LEU B 2 44  ? 107.229 140.998 181.946 1.00 127.11 ? 44  LEU D N   1 
ATOM   3230  C  CA  . LEU B 2 44  ? 105.988 140.898 182.707 1.00 127.11 ? 44  LEU D CA  1 
ATOM   3231  C  C   . LEU B 2 44  ? 104.866 140.311 181.859 1.00 127.11 ? 44  LEU D C   1 
ATOM   3232  O  O   . LEU B 2 44  ? 104.126 139.431 182.314 1.00 127.11 ? 44  LEU D O   1 
ATOM   3233  C  CB  . LEU B 2 44  ? 105.594 142.272 183.249 1.00 127.11 ? 44  LEU D CB  1 
ATOM   3234  N  N   . ASN B 2 45  ? 104.716 140.797 180.623 1.00 130.08 ? 45  ASN D N   1 
ATOM   3235  C  CA  . ASN B 2 45  ? 103.609 140.353 179.782 1.00 130.08 ? 45  ASN D CA  1 
ATOM   3236  C  C   . ASN B 2 45  ? 103.713 138.867 179.463 1.00 130.08 ? 45  ASN D C   1 
ATOM   3237  O  O   . ASN B 2 45  ? 102.701 138.155 179.445 1.00 130.08 ? 45  ASN D O   1 
ATOM   3238  C  CB  . ASN B 2 45  ? 103.557 141.179 178.497 1.00 130.08 ? 45  ASN D CB  1 
ATOM   3239  C  CG  . ASN B 2 45  ? 102.874 142.519 178.693 1.00 130.08 ? 45  ASN D CG  1 
ATOM   3240  O  OD1 . ASN B 2 45  ? 102.418 143.142 177.735 1.00 130.08 ? 45  ASN D OD1 1 
ATOM   3241  N  ND2 . ASN B 2 45  ? 102.807 142.974 179.939 1.00 130.08 ? 45  ASN D ND2 1 
ATOM   3242  N  N   . TYR B 2 46  ? 104.930 138.378 179.215 1.00 125.50 ? 46  TYR D N   1 
ATOM   3243  C  CA  . TYR B 2 46  ? 105.134 136.951 178.994 1.00 125.50 ? 46  TYR D CA  1 
ATOM   3244  C  C   . TYR B 2 46  ? 105.015 136.148 180.280 1.00 125.50 ? 46  TYR D C   1 
ATOM   3245  O  O   . TYR B 2 46  ? 104.839 134.926 180.220 1.00 125.50 ? 46  TYR D O   1 
ATOM   3246  C  CB  . TYR B 2 46  ? 106.508 136.700 178.370 1.00 125.50 ? 46  TYR D CB  1 
ATOM   3247  C  CG  . TYR B 2 46  ? 106.515 136.626 176.861 1.00 125.50 ? 46  TYR D CG  1 
ATOM   3248  C  CD1 . TYR B 2 46  ? 106.069 135.491 176.200 1.00 125.50 ? 46  TYR D CD1 1 
ATOM   3249  C  CD2 . TYR B 2 46  ? 106.990 137.683 176.097 1.00 125.50 ? 46  TYR D CD2 1 
ATOM   3250  C  CE1 . TYR B 2 46  ? 106.076 135.419 174.821 1.00 125.50 ? 46  TYR D CE1 1 
ATOM   3251  C  CE2 . TYR B 2 46  ? 107.006 137.619 174.719 1.00 125.50 ? 46  TYR D CE2 1 
ATOM   3252  C  CZ  . TYR B 2 46  ? 106.547 136.484 174.085 1.00 125.50 ? 46  TYR D CZ  1 
ATOM   3253  O  OH  . TYR B 2 46  ? 106.565 136.412 172.712 1.00 125.50 ? 46  TYR D OH  1 
ATOM   3254  N  N   . GLY B 2 47  ? 105.108 136.800 181.435 1.00 134.35 ? 47  GLY D N   1 
ATOM   3255  C  CA  . GLY B 2 47  ? 104.988 136.129 182.709 1.00 134.35 ? 47  GLY D CA  1 
ATOM   3256  C  C   . GLY B 2 47  ? 106.294 135.645 183.294 1.00 134.35 ? 47  GLY D C   1 
ATOM   3257  O  O   . GLY B 2 47  ? 106.284 135.050 184.380 1.00 134.35 ? 47  GLY D O   1 
ATOM   3258  N  N   . LEU B 2 48  ? 107.416 135.866 182.604 1.00 126.51 ? 48  LEU D N   1 
ATOM   3259  C  CA  . LEU B 2 48  ? 108.720 135.488 183.137 1.00 126.51 ? 48  LEU D CA  1 
ATOM   3260  C  C   . LEU B 2 48  ? 109.009 136.148 184.479 1.00 126.51 ? 48  LEU D C   1 
ATOM   3261  O  O   . LEU B 2 48  ? 109.870 135.665 185.223 1.00 126.51 ? 48  LEU D O   1 
ATOM   3262  C  CB  . LEU B 2 48  ? 109.822 135.851 182.136 1.00 126.51 ? 48  LEU D CB  1 
ATOM   3263  C  CG  . LEU B 2 48  ? 110.129 134.959 180.925 1.00 126.51 ? 48  LEU D CG  1 
ATOM   3264  C  CD1 . LEU B 2 48  ? 108.884 134.352 180.292 1.00 126.51 ? 48  LEU D CD1 1 
ATOM   3265  C  CD2 . LEU B 2 48  ? 110.920 135.743 179.887 1.00 126.51 ? 48  LEU D CD2 1 
ATOM   3266  N  N   . TYR B 2 49  ? 108.313 137.244 184.798 1.00 142.42 ? 49  TYR D N   1 
ATOM   3267  C  CA  . TYR B 2 49  ? 108.583 137.977 186.031 1.00 142.42 ? 49  TYR D CA  1 
ATOM   3268  C  C   . TYR B 2 49  ? 108.328 137.119 187.264 1.00 142.42 ? 49  TYR D C   1 
ATOM   3269  O  O   . TYR B 2 49  ? 109.114 137.146 188.218 1.00 142.42 ? 49  TYR D O   1 
ATOM   3270  C  CB  . TYR B 2 49  ? 107.736 139.248 186.080 1.00 142.42 ? 49  TYR D CB  1 
ATOM   3271  N  N   . ARG B 2 50  ? 107.229 136.355 187.269 1.00 147.84 ? 50  ARG D N   1 
ATOM   3272  C  CA  . ARG B 2 50  ? 106.864 135.615 188.474 1.00 147.84 ? 50  ARG D CA  1 
ATOM   3273  C  C   . ARG B 2 50  ? 107.904 134.554 188.804 1.00 147.84 ? 50  ARG D C   1 
ATOM   3274  O  O   . ARG B 2 50  ? 108.304 134.409 189.965 1.00 147.84 ? 50  ARG D O   1 
ATOM   3275  C  CB  . ARG B 2 50  ? 105.485 134.980 188.303 1.00 147.84 ? 50  ARG D CB  1 
ATOM   3276  N  N   . LYS B 2 51  ? 108.352 133.800 187.798 1.00 145.12 ? 51  LYS D N   1 
ATOM   3277  C  CA  . LYS B 2 51  ? 109.281 132.708 188.051 1.00 145.12 ? 51  LYS D CA  1 
ATOM   3278  C  C   . LYS B 2 51  ? 110.645 133.215 188.492 1.00 145.12 ? 51  LYS D C   1 
ATOM   3279  O  O   . LYS B 2 51  ? 111.455 132.427 188.991 1.00 145.12 ? 51  LYS D O   1 
ATOM   3280  C  CB  . LYS B 2 51  ? 109.424 131.837 186.802 1.00 145.12 ? 51  LYS D CB  1 
ATOM   3281  N  N   . MET B 2 52  ? 110.910 134.503 188.300 1.00 137.12 ? 52  MET D N   1 
ATOM   3282  C  CA  . MET B 2 52  ? 112.210 135.123 188.500 1.00 137.12 ? 52  MET D CA  1 
ATOM   3283  C  C   . MET B 2 52  ? 112.233 135.932 189.795 1.00 137.12 ? 52  MET D C   1 
ATOM   3284  O  O   . MET B 2 52  ? 111.200 136.208 190.409 1.00 137.12 ? 52  MET D O   1 
ATOM   3285  C  CB  . MET B 2 52  ? 112.554 135.989 187.287 1.00 137.12 ? 52  MET D CB  1 
ATOM   3286  C  CG  . MET B 2 52  ? 113.712 135.456 186.476 1.00 137.12 ? 52  MET D CG  1 
ATOM   3287  S  SD  . MET B 2 52  ? 113.884 136.334 184.920 1.00 137.12 ? 52  MET D SD  1 
ATOM   3288  C  CE  . MET B 2 52  ? 113.844 138.027 185.473 1.00 137.12 ? 52  MET D CE  1 
ATOM   3289  N  N   . GLU B 2 53  ? 113.442 136.310 190.207 1.00 126.88 ? 53  GLU D N   1 
ATOM   3290  C  CA  . GLU B 2 53  ? 113.652 137.283 191.273 1.00 126.88 ? 53  GLU D CA  1 
ATOM   3291  C  C   . GLU B 2 53  ? 114.092 138.615 190.674 1.00 126.88 ? 53  GLU D C   1 
ATOM   3292  O  O   . GLU B 2 53  ? 115.088 138.675 189.945 1.00 126.88 ? 53  GLU D O   1 
ATOM   3293  C  CB  . GLU B 2 53  ? 114.673 136.789 192.306 1.00 126.88 ? 53  GLU D CB  1 
ATOM   3294  C  CG  . GLU B 2 53  ? 114.443 135.385 192.920 1.00 126.88 ? 53  GLU D CG  1 
ATOM   3295  C  CD  . GLU B 2 53  ? 114.408 134.218 191.937 1.00 126.88 ? 53  GLU D CD  1 
ATOM   3296  O  OE1 . GLU B 2 53  ? 114.374 133.066 192.408 1.00 126.88 ? 53  GLU D OE1 1 
ATOM   3297  O  OE2 . GLU B 2 53  ? 114.493 134.426 190.712 1.00 126.88 ? 53  GLU D OE2 1 
ATOM   3298  N  N   . ILE B 2 54  ? 113.344 139.672 190.980 1.00 124.64 ? 54  ILE D N   1 
ATOM   3299  C  CA  . ILE B 2 54  ? 113.498 140.981 190.356 1.00 124.64 ? 54  ILE D CA  1 
ATOM   3300  C  C   . ILE B 2 54  ? 113.928 141.991 191.414 1.00 124.64 ? 54  ILE D C   1 
ATOM   3301  O  O   . ILE B 2 54  ? 113.334 142.059 192.495 1.00 124.64 ? 54  ILE D O   1 
ATOM   3302  C  CB  . ILE B 2 54  ? 112.208 141.426 189.636 1.00 124.64 ? 54  ILE D CB  1 
ATOM   3303  C  CG1 . ILE B 2 54  ? 110.954 140.832 190.294 1.00 124.64 ? 54  ILE D CG1 1 
ATOM   3304  C  CG2 . ILE B 2 54  ? 112.261 141.056 188.164 1.00 124.64 ? 54  ILE D CG2 1 
ATOM   3305  C  CD1 . ILE B 2 54  ? 110.523 141.478 191.591 1.00 124.64 ? 54  ILE D CD1 1 
ATOM   3306  N  N   . TYR B 2 55  ? 114.981 142.751 191.111 1.00 125.17 ? 55  TYR D N   1 
ATOM   3307  C  CA  . TYR B 2 55  ? 115.477 143.802 191.988 1.00 125.17 ? 55  TYR D CA  1 
ATOM   3308  C  C   . TYR B 2 55  ? 115.775 145.041 191.156 1.00 125.17 ? 55  TYR D C   1 
ATOM   3309  O  O   . TYR B 2 55  ? 115.690 145.026 189.925 1.00 125.17 ? 55  TYR D O   1 
ATOM   3310  C  CB  . TYR B 2 55  ? 116.739 143.376 192.752 1.00 125.17 ? 55  TYR D CB  1 
ATOM   3311  C  CG  . TYR B 2 55  ? 116.734 141.948 193.241 1.00 125.17 ? 55  TYR D CG  1 
ATOM   3312  C  CD1 . TYR B 2 55  ? 115.819 141.524 194.195 1.00 125.17 ? 55  TYR D CD1 1 
ATOM   3313  C  CD2 . TYR B 2 55  ? 117.651 141.028 192.757 1.00 125.17 ? 55  TYR D CD2 1 
ATOM   3314  C  CE1 . TYR B 2 55  ? 115.812 140.220 194.647 1.00 125.17 ? 55  TYR D CE1 1 
ATOM   3315  C  CE2 . TYR B 2 55  ? 117.654 139.722 193.204 1.00 125.17 ? 55  TYR D CE2 1 
ATOM   3316  C  CZ  . TYR B 2 55  ? 116.732 139.323 194.149 1.00 125.17 ? 55  TYR D CZ  1 
ATOM   3317  O  OH  . TYR B 2 55  ? 116.729 138.023 194.600 1.00 125.17 ? 55  TYR D OH  1 
ATOM   3318  N  N   . ARG B 2 56  ? 116.120 146.129 191.846 1.00 122.26 ? 56  ARG D N   1 
ATOM   3319  C  CA  . ARG B 2 56  ? 116.529 147.348 191.177 1.00 122.26 ? 56  ARG D CA  1 
ATOM   3320  C  C   . ARG B 2 56  ? 117.947 147.735 191.572 1.00 122.26 ? 56  ARG D C   1 
ATOM   3321  O  O   . ARG B 2 56  ? 118.305 147.653 192.752 1.00 122.26 ? 56  ARG D O   1 
ATOM   3322  C  CB  . ARG B 2 56  ? 115.579 148.505 191.524 1.00 122.26 ? 56  ARG D CB  1 
ATOM   3323  N  N   . PRO B 2 57  ? 118.777 148.143 190.614 1.00 128.33 ? 57  PRO D N   1 
ATOM   3324  C  CA  . PRO B 2 57  ? 120.150 148.543 190.951 1.00 128.33 ? 57  PRO D CA  1 
ATOM   3325  C  C   . PRO B 2 57  ? 120.145 149.789 191.822 1.00 128.33 ? 57  PRO D C   1 
ATOM   3326  O  O   . PRO B 2 57  ? 119.595 150.827 191.447 1.00 128.33 ? 57  PRO D O   1 
ATOM   3327  C  CB  . PRO B 2 57  ? 120.787 148.805 189.581 1.00 128.33 ? 57  PRO D CB  1 
ATOM   3328  C  CG  . PRO B 2 57  ? 119.641 149.117 188.681 1.00 128.33 ? 57  PRO D CG  1 
ATOM   3329  C  CD  . PRO B 2 57  ? 118.489 148.294 189.178 1.00 128.33 ? 57  PRO D CD  1 
ATOM   3330  N  N   . HIS B 2 58  ? 120.761 149.682 192.994 1.00 134.36 ? 58  HIS D N   1 
ATOM   3331  C  CA  . HIS B 2 58  ? 120.798 150.818 193.897 1.00 134.36 ? 58  HIS D CA  1 
ATOM   3332  C  C   . HIS B 2 58  ? 121.912 151.780 193.490 1.00 134.36 ? 58  HIS D C   1 
ATOM   3333  O  O   . HIS B 2 58  ? 122.766 151.468 192.655 1.00 134.36 ? 58  HIS D O   1 
ATOM   3334  C  CB  . HIS B 2 58  ? 120.968 150.347 195.342 1.00 134.36 ? 58  HIS D CB  1 
ATOM   3335  C  CG  . HIS B 2 58  ? 122.341 149.847 195.661 1.00 134.36 ? 58  HIS D CG  1 
ATOM   3336  N  ND1 . HIS B 2 58  ? 122.703 148.525 195.517 1.00 134.36 ? 58  HIS D ND1 1 
ATOM   3337  C  CD2 . HIS B 2 58  ? 123.436 150.487 196.134 1.00 134.36 ? 58  HIS D CD2 1 
ATOM   3338  C  CE1 . HIS B 2 58  ? 123.965 148.374 195.876 1.00 134.36 ? 58  HIS D CE1 1 
ATOM   3339  N  NE2 . HIS B 2 58  ? 124.433 149.550 196.255 1.00 134.36 ? 58  HIS D NE2 1 
ATOM   3340  N  N   . LYS B 2 59  ? 121.884 152.972 194.081 1.00 134.50 ? 59  LYS D N   1 
ATOM   3341  C  CA  . LYS B 2 59  ? 122.816 154.023 193.696 1.00 134.50 ? 59  LYS D CA  1 
ATOM   3342  C  C   . LYS B 2 59  ? 124.256 153.581 193.926 1.00 134.50 ? 59  LYS D C   1 
ATOM   3343  O  O   . LYS B 2 59  ? 124.591 153.010 194.967 1.00 134.50 ? 59  LYS D O   1 
ATOM   3344  C  CB  . LYS B 2 59  ? 122.527 155.302 194.484 1.00 134.50 ? 59  LYS D CB  1 
ATOM   3345  N  N   . ALA B 2 60  ? 125.112 153.853 192.945 1.00 136.71 ? 60  ALA D N   1 
ATOM   3346  C  CA  . ALA B 2 60  ? 126.537 153.572 193.060 1.00 136.71 ? 60  ALA D CA  1 
ATOM   3347  C  C   . ALA B 2 60  ? 127.238 154.806 193.612 1.00 136.71 ? 60  ALA D C   1 
ATOM   3348  O  O   . ALA B 2 60  ? 127.195 155.877 192.997 1.00 136.71 ? 60  ALA D O   1 
ATOM   3349  C  CB  . ALA B 2 60  ? 127.122 153.170 191.707 1.00 136.71 ? 60  ALA D CB  1 
ATOM   3350  N  N   . THR B 2 61  ? 127.886 154.655 194.763 1.00 133.19 ? 61  THR D N   1 
ATOM   3351  C  CA  . THR B 2 61  ? 128.527 155.786 195.412 1.00 133.19 ? 61  THR D CA  1 
ATOM   3352  C  C   . THR B 2 61  ? 129.738 156.254 194.611 1.00 133.19 ? 61  THR D C   1 
ATOM   3353  O  O   . THR B 2 61  ? 130.345 155.500 193.846 1.00 133.19 ? 61  THR D O   1 
ATOM   3354  C  CB  . THR B 2 61  ? 128.952 155.423 196.835 1.00 133.19 ? 61  THR D CB  1 
ATOM   3355  O  OG1 . THR B 2 61  ? 130.124 154.599 196.790 1.00 133.19 ? 61  THR D OG1 1 
ATOM   3356  C  CG2 . THR B 2 61  ? 127.838 154.672 197.547 1.00 133.19 ? 61  THR D CG2 1 
ATOM   3357  N  N   . ALA B 2 62  ? 130.083 157.531 194.798 1.00 126.54 ? 62  ALA D N   1 
ATOM   3358  C  CA  . ALA B 2 62  ? 131.245 158.097 194.121 1.00 126.54 ? 62  ALA D CA  1 
ATOM   3359  C  C   . ALA B 2 62  ? 132.520 157.359 194.507 1.00 126.54 ? 62  ALA D C   1 
ATOM   3360  O  O   . ALA B 2 62  ? 133.398 157.137 193.665 1.00 126.54 ? 62  ALA D O   1 
ATOM   3361  C  CB  . ALA B 2 62  ? 131.366 159.586 194.441 1.00 126.54 ? 62  ALA D CB  1 
ATOM   3362  N  N   . GLU B 2 63  ? 132.643 156.979 195.780 1.00 129.75 ? 63  GLU D N   1 
ATOM   3363  C  CA  . GLU B 2 63  ? 133.803 156.209 196.215 1.00 129.75 ? 63  GLU D CA  1 
ATOM   3364  C  C   . GLU B 2 63  ? 133.862 154.860 195.509 1.00 129.75 ? 63  GLU D C   1 
ATOM   3365  O  O   . GLU B 2 63  ? 134.941 154.411 195.105 1.00 129.75 ? 63  GLU D O   1 
ATOM   3366  C  CB  . GLU B 2 63  ? 133.772 156.023 197.732 1.00 129.75 ? 63  GLU D CB  1 
ATOM   3367  N  N   . GLU B 2 64  ? 132.712 154.191 195.371 1.00 131.04 ? 64  GLU D N   1 
ATOM   3368  C  CA  . GLU B 2 64  ? 132.676 152.907 194.674 1.00 131.04 ? 64  GLU D CA  1 
ATOM   3369  C  C   . GLU B 2 64  ? 133.228 153.029 193.259 1.00 131.04 ? 64  GLU D C   1 
ATOM   3370  O  O   . GLU B 2 64  ? 134.003 152.175 192.812 1.00 131.04 ? 64  GLU D O   1 
ATOM   3371  C  CB  . GLU B 2 64  ? 131.248 152.363 194.649 1.00 131.04 ? 64  GLU D CB  1 
ATOM   3372  N  N   . MET B 2 65  ? 132.834 154.080 192.534 1.00 127.66 ? 65  MET D N   1 
ATOM   3373  C  CA  . MET B 2 65  ? 133.378 154.305 191.200 1.00 127.66 ? 65  MET D CA  1 
ATOM   3374  C  C   . MET B 2 65  ? 134.875 154.577 191.228 1.00 127.66 ? 65  MET D C   1 
ATOM   3375  O  O   . MET B 2 65  ? 135.548 154.383 190.209 1.00 127.66 ? 65  MET D O   1 
ATOM   3376  C  CB  . MET B 2 65  ? 132.659 155.464 190.505 1.00 127.66 ? 65  MET D CB  1 
ATOM   3377  C  CG  . MET B 2 65  ? 131.167 155.539 190.765 1.00 127.66 ? 65  MET D CG  1 
ATOM   3378  S  SD  . MET B 2 65  ? 130.314 156.346 189.397 1.00 127.66 ? 65  MET D SD  1 
ATOM   3379  C  CE  . MET B 2 65  ? 128.657 155.704 189.600 1.00 127.66 ? 65  MET D CE  1 
ATOM   3380  N  N   . THR B 2 66  ? 135.412 155.024 192.360 1.00 122.55 ? 66  THR D N   1 
ATOM   3381  C  CA  . THR B 2 66  ? 136.841 155.314 192.473 1.00 122.55 ? 66  THR D CA  1 
ATOM   3382  C  C   . THR B 2 66  ? 137.582 154.042 192.917 1.00 122.55 ? 66  THR D C   1 
ATOM   3383  O  O   . THR B 2 66  ? 138.288 153.955 193.922 1.00 122.55 ? 66  THR D O   1 
ATOM   3384  C  CB  . THR B 2 66  ? 137.042 156.511 193.410 1.00 122.55 ? 66  THR D CB  1 
ATOM   3385  O  OG1 . THR B 2 66  ? 136.778 157.707 192.668 1.00 122.55 ? 66  THR D OG1 1 
ATOM   3386  C  CG2 . THR B 2 66  ? 138.488 156.679 193.879 1.00 122.55 ? 66  THR D CG2 1 
ATOM   3387  N  N   . LYS B 2 67  ? 137.320 152.975 192.168 1.00 117.91 ? 67  LYS D N   1 
ATOM   3388  C  CA  . LYS B 2 67  ? 138.037 151.713 192.297 1.00 117.91 ? 67  LYS D CA  1 
ATOM   3389  C  C   . LYS B 2 67  ? 138.885 151.403 191.077 1.00 117.91 ? 67  LYS D C   1 
ATOM   3390  O  O   . LYS B 2 67  ? 140.000 150.895 191.214 1.00 117.91 ? 67  LYS D O   1 
ATOM   3391  C  CB  . LYS B 2 67  ? 137.052 150.563 192.536 1.00 117.91 ? 67  LYS D CB  1 
ATOM   3392  N  N   . TYR B 2 68  ? 138.373 151.702 189.885 1.00 113.92 ? 68  TYR D N   1 
ATOM   3393  C  CA  . TYR B 2 68  ? 139.136 151.648 188.647 1.00 113.92 ? 68  TYR D CA  1 
ATOM   3394  C  C   . TYR B 2 68  ? 139.316 153.012 188.002 1.00 113.92 ? 68  TYR D C   1 
ATOM   3395  O  O   . TYR B 2 68  ? 140.293 153.217 187.279 1.00 113.92 ? 68  TYR D O   1 
ATOM   3396  C  CB  . TYR B 2 68  ? 138.457 150.702 187.647 1.00 113.92 ? 68  TYR D CB  1 
ATOM   3397  C  CG  . TYR B 2 68  ? 138.857 150.912 186.203 1.00 113.92 ? 68  TYR D CG  1 
ATOM   3398  C  CD1 . TYR B 2 68  ? 140.094 150.488 185.736 1.00 113.92 ? 68  TYR D CD1 1 
ATOM   3399  C  CD2 . TYR B 2 68  ? 137.995 151.527 185.306 1.00 113.92 ? 68  TYR D CD2 1 
ATOM   3400  C  CE1 . TYR B 2 68  ? 140.462 150.677 184.418 1.00 113.92 ? 68  TYR D CE1 1 
ATOM   3401  C  CE2 . TYR B 2 68  ? 138.354 151.720 183.986 1.00 113.92 ? 68  TYR D CE2 1 
ATOM   3402  C  CZ  . TYR B 2 68  ? 139.588 151.293 183.548 1.00 113.92 ? 68  TYR D CZ  1 
ATOM   3403  O  OH  . TYR B 2 68  ? 139.949 151.482 182.234 1.00 113.92 ? 68  TYR D OH  1 
ATOM   3404  N  N   . HIS B 2 69  ? 138.415 153.950 188.270 1.00 113.92 ? 69  HIS D N   1 
ATOM   3405  C  CA  . HIS B 2 69  ? 138.493 155.289 187.712 1.00 113.92 ? 69  HIS D CA  1 
ATOM   3406  C  C   . HIS B 2 69  ? 139.326 156.200 188.610 1.00 113.92 ? 69  HIS D C   1 
ATOM   3407  O  O   . HIS B 2 69  ? 139.656 155.866 189.749 1.00 113.92 ? 69  HIS D O   1 
ATOM   3408  C  CB  . HIS B 2 69  ? 137.089 155.866 187.538 1.00 113.92 ? 69  HIS D CB  1 
ATOM   3409  C  CG  . HIS B 2 69  ? 136.305 155.230 186.433 1.00 113.92 ? 69  HIS D CG  1 
ATOM   3410  N  ND1 . HIS B 2 69  ? 136.579 155.448 185.101 1.00 113.92 ? 69  HIS D ND1 1 
ATOM   3411  C  CD2 . HIS B 2 69  ? 135.256 154.375 186.467 1.00 113.92 ? 69  HIS D CD2 1 
ATOM   3412  C  CE1 . HIS B 2 69  ? 135.730 154.758 184.361 1.00 113.92 ? 69  HIS D CE1 1 
ATOM   3413  N  NE2 . HIS B 2 69  ? 134.918 154.097 185.165 1.00 113.92 ? 69  HIS D NE2 1 
ATOM   3414  N  N   . SER B 2 70  ? 139.666 157.369 188.077 1.00 125.57 ? 70  SER D N   1 
ATOM   3415  C  CA  . SER B 2 70  ? 140.385 158.381 188.834 1.00 125.57 ? 70  SER D CA  1 
ATOM   3416  C  C   . SER B 2 70  ? 139.401 159.248 189.610 1.00 125.57 ? 70  SER D C   1 
ATOM   3417  O  O   . SER B 2 70  ? 138.237 159.395 189.226 1.00 125.57 ? 70  SER D O   1 
ATOM   3418  C  CB  . SER B 2 70  ? 141.242 159.250 187.911 1.00 125.57 ? 70  SER D CB  1 
ATOM   3419  O  OG  . SER B 2 70  ? 140.449 159.905 186.941 1.00 125.57 ? 70  SER D OG  1 
ATOM   3420  N  N   . ASP B 2 71  ? 139.880 159.818 190.717 1.00 125.18 ? 71  ASP D N   1 
ATOM   3421  C  CA  . ASP B 2 71  ? 139.031 160.693 191.520 1.00 125.18 ? 71  ASP D CA  1 
ATOM   3422  C  C   . ASP B 2 71  ? 138.643 161.949 190.749 1.00 125.18 ? 71  ASP D C   1 
ATOM   3423  O  O   . ASP B 2 71  ? 137.490 162.395 190.815 1.00 125.18 ? 71  ASP D O   1 
ATOM   3424  C  CB  . ASP B 2 71  ? 139.742 161.061 192.822 1.00 125.18 ? 71  ASP D CB  1 
ATOM   3425  N  N   . GLU B 2 72  ? 139.591 162.530 190.009 1.00 124.50 ? 72  GLU D N   1 
ATOM   3426  C  CA  . GLU B 2 72  ? 139.314 163.767 189.285 1.00 124.50 ? 72  GLU D CA  1 
ATOM   3427  C  C   . GLU B 2 72  ? 138.244 163.555 188.223 1.00 124.50 ? 72  GLU D C   1 
ATOM   3428  O  O   . GLU B 2 72  ? 137.356 164.397 188.049 1.00 124.50 ? 72  GLU D O   1 
ATOM   3429  C  CB  . GLU B 2 72  ? 140.598 164.305 188.654 1.00 124.50 ? 72  GLU D CB  1 
ATOM   3430  N  N   . TYR B 2 73  ? 138.315 162.436 187.500 1.00 115.12 ? 73  TYR D N   1 
ATOM   3431  C  CA  . TYR B 2 73  ? 137.363 162.176 186.425 1.00 115.12 ? 73  TYR D CA  1 
ATOM   3432  C  C   . TYR B 2 73  ? 135.948 162.012 186.966 1.00 115.12 ? 73  TYR D C   1 
ATOM   3433  O  O   . TYR B 2 73  ? 134.991 162.579 186.422 1.00 115.12 ? 73  TYR D O   1 
ATOM   3434  C  CB  . TYR B 2 73  ? 137.791 160.933 185.647 1.00 115.12 ? 73  TYR D CB  1 
ATOM   3435  C  CG  . TYR B 2 73  ? 136.821 160.510 184.574 1.00 115.12 ? 73  TYR D CG  1 
ATOM   3436  C  CD1 . TYR B 2 73  ? 136.494 161.362 183.528 1.00 115.12 ? 73  TYR D CD1 1 
ATOM   3437  C  CD2 . TYR B 2 73  ? 136.228 159.257 184.610 1.00 115.12 ? 73  TYR D CD2 1 
ATOM   3438  C  CE1 . TYR B 2 73  ? 135.607 160.974 182.546 1.00 115.12 ? 73  TYR D CE1 1 
ATOM   3439  C  CE2 . TYR B 2 73  ? 135.341 158.861 183.636 1.00 115.12 ? 73  TYR D CE2 1 
ATOM   3440  C  CZ  . TYR B 2 73  ? 135.035 159.722 182.606 1.00 115.12 ? 73  TYR D CZ  1 
ATOM   3441  O  OH  . TYR B 2 73  ? 134.148 159.324 181.637 1.00 115.12 ? 73  TYR D OH  1 
ATOM   3442  N  N   . ILE B 2 74  ? 135.794 161.232 188.038 1.00 116.55 ? 74  ILE D N   1 
ATOM   3443  C  CA  . ILE B 2 74  ? 134.471 161.029 188.615 1.00 116.55 ? 74  ILE D CA  1 
ATOM   3444  C  C   . ILE B 2 74  ? 133.951 162.324 189.226 1.00 116.55 ? 74  ILE D C   1 
ATOM   3445  O  O   . ILE B 2 74  ? 132.754 162.623 189.147 1.00 116.55 ? 74  ILE D O   1 
ATOM   3446  C  CB  . ILE B 2 74  ? 134.513 159.887 189.647 1.00 116.55 ? 74  ILE D CB  1 
ATOM   3447  C  CG1 . ILE B 2 74  ? 134.966 158.586 188.982 1.00 116.55 ? 74  ILE D CG1 1 
ATOM   3448  C  CG2 . ILE B 2 74  ? 133.151 159.695 190.295 1.00 116.55 ? 74  ILE D CG2 1 
ATOM   3449  C  CD1 . ILE B 2 74  ? 134.157 158.209 187.761 1.00 116.55 ? 74  ILE D CD1 1 
ATOM   3450  N  N   . LYS B 2 75  ? 134.837 163.119 189.833 1.00 119.59 ? 75  LYS D N   1 
ATOM   3451  C  CA  . LYS B 2 75  ? 134.420 164.420 190.351 1.00 119.59 ? 75  LYS D CA  1 
ATOM   3452  C  C   . LYS B 2 75  ? 133.926 165.323 189.227 1.00 119.59 ? 75  LYS D C   1 
ATOM   3453  O  O   . LYS B 2 75  ? 132.907 166.013 189.372 1.00 119.59 ? 75  LYS D O   1 
ATOM   3454  C  CB  . LYS B 2 75  ? 135.574 165.079 191.105 1.00 119.59 ? 75  LYS D CB  1 
ATOM   3455  N  N   . PHE B 2 76  ? 134.626 165.312 188.090 1.00 117.85 ? 76  PHE D N   1 
ATOM   3456  C  CA  . PHE B 2 76  ? 134.207 166.109 186.943 1.00 117.85 ? 76  PHE D CA  1 
ATOM   3457  C  C   . PHE B 2 76  ? 132.844 165.658 186.443 1.00 117.85 ? 76  PHE D C   1 
ATOM   3458  O  O   . PHE B 2 76  ? 131.968 166.485 186.167 1.00 117.85 ? 76  PHE D O   1 
ATOM   3459  C  CB  . PHE B 2 76  ? 135.254 166.014 185.832 1.00 117.85 ? 76  PHE D CB  1 
ATOM   3460  C  CG  . PHE B 2 76  ? 134.719 166.326 184.462 1.00 117.85 ? 76  PHE D CG  1 
ATOM   3461  C  CD1 . PHE B 2 76  ? 134.508 167.636 184.069 1.00 117.85 ? 76  PHE D CD1 1 
ATOM   3462  C  CD2 . PHE B 2 76  ? 134.437 165.310 183.565 1.00 117.85 ? 76  PHE D CD2 1 
ATOM   3463  C  CE1 . PHE B 2 76  ? 134.020 167.927 182.809 1.00 117.85 ? 76  PHE D CE1 1 
ATOM   3464  C  CE2 . PHE B 2 76  ? 133.949 165.595 182.304 1.00 117.85 ? 76  PHE D CE2 1 
ATOM   3465  C  CZ  . PHE B 2 76  ? 133.740 166.905 181.926 1.00 117.85 ? 76  PHE D CZ  1 
ATOM   3466  N  N   . LEU B 2 77  ? 132.646 164.343 186.321 1.00 123.31 ? 77  LEU D N   1 
ATOM   3467  C  CA  . LEU B 2 77  ? 131.367 163.839 185.826 1.00 123.31 ? 77  LEU D CA  1 
ATOM   3468  C  C   . LEU B 2 77  ? 130.238 164.178 186.791 1.00 123.31 ? 77  LEU D C   1 
ATOM   3469  O  O   . LEU B 2 77  ? 129.122 164.500 186.367 1.00 123.31 ? 77  LEU D O   1 
ATOM   3470  C  CB  . LEU B 2 77  ? 131.442 162.329 185.602 1.00 123.31 ? 77  LEU D CB  1 
ATOM   3471  C  CG  . LEU B 2 77  ? 132.072 161.845 184.296 1.00 123.31 ? 77  LEU D CG  1 
ATOM   3472  C  CD1 . LEU B 2 77  ? 132.116 160.328 184.270 1.00 123.31 ? 77  LEU D CD1 1 
ATOM   3473  C  CD2 . LEU B 2 77  ? 131.321 162.387 183.089 1.00 123.31 ? 77  LEU D CD2 1 
ATOM   3474  N  N   . ARG B 2 78  ? 130.507 164.095 188.095 1.00 124.44 ? 78  ARG D N   1 
ATOM   3475  C  CA  . ARG B 2 78  ? 129.485 164.379 189.095 1.00 124.44 ? 78  ARG D CA  1 
ATOM   3476  C  C   . ARG B 2 78  ? 129.131 165.860 189.140 1.00 124.44 ? 78  ARG D C   1 
ATOM   3477  O  O   . ARG B 2 78  ? 127.979 166.210 189.418 1.00 124.44 ? 78  ARG D O   1 
ATOM   3478  C  CB  . ARG B 2 78  ? 129.951 163.904 190.471 1.00 124.44 ? 78  ARG D CB  1 
ATOM   3479  N  N   . SER B 2 79  ? 130.097 166.738 188.876 1.00 132.15 ? 79  SER D N   1 
ATOM   3480  C  CA  . SER B 2 79  ? 129.908 168.171 189.062 1.00 132.15 ? 79  SER D CA  1 
ATOM   3481  C  C   . SER B 2 79  ? 129.451 168.907 187.806 1.00 132.15 ? 79  SER D C   1 
ATOM   3482  O  O   . SER B 2 79  ? 129.320 170.135 187.849 1.00 132.15 ? 79  SER D O   1 
ATOM   3483  C  CB  . SER B 2 79  ? 131.206 168.803 189.577 1.00 132.15 ? 79  SER D CB  1 
ATOM   3484  O  OG  . SER B 2 79  ? 131.670 168.138 190.739 1.00 132.15 ? 79  SER D OG  1 
ATOM   3485  N  N   . ILE B 2 80  ? 129.207 168.213 186.698 1.00 118.80 ? 80  ILE D N   1 
ATOM   3486  C  CA  . ILE B 2 80  ? 128.790 168.855 185.454 1.00 118.80 ? 80  ILE D CA  1 
ATOM   3487  C  C   . ILE B 2 80  ? 127.287 168.657 185.284 1.00 118.80 ? 80  ILE D C   1 
ATOM   3488  O  O   . ILE B 2 80  ? 126.809 167.533 185.097 1.00 118.80 ? 80  ILE D O   1 
ATOM   3489  C  CB  . ILE B 2 80  ? 129.569 168.325 184.241 1.00 118.80 ? 80  ILE D CB  1 
ATOM   3490  C  CG1 . ILE B 2 80  ? 128.954 168.857 182.945 1.00 118.80 ? 80  ILE D CG1 1 
ATOM   3491  C  CG2 . ILE B 2 80  ? 129.603 166.806 184.218 1.00 118.80 ? 80  ILE D CG2 1 
ATOM   3492  C  CD1 . ILE B 2 80  ? 129.947 169.011 181.819 1.00 118.80 ? 80  ILE D CD1 1 
ATOM   3493  N  N   . ARG B 2 81  ? 126.537 169.747 185.370 1.00 116.61 ? 81  ARG D N   1 
ATOM   3494  C  CA  . ARG B 2 81  ? 125.116 169.767 185.064 1.00 116.61 ? 81  ARG D CA  1 
ATOM   3495  C  C   . ARG B 2 81  ? 124.876 170.525 183.761 1.00 116.61 ? 81  ARG D C   1 
ATOM   3496  O  O   . ARG B 2 81  ? 125.706 171.341 183.345 1.00 116.61 ? 81  ARG D O   1 
ATOM   3497  C  CB  . ARG B 2 81  ? 124.319 170.408 186.211 1.00 116.61 ? 81  ARG D CB  1 
ATOM   3498  N  N   . PRO B 2 82  ? 123.756 170.265 183.078 1.00 131.13 ? 82  PRO D N   1 
ATOM   3499  C  CA  . PRO B 2 82  ? 123.514 170.932 181.785 1.00 131.13 ? 82  PRO D CA  1 
ATOM   3500  C  C   . PRO B 2 82  ? 123.504 172.455 181.833 1.00 131.13 ? 82  PRO D C   1 
ATOM   3501  O  O   . PRO B 2 82  ? 123.912 173.094 180.858 1.00 131.13 ? 82  PRO D O   1 
ATOM   3502  C  CB  . PRO B 2 82  ? 122.154 170.365 181.349 1.00 131.13 ? 82  PRO D CB  1 
ATOM   3503  C  CG  . PRO B 2 82  ? 121.511 169.880 182.599 1.00 131.13 ? 82  PRO D CG  1 
ATOM   3504  C  CD  . PRO B 2 82  ? 122.630 169.399 183.470 1.00 131.13 ? 82  PRO D CD  1 
ATOM   3505  N  N   . ASP B 2 83  ? 123.033 173.070 182.913 1.00 136.83 ? 83  ASP D N   1 
ATOM   3506  C  CA  . ASP B 2 83  ? 123.041 174.530 182.957 1.00 136.83 ? 83  ASP D CA  1 
ATOM   3507  C  C   . ASP B 2 83  ? 124.456 175.107 183.000 1.00 136.83 ? 83  ASP D C   1 
ATOM   3508  O  O   . ASP B 2 83  ? 124.749 176.088 182.308 1.00 136.83 ? 83  ASP D O   1 
ATOM   3509  C  CB  . ASP B 2 83  ? 122.234 175.019 184.160 1.00 136.83 ? 83  ASP D CB  1 
ATOM   3510  N  N   . ASN B 2 84  ? 125.349 174.507 183.788 1.00 139.47 ? 84  ASN D N   1 
ATOM   3511  C  CA  . ASN B 2 84  ? 126.703 175.015 183.991 1.00 139.47 ? 84  ASN D CA  1 
ATOM   3512  C  C   . ASN B 2 84  ? 127.767 174.430 183.054 1.00 139.47 ? 84  ASN D C   1 
ATOM   3513  O  O   . ASN B 2 84  ? 128.917 174.273 183.490 1.00 139.47 ? 84  ASN D O   1 
ATOM   3514  C  CB  . ASN B 2 84  ? 127.113 174.819 185.450 1.00 139.47 ? 84  ASN D CB  1 
ATOM   3515  C  CG  . ASN B 2 84  ? 127.180 173.367 185.842 1.00 139.47 ? 84  ASN D CG  1 
ATOM   3516  O  OD1 . ASN B 2 84  ? 126.161 172.751 186.122 1.00 139.47 ? 84  ASN D OD1 1 
ATOM   3517  N  ND2 . ASN B 2 84  ? 128.377 172.805 185.841 1.00 139.47 ? 84  ASN D ND2 1 
ATOM   3518  N  N   . MET B 2 85  ? 127.446 174.082 181.801 1.00 140.60 ? 85  MET D N   1 
ATOM   3519  C  CA  . MET B 2 85  ? 128.529 173.635 180.921 1.00 140.60 ? 85  MET D CA  1 
ATOM   3520  C  C   . MET B 2 85  ? 129.596 174.705 180.715 1.00 140.60 ? 85  MET D C   1 
ATOM   3521  O  O   . MET B 2 85  ? 130.737 174.365 180.382 1.00 140.60 ? 85  MET D O   1 
ATOM   3522  C  CB  . MET B 2 85  ? 128.074 173.215 179.513 1.00 140.60 ? 85  MET D CB  1 
ATOM   3523  C  CG  . MET B 2 85  ? 127.689 171.752 179.292 1.00 140.60 ? 85  MET D CG  1 
ATOM   3524  S  SD  . MET B 2 85  ? 126.579 171.482 177.883 1.00 140.60 ? 85  MET D SD  1 
ATOM   3525  C  CE  . MET B 2 85  ? 124.949 171.517 178.587 1.00 140.60 ? 85  MET D CE  1 
ATOM   3526  N  N   . SER B 2 86  ? 129.253 175.983 180.889 1.00 138.62 ? 86  SER D N   1 
ATOM   3527  C  CA  . SER B 2 86  ? 130.213 177.057 180.651 1.00 138.62 ? 86  SER D CA  1 
ATOM   3528  C  C   . SER B 2 86  ? 131.412 176.987 181.594 1.00 138.62 ? 86  SER D C   1 
ATOM   3529  O  O   . SER B 2 86  ? 132.551 177.217 181.169 1.00 138.62 ? 86  SER D O   1 
ATOM   3530  C  CB  . SER B 2 86  ? 129.517 178.412 180.779 1.00 138.62 ? 86  SER D CB  1 
ATOM   3531  N  N   . GLU B 2 87  ? 131.184 176.687 182.877 1.00 140.80 ? 87  GLU D N   1 
ATOM   3532  C  CA  . GLU B 2 87  ? 132.291 176.701 183.833 1.00 140.80 ? 87  GLU D CA  1 
ATOM   3533  C  C   . GLU B 2 87  ? 133.325 175.628 183.512 1.00 140.80 ? 87  GLU D C   1 
ATOM   3534  O  O   . GLU B 2 87  ? 134.533 175.867 183.626 1.00 140.80 ? 87  GLU D O   1 
ATOM   3535  C  CB  . GLU B 2 87  ? 131.756 176.525 185.254 1.00 140.80 ? 87  GLU D CB  1 
ATOM   3536  N  N   . TYR B 2 88  ? 132.873 174.439 183.113 1.00 139.94 ? 88  TYR D N   1 
ATOM   3537  C  CA  . TYR B 2 88  ? 133.752 173.305 182.858 1.00 139.94 ? 88  TYR D CA  1 
ATOM   3538  C  C   . TYR B 2 88  ? 134.069 173.123 181.379 1.00 139.94 ? 88  TYR D C   1 
ATOM   3539  O  O   . TYR B 2 88  ? 134.529 172.046 180.983 1.00 139.94 ? 88  TYR D O   1 
ATOM   3540  C  CB  . TYR B 2 88  ? 133.176 172.018 183.453 1.00 139.94 ? 88  TYR D CB  1 
ATOM   3541  C  CG  . TYR B 2 88  ? 132.816 172.123 184.916 1.00 139.94 ? 88  TYR D CG  1 
ATOM   3542  C  CD1 . TYR B 2 88  ? 131.587 172.613 185.327 1.00 139.94 ? 88  TYR D CD1 1 
ATOM   3543  C  CD2 . TYR B 2 88  ? 133.720 171.721 185.892 1.00 139.94 ? 88  TYR D CD2 1 
ATOM   3544  C  CE1 . TYR B 2 88  ? 131.274 172.704 186.671 1.00 139.94 ? 88  TYR D CE1 1 
ATOM   3545  C  CE2 . TYR B 2 88  ? 133.413 171.806 187.234 1.00 139.94 ? 88  TYR D CE2 1 
ATOM   3546  C  CZ  . TYR B 2 88  ? 132.188 172.298 187.619 1.00 139.94 ? 88  TYR D CZ  1 
ATOM   3547  O  OH  . TYR B 2 88  ? 131.873 172.386 188.955 1.00 139.94 ? 88  TYR D OH  1 
ATOM   3548  N  N   . SER B 2 89  ? 133.830 174.149 180.556 1.00 140.37 ? 89  SER D N   1 
ATOM   3549  C  CA  . SER B 2 89  ? 134.093 174.036 179.124 1.00 140.37 ? 89  SER D CA  1 
ATOM   3550  C  C   . SER B 2 89  ? 135.538 173.640 178.850 1.00 140.37 ? 89  SER D C   1 
ATOM   3551  O  O   . SER B 2 89  ? 135.820 172.960 177.857 1.00 140.37 ? 89  SER D O   1 
ATOM   3552  C  CB  . SER B 2 89  ? 133.760 175.354 178.425 1.00 140.37 ? 89  SER D CB  1 
ATOM   3553  N  N   . LYS B 2 90  ? 136.465 174.057 179.715 1.00 133.73 ? 90  LYS D N   1 
ATOM   3554  C  CA  . LYS B 2 90  ? 137.869 173.712 179.521 1.00 133.73 ? 90  LYS D CA  1 
ATOM   3555  C  C   . LYS B 2 90  ? 138.109 172.228 179.776 1.00 133.73 ? 90  LYS D C   1 
ATOM   3556  O  O   . LYS B 2 90  ? 138.844 171.575 179.025 1.00 133.73 ? 90  LYS D O   1 
ATOM   3557  C  CB  . LYS B 2 90  ? 138.756 174.576 180.417 1.00 133.73 ? 90  LYS D CB  1 
ATOM   3558  N  N   . GLN B 2 91  ? 137.504 171.675 180.831 1.00 137.52 ? 91  GLN D N   1 
ATOM   3559  C  CA  . GLN B 2 91  ? 137.724 170.275 181.176 1.00 137.52 ? 91  GLN D CA  1 
ATOM   3560  C  C   . GLN B 2 91  ? 136.958 169.314 180.275 1.00 137.52 ? 91  GLN D C   1 
ATOM   3561  O  O   . GLN B 2 91  ? 137.228 168.109 180.320 1.00 137.52 ? 91  GLN D O   1 
ATOM   3562  C  CB  . GLN B 2 91  ? 137.334 169.983 182.635 1.00 137.52 ? 91  GLN D CB  1 
ATOM   3563  C  CG  . GLN B 2 91  ? 138.130 170.681 183.757 1.00 137.52 ? 91  GLN D CG  1 
ATOM   3564  C  CD  . GLN B 2 91  ? 138.018 172.198 183.781 1.00 137.52 ? 91  GLN D CD  1 
ATOM   3565  O  OE1 . GLN B 2 91  ? 137.927 172.851 182.749 1.00 137.52 ? 91  GLN D OE1 1 
ATOM   3566  N  NE2 . GLN B 2 91  ? 138.032 172.765 184.982 1.00 137.52 ? 91  GLN D NE2 1 
ATOM   3567  N  N   . MET B 2 92  ? 136.018 169.805 179.464 1.00 134.70 ? 92  MET D N   1 
ATOM   3568  C  CA  . MET B 2 92  ? 135.288 168.930 178.553 1.00 134.70 ? 92  MET D CA  1 
ATOM   3569  C  C   . MET B 2 92  ? 136.161 168.388 177.429 1.00 134.70 ? 92  MET D C   1 
ATOM   3570  O  O   . MET B 2 92  ? 135.728 167.470 176.724 1.00 134.70 ? 92  MET D O   1 
ATOM   3571  C  CB  . MET B 2 92  ? 134.090 169.664 177.945 1.00 134.70 ? 92  MET D CB  1 
ATOM   3572  C  CG  . MET B 2 92  ? 133.052 170.146 178.941 1.00 134.70 ? 92  MET D CG  1 
ATOM   3573  S  SD  . MET B 2 92  ? 131.386 169.644 178.464 1.00 134.70 ? 92  MET D SD  1 
ATOM   3574  C  CE  . MET B 2 92  ? 131.264 170.370 176.830 1.00 134.70 ? 92  MET D CE  1 
ATOM   3575  N  N   . GLN B 2 93  ? 137.363 168.926 177.244 1.00 121.24 ? 93  GLN D N   1 
ATOM   3576  C  CA  . GLN B 2 93  ? 138.293 168.419 176.246 1.00 121.24 ? 93  GLN D CA  1 
ATOM   3577  C  C   . GLN B 2 93  ? 139.293 167.428 176.818 1.00 121.24 ? 93  GLN D C   1 
ATOM   3578  O  O   . GLN B 2 93  ? 139.735 166.524 176.100 1.00 121.24 ? 93  GLN D O   1 
ATOM   3579  C  CB  . GLN B 2 93  ? 139.051 169.579 175.590 1.00 121.24 ? 93  GLN D CB  1 
ATOM   3580  N  N   . ARG B 2 94  ? 139.656 167.574 178.093 1.00 127.17 ? 94  ARG D N   1 
ATOM   3581  C  CA  . ARG B 2 94  ? 140.570 166.635 178.732 1.00 127.17 ? 94  ARG D CA  1 
ATOM   3582  C  C   . ARG B 2 94  ? 139.912 165.293 179.019 1.00 127.17 ? 94  ARG D C   1 
ATOM   3583  O  O   . ARG B 2 94  ? 140.612 164.280 179.115 1.00 127.17 ? 94  ARG D O   1 
ATOM   3584  C  CB  . ARG B 2 94  ? 141.109 167.242 180.030 1.00 127.17 ? 94  ARG D CB  1 
ATOM   3585  C  CG  . ARG B 2 94  ? 142.215 166.443 180.700 1.00 127.17 ? 94  ARG D CG  1 
ATOM   3586  C  CD  . ARG B 2 94  ? 142.942 167.283 181.750 1.00 127.17 ? 94  ARG D CD  1 
ATOM   3587  N  NE  . ARG B 2 94  ? 143.224 166.595 183.010 1.00 127.17 ? 94  ARG D NE  1 
ATOM   3588  C  CZ  . ARG B 2 94  ? 143.763 165.388 183.142 1.00 127.17 ? 94  ARG D CZ  1 
ATOM   3589  N  NH1 . ARG B 2 94  ? 144.164 164.682 182.097 1.00 127.17 ? 94  ARG D NH1 1 
ATOM   3590  N  NH2 . ARG B 2 94  ? 143.918 164.880 184.361 1.00 127.17 ? 94  ARG D NH2 1 
ATOM   3591  N  N   . PHE B 2 95  ? 138.586 165.258 179.139 1.00 113.92 ? 95  PHE D N   1 
ATOM   3592  C  CA  . PHE B 2 95  ? 137.872 164.042 179.495 1.00 113.92 ? 95  PHE D CA  1 
ATOM   3593  C  C   . PHE B 2 95  ? 136.940 163.545 178.400 1.00 113.92 ? 95  PHE D C   1 
ATOM   3594  O  O   . PHE B 2 95  ? 136.230 162.556 178.617 1.00 113.92 ? 95  PHE D O   1 
ATOM   3595  C  CB  . PHE B 2 95  ? 137.080 164.260 180.790 1.00 113.92 ? 95  PHE D CB  1 
ATOM   3596  C  CG  . PHE B 2 95  ? 137.946 164.393 182.010 1.00 113.92 ? 95  PHE D CG  1 
ATOM   3597  C  CD1 . PHE B 2 95  ? 138.905 163.439 182.300 1.00 113.92 ? 95  PHE D CD1 1 
ATOM   3598  C  CD2 . PHE B 2 95  ? 137.806 165.475 182.862 1.00 113.92 ? 95  PHE D CD2 1 
ATOM   3599  C  CE1 . PHE B 2 95  ? 139.703 163.557 183.421 1.00 113.92 ? 95  PHE D CE1 1 
ATOM   3600  C  CE2 . PHE B 2 95  ? 138.602 165.598 183.984 1.00 113.92 ? 95  PHE D CE2 1 
ATOM   3601  C  CZ  . PHE B 2 95  ? 139.552 164.638 184.263 1.00 113.92 ? 95  PHE D CZ  1 
ATOM   3602  N  N   . ASN B 2 96  ? 136.922 164.198 177.235 1.00 113.92 ? 96  ASN D N   1 
ATOM   3603  C  CA  . ASN B 2 96  ? 136.171 163.727 176.070 1.00 113.92 ? 96  ASN D CA  1 
ATOM   3604  C  C   . ASN B 2 96  ? 134.682 163.572 176.383 1.00 113.92 ? 96  ASN D C   1 
ATOM   3605  O  O   . ASN B 2 96  ? 134.056 162.568 176.038 1.00 113.92 ? 96  ASN D O   1 
ATOM   3606  C  CB  . ASN B 2 96  ? 136.760 162.420 175.531 1.00 113.92 ? 96  ASN D CB  1 
ATOM   3607  C  CG  . ASN B 2 96  ? 136.200 162.038 174.174 1.00 113.92 ? 96  ASN D CG  1 
ATOM   3608  O  OD1 . ASN B 2 96  ? 136.470 162.696 173.169 1.00 113.92 ? 96  ASN D OD1 1 
ATOM   3609  N  ND2 . ASN B 2 96  ? 135.415 160.968 174.139 1.00 113.92 ? 96  ASN D ND2 1 
ATOM   3610  N  N   . VAL B 2 97  ? 134.110 164.567 177.056 1.00 113.92 ? 97  VAL D N   1 
ATOM   3611  C  CA  . VAL B 2 97  ? 132.681 164.602 177.344 1.00 113.92 ? 97  VAL D CA  1 
ATOM   3612  C  C   . VAL B 2 97  ? 132.101 165.880 176.758 1.00 113.92 ? 97  VAL D C   1 
ATOM   3613  O  O   . VAL B 2 97  ? 132.591 166.978 177.047 1.00 113.92 ? 97  VAL D O   1 
ATOM   3614  C  CB  . VAL B 2 97  ? 132.406 164.537 178.857 1.00 113.92 ? 97  VAL D CB  1 
ATOM   3615  C  CG1 . VAL B 2 97  ? 130.966 164.927 179.155 1.00 113.92 ? 97  VAL D CG1 1 
ATOM   3616  C  CG2 . VAL B 2 97  ? 132.712 163.158 179.400 1.00 113.92 ? 97  VAL D CG2 1 
ATOM   3617  N  N   . GLY B 2 98  ? 131.062 165.739 175.939 1.00 122.55 ? 98  GLY D N   1 
ATOM   3618  C  CA  . GLY B 2 98  ? 130.312 166.888 175.473 1.00 122.55 ? 98  GLY D CA  1 
ATOM   3619  C  C   . GLY B 2 98  ? 129.921 166.856 174.009 1.00 122.55 ? 98  GLY D C   1 
ATOM   3620  O  O   . GLY B 2 98  ? 128.918 167.462 173.621 1.00 122.55 ? 98  GLY D O   1 
ATOM   3621  N  N   . GLU B 2 99  ? 130.694 166.149 173.186 1.00 118.51 ? 99  GLU D N   1 
ATOM   3622  C  CA  . GLU B 2 99  ? 130.414 166.101 171.756 1.00 118.51 ? 99  GLU D CA  1 
ATOM   3623  C  C   . GLU B 2 99  ? 129.935 164.725 171.310 1.00 118.51 ? 99  GLU D C   1 
ATOM   3624  O  O   . GLU B 2 99  ? 128.745 164.530 171.045 1.00 118.51 ? 99  GLU D O   1 
ATOM   3625  C  CB  . GLU B 2 99  ? 131.657 166.504 170.960 1.00 118.51 ? 99  GLU D CB  1 
ATOM   3626  N  N   . ASP B 2 100 ? 130.863 163.770 171.217 1.00 123.89 ? 100 ASP D N   1 
ATOM   3627  C  CA  . ASP B 2 100 ? 130.503 162.426 170.776 1.00 123.89 ? 100 ASP D CA  1 
ATOM   3628  C  C   . ASP B 2 100 ? 129.553 161.757 171.756 1.00 123.89 ? 100 ASP D C   1 
ATOM   3629  O  O   . ASP B 2 100 ? 128.651 161.013 171.353 1.00 123.89 ? 100 ASP D O   1 
ATOM   3630  C  CB  . ASP B 2 100 ? 131.765 161.584 170.605 1.00 123.89 ? 100 ASP D CB  1 
ATOM   3631  N  N   . CYS B 2 101 ? 129.745 162.004 173.049 1.00 130.73 ? 101 CYS D N   1 
ATOM   3632  C  CA  . CYS B 2 101 ? 128.902 161.459 174.108 1.00 130.73 ? 101 CYS D CA  1 
ATOM   3633  C  C   . CYS B 2 101 ? 128.386 162.634 174.933 1.00 130.73 ? 101 CYS D C   1 
ATOM   3634  O  O   . CYS B 2 101 ? 128.799 162.829 176.085 1.00 130.73 ? 101 CYS D O   1 
ATOM   3635  C  CB  . CYS B 2 101 ? 129.679 160.458 174.959 1.00 130.73 ? 101 CYS D CB  1 
ATOM   3636  S  SG  . CYS B 2 101 ? 128.713 159.654 176.232 1.00 130.73 ? 101 CYS D SG  1 
ATOM   3637  N  N   . PRO B 2 102 ? 127.499 163.451 174.361 1.00 134.17 ? 102 PRO D N   1 
ATOM   3638  C  CA  . PRO B 2 102 ? 127.122 164.716 175.007 1.00 134.17 ? 102 PRO D CA  1 
ATOM   3639  C  C   . PRO B 2 102 ? 126.541 164.526 176.401 1.00 134.17 ? 102 PRO D C   1 
ATOM   3640  O  O   . PRO B 2 102 ? 125.994 163.477 176.750 1.00 134.17 ? 102 PRO D O   1 
ATOM   3641  C  CB  . PRO B 2 102 ? 126.079 165.322 174.056 1.00 134.17 ? 102 PRO D CB  1 
ATOM   3642  C  CG  . PRO B 2 102 ? 125.964 164.409 172.893 1.00 134.17 ? 102 PRO D CG  1 
ATOM   3643  C  CD  . PRO B 2 102 ? 126.698 163.147 173.163 1.00 134.17 ? 102 PRO D CD  1 
ATOM   3644  N  N   . VAL B 2 103 ? 126.674 165.581 177.201 1.00 132.07 ? 103 VAL D N   1 
ATOM   3645  C  CA  . VAL B 2 103 ? 126.120 165.631 178.548 1.00 132.07 ? 103 VAL D CA  1 
ATOM   3646  C  C   . VAL B 2 103 ? 124.634 165.955 178.468 1.00 132.07 ? 103 VAL D C   1 
ATOM   3647  O  O   . VAL B 2 103 ? 124.196 166.728 177.608 1.00 132.07 ? 103 VAL D O   1 
ATOM   3648  C  CB  . VAL B 2 103 ? 126.891 166.663 179.394 1.00 132.07 ? 103 VAL D CB  1 
ATOM   3649  C  CG1 . VAL B 2 103 ? 127.100 167.946 178.602 1.00 132.07 ? 103 VAL D CG1 1 
ATOM   3650  C  CG2 . VAL B 2 103 ? 126.184 166.948 180.712 1.00 132.07 ? 103 VAL D CG2 1 
ATOM   3651  N  N   . PHE B 2 104 ? 123.849 165.365 179.371 1.00 122.08 ? 104 PHE D N   1 
ATOM   3652  C  CA  . PHE B 2 104 ? 122.410 165.579 179.423 1.00 122.08 ? 104 PHE D CA  1 
ATOM   3653  C  C   . PHE B 2 104 ? 121.966 165.622 180.880 1.00 122.08 ? 104 PHE D C   1 
ATOM   3654  O  O   . PHE B 2 104 ? 122.784 165.554 181.804 1.00 122.08 ? 104 PHE D O   1 
ATOM   3655  C  CB  . PHE B 2 104 ? 121.669 164.497 178.627 1.00 122.08 ? 104 PHE D CB  1 
ATOM   3656  C  CG  . PHE B 2 104 ? 121.938 163.099 179.106 1.00 122.08 ? 104 PHE D CG  1 
ATOM   3657  C  CD1 . PHE B 2 104 ? 121.220 162.559 180.158 1.00 122.08 ? 104 PHE D CD1 1 
ATOM   3658  C  CD2 . PHE B 2 104 ? 122.919 162.328 178.508 1.00 122.08 ? 104 PHE D CD2 1 
ATOM   3659  C  CE1 . PHE B 2 104 ? 121.469 161.278 180.600 1.00 122.08 ? 104 PHE D CE1 1 
ATOM   3660  C  CE2 . PHE B 2 104 ? 123.174 161.045 178.947 1.00 122.08 ? 104 PHE D CE2 1 
ATOM   3661  C  CZ  . PHE B 2 104 ? 122.447 160.520 179.994 1.00 122.08 ? 104 PHE D CZ  1 
ATOM   3662  N  N   . ASP B 2 105 ? 120.655 165.734 181.087 1.00 127.75 ? 105 ASP D N   1 
ATOM   3663  C  CA  . ASP B 2 105 ? 120.126 165.884 182.436 1.00 127.75 ? 105 ASP D CA  1 
ATOM   3664  C  C   . ASP B 2 105 ? 120.220 164.577 183.212 1.00 127.75 ? 105 ASP D C   1 
ATOM   3665  O  O   . ASP B 2 105 ? 119.862 163.509 182.706 1.00 127.75 ? 105 ASP D O   1 
ATOM   3666  C  CB  . ASP B 2 105 ? 118.674 166.354 182.380 1.00 127.75 ? 105 ASP D CB  1 
ATOM   3667  N  N   . GLY B 2 106 ? 120.692 164.673 184.450 1.00 122.75 ? 106 GLY D N   1 
ATOM   3668  C  CA  . GLY B 2 106 ? 120.836 163.514 185.316 1.00 122.75 ? 106 GLY D CA  1 
ATOM   3669  C  C   . GLY B 2 106 ? 121.823 162.486 184.812 1.00 122.75 ? 106 GLY D C   1 
ATOM   3670  O  O   . GLY B 2 106 ? 121.566 161.280 184.917 1.00 122.75 ? 106 GLY D O   1 
ATOM   3671  N  N   . LEU B 2 107 ? 122.946 162.935 184.247 1.00 116.55 ? 107 LEU D N   1 
ATOM   3672  C  CA  . LEU B 2 107 ? 123.921 161.994 183.706 1.00 116.55 ? 107 LEU D CA  1 
ATOM   3673  C  C   . LEU B 2 107 ? 124.506 161.130 184.817 1.00 116.55 ? 107 LEU D C   1 
ATOM   3674  O  O   . LEU B 2 107 ? 124.604 159.897 184.689 1.00 116.55 ? 107 LEU D O   1 
ATOM   3675  C  CB  . LEU B 2 107 ? 125.021 162.754 182.970 1.00 116.55 ? 107 LEU D CB  1 
ATOM   3676  C  CG  . LEU B 2 107 ? 126.179 161.914 182.442 1.00 116.55 ? 107 LEU D CG  1 
ATOM   3677  C  CD1 . LEU B 2 107 ? 125.626 160.710 181.706 1.00 116.55 ? 107 LEU D CD1 1 
ATOM   3678  C  CD2 . LEU B 2 107 ? 127.067 162.748 181.537 1.00 116.55 ? 107 LEU D CD2 1 
ATOM   3679  N  N   . PHE B 2 108 ? 124.862 161.761 185.938 1.00 125.08 ? 108 PHE D N   1 
ATOM   3680  C  CA  . PHE B 2 108 ? 125.421 160.997 187.040 1.00 125.08 ? 108 PHE D CA  1 
ATOM   3681  C  C   . PHE B 2 108 ? 124.364 160.072 187.615 1.00 125.08 ? 108 PHE D C   1 
ATOM   3682  O  O   . PHE B 2 108 ? 124.680 158.958 188.035 1.00 125.08 ? 108 PHE D O   1 
ATOM   3683  C  CB  . PHE B 2 108 ? 125.980 161.932 188.112 1.00 125.08 ? 108 PHE D CB  1 
ATOM   3684  C  CG  . PHE B 2 108 ? 126.847 161.240 189.127 1.00 125.08 ? 108 PHE D CG  1 
ATOM   3685  C  CD1 . PHE B 2 108 ? 128.021 160.616 188.739 1.00 125.08 ? 108 PHE D CD1 1 
ATOM   3686  C  CD2 . PHE B 2 108 ? 126.497 161.221 190.466 1.00 125.08 ? 108 PHE D CD2 1 
ATOM   3687  C  CE1 . PHE B 2 108 ? 128.825 159.982 189.666 1.00 125.08 ? 108 PHE D CE1 1 
ATOM   3688  C  CE2 . PHE B 2 108 ? 127.300 160.588 191.399 1.00 125.08 ? 108 PHE D CE2 1 
ATOM   3689  C  CZ  . PHE B 2 108 ? 128.465 159.968 190.997 1.00 125.08 ? 108 PHE D CZ  1 
ATOM   3690  N  N   . GLU B 2 109 ? 123.108 160.530 187.681 1.00 121.69 ? 109 GLU D N   1 
ATOM   3691  C  CA  . GLU B 2 109 ? 122.056 159.650 188.175 1.00 121.69 ? 109 GLU D CA  1 
ATOM   3692  C  C   . GLU B 2 109 ? 121.896 158.454 187.247 1.00 121.69 ? 109 GLU D C   1 
ATOM   3693  O  O   . GLU B 2 109 ? 121.540 157.357 187.694 1.00 121.69 ? 109 GLU D O   1 
ATOM   3694  C  CB  . GLU B 2 109 ? 120.741 160.416 188.308 1.00 121.69 ? 109 GLU D CB  1 
ATOM   3695  N  N   . PHE B 2 110 ? 122.159 158.654 185.949 1.00 117.03 ? 110 PHE D N   1 
ATOM   3696  C  CA  . PHE B 2 110 ? 122.094 157.559 184.987 1.00 117.03 ? 110 PHE D CA  1 
ATOM   3697  C  C   . PHE B 2 110 ? 123.175 156.531 185.275 1.00 117.03 ? 110 PHE D C   1 
ATOM   3698  O  O   . PHE B 2 110 ? 122.928 155.319 185.212 1.00 117.03 ? 110 PHE D O   1 
ATOM   3699  C  CB  . PHE B 2 110 ? 122.228 158.081 183.554 1.00 117.03 ? 110 PHE D CB  1 
ATOM   3700  C  CG  . PHE B 2 110 ? 122.266 156.991 182.510 1.00 117.03 ? 110 PHE D CG  1 
ATOM   3701  C  CD1 . PHE B 2 110 ? 121.341 155.959 182.528 1.00 117.03 ? 110 PHE D CD1 1 
ATOM   3702  C  CD2 . PHE B 2 110 ? 123.227 157.000 181.510 1.00 117.03 ? 110 PHE D CD2 1 
ATOM   3703  C  CE1 . PHE B 2 110 ? 121.375 154.956 181.573 1.00 117.03 ? 110 PHE D CE1 1 
ATOM   3704  C  CE2 . PHE B 2 110 ? 123.264 156.000 180.551 1.00 117.03 ? 110 PHE D CE2 1 
ATOM   3705  C  CZ  . PHE B 2 110 ? 122.338 154.979 180.583 1.00 117.03 ? 110 PHE D CZ  1 
ATOM   3706  N  N   . CYS B 2 111 ? 124.379 156.999 185.612 1.00 123.56 ? 111 CYS D N   1 
ATOM   3707  C  CA  . CYS B 2 111 ? 125.436 156.049 185.934 1.00 123.56 ? 111 CYS D CA  1 
ATOM   3708  C  C   . CYS B 2 111 ? 125.322 155.490 187.347 1.00 123.56 ? 111 CYS D C   1 
ATOM   3709  O  O   . CYS B 2 111 ? 125.959 154.475 187.649 1.00 123.56 ? 111 CYS D O   1 
ATOM   3710  C  CB  . CYS B 2 111 ? 126.805 156.708 185.757 1.00 123.56 ? 111 CYS D CB  1 
ATOM   3711  S  SG  . CYS B 2 111 ? 127.131 157.317 184.089 1.00 123.56 ? 111 CYS D SG  1 
ATOM   3712  N  N   . GLN B 2 112 ? 124.537 156.129 188.219 1.00 132.70 ? 112 GLN D N   1 
ATOM   3713  C  CA  . GLN B 2 112 ? 124.201 155.537 189.512 1.00 132.70 ? 112 GLN D CA  1 
ATOM   3714  C  C   . GLN B 2 112 ? 123.460 154.218 189.365 1.00 132.70 ? 112 GLN D C   1 
ATOM   3715  O  O   . GLN B 2 112 ? 123.511 153.381 190.273 1.00 132.70 ? 112 GLN D O   1 
ATOM   3716  C  CB  . GLN B 2 112 ? 123.342 156.493 190.345 1.00 132.70 ? 112 GLN D CB  1 
ATOM   3717  C  CG  . GLN B 2 112 ? 124.012 157.798 190.729 1.00 132.70 ? 112 GLN D CG  1 
ATOM   3718  C  CD  . GLN B 2 112 ? 125.345 157.595 191.410 1.00 132.70 ? 112 GLN D CD  1 
ATOM   3719  O  OE1 . GLN B 2 112 ? 126.394 157.653 190.772 1.00 132.70 ? 112 GLN D OE1 1 
ATOM   3720  N  NE2 . GLN B 2 112 ? 125.314 157.368 192.718 1.00 132.70 ? 112 GLN D NE2 1 
ATOM   3721  N  N   . LEU B 2 113 ? 122.777 154.016 188.243 1.00 126.46 ? 113 LEU D N   1 
ATOM   3722  C  CA  . LEU B 2 113 ? 121.962 152.835 187.997 1.00 126.46 ? 113 LEU D CA  1 
ATOM   3723  C  C   . LEU B 2 113 ? 122.531 151.913 186.934 1.00 126.46 ? 113 LEU D C   1 
ATOM   3724  O  O   . LEU B 2 113 ? 122.396 150.694 187.052 1.00 126.46 ? 113 LEU D O   1 
ATOM   3725  C  CB  . LEU B 2 113 ? 120.544 153.261 187.600 1.00 126.46 ? 113 LEU D CB  1 
ATOM   3726  C  CG  . LEU B 2 113 ? 119.950 154.313 188.542 1.00 126.46 ? 113 LEU D CG  1 
ATOM   3727  C  CD1 . LEU B 2 113 ? 118.557 154.732 188.110 1.00 126.46 ? 113 LEU D CD1 1 
ATOM   3728  C  CD2 . LEU B 2 113 ? 119.934 153.807 189.977 1.00 126.46 ? 113 LEU D CD2 1 
ATOM   3729  N  N   . SER B 2 114 ? 123.154 152.458 185.884 1.00 118.02 ? 114 SER D N   1 
ATOM   3730  C  CA  . SER B 2 114 ? 123.788 151.593 184.894 1.00 118.02 ? 114 SER D CA  1 
ATOM   3731  C  C   . SER B 2 114 ? 124.911 150.769 185.511 1.00 118.02 ? 114 SER D C   1 
ATOM   3732  O  O   . SER B 2 114 ? 125.144 149.627 185.098 1.00 118.02 ? 114 SER D O   1 
ATOM   3733  C  CB  . SER B 2 114 ? 124.317 152.428 183.729 1.00 118.02 ? 114 SER D CB  1 
ATOM   3734  O  OG  . SER B 2 114 ? 124.798 151.598 182.686 1.00 118.02 ? 114 SER D OG  1 
ATOM   3735  N  N   . THR B 2 115 ? 125.618 151.329 186.494 1.00 122.27 ? 115 THR D N   1 
ATOM   3736  C  CA  . THR B 2 115 ? 126.675 150.621 187.206 1.00 122.27 ? 115 THR D CA  1 
ATOM   3737  C  C   . THR B 2 115 ? 126.164 149.901 188.450 1.00 122.27 ? 115 THR D C   1 
ATOM   3738  O  O   . THR B 2 115 ? 126.739 148.878 188.842 1.00 122.27 ? 115 THR D O   1 
ATOM   3739  C  CB  . THR B 2 115 ? 127.789 151.616 187.577 1.00 122.27 ? 115 THR D CB  1 
ATOM   3740  O  OG1 . THR B 2 115 ? 128.614 151.856 186.431 1.00 122.27 ? 115 THR D OG1 1 
ATOM   3741  C  CG2 . THR B 2 115 ? 128.663 151.110 188.719 1.00 122.27 ? 115 THR D CG2 1 
ATOM   3742  N  N   . GLY B 2 116 ? 125.054 150.364 189.027 1.00 123.21 ? 116 GLY D N   1 
ATOM   3743  C  CA  . GLY B 2 116 ? 124.542 149.800 190.265 1.00 123.21 ? 116 GLY D CA  1 
ATOM   3744  C  C   . GLY B 2 116 ? 124.125 148.348 190.168 1.00 123.21 ? 116 GLY D C   1 
ATOM   3745  O  O   . GLY B 2 116 ? 123.988 147.683 191.199 1.00 123.21 ? 116 GLY D O   1 
ATOM   3746  N  N   . GLY B 2 117 ? 123.918 147.842 188.957 1.00 113.92 ? 117 GLY D N   1 
ATOM   3747  C  CA  . GLY B 2 117 ? 123.455 146.483 188.759 1.00 113.92 ? 117 GLY D CA  1 
ATOM   3748  C  C   . GLY B 2 117 ? 124.592 145.497 188.595 1.00 113.92 ? 117 GLY D C   1 
ATOM   3749  O  O   . GLY B 2 117 ? 124.445 144.308 188.893 1.00 113.92 ? 117 GLY D O   1 
ATOM   3750  N  N   . SER B 2 118 ? 125.737 145.984 188.118 1.00 115.21 ? 118 SER D N   1 
ATOM   3751  C  CA  . SER B 2 118 ? 126.882 145.113 187.882 1.00 115.21 ? 118 SER D CA  1 
ATOM   3752  C  C   . SER B 2 118 ? 127.593 144.755 189.181 1.00 115.21 ? 118 SER D C   1 
ATOM   3753  O  O   . SER B 2 118 ? 127.819 143.576 189.462 1.00 115.21 ? 118 SER D O   1 
ATOM   3754  C  CB  . SER B 2 118 ? 127.850 145.782 186.910 1.00 115.21 ? 118 SER D CB  1 
ATOM   3755  O  OG  . SER B 2 118 ? 127.190 146.097 185.701 1.00 115.21 ? 118 SER D OG  1 
ATOM   3756  N  N   . VAL B 2 119 ? 127.981 145.758 189.969 1.00 122.62 ? 119 VAL D N   1 
ATOM   3757  C  CA  . VAL B 2 119 ? 128.644 145.490 191.245 1.00 122.62 ? 119 VAL D CA  1 
ATOM   3758  C  C   . VAL B 2 119 ? 127.708 144.745 192.197 1.00 122.62 ? 119 VAL D C   1 
ATOM   3759  O  O   . VAL B 2 119 ? 128.087 143.738 192.809 1.00 122.62 ? 119 VAL D O   1 
ATOM   3760  C  CB  . VAL B 2 119 ? 129.183 146.797 191.858 1.00 122.62 ? 119 VAL D CB  1 
ATOM   3761  C  CG1 . VAL B 2 119 ? 130.231 147.406 190.942 1.00 122.62 ? 119 VAL D CG1 1 
ATOM   3762  C  CG2 . VAL B 2 119 ? 128.064 147.805 192.089 1.00 122.62 ? 119 VAL D CG2 1 
ATOM   3763  N  N   . ALA B 2 120 ? 126.457 145.202 192.304 1.00 128.55 ? 120 ALA D N   1 
ATOM   3764  C  CA  . ALA B 2 120 ? 125.498 144.557 193.195 1.00 128.55 ? 120 ALA D CA  1 
ATOM   3765  C  C   . ALA B 2 120 ? 125.002 143.222 192.660 1.00 128.55 ? 120 ALA D C   1 
ATOM   3766  O  O   . ALA B 2 120 ? 124.458 142.426 193.432 1.00 128.55 ? 120 ALA D O   1 
ATOM   3767  C  CB  . ALA B 2 120 ? 124.311 145.483 193.454 1.00 128.55 ? 120 ALA D CB  1 
ATOM   3768  N  N   . GLY B 2 121 ? 125.173 142.954 191.369 1.00 122.27 ? 121 GLY D N   1 
ATOM   3769  C  CA  . GLY B 2 121 ? 124.838 141.644 190.851 1.00 122.27 ? 121 GLY D CA  1 
ATOM   3770  C  C   . GLY B 2 121 ? 125.983 140.674 191.044 1.00 122.27 ? 121 GLY D C   1 
ATOM   3771  O  O   . GLY B 2 121 ? 125.770 139.508 191.385 1.00 122.27 ? 121 GLY D O   1 
ATOM   3772  N  N   . ALA B 2 122 ? 127.209 141.151 190.826 1.00 121.64 ? 122 ALA D N   1 
ATOM   3773  C  CA  . ALA B 2 122 ? 128.390 140.355 191.129 1.00 121.64 ? 122 ALA D CA  1 
ATOM   3774  C  C   . ALA B 2 122 ? 128.509 140.055 192.615 1.00 121.64 ? 122 ALA D C   1 
ATOM   3775  O  O   . ALA B 2 122 ? 129.135 139.057 192.982 1.00 121.64 ? 122 ALA D O   1 
ATOM   3776  C  CB  . ALA B 2 122 ? 129.649 141.067 190.633 1.00 121.64 ? 122 ALA D CB  1 
ATOM   3777  N  N   . VAL B 2 123 ? 127.917 140.888 193.477 1.00 122.52 ? 123 VAL D N   1 
ATOM   3778  C  CA  . VAL B 2 123 ? 127.911 140.582 194.907 1.00 122.52 ? 123 VAL D CA  1 
ATOM   3779  C  C   . VAL B 2 123 ? 127.148 139.290 195.168 1.00 122.52 ? 123 VAL D C   1 
ATOM   3780  O  O   . VAL B 2 123 ? 127.600 138.419 195.920 1.00 122.52 ? 123 VAL D O   1 
ATOM   3781  C  CB  . VAL B 2 123 ? 127.312 141.755 195.706 1.00 122.52 ? 123 VAL D CB  1 
ATOM   3782  C  CG1 . VAL B 2 123 ? 126.593 141.249 196.951 1.00 122.52 ? 123 VAL D CG1 1 
ATOM   3783  C  CG2 . VAL B 2 123 ? 128.398 142.725 196.111 1.00 122.52 ? 123 VAL D CG2 1 
ATOM   3784  N  N   . LYS B 2 124 ? 125.972 139.150 194.556 1.00 130.84 ? 124 LYS D N   1 
ATOM   3785  C  CA  . LYS B 2 124 ? 125.217 137.912 194.704 1.00 130.84 ? 124 LYS D CA  1 
ATOM   3786  C  C   . LYS B 2 124 ? 125.866 136.765 193.937 1.00 130.84 ? 124 LYS D C   1 
ATOM   3787  O  O   . LYS B 2 124 ? 125.862 135.620 194.403 1.00 130.84 ? 124 LYS D O   1 
ATOM   3788  C  CB  . LYS B 2 124 ? 123.777 138.128 194.244 1.00 130.84 ? 124 LYS D CB  1 
ATOM   3789  C  CG  . LYS B 2 124 ? 122.772 138.183 195.381 1.00 130.84 ? 124 LYS D CG  1 
ATOM   3790  C  CD  . LYS B 2 124 ? 121.348 138.124 194.862 1.00 130.84 ? 124 LYS D CD  1 
ATOM   3791  C  CE  . LYS B 2 124 ? 120.340 138.174 195.999 1.00 130.84 ? 124 LYS D CE  1 
ATOM   3792  N  NZ  . LYS B 2 124 ? 120.333 139.496 196.682 1.00 130.84 ? 124 LYS D NZ  1 
ATOM   3793  N  N   . LEU B 2 125 ? 126.418 137.051 192.755 1.00 118.35 ? 125 LEU D N   1 
ATOM   3794  C  CA  . LEU B 2 125 ? 126.992 135.999 191.920 1.00 118.35 ? 125 LEU D CA  1 
ATOM   3795  C  C   . LEU B 2 125 ? 128.218 135.358 192.564 1.00 118.35 ? 125 LEU D C   1 
ATOM   3796  O  O   . LEU B 2 125 ? 128.346 134.128 192.580 1.00 118.35 ? 125 LEU D O   1 
ATOM   3797  C  CB  . LEU B 2 125 ? 127.333 136.557 190.540 1.00 118.35 ? 125 LEU D CB  1 
ATOM   3798  C  CG  . LEU B 2 125 ? 128.016 135.577 189.587 1.00 118.35 ? 125 LEU D CG  1 
ATOM   3799  C  CD1 . LEU B 2 125 ? 127.314 135.603 188.252 1.00 118.35 ? 125 LEU D CD1 1 
ATOM   3800  C  CD2 . LEU B 2 125 ? 129.481 135.918 189.414 1.00 118.35 ? 125 LEU D CD2 1 
ATOM   3801  N  N   . ASN B 2 126 ? 129.140 136.171 193.089 1.00 125.73 ? 126 ASN D N   1 
ATOM   3802  C  CA  . ASN B 2 126 ? 130.327 135.606 193.722 1.00 125.73 ? 126 ASN D CA  1 
ATOM   3803  C  C   . ASN B 2 126 ? 129.954 134.813 194.966 1.00 125.73 ? 126 ASN D C   1 
ATOM   3804  O  O   . ASN B 2 126 ? 130.532 133.754 195.237 1.00 125.73 ? 126 ASN D O   1 
ATOM   3805  C  CB  . ASN B 2 126 ? 131.348 136.709 194.033 1.00 125.73 ? 126 ASN D CB  1 
ATOM   3806  C  CG  . ASN B 2 126 ? 130.863 137.712 195.076 1.00 125.73 ? 126 ASN D CG  1 
ATOM   3807  O  OD1 . ASN B 2 126 ? 130.109 137.383 195.990 1.00 125.73 ? 126 ASN D OD1 1 
ATOM   3808  N  ND2 . ASN B 2 126 ? 131.307 138.955 194.933 1.00 125.73 ? 126 ASN D ND2 1 
ATOM   3809  N  N   . ARG B 2 127 ? 128.990 135.311 195.733 1.00 121.70 ? 127 ARG D N   1 
ATOM   3810  C  CA  . ARG B 2 127 ? 128.489 134.588 196.886 1.00 121.70 ? 127 ARG D CA  1 
ATOM   3811  C  C   . ARG B 2 127 ? 127.593 133.441 196.425 1.00 121.70 ? 127 ARG D C   1 
ATOM   3812  O  O   . ARG B 2 127 ? 127.245 133.321 195.247 1.00 121.70 ? 127 ARG D O   1 
ATOM   3813  C  CB  . ARG B 2 127 ? 127.728 135.528 197.820 1.00 121.70 ? 127 ARG D CB  1 
ATOM   3814  N  N   . GLN B 2 128 ? 127.222 132.580 197.371 1.00 124.04 ? 128 GLN D N   1 
ATOM   3815  C  CA  . GLN B 2 128 ? 126.384 131.422 197.066 1.00 124.04 ? 128 GLN D CA  1 
ATOM   3816  C  C   . GLN B 2 128 ? 124.907 131.824 197.054 1.00 124.04 ? 128 GLN D C   1 
ATOM   3817  O  O   . GLN B 2 128 ? 124.098 131.382 197.869 1.00 124.04 ? 128 GLN D O   1 
ATOM   3818  C  CB  . GLN B 2 128 ? 126.651 130.303 198.064 1.00 124.04 ? 128 GLN D CB  1 
ATOM   3819  N  N   . GLN B 2 129 ? 124.563 132.685 196.096 1.00 128.80 ? 129 GLN D N   1 
ATOM   3820  C  CA  . GLN B 2 129 ? 123.199 133.174 195.952 1.00 128.80 ? 129 GLN D CA  1 
ATOM   3821  C  C   . GLN B 2 129 ? 122.599 132.946 194.574 1.00 128.80 ? 129 GLN D C   1 
ATOM   3822  O  O   . GLN B 2 129 ? 121.374 132.849 194.466 1.00 128.80 ? 129 GLN D O   1 
ATOM   3823  C  CB  . GLN B 2 129 ? 123.122 134.682 196.252 1.00 128.80 ? 129 GLN D CB  1 
ATOM   3824  C  CG  . GLN B 2 129 ? 122.715 135.057 197.674 1.00 128.80 ? 129 GLN D CG  1 
ATOM   3825  C  CD  . GLN B 2 129 ? 123.878 135.096 198.649 1.00 128.80 ? 129 GLN D CD  1 
ATOM   3826  O  OE1 . GLN B 2 129 ? 124.817 134.310 198.553 1.00 128.80 ? 129 GLN D OE1 1 
ATOM   3827  N  NE2 . GLN B 2 129 ? 123.818 136.026 199.595 1.00 128.80 ? 129 GLN D NE2 1 
ATOM   3828  N  N   . THR B 2 130 ? 123.411 132.855 193.523 1.00 128.86 ? 130 THR D N   1 
ATOM   3829  C  CA  . THR B 2 130 ? 122.865 132.674 192.186 1.00 128.86 ? 130 THR D CA  1 
ATOM   3830  C  C   . THR B 2 130 ? 123.913 132.053 191.277 1.00 128.86 ? 130 THR D C   1 
ATOM   3831  O  O   . THR B 2 130 ? 125.117 132.177 191.513 1.00 128.86 ? 130 THR D O   1 
ATOM   3832  C  CB  . THR B 2 130 ? 122.379 133.996 191.586 1.00 128.86 ? 130 THR D CB  1 
ATOM   3833  O  OG1 . THR B 2 130 ? 121.820 133.755 190.289 1.00 128.86 ? 130 THR D OG1 1 
ATOM   3834  C  CG2 . THR B 2 130 ? 123.525 134.983 191.461 1.00 128.86 ? 130 THR D CG2 1 
ATOM   3835  N  N   . ASP B 2 131 ? 123.429 131.377 190.238 1.00 130.35 ? 131 ASP D N   1 
ATOM   3836  C  CA  . ASP B 2 131 ? 124.261 130.916 189.138 1.00 130.35 ? 131 ASP D CA  1 
ATOM   3837  C  C   . ASP B 2 131 ? 124.220 131.843 187.931 1.00 130.35 ? 131 ASP D C   1 
ATOM   3838  O  O   . ASP B 2 131 ? 125.068 131.709 187.043 1.00 130.35 ? 131 ASP D O   1 
ATOM   3839  C  CB  . ASP B 2 131 ? 123.839 129.505 188.708 1.00 130.35 ? 131 ASP D CB  1 
ATOM   3840  C  CG  . ASP B 2 131 ? 123.277 128.690 189.855 1.00 130.35 ? 131 ASP D CG  1 
ATOM   3841  O  OD1 . ASP B 2 131 ? 124.037 128.377 190.795 1.00 130.35 ? 131 ASP D OD1 1 
ATOM   3842  O  OD2 . ASP B 2 131 ? 122.073 128.360 189.815 1.00 130.35 ? 131 ASP D OD2 1 
ATOM   3843  N  N   . MET B 2 132 ? 123.273 132.780 187.882 1.00 121.25 ? 132 MET D N   1 
ATOM   3844  C  CA  . MET B 2 132 ? 123.154 133.690 186.747 1.00 121.25 ? 132 MET D CA  1 
ATOM   3845  C  C   . MET B 2 132 ? 122.561 135.009 187.217 1.00 121.25 ? 132 MET D C   1 
ATOM   3846  O  O   . MET B 2 132 ? 121.419 135.042 187.685 1.00 121.25 ? 132 MET D O   1 
ATOM   3847  C  CB  . MET B 2 132 ? 122.267 133.076 185.659 1.00 121.25 ? 132 MET D CB  1 
ATOM   3848  C  CG  . MET B 2 132 ? 122.975 132.141 184.700 1.00 121.25 ? 132 MET D CG  1 
ATOM   3849  S  SD  . MET B 2 132 ? 123.414 132.942 183.152 1.00 121.25 ? 132 MET D SD  1 
ATOM   3850  C  CE  . MET B 2 132 ? 121.817 133.458 182.558 1.00 121.25 ? 132 MET D CE  1 
ATOM   3851  N  N   . ALA B 2 133 ? 123.330 136.087 187.094 1.00 113.92 ? 133 ALA D N   1 
ATOM   3852  C  CA  . ALA B 2 133 ? 122.860 137.437 187.373 1.00 113.92 ? 133 ALA D CA  1 
ATOM   3853  C  C   . ALA B 2 133 ? 122.646 138.185 186.064 1.00 113.92 ? 133 ALA D C   1 
ATOM   3854  O  O   . ALA B 2 133 ? 123.427 138.034 185.121 1.00 113.92 ? 133 ALA D O   1 
ATOM   3855  C  CB  . ALA B 2 133 ? 123.851 138.195 188.258 1.00 113.92 ? 133 ALA D CB  1 
ATOM   3856  N  N   . VAL B 2 134 ? 121.591 138.997 186.011 1.00 113.92 ? 134 VAL D N   1 
ATOM   3857  C  CA  . VAL B 2 134 ? 121.170 139.682 184.793 1.00 113.92 ? 134 VAL D CA  1 
ATOM   3858  C  C   . VAL B 2 134 ? 121.120 141.179 185.069 1.00 113.92 ? 134 VAL D C   1 
ATOM   3859  O  O   . VAL B 2 134 ? 120.601 141.607 186.106 1.00 113.92 ? 134 VAL D O   1 
ATOM   3860  C  CB  . VAL B 2 134 ? 119.803 139.176 184.294 1.00 113.92 ? 134 VAL D CB  1 
ATOM   3861  C  CG1 . VAL B 2 134 ? 119.511 139.724 182.908 1.00 113.92 ? 134 VAL D CG1 1 
ATOM   3862  C  CG2 . VAL B 2 134 ? 119.767 137.657 184.286 1.00 113.92 ? 134 VAL D CG2 1 
ATOM   3863  N  N   . ASN B 2 135 ? 121.661 141.972 184.141 1.00 113.92 ? 135 ASN D N   1 
ATOM   3864  C  CA  . ASN B 2 135 ? 121.579 143.430 184.231 1.00 113.92 ? 135 ASN D CA  1 
ATOM   3865  C  C   . ASN B 2 135 ? 121.617 143.977 182.807 1.00 113.92 ? 135 ASN D C   1 
ATOM   3866  O  O   . ASN B 2 135 ? 122.697 144.118 182.225 1.00 113.92 ? 135 ASN D O   1 
ATOM   3867  C  CB  . ASN B 2 135 ? 122.716 143.990 185.077 1.00 113.92 ? 135 ASN D CB  1 
ATOM   3868  C  CG  . ASN B 2 135 ? 122.804 145.513 185.028 1.00 113.92 ? 135 ASN D CG  1 
ATOM   3869  O  OD1 . ASN B 2 135 ? 121.910 146.192 184.522 1.00 113.92 ? 135 ASN D OD1 1 
ATOM   3870  N  ND2 . ASN B 2 135 ? 123.902 146.052 185.544 1.00 113.92 ? 135 ASN D ND2 1 
ATOM   3871  N  N   . TRP B 2 136 ? 120.443 144.278 182.253 1.00 113.92 ? 136 TRP D N   1 
ATOM   3872  C  CA  . TRP B 2 136 ? 120.372 144.824 180.904 1.00 113.92 ? 136 TRP D CA  1 
ATOM   3873  C  C   . TRP B 2 136 ? 120.731 146.302 180.840 1.00 113.92 ? 136 TRP D C   1 
ATOM   3874  O  O   . TRP B 2 136 ? 120.983 146.814 179.744 1.00 113.92 ? 136 TRP D O   1 
ATOM   3875  C  CB  . TRP B 2 136 ? 118.973 144.613 180.318 1.00 113.92 ? 136 TRP D CB  1 
ATOM   3876  C  CG  . TRP B 2 136 ? 118.593 143.172 180.198 1.00 113.92 ? 136 TRP D CG  1 
ATOM   3877  C  CD1 . TRP B 2 136 ? 117.520 142.557 180.772 1.00 113.92 ? 136 TRP D CD1 1 
ATOM   3878  C  CD2 . TRP B 2 136 ? 119.297 142.157 179.471 1.00 113.92 ? 136 TRP D CD2 1 
ATOM   3879  N  NE1 . TRP B 2 136 ? 117.506 141.224 180.439 1.00 113.92 ? 136 TRP D NE1 1 
ATOM   3880  C  CE2 . TRP B 2 136 ? 118.587 140.954 179.643 1.00 113.92 ? 136 TRP D CE2 1 
ATOM   3881  C  CE3 . TRP B 2 136 ? 120.455 142.151 178.688 1.00 113.92 ? 136 TRP D CE3 1 
ATOM   3882  C  CZ2 . TRP B 2 136 ? 118.997 139.758 179.062 1.00 113.92 ? 136 TRP D CZ2 1 
ATOM   3883  C  CZ3 . TRP B 2 136 ? 120.861 140.963 178.114 1.00 113.92 ? 136 TRP D CZ3 1 
ATOM   3884  C  CH2 . TRP B 2 136 ? 120.135 139.783 178.304 1.00 113.92 ? 136 TRP D CH2 1 
ATOM   3885  N  N   . ALA B 2 137 ? 120.765 146.996 181.979 1.00 113.92 ? 137 ALA D N   1 
ATOM   3886  C  CA  . ALA B 2 137 ? 121.117 148.409 181.996 1.00 113.92 ? 137 ALA D CA  1 
ATOM   3887  C  C   . ALA B 2 137 ? 122.621 148.641 181.947 1.00 113.92 ? 137 ALA D C   1 
ATOM   3888  O  O   . ALA B 2 137 ? 123.052 149.764 181.664 1.00 113.92 ? 137 ALA D O   1 
ATOM   3889  C  CB  . ALA B 2 137 ? 120.534 149.082 183.240 1.00 113.92 ? 137 ALA D CB  1 
ATOM   3890  N  N   . GLY B 2 138 ? 123.422 147.613 182.210 1.00 113.92 ? 138 GLY D N   1 
ATOM   3891  C  CA  . GLY B 2 138 ? 124.864 147.747 182.195 1.00 113.92 ? 138 GLY D CA  1 
ATOM   3892  C  C   . GLY B 2 138 ? 125.464 147.565 180.818 1.00 113.92 ? 138 GLY D C   1 
ATOM   3893  O  O   . GLY B 2 138 ? 124.994 148.162 179.845 1.00 113.92 ? 138 GLY D O   1 
ATOM   3894  N  N   . GLY B 2 139 ? 126.521 146.762 180.727 1.00 113.92 ? 139 GLY D N   1 
ATOM   3895  C  CA  . GLY B 2 139 ? 127.127 146.470 179.444 1.00 113.92 ? 139 GLY D CA  1 
ATOM   3896  C  C   . GLY B 2 139 ? 127.937 147.596 178.852 1.00 113.92 ? 139 GLY D C   1 
ATOM   3897  O  O   . GLY B 2 139 ? 128.194 147.594 177.646 1.00 113.92 ? 139 GLY D O   1 
ATOM   3898  N  N   . LEU B 2 140 ? 128.352 148.561 179.667 1.00 113.92 ? 140 LEU D N   1 
ATOM   3899  C  CA  . LEU B 2 140 ? 129.163 149.677 179.202 1.00 113.92 ? 140 LEU D CA  1 
ATOM   3900  C  C   . LEU B 2 140 ? 130.634 149.308 179.348 1.00 113.92 ? 140 LEU D C   1 
ATOM   3901  O  O   . LEU B 2 140 ? 131.114 149.088 180.465 1.00 113.92 ? 140 LEU D O   1 
ATOM   3902  C  CB  . LEU B 2 140 ? 128.838 150.946 179.987 1.00 113.92 ? 140 LEU D CB  1 
ATOM   3903  C  CG  . LEU B 2 140 ? 127.369 151.375 179.992 1.00 113.92 ? 140 LEU D CG  1 
ATOM   3904  C  CD1 . LEU B 2 140 ? 127.202 152.698 180.719 1.00 113.92 ? 140 LEU D CD1 1 
ATOM   3905  C  CD2 . LEU B 2 140 ? 126.832 151.469 178.573 1.00 113.92 ? 140 LEU D CD2 1 
ATOM   3906  N  N   . HIS B 2 141 ? 131.345 149.240 178.224 1.00 113.92 ? 141 HIS D N   1 
ATOM   3907  C  CA  . HIS B 2 141 ? 132.707 148.720 178.200 1.00 113.92 ? 141 HIS D CA  1 
ATOM   3908  C  C   . HIS B 2 141 ? 133.735 149.665 177.600 1.00 113.92 ? 141 HIS D C   1 
ATOM   3909  O  O   . HIS B 2 141 ? 134.933 149.450 177.818 1.00 113.92 ? 141 HIS D O   1 
ATOM   3910  C  CB  . HIS B 2 141 ? 132.761 147.385 177.438 1.00 113.92 ? 141 HIS D CB  1 
ATOM   3911  C  CG  . HIS B 2 141 ? 132.303 147.473 176.014 1.00 113.92 ? 141 HIS D CG  1 
ATOM   3912  N  ND1 . HIS B 2 141 ? 132.353 146.398 175.153 1.00 113.92 ? 141 HIS D ND1 1 
ATOM   3913  C  CD2 . HIS B 2 141 ? 131.779 148.499 175.302 1.00 113.92 ? 141 HIS D CD2 1 
ATOM   3914  C  CE1 . HIS B 2 141 ? 131.885 146.759 173.972 1.00 113.92 ? 141 HIS D CE1 1 
ATOM   3915  N  NE2 . HIS B 2 141 ? 131.530 148.029 174.036 1.00 113.92 ? 141 HIS D NE2 1 
ATOM   3916  N  N   . HIS B 2 142 ? 133.323 150.693 176.861 1.00 113.92 ? 142 HIS D N   1 
ATOM   3917  C  CA  . HIS B 2 142 ? 134.272 151.560 176.178 1.00 113.92 ? 142 HIS D CA  1 
ATOM   3918  C  C   . HIS B 2 142 ? 134.874 152.624 177.084 1.00 113.92 ? 142 HIS D C   1 
ATOM   3919  O  O   . HIS B 2 142 ? 135.874 153.238 176.701 1.00 113.92 ? 142 HIS D O   1 
ATOM   3920  C  CB  . HIS B 2 142 ? 133.592 152.237 174.988 1.00 113.92 ? 142 HIS D CB  1 
ATOM   3921  C  CG  . HIS B 2 142 ? 133.367 151.326 173.824 1.00 113.92 ? 142 HIS D CG  1 
ATOM   3922  N  ND1 . HIS B 2 142 ? 132.192 151.317 173.103 1.00 113.92 ? 142 HIS D ND1 1 
ATOM   3923  C  CD2 . HIS B 2 142 ? 134.165 150.394 173.254 1.00 113.92 ? 142 HIS D CD2 1 
ATOM   3924  C  CE1 . HIS B 2 142 ? 132.277 150.418 172.139 1.00 113.92 ? 142 HIS D CE1 1 
ATOM   3925  N  NE2 . HIS B 2 142 ? 133.464 149.844 172.208 1.00 113.92 ? 142 HIS D NE2 1 
ATOM   3926  N  N   . ALA B 2 143 ? 134.304 152.851 178.266 1.00 113.92 ? 143 ALA D N   1 
ATOM   3927  C  CA  . ALA B 2 143 ? 134.828 153.875 179.159 1.00 113.92 ? 143 ALA D CA  1 
ATOM   3928  C  C   . ALA B 2 143 ? 136.260 153.558 179.569 1.00 113.92 ? 143 ALA D C   1 
ATOM   3929  O  O   . ALA B 2 143 ? 136.616 152.400 179.806 1.00 113.92 ? 143 ALA D O   1 
ATOM   3930  C  CB  . ALA B 2 143 ? 133.941 153.999 180.398 1.00 113.92 ? 143 ALA D CB  1 
ATOM   3931  N  N   . LYS B 2 144 ? 137.081 154.599 179.653 1.00 113.92 ? 144 LYS D N   1 
ATOM   3932  C  CA  . LYS B 2 144 ? 138.479 154.469 180.025 1.00 113.92 ? 144 LYS D CA  1 
ATOM   3933  C  C   . LYS B 2 144 ? 138.653 154.821 181.499 1.00 113.92 ? 144 LYS D C   1 
ATOM   3934  O  O   . LYS B 2 144 ? 137.696 155.156 182.201 1.00 113.92 ? 144 LYS D O   1 
ATOM   3935  C  CB  . LYS B 2 144 ? 139.354 155.352 179.134 1.00 103.02 ? 144 LYS D CB  1 
ATOM   3936  C  CG  . LYS B 2 144 ? 139.105 155.164 177.649 1.00 103.02 ? 144 LYS D CG  1 
ATOM   3937  C  CD  . LYS B 2 144 ? 139.618 153.817 177.175 1.00 103.02 ? 144 LYS D CD  1 
ATOM   3938  C  CE  . LYS B 2 144 ? 139.385 153.635 175.685 1.00 103.02 ? 144 LYS D CE  1 
ATOM   3939  N  NZ  . LYS B 2 144 ? 139.870 154.806 174.904 1.00 103.02 ? 144 LYS D NZ  1 
ATOM   3940  N  N   . LYS B 2 145 ? 139.898 154.740 181.974 1.00 113.92 ? 145 LYS D N   1 
ATOM   3941  C  CA  . LYS B 2 145 ? 140.170 155.008 183.383 1.00 113.92 ? 145 LYS D CA  1 
ATOM   3942  C  C   . LYS B 2 145 ? 139.814 156.444 183.746 1.00 113.92 ? 145 LYS D C   1 
ATOM   3943  O  O   . LYS B 2 145 ? 139.170 156.697 184.770 1.00 113.92 ? 145 LYS D O   1 
ATOM   3944  C  CB  . LYS B 2 145 ? 141.640 154.721 183.695 1.00 105.22 ? 145 LYS D CB  1 
ATOM   3945  C  CG  . LYS B 2 145 ? 142.027 154.974 185.143 1.00 105.22 ? 145 LYS D CG  1 
ATOM   3946  C  CD  . LYS B 2 145 ? 143.523 154.808 185.351 1.00 105.22 ? 145 LYS D CD  1 
ATOM   3947  C  CE  . LYS B 2 145 ? 143.865 153.408 185.829 1.00 105.22 ? 145 LYS D CE  1 
ATOM   3948  N  NZ  . LYS B 2 145 ? 143.325 153.138 187.189 1.00 105.22 ? 145 LYS D NZ  1 
ATOM   3949  N  N   . SER B 2 146 ? 140.222 157.397 182.914 1.00 113.92 ? 146 SER D N   1 
ATOM   3950  C  CA  . SER B 2 146 ? 139.998 158.814 183.180 1.00 113.92 ? 146 SER D CA  1 
ATOM   3951  C  C   . SER B 2 146 ? 139.526 159.515 181.910 1.00 113.92 ? 146 SER D C   1 
ATOM   3952  O  O   . SER B 2 146 ? 139.995 160.599 181.560 1.00 113.92 ? 146 SER D O   1 
ATOM   3953  C  CB  . SER B 2 146 ? 141.259 159.468 183.741 1.00 104.75 ? 146 SER D CB  1 
ATOM   3954  O  OG  . SER B 2 146 ? 142.324 159.405 182.810 1.00 104.75 ? 146 SER D OG  1 
ATOM   3955  N  N   . GLU B 2 147 ? 138.584 158.894 181.204 1.00 113.92 ? 147 GLU D N   1 
ATOM   3956  C  CA  . GLU B 2 147 ? 138.059 159.455 179.967 1.00 113.92 ? 147 GLU D CA  1 
ATOM   3957  C  C   . GLU B 2 147 ? 136.782 158.716 179.593 1.00 113.92 ? 147 GLU D C   1 
ATOM   3958  O  O   . GLU B 2 147 ? 136.646 157.518 179.856 1.00 113.92 ? 147 GLU D O   1 
ATOM   3959  C  CB  . GLU B 2 147 ? 139.088 159.352 178.831 1.00 113.10 ? 147 GLU D CB  1 
ATOM   3960  C  CG  . GLU B 2 147 ? 138.590 159.827 177.478 1.00 113.10 ? 147 GLU D CG  1 
ATOM   3961  C  CD  . GLU B 2 147 ? 139.537 159.467 176.353 1.00 113.10 ? 147 GLU D CD  1 
ATOM   3962  O  OE1 . GLU B 2 147 ? 140.759 159.655 176.520 1.00 113.10 ? 147 GLU D OE1 1 
ATOM   3963  O  OE2 . GLU B 2 147 ? 139.057 158.995 175.300 1.00 113.10 ? 147 GLU D OE2 1 
ATOM   3964  N  N   . ALA B 2 148 ? 135.853 159.444 178.981 1.00 113.92 ? 148 ALA D N   1 
ATOM   3965  C  CA  . ALA B 2 148 ? 134.637 158.859 178.432 1.00 113.92 ? 148 ALA D CA  1 
ATOM   3966  C  C   . ALA B 2 148 ? 134.841 158.552 176.954 1.00 113.92 ? 148 ALA D C   1 
ATOM   3967  O  O   . ALA B 2 148 ? 135.136 159.454 176.163 1.00 113.92 ? 148 ALA D O   1 
ATOM   3968  C  CB  . ALA B 2 148 ? 133.445 159.793 178.622 1.00 113.92 ? 148 ALA D CB  1 
ATOM   3969  N  N   . SER B 2 149 ? 134.688 157.286 176.585 1.00 117.52 ? 149 SER D N   1 
ATOM   3970  C  CA  . SER B 2 149 ? 134.848 156.849 175.208 1.00 117.52 ? 149 SER D CA  1 
ATOM   3971  C  C   . SER B 2 149 ? 133.554 156.196 174.745 1.00 117.52 ? 149 SER D C   1 
ATOM   3972  O  O   . SER B 2 149 ? 132.851 155.552 175.529 1.00 117.52 ? 149 SER D O   1 
ATOM   3973  C  CB  . SER B 2 149 ? 136.017 155.872 175.054 1.00 117.52 ? 149 SER D CB  1 
ATOM   3974  N  N   . GLY B 2 150 ? 133.248 156.365 173.464 1.00 121.58 ? 150 GLY D N   1 
ATOM   3975  C  CA  . GLY B 2 150 ? 132.003 155.824 172.944 1.00 121.58 ? 150 GLY D CA  1 
ATOM   3976  C  C   . GLY B 2 150 ? 130.812 156.488 173.603 1.00 121.58 ? 150 GLY D C   1 
ATOM   3977  O  O   . GLY B 2 150 ? 130.677 157.716 173.601 1.00 121.58 ? 150 GLY D O   1 
ATOM   3978  N  N   . PHE B 2 151 ? 129.934 155.674 174.181 1.00 113.92 ? 151 PHE D N   1 
ATOM   3979  C  CA  . PHE B 2 151 ? 128.754 156.151 174.889 1.00 113.92 ? 151 PHE D CA  1 
ATOM   3980  C  C   . PHE B 2 151 ? 128.792 155.733 176.354 1.00 113.92 ? 151 PHE D C   1 
ATOM   3981  O  O   . PHE B 2 151 ? 127.761 155.437 176.961 1.00 113.92 ? 151 PHE D O   1 
ATOM   3982  C  CB  . PHE B 2 151 ? 127.473 155.642 174.229 1.00 113.92 ? 151 PHE D CB  1 
ATOM   3983  C  CG  . PHE B 2 151 ? 127.386 155.924 172.753 1.00 113.92 ? 151 PHE D CG  1 
ATOM   3984  C  CD1 . PHE B 2 151 ? 127.957 157.061 172.208 1.00 113.92 ? 151 PHE D CD1 1 
ATOM   3985  C  CD2 . PHE B 2 151 ? 126.736 155.041 171.908 1.00 113.92 ? 151 PHE D CD2 1 
ATOM   3986  C  CE1 . PHE B 2 151 ? 127.877 157.313 170.852 1.00 113.92 ? 151 PHE D CE1 1 
ATOM   3987  C  CE2 . PHE B 2 151 ? 126.654 155.288 170.552 1.00 113.92 ? 151 PHE D CE2 1 
ATOM   3988  C  CZ  . PHE B 2 151 ? 127.225 156.426 170.024 1.00 113.92 ? 151 PHE D CZ  1 
ATOM   3989  N  N   . CYS B 2 152 ? 129.986 155.705 176.943 1.00 117.59 ? 152 CYS D N   1 
ATOM   3990  C  CA  . CYS B 2 152 ? 130.171 155.179 178.286 1.00 117.59 ? 152 CYS D CA  1 
ATOM   3991  C  C   . CYS B 2 152 ? 130.967 156.164 179.129 1.00 117.59 ? 152 CYS D C   1 
ATOM   3992  O  O   . CYS B 2 152 ? 131.862 156.853 178.633 1.00 117.59 ? 152 CYS D O   1 
ATOM   3993  C  CB  . CYS B 2 152 ? 130.888 153.822 178.261 1.00 117.59 ? 152 CYS D CB  1 
ATOM   3994  S  SG  . CYS B 2 152 ? 130.199 152.632 177.087 1.00 117.59 ? 152 CYS D SG  1 
ATOM   3995  N  N   . TYR B 2 153 ? 130.624 156.220 180.414 1.00 123.00 ? 153 TYR D N   1 
ATOM   3996  C  CA  . TYR B 2 153 ? 131.288 157.084 181.381 1.00 123.00 ? 153 TYR D CA  1 
ATOM   3997  C  C   . TYR B 2 153 ? 131.957 156.296 182.492 1.00 123.00 ? 153 TYR D C   1 
ATOM   3998  O  O   . TYR B 2 153 ? 133.154 156.474 182.745 1.00 123.00 ? 153 TYR D O   1 
ATOM   3999  C  CB  . TYR B 2 153 ? 130.286 158.081 181.989 1.00 123.00 ? 153 TYR D CB  1 
ATOM   4000  C  CG  . TYR B 2 153 ? 129.309 158.662 180.997 1.00 123.00 ? 153 TYR D CG  1 
ATOM   4001  C  CD1 . TYR B 2 153 ? 128.165 157.966 180.626 1.00 123.00 ? 153 TYR D CD1 1 
ATOM   4002  C  CD2 . TYR B 2 153 ? 129.531 159.908 180.432 1.00 123.00 ? 153 TYR D CD2 1 
ATOM   4003  C  CE1 . TYR B 2 153 ? 127.276 158.493 179.716 1.00 123.00 ? 153 TYR D CE1 1 
ATOM   4004  C  CE2 . TYR B 2 153 ? 128.646 160.444 179.526 1.00 123.00 ? 153 TYR D CE2 1 
ATOM   4005  C  CZ  . TYR B 2 153 ? 127.518 159.736 179.174 1.00 123.00 ? 153 TYR D CZ  1 
ATOM   4006  O  OH  . TYR B 2 153 ? 126.635 160.273 178.266 1.00 123.00 ? 153 TYR D OH  1 
ATOM   4007  N  N   . VAL B 2 154 ? 131.210 155.427 183.165 1.00 113.64 ? 154 VAL D N   1 
ATOM   4008  C  CA  . VAL B 2 154 ? 131.736 154.549 184.201 1.00 113.64 ? 154 VAL D CA  1 
ATOM   4009  C  C   . VAL B 2 154 ? 131.674 153.124 183.679 1.00 113.64 ? 154 VAL D C   1 
ATOM   4010  O  O   . VAL B 2 154 ? 130.618 152.667 183.224 1.00 113.64 ? 154 VAL D O   1 
ATOM   4011  C  CB  . VAL B 2 154 ? 130.948 154.689 185.515 1.00 113.64 ? 154 VAL D CB  1 
ATOM   4012  C  CG1 . VAL B 2 154 ? 131.780 154.197 186.688 1.00 113.64 ? 154 VAL D CG1 1 
ATOM   4013  C  CG2 . VAL B 2 154 ? 130.520 156.132 185.725 1.00 113.64 ? 154 VAL D CG2 1 
ATOM   4014  N  N   . ASN B 2 155 ? 132.802 152.423 183.741 1.00 113.92 ? 155 ASN D N   1 
ATOM   4015  C  CA  . ASN B 2 155 ? 132.904 151.088 183.161 1.00 113.92 ? 155 ASN D CA  1 
ATOM   4016  C  C   . ASN B 2 155 ? 132.367 150.099 184.184 1.00 113.92 ? 155 ASN D C   1 
ATOM   4017  O  O   . ASN B 2 155 ? 133.092 149.644 185.070 1.00 113.92 ? 155 ASN D O   1 
ATOM   4018  C  CB  . ASN B 2 155 ? 134.345 150.776 182.778 1.00 110.05 ? 155 ASN D CB  1 
ATOM   4019  C  CG  . ASN B 2 155 ? 134.444 149.792 181.631 1.00 110.05 ? 155 ASN D CG  1 
ATOM   4020  O  OD1 . ASN B 2 155 ? 133.644 148.864 181.524 1.00 110.05 ? 155 ASN D OD1 1 
ATOM   4021  N  ND2 . ASN B 2 155 ? 135.430 149.989 180.765 1.00 110.05 ? 155 ASN D ND2 1 
ATOM   4022  N  N   . ASP B 2 156 ? 131.085 149.756 184.050 1.00 123.25 ? 156 ASP D N   1 
ATOM   4023  C  CA  . ASP B 2 156 ? 130.467 148.814 184.975 1.00 123.25 ? 156 ASP D CA  1 
ATOM   4024  C  C   . ASP B 2 156 ? 131.082 147.425 184.870 1.00 123.25 ? 156 ASP D C   1 
ATOM   4025  O  O   . ASP B 2 156 ? 131.170 146.711 185.877 1.00 123.25 ? 156 ASP D O   1 
ATOM   4026  C  CB  . ASP B 2 156 ? 128.959 148.772 184.720 1.00 123.25 ? 156 ASP D CB  1 
ATOM   4027  C  CG  . ASP B 2 156 ? 128.574 147.772 183.645 1.00 123.25 ? 156 ASP D CG  1 
ATOM   4028  O  OD1 . ASP B 2 156 ? 129.206 147.788 182.569 1.00 123.25 ? 156 ASP D OD1 1 
ATOM   4029  O  OD2 . ASP B 2 156 ? 127.636 146.979 183.865 1.00 123.25 ? 156 ASP D OD2 1 
ATOM   4030  N  N   . ILE B 2 157 ? 131.532 147.035 183.676 1.00 113.92 ? 157 ILE D N   1 
ATOM   4031  C  CA  . ILE B 2 157 ? 132.127 145.714 183.501 1.00 113.92 ? 157 ILE D CA  1 
ATOM   4032  C  C   . ILE B 2 157 ? 133.412 145.599 184.307 1.00 113.92 ? 157 ILE D C   1 
ATOM   4033  O  O   . ILE B 2 157 ? 133.651 144.595 184.987 1.00 113.92 ? 157 ILE D O   1 
ATOM   4034  C  CB  . ILE B 2 157 ? 132.382 145.428 182.012 1.00 113.92 ? 157 ILE D CB  1 
ATOM   4035  C  CG1 . ILE B 2 157 ? 131.118 145.672 181.196 1.00 113.92 ? 157 ILE D CG1 1 
ATOM   4036  C  CG2 . ILE B 2 157 ? 132.845 143.998 181.837 1.00 113.92 ? 157 ILE D CG2 1 
ATOM   4037  C  CD1 . ILE B 2 157 ? 131.244 145.225 179.773 1.00 113.92 ? 157 ILE D CD1 1 
ATOM   4038  N  N   . VAL B 2 158 ? 134.271 146.616 184.223 1.00 113.92 ? 158 VAL D N   1 
ATOM   4039  C  CA  . VAL B 2 158 ? 135.550 146.563 184.922 1.00 113.92 ? 158 VAL D CA  1 
ATOM   4040  C  C   . VAL B 2 158 ? 135.341 146.583 186.431 1.00 113.92 ? 158 VAL D C   1 
ATOM   4041  O  O   . VAL B 2 158 ? 136.009 145.850 187.170 1.00 113.92 ? 158 VAL D O   1 
ATOM   4042  C  CB  . VAL B 2 158 ? 136.457 147.714 184.452 1.00 113.92 ? 158 VAL D CB  1 
ATOM   4043  C  CG1 . VAL B 2 158 ? 137.768 147.705 185.213 1.00 113.92 ? 158 VAL D CG1 1 
ATOM   4044  C  CG2 . VAL B 2 158 ? 136.713 147.603 182.960 1.00 113.92 ? 158 VAL D CG2 1 
ATOM   4045  N  N   . LEU B 2 159 ? 134.405 147.404 186.913 1.00 113.92 ? 159 LEU D N   1 
ATOM   4046  C  CA  . LEU B 2 159 ? 134.102 147.407 188.341 1.00 113.92 ? 159 LEU D CA  1 
ATOM   4047  C  C   . LEU B 2 159 ? 133.592 146.047 188.796 1.00 113.92 ? 159 LEU D C   1 
ATOM   4048  O  O   . LEU B 2 159 ? 133.998 145.545 189.851 1.00 113.92 ? 159 LEU D O   1 
ATOM   4049  C  CB  . LEU B 2 159 ? 133.089 148.503 188.672 1.00 113.92 ? 159 LEU D CB  1 
ATOM   4050  C  CG  . LEU B 2 159 ? 133.646 149.884 189.032 1.00 113.92 ? 159 LEU D CG  1 
ATOM   4051  C  CD1 . LEU B 2 159 ? 134.225 150.597 187.823 1.00 113.92 ? 159 LEU D CD1 1 
ATOM   4052  C  CD2 . LEU B 2 159 ? 132.571 150.736 189.694 1.00 113.92 ? 159 LEU D CD2 1 
ATOM   4053  N  N   . ALA B 2 160 ? 132.711 145.429 188.007 1.00 114.52 ? 160 ALA D N   1 
ATOM   4054  C  CA  . ALA B 2 160 ? 132.196 144.115 188.374 1.00 114.52 ? 160 ALA D CA  1 
ATOM   4055  C  C   . ALA B 2 160 ? 133.299 143.065 188.375 1.00 114.52 ? 160 ALA D C   1 
ATOM   4056  O  O   . ALA B 2 160 ? 133.341 142.202 189.258 1.00 114.52 ? 160 ALA D O   1 
ATOM   4057  C  CB  . ALA B 2 160 ? 131.069 143.709 187.425 1.00 114.52 ? 160 ALA D CB  1 
ATOM   4058  N  N   . ILE B 2 161 ? 134.199 143.113 187.391 1.00 113.92 ? 161 ILE D N   1 
ATOM   4059  C  CA  . ILE B 2 161 ? 135.297 142.149 187.345 1.00 113.92 ? 161 ILE D CA  1 
ATOM   4060  C  C   . ILE B 2 161 ? 136.216 142.316 188.552 1.00 113.92 ? 161 ILE D C   1 
ATOM   4061  O  O   . ILE B 2 161 ? 136.611 141.331 189.187 1.00 113.92 ? 161 ILE D O   1 
ATOM   4062  C  CB  . ILE B 2 161 ? 136.067 142.265 186.018 1.00 113.92 ? 161 ILE D CB  1 
ATOM   4063  C  CG1 . ILE B 2 161 ? 135.187 141.793 184.862 1.00 113.92 ? 161 ILE D CG1 1 
ATOM   4064  C  CG2 . ILE B 2 161 ? 137.316 141.409 186.064 1.00 113.92 ? 161 ILE D CG2 1 
ATOM   4065  C  CD1 . ILE B 2 161 ? 135.850 141.884 183.510 1.00 113.92 ? 161 ILE D CD1 1 
ATOM   4066  N  N   . LEU B 2 162 ? 136.572 143.562 188.888 1.00 113.92 ? 162 LEU D N   1 
ATOM   4067  C  CA  . LEU B 2 162 ? 137.384 143.790 190.085 1.00 113.92 ? 162 LEU D CA  1 
ATOM   4068  C  C   . LEU B 2 162 ? 136.681 143.284 191.335 1.00 113.92 ? 162 LEU D C   1 
ATOM   4069  O  O   . LEU B 2 162 ? 137.310 142.665 192.202 1.00 113.92 ? 162 LEU D O   1 
ATOM   4070  C  CB  . LEU B 2 162 ? 137.734 145.271 190.246 1.00 113.92 ? 162 LEU D CB  1 
ATOM   4071  C  CG  . LEU B 2 162 ? 139.013 145.826 189.610 1.00 113.92 ? 162 LEU D CG  1 
ATOM   4072  C  CD1 . LEU B 2 162 ? 138.923 145.924 188.110 1.00 113.92 ? 162 LEU D CD1 1 
ATOM   4073  C  CD2 . LEU B 2 162 ? 139.354 147.181 190.217 1.00 113.92 ? 162 LEU D CD2 1 
ATOM   4074  N  N   . GLU B 2 163 ? 135.379 143.542 191.450 1.00 118.93 ? 163 GLU D N   1 
ATOM   4075  C  CA  . GLU B 2 163 ? 134.621 143.062 192.596 1.00 118.93 ? 163 GLU D CA  1 
ATOM   4076  C  C   . GLU B 2 163 ? 134.530 141.542 192.614 1.00 118.93 ? 163 GLU D C   1 
ATOM   4077  O  O   . GLU B 2 163 ? 134.350 140.950 193.683 1.00 118.93 ? 163 GLU D O   1 
ATOM   4078  C  CB  . GLU B 2 163 ? 133.234 143.703 192.575 1.00 118.93 ? 163 GLU D CB  1 
ATOM   4079  C  CG  . GLU B 2 163 ? 132.378 143.459 193.794 1.00 118.93 ? 163 GLU D CG  1 
ATOM   4080  C  CD  . GLU B 2 163 ? 131.471 144.639 194.073 1.00 118.93 ? 163 GLU D CD  1 
ATOM   4081  O  OE1 . GLU B 2 163 ? 131.934 145.789 193.922 1.00 118.93 ? 163 GLU D OE1 1 
ATOM   4082  O  OE2 . GLU B 2 163 ? 130.298 144.426 194.428 1.00 118.93 ? 163 GLU D OE2 1 
ATOM   4083  N  N   . LEU B 2 164 ? 134.656 140.904 191.449 1.00 113.92 ? 164 LEU D N   1 
ATOM   4084  C  CA  . LEU B 2 164 ? 134.631 139.449 191.363 1.00 113.92 ? 164 LEU D CA  1 
ATOM   4085  C  C   . LEU B 2 164 ? 135.975 138.841 191.749 1.00 113.92 ? 164 LEU D C   1 
ATOM   4086  O  O   . LEU B 2 164 ? 136.017 137.763 192.352 1.00 113.92 ? 164 LEU D O   1 
ATOM   4087  C  CB  . LEU B 2 164 ? 134.233 139.012 189.955 1.00 113.92 ? 164 LEU D CB  1 
ATOM   4088  C  CG  . LEU B 2 164 ? 132.758 138.645 189.805 1.00 113.92 ? 164 LEU D CG  1 
ATOM   4089  C  CD1 . LEU B 2 164 ? 132.409 138.374 188.354 1.00 113.92 ? 164 LEU D CD1 1 
ATOM   4090  C  CD2 . LEU B 2 164 ? 132.437 137.446 190.672 1.00 113.92 ? 164 LEU D CD2 1 
ATOM   4091  N  N   . LEU B 2 165 ? 137.080 139.509 191.399 1.00 113.92 ? 165 LEU D N   1 
ATOM   4092  C  CA  . LEU B 2 165 ? 138.403 138.949 191.663 1.00 113.92 ? 165 LEU D CA  1 
ATOM   4093  C  C   . LEU B 2 165 ? 138.647 138.728 193.147 1.00 113.92 ? 165 LEU D C   1 
ATOM   4094  O  O   . LEU B 2 165 ? 139.545 137.962 193.510 1.00 113.92 ? 165 LEU D O   1 
ATOM   4095  C  CB  . LEU B 2 165 ? 139.501 139.861 191.108 1.00 113.92 ? 165 LEU D CB  1 
ATOM   4096  C  CG  . LEU B 2 165 ? 139.488 140.219 189.624 1.00 113.92 ? 165 LEU D CG  1 
ATOM   4097  C  CD1 . LEU B 2 165 ? 140.871 140.654 189.170 1.00 113.92 ? 165 LEU D CD1 1 
ATOM   4098  C  CD2 . LEU B 2 165 ? 139.007 139.039 188.813 1.00 113.92 ? 165 LEU D CD2 1 
ATOM   4099  N  N   . LYS B 2 166 ? 137.877 139.392 194.009 1.00 128.08 ? 166 LYS D N   1 
ATOM   4100  C  CA  . LYS B 2 166 ? 138.051 139.215 195.444 1.00 128.08 ? 166 LYS D CA  1 
ATOM   4101  C  C   . LYS B 2 166 ? 137.715 137.789 195.861 1.00 128.08 ? 166 LYS D C   1 
ATOM   4102  O  O   . LYS B 2 166 ? 138.355 137.227 196.758 1.00 128.08 ? 166 LYS D O   1 
ATOM   4103  C  CB  . LYS B 2 166 ? 137.179 140.219 196.196 1.00 128.08 ? 166 LYS D CB  1 
ATOM   4104  C  CG  . LYS B 2 166 ? 137.179 141.606 195.576 1.00 128.08 ? 166 LYS D CG  1 
ATOM   4105  C  CD  . LYS B 2 166 ? 136.746 142.664 196.574 1.00 128.08 ? 166 LYS D CD  1 
ATOM   4106  C  CE  . LYS B 2 166 ? 135.320 142.426 197.039 1.00 128.08 ? 166 LYS D CE  1 
ATOM   4107  N  NZ  . LYS B 2 166 ? 134.827 143.535 197.901 1.00 128.08 ? 166 LYS D NZ  1 
ATOM   4108  N  N   . TYR B 2 167 ? 136.716 137.186 195.216 1.00 127.22 ? 167 TYR D N   1 
ATOM   4109  C  CA  . TYR B 2 167 ? 136.257 135.850 195.568 1.00 127.22 ? 167 TYR D CA  1 
ATOM   4110  C  C   . TYR B 2 167 ? 136.769 134.764 194.628 1.00 127.22 ? 167 TYR D C   1 
ATOM   4111  O  O   . TYR B 2 167 ? 136.674 133.581 194.971 1.00 127.22 ? 167 TYR D O   1 
ATOM   4112  C  CB  . TYR B 2 167 ? 134.722 135.809 195.591 1.00 127.22 ? 167 TYR D CB  1 
ATOM   4113  C  CG  . TYR B 2 167 ? 134.088 136.435 196.817 1.00 127.22 ? 167 TYR D CG  1 
ATOM   4114  C  CD1 . TYR B 2 167 ? 134.528 137.657 197.310 1.00 127.22 ? 167 TYR D CD1 1 
ATOM   4115  C  CD2 . TYR B 2 167 ? 133.041 135.804 197.477 1.00 127.22 ? 167 TYR D CD2 1 
ATOM   4116  C  CE1 . TYR B 2 167 ? 133.949 138.231 198.425 1.00 127.22 ? 167 TYR D CE1 1 
ATOM   4117  C  CE2 . TYR B 2 167 ? 132.455 136.371 198.594 1.00 127.22 ? 167 TYR D CE2 1 
ATOM   4118  C  CZ  . TYR B 2 167 ? 132.913 137.584 199.063 1.00 127.22 ? 167 TYR D CZ  1 
ATOM   4119  O  OH  . TYR B 2 167 ? 132.332 138.152 200.174 1.00 127.22 ? 167 TYR D OH  1 
ATOM   4120  N  N   . HIS B 2 168 ? 137.303 135.126 193.461 1.00 117.88 ? 168 HIS D N   1 
ATOM   4121  C  CA  . HIS B 2 168 ? 137.741 134.152 192.472 1.00 117.88 ? 168 HIS D CA  1 
ATOM   4122  C  C   . HIS B 2 168 ? 139.159 134.462 192.014 1.00 117.88 ? 168 HIS D C   1 
ATOM   4123  O  O   . HIS B 2 168 ? 139.577 135.622 191.971 1.00 117.88 ? 168 HIS D O   1 
ATOM   4124  C  CB  . HIS B 2 168 ? 136.799 134.118 191.262 1.00 117.88 ? 168 HIS D CB  1 
ATOM   4125  C  CG  . HIS B 2 168 ? 135.365 133.886 191.622 1.00 117.88 ? 168 HIS D CG  1 
ATOM   4126  N  ND1 . HIS B 2 168 ? 134.868 132.639 191.934 1.00 117.88 ? 168 HIS D ND1 1 
ATOM   4127  C  CD2 . HIS B 2 168 ? 134.321 134.742 191.723 1.00 117.88 ? 168 HIS D CD2 1 
ATOM   4128  C  CE1 . HIS B 2 168 ? 133.580 132.736 192.209 1.00 117.88 ? 168 HIS D CE1 1 
ATOM   4129  N  NE2 . HIS B 2 168 ? 133.223 134.002 192.088 1.00 117.88 ? 168 HIS D NE2 1 
ATOM   4130  N  N   . GLN B 2 169 ? 139.896 133.405 191.668 1.00 123.28 ? 169 GLN D N   1 
ATOM   4131  C  CA  . GLN B 2 169 ? 141.273 133.554 191.206 1.00 123.28 ? 169 GLN D CA  1 
ATOM   4132  C  C   . GLN B 2 169 ? 141.342 133.946 189.732 1.00 123.28 ? 169 GLN D C   1 
ATOM   4133  O  O   . GLN B 2 169 ? 141.900 134.991 189.381 1.00 123.28 ? 169 GLN D O   1 
ATOM   4134  C  CB  . GLN B 2 169 ? 142.047 132.255 191.452 1.00 123.28 ? 169 GLN D CB  1 
ATOM   4135  C  CG  . GLN B 2 169 ? 143.458 132.245 190.883 1.00 123.28 ? 169 GLN D CG  1 
ATOM   4136  C  CD  . GLN B 2 169 ? 144.283 133.440 191.321 1.00 123.28 ? 169 GLN D CD  1 
ATOM   4137  O  OE1 . GLN B 2 169 ? 144.197 133.884 192.467 1.00 123.28 ? 169 GLN D OE1 1 
ATOM   4138  N  NE2 . GLN B 2 169 ? 145.090 133.967 190.408 1.00 123.28 ? 169 GLN D NE2 1 
ATOM   4139  N  N   . ARG B 2 170 ? 140.780 133.115 188.859 1.00 114.04 ? 170 ARG D N   1 
ATOM   4140  C  CA  . ARG B 2 170 ? 140.792 133.337 187.418 1.00 114.04 ? 170 ARG D CA  1 
ATOM   4141  C  C   . ARG B 2 170 ? 139.394 133.705 186.943 1.00 114.04 ? 170 ARG D C   1 
ATOM   4142  O  O   . ARG B 2 170 ? 138.420 133.030 187.291 1.00 114.04 ? 170 ARG D O   1 
ATOM   4143  C  CB  . ARG B 2 170 ? 141.300 132.093 186.689 1.00 114.04 ? 170 ARG D CB  1 
ATOM   4144  C  CG  . ARG B 2 170 ? 142.763 131.784 186.967 1.00 114.04 ? 170 ARG D CG  1 
ATOM   4145  C  CD  . ARG B 2 170 ? 143.203 130.499 186.289 1.00 114.04 ? 170 ARG D CD  1 
ATOM   4146  N  NE  . ARG B 2 170 ? 142.460 129.341 186.771 1.00 114.04 ? 170 ARG D NE  1 
ATOM   4147  C  CZ  . ARG B 2 170 ? 142.762 128.661 187.868 1.00 114.04 ? 170 ARG D CZ  1 
ATOM   4148  N  NH1 . ARG B 2 170 ? 143.791 128.997 188.629 1.00 114.04 ? 170 ARG D NH1 1 
ATOM   4149  N  NH2 . ARG B 2 170 ? 142.012 127.617 188.211 1.00 114.04 ? 170 ARG D NH2 1 
ATOM   4150  N  N   . VAL B 2 171 ? 139.296 134.772 186.150 1.00 113.92 ? 171 VAL D N   1 
ATOM   4151  C  CA  . VAL B 2 171 ? 138.015 135.259 185.648 1.00 113.92 ? 171 VAL D CA  1 
ATOM   4152  C  C   . VAL B 2 171 ? 138.076 135.429 184.134 1.00 113.92 ? 171 VAL D C   1 
ATOM   4153  O  O   . VAL B 2 171 ? 138.939 136.152 183.611 1.00 113.92 ? 171 VAL D O   1 
ATOM   4154  C  CB  . VAL B 2 171 ? 137.596 136.575 186.322 1.00 113.92 ? 171 VAL D CB  1 
ATOM   4155  C  CG1 . VAL B 2 171 ? 136.560 137.299 185.477 1.00 113.92 ? 171 VAL D CG1 1 
ATOM   4156  C  CG2 . VAL B 2 171 ? 137.035 136.291 187.705 1.00 113.92 ? 171 VAL D CG2 1 
ATOM   4157  N  N   . LEU B 2 172 ? 137.208 134.705 183.434 1.00 113.92 ? 172 LEU D N   1 
ATOM   4158  C  CA  . LEU B 2 172 ? 137.066 134.823 181.992 1.00 113.92 ? 172 LEU D CA  1 
ATOM   4159  C  C   . LEU B 2 172 ? 135.982 135.847 181.677 1.00 113.92 ? 172 LEU D C   1 
ATOM   4160  O  O   . LEU B 2 172 ? 134.881 135.786 182.235 1.00 113.92 ? 172 LEU D O   1 
ATOM   4161  C  CB  . LEU B 2 172 ? 136.711 133.469 181.376 1.00 113.92 ? 172 LEU D CB  1 
ATOM   4162  C  CG  . LEU B 2 172 ? 136.172 133.486 179.946 1.00 113.92 ? 172 LEU D CG  1 
ATOM   4163  C  CD1 . LEU B 2 172 ? 137.204 134.065 179.001 1.00 113.92 ? 172 LEU D CD1 1 
ATOM   4164  C  CD2 . LEU B 2 172 ? 135.761 132.091 179.508 1.00 113.92 ? 172 LEU D CD2 1 
ATOM   4165  N  N   . TYR B 2 173 ? 136.295 136.786 180.793 1.00 113.92 ? 173 TYR D N   1 
ATOM   4166  C  CA  . TYR B 2 173 ? 135.350 137.796 180.334 1.00 113.92 ? 173 TYR D CA  1 
ATOM   4167  C  C   . TYR B 2 173 ? 135.098 137.574 178.849 1.00 113.92 ? 173 TYR D C   1 
ATOM   4168  O  O   . TYR B 2 173 ? 136.006 137.740 178.031 1.00 113.92 ? 173 TYR D O   1 
ATOM   4169  C  CB  . TYR B 2 173 ? 135.876 139.206 180.596 1.00 113.92 ? 173 TYR D CB  1 
ATOM   4170  C  CG  . TYR B 2 173 ? 135.207 140.265 179.748 1.00 113.92 ? 173 TYR D CG  1 
ATOM   4171  C  CD1 . TYR B 2 173 ? 133.950 140.755 180.073 1.00 113.92 ? 173 TYR D CD1 1 
ATOM   4172  C  CD2 . TYR B 2 173 ? 135.841 140.783 178.626 1.00 113.92 ? 173 TYR D CD2 1 
ATOM   4173  C  CE1 . TYR B 2 173 ? 133.340 141.721 179.297 1.00 113.92 ? 173 TYR D CE1 1 
ATOM   4174  C  CE2 . TYR B 2 173 ? 135.239 141.749 177.847 1.00 113.92 ? 173 TYR D CE2 1 
ATOM   4175  C  CZ  . TYR B 2 173 ? 133.990 142.216 178.188 1.00 113.92 ? 173 TYR D CZ  1 
ATOM   4176  O  OH  . TYR B 2 173 ? 133.387 143.179 177.413 1.00 113.92 ? 173 TYR D OH  1 
ATOM   4177  N  N   . ILE B 2 174 ? 133.868 137.217 178.499 1.00 113.92 ? 174 ILE D N   1 
ATOM   4178  C  CA  . ILE B 2 174 ? 133.481 137.024 177.108 1.00 113.92 ? 174 ILE D CA  1 
ATOM   4179  C  C   . ILE B 2 174 ? 132.701 138.252 176.667 1.00 113.92 ? 174 ILE D C   1 
ATOM   4180  O  O   . ILE B 2 174 ? 131.739 138.659 177.331 1.00 113.92 ? 174 ILE D O   1 
ATOM   4181  C  CB  . ILE B 2 174 ? 132.650 135.745 176.921 1.00 113.92 ? 174 ILE D CB  1 
ATOM   4182  C  CG1 . ILE B 2 174 ? 133.236 134.592 177.733 1.00 113.92 ? 174 ILE D CG1 1 
ATOM   4183  C  CG2 . ILE B 2 174 ? 132.579 135.370 175.450 1.00 113.92 ? 174 ILE D CG2 1 
ATOM   4184  C  CD1 . ILE B 2 174 ? 132.396 133.335 177.680 1.00 113.92 ? 174 ILE D CD1 1 
ATOM   4185  N  N   . ASP B 2 175 ? 133.128 138.851 175.563 1.00 113.92 ? 175 ASP D N   1 
ATOM   4186  C  CA  . ASP B 2 175 ? 132.503 140.050 175.013 1.00 113.92 ? 175 ASP D CA  1 
ATOM   4187  C  C   . ASP B 2 175 ? 131.796 139.644 173.724 1.00 113.92 ? 175 ASP D C   1 
ATOM   4188  O  O   . ASP B 2 175 ? 132.400 139.642 172.648 1.00 113.92 ? 175 ASP D O   1 
ATOM   4189  C  CB  . ASP B 2 175 ? 133.537 141.147 174.767 1.00 113.92 ? 175 ASP D CB  1 
ATOM   4190  C  CG  . ASP B 2 175 ? 132.921 142.420 174.222 1.00 113.92 ? 175 ASP D CG  1 
ATOM   4191  O  OD1 . ASP B 2 175 ? 132.372 143.206 175.022 1.00 113.92 ? 175 ASP D OD1 1 
ATOM   4192  O  OD2 . ASP B 2 175 ? 132.987 142.635 172.993 1.00 113.92 ? 175 ASP D OD2 1 
ATOM   4193  N  N   . ILE B 2 176 ? 130.527 139.255 173.851 1.00 113.92 ? 176 ILE D N   1 
ATOM   4194  C  CA  . ILE B 2 176 ? 129.639 139.058 172.709 1.00 113.92 ? 176 ILE D CA  1 
ATOM   4195  C  C   . ILE B 2 176 ? 129.126 140.441 172.321 1.00 113.92 ? 176 ILE D C   1 
ATOM   4196  O  O   . ILE B 2 176 ? 128.282 141.015 173.007 1.00 113.92 ? 176 ILE D O   1 
ATOM   4197  C  CB  . ILE B 2 176 ? 128.493 138.097 173.029 1.00 113.92 ? 176 ILE D CB  1 
ATOM   4198  C  CG1 . ILE B 2 176 ? 128.998 136.659 173.039 1.00 113.92 ? 176 ILE D CG1 1 
ATOM   4199  C  CG2 . ILE B 2 176 ? 127.376 138.230 172.005 1.00 113.92 ? 176 ILE D CG2 1 
ATOM   4200  C  CD1 . ILE B 2 176 ? 128.039 135.707 173.678 1.00 113.92 ? 176 ILE D CD1 1 
ATOM   4201  N  N   . ASP B 2 177 ? 129.641 140.983 171.230 1.00 113.92 ? 177 ASP D N   1 
ATOM   4202  C  CA  . ASP B 2 177 ? 129.314 142.341 170.814 1.00 113.92 ? 177 ASP D CA  1 
ATOM   4203  C  C   . ASP B 2 177 ? 129.869 142.532 169.413 1.00 113.92 ? 177 ASP D C   1 
ATOM   4204  O  O   . ASP B 2 177 ? 130.495 141.634 168.842 1.00 113.92 ? 177 ASP D O   1 
ATOM   4205  C  CB  . ASP B 2 177 ? 129.886 143.376 171.787 1.00 113.92 ? 177 ASP D CB  1 
ATOM   4206  C  CG  . ASP B 2 177 ? 129.063 144.645 171.843 1.00 113.92 ? 177 ASP D CG  1 
ATOM   4207  O  OD1 . ASP B 2 177 ? 128.496 145.031 170.801 1.00 113.92 ? 177 ASP D OD1 1 
ATOM   4208  O  OD2 . ASP B 2 177 ? 128.985 145.258 172.929 1.00 113.92 ? 177 ASP D OD2 1 
ATOM   4209  N  N   . ILE B 2 178 ? 129.614 143.710 168.849 1.00 113.92 ? 178 ILE D N   1 
ATOM   4210  C  CA  . ILE B 2 178 ? 130.215 144.075 167.575 1.00 113.92 ? 178 ILE D CA  1 
ATOM   4211  C  C   . ILE B 2 178 ? 131.338 145.087 167.754 1.00 113.92 ? 178 ILE D C   1 
ATOM   4212  O  O   . ILE B 2 178 ? 132.121 145.303 166.815 1.00 113.92 ? 178 ILE D O   1 
ATOM   4213  C  CB  . ILE B 2 178 ? 129.136 144.592 166.599 1.00 113.92 ? 178 ILE D CB  1 
ATOM   4214  C  CG1 . ILE B 2 178 ? 129.666 144.633 165.167 1.00 113.92 ? 178 ILE D CG1 1 
ATOM   4215  C  CG2 . ILE B 2 178 ? 128.635 145.960 167.033 1.00 113.92 ? 178 ILE D CG2 1 
ATOM   4216  C  CD1 . ILE B 2 178 ? 128.594 144.881 164.150 1.00 113.92 ? 178 ILE D CD1 1 
ATOM   4217  N  N   . HIS B 2 179 ? 131.465 145.684 168.936 1.00 113.92 ? 179 HIS D N   1 
ATOM   4218  C  CA  . HIS B 2 179 ? 132.563 146.582 169.255 1.00 113.92 ? 179 HIS D CA  1 
ATOM   4219  C  C   . HIS B 2 179 ? 133.537 145.889 170.197 1.00 113.92 ? 179 HIS D C   1 
ATOM   4220  O  O   . HIS B 2 179 ? 133.123 145.211 171.142 1.00 113.92 ? 179 HIS D O   1 
ATOM   4221  C  CB  . HIS B 2 179 ? 132.052 147.862 169.918 1.00 113.92 ? 179 HIS D CB  1 
ATOM   4222  C  CG  . HIS B 2 179 ? 130.857 148.459 169.244 1.00 113.92 ? 179 HIS D CG  1 
ATOM   4223  N  ND1 . HIS B 2 179 ? 129.573 148.264 169.705 1.00 113.92 ? 179 HIS D ND1 1 
ATOM   4224  C  CD2 . HIS B 2 179 ? 130.749 149.242 168.146 1.00 113.92 ? 179 HIS D CD2 1 
ATOM   4225  C  CE1 . HIS B 2 179 ? 128.725 148.904 168.921 1.00 113.92 ? 179 HIS D CE1 1 
ATOM   4226  N  NE2 . HIS B 2 179 ? 129.412 149.504 167.967 1.00 113.92 ? 179 HIS D NE2 1 
ATOM   4227  N  N   . HIS B 2 180 ? 134.830 146.057 169.932 1.00 113.92 ? 180 HIS D N   1 
ATOM   4228  C  CA  . HIS B 2 180 ? 135.848 145.567 170.850 1.00 113.92 ? 180 HIS D CA  1 
ATOM   4229  C  C   . HIS B 2 180 ? 135.744 146.286 172.189 1.00 113.92 ? 180 HIS D C   1 
ATOM   4230  O  O   . HIS B 2 180 ? 135.538 147.501 172.245 1.00 113.92 ? 180 HIS D O   1 
ATOM   4231  C  CB  . HIS B 2 180 ? 137.242 145.762 170.257 1.00 113.92 ? 180 HIS D CB  1 
ATOM   4232  C  CG  . HIS B 2 180 ? 138.348 145.504 171.232 1.00 113.92 ? 180 HIS D CG  1 
ATOM   4233  N  ND1 . HIS B 2 180 ? 139.204 146.494 171.663 1.00 113.92 ? 180 HIS D ND1 1 
ATOM   4234  C  CD2 . HIS B 2 180 ? 138.730 144.372 171.868 1.00 113.92 ? 180 HIS D CD2 1 
ATOM   4235  C  CE1 . HIS B 2 180 ? 140.069 145.982 172.519 1.00 113.92 ? 180 HIS D CE1 1 
ATOM   4236  N  NE2 . HIS B 2 180 ? 139.804 144.696 172.661 1.00 113.92 ? 180 HIS D NE2 1 
ATOM   4237  N  N   . GLY B 2 181 ? 135.889 145.531 173.274 1.00 113.92 ? 181 GLY D N   1 
ATOM   4238  C  CA  . GLY B 2 181 ? 135.805 146.130 174.591 1.00 113.92 ? 181 GLY D CA  1 
ATOM   4239  C  C   . GLY B 2 181 ? 137.137 146.681 175.051 1.00 113.92 ? 181 GLY D C   1 
ATOM   4240  O  O   . GLY B 2 181 ? 137.976 145.949 175.586 1.00 113.92 ? 181 GLY D O   1 
ATOM   4241  N  N   . ASP B 2 182 ? 137.337 147.984 174.846 1.00 113.92 ? 182 ASP D N   1 
ATOM   4242  C  CA  . ASP B 2 182 ? 138.630 148.599 175.127 1.00 113.92 ? 182 ASP D CA  1 
ATOM   4243  C  C   . ASP B 2 182 ? 138.890 148.695 176.624 1.00 113.92 ? 182 ASP D C   1 
ATOM   4244  O  O   . ASP B 2 182 ? 139.974 148.338 177.101 1.00 113.92 ? 182 ASP D O   1 
ATOM   4245  C  CB  . ASP B 2 182 ? 138.704 149.986 174.490 1.00 100.60 ? 182 ASP D CB  1 
ATOM   4246  C  CG  . ASP B 2 182 ? 138.621 149.942 172.982 1.00 100.60 ? 182 ASP D CG  1 
ATOM   4247  O  OD1 . ASP B 2 182 ? 138.877 148.868 172.401 1.00 100.60 ? 182 ASP D OD1 1 
ATOM   4248  O  OD2 . ASP B 2 182 ? 138.308 150.989 172.379 1.00 100.60 ? 182 ASP D OD2 1 
ATOM   4249  N  N   . GLY B 2 183 ? 137.914 149.198 177.380 1.00 113.92 ? 183 GLY D N   1 
ATOM   4250  C  CA  . GLY B 2 183 ? 138.140 149.418 178.799 1.00 113.92 ? 183 GLY D CA  1 
ATOM   4251  C  C   . GLY B 2 183 ? 138.529 148.154 179.538 1.00 113.92 ? 183 GLY D C   1 
ATOM   4252  O  O   . GLY B 2 183 ? 139.503 148.141 180.291 1.00 113.92 ? 183 GLY D O   1 
ATOM   4253  N  N   . VAL B 2 184 ? 137.798 147.063 179.301 1.00 113.92 ? 184 VAL D N   1 
ATOM   4254  C  CA  . VAL B 2 184 ? 138.083 145.812 180.000 1.00 113.92 ? 184 VAL D CA  1 
ATOM   4255  C  C   . VAL B 2 184 ? 139.452 145.269 179.611 1.00 113.92 ? 184 VAL D C   1 
ATOM   4256  O  O   . VAL B 2 184 ? 140.250 144.872 180.475 1.00 113.92 ? 184 VAL D O   1 
ATOM   4257  C  CB  . VAL B 2 184 ? 136.971 144.785 179.723 1.00 113.92 ? 184 VAL D CB  1 
ATOM   4258  C  CG1 . VAL B 2 184 ? 137.196 143.527 180.545 1.00 113.92 ? 184 VAL D CG1 1 
ATOM   4259  C  CG2 . VAL B 2 184 ? 135.611 145.394 180.016 1.00 113.92 ? 184 VAL D CG2 1 
ATOM   4260  N  N   . GLU B 2 185 ? 139.774 145.299 178.316 1.00 113.92 ? 185 GLU D N   1 
ATOM   4261  C  CA  . GLU B 2 185 ? 141.040 144.722 177.880 1.00 113.92 ? 185 GLU D CA  1 
ATOM   4262  C  C   . GLU B 2 185 ? 142.207 145.510 178.453 1.00 113.92 ? 185 GLU D C   1 
ATOM   4263  O  O   . GLU B 2 185 ? 143.120 144.930 179.048 1.00 113.92 ? 185 GLU D O   1 
ATOM   4264  C  CB  . GLU B 2 185 ? 141.122 144.662 176.356 1.00 113.92 ? 185 GLU D CB  1 
ATOM   4265  C  CG  . GLU B 2 185 ? 142.344 143.890 175.876 1.00 113.92 ? 185 GLU D CG  1 
ATOM   4266  C  CD  . GLU B 2 185 ? 142.425 143.770 174.371 1.00 113.92 ? 185 GLU D CD  1 
ATOM   4267  O  OE1 . GLU B 2 185 ? 142.487 144.815 173.696 1.00 113.92 ? 185 GLU D OE1 1 
ATOM   4268  O  OE2 . GLU B 2 185 ? 142.423 142.629 173.863 1.00 113.92 ? 185 GLU D OE2 1 
ATOM   4269  N  N   . GLU B 2 186 ? 142.191 146.836 178.304 1.00 123.80 ? 186 GLU D N   1 
ATOM   4270  C  CA  . GLU B 2 186 ? 143.302 147.618 178.831 1.00 123.80 ? 186 GLU D CA  1 
ATOM   4271  C  C   . GLU B 2 186 ? 143.351 147.548 180.352 1.00 123.80 ? 186 GLU D C   1 
ATOM   4272  O  O   . GLU B 2 186 ? 144.438 147.615 180.936 1.00 123.80 ? 186 GLU D O   1 
ATOM   4273  C  CB  . GLU B 2 186 ? 143.215 149.067 178.346 1.00 123.80 ? 186 GLU D CB  1 
ATOM   4274  C  CG  . GLU B 2 186 ? 143.730 149.341 176.915 1.00 123.80 ? 186 GLU D CG  1 
ATOM   4275  C  CD  . GLU B 2 186 ? 143.256 148.366 175.839 1.00 123.80 ? 186 GLU D CD  1 
ATOM   4276  O  OE1 . GLU B 2 186 ? 143.881 148.347 174.757 1.00 123.80 ? 186 GLU D OE1 1 
ATOM   4277  O  OE2 . GLU B 2 186 ? 142.266 147.639 176.039 1.00 123.80 ? 186 GLU D OE2 1 
ATOM   4278  N  N   . ALA B 2 187 ? 142.193 147.426 181.012 1.00 115.59 ? 187 ALA D N   1 
ATOM   4279  C  CA  . ALA B 2 187 ? 142.185 147.288 182.461 1.00 115.59 ? 187 ALA D CA  1 
ATOM   4280  C  C   . ALA B 2 187 ? 142.857 145.995 182.894 1.00 115.59 ? 187 ALA D C   1 
ATOM   4281  O  O   . ALA B 2 187 ? 143.431 145.931 183.987 1.00 115.59 ? 187 ALA D O   1 
ATOM   4282  C  CB  . ALA B 2 187 ? 140.751 147.348 182.987 1.00 115.59 ? 187 ALA D CB  1 
ATOM   4283  N  N   . PHE B 2 188 ? 142.798 144.953 182.058 1.00 113.92 ? 188 PHE D N   1 
ATOM   4284  C  CA  . PHE B 2 188 ? 143.389 143.668 182.420 1.00 113.92 ? 188 PHE D CA  1 
ATOM   4285  C  C   . PHE B 2 188 ? 144.339 143.156 181.341 1.00 113.92 ? 188 PHE D C   1 
ATOM   4286  O  O   . PHE B 2 188 ? 144.491 141.944 181.165 1.00 113.92 ? 188 PHE D O   1 
ATOM   4287  C  CB  . PHE B 2 188 ? 142.308 142.632 182.726 1.00 113.92 ? 188 PHE D CB  1 
ATOM   4288  C  CG  . PHE B 2 188 ? 141.186 143.165 183.564 1.00 113.92 ? 188 PHE D CG  1 
ATOM   4289  C  CD1 . PHE B 2 188 ? 141.379 143.424 184.908 1.00 113.92 ? 188 PHE D CD1 1 
ATOM   4290  C  CD2 . PHE B 2 188 ? 139.938 143.393 183.016 1.00 113.92 ? 188 PHE D CD2 1 
ATOM   4291  C  CE1 . PHE B 2 188 ? 140.355 143.916 185.683 1.00 113.92 ? 188 PHE D CE1 1 
ATOM   4292  C  CE2 . PHE B 2 188 ? 138.908 143.884 183.788 1.00 113.92 ? 188 PHE D CE2 1 
ATOM   4293  C  CZ  . PHE B 2 188 ? 139.118 144.148 185.123 1.00 113.92 ? 188 PHE D CZ  1 
ATOM   4294  N  N   . TYR B 2 189 ? 144.984 144.068 180.610 1.00 113.92 ? 189 TYR D N   1 
ATOM   4295  C  CA  . TYR B 2 189 ? 145.874 143.662 179.527 1.00 113.92 ? 189 TYR D CA  1 
ATOM   4296  C  C   . TYR B 2 189 ? 147.160 143.031 180.046 1.00 113.92 ? 189 TYR D C   1 
ATOM   4297  O  O   . TYR B 2 189 ? 147.697 142.114 179.415 1.00 113.92 ? 189 TYR D O   1 
ATOM   4298  C  CB  . TYR B 2 189 ? 146.203 144.868 178.648 1.00 113.92 ? 189 TYR D CB  1 
ATOM   4299  C  CG  . TYR B 2 189 ? 146.702 144.519 177.268 1.00 113.92 ? 189 TYR D CG  1 
ATOM   4300  C  CD1 . TYR B 2 189 ? 145.873 143.897 176.346 1.00 113.92 ? 189 TYR D CD1 1 
ATOM   4301  C  CD2 . TYR B 2 189 ? 148.000 144.820 176.882 1.00 113.92 ? 189 TYR D CD2 1 
ATOM   4302  C  CE1 . TYR B 2 189 ? 146.323 143.579 175.081 1.00 113.92 ? 189 TYR D CE1 1 
ATOM   4303  C  CE2 . TYR B 2 189 ? 148.460 144.507 175.620 1.00 113.92 ? 189 TYR D CE2 1 
ATOM   4304  C  CZ  . TYR B 2 189 ? 147.618 143.887 174.723 1.00 113.92 ? 189 TYR D CZ  1 
ATOM   4305  O  OH  . TYR B 2 189 ? 148.073 143.574 173.464 1.00 113.92 ? 189 TYR D OH  1 
ATOM   4306  N  N   . THR B 2 190 ? 147.667 143.502 181.186 1.00 113.92 ? 190 THR D N   1 
ATOM   4307  C  CA  . THR B 2 190 ? 148.958 143.072 181.709 1.00 113.92 ? 190 THR D CA  1 
ATOM   4308  C  C   . THR B 2 190 ? 148.831 142.213 182.964 1.00 113.92 ? 190 THR D C   1 
ATOM   4309  O  O   . THR B 2 190 ? 149.735 142.200 183.803 1.00 113.92 ? 190 THR D O   1 
ATOM   4310  C  CB  . THR B 2 190 ? 149.843 144.285 181.990 1.00 113.46 ? 190 THR D CB  1 
ATOM   4311  O  OG1 . THR B 2 190 ? 149.209 145.126 182.961 1.00 113.46 ? 190 THR D OG1 1 
ATOM   4312  C  CG2 . THR B 2 190 ? 150.074 145.080 180.714 1.00 113.46 ? 190 THR D CG2 1 
ATOM   4313  N  N   . THR B 2 191 ? 147.725 141.489 183.110 1.00 113.92 ? 191 THR D N   1 
ATOM   4314  C  CA  . THR B 2 191 ? 147.528 140.619 184.259 1.00 113.92 ? 191 THR D CA  1 
ATOM   4315  C  C   . THR B 2 191 ? 146.995 139.270 183.801 1.00 113.92 ? 191 THR D C   1 
ATOM   4316  O  O   . THR B 2 191 ? 146.262 139.174 182.812 1.00 113.92 ? 191 THR D O   1 
ATOM   4317  C  CB  . THR B 2 191 ? 146.570 141.236 185.292 1.00 113.92 ? 191 THR D CB  1 
ATOM   4318  O  OG1 . THR B 2 191 ? 146.424 140.344 186.404 1.00 113.92 ? 191 THR D OG1 1 
ATOM   4319  C  CG2 . THR B 2 191 ? 145.208 141.491 184.678 1.00 113.92 ? 191 THR D CG2 1 
ATOM   4320  N  N   . ASP B 2 192 ? 147.386 138.225 184.524 1.00 116.18 ? 192 ASP D N   1 
ATOM   4321  C  CA  . ASP B 2 192 ? 146.943 136.869 184.238 1.00 116.18 ? 192 ASP D CA  1 
ATOM   4322  C  C   . ASP B 2 192 ? 145.712 136.465 185.038 1.00 116.18 ? 192 ASP D C   1 
ATOM   4323  O  O   . ASP B 2 192 ? 145.207 135.354 184.847 1.00 116.18 ? 192 ASP D O   1 
ATOM   4324  C  CB  . ASP B 2 192 ? 148.077 135.876 184.510 1.00 116.18 ? 192 ASP D CB  1 
ATOM   4325  C  CG  . ASP B 2 192 ? 148.592 135.956 185.933 1.00 116.18 ? 192 ASP D CG  1 
ATOM   4326  O  OD1 . ASP B 2 192 ? 148.624 137.071 186.494 1.00 116.18 ? 192 ASP D OD1 1 
ATOM   4327  O  OD2 . ASP B 2 192 ? 148.965 134.903 186.491 1.00 116.18 ? 192 ASP D OD2 1 
ATOM   4328  N  N   . ARG B 2 193 ? 145.217 137.331 185.924 1.00 113.92 ? 193 ARG D N   1 
ATOM   4329  C  CA  . ARG B 2 193 ? 144.044 136.980 186.712 1.00 113.92 ? 193 ARG D CA  1 
ATOM   4330  C  C   . ARG B 2 193 ? 142.767 136.983 185.887 1.00 113.92 ? 193 ARG D C   1 
ATOM   4331  O  O   . ARG B 2 193 ? 141.811 136.289 186.248 1.00 113.92 ? 193 ARG D O   1 
ATOM   4332  C  CB  . ARG B 2 193 ? 143.896 137.945 187.887 1.00 107.20 ? 193 ARG D CB  1 
ATOM   4333  C  CG  . ARG B 2 193 ? 144.790 137.635 189.072 1.00 107.20 ? 193 ARG D CG  1 
ATOM   4334  C  CD  . ARG B 2 193 ? 144.229 138.264 190.336 1.00 107.20 ? 193 ARG D CD  1 
ATOM   4335  N  NE  . ARG B 2 193 ? 143.138 137.479 190.900 1.00 107.20 ? 193 ARG D NE  1 
ATOM   4336  C  CZ  . ARG B 2 193 ? 142.435 137.831 191.968 1.00 107.20 ? 193 ARG D CZ  1 
ATOM   4337  N  NH1 . ARG B 2 193 ? 142.667 138.968 192.604 1.00 107.20 ? 193 ARG D NH1 1 
ATOM   4338  N  NH2 . ARG B 2 193 ? 141.469 137.028 192.402 1.00 107.20 ? 193 ARG D NH2 1 
ATOM   4339  N  N   . VAL B 2 194 ? 142.727 137.740 184.794 1.00 113.92 ? 194 VAL D N   1 
ATOM   4340  C  CA  . VAL B 2 194 ? 141.527 137.888 183.981 1.00 113.92 ? 194 VAL D CA  1 
ATOM   4341  C  C   . VAL B 2 194 ? 141.922 137.705 182.526 1.00 113.92 ? 194 VAL D C   1 
ATOM   4342  O  O   . VAL B 2 194 ? 142.789 138.428 182.022 1.00 113.92 ? 194 VAL D O   1 
ATOM   4343  C  CB  . VAL B 2 194 ? 140.857 139.258 184.178 1.00 113.92 ? 194 VAL D CB  1 
ATOM   4344  C  CG1 . VAL B 2 194 ? 139.689 139.419 183.218 1.00 113.92 ? 194 VAL D CG1 1 
ATOM   4345  C  CG2 . VAL B 2 194 ? 140.401 139.432 185.610 1.00 113.92 ? 194 VAL D CG2 1 
ATOM   4346  N  N   . MET B 2 195 ? 141.295 136.750 181.851 1.00 113.92 ? 195 MET D N   1 
ATOM   4347  C  CA  . MET B 2 195 ? 141.440 136.648 180.404 1.00 113.92 ? 195 MET D CA  1 
ATOM   4348  C  C   . MET B 2 195 ? 140.190 137.215 179.751 1.00 113.92 ? 195 MET D C   1 
ATOM   4349  O  O   . MET B 2 195 ? 139.075 136.890 180.163 1.00 113.92 ? 195 MET D O   1 
ATOM   4350  C  CB  . MET B 2 195 ? 141.690 135.213 179.938 1.00 98.64  ? 195 MET D CB  1 
ATOM   4351  C  CG  . MET B 2 195 ? 141.552 135.065 178.425 1.00 98.64  ? 195 MET D CG  1 
ATOM   4352  S  SD  . MET B 2 195 ? 141.704 133.394 177.777 1.00 98.64  ? 195 MET D SD  1 
ATOM   4353  C  CE  . MET B 2 195 ? 142.436 132.553 179.167 1.00 98.64  ? 195 MET D CE  1 
ATOM   4354  N  N   . THR B 2 196 ? 140.376 138.039 178.724 1.00 113.92 ? 196 THR D N   1 
ATOM   4355  C  CA  . THR B 2 196 ? 139.276 138.748 178.073 1.00 113.92 ? 196 THR D CA  1 
ATOM   4356  C  C   . THR B 2 196 ? 139.163 138.269 176.629 1.00 113.92 ? 196 THR D C   1 
ATOM   4357  O  O   . THR B 2 196 ? 139.815 138.809 175.733 1.00 113.92 ? 196 THR D O   1 
ATOM   4358  C  CB  . THR B 2 196 ? 139.486 140.261 178.137 1.00 113.92 ? 196 THR D CB  1 
ATOM   4359  O  OG1 . THR B 2 196 ? 140.420 140.656 177.125 1.00 113.92 ? 196 THR D OG1 1 
ATOM   4360  C  CG2 . THR B 2 196 ? 140.023 140.670 179.499 1.00 113.92 ? 196 THR D CG2 1 
ATOM   4361  N  N   . VAL B 2 197 ? 138.329 137.256 176.410 1.00 113.92 ? 197 VAL D N   1 
ATOM   4362  C  CA  . VAL B 2 197 ? 137.989 136.822 175.060 1.00 113.92 ? 197 VAL D CA  1 
ATOM   4363  C  C   . VAL B 2 197 ? 136.912 137.751 174.516 1.00 113.92 ? 197 VAL D C   1 
ATOM   4364  O  O   . VAL B 2 197 ? 135.833 137.883 175.104 1.00 113.92 ? 197 VAL D O   1 
ATOM   4365  C  CB  . VAL B 2 197 ? 137.522 135.360 175.042 1.00 113.92 ? 197 VAL D CB  1 
ATOM   4366  C  CG1 . VAL B 2 197 ? 137.319 134.893 173.611 1.00 113.92 ? 197 VAL D CG1 1 
ATOM   4367  C  CG2 . VAL B 2 197 ? 138.539 134.479 175.739 1.00 113.92 ? 197 VAL D CG2 1 
ATOM   4368  N  N   . SER B 2 198 ? 137.203 138.398 173.393 1.00 113.92 ? 198 SER D N   1 
ATOM   4369  C  CA  . SER B 2 198 ? 136.332 139.416 172.821 1.00 113.92 ? 198 SER D CA  1 
ATOM   4370  C  C   . SER B 2 198 ? 136.037 139.048 171.377 1.00 113.92 ? 198 SER D C   1 
ATOM   4371  O  O   . SER B 2 198 ? 136.957 138.978 170.551 1.00 113.92 ? 198 SER D O   1 
ATOM   4372  C  CB  . SER B 2 198 ? 136.970 140.804 172.911 1.00 113.92 ? 198 SER D CB  1 
ATOM   4373  O  OG  . SER B 2 198 ? 137.557 141.169 171.679 1.00 113.92 ? 198 SER D OG  1 
ATOM   4374  N  N   . PHE B 2 199 ? 134.760 138.806 171.076 1.00 113.92 ? 199 PHE D N   1 
ATOM   4375  C  CA  . PHE B 2 199 ? 134.303 138.533 169.721 1.00 113.92 ? 199 PHE D CA  1 
ATOM   4376  C  C   . PHE B 2 199 ? 133.723 139.834 169.181 1.00 113.92 ? 199 PHE D C   1 
ATOM   4377  O  O   . PHE B 2 199 ? 132.708 140.320 169.687 1.00 113.92 ? 199 PHE D O   1 
ATOM   4378  C  CB  . PHE B 2 199 ? 133.255 137.424 169.725 1.00 113.92 ? 199 PHE D CB  1 
ATOM   4379  C  CG  . PHE B 2 199 ? 133.777 136.098 170.193 1.00 113.92 ? 199 PHE D CG  1 
ATOM   4380  C  CD1 . PHE B 2 199 ? 134.381 135.219 169.314 1.00 113.92 ? 199 PHE D CD1 1 
ATOM   4381  C  CD2 . PHE B 2 199 ? 133.659 135.732 171.523 1.00 113.92 ? 199 PHE D CD2 1 
ATOM   4382  C  CE1 . PHE B 2 199 ? 134.859 134.000 169.753 1.00 113.92 ? 199 PHE D CE1 1 
ATOM   4383  C  CE2 . PHE B 2 199 ? 134.134 134.515 171.968 1.00 113.92 ? 199 PHE D CE2 1 
ATOM   4384  C  CZ  . PHE B 2 199 ? 134.735 133.649 171.083 1.00 113.92 ? 199 PHE D CZ  1 
ATOM   4385  N  N   . HIS B 2 200 ? 134.366 140.403 168.164 1.00 113.92 ? 200 HIS D N   1 
ATOM   4386  C  CA  . HIS B 2 200 ? 134.020 141.755 167.756 1.00 113.92 ? 200 HIS D CA  1 
ATOM   4387  C  C   . HIS B 2 200 ? 134.392 141.953 166.298 1.00 113.92 ? 200 HIS D C   1 
ATOM   4388  O  O   . HIS B 2 200 ? 135.237 141.242 165.747 1.00 113.92 ? 200 HIS D O   1 
ATOM   4389  C  CB  . HIS B 2 200 ? 134.744 142.804 168.606 1.00 113.92 ? 200 HIS D CB  1 
ATOM   4390  C  CG  . HIS B 2 200 ? 136.237 142.738 168.502 1.00 113.92 ? 200 HIS D CG  1 
ATOM   4391  N  ND1 . HIS B 2 200 ? 137.036 142.205 169.489 1.00 113.92 ? 200 HIS D ND1 1 
ATOM   4392  C  CD2 . HIS B 2 200 ? 137.077 143.153 167.523 1.00 113.92 ? 200 HIS D CD2 1 
ATOM   4393  C  CE1 . HIS B 2 200 ? 138.303 142.288 169.121 1.00 113.92 ? 200 HIS D CE1 1 
ATOM   4394  N  NE2 . HIS B 2 200 ? 138.355 142.859 167.932 1.00 113.92 ? 200 HIS D NE2 1 
ATOM   4395  N  N   . LYS B 2 201 ? 133.756 142.946 165.685 1.00 113.92 ? 201 LYS D N   1 
ATOM   4396  C  CA  . LYS B 2 201 ? 134.102 143.334 164.329 1.00 113.92 ? 201 LYS D CA  1 
ATOM   4397  C  C   . LYS B 2 201 ? 135.372 144.169 164.376 1.00 113.92 ? 201 LYS D C   1 
ATOM   4398  O  O   . LYS B 2 201 ? 135.486 145.097 165.182 1.00 113.92 ? 201 LYS D O   1 
ATOM   4399  C  CB  . LYS B 2 201 ? 132.957 144.122 163.691 1.00 87.89  ? 201 LYS D CB  1 
ATOM   4400  C  CG  . LYS B 2 201 ? 132.946 144.133 162.168 1.00 87.89  ? 201 LYS D CG  1 
ATOM   4401  C  CD  . LYS B 2 201 ? 133.853 145.213 161.600 1.00 87.89  ? 201 LYS D CD  1 
ATOM   4402  C  CE  . LYS B 2 201 ? 133.831 145.213 160.082 1.00 87.89  ? 201 LYS D CE  1 
ATOM   4403  N  NZ  . LYS B 2 201 ? 134.689 146.291 159.519 1.00 87.89  ? 201 LYS D NZ  1 
ATOM   4404  N  N   . TYR B 2 202 ? 136.325 143.842 163.512 1.00 113.92 ? 202 TYR D N   1 
ATOM   4405  C  CA  . TYR B 2 202 ? 137.608 144.521 163.482 1.00 113.92 ? 202 TYR D CA  1 
ATOM   4406  C  C   . TYR B 2 202 ? 137.854 145.110 162.103 1.00 113.92 ? 202 TYR D C   1 
ATOM   4407  O  O   . TYR B 2 202 ? 137.346 144.615 161.093 1.00 113.92 ? 202 TYR D O   1 
ATOM   4408  C  CB  . TYR B 2 202 ? 138.756 143.580 163.857 1.00 113.92 ? 202 TYR D CB  1 
ATOM   4409  C  CG  . TYR B 2 202 ? 140.096 144.272 163.959 1.00 113.92 ? 202 TYR D CG  1 
ATOM   4410  C  CD1 . TYR B 2 202 ? 140.455 144.966 165.106 1.00 113.92 ? 202 TYR D CD1 1 
ATOM   4411  C  CD2 . TYR B 2 202 ? 141.001 144.233 162.907 1.00 113.92 ? 202 TYR D CD2 1 
ATOM   4412  C  CE1 . TYR B 2 202 ? 141.677 145.602 165.201 1.00 113.92 ? 202 TYR D CE1 1 
ATOM   4413  C  CE2 . TYR B 2 202 ? 142.225 144.866 162.993 1.00 113.92 ? 202 TYR D CE2 1 
ATOM   4414  C  CZ  . TYR B 2 202 ? 142.557 145.549 164.143 1.00 113.92 ? 202 TYR D CZ  1 
ATOM   4415  O  OH  . TYR B 2 202 ? 143.776 146.180 164.234 1.00 113.92 ? 202 TYR D OH  1 
ATOM   4416  N  N   . GLY B 2 203 ? 138.644 146.175 162.079 1.00 113.92 ? 203 GLY D N   1 
ATOM   4417  C  CA  . GLY B 2 203 ? 138.937 146.878 160.854 1.00 113.92 ? 203 GLY D CA  1 
ATOM   4418  C  C   . GLY B 2 203 ? 139.047 148.358 161.131 1.00 113.92 ? 203 GLY D C   1 
ATOM   4419  O  O   . GLY B 2 203 ? 139.730 148.779 162.070 1.00 113.92 ? 203 GLY D O   1 
ATOM   4420  N  N   . GLU B 2 204 ? 138.372 149.158 160.316 1.00 113.92 ? 204 GLU D N   1 
ATOM   4421  C  CA  . GLU B 2 204 ? 138.268 150.594 160.553 1.00 113.92 ? 204 GLU D CA  1 
ATOM   4422  C  C   . GLU B 2 204 ? 136.976 150.892 161.313 1.00 113.92 ? 204 GLU D C   1 
ATOM   4423  O  O   . GLU B 2 204 ? 136.103 151.644 160.883 1.00 113.92 ? 204 GLU D O   1 
ATOM   4424  C  CB  . GLU B 2 204 ? 138.350 151.334 159.229 1.00 98.61  ? 204 GLU D CB  1 
ATOM   4425  C  CG  . GLU B 2 204 ? 139.708 151.140 158.601 1.00 98.61  ? 204 GLU D CG  1 
ATOM   4426  C  CD  . GLU B 2 204 ? 139.693 151.305 157.108 1.00 98.61  ? 204 GLU D CD  1 
ATOM   4427  O  OE1 . GLU B 2 204 ? 139.125 150.439 156.411 1.00 98.61  ? 204 GLU D OE1 1 
ATOM   4428  O  OE2 . GLU B 2 204 ? 140.281 152.285 156.631 1.00 98.61  ? 204 GLU D OE2 1 
ATOM   4429  N  N   . TYR B 2 205 ? 136.880 150.258 162.477 1.00 113.92 ? 205 TYR D N   1 
ATOM   4430  C  CA  . TYR B 2 205 ? 135.723 150.336 163.347 1.00 113.92 ? 205 TYR D CA  1 
ATOM   4431  C  C   . TYR B 2 205 ? 136.017 151.300 164.494 1.00 113.92 ? 205 TYR D C   1 
ATOM   4432  O  O   . TYR B 2 205 ? 137.126 151.822 164.626 1.00 113.92 ? 205 TYR D O   1 
ATOM   4433  C  CB  . TYR B 2 205 ? 135.383 148.937 163.864 1.00 113.92 ? 205 TYR D CB  1 
ATOM   4434  C  CG  . TYR B 2 205 ? 133.917 148.598 163.846 1.00 113.92 ? 205 TYR D CG  1 
ATOM   4435  C  CD1 . TYR B 2 205 ? 133.181 148.710 162.678 1.00 113.92 ? 205 TYR D CD1 1 
ATOM   4436  C  CD2 . TYR B 2 205 ? 133.274 148.133 164.984 1.00 113.92 ? 205 TYR D CD2 1 
ATOM   4437  C  CE1 . TYR B 2 205 ? 131.846 148.395 162.645 1.00 113.92 ? 205 TYR D CE1 1 
ATOM   4438  C  CE2 . TYR B 2 205 ? 131.935 147.812 164.961 1.00 113.92 ? 205 TYR D CE2 1 
ATOM   4439  C  CZ  . TYR B 2 205 ? 131.230 147.939 163.786 1.00 113.92 ? 205 TYR D CZ  1 
ATOM   4440  O  OH  . TYR B 2 205 ? 129.893 147.630 163.749 1.00 113.92 ? 205 TYR D OH  1 
ATOM   4441  N  N   . PHE B 2 206 ? 135.001 151.552 165.321 1.00 113.92 ? 206 PHE D N   1 
ATOM   4442  C  CA  . PHE B 2 206 ? 135.072 152.591 166.345 1.00 113.92 ? 206 PHE D CA  1 
ATOM   4443  C  C   . PHE B 2 206 ? 136.278 152.413 167.266 1.00 113.92 ? 206 PHE D C   1 
ATOM   4444  O  O   . PHE B 2 206 ? 137.126 153.313 167.329 1.00 113.92 ? 206 PHE D O   1 
ATOM   4445  C  CB  . PHE B 2 206 ? 133.788 152.644 167.177 1.00 113.92 ? 206 PHE D CB  1 
ATOM   4446  C  CG  . PHE B 2 206 ? 133.986 153.233 168.545 1.00 113.92 ? 206 PHE D CG  1 
ATOM   4447  C  CD1 . PHE B 2 206 ? 134.427 154.540 168.694 1.00 113.92 ? 206 PHE D CD1 1 
ATOM   4448  C  CD2 . PHE B 2 206 ? 133.767 152.474 169.680 1.00 113.92 ? 206 PHE D CD2 1 
ATOM   4449  C  CE1 . PHE B 2 206 ? 134.625 155.080 169.945 1.00 113.92 ? 206 PHE D CE1 1 
ATOM   4450  C  CE2 . PHE B 2 206 ? 133.965 153.013 170.935 1.00 113.92 ? 206 PHE D CE2 1 
ATOM   4451  C  CZ  . PHE B 2 206 ? 134.397 154.315 171.065 1.00 113.92 ? 206 PHE D CZ  1 
ATOM   4452  N  N   . PRO B 2 207 ? 136.391 151.301 168.010 1.00 113.92 ? 207 PRO D N   1 
ATOM   4453  C  CA  . PRO B 2 207 ? 137.448 151.235 169.034 1.00 113.92 ? 207 PRO D CA  1 
ATOM   4454  C  C   . PRO B 2 207 ? 138.846 151.410 168.474 1.00 113.92 ? 207 PRO D C   1 
ATOM   4455  O  O   . PRO B 2 207 ? 139.693 152.047 169.113 1.00 113.92 ? 207 PRO D O   1 
ATOM   4456  C  CB  . PRO B 2 207 ? 137.259 149.841 169.654 1.00 113.92 ? 207 PRO D CB  1 
ATOM   4457  C  CG  . PRO B 2 207 ? 135.935 149.360 169.184 1.00 113.92 ? 207 PRO D CG  1 
ATOM   4458  C  CD  . PRO B 2 207 ? 135.709 150.002 167.865 1.00 113.92 ? 207 PRO D CD  1 
ATOM   4459  N  N   . GLY B 2 208 ? 139.113 150.864 167.289 1.00 113.92 ? 208 GLY D N   1 
ATOM   4460  C  CA  . GLY B 2 208 ? 140.429 150.932 166.700 1.00 113.92 ? 208 GLY D CA  1 
ATOM   4461  C  C   . GLY B 2 208 ? 141.412 149.928 167.253 1.00 113.92 ? 208 GLY D C   1 
ATOM   4462  O  O   . GLY B 2 208 ? 142.501 149.774 166.685 1.00 113.92 ? 208 GLY D O   1 
ATOM   4463  N  N   . THR B 2 209 ? 141.065 149.238 168.333 1.00 113.92 ? 209 THR D N   1 
ATOM   4464  C  CA  . THR B 2 209 ? 141.921 148.254 168.971 1.00 113.92 ? 209 THR D CA  1 
ATOM   4465  C  C   . THR B 2 209 ? 141.287 146.873 168.843 1.00 113.92 ? 209 THR D C   1 
ATOM   4466  O  O   . THR B 2 209 ? 140.168 146.716 168.346 1.00 113.92 ? 209 THR D O   1 
ATOM   4467  C  CB  . THR B 2 209 ? 142.162 148.615 170.439 1.00 97.90  ? 209 THR D CB  1 
ATOM   4468  O  OG1 . THR B 2 209 ? 140.906 148.854 171.086 1.00 97.90  ? 209 THR D OG1 1 
ATOM   4469  C  CG2 . THR B 2 209 ? 143.025 149.861 170.545 1.00 97.90  ? 209 THR D CG2 1 
ATOM   4470  N  N   . GLY B 2 210 ? 142.018 145.867 169.299 1.00 113.92 ? 210 GLY D N   1 
ATOM   4471  C  CA  . GLY B 2 210 ? 141.580 144.496 169.215 1.00 113.92 ? 210 GLY D CA  1 
ATOM   4472  C  C   . GLY B 2 210 ? 142.233 143.717 168.100 1.00 113.92 ? 210 GLY D C   1 
ATOM   4473  O  O   . GLY B 2 210 ? 141.587 142.836 167.523 1.00 113.92 ? 210 GLY D O   1 
ATOM   4474  N  N   . ASP B 2 211 ? 143.488 144.015 167.779 1.00 113.92 ? 211 ASP D N   1 
ATOM   4475  C  CA  . ASP B 2 211 ? 144.194 143.315 166.719 1.00 113.92 ? 211 ASP D CA  1 
ATOM   4476  C  C   . ASP B 2 211 ? 144.455 141.867 167.111 1.00 113.92 ? 211 ASP D C   1 
ATOM   4477  O  O   . ASP B 2 211 ? 144.556 141.526 168.292 1.00 113.92 ? 211 ASP D O   1 
ATOM   4478  C  CB  . ASP B 2 211 ? 145.515 144.024 166.414 1.00 109.89 ? 211 ASP D CB  1 
ATOM   4479  C  CG  . ASP B 2 211 ? 146.193 143.493 165.166 1.00 109.89 ? 211 ASP D CG  1 
ATOM   4480  O  OD1 . ASP B 2 211 ? 145.616 142.613 164.495 1.00 109.89 ? 211 ASP D OD1 1 
ATOM   4481  O  OD2 . ASP B 2 211 ? 147.310 143.958 164.856 1.00 109.89 ? 211 ASP D OD2 1 
ATOM   4482  N  N   . LEU B 2 212 ? 144.546 141.006 166.094 1.00 113.92 ? 212 LEU D N   1 
ATOM   4483  C  CA  . LEU B 2 212 ? 144.832 139.597 166.339 1.00 113.92 ? 212 LEU D CA  1 
ATOM   4484  C  C   . LEU B 2 212 ? 146.164 139.423 167.055 1.00 113.92 ? 212 LEU D C   1 
ATOM   4485  O  O   . LEU B 2 212 ? 146.357 138.442 167.781 1.00 113.92 ? 212 LEU D O   1 
ATOM   4486  C  CB  . LEU B 2 212 ? 144.826 138.821 165.022 1.00 113.92 ? 212 LEU D CB  1 
ATOM   4487  C  CG  . LEU B 2 212 ? 145.061 137.313 165.116 1.00 113.92 ? 212 LEU D CG  1 
ATOM   4488  C  CD1 . LEU B 2 212 ? 144.000 136.669 165.988 1.00 113.92 ? 212 LEU D CD1 1 
ATOM   4489  C  CD2 . LEU B 2 212 ? 145.074 136.688 163.736 1.00 113.92 ? 212 LEU D CD2 1 
ATOM   4490  N  N   . ARG B 2 213 ? 147.086 140.367 166.872 1.00 113.92 ? 213 ARG D N   1 
ATOM   4491  C  CA  . ARG B 2 213 ? 148.395 140.310 167.502 1.00 113.92 ? 213 ARG D CA  1 
ATOM   4492  C  C   . ARG B 2 213 ? 148.409 140.942 168.886 1.00 113.92 ? 213 ARG D C   1 
ATOM   4493  O  O   . ARG B 2 213 ? 149.422 140.840 169.586 1.00 113.92 ? 213 ARG D O   1 
ATOM   4494  C  CB  . ARG B 2 213 ? 149.434 141.011 166.622 1.00 112.96 ? 213 ARG D CB  1 
ATOM   4495  C  CG  . ARG B 2 213 ? 149.535 140.458 165.212 1.00 112.96 ? 213 ARG D CG  1 
ATOM   4496  C  CD  . ARG B 2 213 ? 150.855 140.844 164.570 1.00 112.96 ? 213 ARG D CD  1 
ATOM   4497  N  NE  . ARG B 2 213 ? 151.042 142.290 164.542 1.00 112.96 ? 213 ARG D NE  1 
ATOM   4498  C  CZ  . ARG B 2 213 ? 150.621 143.084 163.567 1.00 112.96 ? 213 ARG D CZ  1 
ATOM   4499  N  NH1 . ARG B 2 213 ? 149.980 142.605 162.514 1.00 112.96 ? 213 ARG D NH1 1 
ATOM   4500  N  NH2 . ARG B 2 213 ? 150.850 144.391 163.651 1.00 112.96 ? 213 ARG D NH2 1 
ATOM   4501  N  N   . ASP B 2 214 ? 147.315 141.586 169.299 1.00 116.82 ? 214 ASP D N   1 
ATOM   4502  C  CA  . ASP B 2 214 ? 147.200 142.139 170.648 1.00 116.82 ? 214 ASP D CA  1 
ATOM   4503  C  C   . ASP B 2 214 ? 146.839 141.006 171.609 1.00 116.82 ? 214 ASP D C   1 
ATOM   4504  O  O   . ASP B 2 214 ? 145.740 140.927 172.162 1.00 116.82 ? 214 ASP D O   1 
ATOM   4505  C  CB  . ASP B 2 214 ? 146.170 143.259 170.685 1.00 116.82 ? 214 ASP D CB  1 
ATOM   4506  C  CG  . ASP B 2 214 ? 146.794 144.630 170.527 1.00 116.82 ? 214 ASP D CG  1 
ATOM   4507  O  OD1 . ASP B 2 214 ? 148.038 144.715 170.465 1.00 116.82 ? 214 ASP D OD1 1 
ATOM   4508  O  OD2 . ASP B 2 214 ? 146.040 145.623 170.464 1.00 116.82 ? 214 ASP D OD2 1 
ATOM   4509  N  N   . ILE B 2 215 ? 147.809 140.110 171.804 1.00 120.94 ? 215 ILE D N   1 
ATOM   4510  C  CA  . ILE B 2 215 ? 147.580 138.903 172.591 1.00 120.94 ? 215 ILE D CA  1 
ATOM   4511  C  C   . ILE B 2 215 ? 147.969 139.067 174.053 1.00 120.94 ? 215 ILE D C   1 
ATOM   4512  O  O   . ILE B 2 215 ? 147.703 138.161 174.856 1.00 120.94 ? 215 ILE D O   1 
ATOM   4513  C  CB  . ILE B 2 215 ? 148.294 137.717 171.903 1.00 120.94 ? 215 ILE D CB  1 
ATOM   4514  C  CG1 . ILE B 2 215 ? 149.822 137.816 172.004 1.00 120.94 ? 215 ILE D CG1 1 
ATOM   4515  C  CG2 . ILE B 2 215 ? 147.871 137.615 170.449 1.00 120.94 ? 215 ILE D CG2 1 
ATOM   4516  C  CD1 . ILE B 2 215 ? 150.439 137.106 173.180 1.00 120.94 ? 215 ILE D CD1 1 
ATOM   4517  N  N   . GLY B 2 216 ? 148.552 140.200 174.431 1.00 118.56 ? 216 GLY D N   1 
ATOM   4518  C  CA  . GLY B 2 216 ? 148.864 140.506 175.810 1.00 118.56 ? 216 GLY D CA  1 
ATOM   4519  C  C   . GLY B 2 216 ? 150.296 140.965 175.974 1.00 118.56 ? 216 GLY D C   1 
ATOM   4520  O  O   . GLY B 2 216 ? 151.073 141.033 175.024 1.00 118.56 ? 216 GLY D O   1 
ATOM   4521  N  N   . ALA B 2 217 ? 150.640 141.285 177.220 1.00 129.19 ? 217 ALA D N   1 
ATOM   4522  C  CA  . ALA B 2 217 ? 151.986 141.725 177.559 1.00 129.19 ? 217 ALA D CA  1 
ATOM   4523  C  C   . ALA B 2 217 ? 152.223 141.499 179.045 1.00 129.19 ? 217 ALA D C   1 
ATOM   4524  O  O   . ALA B 2 217 ? 151.281 141.345 179.826 1.00 129.19 ? 217 ALA D O   1 
ATOM   4525  C  CB  . ALA B 2 217 ? 152.207 143.197 177.197 1.00 129.19 ? 217 ALA D CB  1 
ATOM   4526  N  N   . GLY B 2 218 ? 153.501 141.484 179.424 1.00 113.92 ? 218 GLY D N   1 
ATOM   4527  C  CA  . GLY B 2 218 ? 153.858 141.307 180.819 1.00 113.92 ? 218 GLY D CA  1 
ATOM   4528  C  C   . GLY B 2 218 ? 153.485 139.930 181.341 1.00 113.92 ? 218 GLY D C   1 
ATOM   4529  O  O   . GLY B 2 218 ? 153.510 138.930 180.618 1.00 113.92 ? 218 GLY D O   1 
ATOM   4530  N  N   . LYS B 2 219 ? 153.149 139.880 182.633 1.00 113.92 ? 219 LYS D N   1 
ATOM   4531  C  CA  . LYS B 2 219 ? 152.765 138.613 183.250 1.00 113.92 ? 219 LYS D CA  1 
ATOM   4532  C  C   . LYS B 2 219 ? 151.540 138.016 182.573 1.00 113.92 ? 219 LYS D C   1 
ATOM   4533  O  O   . LYS B 2 219 ? 151.419 136.790 182.474 1.00 113.92 ? 219 LYS D O   1 
ATOM   4534  C  CB  . LYS B 2 219 ? 152.505 138.811 184.743 1.00 113.92 ? 219 LYS D CB  1 
ATOM   4535  N  N   . GLY B 2 220 ? 150.627 138.862 182.106 1.00 124.17 ? 220 GLY D N   1 
ATOM   4536  C  CA  . GLY B 2 220 ? 149.461 138.410 181.375 1.00 124.17 ? 220 GLY D CA  1 
ATOM   4537  C  C   . GLY B 2 220 ? 149.727 138.388 179.886 1.00 124.17 ? 220 GLY D C   1 
ATOM   4538  O  O   . GLY B 2 220 ? 148.899 138.844 179.092 1.00 124.17 ? 220 GLY D O   1 
ATOM   4539  N  N   . LYS B 2 221 ? 150.895 137.866 179.500 1.00 127.06 ? 221 LYS D N   1 
ATOM   4540  C  CA  . LYS B 2 221 ? 151.299 137.900 178.098 1.00 127.06 ? 221 LYS D CA  1 
ATOM   4541  C  C   . LYS B 2 221 ? 150.326 137.135 177.213 1.00 127.06 ? 221 LYS D C   1 
ATOM   4542  O  O   . LYS B 2 221 ? 149.965 137.607 176.132 1.00 127.06 ? 221 LYS D O   1 
ATOM   4543  C  CB  . LYS B 2 221 ? 152.713 137.341 177.941 1.00 127.06 ? 221 LYS D CB  1 
ATOM   4544  C  CG  . LYS B 2 221 ? 153.191 137.283 176.499 1.00 127.06 ? 221 LYS D CG  1 
ATOM   4545  C  CD  . LYS B 2 221 ? 154.707 137.310 176.409 1.00 127.06 ? 221 LYS D CD  1 
ATOM   4546  C  CE  . LYS B 2 221 ? 155.174 137.314 174.961 1.00 127.06 ? 221 LYS D CE  1 
ATOM   4547  N  NZ  . LYS B 2 221 ? 154.032 137.289 174.005 1.00 127.06 ? 221 LYS D NZ  1 
ATOM   4548  N  N   . TYR B 2 222 ? 149.887 135.958 177.647 1.00 126.30 ? 222 TYR D N   1 
ATOM   4549  C  CA  . TYR B 2 222 ? 148.974 135.124 176.872 1.00 126.30 ? 222 TYR D CA  1 
ATOM   4550  C  C   . TYR B 2 222 ? 147.591 135.054 177.514 1.00 126.30 ? 222 TYR D C   1 
ATOM   4551  O  O   . TYR B 2 222 ? 146.956 134.000 177.550 1.00 126.30 ? 222 TYR D O   1 
ATOM   4552  C  CB  . TYR B 2 222 ? 149.551 133.726 176.676 1.00 126.30 ? 222 TYR D CB  1 
ATOM   4553  C  CG  . TYR B 2 222 ? 150.578 133.653 175.568 1.00 126.30 ? 222 TYR D CG  1 
ATOM   4554  C  CD1 . TYR B 2 222 ? 150.191 133.440 174.252 1.00 126.30 ? 222 TYR D CD1 1 
ATOM   4555  C  CD2 . TYR B 2 222 ? 151.932 133.805 175.835 1.00 126.30 ? 222 TYR D CD2 1 
ATOM   4556  C  CE1 . TYR B 2 222 ? 151.121 133.376 173.234 1.00 126.30 ? 222 TYR D CE1 1 
ATOM   4557  C  CE2 . TYR B 2 222 ? 152.871 133.741 174.822 1.00 126.30 ? 222 TYR D CE2 1 
ATOM   4558  C  CZ  . TYR B 2 222 ? 152.460 133.527 173.524 1.00 126.30 ? 222 TYR D CZ  1 
ATOM   4559  O  OH  . TYR B 2 222 ? 153.389 133.463 172.512 1.00 126.30 ? 222 TYR D OH  1 
ATOM   4560  N  N   . TYR B 2 223 ? 147.111 136.184 178.024 1.00 113.92 ? 223 TYR D N   1 
ATOM   4561  C  CA  . TYR B 2 223 ? 145.817 136.270 178.687 1.00 113.92 ? 223 TYR D CA  1 
ATOM   4562  C  C   . TYR B 2 223 ? 144.964 137.371 178.072 1.00 113.92 ? 223 TYR D C   1 
ATOM   4563  O  O   . TYR B 2 223 ? 144.266 138.108 178.773 1.00 113.92 ? 223 TYR D O   1 
ATOM   4564  C  CB  . TYR B 2 223 ? 145.993 136.492 180.187 1.00 113.92 ? 223 TYR D CB  1 
ATOM   4565  C  CG  . TYR B 2 223 ? 146.657 135.335 180.902 1.00 113.92 ? 223 TYR D CG  1 
ATOM   4566  C  CD1 . TYR B 2 223 ? 148.038 135.195 180.909 1.00 113.92 ? 223 TYR D CD1 1 
ATOM   4567  C  CD2 . TYR B 2 223 ? 145.900 134.388 181.578 1.00 113.92 ? 223 TYR D CD2 1 
ATOM   4568  C  CE1 . TYR B 2 223 ? 148.646 134.138 181.561 1.00 113.92 ? 223 TYR D CE1 1 
ATOM   4569  C  CE2 . TYR B 2 223 ? 146.499 133.332 182.236 1.00 113.92 ? 223 TYR D CE2 1 
ATOM   4570  C  CZ  . TYR B 2 223 ? 147.871 133.211 182.224 1.00 113.92 ? 223 TYR D CZ  1 
ATOM   4571  O  OH  . TYR B 2 223 ? 148.470 132.158 182.877 1.00 113.92 ? 223 TYR D OH  1 
ATOM   4572  N  N   . ALA B 2 224 ? 145.010 137.501 176.744 1.00 113.92 ? 224 ALA D N   1 
ATOM   4573  C  CA  . ALA B 2 224 ? 144.182 138.479 176.040 1.00 113.92 ? 224 ALA D CA  1 
ATOM   4574  C  C   . ALA B 2 224 ? 143.848 137.898 174.668 1.00 113.92 ? 224 ALA D C   1 
ATOM   4575  O  O   . ALA B 2 224 ? 144.647 138.007 173.734 1.00 113.92 ? 224 ALA D O   1 
ATOM   4576  C  CB  . ALA B 2 224 ? 144.891 139.821 175.923 1.00 113.92 ? 224 ALA D CB  1 
ATOM   4577  N  N   . VAL B 2 225 ? 142.671 137.288 174.559 1.00 113.92 ? 225 VAL D N   1 
ATOM   4578  C  CA  . VAL B 2 225 ? 142.216 136.646 173.330 1.00 113.92 ? 225 VAL D CA  1 
ATOM   4579  C  C   . VAL B 2 225 ? 141.241 137.569 172.614 1.00 113.92 ? 225 VAL D C   1 
ATOM   4580  O  O   . VAL B 2 225 ? 140.251 138.018 173.202 1.00 113.92 ? 225 VAL D O   1 
ATOM   4581  C  CB  . VAL B 2 225 ? 141.570 135.283 173.627 1.00 113.92 ? 225 VAL D CB  1 
ATOM   4582  C  CG1 . VAL B 2 225 ? 141.273 134.555 172.340 1.00 113.92 ? 225 VAL D CG1 1 
ATOM   4583  C  CG2 . VAL B 2 225 ? 142.489 134.451 174.500 1.00 113.92 ? 225 VAL D CG2 1 
ATOM   4584  N  N   . ASN B 2 226 ? 141.515 137.854 171.343 1.00 113.92 ? 226 ASN D N   1 
ATOM   4585  C  CA  . ASN B 2 226 ? 140.627 138.651 170.508 1.00 113.92 ? 226 ASN D CA  1 
ATOM   4586  C  C   . ASN B 2 226 ? 140.339 137.892 169.223 1.00 113.92 ? 226 ASN D C   1 
ATOM   4587  O  O   . ASN B 2 226 ? 141.260 137.341 168.611 1.00 113.92 ? 226 ASN D O   1 
ATOM   4588  C  CB  . ASN B 2 226 ? 141.247 140.014 170.188 1.00 113.92 ? 226 ASN D CB  1 
ATOM   4589  C  CG  . ASN B 2 226 ? 141.346 140.907 171.406 1.00 113.92 ? 226 ASN D CG  1 
ATOM   4590  O  OD1 . ASN B 2 226 ? 140.492 140.868 172.291 1.00 113.92 ? 226 ASN D OD1 1 
ATOM   4591  N  ND2 . ASN B 2 226 ? 142.396 141.717 171.460 1.00 113.92 ? 226 ASN D ND2 1 
ATOM   4592  N  N   . PHE B 2 227 ? 139.069 137.857 168.811 1.00 113.92 ? 227 PHE D N   1 
ATOM   4593  C  CA  . PHE B 2 227 ? 138.673 137.185 167.573 1.00 113.92 ? 227 PHE D CA  1 
ATOM   4594  C  C   . PHE B 2 227 ? 138.131 138.238 166.616 1.00 113.92 ? 227 PHE D C   1 
ATOM   4595  O  O   . PHE B 2 227 ? 136.931 138.553 166.638 1.00 113.92 ? 227 PHE D O   1 
ATOM   4596  C  CB  . PHE B 2 227 ? 137.638 136.091 167.833 1.00 113.92 ? 227 PHE D CB  1 
ATOM   4597  C  CG  . PHE B 2 227 ? 137.567 135.049 166.746 1.00 113.92 ? 227 PHE D CG  1 
ATOM   4598  C  CD1 . PHE B 2 227 ? 137.171 135.387 165.462 1.00 113.92 ? 227 PHE D CD1 1 
ATOM   4599  C  CD2 . PHE B 2 227 ? 137.897 133.732 167.010 1.00 113.92 ? 227 PHE D CD2 1 
ATOM   4600  C  CE1 . PHE B 2 227 ? 137.107 134.432 164.465 1.00 113.92 ? 227 PHE D CE1 1 
ATOM   4601  C  CE2 . PHE B 2 227 ? 137.835 132.773 166.016 1.00 113.92 ? 227 PHE D CE2 1 
ATOM   4602  C  CZ  . PHE B 2 227 ? 137.439 133.124 164.743 1.00 113.92 ? 227 PHE D CZ  1 
ATOM   4603  N  N   . PRO B 2 228 ? 138.983 138.827 165.779 1.00 113.92 ? 228 PRO D N   1 
ATOM   4604  C  CA  . PRO B 2 228 ? 138.499 139.805 164.798 1.00 113.92 ? 228 PRO D CA  1 
ATOM   4605  C  C   . PRO B 2 228 ? 137.502 139.185 163.829 1.00 113.92 ? 228 PRO D C   1 
ATOM   4606  O  O   . PRO B 2 228 ? 137.624 138.022 163.443 1.00 113.92 ? 228 PRO D O   1 
ATOM   4607  C  CB  . PRO B 2 228 ? 139.779 140.248 164.082 1.00 113.92 ? 228 PRO D CB  1 
ATOM   4608  C  CG  . PRO B 2 228 ? 140.887 139.922 165.028 1.00 113.92 ? 228 PRO D CG  1 
ATOM   4609  C  CD  . PRO B 2 228 ? 140.450 138.692 165.758 1.00 113.92 ? 228 PRO D CD  1 
ATOM   4610  N  N   . MET B 2 229 ? 136.504 139.978 163.440 1.00 113.92 ? 229 MET D N   1 
ATOM   4611  C  CA  . MET B 2 229 ? 135.505 139.540 162.478 1.00 113.92 ? 229 MET D CA  1 
ATOM   4612  C  C   . MET B 2 229 ? 135.141 140.679 161.539 1.00 113.92 ? 229 MET D C   1 
ATOM   4613  O  O   . MET B 2 229 ? 135.346 141.856 161.841 1.00 113.92 ? 229 MET D O   1 
ATOM   4614  C  CB  . MET B 2 229 ? 134.241 139.002 163.156 1.00 113.92 ? 229 MET D CB  1 
ATOM   4615  C  CG  . MET B 2 229 ? 134.384 137.590 163.679 1.00 113.92 ? 229 MET D CG  1 
ATOM   4616  S  SD  . MET B 2 229 ? 133.092 137.143 164.843 1.00 113.92 ? 229 MET D SD  1 
ATOM   4617  C  CE  . MET B 2 229 ? 134.082 136.948 166.314 1.00 113.92 ? 229 MET D CE  1 
ATOM   4618  N  N   . ARG B 2 230 ? 134.607 140.302 160.383 1.00 113.92 ? 230 ARG D N   1 
ATOM   4619  C  CA  . ARG B 2 230 ? 134.122 141.251 159.396 1.00 113.92 ? 230 ARG D CA  1 
ATOM   4620  C  C   . ARG B 2 230 ? 132.626 141.480 159.620 1.00 113.92 ? 230 ARG D C   1 
ATOM   4621  O  O   . ARG B 2 230 ? 132.059 141.068 160.635 1.00 113.92 ? 230 ARG D O   1 
ATOM   4622  C  CB  . ARG B 2 230 ? 134.439 140.732 157.996 1.00 113.92 ? 230 ARG D CB  1 
ATOM   4623  C  CG  . ARG B 2 230 ? 135.885 140.283 157.841 1.00 113.92 ? 230 ARG D CG  1 
ATOM   4624  C  CD  . ARG B 2 230 ? 136.188 139.796 156.435 1.00 113.92 ? 230 ARG D CD  1 
ATOM   4625  N  NE  . ARG B 2 230 ? 137.567 139.339 156.305 1.00 113.92 ? 230 ARG D NE  1 
ATOM   4626  C  CZ  . ARG B 2 230 ? 138.034 138.647 155.274 1.00 113.92 ? 230 ARG D CZ  1 
ATOM   4627  N  NH1 . ARG B 2 230 ? 137.254 138.301 154.263 1.00 113.92 ? 230 ARG D NH1 1 
ATOM   4628  N  NH2 . ARG B 2 230 ? 139.314 138.287 155.261 1.00 113.92 ? 230 ARG D NH2 1 
ATOM   4629  N  N   . ASP B 2 231 ? 131.967 142.146 158.675 1.00 113.92 ? 231 ASP D N   1 
ATOM   4630  C  CA  . ASP B 2 231 ? 130.563 142.506 158.825 1.00 113.92 ? 231 ASP D CA  1 
ATOM   4631  C  C   . ASP B 2 231 ? 129.657 141.422 158.252 1.00 113.92 ? 231 ASP D C   1 
ATOM   4632  O  O   . ASP B 2 231 ? 129.920 140.880 157.175 1.00 113.92 ? 231 ASP D O   1 
ATOM   4633  C  CB  . ASP B 2 231 ? 130.268 143.844 158.144 1.00 112.78 ? 231 ASP D CB  1 
ATOM   4634  C  CG  . ASP B 2 231 ? 130.730 143.881 156.704 1.00 112.78 ? 231 ASP D CG  1 
ATOM   4635  O  OD1 . ASP B 2 231 ? 131.736 143.214 156.383 1.00 112.78 ? 231 ASP D OD1 1 
ATOM   4636  O  OD2 . ASP B 2 231 ? 130.085 144.576 155.892 1.00 112.78 ? 231 ASP D OD2 1 
ATOM   4637  N  N   . GLY B 2 232 ? 128.590 141.110 158.985 1.00 113.92 ? 232 GLY D N   1 
ATOM   4638  C  CA  . GLY B 2 232 ? 127.564 140.216 158.489 1.00 113.92 ? 232 GLY D CA  1 
ATOM   4639  C  C   . GLY B 2 232 ? 127.734 138.748 158.801 1.00 113.92 ? 232 GLY D C   1 
ATOM   4640  O  O   . GLY B 2 232 ? 127.327 137.905 157.995 1.00 113.92 ? 232 GLY D O   1 
ATOM   4641  N  N   . ILE B 2 233 ? 128.281 138.407 159.967 1.00 113.92 ? 233 ILE D N   1 
ATOM   4642  C  CA  . ILE B 2 233 ? 128.464 137.007 160.337 1.00 113.92 ? 233 ILE D CA  1 
ATOM   4643  C  C   . ILE B 2 233 ? 127.111 136.367 160.625 1.00 113.92 ? 233 ILE D C   1 
ATOM   4644  O  O   . ILE B 2 233 ? 126.262 136.947 161.315 1.00 113.92 ? 233 ILE D O   1 
ATOM   4645  C  CB  . ILE B 2 233 ? 129.429 136.879 161.528 1.00 113.92 ? 233 ILE D CB  1 
ATOM   4646  C  CG1 . ILE B 2 233 ? 129.815 135.413 161.739 1.00 113.92 ? 233 ILE D CG1 1 
ATOM   4647  C  CG2 . ILE B 2 233 ? 128.851 137.499 162.793 1.00 113.92 ? 233 ILE D CG2 1 
ATOM   4648  C  CD1 . ILE B 2 233 ? 130.882 135.203 162.781 1.00 113.92 ? 233 ILE D CD1 1 
ATOM   4649  N  N   . ASP B 2 234 ? 126.883 135.182 160.055 1.00 117.80 ? 234 ASP D N   1 
ATOM   4650  C  CA  . ASP B 2 234 ? 125.594 134.524 160.202 1.00 117.80 ? 234 ASP D CA  1 
ATOM   4651  C  C   . ASP B 2 234 ? 125.491 133.875 161.576 1.00 117.80 ? 234 ASP D C   1 
ATOM   4652  O  O   . ASP B 2 234 ? 126.421 133.904 162.386 1.00 117.80 ? 234 ASP D O   1 
ATOM   4653  C  CB  . ASP B 2 234 ? 125.378 133.456 159.131 1.00 117.80 ? 234 ASP D CB  1 
ATOM   4654  C  CG  . ASP B 2 234 ? 125.884 133.867 157.777 1.00 117.80 ? 234 ASP D CG  1 
ATOM   4655  O  OD1 . ASP B 2 234 ? 127.098 133.728 157.554 1.00 117.80 ? 234 ASP D OD1 1 
ATOM   4656  O  OD2 . ASP B 2 234 ? 125.071 134.275 156.922 1.00 117.80 ? 234 ASP D OD2 1 
ATOM   4657  N  N   . ASP B 2 235 ? 124.329 133.281 161.840 1.00 121.57 ? 235 ASP D N   1 
ATOM   4658  C  CA  . ASP B 2 235 ? 124.120 132.589 163.104 1.00 121.57 ? 235 ASP D CA  1 
ATOM   4659  C  C   . ASP B 2 235 ? 125.004 131.351 163.204 1.00 121.57 ? 235 ASP D C   1 
ATOM   4660  O  O   . ASP B 2 235 ? 125.661 131.119 164.228 1.00 121.57 ? 235 ASP D O   1 
ATOM   4661  C  CB  . ASP B 2 235 ? 122.650 132.207 163.230 1.00 121.57 ? 235 ASP D CB  1 
ATOM   4662  C  CG  . ASP B 2 235 ? 121.870 133.211 164.028 1.00 121.57 ? 235 ASP D CG  1 
ATOM   4663  O  OD1 . ASP B 2 235 ? 122.486 133.902 164.863 1.00 121.57 ? 235 ASP D OD1 1 
ATOM   4664  O  OD2 . ASP B 2 235 ? 120.644 133.303 163.824 1.00 121.57 ? 235 ASP D OD2 1 
ATOM   4665  N  N   . GLU B 2 236 ? 125.022 130.542 162.142 1.00 118.24 ? 236 GLU D N   1 
ATOM   4666  C  CA  . GLU B 2 236 ? 125.743 129.273 162.162 1.00 118.24 ? 236 GLU D CA  1 
ATOM   4667  C  C   . GLU B 2 236 ? 127.237 129.492 162.358 1.00 118.24 ? 236 GLU D C   1 
ATOM   4668  O  O   . GLU B 2 236 ? 127.874 128.813 163.172 1.00 118.24 ? 236 GLU D O   1 
ATOM   4669  C  CB  . GLU B 2 236 ? 125.476 128.501 160.870 1.00 118.24 ? 236 GLU D CB  1 
ATOM   4670  N  N   . SER B 2 237 ? 127.816 130.429 161.604 1.00 113.92 ? 237 SER D N   1 
ATOM   4671  C  CA  . SER B 2 237 ? 129.246 130.690 161.721 1.00 113.92 ? 237 SER D CA  1 
ATOM   4672  C  C   . SER B 2 237 ? 129.596 131.187 163.117 1.00 113.92 ? 237 SER D C   1 
ATOM   4673  O  O   . SER B 2 237 ? 130.583 130.740 163.715 1.00 113.92 ? 237 SER D O   1 
ATOM   4674  C  CB  . SER B 2 237 ? 129.682 131.705 160.664 1.00 113.92 ? 237 SER D CB  1 
ATOM   4675  O  OG  . SER B 2 237 ? 129.527 131.181 159.357 1.00 113.92 ? 237 SER D OG  1 
ATOM   4676  N  N   . TYR B 2 238 ? 128.797 132.111 163.653 1.00 113.92 ? 238 TYR D N   1 
ATOM   4677  C  CA  . TYR B 2 238 ? 129.078 132.644 164.980 1.00 113.92 ? 238 TYR D CA  1 
ATOM   4678  C  C   . TYR B 2 238 ? 129.011 131.550 166.037 1.00 113.92 ? 238 TYR D C   1 
ATOM   4679  O  O   . TYR B 2 238 ? 129.886 131.466 166.904 1.00 113.92 ? 238 TYR D O   1 
ATOM   4680  C  CB  . TYR B 2 238 ? 128.105 133.774 165.313 1.00 113.92 ? 238 TYR D CB  1 
ATOM   4681  C  CG  . TYR B 2 238 ? 128.604 134.718 166.385 1.00 113.92 ? 238 TYR D CG  1 
ATOM   4682  C  CD1 . TYR B 2 238 ? 128.512 134.383 167.729 1.00 113.92 ? 238 TYR D CD1 1 
ATOM   4683  C  CD2 . TYR B 2 238 ? 129.171 135.942 166.053 1.00 113.92 ? 238 TYR D CD2 1 
ATOM   4684  C  CE1 . TYR B 2 238 ? 128.967 135.239 168.713 1.00 113.92 ? 238 TYR D CE1 1 
ATOM   4685  C  CE2 . TYR B 2 238 ? 129.628 136.806 167.031 1.00 113.92 ? 238 TYR D CE2 1 
ATOM   4686  C  CZ  . TYR B 2 238 ? 129.524 136.449 168.358 1.00 113.92 ? 238 TYR D CZ  1 
ATOM   4687  O  OH  . TYR B 2 238 ? 129.976 137.306 169.335 1.00 113.92 ? 238 TYR D OH  1 
ATOM   4688  N  N   . GLY B 2 239 ? 127.996 130.686 165.969 1.00 115.65 ? 239 GLY D N   1 
ATOM   4689  C  CA  . GLY B 2 239 ? 127.902 129.603 166.938 1.00 115.65 ? 239 GLY D CA  1 
ATOM   4690  C  C   . GLY B 2 239 ? 129.031 128.597 166.812 1.00 115.65 ? 239 GLY D C   1 
ATOM   4691  O  O   . GLY B 2 239 ? 129.592 128.143 167.820 1.00 115.65 ? 239 GLY D O   1 
ATOM   4692  N  N   . GLN B 2 240 ? 129.374 128.226 165.572 1.00 117.57 ? 240 GLN D N   1 
ATOM   4693  C  CA  . GLN B 2 240 ? 130.414 127.232 165.342 1.00 117.57 ? 240 GLN D CA  1 
ATOM   4694  C  C   . GLN B 2 240 ? 131.798 127.763 165.694 1.00 117.57 ? 240 GLN D C   1 
ATOM   4695  O  O   . GLN B 2 240 ? 132.708 126.963 165.914 1.00 117.57 ? 240 GLN D O   1 
ATOM   4696  C  CB  . GLN B 2 240 ? 130.360 126.738 163.892 1.00 117.57 ? 240 GLN D CB  1 
ATOM   4697  C  CG  . GLN B 2 240 ? 131.370 127.355 162.951 1.00 117.57 ? 240 GLN D CG  1 
ATOM   4698  C  CD  . GLN B 2 240 ? 131.190 126.894 161.517 1.00 117.57 ? 240 GLN D CD  1 
ATOM   4699  O  OE1 . GLN B 2 240 ? 130.421 125.974 161.240 1.00 117.57 ? 240 GLN D OE1 1 
ATOM   4700  N  NE2 . GLN B 2 240 ? 131.904 127.531 160.599 1.00 117.57 ? 240 GLN D NE2 1 
ATOM   4701  N  N   . ILE B 2 241 ? 131.999 129.081 165.669 1.00 113.92 ? 241 ILE D N   1 
ATOM   4702  C  CA  . ILE B 2 241 ? 133.244 129.659 166.168 1.00 113.92 ? 241 ILE D CA  1 
ATOM   4703  C  C   . ILE B 2 241 ? 133.190 129.913 167.671 1.00 113.92 ? 241 ILE D C   1 
ATOM   4704  O  O   . ILE B 2 241 ? 134.234 129.882 168.337 1.00 113.92 ? 241 ILE D O   1 
ATOM   4705  C  CB  . ILE B 2 241 ? 133.603 130.944 165.392 1.00 109.97 ? 241 ILE D CB  1 
ATOM   4706  C  CG1 . ILE B 2 241 ? 134.507 130.602 164.211 1.00 109.97 ? 241 ILE D CG1 1 
ATOM   4707  C  CG2 . ILE B 2 241 ? 134.266 131.999 166.281 1.00 109.97 ? 241 ILE D CG2 1 
ATOM   4708  C  CD1 . ILE B 2 241 ? 133.918 129.657 163.255 1.00 109.97 ? 241 ILE D CD1 1 
ATOM   4709  N  N   . PHE B 2 242 ? 131.997 130.072 168.237 1.00 113.92 ? 242 PHE D N   1 
ATOM   4710  C  CA  . PHE B 2 242 ? 131.884 130.423 169.644 1.00 113.92 ? 242 PHE D CA  1 
ATOM   4711  C  C   . PHE B 2 242 ? 132.044 129.206 170.544 1.00 113.92 ? 242 PHE D C   1 
ATOM   4712  O  O   . PHE B 2 242 ? 132.802 129.248 171.519 1.00 113.92 ? 242 PHE D O   1 
ATOM   4713  C  CB  . PHE B 2 242 ? 130.542 131.114 169.885 1.00 113.92 ? 242 PHE D CB  1 
ATOM   4714  C  CG  . PHE B 2 242 ? 130.353 131.600 171.287 1.00 113.92 ? 242 PHE D CG  1 
ATOM   4715  C  CD1 . PHE B 2 242 ? 130.934 132.782 171.707 1.00 113.92 ? 242 PHE D CD1 1 
ATOM   4716  C  CD2 . PHE B 2 242 ? 129.579 130.883 172.182 1.00 113.92 ? 242 PHE D CD2 1 
ATOM   4717  C  CE1 . PHE B 2 242 ? 130.759 133.233 172.998 1.00 113.92 ? 242 PHE D CE1 1 
ATOM   4718  C  CE2 . PHE B 2 242 ? 129.399 131.330 173.473 1.00 113.92 ? 242 PHE D CE2 1 
ATOM   4719  C  CZ  . PHE B 2 242 ? 129.989 132.506 173.882 1.00 113.92 ? 242 PHE D CZ  1 
ATOM   4720  N  N   . LYS B 2 243 ? 131.342 128.112 170.240 1.00 113.92 ? 243 LYS D N   1 
ATOM   4721  C  CA  . LYS B 2 243 ? 131.403 126.953 171.131 1.00 113.92 ? 243 LYS D CA  1 
ATOM   4722  C  C   . LYS B 2 243 ? 132.810 126.376 171.273 1.00 113.92 ? 243 LYS D C   1 
ATOM   4723  O  O   . LYS B 2 243 ? 133.289 126.251 172.416 1.00 113.92 ? 243 LYS D O   1 
ATOM   4724  C  CB  . LYS B 2 243 ? 130.413 125.881 170.657 1.00 113.92 ? 243 LYS D CB  1 
ATOM   4725  C  CG  . LYS B 2 243 ? 130.391 124.635 171.532 1.00 113.92 ? 243 LYS D CG  1 
ATOM   4726  C  CD  . LYS B 2 243 ? 129.317 123.647 171.098 1.00 113.92 ? 243 LYS D CD  1 
ATOM   4727  C  CE  . LYS B 2 243 ? 127.920 124.131 171.439 1.00 113.92 ? 243 LYS D CE  1 
ATOM   4728  N  NZ  . LYS B 2 243 ? 126.916 123.040 171.297 1.00 113.92 ? 243 LYS D NZ  1 
ATOM   4729  N  N   . PRO B 2 244 ? 133.530 126.029 170.195 1.00 113.92 ? 244 PRO D N   1 
ATOM   4730  C  CA  . PRO B 2 244 ? 134.856 125.414 170.386 1.00 113.92 ? 244 PRO D CA  1 
ATOM   4731  C  C   . PRO B 2 244 ? 135.884 126.352 170.987 1.00 113.92 ? 244 PRO D C   1 
ATOM   4732  O  O   . PRO B 2 244 ? 136.687 125.919 171.820 1.00 113.92 ? 244 PRO D O   1 
ATOM   4733  C  CB  . PRO B 2 244 ? 135.253 124.975 168.970 1.00 113.92 ? 244 PRO D CB  1 
ATOM   4734  C  CG  . PRO B 2 244 ? 134.481 125.836 168.084 1.00 113.92 ? 244 PRO D CG  1 
ATOM   4735  C  CD  . PRO B 2 244 ? 133.177 126.092 168.768 1.00 113.92 ? 244 PRO D CD  1 
ATOM   4736  N  N   . ILE B 2 245 ? 135.909 127.616 170.560 1.00 113.92 ? 245 ILE D N   1 
ATOM   4737  C  CA  . ILE B 2 245 ? 136.878 128.564 171.106 1.00 113.92 ? 245 ILE D CA  1 
ATOM   4738  C  C   . ILE B 2 245 ? 136.681 128.713 172.609 1.00 113.92 ? 245 ILE D C   1 
ATOM   4739  O  O   . ILE B 2 245 ? 137.643 128.675 173.384 1.00 113.92 ? 245 ILE D O   1 
ATOM   4740  C  CB  . ILE B 2 245 ? 136.780 129.917 170.380 1.00 101.99 ? 245 ILE D CB  1 
ATOM   4741  C  CG1 . ILE B 2 245 ? 137.269 129.778 168.935 1.00 101.99 ? 245 ILE D CG1 1 
ATOM   4742  C  CG2 . ILE B 2 245 ? 137.562 130.986 171.131 1.00 101.99 ? 245 ILE D CG2 1 
ATOM   4743  C  CD1 . ILE B 2 245 ? 138.710 130.175 168.719 1.00 101.99 ? 245 ILE D CD1 1 
ATOM   4744  N  N   . ILE B 2 246 ? 135.430 128.883 173.042 1.00 113.92 ? 246 ILE D N   1 
ATOM   4745  C  CA  . ILE B 2 246 ? 135.158 129.053 174.465 1.00 113.92 ? 246 ILE D CA  1 
ATOM   4746  C  C   . ILE B 2 246 ? 135.512 127.783 175.229 1.00 113.92 ? 246 ILE D C   1 
ATOM   4747  O  O   . ILE B 2 246 ? 136.087 127.840 176.325 1.00 113.92 ? 246 ILE D O   1 
ATOM   4748  C  CB  . ILE B 2 246 ? 133.692 129.469 174.689 1.00 113.92 ? 246 ILE D CB  1 
ATOM   4749  C  CG1 . ILE B 2 246 ? 133.439 130.861 174.108 1.00 113.92 ? 246 ILE D CG1 1 
ATOM   4750  C  CG2 . ILE B 2 246 ? 133.341 129.442 176.168 1.00 113.92 ? 246 ILE D CG2 1 
ATOM   4751  C  CD1 . ILE B 2 246 ? 134.197 131.964 174.809 1.00 113.92 ? 246 ILE D CD1 1 
ATOM   4752  N  N   . SER B 2 247 ? 135.180 126.617 174.667 1.00 113.92 ? 247 SER D N   1 
ATOM   4753  C  CA  . SER B 2 247 ? 135.504 125.362 175.339 1.00 113.92 ? 247 SER D CA  1 
ATOM   4754  C  C   . SER B 2 247 ? 137.012 125.204 175.510 1.00 113.92 ? 247 SER D C   1 
