data_9D69
# 
_entry.id   9D69 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9D69         pdb_00009d69 10.2210/pdb9d69/pdb 
WWPDB D_1000287364 ?            ?                   
EMDB  EMD-46590    ?            ?                   
# 
_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       2025-01-22 
# 
_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                        9D69 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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        'EAAT3 monomer with L-Cys bound at iOFS' 
_pdbx_database_related.db_id          EMD-46590 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              olb2003@med.cornell.edu 
_pdbx_contact_author.name_first         Olga 
_pdbx_contact_author.name_last          Boudker 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6965-0851 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Qiu, B.'     1 0000-0003-3633-5091 
'Boudker, O.' 2 0000-0001-6965-0851 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural basis of the excitatory amino acid transporter 3 substrate recognition.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.09.05.611541 
_citation.pdbx_database_id_PubMed   39282329 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Qiu, B.'     1 0000-0003-3633-5091 
primary 'Boudker, O.' 2 ?                   
# 
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 'Excitatory amino acid transporter 3' 57120.863 1 ? ? ? ? 
2 non-polymer syn CYSTEINE                              121.158   1 ? ? ? ? 
3 non-polymer syn 'SODIUM ION'                          22.990    3 ? ? ? ? 
4 non-polymer syn 'MERCURY (II) ION'                    200.590   1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Excitatory amino-acid carrier 1,Neuronal and epithelial glutamate transporter,Sodium-dependent glutamate/aspartate transporter 3,Solute carrier family 1 member 1
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPMGKPARKGAEWKRFLKNNWVLLSTVAAVVLGITTGVLVREHSNLSTLEKFYFAFPGEILMRMLKLIILPLIISSMITG
VAALDSNVSGKIGLRAVVYYFATTLIAVILGIVLVVSIKPGVTQKVGEIARTGSTPEVSTVDAMLDLIRNMFPENLVQAA
FQQYKTKREEVKPPSDPEMTMTEESFTAVMTTAISKTKTKEYKIVGMYSDGINVLGLIVFALVFGLVIGKMGEKGQILVD
FFNALSDATMKIVQIIMWYMPLGILFLIAGCIIEVEDWEIFRKLGLYMATVLTGLAIHSIVILPLIYFIVVRKNPFRFAM
GMAQALLTALMISSSSATLPVTFRCAEENNQVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNDLDLGIGQIITIS
ITATSASIGAAGVPQAGLVTMVIVLSAVGLPAEDVTLIIAVDCLLDRFRTMVNVLGDAFGTGIVEKLSKKELEQMDVSSE
VNIVNPFALESTILDNEDSDTKKSYVNGGFAVDKSDTISFTQTSQF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPMGKPARKGAEWKRFLKNNWVLLSTVAAVVLGITTGVLVREHSNLSTLEKFYFAFPGEILMRMLKLIILPLIISSMITG
VAALDSNVSGKIGLRAVVYYFATTLIAVILGIVLVVSIKPGVTQKVGEIARTGSTPEVSTVDAMLDLIRNMFPENLVQAA
FQQYKTKREEVKPPSDPEMTMTEESFTAVMTTAISKTKTKEYKIVGMYSDGINVLGLIVFALVFGLVIGKMGEKGQILVD
FFNALSDATMKIVQIIMWYMPLGILFLIAGCIIEVEDWEIFRKLGLYMATVLTGLAIHSIVILPLIYFIVVRKNPFRFAM
GMAQALLTALMISSSSATLPVTFRCAEENNQVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNDLDLGIGQIITIS
ITATSASIGAAGVPQAGLVTMVIVLSAVGLPAEDVTLIIAVDCLLDRFRTMVNVLGDAFGTGIVEKLSKKELEQMDVSSE
VNIVNPFALESTILDNEDSDTKKSYVNGGFAVDKSDTISFTQTSQF
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 CYSTEINE           CYS 
3 'SODIUM ION'       NA  
4 'MERCURY (II) ION' HG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   MET n 
1 4   GLY n 
1 5   LYS n 
1 6   PRO n 
1 7   ALA n 
1 8   ARG n 
1 9   LYS n 
1 10  GLY n 
1 11  ALA n 
1 12  GLU n 
1 13  TRP n 
1 14  LYS n 
1 15  ARG n 
1 16  PHE n 
1 17  LEU n 
1 18  LYS n 
1 19  ASN n 
1 20  ASN n 
1 21  TRP n 
1 22  VAL n 
1 23  LEU n 
1 24  LEU n 
1 25  SER n 
1 26  THR n 
1 27  VAL n 
1 28  ALA n 
1 29  ALA n 
1 30  VAL n 
1 31  VAL n 
1 32  LEU n 
1 33  GLY n 
1 34  ILE n 
1 35  THR n 
1 36  THR n 
1 37  GLY n 
1 38  VAL n 
1 39  LEU n 
1 40  VAL n 
1 41  ARG n 
1 42  GLU n 
1 43  HIS n 
1 44  SER n 
1 45  ASN n 
1 46  LEU n 
1 47  SER n 
1 48  THR n 
1 49  LEU n 
1 50  GLU n 
1 51  LYS n 
1 52  PHE n 
1 53  TYR n 
1 54  PHE n 
1 55  ALA n 
1 56  PHE n 
1 57  PRO n 
1 58  GLY n 
1 59  GLU n 
1 60  ILE n 
1 61  LEU n 
1 62  MET n 
1 63  ARG n 
1 64  MET n 
1 65  LEU n 
1 66  LYS n 
1 67  LEU n 
1 68  ILE n 
1 69  ILE n 
1 70  LEU n 
1 71  PRO n 
1 72  LEU n 
1 73  ILE n 
1 74  ILE n 
1 75  SER n 
1 76  SER n 
1 77  MET n 
1 78  ILE n 
1 79  THR n 
1 80  GLY n 
1 81  VAL n 
1 82  ALA n 
1 83  ALA n 
1 84  LEU n 
1 85  ASP n 
1 86  SER n 
1 87  ASN n 
1 88  VAL n 
1 89  SER n 
1 90  GLY n 
1 91  LYS n 
1 92  ILE n 
1 93  GLY n 
1 94  LEU n 
1 95  ARG n 
1 96  ALA n 
1 97  VAL n 
1 98  VAL n 
1 99  TYR n 
1 100 TYR n 
1 101 PHE n 
1 102 ALA n 
1 103 THR n 
1 104 THR n 
1 105 LEU n 
1 106 ILE n 
1 107 ALA n 
1 108 VAL n 
1 109 ILE n 
1 110 LEU n 
1 111 GLY n 
1 112 ILE n 
1 113 VAL n 
1 114 LEU n 
1 115 VAL n 
1 116 VAL n 
1 117 SER n 
1 118 ILE n 
1 119 LYS n 
1 120 PRO n 
1 121 GLY n 
1 122 VAL n 
1 123 THR n 
1 124 GLN n 
1 125 LYS n 
1 126 VAL n 
1 127 GLY n 
1 128 GLU n 
1 129 ILE n 
1 130 ALA n 
1 131 ARG n 
1 132 THR n 
1 133 GLY n 
1 134 SER n 
1 135 THR n 
1 136 PRO n 
1 137 GLU n 
1 138 VAL n 
1 139 SER n 
1 140 THR n 
1 141 VAL n 
1 142 ASP n 
1 143 ALA n 
1 144 MET n 
1 145 LEU n 
1 146 ASP n 
1 147 LEU n 
1 148 ILE n 
1 149 ARG n 
1 150 ASN n 
1 151 MET n 
1 152 PHE n 
1 153 PRO n 
1 154 GLU n 
1 155 ASN n 
1 156 LEU n 
1 157 VAL n 
1 158 GLN n 
1 159 ALA n 
1 160 ALA n 
1 161 PHE n 
1 162 GLN n 
1 163 GLN n 
1 164 TYR n 
1 165 LYS n 
1 166 THR n 
1 167 LYS n 
1 168 ARG n 
1 169 GLU n 
1 170 GLU n 
1 171 VAL n 
1 172 LYS n 
1 173 PRO n 
1 174 PRO n 
1 175 SER n 
1 176 ASP n 
1 177 PRO n 
1 178 GLU n 
1 179 MET n 
1 180 THR n 
1 181 MET n 
1 182 THR n 
1 183 GLU n 
1 184 GLU n 
1 185 SER n 
1 186 PHE n 
1 187 THR n 
1 188 ALA n 
1 189 VAL n 
1 190 MET n 
1 191 THR n 
1 192 THR n 
1 193 ALA n 
1 194 ILE n 
1 195 SER n 
1 196 LYS n 
1 197 THR n 
1 198 LYS n 
1 199 THR n 
1 200 LYS n 
1 201 GLU n 
1 202 TYR n 
1 203 LYS n 
1 204 ILE n 
1 205 VAL n 
1 206 GLY n 
1 207 MET n 
1 208 TYR n 
1 209 SER n 
1 210 ASP n 
1 211 GLY n 
1 212 ILE n 
1 213 ASN n 
1 214 VAL n 
1 215 LEU n 
1 216 GLY n 
1 217 LEU n 
1 218 ILE n 
1 219 VAL n 
1 220 PHE n 
1 221 ALA n 
1 222 LEU n 
1 223 VAL n 
1 224 PHE n 
1 225 GLY n 
1 226 LEU n 
1 227 VAL n 
1 228 ILE n 
1 229 GLY n 
1 230 LYS n 
1 231 MET n 
1 232 GLY n 
1 233 GLU n 
1 234 LYS n 
1 235 GLY n 
1 236 GLN n 
1 237 ILE n 
1 238 LEU n 
1 239 VAL n 
1 240 ASP n 
1 241 PHE n 
1 242 PHE n 
1 243 ASN n 
1 244 ALA n 
1 245 LEU n 
1 246 SER n 
1 247 ASP n 
1 248 ALA n 
1 249 THR n 
1 250 MET n 
1 251 LYS n 
1 252 ILE n 
1 253 VAL n 
1 254 GLN n 
1 255 ILE n 
1 256 ILE n 
1 257 MET n 
1 258 TRP n 
1 259 TYR n 
1 260 MET n 
1 261 PRO n 
1 262 LEU n 
1 263 GLY n 
1 264 ILE n 
1 265 LEU n 
1 266 PHE n 
1 267 LEU n 
1 268 ILE n 
1 269 ALA n 
1 270 GLY n 
1 271 CYS n 
1 272 ILE n 
1 273 ILE n 
1 274 GLU n 
1 275 VAL n 
1 276 GLU n 
1 277 ASP n 
1 278 TRP n 
1 279 GLU n 
1 280 ILE n 
1 281 PHE n 
1 282 ARG n 
1 283 LYS n 
1 284 LEU n 
1 285 GLY n 
1 286 LEU n 
1 287 TYR n 
1 288 MET n 
1 289 ALA n 
1 290 THR n 
1 291 VAL n 
1 292 LEU n 
1 293 THR n 
1 294 GLY n 
1 295 LEU n 
1 296 ALA n 
1 297 ILE n 
1 298 HIS n 
1 299 SER n 
1 300 ILE n 
1 301 VAL n 
1 302 ILE n 
1 303 LEU n 
1 304 PRO n 
1 305 LEU n 
1 306 ILE n 
1 307 TYR n 
1 308 PHE n 
1 309 ILE n 
1 310 VAL n 
1 311 VAL n 
1 312 ARG n 
1 313 LYS n 
1 314 ASN n 
1 315 PRO n 
1 316 PHE n 
1 317 ARG n 
1 318 PHE n 
1 319 ALA n 
1 320 MET n 
1 321 GLY n 
1 322 MET n 
1 323 ALA n 
1 324 GLN n 
1 325 ALA n 
1 326 LEU n 
1 327 LEU n 
1 328 THR n 
1 329 ALA n 
1 330 LEU n 
1 331 MET n 
1 332 ILE n 
1 333 SER n 
1 334 SER n 
1 335 SER n 
1 336 SER n 
1 337 ALA n 
1 338 THR n 
1 339 LEU n 
1 340 PRO n 
1 341 VAL n 
1 342 THR n 
1 343 PHE n 
1 344 ARG n 
1 345 CYS n 
1 346 ALA n 
1 347 GLU n 
1 348 GLU n 
1 349 ASN n 
1 350 ASN n 
1 351 GLN n 
1 352 VAL n 
1 353 ASP n 
1 354 LYS n 
1 355 ARG n 
1 356 ILE n 
1 357 THR n 
1 358 ARG n 
1 359 PHE n 
1 360 VAL n 
1 361 LEU n 
1 362 PRO n 
1 363 VAL n 
1 364 GLY n 
1 365 ALA n 
1 366 THR n 
1 367 ILE n 
1 368 ASN n 
1 369 MET n 
1 370 ASP n 
1 371 GLY n 
1 372 THR n 
1 373 ALA n 
1 374 LEU n 
1 375 TYR n 
1 376 GLU n 
1 377 ALA n 
1 378 VAL n 
1 379 ALA n 
1 380 ALA n 
1 381 VAL n 
1 382 PHE n 
1 383 ILE n 
1 384 ALA n 
1 385 GLN n 
1 386 LEU n 
1 387 ASN n 
1 388 ASP n 
1 389 LEU n 
1 390 ASP n 
1 391 LEU n 
1 392 GLY n 
1 393 ILE n 
1 394 GLY n 
1 395 GLN n 
1 396 ILE n 
1 397 ILE n 
1 398 THR n 
1 399 ILE n 
1 400 SER n 
1 401 ILE n 
1 402 THR n 
1 403 ALA n 
1 404 THR n 
1 405 SER n 
1 406 ALA n 
1 407 SER n 
1 408 ILE n 
1 409 GLY n 
1 410 ALA n 
1 411 ALA n 
1 412 GLY n 
1 413 VAL n 
1 414 PRO n 
1 415 GLN n 
1 416 ALA n 
1 417 GLY n 
1 418 LEU n 
1 419 VAL n 
1 420 THR n 
1 421 MET n 
1 422 VAL n 
1 423 ILE n 
1 424 VAL n 
1 425 LEU n 
1 426 SER n 
1 427 ALA n 
1 428 VAL n 
1 429 GLY n 
1 430 LEU n 
1 431 PRO n 
1 432 ALA n 
1 433 GLU n 
1 434 ASP n 
1 435 VAL n 
1 436 THR n 
1 437 LEU n 
1 438 ILE n 
1 439 ILE n 
1 440 ALA n 
1 441 VAL n 
1 442 ASP n 
1 443 CYS n 
1 444 LEU n 
1 445 LEU n 
1 446 ASP n 
1 447 ARG n 
1 448 PHE n 
1 449 ARG n 
1 450 THR n 
1 451 MET n 
1 452 VAL n 
1 453 ASN n 
1 454 VAL n 
1 455 LEU n 
1 456 GLY n 
1 457 ASP n 
1 458 ALA n 
1 459 PHE n 
1 460 GLY n 
1 461 THR n 
1 462 GLY n 
1 463 ILE n 
1 464 VAL n 
1 465 GLU n 
1 466 LYS n 
1 467 LEU n 
1 468 SER n 
1 469 LYS n 
1 470 LYS n 
1 471 GLU n 
1 472 LEU n 
1 473 GLU n 
1 474 GLN n 
1 475 MET n 
1 476 ASP n 
1 477 VAL n 
1 478 SER n 
1 479 SER n 
1 480 GLU n 
1 481 VAL n 
1 482 ASN n 
1 483 ILE n 
1 484 VAL n 
1 485 ASN n 
1 486 PRO n 
1 487 PHE n 
1 488 ALA n 
1 489 LEU n 
1 490 GLU n 
1 491 SER n 
1 492 THR n 
1 493 ILE n 
1 494 LEU n 
1 495 ASP n 
1 496 ASN n 
1 497 GLU n 
1 498 ASP n 
1 499 SER n 
1 500 ASP n 
1 501 THR n 
1 502 LYS n 
1 503 LYS n 
1 504 SER n 
1 505 TYR n 
1 506 VAL n 
1 507 ASN n 
1 508 GLY n 
1 509 GLY n 
1 510 PHE n 
1 511 ALA n 
1 512 VAL n 
1 513 ASP n 
1 514 LYS n 
1 515 SER n 
1 516 ASP n 
1 517 THR n 
1 518 ILE n 
1 519 SER n 
1 520 PHE n 
1 521 THR n 
1 522 GLN n 
1 523 THR n 
1 524 SER n 
1 525 GLN n 
1 526 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   526 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SLC1A1, EAAC1, EAAT3' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'    ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE           ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE            ? 'C2 H5 N O2'     75.067  
HG  non-polymer         . 'MERCURY (II) ION' ? 'Hg 2'           200.590 
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 
NA  non-polymer         . 'SODIUM ION'       ? 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE      ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE            ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE             ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE          ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN         ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE           ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE             ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -1  ?   ?   ?   A . n 
A 1 2   PRO 2   0   ?   ?   ?   A . n 
A 1 3   MET 3   1   ?   ?   ?   A . n 
A 1 4   GLY 4   2   ?   ?   ?   A . n 
A 1 5   LYS 5   3   ?   ?   ?   A . n 
A 1 6   PRO 6   4   ?   ?   ?   A . n 
A 1 7   ALA 7   5   ?   ?   ?   A . n 
A 1 8   ARG 8   6   ?   ?   ?   A . n 
A 1 9   LYS 9   7   ?   ?   ?   A . n 
A 1 10  GLY 10  8   ?   ?   ?   A . n 
A 1 11  ALA 11  9   ?   ?   ?   A . n 
A 1 12  GLU 12  10  ?   ?   ?   A . n 
A 1 13  TRP 13  11  ?   ?   ?   A . n 
A 1 14  LYS 14  12  ?   ?   ?   A . n 
A 1 15  ARG 15  13  ?   ?   ?   A . n 
A 1 16  PHE 16  14  ?   ?   ?   A . n 
A 1 17  LEU 17  15  ?   ?   ?   A . n 
A 1 18  LYS 18  16  ?   ?   ?   A . n 
A 1 19  ASN 19  17  17  ASN ASN A . n 
A 1 20  ASN 20  18  18  ASN ASN A . n 
A 1 21  TRP 21  19  19  TRP TRP A . n 
A 1 22  VAL 22  20  20  VAL VAL A . n 
A 1 23  LEU 23  21  21  LEU LEU A . n 
A 1 24  LEU 24  22  22  LEU LEU A . n 
A 1 25  SER 25  23  23  SER SER A . n 
A 1 26  THR 26  24  24  THR THR A . n 
A 1 27  VAL 27  25  25  VAL VAL A . n 
A 1 28  ALA 28  26  26  ALA ALA A . n 
A 1 29  ALA 29  27  27  ALA ALA A . n 
A 1 30  VAL 30  28  28  VAL VAL A . n 
A 1 31  VAL 31  29  29  VAL VAL A . n 
A 1 32  LEU 32  30  30  LEU LEU A . n 
A 1 33  GLY 33  31  31  GLY GLY A . n 
A 1 34  ILE 34  32  32  ILE ILE A . n 
A 1 35  THR 35  33  33  THR THR A . n 
A 1 36  THR 36  34  34  THR THR A . n 
A 1 37  GLY 37  35  35  GLY GLY A . n 
A 1 38  VAL 38  36  36  VAL VAL A . n 
A 1 39  LEU 39  37  37  LEU LEU A . n 
A 1 40  VAL 40  38  38  VAL VAL A . n 
A 1 41  ARG 41  39  39  ARG ARG A . n 
A 1 42  GLU 42  40  40  GLU GLU A . n 
A 1 43  HIS 43  41  41  HIS HIS A . n 
A 1 44  SER 44  42  42  SER SER A . n 
A 1 45  ASN 45  43  43  ASN ASN A . n 
A 1 46  LEU 46  44  44  LEU LEU A . n 
A 1 47  SER 47  45  45  SER SER A . n 
A 1 48  THR 48  46  46  THR THR A . n 
A 1 49  LEU 49  47  47  LEU LEU A . n 
A 1 50  GLU 50  48  48  GLU GLU A . n 
A 1 51  LYS 51  49  49  LYS LYS A . n 
A 1 52  PHE 52  50  50  PHE PHE A . n 
A 1 53  TYR 53  51  51  TYR TYR A . n 
A 1 54  PHE 54  52  52  PHE PHE A . n 
A 1 55  ALA 55  53  53  ALA ALA A . n 
A 1 56  PHE 56  54  54  PHE PHE A . n 
A 1 57  PRO 57  55  55  PRO PRO A . n 
A 1 58  GLY 58  56  56  GLY GLY A . n 
A 1 59  GLU 59  57  57  GLU GLU A . n 
A 1 60  ILE 60  58  58  ILE ILE A . n 
A 1 61  LEU 61  59  59  LEU LEU A . n 
A 1 62  MET 62  60  60  MET MET A . n 
A 1 63  ARG 63  61  61  ARG ARG A . n 
A 1 64  MET 64  62  62  MET MET A . n 
A 1 65  LEU 65  63  63  LEU LEU A . n 
A 1 66  LYS 66  64  64  LYS LYS A . n 
A 1 67  LEU 67  65  65  LEU LEU A . n 
A 1 68  ILE 68  66  66  ILE ILE A . n 
A 1 69  ILE 69  67  67  ILE ILE A . n 
A 1 70  LEU 70  68  68  LEU LEU A . n 
A 1 71  PRO 71  69  69  PRO PRO A . n 
A 1 72  LEU 72  70  70  LEU LEU A . n 
A 1 73  ILE 73  71  71  ILE ILE A . n 
A 1 74  ILE 74  72  72  ILE ILE A . n 
A 1 75  SER 75  73  73  SER SER A . n 
A 1 76  SER 76  74  74  SER SER A . n 
A 1 77  MET 77  75  75  MET MET A . n 
A 1 78  ILE 78  76  76  ILE ILE A . n 
A 1 79  THR 79  77  77  THR THR A . n 
A 1 80  GLY 80  78  78  GLY GLY A . n 
A 1 81  VAL 81  79  79  VAL VAL A . n 
A 1 82  ALA 82  80  80  ALA ALA A . n 
A 1 83  ALA 83  81  81  ALA ALA A . n 
A 1 84  LEU 84  82  82  LEU LEU A . n 
A 1 85  ASP 85  83  83  ASP ASP A . n 
A 1 86  SER 86  84  84  SER SER A . n 
A 1 87  ASN 87  85  85  ASN ASN A . n 
A 1 88  VAL 88  86  86  VAL VAL A . n 
A 1 89  SER 89  87  87  SER SER A . n 
A 1 90  GLY 90  88  88  GLY GLY A . n 
A 1 91  LYS 91  89  89  LYS LYS A . n 
A 1 92  ILE 92  90  90  ILE ILE A . n 
A 1 93  GLY 93  91  91  GLY GLY A . n 
A 1 94  LEU 94  92  92  LEU LEU A . n 
A 1 95  ARG 95  93  93  ARG ARG A . n 
A 1 96  ALA 96  94  94  ALA ALA A . n 
A 1 97  VAL 97  95  95  VAL VAL A . n 
A 1 98  VAL 98  96  96  VAL VAL A . n 
A 1 99  TYR 99  97  97  TYR TYR A . n 
A 1 100 TYR 100 98  98  TYR TYR A . n 
A 1 101 PHE 101 99  99  PHE PHE A . n 
A 1 102 ALA 102 100 100 ALA ALA A . n 
A 1 103 THR 103 101 101 THR THR A . n 
A 1 104 THR 104 102 102 THR THR A . n 
A 1 105 LEU 105 103 103 LEU LEU A . n 
A 1 106 ILE 106 104 104 ILE ILE A . n 
A 1 107 ALA 107 105 105 ALA ALA A . n 
A 1 108 VAL 108 106 106 VAL VAL A . n 
A 1 109 ILE 109 107 107 ILE ILE A . n 
A 1 110 LEU 110 108 108 LEU LEU A . n 
A 1 111 GLY 111 109 109 GLY GLY A . n 
A 1 112 ILE 112 110 110 ILE ILE A . n 
A 1 113 VAL 113 111 111 VAL VAL A . n 
A 1 114 LEU 114 112 112 LEU LEU A . n 
A 1 115 VAL 115 113 113 VAL VAL A . n 
A 1 116 VAL 116 114 114 VAL VAL A . n 
A 1 117 SER 117 115 115 SER SER A . n 
A 1 118 ILE 118 116 116 ILE ILE A . n 
A 1 119 LYS 119 117 117 LYS LYS A . n 
A 1 120 PRO 120 118 118 PRO PRO A . n 
A 1 121 GLY 121 119 119 GLY GLY A . n 
A 1 122 VAL 122 120 ?   ?   ?   A . n 
A 1 123 THR 123 121 ?   ?   ?   A . n 
A 1 124 GLN 124 122 ?   ?   ?   A . n 
A 1 125 LYS 125 123 ?   ?   ?   A . n 
A 1 126 VAL 126 124 ?   ?   ?   A . n 
A 1 127 GLY 127 125 ?   ?   ?   A . n 
A 1 128 GLU 128 126 ?   ?   ?   A . n 
A 1 129 ILE 129 127 ?   ?   ?   A . n 
A 1 130 ALA 130 128 ?   ?   ?   A . n 
A 1 131 ARG 131 129 ?   ?   ?   A . n 
A 1 132 THR 132 130 ?   ?   ?   A . n 
A 1 133 GLY 133 131 ?   ?   ?   A . n 
A 1 134 SER 134 132 ?   ?   ?   A . n 
A 1 135 THR 135 133 ?   ?   ?   A . n 
A 1 136 PRO 136 134 ?   ?   ?   A . n 
A 1 137 GLU 137 135 ?   ?   ?   A . n 
A 1 138 VAL 138 136 ?   ?   ?   A . n 
A 1 139 SER 139 137 137 SER SER A . n 
A 1 140 THR 140 138 138 THR THR A . n 
A 1 141 VAL 141 139 139 VAL VAL A . n 
A 1 142 ASP 142 140 140 ASP ASP A . n 
A 1 143 ALA 143 141 141 ALA ALA A . n 
A 1 144 MET 144 142 142 MET MET A . n 
A 1 145 LEU 145 143 143 LEU LEU A . n 
A 1 146 ASP 146 144 144 ASP ASP A . n 
A 1 147 LEU 147 145 145 LEU LEU A . n 
A 1 148 ILE 148 146 146 ILE ILE A . n 
A 1 149 ARG 149 147 147 ARG ARG A . n 
A 1 150 ASN 150 148 148 ASN ASN A . n 
A 1 151 MET 151 149 149 MET MET A . n 
A 1 152 PHE 152 150 150 PHE PHE A . n 
A 1 153 PRO 153 151 151 PRO PRO A . n 
A 1 154 GLU 154 152 152 GLU GLU A . n 
A 1 155 ASN 155 153 153 ASN ASN A . n 
A 1 156 LEU 156 154 154 LEU LEU A . n 
A 1 157 VAL 157 155 155 VAL VAL A . n 
A 1 158 GLN 158 156 156 GLN GLN A . n 
A 1 159 ALA 159 157 157 ALA ALA A . n 
A 1 160 ALA 160 158 158 ALA ALA A . n 
A 1 161 PHE 161 159 159 PHE PHE A . n 
A 1 162 GLN 162 160 160 GLN GLN A . n 
A 1 163 GLN 163 161 161 GLN GLN A . n 
A 1 164 TYR 164 162 162 TYR TYR A . n 
A 1 165 LYS 165 163 163 LYS LYS A . n 
A 1 166 THR 166 164 164 THR THR A . n 
A 1 167 LYS 167 165 165 LYS LYS A . n 
A 1 168 ARG 168 166 166 ARG ARG A . n 
A 1 169 GLU 169 167 167 GLU GLU A . n 
A 1 170 GLU 170 168 168 GLU GLU A . n 
A 1 171 VAL 171 169 ?   ?   ?   A . n 
A 1 172 LYS 172 170 ?   ?   ?   A . n 
A 1 173 PRO 173 171 ?   ?   ?   A . n 
A 1 174 PRO 174 172 ?   ?   ?   A . n 
A 1 175 SER 175 173 ?   ?   ?   A . n 
A 1 176 ASP 176 174 ?   ?   ?   A . n 
A 1 177 PRO 177 175 ?   ?   ?   A . n 
A 1 178 GLU 178 176 ?   ?   ?   A . n 
A 1 179 MET 179 177 ?   ?   ?   A . n 
A 1 180 THR 180 178 ?   ?   ?   A . n 
A 1 181 MET 181 179 ?   ?   ?   A . n 
A 1 182 THR 182 180 ?   ?   ?   A . n 
A 1 183 GLU 183 181 ?   ?   ?   A . n 
A 1 184 GLU 184 182 ?   ?   ?   A . n 
A 1 185 SER 185 183 ?   ?   ?   A . n 
A 1 186 PHE 186 184 ?   ?   ?   A . n 
A 1 187 THR 187 185 ?   ?   ?   A . n 
A 1 188 ALA 188 186 ?   ?   ?   A . n 
A 1 189 VAL 189 187 ?   ?   ?   A . n 
A 1 190 MET 190 188 ?   ?   ?   A . n 
A 1 191 THR 191 189 ?   ?   ?   A . n 
A 1 192 THR 192 190 ?   ?   ?   A . n 
A 1 193 ALA 193 191 ?   ?   ?   A . n 
A 1 194 ILE 194 192 ?   ?   ?   A . n 
A 1 195 SER 195 193 ?   ?   ?   A . n 
A 1 196 LYS 196 194 ?   ?   ?   A . n 
A 1 197 THR 197 195 ?   ?   ?   A . n 
A 1 198 LYS 198 196 ?   ?   ?   A . n 
A 1 199 THR 199 197 ?   ?   ?   A . n 
A 1 200 LYS 200 198 ?   ?   ?   A . n 
A 1 201 GLU 201 199 ?   ?   ?   A . n 
A 1 202 TYR 202 200 200 TYR TYR A . n 
A 1 203 LYS 203 201 201 LYS LYS A . n 
A 1 204 ILE 204 202 202 ILE ILE A . n 
A 1 205 VAL 205 203 203 VAL VAL A . n 
A 1 206 GLY 206 204 204 GLY GLY A . n 
A 1 207 MET 207 205 205 MET MET A . n 
A 1 208 TYR 208 206 206 TYR TYR A . n 
A 1 209 SER 209 207 207 SER SER A . n 
A 1 210 ASP 210 208 208 ASP ASP A . n 
A 1 211 GLY 211 209 209 GLY GLY A . n 
A 1 212 ILE 212 210 210 ILE ILE A . n 
A 1 213 ASN 213 211 211 ASN ASN A . n 
A 1 214 VAL 214 212 212 VAL VAL A . n 
A 1 215 LEU 215 213 213 LEU LEU A . n 
A 1 216 GLY 216 214 214 GLY GLY A . n 
A 1 217 LEU 217 215 215 LEU LEU A . n 
A 1 218 ILE 218 216 216 ILE ILE A . n 
A 1 219 VAL 219 217 217 VAL VAL A . n 
A 1 220 PHE 220 218 218 PHE PHE A . n 
A 1 221 ALA 221 219 219 ALA ALA A . n 
A 1 222 LEU 222 220 220 LEU LEU A . n 
A 1 223 VAL 223 221 221 VAL VAL A . n 
A 1 224 PHE 224 222 222 PHE PHE A . n 
A 1 225 GLY 225 223 223 GLY GLY A . n 
A 1 226 LEU 226 224 224 LEU LEU A . n 
A 1 227 VAL 227 225 225 VAL VAL A . n 
A 1 228 ILE 228 226 226 ILE ILE A . n 
A 1 229 GLY 229 227 227 GLY GLY A . n 
A 1 230 LYS 230 228 228 LYS LYS A . n 
A 1 231 MET 231 229 229 MET MET A . n 
A 1 232 GLY 232 230 230 GLY GLY A . n 
A 1 233 GLU 233 231 231 GLU GLU A . n 
A 1 234 LYS 234 232 232 LYS LYS A . n 
A 1 235 GLY 235 233 233 GLY GLY A . n 
A 1 236 GLN 236 234 234 GLN GLN A . n 
A 1 237 ILE 237 235 235 ILE ILE A . n 
A 1 238 LEU 238 236 236 LEU LEU A . n 
A 1 239 VAL 239 237 237 VAL VAL A . n 
A 1 240 ASP 240 238 238 ASP ASP A . n 
A 1 241 PHE 241 239 239 PHE PHE A . n 
A 1 242 PHE 242 240 240 PHE PHE A . n 
A 1 243 ASN 243 241 241 ASN ASN A . n 
A 1 244 ALA 244 242 242 ALA ALA A . n 
A 1 245 LEU 245 243 243 LEU LEU A . n 
A 1 246 SER 246 244 244 SER SER A . n 
A 1 247 ASP 247 245 245 ASP ASP A . n 
A 1 248 ALA 248 246 246 ALA ALA A . n 
A 1 249 THR 249 247 247 THR THR A . n 
A 1 250 MET 250 248 248 MET MET A . n 
A 1 251 LYS 251 249 249 LYS LYS A . n 
A 1 252 ILE 252 250 250 ILE ILE A . n 
A 1 253 VAL 253 251 251 VAL VAL A . n 
A 1 254 GLN 254 252 252 GLN GLN A . n 
A 1 255 ILE 255 253 253 ILE ILE A . n 
A 1 256 ILE 256 254 254 ILE ILE A . n 
A 1 257 MET 257 255 255 MET MET A . n 
A 1 258 TRP 258 256 256 TRP TRP A . n 
A 1 259 TYR 259 257 257 TYR TYR A . n 
A 1 260 MET 260 258 258 MET MET A . n 
A 1 261 PRO 261 259 259 PRO PRO A . n 
A 1 262 LEU 262 260 260 LEU LEU A . n 
A 1 263 GLY 263 261 261 GLY GLY A . n 
A 1 264 ILE 264 262 262 ILE ILE A . n 
A 1 265 LEU 265 263 263 LEU LEU A . n 
A 1 266 PHE 266 264 264 PHE PHE A . n 
A 1 267 LEU 267 265 265 LEU LEU A . n 
A 1 268 ILE 268 266 266 ILE ILE A . n 
A 1 269 ALA 269 267 267 ALA ALA A . n 
A 1 270 GLY 270 268 268 GLY GLY A . n 
A 1 271 CYS 271 269 269 CYS CYS A . n 
A 1 272 ILE 272 270 270 ILE ILE A . n 
A 1 273 ILE 273 271 271 ILE ILE A . n 
A 1 274 GLU 274 272 272 GLU GLU A . n 
A 1 275 VAL 275 273 273 VAL VAL A . n 
A 1 276 GLU 276 274 274 GLU GLU A . n 
A 1 277 ASP 277 275 275 ASP ASP A . n 
A 1 278 TRP 278 276 276 TRP TRP A . n 
A 1 279 GLU 279 277 277 GLU GLU A . n 
A 1 280 ILE 280 278 278 ILE ILE A . n 
A 1 281 PHE 281 279 279 PHE PHE A . n 
A 1 282 ARG 282 280 280 ARG ARG A . n 
A 1 283 LYS 283 281 281 LYS LYS A . n 
A 1 284 LEU 284 282 282 LEU LEU A . n 
A 1 285 GLY 285 283 283 GLY GLY A . n 
A 1 286 LEU 286 284 284 LEU LEU A . n 
A 1 287 TYR 287 285 285 TYR TYR A . n 
A 1 288 MET 288 286 286 MET MET A . n 
A 1 289 ALA 289 287 287 ALA ALA A . n 
A 1 290 THR 290 288 288 THR THR A . n 
A 1 291 VAL 291 289 289 VAL VAL A . n 
A 1 292 LEU 292 290 290 LEU LEU A . n 
A 1 293 THR 293 291 291 THR THR A . n 
A 1 294 GLY 294 292 292 GLY GLY A . n 
A 1 295 LEU 295 293 293 LEU LEU A . n 
A 1 296 ALA 296 294 294 ALA ALA A . n 
A 1 297 ILE 297 295 295 ILE ILE A . n 
A 1 298 HIS 298 296 296 HIS HIS A . n 
A 1 299 SER 299 297 297 SER SER A . n 
A 1 300 ILE 300 298 298 ILE ILE A . n 
A 1 301 VAL 301 299 299 VAL VAL A . n 
A 1 302 ILE 302 300 300 ILE ILE A . n 
A 1 303 LEU 303 301 301 LEU LEU A . n 
A 1 304 PRO 304 302 302 PRO PRO A . n 
A 1 305 LEU 305 303 303 LEU LEU A . n 
A 1 306 ILE 306 304 304 ILE ILE A . n 
A 1 307 TYR 307 305 305 TYR TYR A . n 
A 1 308 PHE 308 306 306 PHE PHE A . n 
A 1 309 ILE 309 307 307 ILE ILE A . n 
A 1 310 VAL 310 308 308 VAL VAL A . n 
A 1 311 VAL 311 309 309 VAL VAL A . n 
A 1 312 ARG 312 310 310 ARG ARG A . n 
A 1 313 LYS 313 311 311 LYS LYS A . n 
A 1 314 ASN 314 312 312 ASN ASN A . n 
A 1 315 PRO 315 313 313 PRO PRO A . n 
A 1 316 PHE 316 314 314 PHE PHE A . n 
A 1 317 ARG 317 315 315 ARG ARG A . n 
A 1 318 PHE 318 316 316 PHE PHE A . n 
A 1 319 ALA 319 317 317 ALA ALA A . n 
A 1 320 MET 320 318 318 MET MET A . n 
A 1 321 GLY 321 319 319 GLY GLY A . n 
A 1 322 MET 322 320 320 MET MET A . n 
A 1 323 ALA 323 321 321 ALA ALA A . n 
A 1 324 GLN 324 322 322 GLN GLN A . n 
A 1 325 ALA 325 323 323 ALA ALA A . n 
A 1 326 LEU 326 324 324 LEU LEU A . n 
A 1 327 LEU 327 325 325 LEU LEU A . n 
A 1 328 THR 328 326 326 THR THR A . n 
A 1 329 ALA 329 327 327 ALA ALA A . n 
A 1 330 LEU 330 328 328 LEU LEU A . n 
A 1 331 MET 331 329 329 MET MET A . n 
A 1 332 ILE 332 330 330 ILE ILE A . n 
A 1 333 SER 333 331 331 SER SER A . n 
A 1 334 SER 334 332 332 SER SER A . n 
A 1 335 SER 335 333 333 SER SER A . n 
A 1 336 SER 336 334 334 SER SER A . n 
A 1 337 ALA 337 335 335 ALA ALA A . n 
A 1 338 THR 338 336 336 THR THR A . n 
A 1 339 LEU 339 337 337 LEU LEU A . n 
A 1 340 PRO 340 338 338 PRO PRO A . n 
A 1 341 VAL 341 339 339 VAL VAL A . n 
A 1 342 THR 342 340 340 THR THR A . n 
A 1 343 PHE 343 341 341 PHE PHE A . n 
A 1 344 ARG 344 342 342 ARG ARG A . n 
A 1 345 CYS 345 343 343 CYS CYS A . n 
A 1 346 ALA 346 344 344 ALA ALA A . n 
A 1 347 GLU 347 345 345 GLU GLU A . n 
A 1 348 GLU 348 346 346 GLU GLU A . n 
A 1 349 ASN 349 347 347 ASN ASN A . n 
A 1 350 ASN 350 348 348 ASN ASN A . n 
A 1 351 GLN 351 349 349 GLN GLN A . n 
A 1 352 VAL 352 350 350 VAL VAL A . n 
A 1 353 ASP 353 351 351 ASP ASP A . n 
A 1 354 LYS 354 352 352 LYS LYS A . n 
A 1 355 ARG 355 353 353 ARG ARG A . n 
A 1 356 ILE 356 354 354 ILE ILE A . n 
A 1 357 THR 357 355 355 THR THR A . n 
A 1 358 ARG 358 356 356 ARG ARG A . n 
A 1 359 PHE 359 357 357 PHE PHE A . n 
A 1 360 VAL 360 358 358 VAL VAL A . n 
A 1 361 LEU 361 359 359 LEU LEU A . n 
A 1 362 PRO 362 360 360 PRO PRO A . n 
A 1 363 VAL 363 361 361 VAL VAL A . n 
A 1 364 GLY 364 362 362 GLY GLY A . n 
A 1 365 ALA 365 363 363 ALA ALA A . n 
A 1 366 THR 366 364 364 THR THR A . n 
A 1 367 ILE 367 365 365 ILE ILE A . n 
A 1 368 ASN 368 366 366 ASN ASN A . n 
A 1 369 MET 369 367 367 MET MET A . n 
A 1 370 ASP 370 368 368 ASP ASP A . n 
A 1 371 GLY 371 369 369 GLY GLY A . n 
A 1 372 THR 372 370 370 THR THR A . n 
A 1 373 ALA 373 371 371 ALA ALA A . n 
A 1 374 LEU 374 372 372 LEU LEU A . n 
A 1 375 TYR 375 373 373 TYR TYR A . n 
A 1 376 GLU 376 374 374 GLU GLU A . n 
A 1 377 ALA 377 375 375 ALA ALA A . n 
A 1 378 VAL 378 376 376 VAL VAL A . n 
A 1 379 ALA 379 377 377 ALA ALA A . n 
A 1 380 ALA 380 378 378 ALA ALA A . n 
A 1 381 VAL 381 379 379 VAL VAL A . n 
A 1 382 PHE 382 380 380 PHE PHE A . n 
A 1 383 ILE 383 381 381 ILE ILE A . n 
A 1 384 ALA 384 382 382 ALA ALA A . n 
A 1 385 GLN 385 383 383 GLN GLN A . n 
A 1 386 LEU 386 384 384 LEU LEU A . n 
A 1 387 ASN 387 385 385 ASN ASN A . n 
A 1 388 ASP 388 386 386 ASP ASP A . n 
A 1 389 LEU 389 387 387 LEU LEU A . n 
A 1 390 ASP 390 388 388 ASP ASP A . n 
A 1 391 LEU 391 389 389 LEU LEU A . n 
A 1 392 GLY 392 390 390 GLY GLY A . n 
A 1 393 ILE 393 391 391 ILE ILE A . n 
A 1 394 GLY 394 392 392 GLY GLY A . n 
A 1 395 GLN 395 393 393 GLN GLN A . n 
A 1 396 ILE 396 394 394 ILE ILE A . n 
A 1 397 ILE 397 395 395 ILE ILE A . n 
A 1 398 THR 398 396 396 THR THR A . n 
A 1 399 ILE 399 397 397 ILE ILE A . n 
A 1 400 SER 400 398 398 SER SER A . n 
A 1 401 ILE 401 399 399 ILE ILE A . n 
A 1 402 THR 402 400 400 THR THR A . n 
A 1 403 ALA 403 401 401 ALA ALA A . n 
A 1 404 THR 404 402 402 THR THR A . n 
A 1 405 SER 405 403 403 SER SER A . n 
A 1 406 ALA 406 404 404 ALA ALA A . n 
A 1 407 SER 407 405 405 SER SER A . n 
A 1 408 ILE 408 406 406 ILE ILE A . n 
A 1 409 GLY 409 407 407 GLY GLY A . n 
A 1 410 ALA 410 408 408 ALA ALA A . n 
A 1 411 ALA 411 409 409 ALA ALA A . n 
A 1 412 GLY 412 410 410 GLY GLY A . n 
A 1 413 VAL 413 411 411 VAL VAL A . n 
A 1 414 PRO 414 412 412 PRO PRO A . n 
A 1 415 GLN 415 413 413 GLN GLN A . n 
A 1 416 ALA 416 414 414 ALA ALA A . n 
A 1 417 GLY 417 415 415 GLY GLY A . n 
A 1 418 LEU 418 416 416 LEU LEU A . n 
A 1 419 VAL 419 417 417 VAL VAL A . n 
A 1 420 THR 420 418 418 THR THR A . n 
A 1 421 MET 421 419 419 MET MET A . n 
A 1 422 VAL 422 420 420 VAL VAL A . n 
A 1 423 ILE 423 421 421 ILE ILE A . n 
A 1 424 VAL 424 422 422 VAL VAL A . n 
A 1 425 LEU 425 423 423 LEU LEU A . n 
A 1 426 SER 426 424 424 SER SER A . n 
A 1 427 ALA 427 425 425 ALA ALA A . n 
A 1 428 VAL 428 426 426 VAL VAL A . n 
A 1 429 GLY 429 427 427 GLY GLY A . n 
A 1 430 LEU 430 428 428 LEU LEU A . n 
A 1 431 PRO 431 429 429 PRO PRO A . n 
A 1 432 ALA 432 430 430 ALA ALA A . n 
A 1 433 GLU 433 431 431 GLU GLU A . n 
A 1 434 ASP 434 432 432 ASP ASP A . n 
A 1 435 VAL 435 433 433 VAL VAL A . n 
A 1 436 THR 436 434 434 THR THR A . n 
A 1 437 LEU 437 435 435 LEU LEU A . n 
A 1 438 ILE 438 436 436 ILE ILE A . n 
A 1 439 ILE 439 437 437 ILE ILE A . n 
A 1 440 ALA 440 438 438 ALA ALA A . n 
A 1 441 VAL 441 439 439 VAL VAL A . n 
A 1 442 ASP 442 440 440 ASP ASP A . n 
A 1 443 CYS 443 441 441 CYS CYS A . n 
A 1 444 LEU 444 442 442 LEU LEU A . n 
A 1 445 LEU 445 443 443 LEU LEU A . n 
A 1 446 ASP 446 444 444 ASP ASP A . n 
A 1 447 ARG 447 445 445 ARG ARG A . n 
A 1 448 PHE 448 446 446 PHE PHE A . n 
A 1 449 ARG 449 447 447 ARG ARG A . n 
A 1 450 THR 450 448 448 THR THR A . n 
A 1 451 MET 451 449 449 MET MET A . n 
A 1 452 VAL 452 450 450 VAL VAL A . n 
A 1 453 ASN 453 451 451 ASN ASN A . n 
A 1 454 VAL 454 452 452 VAL VAL A . n 
A 1 455 LEU 455 453 453 LEU LEU A . n 
A 1 456 GLY 456 454 454 GLY GLY A . n 
A 1 457 ASP 457 455 455 ASP ASP A . n 
A 1 458 ALA 458 456 456 ALA ALA A . n 
A 1 459 PHE 459 457 457 PHE PHE A . n 
A 1 460 GLY 460 458 458 GLY GLY A . n 
A 1 461 THR 461 459 459 THR THR A . n 
A 1 462 GLY 462 460 460 GLY GLY A . n 
A 1 463 ILE 463 461 461 ILE ILE A . n 
A 1 464 VAL 464 462 462 VAL VAL A . n 
A 1 465 GLU 465 463 463 GLU GLU A . n 
A 1 466 LYS 466 464 464 LYS LYS A . n 
A 1 467 LEU 467 465 465 LEU LEU A . n 
A 1 468 SER 468 466 466 SER SER A . n 
A 1 469 LYS 469 467 467 LYS LYS A . n 
A 1 470 LYS 470 468 468 LYS LYS A . n 
A 1 471 GLU 471 469 469 GLU GLU A . n 
A 1 472 LEU 472 470 470 LEU LEU A . n 
A 1 473 GLU 473 471 471 GLU GLU A . n 
A 1 474 GLN 474 472 472 GLN GLN A . n 
A 1 475 MET 475 473 473 MET MET A . n 
A 1 476 ASP 476 474 474 ASP ASP A . n 
A 1 477 VAL 477 475 475 VAL VAL A . n 
A 1 478 SER 478 476 476 SER SER A . n 
A 1 479 SER 479 477 ?   ?   ?   A . n 
A 1 480 GLU 480 478 ?   ?   ?   A . n 
A 1 481 VAL 481 479 ?   ?   ?   A . n 
A 1 482 ASN 482 480 ?   ?   ?   A . n 
A 1 483 ILE 483 481 ?   ?   ?   A . n 
A 1 484 VAL 484 482 ?   ?   ?   A . n 
A 1 485 ASN 485 483 ?   ?   ?   A . n 
A 1 486 PRO 486 484 ?   ?   ?   A . n 
A 1 487 PHE 487 485 ?   ?   ?   A . n 
A 1 488 ALA 488 486 ?   ?   ?   A . n 
A 1 489 LEU 489 487 ?   ?   ?   A . n 
A 1 490 GLU 490 488 ?   ?   ?   A . n 
A 1 491 SER 491 489 ?   ?   ?   A . n 
A 1 492 THR 492 490 ?   ?   ?   A . n 
A 1 493 ILE 493 491 ?   ?   ?   A . n 
A 1 494 LEU 494 492 ?   ?   ?   A . n 
A 1 495 ASP 495 493 ?   ?   ?   A . n 
A 1 496 ASN 496 494 ?   ?   ?   A . n 
A 1 497 GLU 497 495 ?   ?   ?   A . n 
A 1 498 ASP 498 496 ?   ?   ?   A . n 
A 1 499 SER 499 497 ?   ?   ?   A . n 
A 1 500 ASP 500 498 ?   ?   ?   A . n 
A 1 501 THR 501 499 ?   ?   ?   A . n 
A 1 502 LYS 502 500 ?   ?   ?   A . n 
A 1 503 LYS 503 501 ?   ?   ?   A . n 
A 1 504 SER 504 502 ?   ?   ?   A . n 
A 1 505 TYR 505 503 ?   ?   ?   A . n 
A 1 506 VAL 506 504 ?   ?   ?   A . n 
A 1 507 ASN 507 505 ?   ?   ?   A . n 
A 1 508 GLY 508 506 ?   ?   ?   A . n 
A 1 509 GLY 509 507 ?   ?   ?   A . n 
A 1 510 PHE 510 508 ?   ?   ?   A . n 
A 1 511 ALA 511 509 ?   ?   ?   A . n 
A 1 512 VAL 512 510 ?   ?   ?   A . n 
A 1 513 ASP 513 511 ?   ?   ?   A . n 
A 1 514 LYS 514 512 ?   ?   ?   A . n 
A 1 515 SER 515 513 ?   ?   ?   A . n 
A 1 516 ASP 516 514 ?   ?   ?   A . n 
A 1 517 THR 517 515 ?   ?   ?   A . n 
A 1 518 ILE 518 516 ?   ?   ?   A . n 
A 1 519 SER 519 517 ?   ?   ?   A . n 
A 1 520 PHE 520 518 ?   ?   ?   A . n 
A 1 521 THR 521 519 ?   ?   ?   A . n 
A 1 522 GLN 522 520 ?   ?   ?   A . n 
A 1 523 THR 523 521 ?   ?   ?   A . n 
A 1 524 SER 524 522 ?   ?   ?   A . n 
A 1 525 GLN 525 523 ?   ?   ?   A . n 
A 1 526 PHE 526 524 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CYS ? ? CYS ? ? 'SUBJECT OF INVESTIGATION' ? 
2 HG  ? ? HG  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NA  ? ? NA  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
B 2 CYS 1 600 600 CYS CYS A . 
C 3 NA  1 601 601 NA  NA  A . 
D 3 NA  1 602 602 NA  NA  A . 
E 3 NA  1 603 603 NA  NA  A . 
F 4 HG  1 604 604 HG  HG  A . 
# 
_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                   9D69 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9D69 
_struct.title                        
;Human excitatory amino acid transporter 3 (EAAT3) with bound L-Cysteine in an intermediate outward facing state (slight upper position)
;
_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        9D69 
_struct_keywords.text            'human EAAT3, Cysteine, iOFS-upper, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EAA3_HUMAN 
_struct_ref.pdbx_db_accession          P43005 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MGKPARKGCEWKRFLKNNWVLLSTVAAVVLGITTGVLVREHSNLSTLEKFYFAFPGEILMRMLKLIILPLIISSMITGVA
ALDSNVSGKIGLRAVVYYFCTTLIAVILGIVLVVSIKPGVTQKVGEIARTGSTPEVSTVDAMLDLIRNMFPENLVQACFQ
QYKTKREEVKPPSDPEMNMTEESFTAVMTTAISKNKTKEYKIVGMYSDGINVLGLIVFCLVFGLVIGKMGEKGQILVDFF
NALSDATMKIVQIIMCYMPLGILFLIAGKIIEVEDWEIFRKLGLYMATVLTGLAIHSIVILPLIYFIVVRKNPFRFAMGM
AQALLTALMISSSSATLPVTFRCAEENNQVDKRITRFVLPVGATINMDGTALYEAVAAVFIAQLNDLDLGIGQIITISIT
ATSASIGAAGVPQAGLVTMVIVLSAVGLPAEDVTLIIAVDWLLDRFRTMVNVLGDAFGTGIVEKLSKKELEQMDVSSEVN
IVNPFALESTILDNEDSDTKKSYVNGGFAVDKSDTISFTQTSQF
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9D69 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 526 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P43005 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  524 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       524 
# 
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 9D69 GLY A 1   ? UNP P43005 ?   ?   'expression tag'      -1  1  
1 9D69 PRO A 2   ? UNP P43005 ?   ?   'expression tag'      0   2  
1 9D69 ALA A 11  ? UNP P43005 CYS 9   'engineered mutation' 9   3  
1 9D69 ALA A 102 ? UNP P43005 CYS 100 'engineered mutation' 100 4  
1 9D69 ALA A 160 ? UNP P43005 CYS 158 'engineered mutation' 158 5  
1 9D69 THR A 180 ? UNP P43005 ASN 178 'engineered mutation' 178 6  
1 9D69 THR A 197 ? UNP P43005 ASN 195 'engineered mutation' 195 7  
1 9D69 ALA A 221 ? UNP P43005 CYS 219 'engineered mutation' 219 8  
1 9D69 TRP A 258 ? UNP P43005 CYS 256 'engineered mutation' 256 9  
1 9D69 CYS A 271 ? UNP P43005 LYS 269 'engineered mutation' 269 10 
1 9D69 CYS A 443 ? UNP P43005 TRP 441 'engineered mutation' 441 11 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 20  ? SER A 44  ? ASN A 18  SER A 42  1 ? 25 
HELX_P HELX_P2  AA2 SER A 47  ? ALA A 55  ? SER A 45  ALA A 53  1 ? 9  
HELX_P HELX_P3  AA3 ALA A 55  ? LEU A 84  ? ALA A 53  LEU A 82  1 ? 30 
HELX_P HELX_P4  AA4 ASP A 85  ? LYS A 119 ? ASP A 83  LYS A 117 1 ? 35 
HELX_P HELX_P5  AA5 THR A 140 ? PHE A 152 ? THR A 138 PHE A 150 1 ? 13 
HELX_P HELX_P6  AA6 ASN A 155 ? ALA A 160 ? ASN A 153 ALA A 158 1 ? 6  
HELX_P HELX_P7  AA7 ASN A 213 ? GLY A 232 ? ASN A 211 GLY A 230 1 ? 20 
HELX_P HELX_P8  AA8 GLY A 235 ? ILE A 272 ? GLY A 233 ILE A 270 1 ? 38 
HELX_P HELX_P9  AA9 GLU A 279 ? LEU A 284 ? GLU A 277 LEU A 282 1 ? 6  
HELX_P HELX_P10 AB1 LEU A 284 ? VAL A 301 ? LEU A 282 VAL A 299 1 ? 18 
HELX_P HELX_P11 AB2 VAL A 301 ? ARG A 312 ? VAL A 299 ARG A 310 1 ? 12 
HELX_P HELX_P12 AB3 ASN A 314 ? MET A 322 ? ASN A 312 MET A 320 1 ? 9  
HELX_P HELX_P13 AB4 MET A 322 ? SER A 333 ? MET A 320 SER A 331 1 ? 12 
HELX_P HELX_P14 AB5 THR A 338 ? ASN A 350 ? THR A 336 ASN A 348 1 ? 13 
HELX_P HELX_P15 AB6 ASP A 353 ? ALA A 365 ? ASP A 351 ALA A 363 1 ? 13 
HELX_P HELX_P16 AB7 MET A 369 ? ASP A 388 ? MET A 367 ASP A 386 1 ? 20 
HELX_P HELX_P17 AB8 GLY A 392 ? ALA A 410 ? GLY A 390 ALA A 408 1 ? 19 
HELX_P HELX_P18 AB9 GLN A 415 ? GLY A 429 ? GLN A 413 GLY A 427 1 ? 15 
HELX_P HELX_P19 AC1 ASP A 434 ? SER A 468 ? ASP A 432 SER A 466 1 ? 35 
HELX_P HELX_P20 AC2 SER A 468 ? VAL A 477 ? SER A 466 VAL A 475 1 ? 10 
# 
_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 ? ? A TYR 100 O   ? ? ? 1_555 E NA . NA ? ? A TYR 98  A NA 603 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
metalc2  metalc ? ? A THR 103 OG1 ? ? ? 1_555 E NA . NA ? ? A THR 101 A NA 603 1_555 ? ? ? ? ? ? ? 2.462 ? ? 
metalc3  metalc ? ? A THR 104 OG1 ? ? ? 1_555 E NA . NA ? ? A THR 102 A NA 603 1_555 ? ? ? ? ? ? ? 2.108 ? ? 
metalc4  metalc ? ? A CYS 271 SG  ? ? ? 1_555 F HG . HG ? ? A CYS 269 A HG 604 1_555 ? ? ? ? ? ? ? 2.698 ? ? 
metalc5  metalc ? ? A GLY 364 O   ? ? ? 1_555 C NA . NA ? ? A GLY 362 A NA 601 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc6  metalc ? ? A THR 366 O   ? ? ? 1_555 D NA . NA ? ? A THR 364 A NA 602 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc7  metalc ? ? A ASN 368 O   ? ? ? 1_555 C NA . NA ? ? A ASN 366 A NA 601 1_555 ? ? ? ? ? ? ? 2.261 ? ? 
metalc8  metalc ? ? A ASN 368 OD1 ? ? ? 1_555 E NA . NA ? ? A ASN 366 A NA 603 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc9  metalc ? ? A ASP 370 OD1 ? ? ? 1_555 E NA . NA ? ? A ASP 368 A NA 603 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc10 metalc ? ? A SER 407 O   ? ? ? 1_555 D NA . NA ? ? A SER 405 A NA 602 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc11 metalc ? ? A ALA 410 O   ? ? ? 1_555 D NA . NA ? ? A ALA 408 A NA 602 1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc12 metalc ? ? A ASP 457 OD1 ? ? ? 1_555 C NA . NA ? ? A ASP 455 A NA 601 1_555 ? ? ? ? ? ? ? 3.182 ? ? 
metalc13 metalc ? ? A ASP 457 OD2 ? ? ? 1_555 C NA . NA ? ? A ASP 455 A NA 601 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
# 
_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  O   ? A TYR 100 ? A TYR 98  ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OG1 ? A THR 103 ? A THR 101 ? 1_555 75.1  ? 
2  O   ? A TYR 100 ? A TYR 98  ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OG1 ? A THR 104 ? A THR 102 ? 1_555 77.5  ? 
3  OG1 ? A THR 103 ? A THR 101 ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OG1 ? A THR 104 ? A THR 102 ? 1_555 131.5 ? 
4  O   ? A TYR 100 ? A TYR 98  ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OD1 ? A ASN 368 ? A ASN 366 ? 1_555 134.4 ? 
5  OG1 ? A THR 103 ? A THR 101 ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OD1 ? A ASN 368 ? A ASN 366 ? 1_555 109.9 ? 
6  OG1 ? A THR 104 ? A THR 102 ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OD1 ? A ASN 368 ? A ASN 366 ? 1_555 117.9 ? 
7  O   ? A TYR 100 ? A TYR 98  ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OD1 ? A ASP 370 ? A ASP 368 ? 1_555 145.8 ? 
8  OG1 ? A THR 103 ? A THR 101 ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OD1 ? A ASP 370 ? A ASP 368 ? 1_555 81.7  ? 
9  OG1 ? A THR 104 ? A THR 102 ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OD1 ? A ASP 370 ? A ASP 368 ? 1_555 100.5 ? 
10 OD1 ? A ASN 368 ? A ASN 366 ? 1_555 NA ? E NA . ? A NA 603 ? 1_555 OD1 ? A ASP 370 ? A ASP 368 ? 1_555 77.2  ? 
11 O   ? A GLY 364 ? A GLY 362 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 O   ? A ASN 368 ? A ASN 366 ? 1_555 71.6  ? 
12 O   ? A GLY 364 ? A GLY 362 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OD1 ? A ASP 457 ? A ASP 455 ? 1_555 73.6  ? 
13 O   ? A ASN 368 ? A ASN 366 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OD1 ? A ASP 457 ? A ASP 455 ? 1_555 64.7  ? 
14 O   ? A GLY 364 ? A GLY 362 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OD2 ? A ASP 457 ? A ASP 455 ? 1_555 74.4  ? 
15 O   ? A ASN 368 ? A ASN 366 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OD2 ? A ASP 457 ? A ASP 455 ? 1_555 106.2 ? 
16 OD1 ? A ASP 457 ? A ASP 455 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OD2 ? A ASP 457 ? A ASP 455 ? 1_555 43.5  ? 
17 O   ? A THR 366 ? A THR 364 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A SER 407 ? A SER 405 ? 1_555 113.0 ? 
18 O   ? A THR 366 ? A THR 364 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A ALA 410 ? A ALA 408 ? 1_555 94.9  ? 
19 O   ? A SER 407 ? A SER 405 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A ALA 410 ? A ALA 408 ? 1_555 145.1 ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN A 162 ? GLU A 169 ? GLN A 160 GLU A 167 
AA1 2 LYS A 203 ? ASP A 210 ? LYS A 201 ASP A 208 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   GLU 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    169 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    GLU 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     167 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   LYS 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    203 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    LYS 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     201 
# 
_pdbx_entry_details.entry_id                   9D69 
_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     Y 
_pdbx_entry_details.has_protein_modification   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 ASN A 18  ? ? -99.03 37.10   
2 1 GLU A 274 ? ? 65.91  -121.69 
3 1 ASN A 312 ? ? -56.10 107.22  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9D69 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   59.17 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      OTHER 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  8CV3 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                8CV3 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9D69 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     'This is number of monomer from C3 expanded particles.' 