ATOM   4755  O  O   . SER B 2 247 ? 137.493 124.839 176.589 1.00 113.92 ? 247 SER D O   1 
ATOM   4756  C  CB  . SER B 2 247 ? 134.930 124.185 174.549 1.00 113.92 ? 247 SER D CB  1 
ATOM   4757  O  OG  . SER B 2 247 ? 133.522 124.284 174.428 1.00 113.92 ? 247 SER D OG  1 
ATOM   4758  N  N   . LYS B 2 248 ? 137.773 125.486 174.449 1.00 113.92 ? 248 LYS D N   1 
ATOM   4759  C  CA  . LYS B 2 248 ? 139.227 125.384 174.513 1.00 113.92 ? 248 LYS D CA  1 
ATOM   4760  C  C   . LYS B 2 248 ? 139.814 126.381 175.504 1.00 113.92 ? 248 LYS D C   1 
ATOM   4761  O  O   . LYS B 2 248 ? 140.725 126.044 176.273 1.00 113.92 ? 248 LYS D O   1 
ATOM   4762  C  CB  . LYS B 2 248 ? 139.807 125.607 173.116 1.00 108.99 ? 248 LYS D CB  1 
ATOM   4763  C  CG  . LYS B 2 248 ? 141.314 125.467 172.984 1.00 108.99 ? 248 LYS D CG  1 
ATOM   4764  C  CD  . LYS B 2 248 ? 141.813 124.087 173.361 1.00 108.99 ? 248 LYS D CD  1 
ATOM   4765  C  CE  . LYS B 2 248 ? 143.106 123.776 172.620 1.00 108.99 ? 248 LYS D CE  1 
ATOM   4766  N  NZ  . LYS B 2 248 ? 144.321 124.041 173.432 1.00 108.99 ? 248 LYS D NZ  1 
ATOM   4767  N  N   . VAL B 2 249 ? 139.295 127.612 175.507 1.00 113.92 ? 249 VAL D N   1 
ATOM   4768  C  CA  . VAL B 2 249 ? 139.784 128.628 176.434 1.00 113.92 ? 249 VAL D CA  1 
ATOM   4769  C  C   . VAL B 2 249 ? 139.559 128.188 177.872 1.00 113.92 ? 249 VAL D C   1 
ATOM   4770  O  O   . VAL B 2 249 ? 140.457 128.282 178.717 1.00 113.92 ? 249 VAL D O   1 
ATOM   4771  C  CB  . VAL B 2 249 ? 139.104 129.980 176.149 1.00 113.92 ? 249 VAL D CB  1 
ATOM   4772  C  CG1 . VAL B 2 249 ? 139.278 130.922 177.325 1.00 113.92 ? 249 VAL D CG1 1 
ATOM   4773  C  CG2 . VAL B 2 249 ? 139.674 130.602 174.889 1.00 113.92 ? 249 VAL D CG2 1 
ATOM   4774  N  N   . MET B 2 250 ? 138.358 127.690 178.171 1.00 115.75 ? 250 MET D N   1 
ATOM   4775  C  CA  . MET B 2 250 ? 138.087 127.251 179.535 1.00 115.75 ? 250 MET D CA  1 
ATOM   4776  C  C   . MET B 2 250 ? 138.944 126.049 179.911 1.00 115.75 ? 250 MET D C   1 
ATOM   4777  O  O   . MET B 2 250 ? 139.438 125.966 181.040 1.00 115.75 ? 250 MET D O   1 
ATOM   4778  C  CB  . MET B 2 250 ? 136.612 126.945 179.734 1.00 115.75 ? 250 MET D CB  1 
ATOM   4779  C  CG  . MET B 2 250 ? 135.729 128.179 179.713 1.00 115.75 ? 250 MET D CG  1 
ATOM   4780  S  SD  . MET B 2 250 ? 134.274 127.946 180.735 1.00 115.75 ? 250 MET D SD  1 
ATOM   4781  C  CE  . MET B 2 250 ? 134.250 126.165 180.837 1.00 115.75 ? 250 MET D CE  1 
ATOM   4782  N  N   . GLU B 2 251 ? 139.126 125.105 178.980 1.00 117.96 ? 251 GLU D N   1 
ATOM   4783  C  CA  . GLU B 2 251 ? 139.931 123.924 179.274 1.00 117.96 ? 251 GLU D CA  1 
ATOM   4784  C  C   . GLU B 2 251 ? 141.364 124.315 179.600 1.00 117.96 ? 251 GLU D C   1 
ATOM   4785  O  O   . GLU B 2 251 ? 141.990 123.724 180.486 1.00 117.96 ? 251 GLU D O   1 
ATOM   4786  C  CB  . GLU B 2 251 ? 139.894 122.953 178.094 1.00 117.96 ? 251 GLU D CB  1 
ATOM   4787  N  N   . MET B 2 252 ? 141.914 125.277 178.864 1.00 126.03 ? 252 MET D N   1 
ATOM   4788  C  CA  . MET B 2 252 ? 143.288 125.692 179.107 1.00 126.03 ? 252 MET D CA  1 
ATOM   4789  C  C   . MET B 2 252 ? 143.411 126.674 180.267 1.00 126.03 ? 252 MET D C   1 
ATOM   4790  O  O   . MET B 2 252 ? 144.522 126.882 180.767 1.00 126.03 ? 252 MET D O   1 
ATOM   4791  C  CB  . MET B 2 252 ? 143.895 126.283 177.834 1.00 126.03 ? 252 MET D CB  1 
ATOM   4792  C  CG  . MET B 2 252 ? 144.096 125.238 176.755 1.00 126.03 ? 252 MET D CG  1 
ATOM   4793  S  SD  . MET B 2 252 ? 145.161 123.925 177.389 1.00 126.03 ? 252 MET D SD  1 
ATOM   4794  C  CE  . MET B 2 252 ? 144.868 122.612 176.211 1.00 126.03 ? 252 MET D CE  1 
ATOM   4795  N  N   . TYR B 2 253 ? 142.307 127.282 180.705 1.00 113.92 ? 253 TYR D N   1 
ATOM   4796  C  CA  . TYR B 2 253 ? 142.360 128.359 181.685 1.00 113.92 ? 253 TYR D CA  1 
ATOM   4797  C  C   . TYR B 2 253 ? 141.672 128.067 183.013 1.00 113.92 ? 253 TYR D C   1 
ATOM   4798  O  O   . TYR B 2 253 ? 142.068 128.656 184.020 1.00 113.92 ? 253 TYR D O   1 
ATOM   4799  C  CB  . TYR B 2 253 ? 141.744 129.634 181.090 1.00 113.92 ? 253 TYR D CB  1 
ATOM   4800  C  CG  . TYR B 2 253 ? 141.869 130.859 181.967 1.00 113.92 ? 253 TYR D CG  1 
ATOM   4801  C  CD1 . TYR B 2 253 ? 143.112 131.319 182.379 1.00 113.92 ? 253 TYR D CD1 1 
ATOM   4802  C  CD2 . TYR B 2 253 ? 140.744 131.574 182.356 1.00 113.92 ? 253 TYR D CD2 1 
ATOM   4803  C  CE1 . TYR B 2 253 ? 143.229 132.443 183.171 1.00 113.92 ? 253 TYR D CE1 1 
ATOM   4804  C  CE2 . TYR B 2 253 ? 140.852 132.700 183.147 1.00 113.92 ? 253 TYR D CE2 1 
ATOM   4805  C  CZ  . TYR B 2 253 ? 142.097 133.130 183.550 1.00 113.92 ? 253 TYR D CZ  1 
ATOM   4806  O  OH  . TYR B 2 253 ? 142.209 134.251 184.339 1.00 113.92 ? 253 TYR D OH  1 
ATOM   4807  N  N   . GLN B 2 254 ? 140.674 127.174 183.054 1.00 116.07 ? 254 GLN D N   1 
ATOM   4808  C  CA  . GLN B 2 254 ? 139.945 126.874 184.288 1.00 116.07 ? 254 GLN D CA  1 
ATOM   4809  C  C   . GLN B 2 254 ? 139.362 128.141 184.907 1.00 116.07 ? 254 GLN D C   1 
ATOM   4810  O  O   . GLN B 2 254 ? 139.782 128.538 186.001 1.00 116.07 ? 254 GLN D O   1 
ATOM   4811  C  CB  . GLN B 2 254 ? 140.842 126.181 185.323 1.00 116.07 ? 254 GLN D CB  1 
ATOM   4812  C  CG  . GLN B 2 254 ? 141.596 124.913 184.902 1.00 116.07 ? 254 GLN D CG  1 
ATOM   4813  C  CD  . GLN B 2 254 ? 140.866 124.057 183.884 1.00 116.07 ? 254 GLN D CD  1 
ATOM   4814  O  OE1 . GLN B 2 254 ? 140.748 124.417 182.719 1.00 116.07 ? 254 GLN D OE1 1 
ATOM   4815  N  NE2 . GLN B 2 254 ? 140.366 122.911 184.331 1.00 116.07 ? 254 GLN D NE2 1 
ATOM   4816  N  N   . PRO B 2 255 ? 138.408 128.806 184.256 1.00 113.92 ? 255 PRO D N   1 
ATOM   4817  C  CA  . PRO B 2 255 ? 137.810 130.001 184.862 1.00 113.92 ? 255 PRO D CA  1 
ATOM   4818  C  C   . PRO B 2 255 ? 136.969 129.650 186.078 1.00 113.92 ? 255 PRO D C   1 
ATOM   4819  O  O   . PRO B 2 255 ? 136.443 128.541 186.204 1.00 113.92 ? 255 PRO D O   1 
ATOM   4820  C  CB  . PRO B 2 255 ? 136.940 130.580 183.738 1.00 113.92 ? 255 PRO D CB  1 
ATOM   4821  C  CG  . PRO B 2 255 ? 137.359 129.867 182.491 1.00 113.92 ? 255 PRO D CG  1 
ATOM   4822  C  CD  . PRO B 2 255 ? 137.841 128.527 182.928 1.00 113.92 ? 255 PRO D CD  1 
ATOM   4823  N  N   . SER B 2 256 ? 136.846 130.619 186.984 1.00 113.92 ? 256 SER D N   1 
ATOM   4824  C  CA  . SER B 2 256 ? 136.036 130.450 188.183 1.00 113.92 ? 256 SER D CA  1 
ATOM   4825  C  C   . SER B 2 256 ? 134.693 131.159 188.101 1.00 113.92 ? 256 SER D C   1 
ATOM   4826  O  O   . SER B 2 256 ? 133.718 130.686 188.694 1.00 113.92 ? 256 SER D O   1 
ATOM   4827  C  CB  . SER B 2 256 ? 136.798 130.956 189.413 1.00 103.90 ? 256 SER D CB  1 
ATOM   4828  O  OG  . SER B 2 256 ? 137.865 130.084 189.745 1.00 103.90 ? 256 SER D OG  1 
ATOM   4829  N  N   . ALA B 2 257 ? 134.617 132.276 187.381 1.00 113.92 ? 257 ALA D N   1 
ATOM   4830  C  CA  . ALA B 2 257 ? 133.372 133.029 187.253 1.00 113.92 ? 257 ALA D CA  1 
ATOM   4831  C  C   . ALA B 2 257 ? 133.455 133.853 185.981 1.00 113.92 ? 257 ALA D C   1 
ATOM   4832  O  O   . ALA B 2 257 ? 134.305 134.743 185.880 1.00 113.92 ? 257 ALA D O   1 
ATOM   4833  C  CB  . ALA B 2 257 ? 133.141 133.924 188.469 1.00 113.92 ? 257 ALA D CB  1 
ATOM   4834  N  N   . VAL B 2 258 ? 132.590 133.561 185.014 1.00 113.92 ? 258 VAL D N   1 
ATOM   4835  C  CA  . VAL B 2 258 ? 132.654 134.175 183.695 1.00 113.92 ? 258 VAL D CA  1 
ATOM   4836  C  C   . VAL B 2 258 ? 131.685 135.350 183.619 1.00 113.92 ? 258 VAL D C   1 
ATOM   4837  O  O   . VAL B 2 258 ? 130.570 135.309 184.167 1.00 113.92 ? 258 VAL D O   1 
ATOM   4838  C  CB  . VAL B 2 258 ? 132.386 133.129 182.593 1.00 113.92 ? 258 VAL D CB  1 
ATOM   4839  C  CG1 . VAL B 2 258 ? 131.105 132.373 182.865 1.00 113.92 ? 258 VAL D CG1 1 
ATOM   4840  C  CG2 . VAL B 2 258 ? 132.344 133.783 181.224 1.00 113.92 ? 258 VAL D CG2 1 
ATOM   4841  N  N   . VAL B 2 259 ? 132.122 136.405 182.937 1.00 113.92 ? 259 VAL D N   1 
ATOM   4842  C  CA  . VAL B 2 259 ? 131.351 137.628 182.752 1.00 113.92 ? 259 VAL D CA  1 
ATOM   4843  C  C   . VAL B 2 259 ? 131.037 137.750 181.268 1.00 113.92 ? 259 VAL D C   1 
ATOM   4844  O  O   . VAL B 2 259 ? 131.923 138.053 180.459 1.00 113.92 ? 259 VAL D O   1 
ATOM   4845  C  CB  . VAL B 2 259 ? 132.112 138.858 183.261 1.00 113.92 ? 259 VAL D CB  1 
ATOM   4846  C  CG1 . VAL B 2 259 ? 131.371 140.124 182.900 1.00 113.92 ? 259 VAL D CG1 1 
ATOM   4847  C  CG2 . VAL B 2 259 ? 132.319 138.768 184.762 1.00 113.92 ? 259 VAL D CG2 1 
ATOM   4848  N  N   . LEU B 2 260 ? 129.783 137.503 180.904 1.00 113.92 ? 260 LEU D N   1 
ATOM   4849  C  CA  . LEU B 2 260 ? 129.318 137.590 179.529 1.00 113.92 ? 260 LEU D CA  1 
ATOM   4850  C  C   . LEU B 2 260 ? 128.675 138.954 179.306 1.00 113.92 ? 260 LEU D C   1 
ATOM   4851  O  O   . LEU B 2 260 ? 127.687 139.302 179.971 1.00 113.92 ? 260 LEU D O   1 
ATOM   4852  C  CB  . LEU B 2 260 ? 128.319 136.469 179.239 1.00 113.92 ? 260 LEU D CB  1 
ATOM   4853  C  CG  . LEU B 2 260 ? 127.912 136.190 177.795 1.00 113.92 ? 260 LEU D CG  1 
ATOM   4854  C  CD1 . LEU B 2 260 ? 129.097 135.654 177.036 1.00 113.92 ? 260 LEU D CD1 1 
ATOM   4855  C  CD2 . LEU B 2 260 ? 126.762 135.199 177.751 1.00 113.92 ? 260 LEU D CD2 1 
ATOM   4856  N  N   . GLN B 2 261 ? 129.246 139.735 178.394 1.00 113.92 ? 261 GLN D N   1 
ATOM   4857  C  CA  . GLN B 2 261 ? 128.657 141.007 177.995 1.00 113.92 ? 261 GLN D CA  1 
ATOM   4858  C  C   . GLN B 2 261 ? 127.962 140.765 176.665 1.00 113.92 ? 261 GLN D C   1 
ATOM   4859  O  O   . GLN B 2 261 ? 128.615 140.586 175.634 1.00 113.92 ? 261 GLN D O   1 
ATOM   4860  C  CB  . GLN B 2 261 ? 129.703 142.115 177.909 1.00 113.92 ? 261 GLN D CB  1 
ATOM   4861  C  CG  . GLN B 2 261 ? 129.127 143.512 177.639 1.00 113.92 ? 261 GLN D CG  1 
ATOM   4862  C  CD  . GLN B 2 261 ? 129.127 143.932 176.177 1.00 113.92 ? 261 GLN D CD  1 
ATOM   4863  O  OE1 . GLN B 2 261 ? 129.227 143.108 175.274 1.00 113.92 ? 261 GLN D OE1 1 
ATOM   4864  N  NE2 . GLN B 2 261 ? 129.014 145.235 175.945 1.00 113.92 ? 261 GLN D NE2 1 
ATOM   4865  N  N   . CYS B 2 262 ? 126.636 140.690 176.714 1.00 113.92 ? 262 CYS D N   1 
ATOM   4866  C  CA  . CYS B 2 262 ? 125.811 140.498 175.533 1.00 113.92 ? 262 CYS D CA  1 
ATOM   4867  C  C   . CYS B 2 262 ? 125.419 141.859 174.982 1.00 113.92 ? 262 CYS D C   1 
ATOM   4868  O  O   . CYS B 2 262 ? 124.875 142.696 175.709 1.00 113.92 ? 262 CYS D O   1 
ATOM   4869  C  CB  . CYS B 2 262 ? 124.565 139.676 175.859 1.00 113.92 ? 262 CYS D CB  1 
ATOM   4870  S  SG  . CYS B 2 262 ? 124.924 138.076 176.591 1.00 113.92 ? 262 CYS D SG  1 
ATOM   4871  N  N   . GLY B 2 263 ? 125.706 142.084 173.709 1.00 113.92 ? 263 GLY D N   1 
ATOM   4872  C  CA  . GLY B 2 263 ? 125.333 143.335 173.092 1.00 113.92 ? 263 GLY D CA  1 
ATOM   4873  C  C   . GLY B 2 263 ? 124.327 143.109 171.989 1.00 113.92 ? 263 GLY D C   1 
ATOM   4874  O  O   . GLY B 2 263 ? 124.656 142.540 170.944 1.00 113.92 ? 263 GLY D O   1 
ATOM   4875  N  N   . ALA B 2 264 ? 123.090 143.550 172.216 1.00 113.92 ? 264 ALA D N   1 
ATOM   4876  C  CA  . ALA B 2 264 ? 122.036 143.356 171.232 1.00 113.92 ? 264 ALA D CA  1 
ATOM   4877  C  C   . ALA B 2 264 ? 122.298 144.122 169.945 1.00 113.92 ? 264 ALA D C   1 
ATOM   4878  O  O   . ALA B 2 264 ? 121.626 143.862 168.941 1.00 113.92 ? 264 ALA D O   1 
ATOM   4879  C  CB  . ALA B 2 264 ? 120.687 143.758 171.821 1.00 113.92 ? 264 ALA D CB  1 
ATOM   4880  N  N   . ASP B 2 265 ? 123.253 145.055 169.949 1.00 113.92 ? 265 ASP D N   1 
ATOM   4881  C  CA  . ASP B 2 265 ? 123.699 145.686 168.713 1.00 113.92 ? 265 ASP D CA  1 
ATOM   4882  C  C   . ASP B 2 265 ? 124.333 144.689 167.754 1.00 113.92 ? 265 ASP D C   1 
ATOM   4883  O  O   . ASP B 2 265 ? 124.647 145.058 166.617 1.00 113.92 ? 265 ASP D O   1 
ATOM   4884  C  CB  . ASP B 2 265 ? 124.674 146.823 169.028 1.00 100.38 ? 265 ASP D CB  1 
ATOM   4885  C  CG  . ASP B 2 265 ? 125.758 146.408 169.996 1.00 100.38 ? 265 ASP D CG  1 
ATOM   4886  O  OD1 . ASP B 2 265 ? 125.758 145.234 170.416 1.00 100.38 ? 265 ASP D OD1 1 
ATOM   4887  O  OD2 . ASP B 2 265 ? 126.605 147.256 170.345 1.00 100.38 ? 265 ASP D OD2 1 
ATOM   4888  N  N   . SER B 2 266 ? 124.527 143.443 168.187 1.00 113.92 ? 266 SER D N   1 
ATOM   4889  C  CA  . SER B 2 266 ? 124.988 142.365 167.327 1.00 113.92 ? 266 SER D CA  1 
ATOM   4890  C  C   . SER B 2 266 ? 123.860 141.757 166.506 1.00 113.92 ? 266 SER D C   1 
ATOM   4891  O  O   . SER B 2 266 ? 124.127 140.928 165.632 1.00 113.92 ? 266 SER D O   1 
ATOM   4892  C  CB  . SER B 2 266 ? 125.657 141.274 168.165 1.00 113.92 ? 266 SER D CB  1 
ATOM   4893  O  OG  . SER B 2 266 ? 126.563 141.834 169.098 1.00 113.92 ? 266 SER D OG  1 
ATOM   4894  N  N   . LEU B 2 267 ? 122.612 142.118 166.785 1.00 113.92 ? 267 LEU D N   1 
ATOM   4895  C  CA  . LEU B 2 267 ? 121.490 141.550 166.061 1.00 113.92 ? 267 LEU D CA  1 
ATOM   4896  C  C   . LEU B 2 267 ? 121.390 142.150 164.663 1.00 113.92 ? 267 LEU D C   1 
ATOM   4897  O  O   . LEU B 2 267 ? 121.895 143.240 164.385 1.00 113.92 ? 267 LEU D O   1 
ATOM   4898  C  CB  . LEU B 2 267 ? 120.186 141.783 166.818 1.00 113.92 ? 267 LEU D CB  1 
ATOM   4899  C  CG  . LEU B 2 267 ? 119.662 140.567 167.575 1.00 113.92 ? 267 LEU D CG  1 
ATOM   4900  C  CD1 . LEU B 2 267 ? 120.446 140.391 168.856 1.00 113.92 ? 267 LEU D CD1 1 
ATOM   4901  C  CD2 . LEU B 2 267 ? 118.180 140.717 167.857 1.00 113.92 ? 267 LEU D CD2 1 
ATOM   4902  N  N   . SER B 2 268 ? 120.722 141.417 163.778 1.00 113.92 ? 268 SER D N   1 
ATOM   4903  C  CA  . SER B 2 268 ? 120.495 141.905 162.427 1.00 113.92 ? 268 SER D CA  1 
ATOM   4904  C  C   . SER B 2 268 ? 119.468 143.029 162.431 1.00 113.92 ? 268 SER D C   1 
ATOM   4905  O  O   . SER B 2 268 ? 118.428 142.942 163.089 1.00 113.92 ? 268 SER D O   1 
ATOM   4906  C  CB  . SER B 2 268 ? 120.021 140.768 161.523 1.00 113.92 ? 268 SER D CB  1 
ATOM   4907  O  OG  . SER B 2 268 ? 120.132 141.126 160.157 1.00 113.92 ? 268 SER D OG  1 
ATOM   4908  N  N   . GLY B 2 269 ? 119.764 144.091 161.689 1.00 113.92 ? 269 GLY D N   1 
ATOM   4909  C  CA  . GLY B 2 269 ? 118.871 145.224 161.617 1.00 113.92 ? 269 GLY D CA  1 
ATOM   4910  C  C   . GLY B 2 269 ? 119.099 146.308 162.644 1.00 113.92 ? 269 GLY D C   1 
ATOM   4911  O  O   . GLY B 2 269 ? 118.269 147.221 162.744 1.00 113.92 ? 269 GLY D O   1 
ATOM   4912  N  N   . ASP B 2 270 ? 120.180 146.240 163.420 1.00 111.43 ? 270 ASP D N   1 
ATOM   4913  C  CA  . ASP B 2 270 ? 120.443 147.291 164.391 1.00 111.43 ? 270 ASP D CA  1 
ATOM   4914  C  C   . ASP B 2 270 ? 120.765 148.601 163.682 1.00 111.43 ? 270 ASP D C   1 
ATOM   4915  O  O   . ASP B 2 270 ? 121.296 148.623 162.568 1.00 111.43 ? 270 ASP D O   1 
ATOM   4916  C  CB  . ASP B 2 270 ? 121.573 146.895 165.346 1.00 111.43 ? 270 ASP D CB  1 
ATOM   4917  C  CG  . ASP B 2 270 ? 121.875 147.978 166.383 1.00 111.43 ? 270 ASP D CG  1 
ATOM   4918  O  OD1 . ASP B 2 270 ? 122.186 149.129 166.010 1.00 111.43 ? 270 ASP D OD1 1 
ATOM   4919  O  OD2 . ASP B 2 270 ? 121.734 147.693 167.587 1.00 111.43 ? 270 ASP D OD2 1 
ATOM   4920  N  N   . ARG B 2 271 ? 120.431 149.705 164.352 1.00 109.66 ? 271 ARG D N   1 
ATOM   4921  C  CA  . ARG B 2 271 ? 120.572 151.035 163.780 1.00 109.66 ? 271 ARG D CA  1 
ATOM   4922  C  C   . ARG B 2 271 ? 122.007 151.544 163.796 1.00 109.66 ? 271 ARG D C   1 
ATOM   4923  O  O   . ARG B 2 271 ? 122.269 152.617 163.242 1.00 109.66 ? 271 ARG D O   1 
ATOM   4924  C  CB  . ARG B 2 271 ? 119.664 152.010 164.530 1.00 109.66 ? 271 ARG D CB  1 
ATOM   4925  C  CG  . ARG B 2 271 ? 119.169 153.170 163.693 1.00 109.66 ? 271 ARG D CG  1 
ATOM   4926  C  CD  . ARG B 2 271 ? 118.022 153.879 164.389 1.00 109.66 ? 271 ARG D CD  1 
ATOM   4927  N  NE  . ARG B 2 271 ? 116.822 153.055 164.462 1.00 109.66 ? 271 ARG D NE  1 
ATOM   4928  C  CZ  . ARG B 2 271 ? 115.831 153.255 165.320 1.00 109.66 ? 271 ARG D CZ  1 
ATOM   4929  N  NH1 . ARG B 2 271 ? 115.879 154.227 166.215 1.00 109.66 ? 271 ARG D NH1 1 
ATOM   4930  N  NH2 . ARG B 2 271 ? 114.772 152.451 165.287 1.00 109.66 ? 271 ARG D NH2 1 
ATOM   4931  N  N   . LEU B 2 272 ? 122.927 150.838 164.446 1.00 113.92 ? 272 LEU D N   1 
ATOM   4932  C  CA  . LEU B 2 272 ? 124.347 151.163 164.379 1.00 113.92 ? 272 LEU D CA  1 
ATOM   4933  C  C   . LEU B 2 272 ? 125.204 150.005 163.894 1.00 113.92 ? 272 LEU D C   1 
ATOM   4934  O  O   . LEU B 2 272 ? 126.137 150.221 163.117 1.00 113.92 ? 272 LEU D O   1 
ATOM   4935  C  CB  . LEU B 2 272 ? 124.865 151.668 165.731 1.00 113.92 ? 272 LEU D CB  1 
ATOM   4936  C  CG  . LEU B 2 272 ? 124.820 153.196 165.848 1.00 113.92 ? 272 LEU D CG  1 
ATOM   4937  C  CD1 . LEU B 2 272 ? 125.504 153.691 167.112 1.00 113.92 ? 272 LEU D CD1 1 
ATOM   4938  C  CD2 . LEU B 2 272 ? 125.440 153.840 164.618 1.00 113.92 ? 272 LEU D CD2 1 
ATOM   4939  N  N   . GLY B 2 273 ? 124.925 148.779 164.337 1.00 113.92 ? 273 GLY D N   1 
ATOM   4940  C  CA  . GLY B 2 273 ? 125.768 147.648 164.016 1.00 113.92 ? 273 GLY D CA  1 
ATOM   4941  C  C   . GLY B 2 273 ? 125.533 147.113 162.615 1.00 113.92 ? 273 GLY D C   1 
ATOM   4942  O  O   . GLY B 2 273 ? 124.680 147.582 161.862 1.00 113.92 ? 273 GLY D O   1 
ATOM   4943  N  N   . CYS B 2 274 ? 126.327 146.093 162.263 1.00 113.92 ? 274 CYS D N   1 
ATOM   4944  C  CA  . CYS B 2 274 ? 126.237 145.470 160.948 1.00 113.92 ? 274 CYS D CA  1 
ATOM   4945  C  C   . CYS B 2 274 ? 126.338 143.947 161.006 1.00 113.92 ? 274 CYS D C   1 
ATOM   4946  O  O   . CYS B 2 274 ? 126.635 143.318 159.984 1.00 113.92 ? 274 CYS D O   1 
ATOM   4947  C  CB  . CYS B 2 274 ? 127.323 146.016 160.014 1.00 113.92 ? 274 CYS D CB  1 
ATOM   4948  S  SG  . CYS B 2 274 ? 128.976 146.058 160.739 1.00 113.92 ? 274 CYS D SG  1 
ATOM   4949  N  N   . PHE B 2 275 ? 126.102 143.337 162.165 1.00 113.92 ? 275 PHE D N   1 
ATOM   4950  C  CA  . PHE B 2 275 ? 126.060 141.886 162.248 1.00 113.92 ? 275 PHE D CA  1 
ATOM   4951  C  C   . PHE B 2 275 ? 124.685 141.364 161.842 1.00 113.92 ? 275 PHE D C   1 
ATOM   4952  O  O   . PHE B 2 275 ? 123.697 142.102 161.792 1.00 113.92 ? 275 PHE D O   1 
ATOM   4953  C  CB  . PHE B 2 275 ? 126.399 141.408 163.660 1.00 113.92 ? 275 PHE D CB  1 
ATOM   4954  C  CG  . PHE B 2 275 ? 127.870 141.269 163.925 1.00 113.92 ? 275 PHE D CG  1 
ATOM   4955  C  CD1 . PHE B 2 275 ? 128.801 141.586 162.953 1.00 113.92 ? 275 PHE D CD1 1 
ATOM   4956  C  CD2 . PHE B 2 275 ? 128.320 140.812 165.152 1.00 113.92 ? 275 PHE D CD2 1 
ATOM   4957  C  CE1 . PHE B 2 275 ? 130.155 141.454 163.202 1.00 113.92 ? 275 PHE D CE1 1 
ATOM   4958  C  CE2 . PHE B 2 275 ? 129.670 140.678 165.406 1.00 113.92 ? 275 PHE D CE2 1 
ATOM   4959  C  CZ  . PHE B 2 275 ? 130.588 140.999 164.430 1.00 113.92 ? 275 PHE D CZ  1 
ATOM   4960  N  N   . ASN B 2 276 ? 124.633 140.063 161.548 1.00 113.92 ? 276 ASN D N   1 
ATOM   4961  C  CA  . ASN B 2 276 ? 123.429 139.426 161.026 1.00 113.92 ? 276 ASN D CA  1 
ATOM   4962  C  C   . ASN B 2 276 ? 122.865 138.379 161.981 1.00 113.92 ? 276 ASN D C   1 
ATOM   4963  O  O   . ASN B 2 276 ? 122.094 137.512 161.558 1.00 113.92 ? 276 ASN D O   1 
ATOM   4964  C  CB  . ASN B 2 276 ? 123.721 138.799 159.661 1.00 113.92 ? 276 ASN D CB  1 
ATOM   4965  C  CG  . ASN B 2 276 ? 122.489 138.698 158.787 1.00 113.92 ? 276 ASN D CG  1 
ATOM   4966  O  OD1 . ASN B 2 276 ? 121.430 139.226 159.122 1.00 113.92 ? 276 ASN D OD1 1 
ATOM   4967  N  ND2 . ASN B 2 276 ? 122.622 138.019 157.654 1.00 113.92 ? 276 ASN D ND2 1 
ATOM   4968  N  N   . LEU B 2 277 ? 123.236 138.433 163.257 1.00 113.92 ? 277 LEU D N   1 
ATOM   4969  C  CA  . LEU B 2 277 ? 122.723 137.474 164.227 1.00 113.92 ? 277 LEU D CA  1 
ATOM   4970  C  C   . LEU B 2 277 ? 121.227 137.662 164.449 1.00 113.92 ? 277 LEU D C   1 
ATOM   4971  O  O   . LEU B 2 277 ? 120.721 138.787 164.477 1.00 113.92 ? 277 LEU D O   1 
ATOM   4972  C  CB  . LEU B 2 277 ? 123.461 137.615 165.560 1.00 113.92 ? 277 LEU D CB  1 
ATOM   4973  C  CG  . LEU B 2 277 ? 124.821 136.937 165.735 1.00 113.92 ? 277 LEU D CG  1 
ATOM   4974  C  CD1 . LEU B 2 277 ? 125.879 137.572 164.853 1.00 113.92 ? 277 LEU D CD1 1 
ATOM   4975  C  CD2 . LEU B 2 277 ? 125.247 136.987 167.193 1.00 113.92 ? 277 LEU D CD2 1 
ATOM   4976  N  N   . THR B 2 278 ? 120.521 136.548 164.604 1.00 113.92 ? 278 THR D N   1 
ATOM   4977  C  CA  . THR B 2 278 ? 119.117 136.545 164.983 1.00 113.92 ? 278 THR D CA  1 
ATOM   4978  C  C   . THR B 2 278 ? 118.988 136.345 166.490 1.00 113.92 ? 278 THR D C   1 
ATOM   4979  O  O   . THR B 2 278 ? 119.970 136.127 167.203 1.00 113.92 ? 278 THR D O   1 
ATOM   4980  C  CB  . THR B 2 278 ? 118.342 135.461 164.233 1.00 113.92 ? 278 THR D CB  1 
ATOM   4981  O  OG1 . THR B 2 278 ? 118.839 134.172 164.607 1.00 113.92 ? 278 THR D OG1 1 
ATOM   4982  C  CG2 . THR B 2 278 ? 118.499 135.642 162.733 1.00 113.92 ? 278 THR D CG2 1 
ATOM   4983  N  N   . VAL B 2 279 ? 117.747 136.436 166.970 1.00 113.92 ? 279 VAL D N   1 
ATOM   4984  C  CA  . VAL B 2 279 ? 117.471 136.215 168.389 1.00 113.92 ? 279 VAL D CA  1 
ATOM   4985  C  C   . VAL B 2 279 ? 117.856 134.797 168.803 1.00 113.92 ? 279 VAL D C   1 
ATOM   4986  O  O   . VAL B 2 279 ? 118.499 134.587 169.841 1.00 113.92 ? 279 VAL D O   1 
ATOM   4987  C  CB  . VAL B 2 279 ? 115.993 136.517 168.691 1.00 113.92 ? 279 VAL D CB  1 
ATOM   4988  C  CG1 . VAL B 2 279 ? 115.639 136.067 170.083 1.00 113.92 ? 279 VAL D CG1 1 
ATOM   4989  C  CG2 . VAL B 2 279 ? 115.719 138.005 168.533 1.00 113.92 ? 279 VAL D CG2 1 
ATOM   4990  N  N   . LYS B 2 280 ? 117.477 133.802 167.993 1.00 122.83 ? 280 LYS D N   1 
ATOM   4991  C  CA  . LYS B 2 280 ? 117.863 132.420 168.275 1.00 122.83 ? 280 LYS D CA  1 
ATOM   4992  C  C   . LYS B 2 280 ? 119.375 132.262 168.326 1.00 122.83 ? 280 LYS D C   1 
ATOM   4993  O  O   . LYS B 2 280 ? 119.914 131.619 169.234 1.00 122.83 ? 280 LYS D O   1 
ATOM   4994  C  CB  . LYS B 2 280 ? 117.264 131.482 167.224 1.00 122.83 ? 280 LYS D CB  1 
ATOM   4995  C  CG  . LYS B 2 280 ? 115.842 131.025 167.498 1.00 122.83 ? 280 LYS D CG  1 
ATOM   4996  C  CD  . LYS B 2 280 ? 115.598 130.813 168.988 1.00 122.83 ? 280 LYS D CD  1 
ATOM   4997  C  CE  . LYS B 2 280 ? 116.335 129.575 169.502 1.00 122.83 ? 280 LYS D CE  1 
ATOM   4998  N  NZ  . LYS B 2 280 ? 115.529 128.334 169.335 1.00 122.83 ? 280 LYS D NZ  1 
ATOM   4999  N  N   . GLY B 2 281 ? 120.078 132.827 167.348 1.00 116.52 ? 281 GLY D N   1 
ATOM   5000  C  CA  . GLY B 2 281 ? 121.524 132.709 167.340 1.00 116.52 ? 281 GLY D CA  1 
ATOM   5001  C  C   . GLY B 2 281 ? 122.165 133.406 168.522 1.00 116.52 ? 281 GLY D C   1 
ATOM   5002  O  O   . GLY B 2 281 ? 123.157 132.928 169.076 1.00 116.52 ? 281 GLY D O   1 
ATOM   5003  N  N   . HIS B 2 282 ? 121.608 134.549 168.921 1.00 113.92 ? 282 HIS D N   1 
ATOM   5004  C  CA  . HIS B 2 282 ? 122.169 135.274 170.050 1.00 113.92 ? 282 HIS D CA  1 
ATOM   5005  C  C   . HIS B 2 282 ? 121.933 134.513 171.347 1.00 113.92 ? 282 HIS D C   1 
ATOM   5006  O  O   . HIS B 2 282 ? 122.764 134.576 172.260 1.00 113.92 ? 282 HIS D O   1 
ATOM   5007  C  CB  . HIS B 2 282 ? 121.576 136.680 170.128 1.00 113.92 ? 282 HIS D CB  1 
ATOM   5008  C  CG  . HIS B 2 282 ? 122.472 137.678 170.794 1.00 113.92 ? 282 HIS D CG  1 
ATOM   5009  N  ND1 . HIS B 2 282 ? 122.698 137.690 172.153 1.00 113.92 ? 282 HIS D ND1 1 
ATOM   5010  C  CD2 . HIS B 2 282 ? 123.197 138.701 170.283 1.00 113.92 ? 282 HIS D CD2 1 
ATOM   5011  C  CE1 . HIS B 2 282 ? 123.527 138.675 172.451 1.00 113.92 ? 282 HIS D CE1 1 
ATOM   5012  N  NE2 . HIS B 2 282 ? 123.843 139.305 171.334 1.00 113.92 ? 282 HIS D NE2 1 
ATOM   5013  N  N   . ALA B 2 283 ? 120.815 133.787 171.448 1.00 119.45 ? 283 ALA D N   1 
ATOM   5014  C  CA  . ALA B 2 283 ? 120.579 132.980 172.638 1.00 119.45 ? 283 ALA D CA  1 
ATOM   5015  C  C   . ALA B 2 283 ? 121.333 131.661 172.601 1.00 119.45 ? 283 ALA D C   1 
ATOM   5016  O  O   . ALA B 2 283 ? 121.537 131.036 173.653 1.00 119.45 ? 283 ALA D O   1 
ATOM   5017  C  CB  . ALA B 2 283 ? 119.086 132.684 172.791 1.00 119.45 ? 283 ALA D CB  1 
ATOM   5018  N  N   . LYS B 2 284 ? 121.776 131.240 171.418 1.00 126.46 ? 284 LYS D N   1 
ATOM   5019  C  CA  . LYS B 2 284 ? 122.606 130.048 171.336 1.00 126.46 ? 284 LYS D CA  1 
ATOM   5020  C  C   . LYS B 2 284 ? 123.912 130.238 172.094 1.00 126.46 ? 284 LYS D C   1 
ATOM   5021  O  O   . LYS B 2 284 ? 124.383 129.318 172.768 1.00 126.46 ? 284 LYS D O   1 
ATOM   5022  C  CB  . LYS B 2 284 ? 122.862 129.700 169.870 1.00 126.46 ? 284 LYS D CB  1 
ATOM   5023  C  CG  . LYS B 2 284 ? 124.025 128.760 169.628 1.00 126.46 ? 284 LYS D CG  1 
ATOM   5024  C  CD  . LYS B 2 284 ? 124.061 128.318 168.175 1.00 126.46 ? 284 LYS D CD  1 
ATOM   5025  C  CE  . LYS B 2 284 ? 124.315 129.491 167.245 1.00 126.46 ? 284 LYS D CE  1 
ATOM   5026  N  NZ  . LYS B 2 284 ? 124.117 129.126 165.814 1.00 126.46 ? 284 LYS D NZ  1 
ATOM   5027  N  N   . CYS B 2 285 ? 124.488 131.442 172.034 1.00 119.75 ? 285 CYS D N   1 
ATOM   5028  C  CA  . CYS B 2 285 ? 125.736 131.703 172.746 1.00 119.75 ? 285 CYS D CA  1 
ATOM   5029  C  C   . CYS B 2 285 ? 125.556 131.651 174.260 1.00 119.75 ? 285 CYS D C   1 
ATOM   5030  O  O   . CYS B 2 285 ? 126.380 131.055 174.969 1.00 119.75 ? 285 CYS D O   1 
ATOM   5031  C  CB  . CYS B 2 285 ? 126.296 133.056 172.318 1.00 119.75 ? 285 CYS D CB  1 
ATOM   5032  S  SG  . CYS B 2 285 ? 126.585 133.219 170.543 1.00 119.75 ? 285 CYS D SG  1 
ATOM   5033  N  N   . VAL B 2 286 ? 124.488 132.265 174.779 1.00 113.92 ? 286 VAL D N   1 
ATOM   5034  C  CA  . VAL B 2 286 ? 124.273 132.232 176.223 1.00 113.92 ? 286 VAL D CA  1 
ATOM   5035  C  C   . VAL B 2 286 ? 123.999 130.806 176.679 1.00 113.92 ? 286 VAL D C   1 
ATOM   5036  O  O   . VAL B 2 286 ? 124.492 130.376 177.727 1.00 113.92 ? 286 VAL D O   1 
ATOM   5037  C  CB  . VAL B 2 286 ? 123.167 133.212 176.662 1.00 113.92 ? 286 VAL D CB  1 
ATOM   5038  C  CG1 . VAL B 2 286 ? 121.954 133.102 175.798 1.00 113.92 ? 286 VAL D CG1 1 
ATOM   5039  C  CG2 . VAL B 2 286 ? 122.789 132.967 178.114 1.00 113.92 ? 286 VAL D CG2 1 
ATOM   5040  N  N   . GLU B 2 287 ? 123.232 130.038 175.897 1.00 116.31 ? 287 GLU D N   1 
ATOM   5041  C  CA  . GLU B 2 287 ? 122.996 128.650 176.283 1.00 116.31 ? 287 GLU D CA  1 
ATOM   5042  C  C   . GLU B 2 287 ? 124.288 127.839 176.243 1.00 116.31 ? 287 GLU D C   1 
ATOM   5043  O  O   . GLU B 2 287 ? 124.519 126.989 177.114 1.00 116.31 ? 287 GLU D O   1 
ATOM   5044  C  CB  . GLU B 2 287 ? 121.942 128.021 175.374 1.00 116.31 ? 287 GLU D CB  1 
ATOM   5045  C  CG  . GLU B 2 287 ? 121.018 127.048 176.084 1.00 116.31 ? 287 GLU D CG  1 
ATOM   5046  C  CD  . GLU B 2 287 ? 119.672 126.921 175.403 1.00 116.31 ? 287 GLU D CD  1 
ATOM   5047  O  OE1 . GLU B 2 287 ? 119.607 127.113 174.171 1.00 116.31 ? 287 GLU D OE1 1 
ATOM   5048  O  OE2 . GLU B 2 287 ? 118.678 126.627 176.100 1.00 116.31 ? 287 GLU D OE2 1 
ATOM   5049  N  N   . VAL B 2 288 ? 125.144 128.097 175.250 1.00 113.92 ? 288 VAL D N   1 
ATOM   5050  C  CA  . VAL B 2 288 ? 126.445 127.434 175.179 1.00 113.92 ? 288 VAL D CA  1 
ATOM   5051  C  C   . VAL B 2 288 ? 127.248 127.702 176.443 1.00 113.92 ? 288 VAL D C   1 
ATOM   5052  O  O   . VAL B 2 288 ? 127.813 126.785 177.048 1.00 113.92 ? 288 VAL D O   1 
ATOM   5053  C  CB  . VAL B 2 288 ? 127.212 127.886 173.922 1.00 113.92 ? 288 VAL D CB  1 
ATOM   5054  C  CG1 . VAL B 2 288 ? 128.691 127.568 174.061 1.00 113.92 ? 288 VAL D CG1 1 
ATOM   5055  C  CG2 . VAL B 2 288 ? 126.649 127.211 172.687 1.00 113.92 ? 288 VAL D CG2 1 
ATOM   5056  N  N   . VAL B 2 289 ? 127.316 128.968 176.857 1.00 113.92 ? 289 VAL D N   1 
ATOM   5057  C  CA  . VAL B 2 289 ? 128.054 129.281 178.078 1.00 113.92 ? 289 VAL D CA  1 
ATOM   5058  C  C   . VAL B 2 289 ? 127.384 128.653 179.298 1.00 113.92 ? 289 VAL D C   1 
ATOM   5059  O  O   . VAL B 2 289 ? 128.063 128.276 180.262 1.00 113.92 ? 289 VAL D O   1 
ATOM   5060  C  CB  . VAL B 2 289 ? 128.217 130.804 178.237 1.00 113.92 ? 289 VAL D CB  1 
ATOM   5061  C  CG1 . VAL B 2 289 ? 129.050 131.121 179.466 1.00 113.92 ? 289 VAL D CG1 1 
ATOM   5062  C  CG2 . VAL B 2 289 ? 128.863 131.396 177.002 1.00 113.92 ? 289 VAL D CG2 1 
ATOM   5063  N  N   . LYS B 2 290 ? 126.053 128.517 179.281 1.00 115.67 ? 290 LYS D N   1 
ATOM   5064  C  CA  . LYS B 2 290 ? 125.365 127.841 180.379 1.00 115.67 ? 290 LYS D CA  1 
ATOM   5065  C  C   . LYS B 2 290 ? 125.749 126.371 180.484 1.00 115.67 ? 290 LYS D C   1 
ATOM   5066  O  O   . LYS B 2 290 ? 125.785 125.825 181.592 1.00 115.67 ? 290 LYS D O   1 
ATOM   5067  C  CB  . LYS B 2 290 ? 123.850 127.963 180.221 1.00 115.67 ? 290 LYS D CB  1 
ATOM   5068  C  CG  . LYS B 2 290 ? 123.299 129.365 180.379 1.00 115.67 ? 290 LYS D CG  1 
ATOM   5069  C  CD  . LYS B 2 290 ? 121.991 129.332 181.147 1.00 115.67 ? 290 LYS D CD  1 
ATOM   5070  C  CE  . LYS B 2 290 ? 121.002 128.384 180.487 1.00 115.67 ? 290 LYS D CE  1 
ATOM   5071  N  NZ  . LYS B 2 290 ? 119.697 128.354 181.199 1.00 115.67 ? 290 LYS D NZ  1 
ATOM   5072  N  N   . THR B 2 291 ? 126.005 125.709 179.350 1.00 113.92 ? 291 THR D N   1 
ATOM   5073  C  CA  . THR B 2 291 ? 126.341 124.283 179.397 1.00 113.92 ? 291 THR D CA  1 
ATOM   5074  C  C   . THR B 2 291 ? 127.502 124.007 180.347 1.00 113.92 ? 291 THR D C   1 
ATOM   5075  O  O   . THR B 2 291 ? 127.534 122.967 181.015 1.00 113.92 ? 291 THR D O   1 
ATOM   5076  C  CB  . THR B 2 291 ? 126.674 123.726 178.006 1.00 113.92 ? 291 THR D CB  1 
ATOM   5077  O  OG1 . THR B 2 291 ? 128.069 123.906 177.728 1.00 113.92 ? 291 THR D OG1 1 
ATOM   5078  C  CG2 . THR B 2 291 ? 125.824 124.339 176.920 1.00 113.92 ? 291 THR D CG2 1 
ATOM   5079  N  N   . PHE B 2 292 ? 128.468 124.925 180.418 1.00 113.92 ? 292 PHE D N   1 
ATOM   5080  C  CA  . PHE B 2 292 ? 129.640 124.702 181.256 1.00 113.92 ? 292 PHE D CA  1 
ATOM   5081  C  C   . PHE B 2 292 ? 129.327 124.820 182.744 1.00 113.92 ? 292 PHE D C   1 
ATOM   5082  O  O   . PHE B 2 292 ? 130.134 124.379 183.569 1.00 113.92 ? 292 PHE D O   1 
ATOM   5083  C  CB  . PHE B 2 292 ? 130.744 125.671 180.851 1.00 109.27 ? 292 PHE D CB  1 
ATOM   5084  C  CG  . PHE B 2 292 ? 131.127 125.565 179.400 1.00 109.27 ? 292 PHE D CG  1 
ATOM   5085  C  CD1 . PHE B 2 292 ? 132.065 124.640 178.975 1.00 109.27 ? 292 PHE D CD1 1 
ATOM   5086  C  CD2 . PHE B 2 292 ? 130.564 126.414 178.465 1.00 109.27 ? 292 PHE D CD2 1 
ATOM   5087  C  CE1 . PHE B 2 292 ? 132.419 124.554 177.646 1.00 109.27 ? 292 PHE D CE1 1 
ATOM   5088  C  CE2 . PHE B 2 292 ? 130.916 126.331 177.133 1.00 109.27 ? 292 PHE D CE2 1 
ATOM   5089  C  CZ  . PHE B 2 292 ? 131.844 125.400 176.725 1.00 109.27 ? 292 PHE D CZ  1 
ATOM   5090  N  N   . ASN B 2 293 ? 128.188 125.417 183.098 1.00 113.92 ? 293 ASN D N   1 
ATOM   5091  C  CA  . ASN B 2 293 ? 127.693 125.470 184.478 1.00 113.92 ? 293 ASN D CA  1 
ATOM   5092  C  C   . ASN B 2 293 ? 128.649 126.189 185.432 1.00 113.92 ? 293 ASN D C   1 
ATOM   5093  O  O   . ASN B 2 293 ? 129.033 125.661 186.478 1.00 113.92 ? 293 ASN D O   1 
ATOM   5094  C  CB  . ASN B 2 293 ? 127.375 124.062 184.989 1.00 113.92 ? 293 ASN D CB  1 
ATOM   5095  N  N   . LEU B 2 294 ? 129.038 127.402 185.065 1.00 113.92 ? 294 LEU D N   1 
ATOM   5096  C  CA  . LEU B 2 294 ? 129.834 128.272 185.916 1.00 113.92 ? 294 LEU D CA  1 
ATOM   5097  C  C   . LEU B 2 294 ? 129.062 129.556 186.192 1.00 113.92 ? 294 LEU D C   1 
ATOM   5098  O  O   . LEU B 2 294 ? 128.135 129.899 185.448 1.00 113.92 ? 294 LEU D O   1 
ATOM   5099  C  CB  . LEU B 2 294 ? 131.194 128.598 185.282 1.00 109.44 ? 294 LEU D CB  1 
ATOM   5100  C  CG  . LEU B 2 294 ? 132.158 127.419 185.162 1.00 109.44 ? 294 LEU D CG  1 
ATOM   5101  C  CD1 . LEU B 2 294 ? 133.047 127.575 183.952 1.00 109.44 ? 294 LEU D CD1 1 
ATOM   5102  C  CD2 . LEU B 2 294 ? 132.990 127.285 186.428 1.00 109.44 ? 294 LEU D CD2 1 
ATOM   5103  N  N   . PRO B 2 295 ? 129.390 130.272 187.269 1.00 113.92 ? 295 PRO D N   1 
ATOM   5104  C  CA  . PRO B 2 295 ? 128.738 131.566 187.513 1.00 113.92 ? 295 PRO D CA  1 
ATOM   5105  C  C   . PRO B 2 295 ? 128.856 132.481 186.304 1.00 113.92 ? 295 PRO D C   1 
ATOM   5106  O  O   . PRO B 2 295 ? 129.936 132.667 185.745 1.00 113.92 ? 295 PRO D O   1 
ATOM   5107  C  CB  . PRO B 2 295 ? 129.493 132.120 188.727 1.00 113.92 ? 295 PRO D CB  1 
ATOM   5108  C  CG  . PRO B 2 295 ? 130.054 130.921 189.402 1.00 113.92 ? 295 PRO D CG  1 
ATOM   5109  C  CD  . PRO B 2 295 ? 130.365 129.937 188.321 1.00 113.92 ? 295 PRO D CD  1 
ATOM   5110  N  N   . LEU B 2 296 ? 127.723 133.053 185.903 1.00 113.92 ? 296 LEU D N   1 
ATOM   5111  C  CA  . LEU B 2 296 ? 127.594 133.824 184.666 1.00 113.92 ? 296 LEU D CA  1 
ATOM   5112  C  C   . LEU B 2 296 ? 127.004 135.195 184.973 1.00 113.92 ? 296 LEU D C   1 
ATOM   5113  O  O   . LEU B 2 296 ? 125.799 135.317 185.212 1.00 113.92 ? 296 LEU D O   1 
ATOM   5114  C  CB  . LEU B 2 296 ? 126.738 133.079 183.648 1.00 113.92 ? 296 LEU D CB  1 
ATOM   5115  C  CG  . LEU B 2 296 ? 126.820 133.505 182.179 1.00 113.92 ? 296 LEU D CG  1 
ATOM   5116  C  CD1 . LEU B 2 296 ? 128.215 133.934 181.787 1.00 113.92 ? 296 LEU D CD1 1 
ATOM   5117  C  CD2 . LEU B 2 296 ? 126.317 132.399 181.265 1.00 113.92 ? 296 LEU D CD2 1 
ATOM   5118  N  N   . LEU B 2 297 ? 127.845 136.223 184.971 1.00 113.92 ? 297 LEU D N   1 
ATOM   5119  C  CA  . LEU B 2 297 ? 127.331 137.585 185.007 1.00 113.92 ? 297 LEU D CA  1 
ATOM   5120  C  C   . LEU B 2 297 ? 126.892 137.985 183.604 1.00 113.92 ? 297 LEU D C   1 
ATOM   5121  O  O   . LEU B 2 297 ? 127.530 137.615 182.619 1.00 113.92 ? 297 LEU D O   1 
ATOM   5122  C  CB  . LEU B 2 297 ? 128.388 138.550 185.540 1.00 113.92 ? 297 LEU D CB  1 
ATOM   5123  C  CG  . LEU B 2 297 ? 127.889 139.956 185.872 1.00 113.92 ? 297 LEU D CG  1 
ATOM   5124  C  CD1 . LEU B 2 297 ? 126.758 139.895 186.883 1.00 113.92 ? 297 LEU D CD1 1 
ATOM   5125  C  CD2 . LEU B 2 297 ? 129.027 140.811 186.396 1.00 113.92 ? 297 LEU D CD2 1 
ATOM   5126  N  N   . MET B 2 298 ? 125.790 138.729 183.511 1.00 113.92 ? 298 MET D N   1 
ATOM   5127  C  CA  . MET B 2 298 ? 125.165 139.056 182.225 1.00 113.92 ? 298 MET D CA  1 
ATOM   5128  C  C   . MET B 2 298 ? 124.974 140.563 182.098 1.00 113.92 ? 298 MET D C   1 
ATOM   5129  O  O   . MET B 2 298 ? 124.056 141.128 182.702 1.00 113.92 ? 298 MET D O   1 
ATOM   5130  C  CB  . MET B 2 298 ? 123.823 138.343 182.075 1.00 113.92 ? 298 MET D CB  1 
ATOM   5131  C  CG  . MET B 2 298 ? 123.901 136.886 181.670 1.00 113.92 ? 298 MET D CG  1 
ATOM   5132  S  SD  . MET B 2 298 ? 122.448 136.424 180.710 1.00 113.92 ? 298 MET D SD  1 
ATOM   5133  C  CE  . MET B 2 298 ? 123.121 136.414 179.057 1.00 113.92 ? 298 MET D CE  1 
ATOM   5134  N  N   . LEU B 2 299 ? 125.830 141.217 181.315 1.00 113.92 ? 299 LEU D N   1 
ATOM   5135  C  CA  . LEU B 2 299 ? 125.744 142.661 181.120 1.00 113.92 ? 299 LEU D CA  1 
ATOM   5136  C  C   . LEU B 2 299 ? 125.183 142.963 179.736 1.00 113.92 ? 299 LEU D C   1 
ATOM   5137  O  O   . LEU B 2 299 ? 125.743 142.528 178.727 1.00 113.92 ? 299 LEU D O   1 
ATOM   5138  C  CB  . LEU B 2 299 ? 127.104 143.337 181.298 1.00 113.92 ? 299 LEU D CB  1 
ATOM   5139  C  CG  . LEU B 2 299 ? 127.717 143.326 182.698 1.00 113.92 ? 299 LEU D CG  1 
ATOM   5140  C  CD1 . LEU B 2 299 ? 126.652 143.628 183.739 1.00 113.92 ? 299 LEU D CD1 1 
ATOM   5141  C  CD2 . LEU B 2 299 ? 128.408 142.017 182.991 1.00 113.92 ? 299 LEU D CD2 1 
ATOM   5142  N  N   . GLY B 2 300 ? 124.096 143.731 179.694 1.00 121.16 ? 300 GLY D N   1 
ATOM   5143  C  CA  . GLY B 2 300 ? 123.457 144.072 178.438 1.00 121.16 ? 300 GLY D CA  1 
ATOM   5144  C  C   . GLY B 2 300 ? 123.934 145.397 177.879 1.00 121.16 ? 300 GLY D C   1 
ATOM   5145  O  O   . GLY B 2 300 ? 123.501 146.459 178.334 1.00 121.16 ? 300 GLY D O   1 
ATOM   5146  N  N   . GLY B 2 301 ? 124.815 145.347 176.879 1.00 115.51 ? 301 GLY D N   1 
ATOM   5147  C  CA  . GLY B 2 301 ? 125.365 146.538 176.270 1.00 115.51 ? 301 GLY D CA  1 
ATOM   5148  C  C   . GLY B 2 301 ? 124.757 146.847 174.909 1.00 115.51 ? 301 GLY D C   1 
ATOM   5149  O  O   . GLY B 2 301 ? 123.913 146.124 174.385 1.00 115.51 ? 301 GLY D O   1 
ATOM   5150  N  N   . GLY B 2 302 ? 125.219 147.953 174.336 1.00 113.92 ? 302 GLY D N   1 
ATOM   5151  C  CA  . GLY B 2 302 ? 124.724 148.379 173.036 1.00 113.92 ? 302 GLY D CA  1 
ATOM   5152  C  C   . GLY B 2 302 ? 123.238 148.675 173.084 1.00 113.92 ? 302 GLY D C   1 
ATOM   5153  O  O   . GLY B 2 302 ? 122.771 149.529 173.848 1.00 113.92 ? 302 GLY D O   1 
ATOM   5154  N  N   . GLY B 2 303 ? 122.473 147.966 172.262 1.00 113.92 ? 303 GLY D N   1 
ATOM   5155  C  CA  . GLY B 2 303 ? 121.034 148.119 172.270 1.00 113.92 ? 303 GLY D CA  1 
ATOM   5156  C  C   . GLY B 2 303 ? 120.522 149.407 171.663 1.00 113.92 ? 303 GLY D C   1 
ATOM   5157  O  O   . GLY B 2 303 ? 120.042 150.289 172.380 1.00 113.92 ? 303 GLY D O   1 
ATOM   5158  N  N   . TYR B 2 304 ? 120.626 149.535 170.340 1.00 113.92 ? 304 TYR D N   1 
ATOM   5159  C  CA  . TYR B 2 304 ? 120.285 150.772 169.647 1.00 113.92 ? 304 TYR D CA  1 
ATOM   5160  C  C   . TYR B 2 304 ? 118.980 150.700 168.861 1.00 113.92 ? 304 TYR D C   1 
ATOM   5161  O  O   . TYR B 2 304 ? 118.156 151.612 168.966 1.00 113.92 ? 304 TYR D O   1 
ATOM   5162  C  CB  . TYR B 2 304 ? 121.462 151.161 168.742 1.00 102.31 ? 304 TYR D CB  1 
ATOM   5163  C  CG  . TYR B 2 304 ? 122.755 151.346 169.522 1.00 102.31 ? 304 TYR D CG  1 
ATOM   5164  C  CD1 . TYR B 2 304 ? 122.735 151.690 170.868 1.00 102.31 ? 304 TYR D CD1 1 
ATOM   5165  C  CD2 . TYR B 2 304 ? 123.987 151.119 168.933 1.00 102.31 ? 304 TYR D CD2 1 
ATOM   5166  C  CE1 . TYR B 2 304 ? 123.904 151.843 171.589 1.00 102.31 ? 304 TYR D CE1 1 
ATOM   5167  C  CE2 . TYR B 2 304 ? 125.165 151.270 169.648 1.00 102.31 ? 304 TYR D CE2 1 
ATOM   5168  C  CZ  . TYR B 2 304 ? 125.115 151.631 170.976 1.00 102.31 ? 304 TYR D CZ  1 
ATOM   5169  O  OH  . TYR B 2 304 ? 126.280 151.781 171.693 1.00 102.31 ? 304 TYR D OH  1 
ATOM   5170  N  N   . THR B 2 305 ? 118.754 149.645 168.074 1.00 113.92 ? 305 THR D N   1 
ATOM   5171  C  CA  . THR B 2 305 ? 117.445 149.416 167.451 1.00 113.92 ? 305 THR D CA  1 
ATOM   5172  C  C   . THR B 2 305 ? 116.532 148.837 168.520 1.00 113.92 ? 305 THR D C   1 
ATOM   5173  O  O   . THR B 2 305 ? 116.614 147.654 168.851 1.00 113.92 ? 305 THR D O   1 
ATOM   5174  C  CB  . THR B 2 305 ? 117.545 148.503 166.237 1.00 113.92 ? 305 THR D CB  1 
ATOM   5175  O  OG1 . THR B 2 305 ? 118.205 149.203 165.178 1.00 113.92 ? 305 THR D OG1 1 
ATOM   5176  C  CG2 . THR B 2 305 ? 116.156 148.096 165.766 1.00 113.92 ? 305 THR D CG2 1 
ATOM   5177  N  N   . ILE B 2 306 ? 115.624 149.666 169.031 1.00 113.92 ? 306 ILE D N   1 
ATOM   5178  C  CA  . ILE B 2 306 ? 114.962 149.341 170.287 1.00 113.92 ? 306 ILE D CA  1 
ATOM   5179  C  C   . ILE B 2 306 ? 114.021 148.136 170.185 1.00 113.92 ? 306 ILE D C   1 
ATOM   5180  O  O   . ILE B 2 306 ? 113.853 147.399 171.165 1.00 113.92 ? 306 ILE D O   1 
ATOM   5181  C  CB  . ILE B 2 306 ? 114.254 150.615 170.797 1.00 108.85 ? 306 ILE D CB  1 
ATOM   5182  C  CG1 . ILE B 2 306 ? 113.578 151.416 169.672 1.00 108.85 ? 306 ILE D CG1 1 
ATOM   5183  C  CG2 . ILE B 2 306 ? 115.274 151.567 171.367 1.00 108.85 ? 306 ILE D CG2 1 
ATOM   5184  C  CD1 . ILE B 2 306 ? 112.463 150.742 168.911 1.00 108.85 ? 306 ILE D CD1 1 
ATOM   5185  N  N   . ARG B 2 307 ? 113.463 147.856 169.003 1.00 113.92 ? 307 ARG D N   1 
ATOM   5186  C  CA  . ARG B 2 307 ? 112.593 146.687 168.864 1.00 113.92 ? 307 ARG D CA  1 
ATOM   5187  C  C   . ARG B 2 307 ? 113.376 145.380 168.903 1.00 113.92 ? 307 ARG D C   1 
ATOM   5188  O  O   . ARG B 2 307 ? 113.065 144.481 169.699 1.00 113.92 ? 307 ARG D O   1 
ATOM   5189  C  CB  . ARG B 2 307 ? 111.768 146.808 167.583 1.00 113.92 ? 307 ARG D CB  1 
ATOM   5190  C  CG  . ARG B 2 307 ? 112.488 147.482 166.431 1.00 113.92 ? 307 ARG D CG  1 
ATOM   5191  C  CD  . ARG B 2 307 ? 111.954 147.011 165.092 1.00 113.92 ? 307 ARG D CD  1 
ATOM   5192  N  NE  . ARG B 2 307 ? 112.362 147.903 164.013 1.00 113.92 ? 307 ARG D NE  1 
ATOM   5193  C  CZ  . ARG B 2 307 ? 112.447 147.550 162.739 1.00 113.92 ? 307 ARG D CZ  1 
ATOM   5194  N  NH1 . ARG B 2 307 ? 112.180 146.315 162.345 1.00 113.92 ? 307 ARG D NH1 1 
ATOM   5195  N  NH2 . ARG B 2 307 ? 112.818 148.455 161.838 1.00 113.92 ? 307 ARG D NH2 1 
ATOM   5196  N  N   . ASN B 2 308 ? 114.391 145.251 168.044 1.00 113.92 ? 308 ASN D N   1 
ATOM   5197  C  CA  . ASN B 2 308 ? 115.170 144.018 168.016 1.00 113.92 ? 308 ASN D CA  1 
ATOM   5198  C  C   . ASN B 2 308 ? 115.853 143.794 169.353 1.00 113.92 ? 308 ASN D C   1 
ATOM   5199  O  O   . ASN B 2 308 ? 115.929 142.663 169.842 1.00 113.92 ? 308 ASN D O   1 
ATOM   5200  C  CB  . ASN B 2 308 ? 116.204 144.067 166.892 1.00 113.92 ? 308 ASN D CB  1 
ATOM   5201  C  CG  . ASN B 2 308 ? 115.573 144.039 165.516 1.00 113.92 ? 308 ASN D CG  1 
ATOM   5202  O  OD1 . ASN B 2 308 ? 114.377 144.279 165.365 1.00 113.92 ? 308 ASN D OD1 1 
ATOM   5203  N  ND2 . ASN B 2 308 ? 116.378 143.743 164.503 1.00 113.92 ? 308 ASN D ND2 1 
ATOM   5204  N  N   . VAL B 2 309 ? 116.347 144.872 169.958 1.00 113.92 ? 309 VAL D N   1 
ATOM   5205  C  CA  . VAL B 2 309 ? 117.022 144.776 171.246 1.00 113.92 ? 309 VAL D CA  1 
ATOM   5206  C  C   . VAL B 2 309 ? 116.054 144.316 172.325 1.00 113.92 ? 309 VAL D C   1 
ATOM   5207  O  O   . VAL B 2 309 ? 116.382 143.454 173.149 1.00 113.92 ? 309 VAL D O   1 
ATOM   5208  C  CB  . VAL B 2 309 ? 117.673 146.121 171.600 1.00 113.92 ? 309 VAL D CB  1 
ATOM   5209  C  CG1 . VAL B 2 309 ? 118.237 146.085 173.012 1.00 113.92 ? 309 VAL D CG1 1 
ATOM   5210  C  CG2 . VAL B 2 309 ? 118.745 146.429 170.579 1.00 113.92 ? 309 VAL D CG2 1 
ATOM   5211  N  N   . ALA B 2 310 ? 114.850 144.896 172.351 1.00 113.92 ? 310 ALA D N   1 
ATOM   5212  C  CA  . ALA B 2 310 ? 113.875 144.490 173.356 1.00 113.92 ? 310 ALA D CA  1 
ATOM   5213  C  C   . ALA B 2 310 ? 113.529 143.015 173.217 1.00 113.92 ? 310 ALA D C   1 
ATOM   5214  O  O   . ALA B 2 310 ? 113.531 142.264 174.205 1.00 113.92 ? 310 ALA D O   1 
ATOM   5215  C  CB  . ALA B 2 310 ? 112.619 145.354 173.247 1.00 113.92 ? 310 ALA D CB  1 
ATOM   5216  N  N   . ARG B 2 311 ? 113.262 142.573 171.986 1.00 113.92 ? 311 ARG D N   1 
ATOM   5217  C  CA  . ARG B 2 311 ? 112.919 141.171 171.775 1.00 113.92 ? 311 ARG D CA  1 
ATOM   5218  C  C   . ARG B 2 311 ? 114.075 140.256 172.158 1.00 113.92 ? 311 ARG D C   1 
ATOM   5219  O  O   . ARG B 2 311 ? 113.874 139.230 172.822 1.00 113.92 ? 311 ARG D O   1 
ATOM   5220  C  CB  . ARG B 2 311 ? 112.492 140.949 170.325 1.00 113.92 ? 311 ARG D CB  1 
ATOM   5221  C  CG  . ARG B 2 311 ? 111.332 141.840 169.909 1.00 113.92 ? 311 ARG D CG  1 
ATOM   5222  C  CD  . ARG B 2 311 ? 110.573 141.278 168.722 1.00 113.92 ? 311 ARG D CD  1 
ATOM   5223  N  NE  . ARG B 2 311 ? 111.108 141.754 167.453 1.00 113.92 ? 311 ARG D NE  1 
ATOM   5224  C  CZ  . ARG B 2 311 ? 110.468 142.580 166.637 1.00 113.92 ? 311 ARG D CZ  1 
ATOM   5225  N  NH1 . ARG B 2 311 ? 109.271 143.058 166.936 1.00 113.92 ? 311 ARG D NH1 1 
ATOM   5226  N  NH2 . ARG B 2 311 ? 111.043 142.937 165.492 1.00 113.92 ? 311 ARG D NH2 1 
ATOM   5227  N  N   . CYS B 2 312 ? 115.297 140.613 171.755 1.00 113.92 ? 312 CYS D N   1 
ATOM   5228  C  CA  . CYS B 2 312 ? 116.451 139.776 172.058 1.00 113.92 ? 312 CYS D CA  1 
ATOM   5229  C  C   . CYS B 2 312 ? 116.673 139.660 173.557 1.00 113.92 ? 312 CYS D C   1 
ATOM   5230  O  O   . CYS B 2 312 ? 116.912 138.566 174.070 1.00 113.92 ? 312 CYS D O   1 
ATOM   5231  C  CB  . CYS B 2 312 ? 117.704 140.330 171.386 1.00 113.92 ? 312 CYS D CB  1 
ATOM   5232  S  SG  . CYS B 2 312 ? 119.226 139.562 171.990 1.00 113.92 ? 312 CYS D SG  1 
ATOM   5233  N  N   . TRP B 2 313 ? 116.627 140.783 174.276 1.00 113.92 ? 313 TRP D N   1 
ATOM   5234  C  CA  . TRP B 2 313 ? 116.878 140.723 175.712 1.00 113.92 ? 313 TRP D CA  1 
ATOM   5235  C  C   . TRP B 2 313 ? 115.782 139.958 176.444 1.00 113.92 ? 313 TRP D C   1 
ATOM   5236  O  O   . TRP B 2 313 ? 116.073 139.204 177.382 1.00 113.92 ? 313 TRP D O   1 
ATOM   5237  C  CB  . TRP B 2 313 ? 117.060 142.130 176.280 1.00 113.92 ? 313 TRP D CB  1 
ATOM   5238  C  CG  . TRP B 2 313 ? 118.374 142.741 175.876 1.00 113.92 ? 313 TRP D CG  1 
ATOM   5239  C  CD1 . TRP B 2 313 ? 119.414 142.104 175.264 1.00 113.92 ? 313 TRP D CD1 1 
ATOM   5240  C  CD2 . TRP B 2 313 ? 118.797 144.096 176.076 1.00 113.92 ? 313 TRP D CD2 1 
ATOM   5241  N  NE1 . TRP B 2 313 ? 120.452 142.978 175.059 1.00 113.92 ? 313 TRP D NE1 1 
ATOM   5242  C  CE2 . TRP B 2 313 ? 120.099 144.208 175.549 1.00 113.92 ? 313 TRP D CE2 1 
ATOM   5243  C  CE3 . TRP B 2 313 ? 118.201 145.226 176.643 1.00 113.92 ? 313 TRP D CE3 1 
ATOM   5244  C  CZ2 . TRP B 2 313 ? 120.814 145.403 175.572 1.00 113.92 ? 313 TRP D CZ2 1 
ATOM   5245  C  CZ3 . TRP B 2 313 ? 118.913 146.411 176.665 1.00 113.92 ? 313 TRP D CZ3 1 
ATOM   5246  C  CH2 . TRP B 2 313 ? 120.206 146.490 176.133 1.00 113.92 ? 313 TRP D CH2 1 
ATOM   5247  N  N   . THR B 2 314 ? 114.516 140.117 176.036 1.00 113.92 ? 314 THR D N   1 
ATOM   5248  C  CA  . THR B 2 314 ? 113.471 139.317 176.672 1.00 113.92 ? 314 THR D CA  1 
ATOM   5249  C  C   . THR B 2 314 ? 113.685 137.827 176.402 1.00 113.92 ? 314 THR D C   1 
ATOM   5250  O  O   . THR B 2 314 ? 113.503 136.993 177.300 1.00 113.92 ? 314 THR D O   1 
ATOM   5251  C  CB  . THR B 2 314 ? 112.075 139.800 176.247 1.00 113.92 ? 314 THR D CB  1 
ATOM   5252  O  OG1 . THR B 2 314 ? 111.138 139.518 177.296 1.00 113.92 ? 314 THR D OG1 1 
ATOM   5253  C  CG2 . THR B 2 314 ? 111.589 139.149 174.961 1.00 113.92 ? 314 THR D CG2 1 
ATOM   5254  N  N   . TYR B 2 315 ? 114.075 137.467 175.173 1.00 114.38 ? 315 TYR D N   1 
ATOM   5255  C  CA  . TYR B 2 315 ? 114.344 136.063 174.876 1.00 114.38 ? 315 TYR D CA  1 
ATOM   5256  C  C   . TYR B 2 315 ? 115.527 135.560 175.697 1.00 114.38 ? 315 TYR D C   1 
ATOM   5257  O  O   . TYR B 2 315 ? 115.538 134.408 176.142 1.00 114.38 ? 315 TYR D O   1 
ATOM   5258  C  CB  . TYR B 2 315 ? 114.566 135.850 173.378 1.00 114.38 ? 315 TYR D CB  1 
ATOM   5259  C  CG  . TYR B 2 315 ? 114.526 134.387 172.955 1.00 114.38 ? 315 TYR D CG  1 
ATOM   5260  C  CD1 . TYR B 2 315 ? 115.548 133.506 173.284 1.00 114.38 ? 315 TYR D CD1 1 
ATOM   5261  C  CD2 . TYR B 2 315 ? 113.432 133.882 172.265 1.00 114.38 ? 315 TYR D CD2 1 
ATOM   5262  C  CE1 . TYR B 2 315 ? 115.490 132.176 172.913 1.00 114.38 ? 315 TYR D CE1 1 
ATOM   5263  C  CE2 . TYR B 2 315 ? 113.368 132.555 171.892 1.00 114.38 ? 315 TYR D CE2 1 
ATOM   5264  C  CZ  . TYR B 2 315 ? 114.399 131.706 172.221 1.00 114.38 ? 315 TYR D CZ  1 
ATOM   5265  O  OH  . TYR B 2 315 ? 114.340 130.383 171.852 1.00 114.38 ? 315 TYR D OH  1 
ATOM   5266  N  N   . GLU B 2 316 ? 116.556 136.397 175.866 1.00 113.92 ? 316 GLU D N   1 
ATOM   5267  C  CA  . GLU B 2 316 ? 117.721 135.984 176.640 1.00 113.92 ? 316 GLU D CA  1 
ATOM   5268  C  C   . GLU B 2 316 ? 117.325 135.737 178.085 1.00 113.92 ? 316 GLU D C   1 
ATOM   5269  O  O   . GLU B 2 316 ? 117.823 134.808 178.730 1.00 113.92 ? 316 GLU D O   1 
ATOM   5270  C  CB  . GLU B 2 316 ? 118.807 137.065 176.600 1.00 113.36 ? 316 GLU D CB  1 
ATOM   5271  C  CG  . GLU B 2 316 ? 119.487 137.410 175.264 1.00 113.36 ? 316 GLU D CG  1 
ATOM   5272  C  CD  . GLU B 2 316 ? 119.936 136.223 174.441 1.00 113.36 ? 316 GLU D CD  1 
ATOM   5273  O  OE1 . GLU B 2 316 ? 119.105 135.350 174.139 1.00 113.36 ? 316 GLU D OE1 1 
ATOM   5274  O  OE2 . GLU B 2 316 ? 121.134 136.167 174.092 1.00 113.36 ? 316 GLU D OE2 1 
ATOM   5275  N  N   . THR B 2 317 ? 116.419 136.566 178.603 1.00 113.92 ? 317 THR D N   1 
ATOM   5276  C  CA  . THR B 2 317 ? 115.873 136.346 179.937 1.00 113.92 ? 317 THR D CA  1 
ATOM   5277  C  C   . THR B 2 317 ? 115.113 135.026 180.005 1.00 113.92 ? 317 THR D C   1 
ATOM   5278  O  O   . THR B 2 317 ? 115.232 134.275 180.983 1.00 113.92 ? 317 THR D O   1 
ATOM   5279  C  CB  . THR B 2 317 ? 114.969 137.519 180.312 1.00 113.92 ? 317 THR D CB  1 
ATOM   5280  O  OG1 . THR B 2 317 ? 115.727 138.734 180.274 1.00 113.92 ? 317 THR D OG1 1 
ATOM   5281  C  CG2 . THR B 2 317 ? 114.398 137.334 181.694 1.00 113.92 ? 317 THR D CG2 1 
ATOM   5282  N  N   . ALA B 2 318 ? 114.343 134.718 178.958 1.00 123.55 ? 318 ALA D N   1 
ATOM   5283  C  CA  . ALA B 2 318 ? 113.641 133.437 178.902 1.00 123.55 ? 318 ALA D CA  1 
ATOM   5284  C  C   . ALA B 2 318 ? 114.622 132.270 178.917 1.00 123.55 ? 318 ALA D C   1 
ATOM   5285  O  O   . ALA B 2 318 ? 114.400 131.271 179.611 1.00 123.55 ? 318 ALA D O   1 
ATOM   5286  C  CB  . ALA B 2 318 ? 112.755 133.378 177.659 1.00 123.55 ? 318 ALA D CB  1 
ATOM   5287  N  N   . VAL B 2 319 ? 115.705 132.378 178.146 1.00 117.40 ? 319 VAL D N   1 
ATOM   5288  C  CA  . VAL B 2 319 ? 116.727 131.334 178.128 1.00 117.40 ? 319 VAL D CA  1 
ATOM   5289  C  C   . VAL B 2 319 ? 117.331 131.179 179.515 1.00 117.40 ? 319 VAL D C   1 
ATOM   5290  O  O   . VAL B 2 319 ? 117.532 130.061 180.005 1.00 117.40 ? 319 VAL D O   1 
ATOM   5291  C  CB  . VAL B 2 319 ? 117.804 131.648 177.072 1.00 117.40 ? 319 VAL D CB  1 
ATOM   5292  C  CG1 . VAL B 2 319 ? 119.052 130.814 177.316 1.00 117.40 ? 319 VAL D CG1 1 
ATOM   5293  C  CG2 . VAL B 2 319 ? 117.267 131.386 175.685 1.00 117.40 ? 319 VAL D CG2 1 
ATOM   5294  N  N   . ALA B 2 320 ? 117.635 132.305 180.165 1.00 126.62 ? 320 ALA D N   1 
ATOM   5295  C  CA  . ALA B 2 320 ? 118.140 132.274 181.531 1.00 126.62 ? 320 ALA D CA  1 
ATOM   5296  C  C   . ALA B 2 320 ? 117.164 131.584 182.472 1.00 126.62 ? 320 ALA D C   1 
ATOM   5297  O  O   . ALA B 2 320 ? 117.584 130.966 183.456 1.00 126.62 ? 320 ALA D O   1 
ATOM   5298  C  CB  . ALA B 2 320 ? 118.411 133.696 182.017 1.00 126.62 ? 320 ALA D CB  1 
ATOM   5299  N  N   . LEU B 2 321 ? 115.865 131.665 182.187 1.00 138.26 ? 321 LEU D N   1 
ATOM   5300  C  CA  . LEU B 2 321 ? 114.876 130.997 183.023 1.00 138.26 ? 321 LEU D CA  1 
ATOM   5301  C  C   . LEU B 2 321 ? 114.594 129.570 182.570 1.00 138.26 ? 321 LEU D C   1 
ATOM   5302  O  O   . LEU B 2 321 ? 113.897 128.838 183.281 1.00 138.26 ? 321 LEU D O   1 
ATOM   5303  C  CB  . LEU B 2 321 ? 113.565 131.797 183.028 1.00 138.26 ? 321 LEU D CB  1 
ATOM   5304  C  CG  . LEU B 2 321 ? 112.587 131.598 184.192 1.00 138.26 ? 321 LEU D CG  1 
ATOM   5305  C  CD1 . LEU B 2 321 ? 112.082 132.946 184.668 1.00 138.26 ? 321 LEU D CD1 1 
ATOM   5306  C  CD2 . LEU B 2 321 ? 111.419 130.689 183.840 1.00 138.26 ? 321 LEU D CD2 1 
ATOM   5307  N  N   . ASP B 2 322 ? 115.148 129.152 181.430 1.00 140.13 ? 322 ASP D N   1 
ATOM   5308  C  CA  . ASP B 2 322 ? 114.918 127.821 180.865 1.00 140.13 ? 322 ASP D CA  1 
ATOM   5309  C  C   . ASP B 2 322 ? 113.423 127.563 180.672 1.00 140.13 ? 322 ASP D C   1 
ATOM   5310  O  O   . ASP B 2 322 ? 112.900 126.497 181.002 1.00 140.13 ? 322 ASP D O   1 
ATOM   5311  C  CB  . ASP B 2 322 ? 115.562 126.733 181.730 1.00 140.13 ? 322 ASP D CB  1 
ATOM   5312  N  N   . CYS B 2 323 ? 112.735 128.564 180.131 1.00 139.28 ? 323 CYS D N   1 
ATOM   5313  C  CA  . CYS B 2 323 ? 111.306 128.518 179.857 1.00 139.28 ? 323 CYS D CA  1 
ATOM   5314  C  C   . CYS B 2 323 ? 111.051 128.659 178.362 1.00 139.28 ? 323 CYS D C   1 
ATOM   5315  O  O   . CYS B 2 323 ? 111.964 128.904 177.569 1.00 139.28 ? 323 CYS D O   1 
ATOM   5316  C  CB  . CYS B 2 323 ? 110.557 129.615 180.623 1.00 139.28 ? 323 CYS D CB  1 
ATOM   5317  S  SG  . CYS B 2 323 ? 111.029 131.295 180.162 1.00 139.28 ? 323 CYS D SG  1 
ATOM   5318  N  N   . GLU B 2 324 ? 109.787 128.493 177.983 1.00 139.70 ? 324 GLU D N   1 
ATOM   5319  C  CA  . GLU B 2 324 ? 109.359 128.561 176.593 1.00 139.70 ? 324 GLU D CA  1 
ATOM   5320  C  C   . GLU B 2 324 ? 108.461 129.778 176.411 1.00 139.70 ? 324 GLU D C   1 
ATOM   5321  O  O   . GLU B 2 324 ? 107.556 130.013 177.219 1.00 139.70 ? 324 GLU D O   1 
ATOM   5322  C  CB  . GLU B 2 324 ? 108.618 127.286 176.184 1.00 139.70 ? 324 GLU D CB  1 
ATOM   5323  N  N   . ILE B 2 325 ? 108.713 130.544 175.354 1.00 133.16 ? 325 ILE D N   1 
ATOM   5324  C  CA  . ILE B 2 325 ? 107.926 131.736 175.042 1.00 133.16 ? 325 ILE D CA  1 
ATOM   5325  C  C   . ILE B 2 325 ? 107.432 131.657 173.600 1.00 133.16 ? 325 ILE D C   1 
ATOM   5326  O  O   . ILE B 2 325 ? 108.217 131.370 172.685 1.00 133.16 ? 325 ILE D O   1 
ATOM   5327  C  CB  . ILE B 2 325 ? 108.728 133.024 175.306 1.00 133.16 ? 325 ILE D CB  1 
ATOM   5328  C  CG1 . ILE B 2 325 ? 109.948 133.127 174.387 1.00 133.16 ? 325 ILE D CG1 1 
ATOM   5329  C  CG2 . ILE B 2 325 ? 109.142 133.107 176.770 1.00 133.16 ? 325 ILE D CG2 1 
ATOM   5330  C  CD1 . ILE B 2 325 ? 110.819 134.331 174.662 1.00 133.16 ? 325 ILE D CD1 1 
ATOM   5331  N  N   . PRO B 2 326 ? 106.135 131.849 173.360 1.00 134.99 ? 326 PRO D N   1 
ATOM   5332  C  CA  . PRO B 2 326 ? 105.616 131.759 171.990 1.00 134.99 ? 326 PRO D CA  1 
ATOM   5333  C  C   . PRO B 2 326 ? 106.188 132.840 171.084 1.00 134.99 ? 326 PRO D C   1 
ATOM   5334  O  O   . PRO B 2 326 ? 106.537 133.937 171.524 1.00 134.99 ? 326 PRO D O   1 
ATOM   5335  C  CB  . PRO B 2 326 ? 104.103 131.931 172.170 1.00 134.99 ? 326 PRO D CB  1 
ATOM   5336  C  CG  . PRO B 2 326 ? 103.841 131.591 173.602 1.00 134.99 ? 326 PRO D CG  1 
ATOM   5337  C  CD  . PRO B 2 326 ? 105.061 132.023 174.352 1.00 134.99 ? 326 PRO D CD  1 
ATOM   5338  N  N   . ASN B 2 327 ? 106.279 132.505 169.795 1.00 134.49 ? 327 ASN D N   1 
ATOM   5339  C  CA  . ASN B 2 327 ? 106.762 133.454 168.796 1.00 134.49 ? 327 ASN D CA  1 
ATOM   5340  C  C   . ASN B 2 327 ? 105.803 134.630 168.634 1.00 134.49 ? 327 ASN D C   1 
ATOM   5341  O  O   . ASN B 2 327 ? 106.237 135.775 168.465 1.00 134.49 ? 327 ASN D O   1 
ATOM   5342  C  CB  . ASN B 2 327 ? 106.972 132.735 167.462 1.00 134.49 ? 327 ASN D CB  1 
ATOM   5343  C  CG  . ASN B 2 327 ? 107.515 133.648 166.377 1.00 134.49 ? 327 ASN D CG  1 
ATOM   5344  O  OD1 . ASN B 2 327 ? 108.052 134.720 166.657 1.00 134.49 ? 327 ASN D OD1 1 
ATOM   5345  N  ND2 . ASN B 2 327 ? 107.380 133.221 165.127 1.00 134.49 ? 327 ASN D ND2 1 
ATOM   5346  N  N   . GLU B 2 328 ? 104.499 134.368 168.674 1.00 147.37 ? 328 GLU D N   1 
ATOM   5347  C  CA  . GLU B 2 328 ? 103.491 135.411 168.503 1.00 147.37 ? 328 GLU D CA  1 
ATOM   5348  C  C   . GLU B 2 328 ? 103.469 136.330 169.720 1.00 147.37 ? 328 GLU D C   1 
ATOM   5349  O  O   . GLU B 2 328 ? 103.061 135.919 170.811 1.00 147.37 ? 328 GLU D O   1 
ATOM   5350  C  CB  . GLU B 2 328 ? 102.121 134.782 168.270 1.00 147.37 ? 328 GLU D CB  1 
ATOM   5351  C  CG  . GLU B 2 328 ? 101.927 134.192 166.878 1.00 147.37 ? 328 GLU D CG  1 
ATOM   5352  C  CD  . GLU B 2 328 ? 102.685 132.893 166.676 1.00 147.37 ? 328 GLU D CD  1 
ATOM   5353  O  OE1 . GLU B 2 328 ? 103.110 132.287 167.683 1.00 147.37 ? 328 GLU D OE1 1 
ATOM   5354  O  OE2 . GLU B 2 328 ? 102.861 132.480 165.511 1.00 147.37 ? 328 GLU D OE2 1 
ATOM   5355  N  N   . LEU B 2 329 ? 103.916 137.569 169.536 1.00 136.26 ? 329 LEU D N   1 
ATOM   5356  C  CA  . LEU B 2 329 ? 103.986 138.517 170.644 1.00 136.26 ? 329 LEU D CA  1 
ATOM   5357  C  C   . LEU B 2 329 ? 102.596 138.895 171.135 1.00 136.26 ? 329 LEU D C   1 
ATOM   5358  O  O   . LEU B 2 329 ? 101.725 139.225 170.322 1.00 136.26 ? 329 LEU D O   1 
ATOM   5359  C  CB  . LEU B 2 329 ? 104.702 139.801 170.224 1.00 136.26 ? 329 LEU D CB  1 
ATOM   5360  C  CG  . LEU B 2 329 ? 106.159 139.840 169.798 1.00 136.26 ? 329 LEU D CG  1 
ATOM   5361  C  CD1 . LEU B 2 329 ? 106.490 141.199 169.228 1.00 136.26 ? 329 LEU D CD1 1 
ATOM   5362  C  CD2 . LEU B 2 329 ? 106.959 139.635 171.043 1.00 136.26 ? 329 LEU D CD2 1 
ATOM   5363  N  N   . PRO B 2 330 ? 102.347 138.864 172.440 1.00 152.68 ? 330 PRO D N   1 
ATOM   5364  C  CA  . PRO B 2 330 ? 101.050 139.315 172.943 1.00 152.68 ? 330 PRO D CA  1 
ATOM   5365  C  C   . PRO B 2 330 ? 101.003 140.830 172.851 1.00 152.68 ? 330 PRO D C   1 
ATOM   5366  O  O   . PRO B 2 330 ? 102.033 141.502 172.947 1.00 152.68 ? 330 PRO D O   1 
ATOM   5367  C  CB  . PRO B 2 330 ? 101.040 138.831 174.395 1.00 152.68 ? 330 PRO D CB  1 
ATOM   5368  C  CG  . PRO B 2 330 ? 102.486 138.795 174.772 1.00 152.68 ? 330 PRO D CG  1 
ATOM   5369  C  CD  . PRO B 2 330 ? 103.223 138.381 173.522 1.00 152.68 ? 330 PRO D CD  1 
ATOM   5370  N  N   . TYR B 2 331 ? 99.803  141.368 172.627 1.00 176.64 ? 331 TYR D N   1 
ATOM   5371  C  CA  . TYR B 2 331 ? 99.666  142.815 172.489 1.00 176.64 ? 331 TYR D CA  1 
ATOM   5372  C  C   . TYR B 2 331 ? 100.294 143.505 173.693 1.00 176.64 ? 331 TYR D C   1 
ATOM   5373  O  O   . TYR B 2 331 ? 99.796  143.391 174.818 1.00 176.64 ? 331 TYR D O   1 
ATOM   5374  C  CB  . TYR B 2 331 ? 98.198  143.216 172.336 1.00 176.64 ? 331 TYR D CB  1 
ATOM   5375  C  CG  . TYR B 2 331 ? 97.981  144.712 172.284 1.00 176.64 ? 331 TYR D CG  1 
ATOM   5376  C  CD1 . TYR B 2 331 ? 98.225  145.424 171.117 1.00 176.64 ? 331 TYR D CD1 1 
ATOM   5377  C  CD2 . TYR B 2 331 ? 97.538  145.412 173.398 1.00 176.64 ? 331 TYR D CD2 1 
ATOM   5378  C  CE1 . TYR B 2 331 ? 98.033  146.791 171.060 1.00 176.64 ? 331 TYR D CE1 1 
ATOM   5379  C  CE2 . TYR B 2 331 ? 97.343  146.780 173.351 1.00 176.64 ? 331 TYR D CE2 1 
ATOM   5380  C  CZ  . TYR B 2 331 ? 97.592  147.464 172.179 1.00 176.64 ? 331 TYR D CZ  1 
ATOM   5381  O  OH  . TYR B 2 331 ? 97.398  148.825 172.127 1.00 176.64 ? 331 TYR D OH  1 
ATOM   5382  N  N   . ASN B 2 332 ? 101.392 144.220 173.462 1.00 161.53 ? 332 ASN D N   1 
ATOM   5383  C  CA  . ASN B 2 332 ? 102.168 144.830 174.526 1.00 161.53 ? 332 ASN D CA  1 
ATOM   5384  C  C   . ASN B 2 332 ? 101.899 146.334 174.568 1.00 161.53 ? 332 ASN D C   1 
ATOM   5385  O  O   . ASN B 2 332 ? 101.087 146.872 173.812 1.00 161.53 ? 332 ASN D O   1 
ATOM   5386  C  CB  . ASN B 2 332 ? 103.653 144.511 174.300 1.00 161.53 ? 332 ASN D CB  1 
ATOM   5387  C  CG  . ASN B 2 332 ? 104.481 144.555 175.576 1.00 161.53 ? 332 ASN D CG  1 
ATOM   5388  O  OD1 . ASN B 2 332 ? 104.709 143.525 176.209 1.00 161.53 ? 332 ASN D OD1 1 
ATOM   5389  N  ND2 . ASN B 2 332 ? 104.992 145.731 175.919 1.00 161.53 ? 332 ASN D ND2 1 
ATOM   5390  N  N   . ASP B 2 333 ? 102.596 147.019 175.476 1.00 153.69 ? 333 ASP D N   1 
ATOM   5391  C  CA  . ASP B 2 333 ? 102.472 148.467 175.593 1.00 153.69 ? 333 ASP D CA  1 
ATOM   5392  C  C   . ASP B 2 333 ? 102.994 149.170 174.346 1.00 153.69 ? 333 ASP D C   1 
ATOM   5393  O  O   . ASP B 2 333 ? 102.446 150.200 173.937 1.00 153.69 ? 333 ASP D O   1 
ATOM   5394  C  CB  . ASP B 2 333 ? 103.219 148.935 176.847 1.00 153.69 ? 333 ASP D CB  1 
ATOM   5395  C  CG  . ASP B 2 333 ? 102.918 150.380 177.226 1.00 153.69 ? 333 ASP D CG  1 
ATOM   5396  O  OD1 . ASP B 2 333 ? 102.782 151.246 176.340 1.00 153.69 ? 333 ASP D OD1 1 
ATOM   5397  O  OD2 . ASP B 2 333 ? 102.819 150.651 178.441 1.00 153.69 ? 333 ASP D OD2 1 
ATOM   5398  N  N   . TYR B 2 334 ? 104.020 148.609 173.707 1.00 143.45 ? 334 TYR D N   1 
ATOM   5399  C  CA  . TYR B 2 334 ? 104.668 149.221 172.553 1.00 143.45 ? 334 TYR D CA  1 
ATOM   5400  C  C   . TYR B 2 334 ? 104.484 148.380 171.294 1.00 143.45 ? 334 TYR D C   1 
ATOM   5401  O  O   . TYR B 2 334 ? 105.364 148.344 170.431 1.00 143.45 ? 334 TYR D O   1 
ATOM   5402  C  CB  . TYR B 2 334 ? 106.155 149.457 172.827 1.00 143.45 ? 334 TYR D CB  1 
ATOM   5403  C  CG  . TYR B 2 334 ? 106.462 149.967 174.222 1.00 143.45 ? 334 TYR D CG  1 
ATOM   5404  C  CD1 . TYR B 2 334 ? 106.548 149.097 175.303 1.00 143.45 ? 334 TYR D CD1 1 
ATOM   5405  C  CD2 . TYR B 2 334 ? 106.662 151.321 174.456 1.00 143.45 ? 334 TYR D CD2 1 
ATOM   5406  C  CE1 . TYR B 2 334 ? 106.823 149.561 176.574 1.00 143.45 ? 334 TYR D CE1 1 
ATOM   5407  C  CE2 . TYR B 2 334 ? 106.939 151.793 175.724 1.00 143.45 ? 334 TYR D CE2 1 
ATOM   5408  C  CZ  . TYR B 2 334 ? 107.019 150.910 176.779 1.00 143.45 ? 334 TYR D CZ  1 
ATOM   5409  O  OH  . TYR B 2 334 ? 107.294 151.377 178.042 1.00 143.45 ? 334 TYR D OH  1 
ATOM   5410  N  N   . PHE B 2 335 ? 103.348 147.685 171.191 1.00 148.67 ? 335 PHE D N   1 
ATOM   5411  C  CA  . PHE B 2 335 ? 103.098 146.825 170.038 1.00 148.67 ? 335 PHE D CA  1 
ATOM   5412  C  C   . PHE B 2 335 ? 103.159 147.606 168.732 1.00 148.67 ? 335 PHE D C   1 
ATOM   5413  O  O   . PHE B 2 335 ? 103.576 147.060 167.704 1.00 148.67 ? 335 PHE D O   1 
ATOM   5414  C  CB  . PHE B 2 335 ? 101.737 146.139 170.194 1.00 148.67 ? 335 PHE D CB  1 
ATOM   5415  C  CG  . PHE B 2 335 ? 101.486 145.032 169.203 1.00 148.67 ? 335 PHE D CG  1 
ATOM   5416  C  CD1 . PHE B 2 335 ? 101.095 145.314 167.903 1.00 148.67 ? 335 PHE D CD1 1 
ATOM   5417  C  CD2 . PHE B 2 335 ? 101.631 143.708 169.577 1.00 148.67 ? 335 PHE D CD2 1 
ATOM   5418  C  CE1 . PHE B 2 335 ? 100.863 144.300 166.997 1.00 148.67 ? 335 PHE D CE1 1 
ATOM   5419  C  CE2 . PHE B 2 335 ? 101.399 142.689 168.674 1.00 148.67 ? 335 PHE D CE2 1 
ATOM   5420  C  CZ  . PHE B 2 335 ? 101.014 142.987 167.383 1.00 148.67 ? 335 PHE D CZ  1 
ATOM   5421  N  N   . GLU B 2 336 ? 102.749 148.878 168.753 1.00 159.08 ? 336 GLU D N   1 
ATOM   5422  C  CA  . GLU B 2 336 ? 102.808 149.705 167.551 1.00 159.08 ? 336 GLU D CA  1 
ATOM   5423  C  C   . GLU B 2 336 ? 104.215 149.741 166.966 1.00 159.08 ? 336 GLU D C   1 
ATOM   5424  O  O   . GLU B 2 336 ? 104.389 149.741 165.742 1.00 159.08 ? 336 GLU D O   1 
ATOM   5425  C  CB  . GLU B 2 336 ? 102.323 151.121 167.866 1.00 159.08 ? 336 GLU D CB  1 
ATOM   5426  N  N   . TYR B 2 337 ? 105.233 149.780 167.829 1.00 151.76 ? 337 TYR D N   1 
ATOM   5427  C  CA  . TYR B 2 337 ? 106.610 149.711 167.351 1.00 151.76 ? 337 TYR D CA  1 
ATOM   5428  C  C   . TYR B 2 337 ? 106.908 148.360 166.712 1.00 151.76 ? 337 TYR D C   1 
ATOM   5429  O  O   . TYR B 2 337 ? 107.583 148.291 165.679 1.00 151.76 ? 337 TYR D O   1 
ATOM   5430  C  CB  . TYR B 2 337 ? 107.579 149.989 168.500 1.00 151.76 ? 337 TYR D CB  1 
ATOM   5431  N  N   . PHE B 2 338 ? 106.415 147.274 167.316 1.00 140.20 ? 338 PHE D N   1 
ATOM   5432  C  CA  . PHE B 2 338 ? 106.672 145.937 166.792 1.00 140.20 ? 338 PHE D CA  1 
ATOM   5433  C  C   . PHE B 2 338 ? 106.080 145.731 165.404 1.00 140.20 ? 338 PHE D C   1 
ATOM   5434  O  O   . PHE B 2 338 ? 106.545 144.855 164.667 1.00 140.20 ? 338 PHE D O   1 
ATOM   5435  C  CB  . PHE B 2 338 ? 106.120 144.885 167.754 1.00 140.20 ? 338 PHE D CB  1 
ATOM   5436  C  CG  . PHE B 2 338 ? 106.715 144.952 169.132 1.00 140.20 ? 338 PHE D CG  1 
ATOM   5437  C  CD1 . PHE B 2 338 ? 108.013 145.395 169.322 1.00 140.20 ? 338 PHE D CD1 1 
ATOM   5438  C  CD2 . PHE B 2 338 ? 105.972 144.581 170.239 1.00 140.20 ? 338 PHE D CD2 1 
ATOM   5439  C  CE1 . PHE B 2 338 ? 108.561 145.460 170.588 1.00 140.20 ? 338 PHE D CE1 1 
ATOM   5440  C  CE2 . PHE B 2 338 ? 106.515 144.643 171.508 1.00 140.20 ? 338 PHE D CE2 1 
ATOM   5441  C  CZ  . PHE B 2 338 ? 107.810 145.084 171.682 1.00 140.20 ? 338 PHE D CZ  1 
ATOM   5442  N  N   . GLY B 2 339 ? 105.071 146.514 165.033 1.00 152.60 ? 339 GLY D N   1 
ATOM   5443  C  CA  . GLY B 2 339 ? 104.585 146.545 163.676 1.00 152.60 ? 339 GLY D CA  1 
ATOM   5444  C  C   . GLY B 2 339 ? 103.649 145.403 163.334 1.00 152.60 ? 339 GLY D C   1 
ATOM   5445  O  O   . GLY B 2 339 ? 103.156 144.680 164.206 1.00 152.60 ? 339 GLY D O   1 
ATOM   5446  N  N   . PRO B 2 340 ? 103.388 145.227 162.036 1.00 166.01 ? 340 PRO D N   1 
ATOM   5447  C  CA  . PRO B 2 340 ? 102.411 144.213 161.608 1.00 166.01 ? 340 PRO D CA  1 
ATOM   5448  C  C   . PRO B 2 340 ? 102.849 142.782 161.866 1.00 166.01 ? 340 PRO D C   1 
ATOM   5449  O  O   . PRO B 2 340 ? 101.985 141.904 161.975 1.00 166.01 ? 340 PRO D O   1 
ATOM   5450  C  CB  . PRO B 2 340 ? 102.266 144.483 160.106 1.00 166.01 ? 340 PRO D CB  1 
ATOM   5451  C  CG  . PRO B 2 340 ? 103.576 145.078 159.712 1.00 166.01 ? 340 PRO D CG  1 
ATOM   5452  C  CD  . PRO B 2 340 ? 104.035 145.893 160.893 1.00 166.01 ? 340 PRO D CD  1 
ATOM   5453  N  N   . ASP B 2 341 ? 104.156 142.519 161.954 1.00 159.75 ? 341 ASP D N   1 
ATOM   5454  C  CA  . ASP B 2 341 ? 104.633 141.143 162.066 1.00 159.75 ? 341 ASP D CA  1 
ATOM   5455  C  C   . ASP B 2 341 ? 104.121 140.465 163.332 1.00 159.75 ? 341 ASP D C   1 
ATOM   5456  O  O   . ASP B 2 341 ? 103.689 139.307 163.287 1.00 159.75 ? 341 ASP D O   1 
ATOM   5457  C  CB  . ASP B 2 341 ? 106.160 141.116 162.026 1.00 159.75 ? 341 ASP D CB  1 
ATOM   5458  N  N   . PHE B 2 342 ? 104.170 141.161 164.469 1.00 141.18 ? 342 PHE D N   1 
ATOM   5459  C  CA  . PHE B 2 342 ? 103.773 140.662 165.785 1.00 141.18 ? 342 PHE D CA  1 
ATOM   5460  C  C   . PHE B 2 342 ? 104.668 139.534 166.286 1.00 141.18 ? 342 PHE D C   1 
ATOM   5461  O  O   . PHE B 2 342 ? 104.356 138.929 167.317 1.00 141.18 ? 342 PHE D O   1 
ATOM   5462  C  CB  . PHE B 2 342 ? 102.311 140.189 165.820 1.00 141.18 ? 342 PHE D CB  1 
ATOM   5463  N  N   . LYS B 2 343 ? 105.726 139.188 165.561 1.00 140.45 ? 343 LYS D N   1 
ATOM   5464  C  CA  . LYS B 2 343 ? 106.558 138.041 165.899 1.00 140.45 ? 343 LYS D CA  1 
ATOM   5465  C  C   . LYS B 2 343 ? 107.629 138.407 166.922 1.00 140.45 ? 343 LYS D C   1 
ATOM   5466  O  O   . LYS B 2 343 ? 108.165 139.518 166.915 1.00 140.45 ? 343 LYS D O   1 
ATOM   5467  C  CB  . LYS B 2 343 ? 107.217 137.475 164.641 1.00 140.45 ? 343 LYS D CB  1 
ATOM   5468  N  N   . LEU B 2 344 ? 107.935 137.459 167.812 1.00 126.85 ? 344 LEU D N   1 
ATOM   5469  C  CA  . LEU B 2 344 ? 108.989 137.659 168.800 1.00 126.85 ? 344 LEU D CA  1 
ATOM   5470  C  C   . LEU B 2 344 ? 110.366 137.454 168.195 1.00 126.85 ? 344 LEU D C   1 
ATOM   5471  O  O   . LEU B 2 344 ? 111.354 137.953 168.743 1.00 126.85 ? 344 LEU D O   1 
ATOM   5472  C  CB  . LEU B 2 344 ? 108.775 136.698 169.984 1.00 126.85 ? 344 LEU D CB  1 
ATOM   5473  C  CG  . LEU B 2 344 ? 109.581 136.544 171.294 1.00 126.85 ? 344 LEU D CG  1 
ATOM   5474  C  CD1 . LEU B 2 344 ? 111.022 136.098 171.086 1.00 126.85 ? 344 LEU D CD1 1 
ATOM   5475  C  CD2 . LEU B 2 344 ? 109.568 137.796 172.158 1.00 126.85 ? 344 LEU D CD2 1 
ATOM   5476  N  N   . HIS B 2 345 ? 110.443 136.802 167.043 1.00 120.65 ? 345 HIS D N   1 
ATOM   5477  C  CA  . HIS B 2 345 ? 111.701 136.560 166.364 1.00 120.65 ? 345 HIS D CA  1 
ATOM   5478  C  C   . HIS B 2 345 ? 111.802 137.474 165.151 1.00 120.65 ? 345 HIS D C   1 
ATOM   5479  O  O   . HIS B 2 345 ? 110.795 137.922 164.596 1.00 120.65 ? 345 HIS D O   1 
ATOM   5480  C  CB  . HIS B 2 345 ? 111.810 135.092 165.948 1.00 120.65 ? 345 HIS D CB  1 
ATOM   5481  C  CG  . HIS B 2 345 ? 112.282 134.196 167.050 1.00 120.65 ? 345 HIS D CG  1 
ATOM   5482  N  ND1 . HIS B 2 345 ? 111.423 133.398 167.775 1.00 120.65 ? 345 HIS D ND1 1 
ATOM   5483  C  CD2 . HIS B 2 345 ? 113.514 133.995 167.573 1.00 120.65 ? 345 HIS D CD2 1 
ATOM   5484  C  CE1 . HIS B 2 345 ? 112.108 132.729 168.685 1.00 120.65 ? 345 HIS D CE1 1 
ATOM   5485  N  NE2 . HIS B 2 345 ? 113.379 133.076 168.585 1.00 120.65 ? 345 HIS D NE2 1 
ATOM   5486  N  N   . ILE B 2 346 ? 113.035 137.746 164.737 1.00 118.85 ? 346 ILE D N   1 
ATOM   5487  C  CA  . ILE B 2 346 ? 113.311 138.622 163.607 1.00 118.85 ? 346 ILE D CA  1 
ATOM   5488  C  C   . ILE B 2 346 ? 113.991 137.806 162.516 1.00 118.85 ? 346 ILE D C   1 
ATOM   5489  O  O   . ILE B 2 346 ? 114.927 137.044 162.788 1.00 118.85 ? 346 ILE D O   1 
ATOM   5490  C  CB  . ILE B 2 346 ? 114.159 139.843 164.022 1.00 118.85 ? 346 ILE D CB  1 
ATOM   5491  C  CG1 . ILE B 2 346 ? 115.568 139.438 164.467 1.00 118.85 ? 346 ILE D CG1 1 
ATOM   5492  C  CG2 . ILE B 2 346 ? 113.462 140.619 165.129 1.00 118.85 ? 346 ILE D CG2 1 
ATOM   5493  C  CD1 . ILE B 2 346 ? 116.646 139.759 163.449 1.00 118.85 ? 346 ILE D CD1 1 
ATOM   5494  N  N   . SER B 2 347 ? 113.484 137.925 161.297 1.00 123.11 ? 347 SER D N   1 
ATOM   5495  C  CA  . SER B 2 347 ? 114.077 137.212 160.176 1.00 123.11 ? 347 SER D CA  1 
ATOM   5496  C  C   . SER B 2 347 ? 115.400 137.867 159.794 1.00 123.11 ? 347 SER D C   1 
ATOM   5497  O  O   . SER B 2 347 ? 115.472 139.098 159.707 1.00 123.11 ? 347 SER D O   1 
ATOM   5498  C  CB  . SER B 2 347 ? 113.125 137.209 158.982 1.00 123.11 ? 347 SER D CB  1 
ATOM   5499  O  OG  . SER B 2 347 ? 111.891 136.595 159.313 1.00 123.11 ? 347 SER D OG  1 
ATOM   5500  N  N   . PRO B 2 348 ? 116.460 137.091 159.572 1.00 130.84 ? 348 PRO D N   1 
ATOM   5501  C  CA  . PRO B 2 348 ? 117.755 137.692 159.239 1.00 130.84 ? 348 PRO D CA  1 
ATOM   5502  C  C   . PRO B 2 348 ? 117.709 138.422 157.906 1.00 130.84 ? 348 PRO D C   1 
ATOM   5503  O  O   . PRO B 2 348 ? 116.954 138.062 157.000 1.00 130.84 ? 348 PRO D O   1 
ATOM   5504  C  CB  . PRO B 2 348 ? 118.702 136.488 159.187 1.00 130.84 ? 348 PRO D CB  1 
ATOM   5505  C  CG  . PRO B 2 348 ? 117.816 135.331 158.874 1.00 130.84 ? 348 PRO D CG  1 
ATOM   5506  C  CD  . PRO B 2 348 ? 116.506 135.620 159.550 1.00 130.84 ? 348 PRO D CD  1 
ATOM   5507  N  N   . SER B 2 349 ? 118.530 139.463 157.796 1.00 117.53 ? 349 SER D N   1 
ATOM   5508  C  CA  . SER B 2 349 ? 118.600 140.236 156.568 1.00 117.53 ? 349 SER D CA  1 
ATOM   5509  C  C   . SER B 2 349 ? 119.334 139.441 155.489 1.00 117.53 ? 349 SER D C   1 
ATOM   5510  O  O   . SER B 2 349 ? 119.843 138.340 155.719 1.00 117.53 ? 349 SER D O   1 
ATOM   5511  C  CB  . SER B 2 349 ? 119.286 141.576 156.824 1.00 117.53 ? 349 SER D CB  1 
ATOM   5512  O  OG  . SER B 2 349 ? 120.507 141.397 157.519 1.00 117.53 ? 349 SER D OG  1 
ATOM   5513  N  N   . ASN B 2 350 ? 119.388 140.014 154.287 1.00 113.92 ? 350 ASN D N   1 
ATOM   5514  C  CA  . ASN B 2 350 ? 119.996 139.370 153.130 1.00 113.92 ? 350 ASN D CA  1 
ATOM   5515  C  C   . ASN B 2 350 ? 121.409 139.876 152.862 1.00 113.92 ? 350 ASN D C   1 
ATOM   5516  O  O   . ASN B 2 350 ? 121.841 139.926 151.706 1.00 113.92 ? 350 ASN D O   1 
ATOM   5517  C  CB  . ASN B 2 350 ? 119.118 139.566 151.894 1.00 113.92 ? 350 ASN D CB  1 
ATOM   5518  N  N   . MET B 2 351 ? 122.139 140.252 153.907 1.00 113.92 ? 351 MET D N   1 
ATOM   5519  C  CA  . MET B 2 351 ? 123.495 140.747 153.736 1.00 113.92 ? 351 MET D CA  1 
ATOM   5520  C  C   . MET B 2 351 ? 124.497 139.598 153.674 1.00 113.92 ? 351 MET D C   1 
ATOM   5521  O  O   . MET B 2 351 ? 124.288 138.527 154.251 1.00 113.92 ? 351 MET D O   1 
ATOM   5522  C  CB  . MET B 2 351 ? 123.854 141.702 154.875 1.00 113.92 ? 351 MET D CB  1 
ATOM   5523  C  CG  . MET B 2 351 ? 123.984 141.037 156.236 1.00 113.92 ? 351 MET D CG  1 
ATOM   5524  S  SD  . MET B 2 351 ? 124.721 142.110 157.483 1.00 113.92 ? 351 MET D SD  1 
ATOM   5525  C  CE  . MET B 2 351 ? 125.627 143.264 156.458 1.00 113.92 ? 351 MET D CE  1 
ATOM   5526  N  N   . THR B 2 352 ? 125.593 139.835 152.958 1.00 119.96 ? 352 THR D N   1 
ATOM   5527  C  CA  . THR B 2 352 ? 126.615 138.817 152.755 1.00 119.96 ? 352 THR D CA  1 
ATOM   5528  C  C   . THR B 2 352 ? 127.505 138.682 153.984 1.00 119.96 ? 352 THR D C   1 
ATOM   5529  O  O   . THR B 2 352 ? 127.842 139.672 154.640 1.00 119.96 ? 352 THR D O   1 
ATOM   5530  C  CB  . THR B 2 352 ? 127.468 139.149 151.531 1.00 119.96 ? 352 THR D CB  1 
ATOM   5531  O  OG1 . THR B 2 352 ? 128.406 140.180 151.865 1.00 119.96 ? 352 THR D OG1 1 
ATOM   5532  C  CG2 . THR B 2 352 ? 126.588 139.617 150.383 1.00 119.96 ? 352 THR D CG2 1 
ATOM   5533  N  N   . ASN B 2 353 ? 127.882 137.445 154.293 1.00 113.92 ? 353 ASN D N   1 
ATOM   5534  C  CA  . ASN B 2 353 ? 128.835 137.158 155.360 1.00 113.92 ? 353 ASN D CA  1 
ATOM   5535  C  C   . ASN B 2 353 ? 130.248 137.183 154.793 1.00 113.92 ? 353 ASN D C   1 
ATOM   5536  O  O   . ASN B 2 353 ? 130.611 136.333 153.974 1.00 113.92 ? 353 ASN D O   1 
ATOM   5537  C  CB  . ASN B 2 353 ? 128.540 135.805 155.995 1.00 113.92 ? 353 ASN D CB  1 
ATOM   5538  C  CG  . ASN B 2 353 ? 129.458 135.492 157.165 1.00 113.92 ? 353 ASN D CG  1 
ATOM   5539  O  OD1 . ASN B 2 353 ? 130.284 136.312 157.566 1.00 113.92 ? 353 ASN D OD1 1 
ATOM   5540  N  ND2 . ASN B 2 353 ? 129.313 134.296 157.721 1.00 113.92 ? 353 ASN D ND2 1 
ATOM   5541  N  N   . GLN B 2 354 ? 131.044 138.155 155.229 1.00 113.92 ? 354 GLN D N   1 
ATOM   5542  C  CA  . GLN B 2 354 ? 132.399 138.305 154.719 1.00 113.92 ? 354 GLN D CA  1 
ATOM   5543  C  C   . GLN B 2 354 ? 133.391 137.371 155.398 1.00 113.92 ? 354 GLN D C   1 
ATOM   5544  O  O   . GLN B 2 354 ? 134.554 137.325 154.984 1.00 113.92 ? 354 GLN D O   1 
ATOM   5545  C  CB  . GLN B 2 354 ? 132.861 139.755 154.875 1.00 113.92 ? 354 GLN D CB  1 
ATOM   5546  C  CG  . GLN B 2 354 ? 132.038 140.757 154.082 1.00 113.92 ? 354 GLN D CG  1 
ATOM   5547  C  CD  . GLN B 2 354 ? 132.347 140.729 152.597 1.00 113.92 ? 354 GLN D CD  1 
ATOM   5548  O  OE1 . GLN B 2 354 ? 133.208 139.978 152.141 1.00 113.92 ? 354 GLN D OE1 1 
ATOM   5549  N  NE2 . GLN B 2 354 ? 131.639 141.552 151.833 1.00 113.92 ? 354 GLN D NE2 1 
ATOM   5550  N  N   . ASN B 2 355 ? 132.967 136.628 156.421 1.00 113.94 ? 355 ASN D N   1 
ATOM   5551  C  CA  . ASN B 2 355 ? 133.862 135.735 157.156 1.00 113.94 ? 355 ASN D CA  1 
ATOM   5552  C  C   . ASN B 2 355 ? 133.814 134.363 156.498 1.00 113.94 ? 355 ASN D C   1 
ATOM   5553  O  O   . ASN B 2 355 ? 132.968 133.524 156.812 1.00 113.94 ? 355 ASN D O   1 
ATOM   5554  C  CB  . ASN B 2 355 ? 133.461 135.665 158.623 1.00 113.94 ? 355 ASN D CB  1 
ATOM   5555  C  CG  . ASN B 2 355 ? 133.199 137.029 159.219 1.00 113.94 ? 355 ASN D CG  1 
ATOM   5556  O  OD1 . ASN B 2 355 ? 132.583 137.887 158.588 1.00 113.94 ? 355 ASN D OD1 1 
ATOM   5557  N  ND2 . ASN B 2 355 ? 133.665 137.238 160.443 1.00 113.94 ? 355 ASN D ND2 1 
ATOM   5558  N  N   . THR B 2 356 ? 134.739 134.134 155.571 1.00 116.97 ? 356 THR D N   1 
ATOM   5559  C  CA  . THR B 2 356 ? 134.828 132.847 154.905 1.00 116.97 ? 356 THR D CA  1 
ATOM   5560  C  C   . THR B 2 356 ? 135.321 131.775 155.877 1.00 116.97 ? 356 THR D C   1 
ATOM   5561  O  O   . THR B 2 356 ? 136.016 132.082 156.849 1.00 116.97 ? 356 THR D O   1 
ATOM   5562  C  CB  . THR B 2 356 ? 135.768 132.935 153.707 1.00 116.97 ? 356 THR D CB  1 
ATOM   5563  O  OG1 . THR B 2 356 ? 137.081 133.293 154.154 1.00 116.97 ? 356 THR D OG1 1 
ATOM   5564  C  CG2 . THR B 2 356 ? 135.272 133.981 152.721 1.00 116.97 ? 356 THR D CG2 1 
ATOM   5565  N  N   . PRO B 2 357 ? 134.962 130.509 155.643 1.00 113.92 ? 357 PRO D N   1 
ATOM   5566  C  CA  . PRO B 2 357 ? 135.425 129.446 156.549 1.00 113.92 ? 357 PRO D CA  1 
ATOM   5567  C  C   . PRO B 2 357 ? 136.937 129.333 156.651 1.00 113.92 ? 357 PRO D C   1 
ATOM   5568  O  O   . PRO B 2 357 ? 137.435 128.957 157.716 1.00 113.92 ? 357 PRO D O   1 
ATOM   5569  C  CB  . PRO B 2 357 ? 134.796 128.176 155.956 1.00 113.92 ? 357 PRO D CB  1 
ATOM   5570  C  CG  . PRO B 2 357 ? 134.441 128.527 154.554 1.00 113.92 ? 357 PRO D CG  1 
ATOM   5571  C  CD  . PRO B 2 357 ? 134.100 129.983 154.572 1.00 113.92 ? 357 PRO D CD  1 
ATOM   5572  N  N   . GLU B 2 358 ? 137.687 129.608 155.579 1.00 113.92 ? 358 GLU D N   1 
ATOM   5573  C  CA  . GLU B 2 358 ? 139.145 129.564 155.678 1.00 113.92 ? 358 GLU D CA  1 
ATOM   5574  C  C   . GLU B 2 358 ? 139.674 130.621 156.643 1.00 113.92 ? 358 GLU D C   1 
ATOM   5575  O  O   . GLU B 2 358 ? 140.554 130.339 157.464 1.00 113.92 ? 358 GLU D O   1 
ATOM   5576  C  CB  . GLU B 2 358 ? 139.769 129.746 154.294 1.00 113.92 ? 358 GLU D CB  1 
ATOM   5577  N  N   . TYR B 2 359 ? 139.141 131.841 156.561 1.00 113.92 ? 359 TYR D N   1 
ATOM   5578  C  CA  . TYR B 2 359 ? 139.542 132.918 157.464 1.00 113.92 ? 359 TYR D CA  1 
ATOM   5579  C  C   . TYR B 2 359 ? 139.232 132.566 158.914 1.00 113.92 ? 359 TYR D C   1 
ATOM   5580  O  O   . TYR B 2 359 ? 140.082 132.701 159.807 1.00 113.92 ? 359 TYR D O   1 
ATOM   5581  C  CB  . TYR B 2 359 ? 138.826 134.201 157.039 1.00 113.92 ? 359 TYR D CB  1 
ATOM   5582  C  CG  . TYR B 2 359 ? 138.911 135.367 157.994 1.00 113.92 ? 359 TYR D CG  1 
ATOM   5583  C  CD1 . TYR B 2 359 ? 139.994 136.234 157.977 1.00 113.92 ? 359 TYR D CD1 1 
ATOM   5584  C  CD2 . TYR B 2 359 ? 137.881 135.623 158.889 1.00 113.92 ? 359 TYR D CD2 1 
ATOM   5585  C  CE1 . TYR B 2 359 ? 140.059 137.308 158.843 1.00 113.92 ? 359 TYR D CE1 1 
ATOM   5586  C  CE2 . TYR B 2 359 ? 137.937 136.691 159.756 1.00 113.92 ? 359 TYR D CE2 1 
ATOM   5587  C  CZ  . TYR B 2 359 ? 139.024 137.533 159.728 1.00 113.92 ? 359 TYR D CZ  1 
ATOM   5588  O  OH  . TYR B 2 359 ? 139.078 138.598 160.596 1.00 113.92 ? 359 TYR D OH  1 
ATOM   5589  N  N   . MET B 2 360 ? 138.009 132.099 159.154 1.00 114.69 ? 360 MET D N   1 
ATOM   5590  C  CA  . MET B 2 360 ? 137.575 131.707 160.487 1.00 114.69 ? 360 MET D CA  1 
ATOM   5591  C  C   . MET B 2 360 ? 138.426 130.562 161.026 1.00 114.69 ? 360 MET D C   1 
ATOM   5592  O  O   . MET B 2 360 ? 138.856 130.583 162.187 1.00 114.69 ? 360 MET D O   1 
ATOM   5593  C  CB  . MET B 2 360 ? 136.098 131.329 160.382 1.00 114.69 ? 360 MET D CB  1 
ATOM   5594  C  CG  . MET B 2 360 ? 135.207 132.555 160.156 1.00 114.69 ? 360 MET D CG  1 
ATOM   5595  S  SD  . MET B 2 360 ? 133.438 132.276 159.911 1.00 114.69 ? 360 MET D SD  1 
ATOM   5596  C  CE  . MET B 2 360 ? 133.313 130.507 160.090 1.00 114.69 ? 360 MET D CE  1 
ATOM   5597  N  N   . GLU B 2 361 ? 138.716 129.577 160.175 1.00 113.92 ? 361 GLU D N   1 
ATOM   5598  C  CA  . GLU B 2 361 ? 139.492 128.411 160.577 1.00 113.92 ? 361 GLU D CA  1 
ATOM   5599  C  C   . GLU B 2 361 ? 140.924 128.816 160.919 1.00 113.92 ? 361 GLU D C   1 
ATOM   5600  O  O   . GLU B 2 361 ? 141.481 128.377 161.931 1.00 113.92 ? 361 GLU D O   1 
ATOM   5601  C  CB  . GLU B 2 361 ? 139.453 127.397 159.427 1.00 113.92 ? 361 GLU D CB  1 
ATOM   5602  C  CG  . GLU B 2 361 ? 140.136 126.032 159.571 1.00 113.92 ? 361 GLU D CG  1 
ATOM   5603  C  CD  . GLU B 2 361 ? 140.194 125.499 160.989 1.00 113.92 ? 361 GLU D CD  1 
ATOM   5604  O  OE1 . GLU B 2 361 ? 139.355 124.640 161.327 1.00 113.92 ? 361 GLU D OE1 1 
ATOM   5605  O  OE2 . GLU B 2 361 ? 141.102 125.866 161.747 1.00 113.92 ? 361 GLU D OE2 1 
ATOM   5606  N  N   . LYS B 2 362 ? 141.513 129.704 160.110 1.00 113.92 ? 362 LYS D N   1 
ATOM   5607  C  CA  . LYS B 2 362 ? 142.872 130.175 160.361 1.00 113.92 ? 362 LYS D CA  1 
ATOM   5608  C  C   . LYS B 2 362 ? 142.962 130.955 161.665 1.00 113.92 ? 362 LYS D C   1 
ATOM   5609  O  O   . LYS B 2 362 ? 143.900 130.760 162.449 1.00 113.92 ? 362 LYS D O   1 
ATOM   5610  C  CB  . LYS B 2 362 ? 143.364 131.028 159.193 1.00 100.12 ? 362 LYS D CB  1 
ATOM   5611  C  CG  . LYS B 2 362 ? 144.541 130.420 158.453 1.00 100.12 ? 362 LYS D CG  1 
ATOM   5612  C  CD  . LYS B 2 362 ? 144.902 131.236 157.230 1.00 100.12 ? 362 LYS D CD  1 
ATOM   5613  C  CE  . LYS B 2 362 ? 146.073 130.627 156.484 1.00 100.12 ? 362 LYS D CE  1 
ATOM   5614  N  NZ  . LYS B 2 362 ? 147.279 130.517 157.349 1.00 100.12 ? 362 LYS D NZ  1 
ATOM   5615  N  N   . ILE B 2 363 ? 142.003 131.851 161.912 1.00 113.92 ? 363 ILE D N   1 
ATOM   5616  C  CA  . ILE B 2 363 ? 142.028 132.608 163.162 1.00 113.92 ? 363 ILE D CA  1 
ATOM   5617  C  C   . ILE B 2 363 ? 141.844 131.669 164.345 1.00 113.92 ? 363 ILE D C   1 
ATOM   5618  O  O   . ILE B 2 363 ? 142.460 131.849 165.403 1.00 113.92 ? 363 ILE D O   1 
ATOM   5619  C  CB  . ILE B 2 363 ? 140.970 133.725 163.146 1.00 113.92 ? 363 ILE D CB  1 
ATOM   5620  C  CG1 . ILE B 2 363 ? 141.317 134.759 162.078 1.00 113.92 ? 363 ILE D CG1 1 
ATOM   5621  C  CG2 . ILE B 2 363 ? 140.874 134.390 164.510 1.00 113.92 ? 363 ILE D CG2 1 
ATOM   5622  C  CD1 . ILE B 2 363 ? 140.613 136.076 162.260 1.00 113.92 ? 363 ILE D CD1 1 
ATOM   5623  N  N   . LYS B 2 364 ? 141.002 130.647 164.185 1.00 113.92 ? 364 LYS D N   1 
ATOM   5624  C  CA  . LYS B 2 364 ? 140.803 129.691 165.266 1.00 113.92 ? 364 LYS D CA  1 
ATOM   5625  C  C   . LYS B 2 364 ? 142.091 128.926 165.553 1.00 113.92 ? 364 LYS D C   1 
ATOM   5626  O  O   . LYS B 2 364 ? 142.425 128.670 166.716 1.00 113.92 ? 364 LYS D O   1 
ATOM   5627  C  CB  . LYS B 2 364 ? 139.659 128.744 164.908 1.00 106.98 ? 364 LYS D CB  1 
ATOM   5628  C  CG  . LYS B 2 364 ? 139.342 127.703 165.955 1.00 106.98 ? 364 LYS D CG  1 
ATOM   5629  C  CD  . LYS B 2 364 ? 137.867 127.346 165.923 1.00 106.98 ? 364 LYS D CD  1 
ATOM   5630  C  CE  . LYS B 2 364 ? 137.437 126.943 164.523 1.00 106.98 ? 364 LYS D CE  1 
ATOM   5631  N  NZ  . LYS B 2 364 ? 136.064 126.371 164.499 1.00 106.98 ? 364 LYS D NZ  1 
ATOM   5632  N  N   . GLN B 2 365 ? 142.832 128.557 164.503 1.00 113.92 ? 365 GLN D N   1 
ATOM   5633  C  CA  . GLN B 2 365 ? 144.116 127.888 164.710 1.00 113.92 ? 365 GLN D CA  1 
ATOM   5634  C  C   . GLN B 2 365 ? 145.126 128.800 165.390 1.00 113.92 ? 365 GLN D C   1 
ATOM   5635  O  O   . GLN B 2 365 ? 145.879 128.354 166.262 1.00 113.92 ? 365 GLN D O   1 
ATOM   5636  C  CB  . GLN B 2 365 ? 144.695 127.397 163.384 1.00 106.46 ? 365 GLN D CB  1 
ATOM   5637  C  CG  . GLN B 2 365 ? 143.909 126.306 162.715 1.00 106.46 ? 365 GLN D CG  1 
ATOM   5638  C  CD  . GLN B 2 365 ? 143.545 125.184 163.664 1.00 106.46 ? 365 GLN D CD  1 
ATOM   5639  O  OE1 . GLN B 2 365 ? 144.376 124.712 164.441 1.00 106.46 ? 365 GLN D OE1 1 
ATOM   5640  N  NE2 . GLN B 2 365 ? 142.291 124.752 163.610 1.00 106.46 ? 365 GLN D NE2 1 
ATOM   5641  N  N   . ARG B 2 366 ? 145.164 130.078 165.005 1.00 113.92 ? 366 ARG D N   1 
ATOM   5642  C  CA  . ARG B 2 366 ? 146.058 131.014 165.681 1.00 113.92 ? 366 ARG D CA  1 
ATOM   5643  C  C   . ARG B 2 366 ? 145.708 131.136 167.159 1.00 113.92 ? 366 ARG D C   1 
ATOM   5644  O  O   . ARG B 2 366 ? 146.598 131.163 168.019 1.00 113.92 ? 366 ARG D O   1 
ATOM   5645  C  CB  . ARG B 2 366 ? 146.019 132.381 164.997 1.00 113.92 ? 366 ARG D CB  1 
ATOM   5646  C  CG  . ARG B 2 366 ? 146.848 133.442 165.707 1.00 113.92 ? 366 ARG D CG  1 
ATOM   5647  C  CD  . ARG B 2 366 ? 148.341 133.146 165.623 1.00 113.92 ? 366 ARG D CD  1 
ATOM   5648  N  NE  . ARG B 2 366 ? 148.888 133.351 164.287 1.00 113.92 ? 366 ARG D NE  1 
ATOM   5649  C  CZ  . ARG B 2 366 ? 149.278 134.526 163.813 1.00 113.92 ? 366 ARG D CZ  1 
ATOM   5650  N  NH1 . ARG B 2 366 ? 149.201 135.627 164.543 1.00 113.92 ? 366 ARG D NH1 1 
ATOM   5651  N  NH2 . ARG B 2 366 ? 149.763 134.598 162.577 1.00 113.92 ? 366 ARG D NH2 1 
ATOM   5652  N  N   . LEU B 2 367 ? 144.413 131.225 167.473 1.00 113.92 ? 367 LEU D N   1 
ATOM   5653  C  CA  . LEU B 2 367 ? 143.997 131.327 168.868 1.00 113.92 ? 367 LEU D CA  1 
ATOM   5654  C  C   . LEU B 2 367 ? 144.337 130.061 169.650 1.00 113.92 ? 367 LEU D C   1 
ATOM   5655  O  O   . LEU B 2 367 ? 144.780 130.140 170.801 1.00 113.92 ? 367 LEU D O   1 
ATOM   5656  C  CB  . LEU B 2 367 ? 142.501 131.629 168.947 1.00 113.92 ? 367 LEU D CB  1 
ATOM   5657  C  CG  . LEU B 2 367 ? 142.096 133.100 169.064 1.00 113.92 ? 367 LEU D CG  1 
ATOM   5658  C  CD1 . LEU B 2 367 ? 142.619 133.918 167.899 1.00 113.92 ? 367 LEU D CD1 1 
ATOM   5659  C  CD2 . LEU B 2 367 ? 140.587 133.220 169.153 1.00 113.92 ? 367 LEU D CD2 1 
ATOM   5660  N  N   . PHE B 2 368 ? 144.151 128.885 169.041 1.00 113.92 ? 368 PHE D N   1 
ATOM   5661  C  CA  . PHE B 2 368 ? 144.554 127.647 169.703 1.00 113.92 ? 368 PHE D CA  1 
ATOM   5662  C  C   . PHE B 2 368 ? 146.055 127.624 169.956 1.00 113.92 ? 368 PHE D C   1 
ATOM   5663  O  O   . PHE B 2 368 ? 146.510 127.208 171.033 1.00 113.92 ? 368 PHE D O   1 
ATOM   5664  C  CB  . PHE B 2 368 ? 144.143 126.432 168.871 1.00 113.92 ? 368 PHE D CB  1 
ATOM   5665  C  CG  . PHE B 2 368 ? 142.661 126.199 168.817 1.00 113.92 ? 368 PHE D CG  1 
ATOM   5666  C  CD1 . PHE B 2 368 ? 141.826 126.736 169.781 1.00 113.92 ? 368 PHE D CD1 1 
ATOM   5667  C  CD2 . PHE B 2 368 ? 142.109 125.407 167.826 1.00 113.92 ? 368 PHE D CD2 1 
ATOM   5668  C  CE1 . PHE B 2 368 ? 140.463 126.511 169.739 1.00 113.92 ? 368 PHE D CE1 1 
ATOM   5669  C  CE2 . PHE B 2 368 ? 140.748 125.174 167.783 1.00 113.92 ? 368 PHE D CE2 1 
ATOM   5670  C  CZ  . PHE B 2 368 ? 139.925 125.728 168.741 1.00 113.92 ? 368 PHE D CZ  1 
ATOM   5671  N  N   . GLU B 2 369 ? 146.842 128.051 168.966 1.00 113.92 ? 369 GLU D N   1 
ATOM   5672  C  CA  . GLU B 2 369 ? 148.285 128.099 169.147 1.00 113.92 ? 369 GLU D CA  1 
ATOM   5673  C  C   . GLU B 2 369 ? 148.650 129.009 170.307 1.00 113.92 ? 369 GLU D C   1 
ATOM   5674  O  O   . GLU B 2 369 ? 149.405 128.615 171.195 1.00 113.92 ? 369 GLU D O   1 
ATOM   5675  C  CB  . GLU B 2 369 ? 148.972 128.562 167.862 1.00 111.13 ? 369 GLU D CB  1 
ATOM   5676  C  CG  . GLU B 2 369 ? 148.941 127.545 166.739 1.00 111.13 ? 369 GLU D CG  1 
ATOM   5677  C  CD  . GLU B 2 369 ? 149.321 128.146 165.403 1.00 111.13 ? 369 GLU D CD  1 
ATOM   5678  O  OE1 . GLU B 2 369 ? 149.895 129.254 165.394 1.00 111.13 ? 369 GLU D OE1 1 
ATOM   5679  O  OE2 . GLU B 2 369 ? 149.048 127.510 164.363 1.00 111.13 ? 369 GLU D OE2 1 
ATOM   5680  N  N   . ASN B 2 370 ? 148.051 130.200 170.363 1.00 114.23 ? 370 ASN D N   1 
ATOM   5681  C  CA  . ASN B 2 370 ? 148.351 131.119 171.458 1.00 114.23 ? 370 ASN D CA  1 
ATOM   5682  C  C   . ASN B 2 370 ? 147.906 130.555 172.801 1.00 114.23 ? 370 ASN D C   1 
ATOM   5683  O  O   . ASN B 2 370 ? 148.522 130.846 173.832 1.00 114.23 ? 370 ASN D O   1 
ATOM   5684  C  CB  . ASN B 2 370 ? 147.692 132.474 171.211 1.00 114.23 ? 370 ASN D CB  1 
ATOM   5685  C  CG  . ASN B 2 370 ? 148.388 133.272 170.129 1.00 114.23 ? 370 ASN D CG  1 
ATOM   5686  O  OD1 . ASN B 2 370 ? 149.304 134.046 170.405 1.00 114.23 ? 370 ASN D OD1 1 
ATOM   5687  N  ND2 . ASN B 2 370 ? 147.959 133.084 168.888 1.00 114.23 ? 370 ASN D ND2 1 
ATOM   5688  N  N   . LEU B 2 371 ? 146.844 129.750 172.810 1.00 115.68 ? 371 LEU D N   1 
ATOM   5689  C  CA  . LEU B 2 371 ? 146.380 129.151 174.055 1.00 115.68 ? 371 LEU D CA  1 
ATOM   5690  C  C   . LEU B 2 371 ? 147.302 128.029 174.517 1.00 115.68 ? 371 LEU D C   1 
ATOM   5691  O  O   . LEU B 2 371 ? 147.376 127.747 175.718 1.00 115.68 ? 371 LEU D O   1 
ATOM   5692  C  CB  . LEU B 2 371 ? 144.952 128.628 173.894 1.00 115.68 ? 371 LEU D CB  1 
ATOM   5693  C  CG  . LEU B 2 371 ? 143.835 129.672 173.869 1.00 115.68 ? 371 LEU D CG  1 
ATOM   5694  C  CD1 . LEU B 2 371 ? 142.588 129.092 173.227 1.00 115.68 ? 371 LEU D CD1 1 
ATOM   5695  C  CD2 . LEU B 2 371 ? 143.539 130.163 175.275 1.00 115.68 ? 371 LEU D CD2 1 
ATOM   5696  N  N   . ARG B 2 372 ? 148.005 127.378 173.588 1.00 125.08 ? 372 ARG D N   1 
ATOM   5697  C  CA  . ARG B 2 372 ? 148.937 126.326 173.995 1.00 125.08 ? 372 ARG D CA  1 
ATOM   5698  C  C   . ARG B 2 372 ? 150.098 126.823 174.865 1.00 125.08 ? 372 ARG D C   1 
ATOM   5699  O  O   . ARG B 2 372 ? 150.758 125.998 175.504 1.00 125.08 ? 372 ARG D O   1 
ATOM   5700  C  CB  . ARG B 2 372 ? 149.464 125.588 172.763 1.00 125.08 ? 372 ARG D CB  1 
ATOM   5701  C  CG  . ARG B 2 372 ? 148.387 124.783 172.045 1.00 125.08 ? 372 ARG D CG  1 
ATOM   5702  C  CD  . ARG B 2 372 ? 148.943 123.927 170.921 1.00 125.08 ? 372 ARG D CD  1 
ATOM   5703  N  NE  . ARG B 2 372 ? 147.920 123.606 169.933 1.00 125.08 ? 372 ARG D NE  1 
ATOM   5704  C  CZ  . ARG B 2 372 ? 147.972 123.952 168.655 1.00 125.08 ? 372 ARG D CZ  1 
ATOM   5705  N  NH1 . ARG B 2 372 ? 149.013 124.597 168.156 1.00 125.08 ? 372 ARG D NH1 1 
ATOM   5706  N  NH2 . ARG B 2 372 ? 146.967 123.617 167.851 1.00 125.08 ? 372 ARG D NH2 1 
ATOM   5707  N  N   . MET B 2 373 ? 150.380 128.127 174.911 1.00 122.81 ? 373 MET D N   1 
ATOM   5708  C  CA  . MET B 2 373 ? 151.429 128.649 175.787 1.00 122.81 ? 373 MET D CA  1 
ATOM   5709  C  C   . MET B 2 373 ? 150.916 128.993 177.178 1.00 122.81 ? 373 MET D C   1 
ATOM   5710  O  O   . MET B 2 373 ? 151.595 129.717 177.915 1.00 122.81 ? 373 MET D O   1 
ATOM   5711  C  CB  . MET B 2 373 ? 152.141 129.866 175.185 1.00 122.81 ? 373 MET D CB  1 
ATOM   5712  C  CG  . MET B 2 373 ? 152.800 129.679 173.835 1.00 122.81 ? 373 MET D CG  1 
ATOM   5713  S  SD  . MET B 2 373 ? 151.801 128.962 172.554 1.00 122.81 ? 373 MET D SD  1 
ATOM   5714  C  CE  . MET B 2 373 ? 152.721 129.427 171.091 1.00 122.81 ? 373 MET D CE  1 
ATOM   5715  N  N   . LEU B 2 374 ? 149.741 128.497 177.551 1.00 117.18 ? 374 LEU D N   1 
ATOM   5716  C  CA  . LEU B 2 374 ? 149.171 128.811 178.854 1.00 117.18 ? 374 LEU D CA  1 
ATOM   5717  C  C   . LEU B 2 374 ? 149.827 127.943 179.921 1.00 117.18 ? 374 LEU D C   1 
ATOM   5718  O  O   . LEU B 2 374 ? 149.747 126.712 179.838 1.00 117.18 ? 374 LEU D O   1 
ATOM   5719  C  CB  . LEU B 2 374 ? 147.663 128.583 178.847 1.00 117.18 ? 374 LEU D CB  1 
ATOM   5720  C  CG  . LEU B 2 374 ? 146.764 129.820 178.809 1.00 117.18 ? 374 LEU D CG  1 
ATOM   5721  C  CD1 . LEU B 2 374 ? 146.724 130.487 180.174 1.00 117.18 ? 374 LEU D CD1 1 
ATOM   5722  C  CD2 . LEU B 2 374 ? 147.232 130.791 177.744 1.00 117.18 ? 374 LEU D CD2 1 
ATOM   5723  N  N   . PRO B 2 375 ? 150.489 128.534 180.928 1.00 128.35 ? 375 PRO D N   1 
ATOM   5724  C  CA  . PRO B 2 375 ? 151.097 127.781 182.030 1.00 128.35 ? 375 PRO D CA  1 
ATOM   5725  C  C   . PRO B 2 375 ? 150.063 127.044 182.874 1.00 128.35 ? 375 PRO D C   1 
ATOM   5726  O  O   . PRO B 2 375 ? 149.830 125.860 182.631 1.00 128.35 ? 375 PRO D O   1 
ATOM   5727  C  CB  . PRO B 2 375 ? 151.796 128.867 182.858 1.00 128.35 ? 375 PRO D CB  1 
ATOM   5728  C  CG  . PRO B 2 375 ? 151.976 130.015 181.925 1.00 128.35 ? 375 PRO D CG  1 
ATOM   5729  C  CD  . PRO B 2 375 ? 150.788 129.973 181.014 1.00 128.35 ? 375 PRO D CD  1 
ATOM   5730  N  N   . PHE C 1 16  ? 166.409 127.653 126.636 1.00 117.67 ? 32  PHE C N   1 
ATOM   5731  C  CA  . PHE C 1 16  ? 167.534 127.437 125.732 1.00 117.67 ? 32  PHE C CA  1 
ATOM   5732  C  C   . PHE C 1 16  ? 167.136 126.710 124.452 1.00 117.67 ? 32  PHE C C   1 
ATOM   5733  O  O   . PHE C 1 16  ? 167.914 126.657 123.499 1.00 117.67 ? 32  PHE C O   1 
ATOM   5734  C  CB  . PHE C 1 16  ? 168.655 126.686 126.448 1.00 117.67 ? 32  PHE C CB  1 
ATOM   5735  C  CG  . PHE C 1 16  ? 169.589 127.585 127.207 1.00 117.67 ? 32  PHE C CG  1 
ATOM   5736  C  CD1 . PHE C 1 16  ? 169.274 128.028 128.479 1.00 117.67 ? 32  PHE C CD1 1 
ATOM   5737  C  CD2 . PHE C 1 16  ? 170.790 127.983 126.644 1.00 117.67 ? 32  PHE C CD2 1 
ATOM   5738  C  CE1 . PHE C 1 16  ? 170.138 128.856 129.172 1.00 117.67 ? 32  PHE C CE1 1 
ATOM   5739  C  CE2 . PHE C 1 16  ? 171.657 128.809 127.332 1.00 117.67 ? 32  PHE C CE2 1 
ATOM   5740  C  CZ  . PHE C 1 16  ? 171.331 129.246 128.598 1.00 117.67 ? 32  PHE C CZ  1 
ATOM   5741  N  N   . VAL C 1 17  ? 165.924 126.151 124.422 1.00 134.90 ? 33  VAL C N   1 
ATOM   5742  C  CA  . VAL C 1 17  ? 165.442 125.408 123.268 1.00 134.90 ? 33  VAL C CA  1 
ATOM   5743  C  C   . VAL C 1 17  ? 164.145 125.986 122.715 1.00 134.90 ? 33  VAL C C   1 
ATOM   5744  O  O   . VAL C 1 17  ? 164.004 126.141 121.497 1.00 134.90 ? 33  VAL C O   1 
ATOM   5745  C  CB  . VAL C 1 17  ? 165.264 123.912 123.607 1.00 134.90 ? 33  VAL C CB  1 
ATOM   5746  C  CG1 . VAL C 1 17  ? 166.594 123.185 123.506 1.00 134.90 ? 33  VAL C CG1 1 
ATOM   5747  C  CG2 . VAL C 1 17  ? 164.671 123.748 124.998 1.00 134.90 ? 33  VAL C CG2 1 
ATOM   5748  N  N   . ASN C 1 18  ? 163.184 126.308 123.579 1.00 141.07 ? 34  ASN C N   1 
ATOM   5749  C  CA  . ASN C 1 18  ? 161.881 126.767 123.115 1.00 141.07 ? 34  ASN C CA  1 
ATOM   5750  C  C   . ASN C 1 18  ? 161.311 127.802 124.073 1.00 141.07 ? 34  ASN C C   1 
ATOM   5751  O  O   . ASN C 1 18  ? 161.358 127.604 125.289 1.00 141.07 ? 34  ASN C O   1 
ATOM   5752  C  CB  . ASN C 1 18  ? 160.908 125.592 122.972 1.00 141.07 ? 34  ASN C CB  1 
ATOM   5753  C  CG  . ASN C 1 18  ? 159.457 126.024 123.049 1.00 141.07 ? 34  ASN C CG  1 
ATOM   5754  O  OD1 . ASN C 1 18  ? 158.911 126.583 122.098 1.00 141.07 ? 34  ASN C OD1 1 
ATOM   5755  N  ND2 . ASN C 1 18  ? 158.823 125.768 124.188 1.00 141.07 ? 34  ASN C ND2 1 
ATOM   5756  N  N   . TYR C 1 19  ? 160.800 128.904 123.525 1.00 133.58 ? 35  TYR C N   1 
ATOM   5757  C  CA  . TYR C 1 19  ? 160.142 129.953 124.299 1.00 133.58 ? 35  TYR C CA  1 
ATOM   5758  C  C   . TYR C 1 19  ? 159.364 130.796 123.300 1.00 133.58 ? 35  TYR C C   1 
ATOM   5759  O  O   . TYR C 1 19  ? 159.737 130.881 122.127 1.00 133.58 ? 35  TYR C O   1 
ATOM   5760  C  CB  . TYR C 1 19  ? 161.076 130.856 125.115 1.00 133.58 ? 35  TYR C CB  1 
ATOM   5761  C  CG  . TYR C 1 19  ? 162.011 131.721 124.317 1.00 133.58 ? 35  TYR C CG  1 
ATOM   5762  C  CD1 . TYR C 1 19  ? 162.899 131.183 123.409 1.00 133.58 ? 35  TYR C CD1 1 
ATOM   5763  C  CD2 . TYR C 1 19  ? 161.971 133.104 124.455 1.00 133.58 ? 35  TYR C CD2 1 
ATOM   5764  C  CE1 . TYR C 1 19  ? 163.734 131.992 122.682 1.00 133.58 ? 35  TYR C CE1 1 
ATOM   5765  C  CE2 . TYR C 1 19  ? 162.804 133.921 123.727 1.00 133.58 ? 35  TYR C CE2 1 
ATOM   5766  C  CZ  . TYR C 1 19  ? 163.686 133.359 122.837 1.00 133.58 ? 35  TYR C CZ  1 
ATOM   5767  O  OH  . TYR C 1 19  ? 164.530 134.162 122.104 1.00 133.58 ? 35  TYR C OH  1 
ATOM   5768  N  N   . THR C 1 20  ? 158.287 131.417 123.764 1.00 134.81 ? 36  THR C N   1 
ATOM   5769  C  CA  . THR C 1 20  ? 157.526 132.339 122.932 1.00 134.81 ? 36  THR C CA  1 
ATOM   5770  C  C   . THR C 1 20  ? 157.953 133.771 123.227 1.00 134.81 ? 36  THR C C   1 
ATOM   5771  O  O   . THR C 1 20  ? 158.039 134.176 124.391 1.00 134.81 ? 36  THR C O   1 
ATOM   5772  C  CB  . THR C 1 20  ? 156.024 132.180 123.170 1.00 134.81 ? 36  THR C CB  1 
ATOM   5773  N  N   . PHE C 1 21  ? 158.221 134.526 122.160 1.00 141.05 ? 37  PHE C N   1 
ATOM   5774  C  CA  . PHE C 1 21  ? 158.650 135.921 122.223 1.00 141.05 ? 37  PHE C CA  1 
ATOM   5775  C  C   . PHE C 1 21  ? 157.479 136.795 121.790 1.00 141.05 ? 37  PHE C C   1 
ATOM   5776  O  O   . PHE C 1 21  ? 157.082 136.783 120.620 1.00 141.05 ? 37  PHE C O   1 
ATOM   5777  C  CB  . PHE C 1 21  ? 159.887 136.126 121.343 1.00 141.05 ? 37  PHE C CB  1 
ATOM   5778  C  CG  . PHE C 1 21  ? 160.216 137.569 121.030 1.00 141.05 ? 37  PHE C CG  1 
ATOM   5779  C  CD1 . PHE C 1 21  ? 160.102 138.564 121.984 1.00 141.05 ? 37  PHE C CD1 1 
ATOM   5780  C  CD2 . PHE C 1 21  ? 160.687 137.915 119.776 1.00 141.05 ? 37  PHE C CD2 1 
ATOM   5781  C  CE1 . PHE C 1 21  ? 160.421 139.875 121.684 1.00 141.05 ? 37  PHE C CE1 1 
ATOM   5782  C  CE2 . PHE C 1 21  ? 161.006 139.222 119.470 1.00 141.05 ? 37  PHE C CE2 1 
ATOM   5783  C  CZ  . PHE C 1 21  ? 160.874 140.203 120.425 1.00 141.05 ? 37  PHE C CZ  1 
ATOM   5784  N  N   . LYS C 1 22  ? 156.934 137.553 122.739 1.00 127.71 ? 38  LYS C N   1 
ATOM   5785  C  CA  . LYS C 1 22  ? 155.843 138.490 122.499 1.00 127.71 ? 38  LYS C CA  1 
ATOM   5786  C  C   . LYS C 1 22  ? 156.383 139.903 122.676 1.00 127.71 ? 38  LYS C C   1 
ATOM   5787  O  O   . LYS C 1 22  ? 156.754 140.297 123.787 1.00 127.71 ? 38  LYS C O   1 
ATOM   5788  C  CB  . LYS C 1 22  ? 154.675 138.223 123.446 1.00 127.71 ? 38  LYS C CB  1 
ATOM   5789  N  N   . ASP C 1 23  ? 156.424 140.663 121.585 1.00 145.27 ? 39  ASP C N   1 
ATOM   5790  C  CA  . ASP C 1 23  ? 156.951 142.022 121.604 1.00 145.27 ? 39  ASP C CA  1 
ATOM   5791  C  C   . ASP C 1 23  ? 155.820 143.001 121.896 1.00 145.27 ? 39  ASP C C   1 
ATOM   5792  O  O   . ASP C 1 23  ? 154.988 143.282 121.028 1.00 145.27 ? 39  ASP C O   1 
ATOM   5793  C  CB  . ASP C 1 23  ? 157.617 142.335 120.268 1.00 145.27 ? 39  ASP C CB  1 
ATOM   5794  C  CG  . ASP C 1 23  ? 156.899 141.686 119.092 1.00 145.27 ? 39  ASP C CG  1 
ATOM   5795  O  OD1 . ASP C 1 23  ? 155.653 141.615 119.101 1.00 145.27 ? 39  ASP C OD1 1 
ATOM   5796  O  OD2 . ASP C 1 23  ? 157.580 141.237 118.153 1.00 145.27 ? 39  ASP C OD2 1 
ATOM   5797  N  N   . ARG C 1 24  ? 155.792 143.529 123.121 1.00 142.65 ? 40  ARG C N   1 
ATOM   5798  C  CA  . ARG C 1 24  ? 154.734 144.457 123.499 1.00 142.65 ? 40  ARG C CA  1 
ATOM   5799  C  C   . ARG C 1 24  ? 154.810 145.779 122.748 1.00 142.65 ? 40  ARG C C   1 
ATOM   5800  O  O   . ARG C 1 24  ? 153.831 146.533 122.756 1.00 142.65 ? 40  ARG C O   1 
ATOM   5801  C  CB  . ARG C 1 24  ? 154.781 144.715 125.006 1.00 142.65 ? 40  ARG C CB  1 
ATOM   5802  N  N   . SER C 1 25  ? 155.938 146.079 122.106 1.00 148.74 ? 41  SER C N   1 
ATOM   5803  C  CA  . SER C 1 25  ? 156.135 147.337 121.399 1.00 148.74 ? 41  SER C CA  1 
ATOM   5804  C  C   . SER C 1 25  ? 155.911 147.219 119.897 1.00 148.74 ? 41  SER C C   1 
ATOM   5805  O  O   . SER C 1 25  ? 156.158 148.186 119.170 1.00 148.74 ? 41  SER C O   1 
ATOM   5806  C  CB  . SER C 1 25  ? 157.537 147.881 121.678 1.00 148.74 ? 41  SER C CB  1 
ATOM   5807  O  OG  . SER C 1 25  ? 157.723 148.125 123.062 1.00 148.74 ? 41  SER C OG  1 
ATOM   5808  N  N   . HIS C 1 26  ? 155.464 146.058 119.414 1.00 138.10 ? 42  HIS C N   1 
ATOM   5809  C  CA  . HIS C 1 26  ? 155.214 145.898 117.984 1.00 138.10 ? 42  HIS C CA  1 
ATOM   5810  C  C   . HIS C 1 26  ? 154.142 146.867 117.499 1.00 138.10 ? 42  HIS C C   1 
ATOM   5811  O  O   . HIS C 1 26  ? 154.313 147.539 116.474 1.00 138.10 ? 42  HIS C O   1 
ATOM   5812  C  CB  . HIS C 1 26  ? 154.814 144.454 117.682 1.00 138.10 ? 42  HIS C CB  1 
ATOM   5813  C  CG  . HIS C 1 26  ? 154.043 144.295 116.408 1.00 138.10 ? 42  HIS C CG  1 
ATOM   5814  N  ND1 . HIS C 1 26  ? 154.597 144.538 115.170 1.00 138.10 ? 42  HIS C ND1 1 
ATOM   5815  C  CD2 . HIS C 1 26  ? 152.764 143.915 116.180 1.00 138.10 ? 42  HIS C CD2 1 
ATOM   5816  C  CE1 . HIS C 1 26  ? 153.692 144.316 114.234 1.00 138.10 ? 42  HIS C CE1 1 
ATOM   5817  N  NE2 . HIS C 1 26  ? 152.571 143.937 114.820 1.00 138.10 ? 42  HIS C NE2 1 
ATOM   5818  N  N   . SER C 1 27  ? 153.026 146.952 118.228 1.00 140.75 ? 43  SER C N   1 
ATOM   5819  C  CA  . SER C 1 27  ? 151.942 147.840 117.824 1.00 140.75 ? 43  SER C CA  1 
ATOM   5820  C  C   . SER C 1 27  ? 152.387 149.297 117.831 1.00 140.75 ? 43  SER C C   1 
ATOM   5821  O  O   . SER C 1 27  ? 152.087 150.049 116.897 1.00 140.75 ? 43  SER C O   1 
ATOM   5822  C  CB  . SER C 1 27  ? 150.734 147.643 118.739 1.00 140.75 ? 43  SER C CB  1 
ATOM   5823  O  OG  . SER C 1 27  ? 151.058 147.948 120.084 1.00 140.75 ? 43  SER C OG  1 
ATOM   5824  N  N   . GLY C 1 28  ? 153.109 149.712 118.873 1.00 138.73 ? 44  GLY C N   1 
ATOM   5825  C  CA  . GLY C 1 28  ? 153.592 151.082 118.922 1.00 138.73 ? 44  GLY C CA  1 
ATOM   5826  C  C   . GLY C 1 28  ? 154.523 151.407 117.770 1.00 138.73 ? 44  GLY C C   1 
ATOM   5827  O  O   . GLY C 1 28  ? 154.391 152.449 117.120 1.00 138.73 ? 44  GLY C O   1 
ATOM   5828  N  N   . ARG C 1 29  ? 155.478 150.512 117.500 1.00 131.02 ? 45  ARG C N   1 
ATOM   5829  C  CA  . ARG C 1 29  ? 156.426 150.742 116.415 1.00 131.02 ? 45  ARG C CA  1 
ATOM   5830  C  C   . ARG C 1 29  ? 155.711 150.831 115.073 1.00 131.02 ? 45  ARG C C   1 
ATOM   5831  O  O   . ARG C 1 29  ? 155.973 151.742 114.278 1.00 131.02 ? 45  ARG C O   1 
ATOM   5832  C  CB  . ARG C 1 29  ? 157.482 149.634 116.385 1.00 131.02 ? 45  ARG C CB  1 
ATOM   5833  C  CG  . ARG C 1 29  ? 158.525 149.717 117.490 1.00 131.02 ? 45  ARG C CG  1 
ATOM   5834  C  CD  . ARG C 1 29  ? 159.703 148.796 117.197 1.00 131.02 ? 45  ARG C CD  1 
ATOM   5835  N  NE  . ARG C 1 29  ? 159.294 147.410 117.004 1.00 131.02 ? 45  ARG C NE  1 
ATOM   5836  C  CZ  . ARG C 1 29  ? 159.170 146.520 117.979 1.00 131.02 ? 45  ARG C CZ  1 
ATOM   5837  N  NH1 . ARG C 1 29  ? 159.418 146.836 119.239 1.00 131.02 ? 45  ARG C NH1 1 
ATOM   5838  N  NH2 . ARG C 1 29  ? 158.790 145.281 117.682 1.00 131.02 ? 45  ARG C NH2 1 
ATOM   5839  N  N   . VAL C 1 30  ? 154.804 149.889 114.801 1.00 127.75 ? 46  VAL C N   1 
ATOM   5840  C  CA  . VAL C 1 30  ? 154.131 149.883 113.506 1.00 127.75 ? 46  VAL C CA  1 
ATOM   5841  C  C   . VAL C 1 30  ? 153.245 151.115 113.357 1.00 127.75 ? 46  VAL C C   1 
ATOM   5842  O  O   . VAL C 1 30  ? 153.185 151.719 112.280 1.00 127.75 ? 46  VAL C O   1 
ATOM   5843  C  CB  . VAL C 1 30  ? 153.351 148.570 113.287 1.00 127.75 ? 46  VAL C CB  1 
ATOM   5844  C  CG1 . VAL C 1 30  ? 152.191 148.429 114.256 1.00 127.75 ? 46  VAL C CG1 1 
ATOM   5845  C  CG2 . VAL C 1 30  ? 152.863 148.479 111.847 1.00 127.75 ? 46  VAL C CG2 1 
ATOM   5846  N  N   . ALA C 1 31  ? 152.554 151.520 114.429 1.00 124.00 ? 47  ALA C N   1 
ATOM   5847  C  CA  . ALA C 1 31  ? 151.698 152.699 114.357 1.00 124.00 ? 47  ALA C CA  1 
ATOM   5848  C  C   . ALA C 1 31  ? 152.520 153.957 114.106 1.00 124.00 ? 47  ALA C C   1 
ATOM   5849  O  O   . ALA C 1 31  ? 152.168 154.787 113.258 1.00 124.00 ? 47  ALA C O   1 
ATOM   5850  C  CB  . ALA C 1 31  ? 150.881 152.833 115.642 1.00 124.00 ? 47  ALA C CB  1 
ATOM   5851  N  N   . GLN C 1 32  ? 153.623 154.119 114.840 1.00 124.66 ? 48  GLN C N   1 
ATOM   5852  C  CA  . GLN C 1 32  ? 154.458 155.297 114.639 1.00 124.66 ? 48  GLN C CA  1 
ATOM   5853  C  C   . GLN C 1 32  ? 155.029 155.326 113.228 1.00 124.66 ? 48  GLN C C   1 
ATOM   5854  O  O   . GLN C 1 32  ? 155.048 156.379 112.578 1.00 124.66 ? 48  GLN C O   1 
ATOM   5855  C  CB  . GLN C 1 32  ? 155.579 155.329 115.677 1.00 124.66 ? 48  GLN C CB  1 
ATOM   5856  N  N   . GLY C 1 33  ? 155.504 154.179 112.736 1.00 134.24 ? 49  GLY C N   1 
ATOM   5857  C  CA  . GLY C 1 33  ? 156.047 154.139 111.390 1.00 134.24 ? 49  GLY C CA  1 
ATOM   5858  C  C   . GLY C 1 33  ? 155.022 154.422 110.308 1.00 134.24 ? 49  GLY C C   1 
ATOM   5859  O  O   . GLY C 1 33  ? 155.308 155.150 109.354 1.00 134.24 ? 49  GLY C O   1 
ATOM   5860  N  N   . ILE C 1 34  ? 153.813 153.863 110.433 1.00 125.67 ? 50  ILE C N   1 
ATOM   5861  C  CA  . ILE C 1 34  ? 152.784 154.158 109.438 1.00 125.67 ? 50  ILE C CA  1 
ATOM   5862  C  C   . ILE C 1 34  ? 152.441 155.642 109.468 1.00 125.67 ? 50  ILE C C   1 
ATOM   5863  O  O   . ILE C 1 34  ? 152.332 156.288 108.421 1.00 125.67 ? 50  ILE C O   1 
ATOM   5864  C  CB  . ILE C 1 34  ? 151.547 153.244 109.598 1.00 125.67 ? 50  ILE C CB  1 
ATOM   5865  C  CG1 . ILE C 1 34  ? 150.870 153.325 110.971 1.00 125.67 ? 50  ILE C CG1 1 
ATOM   5866  C  CG2 . ILE C 1 34  ? 151.912 151.797 109.280 1.00 125.67 ? 50  ILE C CG2 1 
ATOM   5867  C  CD1 . ILE C 1 34  ? 149.802 154.403 111.106 1.00 125.67 ? 50  ILE C CD1 1 
ATOM   5868  N  N   . MET C 1 35  ? 152.265 156.203 110.670 1.00 131.26 ? 51  MET C N   1 
ATOM   5869  C  CA  . MET C 1 35  ? 152.015 157.636 110.790 1.00 131.26 ? 51  MET C CA  1 
ATOM   5870  C  C   . MET C 1 35  ? 153.084 158.438 110.057 1.00 131.26 ? 51  MET C C   1 
ATOM   5871  O  O   . MET C 1 35  ? 152.774 159.276 109.201 1.00 131.26 ? 51  MET C O   1 
ATOM   5872  C  CB  . MET C 1 35  ? 151.958 158.035 112.266 1.00 131.26 ? 51  MET C CB  1 
ATOM   5873  C  CG  . MET C 1 35  ? 152.188 159.518 112.518 1.00 131.26 ? 51  MET C CG  1 
ATOM   5874  S  SD  . MET C 1 35  ? 152.184 159.963 114.268 1.00 131.26 ? 51  MET C SD  1 
ATOM   5875  C  CE  . MET C 1 35  ? 151.364 158.544 114.992 1.00 131.26 ? 51  MET C CE  1 
ATOM   5876  N  N   . LYS C 1 36  ? 154.356 158.174 110.373 1.00 126.20 ? 52  LYS C N   1 
ATOM   5877  C  CA  . LYS C 1 36  ? 155.448 158.958 109.802 1.00 126.20 ? 52  LYS C CA  1 
ATOM   5878  C  C   . LYS C 1 36  ? 155.484 158.828 108.284 1.00 126.20 ? 52  LYS C C   1 
ATOM   5879  O  O   . LYS C 1 36  ? 155.497 159.834 107.565 1.00 126.20 ? 52  LYS C O   1 
ATOM   5880  C  CB  . LYS C 1 36  ? 156.779 158.525 110.415 1.00 126.20 ? 52  LYS C CB  1 
ATOM   5881  N  N   . LEU C 1 37  ? 155.499 157.594 107.774 1.00 118.21 ? 53  LEU C N   1 
ATOM   5882  C  CA  . LEU C 1 37  ? 155.638 157.415 106.332 1.00 118.21 ? 53  LEU C CA  1 
ATOM   5883  C  C   . LEU C 1 37  ? 154.435 157.975 105.582 1.00 118.21 ? 53  LEU C C   1 
ATOM   5884  O  O   . LEU C 1 37  ? 154.602 158.635 104.552 1.00 118.21 ? 53  LEU C O   1 
ATOM   5885  C  CB  . LEU C 1 37  ? 155.868 155.944 105.982 1.00 118.21 ? 53  LEU C CB  1 
ATOM   5886  C  CG  . LEU C 1 37  ? 157.313 155.437 106.089 1.00 118.21 ? 53  LEU C CG  1 
ATOM   5887  C  CD1 . LEU C 1 37  ? 157.690 154.968 107.483 1.00 118.21 ? 53  LEU C CD1 1 
ATOM   5888  C  CD2 . LEU C 1 37  ? 157.553 154.332 105.069 1.00 118.21 ? 53  LEU C CD2 1 
ATOM   5889  N  N   . CYS C 1 38  ? 153.217 157.735 106.076 1.00 127.38 ? 54  CYS C N   1 
ATOM   5890  C  CA  . CYS C 1 38  ? 152.037 158.230 105.377 1.00 127.38 ? 54  CYS C CA  1 
ATOM   5891  C  C   . CYS C 1 38  ? 151.992 159.754 105.377 1.00 127.38 ? 54  CYS C C   1 
ATOM   5892  O  O   . CYS C 1 38  ? 151.759 160.374 104.332 1.00 127.38 ? 54  CYS C O   1 
ATOM   5893  C  CB  . CYS C 1 38  ? 150.769 157.650 106.007 1.00 127.38 ? 54  CYS C CB  1 
ATOM   5894  S  SG  . CYS C 1 38  ? 150.606 155.856 105.849 1.00 127.38 ? 54  CYS C SG  1 
ATOM   5895  N  N   . LEU C 1 39  ? 152.203 160.381 106.540 1.00 138.45 ? 55  LEU C N   1 
ATOM   5896  C  CA  . LEU C 1 39  ? 152.138 161.838 106.608 1.00 138.45 ? 55  LEU C CA  1 
ATOM   5897  C  C   . LEU C 1 39  ? 153.243 162.494 105.783 1.00 138.45 ? 55  LEU C C   1 
ATOM   5898  O  O   . LEU C 1 39  ? 153.000 163.498 105.103 1.00 138.45 ? 55  LEU C O   1 
ATOM   5899  C  CB  . LEU C 1 39  ? 152.196 162.297 108.065 1.00 138.45 ? 55  LEU C CB  1 
ATOM   5900  N  N   . GLU C 1 40  ? 154.460 161.949 105.825 1.00 141.31 ? 56  GLU C N   1 
ATOM   5901  C  CA  . GLU C 1 40  ? 155.592 162.569 105.144 1.00 141.31 ? 56  GLU C CA  1 
ATOM   5902  C  C   . GLU C 1 40  ? 155.744 162.152 103.685 1.00 141.31 ? 56  GLU C C   1 
ATOM   5903  O  O   . GLU C 1 40  ? 156.627 162.679 103.001 1.00 141.31 ? 56  GLU C O   1 
ATOM   5904  C  CB  . GLU C 1 40  ? 156.903 162.280 105.893 1.00 141.31 ? 56  GLU C CB  1 
ATOM   5905  C  CG  . GLU C 1 40  ? 157.225 163.200 107.086 1.00 141.31 ? 56  GLU C CG  1 
ATOM   5906  C  CD  . GLU C 1 40  ? 156.183 163.218 108.194 1.00 141.31 ? 56  GLU C CD  1 
ATOM   5907  O  OE1 . GLU C 1 40  ? 155.238 162.411 108.164 1.00 141.31 ? 56  GLU C OE1 1 
ATOM   5908  O  OE2 . GLU C 1 40  ? 156.316 164.058 109.108 1.00 141.31 ? 56  GLU C OE2 1 
ATOM   5909  N  N   . GLU C 1 41  ? 154.924 161.232 103.185 1.00 137.13 ? 57  GLU C N   1 
ATOM   5910  C  CA  . GLU C 1 41  ? 155.022 160.841 101.779 1.00 137.13 ? 57  GLU C CA  1 
ATOM   5911  C  C   . GLU C 1 41  ? 153.996 161.587 100.934 1.00 137.13 ? 57  GLU C C   1 
ATOM   5912  O  O   . GLU C 1 41  ? 154.083 161.600 99.706  1.00 137.13 ? 57  GLU C O   1 
ATOM   5913  C  CB  . GLU C 1 41  ? 154.835 159.333 101.611 1.00 137.13 ? 57  GLU C CB  1 
ATOM   5914  N  N   . ARG C 1 60  ? 145.096 152.579 102.345 1.00 118.30 ? 76  ARG C N   1 
ATOM   5915  C  CA  . ARG C 1 60  ? 143.851 151.849 102.550 1.00 118.30 ? 76  ARG C CA  1 
ATOM   5916  C  C   . ARG C 1 60  ? 143.898 151.004 103.819 1.00 118.30 ? 76  ARG C C   1 
ATOM   5917  O  O   . ARG C 1 60  ? 142.880 150.816 104.483 1.00 118.30 ? 76  ARG C O   1 
ATOM   5918  C  CB  . ARG C 1 60  ? 143.543 150.963 101.341 1.00 118.30 ? 76  ARG C CB  1 
ATOM   5919  C  CG  . ARG C 1 60  ? 144.628 149.950 101.015 1.00 118.30 ? 76  ARG C CG  1 
ATOM   5920  C  CD  . ARG C 1 60  ? 144.217 149.044 99.867  1.00 118.30 ? 76  ARG C CD  1 
ATOM   5921  N  NE  . ARG C 1 60  ? 143.057 148.228 100.205 1.00 118.30 ? 76  ARG C NE  1 
ATOM   5922  C  CZ  . ARG C 1 60  ? 143.103 147.135 100.956 1.00 118.30 ? 76  ARG C CZ  1 
ATOM   5923  N  NH1 . ARG C 1 60  ? 144.238 146.705 101.481 1.00 118.30 ? 76  ARG C NH1 1 
ATOM   5924  N  NH2 . ARG C 1 60  ? 141.981 146.461 101.189 1.00 118.30 ? 76  ARG C NH2 1 
ATOM   5925  N  N   . LEU C 1 61  ? 145.087 150.493 104.146 1.00 123.63 ? 77  LEU C N   1 
ATOM   5926  C  CA  . LEU C 1 61  ? 145.226 149.632 105.316 1.00 123.63 ? 77  LEU C CA  1 
ATOM   5927  C  C   . LEU C 1 61  ? 144.922 150.387 106.604 1.00 123.63 ? 77  LEU C C   1 
ATOM   5928  O  O   . LEU C 1 61  ? 144.280 149.846 107.511 1.00 123.63 ? 77  LEU C O   1 
ATOM   5929  C  CB  . LEU C 1 61  ? 146.633 149.035 105.362 1.00 123.63 ? 77  LEU C CB  1 
ATOM   5930  N  N   . VAL C 1 62  ? 145.383 151.636 106.704 1.00 117.45 ? 78  VAL C N   1 
ATOM   5931  C  CA  . VAL C 1 62  ? 145.193 152.409 107.930 1.00 117.45 ? 78  VAL C CA  1 
ATOM   5932  C  C   . VAL C 1 62  ? 143.709 152.629 108.200 1.00 117.45 ? 78  VAL C C   1 
ATOM   5933  O  O   . VAL C 1 62  ? 143.236 152.474 109.333 1.00 117.45 ? 78  VAL C O   1 
ATOM   5934  C  CB  . VAL C 1 62  ? 145.955 153.744 107.845 1.00 117.45 ? 78  VAL C CB  1 
ATOM   5935  N  N   . LEU C 1 63  ? 142.953 152.998 107.164 1.00 135.60 ? 79  LEU C N   1 
ATOM   5936  C  CA  . LEU C 1 63  ? 141.523 153.229 107.344 1.00 135.60 ? 79  LEU C CA  1 
ATOM   5937  C  C   . LEU C 1 63  ? 140.772 151.921 107.547 1.00 135.60 ? 79  LEU C C   1 
ATOM   5938  O  O   . LEU C 1 63  ? 139.903 151.827 108.422 1.00 135.60 ? 79  LEU C O   1 
ATOM   5939  C  CB  . LEU C 1 63  ? 140.962 153.993 106.145 1.00 135.60 ? 79  LEU C CB  1 
ATOM   5940  N  N   . SER C 1 64  ? 141.087 150.902 106.744 1.00 129.66 ? 80  SER C N   1 
ATOM   5941  C  CA  . SER C 1 64  ? 140.392 149.624 106.859 1.00 129.66 ? 80  SER C CA  1 
ATOM   5942  C  C   . SER C 1 64  ? 140.629 148.974 108.216 1.00 129.66 ? 80  SER C C   1 
ATOM   5943  O  O   . SER C 1 64  ? 139.798 148.184 108.677 1.00 129.66 ? 80  SER C O   1 
ATOM   5944  C  CB  . SER C 1 64  ? 140.829 148.686 105.735 1.00 129.66 ? 80  SER C CB  1 
ATOM   5945  O  OG  . SER C 1 64  ? 140.563 149.256 104.466 1.00 129.66 ? 80  SER C OG  1 
ATOM   5946  N  N   . ALA C 1 65  ? 141.751 149.285 108.866 1.00 128.33 ? 81  ALA C N   1 
ATOM   5947  C  CA  . ALA C 1 65  ? 142.033 148.733 110.185 1.00 128.33 ? 81  ALA C CA  1 
ATOM   5948  C  C   . ALA C 1 65  ? 141.259 149.425 111.297 1.00 128.33 ? 81  ALA C C   1 
ATOM   5949  O  O   . ALA C 1 65  ? 141.284 148.948 112.437 1.00 128.33 ? 81  ALA C O   1 
ATOM   5950  C  CB  . ALA C 1 65  ? 143.532 148.825 110.479 1.00 128.33 ? 81  ALA C CB  1 
ATOM   5951  N  N   . GLN C 1 66  ? 140.579 150.527 110.998 1.00 127.37 ? 82  GLN C N   1 
ATOM   5952  C  CA  . GLN C 1 66  ? 139.781 151.255 111.974 1.00 127.37 ? 82  GLN C CA  1 
ATOM   5953  C  C   . GLN C 1 66  ? 138.297 151.268 111.655 1.00 127.37 ? 82  GLN C C   1 
ATOM   5954  O  O   . GLN C 1 66  ? 137.480 151.276 112.578 1.00 127.37 ? 82  GLN C O   1 
ATOM   5955  C  CB  . GLN C 1 66  ? 140.263 152.711 112.080 1.00 127.37 ? 82  GLN C CB  1 
ATOM   5956  C  CG  . GLN C 1 66  ? 141.668 152.882 112.624 1.00 127.37 ? 82  GLN C CG  1 
ATOM   5957  C  CD  . GLN C 1 66  ? 141.674 153.403 114.046 1.00 127.37 ? 82  GLN C CD  1 
ATOM   5958  O  OE1 . GLN C 1 66  ? 141.179 152.748 114.962 1.00 127.37 ? 82  GLN C OE1 1 
ATOM   5959  N  NE2 . GLN C 1 66  ? 142.224 154.596 114.236 1.00 127.37 ? 82  GLN C NE2 1 
ATOM   5960  N  N   . SER C 1 67  ? 137.932 151.270 110.377 1.00 141.44 ? 83  SER C N   1 
ATOM   5961  C  CA  . SER C 1 67  ? 136.553 151.406 109.934 1.00 141.44 ? 83  SER C CA  1 
ATOM   5962  C  C   . SER C 1 67  ? 136.152 150.229 109.056 1.00 141.44 ? 83  SER C C   1 
ATOM   5963  O  O   . SER C 1 67  ? 136.845 149.906 108.086 1.00 141.44 ? 83  SER C O   1 
ATOM   5964  C  CB  . SER C 1 67  ? 136.378 152.717 109.179 1.00 141.44 ? 83  SER C CB  1 
ATOM   5965  O  OG  . SER C 1 67  ? 136.934 152.610 107.895 1.00 141.44 ? 83  SER C OG  1 
ATOM   5966  N  N   . CYS C 1 68  ? 135.031 149.595 109.403 1.00 148.19 ? 84  CYS C N   1 
ATOM   5967  C  CA  . CYS C 1 68  ? 134.518 148.481 108.611 1.00 148.19 ? 84  CYS C CA  1 
ATOM   5968  C  C   . CYS C 1 68  ? 133.985 148.936 107.254 1.00 148.19 ? 84  CYS C C   1 
ATOM   5969  O  O   . CYS C 1 68  ? 134.149 148.230 106.253 1.00 148.19 ? 84  CYS C O   1 
ATOM   5970  C  CB  . CYS C 1 68  ? 133.428 147.747 109.391 1.00 148.19 ? 84  CYS C CB  1 
ATOM   5971  S  SG  . CYS C 1 68  ? 133.858 147.376 111.107 1.00 148.19 ? 84  CYS C SG  1 
ATOM   5972  N  N   . PHE C 1 69  ? 133.324 150.096 107.200 1.00 145.14 ? 85  PHE C N   1 
ATOM   5973  C  CA  . PHE C 1 69  ? 132.750 150.559 105.937 1.00 145.14 ? 85  PHE C CA  1 
ATOM   5974  C  C   . PHE C 1 69  ? 133.821 150.890 104.901 1.00 145.14 ? 85  PHE C C   1 
ATOM   5975  O  O   . PHE C 1 69  ? 133.673 150.543 103.720 1.00 145.14 ? 85  PHE C O   1 
ATOM   5976  C  CB  . PHE C 1 69  ? 131.855 151.771 106.197 1.00 145.14 ? 85  PHE C CB  1 
ATOM   5977  C  CG  . PHE C 1 69  ? 131.578 152.597 104.975 1.00 145.14 ? 85  PHE C CG  1 
ATOM   5978  C  CD1 . PHE C 1 69  ? 130.775 152.108 103.958 1.00 145.14 ? 85  PHE C CD1 1 
ATOM   5979  C  CD2 . PHE C 1 69  ? 132.108 153.870 104.851 1.00 145.14 ? 85  PHE C CD2 1 
ATOM   5980  C  CE1 . PHE C 1 69  ? 130.514 152.870 102.836 1.00 145.14 ? 85  PHE C CE1 1 
ATOM   5981  C  CE2 . PHE C 1 69  ? 131.850 154.636 103.732 1.00 145.14 ? 85  PHE C CE2 1 
ATOM   5982  C  CZ  . PHE C 1 69  ? 131.051 154.136 102.724 1.00 145.14 ? 85  PHE C CZ  1 
ATOM   5983  N  N   . PHE C 1 70  ? 134.905 151.554 105.312 1.00 144.97 ? 86  PHE C N   1 
ATOM   5984  C  CA  . PHE C 1 70  ? 136.012 151.775 104.385 1.00 144.97 ? 86  PHE C CA  1 
ATOM   5985  C  C   . PHE C 1 70  ? 136.585 150.447 103.911 1.00 144.97 ? 86  PHE C C   1 
ATOM   5986  O  O   . PHE C 1 70  ? 136.921 150.292 102.733 1.00 144.97 ? 86  PHE C O   1 
ATOM   5987  C  CB  . PHE C 1 70  ? 137.099 152.637 105.021 1.00 144.97 ? 86  PHE C CB  1 
ATOM   5988  C  CG  . PHE C 1 70  ? 136.869 154.117 104.876 1.00 144.97 ? 86  PHE C CG  1 
ATOM   5989  C  CD1 . PHE C 1 70  ? 136.489 154.658 103.660 1.00 144.97 ? 86  PHE C CD1 1 
ATOM   5990  C  CD2 . PHE C 1 70  ? 137.034 154.967 105.959 1.00 144.97 ? 86  PHE C CD2 1 
ATOM   5991  C  CE1 . PHE C 1 70  ? 136.278 156.016 103.526 1.00 144.97 ? 86  PHE C CE1 1 
ATOM   5992  C  CE2 . PHE C 1 70  ? 136.824 156.326 105.831 1.00 144.97 ? 86  PHE C CE2 1 
ATOM   5993  C  CZ  . PHE C 1 70  ? 136.446 156.851 104.613 1.00 144.97 ? 86  PHE C CZ  1 
ATOM   5994  N  N   . ARG C 1 71  ? 136.698 149.476 104.822 1.00 149.94 ? 87  ARG C N   1 
ATOM   5995  C  CA  . ARG C 1 71  ? 137.156 148.146 104.438 1.00 149.94 ? 87  ARG C CA  1 
ATOM   5996  C  C   . ARG C 1 71  ? 136.251 147.558 103.366 1.00 149.94 ? 87  ARG C C   1 
ATOM   5997  O  O   . ARG C 1 71  ? 136.730 146.945 102.404 1.00 149.94 ? 87  ARG C O   1 
ATOM   5998  C  CB  . ARG C 1 71  ? 137.197 147.235 105.666 1.00 149.94 ? 87  ARG C CB  1 
ATOM   5999  C  CG  . ARG C 1 71  ? 137.776 145.856 105.409 1.00 149.94 ? 87  ARG C CG  1 
ATOM   6000  C  CD  . ARG C 1 71  ? 137.599 144.953 106.623 1.00 149.94 ? 87  ARG C CD  1 
ATOM   6001  N  NE  . ARG C 1 71  ? 137.901 145.643 107.872 1.00 149.94 ? 87  ARG C NE  1 
ATOM   6002  C  CZ  . ARG C 1 71  ? 137.586 145.187 109.077 1.00 149.94 ? 87  ARG C CZ  1 
ATOM   6003  N  NH1 . ARG C 1 71  ? 136.964 144.030 109.239 1.00 149.94 ? 87  ARG C NH1 1 
ATOM   6004  N  NH2 . ARG C 1 71  ? 137.908 145.907 110.148 1.00 149.94 ? 87  ARG C NH2 1 
ATOM   6005  N  N   . SER C 1 72  ? 134.937 147.727 103.522 1.00 140.31 ? 88  SER C N   1 
ATOM   6006  C  CA  . SER C 1 72  ? 134.000 147.194 102.541 1.00 140.31 ? 88  SER C CA  1 
ATOM   6007  C  C   . SER C 1 72  ? 134.189 147.864 101.186 1.00 140.31 ? 88  SER C C   1 
ATOM   6008  O  O   . SER C 1 72  ? 134.212 147.189 100.151 1.00 140.31 ? 88  SER C O   1 
ATOM   6009  C  CB  . SER C 1 72  ? 132.565 147.372 103.035 1.00 140.31 ? 88  SER C CB  1 
ATOM   6010  N  N   . MET C 1 73  ? 134.326 149.195 101.169 1.00 144.50 ? 89  MET C N   1 
ATOM   6011  C  CA  . MET C 1 73  ? 134.468 149.877 99.886  1.00 144.50 ? 89  MET C CA  1 
ATOM   6012  C  C   . MET C 1 73  ? 135.877 149.750 99.317  1.00 144.50 ? 89  MET C C   1 
ATOM   6013  O  O   . MET C 1 73  ? 136.038 149.687 98.093  1.00 144.50 ? 89  MET C O   1 
ATOM   6014  C  CB  . MET C 1 73  ? 134.082 151.355 99.995  1.00 144.50 ? 89  MET C CB  1 
ATOM   6015  C  CG  . MET C 1 73  ? 134.749 152.123 101.113 1.00 144.50 ? 89  MET C CG  1 
ATOM   6016  S  SD  . MET C 1 73  ? 134.640 153.906 100.862 1.00 144.50 ? 89  MET C SD  1 
ATOM   6017  C  CE  . MET C 1 73  ? 133.115 154.031 99.930  1.00 144.50 ? 89  MET C CE  1 
ATOM   6018  N  N   . PHE C 1 74  ? 136.900 149.712 100.167 1.00 142.55 ? 90  PHE C N   1 
ATOM   6019  C  CA  . PHE C 1 74  ? 138.270 149.548 99.685  1.00 142.55 ? 90  PHE C CA  1 
ATOM   6020  C  C   . PHE C 1 74  ? 138.491 148.135 99.153  1.00 142.55 ? 90  PHE C C   1 
ATOM   6021  O  O   . PHE C 1 74  ? 139.027 147.948 98.059  1.00 142.55 ? 90  PHE C O   1 
ATOM   6022  C  CB  . PHE C 1 74  ? 139.284 149.847 100.793 1.00 142.55 ? 90  PHE C CB  1 
ATOM   6023  C  CG  . PHE C 1 74  ? 139.354 151.297 101.182 1.00 142.55 ? 90  PHE C CG  1 
ATOM   6024  C  CD1 . PHE C 1 74  ? 138.974 152.287 100.293 1.00 142.55 ? 90  PHE C CD1 1 
ATOM   6025  C  CD2 . PHE C 1 74  ? 139.808 151.669 102.437 1.00 142.55 ? 90  PHE C CD2 1 
ATOM   6026  C  CE1 . PHE C 1 74  ? 139.041 153.619 100.651 1.00 142.55 ? 90  PHE C CE1 1 
ATOM   6027  C  CE2 . PHE C 1 74  ? 139.879 152.999 102.800 1.00 142.55 ? 90  PHE C CE2 1 
ATOM   6028  C  CZ  . PHE C 1 74  ? 139.494 153.975 101.906 1.00 142.55 ? 90  PHE C CZ  1 
ATOM   6029  N  N   . GLN C 1 89  ? 130.730 162.924 99.757  1.00 147.42 ? 105 GLN C N   1 
ATOM   6030  C  CA  . GLN C 1 89  ? 129.558 163.734 99.448  1.00 147.42 ? 105 GLN C CA  1 
ATOM   6031  C  C   . GLN C 1 89  ? 128.906 164.258 100.722 1.00 147.42 ? 105 GLN C C   1 
ATOM   6032  O  O   . GLN C 1 89  ? 128.740 165.466 100.895 1.00 147.42 ? 105 GLN C O   1 
ATOM   6033  C  CB  . GLN C 1 89  ? 128.547 162.925 98.633  1.00 147.42 ? 105 GLN C CB  1 
ATOM   6034  N  N   . ASP C 1 90  ? 128.530 163.334 101.609 1.00 148.80 ? 106 ASP C N   1 
ATOM   6035  C  CA  . ASP C 1 90  ? 127.886 163.722 102.860 1.00 148.80 ? 106 ASP C CA  1 
ATOM   6036  C  C   . ASP C 1 90  ? 128.820 164.554 103.731 1.00 148.80 ? 106 ASP C C   1 
ATOM   6037  O  O   . ASP C 1 90  ? 128.392 165.532 104.355 1.00 148.80 ? 106 ASP C O   1 
ATOM   6038  C  CB  . ASP C 1 90  ? 127.415 162.480 103.615 1.00 148.80 ? 106 ASP C CB  1 
ATOM   6039  N  N   . VAL C 1 91  ? 130.089 164.181 103.788 1.00 138.77 ? 107 VAL C N   1 
ATOM   6040  C  CA  . VAL C 1 91  ? 131.065 164.848 104.641 1.00 138.77 ? 107 VAL C CA  1 
ATOM   6041  C  C   . VAL C 1 91  ? 131.694 166.004 103.877 1.00 138.77 ? 107 VAL C C   1 
ATOM   6042  O  O   . VAL C 1 91  ? 131.835 165.966 102.650 1.00 138.77 ? 107 VAL C O   1 
ATOM   6043  C  CB  . VAL C 1 91  ? 132.132 163.843 105.122 1.00 138.77 ? 107 VAL C CB  1 
ATOM   6044  C  CG1 . VAL C 1 91  ? 132.925 164.410 106.292 1.00 138.77 ? 107 VAL C CG1 1 
ATOM   6045  C  CG2 . VAL C 1 91  ? 131.484 162.517 105.480 1.00 138.77 ? 107 VAL C CG2 1 
ATOM   6046  N  N   . SER C 1 92  ? 132.076 167.045 104.610 1.00 137.45 ? 108 SER C N   1 
ATOM   6047  C  CA  . SER C 1 92  ? 132.730 168.206 104.028 1.00 137.45 ? 108 SER C CA  1 
ATOM   6048  C  C   . SER C 1 92  ? 134.245 168.025 104.042 1.00 137.45 ? 108 SER C C   1 
ATOM   6049  O  O   . SER C 1 92  ? 134.788 167.177 104.753 1.00 137.45 ? 108 SER C O   1 
ATOM   6050  C  CB  . SER C 1 92  ? 132.346 169.479 104.781 1.00 137.45 ? 108 SER C CB  1 
ATOM   6051  O  OG  . SER C 1 92  ? 133.022 170.606 104.251 1.00 137.45 ? 108 SER C OG  1 
ATOM   6052  N  N   . GLU C 1 93  ? 134.927 168.842 103.234 1.00 139.39 ? 109 GLU C N   1 
ATOM   6053  C  CA  . GLU C 1 93  ? 136.383 168.766 103.165 1.00 139.39 ? 109 GLU C CA  1 
ATOM   6054  C  C   . GLU C 1 93  ? 137.019 169.092 104.511 1.00 139.39 ? 109 GLU C C   1 
ATOM   6055  O  O   . GLU C 1 93  ? 137.961 168.415 104.941 1.00 139.39 ? 109 GLU C O   1 
ATOM   6056  C  CB  . GLU C 1 93  ? 136.906 169.709 102.082 1.00 139.39 ? 109 GLU C CB  1 
ATOM   6057  N  N   . SER C 1 94  ? 136.518 170.127 105.190 1.00 140.98 ? 110 SER C N   1 
ATOM   6058  C  CA  . SER C 1 94  ? 137.053 170.481 106.501 1.00 140.98 ? 110 SER C CA  1 
ATOM   6059  C  C   . SER C 1 94  ? 136.837 169.356 107.506 1.00 140.98 ? 110 SER C C   1 
ATOM   6060  O  O   . SER C 1 94  ? 137.734 169.038 108.295 1.00 140.98 ? 110 SER C O   1 
ATOM   6061  C  CB  . SER C 1 94  ? 136.411 171.775 106.999 1.00 140.98 ? 110 SER C CB  1 
ATOM   6062  O  OG  . SER C 1 94  ? 136.594 171.931 108.395 1.00 140.98 ? 110 SER C OG  1 
ATOM   6063  N  N   . VAL C 1 95  ? 135.651 168.746 107.495 1.00 144.63 ? 111 VAL C N   1 
ATOM   6064  C  CA  . VAL C 1 95  ? 135.379 167.642 108.408 1.00 144.63 ? 111 VAL C CA  1 
ATOM   6065  C  C   . VAL C 1 95  ? 136.176 166.408 108.004 1.00 144.63 ? 111 VAL C C   1 
ATOM   6066  O  O   . VAL C 1 95  ? 136.672 165.664 108.859 1.00 144.63 ? 111 VAL C O   1 
ATOM   6067  C  CB  . VAL C 1 95  ? 133.868 167.353 108.460 1.00 144.63 ? 111 VAL C CB  1 
ATOM   6068  C  CG1 . VAL C 1 95  ? 133.565 166.280 109.496 1.00 144.63 ? 111 VAL C CG1 1 
ATOM   6069  C  CG2 . VAL C 1 95  ? 133.097 168.628 108.765 1.00 144.63 ? 111 VAL C CG2 1 
ATOM   6070  N  N   . PHE C 1 96  ? 136.305 166.161 106.697 1.00 135.78 ? 112 PHE C N   1 
ATOM   6071  C  CA  . PHE C 1 96  ? 137.086 165.014 106.244 1.00 135.78 ? 112 PHE C CA  1 
ATOM   6072  C  C   . PHE C 1 96  ? 138.562 165.163 106.587 1.00 135.78 ? 112 PHE C C   1 
ATOM   6073  O  O   . PHE C 1 96  ? 139.264 164.157 106.733 1.00 135.78 ? 112 PHE C O   1 
ATOM   6074  C  CB  . PHE C 1 96  ? 136.909 164.816 104.739 1.00 135.78 ? 112 PHE C CB  1 
ATOM   6075  C  CG  . PHE C 1 96  ? 137.448 163.509 104.236 1.00 135.78 ? 112 PHE C CG  1 
ATOM   6076  C  CD1 . PHE C 1 96  ? 136.988 162.310 104.754 1.00 135.78 ? 112 PHE C CD1 1 
ATOM   6077  C  CD2 . PHE C 1 96  ? 138.411 163.479 103.242 1.00 135.78 ? 112 PHE C CD2 1 
ATOM   6078  C  CE1 . PHE C 1 96  ? 137.482 161.105 104.293 1.00 135.78 ? 112 PHE C CE1 1 
ATOM   6079  C  CE2 . PHE C 1 96  ? 138.908 162.276 102.775 1.00 135.78 ? 112 PHE C CE2 1 
ATOM   6080  C  CZ  . PHE C 1 96  ? 138.443 161.088 103.302 1.00 135.78 ? 112 PHE C CZ  1 
ATOM   6081  N  N   . GLN C 1 97  ? 139.051 166.398 106.723 1.00 136.39 ? 113 GLN C N   1 
ATOM   6082  C  CA  . GLN C 1 97  ? 140.422 166.602 107.182 1.00 136.39 ? 113 GLN C CA  1 
ATOM   6083  C  C   . GLN C 1 97  ? 140.613 166.045 108.587 1.00 136.39 ? 113 GLN C C   1 
ATOM   6084  O  O   . GLN C 1 97  ? 141.572 165.312 108.857 1.00 136.39 ? 113 GLN C O   1 
ATOM   6085  C  CB  . GLN C 1 97  ? 140.776 168.088 107.134 1.00 136.39 ? 113 GLN C CB  1 
ATOM   6086  N  N   . LEU C 1 98  ? 139.696 166.372 109.499 1.00 129.15 ? 114 LEU C N   1 
ATOM   6087  C  CA  . LEU C 1 98  ? 139.768 165.806 110.840 1.00 129.15 ? 114 LEU C CA  1 
ATOM   6088  C  C   . LEU C 1 98  ? 139.518 164.303 110.816 1.00 129.15 ? 114 LEU C C   1 
ATOM   6089  O  O   . LEU C 1 98  ? 140.100 163.565 111.619 1.00 129.15 ? 114 LEU C O   1 
ATOM   6090  C  CB  . LEU C 1 98  ? 138.764 166.505 111.757 1.00 129.15 ? 114 LEU C CB  1 
ATOM   6091  C  CG  . LEU C 1 98  ? 138.701 166.068 113.221 1.00 129.15 ? 114 LEU C CG  1 
ATOM   6092  C  CD1 . LEU C 1 98  ? 140.103 165.921 113.790 1.00 129.15 ? 114 LEU C CD1 1 
ATOM   6093  C  CD2 . LEU C 1 98  ? 137.889 167.055 114.042 1.00 129.15 ? 114 LEU C CD2 1 
ATOM   6094  N  N   . LEU C 1 99  ? 138.668 163.834 109.899 1.00 131.32 ? 115 LEU C N   1 
ATOM   6095  C  CA  . LEU C 1 99  ? 138.433 162.399 109.765 1.00 131.32 ? 115 LEU C CA  1 
ATOM   6096  C  C   . LEU C 1 99  ? 139.721 161.656 109.425 1.00 131.32 ? 115 LEU C C   1 
ATOM   6097  O  O   . LEU C 1 99  ? 140.071 160.667 110.076 1.00 131.32 ? 115 LEU C O   1 
ATOM   6098  C  CB  . LEU C 1 99  ? 137.365 162.142 108.702 1.00 131.32 ? 115 LEU C CB  1 
ATOM   6099  N  N   . VAL C 1 100 ? 140.446 162.126 108.406 1.00 126.68 ? 116 VAL C N   1 
ATOM   6100  C  CA  . VAL C 1 100 ? 141.697 161.469 108.029 1.00 126.68 ? 116 VAL C CA  1 
ATOM   6101  C  C   . VAL C 1 100 ? 142.754 161.651 109.114 1.00 126.68 ? 116 VAL C C   1 
ATOM   6102  O  O   . VAL C 1 100 ? 143.575 160.753 109.343 1.00 126.68 ? 116 VAL C O   1 
ATOM   6103  C  CB  . VAL C 1 100 ? 142.188 161.950 106.648 1.00 126.68 ? 116 VAL C CB  1 
ATOM   6104  C  CG1 . VAL C 1 100 ? 141.184 161.566 105.571 1.00 126.68 ? 116 VAL C CG1 1 
ATOM   6105  C  CG2 . VAL C 1 100 ? 142.438 163.441 106.633 1.00 126.68 ? 116 VAL C CG2 1 
ATOM   6106  N  N   . ASP C 1 101 ? 142.765 162.805 109.792 1.00 122.80 ? 117 ASP C N   1 
ATOM   6107  C  CA  . ASP C 1 101 ? 143.693 162.997 110.903 1.00 122.80 ? 117 ASP C CA  1 
ATOM   6108  C  C   . ASP C 1 101 ? 143.440 161.976 112.005 1.00 122.80 ? 117 ASP C C   1 
ATOM   6109  O  O   . ASP C 1 101 ? 144.382 161.483 112.636 1.00 122.80 ? 117 ASP C O   1 
ATOM   6110  C  CB  . ASP C 1 101 ? 143.576 164.420 111.448 1.00 122.80 ? 117 ASP C CB  1 
ATOM   6111  N  N   . TYR C 1 102 ? 142.170 161.648 112.250 1.00 125.63 ? 118 TYR C N   1 
ATOM   6112  C  CA  . TYR C 1 102 ? 141.843 160.618 113.230 1.00 125.63 ? 118 TYR C CA  1 
ATOM   6113  C  C   . TYR C 1 102 ? 142.202 159.234 112.708 1.00 125.63 ? 118 TYR C C   1 
ATOM   6114  O  O   . TYR C 1 102 ? 142.621 158.362 113.479 1.00 125.63 ? 118 TYR C O   1 
ATOM   6115  C  CB  . TYR C 1 102 ? 140.358 160.695 113.579 1.00 125.63 ? 118 TYR C CB  1 
ATOM   6116  C  CG  . TYR C 1 102 ? 139.887 159.664 114.577 1.00 125.63 ? 118 TYR C CG  1 
ATOM   6117  C  CD1 . TYR C 1 102 ? 140.165 159.790 115.929 1.00 125.63 ? 118 TYR C CD1 1 
ATOM   6118  C  CD2 . TYR C 1 102 ? 139.143 158.570 114.162 1.00 125.63 ? 118 TYR C CD2 1 
ATOM   6119  C  CE1 . TYR C 1 102 ? 139.722 158.847 116.835 1.00 125.63 ? 118 TYR C CE1 1 
ATOM   6120  C  CE2 . TYR C 1 102 ? 138.698 157.624 115.060 1.00 125.63 ? 118 TYR C CE2 1 
ATOM   6121  C  CZ  . TYR C 1 102 ? 138.990 157.767 116.396 1.00 125.63 ? 118 TYR C CZ  1 
ATOM   6122  O  OH  . TYR C 1 102 ? 138.548 156.824 117.295 1.00 125.63 ? 118 TYR C OH  1 
ATOM   6123  N  N   . ILE C 1 103 ? 142.034 159.013 111.404 1.00 118.80 ? 119 ILE C N   1 
ATOM   6124  C  CA  . ILE C 1 103 ? 142.352 157.712 110.819 1.00 118.80 ? 119 ILE C CA  1 
ATOM   6125  C  C   . ILE C 1 103 ? 143.835 157.409 110.987 1.00 118.80 ? 119 ILE C C   1 
ATOM   6126  O  O   . ILE C 1 103 ? 144.219 156.327 111.446 1.00 118.80 ? 119 ILE C O   1 
ATOM   6127  C  CB  . ILE C 1 103 ? 141.928 157.659 109.340 1.00 118.80 ? 119 ILE C CB  1 
ATOM   6128  C  CG1 . ILE C 1 103 ? 140.405 157.702 109.211 1.00 118.80 ? 119 ILE C CG1 1 
ATOM   6129  C  CG2 . ILE C 1 103 ? 142.495 156.423 108.669 1.00 118.80 ? 119 ILE C CG2 1 
ATOM   6130  C  CD1 . ILE C 1 103 ? 139.914 157.674 107.780 1.00 118.80 ? 119 ILE C CD1 1 
ATOM   6131  N  N   . TYR C 1 104 ? 144.690 158.364 110.622 1.00 107.63 ? 120 TYR C N   1 
ATOM   6132  C  CA  . TYR C 1 104 ? 146.129 158.124 110.632 1.00 107.63 ? 120 TYR C CA  1 
ATOM   6133  C  C   . TYR C 1 104 ? 146.774 158.479 111.968 1.00 107.63 ? 120 TYR C C   1 
ATOM   6134  O  O   . TYR C 1 104 ? 147.537 157.680 112.520 1.00 107.63 ? 120 TYR C O   1 
ATOM   6135  C  CB  . TYR C 1 104 ? 146.795 158.921 109.508 1.00 107.63 ? 120 TYR C CB  1 
ATOM   6136  C  CG  . TYR C 1 104 ? 146.453 158.437 108.120 1.00 107.63 ? 120 TYR C CG  1 
ATOM   6137  C  CD1 . TYR C 1 104 ? 147.034 157.290 107.601 1.00 107.63 ? 120 TYR C CD1 1 
ATOM   6138  C  CD2 . TYR C 1 104 ? 145.548 159.129 107.328 1.00 107.63 ? 120 TYR C CD2 1 
ATOM   6139  C  CE1 . TYR C 1 104 ? 146.725 156.845 106.331 1.00 107.63 ? 120 TYR C CE1 1 
ATOM   6140  C  CE2 . TYR C 1 104 ? 145.232 158.692 106.057 1.00 107.63 ? 120 TYR C CE2 1 
ATOM   6141  C  CZ  . TYR C 1 104 ? 145.823 157.549 105.564 1.00 107.63 ? 120 TYR C CZ  1 
ATOM   6142  O  OH  . TYR C 1 104 ? 145.512 157.109 104.299 1.00 107.63 ? 120 TYR C OH  1 
ATOM   6143  N  N   . HIS C 1 105 ? 146.481 159.662 112.505 1.00 122.59 ? 121 HIS C N   1 
ATOM   6144  C  CA  . HIS C 1 105 ? 147.165 160.145 113.698 1.00 122.59 ? 121 HIS C CA  1 
ATOM   6145  C  C   . HIS C 1 105 ? 146.343 160.001 114.971 1.00 122.59 ? 121 HIS C C   1 
ATOM   6146  O  O   . HIS C 1 105 ? 146.921 159.886 116.056 1.00 122.59 ? 121 HIS C O   1 
ATOM   6147  C  CB  . HIS C 1 105 ? 147.564 161.615 113.522 1.00 122.59 ? 121 HIS C CB  1 
ATOM   6148  C  CG  . HIS C 1 105 ? 148.094 161.939 112.160 1.00 122.59 ? 121 HIS C CG  1 
ATOM   6149  N  ND1 . HIS C 1 105 ? 147.736 163.080 111.474 1.00 122.59 ? 121 HIS C ND1 1 
ATOM   6150  C  CD2 . HIS C 1 105 ? 148.955 161.272 111.355 1.00 122.59 ? 121 HIS C CD2 1 
ATOM   6151  C  CE1 . HIS C 1 105 ? 148.354 163.102 110.307 1.00 122.59 ? 121 HIS C CE1 1 
ATOM   6152  N  NE2 . HIS C 1 105 ? 149.099 162.016 110.209 1.00 122.59 ? 121 HIS C NE2 1 
ATOM   6153  N  N   . GLY C 1 106 ? 145.017 160.005 114.866 1.00 135.65 ? 122 GLY C N   1 
ATOM   6154  C  CA  . GLY C 1 106 ? 144.168 159.925 116.039 1.00 135.65 ? 122 GLY C CA  1 
ATOM   6155  C  C   . GLY C 1 106 ? 144.120 161.173 116.890 1.00 135.65 ? 122 GLY C C   1 
ATOM   6156  O  O   . GLY C 1 106 ? 143.806 161.085 118.080 1.00 135.65 ? 122 GLY C O   1 
ATOM   6157  N  N   . THR C 1 107 ? 144.425 162.336 116.318 1.00 125.12 ? 123 THR C N   1 
ATOM   6158  C  CA  . THR C 1 107 ? 144.409 163.604 117.042 1.00 125.12 ? 123 THR C CA  1 
ATOM   6159  C  C   . THR C 1 107 ? 143.139 164.354 116.656 1.00 125.12 ? 123 THR C C   1 
ATOM   6160  O  O   . THR C 1 107 ? 142.999 164.801 115.513 1.00 125.12 ? 123 THR C O   1 
ATOM   6161  C  CB  . THR C 1 107 ? 145.654 164.431 116.731 1.00 125.12 ? 123 THR C CB  1 
ATOM   6162  N  N   . VAL C 1 108 ? 142.217 164.490 117.604 1.00 128.84 ? 124 VAL C N   1 
ATOM   6163  C  CA  . VAL C 1 108 ? 140.896 165.054 117.348 1.00 128.84 ? 124 VAL C CA  1 
ATOM   6164  C  C   . VAL C 1 108 ? 140.643 166.153 118.372 1.00 128.84 ? 124 VAL C C   1 
ATOM   6165  O  O   . VAL C 1 108 ? 140.575 165.881 119.577 1.00 128.84 ? 124 VAL C O   1 
ATOM   6166  C  CB  . VAL C 1 108 ? 139.788 163.993 117.400 1.00 128.84 ? 124 VAL C CB  1 
ATOM   6167  C  CG1 . VAL C 1 108 ? 138.440 164.625 117.734 1.00 128.84 ? 124 VAL C CG1 1 
ATOM   6168  C  CG2 . VAL C 1 108 ? 139.716 163.237 116.090 1.00 128.84 ? 124 VAL C CG2 1 
ATOM   6169  N  N   . LYS C 1 109 ? 140.551 167.394 117.906 1.00 122.12 ? 125 LYS C N   1 
ATOM   6170  C  CA  . LYS C 1 109 ? 139.983 168.470 118.700 1.00 122.12 ? 125 LYS C CA  1 
ATOM   6171  C  C   . LYS C 1 109 ? 138.756 169.015 117.985 1.00 122.12 ? 125 LYS C C   1 
ATOM   6172  O  O   . LYS C 1 109 ? 138.701 169.050 116.752 1.00 122.12 ? 125 LYS C O   1 
ATOM   6173  C  CB  . LYS C 1 109 ? 141.000 169.592 118.935 1.00 122.12 ? 125 LYS C CB  1 
ATOM   6174  N  N   . LEU C 1 110 ? 137.767 169.436 118.768 1.00 144.78 ? 126 LEU C N   1 
ATOM   6175  C  CA  . LEU C 1 110 ? 136.515 169.951 118.237 1.00 144.78 ? 126 LEU C CA  1 
ATOM   6176  C  C   . LEU C 1 110 ? 136.320 171.416 118.593 1.00 144.78 ? 126 LEU C C   1 
ATOM   6177  O  O   . LEU C 1 110 ? 136.801 171.902 119.621 1.00 144.78 ? 126 LEU C O   1 
ATOM   6178  C  CB  . LEU C 1 110 ? 135.277 169.159 118.698 1.00 144.78 ? 126 LEU C CB  1 
ATOM   6179  C  CG  . LEU C 1 110 ? 134.653 169.325 120.084 1.00 144.78 ? 126 LEU C CG  1 
ATOM   6180  C  CD1 . LEU C 1 110 ? 133.695 170.496 120.189 1.00 144.78 ? 126 LEU C CD1 1 
ATOM   6181  C  CD2 . LEU C 1 110 ? 133.859 168.055 120.315 1.00 144.78 ? 126 LEU C CD2 1 
ATOM   6182  N  N   . ARG C 1 111 ? 135.617 172.104 117.706 1.00 140.30 ? 127 ARG C N   1 
ATOM   6183  C  CA  . ARG C 1 111 ? 134.994 173.388 117.973 1.00 140.30 ? 127 ARG C CA  1 
ATOM   6184  C  C   . ARG C 1 111 ? 133.484 173.195 117.911 1.00 140.30 ? 127 ARG C C   1 
ATOM   6185  O  O   . ARG C 1 111 ? 132.987 172.326 117.192 1.00 140.30 ? 127 ARG C O   1 
ATOM   6186  C  CB  . ARG C 1 111 ? 135.454 174.447 116.968 1.00 140.30 ? 127 ARG C CB  1 
ATOM   6187  C  CG  . ARG C 1 111 ? 136.579 175.339 117.475 1.00 140.30 ? 127 ARG C CG  1 
ATOM   6188  C  CD  . ARG C 1 111 ? 137.781 174.525 117.935 1.00 140.30 ? 127 ARG C CD  1 
ATOM   6189  N  NE  . ARG C 1 111 ? 138.364 173.728 116.862 1.00 140.30 ? 127 ARG C NE  1 
ATOM   6190  C  CZ  . ARG C 1 111 ? 139.488 173.034 116.973 1.00 140.30 ? 127 ARG C CZ  1 
ATOM   6191  N  NH1 . ARG C 1 111 ? 140.179 173.012 118.101 1.00 140.30 ? 127 ARG C NH1 1 
ATOM   6192  N  NH2 . ARG C 1 111 ? 139.929 172.341 115.927 1.00 140.30 ? 127 ARG C NH2 1 
ATOM   6193  N  N   . ALA C 1 112 ? 132.758 173.980 118.709 1.00 146.88 ? 128 ALA C N   1 
ATOM   6194  C  CA  . ALA C 1 112 ? 131.362 173.665 119.008 1.00 146.88 ? 128 ALA C CA  1 
ATOM   6195  C  C   . ALA C 1 112 ? 130.499 173.536 117.754 1.00 146.88 ? 128 ALA C C   1 
ATOM   6196  O  O   . ALA C 1 112 ? 129.485 172.830 117.774 1.00 146.88 ? 128 ALA C O   1 
ATOM   6197  C  CB  . ALA C 1 112 ? 130.777 174.727 119.939 1.00 146.88 ? 128 ALA C CB  1 
ATOM   6198  N  N   . GLU C 1 113 ? 130.878 174.195 116.660 1.00 136.11 ? 129 GLU C N   1 
ATOM   6199  C  CA  . GLU C 1 113 ? 130.021 174.298 115.483 1.00 136.11 ? 129 GLU C CA  1 
ATOM   6200  C  C   . GLU C 1 113 ? 130.080 173.096 114.542 1.00 136.11 ? 129 GLU C C   1 
ATOM   6201  O  O   . GLU C 1 113 ? 129.357 173.096 113.540 1.00 136.11 ? 129 GLU C O   1 
ATOM   6202  C  CB  . GLU C 1 113 ? 130.370 175.565 114.699 1.00 136.11 ? 129 GLU C CB  1 
ATOM   6203  N  N   . GLU C 1 114 ? 130.896 172.075 114.814 1.00 128.62 ? 130 GLU C N   1 
ATOM   6204  C  CA  . GLU C 1 114 ? 131.041 170.962 113.880 1.00 128.62 ? 130 GLU C CA  1 
ATOM   6205  C  C   . GLU C 1 114 ? 130.496 169.638 114.400 1.00 128.62 ? 130 GLU C C   1 
ATOM   6206  O  O   . GLU C 1 114 ? 130.459 168.668 113.629 1.00 128.62 ? 130 GLU C O   1 
ATOM   6207  C  CB  . GLU C 1 114 ? 132.511 170.762 113.474 1.00 128.62 ? 130 GLU C CB  1 
ATOM   6208  C  CG  . GLU C 1 114 ? 133.534 171.169 114.510 1.00 128.62 ? 130 GLU C CG  1 
ATOM   6209  C  CD  . GLU C 1 114 ? 134.960 171.051 114.006 1.00 128.62 ? 130 GLU C CD  1 
ATOM   6210  O  OE1 . GLU C 1 114 ? 135.311 169.988 113.454 1.00 128.62 ? 130 GLU C OE1 1 
ATOM   6211  O  OE2 . GLU C 1 114 ? 135.731 172.020 114.166 1.00 128.62 ? 130 GLU C OE2 1 
ATOM   6212  N  N   . LEU C 1 115 ? 130.044 169.581 115.660 1.00 120.56 ? 131 LEU C N   1 
ATOM   6213  C  CA  . LEU C 1 115 ? 129.581 168.325 116.252 1.00 120.56 ? 131 LEU C CA  1 
ATOM   6214  C  C   . LEU C 1 115 ? 128.647 167.577 115.315 1.00 120.56 ? 131 LEU C C   1 
ATOM   6215  O  O   . LEU C 1 115 ? 128.805 166.369 115.103 1.00 120.56 ? 131 LEU C O   1 
ATOM   6216  C  CB  . LEU C 1 115 ? 128.856 168.598 117.572 1.00 120.56 ? 131 LEU C CB  1 
ATOM   6217  C  CG  . LEU C 1 115 ? 129.611 168.433 118.886 1.00 120.56 ? 131 LEU C CG  1 
ATOM   6218  C  CD1 . LEU C 1 115 ? 129.916 166.973 119.178 1.00 120.56 ? 131 LEU C CD1 1 
ATOM   6219  C  CD2 . LEU C 1 115 ? 130.865 169.242 118.814 1.00 120.56 ? 131 LEU C CD2 1 
ATOM   6220  N  N   . GLN C 1 116 ? 127.690 168.297 114.720 1.00 139.84 ? 132 GLN C N   1 
ATOM   6221  C  CA  . GLN C 1 116 ? 126.752 167.716 113.769 1.00 139.84 ? 132 GLN C CA  1 
ATOM   6222  C  C   . GLN C 1 116 ? 127.458 166.754 112.824 1.00 139.84 ? 132 GLN C C   1 
ATOM   6223  O  O   . GLN C 1 116 ? 127.211 165.542 112.850 1.00 139.84 ? 132 GLN C O   1 
ATOM   6224  C  CB  . GLN C 1 116 ? 126.049 168.830 112.986 1.00 139.84 ? 132 GLN C CB  1 
ATOM   6225  C  CG  . GLN C 1 116 ? 125.045 168.333 111.959 1.00 139.84 ? 132 GLN C CG  1 
ATOM   6226  C  CD  . GLN C 1 116 ? 123.784 167.780 112.593 1.00 139.84 ? 132 GLN C CD  1 
ATOM   6227  O  OE1 . GLN C 1 116 ? 123.513 168.013 113.771 1.00 139.84 ? 132 GLN C OE1 1 
ATOM   6228  N  NE2 . GLN C 1 116 ? 123.002 167.045 111.811 1.00 139.84 ? 132 GLN C NE2 1 
ATOM   6229  N  N   . GLU C 1 117 ? 128.389 167.274 112.021 1.00 139.25 ? 133 GLU C N   1 
ATOM   6230  C  CA  . GLU C 1 117 ? 129.079 166.404 111.077 1.00 139.25 ? 133 GLU C CA  1 
ATOM   6231  C  C   . GLU C 1 117 ? 129.923 165.375 111.810 1.00 139.25 ? 133 GLU C C   1 
ATOM   6232  O  O   . GLU C 1 117 ? 129.883 164.183 111.476 1.00 139.25 ? 133 GLU C O   1 
ATOM   6233  C  CB  . GLU C 1 117 ? 129.935 167.231 110.117 1.00 139.25 ? 133 GLU C CB  1 
ATOM   6234  C  CG  . GLU C 1 117 ? 129.206 167.813 108.896 1.00 139.25 ? 133 GLU C CG  1 
ATOM   6235  C  CD  . GLU C 1 117 ? 128.056 166.959 108.363 1.00 139.25 ? 133 GLU C CD  1 
ATOM   6236  O  OE1 . GLU C 1 117 ? 127.115 167.545 107.792 1.00 139.25 ? 133 GLU C OE1 1 
ATOM   6237  O  OE2 . GLU C 1 117 ? 128.116 165.711 108.427 1.00 139.25 ? 133 GLU C OE2 1 
ATOM   6238  N  N   . ILE C 1 118 ? 130.640 165.806 112.854 1.00 134.48 ? 134 ILE C N   1 
ATOM   6239  C  CA  . ILE C 1 118 ? 131.445 164.889 113.651 1.00 134.48 ? 134 ILE C CA  1 
ATOM   6240  C  C   . ILE C 1 118 ? 130.582 163.755 114.178 1.00 134.48 ? 134 ILE C C   1 
ATOM   6241  O  O   . ILE C 1 118 ? 131.096 162.680 114.504 1.00 134.48 ? 134 ILE C O   1 
ATOM   6242  C  CB  . ILE C 1 118 ? 132.155 165.660 114.787 1.00 134.48 ? 134 ILE C CB  1 
ATOM   6243  C  CG1 . ILE C 1 118 ? 133.064 166.739 114.199 1.00 134.48 ? 134 ILE C CG1 1 
ATOM   6244  C  CG2 . ILE C 1 118 ? 132.995 164.732 115.649 1.00 134.48 ? 134 ILE C CG2 1 
ATOM   6245  C  CD1 . ILE C 1 118 ? 133.834 167.525 115.240 1.00 134.48 ? 134 ILE C CD1 1 
ATOM   6246  N  N   . TYR C 1 119 ? 129.268 163.965 114.257 1.00 128.03 ? 135 TYR C N   1 
ATOM   6247  C  CA  . TYR C 1 119 ? 128.358 162.866 114.547 1.00 128.03 ? 135 TYR C CA  1 
ATOM   6248  C  C   . TYR C 1 119 ? 128.053 162.065 113.286 1.00 128.03 ? 135 TYR C C   1 
ATOM   6249  O  O   . TYR C 1 119 ? 128.444 160.896 113.165 1.00 128.03 ? 135 TYR C O   1 
ATOM   6250  C  CB  . TYR C 1 119 ? 127.068 163.416 115.161 1.00 128.03 ? 135 TYR C CB  1 
ATOM   6251  C  CG  . TYR C 1 119 ? 126.146 162.370 115.739 1.00 128.03 ? 135 TYR C CG  1 
ATOM   6252  C  CD1 . TYR C 1 119 ? 126.244 161.982 117.066 1.00 128.03 ? 135 TYR C CD1 1 
ATOM   6253  C  CD2 . TYR C 1 119 ? 125.163 161.780 114.955 1.00 128.03 ? 135 TYR C CD2 1 
ATOM   6254  C  CE1 . TYR C 1 119 ? 125.393 161.032 117.593 1.00 128.03 ? 135 TYR C CE1 1 
ATOM   6255  C  CE2 . TYR C 1 119 ? 124.312 160.828 115.474 1.00 128.03 ? 135 TYR C CE2 1 
ATOM   6256  C  CZ  . TYR C 1 119 ? 124.431 160.458 116.794 1.00 128.03 ? 135 TYR C CZ  1 
ATOM   6257  O  OH  . TYR C 1 119 ? 123.586 159.509 117.317 1.00 128.03 ? 135 TYR C OH  1 
ATOM   6258  N  N   . GLU C 1 120 ? 127.433 162.724 112.303 1.00 131.61 ? 136 GLU C N   1 
ATOM   6259  C  CA  . GLU C 1 120 ? 126.910 162.045 111.121 1.00 131.61 ? 136 GLU C CA  1 
ATOM   6260  C  C   . GLU C 1 120 ? 127.971 161.185 110.453 1.00 131.61 ? 136 GLU C C   1 
ATOM   6261  O  O   . GLU C 1 120 ? 127.826 159.961 110.343 1.00 131.61 ? 136 GLU C O   1 
ATOM   6262  C  CB  . GLU C 1 120 ? 126.351 163.079 110.143 1.00 131.61 ? 136 GLU C CB  1 
ATOM   6263  C  CG  . GLU C 1 120 ? 124.942 163.534 110.474 1.00 131.61 ? 136 GLU C CG  1 
ATOM   6264  C  CD  . GLU C 1 120 ? 124.201 164.062 109.265 1.00 131.61 ? 136 GLU C CD  1 
ATOM   6265  O  OE1 . GLU C 1 120 ? 124.776 164.896 108.535 1.00 131.61 ? 136 GLU C OE1 1 
ATOM   6266  O  OE2 . GLU C 1 120 ? 123.045 163.645 109.045 1.00 131.61 ? 136 GLU C OE2 1 
ATOM   6267  N  N   . VAL C 1 121 ? 129.066 161.817 110.027 1.00 129.36 ? 137 VAL C N   1 
ATOM   6268  C  CA  . VAL C 1 121 ? 130.139 161.088 109.360 1.00 129.36 ? 137 VAL C CA  1 
ATOM   6269  C  C   . VAL C 1 121 ? 130.629 159.952 110.244 1.00 129.36 ? 137 VAL C C   1 
ATOM   6270  O  O   . VAL C 1 121 ? 130.776 158.808 109.794 1.00 129.36 ? 137 VAL C O   1 
ATOM   6271  C  CB  . VAL C 1 121 ? 131.285 162.045 108.991 1.00 129.36 ? 137 VAL C CB  1 
ATOM   6272  N  N   . SER C 1 122 ? 130.857 160.241 111.526 1.00 123.80 ? 138 SER C N   1 
ATOM   6273  C  CA  . SER C 1 122 ? 131.414 159.224 112.404 1.00 123.80 ? 138 SER C CA  1 
ATOM   6274  C  C   . SER C 1 122 ? 130.448 158.078 112.661 1.00 123.80 ? 138 SER C C   1 
ATOM   6275  O  O   . SER C 1 122 ? 130.870 157.054 113.203 1.00 123.80 ? 138 SER C O   1 
ATOM   6276  C  CB  . SER C 1 122 ? 131.864 159.839 113.724 1.00 123.80 ? 138 SER C CB  1 
ATOM   6277  O  OG  . SER C 1 122 ? 132.701 158.938 114.423 1.00 123.80 ? 138 SER C OG  1 
ATOM   6278  N  N   . ASP C 1 123 ? 129.172 158.222 112.300 1.00 130.81 ? 139 ASP C N   1 
ATOM   6279  C  CA  . ASP C 1 123 ? 128.248 157.098 112.352 1.00 130.81 ? 139 ASP C CA  1 
ATOM   6280  C  C   . ASP C 1 123 ? 128.039 156.435 110.999 1.00 130.81 ? 139 ASP C C   1 
ATOM   6281  O  O   . ASP C 1 123 ? 127.552 155.301 110.953 1.00 130.81 ? 139 ASP C O   1 
ATOM   6282  C  CB  . ASP C 1 123 ? 126.889 157.543 112.907 1.00 130.81 ? 139 ASP C CB  1 
ATOM   6283  C  CG  . ASP C 1 123 ? 126.845 157.526 114.421 1.00 130.81 ? 139 ASP C CG  1 
ATOM   6284  O  OD1 . ASP C 1 123 ? 127.876 157.839 115.050 1.00 130.81 ? 139 ASP C OD1 1 
ATOM   6285  O  OD2 . ASP C 1 123 ? 125.780 157.192 114.982 1.00 130.81 ? 139 ASP C OD2 1 
ATOM   6286  N  N   . MET C 1 124 ? 128.397 157.108 109.906 1.00 121.76 ? 140 MET C N   1 
ATOM   6287  C  CA  . MET C 1 124 ? 128.224 156.568 108.564 1.00 121.76 ? 140 MET C CA  1 
ATOM   6288  C  C   . MET C 1 124 ? 129.512 155.966 108.018 1.00 121.76 ? 140 MET C C   1 
ATOM   6289  O  O   . MET C 1 124 ? 129.505 154.852 107.487 1.00 121.76 ? 140 MET C O   1 
ATOM   6290  C  CB  . MET C 1 124 ? 127.712 157.660 107.617 1.00 121.76 ? 140 MET C CB  1 
ATOM   6291  N  N   . TYR C 1 125 ? 130.624 156.694 108.139 1.00 121.81 ? 141 TYR C N   1 
ATOM   6292  C  CA  . TYR C 1 125 ? 131.900 156.207 107.629 1.00 121.81 ? 141 TYR C CA  1 
ATOM   6293  C  C   . TYR C 1 125 ? 132.456 155.062 108.467 1.00 121.81 ? 141 TYR C C   1 
ATOM   6294  O  O   . TYR C 1 125 ? 133.119 154.171 107.927 1.00 121.81 ? 141 TYR C O   1 
ATOM   6295  C  CB  . TYR C 1 125 ? 132.912 157.351 107.568 1.00 121.81 ? 141 TYR C CB  1 
ATOM   6296  C  CG  . TYR C 1 125 ? 132.867 158.142 106.281 1.00 121.81 ? 141 TYR C CG  1 
ATOM   6297  C  CD1 . TYR C 1 125 ? 131.888 157.899 105.327 1.00 121.81 ? 141 TYR C CD1 1 
ATOM   6298  C  CD2 . TYR C 1 125 ? 133.807 159.130 106.017 1.00 121.81 ? 141 TYR C CD2 1 
ATOM   6299  C  CE1 . TYR C 1 125 ? 131.845 158.618 104.148 1.00 121.81 ? 141 TYR C CE1 1 
ATOM   6300  C  CE2 . TYR C 1 125 ? 133.772 159.854 104.841 1.00 121.81 ? 141 TYR C CE2 1 
ATOM   6301  C  CZ  . TYR C 1 125 ? 132.789 159.594 103.911 1.00 121.81 ? 141 TYR C CZ  1 
ATOM   6302  O  OH  . TYR C 1 125 ? 132.751 160.313 102.739 1.00 121.81 ? 141 TYR C OH  1 
ATOM   6303  N  N   . GLN C 1 126 ? 132.208 155.064 109.775 1.00 117.90 ? 142 GLN C N   1 
ATOM   6304  C  CA  . GLN C 1 126 ? 132.859 154.106 110.658 1.00 117.90 ? 142 GLN C CA  1 
ATOM   6305  C  C   . GLN C 1 126 ? 132.039 153.930 111.925 1.00 117.90 ? 142 GLN C C   1 
ATOM   6306  O  O   . GLN C 1 126 ? 131.088 154.668 112.183 1.00 117.90 ? 142 GLN C O   1 
ATOM   6307  C  CB  . GLN C 1 126 ? 134.273 154.568 111.016 1.00 117.90 ? 142 GLN C CB  1 
ATOM   6308  C  CG  . GLN C 1 126 ? 134.323 155.846 111.835 1.00 117.90 ? 142 GLN C CG  1 
ATOM   6309  C  CD  . GLN C 1 126 ? 135.533 156.698 111.507 1.00 117.90 ? 142 GLN C CD  1 
ATOM   6310  O  OE1 . GLN C 1 126 ? 136.173 156.514 110.472 1.00 117.90 ? 142 GLN C OE1 1 
ATOM   6311  N  NE2 . GLN C 1 126 ? 135.853 157.636 112.391 1.00 117.90 ? 142 GLN C NE2 1 
ATOM   6312  N  N   . LEU C 1 127 ? 132.394 152.898 112.691 1.00 108.77 ? 143 LEU C N   1 
ATOM   6313  C  CA  . LEU C 1 127 ? 131.842 152.677 114.021 1.00 108.77 ? 143 LEU C CA  1 
ATOM   6314  C  C   . LEU C 1 127 ? 132.914 152.867 115.090 1.00 108.77 ? 143 LEU C C   1 
ATOM   6315  O  O   . LEU C 1 127 ? 132.878 152.226 116.143 1.00 108.77 ? 143 LEU C O   1 
ATOM   6316  C  CB  . LEU C 1 127 ? 131.221 151.285 114.122 1.00 108.77 ? 143 LEU C CB  1 
ATOM   6317  N  N   . THR C 1 128 ? 133.874 153.750 114.821 1.00 114.22 ? 144 THR C N   1 
ATOM   6318  C  CA  . THR C 1 128 ? 135.033 153.942 115.679 1.00 114.22 ? 144 THR C CA  1 
ATOM   6319  C  C   . THR C 1 128 ? 134.629 154.585 117.005 1.00 114.22 ? 144 THR C C   1 
ATOM   6320  O  O   . THR C 1 128 ? 133.474 154.959 117.227 1.00 114.22 ? 144 THR C O   1 
ATOM   6321  C  CB  . THR C 1 128 ? 136.083 154.793 114.968 1.00 114.22 ? 144 THR C CB  1 
ATOM   6322  N  N   . SER C 1 129 ? 135.612 154.713 117.901 1.00 126.34 ? 145 SER C N   1 
ATOM   6323  C  CA  . SER C 1 129 ? 135.410 155.435 119.151 1.00 126.34 ? 145 SER C CA  1 
ATOM   6324  C  C   . SER C 1 129 ? 135.149 156.916 118.921 1.00 126.34 ? 145 SER C C   1 
ATOM   6325  O  O   . SER C 1 129 ? 134.692 157.601 119.844 1.00 126.34 ? 145 SER C O   1 
ATOM   6326  C  CB  . SER C 1 129 ? 136.621 155.258 120.068 1.00 126.34 ? 145 SER C CB  1 
ATOM   6327  N  N   . LEU C 1 130 ? 135.422 157.415 117.713 1.00 120.81 ? 146 LEU C N   1 
ATOM   6328  C  CA  . LEU C 1 130 ? 135.095 158.796 117.380 1.00 120.81 ? 146 LEU C CA  1 
ATOM   6329  C  C   . LEU C 1 130 ? 133.594 159.021 117.477 1.00 120.81 ? 146 LEU C C   1 
ATOM   6330  O  O   . LEU C 1 130 ? 133.144 160.045 118.002 1.00 120.81 ? 146 LEU C O   1 
ATOM   6331  C  CB  . LEU C 1 130 ? 135.606 159.138 115.981 1.00 120.81 ? 146 LEU C CB  1 
ATOM   6332  C  CG  . LEU C 1 130 ? 135.368 160.573 115.514 1.00 120.81 ? 146 LEU C CG  1 
ATOM   6333  C  CD1 . LEU C 1 130 ? 136.201 161.535 116.344 1.00 120.81 ? 146 LEU C CD1 1 
ATOM   6334  C  CD2 . LEU C 1 130 ? 135.681 160.723 114.033 1.00 120.81 ? 146 LEU C CD2 1 
ATOM   6335  N  N   . PHE C 1 131 ? 132.805 158.083 116.947 1.00 117.90 ? 147 PHE C N   1 
ATOM   6336  C  CA  . PHE C 1 131 ? 131.352 158.196 117.019 1.00 117.90 ? 147 PHE C CA  1 
ATOM   6337  C  C   . PHE C 1 131 ? 130.878 158.192 118.462 1.00 117.90 ? 147 PHE C C   1 
ATOM   6338  O  O   . PHE C 1 131 ? 130.009 158.985 118.840 1.00 117.90 ? 147 PHE C O   1 
ATOM   6339  C  CB  . PHE C 1 131 ? 130.698 157.052 116.248 1.00 117.90 ? 147 PHE C CB  1 
ATOM   6340  N  N   . GLU C 1 132 ? 131.428 157.299 119.282 1.00 122.13 ? 148 GLU C N   1 
ATOM   6341  C  CA  . GLU C 1 132 ? 131.036 157.249 120.685 1.00 122.13 ? 148 GLU C CA  1 
ATOM   6342  C  C   . GLU C 1 132 ? 131.362 158.563 121.388 1.00 122.13 ? 148 GLU C C   1 
ATOM   6343  O  O   . GLU C 1 132 ? 130.528 159.109 122.121 1.00 122.13 ? 148 GLU C O   1 
ATOM   6344  C  CB  . GLU C 1 132 ? 131.720 156.069 121.371 1.00 122.13 ? 148 GLU C CB  1 
ATOM   6345  N  N   . GLU C 1 133 ? 132.564 159.104 121.154 1.00 134.11 ? 149 GLU C N   1 
ATOM   6346  C  CA  . GLU C 1 133 ? 132.943 160.354 121.808 1.00 134.11 ? 149 GLU C CA  1 
ATOM   6347  C  C   . GLU C 1 133 ? 132.092 161.524 121.334 1.00 134.11 ? 149 GLU C C   1 
ATOM   6348  O  O   . GLU C 1 133 ? 131.632 162.327 122.152 1.00 134.11 ? 149 GLU C O   1 
ATOM   6349  C  CB  . GLU C 1 133 ? 134.422 160.658 121.557 1.00 134.11 ? 149 GLU C CB  1 
ATOM   6350  C  CG  . GLU C 1 133 ? 135.045 161.683 122.511 1.00 134.11 ? 149 GLU C CG  1 
ATOM   6351  C  CD  . GLU C 1 133 ? 135.102 161.230 123.952 1.00 134.11 ? 149 GLU C CD  1 
ATOM   6352  O  OE1 . GLU C 1 133 ? 134.884 160.034 124.214 1.00 134.11 ? 149 GLU C OE1 1 
ATOM   6353  O  OE2 . GLU C 1 133 ? 135.371 162.079 124.827 1.00 134.11 ? 149 GLU C OE2 1 
ATOM   6354  N  N   . CYS C 1 134 ? 131.860 161.634 120.026 1.00 116.67 ? 150 CYS C N   1 
ATOM   6355  C  CA  . CYS C 1 134 ? 131.050 162.734 119.515 1.00 116.67 ? 150 CYS C CA  1 
ATOM   6356  C  C   . CYS C 1 134 ? 129.608 162.646 120.000 1.00 116.67 ? 150 CYS C C   1 
ATOM   6357  O  O   . CYS C 1 134 ? 129.005 163.663 120.364 1.00 116.67 ? 150 CYS C O   1 
ATOM   6358  C  CB  . CYS C 1 134 ? 131.097 162.752 117.990 1.00 116.67 ? 150 CYS C CB  1 
ATOM   6359  S  SG  . CYS C 1 134 ? 130.026 161.529 117.226 1.00 116.67 ? 150 CYS C SG  1 
ATOM   6360  N  N   . SER C 1 135 ? 129.033 161.439 120.011 1.00 122.44 ? 151 SER C N   1 
ATOM   6361  C  CA  . SER C 1 135 ? 127.667 161.287 120.494 1.00 122.44 ? 151 SER C CA  1 
ATOM   6362  C  C   . SER C 1 135 ? 127.556 161.593 121.980 1.00 122.44 ? 151 SER C C   1 
ATOM   6363  O  O   . SER C 1 135 ? 126.601 162.251 122.410 1.00 122.44 ? 151 SER C O   1 
ATOM   6364  C  CB  . SER C 1 135 ? 127.179 159.869 120.211 1.00 122.44 ? 151 SER C CB  1 
ATOM   6365  N  N   . ARG C 1 136 ? 128.516 161.125 122.782 1.00 132.34 ? 152 ARG C N   1 
ATOM   6366  C  CA  . ARG C 1 136 ? 128.521 161.481 124.196 1.00 132.34 ? 152 ARG C CA  1 
ATOM   6367  C  C   . ARG C 1 136 ? 128.654 162.985 124.391 1.00 132.34 ? 152 ARG C C   1 
ATOM   6368  O  O   . ARG C 1 136 ? 127.988 163.569 125.254 1.00 132.34 ? 152 ARG C O   1 
ATOM   6369  C  CB  . ARG C 1 136 ? 129.638 160.750 124.941 1.00 132.34 ? 152 ARG C CB  1 
ATOM   6370  C  CG  . ARG C 1 136 ? 129.338 159.302 125.277 1.00 132.34 ? 152 ARG C CG  1 
ATOM   6371  C  CD  . ARG C 1 136 ? 130.571 158.610 125.836 1.00 132.34 ? 152 ARG C CD  1 
ATOM   6372  N  NE  . ARG C 1 136 ? 131.467 158.076 124.818 1.00 132.34 ? 152 ARG C NE  1 
ATOM   6373  C  CZ  . ARG C 1 136 ? 132.317 157.081 125.029 1.00 132.34 ? 152 ARG C CZ  1 
ATOM   6374  N  NH1 . ARG C 1 136 ? 132.374 156.455 126.193 1.00 132.34 ? 152 ARG C NH1 1 
ATOM   6375  N  NH2 . ARG C 1 136 ? 133.140 156.712 124.053 1.00 132.34 ? 152 ARG C NH2 1 
ATOM   6376  N  N   . PHE C 1 137 ? 129.501 163.630 123.587 1.00 121.52 ? 153 PHE C N   1 
ATOM   6377  C  CA  . PHE C 1 137 ? 129.688 165.073 123.691 1.00 121.52 ? 153 PHE C CA  1 
ATOM   6378  C  C   . PHE C 1 137 ? 128.411 165.826 123.346 1.00 121.52 ? 153 PHE C C   1 
ATOM   6379  O  O   . PHE C 1 137 ? 128.079 166.825 123.995 1.00 121.52 ? 153 PHE C O   1 
ATOM   6380  C  CB  . PHE C 1 137 ? 130.840 165.509 122.786 1.00 121.52 ? 153 PHE C CB  1 
ATOM   6381  C  CG  . PHE C 1 137 ? 131.466 166.809 123.188 1.00 121.52 ? 153 PHE C CG  1 
ATOM   6382  C  CD1 . PHE C 1 137 ? 132.464 166.835 124.146 1.00 121.52 ? 153 PHE C CD1 1 
ATOM   6383  C  CD2 . PHE C 1 137 ? 131.069 168.000 122.609 1.00 121.52 ? 153 PHE C CD2 1 
ATOM   6384  C  CE1 . PHE C 1 137 ? 133.050 168.024 124.525 1.00 121.52 ? 153 PHE C CE1 1 
ATOM   6385  C  CE2 . PHE C 1 137 ? 131.654 169.195 122.983 1.00 121.52 ? 153 PHE C CE2 1 
ATOM   6386  C  CZ  . PHE C 1 137 ? 132.647 169.204 123.941 1.00 121.52 ? 153 PHE C CZ  1 
ATOM   6387  N  N   . LEU C 1 138 ? 127.690 165.376 122.318 1.00 104.41 ? 154 LEU C N   1 
ATOM   6388  C  CA  . LEU C 1 138 ? 126.413 166.004 122.001 1.00 104.41 ? 154 LEU C CA  1 
ATOM   6389  C  C   . LEU C 1 138 ? 125.428 165.845 123.153 1.00 104.41 ? 154 LEU C C   1 
ATOM   6390  O  O   . LEU C 1 138 ? 124.648 166.760 123.442 1.00 104.41 ? 154 LEU C O   1 
ATOM   6391  C  CB  . LEU C 1 138 ? 125.839 165.417 120.713 1.00 104.41 ? 154 LEU C CB  1 
ATOM   6392  C  CG  . LEU C 1 138 ? 126.006 166.284 119.464 1.00 104.41 ? 154 LEU C CG  1 
ATOM   6393  C  CD1 . LEU C 1 138 ? 125.815 165.459 118.204 1.00 104.41 ? 154 LEU C CD1 1 
ATOM   6394  C  CD2 . LEU C 1 138 ? 125.030 167.450 119.497 1.00 104.41 ? 154 LEU C CD2 1 
ATOM   6395  N  N   . ALA C 1 139 ? 125.441 164.689 123.811 1.00 100.33 ? 155 ALA C N   1 
ATOM   6396  C  CA  . ALA C 1 139 ? 124.583 164.437 124.968 1.00 100.33 ? 155 ALA C CA  1 
ATOM   6397  C  C   . ALA C 1 139 ? 124.777 165.488 126.054 1.00 100.33 ? 155 ALA C C   1 
ATOM   6398  O  O   . ALA C 1 139 ? 125.866 166.038 126.209 1.00 100.33 ? 155 ALA C O   1 
ATOM   6399  C  CB  . ALA C 1 139 ? 124.843 163.046 125.527 1.00 100.33 ? 155 ALA C CB  1 
ATOM   6400  N  N   . GLY C 1 145 ? 116.219 173.817 124.259 1.00 114.56 ? 161 GLY C N   1 
ATOM   6401  C  CA  . GLY C 1 145 ? 116.540 174.606 123.084 1.00 114.56 ? 161 GLY C CA  1 
ATOM   6402  C  C   . GLY C 1 145 ? 116.931 173.763 121.887 1.00 114.56 ? 161 GLY C C   1 
ATOM   6403  O  O   . GLY C 1 145 ? 116.411 173.948 120.787 1.00 114.56 ? 161 GLY C O   1 
ATOM   6404  N  N   . ASN C 1 146 ? 117.858 172.832 122.103 1.00 125.55 ? 162 ASN C N   1 
ATOM   6405  C  CA  . ASN C 1 146 ? 118.325 171.932 121.058 1.00 125.55 ? 162 ASN C CA  1 
ATOM   6406  C  C   . ASN C 1 146 ? 117.873 170.495 121.269 1.00 125.55 ? 162 ASN C C   1 
ATOM   6407  O  O   . ASN C 1 146 ? 118.226 169.625 120.465 1.00 125.55 ? 162 ASN C O   1 
ATOM   6408  C  CB  . ASN C 1 146 ? 119.855 171.984 120.965 1.00 125.55 ? 162 ASN C CB  1 
ATOM   6409  C  CG  . ASN C 1 146 ? 120.532 171.494 122.230 1.00 125.55 ? 162 ASN C CG  1 
ATOM   6410  O  OD1 . ASN C 1 146 ? 120.002 171.646 123.330 1.00 125.55 ? 162 ASN C OD1 1 
ATOM   6411  N  ND2 . ASN C 1 146 ? 121.712 170.904 122.079 1.00 125.55 ? 162 ASN C ND2 1 
ATOM   6412  N  N   . CYS C 1 147 ? 117.111 170.222 122.331 1.00 141.26 ? 163 CYS C N   1 
ATOM   6413  C  CA  . CYS C 1 147 ? 116.683 168.855 122.617 1.00 141.26 ? 163 CYS C CA  1 
ATOM   6414  C  C   . CYS C 1 147 ? 115.818 168.287 121.497 1.00 141.26 ? 163 CYS C C   1 
ATOM   6415  O  O   . CYS C 1 147 ? 115.978 167.123 121.113 1.00 141.26 ? 163 CYS C O   1 
ATOM   6416  C  CB  . CYS C 1 147 ? 115.935 168.809 123.950 1.00 141.26 ? 163 CYS C CB  1 
ATOM   6417  S  SG  . CYS C 1 147 ? 114.536 169.945 124.060 1.00 141.26 ? 163 CYS C SG  1 
ATOM   6418  N  N   . LEU C 1 148 ? 114.902 169.094 120.954 1.00 136.82 ? 164 LEU C N   1 
ATOM   6419  C  CA  . LEU C 1 148 ? 113.969 168.594 119.945 1.00 136.82 ? 164 LEU C CA  1 
ATOM   6420  C  C   . LEU C 1 148 ? 114.681 168.130 118.679 1.00 136.82 ? 164 LEU C C   1 
ATOM   6421  O  O   . LEU C 1 148 ? 114.155 167.282 117.950 1.00 136.82 ? 164 LEU C O   1 
ATOM   6422  C  CB  . LEU C 1 148 ? 112.935 169.669 119.612 1.00 136.82 ? 164 LEU C CB  1 
ATOM   6423  C  CG  . LEU C 1 148 ? 112.080 170.151 120.786 1.00 136.82 ? 164 LEU C CG  1 
ATOM   6424  C  CD1 . LEU C 1 148 ? 110.977 171.080 120.306 1.00 136.82 ? 164 LEU C CD1 1 
ATOM   6425  C  CD2 . LEU C 1 148 ? 111.495 168.966 121.539 1.00 136.82 ? 164 LEU C CD2 1 
ATOM   6426  N  N   . GLN C 1 149 ? 115.865 168.669 118.398 1.00 119.81 ? 165 GLN C N   1 
ATOM   6427  C  CA  . GLN C 1 149 ? 116.620 168.298 117.206 1.00 119.81 ? 165 GLN C CA  1 
ATOM   6428  C  C   . GLN C 1 149 ? 117.520 167.099 117.470 1.00 119.81 ? 165 GLN C C   1 
ATOM   6429  O  O   . GLN C 1 149 ? 117.642 166.204 116.624 1.00 119.81 ? 165 GLN C O   1 
ATOM   6430  C  CB  . GLN C 1 149 ? 117.454 169.485 116.716 1.00 119.81 ? 165 GLN C CB  1 
ATOM   6431  N  N   . VAL C 1 150 ? 118.154 167.074 118.643 1.00 129.02 ? 166 VAL C N   1 
ATOM   6432  C  CA  . VAL C 1 150 ? 119.008 165.954 119.015 1.00 129.02 ? 166 VAL C CA  1 
ATOM   6433  C  C   . VAL C 1 150 ? 118.181 164.684 119.206 1.00 129.02 ? 166 VAL C C   1 
ATOM   6434  O  O   . VAL C 1 150 ? 118.677 163.580 118.960 1.00 129.02 ? 166 VAL C O   1 
ATOM   6435  C  CB  . VAL C 1 150 ? 119.852 166.331 120.247 1.00 129.02 ? 166 VAL C CB  1 
ATOM   6436  C  CG1 . VAL C 1 150 ? 119.084 166.123 121.514 1.00 129.02 ? 166 VAL C CG1 1 
ATOM   6437  C  CG2 . VAL C 1 150 ? 121.139 165.516 120.271 1.00 129.02 ? 166 VAL C CG2 1 
ATOM   6438  N  N   . MET C 1 151 ? 116.921 164.807 119.641 1.00 135.85 ? 167 MET C N   1 
ATOM   6439  C  CA  . MET C 1 151 ? 116.027 163.650 119.655 1.00 135.85 ? 167 MET C CA  1 
ATOM   6440  C  C   . MET C 1 151 ? 115.916 163.029 118.270 1.00 135.85 ? 167 MET C C   1 
ATOM   6441  O  O   . MET C 1 151 ? 116.073 161.814 118.105 1.00 135.85 ? 167 MET C O   1 
ATOM   6442  C  CB  . MET C 1 151 ? 114.633 164.048 120.148 1.00 135.85 ? 167 MET C CB  1 
ATOM   6443  C  CG  . MET C 1 151 ? 114.524 164.470 121.593 1.00 135.85 ? 167 MET C CG  1 
ATOM   6444  S  SD  . MET C 1 151 ? 114.658 163.047 122.690 1.00 135.85 ? 167 MET C SD  1 
ATOM   6445  C  CE  . MET C 1 151 ? 112.954 162.866 123.209 1.00 135.85 ? 167 MET C CE  1 
ATOM   6446  N  N   . TRP C 1 152 ? 115.630 163.853 117.261 1.00 126.87 ? 168 TRP C N   1 
ATOM   6447  C  CA  . TRP C 1 152 ? 115.491 163.339 115.904 1.00 126.87 ? 168 TRP C CA  1 
ATOM   6448  C  C   . TRP C 1 152 ? 116.805 162.765 115.395 1.00 126.87 ? 168 TRP C C   1 
ATOM   6449  O  O   . TRP C 1 152 ? 116.817 161.730 114.720 1.00 126.87 ? 168 TRP C O   1 
ATOM   6450  C  CB  . TRP C 1 152 ? 114.994 164.447 114.976 1.00 126.87 ? 168 TRP C CB  1 
ATOM   6451  N  N   . LEU C 1 153 ? 117.923 163.424 115.704 1.00 140.42 ? 169 LEU C N   1 
ATOM   6452  C  CA  . LEU C 1 153 ? 119.221 162.914 115.270 1.00 140.42 ? 169 LEU C CA  1 
ATOM   6453  C  C   . LEU C 1 153 ? 119.511 161.542 115.875 1.00 140.42 ? 169 LEU C C   1 
ATOM   6454  O  O   . LEU C 1 153 ? 119.907 160.606 115.167 1.00 140.42 ? 169 LEU C O   1 
ATOM   6455  C  CB  . LEU C 1 153 ? 120.320 163.910 115.639 1.00 140.42 ? 169 LEU C CB  1 
ATOM   6456  N  N   . ALA C 1 154 ? 119.310 161.402 117.190 1.00 131.73 ? 170 ALA C N   1 
ATOM   6457  C  CA  . ALA C 1 154 ? 119.538 160.121 117.850 1.00 131.73 ? 170 ALA C CA  1 
ATOM   6458  C  C   . ALA C 1 154 ? 118.596 159.045 117.325 1.00 131.73 ? 170 ALA C C   1 
ATOM   6459  O  O   . ALA C 1 154 ? 119.004 157.893 117.137 1.00 131.73 ? 170 ALA C O   1 
ATOM   6460  C  CB  . ALA C 1 154 ? 119.388 160.276 119.364 1.00 131.73 ? 170 ALA C CB  1 
ATOM   6461  N  N   . ASP C 1 155 ? 117.328 159.397 117.094 1.00 134.79 ? 171 ASP C N   1 
ATOM   6462  C  CA  . ASP C 1 155 ? 116.382 158.429 116.550 1.00 134.79 ? 171 ASP C CA  1 
ATOM   6463  C  C   . ASP C 1 155 ? 116.798 157.970 115.159 1.00 134.79 ? 171 ASP C C   1 
ATOM   6464  O  O   . ASP C 1 155 ? 116.718 156.779 114.840 1.00 134.79 ? 171 ASP C O   1 
ATOM   6465  C  CB  . ASP C 1 155 ? 114.977 159.031 116.519 1.00 134.79 ? 171 ASP C CB  1 
ATOM   6466  N  N   . ARG C 1 156 ? 117.244 158.904 114.316 1.00 133.12 ? 172 ARG C N   1 
ATOM   6467  C  CA  . ARG C 1 156 ? 117.596 158.551 112.947 1.00 133.12 ? 172 ARG C CA  1 
ATOM   6468  C  C   . ARG C 1 156 ? 118.901 157.770 112.883 1.00 133.12 ? 172 ARG C C   1 
ATOM   6469  O  O   . ARG C 1 156 ? 119.093 156.968 111.962 1.00 133.12 ? 172 ARG C O   1 
ATOM   6470  C  CB  . ARG C 1 156 ? 117.689 159.810 112.085 1.00 133.12 ? 172 ARG C CB  1 
ATOM   6471  N  N   . HIS C 1 157 ? 119.803 157.979 113.843 1.00 137.10 ? 173 HIS C N   1 
ATOM   6472  C  CA  . HIS C 1 157 ? 121.088 157.292 113.841 1.00 137.10 ? 173 HIS C CA  1 
ATOM   6473  C  C   . HIS C 1 157 ? 121.174 156.181 114.882 1.00 137.10 ? 173 HIS C C   1 
ATOM   6474  O  O   . HIS C 1 157 ? 122.258 155.625 115.087 1.00 137.10 ? 173 HIS C O   1 
ATOM   6475  C  CB  . HIS C 1 157 ? 122.216 158.302 114.054 1.00 137.10 ? 173 HIS C CB  1 
ATOM   6476  C  CG  . HIS C 1 157 ? 122.331 159.315 112.958 1.00 137.10 ? 173 HIS C CG  1 
ATOM   6477  N  ND1 . HIS C 1 157 ? 121.898 160.615 113.101 1.00 137.10 ? 173 HIS C ND1 1 
ATOM   6478  C  CD2 . HIS C 1 157 ? 122.817 159.216 111.698 1.00 137.10 ? 173 HIS C CD2 1 
ATOM   6479  C  CE1 . HIS C 1 157 ? 122.118 161.276 111.979 1.00 137.10 ? 173 HIS C CE1 1 
ATOM   6480  N  NE2 . HIS C 1 157 ? 122.675 160.451 111.112 1.00 137.10 ? 173 HIS C NE2 1 
ATOM   6481  N  N   . SER C 1 158 ? 120.059 155.833 115.526 1.00 141.39 ? 174 SER C N   1 
ATOM   6482  C  CA  . SER C 1 158 ? 119.965 154.671 116.413 1.00 141.39 ? 174 SER C CA  1 
ATOM   6483  C  C   . SER C 1 158 ? 121.049 154.700 117.491 1.00 141.39 ? 174 SER C C   1 
ATOM   6484  O  O   . SER C 1 158 ? 121.898 153.811 117.589 1.00 141.39 ? 174 SER C O   1 
ATOM   6485  C  CB  . SER C 1 158 ? 120.024 153.371 115.608 1.00 141.39 ? 174 SER C CB  1 
ATOM   6486  N  N   . ASP C 1 159 ? 121.011 155.750 118.309 1.00 141.45 ? 175 ASP C N   1 
ATOM   6487  C  CA  . ASP C 1 159 ? 121.938 155.878 119.429 1.00 141.45 ? 175 ASP C CA  1 
ATOM   6488  C  C   . ASP C 1 159 ? 121.159 155.722 120.729 1.00 141.45 ? 175 ASP C C   1 
ATOM   6489  O  O   . ASP C 1 159 ? 120.438 156.646 121.135 1.00 141.45 ? 175 ASP C O   1 
ATOM   6490  C  CB  . ASP C 1 159 ? 122.661 157.229 119.376 1.00 141.45 ? 175 ASP C CB  1 
ATOM   6491  C  CG  . ASP C 1 159 ? 123.598 157.467 120.561 1.00 141.45 ? 175 ASP C CG  1 
ATOM   6492  O  OD1 . ASP C 1 159 ? 123.355 156.987 121.687 1.00 141.45 ? 175 ASP C OD1 1 
ATOM   6493  O  OD2 . ASP C 1 159 ? 124.611 158.160 120.355 1.00 141.45 ? 175 ASP C OD2 1 
ATOM   6494  N  N   . PRO C 1 160 ? 121.262 154.583 121.414 1.00 148.60 ? 176 PRO C N   1 
ATOM   6495  C  CA  . PRO C 1 160 ? 120.514 154.378 122.659 1.00 148.60 ? 176 PRO C CA  1 
ATOM   6496  C  C   . PRO C 1 160 ? 121.089 155.091 123.874 1.00 148.60 ? 176 PRO C C   1 
ATOM   6497  O  O   . PRO C 1 160 ? 120.617 154.846 124.987 1.00 148.60 ? 176 PRO C O   1 
ATOM   6498  C  CB  . PRO C 1 160 ? 120.588 152.855 122.844 1.00 148.60 ? 176 PRO C CB  1 
ATOM   6499  C  CG  . PRO C 1 160 ? 121.872 152.473 122.201 1.00 148.60 ? 176 PRO C CG  1 
ATOM   6500  C  CD  . PRO C 1 160 ? 122.040 153.394 121.026 1.00 148.60 ? 176 PRO C CD  1 
ATOM   6501  N  N   . GLU C 1 161 ? 122.095 155.945 123.704 1.00 146.03 ? 177 GLU C N   1 
ATOM   6502  C  CA  . GLU C 1 161 ? 122.669 156.731 124.793 1.00 146.03 ? 177 GLU C CA  1 
ATOM   6503  C  C   . GLU C 1 161 ? 122.358 158.213 124.675 1.00 146.03 ? 177 GLU C C   1 
ATOM   6504  O  O   . GLU C 1 161 ? 122.011 158.850 125.672 1.00 146.03 ? 177 GLU C O   1 
ATOM   6505  C  CB  . GLU C 1 161 ? 124.187 156.533 124.849 1.00 146.03 ? 177 GLU C CB  1 
ATOM   6506  N  N   . LEU C 1 162 ? 122.494 158.776 123.473 1.00 135.62 ? 178 LEU C N   1 
ATOM   6507  C  CA  . LEU C 1 162 ? 122.074 160.151 123.232 1.00 135.62 ? 178 LEU C CA  1 
ATOM   6508  C  C   . LEU C 1 162 ? 120.566 160.298 123.364 1.00 135.62 ? 178 LEU C C   1 
ATOM   6509  O  O   . LEU C 1 162 ? 120.077 161.341 123.820 1.00 135.62 ? 178 LEU C O   1 
ATOM   6510  C  CB  . LEU C 1 162 ? 122.526 160.583 121.836 1.00 135.62 ? 178 LEU C CB  1 
ATOM   6511  C  CG  . LEU C 1 162 ? 122.273 162.010 121.351 1.00 135.62 ? 178 LEU C CG  1 
ATOM   6512  C  CD1 . LEU C 1 162 ? 122.986 163.011 122.220 1.00 135.62 ? 178 LEU C CD1 1 
ATOM   6513  C  CD2 . LEU C 1 162 ? 122.712 162.154 119.902 1.00 135.62 ? 178 LEU C CD2 1 
ATOM   6514  N  N   . TYR C 1 163 ? 119.821 159.261 122.977 1.00 136.57 ? 179 TYR C N   1 
ATOM   6515  C  CA  . TYR C 1 163 ? 118.365 159.323 123.007 1.00 136.57 ? 179 TYR C CA  1 
ATOM   6516  C  C   . TYR C 1 163 ? 117.834 159.533 124.420 1.00 136.57 ? 179 TYR C C   1 
ATOM   6517  O  O   . TYR C 1 163 ? 116.926 160.341 124.628 1.00 136.57 ? 179 TYR C O   1 
ATOM   6518  C  CB  . TYR C 1 163 ? 117.771 158.061 122.387 1.00 136.57 ? 179 TYR C CB  1 
ATOM   6519  C  CG  . TYR C 1 163 ? 116.385 158.273 121.823 1.00 136.57 ? 179 TYR C CG  1 
ATOM   6520  C  CD1 . TYR C 1 163 ? 116.202 158.927 120.612 1.00 136.57 ? 179 TYR C CD1 1 
ATOM   6521  C  CD2 . TYR C 1 163 ? 115.261 157.820 122.500 1.00 136.57 ? 179 TYR C CD2 1 
ATOM   6522  C  CE1 . TYR C 1 163 ? 114.939 159.125 120.092 1.00 136.57 ? 179 TYR C CE1 1 
ATOM   6523  C  CE2 . TYR C 1 163 ? 113.994 158.014 121.987 1.00 136.57 ? 179 TYR C CE2 1 
ATOM   6524  C  CZ  . TYR C 1 163 ? 113.838 158.666 120.783 1.00 136.57 ? 179 TYR C CZ  1 
ATOM   6525  O  OH  . TYR C 1 163 ? 112.578 158.861 120.269 1.00 136.57 ? 179 TYR C OH  1 
ATOM   6526  N  N   . THR C 1 164 ? 118.374 158.809 125.406 1.00 135.73 ? 180 THR C N   1 
ATOM   6527  C  CA  . THR C 1 164 ? 117.857 158.952 126.767 1.00 135.73 ? 180 THR C CA  1 
ATOM   6528  C  C   . THR C 1 164 ? 118.224 160.304 127.368 1.00 135.73 ? 180 THR C C   1 
ATOM   6529  O  O   . THR C 1 164 ? 117.411 160.912 128.072 1.00 135.73 ? 180 THR C O   1 
ATOM   6530  C  CB  . THR C 1 164 ? 118.377 157.824 127.657 1.00 135.73 ? 180 THR C CB  1 
ATOM   6531  O  OG1 . THR C 1 164 ? 118.797 158.366 128.916 1.00 135.73 ? 180 THR C OG1 1 
ATOM   6532  C  CG2 . THR C 1 164 ? 119.554 157.128 127.003 1.00 135.73 ? 180 THR C CG2 1 
ATOM   6533  N  N   . ALA C 1 165 ? 119.441 160.789 127.110 1.00 131.91 ? 181 ALA C N   1 
ATOM   6534  C  CA  . ALA C 1 165 ? 119.825 162.112 127.596 1.00 131.91 ? 181 ALA C CA  1 
ATOM   6535  C  C   . ALA C 1 165 ? 118.929 163.185 126.995 1.00 131.91 ? 181 ALA C C   1 
ATOM   6536  O  O   . ALA C 1 165 ? 118.475 164.107 127.692 1.00 131.91 ? 181 ALA C O   1 
ATOM   6537  C  CB  . ALA C 1 165 ? 121.292 162.388 127.268 1.00 131.91 ? 181 ALA C CB  1 
ATOM   6538  N  N   . ALA C 1 166 ? 118.610 163.040 125.709 1.00 127.15 ? 182 ALA C N   1 
ATOM   6539  C  CA  . ALA C 1 166 ? 117.749 164.011 125.054 1.00 127.15 ? 182 ALA C CA  1 
ATOM   6540  C  C   . ALA C 1 166 ? 116.319 163.906 125.562 1.00 127.15 ? 182 ALA C C   1 
ATOM   6541  O  O   . ALA C 1 166 ? 115.632 164.924 125.698 1.00 127.15 ? 182 ALA C O   1 
ATOM   6542  C  CB  . ALA C 1 166 ? 117.808 163.801 123.546 1.00 127.15 ? 182 ALA C CB  1 
ATOM   6543  N  N   . LYS C 1 167 ? 115.843 162.688 125.830 1.00 141.02 ? 183 LYS C N   1 
ATOM   6544  C  CA  . LYS C 1 167 ? 114.497 162.538 126.366 1.00 141.02 ? 183 LYS C CA  1 
ATOM   6545  C  C   . LYS C 1 167 ? 114.409 163.160 127.751 1.00 141.02 ? 183 LYS C C   1 
ATOM   6546  O  O   . LYS C 1 167 ? 113.407 163.794 128.095 1.00 141.02 ? 183 LYS C O   1 
ATOM   6547  C  CB  . LYS C 1 167 ? 114.103 161.061 126.403 1.00 141.02 ? 183 LYS C CB  1 
ATOM   6548  N  N   . HIS C 1 168 ? 115.456 162.982 128.560 1.00 147.48 ? 184 HIS C N   1 
ATOM   6549  C  CA  . HIS C 1 168 ? 115.518 163.624 129.868 1.00 147.48 ? 184 HIS C CA  1 
ATOM   6550  C  C   . HIS C 1 168 ? 115.411 165.138 129.733 1.00 147.48 ? 184 HIS C C   1 
ATOM   6551  O  O   . HIS C 1 168 ? 114.605 165.782 130.418 1.00 147.48 ? 184 HIS C O   1 
ATOM   6552  C  CB  . HIS C 1 168 ? 116.809 163.225 130.584 1.00 147.48 ? 184 HIS C CB  1 
ATOM   6553  C  CG  . HIS C 1 168 ? 116.953 163.814 131.952 1.00 147.48 ? 184 HIS C CG  1 
ATOM   6554  N  ND1 . HIS C 1 168 ? 117.213 165.151 132.164 1.00 147.48 ? 184 HIS C ND1 1 
ATOM   6555  C  CD2 . HIS C 1 168 ? 116.871 163.248 133.180 1.00 147.48 ? 184 HIS C CD2 1 
ATOM   6556  C  CE1 . HIS C 1 168 ? 117.289 165.383 133.462 1.00 147.48 ? 184 HIS C CE1 1 
ATOM   6557  N  NE2 . HIS C 1 168 ? 117.084 164.245 134.101 1.00 147.48 ? 184 HIS C NE2 1 
ATOM   6558  N  N   . CYS C 1 169 ? 116.221 165.725 128.844 1.00 149.54 ? 185 CYS C N   1 
ATOM   6559  C  CA  . CYS C 1 169 ? 116.184 167.176 128.677 1.00 149.54 ? 185 CYS C CA  1 
ATOM   6560  C  C   . CYS C 1 169 ? 114.822 167.646 128.173 1.00 149.54 ? 185 CYS C C   1 
ATOM   6561  O  O   . CYS C 1 169 ? 114.288 168.651 128.657 1.00 149.54 ? 185 CYS C O   1 
ATOM   6562  C  CB  . CYS C 1 169 ? 117.290 167.625 127.722 1.00 149.54 ? 185 CYS C CB  1 
ATOM   6563  S  SG  . CYS C 1 169 ? 117.479 169.419 127.591 1.00 149.54 ? 185 CYS C SG  1 
ATOM   6564  N  N   . ALA C 1 170 ? 114.251 166.939 127.195 1.00 144.44 ? 186 ALA C N   1 
ATOM   6565  C  CA  . ALA C 1 170 ? 112.962 167.336 126.634 1.00 144.44 ? 186 ALA C CA  1 
ATOM   6566  C  C   . ALA C 1 170 ? 111.848 167.244 127.669 1.00 144.44 ? 186 ALA C C   1 
ATOM   6567  O  O   . ALA C 1 170 ? 110.989 168.130 127.749 1.00 144.44 ? 186 ALA C O   1 
ATOM   6568  C  CB  . ALA C 1 170 ? 112.632 166.476 125.414 1.00 144.44 ? 186 ALA C CB  1 
ATOM   6569  N  N   . LYS C 1 171 ? 111.842 166.174 128.468 1.00 143.70 ? 187 LYS C N   1 
ATOM   6570  C  CA  . LYS C 1 171 ? 110.832 166.017 129.507 1.00 143.70 ? 187 LYS C CA  1 
ATOM   6571  C  C   . LYS C 1 171 ? 110.975 167.073 130.592 1.00 143.70 ? 187 LYS C C   1 
ATOM   6572  O  O   . LYS C 1 171 ? 109.971 167.597 131.087 1.00 143.70 ? 187 LYS C O   1 
ATOM   6573  C  CB  . LYS C 1 171 ? 110.915 164.614 130.110 1.00 143.70 ? 187 LYS C CB  1 
ATOM   6574  N  N   . THR C 1 172 ? 112.210 167.395 130.986 1.00 148.65 ? 188 THR C N   1 
ATOM   6575  C  CA  . THR C 1 172 ? 112.395 168.403 132.024 1.00 148.65 ? 188 THR C CA  1 
ATOM   6576  C  C   . THR C 1 172 ? 111.910 169.770 131.554 1.00 148.65 ? 188 THR C C   1 
ATOM   6577  O  O   . THR C 1 172 ? 111.316 170.528 132.331 1.00 148.65 ? 188 THR C O   1 
ATOM   6578  C  CB  . THR C 1 172 ? 113.866 168.465 132.438 1.00 148.65 ? 188 THR C CB  1 
ATOM   6579  O  OG1 . THR C 1 172 ? 114.263 167.200 132.983 1.00 148.65 ? 188 THR C OG1 1 
ATOM   6580  C  CG2 . THR C 1 172 ? 114.082 169.545 133.487 1.00 148.65 ? 188 THR C CG2 1 
ATOM   6581  N  N   . HIS C 1 173 ? 112.140 170.098 130.282 1.00 142.59 ? 189 HIS C N   1 
ATOM   6582  C  CA  . HIS C 1 173 ? 111.773 171.391 129.718 1.00 142.59 ? 189 HIS C CA  1 
ATOM   6583  C  C   . HIS C 1 173 ? 110.522 171.316 128.845 1.00 142.59 ? 189 HIS C C   1 
ATOM   6584  O  O   . HIS C 1 173 ? 110.373 172.109 127.909 1.00 142.59 ? 189 HIS C O   1 
ATOM   6585  C  CB  . HIS C 1 173 ? 112.944 171.975 128.927 1.00 142.59 ? 189 HIS C CB  1 
ATOM   6586  C  CG  . HIS C 1 173 ? 114.098 172.394 129.784 1.00 142.59 ? 189 HIS C CG  1 
ATOM   6587  N  ND1 . HIS C 1 173 ? 114.671 171.561 130.721 1.00 142.59 ? 189 HIS C ND1 1 
ATOM   6588  C  CD2 . HIS C 1 173 ? 114.783 173.560 129.849 1.00 142.59 ? 189 HIS C CD2 1 
ATOM   6589  C  CE1 . HIS C 1 173 ? 115.660 172.195 131.325 1.00 142.59 ? 189 HIS C CE1 1 
ATOM   6590  N  NE2 . HIS C 1 173 ? 115.750 173.410 130.814 1.00 142.59 ? 189 HIS C NE2 1 
ATOM   6591  N  N   . LEU C 1 174 ? 109.621 170.371 129.127 1.00 129.45 ? 190 LEU C N   1 
ATOM   6592  C  CA  . LEU C 1 174 ? 108.404 170.249 128.330 1.00 129.45 ? 190 LEU C CA  1 
ATOM   6593  C  C   . LEU C 1 174 ? 107.508 171.472 128.487 1.00 129.45 ? 190 LEU C C   1 
ATOM   6594  O  O   . LEU C 1 174 ? 106.869 171.907 127.522 1.00 129.45 ? 190 LEU C O   1 
ATOM   6595  C  CB  . LEU C 1 174 ? 107.646 168.979 128.716 1.00 129.45 ? 190 LEU C CB  1 
ATOM   6596  C  CG  . LEU C 1 174 ? 106.628 168.452 127.701 1.00 129.45 ? 190 LEU C CG  1 
ATOM   6597  C  CD1 . LEU C 1 174 ? 107.127 168.634 126.275 1.00 129.45 ? 190 LEU C CD1 1 
ATOM   6598  C  CD2 . LEU C 1 174 ? 106.301 166.992 127.976 1.00 129.45 ? 190 LEU C CD2 1 
ATOM   6599  N  N   . ALA C 1 175 ? 107.442 172.034 129.696 1.00 138.53 ? 191 ALA C N   1 
ATOM   6600  C  CA  . ALA C 1 175 ? 106.647 173.239 129.914 1.00 138.53 ? 191 ALA C CA  1 
ATOM   6601  C  C   . ALA C 1 175 ? 107.179 174.410 129.097 1.00 138.53 ? 191 ALA C C   1 
ATOM   6602  O  O   . ALA C 1 175 ? 106.401 175.172 128.510 1.00 138.53 ? 191 ALA C O   1 
ATOM   6603  C  CB  . ALA C 1 175 ? 106.621 173.589 131.401 1.00 138.53 ? 191 ALA C CB  1 
ATOM   6604  N  N   . GLN C 1 176 ? 108.503 174.570 129.045 1.00 148.07 ? 192 GLN C N   1 
ATOM   6605  C  CA  . GLN C 1 176 ? 109.095 175.687 128.319 1.00 148.07 ? 192 GLN C CA  1 
ATOM   6606  C  C   . GLN C 1 176 ? 109.014 175.511 126.808 1.00 148.07 ? 192 GLN C C   1 
ATOM   6607  O  O   . GLN C 1 176 ? 109.148 176.497 126.076 1.00 148.07 ? 192 GLN C O   1 
ATOM   6608  C  CB  . GLN C 1 176 ? 110.552 175.875 128.742 1.00 148.07 ? 192 GLN C CB  1 
ATOM   6609  N  N   . LEU C 1 177 ? 108.800 174.287 126.326 1.00 144.74 ? 193 LEU C N   1 
ATOM   6610  C  CA  . LEU C 1 177 ? 108.707 174.013 124.897 1.00 144.74 ? 193 LEU C CA  1 
ATOM   6611  C  C   . LEU C 1 177 ? 107.300 173.606 124.476 1.00 144.74 ? 193 LEU C C   1 
ATOM   6612  O  O   . LEU C 1 177 ? 107.119 173.049 123.388 1.00 144.74 ? 193 LEU C O   1 
ATOM   6613  C  CB  . LEU C 1 177 ? 109.713 172.933 124.499 1.00 144.74 ? 193 LEU C CB  1 
ATOM   6614  N  N   . GLN C 1 178 ? 106.303 173.867 125.316 1.00 137.40 ? 194 GLN C N   1 
ATOM   6615  C  CA  . GLN C 1 178 ? 104.921 173.519 125.007 1.00 137.40 ? 194 GLN C CA  1 
ATOM   6616  C  C   . GLN C 1 178 ? 104.407 174.306 123.805 1.00 137.40 ? 194 GLN C C   1 
ATOM   6617  O  O   . GLN C 1 178 ? 103.942 173.727 122.823 1.00 137.40 ? 194 GLN C O   1 
ATOM   6618  C  CB  . GLN C 1 178 ? 104.022 173.768 126.220 1.00 137.40 ? 194 GLN C CB  1 
ATOM   6619  N  N   . HIS C 1 188 ? 106.151 162.069 116.664 1.00 136.26 ? 204 HIS C N   1 
ATOM   6620  C  CA  . HIS C 1 188 ? 104.932 161.416 117.125 1.00 136.26 ? 204 HIS C CA  1 
ATOM   6621  C  C   . HIS C 1 188 ? 105.273 160.397 118.208 1.00 136.26 ? 204 HIS C C   1 
ATOM   6622  O  O   . HIS C 1 188 ? 104.905 160.569 119.371 1.00 136.26 ? 204 HIS C O   1 
ATOM   6623  C  CB  . HIS C 1 188 ? 104.203 160.744 115.956 1.00 136.26 ? 204 HIS C CB  1 
ATOM   6624  C  CG  . HIS C 1 188 ? 102.811 160.293 116.281 1.00 136.26 ? 204 HIS C CG  1 
ATOM   6625  N  ND1 . HIS C 1 188 ? 102.450 159.808 117.520 1.00 136.26 ? 204 HIS C ND1 1 
ATOM   6626  C  CD2 . HIS C 1 188 ? 101.689 160.259 115.524 1.00 136.26 ? 204 HIS C CD2 1 
ATOM   6627  C  CE1 . HIS C 1 188 ? 101.167 159.493 117.511 1.00 136.26 ? 204 HIS C CE1 1 
ATOM   6628  N  NE2 . HIS C 1 188 ? 100.682 159.757 116.312 1.00 136.26 ? 204 HIS C NE2 1 
ATOM   6629  N  N   . ARG C 1 189 ? 105.970 159.328 117.814 1.00 132.63 ? 205 ARG C N   1 
ATOM   6630  C  CA  . ARG C 1 189 ? 106.417 158.335 118.786 1.00 132.63 ? 205 ARG C CA  1 
ATOM   6631  C  C   . ARG C 1 189 ? 107.347 158.944 119.827 1.00 132.63 ? 205 ARG C C   1 
ATOM   6632  O  O   . ARG C 1 189 ? 107.344 158.519 120.991 1.00 132.63 ? 205 ARG C O   1 
ATOM   6633  C  CB  . ARG C 1 189 ? 107.108 157.174 118.072 1.00 132.63 ? 205 ARG C CB  1 
ATOM   6634  N  N   . LEU C 1 190 ? 108.145 159.940 119.435 1.00 137.51 ? 206 LEU C N   1 
ATOM   6635  C  CA  . LEU C 1 190 ? 109.008 160.613 120.400 1.00 137.51 ? 206 LEU C CA  1 
ATOM   6636  C  C   . LEU C 1 190 ? 108.191 161.307 121.483 1.00 137.51 ? 206 LEU C C   1 
ATOM   6637  O  O   . LEU C 1 190 ? 108.572 161.290 122.658 1.00 137.51 ? 206 LEU C O   1 
ATOM   6638  C  CB  . LEU C 1 190 ? 109.913 161.615 119.684 1.00 137.51 ? 206 LEU C CB  1 
ATOM   6639  N  N   . LEU C 1 191 ? 107.049 161.894 121.111 1.00 127.31 ? 207 LEU C N   1 
ATOM   6640  C  CA  . LEU C 1 191 ? 106.185 162.527 122.104 1.00 127.31 ? 207 LEU C CA  1 
ATOM   6641  C  C   . LEU C 1 191 ? 105.660 161.504 123.100 1.00 127.31 ? 207 LEU C C   1 
ATOM   6642  O  O   . LEU C 1 191 ? 105.604 161.769 124.309 1.00 127.31 ? 207 LEU C O   1 
ATOM   6643  C  CB  . LEU C 1 191 ? 105.029 163.247 121.411 1.00 127.31 ? 207 LEU C CB  1 
ATOM   6644  N  N   . THR C 1 192 ? 105.271 160.327 122.609 1.00 130.88 ? 208 THR C N   1 
ATOM   6645  C  CA  . THR C 1 192 ? 104.818 159.270 123.502 1.00 130.88 ? 208 THR C CA  1 
ATOM   6646  C  C   . THR C 1 192 ? 105.937 158.830 124.433 1.00 130.88 ? 208 THR C C   1 
ATOM   6647  O  O   . THR C 1 192 ? 105.695 158.547 125.610 1.00 130.88 ? 208 THR C O   1 
ATOM   6648  C  CB  . THR C 1 192 ? 104.289 158.080 122.703 1.00 130.88 ? 208 THR C CB  1 
ATOM   6649  O  OG1 . THR C 1 192 ? 105.151 157.828 121.589 1.00 130.88 ? 208 THR C OG1 1 
ATOM   6650  C  CG2 . THR C 1 192 ? 102.885 158.365 122.191 1.00 130.88 ? 208 THR C CG2 1 
ATOM   6651  N  N   . ASP C 1 193 ? 107.168 158.736 123.919 1.00 137.41 ? 209 ASP C N   1 
ATOM   6652  C  CA  . ASP C 1 193 ? 108.291 158.380 124.783 1.00 137.41 ? 209 ASP C CA  1 
ATOM   6653  C  C   . ASP C 1 193 ? 108.523 159.425 125.873 1.00 137.41 ? 209 ASP C C   1 
ATOM   6654  O  O   . ASP C 1 193 ? 108.751 159.072 127.038 1.00 137.41 ? 209 ASP C O   1 
ATOM   6655  C  CB  . ASP C 1 193 ? 109.555 158.193 123.944 1.00 137.41 ? 209 ASP C CB  1 
ATOM   6656  N  N   . ILE C 1 194 ? 108.468 160.714 125.518 1.00 139.01 ? 210 ILE C N   1 
ATOM   6657  C  CA  . ILE C 1 194 ? 108.576 161.767 126.533 1.00 139.01 ? 210 ILE C CA  1 
ATOM   6658  C  C   . ILE C 1 194 ? 107.491 161.606 127.590 1.00 139.01 ? 210 ILE C C   1 
ATOM   6659  O  O   . ILE C 1 194 ? 107.763 161.657 128.796 1.00 139.01 ? 210 ILE C O   1 
ATOM   6660  C  CB  . ILE C 1 194 ? 108.547 163.175 125.907 1.00 139.01 ? 210 ILE C CB  1 
ATOM   6661  C  CG1 . ILE C 1 194 ? 109.471 163.281 124.695 1.00 139.01 ? 210 ILE C CG1 1 
ATOM   6662  C  CG2 . ILE C 1 194 ? 108.920 164.222 126.943 1.00 139.01 ? 210 ILE C CG2 1 
ATOM   6663  C  CD1 . ILE C 1 194 ? 108.952 164.206 123.614 1.00 139.01 ? 210 ILE C CD1 1 
ATOM   6664  N  N   . ILE C 1 195 ? 106.242 161.426 127.154 1.00 143.26 ? 211 ILE C N   1 
ATOM   6665  C  CA  . ILE C 1 195 ? 105.134 161.329 128.102 1.00 143.26 ? 211 ILE C CA  1 
ATOM   6666  C  C   . ILE C 1 195 ? 105.305 160.110 129.002 1.00 143.26 ? 211 ILE C C   1 
ATOM   6667  O  O   . ILE C 1 195 ? 105.072 160.179 130.215 1.00 143.26 ? 211 ILE C O   1 
ATOM   6668  C  CB  . ILE C 1 195 ? 103.790 161.297 127.351 1.00 143.26 ? 211 ILE C CB  1 
ATOM   6669  N  N   . SER C 1 196 ? 105.706 158.976 128.424 1.00 150.54 ? 212 SER C N   1 
ATOM   6670  C  CA  . SER C 1 196 ? 105.856 157.750 129.200 1.00 150.54 ? 212 SER C CA  1 
ATOM   6671  C  C   . SER C 1 196 ? 106.985 157.879 130.214 1.00 150.54 ? 212 SER C C   1 
ATOM   6672  O  O   . SER C 1 196 ? 106.894 157.338 131.323 1.00 150.54 ? 212 SER C O   1 
ATOM   6673  C  CB  . SER C 1 196 ? 106.104 156.565 128.268 1.00 150.54 ? 212 SER C CB  1 
ATOM   6674  O  OG  . SER C 1 196 ? 105.458 156.753 127.021 1.00 150.54 ? 212 SER C OG  1 
ATOM   6675  N  N   . ASP C 1 197 ? 108.064 158.575 129.845 1.00 146.86 ? 213 ASP C N   1 
ATOM   6676  C  CA  . ASP C 1 197 ? 109.193 158.728 130.758 1.00 146.86 ? 213 ASP C CA  1 
ATOM   6677  C  C   . ASP C 1 197 ? 108.775 159.445 132.036 1.00 146.86 ? 213 ASP C C   1 
ATOM   6678  O  O   . ASP C 1 197 ? 109.172 159.050 133.138 1.00 146.86 ? 213 ASP C O   1 
ATOM   6679  C  CB  . ASP C 1 197 ? 110.329 159.480 130.066 1.00 146.86 ? 213 ASP C CB  1 
ATOM   6680  N  N   . GLY C 1 198 ? 107.981 160.498 131.909 1.00 136.61 ? 214 GLY C N   1 
ATOM   6681  C  CA  . GLY C 1 198 ? 107.478 161.245 133.037 1.00 136.61 ? 214 GLY C CA  1 
ATOM   6682  C  C   . GLY C 1 198 ? 107.550 162.729 132.760 1.00 136.61 ? 214 GLY C C   1 
ATOM   6683  O  O   . GLY C 1 198 ? 107.819 163.158 131.639 1.00 136.61 ? 214 GLY C O   1 
ATOM   6684  N  N   . VAL C 1 199 ? 107.343 163.513 133.815 1.00 121.31 ? 215 VAL C N   1 
ATOM   6685  C  CA  . VAL C 1 199 ? 107.398 164.973 133.756 1.00 121.31 ? 215 VAL C CA  1 
ATOM   6686  C  C   . VAL C 1 199 ? 107.749 165.514 135.136 1.00 121.31 ? 215 VAL C C   1 
ATOM   6687  O  O   . VAL C 1 199 ? 108.740 166.223 135.303 1.00 121.31 ? 215 VAL C O   1 
ATOM   6688  C  CB  . VAL C 1 199 ? 106.066 165.593 133.268 1.00 121.31 ? 215 VAL C CB  1 
ATOM   6689  C  CG1 . VAL C 1 199 ? 105.976 167.046 133.705 1.00 121.31 ? 215 VAL C CG1 1 
ATOM   6690  C  CG2 . VAL C 1 199 ? 105.936 165.514 131.756 1.00 121.31 ? 215 VAL C CG2 1 
ATOM   6691  N  N   . GLN C 1 203 ? 105.637 171.856 134.395 1.00 138.05 ? 219 GLN C N   1 
ATOM   6692  C  CA  . GLN C 1 203 ? 105.034 170.589 134.790 1.00 138.05 ? 219 GLN C CA  1 
ATOM   6693  C  C   . GLN C 1 203 ? 103.551 170.554 134.434 1.00 138.05 ? 219 GLN C C   1 
ATOM   6694  O  O   . GLN C 1 203 ? 102.692 170.536 135.316 1.00 138.05 ? 219 GLN C O   1 
ATOM   6695  C  CB  . GLN C 1 203 ? 105.221 170.351 136.290 1.00 138.05 ? 219 GLN C CB  1 
ATOM   6696  N  N   . ASN C 1 204 ? 103.258 170.544 133.136 1.00 142.43 ? 220 ASN C N   1 
ATOM   6697  C  CA  . ASN C 1 204 ? 101.888 170.513 132.625 1.00 142.43 ? 220 ASN C CA  1 
ATOM   6698  C  C   . ASN C 1 204 ? 101.772 169.425 131.563 1.00 142.43 ? 220 ASN C C   1 
ATOM   6699  O  O   . ASN C 1 204 ? 101.686 169.716 130.364 1.00 142.43 ? 220 ASN C O   1 
ATOM   6700  C  CB  . ASN C 1 204 ? 101.481 171.875 132.063 1.00 142.43 ? 220 ASN C CB  1 
ATOM   6701  N  N   . PRO C 1 205 ? 101.779 168.153 131.973 1.00 134.42 ? 221 PRO C N   1 
ATOM   6702  C  CA  . PRO C 1 205 ? 101.663 167.072 130.975 1.00 134.42 ? 221 PRO C CA  1 
ATOM   6703  C  C   . PRO C 1 205 ? 100.355 167.105 130.203 1.00 134.42 ? 221 PRO C C   1 
ATOM   6704  O  O   . PRO C 1 205 ? 100.362 167.021 128.967 1.00 134.42 ? 221 PRO C O   1 
ATOM   6705  C  CB  . PRO C 1 205 ? 101.798 165.798 131.823 1.00 134.42 ? 221 PRO C CB  1 
ATOM   6706  C  CG  . PRO C 1 205 ? 102.420 166.238 133.109 1.00 134.42 ? 221 PRO C CG  1 
ATOM   6707  C  CD  . PRO C 1 205 ? 101.938 167.631 133.340 1.00 134.42 ? 221 PRO C CD  1 
ATOM   6708  N  N   . THR C 1 206 ? 99.223  167.214 130.905 1.00 132.18 ? 222 THR C N   1 
ATOM   6709  C  CA  . THR C 1 206 ? 97.929  167.227 130.230 1.00 132.18 ? 222 THR C CA  1 
ATOM   6710  C  C   . THR C 1 206 ? 97.791  168.440 129.317 1.00 132.18 ? 222 THR C C   1 
ATOM   6711  O  O   . THR C 1 206 ? 97.266  168.330 128.203 1.00 132.18 ? 222 THR C O   1 
ATOM   6712  C  CB  . THR C 1 206 ? 96.798  167.202 131.258 1.00 132.18 ? 222 THR C CB  1 
ATOM   6713  N  N   . GLU C 1 207 ? 98.244  169.608 129.778 1.00 134.80 ? 223 GLU C N   1 
ATOM   6714  C  CA  . GLU C 1 207 ? 98.166  170.808 128.951 1.00 134.80 ? 223 GLU C CA  1 
ATOM   6715  C  C   . GLU C 1 207 ? 98.999  170.661 127.685 1.00 134.80 ? 223 GLU C C   1 
ATOM   6716  O  O   . GLU C 1 207 ? 98.561  171.048 126.595 1.00 134.80 ? 223 GLU C O   1 
ATOM   6717  C  CB  . GLU C 1 207 ? 98.617  172.029 129.754 1.00 134.80 ? 223 GLU C CB  1 
ATOM   6718  N  N   . ALA C 1 208 ? 100.209 170.109 127.810 1.00 133.86 ? 224 ALA C N   1 
ATOM   6719  C  CA  . ALA C 1 208 ? 101.044 169.887 126.634 1.00 133.86 ? 224 ALA C CA  1 
ATOM   6720  C  C   . ALA C 1 208 ? 100.402 168.885 125.684 1.00 133.86 ? 224 ALA C C   1 
ATOM   6721  O  O   . ALA C 1 208 ? 100.452 169.057 124.461 1.00 133.86 ? 224 ALA C O   1 
ATOM   6722  C  CB  . ALA C 1 208 ? 102.434 169.413 127.058 1.00 133.86 ? 224 ALA C CB  1 
ATOM   6723  N  N   . ILE C 1 209 ? 99.805  167.823 126.231 1.00 128.87 ? 225 ILE C N   1 
ATOM   6724  C  CA  . ILE C 1 209 ? 99.135  166.827 125.399 1.00 128.87 ? 225 ILE C CA  1 
ATOM   6725  C  C   . ILE C 1 209 ? 97.992  167.466 124.621 1.00 128.87 ? 225 ILE C C   1 
ATOM   6726  O  O   . ILE C 1 209 ? 97.820  167.225 123.420 1.00 128.87 ? 225 ILE C O   1 
ATOM   6727  C  CB  . ILE C 1 209 ? 98.643  165.650 126.260 1.00 128.87 ? 225 ILE C CB  1 
ATOM   6728  N  N   . GLU C 1 210 ? 97.185  168.285 125.301 1.00 134.08 ? 226 GLU C N   1 
ATOM   6729  C  CA  . GLU C 1 210 ? 96.102  168.990 124.622 1.00 134.08 ? 226 GLU C CA  1 
ATOM   6730  C  C   . GLU C 1 210 ? 96.641  169.953 123.571 1.00 134.08 ? 226 GLU C C   1 
ATOM   6731  O  O   . GLU C 1 210 ? 96.081  170.063 122.474 1.00 134.08 ? 226 GLU C O   1 
ATOM   6732  C  CB  . GLU C 1 210 ? 95.241  169.735 125.642 1.00 134.08 ? 226 GLU C CB  1 
ATOM   6733  N  N   . ALA C 1 211 ? 97.721  170.659 123.889 1.00 142.10 ? 227 ALA C N   1 
ATOM   6734  C  CA  . ALA C 1 211 ? 98.327  171.601 122.954 1.00 142.10 ? 227 ALA C CA  1 
ATOM   6735  C  C   . ALA C 1 211 ? 98.960  170.871 121.773 1.00 142.10 ? 227 ALA C C   1 
ATOM   6736  O  O   . ALA C 1 211 ? 98.308  170.632 120.756 1.00 142.10 ? 227 ALA C O   1 
ATOM   6737  C  CB  . ALA C 1 211 ? 99.362  172.459 123.663 1.00 142.10 ? 227 ALA C CB  1 
ATOM   6738  N  N   . LEU C 1 227 ? 97.241  156.829 124.549 1.00 150.29 ? 243 LEU C N   1 
ATOM   6739  C  CA  . LEU C 1 227 ? 97.159  158.285 124.574 1.00 150.29 ? 243 LEU C CA  1 
ATOM   6740  C  C   . LEU C 1 227 ? 97.148  158.807 126.006 1.00 150.29 ? 243 LEU C C   1 
ATOM   6741  O  O   . LEU C 1 227 ? 98.194  159.147 126.560 1.00 150.29 ? 243 LEU C O   1 
ATOM   6742  C  CB  . LEU C 1 227 ? 95.913  158.765 123.828 1.00 150.29 ? 243 LEU C CB  1 
ATOM   6743  N  N   . ARG C 1 228 ? 95.952  158.877 126.597 1.00 147.61 ? 244 ARG C N   1 
ATOM   6744  C  CA  . ARG C 1 228 ? 95.831  159.356 127.970 1.00 147.61 ? 244 ARG C CA  1 
ATOM   6745  C  C   . ARG C 1 228 ? 96.560  158.439 128.944 1.00 147.61 ? 244 ARG C C   1 
ATOM   6746  O  O   . ARG C 1 228 ? 97.228  158.912 129.872 1.00 147.61 ? 244 ARG C O   1 
ATOM   6747  C  CB  . ARG C 1 228 ? 94.357  159.483 128.352 1.00 147.61 ? 244 ARG C CB  1 
ATOM   6748  N  N   . THR C 1 229 ? 96.442  157.123 128.753 1.00 160.49 ? 245 THR C N   1 
ATOM   6749  C  CA  . THR C 1 229 ? 97.109  156.178 129.641 1.00 160.49 ? 245 THR C CA  1 
ATOM   6750  C  C   . THR C 1 229 ? 98.624  156.214 129.496 1.00 160.49 ? 245 THR C C   1 
ATOM   6751  O  O   . THR C 1 229 ? 99.332  155.778 130.410 1.00 160.49 ? 245 THR C O   1 
ATOM   6752  C  CB  . THR C 1 229 ? 96.601  154.759 129.381 1.00 160.49 ? 245 THR C CB  1 
ATOM   6753  N  N   . SER C 1 230 ? 99.136  156.722 128.376 1.00 163.45 ? 246 SER C N   1 
ATOM   6754  C  CA  . SER C 1 230 ? 100.578 156.825 128.154 1.00 163.45 ? 246 SER C CA  1 
ATOM   6755  C  C   . SER C 1 230 ? 101.117 158.122 128.760 1.00 163.45 ? 246 SER C C   1 
ATOM   6756  O  O   . SER C 1 230 ? 101.704 158.968 128.087 1.00 163.45 ? 246 SER C O   1 
ATOM   6757  C  CB  . SER C 1 230 ? 100.891 156.732 126.665 1.00 163.45 ? 246 SER C CB  1 
ATOM   6758  N  N   . LEU C 1 231 ? 100.899 158.265 130.065 1.00 153.46 ? 247 LEU C N   1 
ATOM   6759  C  CA  . LEU C 1 231 ? 101.327 159.451 130.790 1.00 153.46 ? 247 LEU C CA  1 
ATOM   6760  C  C   . LEU C 1 231 ? 101.724 159.051 132.203 1.00 153.46 ? 247 LEU C C   1 
ATOM   6761  O  O   . LEU C 1 231 ? 101.229 158.060 132.745 1.00 153.46 ? 247 LEU C O   1 
ATOM   6762  C  CB  . LEU C 1 231 ? 100.223 160.516 130.820 1.00 153.46 ? 247 LEU C CB  1 
ATOM   6763  C  CG  . LEU C 1 231 ? 100.637 161.969 131.065 1.00 153.46 ? 247 LEU C CG  1 
ATOM   6764  C  CD1 . LEU C 1 231 ? 99.799  162.907 130.212 1.00 153.46 ? 247 LEU C CD1 1 
ATOM   6765  C  CD2 . LEU C 1 231 ? 100.505 162.330 132.536 1.00 153.46 ? 247 LEU C CD2 1 
ATOM   6766  N  N   . LYS C 1 232 ? 102.627 159.832 132.792 1.00 171.13 ? 248 LYS C N   1 
ATOM   6767  C  CA  . LYS C 1 232 ? 103.091 159.575 134.146 1.00 171.13 ? 248 LYS C CA  1 
ATOM   6768  C  C   . LYS C 1 232 ? 103.458 160.897 134.802 1.00 171.13 ? 248 LYS C C   1 
ATOM   6769  O  O   . LYS C 1 232 ? 103.651 161.914 134.132 1.00 171.13 ? 248 LYS C O   1 
ATOM   6770  C  CB  . LYS C 1 232 ? 104.289 158.617 134.159 1.00 171.13 ? 248 LYS C CB  1 
ATOM   6771  N  N   . GLU C 1 233 ? 103.551 160.868 136.129 1.00 163.79 ? 249 GLU C N   1 
ATOM   6772  C  CA  . GLU C 1 233 ? 103.871 162.060 136.899 1.00 163.79 ? 249 GLU C CA  1 
ATOM   6773  C  C   . GLU C 1 233 ? 104.714 161.667 138.102 1.00 163.79 ? 249 GLU C C   1 
ATOM   6774  O  O   . GLU C 1 233 ? 104.552 160.581 138.665 1.00 163.79 ? 249 GLU C O   1 
ATOM   6775  C  CB  . GLU C 1 233 ? 102.605 162.794 137.355 1.00 163.79 ? 249 GLU C CB  1 
ATOM   6776  N  N   . ILE C 1 234 ? 105.618 162.564 138.488 1.00 150.74 ? 250 ILE C N   1 
ATOM   6777  C  CA  . ILE C 1 234 ? 106.483 162.348 139.642 1.00 150.74 ? 250 ILE C CA  1 
ATOM   6778  C  C   . ILE C 1 234 ? 106.383 163.556 140.563 1.00 150.74 ? 250 ILE C C   1 
ATOM   6779  O  O   . ILE C 1 234 ? 107.297 163.828 141.350 1.00 150.74 ? 250 ILE C O   1 
ATOM   6780  C  CB  . ILE C 1 234 ? 107.940 162.096 139.213 1.00 150.74 ? 250 ILE C CB  1 
ATOM   6781  N  N   . GLY C 1 235 ? 105.270 164.274 140.479 1.00 155.55 ? 251 GLY C N   1 
ATOM   6782  C  CA  . GLY C 1 235 ? 105.089 165.459 141.300 1.00 155.55 ? 251 GLY C CA  1 
ATOM   6783  C  C   . GLY C 1 235 ? 106.133 166.505 140.962 1.00 155.55 ? 251 GLY C C   1 
ATOM   6784  O  O   . GLY C 1 235 ? 106.243 166.961 139.817 1.00 155.55 ? 251 GLY C O   1 
ATOM   6785  N  N   . GLU C 1 236 ? 106.919 166.897 141.964 1.00 145.16 ? 252 GLU C N   1 
ATOM   6786  C  CA  . GLU C 1 236 ? 107.986 167.886 141.788 1.00 145.16 ? 252 GLU C CA  1 
ATOM   6787  C  C   . GLU C 1 236 ? 109.213 167.361 142.530 1.00 145.16 ? 252 GLU C C   1 
ATOM   6788  O  O   . GLU C 1 236 ? 109.396 167.627 143.721 1.00 145.16 ? 252 GLU C O   1 
ATOM   6789  C  CB  . GLU C 1 236 ? 107.561 169.259 142.290 1.00 145.16 ? 252 GLU C CB  1 
ATOM   6790  N  N   . ASN C 1 237 ? 110.049 166.614 141.816 1.00 140.74 ? 253 ASN C N   1 
ATOM   6791  C  CA  . ASN C 1 237 ? 111.293 166.125 142.391 1.00 140.74 ? 253 ASN C CA  1 
ATOM   6792  C  C   . ASN C 1 237 ? 112.271 167.274 142.597 1.00 140.74 ? 253 ASN C C   1 
ATOM   6793  O  O   . ASN C 1 237 ? 112.369 168.185 141.770 1.00 140.74 ? 253 ASN C O   1 
ATOM   6794  C  CB  . ASN C 1 237 ? 111.914 165.059 141.490 1.00 140.74 ? 253 ASN C CB  1 
ATOM   6795  N  N   . VAL C 1 238 ? 112.998 167.227 143.712 1.00 126.61 ? 254 VAL C N   1 
ATOM   6796  C  CA  . VAL C 1 238 ? 113.950 168.282 144.034 1.00 126.61 ? 254 VAL C CA  1 
ATOM   6797  C  C   . VAL C 1 238 ? 115.124 168.212 143.068 1.00 126.61 ? 254 VAL C C   1 
ATOM   6798  O  O   . VAL C 1 238 ? 115.755 167.159 142.903 1.00 126.61 ? 254 VAL C O   1 
ATOM   6799  C  CB  . VAL C 1 238 ? 114.412 168.160 145.493 1.00 126.61 ? 254 VAL C CB  1 
ATOM   6800  C  CG1 . VAL C 1 238 ? 115.310 169.322 145.865 1.00 126.61 ? 254 VAL C CG1 1 
ATOM   6801  C  CG2 . VAL C 1 238 ? 113.208 168.103 146.418 1.00 126.61 ? 254 VAL C CG2 1 
ATOM   6802  N  N   . HIS C 1 239 ? 115.420 169.338 142.417 1.00 113.73 ? 255 HIS C N   1 
ATOM   6803  C  CA  . HIS C 1 239 ? 116.510 169.361 141.447 1.00 113.73 ? 255 HIS C CA  1 
ATOM   6804  C  C   . HIS C 1 239 ? 117.870 169.305 142.131 1.00 113.73 ? 255 HIS C C   1 
ATOM   6805  O  O   . HIS C 1 239 ? 118.750 168.546 141.709 1.00 113.73 ? 255 HIS C O   1 
ATOM   6806  C  CB  . HIS C 1 239 ? 116.401 170.607 140.570 1.00 113.73 ? 255 HIS C CB  1 
ATOM   6807  N  N   . ILE C 1 240 ? 118.061 170.090 143.188 1.00 108.10 ? 256 ILE C N   1 
ATOM   6808  C  CA  . ILE C 1 240 ? 119.351 170.183 143.864 1.00 108.10 ? 256 ILE C CA  1 
ATOM   6809  C  C   . ILE C 1 240 ? 119.101 170.377 145.352 1.00 108.10 ? 256 ILE C C   1 
ATOM   6810  O  O   . ILE C 1 240 ? 118.199 171.118 145.750 1.00 108.10 ? 256 ILE C O   1 
ATOM   6811  C  CB  . ILE C 1 240 ? 120.201 171.339 143.285 1.00 108.10 ? 256 ILE C CB  1 
ATOM   6812  C  CG1 . ILE C 1 240 ? 120.781 170.969 141.918 1.00 108.10 ? 256 ILE C CG1 1 
ATOM   6813  C  CG2 . ILE C 1 240 ? 121.320 171.736 144.237 1.00 108.10 ? 256 ILE C CG2 1 
ATOM   6814  C  CD1 . ILE C 1 240 ? 121.349 172.148 141.155 1.00 108.10 ? 256 ILE C CD1 1 
ATOM   6815  N  N   . TYR C 1 241 ? 119.903 169.712 146.175 1.00 110.92 ? 257 TYR C N   1 
ATOM   6816  C  CA  . TYR C 1 241 ? 119.882 169.912 147.615 1.00 110.92 ? 257 TYR C CA  1 
ATOM   6817  C  C   . TYR C 1 241 ? 121.134 170.659 148.048 1.00 110.92 ? 257 TYR C C   1 
ATOM   6818  O  O   . TYR C 1 241 ? 122.101 170.794 147.293 1.00 110.92 ? 257 TYR C O   1 
ATOM   6819  C  CB  . TYR C 1 241 ? 119.796 168.576 148.361 1.00 110.92 ? 257 TYR C CB  1 
ATOM   6820  C  CG  . TYR C 1 241 ? 118.470 167.860 148.256 1.00 110.92 ? 257 TYR C CG  1 
ATOM   6821  C  CD1 . TYR C 1 241 ? 118.192 167.017 147.190 1.00 110.92 ? 257 TYR C CD1 1 
ATOM   6822  C  CD2 . TYR C 1 241 ? 117.505 168.007 149.243 1.00 110.92 ? 257 TYR C CD2 1 
ATOM   6823  C  CE1 . TYR C 1 241 ? 116.985 166.351 147.104 1.00 110.92 ? 257 TYR C CE1 1 
ATOM   6824  C  CE2 . TYR C 1 241 ? 116.296 167.350 149.164 1.00 110.92 ? 257 TYR C CE2 1 
ATOM   6825  C  CZ  . TYR C 1 241 ? 116.041 166.523 148.094 1.00 110.92 ? 257 TYR C CZ  1 
ATOM   6826  O  OH  . TYR C 1 241 ? 114.833 165.870 148.013 1.00 110.92 ? 257 TYR C OH  1 
ATOM   6827  N  N   . LEU C 1 242 ? 121.113 171.143 149.288 1.00 102.99 ? 258 LEU C N   1 
ATOM   6828  C  CA  . LEU C 1 242 ? 122.263 171.860 149.820 1.00 102.99 ? 258 LEU C CA  1 
ATOM   6829  C  C   . LEU C 1 242 ? 122.156 171.939 151.332 1.00 102.99 ? 258 LEU C C   1 
ATOM   6830  O  O   . LEU C 1 242 ? 121.126 172.365 151.861 1.00 102.99 ? 258 LEU C O   1 
ATOM   6831  C  CB  . LEU C 1 242 ? 122.358 173.271 149.226 1.00 102.99 ? 258 LEU C CB  1 
ATOM   6832  N  N   . ILE C 1 243 ? 123.221 171.540 152.018 1.00 97.91  ? 259 ILE C N   1 
ATOM   6833  C  CA  . ILE C 1 243 ? 123.296 171.618 153.470 1.00 97.91  ? 259 ILE C CA  1 
ATOM   6834  C  C   . ILE C 1 243 ? 124.058 172.883 153.825 1.00 97.91  ? 259 ILE C C   1 
ATOM   6835  O  O   . ILE C 1 243 ? 125.170 173.108 153.324 1.00 97.91  ? 259 ILE C O   1 
ATOM   6836  C  CB  . ILE C 1 243 ? 123.964 170.373 154.080 1.00 97.91  ? 259 ILE C CB  1 
ATOM   6837  C  CG1 . ILE C 1 243 ? 123.025 169.163 154.039 1.00 97.91  ? 259 ILE C CG1 1 
ATOM   6838  C  CG2 . ILE C 1 243 ? 124.404 170.652 155.510 1.00 97.91  ? 259 ILE C CG2 1 
ATOM   6839  C  CD1 . ILE C 1 243 ? 122.852 168.532 152.683 1.00 97.91  ? 259 ILE C CD1 1 
ATOM   6840  N  N   . GLY C 1 244 ? 123.474 173.684 154.711 1.00 124.07 ? 260 GLY C N   1 
ATOM   6841  C  CA  . GLY C 1 244 ? 124.045 174.934 155.165 1.00 124.07 ? 260 GLY C CA  1 
ATOM   6842  C  C   . GLY C 1 244 ? 124.016 175.075 156.671 1.00 124.07 ? 260 GLY C C   1 
ATOM   6843  O  O   . GLY C 1 244 ? 123.871 174.087 157.396 1.00 124.07 ? 260 GLY C O   1 
ATOM   6844  N  N   . LYS C 1 245 ? 124.120 176.312 157.145 1.00 138.38 ? 261 LYS C N   1 
ATOM   6845  C  CA  . LYS C 1 245 ? 124.066 176.638 158.567 1.00 138.38 ? 261 LYS C CA  1 
ATOM   6846  C  C   . LYS C 1 245 ? 123.439 178.017 158.723 1.00 138.38 ? 261 LYS C C   1 
ATOM   6847  O  O   . LYS C 1 245 ? 122.577 178.408 157.932 1.00 138.38 ? 261 LYS C O   1 
ATOM   6848  C  CB  . LYS C 1 245 ? 125.461 176.637 159.214 1.00 138.38 ? 261 LYS C CB  1 
ATOM   6849  C  CG  . LYS C 1 245 ? 126.340 175.390 159.021 1.00 138.38 ? 261 LYS C CG  1 
ATOM   6850  C  CD  . LYS C 1 245 ? 125.856 174.173 159.815 1.00 138.38 ? 261 LYS C CD  1 
ATOM   6851  C  CE  . LYS C 1 245 ? 125.668 174.452 161.309 1.00 138.38 ? 261 LYS C CE  1 
ATOM   6852  N  NZ  . LYS C 1 245 ? 126.527 175.538 161.870 1.00 138.38 ? 261 LYS C NZ  1 
ATOM   6853  N  N   . SER C 1 252 ? 122.249 174.133 160.551 1.00 131.68 ? 268 SER C N   1 
ATOM   6854  C  CA  . SER C 1 252 ? 122.499 172.738 160.209 1.00 131.68 ? 268 SER C CA  1 
ATOM   6855  C  C   . SER C 1 252 ? 121.440 172.212 159.246 1.00 131.68 ? 268 SER C C   1 
ATOM   6856  O  O   . SER C 1 252 ? 121.604 171.149 158.651 1.00 131.68 ? 268 SER C O   1 
ATOM   6857  C  CB  . SER C 1 252 ? 122.539 171.877 161.473 1.00 131.68 ? 268 SER C CB  1 
ATOM   6858  O  OG  . SER C 1 252 ? 121.288 171.891 162.139 1.00 131.68 ? 268 SER C OG  1 
ATOM   6859  N  N   . LEU C 1 253 ? 120.357 172.969 159.102 1.00 122.40 ? 269 LEU C N   1 
ATOM   6860  C  CA  . LEU C 1 253 ? 119.233 172.547 158.278 1.00 122.40 ? 269 LEU C CA  1 
ATOM   6861  C  C   . LEU C 1 253 ? 119.624 172.466 156.805 1.00 122.40 ? 269 LEU C C   1 
ATOM   6862  O  O   . LEU C 1 253 ? 120.452 173.236 156.311 1.00 122.40 ? 269 LEU C O   1 
ATOM   6863  C  CB  . LEU C 1 253 ? 118.052 173.501 158.474 1.00 122.40 ? 269 LEU C CB  1 
ATOM   6864  C  CG  . LEU C 1 253 ? 118.120 174.911 157.882 1.00 122.40 ? 269 LEU C CG  1 
ATOM   6865  C  CD1 . LEU C 1 253 ? 117.411 174.983 156.540 1.00 122.40 ? 269 LEU C CD1 1 
ATOM   6866  C  CD2 . LEU C 1 253 ? 117.537 175.924 158.855 1.00 122.40 ? 269 LEU C CD2 1 
ATOM   6867  N  N   . ALA C 1 254 ? 119.015 171.512 156.104 1.00 108.31 ? 270 ALA C N   1 
ATOM   6868  C  CA  . ALA C 1 254 ? 119.252 171.288 154.683 1.00 108.31 ? 270 ALA C CA  1 
ATOM   6869  C  C   . ALA C 1 254 ? 118.080 171.831 153.878 1.00 108.31 ? 270 ALA C C   1 
ATOM   6870  O  O   . ALA C 1 254 ? 116.924 171.489 154.150 1.00 108.31 ? 270 ALA C O   1 
ATOM   6871  C  CB  . ALA C 1 254 ? 119.449 169.800 154.390 1.00 108.31 ? 270 ALA C CB  1 
ATOM   6872  N  N   . VAL C 1 255 ? 118.378 172.673 152.890 1.00 110.95 ? 271 VAL C N   1 
ATOM   6873  C  CA  . VAL C 1 255 ? 117.359 173.311 152.063 1.00 110.95 ? 271 VAL C CA  1 
ATOM   6874  C  C   . VAL C 1 255 ? 117.223 172.550 150.752 1.00 110.95 ? 271 VAL C C   1 
ATOM   6875  O  O   . VAL C 1 255 ? 118.221 172.282 150.072 1.00 110.95 ? 271 VAL C O   1 
ATOM   6876  C  CB  . VAL C 1 255 ? 117.707 174.785 151.799 1.00 110.95 ? 271 VAL C CB  1 
ATOM   6877  C  CG1 . VAL C 1 255 ? 116.490 175.527 151.287 1.00 110.95 ? 271 VAL C CG1 1 
ATOM   6878  C  CG2 . VAL C 1 255 ? 118.253 175.438 153.058 1.00 110.95 ? 271 VAL C CG2 1 
ATOM   6879  N  N   . SER C 1 256 ? 115.985 172.196 150.401 1.00 122.66 ? 272 SER C N   1 
ATOM   6880  C  CA  . SER C 1 256 ? 115.692 171.483 149.156 1.00 122.66 ? 272 SER C CA  1 
ATOM   6881  C  C   . SER C 1 256 ? 115.420 172.494 148.042 1.00 122.66 ? 272 SER C C   1 
ATOM   6882  O  O   . SER C 1 256 ? 114.276 172.802 147.702 1.00 122.66 ? 272 SER C O   1 
ATOM   6883  C  CB  . SER C 1 256 ? 114.519 170.530 149.352 1.00 122.66 ? 272 SER C CB  1 
ATOM   6884  O  OG  . SER C 1 256 ? 113.316 171.093 148.860 1.00 122.66 ? 272 SER C OG  1 
ATOM   6885  N  N   . LEU C 1 257 ? 116.501 173.023 147.473 1.00 124.15 ? 273 LEU C N   1 
ATOM   6886  C  CA  . LEU C 1 257 ? 116.382 173.999 146.394 1.00 124.15 ? 273 LEU C CA  1 
ATOM   6887  C  C   . LEU C 1 257 ? 115.685 173.389 145.182 1.00 124.15 ? 273 LEU C C   1 
ATOM   6888  O  O   . LEU C 1 257 ? 115.928 172.236 144.819 1.00 124.15 ? 273 LEU C O   1 
ATOM   6889  C  CB  . LEU C 1 257 ? 117.760 174.534 146.000 1.00 124.15 ? 273 LEU C CB  1 
ATOM   6890  C  CG  . LEU C 1 257 ? 118.473 175.448 147.003 1.00 124.15 ? 273 LEU C CG  1 
ATOM   6891  C  CD1 . LEU C 1 257 ? 117.483 176.399 147.656 1.00 124.15 ? 273 LEU C CD1 1 
ATOM   6892  C  CD2 . LEU C 1 257 ? 119.226 174.650 148.053 1.00 124.15 ? 273 LEU C CD2 1 
ATOM   6893  N  N   . HIS C 1 258 ? 114.816 174.172 144.547 1.00 144.41 ? 274 HIS C N   1 
ATOM   6894  C  CA  . HIS C 1 258 ? 114.035 173.722 143.403 1.00 144.41 ? 274 HIS C CA  1 
ATOM   6895  C  C   . HIS C 1 258 ? 114.330 174.614 142.205 1.00 144.41 ? 274 HIS C C   1 
ATOM   6896  O  O   . HIS C 1 258 ? 114.315 175.843 142.321 1.00 144.41 ? 274 HIS C O   1 
ATOM   6897  C  CB  . HIS C 1 258 ? 112.537 173.732 143.720 1.00 144.41 ? 274 HIS C CB  1 
ATOM   6898  C  CG  . HIS C 1 258 ? 111.788 172.579 143.128 1.00 144.41 ? 274 HIS C CG  1 
ATOM   6899  N  ND1 . HIS C 1 258 ? 111.370 171.500 143.876 1.00 144.41 ? 274 HIS C ND1 1 
ATOM   6900  C  CD2 . HIS C 1 258 ? 111.384 172.336 141.858 1.00 144.41 ? 274 HIS C CD2 1 
ATOM   6901  C  CE1 . HIS C 1 258 ? 110.739 170.642 143.094 1.00 144.41 ? 274 HIS C CE1 1 
ATOM   6902  N  NE2 . HIS C 1 258 ? 110.734 171.125 141.865 1.00 144.41 ? 274 HIS C NE2 1 
ATOM   6903  N  N   . CYS C 1 259 ? 114.608 174.004 141.059 1.00 168.56 ? 275 CYS C N   1 
ATOM   6904  C  CA  . CYS C 1 259 ? 114.928 174.758 139.856 1.00 168.56 ? 275 CYS C CA  1 
ATOM   6905  C  C   . CYS C 1 259 ? 113.695 174.851 138.969 1.00 168.56 ? 275 CYS C C   1 
ATOM   6906  O  O   . CYS C 1 259 ? 113.092 173.830 138.622 1.00 168.56 ? 275 CYS C O   1 
ATOM   6907  C  CB  . CYS C 1 259 ? 116.081 174.105 139.093 1.00 168.56 ? 275 CYS C CB  1 
ATOM   6908  N  N   . ALA C 1 260 ? 113.327 176.079 138.610 1.00 175.66 ? 276 ALA C N   1 
ATOM   6909  C  CA  . ALA C 1 260 ? 112.184 176.359 137.752 1.00 175.66 ? 276 ALA C CA  1 
ATOM   6910  C  C   . ALA C 1 260 ? 112.640 177.181 136.556 1.00 175.66 ? 276 ALA C C   1 
ATOM   6911  O  O   . ALA C 1 260 ? 113.342 178.184 136.721 1.00 175.66 ? 276 ALA C O   1 
ATOM   6912  C  CB  . ALA C 1 260 ? 111.086 177.100 138.519 1.00 175.66 ? 276 ALA C CB  1 
ATOM   6913  N  N   . GLU C 1 261 ? 112.243 176.759 135.361 1.00 178.65 ? 277 GLU C N   1 
ATOM   6914  C  CA  . GLU C 1 261 ? 112.623 177.462 134.141 1.00 178.65 ? 277 GLU C CA  1 
ATOM   6915  C  C   . GLU C 1 261 ? 111.545 178.460 133.729 1.00 178.65 ? 277 GLU C C   1 
ATOM   6916  O  O   . GLU C 1 261 ? 111.834 179.628 133.466 1.00 178.65 ? 277 GLU C O   1 
ATOM   6917  C  CB  . GLU C 1 261 ? 112.883 176.470 133.007 1.00 178.65 ? 277 GLU C CB  1 
ATOM   6918  N  N   . SER C 1 264 ? 116.349 180.568 136.921 1.00 157.88 ? 280 SER C N   1 
ATOM   6919  C  CA  . SER C 1 264 ? 116.034 181.078 138.250 1.00 157.88 ? 280 SER C CA  1 
ATOM   6920  C  C   . SER C 1 264 ? 116.038 179.957 139.285 1.00 157.88 ? 280 SER C C   1 
ATOM   6921  O  O   . SER C 1 264 ? 116.138 178.780 138.938 1.00 157.88 ? 280 SER C O   1 
ATOM   6922  C  CB  . SER C 1 264 ? 114.677 181.786 138.244 1.00 157.88 ? 280 SER C CB  1 
ATOM   6923  O  OG  . SER C 1 264 ? 113.680 180.972 137.652 1.00 157.88 ? 280 SER C OG  1 
ATOM   6924  N  N   . ILE C 1 265 ? 115.927 180.331 140.558 1.00 156.76 ? 281 ILE C N   1 
ATOM   6925  C  CA  . ILE C 1 265 ? 115.972 179.385 141.663 1.00 156.76 ? 281 ILE C CA  1 
ATOM   6926  C  C   . ILE C 1 265 ? 114.755 179.622 142.548 1.00 156.76 ? 281 ILE C C   1 
ATOM   6927  O  O   . ILE C 1 265 ? 114.214 180.730 142.608 1.00 156.76 ? 281 ILE C O   1 
ATOM   6928  C  CB  . ILE C 1 265 ? 117.290 179.519 142.465 1.00 156.76 ? 281 ILE C CB  1 
ATOM   6929  C  CG1 . ILE C 1 265 ? 117.414 178.421 143.525 1.00 156.76 ? 281 ILE C CG1 1 
ATOM   6930  C  CG2 . ILE C 1 265 ? 117.395 180.898 143.099 1.00 156.76 ? 281 ILE C CG2 1 
ATOM   6931  C  CD1 . ILE C 1 265 ? 118.731 178.438 144.269 1.00 156.76 ? 281 ILE C CD1 1 
ATOM   6932  N  N   . SER C 1 266 ? 114.319 178.566 143.232 1.00 149.93 ? 282 SER C N   1 
ATOM   6933  C  CA  . SER C 1 266 ? 113.195 178.622 144.150 1.00 149.93 ? 282 SER C CA  1 
ATOM   6934  C  C   . SER C 1 266 ? 113.547 177.830 145.400 1.00 149.93 ? 282 SER C C   1 
ATOM   6935  O  O   . SER C 1 266 ? 114.396 176.935 145.375 1.00 149.93 ? 282 SER C O   1 
ATOM   6936  C  CB  . SER C 1 266 ? 111.912 178.075 143.510 1.00 149.93 ? 282 SER C CB  1 
ATOM   6937  O  OG  . SER C 1 266 ? 111.683 178.667 142.243 1.00 149.93 ? 282 SER C OG  1 
ATOM   6938  N  N   . VAL C 1 267 ? 112.857 178.142 146.486 1.00 139.40 ? 283 VAL C N   1 
ATOM   6939  C  CA  . VAL C 1 267 ? 113.071 177.479 147.768 1.00 139.40 ? 283 VAL C CA  1 
ATOM   6940  C  C   . VAL C 1 267 ? 111.724 176.906 148.187 1.00 139.40 ? 283 VAL C C   1 
ATOM   6941  O  O   . VAL C 1 267 ? 110.905 177.572 148.828 1.00 139.40 ? 283 VAL C O   1 
ATOM   6942  C  CB  . VAL C 1 267 ? 113.630 178.430 148.830 1.00 139.40 ? 283 VAL C CB  1 
ATOM   6943  C  CG1 . VAL C 1 267 ? 113.933 177.676 150.110 1.00 139.40 ? 283 VAL C CG1 1 
ATOM   6944  C  CG2 . VAL C 1 267 ? 114.877 179.131 148.312 1.00 139.40 ? 283 VAL C CG2 1 
ATOM   6945  N  N   . SER C 1 268 ? 111.489 175.650 147.815 1.00 138.31 ? 284 SER C N   1 
ATOM   6946  C  CA  . SER C 1 268 ? 110.294 174.901 148.194 1.00 138.31 ? 284 SER C CA  1 
ATOM   6947  C  C   . SER C 1 268 ? 110.755 173.656 148.943 1.00 138.31 ? 284 SER C C   1 
ATOM   6948  O  O   . SER C 1 268 ? 111.188 172.677 148.326 1.00 138.31 ? 284 SER C O   1 
ATOM   6949  C  CB  . SER C 1 268 ? 109.462 174.540 146.967 1.00 138.31 ? 284 SER C CB  1 
ATOM   6950  O  OG  . SER C 1 268 ? 110.197 173.711 146.084 1.00 138.31 ? 284 SER C OG  1 
ATOM   6951  N  N   . GLY C 1 269 ? 110.670 173.695 150.268 1.00 129.66 ? 285 GLY C N   1 
ATOM   6952  C  CA  . GLY C 1 269 ? 111.125 172.589 151.084 1.00 129.66 ? 285 GLY C CA  1 
ATOM   6953  C  C   . GLY C 1 269 ? 112.194 172.987 152.079 1.00 129.66 ? 285 GLY C C   1 
ATOM   6954  O  O   . GLY C 1 269 ? 113.112 173.743 151.746 1.00 129.66 ? 285 GLY C O   1 
ATOM   6955  N  N   . GLN C 1 270 ? 112.086 172.480 153.304 1.00 131.77 ? 286 GLN C N   1 
ATOM   6956  C  CA  . GLN C 1 270 ? 113.040 172.803 154.354 1.00 131.77 ? 286 GLN C CA  1 
ATOM   6957  C  C   . GLN C 1 270 ? 112.881 171.800 155.486 1.00 131.77 ? 286 GLN C C   1 
ATOM   6958  O  O   . GLN C 1 270 ? 111.758 171.438 155.844 1.00 131.77 ? 286 GLN C O   1 
ATOM   6959  C  CB  . GLN C 1 270 ? 112.841 174.232 154.871 1.00 131.77 ? 286 GLN C CB  1 
ATOM   6960  C  CG  . GLN C 1 270 ? 113.847 174.653 155.926 1.00 131.77 ? 286 GLN C CG  1 
ATOM   6961  C  CD  . GLN C 1 270 ? 113.603 176.058 156.435 1.00 131.77 ? 286 GLN C CD  1 
ATOM   6962  O  OE1 . GLN C 1 270 ? 112.801 176.804 155.872 1.00 131.77 ? 286 GLN C OE1 1 
ATOM   6963  N  NE2 . GLN C 1 270 ? 114.296 176.428 157.505 1.00 131.77 ? 286 GLN C NE2 1 
ATOM   6964  N  N   . ASN C 1 271 ? 114.007 171.357 156.040 1.00 117.50 ? 287 ASN C N   1 
ATOM   6965  C  CA  . ASN C 1 271 ? 113.989 170.381 157.121 1.00 117.50 ? 287 ASN C CA  1 
ATOM   6966  C  C   . ASN C 1 271 ? 115.298 170.481 157.885 1.00 117.50 ? 287 ASN C C   1 
ATOM   6967  O  O   . ASN C 1 271 ? 116.371 170.501 157.274 1.00 117.50 ? 287 ASN C O   1 
ATOM   6968  C  CB  . ASN C 1 271 ? 113.787 168.960 156.582 1.00 117.50 ? 287 ASN C CB  1 
ATOM   6969  N  N   . SER C 1 272 ? 115.209 170.544 159.208 1.00 121.90 ? 288 SER C N   1 
ATOM   6970  C  CA  . SER C 1 272 ? 116.394 170.651 160.041 1.00 121.90 ? 288 SER C CA  1 
ATOM   6971  C  C   . SER C 1 272 ? 116.890 169.270 160.453 1.00 121.90 ? 288 SER C C   1 
ATOM   6972  O  O   . SER C 1 272 ? 116.149 168.285 160.451 1.00 121.90 ? 288 SER C O   1 
ATOM   6973  C  CB  . SER C 1 272 ? 116.106 171.495 161.283 1.00 121.90 ? 288 SER C CB  1 
ATOM   6974  O  OG  . SER C 1 272 ? 117.182 171.431 162.203 1.00 121.90 ? 288 SER C OG  1 
ATOM   6975  N  N   . LEU C 1 273 ? 118.169 169.212 160.811 1.00 127.19 ? 289 LEU C N   1 
ATOM   6976  C  CA  . LEU C 1 273 ? 118.798 167.994 161.295 1.00 127.19 ? 289 LEU C CA  1 
ATOM   6977  C  C   . LEU C 1 273 ? 119.468 168.277 162.630 1.00 127.19 ? 289 LEU C C   1 
ATOM   6978  O  O   . LEU C 1 273 ? 120.015 169.363 162.842 1.00 127.19 ? 289 LEU C O   1 
ATOM   6979  C  CB  . LEU C 1 273 ? 119.827 167.442 160.293 1.00 127.19 ? 289 LEU C CB  1 
ATOM   6980  C  CG  . LEU C 1 273 ? 119.440 167.346 158.812 1.00 127.19 ? 289 LEU C CG  1 
ATOM   6981  C  CD1 . LEU C 1 273 ? 119.671 168.654 158.068 1.00 127.19 ? 289 LEU C CD1 1 
ATOM   6982  C  CD2 . LEU C 1 273 ? 120.193 166.207 158.137 1.00 127.19 ? 289 LEU C CD2 1 
ATOM   6983  N  N   . CYS C 1 274 ? 119.424 167.296 163.525 1.00 131.53 ? 290 CYS C N   1 
ATOM   6984  C  CA  . CYS C 1 274 ? 120.114 167.382 164.803 1.00 131.53 ? 290 CYS C CA  1 
ATOM   6985  C  C   . CYS C 1 274 ? 121.491 166.737 164.767 1.00 131.53 ? 290 CYS C C   1 
ATOM   6986  O  O   . CYS C 1 274 ? 122.150 166.655 165.809 1.00 131.53 ? 290 CYS C O   1 
ATOM   6987  C  CB  . CYS C 1 274 ? 119.269 166.732 165.904 1.00 131.53 ? 290 CYS C CB  1 
ATOM   6988  N  N   . HIS C 1 275 ? 121.937 166.279 163.602 1.00 121.88 ? 291 HIS C N   1 
ATOM   6989  C  CA  . HIS C 1 275 ? 123.165 165.514 163.474 1.00 121.88 ? 291 HIS C CA  1 
ATOM   6990  C  C   . HIS C 1 275 ? 124.165 166.249 162.592 1.00 121.88 ? 291 HIS C C   1 
ATOM   6991  O  O   . HIS C 1 275 ? 123.789 167.004 161.691 1.00 121.88 ? 291 HIS C O   1 
ATOM   6992  C  CB  . HIS C 1 275 ? 122.888 164.132 162.880 1.00 121.88 ? 291 HIS C CB  1 
ATOM   6993  C  CG  . HIS C 1 275 ? 121.530 163.595 163.208 1.00 121.88 ? 291 HIS C CG  1 
ATOM   6994  N  ND1 . HIS C 1 275 ? 120.483 163.630 162.312 1.00 121.88 ? 291 HIS C ND1 1 
ATOM   6995  C  CD2 . HIS C 1 275 ? 121.045 163.015 164.331 1.00 121.88 ? 291 HIS C CD2 1 
ATOM   6996  C  CE1 . HIS C 1 275 ? 119.413 163.091 162.867 1.00 121.88 ? 291 HIS C CE1 1 
ATOM   6997  N  NE2 . HIS C 1 275 ? 119.727 162.709 164.092 1.00 121.88 ? 291 HIS C NE2 1 
ATOM   6998  N  N   . GLN C 1 276 ? 125.446 166.014 162.860 1.00 124.81 ? 292 GLN C N   1 
ATOM   6999  C  CA  . GLN C 1 276 ? 126.508 166.483 161.983 1.00 124.81 ? 292 GLN C CA  1 
ATOM   7000  C  C   . GLN C 1 276 ? 126.589 165.581 160.761 1.00 124.81 ? 292 GLN C C   1 
ATOM   7001  O  O   . GLN C 1 276 ? 126.462 164.358 160.865 1.00 124.81 ? 292 GLN C O   1 
ATOM   7002  C  CB  . GLN C 1 276 ? 127.849 166.504 162.717 1.00 124.81 ? 292 GLN C CB  1 
ATOM   7003  C  CG  . GLN C 1 276 ? 127.729 166.688 164.220 1.00 124.81 ? 292 GLN C CG  1 
ATOM   7004  C  CD  . GLN C 1 276 ? 129.010 167.204 164.846 1.00 124.81 ? 292 GLN C CD  1 
ATOM   7005  O  OE1 . GLN C 1 276 ? 129.391 168.357 164.645 1.00 124.81 ? 292 GLN C OE1 1 
ATOM   7006  N  NE2 . GLN C 1 276 ? 129.679 166.352 165.616 1.00 124.81 ? 292 GLN C NE2 1 
ATOM   7007  N  N   . ILE C 1 277 ? 126.801 166.187 159.598 1.00 100.90 ? 293 ILE C N   1 
ATOM   7008  C  CA  . ILE C 1 277 ? 126.780 165.475 158.327 1.00 100.90 ? 293 ILE C CA  1 
ATOM   7009  C  C   . ILE C 1 277 ? 128.216 165.339 157.843 1.00 100.90 ? 293 ILE C C   1 
ATOM   7010  O  O   . ILE C 1 277 ? 128.855 166.330 157.470 1.00 100.90 ? 293 ILE C O   1 
ATOM   7011  C  CB  . ILE C 1 277 ? 125.916 166.199 157.287 1.00 100.90 ? 293 ILE C CB  1 
ATOM   7012  C  CG1 . ILE C 1 277 ? 124.482 166.352 157.797 1.00 100.90 ? 293 ILE C CG1 1 
ATOM   7013  C  CG2 . ILE C 1 277 ? 125.943 165.457 155.962 1.00 100.90 ? 293 ILE C CG2 1 
ATOM   7014  C  CD1 . ILE C 1 277 ? 123.879 165.073 158.325 1.00 100.90 ? 293 ILE C CD1 1 
ATOM   7015  N  N   . THR C 1 278 ? 128.724 164.106 157.852 1.00 95.34  ? 294 THR C N   1 
ATOM   7016  C  CA  . THR C 1 278 ? 130.035 163.837 157.273 1.00 95.34  ? 294 THR C CA  1 
ATOM   7017  C  C   . THR C 1 278 ? 129.971 163.790 155.750 1.00 95.34  ? 294 THR C C   1 
ATOM   7018  O  O   . THR C 1 278 ? 130.885 164.275 155.073 1.00 95.34  ? 294 THR C O   1 
ATOM   7019  C  CB  . THR C 1 278 ? 130.590 162.524 157.832 1.00 95.34  ? 294 THR C CB  1 
ATOM   7020  O  OG1 . THR C 1 278 ? 130.982 162.714 159.197 1.00 95.34  ? 294 THR C OG1 1 
ATOM   7021  C  CG2 . THR C 1 278 ? 131.793 162.054 157.030 1.00 95.34  ? 294 THR C CG2 1 
ATOM   7022  N  N   . ALA C 1 279 ? 128.895 163.237 155.195 1.00 89.51  ? 295 ALA C N   1 
ATOM   7023  C  CA  . ALA C 1 279 ? 128.747 163.159 153.749 1.00 89.51  ? 295 ALA C CA  1 
ATOM   7024  C  C   . ALA C 1 279 ? 127.268 163.100 153.397 1.00 89.51  ? 295 ALA C C   1 
ATOM   7025  O  O   . ALA C 1 279 ? 126.423 162.771 154.231 1.00 89.51  ? 295 ALA C O   1 
ATOM   7026  C  CB  . ALA C 1 279 ? 129.494 161.955 153.164 1.00 89.51  ? 295 ALA C CB  1 
ATOM   7027  N  N   . ALA C 1 280 ? 126.964 163.422 152.142 1.00 103.04 ? 296 ALA C N   1 
ATOM   7028  C  CA  . ALA C 1 280 ? 125.590 163.409 151.665 1.00 103.04 ? 296 ALA C CA  1 
ATOM   7029  C  C   . ALA C 1 280 ? 125.578 163.047 150.189 1.00 103.04 ? 296 ALA C C   1 
ATOM   7030  O  O   . ALA C 1 280 ? 126.559 163.264 149.473 1.00 103.04 ? 296 ALA C O   1 
ATOM   7031  C  CB  . ALA C 1 280 ? 124.900 164.759 151.889 1.00 103.04 ? 296 ALA C CB  1 
ATOM   7032  N  N   . CYS C 1 281 ? 124.458 162.482 149.744 1.00 110.94 ? 297 CYS C N   1 
ATOM   7033  C  CA  . CYS C 1 281 ? 124.299 162.096 148.351 1.00 110.94 ? 297 CYS C CA  1 
ATOM   7034  C  C   . CYS C 1 281 ? 122.829 162.177 147.964 1.00 110.94 ? 297 CYS C C   1 
ATOM   7035  O  O   . CYS C 1 281 ? 121.935 162.125 148.814 1.00 110.94 ? 297 CYS C O   1 
ATOM   7036  C  CB  . CYS C 1 281 ? 124.848 160.689 148.093 1.00 110.94 ? 297 CYS C CB  1 
ATOM   7037  S  SG  . CYS C 1 281 ? 125.412 160.419 146.401 1.00 110.94 ? 297 CYS C SG  1 
ATOM   7038  N  N   . LYS C 1 282 ? 122.573 162.546 146.728 1.00 104.57 ? 298 LYS C N   1 
ATOM   7039  C  CA  . LYS C 1 282 ? 121.156 162.637 146.337 1.00 104.57 ? 298 LYS C CA  1 
ATOM   7040  C  C   . LYS C 1 282 ? 120.859 161.448 145.434 1.00 104.57 ? 298 LYS C C   1 
ATOM   7041  O  O   . LYS C 1 282 ? 121.389 161.414 144.310 1.00 104.57 ? 298 LYS C O   1 
ATOM   7042  C  CB  . LYS C 1 282 ? 120.827 163.968 145.666 1.00 104.57 ? 298 LYS C CB  1 
ATOM   7043  C  CG  . LYS C 1 282 ? 119.340 164.241 145.566 1.00 104.57 ? 298 LYS C CG  1 
ATOM   7044  C  CD  . LYS C 1 282 ? 118.993 165.611 145.106 1.00 104.57 ? 298 LYS C CD  1 
ATOM   7045  C  CE  . LYS C 1 282 ? 118.643 165.576 143.645 1.00 104.57 ? 298 LYS C CE  1 
ATOM   7046  N  NZ  . LYS C 1 282 ? 119.751 164.993 142.862 1.00 104.57 ? 298 LYS C NZ  1 
ATOM   7047  N  N   . HIS C 1 283 ? 120.091 160.490 145.945 1.00 30.00  ? 299 HIS C N   1 
ATOM   7048  C  CA  . HIS C 1 283 ? 119.737 159.306 145.136 1.00 30.00  ? 299 HIS C CA  1 
ATOM   7049  C  C   . HIS C 1 283 ? 118.350 159.575 144.575 1.00 30.00  ? 299 HIS C C   1 
ATOM   7050  O  O   . HIS C 1 283 ? 117.442 159.774 145.366 1.00 30.00  ? 299 HIS C O   1 
ATOM   7051  C  CB  . HIS C 1 283 ? 119.784 158.049 146.009 1.00 30.00  ? 299 HIS C CB  1 
ATOM   7052  N  N   . GLY C 1 284 ? 118.239 159.679 143.254 1.00 102.39 ? 300 GLY C N   1 
ATOM   7053  C  CA  . GLY C 1 284 ? 116.942 159.587 142.558 1.00 102.39 ? 300 GLY C CA  1 
ATOM   7054  C  C   . GLY C 1 284 ? 115.912 160.553 143.117 1.00 102.39 ? 300 GLY C C   1 
ATOM   7055  O  O   . GLY C 1 284 ? 114.759 160.139 143.301 1.00 102.39 ? 300 GLY C O   1 
ATOM   7056  N  N   . GLY C 1 285 ? 116.310 161.790 143.403 1.00 115.10 ? 301 GLY C N   1 
ATOM   7057  C  CA  . GLY C 1 285 ? 115.367 162.763 143.973 1.00 115.10 ? 301 GLY C CA  1 
ATOM   7058  C  C   . GLY C 1 285 ? 115.210 162.606 145.475 1.00 115.10 ? 301 GLY C C   1 
ATOM   7059  O  O   . GLY C 1 285 ? 114.299 163.245 146.033 1.00 115.10 ? 301 GLY C O   1 
ATOM   7060  N  N   . ASP C 1 286 ? 116.039 161.780 146.115 1.00 114.23 ? 302 ASP C N   1 
ATOM   7061  C  CA  . ASP C 1 286 ? 115.944 161.623 147.588 1.00 114.23 ? 302 ASP C CA  1 
ATOM   7062  C  C   . ASP C 1 286 ? 117.305 161.964 148.185 1.00 114.23 ? 302 ASP C C   1 
ATOM   7063  O  O   . ASP C 1 286 ? 118.289 161.774 147.491 1.00 114.23 ? 302 ASP C O   1 
ATOM   7064  C  CB  . ASP C 1 286 ? 115.464 160.227 147.974 1.00 114.23 ? 302 ASP C CB  1 
ATOM   7065  N  N   . LEU C 1 287 ? 117.322 162.464 149.415 1.00 109.49 ? 303 LEU C N   1 
ATOM   7066  C  CA  . LEU C 1 287 ? 118.513 162.876 150.150 1.00 109.49 ? 303 LEU C CA  1 
ATOM   7067  C  C   . LEU C 1 287 ? 118.935 161.789 151.130 1.00 109.49 ? 303 LEU C C   1 
ATOM   7068  O  O   . LEU C 1 287 ? 118.140 161.370 151.979 1.00 109.49 ? 303 LEU C O   1 
ATOM   7069  C  CB  . LEU C 1 287 ? 118.265 164.190 150.888 1.00 109.49 ? 303 LEU C CB  1 
ATOM   7070  C  CG  . LEU C 1 287 ? 119.517 164.989 151.249 1.00 109.49 ? 303 LEU C CG  1 
ATOM   7071  C  CD1 . LEU C 1 287 ? 120.247 165.431 149.996 1.00 109.49 ? 303 LEU C CD1 1 
ATOM   7072  C  CD2 . LEU C 1 287 ? 119.152 166.188 152.108 1.00 109.49 ? 303 LEU C CD2 1 
ATOM   7073  N  N   . TYR C 1 288 ? 120.181 161.335 151.007 1.00 107.40 ? 304 TYR C N   1 
ATOM   7074  C  CA  . TYR C 1 288 ? 120.811 160.425 151.952 1.00 107.40 ? 304 TYR C CA  1 
ATOM   7075  C  C   . TYR C 1 288 ? 121.937 161.179 152.646 1.00 107.40 ? 304 TYR C C   1 
ATOM   7076  O  O   . TYR C 1 288 ? 122.744 161.834 151.979 1.00 107.40 ? 304 TYR C O   1 
ATOM   7077  C  CB  . TYR C 1 288 ? 121.361 159.187 151.242 1.00 107.40 ? 304 TYR C CB  1 
ATOM   7078  C  CG  . TYR C 1 288 ? 120.302 158.257 150.694 1.00 107.40 ? 304 TYR C CG  1 
ATOM   7079  C  CD1 . TYR C 1 288 ? 119.783 157.230 151.467 1.00 107.40 ? 304 TYR C CD1 1 
ATOM   7080  C  CD2 . TYR C 1 288 ? 119.834 158.398 149.394 1.00 107.40 ? 304 TYR C CD2 1 
ATOM   7081  C  CE1 . TYR C 1 288 ? 118.823 156.373 150.967 1.00 107.40 ? 304 TYR C CE1 1 
ATOM   7082  C  CE2 . TYR C 1 288 ? 118.873 157.547 148.885 1.00 107.40 ? 304 TYR C CE2 1 
ATOM   7083  C  CZ  . TYR C 1 288 ? 118.370 156.538 149.676 1.00 107.40 ? 304 TYR C CZ  1 
ATOM   7084  O  OH  . TYR C 1 288 ? 117.412 155.689 149.173 1.00 107.40 ? 304 TYR C OH  1 
ATOM   7085  N  N   . VAL C 1 289 ? 121.995 161.097 153.975 1.00 99.98  ? 305 VAL C N   1 
ATOM   7086  C  CA  . VAL C 1 289 ? 123.017 161.795 154.751 1.00 99.98  ? 305 VAL C CA  1 
ATOM   7087  C  C   . VAL C 1 289 ? 123.656 160.818 155.733 1.00 99.98  ? 305 VAL C C   1 
ATOM   7088  O  O   . VAL C 1 289 ? 122.957 160.082 156.436 1.00 99.98  ? 305 VAL C O   1 
ATOM   7089  C  CB  . VAL C 1 289 ? 122.452 163.042 155.472 1.00 99.98  ? 305 VAL C CB  1 
ATOM   7090  C  CG1 . VAL C 1 289 ? 121.546 163.836 154.544 1.00 99.98  ? 305 VAL C CG1 1 
ATOM   7091  C  CG2 . VAL C 1 289 ? 121.677 162.676 156.730 1.00 99.98  ? 305 VAL C CG2 1 
ATOM   7092  N  N   . VAL C 1 290 ? 124.986 160.763 155.732 1.00 93.81  ? 306 VAL C N   1 
ATOM   7093  C  CA  . VAL C 1 290 ? 125.745 159.897 156.626 1.00 93.81  ? 306 VAL C CA  1 
ATOM   7094  C  C   . VAL C 1 290 ? 126.602 160.757 157.546 1.00 93.81  ? 306 VAL C C   1 
ATOM   7095  O  O   . VAL C 1 290 ? 127.248 161.714 157.098 1.00 93.81  ? 306 VAL C O   1 
ATOM   7096  C  CB  . VAL C 1 290 ? 126.597 158.875 155.848 1.00 93.81  ? 306 VAL C CB  1 
ATOM   7097  C  CG1 . VAL C 1 290 ? 127.629 159.563 154.983 1.00 93.81  ? 306 VAL C CG1 1 
ATOM   7098  C  CG2 . VAL C 1 290 ? 127.277 157.931 156.815 1.00 93.81  ? 306 VAL C CG2 1 
ATOM   7099  N  N   . GLY C 1 291 ? 126.580 160.426 158.836 1.00 97.29  ? 307 GLY C N   1 
ATOM   7100  C  CA  . GLY C 1 291 ? 127.326 161.149 159.842 1.00 97.29  ? 307 GLY C CA  1 
ATOM   7101  C  C   . GLY C 1 291 ? 127.064 160.686 161.262 1.00 97.29  ? 307 GLY C C   1 
ATOM   7102  O  O   . GLY C 1 291 ? 126.999 159.481 161.552 1.00 97.29  ? 307 GLY C O   1 
ATOM   7103  N  N   . GLY C 1 292 ? 126.839 161.667 162.135 1.00 113.18 ? 308 GLY C N   1 
ATOM   7104  C  CA  . GLY C 1 292 ? 126.698 161.483 163.566 1.00 113.18 ? 308 GLY C CA  1 
ATOM   7105  C  C   . GLY C 1 292 ? 127.954 161.893 164.312 1.00 113.18 ? 308 GLY C C   1 
ATOM   7106  O  O   . GLY C 1 292 ? 128.682 162.776 163.851 1.00 113.18 ? 308 GLY C O   1 
ATOM   7107  N  N   . SER C 1 293 ? 128.215 161.280 165.464 1.00 122.02 ? 309 SER C N   1 
ATOM   7108  C  CA  . SER C 1 293 ? 129.407 161.613 166.234 1.00 122.02 ? 309 SER C CA  1 
ATOM   7109  C  C   . SER C 1 293 ? 130.663 161.234 165.458 1.00 122.02 ? 309 SER C C   1 
ATOM   7110  O  O   . SER C 1 293 ? 130.656 160.315 164.637 1.00 122.02 ? 309 SER C O   1 
ATOM   7111  C  CB  . SER C 1 293 ? 129.381 160.903 167.588 1.00 122.02 ? 309 SER C CB  1 
ATOM   7112  O  OG  . SER C 1 293 ? 129.513 159.500 167.435 1.00 122.02 ? 309 SER C OG  1 
ATOM   7113  N  N   . ILE C 1 294 ? 131.750 161.958 165.710 1.00 120.64 ? 310 ILE C N   1 
ATOM   7114  C  CA  . ILE C 1 294 ? 132.955 161.769 164.902 1.00 120.64 ? 310 ILE C CA  1 
ATOM   7115  C  C   . ILE C 1 294 ? 133.640 160.426 165.183 1.00 120.64 ? 310 ILE C C   1 
ATOM   7116  O  O   . ILE C 1 294 ? 134.283 159.899 164.264 1.00 120.64 ? 310 ILE C O   1 
ATOM   7117  C  CB  . ILE C 1 294 ? 133.909 162.979 165.028 1.00 120.64 ? 310 ILE C CB  1 
ATOM   7118  C  CG1 . ILE C 1 294 ? 134.306 163.355 166.468 1.00 120.64 ? 310 ILE C CG1 1 
ATOM   7119  C  CG2 . ILE C 1 294 ? 133.309 164.201 164.329 1.00 120.64 ? 310 ILE C CG2 1 
ATOM   7120  C  CD1 . ILE C 1 294 ? 135.307 162.437 167.147 1.00 120.64 ? 310 ILE C CD1 1 
ATOM   7121  N  N   . PRO C 1 295 ? 133.570 159.814 166.383 1.00 118.77 ? 311 PRO C N   1 
ATOM   7122  C  CA  . PRO C 1 295 ? 134.215 158.500 166.535 1.00 118.77 ? 311 PRO C CA  1 
ATOM   7123  C  C   . PRO C 1 295 ? 133.388 157.378 165.939 1.00 118.77 ? 311 PRO C C   1 
ATOM   7124  O  O   . PRO C 1 295 ? 133.946 156.332 165.582 1.00 118.77 ? 311 PRO C O   1 
ATOM   7125  C  CB  . PRO C 1 295 ? 134.347 158.339 168.053 1.00 118.77 ? 311 PRO C CB  1 
ATOM   7126  C  CG  . PRO C 1 295 ? 133.175 159.023 168.571 1.00 118.77 ? 311 PRO C CG  1 
ATOM   7127  C  CD  . PRO C 1 295 ? 132.887 160.179 167.643 1.00 118.77 ? 311 PRO C CD  1 
ATOM   7128  N  N   . ARG C 1 296 ? 132.078 157.576 165.825 1.00 102.89 ? 312 ARG C N   1 
ATOM   7129  C  CA  . ARG C 1 296 ? 131.157 156.627 165.202 1.00 102.89 ? 312 ARG C CA  1 
ATOM   7130  C  C   . ARG C 1 296 ? 130.315 157.378 164.178 1.00 102.89 ? 312 ARG C C   1 
ATOM   7131  O  O   . ARG C 1 296 ? 129.114 157.594 164.379 1.00 102.89 ? 312 ARG C O   1 
ATOM   7132  C  CB  . ARG C 1 296 ? 130.274 155.956 166.254 1.00 102.89 ? 312 ARG C CB  1 
ATOM   7133  C  CG  . ARG C 1 296 ? 130.894 154.738 166.905 1.00 102.89 ? 312 ARG C CG  1 
ATOM   7134  C  CD  . ARG C 1 296 ? 129.922 154.071 167.863 1.00 102.89 ? 312 ARG C CD  1 
ATOM   7135  N  NE  . ARG C 1 296 ? 130.380 154.100 169.246 1.00 102.89 ? 312 ARG C NE  1 
ATOM   7136  C  CZ  . ARG C 1 296 ? 129.832 153.391 170.224 1.00 102.89 ? 312 ARG C CZ  1 
ATOM   7137  N  NH1 . ARG C 1 296 ? 128.803 152.590 170.003 1.00 102.89 ? 312 ARG C NH1 1 
ATOM   7138  N  NH2 . ARG C 1 296 ? 130.333 153.482 171.452 1.00 102.89 ? 312 ARG C NH2 1 
ATOM   7139  N  N   . PRO C 1 297 ? 130.926 157.808 163.053 1.00 104.24 ? 313 PRO C N   1 
ATOM   7140  C  CA  . PRO C 1 297 ? 130.190 158.528 162.008 1.00 104.24 ? 313 PRO C CA  1 
ATOM   7141  C  C   . PRO C 1 297 ? 129.552 157.591 160.988 1.00 104.24 ? 313 PRO C C   1 
ATOM   7142  O  O   . PRO C 1 297 ? 129.771 157.709 159.777 1.00 104.24 ? 313 PRO C O   1 
ATOM   7143  C  CB  . PRO C 1 297 ? 131.280 159.395 161.371 1.00 104.24 ? 313 PRO C CB  1 
ATOM   7144  C  CG  . PRO C 1 297 ? 132.500 158.539 161.471 1.00 104.24 ? 313 PRO C CG  1 
ATOM   7145  C  CD  . PRO C 1 297 ? 132.361 157.710 162.730 1.00 104.24 ? 313 PRO C CD  1 
ATOM   7146  N  N   . ARG C 1 298 ? 128.755 156.643 161.477 1.00 100.53 ? 314 ARG C N   1 
ATOM   7147  C  CA  . ARG C 1 298 ? 128.097 155.667 160.626 1.00 100.53 ? 314 ARG C CA  1 
ATOM   7148  C  C   . ARG C 1 298 ? 126.610 155.905 160.450 1.00 100.53 ? 314 ARG C C   1 
ATOM   7149  O  O   . ARG C 1 298 ? 126.034 155.373 159.497 1.00 100.53 ? 314 ARG C O   1 
ATOM   7150  C  CB  . ARG C 1 298 ? 128.255 154.251 161.191 1.00 100.53 ? 314 ARG C CB  1 
ATOM   7151  C  CG  . ARG C 1 298 ? 128.670 154.203 162.636 1.00 100.53 ? 314 ARG C CG  1 
ATOM   7152  C  CD  . ARG C 1 298 ? 129.500 152.979 162.875 1.00 100.53 ? 314 ARG C CD  1 
ATOM   7153  N  NE  . ARG C 1 298 ? 129.797 152.777 164.284 1.00 100.53 ? 314 ARG C NE  1 
ATOM   7154  C  CZ  . ARG C 1 298 ? 130.014 151.588 164.822 1.00 100.53 ? 314 ARG C CZ  1 
ATOM   7155  N  NH1 . ARG C 1 298 ? 129.965 150.488 164.095 1.00 100.53 ? 314 ARG C NH1 1 
ATOM   7156  N  NH2 . ARG C 1 298 ? 130.306 151.503 166.114 1.00 100.53 ? 314 ARG C NH2 1 
ATOM   7157  N  N   . ARG C 1 299 ? 125.974 156.655 161.351 1.00 100.25 ? 315 ARG C N   1 
ATOM   7158  C  CA  . ARG C 1 299 ? 124.530 156.809 161.267 1.00 100.25 ? 315 ARG C CA  1 
ATOM   7159  C  C   . ARG C 1 299 ? 124.137 157.356 159.904 1.00 100.25 ? 315 ARG C C   1 
ATOM   7160  O  O   . ARG C 1 299 ? 124.742 158.302 159.399 1.00 100.25 ? 315 ARG C O   1 
ATOM   7161  C  CB  . ARG C 1 299 ? 124.056 157.737 162.382 1.00 100.25 ? 315 ARG C CB  1 
ATOM   7162  C  CG  . ARG C 1 299 ? 123.864 157.060 163.727 1.00 100.25 ? 315 ARG C CG  1 
ATOM   7163  C  CD  . ARG C 1 299 ? 122.431 156.604 163.908 1.00 100.25 ? 315 ARG C CD  1 
ATOM   7164  N  NE  . ARG C 1 299 ? 121.639 157.635 164.569 1.00 100.25 ? 315 ARG C NE  1 
ATOM   7165  C  CZ  . ARG C 1 299 ? 120.319 157.606 164.690 1.00 100.25 ? 315 ARG C CZ  1 
ATOM   7166  N  NH1 . ARG C 1 299 ? 119.598 156.634 164.160 1.00 100.25 ? 315 ARG C NH1 1 
ATOM   7167  N  NH2 . ARG C 1 299 ? 119.707 158.585 165.351 1.00 100.25 ? 315 ARG C NH2 1 
ATOM   7168  N  N   . MET C 1 300 ? 123.116 156.757 159.299 1.00 112.18 ? 316 MET C N   1 
ATOM   7169  C  CA  . MET C 1 300 ? 122.675 157.214 157.992 1.00 112.18 ? 316 MET C CA  1 
ATOM   7170  C  C   . MET C 1 300 ? 121.172 157.452 158.033 1.00 112.18 ? 316 MET C C   1 
ATOM   7171  O  O   . MET C 1 300 ? 120.406 156.623 158.546 1.00 112.18 ? 316 MET C O   1 
ATOM   7172  C  CB  . MET C 1 300 ? 123.103 156.216 156.901 1.00 112.18 ? 316 MET C CB  1 
ATOM   7173  C  CG  . MET C 1 300 ? 123.252 156.837 155.514 1.00 112.18 ? 316 MET C CG  1 
ATOM   7174  S  SD  . MET C 1 300 ? 123.394 155.653 154.161 1.00 112.18 ? 316 MET C SD  1 
ATOM   7175  C  CE  . MET C 1 300 ? 121.698 155.469 153.656 1.00 112.18 ? 316 MET C CE  1 
ATOM   7176  N  N   . TRP C 1 301 ? 120.752 158.541 157.398 1.00 100.02 ? 317 TRP C N   1 
ATOM   7177  C  CA  . TRP C 1 301 ? 119.364 158.964 157.389 1.00 100.02 ? 317 TRP C CA  1 
ATOM   7178  C  C   . TRP C 1 301 ? 118.905 159.300 155.980 1.00 100.02 ? 317 TRP C C   1 
ATOM   7179  O  O   . TRP C 1 301 ? 119.683 159.729 155.122 1.00 100.02 ? 317 TRP C O   1 
ATOM   7180  C  CB  . TRP C 1 301 ? 119.124 160.187 158.284 1.00 100.02 ? 317 TRP C CB  1 
ATOM   7181  C  CG  . TRP C 1 301 ? 119.469 159.986 159.721 1.00 100.02 ? 317 TRP C CG  1 
ATOM   7182  C  CD1 . TRP C 1 301 ? 118.666 159.468 160.693 1.00 100.02 ? 317 TRP C CD1 1 
ATOM   7183  C  CD2 . TRP C 1 301 ? 120.695 160.347 160.363 1.00 100.02 ? 317 TRP C CD2 1 
ATOM   7184  N  NE1 . TRP C 1 301 ? 119.326 159.460 161.897 1.00 100.02 ? 317 TRP C NE1 1 
ATOM   7185  C  CE2 . TRP C 1 301 ? 120.574 159.998 161.721 1.00 100.02 ? 317 TRP C CE2 1 
ATOM   7186  C  CE3 . TRP C 1 301 ? 121.889 160.923 159.918 1.00 100.02 ? 317 TRP C CE3 1 
ATOM   7187  C  CZ2 . TRP C 1 301 ? 121.600 160.205 162.637 1.00 100.02 ? 317 TRP C CZ2 1 
ATOM   7188  C  CZ3 . TRP C 1 301 ? 122.906 161.127 160.829 1.00 100.02 ? 317 TRP C CZ3 1 
ATOM   7189  C  CH2 . TRP C 1 301 ? 122.755 160.771 162.172 1.00 100.02 ? 317 TRP C CH2 1 
ATOM   7190  N  N   . LYS C 1 302 ? 117.612 159.089 155.779 1.00 109.94 ? 318 LYS C N   1 
ATOM   7191  C  CA  . LYS C 1 302 ? 116.857 159.321 154.562 1.00 109.94 ? 318 LYS C CA  1 
ATOM   7192  C  C   . LYS C 1 302 ? 115.762 160.286 155.001 1.00 109.94 ? 318 LYS C C   1 
ATOM   7193  O  O   . LYS C 1 302 ? 114.693 159.874 155.464 1.00 109.94 ? 318 LYS C O   1 
ATOM   7194  C  CB  . LYS C 1 302 ? 116.299 158.002 154.028 1.00 109.94 ? 318 LYS C CB  1 
ATOM   7195  C  CG  . LYS C 1 302 ? 115.427 158.084 152.795 1.00 109.94 ? 318 LYS C CG  1 
ATOM   7196  C  CD  . LYS C 1 302 ? 116.203 158.548 151.585 1.00 109.94 ? 318 LYS C CD  1 
ATOM   7197  C  CE  . LYS C 1 302 ? 115.431 158.239 150.319 1.00 109.94 ? 318 LYS C CE  1 
ATOM   7198  N  NZ  . LYS C 1 302 ? 115.112 156.790 150.204 1.00 109.94 ? 318 LYS C NZ  1 
ATOM   7199  N  N   . CYS C 1 303 ? 116.103 161.574 154.989 1.00 118.13 ? 319 CYS C N   1 
ATOM   7200  C  CA  . CYS C 1 303 ? 115.224 162.636 155.459 1.00 118.13 ? 319 CYS C CA  1 
ATOM   7201  C  C   . CYS C 1 303 ? 114.595 163.308 154.244 1.00 118.13 ? 319 CYS C C   1 
ATOM   7202  O  O   . CYS C 1 303 ? 115.263 164.059 153.526 1.00 118.13 ? 319 CYS C O   1 
ATOM   7203  C  CB  . CYS C 1 303 ? 115.999 163.634 156.318 1.00 118.13 ? 319 CYS C CB  1 
ATOM   7204  S  SG  . CYS C 1 303 ? 117.529 164.262 155.586 1.00 118.13 ? 319 CYS C SG  1 
ATOM   7205  N  N   . ASN C 1 304 ? 113.313 163.043 154.015 1.00 134.37 ? 320 ASN C N   1 
ATOM   7206  C  CA  . ASN C 1 304 ? 112.600 163.634 152.886 1.00 134.37 ? 320 ASN C CA  1 
ATOM   7207  C  C   . ASN C 1 304 ? 111.133 163.857 153.232 1.00 134.37 ? 320 ASN C C   1 
ATOM   7208  O  O   . ASN C 1 304 ? 110.352 162.908 153.307 1.00 134.37 ? 320 ASN C O   1 
ATOM   7209  C  CB  . ASN C 1 304 ? 112.714 162.758 151.632 1.00 134.37 ? 320 ASN C CB  1 
ATOM   7210  C  CG  . ASN C 1 304 ? 114.139 162.647 151.114 1.00 134.37 ? 320 ASN C CG  1 
ATOM   7211  O  OD1 . ASN C 1 304 ? 114.522 163.335 150.168 1.00 134.37 ? 320 ASN C OD1 1 
ATOM   7212  N  ND2 . ASN C 1 304 ? 114.921 161.754 151.710 1.00 134.37 ? 320 ASN C ND2 1 
ATOM   7213  N  N   . VAL C 1 308 ? 107.488 163.346 156.650 1.00 145.30 ? 324 VAL C N   1 
ATOM   7214  C  CA  . VAL C 1 308 ? 108.249 162.972 157.835 1.00 145.30 ? 324 VAL C CA  1 
ATOM   7215  C  C   . VAL C 1 308 ? 109.657 162.539 157.445 1.00 145.30 ? 324 VAL C C   1 
ATOM   7216  O  O   . VAL C 1 308 ? 109.841 161.573 156.706 1.00 145.30 ? 324 VAL C O   1 
ATOM   7217  C  CB  . VAL C 1 308 ? 107.538 161.861 158.625 1.00 145.30 ? 324 VAL C CB  1 
ATOM   7218  N  N   . ASP C 1 309 ? 110.648 163.263 157.953 1.00 145.56 ? 325 ASP C N   1 
ATOM   7219  C  CA  . ASP C 1 309 ? 112.047 162.992 157.667 1.00 145.56 ? 325 ASP C CA  1 
ATOM   7220  C  C   . ASP C 1 309 ? 112.612 162.046 158.726 1.00 145.56 ? 325 ASP C C   1 
ATOM   7221  O  O   . ASP C 1 309 ? 111.867 161.446 159.507 1.00 145.56 ? 325 ASP C O   1 
ATOM   7222  C  CB  . ASP C 1 309 ? 112.821 164.306 157.598 1.00 145.56 ? 325 ASP C CB  1 
ATOM   7223  N  N   . TRP C 1 310 ? 113.940 161.875 158.733 1.00 132.07 ? 326 TRP C N   1 
ATOM   7224  C  CA  . TRP C 1 310 ? 114.647 161.069 159.732 1.00 132.07 ? 326 TRP C CA  1 
ATOM   7225  C  C   . TRP C 1 310 ? 114.423 159.567 159.560 1.00 132.07 ? 326 TRP C C   1 
ATOM   7226  O  O   . TRP C 1 310 ? 114.405 158.829 160.548 1.00 132.07 ? 326 TRP C O   1 
ATOM   7227  C  CB  . TRP C 1 310 ? 114.294 161.497 161.162 1.00 132.07 ? 326 TRP C CB  1 
ATOM   7228  N  N   . GLU C 1 311 ? 114.246 159.082 158.331 1.00 128.56 ? 327 GLU C N   1 
ATOM   7229  C  CA  . GLU C 1 311 ? 114.098 157.644 158.128 1.00 128.56 ? 327 GLU C CA  1 
ATOM   7230  C  C   . GLU C 1 311 ? 115.463 156.973 158.250 1.00 128.56 ? 327 GLU C C   1 
ATOM   7231  O  O   . GLU C 1 311 ? 116.380 157.281 157.491 1.00 128.56 ? 327 GLU C O   1 
ATOM   7232  C  CB  . GLU C 1 311 ? 113.473 157.356 156.764 1.00 128.56 ? 327 GLU C CB  1 
ATOM   7233  C  CG  . GLU C 1 311 ? 111.961 157.104 156.772 1.00 128.56 ? 327 GLU C CG  1 
ATOM   7234  C  CD  . GLU C 1 311 ? 111.125 158.310 157.187 1.00 128.56 ? 327 GLU C CD  1 
ATOM   7235  O  OE1 . GLU C 1 311 ? 111.690 159.354 157.574 1.00 128.56 ? 327 GLU C OE1 1 
ATOM   7236  O  OE2 . GLU C 1 311 ? 109.882 158.211 157.119 1.00 128.56 ? 327 GLU C OE2 1 
ATOM   7237  N  N   . TRP C 1 312 ? 115.602 156.044 159.188 1.00 118.36 ? 328 TRP C N   1 
ATOM   7238  C  CA  . TRP C 1 312 ? 116.909 155.459 159.450 1.00 118.36 ? 328 TRP C CA  1 
ATOM   7239  C  C   . TRP C 1 312 ? 117.250 154.410 158.398 1.00 118.36 ? 328 TRP C C   1 
ATOM   7240  O  O   . TRP C 1 312 ? 116.377 153.696 157.898 1.00 118.36 ? 328 TRP C O   1 
ATOM   7241  C  CB  . TRP C 1 312 ? 116.917 154.881 160.873 1.00 118.36 ? 328 TRP C CB  1 
ATOM   7242  C  CG  . TRP C 1 312 ? 116.294 153.499 161.069 1.00 118.36 ? 328 TRP C CG  1 
ATOM   7243  C  CD1 . TRP C 1 312 ? 115.157 153.230 161.778 1.00 118.36 ? 328 TRP C CD1 1 
ATOM   7244  C  CD2 . TRP C 1 312 ? 116.826 152.218 160.681 1.00 118.36 ? 328 TRP C CD2 1 
ATOM   7245  N  NE1 . TRP C 1 312 ? 114.906 151.882 161.789 1.00 118.36 ? 328 TRP C NE1 1 
ATOM   7246  C  CE2 . TRP C 1 312 ? 115.918 151.237 161.132 1.00 118.36 ? 328 TRP C CE2 1 
ATOM   7247  C  CE3 . TRP C 1 312 ? 117.960 151.807 159.977 1.00 118.36 ? 328 TRP C CE3 1 
ATOM   7248  C  CZ2 . TRP C 1 312 ? 116.110 149.877 160.898 1.00 118.36 ? 328 TRP C CZ2 1 
ATOM   7249  C  CZ3 . TRP C 1 312 ? 118.145 150.457 159.740 1.00 118.36 ? 328 TRP C CZ3 1 
ATOM   7250  C  CH2 . TRP C 1 312 ? 117.227 149.508 160.202 1.00 118.36 ? 328 TRP C CH2 1 
ATOM   7251  N  N   . CYS C 1 313 ? 118.540 154.323 158.058 1.00 111.34 ? 329 CYS C N   1 
ATOM   7252  C  CA  . CYS C 1 313 ? 119.002 153.360 157.067 1.00 111.34 ? 329 CYS C CA  1 
ATOM   7253  C  C   . CYS C 1 313 ? 120.149 152.525 157.623 1.00 111.34 ? 329 CYS C C   1 
ATOM   7254  O  O   . CYS C 1 313 ? 120.646 152.765 158.727 1.00 111.34 ? 329 CYS C O   1 
ATOM   7255  C  CB  . CYS C 1 313 ? 119.428 154.061 155.775 1.00 111.34 ? 329 CYS C CB  1 
ATOM   7256  S  SG  . CYS C 1 313 ? 118.065 154.755 154.812 1.00 111.34 ? 329 CYS C SG  1 
ATOM   7257  N  N   . ALA C 1 314 ? 120.564 151.530 156.839 1.00 101.09 ? 330 ALA C N   1 
ATOM   7258  C  CA  . ALA C 1 314 ? 121.586 150.598 157.296 1.00 101.09 ? 330 ALA C CA  1 
ATOM   7259  C  C   . ALA C 1 314 ? 122.911 151.322 157.516 1.00 101.09 ? 330 ALA C C   1 
ATOM   7260  O  O   . ALA C 1 314 ? 123.375 152.045 156.623 1.00 101.09 ? 330 ALA C O   1 
ATOM   7261  C  CB  . ALA C 1 314 ? 121.776 149.468 156.286 1.00 101.09 ? 330 ALA C CB  1 
ATOM   7262  N  N   . PRO C 1 315 ? 123.539 151.161 158.674 1.00 91.49  ? 331 PRO C N   1 
ATOM   7263  C  CA  . PRO C 1 315 ? 124.850 151.775 158.904 1.00 91.49  ? 331 PRO C CA  1 
ATOM   7264  C  C   . PRO C 1 315 ? 125.952 151.127 158.083 1.00 91.49  ? 331 PRO C C   1 
ATOM   7265  O  O   . PRO C 1 315 ? 125.870 149.960 157.692 1.00 91.49  ? 331 PRO C O   1 
ATOM   7266  C  CB  . PRO C 1 315 ? 125.088 151.550 160.400 1.00 91.49  ? 331 PRO C CB  1 
ATOM   7267  C  CG  . PRO C 1 315 ? 123.750 151.250 160.956 1.00 91.49  ? 331 PRO C CG  1 
ATOM   7268  C  CD  . PRO C 1 315 ? 123.000 150.544 159.892 1.00 91.49  ? 331 PRO C CD  1 
ATOM   7269  N  N   . LEU C 1 316 ? 126.991 151.906 157.826 1.00 91.67  ? 332 LEU C N   1 
ATOM   7270  C  CA  . LEU C 1 316 ? 128.192 151.402 157.183 1.00 91.67  ? 332 LEU C CA  1 
ATOM   7271  C  C   . LEU C 1 316 ? 129.069 150.676 158.203 1.00 91.67  ? 332 LEU C C   1 
ATOM   7272  O  O   . LEU C 1 316 ? 129.122 151.063 159.373 1.00 91.67  ? 332 LEU C O   1 
ATOM   7273  C  CB  . LEU C 1 316 ? 128.977 152.539 156.539 1.00 91.67  ? 332 LEU C CB  1 
ATOM   7274  C  CG  . LEU C 1 316 ? 128.252 153.359 155.469 1.00 91.67  ? 332 LEU C CG  1 
ATOM   7275  C  CD1 . LEU C 1 316 ? 127.454 154.495 156.075 1.00 91.67  ? 332 LEU C CD1 1 
ATOM   7276  C  CD2 . LEU C 1 316 ? 129.253 153.892 154.461 1.00 91.67  ? 332 LEU C CD2 1 
ATOM   7277  N  N   . PRO C 1 317 ? 129.768 149.618 157.785 1.00 90.78  ? 333 PRO C N   1 
ATOM   7278  C  CA  . PRO C 1 317 ? 130.642 148.889 158.711 1.00 90.78  ? 333 PRO C CA  1 
ATOM   7279  C  C   . PRO C 1 317 ? 131.989 149.549 158.971 1.00 90.78  ? 333 PRO C C   1 
ATOM   7280  O  O   . PRO C 1 317 ? 132.810 148.964 159.685 1.00 90.78  ? 333 PRO C O   1 
ATOM   7281  C  CB  . PRO C 1 317 ? 130.816 147.535 158.013 1.00 90.78  ? 333 PRO C CB  1 
ATOM   7282  C  CG  . PRO C 1 317 ? 130.701 147.850 156.578 1.00 90.78  ? 333 PRO C CG  1 
ATOM   7283  C  CD  . PRO C 1 317 ? 129.698 148.968 156.465 1.00 90.78  ? 333 PRO C CD  1 
ATOM   7284  N  N   . ARG C 1 318 ? 132.256 150.726 158.409 1.00 100.06 ? 334 ARG C N   1 
ATOM   7285  C  CA  . ARG C 1 318 ? 133.521 151.417 158.609 1.00 100.06 ? 334 ARG C CA  1 
ATOM   7286  C  C   . ARG C 1 318 ? 133.276 152.778 159.244 1.00 100.06 ? 334 ARG C C   1 
ATOM   7287  O  O   . ARG C 1 318 ? 132.199 153.365 159.105 1.00 100.06 ? 334 ARG C O   1 
ATOM   7288  C  CB  . ARG C 1 318 ? 134.279 151.612 157.291 1.00 100.06 ? 334 ARG C CB  1 
ATOM   7289  C  CG  . ARG C 1 318 ? 134.577 150.340 156.528 1.00 100.06 ? 334 ARG C CG  1 
ATOM   7290  C  CD  . ARG C 1 318 ? 135.902 149.711 156.905 1.00 100.06 ? 334 ARG C CD  1 
ATOM   7291  N  NE  . ARG C 1 318 ? 136.330 148.765 155.881 1.00 100.06 ? 334 ARG C NE  1 
ATOM   7292  C  CZ  . ARG C 1 318 ? 137.382 147.965 155.985 1.00 100.06 ? 334 ARG C CZ  1 
ATOM   7293  N  NH1 . ARG C 1 318 ? 138.136 147.952 157.071 1.00 100.06 ? 334 ARG C NH1 1 
ATOM   7294  N  NH2 . ARG C 1 318 ? 137.682 147.154 154.974 1.00 100.06 ? 334 ARG C NH2 1 
ATOM   7295  N  N   . ASP C 1 319 ? 134.292 153.274 159.943 1.00 95.79  ? 335 ASP C N   1 
ATOM   7296  C  CA  . ASP C 1 319 ? 134.280 154.602 160.551 1.00 95.79  ? 335 ASP C CA  1 
ATOM   7297  C  C   . ASP C 1 319 ? 135.345 155.444 159.863 1.00 95.79  ? 335 ASP C C   1 
ATOM   7298  O  O   . ASP C 1 319 ? 136.534 155.346 160.182 1.00 95.79  ? 335 ASP C O   1 
ATOM   7299  C  CB  . ASP C 1 319 ? 134.498 154.524 162.056 1.00 95.79  ? 335 ASP C CB  1 
ATOM   7300  C  CG  . ASP C 1 319 ? 133.287 153.995 162.773 1.00 95.79  ? 335 ASP C CG  1 
ATOM   7301  O  OD1 . ASP C 1 319 ? 132.206 154.028 162.159 1.00 95.79  ? 335 ASP C OD1 1 
ATOM   7302  O  OD2 . ASP C 1 319 ? 133.403 153.555 163.932 1.00 95.79  ? 335 ASP C OD2 1 
ATOM   7303  N  N   . ARG C 1 320 ? 134.911 156.272 158.918 1.00 86.93  ? 336 ARG C N   1 
ATOM   7304  C  CA  . ARG C 1 320 ? 135.813 157.094 158.132 1.00 86.93  ? 336 ARG C CA  1 
ATOM   7305  C  C   . ARG C 1 320 ? 135.227 158.490 158.009 1.00 86.93  ? 336 ARG C C   1 
ATOM   7306  O  O   . ARG C 1 320 ? 134.008 158.667 157.945 1.00 86.93  ? 336 ARG C O   1 
ATOM   7307  C  CB  . ARG C 1 320 ? 136.042 156.491 156.739 1.00 86.93  ? 336 ARG C CB  1 
ATOM   7308  C  CG  . ARG C 1 320 ? 136.591 155.073 156.758 1.00 86.93  ? 336 ARG C CG  1 
ATOM   7309  C  CD  . ARG C 1 320 ? 136.564 154.451 155.375 1.00 86.93  ? 336 ARG C CD  1 
ATOM   7310  N  NE  . ARG C 1 320 ? 135.211 154.398 154.834 1.00 86.93  ? 336 ARG C NE  1 
ATOM   7311  C  CZ  . ARG C 1 320 ? 134.911 154.004 153.605 1.00 86.93  ? 336 ARG C CZ  1 
ATOM   7312  N  NH1 . ARG C 1 320 ? 135.848 153.614 152.757 1.00 86.93  ? 336 ARG C NH1 1 
ATOM   7313  N  NH2 . ARG C 1 320 ? 133.639 154.000 153.217 1.00 86.93  ? 336 ARG C NH2 1 
ATOM   7314  N  N   . LEU C 1 321 ? 136.112 159.480 157.977 1.00 81.67  ? 337 LEU C N   1 
ATOM   7315  C  CA  . LEU C 1 321 ? 135.737 160.872 157.803 1.00 81.67  ? 337 LEU C CA  1 
ATOM   7316  C  C   . LEU C 1 321 ? 136.158 161.339 156.417 1.00 81.67  ? 337 LEU C C   1 
ATOM   7317  O  O   . LEU C 1 321 ? 137.178 160.897 155.880 1.00 81.67  ? 337 LEU C O   1 
ATOM   7318  C  CB  . LEU C 1 321 ? 136.374 161.760 158.876 1.00 81.67  ? 337 LEU C CB  1 
ATOM   7319  C  CG  . LEU C 1 321 ? 135.805 161.618 160.289 1.00 81.67  ? 337 LEU C CG  1 
ATOM   7320  C  CD1 . LEU C 1 321 ? 136.715 162.285 161.307 1.00 81.67  ? 337 LEU C CD1 1 
ATOM   7321  C  CD2 . LEU C 1 321 ? 134.403 162.203 160.360 1.00 81.67  ? 337 LEU C CD2 1 
ATOM   7322  N  N   . GLN C 1 322 ? 135.355 162.237 155.846 1.00 94.82  ? 338 GLN C N   1 
ATOM   7323  C  CA  . GLN C 1 322 ? 135.592 162.767 154.503 1.00 94.82  ? 338 GLN C CA  1 
ATOM   7324  C  C   . GLN C 1 322 ? 135.672 161.644 153.472 1.00 94.82  ? 338 GLN C C   1 
ATOM   7325  O  O   . GLN C 1 322 ? 136.461 161.700 152.527 1.00 94.82  ? 338 GLN C O   1 
ATOM   7326  C  CB  . GLN C 1 322 ? 136.854 163.633 154.465 1.00 94.82  ? 338 GLN C CB  1 
ATOM   7327  C  CG  . GLN C 1 322 ? 136.717 164.962 155.188 1.00 94.82  ? 338 GLN C CG  1 
ATOM   7328  C  CD  . GLN C 1 322 ? 138.011 165.403 155.843 1.00 94.82  ? 338 GLN C CD  1 
ATOM   7329  O  OE1 . GLN C 1 322 ? 138.069 165.587 157.059 1.00 94.82  ? 338 GLN C OE1 1 
ATOM   7330  N  NE2 . GLN C 1 322 ? 139.057 165.572 155.043 1.00 94.82  ? 338 GLN C NE2 1 
ATOM   7331  N  N   . HIS C 1 323 ? 134.851 160.613 153.657 1.00 86.34  ? 339 HIS C N   1 
ATOM   7332  C  CA  . HIS C 1 323 ? 134.774 159.526 152.692 1.00 86.34  ? 339 HIS C CA  1 
ATOM   7333  C  C   . HIS C 1 323 ? 133.852 159.934 151.551 1.00 86.34  ? 339 HIS C C   1 
ATOM   7334  O  O   . HIS C 1 323 ? 132.771 160.485 151.781 1.00 86.34  ? 339 HIS C O   1 
ATOM   7335  C  CB  . HIS C 1 323 ? 134.276 158.243 153.356 1.00 86.34  ? 339 HIS C CB  1 
ATOM   7336  C  CG  . HIS C 1 323 ? 132.875 158.332 153.877 1.00 86.34  ? 339 HIS C CG  1 
ATOM   7337  N  ND1 . HIS C 1 323 ? 131.770 158.148 153.075 1.00 86.34  ? 339 HIS C ND1 1 
ATOM   7338  C  CD2 . HIS C 1 323 ? 132.399 158.583 155.120 1.00 86.34  ? 339 HIS C CD2 1 
ATOM   7339  C  CE1 . HIS C 1 323 ? 130.674 158.284 153.800 1.00 86.34  ? 339 HIS C CE1 1 
ATOM   7340  N  NE2 . HIS C 1 323 ? 131.028 158.548 155.044 1.00 86.34  ? 339 HIS C NE2 1 
ATOM   7341  N  N   . THR C 1 324 ? 134.284 159.672 150.323 1.00 90.70  ? 340 THR C N   1 
ATOM   7342  C  CA  . THR C 1 324 ? 133.534 160.104 149.151 1.00 90.70  ? 340 THR C CA  1 
ATOM   7343  C  C   . THR C 1 324 ? 132.271 159.269 148.971 1.00 90.70  ? 340 THR C C   1 
ATOM   7344  O  O   . THR C 1 324 ? 132.344 158.044 148.825 1.00 90.70  ? 340 THR C O   1 
ATOM   7345  C  CB  . THR C 1 324 ? 134.405 160.012 147.905 1.00 90.70  ? 340 THR C CB  1 
ATOM   7346  O  OG1 . THR C 1 324 ? 135.407 161.033 147.947 1.00 90.70  ? 340 THR C OG1 1 
ATOM   7347  C  CG2 . THR C 1 324 ? 133.554 160.205 146.672 1.00 90.70  ? 340 THR C CG2 1 
ATOM   7348  N  N   . LEU C 1 325 ? 131.116 159.929 148.985 1.00 95.02  ? 341 LEU C N   1 
ATOM   7349  C  CA  . LEU C 1 325 ? 129.831 159.267 148.804 1.00 95.02  ? 341 LEU C CA  1 
ATOM   7350  C  C   . LEU C 1 325 ? 129.311 159.562 147.402 1.00 95.02  ? 341 LEU C C   1 
ATOM   7351  O  O   . LEU C 1 325 ? 129.211 160.726 147.004 1.00 95.02  ? 341 LEU C O   1 
ATOM   7352  C  CB  . LEU C 1 325 ? 128.827 159.732 149.859 1.00 95.02  ? 341 LEU C CB  1 
ATOM   7353  C  CG  . LEU C 1 325 ? 127.635 158.814 150.125 1.00 95.02  ? 341 LEU C CG  1 
ATOM   7354  C  CD1 . LEU C 1 325 ? 128.100 157.508 150.745 1.00 95.02  ? 341 LEU C CD1 1 
ATOM   7355  C  CD2 . LEU C 1 325 ? 126.624 159.502 151.026 1.00 95.02  ? 341 LEU C CD2 1 
ATOM   7356  N  N   . VAL C 1 326 ? 128.982 158.504 146.662 1.00 95.21  ? 342 VAL C N   1 
ATOM   7357  C  CA  . VAL C 1 326 ? 128.565 158.592 145.268 1.00 95.21  ? 342 VAL C CA  1 
ATOM   7358  C  C   . VAL C 1 326 ? 127.284 157.787 145.092 1.00 95.21  ? 342 VAL C C   1 
ATOM   7359  O  O   . VAL C 1 326 ? 127.047 156.812 145.808 1.00 95.21  ? 342 VAL C O   1 
ATOM   7360  C  CB  . VAL C 1 326 ? 129.684 158.084 144.323 1.00 95.21  ? 342 VAL C CB  1 
ATOM   7361  C  CG1 . VAL C 1 326 ? 129.233 158.075 142.876 1.00 95.21  ? 342 VAL C CG1 1 
ATOM   7362  C  CG2 . VAL C 1 326 ? 130.937 158.926 144.477 1.00 95.21  ? 342 VAL C CG2 1 
ATOM   7363  N  N   . SER C 1 327 ? 126.444 158.203 144.147 1.00 104.48 ? 343 SER C N   1 
ATOM   7364  C  CA  . SER C 1 327 ? 125.208 157.497 143.836 1.00 104.48 ? 343 SER C CA  1 
ATOM   7365  C  C   . SER C 1 327 ? 125.290 156.902 142.437 1.00 104.48 ? 343 SER C C   1 
ATOM   7366  O  O   . SER C 1 327 ? 125.750 157.561 141.500 1.00 104.48 ? 343 SER C O   1 
ATOM   7367  C  CB  . SER C 1 327 ? 123.997 158.430 143.928 1.00 104.48 ? 343 SER C CB  1 
ATOM   7368  O  OG  . SER C 1 327 ? 122.844 157.827 143.366 1.00 104.48 ? 343 SER C OG  1 
ATOM   7369  N  N   . VAL C 1 328 ? 124.844 155.655 142.296 1.00 107.79 ? 344 VAL C N   1 
ATOM   7370  C  CA  . VAL C 1 328 ? 124.802 154.973 141.006 1.00 107.79 ? 344 VAL C CA  1 
ATOM   7371  C  C   . VAL C 1 328 ? 123.417 154.360 140.842 1.00 107.79 ? 344 VAL C C   1 
ATOM   7372  O  O   . VAL C 1 328 ? 123.199 153.206 141.243 1.00 107.79 ? 344 VAL C O   1 
ATOM   7373  C  CB  . VAL C 1 328 ? 125.897 153.899 140.893 1.00 107.79 ? 344 VAL C CB  1 
ATOM   7374  C  CG1 . VAL C 1 328 ? 126.020 153.418 139.455 1.00 107.79 ? 344 VAL C CG1 1 
ATOM   7375  C  CG2 . VAL C 1 328 ? 127.235 154.424 141.397 1.00 107.79 ? 344 VAL C CG2 1 
ATOM   7376  N  N   . PRO C 1 329 ? 122.445 155.097 140.298 1.00 103.56 ? 345 PRO C N   1 
ATOM   7377  C  CA  . PRO C 1 329 ? 121.133 154.490 140.022 1.00 103.56 ? 345 PRO C CA  1 
ATOM   7378  C  C   . PRO C 1 329 ? 121.185 153.378 138.991 1.00 103.56 ? 345 PRO C C   1 
ATOM   7379  O  O   . PRO C 1 329 ? 120.248 152.572 138.928 1.00 103.56 ? 345 PRO C O   1 
ATOM   7380  C  CB  . PRO C 1 329 ? 120.292 155.675 139.527 1.00 103.56 ? 345 PRO C CB  1 
ATOM   7381  C  CG  . PRO C 1 329 ? 121.288 156.693 139.071 1.00 103.56 ? 345 PRO C CG  1 
ATOM   7382  C  CD  . PRO C 1 329 ? 122.479 156.529 139.961 1.00 103.56 ? 345 PRO C CD  1 
ATOM   7383  N  N   . GLY C 1 330 ? 122.238 153.316 138.172 1.00 118.26 ? 346 GLY C N   1 
ATOM   7384  C  CA  . GLY C 1 330 ? 122.354 152.232 137.208 1.00 118.26 ? 346 GLY C CA  1 
ATOM   7385  C  C   . GLY C 1 330 ? 122.345 150.868 137.867 1.00 118.26 ? 346 GLY C C   1 
ATOM   7386  O  O   . GLY C 1 330 ? 121.663 149.946 137.413 1.00 118.26 ? 346 GLY C O   1 
ATOM   7387  N  N   . LYS C 1 331 ? 123.107 150.720 138.948 1.00 110.07 ? 347 LYS C N   1 
ATOM   7388  C  CA  . LYS C 1 331 ? 123.095 149.509 139.753 1.00 110.07 ? 347 LYS C CA  1 
ATOM   7389  C  C   . LYS C 1 331 ? 122.317 149.689 141.048 1.00 110.07 ? 347 LYS C C   1 
ATOM   7390  O  O   . LYS C 1 331 ? 122.342 148.798 141.903 1.00 110.07 ? 347 LYS C O   1 
ATOM   7391  C  CB  . LYS C 1 331 ? 124.525 149.055 140.050 1.00 110.07 ? 347 LYS C CB  1 
ATOM   7392  C  CG  . LYS C 1 331 ? 125.425 149.027 138.826 1.00 110.07 ? 347 LYS C CG  1 
ATOM   7393  C  CD  . LYS C 1 331 ? 126.730 148.307 139.111 1.00 110.07 ? 347 LYS C CD  1 
ATOM   7394  C  CE  . LYS C 1 331 ? 127.633 148.309 137.890 1.00 110.07 ? 347 LYS C CE  1 
ATOM   7395  N  NZ  . LYS C 1 331 ? 127.937 149.691 137.428 1.00 110.07 ? 347 LYS C NZ  1 
ATOM   7396  N  N   . ASP C 1 332 ? 121.630 150.824 141.207 1.00 124.61 ? 348 ASP C N   1 
ATOM   7397  C  CA  . ASP C 1 332 ? 120.805 151.099 142.384 1.00 124.61 ? 348 ASP C CA  1 
ATOM   7398  C  C   . ASP C 1 332 ? 121.636 150.997 143.662 1.00 124.61 ? 348 ASP C C   1 
ATOM   7399  O  O   . ASP C 1 332 ? 121.187 150.469 144.682 1.00 124.61 ? 348 ASP C O   1 
ATOM   7400  C  CB  . ASP C 1 332 ? 119.589 150.168 142.434 1.00 124.61 ? 348 ASP C CB  1 
ATOM   7401  C  CG  . ASP C 1 332 ? 118.450 150.732 143.263 1.00 124.61 ? 348 ASP C CG  1 
ATOM   7402  O  OD1 . ASP C 1 332 ? 118.715 151.441 144.255 1.00 124.61 ? 348 ASP C OD1 1 
ATOM   7403  O  OD2 . ASP C 1 332 ? 117.281 150.464 142.918 1.00 124.61 ? 348 ASP C OD2 1 
ATOM   7404  N  N   . ALA C 1 333 ? 122.869 151.495 143.603 1.00 114.88 ? 349 ALA C N   1 
ATOM   7405  C  CA  . ALA C 1 333 ? 123.827 151.319 144.684 1.00 114.88 ? 349 ALA C CA  1 
ATOM   7406  C  C   . ALA C 1 333 ? 124.473 152.649 145.039 1.00 114.88 ? 349 ALA C C   1 
ATOM   7407  O  O   . ALA C 1 333 ? 124.802 153.449 144.160 1.00 114.88 ? 349 ALA C O   1 
ATOM   7408  C  CB  . ALA C 1 333 ? 124.907 150.301 144.303 1.00 114.88 ? 349 ALA C CB  1 
ATOM   7409  N  N   . ILE C 1 334 ? 124.682 152.869 146.332 1.00 103.10 ? 350 ILE C N   1 
ATOM   7410  C  CA  . ILE C 1 334 ? 125.358 154.074 146.810 1.00 103.10 ? 350 ILE C CA  1 
ATOM   7411  C  C   . ILE C 1 334 ? 126.729 153.687 147.343 1.00 103.10 ? 350 ILE C C   1 
ATOM   7412  O  O   . ILE C 1 334 ? 126.832 152.959 148.332 1.00 103.10 ? 350 ILE C O   1 
ATOM   7413  C  CB  . ILE C 1 334 ? 124.536 154.794 147.890 1.00 103.10 ? 350 ILE C CB  1 
ATOM   7414  C  CG1 . ILE C 1 334 ? 123.191 155.250 147.323 1.00 103.10 ? 350 ILE C CG1 1 
ATOM   7415  C  CG2 . ILE C 1 334 ? 125.315 155.971 148.458 1.00 103.10 ? 350 ILE C CG2 1 
ATOM   7416  C  CD1 . ILE C 1 334 ? 122.331 155.994 148.319 1.00 103.10 ? 350 ILE C CD1 1 
ATOM   7417  N  N   . TYR C 1 335 ? 127.779 154.230 146.746 1.00 96.40  ? 351 TYR C N   1 
ATOM   7418  C  CA  . TYR C 1 335 ? 129.131 153.840 147.107 1.00 96.40  ? 351 TYR C CA  1 
ATOM   7419  C  C   . TYR C 1 335 ? 129.764 154.826 148.080 1.00 96.40  ? 351 TYR C C   1 
ATOM   7420  O  O   . TYR C 1 335 ? 129.490 156.028 148.055 1.00 96.40  ? 351 TYR C O   1 
ATOM   7421  C  CB  . TYR C 1 335 ? 130.014 153.705 145.865 1.00 96.40  ? 351 TYR C CB  1 
ATOM   7422  C  CG  . TYR C 1 335 ? 129.930 152.346 145.214 1.00 96.40  ? 351 TYR C CG  1 
ATOM   7423  C  CD1 . TYR C 1 335 ? 128.813 151.968 144.481 1.00 96.40  ? 351 TYR C CD1 1 
ATOM   7424  C  CD2 . TYR C 1 335 ? 130.962 151.430 145.356 1.00 96.40  ? 351 TYR C CD2 1 
ATOM   7425  C  CE1 . TYR C 1 335 ? 128.737 150.717 143.893 1.00 96.40  ? 351 TYR C CE1 1 
ATOM   7426  C  CE2 . TYR C 1 335 ? 130.895 150.183 144.776 1.00 96.40  ? 351 TYR C CE2 1 
ATOM   7427  C  CZ  . TYR C 1 335 ? 129.783 149.829 144.047 1.00 96.40  ? 351 TYR C CZ  1 
ATOM   7428  O  OH  . TYR C 1 335 ? 129.721 148.581 143.475 1.00 96.40  ? 351 TYR C OH  1 
ATOM   7429  N  N   . SER C 1 336 ? 130.617 154.285 148.945 1.00 89.20  ? 352 SER C N   1 
ATOM   7430  C  CA  . SER C 1 336 ? 131.406 155.038 149.914 1.00 89.20  ? 352 SER C CA  1 
ATOM   7431  C  C   . SER C 1 336 ? 132.850 154.596 149.708 1.00 89.20  ? 352 SER C C   1 
ATOM   7432  O  O   . SER C 1 336 ? 133.219 153.471 150.069 1.00 89.20  ? 352 SER C O   1 
ATOM   7433  C  CB  . SER C 1 336 ? 130.935 154.784 151.341 1.00 89.20  ? 352 SER C CB  1 
ATOM   7434  O  OG  . SER C 1 336 ? 131.877 155.268 152.281 1.00 89.20  ? 352 SER C OG  1 
ATOM   7435  N  N   . LEU C 1 337 ? 133.632 155.449 149.052 1.00 80.06  ? 353 LEU C N   1 
ATOM   7436  C  CA  . LEU C 1 337 ? 135.015 155.164 148.709 1.00 80.06  ? 353 LEU C CA  1 
ATOM   7437  C  C   . LEU C 1 337 ? 135.956 156.011 149.556 1.00 80.06  ? 353 LEU C C   1 
ATOM   7438  O  O   . LEU C 1 337 ? 135.588 157.075 150.063 1.00 80.06  ? 353 LEU C O   1 
ATOM   7439  C  CB  . LEU C 1 337 ? 135.281 155.429 147.222 1.00 80.06  ? 353 LEU C CB  1 
ATOM   7440  C  CG  . LEU C 1 337 ? 134.415 154.696 146.197 1.00 80.06  ? 353 LEU C CG  1 
ATOM   7441  C  CD1 . LEU C 1 337 ? 133.173 155.505 145.862 1.00 80.06  ? 353 LEU C CD1 1 
ATOM   7442  C  CD2 . LEU C 1 337 ? 135.212 154.387 144.940 1.00 80.06  ? 353 LEU C CD2 1 
ATOM   7443  N  N   . GLY C 1 338 ? 137.188 155.527 149.689 1.00 89.74  ? 354 GLY C N   1 
ATOM   7444  C  CA  . GLY C 1 338 ? 138.247 156.241 150.372 1.00 89.74  ? 354 GLY C CA  1 
ATOM   7445  C  C   . GLY C 1 338 ? 137.918 156.519 151.826 1.00 89.74  ? 354 GLY C C   1 
ATOM   7446  O  O   . GLY C 1 338 ? 137.236 155.746 152.506 1.00 89.74  ? 354 GLY C O   1 
ATOM   7447  N  N   . GLY C 1 339 ? 138.413 157.649 152.308 1.00 94.54  ? 355 GLY C N   1 
ATOM   7448  C  CA  . GLY C 1 339 ? 138.145 158.120 153.650 1.00 94.54  ? 355 GLY C CA  1 
ATOM   7449  C  C   . GLY C 1 339 ? 139.399 158.150 154.508 1.00 94.54  ? 355 GLY C C   1 
ATOM   7450  O  O   . GLY C 1 339 ? 140.438 157.574 154.183 1.00 94.54  ? 355 GLY C O   1 
ATOM   7451  N  N   . LYS C 1 340 ? 139.276 158.855 155.630 1.00 91.91  ? 356 LYS C N   1 
ATOM   7452  C  CA  . LYS C 1 340 ? 140.340 158.971 156.617 1.00 91.91  ? 356 LYS C CA  1 
ATOM   7453  C  C   . LYS C 1 340 ? 139.853 158.370 157.927 1.00 91.91  ? 356 LYS C C   1 
ATOM   7454  O  O   . LYS C 1 340 ? 138.789 158.747 158.428 1.00 91.91  ? 356 LYS C O   1 
ATOM   7455  C  CB  . LYS C 1 340 ? 140.763 160.432 156.804 1.00 91.91  ? 356 LYS C CB  1 
ATOM   7456  C  CG  . LYS C 1 340 ? 141.121 160.818 158.230 1.00 91.91  ? 356 LYS C CG  1 
ATOM   7457  C  CD  . LYS C 1 340 ? 141.545 162.275 158.311 1.00 91.91  ? 356 LYS C CD  1 
ATOM   7458  C  CE  . LYS C 1 340 ? 142.717 162.564 157.386 1.00 91.91  ? 356 LYS C CE  1 
ATOM   7459  N  NZ  . LYS C 1 340 ? 143.195 163.968 157.523 1.00 91.91  ? 356 LYS C NZ  1 
ATOM   7460  N  N   . THR C 1 341 ? 140.619 157.427 158.467 1.00 100.20 ? 357 THR C N   1 
ATOM   7461  C  CA  . THR C 1 341 ? 140.244 156.785 159.716 1.00 100.20 ? 357 THR C CA  1 
ATOM   7462  C  C   . THR C 1 341 ? 140.437 157.741 160.892 1.00 100.20 ? 357 THR C C   1 
ATOM   7463  O  O   . THR C 1 341 ? 141.100 158.776 160.792 1.00 100.20 ? 357 THR C O   1 
ATOM   7464  C  CB  . THR C 1 341 ? 141.058 155.511 159.935 1.00 100.20 ? 357 THR C CB  1 
ATOM   7465  O  OG1 . THR C 1 341 ? 142.427 155.852 160.183 1.00 100.20 ? 357 THR C OG1 1 
ATOM   7466  C  CG2 . THR C 1 341 ? 140.980 154.619 158.713 1.00 100.20 ? 357 THR C CG2 1 
ATOM   7467  N  N   . LEU C 1 342 ? 139.842 157.374 162.029 1.00 104.83 ? 358 LEU C N   1 
ATOM   7468  C  CA  . LEU C 1 342 ? 139.959 158.181 163.239 1.00 104.83 ? 358 LEU C CA  1 
ATOM   7469  C  C   . LEU C 1 342 ? 141.359 158.147 163.834 1.00 104.83 ? 358 LEU C C   1 
ATOM   7470  O  O   . LEU C 1 342 ? 141.638 158.914 164.761 1.00 104.83 ? 358 LEU C O   1 
ATOM   7471  C  CB  . LEU C 1 342 ? 138.944 157.717 164.287 1.00 104.83 ? 358 LEU C CB  1 
ATOM   7472  C  CG  . LEU C 1 342 ? 137.531 158.312 164.268 1.00 104.83 ? 358 LEU C CG  1 
ATOM   7473  C  CD1 . LEU C 1 342 ? 137.555 159.756 164.746 1.00 104.83 ? 358 LEU C CD1 1 
ATOM   7474  C  CD2 . LEU C 1 342 ? 136.876 158.206 162.896 1.00 104.83 ? 358 LEU C CD2 1 
ATOM   7475  N  N   . GLN C 1 343 ? 142.239 157.281 163.332 1.00 128.07 ? 359 GLN C N   1 
ATOM   7476  C  CA  . GLN C 1 343 ? 143.627 157.227 163.762 1.00 128.07 ? 359 GLN C CA  1 
ATOM   7477  C  C   . GLN C 1 343 ? 144.541 158.076 162.887 1.00 128.07 ? 359 GLN C C   1 
ATOM   7478  O  O   . GLN C 1 343 ? 145.751 157.826 162.847 1.00 128.07 ? 359 GLN C O   1 
ATOM   7479  C  CB  . GLN C 1 343 ? 144.124 155.778 163.787 1.00 128.07 ? 359 GLN C CB  1 
ATOM   7480  C  CG  . GLN C 1 343 ? 143.545 154.919 164.905 1.00 128.07 ? 359 GLN C CG  1 
ATOM   7481  C  CD  . GLN C 1 343 ? 142.077 154.599 164.711 1.00 128.07 ? 359 GLN C CD  1 
ATOM   7482  O  OE1 . GLN C 1 343 ? 141.654 154.212 163.623 1.00 128.07 ? 359 GLN C OE1 1 
ATOM   7483  N  NE2 . GLN C 1 343 ? 141.292 154.758 165.770 1.00 128.07 ? 359 GLN C NE2 1 
ATOM   7484  N  N   . ASP C 1 344 ? 143.983 159.061 162.177 1.00 124.26 ? 360 ASP C N   1 
ATOM   7485  C  CA  . ASP C 1 344 ? 144.744 159.940 161.288 1.00 124.26 ? 360 ASP C CA  1 
ATOM   7486  C  C   . ASP C 1 344 ? 145.421 159.162 160.164 1.00 124.26 ? 360 ASP C C   1 
ATOM   7487  O  O   . ASP C 1 344 ? 146.479 159.559 159.670 1.00 124.26 ? 360 ASP C O   1 
ATOM   7488  C  CB  . ASP C 1 344 ? 145.772 160.769 162.064 1.00 124.26 ? 360 ASP C CB  1 
ATOM   7489  N  N   . THR C 1 345 ? 144.817 158.051 159.751 1.00 112.33 ? 361 THR C N   1 
ATOM   7490  C  CA  . THR C 1 345 ? 145.358 157.196 158.705 1.00 112.33 ? 361 THR C CA  1 
ATOM   7491  C  C   . THR C 1 345 ? 144.380 157.154 157.539 1.00 112.33 ? 361 THR C C   1 
ATOM   7492  O  O   . THR C 1 345 ? 143.178 156.953 157.739 1.00 112.33 ? 361 THR C O   1 
ATOM   7493  C  CB  . THR C 1 345 ? 145.622 155.782 159.233 1.00 112.33 ? 361 THR C CB  1 
ATOM   7494  O  OG1 . THR C 1 345 ? 146.759 155.800 160.105 1.00 112.33 ? 361 THR C OG1 1 
ATOM   7495  C  CG2 . THR C 1 345 ? 145.889 154.817 158.088 1.00 112.33 ? 361 THR C CG2 1 
ATOM   7496  N  N   . LEU C 1 346 ? 144.899 157.345 156.330 1.00 103.19 ? 362 LEU C N   1 
ATOM   7497  C  CA  . LEU C 1 346 ? 144.075 157.302 155.131 1.00 103.19 ? 362 LEU C CA  1 
ATOM   7498  C  C   . LEU C 1 346 ? 143.612 155.878 154.848 1.00 103.19 ? 362 LEU C C   1 
ATOM   7499  O  O   . LEU C 1 346 ? 144.263 154.901 155.227 1.00 103.19 ? 362 LEU C O   1 
ATOM   7500  C  CB  . LEU C 1 346 ? 144.849 157.852 153.938 1.00 103.19 ? 362 LEU C CB  1 
ATOM   7501  C  CG  . LEU C 1 346 ? 145.470 159.231 154.159 1.00 103.19 ? 362 LEU C CG  1 
ATOM   7502  C  CD1 . LEU C 1 346 ? 146.030 159.756 152.861 1.00 103.19 ? 362 LEU C CD1 1 
ATOM   7503  C  CD2 . LEU C 1 346 ? 144.449 160.200 154.730 1.00 103.19 ? 362 LEU C CD2 1 
ATOM   7504  N  N   . SER C 1 347 ? 142.473 155.766 154.170 1.00 103.42 ? 363 SER C N   1 
ATOM   7505  C  CA  . SER C 1 347 ? 141.865 154.477 153.885 1.00 103.42 ? 363 SER C CA  1 
ATOM   7506  C  C   . SER C 1 347 ? 141.654 154.281 152.392 1.00 103.42 ? 363 SER C C   1 
ATOM   7507  O  O   . SER C 1 347 ? 141.457 155.241 151.641 1.00 103.42 ? 363 SER C O   1 
ATOM   7508  C  CB  . SER C 1 347 ? 140.519 154.351 154.591 1.00 103.42 ? 363 SER C CB  1 
ATOM   7509  O  OG  . SER C 1 347 ? 139.529 155.131 153.947 1.00 103.42 ? 363 SER C OG  1 
ATOM   7510  N  N   . ASN C 1 348 ? 141.703 153.016 151.969 1.00 100.90 ? 364 ASN C N   1 
ATOM   7511  C  CA  . ASN C 1 348 ? 141.461 152.647 150.580 1.00 100.90 ? 364 ASN C CA  1 
ATOM   7512  C  C   . ASN C 1 348 ? 140.322 151.642 150.448 1.00 100.90 ? 364 ASN C C   1 
ATOM   7513  O  O   . ASN C 1 348 ? 140.224 150.955 149.428 1.00 100.90 ? 364 ASN C O   1 
ATOM   7514  C  CB  . ASN C 1 348 ? 142.736 152.081 149.953 1.00 100.90 ? 364 ASN C CB  1 
ATOM   7515  C  CG  . ASN C 1 348 ? 143.350 150.976 150.787 1.00 100.90 ? 364 ASN C CG  1 
ATOM   7516  O  OD1 . ASN C 1 348 ? 143.065 150.850 151.978 1.00 100.90 ? 364 ASN C OD1 1 
ATOM   7517  N  ND2 . ASN C 1 348 ? 144.200 150.167 150.165 1.00 100.90 ? 364 ASN C ND2 1 
ATOM   7518  N  N   . ALA C 1 349 ? 139.454 151.547 151.451 1.00 90.41  ? 365 ALA C N   1 
ATOM   7519  C  CA  . ALA C 1 349 ? 138.339 150.614 151.403 1.00 90.41  ? 365 ALA C CA  1 
ATOM   7520  C  C   . ALA C 1 349 ? 137.161 151.202 150.637 1.00 90.41  ? 365 ALA C C   1 
ATOM   7521  O  O   . ALA C 1 349 ? 136.957 152.418 150.607 1.00 90.41  ? 365 ALA C O   1 
ATOM   7522  C  CB  . ALA C 1 349 ? 137.899 150.233 152.817 1.00 90.41  ? 365 ALA C CB  1 
ATOM   7523  N  N   . VAL C 1 350 ? 136.379 150.321 150.013 1.00 86.73  ? 366 VAL C N   1 
ATOM   7524  C  CA  . VAL C 1 350 ? 135.211 150.721 149.237 1.00 86.73  ? 366 VAL C CA  1 
ATOM   7525  C  C   . VAL C 1 350 ? 134.034 149.858 149.671 1.00 86.73  ? 366 VAL C C   1 
ATOM   7526  O  O   . VAL C 1 350 ? 134.156 148.629 149.765 1.00 86.73  ? 366 VAL C O   1 
ATOM   7527  C  CB  . VAL C 1 350 ? 135.449 150.586 147.720 1.00 86.73  ? 366 VAL C CB  1 
ATOM   7528  C  CG1 . VAL C 1 350 ? 134.241 151.090 146.950 1.00 86.73  ? 366 VAL C CG1 1 
ATOM   7529  C  CG2 . VAL C 1 350 ? 136.702 151.340 147.302 1.00 86.73  ? 366 VAL C CG2 1 
ATOM   7530  N  N   . ILE C 1 351 ? 132.893 150.499 149.930 1.00 94.23  ? 367 ILE C N   1 
ATOM   7531  C  CA  . ILE C 1 351 ? 131.675 149.794 150.307 1.00 94.23  ? 367 ILE C CA  1 
ATOM   7532  C  C   . ILE C 1 351 ? 130.536 150.348 149.460 1.00 94.23  ? 367 ILE C C   1 
ATOM   7533  O  O   . ILE C 1 351 ? 130.620 151.452 148.926 1.00 94.23  ? 367 ILE C O   1 
ATOM   7534  C  CB  . ILE C 1 351 ? 131.389 149.931 151.818 1.00 94.23  ? 367 ILE C CB  1 
ATOM   7535  C  CG1 . ILE C 1 351 ? 132.489 149.238 152.606 1.00 94.23  ? 367 ILE C CG1 1 
ATOM   7536  C  CG2 . ILE C 1 351 ? 130.108 149.236 152.218 1.00 94.23  ? 367 ILE C CG2 1 
ATOM   7537  C  CD1 . ILE C 1 351 ? 132.431 149.541 154.049 1.00 94.23  ? 367 ILE C CD1 1 
ATOM   7538  N  N   . TYR C 1 352 ? 129.474 149.559 149.303 1.00 96.96  ? 368 TYR C N   1 
ATOM   7539  C  CA  . TYR C 1 352 ? 128.314 150.039 148.568 1.00 96.96  ? 368 TYR C CA  1 
ATOM   7540  C  C   . TYR C 1 352 ? 127.011 149.576 149.202 1.00 96.96  ? 368 TYR C C   1 
ATOM   7541  O  O   . TYR C 1 352 ? 126.908 148.455 149.700 1.00 96.96  ? 368 TYR C O   1 
ATOM   7542  C  CB  . TYR C 1 352 ? 128.382 149.589 147.102 1.00 96.96  ? 368 TYR C CB  1 
ATOM   7543  C  CG  . TYR C 1 352 ? 128.110 148.119 146.856 1.00 96.96  ? 368 TYR C CG  1 
ATOM   7544  C  CD1 . TYR C 1 352 ? 126.818 147.647 146.661 1.00 96.96  ? 368 TYR C CD1 1 
ATOM   7545  C  CD2 . TYR C 1 352 ? 129.154 147.205 146.808 1.00 96.96  ? 368 TYR C CD2 1 
ATOM   7546  C  CE1 . TYR C 1 352 ? 126.576 146.306 146.433 1.00 96.96  ? 368 TYR C CE1 1 
ATOM   7547  C  CE2 . TYR C 1 352 ? 128.921 145.864 146.581 1.00 96.96  ? 368 TYR C CE2 1 
ATOM   7548  C  CZ  . TYR C 1 352 ? 127.630 145.420 146.394 1.00 96.96  ? 368 TYR C CZ  1 
ATOM   7549  O  OH  . TYR C 1 352 ? 127.395 144.084 146.167 1.00 96.96  ? 368 TYR C OH  1 
ATOM   7550  N  N   . TYR C 1 353 ? 126.016 150.450 149.142 1.00 96.81  ? 369 TYR C N   1 
ATOM   7551  C  CA  . TYR C 1 353 ? 124.683 150.272 149.688 1.00 96.81  ? 369 TYR C CA  1 
ATOM   7552  C  C   . TYR C 1 353 ? 123.738 149.853 148.577 1.00 96.81  ? 369 TYR C C   1 
ATOM   7553  O  O   . TYR C 1 353 ? 123.957 150.171 147.404 1.00 96.81  ? 369 TYR C O   1 
ATOM   7554  C  CB  . TYR C 1 353 ? 124.204 151.582 150.323 1.00 96.81  ? 369 TYR C CB  1 
ATOM   7555  C  CG  . TYR C 1 353 ? 122.837 151.550 150.969 1.00 96.81  ? 369 TYR C CG  1 
ATOM   7556  C  CD1 . TYR C 1 353 ? 122.641 150.984 152.219 1.00 96.81  ? 369 TYR C CD1 1 
ATOM   7557  C  CD2 . TYR C 1 353 ? 121.744 152.122 150.331 1.00 96.81  ? 369 TYR C CD2 1 
ATOM   7558  C  CE1 . TYR C 1 353 ? 121.390 150.971 152.807 1.00 96.81  ? 369 TYR C CE1 1 
ATOM   7559  C  CE2 . TYR C 1 353 ? 120.493 152.114 150.909 1.00 96.81  ? 369 TYR C CE2 1 
ATOM   7560  C  CZ  . TYR C 1 353 ? 120.320 151.537 152.147 1.00 96.81  ? 369 TYR C CZ  1 
ATOM   7561  O  OH  . TYR C 1 353 ? 119.073 151.528 152.725 1.00 96.81  ? 369 TYR C OH  1 
ATOM   7562  N  N   . ARG C 1 354 ? 122.603 149.293 148.986 1.00 110.61 ? 370 ARG C N   1 
ATOM   7563  C  CA  . ARG C 1 354 ? 121.539 148.893 148.073 1.00 110.61 ? 370 ARG C CA  1 
ATOM   7564  C  C   . ARG C 1 354 ? 120.218 149.431 148.594 1.00 110.61 ? 370 ARG C C   1 
ATOM   7565  O  O   . ARG C 1 354 ? 119.780 149.048 149.681 1.00 110.61 ? 370 ARG C O   1 
ATOM   7566  C  CB  . ARG C 1 354 ? 121.467 147.367 147.954 1.00 110.61 ? 370 ARG C CB  1 
ATOM   7567  C  CG  . ARG C 1 354 ? 121.704 146.802 146.566 1.00 110.61 ? 370 ARG C CG  1 
ATOM   7568  C  CD  . ARG C 1 354 ? 123.118 147.069 146.089 1.00 110.61 ? 370 ARG C CD  1 
ATOM   7569  N  NE  . ARG C 1 354 ? 123.339 146.551 144.745 1.00 110.61 ? 370 ARG C NE  1 
ATOM   7570  C  CZ  . ARG C 1 354 ? 123.751 145.318 144.480 1.00 110.61 ? 370 ARG C CZ  1 
ATOM   7571  N  NH1 . ARG C 1 354 ? 123.970 144.440 145.446 1.00 110.61 ? 370 ARG C NH1 1 
ATOM   7572  N  NH2 . ARG C 1 354 ? 123.939 144.954 143.215 1.00 110.61 ? 370 ARG C NH2 1 
ATOM   7573  N  N   . VAL C 1 355 ? 119.591 150.324 147.827 1.00 119.35 ? 371 VAL C N   1 
ATOM   7574  C  CA  . VAL C 1 355 ? 118.318 150.899 148.253 1.00 119.35 ? 371 VAL C CA  1 
ATOM   7575  C  C   . VAL C 1 355 ? 117.245 149.821 148.332 1.00 119.35 ? 371 VAL C C   1 
ATOM   7576  O  O   . VAL C 1 355 ? 116.457 149.776 149.284 1.00 119.35 ? 371 VAL C O   1 
ATOM   7577  C  CB  . VAL C 1 355 ? 117.902 152.045 147.312 1.00 119.35 ? 371 VAL C CB  1 
ATOM   7578  C  CG1 . VAL C 1 355 ? 116.710 152.792 147.885 1.00 119.35 ? 371 VAL C CG1 1 
ATOM   7579  C  CG2 . VAL C 1 355 ? 119.068 152.994 147.088 1.00 119.35 ? 371 VAL C CG2 1 
ATOM   7580  N  N   . GLY C 1 356 ? 117.195 148.937 147.334 1.00 119.49 ? 372 GLY C N   1 
ATOM   7581  C  CA  . GLY C 1 356 ? 116.180 147.896 147.330 1.00 119.49 ? 372 GLY C CA  1 
ATOM   7582  C  C   . GLY C 1 356 ? 116.351 146.892 148.455 1.00 119.49 ? 372 GLY C C   1 
ATOM   7583  O  O   . GLY C 1 356 ? 115.375 146.500 149.100 1.00 119.49 ? 372 GLY C O   1 
ATOM   7584  N  N   . ASP C 1 357 ? 117.587 146.465 148.709 1.00 109.78 ? 373 ASP C N   1 
ATOM   7585  C  CA  . ASP C 1 357 ? 117.845 145.441 149.713 1.00 109.78 ? 373 ASP C CA  1 
ATOM   7586  C  C   . ASP C 1 357 ? 118.176 146.018 151.082 1.00 109.78 ? 373 ASP C C   1 
ATOM   7587  O  O   . ASP C 1 357 ? 118.072 145.297 152.081 1.00 109.78 ? 373 ASP C O   1 
ATOM   7588  C  CB  . ASP C 1 357 ? 118.989 144.529 149.257 1.00 109.78 ? 373 ASP C CB  1 
ATOM   7589  N  N   . ASN C 1 358 ? 118.579 147.288 151.144 1.00 100.41 ? 374 ASN C N   1 
ATOM   7590  C  CA  . ASN C 1 358 ? 118.919 147.970 152.392 1.00 100.41 ? 374 ASN C CA  1 
ATOM   7591  C  C   . ASN C 1 358 ? 120.062 147.235 153.099 1.00 100.41 ? 374 ASN C C   1 
ATOM   7592  O  O   . ASN C 1 358 ? 119.961 146.825 154.257 1.00 100.41 ? 374 ASN C O   1 
ATOM   7593  C  CB  . ASN C 1 358 ? 117.676 148.102 153.284 1.00 100.41 ? 374 ASN C CB  1 
ATOM   7594  C  CG  . ASN C 1 358 ? 117.878 149.046 154.459 1.00 100.41 ? 374 ASN C CG  1 
ATOM   7595  O  OD1 . ASN C 1 358 ? 118.984 149.215 154.963 1.00 100.41 ? 374 ASN C OD1 1 
ATOM   7596  N  ND2 . ASN C 1 358 ? 116.792 149.669 154.900 1.00 100.41 ? 374 ASN C ND2 1 
ATOM   7597  N  N   . VAL C 1 359 ? 121.158 147.054 152.360 1.00 96.77  ? 375 VAL C N   1 
ATOM   7598  C  CA  . VAL C 1 359 ? 122.348 146.381 152.869 1.00 96.77  ? 375 VAL C CA  1 
ATOM   7599  C  C   . VAL C 1 359 ? 123.593 147.094 152.359 1.00 96.77  ? 375 VAL C C   1 
ATOM   7600  O  O   . VAL C 1 359 ? 123.579 147.737 151.302 1.00 96.77  ? 375 VAL C O   1 
ATOM   7601  C  CB  . VAL C 1 359 ? 122.395 144.887 152.468 1.00 96.77  ? 375 VAL C CB  1 
ATOM   7602  C  CG1 . VAL C 1 359 ? 121.237 144.116 153.085 1.00 96.77  ? 375 VAL C CG1 1 
ATOM   7603  C  CG2 . VAL C 1 359 ? 122.394 144.741 150.954 1.00 96.77  ? 375 VAL C CG2 1 
ATOM   7604  N  N   . TRP C 1 360 ? 124.674 146.973 153.129 1.00 93.54  ? 376 TRP C N   1 
ATOM   7605  C  CA  . TRP C 1 360 ? 125.987 147.496 152.773 1.00 93.54  ? 376 TRP C CA  1 
ATOM   7606  C  C   . TRP C 1 360 ? 126.934 146.322 152.546 1.00 93.54  ? 376 TRP C C   1 
ATOM   7607  O  O   . TRP C 1 360 ? 126.991 145.403 153.369 1.00 93.54  ? 376 TRP C O   1 
ATOM   7608  C  CB  . TRP C 1 360 ? 126.542 148.400 153.877 1.00 93.54  ? 376 TRP C CB  1 
ATOM   7609  C  CG  . TRP C 1 360 ? 125.954 149.785 153.931 1.00 93.54  ? 376 TRP C CG  1 
ATOM   7610  C  CD1 . TRP C 1 360 ? 124.908 150.193 154.705 1.00 93.54  ? 376 TRP C CD1 1 
ATOM   7611  C  CD2 . TRP C 1 360 ? 126.367 150.935 153.180 1.00 93.54  ? 376 TRP C CD2 1 
ATOM   7612  N  NE1 . TRP C 1 360 ? 124.653 151.524 154.495 1.00 93.54  ? 376 TRP C NE1 1 
ATOM   7613  C  CE2 . TRP C 1 360 ? 125.531 152.003 153.559 1.00 93.54  ? 376 TRP C CE2 1 
ATOM   7614  C  CE3 . TRP C 1 360 ? 127.360 151.166 152.225 1.00 93.54  ? 376 TRP C CE3 1 
ATOM   7615  C  CZ2 . TRP C 1 360 ? 125.659 153.280 153.019 1.00 93.54  ? 376 TRP C CZ2 1 
ATOM   7616  C  CZ3 . TRP C 1 360 ? 127.487 152.435 151.691 1.00 93.54  ? 376 TRP C CZ3 1 
ATOM   7617  C  CH2 . TRP C 1 360 ? 126.640 153.475 152.088 1.00 93.54  ? 376 TRP C CH2 1 
ATOM   7618  N  N   . THR C 1 361 ? 127.674 146.352 151.440 1.00 87.67  ? 377 THR C N   1 
ATOM   7619  C  CA  . THR C 1 361 ? 128.576 145.270 151.061 1.00 87.67  ? 377 THR C CA  1 
ATOM   7620  C  C   . THR C 1 361 ? 129.950 145.842 150.736 1.00 87.67  ? 377 THR C C   1 
ATOM   7621  O  O   . THR C 1 361 ? 130.056 146.820 149.991 1.00 87.67  ? 377 THR C O   1 
ATOM   7622  C  CB  . THR C 1 361 ? 128.023 144.493 149.859 1.00 87.67  ? 377 THR C CB  1 
ATOM   7623  O  OG1 . THR C 1 361 ? 126.845 143.778 150.254 1.00 87.67  ? 377 THR C OG1 1 
ATOM   7624  C  CG2 . THR C 1 361 ? 129.051 143.503 149.337 1.00 87.67  ? 377 THR C CG2 1 
ATOM   7625  N  N   . GLU C 1 362 ? 130.995 145.226 151.286 1.00 102.66 ? 378 GLU C N   1 
ATOM   7626  C  CA  . GLU C 1 362 ? 132.366 145.613 150.985 1.00 102.66 ? 378 GLU C CA  1 
ATOM   7627  C  C   . GLU C 1 362 ? 132.771 145.128 149.594 1.00 102.66 ? 378 GLU C C   1 
ATOM   7628  O  O   . GLU C 1 362 ? 132.203 144.178 149.050 1.00 102.66 ? 378 GLU C O   1 
ATOM   7629  C  CB  . GLU C 1 362 ? 133.326 145.039 152.028 1.00 102.66 ? 378 GLU C CB  1 
ATOM   7630  C  CG  . GLU C 1 362 ? 133.178 145.632 153.418 1.00 102.66 ? 378 GLU C CG  1 
ATOM   7631  C  CD  . GLU C 1 362 ? 134.355 146.505 153.803 1.00 102.66 ? 378 GLU C CD  1 
ATOM   7632  O  OE1 . GLU C 1 362 ? 135.221 146.752 152.938 1.00 102.66 ? 378 GLU C OE1 1 
ATOM   7633  O  OE2 . GLU C 1 362 ? 134.417 146.943 154.971 1.00 102.66 ? 378 GLU C OE2 1 
ATOM   7634  N  N   . THR C 1 363 ? 133.769 145.788 149.017 1.00 90.99  ? 379 THR C N   1 
ATOM   7635  C  CA  . THR C 1 363 ? 134.225 145.409 147.681 1.00 90.99  ? 379 THR C CA  1 
ATOM   7636  C  C   . THR C 1 363 ? 135.720 145.700 147.583 1.00 90.99  ? 379 THR C C   1 
ATOM   7637  O  O   . THR C 1 363 ? 136.398 145.871 148.601 1.00 90.99  ? 379 THR C O   1 
ATOM   7638  C  CB  . THR C 1 363 ? 133.396 146.122 146.598 1.00 90.99  ? 379 THR C CB  1 
ATOM   7639  O  OG1 . THR C 1 363 ? 133.960 145.852 145.309 1.00 90.99  ? 379 THR C OG1 1 
ATOM   7640  C  CG2 . THR C 1 363 ? 133.379 147.615 146.833 1.00 90.99  ? 379 THR C CG2 1 
ATOM   7641  N  N   . THR C 1 364 ? 136.236 145.741 146.355 1.00 97.27  ? 380 THR C N   1 
ATOM   7642  C  CA  . THR C 1 364 ? 137.672 145.856 146.136 1.00 97.27  ? 380 THR C CA  1 
ATOM   7643  C  C   . THR C 1 364 ? 138.205 147.166 146.706 1.00 97.27  ? 380 THR C C   1 
ATOM   7644  O  O   . THR C 1 364 ? 137.507 148.182 146.754 1.00 97.27  ? 380 THR C O   1 
ATOM   7645  C  CB  . THR C 1 364 ? 137.988 145.769 144.641 1.00 97.27  ? 380 THR C CB  1 
ATOM   7646  O  OG1 . THR C 1 364 ? 137.193 144.737 144.044 1.00 97.27  ? 380 THR C OG1 1 
ATOM   7647  C  CG2 . THR C 1 364 ? 139.458 145.451 144.417 1.00 97.27  ? 380 THR C CG2 1 
ATOM   7648  N  N   . GLN C 1 365 ? 139.460 147.133 147.141 1.00 103.95 ? 381 GLN C N   1 
ATOM   7649  C  CA  . GLN C 1 365 ? 140.102 148.287 147.747 1.00 103.95 ? 381 GLN C CA  1 
ATOM   7650  C  C   . GLN C 1 365 ? 140.712 149.198 146.687 1.00 103.95 ? 381 GLN C C   1 
ATOM   7651  O  O   . GLN C 1 365 ? 140.894 148.818 145.529 1.00 103.95 ? 381 GLN C O   1 
ATOM   7652  C  CB  . GLN C 1 365 ? 141.186 147.840 148.729 1.00 103.95 ? 381 GLN C CB  1 
ATOM   7653  C  CG  . GLN C 1 365 ? 140.656 147.230 150.013 1.00 103.95 ? 381 GLN C CG  1 
ATOM   7654  C  CD  . GLN C 1 365 ? 141.760 146.917 151.003 1.00 103.95 ? 381 GLN C CD  1 
ATOM   7655  O  OE1 . GLN C 1 365 ? 142.826 146.428 150.629 1.00 103.95 ? 381 GLN C OE1 1 
ATOM   7656  N  NE2 . GLN C 1 365 ? 141.510 147.198 152.276 1.00 103.95 ? 381 GLN C NE2 1 
ATOM   7657  N  N   . LEU C 1 366 ? 141.029 150.418 147.108 1.00 100.11 ? 382 LEU C N   1 
ATOM   7658  C  CA  . LEU C 1 366 ? 141.661 151.392 146.233 1.00 100.11 ? 382 LEU C CA  1 
ATOM   7659  C  C   . LEU C 1 366 ? 143.169 151.176 146.198 1.00 100.11 ? 382 LEU C C   1 
ATOM   7660  O  O   . LEU C 1 366 ? 143.776 150.724 147.173 1.00 100.11 ? 382 LEU C O   1 
ATOM   7661  C  CB  . LEU C 1 366 ? 141.352 152.815 146.701 1.00 100.11 ? 382 LEU C CB  1 
ATOM   7662  C  CG  . LEU C 1 366 ? 139.892 153.271 146.675 1.00 100.11 ? 382 LEU C CG  1 
ATOM   7663  C  CD1 . LEU C 1 366 ? 139.741 154.589 147.414 1.00 100.11 ? 382 LEU C CD1 1 
ATOM   7664  C  CD2 . LEU C 1 366 ? 139.377 153.395 145.253 1.00 100.11 ? 382 LEU C CD2 1 
ATOM   7665  N  N   . GLU C 1 367 ? 143.772 151.494 145.051 1.00 106.81 ? 383 GLU C N   1 
ATOM   7666  C  CA  . GLU C 1 367 ? 145.217 151.342 144.920 1.00 106.81 ? 383 GLU C CA  1 
ATOM   7667  C  C   . GLU C 1 367 ? 145.958 152.278 145.866 1.00 106.81 ? 383 GLU C C   1 
ATOM   7668  O  O   . GLU C 1 367 ? 146.913 151.868 146.536 1.00 106.81 ? 383 GLU C O   1 
ATOM   7669  C  CB  . GLU C 1 367 ? 145.641 151.591 143.473 1.00 106.81 ? 383 GLU C CB  1 
ATOM   7670  C  CG  . GLU C 1 367 ? 145.103 150.572 142.483 1.00 106.81 ? 383 GLU C CG  1 
ATOM   7671  C  CD  . GLU C 1 367 ? 146.069 149.429 142.242 1.00 106.81 ? 383 GLU C CD  1 
ATOM   7672  O  OE1 . GLU C 1 367 ? 147.275 149.699 142.064 1.00 106.81 ? 383 GLU C OE1 1 
ATOM   7673  O  OE2 . GLU C 1 367 ? 145.626 148.261 142.230 1.00 106.81 ? 383 GLU C OE2 1 
ATOM   7674  N  N   . VAL C 1 368 ? 145.530 153.536 145.940 1.00 93.99  ? 384 VAL C N   1 
ATOM   7675  C  CA  . VAL C 1 368 ? 146.151 154.541 146.795 1.00 93.99  ? 384 VAL C CA  1 
ATOM   7676  C  C   . VAL C 1 368 ? 145.086 155.093 147.732 1.00 93.99  ? 384 VAL C C   1 
ATOM   7677  O  O   . VAL C 1 368 ? 144.008 155.501 147.282 1.00 93.99  ? 384 VAL C O   1 
ATOM   7678  C  CB  . VAL C 1 368 ? 146.793 155.673 145.971 1.00 93.99  ? 384 VAL C CB  1 
ATOM   7679  C  CG1 . VAL C 1 368 ? 147.558 156.623 146.878 1.00 93.99  ? 384 VAL C CG1 1 
ATOM   7680  C  CG2 . VAL C 1 368 ? 147.706 155.101 144.900 1.00 93.99  ? 384 VAL C CG2 1 
ATOM   7681  N  N   . ALA C 1 369 ? 145.387 155.108 149.028 1.00 94.71  ? 385 ALA C N   1 
ATOM   7682  C  CA  . ALA C 1 369 ? 144.451 155.645 150.006 1.00 94.71  ? 385 ALA C CA  1 
ATOM   7683  C  C   . ALA C 1 369 ? 144.400 157.166 149.923 1.00 94.71  ? 385 ALA C C   1 
ATOM   7684  O  O   . ALA C 1 369 ? 145.438 157.833 149.901 1.00 94.71  ? 385 ALA C O   1 
ATOM   7685  C  CB  . ALA C 1 369 ? 144.849 155.205 151.413 1.00 94.71  ? 385 ALA C CB  1 
ATOM   7686  N  N   . VAL C 1 370 ? 143.184 157.716 149.877 1.00 89.80  ? 386 VAL C N   1 
ATOM   7687  C  CA  . VAL C 1 370 ? 142.972 159.157 149.804 1.00 89.80  ? 386 VAL C CA  1 
ATOM   7688  C  C   . VAL C 1 370 ? 141.834 159.539 150.741 1.00 89.80  ? 386 VAL C C   1 
ATOM   7689  O  O   . VAL C 1 370 ? 141.037 158.700 151.165 1.00 89.80  ? 386 VAL C O   1 
ATOM   7690  C  CB  . VAL C 1 370 ? 142.663 159.643 148.371 1.00 89.80  ? 386 VAL C CB  1 
ATOM   7691  C  CG1 . VAL C 1 370 ? 143.870 159.454 147.467 1.00 89.80  ? 386 VAL C CG1 1 
ATOM   7692  C  CG2 . VAL C 1 370 ? 141.458 158.911 147.818 1.00 89.80  ? 386 VAL C CG2 1 
ATOM   7693  N  N   . SER C 1 371 ? 141.771 160.829 151.063 1.00 93.46  ? 387 SER C N   1 
ATOM   7694  C  CA  . SER C 1 371 ? 140.742 161.366 151.942 1.00 93.46  ? 387 SER C CA  1 
ATOM   7695  C  C   . SER C 1 371 ? 140.253 162.693 151.384 1.00 93.46  ? 387 SER C C   1 
ATOM   7696  O  O   . SER C 1 371 ? 141.052 163.513 150.927 1.00 93.46  ? 387 SER C O   1 
ATOM   7697  C  CB  . SER C 1 371 ? 141.268 161.561 153.368 1.00 93.46  ? 387 SER C CB  1 
ATOM   7698  O  OG  . SER C 1 371 ? 140.345 162.296 154.152 1.00 93.46  ? 387 SER C OG  1 
ATOM   7699  N  N   . GLY C 1 372 ? 138.939 162.903 151.431 1.00 83.78  ? 388 GLY C N   1 
ATOM   7700  C  CA  . GLY C 1 372 ? 138.366 164.147 150.961 1.00 83.78  ? 388 GLY C CA  1 
ATOM   7701  C  C   . GLY C 1 372 ? 138.284 164.293 149.460 1.00 83.78  ? 388 GLY C C   1 
ATOM   7702  O  O   . GLY C 1 372 ? 137.964 165.386 148.978 1.00 83.78  ? 388 GLY C O   1 
ATOM   7703  N  N   . ALA C 1 373 ? 138.563 163.234 148.707 1.00 92.15  ? 389 ALA C N   1 
ATOM   7704  C  CA  . ALA C 1 373 ? 138.529 163.303 147.254 1.00 92.15  ? 389 ALA C CA  1 
ATOM   7705  C  C   . ALA C 1 373 ? 137.102 163.475 146.743 1.00 92.15  ? 389 ALA C C   1 
ATOM   7706  O  O   . ALA C 1 373 ? 136.140 162.983 147.336 1.00 92.15  ? 389 ALA C O   1 
ATOM   7707  C  CB  . ALA C 1 373 ? 139.151 162.046 146.649 1.00 92.15  ? 389 ALA C CB  1 
ATOM   7708  N  N   . ALA C 1 374 ? 136.973 164.197 145.632 1.00 103.71 ? 390 ALA C N   1 
ATOM   7709  C  CA  . ALA C 1 374 ? 135.674 164.407 145.007 1.00 103.71 ? 390 ALA C CA  1 
ATOM   7710  C  C   . ALA C 1 374 ? 135.320 163.219 144.120 1.00 103.71 ? 390 ALA C C   1 
ATOM   7711  O  O   . ALA C 1 374 ? 136.153 162.743 143.343 1.00 103.71 ? 390 ALA C O   1 
ATOM   7712  C  CB  . ALA C 1 374 ? 135.678 165.699 144.191 1.00 103.71 ? 390 ALA C CB  1 
ATOM   7713  N  N   . GLY C 1 375 ? 134.088 162.738 144.246 1.00 95.21  ? 391 GLY C N   1 
ATOM   7714  C  CA  . GLY C 1 375 ? 133.610 161.603 143.471 1.00 95.21  ? 391 GLY C CA  1 
ATOM   7715  C  C   . GLY C 1 375 ? 132.807 162.032 142.256 1.00 95.21  ? 391 GLY C C   1 
ATOM   7716  O  O   . GLY C 1 375 ? 132.084 163.027 142.294 1.00 95.21  ? 391 GLY C O   1 
ATOM   7717  N  N   . ALA C 1 376 ? 132.945 161.265 141.176 1.00 107.81 ? 392 ALA C N   1 
ATOM   7718  C  CA  . ALA C 1 376 ? 132.203 161.519 139.943 1.00 107.81 ? 392 ALA C CA  1 
ATOM   7719  C  C   . ALA C 1 376 ? 131.829 160.180 139.322 1.00 107.81 ? 392 ALA C C   1 
ATOM   7720  O  O   . ALA C 1 376 ? 132.709 159.419 138.914 1.00 107.81 ? 392 ALA C O   1 
ATOM   7721  C  CB  . ALA C 1 376 ? 133.021 162.364 138.968 1.00 107.81 ? 392 ALA C CB  1 
ATOM   7722  N  N   . ASN C 1 377 ? 130.533 159.886 139.257 1.00 110.64 ? 393 ASN C N   1 
ATOM   7723  C  CA  . ASN C 1 377 ? 130.052 158.649 138.650 1.00 110.64 ? 393 ASN C CA  1 
ATOM   7724  C  C   . ASN C 1 377 ? 129.766 158.907 137.175 1.00 110.64 ? 393 ASN C C   1 
ATOM   7725  O  O   . ASN C 1 377 ? 128.815 159.618 136.836 1.00 110.64 ? 393 ASN C O   1 
ATOM   7726  C  CB  . ASN C 1 377 ? 128.805 158.146 139.374 1.00 110.64 ? 393 ASN C CB  1 
ATOM   7727  C  CG  . ASN C 1 377 ? 128.026 157.126 138.565 1.00 110.64 ? 393 ASN C CG  1 
ATOM   7728  O  OD1 . ASN C 1 377 ? 128.603 156.309 137.849 1.00 110.64 ? 393 ASN C OD1 1 
ATOM   7729  N  ND2 . ASN C 1 377 ? 126.704 157.170 138.677 1.00 110.64 ? 393 ASN C ND2 1 
ATOM   7730  N  N   . LEU C 1 378 ? 130.588 158.332 136.300 1.00 112.47 ? 394 LEU C N   1 
ATOM   7731  C  CA  . LEU C 1 378 ? 130.420 158.444 134.855 1.00 112.47 ? 394 LEU C CA  1 
ATOM   7732  C  C   . LEU C 1 378 ? 130.175 157.054 134.285 1.00 112.47 ? 394 LEU C C   1 
ATOM   7733  O  O   . LEU C 1 378 ? 131.072 156.205 134.312 1.00 112.47 ? 394 LEU C O   1 
ATOM   7734  C  CB  . LEU C 1 378 ? 131.649 159.084 134.213 1.00 112.47 ? 394 LEU C CB  1 
ATOM   7735  C  CG  . LEU C 1 378 ? 131.573 160.565 133.851 1.00 112.47 ? 394 LEU C CG  1 
ATOM   7736  C  CD1 . LEU C 1 378 ? 132.533 160.857 132.717 1.00 112.47 ? 394 LEU C CD1 1 
ATOM   7737  C  CD2 . LEU C 1 378 ? 130.158 160.940 133.454 1.00 112.47 ? 394 LEU C CD2 1 
ATOM   7738  N  N   . ASN C 1 379 ? 128.967 156.829 133.762 1.00 111.49 ? 395 ASN C N   1 
ATOM   7739  C  CA  . ASN C 1 379 ? 128.607 155.563 133.119 1.00 111.49 ? 395 ASN C CA  1 
ATOM   7740  C  C   . ASN C 1 379 ? 128.872 154.370 134.035 1.00 111.49 ? 395 ASN C C   1 
ATOM   7741  O  O   . ASN C 1 379 ? 129.205 153.276 133.575 1.00 111.49 ? 395 ASN C O   1 
ATOM   7742  C  CB  . ASN C 1 379 ? 129.343 155.392 131.787 1.00 111.49 ? 395 ASN C CB  1 
ATOM   7743  N  N   . GLY C 1 380 ? 128.727 154.576 135.343 1.00 107.23 ? 396 GLY C N   1 
ATOM   7744  C  CA  . GLY C 1 380 ? 128.915 153.528 136.317 1.00 107.23 ? 396 GLY C CA  1 
ATOM   7745  C  C   . GLY C 1 380 ? 130.314 153.437 136.888 1.00 107.23 ? 396 GLY C C   1 
ATOM   7746  O  O   . GLY C 1 380 ? 130.501 152.802 137.931 1.00 107.23 ? 396 GLY C O   1 
ATOM   7747  N  N   . ILE C 1 381 ? 131.297 154.056 136.243 1.00 109.70 ? 397 ILE C N   1 
ATOM   7748  C  CA  . ILE C 1 381 ? 132.671 154.061 136.731 1.00 109.70 ? 397 ILE C CA  1 
ATOM   7749  C  C   . ILE C 1 381 ? 132.840 155.252 137.663 1.00 109.70 ? 397 ILE C C   1 
ATOM   7750  O  O   . ILE C 1 381 ? 132.466 156.379 137.320 1.00 109.70 ? 397 ILE C O   1 
ATOM   7751  C  CB  . ILE C 1 381 ? 133.682 154.120 135.569 1.00 109.70 ? 397 ILE C CB  1 
ATOM   7752  C  CG1 . ILE C 1 381 ? 133.744 152.798 134.788 1.00 109.70 ? 397 ILE C CG1 1 
ATOM   7753  C  CG2 . ILE C 1 381 ? 135.068 154.465 136.088 1.00 109.70 ? 397 ILE C CG2 1 
ATOM   7754  C  CD1 . ILE C 1 381 ? 132.529 152.471 133.938 1.00 109.70 ? 397 ILE C CD1 1 
ATOM   7755  N  N   . ILE C 1 382 ? 133.392 155.007 138.844 1.00 93.76  ? 398 ILE C N   1 
ATOM   7756  C  CA  . ILE C 1 382 ? 133.593 156.058 139.834 1.00 93.76  ? 398 ILE C CA  1 
ATOM   7757  C  C   . ILE C 1 382 ? 134.993 156.631 139.666 1.00 93.76  ? 398 ILE C C   1 
ATOM   7758  O  O   . ILE C 1 382 ? 135.976 155.887 139.616 1.00 93.76  ? 398 ILE C O   1 
ATOM   7759  C  CB  . ILE C 1 382 ? 133.387 155.513 141.256 1.00 93.76  ? 398 ILE C CB  1 
ATOM   7760  C  CG1 . ILE C 1 382 ? 131.995 154.897 141.387 1.00 93.76  ? 398 ILE C CG1 1 
ATOM   7761  C  CG2 . ILE C 1 382 ? 133.584 156.616 142.283 1.00 93.76  ? 398 ILE C CG2 1 
ATOM   7762  C  CD1 . ILE C 1 382 ? 131.735 154.256 142.725 1.00 93.76  ? 398 ILE C CD1 1 
ATOM   7763  N  N   . TYR C 1 383 ? 135.087 157.952 139.564 1.00 101.73 ? 399 TYR C N   1 
ATOM   7764  C  CA  . TYR C 1 383 ? 136.365 158.646 139.502 1.00 101.73 ? 399 TYR C CA  1 
ATOM   7765  C  C   . TYR C 1 383 ? 136.554 159.441 140.786 1.00 101.73 ? 399 TYR C C   1 
ATOM   7766  O  O   . TYR C 1 383 ? 135.707 160.270 141.141 1.00 101.73 ? 399 TYR C O   1 
ATOM   7767  C  CB  . TYR C 1 383 ? 136.447 159.549 138.272 1.00 101.73 ? 399 TYR C CB  1 
ATOM   7768  C  CG  . TYR C 1 383 ? 136.368 158.782 136.974 1.00 101.73 ? 399 TYR C CG  1 
ATOM   7769  C  CD1 . TYR C 1 383 ? 137.507 158.224 136.409 1.00 101.73 ? 399 TYR C CD1 1 
ATOM   7770  C  CD2 . TYR C 1 383 ? 135.159 158.612 136.314 1.00 101.73 ? 399 TYR C CD2 1 
ATOM   7771  C  CE1 . TYR C 1 383 ? 137.444 157.514 135.226 1.00 101.73 ? 399 TYR C CE1 1 
ATOM   7772  C  CE2 . TYR C 1 383 ? 135.087 157.908 135.127 1.00 101.73 ? 399 TYR C CE2 1 
ATOM   7773  C  CZ  . TYR C 1 383 ? 136.233 157.362 134.588 1.00 101.73 ? 399 TYR C CZ  1 
ATOM   7774  O  OH  . TYR C 1 383 ? 136.168 156.660 133.406 1.00 101.73 ? 399 TYR C OH  1 
ATOM   7775  N  N   . LEU C 1 384 ? 137.652 159.163 141.479 1.00 89.78  ? 400 LEU C N   1 
ATOM   7776  C  CA  . LEU C 1 384 ? 138.015 159.809 142.732 1.00 89.78  ? 400 LEU C CA  1 
ATOM   7777  C  C   . LEU C 1 384 ? 139.143 160.791 142.447 1.00 89.78  ? 400 LEU C C   1 
ATOM   7778  O  O   . LEU C 1 384 ? 140.219 160.385 141.994 1.00 89.78  ? 400 LEU C O   1 
ATOM   7779  C  CB  . LEU C 1 384 ? 138.447 158.766 143.763 1.00 89.78  ? 400 LEU C CB  1 
ATOM   7780  C  CG  . LEU C 1 384 ? 137.876 158.900 145.170 1.00 89.78  ? 400 LEU C CG  1 
ATOM   7781  C  CD1 . LEU C 1 384 ? 136.377 158.738 145.104 1.00 89.78  ? 400 LEU C CD1 1 
ATOM   7782  C  CD2 . LEU C 1 384 ? 138.477 157.857 146.090 1.00 89.78  ? 400 LEU C CD2 1 
ATOM   7783  N  N   . LEU C 1 385 ? 138.896 162.074 142.702 1.00 88.94  ? 401 LEU C N   1 
ATOM   7784  C  CA  . LEU C 1 385 ? 139.778 163.145 142.260 1.00 88.94  ? 401 LEU C CA  1 
ATOM   7785  C  C   . LEU C 1 385 ? 140.339 163.895 143.458 1.00 88.94  ? 401 LEU C C   1 
ATOM   7786  O  O   . LEU C 1 385 ? 139.592 164.267 144.369 1.00 88.94  ? 401 LEU C O   1 
ATOM   7787  C  CB  . LEU C 1 385 ? 139.027 164.119 141.350 1.00 88.94  ? 401 LEU C CB  1 
ATOM   7788  C  CG  . LEU C 1 385 ? 138.371 163.527 140.104 1.00 88.94  ? 401 LEU C CG  1 
ATOM   7789  C  CD1 . LEU C 1 385 ? 137.036 164.197 139.831 1.00 88.94  ? 401 LEU C CD1 1 
ATOM   7790  C  CD2 . LEU C 1 385 ? 139.297 163.689 138.917 1.00 88.94  ? 401 LEU C CD2 1 
ATOM   7791  N  N   . GLY C 1 386 ? 141.651 164.131 143.441 1.00 94.68  ? 402 GLY C N   1 
ATOM   7792  C  CA  . GLY C 1 386 ? 142.271 164.960 144.455 1.00 94.68  ? 402 GLY C CA  1 
ATOM   7793  C  C   . GLY C 1 386 ? 142.217 164.358 145.847 1.00 94.68  ? 402 GLY C C   1 
ATOM   7794  O  O   . GLY C 1 386 ? 142.262 163.140 146.040 1.00 94.68  ? 402 GLY C O   1 
ATOM   7795  N  N   . GLY C 1 387 ? 142.120 165.241 146.837 1.00 102.24 ? 403 GLY C N   1 
ATOM   7796  C  CA  . GLY C 1 387 ? 142.072 164.822 148.220 1.00 102.24 ? 403 GLY C CA  1 
ATOM   7797  C  C   . GLY C 1 387 ? 143.408 164.981 148.912 1.00 102.24 ? 403 GLY C C   1 
ATOM   7798  O  O   . GLY C 1 387 ? 144.143 165.935 148.644 1.00 102.24 ? 403 GLY C O   1 
ATOM   7799  N  N   . GLU C 1 388 ? 143.731 164.055 149.808 1.00 108.76 ? 404 GLU C N   1 
ATOM   7800  C  CA  . GLU C 1 388 ? 144.988 164.075 150.539 1.00 108.76 ? 404 GLU C CA  1 
ATOM   7801  C  C   . GLU C 1 388 ? 145.632 162.704 150.446 1.00 108.76 ? 404 GLU C C   1 
ATOM   7802  O  O   . GLU C 1 388 ? 144.938 161.683 150.434 1.00 108.76 ? 404 GLU C O   1 
ATOM   7803  C  CB  . GLU C 1 388 ? 144.779 164.462 152.008 1.00 108.76 ? 404 GLU C CB  1 
ATOM   7804  C  CG  . GLU C 1 388 ? 143.974 165.734 152.206 1.00 108.76 ? 404 GLU C CG  1 
ATOM   7805  C  CD  . GLU C 1 388 ? 144.604 166.666 153.219 1.00 108.76 ? 404 GLU C CD  1 