_em_3d_reconstruction.resolution                  2.99 
_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               60670 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          1 
_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       '20 mM Hepes-Tris pH 7.4, 200 mM NaCl and 0.01% GDN, 10 mM L-Cysteine' 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'EAAT3 monomer with L-Cys bound at iOFS' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9D69 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI/PHILIPS CM300FEG/T' 
_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             800 
_em_imaging.nominal_defocus_max             2400 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9D69 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9D69 
_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              9D69 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
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 GLY -1  ? A GLY 1   
2   1 Y 1 A PRO 0   ? A PRO 2   
3   1 Y 1 A MET 1   ? A MET 3   
4   1 Y 1 A GLY 2   ? A GLY 4   
5   1 Y 1 A LYS 3   ? A LYS 5   
6   1 Y 1 A PRO 4   ? A PRO 6   
7   1 Y 1 A ALA 5   ? A ALA 7   
8   1 Y 1 A ARG 6   ? A ARG 8   
9   1 Y 1 A LYS 7   ? A LYS 9   
10  1 Y 1 A GLY 8   ? A GLY 10  
11  1 Y 1 A ALA 9   ? A ALA 11  
12  1 Y 1 A GLU 10  ? A GLU 12  
13  1 Y 1 A TRP 11  ? A TRP 13  
14  1 Y 1 A LYS 12  ? A LYS 14  
15  1 Y 1 A ARG 13  ? A ARG 15  
16  1 Y 1 A PHE 14  ? A PHE 16  
17  1 Y 1 A LEU 15  ? A LEU 17  
18  1 Y 1 A LYS 16  ? A LYS 18  
19  1 Y 1 A VAL 120 ? A VAL 122 
20  1 Y 1 A THR 121 ? A THR 123 
21  1 Y 1 A GLN 122 ? A GLN 124 
22  1 Y 1 A LYS 123 ? A LYS 125 
23  1 Y 1 A VAL 124 ? A VAL 126 
24  1 Y 1 A GLY 125 ? A GLY 127 
25  1 Y 1 A GLU 126 ? A GLU 128 
26  1 Y 1 A ILE 127 ? A ILE 129 
27  1 Y 1 A ALA 128 ? A ALA 130 
28  1 Y 1 A ARG 129 ? A ARG 131 
29  1 Y 1 A THR 130 ? A THR 132 
30  1 Y 1 A GLY 131 ? A GLY 133 
31  1 Y 1 A SER 132 ? A SER 134 
32  1 Y 1 A THR 133 ? A THR 135 
33  1 Y 1 A PRO 134 ? A PRO 136 
34  1 Y 1 A GLU 135 ? A GLU 137 
35  1 Y 1 A VAL 136 ? A VAL 138 
36  1 Y 1 A VAL 169 ? A VAL 171 
37  1 Y 1 A LYS 170 ? A LYS 172 
38  1 Y 1 A PRO 171 ? A PRO 173 
39  1 Y 1 A PRO 172 ? A PRO 174 
40  1 Y 1 A SER 173 ? A SER 175 
41  1 Y 1 A ASP 174 ? A ASP 176 
42  1 Y 1 A PRO 175 ? A PRO 177 
43  1 Y 1 A GLU 176 ? A GLU 178 
44  1 Y 1 A MET 177 ? A MET 179 
45  1 Y 1 A THR 178 ? A THR 180 
46  1 Y 1 A MET 179 ? A MET 181 
47  1 Y 1 A THR 180 ? A THR 182 
48  1 Y 1 A GLU 181 ? A GLU 183 
49  1 Y 1 A GLU 182 ? A GLU 184 
50  1 Y 1 A SER 183 ? A SER 185 
51  1 Y 1 A PHE 184 ? A PHE 186 
52  1 Y 1 A THR 185 ? A THR 187 
53  1 Y 1 A ALA 186 ? A ALA 188 
54  1 Y 1 A VAL 187 ? A VAL 189 
55  1 Y 1 A MET 188 ? A MET 190 
56  1 Y 1 A THR 189 ? A THR 191 
57  1 Y 1 A THR 190 ? A THR 192 
58  1 Y 1 A ALA 191 ? A ALA 193 
59  1 Y 1 A ILE 192 ? A ILE 194 
60  1 Y 1 A SER 193 ? A SER 195 
61  1 Y 1 A LYS 194 ? A LYS 196 
62  1 Y 1 A THR 195 ? A THR 197 
63  1 Y 1 A LYS 196 ? A LYS 198 
64  1 Y 1 A THR 197 ? A THR 199 
65  1 Y 1 A LYS 198 ? A LYS 200 
66  1 Y 1 A GLU 199 ? A GLU 201 
67  1 Y 1 A SER 477 ? A SER 479 
68  1 Y 1 A GLU 478 ? A GLU 480 
69  1 Y 1 A VAL 479 ? A VAL 481 
70  1 Y 1 A ASN 480 ? A ASN 482 
71  1 Y 1 A ILE 481 ? A ILE 483 
72  1 Y 1 A VAL 482 ? A VAL 484 
73  1 Y 1 A ASN 483 ? A ASN 485 
74  1 Y 1 A PRO 484 ? A PRO 486 
75  1 Y 1 A PHE 485 ? A PHE 487 
76  1 Y 1 A ALA 486 ? A ALA 488 
77  1 Y 1 A LEU 487 ? A LEU 489 
78  1 Y 1 A GLU 488 ? A GLU 490 
79  1 Y 1 A SER 489 ? A SER 491 
80  1 Y 1 A THR 490 ? A THR 492 
81  1 Y 1 A ILE 491 ? A ILE 493 
82  1 Y 1 A LEU 492 ? A LEU 494 
83  1 Y 1 A ASP 493 ? A ASP 495 
84  1 Y 1 A ASN 494 ? A ASN 496 
85  1 Y 1 A GLU 495 ? A GLU 497 
86  1 Y 1 A ASP 496 ? A ASP 498 
87  1 Y 1 A SER 497 ? A SER 499 
88  1 Y 1 A ASP 498 ? A ASP 500 
89  1 Y 1 A THR 499 ? A THR 501 
90  1 Y 1 A LYS 500 ? A LYS 502 
91  1 Y 1 A LYS 501 ? A LYS 503 
92  1 Y 1 A SER 502 ? A SER 504 
93  1 Y 1 A TYR 503 ? A TYR 505 
94  1 Y 1 A VAL 504 ? A VAL 506 
95  1 Y 1 A ASN 505 ? A ASN 507 
96  1 Y 1 A GLY 506 ? A GLY 508 
97  1 Y 1 A GLY 507 ? A GLY 509 
98  1 Y 1 A PHE 508 ? A PHE 510 
99  1 Y 1 A ALA 509 ? A ALA 511 
100 1 Y 1 A VAL 510 ? A VAL 512 
101 1 Y 1 A ASP 511 ? A ASP 513 
102 1 Y 1 A LYS 512 ? A LYS 514 
103 1 Y 1 A SER 513 ? A SER 515 
104 1 Y 1 A ASP 514 ? A ASP 516 
105 1 Y 1 A THR 515 ? A THR 517 
106 1 Y 1 A ILE 516 ? A ILE 518 
107 1 Y 1 A SER 517 ? A SER 519 
108 1 Y 1 A PHE 518 ? A PHE 520 
109 1 Y 1 A THR 519 ? A THR 521 
110 1 Y 1 A GLN 520 ? A GLN 522 
111 1 Y 1 A THR 521 ? A THR 523 
112 1 Y 1 A SER 522 ? A SER 524 
113 1 Y 1 A GLN 523 ? A GLN 525 
114 1 Y 1 A PHE 524 ? A PHE 526 
# 
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 
HG  HG   HG N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
ILE N    N  N N 159 
ILE CA   C  N S 160 
ILE C    C  N N 161 
ILE O    O  N N 162 
ILE CB   C  N S 163 
ILE CG1  C  N N 164 
ILE CG2  C  N N 165 
ILE CD1  C  N N 166 
ILE OXT  O  N N 167 
ILE H    H  N N 168 
ILE H2   H  N N 169 
ILE HA   H  N N 170 
ILE HB   H  N N 171 
ILE HG12 H  N N 172 
ILE HG13 H  N N 173 
ILE HG21 H  N N 174 
ILE HG22 H  N N 175 
ILE HG23 H  N N 176 
ILE HD11 H  N N 177 
ILE HD12 H  N N 178 
ILE HD13 H  N N 179 
ILE HXT  H  N N 180 
LEU N    N  N N 181 
LEU CA   C  N S 182 
LEU C    C  N N 183 
LEU O    O  N N 184 
LEU CB   C  N N 185 
LEU CG   C  N N 186 
LEU CD1  C  N N 187 
LEU CD2  C  N N 188 
LEU OXT  O  N N 189 
LEU H    H  N N 190 
LEU H2   H  N N 191 
LEU HA   H  N N 192 
LEU HB2  H  N N 193 
LEU HB3  H  N N 194 
LEU HG   H  N N 195 
LEU HD11 H  N N 196 
LEU HD12 H  N N 197 
LEU HD13 H  N N 198 
LEU HD21 H  N N 199 
LEU HD22 H  N N 200 
LEU HD23 H  N N 201 
LEU HXT  H  N N 202 
LYS N    N  N N 203 
LYS CA   C  N S 204 
LYS C    C  N N 205 
LYS O    O  N N 206 
LYS CB   C  N N 207 
LYS CG   C  N N 208 
LYS CD   C  N N 209 
LYS CE   C  N N 210 
LYS NZ   N  N N 211 
LYS OXT  O  N N 212 
LYS H    H  N N 213 
LYS H2   H  N N 214 
LYS HA   H  N N 215 
LYS HB2  H  N N 216 
LYS HB3  H  N N 217 
LYS HG2  H  N N 218 
LYS HG3  H  N N 219 
LYS HD2  H  N N 220 
LYS HD3  H  N N 221 
LYS HE2  H  N N 222 
LYS HE3  H  N N 223 
LYS HZ1  H  N N 224 
LYS HZ2  H  N N 225 
LYS HZ3  H  N N 226 
LYS HXT  H  N N 227 
MET N    N  N N 228 
MET CA   C  N S 229 
MET C    C  N N 230 
MET O    O  N N 231 
MET CB   C  N N 232 
MET CG   C  N N 233 
MET SD   S  N N 234 
MET CE   C  N N 235 
MET OXT  O  N N 236 
MET H    H  N N 237 
MET H2   H  N N 238 
MET HA   H  N N 239 
MET HB2  H  N N 240 
MET HB3  H  N N 241 
MET HG2  H  N N 242 
MET HG3  H  N N 243 
MET HE1  H  N N 244 
MET HE2  H  N N 245 
MET HE3  H  N N 246 
MET HXT  H  N N 247 
NA  NA   NA N N 248 
PHE N    N  N N 249 
PHE CA   C  N S 250 
PHE C    C  N N 251 
PHE O    O  N N 252 
PHE CB   C  N N 253 
PHE CG   C  Y N 254 
PHE CD1  C  Y N 255 
PHE CD2  C  Y N 256 
PHE CE1  C  Y N 257 
PHE CE2  C  Y N 258 
PHE CZ   C  Y N 259 
PHE OXT  O  N N 260 
PHE H    H  N N 261 
PHE H2   H  N N 262 
PHE HA   H  N N 263 
PHE HB2  H  N N 264 
PHE HB3  H  N N 265 
PHE HD1  H  N N 266 
PHE HD2  H  N N 267 
PHE HE1  H  N N 268 
PHE HE2  H  N N 269 
PHE HZ   H  N N 270 
PHE HXT  H  N N 271 
PRO N    N  N N 272 
PRO CA   C  N S 273 
PRO C    C  N N 274 
PRO O    O  N N 275 
PRO CB   C  N N 276 
PRO CG   C  N N 277 
PRO CD   C  N N 278 
PRO OXT  O  N N 279 
PRO H    H  N N 280 
PRO HA   H  N N 281 
PRO HB2  H  N N 282 
PRO HB3  H  N N 283 
PRO HG2  H  N N 284 
PRO HG3  H  N N 285 
PRO HD2  H  N N 286 
PRO HD3  H  N N 287 
PRO HXT  H  N N 288 
SER N    N  N N 289 
SER CA   C  N S 290 
SER C    C  N N 291 
SER O    O  N N 292 
SER CB   C  N N 293 
SER OG   O  N N 294 
SER OXT  O  N N 295 
SER H    H  N N 296 
SER H2   H  N N 297 
SER HA   H  N N 298 
SER HB2  H  N N 299 
SER HB3  H  N N 300 
SER HG   H  N N 301 
SER HXT  H  N N 302 
THR N    N  N N 303 
THR CA   C  N S 304 
THR C    C  N N 305 
THR O    O  N N 306 
THR CB   C  N R 307 
THR OG1  O  N N 308 
THR CG2  C  N N 309 
THR OXT  O  N N 310 
THR H    H  N N 311 
THR H2   H  N N 312 
THR HA   H  N N 313 
THR HB   H  N N 314 
THR HG1  H  N N 315 
THR HG21 H  N N 316 
THR HG22 H  N N 317 
THR HG23 H  N N 318 
THR HXT  H  N N 319 
TRP N    N  N N 320 
TRP CA   C  N S 321 
TRP C    C  N N 322 
TRP O    O  N N 323 
TRP CB   C  N N 324 
TRP CG   C  Y N 325 
TRP CD1  C  Y N 326 
TRP CD2  C  Y N 327 
TRP NE1  N  Y N 328 
TRP CE2  C  Y N 329 
TRP CE3  C  Y N 330 
TRP CZ2  C  Y N 331 
TRP CZ3  C  Y N 332 
TRP CH2  C  Y N 333 
TRP OXT  O  N N 334 
TRP H    H  N N 335 
TRP H2   H  N N 336 
TRP HA   H  N N 337 
TRP HB2  H  N N 338 
TRP HB3  H  N N 339 
TRP HD1  H  N N 340 
TRP HE1  H  N N 341 
TRP HE3  H  N N 342 
TRP HZ2  H  N N 343 
TRP HZ3  H  N N 344 
TRP HH2  H  N N 345 
TRP HXT  H  N N 346 
TYR N    N  N N 347 
TYR CA   C  N S 348 
TYR C    C  N N 349 
TYR O    O  N N 350 
TYR CB   C  N N 351 
TYR CG   C  Y N 352 
TYR CD1  C  Y N 353 
TYR CD2  C  Y N 354 
TYR CE1  C  Y N 355 
TYR CE2  C  Y N 356 
TYR CZ   C  Y N 357 
TYR OH   O  N N 358 
TYR OXT  O  N N 359 
TYR H    H  N N 360 
TYR H2   H  N N 361 
TYR HA   H  N N 362 
TYR HB2  H  N N 363 
TYR HB3  H  N N 364 
TYR HD1  H  N N 365 
TYR HD2  H  N N 366 
TYR HE1  H  N N 367 
TYR HE2  H  N N 368 
TYR HH   H  N N 369 
TYR HXT  H  N N 370 
VAL N    N  N N 371 
VAL CA   C  N S 372 
VAL C    C  N N 373 
VAL O    O  N N 374 
VAL CB   C  N N 375 
VAL CG1  C  N N 376 
VAL CG2  C  N N 377 
VAL OXT  O  N N 378 
VAL H    H  N N 379 
VAL H2   H  N N 380 
VAL HA   H  N N 381 
VAL HB   H  N N 382 
VAL HG11 H  N N 383 
VAL HG12 H  N N 384 
VAL HG13 H  N N 385 
VAL HG21 H  N N 386 
VAL HG22 H  N N 387 
VAL HG23 H  N N 388 
VAL HXT  H  N N 389 
# 
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    2024-08-14 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9D69 
_em_admin.last_update        2025-01-22 
_em_admin.map_release_date   2025-01-22 
_em_admin.title              
;Human excitatory amino acid transporter 3 (EAAT3) with bound L-Cysteine in an intermediate outward facing state (slight upper position)
;
# 
_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         58.25 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
_em_particle_selection.details                  'This is the number of trimer particle from the image' 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   4180263 
_em_particle_selection.reference_model          ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? RELION    ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ?         ? 
MASKING                         ? 3  ? ? ? ?         ? 
'CTF CORRECTION'                ? 4  1 ? ? CTFFIND   ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ? 
'MODEL FITTING'                 ? 7  ? 1 ? Coot      ? 
OTHER                           ? 8  ? ? ? ?         ? 
'MODEL REFINEMENT'              ? 9  ? 1 ? PHENIX    ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? cryoSPARC 3 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC 3 
CLASSIFICATION                  ? 12 1 ? ? RELION    3 
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC 3 
'VOLUME SELECTION'              ? 14 1 1 1 ?         ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ?         ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ?         ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ?         ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ?         ? 
'CRYSTALLOGRAPHY MERGING'       ? 19 1 1 1 ?         ? 
# 
_em_specimen.concentration           5 
_em_specimen.details                 'This sample was monodisperse.' 
_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 
'Howard Hughes Medical Institute (HHMI)'                                                            'United States' ?           1 
'National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)' 'United States' R37NS085318 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8CV3 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9D69 
_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  
HG 
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASN A 1 19  ? 146.759 97.240  137.636 1.00 76.74  ? 17  ASN A N   1 
ATOM   2    C  CA  . ASN A 1 19  ? 148.056 97.326  136.976 1.00 75.54  ? 17  ASN A CA  1 
ATOM   3    C  C   . ASN A 1 19  ? 147.980 98.274  135.782 1.00 74.21  ? 17  ASN A C   1 
ATOM   4    O  O   . ASN A 1 19  ? 147.006 99.011  135.627 1.00 72.94  ? 17  ASN A O   1 
ATOM   5    C  CB  . ASN A 1 19  ? 148.523 95.936  136.534 1.00 74.72  ? 17  ASN A CB  1 
ATOM   6    C  CG  . ASN A 1 19  ? 147.528 95.247  135.620 1.00 71.24  ? 17  ASN A CG  1 
ATOM   7    O  OD1 . ASN A 1 19  ? 146.317 95.410  135.767 1.00 69.32  ? 17  ASN A OD1 1 
ATOM   8    N  ND2 . ASN A 1 19  ? 148.035 94.470  134.670 1.00 70.04  ? 17  ASN A ND2 1 
ATOM   9    N  N   . ASN A 1 20  ? 149.011 98.250  134.939 1.00 73.93  ? 18  ASN A N   1 
ATOM   10   C  CA  . ASN A 1 20  ? 149.112 99.128  133.774 1.00 74.49  ? 18  ASN A CA  1 
ATOM   11   C  C   . ASN A 1 20  ? 148.688 98.418  132.495 1.00 72.14  ? 18  ASN A C   1 
ATOM   12   O  O   . ASN A 1 20  ? 149.273 98.632  131.429 1.00 71.45  ? 18  ASN A O   1 
ATOM   13   C  CB  . ASN A 1 20  ? 150.532 99.671  133.643 1.00 75.27  ? 18  ASN A CB  1 
ATOM   14   C  CG  . ASN A 1 20  ? 151.579 98.576  133.640 1.00 80.35  ? 18  ASN A CG  1 
ATOM   15   O  OD1 . ASN A 1 20  ? 151.280 97.417  133.359 1.00 79.32  ? 18  ASN A OD1 1 
ATOM   16   N  ND2 . ASN A 1 20  ? 152.817 98.939  133.955 1.00 78.66  ? 18  ASN A ND2 1 
ATOM   17   N  N   . TRP A 1 21  ? 147.668 97.561  132.580 1.00 70.37  ? 19  TRP A N   1 
ATOM   18   C  CA  . TRP A 1 21  ? 147.227 96.811  131.409 1.00 73.16  ? 19  TRP A CA  1 
ATOM   19   C  C   . TRP A 1 21  ? 146.831 97.732  130.263 1.00 64.96  ? 19  TRP A C   1 
ATOM   20   O  O   . TRP A 1 21  ? 146.904 97.333  129.095 1.00 59.06  ? 19  TRP A O   1 
ATOM   21   C  CB  . TRP A 1 21  ? 146.053 95.905  131.781 1.00 68.16  ? 19  TRP A CB  1 
ATOM   22   C  CG  . TRP A 1 21  ? 144.756 96.642  131.906 1.00 68.33  ? 19  TRP A CG  1 
ATOM   23   C  CD1 . TRP A 1 21  ? 144.382 97.474  132.920 1.00 66.91  ? 19  TRP A CD1 1 
ATOM   24   C  CD2 . TRP A 1 21  ? 143.663 96.620  130.981 1.00 70.51  ? 19  TRP A CD2 1 
ATOM   25   N  NE1 . TRP A 1 21  ? 143.123 97.970  132.685 1.00 67.28  ? 19  TRP A NE1 1 
ATOM   26   C  CE2 . TRP A 1 21  ? 142.659 97.460  131.501 1.00 66.46  ? 19  TRP A CE2 1 
ATOM   27   C  CE3 . TRP A 1 21  ? 143.434 95.969  129.765 1.00 67.53  ? 19  TRP A CE3 1 
ATOM   28   C  CZ2 . TRP A 1 21  ? 141.446 97.668  130.848 1.00 62.06  ? 19  TRP A CZ2 1 
ATOM   29   C  CZ3 . TRP A 1 21  ? 142.229 96.177  129.118 1.00 67.50  ? 19  TRP A CZ3 1 
ATOM   30   C  CH2 . TRP A 1 21  ? 141.251 97.019  129.661 1.00 66.45  ? 19  TRP A CH2 1 
ATOM   31   N  N   . VAL A 1 22  ? 146.410 98.960  130.568 1.00 61.25  ? 20  VAL A N   1 
ATOM   32   C  CA  . VAL A 1 22  ? 146.011 99.883  129.510 1.00 64.35  ? 20  VAL A CA  1 
ATOM   33   C  C   . VAL A 1 22  ? 147.193 100.180 128.597 1.00 68.86  ? 20  VAL A C   1 
ATOM   34   O  O   . VAL A 1 22  ? 147.059 100.197 127.367 1.00 69.47  ? 20  VAL A O   1 
ATOM   35   C  CB  . VAL A 1 22  ? 145.422 101.174 130.111 1.00 65.17  ? 20  VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 22  ? 144.898 102.081 129.008 1.00 63.93  ? 20  VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 22  ? 144.310 100.850 131.100 1.00 66.16  ? 20  VAL A CG2 1 
ATOM   38   N  N   . LEU A 1 23  ? 148.367 100.424 129.181 1.00 70.51  ? 21  LEU A N   1 
ATOM   39   C  CA  . LEU A 1 23  ? 149.557 100.663 128.372 1.00 66.23  ? 21  LEU A CA  1 
ATOM   40   C  C   . LEU A 1 23  ? 149.976 99.409  127.615 1.00 66.36  ? 21  LEU A C   1 
ATOM   41   O  O   . LEU A 1 23  ? 150.365 99.486  126.445 1.00 68.01  ? 21  LEU A O   1 
ATOM   42   C  CB  . LEU A 1 23  ? 150.698 101.157 129.258 1.00 69.09  ? 21  LEU A CB  1 
ATOM   43   C  CG  . LEU A 1 23  ? 151.865 101.833 128.537 1.00 68.68  ? 21  LEU A CG  1 
ATOM   44   C  CD1 . LEU A 1 23  ? 151.469 103.205 128.016 1.00 63.90  ? 21  LEU A CD1 1 
ATOM   45   C  CD2 . LEU A 1 23  ? 153.056 101.931 129.474 1.00 70.38  ? 21  LEU A CD2 1 
ATOM   46   N  N   . LEU A 1 24  ? 149.911 98.245  128.265 1.00 65.00  ? 22  LEU A N   1 
ATOM   47   C  CA  . LEU A 1 24  ? 150.266 97.004  127.585 1.00 66.24  ? 22  LEU A CA  1 
ATOM   48   C  C   . LEU A 1 24  ? 149.300 96.704  126.448 1.00 60.85  ? 22  LEU A C   1 
ATOM   49   O  O   . LEU A 1 24  ? 149.719 96.294  125.359 1.00 59.96  ? 22  LEU A O   1 
ATOM   50   C  CB  . LEU A 1 24  ? 150.289 95.844  128.583 1.00 67.27  ? 22  LEU A CB  1 
ATOM   51   C  CG  . LEU A 1 24  ? 151.517 95.673  129.484 1.00 66.45  ? 22  LEU A CG  1 
ATOM   52   C  CD1 . LEU A 1 24  ? 152.826 95.689  128.700 1.00 64.23  ? 22  LEU A CD1 1 
ATOM   53   C  CD2 . LEU A 1 24  ? 151.531 96.746  130.559 1.00 63.86  ? 22  LEU A CD2 1 
ATOM   54   N  N   . SER A 1 25  ? 148.001 96.899  126.680 1.00 56.66  ? 23  SER A N   1 
ATOM   55   C  CA  . SER A 1 25  ? 147.017 96.594  125.647 1.00 58.59  ? 23  SER A CA  1 
ATOM   56   C  C   . SER A 1 25  ? 147.212 97.475  124.421 1.00 60.13  ? 23  SER A C   1 
ATOM   57   O  O   . SER A 1 25  ? 147.148 96.992  123.285 1.00 66.34  ? 23  SER A O   1 
ATOM   58   C  CB  . SER A 1 25  ? 145.605 96.759  126.206 1.00 61.07  ? 23  SER A CB  1 
ATOM   59   O  OG  . SER A 1 25  ? 145.475 97.983  126.905 1.00 62.55  ? 23  SER A OG  1 
ATOM   60   N  N   . THR A 1 26  ? 147.452 98.772  124.627 1.00 55.45  ? 24  THR A N   1 
ATOM   61   C  CA  . THR A 1 26  ? 147.620 99.671  123.490 1.00 55.12  ? 24  THR A CA  1 
ATOM   62   C  C   . THR A 1 26  ? 148.952 99.447  122.788 1.00 55.44  ? 24  THR A C   1 
ATOM   63   O  O   . THR A 1 26  ? 149.047 99.634  121.571 1.00 57.69  ? 24  THR A O   1 
ATOM   64   C  CB  . THR A 1 26  ? 147.494 101.128 123.943 1.00 56.74  ? 24  THR A CB  1 
ATOM   65   O  OG1 . THR A 1 26  ? 147.521 101.989 122.799 1.00 59.09  ? 24  THR A OG1 1 
ATOM   66   C  CG2 . THR A 1 26  ? 148.624 101.509 124.889 1.00 57.32  ? 24  THR A CG2 1 
ATOM   67   N  N   . VAL A 1 27  ? 149.989 99.054  123.530 1.00 60.59  ? 25  VAL A N   1 
ATOM   68   C  CA  . VAL A 1 27  ? 151.267 98.739  122.901 1.00 56.00  ? 25  VAL A CA  1 
ATOM   69   C  C   . VAL A 1 27  ? 151.149 97.464  122.075 1.00 59.36  ? 25  VAL A C   1 
ATOM   70   O  O   . VAL A 1 27  ? 151.718 97.361  120.983 1.00 61.12  ? 25  VAL A O   1 
ATOM   71   C  CB  . VAL A 1 27  ? 152.373 98.633  123.968 1.00 58.51  ? 25  VAL A CB  1 
ATOM   72   C  CG1 . VAL A 1 27  ? 153.607 97.921  123.417 1.00 60.25  ? 25  VAL A CG1 1 
ATOM   73   C  CG2 . VAL A 1 27  ? 152.743 100.015 124.477 1.00 58.98  ? 25  VAL A CG2 1 
ATOM   74   N  N   . ALA A 1 28  ? 150.416 96.471  122.584 1.00 56.08  ? 26  ALA A N   1 
ATOM   75   C  CA  . ALA A 1 28  ? 150.200 95.249  121.818 1.00 51.24  ? 26  ALA A CA  1 
ATOM   76   C  C   . ALA A 1 28  ? 149.431 95.527  120.535 1.00 54.72  ? 26  ALA A C   1 
ATOM   77   O  O   . ALA A 1 28  ? 149.589 94.802  119.547 1.00 55.68  ? 26  ALA A O   1 
ATOM   78   C  CB  . ALA A 1 28  ? 149.458 94.219  122.667 1.00 53.67  ? 26  ALA A CB  1 
ATOM   79   N  N   . ALA A 1 29  ? 148.591 96.564  120.531 1.00 56.21  ? 27  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 29  ? 147.861 96.918  119.319 1.00 54.28  ? 27  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 29  ? 148.811 97.362  118.215 1.00 53.80  ? 27  ALA A C   1 
ATOM   82   O  O   . ALA A 1 29  ? 148.585 97.068  117.036 1.00 54.30  ? 27  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 29  ? 146.843 98.015  119.624 1.00 48.47  ? 27  ALA A CB  1 
ATOM   84   N  N   . VAL A 1 30  ? 149.876 98.081  118.575 1.00 48.39  ? 28  VAL A N   1 
ATOM   85   C  CA  . VAL A 1 30  ? 150.841 98.530  117.576 1.00 49.03  ? 28  VAL A CA  1 
ATOM   86   C  C   . VAL A 1 30  ? 151.509 97.332  116.914 1.00 52.68  ? 28  VAL A C   1 
ATOM   87   O  O   . VAL A 1 30  ? 151.655 97.278  115.688 1.00 58.63  ? 28  VAL A O   1 
ATOM   88   C  CB  . VAL A 1 30  ? 151.880 99.467  118.218 1.00 54.79  ? 28  VAL A CB  1 
ATOM   89   C  CG1 . VAL A 1 30  ? 152.978 99.828  117.221 1.00 53.16  ? 28  VAL A CG1 1 
ATOM   90   C  CG2 . VAL A 1 30  ? 151.210 100.716 118.743 1.00 55.72  ? 28  VAL A CG2 1 
ATOM   91   N  N   . VAL A 1 31  ? 151.932 96.356  117.717 1.00 52.96  ? 29  VAL A N   1 
ATOM   92   C  CA  . VAL A 1 31  ? 152.576 95.171  117.161 1.00 55.12  ? 29  VAL A CA  1 
ATOM   93   C  C   . VAL A 1 31  ? 151.586 94.385  116.310 1.00 55.93  ? 29  VAL A C   1 
ATOM   94   O  O   . VAL A 1 31  ? 151.906 93.947  115.199 1.00 55.59  ? 29  VAL A O   1 
ATOM   95   C  CB  . VAL A 1 31  ? 153.169 94.311  118.292 1.00 55.04  ? 29  VAL A CB  1 
ATOM   96   C  CG1 . VAL A 1 31  ? 153.510 92.905  117.800 1.00 53.62  ? 29  VAL A CG1 1 
ATOM   97   C  CG2 . VAL A 1 31  ? 154.396 94.988  118.875 1.00 55.14  ? 29  VAL A CG2 1 
ATOM   98   N  N   . LEU A 1 32  ? 150.368 94.193  116.818 1.00 54.23  ? 30  LEU A N   1 
ATOM   99   C  CA  . LEU A 1 32  ? 149.351 93.490  116.044 1.00 53.35  ? 30  LEU A CA  1 
ATOM   100  C  C   . LEU A 1 32  ? 148.892 94.323  114.854 1.00 50.38  ? 30  LEU A C   1 
ATOM   101  O  O   . LEU A 1 32  ? 148.597 93.778  113.785 1.00 50.69  ? 30  LEU A O   1 
ATOM   102  C  CB  . LEU A 1 32  ? 148.165 93.137  116.941 1.00 54.74  ? 30  LEU A CB  1 
ATOM   103  C  CG  . LEU A 1 32  ? 148.402 91.985  117.918 1.00 54.81  ? 30  LEU A CG  1 
ATOM   104  C  CD1 . LEU A 1 32  ? 147.406 92.043  119.063 1.00 52.62  ? 30  LEU A CD1 1 
ATOM   105  C  CD2 . LEU A 1 32  ? 148.320 90.648  117.200 1.00 53.34  ? 30  LEU A CD2 1 
ATOM   106  N  N   . GLY A 1 33  ? 148.818 95.644  115.023 1.00 51.30  ? 31  GLY A N   1 
ATOM   107  C  CA  . GLY A 1 33  ? 148.402 96.494  113.919 1.00 51.89  ? 31  GLY A CA  1 
ATOM   108  C  C   . GLY A 1 33  ? 149.380 96.462  112.762 1.00 55.99  ? 31  GLY A C   1 
ATOM   109  O  O   . GLY A 1 33  ? 148.986 96.334  111.601 1.00 56.71  ? 31  GLY A O   1 
ATOM   110  N  N   . ILE A 1 34  ? 150.674 96.581  113.064 1.00 58.75  ? 32  ILE A N   1 
ATOM   111  C  CA  . ILE A 1 34  ? 151.685 96.526  112.014 1.00 50.61  ? 32  ILE A CA  1 
ATOM   112  C  C   . ILE A 1 34  ? 151.712 95.142  111.378 1.00 56.82  ? 32  ILE A C   1 
ATOM   113  O  O   . ILE A 1 34  ? 151.789 95.010  110.151 1.00 63.22  ? 32  ILE A O   1 
ATOM   114  C  CB  . ILE A 1 34  ? 153.061 96.925  112.579 1.00 54.56  ? 32  ILE A CB  1 
ATOM   115  C  CG1 . ILE A 1 34  ? 153.097 98.426  112.869 1.00 58.94  ? 32  ILE A CG1 1 
ATOM   116  C  CG2 . ILE A 1 34  ? 154.180 96.564  111.607 1.00 59.45  ? 32  ILE A CG2 1 
ATOM   117  C  CD1 . ILE A 1 34  ? 154.194 98.836  113.823 1.00 55.21  ? 32  ILE A CD1 1 
ATOM   118  N  N   . THR A 1 35  ? 151.655 94.091  112.197 1.00 56.82  ? 33  THR A N   1 
ATOM   119  C  CA  . THR A 1 35  ? 151.652 92.736  111.656 1.00 55.77  ? 33  THR A CA  1 
ATOM   120  C  C   . THR A 1 35  ? 150.416 92.495  110.799 1.00 52.36  ? 33  THR A C   1 
ATOM   121  O  O   . THR A 1 35  ? 150.507 91.940  109.699 1.00 50.61  ? 33  THR A O   1 
ATOM   122  C  CB  . THR A 1 35  ? 151.722 91.719  112.796 1.00 57.18  ? 33  THR A CB  1 
ATOM   123  O  OG1 . THR A 1 35  ? 152.894 91.960  113.583 1.00 61.34  ? 33  THR A OG1 1 
ATOM   124  C  CG2 . THR A 1 35  ? 151.768 90.297  112.252 1.00 56.23  ? 33  THR A CG2 1 
ATOM   125  N  N   . THR A 1 36  ? 149.246 92.910  111.288 1.00 56.35  ? 34  THR A N   1 
ATOM   126  C  CA  . THR A 1 36  ? 148.018 92.728  110.523 1.00 54.21  ? 34  THR A CA  1 
ATOM   127  C  C   . THR A 1 36  ? 148.063 93.521  109.223 1.00 57.84  ? 34  THR A C   1 
ATOM   128  O  O   . THR A 1 36  ? 147.721 93.003  108.153 1.00 60.49  ? 34  THR A O   1 
ATOM   129  C  CB  . THR A 1 36  ? 146.811 93.148  111.364 1.00 55.82  ? 34  THR A CB  1 
ATOM   130  O  OG1 . THR A 1 36  ? 146.786 92.392  112.580 1.00 60.40  ? 34  THR A OG1 1 
ATOM   131  C  CG2 . THR A 1 36  ? 145.512 92.919  110.603 1.00 51.44  ? 34  THR A CG2 1 
ATOM   132  N  N   . GLY A 1 37  ? 148.489 94.782  109.296 1.00 58.25  ? 35  GLY A N   1 
ATOM   133  C  CA  . GLY A 1 37  ? 148.487 95.619  108.109 1.00 54.07  ? 35  GLY A CA  1 
ATOM   134  C  C   . GLY A 1 37  ? 149.418 95.107  107.027 1.00 52.93  ? 35  GLY A C   1 
ATOM   135  O  O   . GLY A 1 37  ? 149.062 95.089  105.848 1.00 59.18  ? 35  GLY A O   1 
ATOM   136  N  N   . VAL A 1 38  ? 150.623 94.684  107.411 1.00 54.19  ? 36  VAL A N   1 
ATOM   137  C  CA  . VAL A 1 38  ? 151.585 94.200  106.425 1.00 56.46  ? 36  VAL A CA  1 
ATOM   138  C  C   . VAL A 1 38  ? 151.085 92.909  105.789 1.00 61.60  ? 36  VAL A C   1 
ATOM   139  O  O   . VAL A 1 38  ? 151.084 92.762  104.561 1.00 64.67  ? 36  VAL A O   1 
ATOM   140  C  CB  . VAL A 1 38  ? 152.968 94.013  107.076 1.00 56.35  ? 36  VAL A CB  1 
ATOM   141  C  CG1 . VAL A 1 38  ? 153.929 93.307  106.124 1.00 58.26  ? 36  VAL A CG1 1 
ATOM   142  C  CG2 . VAL A 1 38  ? 153.535 95.351  107.508 1.00 53.08  ? 36  VAL A CG2 1 
ATOM   143  N  N   . LEU A 1 39  ? 150.652 91.954  106.614 1.00 64.86  ? 37  LEU A N   1 
ATOM   144  C  CA  . LEU A 1 39  ? 150.169 90.685  106.079 1.00 63.19  ? 37  LEU A CA  1 
ATOM   145  C  C   . LEU A 1 39  ? 148.911 90.881  105.244 1.00 61.03  ? 37  LEU A C   1 
ATOM   146  O  O   . LEU A 1 39  ? 148.768 90.279  104.173 1.00 59.01  ? 37  LEU A O   1 
ATOM   147  C  CB  . LEU A 1 39  ? 149.909 89.703  107.220 1.00 64.98  ? 37  LEU A CB  1 
ATOM   148  C  CG  . LEU A 1 39  ? 151.077 88.776  107.556 1.00 64.54  ? 37  LEU A CG  1 
ATOM   149  C  CD1 . LEU A 1 39  ? 152.221 89.558  108.176 1.00 63.64  ? 37  LEU A CD1 1 
ATOM   150  C  CD2 . LEU A 1 39  ? 150.621 87.665  108.484 1.00 65.50  ? 37  LEU A CD2 1 
ATOM   151  N  N   . VAL A 1 40  ? 147.984 91.715  105.717 1.00 57.93  ? 38  VAL A N   1 
ATOM   152  C  CA  . VAL A 1 40  ? 146.769 91.979  104.953 1.00 58.06  ? 38  VAL A CA  1 
ATOM   153  C  C   . VAL A 1 40  ? 147.111 92.656  103.632 1.00 62.60  ? 38  VAL A C   1 
ATOM   154  O  O   . VAL A 1 40  ? 146.564 92.309  102.579 1.00 63.51  ? 38  VAL A O   1 
ATOM   155  C  CB  . VAL A 1 40  ? 145.789 92.823  105.791 1.00 59.95  ? 38  VAL A CB  1 
ATOM   156  C  CG1 . VAL A 1 40  ? 144.704 93.442  104.916 1.00 59.64  ? 38  VAL A CG1 1 
ATOM   157  C  CG2 . VAL A 1 40  ? 145.165 91.973  106.884 1.00 62.04  ? 38  VAL A CG2 1 
ATOM   158  N  N   . ARG A 1 41  ? 148.019 93.633  103.666 1.00 70.46  ? 39  ARG A N   1 
ATOM   159  C  CA  . ARG A 1 41  ? 148.380 94.352  102.449 1.00 69.41  ? 39  ARG A CA  1 
ATOM   160  C  C   . ARG A 1 41  ? 149.074 93.445  101.441 1.00 72.44  ? 39  ARG A C   1 
ATOM   161  O  O   . ARG A 1 41  ? 148.933 93.645  100.230 1.00 69.53  ? 39  ARG A O   1 
ATOM   162  C  CB  . ARG A 1 41  ? 149.273 95.546  102.799 1.00 70.37  ? 39  ARG A CB  1 
ATOM   163  C  CG  . ARG A 1 41  ? 150.288 95.930  101.733 1.00 71.20  ? 39  ARG A CG  1 
ATOM   164  C  CD  . ARG A 1 41  ? 151.090 97.149  102.153 1.00 68.75  ? 39  ARG A CD  1 
ATOM   165  N  NE  . ARG A 1 41  ? 152.207 97.399  101.251 1.00 73.29  ? 39  ARG A NE  1 
ATOM   166  C  CZ  . ARG A 1 41  ? 152.083 97.866  100.016 1.00 74.79  ? 39  ARG A CZ  1 
ATOM   167  N  NH1 . ARG A 1 41  ? 150.899 98.159  99.503  1.00 73.82  ? 39  ARG A NH1 1 
ATOM   168  N  NH2 . ARG A 1 41  ? 153.174 98.044  99.277  1.00 73.33  ? 39  ARG A NH2 1 
ATOM   169  N  N   . GLU A 1 42  ? 149.826 92.452  101.916 1.00 72.55  ? 40  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 42  ? 150.588 91.579  101.032 1.00 73.81  ? 40  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 42  ? 149.776 90.382  100.552 1.00 72.22  ? 40  GLU A C   1 
ATOM   172  O  O   . GLU A 1 42  ? 149.852 90.015  99.375  1.00 71.85  ? 40  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 42  ? 151.854 91.094  101.748 1.00 70.88  ? 40  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 42  ? 152.701 90.089  100.969 1.00 72.95  ? 40  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 42  ? 152.706 90.336  99.471  1.00 77.05  ? 40  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 42  ? 152.775 91.513  99.058  1.00 75.45  ? 40  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 42  ? 152.642 89.351  98.706  1.00 75.30  ? 40  GLU A OE2 1 
ATOM   178  N  N   . HIS A 1 43  ? 148.991 89.770  101.435 1.00 69.96  ? 41  HIS A N   1 
ATOM   179  C  CA  . HIS A 1 43  ? 148.274 88.543  101.124 1.00 70.36  ? 41  HIS A CA  1 
ATOM   180  C  C   . HIS A 1 43  ? 146.880 88.793  100.563 1.00 69.62  ? 41  HIS A C   1 
ATOM   181  O  O   . HIS A 1 43  ? 146.129 87.834  100.358 1.00 70.32  ? 41  HIS A O   1 
ATOM   182  C  CB  . HIS A 1 43  ? 148.179 87.664  102.373 1.00 72.78  ? 41  HIS A CB  1 
ATOM   183  C  CG  . HIS A 1 43  ? 149.504 87.162  102.856 1.00 75.56  ? 41  HIS A CG  1 
ATOM   184  N  ND1 . HIS A 1 43  ? 150.676 87.377  102.164 1.00 73.66  ? 41  HIS A ND1 1 
ATOM   185  C  CD2 . HIS A 1 43  ? 149.842 86.453  103.958 1.00 73.04  ? 41  HIS A CD2 1 
ATOM   186  C  CE1 . HIS A 1 43  ? 151.680 86.824  102.820 1.00 72.38  ? 41  HIS A CE1 1 
ATOM   187  N  NE2 . HIS A 1 43  ? 151.201 86.256  103.912 1.00 73.48  ? 41  HIS A NE2 1 
ATOM   188  N  N   . SER A 1 44  ? 146.517 90.048  100.311 1.00 68.42  ? 42  SER A N   1 
ATOM   189  C  CA  . SER A 1 44  ? 145.213 90.362  99.749  1.00 68.82  ? 42  SER A CA  1 
ATOM   190  C  C   . SER A 1 44  ? 145.333 91.611  98.892  1.00 69.74  ? 42  SER A C   1 
ATOM   191  O  O   . SER A 1 44  ? 146.282 92.388  99.019  1.00 71.16  ? 42  SER A O   1 
ATOM   192  C  CB  . SER A 1 44  ? 144.162 90.566  100.845 1.00 66.70  ? 42  SER A CB  1 
ATOM   193  O  OG  . SER A 1 44  ? 144.461 91.707  101.628 1.00 65.01  ? 42  SER A OG  1 
ATOM   194  N  N   . ASN A 1 45  ? 144.355 91.791  98.010  1.00 69.87  ? 43  ASN A N   1 
ATOM   195  C  CA  . ASN A 1 45  ? 144.248 92.975  97.161  1.00 68.68  ? 43  ASN A CA  1 
ATOM   196  C  C   . ASN A 1 45  ? 142.875 93.585  97.424  1.00 68.35  ? 43  ASN A C   1 
ATOM   197  O  O   . ASN A 1 45  ? 141.909 93.310  96.708  1.00 69.09  ? 43  ASN A O   1 
ATOM   198  C  CB  . ASN A 1 45  ? 144.443 92.618  95.688  1.00 68.67  ? 43  ASN A CB  1 
ATOM   199  C  CG  . ASN A 1 45  ? 143.537 91.488  95.237  1.00 70.88  ? 43  ASN A CG  1 
ATOM   200  O  OD1 . ASN A 1 45  ? 143.551 90.399  95.810  1.00 69.39  ? 43  ASN A OD1 1 
ATOM   201  N  ND2 . ASN A 1 45  ? 142.743 91.742  94.203  1.00 71.87  ? 43  ASN A ND2 1 
ATOM   202  N  N   . LEU A 1 46  ? 142.797 94.419  98.456  1.00 62.48  ? 44  LEU A N   1 
ATOM   203  C  CA  . LEU A 1 46  ? 141.531 95.014  98.857  1.00 65.45  ? 44  LEU A CA  1 
ATOM   204  C  C   . LEU A 1 46  ? 141.202 96.204  97.965  1.00 60.87  ? 44  LEU A C   1 
ATOM   205  O  O   . LEU A 1 46  ? 142.052 97.065  97.723  1.00 60.14  ? 44  LEU A O   1 
ATOM   206  C  CB  . LEU A 1 46  ? 141.593 95.449  100.321 1.00 66.07  ? 44  LEU A CB  1 
ATOM   207  C  CG  . LEU A 1 46  ? 141.967 94.370  101.341 1.00 61.35  ? 44  LEU A CG  1 
ATOM   208  C  CD1 . LEU A 1 46  ? 141.926 94.936  102.750 1.00 60.11  ? 44  LEU A CD1 1 
ATOM   209  C  CD2 . LEU A 1 46  ? 141.052 93.161  101.229 1.00 64.01  ? 44  LEU A CD2 1 
ATOM   210  N  N   . SER A 1 47  ? 139.967 96.248  97.476  1.00 54.33  ? 45  SER A N   1 
ATOM   211  C  CA  . SER A 1 47  ? 139.523 97.375  96.675  1.00 56.22  ? 45  SER A CA  1 
ATOM   212  C  C   . SER A 1 47  ? 139.411 98.624  97.542  1.00 55.51  ? 45  SER A C   1 
ATOM   213  O  O   . SER A 1 47  ? 139.320 98.554  98.771  1.00 63.21  ? 45  SER A O   1 
ATOM   214  C  CB  . SER A 1 47  ? 138.178 97.069  96.017  1.00 63.76  ? 45  SER A CB  1 
ATOM   215  O  OG  . SER A 1 47  ? 137.167 96.876  96.990  1.00 62.37  ? 45  SER A OG  1 
ATOM   216  N  N   . THR A 1 48  ? 139.421 99.784  96.882  1.00 50.78  ? 46  THR A N   1 
ATOM   217  C  CA  . THR A 1 48  ? 139.370 101.048 97.610  1.00 52.18  ? 46  THR A CA  1 
ATOM   218  C  C   . THR A 1 48  ? 138.212 101.067 98.598  1.00 53.85  ? 46  THR A C   1 
ATOM   219  O  O   . THR A 1 48  ? 138.341 101.586 99.712  1.00 51.52  ? 46  THR A O   1 
ATOM   220  C  CB  . THR A 1 48  ? 139.251 102.214 96.629  1.00 57.02  ? 46  THR A CB  1 
ATOM   221  O  OG1 . THR A 1 48  ? 140.245 102.084 95.606  1.00 60.64  ? 46  THR A OG1 1 
ATOM   222  C  CG2 . THR A 1 48  ? 139.439 103.542 97.348  1.00 57.06  ? 46  THR A CG2 1 
ATOM   223  N  N   . LEU A 1 49  ? 137.067 100.509 98.204  1.00 57.14  ? 47  LEU A N   1 
ATOM   224  C  CA  . LEU A 1 49  ? 135.942 100.405 99.126  1.00 55.45  ? 47  LEU A CA  1 
ATOM   225  C  C   . LEU A 1 49  ? 136.219 99.381  100.219 1.00 54.00  ? 47  LEU A C   1 
ATOM   226  O  O   . LEU A 1 49  ? 135.861 99.595  101.382 1.00 51.97  ? 47  LEU A O   1 
ATOM   227  C  CB  . LEU A 1 49  ? 134.673 100.038 98.357  1.00 51.87  ? 47  LEU A CB  1 
ATOM   228  C  CG  . LEU A 1 49  ? 133.368 100.090 99.149  1.00 51.01  ? 47  LEU A CG  1 
ATOM   229  C  CD1 . LEU A 1 49  ? 132.974 101.528 99.446  1.00 50.97  ? 47  LEU A CD1 1 
ATOM   230  C  CD2 . LEU A 1 49  ? 132.265 99.373  98.391  1.00 57.02  ? 47  LEU A CD2 1 
ATOM   231  N  N   . GLU A 1 50  ? 136.854 98.262  99.865  1.00 58.04  ? 48  GLU A N   1 
ATOM   232  C  CA  . GLU A 1 50  ? 137.142 97.231  100.858 1.00 52.19  ? 48  GLU A CA  1 
ATOM   233  C  C   . GLU A 1 50  ? 138.146 97.725  101.892 1.00 56.34  ? 48  GLU A C   1 
ATOM   234  O  O   . GLU A 1 50  ? 138.044 97.384  103.075 1.00 62.89  ? 48  GLU A O   1 
ATOM   235  C  CB  . GLU A 1 50  ? 137.663 95.970  100.170 1.00 52.86  ? 48  GLU A CB  1 
ATOM   236  C  CG  . GLU A 1 50  ? 136.685 94.809  100.188 1.00 62.73  ? 48  GLU A CG  1 
ATOM   237  C  CD  . GLU A 1 50  ? 137.154 93.639  99.346  1.00 63.38  ? 48  GLU A CD  1 
ATOM   238  O  OE1 . GLU A 1 50  ? 137.824 93.875  98.319  1.00 59.88  ? 48  GLU A OE1 1 
ATOM   239  O  OE2 . GLU A 1 50  ? 136.854 92.483  99.711  1.00 63.41  ? 48  GLU A OE2 1 
ATOM   240  N  N   . LYS A 1 51  ? 139.129 98.520  101.464 1.00 55.89  ? 49  LYS A N   1 
ATOM   241  C  CA  . LYS A 1 51  ? 140.099 99.062  102.409 1.00 48.75  ? 49  LYS A CA  1 
ATOM   242  C  C   . LYS A 1 51  ? 139.424 99.970  103.427 1.00 54.12  ? 49  LYS A C   1 
ATOM   243  O  O   . LYS A 1 51  ? 139.804 99.988  104.603 1.00 56.25  ? 49  LYS A O   1 
ATOM   244  C  CB  . LYS A 1 51  ? 141.194 99.822  101.661 1.00 53.79  ? 49  LYS A CB  1 
ATOM   245  C  CG  . LYS A 1 51  ? 142.187 98.929  100.941 1.00 50.66  ? 49  LYS A CG  1 
ATOM   246  C  CD  . LYS A 1 51  ? 143.166 99.742  100.115 1.00 54.66  ? 49  LYS A CD  1 
ATOM   247  C  CE  . LYS A 1 51  ? 144.268 98.867  99.541  1.00 56.75  ? 49  LYS A CE  1 
ATOM   248  N  NZ  . LYS A 1 51  ? 145.259 99.653  98.755  1.00 57.22  ? 49  LYS A NZ  1 
ATOM   249  N  N   . PHE A 1 52  ? 138.425 100.740 102.992 1.00 54.10  ? 50  PHE A N   1 
ATOM   250  C  CA  . PHE A 1 52  ? 137.732 101.635 103.913 1.00 51.54  ? 50  PHE A CA  1 
ATOM   251  C  C   . PHE A 1 52  ? 136.998 100.855 104.995 1.00 47.83  ? 50  PHE A C   1 
ATOM   252  O  O   . PHE A 1 52  ? 137.040 101.225 106.174 1.00 50.38  ? 50  PHE A O   1 
ATOM   253  C  CB  . PHE A 1 52  ? 136.759 102.526 103.144 1.00 47.95  ? 50  PHE A CB  1 
ATOM   254  C  CG  . PHE A 1 52  ? 136.057 103.537 104.003 1.00 49.24  ? 50  PHE A CG  1 
ATOM   255  C  CD1 . PHE A 1 52  ? 134.876 103.216 104.651 1.00 47.93  ? 50  PHE A CD1 1 
ATOM   256  C  CD2 . PHE A 1 52  ? 136.577 104.809 104.162 1.00 47.88  ? 50  PHE A CD2 1 
ATOM   257  C  CE1 . PHE A 1 52  ? 134.230 104.142 105.440 1.00 50.21  ? 50  PHE A CE1 1 
ATOM   258  C  CE2 . PHE A 1 52  ? 135.934 105.740 104.950 1.00 47.17  ? 50  PHE A CE2 1 
ATOM   259  C  CZ  . PHE A 1 52  ? 134.759 105.406 105.591 1.00 49.15  ? 50  PHE A CZ  1 
ATOM   260  N  N   . TYR A 1 53  ? 136.314 99.775  104.617 1.00 38.03  ? 51  TYR A N   1 
ATOM   261  C  CA  . TYR A 1 53  ? 135.576 98.996  105.604 1.00 36.70  ? 51  TYR A CA  1 
ATOM   262  C  C   . TYR A 1 53  ? 136.512 98.261  106.551 1.00 44.50  ? 51  TYR A C   1 
ATOM   263  O  O   . TYR A 1 53  ? 136.138 97.982  107.695 1.00 52.82  ? 51  TYR A O   1 
ATOM   264  C  CB  . TYR A 1 53  ? 134.646 98.004  104.905 1.00 47.85  ? 51  TYR A CB  1 
ATOM   265  C  CG  . TYR A 1 53  ? 133.427 98.636  104.271 1.00 51.53  ? 51  TYR A CG  1 
ATOM   266  C  CD1 . TYR A 1 53  ? 132.683 99.593  104.947 1.00 49.87  ? 51  TYR A CD1 1 
ATOM   267  C  CD2 . TYR A 1 53  ? 133.017 98.272  102.997 1.00 46.89  ? 51  TYR A CD2 1 
ATOM   268  C  CE1 . TYR A 1 53  ? 131.573 100.171 104.373 1.00 48.70  ? 51  TYR A CE1 1 
ATOM   269  C  CE2 . TYR A 1 53  ? 131.906 98.845  102.414 1.00 44.31  ? 51  TYR A CE2 1 
ATOM   270  C  CZ  . TYR A 1 53  ? 131.188 99.795  103.107 1.00 50.58  ? 51  TYR A CZ  1 
ATOM   271  O  OH  . TYR A 1 53  ? 130.078 100.371 102.533 1.00 54.62  ? 51  TYR A OH  1 
ATOM   272  N  N   . PHE A 1 54  ? 137.725 97.938  106.101 1.00 46.24  ? 52  PHE A N   1 
ATOM   273  C  CA  . PHE A 1 54  ? 138.678 97.266  106.977 1.00 43.03  ? 52  PHE A CA  1 
ATOM   274  C  C   . PHE A 1 54  ? 139.040 98.144  108.167 1.00 44.82  ? 52  PHE A C   1 
ATOM   275  O  O   . PHE A 1 54  ? 139.146 97.657  109.298 1.00 54.27  ? 52  PHE A O   1 
ATOM   276  C  CB  . PHE A 1 54  ? 139.934 96.886  106.196 1.00 48.99  ? 52  PHE A CB  1 
ATOM   277  C  CG  . PHE A 1 54  ? 140.975 96.197  107.026 1.00 47.44  ? 52  PHE A CG  1 
ATOM   278  C  CD1 . PHE A 1 54  ? 140.882 94.843  107.291 1.00 47.14  ? 52  PHE A CD1 1 
ATOM   279  C  CD2 . PHE A 1 54  ? 142.043 96.904  107.547 1.00 48.95  ? 52  PHE A CD2 1 
ATOM   280  C  CE1 . PHE A 1 54  ? 141.837 94.208  108.057 1.00 47.35  ? 52  PHE A CE1 1 
ATOM   281  C  CE2 . PHE A 1 54  ? 143.000 96.273  108.314 1.00 52.13  ? 52  PHE A CE2 1 
ATOM   282  C  CZ  . PHE A 1 54  ? 142.897 94.924  108.569 1.00 52.50  ? 52  PHE A CZ  1 
ATOM   283  N  N   . ALA A 1 55  ? 139.232 99.441  107.933 1.00 35.33  ? 53  ALA A N   1 
ATOM   284  C  CA  . ALA A 1 55  ? 139.616 100.377 108.977 1.00 35.42  ? 53  ALA A CA  1 
ATOM   285  C  C   . ALA A 1 55  ? 138.415 100.986 109.689 1.00 38.45  ? 53  ALA A C   1 
ATOM   286  O  O   . ALA A 1 55  ? 138.564 102.005 110.371 1.00 44.87  ? 53  ALA A O   1 
ATOM   287  C  CB  . ALA A 1 55  ? 140.491 101.487 108.393 1.00 36.57  ? 53  ALA A CB  1 
ATOM   288  N  N   . PHE A 1 56  ? 137.232 100.391 109.543 1.00 37.86  ? 54  PHE A N   1 
ATOM   289  C  CA  . PHE A 1 56  ? 136.052 100.938 110.205 1.00 34.27  ? 54  PHE A CA  1 
ATOM   290  C  C   . PHE A 1 56  ? 136.191 100.975 111.720 1.00 39.29  ? 54  PHE A C   1 
ATOM   291  O  O   . PHE A 1 56  ? 135.819 102.000 112.318 1.00 44.73  ? 54  PHE A O   1 
ATOM   292  C  CB  . PHE A 1 56  ? 134.808 100.140 109.799 1.00 30.90  ? 54  PHE A CB  1 
ATOM   293  C  CG  . PHE A 1 56  ? 133.556 100.585 110.495 1.00 32.51  ? 54  PHE A CG  1 
ATOM   294  C  CD1 . PHE A 1 56  ? 132.981 101.807 110.200 1.00 30.84  ? 54  PHE A CD1 1 
ATOM   295  C  CD2 . PHE A 1 56  ? 132.959 99.785  111.452 1.00 39.27  ? 54  PHE A CD2 1 
ATOM   296  C  CE1 . PHE A 1 56  ? 131.835 102.218 110.842 1.00 31.76  ? 54  PHE A CE1 1 
ATOM   297  C  CE2 . PHE A 1 56  ? 131.813 100.194 112.095 1.00 30.47  ? 54  PHE A CE2 1 
ATOM   298  C  CZ  . PHE A 1 56  ? 131.251 101.411 111.789 1.00 31.45  ? 54  PHE A CZ  1 
ATOM   299  N  N   . PRO A 1 57  ? 136.686 99.936  112.397 1.00 40.08  ? 55  PRO A N   1 
ATOM   300  C  CA  . PRO A 1 57  ? 136.863 100.048 113.853 1.00 33.15  ? 55  PRO A CA  1 
ATOM   301  C  C   . PRO A 1 57  ? 137.748 101.212 114.253 1.00 32.54  ? 55  PRO A C   1 
ATOM   302  O  O   . PRO A 1 57  ? 137.523 101.818 115.307 1.00 38.55  ? 55  PRO A O   1 
ATOM   303  C  CB  . PRO A 1 57  ? 137.490 98.701  114.234 1.00 30.58  ? 55  PRO A CB  1 
ATOM   304  C  CG  . PRO A 1 57  ? 137.075 97.772  113.153 1.00 36.01  ? 55  PRO A CG  1 
ATOM   305  C  CD  . PRO A 1 57  ? 137.036 98.593  111.905 1.00 34.78  ? 55  PRO A CD  1 
ATOM   306  N  N   . GLY A 1 58  ? 138.756 101.538 113.445 1.00 30.32  ? 56  GLY A N   1 
ATOM   307  C  CA  . GLY A 1 58  ? 139.535 102.737 113.700 1.00 31.05  ? 56  GLY A CA  1 
ATOM   308  C  C   . GLY A 1 58  ? 138.733 104.005 113.484 1.00 33.20  ? 56  GLY A C   1 
ATOM   309  O  O   . GLY A 1 58  ? 138.908 104.990 114.204 1.00 40.50  ? 56  GLY A O   1 
ATOM   310  N  N   . GLU A 1 59  ? 137.846 104.002 112.487 1.00 37.40  ? 57  GLU A N   1 
ATOM   311  C  CA  . GLU A 1 59  ? 137.016 105.174 112.231 1.00 32.05  ? 57  GLU A CA  1 
ATOM   312  C  C   . GLU A 1 59  ? 136.134 105.495 113.429 1.00 26.70  ? 57  GLU A C   1 
ATOM   313  O  O   . GLU A 1 59  ? 135.982 106.663 113.802 1.00 35.69  ? 57  GLU A O   1 
ATOM   314  C  CB  . GLU A 1 59  ? 136.160 104.946 110.985 1.00 34.29  ? 57  GLU A CB  1 
ATOM   315  C  CG  . GLU A 1 59  ? 135.059 105.976 110.785 1.00 43.11  ? 57  GLU A CG  1 
ATOM   316  C  CD  . GLU A 1 59  ? 134.325 105.798 109.472 1.00 42.40  ? 57  GLU A CD  1 
ATOM   317  O  OE1 . GLU A 1 59  ? 134.686 104.879 108.709 1.00 33.34  ? 57  GLU A OE1 1 
ATOM   318  O  OE2 . GLU A 1 59  ? 133.387 106.577 109.203 1.00 42.35  ? 57  GLU A OE2 1 
ATOM   319  N  N   . ILE A 1 60  ? 135.541 104.471 114.042 1.00 31.14  ? 58  ILE A N   1 
ATOM   320  C  CA  . ILE A 1 60  ? 134.671 104.696 115.192 1.00 30.69  ? 58  ILE A CA  1 
ATOM   321  C  C   . ILE A 1 60  ? 135.455 105.314 116.339 1.00 31.94  ? 58  ILE A C   1 
ATOM   322  O  O   . ILE A 1 60  ? 134.968 106.222 117.022 1.00 41.86  ? 58  ILE A O   1 
ATOM   323  C  CB  . ILE A 1 60  ? 133.989 103.378 115.607 1.00 27.02  ? 58  ILE A CB  1 
ATOM   324  C  CG1 . ILE A 1 60  ? 133.000 102.911 114.533 1.00 39.26  ? 58  ILE A CG1 1 
ATOM   325  C  CG2 . ILE A 1 60  ? 133.266 103.528 116.938 1.00 27.95  ? 58  ILE A CG2 1 
ATOM   326  C  CD1 . ILE A 1 60  ? 131.950 103.939 114.131 1.00 29.59  ? 58  ILE A CD1 1 
ATOM   327  N  N   . LEU A 1 61  ? 136.678 104.837 116.575 1.00 31.94  ? 59  LEU A N   1 
ATOM   328  C  CA  . LEU A 1 61  ? 137.477 105.395 117.659 1.00 30.51  ? 59  LEU A CA  1 
ATOM   329  C  C   . LEU A 1 61  ? 137.710 106.884 117.449 1.00 26.10  ? 59  LEU A C   1 
ATOM   330  O  O   . LEU A 1 61  ? 137.652 107.670 118.401 1.00 38.80  ? 59  LEU A O   1 
ATOM   331  C  CB  . LEU A 1 61  ? 138.810 104.658 117.768 1.00 39.71  ? 59  LEU A CB  1 
ATOM   332  C  CG  . LEU A 1 61  ? 139.774 105.201 118.825 1.00 37.73  ? 59  LEU A CG  1 
ATOM   333  C  CD1 . LEU A 1 61  ? 139.338 104.753 120.207 1.00 36.79  ? 59  LEU A CD1 1 
ATOM   334  C  CD2 . LEU A 1 61  ? 141.195 104.766 118.532 1.00 36.55  ? 59  LEU A CD2 1 
ATOM   335  N  N   . MET A 1 62  ? 137.982 107.292 116.210 1.00 28.06  ? 60  MET A N   1 
ATOM   336  C  CA  . MET A 1 62  ? 138.166 108.710 115.929 1.00 31.85  ? 60  MET A CA  1 
ATOM   337  C  C   . MET A 1 62  ? 136.892 109.493 116.210 1.00 40.27  ? 60  MET A C   1 
ATOM   338  O  O   . MET A 1 62  ? 136.947 110.628 116.696 1.00 51.02  ? 60  MET A O   1 
ATOM   339  C  CB  . MET A 1 62  ? 138.608 108.906 114.481 1.00 40.08  ? 60  MET A CB  1 
ATOM   340  C  CG  . MET A 1 62  ? 139.838 108.104 114.089 1.00 38.48  ? 60  MET A CG  1 
ATOM   341  S  SD  . MET A 1 62  ? 141.361 108.854 114.678 1.00 50.38  ? 60  MET A SD  1 
ATOM   342  C  CE  . MET A 1 62  ? 142.295 108.938 113.154 1.00 42.67  ? 60  MET A CE  1 
ATOM   343  N  N   . ARG A 1 63  ? 135.731 108.909 115.902 1.00 27.86  ? 61  ARG A N   1 
ATOM   344  C  CA  . ARG A 1 63  ? 134.470 109.555 116.249 1.00 9.42   ? 61  ARG A CA  1 
ATOM   345  C  C   . ARG A 1 63  ? 134.330 109.689 117.758 1.00 22.51  ? 61  ARG A C   1 
ATOM   346  O  O   . ARG A 1 63  ? 133.890 110.729 118.259 1.00 39.44  ? 61  ARG A O   1 
ATOM   347  C  CB  . ARG A 1 63  ? 133.289 108.768 115.678 1.00 23.46  ? 61  ARG A CB  1 
ATOM   348  C  CG  . ARG A 1 63  ? 133.436 108.324 114.228 1.00 37.23  ? 61  ARG A CG  1 
ATOM   349  C  CD  . ARG A 1 63  ? 132.592 109.166 113.293 1.00 31.34  ? 61  ARG A CD  1 
ATOM   350  N  NE  . ARG A 1 63  ? 131.168 109.063 113.584 1.00 18.45  ? 61  ARG A NE  1 
ATOM   351  C  CZ  . ARG A 1 63  ? 130.240 109.846 113.055 1.00 30.62  ? 61  ARG A CZ  1 
ATOM   352  N  NH1 . ARG A 1 63  ? 130.550 110.803 112.197 1.00 39.82  ? 61  ARG A NH1 1 
ATOM   353  N  NH2 . ARG A 1 63  ? 128.968 109.669 113.399 1.00 35.24  ? 61  ARG A NH2 1 
ATOM   354  N  N   . MET A 1 64  ? 134.695 108.641 118.500 1.00 24.17  ? 62  MET A N   1 
ATOM   355  C  CA  . MET A 1 64  ? 134.626 108.705 119.955 1.00 19.38  ? 62  MET A CA  1 
ATOM   356  C  C   . MET A 1 64  ? 135.568 109.767 120.502 1.00 26.10  ? 62  MET A C   1 
ATOM   357  O  O   . MET A 1 64  ? 135.205 110.524 121.409 1.00 41.62  ? 62  MET A O   1 
ATOM   358  C  CB  . MET A 1 64  ? 134.964 107.341 120.554 1.00 16.84  ? 62  MET A CB  1 
ATOM   359  C  CG  . MET A 1 64  ? 133.862 106.312 120.422 1.00 27.75  ? 62  MET A CG  1 
ATOM   360  S  SD  . MET A 1 64  ? 134.505 104.638 120.268 1.00 22.09  ? 62  MET A SD  1 
ATOM   361  C  CE  . MET A 1 64  ? 134.470 104.099 121.970 1.00 29.92  ? 62  MET A CE  1 
ATOM   362  N  N   . LEU A 1 65  ? 136.789 109.834 119.970 1.00 36.19  ? 63  LEU A N   1 
ATOM   363  C  CA  . LEU A 1 65  ? 137.740 110.842 120.424 1.00 32.21  ? 63  LEU A CA  1 
ATOM   364  C  C   . LEU A 1 65  ? 137.258 112.245 120.078 1.00 34.99  ? 63  LEU A C   1 
ATOM   365  O  O   . LEU A 1 65  ? 137.256 113.138 120.931 1.00 44.62  ? 63  LEU A O   1 
ATOM   366  C  CB  . LEU A 1 65  ? 139.114 110.581 119.807 1.00 33.41  ? 63  LEU A CB  1 
ATOM   367  C  CG  . LEU A 1 65  ? 139.859 109.322 120.259 1.00 34.06  ? 63  LEU A CG  1 
ATOM   368  C  CD1 . LEU A 1 65  ? 141.234 109.274 119.621 1.00 39.80  ? 63  LEU A CD1 1 
ATOM   369  C  CD2 . LEU A 1 65  ? 139.964 109.228 121.774 1.00 37.78  ? 63  LEU A CD2 1 
ATOM   370  N  N   . LYS A 1 66  ? 136.841 112.457 118.828 1.00 30.36  ? 64  LYS A N   1 
ATOM   371  C  CA  . LYS A 1 66  ? 136.334 113.767 118.434 1.00 29.15  ? 64  LYS A CA  1 
ATOM   372  C  C   . LYS A 1 66  ? 135.054 114.119 119.175 1.00 33.50  ? 64  LYS A C   1 
ATOM   373  O  O   . LYS A 1 66  ? 134.740 115.302 119.344 1.00 42.51  ? 64  LYS A O   1 
ATOM   374  C  CB  . LYS A 1 66  ? 136.088 113.806 116.926 1.00 27.12  ? 64  LYS A CB  1 
ATOM   375  C  CG  . LYS A 1 66  ? 137.106 114.625 116.155 1.00 36.52  ? 64  LYS A CG  1 
ATOM   376  C  CD  . LYS A 1 66  ? 136.931 114.492 114.651 1.00 33.37  ? 64  LYS A CD  1 
ATOM   377  C  CE  . LYS A 1 66  ? 137.080 113.053 114.188 1.00 37.05  ? 64  LYS A CE  1 
ATOM   378  N  NZ  . LYS A 1 66  ? 137.567 112.966 112.785 1.00 41.80  ? 64  LYS A NZ  1 
ATOM   379  N  N   . LEU A 1 67  ? 134.300 113.113 119.619 1.00 31.03  ? 65  LEU A N   1 
ATOM   380  C  CA  . LEU A 1 67  ? 133.052 113.384 120.322 1.00 28.55  ? 65  LEU A CA  1 
ATOM   381  C  C   . LEU A 1 67  ? 133.298 114.043 121.671 1.00 32.44  ? 65  LEU A C   1 
ATOM   382  O  O   . LEU A 1 67  ? 132.431 114.770 122.168 1.00 38.96  ? 65  LEU A O   1 
ATOM   383  C  CB  . LEU A 1 67  ? 132.266 112.084 120.499 1.00 16.86  ? 65  LEU A CB  1 
ATOM   384  C  CG  . LEU A 1 67  ? 131.048 112.098 121.425 1.00 20.23  ? 65  LEU A CG  1 
ATOM   385  C  CD1 . LEU A 1 67  ? 129.877 112.780 120.754 1.00 35.76  ? 65  LEU A CD1 1 
ATOM   386  C  CD2 . LEU A 1 67  ? 130.678 110.686 121.824 1.00 30.66  ? 65  LEU A CD2 1 
ATOM   387  N  N   . ILE A 1 68  ? 134.467 113.815 122.270 1.00 38.36  ? 66  ILE A N   1 
ATOM   388  C  CA  . ILE A 1 68  ? 134.708 114.205 123.656 1.00 29.39  ? 66  ILE A CA  1 
ATOM   389  C  C   . ILE A 1 68  ? 135.551 115.466 123.791 1.00 37.13  ? 66  ILE A C   1 
ATOM   390  O  O   . ILE A 1 68  ? 135.651 116.005 124.904 1.00 51.24  ? 66  ILE A O   1 
ATOM   391  C  CB  . ILE A 1 68  ? 135.362 113.041 124.438 1.00 29.73  ? 66  ILE A CB  1 
ATOM   392  C  CG1 . ILE A 1 68  ? 134.974 113.092 125.916 1.00 37.00  ? 66  ILE A CG1 1 
ATOM   393  C  CG2 . ILE A 1 68  ? 136.884 113.044 124.292 1.00 38.16  ? 66  ILE A CG2 1 
ATOM   394  C  CD1 . ILE A 1 68  ? 133.524 112.749 126.188 1.00 44.02  ? 66  ILE A CD1 1 
ATOM   395  N  N   . ILE A 1 69  ? 136.150 115.964 122.708 1.00 34.66  ? 67  ILE A N   1 
ATOM   396  C  CA  . ILE A 1 69  ? 137.058 117.100 122.844 1.00 31.51  ? 67  ILE A CA  1 
ATOM   397  C  C   . ILE A 1 69  ? 136.294 118.360 123.233 1.00 30.62  ? 67  ILE A C   1 
ATOM   398  O  O   . ILE A 1 69  ? 136.792 119.182 124.011 1.00 47.93  ? 67  ILE A O   1 
ATOM   399  C  CB  . ILE A 1 69  ? 137.880 117.304 121.557 1.00 46.91  ? 67  ILE A CB  1 
ATOM   400  C  CG1 . ILE A 1 69  ? 136.975 117.641 120.368 1.00 50.51  ? 67  ILE A CG1 1 
ATOM   401  C  CG2 . ILE A 1 69  ? 138.726 116.071 121.275 1.00 43.65  ? 67  ILE A CG2 1 
ATOM   402  C  CD1 . ILE A 1 69  ? 137.733 118.036 119.112 1.00 44.07  ? 67  ILE A CD1 1 
ATOM   403  N  N   . LEU A 1 70  ? 135.088 118.547 122.700 1.00 22.96  ? 68  LEU A N   1 
ATOM   404  C  CA  . LEU A 1 70  ? 134.327 119.746 123.046 1.00 33.21  ? 68  LEU A CA  1 
ATOM   405  C  C   . LEU A 1 70  ? 134.014 119.811 124.534 1.00 31.28  ? 68  LEU A C   1 
ATOM   406  O  O   . LEU A 1 70  ? 134.332 120.834 125.164 1.00 35.07  ? 68  LEU A O   1 
ATOM   407  C  CB  . LEU A 1 70  ? 133.058 119.818 122.187 1.00 34.96  ? 68  LEU A CB  1 
ATOM   408  C  CG  . LEU A 1 70  ? 131.871 120.628 122.722 1.00 32.90  ? 68  LEU A CG  1 
ATOM   409  C  CD1 . LEU A 1 70  ? 132.166 122.113 122.665 1.00 23.05  ? 68  LEU A CD1 1 
ATOM   410  C  CD2 . LEU A 1 70  ? 130.615 120.307 121.936 1.00 36.40  ? 68  LEU A CD2 1 
ATOM   411  N  N   . PRO A 1 71  ? 133.409 118.795 125.158 1.00 22.97  ? 69  PRO A N   1 
ATOM   412  C  CA  . PRO A 1 71  ? 133.282 118.829 126.623 1.00 27.01  ? 69  PRO A CA  1 
ATOM   413  C  C   . PRO A 1 71  ? 134.621 118.864 127.331 1.00 29.29  ? 69  PRO A C   1 
ATOM   414  O  O   . PRO A 1 71  ? 134.743 119.487 128.392 1.00 38.14  ? 69  PRO A O   1 
ATOM   415  C  CB  . PRO A 1 71  ? 132.509 117.540 126.939 1.00 25.73  ? 69  PRO A CB  1 
ATOM   416  C  CG  . PRO A 1 71  ? 131.831 117.176 125.678 1.00 25.78  ? 69  PRO A CG  1 
ATOM   417  C  CD  . PRO A 1 71  ? 132.739 117.619 124.581 1.00 31.74  ? 69  PRO A CD  1 
ATOM   418  N  N   . LEU A 1 72  ? 135.632 118.200 126.772 1.00 32.98  ? 70  LEU A N   1 
ATOM   419  C  CA  . LEU A 1 72  ? 136.950 118.173 127.392 1.00 30.61  ? 70  LEU A CA  1 
ATOM   420  C  C   . LEU A 1 72  ? 137.570 119.564 127.418 1.00 36.48  ? 70  LEU A C   1 
ATOM   421  O  O   . LEU A 1 72  ? 138.122 119.993 128.437 1.00 45.99  ? 70  LEU A O   1 
ATOM   422  C  CB  . LEU A 1 72  ? 137.844 117.193 126.630 1.00 37.64  ? 70  LEU A CB  1 
ATOM   423  C  CG  . LEU A 1 72  ? 139.165 116.705 127.225 1.00 40.12  ? 70  LEU A CG  1 
ATOM   424  C  CD1 . LEU A 1 72  ? 139.049 116.404 128.696 1.00 39.52  ? 70  LEU A CD1 1 
ATOM   425  C  CD2 . LEU A 1 72  ? 139.634 115.472 126.476 1.00 46.29  ? 70  LEU A CD2 1 
ATOM   426  N  N   . ILE A 1 73  ? 137.486 120.285 126.300 1.00 32.96  ? 71  ILE A N   1 
ATOM   427  C  CA  . ILE A 1 73  ? 138.100 121.605 126.213 1.00 30.33  ? 71  ILE A CA  1 
ATOM   428  C  C   . ILE A 1 73  ? 137.295 122.623 127.013 1.00 34.82  ? 71  ILE A C   1 
ATOM   429  O  O   . ILE A 1 73  ? 137.852 123.412 127.784 1.00 43.03  ? 71  ILE A O   1 
ATOM   430  C  CB  . ILE A 1 73  ? 138.243 122.019 124.738 1.00 35.39  ? 71  ILE A CB  1 
ATOM   431  C  CG1 . ILE A 1 73  ? 139.319 121.168 124.063 1.00 42.77  ? 71  ILE A CG1 1 
ATOM   432  C  CG2 . ILE A 1 73  ? 138.590 123.499 124.609 1.00 43.94  ? 71  ILE A CG2 1 
ATOM   433  C  CD1 . ILE A 1 73  ? 139.225 121.150 122.557 1.00 41.50  ? 71  ILE A CD1 1 
ATOM   434  N  N   . ILE A 1 74  ? 135.973 122.625 126.838 1.00 31.39  ? 72  ILE A N   1 
ATOM   435  C  CA  . ILE A 1 74  ? 135.136 123.635 127.482 1.00 28.04  ? 72  ILE A CA  1 
ATOM   436  C  C   . ILE A 1 74  ? 135.217 123.506 128.997 1.00 26.66  ? 72  ILE A C   1 
ATOM   437  O  O   . ILE A 1 74  ? 135.388 124.498 129.715 1.00 34.12  ? 72  ILE A O   1 
ATOM   438  C  CB  . ILE A 1 74  ? 133.684 123.519 126.980 1.00 27.78  ? 72  ILE A CB  1 
ATOM   439  C  CG1 . ILE A 1 74  ? 133.542 124.118 125.578 1.00 28.11  ? 72  ILE A CG1 1 
ATOM   440  C  CG2 . ILE A 1 74  ? 132.700 124.168 127.958 1.00 28.62  ? 72  ILE A CG2 1 
ATOM   441  C  CD1 . ILE A 1 74  ? 133.646 125.630 125.522 1.00 32.11  ? 72  ILE A CD1 1 
ATOM   442  N  N   . SER A 1 75  ? 135.093 122.282 129.508 1.00 25.53  ? 73  SER A N   1 
ATOM   443  C  CA  . SER A 1 75  ? 135.048 122.093 130.953 1.00 25.90  ? 73  SER A CA  1 
ATOM   444  C  C   . SER A 1 75  ? 136.423 122.269 131.582 1.00 30.83  ? 73  SER A C   1 
ATOM   445  O  O   . SER A 1 75  ? 136.548 122.876 132.650 1.00 38.51  ? 73  SER A O   1 
ATOM   446  C  CB  . SER A 1 75  ? 134.487 120.712 131.277 1.00 32.22  ? 73  SER A CB  1 
ATOM   447  O  OG  . SER A 1 75  ? 133.387 120.408 130.441 1.00 45.74  ? 73  SER A OG  1 
ATOM   448  N  N   . SER A 1 76  ? 137.468 121.749 130.936 1.00 34.50  ? 74  SER A N   1 
ATOM   449  C  CA  . SER A 1 76  ? 138.804 121.833 131.517 1.00 30.82  ? 74  SER A CA  1 
ATOM   450  C  C   . SER A 1 76  ? 139.353 123.252 131.467 1.00 35.49  ? 74  SER A C   1 
ATOM   451  O  O   . SER A 1 76  ? 140.093 123.659 132.369 1.00 38.27  ? 74  SER A O   1 
ATOM   452  C  CB  . SER A 1 76  ? 139.745 120.875 130.794 1.00 40.63  ? 74  SER A CB  1 
ATOM   453  O  OG  . SER A 1 76  ? 139.245 119.551 130.838 1.00 48.66  ? 74  SER A OG  1 
ATOM   454  N  N   . MET A 1 77  ? 139.019 124.012 130.423 1.00 38.01  ? 75  MET A N   1 
ATOM   455  C  CA  . MET A 1 77  ? 139.430 125.410 130.370 1.00 25.02  ? 75  MET A CA  1 
ATOM   456  C  C   . MET A 1 77  ? 138.773 126.221 131.478 1.00 29.27  ? 75  MET A C   1 
ATOM   457  O  O   . MET A 1 77  ? 139.420 127.062 132.111 1.00 40.31  ? 75  MET A O   1 
ATOM   458  C  CB  . MET A 1 77  ? 139.094 126.003 129.003 1.00 28.06  ? 75  MET A CB  1 
ATOM   459  C  CG  . MET A 1 77  ? 139.999 125.507 127.883 1.00 36.93  ? 75  MET A CG  1 
ATOM   460  S  SD  . MET A 1 77  ? 141.679 126.181 127.855 1.00 67.46  ? 75  MET A SD  1 
ATOM   461  C  CE  . MET A 1 77  ? 141.536 127.701 128.796 1.00 43.32  ? 75  MET A CE  1 
ATOM   462  N  N   . ILE A 1 78  ? 137.484 125.988 131.726 1.00 32.84  ? 76  ILE A N   1 
ATOM   463  C  CA  . ILE A 1 78  ? 136.769 126.768 132.730 1.00 25.35  ? 76  ILE A CA  1 
ATOM   464  C  C   . ILE A 1 78  ? 137.240 126.402 134.133 1.00 27.63  ? 76  ILE A C   1 
ATOM   465  O  O   . ILE A 1 78  ? 137.459 127.280 134.975 1.00 38.18  ? 76  ILE A O   1 
ATOM   466  C  CB  . ILE A 1 78  ? 135.251 126.570 132.568 1.00 13.40  ? 76  ILE A CB  1 
ATOM   467  C  CG1 . ILE A 1 78  ? 134.786 127.141 131.229 1.00 15.21  ? 76  ILE A CG1 1 
ATOM   468  C  CG2 . ILE A 1 78  ? 134.494 127.235 133.704 1.00 29.46  ? 76  ILE A CG2 1 
ATOM   469  C  CD1 . ILE A 1 78  ? 133.449 126.623 130.777 1.00 26.97  ? 76  ILE A CD1 1 
ATOM   470  N  N   . THR A 1 79  ? 137.395 125.107 134.413 1.00 27.26  ? 77  THR A N   1 
ATOM   471  C  CA  . THR A 1 79  ? 137.770 124.686 135.760 1.00 24.14  ? 77  THR A CA  1 
ATOM   472  C  C   . THR A 1 79  ? 139.210 125.061 136.085 1.00 34.87  ? 77  THR A C   1 
ATOM   473  O  O   . THR A 1 79  ? 139.516 125.434 137.223 1.00 42.87  ? 77  THR A O   1 
ATOM   474  C  CB  . THR A 1 79  ? 137.569 123.181 135.918 1.00 26.92  ? 77  THR A CB  1 
ATOM   475  O  OG1 . THR A 1 79  ? 138.366 122.483 134.955 1.00 41.06  ? 77  THR A OG1 1 
ATOM   476  C  CG2 . THR A 1 79  ? 136.114 122.818 135.730 1.00 33.64  ? 77  THR A CG2 1 
ATOM   477  N  N   . GLY A 1 80  ? 140.113 124.955 135.111 1.00 33.66  ? 78  GLY A N   1 
ATOM   478  C  CA  . GLY A 1 80  ? 141.498 125.308 135.373 1.00 38.46  ? 78  GLY A CA  1 
ATOM   479  C  C   . GLY A 1 80  ? 141.667 126.778 135.698 1.00 33.01  ? 78  GLY A C   1 
ATOM   480  O  O   . GLY A 1 80  ? 142.342 127.143 136.662 1.00 44.44  ? 78  GLY A O   1 
ATOM   481  N  N   . VAL A 1 81  ? 141.048 127.643 134.896 1.00 22.60  ? 79  VAL A N   1 
ATOM   482  C  CA  . VAL A 1 81  ? 141.167 129.080 135.115 1.00 32.29  ? 79  VAL A CA  1 
ATOM   483  C  C   . VAL A 1 81  ? 140.402 129.498 136.364 1.00 40.02  ? 79  VAL A C   1 
ATOM   484  O  O   . VAL A 1 81  ? 140.856 130.358 137.128 1.00 46.95  ? 79  VAL A O   1 
ATOM   485  C  CB  . VAL A 1 81  ? 140.685 129.846 133.871 1.00 30.23  ? 79  VAL A CB  1 
ATOM   486  C  CG1 . VAL A 1 81  ? 140.886 131.333 134.053 1.00 39.91  ? 79  VAL A CG1 1 
ATOM   487  C  CG2 . VAL A 1 81  ? 141.428 129.376 132.639 1.00 36.56  ? 79  VAL A CG2 1 
ATOM   488  N  N   . ALA A 1 82  ? 139.227 128.907 136.590 1.00 39.84  ? 80  ALA A N   1 
ATOM   489  C  CA  . ALA A 1 82  ? 138.401 129.309 137.723 1.00 31.69  ? 80  ALA A CA  1 
ATOM   490  C  C   . ALA A 1 82  ? 139.088 129.010 139.048 1.00 35.31  ? 80  ALA A C   1 
ATOM   491  O  O   . ALA A 1 82  ? 138.995 129.799 139.995 1.00 46.52  ? 80  ALA A O   1 
ATOM   492  C  CB  . ALA A 1 82  ? 137.046 128.608 137.654 1.00 25.18  ? 80  ALA A CB  1 
ATOM   493  N  N   . ALA A 1 83  ? 139.781 127.873 139.139 1.00 36.98  ? 81  ALA A N   1 
ATOM   494  C  CA  . ALA A 1 83  ? 140.432 127.508 140.392 1.00 42.08  ? 81  ALA A CA  1 
ATOM   495  C  C   . ALA A 1 83  ? 141.449 128.560 140.813 1.00 48.32  ? 81  ALA A C   1 
ATOM   496  O  O   . ALA A 1 83  ? 141.531 128.919 141.992 1.00 51.73  ? 81  ALA A O   1 
ATOM   497  C  CB  . ALA A 1 83  ? 141.102 126.143 140.255 1.00 42.81  ? 81  ALA A CB  1 
ATOM   498  N  N   . LEU A 1 84  ? 142.236 129.059 139.865 1.00 54.40  ? 82  LEU A N   1 
ATOM   499  C  CA  . LEU A 1 84  ? 143.219 130.086 140.175 1.00 55.23  ? 82  LEU A CA  1 
ATOM   500  C  C   . LEU A 1 84  ? 142.542 131.331 140.732 1.00 59.21  ? 82  LEU A C   1 
ATOM   501  O  O   . LEU A 1 84  ? 141.479 131.747 140.263 1.00 56.26  ? 82  LEU A O   1 
ATOM   502  C  CB  . LEU A 1 84  ? 144.022 130.441 138.925 1.00 54.24  ? 82  LEU A CB  1 
ATOM   503  C  CG  . LEU A 1 84  ? 144.849 129.312 138.311 1.00 55.58  ? 82  LEU A CG  1 
ATOM   504  C  CD1 . LEU A 1 84  ? 145.617 129.824 137.114 1.00 55.87  ? 82  LEU A CD1 1 
ATOM   505  C  CD2 . LEU A 1 84  ? 145.802 128.700 139.326 1.00 57.19  ? 82  LEU A CD2 1 
ATOM   506  N  N   . ASP A 1 85  ? 143.170 131.929 141.741 1.00 68.00  ? 83  ASP A N   1 
ATOM   507  C  CA  . ASP A 1 85  ? 142.643 133.146 142.336 1.00 68.20  ? 83  ASP A CA  1 
ATOM   508  C  C   . ASP A 1 85  ? 142.695 134.294 141.336 1.00 67.83  ? 83  ASP A C   1 
ATOM   509  O  O   . ASP A 1 85  ? 143.527 134.321 140.426 1.00 63.65  ? 83  ASP A O   1 
ATOM   510  C  CB  . ASP A 1 85  ? 143.433 133.512 143.591 1.00 63.73  ? 83  ASP A CB  1 
ATOM   511  C  CG  . ASP A 1 85  ? 143.168 132.566 144.741 1.00 66.69  ? 83  ASP A CG  1 
ATOM   512  O  OD1 . ASP A 1 85  ? 142.435 131.575 144.538 1.00 66.91  ? 83  ASP A OD1 1 
ATOM   513  O  OD2 . ASP A 1 85  ? 143.687 132.815 145.848 1.00 69.80  ? 83  ASP A OD2 1 
ATOM   514  N  N   . SER A 1 86  ? 141.788 135.256 141.518 1.00 65.37  ? 84  SER A N   1 
ATOM   515  C  CA  . SER A 1 86  ? 141.681 136.358 140.569 1.00 66.53  ? 84  SER A CA  1 
ATOM   516  C  C   . SER A 1 86  ? 142.994 137.120 140.456 1.00 66.15  ? 84  SER A C   1 
ATOM   517  O  O   . SER A 1 86  ? 143.403 137.508 139.355 1.00 63.53  ? 84  SER A O   1 
ATOM   518  C  CB  . SER A 1 86  ? 140.551 137.298 140.989 1.00 66.40  ? 84  SER A CB  1 
ATOM   519  O  OG  . SER A 1 86  ? 140.671 138.556 140.350 1.00 66.97  ? 84  SER A OG  1 
ATOM   520  N  N   . ASN A 1 87  ? 143.672 137.342 141.583 1.00 64.89  ? 85  ASN A N   1 
ATOM   521  C  CA  . ASN A 1 87  ? 144.888 138.150 141.563 1.00 65.55  ? 85  ASN A CA  1 
ATOM   522  C  C   . ASN A 1 87  ? 145.986 137.480 140.748 1.00 68.69  ? 85  ASN A C   1 
ATOM   523  O  O   . ASN A 1 87  ? 146.660 138.136 139.945 1.00 73.14  ? 85  ASN A O   1 
ATOM   524  C  CB  . ASN A 1 87  ? 145.374 138.416 142.989 1.00 63.65  ? 85  ASN A CB  1 
ATOM   525  C  CG  . ASN A 1 87  ? 144.238 138.552 143.981 1.00 68.91  ? 85  ASN A CG  1 
ATOM   526  O  OD1 . ASN A 1 87  ? 143.242 139.222 143.712 1.00 73.01  ? 85  ASN A OD1 1 
ATOM   527  N  ND2 . ASN A 1 87  ? 144.379 137.910 145.135 1.00 68.48  ? 85  ASN A ND2 1 
ATOM   528  N  N   . VAL A 1 88  ? 146.179 136.172 140.934 1.00 67.96  ? 86  VAL A N   1 
ATOM   529  C  CA  . VAL A 1 88  ? 147.297 135.467 140.313 1.00 70.18  ? 86  VAL A CA  1 
ATOM   530  C  C   . VAL A 1 88  ? 146.911 134.753 139.025 1.00 67.80  ? 86  VAL A C   1 
ATOM   531  O  O   . VAL A 1 88  ? 147.795 134.195 138.355 1.00 64.89  ? 86  VAL A O   1 
ATOM   532  C  CB  . VAL A 1 88  ? 147.930 134.459 141.299 1.00 69.09  ? 86  VAL A CB  1 
ATOM   533  C  CG1 . VAL A 1 88  ? 148.102 135.090 142.674 1.00 67.66  ? 86  VAL A CG1 1 
ATOM   534  C  CG2 . VAL A 1 88  ? 147.093 133.187 141.403 1.00 66.43  ? 86  VAL A CG2 1 
ATOM   535  N  N   . SER A 1 89  ? 145.630 134.747 138.654 1.00 61.83  ? 87  SER A N   1 
ATOM   536  C  CA  . SER A 1 89  ? 145.231 134.092 137.413 1.00 61.09  ? 87  SER A CA  1 
ATOM   537  C  C   . SER A 1 89  ? 145.857 134.777 136.205 1.00 61.21  ? 87  SER A C   1 
ATOM   538  O  O   . SER A 1 89  ? 146.276 134.111 135.251 1.00 55.14  ? 87  SER A O   1 
ATOM   539  C  CB  . SER A 1 89  ? 143.708 134.081 137.291 1.00 60.55  ? 87  SER A CB  1 
ATOM   540  O  OG  . SER A 1 89  ? 143.296 133.348 136.152 1.00 60.38  ? 87  SER A OG  1 
ATOM   541  N  N   . GLY A 1 90  ? 145.924 136.108 136.223 1.00 69.14  ? 88  GLY A N   1 
ATOM   542  C  CA  . GLY A 1 90  ? 146.495 136.824 135.095 1.00 67.04  ? 88  GLY A CA  1 
ATOM   543  C  C   . GLY A 1 90  ? 147.978 136.563 134.919 1.00 67.53  ? 88  GLY A C   1 
ATOM   544  O  O   . GLY A 1 90  ? 148.451 136.357 133.798 1.00 65.88  ? 88  GLY A O   1 
ATOM   545  N  N   . LYS A 1 91  ? 148.735 136.573 136.018 1.00 65.89  ? 89  LYS A N   1 
ATOM   546  C  CA  . LYS A 1 91  ? 150.175 136.353 135.919 1.00 64.84  ? 89  LYS A CA  1 
ATOM   547  C  C   . LYS A 1 91  ? 150.486 134.947 135.425 1.00 69.00  ? 89  LYS A C   1 
ATOM   548  O  O   . LYS A 1 91  ? 151.346 134.765 134.556 1.00 66.36  ? 89  LYS A O   1 
ATOM   549  C  CB  . LYS A 1 91  ? 150.843 136.604 137.271 1.00 62.85  ? 89  LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 91  ? 150.465 137.926 137.926 1.00 69.09  ? 89  LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 91  ? 150.967 138.010 139.360 1.00 71.41  ? 89  LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 91  ? 152.485 138.019 139.427 1.00 66.95  ? 89  LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 91  ? 152.979 138.144 140.825 1.00 64.15  ? 89  LYS A NZ  1 
ATOM   554  N  N   . ILE A 1 92  ? 149.799 133.938 135.965 1.00 68.33  ? 90  ILE A N   1 
ATOM   555  C  CA  . ILE A 1 92  ? 150.027 132.567 135.520 1.00 62.57  ? 90  ILE A CA  1 
ATOM   556  C  C   . ILE A 1 92  ? 149.615 132.408 134.063 1.00 64.74  ? 90  ILE A C   1 
ATOM   557  O  O   . ILE A 1 92  ? 150.318 131.771 133.269 1.00 65.91  ? 90  ILE A O   1 
ATOM   558  C  CB  . ILE A 1 92  ? 149.283 131.578 136.437 1.00 65.61  ? 90  ILE A CB  1 
ATOM   559  C  CG1 . ILE A 1 92  ? 149.889 131.623 137.843 1.00 63.49  ? 90  ILE A CG1 1 
ATOM   560  C  CG2 . ILE A 1 92  ? 149.336 130.162 135.862 1.00 62.81  ? 90  ILE A CG2 1 
ATOM   561  C  CD1 . ILE A 1 92  ? 149.191 130.741 138.860 1.00 65.31  ? 90  ILE A CD1 1 
ATOM   562  N  N   . GLY A 1 93  ? 148.471 132.981 133.687 1.00 59.94  ? 91  GLY A N   1 
ATOM   563  C  CA  . GLY A 1 93  ? 148.052 132.920 132.297 1.00 60.49  ? 91  GLY A CA  1 
ATOM   564  C  C   . GLY A 1 93  ? 149.044 133.586 131.364 1.00 59.46  ? 91  GLY A C   1 
ATOM   565  O  O   . GLY A 1 93  ? 149.324 133.081 130.275 1.00 55.39  ? 91  GLY A O   1 
ATOM   566  N  N   . LEU A 1 94  ? 149.588 134.732 131.777 1.00 59.87  ? 92  LEU A N   1 
ATOM   567  C  CA  . LEU A 1 94  ? 150.609 135.394 130.973 1.00 61.53  ? 92  LEU A CA  1 
ATOM   568  C  C   . LEU A 1 94  ? 151.853 134.525 130.849 1.00 59.49  ? 92  LEU A C   1 
ATOM   569  O  O   . LEU A 1 94  ? 152.459 134.444 129.775 1.00 63.30  ? 92  LEU A O   1 
ATOM   570  C  CB  . LEU A 1 94  ? 150.955 136.752 131.586 1.00 62.86  ? 92  LEU A CB  1 
ATOM   571  C  CG  . LEU A 1 94  ? 152.278 137.400 131.170 1.00 62.97  ? 92  LEU A CG  1 
ATOM   572  C  CD1 . LEU A 1 94  ? 152.238 137.791 129.703 1.00 63.32  ? 92  LEU A CD1 1 
ATOM   573  C  CD2 . LEU A 1 94  ? 152.572 138.611 132.041 1.00 60.06  ? 92  LEU A CD2 1 
ATOM   574  N  N   . ARG A 1 95  ? 152.252 133.871 131.941 1.00 60.38  ? 93  ARG A N   1 
ATOM   575  C  CA  . ARG A 1 95  ? 153.432 133.014 131.898 1.00 60.97  ? 93  ARG A CA  1 
ATOM   576  C  C   . ARG A 1 95  ? 153.233 131.846 130.940 1.00 62.60  ? 93  ARG A C   1 
ATOM   577  O  O   . ARG A 1 95  ? 154.138 131.505 130.169 1.00 58.94  ? 93  ARG A O   1 
ATOM   578  C  CB  . ARG A 1 95  ? 153.755 132.503 133.301 1.00 63.11  ? 93  ARG A CB  1 
ATOM   579  C  CG  . ARG A 1 95  ? 155.196 132.711 133.722 1.00 59.59  ? 93  ARG A CG  1 
ATOM   580  C  CD  . ARG A 1 95  ? 155.310 132.890 135.221 1.00 62.94  ? 93  ARG A CD  1 
ATOM   581  N  NE  . ARG A 1 95  ? 154.760 134.163 135.668 1.00 65.82  ? 93  ARG A NE  1 
ATOM   582  C  CZ  . ARG A 1 95  ? 154.752 134.574 136.929 1.00 66.57  ? 93  ARG A CZ  1 
ATOM   583  N  NH1 . ARG A 1 95  ? 155.252 133.833 137.902 1.00 64.59  ? 93  ARG A NH1 1 
ATOM   584  N  NH2 . ARG A 1 95  ? 154.232 135.763 137.220 1.00 67.36  ? 93  ARG A NH2 1 
ATOM   585  N  N   . ALA A 1 96  ? 152.056 131.217 130.977 1.00 62.76  ? 94  ALA A N   1 
ATOM   586  C  CA  . ALA A 1 96  ? 151.800 130.080 130.100 1.00 58.44  ? 94  ALA A CA  1 
ATOM   587  C  C   . ALA A 1 96  ? 151.803 130.495 128.635 1.00 64.75  ? 94  ALA A C   1 
ATOM   588  O  O   . ALA A 1 96  ? 152.377 129.804 127.787 1.00 62.14  ? 94  ALA A O   1 
ATOM   589  C  CB  . ALA A 1 96  ? 150.468 129.428 130.467 1.00 57.12  ? 94  ALA A CB  1 
ATOM   590  N  N   . VAL A 1 97  ? 151.168 131.625 128.316 1.00 64.78  ? 95  VAL A N   1 
ATOM   591  C  CA  . VAL A 1 97  ? 151.062 132.047 126.923 1.00 59.04  ? 95  VAL A CA  1 
ATOM   592  C  C   . VAL A 1 97  ? 152.437 132.371 126.353 1.00 58.64  ? 95  VAL A C   1 
ATOM   593  O  O   . VAL A 1 97  ? 152.733 132.051 125.196 1.00 61.34  ? 95  VAL A O   1 
ATOM   594  C  CB  . VAL A 1 97  ? 150.094 133.239 126.807 1.00 59.18  ? 95  VAL A CB  1 
ATOM   595  C  CG1 . VAL A 1 97  ? 150.309 134.006 125.504 1.00 60.24  ? 95  VAL A CG1 1 
ATOM   596  C  CG2 . VAL A 1 97  ? 148.657 132.754 126.906 1.00 58.69  ? 95  VAL A CG2 1 
ATOM   597  N  N   . VAL A 1 98  ? 153.295 133.016 127.144 1.00 53.09  ? 96  VAL A N   1 
ATOM   598  C  CA  . VAL A 1 98  ? 154.636 133.339 126.665 1.00 53.87  ? 96  VAL A CA  1 
ATOM   599  C  C   . VAL A 1 98  ? 155.419 132.063 126.385 1.00 61.90  ? 96  VAL A C   1 
ATOM   600  O  O   . VAL A 1 98  ? 156.149 131.969 125.391 1.00 61.98  ? 96  VAL A O   1 
ATOM   601  C  CB  . VAL A 1 98  ? 155.362 134.243 127.679 1.00 57.64  ? 96  VAL A CB  1 
ATOM   602  C  CG1 . VAL A 1 98  ? 156.826 134.428 127.293 1.00 60.40  ? 96  VAL A CG1 1 
ATOM   603  C  CG2 . VAL A 1 98  ? 154.666 135.589 127.776 1.00 61.64  ? 96  VAL A CG2 1 
ATOM   604  N  N   . TYR A 1 99  ? 155.289 131.063 127.260 1.00 60.46  ? 97  TYR A N   1 
ATOM   605  C  CA  . TYR A 1 99  ? 155.975 129.795 127.033 1.00 55.05  ? 97  TYR A CA  1 
ATOM   606  C  C   . TYR A 1 99  ? 155.462 129.106 125.775 1.00 59.07  ? 97  TYR A C   1 
ATOM   607  O  O   . TYR A 1 99  ? 156.248 128.550 124.999 1.00 56.96  ? 97  TYR A O   1 
ATOM   608  C  CB  . TYR A 1 99  ? 155.805 128.878 128.241 1.00 53.20  ? 97  TYR A CB  1 
ATOM   609  C  CG  . TYR A 1 99  ? 156.243 127.458 127.972 1.00 56.36  ? 97  TYR A CG  1 
ATOM   610  C  CD1 . TYR A 1 99  ? 157.588 127.122 127.930 1.00 57.48  ? 97  TYR A CD1 1 
ATOM   611  C  CD2 . TYR A 1 99  ? 155.311 126.457 127.742 1.00 60.87  ? 97  TYR A CD2 1 
ATOM   612  C  CE1 . TYR A 1 99  ? 157.992 125.828 127.676 1.00 59.98  ? 97  TYR A CE1 1 
ATOM   613  C  CE2 . TYR A 1 99  ? 155.706 125.160 127.485 1.00 60.34  ? 97  TYR A CE2 1 
ATOM   614  C  CZ  . TYR A 1 99  ? 157.047 124.850 127.454 1.00 61.92  ? 97  TYR A CZ  1 
ATOM   615  O  OH  . TYR A 1 99  ? 157.443 123.558 127.200 1.00 59.40  ? 97  TYR A OH  1 
ATOM   616  N  N   . TYR A 1 100 ? 154.146 129.127 125.557 1.00 60.31  ? 98  TYR A N   1 
ATOM   617  C  CA  . TYR A 1 100 ? 153.579 128.443 124.400 1.00 56.24  ? 98  TYR A CA  1 
ATOM   618  C  C   . TYR A 1 100 ? 154.095 129.042 123.098 1.00 58.32  ? 98  TYR A C   1 
ATOM   619  O  O   . TYR A 1 100 ? 154.605 128.326 122.230 1.00 61.44  ? 98  TYR A O   1 
ATOM   620  C  CB  . TYR A 1 100 ? 152.053 128.515 124.448 1.00 54.69  ? 98  TYR A CB  1 
ATOM   621  C  CG  . TYR A 1 100 ? 151.417 127.709 125.560 1.00 57.98  ? 98  TYR A CG  1 
ATOM   622  C  CD1 . TYR A 1 100 ? 152.173 126.862 126.358 1.00 60.00  ? 98  TYR A CD1 1 
ATOM   623  C  CD2 . TYR A 1 100 ? 150.056 127.793 125.806 1.00 61.30  ? 98  TYR A CD2 1 
ATOM   624  C  CE1 . TYR A 1 100 ? 151.593 126.127 127.367 1.00 60.88  ? 98  TYR A CE1 1 
ATOM   625  C  CE2 . TYR A 1 100 ? 149.468 127.061 126.813 1.00 58.98  ? 98  TYR A CE2 1 
ATOM   626  C  CZ  . TYR A 1 100 ? 150.240 126.228 127.590 1.00 61.27  ? 98  TYR A CZ  1 
ATOM   627  O  OH  . TYR A 1 100 ? 149.662 125.494 128.598 1.00 60.72  ? 98  TYR A OH  1 
ATOM   628  N  N   . PHE A 1 101 ? 153.971 130.361 122.946 1.00 55.39  ? 99  PHE A N   1 
ATOM   629  C  CA  . PHE A 1 101 ? 154.405 131.000 121.708 1.00 56.86  ? 99  PHE A CA  1 
ATOM   630  C  C   . PHE A 1 101 ? 155.917 130.923 121.549 1.00 56.96  ? 99  PHE A C   1 
ATOM   631  O  O   . PHE A 1 101 ? 156.420 130.734 120.436 1.00 59.10  ? 99  PHE A O   1 
ATOM   632  C  CB  . PHE A 1 101 ? 153.929 132.452 121.672 1.00 58.86  ? 99  PHE A CB  1 
ATOM   633  C  CG  . PHE A 1 101 ? 152.454 132.607 121.398 1.00 61.74  ? 99  PHE A CG  1 
ATOM   634  C  CD1 . PHE A 1 101 ? 151.626 131.500 121.271 1.00 58.27  ? 99  PHE A CD1 1 
ATOM   635  C  CD2 . PHE A 1 101 ? 151.895 133.867 121.268 1.00 61.97  ? 99  PHE A CD2 1 
ATOM   636  C  CE1 . PHE A 1 101 ? 150.278 131.650 121.019 1.00 58.37  ? 99  PHE A CE1 1 
ATOM   637  C  CE2 . PHE A 1 101 ? 150.546 134.020 121.015 1.00 63.35  ? 99  PHE A CE2 1 
ATOM   638  C  CZ  . PHE A 1 101 ? 149.738 132.911 120.892 1.00 62.67  ? 99  PHE A CZ  1 
ATOM   639  N  N   . ALA A 1 102 ? 156.660 131.065 122.648 1.00 56.71  ? 100 ALA A N   1 
ATOM   640  C  CA  . ALA A 1 102 ? 158.115 130.993 122.565 1.00 59.19  ? 100 ALA A CA  1 
ATOM   641  C  C   . ALA A 1 102 ? 158.567 129.641 122.028 1.00 61.91  ? 100 ALA A C   1 
ATOM   642  O  O   . ALA A 1 102 ? 159.465 129.570 121.181 1.00 60.83  ? 100 ALA A O   1 
ATOM   643  C  CB  . ALA A 1 102 ? 158.732 131.256 123.937 1.00 58.96  ? 100 ALA A CB  1 
ATOM   644  N  N   . THR A 1 103 ? 157.958 128.556 122.509 1.00 64.03  ? 101 THR A N   1 
ATOM   645  C  CA  . THR A 1 103 ? 158.332 127.230 122.031 1.00 61.68  ? 101 THR A CA  1 
ATOM   646  C  C   . THR A 1 103 ? 157.809 126.981 120.622 1.00 60.73  ? 101 THR A C   1 
ATOM   647  O  O   . THR A 1 103 ? 158.520 126.418 119.782 1.00 62.18  ? 101 THR A O   1 
ATOM   648  C  CB  . THR A 1 103 ? 157.810 126.162 122.991 1.00 56.67  ? 101 THR A CB  1 
ATOM   649  O  OG1 . THR A 1 103 ? 156.428 126.404 123.274 1.00 55.03  ? 101 THR A OG1 1 
ATOM   650  C  CG2 . THR A 1 103 ? 158.601 126.178 124.286 1.00 56.96  ? 101 THR A CG2 1 
ATOM   651  N  N   . THR A 1 104 ? 156.568 127.388 120.343 1.00 59.46  ? 102 THR A N   1 
ATOM   652  C  CA  . THR A 1 104 ? 156.005 127.172 119.014 1.00 61.29  ? 102 THR A CA  1 
ATOM   653  C  C   . THR A 1 104 ? 156.791 127.932 117.952 1.00 60.97  ? 102 THR A C   1 
ATOM   654  O  O   . THR A 1 104 ? 157.067 127.397 116.873 1.00 61.53  ? 102 THR A O   1 
ATOM   655  C  CB  . THR A 1 104 ? 154.536 127.591 118.991 1.00 60.63  ? 102 THR A CB  1 
ATOM   656  O  OG1 . THR A 1 104 ? 153.834 126.935 120.054 1.00 63.71  ? 102 THR A OG1 1 
ATOM   657  C  CG2 . THR A 1 104 ? 153.892 127.212 117.671 1.00 61.33  ? 102 THR A CG2 1 
ATOM   658  N  N   . LEU A 1 105 ? 157.157 129.184 118.236 1.00 62.61  ? 103 LEU A N   1 
ATOM   659  C  CA  . LEU A 1 105 ? 157.968 129.942 117.289 1.00 62.45  ? 103 LEU A CA  1 
ATOM   660  C  C   . LEU A 1 105 ? 159.344 129.313 117.125 1.00 58.36  ? 103 LEU A C   1 
ATOM   661  O  O   . LEU A 1 105 ? 159.883 129.261 116.014 1.00 63.89  ? 103 LEU A O   1 
ATOM   662  C  CB  . LEU A 1 105 ? 158.102 131.396 117.751 1.00 60.62  ? 103 LEU A CB  1 
ATOM   663  C  CG  . LEU A 1 105 ? 157.186 132.489 117.180 1.00 58.61  ? 103 LEU A CG  1 
ATOM   664  C  CD1 . LEU A 1 105 ? 157.889 133.833 117.271 1.00 62.40  ? 103 LEU A CD1 1 
ATOM   665  C  CD2 . LEU A 1 105 ? 156.732 132.235 115.745 1.00 61.59  ? 103 LEU A CD2 1 
ATOM   666  N  N   . ILE A 1 106 ? 159.935 128.838 118.222 1.00 53.80  ? 104 ILE A N   1 
ATOM   667  C  CA  . ILE A 1 106 ? 161.226 128.167 118.128 1.00 62.56  ? 104 ILE A CA  1 
ATOM   668  C  C   . ILE A 1 106 ? 161.089 126.872 117.339 1.00 67.96  ? 104 ILE A C   1 
ATOM   669  O  O   . ILE A 1 106 ? 161.994 126.486 116.589 1.00 64.46  ? 104 ILE A O   1 
ATOM   670  C  CB  . ILE A 1 106 ? 161.801 127.931 119.538 1.00 58.12  ? 104 ILE A CB  1 
ATOM   671  C  CG1 . ILE A 1 106 ? 162.525 129.197 120.016 1.00 60.23  ? 104 ILE A CG1 1 
ATOM   672  C  CG2 . ILE A 1 106 ? 162.727 126.714 119.551 1.00 60.08  ? 104 ILE A CG2 1 
ATOM   673  C  CD1 . ILE A 1 106 ? 163.392 129.027 121.255 1.00 61.63  ? 104 ILE A CD1 1 
ATOM   674  N  N   . ALA A 1 107 ? 159.962 126.176 117.500 1.00 66.65  ? 105 ALA A N   1 
ATOM   675  C  CA  . ALA A 1 107 ? 159.720 124.967 116.721 1.00 56.11  ? 105 ALA A CA  1 
ATOM   676  C  C   . ALA A 1 107 ? 159.659 125.285 115.233 1.00 61.87  ? 105 ALA A C   1 
ATOM   677  O  O   . ALA A 1 107 ? 160.292 124.611 114.413 1.00 64.92  ? 105 ALA A O   1 
ATOM   678  C  CB  . ALA A 1 107 ? 158.425 124.300 117.182 1.00 56.90  ? 105 ALA A CB  1 
ATOM   679  N  N   . VAL A 1 108 ? 158.900 126.319 114.868 1.00 66.95  ? 106 VAL A N   1 
ATOM   680  C  CA  . VAL A 1 108 ? 158.769 126.689 113.462 1.00 65.60  ? 106 VAL A CA  1 
ATOM   681  C  C   . VAL A 1 108 ? 160.112 127.141 112.904 1.00 64.25  ? 106 VAL A C   1 
ATOM   682  O  O   . VAL A 1 108 ? 160.499 126.757 111.794 1.00 68.77  ? 106 VAL A O   1 
ATOM   683  C  CB  . VAL A 1 108 ? 157.690 127.776 113.303 1.00 65.08  ? 106 VAL A CB  1 
ATOM   684  C  CG1 . VAL A 1 108 ? 157.693 128.348 111.897 1.00 64.73  ? 106 VAL A CG1 1 
ATOM   685  C  CG2 . VAL A 1 108 ? 156.324 127.212 113.640 1.00 65.98  ? 106 VAL A CG2 1 
ATOM   686  N  N   . ILE A 1 109 ? 160.842 127.963 113.659 1.00 61.42  ? 107 ILE A N   1 
ATOM   687  C  CA  . ILE A 1 109 ? 162.156 128.407 113.206 1.00 63.47  ? 107 ILE A CA  1 
ATOM   688  C  C   . ILE A 1 109 ? 163.082 127.212 113.024 1.00 66.14  ? 107 ILE A C   1 
ATOM   689  O  O   . ILE A 1 109 ? 163.821 127.125 112.037 1.00 64.69  ? 107 ILE A O   1 
ATOM   690  C  CB  . ILE A 1 109 ? 162.738 129.439 114.193 1.00 64.58  ? 107 ILE A CB  1 
ATOM   691  C  CG1 . ILE A 1 109 ? 161.997 130.776 114.059 1.00 63.02  ? 107 ILE A CG1 1 
ATOM   692  C  CG2 . ILE A 1 109 ? 164.250 129.606 113.996 1.00 66.96  ? 107 ILE A CG2 1 
ATOM   693  C  CD1 . ILE A 1 109 ? 162.426 131.627 112.877 1.00 62.43  ? 107 ILE A CD1 1 
ATOM   694  N  N   . LEU A 1 110 ? 163.057 126.273 113.972 1.00 66.51  ? 108 LEU A N   1 
ATOM   695  C  CA  . LEU A 1 110 ? 163.875 125.072 113.836 1.00 65.27  ? 108 LEU A CA  1 
ATOM   696  C  C   . LEU A 1 110 ? 163.462 124.262 112.615 1.00 66.11  ? 108 LEU A C   1 
ATOM   697  O  O   . LEU A 1 110 ? 164.317 123.771 111.869 1.00 66.96  ? 108 LEU A O   1 
ATOM   698  C  CB  . LEU A 1 110 ? 163.771 124.222 115.101 1.00 66.08  ? 108 LEU A CB  1 
ATOM   699  C  CG  . LEU A 1 110 ? 164.340 122.805 115.003 1.00 63.77  ? 108 LEU A CG  1 
ATOM   700  C  CD1 . LEU A 1 110 ? 165.804 122.839 114.596 1.00 66.06  ? 108 LEU A CD1 1 
ATOM   701  C  CD2 . LEU A 1 110 ? 164.174 122.080 116.320 1.00 62.70  ? 108 LEU A CD2 1 
ATOM   702  N  N   . GLY A 1 111 ? 162.156 124.106 112.395 1.00 65.49  ? 109 GLY A N   1 
ATOM   703  C  CA  . GLY A 1 111 ? 161.699 123.354 111.240 1.00 66.65  ? 109 GLY A CA  1 
ATOM   704  C  C   . GLY A 1 111 ? 162.041 124.032 109.927 1.00 69.02  ? 109 GLY A C   1 
ATOM   705  O  O   . GLY A 1 111 ? 162.483 123.379 108.978 1.00 65.19  ? 109 GLY A O   1 
ATOM   706  N  N   . ILE A 1 112 ? 161.845 125.350 109.853 1.00 74.13  ? 110 ILE A N   1 
ATOM   707  C  CA  . ILE A 1 112 ? 162.132 126.070 108.617 1.00 73.35  ? 110 ILE A CA  1 
ATOM   708  C  C   . ILE A 1 112 ? 163.620 126.011 108.301 1.00 75.88  ? 110 ILE A C   1 
ATOM   709  O  O   . ILE A 1 112 ? 164.016 125.814 107.147 1.00 78.31  ? 110 ILE A O   1 
ATOM   710  C  CB  . ILE A 1 112 ? 161.621 127.520 108.714 1.00 70.75  ? 110 ILE A CB  1 
ATOM   711  C  CG1 . ILE A 1 112 ? 160.104 127.539 108.527 1.00 70.86  ? 110 ILE A CG1 1 
ATOM   712  C  CG2 . ILE A 1 112 ? 162.293 128.414 107.672 1.00 71.63  ? 110 ILE A CG2 1 
ATOM   713  C  CD1 . ILE A 1 112 ? 159.457 128.850 108.879 1.00 73.01  ? 110 ILE A CD1 1 
ATOM   714  N  N   . VAL A 1 113 ? 164.469 126.181 109.316 1.00 69.18  ? 111 VAL A N   1 
ATOM   715  C  CA  . VAL A 1 113 ? 165.908 126.108 109.084 1.00 69.20  ? 111 VAL A CA  1 
ATOM   716  C  C   . VAL A 1 113 ? 166.292 124.739 108.543 1.00 71.68  ? 111 VAL A C   1 
ATOM   717  O  O   . VAL A 1 113 ? 167.256 124.613 107.778 1.00 70.10  ? 111 VAL A O   1 
ATOM   718  C  CB  . VAL A 1 113 ? 166.670 126.443 110.382 1.00 69.09  ? 111 VAL A CB  1 
ATOM   719  C  CG1 . VAL A 1 113 ? 168.141 126.045 110.276 1.00 69.32  ? 111 VAL A CG1 1 
ATOM   720  C  CG2 . VAL A 1 113 ? 166.544 127.922 110.700 1.00 69.32  ? 111 VAL A CG2 1 
ATOM   721  N  N   . LEU A 1 114 ? 165.555 123.695 108.925 1.00 67.81  ? 112 LEU A N   1 
ATOM   722  C  CA  . LEU A 1 114 ? 165.904 122.350 108.483 1.00 67.54  ? 112 LEU A CA  1 
ATOM   723  C  C   . LEU A 1 114 ? 165.572 122.143 107.010 1.00 71.47  ? 112 LEU A C   1 
ATOM   724  O  O   . LEU A 1 114 ? 166.384 121.591 106.259 1.00 75.33  ? 112 LEU A O   1 
ATOM   725  C  CB  . LEU A 1 114 ? 165.184 121.315 109.346 1.00 70.22  ? 112 LEU A CB  1 
ATOM   726  C  CG  . LEU A 1 114 ? 165.757 121.080 110.746 1.00 68.92  ? 112 LEU A CG  1 
ATOM   727  C  CD1 . LEU A 1 114 ? 164.850 120.156 111.533 1.00 71.00  ? 112 LEU A CD1 1 
ATOM   728  C  CD2 . LEU A 1 114 ? 167.163 120.504 110.682 1.00 67.06  ? 112 LEU A CD2 1 
ATOM   729  N  N   . VAL A 1 115 ? 164.387 122.577 106.576 1.00 74.78  ? 113 VAL A N   1 
ATOM   730  C  CA  . VAL A 1 115 ? 163.975 122.330 105.194 1.00 75.95  ? 113 VAL A CA  1 
ATOM   731  C  C   . VAL A 1 115 ? 164.920 123.031 104.227 1.00 74.63  ? 113 VAL A C   1 
ATOM   732  O  O   . VAL A 1 115 ? 165.362 122.447 103.231 1.00 72.87  ? 113 VAL A O   1 
ATOM   733  C  CB  . VAL A 1 115 ? 162.515 122.769 104.963 1.00 75.88  ? 113 VAL A CB  1 
ATOM   734  C  CG1 . VAL A 1 115 ? 161.558 121.693 105.436 1.00 73.25  ? 113 VAL A CG1 1 
ATOM   735  C  CG2 . VAL A 1 115 ? 162.209 124.108 105.629 1.00 75.29  ? 113 VAL A CG2 1 
ATOM   736  N  N   . VAL A 1 116 ? 165.250 124.293 104.508 1.00 74.04  ? 114 VAL A N   1 
ATOM   737  C  CA  . VAL A 1 116 ? 166.166 125.017 103.631 1.00 74.93  ? 114 VAL A CA  1 
ATOM   738  C  C   . VAL A 1 116 ? 167.554 124.392 103.676 1.00 74.07  ? 114 VAL A C   1 
ATOM   739  O  O   . VAL A 1 116 ? 168.296 124.440 102.687 1.00 70.79  ? 114 VAL A O   1 
ATOM   740  C  CB  . VAL A 1 116 ? 166.202 126.519 103.987 1.00 75.26  ? 114 VAL A CB  1 
ATOM   741  C  CG1 . VAL A 1 116 ? 164.798 127.059 104.244 1.00 69.90  ? 114 VAL A CG1 1 
ATOM   742  C  CG2 . VAL A 1 116 ? 167.092 126.775 105.200 1.00 75.15  ? 114 VAL A CG2 1 
ATOM   743  N  N   . SER A 1 117 ? 167.933 123.804 104.810 1.00 75.38  ? 115 SER A N   1 
ATOM   744  C  CA  . SER A 1 117 ? 169.230 123.143 104.912 1.00 77.11  ? 115 SER A CA  1 
ATOM   745  C  C   . SER A 1 117 ? 169.192 121.758 104.274 1.00 78.32  ? 115 SER A C   1 
ATOM   746  O  O   . SER A 1 117 ? 169.942 121.472 103.336 1.00 74.67  ? 115 SER A O   1 
ATOM   747  C  CB  . SER A 1 117 ? 169.653 123.049 106.379 1.00 75.51  ? 115 SER A CB  1 
ATOM   748  O  OG  . SER A 1 117 ? 170.770 122.191 106.531 1.00 78.98  ? 115 SER A OG  1 
ATOM   749  N  N   . ILE A 1 118 ? 168.317 120.884 104.776 1.00 79.61  ? 116 ILE A N   1 
ATOM   750  C  CA  . ILE A 1 118 ? 168.242 119.524 104.253 1.00 77.58  ? 116 ILE A CA  1 
ATOM   751  C  C   . ILE A 1 118 ? 167.691 119.525 102.832 1.00 76.05  ? 116 ILE A C   1 
ATOM   752  O  O   . ILE A 1 118 ? 168.127 118.738 101.983 1.00 74.54  ? 116 ILE A O   1 
ATOM   753  C  CB  . ILE A 1 118 ? 167.397 118.637 105.186 1.00 76.39  ? 116 ILE A CB  1 
ATOM   754  C  CG1 . ILE A 1 118 ? 167.877 118.789 106.636 1.00 73.96  ? 116 ILE A CG1 1 
ATOM   755  C  CG2 . ILE A 1 118 ? 167.463 117.184 104.726 1.00 78.11  ? 116 ILE A CG2 1 
ATOM   756  C  CD1 . ILE A 1 118 ? 167.177 117.887 107.637 1.00 76.05  ? 116 ILE A CD1 1 
ATOM   757  N  N   . LYS A 1 119 ? 166.726 120.399 102.551 1.00 77.34  ? 117 LYS A N   1 
ATOM   758  C  CA  . LYS A 1 119 ? 166.119 120.486 101.229 1.00 79.90  ? 117 LYS A CA  1 
ATOM   759  C  C   . LYS A 1 119 ? 165.528 119.138 100.837 1.00 80.55  ? 117 LYS A C   1 
ATOM   760  O  O   . LYS A 1 119 ? 166.016 118.495 99.899  1.00 84.18  ? 117 LYS A O   1 
ATOM   761  C  CB  . LYS A 1 119 ? 167.145 120.939 100.188 1.00 83.31  ? 117 LYS A CB  1 
ATOM   762  C  CG  . LYS A 1 119 ? 167.533 122.403 100.305 1.00 83.31  ? 117 LYS A CG  1 
ATOM   763  C  CD  . LYS A 1 119 ? 168.639 122.773 99.327  1.00 81.15  ? 117 LYS A CD  1 
ATOM   764  C  CE  . LYS A 1 119 ? 169.994 122.247 99.778  1.00 82.20  ? 117 LYS A CE  1 
ATOM   765  N  NZ  . LYS A 1 119 ? 170.372 122.736 101.133 1.00 79.91  ? 117 LYS A NZ  1 
ATOM   766  N  N   . PRO A 1 120 ? 164.484 118.676 101.528 1.00 76.79  ? 118 PRO A N   1 
ATOM   767  C  CA  . PRO A 1 120 ? 163.867 117.398 101.140 1.00 79.41  ? 118 PRO A CA  1 
ATOM   768  C  C   . PRO A 1 120 ? 163.329 117.396 99.721  1.00 82.10  ? 118 PRO A C   1 
ATOM   769  O  O   . PRO A 1 120 ? 163.300 116.338 99.081  1.00 80.65  ? 118 PRO A O   1 
ATOM   770  C  CB  . PRO A 1 120 ? 162.745 117.218 102.173 1.00 77.78  ? 118 PRO A CB  1 
ATOM   771  C  CG  . PRO A 1 120 ? 162.506 118.574 102.742 1.00 76.64  ? 118 PRO A CG  1 
ATOM   772  C  CD  . PRO A 1 120 ? 163.815 119.290 102.685 1.00 78.08  ? 118 PRO A CD  1 
ATOM   773  N  N   . GLY A 1 121 ? 162.899 118.545 99.210  1.00 82.69  ? 119 GLY A N   1 
ATOM   774  C  CA  . GLY A 1 121 ? 162.377 118.629 97.860  1.00 81.25  ? 119 GLY A CA  1 
ATOM   775  C  C   . GLY A 1 121 ? 163.463 118.842 96.823  1.00 80.57  ? 119 GLY A C   1 
ATOM   776  O  O   . GLY A 1 121 ? 164.647 118.655 97.103  1.00 78.52  ? 119 GLY A O   1 
ATOM   777  N  N   . SER A 1 139 ? 146.025 136.651 99.438  1.00 65.03  ? 137 SER A N   1 
ATOM   778  C  CA  . SER A 1 139 ? 145.139 136.400 100.567 1.00 67.74  ? 137 SER A CA  1 
ATOM   779  C  C   . SER A 1 139 ? 145.934 136.111 101.834 1.00 65.40  ? 137 SER A C   1 
ATOM   780  O  O   . SER A 1 139 ? 145.440 135.450 102.747 1.00 62.12  ? 137 SER A O   1 
ATOM   781  C  CB  . SER A 1 139 ? 144.203 135.229 100.263 1.00 67.12  ? 137 SER A CB  1 
ATOM   782  O  OG  . SER A 1 139 ? 144.925 134.016 100.143 1.00 67.11  ? 137 SER A OG  1 
ATOM   783  N  N   . THR A 1 140 ? 147.173 136.605 101.884 1.00 73.04  ? 138 THR A N   1 
ATOM   784  C  CA  . THR A 1 140 ? 148.003 136.381 103.063 1.00 77.77  ? 138 THR A CA  1 
ATOM   785  C  C   . THR A 1 140 ? 147.390 137.026 104.300 1.00 76.44  ? 138 THR A C   1 
ATOM   786  O  O   . THR A 1 140 ? 147.381 136.427 105.381 1.00 73.47  ? 138 THR A O   1 
ATOM   787  C  CB  . THR A 1 140 ? 149.420 136.914 102.829 1.00 79.14  ? 138 THR A CB  1 
ATOM   788  O  OG1 . THR A 1 140 ? 150.182 136.794 104.037 1.00 79.09  ? 138 THR A OG1 1 
ATOM   789  C  CG2 . THR A 1 140 ? 149.402 138.379 102.394 1.00 75.80  ? 138 THR A CG2 1 
ATOM   790  N  N   . VAL A 1 141 ? 146.879 138.251 104.163 1.00 71.18  ? 139 VAL A N   1 
ATOM   791  C  CA  . VAL A 1 141 ? 146.269 138.930 105.301 1.00 65.99  ? 139 VAL A CA  1 
ATOM   792  C  C   . VAL A 1 141 ? 144.933 138.288 105.656 1.00 61.58  ? 139 VAL A C   1 
ATOM   793  O  O   . VAL A 1 141 ? 144.615 138.102 106.835 1.00 64.45  ? 139 VAL A O   1 
ATOM   794  C  CB  . VAL A 1 141 ? 146.124 140.436 105.007 1.00 62.50  ? 139 VAL A CB  1 
ATOM   795  C  CG1 . VAL A 1 141 ? 145.213 140.680 103.809 1.00 65.18  ? 139 VAL A CG1 1 
ATOM   796  C  CG2 . VAL A 1 141 ? 145.611 141.171 106.235 1.00 64.72  ? 139 VAL A CG2 1 
ATOM   797  N  N   . ASP A 1 142 ? 144.134 137.933 104.647 1.00 56.22  ? 140 ASP A N   1 
ATOM   798  C  CA  . ASP A 1 142 ? 142.810 137.382 104.915 1.00 60.03  ? 140 ASP A CA  1 
ATOM   799  C  C   . ASP A 1 142 ? 142.887 136.113 105.752 1.00 58.42  ? 140 ASP A C   1 
ATOM   800  O  O   . ASP A 1 142 ? 141.992 135.850 106.561 1.00 58.43  ? 140 ASP A O   1 
ATOM   801  C  CB  . ASP A 1 142 ? 142.082 137.102 103.601 1.00 64.32  ? 140 ASP A CB  1 