ATOM   7806  O  OE1 . GLU C 1 388 ? 144.857 167.839 152.873 1.00 108.76 ? 404 GLU C OE1 1 
ATOM   7807  O  OE2 . GLU C 1 388 ? 144.849 166.224 154.361 1.00 108.76 ? 404 GLU C OE2 1 
ATOM   7808  N  N   . GLU C 1 389 ? 146.959 162.682 150.375 1.00 113.61 ? 405 GLU C N   1 
ATOM   7809  C  CA  . GLU C 1 389 ? 147.697 161.435 150.260 1.00 113.61 ? 405 GLU C CA  1 
ATOM   7810  C  C   . GLU C 1 389 ? 148.838 161.420 151.267 1.00 113.61 ? 405 GLU C C   1 
ATOM   7811  O  O   . GLU C 1 389 ? 149.311 162.466 151.718 1.00 113.61 ? 405 GLU C O   1 
ATOM   7812  C  CB  . GLU C 1 389 ? 148.228 161.225 148.836 1.00 113.61 ? 405 GLU C CB  1 
ATOM   7813  C  CG  . GLU C 1 389 ? 149.191 162.293 148.359 1.00 113.61 ? 405 GLU C CG  1 
ATOM   7814  C  CD  . GLU C 1 389 ? 149.737 162.000 146.977 1.00 113.61 ? 405 GLU C CD  1 
ATOM   7815  O  OE1 . GLU C 1 389 ? 149.299 161.003 146.368 1.00 113.61 ? 405 GLU C OE1 1 
ATOM   7816  O  OE2 . GLU C 1 389 ? 150.601 162.763 146.498 1.00 113.61 ? 405 GLU C OE2 1 
ATOM   7817  N  N   . ASN C 1 390 ? 149.276 160.209 151.613 1.00 119.47 ? 406 ASN C N   1 
ATOM   7818  C  CA  . ASN C 1 390 ? 150.302 160.044 152.635 1.00 119.47 ? 406 ASN C CA  1 
ATOM   7819  C  C   . ASN C 1 390 ? 151.592 160.744 152.229 1.00 119.47 ? 406 ASN C C   1 
ATOM   7820  O  O   . ASN C 1 390 ? 151.975 160.750 151.056 1.00 119.47 ? 406 ASN C O   1 
ATOM   7821  C  CB  . ASN C 1 390 ? 150.566 158.559 152.884 1.00 119.47 ? 406 ASN C CB  1 
ATOM   7822  C  CG  . ASN C 1 390 ? 149.292 157.770 153.103 1.00 119.47 ? 406 ASN C CG  1 
ATOM   7823  O  OD1 . ASN C 1 390 ? 148.680 157.281 152.154 1.00 119.47 ? 406 ASN C OD1 1 
ATOM   7824  N  ND2 . ASN C 1 390 ? 148.885 157.642 154.360 1.00 119.47 ? 406 ASN C ND2 1 
ATOM   7825  N  N   . ASP C 1 391 ? 152.266 161.334 153.213 1.00 123.44 ? 407 ASP C N   1 
ATOM   7826  C  CA  . ASP C 1 391 ? 153.525 162.020 152.973 1.00 123.44 ? 407 ASP C CA  1 
ATOM   7827  C  C   . ASP C 1 391 ? 154.290 162.082 154.286 1.00 123.44 ? 407 ASP C C   1 
ATOM   7828  O  O   . ASP C 1 391 ? 153.690 162.264 155.351 1.00 123.44 ? 407 ASP C O   1 
ATOM   7829  C  CB  . ASP C 1 391 ? 153.290 163.429 152.414 1.00 123.44 ? 407 ASP C CB  1 
ATOM   7830  C  CG  . ASP C 1 391 ? 154.575 164.213 152.237 1.00 123.44 ? 407 ASP C CG  1 
ATOM   7831  O  OD1 . ASP C 1 391 ? 155.647 163.586 152.101 1.00 123.44 ? 407 ASP C OD1 1 
ATOM   7832  O  OD2 . ASP C 1 391 ? 154.507 165.459 152.198 1.00 123.44 ? 407 ASP C OD2 1 
ATOM   7833  N  N   . LEU C 1 392 ? 155.610 161.905 154.201 1.00 115.25 ? 408 LEU C N   1 
ATOM   7834  C  CA  . LEU C 1 392 ? 156.528 162.015 155.334 1.00 115.25 ? 408 LEU C CA  1 
ATOM   7835  C  C   . LEU C 1 392 ? 156.277 160.948 156.396 1.00 115.25 ? 408 LEU C C   1 
ATOM   7836  O  O   . LEU C 1 392 ? 156.718 161.097 157.541 1.00 115.25 ? 408 LEU C O   1 
ATOM   7837  C  CB  . LEU C 1 392 ? 156.480 163.416 155.958 1.00 115.25 ? 408 LEU C CB  1 
ATOM   7838  C  CG  . LEU C 1 392 ? 156.820 164.557 154.996 1.00 115.25 ? 408 LEU C CG  1 
ATOM   7839  C  CD1 . LEU C 1 392 ? 156.636 165.907 155.662 1.00 115.25 ? 408 LEU C CD1 1 
ATOM   7840  C  CD2 . LEU C 1 392 ? 158.231 164.411 154.452 1.00 115.25 ? 408 LEU C CD2 1 
ATOM   7841  N  N   . ASP C 1 393 ? 155.534 159.895 156.039 1.00 109.01 ? 409 ASP C N   1 
ATOM   7842  C  CA  . ASP C 1 393 ? 155.329 158.703 156.864 1.00 109.01 ? 409 ASP C CA  1 
ATOM   7843  C  C   . ASP C 1 393 ? 154.397 158.969 158.041 1.00 109.01 ? 409 ASP C C   1 
ATOM   7844  O  O   . ASP C 1 393 ? 154.035 158.040 158.770 1.00 109.01 ? 409 ASP C O   1 
ATOM   7845  C  CB  . ASP C 1 393 ? 156.663 158.130 157.361 1.00 109.01 ? 409 ASP C CB  1 
ATOM   7846  C  CG  . ASP C 1 393 ? 157.768 158.227 156.325 1.00 109.01 ? 409 ASP C CG  1 
ATOM   7847  O  OD1 . ASP C 1 393 ? 157.525 157.849 155.160 1.00 109.01 ? 409 ASP C OD1 1 
ATOM   7848  O  OD2 . ASP C 1 393 ? 158.876 158.684 156.675 1.00 109.01 ? 409 ASP C OD2 1 
ATOM   7849  N  N   . PHE C 1 394 ? 153.998 160.225 158.235 1.00 100.18 ? 410 PHE C N   1 
ATOM   7850  C  CA  . PHE C 1 394 ? 153.103 160.569 159.333 1.00 100.18 ? 410 PHE C CA  1 
ATOM   7851  C  C   . PHE C 1 394 ? 152.038 161.590 158.970 1.00 100.18 ? 410 PHE C C   1 
ATOM   7852  O  O   . PHE C 1 394 ? 151.083 161.740 159.737 1.00 100.18 ? 410 PHE C O   1 
ATOM   7853  C  CB  . PHE C 1 394 ? 153.898 161.097 160.537 1.00 100.18 ? 410 PHE C CB  1 
ATOM   7854  C  CG  . PHE C 1 394 ? 154.966 160.160 161.021 1.00 100.18 ? 410 PHE C CG  1 
ATOM   7855  C  CD1 . PHE C 1 394 ? 154.651 159.107 161.862 1.00 100.18 ? 410 PHE C CD1 1 
ATOM   7856  C  CD2 . PHE C 1 394 ? 156.286 160.338 160.644 1.00 100.18 ? 410 PHE C CD2 1 
ATOM   7857  C  CE1 . PHE C 1 394 ? 155.631 158.244 162.311 1.00 100.18 ? 410 PHE C CE1 1 
ATOM   7858  C  CE2 . PHE C 1 394 ? 157.271 159.478 161.092 1.00 100.18 ? 410 PHE C CE2 1 
ATOM   7859  C  CZ  . PHE C 1 394 ? 156.942 158.430 161.926 1.00 100.18 ? 410 PHE C CZ  1 
ATOM   7860  N  N   . PHE C 1 395 ? 152.154 162.294 157.845 1.00 97.54  ? 411 PHE C N   1 
ATOM   7861  C  CA  . PHE C 1 395 ? 151.242 163.394 157.564 1.00 97.54  ? 411 PHE C CA  1 
ATOM   7862  C  C   . PHE C 1 395 ? 150.591 163.227 156.200 1.00 97.54  ? 411 PHE C C   1 
ATOM   7863  O  O   . PHE C 1 395 ? 150.775 162.203 155.534 1.00 97.54  ? 411 PHE C O   1 
ATOM   7864  C  CB  . PHE C 1 395 ? 151.976 164.733 157.638 1.00 97.54  ? 411 PHE C CB  1 
ATOM   7865  C  CG  . PHE C 1 395 ? 152.795 164.906 158.882 1.00 97.54  ? 411 PHE C CG  1 
ATOM   7866  C  CD1 . PHE C 1 395 ? 152.212 165.369 160.049 1.00 97.54  ? 411 PHE C CD1 1 
ATOM   7867  C  CD2 . PHE C 1 395 ? 154.145 164.605 158.887 1.00 97.54  ? 411 PHE C CD2 1 
ATOM   7868  C  CE1 . PHE C 1 395 ? 152.961 165.529 161.197 1.00 97.54  ? 411 PHE C CE1 1 
ATOM   7869  C  CE2 . PHE C 1 395 ? 154.899 164.763 160.032 1.00 97.54  ? 411 PHE C CE2 1 
ATOM   7870  C  CZ  . PHE C 1 395 ? 154.306 165.226 161.188 1.00 97.54  ? 411 PHE C CZ  1 
ATOM   7871  N  N   . THR C 1 396 ? 149.845 164.237 155.766 1.00 97.36  ? 412 THR C N   1 
ATOM   7872  C  CA  . THR C 1 396 ? 149.149 164.192 154.493 1.00 97.36  ? 412 THR C CA  1 
ATOM   7873  C  C   . THR C 1 396 ? 149.474 165.443 153.694 1.00 97.36  ? 412 THR C C   1 
ATOM   7874  O  O   . THR C 1 396 ? 149.653 166.530 154.250 1.00 97.36  ? 412 THR C O   1 
ATOM   7875  C  CB  . THR C 1 396 ? 147.627 164.079 154.677 1.00 97.36  ? 412 THR C CB  1 
ATOM   7876  O  OG1 . THR C 1 396 ? 147.168 165.127 155.538 1.00 97.36  ? 412 THR C OG1 1 
ATOM   7877  C  CG2 . THR C 1 396 ? 147.260 162.733 155.282 1.00 97.36  ? 412 THR C CG2 1 
ATOM   7878  N  N   . LYS C 1 397 ? 149.552 165.272 152.381 1.00 101.46 ? 413 LYS C N   1 
ATOM   7879  C  CA  . LYS C 1 397 ? 149.774 166.361 151.452 1.00 101.46 ? 413 LYS C CA  1 
ATOM   7880  C  C   . LYS C 1 397 ? 148.619 166.437 150.463 1.00 101.46 ? 413 LYS C C   1 
ATOM   7881  O  O   . LYS C 1 397 ? 147.974 165.421 150.180 1.00 101.46 ? 413 LYS C O   1 
ATOM   7882  C  CB  . LYS C 1 397 ? 151.096 166.187 150.694 1.00 101.46 ? 413 LYS C CB  1 
ATOM   7883  C  CG  . LYS C 1 397 ? 151.166 164.939 149.834 1.00 101.46 ? 413 LYS C CG  1 
ATOM   7884  C  CD  . LYS C 1 397 ? 152.408 164.942 148.962 1.00 101.46 ? 413 LYS C CD  1 
ATOM   7885  C  CE  . LYS C 1 397 ? 152.885 163.529 148.676 1.00 101.46 ? 413 LYS C CE  1 
ATOM   7886  N  NZ  . LYS C 1 397 ? 153.959 163.504 147.646 1.00 101.46 ? 413 LYS C NZ  1 
ATOM   7887  N  N   . PRO C 1 398 ? 148.320 167.633 149.938 1.00 98.43  ? 414 PRO C N   1 
ATOM   7888  C  CA  . PRO C 1 398 ? 147.277 167.750 148.909 1.00 98.43  ? 414 PRO C CA  1 
ATOM   7889  C  C   . PRO C 1 398 ? 147.519 166.811 147.741 1.00 98.43  ? 414 PRO C C   1 
ATOM   7890  O  O   . PRO C 1 398 ? 148.507 166.953 147.014 1.00 98.43  ? 414 PRO C O   1 
ATOM   7891  C  CB  . PRO C 1 398 ? 147.375 169.218 148.478 1.00 98.43  ? 414 PRO C CB  1 
ATOM   7892  C  CG  . PRO C 1 398 ? 147.937 169.917 149.662 1.00 98.43  ? 414 PRO C CG  1 
ATOM   7893  C  CD  . PRO C 1 398 ? 148.879 168.944 150.311 1.00 98.43  ? 414 PRO C CD  1 
ATOM   7894  N  N   . SER C 1 399 ? 146.624 165.847 147.554 1.00 104.51 ? 415 SER C N   1 
ATOM   7895  C  CA  . SER C 1 399 ? 146.792 164.883 146.483 1.00 104.51 ? 415 SER C CA  1 
ATOM   7896  C  C   . SER C 1 399 ? 146.301 165.459 145.164 1.00 104.51 ? 415 SER C C   1 
ATOM   7897  O  O   . SER C 1 399 ? 145.394 166.295 145.121 1.00 104.51 ? 415 SER C O   1 
ATOM   7898  C  CB  . SER C 1 399 ? 146.037 163.592 146.798 1.00 104.51 ? 415 SER C CB  1 
ATOM   7899  O  OG  . SER C 1 399 ? 146.167 162.656 145.743 1.00 104.51 ? 415 SER C OG  1 
ATOM   7900  N  N   . ARG C 1 400 ? 146.913 164.997 144.078 1.00 109.54 ? 416 ARG C N   1 
ATOM   7901  C  CA  . ARG C 1 400 ? 146.521 165.381 142.729 1.00 109.54 ? 416 ARG C CA  1 
ATOM   7902  C  C   . ARG C 1 400 ? 146.378 164.157 141.830 1.00 109.54 ? 416 ARG C C   1 
ATOM   7903  O  O   . ARG C 1 400 ? 146.631 164.227 140.624 1.00 109.54 ? 416 ARG C O   1 
ATOM   7904  C  CB  . ARG C 1 400 ? 147.514 166.394 142.157 1.00 109.54 ? 416 ARG C CB  1 
ATOM   7905  C  CG  . ARG C 1 400 ? 148.949 165.903 142.125 1.00 109.54 ? 416 ARG C CG  1 
ATOM   7906  C  CD  . ARG C 1 400 ? 149.905 166.962 141.584 1.00 109.54 ? 416 ARG C CD  1 
ATOM   7907  N  NE  . ARG C 1 400 ? 150.014 168.124 142.457 1.00 109.54 ? 416 ARG C NE  1 
ATOM   7908  C  CZ  . ARG C 1 400 ? 149.856 169.378 142.056 1.00 109.54 ? 416 ARG C CZ  1 
ATOM   7909  N  NH1 . ARG C 1 400 ? 149.610 169.673 140.790 1.00 109.54 ? 416 ARG C NH1 1 
ATOM   7910  N  NH2 . ARG C 1 400 ? 149.961 170.361 142.946 1.00 109.54 ? 416 ARG C NH2 1 
ATOM   7911  N  N   . LEU C 1 401 ? 145.969 163.032 142.409 1.00 104.00 ? 417 LEU C N   1 
ATOM   7912  C  CA  . LEU C 1 401 ? 145.790 161.776 141.698 1.00 104.00 ? 417 LEU C CA  1 
ATOM   7913  C  C   . LEU C 1 401 ? 144.349 161.624 141.222 1.00 104.00 ? 417 LEU C C   1 
ATOM   7914  O  O   . LEU C 1 401 ? 143.429 162.274 141.723 1.00 104.00 ? 417 LEU C O   1 
ATOM   7915  C  CB  . LEU C 1 401 ? 146.168 160.586 142.582 1.00 104.00 ? 417 LEU C CB  1 
ATOM   7916  C  CG  . LEU C 1 401 ? 147.643 160.389 142.930 1.00 104.00 ? 417 LEU C CG  1 
ATOM   7917  C  CD1 . LEU C 1 401 ? 147.784 159.373 144.050 1.00 104.00 ? 417 LEU C CD1 1 
ATOM   7918  C  CD2 . LEU C 1 401 ? 148.428 159.951 141.705 1.00 104.00 ? 417 LEU C CD2 1 
ATOM   7919  N  N   . ILE C 1 402 ? 144.163 160.748 140.238 1.00 103.25 ? 418 ILE C N   1 
ATOM   7920  C  CA  . ILE C 1 402 ? 142.840 160.363 139.759 1.00 103.25 ? 418 ILE C CA  1 
ATOM   7921  C  C   . ILE C 1 402 ? 142.743 158.846 139.837 1.00 103.25 ? 418 ILE C C   1 
ATOM   7922  O  O   . ILE C 1 402 ? 143.481 158.139 139.140 1.00 103.25 ? 418 ILE C O   1 
ATOM   7923  C  CB  . ILE C 1 402 ? 142.575 160.842 138.322 1.00 103.25 ? 418 ILE C CB  1 
ATOM   7924  C  CG1 . ILE C 1 402 ? 142.938 162.319 138.168 1.00 103.25 ? 418 ILE C CG1 1 
ATOM   7925  C  CG2 . ILE C 1 402 ? 141.121 160.612 137.946 1.00 103.25 ? 418 ILE C CG2 1 
ATOM   7926  C  CD1 . ILE C 1 402 ? 144.064 162.569 137.191 1.00 103.25 ? 418 ILE C CD1 1 
ATOM   7927  N  N   . GLN C 1 403 ? 141.842 158.349 140.678 1.00 95.97  ? 419 GLN C N   1 
ATOM   7928  C  CA  . GLN C 1 403 ? 141.604 156.919 140.804 1.00 95.97  ? 419 GLN C CA  1 
ATOM   7929  C  C   . GLN C 1 403 ? 140.308 156.539 140.099 1.00 95.97  ? 419 GLN C C   1 
ATOM   7930  O  O   . GLN C 1 403 ? 139.359 157.323 140.047 1.00 95.97  ? 419 GLN C O   1 
ATOM   7931  C  CB  . GLN C 1 403 ? 141.537 156.506 142.275 1.00 95.97  ? 419 GLN C CB  1 
ATOM   7932  C  CG  . GLN C 1 403 ? 142.719 156.979 143.103 1.00 95.97  ? 419 GLN C CG  1 
ATOM   7933  C  CD  . GLN C 1 403 ? 142.971 156.102 144.311 1.00 95.97  ? 419 GLN C CD  1 
ATOM   7934  O  OE1 . GLN C 1 403 ? 143.091 154.884 144.193 1.00 95.97  ? 419 GLN C OE1 1 
ATOM   7935  N  NE2 . GLN C 1 403 ? 143.050 156.719 145.483 1.00 95.97  ? 419 GLN C NE2 1 
ATOM   7936  N  N   . CYS C 1 404 ? 140.274 155.320 139.563 1.00 117.48 ? 420 CYS C N   1 
ATOM   7937  C  CA  . CYS C 1 404 ? 139.143 154.828 138.788 1.00 117.48 ? 420 CYS C CA  1 
ATOM   7938  C  C   . CYS C 1 404 ? 138.691 153.495 139.360 1.00 117.48 ? 420 CYS C C   1 
ATOM   7939  O  O   . CYS C 1 404 ? 139.478 152.543 139.417 1.00 117.48 ? 420 CYS C O   1 
ATOM   7940  C  CB  . CYS C 1 404 ? 139.510 154.679 137.312 1.00 117.48 ? 420 CYS C CB  1 
ATOM   7941  S  SG  . CYS C 1 404 ? 140.376 156.101 136.636 1.00 117.48 ? 420 CYS C SG  1 
ATOM   7942  N  N   . PHE C 1 405 ? 137.434 153.437 139.787 1.00 105.59 ? 421 PHE C N   1 
ATOM   7943  C  CA  . PHE C 1 405 ? 136.793 152.227 140.283 1.00 105.59 ? 421 PHE C CA  1 
ATOM   7944  C  C   . PHE C 1 405 ? 135.771 151.790 139.240 1.00 105.59 ? 421 PHE C C   1 
ATOM   7945  O  O   . PHE C 1 405 ? 134.727 152.432 139.079 1.00 105.59 ? 421 PHE C O   1 
ATOM   7946  C  CB  . PHE C 1 405 ? 136.134 152.482 141.637 1.00 105.59 ? 421 PHE C CB  1 
ATOM   7947  C  CG  . PHE C 1 405 ? 135.732 151.233 142.369 1.00 105.59 ? 421 PHE C CG  1 
ATOM   7948  C  CD1 . PHE C 1 405 ? 134.552 150.580 142.056 1.00 105.59 ? 421 PHE C CD1 1 
ATOM   7949  C  CD2 . PHE C 1 405 ? 136.527 150.722 143.379 1.00 105.59 ? 421 PHE C CD2 1 
ATOM   7950  C  CE1 . PHE C 1 405 ? 134.178 149.434 142.730 1.00 105.59 ? 421 PHE C CE1 1 
ATOM   7951  C  CE2 . PHE C 1 405 ? 136.157 149.576 144.057 1.00 105.59 ? 421 PHE C CE2 1 
ATOM   7952  C  CZ  . PHE C 1 405 ? 134.981 148.932 143.732 1.00 105.59 ? 421 PHE C CZ  1 
ATOM   7953  N  N   . ASP C 1 406 ? 136.085 150.716 138.521 1.00 114.50 ? 422 ASP C N   1 
ATOM   7954  C  CA  . ASP C 1 406 ? 135.159 150.093 137.586 1.00 114.50 ? 422 ASP C CA  1 
ATOM   7955  C  C   . ASP C 1 406 ? 134.183 149.253 138.398 1.00 114.50 ? 422 ASP C C   1 
ATOM   7956  O  O   . ASP C 1 406 ? 134.575 148.262 139.027 1.00 114.50 ? 422 ASP C O   1 
ATOM   7957  C  CB  . ASP C 1 406 ? 135.922 149.247 136.569 1.00 114.50 ? 422 ASP C CB  1 
ATOM   7958  C  CG  . ASP C 1 406 ? 135.028 148.673 135.478 1.00 114.50 ? 422 ASP C CG  1 
ATOM   7959  O  OD1 . ASP C 1 406 ? 133.815 148.483 135.707 1.00 114.50 ? 422 ASP C OD1 1 
ATOM   7960  O  OD2 . ASP C 1 406 ? 135.551 148.406 134.376 1.00 114.50 ? 422 ASP C OD2 1 
ATOM   7961  N  N   . THR C 1 407 ? 132.913 149.665 138.394 1.00 104.74 ? 423 THR C N   1 
ATOM   7962  C  CA  . THR C 1 407 ? 131.892 149.010 139.202 1.00 104.74 ? 423 THR C CA  1 
ATOM   7963  C  C   . THR C 1 407 ? 131.441 147.690 138.589 1.00 104.74 ? 423 THR C C   1 
ATOM   7964  O  O   . THR C 1 407 ? 131.167 146.729 139.316 1.00 104.74 ? 423 THR C O   1 
ATOM   7965  C  CB  . THR C 1 407 ? 130.697 149.946 139.379 1.00 104.74 ? 423 THR C CB  1 
ATOM   7966  O  OG1 . THR C 1 407 ? 131.162 151.282 139.600 1.00 104.74 ? 423 THR C OG1 1 
ATOM   7967  C  CG2 . THR C 1 407 ? 129.852 149.515 140.553 1.00 104.74 ? 423 THR C CG2 1 
ATOM   7968  N  N   . GLU C 1 408 ? 131.344 147.627 137.258 1.00 111.54 ? 424 GLU C N   1 
ATOM   7969  C  CA  . GLU C 1 408 ? 130.940 146.384 136.609 1.00 111.54 ? 424 GLU C CA  1 
ATOM   7970  C  C   . GLU C 1 408 ? 131.942 145.270 136.881 1.00 111.54 ? 424 GLU C C   1 
ATOM   7971  O  O   . GLU C 1 408 ? 131.554 144.131 137.166 1.00 111.54 ? 424 GLU C O   1 
ATOM   7972  C  CB  . GLU C 1 408 ? 130.775 146.606 135.105 1.00 111.54 ? 424 GLU C CB  1 
ATOM   7973  N  N   . THR C 1 409 ? 133.235 145.579 136.797 1.00 113.61 ? 425 THR C N   1 
ATOM   7974  C  CA  . THR C 1 409 ? 134.285 144.616 137.091 1.00 113.61 ? 425 THR C CA  1 
ATOM   7975  C  C   . THR C 1 409 ? 134.795 144.725 138.524 1.00 113.61 ? 425 THR C C   1 
ATOM   7976  O  O   . THR C 1 409 ? 135.497 143.820 138.987 1.00 113.61 ? 425 THR C O   1 
ATOM   7977  C  CB  . THR C 1 409 ? 135.449 144.799 136.106 1.00 113.61 ? 425 THR C CB  1 
ATOM   7978  O  OG1 . THR C 1 409 ? 134.925 144.981 134.784 1.00 113.61 ? 425 THR C OG1 1 
ATOM   7979  C  CG2 . THR C 1 409 ? 136.345 143.570 136.089 1.00 113.61 ? 425 THR C CG2 1 
ATOM   7980  N  N   . ASP C 1 410 ? 134.429 145.791 139.240 1.00 104.51 ? 426 ASP C N   1 
ATOM   7981  C  CA  . ASP C 1 410 ? 134.855 146.012 140.623 1.00 104.51 ? 426 ASP C CA  1 
ATOM   7982  C  C   . ASP C 1 410 ? 136.379 146.018 140.745 1.00 104.51 ? 426 ASP C C   1 
ATOM   7983  O  O   . ASP C 1 410 ? 136.965 145.275 141.533 1.00 104.51 ? 426 ASP C O   1 
ATOM   7984  C  CB  . ASP C 1 410 ? 134.231 144.976 141.562 1.00 104.51 ? 426 ASP C CB  1 
ATOM   7985  N  N   . LYS C 1 411 ? 137.026 146.868 139.949 1.00 110.10 ? 427 LYS C N   1 
ATOM   7986  C  CA  . LYS C 1 411 ? 138.482 146.933 139.911 1.00 110.10 ? 427 LYS C CA  1 
ATOM   7987  C  C   . LYS C 1 411 ? 138.950 148.378 139.992 1.00 110.10 ? 427 LYS C C   1 
ATOM   7988  O  O   . LYS C 1 411 ? 138.354 149.265 139.381 1.00 110.10 ? 427 LYS C O   1 
ATOM   7989  C  CB  . LYS C 1 411 ? 139.046 146.286 138.640 1.00 110.10 ? 427 LYS C CB  1 
ATOM   7990  C  CG  . LYS C 1 411 ? 138.930 144.771 138.599 1.00 110.10 ? 427 LYS C CG  1 
ATOM   7991  C  CD  . LYS C 1 411 ? 139.668 144.131 137.412 1.00 110.10 ? 427 LYS C CD  1 
ATOM   7992  C  CE  . LYS C 1 411 ? 141.194 144.307 137.431 1.00 110.10 ? 427 LYS C CE  1 
ATOM   7993  N  NZ  . LYS C 1 411 ? 141.719 145.699 137.337 1.00 110.10 ? 427 LYS C NZ  1 
ATOM   7994  N  N   . CYS C 1 412 ? 140.029 148.612 140.731 1.00 114.28 ? 428 CYS C N   1 
ATOM   7995  C  CA  . CYS C 1 412 ? 140.551 149.957 140.935 1.00 114.28 ? 428 CYS C CA  1 
ATOM   7996  C  C   . CYS C 1 412 ? 141.902 150.116 140.254 1.00 114.28 ? 428 CYS C C   1 
ATOM   7997  O  O   . CYS C 1 412 ? 142.725 149.195 140.262 1.00 114.28 ? 428 CYS C O   1 
ATOM   7998  C  CB  . CYS C 1 412 ? 140.692 150.276 142.425 1.00 114.28 ? 428 CYS C CB  1 
ATOM   7999  S  SG  . CYS C 1 412 ? 141.376 151.918 142.737 1.00 114.28 ? 428 CYS C SG  1 
ATOM   8000  N  N   . HIS C 1 413 ? 142.123 151.290 139.664 1.00 104.89 ? 429 HIS C N   1 
ATOM   8001  C  CA  . HIS C 1 413 ? 143.412 151.599 139.060 1.00 104.89 ? 429 HIS C CA  1 
ATOM   8002  C  C   . HIS C 1 413 ? 143.631 153.106 139.040 1.00 104.89 ? 429 HIS C C   1 
ATOM   8003  O  O   . HIS C 1 413 ? 142.683 153.887 138.947 1.00 104.89 ? 429 HIS C O   1 
ATOM   8004  C  CB  . HIS C 1 413 ? 143.517 151.025 137.640 1.00 104.89 ? 429 HIS C CB  1 
ATOM   8005  C  CG  . HIS C 1 413 ? 142.978 151.930 136.577 1.00 104.89 ? 429 HIS C CG  1 
ATOM   8006  N  ND1 . HIS C 1 413 ? 141.661 151.902 136.173 1.00 104.89 ? 429 HIS C ND1 1 
ATOM   8007  C  CD2 . HIS C 1 413 ? 143.581 152.879 135.822 1.00 104.89 ? 429 HIS C CD2 1 
ATOM   8008  C  CE1 . HIS C 1 413 ? 141.474 152.800 135.222 1.00 104.89 ? 429 HIS C CE1 1 
ATOM   8009  N  NE2 . HIS C 1 413 ? 142.624 153.407 134.991 1.00 104.89 ? 429 HIS C NE2 1 
ATOM   8010  N  N   . VAL C 1 414 ? 144.898 153.507 139.118 1.00 103.79 ? 430 VAL C N   1 
ATOM   8011  C  CA  . VAL C 1 414 ? 145.287 154.914 139.152 1.00 103.79 ? 430 VAL C CA  1 
ATOM   8012  C  C   . VAL C 1 414 ? 145.692 155.351 137.753 1.00 103.79 ? 430 VAL C C   1 
ATOM   8013  O  O   . VAL C 1 414 ? 146.413 154.633 137.050 1.00 103.79 ? 430 VAL C O   1 
ATOM   8014  C  CB  . VAL C 1 414 ? 146.428 155.156 140.157 1.00 103.79 ? 430 VAL C CB  1 
ATOM   8015  C  CG1 . VAL C 1 414 ? 146.713 156.642 140.288 1.00 103.79 ? 430 VAL C CG1 1 
ATOM   8016  C  CG2 . VAL C 1 414 ? 146.074 154.566 141.507 1.00 103.79 ? 430 VAL C CG2 1 
ATOM   8017  N  N   . LYS C 1 415 ? 145.221 156.527 137.344 1.00 103.29 ? 431 LYS C N   1 
ATOM   8018  C  CA  . LYS C 1 415 ? 145.560 157.048 136.030 1.00 103.29 ? 431 LYS C CA  1 
ATOM   8019  C  C   . LYS C 1 415 ? 147.061 157.324 135.938 1.00 103.29 ? 431 LYS C C   1 
ATOM   8020  O  O   . LYS C 1 415 ? 147.708 157.636 136.943 1.00 103.29 ? 431 LYS C O   1 
ATOM   8021  C  CB  . LYS C 1 415 ? 144.778 158.328 135.742 1.00 103.29 ? 431 LYS C CB  1 
ATOM   8022  C  CG  . LYS C 1 415 ? 143.273 158.147 135.692 1.00 103.29 ? 431 LYS C CG  1 
ATOM   8023  C  CD  . LYS C 1 415 ? 142.865 157.355 134.461 1.00 103.29 ? 431 LYS C CD  1 
ATOM   8024  C  CE  . LYS C 1 415 ? 141.551 157.859 133.888 1.00 103.29 ? 431 LYS C CE  1 
ATOM   8025  N  NZ  . LYS C 1 415 ? 141.024 156.960 132.826 1.00 103.29 ? 431 LYS C NZ  1 
ATOM   8026  N  N   . PRO C 1 416 ? 147.642 157.216 134.741 1.00 106.66 ? 432 PRO C N   1 
ATOM   8027  C  CA  . PRO C 1 416 ? 149.078 157.474 134.581 1.00 106.66 ? 432 PRO C CA  1 
ATOM   8028  C  C   . PRO C 1 416 ? 149.443 158.946 134.496 1.00 106.66 ? 432 PRO C C   1 
ATOM   8029  O  O   . PRO C 1 416 ? 150.636 159.264 134.435 1.00 106.66 ? 432 PRO C O   1 
ATOM   8030  C  CB  . PRO C 1 416 ? 149.416 156.753 133.261 1.00 106.66 ? 432 PRO C CB  1 
ATOM   8031  C  CG  . PRO C 1 416 ? 148.165 155.997 132.865 1.00 106.66 ? 432 PRO C CG  1 
ATOM   8032  C  CD  . PRO C 1 416 ? 147.036 156.727 133.495 1.00 106.66 ? 432 PRO C CD  1 
ATOM   8033  N  N   . TYR C 1 417 ? 148.469 159.850 134.492 1.00 114.17 ? 433 TYR C N   1 
ATOM   8034  C  CA  . TYR C 1 417 ? 148.724 161.281 134.411 1.00 114.17 ? 433 TYR C CA  1 
ATOM   8035  C  C   . TYR C 1 417 ? 148.240 161.953 135.692 1.00 114.17 ? 433 TYR C C   1 
ATOM   8036  O  O   . TYR C 1 417 ? 147.765 161.300 136.624 1.00 114.17 ? 433 TYR C O   1 
ATOM   8037  C  CB  . TYR C 1 417 ? 148.061 161.897 133.176 1.00 114.17 ? 433 TYR C CB  1 
ATOM   8038  C  CG  . TYR C 1 417 ? 146.651 161.428 132.906 1.00 114.17 ? 433 TYR C CG  1 
ATOM   8039  C  CD1 . TYR C 1 417 ? 145.562 162.089 133.458 1.00 114.17 ? 433 TYR C CD1 1 
ATOM   8040  C  CD2 . TYR C 1 417 ? 146.406 160.333 132.088 1.00 114.17 ? 433 TYR C CD2 1 
ATOM   8041  C  CE1 . TYR C 1 417 ? 144.271 161.671 133.209 1.00 114.17 ? 433 TYR C CE1 1 
ATOM   8042  C  CE2 . TYR C 1 417 ? 145.118 159.906 131.835 1.00 114.17 ? 433 TYR C CE2 1 
ATOM   8043  C  CZ  . TYR C 1 417 ? 144.055 160.579 132.397 1.00 114.17 ? 433 TYR C CZ  1 
ATOM   8044  O  OH  . TYR C 1 417 ? 142.771 160.160 132.146 1.00 114.17 ? 433 TYR C OH  1 
ATOM   8045  N  N   . VAL C 1 418 ? 148.369 163.278 135.733 1.00 111.44 ? 434 VAL C N   1 
ATOM   8046  C  CA  . VAL C 1 418 ? 148.223 164.028 136.971 1.00 111.44 ? 434 VAL C CA  1 
ATOM   8047  C  C   . VAL C 1 418 ? 147.204 165.146 136.782 1.00 111.44 ? 434 VAL C C   1 
ATOM   8048  O  O   . VAL C 1 418 ? 146.938 165.598 135.666 1.00 111.44 ? 434 VAL C O   1 
ATOM   8049  C  CB  . VAL C 1 418 ? 149.581 164.594 137.441 1.00 111.44 ? 434 VAL C CB  1 
ATOM   8050  C  CG1 . VAL C 1 418 ? 149.883 165.929 136.765 1.00 111.44 ? 434 VAL C CG1 1 
ATOM   8051  C  CG2 . VAL C 1 418 ? 149.622 164.699 138.943 1.00 111.44 ? 434 VAL C CG2 1 
ATOM   8052  N  N   . LEU C 1 419 ? 146.617 165.582 137.907 1.00 99.80  ? 435 LEU C N   1 
ATOM   8053  C  CA  . LEU C 1 419 ? 145.646 166.666 137.909 1.00 99.80  ? 435 LEU C CA  1 
ATOM   8054  C  C   . LEU C 1 419 ? 146.350 168.020 137.830 1.00 99.80  ? 435 LEU C C   1 
ATOM   8055  O  O   . LEU C 1 419 ? 147.500 168.153 138.259 1.00 99.80  ? 435 LEU C O   1 
ATOM   8056  C  CB  . LEU C 1 419 ? 144.789 166.613 139.169 1.00 99.80  ? 435 LEU C CB  1 
ATOM   8057  C  CG  . LEU C 1 419 ? 143.541 165.731 139.140 1.00 99.80  ? 435 LEU C CG  1 
ATOM   8058  C  CD1 . LEU C 1 419 ? 143.021 165.494 140.549 1.00 99.80  ? 435 LEU C CD1 1 
ATOM   8059  C  CD2 . LEU C 1 419 ? 142.464 166.352 138.267 1.00 99.80  ? 435 LEU C CD2 1 
ATOM   8060  N  N   . PRO C 1 420 ? 145.687 169.037 137.269 1.00 100.55 ? 436 PRO C N   1 
ATOM   8061  C  CA  . PRO C 1 420 ? 146.316 170.368 137.223 1.00 100.55 ? 436 PRO C CA  1 
ATOM   8062  C  C   . PRO C 1 420 ? 146.663 170.933 138.591 1.00 100.55 ? 436 PRO C C   1 
ATOM   8063  O  O   . PRO C 1 420 ? 147.702 171.586 138.738 1.00 100.55 ? 436 PRO C O   1 
ATOM   8064  C  CB  . PRO C 1 420 ? 145.262 171.224 136.506 1.00 100.55 ? 436 PRO C CB  1 
ATOM   8065  C  CG  . PRO C 1 420 ? 144.449 170.249 135.722 1.00 100.55 ? 436 PRO C CG  1 
ATOM   8066  C  CD  . PRO C 1 420 ? 144.399 169.007 136.557 1.00 100.55 ? 436 PRO C CD  1 
ATOM   8067  N  N   . PHE C 1 421 ? 145.824 170.701 139.601 1.00 98.65  ? 437 PHE C N   1 
ATOM   8068  C  CA  . PHE C 1 421 ? 146.037 171.260 140.931 1.00 98.65  ? 437 PHE C CA  1 
ATOM   8069  C  C   . PHE C 1 421 ? 145.780 170.185 141.980 1.00 98.65  ? 437 PHE C C   1 
ATOM   8070  O  O   . PHE C 1 421 ? 145.488 169.028 141.659 1.00 98.65  ? 437 PHE C O   1 
ATOM   8071  C  CB  . PHE C 1 421 ? 145.178 172.512 141.156 1.00 98.65  ? 437 PHE C CB  1 
ATOM   8072  C  CG  . PHE C 1 421 ? 143.797 172.427 140.572 1.00 98.65  ? 437 PHE C CG  1 
ATOM   8073  C  CD1 . PHE C 1 421 ? 142.923 171.421 140.943 1.00 98.65  ? 437 PHE C CD1 1 
ATOM   8074  C  CD2 . PHE C 1 421 ? 143.371 173.371 139.653 1.00 98.65  ? 437 PHE C CD2 1 
ATOM   8075  C  CE1 . PHE C 1 421 ? 141.656 171.356 140.400 1.00 98.65  ? 437 PHE C CE1 1 
ATOM   8076  C  CE2 . PHE C 1 421 ? 142.106 173.309 139.111 1.00 98.65  ? 437 PHE C CE2 1 
ATOM   8077  C  CZ  . PHE C 1 421 ? 141.248 172.303 139.487 1.00 98.65  ? 437 PHE C CZ  1 
ATOM   8078  N  N   . ALA C 1 422 ? 145.892 170.576 143.249 1.00 93.88  ? 438 ALA C N   1 
ATOM   8079  C  CA  . ALA C 1 422 ? 145.749 169.650 144.362 1.00 93.88  ? 438 ALA C CA  1 
ATOM   8080  C  C   . ALA C 1 422 ? 145.104 170.358 145.545 1.00 93.88  ? 438 ALA C C   1 
ATOM   8081  O  O   . ALA C 1 422 ? 145.230 171.575 145.704 1.00 93.88  ? 438 ALA C O   1 
ATOM   8082  C  CB  . ALA C 1 422 ? 147.101 169.058 144.774 1.00 93.88  ? 438 ALA C CB  1 
ATOM   8083  N  N   . GLY C 1 423 ? 144.410 169.578 146.373 1.00 99.14  ? 439 GLY C N   1 
ATOM   8084  C  CA  . GLY C 1 423 ? 143.841 170.068 147.615 1.00 99.14  ? 439 GLY C CA  1 
ATOM   8085  C  C   . GLY C 1 423 ? 142.346 169.844 147.725 1.00 99.14  ? 439 GLY C C   1 
ATOM   8086  O  O   . GLY C 1 423 ? 141.803 168.969 147.044 1.00 99.14  ? 439 GLY C O   1 
ATOM   8087  N  N   . ARG C 1 424 ? 141.673 170.609 148.588 1.00 103.20 ? 440 ARG C N   1 
ATOM   8088  C  CA  . ARG C 1 424 ? 140.228 170.477 148.727 1.00 103.20 ? 440 ARG C CA  1 
ATOM   8089  C  C   . ARG C 1 424 ? 139.557 170.714 147.382 1.00 103.20 ? 440 ARG C C   1 
ATOM   8090  O  O   . ARG C 1 424 ? 139.890 171.659 146.662 1.00 103.20 ? 440 ARG C O   1 
ATOM   8091  C  CB  . ARG C 1 424 ? 139.700 171.465 149.768 1.00 103.20 ? 440 ARG C CB  1 
ATOM   8092  N  N   . MET C 1 425 ? 138.604 169.851 147.041 1.00 105.71 ? 441 MET C N   1 
ATOM   8093  C  CA  . MET C 1 425 ? 138.081 169.835 145.686 1.00 105.71 ? 441 MET C CA  1 
ATOM   8094  C  C   . MET C 1 425 ? 136.588 169.521 145.685 1.00 105.71 ? 441 MET C C   1 
ATOM   8095  O  O   . MET C 1 425 ? 136.074 168.870 146.598 1.00 105.71 ? 441 MET C O   1 
ATOM   8096  C  CB  . MET C 1 425 ? 138.885 168.842 144.843 1.00 105.71 ? 441 MET C CB  1 
ATOM   8097  C  CG  . MET C 1 425 ? 138.579 168.891 143.383 1.00 105.71 ? 441 MET C CG  1 
ATOM   8098  S  SD  . MET C 1 425 ? 140.073 169.136 142.404 1.00 105.71 ? 441 MET C SD  1 
ATOM   8099  C  CE  . MET C 1 425 ? 141.177 167.951 143.141 1.00 105.71 ? 441 MET C CE  1 
ATOM   8100  N  N   . HIS C 1 426 ? 135.898 169.999 144.647 1.00 109.70 ? 442 HIS C N   1 
ATOM   8101  C  CA  . HIS C 1 426 ? 134.479 169.739 144.437 1.00 109.70 ? 442 HIS C CA  1 
ATOM   8102  C  C   . HIS C 1 426 ? 134.235 169.404 142.973 1.00 109.70 ? 442 HIS C C   1 
ATOM   8103  O  O   . HIS C 1 426 ? 134.835 170.011 142.081 1.00 109.70 ? 442 HIS C O   1 
ATOM   8104  C  CB  . HIS C 1 426 ? 133.619 170.943 144.844 1.00 109.70 ? 442 HIS C CB  1 
ATOM   8105  C  CG  . HIS C 1 426 ? 132.226 170.579 145.255 1.00 109.70 ? 442 HIS C CG  1 
ATOM   8106  N  ND1 . HIS C 1 426 ? 131.181 170.505 144.359 1.00 109.70 ? 442 HIS C ND1 1 
ATOM   8107  C  CD2 . HIS C 1 426 ? 131.705 170.272 146.466 1.00 109.70 ? 442 HIS C CD2 1 
ATOM   8108  C  CE1 . HIS C 1 426 ? 130.077 170.166 145.000 1.00 109.70 ? 442 HIS C CE1 1 
ATOM   8109  N  NE2 . HIS C 1 426 ? 130.368 170.018 146.280 1.00 109.70 ? 442 HIS C NE2 1 
ATOM   8110  N  N   . ALA C 1 427 ? 133.353 168.434 142.731 1.00 91.02  ? 443 ALA C N   1 
ATOM   8111  C  CA  . ALA C 1 427 ? 133.081 167.932 141.392 1.00 91.02  ? 443 ALA C CA  1 
ATOM   8112  C  C   . ALA C 1 427 ? 131.579 167.821 141.158 1.00 91.02  ? 443 ALA C C   1 
ATOM   8113  O  O   . ALA C 1 427 ? 130.789 167.708 142.098 1.00 91.02  ? 443 ALA C O   1 
ATOM   8114  C  CB  . ALA C 1 427 ? 133.746 166.569 141.164 1.00 91.02  ? 443 ALA C CB  1 
ATOM   8115  N  N   . ALA C 1 428 ? 131.194 167.857 139.882 1.00 96.17  ? 444 ALA C N   1 
ATOM   8116  C  CA  . ALA C 1 428 ? 129.794 167.736 139.482 1.00 96.17  ? 444 ALA C CA  1 
ATOM   8117  C  C   . ALA C 1 428 ? 129.735 167.180 138.067 1.00 96.17  ? 444 ALA C C   1 
ATOM   8118  O  O   . ALA C 1 428 ? 130.327 167.757 137.150 1.00 96.17  ? 444 ALA C O   1 
ATOM   8119  C  CB  . ALA C 1 428 ? 129.077 169.084 139.562 1.00 96.17  ? 444 ALA C CB  1 
ATOM   8120  N  N   . VAL C 1 429 ? 129.023 166.069 137.893 1.00 97.34  ? 445 VAL C N   1 
ATOM   8121  C  CA  . VAL C 1 429 ? 128.954 165.386 136.604 1.00 97.34  ? 445 VAL C CA  1 
ATOM   8122  C  C   . VAL C 1 429 ? 127.990 166.111 135.674 1.00 97.34  ? 445 VAL C C   1 
ATOM   8123  O  O   . VAL C 1 429 ? 126.844 166.397 136.042 1.00 97.34  ? 445 VAL C O   1 
ATOM   8124  C  CB  . VAL C 1 429 ? 128.528 163.922 136.795 1.00 97.34  ? 445 VAL C CB  1 
ATOM   8125  C  CG1 . VAL C 1 429 ? 128.292 163.257 135.451 1.00 97.34  ? 445 VAL C CG1 1 
ATOM   8126  C  CG2 . VAL C 1 429 ? 129.572 163.167 137.599 1.00 97.34  ? 445 VAL C CG2 1 
ATOM   8127  N  N   . HIS C 1 430 ? 128.453 166.404 134.458 1.00 116.92 ? 446 HIS C N   1 
ATOM   8128  C  CA  . HIS C 1 430 ? 127.633 167.026 133.423 1.00 116.92 ? 446 HIS C CA  1 
ATOM   8129  C  C   . HIS C 1 430 ? 127.954 166.334 132.107 1.00 116.92 ? 446 HIS C C   1 
ATOM   8130  O  O   . HIS C 1 430 ? 129.094 166.407 131.636 1.00 116.92 ? 446 HIS C O   1 
ATOM   8131  C  CB  . HIS C 1 430 ? 127.890 168.535 133.335 1.00 116.92 ? 446 HIS C CB  1 
ATOM   8132  C  CG  . HIS C 1 430 ? 126.941 169.264 132.434 1.00 116.92 ? 446 HIS C CG  1 
ATOM   8133  N  ND1 . HIS C 1 430 ? 126.524 170.553 132.687 1.00 116.92 ? 446 HIS C ND1 1 
ATOM   8134  C  CD2 . HIS C 1 430 ? 126.330 168.891 131.285 1.00 116.92 ? 446 HIS C CD2 1 
ATOM   8135  C  CE1 . HIS C 1 430 ? 125.696 170.942 131.734 1.00 116.92 ? 446 HIS C CE1 1 
ATOM   8136  N  NE2 . HIS C 1 430 ? 125.561 169.952 130.870 1.00 116.92 ? 446 HIS C NE2 1 
ATOM   8137  N  N   . LYS C 1 431 ? 126.957 165.675 131.515 1.00 117.42 ? 447 LYS C N   1 
ATOM   8138  C  CA  . LYS C 1 431 ? 127.119 164.900 130.278 1.00 117.42 ? 447 LYS C CA  1 
ATOM   8139  C  C   . LYS C 1 431 ? 128.210 163.866 130.530 1.00 117.42 ? 447 LYS C C   1 
ATOM   8140  O  O   . LYS C 1 431 ? 128.020 163.003 131.405 1.00 117.42 ? 447 LYS C O   1 
ATOM   8141  C  CB  . LYS C 1 431 ? 127.359 165.857 129.107 1.00 117.42 ? 447 LYS C CB  1 
ATOM   8142  N  N   . ASP C 1 432 ? 129.333 163.887 129.809 1.00 118.60 ? 448 ASP C N   1 
ATOM   8143  C  CA  . ASP C 1 432 ? 130.429 162.953 130.044 1.00 118.60 ? 448 ASP C CA  1 
ATOM   8144  C  C   . ASP C 1 432 ? 131.619 163.655 130.676 1.00 118.60 ? 448 ASP C C   1 
ATOM   8145  O  O   . ASP C 1 432 ? 132.751 163.177 130.564 1.00 118.60 ? 448 ASP C O   1 
ATOM   8146  C  CB  . ASP C 1 432 ? 130.877 162.279 128.751 1.00 118.60 ? 448 ASP C CB  1 
ATOM   8147  C  CG  . ASP C 1 432 ? 131.005 163.250 127.615 1.00 118.60 ? 448 ASP C CG  1 
ATOM   8148  O  OD1 . ASP C 1 432 ? 131.935 164.077 127.637 1.00 118.60 ? 448 ASP C OD1 1 
ATOM   8149  O  OD2 . ASP C 1 432 ? 130.207 163.170 126.679 1.00 118.60 ? 448 ASP C OD2 1 
ATOM   8150  N  N   . LEU C 1 433 ? 131.388 164.791 131.319 1.00 103.14 ? 449 LEU C N   1 
ATOM   8151  C  CA  . LEU C 1 433 ? 132.465 165.600 131.853 1.00 103.14 ? 449 LEU C CA  1 
ATOM   8152  C  C   . LEU C 1 433 ? 132.315 165.721 133.358 1.00 103.14 ? 449 LEU C C   1 
ATOM   8153  O  O   . LEU C 1 433 ? 131.270 165.422 133.940 1.00 103.14 ? 449 LEU C O   1 
ATOM   8154  C  CB  . LEU C 1 433 ? 132.455 167.014 131.253 1.00 103.14 ? 449 LEU C CB  1 
ATOM   8155  C  CG  . LEU C 1 433 ? 132.525 167.292 129.751 1.00 103.14 ? 449 LEU C CG  1 
ATOM   8156  C  CD1 . LEU C 1 433 ? 133.482 166.346 129.063 1.00 103.14 ? 449 LEU C CD1 1 
ATOM   8157  C  CD2 . LEU C 1 433 ? 131.140 167.236 129.118 1.00 103.14 ? 449 LEU C CD2 1 
ATOM   8158  N  N   . VAL C 1 434 ? 133.400 166.162 133.977 1.00 89.39  ? 450 VAL C N   1 
ATOM   8159  C  CA  . VAL C 1 434 ? 133.425 166.506 135.386 1.00 89.39  ? 450 VAL C CA  1 
ATOM   8160  C  C   . VAL C 1 434 ? 133.931 167.935 135.460 1.00 89.39  ? 450 VAL C C   1 
ATOM   8161  O  O   . VAL C 1 434 ? 135.046 168.228 135.005 1.00 89.39  ? 450 VAL C O   1 
ATOM   8162  C  CB  . VAL C 1 434 ? 134.314 165.554 136.201 1.00 89.39  ? 450 VAL C CB  1 
ATOM   8163  C  CG1 . VAL C 1 434 ? 134.168 165.839 137.680 1.00 89.39  ? 450 VAL C CG1 1 
ATOM   8164  C  CG2 . VAL C 1 434 ? 133.966 164.108 135.894 1.00 89.39  ? 450 VAL C CG2 1 
ATOM   8165  N  N   . PHE C 1 435 ? 133.104 168.831 135.987 1.00 98.50  ? 451 PHE C N   1 
ATOM   8166  C  CA  . PHE C 1 435 ? 133.498 170.226 136.138 1.00 98.50  ? 451 PHE C CA  1 
ATOM   8167  C  C   . PHE C 1 435 ? 134.038 170.342 137.553 1.00 98.50  ? 451 PHE C C   1 
ATOM   8168  O  O   . PHE C 1 435 ? 133.281 170.470 138.517 1.00 98.50  ? 451 PHE C O   1 
ATOM   8169  C  CB  . PHE C 1 435 ? 132.329 171.163 135.872 1.00 98.50  ? 451 PHE C CB  1 
ATOM   8170  C  CG  . PHE C 1 435 ? 131.996 171.312 134.417 1.00 98.50  ? 451 PHE C CG  1 
ATOM   8171  C  CD1 . PHE C 1 435 ? 131.108 170.447 133.804 1.00 98.50  ? 451 PHE C CD1 1 
ATOM   8172  C  CD2 . PHE C 1 435 ? 132.586 172.307 133.658 1.00 98.50  ? 451 PHE C CD2 1 
ATOM   8173  C  CE1 . PHE C 1 435 ? 130.806 170.581 132.463 1.00 98.50  ? 451 PHE C CE1 1 
ATOM   8174  C  CE2 . PHE C 1 435 ? 132.289 172.444 132.318 1.00 98.50  ? 451 PHE C CE2 1 
ATOM   8175  C  CZ  . PHE C 1 435 ? 131.399 171.581 131.721 1.00 98.50  ? 451 PHE C CZ  1 
ATOM   8176  N  N   . ILE C 1 436 ? 135.358 170.300 137.670 1.00 96.67  ? 452 ILE C N   1 
ATOM   8177  C  CA  . ILE C 1 436 ? 136.040 170.218 138.950 1.00 96.67  ? 452 ILE C CA  1 
ATOM   8178  C  C   . ILE C 1 436 ? 136.488 171.616 139.344 1.00 96.67  ? 452 ILE C C   1 
ATOM   8179  O  O   . ILE C 1 436 ? 137.097 172.334 138.540 1.00 96.67  ? 452 ILE C O   1 
ATOM   8180  C  CB  . ILE C 1 436 ? 137.233 169.255 138.867 1.00 96.67  ? 452 ILE C CB  1 
ATOM   8181  C  CG1 . ILE C 1 436 ? 136.881 168.040 138.018 1.00 96.67  ? 452 ILE C CG1 1 
ATOM   8182  C  CG2 . ILE C 1 436 ? 137.536 168.720 140.208 1.00 96.67  ? 452 ILE C CG2 1 
ATOM   8183  C  CD1 . ILE C 1 436 ? 138.086 167.238 137.584 1.00 96.67  ? 452 ILE C CD1 1 
ATOM   8184  N  N   . VAL C 1 437 ? 136.193 172.001 140.582 1.00 103.73 ? 453 VAL C N   1 
ATOM   8185  C  CA  . VAL C 1 437 ? 136.491 173.333 141.092 1.00 103.73 ? 453 VAL C CA  1 
ATOM   8186  C  C   . VAL C 1 437 ? 137.322 173.192 142.358 1.00 103.73 ? 453 VAL C C   1 
ATOM   8187  O  O   . VAL C 1 437 ? 136.992 172.387 143.237 1.00 103.73 ? 453 VAL C O   1 
ATOM   8188  C  CB  . VAL C 1 437 ? 135.202 174.128 141.369 1.00 103.73 ? 453 VAL C CB  1 
ATOM   8189  C  CG1 . VAL C 1 437 ? 135.513 175.401 142.133 1.00 103.73 ? 453 VAL C CG1 1 
ATOM   8190  C  CG2 . VAL C 1 437 ? 134.483 174.440 140.067 1.00 103.73 ? 453 VAL C CG2 1 
ATOM   8191  N  N   . ALA C 1 438 ? 138.397 173.972 142.448 1.00 111.48 ? 454 ALA C N   1 
ATOM   8192  C  CA  . ALA C 1 438 ? 139.282 173.935 143.603 1.00 111.48 ? 454 ALA C CA  1 
ATOM   8193  C  C   . ALA C 1 438 ? 140.030 175.257 143.687 1.00 111.48 ? 454 ALA C C   1 
ATOM   8194  O  O   . ALA C 1 438 ? 140.115 176.005 142.710 1.00 111.48 ? 454 ALA C O   1 
ATOM   8195  C  CB  . ALA C 1 438 ? 140.264 172.761 143.526 1.00 111.48 ? 454 ALA C CB  1 
ATOM   8196  N  N   . GLU C 1 439 ? 140.570 175.528 144.874 1.00 127.30 ? 455 GLU C N   1 
ATOM   8197  C  CA  . GLU C 1 439 ? 141.373 176.729 145.154 1.00 127.30 ? 455 GLU C CA  1 
ATOM   8198  C  C   . GLU C 1 439 ? 140.504 177.950 144.857 1.00 127.30 ? 455 GLU C C   1 
ATOM   8199  O  O   . GLU C 1 439 ? 139.369 178.021 145.356 1.00 127.30 ? 455 GLU C O   1 
ATOM   8200  C  CB  . GLU C 1 439 ? 142.684 176.648 144.381 1.00 127.30 ? 455 GLU C CB  1 
ATOM   8201  N  N   . GLY C 1 440 ? 140.972 178.915 144.070 1.00 132.79 ? 456 GLY C N   1 
ATOM   8202  C  CA  . GLY C 1 440 ? 140.179 180.083 143.743 1.00 132.79 ? 456 GLY C CA  1 
ATOM   8203  C  C   . GLY C 1 440 ? 140.372 180.510 142.304 1.00 132.79 ? 456 GLY C C   1 
ATOM   8204  O  O   . GLY C 1 440 ? 141.500 180.521 141.802 1.00 132.79 ? 456 GLY C O   1 
ATOM   8205  N  N   . ASP C 1 441 ? 139.273 180.859 141.633 1.00 136.76 ? 457 ASP C N   1 
ATOM   8206  C  CA  . ASP C 1 441 ? 139.287 181.241 140.221 1.00 136.76 ? 457 ASP C CA  1 
ATOM   8207  C  C   . ASP C 1 441 ? 139.871 180.129 139.354 1.00 136.76 ? 457 ASP C C   1 
ATOM   8208  O  O   . ASP C 1 441 ? 140.490 180.389 138.319 1.00 136.76 ? 457 ASP C O   1 
ATOM   8209  C  CB  . ASP C 1 441 ? 140.047 182.552 139.999 1.00 136.76 ? 457 ASP C CB  1 
ATOM   8210  N  N   . SER C 1 442 ? 139.674 178.883 139.776 1.00 121.79 ? 458 SER C N   1 
ATOM   8211  C  CA  . SER C 1 442 ? 140.177 177.713 139.071 1.00 121.79 ? 458 SER C CA  1 
ATOM   8212  C  C   . SER C 1 442 ? 139.019 176.765 138.811 1.00 121.79 ? 458 SER C C   1 
ATOM   8213  O  O   . SER C 1 442 ? 138.251 176.450 139.725 1.00 121.79 ? 458 SER C O   1 
ATOM   8214  C  CB  . SER C 1 442 ? 141.277 177.009 139.870 1.00 121.79 ? 458 SER C CB  1 
ATOM   8215  N  N   . LEU C 1 443 ? 138.902 176.310 137.568 1.00 122.35 ? 459 LEU C N   1 
ATOM   8216  C  CA  . LEU C 1 443 ? 137.841 175.394 137.174 1.00 122.35 ? 459 LEU C CA  1 
ATOM   8217  C  C   . LEU C 1 443 ? 138.336 174.607 135.974 1.00 122.35 ? 459 LEU C C   1 
ATOM   8218  O  O   . LEU C 1 443 ? 138.828 175.198 135.009 1.00 122.35 ? 459 LEU C O   1 
ATOM   8219  C  CB  . LEU C 1 443 ? 136.546 176.147 136.847 1.00 122.35 ? 459 LEU C CB  1 
ATOM   8220  C  CG  . LEU C 1 443 ? 135.304 175.350 136.436 1.00 122.35 ? 459 LEU C CG  1 
ATOM   8221  C  CD1 . LEU C 1 443 ? 134.067 176.122 136.833 1.00 122.35 ? 459 LEU C CD1 1 
ATOM   8222  C  CD2 . LEU C 1 443 ? 135.270 175.073 134.938 1.00 122.35 ? 459 LEU C CD2 1 
ATOM   8223  N  N   . VAL C 1 444 ? 138.206 173.285 136.031 1.00 110.09 ? 460 VAL C N   1 
ATOM   8224  C  CA  . VAL C 1 444 ? 138.710 172.417 134.978 1.00 110.09 ? 460 VAL C CA  1 
ATOM   8225  C  C   . VAL C 1 444 ? 137.594 171.498 134.511 1.00 110.09 ? 460 VAL C C   1 
ATOM   8226  O  O   . VAL C 1 444 ? 136.908 170.870 135.324 1.00 110.09 ? 460 VAL C O   1 
ATOM   8227  C  CB  . VAL C 1 444 ? 139.920 171.583 135.446 1.00 110.09 ? 460 VAL C CB  1 
ATOM   8228  C  CG1 . VAL C 1 444 ? 141.169 172.439 135.505 1.00 110.09 ? 460 VAL C CG1 1 
ATOM   8229  C  CG2 . VAL C 1 444 ? 139.645 170.944 136.794 1.00 110.09 ? 460 VAL C CG2 1 
ATOM   8230  N  N   . CYS C 1 445 ? 137.412 171.428 133.200 1.00 112.87 ? 461 CYS C N   1 
ATOM   8231  C  CA  . CYS C 1 445 ? 136.495 170.475 132.593 1.00 112.87 ? 461 CYS C CA  1 
ATOM   8232  C  C   . CYS C 1 445 ? 137.319 169.257 132.200 1.00 112.87 ? 461 CYS C C   1 
ATOM   8233  O  O   . CYS C 1 445 ? 138.207 169.349 131.341 1.00 112.87 ? 461 CYS C O   1 
ATOM   8234  C  CB  . CYS C 1 445 ? 135.786 171.089 131.390 1.00 112.87 ? 461 CYS C CB  1 
ATOM   8235  S  SG  . CYS C 1 445 ? 134.731 169.946 130.484 1.00 112.87 ? 461 CYS C SG  1 
ATOM   8236  N  N   . TYR C 1 446 ? 137.086 168.147 132.892 1.00 112.26 ? 462 TYR C N   1 
ATOM   8237  C  CA  . TYR C 1 446 ? 137.886 166.942 132.744 1.00 112.26 ? 462 TYR C CA  1 
ATOM   8238  C  C   . TYR C 1 446 ? 137.011 165.851 132.145 1.00 112.26 ? 462 TYR C C   1 
ATOM   8239  O  O   . TYR C 1 446 ? 135.917 165.579 132.651 1.00 112.26 ? 462 TYR C O   1 
ATOM   8240  C  CB  . TYR C 1 446 ? 138.453 166.515 134.102 1.00 112.26 ? 462 TYR C CB  1 
ATOM   8241  C  CG  . TYR C 1 446 ? 139.092 165.141 134.186 1.00 112.26 ? 462 TYR C CG  1 
ATOM   8242  C  CD1 . TYR C 1 446 ? 139.681 164.541 133.078 1.00 112.26 ? 462 TYR C CD1 1 
ATOM   8243  C  CD2 . TYR C 1 446 ? 139.196 164.492 135.406 1.00 112.26 ? 462 TYR C CD2 1 
ATOM   8244  C  CE1 . TYR C 1 446 ? 140.288 163.306 133.177 1.00 112.26 ? 462 TYR C CE1 1 
ATOM   8245  C  CE2 . TYR C 1 446 ? 139.793 163.256 135.510 1.00 112.26 ? 462 TYR C CE2 1 
ATOM   8246  C  CZ  . TYR C 1 446 ? 140.338 162.667 134.395 1.00 112.26 ? 462 TYR C CZ  1 
ATOM   8247  O  OH  . TYR C 1 446 ? 140.939 161.435 134.504 1.00 112.26 ? 462 TYR C OH  1 
ATOM   8248  N  N   . ASN C 1 447 ? 137.489 165.233 131.069 1.00 126.21 ? 463 ASN C N   1 
ATOM   8249  C  CA  . ASN C 1 447 ? 136.837 164.077 130.461 1.00 126.21 ? 463 ASN C CA  1 
ATOM   8250  C  C   . ASN C 1 447 ? 137.634 162.788 130.703 1.00 126.21 ? 463 ASN C C   1 
ATOM   8251  O  O   . ASN C 1 447 ? 138.590 162.463 129.990 1.00 126.21 ? 463 ASN C O   1 
ATOM   8252  C  CB  . ASN C 1 447 ? 136.473 164.368 128.989 1.00 126.21 ? 463 ASN C CB  1 
ATOM   8253  C  CG  . ASN C 1 447 ? 137.560 164.108 127.944 1.00 126.21 ? 463 ASN C CG  1 
ATOM   8254  O  OD1 . ASN C 1 447 ? 138.738 163.908 128.214 1.00 126.21 ? 463 ASN C OD1 1 
ATOM   8255  N  ND2 . ASN C 1 447 ? 137.128 164.173 126.697 1.00 126.21 ? 463 ASN C ND2 1 
ATOM   8256  N  N   . PRO C 1 448 ? 137.305 162.052 131.771 1.00 114.72 ? 464 PRO C N   1 
ATOM   8257  C  CA  . PRO C 1 448 ? 138.162 160.935 132.213 1.00 114.72 ? 464 PRO C CA  1 
ATOM   8258  C  C   . PRO C 1 448 ? 138.360 159.790 131.234 1.00 114.72 ? 464 PRO C C   1 
ATOM   8259  O  O   . PRO C 1 448 ? 139.373 159.089 131.352 1.00 114.72 ? 464 PRO C O   1 
ATOM   8260  C  CB  . PRO C 1 448 ? 137.460 160.452 133.490 1.00 114.72 ? 464 PRO C CB  1 
ATOM   8261  C  CG  . PRO C 1 448 ? 136.620 161.603 133.938 1.00 114.72 ? 464 PRO C CG  1 
ATOM   8262  C  CD  . PRO C 1 448 ? 136.168 162.271 132.681 1.00 114.72 ? 464 PRO C CD  1 
ATOM   8263  N  N   . LEU C 1 449 ? 137.438 159.531 130.306 1.00 127.57 ? 465 LEU C N   1 
ATOM   8264  C  CA  . LEU C 1 449 ? 137.716 158.500 129.307 1.00 127.57 ? 465 LEU C CA  1 
ATOM   8265  C  C   . LEU C 1 449 ? 138.979 158.820 128.509 1.00 127.57 ? 465 LEU C C   1 
ATOM   8266  O  O   . LEU C 1 449 ? 139.661 157.909 128.026 1.00 127.57 ? 465 LEU C O   1 
ATOM   8267  C  CB  . LEU C 1 449 ? 136.510 158.308 128.388 1.00 127.57 ? 465 LEU C CB  1 
ATOM   8268  C  CG  . LEU C 1 449 ? 136.755 157.699 127.007 1.00 127.57 ? 465 LEU C CG  1 
ATOM   8269  C  CD1 . LEU C 1 449 ? 137.146 156.236 127.126 1.00 127.57 ? 465 LEU C CD1 1 
ATOM   8270  C  CD2 . LEU C 1 449 ? 135.520 157.817 126.172 1.00 127.57 ? 465 LEU C CD2 1 
ATOM   8271  N  N   . LEU C 1 450 ? 139.337 160.095 128.415 1.00 115.49 ? 466 LEU C N   1 
ATOM   8272  C  CA  . LEU C 1 450 ? 140.505 160.570 127.687 1.00 115.49 ? 466 LEU C CA  1 
ATOM   8273  C  C   . LEU C 1 450 ? 141.472 161.218 128.674 1.00 115.49 ? 466 LEU C C   1 
ATOM   8274  O  O   . LEU C 1 450 ? 141.286 161.153 129.891 1.00 115.49 ? 466 LEU C O   1 
ATOM   8275  C  CB  . LEU C 1 450 ? 140.107 161.536 126.571 1.00 115.49 ? 466 LEU C CB  1 
ATOM   8276  C  CG  . LEU C 1 450 ? 138.821 161.236 125.807 1.00 115.49 ? 466 LEU C CG  1 
ATOM   8277  C  CD1 . LEU C 1 450 ? 138.607 162.319 124.783 1.00 115.49 ? 466 LEU C CD1 1 
ATOM   8278  C  CD2 . LEU C 1 450 ? 138.884 159.874 125.137 1.00 115.49 ? 466 LEU C CD2 1 
ATOM   8279  N  N   . ASP C 1 451 ? 142.524 161.838 128.140 1.00 129.15 ? 467 ASP C N   1 
ATOM   8280  C  CA  . ASP C 1 451 ? 143.562 162.471 128.952 1.00 129.15 ? 467 ASP C CA  1 
ATOM   8281  C  C   . ASP C 1 451 ? 143.744 163.914 128.493 1.00 129.15 ? 467 ASP C C   1 
ATOM   8282  O  O   . ASP C 1 451 ? 144.602 164.208 127.656 1.00 129.15 ? 467 ASP C O   1 
ATOM   8283  C  CB  . ASP C 1 451 ? 144.868 161.688 128.859 1.00 129.15 ? 467 ASP C CB  1 
ATOM   8284  N  N   . SER C 1 452 ? 142.929 164.807 129.051 1.00 116.72 ? 468 SER C N   1 
ATOM   8285  C  CA  . SER C 1 452 ? 143.033 166.238 128.807 1.00 116.72 ? 468 SER C CA  1 
ATOM   8286  C  C   . SER C 1 452 ? 142.126 166.966 129.786 1.00 116.72 ? 468 SER C C   1 
ATOM   8287  O  O   . SER C 1 452 ? 141.029 166.493 130.092 1.00 116.72 ? 468 SER C O   1 
ATOM   8288  C  CB  . SER C 1 452 ? 142.646 166.596 127.365 1.00 116.72 ? 468 SER C CB  1 
ATOM   8289  O  OG  . SER C 1 452 ? 141.270 166.355 127.126 1.00 116.72 ? 468 SER C OG  1 
ATOM   8290  N  N   . PHE C 1 453 ? 142.594 168.115 130.266 1.00 112.68 ? 469 PHE C N   1 
ATOM   8291  C  CA  . PHE C 1 453 ? 141.855 168.955 131.199 1.00 112.68 ? 469 PHE C CA  1 
ATOM   8292  C  C   . PHE C 1 453 ? 141.795 170.349 130.599 1.00 112.68 ? 469 PHE C C   1 
ATOM   8293  O  O   . PHE C 1 453 ? 142.832 170.900 130.217 1.00 112.68 ? 469 PHE C O   1 
ATOM   8294  C  CB  . PHE C 1 453 ? 142.520 169.005 132.583 1.00 112.68 ? 469 PHE C CB  1 
ATOM   8295  C  CG  . PHE C 1 453 ? 142.936 167.661 133.118 1.00 112.68 ? 469 PHE C CG  1 
ATOM   8296  C  CD1 . PHE C 1 453 ? 144.086 167.038 132.659 1.00 112.68 ? 469 PHE C CD1 1 
ATOM   8297  C  CD2 . PHE C 1 453 ? 142.185 167.028 134.093 1.00 112.68 ? 469 PHE C CD2 1 
ATOM   8298  C  CE1 . PHE C 1 453 ? 144.470 165.808 133.153 1.00 112.68 ? 469 PHE C CE1 1 
ATOM   8299  C  CE2 . PHE C 1 453 ? 142.567 165.797 134.591 1.00 112.68 ? 469 PHE C CE2 1 
ATOM   8300  C  CZ  . PHE C 1 453 ? 143.710 165.187 134.120 1.00 112.68 ? 469 PHE C CZ  1 
ATOM   8301  N  N   . THR C 1 454 ? 140.600 170.921 130.511 1.00 115.84 ? 470 THR C N   1 
ATOM   8302  C  CA  . THR C 1 454 ? 140.488 172.305 130.077 1.00 115.84 ? 470 THR C CA  1 
ATOM   8303  C  C   . THR C 1 454 ? 140.199 173.224 131.256 1.00 115.84 ? 470 THR C C   1 
ATOM   8304  O  O   . THR C 1 454 ? 139.782 172.782 132.326 1.00 115.84 ? 470 THR C O   1 
ATOM   8305  C  CB  . THR C 1 454 ? 139.404 172.439 129.014 1.00 115.84 ? 470 THR C CB  1 
ATOM   8306  O  OG1 . THR C 1 454 ? 138.137 172.086 129.576 1.00 115.84 ? 470 THR C OG1 1 
ATOM   8307  C  CG2 . THR C 1 454 ? 139.712 171.485 127.890 1.00 115.84 ? 470 THR C CG2 1 
ATOM   8308  N  N   . ARG C 1 455 ? 140.391 174.524 131.033 1.00 126.47 ? 471 ARG C N   1 
ATOM   8309  C  CA  . ARG C 1 455 ? 140.158 175.529 132.061 1.00 126.47 ? 471 ARG C CA  1 
ATOM   8310  C  C   . ARG C 1 455 ? 139.276 176.647 131.527 1.00 126.47 ? 471 ARG C C   1 
ATOM   8311  O  O   . ARG C 1 455 ? 139.431 177.083 130.383 1.00 126.47 ? 471 ARG C O   1 
ATOM   8312  C  CB  . ARG C 1 455 ? 141.483 176.122 132.556 1.00 126.47 ? 471 ARG C CB  1 
ATOM   8313  C  CG  . ARG C 1 455 ? 142.032 175.486 133.820 1.00 126.47 ? 471 ARG C CG  1 
ATOM   8314  C  CD  . ARG C 1 455 ? 142.465 176.544 134.821 1.00 126.47 ? 471 ARG C CD  1 
ATOM   8315  N  NE  . ARG C 1 455 ? 143.063 175.964 136.017 1.00 126.47 ? 471 ARG C NE  1 
ATOM   8316  C  CZ  . ARG C 1 455 ? 144.309 175.515 136.090 1.00 126.47 ? 471 ARG C CZ  1 
ATOM   8317  N  NH1 . ARG C 1 455 ? 145.112 175.531 135.039 1.00 126.47 ? 471 ARG C NH1 1 
ATOM   8318  N  NH2 . ARG C 1 455 ? 144.759 175.035 137.246 1.00 126.47 ? 471 ARG C NH2 1 
ATOM   8319  N  N   . LEU C 1 456 ? 138.356 177.110 132.371 1.00 144.85 ? 472 LEU C N   1 
ATOM   8320  C  CA  . LEU C 1 456 ? 137.456 178.211 132.057 1.00 144.85 ? 472 LEU C CA  1 
ATOM   8321  C  C   . LEU C 1 456 ? 137.667 179.337 133.059 1.00 144.85 ? 472 LEU C C   1 
ATOM   8322  O  O   . LEU C 1 456 ? 137.819 179.090 134.261 1.00 144.85 ? 472 LEU C O   1 
ATOM   8323  C  CB  . LEU C 1 456 ? 135.983 177.771 132.075 1.00 144.85 ? 472 LEU C CB  1 
ATOM   8324  C  CG  . LEU C 1 456 ? 135.539 176.452 131.434 1.00 144.85 ? 472 LEU C CG  1 
ATOM   8325  C  CD1 . LEU C 1 456 ? 134.034 176.474 131.229 1.00 144.85 ? 472 LEU C CD1 1 
ATOM   8326  C  CD2 . LEU C 1 456 ? 136.238 176.208 130.106 1.00 144.85 ? 472 LEU C CD2 1 
ATOM   8327  N  N   . CYS C 1 457 ? 137.677 180.571 132.563 1.00 152.16 ? 473 CYS C N   1 
ATOM   8328  C  CA  . CYS C 1 457 ? 137.879 181.722 133.431 1.00 152.16 ? 473 CYS C CA  1 
ATOM   8329  C  C   . CYS C 1 457 ? 136.658 181.946 134.315 1.00 152.16 ? 473 CYS C C   1 
ATOM   8330  O  O   . CYS C 1 457 ? 135.515 181.880 133.853 1.00 152.16 ? 473 CYS C O   1 
ATOM   8331  C  CB  . CYS C 1 457 ? 138.161 182.973 132.600 1.00 152.16 ? 473 CYS C CB  1 
ATOM   8332  N  N   . LEU C 1 458 ? 136.905 182.215 135.587 1.00 161.92 ? 474 LEU C N   1 
ATOM   8333  C  CA  . LEU C 1 458 ? 135.870 182.537 136.554 1.00 161.92 ? 474 LEU C CA  1 
ATOM   8334  C  C   . LEU C 1 458 ? 135.770 184.050 136.720 1.00 161.92 ? 474 LEU C C   1 
ATOM   8335  O  O   . LEU C 1 458 ? 136.624 184.796 136.233 1.00 161.92 ? 474 LEU C O   1 
ATOM   8336  C  CB  . LEU C 1 458 ? 136.195 181.857 137.889 1.00 161.92 ? 474 LEU C CB  1 
ATOM   8337  C  CG  . LEU C 1 458 ? 135.650 180.439 138.088 1.00 161.92 ? 474 LEU C CG  1 
ATOM   8338  C  CD1 . LEU C 1 458 ? 135.899 179.957 139.510 1.00 161.92 ? 474 LEU C CD1 1 
ATOM   8339  C  CD2 . LEU C 1 458 ? 134.172 180.346 137.735 1.00 161.92 ? 474 LEU C CD2 1 
ATOM   8340  N  N   . PRO C 1 459 ? 134.723 184.559 137.413 1.00 175.63 ? 475 PRO C N   1 
ATOM   8341  C  CA  . PRO C 1 459 ? 134.542 186.019 137.464 1.00 175.63 ? 475 PRO C CA  1 
ATOM   8342  C  C   . PRO C 1 459 ? 135.534 186.728 138.375 1.00 175.63 ? 475 PRO C C   1 
ATOM   8343  O  O   . PRO C 1 459 ? 135.372 187.920 138.657 1.00 175.63 ? 475 PRO C O   1 
ATOM   8344  C  CB  . PRO C 1 459 ? 133.103 186.180 137.970 1.00 175.63 ? 475 PRO C CB  1 
ATOM   8345  C  CG  . PRO C 1 459 ? 132.827 184.947 138.727 1.00 175.63 ? 475 PRO C CG  1 
ATOM   8346  C  CD  . PRO C 1 459 ? 133.586 183.854 138.037 1.00 175.63 ? 475 PRO C CD  1 
ATOM   8347  N  N   . GLU C 1 460 ? 136.557 186.009 138.842 1.00 182.01 ? 476 GLU C N   1 
ATOM   8348  C  CA  . GLU C 1 460 ? 137.651 186.584 139.626 1.00 182.01 ? 476 GLU C CA  1 
ATOM   8349  C  C   . GLU C 1 460 ? 137.124 187.247 140.902 1.00 182.01 ? 476 GLU C C   1 
ATOM   8350  O  O   . GLU C 1 460 ? 137.241 188.457 141.105 1.00 182.01 ? 476 GLU C O   1 
ATOM   8351  C  CB  . GLU C 1 460 ? 138.469 187.570 138.785 1.00 182.01 ? 476 GLU C CB  1 
ATOM   8352  N  N   . ALA C 1 461 ? 136.532 186.424 141.761 1.00 172.40 ? 477 ALA C N   1 
ATOM   8353  C  CA  . ALA C 1 461 ? 136.015 186.896 143.041 1.00 172.40 ? 477 ALA C CA  1 
ATOM   8354  C  C   . ALA C 1 461 ? 137.144 187.363 143.953 1.00 172.40 ? 477 ALA C C   1 
ATOM   8355  O  O   . ALA C 1 461 ? 138.113 186.638 144.180 1.00 172.40 ? 477 ALA C O   1 
ATOM   8356  C  CB  . ALA C 1 461 ? 135.203 185.804 143.718 1.00 172.40 ? 477 ALA C CB  1 
ATOM   8357  N  N   . LEU C 1 468 ? 136.045 179.790 147.859 1.00 122.86 ? 484 LEU C N   1 
ATOM   8358  C  CA  . LEU C 1 468 ? 135.796 178.354 147.890 1.00 122.86 ? 484 LEU C CA  1 
ATOM   8359  C  C   . LEU C 1 468 ? 134.466 178.015 147.227 1.00 122.86 ? 484 LEU C C   1 
ATOM   8360  O  O   . LEU C 1 468 ? 133.459 177.807 147.904 1.00 122.86 ? 484 LEU C O   1 
ATOM   8361  C  CB  . LEU C 1 468 ? 135.815 177.837 149.329 1.00 122.86 ? 484 LEU C CB  1 
ATOM   8362  N  N   . TRP C 1 469 ? 134.471 177.960 145.899 1.00 132.53 ? 485 TRP C N   1 
ATOM   8363  C  CA  . TRP C 1 469 ? 133.259 177.659 145.153 1.00 132.53 ? 485 TRP C CA  1 
ATOM   8364  C  C   . TRP C 1 469 ? 132.852 176.200 145.328 1.00 132.53 ? 485 TRP C C   1 
ATOM   8365  O  O   . TRP C 1 469 ? 133.679 175.325 145.597 1.00 132.53 ? 485 TRP C O   1 
ATOM   8366  C  CB  . TRP C 1 469 ? 133.454 177.959 143.667 1.00 132.53 ? 485 TRP C CB  1 
ATOM   8367  C  CG  . TRP C 1 469 ? 133.789 179.384 143.369 1.00 132.53 ? 485 TRP C CG  1 
ATOM   8368  C  CD1 . TRP C 1 469 ? 134.999 179.879 142.980 1.00 132.53 ? 485 TRP C CD1 1 
ATOM   8369  C  CD2 . TRP C 1 469 ? 132.896 180.502 143.422 1.00 132.53 ? 485 TRP C CD2 1 
ATOM   8370  N  NE1 . TRP C 1 469 ? 134.917 181.237 142.793 1.00 132.53 ? 485 TRP C NE1 1 
ATOM   8371  C  CE2 . TRP C 1 469 ? 133.636 181.644 143.059 1.00 132.53 ? 485 TRP C CE2 1 
ATOM   8372  C  CE3 . TRP C 1 469 ? 131.544 180.649 143.746 1.00 132.53 ? 485 TRP C CE3 1 
ATOM   8373  C  CZ2 . TRP C 1 469 ? 133.069 182.915 143.009 1.00 132.53 ? 485 TRP C CZ2 1 
ATOM   8374  C  CZ3 . TRP C 1 469 ? 130.984 181.911 143.696 1.00 132.53 ? 485 TRP C CZ3 1 
ATOM   8375  C  CH2 . TRP C 1 469 ? 131.745 183.027 143.331 1.00 132.53 ? 485 TRP C CH2 1 
ATOM   8376  N  N   . LYS C 1 470 ? 131.555 175.948 145.171 1.00 103.05 ? 486 LYS C N   1 
ATOM   8377  C  CA  . LYS C 1 470 ? 131.011 174.598 145.117 1.00 103.05 ? 486 LYS C CA  1 
ATOM   8378  C  C   . LYS C 1 470 ? 130.058 174.524 143.935 1.00 103.05 ? 486 LYS C C   1 
ATOM   8379  O  O   . LYS C 1 470 ? 129.156 175.355 143.807 1.00 103.05 ? 486 LYS C O   1 
ATOM   8380  C  CB  . LYS C 1 470 ? 130.295 174.227 146.419 1.00 103.05 ? 486 LYS C CB  1 
ATOM   8381  C  CG  . LYS C 1 470 ? 131.226 174.073 147.610 1.00 103.05 ? 486 LYS C CG  1 
ATOM   8382  C  CD  . LYS C 1 470 ? 130.460 173.750 148.880 1.00 103.05 ? 486 LYS C CD  1 
ATOM   8383  C  CE  . LYS C 1 470 ? 131.373 173.774 150.093 1.00 103.05 ? 486 LYS C CE  1 
ATOM   8384  N  NZ  . LYS C 1 470 ? 132.049 172.465 150.302 1.00 103.05 ? 486 LYS C NZ  1 
ATOM   8385  N  N   . ILE C 1 471 ? 130.259 173.537 143.080 1.00 103.22 ? 487 ILE C N   1 
ATOM   8386  C  CA  . ILE C 1 471 ? 129.543 173.446 141.816 1.00 103.22 ? 487 ILE C CA  1 
ATOM   8387  C  C   . ILE C 1 471 ? 128.448 172.395 141.930 1.00 103.22 ? 487 ILE C C   1 
ATOM   8388  O  O   . ILE C 1 471 ? 128.535 171.460 142.734 1.00 103.22 ? 487 ILE C O   1 
ATOM   8389  C  CB  . ILE C 1 471 ? 130.532 173.139 140.670 1.00 103.22 ? 487 ILE C CB  1 
ATOM   8390  C  CG1 . ILE C 1 471 ? 129.837 173.180 139.312 1.00 103.22 ? 487 ILE C CG1 1 
ATOM   8391  C  CG2 . ILE C 1 471 ? 131.208 171.794 140.894 1.00 103.22 ? 487 ILE C CG2 1 
ATOM   8392  C  CD1 . ILE C 1 471 ? 130.801 173.215 138.169 1.00 103.22 ? 487 ILE C CD1 1 
ATOM   8393  N  N   . ALA C 1 472 ? 127.397 172.551 141.124 1.00 107.08 ? 488 ALA C N   1 
ATOM   8394  C  CA  . ALA C 1 472 ? 126.310 171.583 141.098 1.00 107.08 ? 488 ALA C CA  1 
ATOM   8395  C  C   . ALA C 1 472 ? 125.643 171.605 139.733 1.00 107.08 ? 488 ALA C C   1 
ATOM   8396  O  O   . ALA C 1 472 ? 125.285 172.673 139.227 1.00 107.08 ? 488 ALA C O   1 
ATOM   8397  C  CB  . ALA C 1 472 ? 125.280 171.877 142.192 1.00 107.08 ? 488 ALA C CB  1 
ATOM   8398  N  N   . SER C 1 473 ? 125.482 170.428 139.142 1.00 117.97 ? 489 SER C N   1 
ATOM   8399  C  CA  . SER C 1 473 ? 124.874 170.317 137.828 1.00 117.97 ? 489 SER C CA  1 
ATOM   8400  C  C   . SER C 1 473 ? 123.381 170.041 137.953 1.00 117.97 ? 489 SER C C   1 
ATOM   8401  O  O   . SER C 1 473 ? 122.923 169.383 138.890 1.00 117.97 ? 489 SER C O   1 
ATOM   8402  C  CB  . SER C 1 473 ? 125.542 169.207 137.015 1.00 117.97 ? 489 SER C CB  1 
ATOM   8403  O  OG  . SER C 1 473 ? 124.989 169.124 135.713 1.00 117.97 ? 489 SER C OG  1 
ATOM   8404  N  N   . CYS C 1 474 ? 122.626 170.559 136.993 1.00 137.84 ? 490 CYS C N   1 
ATOM   8405  C  CA  . CYS C 1 474 ? 121.188 170.361 136.900 1.00 137.84 ? 490 CYS C CA  1 
ATOM   8406  C  C   . CYS C 1 474 ? 120.883 169.625 135.598 1.00 137.84 ? 490 CYS C C   1 
ATOM   8407  O  O   . CYS C 1 474 ? 121.785 169.108 134.932 1.00 137.84 ? 490 CYS C O   1 
ATOM   8408  C  CB  . CYS C 1 474 ? 120.450 171.698 136.986 1.00 137.84 ? 490 CYS C CB  1 
ATOM   8409  S  SG  . CYS C 1 474 ? 118.648 171.552 136.985 1.00 137.84 ? 490 CYS C SG  1 
ATOM   8410  N  N   . ASN C 1 475 ? 119.592 169.549 135.260 1.00 151.50 ? 491 ASN C N   1 
ATOM   8411  C  CA  . ASN C 1 475 ? 119.175 168.838 134.055 1.00 151.50 ? 491 ASN C CA  1 
ATOM   8412  C  C   . ASN C 1 475 ? 119.961 169.303 132.834 1.00 151.50 ? 491 ASN C C   1 
ATOM   8413  O  O   . ASN C 1 475 ? 120.383 168.486 132.008 1.00 151.50 ? 491 ASN C O   1 
ATOM   8414  C  CB  . ASN C 1 475 ? 117.674 169.026 133.829 1.00 151.50 ? 491 ASN C CB  1 
ATOM   8415  N  N   . GLY C 1 476 ? 120.166 170.612 132.704 1.00 142.99 ? 492 GLY C N   1 
ATOM   8416  C  CA  . GLY C 1 476 ? 120.954 171.146 131.611 1.00 142.99 ? 492 GLY C CA  1 
ATOM   8417  C  C   . GLY C 1 476 ? 121.744 172.387 131.976 1.00 142.99 ? 492 GLY C C   1 
ATOM   8418  O  O   . GLY C 1 476 ? 122.308 173.044 131.096 1.00 142.99 ? 492 GLY C O   1 
ATOM   8419  N  N   . SER C 1 477 ? 121.799 172.719 133.265 1.00 129.36 ? 493 SER C N   1 
ATOM   8420  C  CA  . SER C 1 477 ? 122.406 173.961 133.721 1.00 129.36 ? 493 SER C CA  1 
ATOM   8421  C  C   . SER C 1 477 ? 123.433 173.683 134.809 1.00 129.36 ? 493 SER C C   1 
ATOM   8422  O  O   . SER C 1 477 ? 123.329 172.702 135.550 1.00 129.36 ? 493 SER C O   1 
ATOM   8423  C  CB  . SER C 1 477 ? 121.345 174.938 134.248 1.00 129.36 ? 493 SER C CB  1 
ATOM   8424  O  OG  . SER C 1 477 ? 120.263 175.051 133.341 1.00 129.36 ? 493 SER C OG  1 
ATOM   8425  N  N   . ILE C 1 478 ? 124.428 174.563 134.897 1.00 119.33 ? 494 ILE C N   1 
ATOM   8426  C  CA  . ILE C 1 478 ? 125.492 174.479 135.891 1.00 119.33 ? 494 ILE C CA  1 
ATOM   8427  C  C   . ILE C 1 478 ? 125.351 175.657 136.843 1.00 119.33 ? 494 ILE C C   1 
ATOM   8428  O  O   . ILE C 1 478 ? 125.338 176.815 136.407 1.00 119.33 ? 494 ILE C O   1 
ATOM   8429  C  CB  . ILE C 1 478 ? 126.881 174.479 135.231 1.00 119.33 ? 494 ILE C CB  1 
ATOM   8430  C  CG1 . ILE C 1 478 ? 126.938 173.454 134.099 1.00 119.33 ? 494 ILE C CG1 1 
ATOM   8431  C  CG2 . ILE C 1 478 ? 127.953 174.197 136.262 1.00 119.33 ? 494 ILE C CG2 1 
ATOM   8432  C  CD1 . ILE C 1 478 ? 128.281 173.388 133.406 1.00 119.33 ? 494 ILE C CD1 1 
ATOM   8433  N  N   . TYR C 1 479 ? 125.268 175.369 138.142 1.00 114.65 ? 495 TYR C N   1 
ATOM   8434  C  CA  . TYR C 1 479 ? 125.119 176.394 139.166 1.00 114.65 ? 495 TYR C CA  1 
ATOM   8435  C  C   . TYR C 1 479 ? 126.339 176.369 140.076 1.00 114.65 ? 495 TYR C C   1 
ATOM   8436  O  O   . TYR C 1 479 ? 126.653 175.333 140.672 1.00 114.65 ? 495 TYR C O   1 
ATOM   8437  C  CB  . TYR C 1 479 ? 123.841 176.173 139.976 1.00 114.65 ? 495 TYR C CB  1 
ATOM   8438  C  CG  . TYR C 1 479 ? 122.566 176.505 139.234 1.00 114.65 ? 495 TYR C CG  1 
ATOM   8439  C  CD1 . TYR C 1 479 ? 122.064 177.799 139.219 1.00 114.65 ? 495 TYR C CD1 1 
ATOM   8440  C  CD2 . TYR C 1 479 ? 121.860 175.520 138.557 1.00 114.65 ? 495 TYR C CD2 1 
ATOM   8441  C  CE1 . TYR C 1 479 ? 120.896 178.103 138.545 1.00 114.65 ? 495 TYR C CE1 1 
ATOM   8442  C  CE2 . TYR C 1 479 ? 120.693 175.815 137.881 1.00 114.65 ? 495 TYR C CE2 1 
ATOM   8443  C  CZ  . TYR C 1 479 ? 120.216 177.107 137.879 1.00 114.65 ? 495 TYR C CZ  1 
ATOM   8444  O  OH  . TYR C 1 479 ? 119.053 177.405 137.207 1.00 114.65 ? 495 TYR C OH  1 
ATOM   8445  N  N   . VAL C 1 480 ? 127.018 177.505 140.183 1.00 115.67 ? 496 VAL C N   1 
ATOM   8446  C  CA  . VAL C 1 480 ? 128.146 177.670 141.091 1.00 115.67 ? 496 VAL C CA  1 
ATOM   8447  C  C   . VAL C 1 480 ? 127.671 178.446 142.310 1.00 115.67 ? 496 VAL C C   1 
ATOM   8448  O  O   . VAL C 1 480 ? 126.923 179.424 142.186 1.00 115.67 ? 496 VAL C O   1 
ATOM   8449  C  CB  . VAL C 1 480 ? 129.321 178.386 140.400 1.00 115.67 ? 496 VAL C CB  1 
ATOM   8450  C  CG1 . VAL C 1 480 ? 130.578 178.285 141.248 1.00 115.67 ? 496 VAL C CG1 1 
ATOM   8451  C  CG2 . VAL C 1 480 ? 129.556 177.807 139.014 1.00 115.67 ? 496 VAL C CG2 1 
ATOM   8452  N  N   . PHE C 1 481 ? 128.091 178.010 143.493 1.00 113.67 ? 497 PHE C N   1 
ATOM   8453  C  CA  . PHE C 1 481 ? 127.658 178.621 144.738 1.00 113.67 ? 497 PHE C CA  1 
ATOM   8454  C  C   . PHE C 1 481 ? 128.877 179.013 145.557 1.00 113.67 ? 497 PHE C C   1 
ATOM   8455  O  O   . PHE C 1 481 ? 129.869 178.279 145.601 1.00 113.67 ? 497 PHE C O   1 
ATOM   8456  C  CB  . PHE C 1 481 ? 126.776 177.668 145.552 1.00 113.67 ? 497 PHE C CB  1 
ATOM   8457  C  CG  . PHE C 1 481 ? 125.523 177.237 144.846 1.00 113.67 ? 497 PHE C CG  1 
ATOM   8458  C  CD1 . PHE C 1 481 ? 125.538 176.162 143.974 1.00 113.67 ? 497 PHE C CD1 1 
ATOM   8459  C  CD2 . PHE C 1 481 ? 124.327 177.901 145.060 1.00 113.67 ? 497 PHE C CD2 1 
ATOM   8460  C  CE1 . PHE C 1 481 ? 124.387 175.759 143.331 1.00 113.67 ? 497 PHE C CE1 1 
ATOM   8461  C  CE2 . PHE C 1 481 ? 123.173 177.503 144.415 1.00 113.67 ? 497 PHE C CE2 1 
ATOM   8462  C  CZ  . PHE C 1 481 ? 123.203 176.431 143.549 1.00 113.67 ? 497 PHE C CZ  1 
ATOM   8463  N  N   . ARG C 1 482 ? 128.797 180.171 146.205 1.00 129.94 ? 498 ARG C N   1 
ATOM   8464  C  CA  . ARG C 1 482 ? 129.869 180.626 147.077 1.00 129.94 ? 498 ARG C CA  1 
ATOM   8465  C  C   . ARG C 1 482 ? 129.749 179.957 148.439 1.00 129.94 ? 498 ARG C C   1 
ATOM   8466  O  O   . ARG C 1 482 ? 128.643 179.712 148.929 1.00 129.94 ? 498 ARG C O   1 
ATOM   8467  C  CB  . ARG C 1 482 ? 129.828 182.146 147.231 1.00 129.94 ? 498 ARG C CB  1 
ATOM   8468  N  N   . ASP C 1 483 ? 130.898 179.652 149.047 1.00 128.84 ? 499 ASP C N   1 
ATOM   8469  C  CA  . ASP C 1 483 ? 130.891 179.026 150.366 1.00 128.84 ? 499 ASP C CA  1 
ATOM   8470  C  C   . ASP C 1 483 ? 130.190 179.909 151.390 1.00 128.84 ? 499 ASP C C   1 
ATOM   8471  O  O   . ASP C 1 483 ? 129.469 179.411 152.261 1.00 128.84 ? 499 ASP C O   1 
ATOM   8472  C  CB  . ASP C 1 483 ? 132.321 178.719 150.810 1.00 128.84 ? 499 ASP C CB  1 
ATOM   8473  N  N   . ARG C 1 484 ? 130.388 181.221 151.299 1.00 136.78 ? 500 ARG C N   1 
ATOM   8474  C  CA  . ARG C 1 484 ? 129.731 182.185 152.168 1.00 136.78 ? 500 ARG C CA  1 
ATOM   8475  C  C   . ARG C 1 484 ? 128.850 183.099 151.330 1.00 136.78 ? 500 ARG C C   1 
ATOM   8476  O  O   . ARG C 1 484 ? 129.255 183.547 150.252 1.00 136.78 ? 500 ARG C O   1 
ATOM   8477  C  CB  . ARG C 1 484 ? 130.752 183.013 152.955 1.00 136.78 ? 500 ARG C CB  1 
ATOM   8478  N  N   . TYR C 1 485 ? 127.642 183.358 151.823 1.00 138.84 ? 501 TYR C N   1 
ATOM   8479  C  CA  . TYR C 1 485 ? 126.675 184.196 151.120 1.00 138.84 ? 501 TYR C CA  1 
ATOM   8480  C  C   . TYR C 1 485 ? 127.239 185.581 150.812 1.00 138.84 ? 501 TYR C C   1 
ATOM   8481  O  O   . TYR C 1 485 ? 127.534 185.898 149.659 1.00 138.84 ? 501 TYR C O   1 
ATOM   8482  C  CB  . TYR C 1 485 ? 125.390 184.328 151.940 1.00 138.84 ? 501 TYR C CB  1 
ATOM   8483  N  N   . ALA C 1 490 ? 126.797 188.338 145.024 1.00 143.16 ? 506 ALA C N   1 
ATOM   8484  C  CA  . ALA C 1 490 ? 125.761 187.343 144.774 1.00 143.16 ? 506 ALA C CA  1 
ATOM   8485  C  C   . ALA C 1 490 ? 126.136 186.001 145.393 1.00 143.16 ? 506 ALA C C   1 
ATOM   8486  O  O   . ALA C 1 490 ? 127.313 185.649 145.467 1.00 143.16 ? 506 ALA C O   1 
ATOM   8487  C  CB  . ALA C 1 490 ? 125.522 187.191 143.283 1.00 143.16 ? 506 ALA C CB  1 
ATOM   8488  N  N   . ASN C 1 491 ? 125.126 185.254 145.839 1.00 131.12 ? 507 ASN C N   1 
ATOM   8489  C  CA  . ASN C 1 491 ? 125.361 183.960 146.464 1.00 131.12 ? 507 ASN C CA  1 
ATOM   8490  C  C   . ASN C 1 491 ? 125.345 182.803 145.475 1.00 131.12 ? 507 ASN C C   1 
ATOM   8491  O  O   . ASN C 1 491 ? 125.939 181.758 145.760 1.00 131.12 ? 507 ASN C O   1 
ATOM   8492  C  CB  . ASN C 1 491 ? 124.317 183.705 147.556 1.00 131.12 ? 507 ASN C CB  1 
ATOM   8493  N  N   . THR C 1 492 ? 124.687 182.959 144.328 1.00 138.71 ? 508 THR C N   1 
ATOM   8494  C  CA  . THR C 1 492 ? 124.608 181.898 143.336 1.00 138.71 ? 508 THR C CA  1 
ATOM   8495  C  C   . THR C 1 492 ? 124.866 182.479 141.954 1.00 138.71 ? 508 THR C C   1 
ATOM   8496  O  O   . THR C 1 492 ? 124.548 183.639 141.681 1.00 138.71 ? 508 THR C O   1 
ATOM   8497  C  CB  . THR C 1 492 ? 123.243 181.195 143.363 1.00 138.71 ? 508 THR C CB  1 
ATOM   8498  O  OG1 . THR C 1 492 ? 123.152 180.275 142.268 1.00 138.71 ? 508 THR C OG1 1 
ATOM   8499  C  CG2 . THR C 1 492 ? 122.115 182.211 143.262 1.00 138.71 ? 508 THR C CG2 1 
ATOM   8500  N  N   . TYR C 1 493 ? 125.453 181.659 141.083 1.00 126.03 ? 509 TYR C N   1 
ATOM   8501  C  CA  . TYR C 1 493 ? 125.757 182.057 139.719 1.00 126.03 ? 509 TYR C CA  1 
ATOM   8502  C  C   . TYR C 1 493 ? 125.441 180.899 138.783 1.00 126.03 ? 509 TYR C C   1 
ATOM   8503  O  O   . TYR C 1 493 ? 125.458 179.733 139.184 1.00 126.03 ? 509 TYR C O   1 
ATOM   8504  C  CB  . TYR C 1 493 ? 127.223 182.486 139.569 1.00 126.03 ? 509 TYR C CB  1 
ATOM   8505  C  CG  . TYR C 1 493 ? 127.679 183.525 140.575 1.00 126.03 ? 509 TYR C CG  1 
ATOM   8506  C  CD1 . TYR C 1 493 ? 128.086 183.153 141.852 1.00 126.03 ? 509 TYR C CD1 1 
ATOM   8507  C  CD2 . TYR C 1 493 ? 127.689 184.875 140.255 1.00 126.03 ? 509 TYR C CD2 1 
ATOM   8508  C  CE1 . TYR C 1 493 ? 128.498 184.096 142.773 1.00 126.03 ? 509 TYR C CE1 1 
ATOM   8509  C  CE2 . TYR C 1 493 ? 128.102 185.825 141.170 1.00 126.03 ? 509 TYR C CE2 1 
ATOM   8510  C  CZ  . TYR C 1 493 ? 128.504 185.429 142.428 1.00 126.03 ? 509 TYR C CZ  1 
ATOM   8511  O  OH  . TYR C 1 493 ? 128.915 186.371 143.343 1.00 126.03 ? 509 TYR C OH  1 
ATOM   8512  N  N   . LYS C 1 494 ? 125.169 181.226 137.523 1.00 127.29 ? 510 LYS C N   1 
ATOM   8513  C  CA  . LYS C 1 494 ? 124.900 180.238 136.488 1.00 127.29 ? 510 LYS C CA  1 
ATOM   8514  C  C   . LYS C 1 494 ? 126.010 180.292 135.449 1.00 127.29 ? 510 LYS C C   1 
ATOM   8515  O  O   . LYS C 1 494 ? 126.312 181.363 134.909 1.00 127.29 ? 510 LYS C O   1 
ATOM   8516  C  CB  . LYS C 1 494 ? 123.545 180.489 135.825 1.00 127.29 ? 510 LYS C CB  1 
ATOM   8517  C  CG  . LYS C 1 494 ? 123.272 179.611 134.615 1.00 127.29 ? 510 LYS C CG  1 
ATOM   8518  C  CD  . LYS C 1 494 ? 121.795 179.612 134.257 1.00 127.29 ? 510 LYS C CD  1 
ATOM   8519  C  CE  . LYS C 1 494 ? 121.515 178.714 133.063 1.00 127.29 ? 510 LYS C CE  1 
ATOM   8520  N  NZ  . LYS C 1 494 ? 122.722 177.947 132.645 1.00 127.29 ? 510 LYS C NZ  1 
ATOM   8521  N  N   . LEU C 1 495 ? 126.627 179.141 135.195 1.00 124.38 ? 511 LEU C N   1 
ATOM   8522  C  CA  . LEU C 1 495 ? 127.765 179.034 134.294 1.00 124.38 ? 511 LEU C CA  1 
ATOM   8523  C  C   . LEU C 1 495 ? 127.277 178.517 132.947 1.00 124.38 ? 511 LEU C C   1 
ATOM   8524  O  O   . LEU C 1 495 ? 126.685 177.436 132.871 1.00 124.38 ? 511 LEU C O   1 
ATOM   8525  C  CB  . LEU C 1 495 ? 128.827 178.105 134.883 1.00 124.38 ? 511 LEU C CB  1 
ATOM   8526  C  CG  . LEU C 1 495 ? 130.289 178.127 134.417 1.00 124.38 ? 511 LEU C CG  1 
ATOM   8527  C  CD1 . LEU C 1 495 ? 131.063 177.068 135.176 1.00 124.38 ? 511 LEU C CD1 1 
ATOM   8528  C  CD2 . LEU C 1 495 ? 130.459 177.915 132.916 1.00 124.38 ? 511 LEU C CD2 1 
ATOM   8529  N  N   . ASP C 1 496 ? 127.528 179.287 131.889 1.00 149.44 ? 512 ASP C N   1 
ATOM   8530  C  CA  . ASP C 1 496 ? 127.209 178.851 130.537 1.00 149.44 ? 512 ASP C CA  1 
ATOM   8531  C  C   . ASP C 1 496 ? 128.436 178.149 129.974 1.00 149.44 ? 512 ASP C C   1 
ATOM   8532  O  O   . ASP C 1 496 ? 129.466 178.805 129.765 1.00 149.44 ? 512 ASP C O   1 
ATOM   8533  C  CB  . ASP C 1 496 ? 126.817 180.032 129.663 1.00 149.44 ? 512 ASP C CB  1 
ATOM   8534  C  CG  . ASP C 1 496 ? 126.388 179.610 128.272 1.00 149.44 ? 512 ASP C CG  1 
ATOM   8535  O  OD1 . ASP C 1 496 ? 125.802 178.515 128.138 1.00 149.44 ? 512 ASP C OD1 1 
ATOM   8536  O  OD2 . ASP C 1 496 ? 126.632 180.374 127.315 1.00 149.44 ? 512 ASP C OD2 1 
ATOM   8537  N  N   . PRO C 1 497 ? 128.386 176.838 129.720 1.00 134.05 ? 513 PRO C N   1 
ATOM   8538  C  CA  . PRO C 1 497 ? 129.593 176.145 129.236 1.00 134.05 ? 513 PRO C CA  1 
ATOM   8539  C  C   . PRO C 1 497 ? 130.123 176.684 127.918 1.00 134.05 ? 513 PRO C C   1 
ATOM   8540  O  O   . PRO C 1 497 ? 131.343 176.739 127.723 1.00 134.05 ? 513 PRO C O   1 
ATOM   8541  C  CB  . PRO C 1 497 ? 129.129 174.687 129.108 1.00 134.05 ? 513 PRO C CB  1 
ATOM   8542  C  CG  . PRO C 1 497 ? 127.872 174.593 129.923 1.00 134.05 ? 513 PRO C CG  1 
ATOM   8543  C  CD  . PRO C 1 497 ? 127.231 175.935 129.838 1.00 134.05 ? 513 PRO C CD  1 
ATOM   8544  N  N   . ALA C 1 498 ? 129.237 177.080 127.003 1.00 146.63 ? 514 ALA C N   1 
ATOM   8545  C  CA  . ALA C 1 498 ? 129.677 177.511 125.680 1.00 146.63 ? 514 ALA C CA  1 
ATOM   8546  C  C   . ALA C 1 498 ? 130.408 178.848 125.743 1.00 146.63 ? 514 ALA C C   1 
ATOM   8547  O  O   . ALA C 1 498 ? 131.495 179.001 125.173 1.00 146.63 ? 514 ALA C O   1 
ATOM   8548  C  CB  . ALA C 1 498 ? 128.480 177.596 124.733 1.00 146.63 ? 514 ALA C CB  1 
ATOM   8549  N  N   . THR C 1 499 ? 129.827 179.828 126.434 1.00 141.02 ? 515 THR C N   1 
ATOM   8550  C  CA  . THR C 1 499 ? 130.382 181.173 126.511 1.00 141.02 ? 515 THR C CA  1 
ATOM   8551  C  C   . THR C 1 499 ? 131.209 181.430 127.764 1.00 141.02 ? 515 THR C C   1 
ATOM   8552  O  O   . THR C 1 499 ? 131.861 182.477 127.843 1.00 141.02 ? 515 THR C O   1 
ATOM   8553  C  CB  . THR C 1 499 ? 129.258 182.214 126.433 1.00 141.02 ? 515 THR C CB  1 
ATOM   8554  N  N   . SER C 1 500 ? 131.197 180.518 128.738 1.00 130.60 ? 516 SER C N   1 
ATOM   8555  C  CA  . SER C 1 500 ? 131.906 180.686 130.008 1.00 130.60 ? 516 SER C CA  1 
ATOM   8556  C  C   . SER C 1 500 ? 131.472 181.945 130.753 1.00 130.60 ? 516 SER C C   1 
ATOM   8557  O  O   . SER C 1 500 ? 132.218 182.464 131.589 1.00 130.60 ? 516 SER C O   1 
ATOM   8558  C  CB  . SER C 1 500 ? 133.426 180.689 129.804 1.00 130.60 ? 516 SER C CB  1 
ATOM   8559  O  OG  . SER C 1 500 ? 134.105 180.632 131.047 1.00 130.60 ? 516 SER C OG  1 
ATOM   8560  N  N   . ALA C 1 501 ? 130.274 182.445 130.463 1.00 127.93 ? 517 ALA C N   1 
ATOM   8561  C  CA  . ALA C 1 501 ? 129.777 183.682 131.052 1.00 127.93 ? 517 ALA C CA  1 
ATOM   8562  C  C   . ALA C 1 501 ? 129.018 183.367 132.336 1.00 127.93 ? 517 ALA C C   1 
ATOM   8563  O  O   . ALA C 1 501 ? 128.019 182.639 132.313 1.00 127.93 ? 517 ALA C O   1 
ATOM   8564  C  CB  . ALA C 1 501 ? 128.880 184.428 130.066 1.00 127.93 ? 517 ALA C CB  1 
ATOM   8565  N  N   . VAL C 1 502 ? 129.492 183.918 133.450 1.00 129.46 ? 518 VAL C N   1 
ATOM   8566  C  CA  . VAL C 1 502 ? 128.851 183.745 134.750 1.00 129.46 ? 518 VAL C CA  1 
ATOM   8567  C  C   . VAL C 1 502 ? 127.727 184.772 134.858 1.00 129.46 ? 518 VAL C C   1 
ATOM   8568  O  O   . VAL C 1 502 ? 127.977 185.980 134.885 1.00 129.46 ? 518 VAL C O   1 
ATOM   8569  C  CB  . VAL C 1 502 ? 129.861 183.893 135.893 1.00 129.46 ? 518 VAL C CB  1 
ATOM   8570  C  CG1 . VAL C 1 502 ? 129.164 184.266 137.186 1.00 129.46 ? 518 VAL C CG1 1 
ATOM   8571  C  CG2 . VAL C 1 502 ? 130.655 182.607 136.066 1.00 129.46 ? 518 VAL C CG2 1 
ATOM   8572  N  N   . THR C 1 503 ? 126.483 184.297 134.890 1.00 132.64 ? 519 THR C N   1 
ATOM   8573  C  CA  . THR C 1 503 ? 125.312 185.163 134.983 1.00 132.64 ? 519 THR C CA  1 
ATOM   8574  C  C   . THR C 1 503 ? 124.616 184.966 136.324 1.00 132.64 ? 519 THR C C   1 
ATOM   8575  O  O   . THR C 1 503 ? 124.275 183.837 136.691 1.00 132.64 ? 519 THR C O   1 
ATOM   8576  C  CB  . THR C 1 503 ? 124.338 184.887 133.838 1.00 132.64 ? 519 THR C CB  1 
ATOM   8577  O  OG1 . THR C 1 503 ? 123.506 183.770 134.175 1.00 132.64 ? 519 THR C OG1 1 
ATOM   8578  C  CG2 . THR C 1 503 ? 125.095 184.578 132.555 1.00 132.64 ? 519 THR C CG2 1 
ATOM   8579  N  N   . VAL C 1 504 ? 124.435 186.058 137.066 1.00 141.46 ? 520 VAL C N   1 
ATOM   8580  C  CA  . VAL C 1 504 ? 123.780 185.983 138.366 1.00 141.46 ? 520 VAL C CA  1 
ATOM   8581  C  C   . VAL C 1 504 ? 122.306 185.657 138.168 1.00 141.46 ? 520 VAL C C   1 
ATOM   8582  O  O   . VAL C 1 504 ? 121.611 186.304 137.374 1.00 141.46 ? 520 VAL C O   1 
ATOM   8583  C  CB  . VAL C 1 504 ? 123.960 187.297 139.139 1.00 141.46 ? 520 VAL C CB  1 
ATOM   8584  C  CG1 . VAL C 1 504 ? 123.210 187.242 140.459 1.00 141.46 ? 520 VAL C CG1 1 
ATOM   8585  C  CG2 . VAL C 1 504 ? 125.436 187.574 139.373 1.00 141.46 ? 520 VAL C CG2 1 
ATOM   8586  N  N   . THR C 1 505 ? 121.819 184.651 138.889 1.00 134.79 ? 521 THR C N   1 
ATOM   8587  C  CA  . THR C 1 505 ? 120.422 184.246 138.778 1.00 134.79 ? 521 THR C CA  1 
ATOM   8588  C  C   . THR C 1 505 ? 119.548 184.993 139.780 1.00 134.79 ? 521 THR C C   1 
ATOM   8589  O  O   . THR C 1 505 ? 118.463 184.534 140.136 1.00 134.79 ? 521 THR C O   1 
ATOM   8590  C  CB  . THR C 1 505 ? 120.249 182.732 138.995 1.00 134.79 ? 521 THR C CB  1 
ATOM   8591  O  OG1 . THR C 1 505 ? 120.745 182.371 140.290 1.00 134.79 ? 521 THR C OG1 1 
ATOM   8592  C  CG2 . THR C 1 505 ? 121.003 181.952 137.931 1.00 134.79 ? 521 THR C CG2 1 
ATOM   8593  N  N   . LYS C 1 509 ? 117.210 183.059 145.629 1.00 142.04 ? 525 LYS C N   1 
ATOM   8594  C  CA  . LYS C 1 509 ? 116.810 183.111 147.029 1.00 142.04 ? 525 LYS C CA  1 
ATOM   8595  C  C   . LYS C 1 509 ? 117.713 182.237 147.893 1.00 142.04 ? 525 LYS C C   1 
ATOM   8596  O  O   . LYS C 1 509 ? 117.744 181.017 147.738 1.00 142.04 ? 525 LYS C O   1 
ATOM   8597  C  CB  . LYS C 1 509 ? 115.353 182.672 147.185 1.00 142.04 ? 525 LYS C CB  1 
ATOM   8598  N  N   . VAL C 1 510 ? 118.455 182.871 148.798 1.00 162.62 ? 526 VAL C N   1 
ATOM   8599  C  CA  . VAL C 1 510 ? 119.361 182.180 149.707 1.00 162.62 ? 526 VAL C CA  1 
ATOM   8600  C  C   . VAL C 1 510 ? 119.086 182.672 151.120 1.00 162.62 ? 526 VAL C C   1 
ATOM   8601  O  O   . VAL C 1 510 ? 119.059 183.884 151.364 1.00 162.62 ? 526 VAL C O   1 
ATOM   8602  C  CB  . VAL C 1 510 ? 120.838 182.411 149.332 1.00 162.62 ? 526 VAL C CB  1 
ATOM   8603  N  N   . LEU C 1 511 ? 118.892 181.736 152.050 1.00 151.72 ? 527 LEU C N   1 
ATOM   8604  C  CA  . LEU C 1 511 ? 118.626 182.065 153.446 1.00 151.72 ? 527 LEU C CA  1 
ATOM   8605  C  C   . LEU C 1 511 ? 119.620 181.417 154.400 1.00 151.72 ? 527 LEU C C   1 
ATOM   8606  O  O   . LEU C 1 511 ? 119.370 181.389 155.611 1.00 151.72 ? 527 LEU C O   1 
ATOM   8607  C  CB  . LEU C 1 511 ? 117.203 181.651 153.834 1.00 151.72 ? 527 LEU C CB  1 
ATOM   8608  C  CG  . LEU C 1 511 ? 116.104 181.835 152.788 1.00 151.72 ? 527 LEU C CG  1 
ATOM   8609  C  CD1 . LEU C 1 511 ? 114.798 181.244 153.290 1.00 151.72 ? 527 LEU C CD1 1 
ATOM   8610  C  CD2 . LEU C 1 511 ? 115.933 183.307 152.447 1.00 151.72 ? 527 LEU C CD2 1 
ATOM   8611  N  N   . LEU C 1 512 ? 120.730 180.891 153.894 1.00 146.87 ? 528 LEU C N   1 
ATOM   8612  C  CA  . LEU C 1 512 ? 121.712 180.193 154.712 1.00 146.87 ? 528 LEU C CA  1 
ATOM   8613  C  C   . LEU C 1 512 ? 123.032 180.955 154.734 1.00 146.87 ? 528 LEU C C   1 
ATOM   8614  O  O   . LEU C 1 512 ? 123.548 181.356 153.685 1.00 146.87 ? 528 LEU C O   1 
ATOM   8615  C  CB  . LEU C 1 512 ? 121.877 178.746 154.224 1.00 146.87 ? 528 LEU C CB  1 
ATOM   8616  C  CG  . LEU C 1 512 ? 122.098 178.292 152.766 1.00 146.87 ? 528 LEU C CG  1 
ATOM   8617  C  CD1 . LEU C 1 512 ? 123.296 178.895 152.052 1.00 146.87 ? 528 LEU C CD1 1 
ATOM   8618  C  CD2 . LEU C 1 512 ? 122.151 176.773 152.689 1.00 146.87 ? 528 LEU C CD2 1 
ATOM   8619  N  N   . THR C 1 513 ? 123.538 181.212 155.942 1.00 149.56 ? 529 THR C N   1 
ATOM   8620  C  CA  . THR C 1 513 ? 124.806 181.922 156.078 1.00 149.56 ? 529 THR C CA  1 
ATOM   8621  C  C   . THR C 1 513 ? 125.966 181.095 155.535 1.00 149.56 ? 529 THR C C   1 
ATOM   8622  O  O   . THR C 1 513 ? 126.873 181.636 154.892 1.00 149.56 ? 529 THR C O   1 
ATOM   8623  C  CB  . THR C 1 513 ? 125.045 182.311 157.539 1.00 149.56 ? 529 THR C CB  1 
ATOM   8624  O  OG1 . THR C 1 513 ? 126.373 182.825 157.688 1.00 149.56 ? 529 THR C OG1 1 
ATOM   8625  C  CG2 . THR C 1 513 ? 124.852 181.120 158.467 1.00 149.56 ? 529 THR C CG2 1 
ATOM   8626  N  N   . ASN C 1 514 ? 125.952 179.787 155.774 1.00 144.80 ? 530 ASN C N   1 
ATOM   8627  C  CA  . ASN C 1 514 ? 127.042 178.903 155.396 1.00 144.80 ? 530 ASN C CA  1 
ATOM   8628  C  C   . ASN C 1 514 ? 126.542 177.883 154.382 1.00 144.80 ? 530 ASN C C   1 
ATOM   8629  O  O   . ASN C 1 514 ? 125.337 177.676 154.219 1.00 144.80 ? 530 ASN C O   1 
ATOM   8630  C  CB  . ASN C 1 514 ? 127.631 178.191 156.622 1.00 144.80 ? 530 ASN C CB  1 
ATOM   8631  C  CG  . ASN C 1 514 ? 129.038 177.676 156.380 1.00 144.80 ? 530 ASN C CG  1 
ATOM   8632  O  OD1 . ASN C 1 514 ? 129.369 177.225 155.282 1.00 144.80 ? 530 ASN C OD1 1 
ATOM   8633  N  ND2 . ASN C 1 514 ? 129.874 177.739 157.409 1.00 144.80 ? 530 ASN C ND2 1 
ATOM   8634  N  N   . LEU C 1 515 ? 127.489 177.253 153.687 1.00 122.70 ? 531 LEU C N   1 
ATOM   8635  C  CA  . LEU C 1 515 ? 127.184 176.281 152.633 1.00 122.70 ? 531 LEU C CA  1 
ATOM   8636  C  C   . LEU C 1 515 ? 128.134 175.094 152.780 1.00 122.70 ? 531 LEU C C   1 
ATOM   8637  O  O   . LEU C 1 515 ? 129.243 175.105 152.241 1.00 122.70 ? 531 LEU C O   1 
ATOM   8638  C  CB  . LEU C 1 515 ? 127.306 176.932 151.265 1.00 122.70 ? 531 LEU C CB  1 
ATOM   8639  C  CG  . LEU C 1 515 ? 126.661 176.240 150.071 1.00 122.70 ? 531 LEU C CG  1 
ATOM   8640  C  CD1 . LEU C 1 515 ? 125.170 176.516 150.011 1.00 122.70 ? 531 LEU C CD1 1 
ATOM   8641  C  CD2 . LEU C 1 515 ? 127.348 176.726 148.821 1.00 122.70 ? 531 LEU C CD2 1 
ATOM   8642  N  N   . GLN C 1 516 ? 127.693 174.071 153.512 1.00 106.77 ? 532 GLN C N   1 
ATOM   8643  C  CA  . GLN C 1 516 ? 128.560 172.923 153.750 1.00 106.77 ? 532 GLN C CA  1 
ATOM   8644  C  C   . GLN C 1 516 ? 128.563 171.962 152.566 1.00 106.77 ? 532 GLN C C   1 
ATOM   8645  O  O   . GLN C 1 516 ? 129.630 171.570 152.082 1.00 106.77 ? 532 GLN C O   1 
ATOM   8646  C  CB  . GLN C 1 516 ? 128.141 172.199 155.031 1.00 106.77 ? 532 GLN C CB  1 
ATOM   8647  C  CG  . GLN C 1 516 ? 129.091 171.082 155.439 1.00 106.77 ? 532 GLN C CG  1 
ATOM   8648  C  CD  . GLN C 1 516 ? 128.626 170.339 156.677 1.00 106.77 ? 532 GLN C CD  1 
ATOM   8649  O  OE1 . GLN C 1 516 ? 127.457 169.975 156.794 1.00 106.77 ? 532 GLN C OE1 1 
ATOM   8650  N  NE2 . GLN C 1 516 ? 129.544 170.113 157.610 1.00 106.77 ? 532 GLN C NE2 1 
ATOM   8651  N  N   . PHE C 1 517 ? 127.384 171.572 152.083 1.00 93.42  ? 533 PHE C N   1 
ATOM   8652  C  CA  . PHE C 1 517 ? 127.288 170.618 150.983 1.00 93.42  ? 533 PHE C CA  1 
ATOM   8653  C  C   . PHE C 1 517 ? 126.378 171.144 149.885 1.00 93.42  ? 533 PHE C C   1 
ATOM   8654  O  O   . PHE C 1 517 ? 125.369 171.790 150.167 1.00 93.42  ? 533 PHE C O   1 
ATOM   8655  C  CB  . PHE C 1 517 ? 126.757 169.264 151.473 1.00 93.42  ? 533 PHE C CB  1 
ATOM   8656  C  CG  . PHE C 1 517 ? 127.774 168.444 152.213 1.00 93.42  ? 533 PHE C CG  1 
ATOM   8657  C  CD1 . PHE C 1 517 ? 128.726 167.714 151.525 1.00 93.42  ? 533 PHE C CD1 1 
ATOM   8658  C  CD2 . PHE C 1 517 ? 127.770 168.395 153.596 1.00 93.42  ? 533 PHE C CD2 1 
ATOM   8659  C  CE1 . PHE C 1 517 ? 129.661 166.956 152.202 1.00 93.42  ? 533 PHE C CE1 1 
ATOM   8660  C  CE2 . PHE C 1 517 ? 128.703 167.638 154.279 1.00 93.42  ? 533 PHE C CE2 1 
ATOM   8661  C  CZ  . PHE C 1 517 ? 129.649 166.918 153.581 1.00 93.42  ? 533 PHE C CZ  1 
ATOM   8662  N  N   . VAL C 1 518 ? 126.739 170.867 148.631 1.00 103.07 ? 534 VAL C N   1 
ATOM   8663  C  CA  . VAL C 1 518 ? 125.902 171.196 147.475 1.00 103.07 ? 534 VAL C CA  1 
ATOM   8664  C  C   . VAL C 1 518 ? 125.786 169.926 146.635 1.00 103.07 ? 534 VAL C C   1 
ATOM   8665  O  O   . VAL C 1 518 ? 126.627 169.655 145.773 1.00 103.07 ? 534 VAL C O   1 
ATOM   8666  C  CB  . VAL C 1 518 ? 126.462 172.355 146.646 1.00 103.07 ? 534 VAL C CB  1 
ATOM   8667  C  CG1 . VAL C 1 518 ? 125.417 172.843 145.655 1.00 103.07 ? 534 VAL C CG1 1 
ATOM   8668  C  CG2 . VAL C 1 518 ? 126.915 173.480 147.545 1.00 103.07 ? 534 VAL C CG2 1 
ATOM   8669  N  N   . LEU C 1 519 ? 124.740 169.142 146.878 1.00 104.89 ? 535 LEU C N   1 
ATOM   8670  C  CA  . LEU C 1 519 ? 124.585 167.878 146.176 1.00 104.89 ? 535 LEU C CA  1 
ATOM   8671  C  C   . LEU C 1 519 ? 124.022 168.107 144.777 1.00 104.89 ? 535 LEU C C   1 
ATOM   8672  O  O   . LEU C 1 519 ? 123.504 169.178 144.452 1.00 104.89 ? 535 LEU C O   1 
ATOM   8673  C  CB  . LEU C 1 519 ? 123.682 166.921 146.954 1.00 104.89 ? 535 LEU C CB  1 
ATOM   8674  C  CG  . LEU C 1 519 ? 124.133 166.482 148.351 1.00 104.89 ? 535 LEU C CG  1 
ATOM   8675  C  CD1 . LEU C 1 519 ? 125.622 166.165 148.361 1.00 104.89 ? 535 LEU C CD1 1 
ATOM   8676  C  CD2 . LEU C 1 519 ? 123.788 167.508 149.414 1.00 104.89 ? 535 LEU C CD2 1 
ATOM   8677  N  N   . ALA C 1 520 ? 124.146 167.078 143.942 1.00 126.89 ? 536 ALA C N   1 
ATOM   8678  C  CA  . ALA C 1 520 ? 123.710 167.129 142.548 1.00 126.89 ? 536 ALA C CA  1 
ATOM   8679  C  C   . ALA C 1 520 ? 122.250 167.553 142.403 1.00 126.89 ? 536 ALA C C   1 
ATOM   8680  O  O   . ALA C 1 520 ? 121.813 167.942 141.321 1.00 126.89 ? 536 ALA C O   1 
ATOM   8681  C  CB  . ALA C 1 520 ? 123.929 165.780 141.883 1.00 126.89 ? 536 ALA C CB  1 
ATOM   8682  O  OXT . ALA C 1 520 ? 121.473 167.516 143.356 1.00 126.89 ? 536 ALA C OXT 1 
ATOM   8683  N  N   . LYS D 2 9   ? 183.381 174.741 190.523 1.00 151.05 ? 9   LYS B N   1 
ATOM   8684  C  CA  . LYS D 2 9   ? 182.667 174.721 189.252 1.00 151.05 ? 9   LYS B CA  1 
ATOM   8685  C  C   . LYS D 2 9   ? 181.509 173.729 189.290 1.00 151.05 ? 9   LYS B C   1 
ATOM   8686  O  O   . LYS D 2 9   ? 180.724 173.708 190.238 1.00 151.05 ? 9   LYS B O   1 
ATOM   8687  C  CB  . LYS D 2 9   ? 183.622 174.377 188.107 1.00 151.05 ? 9   LYS B CB  1 
ATOM   8688  N  N   . LYS D 2 10  ? 181.411 172.906 188.249 1.00 149.35 ? 10  LYS B N   1 
ATOM   8689  C  CA  . LYS D 2 10  ? 180.354 171.905 188.116 1.00 149.35 ? 10  LYS B CA  1 
ATOM   8690  C  C   . LYS D 2 10  ? 180.887 170.571 188.626 1.00 149.35 ? 10  LYS B C   1 
ATOM   8691  O  O   . LYS D 2 10  ? 181.675 169.907 187.948 1.00 149.35 ? 10  LYS B O   1 
ATOM   8692  C  CB  . LYS D 2 10  ? 179.884 171.803 186.669 1.00 149.35 ? 10  LYS B CB  1 
ATOM   8693  N  N   . LYS D 2 11  ? 180.468 170.187 189.832 1.00 140.29 ? 11  LYS B N   1 
ATOM   8694  C  CA  . LYS D 2 11  ? 180.923 168.935 190.422 1.00 140.29 ? 11  LYS B CA  1 
ATOM   8695  C  C   . LYS D 2 11  ? 180.461 167.760 189.569 1.00 140.29 ? 11  LYS B C   1 
ATOM   8696  O  O   . LYS D 2 11  ? 179.286 167.672 189.201 1.00 140.29 ? 11  LYS B O   1 
ATOM   8697  C  CB  . LYS D 2 11  ? 180.350 168.817 191.835 1.00 140.29 ? 11  LYS B CB  1 
ATOM   8698  C  CG  . LYS D 2 11  ? 180.955 167.753 192.729 1.00 140.29 ? 11  LYS B CG  1 
ATOM   8699  C  CD  . LYS D 2 11  ? 182.399 168.055 193.067 1.00 140.29 ? 11  LYS B CD  1 
ATOM   8700  C  CE  . LYS D 2 11  ? 182.864 167.191 194.228 1.00 140.29 ? 11  LYS B CE  1 
ATOM   8701  N  NZ  . LYS D 2 11  ? 184.125 167.705 194.833 1.00 140.29 ? 11  LYS B NZ  1 
ATOM   8702  N  N   . VAL D 2 12  ? 181.381 166.847 189.257 1.00 131.67 ? 12  VAL B N   1 
ATOM   8703  C  CA  . VAL D 2 12  ? 181.073 165.692 188.421 1.00 131.67 ? 12  VAL B CA  1 
ATOM   8704  C  C   . VAL D 2 12  ? 181.460 164.410 189.147 1.00 131.67 ? 12  VAL B C   1 
ATOM   8705  O  O   . VAL D 2 12  ? 182.464 164.371 189.867 1.00 131.67 ? 12  VAL B O   1 
ATOM   8706  C  CB  . VAL D 2 12  ? 181.793 165.788 187.057 1.00 131.67 ? 12  VAL B CB  1 
ATOM   8707  C  CG1 . VAL D 2 12  ? 181.465 164.590 186.179 1.00 131.67 ? 12  VAL B CG1 1 
ATOM   8708  C  CG2 . VAL D 2 12  ? 181.419 167.077 186.349 1.00 131.67 ? 12  VAL B CG2 1 
ATOM   8709  N  N   . CYS D 2 13  ? 180.660 163.362 188.951 1.00 123.10 ? 13  CYS B N   1 
ATOM   8710  C  CA  . CYS D 2 13  ? 180.858 162.068 189.590 1.00 123.10 ? 13  CYS B CA  1 
ATOM   8711  C  C   . CYS D 2 13  ? 181.050 160.995 188.527 1.00 123.10 ? 13  CYS B C   1 
ATOM   8712  O  O   . CYS D 2 13  ? 180.322 160.961 187.530 1.00 123.10 ? 13  CYS B O   1 
ATOM   8713  C  CB  . CYS D 2 13  ? 179.688 161.697 190.503 1.00 123.10 ? 13  CYS B CB  1 
ATOM   8714  S  SG  . CYS D 2 13  ? 179.426 162.844 191.866 1.00 123.10 ? 13  CYS B SG  1 
ATOM   8715  N  N   . TYR D 2 14  ? 182.031 160.123 188.738 1.00 116.74 ? 14  TYR B N   1 
ATOM   8716  C  CA  . TYR D 2 14  ? 182.367 159.068 187.791 1.00 116.74 ? 14  TYR B CA  1 
ATOM   8717  C  C   . TYR D 2 14  ? 182.161 157.719 188.459 1.00 116.74 ? 14  TYR B C   1 
ATOM   8718  O  O   . TYR D 2 14  ? 182.412 157.565 189.658 1.00 116.74 ? 14  TYR B O   1 
ATOM   8719  C  CB  . TYR D 2 14  ? 183.804 159.186 187.289 1.00 116.74 ? 14  TYR B CB  1 
ATOM   8720  C  CG  . TYR D 2 14  ? 184.054 158.470 185.976 1.00 116.74 ? 14  TYR B CG  1 
ATOM   8721  C  CD1 . TYR D 2 14  ? 183.454 158.901 184.800 1.00 116.74 ? 14  TYR B CD1 1 
ATOM   8722  C  CD2 . TYR D 2 14  ? 184.903 157.373 185.913 1.00 116.74 ? 14  TYR B CD2 1 
ATOM   8723  C  CE1 . TYR D 2 14  ? 183.685 158.253 183.600 1.00 116.74 ? 14  TYR B CE1 1 
ATOM   8724  C  CE2 . TYR D 2 14  ? 185.142 156.721 184.718 1.00 116.74 ? 14  TYR B CE2 1 
ATOM   8725  C  CZ  . TYR D 2 14  ? 184.531 157.164 183.564 1.00 116.74 ? 14  TYR B CZ  1 
ATOM   8726  O  OH  . TYR D 2 14  ? 184.766 156.516 182.374 1.00 116.74 ? 14  TYR B OH  1 
ATOM   8727  N  N   . TYR D 2 15  ? 181.701 156.744 187.681 1.00 117.33 ? 15  TYR B N   1 
ATOM   8728  C  CA  . TYR D 2 15  ? 181.406 155.414 188.198 1.00 117.33 ? 15  TYR B CA  1 
ATOM   8729  C  C   . TYR D 2 15  ? 182.026 154.386 187.267 1.00 117.33 ? 15  TYR B C   1 
ATOM   8730  O  O   . TYR D 2 15  ? 181.673 154.330 186.084 1.00 117.33 ? 15  TYR B O   1 
ATOM   8731  C  CB  . TYR D 2 15  ? 179.896 155.202 188.319 1.00 117.33 ? 15  TYR B CB  1 
ATOM   8732  C  CG  . TYR D 2 15  ? 179.294 155.884 189.523 1.00 117.33 ? 15  TYR B CG  1 
ATOM   8733  C  CD1 . TYR D 2 15  ? 179.317 155.282 190.772 1.00 117.33 ? 15  TYR B CD1 1 
ATOM   8734  C  CD2 . TYR D 2 15  ? 178.724 157.145 189.414 1.00 117.33 ? 15  TYR B CD2 1 
ATOM   8735  C  CE1 . TYR D 2 15  ? 178.772 155.908 191.877 1.00 117.33 ? 15  TYR B CE1 1 
ATOM   8736  C  CE2 . TYR D 2 15  ? 178.181 157.779 190.511 1.00 117.33 ? 15  TYR B CE2 1 
ATOM   8737  C  CZ  . TYR D 2 15  ? 178.206 157.158 191.740 1.00 117.33 ? 15  TYR B CZ  1 
ATOM   8738  O  OH  . TYR D 2 15  ? 177.661 157.789 192.834 1.00 117.33 ? 15  TYR B OH  1 
ATOM   8739  N  N   . TYR D 2 16  ? 182.938 153.573 187.799 1.00 129.83 ? 16  TYR B N   1 
ATOM   8740  C  CA  . TYR D 2 16  ? 183.600 152.573 186.978 1.00 129.83 ? 16  TYR B CA  1 
ATOM   8741  C  C   . TYR D 2 16  ? 184.309 151.532 187.832 1.00 129.83 ? 16  TYR B C   1 
ATOM   8742  O  O   . TYR D 2 16  ? 185.011 151.873 188.786 1.00 129.83 ? 16  TYR B O   1 
ATOM   8743  C  CB  . TYR D 2 16  ? 184.610 153.221 186.024 1.00 129.83 ? 16  TYR B CB  1 
ATOM   8744  C  CG  . TYR D 2 16  ? 185.072 152.244 184.991 1.00 129.83 ? 16  TYR B CG  1 
ATOM   8745  C  CD1 . TYR D 2 16  ? 186.096 151.348 185.269 1.00 129.83 ? 16  TYR B CD1 1 
ATOM   8746  C  CD2 . TYR D 2 16  ? 184.434 152.155 183.771 1.00 129.83 ? 16  TYR B CD2 1 
ATOM   8747  C  CE1 . TYR D 2 16  ? 186.494 150.427 184.350 1.00 129.83 ? 16  TYR B CE1 1 
ATOM   8748  C  CE2 . TYR D 2 16  ? 184.832 151.243 182.846 1.00 129.83 ? 16  TYR B CE2 1 
ATOM   8749  C  CZ  . TYR D 2 16  ? 185.858 150.376 183.141 1.00 129.83 ? 16  TYR B CZ  1 
ATOM   8750  O  OH  . TYR D 2 16  ? 186.257 149.450 182.223 1.00 129.83 ? 16  TYR B OH  1 
ATOM   8751  N  N   . ASP D 2 17  ? 184.166 150.265 187.432 1.00 136.59 ? 17  ASP B N   1 
ATOM   8752  C  CA  . ASP D 2 17  ? 184.887 149.142 188.012 1.00 136.59 ? 17  ASP B CA  1 
ATOM   8753  C  C   . ASP D 2 17  ? 185.605 148.391 186.898 1.00 136.59 ? 17  ASP B C   1 
ATOM   8754  O  O   . ASP D 2 17  ? 185.051 148.198 185.812 1.00 136.59 ? 17  ASP B O   1 
ATOM   8755  C  CB  . ASP D 2 17  ? 183.944 148.192 188.763 1.00 136.59 ? 17  ASP B CB  1 
ATOM   8756  C  CG  . ASP D 2 17  ? 184.687 147.091 189.502 1.00 136.59 ? 17  ASP B CG  1 
ATOM   8757  O  OD1 . ASP D 2 17  ? 185.934 147.135 189.554 1.00 136.59 ? 17  ASP B OD1 1 
ATOM   8758  O  OD2 . ASP D 2 17  ? 184.019 146.175 190.025 1.00 136.59 ? 17  ASP B OD2 1 
ATOM   8759  N  N   . GLY D 2 18  ? 186.835 147.956 187.183 1.00 134.88 ? 18  GLY B N   1 
ATOM   8760  C  CA  . GLY D 2 18  ? 187.650 147.316 186.159 1.00 134.88 ? 18  GLY B CA  1 
ATOM   8761  C  C   . GLY D 2 18  ? 187.108 145.982 185.680 1.00 134.88 ? 18  GLY B C   1 
ATOM   8762  O  O   . GLY D 2 18  ? 187.080 145.708 184.474 1.00 134.88 ? 18  GLY B O   1 
ATOM   8763  N  N   . ASP D 2 19  ? 186.635 145.147 186.613 1.00 139.26 ? 19  ASP B N   1 
ATOM   8764  C  CA  . ASP D 2 19  ? 186.242 143.781 186.281 1.00 139.26 ? 19  ASP B CA  1 
ATOM   8765  C  C   . ASP D 2 19  ? 185.160 143.720 185.213 1.00 139.26 ? 19  ASP B C   1 
ATOM   8766  O  O   . ASP D 2 19  ? 185.018 142.679 184.556 1.00 139.26 ? 19  ASP B O   1 
ATOM   8767  C  CB  . ASP D 2 19  ? 185.769 143.054 187.540 1.00 139.26 ? 19  ASP B CB  1 
ATOM   8768  N  N   . ILE D 2 20  ? 184.411 144.807 185.011 1.00 132.61 ? 20  ILE B N   1 
ATOM   8769  C  CA  . ILE D 2 20  ? 183.357 144.816 184.005 1.00 132.61 ? 20  ILE B CA  1 
ATOM   8770  C  C   . ILE D 2 20  ? 183.919 144.446 182.638 1.00 132.61 ? 20  ILE B C   1 
ATOM   8771  O  O   . ILE D 2 20  ? 183.176 143.987 181.763 1.00 132.61 ? 20  ILE B O   1 
ATOM   8772  C  CB  . ILE D 2 20  ? 182.657 146.191 183.962 1.00 132.61 ? 20  ILE B CB  1 
ATOM   8773  C  CG1 . ILE D 2 20  ? 182.139 146.568 185.345 1.00 132.61 ? 20  ILE B CG1 1 
ATOM   8774  C  CG2 . ILE D 2 20  ? 181.459 146.148 183.031 1.00 132.61 ? 20  ILE B CG2 1 
ATOM   8775  C  CD1 . ILE D 2 20  ? 181.775 148.029 185.479 1.00 132.61 ? 20  ILE B CD1 1 
ATOM   8776  N  N   . GLY D 2 21  ? 185.229 144.603 182.442 1.00 124.90 ? 21  GLY B N   1 
ATOM   8777  C  CA  . GLY D 2 21  ? 185.816 144.305 181.152 1.00 124.90 ? 21  GLY B CA  1 
ATOM   8778  C  C   . GLY D 2 21  ? 185.983 142.832 180.841 1.00 124.90 ? 21  GLY B C   1 
ATOM   8779  O  O   . GLY D 2 21  ? 186.391 142.494 179.726 1.00 124.90 ? 21  GLY B O   1 
ATOM   8780  N  N   . ASN D 2 22  ? 185.686 141.947 181.790 1.00 131.60 ? 22  ASN B N   1 
ATOM   8781  C  CA  . ASN D 2 22  ? 185.898 140.518 181.603 1.00 131.60 ? 22  ASN B CA  1 
ATOM   8782  C  C   . ASN D 2 22  ? 184.608 139.763 181.301 1.00 131.60 ? 22  ASN B C   1 
ATOM   8783  O  O   . ASN D 2 22  ? 184.616 138.529 181.275 1.00 131.60 ? 22  ASN B O   1 
ATOM   8784  C  CB  . ASN D 2 22  ? 186.579 139.921 182.835 1.00 131.60 ? 22  ASN B CB  1 
ATOM   8785  C  CG  . ASN D 2 22  ? 187.775 140.734 183.288 1.00 131.60 ? 22  ASN B CG  1 
ATOM   8786  O  OD1 . ASN D 2 22  ? 188.619 141.122 182.481 1.00 131.60 ? 22  ASN B OD1 1 
ATOM   8787  N  ND2 . ASN D 2 22  ? 187.853 140.999 184.587 1.00 131.60 ? 22  ASN B ND2 1 
ATOM   8788  N  N   . TYR D 2 23  ? 183.502 140.474 181.071 1.00 116.93 ? 23  TYR B N   1 
ATOM   8789  C  CA  . TYR D 2 23  ? 182.207 139.850 180.794 1.00 116.93 ? 23  TYR B CA  1 
ATOM   8790  C  C   . TYR D 2 23  ? 182.064 139.629 179.290 1.00 116.93 ? 23  TYR B C   1 
ATOM   8791  O  O   . TYR D 2 23  ? 181.395 140.378 178.577 1.00 116.93 ? 23  TYR B O   1 
ATOM   8792  C  CB  . TYR D 2 23  ? 181.075 140.710 181.344 1.00 116.93 ? 23  TYR B CB  1 
ATOM   8793  C  CG  . TYR D 2 23  ? 181.051 140.795 182.852 1.00 116.93 ? 23  TYR B CG  1 
ATOM   8794  C  CD1 . TYR D 2 23  ? 180.775 139.680 183.629 1.00 116.93 ? 23  TYR B CD1 1 
ATOM   8795  C  CD2 . TYR D 2 23  ? 181.308 141.995 183.497 1.00 116.93 ? 23  TYR B CD2 1 
ATOM   8796  C  CE1 . TYR D 2 23  ? 180.754 139.760 185.011 1.00 116.93 ? 23  TYR B CE1 1 
ATOM   8797  C  CE2 . TYR D 2 23  ? 181.290 142.085 184.874 1.00 116.93 ? 23  TYR B CE2 1 
ATOM   8798  C  CZ  . TYR D 2 23  ? 181.013 140.966 185.626 1.00 116.93 ? 23  TYR B CZ  1 
ATOM   8799  O  OH  . TYR D 2 23  ? 180.996 141.059 186.998 1.00 116.93 ? 23  TYR B OH  1 
ATOM   8800  N  N   . TYR D 2 24  ? 182.712 138.574 178.804 1.00 122.64 ? 24  TYR B N   1 
ATOM   8801  C  CA  . TYR D 2 24  ? 182.641 138.235 177.387 1.00 122.64 ? 24  TYR B CA  1 
ATOM   8802  C  C   . TYR D 2 24  ? 181.223 137.817 177.008 1.00 122.64 ? 24  TYR B C   1 
ATOM   8803  O  O   . TYR D 2 24  ? 180.711 136.808 177.503 1.00 122.64 ? 24  TYR B O   1 
ATOM   8804  C  CB  . TYR D 2 24  ? 183.633 137.126 177.052 1.00 122.64 ? 24  TYR B CB  1 
ATOM   8805  C  CG  . TYR D 2 24  ? 183.767 136.867 175.568 1.00 122.64 ? 24  TYR B CG  1 
ATOM   8806  C  CD1 . TYR D 2 24  ? 184.186 137.869 174.703 1.00 122.64 ? 24  TYR B CD1 1 
ATOM   8807  C  CD2 . TYR D 2 24  ? 183.472 135.621 175.032 1.00 122.64 ? 24  TYR B CD2 1 
ATOM   8808  C  CE1 . TYR D 2 24  ? 184.307 137.637 173.345 1.00 122.64 ? 24  TYR B CE1 1 
ATOM   8809  C  CE2 . TYR D 2 24  ? 183.592 135.378 173.677 1.00 122.64 ? 24  TYR B CE2 1 
ATOM   8810  C  CZ  . TYR D 2 24  ? 184.008 136.390 172.838 1.00 122.64 ? 24  TYR B CZ  1 
ATOM   8811  O  OH  . TYR D 2 24  ? 184.128 136.151 171.489 1.00 122.64 ? 24  TYR B OH  1 
ATOM   8812  N  N   . TYR D 2 25  ? 180.592 138.603 176.132 1.00 128.40 ? 25  TYR B N   1 
ATOM   8813  C  CA  . TYR D 2 25  ? 179.224 138.322 175.709 1.00 128.40 ? 25  TYR B CA  1 
ATOM   8814  C  C   . TYR D 2 25  ? 179.126 136.984 174.986 1.00 128.40 ? 25  TYR B C   1 
ATOM   8815  O  O   . TYR D 2 25  ? 178.190 136.209 175.220 1.00 128.40 ? 25  TYR B O   1 
ATOM   8816  C  CB  . TYR D 2 25  ? 178.726 139.451 174.809 1.00 128.40 ? 25  TYR B CB  1 
ATOM   8817  C  CG  . TYR D 2 25  ? 177.260 139.802 174.924 1.00 128.40 ? 25  TYR B CG  1 
ATOM   8818  C  CD1 . TYR D 2 25  ? 176.739 140.344 176.092 1.00 128.40 ? 25  TYR B CD1 1 
ATOM   8819  C  CD2 . TYR D 2 25  ? 176.400 139.615 173.848 1.00 128.40 ? 25  TYR B CD2 1 
ATOM   8820  C  CE1 . TYR D 2 25  ? 175.400 140.674 176.188 1.00 128.40 ? 25  TYR B CE1 1 
ATOM   8821  C  CE2 . TYR D 2 25  ? 175.062 139.941 173.936 1.00 128.40 ? 25  TYR B CE2 1 
ATOM   8822  C  CZ  . TYR D 2 25  ? 174.566 140.470 175.107 1.00 128.40 ? 25  TYR B CZ  1 
ATOM   8823  O  OH  . TYR D 2 25  ? 173.233 140.796 175.199 1.00 128.40 ? 25  TYR B OH  1 
ATOM   8824  N  N   . GLY D 2 26  ? 180.074 136.694 174.110 1.00 126.15 ? 26  GLY B N   1 
ATOM   8825  C  CA  . GLY D 2 26  ? 180.051 135.462 173.344 1.00 126.15 ? 26  GLY B CA  1 
ATOM   8826  C  C   . GLY D 2 26  ? 180.660 135.672 171.975 1.00 126.15 ? 26  GLY B C   1 
ATOM   8827  O  O   . GLY D 2 26  ? 180.907 136.792 171.540 1.00 126.15 ? 26  GLY B O   1 
ATOM   8828  N  N   . GLN D 2 27  ? 180.950 134.555 171.312 1.00 127.29 ? 27  GLN B N   1 
ATOM   8829  C  CA  . GLN D 2 27  ? 181.535 134.618 169.978 1.00 127.29 ? 27  GLN B CA  1 
ATOM   8830  C  C   . GLN D 2 27  ? 180.613 135.385 169.037 1.00 127.29 ? 27  GLN B C   1 
ATOM   8831  O  O   . GLN D 2 27  ? 179.399 135.160 169.020 1.00 127.29 ? 27  GLN B O   1 
ATOM   8832  C  CB  . GLN D 2 27  ? 181.787 133.208 169.444 1.00 127.29 ? 27  GLN B CB  1 
ATOM   8833  N  N   . GLY D 2 28  ? 181.191 136.285 168.248 1.00 129.51 ? 28  GLY B N   1 
ATOM   8834  C  CA  . GLY D 2 28  ? 180.386 137.073 167.324 1.00 129.51 ? 28  GLY B CA  1 
ATOM   8835  C  C   . GLY D 2 28  ? 179.401 137.990 168.015 1.00 129.51 ? 28  GLY B C   1 
ATOM   8836  O  O   . GLY D 2 28  ? 178.235 138.071 167.607 1.00 129.51 ? 28  GLY B O   1 
ATOM   8837  N  N   . HIS D 2 29  ? 179.848 138.693 169.056 1.00 127.43 ? 29  HIS B N   1 
ATOM   8838  C  CA  . HIS D 2 29  ? 178.968 139.517 169.873 1.00 127.43 ? 29  HIS B CA  1 
ATOM   8839  C  C   . HIS D 2 29  ? 179.064 140.981 169.476 1.00 127.43 ? 29  HIS B C   1 
ATOM   8840  O  O   . HIS D 2 29  ? 180.153 141.572 169.563 1.00 127.43 ? 29  HIS B O   1 
ATOM   8841  C  CB  . HIS D 2 29  ? 179.321 139.352 171.347 1.00 127.43 ? 29  HIS B CB  1 
ATOM   8842  C  CG  . HIS D 2 29  ? 180.712 139.797 171.698 1.00 127.43 ? 29  HIS B CG  1 
ATOM   8843  N  ND1 . HIS D 2 29  ? 181.751 139.778 170.791 1.00 127.43 ? 29  HIS B ND1 1 
ATOM   8844  C  CD2 . HIS D 2 29  ? 181.236 140.265 172.855 1.00 127.43 ? 29  HIS B CD2 1 
ATOM   8845  C  CE1 . HIS D 2 29  ? 182.851 140.218 171.374 1.00 127.43 ? 29  HIS B CE1 1 
ATOM   8846  N  NE2 . HIS D 2 29  ? 182.566 140.522 172.627 1.00 127.43 ? 29  HIS B NE2 1 
ATOM   8847  N  N   . PRO D 2 30  ? 177.974 141.591 169.004 1.00 113.92 ? 30  PRO B N   1 
ATOM   8848  C  CA  . PRO D 2 30  ? 178.001 143.042 168.757 1.00 113.92 ? 30  PRO B CA  1 
ATOM   8849  C  C   . PRO D 2 30  ? 178.295 143.849 170.011 1.00 113.92 ? 30  PRO B C   1 
ATOM   8850  O  O   . PRO D 2 30  ? 178.980 144.877 169.942 1.00 113.92 ? 30  PRO B O   1 
ATOM   8851  C  CB  . PRO D 2 30  ? 176.600 143.330 168.200 1.00 113.92 ? 30  PRO B CB  1 
ATOM   8852  C  CG  . PRO D 2 30  ? 176.085 142.005 167.726 1.00 113.92 ? 30  PRO B CG  1 
ATOM   8853  C  CD  . PRO D 2 30  ? 176.685 140.985 168.637 1.00 113.92 ? 30  PRO B CD  1 
ATOM   8854  N  N   . MET D 2 31  ? 177.788 143.405 171.159 1.00 114.06 ? 31  MET B N   1 
ATOM   8855  C  CA  . MET D 2 31  ? 177.935 144.124 172.419 1.00 114.06 ? 31  MET B CA  1 
ATOM   8856  C  C   . MET D 2 31  ? 179.200 143.658 173.130 1.00 114.06 ? 31  MET B C   1 
ATOM   8857  O  O   . MET D 2 31  ? 179.323 142.478 173.476 1.00 114.06 ? 31  MET B O   1 
ATOM   8858  C  CB  . MET D 2 31  ? 176.710 143.899 173.304 1.00 114.06 ? 31  MET B CB  1 
ATOM   8859  C  CG  . MET D 2 31  ? 176.181 145.149 173.983 1.00 114.06 ? 31  MET B CG  1 
ATOM   8860  S  SD  . MET D 2 31  ? 176.998 145.482 175.555 1.00 114.06 ? 31  MET B SD  1 
ATOM   8861  C  CE  . MET D 2 31  ? 176.164 144.307 176.620 1.00 114.06 ? 31  MET B CE  1 
ATOM   8862  N  N   . LYS D 2 32  ? 180.130 144.583 173.360 1.00 113.92 ? 32  LYS B N   1 
ATOM   8863  C  CA  . LYS D 2 32  ? 181.420 144.273 173.974 1.00 113.92 ? 32  LYS B CA  1 
ATOM   8864  C  C   . LYS D 2 32  ? 181.636 145.209 175.154 1.00 113.92 ? 32  LYS B C   1 
ATOM   8865  O  O   . LYS D 2 32  ? 182.172 146.315 174.995 1.00 113.92 ? 32  LYS B O   1 
ATOM   8866  C  CB  . LYS D 2 32  ? 182.559 144.389 172.963 1.00 101.97 ? 32  LYS B CB  1 
ATOM   8867  C  CG  . LYS D 2 32  ? 182.187 143.978 171.546 1.00 101.97 ? 32  LYS B CG  1 
ATOM   8868  C  CD  . LYS D 2 32  ? 183.426 143.696 170.710 1.00 101.97 ? 32  LYS B CD  1 
ATOM   8869  C  CE  . LYS D 2 32  ? 183.065 143.041 169.388 1.00 101.97 ? 32  LYS B CE  1 
ATOM   8870  N  NZ  . LYS D 2 32  ? 182.170 143.901 168.569 1.00 101.97 ? 32  LYS B NZ  1 
ATOM   8871  N  N   . PRO D 2 33  ? 181.217 144.804 176.355 1.00 110.73 ? 33  PRO B N   1 
ATOM   8872  C  CA  . PRO D 2 33  ? 181.319 145.704 177.519 1.00 110.73 ? 33  PRO B CA  1 
ATOM   8873  C  C   . PRO D 2 33  ? 182.735 146.163 177.820 1.00 110.73 ? 33  PRO B C   1 
ATOM   8874  O  O   . PRO D 2 33  ? 182.924 147.302 178.271 1.00 110.73 ? 33  PRO B O   1 
ATOM   8875  C  CB  . PRO D 2 33  ? 180.741 144.861 178.665 1.00 110.73 ? 33  PRO B CB  1 
ATOM   8876  C  CG  . PRO D 2 33  ? 180.813 143.451 178.189 1.00 110.73 ? 33  PRO B CG  1 
ATOM   8877  C  CD  . PRO D 2 33  ? 180.628 143.504 176.709 1.00 110.73 ? 33  PRO B CD  1 
ATOM   8878  N  N   . HIS D 2 34  ? 183.740 145.322 177.560 1.00 113.45 ? 34  HIS B N   1 
ATOM   8879  C  CA  . HIS D 2 34  ? 185.137 145.659 177.816 1.00 113.45 ? 34  HIS B CA  1 
ATOM   8880  C  C   . HIS D 2 34  ? 185.540 146.960 177.131 1.00 113.45 ? 34  HIS B C   1 
ATOM   8881  O  O   . HIS D 2 34  ? 186.565 147.559 177.476 1.00 113.45 ? 34  HIS B O   1 
ATOM   8882  C  CB  . HIS D 2 34  ? 186.039 144.506 177.356 1.00 113.45 ? 34  HIS B CB  1 
ATOM   8883  C  CG  . HIS D 2 34  ? 187.468 144.897 177.132 1.00 113.45 ? 34  HIS B CG  1 
ATOM   8884  N  ND1 . HIS D 2 34  ? 188.233 145.507 178.103 1.00 113.45 ? 34  HIS B ND1 1 
ATOM   8885  C  CD2 . HIS D 2 34  ? 188.270 144.768 176.048 1.00 113.45 ? 34  HIS B CD2 1 
ATOM   8886  C  CE1 . HIS D 2 34  ? 189.444 145.735 177.628 1.00 113.45 ? 34  HIS B CE1 1 
ATOM   8887  N  NE2 . HIS D 2 34  ? 189.493 145.296 176.383 1.00 113.45 ? 34  HIS B NE2 1 
ATOM   8888  N  N   . ARG D 2 35  ? 184.717 147.428 176.186 1.00 123.72 ? 35  ARG B N   1 
ATOM   8889  C  CA  . ARG D 2 35  ? 185.007 148.687 175.512 1.00 123.72 ? 35  ARG B CA  1 
ATOM   8890  C  C   . ARG D 2 35  ? 185.141 149.826 176.502 1.00 123.72 ? 35  ARG B C   1 
ATOM   8891  O  O   . ARG D 2 35  ? 185.992 150.707 176.326 1.00 123.72 ? 35  ARG B O   1 
ATOM   8892  C  CB  . ARG D 2 35  ? 183.895 149.017 174.521 1.00 123.72 ? 35  ARG B CB  1 
ATOM   8893  N  N   . ILE D 2 36  ? 184.357 149.786 177.581 1.00 115.40 ? 36  ILE B N   1 
ATOM   8894  C  CA  . ILE D 2 36  ? 184.425 150.848 178.577 1.00 115.40 ? 36  ILE B CA  1 
ATOM   8895  C  C   . ILE D 2 36  ? 185.821 150.962 179.177 1.00 115.40 ? 36  ILE B C   1 
ATOM   8896  O  O   . ILE D 2 36  ? 186.273 152.071 179.490 1.00 115.40 ? 36  ILE B O   1 
ATOM   8897  C  CB  . ILE D 2 36  ? 183.322 150.635 179.632 1.00 115.40 ? 36  ILE B CB  1 
ATOM   8898  C  CG1 . ILE D 2 36  ? 183.604 149.402 180.484 1.00 115.40 ? 36  ILE B CG1 1 
ATOM   8899  C  CG2 . ILE D 2 36  ? 181.963 150.519 178.957 1.00 115.40 ? 36  ILE B CG2 1 
ATOM   8900  C  CD1 . ILE D 2 36  ? 182.470 149.058 181.407 1.00 115.40 ? 36  ILE B CD1 1 
ATOM   8901  N  N   . ARG D 2 37  ? 186.566 149.852 179.272 1.00 129.28 ? 37  ARG B N   1 
ATOM   8902  C  CA  . ARG D 2 37  ? 187.891 149.998 179.862 1.00 129.28 ? 37  ARG B CA  1 
ATOM   8903  C  C   . ARG D 2 37  ? 188.819 150.665 178.872 1.00 129.28 ? 37  ARG B C   1 
ATOM   8904  O  O   . ARG D 2 37  ? 189.641 151.507 179.258 1.00 129.28 ? 37  ARG B O   1 
ATOM   8905  C  CB  . ARG D 2 37  ? 188.452 148.635 180.278 1.00 129.28 ? 37  ARG B CB  1 
ATOM   8906  C  CG  . ARG D 2 37  ? 189.974 148.556 180.252 1.00 129.28 ? 37  ARG B CG  1 
ATOM   8907  C  CD  . ARG D 2 37  ? 190.526 147.683 181.368 1.00 129.28 ? 37  ARG B CD  1 
ATOM   8908  N  NE  . ARG D 2 37  ? 190.458 146.262 181.046 1.00 129.28 ? 37  ARG B NE  1 
ATOM   8909  C  CZ  . ARG D 2 37  ? 189.543 145.429 181.522 1.00 129.28 ? 37  ARG B CZ  1 
ATOM   8910  N  NH1 . ARG D 2 37  ? 188.597 145.841 182.350 1.00 129.28 ? 37  ARG B NH1 1 
ATOM   8911  N  NH2 . ARG D 2 37  ? 189.582 144.150 181.163 1.00 129.28 ? 37  ARG B NH2 1 
ATOM   8912  N  N   . MET D 2 38  ? 188.638 150.362 177.589 1.00 128.99 ? 38  MET B N   1 
ATOM   8913  C  CA  . MET D 2 38  ? 189.415 151.024 176.557 1.00 128.99 ? 38  MET B CA  1 
ATOM   8914  C  C   . MET D 2 38  ? 189.083 152.510 176.552 1.00 128.99 ? 38  MET B C   1 
ATOM   8915  O  O   . MET D 2 38  ? 189.838 153.317 175.999 1.00 128.99 ? 38  MET B O   1 
ATOM   8916  C  CB  . MET D 2 38  ? 189.207 150.310 175.218 1.00 128.99 ? 38  MET B CB  1 
ATOM   8917  C  CG  . MET D 2 38  ? 189.246 151.139 173.968 1.00 128.99 ? 38  MET B CG  1 
ATOM   8918  S  SD  . MET D 2 38  ? 189.240 149.988 172.582 1.00 128.99 ? 38  MET B SD  1 
ATOM   8919  C  CE  . MET D 2 38  ? 188.821 151.072 171.238 1.00 128.99 ? 38  MET B CE  1 
ATOM   8920  N  N   . THR D 2 39  ? 187.972 152.879 177.201 1.00 113.92 ? 39  THR B N   1 
ATOM   8921  C  CA  . THR D 2 39  ? 187.574 154.259 177.430 1.00 113.92 ? 39  THR B CA  1 
ATOM   8922  C  C   . THR D 2 39  ? 188.221 154.801 178.697 1.00 113.92 ? 39  THR B C   1 
ATOM   8923  O  O   . THR D 2 39  ? 188.741 155.921 178.696 1.00 113.92 ? 39  THR B O   1 
ATOM   8924  C  CB  . THR D 2 39  ? 186.047 154.350 177.564 1.00 113.92 ? 39  THR B CB  1 
ATOM   8925  O  OG1 . THR D 2 39  ? 185.440 154.369 176.273 1.00 113.92 ? 39  THR B OG1 1 
ATOM   8926  C  CG2 . THR D 2 39  ? 185.639 155.605 178.318 1.00 113.92 ? 39  THR B CG2 1 
ATOM   8927  N  N   . HIS D 2 40  ? 188.192 154.016 179.781 1.00 118.62 ? 40  HIS B N   1 
ATOM   8928  C  CA  . HIS D 2 40  ? 188.719 154.494 181.057 1.00 118.62 ? 40  HIS B CA  1 
ATOM   8929  C  C   . HIS D 2 40  ? 190.151 154.991 180.917 1.00 118.62 ? 40  HIS B C   1 
ATOM   8930  O  O   . HIS D 2 40  ? 190.513 156.031 181.481 1.00 118.62 ? 40  HIS B O   1 
ATOM   8931  C  CB  . HIS D 2 40  ? 188.643 153.386 182.107 1.00 118.62 ? 40  HIS B CB  1 
ATOM   8932  C  CG  . HIS D 2 40  ? 188.932 153.857 183.498 1.00 118.62 ? 40  HIS B CG  1 
ATOM   8933  N  ND1 . HIS D 2 40  ? 188.006 154.527 184.267 1.00 118.62 ? 40  HIS B ND1 1 
ATOM   8934  C  CD2 . HIS D 2 40  ? 190.051 153.764 184.254 1.00 118.62 ? 40  HIS B CD2 1 
ATOM   8935  C  CE1 . HIS D 2 40  ? 188.541 154.823 185.438 1.00 118.62 ? 40  HIS B CE1 1 
ATOM   8936  N  NE2 . HIS D 2 40  ? 189.781 154.371 185.456 1.00 118.62 ? 40  HIS B NE2 1 
ATOM   8937  N  N   . ASN D 2 41  ? 190.973 154.279 180.141 1.00 128.16 ? 41  ASN B N   1 
ATOM   8938  C  CA  . ASN D 2 41  ? 192.372 154.670 180.006 1.00 128.16 ? 41  ASN B CA  1 
ATOM   8939  C  C   . ASN D 2 41  ? 192.495 156.033 179.344 1.00 128.16 ? 41  ASN B C   1 
ATOM   8940  O  O   . ASN D 2 41  ? 193.352 156.840 179.732 1.00 128.16 ? 41  ASN B O   1 
ATOM   8941  C  CB  . ASN D 2 41  ? 193.141 153.616 179.211 1.00 128.16 ? 41  ASN B CB  1 
ATOM   8942  C  CG  . ASN D 2 41  ? 194.461 153.246 179.860 1.00 128.16 ? 41  ASN B CG  1 
ATOM   8943  O  OD1 . ASN D 2 41  ? 195.434 153.995 179.786 1.00 128.16 ? 41  ASN B OD1 1 
ATOM   8944  N  ND2 . ASN D 2 41  ? 194.498 152.086 180.505 1.00 128.16 ? 41  ASN B ND2 1 
ATOM   8945  N  N   . LEU D 2 42  ? 191.598 156.340 178.403 1.00 115.35 ? 42  LEU B N   1 
ATOM   8946  C  CA  . LEU D 2 42  ? 191.627 157.639 177.746 1.00 115.35 ? 42  LEU B CA  1 
ATOM   8947  C  C   . LEU D 2 42  ? 191.298 158.751 178.726 1.00 115.35 ? 42  LEU B C   1 
ATOM   8948  O  O   . LEU D 2 42  ? 191.695 159.899 178.504 1.00 115.35 ? 42  LEU B O   1 
ATOM   8949  C  CB  . LEU D 2 42  ? 190.657 157.660 176.565 1.00 115.35 ? 42  LEU B CB  1 
ATOM   8950  C  CG  . LEU D 2 42  ? 191.210 157.133 175.239 1.00 115.35 ? 42  LEU B CG  1 
ATOM   8951  C  CD1 . LEU D 2 42  ? 190.143 156.374 174.468 1.00 115.35 ? 42  LEU B CD1 1 
ATOM   8952  C  CD2 . LEU D 2 42  ? 191.771 158.269 174.402 1.00 115.35 ? 42  LEU B CD2 1 
ATOM   8953  N  N   . LEU D 2 43  ? 190.581 158.431 179.804 1.00 118.21 ? 43  LEU B N   1 
ATOM   8954  C  CA  . LEU D 2 43  ? 190.396 159.398 180.877 1.00 118.21 ? 43  LEU B CA  1 
ATOM   8955  C  C   . LEU D 2 43  ? 191.684 159.576 181.669 1.00 118.21 ? 43  LEU B C   1 
ATOM   8956  O  O   . LEU D 2 43  ? 192.066 160.706 181.998 1.00 118.21 ? 43  LEU B O   1 
ATOM   8957  C  CB  . LEU D 2 43  ? 189.254 158.957 181.793 1.00 118.21 ? 43  LEU B CB  1 
ATOM   8958  N  N   . LEU D 2 44  ? 192.366 158.474 181.989 1.00 127.11 ? 44  LEU B N   1 
ATOM   8959  C  CA  . LEU D 2 44  ? 193.607 158.572 182.749 1.00 127.11 ? 44  LEU B CA  1 
ATOM   8960  C  C   . LEU D 2 44  ? 194.730 159.158 181.902 1.00 127.11 ? 44  LEU B C   1 
ATOM   8961  O  O   . LEU D 2 44  ? 195.471 160.037 182.358 1.00 127.11 ? 44  LEU B O   1 
ATOM   8962  C  CB  . LEU D 2 44  ? 194.000 157.197 183.290 1.00 127.11 ? 44  LEU B CB  1 
ATOM   8963  N  N   . ASN D 2 45  ? 194.879 158.674 180.665 1.00 130.08 ? 45  ASN B N   1 
ATOM   8964  C  CA  . ASN D 2 45  ? 195.986 159.117 179.825 1.00 130.08 ? 45  ASN B CA  1 
ATOM   8965  C  C   . ASN D 2 45  ? 195.884 160.604 179.507 1.00 130.08 ? 45  ASN B C   1 
ATOM   8966  O  O   . ASN D 2 45  ? 196.897 161.314 179.490 1.00 130.08 ? 45  ASN B O   1 
ATOM   8967  C  CB  . ASN D 2 45  ? 196.037 158.293 178.539 1.00 130.08 ? 45  ASN B CB  1 
ATOM   8968  C  CG  . ASN D 2 45  ? 196.718 156.951 178.733 1.00 130.08 ? 45  ASN B CG  1 
ATOM   8969  O  OD1 . ASN D 2 45  ? 197.174 156.329 177.774 1.00 130.08 ? 45  ASN B OD1 1 
ATOM   8970  N  ND2 . ASN D 2 45  ? 196.785 156.495 179.979 1.00 130.08 ? 45  ASN B ND2 1 
ATOM   8971  N  N   . TYR D 2 46  ? 194.668 161.094 179.260 1.00 125.50 ? 46  TYR B N   1 
ATOM   8972  C  CA  . TYR D 2 46  ? 194.465 162.522 179.041 1.00 125.50 ? 46  TYR B CA  1 
ATOM   8973  C  C   . TYR D 2 46  ? 194.586 163.323 180.328 1.00 125.50 ? 46  TYR B C   1 
ATOM   8974  O  O   . TYR D 2 46  ? 194.763 164.545 180.269 1.00 125.50 ? 46  TYR B O   1 
ATOM   8975  C  CB  . TYR D 2 46  ? 193.092 162.775 178.417 1.00 125.50 ? 46  TYR B CB  1 
ATOM   8976  C  CG  . TYR D 2 46  ? 193.084 162.851 176.908 1.00 125.50 ? 46  TYR B CG  1 
ATOM   8977  C  CD1 . TYR D 2 46  ? 193.532 163.986 176.249 1.00 125.50 ? 46  TYR B CD1 1 
ATOM   8978  C  CD2 . TYR D 2 46  ? 192.608 161.796 176.143 1.00 125.50 ? 46  TYR B CD2 1 
ATOM   8979  C  CE1 . TYR D 2 46  ? 193.525 164.060 174.870 1.00 125.50 ? 46  TYR B CE1 1 
ATOM   8980  C  CE2 . TYR D 2 46  ? 192.592 161.861 174.765 1.00 125.50 ? 46  TYR B CE2 1 
ATOM   8981  C  CZ  . TYR D 2 46  ? 193.052 162.996 174.132 1.00 125.50 ? 46  TYR B CZ  1 
ATOM   8982  O  OH  . TYR D 2 46  ? 193.034 163.070 172.760 1.00 125.50 ? 46  TYR B OH  1 
ATOM   8983  N  N   . GLY D 2 47  ? 194.492 162.670 181.482 1.00 134.35 ? 47  GLY B N   1 
ATOM   8984  C  CA  . GLY D 2 47  ? 194.613 163.340 182.757 1.00 134.35 ? 47  GLY B CA  1 
ATOM   8985  C  C   . GLY D 2 47  ? 193.308 163.825 183.342 1.00 134.35 ? 47  GLY B C   1 
ATOM   8986  O  O   . GLY D 2 47  ? 193.319 164.418 184.429 1.00 134.35 ? 47  GLY B O   1 
ATOM   8987  N  N   . LEU D 2 48  ? 192.185 163.606 182.652 1.00 126.51 ? 48  LEU B N   1 
ATOM   8988  C  CA  . LEU D 2 48  ? 190.882 163.985 183.186 1.00 126.51 ? 48  LEU B CA  1 
ATOM   8989  C  C   . LEU D 2 48  ? 190.592 163.324 184.527 1.00 126.51 ? 48  LEU B C   1 
ATOM   8990  O  O   . LEU D 2 48  ? 189.732 163.807 185.272 1.00 126.51 ? 48  LEU B O   1 
ATOM   8991  C  CB  . LEU D 2 48  ? 189.779 163.624 182.185 1.00 126.51 ? 48  LEU B CB  1 
ATOM   8992  C  CG  . LEU D 2 48  ? 189.473 164.518 180.975 1.00 126.51 ? 48  LEU B CG  1 
ATOM   8993  C  CD1 . LEU D 2 48  ? 190.719 165.124 180.342 1.00 126.51 ? 48  LEU B CD1 1 
ATOM   8994  C  CD2 . LEU D 2 48  ? 188.681 163.736 179.936 1.00 126.51 ? 48  LEU B CD2 1 
ATOM   8995  N  N   . TYR D 2 49  ? 191.287 162.226 184.845 1.00 142.42 ? 49  TYR B N   1 
ATOM   8996  C  CA  . TYR D 2 49  ? 191.016 161.492 186.077 1.00 142.42 ? 49  TYR B CA  1 
ATOM   8997  C  C   . TYR D 2 49  ? 191.273 162.349 187.311 1.00 142.42 ? 49  TYR B C   1 
ATOM   8998  O  O   . TYR D 2 49  ? 190.487 162.322 188.265 1.00 142.42 ? 49  TYR B O   1 
ATOM   8999  C  CB  . TYR D 2 49  ? 191.862 160.220 186.125 1.00 142.42 ? 49  TYR B CB  1 
ATOM   9000  N  N   . ARG D 2 50  ? 192.373 163.111 187.317 1.00 147.84 ? 50  ARG B N   1 
ATOM   9001  C  CA  . ARG D 2 50  ? 192.739 163.849 188.523 1.00 147.84 ? 50  ARG B CA  1 
ATOM   9002  C  C   . ARG D 2 50  ? 191.700 164.911 188.854 1.00 147.84 ? 50  ARG B C   1 
ATOM   9003  O  O   . ARG D 2 50  ? 191.301 165.056 190.015 1.00 147.84 ? 50  ARG B O   1 
ATOM   9004  C  CB  . ARG D 2 50  ? 194.119 164.483 188.352 1.00 147.84 ? 50  ARG B CB  1 
ATOM   9005  N  N   . LYS D 2 51  ? 191.253 165.667 187.849 1.00 145.12 ? 51  LYS B N   1 
ATOM   9006  C  CA  . LYS D 2 51  ? 190.325 166.760 188.103 1.00 145.12 ? 51  LYS B CA  1 
ATOM   9007  C  C   . LYS D 2 51  ? 188.961 166.254 188.544 1.00 145.12 ? 51  LYS B C   1 
ATOM   9008  O  O   . LYS D 2 51  ? 188.152 167.043 189.044 1.00 145.12 ? 51  LYS B O   1 
ATOM   9009  C  CB  . LYS D 2 51  ? 190.183 167.633 186.855 1.00 145.12 ? 51  LYS B CB  1 
ATOM   9010  N  N   . MET D 2 52  ? 188.694 164.967 188.350 1.00 137.12 ? 52  MET B N   1 
ATOM   9011  C  CA  . MET D 2 52  ? 187.393 164.348 188.550 1.00 137.12 ? 52  MET B CA  1 
ATOM   9012  C  C   . MET D 2 52  ? 187.370 163.538 189.844 1.00 137.12 ? 52  MET B C   1 
ATOM   9013  O  O   . MET D 2 52  ? 188.402 163.260 190.458 1.00 137.12 ? 52  MET B O   1 
ATOM   9014  C  CB  . MET D 2 52  ? 187.048 163.484 187.336 1.00 137.12 ? 52  MET B CB  1 
ATOM   9015  C  CG  . MET D 2 52  ? 185.891 164.019 186.526 1.00 137.12 ? 52  MET B CG  1 
ATOM   9016  S  SD  . MET D 2 52  ? 185.717 163.143 184.969 1.00 137.12 ? 52  MET B SD  1 
ATOM   9017  C  CE  . MET D 2 52  ? 185.755 161.449 185.520 1.00 137.12 ? 52  MET B CE  1 
ATOM   9018  N  N   . GLU D 2 53  ? 186.160 163.161 190.256 1.00 126.88 ? 53  GLU B N   1 
ATOM   9019  C  CA  . GLU D 2 53  ? 185.949 162.187 191.321 1.00 126.88 ? 53  GLU B CA  1 
ATOM   9020  C  C   . GLU D 2 53  ? 185.507 160.856 190.720 1.00 126.88 ? 53  GLU B C   1 
ATOM   9021  O  O   . GLU D 2 53  ? 184.511 160.798 189.992 1.00 126.88 ? 53  GLU B O   1 
ATOM   9022  C  CB  . GLU D 2 53  ? 184.929 162.681 192.355 1.00 126.88 ? 53  GLU B CB  1 
ATOM   9023  C  CG  . GLU D 2 53  ? 185.161 164.084 192.970 1.00 126.88 ? 53  GLU B CG  1 
ATOM   9024  C  CD  . GLU D 2 53  ? 185.197 165.252 191.988 1.00 126.88 ? 53  GLU B CD  1 
ATOM   9025  O  OE1 . GLU D 2 53  ? 185.233 166.403 192.461 1.00 126.88 ? 53  GLU B OE1 1 
ATOM   9026  O  OE2 . GLU D 2 53  ? 185.112 165.045 190.763 1.00 126.88 ? 53  GLU B OE2 1 
ATOM   9027  N  N   . ILE D 2 54  ? 186.254 159.798 191.025 1.00 124.64 ? 54  ILE B N   1 
ATOM   9028  C  CA  . ILE D 2 54  ? 186.098 158.490 190.400 1.00 124.64 ? 54  ILE B CA  1 
ATOM   9029  C  C   . ILE D 2 54  ? 185.667 157.479 191.457 1.00 124.64 ? 54  ILE B C   1 
ATOM   9030  O  O   . ILE D 2 54  ? 186.261 157.409 192.537 1.00 124.64 ? 54  ILE B O   1 
ATOM   9031  C  CB  . ILE D 2 54  ? 187.388 158.044 189.679 1.00 124.64 ? 54  ILE B CB  1 
ATOM   9032  C  CG1 . ILE D 2 54  ? 188.643 158.636 190.337 1.00 124.64 ? 54  ILE B CG1 1 
ATOM   9033  C  CG2 . ILE D 2 54  ? 187.335 158.416 188.207 1.00 124.64 ? 54  ILE B CG2 1 
ATOM   9034  C  CD1 . ILE D 2 54  ? 189.073 157.988 191.634 1.00 124.64 ? 54  ILE B CD1 1 
ATOM   9035  N  N   . TYR D 2 55  ? 184.613 156.721 191.153 1.00 125.17 ? 55  TYR B N   1 
ATOM   9036  C  CA  . TYR D 2 55  ? 184.116 155.669 192.029 1.00 125.17 ? 55  TYR B CA  1 
ATOM   9037  C  C   . TYR D 2 55  ? 183.817 154.432 191.195 1.00 125.17 ? 55  TYR B C   1 
ATOM   9038  O  O   . TYR D 2 55  ? 183.901 154.448 189.964 1.00 125.17 ? 55  TYR B O   1 
ATOM   9039  C  CB  . TYR D 2 55  ? 182.855 156.096 192.794 1.00 125.17 ? 55  TYR B CB  1 
ATOM   9040  C  CG  . TYR D 2 55  ? 182.862 157.523 193.284 1.00 125.17 ? 55  TYR B CG  1 
ATOM   9041  C  CD1 . TYR D 2 55  ? 183.777 157.945 194.238 1.00 125.17 ? 55  TYR B CD1 1 
ATOM   9042  C  CD2 . TYR D 2 55  ? 181.946 158.445 192.801 1.00 125.17 ? 55  TYR B CD2 1 
ATOM   9043  C  CE1 . TYR D 2 55  ? 183.786 159.249 194.692 1.00 125.17 ? 55  TYR B CE1 1 
ATOM   9044  C  CE2 . TYR D 2 55  ? 181.944 159.751 193.250 1.00 125.17 ? 55  TYR B CE2 1 
ATOM   9045  C  CZ  . TYR D 2 55  ? 182.867 160.147 194.195 1.00 125.17 ? 55  TYR B CZ  1 
ATOM   9046  O  OH  . TYR D 2 55  ? 182.872 161.447 194.648 1.00 125.17 ? 55  TYR B OH  1 
ATOM   9047  N  N   . ARG D 2 56  ? 183.470 153.343 191.884 1.00 122.26 ? 56  ARG B N   1 
ATOM   9048  C  CA  . ARG D 2 56  ? 183.060 152.125 191.214 1.00 122.26 ? 56  ARG B CA  1 
ATOM   9049  C  C   . ARG D 2 56  ? 181.641 151.740 191.609 1.00 122.26 ? 56  ARG B C   1 
ATOM   9050  O  O   . ARG D 2 56  ? 181.284 151.821 192.789 1.00 122.26 ? 56  ARG B O   1 
ATOM   9051  C  CB  . ARG D 2 56  ? 184.008 150.967 191.560 1.00 122.26 ? 56  ARG B CB  1 
ATOM   9052  N  N   . PRO D 2 57  ? 180.811 151.334 190.651 1.00 128.33 ? 57  PRO B N   1 
ATOM   9053  C  CA  . PRO D 2 57  ? 179.437 150.935 190.987 1.00 128.33 ? 57  PRO B CA  1 
ATOM   9054  C  C   . PRO D 2 57  ? 179.441 149.688 191.857 1.00 128.33 ? 57  PRO B C   1 
ATOM   9055  O  O   . PRO D 2 57  ? 179.989 148.650 191.481 1.00 128.33 ? 57  PRO B O   1 
ATOM   9056  C  CB  . PRO D 2 57  ? 178.800 150.676 189.617 1.00 128.33 ? 57  PRO B CB  1 
ATOM   9057  C  CG  . PRO D 2 57  ? 179.945 150.363 188.717 1.00 128.33 ? 57  PRO B CG  1 
ATOM   9058  C  CD  . PRO D 2 57  ? 181.098 151.184 189.214 1.00 128.33 ? 57  PRO B CD  1 
ATOM   9059  N  N   . HIS D 2 58  ? 178.825 149.795 193.029 1.00 134.36 ? 58  HIS B N   1 
ATOM   9060  C  CA  . HIS D 2 58  ? 178.787 148.658 193.931 1.00 134.36 ? 58  HIS B CA  1 
ATOM   9061  C  C   . HIS D 2 58  ? 177.672 147.698 193.523 1.00 134.36 ? 58  HIS B C   1 
ATOM   9062  O  O   . HIS D 2 58  ? 176.818 148.012 192.688 1.00 134.36 ? 58  HIS B O   1 
ATOM   9063  C  CB  . HIS D 2 58  ? 178.618 149.127 195.376 1.00 134.36 ? 58  HIS B CB  1 
ATOM   9064  C  CG  . HIS D 2 58  ? 177.245 149.629 195.696 1.00 134.36 ? 58  HIS B CG  1 
ATOM   9065  N  ND1 . HIS D 2 58  ? 176.885 150.951 195.554 1.00 134.36 ? 58  HIS B ND1 1 
ATOM   9066  C  CD2 . HIS D 2 58  ? 176.150 148.989 196.169 1.00 134.36 ? 58  HIS B CD2 1 
ATOM   9067  C  CE1 . HIS D 2 58  ? 175.623 151.103 195.913 1.00 134.36 ? 58  HIS B CE1 1 
ATOM   9068  N  NE2 . HIS D 2 58  ? 175.154 149.928 196.291 1.00 134.36 ? 58  HIS B NE2 1 
ATOM   9069  N  N   . LYS D 2 59  ? 177.698 146.505 194.113 1.00 134.50 ? 59  LYS B N   1 
ATOM   9070  C  CA  . LYS D 2 59  ? 176.765 145.455 193.727 1.00 134.50 ? 59  LYS B CA  1 
ATOM   9071  C  C   . LYS D 2 59  ? 175.325 145.899 193.957 1.00 134.50 ? 59  LYS B C   1 
ATOM   9072  O  O   . LYS D 2 59  ? 174.991 146.469 194.999 1.00 134.50 ? 59  LYS B O   1 
ATOM   9073  C  CB  . LYS D 2 59  ? 177.052 144.175 194.513 1.00 134.50 ? 59  LYS B CB  1 
ATOM   9074  N  N   . ALA D 2 60  ? 174.469 145.629 192.976 1.00 136.71 ? 60  ALA B N   1 
ATOM   9075  C  CA  . ALA D 2 60  ? 173.044 145.912 193.092 1.00 136.71 ? 60  ALA B CA  1 
ATOM   9076  C  C   . ALA D 2 60  ? 172.342 144.678 193.643 1.00 136.71 ? 60  ALA B C   1 
ATOM   9077  O  O   . ALA D 2 60  ? 172.383 143.608 193.026 1.00 136.71 ? 60  ALA B O   1 
ATOM   9078  C  CB  . ALA D 2 60  ? 172.460 146.316 191.739 1.00 136.71 ? 60  ALA B CB  1 
ATOM   9079  N  N   . THR D 2 61  ? 171.694 144.829 194.794 1.00 133.19 ? 61  THR B N   1 
ATOM   9080  C  CA  . THR D 2 61  ? 171.052 143.698 195.442 1.00 133.19 ? 61  THR B CA  1 
ATOM   9081  C  C   . THR D 2 61  ? 169.840 143.232 194.640 1.00 133.19 ? 61  THR B C   1 
ATOM   9082  O  O   . THR D 2 61  ? 169.234 143.988 193.876 1.00 133.19 ? 61  THR B O   1 
ATOM   9083  C  CB  . THR D 2 61  ? 170.628 144.060 196.865 1.00 133.19 ? 61  THR B CB  1 
ATOM   9084  O  OG1 . THR D 2 61  ? 169.457 144.885 196.821 1.00 133.19 ? 61  THR B OG1 1 
ATOM   9085  C  CG2 . THR D 2 61  ? 171.743 144.808 197.578 1.00 133.19 ? 61  THR B CG2 1 
ATOM   9086  N  N   . ALA D 2 62  ? 169.494 141.955 194.826 1.00 126.54 ? 62  ALA B N   1 
ATOM   9087  C  CA  . ALA D 2 62  ? 168.331 141.391 194.149 1.00 126.54 ? 62  ALA B CA  1 
ATOM   9088  C  C   . ALA D 2 62  ? 167.057 142.131 194.536 1.00 126.54 ? 62  ALA B C   1 
ATOM   9089  O  O   . ALA D 2 62  ? 166.179 142.355 193.694 1.00 126.54 ? 62  ALA B O   1 
ATOM   9090  C  CB  . ALA D 2 62  ? 168.208 139.902 194.467 1.00 126.54 ? 62  ALA B CB  1 
ATOM   9091  N  N   . GLU D 2 63  ? 166.935 142.509 195.809 1.00 129.75 ? 63  GLU B N   1 
ATOM   9092  C  CA  . GLU D 2 63  ? 165.776 143.280 196.245 1.00 129.75 ? 63  GLU B CA  1 
ATOM   9093  C  C   . GLU D 2 63  ? 165.718 144.630 195.541 1.00 129.75 ? 63  GLU B C   1 
ATOM   9094  O  O   . GLU D 2 63  ? 164.640 145.081 195.137 1.00 129.75 ? 63  GLU B O   1 
ATOM   9095  C  CB  . GLU D 2 63  ? 165.807 143.464 197.762 1.00 129.75 ? 63  GLU B CB  1 
ATOM   9096  N  N   . GLU D 2 64  ? 166.869 145.298 195.403 1.00 131.04 ? 64  GLU B N   1 
ATOM   9097  C  CA  . GLU D 2 64  ? 166.906 146.583 194.708 1.00 131.04 ? 64  GLU B CA  1 
ATOM   9098  C  C   . GLU D 2 64  ? 166.354 146.463 193.293 1.00 131.04 ? 64  GLU B C   1 
ATOM   9099  O  O   . GLU D 2 64  ? 165.580 147.318 192.847 1.00 131.04 ? 64  GLU B O   1 
ATOM   9100  C  CB  . GLU D 2 64  ? 168.335 147.125 194.683 1.00 131.04 ? 64  GLU B CB  1 
ATOM   9101  N  N   . MET D 2 65  ? 166.747 145.412 192.566 1.00 127.66 ? 65  MET B N   1 
ATOM   9102  C  CA  . MET D 2 65  ? 166.202 145.189 191.232 1.00 127.66 ? 65  MET B CA  1 
ATOM   9103  C  C   . MET D 2 65  ? 164.705 144.919 191.260 1.00 127.66 ? 65  MET B C   1 
ATOM   9104  O  O   . MET D 2 65  ? 164.032 145.115 190.241 1.00 127.66 ? 65  MET B O   1 
ATOM   9105  C  CB  . MET D 2 65  ? 166.919 144.030 190.536 1.00 127.66 ? 65  MET B CB  1 
ATOM   9106  C  CG  . MET D 2 65  ? 168.411 143.953 190.795 1.00 127.66 ? 65  MET B CG  1 
ATOM   9107  S  SD  . MET D 2 65  ? 169.263 143.147 189.426 1.00 127.66 ? 65  MET B SD  1 
ATOM   9108  C  CE  . MET D 2 65  ? 170.921 143.786 189.630 1.00 127.66 ? 65  MET B CE  1 
ATOM   9109  N  N   . THR D 2 66  ? 164.167 144.472 192.392 1.00 122.55 ? 66  THR B N   1 
ATOM   9110  C  CA  . THR D 2 66  ? 162.738 144.183 192.505 1.00 122.55 ? 66  THR B CA  1 
ATOM   9111  C  C   . THR D 2 66  ? 161.999 145.456 192.950 1.00 122.55 ? 66  THR B C   1 
ATOM   9112  O  O   . THR D 2 66  ? 161.293 145.542 193.955 1.00 122.55 ? 66  THR B O   1 
ATOM   9113  C  CB  . THR D 2 66  ? 162.536 142.985 193.440 1.00 122.55 ? 66  THR B CB  1 
ATOM   9114  O  OG1 . THR D 2 66  ? 162.798 141.790 192.697 1.00 122.55 ? 66  THR B OG1 1 
ATOM   9115  C  CG2 . THR D 2 66  ? 161.090 142.819 193.909 1.00 122.55 ? 66  THR B CG2 1 
ATOM   9116  N  N   . LYS D 2 67  ? 162.262 146.523 192.202 1.00 117.91 ? 67  LYS B N   1 
ATOM   9117  C  CA  . LYS D 2 67  ? 161.546 147.786 192.333 1.00 117.91 ? 67  LYS B CA  1 
ATOM   9118  C  C   . LYS D 2 67  ? 160.699 148.098 191.113 1.00 117.91 ? 67  LYS B C   1 
ATOM   9119  O  O   . LYS D 2 67  ? 159.584 148.608 191.251 1.00 117.91 ? 67  LYS B O   1 
ATOM   9120  C  CB  . LYS D 2 67  ? 162.533 148.934 192.573 1.00 117.91 ? 67  LYS B CB  1 
ATOM   9121  N  N   . TYR D 2 68  ? 161.210 147.800 189.921 1.00 113.92 ? 68  TYR B N   1 
ATOM   9122  C  CA  . TYR D 2 68  ? 160.447 147.856 188.683 1.00 113.92 ? 68  TYR B CA  1 
ATOM   9123  C  C   . TYR D 2 68  ? 160.265 146.493 188.037 1.00 113.92 ? 68  TYR B C   1 
ATOM   9124  O  O   . TYR D 2 68  ? 159.288 146.290 187.314 1.00 113.92 ? 68  TYR B O   1 
ATOM   9125  C  CB  . TYR D 2 68  ? 161.127 148.803 187.684 1.00 113.92 ? 68  TYR B CB  1 
ATOM   9126  C  CG  . TYR D 2 68  ? 160.726 148.595 186.240 1.00 113.92 ? 68  TYR B CG  1 
ATOM   9127  C  CD1 . TYR D 2 68  ? 159.490 149.021 185.774 1.00 113.92 ? 68  TYR B CD1 1 
ATOM   9128  C  CD2 . TYR D 2 68  ? 161.587 147.980 185.342 1.00 113.92 ? 68  TYR B CD2 1 
ATOM   9129  C  CE1 . TYR D 2 68  ? 159.121 148.834 184.455 1.00 113.92 ? 68  TYR B CE1 1 
ATOM   9130  C  CE2 . TYR D 2 68  ? 161.228 147.789 184.022 1.00 113.92 ? 68  TYR B CE2 1 
ATOM   9131  C  CZ  . TYR D 2 68  ? 159.994 148.218 183.585 1.00 113.92 ? 68  TYR B CZ  1 
ATOM   9132  O  OH  . TYR D 2 68  ? 159.633 148.031 182.270 1.00 113.92 ? 68  TYR B OH  1 
ATOM   9133  N  N   . HIS D 2 69  ? 161.165 145.554 188.303 1.00 113.92 ? 69  HIS B N   1 
ATOM   9134  C  CA  . HIS D 2 69  ? 161.085 144.216 187.744 1.00 113.92 ? 69  HIS B CA  1 
ATOM   9135  C  C   . HIS D 2 69  ? 160.251 143.305 188.641 1.00 113.92 ? 69  HIS B C   1 
ATOM   9136  O  O   . HIS D 2 69  ? 159.922 143.638 189.780 1.00 113.92 ? 69  HIS B O   1 
ATOM   9137  C  CB  . HIS D 2 69  ? 162.488 143.637 187.569 1.00 113.92 ? 69  HIS B CB  1 
ATOM   9138  C  CG  . HIS D 2 69  ? 163.273 144.273 186.465 1.00 113.92 ? 69  HIS B CG  1 
ATOM   9139  N  ND1 . HIS D 2 69  ? 162.999 144.057 185.132 1.00 113.92 ? 69  HIS B ND1 1 
ATOM   9140  C  CD2 . HIS D 2 69  ? 164.323 145.127 186.499 1.00 113.92 ? 69  HIS B CD2 1 
ATOM   9141  C  CE1 . HIS D 2 69  ? 163.848 144.747 184.393 1.00 113.92 ? 69  HIS B CE1 1 
ATOM   9142  N  NE2 . HIS D 2 69  ? 164.661 145.406 185.198 1.00 113.92 ? 69  HIS B NE2 1 
ATOM   9143  N  N   . SER D 2 70  ? 159.910 142.137 188.107 1.00 125.57 ? 70  SER B N   1 
ATOM   9144  C  CA  . SER D 2 70  ? 159.190 141.125 188.863 1.00 125.57 ? 70  SER B CA  1 
ATOM   9145  C  C   . SER D 2 70  ? 160.173 140.256 189.638 1.00 125.57 ? 70  SER B C   1 
ATOM   9146  O  O   . SER D 2 70  ? 161.336 140.108 189.253 1.00 125.57 ? 70  SER B O   1 
ATOM   9147  C  CB  . SER D 2 70  ? 158.331 140.258 187.939 1.00 125.57 ? 70  SER B CB  1 
ATOM   9148  O  OG  . SER D 2 70  ? 159.123 139.603 186.968 1.00 125.57 ? 70  SER B OG  1 
ATOM   9149  N  N   . ASP D 2 71  ? 159.693 139.685 190.744 1.00 125.18 ? 71  ASP B N   1 
ATOM   9150  C  CA  . ASP D 2 71  ? 160.541 138.808 191.546 1.00 125.18 ? 71  ASP B CA  1 
ATOM   9151  C  C   . ASP D 2 71  ? 160.927 137.552 190.773 1.00 125.18 ? 71  ASP B C   1 
ATOM   9152  O  O   . ASP D 2 71  ? 162.080 137.105 190.839 1.00 125.18 ? 71  ASP B O   1 
ATOM   9153  C  CB  . ASP D 2 71  ? 159.830 138.439 192.848 1.00 125.18 ? 71  ASP B CB  1 
ATOM   9154  N  N   . GLU D 2 72  ? 159.979 136.973 190.033 1.00 124.50 ? 72  GLU B N   1 
ATOM   9155  C  CA  . GLU D 2 72  ? 160.254 135.737 189.308 1.00 124.50 ? 72  GLU B CA  1 
ATOM   9156  C  C   . GLU D 2 72  ? 161.324 135.949 188.246 1.00 124.50 ? 72  GLU B C   1 
ATOM   9157  O  O   . GLU D 2 72  ? 162.211 135.106 188.071 1.00 124.50 ? 72  GLU B O   1 
ATOM   9158  C  CB  . GLU D 2 72  ? 158.969 135.201 188.676 1.00 124.50 ? 72  GLU B CB  1 
ATOM   9159  N  N   . TYR D 2 73  ? 161.254 137.069 187.524 1.00 115.12 ? 73  TYR B N   1 
ATOM   9160  C  CA  . TYR D 2 73  ? 162.206 137.329 186.449 1.00 115.12 ? 73  TYR B CA  1 
ATOM   9161  C  C   . TYR D 2 73  ? 163.622 137.490 186.990 1.00 115.12 ? 73  TYR B C   1 
ATOM   9162  O  O   . TYR D 2 73  ? 164.578 136.923 186.445 1.00 115.12 ? 73  TYR B O   1 
ATOM   9163  C  CB  . TYR D 2 73  ? 161.780 138.573 185.672 1.00 115.12 ? 73  TYR B CB  1 
ATOM   9164  C  CG  . TYR D 2 73  ? 162.750 138.996 184.600 1.00 115.12 ? 73  TYR B CG  1 
ATOM   9165  C  CD1 . TYR D 2 73  ? 163.076 138.145 183.553 1.00 115.12 ? 73  TYR B CD1 1 
ATOM   9166  C  CD2 . TYR D 2 73  ? 163.345 140.248 184.637 1.00 115.12 ? 73  TYR B CD2 1 
ATOM   9167  C  CE1 . TYR D 2 73  ? 163.963 138.533 182.571 1.00 115.12 ? 73  TYR B CE1 1 
ATOM   9168  C  CE2 . TYR D 2 73  ? 164.232 140.644 183.663 1.00 115.12 ? 73  TYR B CE2 1 
ATOM   9169  C  CZ  . TYR D 2 73  ? 164.537 139.784 182.632 1.00 115.12 ? 73  TYR B CZ  1 
ATOM   9170  O  OH  . TYR D 2 73  ? 165.424 140.182 181.664 1.00 115.12 ? 73  TYR B OH  1 
ATOM   9171  N  N   . ILE D 2 74  ? 163.777 138.269 188.063 1.00 116.55 ? 74  ILE B N   1 
ATOM   9172  C  CA  . ILE D 2 74  ? 165.100 138.470 188.640 1.00 116.55 ? 74  ILE B CA  1 
ATOM   9173  C  C   . ILE D 2 74  ? 165.619 137.173 189.249 1.00 116.55 ? 74  ILE B C   1 
ATOM   9174  O  O   . ILE D 2 74  ? 166.815 136.873 189.170 1.00 116.55 ? 74  ILE B O   1 
ATOM   9175  C  CB  . ILE D 2 74  ? 165.060 139.610 189.673 1.00 116.55 ? 74  ILE B CB  1 
ATOM   9176  C  CG1 . ILE D 2 74  ? 164.608 140.913 189.010 1.00 116.55 ? 74  ILE B CG1 1 
ATOM   9177  C  CG2 . ILE D 2 74  ? 166.422 139.800 190.321 1.00 116.55 ? 74  ILE B CG2 1 
ATOM   9178  C  CD1 . ILE D 2 74  ? 165.418 141.290 187.789 1.00 116.55 ? 74  ILE B CD1 1 
ATOM   9179  N  N   . LYS D 2 75  ? 164.732 136.379 189.856 1.00 119.59 ? 75  LYS B N   1 
ATOM   9180  C  CA  . LYS D 2 75  ? 165.147 135.077 190.372 1.00 119.59 ? 75  LYS B CA  1 
ATOM   9181  C  C   . LYS D 2 75  ? 165.640 134.174 189.247 1.00 119.59 ? 75  LYS B C   1 
ATOM   9182  O  O   . LYS D 2 75  ? 166.658 133.483 189.391 1.00 119.59 ? 75  LYS B O   1 
ATOM   9183  C  CB  . LYS D 2 75  ? 163.993 134.418 191.125 1.00 119.59 ? 75  LYS B CB  1 
ATOM   9184  N  N   . PHE D 2 76  ? 164.940 134.187 188.110 1.00 117.85 ? 76  PHE B N   1 
ATOM   9185  C  CA  . PHE D 2 76  ? 165.358 133.391 186.962 1.00 117.85 ? 76  PHE B CA  1 
ATOM   9186  C  C   . PHE D 2 76  ? 166.721 133.841 186.462 1.00 117.85 ? 76  PHE B C   1 
ATOM   9187  O  O   . PHE D 2 76  ? 167.596 133.013 186.185 1.00 117.85 ? 76  PHE B O   1 
ATOM   9188  C  CB  . PHE D 2 76  ? 164.311 133.489 185.851 1.00 117.85 ? 76  PHE B CB  1 
ATOM   9189  C  CG  . PHE D 2 76  ? 164.845 133.178 184.481 1.00 117.85 ? 76  PHE B CG  1 
ATOM   9190  C  CD1 . PHE D 2 76  ? 165.054 131.868 184.086 1.00 117.85 ? 76  PHE B CD1 1 
ATOM   9191  C  CD2 . PHE D 2 76  ? 165.128 134.194 183.585 1.00 117.85 ? 76  PHE B CD2 1 
ATOM   9192  C  CE1 . PHE D 2 76  ? 165.542 131.578 182.826 1.00 117.85 ? 76  PHE B CE1 1 
ATOM   9193  C  CE2 . PHE D 2 76  ? 165.616 133.910 182.324 1.00 117.85 ? 76  PHE B CE2 1 
ATOM   9194  C  CZ  . PHE D 2 76  ? 165.823 132.600 181.944 1.00 117.85 ? 76  PHE B CZ  1 
ATOM   9195  N  N   . LEU D 2 77  ? 166.921 135.156 186.342 1.00 123.31 ? 77  LEU B N   1 
ATOM   9196  C  CA  . LEU D 2 77  ? 168.200 135.659 185.847 1.00 123.31 ? 77  LEU B CA  1 
ATOM   9197  C  C   . LEU D 2 77  ? 169.329 135.317 186.812 1.00 123.31 ? 77  LEU B C   1 
ATOM   9198  O  O   . LEU D 2 77  ? 170.445 134.994 186.387 1.00 123.31 ? 77  LEU B O   1 
ATOM   9199  C  CB  . LEU D 2 77  ? 168.127 137.169 185.625 1.00 123.31 ? 77  LEU B CB  1 
ATOM   9200  C  CG  . LEU D 2 77  ? 167.498 137.655 184.319 1.00 123.31 ? 77  LEU B CG  1 
ATOM   9201  C  CD1 . LEU D 2 77  ? 167.455 139.173 184.295 1.00 123.31 ? 77  LEU B CD1 1 
ATOM   9202  C  CD2 . LEU D 2 77  ? 168.248 137.114 183.112 1.00 123.31 ? 77  LEU B CD2 1 
ATOM   9203  N  N   . ARG D 2 78  ? 169.060 135.399 188.116 1.00 124.44 ? 78  ARG B N   1 
ATOM   9204  C  CA  . ARG D 2 78  ? 170.082 135.113 189.115 1.00 124.44 ? 78  ARG B CA  1 
ATOM   9205  C  C   . ARG D 2 78  ? 170.434 133.631 189.158 1.00 124.44 ? 78  ARG B C   1 
ATOM   9206  O  O   . ARG D 2 78  ? 171.586 133.280 189.436 1.00 124.44 ? 78  ARG B O   1 
ATOM   9207  C  CB  . ARG D 2 78  ? 169.617 135.587 190.492 1.00 124.44 ? 78  ARG B CB  1 
ATOM   9208  N  N   . SER D 2 79  ? 169.467 132.755 188.894 1.00 132.15 ? 79  SER B N   1 
ATOM   9209  C  CA  . SER D 2 79  ? 169.654 131.321 189.078 1.00 132.15 ? 79  SER B CA  1 
ATOM   9210  C  C   . SER D 2 79  ? 170.110 130.586 187.821 1.00 132.15 ? 79  SER B C   1 
ATOM   9211  O  O   . SER D 2 79  ? 170.240 129.358 187.863 1.00 132.15 ? 79  SER B O   1 
ATOM   9212  C  CB  . SER D 2 79  ? 168.356 130.690 189.593 1.00 132.15 ? 79  SER B CB  1 
ATOM   9213  O  OG  . SER D 2 79  ? 167.893 131.355 190.755 1.00 132.15 ? 79  SER B OG  1 
ATOM   9214  N  N   . ILE D 2 80  ? 170.355 131.281 186.714 1.00 118.80 ? 80  ILE B N   1 
ATOM   9215  C  CA  . ILE D 2 80  ? 170.771 130.640 185.469 1.00 118.80 ? 80  ILE B CA  1 
ATOM   9216  C  C   . ILE D 2 80  ? 172.274 130.836 185.299 1.00 118.80 ? 80  ILE B C   1 
ATOM   9217  O  O   . ILE D 2 80  ? 172.754 131.960 185.113 1.00 118.80 ? 80  ILE B O   1 
ATOM   9218  C  CB  . ILE D 2 80  ? 169.992 131.172 184.257 1.00 118.80 ? 80  ILE B CB  1 
ATOM   9219  C  CG1 . ILE D 2 80  ? 170.607 130.641 182.960 1.00 118.80 ? 80  ILE B CG1 1 
ATOM   9220  C  CG2 . ILE D 2 80  ? 169.960 132.691 184.235 1.00 118.80 ? 80  ILE B CG2 1 
ATOM   9221  C  CD1 . ILE D 2 80  ? 169.613 130.490 181.834 1.00 118.80 ? 80  ILE B CD1 1 
ATOM   9222  N  N   . ARG D 2 81  ? 173.023 129.745 185.384 1.00 116.61 ? 81  ARG B N   1 
ATOM   9223  C  CA  . ARG D 2 81  ? 174.444 129.724 185.077 1.00 116.61 ? 81  ARG B CA  1 
ATOM   9224  C  C   . ARG D 2 81  ? 174.683 128.967 183.773 1.00 116.61 ? 81  ARG B C   1 
ATOM   9225  O  O   . ARG D 2 81  ? 173.852 128.153 183.357 1.00 116.61 ? 81  ARG B O   1 
ATOM   9226  C  CB  . ARG D 2 81  ? 175.240 129.081 186.224 1.00 116.61 ? 81  ARG B CB  1 
ATOM   9227  N  N   . PRO D 2 82  ? 175.803 129.227 183.091 1.00 131.13 ? 82  PRO B N   1 
ATOM   9228  C  CA  . PRO D 2 82  ? 176.044 128.561 181.797 1.00 131.13 ? 82  PRO B CA  1 
ATOM   9229  C  C   . PRO D 2 82  ? 176.052 127.038 181.843 1.00 131.13 ? 82  PRO B C   1 
ATOM   9230  O  O   . PRO D 2 82  ? 175.643 126.400 180.867 1.00 131.13 ? 82  PRO B O   1 
ATOM   9231  C  CB  . PRO D 2 82  ? 177.404 129.126 181.361 1.00 131.13 ? 82  PRO B CB  1 
ATOM   9232  C  CG  . PRO D 2 82  ? 178.048 129.609 182.612 1.00 131.13 ? 82  PRO B CG  1 
ATOM   9233  C  CD  . PRO D 2 82  ? 176.930 130.091 183.483 1.00 131.13 ? 82  PRO B CD  1 
ATOM   9234  N  N   . ASP D 2 83  ? 176.522 126.421 182.922 1.00 136.83 ? 83  ASP B N   1 
ATOM   9235  C  CA  . ASP D 2 83  ? 176.513 124.961 182.965 1.00 136.83 ? 83  ASP B CA  1 
ATOM   9236  C  C   . ASP D 2 83  ? 175.097 124.385 183.007 1.00 136.83 ? 83  ASP B C   1 
ATOM   9237  O  O   . ASP D 2 83  ? 174.802 123.406 182.314 1.00 136.83 ? 83  ASP B O   1 
ATOM   9238  C  CB  . ASP D 2 83  ? 177.319 124.469 184.167 1.00 136.83 ? 83  ASP B CB  1 
ATOM   9239  N  N   . ASN D 2 84  ? 174.205 124.986 183.796 1.00 139.47 ? 84  ASN B N   1 
ATOM   9240  C  CA  . ASN D 2 84  ? 172.850 124.479 183.999 1.00 139.47 ? 84  ASN B CA  1 
ATOM   9241  C  C   . ASN D 2 84  ? 171.787 125.067 183.063 1.00 139.47 ? 84  ASN B C   1 
ATOM   9242  O  O   . ASN D 2 84  ? 170.637 125.224 183.499 1.00 139.47 ? 84  ASN B O   1 
ATOM   9243  C  CB  . ASN D 2 84  ? 172.441 124.674 185.458 1.00 139.47 ? 84  ASN B CB  1 
ATOM   9244  C  CG  . ASN D 2 84  ? 172.375 126.126 185.852 1.00 139.47 ? 84  ASN B CG  1 
ATOM   9245  O  OD1 . ASN D 2 84  ? 173.395 126.740 186.132 1.00 139.47 ? 84  ASN B OD1 1 
ATOM   9246  N  ND2 . ASN D 2 84  ? 171.179 126.689 185.852 1.00 139.47 ? 84  ASN B ND2 1 
ATOM   9247  N  N   . MET D 2 85  ? 172.108 125.416 181.810 1.00 140.60 ? 85  MET B N   1 
ATOM   9248  C  CA  . MET D 2 85  ? 171.025 125.865 180.931 1.00 140.60 ? 85  MET B CA  1 
ATOM   9249  C  C   . MET D 2 85  ? 169.957 124.796 180.724 1.00 140.60 ? 85  MET B C   1 
ATOM   9250  O  O   . MET D 2 85  ? 168.816 125.138 180.391 1.00 140.60 ? 85  MET B O   1 
ATOM   9251  C  CB  . MET D 2 85  ? 171.481 126.286 179.523 1.00 140.60 ? 85  MET B CB  1 
ATOM   9252  C  CG  . MET D 2 85  ? 171.867 127.749 179.304 1.00 140.60 ? 85  MET B CG  1 
ATOM   9253  S  SD  . MET D 2 85  ? 172.977 128.019 177.895 1.00 140.60 ? 85  MET B SD  1 
ATOM   9254  C  CE  . MET D 2 85  ? 174.608 127.981 178.598 1.00 140.60 ? 85  MET B CE  1 
ATOM   9255  N  N   . SER D 2 86  ? 170.298 123.518 180.896 1.00 138.62 ? 86  SER B N   1 
ATOM   9256  C  CA  . SER D 2 86  ? 169.337 122.445 180.657 1.00 138.62 ? 86  SER B CA  1 
ATOM   9257  C  C   . SER D 2 86  ? 168.138 122.516 181.600 1.00 138.62 ? 86  SER B C   1 
ATOM   9258  O  O   . SER D 2 86  ? 166.999 122.288 181.175 1.00 138.62 ? 86  SER B O   1 
ATOM   9259  C  CB  . SER D 2 86  ? 170.031 121.089 180.783 1.00 138.62 ? 86  SER B CB  1 
ATOM   9260  N  N   . GLU D 2 87  ? 168.367 122.814 182.884 1.00 140.80 ? 87  GLU B N   1 
ATOM   9261  C  CA  . GLU D 2 87  ? 167.260 122.800 183.840 1.00 140.80 ? 87  GLU B CA  1 
ATOM   9262  C  C   . GLU D 2 87  ? 166.227 123.875 183.520 1.00 140.80 ? 87  GLU B C   1 
ATOM   9263  O  O   . GLU D 2 87  ? 165.019 123.637 183.634 1.00 140.80 ? 87  GLU B O   1 
ATOM   9264  C  CB  . GLU D 2 87  ? 167.795 122.974 185.261 1.00 140.80 ? 87  GLU B CB  1 
ATOM   9265  N  N   . TYR D 2 88  ? 166.681 125.064 183.122 1.00 139.94 ? 88  TYR B N   1 
ATOM   9266  C  CA  . TYR D 2 88  ? 165.803 126.199 182.869 1.00 139.94 ? 88  TYR B CA  1 
ATOM   9267  C  C   . TYR D 2 88  ? 165.486 126.383 181.390 1.00 139.94 ? 88  TYR B C   1 
ATOM   9268  O  O   . TYR D 2 88  ? 165.027 127.461 180.995 1.00 139.94 ? 88  TYR B O   1 
ATOM   9269  C  CB  . TYR D 2 88  ? 166.381 127.485 183.465 1.00 139.94 ? 88  TYR B CB  1 
ATOM   9270  C  CG  . TYR D 2 88  ? 166.741 127.378 184.928 1.00 139.94 ? 88  TYR B CG  1 
ATOM   9271  C  CD1 . TYR D 2 88  ? 167.969 126.886 185.338 1.00 139.94 ? 88  TYR B CD1 1 
ATOM   9272  C  CD2 . TYR D 2 88  ? 165.838 127.780 185.905 1.00 139.94 ? 88  TYR B CD2 1 
ATOM   9273  C  CE1 . TYR D 2 88  ? 168.282 126.793 186.682 1.00 139.94 ? 88  TYR B CE1 1 
ATOM   9274  C  CE2 . TYR D 2 88  ? 166.145 127.693 187.247 1.00 139.94 ? 88  TYR B CE2 1 
ATOM   9275  C  CZ  . TYR D 2 88  ? 167.369 127.199 187.631 1.00 139.94 ? 88  TYR B CZ  1 
ATOM   9276  O  OH  . TYR D 2 88  ? 167.684 127.109 188.967 1.00 139.94 ? 88  TYR B OH  1 
ATOM   9277  N  N   . SER D 2 89  ? 165.724 125.358 180.566 1.00 140.37 ? 89  SER B N   1 
ATOM   9278  C  CA  . SER D 2 89  ? 165.460 125.473 179.134 1.00 140.37 ? 89  SER B CA  1 
ATOM   9279  C  C   . SER D 2 89  ? 164.016 125.871 178.861 1.00 140.37 ? 89  SER B C   1 
ATOM   9280  O  O   . SER D 2 89  ? 163.735 126.552 177.869 1.00 140.37 ? 89  SER B O   1 
ATOM   9281  C  CB  . SER D 2 89  ? 165.792 124.155 178.434 1.00 140.37 ? 89  SER B CB  1 
ATOM   9282  N  N   . LYS D 2 90  ? 163.089 125.454 179.726 1.00 133.73 ? 90  LYS B N   1 
ATOM   9283  C  CA  . LYS D 2 90  ? 161.685 125.801 179.532 1.00 133.73 ? 90  LYS B CA  1 
ATOM   9284  C  C   . LYS D 2 90  ? 161.447 127.285 179.789 1.00 133.73 ? 90  LYS B C   1 
ATOM   9285  O  O   . LYS D 2 90  ? 160.713 127.940 179.039 1.00 133.73 ? 90  LYS B O   1 
ATOM   9286  C  CB  . LYS D 2 90  ? 160.797 124.937 180.427 1.00 133.73 ? 90  LYS B CB  1 
ATOM   9287  N  N   . GLN D 2 91  ? 162.053 127.836 180.844 1.00 137.52 ? 91  GLN B N   1 
ATOM   9288  C  CA  . GLN D 2 91  ? 161.835 129.236 181.191 1.00 137.52 ? 91  GLN B CA  1 
ATOM   9289  C  C   . GLN D 2 91  ? 162.602 130.197 180.291 1.00 137.52 ? 91  GLN B C   1 
ATOM   9290  O  O   . GLN D 2 91  ? 162.333 131.402 180.337 1.00 137.52 ? 91  GLN B O   1 
ATOM   9291  C  CB  . GLN D 2 91  ? 162.225 129.526 182.650 1.00 137.52 ? 91  GLN B CB  1 
ATOM   9292  C  CG  . GLN D 2 91  ? 161.428 128.828 183.772 1.00 137.52 ? 91  GLN B CG  1 
ATOM   9293  C  CD  . GLN D 2 91  ? 161.539 127.310 183.794 1.00 137.52 ? 91  GLN B CD  1 
ATOM   9294  O  OE1 . GLN D 2 91  ? 161.629 126.658 182.761 1.00 137.52 ? 91  GLN B OE1 1 
ATOM   9295  N  NE2 . GLN D 2 91  ? 161.524 126.742 184.994 1.00 137.52 ? 91  GLN B NE2 1 
ATOM   9296  N  N   . MET D 2 92  ? 163.541 129.706 179.479 1.00 134.70 ? 92  MET B N   1 
ATOM   9297  C  CA  . MET D 2 92  ? 164.272 130.581 178.569 1.00 134.70 ? 92  MET B CA  1 
ATOM   9298  C  C   . MET D 2 92  ? 163.399 131.125 177.446 1.00 134.70 ? 92  MET B C   1 
ATOM   9299  O  O   . MET D 2 92  ? 163.833 132.044 176.742 1.00 134.70 ? 92  MET B O   1 
ATOM   9300  C  CB  . MET D 2 92  ? 165.469 129.846 177.960 1.00 134.70 ? 92  MET B CB  1 
ATOM   9301  C  CG  . MET D 2 92  ? 166.506 129.362 178.955 1.00 134.70 ? 92  MET B CG  1 
ATOM   9302  S  SD  . MET D 2 92  ? 168.173 129.862 178.479 1.00 134.70 ? 92  MET B SD  1 
ATOM   9303  C  CE  . MET D 2 92  ? 168.294 129.138 176.844 1.00 134.70 ? 92  MET B CE  1 
ATOM   9304  N  N   . GLN D 2 93  ? 162.197 130.589 177.260 1.00 121.24 ? 93  GLN B N   1 
ATOM   9305  C  CA  . GLN D 2 93  ? 161.267 131.098 176.263 1.00 121.24 ? 93  GLN B CA  1 
ATOM   9306  C  C   . GLN D 2 93  ? 160.268 132.090 176.836 1.00 121.24 ? 93  GLN B C   1 
ATOM   9307  O  O   . GLN D 2 93  ? 159.827 132.995 176.120 1.00 121.24 ? 93  GLN B O   1 
ATOM   9308  C  CB  . GLN D 2 93  ? 160.507 129.940 175.606 1.00 121.24 ? 93  GLN B CB  1 
ATOM   9309  N  N   . ARG D 2 94  ? 159.905 131.943 178.111 1.00 127.17 ? 94  ARG B N   1 
ATOM   9310  C  CA  . ARG D 2 94  ? 158.993 132.882 178.752 1.00 127.17 ? 94  ARG B CA  1 
ATOM   9311  C  C   . ARG D 2 94  ? 159.652 134.223 179.040 1.00 127.17 ? 94  ARG B C   1 
ATOM   9312  O  O   . ARG D 2 94  ? 158.954 135.237 179.137 1.00 127.17 ? 94  ARG B O   1 
ATOM   9313  C  CB  . ARG D 2 94  ? 158.453 132.274 180.049 1.00 127.17 ? 94  ARG B CB  1 
ATOM   9314  C  CG  . ARG D 2 94  ? 157.348 133.074 180.720 1.00 127.17 ? 94  ARG B CG  1 
ATOM   9315  C  CD  . ARG D 2 94  ? 156.620 132.234 181.769 1.00 127.17 ? 94  ARG B CD  1 
ATOM   9316  N  NE  . ARG D 2 94  ? 156.339 132.921 183.030 1.00 127.17 ? 94  ARG B NE  1 
ATOM   9317  C  CZ  . ARG D 2 94  ? 155.802 134.128 183.164 1.00 127.17 ? 94  ARG B CZ  1 
ATOM   9318  N  NH1 . ARG D 2 94  ? 155.402 134.836 182.119 1.00 127.17 ? 94  ARG B NH1 1 
ATOM   9319  N  NH2 . ARG D 2 94  ? 155.648 134.635 184.383 1.00 127.17 ? 94  ARG B NH2 1 
ATOM   9320  N  N   . PHE D 2 95  ? 160.978 134.256 179.160 1.00 113.92 ? 95  PHE B N   1 
ATOM   9321  C  CA  . PHE D 2 95  ? 161.694 135.471 179.517 1.00 113.92 ? 95  PHE B CA  1 
ATOM   9322  C  C   . PHE D 2 95  ? 162.626 135.968 178.422 1.00 113.92 ? 95  PHE B C   1 
ATOM   9323  O  O   . PHE D 2 95  ? 163.338 136.956 178.640 1.00 113.92 ? 95  PHE B O   1 
ATOM   9324  C  CB  . PHE D 2 95  ? 162.486 135.251 180.812 1.00 113.92 ? 95  PHE B CB  1 
ATOM   9325  C  CG  . PHE D 2 95  ? 161.620 135.117 182.032 1.00 113.92 ? 95  PHE B CG  1 
ATOM   9326  C  CD1 . PHE D 2 95  ? 160.662 136.072 182.323 1.00 113.92 ? 95  PHE B CD1 1 
ATOM   9327  C  CD2 . PHE D 2 95  ? 161.759 134.034 182.882 1.00 113.92 ? 95  PHE B CD2 1 
ATOM   9328  C  CE1 . PHE D 2 95  ? 159.864 135.954 183.444 1.00 113.92 ? 95  PHE B CE1 1 
ATOM   9329  C  CE2 . PHE D 2 95  ? 160.963 133.911 184.004 1.00 113.92 ? 95  PHE B CE2 1 
ATOM   9330  C  CZ  . PHE D 2 95  ? 160.014 134.872 184.285 1.00 113.92 ? 95  PHE B CZ  1 