ATOM   802  C  CG  . ASP A 1 142 ? 141.777 138.366 102.825 1.00 67.02  ? 140 ASP A CG  1 
ATOM   803  O  OD1 . ASP A 1 142 ? 142.162 139.459 103.288 1.00 68.19  ? 140 ASP A OD1 1 
ATOM   804  O  OD2 . ASP A 1 142 ? 141.150 138.267 101.751 1.00 65.87  ? 140 ASP A OD2 1 
ATOM   805  N  N   . ALA A 1 143 ? 143.936 135.310 105.569 1.00 61.82  ? 141 ALA A N   1 
ATOM   806  C  CA  . ALA A 1 143 ? 144.102 134.125 106.402 1.00 60.17  ? 141 ALA A CA  1 
ATOM   807  C  C   . ALA A 1 143 ? 144.321 134.507 107.860 1.00 59.29  ? 141 ALA A C   1 
ATOM   808  O  O   . ALA A 1 143 ? 143.763 133.877 108.766 1.00 60.18  ? 141 ALA A O   1 
ATOM   809  C  CB  . ALA A 1 143 ? 145.268 133.281 105.890 1.00 64.25  ? 141 ALA A CB  1 
ATOM   810  N  N   . MET A 1 144 ? 145.137 135.533 108.106 1.00 61.14  ? 142 MET A N   1 
ATOM   811  C  CA  . MET A 1 144 ? 145.375 135.973 109.476 1.00 59.43  ? 142 MET A CA  1 
ATOM   812  C  C   . MET A 1 144 ? 144.118 136.571 110.090 1.00 63.22  ? 142 MET A C   1 
ATOM   813  O  O   . MET A 1 144 ? 143.807 136.311 111.258 1.00 69.79  ? 142 MET A O   1 
ATOM   814  C  CB  . MET A 1 144 ? 146.520 136.983 109.510 1.00 60.99  ? 142 MET A CB  1 
ATOM   815  C  CG  . MET A 1 144 ? 147.782 136.518 108.800 1.00 67.73  ? 142 MET A CG  1 
ATOM   816  S  SD  . MET A 1 144 ? 147.878 134.728 108.610 1.00 80.55  ? 142 MET A SD  1 
ATOM   817  C  CE  . MET A 1 144 ? 148.299 134.237 110.277 1.00 65.70  ? 142 MET A CE  1 
ATOM   818  N  N   . LEU A 1 145 ? 143.381 137.376 109.323 1.00 57.45  ? 143 LEU A N   1 
ATOM   819  C  CA  . LEU A 1 145 ? 142.170 137.988 109.857 1.00 49.77  ? 143 LEU A CA  1 
ATOM   820  C  C   . LEU A 1 145 ? 141.141 136.929 110.226 1.00 44.35  ? 143 LEU A C   1 
ATOM   821  O  O   . LEU A 1 145 ? 140.469 137.041 111.257 1.00 56.67  ? 143 LEU A O   1 
ATOM   822  C  CB  . LEU A 1 145 ? 141.591 138.977 108.846 1.00 49.86  ? 143 LEU A CB  1 
ATOM   823  C  CG  . LEU A 1 145 ? 142.506 140.122 108.398 1.00 51.69  ? 143 LEU A CG  1 
ATOM   824  C  CD1 . LEU A 1 145 ? 141.705 141.182 107.665 1.00 52.23  ? 143 LEU A CD1 1 
ATOM   825  C  CD2 . LEU A 1 145 ? 143.261 140.742 109.567 1.00 49.75  ? 143 LEU A CD2 1 
ATOM   826  N  N   . ASP A 1 146 ? 141.004 135.890 109.399 1.00 41.42  ? 144 ASP A N   1 
ATOM   827  C  CA  . ASP A 1 146 ? 140.067 134.819 109.719 1.00 43.53  ? 144 ASP A CA  1 
ATOM   828  C  C   . ASP A 1 146 ? 140.384 134.190 111.067 1.00 44.15  ? 144 ASP A C   1 
ATOM   829  O  O   . ASP A 1 146 ? 139.492 133.636 111.718 1.00 49.96  ? 144 ASP A O   1 
ATOM   830  C  CB  . ASP A 1 146 ? 140.090 133.750 108.628 1.00 46.54  ? 144 ASP A CB  1 
ATOM   831  C  CG  . ASP A 1 146 ? 139.639 134.279 107.287 1.00 50.90  ? 144 ASP A CG  1 
ATOM   832  O  OD1 . ASP A 1 146 ? 139.350 135.488 107.191 1.00 58.72  ? 144 ASP A OD1 1 
ATOM   833  O  OD2 . ASP A 1 146 ? 139.574 133.485 106.327 1.00 47.56  ? 144 ASP A OD2 1 
ATOM   834  N  N   . LEU A 1 147 ? 141.646 134.252 111.497 1.00 48.66  ? 145 LEU A N   1 
ATOM   835  C  CA  . LEU A 1 147 ? 142.001 133.726 112.810 1.00 49.83  ? 145 LEU A CA  1 
ATOM   836  C  C   . LEU A 1 147 ? 141.404 134.577 113.921 1.00 41.32  ? 145 LEU A C   1 
ATOM   837  O  O   . LEU A 1 147 ? 140.873 134.043 114.899 1.00 45.29  ? 145 LEU A O   1 
ATOM   838  C  CB  . LEU A 1 147 ? 143.520 133.653 112.952 1.00 53.04  ? 145 LEU A CB  1 
ATOM   839  C  CG  . LEU A 1 147 ? 144.030 132.663 114.000 1.00 55.24  ? 145 LEU A CG  1 
ATOM   840  C  CD1 . LEU A 1 147 ? 144.118 131.265 113.413 1.00 49.03  ? 145 LEU A CD1 1 
ATOM   841  C  CD2 . LEU A 1 147 ? 145.375 133.107 114.548 1.00 58.29  ? 145 LEU A CD2 1 
ATOM   842  N  N   . ILE A 1 148 ? 141.480 135.903 113.788 1.00 35.31  ? 146 ILE A N   1 
ATOM   843  C  CA  . ILE A 1 148 ? 140.882 136.783 114.787 1.00 43.40  ? 146 ILE A CA  1 
ATOM   844  C  C   . ILE A 1 148 ? 139.362 136.734 114.695 1.00 38.34  ? 146 ILE A C   1 
ATOM   845  O  O   . ILE A 1 148 ? 138.663 136.807 115.712 1.00 39.31  ? 146 ILE A O   1 
ATOM   846  C  CB  . ILE A 1 148 ? 141.417 138.218 114.634 1.00 40.51  ? 146 ILE A CB  1 
ATOM   847  C  CG1 . ILE A 1 148 ? 142.949 138.210 114.630 1.00 42.42  ? 146 ILE A CG1 1 
ATOM   848  C  CG2 . ILE A 1 148 ? 140.882 139.099 115.756 1.00 38.65  ? 146 ILE A CG2 1 
ATOM   849  C  CD1 . ILE A 1 148 ? 143.587 139.574 114.466 1.00 44.75  ? 146 ILE A CD1 1 
ATOM   850  N  N   . ARG A 1 149 ? 138.825 136.615 113.480 1.00 34.16  ? 147 ARG A N   1 
ATOM   851  C  CA  . ARG A 1 149 ? 137.386 136.455 113.324 1.00 29.87  ? 147 ARG A CA  1 
ATOM   852  C  C   . ARG A 1 149 ? 136.889 135.159 113.947 1.00 44.78  ? 147 ARG A C   1 
ATOM   853  O  O   . ARG A 1 149 ? 135.679 135.005 114.147 1.00 50.00  ? 147 ARG A O   1 
ATOM   854  C  CB  . ARG A 1 149 ? 137.004 136.489 111.845 1.00 30.79  ? 147 ARG A CB  1 
ATOM   855  C  CG  . ARG A 1 149 ? 137.166 137.843 111.190 1.00 35.52  ? 147 ARG A CG  1 
ATOM   856  C  CD  . ARG A 1 149 ? 136.796 137.776 109.722 1.00 33.78  ? 147 ARG A CD  1 
ATOM   857  N  NE  . ARG A 1 149 ? 136.943 139.063 109.052 1.00 38.75  ? 147 ARG A NE  1 
ATOM   858  C  CZ  . ARG A 1 149 ? 137.773 139.312 108.046 1.00 47.10  ? 147 ARG A CZ  1 
ATOM   859  N  NH1 . ARG A 1 149 ? 138.581 138.382 107.563 1.00 45.98  ? 147 ARG A NH1 1 
ATOM   860  N  NH2 . ARG A 1 149 ? 137.792 140.528 107.509 1.00 49.07  ? 147 ARG A NH2 1 
ATOM   861  N  N   . ASN A 1 150 ? 137.791 134.224 114.248 1.00 42.47  ? 148 ASN A N   1 
ATOM   862  C  CA  . ASN A 1 150 ? 137.425 132.966 114.881 1.00 28.52  ? 148 ASN A CA  1 
ATOM   863  C  C   . ASN A 1 150 ? 137.687 132.952 116.380 1.00 28.73  ? 148 ASN A C   1 
ATOM   864  O  O   . ASN A 1 150 ? 137.104 132.121 117.082 1.00 40.61  ? 148 ASN A O   1 
ATOM   865  C  CB  . ASN A 1 150 ? 138.186 131.808 114.229 1.00 32.74  ? 148 ASN A CB  1 
ATOM   866  C  CG  . ASN A 1 150 ? 137.548 131.351 112.936 1.00 32.76  ? 148 ASN A CG  1 
ATOM   867  O  OD1 . ASN A 1 150 ? 136.371 131.000 112.903 1.00 41.81  ? 148 ASN A OD1 1 
ATOM   868  N  ND2 . ASN A 1 150 ? 138.322 131.357 111.860 1.00 33.32  ? 148 ASN A ND2 1 
ATOM   869  N  N   . MET A 1 151 ? 138.546 133.840 116.886 1.00 25.00  ? 149 MET A N   1 
ATOM   870  C  CA  . MET A 1 151 ? 138.688 133.974 118.331 1.00 24.14  ? 149 MET A CA  1 
ATOM   871  C  C   . MET A 1 151 ? 137.418 134.522 118.962 1.00 32.98  ? 149 MET A C   1 
ATOM   872  O  O   . MET A 1 151 ? 137.160 134.279 120.146 1.00 32.31  ? 149 MET A O   1 
ATOM   873  C  CB  . MET A 1 151 ? 139.864 134.886 118.672 1.00 25.24  ? 149 MET A CB  1 
ATOM   874  C  CG  . MET A 1 151 ? 141.184 134.475 118.044 1.00 32.72  ? 149 MET A CG  1 
ATOM   875  S  SD  . MET A 1 151 ? 142.667 135.298 118.680 1.00 59.18  ? 149 MET A SD  1 
ATOM   876  C  CE  . MET A 1 151 ? 142.077 136.158 120.137 1.00 37.76  ? 149 MET A CE  1 
ATOM   877  N  N   . PHE A 1 152 ? 136.620 135.261 118.194 1.00 31.25  ? 150 PHE A N   1 
ATOM   878  C  CA  . PHE A 1 152 ? 135.387 135.881 118.675 1.00 21.69  ? 150 PHE A CA  1 
ATOM   879  C  C   . PHE A 1 152 ? 134.263 135.474 117.734 1.00 28.80  ? 150 PHE A C   1 
ATOM   880  O  O   . PHE A 1 152 ? 133.846 136.258 116.871 1.00 34.77  ? 150 PHE A O   1 
ATOM   881  C  CB  . PHE A 1 152 ? 135.527 137.401 118.751 1.00 14.10  ? 150 PHE A CB  1 
ATOM   882  C  CG  . PHE A 1 152 ? 136.755 137.857 119.481 1.00 24.29  ? 150 PHE A CG  1 
ATOM   883  C  CD1 . PHE A 1 152 ? 136.803 137.837 120.862 1.00 26.88  ? 150 PHE A CD1 1 
ATOM   884  C  CD2 . PHE A 1 152 ? 137.866 138.297 118.785 1.00 29.80  ? 150 PHE A CD2 1 
ATOM   885  C  CE1 . PHE A 1 152 ? 137.932 138.252 121.534 1.00 25.22  ? 150 PHE A CE1 1 
ATOM   886  C  CE2 . PHE A 1 152 ? 138.996 138.713 119.453 1.00 22.98  ? 150 PHE A CE2 1 
ATOM   887  C  CZ  . PHE A 1 152 ? 139.029 138.690 120.828 1.00 24.68  ? 150 PHE A CZ  1 
ATOM   888  N  N   . PRO A 1 153 ? 133.755 134.252 117.863 1.00 27.60  ? 151 PRO A N   1 
ATOM   889  C  CA  . PRO A 1 153 ? 132.679 133.808 116.975 1.00 12.23  ? 151 PRO A CA  1 
ATOM   890  C  C   . PRO A 1 153 ? 131.392 134.575 117.232 1.00 16.61  ? 151 PRO A C   1 
ATOM   891  O  O   . PRO A 1 153 ? 131.164 135.126 118.310 1.00 33.61  ? 151 PRO A O   1 
ATOM   892  C  CB  . PRO A 1 153 ? 132.524 132.325 117.318 1.00 20.78  ? 151 PRO A CB  1 
ATOM   893  C  CG  . PRO A 1 153 ? 133.021 132.209 118.709 1.00 14.77  ? 151 PRO A CG  1 
ATOM   894  C  CD  . PRO A 1 153 ? 134.123 133.214 118.840 1.00 26.26  ? 151 PRO A CD  1 
ATOM   895  N  N   . GLU A 1 154 ? 130.544 134.608 116.208 1.00 7.11   ? 152 GLU A N   1 
ATOM   896  C  CA  . GLU A 1 154 ? 129.257 135.282 116.304 1.00 8.26   ? 152 GLU A CA  1 
ATOM   897  C  C   . GLU A 1 154 ? 128.192 134.435 116.986 1.00 26.67  ? 152 GLU A C   1 
ATOM   898  O  O   . GLU A 1 154 ? 127.066 134.911 117.160 1.00 40.48  ? 152 GLU A O   1 
ATOM   899  C  CB  . GLU A 1 154 ? 128.769 135.676 114.910 1.00 20.07  ? 152 GLU A CB  1 
ATOM   900  C  CG  . GLU A 1 154 ? 129.527 136.830 114.291 1.00 25.92  ? 152 GLU A CG  1 
ATOM   901  C  CD  . GLU A 1 154 ? 129.173 137.044 112.834 1.00 34.32  ? 152 GLU A CD  1 
ATOM   902  O  OE1 . GLU A 1 154 ? 128.450 136.200 112.265 1.00 34.92  ? 152 GLU A OE1 1 
ATOM   903  O  OE2 . GLU A 1 154 ? 129.613 138.059 112.256 1.00 40.02  ? 152 GLU A OE2 1 
ATOM   904  N  N   . ASN A 1 155 ? 128.509 133.200 117.368 1.00 22.03  ? 153 ASN A N   1 
ATOM   905  C  CA  . ASN A 1 155 ? 127.529 132.325 117.997 1.00 20.06  ? 153 ASN A CA  1 
ATOM   906  C  C   . ASN A 1 155 ? 128.275 131.177 118.658 1.00 15.24  ? 153 ASN A C   1 
ATOM   907  O  O   . ASN A 1 155 ? 129.078 130.505 118.006 1.00 28.19  ? 153 ASN A O   1 
ATOM   908  C  CB  . ASN A 1 155 ? 126.518 131.808 116.968 1.00 22.13  ? 153 ASN A CB  1 
ATOM   909  C  CG  . ASN A 1 155 ? 125.320 131.139 117.608 1.00 24.20  ? 153 ASN A CG  1 
ATOM   910  O  OD1 . ASN A 1 155 ? 124.907 131.498 118.709 1.00 28.35  ? 153 ASN A OD1 1 
ATOM   911  N  ND2 . ASN A 1 155 ? 124.746 130.169 116.915 1.00 33.38  ? 153 ASN A ND2 1 
ATOM   912  N  N   . LEU A 1 156 ? 128.020 130.964 119.950 1.00 17.72  ? 154 LEU A N   1 
ATOM   913  C  CA  . LEU A 1 156 ? 128.681 129.874 120.660 1.00 23.82  ? 154 LEU A CA  1 
ATOM   914  C  C   . LEU A 1 156 ? 128.206 128.514 120.166 1.00 25.85  ? 154 LEU A C   1 
ATOM   915  O  O   . LEU A 1 156 ? 129.018 127.604 119.967 1.00 34.42  ? 154 LEU A O   1 
ATOM   916  C  CB  . LEU A 1 156 ? 128.439 130.003 122.162 1.00 25.55  ? 154 LEU A CB  1 
ATOM   917  C  CG  . LEU A 1 156 ? 129.030 131.230 122.856 1.00 27.90  ? 154 LEU A CG  1 
ATOM   918  C  CD1 . LEU A 1 156 ? 128.698 131.193 124.335 1.00 21.43  ? 154 LEU A CD1 1 
ATOM   919  C  CD2 . LEU A 1 156 ? 130.536 131.315 122.647 1.00 24.39  ? 154 LEU A CD2 1 
ATOM   920  N  N   . VAL A 1 157 ? 126.898 128.348 119.970 1.00 18.58  ? 155 VAL A N   1 
ATOM   921  C  CA  . VAL A 1 157 ? 126.381 127.057 119.524 1.00 11.64  ? 155 VAL A CA  1 
ATOM   922  C  C   . VAL A 1 157 ? 126.940 126.710 118.151 1.00 21.29  ? 155 VAL A C   1 
ATOM   923  O  O   . VAL A 1 157 ? 127.360 125.574 117.906 1.00 33.22  ? 155 VAL A O   1 
ATOM   924  C  CB  . VAL A 1 157 ? 124.841 127.068 119.531 1.00 12.79  ? 155 VAL A CB  1 
ATOM   925  C  CG1 . VAL A 1 157 ? 124.279 125.862 118.786 1.00 19.58  ? 155 VAL A CG1 1 
ATOM   926  C  CG2 . VAL A 1 157 ? 124.323 127.099 120.956 1.00 16.98  ? 155 VAL A CG2 1 
ATOM   927  N  N   . GLN A 1 158 ? 126.948 127.676 117.232 1.00 23.53  ? 156 GLN A N   1 
ATOM   928  C  CA  . GLN A 1 158 ? 127.519 127.429 115.912 1.00 11.97  ? 156 GLN A CA  1 
ATOM   929  C  C   . GLN A 1 158 ? 129.020 127.193 115.996 1.00 17.67  ? 156 GLN A C   1 
ATOM   930  O  O   . GLN A 1 158 ? 129.558 126.335 115.290 1.00 32.57  ? 156 GLN A O   1 
ATOM   931  C  CB  . GLN A 1 158 ? 127.220 128.601 114.983 1.00 16.13  ? 156 GLN A CB  1 
ATOM   932  C  CG  . GLN A 1 158 ? 127.671 128.383 113.556 1.00 10.10  ? 156 GLN A CG  1 
ATOM   933  C  CD  . GLN A 1 158 ? 127.048 129.373 112.598 1.00 24.02  ? 156 GLN A CD  1 
ATOM   934  O  OE1 . GLN A 1 158 ? 127.037 130.575 112.853 1.00 29.56  ? 156 GLN A OE1 1 
ATOM   935  N  NE2 . GLN A 1 158 ? 126.529 128.873 111.484 1.00 30.99  ? 156 GLN A NE2 1 
ATOM   936  N  N   . ALA A 1 159 ? 129.714 127.948 116.849 1.00 22.46  ? 157 ALA A N   1 
ATOM   937  C  CA  . ALA A 1 159 ? 131.153 127.768 116.996 1.00 14.26  ? 157 ALA A CA  1 
ATOM   938  C  C   . ALA A 1 159 ? 131.510 126.362 117.449 1.00 24.82  ? 157 ALA A C   1 
ATOM   939  O  O   . ALA A 1 159 ? 132.645 125.924 117.240 1.00 32.69  ? 157 ALA A O   1 
ATOM   940  C  CB  . ALA A 1 159 ? 131.712 128.785 117.989 1.00 13.07  ? 157 ALA A CB  1 
ATOM   941  N  N   . ALA A 1 160 ? 130.570 125.645 118.066 1.00 26.53  ? 158 ALA A N   1 
ATOM   942  C  CA  . ALA A 1 160 ? 130.853 124.298 118.537 1.00 16.79  ? 158 ALA A CA  1 
ATOM   943  C  C   . ALA A 1 160 ? 131.084 123.318 117.398 1.00 17.25  ? 158 ALA A C   1 
ATOM   944  O  O   . ALA A 1 160 ? 131.703 122.274 117.619 1.00 35.12  ? 158 ALA A O   1 
ATOM   945  C  CB  . ALA A 1 160 ? 129.710 123.799 119.419 1.00 14.38  ? 158 ALA A CB  1 
ATOM   946  N  N   . PHE A 1 161 ? 130.589 123.612 116.191 1.00 11.57  ? 159 PHE A N   1 
ATOM   947  C  CA  . PHE A 1 161 ? 130.775 122.696 115.073 1.00 17.71  ? 159 PHE A CA  1 
ATOM   948  C  C   . PHE A 1 161 ? 131.034 123.386 113.739 1.00 22.28  ? 159 PHE A C   1 
ATOM   949  O  O   . PHE A 1 161 ? 131.106 122.695 112.716 1.00 30.40  ? 159 PHE A O   1 
ATOM   950  C  CB  . PHE A 1 161 ? 129.556 121.778 114.936 1.00 20.93  ? 159 PHE A CB  1 
ATOM   951  C  CG  . PHE A 1 161 ? 128.337 122.465 114.397 1.00 15.08  ? 159 PHE A CG  1 
ATOM   952  C  CD1 . PHE A 1 161 ? 127.567 123.273 115.209 1.00 7.48   ? 159 PHE A CD1 1 
ATOM   953  C  CD2 . PHE A 1 161 ? 127.963 122.302 113.077 1.00 19.93  ? 159 PHE A CD2 1 
ATOM   954  C  CE1 . PHE A 1 161 ? 126.450 123.904 114.716 1.00 16.58  ? 159 PHE A CE1 1 
ATOM   955  C  CE2 . PHE A 1 161 ? 126.847 122.932 112.580 1.00 19.30  ? 159 PHE A CE2 1 
ATOM   956  C  CZ  . PHE A 1 161 ? 126.090 123.734 113.400 1.00 24.65  ? 159 PHE A CZ  1 
ATOM   957  N  N   . GLN A 1 162 ? 131.175 124.709 113.700 1.00 13.26  ? 160 GLN A N   1 
ATOM   958  C  CA  . GLN A 1 162 ? 131.379 125.416 112.444 1.00 6.07   ? 160 GLN A CA  1 
ATOM   959  C  C   . GLN A 1 162 ? 132.463 126.470 112.606 1.00 21.11  ? 160 GLN A C   1 
ATOM   960  O  O   . GLN A 1 162 ? 132.685 126.994 113.699 1.00 26.96  ? 160 GLN A O   1 
ATOM   961  C  CB  . GLN A 1 162 ? 130.088 126.074 111.952 1.00 14.91  ? 160 GLN A CB  1 
ATOM   962  C  CG  . GLN A 1 162 ? 129.313 125.231 110.959 1.00 18.16  ? 160 GLN A CG  1 
ATOM   963  C  CD  . GLN A 1 162 ? 128.159 125.982 110.338 1.00 28.88  ? 160 GLN A CD  1 
ATOM   964  O  OE1 . GLN A 1 162 ? 127.894 127.131 110.684 1.00 34.71  ? 160 GLN A OE1 1 
ATOM   965  N  NE2 . GLN A 1 162 ? 127.467 125.338 109.408 1.00 38.50  ? 160 GLN A NE2 1 
ATOM   966  N  N   . GLN A 1 163 ? 133.127 126.780 111.495 1.00 38.97  ? 161 GLN A N   1 
ATOM   967  C  CA  . GLN A 1 163 ? 134.245 127.709 111.469 1.00 24.47  ? 161 GLN A CA  1 
ATOM   968  C  C   . GLN A 1 163 ? 134.020 128.750 110.384 1.00 33.82  ? 161 GLN A C   1 
ATOM   969  O  O   . GLN A 1 163 ? 133.343 128.492 109.386 1.00 48.22  ? 161 GLN A O   1 
ATOM   970  C  CB  . GLN A 1 163 ? 135.567 126.983 111.215 1.00 30.73  ? 161 GLN A CB  1 
ATOM   971  C  CG  . GLN A 1 163 ? 136.659 127.326 112.202 1.00 38.73  ? 161 GLN A CG  1 
ATOM   972  C  CD  . GLN A 1 163 ? 137.891 126.473 112.017 1.00 45.80  ? 161 GLN A CD  1 
ATOM   973  O  OE1 . GLN A 1 163 ? 137.954 125.641 111.114 1.00 40.90  ? 161 GLN A OE1 1 
ATOM   974  N  NE2 . GLN A 1 163 ? 138.884 126.675 112.874 1.00 45.15  ? 161 GLN A NE2 1 
ATOM   975  N  N   . TYR A 1 164 ? 134.602 129.926 110.584 1.00 39.56  ? 162 TYR A N   1 
ATOM   976  C  CA  . TYR A 1 164 ? 134.427 131.056 109.684 1.00 35.92  ? 162 TYR A CA  1 
ATOM   977  C  C   . TYR A 1 164 ? 135.592 131.137 108.708 1.00 40.90  ? 162 TYR A C   1 
ATOM   978  O  O   . TYR A 1 164 ? 136.748 130.925 109.085 1.00 47.42  ? 162 TYR A O   1 
ATOM   979  C  CB  . TYR A 1 164 ? 134.318 132.360 110.474 1.00 38.47  ? 162 TYR A CB  1 
ATOM   980  C  CG  . TYR A 1 164 ? 133.793 133.528 109.675 1.00 39.12  ? 162 TYR A CG  1 
ATOM   981  C  CD1 . TYR A 1 164 ? 132.483 133.553 109.226 1.00 43.35  ? 162 TYR A CD1 1 
ATOM   982  C  CD2 . TYR A 1 164 ? 134.605 134.609 109.376 1.00 40.50  ? 162 TYR A CD2 1 
ATOM   983  C  CE1 . TYR A 1 164 ? 131.998 134.620 108.500 1.00 40.56  ? 162 TYR A CE1 1 
ATOM   984  C  CE2 . TYR A 1 164 ? 134.127 135.678 108.651 1.00 39.81  ? 162 TYR A CE2 1 
ATOM   985  C  CZ  . TYR A 1 164 ? 132.825 135.679 108.216 1.00 38.02  ? 162 TYR A CZ  1 
ATOM   986  O  OH  . TYR A 1 164 ? 132.352 136.747 107.493 1.00 39.33  ? 162 TYR A OH  1 
ATOM   987  N  N   . LYS A 1 165 ? 135.279 131.440 107.451 1.00 45.40  ? 163 LYS A N   1 
ATOM   988  C  CA  . LYS A 1 165 ? 136.285 131.611 106.414 1.00 47.83  ? 163 LYS A CA  1 
ATOM   989  C  C   . LYS A 1 165 ? 135.865 132.746 105.496 1.00 45.30  ? 163 LYS A C   1 
ATOM   990  O  O   . LYS A 1 165 ? 134.693 132.852 105.128 1.00 52.59  ? 163 LYS A O   1 
ATOM   991  C  CB  . LYS A 1 165 ? 136.478 130.328 105.597 1.00 46.15  ? 163 LYS A CB  1 
ATOM   992  C  CG  . LYS A 1 165 ? 137.538 129.391 106.154 1.00 50.50  ? 163 LYS A CG  1 
ATOM   993  C  CD  . LYS A 1 165 ? 137.057 127.945 106.179 1.00 53.70  ? 163 LYS A CD  1 
ATOM   994  C  CE  . LYS A 1 165 ? 137.788 127.118 107.229 1.00 54.42  ? 163 LYS A CE  1 
ATOM   995  N  NZ  . LYS A 1 165 ? 136.885 126.130 107.881 1.00 54.18  ? 163 LYS A NZ  1 
ATOM   996  N  N   . THR A 1 166 ? 136.824 133.590 105.130 1.00 46.84  ? 164 THR A N   1 
ATOM   997  C  CA  . THR A 1 166 ? 136.591 134.704 104.223 1.00 53.13  ? 164 THR A CA  1 
ATOM   998  C  C   . THR A 1 166 ? 137.445 134.532 102.976 1.00 51.72  ? 164 THR A C   1 
ATOM   999  O  O   . THR A 1 166 ? 138.571 134.030 103.046 1.00 51.01  ? 164 THR A O   1 
ATOM   1000 C  CB  . THR A 1 166 ? 136.912 136.049 104.885 1.00 50.63  ? 164 THR A CB  1 
ATOM   1001 O  OG1 . THR A 1 166 ? 138.327 136.272 104.869 1.00 50.53  ? 164 THR A OG1 1 
ATOM   1002 C  CG2 . THR A 1 166 ? 136.408 136.079 106.317 1.00 47.14  ? 164 THR A CG2 1 
ATOM   1003 N  N   . LYS A 1 167 ? 136.901 134.950 101.836 1.00 55.99  ? 165 LYS A N   1 
ATOM   1004 C  CA  . LYS A 1 167 ? 137.584 134.829 100.558 1.00 60.67  ? 165 LYS A CA  1 
ATOM   1005 C  C   . LYS A 1 167 ? 137.292 136.059 99.715  1.00 60.15  ? 165 LYS A C   1 
ATOM   1006 O  O   . LYS A 1 167 ? 136.156 136.538 99.676  1.00 61.92  ? 165 LYS A O   1 
ATOM   1007 C  CB  . LYS A 1 167 ? 137.147 133.563 99.811  1.00 61.21  ? 165 LYS A CB  1 
ATOM   1008 C  CG  . LYS A 1 167 ? 135.824 133.702 99.072  1.00 61.63  ? 165 LYS A CG  1 
ATOM   1009 C  CD  . LYS A 1 167 ? 135.146 132.357 98.841  1.00 65.97  ? 165 LYS A CD  1 
ATOM   1010 C  CE  . LYS A 1 167 ? 136.086 131.330 98.222  1.00 63.75  ? 165 LYS A CE  1 
ATOM   1011 N  NZ  . LYS A 1 167 ? 135.402 130.029 97.982  1.00 60.06  ? 165 LYS A NZ  1 
ATOM   1012 N  N   . ARG A 1 168 ? 138.323 136.570 99.047  1.00 64.17  ? 166 ARG A N   1 
ATOM   1013 C  CA  . ARG A 1 168 ? 138.138 137.686 98.130  1.00 66.15  ? 166 ARG A CA  1 
ATOM   1014 C  C   . ARG A 1 168 ? 137.421 137.210 96.874  1.00 67.09  ? 166 ARG A C   1 
ATOM   1015 O  O   . ARG A 1 168 ? 137.758 136.164 96.312  1.00 69.69  ? 166 ARG A O   1 
ATOM   1016 C  CB  . ARG A 1 168 ? 139.484 138.308 97.768  1.00 66.14  ? 166 ARG A CB  1 
ATOM   1017 C  CG  . ARG A 1 168 ? 140.109 139.108 98.892  1.00 67.29  ? 166 ARG A CG  1 
ATOM   1018 C  CD  . ARG A 1 168 ? 141.568 139.425 98.612  1.00 66.44  ? 166 ARG A CD  1 
ATOM   1019 N  NE  . ARG A 1 168 ? 142.206 140.094 99.739  1.00 67.24  ? 166 ARG A NE  1 
ATOM   1020 C  CZ  . ARG A 1 168 ? 143.465 140.511 99.748  1.00 66.46  ? 166 ARG A CZ  1 
ATOM   1021 N  NH1 . ARG A 1 168 ? 144.254 140.353 98.699  1.00 69.80  ? 166 ARG A NH1 1 
ATOM   1022 N  NH2 . ARG A 1 168 ? 143.944 141.102 100.839 1.00 62.82  ? 166 ARG A NH2 1 
ATOM   1023 N  N   . GLU A 1 169 ? 136.429 137.981 96.436  1.00 71.82  ? 167 GLU A N   1 
ATOM   1024 C  CA  . GLU A 1 169 ? 135.642 137.620 95.269  1.00 74.23  ? 167 GLU A CA  1 
ATOM   1025 C  C   . GLU A 1 169 ? 135.136 138.889 94.603  1.00 75.78  ? 167 GLU A C   1 
ATOM   1026 O  O   . GLU A 1 169 ? 135.098 139.961 95.211  1.00 77.47  ? 167 GLU A O   1 
ATOM   1027 C  CB  . GLU A 1 169 ? 134.475 136.699 95.649  1.00 73.00  ? 167 GLU A CB  1 
ATOM   1028 C  CG  . GLU A 1 169 ? 133.301 137.411 96.307  1.00 72.87  ? 167 GLU A CG  1 
ATOM   1029 C  CD  . GLU A 1 169 ? 132.257 137.879 95.311  1.00 73.20  ? 167 GLU A CD  1 
ATOM   1030 O  OE1 . GLU A 1 169 ? 132.486 137.742 94.092  1.00 72.18  ? 167 GLU A OE1 1 
ATOM   1031 O  OE2 . GLU A 1 169 ? 131.203 138.384 95.751  1.00 75.86  ? 167 GLU A OE2 1 
ATOM   1032 N  N   . GLU A 1 170 ? 134.748 138.754 93.339  1.00 75.90  ? 168 GLU A N   1 
ATOM   1033 C  CA  . GLU A 1 170 ? 134.260 139.888 92.565  1.00 77.05  ? 168 GLU A CA  1 
ATOM   1034 C  C   . GLU A 1 170 ? 133.322 139.423 91.457  1.00 75.80  ? 168 GLU A C   1 
ATOM   1035 O  O   . GLU A 1 170 ? 132.260 138.863 91.724  1.00 74.09  ? 168 GLU A O   1 
ATOM   1036 C  CB  . GLU A 1 170 ? 135.433 140.671 91.968  1.00 76.45  ? 168 GLU A CB  1 
ATOM   1037 C  CG  . GLU A 1 170 ? 135.029 141.920 91.198  1.00 78.84  ? 168 GLU A CG  1 
ATOM   1038 C  CD  . GLU A 1 170 ? 134.187 142.873 92.023  1.00 78.26  ? 168 GLU A CD  1 
ATOM   1039 O  OE1 . GLU A 1 170 ? 134.679 143.350 93.067  1.00 74.98  ? 168 GLU A OE1 1 
ATOM   1040 O  OE2 . GLU A 1 170 ? 133.033 143.144 91.628  1.00 76.32  ? 168 GLU A OE2 1 
ATOM   1041 N  N   . TYR A 1 202 ? 137.235 143.712 94.058  1.00 78.86  ? 200 TYR A N   1 
ATOM   1042 C  CA  . TYR A 1 202 ? 137.336 142.610 95.007  1.00 78.95  ? 200 TYR A CA  1 
ATOM   1043 C  C   . TYR A 1 202 ? 136.767 142.999 96.366  1.00 77.99  ? 200 TYR A C   1 
ATOM   1044 O  O   . TYR A 1 202 ? 137.204 143.973 96.978  1.00 80.20  ? 200 TYR A O   1 
ATOM   1045 C  CB  . TYR A 1 202 ? 138.797 142.171 95.163  1.00 76.91  ? 200 TYR A CB  1 
ATOM   1046 C  CG  . TYR A 1 202 ? 139.223 141.008 94.288  1.00 76.94  ? 200 TYR A CG  1 
ATOM   1047 C  CD1 . TYR A 1 202 ? 138.363 139.948 94.022  1.00 76.91  ? 200 TYR A CD1 1 
ATOM   1048 C  CD2 . TYR A 1 202 ? 140.495 140.970 93.734  1.00 78.37  ? 200 TYR A CD2 1 
ATOM   1049 C  CE1 . TYR A 1 202 ? 138.757 138.890 93.228  1.00 79.57  ? 200 TYR A CE1 1 
ATOM   1050 C  CE2 . TYR A 1 202 ? 140.897 139.914 92.938  1.00 81.90  ? 200 TYR A CE2 1 
ATOM   1051 C  CZ  . TYR A 1 202 ? 140.024 138.877 92.689  1.00 81.61  ? 200 TYR A CZ  1 
ATOM   1052 O  OH  . TYR A 1 202 ? 140.421 137.823 91.898  1.00 76.53  ? 200 TYR A OH  1 
ATOM   1053 N  N   . LYS A 1 203 ? 135.787 142.228 96.832  1.00 65.07  ? 201 LYS A N   1 
ATOM   1054 C  CA  . LYS A 1 203 ? 135.182 142.425 98.141  1.00 65.62  ? 201 LYS A CA  1 
ATOM   1055 C  C   . LYS A 1 203 ? 135.260 141.125 98.924  1.00 67.08  ? 201 LYS A C   1 
ATOM   1056 O  O   . LYS A 1 203 ? 135.119 140.039 98.356  1.00 70.68  ? 201 LYS A O   1 
ATOM   1057 C  CB  . LYS A 1 203 ? 133.722 142.890 98.021  1.00 69.15  ? 201 LYS A CB  1 
ATOM   1058 C  CG  . LYS A 1 203 ? 132.757 141.840 97.482  1.00 68.32  ? 201 LYS A CG  1 
ATOM   1059 C  CD  . LYS A 1 203 ? 131.313 142.243 97.726  1.00 68.42  ? 201 LYS A CD  1 
ATOM   1060 C  CE  . LYS A 1 203 ? 130.361 141.095 97.430  1.00 71.00  ? 201 LYS A CE  1 
ATOM   1061 N  NZ  . LYS A 1 203 ? 128.947 141.442 97.743  1.00 70.24  ? 201 LYS A NZ  1 
ATOM   1062 N  N   . ILE A 1 204 ? 135.485 141.240 100.228 1.00 59.64  ? 202 ILE A N   1 
ATOM   1063 C  CA  . ILE A 1 204 ? 135.602 140.070 101.089 1.00 57.49  ? 202 ILE A CA  1 
ATOM   1064 C  C   . ILE A 1 204 ? 134.205 139.558 101.413 1.00 57.69  ? 202 ILE A C   1 
ATOM   1065 O  O   . ILE A 1 204 ? 133.325 140.329 101.812 1.00 60.54  ? 202 ILE A O   1 
ATOM   1066 C  CB  . ILE A 1 204 ? 136.388 140.412 102.365 1.00 58.44  ? 202 ILE A CB  1 
ATOM   1067 C  CG1 . ILE A 1 204 ? 137.888 140.492 102.068 1.00 59.73  ? 202 ILE A CG1 1 
ATOM   1068 C  CG2 . ILE A 1 204 ? 136.146 139.379 103.455 1.00 59.74  ? 202 ILE A CG2 1 
ATOM   1069 C  CD1 . ILE A 1 204 ? 138.318 141.760 101.362 1.00 62.00  ? 202 ILE A CD1 1 
ATOM   1070 N  N   . VAL A 1 205 ? 133.997 138.255 101.237 1.00 58.50  ? 203 VAL A N   1 
ATOM   1071 C  CA  . VAL A 1 205 ? 132.732 137.604 101.556 1.00 60.13  ? 203 VAL A CA  1 
ATOM   1072 C  C   . VAL A 1 205 ? 133.021 136.395 102.434 1.00 62.05  ? 203 VAL A C   1 
ATOM   1073 O  O   . VAL A 1 205 ? 133.873 135.567 102.093 1.00 64.21  ? 203 VAL A O   1 
ATOM   1074 C  CB  . VAL A 1 205 ? 131.968 137.175 100.289 1.00 58.80  ? 203 VAL A CB  1 
ATOM   1075 C  CG1 . VAL A 1 205 ? 130.515 136.890 100.619 1.00 63.48  ? 203 VAL A CG1 1 
ATOM   1076 C  CG2 . VAL A 1 205 ? 132.068 138.244 99.214  1.00 60.15  ? 203 VAL A CG2 1 
ATOM   1077 N  N   . GLY A 1 206 ? 132.313 136.293 103.558 1.00 52.71  ? 204 GLY A N   1 
ATOM   1078 C  CA  . GLY A 1 206 ? 132.532 135.227 104.507 1.00 49.30  ? 204 GLY A CA  1 
ATOM   1079 C  C   . GLY A 1 206 ? 131.443 134.171 104.453 1.00 52.97  ? 204 GLY A C   1 
ATOM   1080 O  O   . GLY A 1 206 ? 130.331 134.418 103.995 1.00 59.19  ? 204 GLY A O   1 
ATOM   1081 N  N   . MET A 1 207 ? 131.784 132.976 104.933 1.00 47.72  ? 205 MET A N   1 
ATOM   1082 C  CA  . MET A 1 207 ? 130.831 131.875 104.996 1.00 45.52  ? 205 MET A CA  1 
ATOM   1083 C  C   . MET A 1 207 ? 131.280 130.907 106.079 1.00 34.61  ? 205 MET A C   1 
ATOM   1084 O  O   . MET A 1 207 ? 132.465 130.574 106.159 1.00 38.16  ? 205 MET A O   1 
ATOM   1085 C  CB  . MET A 1 207 ? 130.699 131.161 103.642 1.00 48.33  ? 205 MET A CB  1 
ATOM   1086 C  CG  . MET A 1 207 ? 131.983 131.038 102.829 1.00 53.91  ? 205 MET A CG  1 
ATOM   1087 S  SD  . MET A 1 207 ? 132.883 129.514 103.165 1.00 66.86  ? 205 MET A SD  1 
ATOM   1088 C  CE  . MET A 1 207 ? 131.830 128.321 102.340 1.00 48.48  ? 205 MET A CE  1 
ATOM   1089 N  N   . TYR A 1 208 ? 130.336 130.463 106.905 1.00 30.21  ? 206 TYR A N   1 
ATOM   1090 C  CA  . TYR A 1 208 ? 130.620 129.551 108.014 1.00 30.48  ? 206 TYR A CA  1 
ATOM   1091 C  C   . TYR A 1 208 ? 130.677 128.124 107.490 1.00 37.52  ? 206 TYR A C   1 
ATOM   1092 O  O   . TYR A 1 208 ? 129.669 127.420 107.420 1.00 40.82  ? 206 TYR A O   1 
ATOM   1093 C  CB  . TYR A 1 208 ? 129.568 129.680 109.108 1.00 32.40  ? 206 TYR A CB  1 
ATOM   1094 C  CG  . TYR A 1 208 ? 129.789 130.832 110.053 1.00 30.75  ? 206 TYR A CG  1 
ATOM   1095 C  CD1 . TYR A 1 208 ? 129.373 132.113 109.728 1.00 40.12  ? 206 TYR A CD1 1 
ATOM   1096 C  CD2 . TYR A 1 208 ? 130.421 130.640 111.271 1.00 29.10  ? 206 TYR A CD2 1 
ATOM   1097 C  CE1 . TYR A 1 208 ? 129.572 133.166 110.591 1.00 41.22  ? 206 TYR A CE1 1 
ATOM   1098 C  CE2 . TYR A 1 208 ? 130.627 131.687 112.140 1.00 32.01  ? 206 TYR A CE2 1 
ATOM   1099 C  CZ  . TYR A 1 208 ? 130.201 132.948 111.795 1.00 34.02  ? 206 TYR A CZ  1 
ATOM   1100 O  OH  . TYR A 1 208 ? 130.405 133.998 112.657 1.00 38.65  ? 206 TYR A OH  1 
ATOM   1101 N  N   . SER A 1 209 ? 131.876 127.687 107.118 1.00 39.58  ? 207 SER A N   1 
ATOM   1102 C  CA  . SER A 1 209 ? 132.080 126.312 106.699 1.00 33.73  ? 207 SER A CA  1 
ATOM   1103 C  C   . SER A 1 209 ? 132.092 125.401 107.924 1.00 31.12  ? 207 SER A C   1 
ATOM   1104 O  O   . SER A 1 209 ? 131.861 125.834 109.054 1.00 40.12  ? 207 SER A O   1 
ATOM   1105 C  CB  . SER A 1 209 ? 133.377 126.189 105.905 1.00 42.70  ? 207 SER A CB  1 
ATOM   1106 O  OG  . SER A 1 209 ? 134.500 126.191 106.768 1.00 41.87  ? 207 SER A OG  1 
ATOM   1107 N  N   . ASP A 1 210 ? 132.369 124.121 107.705 1.00 33.72  ? 208 ASP A N   1 
ATOM   1108 C  CA  . ASP A 1 210 ? 132.298 123.137 108.773 1.00 31.71  ? 208 ASP A CA  1 
ATOM   1109 C  C   . ASP A 1 210 ? 133.651 122.990 109.466 1.00 34.70  ? 208 ASP A C   1 
ATOM   1110 O  O   . ASP A 1 210 ? 134.689 123.436 108.973 1.00 37.39  ? 208 ASP A O   1 
ATOM   1111 C  CB  . ASP A 1 210 ? 131.834 121.788 108.221 1.00 34.00  ? 208 ASP A CB  1 
ATOM   1112 C  CG  . ASP A 1 210 ? 130.685 121.189 109.015 1.00 40.42  ? 208 ASP A CG  1 
ATOM   1113 O  OD1 . ASP A 1 210 ? 130.060 121.909 109.821 1.00 42.53  ? 208 ASP A OD1 1 
ATOM   1114 O  OD2 . ASP A 1 210 ? 130.405 119.986 108.830 1.00 44.74  ? 208 ASP A OD2 1 
ATOM   1115 N  N   . GLY A 1 211 ? 133.624 122.349 110.631 1.00 35.66  ? 209 GLY A N   1 
ATOM   1116 C  CA  . GLY A 1 211 ? 134.813 122.182 111.443 1.00 35.15  ? 209 GLY A CA  1 
ATOM   1117 C  C   . GLY A 1 211 ? 134.706 122.903 112.770 1.00 28.56  ? 209 GLY A C   1 
ATOM   1118 O  O   . GLY A 1 211 ? 134.498 124.118 112.803 1.00 34.36  ? 209 GLY A O   1 
ATOM   1119 N  N   . ILE A 1 212 ? 134.841 122.164 113.873 1.00 26.42  ? 210 ILE A N   1 
ATOM   1120 C  CA  . ILE A 1 212 ? 134.714 122.771 115.191 1.00 28.72  ? 210 ILE A CA  1 
ATOM   1121 C  C   . ILE A 1 212 ? 135.672 123.946 115.307 1.00 33.08  ? 210 ILE A C   1 
ATOM   1122 O  O   . ILE A 1 212 ? 136.810 123.898 114.829 1.00 37.50  ? 210 ILE A O   1 
ATOM   1123 C  CB  . ILE A 1 212 ? 134.968 121.729 116.296 1.00 19.96  ? 210 ILE A CB  1 
ATOM   1124 C  CG1 . ILE A 1 212 ? 134.831 122.379 117.674 1.00 19.24  ? 210 ILE A CG1 1 
ATOM   1125 C  CG2 . ILE A 1 212 ? 136.346 121.103 116.136 1.00 32.62  ? 210 ILE A CG2 1 
ATOM   1126 C  CD1 . ILE A 1 212 ? 134.843 121.402 118.824 1.00 33.26  ? 210 ILE A CD1 1 
ATOM   1127 N  N   . ASN A 1 213 ? 135.201 125.018 115.945 1.00 20.68  ? 211 ASN A N   1 
ATOM   1128 C  CA  . ASN A 1 213 ? 135.999 126.226 116.147 1.00 15.78  ? 211 ASN A CA  1 
ATOM   1129 C  C   . ASN A 1 213 ? 136.652 126.143 117.522 1.00 30.58  ? 211 ASN A C   1 
ATOM   1130 O  O   . ASN A 1 213 ? 136.194 126.726 118.505 1.00 38.33  ? 211 ASN A O   1 
ATOM   1131 C  CB  . ASN A 1 213 ? 135.131 127.469 116.007 1.00 19.01  ? 211 ASN A CB  1 
ATOM   1132 C  CG  . ASN A 1 213 ? 135.930 128.748 116.086 1.00 17.33  ? 211 ASN A CG  1 
ATOM   1133 O  OD1 . ASN A 1 213 ? 137.143 128.722 116.276 1.00 28.06  ? 211 ASN A OD1 1 
ATOM   1134 N  ND2 . ASN A 1 213 ? 135.253 129.878 115.936 1.00 19.50  ? 211 ASN A ND2 1 
ATOM   1135 N  N   . VAL A 1 214 ? 137.757 125.400 117.581 1.00 36.61  ? 212 VAL A N   1 
ATOM   1136 C  CA  . VAL A 1 214 ? 138.454 125.207 118.850 1.00 31.80  ? 212 VAL A CA  1 
ATOM   1137 C  C   . VAL A 1 214 ? 139.011 126.529 119.357 1.00 30.62  ? 212 VAL A C   1 
ATOM   1138 O  O   . VAL A 1 214 ? 139.017 126.795 120.565 1.00 33.78  ? 212 VAL A O   1 
ATOM   1139 C  CB  . VAL A 1 214 ? 139.559 124.146 118.693 1.00 34.08  ? 212 VAL A CB  1 
ATOM   1140 C  CG1 . VAL A 1 214 ? 140.237 123.884 120.019 1.00 37.57  ? 212 VAL A CG1 1 
ATOM   1141 C  CG2 . VAL A 1 214 ? 138.986 122.858 118.139 1.00 36.83  ? 212 VAL A CG2 1 
ATOM   1142 N  N   . LEU A 1 215 ? 139.494 127.375 118.448 1.00 30.00  ? 213 LEU A N   1 
ATOM   1143 C  CA  . LEU A 1 215 ? 140.075 128.650 118.856 1.00 25.96  ? 213 LEU A CA  1 
ATOM   1144 C  C   . LEU A 1 215 ? 139.026 129.558 119.483 1.00 26.26  ? 213 LEU A C   1 
ATOM   1145 O  O   . LEU A 1 215 ? 139.312 130.273 120.449 1.00 30.80  ? 213 LEU A O   1 
ATOM   1146 C  CB  . LEU A 1 215 ? 140.733 129.330 117.658 1.00 29.81  ? 213 LEU A CB  1 
ATOM   1147 C  CG  . LEU A 1 215 ? 141.435 130.661 117.932 1.00 39.33  ? 213 LEU A CG  1 
ATOM   1148 C  CD1 . LEU A 1 215 ? 142.471 130.535 119.039 1.00 39.59  ? 213 LEU A CD1 1 
ATOM   1149 C  CD2 . LEU A 1 215 ? 142.077 131.174 116.660 1.00 42.27  ? 213 LEU A CD2 1 
ATOM   1150 N  N   . GLY A 1 216 ? 137.809 129.552 118.940 1.00 25.96  ? 214 GLY A N   1 
ATOM   1151 C  CA  . GLY A 1 216 ? 136.764 130.408 119.480 1.00 21.76  ? 214 GLY A CA  1 
ATOM   1152 C  C   . GLY A 1 216 ? 136.298 129.956 120.850 1.00 16.51  ? 214 GLY A C   1 
ATOM   1153 O  O   . GLY A 1 216 ? 136.125 130.770 121.760 1.00 27.21  ? 214 GLY A O   1 
ATOM   1154 N  N   . LEU A 1 217 ? 136.072 128.651 121.012 1.00 23.78  ? 215 LEU A N   1 
ATOM   1155 C  CA  . LEU A 1 217 ? 135.550 128.141 122.275 1.00 23.30  ? 215 LEU A CA  1 
ATOM   1156 C  C   . LEU A 1 217 ? 136.511 128.412 123.425 1.00 26.79  ? 215 LEU A C   1 
ATOM   1157 O  O   . LEU A 1 217 ? 136.082 128.768 124.528 1.00 35.30  ? 215 LEU A O   1 
ATOM   1158 C  CB  . LEU A 1 217 ? 135.267 126.645 122.157 1.00 24.74  ? 215 LEU A CB  1 
ATOM   1159 C  CG  . LEU A 1 217 ? 134.285 126.225 121.064 1.00 19.74  ? 215 LEU A CG  1 
ATOM   1160 C  CD1 . LEU A 1 217 ? 134.253 124.715 120.942 1.00 25.87  ? 215 LEU A CD1 1 
ATOM   1161 C  CD2 . LEU A 1 217 ? 132.896 126.769 121.346 1.00 18.23  ? 215 LEU A CD2 1 
ATOM   1162 N  N   . ILE A 1 218 ? 137.814 128.245 123.195 1.00 30.44  ? 216 ILE A N   1 
ATOM   1163 C  CA  . ILE A 1 218 ? 138.787 128.470 124.261 1.00 27.16  ? 216 ILE A CA  1 
ATOM   1164 C  C   . ILE A 1 218 ? 138.794 129.935 124.674 1.00 28.68  ? 216 ILE A C   1 
ATOM   1165 O  O   . ILE A 1 218 ? 138.746 130.258 125.866 1.00 43.77  ? 216 ILE A O   1 
ATOM   1166 C  CB  . ILE A 1 218 ? 140.187 127.997 123.832 1.00 35.00  ? 216 ILE A CB  1 
ATOM   1167 C  CG1 . ILE A 1 218 ? 140.169 126.511 123.470 1.00 37.63  ? 216 ILE A CG1 1 
ATOM   1168 C  CG2 . ILE A 1 218 ? 141.204 128.257 124.932 1.00 34.10  ? 216 ILE A CG2 1 
ATOM   1169 C  CD1 . ILE A 1 218 ? 141.298 126.101 122.562 1.00 40.58  ? 216 ILE A CD1 1 
ATOM   1170 N  N   . VAL A 1 219 ? 138.871 130.845 123.702 1.00 24.85  ? 217 VAL A N   1 
ATOM   1171 C  CA  . VAL A 1 219 ? 138.851 132.270 124.024 1.00 24.01  ? 217 VAL A CA  1 
ATOM   1172 C  C   . VAL A 1 219 ? 137.623 132.615 124.851 1.00 26.17  ? 217 VAL A C   1 
ATOM   1173 O  O   . VAL A 1 219 ? 137.656 133.543 125.666 1.00 31.89  ? 217 VAL A O   1 
ATOM   1174 C  CB  . VAL A 1 219 ? 138.926 133.112 122.736 1.00 34.58  ? 217 VAL A CB  1 
ATOM   1175 C  CG1 . VAL A 1 219 ? 138.727 134.590 123.043 1.00 30.71  ? 217 VAL A CG1 1 
ATOM   1176 C  CG2 . VAL A 1 219 ? 140.260 132.892 122.050 1.00 34.62  ? 217 VAL A CG2 1 
ATOM   1177 N  N   . PHE A 1 220 ? 136.522 131.889 124.656 1.00 22.75  ? 218 PHE A N   1 
ATOM   1178 C  CA  . PHE A 1 220 ? 135.340 132.109 125.483 1.00 24.17  ? 218 PHE A CA  1 
ATOM   1179 C  C   . PHE A 1 220 ? 135.491 131.411 126.828 1.00 30.06  ? 218 PHE A C   1 
ATOM   1180 O  O   . PHE A 1 220 ? 135.267 132.019 127.880 1.00 33.14  ? 218 PHE A O   1 
ATOM   1181 C  CB  . PHE A 1 220 ? 134.085 131.618 124.764 1.00 23.57  ? 218 PHE A CB  1 
ATOM   1182 C  CG  . PHE A 1 220 ? 132.842 131.705 125.601 1.00 27.91  ? 218 PHE A CG  1 
ATOM   1183 C  CD1 . PHE A 1 220 ? 132.192 132.915 125.773 1.00 23.04  ? 218 PHE A CD1 1 
ATOM   1184 C  CD2 . PHE A 1 220 ? 132.330 130.581 126.225 1.00 29.55  ? 218 PHE A CD2 1 
ATOM   1185 C  CE1 . PHE A 1 220 ? 131.054 133.001 126.545 1.00 22.89  ? 218 PHE A CE1 1 
ATOM   1186 C  CE2 . PHE A 1 220 ? 131.190 130.662 126.998 1.00 31.46  ? 218 PHE A CE2 1 
ATOM   1187 C  CZ  . PHE A 1 220 ? 130.552 131.874 127.157 1.00 28.15  ? 218 PHE A CZ  1 
ATOM   1188 N  N   . ALA A 1 221 ? 135.861 130.129 126.810 1.00 31.17  ? 219 ALA A N   1 
ATOM   1189 C  CA  . ALA A 1 221 ? 135.987 129.375 128.051 1.00 19.29  ? 219 ALA A CA  1 
ATOM   1190 C  C   . ALA A 1 221 ? 136.986 130.037 128.989 1.00 26.83  ? 219 ALA A C   1 
ATOM   1191 O  O   . ALA A 1 221 ? 136.758 130.110 130.201 1.00 36.60  ? 219 ALA A O   1 
ATOM   1192 C  CB  . ALA A 1 221 ? 136.405 127.938 127.750 1.00 24.34  ? 219 ALA A CB  1 
ATOM   1193 N  N   . LEU A 1 222 ? 138.104 130.522 128.447 1.00 21.60  ? 220 LEU A N   1 
ATOM   1194 C  CA  . LEU A 1 222 ? 139.077 131.233 129.269 1.00 22.15  ? 220 LEU A CA  1 
ATOM   1195 C  C   . LEU A 1 222 ? 138.456 132.481 129.884 1.00 32.88  ? 220 LEU A C   1 
ATOM   1196 O  O   . LEU A 1 222 ? 138.605 132.735 131.084 1.00 42.77  ? 220 LEU A O   1 
ATOM   1197 C  CB  . LEU A 1 222 ? 140.297 131.598 128.423 1.00 30.77  ? 220 LEU A CB  1 
ATOM   1198 C  CG  . LEU A 1 222 ? 141.424 132.358 129.124 1.00 34.57  ? 220 LEU A CG  1 
ATOM   1199 C  CD1 . LEU A 1 222 ? 142.549 131.411 129.498 1.00 37.57  ? 220 LEU A CD1 1 
ATOM   1200 C  CD2 . LEU A 1 222 ? 141.936 133.489 128.247 1.00 31.12  ? 220 LEU A CD2 1 
ATOM   1201 N  N   . VAL A 1 223 ? 137.754 133.275 129.075 1.00 26.79  ? 221 VAL A N   1 
ATOM   1202 C  CA  . VAL A 1 223 ? 137.094 134.465 129.602 1.00 24.07  ? 221 VAL A CA  1 
ATOM   1203 C  C   . VAL A 1 223 ? 135.989 134.070 130.572 1.00 25.39  ? 221 VAL A C   1 
ATOM   1204 O  O   . VAL A 1 223 ? 135.843 134.668 131.643 1.00 33.15  ? 221 VAL A O   1 
ATOM   1205 C  CB  . VAL A 1 223 ? 136.563 135.334 128.446 1.00 19.28  ? 221 VAL A CB  1 
ATOM   1206 C  CG1 . VAL A 1 223 ? 135.683 136.460 128.967 1.00 15.61  ? 221 VAL A CG1 1 
ATOM   1207 C  CG2 . VAL A 1 223 ? 137.720 135.904 127.650 1.00 35.43  ? 221 VAL A CG2 1 
ATOM   1208 N  N   . PHE A 1 224 ? 135.198 133.056 130.218 1.00 26.51  ? 222 PHE A N   1 
ATOM   1209 C  CA  . PHE A 1 224 ? 134.149 132.591 131.119 1.00 19.01  ? 222 PHE A CA  1 
ATOM   1210 C  C   . PHE A 1 224 ? 134.740 132.059 132.418 1.00 24.47  ? 222 PHE A C   1 
ATOM   1211 O  O   . PHE A 1 224 ? 134.196 132.301 133.501 1.00 28.29  ? 222 PHE A O   1 
ATOM   1212 C  CB  . PHE A 1 224 ? 133.313 131.513 130.432 1.00 20.94  ? 222 PHE A CB  1 
ATOM   1213 C  CG  . PHE A 1 224 ? 132.041 131.179 131.153 1.00 19.87  ? 222 PHE A CG  1 
ATOM   1214 C  CD1 . PHE A 1 224 ? 131.034 132.117 131.283 1.00 24.53  ? 222 PHE A CD1 1 
ATOM   1215 C  CD2 . PHE A 1 224 ? 131.851 129.922 131.696 1.00 17.45  ? 222 PHE A CD2 1 
ATOM   1216 C  CE1 . PHE A 1 224 ? 129.864 131.808 131.944 1.00 24.53  ? 222 PHE A CE1 1 
ATOM   1217 C  CE2 . PHE A 1 224 ? 130.685 129.609 132.357 1.00 25.11  ? 222 PHE A CE2 1 
ATOM   1218 C  CZ  . PHE A 1 224 ? 129.690 130.553 132.481 1.00 26.91  ? 222 PHE A CZ  1 
ATOM   1219 N  N   . GLY A 1 225 ? 135.849 131.324 132.331 1.00 22.83  ? 223 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 225 ? 136.485 130.823 133.537 1.00 15.82  ? 223 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 225 ? 136.988 131.935 134.436 1.00 22.31  ? 223 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 225 ? 136.851 131.867 135.659 1.00 28.99  ? 223 GLY A O   1 
ATOM   1223 N  N   . LEU A 1 226 ? 137.581 132.974 133.845 1.00 25.64  ? 224 LEU A N   1 
ATOM   1224 C  CA  . LEU A 1 226 ? 138.076 134.089 134.645 1.00 20.97  ? 224 LEU A CA  1 
ATOM   1225 C  C   . LEU A 1 226 ? 136.938 134.788 135.374 1.00 25.77  ? 224 LEU A C   1 
ATOM   1226 O  O   . LEU A 1 226 ? 137.070 135.146 136.549 1.00 36.02  ? 224 LEU A O   1 
ATOM   1227 C  CB  . LEU A 1 226 ? 138.821 135.087 133.760 1.00 24.15  ? 224 LEU A CB  1 
ATOM   1228 C  CG  . LEU A 1 226 ? 140.230 134.708 133.306 1.00 29.91  ? 224 LEU A CG  1 
ATOM   1229 C  CD1 . LEU A 1 226 ? 140.717 135.670 132.236 1.00 29.72  ? 224 LEU A CD1 1 
ATOM   1230 C  CD2 . LEU A 1 226 ? 141.196 134.675 134.478 1.00 29.89  ? 224 LEU A CD2 1 
ATOM   1231 N  N   . VAL A 1 227 ? 135.810 134.991 134.693 1.00 31.46  ? 225 VAL A N   1 
ATOM   1232 C  CA  . VAL A 1 227 ? 134.704 135.736 135.286 1.00 20.01  ? 225 VAL A CA  1 
ATOM   1233 C  C   . VAL A 1 227 ? 134.129 134.978 136.476 1.00 28.69  ? 225 VAL A C   1 
ATOM   1234 O  O   . VAL A 1 227 ? 134.128 135.477 137.606 1.00 40.24  ? 225 VAL A O   1 
ATOM   1235 C  CB  . VAL A 1 227 ? 133.627 136.028 134.227 1.00 15.05  ? 225 VAL A CB  1 
ATOM   1236 C  CG1 . VAL A 1 227 ? 132.387 136.624 134.868 1.00 31.29  ? 225 VAL A CG1 1 
ATOM   1237 C  CG2 . VAL A 1 227 ? 134.175 136.965 133.169 1.00 24.55  ? 225 VAL A CG2 1 
ATOM   1238 N  N   . ILE A 1 228 ? 133.648 133.753 136.245 1.00 25.01  ? 226 ILE A N   1 
ATOM   1239 C  CA  . ILE A 1 228 ? 132.968 133.017 137.310 1.00 22.92  ? 226 ILE A CA  1 
ATOM   1240 C  C   . ILE A 1 228 ? 133.884 132.837 138.510 1.00 27.53  ? 226 ILE A C   1 
ATOM   1241 O  O   . ILE A 1 228 ? 133.415 132.754 139.651 1.00 35.07  ? 226 ILE A O   1 
ATOM   1242 C  CB  . ILE A 1 228 ? 132.446 131.661 136.791 1.00 15.68  ? 226 ILE A CB  1 
ATOM   1243 C  CG1 . ILE A 1 228 ? 133.608 130.726 136.440 1.00 25.03  ? 226 ILE A CG1 1 
ATOM   1244 C  CG2 . ILE A 1 228 ? 131.535 131.873 135.592 1.00 27.87  ? 226 ILE A CG2 1 
ATOM   1245 C  CD1 . ILE A 1 228 ? 133.181 129.322 136.065 1.00 20.16  ? 226 ILE A CD1 1 
ATOM   1246 N  N   . GLY A 1 229 ? 135.195 132.770 138.282 1.00 23.25  ? 227 GLY A N   1 
ATOM   1247 C  CA  . GLY A 1 229 ? 136.123 132.743 139.398 1.00 24.66  ? 227 GLY A CA  1 
ATOM   1248 C  C   . GLY A 1 229 ? 136.126 134.044 140.176 1.00 38.56  ? 227 GLY A C   1 
ATOM   1249 O  O   . GLY A 1 229 ? 136.269 134.045 141.401 1.00 50.73  ? 227 GLY A O   1 
ATOM   1250 N  N   . LYS A 1 230 ? 135.972 135.170 139.477 1.00 30.29  ? 228 LYS A N   1 
ATOM   1251 C  CA  . LYS A 1 230 ? 135.976 136.469 140.139 1.00 26.43  ? 228 LYS A CA  1 
ATOM   1252 C  C   . LYS A 1 230 ? 134.664 136.764 140.852 1.00 32.12  ? 228 LYS A C   1 
ATOM   1253 O  O   . LYS A 1 230 ? 134.664 137.489 141.853 1.00 37.05  ? 228 LYS A O   1 
ATOM   1254 C  CB  . LYS A 1 230 ? 136.268 137.574 139.123 1.00 34.38  ? 228 LYS A CB  1 
ATOM   1255 C  CG  . LYS A 1 230 ? 137.739 137.710 138.757 1.00 39.39  ? 228 LYS A CG  1 
ATOM   1256 C  CD  . LYS A 1 230 ? 137.937 138.219 137.332 1.00 41.53  ? 228 LYS A CD  1 
ATOM   1257 C  CE  . LYS A 1 230 ? 137.162 139.500 137.054 1.00 40.96  ? 228 LYS A CE  1 
ATOM   1258 N  NZ  . LYS A 1 230 ? 137.210 139.866 135.613 1.00 43.64  ? 228 LYS A NZ  1 
ATOM   1259 N  N   . MET A 1 231 ? 133.543 136.228 140.364 1.00 27.30  ? 229 MET A N   1 
ATOM   1260 C  CA  . MET A 1 231 ? 132.256 136.517 140.988 1.00 32.06  ? 229 MET A CA  1 
ATOM   1261 C  C   . MET A 1 231 ? 132.161 135.963 142.403 1.00 34.04  ? 229 MET A C   1 
ATOM   1262 O  O   . MET A 1 231 ? 131.343 136.449 143.189 1.00 39.47  ? 229 MET A O   1 
ATOM   1263 C  CB  . MET A 1 231 ? 131.105 135.969 140.140 1.00 26.40  ? 229 MET A CB  1 
ATOM   1264 C  CG  . MET A 1 231 ? 131.166 136.365 138.669 1.00 27.36  ? 229 MET A CG  1 
ATOM   1265 S  SD  . MET A 1 231 ? 130.021 135.503 137.567 1.00 35.93  ? 229 MET A SD  1 
ATOM   1266 C  CE  . MET A 1 231 ? 128.952 134.636 138.705 1.00 29.89  ? 229 MET A CE  1 
ATOM   1267 N  N   . GLY A 1 232 ? 132.973 134.968 142.747 1.00 30.76  ? 230 GLY A N   1 
ATOM   1268 C  CA  . GLY A 1 232 ? 133.017 134.474 144.108 1.00 35.29  ? 230 GLY A CA  1 
ATOM   1269 C  C   . GLY A 1 232 ? 131.870 133.550 144.457 1.00 41.44  ? 230 GLY A C   1 