ATOM   9331  N  N   . ASN D 2 96  ? 162.643 135.316 177.257 1.00 113.92 ? 96  ASN B N   1 
ATOM   9332  C  CA  . ASN D 2 96  ? 163.395 135.788 176.092 1.00 113.92 ? 96  ASN B CA  1 
ATOM   9333  C  C   . ASN D 2 96  ? 164.884 135.941 176.405 1.00 113.92 ? 96  ASN B C   1 
ATOM   9334  O  O   . ASN D 2 96  ? 165.511 136.944 176.061 1.00 113.92 ? 96  ASN B O   1 
ATOM   9335  C  CB  . ASN D 2 96  ? 162.807 137.096 175.555 1.00 113.92 ? 96  ASN B CB  1 
ATOM   9336  C  CG  . ASN D 2 96  ? 163.368 137.479 174.198 1.00 113.92 ? 96  ASN B CG  1 
ATOM   9337  O  OD1 . ASN D 2 96  ? 163.097 136.822 173.192 1.00 113.92 ? 96  ASN B OD1 1 
ATOM   9338  N  ND2 . ASN D 2 96  ? 164.154 138.548 174.164 1.00 113.92 ? 96  ASN B ND2 1 
ATOM   9339  N  N   . VAL D 2 97  ? 165.455 134.944 177.077 1.00 113.92 ? 97  VAL B N   1 
ATOM   9340  C  CA  . VAL D 2 97  ? 166.884 134.907 177.364 1.00 113.92 ? 97  VAL B CA  1 
ATOM   9341  C  C   . VAL D 2 97  ? 167.462 133.629 176.777 1.00 113.92 ? 97  VAL B C   1 
ATOM   9342  O  O   . VAL D 2 97  ? 166.971 132.531 177.065 1.00 113.92 ? 97  VAL B O   1 
ATOM   9343  C  CB  . VAL D 2 97  ? 167.159 134.970 178.878 1.00 113.92 ? 97  VAL B CB  1 
ATOM   9344  C  CG1 . VAL D 2 97  ? 168.599 134.578 179.175 1.00 113.92 ? 97  VAL B CG1 1 
ATOM   9345  C  CG2 . VAL D 2 97  ? 166.855 136.349 179.422 1.00 113.92 ? 97  VAL B CG2 1 
ATOM   9346  N  N   . GLY D 2 98  ? 168.501 133.770 175.958 1.00 122.55 ? 98  GLY B N   1 
ATOM   9347  C  CA  . GLY D 2 98  ? 169.250 132.620 175.491 1.00 122.55 ? 98  GLY B CA  1 
ATOM   9348  C  C   . GLY D 2 98  ? 169.641 132.653 174.026 1.00 122.55 ? 98  GLY B C   1 
ATOM   9349  O  O   . GLY D 2 98  ? 170.643 132.047 173.638 1.00 122.55 ? 98  GLY B O   1 
ATOM   9350  N  N   . GLU D 2 99  ? 168.868 133.362 173.204 1.00 118.51 ? 99  GLU B N   1 
ATOM   9351  C  CA  . GLU D 2 99  ? 169.148 133.411 171.774 1.00 118.51 ? 99  GLU B CA  1 
ATOM   9352  C  C   . GLU D 2 99  ? 169.629 134.787 171.330 1.00 118.51 ? 99  GLU B C   1 
ATOM   9353  O  O   . GLU D 2 99  ? 170.819 134.981 171.065 1.00 118.51 ? 99  GLU B O   1 
ATOM   9354  C  CB  . GLU D 2 99  ? 167.904 133.011 170.978 1.00 118.51 ? 99  GLU B CB  1 
ATOM   9355  N  N   . ASP D 2 100 ? 168.702 135.744 171.238 1.00 123.89 ? 100 ASP B N   1 
ATOM   9356  C  CA  . ASP D 2 100 ? 169.063 137.088 170.799 1.00 123.89 ? 100 ASP B CA  1 
ATOM   9357  C  C   . ASP D 2 100 ? 170.014 137.754 171.779 1.00 123.89 ? 100 ASP B C   1 
ATOM   9358  O  O   . ASP D 2 100 ? 170.917 138.498 171.377 1.00 123.89 ? 100 ASP B O   1 
ATOM   9359  C  CB  . ASP D 2 100 ? 167.802 137.931 170.629 1.00 123.89 ? 100 ASP B CB  1 
ATOM   9360  N  N   . CYS D 2 101 ? 169.822 137.506 173.072 1.00 130.73 ? 101 CYS B N   1 
ATOM   9361  C  CA  . CYS D 2 101 ? 170.666 138.049 174.131 1.00 130.73 ? 101 CYS B CA  1 
ATOM   9362  C  C   . CYS D 2 101 ? 171.181 136.872 174.955 1.00 130.73 ? 101 CYS B C   1 
ATOM   9363  O  O   . CYS D 2 101 ? 170.768 136.677 176.107 1.00 130.73 ? 101 CYS B O   1 
ATOM   9364  C  CB  . CYS D 2 101 ? 169.891 139.050 174.984 1.00 130.73 ? 101 CYS B CB  1 
ATOM   9365  S  SG  . CYS D 2 101 ? 170.858 139.851 176.257 1.00 130.73 ? 101 CYS B SG  1 
ATOM   9366  N  N   . PRO D 2 102 ? 172.067 136.055 174.382 1.00 134.17 ? 102 PRO B N   1 
ATOM   9367  C  CA  . PRO D 2 102 ? 172.442 134.789 175.026 1.00 134.17 ? 102 PRO B CA  1 
ATOM   9368  C  C   . PRO D 2 102 ? 173.024 134.976 176.421 1.00 134.17 ? 102 PRO B C   1 
ATOM   9369  O  O   . PRO D 2 102 ? 173.572 136.024 176.771 1.00 134.17 ? 102 PRO B O   1 
ATOM   9370  C  CB  . PRO D 2 102 ? 173.484 134.183 174.075 1.00 134.17 ? 102 PRO B CB  1 
ATOM   9371  C  CG  . PRO D 2 102 ? 173.600 135.097 172.913 1.00 134.17 ? 102 PRO B CG  1 
ATOM   9372  C  CD  . PRO D 2 102 ? 172.868 136.359 173.184 1.00 134.17 ? 102 PRO B CD  1 
ATOM   9373  N  N   . VAL D 2 103 ? 172.890 133.921 177.219 1.00 132.07 ? 103 VAL B N   1 
ATOM   9374  C  CA  . VAL D 2 103 ? 173.444 133.869 178.566 1.00 132.07 ? 103 VAL B CA  1 
ATOM   9375  C  C   . VAL D 2 103 ? 174.929 133.543 178.486 1.00 132.07 ? 103 VAL B C   1 
ATOM   9376  O  O   . VAL D 2 103 ? 175.366 132.770 177.625 1.00 132.07 ? 103 VAL B O   1 
ATOM   9377  C  CB  . VAL D 2 103 ? 172.672 132.837 179.411 1.00 132.07 ? 103 VAL B CB  1 
ATOM   9378  C  CG1 . VAL D 2 103 ? 172.461 131.555 178.618 1.00 132.07 ? 103 VAL B CG1 1 
ATOM   9379  C  CG2 . VAL D 2 103 ? 173.379 132.549 180.729 1.00 132.07 ? 103 VAL B CG2 1 
ATOM   9380  N  N   . PHE D 2 104 ? 175.715 134.131 179.389 1.00 122.08 ? 104 PHE B N   1 
ATOM   9381  C  CA  . PHE D 2 104 ? 177.154 133.915 179.441 1.00 122.08 ? 104 PHE B CA  1 
ATOM   9382  C  C   . PHE D 2 104 ? 177.598 133.870 180.897 1.00 122.08 ? 104 PHE B C   1 
ATOM   9383  O  O   . PHE D 2 104 ? 176.780 133.938 181.822 1.00 122.08 ? 104 PHE B O   1 
ATOM   9384  C  CB  . PHE D 2 104 ? 177.896 134.997 178.646 1.00 122.08 ? 104 PHE B CB  1 
ATOM   9385  C  CG  . PHE D 2 104 ? 177.629 136.395 179.126 1.00 122.08 ? 104 PHE B CG  1 
ATOM   9386  C  CD1 . PHE D 2 104 ? 178.348 136.933 180.179 1.00 122.08 ? 104 PHE B CD1 1 
ATOM   9387  C  CD2 . PHE D 2 104 ? 176.649 137.168 178.529 1.00 122.08 ? 104 PHE B CD2 1 
ATOM   9388  C  CE1 . PHE D 2 104 ? 178.101 138.213 180.622 1.00 122.08 ? 104 PHE B CE1 1 
ATOM   9389  C  CE2 . PHE D 2 104 ? 176.396 138.450 178.970 1.00 122.08 ? 104 PHE B CE2 1 
ATOM   9390  C  CZ  . PHE D 2 104 ? 177.123 138.973 180.017 1.00 122.08 ? 104 PHE B CZ  1 
ATOM   9391  N  N   . ASP D 2 105 ? 178.909 133.756 181.104 1.00 127.75 ? 105 ASP B N   1 
ATOM   9392  C  CA  . ASP D 2 105 ? 179.438 133.604 182.453 1.00 127.75 ? 105 ASP B CA  1 
ATOM   9393  C  C   . ASP D 2 105 ? 179.346 134.910 183.230 1.00 127.75 ? 105 ASP B C   1 
ATOM   9394  O  O   . ASP D 2 105 ? 179.705 135.978 182.725 1.00 127.75 ? 105 ASP B O   1 
ATOM   9395  C  CB  . ASP D 2 105 ? 180.890 133.132 182.396 1.00 127.75 ? 105 ASP B CB  1 
ATOM   9396  N  N   . GLY D 2 106 ? 178.874 134.813 184.468 1.00 122.75 ? 106 GLY B N   1 
ATOM   9397  C  CA  . GLY D 2 106 ? 178.732 135.971 185.336 1.00 122.75 ? 106 GLY B CA  1 
ATOM   9398  C  C   . GLY D 2 106 ? 177.746 137.001 184.833 1.00 122.75 ? 106 GLY B C   1 
ATOM   9399  O  O   . GLY D 2 106 ? 178.004 138.207 184.939 1.00 122.75 ? 106 GLY B O   1 
ATOM   9400  N  N   . LEU D 2 107 ? 176.622 136.554 184.268 1.00 116.55 ? 107 LEU B N   1 
ATOM   9401  C  CA  . LEU D 2 107 ? 175.648 137.497 183.728 1.00 116.55 ? 107 LEU B CA  1 
ATOM   9402  C  C   . LEU D 2 107 ? 175.064 138.360 184.840 1.00 116.55 ? 107 LEU B C   1 
ATOM   9403  O  O   . LEU D 2 107 ? 174.968 139.594 184.713 1.00 116.55 ? 107 LEU B O   1 
ATOM   9404  C  CB  . LEU D 2 107 ? 174.547 136.739 182.991 1.00 116.55 ? 107 LEU B CB  1 
ATOM   9405  C  CG  . LEU D 2 107 ? 173.390 137.581 182.464 1.00 116.55 ? 107 LEU B CG  1 
ATOM   9406  C  CD1 . LEU D 2 107 ? 173.944 138.785 181.730 1.00 116.55 ? 107 LEU B CD1 1 
ATOM   9407  C  CD2 . LEU D 2 107 ? 172.501 136.749 181.559 1.00 116.55 ? 107 LEU B CD2 1 
ATOM   9408  N  N   . PHE D 2 108 ? 174.708 137.729 185.960 1.00 125.08 ? 108 PHE B N   1 
ATOM   9409  C  CA  . PHE D 2 108 ? 174.150 138.492 187.063 1.00 125.08 ? 108 PHE B CA  1 
ATOM   9410  C  C   . PHE D 2 108 ? 175.208 139.415 187.639 1.00 125.08 ? 108 PHE B C   1 
ATOM   9411  O  O   . PHE D 2 108 ? 174.894 140.529 188.060 1.00 125.08 ? 108 PHE B O   1 
ATOM   9412  C  CB  . PHE D 2 108 ? 173.590 137.557 188.134 1.00 125.08 ? 108 PHE B CB  1 
ATOM   9413  C  CG  . PHE D 2 108 ? 172.724 138.249 189.150 1.00 125.08 ? 108 PHE B CG  1 
ATOM   9414  C  CD1 . PHE D 2 108 ? 171.551 138.874 188.763 1.00 125.08 ? 108 PHE B CD1 1 
ATOM   9415  C  CD2 . PHE D 2 108 ? 173.074 138.266 190.489 1.00 125.08 ? 108 PHE B CD2 1 
ATOM   9416  C  CE1 . PHE D 2 108 ? 170.748 139.508 189.691 1.00 125.08 ? 108 PHE B CE1 1 
ATOM   9417  C  CE2 . PHE D 2 108 ? 172.272 138.899 191.423 1.00 125.08 ? 108 PHE B CE2 1 
ATOM   9418  C  CZ  . PHE D 2 108 ? 171.108 139.520 191.022 1.00 125.08 ? 108 PHE B CZ  1 
ATOM   9419  N  N   . GLU D 2 109 ? 176.464 138.956 187.704 1.00 121.69 ? 109 GLU B N   1 
ATOM   9420  C  CA  . GLU D 2 109 ? 177.517 139.834 188.199 1.00 121.69 ? 109 GLU B CA  1 
ATOM   9421  C  C   . GLU D 2 109 ? 177.678 141.031 187.273 1.00 121.69 ? 109 GLU B C   1 
ATOM   9422  O  O   . GLU D 2 109 ? 178.036 142.127 187.721 1.00 121.69 ? 109 GLU B O   1 
ATOM   9423  C  CB  . GLU D 2 109 ? 178.831 139.066 188.331 1.00 121.69 ? 109 GLU B CB  1 
ATOM   9424  N  N   . PHE D 2 110 ? 177.415 140.832 185.974 1.00 117.03 ? 110 PHE B N   1 
ATOM   9425  C  CA  . PHE D 2 110 ? 177.481 141.928 185.014 1.00 117.03 ? 110 PHE B CA  1 
ATOM   9426  C  C   . PHE D 2 110 ? 176.401 142.957 185.303 1.00 117.03 ? 110 PHE B C   1 
ATOM   9427  O  O   . PHE D 2 110 ? 176.650 144.169 185.241 1.00 117.03 ? 110 PHE B O   1 
ATOM   9428  C  CB  . PHE D 2 110 ? 177.346 141.408 183.580 1.00 117.03 ? 110 PHE B CB  1 
ATOM   9429  C  CG  . PHE D 2 110 ? 177.309 142.499 182.537 1.00 117.03 ? 110 PHE B CG  1 
ATOM   9430  C  CD1 . PHE D 2 110 ? 178.235 143.530 182.556 1.00 117.03 ? 110 PHE B CD1 1 
ATOM   9431  C  CD2 . PHE D 2 110 ? 176.348 142.493 181.537 1.00 117.03 ? 110 PHE B CD2 1 
ATOM   9432  C  CE1 . PHE D 2 110 ? 178.203 144.534 181.602 1.00 117.03 ? 110 PHE B CE1 1 
ATOM   9433  C  CE2 . PHE D 2 110 ? 176.312 143.494 180.580 1.00 117.03 ? 110 PHE B CE2 1 
ATOM   9434  C  CZ  . PHE D 2 110 ? 177.239 144.514 180.612 1.00 117.03 ? 110 PHE B CZ  1 
ATOM   9435  N  N   . CYS D 2 111 ? 175.197 142.490 185.640 1.00 123.56 ? 111 CYS B N   1 
ATOM   9436  C  CA  . CYS D 2 111 ? 174.141 143.441 185.963 1.00 123.56 ? 111 CYS B CA  1 
ATOM   9437  C  C   . CYS D 2 111 ? 174.256 143.999 187.376 1.00 123.56 ? 111 CYS B C   1 
ATOM   9438  O  O   . CYS D 2 111 ? 173.620 145.014 187.680 1.00 123.56 ? 111 CYS B O   1 
ATOM   9439  C  CB  . CYS D 2 111 ? 172.771 142.784 185.785 1.00 123.56 ? 111 CYS B CB  1 
ATOM   9440  S  SG  . CYS D 2 111 ? 172.444 142.178 184.117 1.00 123.56 ? 111 CYS B SG  1 
ATOM   9441  N  N   . GLN D 2 112 ? 175.040 143.358 188.248 1.00 132.70 ? 112 GLN B N   1 
ATOM   9442  C  CA  . GLN D 2 112 ? 175.377 143.948 189.541 1.00 132.70 ? 112 GLN B CA  1 
ATOM   9443  C  C   . GLN D 2 112 ? 176.120 145.266 189.396 1.00 132.70 ? 112 GLN B C   1 
ATOM   9444  O  O   . GLN D 2 112 ? 176.070 146.102 190.304 1.00 132.70 ? 112 GLN B O   1 
ATOM   9445  C  CB  . GLN D 2 112 ? 176.235 142.990 190.373 1.00 132.70 ? 112 GLN B CB  1 
ATOM   9446  C  CG  . GLN D 2 112 ? 175.564 141.685 190.756 1.00 132.70 ? 112 GLN B CG  1 
ATOM   9447  C  CD  . GLN D 2 112 ? 174.231 141.889 191.437 1.00 132.70 ? 112 GLN B CD  1 
ATOM   9448  O  OE1 . GLN D 2 112 ? 173.182 141.833 190.799 1.00 132.70 ? 112 GLN B OE1 1 
ATOM   9449  N  NE2 . GLN D 2 112 ? 174.263 142.115 192.745 1.00 132.70 ? 112 GLN B NE2 1 
ATOM   9450  N  N   . LEU D 2 113 ? 176.803 145.468 188.274 1.00 126.46 ? 113 LEU B N   1 
ATOM   9451  C  CA  . LEU D 2 113 ? 177.619 146.649 188.029 1.00 126.46 ? 113 LEU B CA  1 
ATOM   9452  C  C   . LEU D 2 113 ? 177.051 147.573 186.967 1.00 126.46 ? 113 LEU B C   1 
ATOM   9453  O  O   . LEU D 2 113 ? 177.188 148.791 187.086 1.00 126.46 ? 113 LEU B O   1 
ATOM   9454  C  CB  . LEU D 2 113 ? 179.037 146.221 187.631 1.00 126.46 ? 113 LEU B CB  1 
ATOM   9455  C  CG  . LEU D 2 113 ? 179.630 145.168 188.572 1.00 126.46 ? 113 LEU B CG  1 
ATOM   9456  C  CD1 . LEU D 2 113 ? 181.022 144.747 188.139 1.00 126.46 ? 113 LEU B CD1 1 
ATOM   9457  C  CD2 . LEU D 2 113 ? 179.646 145.672 190.007 1.00 126.46 ? 113 LEU B CD2 1 
ATOM   9458  N  N   . SER D 2 114 ? 176.427 147.030 185.916 1.00 118.02 ? 114 SER B N   1 
ATOM   9459  C  CA  . SER D 2 114 ? 175.794 147.896 184.928 1.00 118.02 ? 114 SER B CA  1 
ATOM   9460  C  C   . SER D 2 114 ? 174.672 148.721 185.546 1.00 118.02 ? 114 SER B C   1 
ATOM   9461  O  O   . SER D 2 114 ? 174.441 149.864 185.134 1.00 118.02 ? 114 SER B O   1 
ATOM   9462  C  CB  . SER D 2 114 ? 175.264 147.063 183.762 1.00 118.02 ? 114 SER B CB  1 
ATOM   9463  O  OG  . SER D 2 114 ? 174.784 147.895 182.720 1.00 118.02 ? 114 SER B OG  1 
ATOM   9464  N  N   . THR D 2 115 ? 173.965 148.161 186.528 1.00 122.27 ? 115 THR B N   1 
ATOM   9465  C  CA  . THR D 2 115 ? 172.909 148.869 187.241 1.00 122.27 ? 115 THR B CA  1 
ATOM   9466  C  C   . THR D 2 115 ? 173.421 149.587 188.486 1.00 122.27 ? 115 THR B C   1 
ATOM   9467  O  O   . THR D 2 115 ? 172.847 150.611 188.879 1.00 122.27 ? 115 THR B O   1 
ATOM   9468  C  CB  . THR D 2 115 ? 171.794 147.875 187.611 1.00 122.27 ? 115 THR B CB  1 
ATOM   9469  O  OG1 . THR D 2 115 ? 170.968 147.638 186.465 1.00 122.27 ? 115 THR B OG1 1 
ATOM   9470  C  CG2 . THR D 2 115 ? 170.921 148.381 188.754 1.00 122.27 ? 115 THR B CG2 1 
ATOM   9471  N  N   . GLY D 2 116 ? 174.531 149.122 189.062 1.00 123.21 ? 116 GLY B N   1 
ATOM   9472  C  CA  . GLY D 2 116 ? 175.043 149.684 190.301 1.00 123.21 ? 116 GLY B CA  1 
ATOM   9473  C  C   . GLY D 2 116 ? 175.462 151.136 190.205 1.00 123.21 ? 116 GLY B C   1 
ATOM   9474  O  O   . GLY D 2 116 ? 175.600 151.800 191.237 1.00 123.21 ? 116 GLY B O   1 
ATOM   9475  N  N   . GLY D 2 117 ? 175.670 151.643 188.995 1.00 113.92 ? 117 GLY B N   1 
ATOM   9476  C  CA  . GLY D 2 117 ? 176.134 153.002 188.798 1.00 113.92 ? 117 GLY B CA  1 
ATOM   9477  C  C   . GLY D 2 117 ? 174.999 153.989 188.636 1.00 113.92 ? 117 GLY B C   1 
ATOM   9478  O  O   . GLY D 2 117 ? 175.147 155.178 188.935 1.00 113.92 ? 117 GLY B O   1 
ATOM   9479  N  N   . SER D 2 118 ? 173.853 153.504 188.158 1.00 115.21 ? 118 SER B N   1 
ATOM   9480  C  CA  . SER D 2 118 ? 172.709 154.377 187.923 1.00 115.21 ? 118 SER B CA  1 
ATOM   9481  C  C   . SER D 2 118 ? 171.999 154.734 189.223 1.00 115.21 ? 118 SER B C   1 
ATOM   9482  O  O   . SER D 2 118 ? 171.774 155.913 189.505 1.00 115.21 ? 118 SER B O   1 
ATOM   9483  C  CB  . SER D 2 118 ? 171.740 153.710 186.951 1.00 115.21 ? 118 SER B CB  1 
ATOM   9484  O  OG  . SER D 2 118 ? 172.399 153.396 185.741 1.00 115.21 ? 118 SER B OG  1 
ATOM   9485  N  N   . VAL D 2 119 ? 171.609 153.731 190.010 1.00 122.62 ? 119 VAL B N   1 
ATOM   9486  C  CA  . VAL D 2 119 ? 170.947 153.998 191.286 1.00 122.62 ? 119 VAL B CA  1 
ATOM   9487  C  C   . VAL D 2 119 ? 171.884 154.741 192.239 1.00 122.62 ? 119 VAL B C   1 
ATOM   9488  O  O   . VAL D 2 119 ? 171.506 155.748 192.852 1.00 122.62 ? 119 VAL B O   1 
ATOM   9489  C  CB  . VAL D 2 119 ? 170.406 152.691 191.898 1.00 122.62 ? 119 VAL B CB  1 
ATOM   9490  C  CG1 . VAL D 2 119 ? 169.358 152.085 190.981 1.00 122.62 ? 119 VAL B CG1 1 
ATOM   9491  C  CG2 . VAL D 2 119 ? 171.524 151.682 192.128 1.00 122.62 ? 119 VAL B CG2 1 
ATOM   9492  N  N   . ALA D 2 120 ? 173.135 154.282 192.345 1.00 128.55 ? 120 ALA B N   1 
ATOM   9493  C  CA  . ALA D 2 120 ? 174.094 154.925 193.237 1.00 128.55 ? 120 ALA B CA  1 
ATOM   9494  C  C   . ALA D 2 120 ? 174.592 156.260 192.703 1.00 128.55 ? 120 ALA B C   1 
ATOM   9495  O  O   . ALA D 2 120 ? 175.137 157.055 193.476 1.00 128.55 ? 120 ALA B O   1 
ATOM   9496  C  CB  . ALA D 2 120 ? 175.280 153.998 193.494 1.00 128.55 ? 120 ALA B CB  1 
ATOM   9497  N  N   . GLY D 2 121 ? 174.421 156.530 191.412 1.00 122.27 ? 121 GLY B N   1 
ATOM   9498  C  CA  . GLY D 2 121 ? 174.758 157.840 190.896 1.00 122.27 ? 121 GLY B CA  1 
ATOM   9499  C  C   . GLY D 2 121 ? 173.614 158.811 191.090 1.00 122.27 ? 121 GLY B C   1 
ATOM   9500  O  O   . GLY D 2 121 ? 173.828 159.977 191.432 1.00 122.27 ? 121 GLY B O   1 
ATOM   9501  N  N   . ALA D 2 122 ? 172.387 158.336 190.872 1.00 121.64 ? 122 ALA B N   1 
ATOM   9502  C  CA  . ALA D 2 122 ? 171.207 159.133 191.176 1.00 121.64 ? 122 ALA B CA  1 
ATOM   9503  C  C   . ALA D 2 122 ? 171.089 159.432 192.662 1.00 121.64 ? 122 ALA B C   1 
ATOM   9504  O  O   . ALA D 2 122 ? 170.464 160.430 193.031 1.00 121.64 ? 122 ALA B O   1 
ATOM   9505  C  CB  . ALA D 2 122 ? 169.947 158.423 190.679 1.00 121.64 ? 122 ALA B CB  1 
ATOM   9506  N  N   . VAL D 2 123 ? 171.680 158.597 193.523 1.00 122.52 ? 123 VAL B N   1 
ATOM   9507  C  CA  . VAL D 2 123 ? 171.687 158.901 194.954 1.00 122.52 ? 123 VAL B CA  1 
ATOM   9508  C  C   . VAL D 2 123 ? 172.451 160.192 195.216 1.00 122.52 ? 123 VAL B C   1 
ATOM   9509  O  O   . VAL D 2 123 ? 172.001 161.063 195.969 1.00 122.52 ? 123 VAL B O   1 
ATOM   9510  C  CB  . VAL D 2 123 ? 172.284 157.727 195.751 1.00 122.52 ? 123 VAL B CB  1 
ATOM   9511  C  CG1 . VAL D 2 123 ? 173.004 158.230 196.997 1.00 122.52 ? 123 VAL B CG1 1 
ATOM   9512  C  CG2 . VAL D 2 123 ? 171.197 156.758 196.155 1.00 122.52 ? 123 VAL B CG2 1 
ATOM   9513  N  N   . LYS D 2 124 ? 173.627 160.331 194.604 1.00 130.84 ? 124 LYS B N   1 
ATOM   9514  C  CA  . LYS D 2 124 ? 174.384 161.568 194.753 1.00 130.84 ? 124 LYS B CA  1 
ATOM   9515  C  C   . LYS D 2 124 ? 173.736 162.717 193.988 1.00 130.84 ? 124 LYS B C   1 
ATOM   9516  O  O   . LYS D 2 124 ? 173.742 163.861 194.455 1.00 130.84 ? 124 LYS B O   1 
ATOM   9517  C  CB  . LYS D 2 124 ? 175.824 161.351 194.293 1.00 130.84 ? 124 LYS B CB  1 
ATOM   9518  C  CG  . LYS D 2 124 ? 176.829 161.293 195.429 1.00 130.84 ? 124 LYS B CG  1 
ATOM   9519  C  CD  . LYS D 2 124 ? 178.253 161.351 194.910 1.00 130.84 ? 124 LYS B CD  1 
ATOM   9520  C  CE  . LYS D 2 124 ? 179.261 161.299 196.047 1.00 130.84 ? 124 LYS B CE  1 
ATOM   9521  N  NZ  . LYS D 2 124 ? 179.266 159.976 196.728 1.00 130.84 ? 124 LYS B NZ  1 
ATOM   9522  N  N   . LEU D 2 125 ? 173.184 162.433 192.805 1.00 118.35 ? 125 LEU B N   1 
ATOM   9523  C  CA  . LEU D 2 125 ? 172.611 163.487 191.972 1.00 118.35 ? 125 LEU B CA  1 
ATOM   9524  C  C   . LEU D 2 125 ? 171.386 164.128 192.617 1.00 118.35 ? 125 LEU B C   1 
ATOM   9525  O  O   . LEU D 2 125 ? 171.259 165.359 192.634 1.00 118.35 ? 125 LEU B O   1 
ATOM   9526  C  CB  . LEU D 2 125 ? 172.269 162.931 190.591 1.00 118.35 ? 125 LEU B CB  1 
ATOM   9527  C  CG  . LEU D 2 125 ? 171.587 163.912 189.639 1.00 118.35 ? 125 LEU B CG  1 
ATOM   9528  C  CD1 . LEU D 2 125 ? 172.289 163.887 188.304 1.00 118.35 ? 125 LEU B CD1 1 
ATOM   9529  C  CD2 . LEU D 2 125 ? 170.122 163.573 189.466 1.00 118.35 ? 125 LEU B CD2 1 
ATOM   9530  N  N   . ASN D 2 126 ? 170.463 163.316 193.141 1.00 125.73 ? 126 ASN B N   1 
ATOM   9531  C  CA  . ASN D 2 126 ? 169.277 163.882 193.775 1.00 125.73 ? 126 ASN B CA  1 
ATOM   9532  C  C   . ASN D 2 126 ? 169.651 164.673 195.019 1.00 125.73 ? 126 ASN B C   1 
ATOM   9533  O  O   . ASN D 2 126 ? 169.074 165.732 195.292 1.00 125.73 ? 126 ASN B O   1 
ATOM   9534  C  CB  . ASN D 2 126 ? 168.254 162.780 194.085 1.00 125.73 ? 126 ASN B CB  1 
ATOM   9535  C  CG  . ASN D 2 126 ? 168.738 161.775 195.126 1.00 125.73 ? 126 ASN B CG  1 
ATOM   9536  O  OD1 . ASN D 2 126 ? 169.493 162.102 196.041 1.00 125.73 ? 126 ASN B OD1 1 
ATOM   9537  N  ND2 . ASN D 2 126 ? 168.293 160.533 194.982 1.00 125.73 ? 126 ASN B ND2 1 
ATOM   9538  N  N   . ARG D 2 127 ? 170.614 164.173 195.786 1.00 121.70 ? 127 ARG B N   1 
ATOM   9539  C  CA  . ARG D 2 127 ? 171.116 164.894 196.939 1.00 121.70 ? 127 ARG B CA  1 
ATOM   9540  C  C   . ARG D 2 127 ? 172.014 166.040 196.480 1.00 121.70 ? 127 ARG B C   1 
ATOM   9541  O  O   . ARG D 2 127 ? 172.362 166.161 195.302 1.00 121.70 ? 127 ARG B O   1 
ATOM   9542  C  CB  . ARG D 2 127 ? 171.876 163.952 197.872 1.00 121.70 ? 127 ARG B CB  1 
ATOM   9543  N  N   . GLN D 2 128 ? 172.386 166.900 197.426 1.00 124.04 ? 128 GLN B N   1 
ATOM   9544  C  CA  . GLN D 2 128 ? 173.225 168.057 197.123 1.00 124.04 ? 128 GLN B CA  1 
ATOM   9545  C  C   . GLN D 2 128 ? 174.702 167.653 197.110 1.00 124.04 ? 128 GLN B C   1 
ATOM   9546  O  O   . GLN D 2 128 ? 175.512 168.093 197.925 1.00 124.04 ? 128 GLN B O   1 
ATOM   9547  C  CB  . GLN D 2 128 ? 172.960 169.175 198.122 1.00 124.04 ? 128 GLN B CB  1 
ATOM   9548  N  N   . GLN D 2 129 ? 175.045 166.793 196.151 1.00 128.80 ? 129 GLN B N   1 
ATOM   9549  C  CA  . GLN D 2 129 ? 176.408 166.302 196.006 1.00 128.80 ? 129 GLN B CA  1 
ATOM   9550  C  C   . GLN D 2 129 ? 177.008 166.531 194.628 1.00 128.80 ? 129 GLN B C   1 
ATOM   9551  O  O   . GLN D 2 129 ? 178.233 166.627 194.520 1.00 128.80 ? 129 GLN B O   1 
ATOM   9552  C  CB  . GLN D 2 129 ? 176.483 164.794 196.304 1.00 128.80 ? 129 GLN B CB  1 
ATOM   9553  C  CG  . GLN D 2 129 ? 176.890 164.417 197.726 1.00 128.80 ? 129 GLN B CG  1 
ATOM   9554  C  CD  . GLN D 2 129 ? 175.727 164.378 198.701 1.00 128.80 ? 129 GLN B CD  1 
ATOM   9555  O  OE1 . GLN D 2 129 ? 174.789 165.165 198.606 1.00 128.80 ? 129 GLN B OE1 1 
ATOM   9556  N  NE2 . GLN D 2 129 ? 175.786 163.447 199.646 1.00 128.80 ? 129 GLN B NE2 1 
ATOM   9557  N  N   . THR D 2 130 ? 176.196 166.624 193.577 1.00 128.86 ? 130 THR B N   1 
ATOM   9558  C  CA  . THR D 2 130 ? 176.742 166.806 192.241 1.00 128.86 ? 130 THR B CA  1 
ATOM   9559  C  C   . THR D 2 130 ? 175.695 167.429 191.332 1.00 128.86 ? 130 THR B C   1 
ATOM   9560  O  O   . THR D 2 130 ? 174.491 167.307 191.569 1.00 128.86 ? 130 THR B O   1 
ATOM   9561  C  CB  . THR D 2 130 ? 177.226 165.484 191.639 1.00 128.86 ? 130 THR B CB  1 
ATOM   9562  O  OG1 . THR D 2 130 ? 177.785 165.726 190.342 1.00 128.86 ? 130 THR B OG1 1 
ATOM   9563  C  CG2 . THR D 2 130 ? 176.079 164.499 191.513 1.00 128.86 ? 130 THR B CG2 1 
ATOM   9564  N  N   . ASP D 2 131 ? 176.179 168.106 190.294 1.00 130.35 ? 131 ASP B N   1 
ATOM   9565  C  CA  . ASP D 2 131 ? 175.348 168.569 189.195 1.00 130.35 ? 131 ASP B CA  1 
ATOM   9566  C  C   . ASP D 2 131 ? 175.387 167.644 187.987 1.00 130.35 ? 131 ASP B C   1 
ATOM   9567  O  O   . ASP D 2 131 ? 174.539 167.780 187.099 1.00 130.35 ? 131 ASP B O   1 
ATOM   9568  C  CB  . ASP D 2 131 ? 175.771 169.980 188.766 1.00 130.35 ? 131 ASP B CB  1 
ATOM   9569  C  CG  . ASP D 2 131 ? 176.335 170.793 189.914 1.00 130.35 ? 131 ASP B CG  1 
ATOM   9570  O  OD1 . ASP D 2 131 ? 175.575 171.106 190.855 1.00 130.35 ? 131 ASP B OD1 1 
ATOM   9571  O  OD2 . ASP D 2 131 ? 177.539 171.122 189.874 1.00 130.35 ? 131 ASP B OD2 1 
ATOM   9572  N  N   . MET D 2 132 ? 176.333 166.705 187.937 1.00 121.25 ? 132 MET B N   1 
ATOM   9573  C  CA  . MET D 2 132 ? 176.451 165.797 186.801 1.00 121.25 ? 132 MET B CA  1 
ATOM   9574  C  C   . MET D 2 132 ? 177.042 164.476 187.269 1.00 121.25 ? 132 MET B C   1 
ATOM   9575  O  O   . MET D 2 132 ? 178.184 164.441 187.737 1.00 121.25 ? 132 MET B O   1 
ATOM   9576  C  CB  . MET D 2 132 ? 177.338 166.411 185.713 1.00 121.25 ? 132 MET B CB  1 
ATOM   9577  C  CG  . MET D 2 132 ? 176.631 167.348 184.755 1.00 121.25 ? 132 MET B CG  1 
ATOM   9578  S  SD  . MET D 2 132 ? 176.191 166.549 183.206 1.00 121.25 ? 132 MET B SD  1 
ATOM   9579  C  CE  . MET D 2 132 ? 177.787 166.032 182.612 1.00 121.25 ? 132 MET B CE  1 
ATOM   9580  N  N   . ALA D 2 133 ? 176.272 163.399 187.145 1.00 113.92 ? 133 ALA B N   1 
ATOM   9581  C  CA  . ALA D 2 133 ? 176.740 162.049 187.422 1.00 113.92 ? 133 ALA B CA  1 
ATOM   9582  C  C   . ALA D 2 133 ? 176.953 161.302 186.112 1.00 113.92 ? 133 ALA B C   1 
ATOM   9583  O  O   . ALA D 2 133 ? 176.172 161.455 185.170 1.00 113.92 ? 133 ALA B O   1 
ATOM   9584  C  CB  . ALA D 2 133 ? 175.749 161.291 188.307 1.00 113.92 ? 133 ALA B CB  1 
ATOM   9585  N  N   . VAL D 2 134 ? 178.007 160.489 186.058 1.00 113.92 ? 134 VAL B N   1 
ATOM   9586  C  CA  . VAL D 2 134 ? 178.427 159.804 184.839 1.00 113.92 ? 134 VAL B CA  1 
ATOM   9587  C  C   . VAL D 2 134 ? 178.475 158.307 185.114 1.00 113.92 ? 134 VAL B C   1 
ATOM   9588  O  O   . VAL D 2 134 ? 178.994 157.877 186.150 1.00 113.92 ? 134 VAL B O   1 
ATOM   9589  C  CB  . VAL D 2 134 ? 179.795 160.309 184.341 1.00 113.92 ? 134 VAL B CB  1 
ATOM   9590  C  CG1 . VAL D 2 134 ? 180.086 159.762 182.954 1.00 113.92 ? 134 VAL B CG1 1 
ATOM   9591  C  CG2 . VAL D 2 134 ? 179.833 161.828 184.334 1.00 113.92 ? 134 VAL B CG2 1 
ATOM   9592  N  N   . ASN D 2 135 ? 177.933 157.516 184.185 1.00 113.92 ? 135 ASN B N   1 
ATOM   9593  C  CA  . ASN D 2 135 ? 178.013 156.057 184.273 1.00 113.92 ? 135 ASN B CA  1 
ATOM   9594  C  C   . ASN D 2 135 ? 177.974 155.512 182.849 1.00 113.92 ? 135 ASN B C   1 
ATOM   9595  O  O   . ASN D 2 135 ? 176.894 155.373 182.267 1.00 113.92 ? 135 ASN B O   1 
ATOM   9596  C  CB  . ASN D 2 135 ? 176.876 155.498 185.119 1.00 113.92 ? 135 ASN B CB  1 
ATOM   9597  C  CG  . ASN D 2 135 ? 176.786 153.975 185.068 1.00 113.92 ? 135 ASN B CG  1 
ATOM   9598  O  OD1 . ASN D 2 135 ? 177.679 153.296 184.561 1.00 113.92 ? 135 ASN B OD1 1 
ATOM   9599  N  ND2 . ASN D 2 135 ? 175.687 153.437 185.584 1.00 113.92 ? 135 ASN B ND2 1 
ATOM   9600  N  N   . TRP D 2 136 ? 179.148 155.210 182.294 1.00 113.92 ? 136 TRP B N   1 
ATOM   9601  C  CA  . TRP D 2 136 ? 179.218 154.666 180.945 1.00 113.92 ? 136 TRP B CA  1 
ATOM   9602  C  C   . TRP D 2 136 ? 178.857 153.188 180.879 1.00 113.92 ? 136 TRP B C   1 
ATOM   9603  O  O   . TRP D 2 136 ? 178.604 152.678 179.782 1.00 113.92 ? 136 TRP B O   1 
ATOM   9604  C  CB  . TRP D 2 136 ? 180.617 154.876 180.359 1.00 113.92 ? 136 TRP B CB  1 
ATOM   9605  C  CG  . TRP D 2 136 ? 180.999 156.316 180.240 1.00 113.92 ? 136 TRP B CG  1 
ATOM   9606  C  CD1 . TRP D 2 136 ? 182.073 156.929 180.815 1.00 113.92 ? 136 TRP B CD1 1 
ATOM   9607  C  CD2 . TRP D 2 136 ? 180.296 157.333 179.514 1.00 113.92 ? 136 TRP B CD2 1 
ATOM   9608  N  NE1 . TRP D 2 136 ? 182.088 158.263 180.483 1.00 113.92 ? 136 TRP B NE1 1 
ATOM   9609  C  CE2 . TRP D 2 136 ? 181.008 158.535 179.688 1.00 113.92 ? 136 TRP B CE2 1 
ATOM   9610  C  CE3 . TRP D 2 136 ? 179.138 157.341 178.732 1.00 113.92 ? 136 TRP B CE3 1 
ATOM   9611  C  CZ2 . TRP D 2 136 ? 180.599 159.732 179.108 1.00 113.92 ? 136 TRP B CZ2 1 
ATOM   9612  C  CZ3 . TRP D 2 136 ? 178.733 158.530 178.159 1.00 113.92 ? 136 TRP B CZ3 1 
ATOM   9613  C  CH2 . TRP D 2 136 ? 179.461 159.709 178.350 1.00 113.92 ? 136 TRP B CH2 1 
ATOM   9614  N  N   . ALA D 2 137 ? 178.823 152.493 182.017 1.00 113.92 ? 137 ALA B N   1 
ATOM   9615  C  CA  . ALA D 2 137 ? 178.469 151.080 182.033 1.00 113.92 ? 137 ALA B CA  1 
ATOM   9616  C  C   . ALA D 2 137 ? 176.964 150.850 181.984 1.00 113.92 ? 137 ALA B C   1 
ATOM   9617  O  O   . ALA D 2 137 ? 176.532 149.728 181.699 1.00 113.92 ? 137 ALA B O   1 
ATOM   9618  C  CB  . ALA D 2 137 ? 179.051 150.405 183.276 1.00 113.92 ? 137 ALA B CB  1 
ATOM   9619  N  N   . GLY D 2 138 ? 176.165 151.879 182.248 1.00 113.92 ? 138 GLY B N   1 
ATOM   9620  C  CA  . GLY D 2 138 ? 174.723 151.747 182.233 1.00 113.92 ? 138 GLY B CA  1 
ATOM   9621  C  C   . GLY D 2 138 ? 174.123 151.931 180.856 1.00 113.92 ? 138 GLY B C   1 
ATOM   9622  O  O   . GLY D 2 138 ? 174.592 151.335 179.883 1.00 113.92 ? 138 GLY B O   1 
ATOM   9623  N  N   . GLY D 2 139 ? 173.067 152.736 180.766 1.00 113.92 ? 139 GLY B N   1 
ATOM   9624  C  CA  . GLY D 2 139 ? 172.461 153.030 179.484 1.00 113.92 ? 139 GLY B CA  1 
ATOM   9625  C  C   . GLY D 2 139 ? 171.649 151.905 178.891 1.00 113.92 ? 139 GLY B C   1 
ATOM   9626  O  O   . GLY D 2 139 ? 171.392 151.909 177.685 1.00 113.92 ? 139 GLY B O   1 
ATOM   9627  N  N   . LEU D 2 140 ? 171.233 150.940 179.705 1.00 113.92 ? 140 LEU B N   1 
ATOM   9628  C  CA  . LEU D 2 140 ? 170.421 149.826 179.239 1.00 113.92 ? 140 LEU B CA  1 
ATOM   9629  C  C   . LEU D 2 140 ? 168.950 150.196 179.385 1.00 113.92 ? 140 LEU B C   1 
ATOM   9630  O  O   . LEU D 2 140 ? 168.471 150.416 180.503 1.00 113.92 ? 140 LEU B O   1 
ATOM   9631  C  CB  . LEU D 2 140 ? 170.744 148.555 180.022 1.00 113.92 ? 140 LEU B CB  1 
ATOM   9632  C  CG  . LEU D 2 140 ? 172.213 148.124 180.026 1.00 113.92 ? 140 LEU B CG  1 
ATOM   9633  C  CD1 . LEU D 2 140 ? 172.378 146.800 180.752 1.00 113.92 ? 140 LEU B CD1 1 
ATOM   9634  C  CD2 . LEU D 2 140 ? 172.749 148.031 178.607 1.00 113.92 ? 140 LEU B CD2 1 
ATOM   9635  N  N   . HIS D 2 141 ? 168.239 150.266 178.261 1.00 113.92 ? 141 HIS B N   1 
ATOM   9636  C  CA  . HIS D 2 141 ? 166.878 150.788 178.238 1.00 113.92 ? 141 HIS B CA  1 
ATOM   9637  C  C   . HIS D 2 141 ? 165.848 149.845 177.637 1.00 113.92 ? 141 HIS B C   1 
ATOM   9638  O  O   . HIS D 2 141 ? 164.651 150.061 177.856 1.00 113.92 ? 141 HIS B O   1 
ATOM   9639  C  CB  . HIS D 2 141 ? 166.825 152.124 177.478 1.00 113.92 ? 141 HIS B CB  1 
ATOM   9640  C  CG  . HIS D 2 141 ? 167.283 152.037 176.054 1.00 113.92 ? 141 HIS B CG  1 
ATOM   9641  N  ND1 . HIS D 2 141 ? 167.234 153.113 175.194 1.00 113.92 ? 141 HIS B ND1 1 
ATOM   9642  C  CD2 . HIS D 2 141 ? 167.806 151.011 175.340 1.00 113.92 ? 141 HIS B CD2 1 
ATOM   9643  C  CE1 . HIS D 2 141 ? 167.701 152.753 174.012 1.00 113.92 ? 141 HIS B CE1 1 
ATOM   9644  N  NE2 . HIS D 2 141 ? 168.055 151.482 174.075 1.00 113.92 ? 141 HIS B NE2 1 
ATOM   9645  N  N   . HIS D 2 142 ? 166.259 148.817 176.897 1.00 113.92 ? 142 HIS B N   1 
ATOM   9646  C  CA  . HIS D 2 142 ? 165.309 147.952 176.213 1.00 113.92 ? 142 HIS B CA  1 
ATOM   9647  C  C   . HIS D 2 142 ? 164.706 146.888 177.118 1.00 113.92 ? 142 HIS B C   1 
ATOM   9648  O  O   . HIS D 2 142 ? 163.705 146.276 176.735 1.00 113.92 ? 142 HIS B O   1 
ATOM   9649  C  CB  . HIS D 2 142 ? 165.988 147.276 175.023 1.00 113.92 ? 142 HIS B CB  1 
ATOM   9650  C  CG  . HIS D 2 142 ? 166.214 148.188 173.860 1.00 113.92 ? 142 HIS B CG  1 
ATOM   9651  N  ND1 . HIS D 2 142 ? 167.389 148.196 173.138 1.00 113.92 ? 142 HIS B ND1 1 
ATOM   9652  C  CD2 . HIS D 2 142 ? 165.417 149.121 173.291 1.00 113.92 ? 142 HIS B CD2 1 
ATOM   9653  C  CE1 . HIS D 2 142 ? 167.305 149.096 172.175 1.00 113.92 ? 142 HIS B CE1 1 
ATOM   9654  N  NE2 . HIS D 2 142 ? 166.118 149.672 172.245 1.00 113.92 ? 142 HIS B NE2 1 
ATOM   9655  N  N   . ALA D 2 143 ? 165.276 146.659 178.300 1.00 113.92 ? 143 ALA B N   1 
ATOM   9656  C  CA  . ALA D 2 143 ? 164.751 145.635 179.192 1.00 113.92 ? 143 ALA B CA  1 
ATOM   9657  C  C   . ALA D 2 143 ? 163.319 145.953 179.602 1.00 113.92 ? 143 ALA B C   1 
ATOM   9658  O  O   . ALA D 2 143 ? 162.964 147.111 179.841 1.00 113.92 ? 143 ALA B O   1 
ATOM   9659  C  CB  . ALA D 2 143 ? 165.638 145.508 180.431 1.00 113.92 ? 143 ALA B CB  1 
ATOM   9660  N  N   . LYS D 2 144 ? 162.497 144.913 179.685 1.00 113.92 ? 144 LYS B N   1 
ATOM   9661  C  CA  . LYS D 2 144 ? 161.099 145.044 180.058 1.00 113.92 ? 144 LYS B CA  1 
ATOM   9662  C  C   . LYS D 2 144 ? 160.925 144.691 181.531 1.00 113.92 ? 144 LYS B C   1 
ATOM   9663  O  O   . LYS D 2 144 ? 161.881 144.354 182.233 1.00 113.92 ? 144 LYS B O   1 
ATOM   9664  C  CB  . LYS D 2 144 ? 160.223 144.163 179.166 1.00 103.02 ? 144 LYS B CB  1 
ATOM   9665  C  CG  . LYS D 2 144 ? 160.472 144.353 177.681 1.00 103.02 ? 144 LYS B CG  1 
ATOM   9666  C  CD  . LYS D 2 144 ? 159.960 145.701 177.209 1.00 103.02 ? 144 LYS B CD  1 
ATOM   9667  C  CE  . LYS D 2 144 ? 160.193 145.884 175.719 1.00 103.02 ? 144 LYS B CE  1 
ATOM   9668  N  NZ  . LYS D 2 144 ? 159.707 144.715 174.937 1.00 103.02 ? 144 LYS B NZ  1 
ATOM   9669  N  N   . LYS D 2 145 ? 159.680 144.773 182.007 1.00 113.92 ? 145 LYS B N   1 
ATOM   9670  C  CA  . LYS D 2 145 ? 159.408 144.504 183.416 1.00 113.92 ? 145 LYS B CA  1 
ATOM   9671  C  C   . LYS D 2 145 ? 159.762 143.067 183.777 1.00 113.92 ? 145 LYS B C   1 
ATOM   9672  O  O   . LYS D 2 145 ? 160.406 142.812 184.800 1.00 113.92 ? 145 LYS B O   1 
ATOM   9673  C  CB  . LYS D 2 145 ? 157.938 144.792 183.728 1.00 105.22 ? 145 LYS B CB  1 
ATOM   9674  C  CG  . LYS D 2 145 ? 157.551 144.538 185.176 1.00 105.22 ? 145 LYS B CG  1 
ATOM   9675  C  CD  . LYS D 2 145 ? 156.055 144.705 185.384 1.00 105.22 ? 145 LYS B CD  1 
ATOM   9676  C  CE  . LYS D 2 145 ? 155.715 146.105 185.864 1.00 105.22 ? 145 LYS B CE  1 
ATOM   9677  N  NZ  . LYS D 2 145 ? 156.256 146.373 187.224 1.00 105.22 ? 145 LYS B NZ  1 
ATOM   9678  N  N   . SER D 2 146 ? 159.353 142.115 182.944 1.00 113.92 ? 146 SER B N   1 
ATOM   9679  C  CA  . SER D 2 146 ? 159.575 140.698 183.208 1.00 113.92 ? 146 SER B CA  1 
ATOM   9680  C  C   . SER D 2 146 ? 160.046 139.997 181.937 1.00 113.92 ? 146 SER B C   1 
ATOM   9681  O  O   . SER D 2 146 ? 159.576 138.914 181.586 1.00 113.92 ? 146 SER B O   1 
ATOM   9682  C  CB  . SER D 2 146 ? 158.313 140.044 183.769 1.00 104.75 ? 146 SER B CB  1 
ATOM   9683  O  OG  . SER D 2 146 ? 157.248 140.110 182.838 1.00 104.75 ? 146 SER B OG  1 
ATOM   9684  N  N   . GLU D 2 147 ? 160.989 140.618 181.232 1.00 113.92 ? 147 GLU B N   1 
ATOM   9685  C  CA  . GLU D 2 147 ? 161.513 140.058 179.994 1.00 113.92 ? 147 GLU B CA  1 
ATOM   9686  C  C   . GLU D 2 147 ? 162.791 140.796 179.621 1.00 113.92 ? 147 GLU B C   1 
ATOM   9687  O  O   . GLU D 2 147 ? 162.928 141.993 179.885 1.00 113.92 ? 147 GLU B O   1 
ATOM   9688  C  CB  . GLU D 2 147 ? 160.484 140.163 178.858 1.00 113.10 ? 147 GLU B CB  1 
ATOM   9689  C  CG  . GLU D 2 147 ? 160.981 139.689 177.505 1.00 113.10 ? 147 GLU B CG  1 
ATOM   9690  C  CD  . GLU D 2 147 ? 160.034 140.052 176.380 1.00 113.10 ? 147 GLU B CD  1 
ATOM   9691  O  OE1 . GLU D 2 147 ? 158.812 139.865 176.547 1.00 113.10 ? 147 GLU B OE1 1 
ATOM   9692  O  OE2 . GLU D 2 147 ? 160.514 140.524 175.328 1.00 113.10 ? 147 GLU B OE2 1 
ATOM   9693  N  N   . ALA D 2 148 ? 163.719 140.067 179.008 1.00 113.92 ? 148 ALA B N   1 
ATOM   9694  C  CA  . ALA D 2 148 ? 164.935 140.651 178.459 1.00 113.92 ? 148 ALA B CA  1 
ATOM   9695  C  C   . ALA D 2 148 ? 164.731 140.960 176.982 1.00 113.92 ? 148 ALA B C   1 
ATOM   9696  O  O   . ALA D 2 148 ? 164.435 140.059 176.190 1.00 113.92 ? 148 ALA B O   1 
ATOM   9697  C  CB  . ALA D 2 148 ? 166.126 139.716 178.648 1.00 113.92 ? 148 ALA B CB  1 
ATOM   9698  N  N   . SER D 2 149 ? 164.886 142.226 176.614 1.00 117.52 ? 149 SER B N   1 
ATOM   9699  C  CA  . SER D 2 149 ? 164.726 142.665 175.238 1.00 117.52 ? 149 SER B CA  1 
ATOM   9700  C  C   . SER D 2 149 ? 166.021 143.317 174.775 1.00 117.52 ? 149 SER B C   1 
ATOM   9701  O  O   . SER D 2 149 ? 166.725 143.959 175.560 1.00 117.52 ? 149 SER B O   1 
ATOM   9702  C  CB  . SER D 2 149 ? 163.558 143.644 175.085 1.00 117.52 ? 149 SER B CB  1 
ATOM   9703  N  N   . GLY D 2 150 ? 166.326 143.149 173.494 1.00 121.58 ? 150 GLY B N   1 
ATOM   9704  C  CA  . GLY D 2 150 ? 167.572 143.689 172.974 1.00 121.58 ? 150 GLY B CA  1 
ATOM   9705  C  C   . GLY D 2 150 ? 168.762 143.023 173.632 1.00 121.58 ? 150 GLY B C   1 
ATOM   9706  O  O   . GLY D 2 150 ? 168.896 141.795 173.629 1.00 121.58 ? 150 GLY B O   1 
ATOM   9707  N  N   . PHE D 2 151 ? 169.641 143.835 174.211 1.00 113.92 ? 151 PHE B N   1 
ATOM   9708  C  CA  . PHE D 2 151 ? 170.821 143.356 174.918 1.00 113.92 ? 151 PHE B CA  1 
ATOM   9709  C  C   . PHE D 2 151 ? 170.784 143.772 176.384 1.00 113.92 ? 151 PHE B C   1 
ATOM   9710  O  O   . PHE D 2 151 ? 171.815 144.066 176.991 1.00 113.92 ? 151 PHE B O   1 
ATOM   9711  C  CB  . PHE D 2 151 ? 172.102 143.864 174.259 1.00 113.92 ? 151 PHE B CB  1 
ATOM   9712  C  CG  . PHE D 2 151 ? 172.189 143.584 172.782 1.00 113.92 ? 151 PHE B CG  1 
ATOM   9713  C  CD1 . PHE D 2 151 ? 171.616 142.448 172.236 1.00 113.92 ? 151 PHE B CD1 1 
ATOM   9714  C  CD2 . PHE D 2 151 ? 172.840 144.467 171.938 1.00 113.92 ? 151 PHE B CD2 1 
ATOM   9715  C  CE1 . PHE D 2 151 ? 171.696 142.197 170.880 1.00 113.92 ? 151 PHE B CE1 1 
ATOM   9716  C  CE2 . PHE D 2 151 ? 172.921 144.221 170.582 1.00 113.92 ? 151 PHE B CE2 1 
ATOM   9717  C  CZ  . PHE D 2 151 ? 172.349 143.084 170.053 1.00 113.92 ? 151 PHE B CZ  1 
ATOM   9718  N  N   . CYS D 2 152 ? 169.590 143.801 176.973 1.00 117.59 ? 152 CYS B N   1 
ATOM   9719  C  CA  . CYS D 2 152 ? 169.406 144.326 178.317 1.00 117.59 ? 152 CYS B CA  1 
ATOM   9720  C  C   . CYS D 2 152 ? 168.609 143.341 179.159 1.00 117.59 ? 152 CYS B C   1 
ATOM   9721  O  O   . CYS D 2 152 ? 167.713 142.654 178.662 1.00 117.59 ? 152 CYS B O   1 
ATOM   9722  C  CB  . CYS D 2 152 ? 168.690 145.684 178.293 1.00 117.59 ? 152 CYS B CB  1 
ATOM   9723  S  SG  . CYS D 2 152 ? 169.381 146.874 177.120 1.00 117.59 ? 152 CYS B SG  1 
ATOM   9724  N  N   . TYR D 2 153 ? 168.952 143.283 180.444 1.00 123.00 ? 153 TYR B N   1 
ATOM   9725  C  CA  . TYR D 2 153 ? 168.287 142.419 181.410 1.00 123.00 ? 153 TYR B CA  1 
ATOM   9726  C  C   . TYR D 2 153 ? 167.619 143.206 182.522 1.00 123.00 ? 153 TYR B C   1 
ATOM   9727  O  O   . TYR D 2 153 ? 166.422 143.030 182.775 1.00 123.00 ? 153 TYR B O   1 
ATOM   9728  C  CB  . TYR D 2 153 ? 169.288 141.420 182.016 1.00 123.00 ? 153 TYR B CB  1 
ATOM   9729  C  CG  . TYR D 2 153 ? 170.264 140.839 181.024 1.00 123.00 ? 153 TYR B CG  1 
ATOM   9730  C  CD1 . TYR D 2 153 ? 171.409 141.534 180.653 1.00 123.00 ? 153 TYR B CD1 1 
ATOM   9731  C  CD2 . TYR D 2 153 ? 170.040 139.594 180.457 1.00 123.00 ? 153 TYR B CD2 1 
ATOM   9732  C  CE1 . TYR D 2 153 ? 172.297 141.007 179.742 1.00 123.00 ? 153 TYR B CE1 1 
ATOM   9733  C  CE2 . TYR D 2 153 ? 170.924 139.058 179.550 1.00 123.00 ? 153 TYR B CE2 1 
ATOM   9734  C  CZ  . TYR D 2 153 ? 172.053 139.765 179.199 1.00 123.00 ? 153 TYR B CZ  1 
ATOM   9735  O  OH  . TYR D 2 153 ? 172.935 139.227 178.290 1.00 123.00 ? 153 TYR B OH  1 
ATOM   9736  N  N   . VAL D 2 154 ? 168.367 144.074 183.196 1.00 113.64 ? 154 VAL B N   1 
ATOM   9737  C  CA  . VAL D 2 154 ? 167.843 144.951 184.233 1.00 113.64 ? 154 VAL B CA  1 
ATOM   9738  C  C   . VAL D 2 154 ? 167.906 146.377 183.712 1.00 113.64 ? 154 VAL B C   1 
ATOM   9739  O  O   . VAL D 2 154 ? 168.963 146.833 183.258 1.00 113.64 ? 154 VAL B O   1 
ATOM   9740  C  CB  . VAL D 2 154 ? 168.631 144.809 185.546 1.00 113.64 ? 154 VAL B CB  1 
ATOM   9741  C  CG1 . VAL D 2 154 ? 167.799 145.300 186.720 1.00 113.64 ? 154 VAL B CG1 1 
ATOM   9742  C  CG2 . VAL D 2 154 ? 169.057 143.365 185.755 1.00 113.64 ? 154 VAL B CG2 1 
ATOM   9743  N  N   . ASN D 2 155 ? 166.779 147.079 183.775 1.00 113.92 ? 155 ASN B N   1 
ATOM   9744  C  CA  . ASN D 2 155 ? 166.679 148.415 183.197 1.00 113.92 ? 155 ASN B CA  1 
ATOM   9745  C  C   . ASN D 2 155 ? 167.217 149.402 184.221 1.00 113.92 ? 155 ASN B C   1 
ATOM   9746  O  O   . ASN D 2 155 ? 166.493 149.857 185.107 1.00 113.92 ? 155 ASN B O   1 
ATOM   9747  C  CB  . ASN D 2 155 ? 165.238 148.729 182.814 1.00 110.05 ? 155 ASN B CB  1 
ATOM   9748  C  CG  . ASN D 2 155 ? 165.140 149.714 181.668 1.00 110.05 ? 155 ASN B CG  1 
ATOM   9749  O  OD1 . ASN D 2 155 ? 165.941 150.642 181.562 1.00 110.05 ? 155 ASN B OD1 1 
ATOM   9750  N  ND2 . ASN D 2 155 ? 164.154 149.520 180.802 1.00 110.05 ? 155 ASN B ND2 1 
ATOM   9751  N  N   . ASP D 2 156 ? 168.499 149.743 184.087 1.00 123.25 ? 156 ASP B N   1 
ATOM   9752  C  CA  . ASP D 2 156 ? 169.119 150.684 185.013 1.00 123.25 ? 156 ASP B CA  1 
ATOM   9753  C  C   . ASP D 2 156 ? 168.505 152.074 184.909 1.00 123.25 ? 156 ASP B C   1 
ATOM   9754  O  O   . ASP D 2 156 ? 168.419 152.787 185.917 1.00 123.25 ? 156 ASP B O   1 
ATOM   9755  C  CB  . ASP D 2 156 ? 170.627 150.724 184.758 1.00 123.25 ? 156 ASP B CB  1 
ATOM   9756  C  CG  . ASP D 2 156 ? 171.013 151.725 183.684 1.00 123.25 ? 156 ASP B CG  1 
ATOM   9757  O  OD1 . ASP D 2 156 ? 170.381 151.711 182.608 1.00 123.25 ? 156 ASP B OD1 1 
ATOM   9758  O  OD2 . ASP D 2 156 ? 171.952 152.516 183.904 1.00 123.25 ? 156 ASP B OD2 1 
ATOM   9759  N  N   . ILE D 2 157 ? 168.056 152.465 183.716 1.00 113.92 ? 157 ILE B N   1 
ATOM   9760  C  CA  . ILE D 2 157 ? 167.462 153.787 183.543 1.00 113.92 ? 157 ILE B CA  1 
ATOM   9761  C  C   . ILE D 2 157 ? 166.178 153.903 184.349 1.00 113.92 ? 157 ILE B C   1 
ATOM   9762  O  O   . ILE D 2 157 ? 165.940 154.907 185.030 1.00 113.92 ? 157 ILE B O   1 
ATOM   9763  C  CB  . ILE D 2 157 ? 167.207 154.075 182.054 1.00 113.92 ? 157 ILE B CB  1 
ATOM   9764  C  CG1 . ILE D 2 157 ? 168.471 153.831 181.237 1.00 113.92 ? 157 ILE B CG1 1 
ATOM   9765  C  CG2 . ILE D 2 157 ? 166.746 155.506 181.881 1.00 113.92 ? 157 ILE B CG2 1 
ATOM   9766  C  CD1 . ILE D 2 157 ? 168.345 154.279 179.815 1.00 113.92 ? 157 ILE B CD1 1 
ATOM   9767  N  N   . VAL D 2 158 ? 165.317 152.887 184.264 1.00 113.92 ? 158 VAL B N   1 
ATOM   9768  C  CA  . VAL D 2 158 ? 164.039 152.941 184.963 1.00 113.92 ? 158 VAL B CA  1 
ATOM   9769  C  C   . VAL D 2 158 ? 164.248 152.919 186.472 1.00 113.92 ? 158 VAL B C   1 
ATOM   9770  O  O   . VAL D 2 158 ? 163.581 153.652 187.212 1.00 113.92 ? 158 VAL B O   1 
ATOM   9771  C  CB  . VAL D 2 158 ? 163.130 151.792 184.492 1.00 113.92 ? 158 VAL B CB  1 
ATOM   9772  C  CG1 . VAL D 2 158 ? 161.819 151.801 185.253 1.00 113.92 ? 158 VAL B CG1 1 
ATOM   9773  C  CG2 . VAL D 2 158 ? 162.874 151.905 183.000 1.00 113.92 ? 158 VAL B CG2 1 
ATOM   9774  N  N   . LEU D 2 159 ? 165.183 152.096 186.953 1.00 113.92 ? 159 LEU B N   1 
ATOM   9775  C  CA  . LEU D 2 159 ? 165.486 152.091 188.381 1.00 113.92 ? 159 LEU B CA  1 
ATOM   9776  C  C   . LEU D 2 159 ? 165.998 153.450 188.837 1.00 113.92 ? 159 LEU B C   1 
ATOM   9777  O  O   . LEU D 2 159 ? 165.593 153.952 189.893 1.00 113.92 ? 159 LEU B O   1 
ATOM   9778  C  CB  . LEU D 2 159 ? 166.498 150.994 188.711 1.00 113.92 ? 159 LEU B CB  1 
ATOM   9779  C  CG  . LEU D 2 159 ? 165.939 149.613 189.069 1.00 113.92 ? 159 LEU B CG  1 
ATOM   9780  C  CD1 . LEU D 2 159 ? 165.359 148.902 187.859 1.00 113.92 ? 159 LEU B CD1 1 
ATOM   9781  C  CD2 . LEU D 2 159 ? 167.013 148.759 189.730 1.00 113.92 ? 159 LEU B CD2 1 
ATOM   9782  N  N   . ALA D 2 160 ? 166.880 154.068 188.049 1.00 114.52 ? 160 ALA B N   1 
ATOM   9783  C  CA  . ALA D 2 160 ? 167.396 155.381 188.417 1.00 114.52 ? 160 ALA B CA  1 
ATOM   9784  C  C   . ALA D 2 160 ? 166.295 156.432 188.420 1.00 114.52 ? 160 ALA B C   1 
ATOM   9785  O  O   . ALA D 2 160 ? 166.254 157.294 189.304 1.00 114.52 ? 160 ALA B O   1 
ATOM   9786  C  CB  . ALA D 2 160 ? 168.524 155.787 187.469 1.00 114.52 ? 160 ALA B CB  1 
ATOM   9787  N  N   . ILE D 2 161 ? 165.394 156.387 187.436 1.00 113.92 ? 161 ILE B N   1 
ATOM   9788  C  CA  . ILE D 2 161 ? 164.297 157.352 187.391 1.00 113.92 ? 161 ILE B CA  1 
ATOM   9789  C  C   . ILE D 2 161 ? 163.378 157.185 188.598 1.00 113.92 ? 161 ILE B C   1 
ATOM   9790  O  O   . ILE D 2 161 ? 162.985 158.170 189.234 1.00 113.92 ? 161 ILE B O   1 
ATOM   9791  C  CB  . ILE D 2 161 ? 163.527 157.238 186.064 1.00 113.92 ? 161 ILE B CB  1 
ATOM   9792  C  CG1 . ILE D 2 161 ? 164.407 157.711 184.909 1.00 113.92 ? 161 ILE B CG1 1 
ATOM   9793  C  CG2 . ILE D 2 161 ? 162.279 158.096 186.111 1.00 113.92 ? 161 ILE B CG2 1 
ATOM   9794  C  CD1 . ILE D 2 161 ? 163.744 157.622 183.557 1.00 113.92 ? 161 ILE B CD1 1 
ATOM   9795  N  N   . LEU D 2 162 ? 163.021 155.939 188.933 1.00 113.92 ? 162 LEU B N   1 
ATOM   9796  C  CA  . LEU D 2 162 ? 162.209 155.711 190.130 1.00 113.92 ? 162 LEU B CA  1 
ATOM   9797  C  C   . LEU D 2 162 ? 162.913 156.214 191.380 1.00 113.92 ? 162 LEU B C   1 
ATOM   9798  O  O   . LEU D 2 162 ? 162.285 156.833 192.248 1.00 113.92 ? 162 LEU B O   1 
ATOM   9799  C  CB  . LEU D 2 162 ? 161.857 154.230 190.289 1.00 113.92 ? 162 LEU B CB  1 
ATOM   9800  C  CG  . LEU D 2 162 ? 160.577 153.677 189.653 1.00 113.92 ? 162 LEU B CG  1 
ATOM   9801  C  CD1 . LEU D 2 162 ? 160.667 153.581 188.153 1.00 113.92 ? 162 LEU B CD1 1 
ATOM   9802  C  CD2 . LEU D 2 162 ? 160.235 152.322 190.258 1.00 113.92 ? 162 LEU B CD2 1 
ATOM   9803  N  N   . GLU D 2 163 ? 164.214 155.955 191.495 1.00 118.93 ? 163 GLU B N   1 
ATOM   9804  C  CA  . GLU D 2 163 ? 164.973 156.432 192.641 1.00 118.93 ? 163 GLU B CA  1 
ATOM   9805  C  C   . GLU D 2 163 ? 165.066 157.952 192.661 1.00 118.93 ? 163 GLU B C   1 
ATOM   9806  O  O   . GLU D 2 163 ? 165.247 158.543 193.730 1.00 118.93 ? 163 GLU B O   1 
ATOM   9807  C  CB  . GLU D 2 163 ? 166.359 155.790 192.619 1.00 118.93 ? 163 GLU B CB  1 
ATOM   9808  C  CG  . GLU D 2 163 ? 167.216 156.031 193.838 1.00 118.93 ? 163 GLU B CG  1 
ATOM   9809  C  CD  . GLU D 2 163 ? 168.122 154.850 194.116 1.00 118.93 ? 163 GLU B CD  1 
ATOM   9810  O  OE1 . GLU D 2 163 ? 167.657 153.700 193.963 1.00 118.93 ? 163 GLU B OE1 1 
ATOM   9811  O  OE2 . GLU D 2 163 ? 169.295 155.061 194.471 1.00 118.93 ? 163 GLU B OE2 1 
ATOM   9812  N  N   . LEU D 2 164 ? 164.941 158.592 191.496 1.00 113.92 ? 164 LEU B N   1 
ATOM   9813  C  CA  . LEU D 2 164 ? 164.968 160.047 191.412 1.00 113.92 ? 164 LEU B CA  1 
ATOM   9814  C  C   . LEU D 2 164 ? 163.624 160.656 191.799 1.00 113.92 ? 164 LEU B C   1 
ATOM   9815  O  O   . LEU D 2 164 ? 163.584 161.733 192.403 1.00 113.92 ? 164 LEU B O   1 
ATOM   9816  C  CB  . LEU D 2 164 ? 165.366 160.485 190.004 1.00 113.92 ? 164 LEU B CB  1 
ATOM   9817  C  CG  . LEU D 2 164 ? 166.841 160.850 189.855 1.00 113.92 ? 164 LEU B CG  1 
ATOM   9818  C  CD1 . LEU D 2 164 ? 167.190 161.122 188.404 1.00 113.92 ? 164 LEU B CD1 1 
ATOM   9819  C  CD2 . LEU D 2 164 ? 167.164 162.048 190.723 1.00 113.92 ? 164 LEU B CD2 1 
ATOM   9820  N  N   . LEU D 2 165 ? 162.518 159.990 191.448 1.00 113.92 ? 165 LEU B N   1 
ATOM   9821  C  CA  . LEU D 2 165 ? 161.196 160.551 191.713 1.00 113.92 ? 165 LEU B CA  1 
ATOM   9822  C  C   . LEU D 2 165 ? 160.953 160.771 193.198 1.00 113.92 ? 165 LEU B C   1 
ATOM   9823  O  O   . LEU D 2 165 ? 160.056 161.537 193.562 1.00 113.92 ? 165 LEU B O   1 
ATOM   9824  C  CB  . LEU D 2 165 ? 160.097 159.641 191.157 1.00 113.92 ? 165 LEU B CB  1 
ATOM   9825  C  CG  . LEU D 2 165 ? 160.109 159.285 189.673 1.00 113.92 ? 165 LEU B CG  1 
ATOM   9826  C  CD1 . LEU D 2 165 ? 158.726 158.852 189.219 1.00 113.92 ? 165 LEU B CD1 1 
ATOM   9827  C  CD2 . LEU D 2 165 ? 160.592 160.465 188.863 1.00 113.92 ? 165 LEU B CD2 1 
ATOM   9828  N  N   . LYS D 2 166 ? 161.722 160.105 194.059 1.00 128.08 ? 166 LYS B N   1 
ATOM   9829  C  CA  . LYS D 2 166 ? 161.549 160.280 195.494 1.00 128.08 ? 166 LYS B CA  1 
ATOM   9830  C  C   . LYS D 2 166 ? 161.886 161.705 195.912 1.00 128.08 ? 166 LYS B C   1 
ATOM   9831  O  O   . LYS D 2 166 ? 161.247 162.267 196.810 1.00 128.08 ? 166 LYS B O   1 
ATOM   9832  C  CB  . LYS D 2 166 ? 162.419 159.274 196.245 1.00 128.08 ? 166 LYS B CB  1 
ATOM   9833  C  CG  . LYS D 2 166 ? 162.418 157.888 195.623 1.00 128.08 ? 166 LYS B CG  1 
ATOM   9834  C  CD  . LYS D 2 166 ? 162.849 156.828 196.620 1.00 128.08 ? 166 LYS B CD  1 
ATOM   9835  C  CE  . LYS D 2 166 ? 164.276 157.064 197.085 1.00 128.08 ? 166 LYS B CE  1 
ATOM   9836  N  NZ  . LYS D 2 166 ? 164.768 155.954 197.945 1.00 128.08 ? 166 LYS B NZ  1 
ATOM   9837  N  N   . TYR D 2 167 ? 162.886 162.308 195.268 1.00 127.22 ? 167 TYR B N   1 
ATOM   9838  C  CA  . TYR D 2 167 ? 163.347 163.643 195.621 1.00 127.22 ? 167 TYR B CA  1 
ATOM   9839  C  C   . TYR D 2 167 ? 162.836 164.731 194.683 1.00 127.22 ? 167 TYR B C   1 
ATOM   9840  O  O   . TYR D 2 167 ? 162.932 165.913 195.027 1.00 127.22 ? 167 TYR B O   1 
ATOM   9841  C  CB  . TYR D 2 167 ? 164.882 163.682 195.644 1.00 127.22 ? 167 TYR B CB  1 
ATOM   9842  C  CG  . TYR D 2 167 ? 165.515 163.054 196.869 1.00 127.22 ? 167 TYR B CG  1 
ATOM   9843  C  CD1 . TYR D 2 167 ? 165.074 161.832 197.361 1.00 127.22 ? 167 TYR B CD1 1 
ATOM   9844  C  CD2 . TYR D 2 167 ? 166.563 163.683 197.530 1.00 127.22 ? 167 TYR B CD2 1 
ATOM   9845  C  CE1 . TYR D 2 167 ? 165.652 161.256 198.475 1.00 127.22 ? 167 TYR B CE1 1 
ATOM   9846  C  CE2 . TYR D 2 167 ? 167.149 163.114 198.646 1.00 127.22 ? 167 TYR B CE2 1 
ATOM   9847  C  CZ  . TYR D 2 167 ? 166.689 161.901 199.114 1.00 127.22 ? 167 TYR B CZ  1 
ATOM   9848  O  OH  . TYR D 2 167 ? 167.270 161.331 200.224 1.00 127.22 ? 167 TYR B OH  1 
ATOM   9849  N  N   . HIS D 2 168 ? 162.301 164.371 193.515 1.00 117.88 ? 168 HIS B N   1 
ATOM   9850  C  CA  . HIS D 2 168 ? 161.864 165.346 192.528 1.00 117.88 ? 168 HIS B CA  1 
ATOM   9851  C  C   . HIS D 2 168 ? 160.446 165.039 192.069 1.00 117.88 ? 168 HIS B C   1 
ATOM   9852  O  O   . HIS D 2 168 ? 160.026 163.879 192.025 1.00 117.88 ? 168 HIS B O   1 
ATOM   9853  C  CB  . HIS D 2 168 ? 162.806 165.380 191.317 1.00 117.88 ? 168 HIS B CB  1 
ATOM   9854  C  CG  . HIS D 2 168 ? 164.240 165.610 191.677 1.00 117.88 ? 168 HIS B CG  1 
ATOM   9855  N  ND1 . HIS D 2 168 ? 164.739 166.856 191.991 1.00 117.88 ? 168 HIS B ND1 1 
ATOM   9856  C  CD2 . HIS D 2 168 ? 165.283 164.753 191.777 1.00 117.88 ? 168 HIS B CD2 1 
ATOM   9857  C  CE1 . HIS D 2 168 ? 166.027 166.757 192.265 1.00 117.88 ? 168 HIS B CE1 1 
ATOM   9858  N  NE2 . HIS D 2 168 ? 166.382 165.491 192.143 1.00 117.88 ? 168 HIS B NE2 1 
ATOM   9859  N  N   . GLN D 2 169 ? 159.710 166.097 191.725 1.00 123.28 ? 169 GLN B N   1 
ATOM   9860  C  CA  . GLN D 2 169 ? 158.333 165.950 191.263 1.00 123.28 ? 169 GLN B CA  1 
ATOM   9861  C  C   . GLN D 2 169 ? 158.263 165.560 189.788 1.00 123.28 ? 169 GLN B C   1 
ATOM   9862  O  O   . GLN D 2 169 ? 157.704 164.516 189.436 1.00 123.28 ? 169 GLN B O   1 
ATOM   9863  C  CB  . GLN D 2 169 ? 157.560 167.250 191.510 1.00 123.28 ? 169 GLN B CB  1 
ATOM   9864  C  CG  . GLN D 2 169 ? 156.149 167.262 190.942 1.00 123.28 ? 169 GLN B CG  1 
ATOM   9865  C  CD  . GLN D 2 169 ? 155.323 166.068 191.378 1.00 123.28 ? 169 GLN B CD  1 
ATOM   9866  O  OE1 . GLN D 2 169 ? 155.409 165.622 192.524 1.00 123.28 ? 169 GLN B OE1 1 
ATOM   9867  N  NE2 . GLN D 2 169 ? 154.515 165.543 190.465 1.00 123.28 ? 169 GLN B NE2 1 
ATOM   9868  N  N   . ARG D 2 170 ? 158.826 166.391 188.916 1.00 114.04 ? 170 ARG B N   1 
ATOM   9869  C  CA  . ARG D 2 170 ? 158.813 166.171 187.475 1.00 114.04 ? 170 ARG B CA  1 
ATOM   9870  C  C   . ARG D 2 170 ? 160.211 165.802 186.999 1.00 114.04 ? 170 ARG B C   1 
ATOM   9871  O  O   . ARG D 2 170 ? 161.186 166.475 187.348 1.00 114.04 ? 170 ARG B O   1 
ATOM   9872  C  CB  . ARG D 2 170 ? 158.307 167.416 186.747 1.00 114.04 ? 170 ARG B CB  1 
ATOM   9873  C  CG  . ARG D 2 170 ? 156.844 167.727 187.026 1.00 114.04 ? 170 ARG B CG  1 
ATOM   9874  C  CD  . ARG D 2 170 ? 156.406 169.013 186.350 1.00 114.04 ? 170 ARG B CD  1 
ATOM   9875  N  NE  . ARG D 2 170 ? 157.150 170.170 186.833 1.00 114.04 ? 170 ARG B NE  1 
ATOM   9876  C  CZ  . ARG D 2 170 ? 156.849 170.849 187.931 1.00 114.04 ? 170 ARG B CZ  1 
ATOM   9877  N  NH1 . ARG D 2 170 ? 155.820 170.513 188.691 1.00 114.04 ? 170 ARG B NH1 1 
ATOM   9878  N  NH2 . ARG D 2 170 ? 157.601 171.891 188.275 1.00 114.04 ? 170 ARG B NH2 1 
ATOM   9879  N  N   . VAL D 2 171 ? 160.307 164.735 186.205 1.00 113.92 ? 171 VAL B N   1 
ATOM   9880  C  CA  . VAL D 2 171 ? 161.588 164.247 185.702 1.00 113.92 ? 171 VAL B CA  1 
ATOM   9881  C  C   . VAL D 2 171 ? 161.526 164.079 184.188 1.00 113.92 ? 171 VAL B C   1 
ATOM   9882  O  O   . VAL D 2 171 ? 160.662 163.358 183.664 1.00 113.92 ? 171 VAL B O   1 
ATOM   9883  C  CB  . VAL D 2 171 ? 162.005 162.930 186.375 1.00 113.92 ? 171 VAL B CB  1 
ATOM   9884  C  CG1 . VAL D 2 171 ? 163.040 162.206 185.529 1.00 113.92 ? 171 VAL B CG1 1 
ATOM   9885  C  CG2 . VAL D 2 171 ? 162.567 163.212 187.758 1.00 113.92 ? 171 VAL B CG2 1 
ATOM   9886  N  N   . LEU D 2 172 ? 162.395 164.803 183.489 1.00 113.92 ? 172 LEU B N   1 
ATOM   9887  C  CA  . LEU D 2 172 ? 162.537 164.686 182.047 1.00 113.92 ? 172 LEU B CA  1 
ATOM   9888  C  C   . LEU D 2 172 ? 163.619 163.661 181.730 1.00 113.92 ? 172 LEU B C   1 
ATOM   9889  O  O   . LEU D 2 172 ? 164.720 163.720 182.288 1.00 113.92 ? 172 LEU B O   1 
ATOM   9890  C  CB  . LEU D 2 172 ? 162.893 166.040 181.432 1.00 113.92 ? 172 LEU B CB  1 
ATOM   9891  C  CG  . LEU D 2 172 ? 163.432 166.024 180.002 1.00 113.92 ? 172 LEU B CG  1 
ATOM   9892  C  CD1 . LEU D 2 172 ? 162.399 165.448 179.057 1.00 113.92 ? 172 LEU B CD1 1 
ATOM   9893  C  CD2 . LEU D 2 172 ? 163.845 167.419 179.565 1.00 113.92 ? 172 LEU B CD2 1 
ATOM   9894  N  N   . TYR D 2 173 ? 163.305 162.724 180.845 1.00 113.92 ? 173 TYR B N   1 
ATOM   9895  C  CA  . TYR D 2 173 ? 164.249 161.713 180.385 1.00 113.92 ? 173 TYR B CA  1 
ATOM   9896  C  C   . TYR D 2 173 ? 164.501 161.936 178.900 1.00 113.92 ? 173 TYR B C   1 
ATOM   9897  O  O   . TYR D 2 173 ? 163.592 161.772 178.082 1.00 113.92 ? 173 TYR B O   1 
ATOM   9898  C  CB  . TYR D 2 173 ? 163.721 160.303 180.646 1.00 113.92 ? 173 TYR B CB  1 
ATOM   9899  C  CG  . TYR D 2 173 ? 164.389 159.244 179.796 1.00 113.92 ? 173 TYR B CG  1 
ATOM   9900  C  CD1 . TYR D 2 173 ? 165.645 158.753 180.120 1.00 113.92 ? 173 TYR B CD1 1 
ATOM   9901  C  CD2 . TYR D 2 173 ? 163.754 158.728 178.674 1.00 113.92 ? 173 TYR B CD2 1 
ATOM   9902  C  CE1 . TYR D 2 173 ? 166.254 157.787 179.343 1.00 113.92 ? 173 TYR B CE1 1 
ATOM   9903  C  CE2 . TYR D 2 173 ? 164.354 157.763 177.894 1.00 113.92 ? 173 TYR B CE2 1 
ATOM   9904  C  CZ  . TYR D 2 173 ? 165.603 157.294 178.234 1.00 113.92 ? 173 TYR B CZ  1 
ATOM   9905  O  OH  . TYR D 2 173 ? 166.204 156.331 177.458 1.00 113.92 ? 173 TYR B OH  1 
ATOM   9906  N  N   . ILE D 2 174 ? 165.731 162.292 178.550 1.00 113.92 ? 174 ILE B N   1 
ATOM   9907  C  CA  . ILE D 2 174 ? 166.118 162.486 177.160 1.00 113.92 ? 174 ILE B CA  1 
ATOM   9908  C  C   . ILE D 2 174 ? 166.896 161.258 176.717 1.00 113.92 ? 174 ILE B C   1 
ATOM   9909  O  O   . ILE D 2 174 ? 167.858 160.849 177.380 1.00 113.92 ? 174 ILE B O   1 
ATOM   9910  C  CB  . ILE D 2 174 ? 166.951 163.764 176.974 1.00 113.92 ? 174 ILE B CB  1 
ATOM   9911  C  CG1 . ILE D 2 174 ? 166.366 164.917 177.787 1.00 113.92 ? 174 ILE B CG1 1 
ATOM   9912  C  CG2 . ILE D 2 174 ? 167.022 164.141 175.503 1.00 113.92 ? 174 ILE B CG2 1 
ATOM   9913  C  CD1 . ILE D 2 174 ? 167.208 166.173 177.736 1.00 113.92 ? 174 ILE B CD1 1 
ATOM   9914  N  N   . ASP D 2 175 ? 166.469 160.661 175.612 1.00 113.92 ? 175 ASP B N   1 
ATOM   9915  C  CA  . ASP D 2 175 ? 167.092 159.461 175.061 1.00 113.92 ? 175 ASP B CA  1 
ATOM   9916  C  C   . ASP D 2 175 ? 167.799 159.868 173.772 1.00 113.92 ? 175 ASP B C   1 
ATOM   9917  O  O   . ASP D 2 175 ? 167.195 159.872 172.696 1.00 113.92 ? 175 ASP B O   1 
ATOM   9918  C  CB  . ASP D 2 175 ? 166.057 158.366 174.814 1.00 113.92 ? 175 ASP B CB  1 
ATOM   9919  C  CG  . ASP D 2 175 ? 166.671 157.093 174.267 1.00 113.92 ? 175 ASP B CG  1 
ATOM   9920  O  OD1 . ASP D 2 175 ? 167.219 156.305 175.066 1.00 113.92 ? 175 ASP B OD1 1 
ATOM   9921  O  OD2 . ASP D 2 175 ? 166.604 156.879 173.038 1.00 113.92 ? 175 ASP B OD2 1 
ATOM   9922  N  N   . ILE D 2 176 ? 169.069 160.255 173.900 1.00 113.92 ? 176 ILE B N   1 
ATOM   9923  C  CA  . ILE D 2 176 ? 169.957 160.452 172.758 1.00 113.92 ? 176 ILE B CA  1 
ATOM   9924  C  C   . ILE D 2 176 ? 170.468 159.069 172.368 1.00 113.92 ? 176 ILE B C   1 
ATOM   9925  O  O   . ILE D 2 176 ? 171.311 158.493 173.053 1.00 113.92 ? 176 ILE B O   1 
ATOM   9926  C  CB  . ILE D 2 176 ? 171.104 161.412 173.078 1.00 113.92 ? 176 ILE B CB  1 
ATOM   9927  C  CG1 . ILE D 2 176 ? 170.601 162.850 173.090 1.00 113.92 ? 176 ILE B CG1 1 
ATOM   9928  C  CG2 . ILE D 2 176 ? 172.221 161.278 172.054 1.00 113.92 ? 176 ILE B CG2 1 
ATOM   9929  C  CD1 . ILE D 2 176 ? 171.561 163.800 173.730 1.00 113.92 ? 176 ILE B CD1 1 
ATOM   9930  N  N   . ASP D 2 177 ? 169.952 158.529 171.276 1.00 113.92 ? 177 ASP B N   1 
ATOM   9931  C  CA  . ASP D 2 177 ? 170.277 157.171 170.859 1.00 113.92 ? 177 ASP B CA  1 
ATOM   9932  C  C   . ASP D 2 177 ? 169.722 156.982 169.458 1.00 113.92 ? 177 ASP B C   1 
ATOM   9933  O  O   . ASP D 2 177 ? 169.097 157.882 168.888 1.00 113.92 ? 177 ASP B O   1 
ATOM   9934  C  CB  . ASP D 2 177 ? 169.704 156.136 171.831 1.00 113.92 ? 177 ASP B CB  1 
ATOM   9935  C  CG  . ASP D 2 177 ? 170.526 154.866 171.885 1.00 113.92 ? 177 ASP B CG  1 
ATOM   9936  O  OD1 . ASP D 2 177 ? 171.092 154.480 170.843 1.00 113.92 ? 177 ASP B OD1 1 
ATOM   9937  O  OD2 . ASP D 2 177 ? 170.603 154.251 172.971 1.00 113.92 ? 177 ASP B OD2 1 
ATOM   9938  N  N   . ILE D 2 178 ? 169.975 155.805 168.892 1.00 113.92 ? 178 ILE B N   1 
ATOM   9939  C  CA  . ILE D 2 178 ? 169.374 155.442 167.618 1.00 113.92 ? 178 ILE B CA  1 
ATOM   9940  C  C   . ILE D 2 178 ? 168.249 154.431 167.796 1.00 113.92 ? 178 ILE B C   1 
ATOM   9941  O  O   . ILE D 2 178 ? 167.466 154.217 166.857 1.00 113.92 ? 178 ILE B O   1 
ATOM   9942  C  CB  . ILE D 2 178 ? 170.452 154.925 166.641 1.00 113.92 ? 178 ILE B CB  1 
ATOM   9943  C  CG1 . ILE D 2 178 ? 169.922 154.886 165.209 1.00 113.92 ? 178 ILE B CG1 1 
ATOM   9944  C  CG2 . ILE D 2 178 ? 170.951 153.556 167.074 1.00 113.92 ? 178 ILE B CG2 1 
ATOM   9945  C  CD1 . ILE D 2 178 ? 170.993 154.638 164.192 1.00 113.92 ? 178 ILE B CD1 1 
ATOM   9946  N  N   . HIS D 2 179 ? 168.122 153.833 168.978 1.00 113.92 ? 179 HIS B N   1 
ATOM   9947  C  CA  . HIS D 2 179 ? 167.023 152.936 169.296 1.00 113.92 ? 179 HIS B CA  1 
ATOM   9948  C  C   . HIS D 2 179 ? 166.050 153.629 170.239 1.00 113.92 ? 179 HIS B C   1 
ATOM   9949  O  O   . HIS D 2 179 ? 166.465 154.306 171.184 1.00 113.92 ? 179 HIS B O   1 
ATOM   9950  C  CB  . HIS D 2 179 ? 167.532 151.655 169.957 1.00 113.92 ? 179 HIS B CB  1 
ATOM   9951  C  CG  . HIS D 2 179 ? 168.727 151.057 169.282 1.00 113.92 ? 179 HIS B CG  1 
ATOM   9952  N  ND1 . HIS D 2 179 ? 170.011 151.250 169.743 1.00 113.92 ? 179 HIS B ND1 1 
ATOM   9953  C  CD2 . HIS D 2 179 ? 168.833 150.275 168.183 1.00 113.92 ? 179 HIS B CD2 1 
ATOM   9954  C  CE1 . HIS D 2 179 ? 170.858 150.610 168.958 1.00 113.92 ? 179 HIS B CE1 1 
ATOM   9955  N  NE2 . HIS D 2 179 ? 170.170 150.011 168.004 1.00 113.92 ? 179 HIS B NE2 1 
ATOM   9956  N  N   . HIS D 2 180 ? 164.757 153.463 169.974 1.00 113.92 ? 180 HIS B N   1 
ATOM   9957  C  CA  . HIS D 2 180 ? 163.739 153.953 170.892 1.00 113.92 ? 180 HIS B CA  1 
ATOM   9958  C  C   . HIS D 2 180 ? 163.843 153.233 172.231 1.00 113.92 ? 180 HIS B C   1 
ATOM   9959  O  O   . HIS D 2 180 ? 164.047 152.017 172.285 1.00 113.92 ? 180 HIS B O   1 
ATOM   9960  C  CB  . HIS D 2 180 ? 162.345 153.761 170.299 1.00 113.92 ? 180 HIS B CB  1 
ATOM   9961  C  CG  . HIS D 2 180 ? 161.240 154.019 171.275 1.00 113.92 ? 180 HIS B CG  1 
ATOM   9962  N  ND1 . HIS D 2 180 ? 160.382 153.029 171.705 1.00 113.92 ? 180 HIS B ND1 1 
ATOM   9963  C  CD2 . HIS D 2 180 ? 160.859 155.151 171.912 1.00 113.92 ? 180 HIS B CD2 1 
ATOM   9964  C  CE1 . HIS D 2 180 ? 159.518 153.542 172.562 1.00 113.92 ? 180 HIS B CE1 1 
ATOM   9965  N  NE2 . HIS D 2 180 ? 159.785 154.827 172.705 1.00 113.92 ? 180 HIS B NE2 1 
ATOM   9966  N  N   . GLY D 2 181 ? 163.699 153.987 173.316 1.00 113.92 ? 181 GLY B N   1 
ATOM   9967  C  CA  . GLY D 2 181 ? 163.782 153.386 174.633 1.00 113.92 ? 181 GLY B CA  1 
ATOM   9968  C  C   . GLY D 2 181 ? 162.450 152.836 175.092 1.00 113.92 ? 181 GLY B C   1 
ATOM   9969  O  O   . GLY D 2 181 ? 161.612 153.569 175.628 1.00 113.92 ? 181 GLY B O   1 
ATOM   9970  N  N   . ASP D 2 182 ? 162.248 151.534 174.886 1.00 113.92 ? 182 ASP B N   1 
ATOM   9971  C  CA  . ASP D 2 182 ? 160.954 150.920 175.166 1.00 113.92 ? 182 ASP B CA  1 
ATOM   9972  C  C   . ASP D 2 182 ? 160.695 150.823 176.663 1.00 113.92 ? 182 ASP B C   1 
ATOM   9973  O  O   . ASP D 2 182 ? 159.611 151.180 177.141 1.00 113.92 ? 182 ASP B O   1 
ATOM   9974  C  CB  . ASP D 2 182 ? 160.879 149.534 174.528 1.00 100.60 ? 182 ASP B CB  1 
ATOM   9975  C  CG  . ASP D 2 182 ? 160.961 149.579 173.020 1.00 100.60 ? 182 ASP B CG  1 
ATOM   9976  O  OD1 . ASP D 2 182 ? 160.707 150.654 172.440 1.00 100.60 ? 182 ASP B OD1 1 
ATOM   9977  O  OD2 . ASP D 2 182 ? 161.273 148.533 172.416 1.00 100.60 ? 182 ASP B OD2 1 
ATOM   9978  N  N   . GLY D 2 183 ? 161.670 150.317 177.419 1.00 113.92 ? 183 GLY B N   1 
ATOM   9979  C  CA  . GLY D 2 183 ? 161.444 150.096 178.837 1.00 113.92 ? 183 GLY B CA  1 
ATOM   9980  C  C   . GLY D 2 183 ? 161.057 151.360 179.578 1.00 113.92 ? 183 GLY B C   1 
ATOM   9981  O  O   . GLY D 2 183 ? 160.083 151.373 180.331 1.00 113.92 ? 183 GLY B O   1 
ATOM   9982  N  N   . VAL D 2 184 ? 161.789 152.450 179.342 1.00 113.92 ? 184 VAL B N   1 
ATOM   9983  C  CA  . VAL D 2 184 ? 161.506 153.701 180.043 1.00 113.92 ? 184 VAL B CA  1 
ATOM   9984  C  C   . VAL D 2 184 ? 160.137 154.246 179.654 1.00 113.92 ? 184 VAL B C   1 
ATOM   9985  O  O   . VAL D 2 184 ? 159.340 154.643 180.519 1.00 113.92 ? 184 VAL B O   1 
ATOM   9986  C  CB  . VAL D 2 184 ? 162.619 154.727 179.766 1.00 113.92 ? 184 VAL B CB  1 
ATOM   9987  C  CG1 . VAL D 2 184 ? 162.396 155.984 180.590 1.00 113.92 ? 184 VAL B CG1 1 
ATOM   9988  C  CG2 . VAL D 2 184 ? 163.978 154.116 180.059 1.00 113.92 ? 184 VAL B CG2 1 
ATOM   9989  N  N   . GLU D 2 185 ? 159.815 154.218 178.359 1.00 113.92 ? 185 GLU B N   1 
ATOM   9990  C  CA  . GLU D 2 185 ? 158.550 154.797 177.924 1.00 113.92 ? 185 GLU B CA  1 
ATOM   9991  C  C   . GLU D 2 185 ? 157.382 154.010 178.497 1.00 113.92 ? 185 GLU B C   1 
ATOM   9992  O  O   . GLU D 2 185 ? 156.470 154.590 179.092 1.00 113.92 ? 185 GLU B O   1 
ATOM   9993  C  CB  . GLU D 2 185 ? 158.467 154.859 176.400 1.00 113.92 ? 185 GLU B CB  1 
ATOM   9994  C  CG  . GLU D 2 185 ? 157.246 155.633 175.921 1.00 113.92 ? 185 GLU B CG  1 
ATOM   9995  C  CD  . GLU D 2 185 ? 157.165 155.754 174.417 1.00 113.92 ? 185 GLU B CD  1 
ATOM   9996  O  OE1 . GLU D 2 185 ? 157.102 154.710 173.740 1.00 113.92 ? 185 GLU B OE1 1 
ATOM   9997  O  OE2 . GLU D 2 185 ? 157.169 156.896 173.910 1.00 113.92 ? 185 GLU B OE2 1 
ATOM   9998  N  N   . GLU D 2 186 ? 157.396 152.684 178.346 1.00 123.80 ? 186 GLU B N   1 
ATOM   9999  C  CA  . GLU D 2 186 ? 156.284 151.903 178.872 1.00 123.80 ? 186 GLU B CA  1 
ATOM   10000 C  C   . GLU D 2 186 ? 156.236 151.971 180.393 1.00 123.80 ? 186 GLU B C   1 
ATOM   10001 O  O   . GLU D 2 186 ? 155.149 151.905 180.978 1.00 123.80 ? 186 GLU B O   1 
ATOM   10002 C  CB  . GLU D 2 186 ? 156.369 150.454 178.386 1.00 123.80 ? 186 GLU B CB  1 
ATOM   10003 C  CG  . GLU D 2 186 ? 155.854 150.182 176.955 1.00 123.80 ? 186 GLU B CG  1 
ATOM   10004 C  CD  . GLU D 2 186 ? 156.329 151.158 175.880 1.00 123.80 ? 186 GLU B CD  1 
ATOM   10005 O  OE1 . GLU D 2 186 ? 155.704 151.179 174.798 1.00 123.80 ? 186 GLU B OE1 1 
ATOM   10006 O  OE2 . GLU D 2 186 ? 157.320 151.883 176.080 1.00 123.80 ? 186 GLU B OE2 1 
ATOM   10007 N  N   . ALA D 2 187 ? 157.394 152.091 181.053 1.00 115.59 ? 187 ALA B N   1 
ATOM   10008 C  CA  . ALA D 2 187 ? 157.402 152.227 182.503 1.00 115.59 ? 187 ALA B CA  1 
ATOM   10009 C  C   . ALA D 2 187 ? 156.732 153.520 182.937 1.00 115.59 ? 187 ALA B C   1 
ATOM   10010 O  O   . ALA D 2 187 ? 156.158 153.584 184.030 1.00 115.59 ? 187 ALA B O   1 
ATOM   10011 C  CB  . ALA D 2 187 ? 158.836 152.165 183.028 1.00 115.59 ? 187 ALA B CB  1 
ATOM   10012 N  N   . PHE D 2 188 ? 156.792 154.563 182.102 1.00 113.92 ? 188 PHE B N   1 
ATOM   10013 C  CA  . PHE D 2 188 ? 156.203 155.849 182.466 1.00 113.92 ? 188 PHE B CA  1 
ATOM   10014 C  C   . PHE D 2 188 ? 155.253 156.363 181.388 1.00 113.92 ? 188 PHE B C   1 
ATOM   10015 O  O   . PHE D 2 188 ? 155.103 157.575 181.213 1.00 113.92 ? 188 PHE B O   1 
ATOM   10016 C  CB  . PHE D 2 188 ? 157.285 156.883 182.773 1.00 113.92 ? 188 PHE B CB  1 
ATOM   10017 C  CG  . PHE D 2 188 ? 158.407 156.348 183.610 1.00 113.92 ? 188 PHE B CG  1 
ATOM   10018 C  CD1 . PHE D 2 188 ? 158.213 156.087 184.954 1.00 113.92 ? 188 PHE B CD1 1 
ATOM   10019 C  CD2 . PHE D 2 188 ? 159.654 156.119 183.062 1.00 113.92 ? 188 PHE B CD2 1 
ATOM   10020 C  CE1 . PHE D 2 188 ? 159.237 155.593 185.728 1.00 113.92 ? 188 PHE B CE1 1 
ATOM   10021 C  CE2 . PHE D 2 188 ? 160.684 155.625 183.833 1.00 113.92 ? 188 PHE B CE2 1 
ATOM   10022 C  CZ  . PHE D 2 188 ? 160.474 155.360 185.168 1.00 113.92 ? 188 PHE B CZ  1 
ATOM   10023 N  N   . TYR D 2 189 ? 154.607 155.453 180.656 1.00 113.92 ? 189 TYR B N   1 
ATOM   10024 C  CA  . TYR D 2 189 ? 153.717 155.861 179.573 1.00 113.92 ? 189 TYR B CA  1 
ATOM   10025 C  C   . TYR D 2 189 ? 152.432 156.493 180.093 1.00 113.92 ? 189 TYR B C   1 
ATOM   10026 O  O   . TYR D 2 189 ? 151.896 157.411 179.463 1.00 113.92 ? 189 TYR B O   1 
ATOM   10027 C  CB  . TYR D 2 189 ? 153.387 154.656 178.693 1.00 113.92 ? 189 TYR B CB  1 
ATOM   10028 C  CG  . TYR D 2 189 ? 152.888 155.007 177.313 1.00 113.92 ? 189 TYR B CG  1 
ATOM   10029 C  CD1 . TYR D 2 189 ? 153.717 155.629 176.392 1.00 113.92 ? 189 TYR B CD1 1 
ATOM   10030 C  CD2 . TYR D 2 189 ? 151.589 154.709 176.927 1.00 113.92 ? 189 TYR B CD2 1 
ATOM   10031 C  CE1 . TYR D 2 189 ? 153.268 155.949 175.127 1.00 113.92 ? 189 TYR B CE1 1 
ATOM   10032 C  CE2 . TYR D 2 189 ? 151.130 155.024 175.666 1.00 113.92 ? 189 TYR B CE2 1 
ATOM   10033 C  CZ  . TYR D 2 189 ? 151.972 155.643 174.769 1.00 113.92 ? 189 TYR B CZ  1 
ATOM   10034 O  OH  . TYR D 2 189 ? 151.517 155.958 173.511 1.00 113.92 ? 189 TYR B OH  1 
ATOM   10035 N  N   . THR D 2 190 ? 151.925 156.021 181.233 1.00 113.92 ? 190 THR B N   1 
ATOM   10036 C  CA  . THR D 2 190 ? 150.634 156.452 181.756 1.00 113.92 ? 190 THR B CA  1 
ATOM   10037 C  C   . THR D 2 190 ? 150.763 157.310 183.012 1.00 113.92 ? 190 THR B C   1 
ATOM   10038 O  O   . THR D 2 190 ? 149.859 157.323 183.852 1.00 113.92 ? 190 THR B O   1 
ATOM   10039 C  CB  . THR D 2 190 ? 149.748 155.240 182.036 1.00 113.46 ? 190 THR B CB  1 
ATOM   10040 O  OG1 . THR D 2 190 ? 150.381 154.397 183.006 1.00 113.46 ? 190 THR B OG1 1 
ATOM   10041 C  CG2 . THR D 2 190 ? 149.516 154.447 180.759 1.00 113.46 ? 190 THR B CG2 1 
ATOM   10042 N  N   . THR D 2 191 ? 151.870 158.032 183.159 1.00 113.92 ? 191 THR B N   1 
ATOM   10043 C  CA  . THR D 2 191 ? 152.068 158.901 184.309 1.00 113.92 ? 191 THR B CA  1 
ATOM   10044 C  C   . THR D 2 191 ? 152.602 160.250 183.852 1.00 113.92 ? 191 THR B C   1 
ATOM   10045 O  O   . THR D 2 191 ? 153.335 160.346 182.863 1.00 113.92 ? 191 THR B O   1 
ATOM   10046 C  CB  . THR D 2 191 ? 153.025 158.281 185.341 1.00 113.92 ? 191 THR B CB  1 
ATOM   10047 O  OG1 . THR D 2 191 ? 153.173 159.172 186.454 1.00 113.92 ? 191 THR B OG1 1 
ATOM   10048 C  CG2 . THR D 2 191 ? 154.387 158.025 184.727 1.00 113.92 ? 191 THR B CG2 1 
ATOM   10049 N  N   . ASP D 2 192 ? 152.213 161.294 184.577 1.00 116.18 ? 192 ASP B N   1 
ATOM   10050 C  CA  . ASP D 2 192 ? 152.657 162.650 184.292 1.00 116.18 ? 192 ASP B CA  1 
ATOM   10051 C  C   . ASP D 2 192 ? 153.889 163.052 185.092 1.00 116.18 ? 192 ASP B C   1 
ATOM   10052 O  O   . ASP D 2 192 ? 154.395 164.162 184.902 1.00 116.18 ? 192 ASP B O   1 
ATOM   10053 C  CB  . ASP D 2 192 ? 151.525 163.644 184.565 1.00 116.18 ? 192 ASP B CB  1 
ATOM   10054 C  CG  . ASP D 2 192 ? 151.010 163.563 185.988 1.00 116.18 ? 192 ASP B CG  1 
ATOM   10055 O  OD1 . ASP D 2 192 ? 150.977 162.447 186.548 1.00 116.18 ? 192 ASP B OD1 1 
ATOM   10056 O  OD2 . ASP D 2 192 ? 150.638 164.616 186.548 1.00 116.18 ? 192 ASP B OD2 1 
ATOM   10057 N  N   . ARG D 2 193 ? 154.383 162.184 185.977 1.00 113.92 ? 193 ARG B N   1 
ATOM   10058 C  CA  . ARG D 2 193 ? 155.557 162.533 186.765 1.00 113.92 ? 193 ARG B CA  1 
ATOM   10059 C  C   . ARG D 2 193 ? 156.834 162.529 185.940 1.00 113.92 ? 193 ARG B C   1 
ATOM   10060 O  O   . ARG D 2 193 ? 157.791 163.221 186.302 1.00 113.92 ? 193 ARG B O   1 
ATOM   10061 C  CB  . ARG D 2 193 ? 155.704 161.566 187.939 1.00 107.20 ? 193 ARG B CB  1 
ATOM   10062 C  CG  . ARG D 2 193 ? 154.810 161.876 189.125 1.00 107.20 ? 193 ARG B CG  1 
ATOM   10063 C  CD  . ARG D 2 193 ? 155.371 161.245 190.388 1.00 107.20 ? 193 ARG B CD  1 
ATOM   10064 N  NE  . ARG D 2 193 ? 156.463 162.028 190.953 1.00 107.20 ? 193 ARG B NE  1 
ATOM   10065 C  CZ  . ARG D 2 193 ? 157.166 161.674 192.020 1.00 107.20 ? 193 ARG B CZ  1 
ATOM   10066 N  NH1 . ARG D 2 193 ? 156.932 160.536 192.655 1.00 107.20 ? 193 ARG B NH1 1 
ATOM   10067 N  NH2 . ARG D 2 193 ? 158.133 162.475 192.455 1.00 107.20 ? 193 ARG B NH2 1 
ATOM   10068 N  N   . VAL D 2 194 ? 156.873 161.773 184.846 1.00 113.92 ? 194 VAL B N   1 
ATOM   10069 C  CA  . VAL D 2 194 ? 158.072 161.625 184.033 1.00 113.92 ? 194 VAL B CA  1 
ATOM   10070 C  C   . VAL D 2 194 ? 157.677 161.810 182.578 1.00 113.92 ? 194 VAL B C   1 
ATOM   10071 O  O   . VAL D 2 194 ? 156.809 161.088 182.074 1.00 113.92 ? 194 VAL B O   1 
ATOM   10072 C  CB  . VAL D 2 194 ? 158.741 160.253 184.228 1.00 113.92 ? 194 VAL B CB  1 
ATOM   10073 C  CG1 . VAL D 2 194 ? 159.908 160.092 183.268 1.00 113.92 ? 194 VAL B CG1 1 
ATOM   10074 C  CG2 . VAL D 2 194 ? 159.197 160.077 185.660 1.00 113.92 ? 194 VAL B CG2 1 
ATOM   10075 N  N   . MET D 2 195 ? 158.305 162.765 181.904 1.00 113.92 ? 195 MET B N   1 
ATOM   10076 C  CA  . MET D 2 195 ? 158.160 162.868 180.457 1.00 113.92 ? 195 MET B CA  1 
ATOM   10077 C  C   . MET D 2 195 ? 159.409 162.301 179.804 1.00 113.92 ? 195 MET B C   1 
ATOM   10078 O  O   . MET D 2 195 ? 160.525 162.624 180.216 1.00 113.92 ? 195 MET B O   1 
ATOM   10079 C  CB  . MET D 2 195 ? 157.912 164.304 179.993 1.00 98.64  ? 195 MET B CB  1 
ATOM   10080 C  CG  . MET D 2 195 ? 158.050 164.454 178.480 1.00 98.64  ? 195 MET B CG  1 
ATOM   10081 S  SD  . MET D 2 195 ? 157.900 166.126 177.834 1.00 98.64  ? 195 MET B SD  1 
ATOM   10082 C  CE  . MET D 2 195 ? 157.169 166.966 179.225 1.00 98.64  ? 195 MET B CE  1 
ATOM   10083 N  N   . THR D 2 196 ? 159.222 161.478 178.776 1.00 113.92 ? 196 THR B N   1 
ATOM   10084 C  CA  . THR D 2 196 ? 160.321 160.768 178.124 1.00 113.92 ? 196 THR B CA  1 
ATOM   10085 C  C   . THR D 2 196 ? 160.434 161.249 176.680 1.00 113.92 ? 196 THR B C   1 
ATOM   10086 O  O   . THR D 2 196 ? 159.782 160.711 175.784 1.00 113.92 ? 196 THR B O   1 
ATOM   10087 C  CB  . THR D 2 196 ? 160.109 159.256 178.186 1.00 113.92 ? 196 THR B CB  1 
ATOM   10088 O  OG1 . THR D 2 196 ? 159.175 158.863 177.174 1.00 113.92 ? 196 THR B OG1 1 
ATOM   10089 C  CG2 . THR D 2 196 ? 159.572 158.846 179.548 1.00 113.92 ? 196 THR B CG2 1 
ATOM   10090 N  N   . VAL D 2 197 ? 161.270 162.261 176.462 1.00 113.92 ? 197 VAL B N   1 
ATOM   10091 C  CA  . VAL D 2 197 ? 161.610 162.696 175.113 1.00 113.92 ? 197 VAL B CA  1 
ATOM   10092 C  C   . VAL D 2 197 ? 162.686 161.766 174.567 1.00 113.92 ? 197 VAL B C   1 
ATOM   10093 O  O   . VAL D 2 197 ? 163.765 161.632 175.155 1.00 113.92 ? 197 VAL B O   1 
ATOM   10094 C  CB  . VAL D 2 197 ? 162.079 164.158 175.096 1.00 113.92 ? 197 VAL B CB  1 
ATOM   10095 C  CG1 . VAL D 2 197 ? 162.282 164.626 173.666 1.00 113.92 ? 197 VAL B CG1 1 
ATOM   10096 C  CG2 . VAL D 2 197 ? 161.063 165.039 175.794 1.00 113.92 ? 197 VAL B CG2 1 
ATOM   10097 N  N   . SER D 2 198 ? 162.394 161.121 173.444 1.00 113.92 ? 198 SER B N   1 
ATOM   10098 C  CA  . SER D 2 198 ? 163.263 160.103 172.870 1.00 113.92 ? 198 SER B CA  1 
ATOM   10099 C  C   . SER D 2 198 ? 163.559 160.472 171.427 1.00 113.92 ? 198 SER B C   1 
ATOM   10100 O  O   . SER D 2 198 ? 162.639 160.544 170.601 1.00 113.92 ? 198 SER B O   1 
ATOM   10101 C  CB  . SER D 2 198 ? 162.624 158.715 172.959 1.00 113.92 ? 198 SER B CB  1 
ATOM   10102 O  OG  . SER D 2 198 ? 162.036 158.352 171.727 1.00 113.92 ? 198 SER B OG  1 
ATOM   10103 N  N   . PHE D 2 199 ? 164.836 160.713 171.126 1.00 113.92 ? 199 PHE B N   1 
ATOM   10104 C  CA  . PHE D 2 199 ? 165.293 160.987 169.771 1.00 113.92 ? 199 PHE B CA  1 
ATOM   10105 C  C   . PHE D 2 199 ? 165.871 159.685 169.229 1.00 113.92 ? 199 PHE B C   1 
ATOM   10106 O  O   . PHE D 2 199 ? 166.886 159.198 169.735 1.00 113.92 ? 199 PHE B O   1 
ATOM   10107 C  CB  . PHE D 2 199 ? 166.342 162.094 169.776 1.00 113.92 ? 199 PHE B CB  1 
ATOM   10108 C  CG  . PHE D 2 199 ? 165.822 163.420 170.246 1.00 113.92 ? 199 PHE B CG  1 
ATOM   10109 C  CD1 . PHE D 2 199 ? 165.219 164.301 169.368 1.00 113.92 ? 199 PHE B CD1 1 
ATOM   10110 C  CD2 . PHE D 2 199 ? 165.941 163.785 171.576 1.00 113.92 ? 199 PHE B CD2 1 
ATOM   10111 C  CE1 . PHE D 2 199 ? 164.743 165.520 169.808 1.00 113.92 ? 199 PHE B CE1 1 
ATOM   10112 C  CE2 . PHE D 2 199 ? 165.467 165.002 172.022 1.00 113.92 ? 199 PHE B CE2 1 
ATOM   10113 C  CZ  . PHE D 2 199 ? 164.867 165.870 171.139 1.00 113.92 ? 199 PHE B CZ  1 
ATOM   10114 N  N   . HIS D 2 200 ? 165.227 159.118 168.212 1.00 113.92 ? 200 HIS B N   1 
ATOM   10115 C  CA  . HIS D 2 200 ? 165.572 157.766 167.802 1.00 113.92 ? 200 HIS B CA  1 
ATOM   10116 C  C   . HIS D 2 200 ? 165.199 157.571 166.344 1.00 113.92 ? 200 HIS B C   1 
ATOM   10117 O  O   . HIS D 2 200 ? 164.355 158.283 165.794 1.00 113.92 ? 200 HIS B O   1 
ATOM   10118 C  CB  . HIS D 2 200 ? 164.846 156.717 168.651 1.00 113.92 ? 200 HIS B CB  1 
ATOM   10119 C  CG  . HIS D 2 200 ? 163.353 156.785 168.548 1.00 113.92 ? 200 HIS B CG  1 
ATOM   10120 N  ND1 . HIS D 2 200 ? 162.555 157.318 169.535 1.00 113.92 ? 200 HIS B ND1 1 
ATOM   10121 C  CD2 . HIS D 2 200 ? 162.513 156.372 167.568 1.00 113.92 ? 200 HIS B CD2 1 
ATOM   10122 C  CE1 . HIS D 2 200 ? 161.288 157.237 169.168 1.00 113.92 ? 200 HIS B CE1 1 
ATOM   10123 N  NE2 . HIS D 2 200 ? 161.235 156.668 167.978 1.00 113.92 ? 200 HIS B NE2 1 
ATOM   10124 N  N   . LYS D 2 201 ? 165.834 156.577 165.730 1.00 113.92 ? 201 LYS B N   1 
ATOM   10125 C  CA  . LYS D 2 201 ? 165.487 156.191 164.374 1.00 113.92 ? 201 LYS B CA  1 
ATOM   10126 C  C   . LYS D 2 201 ? 164.216 155.358 164.420 1.00 113.92 ? 201 LYS B C   1 
ATOM   10127 O  O   . LYS D 2 201 ? 164.101 154.429 165.225 1.00 113.92 ? 201 LYS B O   1 
ATOM   10128 C  CB  . LYS D 2 201 ? 166.631 155.403 163.735 1.00 87.89  ? 201 LYS B CB  1 
ATOM   10129 C  CG  . LYS D 2 201 ? 166.642 155.393 162.212 1.00 87.89  ? 201 LYS B CG  1 
ATOM   10130 C  CD  . LYS D 2 201 ? 165.733 154.315 161.642 1.00 87.89  ? 201 LYS B CD  1 
ATOM   10131 C  CE  . LYS D 2 201 ? 165.755 154.317 160.124 1.00 87.89  ? 201 LYS B CE  1 
ATOM   10132 N  NZ  . LYS D 2 201 ? 164.896 153.240 159.560 1.00 87.89  ? 201 LYS B NZ  1 
ATOM   10133 N  N   . TYR D 2 202 ? 163.263 155.687 163.556 1.00 113.92 ? 202 TYR B N   1 
ATOM   10134 C  CA  . TYR D 2 202 ? 161.979 155.010 163.526 1.00 113.92 ? 202 TYR B CA  1 
ATOM   10135 C  C   . TYR D 2 202 ? 161.732 154.423 162.146 1.00 113.92 ? 202 TYR B C   1 
ATOM   10136 O  O   . TYR D 2 202 ? 162.241 154.918 161.137 1.00 113.92 ? 202 TYR B O   1 
ATOM   10137 C  CB  . TYR D 2 202 ? 160.833 155.952 163.902 1.00 113.92 ? 202 TYR B CB  1 
ATOM   10138 C  CG  . TYR D 2 202 ? 159.492 155.261 164.004 1.00 113.92 ? 202 TYR B CG  1 
ATOM   10139 C  CD1 . TYR D 2 202 ? 159.132 154.566 165.150 1.00 113.92 ? 202 TYR B CD1 1 
ATOM   10140 C  CD2 . TYR D 2 202 ? 158.587 155.303 162.952 1.00 113.92 ? 202 TYR B CD2 1 
ATOM   10141 C  CE1 . TYR D 2 202 ? 157.909 153.932 165.244 1.00 113.92 ? 202 TYR B CE1 1 
ATOM   10142 C  CE2 . TYR D 2 202 ? 157.362 154.671 163.037 1.00 113.92 ? 202 TYR B CE2 1 
ATOM   10143 C  CZ  . TYR D 2 202 ? 157.029 153.987 164.187 1.00 113.92 ? 202 TYR B CZ  1 
ATOM   10144 O  OH  . TYR D 2 202 ? 155.809 153.357 164.277 1.00 113.92 ? 202 TYR B OH  1 
ATOM   10145 N  N   . GLY D 2 203 ? 160.941 153.359 162.121 1.00 113.92 ? 203 GLY B N   1 
ATOM   10146 C  CA  . GLY D 2 203 ? 160.647 152.657 160.895 1.00 113.92 ? 203 GLY B CA  1 
ATOM   10147 C  C   . GLY D 2 203 ? 160.535 151.177 161.171 1.00 113.92 ? 203 GLY B C   1 
ATOM   10148 O  O   . GLY D 2 203 ? 159.852 150.756 162.109 1.00 113.92 ? 203 GLY B O   1 
ATOM   10149 N  N   . GLU D 2 204 ? 161.209 150.377 160.355 1.00 113.92 ? 204 GLU B N   1 
ATOM   10150 C  CA  . GLU D 2 204 ? 161.311 148.941 160.590 1.00 113.92 ? 204 GLU B CA  1 
ATOM   10151 C  C   . GLU D 2 204 ? 162.603 148.640 161.350 1.00 113.92 ? 204 GLU B C   1 
ATOM   10152 O  O   . GLU D 2 204 ? 163.475 147.888 160.919 1.00 113.92 ? 204 GLU B O   1 
ATOM   10153 C  CB  . GLU D 2 204 ? 161.228 148.202 159.265 1.00 98.61  ? 204 GLU B CB  1 
ATOM   10154 C  CG  . GLU D 2 204 ? 159.870 148.399 158.638 1.00 98.61  ? 204 GLU B CG  1 
ATOM   10155 C  CD  . GLU D 2 204 ? 159.885 148.235 157.145 1.00 98.61  ? 204 GLU B CD  1 
ATOM   10156 O  OE1 . GLU D 2 204 ? 160.454 149.101 156.449 1.00 98.61  ? 204 GLU B OE1 1 
ATOM   10157 O  OE2 . GLU D 2 204 ? 159.296 147.257 156.667 1.00 98.61  ? 204 GLU B OE2 1 
ATOM   10158 N  N   . TYR D 2 205 ? 162.700 149.273 162.514 1.00 113.92 ? 205 TYR B N   1 
ATOM   10159 C  CA  . TYR D 2 205 ? 163.857 149.192 163.384 1.00 113.92 ? 205 TYR B CA  1 
ATOM   10160 C  C   . TYR D 2 205 ? 163.562 148.228 164.530 1.00 113.92 ? 205 TYR B C   1 
ATOM   10161 O  O   . TYR D 2 205 ? 162.453 147.707 164.662 1.00 113.92 ? 205 TYR B O   1 
ATOM   10162 C  CB  . TYR D 2 205 ? 164.199 150.590 163.903 1.00 113.92 ? 205 TYR B CB  1 
ATOM   10163 C  CG  . TYR D 2 205 ? 165.665 150.928 163.885 1.00 113.92 ? 205 TYR B CG  1 
ATOM   10164 C  CD1 . TYR D 2 205 ? 166.401 150.816 162.716 1.00 113.92 ? 205 TYR B CD1 1 
ATOM   10165 C  CD2 . TYR D 2 205 ? 166.309 151.391 165.023 1.00 113.92 ? 205 TYR B CD2 1 
ATOM   10166 C  CE1 . TYR D 2 205 ? 167.736 151.129 162.684 1.00 113.92 ? 205 TYR B CE1 1 
ATOM   10167 C  CE2 . TYR D 2 205 ? 167.649 151.710 165.000 1.00 113.92 ? 205 TYR B CE2 1 
ATOM   10168 C  CZ  . TYR D 2 205 ? 168.353 151.583 163.825 1.00 113.92 ? 205 TYR B CZ  1 
ATOM   10169 O  OH  . TYR D 2 205 ? 169.691 151.891 163.788 1.00 113.92 ? 205 TYR B OH  1 
ATOM   10170 N  N   . PHE D 2 206 ? 164.578 147.973 165.357 1.00 113.92 ? 206 PHE B N   1 
ATOM   10171 C  CA  . PHE D 2 206 ? 164.506 146.933 166.379 1.00 113.92 ? 206 PHE B CA  1 
ATOM   10172 C  C   . PHE D 2 206 ? 163.300 147.112 167.301 1.00 113.92 ? 206 PHE B C   1 
ATOM   10173 O  O   . PHE D 2 206 ? 162.451 146.213 167.363 1.00 113.92 ? 206 PHE B O   1 
ATOM   10174 C  CB  . PHE D 2 206 ? 165.790 146.878 167.211 1.00 113.92 ? 206 PHE B CB  1 
ATOM   10175 C  CG  . PHE D 2 206 ? 165.591 146.287 168.578 1.00 113.92 ? 206 PHE B CG  1 
ATOM   10176 C  CD1 . PHE D 2 206 ? 165.149 144.981 168.726 1.00 113.92 ? 206 PHE B CD1 1 
ATOM   10177 C  CD2 . PHE D 2 206 ? 165.812 147.045 169.714 1.00 113.92 ? 206 PHE B CD2 1 
ATOM   10178 C  CE1 . PHE D 2 206 ? 164.950 144.440 169.977 1.00 113.92 ? 206 PHE B CE1 1 
ATOM   10179 C  CE2 . PHE D 2 206 ? 165.613 146.505 170.969 1.00 113.92 ? 206 PHE B CE2 1 
ATOM   10180 C  CZ  . PHE D 2 206 ? 165.180 145.203 171.097 1.00 113.92 ? 206 PHE B CZ  1 
ATOM   10181 N  N   . PRO D 2 207 ? 163.189 148.223 168.046 1.00 113.92 ? 207 PRO B N   1 
ATOM   10182 C  CA  . PRO D 2 207 ? 162.132 148.289 169.070 1.00 113.92 ? 207 PRO B CA  1 
ATOM   10183 C  C   . PRO D 2 207 ? 160.734 148.117 168.510 1.00 113.92 ? 207 PRO B C   1 
ATOM   10184 O  O   . PRO D 2 207 ? 159.886 147.480 169.149 1.00 113.92 ? 207 PRO B O   1 
ATOM   10185 C  CB  . PRO D 2 207 ? 162.323 149.682 169.692 1.00 113.92 ? 207 PRO B CB  1 
ATOM   10186 C  CG  . PRO D 2 207 ? 163.647 150.162 169.222 1.00 113.92 ? 207 PRO B CG  1 
ATOM   10187 C  CD  . PRO D 2 207 ? 163.872 149.521 167.902 1.00 113.92 ? 207 PRO B CD  1 
ATOM   10188 N  N   . GLY D 2 208 ? 160.467 148.664 167.326 1.00 113.92 ? 208 GLY B N   1 
ATOM   10189 C  CA  . GLY D 2 208 ? 159.151 148.599 166.737 1.00 113.92 ? 208 GLY B CA  1 
ATOM   10190 C  C   . GLY D 2 208 ? 158.169 149.603 167.291 1.00 113.92 ? 208 GLY B C   1 
ATOM   10191 O  O   . GLY D 2 208 ? 157.080 149.759 166.724 1.00 113.92 ? 208 GLY B O   1 
ATOM   10192 N  N   . THR D 2 209 ? 158.517 150.292 168.372 1.00 113.92 ? 209 THR B N   1 
ATOM   10193 C  CA  . THR D 2 209 ? 157.663 151.276 169.011 1.00 113.92 ? 209 THR B CA  1 
ATOM   10194 C  C   . THR D 2 209 ? 158.298 152.656 168.885 1.00 113.92 ? 209 THR B C   1 
ATOM   10195 O  O   . THR D 2 209 ? 159.418 152.812 168.388 1.00 113.92 ? 209 THR B O   1 
ATOM   10196 C  CB  . THR D 2 209 ? 157.422 150.914 170.479 1.00 97.90  ? 209 THR B CB  1 
ATOM   10197 O  OG1 . THR D 2 209 ? 158.677 150.672 171.126 1.00 97.90  ? 209 THR B OG1 1 
ATOM   10198 C  CG2 . THR D 2 209 ? 156.557 149.668 170.584 1.00 97.90  ? 209 THR B CG2 1 
ATOM   10199 N  N   . GLY D 2 210 ? 157.569 153.663 169.342 1.00 113.92 ? 210 GLY B N   1 
ATOM   10200 C  CA  . GLY D 2 210 ? 158.008 155.033 169.260 1.00 113.92 ? 210 GLY B CA  1 
ATOM   10201 C  C   . GLY D 2 210 ? 157.356 155.814 168.146 1.00 113.92 ? 210 GLY B C   1 
ATOM   10202 O  O   . GLY D 2 210 ? 158.003 156.695 167.569 1.00 113.92 ? 210 GLY B O   1 
ATOM   10203 N  N   . ASP D 2 211 ? 156.101 155.518 167.824 1.00 113.92 ? 211 ASP B N   1 
ATOM   10204 C  CA  . ASP D 2 211 ? 155.395 156.220 166.765 1.00 113.92 ? 211 ASP B CA  1 
ATOM   10205 C  C   . ASP D 2 211 ? 155.136 157.668 167.159 1.00 113.92 ? 211 ASP B C   1 
ATOM   10206 O  O   . ASP D 2 211 ? 155.036 158.008 168.340 1.00 113.92 ? 211 ASP B O   1 
ATOM   10207 C  CB  . ASP D 2 211 ? 154.074 155.513 166.460 1.00 109.89 ? 211 ASP B CB  1 
ATOM   10208 C  CG  . ASP D 2 211 ? 153.396 156.046 165.213 1.00 109.89 ? 211 ASP B CG  1 
ATOM   10209 O  OD1 . ASP D 2 211 ? 153.974 156.926 164.542 1.00 109.89 ? 211 ASP B OD1 1 
ATOM   10210 O  OD2 . ASP D 2 211 ? 152.278 155.583 164.902 1.00 109.89 ? 211 ASP B OD2 1 
ATOM   10211 N  N   . LEU D 2 212 ? 155.046 158.530 166.143 1.00 113.92 ? 212 LEU B N   1 
ATOM   10212 C  CA  . LEU D 2 212 ? 154.762 159.939 166.390 1.00 113.92 ? 212 LEU B CA  1 
ATOM   10213 C  C   . LEU D 2 212 ? 153.430 160.114 167.106 1.00 113.92 ? 212 LEU B C   1 
ATOM   10214 O  O   . LEU D 2 212 ? 153.239 161.095 167.833 1.00 113.92 ? 212 LEU B O   1 
ATOM   10215 C  CB  . LEU D 2 212 ? 154.769 160.717 165.074 1.00 113.92 ? 212 LEU B CB  1 
ATOM   10216 C  CG  . LEU D 2 212 ? 154.536 162.225 165.169 1.00 113.92 ? 212 LEU B CG  1 
ATOM   10217 C  CD1 . LEU D 2 212 ? 155.598 162.867 166.042 1.00 113.92 ? 212 LEU B CD1 1 
ATOM   10218 C  CD2 . LEU D 2 212 ? 154.523 162.852 163.790 1.00 113.92 ? 212 LEU B CD2 1 
ATOM   10219 N  N   . ARG D 2 213 ? 152.507 159.172 166.922 1.00 113.92 ? 213 ARG B N   1 
ATOM   10220 C  CA  . ARG D 2 213 ? 151.198 159.230 167.552 1.00 113.92 ? 213 ARG B CA  1 
ATOM   10221 C  C   . ARG D 2 213 ? 151.184 158.596 168.936 1.00 113.92 ? 213 ARG B C   1 
ATOM   10222 O  O   . ARG D 2 213 ? 150.171 158.698 169.636 1.00 113.92 ? 213 ARG B O   1 
ATOM   10223 C  CB  . ARG D 2 213 ? 150.158 158.531 166.672 1.00 112.96 ? 213 ARG B CB  1 
ATOM   10224 C  CG  . ARG D 2 213 ? 150.058 159.086 165.263 1.00 112.96 ? 213 ARG B CG  1 
ATOM   10225 C  CD  . ARG D 2 213 ? 148.737 158.702 164.620 1.00 112.96 ? 213 ARG B CD  1 
ATOM   10226 N  NE  . ARG D 2 213 ? 148.548 157.256 164.591 1.00 112.96 ? 213 ARG B NE  1 
ATOM   10227 C  CZ  . ARG D 2 213 ? 148.968 156.463 163.615 1.00 112.96 ? 213 ARG B CZ  1 
ATOM   10228 N  NH1 . ARG D 2 213 ? 149.610 156.942 162.562 1.00 112.96 ? 213 ARG B NH1 1 
ATOM   10229 N  NH2 . ARG D 2 213 ? 148.738 155.156 163.697 1.00 112.96 ? 213 ARG B NH2 1 
ATOM   10230 N  N   . ASP D 2 214 ? 152.277 157.950 169.348 1.00 116.82 ? 214 ASP B N   1 
ATOM   10231 C  CA  . ASP D 2 214 ? 152.392 157.396 170.696 1.00 116.82 ? 214 ASP B CA  1 
ATOM   10232 C  C   . ASP D 2 214 ? 152.754 158.527 171.658 1.00 116.82 ? 214 ASP B C   1 
ATOM   10233 O  O   . ASP D 2 214 ? 153.853 158.604 172.211 1.00 116.82 ? 214 ASP B O   1 
ATOM   10234 C  CB  . ASP D 2 214 ? 153.420 156.274 170.732 1.00 116.82 ? 214 ASP B CB  1 
ATOM   10235 C  CG  . ASP D 2 214 ? 152.795 154.904 170.572 1.00 116.82 ? 214 ASP B CG  1 
ATOM   10236 O  OD1 . ASP D 2 214 ? 151.550 154.821 170.510 1.00 116.82 ? 214 ASP B OD1 1 
ATOM   10237 O  OD2 . ASP D 2 214 ? 153.547 153.910 170.508 1.00 116.82 ? 214 ASP B OD2 1 
ATOM   10238 N  N   . ILE D 2 215 ? 151.785 159.424 171.855 1.00 120.94 ? 215 ILE B N   1 
ATOM   10239 C  CA  . ILE D 2 215 ? 152.016 160.630 172.643 1.00 120.94 ? 215 ILE B CA  1 
ATOM   10240 C  C   . ILE D 2 215 ? 151.627 160.465 174.105 1.00 120.94 ? 215 ILE B C   1 
ATOM   10241 O  O   . ILE D 2 215 ? 151.894 161.369 174.909 1.00 120.94 ? 215 ILE B O   1 
ATOM   10242 C  CB  . ILE D 2 215 ? 151.303 161.817 171.956 1.00 120.94 ? 215 ILE B CB  1 
ATOM   10243 C  CG1 . ILE D 2 215 ? 149.775 161.720 172.058 1.00 120.94 ? 215 ILE B CG1 1 
ATOM   10244 C  CG2 . ILE D 2 215 ? 151.726 161.921 170.502 1.00 120.94 ? 215 ILE B CG2 1 
ATOM   10245 C  CD1 . ILE D 2 215 ? 149.159 162.430 173.234 1.00 120.94 ? 215 ILE B CD1 1 
ATOM   10246 N  N   . GLY D 2 216 ? 151.043 159.332 174.482 1.00 118.56 ? 216 GLY B N   1 
ATOM   10247 C  CA  . GLY D 2 216 ? 150.731 159.025 175.860 1.00 118.56 ? 216 GLY B CA  1 
ATOM   10248 C  C   . GLY D 2 216 ? 149.298 158.567 176.024 1.00 118.56 ? 216 GLY B C   1 
ATOM   10249 O  O   . GLY D 2 216 ? 148.521 158.501 175.074 1.00 118.56 ? 216 GLY B O   1 
ATOM   10250 N  N   . ALA D 2 217 ? 148.954 158.246 177.270 1.00 129.19 ? 217 ALA B N   1 
ATOM   10251 C  CA  . ALA D 2 217 ? 147.607 157.808 177.609 1.00 129.19 ? 217 ALA B CA  1 
ATOM   10252 C  C   . ALA D 2 217 ? 147.371 158.032 179.095 1.00 129.19 ? 217 ALA B C   1 
ATOM   10253 O  O   . ALA D 2 217 ? 148.313 158.184 179.876 1.00 129.19 ? 217 ALA B O   1 
ATOM   10254 C  CB  . ALA D 2 217 ? 147.384 156.336 177.245 1.00 129.19 ? 217 ALA B CB  1 
ATOM   10255 N  N   . GLY D 2 218 ? 146.093 158.048 179.474 1.00 113.92 ? 218 GLY B N   1 
ATOM   10256 C  CA  . GLY D 2 218 ? 145.736 158.224 180.869 1.00 113.92 ? 218 GLY B CA  1 
ATOM   10257 C  C   . GLY D 2 218 ? 146.111 159.600 181.393 1.00 113.92 ? 218 GLY B C   1 
ATOM   10258 O  O   . GLY D 2 218 ? 146.087 160.601 180.671 1.00 113.92 ? 218 GLY B O   1 
ATOM   10259 N  N   . LYS D 2 219 ? 146.447 159.648 182.685 1.00 113.92 ? 219 LYS B N   1 
ATOM   10260 C  CA  . LYS D 2 219 ? 146.833 160.914 183.303 1.00 113.92 ? 219 LYS B CA  1 
ATOM   10261 C  C   . LYS D 2 219 ? 148.059 161.511 182.627 1.00 113.92 ? 219 LYS B C   1 
ATOM   10262 O  O   . LYS D 2 219 ? 148.181 162.736 182.529 1.00 113.92 ? 219 LYS B O   1 
ATOM   10263 C  CB  . LYS D 2 219 ? 147.093 160.714 184.796 1.00 113.92 ? 219 LYS B CB  1 
ATOM   10264 N  N   . GLY D 2 220 ? 148.971 160.664 182.158 1.00 124.17 ? 220 GLY B N   1 
ATOM   10265 C  CA  . GLY D 2 220 ? 150.137 161.115 181.428 1.00 124.17 ? 220 GLY B CA  1 
ATOM   10266 C  C   . GLY D 2 220 ? 149.871 161.139 179.939 1.00 124.17 ? 220 GLY B C   1 
ATOM   10267 O  O   . GLY D 2 220 ? 150.698 160.683 179.144 1.00 124.17 ? 220 GLY B O   1 
ATOM   10268 N  N   . LYS D 2 221 ? 148.703 161.663 179.554 1.00 127.06 ? 221 LYS B N   1 
ATOM   10269 C  CA  . LYS D 2 221 ? 148.299 161.631 178.152 1.00 127.06 ? 221 LYS B CA  1 
ATOM   10270 C  C   . LYS D 2 221 ? 149.273 162.396 177.267 1.00 127.06 ? 221 LYS B C   1 
ATOM   10271 O  O   . LYS D 2 221 ? 149.633 161.925 176.186 1.00 127.06 ? 221 LYS B O   1 
ATOM   10272 C  CB  . LYS D 2 221 ? 146.886 162.192 177.996 1.00 127.06 ? 221 LYS B CB  1 
ATOM   10273 C  CG  . LYS D 2 221 ? 146.408 162.252 176.554 1.00 127.06 ? 221 LYS B CG  1 
ATOM   10274 C  CD  . LYS D 2 221 ? 144.892 162.227 176.464 1.00 127.06 ? 221 LYS B CD  1 
ATOM   10275 C  CE  . LYS D 2 221 ? 144.424 162.226 175.016 1.00 127.06 ? 221 LYS B CE  1 
ATOM   10276 N  NZ  . LYS D 2 221 ? 145.566 162.250 174.060 1.00 127.06 ? 221 LYS B NZ  1 
ATOM   10277 N  N   . TYR D 2 222 ? 149.713 163.572 177.703 1.00 126.30 ? 222 TYR B N   1 
ATOM   10278 C  CA  . TYR D 2 222 ? 150.627 164.406 176.928 1.00 126.30 ? 222 TYR B CA  1 
ATOM   10279 C  C   . TYR D 2 222 ? 152.011 164.473 177.570 1.00 126.30 ? 222 TYR B C   1 
ATOM   10280 O  O   . TYR D 2 222 ? 152.647 165.526 177.607 1.00 126.30 ? 222 TYR B O   1 
ATOM   10281 C  CB  . TYR D 2 222 ? 150.052 165.805 176.734 1.00 126.30 ? 222 TYR B CB  1 
ATOM   10282 C  CG  . TYR D 2 222 ? 149.025 165.880 175.626 1.00 126.30 ? 222 TYR B CG  1 
ATOM   10283 C  CD1 . TYR D 2 222 ? 149.412 166.094 174.310 1.00 126.30 ? 222 TYR B CD1 1 
ATOM   10284 C  CD2 . TYR D 2 222 ? 147.671 165.730 175.893 1.00 126.30 ? 222 TYR B CD2 1 
ATOM   10285 C  CE1 . TYR D 2 222 ? 148.482 166.160 173.293 1.00 126.30 ? 222 TYR B CE1 1 
ATOM   10286 C  CE2 . TYR D 2 222 ? 146.732 165.796 174.881 1.00 126.30 ? 222 TYR B CE2 1 
ATOM   10287 C  CZ  . TYR D 2 222 ? 147.143 166.011 173.583 1.00 126.30 ? 222 TYR B CZ  1 
ATOM   10288 O  OH  . TYR D 2 222 ? 146.214 166.077 172.571 1.00 126.30 ? 222 TYR B OH  1 
ATOM   10289 N  N   . TYR D 2 223 ? 152.489 163.342 178.079 1.00 113.92 ? 223 TYR B N   1 
ATOM   10290 C  CA  . TYR D 2 223 ? 153.783 163.254 178.742 1.00 113.92 ? 223 TYR B CA  1 
ATOM   10291 C  C   . TYR D 2 223 ? 154.635 162.152 178.125 1.00 113.92 ? 223 TYR B C   1 
ATOM   10292 O  O   . TYR D 2 223 ? 155.332 161.414 178.825 1.00 113.92 ? 223 TYR B O   1 
ATOM   10293 C  CB  . TYR D 2 223 ? 153.607 163.030 180.241 1.00 113.92 ? 223 TYR B CB  1 
ATOM   10294 C  CG  . TYR D 2 223 ? 152.945 164.187 180.958 1.00 113.92 ? 223 TYR B CG  1 
ATOM   10295 C  CD1 . TYR D 2 223 ? 151.564 164.329 180.965 1.00 113.92 ? 223 TYR B CD1 1 
ATOM   10296 C  CD2 . TYR D 2 223 ? 153.703 165.133 181.635 1.00 113.92 ? 223 TYR B CD2 1 
ATOM   10297 C  CE1 . TYR D 2 223 ? 150.957 165.386 181.618 1.00 113.92 ? 223 TYR B CE1 1 
ATOM   10298 C  CE2 . TYR D 2 223 ? 153.106 166.189 182.294 1.00 113.92 ? 223 TYR B CE2 1 
ATOM   10299 C  CZ  . TYR D 2 223 ? 151.734 166.311 182.282 1.00 113.92 ? 223 TYR B CZ  1 
ATOM   10300 O  OH  . TYR D 2 223 ? 151.136 167.364 182.937 1.00 113.92 ? 223 TYR B OH  1 
ATOM   10301 N  N   . ALA D 2 224 ? 154.588 162.024 176.797 1.00 113.92 ? 224 ALA B N   1 
ATOM   10302 C  CA  . ALA D 2 224 ? 155.415 161.046 176.092 1.00 113.92 ? 224 ALA B CA  1 
ATOM   10303 C  C   . ALA D 2 224 ? 155.750 161.628 174.720 1.00 113.92 ? 224 ALA B C   1 
ATOM   10304 O  O   . ALA D 2 224 ? 154.950 161.521 173.786 1.00 113.92 ? 224 ALA B O   1 
ATOM   10305 C  CB  . ALA D 2 224 ? 154.704 159.705 175.973 1.00 113.92 ? 224 ALA B CB  1 
ATOM   10306 N  N   . VAL D 2 225 ? 156.927 162.237 174.612 1.00 113.92 ? 225 VAL B N   1 
ATOM   10307 C  CA  . VAL D 2 225 ? 157.383 162.879 173.384 1.00 113.92 ? 225 VAL B CA  1 
ATOM   10308 C  C   . VAL D 2 225 ? 158.357 161.956 172.666 1.00 113.92 ? 225 VAL B C   1 
ATOM   10309 O  O   . VAL D 2 225 ? 159.346 161.505 173.254 1.00 113.92 ? 225 VAL B O   1 
ATOM   10310 C  CB  . VAL D 2 225 ? 158.031 164.241 173.682 1.00 113.92 ? 225 VAL B CB  1 
ATOM   10311 C  CG1 . VAL D 2 225 ? 158.328 164.970 172.396 1.00 113.92 ? 225 VAL B CG1 1 
ATOM   10312 C  CG2 . VAL D 2 225 ? 157.113 165.073 174.556 1.00 113.92 ? 225 VAL B CG2 1 
ATOM   10313 N  N   . ASN D 2 226 ? 158.082 161.673 171.395 1.00 113.92 ? 226 ASN B N   1 
ATOM   10314 C  CA  . ASN D 2 226 ? 158.969 160.876 170.559 1.00 113.92 ? 226 ASN B CA  1 
ATOM   10315 C  C   . ASN D 2 226 ? 159.258 161.636 169.275 1.00 113.92 ? 226 ASN B C   1 
ATOM   10316 O  O   . ASN D 2 226 ? 158.337 162.188 168.664 1.00 113.92 ? 226 ASN B O   1 
ATOM   10317 C  CB  . ASN D 2 226 ? 158.347 159.514 170.238 1.00 113.92 ? 226 ASN B CB  1 
ATOM   10318 C  CG  . ASN D 2 226 ? 158.247 158.619 171.455 1.00 113.92 ? 226 ASN B CG  1 
ATOM   10319 O  OD1 . ASN D 2 226 ? 159.101 158.656 172.339 1.00 113.92 ? 226 ASN B OD1 1 
ATOM   10320 N  ND2 . ASN D 2 226 ? 157.196 157.811 171.508 1.00 113.92 ? 226 ASN B ND2 1 
ATOM   10321 N  N   . PHE D 2 227 ? 160.528 161.669 168.863 1.00 113.92 ? 227 PHE B N   1 
ATOM   10322 C  CA  . PHE D 2 227 ? 160.924 162.342 167.625 1.00 113.92 ? 227 PHE B CA  1 
ATOM   10323 C  C   . PHE D 2 227 ? 161.465 161.290 166.667 1.00 113.92 ? 227 PHE B C   1 
ATOM   10324 O  O   . PHE D 2 227 ? 162.664 160.973 166.688 1.00 113.92 ? 227 PHE B O   1 
ATOM   10325 C  CB  . PHE D 2 227 ? 161.961 163.435 167.886 1.00 113.92 ? 227 PHE B CB  1 
ATOM   10326 C  CG  . PHE D 2 227 ? 162.033 164.478 166.800 1.00 113.92 ? 227 PHE B CG  1 
ATOM   10327 C  CD1 . PHE D 2 227 ? 162.428 164.141 165.516 1.00 113.92 ? 227 PHE B CD1 1 
ATOM   10328 C  CD2 . PHE D 2 227 ? 161.704 165.795 167.066 1.00 113.92 ? 227 PHE B CD2 1 
ATOM   10329 C  CE1 . PHE D 2 227 ? 162.493 165.097 164.520 1.00 113.92 ? 227 PHE B CE1 1 
ATOM   10330 C  CE2 . PHE D 2 227 ? 161.767 166.755 166.073 1.00 113.92 ? 227 PHE B CE2 1 
ATOM   10331 C  CZ  . PHE D 2 227 ? 162.163 166.405 164.800 1.00 113.92 ? 227 PHE B CZ  1 
ATOM   10332 N  N   . PRO D 2 228 ? 160.612 160.703 165.830 1.00 113.92 ? 228 PRO B N   1 
ATOM   10333 C  CA  . PRO D 2 228 ? 161.095 159.725 164.847 1.00 113.92 ? 228 PRO B CA  1 
ATOM   10334 C  C   . PRO D 2 228 ? 162.092 160.345 163.879 1.00 113.92 ? 228 PRO B C   1 
ATOM   10335 O  O   . PRO D 2 228 ? 161.971 161.509 163.494 1.00 113.92 ? 228 PRO B O   1 
ATOM   10336 C  CB  . PRO D 2 228 ? 159.814 159.285 164.131 1.00 113.92 ? 228 PRO B CB  1 
ATOM   10337 C  CG  . PRO D 2 228 ? 158.706 159.611 165.078 1.00 113.92 ? 228 PRO B CG  1 
ATOM   10338 C  CD  . PRO D 2 228 ? 159.145 160.840 165.809 1.00 113.92 ? 228 PRO B CD  1 
ATOM   10339 N  N   . MET D 2 229 ? 163.089 159.551 163.489 1.00 113.92 ? 229 MET B N   1 
ATOM   10340 C  CA  . MET D 2 229 ? 164.088 159.989 162.527 1.00 113.92 ? 229 MET B CA  1 
ATOM   10341 C  C   . MET D 2 229 ? 164.451 158.851 161.587 1.00 113.92 ? 229 MET B C   1 
ATOM   10342 O  O   . MET D 2 229 ? 164.244 157.674 161.887 1.00 113.92 ? 229 MET B O   1 
ATOM   10343 C  CB  . MET D 2 229 ? 165.353 160.525 163.205 1.00 113.92 ? 229 MET B CB  1 
ATOM   10344 C  CG  . MET D 2 229 ? 165.212 161.936 163.730 1.00 113.92 ? 229 MET B CG  1 
ATOM   10345 S  SD  . MET D 2 229 ? 166.505 162.381 164.894 1.00 113.92 ? 229 MET B SD  1 
ATOM   10346 C  CE  . MET D 2 229 ? 165.515 162.575 166.366 1.00 113.92 ? 229 MET B CE  1 
ATOM   10347 N  N   . ARG D 2 230 ? 164.985 159.228 160.431 1.00 113.92 ? 230 ARG B N   1 
ATOM   10348 C  CA  . ARG D 2 230 ? 165.469 158.280 159.443 1.00 113.92 ? 230 ARG B CA  1 
ATOM   10349 C  C   . ARG D 2 230 ? 166.965 158.049 159.666 1.00 113.92 ? 230 ARG B C   1 
ATOM   10350 O  O   . ARG D 2 230 ? 167.532 158.459 160.682 1.00 113.92 ? 230 ARG B O   1 
ATOM   10351 C  CB  . ARG D 2 230 ? 165.152 158.801 158.044 1.00 113.92 ? 230 ARG B CB  1 
ATOM   10352 C  CG  . ARG D 2 230 ? 163.707 159.252 157.889 1.00 113.92 ? 230 ARG B CG  1 
ATOM   10353 C  CD  . ARG D 2 230 ? 163.404 159.741 156.484 1.00 113.92 ? 230 ARG B CD  1 
ATOM   10354 N  NE  . ARG D 2 230 ? 162.026 160.200 156.355 1.00 113.92 ? 230 ARG B NE  1 
ATOM   10355 C  CZ  . ARG D 2 230 ? 161.559 160.893 155.325 1.00 113.92 ? 230 ARG B CZ  1 
ATOM   10356 N  NH1 . ARG D 2 230 ? 162.340 161.240 154.314 1.00 113.92 ? 230 ARG B NH1 1 
ATOM   10357 N  NH2 . ARG D 2 230 ? 160.280 161.255 155.312 1.00 113.92 ? 230 ARG B NH2 1 
ATOM   10358 N  N   . ASP D 2 231 ? 167.623 157.383 158.721 1.00 113.92 ? 231 ASP B N   1 
ATOM   10359 C  CA  . ASP D 2 231 ? 169.026 157.021 158.870 1.00 113.92 ? 231 ASP B CA  1 
ATOM   10360 C  C   . ASP D 2 231 ? 169.933 158.105 158.298 1.00 113.92 ? 231 ASP B C   1 
ATOM   10361 O  O   . ASP D 2 231 ? 169.671 158.648 157.222 1.00 113.92 ? 231 ASP B O   1 
ATOM   10362 C  CB  . ASP D 2 231 ? 169.319 155.684 158.187 1.00 112.78 ? 231 ASP B CB  1 
ATOM   10363 C  CG  . ASP D 2 231 ? 168.857 155.649 156.747 1.00 112.78 ? 231 ASP B CG  1 
ATOM   10364 O  OD1 . ASP D 2 231 ? 167.852 156.317 156.427 1.00 112.78 ? 231 ASP B OD1 1 
ATOM   10365 O  OD2 . ASP D 2 231 ? 169.501 154.954 155.935 1.00 112.78 ? 231 ASP B OD2 1 
ATOM   10366 N  N   . GLY D 2 232 ? 171.001 158.415 159.031 1.00 113.92 ? 232 GLY B N   1 
ATOM   10367 C  CA  . GLY D 2 232 ? 172.028 159.308 158.536 1.00 113.92 ? 232 GLY B CA  1 
ATOM   10368 C  C   . GLY D 2 232 ? 171.860 160.776 158.850 1.00 113.92 ? 232 GLY B C   1 
ATOM   10369 O  O   . GLY D 2 232 ? 172.268 161.619 158.045 1.00 113.92 ? 232 GLY B O   1 
ATOM   10370 N  N   . ILE D 2 233 ? 171.313 161.116 160.016 1.00 113.92 ? 233 ILE B N   1 
ATOM   10371 C  CA  . ILE D 2 233 ? 171.132 162.516 160.388 1.00 113.92 ? 233 ILE B CA  1 
ATOM   10372 C  C   . ILE D 2 233 ? 172.486 163.154 160.676 1.00 113.92 ? 233 ILE B C   1 
ATOM   10373 O  O   . ILE D 2 233 ? 173.334 162.572 161.365 1.00 113.92 ? 233 ILE B O   1 
ATOM   10374 C  CB  . ILE D 2 233 ? 170.168 162.644 161.579 1.00 113.92 ? 233 ILE B CB  1 
ATOM   10375 C  CG1 . ILE D 2 233 ? 169.783 164.110 161.792 1.00 113.92 ? 233 ILE B CG1 1 
ATOM   10376 C  CG2 . ILE D 2 233 ? 170.745 162.022 162.843 1.00 113.92 ? 233 ILE B CG2 1 
ATOM   10377 C  CD1 . ILE D 2 233 ? 168.717 164.320 162.834 1.00 113.92 ? 233 ILE B CD1 1 
ATOM   10378 N  N   . ASP D 2 234 ? 172.715 164.339 160.107 1.00 117.80 ? 234 ASP B N   1 
ATOM   10379 C  CA  . ASP D 2 234 ? 174.005 164.995 160.255 1.00 117.80 ? 234 ASP B CA  1 
ATOM   10380 C  C   . ASP D 2 234 ? 174.109 165.643 161.630 1.00 117.80 ? 234 ASP B C   1 
ATOM   10381 O  O   . ASP D 2 234 ? 173.179 165.614 162.440 1.00 117.80 ? 234 ASP B O   1 
ATOM   10382 C  CB  . ASP D 2 234 ? 174.222 166.064 159.185 1.00 117.80 ? 234 ASP B CB  1 
ATOM   10383 C  CG  . ASP D 2 234 ? 173.716 165.655 157.831 1.00 117.80 ? 234 ASP B CG  1 
ATOM   10384 O  OD1 . ASP D 2 234 ? 172.502 165.796 157.608 1.00 117.80 ? 234 ASP B OD1 1 
ATOM   10385 O  OD2 . ASP D 2 234 ? 174.528 165.247 156.975 1.00 117.80 ? 234 ASP B OD2 1 
ATOM   10386 N  N   . ASP D 2 235 ? 175.272 166.235 161.894 1.00 121.57 ? 235 ASP B N   1 
ATOM   10387 C  CA  . ASP D 2 235 ? 175.482 166.925 163.159 1.00 121.57 ? 235 ASP B CA  1 
ATOM   10388 C  C   . ASP D 2 235 ? 174.600 168.164 163.260 1.00 121.57 ? 235 ASP B C   1 
ATOM   10389 O  O   . ASP D 2 235 ? 173.943 168.396 164.285 1.00 121.57 ? 235 ASP B O   1 
ATOM   10390 C  CB  . ASP D 2 235 ? 176.953 167.305 163.285 1.00 121.57 ? 235 ASP B CB  1 
ATOM   10391 C  CG  . ASP D 2 235 ? 177.732 166.300 164.082 1.00 121.57 ? 235 ASP B CG  1 
ATOM   10392 O  OD1 . ASP D 2 235 ? 177.115 165.608 164.916 1.00 121.57 ? 235 ASP B OD1 1 
ATOM   10393 O  OD2 . ASP D 2 235 ? 178.957 166.206 163.878 1.00 121.57 ? 235 ASP B OD2 1 
ATOM   10394 N  N   . GLU D 2 236 ? 174.583 168.975 162.199 1.00 118.24 ? 236 GLU B N   1 
ATOM   10395 C  CA  . GLU D 2 236 ? 173.863 170.244 162.221 1.00 118.24 ? 236 GLU B CA  1 
ATOM   10396 C  C   . GLU D 2 236 ? 172.369 170.027 162.417 1.00 118.24 ? 236 GLU B C   1 
ATOM   10397 O  O   . GLU D 2 236 ? 171.733 170.706 163.232 1.00 118.24 ? 236 GLU B O   1 
ATOM   10398 C  CB  . GLU D 2 236 ? 174.131 171.018 160.930 1.00 118.24 ? 236 GLU B CB  1 
ATOM   10399 N  N   . SER D 2 237 ? 171.789 169.092 161.662 1.00 113.92 ? 237 SER B N   1 
ATOM   10400 C  CA  . SER D 2 237 ? 170.358 168.832 161.779 1.00 113.92 ? 237 SER B CA  1 
ATOM   10401 C  C   . SER D 2 237 ? 170.008 168.334 163.174 1.00 113.92 ? 237 SER B C   1 
ATOM   10402 O  O   . SER D 2 237 ? 169.022 168.782 163.773 1.00 113.92 ? 237 SER B O   1 
ATOM   10403 C  CB  . SER D 2 237 ? 169.921 167.819 160.721 1.00 113.92 ? 237 SER B CB  1 
ATOM   10404 O  OG  . SER D 2 237 ? 170.076 168.344 159.414 1.00 113.92 ? 237 SER B OG  1 
ATOM   10405 N  N   . TYR D 2 238 ? 170.806 167.409 163.709 1.00 113.92 ? 238 TYR B N   1 
ATOM   10406 C  CA  . TYR D 2 238 ? 170.524 166.874 165.036 1.00 113.92 ? 238 TYR B CA  1 
ATOM   10407 C  C   . TYR D 2 238 ? 170.593 167.967 166.094 1.00 113.92 ? 238 TYR B C   1 
ATOM   10408 O  O   . TYR D 2 238 ? 169.718 168.051 166.961 1.00 113.92 ? 238 TYR B O   1 
ATOM   10409 C  CB  . TYR D 2 238 ? 171.496 165.743 165.367 1.00 113.92 ? 238 TYR B CB  1 
ATOM   10410 C  CG  . TYR D 2 238 ? 170.996 164.798 166.438 1.00 113.92 ? 238 TYR B CG  1 
ATOM   10411 C  CD1 . TYR D 2 238 ? 171.089 165.132 167.783 1.00 113.92 ? 238 TYR B CD1 1 
ATOM   10412 C  CD2 . TYR D 2 238 ? 170.428 163.575 166.105 1.00 113.92 ? 238 TYR B CD2 1 
ATOM   10413 C  CE1 . TYR D 2 238 ? 170.633 164.275 168.766 1.00 113.92 ? 238 TYR B CE1 1 
ATOM   10414 C  CE2 . TYR D 2 238 ? 169.970 162.711 167.082 1.00 113.92 ? 238 TYR B CE2 1 
ATOM   10415 C  CZ  . TYR D 2 238 ? 170.074 163.066 168.410 1.00 113.92 ? 238 TYR B CZ  1 
ATOM   10416 O  OH  . TYR D 2 238 ? 169.621 162.209 169.386 1.00 113.92 ? 238 TYR B OH  1 
ATOM   10417 N  N   . GLY D 2 239 ? 171.609 168.830 166.027 1.00 115.65 ? 239 GLY B N   1 
ATOM   10418 C  CA  . GLY D 2 239 ? 171.705 169.912 166.997 1.00 115.65 ? 239 GLY B CA  1 
ATOM   10419 C  C   . GLY D 2 239 ? 170.577 170.919 166.872 1.00 115.65 ? 239 GLY B C   1 
ATOM   10420 O  O   . GLY D 2 239 ? 170.016 171.373 167.881 1.00 115.65 ? 239 GLY B O   1 
ATOM   10421 N  N   . GLN D 2 240 ? 170.234 171.292 165.633 1.00 117.57 ? 240 GLN B N   1 
ATOM   10422 C  CA  . GLN D 2 240 ? 169.195 172.288 165.404 1.00 117.57 ? 240 GLN B CA  1 
ATOM   10423 C  C   . GLN D 2 240 ? 167.811 171.758 165.756 1.00 117.57 ? 240 GLN B C   1 
ATOM   10424 O  O   . GLN D 2 240 ? 166.902 172.559 165.977 1.00 117.57 ? 240 GLN B O   1 
ATOM   10425 C  CB  . GLN D 2 240 ? 169.250 172.783 163.955 1.00 117.57 ? 240 GLN B CB  1 
ATOM   10426 C  CG  . GLN D 2 240 ? 168.239 172.168 163.013 1.00 117.57 ? 240 GLN B CG  1 
ATOM   10427 C  CD  . GLN D 2 240 ? 168.419 172.631 161.580 1.00 117.57 ? 240 GLN B CD  1 
ATOM   10428 O  OE1 . GLN D 2 240 ? 169.189 173.550 161.303 1.00 117.57 ? 240 GLN B OE1 1 
ATOM   10429 N  NE2 . GLN D 2 240 ? 167.704 171.996 160.661 1.00 117.57 ? 240 GLN B NE2 1 
ATOM   10430 N  N   . ILE D 2 241 ? 167.608 170.440 165.729 1.00 113.92 ? 241 ILE B N   1 
ATOM   10431 C  CA  . ILE D 2 241 ? 166.362 169.863 166.228 1.00 113.92 ? 241 ILE B CA  1 
ATOM   10432 C  C   . ILE D 2 241 ? 166.416 169.607 167.730 1.00 113.92 ? 241 ILE B C   1 
ATOM   10433 O  O   . ILE D 2 241 ? 165.372 169.639 168.397 1.00 113.92 ? 241 ILE B O   1 
ATOM   10434 C  CB  . ILE D 2 241 ? 166.002 168.580 165.450 1.00 109.97 ? 241 ILE B CB  1 
ATOM   10435 C  CG1 . ILE D 2 241 ? 165.098 168.924 164.270 1.00 109.97 ? 241 ILE B CG1 1 
ATOM   10436 C  CG2 . ILE D 2 241 ? 165.337 167.524 166.338 1.00 109.97 ? 241 ILE B CG2 1 
ATOM   10437 C  CD1 . ILE D 2 241 ? 165.688 169.869 163.315 1.00 109.97 ? 241 ILE B CD1 1 
ATOM   10438 N  N   . PHE D 2 242 ? 167.609 169.446 168.296 1.00 113.92 ? 242 PHE B N   1 
ATOM   10439 C  CA  . PHE D 2 242 ? 167.722 169.094 169.703 1.00 113.92 ? 242 PHE B CA  1 
ATOM   10440 C  C   . PHE D 2 242 ? 167.564 170.310 170.604 1.00 113.92 ? 242 PHE B C   1 
ATOM   10441 O  O   . PHE D 2 242 ? 166.806 170.268 171.579 1.00 113.92 ? 242 PHE B O   1 
ATOM   10442 C  CB  . PHE D 2 242 ? 169.063 168.401 169.943 1.00 113.92 ? 242 PHE B CB  1 
ATOM   10443 C  CG  . PHE D 2 242 ? 169.252 167.913 171.344 1.00 113.92 ? 242 PHE B CG  1 
ATOM   10444 C  CD1 . PHE D 2 242 ? 168.669 166.731 171.763 1.00 113.92 ? 242 PHE B CD1 1 
ATOM   10445 C  CD2 . PHE D 2 242 ? 170.027 168.628 172.240 1.00 113.92 ? 242 PHE B CD2 1 
ATOM   10446 C  CE1 . PHE D 2 242 ? 168.844 166.278 173.053 1.00 113.92 ? 242 PHE B CE1 1 
ATOM   10447 C  CE2 . PHE D 2 242 ? 170.207 168.179 173.530 1.00 113.92 ? 242 PHE B CE2 1 
ATOM   10448 C  CZ  . PHE D 2 242 ? 169.615 167.004 173.938 1.00 113.92 ? 242 PHE B CZ  1 
ATOM   10449 N  N   . LYS D 2 243 ? 168.267 171.403 170.301 1.00 113.92 ? 243 LYS B N   1 
ATOM   10450 C  CA  . LYS D 2 243 ? 168.208 172.561 171.194 1.00 113.92 ? 243 LYS B CA  1 
ATOM   10451 C  C   . LYS D 2 243 ? 166.801 173.140 171.336 1.00 113.92 ? 243 LYS B C   1 
ATOM   10452 O  O   . LYS D 2 243 ? 166.323 173.264 172.480 1.00 113.92 ? 243 LYS B O   1 
ATOM   10453 C  CB  . LYS D 2 243 ? 169.199 173.633 170.721 1.00 113.92 ? 243 LYS B CB  1 
ATOM   10454 C  CG  . LYS D 2 243 ? 169.222 174.878 171.597 1.00 113.92 ? 243 LYS B CG  1 
ATOM   10455 C  CD  . LYS D 2 243 ? 170.298 175.865 171.164 1.00 113.92 ? 243 LYS B CD  1 
ATOM   10456 C  CE  . LYS D 2 243 ? 171.694 175.379 171.504 1.00 113.92 ? 243 LYS B CE  1 
ATOM   10457 N  NZ  . LYS D 2 243 ? 172.699 176.469 171.363 1.00 113.92 ? 243 LYS B NZ  1 
ATOM   10458 N  N   . PRO D 2 244 ? 166.082 173.489 170.259 1.00 113.92 ? 244 PRO B N   1 
ATOM   10459 C  CA  . PRO D 2 244 ? 164.756 174.105 170.451 1.00 113.92 ? 244 PRO B CA  1 
ATOM   10460 C  C   . PRO D 2 244 ? 163.727 173.168 171.051 1.00 113.92 ? 244 PRO B C   1 
ATOM   10461 O  O   . PRO D 2 244 ? 162.925 173.601 171.885 1.00 113.92 ? 244 PRO B O   1 
ATOM   10462 C  CB  . PRO D 2 244 ? 164.360 174.547 169.035 1.00 113.92 ? 244 PRO B CB  1 
ATOM   10463 C  CG  . PRO D 2 244 ? 165.130 173.686 168.148 1.00 113.92 ? 244 PRO B CG  1 
ATOM   10464 C  CD  . PRO D 2 244 ? 166.434 173.427 168.832 1.00 113.92 ? 244 PRO B CD  1 
ATOM   10465 N  N   . ILE D 2 245 ? 163.701 171.905 170.623 1.00 113.92 ? 245 ILE B N   1 
ATOM   10466 C  CA  . ILE D 2 245 ? 162.731 170.957 171.168 1.00 113.92 ? 245 ILE B CA  1 
ATOM   10467 C  C   . ILE D 2 245 ? 162.928 170.806 172.670 1.00 113.92 ? 245 ILE B C   1 
ATOM   10468 O  O   . ILE D 2 245 ? 161.966 170.845 173.446 1.00 113.92 ? 245 ILE B O   1 
ATOM   10469 C  CB  . ILE D 2 245 ? 162.827 169.605 170.440 1.00 101.99 ? 245 ILE B CB  1 
ATOM   10470 C  CG1 . ILE D 2 245 ? 162.338 169.746 168.995 1.00 101.99 ? 245 ILE B CG1 1 
ATOM   10471 C  CG2 . ILE D 2 245 ? 162.044 168.536 171.190 1.00 101.99 ? 245 ILE B CG2 1 
ATOM   10472 C  CD1 . ILE D 2 245 ? 160.896 169.351 168.779 1.00 101.99 ? 245 ILE B CD1 1 
ATOM   10473 N  N   . ILE D 2 246 ? 164.178 170.634 173.103 1.00 113.92 ? 246 ILE B N   1 
ATOM   10474 C  CA  . ILE D 2 246 ? 164.451 170.462 174.526 1.00 113.92 ? 246 ILE B CA  1 
ATOM   10475 C  C   . ILE D 2 246 ? 164.098 171.732 175.291 1.00 113.92 ? 246 ILE B C   1 
ATOM   10476 O  O   . ILE D 2 246 ? 163.523 171.674 176.387 1.00 113.92 ? 246 ILE B O   1 
ATOM   10477 C  CB  . ILE D 2 246 ? 165.916 170.044 174.749 1.00 113.92 ? 246 ILE B CB  1 
ATOM   10478 C  CG1 . ILE D 2 246 ? 166.167 168.653 174.166 1.00 113.92 ? 246 ILE B CG1 1 
ATOM   10479 C  CG2 . ILE D 2 246 ? 166.267 170.069 176.228 1.00 113.92 ? 246 ILE B CG2 1 
ATOM   10480 C  CD1 . ILE D 2 246 ? 165.408 167.550 174.866 1.00 113.92 ? 246 ILE B CD1 1 
ATOM   10481 N  N   . SER D 2 247 ? 164.432 172.898 174.731 1.00 113.92 ? 247 SER B N   1 
ATOM   10482 C  CA  . SER D 2 247 ? 164.109 174.153 175.404 1.00 113.92 ? 247 SER B CA  1 
ATOM   10483 C  C   . SER D 2 247 ? 162.601 174.312 175.575 1.00 113.92 ? 247 SER B C   1 
ATOM   10484 O  O   . SER D 2 247 ? 162.121 174.677 176.655 1.00 113.92 ? 247 SER B O   1 
ATOM   10485 C  CB  . SER D 2 247 ? 164.685 175.330 174.615 1.00 113.92 ? 247 SER B CB  1 
ATOM   10486 O  OG  . SER D 2 247 ? 166.092 175.229 174.494 1.00 113.92 ? 247 SER B OG  1 
ATOM   10487 N  N   . LYS D 2 248 ? 161.840 174.033 174.514 1.00 113.92 ? 248 LYS B N   1 
ATOM   10488 C  CA  . LYS D 2 248 ? 160.386 174.136 174.579 1.00 113.92 ? 248 LYS B CA  1 
ATOM   10489 C  C   . LYS D 2 248 ? 159.798 173.139 175.569 1.00 113.92 ? 248 LYS B C   1 
ATOM   10490 O  O   . LYS D 2 248 ? 158.888 173.476 176.338 1.00 113.92 ? 248 LYS B O   1 
ATOM   10491 C  CB  . LYS D 2 248 ? 159.806 173.916 173.181 1.00 108.99 ? 248 LYS B CB  1 
ATOM   10492 C  CG  . LYS D 2 248 ? 158.299 174.058 173.050 1.00 108.99 ? 248 LYS B CG  1 
ATOM   10493 C  CD  . LYS D 2 248 ? 157.801 175.438 173.429 1.00 108.99 ? 248 LYS B CD  1 
ATOM   10494 C  CE  . LYS D 2 248 ? 156.509 175.751 172.688 1.00 108.99 ? 248 LYS B CE  1 
ATOM   10495 N  NZ  . LYS D 2 248 ? 155.294 175.487 173.500 1.00 108.99 ? 248 LYS B NZ  1 
ATOM   10496 N  N   . VAL D 2 249 ? 160.315 171.907 175.570 1.00 113.92 ? 249 VAL B N   1 
ATOM   10497 C  CA  . VAL D 2 249 ? 159.825 170.891 176.496 1.00 113.92 ? 249 VAL B CA  1 
ATOM   10498 C  C   . VAL D 2 249 ? 160.051 171.329 177.935 1.00 113.92 ? 249 VAL B C   1 
ATOM   10499 O  O   . VAL D 2 249 ? 159.153 171.235 178.780 1.00 113.92 ? 249 VAL B O   1 
ATOM   10500 C  CB  . VAL D 2 249 ? 160.504 169.538 176.209 1.00 113.92 ? 249 VAL B CB  1 
ATOM   10501 C  CG1 . VAL D 2 249 ? 160.329 168.595 177.384 1.00 113.92 ? 249 VAL B CG1 1 
ATOM   10502 C  CG2 . VAL D 2 249 ? 159.933 168.918 174.949 1.00 113.92 ? 249 VAL B CG2 1 
ATOM   10503 N  N   . MET D 2 250 ? 161.253 171.825 178.234 1.00 115.75 ? 250 MET B N   1 
ATOM   10504 C  CA  . MET D 2 250 ? 161.525 172.262 179.598 1.00 115.75 ? 250 MET B CA  1 
ATOM   10505 C  C   . MET D 2 250 ? 160.669 173.465 179.976 1.00 115.75 ? 250 MET B C   1 
ATOM   10506 O  O   . MET D 2 250 ? 160.175 173.547 181.105 1.00 115.75 ? 250 MET B O   1 
ATOM   10507 C  CB  . MET D 2 250 ? 163.000 172.566 179.797 1.00 115.75 ? 250 MET B CB  1 
ATOM   10508 C  CG  . MET D 2 250 ? 163.881 171.331 179.775 1.00 115.75 ? 250 MET B CG  1 
ATOM   10509 S  SD  . MET D 2 250 ? 165.337 171.561 180.797 1.00 115.75 ? 250 MET B SD  1 
ATOM   10510 C  CE  . MET D 2 250 ? 165.363 173.342 180.901 1.00 115.75 ? 250 MET B CE  1 
ATOM   10511 N  N   . GLU D 2 251 ? 160.488 174.410 179.046 1.00 117.96 ? 251 GLU B N   1 
ATOM   10512 C  CA  . GLU D 2 251 ? 159.685 175.592 179.341 1.00 117.96 ? 251 GLU B CA  1 
ATOM   10513 C  C   . GLU D 2 251 ? 158.251 175.202 179.667 1.00 117.96 ? 251 GLU B C   1 
ATOM   10514 O  O   . GLU D 2 251 ? 157.626 175.793 180.554 1.00 117.96 ? 251 GLU B O   1 
ATOM   10515 C  CB  . GLU D 2 251 ? 159.723 176.564 178.162 1.00 117.96 ? 251 GLU B CB  1 
ATOM   10516 N  N   . MET D 2 252 ? 157.700 174.242 178.930 1.00 126.03 ? 252 MET B N   1 
ATOM   10517 C  CA  . MET D 2 252 ? 156.325 173.828 179.173 1.00 126.03 ? 252 MET B CA  1 
ATOM   10518 C  C   . MET D 2 252 ? 156.201 172.845 180.332 1.00 126.03 ? 252 MET B C   1 
ATOM   10519 O  O   . MET D 2 252 ? 155.090 172.638 180.832 1.00 126.03 ? 252 MET B O   1 
ATOM   10520 C  CB  . MET D 2 252 ? 155.718 173.239 177.899 1.00 126.03 ? 252 MET B CB  1 
ATOM   10521 C  CG  . MET D 2 252 ? 155.518 174.286 176.822 1.00 126.03 ? 252 MET B CG  1 
ATOM   10522 S  SD  . MET D 2 252 ? 154.454 175.599 177.457 1.00 126.03 ? 252 MET B SD  1 
ATOM   10523 C  CE  . MET D 2 252 ? 154.749 176.913 176.281 1.00 126.03 ? 252 MET B CE  1 
ATOM   10524 N  N   . TYR D 2 253 ? 157.305 172.235 180.769 1.00 113.92 ? 253 TYR B N   1 
ATOM   10525 C  CA  . TYR D 2 253 ? 157.251 171.157 181.748 1.00 113.92 ? 253 TYR B CA  1 
ATOM   10526 C  C   . TYR D 2 253 ? 157.939 171.447 183.076 1.00 113.92 ? 253 TYR B C   1 
ATOM   10527 O  O   . TYR D 2 253 ? 157.543 170.857 184.082 1.00 113.92 ? 253 TYR B O   1 
ATOM   10528 C  CB  . TYR D 2 253 ? 157.865 169.882 181.151 1.00 113.92 ? 253 TYR B CB  1 
ATOM   10529 C  CG  . TYR D 2 253 ? 157.739 168.656 182.027 1.00 113.92 ? 253 TYR B CG  1 
ATOM   10530 C  CD1 . TYR D 2 253 ? 156.495 168.197 182.439 1.00 113.92 ? 253 TYR B CD1 1 
ATOM   10531 C  CD2 . TYR D 2 253 ? 158.863 167.939 182.415 1.00 113.92 ? 253 TYR B CD2 1 
ATOM   10532 C  CE1 . TYR D 2 253 ? 156.377 167.073 183.229 1.00 113.92 ? 253 TYR B CE1 1 
ATOM   10533 C  CE2 . TYR D 2 253 ? 158.753 166.813 183.205 1.00 113.92 ? 253 TYR B CE2 1 
ATOM   10534 C  CZ  . TYR D 2 253 ? 157.508 166.384 183.607 1.00 113.92 ? 253 TYR B CZ  1 
ATOM   10535 O  OH  . TYR D 2 253 ? 157.395 165.262 184.395 1.00 113.92 ? 253 TYR B OH  1 
ATOM   10536 N  N   . GLN D 2 254 ? 158.938 172.338 183.118 1.00 116.07 ? 254 GLN B N   1 
ATOM   10537 C  CA  . GLN D 2 254 ? 159.668 172.636 184.352 1.00 116.07 ? 254 GLN B CA  1 
ATOM   10538 C  C   . GLN D 2 254 ? 160.249 171.368 184.970 1.00 116.07 ? 254 GLN B C   1 
ATOM   10539 O  O   . GLN D 2 254 ? 159.829 170.970 186.063 1.00 116.07 ? 254 GLN B O   1 
ATOM   10540 C  CB  . GLN D 2 254 ? 158.772 173.329 185.388 1.00 116.07 ? 254 GLN B CB  1 
ATOM   10541 C  CG  . GLN D 2 254 ? 158.019 174.599 184.969 1.00 116.07 ? 254 GLN B CG  1 
ATOM   10542 C  CD  . GLN D 2 254 ? 158.750 175.455 183.951 1.00 116.07 ? 254 GLN B CD  1 
ATOM   10543 O  OE1 . GLN D 2 254 ? 158.868 175.096 182.786 1.00 116.07 ? 254 GLN B OE1 1 
ATOM   10544 N  NE2 . GLN D 2 254 ? 159.252 176.600 184.400 1.00 116.07 ? 254 GLN B NE2 1 
ATOM   10545 N  N   . PRO D 2 255 ? 161.203 170.702 184.318 1.00 113.92 ? 255 PRO B N   1 
ATOM   10546 C  CA  . PRO D 2 255 ? 161.799 169.506 184.922 1.00 113.92 ? 255 PRO B CA  1 
ATOM   10547 C  C   . PRO D 2 255 ? 162.641 169.854 186.138 1.00 113.92 ? 255 PRO B C   1 
ATOM   10548 O  O   . PRO D 2 255 ? 163.168 170.963 186.266 1.00 113.92 ? 255 PRO B O   1 
ATOM   10549 C  CB  . PRO D 2 255 ? 162.668 168.927 183.797 1.00 113.92 ? 255 PRO B CB  1 
ATOM   10550 C  CG  . PRO D 2 255 ? 162.250 169.642 182.551 1.00 113.92 ? 255 PRO B CG  1 
ATOM   10551 C  CD  . PRO D 2 255 ? 161.770 170.982 182.990 1.00 113.92 ? 255 PRO B CD  1 
ATOM   10552 N  N   . SER D 2 256 ? 162.763 168.884 187.043 1.00 113.92 ? 256 SER B N   1 
ATOM   10553 C  CA  . SER D 2 256 ? 163.573 169.051 188.242 1.00 113.92 ? 256 SER B CA  1 
ATOM   10554 C  C   . SER D 2 256 ? 164.915 168.340 188.159 1.00 113.92 ? 256 SER B C   1 
ATOM   10555 O  O   . SER D 2 256 ? 165.891 168.812 188.753 1.00 113.92 ? 256 SER B O   1 
ATOM   10556 C  CB  . SER D 2 256 ? 162.811 168.545 189.472 1.00 103.90 ? 256 SER B CB  1 
ATOM   10557 O  OG  . SER D 2 256 ? 161.745 169.417 189.805 1.00 103.90 ? 256 SER B OG  1 
ATOM   10558 N  N   . ALA D 2 257 ? 164.990 167.224 187.438 1.00 113.92 ? 257 ALA B N   1 
ATOM   10559 C  CA  . ALA D 2 257 ? 166.234 166.470 187.309 1.00 113.92 ? 257 ALA B CA  1 
ATOM   10560 C  C   . ALA D 2 257 ? 166.150 165.647 186.036 1.00 113.92 ? 257 ALA B C   1 
ATOM   10561 O  O   . ALA D 2 257 ? 165.298 164.758 185.934 1.00 113.92 ? 257 ALA B O   1 
ATOM   10562 C  CB  . ALA D 2 257 ? 166.464 165.573 188.524 1.00 113.92 ? 257 ALA B CB  1 
ATOM   10563 N  N   . VAL D 2 258 ? 167.015 165.939 185.069 1.00 113.92 ? 258 VAL B N   1 
ATOM   10564 C  CA  . VAL D 2 258 ? 166.950 165.327 183.750 1.00 113.92 ? 258 VAL B CA  1 
ATOM   10565 C  C   . VAL D 2 258 ? 167.917 164.151 183.672 1.00 113.92 ? 258 VAL B C   1 
ATOM   10566 O  O   . VAL D 2 258 ? 169.032 164.190 184.220 1.00 113.92 ? 258 VAL B O   1 
ATOM   10567 C  CB  . VAL D 2 258 ? 167.219 166.374 182.649 1.00 113.92 ? 258 VAL B CB  1 
ATOM   10568 C  CG1 . VAL D 2 258 ? 168.501 167.128 182.921 1.00 113.92 ? 258 VAL B CG1 1 
ATOM   10569 C  CG2 . VAL D 2 258 ? 167.260 165.721 181.279 1.00 113.92 ? 258 VAL B CG2 1 
ATOM   10570 N  N   . VAL D 2 259 ? 167.479 163.097 182.989 1.00 113.92 ? 259 VAL B N   1 
ATOM   10571 C  CA  . VAL D 2 259 ? 168.248 161.873 182.803 1.00 113.92 ? 259 VAL B CA  1 
ATOM   10572 C  C   . VAL D 2 259 ? 168.562 161.753 181.318 1.00 113.92 ? 259 VAL B C   1 
ATOM   10573 O  O   . VAL D 2 259 ? 167.675 161.452 180.509 1.00 113.92 ? 259 VAL B O   1 
ATOM   10574 C  CB  . VAL D 2 259 ? 167.486 160.644 183.310 1.00 113.92 ? 259 VAL B CB  1 
ATOM   10575 C  CG1 . VAL D 2 259 ? 168.225 159.377 182.948 1.00 113.92 ? 259 VAL B CG1 1 
ATOM   10576 C  CG2 . VAL D 2 259 ? 167.279 160.732 184.811 1.00 113.92 ? 259 VAL B CG2 1 
ATOM   10577 N  N   . LEU D 2 260 ? 169.816 161.998 180.954 1.00 113.92 ? 260 LEU B N   1 
ATOM   10578 C  CA  . LEU D 2 260 ? 170.281 161.912 179.579 1.00 113.92 ? 260 LEU B CA  1 
ATOM   10579 C  C   . LEU D 2 260 ? 170.922 160.548 179.355 1.00 113.92 ? 260 LEU B C   1 
ATOM   10580 O  O   . LEU D 2 260 ? 171.910 160.198 180.019 1.00 113.92 ? 260 LEU B O   1 
ATOM   10581 C  CB  . LEU D 2 260 ? 171.281 163.032 179.290 1.00 113.92 ? 260 LEU B CB  1 
ATOM   10582 C  CG  . LEU D 2 260 ? 171.688 163.313 177.847 1.00 113.92 ? 260 LEU B CG  1 
ATOM   10583 C  CD1 . LEU D 2 260 ? 170.504 163.851 177.088 1.00 113.92 ? 260 LEU B CD1 1 
ATOM   10584 C  CD2 . LEU D 2 260 ? 172.839 164.302 177.803 1.00 113.92 ? 260 LEU B CD2 1 
ATOM   10585 N  N   . GLN D 2 261 ? 170.350 159.769 178.442 1.00 113.92 ? 261 GLN B N   1 
ATOM   10586 C  CA  . GLN D 2 261 ? 170.937 158.496 178.041 1.00 113.92 ? 261 GLN B CA  1 
ATOM   10587 C  C   . GLN D 2 261 ? 171.632 158.739 176.711 1.00 113.92 ? 261 GLN B C   1 
ATOM   10588 O  O   . GLN D 2 261 ? 170.979 158.920 175.681 1.00 113.92 ? 261 GLN B O   1 
ATOM   10589 C  CB  . GLN D 2 261 ? 169.890 157.390 177.954 1.00 113.92 ? 261 GLN B CB  1 
ATOM   10590 C  CG  . GLN D 2 261 ? 170.464 155.992 177.683 1.00 113.92 ? 261 GLN B CG  1 
ATOM   10591 C  CD  . GLN D 2 261 ? 170.463 155.574 176.220 1.00 113.92 ? 261 GLN B CD  1 
ATOM   10592 O  OE1 . GLN D 2 261 ? 170.364 156.399 175.318 1.00 113.92 ? 261 GLN B OE1 1 
ATOM   10593 N  NE2 . GLN D 2 261 ? 170.575 154.271 175.987 1.00 113.92 ? 261 GLN B NE2 1 
ATOM   10594 N  N   . CYS D 2 262 ? 172.958 158.812 176.760 1.00 113.92 ? 262 CYS B N   1 
ATOM   10595 C  CA  . CYS D 2 262 ? 173.783 159.004 175.579 1.00 113.92 ? 262 CYS B CA  1 
ATOM   10596 C  C   . CYS D 2 262 ? 174.174 157.644 175.027 1.00 113.92 ? 262 CYS B C   1 
ATOM   10597 O  O   . CYS D 2 262 ? 174.717 156.805 175.753 1.00 113.92 ? 262 CYS B O   1 
ATOM   10598 C  CB  . CYS D 2 262 ? 175.031 159.825 175.906 1.00 113.92 ? 262 CYS B CB  1 
ATOM   10599 S  SG  . CYS D 2 262 ? 174.674 161.424 176.640 1.00 113.92 ? 262 CYS B SG  1 
ATOM   10600 N  N   . GLY D 2 263 ? 173.886 157.420 173.754 1.00 113.92 ? 263 GLY B N   1 
ATOM   10601 C  CA  . GLY D 2 263 ? 174.258 156.170 173.135 1.00 113.92 ? 263 GLY B CA  1 
ATOM   10602 C  C   . GLY D 2 263 ? 175.264 156.396 172.032 1.00 113.92 ? 263 GLY B C   1 
ATOM   10603 O  O   . GLY D 2 263 ? 174.935 156.966 170.988 1.00 113.92 ? 263 GLY B O   1 
ATOM   10604 N  N   . ALA D 2 264 ? 176.500 155.953 172.258 1.00 113.92 ? 264 ALA B N   1 
ATOM   10605 C  CA  . ALA D 2 264 ? 177.554 156.147 171.274 1.00 113.92 ? 264 ALA B CA  1 
ATOM   10606 C  C   . ALA D 2 264 ? 177.291 155.382 169.987 1.00 113.92 ? 264 ALA B C   1 
ATOM   10607 O  O   . ALA D 2 264 ? 177.963 155.643 168.983 1.00 113.92 ? 264 ALA B O   1 
ATOM   10608 C  CB  . ALA D 2 264 ? 178.903 155.742 171.863 1.00 113.92 ? 264 ALA B CB  1 
ATOM   10609 N  N   . ASP D 2 265 ? 176.335 154.451 169.990 1.00 113.92 ? 265 ASP B N   1 
ATOM   10610 C  CA  . ASP D 2 265 ? 175.888 153.822 168.753 1.00 113.92 ? 265 ASP B CA  1 
ATOM   10611 C  C   . ASP D 2 265 ? 175.255 154.820 167.795 1.00 113.92 ? 265 ASP B C   1 
ATOM   10612 O  O   . ASP D 2 265 ? 174.940 154.453 166.658 1.00 113.92 ? 265 ASP B O   1 
ATOM   10613 C  CB  . ASP D 2 265 ? 174.912 152.685 169.067 1.00 100.38 ? 265 ASP B CB  1 
ATOM   10614 C  CG  . ASP D 2 265 ? 173.828 153.101 170.036 1.00 100.38 ? 265 ASP B CG  1 
ATOM   10615 O  OD1 . ASP D 2 265 ? 173.830 154.274 170.457 1.00 100.38 ? 265 ASP B OD1 1 
ATOM   10616 O  OD2 . ASP D 2 265 ? 172.980 152.253 170.384 1.00 100.38 ? 265 ASP B OD2 1 
ATOM   10617 N  N   . SER D 2 266 ? 175.063 156.066 168.230 1.00 113.92 ? 266 SER B N   1 
ATOM   10618 C  CA  . SER D 2 266 ? 174.603 157.146 167.371 1.00 113.92 ? 266 SER B CA  1 
ATOM   10619 C  C   . SER D 2 266 ? 175.731 157.753 166.551 1.00 113.92 ? 266 SER B C   1 
ATOM   10620 O  O   . SER D 2 266 ? 175.465 158.584 165.678 1.00 113.92 ? 266 SER B O   1 
ATOM   10621 C  CB  . SER D 2 266 ? 173.935 158.237 168.210 1.00 113.92 ? 266 SER B CB  1 
ATOM   10622 O  OG  . SER D 2 266 ? 173.029 157.677 169.143 1.00 113.92 ? 266 SER B OG  1 
ATOM   10623 N  N   . LEU D 2 267 ? 176.979 157.390 166.829 1.00 113.92 ? 267 LEU B N   1 
ATOM   10624 C  CA  . LEU D 2 267 ? 178.102 157.958 166.105 1.00 113.92 ? 267 LEU B CA  1 
ATOM   10625 C  C   . LEU D 2 267 ? 178.201 157.359 164.707 1.00 113.92 ? 267 LEU B C   1 
ATOM   10626 O  O   . LEU D 2 267 ? 177.694 156.270 164.428 1.00 113.92 ? 267 LEU B O   1 
ATOM   10627 C  CB  . LEU D 2 267 ? 179.405 157.722 166.862 1.00 113.92 ? 267 LEU B CB  1 
ATOM   10628 C  CG  . LEU D 2 267 ? 179.931 158.937 167.620 1.00 113.92 ? 267 LEU B CG  1 
ATOM   10629 C  CD1 . LEU D 2 267 ? 179.147 159.112 168.902 1.00 113.92 ? 267 LEU B CD1 1 
ATOM   10630 C  CD2 . LEU D 2 267 ? 181.413 158.785 167.902 1.00 113.92 ? 267 LEU B CD2 1 
ATOM   10631 N  N   . SER D 2 268 ? 178.869 158.092 163.822 1.00 113.92 ? 268 SER B N   1 
ATOM   10632 C  CA  . SER D 2 268 ? 179.095 157.606 162.471 1.00 113.92 ? 268 SER B CA  1 
ATOM   10633 C  C   . SER D 2 268 ? 180.121 156.480 162.473 1.00 113.92 ? 268 SER B C   1 
ATOM   10634 O  O   . SER D 2 268 ? 181.161 156.565 163.131 1.00 113.92 ? 268 SER B O   1 
ATOM   10635 C  CB  . SER D 2 268 ? 179.571 158.743 161.568 1.00 113.92 ? 268 SER B CB  1 
ATOM   10636 O  OG  . SER D 2 268 ? 179.459 158.387 160.202 1.00 113.92 ? 268 SER B OG  1 
ATOM   10637 N  N   . GLY D 2 269 ? 179.824 155.420 161.730 1.00 113.92 ? 269 GLY B N   1 
ATOM   10638 C  CA  . GLY D 2 269 ? 180.715 154.286 161.657 1.00 113.92 ? 269 GLY B CA  1 
ATOM   10639 C  C   . GLY D 2 269 ? 180.486 153.201 162.683 1.00 113.92 ? 269 GLY B C   1 
ATOM   10640 O  O   . GLY D 2 269 ? 181.315 152.286 162.781 1.00 113.92 ? 269 GLY B O   1 
ATOM   10641 N  N   . ASP D 2 270 ? 179.405 153.269 163.459 1.00 111.43 ? 270 ASP B N   1 
ATOM   10642 C  CA  . ASP D 2 270 ? 179.141 152.217 164.429 1.00 111.43 ? 270 ASP B CA  1 
ATOM   10643 C  C   . ASP D 2 270 ? 178.817 150.909 163.718 1.00 111.43 ? 270 ASP B C   1 
ATOM   10644 O  O   . ASP D 2 270 ? 178.286 150.888 162.604 1.00 111.43 ? 270 ASP B O   1 
ATOM   10645 C  CB  . ASP D 2 270 ? 178.012 152.614 165.384 1.00 111.43 ? 270 ASP B CB  1 
ATOM   10646 C  CG  . ASP D 2 270 ? 177.709 151.530 166.420 1.00 111.43 ? 270 ASP B CG  1 
ATOM   10647 O  OD1 . ASP D 2 270 ? 177.396 150.380 166.046 1.00 111.43 ? 270 ASP B OD1 1 
ATOM   10648 O  OD2 . ASP D 2 270 ? 177.850 151.813 167.625 1.00 111.43 ? 270 ASP B OD2 1 
ATOM   10649 N  N   . ARG D 2 271 ? 179.150 149.803 164.387 1.00 109.66 ? 271 ARG B N   1 
ATOM   10650 C  CA  . ARG D 2 271 ? 179.007 148.474 163.814 1.00 109.66 ? 271 ARG B CA  1 
ATOM   10651 C  C   . ARG D 2 271 ? 177.572 147.967 163.829 1.00 109.66 ? 271 ARG B C   1 
ATOM   10652 O  O   . ARG D 2 271 ? 177.308 146.895 163.274 1.00 109.66 ? 271 ARG B O   1 
ATOM   10653 C  CB  . ARG D 2 271 ? 179.914 147.497 164.562 1.00 109.66 ? 271 ARG B CB  1 
ATOM   10654 C  CG  . ARG D 2 271 ? 180.408 146.338 163.724 1.00 109.66 ? 271 ARG B CG  1 
ATOM   10655 C  CD  . ARG D 2 271 ? 181.554 145.626 164.419 1.00 109.66 ? 271 ARG B CD  1 
ATOM   10656 N  NE  . ARG D 2 271 ? 182.755 146.449 164.493 1.00 109.66 ? 271 ARG B NE  1 
ATOM   10657 C  CZ  . ARG D 2 271 ? 183.746 146.247 165.350 1.00 109.66 ? 271 ARG B CZ  1 
ATOM   10658 N  NH1 . ARG D 2 271 ? 183.697 145.274 166.244 1.00 109.66 ? 271 ARG B NH1 1 
ATOM   10659 N  NH2 . ARG D 2 271 ? 184.806 147.049 165.318 1.00 109.66 ? 271 ARG B NH2 1 
ATOM   10660 N  N   . LEU D 2 272 ? 176.653 148.673 164.480 1.00 113.92 ? 272 LEU B N   1 
ATOM   10661 C  CA  . LEU D 2 272 ? 175.232 148.350 164.413 1.00 113.92 ? 272 LEU B CA  1 
ATOM   10662 C  C   . LEU D 2 272 ? 174.377 149.510 163.930 1.00 113.92 ? 272 LEU B C   1 
ATOM   10663 O  O   . LEU D 2 272 ? 173.443 149.296 163.152 1.00 113.92 ? 272 LEU B O   1 
ATOM   10664 C  CB  . LEU D 2 272 ? 174.714 147.844 165.765 1.00 113.92 ? 272 LEU B CB  1 
ATOM   10665 C  CG  . LEU D 2 272 ? 174.757 146.316 165.880 1.00 113.92 ? 272 LEU B CG  1 
ATOM   10666 C  CD1 . LEU D 2 272 ? 174.073 145.821 167.143 1.00 113.92 ? 272 LEU B CD1 1 
ATOM   10667 C  CD2 . LEU D 2 272 ? 174.136 145.674 164.649 1.00 113.92 ? 272 LEU B CD2 1 
ATOM   10668 N  N   . GLY D 2 273 ? 174.657 150.735 164.374 1.00 113.92 ? 273 GLY B N   1 
ATOM   10669 C  CA  . GLY D 2 273 ? 173.816 151.867 164.054 1.00 113.92 ? 273 GLY B CA  1 
ATOM   10670 C  C   . GLY D 2 273 ? 174.051 152.404 162.654 1.00 113.92 ? 273 GLY B C   1 
ATOM   10671 O  O   . GLY D 2 273 ? 174.903 151.934 161.900 1.00 113.92 ? 273 GLY B O   1 
ATOM   10672 N  N   . CYS D 2 274 ? 173.258 153.425 162.303 1.00 113.92 ? 274 CYS B N   1 
ATOM   10673 C  CA  . CYS D 2 274 ? 173.349 154.049 160.989 1.00 113.92 ? 274 CYS B CA  1 
ATOM   10674 C  C   . CYS D 2 274 ? 173.250 155.572 161.049 1.00 113.92 ? 274 CYS B C   1 
ATOM   10675 O  O   . CYS D 2 274 ? 172.953 156.203 160.027 1.00 113.92 ? 274 CYS B O   1 
ATOM   10676 C  CB  . CYS D 2 274 ? 172.262 153.506 160.054 1.00 113.92 ? 274 CYS B CB  1 
ATOM   10677 S  SG  . CYS D 2 274 ? 170.609 153.465 160.780 1.00 113.92 ? 274 CYS B SG  1 
ATOM   10678 N  N   . PHE D 2 275 ? 173.487 156.181 162.208 1.00 113.92 ? 275 PHE B N   1 
ATOM   10679 C  CA  . PHE D 2 275 ? 173.530 157.632 162.293 1.00 113.92 ? 275 PHE B CA  1 
ATOM   10680 C  C   . PHE D 2 275 ? 174.906 158.152 161.887 1.00 113.92 ? 275 PHE B C   1 
ATOM   10681 O  O   . PHE D 2 275 ? 175.893 157.413 161.836 1.00 113.92 ? 275 PHE B O   1 
ATOM   10682 C  CB  . PHE D 2 275 ? 173.192 158.109 163.705 1.00 113.92 ? 275 PHE B CB  1 
ATOM   10683 C  CG  . PHE D 2 275 ? 171.722 158.249 163.971 1.00 113.92 ? 275 PHE B CG  1 
ATOM   10684 C  CD1 . PHE D 2 275 ? 170.790 157.934 162.999 1.00 113.92 ? 275 PHE B CD1 1 
ATOM   10685 C  CD2 . PHE D 2 275 ? 171.272 158.705 165.198 1.00 113.92 ? 275 PHE B CD2 1 
ATOM   10686 C  CE1 . PHE D 2 275 ? 169.436 158.068 163.248 1.00 113.92 ? 275 PHE B CE1 1 
ATOM   10687 C  CE2 . PHE D 2 275 ? 169.923 158.841 165.453 1.00 113.92 ? 275 PHE B CE2 1 
ATOM   10688 C  CZ  . PHE D 2 275 ? 169.004 158.522 164.477 1.00 113.92 ? 275 PHE B CZ  1 
ATOM   10689 N  N   . ASN D 2 276 ? 174.960 159.454 161.595 1.00 113.92 ? 276 ASN B N   1 
ATOM   10690 C  CA  . ASN D 2 276 ? 176.164 160.090 161.073 1.00 113.92 ? 276 ASN B CA  1 
ATOM   10691 C  C   . ASN D 2 276 ? 176.730 161.135 162.029 1.00 113.92 ? 276 ASN B C   1 
ATOM   10692 O  O   . ASN D 2 276 ? 177.502 162.002 161.607 1.00 113.92 ? 276 ASN B O   1 
ATOM   10693 C  CB  . ASN D 2 276 ? 175.873 160.719 159.709 1.00 113.92 ? 276 ASN B CB  1 
ATOM   10694 C  CG  . ASN D 2 276 ? 177.105 160.819 158.835 1.00 113.92 ? 276 ASN B CG  1 
ATOM   10695 O  OD1 . ASN D 2 276 ? 178.163 160.289 159.169 1.00 113.92 ? 276 ASN B OD1 1 
ATOM   10696 N  ND2 . ASN D 2 276 ? 176.972 161.500 157.703 1.00 113.92 ? 276 ASN B ND2 1 
ATOM   10697 N  N   . LEU D 2 277 ? 176.359 161.080 163.305 1.00 113.92 ? 277 LEU B N   1 
ATOM   10698 C  CA  . LEU D 2 277 ? 176.873 162.037 164.276 1.00 113.92 ? 277 LEU B CA  1 
ATOM   10699 C  C   . LEU D 2 277 ? 178.369 161.847 164.498 1.00 113.92 ? 277 LEU B C   1 
ATOM   10700 O  O   . LEU D 2 277 ? 178.874 160.722 164.524 1.00 113.92 ? 277 LEU B O   1 
ATOM   10701 C  CB  . LEU D 2 277 ? 176.135 161.896 165.609 1.00 113.92 ? 277 LEU B CB  1 
ATOM   10702 C  CG  . LEU D 2 277 ? 174.776 162.575 165.785 1.00 113.92 ? 277 LEU B CG  1 
ATOM   10703 C  CD1 . LEU D 2 277 ? 173.717 161.943 164.903 1.00 113.92 ? 277 LEU B CD1 1 
ATOM   10704 C  CD2 . LEU D 2 277 ? 174.350 162.524 167.243 1.00 113.92 ? 277 LEU B CD2 1 
ATOM   10705 N  N   . THR D 2 278 ? 179.076 162.960 164.654 1.00 113.92 ? 278 THR B N   1 
ATOM   10706 C  CA  . THR D 2 278 ? 180.481 162.961 165.033 1.00 113.92 ? 278 THR B CA  1 
ATOM   10707 C  C   . THR D 2 278 ? 180.610 163.159 166.540 1.00 113.92 ? 278 THR B C   1 
ATOM   10708 O  O   . THR D 2 278 ? 179.628 163.378 167.253 1.00 113.92 ? 278 THR B O   1 
ATOM   10709 C  CB  . THR D 2 278 ? 181.257 164.045 164.284 1.00 113.92 ? 278 THR B CB  1 
ATOM   10710 O  OG1 . THR D 2 278 ? 180.761 165.334 164.659 1.00 113.92 ? 278 THR B OG1 1 
ATOM   10711 C  CG2 . THR D 2 278 ? 181.099 163.866 162.784 1.00 113.92 ? 278 THR B CG2 1 
ATOM   10712 N  N   . VAL D 2 279 ? 181.851 163.066 167.020 1.00 113.92 ? 279 VAL B N   1 
ATOM   10713 C  CA  . VAL D 2 279 ? 182.128 163.285 168.439 1.00 113.92 ? 279 VAL B CA  1 
ATOM   10714 C  C   . VAL D 2 279 ? 181.744 164.703 168.854 1.00 113.92 ? 279 VAL B C   1 
ATOM   10715 O  O   . VAL D 2 279 ? 181.102 164.913 169.893 1.00 113.92 ? 279 VAL B O   1 
ATOM   10716 C  CB  . VAL D 2 279 ? 183.605 162.981 168.740 1.00 113.92 ? 279 VAL B CB  1 
ATOM   10717 C  CG1 . VAL D 2 279 ? 183.960 163.429 170.133 1.00 113.92 ? 279 VAL B CG1 1 
ATOM   10718 C  CG2 . VAL D 2 279 ? 183.877 161.493 168.580 1.00 113.92 ? 279 VAL B CG2 1 
ATOM   10719 N  N   . LYS D 2 280 ? 182.124 165.699 168.045 1.00 122.83 ? 280 LYS B N   1 
ATOM   10720 C  CA  . LYS D 2 280 ? 181.740 167.081 168.329 1.00 122.83 ? 280 LYS B CA  1 
ATOM   10721 C  C   . LYS D 2 280 ? 180.228 167.241 168.380 1.00 122.83 ? 280 LYS B C   1 
ATOM   10722 O  O   . LYS D 2 280 ? 179.690 167.883 169.289 1.00 122.83 ? 280 LYS B O   1 
ATOM   10723 C  CB  . LYS D 2 280 ? 182.340 168.019 167.279 1.00 122.83 ? 280 LYS B CB  1 
ATOM   10724 C  CG  . LYS D 2 280 ? 183.763 168.474 167.553 1.00 122.83 ? 280 LYS B CG  1 
ATOM   10725 C  CD  . LYS D 2 280 ? 184.007 168.684 169.043 1.00 122.83 ? 280 LYS B CD  1 
ATOM   10726 C  CE  . LYS D 2 280 ? 183.272 169.922 169.559 1.00 122.83 ? 280 LYS B CE  1 
ATOM   10727 N  NZ  . LYS D 2 280 ? 184.079 171.163 169.393 1.00 122.83 ? 280 LYS B NZ  1 
ATOM   10728 N  N   . GLY D 2 281 ? 179.525 166.678 167.402 1.00 116.52 ? 281 GLY B N   1 
ATOM   10729 C  CA  . GLY D 2 281 ? 178.079 166.797 167.394 1.00 116.52 ? 281 GLY B CA  1 
ATOM   10730 C  C   . GLY D 2 281 ? 177.437 166.100 168.576 1.00 116.52 ? 281 GLY B C   1 
ATOM   10731 O  O   . GLY D 2 281 ? 176.446 166.578 169.130 1.00 116.52 ? 281 GLY B O   1 
ATOM   10732 N  N   . HIS D 2 282 ? 177.993 164.956 168.973 1.00 113.92 ? 282 HIS B N   1 
ATOM   10733 C  CA  . HIS D 2 282 ? 177.431 164.230 170.102 1.00 113.92 ? 282 HIS B CA  1 
ATOM   10734 C  C   . HIS D 2 282 ? 177.668 164.989 171.399 1.00 113.92 ? 282 HIS B C   1 
ATOM   10735 O  O   . HIS D 2 282 ? 176.837 164.926 172.312 1.00 113.92 ? 282 HIS B O   1 
ATOM   10736 C  CB  . HIS D 2 282 ? 178.022 162.823 170.178 1.00 113.92 ? 282 HIS B CB  1 
ATOM   10737 C  CG  . HIS D 2 282 ? 177.125 161.826 170.843 1.00 113.92 ? 282 HIS B CG  1 
ATOM   10738 N  ND1 . HIS D 2 282 ? 176.899 161.812 172.202 1.00 113.92 ? 282 HIS B ND1 1 
ATOM   10739 C  CD2 . HIS D 2 282 ? 176.399 160.804 170.331 1.00 113.92 ? 282 HIS B CD2 1 
ATOM   10740 C  CE1 . HIS D 2 282 ? 176.069 160.828 172.499 1.00 113.92 ? 282 HIS B CE1 1 
ATOM   10741 N  NE2 . HIS D 2 282 ? 175.752 160.200 171.381 1.00 113.92 ? 282 HIS B NE2 1 
ATOM   10742 N  N   . ALA D 2 283 ? 178.787 165.714 171.501 1.00 119.45 ? 283 ALA B N   1 
ATOM   10743 C  CA  . ALA D 2 283 ? 179.024 166.519 172.692 1.00 119.45 ? 283 ALA B CA  1 
ATOM   10744 C  C   . ALA D 2 283 ? 178.272 167.839 172.656 1.00 119.45 ? 283 ALA B C   1 
ATOM   10745 O  O   . ALA D 2 283 ? 178.069 168.463 173.709 1.00 119.45 ? 283 ALA B O   1 
ATOM   10746 C  CB  . ALA D 2 283 ? 180.518 166.813 172.845 1.00 119.45 ? 283 ALA B CB  1 
ATOM   10747 N  N   . LYS D 2 284 ? 177.829 168.262 171.474 1.00 126.46 ? 284 LYS B N   1 
ATOM   10748 C  CA  . LYS D 2 284 ? 177.001 169.455 171.394 1.00 126.46 ? 284 LYS B CA  1 
ATOM   10749 C  C   . LYS D 2 284 ? 175.695 169.266 172.152 1.00 126.46 ? 284 LYS B C   1 
ATOM   10750 O  O   . LYS D 2 284 ? 175.225 170.186 172.827 1.00 126.46 ? 284 LYS B O   1 
ATOM   10751 C  CB  . LYS D 2 284 ? 176.745 169.805 169.928 1.00 126.46 ? 284 LYS B CB  1 
ATOM   10752 C  CG  . LYS D 2 284 ? 175.583 170.747 169.687 1.00 126.46 ? 284 LYS B CG  1 
ATOM   10753 C  CD  . LYS D 2 284 ? 175.547 171.191 168.235 1.00 126.46 ? 284 LYS B CD  1 
ATOM   10754 C  CE  . LYS D 2 284 ? 175.292 170.019 167.303 1.00 126.46 ? 284 LYS B CE  1 
ATOM   10755 N  NZ  . LYS D 2 284 ? 175.490 170.385 165.873 1.00 126.46 ? 284 LYS B NZ  1 
ATOM   10756 N  N   . CYS D 2 285 ? 175.117 168.063 172.090 1.00 119.75 ? 285 CYS B N   1 
ATOM   10757 C  CA  . CYS D 2 285 ? 173.869 167.803 172.802 1.00 119.75 ? 285 CYS B CA  1 
ATOM   10758 C  C   . CYS D 2 285 ? 174.049 167.853 174.316 1.00 119.75 ? 285 CYS B C   1 
ATOM   10759 O  O   . CYS D 2 285 ? 173.226 168.449 175.026 1.00 119.75 ? 285 CYS B O   1 
ATOM   10760 C  CB  . CYS D 2 285 ? 173.307 166.451 172.373 1.00 119.75 ? 285 CYS B CB  1 
ATOM   10761 S  SG  . CYS D 2 285 ? 173.018 166.290 170.598 1.00 119.75 ? 285 CYS B SG  1 
ATOM   10762 N  N   . VAL D 2 286 ? 175.117 167.237 174.834 1.00 113.92 ? 286 VAL B N   1 
ATOM   10763 C  CA  . VAL D 2 286 ? 175.332 167.268 176.278 1.00 113.92 ? 286 VAL B CA  1 
ATOM   10764 C  C   . VAL D 2 286 ? 175.608 168.693 176.736 1.00 113.92 ? 286 VAL B C   1 
ATOM   10765 O  O   . VAL D 2 286 ? 175.115 169.122 177.784 1.00 113.92 ? 286 VAL B O   1 
ATOM   10766 C  CB  . VAL D 2 286 ? 176.437 166.286 176.716 1.00 113.92 ? 286 VAL B CB  1 
ATOM   10767 C  CG1 . VAL D 2 286 ? 177.650 166.395 175.852 1.00 113.92 ? 286 VAL B CG1 1 
ATOM   10768 C  CG2 . VAL D 2 286 ? 176.815 166.529 178.168 1.00 113.92 ? 286 VAL B CG2 1 
ATOM   10769 N  N   . GLU D 2 287 ? 176.376 169.461 175.955 1.00 116.31 ? 287 GLU B N   1 
ATOM   10770 C  CA  . GLU D 2 287 ? 176.613 170.848 176.342 1.00 116.31 ? 287 GLU B CA  1 
ATOM   10771 C  C   . GLU D 2 287 ? 175.322 171.661 176.303 1.00 116.31 ? 287 GLU B C   1 
ATOM   10772 O  O   . GLU D 2 287 ? 175.093 172.510 177.175 1.00 116.31 ? 287 GLU B O   1 
ATOM   10773 C  CB  . GLU D 2 287 ? 177.668 171.477 175.434 1.00 116.31 ? 287 GLU B CB  1 
ATOM   10774 C  CG  . GLU D 2 287 ? 178.593 172.448 176.145 1.00 116.31 ? 287 GLU B CG  1 
ATOM   10775 C  CD  . GLU D 2 287 ? 179.939 172.574 175.464 1.00 116.31 ? 287 GLU B CD  1 
ATOM   10776 O  OE1 . GLU D 2 287 ? 180.004 172.383 174.231 1.00 116.31 ? 287 GLU B OE1 1 
ATOM   10777 O  OE2 . GLU D 2 287 ? 180.934 172.866 176.161 1.00 116.31 ? 287 GLU B OE2 1 
ATOM   10778 N  N   . VAL D 2 288 ? 174.466 171.405 175.310 1.00 113.92 ? 288 VAL B N   1 
ATOM   10779 C  CA  . VAL D 2 288 ? 173.166 172.070 175.240 1.00 113.92 ? 288 VAL B CA  1 
ATOM   10780 C  C   . VAL D 2 288 ? 172.363 171.801 176.504 1.00 113.92 ? 288 VAL B C   1 
ATOM   10781 O  O   . VAL D 2 288 ? 171.799 172.718 177.110 1.00 113.92 ? 288 VAL B O   1 
ATOM   10782 C  CB  . VAL D 2 288 ? 172.398 171.620 173.983 1.00 113.92 ? 288 VAL B CB  1 
ATOM   10783 C  CG1 . VAL D 2 288 ? 170.919 171.940 174.122 1.00 113.92 ? 288 VAL B CG1 1 
ATOM   10784 C  CG2 . VAL D 2 288 ? 172.961 172.296 172.748 1.00 113.92 ? 288 VAL B CG2 1 
ATOM   10785 N  N   . VAL D 2 289 ? 172.293 170.535 176.917 1.00 113.92 ? 289 VAL B N   1 
ATOM   10786 C  CA  . VAL D 2 289 ? 171.555 170.221 178.137 1.00 113.92 ? 289 VAL B CA  1 
ATOM   10787 C  C   . VAL D 2 289 ? 172.226 170.847 179.358 1.00 113.92 ? 289 VAL B C   1 
ATOM   10788 O  O   . VAL D 2 289 ? 171.547 171.224 180.322 1.00 113.92 ? 289 VAL B O   1 
ATOM   10789 C  CB  . VAL D 2 289 ? 171.390 168.698 178.295 1.00 113.92 ? 289 VAL B CB  1 
ATOM   10790 C  CG1 . VAL D 2 289 ? 170.557 168.381 179.523 1.00 113.92 ? 289 VAL B CG1 1 
ATOM   10791 C  CG2 . VAL D 2 289 ? 170.743 168.109 177.059 1.00 113.92 ? 289 VAL B CG2 1 
ATOM   10792 N  N   . LYS D 2 290 ? 173.557 170.982 179.341 1.00 115.67 ? 290 LYS B N   1 
ATOM   10793 C  CA  . LYS D 2 290 ? 174.246 171.655 180.439 1.00 115.67 ? 290 LYS B CA  1 
ATOM   10794 C  C   . LYS D 2 290 ? 173.864 173.126 180.546 1.00 115.67 ? 290 LYS B C   1 
ATOM   10795 O  O   . LYS D 2 290 ? 173.829 173.671 181.655 1.00 115.67 ? 290 LYS B O   1 
ATOM   10796 C  CB  . LYS D 2 290 ? 175.761 171.532 180.281 1.00 115.67 ? 290 LYS B CB  1 
ATOM   10797 C  CG  . LYS D 2 290 ? 176.310 170.129 180.437 1.00 115.67 ? 290 LYS B CG  1 
ATOM   10798 C  CD  . LYS D 2 290 ? 177.618 170.159 181.205 1.00 115.67 ? 290 LYS B CD  1 
ATOM   10799 C  CE  . LYS D 2 290 ? 178.608 171.107 180.546 1.00 115.67 ? 290 LYS B CE  1 
ATOM   10800 N  NZ  . LYS D 2 290 ? 179.914 171.135 181.258 1.00 115.67 ? 290 LYS B NZ  1 
ATOM   10801 N  N   . THR D 2 291 ? 173.608 173.789 179.413 1.00 113.92 ? 291 THR B N   1 
ATOM   10802 C  CA  . THR D 2 291 ? 173.274 175.216 179.462 1.00 113.92 ? 291 THR B CA  1 
ATOM   10803 C  C   . THR D 2 291 ? 172.114 175.492 180.412 1.00 113.92 ? 291 THR B C   1 
ATOM   10804 O  O   . THR D 2 291 ? 172.083 176.531 181.081 1.00 113.92 ? 291 THR B O   1 
ATOM   10805 C  CB  . THR D 2 291 ? 172.942 175.775 178.071 1.00 113.92 ? 291 THR B CB  1 
ATOM   10806 O  OG1 . THR D 2 291 ? 171.546 175.597 177.793 1.00 113.92 ? 291 THR B OG1 1 
ATOM   10807 C  CG2 . THR D 2 291 ? 173.791 175.162 176.984 1.00 113.92 ? 291 THR B CG2 1 
ATOM   10808 N  N   . PHE D 2 292 ? 171.147 174.575 180.482 1.00 113.92 ? 292 PHE B N   1 
ATOM   10809 C  CA  . PHE D 2 292 ? 169.975 174.799 181.321 1.00 113.92 ? 292 PHE B CA  1 
ATOM   10810 C  C   . PHE D 2 292 ? 170.288 174.679 182.809 1.00 113.92 ? 292 PHE B C   1 
ATOM   10811 O  O   . PHE D 2 292 ? 169.482 175.120 183.634 1.00 113.92 ? 292 PHE B O   1 
ATOM   10812 C  CB  . PHE D 2 292 ? 168.870 173.832 180.915 1.00 109.27 ? 292 PHE B CB  1 
ATOM   10813 C  CG  . PHE D 2 292 ? 168.487 173.940 179.464 1.00 109.27 ? 292 PHE B CG  1 
ATOM   10814 C  CD1 . PHE D 2 292 ? 167.550 174.866 179.040 1.00 109.27 ? 292 PHE B CD1 1 
ATOM   10815 C  CD2 . PHE D 2 292 ? 169.048 173.091 178.528 1.00 109.27 ? 292 PHE B CD2 1 
ATOM   10816 C  CE1 . PHE D 2 292 ? 167.196 174.954 177.711 1.00 109.27 ? 292 PHE B CE1 1 
ATOM   10817 C  CE2 . PHE D 2 292 ? 168.696 173.176 177.196 1.00 109.27 ? 292 PHE B CE2 1 
ATOM   10818 C  CZ  . PHE D 2 292 ? 167.769 174.109 176.789 1.00 109.27 ? 292 PHE B CZ  1 
ATOM   10819 N  N   . ASN D 2 293 ? 171.426 174.080 183.162 1.00 113.92 ? 293 ASN B N   1 
ATOM   10820 C  CA  . ASN D 2 293 ? 171.922 174.025 184.542 1.00 113.92 ? 293 ASN B CA  1 
ATOM   10821 C  C   . ASN D 2 293 ? 170.965 173.306 185.495 1.00 113.92 ? 293 ASN B C   1 
ATOM   10822 O  O   . ASN D 2 293 ? 170.582 173.833 186.542 1.00 113.92 ? 293 ASN B O   1 
ATOM   10823 C  CB  . ASN D 2 293 ? 172.242 175.432 185.054 1.00 113.92 ? 293 ASN B CB  1 
ATOM   10824 N  N   . LEU D 2 294 ? 170.574 172.094 185.127 1.00 113.92 ? 294 LEU B N   1 
ATOM   10825 C  CA  . LEU D 2 294 ? 169.777 171.224 185.977 1.00 113.92 ? 294 LEU B CA  1 
ATOM   10826 C  C   . LEU D 2 294 ? 170.548 169.939 186.251 1.00 113.92 ? 294 LEU B C   1 
ATOM   10827 O  O   . LEU D 2 294 ? 171.474 169.595 185.507 1.00 113.92 ? 294 LEU B O   1 
ATOM   10828 C  CB  . LEU D 2 294 ? 168.417 170.900 185.343 1.00 109.44 ? 294 LEU B CB  1 
ATOM   10829 C  CG  . LEU D 2 294 ? 167.454 172.081 185.224 1.00 109.44 ? 294 LEU B CG  1 
ATOM   10830 C  CD1 . LEU D 2 294 ? 166.565 171.927 184.014 1.00 109.44 ? 294 LEU B CD1 1 
ATOM   10831 C  CD2 . LEU D 2 294 ? 166.623 172.214 186.490 1.00 109.44 ? 294 LEU B CD2 1 
ATOM   10832 N  N   . PRO D 2 295 ? 170.219 169.222 187.327 1.00 113.92 ? 295 PRO B N   1 
ATOM   10833 C  CA  . PRO D 2 295 ? 170.870 167.927 187.570 1.00 113.92 ? 295 PRO B CA  1 
ATOM   10834 C  C   . PRO D 2 295 ? 170.750 167.013 186.360 1.00 113.92 ? 295 PRO B C   1 
ATOM   10835 O  O   . PRO D 2 295 ? 169.670 166.829 185.801 1.00 113.92 ? 295 PRO B O   1 
ATOM   10836 C  CB  . PRO D 2 295 ? 170.114 167.372 188.783 1.00 113.92 ? 295 PRO B CB  1 
ATOM   10837 C  CG  . PRO D 2 295 ? 169.555 168.571 189.460 1.00 113.92 ? 295 PRO B CG  1 
ATOM   10838 C  CD  . PRO D 2 295 ? 169.245 169.557 188.380 1.00 113.92 ? 295 PRO B CD  1 
ATOM   10839 N  N   . LEU D 2 296 ? 171.883 166.440 185.958 1.00 113.92 ? 296 LEU B N   1 
ATOM   10840 C  CA  . LEU D 2 296 ? 172.010 165.670 184.720 1.00 113.92 ? 296 LEU B CA  1 
ATOM   10841 C  C   . LEU D 2 296 ? 172.599 164.298 185.025 1.00 113.92 ? 296 LEU B C   1 
ATOM   10842 O  O   . LEU D 2 296 ? 173.804 164.175 185.264 1.00 113.92 ? 296 LEU B O   1 
ATOM   10843 C  CB  . LEU D 2 296 ? 172.867 166.416 183.703 1.00 113.92 ? 296 LEU B CB  1 
ATOM   10844 C  CG  . LEU D 2 296 ? 172.784 165.991 182.233 1.00 113.92 ? 296 LEU B CG  1 
ATOM   10845 C  CD1 . LEU D 2 296 ? 171.389 165.564 181.841 1.00 113.92 ? 296 LEU B CD1 1 
ATOM   10846 C  CD2 . LEU D 2 296 ? 173.289 167.098 181.321 1.00 113.92 ? 296 LEU B CD2 1 
ATOM   10847 N  N   . LEU D 2 297 ? 171.756 163.271 185.022 1.00 113.92 ? 297 LEU B N   1 
ATOM   10848 C  CA  . LEU D 2 297 ? 172.269 161.909 185.057 1.00 113.92 ? 297 LEU B CA  1 
ATOM   10849 C  C   . LEU D 2 297 ? 172.707 161.510 183.653 1.00 113.92 ? 297 LEU B C   1 
ATOM   10850 O  O   . LEU D 2 297 ? 172.069 161.882 182.669 1.00 113.92 ? 297 LEU B O   1 
ATOM   10851 C  CB  . LEU D 2 297 ? 171.211 160.944 185.589 1.00 113.92 ? 297 LEU B CB  1 
ATOM   10852 C  CG  . LEU D 2 297 ? 171.708 159.537 185.919 1.00 113.92 ? 297 LEU B CG  1 
ATOM   10853 C  CD1 . LEU D 2 297 ? 172.839 159.596 186.930 1.00 113.92 ? 297 LEU B CD1 1 
ATOM   10854 C  CD2 . LEU D 2 297 ? 170.569 158.683 186.443 1.00 113.92 ? 297 LEU B CD2 1 
ATOM   10855 N  N   . MET D 2 298 ? 173.808 160.765 183.559 1.00 113.92 ? 298 MET B N   1 
ATOM   10856 C  CA  . MET D 2 298 ? 174.432 160.438 182.273 1.00 113.92 ? 298 MET B CA  1 