ATOM   1270 O  O   . GLY A 1 232 ? 131.478 132.703 143.649 1.00 43.27  ? 230 GLY A O   1 
ATOM   1271 N  N   . GLU A 1 233 ? 131.322 133.703 145.665 1.00 35.55  ? 231 GLU A N   1 
ATOM   1272 C  CA  . GLU A 1 233 ? 130.256 132.814 146.112 1.00 34.33  ? 231 GLU A CA  1 
ATOM   1273 C  C   . GLU A 1 233 ? 129.047 132.870 145.188 1.00 41.76  ? 231 GLU A C   1 
ATOM   1274 O  O   . GLU A 1 233 ? 128.292 131.897 145.098 1.00 48.01  ? 231 GLU A O   1 
ATOM   1275 C  CB  . GLU A 1 233 ? 129.844 133.168 147.540 1.00 33.52  ? 231 GLU A CB  1 
ATOM   1276 C  CG  . GLU A 1 233 ? 130.882 132.805 148.590 1.00 41.45  ? 231 GLU A CG  1 
ATOM   1277 C  CD  . GLU A 1 233 ? 131.554 134.023 149.196 1.00 49.56  ? 231 GLU A CD  1 
ATOM   1278 O  OE1 . GLU A 1 233 ? 132.463 134.585 148.550 1.00 53.88  ? 231 GLU A OE1 1 
ATOM   1279 O  OE2 . GLU A 1 233 ? 131.175 134.415 150.320 1.00 43.45  ? 231 GLU A OE2 1 
ATOM   1280 N  N   . LYS A 1 234 ? 128.842 133.994 144.498 1.00 39.84  ? 232 LYS A N   1 
ATOM   1281 C  CA  . LYS A 1 234 ? 127.742 134.074 143.544 1.00 33.45  ? 232 LYS A CA  1 
ATOM   1282 C  C   . LYS A 1 234 ? 127.951 133.129 142.370 1.00 34.80  ? 232 LYS A C   1 
ATOM   1283 O  O   . LYS A 1 234 ? 126.976 132.678 141.759 1.00 33.01  ? 232 LYS A O   1 
ATOM   1284 C  CB  . LYS A 1 234 ? 127.582 135.508 143.040 1.00 34.98  ? 232 LYS A CB  1 
ATOM   1285 C  CG  . LYS A 1 234 ? 127.456 136.546 144.141 1.00 40.04  ? 232 LYS A CG  1 
ATOM   1286 C  CD  . LYS A 1 234 ? 127.280 137.947 143.577 1.00 43.34  ? 232 LYS A CD  1 
ATOM   1287 C  CE  . LYS A 1 234 ? 125.949 138.104 142.858 1.00 45.56  ? 232 LYS A CE  1 
ATOM   1288 N  NZ  . LYS A 1 234 ? 125.674 139.521 142.499 1.00 42.89  ? 232 LYS A NZ  1 
ATOM   1289 N  N   . GLY A 1 235 ? 129.204 132.825 142.037 1.00 36.53  ? 233 GLY A N   1 
ATOM   1290 C  CA  . GLY A 1 235 ? 129.524 131.935 140.940 1.00 26.71  ? 233 GLY A CA  1 
ATOM   1291 C  C   . GLY A 1 235 ? 130.062 130.583 141.341 1.00 21.60  ? 233 GLY A C   1 
ATOM   1292 O  O   . GLY A 1 235 ? 130.569 129.858 140.475 1.00 28.42  ? 233 GLY A O   1 
ATOM   1293 N  N   . GLN A 1 236 ? 129.981 130.207 142.617 1.00 25.34  ? 234 GLN A N   1 
ATOM   1294 C  CA  . GLN A 1 236 ? 130.497 128.913 143.040 1.00 28.01  ? 234 GLN A CA  1 
ATOM   1295 C  C   . GLN A 1 236 ? 129.700 127.757 142.455 1.00 27.80  ? 234 GLN A C   1 
ATOM   1296 O  O   . GLN A 1 236 ? 130.227 126.645 142.360 1.00 31.27  ? 234 GLN A O   1 
ATOM   1297 C  CB  . GLN A 1 236 ? 130.497 128.820 144.565 1.00 34.88  ? 234 GLN A CB  1 
ATOM   1298 C  CG  . GLN A 1 236 ? 131.328 127.674 145.117 1.00 33.25  ? 234 GLN A CG  1 
ATOM   1299 C  CD  . GLN A 1 236 ? 132.803 127.817 144.800 1.00 37.84  ? 234 GLN A CD  1 
ATOM   1300 O  OE1 . GLN A 1 236 ? 133.443 128.790 145.197 1.00 37.45  ? 234 GLN A OE1 1 
ATOM   1301 N  NE2 . GLN A 1 236 ? 133.350 126.847 144.080 1.00 34.73  ? 234 GLN A NE2 1 
ATOM   1302 N  N   . ILE A 1 237 ? 128.444 127.987 142.069 1.00 30.32  ? 235 ILE A N   1 
ATOM   1303 C  CA  . ILE A 1 237 ? 127.655 126.918 141.466 1.00 19.58  ? 235 ILE A CA  1 
ATOM   1304 C  C   . ILE A 1 237 ? 128.179 126.590 140.074 1.00 20.53  ? 235 ILE A C   1 
ATOM   1305 O  O   . ILE A 1 237 ? 128.235 125.421 139.679 1.00 43.23  ? 235 ILE A O   1 
ATOM   1306 C  CB  . ILE A 1 237 ? 126.163 127.296 141.438 1.00 14.40  ? 235 ILE A CB  1 
ATOM   1307 C  CG1 . ILE A 1 237 ? 125.350 126.157 140.825 1.00 23.75  ? 235 ILE A CG1 1 
ATOM   1308 C  CG2 . ILE A 1 237 ? 125.937 128.580 140.656 1.00 20.91  ? 235 ILE A CG2 1 
ATOM   1309 C  CD1 . ILE A 1 237 ? 123.877 126.225 141.135 1.00 33.63  ? 235 ILE A CD1 1 
ATOM   1310 N  N   . LEU A 1 238 ? 128.564 127.610 139.305 1.00 14.34  ? 236 LEU A N   1 
ATOM   1311 C  CA  . LEU A 1 238 ? 129.123 127.357 137.983 1.00 13.42  ? 236 LEU A CA  1 
ATOM   1312 C  C   . LEU A 1 238 ? 130.496 126.708 138.076 1.00 15.94  ? 236 LEU A C   1 
ATOM   1313 O  O   . LEU A 1 238 ? 130.856 125.898 137.216 1.00 24.41  ? 236 LEU A O   1 
ATOM   1314 C  CB  . LEU A 1 238 ? 129.206 128.659 137.188 1.00 27.19  ? 236 LEU A CB  1 
ATOM   1315 C  CG  . LEU A 1 238 ? 127.887 129.278 136.719 1.00 12.95  ? 236 LEU A CG  1 
ATOM   1316 C  CD1 . LEU A 1 238 ? 128.165 130.561 135.970 1.00 26.47  ? 236 LEU A CD1 1 
ATOM   1317 C  CD2 . LEU A 1 238 ? 127.096 128.321 135.845 1.00 14.36  ? 236 LEU A CD2 1 
ATOM   1318 N  N   . VAL A 1 239 ? 131.279 127.054 139.098 1.00 24.25  ? 237 VAL A N   1 
ATOM   1319 C  CA  . VAL A 1 239 ? 132.542 126.361 139.330 1.00 22.55  ? 237 VAL A CA  1 
ATOM   1320 C  C   . VAL A 1 239 ? 132.281 124.904 139.687 1.00 29.67  ? 237 VAL A C   1 
ATOM   1321 O  O   . VAL A 1 239 ? 132.951 123.995 139.183 1.00 38.21  ? 237 VAL A O   1 
ATOM   1322 C  CB  . VAL A 1 239 ? 133.350 127.081 140.426 1.00 20.35  ? 237 VAL A CB  1 
ATOM   1323 C  CG1 . VAL A 1 239 ? 134.592 126.286 140.802 1.00 26.78  ? 237 VAL A CG1 1 
ATOM   1324 C  CG2 . VAL A 1 239 ? 133.730 128.475 139.968 1.00 26.42  ? 237 VAL A CG2 1 
ATOM   1325 N  N   . ASP A 1 240 ? 131.306 124.659 140.564 1.00 22.39  ? 238 ASP A N   1 
ATOM   1326 C  CA  . ASP A 1 240 ? 130.963 123.289 140.929 1.00 13.10  ? 238 ASP A CA  1 
ATOM   1327 C  C   . ASP A 1 240 ? 130.406 122.521 139.739 1.00 22.27  ? 238 ASP A C   1 
ATOM   1328 O  O   . ASP A 1 240 ? 130.727 121.343 139.550 1.00 37.31  ? 238 ASP A O   1 
ATOM   1329 C  CB  . ASP A 1 240 ? 129.955 123.292 142.076 1.00 26.88  ? 238 ASP A CB  1 
ATOM   1330 C  CG  . ASP A 1 240 ? 130.563 123.750 143.384 1.00 40.73  ? 238 ASP A CG  1 
ATOM   1331 O  OD1 . ASP A 1 240 ? 131.795 123.942 143.435 1.00 38.89  ? 238 ASP A OD1 1 
ATOM   1332 O  OD2 . ASP A 1 240 ? 129.807 123.917 144.364 1.00 39.49  ? 238 ASP A OD2 1 
ATOM   1333 N  N   . PHE A 1 241 ? 129.562 123.164 138.932 1.00 21.50  ? 239 PHE A N   1 
ATOM   1334 C  CA  . PHE A 1 241 ? 128.963 122.478 137.792 1.00 13.50  ? 239 PHE A CA  1 
ATOM   1335 C  C   . PHE A 1 241 ? 130.026 122.045 136.792 1.00 16.65  ? 239 PHE A C   1 
ATOM   1336 O  O   . PHE A 1 241 ? 130.005 120.913 136.298 1.00 38.53  ? 239 PHE A O   1 
ATOM   1337 C  CB  . PHE A 1 241 ? 127.933 123.383 137.120 1.00 16.24  ? 239 PHE A CB  1 
ATOM   1338 C  CG  . PHE A 1 241 ? 127.330 122.793 135.880 1.00 18.10  ? 239 PHE A CG  1 
ATOM   1339 C  CD1 . PHE A 1 241 ? 126.286 121.892 135.965 1.00 27.84  ? 239 PHE A CD1 1 
ATOM   1340 C  CD2 . PHE A 1 241 ? 127.815 123.130 134.631 1.00 16.37  ? 239 PHE A CD2 1 
ATOM   1341 C  CE1 . PHE A 1 241 ? 125.734 121.345 134.828 1.00 25.60  ? 239 PHE A CE1 1 
ATOM   1342 C  CE2 . PHE A 1 241 ? 127.266 122.587 133.492 1.00 25.13  ? 239 PHE A CE2 1 
ATOM   1343 C  CZ  . PHE A 1 241 ? 126.225 121.694 133.590 1.00 26.23  ? 239 PHE A CZ  1 
ATOM   1344 N  N   . PHE A 1 242 ? 130.967 122.935 136.477 1.00 21.20  ? 240 PHE A N   1 
ATOM   1345 C  CA  . PHE A 1 242 ? 132.000 122.609 135.503 1.00 15.80  ? 240 PHE A CA  1 
ATOM   1346 C  C   . PHE A 1 242 ? 133.117 121.766 136.098 1.00 23.42  ? 240 PHE A C   1 
ATOM   1347 O  O   . PHE A 1 242 ? 133.803 121.062 135.351 1.00 39.07  ? 240 PHE A O   1 
ATOM   1348 C  CB  . PHE A 1 242 ? 132.572 123.890 134.897 1.00 16.00  ? 240 PHE A CB  1 
ATOM   1349 C  CG  . PHE A 1 242 ? 131.680 124.511 133.863 1.00 20.90  ? 240 PHE A CG  1 
ATOM   1350 C  CD1 . PHE A 1 242 ? 131.581 123.962 132.599 1.00 23.31  ? 240 PHE A CD1 1 
ATOM   1351 C  CD2 . PHE A 1 242 ? 130.919 125.627 134.163 1.00 22.32  ? 240 PHE A CD2 1 
ATOM   1352 C  CE1 . PHE A 1 242 ? 130.755 124.522 131.651 1.00 21.60  ? 240 PHE A CE1 1 
ATOM   1353 C  CE2 . PHE A 1 242 ? 130.090 126.189 133.218 1.00 21.26  ? 240 PHE A CE2 1 
ATOM   1354 C  CZ  . PHE A 1 242 ? 130.008 125.637 131.962 1.00 20.78  ? 240 PHE A CZ  1 
ATOM   1355 N  N   . ASN A 1 243 ? 133.320 121.818 137.415 1.00 25.31  ? 241 ASN A N   1 
ATOM   1356 C  CA  . ASN A 1 243 ? 134.230 120.871 138.050 1.00 20.10  ? 241 ASN A CA  1 
ATOM   1357 C  C   . ASN A 1 243 ? 133.724 119.445 137.886 1.00 35.59  ? 241 ASN A C   1 
ATOM   1358 O  O   . ASN A 1 243 ? 134.496 118.536 137.564 1.00 39.11  ? 241 ASN A O   1 
ATOM   1359 C  CB  . ASN A 1 243 ? 134.395 121.209 139.530 1.00 17.08  ? 241 ASN A CB  1 
ATOM   1360 C  CG  . ASN A 1 243 ? 135.420 122.294 139.770 1.00 31.81  ? 241 ASN A CG  1 
ATOM   1361 O  OD1 . ASN A 1 243 ? 136.103 122.736 138.848 1.00 36.44  ? 241 ASN A OD1 1 
ATOM   1362 N  ND2 . ASN A 1 243 ? 135.534 122.732 141.018 1.00 39.15  ? 241 ASN A ND2 1 
ATOM   1363 N  N   . ALA A 1 244 ? 132.425 119.231 138.105 1.00 30.34  ? 242 ALA A N   1 
ATOM   1364 C  CA  . ALA A 1 244 ? 131.853 117.903 137.925 1.00 11.45  ? 242 ALA A CA  1 
ATOM   1365 C  C   . ALA A 1 244 ? 131.788 117.528 136.452 1.00 15.43  ? 242 ALA A C   1 
ATOM   1366 O  O   . ALA A 1 244 ? 132.029 116.372 136.089 1.00 40.42  ? 242 ALA A O   1 
ATOM   1367 C  CB  . ALA A 1 244 ? 130.463 117.843 138.554 1.00 18.68  ? 242 ALA A CB  1 
ATOM   1368 N  N   . LEU A 1 245 ? 131.459 118.488 135.587 1.00 16.76  ? 243 LEU A N   1 
ATOM   1369 C  CA  . LEU A 1 245 ? 131.426 118.206 134.157 1.00 18.40  ? 243 LEU A CA  1 
ATOM   1370 C  C   . LEU A 1 245 ? 132.810 117.861 133.629 1.00 19.90  ? 243 LEU A C   1 
ATOM   1371 O  O   . LEU A 1 245 ? 132.933 117.132 132.639 1.00 14.46  ? 243 LEU A O   1 
ATOM   1372 C  CB  . LEU A 1 245 ? 130.855 119.403 133.400 1.00 19.48  ? 243 LEU A CB  1 
ATOM   1373 C  CG  . LEU A 1 245 ? 130.364 119.126 131.979 1.00 20.92  ? 243 LEU A CG  1 
ATOM   1374 C  CD1 . LEU A 1 245 ? 129.075 118.325 132.000 1.00 28.59  ? 243 LEU A CD1 1 
ATOM   1375 C  CD2 . LEU A 1 245 ? 130.177 120.425 131.218 1.00 24.51  ? 243 LEU A CD2 1 
ATOM   1376 N  N   . SER A 1 246 ? 133.862 118.381 134.265 1.00 35.74  ? 244 SER A N   1 
ATOM   1377 C  CA  . SER A 1 246 ? 135.218 118.023 133.865 1.00 26.80  ? 244 SER A CA  1 
ATOM   1378 C  C   . SER A 1 246 ? 135.576 116.620 134.334 1.00 28.41  ? 244 SER A C   1 
ATOM   1379 O  O   . SER A 1 246 ? 136.211 115.857 133.599 1.00 40.47  ? 244 SER A O   1 
ATOM   1380 C  CB  . SER A 1 246 ? 136.211 119.041 134.419 1.00 22.42  ? 244 SER A CB  1 
ATOM   1381 O  OG  . SER A 1 246 ? 137.530 118.735 134.008 1.00 42.30  ? 244 SER A OG  1 
ATOM   1382 N  N   . ASP A 1 247 ? 135.185 116.265 135.560 1.00 26.42  ? 245 ASP A N   1 
ATOM   1383 C  CA  . ASP A 1 247 ? 135.434 114.915 136.052 1.00 23.52  ? 245 ASP A CA  1 
ATOM   1384 C  C   . ASP A 1 247 ? 134.628 113.887 135.269 1.00 20.79  ? 245 ASP A C   1 
ATOM   1385 O  O   . ASP A 1 247 ? 135.125 112.795 134.975 1.00 34.14  ? 245 ASP A O   1 
ATOM   1386 C  CB  . ASP A 1 247 ? 135.104 114.832 137.540 1.00 28.29  ? 245 ASP A CB  1 
ATOM   1387 C  CG  . ASP A 1 247 ? 135.950 115.767 138.374 1.00 37.92  ? 245 ASP A CG  1 
ATOM   1388 O  OD1 . ASP A 1 247 ? 136.873 116.391 137.813 1.00 42.39  ? 245 ASP A OD1 1 
ATOM   1389 O  OD2 . ASP A 1 247 ? 135.690 115.882 139.589 1.00 37.28  ? 245 ASP A OD2 1 
ATOM   1390 N  N   . ALA A 1 248 ? 133.380 114.215 134.929 1.00 25.40  ? 246 ALA A N   1 
ATOM   1391 C  CA  . ALA A 1 248 ? 132.570 113.295 134.140 1.00 21.88  ? 246 ALA A CA  1 
ATOM   1392 C  C   . ALA A 1 248 ? 133.190 113.051 132.774 1.00 25.89  ? 246 ALA A C   1 
ATOM   1393 O  O   . ALA A 1 248 ? 133.063 111.953 132.222 1.00 34.67  ? 246 ALA A O   1 
ATOM   1394 C  CB  . ALA A 1 248 ? 131.151 113.840 133.990 1.00 15.16  ? 246 ALA A CB  1 
ATOM   1395 N  N   . THR A 1 249 ? 133.852 114.060 132.208 1.00 33.63  ? 247 THR A N   1 
ATOM   1396 C  CA  . THR A 1 249 ? 134.552 113.881 130.943 1.00 25.70  ? 247 THR A CA  1 
ATOM   1397 C  C   . THR A 1 249 ? 135.865 113.132 131.126 1.00 28.05  ? 247 THR A C   1 
ATOM   1398 O  O   . THR A 1 249 ? 136.313 112.445 130.203 1.00 37.49  ? 247 THR A O   1 
ATOM   1399 C  CB  . THR A 1 249 ? 134.808 115.236 130.287 1.00 31.52  ? 247 THR A CB  1 
ATOM   1400 O  OG1 . THR A 1 249 ? 133.593 115.995 130.266 1.00 37.26  ? 247 THR A OG1 1 
ATOM   1401 C  CG2 . THR A 1 249 ? 135.303 115.054 128.865 1.00 34.28  ? 247 THR A CG2 1 
ATOM   1402 N  N   . MET A 1 250 ? 136.498 113.255 132.295 1.00 31.21  ? 248 MET A N   1 
ATOM   1403 C  CA  . MET A 1 250 ? 137.674 112.441 132.582 1.00 28.45  ? 248 MET A CA  1 
ATOM   1404 C  C   . MET A 1 250 ? 137.328 110.961 132.555 1.00 38.85  ? 248 MET A C   1 
ATOM   1405 O  O   . MET A 1 250 ? 138.076 110.149 132.000 1.00 39.59  ? 248 MET A O   1 
ATOM   1406 C  CB  . MET A 1 250 ? 138.247 112.802 133.956 1.00 36.54  ? 248 MET A CB  1 
ATOM   1407 C  CG  . MET A 1 250 ? 139.245 113.957 134.031 1.00 42.42  ? 248 MET A CG  1 
ATOM   1408 S  SD  . MET A 1 250 ? 140.278 114.262 132.589 1.00 49.42  ? 248 MET A SD  1 
ATOM   1409 C  CE  . MET A 1 250 ? 139.432 115.667 131.888 1.00 38.41  ? 248 MET A CE  1 
ATOM   1410 N  N   . LYS A 1 251 ? 136.196 110.591 133.155 1.00 34.06  ? 249 LYS A N   1 
ATOM   1411 C  CA  . LYS A 1 251 ? 135.822 109.187 133.263 1.00 23.60  ? 249 LYS A CA  1 
ATOM   1412 C  C   . LYS A 1 251 ? 135.281 108.629 131.956 1.00 28.08  ? 249 LYS A C   1 
ATOM   1413 O  O   . LYS A 1 251 ? 135.426 107.431 131.696 1.00 39.45  ? 249 LYS A O   1 
ATOM   1414 C  CB  . LYS A 1 251 ? 134.792 109.010 134.377 1.00 30.33  ? 249 LYS A CB  1 
ATOM   1415 C  CG  . LYS A 1 251 ? 135.307 109.421 135.745 1.00 34.36  ? 249 LYS A CG  1 
ATOM   1416 C  CD  . LYS A 1 251 ? 134.473 108.828 136.863 1.00 39.60  ? 249 LYS A CD  1 
ATOM   1417 C  CE  . LYS A 1 251 ? 135.127 109.054 138.215 1.00 37.22  ? 249 LYS A CE  1 
ATOM   1418 N  NZ  . LYS A 1 251 ? 134.463 108.276 139.295 1.00 43.43  ? 249 LYS A NZ  1 
ATOM   1419 N  N   . ILE A 1 252 ? 134.648 109.463 131.129 1.00 29.14  ? 250 ILE A N   1 
ATOM   1420 C  CA  . ILE A 1 252 ? 134.212 108.993 129.819 1.00 25.91  ? 250 ILE A CA  1 
ATOM   1421 C  C   . ILE A 1 252 ? 135.413 108.691 128.935 1.00 30.68  ? 250 ILE A C   1 
ATOM   1422 O  O   . ILE A 1 252 ? 135.370 107.768 128.116 1.00 39.86  ? 250 ILE A O   1 
ATOM   1423 C  CB  . ILE A 1 252 ? 133.267 110.022 129.171 1.00 26.40  ? 250 ILE A CB  1 
ATOM   1424 C  CG1 . ILE A 1 252 ? 131.919 110.016 129.893 1.00 28.61  ? 250 ILE A CG1 1 
ATOM   1425 C  CG2 . ILE A 1 252 ? 133.070 109.720 127.688 1.00 33.09  ? 250 ILE A CG2 1 
ATOM   1426 C  CD1 . ILE A 1 252 ? 130.979 111.120 129.465 1.00 34.01  ? 250 ILE A CD1 1 
ATOM   1427 N  N   . VAL A 1 253 ? 136.494 109.462 129.069 1.00 34.35  ? 251 VAL A N   1 
ATOM   1428 C  CA  . VAL A 1 253 ? 137.694 109.186 128.286 1.00 32.64  ? 251 VAL A CA  1 
ATOM   1429 C  C   . VAL A 1 253 ? 138.339 107.881 128.736 1.00 31.36  ? 251 VAL A C   1 
ATOM   1430 O  O   . VAL A 1 253 ? 139.006 107.208 127.943 1.00 44.64  ? 251 VAL A O   1 
ATOM   1431 C  CB  . VAL A 1 253 ? 138.673 110.370 128.373 1.00 30.80  ? 251 VAL A CB  1 
ATOM   1432 C  CG1 . VAL A 1 253 ? 140.008 110.020 127.732 1.00 33.78  ? 251 VAL A CG1 1 
ATOM   1433 C  CG2 . VAL A 1 253 ? 138.077 111.591 127.701 1.00 33.62  ? 251 VAL A CG2 1 
ATOM   1434 N  N   . GLN A 1 254 ? 138.168 107.504 130.005 1.00 34.27  ? 252 GLN A N   1 
ATOM   1435 C  CA  . GLN A 1 254 ? 138.667 106.209 130.458 1.00 27.72  ? 252 GLN A CA  1 
ATOM   1436 C  C   . GLN A 1 254 ? 137.810 105.066 129.933 1.00 31.47  ? 252 GLN A C   1 
ATOM   1437 O  O   . GLN A 1 254 ? 138.305 103.944 129.779 1.00 50.39  ? 252 GLN A O   1 
ATOM   1438 C  CB  . GLN A 1 254 ? 138.728 106.166 131.984 1.00 36.02  ? 252 GLN A CB  1 
ATOM   1439 C  CG  . GLN A 1 254 ? 139.595 107.252 132.595 1.00 47.36  ? 252 GLN A CG  1 
ATOM   1440 C  CD  . GLN A 1 254 ? 139.881 107.015 134.063 1.00 47.74  ? 252 GLN A CD  1 
ATOM   1441 O  OE1 . GLN A 1 254 ? 138.967 106.794 134.857 1.00 46.24  ? 252 GLN A OE1 1 
ATOM   1442 N  NE2 . GLN A 1 254 ? 141.154 107.066 134.433 1.00 48.59  ? 252 GLN A NE2 1 
ATOM   1443 N  N   . ILE A 1 255 ? 136.528 105.316 129.671 1.00 30.19  ? 253 ILE A N   1 
ATOM   1444 C  CA  . ILE A 1 255 ? 135.705 104.311 129.007 1.00 29.05  ? 253 ILE A CA  1 
ATOM   1445 C  C   . ILE A 1 255 ? 136.215 104.079 127.592 1.00 38.47  ? 253 ILE A C   1 
ATOM   1446 O  O   . ILE A 1 255 ? 136.272 102.940 127.115 1.00 42.51  ? 253 ILE A O   1 
ATOM   1447 C  CB  . ILE A 1 255 ? 134.227 104.738 129.024 1.00 29.75  ? 253 ILE A CB  1 
ATOM   1448 C  CG1 . ILE A 1 255 ? 133.716 104.775 130.469 1.00 33.18  ? 253 ILE A CG1 1 
ATOM   1449 C  CG2 . ILE A 1 255 ? 133.383 103.796 128.170 1.00 37.36  ? 253 ILE A CG2 1 
ATOM   1450 C  CD1 . ILE A 1 255 ? 132.290 105.258 130.620 1.00 37.80  ? 253 ILE A CD1 1 
ATOM   1451 N  N   . ILE A 1 256 ? 136.594 105.155 126.902 1.00 36.38  ? 254 ILE A N   1 
ATOM   1452 C  CA  . ILE A 1 256 ? 137.162 105.036 125.565 1.00 23.72  ? 254 ILE A CA  1 
ATOM   1453 C  C   . ILE A 1 256 ? 138.497 104.307 125.615 1.00 33.14  ? 254 ILE A C   1 
ATOM   1454 O  O   . ILE A 1 256 ? 138.875 103.625 124.655 1.00 46.41  ? 254 ILE A O   1 
ATOM   1455 C  CB  . ILE A 1 256 ? 137.302 106.428 124.923 1.00 23.94  ? 254 ILE A CB  1 
ATOM   1456 C  CG1 . ILE A 1 256 ? 135.930 107.094 124.797 1.00 27.57  ? 254 ILE A CG1 1 
ATOM   1457 C  CG2 . ILE A 1 256 ? 137.967 106.322 123.557 1.00 29.51  ? 254 ILE A CG2 1 
ATOM   1458 C  CD1 . ILE A 1 256 ? 135.998 108.569 124.485 1.00 32.12  ? 254 ILE A CD1 1 
ATOM   1459 N  N   . MET A 1 257 ? 139.240 104.440 126.716 1.00 38.80  ? 255 MET A N   1 
ATOM   1460 C  CA  . MET A 1 257 ? 140.531 103.767 126.817 1.00 30.84  ? 255 MET A CA  1 
ATOM   1461 C  C   . MET A 1 257 ? 140.386 102.265 126.615 1.00 43.28  ? 255 MET A C   1 
ATOM   1462 O  O   . MET A 1 257 ? 141.292 101.620 126.076 1.00 51.78  ? 255 MET A O   1 
ATOM   1463 C  CB  . MET A 1 257 ? 141.146 103.991 128.201 1.00 42.53  ? 255 MET A CB  1 
ATOM   1464 C  CG  . MET A 1 257 ? 142.040 105.213 128.423 1.00 49.78  ? 255 MET A CG  1 
ATOM   1465 S  SD  . MET A 1 257 ? 143.154 105.774 127.128 1.00 64.00  ? 255 MET A SD  1 
ATOM   1466 C  CE  . MET A 1 257 ? 142.144 107.084 126.447 1.00 44.54  ? 255 MET A CE  1 
ATOM   1467 N  N   . TRP A 1 258 ? 139.262 101.691 127.056 1.00 38.08  ? 256 TRP A N   1 
ATOM   1468 C  CA  . TRP A 1 258 ? 139.066 100.246 126.958 1.00 34.34  ? 256 TRP A CA  1 
ATOM   1469 C  C   . TRP A 1 258 ? 138.881 99.788  125.516 1.00 36.61  ? 256 TRP A C   1 
ATOM   1470 O  O   . TRP A 1 258 ? 139.354 98.711  125.139 1.00 48.54  ? 256 TRP A O   1 
ATOM   1471 C  CB  . TRP A 1 258 ? 137.864 99.834  127.808 1.00 35.37  ? 256 TRP A CB  1 
ATOM   1472 C  CG  . TRP A 1 258 ? 138.002 100.196 129.261 1.00 40.93  ? 256 TRP A CG  1 
ATOM   1473 C  CD1 . TRP A 1 258 ? 139.162 100.297 129.968 1.00 44.89  ? 256 TRP A CD1 1 
ATOM   1474 C  CD2 . TRP A 1 258 ? 136.945 100.506 130.179 1.00 44.37  ? 256 TRP A CD2 1 
ATOM   1475 N  NE1 . TRP A 1 258 ? 138.897 100.648 131.268 1.00 39.96  ? 256 TRP A NE1 1 
ATOM   1476 C  CE2 . TRP A 1 258 ? 137.543 100.783 131.423 1.00 37.76  ? 256 TRP A CE2 1 
ATOM   1477 C  CE3 . TRP A 1 258 ? 135.553 100.576 130.070 1.00 46.00  ? 256 TRP A CE3 1 
ATOM   1478 C  CZ2 . TRP A 1 258 ? 136.799 101.124 132.550 1.00 42.02  ? 256 TRP A CZ2 1 
ATOM   1479 C  CZ3 . TRP A 1 258 ? 134.815 100.914 131.191 1.00 46.37  ? 256 TRP A CZ3 1 
ATOM   1480 C  CH2 . TRP A 1 258 ? 135.440 101.185 132.414 1.00 49.94  ? 256 TRP A CH2 1 
ATOM   1481 N  N   . TYR A 1 259 ? 138.201 100.587 124.696 1.00 29.66  ? 257 TYR A N   1 
ATOM   1482 C  CA  . TYR A 1 259 ? 138.047 100.269 123.282 1.00 32.02  ? 257 TYR A CA  1 
ATOM   1483 C  C   . TYR A 1 259 ? 139.270 100.632 122.454 1.00 37.56  ? 257 TYR A C   1 
ATOM   1484 O  O   . TYR A 1 259 ? 139.405 100.149 121.326 1.00 44.35  ? 257 TYR A O   1 
ATOM   1485 C  CB  . TYR A 1 259 ? 136.831 101.003 122.717 1.00 37.69  ? 257 TYR A CB  1 
ATOM   1486 C  CG  . TYR A 1 259 ? 136.633 100.814 121.232 1.00 36.57  ? 257 TYR A CG  1 
ATOM   1487 C  CD1 . TYR A 1 259 ? 136.176 99.614  120.713 1.00 39.32  ? 257 TYR A CD1 1 
ATOM   1488 C  CD2 . TYR A 1 259 ? 136.935 101.836 120.347 1.00 31.65  ? 257 TYR A CD2 1 
ATOM   1489 C  CE1 . TYR A 1 259 ? 136.007 99.447  119.355 1.00 37.95  ? 257 TYR A CE1 1 
ATOM   1490 C  CE2 . TYR A 1 259 ? 136.770 101.678 118.994 1.00 28.92  ? 257 TYR A CE2 1 
ATOM   1491 C  CZ  . TYR A 1 259 ? 136.307 100.484 118.501 1.00 36.18  ? 257 TYR A CZ  1 
ATOM   1492 O  OH  . TYR A 1 259 ? 136.145 100.331 117.145 1.00 48.58  ? 257 TYR A OH  1 
ATOM   1493 N  N   . MET A 1 260 ? 140.158 101.461 122.990 1.00 40.58  ? 258 MET A N   1 
ATOM   1494 C  CA  . MET A 1 260 ? 141.252 101.995 122.186 1.00 33.86  ? 258 MET A CA  1 
ATOM   1495 C  C   . MET A 1 260 ? 142.148 100.927 121.576 1.00 41.18  ? 258 MET A C   1 
ATOM   1496 O  O   . MET A 1 260 ? 142.532 101.085 120.405 1.00 51.79  ? 258 MET A O   1 
ATOM   1497 C  CB  . MET A 1 260 ? 142.070 102.958 123.047 1.00 37.22  ? 258 MET A CB  1 
ATOM   1498 C  CG  . MET A 1 260 ? 143.125 103.720 122.301 1.00 41.23  ? 258 MET A CG  1 
ATOM   1499 S  SD  . MET A 1 260 ? 142.495 105.370 121.996 1.00 59.25  ? 258 MET A SD  1 
ATOM   1500 C  CE  . MET A 1 260 ? 142.564 106.025 123.651 1.00 48.63  ? 258 MET A CE  1 
ATOM   1501 N  N   . PRO A 1 261 ? 142.531 99.858  122.277 1.00 42.06  ? 259 PRO A N   1 
ATOM   1502 C  CA  . PRO A 1 261 ? 143.372 98.841  121.626 1.00 42.54  ? 259 PRO A CA  1 
ATOM   1503 C  C   . PRO A 1 261 ? 142.762 98.302  120.346 1.00 44.33  ? 259 PRO A C   1 
ATOM   1504 O  O   . PRO A 1 261 ? 143.484 98.060  119.372 1.00 42.79  ? 259 PRO A O   1 
ATOM   1505 C  CB  . PRO A 1 261 ? 143.496 97.755  122.701 1.00 44.82  ? 259 PRO A CB  1 
ATOM   1506 C  CG  . PRO A 1 261 ? 143.284 98.466  123.983 1.00 44.59  ? 259 PRO A CG  1 
ATOM   1507 C  CD  . PRO A 1 261 ? 142.290 99.545  123.695 1.00 44.40  ? 259 PRO A CD  1 
ATOM   1508 N  N   . LEU A 1 262 ? 141.443 98.109  120.320 1.00 47.89  ? 260 LEU A N   1 
ATOM   1509 C  CA  . LEU A 1 262 ? 140.791 97.658  119.098 1.00 42.61  ? 260 LEU A CA  1 
ATOM   1510 C  C   . LEU A 1 262 ? 140.858 98.725  118.014 1.00 40.61  ? 260 LEU A C   1 
ATOM   1511 O  O   . LEU A 1 262 ? 141.087 98.412  116.842 1.00 43.44  ? 260 LEU A O   1 
ATOM   1512 C  CB  . LEU A 1 262 ? 139.339 97.281  119.389 1.00 36.92  ? 260 LEU A CB  1 
ATOM   1513 C  CG  . LEU A 1 262 ? 139.028 95.787  119.486 1.00 39.81  ? 260 LEU A CG  1 
ATOM   1514 C  CD1 . LEU A 1 262 ? 139.158 95.135  118.121 1.00 45.70  ? 260 LEU A CD1 1 
ATOM   1515 C  CD2 . LEU A 1 262 ? 139.931 95.105  120.503 1.00 43.55  ? 260 LEU A CD2 1 
ATOM   1516 N  N   . GLY A 1 263 ? 140.655 99.990  118.383 1.00 28.69  ? 261 GLY A N   1 
ATOM   1517 C  CA  . GLY A 1 263 ? 140.724 101.053 117.396 1.00 20.44  ? 261 GLY A CA  1 
ATOM   1518 C  C   . GLY A 1 263 ? 142.120 101.252 116.835 1.00 36.88  ? 261 GLY A C   1 
ATOM   1519 O  O   . GLY A 1 263 ? 142.290 101.454 115.631 1.00 49.10  ? 261 GLY A O   1 
ATOM   1520 N  N   . ILE A 1 264 ? 143.137 101.200 117.698 1.00 46.56  ? 262 ILE A N   1 
ATOM   1521 C  CA  . ILE A 1 264 ? 144.510 101.407 117.244 1.00 39.95  ? 262 ILE A CA  1 
ATOM   1522 C  C   . ILE A 1 264 ? 144.950 100.265 116.339 1.00 37.85  ? 262 ILE A C   1 
ATOM   1523 O  O   . ILE A 1 264 ? 145.685 100.473 115.368 1.00 42.59  ? 262 ILE A O   1 
ATOM   1524 C  CB  . ILE A 1 264 ? 145.450 101.572 118.452 1.00 39.89  ? 262 ILE A CB  1 
ATOM   1525 C  CG1 . ILE A 1 264 ? 145.055 102.800 119.277 1.00 36.72  ? 262 ILE A CG1 1 
ATOM   1526 C  CG2 . ILE A 1 264 ? 146.905 101.669 118.004 1.00 48.06  ? 262 ILE A CG2 1 
ATOM   1527 C  CD1 . ILE A 1 264 ? 145.155 104.121 118.540 1.00 43.41  ? 262 ILE A CD1 1 
ATOM   1528 N  N   . LEU A 1 265 ? 144.515 99.042  116.646 1.00 40.19  ? 263 LEU A N   1 
ATOM   1529 C  CA  . LEU A 1 265 ? 144.883 97.899  115.820 1.00 39.96  ? 263 LEU A CA  1 
ATOM   1530 C  C   . LEU A 1 265 ? 144.494 98.114  114.366 1.00 42.18  ? 263 LEU A C   1 
ATOM   1531 O  O   . LEU A 1 265 ? 145.189 97.638  113.462 1.00 52.26  ? 263 LEU A O   1 
ATOM   1532 C  CB  . LEU A 1 265 ? 144.218 96.635  116.367 1.00 41.87  ? 263 LEU A CB  1 
ATOM   1533 C  CG  . LEU A 1 265 ? 144.838 95.291  115.985 1.00 39.48  ? 263 LEU A CG  1 
ATOM   1534 C  CD1 . LEU A 1 265 ? 144.529 94.263  117.057 1.00 46.31  ? 263 LEU A CD1 1 
ATOM   1535 C  CD2 . LEU A 1 265 ? 144.344 94.808  114.633 1.00 40.97  ? 263 LEU A CD2 1 
ATOM   1536 N  N   . PHE A 1 266 ? 143.404 98.838  114.118 1.00 40.52  ? 264 PHE A N   1 
ATOM   1537 C  CA  . PHE A 1 266 ? 142.920 99.063  112.764 1.00 34.50  ? 264 PHE A CA  1 
ATOM   1538 C  C   . PHE A 1 266 ? 143.293 100.431 112.215 1.00 42.71  ? 264 PHE A C   1 
ATOM   1539 O  O   . PHE A 1 266 ? 143.421 100.579 110.996 1.00 51.52  ? 264 PHE A O   1 
ATOM   1540 C  CB  . PHE A 1 266 ? 141.400 98.889  112.719 1.00 33.03  ? 264 PHE A CB  1 
ATOM   1541 C  CG  . PHE A 1 266 ? 140.957 97.468  112.910 1.00 45.69  ? 264 PHE A CG  1 
ATOM   1542 C  CD1 . PHE A 1 266 ? 140.937 96.586  111.845 1.00 44.76  ? 264 PHE A CD1 1 
ATOM   1543 C  CD2 . PHE A 1 266 ? 140.587 97.006  114.160 1.00 43.94  ? 264 PHE A CD2 1 
ATOM   1544 C  CE1 . PHE A 1 266 ? 140.541 95.276  112.020 1.00 40.50  ? 264 PHE A CE1 1 
ATOM   1545 C  CE2 . PHE A 1 266 ? 140.192 95.698  114.341 1.00 35.89  ? 264 PHE A CE2 1 
ATOM   1546 C  CZ  . PHE A 1 266 ? 140.170 94.832  113.269 1.00 39.17  ? 264 PHE A CZ  1 
ATOM   1547 N  N   . LEU A 1 267 ? 143.474 101.433 113.075 1.00 47.55  ? 265 LEU A N   1 
ATOM   1548 C  CA  . LEU A 1 267 ? 144.016 102.705 112.611 1.00 41.65  ? 265 LEU A CA  1 
ATOM   1549 C  C   . LEU A 1 267 ? 145.424 102.519 112.064 1.00 46.98  ? 265 LEU A C   1 
ATOM   1550 O  O   . LEU A 1 267 ? 145.766 103.043 110.999 1.00 50.93  ? 265 LEU A O   1 
ATOM   1551 C  CB  . LEU A 1 267 ? 144.019 103.725 113.750 1.00 40.66  ? 265 LEU A CB  1 
ATOM   1552 C  CG  . LEU A 1 267 ? 142.725 104.483 114.038 1.00 36.60  ? 265 LEU A CG  1 
ATOM   1553 C  CD1 . LEU A 1 267 ? 142.911 105.391 115.240 1.00 38.54  ? 265 LEU A CD1 1 
ATOM   1554 C  CD2 . LEU A 1 267 ? 142.275 105.286 112.831 1.00 44.64  ? 265 LEU A CD2 1 
ATOM   1555 N  N   . ILE A 1 268 ? 146.260 101.775 112.790 1.00 49.30  ? 266 ILE A N   1 
ATOM   1556 C  CA  . ILE A 1 268 ? 147.616 101.509 112.324 1.00 47.71  ? 266 ILE A CA  1 
ATOM   1557 C  C   . ILE A 1 268 ? 147.592 100.556 111.138 1.00 52.10  ? 266 ILE A C   1 
ATOM   1558 O  O   . ILE A 1 268 ? 148.291 100.767 110.141 1.00 54.31  ? 266 ILE A O   1 
ATOM   1559 C  CB  . ILE A 1 268 ? 148.471 100.965 113.482 1.00 48.84  ? 266 ILE A CB  1 
ATOM   1560 C  CG1 . ILE A 1 268 ? 148.651 102.059 114.538 1.00 49.24  ? 266 ILE A CG1 1 
ATOM   1561 C  CG2 . ILE A 1 268 ? 149.821 100.469 112.971 1.00 50.97  ? 266 ILE A CG2 1 
ATOM   1562 C  CD1 . ILE A 1 268 ? 149.449 101.641 115.749 1.00 53.06  ? 266 ILE A CD1 1 
ATOM   1563 N  N   . ALA A 1 269 ? 146.793 99.490  111.224 1.00 52.41  ? 267 ALA A N   1 
ATOM   1564 C  CA  . ALA A 1 269 ? 146.721 98.536  110.123 1.00 50.14  ? 267 ALA A CA  1 
ATOM   1565 C  C   . ALA A 1 269 ? 146.144 99.185  108.874 1.00 54.63  ? 267 ALA A C   1 
ATOM   1566 O  O   . ALA A 1 269 ? 146.654 98.983  107.767 1.00 58.91  ? 267 ALA A O   1 
ATOM   1567 C  CB  . ALA A 1 269 ? 145.886 97.325  110.532 1.00 49.43  ? 267 ALA A CB  1 
ATOM   1568 N  N   . GLY A 1 270 ? 145.079 99.972  109.030 1.00 59.26  ? 268 GLY A N   1 
ATOM   1569 C  CA  . GLY A 1 270 ? 144.495 100.641 107.882 1.00 58.83  ? 268 GLY A CA  1 
ATOM   1570 C  C   . GLY A 1 270 ? 145.446 101.634 107.247 1.00 62.40  ? 268 GLY A C   1 
ATOM   1571 O  O   . GLY A 1 270 ? 145.423 101.834 106.030 1.00 60.39  ? 268 GLY A O   1 
ATOM   1572 N  N   . CYS A 1 271 ? 146.288 102.273 108.061 1.00 66.78  ? 269 CYS A N   1 
ATOM   1573 C  CA  . CYS A 1 271 ? 147.224 103.262 107.539 1.00 60.25  ? 269 CYS A CA  1 
ATOM   1574 C  C   . CYS A 1 271 ? 148.225 102.638 106.577 1.00 63.75  ? 269 CYS A C   1 
ATOM   1575 O  O   . CYS A 1 271 ? 148.500 103.198 105.509 1.00 64.89  ? 269 CYS A O   1 
ATOM   1576 C  CB  . CYS A 1 271 ? 147.960 103.933 108.694 1.00 60.73  ? 269 CYS A CB  1 
ATOM   1577 S  SG  . CYS A 1 271 ? 149.566 104.598 108.228 1.00 69.67  ? 269 CYS A SG  1 
ATOM   1578 N  N   . ILE A 1 272 ? 148.778 101.478 106.929 1.00 61.18  ? 270 ILE A N   1 
ATOM   1579 C  CA  . ILE A 1 272 ? 149.856 100.887 106.143 1.00 63.07  ? 270 ILE A CA  1 
ATOM   1580 C  C   . ILE A 1 272 ? 149.279 100.003 105.045 1.00 61.73  ? 270 ILE A C   1 
ATOM   1581 O  O   . ILE A 1 272 ? 150.019 99.292  104.355 1.00 57.38  ? 270 ILE A O   1 
ATOM   1582 C  CB  . ILE A 1 272 ? 150.842 100.112 107.041 1.00 62.17  ? 270 ILE A CB  1 
ATOM   1583 C  CG1 . ILE A 1 272 ? 150.279 98.742  107.439 1.00 60.95  ? 270 ILE A CG1 1 
ATOM   1584 C  CG2 . ILE A 1 272 ? 151.192 100.944 108.274 1.00 64.08  ? 270 ILE A CG2 1 
ATOM   1585 C  CD1 . ILE A 1 272 ? 151.221 97.928  108.308 1.00 62.50  ? 270 ILE A CD1 1 
ATOM   1586 N  N   . ILE A 1 273 ? 147.958 100.041 104.874 1.00 65.51  ? 271 ILE A N   1 
ATOM   1587 C  CA  . ILE A 1 273 ? 147.306 99.312  103.793 1.00 69.23  ? 271 ILE A CA  1 
ATOM   1588 C  C   . ILE A 1 273 ? 146.926 100.241 102.644 1.00 66.18  ? 271 ILE A C   1 
ATOM   1589 O  O   . ILE A 1 273 ? 146.812 99.775  101.500 1.00 65.35  ? 271 ILE A O   1 
ATOM   1590 C  CB  . ILE A 1 273 ? 146.065 98.552  104.311 1.00 63.90  ? 271 ILE A CB  1 
ATOM   1591 C  CG1 . ILE A 1 273 ? 146.503 97.322  105.108 1.00 59.14  ? 271 ILE A CG1 1 
ATOM   1592 C  CG2 . ILE A 1 273 ? 145.149 98.129  103.162 1.00 62.60  ? 271 ILE A CG2 1 
ATOM   1593 C  CD1 . ILE A 1 273 ? 145.386 96.651  105.875 1.00 60.27  ? 271 ILE A CD1 1 
ATOM   1594 N  N   . GLU A 1 274 ? 146.734 101.530 102.909 1.00 66.40  ? 272 GLU A N   1 
ATOM   1595 C  CA  . GLU A 1 274 ? 146.356 102.497 101.888 1.00 68.46  ? 272 GLU A CA  1 
ATOM   1596 C  C   . GLU A 1 274 ? 147.560 103.100 101.176 1.00 72.65  ? 272 GLU A C   1 
ATOM   1597 O  O   . GLU A 1 274 ? 147.379 103.901 100.253 1.00 72.84  ? 272 GLU A O   1 
ATOM   1598 C  CB  . GLU A 1 274 ? 145.506 103.610 102.516 1.00 68.03  ? 272 GLU A CB  1 
ATOM   1599 C  CG  . GLU A 1 274 ? 146.273 104.875 102.881 1.00 75.32  ? 272 GLU A CG  1 
ATOM   1600 C  CD  . GLU A 1 274 ? 145.416 105.880 103.626 1.00 75.84  ? 272 GLU A CD  1 
ATOM   1601 O  OE1 . GLU A 1 274 ? 144.376 105.477 104.188 1.00 69.60  ? 272 GLU A OE1 1 
ATOM   1602 O  OE2 . GLU A 1 274 ? 145.783 107.074 103.651 1.00 73.42  ? 272 GLU A OE2 1 
ATOM   1603 N  N   . VAL A 1 275 ? 148.779 102.733 101.577 1.00 77.82  ? 273 VAL A N   1 
ATOM   1604 C  CA  . VAL A 1 275 ? 149.972 103.291 100.947 1.00 80.06  ? 273 VAL A CA  1 
ATOM   1605 C  C   . VAL A 1 275 ? 150.023 102.917 99.471  1.00 80.38  ? 273 VAL A C   1 
ATOM   1606 O  O   . VAL A 1 275 ? 150.483 103.703 98.634  1.00 80.89  ? 273 VAL A O   1 
ATOM   1607 C  CB  . VAL A 1 275 ? 151.241 102.830 101.690 1.00 80.10  ? 273 VAL A CB  1 
ATOM   1608 C  CG1 . VAL A 1 275 ? 151.225 103.324 103.128 1.00 79.50  ? 273 VAL A CG1 1 
ATOM   1609 C  CG2 . VAL A 1 275 ? 151.378 101.313 101.641 1.00 78.79  ? 273 VAL A CG2 1 
ATOM   1610 N  N   . GLU A 1 276 ? 149.567 101.711 99.131  1.00 79.64  ? 274 GLU A N   1 
ATOM   1611 C  CA  . GLU A 1 276 ? 149.659 101.209 97.765  1.00 80.88  ? 274 GLU A CA  1 
ATOM   1612 C  C   . GLU A 1 276 ? 151.129 101.019 97.409  1.00 79.33  ? 274 GLU A C   1 
ATOM   1613 O  O   . GLU A 1 276 ? 151.832 100.264 98.088  1.00 80.34  ? 274 GLU A O   1 
ATOM   1614 C  CB  . GLU A 1 276 ? 148.957 102.151 96.780  1.00 80.31  ? 274 GLU A CB  1 
ATOM   1615 C  CG  . GLU A 1 276 ? 147.497 102.410 97.111  1.00 80.13  ? 274 GLU A CG  1 
ATOM   1616 C  CD  . GLU A 1 276 ? 146.860 103.430 96.189  1.00 80.51  ? 274 GLU A CD  1 
ATOM   1617 O  OE1 . GLU A 1 276 ? 146.828 103.187 94.964  1.00 78.71  ? 274 GLU A OE1 1 
ATOM   1618 O  OE2 . GLU A 1 276 ? 146.390 104.473 96.690  1.00 81.08  ? 274 GLU A OE2 1 
ATOM   1619 N  N   . ASP A 1 277 ? 151.610 101.681 96.359  1.00 84.00  ? 275 ASP A N   1 
ATOM   1620 C  CA  . ASP A 1 277 ? 153.007 101.532 95.978  1.00 86.81  ? 275 ASP A CA  1 
ATOM   1621 C  C   . ASP A 1 277 ? 153.900 101.952 97.138  1.00 88.77  ? 275 ASP A C   1 
ATOM   1622 O  O   . ASP A 1 277 ? 153.802 103.079 97.634  1.00 86.99  ? 275 ASP A O   1 
ATOM   1623 C  CB  . ASP A 1 277 ? 153.308 102.369 94.736  1.00 86.03  ? 275 ASP A CB  1 
ATOM   1624 C  CG  . ASP A 1 277 ? 154.779 102.353 94.366  1.00 88.37  ? 275 ASP A CG  1 
ATOM   1625 O  OD1 . ASP A 1 277 ? 155.323 101.252 94.139  1.00 85.01  ? 275 ASP A OD1 1 
ATOM   1626 O  OD2 . ASP A 1 277 ? 155.390 103.440 94.300  1.00 89.39  ? 275 ASP A OD2 1 
ATOM   1627 N  N   . TRP A 1 278 ? 154.774 101.040 97.567  1.00 89.30  ? 276 TRP A N   1 
ATOM   1628 C  CA  . TRP A 1 278 ? 155.635 101.286 98.716  1.00 89.14  ? 276 TRP A CA  1 
ATOM   1629 C  C   . TRP A 1 278 ? 156.774 102.247 98.406  1.00 87.84  ? 276 TRP A C   1 
ATOM   1630 O  O   . TRP A 1 278 ? 157.442 102.708 99.337  1.00 86.45  ? 276 TRP A O   1 
ATOM   1631 C  CB  . TRP A 1 278 ? 156.202 99.960  99.226  1.00 89.34  ? 276 TRP A CB  1 
ATOM   1632 C  CG  . TRP A 1 278 ? 156.993 100.087 100.490 1.00 90.06  ? 276 TRP A CG  1 
ATOM   1633 C  CD1 . TRP A 1 278 ? 158.351 100.063 100.616 1.00 89.30  ? 276 TRP A CD1 1 
ATOM   1634 C  CD2 . TRP A 1 278 ? 156.470 100.253 101.813 1.00 91.88  ? 276 TRP A CD2 1 
ATOM   1635 N  NE1 . TRP A 1 278 ? 158.706 100.207 101.936 1.00 93.80  ? 276 TRP A NE1 1 
ATOM   1636 C  CE2 . TRP A 1 278 ? 157.569 100.326 102.691 1.00 96.50  ? 276 TRP A CE2 1 
ATOM   1637 C  CE3 . TRP A 1 278 ? 155.178 100.350 102.340 1.00 86.92  ? 276 TRP A CE3 1 
ATOM   1638 C  CZ2 . TRP A 1 278 ? 157.416 100.490 104.067 1.00 93.70  ? 276 TRP A CZ2 1 
ATOM   1639 C  CZ3 . TRP A 1 278 ? 155.028 100.513 103.705 1.00 89.15  ? 276 TRP A CZ3 1 
ATOM   1640 C  CH2 . TRP A 1 278 ? 156.141 100.581 104.552 1.00 90.17  ? 276 TRP A CH2 1 
ATOM   1641 N  N   . GLU A 1 279 ? 157.009 102.561 97.132  1.00 89.26  ? 277 GLU A N   1 
ATOM   1642 C  CA  . GLU A 1 279 ? 158.098 103.454 96.758  1.00 89.85  ? 277 GLU A CA  1 
ATOM   1643 C  C   . GLU A 1 279 ? 157.807 104.915 97.072  1.00 89.08  ? 277 GLU A C   1 
ATOM   1644 O  O   . GLU A 1 279 ? 158.734 105.730 97.034  1.00 88.78  ? 277 GLU A O   1 
ATOM   1645 C  CB  . GLU A 1 279 ? 158.402 103.306 95.266  1.00 90.21  ? 277 GLU A CB  1 
ATOM   1646 C  CG  . GLU A 1 279 ? 159.841 103.626 94.898  1.00 91.05  ? 277 GLU A CG  1 
ATOM   1647 C  CD  . GLU A 1 279 ? 160.740 102.407 94.960  1.00 92.99  ? 277 GLU A CD  1 
ATOM   1648 O  OE1 . GLU A 1 279 ? 160.641 101.547 94.059  1.00 91.75  ? 277 GLU A OE1 1 
ATOM   1649 O  OE2 . GLU A 1 279 ? 161.544 102.308 95.911  1.00 90.64  ? 277 GLU A OE2 1 
ATOM   1650 N  N   . ILE A 1 280 ? 156.557 105.269 97.378  1.00 84.18  ? 278 ILE A N   1 
ATOM   1651 C  CA  . ILE A 1 280 ? 156.256 106.652 97.735  1.00 83.61  ? 278 ILE A CA  1 
ATOM   1652 C  C   . ILE A 1 280 ? 157.015 107.065 98.987  1.00 85.79  ? 278 ILE A C   1 
ATOM   1653 O  O   . ILE A 1 280 ? 157.342 108.245 99.161  1.00 88.10  ? 278 ILE A O   1 
ATOM   1654 C  CB  . ILE A 1 280 ? 154.735 106.846 97.906  1.00 83.63  ? 278 ILE A CB  1 
ATOM   1655 C  CG1 . ILE A 1 280 ? 154.245 106.101 99.155  1.00 85.37  ? 278 ILE A CG1 1 
ATOM   1656 C  CG2 . ILE A 1 280 ? 154.002 106.406 96.637  1.00 86.69  ? 278 ILE A CG2 1 
ATOM   1657 C  CD1 . ILE A 1 280 ? 152.736 106.022 99.299  1.00 86.03  ? 278 ILE A CD1 1 
ATOM   1658 N  N   . PHE A 1 281 ? 157.306 106.116 99.880  1.00 87.62  ? 279 PHE A N   1 
ATOM   1659 C  CA  . PHE A 1 281 ? 158.131 106.433 101.042 1.00 86.16  ? 279 PHE A CA  1 
ATOM   1660 C  C   . PHE A 1 281 ? 159.539 106.838 100.627 1.00 85.46  ? 279 PHE A C   1 
ATOM   1661 O  O   . PHE A 1 281 ? 160.127 107.753 101.214 1.00 87.33  ? 279 PHE A O   1 
ATOM   1662 C  CB  . PHE A 1 281 ? 158.179 105.246 102.003 1.00 83.57  ? 279 PHE A CB  1 
ATOM   1663 C  CG  . PHE A 1 281 ? 157.018 105.187 102.955 1.00 86.20  ? 279 PHE A CG  1 
ATOM   1664 C  CD1 . PHE A 1 281 ? 155.762 105.628 102.573 1.00 86.63  ? 279 PHE A CD1 1 
ATOM   1665 C  CD2 . PHE A 1 281 ? 157.187 104.693 104.237 1.00 86.61  ? 279 PHE A CD2 1 
ATOM   1666 C  CE1 . PHE A 1 281 ? 154.698 105.576 103.451 1.00 85.93  ? 279 PHE A CE1 1 
ATOM   1667 C  CE2 . PHE A 1 281 ? 156.127 104.638 105.119 1.00 87.42  ? 279 PHE A CE2 1 
ATOM   1668 C  CZ  . PHE A 1 281 ? 154.881 105.080 104.726 1.00 87.83  ? 279 PHE A CZ  1 
ATOM   1669 N  N   . ARG A 1 282 ? 160.098 106.169 99.617  1.00 88.13  ? 280 ARG A N   1 
ATOM   1670 C  CA  . ARG A 1 282 ? 161.429 106.538 99.147  1.00 89.87  ? 280 ARG A CA  1 
ATOM   1671 C  C   . ARG A 1 282 ? 161.446 107.975 98.643  1.00 89.94  ? 280 ARG A C   1 
ATOM   1672 O  O   . ARG A 1 282 ? 162.386 108.728 98.924  1.00 88.98  ? 280 ARG A O   1 
ATOM   1673 C  CB  . ARG A 1 282 ? 161.881 105.570 98.052  1.00 90.83  ? 280 ARG A CB  1 
ATOM   1674 C  CG  . ARG A 1 282 ? 163.034 106.073 97.193  1.00 92.72  ? 280 ARG A CG  1 
ATOM   1675 C  CD  . ARG A 1 282 ? 164.026 104.960 96.901  1.00 92.50  ? 280 ARG A CD  1 
ATOM   1676 N  NE  . ARG A 1 282 ? 164.962 104.763 98.003  1.00 94.16  ? 280 ARG A NE  1 
ATOM   1677 C  CZ  . ARG A 1 282 ? 166.090 105.443 98.166  1.00 93.88  ? 280 ARG A CZ  1 
ATOM   1678 N  NH1 . ARG A 1 282 ? 166.458 106.389 97.317  1.00 91.62  ? 280 ARG A NH1 1 
ATOM   1679 N  NH2 . ARG A 1 282 ? 166.867 105.169 99.210  1.00 93.15  ? 280 ARG A NH2 1 
ATOM   1680 N  N   . LYS A 1 283 ? 160.415 108.376 97.896  1.00 84.38  ? 281 LYS A N   1 
ATOM   1681 C  CA  . LYS A 1 283 ? 160.315 109.767 97.469  1.00 84.48  ? 281 LYS A CA  1 
ATOM   1682 C  C   . LYS A 1 283 ? 160.166 110.695 98.669  1.00 85.59  ? 281 LYS A C   1 
ATOM   1683 O  O   . LYS A 1 283 ? 160.746 111.786 98.697  1.00 86.68  ? 281 LYS A O   1 
ATOM   1684 C  CB  . LYS A 1 283 ? 159.138 109.934 96.508  1.00 85.23  ? 281 LYS A CB  1 
ATOM   1685 C  CG  . LYS A 1 283 ? 158.768 111.380 96.205  1.00 86.36  ? 281 LYS A CG  1 
ATOM   1686 C  CD  . LYS A 1 283 ? 157.582 111.840 97.041  1.00 82.44  ? 281 LYS A CD  1 
ATOM   1687 C  CE  . LYS A 1 283 ? 157.208 113.281 96.737  1.00 84.16  ? 281 LYS A CE  1 
ATOM   1688 N  NZ  . LYS A 1 283 ? 156.729 113.454 95.340  1.00 84.32  ? 281 LYS A NZ  1 
ATOM   1689 N  N   . LEU A 1 284 ? 159.393 110.276 99.668  1.00 80.37  ? 282 LEU A N   1 
ATOM   1690 C  CA  . LEU A 1 284 ? 159.181 111.048 100.884 1.00 77.40  ? 282 LEU A CA  1 
ATOM   1691 C  C   . LEU A 1 284 ? 160.214 110.748 101.963 1.00 77.28  ? 282 LEU A C   1 
ATOM   1692 O  O   . LEU A 1 284 ? 160.084 111.250 103.083 1.00 78.02  ? 282 LEU A O   1 
ATOM   1693 C  CB  . LEU A 1 284 ? 157.778 110.779 101.437 1.00 76.93  ? 282 LEU A CB  1 
ATOM   1694 C  CG  . LEU A 1 284 ? 156.593 111.241 100.585 1.00 79.24  ? 282 LEU A CG  1 
ATOM   1695 C  CD1 . LEU A 1 284 ? 155.286 110.766 101.198 1.00 79.77  ? 282 LEU A CD1 1 
ATOM   1696 C  CD2 . LEU A 1 284 ? 156.586 112.753 100.426 1.00 80.27  ? 282 LEU A CD2 1 
ATOM   1697 N  N   . GLY A 1 285 ? 161.231 109.940 101.657 1.00 79.31  ? 283 GLY A N   1 
ATOM   1698 C  CA  . GLY A 1 285 ? 162.179 109.546 102.687 1.00 78.60  ? 283 GLY A CA  1 
ATOM   1699 C  C   . GLY A 1 285 ? 162.915 110.725 103.293 1.00 77.82  ? 283 GLY A C   1 
ATOM   1700 O  O   . GLY A 1 285 ? 163.008 110.852 104.516 1.00 77.89  ? 283 GLY A O   1 
ATOM   1701 N  N   . LEU A 1 286 ? 163.450 111.606 102.445 1.00 76.42  ? 284 LEU A N   1 
ATOM   1702 C  CA  . LEU A 1 286 ? 164.186 112.756 102.961 1.00 74.33  ? 284 LEU A CA  1 
ATOM   1703 C  C   . LEU A 1 286 ? 163.263 113.709 103.708 1.00 74.86  ? 284 LEU A C   1 
ATOM   1704 O  O   . LEU A 1 286 ? 163.629 114.236 104.765 1.00 75.86  ? 284 LEU A O   1 
ATOM   1705 C  CB  . LEU A 1 286 ? 164.901 113.479 101.819 1.00 74.60  ? 284 LEU A CB  1 
ATOM   1706 C  CG  . LEU A 1 286 ? 166.355 113.883 102.079 1.00 77.14  ? 284 LEU A CG  1 
ATOM   1707 C  CD1 . LEU A 1 286 ? 167.244 112.665 102.288 1.00 78.13  ? 284 LEU A CD1 1 
ATOM   1708 C  CD2 . LEU A 1 286 ? 166.884 114.731 100.935 1.00 77.43  ? 284 LEU A CD2 1 
ATOM   1709 N  N   . TYR A 1 287 ? 162.061 113.942 103.177 1.00 73.76  ? 285 TYR A N   1 
ATOM   1710 C  CA  . TYR A 1 287 ? 161.092 114.773 103.883 1.00 73.24  ? 285 TYR A CA  1 
ATOM   1711 C  C   . TYR A 1 287 ? 160.719 114.151 105.221 1.00 75.06  ? 285 TYR A C   1 
ATOM   1712 O  O   . TYR A 1 287 ? 160.528 114.861 106.214 1.00 75.39  ? 285 TYR A O   1 
ATOM   1713 C  CB  . TYR A 1 287 ? 159.853 114.980 103.013 1.00 78.54  ? 285 TYR A CB  1 
ATOM   1714 C  CG  . TYR A 1 287 ? 158.557 115.063 103.784 1.00 77.52  ? 285 TYR A CG  1 
ATOM   1715 C  CD1 . TYR A 1 287 ? 158.183 116.233 104.428 1.00 71.52  ? 285 TYR A CD1 1 
ATOM   1716 C  CD2 . TYR A 1 287 ? 157.704 113.972 103.862 1.00 79.84  ? 285 TYR A CD2 1 
ATOM   1717 C  CE1 . TYR A 1 287 ? 157.001 116.313 105.129 1.00 71.62  ? 285 TYR A CE1 1 
ATOM   1718 C  CE2 . TYR A 1 287 ? 156.519 114.043 104.561 1.00 79.03  ? 285 TYR A CE2 1 
ATOM   1719 C  CZ  . TYR A 1 287 ? 156.173 115.216 105.192 1.00 76.54  ? 285 TYR A CZ  1 
ATOM   1720 O  OH  . TYR A 1 287 ? 154.992 115.291 105.889 1.00 77.42  ? 285 TYR A OH  1 
ATOM   1721 N  N   . MET A 1 288 ? 160.607 112.823 105.263 1.00 74.71  ? 286 MET A N   1 
ATOM   1722 C  CA  . MET A 1 288 ? 160.384 112.135 106.529 1.00 71.39  ? 286 MET A CA  1 
ATOM   1723 C  C   . MET A 1 288 ? 161.460 112.502 107.542 1.00 73.12  ? 286 MET A C   1 
ATOM   1724 O  O   . MET A 1 288 ? 161.158 112.929 108.661 1.00 74.93  ? 286 MET A O   1 
ATOM   1725 C  CB  . MET A 1 288 ? 160.371 110.625 106.297 1.00 75.78  ? 286 MET A CB  1 
ATOM   1726 C  CG  . MET A 1 288 ? 158.999 109.993 106.286 1.00 75.67  ? 286 MET A CG  1 
ATOM   1727 S  SD  . MET A 1 288 ? 159.057 108.336 105.577 1.00 88.81  ? 286 MET A SD  1 
ATOM   1728 C  CE  . MET A 1 288 ? 159.665 107.396 106.974 1.00 78.32  ? 286 MET A CE  1 
ATOM   1729 N  N   . ALA A 1 289 ? 162.729 112.363 107.153 1.00 69.78  ? 287 ALA A N   1 
ATOM   1730 C  CA  . ALA A 1 289 ? 163.823 112.618 108.082 1.00 68.01  ? 287 ALA A CA  1 
ATOM   1731 C  C   . ALA A 1 289 ? 163.794 114.053 108.589 1.00 70.13  ? 287 ALA A C   1 
ATOM   1732 O  O   . ALA A 1 289 ? 164.102 114.313 109.758 1.00 74.56  ? 287 ALA A O   1 
ATOM   1733 C  CB  . ALA A 1 289 ? 165.161 112.317 107.409 1.00 70.35  ? 287 ALA A CB  1 
ATOM   1734 N  N   . THR A 1 290 ? 163.430 115.001 107.724 1.00 69.95  ? 288 THR A N   1 
ATOM   1735 C  CA  . THR A 1 290 ? 163.403 116.401 108.133 1.00 69.74  ? 288 THR A CA  1 
ATOM   1736 C  C   . THR A 1 290 ? 162.396 116.630 109.253 1.00 70.35  ? 288 THR A C   1 
ATOM   1737 O  O   . THR A 1 290 ? 162.677 117.366 110.207 1.00 69.95  ? 288 THR A O   1 