ATOM   10857 C  C   . MET D 2 298 ? 174.622 158.931 182.144 1.00 113.92 ? 298 MET B C   1 
ATOM   10858 O  O   . MET D 2 298 ? 175.539 158.364 182.747 1.00 113.92 ? 298 MET B O   1 
ATOM   10859 C  CB  . MET D 2 298 ? 175.775 161.150 182.123 1.00 113.92 ? 298 MET B CB  1 
ATOM   10860 C  CG  . MET D 2 298 ? 175.699 162.607 181.720 1.00 113.92 ? 298 MET B CG  1 
ATOM   10861 S  SD  . MET D 2 298 ? 177.152 163.069 180.760 1.00 113.92 ? 298 MET B SD  1 
ATOM   10862 C  CE  . MET D 2 298 ? 176.479 163.081 179.107 1.00 113.92 ? 298 MET B CE  1 
ATOM   10863 N  N   . LEU D 2 299 ? 173.765 158.279 181.361 1.00 113.92 ? 299 LEU B N   1 
ATOM   10864 C  CA  . LEU D 2 299 ? 173.849 156.835 181.164 1.00 113.92 ? 299 LEU B CA  1 
ATOM   10865 C  C   . LEU D 2 299 ? 174.409 156.534 179.779 1.00 113.92 ? 299 LEU B C   1 
ATOM   10866 O  O   . LEU D 2 299 ? 173.850 156.971 178.771 1.00 113.92 ? 299 LEU B O   1 
ATOM   10867 C  CB  . LEU D 2 299 ? 172.488 156.161 181.341 1.00 113.92 ? 299 LEU B CB  1 
ATOM   10868 C  CG  . LEU D 2 299 ? 171.875 156.171 182.741 1.00 113.92 ? 299 LEU B CG  1 
ATOM   10869 C  CD1 . LEU D 2 299 ? 172.940 155.866 183.782 1.00 113.92 ? 299 LEU B CD1 1 
ATOM   10870 C  CD2 . LEU D 2 299 ? 171.186 157.480 183.036 1.00 113.92 ? 299 LEU B CD2 1 
ATOM   10871 N  N   . GLY D 2 300 ? 175.495 155.765 179.736 1.00 121.16 ? 300 GLY B N   1 
ATOM   10872 C  CA  . GLY D 2 300 ? 176.134 155.424 178.480 1.00 121.16 ? 300 GLY B CA  1 
ATOM   10873 C  C   . GLY D 2 300 ? 175.655 154.101 177.920 1.00 121.16 ? 300 GLY B C   1 
ATOM   10874 O  O   . GLY D 2 300 ? 176.087 153.037 178.373 1.00 121.16 ? 300 GLY B O   1 
ATOM   10875 N  N   . GLY D 2 301 ? 174.774 154.153 176.920 1.00 115.51 ? 301 GLY B N   1 
ATOM   10876 C  CA  . GLY D 2 301 ? 174.222 152.963 176.309 1.00 115.51 ? 301 GLY B CA  1 
ATOM   10877 C  C   . GLY D 2 301 ? 174.829 152.655 174.948 1.00 115.51 ? 301 GLY B C   1 
ATOM   10878 O  O   . GLY D 2 301 ? 175.674 153.377 174.425 1.00 115.51 ? 301 GLY B O   1 
ATOM   10879 N  N   . GLY D 2 302 ? 174.366 151.550 174.374 1.00 113.92 ? 302 GLY B N   1 
ATOM   10880 C  CA  . GLY D 2 302 ? 174.860 151.125 173.073 1.00 113.92 ? 302 GLY B CA  1 
ATOM   10881 C  C   . GLY D 2 302 ? 176.346 150.827 173.121 1.00 113.92 ? 302 GLY B C   1 
ATOM   10882 O  O   . GLY D 2 302 ? 176.812 149.972 173.884 1.00 113.92 ? 302 GLY B O   1 
ATOM   10883 N  N   . GLY D 2 303 ? 177.112 151.536 172.299 1.00 113.92 ? 303 GLY B N   1 
ATOM   10884 C  CA  . GLY D 2 303 ? 178.550 151.381 172.307 1.00 113.92 ? 303 GLY B CA  1 
ATOM   10885 C  C   . GLY D 2 303 ? 179.061 150.093 171.698 1.00 113.92 ? 303 GLY B C   1 
ATOM   10886 O  O   . GLY D 2 303 ? 179.540 149.210 172.414 1.00 113.92 ? 303 GLY B O   1 
ATOM   10887 N  N   . TYR D 2 304 ? 178.956 149.967 170.375 1.00 113.92 ? 304 TYR B N   1 
ATOM   10888 C  CA  . TYR D 2 304 ? 179.296 148.730 169.681 1.00 113.92 ? 304 TYR B CA  1 
ATOM   10889 C  C   . TYR D 2 304 ? 180.601 148.802 168.895 1.00 113.92 ? 304 TYR B C   1 
ATOM   10890 O  O   . TYR D 2 304 ? 181.424 147.888 168.999 1.00 113.92 ? 304 TYR B O   1 
ATOM   10891 C  CB  . TYR D 2 304 ? 178.118 148.344 168.776 1.00 102.31 ? 304 TYR B CB  1 
ATOM   10892 C  CG  . TYR D 2 304 ? 176.825 148.159 169.556 1.00 102.31 ? 304 TYR B CG  1 
ATOM   10893 C  CD1 . TYR D 2 304 ? 176.845 147.814 170.901 1.00 102.31 ? 304 TYR B CD1 1 
ATOM   10894 C  CD2 . TYR D 2 304 ? 175.593 148.389 168.967 1.00 102.31 ? 304 TYR B CD2 1 
ATOM   10895 C  CE1 . TYR D 2 304 ? 175.676 147.662 171.622 1.00 102.31 ? 304 TYR B CE1 1 
ATOM   10896 C  CE2 . TYR D 2 304 ? 174.415 148.238 169.682 1.00 102.31 ? 304 TYR B CE2 1 
ATOM   10897 C  CZ  . TYR D 2 304 ? 174.465 147.876 171.010 1.00 102.31 ? 304 TYR B CZ  1 
ATOM   10898 O  OH  . TYR D 2 304 ? 173.300 147.726 171.727 1.00 102.31 ? 304 TYR B OH  1 
ATOM   10899 N  N   . THR D 2 305 ? 180.828 149.857 168.109 1.00 113.92 ? 305 THR B N   1 
ATOM   10900 C  CA  . THR D 2 305 ? 182.137 150.085 167.486 1.00 113.92 ? 305 THR B CA  1 
ATOM   10901 C  C   . THR D 2 305 ? 183.051 150.662 168.555 1.00 113.92 ? 305 THR B C   1 
ATOM   10902 O  O   . THR D 2 305 ? 182.970 151.845 168.888 1.00 113.92 ? 305 THR B O   1 
ATOM   10903 C  CB  . THR D 2 305 ? 182.038 151.000 166.273 1.00 113.92 ? 305 THR B CB  1 
ATOM   10904 O  OG1 . THR D 2 305 ? 181.377 150.302 165.213 1.00 113.92 ? 305 THR B OG1 1 
ATOM   10905 C  CG2 . THR D 2 305 ? 183.427 151.405 165.802 1.00 113.92 ? 305 THR B CG2 1 
ATOM   10906 N  N   . ILE D 2 306 ? 183.958 149.831 169.065 1.00 113.92 ? 306 ILE B N   1 
ATOM   10907 C  CA  . ILE D 2 306 ? 184.621 150.154 170.322 1.00 113.92 ? 306 ILE B CA  1 
ATOM   10908 C  C   . ILE D 2 306 ? 185.563 151.358 170.221 1.00 113.92 ? 306 ILE B C   1 
ATOM   10909 O  O   . ILE D 2 306 ? 185.732 152.094 171.202 1.00 113.92 ? 306 ILE B O   1 
ATOM   10910 C  CB  . ILE D 2 306 ? 185.327 148.878 170.830 1.00 108.85 ? 306 ILE B CB  1 
ATOM   10911 C  CG1 . ILE D 2 306 ? 186.002 148.078 169.704 1.00 108.85 ? 306 ILE B CG1 1 
ATOM   10912 C  CG2 . ILE D 2 306 ? 184.306 147.927 171.399 1.00 108.85 ? 306 ILE B CG2 1 
ATOM   10913 C  CD1 . ILE D 2 306 ? 187.118 148.751 168.944 1.00 108.85 ? 306 ILE B CD1 1 
ATOM   10914 N  N   . ARG D 2 307 ? 186.121 151.639 169.039 1.00 113.92 ? 307 ARG B N   1 
ATOM   10915 C  CA  . ARG D 2 307 ? 186.993 152.807 168.901 1.00 113.92 ? 307 ARG B CA  1 
ATOM   10916 C  C   . ARG D 2 307 ? 186.211 154.115 168.942 1.00 113.92 ? 307 ARG B C   1 
ATOM   10917 O  O   . ARG D 2 307 ? 186.524 155.012 169.739 1.00 113.92 ? 307 ARG B O   1 
ATOM   10918 C  CB  . ARG D 2 307 ? 187.817 152.686 167.620 1.00 113.92 ? 307 ARG B CB  1 
ATOM   10919 C  CG  . ARG D 2 307 ? 187.096 152.014 166.467 1.00 113.92 ? 307 ARG B CG  1 
ATOM   10920 C  CD  . ARG D 2 307 ? 187.631 152.486 165.129 1.00 113.92 ? 307 ARG B CD  1 
ATOM   10921 N  NE  . ARG D 2 307 ? 187.221 151.596 164.049 1.00 113.92 ? 307 ARG B NE  1 
ATOM   10922 C  CZ  . ARG D 2 307 ? 187.137 151.950 162.775 1.00 113.92 ? 307 ARG B CZ  1 
ATOM   10923 N  NH1 . ARG D 2 307 ? 187.405 153.185 162.382 1.00 113.92 ? 307 ARG B NH1 1 
ATOM   10924 N  NH2 . ARG D 2 307 ? 186.764 151.047 161.873 1.00 113.92 ? 307 ARG B NH2 1 
ATOM   10925 N  N   . ASN D 2 308 ? 185.196 154.246 168.083 1.00 113.92 ? 308 ASN B N   1 
ATOM   10926 C  CA  . ASN D 2 308 ? 184.419 155.480 168.057 1.00 113.92 ? 308 ASN B CA  1 
ATOM   10927 C  C   . ASN D 2 308 ? 183.736 155.703 169.394 1.00 113.92 ? 308 ASN B C   1 
ATOM   10928 O  O   . ASN D 2 308 ? 183.662 156.834 169.884 1.00 113.92 ? 308 ASN B O   1 
ATOM   10929 C  CB  . ASN D 2 308 ? 183.385 155.433 166.933 1.00 113.92 ? 308 ASN B CB  1 
ATOM   10930 C  CG  . ASN D 2 308 ? 184.015 155.462 165.557 1.00 113.92 ? 308 ASN B CG  1 
ATOM   10931 O  OD1 . ASN D 2 308 ? 185.211 155.221 165.405 1.00 113.92 ? 308 ASN B OD1 1 
ATOM   10932 N  ND2 . ASN D 2 308 ? 183.211 155.760 164.544 1.00 113.92 ? 308 ASN B ND2 1 
ATOM   10933 N  N   . VAL D 2 309 ? 183.241 154.625 169.998 1.00 113.92 ? 309 VAL B N   1 
ATOM   10934 C  CA  . VAL D 2 309 ? 182.566 154.720 171.286 1.00 113.92 ? 309 VAL B CA  1 
ATOM   10935 C  C   . VAL D 2 309 ? 183.535 155.178 172.365 1.00 113.92 ? 309 VAL B C   1 
ATOM   10936 O  O   . VAL D 2 309 ? 183.208 156.039 173.190 1.00 113.92 ? 309 VAL B O   1 
ATOM   10937 C  CB  . VAL D 2 309 ? 181.914 153.376 171.639 1.00 113.92 ? 309 VAL B CB  1 
ATOM   10938 C  CG1 . VAL D 2 309 ? 181.350 153.411 173.051 1.00 113.92 ? 309 VAL B CG1 1 
ATOM   10939 C  CG2 . VAL D 2 309 ? 180.841 153.070 170.617 1.00 113.92 ? 309 VAL B CG2 1 
ATOM   10940 N  N   . ALA D 2 310 ? 184.738 154.596 172.391 1.00 113.92 ? 310 ALA B N   1 
ATOM   10941 C  CA  . ALA D 2 310 ? 185.714 155.000 173.396 1.00 113.92 ? 310 ALA B CA  1 
ATOM   10942 C  C   . ALA D 2 310 ? 186.062 156.475 173.258 1.00 113.92 ? 310 ALA B C   1 
ATOM   10943 O  O   . ALA D 2 310 ? 186.061 157.225 174.247 1.00 113.92 ? 310 ALA B O   1 
ATOM   10944 C  CB  . ALA D 2 310 ? 186.969 154.135 173.286 1.00 113.92 ? 310 ALA B CB  1 
ATOM   10945 N  N   . ARG D 2 311 ? 186.329 156.918 172.028 1.00 113.92 ? 311 ARG B N   1 
ATOM   10946 C  CA  . ARG D 2 311 ? 186.674 158.320 171.818 1.00 113.92 ? 311 ARG B CA  1 
ATOM   10947 C  C   . ARG D 2 311 ? 185.519 159.236 172.203 1.00 113.92 ? 311 ARG B C   1 
ATOM   10948 O  O   . ARG D 2 311 ? 185.722 160.261 172.868 1.00 113.92 ? 311 ARG B O   1 
ATOM   10949 C  CB  . ARG D 2 311 ? 187.101 158.543 170.369 1.00 113.92 ? 311 ARG B CB  1 
ATOM   10950 C  CG  . ARG D 2 311 ? 188.260 157.651 169.951 1.00 113.92 ? 311 ARG B CG  1 
ATOM   10951 C  CD  . ARG D 2 311 ? 189.019 158.213 168.765 1.00 113.92 ? 311 ARG B CD  1 
ATOM   10952 N  NE  . ARG D 2 311 ? 188.484 157.739 167.495 1.00 113.92 ? 311 ARG B NE  1 
ATOM   10953 C  CZ  . ARG D 2 311 ? 189.122 156.913 166.678 1.00 113.92 ? 311 ARG B CZ  1 
ATOM   10954 N  NH1 . ARG D 2 311 ? 190.319 156.434 166.977 1.00 113.92 ? 311 ARG B NH1 1 
ATOM   10955 N  NH2 . ARG D 2 311 ? 188.547 156.558 165.533 1.00 113.92 ? 311 ARG B NH2 1 
ATOM   10956 N  N   . CYS D 2 312 ? 184.297 158.881 171.799 1.00 113.92 ? 312 CYS B N   1 
ATOM   10957 C  CA  . CYS D 2 312 ? 183.144 159.719 172.104 1.00 113.92 ? 312 CYS B CA  1 
ATOM   10958 C  C   . CYS D 2 312 ? 182.922 159.833 173.603 1.00 113.92 ? 312 CYS B C   1 
ATOM   10959 O  O   . CYS D 2 312 ? 182.685 160.927 174.117 1.00 113.92 ? 312 CYS B O   1 
ATOM   10960 C  CB  . CYS D 2 312 ? 181.890 159.167 171.431 1.00 113.92 ? 312 CYS B CB  1 
ATOM   10961 S  SG  . CYS D 2 312 ? 180.369 159.936 172.036 1.00 113.92 ? 312 CYS B SG  1 
ATOM   10962 N  N   . TRP D 2 313 ? 182.967 158.710 174.320 1.00 113.92 ? 313 TRP B N   1 
ATOM   10963 C  CA  . TRP D 2 313 ? 182.716 158.768 175.757 1.00 113.92 ? 313 TRP B CA  1 
ATOM   10964 C  C   . TRP D 2 313 ? 183.813 159.531 176.489 1.00 113.92 ? 313 TRP B C   1 
ATOM   10965 O  O   . TRP D 2 313 ? 183.523 160.284 177.428 1.00 113.92 ? 313 TRP B O   1 
ATOM   10966 C  CB  . TRP D 2 313 ? 182.533 157.361 176.323 1.00 113.92 ? 313 TRP B CB  1 
ATOM   10967 C  CG  . TRP D 2 313 ? 181.218 156.752 175.919 1.00 113.92 ? 313 TRP B CG  1 
ATOM   10968 C  CD1 . TRP D 2 313 ? 180.178 157.391 175.307 1.00 113.92 ? 313 TRP B CD1 1 
ATOM   10969 C  CD2 . TRP D 2 313 ? 180.793 155.397 176.117 1.00 113.92 ? 313 TRP B CD2 1 
ATOM   10970 N  NE1 . TRP D 2 313 ? 179.139 156.518 175.102 1.00 113.92 ? 313 TRP B NE1 1 
ATOM   10971 C  CE2 . TRP D 2 313 ? 179.491 155.287 175.590 1.00 113.92 ? 313 TRP B CE2 1 
ATOM   10972 C  CE3 . TRP D 2 313 ? 181.388 154.266 176.683 1.00 113.92 ? 313 TRP B CE3 1 
ATOM   10973 C  CZ2 . TRP D 2 313 ? 178.774 154.093 175.612 1.00 113.92 ? 313 TRP B CZ2 1 
ATOM   10974 C  CZ3 . TRP D 2 313 ? 180.674 153.082 176.704 1.00 113.92 ? 313 TRP B CZ3 1 
ATOM   10975 C  CH2 . TRP D 2 313 ? 179.381 153.005 176.172 1.00 113.92 ? 313 TRP B CH2 1 
ATOM   10976 N  N   . THR D 2 314 ? 185.079 159.371 176.081 1.00 113.92 ? 314 THR B N   1 
ATOM   10977 C  CA  . THR D 2 314 ? 186.125 160.169 176.718 1.00 113.92 ? 314 THR B CA  1 
ATOM   10978 C  C   . THR D 2 314 ? 185.913 161.659 176.449 1.00 113.92 ? 314 THR B C   1 
ATOM   10979 O  O   . THR D 2 314 ? 186.096 162.492 177.348 1.00 113.92 ? 314 THR B O   1 
ATOM   10980 C  CB  . THR D 2 314 ? 187.520 159.685 176.292 1.00 113.92 ? 314 THR B CB  1 
ATOM   10981 O  OG1 . THR D 2 314 ? 188.458 159.964 177.341 1.00 113.92 ? 314 THR B OG1 1 
ATOM   10982 C  CG2 . THR D 2 314 ? 188.007 160.336 175.006 1.00 113.92 ? 314 THR B CG2 1 
ATOM   10983 N  N   . TYR D 2 315 ? 185.523 162.021 175.221 1.00 114.38 ? 315 TYR B N   1 
ATOM   10984 C  CA  . TYR D 2 315 ? 185.256 163.426 174.925 1.00 114.38 ? 315 TYR B CA  1 
ATOM   10985 C  C   . TYR D 2 315 ? 184.074 163.930 175.747 1.00 114.38 ? 315 TYR B C   1 
ATOM   10986 O  O   . TYR D 2 315 ? 184.064 165.081 176.193 1.00 114.38 ? 315 TYR B O   1 
ATOM   10987 C  CB  . TYR D 2 315 ? 185.034 163.641 173.428 1.00 114.38 ? 315 TYR B CB  1 
ATOM   10988 C  CG  . TYR D 2 315 ? 185.076 165.104 173.006 1.00 114.38 ? 315 TYR B CG  1 
ATOM   10989 C  CD1 . TYR D 2 315 ? 184.055 165.986 173.336 1.00 114.38 ? 315 TYR B CD1 1 
ATOM   10990 C  CD2 . TYR D 2 315 ? 186.170 165.609 172.317 1.00 114.38 ? 315 TYR B CD2 1 
ATOM   10991 C  CE1 . TYR D 2 315 ? 184.114 167.317 172.967 1.00 114.38 ? 315 TYR B CE1 1 
ATOM   10992 C  CE2 . TYR D 2 315 ? 186.236 166.936 171.945 1.00 114.38 ? 315 TYR B CE2 1 
ATOM   10993 C  CZ  . TYR D 2 315 ? 185.206 167.786 172.275 1.00 114.38 ? 315 TYR B CZ  1 
ATOM   10994 O  OH  . TYR D 2 315 ? 185.266 169.109 171.908 1.00 114.38 ? 315 TYR B OH  1 
ATOM   10995 N  N   . GLU D 2 316 ? 183.044 163.094 175.915 1.00 113.92 ? 316 GLU B N   1 
ATOM   10996 C  CA  . GLU D 2 316 ? 181.879 163.507 176.690 1.00 113.92 ? 316 GLU B CA  1 
ATOM   10997 C  C   . GLU D 2 316 ? 182.276 163.752 178.135 1.00 113.92 ? 316 GLU B C   1 
ATOM   10998 O  O   . GLU D 2 316 ? 181.779 164.681 178.781 1.00 113.92 ? 316 GLU B O   1 
ATOM   10999 C  CB  . GLU D 2 316 ? 180.792 162.428 176.649 1.00 113.36 ? 316 GLU B CB  1 
ATOM   11000 C  CG  . GLU D 2 316 ? 180.111 162.085 175.313 1.00 113.36 ? 316 GLU B CG  1 
ATOM   11001 C  CD  . GLU D 2 316 ? 179.664 163.273 174.491 1.00 113.36 ? 316 GLU B CD  1 
ATOM   11002 O  OE1 . GLU D 2 316 ? 180.496 164.146 174.190 1.00 113.36 ? 316 GLU B OE1 1 
ATOM   11003 O  OE2 . GLU D 2 316 ? 178.466 163.331 174.142 1.00 113.36 ? 316 GLU B OE2 1 
ATOM   11004 N  N   . THR D 2 317 ? 183.181 162.921 178.652 1.00 113.92 ? 317 THR B N   1 
ATOM   11005 C  CA  . THR D 2 317 ? 183.727 163.139 179.986 1.00 113.92 ? 317 THR B CA  1 
ATOM   11006 C  C   . THR D 2 317 ? 184.489 164.458 180.056 1.00 113.92 ? 317 THR B C   1 
ATOM   11007 O  O   . THR D 2 317 ? 184.371 165.208 181.034 1.00 113.92 ? 317 THR B O   1 
ATOM   11008 C  CB  . THR D 2 317 ? 184.630 161.965 180.360 1.00 113.92 ? 317 THR B CB  1 
ATOM   11009 O  OG1 . THR D 2 317 ? 183.870 160.751 180.321 1.00 113.92 ? 317 THR B OG1 1 
ATOM   11010 C  CG2 . THR D 2 317 ? 185.201 162.147 181.742 1.00 113.92 ? 317 THR B CG2 1 
ATOM   11011 N  N   . ALA D 2 318 ? 185.259 164.766 179.009 1.00 123.55 ? 318 ALA B N   1 
ATOM   11012 C  CA  . ALA D 2 318 ? 185.963 166.047 178.954 1.00 123.55 ? 318 ALA B CA  1 
ATOM   11013 C  C   . ALA D 2 318 ? 184.983 167.215 178.971 1.00 123.55 ? 318 ALA B C   1 
ATOM   11014 O  O   . ALA D 2 318 ? 185.207 168.213 179.666 1.00 123.55 ? 318 ALA B O   1 
ATOM   11015 C  CB  . ALA D 2 318 ? 186.849 166.106 177.711 1.00 123.55 ? 318 ALA B CB  1 
ATOM   11016 N  N   . VAL D 2 319 ? 183.900 167.109 178.200 1.00 117.40 ? 319 VAL B N   1 
ATOM   11017 C  CA  . VAL D 2 319 ? 182.879 168.154 178.183 1.00 117.40 ? 319 VAL B CA  1 
ATOM   11018 C  C   . VAL D 2 319 ? 182.276 168.308 179.570 1.00 117.40 ? 319 VAL B C   1 
ATOM   11019 O  O   . VAL D 2 319 ? 182.076 169.426 180.062 1.00 117.40 ? 319 VAL B O   1 
ATOM   11020 C  CB  . VAL D 2 319 ? 181.802 167.843 177.127 1.00 117.40 ? 319 VAL B CB  1 
ATOM   11021 C  CG1 . VAL D 2 319 ? 180.555 168.678 177.372 1.00 117.40 ? 319 VAL B CG1 1 
ATOM   11022 C  CG2 . VAL D 2 319 ? 182.339 168.106 175.740 1.00 117.40 ? 319 VAL B CG2 1 
ATOM   11023 N  N   . ALA D 2 320 ? 181.970 167.182 180.219 1.00 126.62 ? 320 ALA B N   1 
ATOM   11024 C  CA  . ALA D 2 320 ? 181.466 167.212 181.585 1.00 126.62 ? 320 ALA B CA  1 
ATOM   11025 C  C   . ALA D 2 320 ? 182.443 167.900 182.527 1.00 126.62 ? 320 ALA B C   1 
ATOM   11026 O  O   . ALA D 2 320 ? 182.024 168.517 183.512 1.00 126.62 ? 320 ALA B O   1 
ATOM   11027 C  CB  . ALA D 2 320 ? 181.193 165.790 182.070 1.00 126.62 ? 320 ALA B CB  1 
ATOM   11028 N  N   . LEU D 2 321 ? 183.742 167.818 182.242 1.00 138.26 ? 321 LEU B N   1 
ATOM   11029 C  CA  . LEU D 2 321 ? 184.732 168.484 183.078 1.00 138.26 ? 321 LEU B CA  1 
ATOM   11030 C  C   . LEU D 2 321 ? 185.015 169.911 182.627 1.00 138.26 ? 321 LEU B C   1 
ATOM   11031 O  O   . LEU D 2 321 ? 185.713 170.641 183.338 1.00 138.26 ? 321 LEU B O   1 
ATOM   11032 C  CB  . LEU D 2 321 ? 186.042 167.682 183.082 1.00 138.26 ? 321 LEU B CB  1 
ATOM   11033 C  CG  . LEU D 2 321 ? 187.020 167.878 184.246 1.00 138.26 ? 321 LEU B CG  1 
ATOM   11034 C  CD1 . LEU D 2 321 ? 187.523 166.529 184.720 1.00 138.26 ? 321 LEU B CD1 1 
ATOM   11035 C  CD2 . LEU D 2 321 ? 188.189 168.786 183.895 1.00 138.26 ? 321 LEU B CD2 1 
ATOM   11036 N  N   . ASP D 2 322 ? 184.462 170.331 181.487 1.00 140.13 ? 322 ASP B N   1 
ATOM   11037 C  CA  . ASP D 2 322 ? 184.693 171.662 180.924 1.00 140.13 ? 322 ASP B CA  1 
ATOM   11038 C  C   . ASP D 2 322 ? 186.188 171.918 180.731 1.00 140.13 ? 322 ASP B C   1 
ATOM   11039 O  O   . ASP D 2 322 ? 186.713 172.983 181.062 1.00 140.13 ? 322 ASP B O   1 
ATOM   11040 C  CB  . ASP D 2 322 ? 184.051 172.750 181.790 1.00 140.13 ? 322 ASP B CB  1 
ATOM   11041 N  N   . CYS D 2 323 ? 186.875 170.917 180.188 1.00 139.28 ? 323 CYS B N   1 
ATOM   11042 C  CA  . CYS D 2 323 ? 188.304 170.962 179.914 1.00 139.28 ? 323 CYS B CA  1 
ATOM   11043 C  C   . CYS D 2 323 ? 188.559 170.822 178.419 1.00 139.28 ? 323 CYS B C   1 
ATOM   11044 O  O   . CYS D 2 323 ? 187.645 170.579 177.626 1.00 139.28 ? 323 CYS B O   1 
ATOM   11045 C  CB  . CYS D 2 323 ? 189.052 169.863 180.679 1.00 139.28 ? 323 CYS B CB  1 
ATOM   11046 S  SG  . CYS D 2 323 ? 188.578 168.184 180.216 1.00 139.28 ? 323 CYS B SG  1 
ATOM   11047 N  N   . GLU D 2 324 ? 189.823 170.987 178.040 1.00 139.70 ? 324 GLU B N   1 
ATOM   11048 C  CA  . GLU D 2 324 ? 190.250 170.920 176.650 1.00 139.70 ? 324 GLU B CA  1 
ATOM   11049 C  C   . GLU D 2 324 ? 191.147 169.702 176.466 1.00 139.70 ? 324 GLU B C   1 
ATOM   11050 O  O   . GLU D 2 324 ? 192.052 169.465 177.274 1.00 139.70 ? 324 GLU B O   1 
ATOM   11051 C  CB  . GLU D 2 324 ? 190.993 172.194 176.242 1.00 139.70 ? 324 GLU B CB  1 
ATOM   11052 N  N   . ILE D 2 325 ? 190.894 168.937 175.409 1.00 133.16 ? 325 ILE B N   1 
ATOM   11053 C  CA  . ILE D 2 325 ? 191.679 167.745 175.095 1.00 133.16 ? 325 ILE B CA  1 
ATOM   11054 C  C   . ILE D 2 325 ? 192.173 167.825 173.653 1.00 133.16 ? 325 ILE B C   1 
ATOM   11055 O  O   . ILE D 2 325 ? 191.388 168.114 172.739 1.00 133.16 ? 325 ILE B O   1 
ATOM   11056 C  CB  . ILE D 2 325 ? 190.876 166.458 175.358 1.00 133.16 ? 325 ILE B CB  1 
ATOM   11057 C  CG1 . ILE D 2 325 ? 189.655 166.357 174.439 1.00 133.16 ? 325 ILE B CG1 1 
ATOM   11058 C  CG2 . ILE D 2 325 ? 190.462 166.373 176.822 1.00 133.16 ? 325 ILE B CG2 1 
ATOM   11059 C  CD1 . ILE D 2 325 ? 188.783 165.154 174.713 1.00 133.16 ? 325 ILE B CD1 1 
ATOM   11060 N  N   . PRO D 2 326 ? 193.470 167.632 173.413 1.00 134.99 ? 326 PRO B N   1 
ATOM   11061 C  CA  . PRO D 2 326 ? 193.989 167.722 172.043 1.00 134.99 ? 326 PRO B CA  1 
ATOM   11062 C  C   . PRO D 2 326 ? 193.415 166.643 171.136 1.00 134.99 ? 326 PRO B C   1 
ATOM   11063 O  O   . PRO D 2 326 ? 193.065 165.546 171.574 1.00 134.99 ? 326 PRO B O   1 
ATOM   11064 C  CB  . PRO D 2 326 ? 195.502 167.548 172.222 1.00 134.99 ? 326 PRO B CB  1 
ATOM   11065 C  CG  . PRO D 2 326 ? 195.764 167.886 173.655 1.00 134.99 ? 326 PRO B CG  1 
ATOM   11066 C  CD  . PRO D 2 326 ? 194.544 167.455 174.404 1.00 134.99 ? 326 PRO B CD  1 
ATOM   11067 N  N   . ASN D 2 327 ? 193.324 166.980 169.847 1.00 134.49 ? 327 ASN B N   1 
ATOM   11068 C  CA  . ASN D 2 327 ? 192.840 166.032 168.847 1.00 134.49 ? 327 ASN B CA  1 
ATOM   11069 C  C   . ASN D 2 327 ? 193.798 164.855 168.683 1.00 134.49 ? 327 ASN B C   1 
ATOM   11070 O  O   . ASN D 2 327 ? 193.362 163.711 168.513 1.00 134.49 ? 327 ASN B O   1 
ATOM   11071 C  CB  . ASN D 2 327 ? 192.631 166.753 167.514 1.00 134.49 ? 327 ASN B CB  1 
ATOM   11072 C  CG  . ASN D 2 327 ? 192.086 165.842 166.428 1.00 134.49 ? 327 ASN B CG  1 
ATOM   11073 O  OD1 . ASN D 2 327 ? 191.548 164.770 166.707 1.00 134.49 ? 327 ASN B OD1 1 
ATOM   11074 N  ND2 . ASN D 2 327 ? 192.222 166.270 165.178 1.00 134.49 ? 327 ASN B ND2 1 
ATOM   11075 N  N   . GLU D 2 328 ? 195.102 165.116 168.724 1.00 147.37 ? 328 GLU B N   1 
ATOM   11076 C  CA  . GLU D 2 328 ? 196.109 164.072 168.551 1.00 147.37 ? 328 GLU B CA  1 
ATOM   11077 C  C   . GLU D 2 328 ? 196.130 163.151 169.767 1.00 147.37 ? 328 GLU B C   1 
ATOM   11078 O  O   . GLU D 2 328 ? 196.538 163.561 170.859 1.00 147.37 ? 328 GLU B O   1 
ATOM   11079 C  CB  . GLU D 2 328 ? 197.479 164.699 168.319 1.00 147.37 ? 328 GLU B CB  1 
ATOM   11080 C  CG  . GLU D 2 328 ? 197.674 165.291 166.927 1.00 147.37 ? 328 GLU B CG  1 
ATOM   11081 C  CD  . GLU D 2 328 ? 196.917 166.591 166.727 1.00 147.37 ? 328 GLU B CD  1 
ATOM   11082 O  OE1 . GLU D 2 328 ? 196.493 167.196 167.735 1.00 147.37 ? 328 GLU B OE1 1 
ATOM   11083 O  OE2 . GLU D 2 328 ? 196.742 167.005 165.562 1.00 147.37 ? 328 GLU B OE2 1 
ATOM   11084 N  N   . LEU D 2 329 ? 195.681 161.913 169.582 1.00 136.26 ? 329 LEU B N   1 
ATOM   11085 C  CA  . LEU D 2 329 ? 195.610 160.964 170.689 1.00 136.26 ? 329 LEU B CA  1 
ATOM   11086 C  C   . LEU D 2 329 ? 197.000 160.584 171.179 1.00 136.26 ? 329 LEU B C   1 
ATOM   11087 O  O   . LEU D 2 329 ? 197.870 160.253 170.366 1.00 136.26 ? 329 LEU B O   1 
ATOM   11088 C  CB  . LEU D 2 329 ? 194.892 159.681 170.267 1.00 136.26 ? 329 LEU B CB  1 
ATOM   11089 C  CG  . LEU D 2 329 ? 193.435 159.645 169.842 1.00 136.26 ? 329 LEU B CG  1 
ATOM   11090 C  CD1 . LEU D 2 329 ? 193.103 158.287 169.270 1.00 136.26 ? 329 LEU B CD1 1 
ATOM   11091 C  CD2 . LEU D 2 329 ? 192.636 159.849 171.087 1.00 136.26 ? 329 LEU B CD2 1 
ATOM   11092 N  N   . PRO D 2 330 ? 197.249 160.613 172.484 1.00 152.68 ? 330 PRO B N   1 
ATOM   11093 C  CA  . PRO D 2 330 ? 198.545 160.160 172.986 1.00 152.68 ? 330 PRO B CA  1 
ATOM   11094 C  C   . PRO D 2 330 ? 198.591 158.645 172.893 1.00 152.68 ? 330 PRO B C   1 
ATOM   11095 O  O   . PRO D 2 330 ? 197.560 157.974 172.988 1.00 152.68 ? 330 PRO B O   1 
ATOM   11096 C  CB  . PRO D 2 330 ? 198.556 160.642 174.439 1.00 152.68 ? 330 PRO B CB  1 
ATOM   11097 C  CG  . PRO D 2 330 ? 197.110 160.679 174.816 1.00 152.68 ? 330 PRO B CG  1 
ATOM   11098 C  CD  . PRO D 2 330 ? 196.374 161.096 173.567 1.00 152.68 ? 330 PRO B CD  1 
ATOM   11099 N  N   . TYR D 2 331 ? 199.790 158.105 172.668 1.00 176.64 ? 331 TYR B N   1 
ATOM   11100 C  CA  . TYR D 2 331 ? 199.925 156.658 172.528 1.00 176.64 ? 331 TYR B CA  1 
ATOM   11101 C  C   . TYR D 2 331 ? 199.296 155.968 173.732 1.00 176.64 ? 331 TYR B C   1 
ATOM   11102 O  O   . TYR D 2 331 ? 199.795 156.080 174.857 1.00 176.64 ? 331 TYR B O   1 
ATOM   11103 C  CB  . TYR D 2 331 ? 201.393 156.256 172.374 1.00 176.64 ? 331 TYR B CB  1 
ATOM   11104 C  CG  . TYR D 2 331 ? 201.608 154.760 172.321 1.00 176.64 ? 331 TYR B CG  1 
ATOM   11105 C  CD1 . TYR D 2 331 ? 201.363 154.049 171.153 1.00 176.64 ? 331 TYR B CD1 1 
ATOM   11106 C  CD2 . TYR D 2 331 ? 202.050 154.058 173.434 1.00 176.64 ? 331 TYR B CD2 1 
ATOM   11107 C  CE1 . TYR D 2 331 ? 201.553 152.682 171.094 1.00 176.64 ? 331 TYR B CE1 1 
ATOM   11108 C  CE2 . TYR D 2 331 ? 202.243 152.690 173.385 1.00 176.64 ? 331 TYR B CE2 1 
ATOM   11109 C  CZ  . TYR D 2 331 ? 201.993 152.007 172.213 1.00 176.64 ? 331 TYR B CZ  1 
ATOM   11110 O  OH  . TYR D 2 331 ? 202.186 150.646 172.159 1.00 176.64 ? 331 TYR B OH  1 
ATOM   11111 N  N   . ASN D 2 332 ? 198.197 155.255 173.500 1.00 161.53 ? 332 ASN B N   1 
ATOM   11112 C  CA  . ASN D 2 332 ? 197.421 154.644 174.563 1.00 161.53 ? 332 ASN B CA  1 
ATOM   11113 C  C   . ASN D 2 332 ? 197.688 153.140 174.604 1.00 161.53 ? 332 ASN B C   1 
ATOM   11114 O  O   . ASN D 2 332 ? 198.499 152.602 173.847 1.00 161.53 ? 332 ASN B O   1 
ATOM   11115 C  CB  . ASN D 2 332 ? 195.936 154.965 174.338 1.00 161.53 ? 332 ASN B CB  1 
ATOM   11116 C  CG  . ASN D 2 332 ? 195.108 154.921 175.614 1.00 161.53 ? 332 ASN B CG  1 
ATOM   11117 O  OD1 . ASN D 2 332 ? 194.882 155.951 176.248 1.00 161.53 ? 332 ASN B OD1 1 
ATOM   11118 N  ND2 . ASN D 2 332 ? 194.596 153.745 175.956 1.00 161.53 ? 332 ASN B ND2 1 
ATOM   11119 N  N   . ASP D 2 333 ? 196.990 152.455 175.511 1.00 153.69 ? 333 ASP B N   1 
ATOM   11120 C  CA  . ASP D 2 333 ? 197.113 151.006 175.626 1.00 153.69 ? 333 ASP B CA  1 
ATOM   11121 C  C   . ASP D 2 333 ? 196.589 150.306 174.379 1.00 153.69 ? 333 ASP B C   1 
ATOM   11122 O  O   . ASP D 2 333 ? 197.136 149.275 173.968 1.00 153.69 ? 333 ASP B O   1 
ATOM   11123 C  CB  . ASP D 2 333 ? 196.365 150.538 176.880 1.00 153.69 ? 333 ASP B CB  1 
ATOM   11124 C  CG  . ASP D 2 333 ? 196.664 149.092 177.257 1.00 153.69 ? 333 ASP B CG  1 
ATOM   11125 O  OD1 . ASP D 2 333 ? 196.799 148.227 176.370 1.00 153.69 ? 333 ASP B OD1 1 
ATOM   11126 O  OD2 . ASP D 2 333 ? 196.763 148.820 178.472 1.00 153.69 ? 333 ASP B OD2 1 
ATOM   11127 N  N   . TYR D 2 334 ? 195.564 150.869 173.740 1.00 143.45 ? 334 TYR B N   1 
ATOM   11128 C  CA  . TYR D 2 334 ? 194.915 150.259 172.586 1.00 143.45 ? 334 TYR B CA  1 
ATOM   11129 C  C   . TYR D 2 334 ? 195.100 151.101 171.328 1.00 143.45 ? 334 TYR B C   1 
ATOM   11130 O  O   . TYR D 2 334 ? 194.220 151.139 170.465 1.00 143.45 ? 334 TYR B O   1 
ATOM   11131 C  CB  . TYR D 2 334 ? 193.428 150.024 172.860 1.00 143.45 ? 334 TYR B CB  1 
ATOM   11132 C  CG  . TYR D 2 334 ? 193.120 149.513 174.254 1.00 143.45 ? 334 TYR B CG  1 
ATOM   11133 C  CD1 . TYR D 2 334 ? 193.036 150.382 175.336 1.00 143.45 ? 334 TYR B CD1 1 
ATOM   11134 C  CD2 . TYR D 2 334 ? 192.919 148.159 174.487 1.00 143.45 ? 334 TYR B CD2 1 
ATOM   11135 C  CE1 . TYR D 2 334 ? 192.760 149.917 176.607 1.00 143.45 ? 334 TYR B CE1 1 
ATOM   11136 C  CE2 . TYR D 2 334 ? 192.641 147.686 175.754 1.00 143.45 ? 334 TYR B CE2 1 
ATOM   11137 C  CZ  . TYR D 2 334 ? 192.563 148.568 176.810 1.00 143.45 ? 334 TYR B CZ  1 
ATOM   11138 O  OH  . TYR D 2 334 ? 192.287 148.100 178.073 1.00 143.45 ? 334 TYR B OH  1 
ATOM   11139 N  N   . PHE D 2 335 ? 196.237 151.795 171.225 1.00 148.67 ? 335 PHE B N   1 
ATOM   11140 C  CA  . PHE D 2 335 ? 196.488 152.655 170.073 1.00 148.67 ? 335 PHE B CA  1 
ATOM   11141 C  C   . PHE D 2 335 ? 196.425 151.876 168.766 1.00 148.67 ? 335 PHE B C   1 
ATOM   11142 O  O   . PHE D 2 335 ? 196.009 152.424 167.739 1.00 148.67 ? 335 PHE B O   1 
ATOM   11143 C  CB  . PHE D 2 335 ? 197.850 153.340 170.230 1.00 148.67 ? 335 PHE B CB  1 
ATOM   11144 C  CG  . PHE D 2 335 ? 198.102 154.447 169.240 1.00 148.67 ? 335 PHE B CG  1 
ATOM   11145 C  CD1 . PHE D 2 335 ? 198.492 154.166 167.940 1.00 148.67 ? 335 PHE B CD1 1 
ATOM   11146 C  CD2 . PHE D 2 335 ? 197.958 155.771 169.616 1.00 148.67 ? 335 PHE B CD2 1 
ATOM   11147 C  CE1 . PHE D 2 335 ? 198.725 155.181 167.035 1.00 148.67 ? 335 PHE B CE1 1 
ATOM   11148 C  CE2 . PHE D 2 335 ? 198.192 156.791 168.714 1.00 148.67 ? 335 PHE B CE2 1 
ATOM   11149 C  CZ  . PHE D 2 335 ? 198.576 156.494 167.422 1.00 148.67 ? 335 PHE B CZ  1 
ATOM   11150 N  N   . GLU D 2 336 ? 196.834 150.603 168.786 1.00 159.08 ? 336 GLU B N   1 
ATOM   11151 C  CA  . GLU D 2 336 ? 196.774 149.778 167.583 1.00 159.08 ? 336 GLU B CA  1 
ATOM   11152 C  C   . GLU D 2 336 ? 195.367 149.744 166.998 1.00 159.08 ? 336 GLU B C   1 
ATOM   11153 O  O   . GLU D 2 336 ? 195.192 149.746 165.774 1.00 159.08 ? 336 GLU B O   1 
ATOM   11154 C  CB  . GLU D 2 336 ? 197.257 148.361 167.896 1.00 159.08 ? 336 GLU B CB  1 
ATOM   11155 N  N   . TYR D 2 337 ? 194.349 149.706 167.861 1.00 151.76 ? 337 TYR B N   1 
ATOM   11156 C  CA  . TYR D 2 337 ? 192.972 149.777 167.384 1.00 151.76 ? 337 TYR B CA  1 
ATOM   11157 C  C   . TYR D 2 337 ? 192.675 151.129 166.746 1.00 151.76 ? 337 TYR B C   1 
ATOM   11158 O  O   . TYR D 2 337 ? 192.000 151.200 165.713 1.00 151.76 ? 337 TYR B O   1 
ATOM   11159 C  CB  . TYR D 2 337 ? 192.002 149.499 168.533 1.00 151.76 ? 337 TYR B CB  1 
ATOM   11160 N  N   . PHE D 2 338 ? 193.170 152.214 167.351 1.00 140.20 ? 338 PHE B N   1 
ATOM   11161 C  CA  . PHE D 2 338 ? 192.914 153.552 166.829 1.00 140.20 ? 338 PHE B CA  1 
ATOM   11162 C  C   . PHE D 2 338 ? 193.506 153.758 165.441 1.00 140.20 ? 338 PHE B C   1 
ATOM   11163 O  O   . PHE D 2 338 ? 193.042 154.636 164.705 1.00 140.20 ? 338 PHE B O   1 
ATOM   11164 C  CB  . PHE D 2 338 ? 193.468 154.602 167.792 1.00 140.20 ? 338 PHE B CB  1 
ATOM   11165 C  CG  . PHE D 2 338 ? 192.873 154.534 169.170 1.00 140.20 ? 338 PHE B CG  1 
ATOM   11166 C  CD1 . PHE D 2 338 ? 191.574 154.092 169.360 1.00 140.20 ? 338 PHE B CD1 1 
ATOM   11167 C  CD2 . PHE D 2 338 ? 193.616 154.903 170.277 1.00 140.20 ? 338 PHE B CD2 1 
ATOM   11168 C  CE1 . PHE D 2 338 ? 191.026 154.027 170.626 1.00 140.20 ? 338 PHE B CE1 1 
ATOM   11169 C  CE2 . PHE D 2 338 ? 193.074 154.840 171.546 1.00 140.20 ? 338 PHE B CE2 1 
ATOM   11170 C  CZ  . PHE D 2 338 ? 191.778 154.400 171.720 1.00 140.20 ? 338 PHE B CZ  1 
ATOM   11171 N  N   . GLY D 2 339 ? 194.514 152.975 165.069 1.00 152.60 ? 339 GLY B N   1 
ATOM   11172 C  CA  . GLY D 2 339 ? 195.000 152.944 163.712 1.00 152.60 ? 339 GLY B CA  1 
ATOM   11173 C  C   . GLY D 2 339 ? 195.937 154.086 163.371 1.00 152.60 ? 339 GLY B C   1 
ATOM   11174 O  O   . GLY D 2 339 ? 196.431 154.807 164.244 1.00 152.60 ? 339 GLY B O   1 
ATOM   11175 N  N   . PRO D 2 340 ? 196.198 154.263 162.073 1.00 166.01 ? 340 PRO B N   1 
ATOM   11176 C  CA  . PRO D 2 340 ? 197.176 155.276 161.646 1.00 166.01 ? 340 PRO B CA  1 
ATOM   11177 C  C   . PRO D 2 340 ? 196.740 156.707 161.906 1.00 166.01 ? 340 PRO B C   1 
ATOM   11178 O  O   . PRO D 2 340 ? 197.605 157.584 162.016 1.00 166.01 ? 340 PRO B O   1 
ATOM   11179 C  CB  . PRO D 2 340 ? 197.321 155.008 160.144 1.00 166.01 ? 340 PRO B CB  1 
ATOM   11180 C  CG  . PRO D 2 340 ? 196.010 154.415 159.749 1.00 166.01 ? 340 PRO B CG  1 
ATOM   11181 C  CD  . PRO D 2 340 ? 195.550 153.599 160.930 1.00 166.01 ? 340 PRO B CD  1 
ATOM   11182 N  N   . ASP D 2 341 ? 195.434 156.972 161.994 1.00 159.75 ? 341 ASP B N   1 
ATOM   11183 C  CA  . ASP D 2 341 ? 194.958 158.348 162.108 1.00 159.75 ? 341 ASP B CA  1 
ATOM   11184 C  C   . ASP D 2 341 ? 195.471 159.024 163.375 1.00 159.75 ? 341 ASP B C   1 
ATOM   11185 O  O   . ASP D 2 341 ? 195.905 160.182 163.331 1.00 159.75 ? 341 ASP B O   1 
ATOM   11186 C  CB  . ASP D 2 341 ? 193.431 158.377 162.068 1.00 159.75 ? 341 ASP B CB  1 
ATOM   11187 N  N   . PHE D 2 342 ? 195.422 158.327 164.511 1.00 141.18 ? 342 PHE B N   1 
ATOM   11188 C  CA  . PHE D 2 342 ? 195.820 158.824 165.827 1.00 141.18 ? 342 PHE B CA  1 
ATOM   11189 C  C   . PHE D 2 342 ? 194.926 159.953 166.330 1.00 141.18 ? 342 PHE B C   1 
ATOM   11190 O  O   . PHE D 2 342 ? 195.239 160.556 167.361 1.00 141.18 ? 342 PHE B O   1 
ATOM   11191 C  CB  . PHE D 2 342 ? 197.282 159.295 165.863 1.00 141.18 ? 342 PHE B CB  1 
ATOM   11192 N  N   . LYS D 2 343 ? 193.868 160.301 165.605 1.00 140.45 ? 343 LYS B N   1 
ATOM   11193 C  CA  . LYS D 2 343 ? 193.038 161.448 165.945 1.00 140.45 ? 343 LYS B CA  1 
ATOM   11194 C  C   . LYS D 2 343 ? 191.967 161.083 166.968 1.00 140.45 ? 343 LYS B C   1 
ATOM   11195 O  O   . LYS D 2 343 ? 191.429 159.972 166.959 1.00 140.45 ? 343 LYS B O   1 
ATOM   11196 C  CB  . LYS D 2 343 ? 192.379 162.017 164.688 1.00 140.45 ? 343 LYS B CB  1 
ATOM   11197 N  N   . LEU D 2 344 ? 191.662 162.030 167.859 1.00 126.85 ? 344 LEU B N   1 
ATOM   11198 C  CA  . LEU D 2 344 ? 190.608 161.830 168.847 1.00 126.85 ? 344 LEU B CA  1 
ATOM   11199 C  C   . LEU D 2 344 ? 189.231 162.038 168.242 1.00 126.85 ? 344 LEU B C   1 
ATOM   11200 O  O   . LEU D 2 344 ? 188.242 161.539 168.790 1.00 126.85 ? 344 LEU B O   1 
ATOM   11201 C  CB  . LEU D 2 344 ? 190.823 162.790 170.032 1.00 126.85 ? 344 LEU B CB  1 
ATOM   11202 C  CG  . LEU D 2 344 ? 190.018 162.943 171.342 1.00 126.85 ? 344 LEU B CG  1 
ATOM   11203 C  CD1 . LEU D 2 344 ? 188.577 163.391 171.135 1.00 126.85 ? 344 LEU B CD1 1 
ATOM   11204 C  CD2 . LEU D 2 344 ? 190.029 161.690 172.205 1.00 126.85 ? 344 LEU B CD2 1 
ATOM   11205 N  N   . HIS D 2 345 ? 189.155 162.691 167.091 1.00 120.65 ? 345 HIS B N   1 
ATOM   11206 C  CA  . HIS D 2 345 ? 187.897 162.935 166.412 1.00 120.65 ? 345 HIS B CA  1 
ATOM   11207 C  C   . HIS D 2 345 ? 187.794 162.023 165.198 1.00 120.65 ? 345 HIS B C   1 
ATOM   11208 O  O   . HIS D 2 345 ? 188.801 161.574 164.643 1.00 120.65 ? 345 HIS B O   1 
ATOM   11209 C  CB  . HIS D 2 345 ? 187.790 164.404 165.998 1.00 120.65 ? 345 HIS B CB  1 
ATOM   11210 C  CG  . HIS D 2 345 ? 187.319 165.299 167.101 1.00 120.65 ? 345 HIS B CG  1 
ATOM   11211 N  ND1 . HIS D 2 345 ? 188.179 166.095 167.827 1.00 120.65 ? 345 HIS B ND1 1 
ATOM   11212 C  CD2 . HIS D 2 345 ? 186.087 165.501 167.625 1.00 120.65 ? 345 HIS B CD2 1 
ATOM   11213 C  CE1 . HIS D 2 345 ? 187.495 166.764 168.738 1.00 120.65 ? 345 HIS B CE1 1 
ATOM   11214 N  NE2 . HIS D 2 345 ? 186.223 166.419 168.638 1.00 120.65 ? 345 HIS B NE2 1 
ATOM   11215 N  N   . ILE D 2 346 ? 186.561 161.753 164.784 1.00 118.85 ? 346 ILE B N   1 
ATOM   11216 C  CA  . ILE D 2 346 ? 186.284 160.878 163.653 1.00 118.85 ? 346 ILE B CA  1 
ATOM   11217 C  C   . ILE D 2 346 ? 185.605 161.696 162.563 1.00 118.85 ? 346 ILE B C   1 
ATOM   11218 O  O   . ILE D 2 346 ? 184.670 162.459 162.836 1.00 118.85 ? 346 ILE B O   1 
ATOM   11219 C  CB  . ILE D 2 346 ? 185.434 159.658 164.067 1.00 118.85 ? 346 ILE B CB  1 
ATOM   11220 C  CG1 . ILE D 2 346 ? 184.026 160.064 164.513 1.00 118.85 ? 346 ILE B CG1 1 
ATOM   11221 C  CG2 . ILE D 2 346 ? 186.131 158.880 165.173 1.00 118.85 ? 346 ILE B CG2 1 
ATOM   11222 C  CD1 . ILE D 2 346 ? 182.947 159.746 163.495 1.00 118.85 ? 346 ILE B CD1 1 
ATOM   11223 N  N   . SER D 2 347 ? 186.111 161.578 161.344 1.00 123.11 ? 347 SER B N   1 
ATOM   11224 C  CA  . SER D 2 347 ? 185.519 162.293 160.224 1.00 123.11 ? 347 SER B CA  1 
ATOM   11225 C  C   . SER D 2 347 ? 184.195 161.640 159.841 1.00 123.11 ? 347 SER B C   1 
ATOM   11226 O  O   . SER D 2 347 ? 184.121 160.409 159.753 1.00 123.11 ? 347 SER B O   1 
ATOM   11227 C  CB  . SER D 2 347 ? 186.471 162.296 159.030 1.00 123.11 ? 347 SER B CB  1 
ATOM   11228 O  OG  . SER D 2 347 ? 187.706 162.908 159.361 1.00 123.11 ? 347 SER B OG  1 
ATOM   11229 N  N   . PRO D 2 348 ? 183.136 162.418 159.621 1.00 130.84 ? 348 PRO B N   1 
ATOM   11230 C  CA  . PRO D 2 348 ? 181.840 161.819 159.287 1.00 130.84 ? 348 PRO B CA  1 
ATOM   11231 C  C   . PRO D 2 348 ? 181.885 161.090 157.953 1.00 130.84 ? 348 PRO B C   1 
ATOM   11232 O  O   . PRO D 2 348 ? 182.640 161.450 157.048 1.00 130.84 ? 348 PRO B O   1 
ATOM   11233 C  CB  . PRO D 2 348 ? 180.895 163.024 159.237 1.00 130.84 ? 348 PRO B CB  1 
ATOM   11234 C  CG  . PRO D 2 348 ? 181.782 164.180 158.925 1.00 130.84 ? 348 PRO B CG  1 
ATOM   11235 C  CD  . PRO D 2 348 ? 183.092 163.889 159.600 1.00 130.84 ? 348 PRO B CD  1 
ATOM   11236 N  N   . SER D 2 349 ? 181.063 160.050 157.842 1.00 117.53 ? 349 SER B N   1 
ATOM   11237 C  CA  . SER D 2 349 ? 180.992 159.279 156.613 1.00 117.53 ? 349 SER B CA  1 
ATOM   11238 C  C   . SER D 2 349 ? 180.258 160.076 155.535 1.00 117.53 ? 349 SER B C   1 
ATOM   11239 O  O   . SER D 2 349 ? 179.751 161.177 155.767 1.00 117.53 ? 349 SER B O   1 
ATOM   11240 C  CB  . SER D 2 349 ? 180.304 157.939 156.868 1.00 117.53 ? 349 SER B CB  1 
ATOM   11241 O  OG  . SER D 2 349 ? 179.083 158.119 157.563 1.00 117.53 ? 349 SER B OG  1 
ATOM   11242 N  N   . ASN D 2 350 ? 180.203 159.504 154.333 1.00 113.92 ? 350 ASN B N   1 
ATOM   11243 C  CA  . ASN D 2 350 ? 179.596 160.150 153.177 1.00 113.92 ? 350 ASN B CA  1 
ATOM   11244 C  C   . ASN D 2 350 ? 178.182 159.646 152.908 1.00 113.92 ? 350 ASN B C   1 
ATOM   11245 O  O   . ASN D 2 350 ? 177.750 159.598 151.752 1.00 113.92 ? 350 ASN B O   1 
ATOM   11246 C  CB  . ASN D 2 350 ? 180.474 159.955 151.940 1.00 113.92 ? 350 ASN B CB  1 
ATOM   11247 N  N   . MET D 2 351 ? 177.452 159.270 153.953 1.00 113.92 ? 351 MET B N   1 
ATOM   11248 C  CA  . MET D 2 351 ? 176.095 158.777 153.782 1.00 113.92 ? 351 MET B CA  1 
ATOM   11249 C  C   . MET D 2 351 ? 175.095 159.927 153.721 1.00 113.92 ? 351 MET B C   1 
ATOM   11250 O  O   . MET D 2 351 ? 175.305 160.997 154.299 1.00 113.92 ? 351 MET B O   1 
ATOM   11251 C  CB  . MET D 2 351 ? 175.735 157.821 154.920 1.00 113.92 ? 351 MET B CB  1 
ATOM   11252 C  CG  . MET D 2 351 ? 175.606 158.485 156.281 1.00 113.92 ? 351 MET B CG  1 
ATOM   11253 S  SD  . MET D 2 351 ? 174.868 157.411 157.527 1.00 113.92 ? 351 MET B SD  1 
ATOM   11254 C  CE  . MET D 2 351 ? 173.961 156.260 156.501 1.00 113.92 ? 351 MET B CE  1 
ATOM   11255 N  N   . THR D 2 352 ? 173.998 159.693 153.005 1.00 119.96 ? 352 THR B N   1 
ATOM   11256 C  CA  . THR D 2 352 ? 172.978 160.712 152.803 1.00 119.96 ? 352 THR B CA  1 
ATOM   11257 C  C   . THR D 2 352 ? 172.088 160.847 154.033 1.00 119.96 ? 352 THR B C   1 
ATOM   11258 O  O   . THR D 2 352 ? 171.750 159.856 154.688 1.00 119.96 ? 352 THR B O   1 
ATOM   11259 C  CB  . THR D 2 352 ? 172.124 160.382 151.579 1.00 119.96 ? 352 THR B CB  1 
ATOM   11260 O  OG1 . THR D 2 352 ? 171.185 159.352 151.912 1.00 119.96 ? 352 THR B OG1 1 
ATOM   11261 C  CG2 . THR D 2 352 ? 173.003 159.915 150.430 1.00 119.96 ? 352 THR B CG2 1 
ATOM   11262 N  N   . ASN D 2 353 ? 171.713 162.084 154.343 1.00 113.92 ? 353 ASN B N   1 
ATOM   11263 C  CA  . ASN D 2 353 ? 170.760 162.371 155.411 1.00 113.92 ? 353 ASN B CA  1 
ATOM   11264 C  C   . ASN D 2 353 ? 169.347 162.348 154.844 1.00 113.92 ? 353 ASN B C   1 
ATOM   11265 O  O   . ASN D 2 353 ? 168.985 163.200 154.026 1.00 113.92 ? 353 ASN B O   1 
ATOM   11266 C  CB  . ASN D 2 353 ? 171.057 163.723 156.047 1.00 113.92 ? 353 ASN B CB  1 
ATOM   11267 C  CG  . ASN D 2 353 ? 170.140 164.036 157.218 1.00 113.92 ? 353 ASN B CG  1 
ATOM   11268 O  OD1 . ASN D 2 353 ? 169.313 163.216 157.618 1.00 113.92 ? 353 ASN B OD1 1 
ATOM   11269 N  ND2 . ASN D 2 353 ? 170.286 165.231 157.775 1.00 113.92 ? 353 ASN B ND2 1 
ATOM   11270 N  N   . GLN D 2 354 ? 168.550 161.377 155.279 1.00 113.92 ? 354 GLN B N   1 
ATOM   11271 C  CA  . GLN D 2 354 ? 167.195 161.229 154.769 1.00 113.92 ? 354 GLN B CA  1 
ATOM   11272 C  C   . GLN D 2 354 ? 166.204 162.163 155.449 1.00 113.92 ? 354 GLN B C   1 
ATOM   11273 O  O   . GLN D 2 354 ? 165.041 162.211 155.035 1.00 113.92 ? 354 GLN B O   1 
ATOM   11274 C  CB  . GLN D 2 354 ? 166.731 159.779 154.923 1.00 113.92 ? 354 GLN B CB  1 
ATOM   11275 C  CG  . GLN D 2 354 ? 167.552 158.777 154.129 1.00 113.92 ? 354 GLN B CG  1 
ATOM   11276 C  CD  . GLN D 2 354 ? 167.243 158.807 152.644 1.00 113.92 ? 354 GLN B CD  1 
ATOM   11277 O  OE1 . GLN D 2 354 ? 166.383 159.560 152.189 1.00 113.92 ? 354 GLN B OE1 1 
ATOM   11278 N  NE2 . GLN D 2 354 ? 167.950 157.984 151.879 1.00 113.92 ? 354 GLN B NE2 1 
ATOM   11279 N  N   . ASN D 2 355 ? 166.629 162.905 156.473 1.00 113.94 ? 355 ASN B N   1 
ATOM   11280 C  CA  . ASN D 2 355 ? 165.735 163.798 157.209 1.00 113.94 ? 355 ASN B CA  1 
ATOM   11281 C  C   . ASN D 2 355 ? 165.785 165.171 156.553 1.00 113.94 ? 355 ASN B C   1 
ATOM   11282 O  O   . ASN D 2 355 ? 166.632 166.008 156.867 1.00 113.94 ? 355 ASN B O   1 
ATOM   11283 C  CB  . ASN D 2 355 ? 166.137 163.866 158.676 1.00 113.94 ? 355 ASN B CB  1 
ATOM   11284 C  CG  . ASN D 2 355 ? 166.397 162.501 159.271 1.00 113.94 ? 355 ASN B CG  1 
ATOM   11285 O  OD1 . ASN D 2 355 ? 167.012 161.643 158.638 1.00 113.94 ? 355 ASN B OD1 1 
ATOM   11286 N  ND2 . ASN D 2 355 ? 165.931 162.291 160.494 1.00 113.94 ? 355 ASN B ND2 1 
ATOM   11287 N  N   . THR D 2 356 ? 164.860 165.402 155.626 1.00 116.97 ? 356 THR B N   1 
ATOM   11288 C  CA  . THR D 2 356 ? 164.772 166.690 154.961 1.00 116.97 ? 356 THR B CA  1 
ATOM   11289 C  C   . THR D 2 356 ? 164.281 167.761 155.935 1.00 116.97 ? 356 THR B C   1 
ATOM   11290 O  O   . THR D 2 356 ? 163.586 167.454 156.907 1.00 116.97 ? 356 THR B O   1 
ATOM   11291 C  CB  . THR D 2 356 ? 163.832 166.604 153.764 1.00 116.97 ? 356 THR B CB  1 
ATOM   11292 O  OG1 . THR D 2 356 ? 162.519 166.247 154.210 1.00 116.97 ? 356 THR B OG1 1 
ATOM   11293 C  CG2 . THR D 2 356 ? 164.327 165.559 152.776 1.00 116.97 ? 356 THR B CG2 1 
ATOM   11294 N  N   . PRO D 2 357 ? 164.641 169.027 155.702 1.00 113.92 ? 357 PRO B N   1 
ATOM   11295 C  CA  . PRO D 2 357 ? 164.180 170.090 156.609 1.00 113.92 ? 357 PRO B CA  1 
ATOM   11296 C  C   . PRO D 2 357 ? 162.668 170.204 156.712 1.00 113.92 ? 357 PRO B C   1 
ATOM   11297 O  O   . PRO D 2 357 ? 162.171 170.580 157.777 1.00 113.92 ? 357 PRO B O   1 
ATOM   11298 C  CB  . PRO D 2 357 ? 164.810 171.360 156.018 1.00 113.92 ? 357 PRO B CB  1 
ATOM   11299 C  CG  . PRO D 2 357 ? 165.165 171.010 154.615 1.00 113.92 ? 357 PRO B CG  1 
ATOM   11300 C  CD  . PRO D 2 357 ? 165.504 169.553 154.632 1.00 113.92 ? 357 PRO B CD  1 
ATOM   11301 N  N   . GLU D 2 358 ? 161.918 169.932 155.640 1.00 113.92 ? 358 GLU B N   1 
ATOM   11302 C  CA  . GLU D 2 358 ? 160.460 169.977 155.739 1.00 113.92 ? 358 GLU B CA  1 
ATOM   11303 C  C   . GLU D 2 358 ? 159.929 168.920 156.703 1.00 113.92 ? 358 GLU B C   1 
ATOM   11304 O  O   . GLU D 2 358 ? 159.050 169.202 157.524 1.00 113.92 ? 358 GLU B O   1 
ATOM   11305 C  CB  . GLU D 2 358 ? 159.835 169.798 154.355 1.00 113.92 ? 358 GLU B CB  1 
ATOM   11306 N  N   . TYR D 2 359 ? 160.461 167.699 156.619 1.00 113.92 ? 359 TYR B N   1 
ATOM   11307 C  CA  . TYR D 2 359 ? 160.059 166.622 157.521 1.00 113.92 ? 359 TYR B CA  1 
ATOM   11308 C  C   . TYR D 2 359 ? 160.369 166.972 158.972 1.00 113.92 ? 359 TYR B C   1 
ATOM   11309 O  O   . TYR D 2 359 ? 159.519 166.837 159.865 1.00 113.92 ? 359 TYR B O   1 
ATOM   11310 C  CB  . TYR D 2 359 ? 160.773 165.338 157.095 1.00 113.92 ? 359 TYR B CB  1 
ATOM   11311 C  CG  . TYR D 2 359 ? 160.687 164.171 158.048 1.00 113.92 ? 359 TYR B CG  1 
ATOM   11312 C  CD1 . TYR D 2 359 ? 159.603 163.306 158.031 1.00 113.92 ? 359 TYR B CD1 1 
ATOM   11313 C  CD2 . TYR D 2 359 ? 161.717 163.913 158.943 1.00 113.92 ? 359 TYR B CD2 1 
ATOM   11314 C  CE1 . TYR D 2 359 ? 159.537 162.231 158.895 1.00 113.92 ? 359 TYR B CE1 1 
ATOM   11315 C  CE2 . TYR D 2 359 ? 161.659 162.844 159.809 1.00 113.92 ? 359 TYR B CE2 1 
ATOM   11316 C  CZ  . TYR D 2 359 ? 160.571 162.004 159.780 1.00 113.92 ? 359 TYR B CZ  1 
ATOM   11317 O  OH  . TYR D 2 359 ? 160.516 160.938 160.647 1.00 113.92 ? 359 TYR B OH  1 
ATOM   11318 N  N   . MET D 2 360 ? 161.593 167.437 159.212 1.00 114.69 ? 360 MET B N   1 
ATOM   11319 C  CA  . MET D 2 360 ? 162.028 167.827 160.545 1.00 114.69 ? 360 MET B CA  1 
ATOM   11320 C  C   . MET D 2 360 ? 161.178 168.972 161.086 1.00 114.69 ? 360 MET B C   1 
ATOM   11321 O  O   . MET D 2 360 ? 160.748 168.951 162.247 1.00 114.69 ? 360 MET B O   1 
ATOM   11322 C  CB  . MET D 2 360 ? 163.505 168.203 160.440 1.00 114.69 ? 360 MET B CB  1 
ATOM   11323 C  CG  . MET D 2 360 ? 164.395 166.976 160.213 1.00 114.69 ? 360 MET B CG  1 
ATOM   11324 S  SD  . MET D 2 360 ? 166.164 167.253 159.968 1.00 114.69 ? 360 MET B SD  1 
ATOM   11325 C  CE  . MET D 2 360 ? 166.291 169.022 160.149 1.00 114.69 ? 360 MET B CE  1 
ATOM   11326 N  N   . GLU D 2 361 ? 160.889 169.959 160.236 1.00 113.92 ? 361 GLU B N   1 
ATOM   11327 C  CA  . GLU D 2 361 ? 160.115 171.125 160.639 1.00 113.92 ? 361 GLU B CA  1 
ATOM   11328 C  C   . GLU D 2 361 ? 158.682 170.722 160.981 1.00 113.92 ? 361 GLU B C   1 
ATOM   11329 O  O   . GLU D 2 361 ? 158.126 171.160 161.994 1.00 113.92 ? 361 GLU B O   1 
ATOM   11330 C  CB  . GLU D 2 361 ? 160.155 172.140 159.490 1.00 113.92 ? 361 GLU B CB  1 
ATOM   11331 C  CG  . GLU D 2 361 ? 159.474 173.506 159.636 1.00 113.92 ? 361 GLU B CG  1 
ATOM   11332 C  CD  . GLU D 2 361 ? 159.417 174.038 161.055 1.00 113.92 ? 361 GLU B CD  1 
ATOM   11333 O  OE1 . GLU D 2 361 ? 160.257 174.895 161.393 1.00 113.92 ? 361 GLU B OE1 1 
ATOM   11334 O  OE2 . GLU D 2 361 ? 158.508 173.671 161.812 1.00 113.92 ? 361 GLU B OE2 1 
ATOM   11335 N  N   . LYS D 2 362 ? 158.092 169.835 160.171 1.00 113.92 ? 362 LYS B N   1 
ATOM   11336 C  CA  . LYS D 2 362 ? 156.733 169.366 160.422 1.00 113.92 ? 362 LYS B CA  1 
ATOM   11337 C  C   . LYS D 2 362 ? 156.642 168.584 161.725 1.00 113.92 ? 362 LYS B C   1 
ATOM   11338 O  O   . LYS D 2 362 ? 155.704 168.780 162.509 1.00 113.92 ? 362 LYS B O   1 
ATOM   11339 C  CB  . LYS D 2 362 ? 156.239 168.515 159.253 1.00 100.12 ? 362 LYS B CB  1 
ATOM   11340 C  CG  . LYS D 2 362 ? 155.063 169.125 158.514 1.00 100.12 ? 362 LYS B CG  1 
ATOM   11341 C  CD  . LYS D 2 362 ? 154.701 168.311 157.290 1.00 100.12 ? 362 LYS B CD  1 
ATOM   11342 C  CE  . LYS D 2 362 ? 153.530 168.922 156.545 1.00 100.12 ? 362 LYS B CE  1 
ATOM   11343 N  NZ  . LYS D 2 362 ? 152.325 169.033 157.410 1.00 100.12 ? 362 LYS B NZ  1 
ATOM   11344 N  N   . ILE D 2 363 ? 157.600 167.687 161.971 1.00 113.92 ? 363 ILE B N   1 
ATOM   11345 C  CA  . ILE D 2 363 ? 157.574 166.928 163.220 1.00 113.92 ? 363 ILE B CA  1 
ATOM   11346 C  C   . ILE D 2 363 ? 157.760 167.866 164.404 1.00 113.92 ? 363 ILE B C   1 
ATOM   11347 O  O   . ILE D 2 363 ? 157.143 167.686 165.462 1.00 113.92 ? 363 ILE B O   1 
ATOM   11348 C  CB  . ILE D 2 363 ? 158.631 165.810 163.203 1.00 113.92 ? 363 ILE B CB  1 
ATOM   11349 C  CG1 . ILE D 2 363 ? 158.282 164.778 162.133 1.00 113.92 ? 363 ILE B CG1 1 
ATOM   11350 C  CG2 . ILE D 2 363 ? 158.726 165.144 164.566 1.00 113.92 ? 363 ILE B CG2 1 
ATOM   11351 C  CD1 . ILE D 2 363 ? 158.985 163.460 162.314 1.00 113.92 ? 363 ILE B CD1 1 
ATOM   11352 N  N   . LYS D 2 364 ? 158.603 168.887 164.245 1.00 113.92 ? 364 LYS B N   1 
ATOM   11353 C  CA  . LYS D 2 364 ? 158.803 169.842 165.327 1.00 113.92 ? 364 LYS B CA  1 
ATOM   11354 C  C   . LYS D 2 364 ? 157.516 170.608 165.615 1.00 113.92 ? 364 LYS B C   1 
ATOM   11355 O  O   . LYS D 2 364 ? 157.183 170.863 166.778 1.00 113.92 ? 364 LYS B O   1 
ATOM   11356 C  CB  . LYS D 2 364 ? 159.948 170.788 164.970 1.00 106.98 ? 364 LYS B CB  1 
ATOM   11357 C  CG  . LYS D 2 364 ? 160.267 171.827 166.018 1.00 106.98 ? 364 LYS B CG  1 
ATOM   11358 C  CD  . LYS D 2 364 ? 161.742 172.182 165.986 1.00 106.98 ? 364 LYS B CD  1 
ATOM   11359 C  CE  . LYS D 2 364 ? 162.172 172.586 164.587 1.00 106.98 ? 364 LYS B CE  1 
ATOM   11360 N  NZ  . LYS D 2 364 ? 163.546 173.157 164.563 1.00 106.98 ? 364 LYS B NZ  1 
ATOM   11361 N  N   . GLN D 2 365 ? 156.775 170.979 164.566 1.00 113.92 ? 365 GLN B N   1 
ATOM   11362 C  CA  . GLN D 2 365 ? 155.492 171.649 164.774 1.00 113.92 ? 365 GLN B CA  1 
ATOM   11363 C  C   . GLN D 2 365 ? 154.481 170.738 165.453 1.00 113.92 ? 365 GLN B C   1 
ATOM   11364 O  O   . GLN D 2 365 ? 153.729 171.184 166.325 1.00 113.92 ? 365 GLN B O   1 
ATOM   11365 C  CB  . GLN D 2 365 ? 154.914 172.143 163.448 1.00 106.46 ? 365 GLN B CB  1 
ATOM   11366 C  CG  . GLN D 2 365 ? 155.701 173.233 162.780 1.00 106.46 ? 365 GLN B CG  1 
ATOM   11367 C  CD  . GLN D 2 365 ? 156.066 174.354 163.731 1.00 106.46 ? 365 GLN B CD  1 
ATOM   11368 O  OE1 . GLN D 2 365 ? 155.236 174.826 164.508 1.00 106.46 ? 365 GLN B OE1 1 
ATOM   11369 N  NE2 . GLN D 2 365 ? 157.321 174.784 163.677 1.00 106.46 ? 365 GLN B NE2 1 
ATOM   11370 N  N   . ARG D 2 366 ? 154.442 169.460 165.066 1.00 113.92 ? 366 ARG B N   1 
ATOM   11371 C  CA  . ARG D 2 366 ? 153.547 168.525 165.741 1.00 113.92 ? 366 ARG B CA  1 
ATOM   11372 C  C   . ARG D 2 366 ? 153.897 168.401 167.219 1.00 113.92 ? 366 ARG B C   1 
ATOM   11373 O  O   . ARG D 2 366 ? 153.007 168.374 168.079 1.00 113.92 ? 366 ARG B O   1 
ATOM   11374 C  CB  . ARG D 2 366 ? 153.584 167.158 165.056 1.00 113.92 ? 366 ARG B CB  1 
ATOM   11375 C  CG  . ARG D 2 366 ? 152.754 166.098 165.765 1.00 113.92 ? 366 ARG B CG  1 
ATOM   11376 C  CD  . ARG D 2 366 ? 151.261 166.396 165.682 1.00 113.92 ? 366 ARG B CD  1 
ATOM   11377 N  NE  . ARG D 2 366 ? 150.713 166.193 164.345 1.00 113.92 ? 366 ARG B NE  1 
ATOM   11378 C  CZ  . ARG D 2 366 ? 150.322 165.019 163.870 1.00 113.92 ? 366 ARG B CZ  1 
ATOM   11379 N  NH1 . ARG D 2 366 ? 150.398 163.917 164.599 1.00 113.92 ? 366 ARG B NH1 1 
ATOM   11380 N  NH2 . ARG D 2 366 ? 149.837 164.949 162.634 1.00 113.92 ? 366 ARG B NH2 1 
ATOM   11381 N  N   . LEU D 2 367 ? 155.192 168.310 167.533 1.00 113.92 ? 367 LEU B N   1 
ATOM   11382 C  CA  . LEU D 2 367 ? 155.608 168.206 168.928 1.00 113.92 ? 367 LEU B CA  1 
ATOM   11383 C  C   . LEU D 2 367 ? 155.269 169.471 169.711 1.00 113.92 ? 367 LEU B C   1 
ATOM   11384 O  O   . LEU D 2 367 ? 154.827 169.391 170.862 1.00 113.92 ? 367 LEU B O   1 
ATOM   11385 C  CB  . LEU D 2 367 ? 157.103 167.902 169.006 1.00 113.92 ? 367 LEU B CB  1 
ATOM   11386 C  CG  . LEU D 2 367 ? 157.507 166.430 169.121 1.00 113.92 ? 367 LEU B CG  1 
ATOM   11387 C  CD1 . LEU D 2 367 ? 156.982 165.614 167.956 1.00 113.92 ? 367 LEU B CD1 1 
ATOM   11388 C  CD2 . LEU D 2 367 ? 159.015 166.308 169.210 1.00 113.92 ? 367 LEU B CD2 1 
ATOM   11389 N  N   . PHE D 2 368 ? 155.457 170.648 169.104 1.00 113.92 ? 368 PHE B N   1 
ATOM   11390 C  CA  . PHE D 2 368 ? 155.055 171.885 169.767 1.00 113.92 ? 368 PHE B CA  1 
ATOM   11391 C  C   . PHE D 2 368 ? 153.555 171.910 170.020 1.00 113.92 ? 368 PHE B C   1 
ATOM   11392 O  O   . PHE D 2 368 ? 153.100 172.325 171.098 1.00 113.92 ? 368 PHE B O   1 
ATOM   11393 C  CB  . PHE D 2 368 ? 155.468 173.101 168.936 1.00 113.92 ? 368 PHE B CB  1 
ATOM   11394 C  CG  . PHE D 2 368 ? 156.950 173.332 168.882 1.00 113.92 ? 368 PHE B CG  1 
ATOM   11395 C  CD1 . PHE D 2 368 ? 157.785 172.793 169.846 1.00 113.92 ? 368 PHE B CD1 1 
ATOM   11396 C  CD2 . PHE D 2 368 ? 157.503 174.124 167.892 1.00 113.92 ? 368 PHE B CD2 1 
ATOM   11397 C  CE1 . PHE D 2 368 ? 159.148 173.016 169.804 1.00 113.92 ? 368 PHE B CE1 1 
ATOM   11398 C  CE2 . PHE D 2 368 ? 158.864 174.356 167.849 1.00 113.92 ? 368 PHE B CE2 1 
ATOM   11399 C  CZ  . PHE D 2 368 ? 159.687 173.800 168.806 1.00 113.92 ? 368 PHE B CZ  1 
ATOM   11400 N  N   . GLU D 2 369 ? 152.767 171.485 169.030 1.00 113.92 ? 369 GLU B N   1 
ATOM   11401 C  CA  . GLU D 2 369 ? 151.324 171.439 169.211 1.00 113.92 ? 369 GLU B CA  1 
ATOM   11402 C  C   . GLU D 2 369 ? 150.958 170.528 170.370 1.00 113.92 ? 369 GLU B C   1 
ATOM   11403 O  O   . GLU D 2 369 ? 150.203 170.922 171.259 1.00 113.92 ? 369 GLU B O   1 
ATOM   11404 C  CB  . GLU D 2 369 ? 150.636 170.978 167.926 1.00 111.13 ? 369 GLU B CB  1 
ATOM   11405 C  CG  . GLU D 2 369 ? 150.668 171.996 166.804 1.00 111.13 ? 369 GLU B CG  1 
ATOM   11406 C  CD  . GLU D 2 369 ? 150.287 171.397 165.467 1.00 111.13 ? 369 GLU B CD  1 
ATOM   11407 O  OE1 . GLU D 2 369 ? 149.712 170.290 165.457 1.00 111.13 ? 369 GLU B OE1 1 
ATOM   11408 O  OE2 . GLU D 2 369 ? 150.561 172.034 164.428 1.00 111.13 ? 369 GLU B OE2 1 
ATOM   11409 N  N   . ASN D 2 370 ? 151.555 169.336 170.425 1.00 114.23 ? 370 ASN B N   1 
ATOM   11410 C  CA  . ASN D 2 370 ? 151.254 168.416 171.519 1.00 114.23 ? 370 ASN B CA  1 
ATOM   11411 C  C   . ASN D 2 370 ? 151.700 168.978 172.862 1.00 114.23 ? 370 ASN B C   1 
ATOM   11412 O  O   . ASN D 2 370 ? 151.084 168.687 173.893 1.00 114.23 ? 370 ASN B O   1 
ATOM   11413 C  CB  . ASN D 2 370 ? 151.912 167.060 171.270 1.00 114.23 ? 370 ASN B CB  1 
ATOM   11414 C  CG  . ASN D 2 370 ? 151.215 166.265 170.187 1.00 114.23 ? 370 ASN B CG  1 
ATOM   11415 O  OD1 . ASN D 2 370 ? 150.298 165.491 170.463 1.00 114.23 ? 370 ASN B OD1 1 
ATOM   11416 N  ND2 . ASN D 2 370 ? 151.644 166.453 168.947 1.00 114.23 ? 370 ASN B ND2 1 
ATOM   11417 N  N   . LEU D 2 371 ? 152.763 169.782 172.872 1.00 115.68 ? 371 LEU B N   1 
ATOM   11418 C  CA  . LEU D 2 371 ? 153.228 170.379 174.118 1.00 115.68 ? 371 LEU B CA  1 
ATOM   11419 C  C   . LEU D 2 371 ? 152.308 171.501 174.581 1.00 115.68 ? 371 LEU B C   1 
ATOM   11420 O  O   . LEU D 2 371 ? 152.234 171.782 175.782 1.00 115.68 ? 371 LEU B O   1 
ATOM   11421 C  CB  . LEU D 2 371 ? 154.657 170.900 173.957 1.00 115.68 ? 371 LEU B CB  1 
ATOM   11422 C  CG  . LEU D 2 371 ? 155.773 169.855 173.931 1.00 115.68 ? 371 LEU B CG  1 
ATOM   11423 C  CD1 . LEU D 2 371 ? 157.020 170.434 173.289 1.00 115.68 ? 371 LEU B CD1 1 
ATOM   11424 C  CD2 . LEU D 2 371 ? 156.068 169.362 175.336 1.00 115.68 ? 371 LEU B CD2 1 
ATOM   11425 N  N   . ARG D 2 372 ? 151.605 172.154 173.653 1.00 125.08 ? 372 ARG B N   1 
ATOM   11426 C  CA  . ARG D 2 372 ? 150.675 173.207 174.061 1.00 125.08 ? 372 ARG B CA  1 
ATOM   11427 C  C   . ARG D 2 372 ? 149.513 172.710 174.931 1.00 125.08 ? 372 ARG B C   1 
ATOM   11428 O  O   . ARG D 2 372 ? 148.854 173.535 175.571 1.00 125.08 ? 372 ARG B O   1 
ATOM   11429 C  CB  . ARG D 2 372 ? 150.149 173.947 172.830 1.00 125.08 ? 372 ARG B CB  1 
ATOM   11430 C  CG  . ARG D 2 372 ? 151.226 174.751 172.113 1.00 125.08 ? 372 ARG B CG  1 
ATOM   11431 C  CD  . ARG D 2 372 ? 150.671 175.609 170.990 1.00 125.08 ? 372 ARG B CD  1 
ATOM   11432 N  NE  . ARG D 2 372 ? 151.694 175.930 170.002 1.00 125.08 ? 372 ARG B NE  1 
ATOM   11433 C  CZ  . ARG D 2 372 ? 151.642 175.586 168.724 1.00 125.08 ? 372 ARG B CZ  1 
ATOM   11434 N  NH1 . ARG D 2 372 ? 150.600 174.943 168.224 1.00 125.08 ? 372 ARG B NH1 1 
ATOM   11435 N  NH2 . ARG D 2 372 ? 152.647 175.920 167.920 1.00 125.08 ? 372 ARG B NH2 1 
ATOM   11436 N  N   . MET D 2 373 ? 149.230 171.407 174.975 1.00 122.81 ? 373 MET B N   1 
ATOM   11437 C  CA  . MET D 2 373 ? 148.180 170.885 175.851 1.00 122.81 ? 373 MET B CA  1 
ATOM   11438 C  C   . MET D 2 373 ? 148.693 170.539 177.242 1.00 122.81 ? 373 MET B C   1 
ATOM   11439 O  O   . MET D 2 373 ? 148.013 169.815 177.978 1.00 122.81 ? 373 MET B O   1 
ATOM   11440 C  CB  . MET D 2 373 ? 147.467 169.670 175.248 1.00 122.81 ? 373 MET B CB  1 
ATOM   11441 C  CG  . MET D 2 373 ? 146.808 169.859 173.898 1.00 122.81 ? 373 MET B CG  1 
ATOM   11442 S  SD  . MET D 2 373 ? 147.807 170.576 172.618 1.00 122.81 ? 373 MET B SD  1 
ATOM   11443 C  CE  . MET D 2 373 ? 146.886 170.114 171.154 1.00 122.81 ? 373 MET B CE  1 
ATOM   11444 N  N   . LEU D 2 374 ? 149.869 171.033 177.615 1.00 117.18 ? 374 LEU B N   1 
ATOM   11445 C  CA  . LEU D 2 374 ? 150.439 170.717 178.918 1.00 117.18 ? 374 LEU B CA  1 
ATOM   11446 C  C   . LEU D 2 374 ? 149.784 171.584 179.986 1.00 117.18 ? 374 LEU B C   1 
ATOM   11447 O  O   . LEU D 2 374 ? 149.865 172.815 179.904 1.00 117.18 ? 374 LEU B O   1 
ATOM   11448 C  CB  . LEU D 2 374 ? 151.947 170.943 178.910 1.00 117.18 ? 374 LEU B CB  1 
ATOM   11449 C  CG  . LEU D 2 374 ? 152.844 169.705 178.871 1.00 117.18 ? 374 LEU B CG  1 
ATOM   11450 C  CD1 . LEU D 2 374 ? 152.884 169.036 180.235 1.00 117.18 ? 374 LEU B CD1 1 
ATOM   11451 C  CD2 . LEU D 2 374 ? 152.375 168.736 177.805 1.00 117.18 ? 374 LEU B CD2 1 
ATOM   11452 N  N   . PRO D 2 375 ? 149.121 170.993 180.992 1.00 128.35 ? 375 PRO B N   1 
ATOM   11453 C  CA  . PRO D 2 375 ? 148.514 171.746 182.095 1.00 128.35 ? 375 PRO B CA  1 
ATOM   11454 C  C   . PRO D 2 375 ? 149.549 172.480 182.940 1.00 128.35 ? 375 PRO B C   1 
ATOM   11455 O  O   . PRO D 2 375 ? 149.784 173.664 182.698 1.00 128.35 ? 375 PRO B O   1 
ATOM   11456 C  CB  . PRO D 2 375 ? 147.814 170.660 182.922 1.00 128.35 ? 375 PRO B CB  1 
ATOM   11457 C  CG  . PRO D 2 375 ? 147.633 169.513 181.988 1.00 128.35 ? 375 PRO B CG  1 
ATOM   11458 C  CD  . PRO D 2 375 ? 148.821 169.554 181.076 1.00 128.35 ? 375 PRO B CD  1 
HETATM 11459 ZN ZN  . ZN  E 3 .   ? 128.459 147.156 171.384 1.00 187.73 ? 501 ZN  D ZN  1 
HETATM 11460 ZN ZN  . ZN  F 3 .   ? 171.127 152.354 171.423 1.00 187.73 ? 501 ZN  B ZN  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
2964  N N   . LYS B 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS D N   
2965  C CA  . LYS B 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS D CA  
2966  C C   . LYS B 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS D C   
2967  O O   . LYS B 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS D O   
2973  N N   . VAL B 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL D N   
2974  C CA  . VAL B 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL D CA  
2975  C C   . VAL B 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL D C   
2976  O O   . VAL B 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL D O   
2977  C CB  . VAL B 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL D CB  
2978  C CG1 . VAL B 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL D CG1 
2979  C CG2 . VAL B 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL D CG2 
2980  N N   . CYS B 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS D N   
2981  C CA  . CYS B 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS D CA  
2982  C C   . CYS B 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS D C   
2983  O O   . CYS B 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS D O   
2984  C CB  . CYS B 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS D CB  
2985  S SG  . CYS B 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS D SG  
2986  N N   . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D N   
2987  C CA  . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CA  
2988  C C   . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D C   
2989  O O   . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D O   
2990  C CB  . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CB  
2991  C CG  . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CG  
2992  C CD1 . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CD1 
2993  C CD2 . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CD2 
2994  C CE1 . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CE1 
2995  C CE2 . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CE2 
2996  C CZ  . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D CZ  
2997  O OH  . TYR B 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR D OH  
2998  N N   . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D N   
2999  C CA  . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CA  
3000  C C   . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D C   
3001  O O   . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D O   
3002  C CB  . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CB  
3003  C CG  . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CG  
3004  C CD1 . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CD1 
3005  C CD2 . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CD2 
3006  C CE1 . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CE1 
3007  C CE2 . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CE2 
3008  C CZ  . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D CZ  
3009  O OH  . TYR B 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR D OH  
3010  N N   . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D N   
3011  C CA  . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CA  
3012  C C   . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D C   
3013  O O   . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D O   
3014  C CB  . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CB  
3015  C CG  . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CG  
3016  C CD1 . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CD1 
3017  C CD2 . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CD2 
3018  C CE1 . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CE1 
3019  C CE2 . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CE2 
3020  C CZ  . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D CZ  
3021  O OH  . TYR B 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR D OH  
3022  N N   . ASP B 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP D N   
3023  C CA  . ASP B 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP D CA  
3024  C C   . ASP B 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP D C   
3025  O O   . ASP B 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP D O   
3030  N N   . GLY B 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY D N   
3031  C CA  . GLY B 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY D CA  
3032  C C   . GLY B 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY D C   
3033  O O   . GLY B 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY D O   
3034  N N   . ASP B 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP D N   
3035  C CA  . ASP B 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP D CA  
3036  C C   . ASP B 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP D C   
3037  O O   . ASP B 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP D O   
3051  N N   . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D N   
3052  C CA  . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D CA  
3053  C C   . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D C   
3054  O O   . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D O   
3055  C CB  . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D CB  
3056  C CG  . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D CG  
3057  O OD1 . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D OD1 
3058  N ND2 . ASN B 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN D ND2 
3059  N N   . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D N   
3060  C CA  . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CA  
3061  C C   . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D C   
3062  O O   . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D O   
3063  C CB  . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CB  
3064  C CG  . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CG  
3065  C CD1 . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CD1 
3066  C CD2 . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CD2 
3067  C CE1 . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CE1 
3068  C CE2 . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CE2 
3069  C CZ  . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D CZ  
3070  O OH  . TYR B 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR D OH  
3071  N N   . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D N   
3072  C CA  . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CA  
3073  C C   . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D C   
3074  O O   . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D O   
3075  C CB  . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CB  
3076  C CG  . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CG  
3077  C CD1 . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CD1 
3078  C CD2 . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CD2 
3079  C CE1 . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CE1 
3080  C CE2 . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CE2 
3081  C CZ  . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D CZ  
3082  O OH  . TYR B 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR D OH  
3083  N N   . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D N   
3084  C CA  . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CA  
3085  C C   . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D C   
3086  O O   . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D O   
3087  C CB  . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CB  
3088  C CG  . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CG  
3089  C CD1 . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CD1 
3090  C CD2 . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CD2 
3091  C CE1 . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CE1 
3092  C CE2 . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CE2 
3093  C CZ  . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D CZ  
3094  O OH  . TYR B 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR D OH  
3095  N N   . GLY B 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY D N   
3096  C CA  . GLY B 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY D CA  
3097  C C   . GLY B 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY D C   
3098  O O   . GLY B 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY D O   
3099  N N   . GLN B 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN D N   
3100  C CA  . GLN B 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN D CA  
3101  C C   . GLN B 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN D C   
3102  O O   . GLN B 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN D O   
3103  C CB  . GLN B 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN D CB  
3104  N N   . GLY B 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY D N   
3105  C CA  . GLY B 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY D CA  
3106  C C   . GLY B 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY D C   
3107  O O   . GLY B 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY D O   
3108  N N   . HIS B 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS D N   
3109  C CA  . HIS B 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS D CA  
3110  C C   . HIS B 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS D C   
3111  O O   . HIS B 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS D O   
3118  N N   . PRO B 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO D N   
3119  C CA  . PRO B 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO D CA  
3120  C C   . PRO B 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO D C   
3121  O O   . PRO B 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO D O   
3122  C CB  . PRO B 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO D CB  
3123  C CG  . PRO B 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO D CG  
3124  C CD  . PRO B 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO D CD  
3125  N N   . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D N   
3126  C CA  . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D CA  
3127  C C   . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D C   
3128  O O   . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D O   
3129  C CB  . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D CB  
3130  C CG  . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D CG  
3131  S SD  . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D SD  
3132  C CE  . MET B 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET D CE  
3133  N N   . LYS B 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS D N   
3134  C CA  . LYS B 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS D CA  
3135  C C   . LYS B 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS D C   
3136  O O   . LYS B 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS D O   
3159  N N   . ARG B 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG D N   
3160  C CA  . ARG B 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG D CA  
3161  C C   . ARG B 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG D C   
3162  O O   . ARG B 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG D O   
3164  N N   . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D N   
3165  C CA  . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D CA  
3166  C C   . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D C   
3167  O O   . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D O   
3168  C CB  . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D CB  
3169  C CG1 . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D CG1 
3170  C CG2 . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D CG2 
3171  C CD1 . ILE B 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE D CD1 
3172  N N   . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D N   
3173  C CA  . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D CA  
3174  C C   . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D C   
3175  O O   . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D O   
3176  C CB  . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D CB  
3177  C CG  . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D CG  
3178  C CD  . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D CD  
3179  N NE  . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D NE  
3180  C CZ  . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D CZ  
3181  N NH1 . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D NH1 
3182  N NH2 . ARG B 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG D NH2 
3183  N N   . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D N   
3184  C CA  . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D CA  
3185  C C   . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D C   
3186  O O   . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D O   
3187  C CB  . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D CB  
3188  C CG  . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D CG  
3189  S SD  . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D SD  
3190  C CE  . MET B 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET D CE  
3191  N N   . THR B 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR D N   
3192  C CA  . THR B 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR D CA  
3193  C C   . THR B 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR D C   
3194  O O   . THR B 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR D O   
3195  C CB  . THR B 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR D CB  
3196  O OG1 . THR B 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR D OG1 
3197  C CG2 . THR B 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR D CG2 
3198  N N   . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D N   
3199  C CA  . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D CA  
3200  C C   . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D C   
3201  O O   . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D O   
3202  C CB  . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D CB  
3203  C CG  . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D CG  
3204  N ND1 . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D ND1 
3205  C CD2 . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D CD2 
3206  C CE1 . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D CE1 
3207  N NE2 . HIS B 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS D NE2 
3208  N N   . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D N   
3209  C CA  . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D CA  
3210  C C   . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D C   
3211  O O   . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D O   
3212  C CB  . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D CB  
3213  C CG  . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D CG  
3214  O OD1 . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D OD1 
3215  N ND2 . ASN B 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN D ND2 
3216  N N   . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D N   
3217  C CA  . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D CA  
3218  C C   . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D C   
3219  O O   . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D O   
3220  C CB  . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D CB  
3221  C CG  . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D CG  
3222  C CD1 . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D CD1 
3223  C CD2 . LEU B 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU D CD2 
3224  N N   . LEU B 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU D N   
3225  C CA  . LEU B 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU D CA  
3226  C C   . LEU B 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU D C   
3227  O O   . LEU B 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU D O   
3228  C CB  . LEU B 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU D CB  
3229  N N   . LEU B 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU D N   
3230  C CA  . LEU B 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU D CA  
3231  C C   . LEU B 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU D C   
3232  O O   . LEU B 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU D O   
3233  C CB  . LEU B 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU D CB  
3234  N N   . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D N   
3235  C CA  . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D CA  
3236  C C   . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D C   
3237  O O   . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D O   
3238  C CB  . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D CB  
3239  C CG  . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D CG  
3240  O OD1 . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D OD1 
3241  N ND2 . ASN B 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN D ND2 
3242  N N   . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D N   
3243  C CA  . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CA  
3244  C C   . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D C   
3245  O O   . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D O   
3246  C CB  . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CB  
3247  C CG  . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CG  
3248  C CD1 . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CD1 
3249  C CD2 . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CD2 
3250  C CE1 . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CE1 
3251  C CE2 . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CE2 
3252  C CZ  . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D CZ  
3253  O OH  . TYR B 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR D OH  
3254  N N   . GLY B 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY D N   
3255  C CA  . GLY B 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY D CA  
3256  C C   . GLY B 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY D C   
3257  O O   . GLY B 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY D O   
3258  N N   . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D N   
3259  C CA  . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D CA  
3260  C C   . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D C   
3261  O O   . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D O   
3262  C CB  . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D CB  
3263  C CG  . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D CG  
3264  C CD1 . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D CD1 
3265  C CD2 . LEU B 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU D CD2 
3266  N N   . TYR B 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR D N   
3267  C CA  . TYR B 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR D CA  
3268  C C   . TYR B 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR D C   
3269  O O   . TYR B 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR D O   
3270  C CB  . TYR B 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR D CB  
3271  N N   . ARG B 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG D N   
3272  C CA  . ARG B 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG D CA  
3273  C C   . ARG B 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG D C   
3274  O O   . ARG B 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG D O   
3275  C CB  . ARG B 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG D CB  
3276  N N   . LYS B 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS D N   
3277  C CA  . LYS B 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS D CA  
3278  C C   . LYS B 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS D C   
3279  O O   . LYS B 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS D O   
3280  C CB  . LYS B 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS D CB  
3281  N N   . MET B 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET D N   
3282  C CA  . MET B 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET D CA  
3283  C C   . MET B 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET D C   
3284  O O   . MET B 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET D O   
3289  N N   . GLU B 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU D N   
3290  C CA  . GLU B 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU D CA  
3291  C C   . GLU B 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU D C   
3292  O O   . GLU B 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU D O   
3298  N N   . ILE B 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE D N   
3299  C CA  . ILE B 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE D CA  
3300  C C   . ILE B 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE D C   
3301  O O   . ILE B 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE D O   
3306  N N   . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D N   
3307  C CA  . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CA  
3308  C C   . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D C   
3309  O O   . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D O   
3310  C CB  . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CB  
3311  C CG  . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CG  
3312  C CD1 . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CD1 
3313  C CD2 . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CD2 
3314  C CE1 . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CE1 
3315  C CE2 . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CE2 
3316  C CZ  . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D CZ  
3317  O OH  . TYR B 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR D OH  
3318  N N   . ARG B 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG D N   
3319  C CA  . ARG B 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG D CA  
3320  C C   . ARG B 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG D C   
3321  O O   . ARG B 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG D O   
3323  N N   . PRO B 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO D N   
3324  C CA  . PRO B 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO D CA  
3325  C C   . PRO B 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO D C   
3326  O O   . PRO B 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO D O   
3327  C CB  . PRO B 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO D CB  
3328  C CG  . PRO B 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO D CG  
3329  C CD  . PRO B 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO D CD  
3330  N N   . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D N   
3331  C CA  . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D CA  
3332  C C   . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D C   
3333  O O   . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D O   
3334  C CB  . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D CB  
3335  C CG  . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D CG  
3336  N ND1 . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D ND1 
3337  C CD2 . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D CD2 
3338  C CE1 . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D CE1 
3339  N NE2 . HIS B 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS D NE2 
3340  N N   . LYS B 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS D N   
3341  C CA  . LYS B 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS D CA  
3342  C C   . LYS B 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS D C   
3343  O O   . LYS B 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS D O   
3345  N N   . ALA B 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA D N   
3346  C CA  . ALA B 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA D CA  
3347  C C   . ALA B 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA D C   
3348  O O   . ALA B 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA D O   
3349  C CB  . ALA B 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA D CB  
3350  N N   . THR B 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR D N   
3351  C CA  . THR B 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR D CA  
3352  C C   . THR B 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR D C   
3353  O O   . THR B 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR D O   
3357  N N   . ALA B 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA D N   
3358  C CA  . ALA B 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA D CA  
3359  C C   . ALA B 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA D C   
3360  O O   . ALA B 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA D O   
3361  C CB  . ALA B 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA D CB  
3362  N N   . GLU B 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU D N   
3363  C CA  . GLU B 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU D CA  
3364  C C   . GLU B 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU D C   
3365  O O   . GLU B 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU D O   
3367  N N   . GLU B 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU D N   
3368  C CA  . GLU B 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU D CA  
3369  C C   . GLU B 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU D C   
3370  O O   . GLU B 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU D O   
3372  N N   . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D N   
3373  C CA  . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D CA  
3374  C C   . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D C   
3375  O O   . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D O   
3376  C CB  . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D CB  
3377  C CG  . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D CG  
3378  S SD  . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D SD  
3379  C CE  . MET B 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET D CE  
3380  N N   . THR B 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR D N   
3381  C CA  . THR B 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR D CA  
3382  C C   . THR B 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR D C   
3383  O O   . THR B 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR D O   
3384  C CB  . THR B 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR D CB  
3385  O OG1 . THR B 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR D OG1 
3386  C CG2 . THR B 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR D CG2 
3387  N N   . LYS B 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS D N   
3388  C CA  . LYS B 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS D CA  
3389  C C   . LYS B 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS D C   
3390  O O   . LYS B 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS D O   
3391  C CB  . LYS B 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS D CB  
3392  N N   . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D N   
3393  C CA  . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CA  
3394  C C   . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D C   
3395  O O   . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D O   
3396  C CB  . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CB  
3397  C CG  . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CG  
3398  C CD1 . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CD1 
3399  C CD2 . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CD2 
3400  C CE1 . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CE1 
3401  C CE2 . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CE2 
3402  C CZ  . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D CZ  
3403  O OH  . TYR B 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR D OH  
3404  N N   . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D N   
3405  C CA  . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D CA  
3406  C C   . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D C   
3407  O O   . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D O   
3408  C CB  . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D CB  
3409  C CG  . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D CG  
3410  N ND1 . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D ND1 
3411  C CD2 . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D CD2 
3412  C CE1 . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D CE1 
3413  N NE2 . HIS B 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS D NE2 
3414  N N   . SER B 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER D N   
3415  C CA  . SER B 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER D CA  
3416  C C   . SER B 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER D C   
3417  O O   . SER B 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER D O   
3420  N N   . ASP B 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP D N   
3421  C CA  . ASP B 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP D CA  
3422  C C   . ASP B 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP D C   
3423  O O   . ASP B 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP D O   
3424  C CB  . ASP B 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP D CB  
3425  N N   . GLU B 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU D N   
3426  C CA  . GLU B 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU D CA  
3427  C C   . GLU B 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU D C   
3428  O O   . GLU B 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU D O   
3429  C CB  . GLU B 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU D CB  
3430  N N   . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D N   
3431  C CA  . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CA  
3432  C C   . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D C   
3433  O O   . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D O   
3434  C CB  . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CB  
3435  C CG  . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CG  
3436  C CD1 . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CD1 
3437  C CD2 . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CD2 
3438  C CE1 . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CE1 
3439  C CE2 . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CE2 
3440  C CZ  . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D CZ  
3441  O OH  . TYR B 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR D OH  
3442  N N   . ILE B 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE D N   
3443  C CA  . ILE B 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE D CA  
3444  C C   . ILE B 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE D C   
3445  O O   . ILE B 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE D O   
3450  N N   . LYS B 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS D N   
3451  C CA  . LYS B 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS D CA  
3452  C C   . LYS B 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS D C   
3453  O O   . LYS B 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS D O   
3454  C CB  . LYS B 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS D CB  
3455  N N   . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D N   
3456  C CA  . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CA  
3457  C C   . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D C   
3458  O O   . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D O   
3459  C CB  . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CB  
3460  C CG  . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CG  
3461  C CD1 . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CD1 
3462  C CD2 . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CD2 
3463  C CE1 . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CE1 
3464  C CE2 . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CE2 
3465  C CZ  . PHE B 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE D CZ  
3466  N N   . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D N   
3467  C CA  . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D CA  
3468  C C   . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D C   
3469  O O   . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D O   
3470  C CB  . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D CB  
3471  C CG  . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D CG  
3472  C CD1 . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D CD1 
3473  C CD2 . LEU B 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU D CD2 
3474  N N   . ARG B 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG D N   
3475  C CA  . ARG B 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG D CA  
3476  C C   . ARG B 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG D C   
3477  O O   . ARG B 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG D O   
3479  N N   . SER B 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER D N   
3480  C CA  . SER B 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER D CA  
3481  C C   . SER B 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER D C   
3482  O O   . SER B 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER D O   
3485  N N   . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D N   
3486  C CA  . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D CA  
3487  C C   . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D C   
3488  O O   . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D O   
3489  C CB  . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D CB  
3490  C CG1 . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D CG1 
3491  C CG2 . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D CG2 
3492  C CD1 . ILE B 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE D CD1 
3493  N N   . ARG B 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG D N   
3494  C CA  . ARG B 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG D CA  
3495  C C   . ARG B 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG D C   
3496  O O   . ARG B 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG D O   
3497  C CB  . ARG B 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG D CB  
3498  N N   . PRO B 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO D N   
3499  C CA  . PRO B 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO D CA  
3500  C C   . PRO B 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO D C   
3501  O O   . PRO B 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO D O   
3502  C CB  . PRO B 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO D CB  
3503  C CG  . PRO B 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO D CG  
3504  C CD  . PRO B 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO D CD  
3505  N N   . ASP B 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP D N   
3506  C CA  . ASP B 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP D CA  
3507  C C   . ASP B 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP D C   
3508  O O   . ASP B 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP D O   
3509  C CB  . ASP B 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP D CB  
3510  N N   . ASN B 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN D N   
3511  C CA  . ASN B 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN D CA  
3512  C C   . ASN B 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN D C   
3513  O O   . ASN B 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN D O   
3518  N N   . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D N   
3519  C CA  . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D CA  
3520  C C   . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D C   
3521  O O   . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D O   
3522  C CB  . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D CB  
3523  C CG  . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D CG  
3524  S SD  . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D SD  
3525  C CE  . MET B 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET D CE  
3526  N N   . SER B 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER D N   
3527  C CA  . SER B 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER D CA  
3528  C C   . SER B 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER D C   
3529  O O   . SER B 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER D O   
3530  C CB  . SER B 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER D CB  
3531  N N   . GLU B 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU D N   
3532  C CA  . GLU B 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU D CA  
3533  C C   . GLU B 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU D C   
3534  O O   . GLU B 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU D O   
3535  C CB  . GLU B 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU D CB  
3536  N N   . TYR B 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR D N   
3537  C CA  . TYR B 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR D CA  
3538  C C   . TYR B 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR D C   
3539  O O   . TYR B 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR D O   
3548  N N   . SER B 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER D N   
3549  C CA  . SER B 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER D CA  
3550  C C   . SER B 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER D C   
3551  O O   . SER B 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER D O   
3552  C CB  . SER B 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER D CB  
3553  N N   . LYS B 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS D N   
3554  C CA  . LYS B 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS D CA  
3555  C C   . LYS B 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS D C   
3556  O O   . LYS B 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS D O   
3557  C CB  . LYS B 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS D CB  
3558  N N   . GLN B 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN D N   
3559  C CA  . GLN B 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN D CA  
3560  C C   . GLN B 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN D C   
3561  O O   . GLN B 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN D O   
3567  N N   . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D N   
3568  C CA  . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D CA  
3569  C C   . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D C   
3570  O O   . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D O   
3571  C CB  . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D CB  
3572  C CG  . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D CG  
3573  S SD  . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D SD  
3574  C CE  . MET B 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET D CE  
3575  N N   . GLN B 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN D N   
3576  C CA  . GLN B 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN D CA  
3577  C C   . GLN B 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN D C   
3578  O O   . GLN B 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN D O   
3580  N N   . ARG B 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG D N   
3581  C CA  . ARG B 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG D CA  
3582  C C   . ARG B 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG D C   
3583  O O   . ARG B 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG D O   
3591  N N   . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D N   
3592  C CA  . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CA  
3593  C C   . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D C   
3594  O O   . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D O   
3595  C CB  . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CB  
3596  C CG  . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CG  
3597  C CD1 . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CD1 
3598  C CD2 . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CD2 
3599  C CE1 . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CE1 
3600  C CE2 . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CE2 
3601  C CZ  . PHE B 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE D CZ  
3602  N N   . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D N   
3603  C CA  . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D CA  
3604  C C   . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D C   
3605  O O   . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D O   
3606  C CB  . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D CB  
3607  C CG  . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D CG  
3608  O OD1 . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D OD1 
3609  N ND2 . ASN B 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN D ND2 
3610  N N   . VAL B 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL D N   
3611  C CA  . VAL B 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL D CA  
3612  C C   . VAL B 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL D C   
3613  O O   . VAL B 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL D O   
3614  C CB  . VAL B 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL D CB  
3615  C CG1 . VAL B 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL D CG1 
3616  C CG2 . VAL B 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL D CG2 
3617  N N   . GLY B 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY D N   
3618  C CA  . GLY B 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY D CA  
3619  C C   . GLY B 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY D C   
3620  O O   . GLY B 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY D O   
3631  N N   . CYS B 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS D N   
3632  C CA  . CYS B 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS D CA  
3633  C C   . CYS B 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS D C   
3634  O O   . CYS B 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS D O   
3635  C CB  . CYS B 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS D CB  
3636  S SG  . CYS B 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS D SG  
3637  N N   . PRO B 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO D N   
3638  C CA  . PRO B 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO D CA  
3639  C C   . PRO B 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO D C   
3640  O O   . PRO B 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO D O   
3641  C CB  . PRO B 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO D CB  
3642  C CG  . PRO B 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO D CG  
3643  C CD  . PRO B 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO D CD  
3644  N N   . VAL B 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL D N   
3645  C CA  . VAL B 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL D CA  
3646  C C   . VAL B 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL D C   
3647  O O   . VAL B 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL D O   
3648  C CB  . VAL B 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL D CB  
3649  C CG1 . VAL B 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL D CG1 
3650  C CG2 . VAL B 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL D CG2 
3651  N N   . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D N   
3652  C CA  . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CA  
3653  C C   . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D C   
3654  O O   . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D O   
3655  C CB  . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CB  
3656  C CG  . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CG  
3657  C CD1 . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CD1 
3658  C CD2 . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CD2 
3659  C CE1 . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CE1 
3660  C CE2 . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CE2 
3661  C CZ  . PHE B 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE D CZ  
3662  N N   . ASP B 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP D N   
3663  C CA  . ASP B 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP D CA  
3664  C C   . ASP B 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP D C   
3665  O O   . ASP B 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP D O   
3666  C CB  . ASP B 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP D CB  
3667  N N   . GLY B 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY D N   
3668  C CA  . GLY B 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY D CA  
3669  C C   . GLY B 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY D C   
3670  O O   . GLY B 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY D O   
3671  N N   . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D N   
3672  C CA  . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D CA  
3673  C C   . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D C   
3674  O O   . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D O   
3675  C CB  . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D CB  
3676  C CG  . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D CG  
3677  C CD1 . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D CD1 
3678  C CD2 . LEU B 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU D CD2 
3679  N N   . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D N   
3680  C CA  . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CA  
3681  C C   . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D C   
3682  O O   . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D O   
3683  C CB  . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CB  
3684  C CG  . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CG  
3685  C CD1 . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CD1 
3686  C CD2 . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CD2 
3687  C CE1 . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CE1 
3688  C CE2 . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CE2 
3689  C CZ  . PHE B 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE D CZ  
3690  N N   . GLU B 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU D N   
3691  C CA  . GLU B 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU D CA  
3692  C C   . GLU B 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU D C   
3693  O O   . GLU B 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU D O   
3694  C CB  . GLU B 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU D CB  
3695  N N   . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D N   
3696  C CA  . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CA  
3697  C C   . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D C   
3698  O O   . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D O   
3699  C CB  . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CB  
3700  C CG  . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CG  
3701  C CD1 . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CD1 
3702  C CD2 . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CD2 
3703  C CE1 . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CE1 
3704  C CE2 . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CE2 
3705  C CZ  . PHE B 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE D CZ  
3706  N N   . CYS B 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS D N   
3707  C CA  . CYS B 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS D CA  
3708  C C   . CYS B 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS D C   
3709  O O   . CYS B 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS D O   
3710  C CB  . CYS B 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS D CB  
3711  S SG  . CYS B 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS D SG  
3712  N N   . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D N   
3713  C CA  . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D CA  
3714  C C   . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D C   
3715  O O   . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D O   
3716  C CB  . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D CB  
3717  C CG  . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D CG  
3718  C CD  . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D CD  
3719  O OE1 . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D OE1 
3720  N NE2 . GLN B 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN D NE2 
3721  N N   . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D N   
3722  C CA  . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D CA  
3723  C C   . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D C   
3724  O O   . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D O   
3725  C CB  . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D CB  
3726  C CG  . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D CG  
3727  C CD1 . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D CD1 
3728  C CD2 . LEU B 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU D CD2 
3729  N N   . SER B 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER D N   
3730  C CA  . SER B 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER D CA  
3731  C C   . SER B 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER D C   
3732  O O   . SER B 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER D O   
3733  C CB  . SER B 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER D CB  
3734  O OG  . SER B 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER D OG  
3735  N N   . THR B 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR D N   
3736  C CA  . THR B 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR D CA  
3737  C C   . THR B 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR D C   
3738  O O   . THR B 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR D O   
3739  C CB  . THR B 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR D CB  
3740  O OG1 . THR B 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR D OG1 
3741  C CG2 . THR B 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR D CG2 
3742  N N   . GLY B 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY D N   
3743  C CA  . GLY B 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY D CA  
3744  C C   . GLY B 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY D C   
3745  O O   . GLY B 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY D O   
3746  N N   . GLY B 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY D N   
3747  C CA  . GLY B 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY D CA  
3748  C C   . GLY B 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY D C   
3749  O O   . GLY B 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY D O   
3750  N N   . SER B 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER D N   
3751  C CA  . SER B 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER D CA  
3752  C C   . SER B 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER D C   
3753  O O   . SER B 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER D O   
3756  N N   . VAL B 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL D N   
3757  C CA  . VAL B 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL D CA  
3758  C C   . VAL B 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL D C   
3759  O O   . VAL B 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL D O   
3760  C CB  . VAL B 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL D CB  
3761  C CG1 . VAL B 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL D CG1 
3762  C CG2 . VAL B 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL D CG2 
3763  N N   . ALA B 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA D N   
3764  C CA  . ALA B 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA D CA  
3765  C C   . ALA B 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA D C   
3766  O O   . ALA B 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA D O   
3767  C CB  . ALA B 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA D CB  
3768  N N   . GLY B 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY D N   
3769  C CA  . GLY B 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY D CA  
3770  C C   . GLY B 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY D C   
3771  O O   . GLY B 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY D O   
3772  N N   . ALA B 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA D N   
3773  C CA  . ALA B 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA D CA  
3774  C C   . ALA B 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA D C   
3775  O O   . ALA B 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA D O   
3776  C CB  . ALA B 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA D CB  
3777  N N   . VAL B 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL D N   
3778  C CA  . VAL B 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL D CA  
3779  C C   . VAL B 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL D C   
3780  O O   . VAL B 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL D O   
3784  N N   . LYS B 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS D N   
3785  C CA  . LYS B 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS D CA  
3786  C C   . LYS B 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS D C   
3787  O O   . LYS B 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS D O   
3793  N N   . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D N   
3794  C CA  . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D CA  
3795  C C   . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D C   
3796  O O   . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D O   
3797  C CB  . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D CB  
3798  C CG  . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D CG  
3799  C CD1 . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D CD1 
3800  C CD2 . LEU B 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU D CD2 
3801  N N   . ASN B 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN D N   
3802  C CA  . ASN B 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN D CA  
3803  C C   . ASN B 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN D C   
3804  O O   . ASN B 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN D O   
3809  N N   . ARG B 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG D N   
3810  C CA  . ARG B 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG D CA  
3811  C C   . ARG B 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG D C   
3812  O O   . ARG B 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG D O   
3813  C CB  . ARG B 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG D CB  
3814  N N   . GLN B 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN D N   
3815  C CA  . GLN B 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN D CA  
3816  C C   . GLN B 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN D C   
3817  O O   . GLN B 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN D O   
3819  N N   . GLN B 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN D N   
3820  C CA  . GLN B 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN D CA  
3821  C C   . GLN B 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN D C   
3822  O O   . GLN B 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN D O   
3828  N N   . THR B 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR D N   
3829  C CA  . THR B 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR D CA  
3830  C C   . THR B 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR D C   
3831  O O   . THR B 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR D O   
3835  N N   . ASP B 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP D N   
3836  C CA  . ASP B 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP D CA  
3837  C C   . ASP B 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP D C   
3838  O O   . ASP B 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP D O   
3843  N N   . MET B 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET D N   
3844  C CA  . MET B 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET D CA  
3845  C C   . MET B 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET D C   
3846  O O   . MET B 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET D O   
3851  N N   . ALA B 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA D N   
3852  C CA  . ALA B 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA D CA  
3853  C C   . ALA B 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA D C   
3854  O O   . ALA B 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA D O   
3855  C CB  . ALA B 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA D CB  
3856  N N   . VAL B 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL D N   
3857  C CA  . VAL B 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL D CA  
3858  C C   . VAL B 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL D C   
3859  O O   . VAL B 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL D O   
3860  C CB  . VAL B 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL D CB  
3861  C CG1 . VAL B 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL D CG1 
3862  C CG2 . VAL B 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL D CG2 
3863  N N   . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D N   
3864  C CA  . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D CA  
3865  C C   . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D C   
3866  O O   . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D O   
3867  C CB  . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D CB  
3868  C CG  . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D CG  
3869  O OD1 . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D OD1 
3870  N ND2 . ASN B 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN D ND2 
3871  N N   . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D N   
3872  C CA  . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CA  
3873  C C   . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D C   
3874  O O   . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D O   
3875  C CB  . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CB  
3876  C CG  . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CG  
3877  C CD1 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CD1 
3878  C CD2 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CD2 
3879  N NE1 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D NE1 
3880  C CE2 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CE2 
3881  C CE3 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CE3 
3882  C CZ2 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CZ2 
3883  C CZ3 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CZ3 
3884  C CH2 . TRP B 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP D CH2 
3885  N N   . ALA B 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA D N   
3886  C CA  . ALA B 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA D CA  
3887  C C   . ALA B 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA D C   
3888  O O   . ALA B 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA D O   
3889  C CB  . ALA B 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA D CB  
3890  N N   . GLY B 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY D N   
3891  C CA  . GLY B 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY D CA  
3892  C C   . GLY B 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY D C   
3893  O O   . GLY B 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY D O   
3894  N N   . GLY B 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY D N   
3895  C CA  . GLY B 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY D CA  
3896  C C   . GLY B 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY D C   
3897  O O   . GLY B 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY D O   
3898  N N   . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D N   
3899  C CA  . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D CA  
3900  C C   . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D C   
3901  O O   . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D O   
3902  C CB  . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D CB  
3903  C CG  . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D CG  
3904  C CD1 . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D CD1 
3905  C CD2 . LEU B 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU D CD2 
3906  N N   . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D N   
3907  C CA  . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D CA  
3908  C C   . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D C   
3909  O O   . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D O   
3910  C CB  . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D CB  
3911  C CG  . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D CG  
3912  N ND1 . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D ND1 
3913  C CD2 . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D CD2 
3914  C CE1 . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D CE1 
3915  N NE2 . HIS B 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS D NE2 
3916  N N   . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D N   
3917  C CA  . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D CA  
3918  C C   . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D C   
3919  O O   . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D O   
3920  C CB  . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D CB  
3921  C CG  . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D CG  
3922  N ND1 . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D ND1 
3923  C CD2 . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D CD2 
3924  C CE1 . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D CE1 
3925  N NE2 . HIS B 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS D NE2 
3926  N N   . ALA B 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA D N   
3927  C CA  . ALA B 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA D CA  
3928  C C   . ALA B 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA D C   
3929  O O   . ALA B 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA D O   
3930  C CB  . ALA B 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA D CB  
3931  N N   . LYS B 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS D N   
3932  C CA  . LYS B 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS D CA  
3933  C C   . LYS B 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS D C   
3934  O O   . LYS B 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS D O   
3940  N N   . LYS B 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS D N   
3941  C CA  . LYS B 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS D CA  
3942  C C   . LYS B 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS D C   
3943  O O   . LYS B 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS D O   
3949  N N   . SER B 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER D N   
3950  C CA  . SER B 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER D CA  
3951  C C   . SER B 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER D C   
3952  O O   . SER B 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER D O   
3955  N N   . GLU B 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU D N   
3956  C CA  . GLU B 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU D CA  
3957  C C   . GLU B 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU D C   
3958  O O   . GLU B 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU D O   
3964  N N   . ALA B 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA D N   
3965  C CA  . ALA B 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA D CA  
3966  C C   . ALA B 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA D C   
3967  O O   . ALA B 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA D O   
3968  C CB  . ALA B 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA D CB  
3969  N N   . SER B 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER D N   
3970  C CA  . SER B 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER D CA  
3971  C C   . SER B 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER D C   
3972  O O   . SER B 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER D O   
3974  N N   . GLY B 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY D N   
3975  C CA  . GLY B 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY D CA  
3976  C C   . GLY B 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY D C   
3977  O O   . GLY B 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY D O   
3978  N N   . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D N   
3979  C CA  . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CA  
3980  C C   . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D C   
3981  O O   . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D O   
3982  C CB  . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CB  
3983  C CG  . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CG  
3984  C CD1 . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CD1 
3985  C CD2 . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CD2 
3986  C CE1 . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CE1 
3987  C CE2 . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CE2 
3988  C CZ  . PHE B 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE D CZ  
3989  N N   . CYS B 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS D N   
3990  C CA  . CYS B 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS D CA  
3991  C C   . CYS B 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS D C   
3992  O O   . CYS B 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS D O   
3995  N N   . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D N   
3996  C CA  . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CA  
3997  C C   . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D C   
3998  O O   . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D O   
3999  C CB  . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CB  
4000  C CG  . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CG  
4001  C CD1 . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CD1 
4002  C CD2 . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CD2 
4003  C CE1 . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CE1 
4004  C CE2 . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CE2 
4005  C CZ  . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D CZ  
4006  O OH  . TYR B 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR D OH  
4014  N N   . ASN B 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN D N   
4015  C CA  . ASN B 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN D CA  
4016  C C   . ASN B 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN D C   
4017  O O   . ASN B 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN D O   
4022  N N   . ASP B 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP D N   
4023  C CA  . ASP B 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP D CA  
4024  C C   . ASP B 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP D C   
4025  O O   . ASP B 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP D O   
4030  N N   . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D N   
4031  C CA  . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D CA  
4032  C C   . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D C   
4033  O O   . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D O   
4034  C CB  . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D CB  
4035  C CG1 . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D CG1 
4036  C CG2 . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D CG2 
4037  C CD1 . ILE B 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE D CD1 
4038  N N   . VAL B 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL D N   
4039  C CA  . VAL B 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL D CA  
4040  C C   . VAL B 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL D C   
4041  O O   . VAL B 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL D O   
4042  C CB  . VAL B 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL D CB  
4043  C CG1 . VAL B 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL D CG1 
4044  C CG2 . VAL B 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL D CG2 
4045  N N   . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D N   
4046  C CA  . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D CA  
4047  C C   . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D C   
4048  O O   . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D O   
4049  C CB  . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D CB  
4050  C CG  . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D CG  
4051  C CD1 . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D CD1 
4052  C CD2 . LEU B 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU D CD2 
4053  N N   . ALA B 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA D N   
4054  C CA  . ALA B 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA D CA  
4055  C C   . ALA B 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA D C   
4056  O O   . ALA B 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA D O   
4057  C CB  . ALA B 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA D CB  
4058  N N   . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D N   
4059  C CA  . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D CA  
4060  C C   . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D C   
4061  O O   . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D O   
4062  C CB  . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D CB  
4063  C CG1 . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D CG1 
4064  C CG2 . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D CG2 
4065  C CD1 . ILE B 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE D CD1 
4066  N N   . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D N   
4067  C CA  . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D CA  
4068  C C   . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D C   
4069  O O   . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D O   
4070  C CB  . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D CB  
4071  C CG  . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D CG  
4072  C CD1 . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D CD1 
4073  C CD2 . LEU B 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU D CD2 
4074  N N   . GLU B 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU D N   
4075  C CA  . GLU B 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU D CA  
4076  C C   . GLU B 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU D C   
4077  O O   . GLU B 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU D O   
4083  N N   . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D N   
4084  C CA  . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D CA  
4085  C C   . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D C   
4086  O O   . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D O   
4087  C CB  . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D CB  
4088  C CG  . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D CG  
4089  C CD1 . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D CD1 
4090  C CD2 . LEU B 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU D CD2 
4091  N N   . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D N   
4092  C CA  . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D CA  
4093  C C   . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D C   
4094  O O   . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D O   
4095  C CB  . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D CB  
4096  C CG  . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D CG  
4097  C CD1 . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D CD1 
4098  C CD2 . LEU B 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU D CD2 
4099  N N   . LYS B 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS D N   
4100  C CA  . LYS B 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS D CA  
4101  C C   . LYS B 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS D C   
4102  O O   . LYS B 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS D O   
4108  N N   . TYR B 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR D N   
4109  C CA  . TYR B 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR D CA  
4110  C C   . TYR B 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR D C   
4111  O O   . TYR B 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR D O   
4120  N N   . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D N   
4121  C CA  . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D CA  
4122  C C   . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D C   
4123  O O   . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D O   
4124  C CB  . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D CB  
4125  C CG  . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D CG  
4126  N ND1 . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D ND1 
4127  C CD2 . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D CD2 
4128  C CE1 . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D CE1 
4129  N NE2 . HIS B 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS D NE2 
4130  N N   . GLN B 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN D N   
4131  C CA  . GLN B 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN D CA  
4132  C C   . GLN B 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN D C   
4133  O O   . GLN B 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN D O   
4139  N N   . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D N   
4140  C CA  . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D CA  
4141  C C   . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D C   
4142  O O   . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D O   
4143  C CB  . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D CB  
4144  C CG  . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D CG  
4145  C CD  . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D CD  
4146  N NE  . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D NE  
4147  C CZ  . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D CZ  
4148  N NH1 . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D NH1 
4149  N NH2 . ARG B 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG D NH2 
4150  N N   . VAL B 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL D N   
4151  C CA  . VAL B 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL D CA  
4152  C C   . VAL B 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL D C   
4153  O O   . VAL B 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL D O   
4154  C CB  . VAL B 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL D CB  
4155  C CG1 . VAL B 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL D CG1 
4156  C CG2 . VAL B 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL D CG2 
4157  N N   . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D N   
4158  C CA  . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D CA  
4159  C C   . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D C   
4160  O O   . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D O   
4161  C CB  . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D CB  
4162  C CG  . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D CG  
4163  C CD1 . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D CD1 
4164  C CD2 . LEU B 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU D CD2 
4165  N N   . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D N   
4166  C CA  . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CA  
4167  C C   . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D C   
4168  O O   . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D O   
4169  C CB  . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CB  
4170  C CG  . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CG  
4171  C CD1 . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CD1 
4172  C CD2 . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CD2 
4173  C CE1 . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CE1 
4174  C CE2 . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CE2 
4175  C CZ  . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D CZ  
4176  O OH  . TYR B 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR D OH  
4177  N N   . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D N   
4178  C CA  . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D CA  
4179  C C   . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D C   
4180  O O   . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D O   
4181  C CB  . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D CB  
4182  C CG1 . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D CG1 
4183  C CG2 . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D CG2 
4184  C CD1 . ILE B 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE D CD1 
4185  N N   . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D N   
4186  C CA  . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D CA  
4187  C C   . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D C   
4188  O O   . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D O   
4189  C CB  . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D CB  
4190  C CG  . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D CG  
4191  O OD1 . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D OD1 
4192  O OD2 . ASP B 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP D OD2 
4193  N N   . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D N   
4194  C CA  . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D CA  
4195  C C   . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D C   
4196  O O   . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D O   
4197  C CB  . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D CB  
4198  C CG1 . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D CG1 
4199  C CG2 . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D CG2 
4200  C CD1 . ILE B 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE D CD1 
4201  N N   . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D N   
4202  C CA  . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D CA  
4203  C C   . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D C   
4204  O O   . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D O   
4205  C CB  . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D CB  
4206  C CG  . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D CG  
4207  O OD1 . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D OD1 
4208  O OD2 . ASP B 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP D OD2 
4209  N N   . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D N   
4210  C CA  . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D CA  
4211  C C   . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D C   
4212  O O   . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D O   
4213  C CB  . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D CB  
4214  C CG1 . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D CG1 
4215  C CG2 . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D CG2 
4216  C CD1 . ILE B 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE D CD1 
4217  N N   . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D N   
4218  C CA  . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D CA  
4219  C C   . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D C   
4220  O O   . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D O   
4221  C CB  . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D CB  
4222  C CG  . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D CG  
4223  N ND1 . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D ND1 
4224  C CD2 . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D CD2 
4225  C CE1 . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D CE1 
4226  N NE2 . HIS B 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS D NE2 
4227  N N   . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D N   
4228  C CA  . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D CA  
4229  C C   . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D C   
4230  O O   . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D O   
4231  C CB  . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D CB  
4232  C CG  . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D CG  
4233  N ND1 . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D ND1 
4234  C CD2 . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D CD2 
4235  C CE1 . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D CE1 
4236  N NE2 . HIS B 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS D NE2 
4237  N N   . GLY B 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY D N   
4238  C CA  . GLY B 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY D CA  
4239  C C   . GLY B 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY D C   
4240  O O   . GLY B 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY D O   
4241  N N   . ASP B 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP D N   
4242  C CA  . ASP B 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP D CA  
4243  C C   . ASP B 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP D C   
4244  O O   . ASP B 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP D O   
4249  N N   . GLY B 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY D N   
4250  C CA  . GLY B 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY D CA  
4251  C C   . GLY B 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY D C   
4252  O O   . GLY B 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY D O   
4253  N N   . VAL B 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL D N   