ATOM   1738 C  CB  . THR A 1 290 ? 163.080 117.290 106.934 1.00 71.59  ? 288 THR A CB  1 
ATOM   1739 O  OG1 . THR A 1 290 ? 164.008 117.021 105.876 1.00 76.14  ? 288 THR A OG1 1 
ATOM   1740 C  CG2 . THR A 1 290 ? 163.169 118.758 107.315 1.00 71.14  ? 288 THR A CG2 1 
ATOM   1741 N  N   . VAL A 1 291 ? 161.215 116.019 109.156 1.00 66.57  ? 289 VAL A N   1 
ATOM   1742 C  CA  . VAL A 1 291 ? 160.212 116.195 110.201 1.00 66.48  ? 289 VAL A CA  1 
ATOM   1743 C  C   . VAL A 1 291 ? 160.668 115.527 111.493 1.00 67.85  ? 289 VAL A C   1 
ATOM   1744 O  O   . VAL A 1 291 ? 160.646 116.140 112.566 1.00 69.41  ? 289 VAL A O   1 
ATOM   1745 C  CB  . VAL A 1 291 ? 158.849 115.651 109.737 1.00 67.07  ? 289 VAL A CB  1 
ATOM   1746 C  CG1 . VAL A 1 291 ? 157.791 115.874 110.810 1.00 67.34  ? 289 VAL A CG1 1 
ATOM   1747 C  CG2 . VAL A 1 291 ? 158.426 116.312 108.435 1.00 70.56  ? 289 VAL A CG2 1 
ATOM   1748 N  N   . LEU A 1 292 ? 161.101 114.267 111.412 1.00 64.58  ? 290 LEU A N   1 
ATOM   1749 C  CA  . LEU A 1 292 ? 161.565 113.581 112.614 1.00 61.53  ? 290 LEU A CA  1 
ATOM   1750 C  C   . LEU A 1 292 ? 162.800 114.256 113.194 1.00 63.62  ? 290 LEU A C   1 
ATOM   1751 O  O   . LEU A 1 292 ? 162.939 114.364 114.417 1.00 65.80  ? 290 LEU A O   1 
ATOM   1752 C  CB  . LEU A 1 292 ? 161.851 112.107 112.317 1.00 63.37  ? 290 LEU A CB  1 
ATOM   1753 C  CG  . LEU A 1 292 ? 160.676 111.144 112.086 1.00 66.72  ? 290 LEU A CG  1 
ATOM   1754 C  CD1 . LEU A 1 292 ? 159.564 111.337 113.114 1.00 64.17  ? 290 LEU A CD1 1 
ATOM   1755 C  CD2 . LEU A 1 292 ? 160.124 111.264 110.680 1.00 65.88  ? 290 LEU A CD2 1 
ATOM   1756 N  N   . THR A 1 293 ? 163.713 114.716 112.335 1.00 65.30  ? 291 THR A N   1 
ATOM   1757 C  CA  . THR A 1 293 ? 164.901 115.398 112.836 1.00 63.48  ? 291 THR A CA  1 
ATOM   1758 C  C   . THR A 1 293 ? 164.522 116.654 113.608 1.00 65.98  ? 291 THR A C   1 
ATOM   1759 O  O   . THR A 1 293 ? 165.067 116.917 114.686 1.00 69.77  ? 291 THR A O   1 
ATOM   1760 C  CB  . THR A 1 293 ? 165.837 115.743 111.678 1.00 62.95  ? 291 THR A CB  1 
ATOM   1761 O  OG1 . THR A 1 293 ? 166.145 114.554 110.941 1.00 69.91  ? 291 THR A OG1 1 
ATOM   1762 C  CG2 . THR A 1 293 ? 167.130 116.354 112.196 1.00 62.92  ? 291 THR A CG2 1 
ATOM   1763 N  N   . GLY A 1 294 ? 163.587 117.442 113.076 1.00 63.47  ? 292 GLY A N   1 
ATOM   1764 C  CA  . GLY A 1 294 ? 163.130 118.615 113.802 1.00 63.77  ? 292 GLY A CA  1 
ATOM   1765 C  C   . GLY A 1 294 ? 162.410 118.254 115.085 1.00 61.13  ? 292 GLY A C   1 
ATOM   1766 O  O   . GLY A 1 294 ? 162.621 118.885 116.124 1.00 62.17  ? 292 GLY A O   1 
ATOM   1767 N  N   . LEU A 1 295 ? 161.547 117.238 115.033 1.00 62.22  ? 293 LEU A N   1 
ATOM   1768 C  CA  . LEU A 1 295 ? 160.863 116.791 116.241 1.00 61.26  ? 293 LEU A CA  1 
ATOM   1769 C  C   . LEU A 1 295 ? 161.851 116.229 117.254 1.00 59.44  ? 293 LEU A C   1 
ATOM   1770 O  O   . LEU A 1 295 ? 161.707 116.452 118.461 1.00 65.39  ? 293 LEU A O   1 
ATOM   1771 C  CB  . LEU A 1 295 ? 159.803 115.747 115.887 1.00 65.09  ? 293 LEU A CB  1 
ATOM   1772 C  CG  . LEU A 1 295 ? 158.637 116.201 115.002 1.00 61.97  ? 293 LEU A CG  1 
ATOM   1773 C  CD1 . LEU A 1 295 ? 157.665 115.057 114.790 1.00 60.26  ? 293 LEU A CD1 1 
ATOM   1774 C  CD2 . LEU A 1 295 ? 157.917 117.401 115.595 1.00 64.54  ? 293 LEU A CD2 1 
ATOM   1775 N  N   . ALA A 1 296 ? 162.860 115.493 116.784 1.00 59.83  ? 294 ALA A N   1 
ATOM   1776 C  CA  . ALA A 1 296 ? 163.879 114.974 117.690 1.00 62.09  ? 294 ALA A CA  1 
ATOM   1777 C  C   . ALA A 1 296 ? 164.709 116.099 118.294 1.00 66.20  ? 294 ALA A C   1 
ATOM   1778 O  O   . ALA A 1 296 ? 164.981 116.098 119.500 1.00 67.18  ? 294 ALA A O   1 
ATOM   1779 C  CB  . ALA A 1 296 ? 164.779 113.984 116.954 1.00 61.52  ? 294 ALA A CB  1 
ATOM   1780 N  N   . ILE A 1 297 ? 165.122 117.066 117.473 1.00 61.87  ? 295 ILE A N   1 
ATOM   1781 C  CA  . ILE A 1 297 ? 165.932 118.173 117.975 1.00 58.43  ? 295 ILE A CA  1 
ATOM   1782 C  C   . ILE A 1 297 ? 165.144 118.995 118.986 1.00 62.45  ? 295 ILE A C   1 
ATOM   1783 O  O   . ILE A 1 297 ? 165.668 119.386 120.035 1.00 64.59  ? 295 ILE A O   1 
ATOM   1784 C  CB  . ILE A 1 297 ? 166.432 119.039 116.803 1.00 59.45  ? 295 ILE A CB  1 
ATOM   1785 C  CG1 . ILE A 1 297 ? 167.484 118.275 115.996 1.00 60.25  ? 295 ILE A CG1 1 
ATOM   1786 C  CG2 . ILE A 1 297 ? 167.006 120.363 117.307 1.00 63.28  ? 295 ILE A CG2 1 
ATOM   1787 C  CD1 . ILE A 1 297 ? 167.841 118.929 114.678 1.00 61.01  ? 295 ILE A CD1 1 
ATOM   1788 N  N   . HIS A 1 298 ? 163.876 119.279 118.685 1.00 58.46  ? 296 HIS A N   1 
ATOM   1789 C  CA  . HIS A 1 298 ? 163.073 120.111 119.574 1.00 52.90  ? 296 HIS A CA  1 
ATOM   1790 C  C   . HIS A 1 298 ? 162.859 119.433 120.922 1.00 55.08  ? 296 HIS A C   1 
ATOM   1791 O  O   . HIS A 1 298 ? 163.032 120.054 121.976 1.00 59.53  ? 296 HIS A O   1 
ATOM   1792 C  CB  . HIS A 1 298 ? 161.732 120.427 118.915 1.00 57.40  ? 296 HIS A CB  1 
ATOM   1793 C  CG  . HIS A 1 298 ? 161.023 121.594 119.523 1.00 55.91  ? 296 HIS A CG  1 
ATOM   1794 N  ND1 . HIS A 1 298 ? 159.830 121.469 120.201 1.00 53.83  ? 296 HIS A ND1 1 
ATOM   1795 C  CD2 . HIS A 1 298 ? 161.335 122.911 119.552 1.00 58.30  ? 296 HIS A CD2 1 
ATOM   1796 C  CE1 . HIS A 1 298 ? 159.440 122.657 120.625 1.00 56.92  ? 296 HIS A CE1 1 
ATOM   1797 N  NE2 . HIS A 1 298 ? 160.336 123.549 120.244 1.00 57.08  ? 296 HIS A NE2 1 
ATOM   1798 N  N   . SER A 1 299 ? 162.484 118.155 120.907 1.00 58.53  ? 297 SER A N   1 
ATOM   1799 C  CA  . SER A 1 299 ? 162.109 117.466 122.136 1.00 57.97  ? 297 SER A CA  1 
ATOM   1800 C  C   . SER A 1 299 ? 163.307 116.993 122.948 1.00 58.71  ? 297 SER A C   1 
ATOM   1801 O  O   . SER A 1 299 ? 163.176 116.810 124.162 1.00 60.15  ? 297 SER A O   1 
ATOM   1802 C  CB  . SER A 1 299 ? 161.214 116.268 121.815 1.00 61.14  ? 297 SER A CB  1 
ATOM   1803 O  OG  . SER A 1 299 ? 161.585 115.668 120.589 1.00 68.79  ? 297 SER A OG  1 
ATOM   1804 N  N   . ILE A 1 300 ? 164.461 116.786 122.316 1.00 59.18  ? 298 ILE A N   1 
ATOM   1805 C  CA  . ILE A 1 300 ? 165.604 116.185 122.994 1.00 59.89  ? 298 ILE A CA  1 
ATOM   1806 C  C   . ILE A 1 300 ? 166.602 117.259 123.408 1.00 62.97  ? 298 ILE A C   1 
ATOM   1807 O  O   . ILE A 1 300 ? 167.365 117.070 124.362 1.00 70.75  ? 298 ILE A O   1 
ATOM   1808 C  CB  . ILE A 1 300 ? 166.277 115.125 122.103 1.00 58.80  ? 298 ILE A CB  1 
ATOM   1809 C  CG1 . ILE A 1 300 ? 165.273 114.021 121.758 1.00 61.10  ? 298 ILE A CG1 1 
ATOM   1810 C  CG2 . ILE A 1 300 ? 167.508 114.543 122.798 1.00 58.85  ? 298 ILE A CG2 1 
ATOM   1811 C  CD1 . ILE A 1 300 ? 165.810 112.943 120.836 1.00 62.06  ? 298 ILE A CD1 1 
ATOM   1812 N  N   . VAL A 1 301 ? 166.608 118.390 122.705 1.00 58.79  ? 299 VAL A N   1 
ATOM   1813 C  CA  . VAL A 1 301 ? 167.613 119.419 122.946 1.00 57.99  ? 299 VAL A CA  1 
ATOM   1814 C  C   . VAL A 1 301 ? 166.951 120.696 123.445 1.00 59.17  ? 299 VAL A C   1 
ATOM   1815 O  O   . VAL A 1 301 ? 167.218 121.149 124.563 1.00 60.81  ? 299 VAL A O   1 
ATOM   1816 C  CB  . VAL A 1 301 ? 168.438 119.690 121.673 1.00 60.95  ? 299 VAL A CB  1 
ATOM   1817 C  CG1 . VAL A 1 301 ? 169.483 120.769 121.927 1.00 63.05  ? 299 VAL A CG1 1 
ATOM   1818 C  CG2 . VAL A 1 301 ? 169.099 118.412 121.186 1.00 57.59  ? 299 VAL A CG2 1 
ATOM   1819 N  N   . ILE A 1 302 ? 166.079 121.283 122.626 1.00 59.63  ? 300 ILE A N   1 
ATOM   1820 C  CA  . ILE A 1 302 ? 165.543 122.606 122.938 1.00 58.27  ? 300 ILE A CA  1 
ATOM   1821 C  C   . ILE A 1 302 ? 164.675 122.552 124.189 1.00 62.32  ? 300 ILE A C   1 
ATOM   1822 O  O   . ILE A 1 302 ? 164.957 123.221 125.189 1.00 62.69  ? 300 ILE A O   1 
ATOM   1823 C  CB  . ILE A 1 302 ? 164.767 123.166 121.735 1.00 56.85  ? 300 ILE A CB  1 
ATOM   1824 C  CG1 . ILE A 1 302 ? 165.737 123.432 120.580 1.00 54.98  ? 300 ILE A CG1 1 
ATOM   1825 C  CG2 . ILE A 1 302 ? 164.005 124.428 122.127 1.00 57.29  ? 300 ILE A CG2 1 
ATOM   1826 C  CD1 . ILE A 1 302 ? 165.088 123.978 119.329 1.00 60.80  ? 300 ILE A CD1 1 
ATOM   1827 N  N   . LEU A 1 303 ? 163.601 121.764 124.149 1.00 65.22  ? 301 LEU A N   1 
ATOM   1828 C  CA  . LEU A 1 303 ? 162.689 121.720 125.290 1.00 58.30  ? 301 LEU A CA  1 
ATOM   1829 C  C   . LEU A 1 303 ? 163.406 121.340 126.576 1.00 60.23  ? 301 LEU A C   1 
ATOM   1830 O  O   . LEU A 1 303 ? 163.210 122.028 127.593 1.00 61.45  ? 301 LEU A O   1 
ATOM   1831 C  CB  . LEU A 1 303 ? 161.526 120.770 124.985 1.00 57.88  ? 301 LEU A CB  1 
ATOM   1832 C  CG  . LEU A 1 303 ? 160.423 121.286 124.054 1.00 60.05  ? 301 LEU A CG  1 
ATOM   1833 C  CD1 . LEU A 1 303 ? 159.358 120.220 123.863 1.00 57.38  ? 301 LEU A CD1 1 
ATOM   1834 C  CD2 . LEU A 1 303 ? 159.791 122.571 124.571 1.00 59.17  ? 301 LEU A CD2 1 
ATOM   1835 N  N   . PRO A 1 304 ? 164.232 120.292 126.618 1.00 65.18  ? 302 PRO A N   1 
ATOM   1836 C  CA  . PRO A 1 304 ? 165.037 120.066 127.829 1.00 62.88  ? 302 PRO A CA  1 
ATOM   1837 C  C   . PRO A 1 304 ? 165.936 121.238 128.177 1.00 59.71  ? 302 PRO A C   1 
ATOM   1838 O  O   . PRO A 1 304 ? 166.127 121.534 129.363 1.00 65.25  ? 302 PRO A O   1 
ATOM   1839 C  CB  . PRO A 1 304 ? 165.844 118.811 127.473 1.00 65.73  ? 302 PRO A CB  1 
ATOM   1840 C  CG  . PRO A 1 304 ? 165.000 118.098 126.489 1.00 64.91  ? 302 PRO A CG  1 
ATOM   1841 C  CD  . PRO A 1 304 ? 164.348 119.171 125.671 1.00 64.79  ? 302 PRO A CD  1 
ATOM   1842 N  N   . LEU A 1 305 ? 166.501 121.917 127.176 1.00 58.79  ? 303 LEU A N   1 
ATOM   1843 C  CA  . LEU A 1 305 ? 167.363 123.061 127.458 1.00 63.38  ? 303 LEU A CA  1 
ATOM   1844 C  C   . LEU A 1 305 ? 166.581 124.188 128.118 1.00 65.81  ? 303 LEU A C   1 
ATOM   1845 O  O   . LEU A 1 305 ? 167.029 124.770 129.112 1.00 68.57  ? 303 LEU A O   1 
ATOM   1846 C  CB  . LEU A 1 305 ? 168.023 123.552 126.170 1.00 67.00  ? 303 LEU A CB  1 
ATOM   1847 C  CG  . LEU A 1 305 ? 169.140 124.581 126.352 1.00 66.85  ? 303 LEU A CG  1 
ATOM   1848 C  CD1 . LEU A 1 305 ? 170.503 123.924 126.210 1.00 64.80  ? 303 LEU A CD1 1 
ATOM   1849 C  CD2 . LEU A 1 305 ? 168.983 125.722 125.358 1.00 61.81  ? 303 LEU A CD2 1 
ATOM   1850 N  N   . ILE A 1 306 ? 165.400 124.508 127.584 1.00 61.37  ? 304 ILE A N   1 
ATOM   1851 C  CA  . ILE A 1 306 ? 164.574 125.542 128.199 1.00 54.89  ? 304 ILE A CA  1 
ATOM   1852 C  C   . ILE A 1 306 ? 164.194 125.137 129.615 1.00 59.23  ? 304 ILE A C   1 
ATOM   1853 O  O   . ILE A 1 306 ? 164.149 125.972 130.526 1.00 62.63  ? 304 ILE A O   1 
ATOM   1854 C  CB  . ILE A 1 306 ? 163.329 125.818 127.334 1.00 57.25  ? 304 ILE A CB  1 
ATOM   1855 C  CG1 . ILE A 1 306 ? 163.749 126.368 125.969 1.00 61.46  ? 304 ILE A CG1 1 
ATOM   1856 C  CG2 . ILE A 1 306 ? 162.390 126.793 128.040 1.00 59.70  ? 304 ILE A CG2 1 
ATOM   1857 C  CD1 . ILE A 1 306 ? 162.606 126.551 124.988 1.00 63.25  ? 304 ILE A CD1 1 
ATOM   1858 N  N   . TYR A 1 307 ? 163.907 123.851 129.822 1.00 64.80  ? 305 TYR A N   1 
ATOM   1859 C  CA  . TYR A 1 307 ? 163.573 123.374 131.158 1.00 63.50  ? 305 TYR A CA  1 
ATOM   1860 C  C   . TYR A 1 307 ? 164.730 123.587 132.126 1.00 65.17  ? 305 TYR A C   1 
ATOM   1861 O  O   . TYR A 1 307 ? 164.551 124.145 133.214 1.00 68.53  ? 305 TYR A O   1 
ATOM   1862 C  CB  . TYR A 1 307 ? 163.190 121.897 131.101 1.00 63.55  ? 305 TYR A CB  1 
ATOM   1863 C  CG  . TYR A 1 307 ? 162.545 121.389 132.366 1.00 65.16  ? 305 TYR A CG  1 
ATOM   1864 C  CD1 . TYR A 1 307 ? 161.254 121.759 132.708 1.00 70.15  ? 305 TYR A CD1 1 
ATOM   1865 C  CD2 . TYR A 1 307 ? 163.235 120.554 133.230 1.00 64.78  ? 305 TYR A CD2 1 
ATOM   1866 C  CE1 . TYR A 1 307 ? 160.664 121.300 133.867 1.00 68.31  ? 305 TYR A CE1 1 
ATOM   1867 C  CE2 . TYR A 1 307 ? 162.655 120.089 134.389 1.00 65.55  ? 305 TYR A CE2 1 
ATOM   1868 C  CZ  . TYR A 1 307 ? 161.370 120.465 134.704 1.00 67.06  ? 305 TYR A CZ  1 
ATOM   1869 O  OH  . TYR A 1 307 ? 160.789 120.006 135.862 1.00 71.15  ? 305 TYR A OH  1 
ATOM   1870 N  N   . PHE A 1 308 ? 165.934 123.159 131.739 1.00 67.58  ? 306 PHE A N   1 
ATOM   1871 C  CA  . PHE A 1 308 ? 167.077 123.272 132.639 1.00 67.40  ? 306 PHE A CA  1 
ATOM   1872 C  C   . PHE A 1 308 ? 167.404 124.727 132.943 1.00 67.84  ? 306 PHE A C   1 
ATOM   1873 O  O   . PHE A 1 308 ? 167.775 125.064 134.073 1.00 72.24  ? 306 PHE A O   1 
ATOM   1874 C  CB  . PHE A 1 308 ? 168.292 122.571 132.034 1.00 70.82  ? 306 PHE A CB  1 
ATOM   1875 C  CG  . PHE A 1 308 ? 169.514 122.627 132.904 1.00 73.96  ? 306 PHE A CG  1 
ATOM   1876 C  CD1 . PHE A 1 308 ? 169.634 121.794 134.003 1.00 71.41  ? 306 PHE A CD1 1 
ATOM   1877 C  CD2 . PHE A 1 308 ? 170.538 123.515 132.627 1.00 72.19  ? 306 PHE A CD2 1 
ATOM   1878 C  CE1 . PHE A 1 308 ? 170.756 121.842 134.808 1.00 71.41  ? 306 PHE A CE1 1 
ATOM   1879 C  CE2 . PHE A 1 308 ? 171.662 123.569 133.430 1.00 70.66  ? 306 PHE A CE2 1 
ATOM   1880 C  CZ  . PHE A 1 308 ? 171.770 122.731 134.521 1.00 70.83  ? 306 PHE A CZ  1 
ATOM   1881 N  N   . ILE A 1 309 ? 167.272 125.606 131.950 1.00 64.72  ? 307 ILE A N   1 
ATOM   1882 C  CA  . ILE A 1 309 ? 167.605 127.011 132.162 1.00 65.64  ? 307 ILE A CA  1 
ATOM   1883 C  C   . ILE A 1 309 ? 166.724 127.604 133.253 1.00 66.50  ? 307 ILE A C   1 
ATOM   1884 O  O   . ILE A 1 309 ? 167.205 128.323 134.137 1.00 68.91  ? 307 ILE A O   1 
ATOM   1885 C  CB  . ILE A 1 309 ? 167.482 127.793 130.837 1.00 62.91  ? 307 ILE A CB  1 
ATOM   1886 C  CG1 . ILE A 1 309 ? 168.636 127.478 129.867 1.00 66.75  ? 307 ILE A CG1 1 
ATOM   1887 C  CG2 . ILE A 1 309 ? 167.439 129.299 131.091 1.00 63.68  ? 307 ILE A CG2 1 
ATOM   1888 C  CD1 . ILE A 1 309 ? 170.001 127.199 130.494 1.00 65.70  ? 307 ILE A CD1 1 
ATOM   1889 N  N   . VAL A 1 310 ? 165.426 127.312 133.213 1.00 63.77  ? 308 VAL A N   1 
ATOM   1890 C  CA  . VAL A 1 310 ? 164.486 127.949 134.131 1.00 63.01  ? 308 VAL A CA  1 
ATOM   1891 C  C   . VAL A 1 310 ? 164.510 127.263 135.491 1.00 65.65  ? 308 VAL A C   1 
ATOM   1892 O  O   . VAL A 1 310 ? 164.836 127.879 136.512 1.00 68.05  ? 308 VAL A O   1 
ATOM   1893 C  CB  . VAL A 1 310 ? 163.070 127.951 133.524 1.00 63.22  ? 308 VAL A CB  1 
ATOM   1894 C  CG1 . VAL A 1 310 ? 162.023 128.308 134.572 1.00 64.74  ? 308 VAL A CG1 1 
ATOM   1895 C  CG2 . VAL A 1 310 ? 163.000 128.915 132.352 1.00 63.06  ? 308 VAL A CG2 1 
ATOM   1896 N  N   . VAL A 1 311 ? 164.166 125.975 135.525 1.00 67.49  ? 309 VAL A N   1 
ATOM   1897 C  CA  . VAL A 1 311 ? 164.015 125.285 136.802 1.00 69.00  ? 309 VAL A CA  1 
ATOM   1898 C  C   . VAL A 1 311 ? 165.366 124.843 137.356 1.00 68.37  ? 309 VAL A C   1 
ATOM   1899 O  O   . VAL A 1 311 ? 165.528 124.730 138.576 1.00 66.67  ? 309 VAL A O   1 
ATOM   1900 C  CB  . VAL A 1 311 ? 163.033 124.105 136.671 1.00 69.16  ? 309 VAL A CB  1 
ATOM   1901 C  CG1 . VAL A 1 311 ? 162.967 123.307 137.972 1.00 64.61  ? 309 VAL A CG1 1 
ATOM   1902 C  CG2 . VAL A 1 311 ? 161.652 124.570 136.257 1.00 70.94  ? 309 VAL A CG2 1 
ATOM   1903 N  N   . ARG A 1 312 ? 166.343 124.566 136.489 1.00 72.16  ? 310 ARG A N   1 
ATOM   1904 C  CA  . ARG A 1 312 ? 167.667 124.102 136.911 1.00 73.04  ? 310 ARG A CA  1 
ATOM   1905 C  C   . ARG A 1 312 ? 167.592 122.711 137.542 1.00 71.72  ? 310 ARG A C   1 
ATOM   1906 O  O   . ARG A 1 312 ? 168.252 122.427 138.542 1.00 73.99  ? 310 ARG A O   1 
ATOM   1907 C  CB  . ARG A 1 312 ? 168.333 125.101 137.866 1.00 70.16  ? 310 ARG A CB  1 
ATOM   1908 C  CG  . ARG A 1 312 ? 169.082 126.248 137.189 1.00 71.51  ? 310 ARG A CG  1 
ATOM   1909 C  CD  . ARG A 1 312 ? 170.172 125.766 136.227 1.00 70.02  ? 310 ARG A CD  1 
ATOM   1910 N  NE  . ARG A 1 312 ? 170.934 126.856 135.626 1.00 71.34  ? 310 ARG A NE  1 
ATOM   1911 C  CZ  . ARG A 1 312 ? 171.670 127.737 136.292 1.00 72.84  ? 310 ARG A CZ  1 
ATOM   1912 N  NH1 . ARG A 1 312 ? 171.756 127.718 137.612 1.00 70.02  ? 310 ARG A NH1 1 
ATOM   1913 N  NH2 . ARG A 1 312 ? 172.323 128.677 135.615 1.00 74.09  ? 310 ARG A NH2 1 
ATOM   1914 N  N   . LYS A 1 313 ? 166.776 121.843 136.951 1.00 72.97  ? 311 LYS A N   1 
ATOM   1915 C  CA  . LYS A 1 313 ? 166.635 120.463 137.383 1.00 75.71  ? 311 LYS A CA  1 
ATOM   1916 C  C   . LYS A 1 313 ? 166.767 119.562 136.164 1.00 75.73  ? 311 LYS A C   1 
ATOM   1917 O  O   . LYS A 1 313 ? 166.546 119.987 135.028 1.00 75.80  ? 311 LYS A O   1 
ATOM   1918 C  CB  . LYS A 1 313 ? 165.290 120.218 138.080 1.00 75.70  ? 311 LYS A CB  1 
ATOM   1919 C  CG  . LYS A 1 313 ? 165.190 120.844 139.465 1.00 77.05  ? 311 LYS A CG  1 
ATOM   1920 C  CD  . LYS A 1 313 ? 164.033 120.272 140.276 1.00 77.57  ? 311 LYS A CD  1 
ATOM   1921 C  CE  . LYS A 1 313 ? 162.676 120.593 139.660 1.00 76.28  ? 311 LYS A CE  1 
ATOM   1922 N  NZ  . LYS A 1 313 ? 161.636 119.607 140.062 1.00 75.86  ? 311 LYS A NZ  1 
ATOM   1923 N  N   . ASN A 1 314 ? 167.136 118.307 136.410 1.00 75.23  ? 312 ASN A N   1 
ATOM   1924 C  CA  . ASN A 1 314 ? 167.388 117.363 135.329 1.00 75.43  ? 312 ASN A CA  1 
ATOM   1925 C  C   . ASN A 1 314 ? 166.163 117.257 134.426 1.00 73.51  ? 312 ASN A C   1 
ATOM   1926 O  O   . ASN A 1 314 ? 165.153 116.662 134.823 1.00 67.80  ? 312 ASN A O   1 
ATOM   1927 C  CB  . ASN A 1 314 ? 167.752 115.990 135.893 1.00 74.33  ? 312 ASN A CB  1 
ATOM   1928 C  CG  . ASN A 1 314 ? 168.602 115.174 134.940 1.00 77.21  ? 312 ASN A CG  1 
ATOM   1929 O  OD1 . ASN A 1 314 ? 169.076 115.678 133.922 1.00 75.22  ? 312 ASN A OD1 1 
ATOM   1930 N  ND2 . ASN A 1 314 ? 168.800 113.902 135.267 1.00 76.54  ? 312 ASN A ND2 1 
ATOM   1931 N  N   . PRO A 1 315 ? 166.206 117.813 133.212 1.00 74.66  ? 313 PRO A N   1 
ATOM   1932 C  CA  . PRO A 1 315 ? 165.027 117.722 132.336 1.00 68.96  ? 313 PRO A CA  1 
ATOM   1933 C  C   . PRO A 1 315 ? 164.632 116.298 132.008 1.00 68.58  ? 313 PRO A C   1 
ATOM   1934 O  O   . PRO A 1 315 ? 163.439 116.015 131.847 1.00 71.54  ? 313 PRO A O   1 
ATOM   1935 C  CB  . PRO A 1 315 ? 165.460 118.489 131.078 1.00 68.94  ? 313 PRO A CB  1 
ATOM   1936 C  CG  . PRO A 1 315 ? 166.624 119.314 131.498 1.00 69.74  ? 313 PRO A CG  1 
ATOM   1937 C  CD  . PRO A 1 315 ? 167.314 118.526 132.555 1.00 73.62  ? 313 PRO A CD  1 
ATOM   1938 N  N   . PHE A 1 316 ? 165.602 115.390 131.901 1.00 75.27  ? 314 PHE A N   1 
ATOM   1939 C  CA  . PHE A 1 316 ? 165.297 114.031 131.471 1.00 76.08  ? 314 PHE A CA  1 
ATOM   1940 C  C   . PHE A 1 316 ? 164.613 113.232 132.573 1.00 73.78  ? 314 PHE A C   1 
ATOM   1941 O  O   . PHE A 1 316 ? 163.871 112.288 132.280 1.00 70.94  ? 314 PHE A O   1 
ATOM   1942 C  CB  . PHE A 1 316 ? 166.579 113.346 131.005 1.00 72.20  ? 314 PHE A CB  1 
ATOM   1943 C  CG  . PHE A 1 316 ? 167.320 114.121 129.953 1.00 75.80  ? 314 PHE A CG  1 
ATOM   1944 C  CD1 . PHE A 1 316 ? 166.782 114.280 128.687 1.00 75.10  ? 314 PHE A CD1 1 
ATOM   1945 C  CD2 . PHE A 1 316 ? 168.533 114.722 130.239 1.00 76.05  ? 314 PHE A CD2 1 
ATOM   1946 C  CE1 . PHE A 1 316 ? 167.451 115.003 127.719 1.00 72.52  ? 314 PHE A CE1 1 
ATOM   1947 C  CE2 . PHE A 1 316 ? 169.206 115.449 129.273 1.00 76.03  ? 314 PHE A CE2 1 
ATOM   1948 C  CZ  . PHE A 1 316 ? 168.664 115.588 128.012 1.00 71.40  ? 314 PHE A CZ  1 
ATOM   1949 N  N   . ARG A 1 317 ? 164.846 113.586 133.838 1.00 73.86  ? 315 ARG A N   1 
ATOM   1950 C  CA  . ARG A 1 317 ? 164.067 112.983 134.914 1.00 73.79  ? 315 ARG A CA  1 
ATOM   1951 C  C   . ARG A 1 317 ? 162.601 113.386 134.818 1.00 75.59  ? 315 ARG A C   1 
ATOM   1952 O  O   . ARG A 1 317 ? 161.709 112.548 134.990 1.00 76.27  ? 315 ARG A O   1 
ATOM   1953 C  CB  . ARG A 1 317 ? 164.644 113.383 136.272 1.00 73.06  ? 315 ARG A CB  1 
ATOM   1954 C  CG  . ARG A 1 317 ? 165.626 112.378 136.857 1.00 75.73  ? 315 ARG A CG  1 
ATOM   1955 C  CD  . ARG A 1 317 ? 164.936 111.078 137.244 1.00 77.20  ? 315 ARG A CD  1 
ATOM   1956 N  NE  . ARG A 1 317 ? 165.823 110.178 137.973 1.00 78.20  ? 315 ARG A NE  1 
ATOM   1957 C  CZ  . ARG A 1 317 ? 166.252 110.384 139.210 1.00 77.60  ? 315 ARG A CZ  1 
ATOM   1958 N  NH1 . ARG A 1 317 ? 165.887 111.453 139.901 1.00 74.82  ? 315 ARG A NH1 1 
ATOM   1959 N  NH2 . ARG A 1 317 ? 167.066 109.495 139.771 1.00 76.24  ? 315 ARG A NH2 1 
ATOM   1960 N  N   . PHE A 1 318 ? 162.332 114.666 134.545 1.00 69.67  ? 316 PHE A N   1 
ATOM   1961 C  CA  . PHE A 1 318 ? 160.953 115.105 134.363 1.00 67.04  ? 316 PHE A CA  1 
ATOM   1962 C  C   . PHE A 1 318 ? 160.316 114.424 133.160 1.00 65.81  ? 316 PHE A C   1 
ATOM   1963 O  O   . PHE A 1 318 ? 159.170 113.966 133.230 1.00 65.07  ? 316 PHE A O   1 
ATOM   1964 C  CB  . PHE A 1 318 ? 160.901 116.623 134.205 1.00 68.27  ? 316 PHE A CB  1 
ATOM   1965 C  CG  . PHE A 1 318 ? 159.507 117.176 134.128 1.00 69.92  ? 316 PHE A CG  1 
ATOM   1966 C  CD1 . PHE A 1 318 ? 158.757 117.367 135.273 1.00 67.65  ? 316 PHE A CD1 1 
ATOM   1967 C  CD2 . PHE A 1 318 ? 158.947 117.503 132.906 1.00 70.00  ? 316 PHE A CD2 1 
ATOM   1968 C  CE1 . PHE A 1 318 ? 157.475 117.874 135.200 1.00 68.79  ? 316 PHE A CE1 1 
ATOM   1969 C  CE2 . PHE A 1 318 ? 157.667 118.009 132.829 1.00 65.14  ? 316 PHE A CE2 1 
ATOM   1970 C  CZ  . PHE A 1 318 ? 156.931 118.194 133.976 1.00 66.35  ? 316 PHE A CZ  1 
ATOM   1971 N  N   . ALA A 1 319 ? 161.044 114.347 132.044 1.00 67.85  ? 317 ALA A N   1 
ATOM   1972 C  CA  . ALA A 1 319 ? 160.516 113.664 130.869 1.00 71.60  ? 317 ALA A CA  1 
ATOM   1973 C  C   . ALA A 1 319 ? 160.366 112.170 131.117 1.00 75.41  ? 317 ALA A C   1 
ATOM   1974 O  O   . ALA A 1 319 ? 159.469 111.536 130.552 1.00 71.32  ? 317 ALA A O   1 
ATOM   1975 C  CB  . ALA A 1 319 ? 161.424 113.912 129.666 1.00 69.45  ? 317 ALA A CB  1 
ATOM   1976 N  N   . MET A 1 320 ? 161.234 111.593 131.952 1.00 76.80  ? 318 MET A N   1 
ATOM   1977 C  CA  . MET A 1 320 ? 161.136 110.169 132.250 1.00 76.03  ? 318 MET A CA  1 
ATOM   1978 C  C   . MET A 1 320 ? 159.824 109.847 132.953 1.00 75.47  ? 318 MET A C   1 
ATOM   1979 O  O   . MET A 1 320 ? 159.192 108.824 132.668 1.00 72.65  ? 318 MET A O   1 
ATOM   1980 C  CB  . MET A 1 320 ? 162.328 109.734 133.103 1.00 75.10  ? 318 MET A CB  1 
ATOM   1981 C  CG  . MET A 1 320 ? 162.211 108.322 133.670 1.00 75.53  ? 318 MET A CG  1 
ATOM   1982 S  SD  . MET A 1 320 ? 163.705 107.694 134.473 1.00 84.97  ? 318 MET A SD  1 
ATOM   1983 C  CE  . MET A 1 320 ? 164.982 108.055 133.267 1.00 75.03  ? 318 MET A CE  1 
ATOM   1984 N  N   . GLY A 1 321 ? 159.400 110.708 133.879 1.00 72.12  ? 319 GLY A N   1 
ATOM   1985 C  CA  . GLY A 1 321 ? 158.156 110.458 134.589 1.00 73.45  ? 319 GLY A CA  1 
ATOM   1986 C  C   . GLY A 1 321 ? 156.954 110.442 133.666 1.00 73.78  ? 319 GLY A C   1 
ATOM   1987 O  O   . GLY A 1 321 ? 156.022 109.657 133.859 1.00 73.39  ? 319 GLY A O   1 
ATOM   1988 N  N   . MET A 1 322 ? 156.958 111.303 132.651 1.00 71.55  ? 320 MET A N   1 
ATOM   1989 C  CA  . MET A 1 322 ? 155.859 111.393 131.698 1.00 67.22  ? 320 MET A CA  1 
ATOM   1990 C  C   . MET A 1 322 ? 155.852 110.245 130.696 1.00 68.69  ? 320 MET A C   1 
ATOM   1991 O  O   . MET A 1 322 ? 155.063 110.283 129.747 1.00 67.49  ? 320 MET A O   1 
ATOM   1992 C  CB  . MET A 1 322 ? 155.930 112.721 130.937 1.00 63.80  ? 320 MET A CB  1 
ATOM   1993 C  CG  . MET A 1 322 ? 155.927 113.967 131.812 1.00 68.56  ? 320 MET A CG  1 
ATOM   1994 S  SD  . MET A 1 322 ? 154.577 114.019 133.000 1.00 80.54  ? 320 MET A SD  1 
ATOM   1995 C  CE  . MET A 1 322 ? 153.277 114.756 132.015 1.00 71.60  ? 320 MET A CE  1 
ATOM   1996 N  N   . ALA A 1 323 ? 156.702 109.232 130.885 1.00 73.08  ? 321 ALA A N   1 
ATOM   1997 C  CA  . ALA A 1 323 ? 156.803 108.147 129.914 1.00 69.73  ? 321 ALA A CA  1 
ATOM   1998 C  C   . ALA A 1 323 ? 155.439 107.550 129.592 1.00 64.72  ? 321 ALA A C   1 
ATOM   1999 O  O   . ALA A 1 323 ? 155.145 107.246 128.431 1.00 67.75  ? 321 ALA A O   1 
ATOM   2000 C  CB  . ALA A 1 323 ? 157.747 107.065 130.437 1.00 67.19  ? 321 ALA A CB  1 
ATOM   2001 N  N   . GLN A 1 324 ? 154.589 107.375 130.605 1.00 64.38  ? 322 GLN A N   1 
ATOM   2002 C  CA  . GLN A 1 324 ? 153.251 106.855 130.344 1.00 72.41  ? 322 GLN A CA  1 
ATOM   2003 C  C   . GLN A 1 324 ? 152.470 107.803 129.444 1.00 69.22  ? 322 GLN A C   1 
ATOM   2004 O  O   . GLN A 1 324 ? 151.778 107.365 128.518 1.00 68.43  ? 322 GLN A O   1 
ATOM   2005 C  CB  . GLN A 1 324 ? 152.497 106.624 131.654 1.00 76.12  ? 322 GLN A CB  1 
ATOM   2006 C  CG  . GLN A 1 324 ? 153.273 105.862 132.724 1.00 74.04  ? 322 GLN A CG  1 
ATOM   2007 C  CD  . GLN A 1 324 ? 153.465 104.401 132.380 1.00 76.10  ? 322 GLN A CD  1 
ATOM   2008 O  OE1 . GLN A 1 324 ? 154.105 104.065 131.385 1.00 73.76  ? 322 GLN A OE1 1 
ATOM   2009 N  NE2 . GLN A 1 324 ? 152.912 103.521 133.206 1.00 75.84  ? 322 GLN A NE2 1 
ATOM   2010 N  N   . ALA A 1 325 ? 152.569 109.110 129.699 1.00 65.85  ? 323 ALA A N   1 
ATOM   2011 C  CA  . ALA A 1 325 ? 151.905 110.084 128.839 1.00 65.07  ? 323 ALA A CA  1 
ATOM   2012 C  C   . ALA A 1 325 ? 152.581 110.171 127.477 1.00 66.70  ? 323 ALA A C   1 
ATOM   2013 O  O   . ALA A 1 325 ? 151.903 110.263 126.448 1.00 68.89  ? 323 ALA A O   1 
ATOM   2014 C  CB  . ALA A 1 325 ? 151.885 111.453 129.515 1.00 62.27  ? 323 ALA A CB  1 
ATOM   2015 N  N   . LEU A 1 326 ? 153.915 110.155 127.449 1.00 64.39  ? 324 LEU A N   1 
ATOM   2016 C  CA  . LEU A 1 326 ? 154.623 110.198 126.174 1.00 60.87  ? 324 LEU A CA  1 
ATOM   2017 C  C   . LEU A 1 326 ? 154.378 108.926 125.374 1.00 65.35  ? 324 LEU A C   1 
ATOM   2018 O  O   . LEU A 1 326 ? 154.011 108.983 124.195 1.00 66.10  ? 324 LEU A O   1 
ATOM   2019 C  CB  . LEU A 1 326 ? 156.121 110.400 126.406 1.00 64.56  ? 324 LEU A CB  1 
ATOM   2020 C  CG  . LEU A 1 326 ? 156.559 111.632 127.201 1.00 70.92  ? 324 LEU A CG  1 
ATOM   2021 C  CD1 . LEU A 1 326 ? 158.074 111.741 127.199 1.00 65.01  ? 324 LEU A CD1 1 
ATOM   2022 C  CD2 . LEU A 1 326 ? 155.930 112.902 126.650 1.00 69.08  ? 324 LEU A CD2 1 
ATOM   2023 N  N   . LEU A 1 327 ? 154.569 107.764 126.004 1.00 69.94  ? 325 LEU A N   1 
ATOM   2024 C  CA  . LEU A 1 327 ? 154.343 106.505 125.303 1.00 66.65  ? 325 LEU A CA  1 
ATOM   2025 C  C   . LEU A 1 327 ? 152.885 106.365 124.891 1.00 61.17  ? 325 LEU A C   1 
ATOM   2026 O  O   . LEU A 1 327 ? 152.586 105.880 123.794 1.00 59.13  ? 325 LEU A O   1 
ATOM   2027 C  CB  . LEU A 1 327 ? 154.766 105.326 126.181 1.00 64.39  ? 325 LEU A CB  1 
ATOM   2028 C  CG  . LEU A 1 327 ? 155.047 104.010 125.450 1.00 68.57  ? 325 LEU A CG  1 
ATOM   2029 C  CD1 . LEU A 1 327 ? 156.228 104.138 124.494 1.00 64.59  ? 325 LEU A CD1 1 
ATOM   2030 C  CD2 . LEU A 1 327 ? 155.282 102.884 126.441 1.00 67.07  ? 325 LEU A CD2 1 
ATOM   2031 N  N   . THR A 1 328 ? 151.961 106.779 125.759 1.00 55.89  ? 326 THR A N   1 
ATOM   2032 C  CA  . THR A 1 328 ? 150.555 106.793 125.375 1.00 62.78  ? 326 THR A CA  1 
ATOM   2033 C  C   . THR A 1 328 ? 150.336 107.695 124.169 1.00 64.21  ? 326 THR A C   1 
ATOM   2034 O  O   . THR A 1 328 ? 149.682 107.302 123.198 1.00 66.64  ? 326 THR A O   1 
ATOM   2035 C  CB  . THR A 1 328 ? 149.691 107.249 126.552 1.00 62.31  ? 326 THR A CB  1 
ATOM   2036 O  OG1 . THR A 1 328 ? 149.809 106.310 127.628 1.00 66.03  ? 326 THR A OG1 1 
ATOM   2037 C  CG2 . THR A 1 328 ? 148.226 107.360 126.144 1.00 59.20  ? 326 THR A CG2 1 
ATOM   2038 N  N   . ALA A 1 329 ? 150.919 108.895 124.192 1.00 64.42  ? 327 ALA A N   1 
ATOM   2039 C  CA  . ALA A 1 329 ? 150.676 109.855 123.120 1.00 62.66  ? 327 ALA A CA  1 
ATOM   2040 C  C   . ALA A 1 329 ? 151.092 109.289 121.771 1.00 64.66  ? 327 ALA A C   1 
ATOM   2041 O  O   . ALA A 1 329 ? 150.401 109.486 120.765 1.00 66.72  ? 327 ALA A O   1 
ATOM   2042 C  CB  . ALA A 1 329 ? 151.426 111.154 123.409 1.00 67.47  ? 327 ALA A CB  1 
ATOM   2043 N  N   . LEU A 1 330 ? 152.223 108.587 121.729 1.00 60.58  ? 328 LEU A N   1 
ATOM   2044 C  CA  . LEU A 1 330 ? 152.658 107.934 120.500 1.00 60.08  ? 328 LEU A CA  1 
ATOM   2045 C  C   . LEU A 1 330 ? 151.595 106.975 119.979 1.00 62.69  ? 328 LEU A C   1 
ATOM   2046 O  O   . LEU A 1 330 ? 151.148 107.083 118.833 1.00 61.62  ? 328 LEU A O   1 
ATOM   2047 C  CB  . LEU A 1 330 ? 153.976 107.194 120.734 1.00 59.50  ? 328 LEU A CB  1 
ATOM   2048 C  CG  . LEU A 1 330 ? 155.254 107.988 120.470 1.00 60.26  ? 328 LEU A CG  1 
ATOM   2049 C  CD1 . LEU A 1 330 ? 156.423 107.359 121.203 1.00 56.89  ? 328 LEU A CD1 1 
ATOM   2050 C  CD2 . LEU A 1 330 ? 155.532 108.065 118.981 1.00 64.41  ? 328 LEU A CD2 1 
ATOM   2051 N  N   . MET A 1 331 ? 151.163 106.034 120.822 1.00 63.58  ? 329 MET A N   1 
ATOM   2052 C  CA  . MET A 1 331 ? 150.254 104.987 120.362 1.00 64.30  ? 329 MET A CA  1 
ATOM   2053 C  C   . MET A 1 331 ? 148.947 105.556 119.817 1.00 61.53  ? 329 MET A C   1 
ATOM   2054 O  O   . MET A 1 331 ? 148.475 105.122 118.760 1.00 66.10  ? 329 MET A O   1 
ATOM   2055 C  CB  . MET A 1 331 ? 149.967 104.021 121.512 1.00 58.79  ? 329 MET A CB  1 
ATOM   2056 C  CG  . MET A 1 331 ? 150.907 102.834 121.574 1.00 64.57  ? 329 MET A CG  1 
ATOM   2057 S  SD  . MET A 1 331 ? 152.516 103.235 122.283 1.00 78.74  ? 329 MET A SD  1 
ATOM   2058 C  CE  . MET A 1 331 ? 153.562 103.133 120.833 1.00 63.44  ? 329 MET A CE  1 
ATOM   2059 N  N   . ILE A 1 332 ? 148.344 106.520 120.514 1.00 49.28  ? 330 ILE A N   1 
ATOM   2060 C  CA  . ILE A 1 332 ? 147.038 107.018 120.086 1.00 49.72  ? 330 ILE A CA  1 
ATOM   2061 C  C   . ILE A 1 332 ? 147.126 108.268 119.220 1.00 62.07  ? 330 ILE A C   1 
ATOM   2062 O  O   . ILE A 1 332 ? 146.221 108.509 118.408 1.00 59.58  ? 330 ILE A O   1 
ATOM   2063 C  CB  . ILE A 1 332 ? 146.115 107.327 121.280 1.00 52.17  ? 330 ILE A CB  1 
ATOM   2064 C  CG1 . ILE A 1 332 ? 146.742 108.417 122.167 1.00 59.05  ? 330 ILE A CG1 1 
ATOM   2065 C  CG2 . ILE A 1 332 ? 145.811 106.070 122.082 1.00 55.22  ? 330 ILE A CG2 1 
ATOM   2066 C  CD1 . ILE A 1 332 ? 145.852 108.930 123.212 1.00 53.13  ? 330 ILE A CD1 1 
ATOM   2067 N  N   . SER A 1 333 ? 148.191 109.053 119.343 1.00 62.98  ? 331 SER A N   1 
ATOM   2068 C  CA  . SER A 1 333 ? 148.401 110.205 118.472 1.00 59.07  ? 331 SER A CA  1 
ATOM   2069 C  C   . SER A 1 333 ? 147.293 111.247 118.649 1.00 56.59  ? 331 SER A C   1 
ATOM   2070 O  O   . SER A 1 333 ? 146.750 111.777 117.679 1.00 51.19  ? 331 SER A O   1 
ATOM   2071 C  CB  . SER A 1 333 ? 148.504 109.758 117.014 1.00 62.74  ? 331 SER A CB  1 
ATOM   2072 O  OG  . SER A 1 333 ? 149.647 108.957 116.808 1.00 67.67  ? 331 SER A OG  1 
ATOM   2073 N  N   . SER A 1 334 ? 146.958 111.544 119.906 1.00 60.16  ? 332 SER A N   1 
ATOM   2074 C  CA  . SER A 1 334 ? 145.959 112.567 120.210 1.00 60.38  ? 332 SER A CA  1 
ATOM   2075 C  C   . SER A 1 334 ? 146.290 113.198 121.554 1.00 55.43  ? 332 SER A C   1 
ATOM   2076 O  O   . SER A 1 334 ? 146.289 112.512 122.579 1.00 51.61  ? 332 SER A O   1 
ATOM   2077 C  CB  . SER A 1 334 ? 144.552 111.968 120.232 1.00 56.23  ? 332 SER A CB  1 
ATOM   2078 O  OG  . SER A 1 334 ? 143.569 112.984 120.317 1.00 61.51  ? 332 SER A OG  1 
ATOM   2079 N  N   . SER A 1 335 ? 146.570 114.505 121.540 1.00 55.52  ? 333 SER A N   1 
ATOM   2080 C  CA  . SER A 1 335 ? 146.907 115.220 122.770 1.00 59.32  ? 333 SER A CA  1 
ATOM   2081 C  C   . SER A 1 335 ? 145.749 115.265 123.764 1.00 63.56  ? 333 SER A C   1 
ATOM   2082 O  O   . SER A 1 335 ? 145.950 115.058 124.966 1.00 64.69  ? 333 SER A O   1 
ATOM   2083 C  CB  . SER A 1 335 ? 147.357 116.641 122.432 1.00 61.69  ? 333 SER A CB  1 
ATOM   2084 O  OG  . SER A 1 335 ? 148.520 116.628 121.627 1.00 64.67  ? 333 SER A OG  1 
ATOM   2085 N  N   . SER A 1 336 ? 144.529 115.529 123.286 1.00 56.76  ? 334 SER A N   1 
ATOM   2086 C  CA  . SER A 1 336 ? 143.389 115.619 124.197 1.00 58.19  ? 334 SER A CA  1 
ATOM   2087 C  C   . SER A 1 336 ? 143.075 114.277 124.842 1.00 60.57  ? 334 SER A C   1 
ATOM   2088 O  O   . SER A 1 336 ? 142.808 114.207 126.048 1.00 58.68  ? 334 SER A O   1 
ATOM   2089 C  CB  . SER A 1 336 ? 142.165 116.141 123.446 1.00 59.33  ? 334 SER A CB  1 
ATOM   2090 O  OG  . SER A 1 336 ? 142.423 117.403 122.859 1.00 54.55  ? 334 SER A OG  1 
ATOM   2091 N  N   . ALA A 1 337 ? 143.104 113.204 124.056 1.00 53.64  ? 335 ALA A N   1 
ATOM   2092 C  CA  . ALA A 1 337 ? 142.787 111.883 124.581 1.00 52.31  ? 335 ALA A CA  1 
ATOM   2093 C  C   . ALA A 1 337 ? 143.778 111.443 125.649 1.00 57.90  ? 335 ALA A C   1 
ATOM   2094 O  O   . ALA A 1 337 ? 143.410 110.702 126.567 1.00 60.11  ? 335 ALA A O   1 
ATOM   2095 C  CB  . ALA A 1 337 ? 142.753 110.882 123.438 1.00 53.55  ? 335 ALA A CB  1 
ATOM   2096 N  N   . THR A 1 338 ? 145.031 111.873 125.545 1.00 63.75  ? 336 THR A N   1 
ATOM   2097 C  CA  . THR A 1 338 ? 146.046 111.544 126.536 1.00 60.83  ? 336 THR A CA  1 
ATOM   2098 C  C   . THR A 1 338 ? 146.146 112.597 127.629 1.00 55.35  ? 336 THR A C   1 
ATOM   2099 O  O   . THR A 1 338 ? 146.989 112.466 128.521 1.00 59.28  ? 336 THR A O   1 
ATOM   2100 C  CB  . THR A 1 338 ? 147.412 111.367 125.859 1.00 63.34  ? 336 THR A CB  1 
ATOM   2101 O  OG1 . THR A 1 338 ? 148.373 110.906 126.818 1.00 63.81  ? 336 THR A OG1 1 
ATOM   2102 C  CG2 . THR A 1 338 ? 147.899 112.678 125.267 1.00 63.66  ? 336 THR A CG2 1 
ATOM   2103 N  N   . LEU A 1 339 ? 145.312 113.634 127.575 1.00 54.11  ? 337 LEU A N   1 
ATOM   2104 C  CA  . LEU A 1 339 ? 145.312 114.630 128.641 1.00 59.68  ? 337 LEU A CA  1 
ATOM   2105 C  C   . LEU A 1 339 ? 145.067 114.004 130.007 1.00 60.26  ? 337 LEU A C   1 
ATOM   2106 O  O   . LEU A 1 339 ? 145.768 114.383 130.961 1.00 58.08  ? 337 LEU A O   1 
ATOM   2107 C  CB  . LEU A 1 339 ? 144.267 115.710 128.336 1.00 56.82  ? 337 LEU A CB  1 
ATOM   2108 C  CG  . LEU A 1 339 ? 144.315 116.956 129.218 1.00 59.90  ? 337 LEU A CG  1 
ATOM   2109 C  CD1 . LEU A 1 339 ? 145.308 117.959 128.664 1.00 61.43  ? 337 LEU A CD1 1 
ATOM   2110 C  CD2 . LEU A 1 339 ? 142.935 117.579 129.343 1.00 55.52  ? 337 LEU A CD2 1 
ATOM   2111 N  N   . PRO A 1 340 ? 144.124 113.072 130.181 1.00 55.53  ? 338 PRO A N   1 
ATOM   2112 C  CA  . PRO A 1 340 ? 143.994 112.428 131.498 1.00 54.44  ? 338 PRO A CA  1 
ATOM   2113 C  C   . PRO A 1 340 ? 145.278 111.762 131.953 1.00 58.70  ? 338 PRO A C   1 
ATOM   2114 O  O   . PRO A 1 340 ? 145.587 111.768 133.151 1.00 61.07  ? 338 PRO A O   1 
ATOM   2115 C  CB  . PRO A 1 340 ? 142.868 111.409 131.275 1.00 56.38  ? 338 PRO A CB  1 
ATOM   2116 C  CG  . PRO A 1 340 ? 142.083 111.953 130.145 1.00 54.32  ? 338 PRO A CG  1 
ATOM   2117 C  CD  . PRO A 1 340 ? 143.073 112.630 129.249 1.00 56.45  ? 338 PRO A CD  1 
ATOM   2118 N  N   . VAL A 1 341 ? 146.037 111.180 131.024 1.00 59.71  ? 339 VAL A N   1 
ATOM   2119 C  CA  . VAL A 1 341 ? 147.304 110.556 131.390 1.00 62.11  ? 339 VAL A CA  1 
ATOM   2120 C  C   . VAL A 1 341 ? 148.322 111.620 131.775 1.00 63.93  ? 339 VAL A C   1 
ATOM   2121 O  O   . VAL A 1 341 ? 149.103 111.440 132.718 1.00 63.09  ? 339 VAL A O   1 
ATOM   2122 C  CB  . VAL A 1 341 ? 147.819 109.668 130.243 1.00 65.74  ? 339 VAL A CB  1 
ATOM   2123 C  CG1 . VAL A 1 341 ? 149.041 108.880 130.690 1.00 62.31  ? 339 VAL A CG1 1 
ATOM   2124 C  CG2 . VAL A 1 341 ? 146.727 108.723 129.762 1.00 70.67  ? 339 VAL A CG2 1 
ATOM   2125 N  N   . THR A 1 342 ? 148.337 112.743 131.052 1.00 66.12  ? 340 THR A N   1 
ATOM   2126 C  CA  . THR A 1 342 ? 149.288 113.803 131.364 1.00 69.21  ? 340 THR A CA  1 
ATOM   2127 C  C   . THR A 1 342 ? 149.062 114.335 132.772 1.00 65.90  ? 340 THR A C   1 
ATOM   2128 O  O   . THR A 1 342 ? 150.021 114.556 133.522 1.00 61.69  ? 340 THR A O   1 
ATOM   2129 C  CB  . THR A 1 342 ? 149.175 114.933 130.342 1.00 66.07  ? 340 THR A CB  1 
ATOM   2130 O  OG1 . THR A 1 342 ? 149.011 114.382 129.030 1.00 64.81  ? 340 THR A OG1 1 
ATOM   2131 C  CG2 . THR A 1 342 ? 150.423 115.799 130.367 1.00 62.37  ? 340 THR A CG2 1 
ATOM   2132 N  N   . PHE A 1 343 ? 147.800 114.556 133.149 1.00 58.66  ? 341 PHE A N   1 
ATOM   2133 C  CA  . PHE A 1 343 ? 147.509 115.054 134.488 1.00 58.10  ? 341 PHE A CA  1 
ATOM   2134 C  C   . PHE A 1 343 ? 148.149 114.159 135.539 1.00 63.09  ? 341 PHE A C   1 
ATOM   2135 O  O   . PHE A 1 343 ? 148.908 114.625 136.396 1.00 63.96  ? 341 PHE A O   1 
ATOM   2136 C  CB  . PHE A 1 343 ? 145.996 115.126 134.712 1.00 53.45  ? 341 PHE A CB  1 
ATOM   2137 C  CG  . PHE A 1 343 ? 145.315 116.240 133.971 1.00 51.75  ? 341 PHE A CG  1 
ATOM   2138 C  CD1 . PHE A 1 343 ? 145.769 117.541 134.068 1.00 57.03  ? 341 PHE A CD1 1 
ATOM   2139 C  CD2 . PHE A 1 343 ? 144.188 115.988 133.210 1.00 60.13  ? 341 PHE A CD2 1 
ATOM   2140 C  CE1 . PHE A 1 343 ? 145.129 118.563 133.399 1.00 59.73  ? 341 PHE A CE1 1 
ATOM   2141 C  CE2 . PHE A 1 343 ? 143.544 117.007 132.543 1.00 57.15  ? 341 PHE A CE2 1 
ATOM   2142 C  CZ  . PHE A 1 343 ? 144.015 118.295 132.635 1.00 57.84  ? 341 PHE A CZ  1 
ATOM   2143 N  N   . ARG A 1 344 ? 147.833 112.867 135.481 1.00 65.28  ? 342 ARG A N   1 
ATOM   2144 C  CA  . ARG A 1 344 ? 148.353 111.933 136.512 1.00 65.15  ? 342 ARG A CA  1 
ATOM   2145 C  C   . ARG A 1 344 ? 149.882 111.970 136.513 1.00 66.79  ? 342 ARG A C   1 
ATOM   2146 O  O   . ARG A 1 344 ? 150.456 112.225 137.574 1.00 68.54  ? 342 ARG A O   1 
ATOM   2147 C  CB  . ARG A 1 344 ? 147.840 110.517 136.238 1.00 64.18  ? 342 ARG A CB  1 
ATOM   2148 C  CG  . ARG A 1 344 ? 146.345 110.354 136.468 1.00 69.35  ? 342 ARG A CG  1 
ATOM   2149 C  CD  . ARG A 1 344 ? 145.898 108.906 136.503 1.00 69.44  ? 342 ARG A CD  1 
ATOM   2150 N  NE  . ARG A 1 344 ? 146.121 108.216 135.241 1.00 69.24  ? 342 ARG A NE  1 
ATOM   2151 C  CZ  . ARG A 1 344 ? 145.270 108.223 134.222 1.00 69.55  ? 342 ARG A CZ  1 
ATOM   2152 N  NH1 . ARG A 1 344 ? 144.031 108.644 134.399 1.00 69.98  ? 342 ARG A NH1 1 
ATOM   2153 N  NH2 . ARG A 1 344 ? 145.660 107.809 133.029 1.00 65.34  ? 342 ARG A NH2 1 
ATOM   2154 N  N   . CYS A 1 345 ? 150.516 111.783 135.357 1.00 69.01  ? 343 CYS A N   1 
ATOM   2155 C  CA  . CYS A 1 345 ? 151.970 111.679 135.327 1.00 66.67  ? 343 CYS A CA  1 
ATOM   2156 C  C   . CYS A 1 345 ? 152.628 112.930 135.891 1.00 68.17  ? 343 CYS A C   1 
ATOM   2157 O  O   . CYS A 1 345 ? 153.567 112.845 136.691 1.00 70.37  ? 343 CYS A O   1 
ATOM   2158 C  CB  . CYS A 1 345 ? 152.447 111.410 133.903 1.00 65.91  ? 343 CYS A CB  1 
ATOM   2159 S  SG  . CYS A 1 345 ? 152.520 109.666 133.495 1.00 71.84  ? 343 CYS A SG  1 
ATOM   2160 N  N   . ALA A 1 346 ? 152.150 114.106 135.486 1.00 66.32  ? 344 ALA A N   1 
ATOM   2161 C  CA  . ALA A 1 346 ? 152.764 115.343 135.950 1.00 63.97  ? 344 ALA A CA  1 
ATOM   2162 C  C   . ALA A 1 346 ? 152.557 115.502 137.449 1.00 66.87  ? 344 ALA A C   1 
ATOM   2163 O  O   . ALA A 1 346 ? 153.503 115.766 138.199 1.00 65.91  ? 344 ALA A O   1 
ATOM   2164 C  CB  . ALA A 1 346 ? 152.188 116.539 135.191 1.00 62.51  ? 344 ALA A CB  1 
ATOM   2165 N  N   . GLU A 1 347 ? 151.316 115.334 137.898 1.00 67.54  ? 345 GLU A N   1 
ATOM   2166 C  CA  . GLU A 1 347 ? 150.938 115.591 139.278 1.00 65.73  ? 345 GLU A CA  1 
ATOM   2167 C  C   . GLU A 1 347 ? 151.385 114.491 140.232 1.00 67.86  ? 345 GLU A C   1 
ATOM   2168 O  O   . GLU A 1 347 ? 151.463 114.738 141.441 1.00 71.15  ? 345 GLU A O   1 
ATOM   2169 C  CB  . GLU A 1 347 ? 149.423 115.756 139.343 1.00 62.46  ? 345 GLU A CB  1 
ATOM   2170 C  CG  . GLU A 1 347 ? 148.950 116.995 138.620 1.00 66.20  ? 345 GLU A CG  1 
ATOM   2171 C  CD  . GLU A 1 347 ? 147.450 117.086 138.546 1.00 68.77  ? 345 GLU A CD  1 
ATOM   2172 O  OE1 . GLU A 1 347 ? 146.869 116.545 137.584 1.00 66.37  ? 345 GLU A OE1 1 
ATOM   2173 O  OE2 . GLU A 1 347 ? 146.850 117.700 139.444 1.00 67.13  ? 345 GLU A OE2 1 
ATOM   2174 N  N   . GLU A 1 348 ? 151.676 113.292 139.727 1.00 72.80  ? 346 GLU A N   1 
ATOM   2175 C  CA  . GLU A 1 348 ? 152.051 112.154 140.561 1.00 73.26  ? 346 GLU A CA  1 
ATOM   2176 C  C   . GLU A 1 348 ? 153.523 111.789 140.428 1.00 72.62  ? 346 GLU A C   1 
ATOM   2177 O  O   . GLU A 1 348 ? 154.221 111.686 141.441 1.00 70.87  ? 346 GLU A O   1 
ATOM   2178 C  CB  . GLU A 1 348 ? 151.166 110.942 140.225 1.00 71.91  ? 346 GLU A CB  1 
ATOM   2179 C  CG  . GLU A 1 348 ? 149.672 111.248 140.259 1.00 74.69  ? 346 GLU A CG  1 
ATOM   2180 C  CD  . GLU A 1 348 ? 148.865 110.170 140.955 1.00 76.44  ? 346 GLU A CD  1 
ATOM   2181 O  OE1 . GLU A 1 348 ? 148.554 110.339 142.153 1.00 77.37  ? 346 GLU A OE1 1 
ATOM   2182 O  OE2 . GLU A 1 348 ? 148.537 109.156 140.306 1.00 75.45  ? 346 GLU A OE2 1 
ATOM   2183 N  N   . ASN A 1 349 ? 154.027 111.592 139.206 1.00 73.15  ? 347 ASN A N   1 
ATOM   2184 C  CA  . ASN A 1 349 ? 155.426 111.197 139.057 1.00 76.67  ? 347 ASN A CA  1 
ATOM   2185 C  C   . ASN A 1 349 ? 156.359 112.374 139.309 1.00 75.08  ? 347 ASN A C   1 
ATOM   2186 O  O   . ASN A 1 349 ? 157.455 112.193 139.850 1.00 75.07  ? 347 ASN A O   1 
ATOM   2187 C  CB  . ASN A 1 349 ? 155.703 110.589 137.678 1.00 70.09  ? 347 ASN A CB  1 
ATOM   2188 C  CG  . ASN A 1 349 ? 154.659 109.580 137.257 1.00 72.95  ? 347 ASN A CG  1 
ATOM   2189 O  OD1 . ASN A 1 349 ? 153.985 109.756 136.248 1.00 76.33  ? 347 ASN A OD1 1 
ATOM   2190 N  ND2 . ASN A 1 349 ? 154.533 108.503 138.022 1.00 70.22  ? 347 ASN A ND2 1 
ATOM   2191 N  N   . ASN A 1 350 ? 155.950 113.581 138.920 1.00 71.53  ? 348 ASN A N   1 
ATOM   2192 C  CA  . ASN A 1 350 ? 156.779 114.770 139.059 1.00 70.69  ? 348 ASN A CA  1 
ATOM   2193 C  C   . ASN A 1 350 ? 156.333 115.667 140.204 1.00 69.93  ? 348 ASN A C   1 
ATOM   2194 O  O   . ASN A 1 350 ? 156.961 116.704 140.440 1.00 68.50  ? 348 ASN A O   1 
ATOM   2195 C  CB  . ASN A 1 350 ? 156.779 115.569 137.751 1.00 69.56  ? 348 ASN A CB  1 
ATOM   2196 C  CG  . ASN A 1 350 ? 157.105 114.713 136.549 1.00 68.90  ? 348 ASN A CG  1 
ATOM   2197 O  OD1 . ASN A 1 350 ? 156.307 114.596 135.621 1.00 70.17  ? 348 ASN A OD1 1 
ATOM   2198 N  ND2 . ASN A 1 350 ? 158.283 114.103 136.562 1.00 69.60  ? 348 ASN A ND2 1 
ATOM   2199 N  N   . GLN A 1 351 ? 155.278 115.292 140.924 1.00 72.06  ? 349 GLN A N   1 
ATOM   2200 C  CA  . GLN A 1 351 ? 154.808 116.026 142.096 1.00 73.67  ? 349 GLN A CA  1 
ATOM   2201 C  C   . GLN A 1 351 ? 154.685 117.521 141.803 1.00 72.48  ? 349 GLN A C   1 
ATOM   2202 O  O   . GLN A 1 351 ? 155.272 118.370 142.476 1.00 74.89  ? 349 GLN A O   1 
ATOM   2203 C  CB  . GLN A 1 351 ? 155.741 115.774 143.282 1.00 73.36  ? 349 GLN A CB  1 
ATOM   2204 C  CG  . GLN A 1 351 ? 155.935 114.301 143.607 1.00 74.22  ? 349 GLN A CG  1 
ATOM   2205 C  CD  . GLN A 1 351 ? 156.756 114.084 144.861 1.00 72.87  ? 349 GLN A CD  1 
ATOM   2206 O  OE1 . GLN A 1 351 ? 157.914 114.495 144.936 1.00 71.92  ? 349 GLN A OE1 1 