4254  C CA  . VAL B 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL D CA  
4255  C C   . VAL B 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL D C   
4256  O O   . VAL B 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL D O   
4257  C CB  . VAL B 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL D CB  
4258  C CG1 . VAL B 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL D CG1 
4259  C CG2 . VAL B 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL D CG2 
4260  N N   . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D N   
4261  C CA  . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D CA  
4262  C C   . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D C   
4263  O O   . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D O   
4264  C CB  . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D CB  
4265  C CG  . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D CG  
4266  C CD  . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D CD  
4267  O OE1 . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D OE1 
4268  O OE2 . GLU B 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU D OE2 
4269  N N   . GLU B 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU D N   
4270  C CA  . GLU B 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU D CA  
4271  C C   . GLU B 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU D C   
4272  O O   . GLU B 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU D O   
4278  N N   . ALA B 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA D N   
4279  C CA  . ALA B 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA D CA  
4280  C C   . ALA B 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA D C   
4281  O O   . ALA B 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA D O   
4282  C CB  . ALA B 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA D CB  
4283  N N   . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D N   
4284  C CA  . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CA  
4285  C C   . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D C   
4286  O O   . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D O   
4287  C CB  . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CB  
4288  C CG  . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CG  
4289  C CD1 . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CD1 
4290  C CD2 . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CD2 
4291  C CE1 . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CE1 
4292  C CE2 . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CE2 
4293  C CZ  . PHE B 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE D CZ  
4294  N N   . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D N   
4295  C CA  . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CA  
4296  C C   . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D C   
4297  O O   . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D O   
4298  C CB  . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CB  
4299  C CG  . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CG  
4300  C CD1 . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CD1 
4301  C CD2 . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CD2 
4302  C CE1 . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CE1 
4303  C CE2 . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CE2 
4304  C CZ  . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D CZ  
4305  O OH  . TYR B 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR D OH  
4306  N N   . THR B 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR D N   
4307  C CA  . THR B 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR D CA  
4308  C C   . THR B 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR D C   
4309  O O   . THR B 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR D O   
4313  N N   . THR B 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR D N   
4314  C CA  . THR B 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR D CA  
4315  C C   . THR B 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR D C   
4316  O O   . THR B 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR D O   
4317  C CB  . THR B 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR D CB  
4318  O OG1 . THR B 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR D OG1 
4319  C CG2 . THR B 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR D CG2 
4320  N N   . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D N   
4321  C CA  . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D CA  
4322  C C   . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D C   
4323  O O   . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D O   
4324  C CB  . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D CB  
4325  C CG  . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D CG  
4326  O OD1 . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D OD1 
4327  O OD2 . ASP B 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP D OD2 
4328  N N   . ARG B 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG D N   
4329  C CA  . ARG B 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG D CA  
4330  C C   . ARG B 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG D C   
4331  O O   . ARG B 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG D O   
4339  N N   . VAL B 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL D N   
4340  C CA  . VAL B 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL D CA  
4341  C C   . VAL B 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL D C   
4342  O O   . VAL B 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL D O   
4343  C CB  . VAL B 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL D CB  
4344  C CG1 . VAL B 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL D CG1 
4345  C CG2 . VAL B 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL D CG2 
4346  N N   . MET B 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET D N   
4347  C CA  . MET B 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET D CA  
4348  C C   . MET B 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET D C   
4349  O O   . MET B 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET D O   
4354  N N   . THR B 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR D N   
4355  C CA  . THR B 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR D CA  
4356  C C   . THR B 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR D C   
4357  O O   . THR B 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR D O   
4358  C CB  . THR B 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR D CB  
4359  O OG1 . THR B 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR D OG1 
4360  C CG2 . THR B 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR D CG2 
4361  N N   . VAL B 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL D N   
4362  C CA  . VAL B 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL D CA  
4363  C C   . VAL B 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL D C   
4364  O O   . VAL B 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL D O   
4365  C CB  . VAL B 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL D CB  
4366  C CG1 . VAL B 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL D CG1 
4367  C CG2 . VAL B 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL D CG2 
4368  N N   . SER B 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER D N   
4369  C CA  . SER B 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER D CA  
4370  C C   . SER B 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER D C   
4371  O O   . SER B 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER D O   
4372  C CB  . SER B 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER D CB  
4373  O OG  . SER B 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER D OG  
4374  N N   . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D N   
4375  C CA  . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CA  
4376  C C   . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D C   
4377  O O   . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D O   
4378  C CB  . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CB  
4379  C CG  . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CG  
4380  C CD1 . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CD1 
4381  C CD2 . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CD2 
4382  C CE1 . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CE1 
4383  C CE2 . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CE2 
4384  C CZ  . PHE B 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE D CZ  
4385  N N   . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D N   
4386  C CA  . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D CA  
4387  C C   . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D C   
4388  O O   . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D O   
4389  C CB  . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D CB  
4390  C CG  . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D CG  
4391  N ND1 . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D ND1 
4392  C CD2 . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D CD2 
4393  C CE1 . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D CE1 
4394  N NE2 . HIS B 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS D NE2 
4395  N N   . LYS B 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS D N   
4396  C CA  . LYS B 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS D CA  
4397  C C   . LYS B 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS D C   
4398  O O   . LYS B 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS D O   
4404  N N   . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D N   
4405  C CA  . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CA  
4406  C C   . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D C   
4407  O O   . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D O   
4408  C CB  . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CB  
4409  C CG  . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CG  
4410  C CD1 . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CD1 
4411  C CD2 . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CD2 
4412  C CE1 . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CE1 
4413  C CE2 . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CE2 
4414  C CZ  . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D CZ  
4415  O OH  . TYR B 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR D OH  
4416  N N   . GLY B 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY D N   
4417  C CA  . GLY B 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY D CA  
4418  C C   . GLY B 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY D C   
4419  O O   . GLY B 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY D O   
4420  N N   . GLU B 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU D N   
4421  C CA  . GLU B 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU D CA  
4422  C C   . GLU B 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU D C   
4423  O O   . GLU B 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU D O   
4429  N N   . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D N   
4430  C CA  . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CA  
4431  C C   . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D C   
4432  O O   . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D O   
4433  C CB  . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CB  
4434  C CG  . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CG  
4435  C CD1 . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CD1 
4436  C CD2 . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CD2 
4437  C CE1 . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CE1 
4438  C CE2 . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CE2 
4439  C CZ  . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D CZ  
4440  O OH  . TYR B 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR D OH  
4441  N N   . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D N   
4442  C CA  . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CA  
4443  C C   . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D C   
4444  O O   . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D O   
4445  C CB  . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CB  
4446  C CG  . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CG  
4447  C CD1 . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CD1 
4448  C CD2 . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CD2 
4449  C CE1 . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CE1 
4450  C CE2 . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CE2 
4451  C CZ  . PHE B 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE D CZ  
4452  N N   . PRO B 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO D N   
4453  C CA  . PRO B 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO D CA  
4454  C C   . PRO B 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO D C   
4455  O O   . PRO B 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO D O   
4456  C CB  . PRO B 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO D CB  
4457  C CG  . PRO B 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO D CG  
4458  C CD  . PRO B 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO D CD  
4459  N N   . GLY B 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY D N   
4460  C CA  . GLY B 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY D CA  
4461  C C   . GLY B 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY D C   
4462  O O   . GLY B 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY D O   
4463  N N   . THR B 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR D N   
4464  C CA  . THR B 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR D CA  
4465  C C   . THR B 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR D C   
4466  O O   . THR B 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR D O   
4470  N N   . GLY B 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY D N   
4471  C CA  . GLY B 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY D CA  
4472  C C   . GLY B 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY D C   
4473  O O   . GLY B 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY D O   
4474  N N   . ASP B 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP D N   
4475  C CA  . ASP B 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP D CA  
4476  C C   . ASP B 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP D C   
4477  O O   . ASP B 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP D O   
4482  N N   . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D N   
4483  C CA  . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D CA  
4484  C C   . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D C   
4485  O O   . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D O   
4486  C CB  . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D CB  
4487  C CG  . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D CG  
4488  C CD1 . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D CD1 
4489  C CD2 . LEU B 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU D CD2 
4490  N N   . ARG B 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG D N   
4491  C CA  . ARG B 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG D CA  
4492  C C   . ARG B 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG D C   
4493  O O   . ARG B 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG D O   
4501  N N   . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D N   
4502  C CA  . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D CA  
4503  C C   . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D C   
4504  O O   . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D O   
4505  C CB  . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D CB  
4506  C CG  . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D CG  
4507  O OD1 . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D OD1 
4508  O OD2 . ASP B 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP D OD2 
4509  N N   . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D N   
4510  C CA  . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D CA  
4511  C C   . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D C   
4512  O O   . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D O   
4513  C CB  . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D CB  
4514  C CG1 . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D CG1 
4515  C CG2 . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D CG2 
4516  C CD1 . ILE B 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE D CD1 
4517  N N   . GLY B 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY D N   
4518  C CA  . GLY B 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY D CA  
4519  C C   . GLY B 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY D C   
4520  O O   . GLY B 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY D O   
4521  N N   . ALA B 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA D N   
4522  C CA  . ALA B 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA D CA  
4523  C C   . ALA B 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA D C   
4524  O O   . ALA B 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA D O   
4525  C CB  . ALA B 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA D CB  
4526  N N   . GLY B 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY D N   
4527  C CA  . GLY B 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY D CA  
4528  C C   . GLY B 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY D C   
4529  O O   . GLY B 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY D O   
4530  N N   . LYS B 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS D N   
4531  C CA  . LYS B 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS D CA  
4532  C C   . LYS B 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS D C   
4533  O O   . LYS B 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS D O   
4534  C CB  . LYS B 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS D CB  
4535  N N   . GLY B 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY D N   
4536  C CA  . GLY B 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY D CA  
4537  C C   . GLY B 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY D C   
4538  O O   . GLY B 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY D O   
4539  N N   . LYS B 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS D N   
4540  C CA  . LYS B 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS D CA  
4541  C C   . LYS B 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS D C   
4542  O O   . LYS B 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS D O   
4548  N N   . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D N   
4549  C CA  . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CA  
4550  C C   . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D C   
4551  O O   . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D O   
4552  C CB  . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CB  
4553  C CG  . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CG  
4554  C CD1 . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CD1 
4555  C CD2 . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CD2 
4556  C CE1 . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CE1 
4557  C CE2 . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CE2 
4558  C CZ  . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D CZ  
4559  O OH  . TYR B 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR D OH  
4560  N N   . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D N   
4561  C CA  . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CA  
4562  C C   . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D C   
4563  O O   . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D O   
4564  C CB  . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CB  
4565  C CG  . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CG  
4566  C CD1 . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CD1 
4567  C CD2 . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CD2 
4568  C CE1 . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CE1 
4569  C CE2 . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CE2 
4570  C CZ  . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D CZ  
4571  O OH  . TYR B 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR D OH  
4572  N N   . ALA B 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA D N   
4573  C CA  . ALA B 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA D CA  
4574  C C   . ALA B 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA D C   
4575  O O   . ALA B 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA D O   
4576  C CB  . ALA B 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA D CB  
4577  N N   . VAL B 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL D N   
4578  C CA  . VAL B 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL D CA  
4579  C C   . VAL B 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL D C   
4580  O O   . VAL B 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL D O   
4581  C CB  . VAL B 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL D CB  
4582  C CG1 . VAL B 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL D CG1 
4583  C CG2 . VAL B 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL D CG2 
4584  N N   . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D N   
4585  C CA  . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D CA  
4586  C C   . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D C   
4587  O O   . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D O   
4588  C CB  . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D CB  
4589  C CG  . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D CG  
4590  O OD1 . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D OD1 
4591  N ND2 . ASN B 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN D ND2 
4592  N N   . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D N   
4593  C CA  . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CA  
4594  C C   . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D C   
4595  O O   . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D O   
4596  C CB  . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CB  
4597  C CG  . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CG  
4598  C CD1 . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CD1 
4599  C CD2 . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CD2 
4600  C CE1 . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CE1 
4601  C CE2 . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CE2 
4602  C CZ  . PHE B 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE D CZ  
4603  N N   . PRO B 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO D N   
4604  C CA  . PRO B 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO D CA  
4605  C C   . PRO B 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO D C   
4606  O O   . PRO B 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO D O   
4607  C CB  . PRO B 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO D CB  
4608  C CG  . PRO B 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO D CG  
4609  C CD  . PRO B 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO D CD  
4610  N N   . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D N   
4611  C CA  . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D CA  
4612  C C   . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D C   
4613  O O   . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D O   
4614  C CB  . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D CB  
4615  C CG  . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D CG  
4616  S SD  . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D SD  
4617  C CE  . MET B 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET D CE  
4618  N N   . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D N   
4619  C CA  . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D CA  
4620  C C   . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D C   
4621  O O   . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D O   
4622  C CB  . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D CB  
4623  C CG  . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D CG  
4624  C CD  . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D CD  
4625  N NE  . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D NE  
4626  C CZ  . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D CZ  
4627  N NH1 . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D NH1 
4628  N NH2 . ARG B 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG D NH2 
4629  N N   . ASP B 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP D N   
4630  C CA  . ASP B 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP D CA  
4631  C C   . ASP B 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP D C   
4632  O O   . ASP B 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP D O   
4637  N N   . GLY B 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY D N   
4638  C CA  . GLY B 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY D CA  
4639  C C   . GLY B 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY D C   
4640  O O   . GLY B 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY D O   
4641  N N   . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D N   
4642  C CA  . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D CA  
4643  C C   . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D C   
4644  O O   . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D O   
4645  C CB  . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D CB  
4646  C CG1 . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D CG1 
4647  C CG2 . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D CG2 
4648  C CD1 . ILE B 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE D CD1 
4649  N N   . ASP B 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP D N   
4650  C CA  . ASP B 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP D CA  
4651  C C   . ASP B 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP D C   
4652  O O   . ASP B 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP D O   
4657  N N   . ASP B 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP D N   
4658  C CA  . ASP B 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP D CA  
4659  C C   . ASP B 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP D C   
4660  O O   . ASP B 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP D O   
4665  N N   . GLU B 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU D N   
4666  C CA  . GLU B 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU D CA  
4667  C C   . GLU B 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU D C   
4668  O O   . GLU B 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU D O   
4669  C CB  . GLU B 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU D CB  
4670  N N   . SER B 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER D N   
4671  C CA  . SER B 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER D CA  
4672  C C   . SER B 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER D C   
4673  O O   . SER B 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER D O   
4674  C CB  . SER B 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER D CB  
4675  O OG  . SER B 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER D OG  
4676  N N   . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D N   
4677  C CA  . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CA  
4678  C C   . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D C   
4679  O O   . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D O   
4680  C CB  . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CB  
4681  C CG  . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CG  
4682  C CD1 . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CD1 
4683  C CD2 . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CD2 
4684  C CE1 . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CE1 
4685  C CE2 . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CE2 
4686  C CZ  . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D CZ  
4687  O OH  . TYR B 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR D OH  
4688  N N   . GLY B 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY D N   
4689  C CA  . GLY B 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY D CA  
4690  C C   . GLY B 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY D C   
4691  O O   . GLY B 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY D O   
4692  N N   . GLN B 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN D N   
4693  C CA  . GLN B 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN D CA  
4694  C C   . GLN B 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN D C   
4695  O O   . GLN B 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN D O   
4701  N N   . ILE B 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE D N   
4702  C CA  . ILE B 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE D CA  
4703  C C   . ILE B 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE D C   
4704  O O   . ILE B 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE D O   
4709  N N   . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D N   
4710  C CA  . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CA  
4711  C C   . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D C   
4712  O O   . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D O   
4713  C CB  . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CB  
4714  C CG  . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CG  
4715  C CD1 . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CD1 
4716  C CD2 . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CD2 
4717  C CE1 . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CE1 
4718  C CE2 . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CE2 
4719  C CZ  . PHE B 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE D CZ  
4720  N N   . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D N   
4721  C CA  . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D CA  
4722  C C   . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D C   
4723  O O   . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D O   
4724  C CB  . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D CB  
4725  C CG  . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D CG  
4726  C CD  . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D CD  
4727  C CE  . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D CE  
4728  N NZ  . LYS B 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS D NZ  
4729  N N   . PRO B 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO D N   
4730  C CA  . PRO B 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO D CA  
4731  C C   . PRO B 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO D C   
4732  O O   . PRO B 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO D O   
4733  C CB  . PRO B 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO D CB  
4734  C CG  . PRO B 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO D CG  
4735  C CD  . PRO B 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO D CD  
4736  N N   . ILE B 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE D N   
4737  C CA  . ILE B 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE D CA  
4738  C C   . ILE B 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE D C   
4739  O O   . ILE B 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE D O   
4744  N N   . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D N   
4745  C CA  . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D CA  
4746  C C   . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D C   
4747  O O   . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D O   
4748  C CB  . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D CB  
4749  C CG1 . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D CG1 
4750  C CG2 . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D CG2 
4751  C CD1 . ILE B 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE D CD1 
4752  N N   . SER B 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER D N   
4753  C CA  . SER B 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER D CA  
4754  C C   . SER B 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER D C   
4755  O O   . SER B 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER D O   
4756  C CB  . SER B 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER D CB  
4757  O OG  . SER B 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER D OG  
4758  N N   . LYS B 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS D N   
4759  C CA  . LYS B 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS D CA  
4760  C C   . LYS B 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS D C   
4761  O O   . LYS B 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS D O   
4767  N N   . VAL B 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL D N   
4768  C CA  . VAL B 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL D CA  
4769  C C   . VAL B 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL D C   
4770  O O   . VAL B 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL D O   
4771  C CB  . VAL B 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL D CB  
4772  C CG1 . VAL B 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL D CG1 
4773  C CG2 . VAL B 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL D CG2 
4774  N N   . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D N   
4775  C CA  . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D CA  
4776  C C   . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D C   
4777  O O   . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D O   
4778  C CB  . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D CB  
4779  C CG  . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D CG  
4780  S SD  . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D SD  
4781  C CE  . MET B 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET D CE  
4782  N N   . GLU B 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU D N   
4783  C CA  . GLU B 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU D CA  
4784  C C   . GLU B 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU D C   
4785  O O   . GLU B 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU D O   
4786  C CB  . GLU B 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU D CB  
4787  N N   . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D N   
4788  C CA  . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D CA  
4789  C C   . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D C   
4790  O O   . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D O   
4791  C CB  . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D CB  
4792  C CG  . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D CG  
4793  S SD  . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D SD  
4794  C CE  . MET B 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET D CE  
4795  N N   . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D N   
4796  C CA  . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CA  
4797  C C   . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D C   
4798  O O   . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D O   
4799  C CB  . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CB  
4800  C CG  . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CG  
4801  C CD1 . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CD1 
4802  C CD2 . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CD2 
4803  C CE1 . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CE1 
4804  C CE2 . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CE2 
4805  C CZ  . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D CZ  
4806  O OH  . TYR B 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR D OH  
4807  N N   . GLN B 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN D N   
4808  C CA  . GLN B 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN D CA  
4809  C C   . GLN B 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN D C   
4810  O O   . GLN B 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN D O   
4816  N N   . PRO B 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO D N   
4817  C CA  . PRO B 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO D CA  
4818  C C   . PRO B 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO D C   
4819  O O   . PRO B 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO D O   
4820  C CB  . PRO B 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO D CB  
4821  C CG  . PRO B 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO D CG  
4822  C CD  . PRO B 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO D CD  
4823  N N   . SER B 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER D N   
4824  C CA  . SER B 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER D CA  
4825  C C   . SER B 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER D C   
4826  O O   . SER B 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER D O   
4829  N N   . ALA B 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA D N   
4830  C CA  . ALA B 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA D CA  
4831  C C   . ALA B 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA D C   
4832  O O   . ALA B 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA D O   
4833  C CB  . ALA B 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA D CB  
4834  N N   . VAL B 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL D N   
4835  C CA  . VAL B 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL D CA  
4836  C C   . VAL B 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL D C   
4837  O O   . VAL B 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL D O   
4838  C CB  . VAL B 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL D CB  
4839  C CG1 . VAL B 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL D CG1 
4840  C CG2 . VAL B 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL D CG2 
4841  N N   . VAL B 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL D N   
4842  C CA  . VAL B 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL D CA  
4843  C C   . VAL B 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL D C   
4844  O O   . VAL B 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL D O   
4845  C CB  . VAL B 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL D CB  
4846  C CG1 . VAL B 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL D CG1 
4847  C CG2 . VAL B 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL D CG2 
4848  N N   . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D N   
4849  C CA  . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D CA  
4850  C C   . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D C   
4851  O O   . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D O   
4852  C CB  . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D CB  
4853  C CG  . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D CG  
4854  C CD1 . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D CD1 
4855  C CD2 . LEU B 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU D CD2 
4856  N N   . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D N   
4857  C CA  . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D CA  
4858  C C   . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D C   
4859  O O   . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D O   
4860  C CB  . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D CB  
4861  C CG  . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D CG  
4862  C CD  . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D CD  
4863  O OE1 . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D OE1 
4864  N NE2 . GLN B 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN D NE2 
4865  N N   . CYS B 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS D N   
4866  C CA  . CYS B 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS D CA  
4867  C C   . CYS B 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS D C   
4868  O O   . CYS B 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS D O   
4869  C CB  . CYS B 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS D CB  
4870  S SG  . CYS B 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS D SG  
4871  N N   . GLY B 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY D N   
4872  C CA  . GLY B 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY D CA  
4873  C C   . GLY B 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY D C   
4874  O O   . GLY B 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY D O   
4875  N N   . ALA B 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA D N   
4876  C CA  . ALA B 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA D CA  
4877  C C   . ALA B 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA D C   
4878  O O   . ALA B 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA D O   
4879  C CB  . ALA B 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA D CB  
4880  N N   . ASP B 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP D N   
4881  C CA  . ASP B 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP D CA  
4882  C C   . ASP B 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP D C   
4883  O O   . ASP B 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP D O   
4888  N N   . SER B 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER D N   
4889  C CA  . SER B 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER D CA  
4890  C C   . SER B 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER D C   
4891  O O   . SER B 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER D O   
4892  C CB  . SER B 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER D CB  
4893  O OG  . SER B 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER D OG  
4894  N N   . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D N   
4895  C CA  . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D CA  
4896  C C   . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D C   
4897  O O   . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D O   
4898  C CB  . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D CB  
4899  C CG  . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D CG  
4900  C CD1 . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D CD1 
4901  C CD2 . LEU B 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU D CD2 
4902  N N   . SER B 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER D N   
4903  C CA  . SER B 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER D CA  
4904  C C   . SER B 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER D C   
4905  O O   . SER B 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER D O   
4906  C CB  . SER B 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER D CB  
4907  O OG  . SER B 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER D OG  
4908  N N   . GLY B 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY D N   
4909  C CA  . GLY B 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY D CA  
4910  C C   . GLY B 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY D C   
4911  O O   . GLY B 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY D O   
4931  N N   . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D N   
4932  C CA  . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D CA  
4933  C C   . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D C   
4934  O O   . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D O   
4935  C CB  . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D CB  
4936  C CG  . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D CG  
4937  C CD1 . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D CD1 
4938  C CD2 . LEU B 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU D CD2 
4939  N N   . GLY B 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY D N   
4940  C CA  . GLY B 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY D CA  
4941  C C   . GLY B 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY D C   
4942  O O   . GLY B 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY D O   
4943  N N   . CYS B 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS D N   
4944  C CA  . CYS B 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS D CA  
4945  C C   . CYS B 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS D C   
4946  O O   . CYS B 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS D O   
4947  C CB  . CYS B 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS D CB  
4948  S SG  . CYS B 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS D SG  
4949  N N   . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D N   
4950  C CA  . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CA  
4951  C C   . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D C   
4952  O O   . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D O   
4953  C CB  . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CB  
4954  C CG  . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CG  
4955  C CD1 . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CD1 
4956  C CD2 . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CD2 
4957  C CE1 . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CE1 
4958  C CE2 . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CE2 
4959  C CZ  . PHE B 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE D CZ  
4960  N N   . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D N   
4961  C CA  . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D CA  
4962  C C   . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D C   
4963  O O   . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D O   
4964  C CB  . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D CB  
4965  C CG  . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D CG  
4966  O OD1 . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D OD1 
4967  N ND2 . ASN B 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN D ND2 
4968  N N   . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D N   
4969  C CA  . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D CA  
4970  C C   . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D C   
4971  O O   . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D O   
4972  C CB  . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D CB  
4973  C CG  . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D CG  
4974  C CD1 . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D CD1 
4975  C CD2 . LEU B 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU D CD2 
4976  N N   . THR B 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR D N   
4977  C CA  . THR B 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR D CA  
4978  C C   . THR B 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR D C   
4979  O O   . THR B 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR D O   
4980  C CB  . THR B 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR D CB  
4981  O OG1 . THR B 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR D OG1 
4982  C CG2 . THR B 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR D CG2 
4983  N N   . VAL B 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL D N   
4984  C CA  . VAL B 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL D CA  
4985  C C   . VAL B 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL D C   
4986  O O   . VAL B 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL D O   
4987  C CB  . VAL B 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL D CB  
4988  C CG1 . VAL B 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL D CG1 
4989  C CG2 . VAL B 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL D CG2 
4990  N N   . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D N   
4991  C CA  . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D CA  
4992  C C   . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D C   
4993  O O   . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D O   
4994  C CB  . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D CB  
4995  C CG  . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D CG  
4996  C CD  . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D CD  
4997  C CE  . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D CE  
4998  N NZ  . LYS B 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS D NZ  
4999  N N   . GLY B 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY D N   
5000  C CA  . GLY B 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY D CA  
5001  C C   . GLY B 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY D C   
5002  O O   . GLY B 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY D O   
5003  N N   . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D N   
5004  C CA  . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D CA  
5005  C C   . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D C   
5006  O O   . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D O   
5007  C CB  . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D CB  
5008  C CG  . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D CG  
5009  N ND1 . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D ND1 
5010  C CD2 . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D CD2 
5011  C CE1 . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D CE1 
5012  N NE2 . HIS B 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS D NE2 
5013  N N   . ALA B 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA D N   
5014  C CA  . ALA B 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA D CA  
5015  C C   . ALA B 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA D C   
5016  O O   . ALA B 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA D O   
5017  C CB  . ALA B 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA D CB  
5018  N N   . LYS B 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS D N   
5019  C CA  . LYS B 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS D CA  
5020  C C   . LYS B 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS D C   
5021  O O   . LYS B 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS D O   
5027  N N   . CYS B 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS D N   
5028  C CA  . CYS B 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS D CA  
5029  C C   . CYS B 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS D C   
5030  O O   . CYS B 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS D O   
5033  N N   . VAL B 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL D N   
5034  C CA  . VAL B 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL D CA  
5035  C C   . VAL B 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL D C   
5036  O O   . VAL B 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL D O   
5037  C CB  . VAL B 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL D CB  
5038  C CG1 . VAL B 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL D CG1 
5039  C CG2 . VAL B 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL D CG2 
5040  N N   . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D N   
5041  C CA  . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D CA  
5042  C C   . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D C   
5043  O O   . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D O   
5044  C CB  . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D CB  
5045  C CG  . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D CG  
5046  C CD  . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D CD  
5047  O OE1 . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D OE1 
5048  O OE2 . GLU B 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU D OE2 
5049  N N   . VAL B 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL D N   
5050  C CA  . VAL B 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL D CA  
5051  C C   . VAL B 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL D C   
5052  O O   . VAL B 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL D O   
5053  C CB  . VAL B 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL D CB  
5054  C CG1 . VAL B 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL D CG1 
5055  C CG2 . VAL B 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL D CG2 
5056  N N   . VAL B 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL D N   
5057  C CA  . VAL B 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL D CA  
5058  C C   . VAL B 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL D C   
5059  O O   . VAL B 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL D O   
5060  C CB  . VAL B 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL D CB  
5061  C CG1 . VAL B 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL D CG1 
5062  C CG2 . VAL B 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL D CG2 
5063  N N   . LYS B 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS D N   
5064  C CA  . LYS B 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS D CA  
5065  C C   . LYS B 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS D C   
5066  O O   . LYS B 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS D O   
5072  N N   . THR B 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR D N   
5073  C CA  . THR B 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR D CA  
5074  C C   . THR B 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR D C   
5075  O O   . THR B 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR D O   
5076  C CB  . THR B 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR D CB  
5077  O OG1 . THR B 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR D OG1 
5078  C CG2 . THR B 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR D CG2 
5079  N N   . PHE B 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE D N   
5080  C CA  . PHE B 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE D CA  
5081  C C   . PHE B 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE D C   
5082  O O   . PHE B 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE D O   
5090  N N   . ASN B 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN D N   
5091  C CA  . ASN B 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN D CA  
5092  C C   . ASN B 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN D C   
5093  O O   . ASN B 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN D O   
5094  C CB  . ASN B 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN D CB  
5095  N N   . LEU B 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU D N   
5096  C CA  . LEU B 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU D CA  
5097  C C   . LEU B 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU D C   
5098  O O   . LEU B 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU D O   
5103  N N   . PRO B 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO D N   
5104  C CA  . PRO B 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO D CA  
5105  C C   . PRO B 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO D C   
5106  O O   . PRO B 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO D O   
5107  C CB  . PRO B 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO D CB  
5108  C CG  . PRO B 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO D CG  
5109  C CD  . PRO B 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO D CD  
5110  N N   . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D N   
5111  C CA  . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D CA  
5112  C C   . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D C   
5113  O O   . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D O   
5114  C CB  . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D CB  
5115  C CG  . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D CG  
5116  C CD1 . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D CD1 
5117  C CD2 . LEU B 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU D CD2 
5118  N N   . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D N   
5119  C CA  . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D CA  
5120  C C   . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D C   
5121  O O   . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D O   
5122  C CB  . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D CB  
5123  C CG  . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D CG  
5124  C CD1 . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D CD1 
5125  C CD2 . LEU B 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU D CD2 
5126  N N   . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D N   
5127  C CA  . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D CA  
5128  C C   . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D C   
5129  O O   . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D O   
5130  C CB  . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D CB  
5131  C CG  . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D CG  
5132  S SD  . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D SD  
5133  C CE  . MET B 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET D CE  
5134  N N   . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D N   
5135  C CA  . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D CA  
5136  C C   . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D C   
5137  O O   . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D O   
5138  C CB  . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D CB  
5139  C CG  . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D CG  
5140  C CD1 . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D CD1 
5141  C CD2 . LEU B 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU D CD2 
5142  N N   . GLY B 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY D N   
5143  C CA  . GLY B 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY D CA  
5144  C C   . GLY B 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY D C   
5145  O O   . GLY B 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY D O   
5146  N N   . GLY B 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY D N   
5147  C CA  . GLY B 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY D CA  
5148  C C   . GLY B 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY D C   
5149  O O   . GLY B 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY D O   
5150  N N   . GLY B 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY D N   
5151  C CA  . GLY B 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY D CA  
5152  C C   . GLY B 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY D C   
5153  O O   . GLY B 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY D O   
5154  N N   . GLY B 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY D N   
5155  C CA  . GLY B 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY D CA  
5156  C C   . GLY B 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY D C   
5157  O O   . GLY B 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY D O   
5158  N N   . TYR B 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR D N   
5159  C CA  . TYR B 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR D CA  
5160  C C   . TYR B 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR D C   
5161  O O   . TYR B 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR D O   
5170  N N   . THR B 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR D N   
5171  C CA  . THR B 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR D CA  
5172  C C   . THR B 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR D C   
5173  O O   . THR B 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR D O   
5174  C CB  . THR B 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR D CB  
5175  O OG1 . THR B 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR D OG1 
5176  C CG2 . THR B 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR D CG2 
5177  N N   . ILE B 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE D N   
5178  C CA  . ILE B 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE D CA  
5179  C C   . ILE B 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE D C   
5180  O O   . ILE B 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE D O   
5185  N N   . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D N   
5186  C CA  . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D CA  
5187  C C   . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D C   
5188  O O   . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D O   
5189  C CB  . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D CB  
5190  C CG  . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D CG  
5191  C CD  . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D CD  
5192  N NE  . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D NE  
5193  C CZ  . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D CZ  
5194  N NH1 . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D NH1 
5195  N NH2 . ARG B 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG D NH2 
5196  N N   . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D N   
5197  C CA  . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D CA  
5198  C C   . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D C   
5199  O O   . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D O   
5200  C CB  . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D CB  
5201  C CG  . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D CG  
5202  O OD1 . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D OD1 
5203  N ND2 . ASN B 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN D ND2 
5204  N N   . VAL B 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL D N   
5205  C CA  . VAL B 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL D CA  
5206  C C   . VAL B 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL D C   
5207  O O   . VAL B 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL D O   
5208  C CB  . VAL B 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL D CB  
5209  C CG1 . VAL B 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL D CG1 
5210  C CG2 . VAL B 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL D CG2 
5211  N N   . ALA B 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA D N   
5212  C CA  . ALA B 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA D CA  
5213  C C   . ALA B 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA D C   
5214  O O   . ALA B 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA D O   
5215  C CB  . ALA B 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA D CB  
5216  N N   . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D N   
5217  C CA  . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D CA  
5218  C C   . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D C   
5219  O O   . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D O   
5220  C CB  . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D CB  
5221  C CG  . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D CG  
5222  C CD  . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D CD  
5223  N NE  . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D NE  
5224  C CZ  . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D CZ  
5225  N NH1 . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D NH1 
5226  N NH2 . ARG B 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG D NH2 
5227  N N   . CYS B 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS D N   
5228  C CA  . CYS B 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS D CA  
5229  C C   . CYS B 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS D C   
5230  O O   . CYS B 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS D O   
5231  C CB  . CYS B 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS D CB  
5232  S SG  . CYS B 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS D SG  
5233  N N   . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D N   
5234  C CA  . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CA  
5235  C C   . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D C   
5236  O O   . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D O   
5237  C CB  . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CB  
5238  C CG  . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CG  
5239  C CD1 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CD1 
5240  C CD2 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CD2 
5241  N NE1 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D NE1 
5242  C CE2 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CE2 
5243  C CE3 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CE3 
5244  C CZ2 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CZ2 
5245  C CZ3 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CZ3 
5246  C CH2 . TRP B 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP D CH2 
5247  N N   . THR B 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR D N   
5248  C CA  . THR B 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR D CA  
5249  C C   . THR B 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR D C   
5250  O O   . THR B 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR D O   
5251  C CB  . THR B 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR D CB  
5252  O OG1 . THR B 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR D OG1 
5253  C CG2 . THR B 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR D CG2 
5254  N N   . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D N   
5255  C CA  . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CA  
5256  C C   . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D C   
5257  O O   . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D O   
5258  C CB  . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CB  
5259  C CG  . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CG  
5260  C CD1 . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CD1 
5261  C CD2 . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CD2 
5262  C CE1 . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CE1 
5263  C CE2 . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CE2 
5264  C CZ  . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D CZ  
5265  O OH  . TYR B 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR D OH  
5266  N N   . GLU B 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU D N   
5267  C CA  . GLU B 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU D CA  
5268  C C   . GLU B 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU D C   
5269  O O   . GLU B 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU D O   
5275  N N   . THR B 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR D N   
5276  C CA  . THR B 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR D CA  
5277  C C   . THR B 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR D C   
5278  O O   . THR B 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR D O   
5279  C CB  . THR B 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR D CB  
5280  O OG1 . THR B 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR D OG1 
5281  C CG2 . THR B 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR D CG2 
5282  N N   . ALA B 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA D N   
5283  C CA  . ALA B 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA D CA  
5284  C C   . ALA B 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA D C   
5285  O O   . ALA B 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA D O   
5286  C CB  . ALA B 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA D CB  
5287  N N   . VAL B 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL D N   
5288  C CA  . VAL B 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL D CA  
5289  C C   . VAL B 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL D C   
5290  O O   . VAL B 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL D O   
5294  N N   . ALA B 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA D N   
5295  C CA  . ALA B 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA D CA  
5296  C C   . ALA B 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA D C   
5297  O O   . ALA B 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA D O   
5298  C CB  . ALA B 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA D CB  
5299  N N   . LEU B 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU D N   
5300  C CA  . LEU B 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU D CA  
5301  C C   . LEU B 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU D C   
5302  O O   . LEU B 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU D O   
5312  N N   . CYS B 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS D N   
5313  C CA  . CYS B 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS D CA  
5314  C C   . CYS B 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS D C   
5315  O O   . CYS B 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS D O   
5318  N N   . GLU B 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU D N   
5319  C CA  . GLU B 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU D CA  
5320  C C   . GLU B 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU D C   
5321  O O   . GLU B 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU D O   
5322  C CB  . GLU B 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU D CB  
5323  N N   . ILE B 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE D N   
5324  C CA  . ILE B 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE D CA  
5325  C C   . ILE B 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE D C   
5326  O O   . ILE B 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE D O   
5331  N N   . PRO B 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO D N   
5332  C CA  . PRO B 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO D CA  
5333  C C   . PRO B 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO D C   
5334  O O   . PRO B 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO D O   
5335  C CB  . PRO B 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO D CB  
5336  C CG  . PRO B 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO D CG  
5337  C CD  . PRO B 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO D CD  
5338  N N   . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D N   
5339  C CA  . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D CA  
5340  C C   . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D C   
5341  O O   . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D O   
5342  C CB  . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D CB  
5343  C CG  . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D CG  
5344  O OD1 . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D OD1 
5345  N ND2 . ASN B 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN D ND2 
5363  N N   . PRO B 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO D N   
5364  C CA  . PRO B 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO D CA  
5365  C C   . PRO B 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO D C   
5366  O O   . PRO B 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO D O   
5367  C CB  . PRO B 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO D CB  
5368  C CG  . PRO B 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO D CG  
5369  C CD  . PRO B 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO D CD  
5382  N N   . ASN B 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN D N   
5383  C CA  . ASN B 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN D CA  
5384  C C   . ASN B 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN D C   
5385  O O   . ASN B 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN D O   
5390  N N   . ASP B 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP D N   
5391  C CA  . ASP B 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP D CA  
5392  C C   . ASP B 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP D C   
5393  O O   . ASP B 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP D O   
5398  N N   . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D N   
5399  C CA  . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CA  
5400  C C   . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D C   
5401  O O   . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D O   
5402  C CB  . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CB  
5403  C CG  . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CG  
5404  C CD1 . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CD1 
5405  C CD2 . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CD2 
5406  C CE1 . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CE1 
5407  C CE2 . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CE2 
5408  C CZ  . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D CZ  
5409  O OH  . TYR B 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR D OH  
5410  N N   . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D N   
5411  C CA  . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CA  
5412  C C   . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D C   
5413  O O   . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D O   
5414  C CB  . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CB  
5415  C CG  . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CG  
5416  C CD1 . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CD1 
5417  C CD2 . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CD2 
5418  C CE1 . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CE1 
5419  C CE2 . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CE2 
5420  C CZ  . PHE B 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE D CZ  
5421  N N   . GLU B 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU D N   
5422  C CA  . GLU B 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU D CA  
5423  C C   . GLU B 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU D C   
5424  O O   . GLU B 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU D O   
5425  C CB  . GLU B 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU D CB  
5426  N N   . TYR B 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR D N   
5427  C CA  . TYR B 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR D CA  
5428  C C   . TYR B 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR D C   
5429  O O   . TYR B 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR D O   
5430  C CB  . TYR B 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR D CB  
5431  N N   . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D N   
5432  C CA  . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CA  
5433  C C   . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D C   
5434  O O   . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D O   
5435  C CB  . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CB  
5436  C CG  . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CG  
5437  C CD1 . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CD1 
5438  C CD2 . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CD2 
5439  C CE1 . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CE1 
5440  C CE2 . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CE2 
5441  C CZ  . PHE B 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE D CZ  
5446  N N   . PRO B 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO D N   
5447  C CA  . PRO B 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO D CA  
5448  C C   . PRO B 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO D C   
5449  O O   . PRO B 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO D O   
5450  C CB  . PRO B 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO D CB  
5451  C CG  . PRO B 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO D CG  
5452  C CD  . PRO B 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO D CD  
5453  N N   . ASP B 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP D N   
5454  C CA  . ASP B 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP D CA  
5455  C C   . ASP B 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP D C   
5456  O O   . ASP B 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP D O   
5457  C CB  . ASP B 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP D CB  
5458  N N   . PHE B 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE D N   
5459  C CA  . PHE B 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE D CA  
5460  C C   . PHE B 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE D C   
5461  O O   . PHE B 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE D O   
5463  N N   . LYS B 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS D N   
5464  C CA  . LYS B 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS D CA  
5465  C C   . LYS B 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS D C   
5466  O O   . LYS B 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS D O   
5468  N N   . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D N   
5469  C CA  . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D CA  
5470  C C   . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D C   
5471  O O   . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D O   
5472  C CB  . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D CB  
5473  C CG  . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D CG  
5474  C CD1 . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D CD1 
5475  C CD2 . LEU B 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU D CD2 
5476  N N   . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D N   
5477  C CA  . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D CA  
5478  C C   . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D C   
5479  O O   . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D O   
5480  C CB  . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D CB  
5481  C CG  . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D CG  
5482  N ND1 . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D ND1 
5483  C CD2 . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D CD2 
5484  C CE1 . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D CE1 
5485  N NE2 . HIS B 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS D NE2 
5486  N N   . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D N   
5487  C CA  . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D CA  
5488  C C   . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D C   
5489  O O   . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D O   
5490  C CB  . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D CB  
5491  C CG1 . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D CG1 
5492  C CG2 . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D CG2 
5493  C CD1 . ILE B 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE D CD1 
5494  N N   . SER B 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER D N   
5495  C CA  . SER B 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER D CA  
5496  C C   . SER B 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER D C   
5497  O O   . SER B 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER D O   
5500  N N   . PRO B 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO D N   
5501  C CA  . PRO B 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO D CA  
5502  C C   . PRO B 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO D C   
5503  O O   . PRO B 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO D O   
5504  C CB  . PRO B 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO D CB  
5505  C CG  . PRO B 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO D CG  
5506  C CD  . PRO B 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO D CD  
5507  N N   . SER B 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER D N   
5508  C CA  . SER B 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER D CA  
5509  C C   . SER B 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER D C   
5510  O O   . SER B 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER D O   
5511  C CB  . SER B 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER D CB  
5512  O OG  . SER B 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER D OG  
5513  N N   . ASN B 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN D N   
5514  C CA  . ASN B 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN D CA  
5515  C C   . ASN B 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN D C   
5516  O O   . ASN B 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN D O   
5517  C CB  . ASN B 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN D CB  
5518  N N   . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D N   
5519  C CA  . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D CA  
5520  C C   . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D C   
5521  O O   . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D O   
5522  C CB  . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D CB  
5523  C CG  . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D CG  
5524  S SD  . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D SD  
5525  C CE  . MET B 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET D CE  
5526  N N   . THR B 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR D N   
5527  C CA  . THR B 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR D CA  
5528  C C   . THR B 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR D C   
5529  O O   . THR B 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR D O   
5530  C CB  . THR B 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR D CB  
5531  O OG1 . THR B 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR D OG1 
5532  C CG2 . THR B 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR D CG2 
5533  N N   . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D N   
5534  C CA  . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D CA  
5535  C C   . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D C   
5536  O O   . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D O   
5537  C CB  . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D CB  
5538  C CG  . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D CG  
5539  O OD1 . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D OD1 
5540  N ND2 . ASN B 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN D ND2 
5541  N N   . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D N   
5542  C CA  . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D CA  
5543  C C   . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D C   
5544  O O   . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D O   
5545  C CB  . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D CB  
5546  C CG  . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D CG  
5547  C CD  . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D CD  
5548  O OE1 . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D OE1 
5549  N NE2 . GLN B 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN D NE2 
5550  N N   . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D N   
5551  C CA  . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D CA  
5552  C C   . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D C   
5553  O O   . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D O   
5554  C CB  . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D CB  
5555  C CG  . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D CG  
5556  O OD1 . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D OD1 
5557  N ND2 . ASN B 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN D ND2 
5558  N N   . THR B 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR D N   
5559  C CA  . THR B 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR D CA  
5560  C C   . THR B 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR D C   
5561  O O   . THR B 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR D O   
5562  C CB  . THR B 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR D CB  
5563  O OG1 . THR B 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR D OG1 
5564  C CG2 . THR B 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR D CG2 
5565  N N   . PRO B 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO D N   
5566  C CA  . PRO B 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO D CA  
5567  C C   . PRO B 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO D C   
5568  O O   . PRO B 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO D O   
5569  C CB  . PRO B 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO D CB  
5570  C CG  . PRO B 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO D CG  
5571  C CD  . PRO B 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO D CD  
5572  N N   . GLU B 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU D N   
5573  C CA  . GLU B 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU D CA  
5574  C C   . GLU B 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU D C   
5575  O O   . GLU B 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU D O   
5576  C CB  . GLU B 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU D CB  
5577  N N   . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D N   
5578  C CA  . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CA  
5579  C C   . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D C   
5580  O O   . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D O   
5581  C CB  . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CB  
5582  C CG  . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CG  
5583  C CD1 . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CD1 
5584  C CD2 . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CD2 
5585  C CE1 . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CE1 
5586  C CE2 . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CE2 
5587  C CZ  . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D CZ  
5588  O OH  . TYR B 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR D OH  
5589  N N   . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D N   
5590  C CA  . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D CA  
5591  C C   . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D C   
5592  O O   . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D O   
5593  C CB  . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D CB  
5594  C CG  . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D CG  
5595  S SD  . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D SD  
5596  C CE  . MET B 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET D CE  
5597  N N   . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D N   
5598  C CA  . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D CA  
5599  C C   . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D C   
5600  O O   . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D O   
5601  C CB  . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D CB  
5602  C CG  . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D CG  
5603  C CD  . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D CD  
5604  O OE1 . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D OE1 
5605  O OE2 . GLU B 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU D OE2 
5606  N N   . LYS B 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS D N   
5607  C CA  . LYS B 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS D CA  
5608  C C   . LYS B 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS D C   
5609  O O   . LYS B 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS D O   
5615  N N   . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D N   
5616  C CA  . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D CA  
5617  C C   . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D C   
5618  O O   . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D O   
5619  C CB  . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D CB  
5620  C CG1 . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D CG1 
5621  C CG2 . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D CG2 
5622  C CD1 . ILE B 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE D CD1 
5623  N N   . LYS B 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS D N   
5624  C CA  . LYS B 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS D CA  
5625  C C   . LYS B 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS D C   
5626  O O   . LYS B 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS D O   
5632  N N   . GLN B 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN D N   
5633  C CA  . GLN B 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN D CA  
5634  C C   . GLN B 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN D C   
5635  O O   . GLN B 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN D O   
5641  N N   . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D N   
5642  C CA  . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D CA  
5643  C C   . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D C   
5644  O O   . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D O   
5645  C CB  . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D CB  
5646  C CG  . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D CG  
5647  C CD  . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D CD  
5648  N NE  . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D NE  
5649  C CZ  . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D CZ  
5650  N NH1 . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D NH1 
5651  N NH2 . ARG B 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG D NH2 
5652  N N   . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D N   
5653  C CA  . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D CA  
5654  C C   . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D C   
5655  O O   . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D O   
5656  C CB  . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D CB  
5657  C CG  . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D CG  
5658  C CD1 . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D CD1 
5659  C CD2 . LEU B 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU D CD2 
5660  N N   . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D N   
5661  C CA  . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CA  
5662  C C   . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D C   
5663  O O   . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D O   
5664  C CB  . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CB  
5665  C CG  . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CG  
5666  C CD1 . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CD1 
5667  C CD2 . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CD2 
5668  C CE1 . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CE1 
5669  C CE2 . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CE2 
5670  C CZ  . PHE B 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE D CZ  
5671  N N   . GLU B 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU D N   
5672  C CA  . GLU B 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU D CA  
5673  C C   . GLU B 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU D C   
5674  O O   . GLU B 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU D O   
5680  N N   . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D N   
5681  C CA  . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D CA  
5682  C C   . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D C   
5683  O O   . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D O   
5684  C CB  . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D CB  
5685  C CG  . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D CG  
5686  O OD1 . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D OD1 
5687  N ND2 . ASN B 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN D ND2 
5688  N N   . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D N   
5689  C CA  . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D CA  
5690  C C   . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D C   
5691  O O   . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D O   
5692  C CB  . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D CB  
5693  C CG  . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D CG  
5694  C CD1 . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D CD1 
5695  C CD2 . LEU B 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU D CD2 
5696  N N   . ARG B 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG D N   
5697  C CA  . ARG B 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG D CA  
5698  C C   . ARG B 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG D C   
5699  O O   . ARG B 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG D O   
5707  N N   . MET B 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET D N   
5708  C CA  . MET B 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET D CA  
5709  C C   . MET B 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET D C   
5710  O O   . MET B 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET D O   
5715  N N   . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D N   
5716  C CA  . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D CA  
5717  C C   . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D C   
5718  O O   . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D O   
5719  C CB  . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D CB  
5720  C CG  . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D CG  
5721  C CD1 . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D CD1 
5722  C CD2 . LEU B 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU D CD2 
5723  N N   . PRO B 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO D N   
5724  C CA  . PRO B 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO D CA  
5725  C C   . PRO B 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO D C   
5726  O O   . PRO B 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO D O   
5727  C CB  . PRO B 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO D CB  
5728  C CG  . PRO B 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO D CG  
5729  C CD  . PRO B 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO D CD  
8693  N N   . LYS D 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS B N   
8694  C CA  . LYS D 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS B CA  
8695  C C   . LYS D 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS B C   
8696  O O   . LYS D 11  ? 1.7768 1.7768 1.7768 0.0000 0.0000 0.0000 11  LYS B O   
8702  N N   . VAL D 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL B N   
8703  C CA  . VAL D 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL B CA  
8704  C C   . VAL D 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL B C   
8705  O O   . VAL D 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL B O   
8706  C CB  . VAL D 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL B CB  
8707  C CG1 . VAL D 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL B CG1 
8708  C CG2 . VAL D 12  ? 1.6676 1.6676 1.6676 0.0000 0.0000 0.0000 12  VAL B CG2 
8709  N N   . CYS D 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS B N   
8710  C CA  . CYS D 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS B CA  
8711  C C   . CYS D 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS B C   
8712  O O   . CYS D 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS B O   
8713  C CB  . CYS D 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS B CB  
8714  S SG  . CYS D 13  ? 1.5590 1.5590 1.5590 0.0000 0.0000 0.0000 13  CYS B SG  
8715  N N   . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B N   
8716  C CA  . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CA  
8717  C C   . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B C   
8718  O O   . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B O   
8719  C CB  . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CB  
8720  C CG  . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CG  
8721  C CD1 . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CD1 
8722  C CD2 . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CD2 
8723  C CE1 . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CE1 
8724  C CE2 . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CE2 
8725  C CZ  . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B CZ  
8726  O OH  . TYR D 14  ? 1.4786 1.4786 1.4786 0.0000 0.0000 0.0000 14  TYR B OH  
8727  N N   . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B N   
8728  C CA  . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CA  
8729  C C   . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B C   
8730  O O   . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B O   
8731  C CB  . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CB  
8732  C CG  . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CG  
8733  C CD1 . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CD1 
8734  C CD2 . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CD2 
8735  C CE1 . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CE1 
8736  C CE2 . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CE2 
8737  C CZ  . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B CZ  
8738  O OH  . TYR D 15  ? 1.4860 1.4860 1.4860 0.0000 0.0000 0.0000 15  TYR B OH  
8739  N N   . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B N   
8740  C CA  . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CA  
8741  C C   . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B C   
8742  O O   . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B O   
8743  C CB  . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CB  
8744  C CG  . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CG  
8745  C CD1 . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CD1 
8746  C CD2 . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CD2 
8747  C CE1 . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CE1 
8748  C CE2 . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CE2 
8749  C CZ  . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B CZ  
8750  O OH  . TYR D 16  ? 1.6444 1.6444 1.6444 0.0000 0.0000 0.0000 16  TYR B OH  
8751  N N   . ASP D 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP B N   
8752  C CA  . ASP D 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP B CA  
8753  C C   . ASP D 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP B C   
8754  O O   . ASP D 17  ? 1.7300 1.7300 1.7300 0.0000 0.0000 0.0000 17  ASP B O   
8759  N N   . GLY D 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY B N   
8760  C CA  . GLY D 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY B CA  
8761  C C   . GLY D 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY B C   
8762  O O   . GLY D 18  ? 1.7083 1.7083 1.7083 0.0000 0.0000 0.0000 18  GLY B O   
8763  N N   . ASP D 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP B N   
8764  C CA  . ASP D 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP B CA  
8765  C C   . ASP D 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP B C   
8766  O O   . ASP D 19  ? 1.7637 1.7637 1.7637 0.0000 0.0000 0.0000 19  ASP B O   
8780  N N   . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B N   
8781  C CA  . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B CA  
8782  C C   . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B C   
8783  O O   . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B O   
8784  C CB  . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B CB  
8785  C CG  . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B CG  
8786  O OD1 . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B OD1 
8787  N ND2 . ASN D 22  ? 1.6668 1.6668 1.6668 0.0000 0.0000 0.0000 22  ASN B ND2 
8788  N N   . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B N   
8789  C CA  . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CA  
8790  C C   . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B C   
8791  O O   . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B O   
8792  C CB  . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CB  
8793  C CG  . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CG  
8794  C CD1 . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CD1 
8795  C CD2 . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CD2 
8796  C CE1 . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CE1 
8797  C CE2 . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CE2 
8798  C CZ  . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B CZ  
8799  O OH  . TYR D 23  ? 1.4809 1.4809 1.4809 0.0000 0.0000 0.0000 23  TYR B OH  
8800  N N   . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B N   
8801  C CA  . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CA  
8802  C C   . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B C   
8803  O O   . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B O   
8804  C CB  . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CB  
8805  C CG  . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CG  
8806  C CD1 . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CD1 
8807  C CD2 . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CD2 
8808  C CE1 . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CE1 
8809  C CE2 . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CE2 
8810  C CZ  . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B CZ  
8811  O OH  . TYR D 24  ? 1.5533 1.5533 1.5533 0.0000 0.0000 0.0000 24  TYR B OH  
8812  N N   . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B N   
8813  C CA  . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CA  
8814  C C   . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B C   
8815  O O   . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B O   
8816  C CB  . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CB  
8817  C CG  . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CG  
8818  C CD1 . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CD1 
8819  C CD2 . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CD2 
8820  C CE1 . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CE1 
8821  C CE2 . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CE2 
8822  C CZ  . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B CZ  
8823  O OH  . TYR D 25  ? 1.6262 1.6262 1.6262 0.0000 0.0000 0.0000 25  TYR B OH  
8824  N N   . GLY D 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY B N   
8825  C CA  . GLY D 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY B CA  
8826  C C   . GLY D 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY B C   
8827  O O   . GLY D 26  ? 1.5977 1.5977 1.5977 0.0000 0.0000 0.0000 26  GLY B O   
8828  N N   . GLN D 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN B N   
8829  C CA  . GLN D 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN B CA  
8830  C C   . GLN D 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN B C   
8831  O O   . GLN D 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN B O   
8832  C CB  . GLN D 27  ? 1.6122 1.6122 1.6122 0.0000 0.0000 0.0000 27  GLN B CB  
8833  N N   . GLY D 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY B N   
8834  C CA  . GLY D 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY B CA  
8835  C C   . GLY D 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY B C   
8836  O O   . GLY D 28  ? 1.6402 1.6402 1.6402 0.0000 0.0000 0.0000 28  GLY B O   
8837  N N   . HIS D 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS B N   
8838  C CA  . HIS D 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS B CA  
8839  C C   . HIS D 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS B C   
8840  O O   . HIS D 29  ? 1.6140 1.6140 1.6140 0.0000 0.0000 0.0000 29  HIS B O   
8847  N N   . PRO D 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO B N   
8848  C CA  . PRO D 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO B CA  
8849  C C   . PRO D 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO B C   
8850  O O   . PRO D 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO B O   
8851  C CB  . PRO D 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO B CB  
8852  C CG  . PRO D 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO B CG  
8853  C CD  . PRO D 30  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 30  PRO B CD  
8854  N N   . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B N   
8855  C CA  . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B CA  
8856  C C   . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B C   
8857  O O   . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B O   
8858  C CB  . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B CB  
8859  C CG  . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B CG  
8860  S SD  . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B SD  
8861  C CE  . MET D 31  ? 1.4446 1.4446 1.4446 0.0000 0.0000 0.0000 31  MET B CE  
8862  N N   . LYS D 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS B N   
8863  C CA  . LYS D 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS B CA  
8864  C C   . LYS D 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS B C   
8865  O O   . LYS D 32  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 32  LYS B O   
8888  N N   . ARG D 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG B N   
8889  C CA  . ARG D 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG B CA  
8890  C C   . ARG D 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG B C   
8891  O O   . ARG D 35  ? 1.5670 1.5670 1.5670 0.0000 0.0000 0.0000 35  ARG B O   
8893  N N   . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B N   
8894  C CA  . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B CA  
8895  C C   . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B C   
8896  O O   . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B O   
8897  C CB  . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B CB  
8898  C CG1 . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B CG1 
8899  C CG2 . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B CG2 
8900  C CD1 . ILE D 36  ? 1.4615 1.4615 1.4615 0.0000 0.0000 0.0000 36  ILE B CD1 
8901  N N   . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B N   
8902  C CA  . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B CA  
8903  C C   . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B C   
8904  O O   . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B O   
8905  C CB  . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B CB  
8906  C CG  . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B CG  
8907  C CD  . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B CD  
8908  N NE  . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B NE  
8909  C CZ  . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B CZ  
8910  N NH1 . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B NH1 
8911  N NH2 . ARG D 37  ? 1.6373 1.6373 1.6373 0.0000 0.0000 0.0000 37  ARG B NH2 
8912  N N   . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B N   
8913  C CA  . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B CA  
8914  C C   . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B C   
8915  O O   . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B O   
8916  C CB  . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B CB  
8917  C CG  . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B CG  
8918  S SD  . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B SD  
8919  C CE  . MET D 38  ? 1.6337 1.6337 1.6337 0.0000 0.0000 0.0000 38  MET B CE  
8920  N N   . THR D 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR B N   
8921  C CA  . THR D 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR B CA  
8922  C C   . THR D 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR B C   
8923  O O   . THR D 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR B O   
8924  C CB  . THR D 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR B CB  
8925  O OG1 . THR D 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR B OG1 
8926  C CG2 . THR D 39  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 39  THR B CG2 
8927  N N   . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B N   
8928  C CA  . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B CA  
8929  C C   . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B C   
8930  O O   . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B O   
8931  C CB  . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B CB  
8932  C CG  . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B CG  
8933  N ND1 . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B ND1 
8934  C CD2 . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B CD2 
8935  C CE1 . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B CE1 
8936  N NE2 . HIS D 40  ? 1.5024 1.5024 1.5024 0.0000 0.0000 0.0000 40  HIS B NE2 
8937  N N   . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B N   
8938  C CA  . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B CA  
8939  C C   . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B C   
8940  O O   . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B O   
8941  C CB  . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B CB  
8942  C CG  . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B CG  
8943  O OD1 . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B OD1 
8944  N ND2 . ASN D 41  ? 1.6232 1.6232 1.6232 0.0000 0.0000 0.0000 41  ASN B ND2 
8945  N N   . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B N   
8946  C CA  . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B CA  
8947  C C   . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B C   
8948  O O   . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B O   
8949  C CB  . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B CB  
8950  C CG  . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B CG  
8951  C CD1 . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B CD1 
8952  C CD2 . LEU D 42  ? 1.4609 1.4609 1.4609 0.0000 0.0000 0.0000 42  LEU B CD2 
8953  N N   . LEU D 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU B N   
8954  C CA  . LEU D 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU B CA  
8955  C C   . LEU D 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU B C   
8956  O O   . LEU D 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU B O   
8957  C CB  . LEU D 43  ? 1.4971 1.4971 1.4971 0.0000 0.0000 0.0000 43  LEU B CB  
8958  N N   . LEU D 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU B N   
8959  C CA  . LEU D 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU B CA  
8960  C C   . LEU D 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU B C   
8961  O O   . LEU D 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU B O   
8962  C CB  . LEU D 44  ? 1.6099 1.6099 1.6099 0.0000 0.0000 0.0000 44  LEU B CB  
8963  N N   . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B N   
8964  C CA  . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B CA  
8965  C C   . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B C   
8966  O O   . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B O   
8967  C CB  . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B CB  
8968  C CG  . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B CG  
8969  O OD1 . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B OD1 
8970  N ND2 . ASN D 45  ? 1.6475 1.6475 1.6475 0.0000 0.0000 0.0000 45  ASN B ND2 
8971  N N   . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B N   
8972  C CA  . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CA  
8973  C C   . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B C   
8974  O O   . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B O   
8975  C CB  . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CB  
8976  C CG  . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CG  
8977  C CD1 . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CD1 
8978  C CD2 . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CD2 
8979  C CE1 . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CE1 
8980  C CE2 . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CE2 
8981  C CZ  . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B CZ  
8982  O OH  . TYR D 46  ? 1.5894 1.5894 1.5894 0.0000 0.0000 0.0000 46  TYR B OH  
8983  N N   . GLY D 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY B N   
8984  C CA  . GLY D 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY B CA  
8985  C C   . GLY D 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY B C   
8986  O O   . GLY D 47  ? 1.7016 1.7016 1.7016 0.0000 0.0000 0.0000 47  GLY B O   
8987  N N   . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B N   
8988  C CA  . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B CA  
8989  C C   . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B C   
8990  O O   . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B O   
8991  C CB  . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B CB  
8992  C CG  . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B CG  
8993  C CD1 . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B CD1 
8994  C CD2 . LEU D 48  ? 1.6023 1.6023 1.6023 0.0000 0.0000 0.0000 48  LEU B CD2 
8995  N N   . TYR D 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR B N   
8996  C CA  . TYR D 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR B CA  
8997  C C   . TYR D 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR B C   
8998  O O   . TYR D 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR B O   
8999  C CB  . TYR D 49  ? 1.8038 1.8038 1.8038 0.0000 0.0000 0.0000 49  TYR B CB  
9000  N N   . ARG D 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG B N   
9001  C CA  . ARG D 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG B CA  
9002  C C   . ARG D 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG B C   
9003  O O   . ARG D 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG B O   
9004  C CB  . ARG D 50  ? 1.8724 1.8724 1.8724 0.0000 0.0000 0.0000 50  ARG B CB  
9005  N N   . LYS D 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS B N   
9006  C CA  . LYS D 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS B CA  
9007  C C   . LYS D 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS B C   
9008  O O   . LYS D 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS B O   
9009  C CB  . LYS D 51  ? 1.8380 1.8380 1.8380 0.0000 0.0000 0.0000 51  LYS B CB  
9010  N N   . MET D 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET B N   
9011  C CA  . MET D 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET B CA  
9012  C C   . MET D 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET B C   
9013  O O   . MET D 52  ? 1.7367 1.7367 1.7367 0.0000 0.0000 0.0000 52  MET B O   
9018  N N   . GLU D 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU B N   
9019  C CA  . GLU D 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU B CA  
9020  C C   . GLU D 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU B C   
9021  O O   . GLU D 53  ? 1.6070 1.6070 1.6070 0.0000 0.0000 0.0000 53  GLU B O   
9027  N N   . ILE D 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE B N   
9028  C CA  . ILE D 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE B CA  
9029  C C   . ILE D 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE B C   
9030  O O   . ILE D 54  ? 1.5785 1.5785 1.5785 0.0000 0.0000 0.0000 54  ILE B O   
9035  N N   . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B N   
9036  C CA  . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CA  
9037  C C   . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B C   
9038  O O   . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B O   
9039  C CB  . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CB  
9040  C CG  . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CG  
9041  C CD1 . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CD1 
9042  C CD2 . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CD2 
9043  C CE1 . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CE1 
9044  C CE2 . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CE2 
9045  C CZ  . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B CZ  
9046  O OH  . TYR D 55  ? 1.5853 1.5853 1.5853 0.0000 0.0000 0.0000 55  TYR B OH  
9047  N N   . ARG D 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG B N   
9048  C CA  . ARG D 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG B CA  
9049  C C   . ARG D 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG B C   
9050  O O   . ARG D 56  ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 56  ARG B O   
9052  N N   . PRO D 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO B N   
9053  C CA  . PRO D 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO B CA  
9054  C C   . PRO D 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO B C   
9055  O O   . PRO D 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO B O   
9056  C CB  . PRO D 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO B CB  
9057  C CG  . PRO D 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO B CG  
9058  C CD  . PRO D 57  ? 1.6254 1.6254 1.6254 0.0000 0.0000 0.0000 57  PRO B CD  
9059  N N   . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B N   
9060  C CA  . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B CA  
9061  C C   . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B C   
9062  O O   . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B O   
9063  C CB  . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B CB  
9064  C CG  . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B CG  
9065  N ND1 . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B ND1 
9066  C CD2 . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B CD2 
9067  C CE1 . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B CE1 
9068  N NE2 . HIS D 58  ? 1.7017 1.7017 1.7017 0.0000 0.0000 0.0000 58  HIS B NE2 
9069  N N   . LYS D 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS B N   
9070  C CA  . LYS D 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS B CA  
9071  C C   . LYS D 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS B C   
9072  O O   . LYS D 59  ? 1.7035 1.7035 1.7035 0.0000 0.0000 0.0000 59  LYS B O   
9074  N N   . ALA D 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA B N   
9075  C CA  . ALA D 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA B CA  
9076  C C   . ALA D 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA B C   
9077  O O   . ALA D 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA B O   
9078  C CB  . ALA D 60  ? 1.7315 1.7315 1.7315 0.0000 0.0000 0.0000 60  ALA B CB  
9079  N N   . THR D 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR B N   
9080  C CA  . THR D 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR B CA  
9081  C C   . THR D 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR B C   
9082  O O   . THR D 61  ? 1.6868 1.6868 1.6868 0.0000 0.0000 0.0000 61  THR B O   
9086  N N   . ALA D 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA B N   
9087  C CA  . ALA D 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA B CA  
9088  C C   . ALA D 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA B C   
9089  O O   . ALA D 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA B O   
9090  C CB  . ALA D 62  ? 1.6026 1.6026 1.6026 0.0000 0.0000 0.0000 62  ALA B CB  
9091  N N   . GLU D 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU B N   
9092  C CA  . GLU D 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU B CA  
9093  C C   . GLU D 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU B C   
9094  O O   . GLU D 63  ? 1.6432 1.6432 1.6432 0.0000 0.0000 0.0000 63  GLU B O   
9096  N N   . GLU D 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU B N   
9097  C CA  . GLU D 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU B CA  
9098  C C   . GLU D 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU B C   
9099  O O   . GLU D 64  ? 1.6597 1.6597 1.6597 0.0000 0.0000 0.0000 64  GLU B O   
9101  N N   . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B N   
9102  C CA  . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B CA  
9103  C C   . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B C   
9104  O O   . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B O   
9105  C CB  . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B CB  
9106  C CG  . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B CG  
9107  S SD  . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B SD  
9108  C CE  . MET D 65  ? 1.6168 1.6168 1.6168 0.0000 0.0000 0.0000 65  MET B CE  
9109  N N   . THR D 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR B N   
9110  C CA  . THR D 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR B CA  
9111  C C   . THR D 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR B C   
9112  O O   . THR D 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR B O   
9113  C CB  . THR D 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR B CB  
9114  O OG1 . THR D 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR B OG1 
9115  C CG2 . THR D 66  ? 1.5522 1.5522 1.5522 0.0000 0.0000 0.0000 66  THR B CG2 
9116  N N   . LYS D 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS B N   
9117  C CA  . LYS D 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS B CA  
9118  C C   . LYS D 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS B C   
9119  O O   . LYS D 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS B O   
9120  C CB  . LYS D 67  ? 1.4934 1.4934 1.4934 0.0000 0.0000 0.0000 67  LYS B CB  
9121  N N   . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B N   
9122  C CA  . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CA  
9123  C C   . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B C   
9124  O O   . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B O   
9125  C CB  . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CB  
9126  C CG  . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CG  
9127  C CD1 . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CD1 
9128  C CD2 . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CD2 
9129  C CE1 . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CE1 
9130  C CE2 . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CE2 
9131  C CZ  . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B CZ  
9132  O OH  . TYR D 68  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 68  TYR B OH  
9133  N N   . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B N   
9134  C CA  . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B CA  
9135  C C   . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B C   
9136  O O   . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B O   
9137  C CB  . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B CB  
9138  C CG  . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B CG  
9139  N ND1 . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B ND1 
9140  C CD2 . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B CD2 
9141  C CE1 . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B CE1 
9142  N NE2 . HIS D 69  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 69  HIS B NE2 
9143  N N   . SER D 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER B N   
9144  C CA  . SER D 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER B CA  
9145  C C   . SER D 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER B C   
9146  O O   . SER D 70  ? 1.5904 1.5904 1.5904 0.0000 0.0000 0.0000 70  SER B O   
9149  N N   . ASP D 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP B N   
9150  C CA  . ASP D 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP B CA  
9151  C C   . ASP D 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP B C   
9152  O O   . ASP D 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP B O   
9153  C CB  . ASP D 71  ? 1.5855 1.5855 1.5855 0.0000 0.0000 0.0000 71  ASP B CB  
9154  N N   . GLU D 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU B N   
9155  C CA  . GLU D 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU B CA  
9156  C C   . GLU D 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU B C   
9157  O O   . GLU D 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU B O   
9158  C CB  . GLU D 72  ? 1.5768 1.5768 1.5768 0.0000 0.0000 0.0000 72  GLU B CB  
9159  N N   . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B N   
9160  C CA  . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CA  
9161  C C   . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B C   
9162  O O   . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B O   
9163  C CB  . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CB  
9164  C CG  . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CG  
9165  C CD1 . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CD1 
9166  C CD2 . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CD2 
9167  C CE1 . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CE1 
9168  C CE2 . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CE2 
9169  C CZ  . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B CZ  
9170  O OH  . TYR D 73  ? 1.4580 1.4580 1.4580 0.0000 0.0000 0.0000 73  TYR B OH  
9171  N N   . ILE D 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE B N   
9172  C CA  . ILE D 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE B CA  
9173  C C   . ILE D 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE B C   
9174  O O   . ILE D 74  ? 1.4761 1.4761 1.4761 0.0000 0.0000 0.0000 74  ILE B O   
9179  N N   . LYS D 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS B N   
9180  C CA  . LYS D 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS B CA  
9181  C C   . LYS D 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS B C   
9182  O O   . LYS D 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS B O   
9183  C CB  . LYS D 75  ? 1.5146 1.5146 1.5146 0.0000 0.0000 0.0000 75  LYS B CB  
9184  N N   . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B N   
9185  C CA  . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CA  
9186  C C   . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B C   
9187  O O   . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B O   
9188  C CB  . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CB  
9189  C CG  . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CG  
9190  C CD1 . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CD1 
9191  C CD2 . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CD2 
9192  C CE1 . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CE1 
9193  C CE2 . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CE2 
9194  C CZ  . PHE D 76  ? 1.4926 1.4926 1.4926 0.0000 0.0000 0.0000 76  PHE B CZ  
9195  N N   . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B N   
9196  C CA  . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B CA  
9197  C C   . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B C   
9198  O O   . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B O   
9199  C CB  . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B CB  
9200  C CG  . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B CG  
9201  C CD1 . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B CD1 
9202  C CD2 . LEU D 77  ? 1.5617 1.5617 1.5617 0.0000 0.0000 0.0000 77  LEU B CD2 
9203  N N   . ARG D 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG B N   
9204  C CA  . ARG D 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG B CA  
9205  C C   . ARG D 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG B C   
9206  O O   . ARG D 78  ? 1.5761 1.5761 1.5761 0.0000 0.0000 0.0000 78  ARG B O   
9208  N N   . SER D 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER B N   
9209  C CA  . SER D 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER B CA  
9210  C C   . SER D 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER B C   
9211  O O   . SER D 79  ? 1.6737 1.6737 1.6737 0.0000 0.0000 0.0000 79  SER B O   
9214  N N   . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B N   
9215  C CA  . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B CA  
9216  C C   . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B C   
9217  O O   . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B O   
9218  C CB  . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B CB  
9219  C CG1 . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B CG1 
9220  C CG2 . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B CG2 
9221  C CD1 . ILE D 80  ? 1.5046 1.5046 1.5046 0.0000 0.0000 0.0000 80  ILE B CD1 
9222  N N   . ARG D 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG B N   
9223  C CA  . ARG D 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG B CA  
9224  C C   . ARG D 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG B C   
9225  O O   . ARG D 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG B O   
9226  C CB  . ARG D 81  ? 1.4769 1.4769 1.4769 0.0000 0.0000 0.0000 81  ARG B CB  
9227  N N   . PRO D 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO B N   
9228  C CA  . PRO D 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO B CA  
9229  C C   . PRO D 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO B C   
9230  O O   . PRO D 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO B O   
9231  C CB  . PRO D 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO B CB  
9232  C CG  . PRO D 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO B CG  
9233  C CD  . PRO D 82  ? 1.6608 1.6608 1.6608 0.0000 0.0000 0.0000 82  PRO B CD  
9234  N N   . ASP D 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP B N   
9235  C CA  . ASP D 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP B CA  
9236  C C   . ASP D 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP B C   
9237  O O   . ASP D 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP B O   
9238  C CB  . ASP D 83  ? 1.7330 1.7330 1.7330 0.0000 0.0000 0.0000 83  ASP B CB  
9239  N N   . ASN D 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN B N   
9240  C CA  . ASN D 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN B CA  
9241  C C   . ASN D 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN B C   
9242  O O   . ASN D 84  ? 1.7664 1.7664 1.7664 0.0000 0.0000 0.0000 84  ASN B O   
9247  N N   . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B N   
9248  C CA  . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B CA  
9249  C C   . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B C   
9250  O O   . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B O   
9251  C CB  . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B CB  
9252  C CG  . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B CG  
9253  S SD  . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B SD  
9254  C CE  . MET D 85  ? 1.7808 1.7808 1.7808 0.0000 0.0000 0.0000 85  MET B CE  
9255  N N   . SER D 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER B N   
9256  C CA  . SER D 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER B CA  
9257  C C   . SER D 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER B C   
9258  O O   . SER D 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER B O   
9259  C CB  . SER D 86  ? 1.7556 1.7556 1.7556 0.0000 0.0000 0.0000 86  SER B CB  
9260  N N   . GLU D 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU B N   
9261  C CA  . GLU D 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU B CA  
9262  C C   . GLU D 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU B C   
9263  O O   . GLU D 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU B O   
9264  C CB  . GLU D 87  ? 1.7833 1.7833 1.7833 0.0000 0.0000 0.0000 87  GLU B CB  
9265  N N   . TYR D 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR B N   
9266  C CA  . TYR D 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR B CA  
9267  C C   . TYR D 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR B C   
9268  O O   . TYR D 88  ? 1.7724 1.7724 1.7724 0.0000 0.0000 0.0000 88  TYR B O   
9277  N N   . SER D 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER B N   
9278  C CA  . SER D 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER B CA  
9279  C C   . SER D 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER B C   
9280  O O   . SER D 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER B O   
9281  C CB  . SER D 89  ? 1.7778 1.7778 1.7778 0.0000 0.0000 0.0000 89  SER B CB  
9282  N N   . LYS D 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS B N   
9283  C CA  . LYS D 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS B CA  
9284  C C   . LYS D 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS B C   
9285  O O   . LYS D 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS B O   
9286  C CB  . LYS D 90  ? 1.6938 1.6938 1.6938 0.0000 0.0000 0.0000 90  LYS B CB  
9287  N N   . GLN D 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN B N   
9288  C CA  . GLN D 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN B CA  
9289  C C   . GLN D 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN B C   
9290  O O   . GLN D 91  ? 1.7417 1.7417 1.7417 0.0000 0.0000 0.0000 91  GLN B O   
9296  N N   . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B N   
9297  C CA  . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B CA  
9298  C C   . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B C   
9299  O O   . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B O   
9300  C CB  . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B CB  
9301  C CG  . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B CG  
9302  S SD  . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B SD  
9303  C CE  . MET D 92  ? 1.7060 1.7060 1.7060 0.0000 0.0000 0.0000 92  MET B CE  
9304  N N   . GLN D 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN B N   
9305  C CA  . GLN D 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN B CA  
9306  C C   . GLN D 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN B C   
9307  O O   . GLN D 93  ? 1.5355 1.5355 1.5355 0.0000 0.0000 0.0000 93  GLN B O   
9309  N N   . ARG D 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG B N   
9310  C CA  . ARG D 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG B CA  
9311  C C   . ARG D 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG B C   
9312  O O   . ARG D 94  ? 1.6106 1.6106 1.6106 0.0000 0.0000 0.0000 94  ARG B O   
9320  N N   . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B N   
9321  C CA  . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CA  
9322  C C   . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B C   
9323  O O   . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B O   
9324  C CB  . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CB  
9325  C CG  . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CG  
9326  C CD1 . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CD1 
9327  C CD2 . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CD2 
9328  C CE1 . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CE1 
9329  C CE2 . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CE2 
9330  C CZ  . PHE D 95  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 95  PHE B CZ  
9331  N N   . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B N   
9332  C CA  . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B CA  
9333  C C   . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B C   
9334  O O   . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B O   
9335  C CB  . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B CB  
9336  C CG  . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B CG  
9337  O OD1 . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B OD1 
9338  N ND2 . ASN D 96  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 96  ASN B ND2 
9339  N N   . VAL D 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL B N   
9340  C CA  . VAL D 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL B CA  
9341  C C   . VAL D 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL B C   
9342  O O   . VAL D 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL B O   
9343  C CB  . VAL D 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL B CB  
9344  C CG1 . VAL D 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL B CG1 
9345  C CG2 . VAL D 97  ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 97  VAL B CG2 
9346  N N   . GLY D 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY B N   
9347  C CA  . GLY D 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY B CA  
9348  C C   . GLY D 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY B C   
9349  O O   . GLY D 98  ? 1.5521 1.5521 1.5521 0.0000 0.0000 0.0000 98  GLY B O   
9360  N N   . CYS D 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS B N   
9361  C CA  . CYS D 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS B CA  
9362  C C   . CYS D 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS B C   
9363  O O   . CYS D 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS B O   
9364  C CB  . CYS D 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS B CB  
9365  S SG  . CYS D 101 ? 1.6557 1.6557 1.6557 0.0000 0.0000 0.0000 101 CYS B SG  
9366  N N   . PRO D 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO B N   
9367  C CA  . PRO D 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO B CA  
9368  C C   . PRO D 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO B C   
9369  O O   . PRO D 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO B O   
9370  C CB  . PRO D 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO B CB  
9371  C CG  . PRO D 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO B CG  
9372  C CD  . PRO D 102 ? 1.6993 1.6993 1.6993 0.0000 0.0000 0.0000 102 PRO B CD  
9373  N N   . VAL D 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL B N   
9374  C CA  . VAL D 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL B CA  
9375  C C   . VAL D 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL B C   
9376  O O   . VAL D 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL B O   
9377  C CB  . VAL D 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL B CB  
9378  C CG1 . VAL D 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL B CG1 
9379  C CG2 . VAL D 103 ? 1.6727 1.6727 1.6727 0.0000 0.0000 0.0000 103 VAL B CG2 
9380  N N   . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B N   
9381  C CA  . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CA  
9382  C C   . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B C   
9383  O O   . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B O   
9384  C CB  . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CB  
9385  C CG  . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CG  
9386  C CD1 . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CD1 
9387  C CD2 . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CD2 
9388  C CE1 . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CE1 
9389  C CE2 . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CE2 
9390  C CZ  . PHE D 104 ? 1.5461 1.5461 1.5461 0.0000 0.0000 0.0000 104 PHE B CZ  
9391  N N   . ASP D 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP B N   
9392  C CA  . ASP D 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP B CA  
9393  C C   . ASP D 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP B C   
9394  O O   . ASP D 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP B O   
9395  C CB  . ASP D 105 ? 1.6180 1.6180 1.6180 0.0000 0.0000 0.0000 105 ASP B CB  
9396  N N   . GLY D 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY B N   
9397  C CA  . GLY D 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY B CA  
9398  C C   . GLY D 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY B C   
9399  O O   . GLY D 106 ? 1.5547 1.5547 1.5547 0.0000 0.0000 0.0000 106 GLY B O   
9400  N N   . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B N   
9401  C CA  . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B CA  
9402  C C   . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B C   
9403  O O   . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B O   
9404  C CB  . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B CB  
9405  C CG  . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B CG  
9406  C CD1 . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B CD1 
9407  C CD2 . LEU D 107 ? 1.4762 1.4762 1.4762 0.0000 0.0000 0.0000 107 LEU B CD2 
9408  N N   . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B N   
9409  C CA  . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CA  
9410  C C   . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B C   
9411  O O   . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B O   
9412  C CB  . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CB  
9413  C CG  . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CG  
9414  C CD1 . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CD1 
9415  C CD2 . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CD2 
9416  C CE1 . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CE1 
9417  C CE2 . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CE2 
9418  C CZ  . PHE D 108 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 108 PHE B CZ  
9419  N N   . GLU D 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU B N   
9420  C CA  . GLU D 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU B CA  
9421  C C   . GLU D 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU B C   
9422  O O   . GLU D 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU B O   
9423  C CB  . GLU D 109 ? 1.5412 1.5412 1.5412 0.0000 0.0000 0.0000 109 GLU B CB  
9424  N N   . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B N   
9425  C CA  . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CA  
9426  C C   . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B C   
9427  O O   . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B O   
9428  C CB  . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CB  
9429  C CG  . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CG  
9430  C CD1 . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CD1 
9431  C CD2 . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CD2 
9432  C CE1 . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CE1 
9433  C CE2 . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CE2 
9434  C CZ  . PHE D 110 ? 1.4822 1.4822 1.4822 0.0000 0.0000 0.0000 110 PHE B CZ  
9435  N N   . CYS D 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS B N   
9436  C CA  . CYS D 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS B CA  
9437  C C   . CYS D 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS B C   
9438  O O   . CYS D 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS B O   
9439  C CB  . CYS D 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS B CB  
9440  S SG  . CYS D 111 ? 1.5650 1.5650 1.5650 0.0000 0.0000 0.0000 111 CYS B SG  
9441  N N   . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B N   
9442  C CA  . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B CA  
9443  C C   . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B C   
9444  O O   . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B O   
9445  C CB  . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B CB  
9446  C CG  . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B CG  
9447  C CD  . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B CD  
9448  O OE1 . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B OE1 
9449  N NE2 . GLN D 112 ? 1.6807 1.6807 1.6807 0.0000 0.0000 0.0000 112 GLN B NE2 
9450  N N   . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B N   
9451  C CA  . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B CA  
9452  C C   . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B C   
9453  O O   . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B O   
9454  C CB  . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B CB  
9455  C CG  . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B CG  
9456  C CD1 . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B CD1 
9457  C CD2 . LEU D 113 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 113 LEU B CD2 
9458  N N   . SER D 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER B N   
9459  C CA  . SER D 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER B CA  
9460  C C   . SER D 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER B C   
9461  O O   . SER D 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER B O   
9462  C CB  . SER D 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER B CB  
9463  O OG  . SER D 114 ? 1.4947 1.4947 1.4947 0.0000 0.0000 0.0000 114 SER B OG  
9464  N N   . THR D 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR B N   
9465  C CA  . THR D 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR B CA  
9466  C C   . THR D 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR B C   
9467  O O   . THR D 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR B O   
9468  C CB  . THR D 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR B CB  
9469  O OG1 . THR D 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR B OG1 
9470  C CG2 . THR D 115 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 115 THR B CG2 
9471  N N   . GLY D 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY B N   
9472  C CA  . GLY D 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY B CA  
9473  C C   . GLY D 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY B C   
9474  O O   . GLY D 116 ? 1.5604 1.5604 1.5604 0.0000 0.0000 0.0000 116 GLY B O   
9475  N N   . GLY D 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY B N   
9476  C CA  . GLY D 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY B CA  
9477  C C   . GLY D 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY B C   
9478  O O   . GLY D 117 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 117 GLY B O   
9479  N N   . SER D 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER B N   
9480  C CA  . SER D 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER B CA  
9481  C C   . SER D 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER B C   
9482  O O   . SER D 118 ? 1.4591 1.4591 1.4591 0.0000 0.0000 0.0000 118 SER B O   
9485  N N   . VAL D 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL B N   
9486  C CA  . VAL D 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL B CA  
9487  C C   . VAL D 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL B C   
9488  O O   . VAL D 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL B O   
9489  C CB  . VAL D 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL B CB  
9490  C CG1 . VAL D 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL B CG1 
9491  C CG2 . VAL D 119 ? 1.5530 1.5530 1.5530 0.0000 0.0000 0.0000 119 VAL B CG2 
9492  N N   . ALA D 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA B N   
9493  C CA  . ALA D 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA B CA  
9494  C C   . ALA D 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA B C   
9495  O O   . ALA D 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA B O   
9496  C CB  . ALA D 120 ? 1.6281 1.6281 1.6281 0.0000 0.0000 0.0000 120 ALA B CB  
9497  N N   . GLY D 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY B N   
9498  C CA  . GLY D 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY B CA  
9499  C C   . GLY D 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY B C   
9500  O O   . GLY D 121 ? 1.5485 1.5485 1.5485 0.0000 0.0000 0.0000 121 GLY B O   
9501  N N   . ALA D 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA B N   
9502  C CA  . ALA D 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA B CA  
9503  C C   . ALA D 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA B C   
9504  O O   . ALA D 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA B O   
9505  C CB  . ALA D 122 ? 1.5406 1.5406 1.5406 0.0000 0.0000 0.0000 122 ALA B CB  
9506  N N   . VAL D 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL B N   
9507  C CA  . VAL D 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL B CA  
9508  C C   . VAL D 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL B C   
9509  O O   . VAL D 123 ? 1.5518 1.5518 1.5518 0.0000 0.0000 0.0000 123 VAL B O   
9513  N N   . LYS D 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS B N   
9514  C CA  . LYS D 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS B CA  
9515  C C   . LYS D 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS B C   
9516  O O   . LYS D 124 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 124 LYS B O   
9522  N N   . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B N   
9523  C CA  . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B CA  
9524  C C   . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B C   
9525  O O   . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B O   
9526  C CB  . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B CB  
9527  C CG  . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B CG  
9528  C CD1 . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B CD1 
9529  C CD2 . LEU D 125 ? 1.4989 1.4989 1.4989 0.0000 0.0000 0.0000 125 LEU B CD2 
9530  N N   . ASN D 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN B N   
9531  C CA  . ASN D 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN B CA  
9532  C C   . ASN D 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN B C   
9533  O O   . ASN D 126 ? 1.5924 1.5924 1.5924 0.0000 0.0000 0.0000 126 ASN B O   
9538  N N   . ARG D 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG B N   
9539  C CA  . ARG D 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG B CA  
9540  C C   . ARG D 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG B C   
9541  O O   . ARG D 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG B O   
9542  C CB  . ARG D 127 ? 1.5413 1.5413 1.5413 0.0000 0.0000 0.0000 127 ARG B CB  
9543  N N   . GLN D 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN B N   
9544  C CA  . GLN D 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN B CA  
9545  C C   . GLN D 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN B C   
9546  O O   . GLN D 128 ? 1.5710 1.5710 1.5710 0.0000 0.0000 0.0000 128 GLN B O   
9548  N N   . GLN D 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN B N   
9549  C CA  . GLN D 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN B CA  
9550  C C   . GLN D 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN B C   
9551  O O   . GLN D 129 ? 1.6312 1.6312 1.6312 0.0000 0.0000 0.0000 129 GLN B O   
9557  N N   . THR D 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR B N   
9558  C CA  . THR D 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR B CA  
9559  C C   . THR D 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR B C   
9560  O O   . THR D 130 ? 1.6321 1.6321 1.6321 0.0000 0.0000 0.0000 130 THR B O   
9564  N N   . ASP D 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP B N   
9565  C CA  . ASP D 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP B CA  
9566  C C   . ASP D 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP B C   
9567  O O   . ASP D 131 ? 1.6509 1.6509 1.6509 0.0000 0.0000 0.0000 131 ASP B O   
9572  N N   . MET D 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET B N   
9573  C CA  . MET D 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET B CA  
9574  C C   . MET D 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET B C   
9575  O O   . MET D 132 ? 1.5356 1.5356 1.5356 0.0000 0.0000 0.0000 132 MET B O   
9580  N N   . ALA D 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA B N   
9581  C CA  . ALA D 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA B CA  
9582  C C   . ALA D 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA B C   
9583  O O   . ALA D 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA B O   
9584  C CB  . ALA D 133 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 133 ALA B CB  
9585  N N   . VAL D 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL B N   
9586  C CA  . VAL D 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL B CA  
9587  C C   . VAL D 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL B C   
9588  O O   . VAL D 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL B O   
9589  C CB  . VAL D 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL B CB  
9590  C CG1 . VAL D 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL B CG1 
9591  C CG2 . VAL D 134 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 134 VAL B CG2 
9592  N N   . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B N   
9593  C CA  . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B CA  
9594  C C   . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B C   
9595  O O   . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B O   
9596  C CB  . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B CB  
9597  C CG  . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B CG  
9598  O OD1 . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B OD1 
9599  N ND2 . ASN D 135 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 135 ASN B ND2 
9600  N N   . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B N   
9601  C CA  . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CA  
9602  C C   . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B C   
9603  O O   . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B O   
9604  C CB  . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CB  
9605  C CG  . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CG  
9606  C CD1 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CD1 
9607  C CD2 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CD2 
9608  N NE1 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B NE1 
9609  C CE2 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CE2 
9610  C CE3 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CE3 
9611  C CZ2 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CZ2 
9612  C CZ3 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CZ3 
9613  C CH2 . TRP D 136 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 136 TRP B CH2 
9614  N N   . ALA D 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA B N   
9615  C CA  . ALA D 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA B CA  
9616  C C   . ALA D 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA B C   
9617  O O   . ALA D 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA B O   
9618  C CB  . ALA D 137 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 137 ALA B CB  
9619  N N   . GLY D 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY B N   
9620  C CA  . GLY D 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY B CA  
9621  C C   . GLY D 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY B C   
9622  O O   . GLY D 138 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 138 GLY B O   
9623  N N   . GLY D 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY B N   
9624  C CA  . GLY D 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY B CA  
9625  C C   . GLY D 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY B C   
9626  O O   . GLY D 139 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 139 GLY B O   
9627  N N   . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B N   
9628  C CA  . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B CA  
9629  C C   . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B C   
9630  O O   . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B O   
9631  C CB  . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B CB  
9632  C CG  . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B CG  
9633  C CD1 . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B CD1 
9634  C CD2 . LEU D 140 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 140 LEU B CD2 
9635  N N   . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B N   
9636  C CA  . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B CA  
9637  C C   . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B C   
9638  O O   . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B O   
9639  C CB  . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B CB  
9640  C CG  . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B CG  
9641  N ND1 . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B ND1 
9642  C CD2 . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B CD2 
9643  C CE1 . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B CE1 
9644  N NE2 . HIS D 141 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 141 HIS B NE2 
9645  N N   . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B N   
9646  C CA  . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B CA  
9647  C C   . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B C   
9648  O O   . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B O   
9649  C CB  . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B CB  
9650  C CG  . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B CG  
9651  N ND1 . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B ND1 
9652  C CD2 . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B CD2 
9653  C CE1 . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B CE1 
9654  N NE2 . HIS D 142 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 142 HIS B NE2 
9655  N N   . ALA D 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA B N   
9656  C CA  . ALA D 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA B CA  
9657  C C   . ALA D 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA B C   
9658  O O   . ALA D 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA B O   
9659  C CB  . ALA D 143 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 143 ALA B CB  
9660  N N   . LYS D 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS B N   
9661  C CA  . LYS D 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS B CA  
9662  C C   . LYS D 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS B C   
9663  O O   . LYS D 144 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 144 LYS B O   
9669  N N   . LYS D 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS B N   
9670  C CA  . LYS D 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS B CA  
9671  C C   . LYS D 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS B C   
9672  O O   . LYS D 145 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 145 LYS B O   
9678  N N   . SER D 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER B N   
9679  C CA  . SER D 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER B CA  
9680  C C   . SER D 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER B C   
9681  O O   . SER D 146 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 146 SER B O   
9684  N N   . GLU D 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU B N   
9685  C CA  . GLU D 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU B CA  
9686  C C   . GLU D 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU B C   
9687  O O   . GLU D 147 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 147 GLU B O   
9693  N N   . ALA D 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA B N   
9694  C CA  . ALA D 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA B CA  
9695  C C   . ALA D 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA B C   
9696  O O   . ALA D 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA B O   
9697  C CB  . ALA D 148 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 148 ALA B CB  
9698  N N   . SER D 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER B N   
9699  C CA  . SER D 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER B CA  
9700  C C   . SER D 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER B C   
9701  O O   . SER D 149 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 149 SER B O   
9703  N N   . GLY D 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY B N   
9704  C CA  . GLY D 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY B CA  
9705  C C   . GLY D 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY B C   
9706  O O   . GLY D 150 ? 1.5398 1.5398 1.5398 0.0000 0.0000 0.0000 150 GLY B O   
9707  N N   . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B N   
9708  C CA  . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CA  
9709  C C   . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B C   
9710  O O   . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B O   
9711  C CB  . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CB  
9712  C CG  . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CG  
9713  C CD1 . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CD1 
9714  C CD2 . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CD2 
9715  C CE1 . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CE1 
9716  C CE2 . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CE2 
9717  C CZ  . PHE D 151 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 151 PHE B CZ  
9718  N N   . CYS D 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS B N   
9719  C CA  . CYS D 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS B CA  
9720  C C   . CYS D 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS B C   
9721  O O   . CYS D 152 ? 1.4893 1.4893 1.4893 0.0000 0.0000 0.0000 152 CYS B O   
9724  N N   . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B N   
9725  C CA  . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CA  
9726  C C   . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B C   
9727  O O   . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B O   
9728  C CB  . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CB  
9729  C CG  . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CG  
9730  C CD1 . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CD1 
9731  C CD2 . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CD2 
9732  C CE1 . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CE1 
9733  C CE2 . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CE2 
9734  C CZ  . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B CZ  
9735  O OH  . TYR D 153 ? 1.5579 1.5579 1.5579 0.0000 0.0000 0.0000 153 TYR B OH  
9743  N N   . ASN D 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN B N   
9744  C CA  . ASN D 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN B CA  
9745  C C   . ASN D 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN B C   
9746  O O   . ASN D 155 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 155 ASN B O   
9751  N N   . ASP D 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP B N   
9752  C CA  . ASP D 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP B CA  
9753  C C   . ASP D 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP B C   
9754  O O   . ASP D 156 ? 1.5609 1.5609 1.5609 0.0000 0.0000 0.0000 156 ASP B O   
9759  N N   . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B N   
9760  C CA  . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B CA  
9761  C C   . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B C   
9762  O O   . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B O   
9763  C CB  . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B CB  
9764  C CG1 . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B CG1 
9765  C CG2 . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B CG2 
9766  C CD1 . ILE D 157 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 157 ILE B CD1 
9767  N N   . VAL D 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL B N   
9768  C CA  . VAL D 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL B CA  
9769  C C   . VAL D 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL B C   
9770  O O   . VAL D 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL B O   
9771  C CB  . VAL D 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL B CB  
9772  C CG1 . VAL D 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL B CG1 
9773  C CG2 . VAL D 158 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 158 VAL B CG2 
9774  N N   . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B N   
9775  C CA  . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B CA  
9776  C C   . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B C   
9777  O O   . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B O   
9778  C CB  . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B CB  
9779  C CG  . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B CG  
9780  C CD1 . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B CD1 
9781  C CD2 . LEU D 159 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 159 LEU B CD2 
9782  N N   . ALA D 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA B N   
9783  C CA  . ALA D 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA B CA  
9784  C C   . ALA D 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA B C   
9785  O O   . ALA D 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA B O   
9786  C CB  . ALA D 160 ? 1.4504 1.4504 1.4504 0.0000 0.0000 0.0000 160 ALA B CB  
9787  N N   . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B N   
9788  C CA  . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B CA  
9789  C C   . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B C   
9790  O O   . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B O   
9791  C CB  . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B CB  
9792  C CG1 . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B CG1 
9793  C CG2 . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B CG2 
9794  C CD1 . ILE D 161 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 161 ILE B CD1 
9795  N N   . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B N   
9796  C CA  . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B CA  
9797  C C   . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B C   
9798  O O   . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B O   
9799  C CB  . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B CB  
9800  C CG  . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B CG  
9801  C CD1 . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B CD1 
9802  C CD2 . LEU D 162 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 162 LEU B CD2 
9803  N N   . GLU D 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU B N   
9804  C CA  . GLU D 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU B CA  
9805  C C   . GLU D 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU B C   
9806  O O   . GLU D 163 ? 1.5063 1.5063 1.5063 0.0000 0.0000 0.0000 163 GLU B O   
9812  N N   . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B N   
9813  C CA  . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B CA  
9814  C C   . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B C   
9815  O O   . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B O   
9816  C CB  . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B CB  
9817  C CG  . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B CG  
9818  C CD1 . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B CD1 
9819  C CD2 . LEU D 164 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 164 LEU B CD2 
9820  N N   . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B N   
9821  C CA  . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B CA  
9822  C C   . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B C   
9823  O O   . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B O   
9824  C CB  . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B CB  
9825  C CG  . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B CG  
9826  C CD1 . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B CD1 
9827  C CD2 . LEU D 165 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 165 LEU B CD2 
9828  N N   . LYS D 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS B N   
9829  C CA  . LYS D 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS B CA  
9830  C C   . LYS D 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS B C   
9831  O O   . LYS D 166 ? 1.6222 1.6222 1.6222 0.0000 0.0000 0.0000 166 LYS B O   
9837  N N   . TYR D 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR B N   
9838  C CA  . TYR D 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR B CA  
9839  C C   . TYR D 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR B C   
9840  O O   . TYR D 167 ? 1.6113 1.6113 1.6113 0.0000 0.0000 0.0000 167 TYR B O   
9849  N N   . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B N   
9850  C CA  . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B CA  
9851  C C   . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B C   
9852  O O   . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B O   
9853  C CB  . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B CB  
9854  C CG  . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B CG  
9855  N ND1 . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B ND1 
9856  C CD2 . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B CD2 
9857  C CE1 . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B CE1 
9858  N NE2 . HIS D 168 ? 1.4929 1.4929 1.4929 0.0000 0.0000 0.0000 168 HIS B NE2 
9859  N N   . GLN D 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN B N   
9860  C CA  . GLN D 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN B CA  
9861  C C   . GLN D 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN B C   
9862  O O   . GLN D 169 ? 1.5614 1.5614 1.5614 0.0000 0.0000 0.0000 169 GLN B O   
9868  N N   . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B N   
9869  C CA  . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B CA  
9870  C C   . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B C   
9871  O O   . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B O   
9872  C CB  . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B CB  
9873  C CG  . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B CG  
9874  C CD  . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B CD  
9875  N NE  . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B NE  
9876  C CZ  . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B CZ  
9877  N NH1 . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B NH1 
9878  N NH2 . ARG D 170 ? 1.4443 1.4443 1.4443 0.0000 0.0000 0.0000 170 ARG B NH2 
9879  N N   . VAL D 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL B N   
9880  C CA  . VAL D 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL B CA  
9881  C C   . VAL D 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL B C   
9882  O O   . VAL D 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL B O   
9883  C CB  . VAL D 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL B CB  
9884  C CG1 . VAL D 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL B CG1 
9885  C CG2 . VAL D 171 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 171 VAL B CG2 
9886  N N   . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B N   
9887  C CA  . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B CA  
9888  C C   . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B C   
9889  O O   . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B O   
9890  C CB  . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B CB  
9891  C CG  . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B CG  
9892  C CD1 . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B CD1 
9893  C CD2 . LEU D 172 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 172 LEU B CD2 
9894  N N   . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B N   
9895  C CA  . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CA  
9896  C C   . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B C   
9897  O O   . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B O   
9898  C CB  . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CB  
9899  C CG  . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CG  
9900  C CD1 . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CD1 
9901  C CD2 . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CD2 
9902  C CE1 . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CE1 
9903  C CE2 . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CE2 
9904  C CZ  . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B CZ  
9905  O OH  . TYR D 173 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 173 TYR B OH  
9906  N N   . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B N   
9907  C CA  . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B CA  
9908  C C   . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B C   
9909  O O   . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B O   
9910  C CB  . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B CB  
9911  C CG1 . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B CG1 
9912  C CG2 . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B CG2 
9913  C CD1 . ILE D 174 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 174 ILE B CD1 
9914  N N   . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B N   
9915  C CA  . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B CA  
9916  C C   . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B C   
9917  O O   . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B O   
9918  C CB  . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B CB  
9919  C CG  . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B CG  
9920  O OD1 . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B OD1 
9921  O OD2 . ASP D 175 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 175 ASP B OD2 
9922  N N   . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B N   
9923  C CA  . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B CA  
9924  C C   . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B C   
9925  O O   . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B O   
9926  C CB  . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B CB  
9927  C CG1 . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B CG1 
9928  C CG2 . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B CG2 
9929  C CD1 . ILE D 176 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 176 ILE B CD1 
9930  N N   . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B N   
9931  C CA  . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B CA  
9932  C C   . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B C   
9933  O O   . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B O   
9934  C CB  . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B CB  
9935  C CG  . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B CG  
9936  O OD1 . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B OD1 
9937  O OD2 . ASP D 177 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 177 ASP B OD2 
9938  N N   . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B N   
9939  C CA  . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B CA  
9940  C C   . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B C   
9941  O O   . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B O   
9942  C CB  . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B CB  
9943  C CG1 . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B CG1 
9944  C CG2 . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B CG2 
9945  C CD1 . ILE D 178 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 178 ILE B CD1 
9946  N N   . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B N   
9947  C CA  . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B CA  
9948  C C   . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B C   
9949  O O   . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B O   
9950  C CB  . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B CB  
9951  C CG  . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B CG  
9952  N ND1 . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B ND1 
9953  C CD2 . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B CD2 
9954  C CE1 . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B CE1 
9955  N NE2 . HIS D 179 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 179 HIS B NE2 
9956  N N   . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B N   
9957  C CA  . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B CA  
9958  C C   . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B C   
9959  O O   . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B O   
9960  C CB  . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B CB  
9961  C CG  . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B CG  
9962  N ND1 . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B ND1 
9963  C CD2 . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B CD2 
9964  C CE1 . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B CE1 
9965  N NE2 . HIS D 180 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 180 HIS B NE2 
9966  N N   . GLY D 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY B N   
9967  C CA  . GLY D 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY B CA  
9968  C C   . GLY D 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY B C   
9969  O O   . GLY D 181 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 181 GLY B O   
9970  N N   . ASP D 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP B N   
9971  C CA  . ASP D 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP B CA  
9972  C C   . ASP D 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP B C   
9973  O O   . ASP D 182 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 182 ASP B O   
9978  N N   . GLY D 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY B N   
9979  C CA  . GLY D 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY B CA  
9980  C C   . GLY D 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY B C   
9981  O O   . GLY D 183 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 183 GLY B O   
9982  N N   . VAL D 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL B N   
9983  C CA  . VAL D 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL B CA  
9984  C C   . VAL D 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL B C   
9985  O O   . VAL D 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL B O   
9986  C CB  . VAL D 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL B CB  
9987  C CG1 . VAL D 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL B CG1 
9988  C CG2 . VAL D 184 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 184 VAL B CG2 
9989  N N   . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B N   
9990  C CA  . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B CA  
9991  C C   . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B C   
9992  O O   . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B O   
9993  C CB  . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B CB  
9994  C CG  . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B CG  
9995  C CD  . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B CD  
9996  O OE1 . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B OE1 
9997  O OE2 . GLU D 185 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 185 GLU B OE2 
9998  N N   . GLU D 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU B N   
9999  C CA  . GLU D 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU B CA  
10000 C C   . GLU D 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU B C   
10001 O O   . GLU D 186 ? 1.5680 1.5680 1.5680 0.0000 0.0000 0.0000 186 GLU B O   
10007 N N   . ALA D 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA B N   
10008 C CA  . ALA D 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA B CA  
10009 C C   . ALA D 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA B C   
10010 O O   . ALA D 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA B O   
10011 C CB  . ALA D 187 ? 1.4640 1.4640 1.4640 0.0000 0.0000 0.0000 187 ALA B CB  
10012 N N   . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B N   
10013 C CA  . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CA  
10014 C C   . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B C   
10015 O O   . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B O   
10016 C CB  . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CB  
10017 C CG  . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CG  
10018 C CD1 . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CD1 
10019 C CD2 . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CD2 
10020 C CE1 . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CE1 
10021 C CE2 . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CE2 
10022 C CZ  . PHE D 188 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 188 PHE B CZ  
10023 N N   . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B N   
10024 C CA  . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CA  
10025 C C   . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B C   
10026 O O   . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B O   
10027 C CB  . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CB  
10028 C CG  . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CG  
10029 C CD1 . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CD1 
10030 C CD2 . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CD2 
10031 C CE1 . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CE1 
10032 C CE2 . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CE2 
10033 C CZ  . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B CZ  
10034 O OH  . TYR D 189 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 189 TYR B OH  
10035 N N   . THR D 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR B N   
10036 C CA  . THR D 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR B CA  
10037 C C   . THR D 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR B C   
10038 O O   . THR D 190 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 190 THR B O   
10042 N N   . THR D 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR B N   
10043 C CA  . THR D 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR B CA  
10044 C C   . THR D 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR B C   
10045 O O   . THR D 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR B O   
10046 C CB  . THR D 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR B CB  
10047 O OG1 . THR D 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR B OG1 
10048 C CG2 . THR D 191 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 191 THR B CG2 
10049 N N   . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B N   
10050 C CA  . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B CA  
10051 C C   . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B C   
10052 O O   . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B O   
10053 C CB  . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B CB  
10054 C CG  . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B CG  
10055 O OD1 . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B OD1 
10056 O OD2 . ASP D 192 ? 1.4715 1.4715 1.4715 0.0000 0.0000 0.0000 192 ASP B OD2 
10057 N N   . ARG D 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG B N   
10058 C CA  . ARG D 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG B CA  
10059 C C   . ARG D 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG B C   
10060 O O   . ARG D 193 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 193 ARG B O   
10068 N N   . VAL D 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL B N   
10069 C CA  . VAL D 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL B CA  
10070 C C   . VAL D 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL B C   
10071 O O   . VAL D 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL B O   
10072 C CB  . VAL D 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL B CB  
10073 C CG1 . VAL D 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL B CG1 
10074 C CG2 . VAL D 194 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 194 VAL B CG2 
10075 N N   . MET D 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET B N   
10076 C CA  . MET D 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET B CA  
10077 C C   . MET D 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET B C   
10078 O O   . MET D 195 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 195 MET B O   
10083 N N   . THR D 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR B N   
10084 C CA  . THR D 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR B CA  
10085 C C   . THR D 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR B C   
10086 O O   . THR D 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR B O   
10087 C CB  . THR D 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR B CB  
10088 O OG1 . THR D 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR B OG1 
10089 C CG2 . THR D 196 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 196 THR B CG2 
10090 N N   . VAL D 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL B N   
10091 C CA  . VAL D 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL B CA  
10092 C C   . VAL D 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL B C   
10093 O O   . VAL D 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL B O   
10094 C CB  . VAL D 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL B CB  
10095 C CG1 . VAL D 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL B CG1 
10096 C CG2 . VAL D 197 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 197 VAL B CG2 
10097 N N   . SER D 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER B N   
10098 C CA  . SER D 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER B CA  
10099 C C   . SER D 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER B C   
10100 O O   . SER D 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER B O   
10101 C CB  . SER D 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER B CB  
10102 O OG  . SER D 198 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 198 SER B OG  
10103 N N   . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B N   
10104 C CA  . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CA  
10105 C C   . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B C   
10106 O O   . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B O   
10107 C CB  . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CB  
10108 C CG  . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CG  
10109 C CD1 . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CD1 
10110 C CD2 . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CD2 
10111 C CE1 . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CE1 
10112 C CE2 . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CE2 
10113 C CZ  . PHE D 199 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 199 PHE B CZ  
10114 N N   . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B N   
10115 C CA  . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B CA  
10116 C C   . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B C   
10117 O O   . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B O   
10118 C CB  . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B CB  
10119 C CG  . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B CG  
10120 N ND1 . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B ND1 
10121 C CD2 . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B CD2 
10122 C CE1 . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B CE1 
10123 N NE2 . HIS D 200 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 200 HIS B NE2 
10124 N N   . LYS D 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS B N   
10125 C CA  . LYS D 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS B CA  
10126 C C   . LYS D 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS B C   
10127 O O   . LYS D 201 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 201 LYS B O   
10133 N N   . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B N   
10134 C CA  . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CA  
10135 C C   . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B C   
10136 O O   . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B O   
10137 C CB  . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CB  
10138 C CG  . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CG  
10139 C CD1 . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CD1 
10140 C CD2 . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CD2 
10141 C CE1 . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CE1 
10142 C CE2 . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CE2 
10143 C CZ  . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B CZ  
10144 O OH  . TYR D 202 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 202 TYR B OH  
10145 N N   . GLY D 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY B N   
10146 C CA  . GLY D 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY B CA  
10147 C C   . GLY D 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY B C   
10148 O O   . GLY D 203 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 203 GLY B O   
10149 N N   . GLU D 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU B N   
10150 C CA  . GLU D 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU B CA  
10151 C C   . GLU D 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU B C   
10152 O O   . GLU D 204 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 204 GLU B O   
10158 N N   . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B N   
10159 C CA  . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CA  
10160 C C   . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B C   
10161 O O   . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B O   
10162 C CB  . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CB  
10163 C CG  . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CG  
10164 C CD1 . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CD1 
10165 C CD2 . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CD2 
10166 C CE1 . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CE1 
10167 C CE2 . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CE2 
10168 C CZ  . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B CZ  
10169 O OH  . TYR D 205 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 205 TYR B OH  
10170 N N   . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B N   
10171 C CA  . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CA  
10172 C C   . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B C   
10173 O O   . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B O   
10174 C CB  . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CB  
10175 C CG  . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CG  
10176 C CD1 . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CD1 
10177 C CD2 . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CD2 
10178 C CE1 . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CE1 
10179 C CE2 . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CE2 
10180 C CZ  . PHE D 206 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 206 PHE B CZ  
10181 N N   . PRO D 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO B N   
10182 C CA  . PRO D 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO B CA  
10183 C C   . PRO D 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO B C   
10184 O O   . PRO D 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO B O   
10185 C CB  . PRO D 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO B CB  
10186 C CG  . PRO D 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO B CG  
10187 C CD  . PRO D 207 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 207 PRO B CD  
10188 N N   . GLY D 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY B N   
10189 C CA  . GLY D 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY B CA  
10190 C C   . GLY D 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY B C   
10191 O O   . GLY D 208 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 208 GLY B O   
10192 N N   . THR D 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR B N   
10193 C CA  . THR D 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR B CA  
10194 C C   . THR D 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR B C   
10195 O O   . THR D 209 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 209 THR B O   
10199 N N   . GLY D 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY B N   
10200 C CA  . GLY D 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY B CA  
10201 C C   . GLY D 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY B C   
10202 O O   . GLY D 210 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 210 GLY B O   
10203 N N   . ASP D 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP B N   
10204 C CA  . ASP D 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP B CA  
10205 C C   . ASP D 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP B C   
10206 O O   . ASP D 211 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 211 ASP B O   
10211 N N   . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B N   
10212 C CA  . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B CA  
10213 C C   . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B C   
10214 O O   . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B O   
10215 C CB  . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B CB  
10216 C CG  . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B CG  
10217 C CD1 . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B CD1 
10218 C CD2 . LEU D 212 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 212 LEU B CD2 
10219 N N   . ARG D 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG B N   
10220 C CA  . ARG D 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG B CA  
10221 C C   . ARG D 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG B C   
10222 O O   . ARG D 213 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 213 ARG B O   
10230 N N   . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B N   
10231 C CA  . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B CA  
10232 C C   . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B C   
10233 O O   . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B O   
10234 C CB  . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B CB  
10235 C CG  . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B CG  
10236 O OD1 . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B OD1 
10237 O OD2 . ASP D 214 ? 1.4795 1.4795 1.4795 0.0000 0.0000 0.0000 214 ASP B OD2 
10238 N N   . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B N   
10239 C CA  . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B CA  
10240 C C   . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B C   
10241 O O   . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B O   
10242 C CB  . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B CB  
10243 C CG1 . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B CG1 
10244 C CG2 . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B CG2 
10245 C CD1 . ILE D 215 ? 1.5317 1.5317 1.5317 0.0000 0.0000 0.0000 215 ILE B CD1 
10246 N N   . GLY D 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY B N   
10247 C CA  . GLY D 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY B CA  
10248 C C   . GLY D 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY B C   
10249 O O   . GLY D 216 ? 1.5016 1.5016 1.5016 0.0000 0.0000 0.0000 216 GLY B O   
10250 N N   . ALA D 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA B N   
10251 C CA  . ALA D 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA B CA  
10252 C C   . ALA D 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA B C   
10253 O O   . ALA D 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA B O   
10254 C CB  . ALA D 217 ? 1.6363 1.6363 1.6363 0.0000 0.0000 0.0000 217 ALA B CB  
10255 N N   . GLY D 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY B N   
10256 C CA  . GLY D 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY B CA  
10257 C C   . GLY D 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY B C   
10258 O O   . GLY D 218 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 218 GLY B O   
10259 N N   . LYS D 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS B N   
10260 C CA  . LYS D 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS B CA  
10261 C C   . LYS D 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS B C   
10262 O O   . LYS D 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS B O   
10263 C CB  . LYS D 219 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 219 LYS B CB  
10264 N N   . GLY D 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY B N   
10265 C CA  . GLY D 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY B CA  
10266 C C   . GLY D 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY B C   
10267 O O   . GLY D 220 ? 1.5726 1.5726 1.5726 0.0000 0.0000 0.0000 220 GLY B O   
10268 N N   . LYS D 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS B N   
10269 C CA  . LYS D 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS B CA  
10270 C C   . LYS D 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS B C   
10271 O O   . LYS D 221 ? 1.6093 1.6093 1.6093 0.0000 0.0000 0.0000 221 LYS B O   
10277 N N   . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B N   
10278 C CA  . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CA  
10279 C C   . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B C   
10280 O O   . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B O   
10281 C CB  . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CB  
10282 C CG  . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CG  
10283 C CD1 . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CD1 
10284 C CD2 . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CD2 
10285 C CE1 . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CE1 
10286 C CE2 . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CE2 
10287 C CZ  . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B CZ  
10288 O OH  . TYR D 222 ? 1.5996 1.5996 1.5996 0.0000 0.0000 0.0000 222 TYR B OH  
10289 N N   . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B N   
10290 C CA  . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CA  
10291 C C   . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B C   
10292 O O   . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B O   
10293 C CB  . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CB  
10294 C CG  . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CG  
10295 C CD1 . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CD1 
10296 C CD2 . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CD2 
10297 C CE1 . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CE1 
10298 C CE2 . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CE2 
10299 C CZ  . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B CZ  
10300 O OH  . TYR D 223 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 223 TYR B OH  
10301 N N   . ALA D 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA B N   
10302 C CA  . ALA D 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA B CA  
10303 C C   . ALA D 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA B C   
10304 O O   . ALA D 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA B O   
10305 C CB  . ALA D 224 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 224 ALA B CB  
10306 N N   . VAL D 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL B N   
10307 C CA  . VAL D 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL B CA  
10308 C C   . VAL D 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL B C   
10309 O O   . VAL D 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL B O   
10310 C CB  . VAL D 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL B CB  
10311 C CG1 . VAL D 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL B CG1 
10312 C CG2 . VAL D 225 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 225 VAL B CG2 
10313 N N   . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B N   
10314 C CA  . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B CA  
10315 C C   . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B C   
10316 O O   . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B O   
10317 C CB  . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B CB  
10318 C CG  . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B CG  
10319 O OD1 . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B OD1 
10320 N ND2 . ASN D 226 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 226 ASN B ND2 
10321 N N   . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B N   
10322 C CA  . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CA  
10323 C C   . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B C   
10324 O O   . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B O   
10325 C CB  . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CB  
10326 C CG  . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CG  
10327 C CD1 . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CD1 
10328 C CD2 . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CD2 
10329 C CE1 . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CE1 
10330 C CE2 . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CE2 
10331 C CZ  . PHE D 227 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 227 PHE B CZ  
10332 N N   . PRO D 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO B N   
10333 C CA  . PRO D 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO B CA  
10334 C C   . PRO D 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO B C   
10335 O O   . PRO D 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO B O   
10336 C CB  . PRO D 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO B CB  
10337 C CG  . PRO D 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO B CG  
10338 C CD  . PRO D 228 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 228 PRO B CD  
10339 N N   . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B N   
10340 C CA  . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B CA  
10341 C C   . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B C   
10342 O O   . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B O   
10343 C CB  . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B CB  
10344 C CG  . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B CG  
10345 S SD  . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B SD  
10346 C CE  . MET D 229 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 229 MET B CE  
10347 N N   . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B N   
10348 C CA  . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B CA  
10349 C C   . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B C   
10350 O O   . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B O   
10351 C CB  . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B CB  
10352 C CG  . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B CG  
10353 C CD  . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B CD  
10354 N NE  . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B NE  
10355 C CZ  . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B CZ  
10356 N NH1 . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B NH1 
10357 N NH2 . ARG D 230 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 230 ARG B NH2 
10358 N N   . ASP D 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP B N   
10359 C CA  . ASP D 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP B CA  
10360 C C   . ASP D 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP B C   
10361 O O   . ASP D 231 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 231 ASP B O   
10366 N N   . GLY D 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY B N   
10367 C CA  . GLY D 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY B CA  
10368 C C   . GLY D 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY B C   
10369 O O   . GLY D 232 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 232 GLY B O   
10370 N N   . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B N   
10371 C CA  . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B CA  
10372 C C   . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B C   
10373 O O   . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B O   
10374 C CB  . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B CB  
10375 C CG1 . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B CG1 
10376 C CG2 . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B CG2 
10377 C CD1 . ILE D 233 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 233 ILE B CD1 
10378 N N   . ASP D 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP B N   
10379 C CA  . ASP D 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP B CA  
10380 C C   . ASP D 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP B C   
10381 O O   . ASP D 234 ? 1.4920 1.4920 1.4920 0.0000 0.0000 0.0000 234 ASP B O   
10386 N N   . ASP D 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP B N   
10387 C CA  . ASP D 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP B CA  
10388 C C   . ASP D 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP B C   
10389 O O   . ASP D 235 ? 1.5397 1.5397 1.5397 0.0000 0.0000 0.0000 235 ASP B O   
10394 N N   . GLU D 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU B N   
10395 C CA  . GLU D 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU B CA  
10396 C C   . GLU D 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU B C   
10397 O O   . GLU D 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU B O   
10398 C CB  . GLU D 236 ? 1.4976 1.4976 1.4976 0.0000 0.0000 0.0000 236 GLU B CB  
10399 N N   . SER D 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER B N   
10400 C CA  . SER D 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER B CA  
10401 C C   . SER D 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER B C   
10402 O O   . SER D 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER B O   
10403 C CB  . SER D 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER B CB  
10404 O OG  . SER D 237 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 237 SER B OG  
10405 N N   . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B N   
10406 C CA  . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CA  
10407 C C   . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B C   
10408 O O   . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B O   
10409 C CB  . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CB  
10410 C CG  . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CG  
10411 C CD1 . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CD1 
10412 C CD2 . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CD2 
10413 C CE1 . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CE1 
10414 C CE2 . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CE2 
10415 C CZ  . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B CZ  
10416 O OH  . TYR D 238 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 238 TYR B OH  
10417 N N   . GLY D 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY B N   
10418 C CA  . GLY D 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY B CA  
10419 C C   . GLY D 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY B C   
10420 O O   . GLY D 239 ? 1.4647 1.4647 1.4647 0.0000 0.0000 0.0000 239 GLY B O   
10421 N N   . GLN D 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN B N   
10422 C CA  . GLN D 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN B CA  
10423 C C   . GLN D 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN B C   
10424 O O   . GLN D 240 ? 1.4890 1.4890 1.4890 0.0000 0.0000 0.0000 240 GLN B O   
10430 N N   . ILE D 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE B N   
10431 C CA  . ILE D 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE B CA  
10432 C C   . ILE D 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE B C   
10433 O O   . ILE D 241 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 241 ILE B O   
10438 N N   . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B N   
10439 C CA  . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CA  
10440 C C   . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B C   
10441 O O   . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B O   
10442 C CB  . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CB  
10443 C CG  . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CG  
10444 C CD1 . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CD1 
10445 C CD2 . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CD2 
10446 C CE1 . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CE1 
10447 C CE2 . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CE2 
10448 C CZ  . PHE D 242 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 242 PHE B CZ  
10449 N N   . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B N   
10450 C CA  . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B CA  
10451 C C   . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B C   
10452 O O   . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B O   
10453 C CB  . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B CB  
10454 C CG  . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B CG  
10455 C CD  . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B CD  
10456 C CE  . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B CE  
10457 N NZ  . LYS D 243 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 243 LYS B NZ  
10458 N N   . PRO D 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO B N   
10459 C CA  . PRO D 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO B CA  
10460 C C   . PRO D 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO B C   
10461 O O   . PRO D 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO B O   
10462 C CB  . PRO D 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO B CB  
10463 C CG  . PRO D 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO B CG  
10464 C CD  . PRO D 244 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 244 PRO B CD  
10465 N N   . ILE D 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE B N   
10466 C CA  . ILE D 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE B CA  
10467 C C   . ILE D 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE B C   
10468 O O   . ILE D 245 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 245 ILE B O   
10473 N N   . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B N   
10474 C CA  . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B CA  
10475 C C   . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B C   
10476 O O   . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B O   
10477 C CB  . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B CB  
10478 C CG1 . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B CG1 
10479 C CG2 . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B CG2 
10480 C CD1 . ILE D 246 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 246 ILE B CD1 
10481 N N   . SER D 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER B N   
10482 C CA  . SER D 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER B CA  
10483 C C   . SER D 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER B C   
10484 O O   . SER D 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER B O   
10485 C CB  . SER D 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER B CB  
10486 O OG  . SER D 247 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 247 SER B OG  
10487 N N   . LYS D 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS B N   
10488 C CA  . LYS D 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS B CA  
10489 C C   . LYS D 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS B C   
10490 O O   . LYS D 248 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 248 LYS B O   
10496 N N   . VAL D 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL B N   
10497 C CA  . VAL D 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL B CA  
10498 C C   . VAL D 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL B C   
10499 O O   . VAL D 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL B O   
10500 C CB  . VAL D 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL B CB  
10501 C CG1 . VAL D 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL B CG1 
10502 C CG2 . VAL D 249 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 249 VAL B CG2 
10503 N N   . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B N   
10504 C CA  . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B CA  
10505 C C   . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B C   
10506 O O   . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B O   
10507 C CB  . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B CB  
10508 C CG  . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B CG  
10509 S SD  . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B SD  
10510 C CE  . MET D 250 ? 1.4660 1.4660 1.4660 0.0000 0.0000 0.0000 250 MET B CE  
10511 N N   . GLU D 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU B N   
10512 C CA  . GLU D 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU B CA  
10513 C C   . GLU D 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU B C   
10514 O O   . GLU D 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU B O   
10515 C CB  . GLU D 251 ? 1.4939 1.4939 1.4939 0.0000 0.0000 0.0000 251 GLU B CB  
10516 N N   . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B N   
10517 C CA  . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B CA  
10518 C C   . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B C   
10519 O O   . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B O   
10520 C CB  . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B CB  
10521 C CG  . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B CG  
10522 S SD  . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B SD  
10523 C CE  . MET D 252 ? 1.5962 1.5962 1.5962 0.0000 0.0000 0.0000 252 MET B CE  
10524 N N   . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B N   
10525 C CA  . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CA  
10526 C C   . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B C   
10527 O O   . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B O   
10528 C CB  . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CB  
10529 C CG  . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CG  
10530 C CD1 . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CD1 
10531 C CD2 . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CD2 
10532 C CE1 . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CE1 
10533 C CE2 . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CE2 
10534 C CZ  . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B CZ  
10535 O OH  . TYR D 253 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 253 TYR B OH  
10536 N N   . GLN D 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN B N   
10537 C CA  . GLN D 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN B CA  
10538 C C   . GLN D 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN B C   
10539 O O   . GLN D 254 ? 1.4701 1.4701 1.4701 0.0000 0.0000 0.0000 254 GLN B O   
10545 N N   . PRO D 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO B N   
10546 C CA  . PRO D 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO B CA  
10547 C C   . PRO D 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO B C   
10548 O O   . PRO D 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO B O   
10549 C CB  . PRO D 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO B CB  
10550 C CG  . PRO D 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO B CG  
10551 C CD  . PRO D 255 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 255 PRO B CD  
10552 N N   . SER D 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER B N   
10553 C CA  . SER D 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER B CA  
10554 C C   . SER D 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER B C   
10555 O O   . SER D 256 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 256 SER B O   
10558 N N   . ALA D 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA B N   
10559 C CA  . ALA D 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA B CA  
10560 C C   . ALA D 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA B C   
10561 O O   . ALA D 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA B O   
10562 C CB  . ALA D 257 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 257 ALA B CB  
10563 N N   . VAL D 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL B N   
10564 C CA  . VAL D 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL B CA  
10565 C C   . VAL D 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL B C   
10566 O O   . VAL D 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL B O   
10567 C CB  . VAL D 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL B CB  
10568 C CG1 . VAL D 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL B CG1 
10569 C CG2 . VAL D 258 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 258 VAL B CG2 
10570 N N   . VAL D 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL B N   
10571 C CA  . VAL D 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL B CA  
10572 C C   . VAL D 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL B C   
10573 O O   . VAL D 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL B O   
10574 C CB  . VAL D 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL B CB  
10575 C CG1 . VAL D 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL B CG1 
10576 C CG2 . VAL D 259 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 259 VAL B CG2 
10577 N N   . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B N   
10578 C CA  . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B CA  
10579 C C   . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B C   
10580 O O   . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B O   
10581 C CB  . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B CB  
10582 C CG  . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B CG  
10583 C CD1 . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B CD1 
10584 C CD2 . LEU D 260 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 260 LEU B CD2 
10585 N N   . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B N   
10586 C CA  . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B CA  
10587 C C   . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B C   
10588 O O   . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B O   
10589 C CB  . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B CB  
10590 C CG  . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B CG  
10591 C CD  . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B CD  
10592 O OE1 . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B OE1 
10593 N NE2 . GLN D 261 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 261 GLN B NE2 
10594 N N   . CYS D 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS B N   
10595 C CA  . CYS D 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS B CA  
10596 C C   . CYS D 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS B C   
10597 O O   . CYS D 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS B O   
10598 C CB  . CYS D 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS B CB  
10599 S SG  . CYS D 262 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 262 CYS B SG  
10600 N N   . GLY D 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY B N   
10601 C CA  . GLY D 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY B CA  
10602 C C   . GLY D 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY B C   
10603 O O   . GLY D 263 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 263 GLY B O   
10604 N N   . ALA D 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA B N   
10605 C CA  . ALA D 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA B CA  
10606 C C   . ALA D 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA B C   
10607 O O   . ALA D 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA B O   
10608 C CB  . ALA D 264 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 264 ALA B CB  
10609 N N   . ASP D 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP B N   
10610 C CA  . ASP D 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP B CA  
10611 C C   . ASP D 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP B C   
10612 O O   . ASP D 265 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 265 ASP B O   
10617 N N   . SER D 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER B N   
10618 C CA  . SER D 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER B CA  
10619 C C   . SER D 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER B C   
10620 O O   . SER D 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER B O   
10621 C CB  . SER D 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER B CB  
10622 O OG  . SER D 266 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 266 SER B OG  
10623 N N   . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B N   
10624 C CA  . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B CA  
10625 C C   . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B C   
10626 O O   . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B O   
10627 C CB  . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B CB  
10628 C CG  . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B CG  
10629 C CD1 . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B CD1 
10630 C CD2 . LEU D 267 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 267 LEU B CD2 
10631 N N   . SER D 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER B N   
10632 C CA  . SER D 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER B CA  
10633 C C   . SER D 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER B C   
10634 O O   . SER D 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER B O   
10635 C CB  . SER D 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER B CB  
10636 O OG  . SER D 268 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 268 SER B OG  
10637 N N   . GLY D 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY B N   
10638 C CA  . GLY D 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY B CA  
10639 C C   . GLY D 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY B C   
10640 O O   . GLY D 269 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 269 GLY B O   
10660 N N   . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B N   
10661 C CA  . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B CA  
10662 C C   . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B C   
10663 O O   . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B O   
10664 C CB  . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B CB  
10665 C CG  . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B CG  
10666 C CD1 . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B CD1 
10667 C CD2 . LEU D 272 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 272 LEU B CD2 
10668 N N   . GLY D 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY B N   
10669 C CA  . GLY D 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY B CA  
10670 C C   . GLY D 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY B C   
10671 O O   . GLY D 273 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 273 GLY B O   
10672 N N   . CYS D 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS B N   
10673 C CA  . CYS D 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS B CA  
10674 C C   . CYS D 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS B C   
10675 O O   . CYS D 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS B O   
10676 C CB  . CYS D 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS B CB  
10677 S SG  . CYS D 274 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 274 CYS B SG  
10678 N N   . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B N   
10679 C CA  . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CA  
10680 C C   . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B C   
10681 O O   . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B O   
10682 C CB  . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CB  
10683 C CG  . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CG  
10684 C CD1 . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CD1 
10685 C CD2 . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CD2 
10686 C CE1 . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CE1 
10687 C CE2 . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CE2 
10688 C CZ  . PHE D 275 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 275 PHE B CZ  
10689 N N   . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B N   
10690 C CA  . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B CA  
10691 C C   . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B C   
10692 O O   . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B O   
10693 C CB  . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B CB  
10694 C CG  . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B CG  
10695 O OD1 . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B OD1 
10696 N ND2 . ASN D 276 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 276 ASN B ND2 
10697 N N   . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B N   
10698 C CA  . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B CA  
10699 C C   . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B C   
10700 O O   . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B O   
10701 C CB  . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B CB  
10702 C CG  . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B CG  
10703 C CD1 . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B CD1 
10704 C CD2 . LEU D 277 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 277 LEU B CD2 
10705 N N   . THR D 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR B N   
10706 C CA  . THR D 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR B CA  
10707 C C   . THR D 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR B C   
10708 O O   . THR D 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR B O   
10709 C CB  . THR D 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR B CB  
10710 O OG1 . THR D 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR B OG1 
10711 C CG2 . THR D 278 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 278 THR B CG2 
10712 N N   . VAL D 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL B N   
10713 C CA  . VAL D 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL B CA  
10714 C C   . VAL D 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL B C   
10715 O O   . VAL D 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL B O   
10716 C CB  . VAL D 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL B CB  
10717 C CG1 . VAL D 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL B CG1 
10718 C CG2 . VAL D 279 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 279 VAL B CG2 
10719 N N   . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B N   
10720 C CA  . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B CA  
10721 C C   . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B C   
10722 O O   . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B O   
10723 C CB  . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B CB  
10724 C CG  . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B CG  
10725 C CD  . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B CD  
10726 C CE  . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B CE  
10727 N NZ  . LYS D 280 ? 1.5556 1.5556 1.5556 0.0000 0.0000 0.0000 280 LYS B NZ  
10728 N N   . GLY D 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY B N   
10729 C CA  . GLY D 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY B CA  
10730 C C   . GLY D 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY B C   
10731 O O   . GLY D 281 ? 1.4757 1.4757 1.4757 0.0000 0.0000 0.0000 281 GLY B O   
10732 N N   . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B N   
10733 C CA  . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B CA  
10734 C C   . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B C   
10735 O O   . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B O   
10736 C CB  . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B CB  
10737 C CG  . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B CG  
10738 N ND1 . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B ND1 
10739 C CD2 . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B CD2 
10740 C CE1 . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B CE1 
10741 N NE2 . HIS D 282 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 282 HIS B NE2 
10742 N N   . ALA D 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA B N   
10743 C CA  . ALA D 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA B CA  
10744 C C   . ALA D 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA B C   
10745 O O   . ALA D 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA B O   
10746 C CB  . ALA D 283 ? 1.5129 1.5129 1.5129 0.0000 0.0000 0.0000 283 ALA B CB  
10747 N N   . LYS D 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS B N   
10748 C CA  . LYS D 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS B CA  
10749 C C   . LYS D 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS B C   
10750 O O   . LYS D 284 ? 1.6016 1.6016 1.6016 0.0000 0.0000 0.0000 284 LYS B O   
10756 N N   . CYS D 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS B N   
10757 C CA  . CYS D 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS B CA  
10758 C C   . CYS D 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS B C   
10759 O O   . CYS D 285 ? 1.5166 1.5166 1.5166 0.0000 0.0000 0.0000 285 CYS B O   
10762 N N   . VAL D 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL B N   
10763 C CA  . VAL D 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL B CA  
10764 C C   . VAL D 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL B C   
10765 O O   . VAL D 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL B O   
10766 C CB  . VAL D 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL B CB  
10767 C CG1 . VAL D 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL B CG1 
10768 C CG2 . VAL D 286 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 286 VAL B CG2 
10769 N N   . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B N   
10770 C CA  . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B CA  
10771 C C   . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B C   
10772 O O   . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B O   
10773 C CB  . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B CB  
10774 C CG  . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B CG  
10775 C CD  . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B CD  
10776 O OE1 . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B OE1 
10777 O OE2 . GLU D 287 ? 1.4731 1.4731 1.4731 0.0000 0.0000 0.0000 287 GLU B OE2 
10778 N N   . VAL D 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL B N   
10779 C CA  . VAL D 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL B CA  
10780 C C   . VAL D 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL B C   
10781 O O   . VAL D 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL B O   
10782 C CB  . VAL D 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL B CB  
10783 C CG1 . VAL D 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL B CG1 
10784 C CG2 . VAL D 288 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 288 VAL B CG2 
10785 N N   . VAL D 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL B N   
10786 C CA  . VAL D 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL B CA  
10787 C C   . VAL D 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL B C   
10788 O O   . VAL D 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL B O   
10789 C CB  . VAL D 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL B CB  
10790 C CG1 . VAL D 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL B CG1 
10791 C CG2 . VAL D 289 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 289 VAL B CG2 
10792 N N   . LYS D 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS B N   
10793 C CA  . LYS D 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS B CA  
10794 C C   . LYS D 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS B C   
10795 O O   . LYS D 290 ? 1.4649 1.4649 1.4649 0.0000 0.0000 0.0000 290 LYS B O   
10801 N N   . THR D 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR B N   
10802 C CA  . THR D 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR B CA  
10803 C C   . THR D 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR B C   
10804 O O   . THR D 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR B O   
10805 C CB  . THR D 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR B CB  
10806 O OG1 . THR D 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR B OG1 
10807 C CG2 . THR D 291 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 291 THR B CG2 
10808 N N   . PHE D 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE B N   
10809 C CA  . PHE D 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE B CA  
10810 C C   . PHE D 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE B C   
10811 O O   . PHE D 292 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 292 PHE B O   
10819 N N   . ASN D 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN B N   
10820 C CA  . ASN D 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN B CA  
10821 C C   . ASN D 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN B C   
10822 O O   . ASN D 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN B O   
10823 C CB  . ASN D 293 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 293 ASN B CB  
10824 N N   . LEU D 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU B N   
10825 C CA  . LEU D 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU B CA  
10826 C C   . LEU D 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU B C   
10827 O O   . LEU D 294 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 294 LEU B O   
10832 N N   . PRO D 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO B N   
10833 C CA  . PRO D 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO B CA  
10834 C C   . PRO D 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO B C   
10835 O O   . PRO D 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO B O   
10836 C CB  . PRO D 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO B CB  
10837 C CG  . PRO D 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO B CG  
10838 C CD  . PRO D 295 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 295 PRO B CD  
10839 N N   . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B N   
10840 C CA  . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B CA  
10841 C C   . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B C   
10842 O O   . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B O   
10843 C CB  . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B CB  
10844 C CG  . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B CG  
10845 C CD1 . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B CD1 
10846 C CD2 . LEU D 296 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 296 LEU B CD2 
10847 N N   . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B N   
10848 C CA  . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B CA  
10849 C C   . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B C   
10850 O O   . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B O   
10851 C CB  . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B CB  
10852 C CG  . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B CG  
10853 C CD1 . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B CD1 
10854 C CD2 . LEU D 297 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 297 LEU B CD2 
10855 N N   . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B N   
10856 C CA  . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B CA  
10857 C C   . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B C   
10858 O O   . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B O   
10859 C CB  . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B CB  
10860 C CG  . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B CG  
10861 S SD  . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B SD  
10862 C CE  . MET D 298 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 298 MET B CE  
10863 N N   . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B N   
10864 C CA  . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B CA  
10865 C C   . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B C   
10866 O O   . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B O   
10867 C CB  . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B CB  
10868 C CG  . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B CG  
10869 C CD1 . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B CD1 
10870 C CD2 . LEU D 299 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 299 LEU B CD2 
10871 N N   . GLY D 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY B N   
10872 C CA  . GLY D 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY B CA  
10873 C C   . GLY D 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY B C   
10874 O O   . GLY D 300 ? 1.5345 1.5345 1.5345 0.0000 0.0000 0.0000 300 GLY B O   
10875 N N   . GLY D 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY B N   
10876 C CA  . GLY D 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY B CA  
10877 C C   . GLY D 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY B C   
10878 O O   . GLY D 301 ? 1.4629 1.4629 1.4629 0.0000 0.0000 0.0000 301 GLY B O   
10879 N N   . GLY D 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY B N   
10880 C CA  . GLY D 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY B CA  
10881 C C   . GLY D 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY B C   
10882 O O   . GLY D 302 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 302 GLY B O   
10883 N N   . GLY D 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY B N   
10884 C CA  . GLY D 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY B CA  
10885 C C   . GLY D 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY B C   
10886 O O   . GLY D 303 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 303 GLY B O   
10887 N N   . TYR D 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR B N   
10888 C CA  . TYR D 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR B CA  
10889 C C   . TYR D 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR B C   
10890 O O   . TYR D 304 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 304 TYR B O   
10899 N N   . THR D 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR B N   
10900 C CA  . THR D 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR B CA  
10901 C C   . THR D 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR B C   
10902 O O   . THR D 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR B O   
10903 C CB  . THR D 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR B CB  
10904 O OG1 . THR D 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR B OG1 
10905 C CG2 . THR D 305 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 305 THR B CG2 
10906 N N   . ILE D 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE B N   
10907 C CA  . ILE D 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE B CA  
10908 C C   . ILE D 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE B C   
10909 O O   . ILE D 306 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 306 ILE B O   
10914 N N   . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B N   
10915 C CA  . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B CA  
10916 C C   . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B C   
10917 O O   . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B O   
10918 C CB  . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B CB  
10919 C CG  . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B CG  
10920 C CD  . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B CD  
10921 N NE  . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B NE  
10922 C CZ  . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B CZ  
10923 N NH1 . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B NH1 
10924 N NH2 . ARG D 307 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 307 ARG B NH2 
10925 N N   . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B N   
10926 C CA  . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B CA  
10927 C C   . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B C   
10928 O O   . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B O   
10929 C CB  . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B CB  
10930 C CG  . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B CG  
10931 O OD1 . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B OD1 
10932 N ND2 . ASN D 308 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 308 ASN B ND2 
10933 N N   . VAL D 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL B N   
10934 C CA  . VAL D 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL B CA  
10935 C C   . VAL D 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL B C   
10936 O O   . VAL D 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL B O   
10937 C CB  . VAL D 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL B CB  
10938 C CG1 . VAL D 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL B CG1 
10939 C CG2 . VAL D 309 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 309 VAL B CG2 
10940 N N   . ALA D 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA B N   
10941 C CA  . ALA D 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA B CA  
10942 C C   . ALA D 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA B C   
10943 O O   . ALA D 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA B O   
10944 C CB  . ALA D 310 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 310 ALA B CB  
10945 N N   . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B N   
10946 C CA  . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B CA  
10947 C C   . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B C   
10948 O O   . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B O   
10949 C CB  . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B CB  
10950 C CG  . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B CG  
10951 C CD  . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B CD  
10952 N NE  . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B NE  
10953 C CZ  . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B CZ  
10954 N NH1 . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B NH1 
10955 N NH2 . ARG D 311 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 311 ARG B NH2 
10956 N N   . CYS D 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS B N   
10957 C CA  . CYS D 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS B CA  
10958 C C   . CYS D 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS B C   
10959 O O   . CYS D 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS B O   
10960 C CB  . CYS D 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS B CB  
10961 S SG  . CYS D 312 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 312 CYS B SG  
10962 N N   . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B N   
10963 C CA  . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CA  
10964 C C   . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B C   
10965 O O   . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B O   
10966 C CB  . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CB  
10967 C CG  . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CG  
10968 C CD1 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CD1 
10969 C CD2 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CD2 
10970 N NE1 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B NE1 
10971 C CE2 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CE2 
10972 C CE3 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CE3 
10973 C CZ2 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CZ2 
10974 C CZ3 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CZ3 
10975 C CH2 . TRP D 313 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 313 TRP B CH2 
10976 N N   . THR D 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR B N   
10977 C CA  . THR D 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR B CA  
10978 C C   . THR D 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR B C   
10979 O O   . THR D 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR B O   
10980 C CB  . THR D 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR B CB  
10981 O OG1 . THR D 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR B OG1 
10982 C CG2 . THR D 314 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 314 THR B CG2 
10983 N N   . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B N   
10984 C CA  . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CA  
10985 C C   . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B C   
10986 O O   . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B O   
10987 C CB  . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CB  
10988 C CG  . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CG  
10989 C CD1 . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CD1 
10990 C CD2 . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CD2 
10991 C CE1 . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CE1 
10992 C CE2 . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CE2 
10993 C CZ  . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B CZ  
10994 O OH  . TYR D 315 ? 1.4487 1.4487 1.4487 0.0000 0.0000 0.0000 315 TYR B OH  
10995 N N   . GLU D 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU B N   
10996 C CA  . GLU D 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU B CA  
10997 C C   . GLU D 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU B C   
10998 O O   . GLU D 316 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 316 GLU B O   
11004 N N   . THR D 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR B N   
11005 C CA  . THR D 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR B CA  
11006 C C   . THR D 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR B C   
11007 O O   . THR D 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR B O   
11008 C CB  . THR D 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR B CB  
11009 O OG1 . THR D 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR B OG1 
11010 C CG2 . THR D 317 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 317 THR B CG2 
11011 N N   . ALA D 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA B N   
11012 C CA  . ALA D 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA B CA  
11013 C C   . ALA D 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA B C   
11014 O O   . ALA D 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA B O   
11015 C CB  . ALA D 318 ? 1.5648 1.5648 1.5648 0.0000 0.0000 0.0000 318 ALA B CB  
11016 N N   . VAL D 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL B N   
11017 C CA  . VAL D 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL B CA  
11018 C C   . VAL D 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL B C   
11019 O O   . VAL D 319 ? 1.4868 1.4868 1.4868 0.0000 0.0000 0.0000 319 VAL B O   
11023 N N   . ALA D 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA B N   
11024 C CA  . ALA D 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA B CA  
11025 C C   . ALA D 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA B C   
11026 O O   . ALA D 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA B O   
11027 C CB  . ALA D 320 ? 1.6037 1.6037 1.6037 0.0000 0.0000 0.0000 320 ALA B CB  
11028 N N   . LEU D 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU B N   
11029 C CA  . LEU D 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU B CA  
11030 C C   . LEU D 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU B C   
11031 O O   . LEU D 321 ? 1.7510 1.7510 1.7510 0.0000 0.0000 0.0000 321 LEU B O   
11041 N N   . CYS D 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS B N   
11042 C CA  . CYS D 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS B CA  
11043 C C   . CYS D 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS B C   
11044 O O   . CYS D 323 ? 1.7640 1.7640 1.7640 0.0000 0.0000 0.0000 323 CYS B O   
11047 N N   . GLU D 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU B N   
11048 C CA  . GLU D 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU B CA  
11049 C C   . GLU D 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU B C   
11050 O O   . GLU D 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU B O   
11051 C CB  . GLU D 324 ? 1.7693 1.7693 1.7693 0.0000 0.0000 0.0000 324 GLU B CB  
11052 N N   . ILE D 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE B N   
11053 C CA  . ILE D 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE B CA  
11054 C C   . ILE D 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE B C   
11055 O O   . ILE D 325 ? 1.6865 1.6865 1.6865 0.0000 0.0000 0.0000 325 ILE B O   
11060 N N   . PRO D 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO B N   
11061 C CA  . PRO D 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO B CA  
11062 C C   . PRO D 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO B C   
11063 O O   . PRO D 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO B O   
11064 C CB  . PRO D 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO B CB  
11065 C CG  . PRO D 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO B CG  
11066 C CD  . PRO D 326 ? 1.7096 1.7096 1.7096 0.0000 0.0000 0.0000 326 PRO B CD  
11067 N N   . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B N   
11068 C CA  . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B CA  
11069 C C   . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B C   
11070 O O   . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B O   
11071 C CB  . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B CB  
11072 C CG  . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B CG  
11073 O OD1 . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B OD1 
11074 N ND2 . ASN D 327 ? 1.7034 1.7034 1.7034 0.0000 0.0000 0.0000 327 ASN B ND2 
11092 N N   . PRO D 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO B N   
11093 C CA  . PRO D 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO B CA  
11094 C C   . PRO D 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO B C   
11095 O O   . PRO D 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO B O   
11096 C CB  . PRO D 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO B CB  
11097 C CG  . PRO D 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO B CG  
11098 C CD  . PRO D 330 ? 1.9337 1.9337 1.9337 0.0000 0.0000 0.0000 330 PRO B CD  
11111 N N   . ASN D 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN B N   
11112 C CA  . ASN D 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN B CA  
11113 C C   . ASN D 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN B C   
11114 O O   . ASN D 332 ? 2.0459 2.0459 2.0459 0.0000 0.0000 0.0000 332 ASN B O   
11119 N N   . ASP D 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP B N   
11120 C CA  . ASP D 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP B CA  
11121 C C   . ASP D 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP B C   
11122 O O   . ASP D 333 ? 1.9465 1.9465 1.9465 0.0000 0.0000 0.0000 333 ASP B O   
11127 N N   . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B N   
11128 C CA  . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CA  
11129 C C   . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B C   
11130 O O   . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B O   
11131 C CB  . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CB  
11132 C CG  . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CG  
11133 C CD1 . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CD1 
11134 C CD2 . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CD2 
11135 C CE1 . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CE1 
11136 C CE2 . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CE2 
11137 C CZ  . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B CZ  
11138 O OH  . TYR D 334 ? 1.8168 1.8168 1.8168 0.0000 0.0000 0.0000 334 TYR B OH  
11139 N N   . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B N   
11140 C CA  . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CA  
11141 C C   . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B C   
11142 O O   . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B O   
11143 C CB  . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CB  
11144 C CG  . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CG  
11145 C CD1 . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CD1 
11146 C CD2 . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CD2 
11147 C CE1 . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CE1 
11148 C CE2 . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CE2 
11149 C CZ  . PHE D 335 ? 1.8830 1.8830 1.8830 0.0000 0.0000 0.0000 335 PHE B CZ  
11150 N N   . GLU D 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU B N   
11151 C CA  . GLU D 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU B CA  
11152 C C   . GLU D 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU B C   
11153 O O   . GLU D 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU B O   
11154 C CB  . GLU D 336 ? 2.0148 2.0148 2.0148 0.0000 0.0000 0.0000 336 GLU B CB  
11155 N N   . TYR D 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR B N   
11156 C CA  . TYR D 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR B CA  
11157 C C   . TYR D 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR B C   
11158 O O   . TYR D 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR B O   
11159 C CB  . TYR D 337 ? 1.9220 1.9220 1.9220 0.0000 0.0000 0.0000 337 TYR B CB  
11160 N N   . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B N   
11161 C CA  . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CA  
11162 C C   . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B C   
11163 O O   . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B O   
11164 C CB  . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CB  
11165 C CG  . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CG  
11166 C CD1 . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CD1 
11167 C CD2 . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CD2 
11168 C CE1 . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CE1 
11169 C CE2 . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CE2 
11170 C CZ  . PHE D 338 ? 1.7757 1.7757 1.7757 0.0000 0.0000 0.0000 338 PHE B CZ  
11175 N N   . PRO D 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO B N   
11176 C CA  . PRO D 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO B CA  
11177 C C   . PRO D 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO B C   
11178 O O   . PRO D 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO B O   
11179 C CB  . PRO D 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO B CB  
11180 C CG  . PRO D 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO B CG  
11181 C CD  . PRO D 340 ? 2.1025 2.1025 2.1025 0.0000 0.0000 0.0000 340 PRO B CD  
11182 N N   . ASP D 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP B N   
11183 C CA  . ASP D 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP B CA  
11184 C C   . ASP D 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP B C   
11185 O O   . ASP D 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP B O   
11186 C CB  . ASP D 341 ? 2.0232 2.0232 2.0232 0.0000 0.0000 0.0000 341 ASP B CB  
11187 N N   . PHE D 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE B N   
11188 C CA  . PHE D 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE B CA  
11189 C C   . PHE D 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE B C   
11190 O O   . PHE D 342 ? 1.7881 1.7881 1.7881 0.0000 0.0000 0.0000 342 PHE B O   
11192 N N   . LYS D 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS B N   
11193 C CA  . LYS D 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS B CA  
11194 C C   . LYS D 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS B C   
11195 O O   . LYS D 343 ? 1.7789 1.7789 1.7789 0.0000 0.0000 0.0000 343 LYS B O   
11197 N N   . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B N   
11198 C CA  . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B CA  
11199 C C   . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B C   
11200 O O   . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B O   
11201 C CB  . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B CB  
11202 C CG  . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B CG  
11203 C CD1 . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B CD1 
11204 C CD2 . LEU D 344 ? 1.6065 1.6065 1.6065 0.0000 0.0000 0.0000 344 LEU B CD2 
11205 N N   . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B N   
11206 C CA  . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B CA  
11207 C C   . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B C   
11208 O O   . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B O   
11209 C CB  . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B CB  
11210 C CG  . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B CG  
11211 N ND1 . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B ND1 
11212 C CD2 . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B CD2 
11213 C CE1 . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B CE1 
11214 N NE2 . HIS D 345 ? 1.5280 1.5280 1.5280 0.0000 0.0000 0.0000 345 HIS B NE2 
11215 N N   . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B N   
11216 C CA  . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B CA  
11217 C C   . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B C   
11218 O O   . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B O   
11219 C CB  . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B CB  
11220 C CG1 . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B CG1 
11221 C CG2 . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B CG2 
11222 C CD1 . ILE D 346 ? 1.5053 1.5053 1.5053 0.0000 0.0000 0.0000 346 ILE B CD1 
11223 N N   . SER D 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER B N   
11224 C CA  . SER D 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER B CA  
11225 C C   . SER D 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER B C   
11226 O O   . SER D 347 ? 1.5593 1.5593 1.5593 0.0000 0.0000 0.0000 347 SER B O   
11229 N N   . PRO D 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO B N   
11230 C CA  . PRO D 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO B CA  
11231 C C   . PRO D 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO B C   
11232 O O   . PRO D 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO B O   
11233 C CB  . PRO D 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO B CB  
11234 C CG  . PRO D 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO B CG  
11235 C CD  . PRO D 348 ? 1.6571 1.6571 1.6571 0.0000 0.0000 0.0000 348 PRO B CD  
11236 N N   . SER D 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER B N   
11237 C CA  . SER D 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER B CA  
11238 C C   . SER D 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER B C   
11239 O O   . SER D 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER B O   
11240 C CB  . SER D 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER B CB  
11241 O OG  . SER D 349 ? 1.4885 1.4885 1.4885 0.0000 0.0000 0.0000 349 SER B OG  
11242 N N   . ASN D 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN B N   
11243 C CA  . ASN D 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN B CA  
11244 C C   . ASN D 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN B C   
11245 O O   . ASN D 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN B O   
11246 C CB  . ASN D 350 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 350 ASN B CB  
11247 N N   . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B N   
11248 C CA  . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B CA  
11249 C C   . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B C   
11250 O O   . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B O   
11251 C CB  . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B CB  
11252 C CG  . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B CG  
11253 S SD  . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B SD  
11254 C CE  . MET D 351 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 351 MET B CE  
11255 N N   . THR D 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR B N   
11256 C CA  . THR D 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR B CA  
11257 C C   . THR D 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR B C   
11258 O O   . THR D 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR B O   
11259 C CB  . THR D 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR B CB  
11260 O OG1 . THR D 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR B OG1 
11261 C CG2 . THR D 352 ? 1.5194 1.5194 1.5194 0.0000 0.0000 0.0000 352 THR B CG2 
11262 N N   . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B N   
11263 C CA  . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B CA  
11264 C C   . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B C   
11265 O O   . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B O   
11266 C CB  . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B CB  
11267 C CG  . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B CG  
11268 O OD1 . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B OD1 
11269 N ND2 . ASN D 353 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 353 ASN B ND2 
11270 N N   . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B N   
11271 C CA  . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B CA  
11272 C C   . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B C   
11273 O O   . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B O   
11274 C CB  . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B CB  
11275 C CG  . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B CG  
11276 C CD  . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B CD  
11277 O OE1 . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B OE1 
11278 N NE2 . GLN D 354 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 354 GLN B NE2 
11279 N N   . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B N   
11280 C CA  . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B CA  
11281 C C   . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B C   
11282 O O   . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B O   
11283 C CB  . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B CB  
11284 C CG  . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B CG  
11285 O OD1 . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B OD1 
11286 N ND2 . ASN D 355 ? 1.4431 1.4431 1.4431 0.0000 0.0000 0.0000 355 ASN B ND2 
11287 N N   . THR D 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR B N   
11288 C CA  . THR D 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR B CA  
11289 C C   . THR D 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR B C   
11290 O O   . THR D 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR B O   
11291 C CB  . THR D 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR B CB  
11292 O OG1 . THR D 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR B OG1 
11293 C CG2 . THR D 356 ? 1.4814 1.4814 1.4814 0.0000 0.0000 0.0000 356 THR B CG2 
11294 N N   . PRO D 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO B N   
11295 C CA  . PRO D 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO B CA  
11296 C C   . PRO D 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO B C   
11297 O O   . PRO D 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO B O   
11298 C CB  . PRO D 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO B CB  
11299 C CG  . PRO D 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO B CG  
11300 C CD  . PRO D 357 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 357 PRO B CD  
11301 N N   . GLU D 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU B N   
11302 C CA  . GLU D 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU B CA  
11303 C C   . GLU D 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU B C   
11304 O O   . GLU D 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU B O   
11305 C CB  . GLU D 358 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 358 GLU B CB  
11306 N N   . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B N   
11307 C CA  . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CA  
11308 C C   . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B C   
11309 O O   . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B O   
11310 C CB  . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CB  
11311 C CG  . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CG  
11312 C CD1 . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CD1 
11313 C CD2 . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CD2 
11314 C CE1 . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CE1 
11315 C CE2 . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CE2 
11316 C CZ  . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B CZ  
11317 O OH  . TYR D 359 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 359 TYR B OH  
11318 N N   . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B N   
11319 C CA  . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B CA  
11320 C C   . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B C   
11321 O O   . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B O   
11322 C CB  . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B CB  
11323 C CG  . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B CG  
11324 S SD  . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B SD  
11325 C CE  . MET D 360 ? 1.4526 1.4526 1.4526 0.0000 0.0000 0.0000 360 MET B CE  
11326 N N   . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B N   
11327 C CA  . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B CA  
11328 C C   . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B C   
11329 O O   . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B O   
11330 C CB  . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B CB  
11331 C CG  . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B CG  
11332 C CD  . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B CD  
11333 O OE1 . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B OE1 
11334 O OE2 . GLU D 361 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 361 GLU B OE2 
11335 N N   . LYS D 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS B N   
11336 C CA  . LYS D 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS B CA  
11337 C C   . LYS D 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS B C   
11338 O O   . LYS D 362 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 362 LYS B O   
11344 N N   . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B N   
11345 C CA  . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B CA  
11346 C C   . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B C   
11347 O O   . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B O   
11348 C CB  . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B CB  
11349 C CG1 . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B CG1 
11350 C CG2 . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B CG2 
11351 C CD1 . ILE D 363 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 363 ILE B CD1 
11352 N N   . LYS D 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS B N   
11353 C CA  . LYS D 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS B CA  
11354 C C   . LYS D 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS B C   
11355 O O   . LYS D 364 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 364 LYS B O   
11361 N N   . GLN D 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN B N   
11362 C CA  . GLN D 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN B CA  
11363 C C   . GLN D 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN B C   
11364 O O   . GLN D 365 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 365 GLN B O   
11370 N N   . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B N   
11371 C CA  . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B CA  
11372 C C   . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B C   
11373 O O   . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B O   
11374 C CB  . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B CB  
11375 C CG  . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B CG  
11376 C CD  . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B CD  
11377 N NE  . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B NE  
11378 C CZ  . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B CZ  
11379 N NH1 . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B NH1 
11380 N NH2 . ARG D 366 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 366 ARG B NH2 
11381 N N   . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B N   
11382 C CA  . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B CA  
11383 C C   . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B C   
11384 O O   . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B O   
11385 C CB  . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B CB  
11386 C CG  . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B CG  
11387 C CD1 . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B CD1 
11388 C CD2 . LEU D 367 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 367 LEU B CD2 
11389 N N   . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B N   
11390 C CA  . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CA  
11391 C C   . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B C   
11392 O O   . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B O   
11393 C CB  . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CB  
11394 C CG  . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CG  
11395 C CD1 . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CD1 
11396 C CD2 . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CD2 
11397 C CE1 . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CE1 
11398 C CE2 . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CE2 
11399 C CZ  . PHE D 368 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 368 PHE B CZ  
11400 N N   . GLU D 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU B N   
11401 C CA  . GLU D 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU B CA  
11402 C C   . GLU D 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU B C   
11403 O O   . GLU D 369 ? 1.4428 1.4428 1.4428 0.0000 0.0000 0.0000 369 GLU B O   
11409 N N   . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B N   
11410 C CA  . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B CA  
11411 C C   . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B C   
11412 O O   . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B O   
11413 C CB  . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B CB  
11414 C CG  . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B CG  
11415 O OD1 . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B OD1 
11416 N ND2 . ASN D 370 ? 1.4467 1.4467 1.4467 0.0000 0.0000 0.0000 370 ASN B ND2 
11417 N N   . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B N   
11418 C CA  . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B CA  
11419 C C   . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B C   
11420 O O   . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B O   
11421 C CB  . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B CB  
11422 C CG  . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B CG  
11423 C CD1 . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B CD1 
11424 C CD2 . LEU D 371 ? 1.4651 1.4651 1.4651 0.0000 0.0000 0.0000 371 LEU B CD2 
11425 N N   . ARG D 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG B N   
11426 C CA  . ARG D 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG B CA  
11427 C C   . ARG D 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG B C   
11428 O O   . ARG D 372 ? 1.5842 1.5842 1.5842 0.0000 0.0000 0.0000 372 ARG B O   
11436 N N   . MET D 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET B N   
11437 C CA  . MET D 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET B CA  
11438 C C   . MET D 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET B C   
11439 O O   . MET D 373 ? 1.5554 1.5554 1.5554 0.0000 0.0000 0.0000 373 MET B O   
11444 N N   . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B N   
11445 C CA  . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B CA  
11446 C C   . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B C   
11447 O O   . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B O   
11448 C CB  . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B CB  
11449 C CG  . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B CG  
11450 C CD1 . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B CD1 
11451 C CD2 . LEU D 374 ? 1.4841 1.4841 1.4841 0.0000 0.0000 0.0000 374 LEU B CD2 
11452 N N   . PRO D 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO B N   
11453 C CA  . PRO D 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO B CA  
11454 C C   . PRO D 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO B C   
11455 O O   . PRO D 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO B O   
11456 C CB  . PRO D 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO B CB  
11457 C CG  . PRO D 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO B CG  
11458 C CD  . PRO D 375 ? 1.6255 1.6255 1.6255 0.0000 0.0000 0.0000 375 PRO B CD  
# 