ATOM   2207 N  NE2 . GLN A 1 351 ? 156.162 113.431 145.853 1.00 73.10  ? 349 GLN A NE2 1 
ATOM   2208 N  N   . VAL A 1 352 ? 153.902 117.830 140.777 1.00 66.99  ? 350 VAL A N   1 
ATOM   2209 C  CA  . VAL A 1 352 ? 153.657 119.203 140.376 1.00 64.12  ? 350 VAL A CA  1 
ATOM   2210 C  C   . VAL A 1 352 ? 152.336 119.662 140.981 1.00 67.59  ? 350 VAL A C   1 
ATOM   2211 O  O   . VAL A 1 352 ? 151.450 118.865 141.300 1.00 68.41  ? 350 VAL A O   1 
ATOM   2212 C  CB  . VAL A 1 352 ? 153.655 119.353 138.837 1.00 61.03  ? 350 VAL A CB  1 
ATOM   2213 C  CG1 . VAL A 1 352 ? 153.601 120.811 138.443 1.00 60.32  ? 350 VAL A CG1 1 
ATOM   2214 C  CG2 . VAL A 1 352 ? 154.884 118.696 138.237 1.00 64.62  ? 350 VAL A CG2 1 
ATOM   2215 N  N   . ASP A 1 353 ? 152.206 120.976 141.146 1.00 68.64  ? 351 ASP A N   1 
ATOM   2216 C  CA  . ASP A 1 353 ? 151.003 121.554 141.727 1.00 61.45  ? 351 ASP A CA  1 
ATOM   2217 C  C   . ASP A 1 353 ? 149.776 121.261 140.871 1.00 60.99  ? 351 ASP A C   1 
ATOM   2218 O  O   . ASP A 1 353 ? 149.811 121.373 139.643 1.00 59.48  ? 351 ASP A O   1 
ATOM   2219 C  CB  . ASP A 1 353 ? 151.176 123.064 141.890 1.00 64.61  ? 351 ASP A CB  1 
ATOM   2220 C  CG  . ASP A 1 353 ? 150.304 123.635 142.987 1.00 66.74  ? 351 ASP A CG  1 
ATOM   2221 O  OD1 . ASP A 1 353 ? 149.078 123.742 142.778 1.00 67.21  ? 351 ASP A OD1 1 
ATOM   2222 O  OD2 . ASP A 1 353 ? 150.847 123.978 144.058 1.00 65.32  ? 351 ASP A OD2 1 
ATOM   2223 N  N   . LYS A 1 354 ? 148.683 120.879 141.536 1.00 69.08  ? 352 LYS A N   1 
ATOM   2224 C  CA  . LYS A 1 354 ? 147.443 120.582 140.825 1.00 69.61  ? 352 LYS A CA  1 
ATOM   2225 C  C   . LYS A 1 354 ? 146.889 121.824 140.143 1.00 66.67  ? 352 LYS A C   1 
ATOM   2226 O  O   . LYS A 1 354 ? 146.339 121.746 139.039 1.00 67.37  ? 352 LYS A O   1 
ATOM   2227 C  CB  . LYS A 1 354 ? 146.407 120.025 141.805 1.00 70.60  ? 352 LYS A CB  1 
ATOM   2228 C  CG  . LYS A 1 354 ? 145.198 119.358 141.154 1.00 70.86  ? 352 LYS A CG  1 
ATOM   2229 C  CD  . LYS A 1 354 ? 144.015 119.263 142.106 1.00 71.77  ? 352 LYS A CD  1 
ATOM   2230 C  CE  . LYS A 1 354 ? 142.749 119.805 141.463 1.00 68.70  ? 352 LYS A CE  1 
ATOM   2231 N  NZ  . LYS A 1 354 ? 142.775 121.287 141.338 1.00 63.83  ? 352 LYS A NZ  1 
ATOM   2232 N  N   . ARG A 1 355 ? 147.021 122.981 140.792 1.00 59.98  ? 353 ARG A N   1 
ATOM   2233 C  CA  . ARG A 1 355 ? 146.474 124.215 140.240 1.00 61.35  ? 353 ARG A CA  1 
ATOM   2234 C  C   . ARG A 1 355 ? 147.142 124.593 138.923 1.00 67.07  ? 353 ARG A C   1 
ATOM   2235 O  O   . ARG A 1 355 ? 146.468 125.027 137.981 1.00 61.44  ? 353 ARG A O   1 
ATOM   2236 C  CB  . ARG A 1 355 ? 146.618 125.335 141.268 1.00 62.04  ? 353 ARG A CB  1 
ATOM   2237 C  CG  . ARG A 1 355 ? 145.991 124.990 142.614 1.00 67.92  ? 353 ARG A CG  1 
ATOM   2238 C  CD  . ARG A 1 355 ? 146.262 126.051 143.658 1.00 65.41  ? 353 ARG A CD  1 
ATOM   2239 N  NE  . ARG A 1 355 ? 147.631 125.985 144.159 1.00 66.18  ? 353 ARG A NE  1 
ATOM   2240 C  CZ  . ARG A 1 355 ? 147.971 125.842 145.434 1.00 68.49  ? 353 ARG A CZ  1 
ATOM   2241 N  NH1 . ARG A 1 355 ? 147.063 125.750 146.393 1.00 68.41  ? 353 ARG A NH1 1 
ATOM   2242 N  NH2 . ARG A 1 355 ? 149.260 125.789 145.758 1.00 66.42  ? 353 ARG A NH2 1 
ATOM   2243 N  N   . ILE A 1 356 ? 148.464 124.441 138.834 1.00 69.22  ? 354 ILE A N   1 
ATOM   2244 C  CA  . ILE A 1 356 ? 149.156 124.737 137.583 1.00 57.29  ? 354 ILE A CA  1 
ATOM   2245 C  C   . ILE A 1 356 ? 148.827 123.695 136.523 1.00 58.71  ? 354 ILE A C   1 
ATOM   2246 O  O   . ILE A 1 356 ? 148.577 124.031 135.360 1.00 61.37  ? 354 ILE A O   1 
ATOM   2247 C  CB  . ILE A 1 356 ? 150.674 124.836 137.820 1.00 56.78  ? 354 ILE A CB  1 
ATOM   2248 C  CG1 . ILE A 1 356 ? 150.988 125.872 138.905 1.00 59.16  ? 354 ILE A CG1 1 
ATOM   2249 C  CG2 . ILE A 1 356 ? 151.401 125.157 136.517 1.00 63.95  ? 354 ILE A CG2 1 
ATOM   2250 C  CD1 . ILE A 1 356 ? 150.780 127.313 138.483 1.00 63.68  ? 354 ILE A CD1 1 
ATOM   2251 N  N   . THR A 1 357 ? 148.826 122.415 136.899 1.00 64.14  ? 355 THR A N   1 
ATOM   2252 C  CA  . THR A 1 357 ? 148.600 121.362 135.915 1.00 59.52  ? 355 THR A CA  1 
ATOM   2253 C  C   . THR A 1 357 ? 147.211 121.464 135.300 1.00 56.17  ? 355 THR A C   1 
ATOM   2254 O  O   . THR A 1 357 ? 147.045 121.275 134.090 1.00 54.46  ? 355 THR A O   1 
ATOM   2255 C  CB  . THR A 1 357 ? 148.801 119.990 136.553 1.00 57.60  ? 355 THR A CB  1 
ATOM   2256 O  OG1 . THR A 1 357 ? 149.926 120.030 137.439 1.00 60.20  ? 355 THR A OG1 1 
ATOM   2257 C  CG2 . THR A 1 357 ? 149.043 118.948 135.481 1.00 59.68  ? 355 THR A CG2 1 
ATOM   2258 N  N   . ARG A 1 358 ? 146.199 121.765 136.115 1.00 60.99  ? 356 ARG A N   1 
ATOM   2259 C  CA  . ARG A 1 358 ? 144.827 121.807 135.625 1.00 60.16  ? 356 ARG A CA  1 
ATOM   2260 C  C   . ARG A 1 358 ? 144.545 123.019 134.751 1.00 60.58  ? 356 ARG A C   1 
ATOM   2261 O  O   . ARG A 1 358 ? 143.455 123.098 134.175 1.00 54.61  ? 356 ARG A O   1 
ATOM   2262 C  CB  . ARG A 1 358 ? 143.851 121.784 136.802 1.00 60.66  ? 356 ARG A CB  1 
ATOM   2263 C  CG  . ARG A 1 358 ? 143.659 120.411 137.426 1.00 58.95  ? 356 ARG A CG  1 
ATOM   2264 C  CD  . ARG A 1 358 ? 142.879 119.491 136.496 1.00 60.39  ? 356 ARG A CD  1 
ATOM   2265 N  NE  . ARG A 1 358 ? 142.597 118.194 137.100 1.00 66.05  ? 356 ARG A NE  1 
ATOM   2266 C  CZ  . ARG A 1 358 ? 143.506 117.256 137.325 1.00 65.08  ? 356 ARG A CZ  1 
ATOM   2267 N  NH1 . ARG A 1 358 ? 144.777 117.433 137.004 1.00 67.13  ? 356 ARG A NH1 1 
ATOM   2268 N  NH2 . ARG A 1 358 ? 143.131 116.110 137.885 1.00 60.49  ? 356 ARG A NH2 1 
ATOM   2269 N  N   . PHE A 1 359 ? 145.481 123.959 134.640 1.00 60.76  ? 357 PHE A N   1 
ATOM   2270 C  CA  . PHE A 1 359 ? 145.340 125.103 133.750 1.00 55.74  ? 357 PHE A CA  1 
ATOM   2271 C  C   . PHE A 1 359 ? 146.287 125.032 132.563 1.00 53.54  ? 357 PHE A C   1 
ATOM   2272 O  O   . PHE A 1 359 ? 145.847 125.159 131.420 1.00 53.68  ? 357 PHE A O   1 
ATOM   2273 C  CB  . PHE A 1 359 ? 145.585 126.410 134.521 1.00 54.02  ? 357 PHE A CB  1 
ATOM   2274 C  CG  . PHE A 1 359 ? 145.526 127.650 133.662 1.00 56.23  ? 357 PHE A CG  1 
ATOM   2275 C  CD1 . PHE A 1 359 ? 144.808 127.670 132.477 1.00 55.04  ? 357 PHE A CD1 1 
ATOM   2276 C  CD2 . PHE A 1 359 ? 146.195 128.798 134.045 1.00 57.61  ? 357 PHE A CD2 1 
ATOM   2277 C  CE1 . PHE A 1 359 ? 144.760 128.807 131.696 1.00 55.26  ? 357 PHE A CE1 1 
ATOM   2278 C  CE2 . PHE A 1 359 ? 146.149 129.938 133.268 1.00 58.10  ? 357 PHE A CE2 1 
ATOM   2279 C  CZ  . PHE A 1 359 ? 145.431 129.941 132.092 1.00 53.43  ? 357 PHE A CZ  1 
ATOM   2280 N  N   . VAL A 1 360 ? 147.579 124.806 132.806 1.00 58.95  ? 358 VAL A N   1 
ATOM   2281 C  CA  . VAL A 1 360 ? 148.561 124.837 131.725 1.00 57.38  ? 358 VAL A CA  1 
ATOM   2282 C  C   . VAL A 1 360 ? 148.274 123.743 130.704 1.00 58.49  ? 358 VAL A C   1 
ATOM   2283 O  O   . VAL A 1 360 ? 148.349 123.972 129.491 1.00 59.49  ? 358 VAL A O   1 
ATOM   2284 C  CB  . VAL A 1 360 ? 149.985 124.719 132.302 1.00 54.94  ? 358 VAL A CB  1 
ATOM   2285 C  CG1 . VAL A 1 360 ? 150.999 124.387 131.211 1.00 56.98  ? 358 VAL A CG1 1 
ATOM   2286 C  CG2 . VAL A 1 360 ? 150.371 126.001 133.017 1.00 57.33  ? 358 VAL A CG2 1 
ATOM   2287 N  N   . LEU A 1 361 ? 147.943 122.534 131.175 1.00 58.59  ? 359 LEU A N   1 
ATOM   2288 C  CA  . LEU A 1 361 ? 147.792 121.412 130.247 1.00 58.96  ? 359 LEU A CA  1 
ATOM   2289 C  C   . LEU A 1 361 ? 146.575 121.584 129.349 1.00 64.21  ? 359 LEU A C   1 
ATOM   2290 O  O   . LEU A 1 361 ? 146.734 121.599 128.116 1.00 60.04  ? 359 LEU A O   1 
ATOM   2291 C  CB  . LEU A 1 361 ? 147.750 120.094 131.023 1.00 54.71  ? 359 LEU A CB  1 
ATOM   2292 C  CG  . LEU A 1 361 ? 149.050 119.603 131.673 1.00 61.63  ? 359 LEU A CG  1 
ATOM   2293 C  CD1 . LEU A 1 361 ? 148.860 118.197 132.209 1.00 62.98  ? 359 LEU A CD1 1 
ATOM   2294 C  CD2 . LEU A 1 361 ? 150.233 119.640 130.717 1.00 63.30  ? 359 LEU A CD2 1 
ATOM   2295 N  N   . PRO A 1 362 ? 145.350 121.712 129.873 1.00 66.68  ? 360 PRO A N   1 
ATOM   2296 C  CA  . PRO A 1 362 ? 144.180 121.771 128.977 1.00 58.97  ? 360 PRO A CA  1 
ATOM   2297 C  C   . PRO A 1 362 ? 144.309 122.797 127.864 1.00 51.65  ? 360 PRO A C   1 
ATOM   2298 O  O   . PRO A 1 362 ? 144.039 122.478 126.700 1.00 50.38  ? 360 PRO A O   1 
ATOM   2299 C  CB  . PRO A 1 362 ? 143.027 122.106 129.938 1.00 61.32  ? 360 PRO A CB  1 
ATOM   2300 C  CG  . PRO A 1 362 ? 143.682 122.502 131.233 1.00 57.26  ? 360 PRO A CG  1 
ATOM   2301 C  CD  . PRO A 1 362 ? 144.934 121.710 131.282 1.00 60.70  ? 360 PRO A CD  1 
ATOM   2302 N  N   . VAL A 1 363 ? 144.709 124.028 128.185 1.00 47.14  ? 361 VAL A N   1 
ATOM   2303 C  CA  . VAL A 1 363 ? 144.954 125.008 127.133 1.00 52.40  ? 361 VAL A CA  1 
ATOM   2304 C  C   . VAL A 1 363 ? 146.107 124.546 126.253 1.00 58.98  ? 361 VAL A C   1 
ATOM   2305 O  O   . VAL A 1 363 ? 146.033 124.607 125.022 1.00 62.02  ? 361 VAL A O   1 
ATOM   2306 C  CB  . VAL A 1 363 ? 145.214 126.403 127.738 1.00 57.10  ? 361 VAL A CB  1 
ATOM   2307 C  CG1 . VAL A 1 363 ? 146.416 126.385 128.659 1.00 61.06  ? 361 VAL A CG1 1 
ATOM   2308 C  CG2 . VAL A 1 363 ? 145.410 127.435 126.643 1.00 51.48  ? 361 VAL A CG2 1 
ATOM   2309 N  N   . GLY A 1 364 ? 147.176 124.038 126.868 1.00 60.70  ? 362 GLY A N   1 
ATOM   2310 C  CA  . GLY A 1 364 ? 148.325 123.608 126.094 1.00 58.91  ? 362 GLY A CA  1 
ATOM   2311 C  C   . GLY A 1 364 ? 148.008 122.475 125.140 1.00 62.81  ? 362 GLY A C   1 
ATOM   2312 O  O   . GLY A 1 364 ? 148.617 122.370 124.072 1.00 63.40  ? 362 GLY A O   1 
ATOM   2313 N  N   . ALA A 1 365 ? 147.057 121.614 125.503 1.00 62.71  ? 363 ALA A N   1 
ATOM   2314 C  CA  . ALA A 1 365 ? 146.743 120.464 124.667 1.00 58.73  ? 363 ALA A CA  1 
ATOM   2315 C  C   . ALA A 1 365 ? 146.145 120.853 123.321 1.00 56.89  ? 363 ALA A C   1 
ATOM   2316 O  O   . ALA A 1 365 ? 146.048 119.990 122.442 1.00 58.43  ? 363 ALA A O   1 
ATOM   2317 C  CB  . ALA A 1 365 ? 145.782 119.531 125.403 1.00 56.41  ? 363 ALA A CB  1 
ATOM   2318 N  N   . THR A 1 366 ? 145.745 122.109 123.132 1.00 48.78  ? 364 THR A N   1 
ATOM   2319 C  CA  . THR A 1 366 ? 145.088 122.531 121.900 1.00 51.78  ? 364 THR A CA  1 
ATOM   2320 C  C   . THR A 1 366 ? 145.802 123.679 121.208 1.00 55.52  ? 364 THR A C   1 
ATOM   2321 O  O   . THR A 1 366 ? 145.963 123.647 119.986 1.00 60.86  ? 364 THR A O   1 
ATOM   2322 C  CB  . THR A 1 366 ? 143.636 122.937 122.190 1.00 52.93  ? 364 THR A CB  1 
ATOM   2323 O  OG1 . THR A 1 366 ? 142.939 123.148 120.957 1.00 55.67  ? 364 THR A OG1 1 
ATOM   2324 C  CG2 . THR A 1 366 ? 143.595 124.213 123.014 1.00 51.32  ? 364 THR A CG2 1 
ATOM   2325 N  N   . ILE A 1 367 ? 146.236 124.695 121.952 1.00 59.29  ? 365 ILE A N   1 
ATOM   2326 C  CA  . ILE A 1 367 ? 146.888 125.847 121.334 1.00 60.45  ? 365 ILE A CA  1 
ATOM   2327 C  C   . ILE A 1 367 ? 148.398 125.633 121.268 1.00 63.03  ? 365 ILE A C   1 
ATOM   2328 O  O   . ILE A 1 367 ? 149.049 126.102 120.329 1.00 58.57  ? 365 ILE A O   1 
ATOM   2329 C  CB  . ILE A 1 367 ? 146.540 127.172 122.047 1.00 59.23  ? 365 ILE A CB  1 
ATOM   2330 C  CG1 . ILE A 1 367 ? 145.052 127.502 121.880 1.00 60.37  ? 365 ILE A CG1 1 
ATOM   2331 C  CG2 . ILE A 1 367 ? 147.398 128.319 121.561 1.00 54.36  ? 365 ILE A CG2 1 
ATOM   2332 C  CD1 . ILE A 1 367 ? 144.565 128.639 122.762 1.00 56.27  ? 365 ILE A CD1 1 
ATOM   2333 N  N   . ASN A 1 368 ? 148.968 124.939 122.251 1.00 62.66  ? 366 ASN A N   1 
ATOM   2334 C  CA  . ASN A 1 368 ? 150.403 124.663 122.298 1.00 61.34  ? 366 ASN A CA  1 
ATOM   2335 C  C   . ASN A 1 368 ? 150.656 123.334 121.600 1.00 61.29  ? 366 ASN A C   1 
ATOM   2336 O  O   . ASN A 1 368 ? 150.519 122.267 122.202 1.00 66.69  ? 366 ASN A O   1 
ATOM   2337 C  CB  . ASN A 1 368 ? 150.906 124.623 123.736 1.00 62.01  ? 366 ASN A CB  1 
ATOM   2338 C  CG  . ASN A 1 368 ? 152.416 124.537 123.818 1.00 62.54  ? 366 ASN A CG  1 
ATOM   2339 O  OD1 . ASN A 1 368 ? 153.109 124.649 122.809 1.00 63.25  ? 366 ASN A OD1 1 
ATOM   2340 N  ND2 . ASN A 1 368 ? 152.931 124.309 125.018 1.00 60.56  ? 366 ASN A ND2 1 
ATOM   2341 N  N   . MET A 1 369 ? 151.027 123.397 120.323 1.00 59.43  ? 367 MET A N   1 
ATOM   2342 C  CA  . MET A 1 369 ? 151.372 122.211 119.540 1.00 63.86  ? 367 MET A CA  1 
ATOM   2343 C  C   . MET A 1 369 ? 152.685 122.508 118.822 1.00 63.61  ? 367 MET A C   1 
ATOM   2344 O  O   . MET A 1 369 ? 152.698 122.907 117.656 1.00 65.00  ? 367 MET A O   1 
ATOM   2345 C  CB  . MET A 1 369 ? 150.254 121.862 118.570 1.00 66.98  ? 367 MET A CB  1 
ATOM   2346 C  CG  . MET A 1 369 ? 149.044 121.232 119.234 1.00 60.14  ? 367 MET A CG  1 
ATOM   2347 S  SD  . MET A 1 369 ? 147.774 120.764 118.049 1.00 66.20  ? 367 MET A SD  1 
ATOM   2348 C  CE  . MET A 1 369 ? 146.947 119.461 118.951 1.00 62.11  ? 367 MET A CE  1 
ATOM   2349 N  N   . ASP A 1 370 ? 153.797 122.320 119.537 1.00 65.27  ? 368 ASP A N   1 
ATOM   2350 C  CA  . ASP A 1 370 ? 155.100 122.643 118.968 1.00 59.68  ? 368 ASP A CA  1 
ATOM   2351 C  C   . ASP A 1 370 ? 155.433 121.729 117.797 1.00 60.27  ? 368 ASP A C   1 
ATOM   2352 O  O   . ASP A 1 370 ? 155.921 122.192 116.760 1.00 60.71  ? 368 ASP A O   1 
ATOM   2353 C  CB  . ASP A 1 370 ? 156.185 122.547 120.039 1.00 58.65  ? 368 ASP A CB  1 
ATOM   2354 C  CG  . ASP A 1 370 ? 155.764 123.166 121.355 1.00 61.78  ? 368 ASP A CG  1 
ATOM   2355 O  OD1 . ASP A 1 370 ? 155.339 124.339 121.353 1.00 66.13  ? 368 ASP A OD1 1 
ATOM   2356 O  OD2 . ASP A 1 370 ? 155.862 122.482 122.394 1.00 63.19  ? 368 ASP A OD2 1 
ATOM   2357 N  N   . GLY A 1 371 ? 155.180 120.427 117.945 1.00 65.21  ? 369 GLY A N   1 
ATOM   2358 C  CA  . GLY A 1 371 ? 155.475 119.501 116.865 1.00 62.09  ? 369 GLY A CA  1 
ATOM   2359 C  C   . GLY A 1 371 ? 154.671 119.785 115.613 1.00 63.84  ? 369 GLY A C   1 
ATOM   2360 O  O   . GLY A 1 371 ? 155.206 119.766 114.502 1.00 63.92  ? 369 GLY A O   1 
ATOM   2361 N  N   . THR A 1 372 ? 153.373 120.052 115.772 1.00 65.16  ? 370 THR A N   1 
ATOM   2362 C  CA  . THR A 1 372 ? 152.543 120.361 114.613 1.00 64.83  ? 370 THR A CA  1 
ATOM   2363 C  C   . THR A 1 372 ? 153.010 121.639 113.928 1.00 65.66  ? 370 THR A C   1 
ATOM   2364 O  O   . THR A 1 372 ? 153.076 121.703 112.696 1.00 68.01  ? 370 THR A O   1 
ATOM   2365 C  CB  . THR A 1 372 ? 151.080 120.486 115.035 1.00 61.96  ? 370 THR A CB  1 
ATOM   2366 O  OG1 . THR A 1 372 ? 150.707 119.342 115.812 1.00 64.24  ? 370 THR A OG1 1 
ATOM   2367 C  CG2 . THR A 1 372 ? 150.175 120.587 113.817 1.00 65.60  ? 370 THR A CG2 1 
ATOM   2368 N  N   . ALA A 1 373 ? 153.352 122.663 114.711 1.00 64.54  ? 371 ALA A N   1 
ATOM   2369 C  CA  . ALA A 1 373 ? 153.857 123.900 114.124 1.00 66.83  ? 371 ALA A CA  1 
ATOM   2370 C  C   . ALA A 1 373 ? 155.146 123.658 113.351 1.00 66.34  ? 371 ALA A C   1 
ATOM   2371 O  O   . ALA A 1 373 ? 155.341 124.213 112.264 1.00 66.78  ? 371 ALA A O   1 
ATOM   2372 C  CB  . ALA A 1 373 ? 154.074 124.944 115.217 1.00 66.96  ? 371 ALA A CB  1 
ATOM   2373 N  N   . LEU A 1 374 ? 156.041 122.833 113.897 1.00 63.85  ? 372 LEU A N   1 
ATOM   2374 C  CA  . LEU A 1 374 ? 157.222 122.427 113.145 1.00 61.37  ? 372 LEU A CA  1 
ATOM   2375 C  C   . LEU A 1 374 ? 156.834 121.633 111.907 1.00 66.10  ? 372 LEU A C   1 
ATOM   2376 O  O   . LEU A 1 374 ? 157.478 121.743 110.858 1.00 70.76  ? 372 LEU A O   1 
ATOM   2377 C  CB  . LEU A 1 374 ? 158.141 121.593 114.038 1.00 61.75  ? 372 LEU A CB  1 
ATOM   2378 C  CG  . LEU A 1 374 ? 159.589 121.419 113.583 1.00 62.33  ? 372 LEU A CG  1 
ATOM   2379 C  CD1 . LEU A 1 374 ? 160.512 121.340 114.785 1.00 62.93  ? 372 LEU A CD1 1 
ATOM   2380 C  CD2 . LEU A 1 374 ? 159.738 120.186 112.709 1.00 63.50  ? 372 LEU A CD2 1 
ATOM   2381 N  N   . TYR A 1 375 ? 155.782 120.825 112.015 1.00 70.06  ? 373 TYR A N   1 
ATOM   2382 C  CA  . TYR A 1 375 ? 155.348 119.996 110.897 1.00 67.27  ? 373 TYR A CA  1 
ATOM   2383 C  C   . TYR A 1 375 ? 154.731 120.833 109.784 1.00 72.51  ? 373 TYR A C   1 
ATOM   2384 O  O   . TYR A 1 375 ? 155.058 120.651 108.606 1.00 74.12  ? 373 TYR A O   1 
ATOM   2385 C  CB  . TYR A 1 375 ? 154.373 118.944 111.407 1.00 67.94  ? 373 TYR A CB  1 
ATOM   2386 C  CG  . TYR A 1 375 ? 153.768 118.062 110.344 1.00 67.35  ? 373 TYR A CG  1 
ATOM   2387 C  CD1 . TYR A 1 375 ? 154.507 117.045 109.762 1.00 69.97  ? 373 TYR A CD1 1 
ATOM   2388 C  CD2 . TYR A 1 375 ? 152.448 118.219 109.951 1.00 66.05  ? 373 TYR A CD2 1 
ATOM   2389 C  CE1 . TYR A 1 375 ? 153.960 116.228 108.803 1.00 72.16  ? 373 TYR A CE1 1 
ATOM   2390 C  CE2 . TYR A 1 375 ? 151.891 117.402 108.992 1.00 69.50  ? 373 TYR A CE2 1 
ATOM   2391 C  CZ  . TYR A 1 375 ? 152.652 116.407 108.422 1.00 73.69  ? 373 TYR A CZ  1 
ATOM   2392 O  OH  . TYR A 1 375 ? 152.104 115.589 107.463 1.00 76.65  ? 373 TYR A OH  1 
ATOM   2393 N  N   . GLU A 1 376 ? 153.830 121.755 110.134 1.00 72.95  ? 374 GLU A N   1 
ATOM   2394 C  CA  . GLU A 1 376 ? 153.169 122.553 109.107 1.00 69.84  ? 374 GLU A CA  1 
ATOM   2395 C  C   . GLU A 1 376 ? 154.184 123.370 108.320 1.00 68.64  ? 374 GLU A C   1 
ATOM   2396 O  O   . GLU A 1 376 ? 154.114 123.440 107.088 1.00 72.60  ? 374 GLU A O   1 
ATOM   2397 C  CB  . GLU A 1 376 ? 152.123 123.475 109.737 1.00 68.76  ? 374 GLU A CB  1 
ATOM   2398 C  CG  . GLU A 1 376 ? 151.011 122.787 110.531 1.00 68.45  ? 374 GLU A CG  1 
ATOM   2399 C  CD  . GLU A 1 376 ? 150.220 121.772 109.725 1.00 75.68  ? 374 GLU A CD  1 
ATOM   2400 O  OE1 . GLU A 1 376 ? 150.832 120.888 109.095 1.00 77.23  ? 374 GLU A OE1 1 
ATOM   2401 O  OE2 . GLU A 1 376 ? 148.975 121.861 109.722 1.00 75.13  ? 374 GLU A OE2 1 
ATOM   2402 N  N   . ALA A 1 377 ? 155.134 123.998 109.012 1.00 67.24  ? 375 ALA A N   1 
ATOM   2403 C  CA  . ALA A 1 377 ? 156.137 124.794 108.316 1.00 70.33  ? 375 ALA A CA  1 
ATOM   2404 C  C   . ALA A 1 377 ? 157.047 123.912 107.471 1.00 71.92  ? 375 ALA A C   1 
ATOM   2405 O  O   . ALA A 1 377 ? 157.368 124.258 106.328 1.00 72.38  ? 375 ALA A O   1 
ATOM   2406 C  CB  . ALA A 1 377 ? 156.956 125.600 109.322 1.00 73.46  ? 375 ALA A CB  1 
ATOM   2407 N  N   . VAL A 1 378 ? 157.472 122.770 108.013 1.00 68.93  ? 376 VAL A N   1 
ATOM   2408 C  CA  . VAL A 1 378 ? 158.396 121.900 107.289 1.00 71.79  ? 376 VAL A CA  1 
ATOM   2409 C  C   . VAL A 1 378 ? 157.732 121.358 106.030 1.00 74.33  ? 376 VAL A C   1 
ATOM   2410 O  O   . VAL A 1 378 ? 158.323 121.356 104.944 1.00 74.97  ? 376 VAL A O   1 
ATOM   2411 C  CB  . VAL A 1 378 ? 158.888 120.766 108.208 1.00 71.57  ? 376 VAL A CB  1 
ATOM   2412 C  CG1 . VAL A 1 378 ? 159.469 119.604 107.404 1.00 72.47  ? 376 VAL A CG1 1 
ATOM   2413 C  CG2 . VAL A 1 378 ? 159.927 121.293 109.182 1.00 72.05  ? 376 VAL A CG2 1 
ATOM   2414 N  N   . ALA A 1 379 ? 156.491 120.887 106.157 1.00 76.05  ? 377 ALA A N   1 
ATOM   2415 C  CA  . ALA A 1 379 ? 155.823 120.263 105.020 1.00 76.01  ? 377 ALA A CA  1 
ATOM   2416 C  C   . ALA A 1 379 ? 155.412 121.298 103.981 1.00 77.91  ? 377 ALA A C   1 
ATOM   2417 O  O   . ALA A 1 379 ? 155.526 121.053 102.775 1.00 76.91  ? 377 ALA A O   1 
ATOM   2418 C  CB  . ALA A 1 379 ? 154.610 119.477 105.501 1.00 74.36  ? 377 ALA A CB  1 
ATOM   2419 N  N   . ALA A 1 380 ? 154.924 122.458 104.427 1.00 84.50  ? 378 ALA A N   1 
ATOM   2420 C  CA  . ALA A 1 380 ? 154.500 123.486 103.484 1.00 82.54  ? 378 ALA A CA  1 
ATOM   2421 C  C   . ALA A 1 380 ? 155.664 123.938 102.614 1.00 82.92  ? 378 ALA A C   1 
ATOM   2422 O  O   . ALA A 1 380 ? 155.523 124.074 101.393 1.00 85.01  ? 378 ALA A O   1 
ATOM   2423 C  CB  . ALA A 1 380 ? 153.898 124.672 104.235 1.00 82.59  ? 378 ALA A CB  1 
ATOM   2424 N  N   . VAL A 1 381 ? 156.825 124.171 103.226 1.00 77.86  ? 379 VAL A N   1 
ATOM   2425 C  CA  . VAL A 1 381 ? 158.015 124.506 102.454 1.00 77.80  ? 379 VAL A CA  1 
ATOM   2426 C  C   . VAL A 1 381 ? 158.424 123.328 101.580 1.00 81.16  ? 379 VAL A C   1 
ATOM   2427 O  O   . VAL A 1 381 ? 158.777 123.501 100.407 1.00 83.93  ? 379 VAL A O   1 
ATOM   2428 C  CB  . VAL A 1 381 ? 159.147 124.950 103.400 1.00 77.88  ? 379 VAL A CB  1 
ATOM   2429 C  CG1 . VAL A 1 381 ? 160.504 124.900 102.709 1.00 77.46  ? 379 VAL A CG1 1 
ATOM   2430 C  CG2 . VAL A 1 381 ? 158.872 126.347 103.928 1.00 83.00  ? 379 VAL A CG2 1 
ATOM   2431 N  N   . PHE A 1 382 ? 158.362 122.111 102.125 1.00 81.66  ? 380 PHE A N   1 
ATOM   2432 C  CA  . PHE A 1 382 ? 158.732 120.931 101.348 1.00 82.92  ? 380 PHE A CA  1 
ATOM   2433 C  C   . PHE A 1 382 ? 157.859 120.790 100.109 1.00 81.32  ? 380 PHE A C   1 
ATOM   2434 O  O   . PHE A 1 382 ? 158.361 120.513 99.014  1.00 83.59  ? 380 PHE A O   1 
ATOM   2435 C  CB  . PHE A 1 382 ? 158.627 119.677 102.215 1.00 82.27  ? 380 PHE A CB  1 
ATOM   2436 C  CG  . PHE A 1 382 ? 158.558 118.400 101.425 1.00 83.94  ? 380 PHE A CG  1 
ATOM   2437 C  CD1 . PHE A 1 382 ? 159.619 118.004 100.629 1.00 81.45  ? 380 PHE A CD1 1 
ATOM   2438 C  CD2 . PHE A 1 382 ? 157.431 117.598 101.477 1.00 83.00  ? 380 PHE A CD2 1 
ATOM   2439 C  CE1 . PHE A 1 382 ? 159.557 116.831 99.902  1.00 78.97  ? 380 PHE A CE1 1 
ATOM   2440 C  CE2 . PHE A 1 382 ? 157.365 116.424 100.751 1.00 80.57  ? 380 PHE A CE2 1 
ATOM   2441 C  CZ  . PHE A 1 382 ? 158.429 116.041 99.963  1.00 79.16  ? 380 PHE A CZ  1 
ATOM   2442 N  N   . ILE A 1 383 ? 156.548 120.980 100.258 1.00 82.15  ? 381 ILE A N   1 
ATOM   2443 C  CA  . ILE A 1 383 ? 155.657 120.907 99.105  1.00 83.91  ? 381 ILE A CA  1 
ATOM   2444 C  C   . ILE A 1 383 ? 155.987 122.018 98.117  1.00 86.22  ? 381 ILE A C   1 
ATOM   2445 O  O   . ILE A 1 383 ? 155.885 121.836 96.898  1.00 87.40  ? 381 ILE A O   1 
ATOM   2446 C  CB  . ILE A 1 383 ? 154.187 120.965 99.565  1.00 83.46  ? 381 ILE A CB  1 
ATOM   2447 C  CG1 . ILE A 1 383 ? 153.846 119.712 100.376 1.00 85.35  ? 381 ILE A CG1 1 
ATOM   2448 C  CG2 . ILE A 1 383 ? 153.247 121.093 98.367  1.00 85.03  ? 381 ILE A CG2 1 
ATOM   2449 C  CD1 . ILE A 1 383 ? 152.491 119.755 101.049 1.00 86.40  ? 381 ILE A CD1 1 
ATOM   2450 N  N   . ALA A 1 384 ? 156.389 123.184 98.625  1.00 85.11  ? 382 ALA A N   1 
ATOM   2451 C  CA  . ALA A 1 384 ? 156.769 124.278 97.738  1.00 85.64  ? 382 ALA A CA  1 
ATOM   2452 C  C   . ALA A 1 384 ? 157.954 123.891 96.862  1.00 84.15  ? 382 ALA A C   1 
ATOM   2453 O  O   . ALA A 1 384 ? 157.980 124.210 95.667  1.00 86.43  ? 382 ALA A O   1 
ATOM   2454 C  CB  . ALA A 1 384 ? 157.090 125.528 98.555  1.00 89.48  ? 382 ALA A CB  1 
ATOM   2455 N  N   . GLN A 1 385 ? 158.947 123.203 97.432  1.00 79.14  ? 383 GLN A N   1 
ATOM   2456 C  CA  . GLN A 1 385 ? 160.059 122.726 96.616  1.00 82.97  ? 383 GLN A CA  1 
ATOM   2457 C  C   . GLN A 1 385 ? 159.573 121.769 95.536  1.00 87.35  ? 383 GLN A C   1 
ATOM   2458 O  O   . GLN A 1 385 ? 160.059 121.803 94.400  1.00 86.58  ? 383 GLN A O   1 
ATOM   2459 C  CB  . GLN A 1 385 ? 161.117 122.043 97.484  1.00 83.67  ? 383 GLN A CB  1 
ATOM   2460 C  CG  . GLN A 1 385 ? 162.029 122.995 98.242  1.00 85.84  ? 383 GLN A CG  1 
ATOM   2461 C  CD  . GLN A 1 385 ? 162.104 122.685 99.722  1.00 84.55  ? 383 GLN A CD  1 
ATOM   2462 O  OE1 . GLN A 1 385 ? 161.156 122.919 100.464 1.00 83.71  ? 383 GLN A OE1 1 
ATOM   2463 N  NE2 . GLN A 1 385 ? 163.240 122.156 100.159 1.00 83.76  ? 383 GLN A NE2 1 
ATOM   2464 N  N   . LEU A 1 386 ? 158.612 120.905 95.872  1.00 86.83  ? 384 LEU A N   1 
ATOM   2465 C  CA  . LEU A 1 386 ? 158.043 120.014 94.868  1.00 86.15  ? 384 LEU A CA  1 
ATOM   2466 C  C   . LEU A 1 386 ? 157.401 120.808 93.738  1.00 87.64  ? 384 LEU A C   1 
ATOM   2467 O  O   . LEU A 1 386 ? 157.549 120.458 92.561  1.00 85.12  ? 384 LEU A O   1 
ATOM   2468 C  CB  . LEU A 1 386 ? 157.021 119.079 95.515  1.00 85.13  ? 384 LEU A CB  1 
ATOM   2469 C  CG  . LEU A 1 386 ? 157.546 117.777 96.131  1.00 86.82  ? 384 LEU A CG  1 
ATOM   2470 C  CD1 . LEU A 1 386 ? 158.916 117.953 96.775  1.00 86.61  ? 384 LEU A CD1 1 
ATOM   2471 C  CD2 . LEU A 1 386 ? 156.549 117.239 97.145  1.00 87.16  ? 384 LEU A CD2 1 
ATOM   2472 N  N   . ASN A 1 387 ? 156.685 121.882 94.076  1.00 93.40  ? 385 ASN A N   1 
ATOM   2473 C  CA  . ASN A 1 387 ? 156.103 122.750 93.060  1.00 93.52  ? 385 ASN A CA  1 
ATOM   2474 C  C   . ASN A 1 387 ? 157.152 123.566 92.317  1.00 92.96  ? 385 ASN A C   1 
ATOM   2475 O  O   . ASN A 1 387 ? 156.817 124.205 91.315  1.00 91.69  ? 385 ASN A O   1 
ATOM   2476 C  CB  . ASN A 1 387 ? 155.079 123.686 93.701  1.00 93.25  ? 385 ASN A CB  1 
ATOM   2477 C  CG  . ASN A 1 387 ? 153.821 122.961 94.134  1.00 94.18  ? 385 ASN A CG  1 
ATOM   2478 O  OD1 . ASN A 1 387 ? 153.873 122.040 94.947  1.00 93.37  ? 385 ASN A OD1 1 
ATOM   2479 N  ND2 . ASN A 1 387 ? 152.682 123.377 93.594  1.00 94.87  ? 385 ASN A ND2 1 
ATOM   2480 N  N   . ASP A 1 388 ? 158.401 123.566 92.784  1.00 93.10  ? 386 ASP A N   1 
ATOM   2481 C  CA  . ASP A 1 388 ? 159.501 124.233 92.089  1.00 92.68  ? 386 ASP A CA  1 
ATOM   2482 C  C   . ASP A 1 388 ? 159.287 125.745 92.042  1.00 93.61  ? 386 ASP A C   1 
ATOM   2483 O  O   . ASP A 1 388 ? 159.543 126.397 91.027  1.00 96.36  ? 386 ASP A O   1 
ATOM   2484 C  CB  . ASP A 1 388 ? 159.681 123.663 90.679  1.00 95.38  ? 386 ASP A CB  1 
ATOM   2485 C  CG  . ASP A 1 388 ? 160.934 124.178 89.992  1.00 96.68  ? 386 ASP A CG  1 
ATOM   2486 O  OD1 . ASP A 1 388 ? 161.647 125.013 90.587  1.00 94.55  ? 386 ASP A OD1 1 
ATOM   2487 O  OD2 . ASP A 1 388 ? 161.213 123.735 88.858  1.00 95.86  ? 386 ASP A OD2 1 
ATOM   2488 N  N   . LEU A 1 389 ? 158.802 126.308 93.144  1.00 91.35  ? 387 LEU A N   1 
ATOM   2489 C  CA  . LEU A 1 389 ? 158.664 127.750 93.297  1.00 93.72  ? 387 LEU A CA  1 
ATOM   2490 C  C   . LEU A 1 389 ? 159.695 128.237 94.305  1.00 94.09  ? 387 LEU A C   1 
ATOM   2491 O  O   . LEU A 1 389 ? 159.829 127.661 95.390  1.00 93.08  ? 387 LEU A O   1 
ATOM   2492 C  CB  . LEU A 1 389 ? 157.251 128.132 93.746  1.00 93.42  ? 387 LEU A CB  1 
ATOM   2493 C  CG  . LEU A 1 389 ? 156.796 127.640 95.119  1.00 94.69  ? 387 LEU A CG  1 
ATOM   2494 C  CD1 . LEU A 1 389 ? 156.977 128.724 96.170  1.00 94.04  ? 387 LEU A CD1 1 
ATOM   2495 C  CD2 . LEU A 1 389 ? 155.347 127.193 95.065  1.00 93.75  ? 387 LEU A CD2 1 
ATOM   2496 N  N   . ASP A 1 390 ? 160.425 129.287 93.940  1.00 95.50  ? 388 ASP A N   1 
ATOM   2497 C  CA  . ASP A 1 390 ? 161.478 129.798 94.805  1.00 94.26  ? 388 ASP A CA  1 
ATOM   2498 C  C   . ASP A 1 390 ? 160.892 130.325 96.108  1.00 93.28  ? 388 ASP A C   1 
ATOM   2499 O  O   . ASP A 1 390 ? 159.825 130.945 96.125  1.00 89.62  ? 388 ASP A O   1 
ATOM   2500 C  CB  . ASP A 1 390 ? 162.256 130.903 94.092  1.00 94.28  ? 388 ASP A CB  1 
ATOM   2501 C  CG  . ASP A 1 390 ? 162.895 130.425 92.805  1.00 95.03  ? 388 ASP A CG  1 
ATOM   2502 O  OD1 . ASP A 1 390 ? 163.735 129.502 92.865  1.00 93.80  ? 388 ASP A OD1 1 
ATOM   2503 O  OD2 . ASP A 1 390 ? 162.557 130.970 91.734  1.00 95.87  ? 388 ASP A OD2 1 
ATOM   2504 N  N   . LEU A 1 391 ? 161.599 130.072 97.205  1.00 92.91  ? 389 LEU A N   1 
ATOM   2505 C  CA  . LEU A 1 391 ? 161.196 130.505 98.541  1.00 93.35  ? 389 LEU A CA  1 
ATOM   2506 C  C   . LEU A 1 391 ? 162.324 131.357 99.114  1.00 92.36  ? 389 LEU A C   1 
ATOM   2507 O  O   . LEU A 1 391 ? 163.223 130.848 99.787  1.00 90.52  ? 389 LEU A O   1 
ATOM   2508 C  CB  . LEU A 1 391 ? 160.882 129.310 99.442  1.00 93.00  ? 389 LEU A CB  1 
ATOM   2509 C  CG  . LEU A 1 391 ? 159.552 128.576 99.240  1.00 91.63  ? 389 LEU A CG  1 
ATOM   2510 C  CD1 . LEU A 1 391 ? 159.349 127.587 100.369 1.00 90.50  ? 389 LEU A CD1 1 
ATOM   2511 C  CD2 . LEU A 1 391 ? 158.363 129.524 99.151  1.00 91.67  ? 389 LEU A CD2 1 
ATOM   2512 N  N   . GLY A 1 392 ? 162.271 132.657 98.843  1.00 94.50  ? 390 GLY A N   1 
ATOM   2513 C  CA  . GLY A 1 392 ? 163.222 133.594 99.395  1.00 93.32  ? 390 GLY A CA  1 
ATOM   2514 C  C   . GLY A 1 392 ? 162.835 134.026 100.796 1.00 94.19  ? 390 GLY A C   1 
ATOM   2515 O  O   . GLY A 1 392 ? 161.885 133.528 101.401 1.00 94.23  ? 390 GLY A O   1 
ATOM   2516 N  N   . ILE A 1 393 ? 163.597 134.989 101.315 1.00 92.03  ? 391 ILE A N   1 
ATOM   2517 C  CA  . ILE A 1 393 ? 163.367 135.461 102.677 1.00 92.14  ? 391 ILE A CA  1 
ATOM   2518 C  C   . ILE A 1 393 ? 161.980 136.079 102.801 1.00 91.79  ? 391 ILE A C   1 
ATOM   2519 O  O   . ILE A 1 393 ? 161.266 135.845 103.782 1.00 87.63  ? 391 ILE A O   1 
ATOM   2520 C  CB  . ILE A 1 393 ? 164.469 136.456 103.089 1.00 91.76  ? 391 ILE A CB  1 
ATOM   2521 C  CG1 . ILE A 1 393 ? 165.846 135.796 102.998 1.00 92.58  ? 391 ILE A CG1 1 
ATOM   2522 C  CG2 . ILE A 1 393 ? 164.231 136.968 104.505 1.00 90.56  ? 391 ILE A CG2 1 
ATOM   2523 C  CD1 . ILE A 1 393 ? 166.650 136.215 101.783 1.00 92.64  ? 391 ILE A CD1 1 
ATOM   2524 N  N   . GLY A 1 394 ? 161.573 136.869 101.808 1.00 93.81  ? 392 GLY A N   1 
ATOM   2525 C  CA  . GLY A 1 394 ? 160.330 137.613 101.932 1.00 93.81  ? 392 GLY A CA  1 
ATOM   2526 C  C   . GLY A 1 394 ? 159.115 136.723 102.108 1.00 95.07  ? 392 GLY A C   1 
ATOM   2527 O  O   . GLY A 1 394 ? 158.238 137.010 102.925 1.00 94.12  ? 392 GLY A O   1 
ATOM   2528 N  N   . GLN A 1 395 ? 159.037 135.638 101.339 1.00 94.28  ? 393 GLN A N   1 
ATOM   2529 C  CA  . GLN A 1 395 ? 157.828 134.822 101.327 1.00 95.41  ? 393 GLN A CA  1 
ATOM   2530 C  C   . GLN A 1 395 ? 157.790 133.785 102.443 1.00 94.91  ? 393 GLN A C   1 
ATOM   2531 O  O   . GLN A 1 395 ? 156.699 133.416 102.888 1.00 90.06  ? 393 GLN A O   1 
ATOM   2532 C  CB  . GLN A 1 395 ? 157.660 134.121 99.973  1.00 92.14  ? 393 GLN A CB  1 
ATOM   2533 C  CG  . GLN A 1 395 ? 158.884 133.388 99.442  1.00 89.84  ? 393 GLN A CG  1 
ATOM   2534 C  CD  . GLN A 1 395 ? 158.756 133.060 97.967  1.00 92.96  ? 393 GLN A CD  1 
ATOM   2535 O  OE1 . GLN A 1 395 ? 157.846 132.341 97.557  1.00 94.65  ? 393 GLN A OE1 1 
ATOM   2536 N  NE2 . GLN A 1 395 ? 159.666 133.593 97.160  1.00 93.90  ? 393 GLN A NE2 1 
ATOM   2537 N  N   . ILE A 1 396 ? 158.943 133.301 102.910 1.00 91.83  ? 394 ILE A N   1 
ATOM   2538 C  CA  . ILE A 1 396 ? 158.943 132.269 103.944 1.00 90.54  ? 394 ILE A CA  1 
ATOM   2539 C  C   . ILE A 1 396 ? 158.358 132.774 105.257 1.00 87.63  ? 394 ILE A C   1 
ATOM   2540 O  O   . ILE A 1 396 ? 157.997 131.967 106.120 1.00 81.52  ? 394 ILE A O   1 
ATOM   2541 C  CB  . ILE A 1 396 ? 160.367 131.716 104.165 1.00 89.70  ? 394 ILE A CB  1 
ATOM   2542 C  CG1 . ILE A 1 396 ? 161.335 132.846 104.531 1.00 89.57  ? 394 ILE A CG1 1 
ATOM   2543 C  CG2 . ILE A 1 396 ? 160.831 130.956 102.929 1.00 85.73  ? 394 ILE A CG2 1 
ATOM   2544 C  CD1 . ILE A 1 396 ? 162.720 132.372 104.928 1.00 87.64  ? 394 ILE A CD1 1 
ATOM   2545 N  N   . ILE A 1 397 ? 158.248 134.093 105.434 1.00 90.31  ? 395 ILE A N   1 
ATOM   2546 C  CA  . ILE A 1 397 ? 157.722 134.623 106.692 1.00 89.86  ? 395 ILE A CA  1 
ATOM   2547 C  C   . ILE A 1 397 ? 156.265 134.220 106.880 1.00 87.41  ? 395 ILE A C   1 
ATOM   2548 O  O   . ILE A 1 397 ? 155.862 133.805 107.973 1.00 87.55  ? 395 ILE A O   1 
ATOM   2549 C  CB  . ILE A 1 397 ? 157.895 136.155 106.783 1.00 89.65  ? 395 ILE A CB  1 
ATOM   2550 C  CG1 . ILE A 1 397 ? 159.122 136.660 106.008 1.00 87.49  ? 395 ILE A CG1 1 
ATOM   2551 C  CG2 . ILE A 1 397 ? 157.960 136.591 108.243 1.00 86.98  ? 395 ILE A CG2 1 
ATOM   2552 C  CD1 . ILE A 1 397 ? 160.444 136.145 106.546 1.00 89.04  ? 395 ILE A CD1 1 
ATOM   2553 N  N   . THR A 1 398 ? 155.447 134.334 105.830 1.00 85.33  ? 396 THR A N   1 
ATOM   2554 C  CA  . THR A 1 398 ? 154.034 134.004 105.990 1.00 88.03  ? 396 THR A CA  1 
ATOM   2555 C  C   . THR A 1 398 ? 153.850 132.539 106.363 1.00 88.65  ? 396 THR A C   1 
ATOM   2556 O  O   . THR A 1 398 ? 152.899 132.195 107.072 1.00 83.18  ? 396 THR A O   1 
ATOM   2557 C  CB  . THR A 1 398 ? 153.247 134.334 104.718 1.00 87.31  ? 396 THR A CB  1 
ATOM   2558 O  OG1 . THR A 1 398 ? 151.843 134.235 104.987 1.00 87.52  ? 396 THR A OG1 1 
ATOM   2559 C  CG2 . THR A 1 398 ? 153.594 133.380 103.583 1.00 83.90  ? 396 THR A CG2 1 
ATOM   2560 N  N   . ILE A 1 399 ? 154.754 131.666 105.919 1.00 87.03  ? 397 ILE A N   1 
ATOM   2561 C  CA  . ILE A 1 399 ? 154.704 130.278 106.365 1.00 84.61  ? 397 ILE A CA  1 
ATOM   2562 C  C   . ILE A 1 399 ? 154.971 130.200 107.862 1.00 84.90  ? 397 ILE A C   1 
ATOM   2563 O  O   . ILE A 1 399 ? 154.297 129.461 108.590 1.00 80.88  ? 397 ILE A O   1 
ATOM   2564 C  CB  . ILE A 1 399 ? 155.699 129.415 105.566 1.00 80.61  ? 397 ILE A CB  1 
ATOM   2565 C  CG1 . ILE A 1 399 ? 155.458 129.580 104.062 1.00 82.31  ? 397 ILE A CG1 1 
ATOM   2566 C  CG2 . ILE A 1 399 ? 155.575 127.952 105.979 1.00 82.43  ? 397 ILE A CG2 1 
ATOM   2567 C  CD1 . ILE A 1 399 ? 156.412 128.795 103.182 1.00 83.58  ? 397 ILE A CD1 1 
ATOM   2568 N  N   . SER A 1 400 ? 155.955 130.960 108.346 1.00 83.37  ? 398 SER A N   1 
ATOM   2569 C  CA  . SER A 1 400 ? 156.238 130.975 109.776 1.00 77.93  ? 398 SER A CA  1 
ATOM   2570 C  C   . SER A 1 400 ? 155.045 131.484 110.574 1.00 80.58  ? 398 SER A C   1 
ATOM   2571 O  O   . SER A 1 400 ? 154.682 130.900 111.602 1.00 81.38  ? 398 SER A O   1 
ATOM   2572 C  CB  . SER A 1 400 ? 157.466 131.840 110.057 1.00 80.02  ? 398 SER A CB  1 
ATOM   2573 O  OG  . SER A 1 400 ? 158.551 131.478 109.224 1.00 81.77  ? 398 SER A OG  1 
ATOM   2574 N  N   . ILE A 1 401 ? 154.421 132.573 110.121 1.00 81.64  ? 399 ILE A N   1 
ATOM   2575 C  CA  . ILE A 1 401 ? 153.276 133.114 110.846 1.00 84.86  ? 399 ILE A CA  1 
ATOM   2576 C  C   . ILE A 1 401 ? 152.066 132.198 110.700 1.00 81.45  ? 399 ILE A C   1 
ATOM   2577 O  O   . ILE A 1 401 ? 151.350 131.934 111.674 1.00 79.29  ? 399 ILE A O   1 
ATOM   2578 C  CB  . ILE A 1 401 ? 152.966 134.545 110.368 1.00 82.85  ? 399 ILE A CB  1 
ATOM   2579 C  CG1 . ILE A 1 401 ? 154.234 135.406 110.400 1.00 78.84  ? 399 ILE A CG1 1 
ATOM   2580 C  CG2 . ILE A 1 401 ? 151.903 135.169 111.259 1.00 79.80  ? 399 ILE A CG2 1 
ATOM   2581 C  CD1 . ILE A 1 401 ? 154.055 136.810 109.850 1.00 79.95  ? 399 ILE A CD1 1 
ATOM   2582 N  N   . THR A 1 402 ? 151.813 131.699 109.487 1.00 76.58  ? 400 THR A N   1 
ATOM   2583 C  CA  . THR A 1 402 ? 150.652 130.838 109.276 1.00 80.10  ? 400 THR A CA  1 
ATOM   2584 C  C   . THR A 1 402 ? 150.827 129.492 109.968 1.00 82.24  ? 400 THR A C   1 
ATOM   2585 O  O   . THR A 1 402 ? 149.866 128.944 110.520 1.00 78.04  ? 400 THR A O   1 
ATOM   2586 C  CB  . THR A 1 402 ? 150.386 130.651 107.781 1.00 80.21  ? 400 THR A CB  1 
ATOM   2587 O  OG1 . THR A 1 402 ? 151.537 130.080 107.147 1.00 81.15  ? 400 THR A OG1 1 
ATOM   2588 C  CG2 . THR A 1 402 ? 150.001 131.975 107.122 1.00 80.70  ? 400 THR A CG2 1 
ATOM   2589 N  N   . ALA A 1 403 ? 152.043 128.942 109.949 1.00 77.03  ? 401 ALA A N   1 
ATOM   2590 C  CA  . ALA A 1 403 ? 152.278 127.666 110.617 1.00 71.53  ? 401 ALA A CA  1 
ATOM   2591 C  C   . ALA A 1 403 ? 151.993 127.774 112.108 1.00 67.87  ? 401 ALA A C   1 
ATOM   2592 O  O   . ALA A 1 403 ? 151.373 126.881 112.696 1.00 67.11  ? 401 ALA A O   1 
ATOM   2593 C  CB  . ALA A 1 403 ? 153.714 127.205 110.378 1.00 72.68  ? 401 ALA A CB  1 
ATOM   2594 N  N   . THR A 1 404 ? 152.438 128.863 112.737 1.00 70.01  ? 402 THR A N   1 
ATOM   2595 C  CA  . THR A 1 404 ? 152.111 129.088 114.140 1.00 74.80  ? 402 THR A CA  1 
ATOM   2596 C  C   . THR A 1 404 ? 150.607 129.239 114.330 1.00 74.02  ? 402 THR A C   1 
ATOM   2597 O  O   . THR A 1 404 ? 150.032 128.683 115.273 1.00 68.82  ? 402 THR A O   1 
ATOM   2598 C  CB  . THR A 1 404 ? 152.837 130.331 114.654 1.00 72.86  ? 402 THR A CB  1 
ATOM   2599 O  OG1 . THR A 1 404 ? 154.206 130.298 114.231 1.00 70.73  ? 402 THR A OG1 1 
ATOM   2600 C  CG2 . THR A 1 404 ? 152.776 130.401 116.174 1.00 69.69  ? 402 THR A CG2 1 
ATOM   2601 N  N   . SER A 1 405 ? 149.951 129.989 113.441 1.00 75.01  ? 403 SER A N   1 
ATOM   2602 C  CA  . SER A 1 405 ? 148.509 130.183 113.549 1.00 74.04  ? 403 SER A CA  1 
ATOM   2603 C  C   . SER A 1 405 ? 147.754 128.879 113.319 1.00 73.70  ? 403 SER A C   1 
ATOM   2604 O  O   . SER A 1 405 ? 146.778 128.589 114.021 1.00 70.89  ? 403 SER A O   1 
ATOM   2605 C  CB  . SER A 1 405 ? 148.050 131.246 112.553 1.00 71.85  ? 403 SER A CB  1 
ATOM   2606 O  OG  . SER A 1 405 ? 148.083 130.747 111.229 1.00 71.07  ? 403 SER A OG  1 
ATOM   2607 N  N   . ALA A 1 406 ? 148.184 128.083 112.338 1.00 72.11  ? 404 ALA A N   1 
ATOM   2608 C  CA  . ALA A 1 406 ? 147.499 126.825 112.059 1.00 75.35  ? 404 ALA A CA  1 
ATOM   2609 C  C   . ALA A 1 406 ? 147.578 125.881 113.251 1.00 75.79  ? 404 ALA A C   1 
ATOM   2610 O  O   . ALA A 1 406 ? 146.587 125.232 113.606 1.00 72.61  ? 404 ALA A O   1 
ATOM   2611 C  CB  . ALA A 1 406 ? 148.095 126.169 110.815 1.00 77.27  ? 404 ALA A CB  1 
ATOM   2612 N  N   . SER A 1 407 ? 148.750 125.789 113.883 1.00 70.71  ? 405 SER A N   1 
ATOM   2613 C  CA  . SER A 1 407 ? 148.889 124.929 115.052 1.00 69.98  ? 405 SER A CA  1 
ATOM   2614 C  C   . SER A 1 407 ? 148.004 125.400 116.198 1.00 68.06  ? 405 SER A C   1 
ATOM   2615 O  O   . SER A 1 407 ? 147.561 124.586 117.016 1.00 69.60  ? 405 SER A O   1 
ATOM   2616 C  CB  . SER A 1 407 ? 150.351 124.883 115.497 1.00 70.79  ? 405 SER A CB  1 
ATOM   2617 O  OG  . SER A 1 407 ? 150.788 126.155 115.941 1.00 73.45  ? 405 SER A OG  1 
ATOM   2618 N  N   . ILE A 1 408 ? 147.740 126.705 116.276 1.00 61.67  ? 406 ILE A N   1 
ATOM   2619 C  CA  . ILE A 1 408 ? 146.896 127.234 117.343 1.00 63.10  ? 406 ILE A CA  1 
ATOM   2620 C  C   . ILE A 1 408 ? 145.473 126.706 117.204 1.00 65.70  ? 406 ILE A C   1 
ATOM   2621 O  O   . ILE A 1 408 ? 144.860 126.260 118.182 1.00 63.46  ? 406 ILE A O   1 
ATOM   2622 C  CB  . ILE A 1 408 ? 146.935 128.774 117.333 1.00 61.05  ? 406 ILE A CB  1 
ATOM   2623 C  CG1 . ILE A 1 408 ? 148.276 129.268 117.884 1.00 62.39  ? 406 ILE A CG1 1 
ATOM   2624 C  CG2 . ILE A 1 408 ? 145.781 129.355 118.145 1.00 61.98  ? 406 ILE A CG2 1 
ATOM   2625 C  CD1 . ILE A 1 408 ? 148.492 130.760 117.758 1.00 63.65  ? 406 ILE A CD1 1 
ATOM   2626 N  N   . GLY A 1 409 ? 144.925 126.749 115.988 1.00 65.54  ? 407 GLY A N   1 
ATOM   2627 C  CA  . GLY A 1 409 ? 143.553 126.326 115.772 1.00 62.65  ? 407 GLY A CA  1 
ATOM   2628 C  C   . GLY A 1 409 ? 143.358 124.829 115.679 1.00 62.24  ? 407 GLY A C   1 
ATOM   2629 O  O   . GLY A 1 409 ? 142.222 124.357 115.795 1.00 65.65  ? 407 GLY A O   1 
ATOM   2630 N  N   . ALA A 1 410 ? 144.432 124.071 115.474 1.00 65.89  ? 408 ALA A N   1 
ATOM   2631 C  CA  . ALA A 1 410 ? 144.308 122.628 115.315 1.00 69.66  ? 408 ALA A CA  1 
ATOM   2632 C  C   . ALA A 1 410 ? 143.729 121.995 116.574 1.00 69.68  ? 408 ALA A C   1 
ATOM   2633 O  O   . ALA A 1 410 ? 144.159 122.294 117.692 1.00 64.37  ? 408 ALA A O   1 
ATOM   2634 C  CB  . ALA A 1 410 ? 145.671 122.015 114.997 1.00 65.32  ? 408 ALA A CB  1 
ATOM   2635 N  N   . ALA A 1 411 ? 142.751 121.113 116.386 1.00 59.92  ? 409 ALA A N   1 
ATOM   2636 C  CA  . ALA A 1 411 ? 142.166 120.386 117.499 1.00 54.65  ? 409 ALA A CA  1 
ATOM   2637 C  C   . ALA A 1 411 ? 143.118 119.294 117.980 1.00 58.31  ? 409 ALA A C   1 
ATOM   2638 O  O   . ALA A 1 411 ? 144.006 118.839 117.255 1.00 60.55  ? 409 ALA A O   1 
ATOM   2639 C  CB  . ALA A 1 411 ? 140.829 119.769 117.093 1.00 55.62  ? 409 ALA A CB  1 
ATOM   2640 N  N   . GLY A 1 412 ? 142.921 118.872 119.225 1.00 59.18  ? 410 GLY A N   1 
ATOM   2641 C  CA  . GLY A 1 412 ? 143.764 117.846 119.807 1.00 61.80  ? 410 GLY A CA  1 
ATOM   2642 C  C   . GLY A 1 412 ? 143.371 116.446 119.386 1.00 63.04  ? 410 GLY A C   1 
ATOM   2643 O  O   . GLY A 1 412 ? 143.213 115.560 120.232 1.00 61.34  ? 410 GLY A O   1 
ATOM   2644 N  N   . VAL A 1 413 ? 143.217 116.232 118.083 1.00 60.99  ? 411 VAL A N   1 
ATOM   2645 C  CA  . VAL A 1 413 ? 142.798 114.935 117.554 1.00 59.50  ? 411 VAL A CA  1 
ATOM   2646 C  C   . VAL A 1 413 ? 143.800 114.503 116.492 1.00 59.64  ? 411 VAL A C   1 
ATOM   2647 O  O   . VAL A 1 413 ? 144.509 115.338 115.910 1.00 62.72  ? 411 VAL A O   1 
ATOM   2648 C  CB  . VAL A 1 413 ? 141.363 114.990 116.980 1.00 53.90  ? 411 VAL A CB  1 
ATOM   2649 C  CG1 . VAL A 1 413 ? 140.361 115.213 118.098 1.00 53.20  ? 411 VAL A CG1 1 
ATOM   2650 C  CG2 . VAL A 1 413 ? 141.246 116.080 115.927 1.00 51.01  ? 411 VAL A CG2 1 
ATOM   2651 N  N   . PRO A 1 414 ? 143.886 113.191 116.164 1.00 59.68  ? 412 PRO A N   1 
ATOM   2652 C  CA  . PRO A 1 414 ? 144.755 112.735 115.077 1.00 60.87  ? 412 PRO A CA  1 
ATOM   2653 C  C   . PRO A 1 414 ? 144.331 113.357 113.740 1.00 61.22  ? 412 PRO A C   1 
ATOM   2654 O  O   . PRO A 1 414 ? 143.160 113.649 113.590 1.00 64.12  ? 412 PRO A O   1 
ATOM   2655 C  CB  . PRO A 1 414 ? 144.514 111.221 115.019 1.00 56.65  ? 412 PRO A CB  1 
ATOM   2656 C  CG  . PRO A 1 414 ? 144.019 110.870 116.401 1.00 59.07  ? 412 PRO A CG  1 
ATOM   2657 C  CD  . PRO A 1 414 ? 143.199 112.071 116.821 1.00 57.50  ? 412 PRO A CD  1 
ATOM   2658 N  N   . GLN A 1 415 ? 145.281 113.554 112.822 1.00 59.70  ? 413 GLN A N   1 
ATOM   2659 C  CA  . GLN A 1 415 ? 144.964 114.100 111.473 1.00 63.92  ? 413 GLN A CA  1 
ATOM   2660 C  C   . GLN A 1 415 ? 144.534 115.568 111.579 1.00 65.41  ? 413 GLN A C   1 
ATOM   2661 O  O   . GLN A 1 415 ? 144.086 116.117 110.555 1.00 64.52  ? 413 GLN A O   1 
ATOM   2662 C  CB  . GLN A 1 415 ? 143.875 113.263 110.800 1.00 67.56  ? 413 GLN A CB  1 
ATOM   2663 C  CG  . GLN A 1 415 ? 144.199 111.778 110.736 1.00 67.44  ? 413 GLN A CG  1 
ATOM   2664 C  CD  . GLN A 1 415 ? 143.050 110.973 110.180 1.00 68.67  ? 413 GLN A CD  1 
ATOM   2665 O  OE1 . GLN A 1 415 ? 142.049 111.518 109.721 1.00 68.84  ? 413 GLN A OE1 1 
ATOM   2666 N  NE2 . GLN A 1 415 ? 143.189 109.658 110.216 1.00 67.39  ? 413 GLN A NE2 1 
ATOM   2667 N  N   . ALA A 1 416 ? 144.667 116.179 112.760 1.00 68.61  ? 414 ALA A N   1 
ATOM   2668 C  CA  . ALA A 1 416 ? 144.343 117.618 112.908 1.00 71.12  ? 414 ALA A CA  1 
ATOM   2669 C  C   . ALA A 1 416 ? 145.295 118.430 112.028 1.00 74.13  ? 414 ALA A C   1 
ATOM   2670 O  O   . ALA A 1 416 ? 144.881 119.490 111.524 1.00 70.04  ? 414 ALA A O   1 
ATOM   2671 C  CB  . ALA A 1 416 ? 144.448 118.026 114.354 1.00 68.12  ? 414 ALA A CB  1 
ATOM   2672 N  N   . GLY A 1 417 ? 146.526 117.946 111.857 1.00 76.20  ? 415 GLY A N   1 
ATOM   2673 C  CA  . GLY A 1 417 ? 147.494 118.627 111.016 1.00 75.55  ? 415 GLY A CA  1 
ATOM   2674 C  C   . GLY A 1 417 ? 147.052 118.683 109.567 1.00 77.26  ? 415 GLY A C   1 
ATOM   2675 O  O   . GLY A 1 417 ? 147.239 119.697 108.889 1.00 75.59  ? 415 GLY A O   1 
ATOM   2676 N  N   . LEU A 1 418 ? 146.457 117.595 109.074 1.00 78.59  ? 416 LEU A N   1 
ATOM   2677 C  CA  . LEU A 1 418 ? 146.046 117.534 107.675 1.00 79.64  ? 416 LEU A CA  1 
ATOM   2678 C  C   . LEU A 1 418 ? 144.946 118.543 107.369 1.00 77.94  ? 416 LEU A C   1 
ATOM   2679 O  O   . LEU A 1 418 ? 144.952 119.171 106.304 1.00 76.52  ? 416 LEU A O   1 
ATOM   2680 C  CB  . LEU A 1 418 ? 145.582 116.118 107.338 1.00 80.38  ? 416 LEU A CB  1 
ATOM   2681 C  CG  . LEU A 1 418 ? 146.656 115.029 107.370 1.00 80.18  ? 416 LEU A CG  1 
ATOM   2682 C  CD1 . LEU A 1 418 ? 146.027 113.666 107.152 1.00 76.54  ? 416 LEU A CD1 1 
ATOM   2683 C  CD2 . LEU A 1 418 ? 147.735 115.285 106.329 1.00 79.27  ? 416 LEU A CD2 1 
ATOM   2684 N  N   . VAL A 1 419 ? 143.982 118.702 108.277 1.00 78.23  ? 417 VAL A N   1 
ATOM   2685 C  CA  . VAL A 1 419 ? 142.862 119.598 108.007 1.00 82.00  ? 417 VAL A CA  1 
ATOM   2686 C  C   . VAL A 1 419 ? 143.320 121.052 108.017 1.00 76.86  ? 417 VAL A C   1 
ATOM   2687 O  O   . VAL A 1 419 ? 142.878 121.860 107.192 1.00 75.19  ? 417 VAL A O   1 
ATOM   2688 C  CB  . VAL A 1 419 ? 141.717 119.344 109.007 1.00 84.46  ? 417 VAL A CB  1 
ATOM   2689 C  CG1 . VAL A 1 419 ? 141.331 117.870 109.008 1.00 80.35  ? 417 VAL A CG1 1 
ATOM   2690 C  CG2 . VAL A 1 419 ? 142.099 119.791 110.414 1.00 78.29  ? 417 VAL A CG2 1 
ATOM   2691 N  N   . THR A 1 420 ? 144.208 121.411 108.944 1.00 76.76  ? 418 THR A N   1 
ATOM   2692 C  CA  . THR A 1 420 ? 144.738 122.767 109.008 1.00 80.43  ? 418 THR A CA  1 
ATOM   2693 C  C   . THR A 1 420 ? 145.795 123.041 107.947 1.00 77.78  ? 418 THR A C   1 
ATOM   2694 O  O   . THR A 1 420 ? 146.218 124.193 107.801 1.00 77.75  ? 418 THR A O   1 
ATOM   2695 C  CB  . THR A 1 420 ? 145.332 123.043 110.393 1.00 80.47  ? 418 THR A CB  1 
ATOM   2696 O  OG1 . THR A 1 420 ? 146.536 122.285 110.563 1.00 79.81  ? 418 THR A OG1 1 
ATOM   2697 C  CG2 . THR A 1 420 ? 144.337 122.690 111.491 1.00 78.88  ? 418 THR A CG2 1 
ATOM   2698 N  N   . MET A 1 421 ? 146.229 122.019 107.209 1.00 77.62  ? 419 MET A N   1 
ATOM   2699 C  CA  . MET A 1 421 ? 147.222 122.227 106.162 1.00 79.96  ? 419 MET A CA  1 
ATOM   2700 C  C   . MET A 1 421 ? 146.716 123.183 105.091 1.00 81.52  ? 419 MET A C   1 
ATOM   2701 O  O   . MET A 1 421 ? 147.514 123.862 104.436 1.00 78.42  ? 419 MET A O   1 
ATOM   2702 C  CB  . MET A 1 421 ? 147.586 120.886 105.532 1.00 82.40  ? 419 MET A CB  1 
ATOM   2703 C  CG  . MET A 1 421 ? 148.691 120.159 106.248 1.00 82.60  ? 419 MET A CG  1 
ATOM   2704 S  SD  . MET A 1 421 ? 150.321 120.490 105.582 1.00 87.73  ? 419 MET A SD  1 
ATOM   2705 C  CE  . MET A 1 421 ? 151.204 119.182 106.408 1.00 79.90  ? 419 MET A CE  1 
ATOM   2706 N  N   . VAL A 1 422 ? 145.397 123.250 104.899 1.00 88.42  ? 420 VAL A N   1 
ATOM   2707 C  CA  . VAL A 1 422 ? 144.841 124.111 103.859 1.00 89.34  ? 420 VAL A CA  1 
ATOM   2708 C  C   . VAL A 1 422 ? 145.157 125.570 104.156 1.00 85.94  ? 420 VAL A C   1 
ATOM   2709 O  O   . VAL A 1 422 ? 145.421 126.362 103.242 1.00 83.03  ? 420 VAL A O   1 
ATOM   2710 C  CB  . VAL A 1 422 ? 143.325 123.873 103.726 1.00 89.67  ? 420 VAL A CB  1 
ATOM   2711 C  CG1 . VAL A 1 422 ? 142.743 124.725 102.606 1.00 86.27  ? 420 VAL A CG1 1 
ATOM   2712 C  CG2 . VAL A 1 422 ? 143.034 122.398 103.478 1.00 85.68  ? 420 VAL A CG2 1 
ATOM   2713 N  N   . ILE A 1 423 ? 145.131 125.952 105.434 1.00 83.57  ? 421 ILE A N   1 
ATOM   2714 C  CA  . ILE A 1 423 ? 145.398 127.341 105.800 1.00 84.51  ? 421 ILE A CA  1 
ATOM   2715 C  C   . ILE A 1 423 ? 146.820 127.728 105.409 1.00 84.44  ? 421 ILE A C   1 
ATOM   2716 O  O   . ILE A 1 423 ? 147.056 128.800 104.839 1.00 80.65  ? 421 ILE A O   1 
ATOM   2717 C  CB  . ILE A 1 423 ? 145.149 127.558 107.305 1.00 80.67  ? 421 ILE A CB  1 
ATOM   2718 C  CG1 . ILE A 1 423 ? 143.730 127.114 107.681 1.00 78.62  ? 421 ILE A CG1 1 
ATOM   2719 C  CG2 . ILE A 1 423 ? 145.373 129.022 107.674 1.00 80.08  ? 421 ILE A CG2 1 
ATOM   2720 C  CD1 . ILE A 1 423 ? 143.434 127.169 109.166 1.00 80.65  ? 421 ILE A CD1 1 
ATOM   2721 N  N   . VAL A 1 424 ? 147.790 126.864 105.715 1.00 85.20  ? 422 VAL A N   1 
ATOM   2722 C  CA  . VAL A 1 424 ? 149.176 127.161 105.365 1.00 84.97  ? 422 VAL A CA  1 
ATOM   2723 C  C   . VAL A 1 424 ? 149.405 126.976 103.870 1.00 85.13  ? 422 VAL A C   1 
ATOM   2724 O  O   . VAL A 1 424 ? 150.106 127.773 103.235 1.00 83.88  ? 422 VAL A O   1 
ATOM   2725 C  CB  . VAL A 1 424 ? 150.139 126.300 106.205 1.00 83.30  ? 422 VAL A CB  1 
ATOM   2726 C  CG1 . VAL A 1 424 ? 149.921 124.814 105.944 1.00 84.33  ? 422 VAL A CG1 1 
ATOM   2727 C  CG2 . VAL A 1 424 ? 151.587 126.689 105.925 1.00 79.97  ? 422 VAL A CG2 1 
ATOM   2728 N  N   . LEU A 1 425 ? 148.827 125.926 103.283 1.00 87.40  ? 423 LEU A N   1 
ATOM   2729 C  CA  . LEU A 1 425 ? 149.038 125.670 101.861 1.00 87.74  ? 423 LEU A CA  1 
ATOM   2730 C  C   . LEU A 1 425 ? 148.471 126.795 101.004 1.00 87.70  ? 423 LEU A C   1 
ATOM   2731 O  O   . LEU A 1 425 ? 149.107 127.229 100.037 1.00 85.99  ? 423 LEU A O   1 
ATOM   2732 C  CB  . LEU A 1 425 ? 148.408 124.333 101.466 1.00 87.46  ? 423 LEU A CB  1 
ATOM   2733 C  CG  . LEU A 1 425 ? 149.117 123.024 101.841 1.00 85.71  ? 423 LEU A CG  1 
ATOM   2734 C  CD1 . LEU A 1 425 ? 148.600 121.895 100.965 1.00 85.07  ? 423 LEU A CD1 1 
ATOM   2735 C  CD2 . LEU A 1 425 ? 150.633 123.116 101.732 1.00 85.58  ? 423 LEU A CD2 1 
ATOM   2736 N  N   . SER A 1 426 ? 147.273 127.277 101.339 1.00 89.56  ? 424 SER A N   1 
ATOM   2737 C  CA  . SER A 1 426 ? 146.656 128.334 100.545 1.00 88.56  ? 424 SER A CA  1 
ATOM   2738 C  C   . SER A 1 426 ? 147.432 129.640 100.659 1.00 86.51  ? 424 SER A C   1 
ATOM   2739 O  O   . SER A 1 426 ? 147.663 130.321 99.653  1.00 85.91  ? 424 SER A O   1 
ATOM   2740 C  CB  . SER A 1 426 ? 145.205 128.536 100.982 1.00 88.40  ? 424 SER A CB  1 
ATOM   2741 O  OG  . SER A 1 426 ? 145.135 128.988 102.322 1.00 85.34  ? 424 SER A OG  1 
ATOM   2742 N  N   . ALA A 1 427 ? 147.845 130.006 101.874 1.00 86.41  ? 425 ALA A N   1 
ATOM   2743 C  CA  . ALA A 1 427 ? 148.509 131.290 102.076 1.00 87.15  ? 425 ALA A CA  1 
ATOM   2744 C  C   . ALA A 1 427 ? 149.802 131.375 101.274 1.00 87.25  ? 425 ALA A C   1 
ATOM   2745 O  O   . ALA A 1 427 ? 150.077 132.388 100.623 1.00 87.78  ? 425 ALA A O   1 
ATOM   2746 C  CB  . ALA A 1 427 ? 148.782 131.506 103.564 1.00 84.96  ? 425 ALA A CB  1 
ATOM   2747 N  N   . VAL A 1 428 ? 150.612 130.314 101.309 1.00 88.00  ? 426 VAL A N   1 
ATOM   2748 C  CA  . VAL A 1 428 ? 151.879 130.331 100.590 1.00 87.41  ? 426 VAL A CA  1 
ATOM   2749 C  C   . VAL A 1 428 ? 151.669 130.350 99.082  1.00 90.20  ? 426 VAL A C   1 
ATOM   2750 O  O   . VAL A 1 428 ? 152.592 130.700 98.336  1.00 90.94  ? 426 VAL A O   1 
ATOM   2751 C  CB  . VAL A 1 428 ? 152.744 129.126 101.011 1.00 90.29  ? 426 VAL A CB  1 
ATOM   2752 C  CG1 . VAL A 1 428 ? 152.053 127.813 100.665 1.00 87.37  ? 426 VAL A CG1 1 
ATOM   2753 C  CG2 . VAL A 1 428 ? 154.125 129.196 100.366 1.00 91.17  ? 426 VAL A CG2 1 
ATOM   2754 N  N   . GLY A 1 429 ? 150.476 129.999 98.609  1.00 88.12  ? 427 GLY A N   1 
ATOM   2755 C  CA  . GLY A 1 429 ? 150.205 129.982 97.185  1.00 87.04  ? 427 GLY A CA  1 
ATOM   2756 C  C   . GLY A 1 429 ? 150.405 128.616 96.563  1.00 89.49  ? 427 GLY A C   1 
ATOM   2757 O  O   . GLY A 1 429 ? 151.115 128.479 95.563  1.00 90.76  ? 427 GLY A O   1 
ATOM   2758 N  N   . LEU A 1 430 ? 149.783 127.599 97.150  1.00 91.99  ? 428 LEU A N   1 
ATOM   2759 C  CA  . LEU A 1 430 ? 149.883 126.227 96.683  1.00 91.15  ? 428 LEU A CA  1 
ATOM   2760 C  C   . LEU A 1 430 ? 148.494 125.626 96.542  1.00 90.20  ? 428 LEU A C   1 
ATOM   2761 O  O   . LEU A 1 430 ? 147.564 126.035 97.244  1.00 87.87  ? 428 LEU A O   1 
ATOM   2762 C  CB  . LEU A 1 430 ? 150.710 125.368 97.650  1.00 92.26  ? 428 LEU A CB  1 
ATOM   2763 C  CG  . LEU A 1 430 ? 152.223 125.586 97.641  1.00 92.58  ? 428 LEU A CG  1 
ATOM   2764 C  CD1 . LEU A 1 430 ? 152.868 124.903 98.835  1.00 91.28  ? 428 LEU A CD1 1 
ATOM   2765 C  CD2 . LEU A 1 430 ? 152.819 125.066 96.347  1.00 91.18  ? 428 LEU A CD2 1 
ATOM   2766 N  N   . PRO A 1 431 ? 148.319 124.657 95.643  1.00 94.88  ? 429 PRO A N   1 
ATOM   2767 C  CA  . PRO A 1 431 ? 147.010 124.005 95.523  1.00 95.99  ? 429 PRO A CA  1 
ATOM   2768 C  C   . PRO A 1 431 ? 146.600 123.357 96.836  1.00 94.50  ? 429 PRO A C   1 
ATOM   2769 O  O   . PRO A 1 431 ? 147.428 122.810 97.567  1.00 93.90  ? 429 PRO A O   1 
ATOM   2770 C  CB  . PRO A 1 431 ? 147.229 122.962 94.421  1.00 95.23  ? 429 PRO A CB  1 
ATOM   2771 C  CG  . PRO A 1 431 ? 148.397 123.458 93.647  1.00 95.43  ? 429 PRO A CG  1 
ATOM   2772 C  CD  . PRO A 1 431 ? 149.273 124.166 94.633  1.00 93.86  ? 429 PRO A CD  1 
ATOM   2773 N  N   . ALA A 1 432 ? 145.301 123.424 97.132  1.00 93.37  ? 430 ALA A N   1 
ATOM   2774 C  CA  . ALA A 1 432 ? 144.778 122.861 98.370  1.00 92.95  ? 430 ALA A CA  1 
ATOM   2775 C  C   . ALA A 1 432 ? 144.740 121.339 98.359  1.00 92.58  ? 430 ALA A C   1 
ATOM   2776 O  O   . ALA A 1 432 ? 144.512 120.737 99.415  1.00 92.25  ? 430 ALA A O   1 
ATOM   2777 C  CB  . ALA A 1 432 ? 143.375 123.405 98.638  1.00 91.76  ? 430 ALA A CB  1 
ATOM   2778 N  N   . GLU A 1 433 ? 144.952 120.706 97.208  1.00 94.84  ? 431 GLU A N   1 
ATOM   2779 C  CA  . GLU A 1 433 ? 144.919 119.255 97.096  1.00 94.70  ? 431 GLU A CA  1 
ATOM   2780 C  C   . GLU A 1 433 ? 146.294 118.617 97.234  1.00 94.09  ? 431 GLU A C   1 
ATOM   2781 O  O   . GLU A 1 433 ? 146.401 117.389 97.147  1.00 94.71  ? 431 GLU A O   1 
ATOM   2782 C  CB  . GLU A 1 433 ? 144.301 118.845 95.755  1.00 93.97  ? 431 GLU A CB  1 
ATOM   2783 C  CG  . GLU A 1 433 ? 142.930 119.447 95.491  1.00 96.53  ? 431 GLU A CG  1 
ATOM   2784 C  CD  . GLU A 1 433 ? 141.866 118.915 96.431  1.00 95.84  ? 431 GLU A CD  1 
ATOM   2785 O  OE1 . GLU A 1 433 ? 142.177 118.014 97.239  1.00 94.94  ? 431 GLU A OE1 1 
ATOM   2786 O  OE2 . GLU A 1 433 ? 140.716 119.398 96.363  1.00 94.45  ? 431 GLU A OE2 1 
ATOM   2787 N  N   . ASP A 1 434 ? 147.345 119.412 97.446  1.00 90.11  ? 432 ASP A N   1 
ATOM   2788 C  CA  . ASP A 1 434 ? 148.685 118.860 97.604  1.00 92.17  ? 432 ASP A CA  1 
ATOM   2789 C  C   . ASP A 1 434 ? 148.860 118.088 98.905  1.00 88.23  ? 432 ASP A C   1 
ATOM   2790 O  O   . ASP A 1 434 ? 149.882 117.414 99.069  1.00 84.62  ? 432 ASP A O   1 
ATOM   2791 C  CB  . ASP A 1 434 ? 149.723 119.981 97.529  1.00 91.90  ? 432 ASP A CB  1 
ATOM   2792 C  CG  . ASP A 1 434 ? 149.995 120.429 96.107  1.00 91.60  ? 432 ASP A CG  1 
ATOM   2793 O  OD1 . ASP A 1 434 ? 149.397 119.854 95.174  1.00 89.72  ? 432 ASP A OD1 1 
ATOM   2794 O  OD2 . ASP A 1 434 ? 150.810 121.357 95.921  1.00 90.98  ? 432 ASP A OD2 1 
ATOM   2795 N  N   . VAL A 1 435 ? 147.908 118.176 99.836  1.00 83.18  ? 433 VAL A N   1 
ATOM   2796 C  CA  . VAL A 1 435 ? 148.022 117.398 101.065 1.00 85.65  ? 433 VAL A CA  1 
ATOM   2797 C  C   . VAL A 1 435 ? 148.033 115.909 100.747 1.00 88.23  ? 433 VAL A C   1 
ATOM   2798 O  O   . VAL A 1 435 ? 148.635 115.113 101.478 1.00 88.93  ? 433 VAL A O   1 
ATOM   2799 C  CB  . VAL A 1 435 ? 146.881 117.761 102.037 1.00 85.47  ? 433 VAL A CB  1 
ATOM   2800 C  CG1 . VAL A 1 435 ? 147.006 116.971 103.331 1.00 82.95  ? 433 VAL A CG1 1 
ATOM   2801 C  CG2 . VAL A 1 435 ? 146.878 119.255 102.324 1.00 86.93  ? 433 VAL A CG2 1 
ATOM   2802 N  N   . THR A 1 436 ? 147.372 115.507 99.659  1.00 90.11  ? 434 THR A N   1 
ATOM   2803 C  CA  . THR A 1 436 ? 147.377 114.106 99.256  1.00 87.35  ? 434 THR A CA  1 
ATOM   2804 C  C   . THR A 1 436 ? 148.767 113.623 98.862  1.00 86.03  ? 434 THR A C   1 
ATOM   2805 O  O   . THR A 1 436 ? 149.011 112.412 98.854  1.00 82.41  ? 434 THR A O   1 
ATOM   2806 C  CB  . THR A 1 436 ? 146.409 113.882 98.092  1.00 88.11  ? 434 THR A CB  1 
ATOM   2807 O  OG1 . THR A 1 436 ? 146.879 114.581 96.933  1.00 89.16  ? 434 THR A OG1 1 
ATOM   2808 C  CG2 . THR A 1 436 ? 145.009 114.368 98.450  1.00 85.44  ? 434 THR A CG2 1 
ATOM   2809 N  N   . LEU A 1 437 ? 149.677 114.534 98.515  1.00 88.01  ? 435 LEU A N   1 
ATOM   2810 C  CA  . LEU A 1 437 ? 151.035 114.120 98.179  1.00 88.20  ? 435 LEU A CA  1 
ATOM   2811 C  C   . LEU A 1 437 ? 151.740 113.515 99.388  1.00 87.97  ? 435 LEU A C   1 
ATOM   2812 O  O   . LEU A 1 437 ? 152.488 112.540 99.257  1.00 86.58  ? 435 LEU A O   1 
ATOM   2813 C  CB  . LEU A 1 437 ? 151.830 115.307 97.629  1.00 86.80  ? 435 LEU A CB  1 
ATOM   2814 C  CG  . LEU A 1 437 ? 151.174 116.199 96.566  1.00 87.46  ? 435 LEU A CG  1 
ATOM   2815 C  CD1 . LEU A 1 437 ? 152.243 116.961 95.801  1.00 86.38  ? 435 LEU A CD1 1 
ATOM   2816 C  CD2 . LEU A 1 437 ? 150.314 115.397 95.593  1.00 87.46  ? 435 LEU A CD2 1 
ATOM   2817 N  N   . ILE A 1 438 ? 151.512 114.082 100.572 1.00 86.18  ? 436 ILE A N   1 
ATOM   2818 C  CA  . ILE A 1 438 ? 152.213 113.696 101.792 1.00 84.37  ? 436 ILE A CA  1 
ATOM   2819 C  C   . ILE A 1 438 ? 151.336 112.911 102.754 1.00 84.00  ? 436 ILE A C   1 
ATOM   2820 O  O   . ILE A 1 438 ? 151.822 112.501 103.817 1.00 83.71  ? 436 ILE A O   1 
ATOM   2821 C  CB  . ILE A 1 438 ? 152.806 114.927 102.503 1.00 84.87  ? 436 ILE A CB  1 
ATOM   2822 C  CG1 . ILE A 1 438 ? 151.692 115.863 102.974 1.00 82.48  ? 436 ILE A CG1 1 
ATOM   2823 C  CG2 . ILE A 1 438 ? 153.760 115.666 101.577 1.00 80.80  ? 436 ILE A CG2 1 
ATOM   2824 C  CD1 . ILE A 1 438 ? 151.872 116.346 104.384 1.00 82.22  ? 436 ILE A CD1 1 
ATOM   2825 N  N   . ILE A 1 439 ? 150.061 112.687 102.424 1.00 84.00  ? 437 ILE A N   1 
ATOM   2826 C  CA  . ILE A 1 439 ? 149.158 112.001 103.344 1.00 83.54  ? 437 ILE A CA  1 
ATOM   2827 C  C   . ILE A 1 439 ? 149.590 110.567 103.603 1.00 82.41  ? 437 ILE A C   1 
ATOM   2828 O  O   . ILE A 1 439 ? 149.219 109.987 104.629 1.00 82.53  ? 437 ILE A O   1 
ATOM   2829 C  CB  . ILE A 1 439 ? 147.717 112.028 102.798 1.00 83.63  ? 437 ILE A CB  1 
ATOM   2830 C  CG1 . ILE A 1 439 ? 146.752 111.395 103.799 1.00 83.81  ? 437 ILE A CG1 1 
ATOM   2831 C  CG2 . ILE A 1 439 ? 147.628 111.276 101.485 1.00 83.75  ? 437 ILE A CG2 1 
ATOM   2832 C  CD1 . ILE A 1 439 ? 145.449 112.145 103.927 1.00 82.65  ? 437 ILE A CD1 1 
ATOM   2833 N  N   . ALA A 1 440 ? 150.367 109.973 102.697 1.00 81.56  ? 438 ALA A N   1 
ATOM   2834 C  CA  . ALA A 1 440 ? 150.727 108.567 102.846 1.00 82.29  ? 438 ALA A CA  1 
ATOM   2835 C  C   . ALA A 1 440 ? 151.467 108.319 104.153 1.00 83.19  ? 438 ALA A C   1 
ATOM   2836 O  O   . ALA A 1 440 ? 151.193 107.337 104.852 1.00 82.76  ? 438 ALA A O   1 
ATOM   2837 C  CB  . ALA A 1 440 ? 151.577 108.117 101.659 1.00 80.97  ? 438 ALA A CB  1 
ATOM   2838 N  N   . VAL A 1 441 ? 152.406 109.201 104.505 1.00 76.01  ? 439 VAL A N   1 
ATOM   2839 C  CA  . VAL A 1 441 ? 153.226 109.008 105.697 1.00 76.33  ? 439 VAL A CA  1 
ATOM   2840 C  C   . VAL A 1 441 ? 152.760 109.852 106.876 1.00 75.15  ? 439 VAL A C   1 
ATOM   2841 O  O   . VAL A 1 441 ? 153.273 109.670 107.992 1.00 71.98  ? 439 VAL A O   1 
ATOM   2842 C  CB  . VAL A 1 441 ? 154.711 109.303 105.390 1.00 76.18  ? 439 VAL A CB  1 
ATOM   2843 C  CG1 . VAL A 1 441 ? 154.913 110.777 105.046 1.00 78.68  ? 439 VAL A CG1 1 
ATOM   2844 C  CG2 . VAL A 1 441 ? 155.609 108.879 106.545 1.00 74.60  ? 439 VAL A CG2 1 
ATOM   2845 N  N   . ASP A 1 442 ? 151.785 110.743 106.681 1.00 75.61  ? 440 ASP A N   1 
ATOM   2846 C  CA  . ASP A 1 442 ? 151.399 111.645 107.760 1.00 75.68  ? 440 ASP A CA  1 
ATOM   2847 C  C   . ASP A 1 442 ? 150.973 110.886 109.007 1.00 73.01  ? 440 ASP A C   1 
ATOM   2848 O  O   . ASP A 1 442 ? 151.077 111.415 110.119 1.00 74.07  ? 440 ASP A O   1 
ATOM   2849 C  CB  . ASP A 1 442 ? 150.268 112.564 107.306 1.00 74.20  ? 440 ASP A CB  1 
ATOM   2850 C  CG  . ASP A 1 442 ? 149.768 113.458 108.421 1.00 75.40  ? 440 ASP A CG  1 
ATOM   2851 O  OD1 . ASP A 1 442 ? 150.534 114.336 108.870 1.00 77.15  ? 440 ASP A OD1 1 
ATOM   2852 O  OD2 . ASP A 1 442 ? 148.612 113.278 108.856 1.00 78.42  ? 440 ASP A OD2 1 
ATOM   2853 N  N   . CYS A 1 443 ? 150.489 109.654 108.849 1.00 70.06  ? 441 CYS A N   1 
ATOM   2854 C  CA  . CYS A 1 443 ? 150.129 108.857 110.015 1.00 72.46  ? 441 CYS A CA  1 
ATOM   2855 C  C   . CYS A 1 443 ? 151.352 108.544 110.867 1.00 71.53  ? 441 CYS A C   1 
ATOM   2856 O  O   . CYS A 1 443 ? 151.298 108.635 112.099 1.00 74.37  ? 441 CYS A O   1 
ATOM   2857 C  CB  . CYS A 1 443 ? 149.440 107.572 109.570 1.00 74.82  ? 441 CYS A CB  1 
ATOM   2858 S  SG  . CYS A 1 443 ? 147.851 107.831 108.752 1.00 77.04  ? 441 CYS A SG  1 
ATOM   2859 N  N   . LEU A 1 444 ? 152.465 108.171 110.232 1.00 68.68  ? 442 LEU A N   1 
ATOM   2860 C  CA  . LEU A 1 444 ? 153.677 107.884 110.993 1.00 70.19  ? 442 LEU A CA  1 
ATOM   2861 C  C   . LEU A 1 444 ? 154.232 109.152 111.630 1.00 69.05  ? 442 LEU A C   1 
ATOM   2862 O  O   . LEU A 1 444 ? 154.635 109.140 112.798 1.00 68.11  ? 442 LEU A O   1 
ATOM   2863 C  CB  . LEU A 1 444 ? 154.719 107.225 110.089 1.00 72.20  ? 442 LEU A CB  1 
ATOM   2864 C  CG  . LEU A 1 444 ? 156.188 107.314 110.514 1.00 70.57  ? 442 LEU A CG  1 
ATOM   2865 C  CD1 . LEU A 1 444 ? 156.432 106.501 111.771 1.00 67.43  ? 442 LEU A CD1 1 
ATOM   2866 C  CD2 . LEU A 1 444 ? 157.079 106.827 109.391 1.00 70.25  ? 442 LEU A CD2 1 
ATOM   2867 N  N   . LEU A 1 445 ? 154.266 110.253 110.877 1.00 67.89  ? 443 LEU A N   1 
ATOM   2868 C  CA  . LEU A 1 445 ? 154.726 111.514 111.446 1.00 65.53  ? 443 LEU A CA  1 
ATOM   2869 C  C   . LEU A 1 445 ? 153.782 111.981 112.544 1.00 63.70  ? 443 LEU A C   1 
ATOM   2870 O  O   . LEU A 1 445 ? 154.226 112.426 113.608 1.00 68.69  ? 443 LEU A O   1 
ATOM   2871 C  CB  . LEU A 1 445 ? 154.846 112.576 110.353 1.00 66.01  ? 443 LEU A CB  1 
ATOM   2872 C  CG  . LEU A 1 445 ? 155.717 112.198 109.155 1.00 71.33  ? 443 LEU A CG  1 
ATOM   2873 C  CD1 . LEU A 1 445 ? 155.611 113.244 108.060 1.00 70.20  ? 443 LEU A CD1 1 
ATOM   2874 C  CD2 . LEU A 1 445 ? 157.161 112.021 109.584 1.00 72.94  ? 443 LEU A CD2 1 
ATOM   2875 N  N   . ASP A 1 446 ? 152.473 111.871 112.306 1.00 59.85  ? 444 ASP A N   1 
ATOM   2876 C  CA  . ASP A 1 446 ? 151.496 112.270 113.311 1.00 57.66  ? 444 ASP A CA  1 
ATOM   2877 C  C   . ASP A 1 446 ? 151.790 111.589 114.640 1.00 57.51  ? 444 ASP A C   1 
ATOM   2878 O  O   . ASP A 1 446 ? 151.675 112.206 115.704 1.00 64.39  ? 444 ASP A O   1 
ATOM   2879 C  CB  . ASP A 1 446 ? 150.084 111.945 112.825 1.00 66.33  ? 444 ASP A CB  1 
ATOM   2880 C  CG  . ASP A 1 446 ? 149.020 112.345 113.820 1.00 68.26  ? 444 ASP A CG  1 
ATOM   2881 O  OD1 . ASP A 1 446 ? 149.314 113.171 114.708 1.00 67.56  ? 444 ASP A OD1 1 
ATOM   2882 O  OD2 . ASP A 1 446 ? 147.885 111.834 113.716 1.00 68.39  ? 444 ASP A OD2 1 
ATOM   2883 N  N   . ARG A 1 447 ? 152.154 110.306 114.595 1.00 62.84  ? 445 ARG A N   1 
ATOM   2884 C  CA  . ARG A 1 447 ? 152.409 109.555 115.820 1.00 66.26  ? 445 ARG A CA  1 
ATOM   2885 C  C   . ARG A 1 447 ? 153.413 110.292 116.697 1.00 64.10  ? 445 ARG A C   1 
ATOM   2886 O  O   . ARG A 1 447 ? 153.209 110.447 117.906 1.00 63.34  ? 445 ARG A O   1 
ATOM   2887 C  CB  . ARG A 1 447 ? 152.919 108.153 115.476 1.00 65.65  ? 445 ARG A CB  1 
ATOM   2888 C  CG  . ARG A 1 447 ? 151.926 107.042 115.757 1.00 64.98  ? 445 ARG A CG  1 
ATOM   2889 C  CD  . ARG A 1 447 ? 150.825 106.976 114.717 1.00 65.41  ? 445 ARG A CD  1 
ATOM   2890 N  NE  . ARG A 1 447 ? 149.835 105.962 115.059 1.00 66.29  ? 445 ARG A NE  1 
ATOM   2891 C  CZ  . ARG A 1 447 ? 148.535 106.182 115.207 1.00 66.93  ? 445 ARG A CZ  1 
ATOM   2892 N  NH1 . ARG A 1 447 ? 147.957 107.274 114.734 1.00 66.32  ? 445 ARG A NH1 1 
ATOM   2893 N  NH2 . ARG A 1 447 ? 147.780 105.242 115.769 1.00 64.56  ? 445 ARG A NH2 1 
ATOM   2894 N  N   . PHE A 1 448 ? 154.509 110.757 116.097 1.00 60.90  ? 446 PHE A N   1 
ATOM   2895 C  CA  . PHE A 1 448 ? 155.571 111.399 116.858 1.00 55.19  ? 446 PHE A CA  1 
ATOM   2896 C  C   . PHE A 1 448 ? 155.229 112.842 117.200 1.00 60.06  ? 446 PHE A C   1 
ATOM   2897 O  O   . PHE A 1 448 ? 155.640 113.333 118.257 1.00 70.95  ? 446 PHE A O   1 
ATOM   2898 C  CB  . PHE A 1 448 ? 156.885 111.339 116.082 1.00 57.87  ? 446 PHE A CB  1 
ATOM   2899 C  CG  . PHE A 1 448 ? 157.445 109.953 115.953 1.00 63.34  ? 446 PHE A CG  1 
ATOM   2900 C  CD1 . PHE A 1 448 ? 158.254 109.428 116.944 1.00 64.48  ? 446 PHE A CD1 1 
ATOM   2901 C  CD2 . PHE A 1 448 ? 157.144 109.168 114.856 1.00 64.73  ? 446 PHE A CD2 1 
ATOM   2902 C  CE1 . PHE A 1 448 ? 158.764 108.152 116.836 1.00 62.54  ? 446 PHE A CE1 1 
ATOM   2903 C  CE2 . PHE A 1 448 ? 157.652 107.891 114.744 1.00 65.62  ? 446 PHE A CE2 1 
ATOM   2904 C  CZ  . PHE A 1 448 ? 158.463 107.384 115.733 1.00 64.44  ? 446 PHE A CZ  1 
ATOM   2905 N  N   . ARG A 1 449 ? 154.496 113.538 116.327 1.00 60.34  ? 447 ARG A N   1 
ATOM   2906 C  CA  . ARG A 1 449 ? 154.126 114.919 116.614 1.00 58.64  ? 447 ARG A CA  1 
ATOM   2907 C  C   . ARG A 1 449 ? 153.448 115.023 117.970 1.00 60.33  ? 447 ARG A C   1 
ATOM   2908 O  O   . ARG A 1 449 ? 153.755 115.913 118.769 1.00 65.16  ? 447 ARG A O   1 
ATOM   2909 C  CB  . ARG A 1 449 ? 153.190 115.463 115.536 1.00 62.23  ? 447 ARG A CB  1 
ATOM   2910 C  CG  . ARG A 1 449 ? 153.808 115.581 114.175 1.00 61.22  ? 447 ARG A CG  1 
ATOM   2911 C  CD  . ARG A 1 449 ? 152.997 116.490 113.280 1.00 63.51  ? 447 ARG A CD  1 
ATOM   2912 N  NE  . ARG A 1 449 ? 152.063 115.801 112.399 1.00 68.54  ? 447 ARG A NE  1 
ATOM   2913 C  CZ  . ARG A 1 449 ? 150.789 115.565 112.683 1.00 66.18  ? 447 ARG A CZ  1 
ATOM   2914 N  NH1 . ARG A 1 449 ? 150.254 115.940 113.834 1.00 62.01  ? 447 ARG A NH1 1 
ATOM   2915 N  NH2 . ARG A 1 449 ? 150.030 114.944 111.786 1.00 68.55  ? 447 ARG A NH2 1 
ATOM   2916 N  N   . THR A 1 450 ? 152.517 114.110 118.245 1.00 58.53  ? 448 THR A N   1 
ATOM   2917 C  CA  . THR A 1 450 ? 151.771 114.169 119.496 1.00 57.45  ? 448 THR A CA  1 
ATOM   2918 C  C   . THR A 1 450 ? 152.712 114.072 120.688 1.00 61.97  ? 448 THR A C   1 
ATOM   2919 O  O   . THR A 1 450 ? 152.591 114.836 121.651 1.00 64.90  ? 448 THR A O   1 
ATOM   2920 C  CB  . THR A 1 450 ? 150.732 113.052 119.539 1.00 58.14  ? 448 THR A CB  1 
ATOM   2921 O  OG1 . THR A 1 450 ? 149.991 113.043 118.313 1.00 60.45  ? 448 THR A OG1 1 
ATOM   2922 C  CG2 . THR A 1 450 ? 149.773 113.271 120.694 1.00 61.44  ? 448 THR A CG2 1 
ATOM   2923 N  N   . MET A 1 451 ? 153.656 113.130 120.643 1.00 56.41  ? 449 MET A N   1 
ATOM   2924 C  CA  . MET A 1 451 ? 154.615 113.005 121.734 1.00 54.04  ? 449 MET A CA  1 
ATOM   2925 C  C   . MET A 1 451 ? 155.297 114.341 121.998 1.00 59.18  ? 449 MET A C   1 
ATOM   2926 O  O   . MET A 1 451 ? 155.478 114.739 123.154 1.00 61.49  ? 449 MET A O   1 
ATOM   2927 C  CB  . MET A 1 451 ? 155.641 111.919 121.397 1.00 53.58  ? 449 MET A CB  1 
ATOM   2928 C  CG  . MET A 1 451 ? 156.898 111.907 122.265 1.00 57.42  ? 449 MET A CG  1 
ATOM   2929 S  SD  . MET A 1 451 ? 158.232 110.958 121.513 1.00 64.28  ? 449 MET A SD  1 
ATOM   2930 C  CE  . MET A 1 451 ? 159.493 112.219 121.343 1.00 58.74  ? 449 MET A CE  1 
ATOM   2931 N  N   . VAL A 1 452 ? 155.680 115.051 120.936 1.00 61.28  ? 450 VAL A N   1 
ATOM   2932 C  CA  . VAL A 1 452 ? 156.264 116.377 121.106 1.00 58.53  ? 450 VAL A CA  1 
ATOM   2933 C  C   . VAL A 1 452 ? 155.210 117.362 121.597 1.00 59.49  ? 450 VAL A C   1 
ATOM   2934 O  O   . VAL A 1 452 ? 155.500 118.248 122.409 1.00 64.63  ? 450 VAL A O   1 
ATOM   2935 C  CB  . VAL A 1 452 ? 156.909 116.846 119.789 1.00 54.98  ? 450 VAL A CB  1 
ATOM   2936 C  CG1 . VAL A 1 452 ? 157.525 118.226 119.953 1.00 62.45  ? 450 VAL A CG1 1 
ATOM   2937 C  CG2 . VAL A 1 452 ? 157.956 115.847 119.332 1.00 58.21  ? 450 VAL A CG2 1 
ATOM   2938 N  N   . ASN A 1 453 ? 153.975 117.230 121.110 1.00 59.22  ? 451 ASN A N   1 
ATOM   2939 C  CA  . ASN A 1 453 ? 152.916 118.145 121.524 1.00 57.95  ? 451 ASN A CA  1 
ATOM   2940 C  C   . ASN A 1 453 ? 152.647 118.025 123.018 1.00 55.02  ? 451 ASN A C   1 
ATOM   2941 O  O   . ASN A 1 453 ? 152.555 119.032 123.728 1.00 60.89  ? 451 ASN A O   1 
ATOM   2942 C  CB  . ASN A 1 453 ? 151.644 117.874 120.722 1.00 60.99  ? 451 ASN A CB  1 
ATOM   2943 C  CG  . ASN A 1 453 ? 151.766 118.308 119.276 1.00 58.62  ? 451 ASN A CG  1 
ATOM   2944 O  OD1 . ASN A 1 453 ? 152.821 118.762 118.840 1.00 57.13  ? 451 ASN A OD1 1 
ATOM   2945 N  ND2 . ASN A 1 453 ? 150.681 118.177 118.527 1.00 59.29  ? 451 ASN A ND2 1 
ATOM   2946 N  N   . VAL A 1 454 ? 152.512 116.794 123.515 1.00 55.42  ? 452 VAL A N   1 
ATOM   2947 C  CA  . VAL A 1 454 ? 152.299 116.597 124.944 1.00 58.91  ? 452 VAL A CA  1 
ATOM   2948 C  C   . VAL A 1 454 ? 153.569 116.922 125.719 1.00 60.03  ? 452 VAL A C   1 
ATOM   2949 O  O   . VAL A 1 454 ? 153.515 117.500 126.810 1.00 64.43  ? 452 VAL A O   1 
ATOM   2950 C  CB  . VAL A 1 454 ? 151.805 115.165 125.228 1.00 53.89  ? 452 VAL A CB  1 
ATOM   2951 C  CG1 . VAL A 1 454 ? 150.637 114.812 124.323 1.00 57.40  ? 452 VAL A CG1 1 
ATOM   2952 C  CG2 . VAL A 1 454 ? 152.926 114.147 125.069 1.00 55.33  ? 452 VAL A CG2 1 
ATOM   2953 N  N   . LEU A 1 455 ? 154.730 116.555 125.173 1.00 54.23  ? 453 LEU A N   1 
ATOM   2954 C  CA  . LEU A 1 455 ? 155.984 116.836 125.863 1.00 52.04  ? 453 LEU A CA  1 
ATOM   2955 C  C   . LEU A 1 455 ? 156.182 118.334 126.042 1.00 60.19  ? 453 LEU A C   1 
ATOM   2956 O  O   . LEU A 1 455 ? 156.604 118.789 127.112 1.00 65.27  ? 453 LEU A O   1 
ATOM   2957 C  CB  . LEU A 1 455 ? 157.154 116.228 125.091 1.00 54.60  ? 453 LEU A CB  1 
ATOM   2958 C  CG  . LEU A 1 455 ? 158.528 116.341 125.750 1.00 57.96  ? 453 LEU A CG  1 
ATOM   2959 C  CD1 . LEU A 1 455 ? 158.591 115.499 127.011 1.00 59.96  ? 453 LEU A CD1 1 
ATOM   2960 C  CD2 . LEU A 1 455 ? 159.615 115.931 124.775 1.00 60.76  ? 453 LEU A CD2 1 
ATOM   2961 N  N   . GLY A 1 456 ? 155.884 119.119 125.006 1.00 59.89  ? 454 GLY A N   1 
ATOM   2962 C  CA  . GLY A 1 456 ? 155.974 120.563 125.142 1.00 57.75  ? 454 GLY A CA  1 
ATOM   2963 C  C   . GLY A 1 456 ? 155.043 121.094 126.214 1.00 61.92  ? 454 GLY A C   1 
ATOM   2964 O  O   . GLY A 1 456 ? 155.431 121.923 127.039 1.00 65.60  ? 454 GLY A O   1 
ATOM   2965 N  N   . ASP A 1 457 ? 153.795 120.620 126.213 1.00 61.22  ? 455 ASP A N   1 
ATOM   2966 C  CA  . ASP A 1 457 ? 152.866 120.990 127.275 1.00 57.18  ? 455 ASP A CA  1 
ATOM   2967 C  C   . ASP A 1 457 ? 153.327 120.443 128.617 1.00 59.25  ? 455 ASP A C   1 
ATOM   2968 O  O   . ASP A 1 457 ? 153.246 121.135 129.638 1.00 60.12  ? 455 ASP A O   1 
ATOM   2969 C  CB  . ASP A 1 457 ? 151.463 120.481 126.949 1.00 58.59  ? 455 ASP A CB  1 
ATOM   2970 C  CG  . ASP A 1 457 ? 151.049 120.783 125.524 1.00 64.53  ? 455 ASP A CG  1 
ATOM   2971 O  OD1 . ASP A 1 457 ? 151.778 121.528 124.837 1.00 60.99  ? 455 ASP A OD1 1 
ATOM   2972 O  OD2 . ASP A 1 457 ? 149.995 120.272 125.090 1.00 64.47  ? 455 ASP A OD2 1 
ATOM   2973 N  N   . ALA A 1 458 ? 153.815 119.200 128.635 1.00 60.08  ? 456 ALA A N   1 
ATOM   2974 C  CA  . ALA A 1 458 ? 154.267 118.603 129.886 1.00 59.32  ? 456 ALA A CA  1 
ATOM   2975 C  C   . ALA A 1 458 ? 155.414 119.398 130.491 1.00 58.31  ? 456 ALA A C   1 
ATOM   2976 O  O   . ALA A 1 458 ? 155.442 119.634 131.704 1.00 65.01  ? 456 ALA A O   1 
ATOM   2977 C  CB  . ALA A 1 458 ? 154.689 117.154 129.651 1.00 64.12  ? 456 ALA A CB  1 
ATOM   2978 N  N   . PHE A 1 459 ? 156.373 119.817 129.664 1.00 58.60  ? 457 PHE A N   1 
ATOM   2979 C  CA  . PHE A 1 459 ? 157.455 120.656 130.167 1.00 60.33  ? 457 PHE A CA  1 
ATOM   2980 C  C   . PHE A 1 459 ? 156.941 122.019 130.606 1.00 58.89  ? 457 PHE A C   1 
ATOM   2981 O  O   . PHE A 1 459 ? 157.483 122.610 131.545 1.00 59.39  ? 457 PHE A O   1 
ATOM   2982 C  CB  . PHE A 1 459 ? 158.535 120.822 129.098 1.00 59.41  ? 457 PHE A CB  1 
ATOM   2983 C  CG  . PHE A 1 459 ? 159.574 119.738 129.108 1.00 59.84  ? 457 PHE A CG  1 
ATOM   2984 C  CD1 . PHE A 1 459 ? 160.335 119.498 130.238 1.00 61.64  ? 457 PHE A CD1 1 
ATOM   2985 C  CD2 . PHE A 1 459 ? 159.797 118.968 127.983 1.00 58.39  ? 457 PHE A CD2 1 
ATOM   2986 C  CE1 . PHE A 1 459 ? 161.291 118.506 130.247 1.00 63.32  ? 457 PHE A CE1 1 
ATOM   2987 C  CE2 . PHE A 1 459 ? 160.752 117.975 127.986 1.00 59.12  ? 457 PHE A CE2 1 
ATOM   2988 C  CZ  . PHE A 1 459 ? 161.500 117.744 129.119 1.00 63.79  ? 457 PHE A CZ  1 
ATOM   2989 N  N   . GLY A 1 460 ? 155.905 122.532 129.941 1.00 57.84  ? 458 GLY A N   1 
ATOM   2990 C  CA  . GLY A 1 460 ? 155.356 123.820 130.329 1.00 59.19  ? 458 GLY A CA  1 
ATOM   2991 C  C   . GLY A 1 460 ? 154.840 123.828 131.753 1.00 58.60  ? 458 GLY A C   1 
ATOM   2992 O  O   . GLY A 1 460 ? 154.973 124.824 132.466 1.00 62.37  ? 458 GLY A O   1 
ATOM   2993 N  N   . THR A 1 461 ? 154.242 122.718 132.185 1.00 56.82  ? 459 THR A N   1 
ATOM   2994 C  CA  . THR A 1 461 ? 153.738 122.641 133.551 1.00 54.68  ? 459 THR A CA  1 
ATOM   2995 C  C   . THR A 1 461 ? 154.865 122.837 134.556 1.00 55.84  ? 459 THR A C   1 
ATOM   2996 O  O   . THR A 1 461 ? 154.716 123.580 135.532 1.00 61.57  ? 459 THR A O   1 
ATOM   2997 C  CB  . THR A 1 461 ? 153.045 121.299 133.776 1.00 56.66  ? 459 THR A CB  1 
ATOM   2998 O  OG1 . THR A 1 461 ? 152.210 120.997 132.653 1.00 57.30  ? 459 THR A OG1 1 
ATOM   2999 C  CG2 . THR A 1 461 ? 152.180 121.359 135.013 1.00 61.89  ? 459 THR A CG2 1 
ATOM   3000 N  N   . GLY A 1 462 ? 156.003 122.179 134.332 1.00 57.18  ? 460 GLY A N   1 
ATOM   3001 C  CA  . GLY A 1 462 ? 157.137 122.358 135.223 1.00 59.47  ? 460 GLY A CA  1 
ATOM   3002 C  C   . GLY A 1 462 ? 157.718 123.758 135.155 1.00 61.01  ? 460 GLY A C   1 
ATOM   3003 O  O   . GLY A 1 462 ? 158.072 124.343 136.182 1.00 62.73  ? 460 GLY A O   1 
ATOM   3004 N  N   . ILE A 1 463 ? 157.830 124.311 133.947 1.00 61.51  ? 461 ILE A N   1 
ATOM   3005 C  CA  . ILE A 1 463 ? 158.397 125.647 133.788 1.00 60.14  ? 461 ILE A CA  1 
ATOM   3006 C  C   . ILE A 1 463 ? 157.485 126.688 134.423 1.00 63.02  ? 461 ILE A C   1 
ATOM   3007 O  O   . ILE A 1 463 ? 157.934 127.547 135.191 1.00 67.12  ? 461 ILE A O   1 
ATOM   3008 C  CB  . ILE A 1 463 ? 158.645 125.944 132.297 1.00 58.32  ? 461 ILE A CB  1 
ATOM   3009 C  CG1 . ILE A 1 463 ? 159.870 125.173 131.803 1.00 60.61  ? 461 ILE A CG1 1 
ATOM   3010 C  CG2 . ILE A 1 463 ? 158.833 127.440 132.052 1.00 60.43  ? 461 ILE A CG2 1 
ATOM   3011 C  CD1 . ILE A 1 463 ? 159.966 125.077 130.298 1.00 59.81  ? 461 ILE A CD1 1 
ATOM   3012 N  N   . VAL A 1 464 ? 156.188 126.627 134.115 1.00 62.38  ? 462 VAL A N   1 
ATOM   3013 C  CA  . VAL A 1 464 ? 155.255 127.619 134.638 1.00 60.02  ? 462 VAL A CA  1 
ATOM   3014 C  C   . VAL A 1 464 ? 155.157 127.508 136.153 1.00 60.27  ? 462 VAL A C   1 
ATOM   3015 O  O   . VAL A 1 464 ? 155.069 128.520 136.859 1.00 62.57  ? 462 VAL A O   1 
ATOM   3016 C  CB  . VAL A 1 464 ? 153.881 127.461 133.962 1.00 55.51  ? 462 VAL A CB  1 
ATOM   3017 C  CG1 . VAL A 1 464 ? 152.816 128.280 134.682 1.00 59.11  ? 462 VAL A CG1 1 
ATOM   3018 C  CG2 . VAL A 1 464 ? 153.966 127.865 132.502 1.00 58.99  ? 462 VAL A CG2 1 
ATOM   3019 N  N   . GLU A 1 465 ? 155.166 126.282 136.679 1.00 56.40  ? 463 GLU A N   1 
ATOM   3020 C  CA  . GLU A 1 465 ? 155.090 126.102 138.124 1.00 60.58  ? 463 GLU A CA  1 
ATOM   3021 C  C   . GLU A 1 465 ? 156.291 126.732 138.819 1.00 65.02  ? 463 GLU A C   1 
ATOM   3022 O  O   . GLU A 1 465 ? 156.144 127.383 139.859 1.00 63.00  ? 463 GLU A O   1 
ATOM   3023 C  CB  . GLU A 1 465 ? 154.995 124.613 138.459 1.00 59.75  ? 463 GLU A CB  1 
ATOM   3024 C  CG  . GLU A 1 465 ? 154.916 124.299 139.949 1.00 61.38  ? 463 GLU A CG  1 
ATOM   3025 C  CD  . GLU A 1 465 ? 155.729 123.079 140.334 1.00 65.54  ? 463 GLU A CD  1 
ATOM   3026 O  OE1 . GLU A 1 465 ? 156.877 122.951 139.860 1.00 65.93  ? 463 GLU A OE1 1 
ATOM   3027 O  OE2 . GLU A 1 465 ? 155.220 122.248 141.113 1.00 67.05  ? 463 GLU A OE2 1 
ATOM   3028 N  N   . LYS A 1 466 ? 157.489 126.548 138.261 1.00 64.36  ? 464 LYS A N   1 
ATOM   3029 C  CA  . LYS A 1 466 ? 158.688 127.094 138.888 1.00 61.38  ? 464 LYS A CA  1 
ATOM   3030 C  C   . LYS A 1 466 ? 158.629 128.614 138.950 1.00 66.55  ? 464 LYS A C   1 
ATOM   3031 O  O   . LYS A 1 466 ? 158.905 129.217 139.993 1.00 71.25  ? 464 LYS A O   1 
ATOM   3032 C  CB  . LYS A 1 466 ? 159.928 126.634 138.122 1.00 60.72  ? 464 LYS A CB  1 
ATOM   3033 C  CG  . LYS A 1 466 ? 161.213 127.359 138.497 1.00 62.17  ? 464 LYS A CG  1 
ATOM   3034 C  CD  . LYS A 1 466 ? 161.625 127.064 139.927 1.00 66.80  ? 464 LYS A CD  1 
ATOM   3035 C  CE  . LYS A 1 466 ? 163.080 127.425 140.166 1.00 63.76  ? 464 LYS A CE  1 
ATOM   3036 N  NZ  . LYS A 1 466 ? 163.410 128.782 139.654 1.00 66.16  ? 464 LYS A NZ  1 
ATOM   3037 N  N   . LEU A 1 467 ? 158.275 129.255 137.834 1.00 63.72  ? 465 LEU A N   1 
ATOM   3038 C  CA  . LEU A 1 467 ? 158.208 130.711 137.816 1.00 64.54  ? 465 LEU A CA  1 
ATOM   3039 C  C   . LEU A 1 467 ? 157.026 131.227 138.622 1.00 65.45  ? 465 LEU A C   1 
ATOM   3040 O  O   . LEU A 1 467 ? 157.097 132.320 139.195 1.00 66.83  ? 465 LEU A O   1 
ATOM   3041 C  CB  . LEU A 1 467 ? 158.126 131.212 136.376 1.00 62.11  ? 465 LEU A CB  1 
ATOM   3042 C  CG  . LEU A 1 467 ? 159.275 130.817 135.449 1.00 64.78  ? 465 LEU A CG  1 
ATOM   3043 C  CD1 . LEU A 1 467 ? 159.008 131.302 134.036 1.00 63.68  ? 465 LEU A CD1 1 
ATOM   3044 C  CD2 . LEU A 1 467 ? 160.589 131.381 135.965 1.00 68.28  ? 465 LEU A CD2 1 
ATOM   3045 N  N   . SER A 1 468 ? 155.937 130.463 138.683 1.00 68.07  ? 466 SER A N   1 
ATOM   3046 C  CA  . SER A 1 468 ? 154.756 130.840 139.444 1.00 67.26  ? 466 SER A CA  1 
ATOM   3047 C  C   . SER A 1 468 ? 154.838 130.397 140.900 1.00 67.15  ? 466 SER A C   1 
ATOM   3048 O  O   . SER A 1 468 ? 153.799 130.245 141.552 1.00 65.77  ? 466 SER A O   1 
ATOM   3049 C  CB  . SER A 1 468 ? 153.504 130.255 138.790 1.00 69.62  ? 466 SER A CB  1 
ATOM   3050 O  OG  . SER A 1 468 ? 153.464 130.558 137.407 1.00 69.94  ? 466 SER A OG  1 
ATOM   3051 N  N   . LYS A 1 469 ? 156.048 130.184 141.419 1.00 69.53  ? 467 LYS A N   1 
ATOM   3052 C  CA  . LYS A 1 469 ? 156.194 129.726 142.796 1.00 71.11  ? 467 LYS A CA  1 
ATOM   3053 C  C   . LYS A 1 469 ? 155.624 130.741 143.777 1.00 72.54  ? 467 LYS A C   1 
ATOM   3054 O  O   . LYS A 1 469 ? 154.938 130.371 144.737 1.00 70.15  ? 467 LYS A O   1 
ATOM   3055 C  CB  . LYS A 1 469 ? 157.669 129.455 143.096 1.00 69.23  ? 467 LYS A CB  1 
ATOM   3056 C  CG  . LYS A 1 469 ? 157.953 128.990 144.515 1.00 70.46  ? 467 LYS A CG  1 
ATOM   3057 C  CD  . LYS A 1 469 ? 159.447 128.859 144.754 1.00 70.92  ? 467 LYS A CD  1 
ATOM   3058 C  CE  . LYS A 1 469 ? 159.750 128.421 146.176 1.00 70.84  ? 467 LYS A CE  1 
ATOM   3059 N  NZ  . LYS A 1 469 ? 161.213 128.346 146.434 1.00 70.12  ? 467 LYS A NZ  1 
ATOM   3060 N  N   . LYS A 1 470 ? 155.896 132.028 143.554 1.00 74.08  ? 468 LYS A N   1 
ATOM   3061 C  CA  . LYS A 1 470 ? 155.389 133.054 144.460 1.00 73.31  ? 468 LYS A CA  1 
ATOM   3062 C  C   . LYS A 1 470 ? 153.866 133.067 144.475 1.00 72.16  ? 468 LYS A C   1 
ATOM   3063 O  O   . LYS A 1 470 ? 153.249 133.172 145.541 1.00 70.64  ? 468 LYS A O   1 
ATOM   3064 C  CB  . LYS A 1 470 ? 155.932 134.425 144.059 1.00 74.76  ? 468 LYS A CB  1 
ATOM   3065 C  CG  . LYS A 1 470 ? 156.675 135.143 145.175 1.00 73.87  ? 468 LYS A CG  1 
ATOM   3066 C  CD  . LYS A 1 470 ? 157.377 136.399 144.676 1.00 74.50  ? 468 LYS A CD  1 
ATOM   3067 C  CE  . LYS A 1 470 ? 158.605 136.068 143.839 1.00 75.85  ? 468 LYS A CE  1 
ATOM   3068 N  NZ  . LYS A 1 470 ? 159.300 137.291 143.355 1.00 72.56  ? 468 LYS A NZ  1 
ATOM   3069 N  N   . GLU A 1 471 ? 153.242 132.961 143.301 1.00 71.70  ? 469 GLU A N   1 
ATOM   3070 C  CA  . GLU A 1 471 ? 151.785 132.972 143.240 1.00 69.71  ? 469 GLU A CA  1 
ATOM   3071 C  C   . GLU A 1 471 ? 151.197 131.775 143.974 1.00 70.99  ? 469 GLU A C   1 
ATOM   3072 O  O   . GLU A 1 471 ? 150.203 131.906 144.696 1.00 69.94  ? 469 GLU A O   1 
ATOM   3073 C  CB  . GLU A 1 471 ? 151.325 132.988 141.783 1.00 69.92  ? 469 GLU A CB  1 
ATOM   3074 C  CG  . GLU A 1 471 ? 151.481 134.337 141.104 1.00 72.21  ? 469 GLU A CG  1 
ATOM   3075 C  CD  . GLU A 1 471 ? 152.918 134.646 140.742 1.00 75.03  ? 469 GLU A CD  1 
ATOM   3076 O  OE1 . GLU A 1 471 ? 153.639 135.204 141.595 1.00 71.08  ? 469 GLU A OE1 1 
ATOM   3077 O  OE2 . GLU A 1 471 ? 153.326 134.333 139.604 1.00 75.35  ? 469 GLU A OE2 1 
ATOM   3078 N  N   . LEU A 1 472 ? 151.796 130.596 143.798 1.00 72.00  ? 470 LEU A N   1 
ATOM   3079 C  CA  . LEU A 1 472 ? 151.309 129.413 144.496 1.00 68.67  ? 470 LEU A CA  1 
ATOM   3080 C  C   . LEU A 1 472 ? 151.510 129.529 146.000 1.00 72.38  ? 470 LEU A C   1 
ATOM   3081 O  O   . LEU A 1 472 ? 150.682 129.036 146.775 1.00 72.83  ? 470 LEU A O   1 
ATOM   3082 C  CB  . LEU A 1 472 ? 152.015 128.165 143.970 1.00 68.41  ? 470 LEU A CB  1 
ATOM   3083 C  CG  . LEU A 1 472 ? 151.778 127.806 142.503 1.00 68.98  ? 470 LEU A CG  1 
ATOM   3084 C  CD1 . LEU A 1 472 ? 152.602 126.587 142.135 1.00 69.27  ? 470 LEU A CD1 1 
ATOM   3085 C  CD2 . LEU A 1 472 ? 150.304 127.561 142.222 1.00 69.16  ? 470 LEU A CD2 1 
ATOM   3086 N  N   . GLU A 1 473 ? 152.600 130.168 146.432 1.00 76.04  ? 471 GLU A N   1 
ATOM   3087 C  CA  . GLU A 1 473 ? 152.859 130.298 147.862 1.00 75.53  ? 471 GLU A CA  1 
ATOM   3088 C  C   . GLU A 1 473 ? 151.756 131.090 148.550 1.00 75.79  ? 471 GLU A C   1 
ATOM   3089 O  O   . GLU A 1 473 ? 151.319 130.734 149.651 1.00 72.90  ? 471 GLU A O   1 
ATOM   3090 C  CB  . GLU A 1 473 ? 154.219 130.960 148.087 1.00 72.75  ? 471 GLU A CB  1 
ATOM   3091 C  CG  . GLU A 1 473 ? 154.529 131.268 149.547 1.00 73.52  ? 471 GLU A CG  1 
ATOM   3092 C  CD  . GLU A 1 473 ? 154.217 132.703 149.935 1.00 77.95  ? 471 GLU A CD  1 
ATOM   3093 O  OE1 . GLU A 1 473 ? 153.722 133.466 149.079 1.00 79.95  ? 471 GLU A OE1 1 
ATOM   3094 O  OE2 . GLU A 1 473 ? 154.470 133.068 151.102 1.00 76.39  ? 471 GLU A OE2 1 
ATOM   3095 N  N   . GLN A 1 474 ? 151.292 132.167 147.920 1.00 76.16  ? 472 GLN A N   1 
ATOM   3096 C  CA  . GLN A 1 474 ? 150.228 132.984 148.487 1.00 75.79  ? 472 GLN A CA  1 
ATOM   3097 C  C   . GLN A 1 474 ? 148.841 132.430 148.195 1.00 75.29  ? 472 GLN A C   1 
ATOM   3098 O  O   . GLN A 1 474 ? 147.853 133.009 148.658 1.00 74.94  ? 472 GLN A O   1 
ATOM   3099 C  CB  . GLN A 1 474 ? 150.324 134.419 147.963 1.00 77.92  ? 472 GLN A CB  1 
ATOM   3100 C  CG  . GLN A 1 474 ? 150.099 134.559 146.468 1.00 75.61  ? 472 GLN A CG  1 
ATOM   3101 C  CD  . GLN A 1 474 ? 150.574 135.894 145.933 1.00 77.88  ? 472 GLN A CD  1 
ATOM   3102 O  OE1 . GLN A 1 474 ? 151.760 136.214 145.994 1.00 76.85  ? 472 GLN A OE1 1 
ATOM   3103 N  NE2 . GLN A 1 474 ? 149.645 136.685 145.407 1.00 76.76  ? 472 GLN A NE2 1 
ATOM   3104 N  N   . MET A 1 475 ? 148.739 131.335 147.441 1.00 72.67  ? 473 MET A N   1 
ATOM   3105 C  CA  . MET A 1 475 ? 147.456 130.681 147.221 1.00 73.56  ? 473 MET A CA  1 
ATOM   3106 C  C   . MET A 1 475 ? 147.146 129.627 148.273 1.00 74.59  ? 473 MET A C   1 
ATOM   3107 O  O   . MET A 1 475 ? 145.974 129.438 148.617 1.00 76.19  ? 473 MET A O   1 
ATOM   3108 C  CB  . MET A 1 475 ? 147.419 130.028 145.839 1.00 75.15  ? 473 MET A CB  1 
ATOM   3109 C  CG  . MET A 1 475 ? 146.945 130.949 144.734 1.00 75.03  ? 473 MET A CG  1 
ATOM   3110 S  SD  . MET A 1 475 ? 146.986 130.132 143.133 1.00 90.74  ? 473 MET A SD  1 
ATOM   3111 C  CE  . MET A 1 475 ? 145.345 129.421 143.109 1.00 76.61  ? 473 MET A CE  1 
ATOM   3112 N  N   . ASP A 1 476 ? 148.162 128.931 148.790 1.00 78.31  ? 474 ASP A N   1 
ATOM   3113 C  CA  . ASP A 1 476 ? 147.910 127.956 149.845 1.00 81.17  ? 474 ASP A CA  1 
ATOM   3114 C  C   . ASP A 1 476 ? 147.313 128.633 151.070 1.00 82.17  ? 474 ASP A C   1 
ATOM   3115 O  O   . ASP A 1 476 ? 146.387 128.102 151.694 1.00 84.18  ? 474 ASP A O   1 
ATOM   3116 C  CB  . ASP A 1 476 ? 149.200 127.218 150.205 1.00 82.46  ? 474 ASP A CB  1 
ATOM   3117 C  CG  . ASP A 1 476 ? 150.297 128.152 150.676 1.00 85.33  ? 474 ASP A CG  1 
ATOM   3118 O  OD1 . ASP A 1 476 ? 150.095 128.848 151.692 1.00 85.61  ? 474 ASP A OD1 1 
ATOM   3119 O  OD2 . ASP A 1 476 ? 151.367 128.183 150.032 1.00 84.23  ? 474 ASP A OD2 1 
ATOM   3120 N  N   . VAL A 1 477 ? 147.829 129.806 151.428 1.00 77.53  ? 475 VAL A N   1 
ATOM   3121 C  CA  . VAL A 1 477 ? 147.207 130.660 152.433 1.00 75.33  ? 475 VAL A CA  1 
ATOM   3122 C  C   . VAL A 1 477 ? 146.235 131.575 151.691 1.00 78.68  ? 475 VAL A C   1 
ATOM   3123 O  O   . VAL A 1 477 ? 146.633 132.534 151.030 1.00 77.45  ? 475 VAL A O   1 
ATOM   3124 C  CB  . VAL A 1 477 ? 148.249 131.425 153.257 1.00 75.62  ? 475 VAL A CB  1 
ATOM   3125 C  CG1 . VAL A 1 477 ? 149.039 132.436 152.418 1.00 77.36  ? 475 VAL A CG1 1 
ATOM   3126 C  CG2 . VAL A 1 477 ? 147.578 132.124 154.431 1.00 77.83  ? 475 VAL A CG2 1 
ATOM   3127 N  N   . SER A 1 478 ? 144.951 131.242 151.760 1.00 81.28  ? 476 SER A N   1 
ATOM   3128 C  CA  . SER A 1 478 ? 143.928 131.973 151.023 1.00 81.97  ? 476 SER A CA  1 
ATOM   3129 C  C   . SER A 1 478 ? 143.900 133.442 151.430 1.00 81.00  ? 476 SER A C   1 
ATOM   3130 O  O   . SER A 1 478 ? 143.939 134.332 150.579 1.00 81.22  ? 476 SER A O   1 
ATOM   3131 C  CB  . SER A 1 478 ? 142.555 131.339 151.248 1.00 81.27  ? 476 SER A CB  1 
ATOM   3132 O  OG  . SER A 1 478 ? 142.591 129.945 150.995 1.00 78.82  ? 476 SER A OG  1 
HETATM 3133 N  N   . CYS B 2 .   ? 147.732 114.904 115.732 1.00 60.72  ? 600 CYS A N   1 
HETATM 3134 C  CA  . CYS B 2 .   ? 148.261 115.949 116.597 1.00 65.91  ? 600 CYS A CA  1 
HETATM 3135 C  C   . CYS B 2 .   ? 147.798 115.737 118.032 1.00 68.22  ? 600 CYS A C   1 
HETATM 3136 O  O   . CYS B 2 .   ? 148.452 116.160 118.984 1.00 70.54  ? 600 CYS A O   1 
HETATM 3137 C  CB  . CYS B 2 .   ? 147.822 117.327 116.105 1.00 63.25  ? 600 CYS A CB  1 
HETATM 3138 S  SG  . CYS B 2 .   ? 148.483 117.783 114.488 1.00 71.52  ? 600 CYS A SG  1 
HETATM 3139 O  OXT . CYS B 2 .   ? 146.754 115.134 118.272 1.00 64.87  ? 600 CYS A OXT 1 
HETATM 3140 NA NA  . NA  C 3 .   ? 149.393 120.481 123.010 1.00 54.38  ? 601 NA  A NA  1 
HETATM 3141 NA NA  . NA  D 3 .   ? 146.167 123.309 117.922 1.00 74.96  ? 602 NA  A NA  1 
HETATM 3142 NA NA  . NA  E 3 .   ? 154.374 126.162 121.939 1.00 75.55  ? 603 NA  A NA  1 
HETATM 3143 HG HG  . HG  F 4 .   ? 148.814 105.127 110.764 1.00 211.09 ? 604 HG  A HG  1 
# 
