data_9D6A
# 
_entry.id   9D6A 
# 
_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   9D6A         pdb_00009d6a 10.2210/pdb9d6a/pdb 
WWPDB D_1000287369 ?            ?                   
EMDB  EMD-46591    ?            ?                   
# 
_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                        9D6A 
_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-46591 
_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 ? ? ? ? 
5 water       nat water                                 18.015    9 ? ? ? ? 
# 
_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  
5 water              HOH 
# 
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 
HOH non-polymer         . WATER              ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE         ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE            ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE             ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE         ? 'C5 H11 N O2 S'  149.211 
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 ?   ?   ?   A . n 
A 1 474 GLN 474 472 ?   ?   ?   A . n 
A 1 475 MET 475 473 ?   ?   ?   A . n 
A 1 476 ASP 476 474 ?   ?   ?   A . n 
A 1 477 VAL 477 475 ?   ?   ?   A . n 
A 1 478 SER 478 476 ?   ?   ?   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 . 
G 5 HOH 1 701 612 HOH HOH A . 
G 5 HOH 2 702 611 HOH HOH A . 
G 5 HOH 3 703 606 HOH HOH A . 
G 5 HOH 4 704 609 HOH HOH A . 
G 5 HOH 5 705 607 HOH HOH A . 
G 5 HOH 6 706 613 HOH HOH A . 
G 5 HOH 7 707 610 HOH HOH A . 
G 5 HOH 8 708 608 HOH HOH A . 
G 5 HOH 9 709 605 HOH HOH 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                   9D6A 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9D6A 
_struct.title                        
'Human excitatory amino acid transporter 3 (EAAT3) with bound L-Cysteine in an intermediate outward facing state' 
_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        9D6A 
_struct_keywords.text            'human EAAT3, Cysteine, iOFS-star, PROTEIN TRANSPORT' 
_struct_keywords.pdbx_keywords   'PROTEIN TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
# 
_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              9D6A 
_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 9D6A GLY A 1   ? UNP P43005 ?   ?   'expression tag'      -1  1  
1 9D6A PRO A 2   ? UNP P43005 ?   ?   'expression tag'      0   2  
1 9D6A ALA A 11  ? UNP P43005 CYS 9   'engineered mutation' 9   3  
1 9D6A ALA A 102 ? UNP P43005 CYS 100 'engineered mutation' 100 4  
1 9D6A ALA A 160 ? UNP P43005 CYS 158 'engineered mutation' 158 5  
1 9D6A THR A 180 ? UNP P43005 ASN 178 'engineered mutation' 178 6  
1 9D6A THR A 197 ? UNP P43005 ASN 195 'engineered mutation' 195 7  
1 9D6A ALA A 221 ? UNP P43005 CYS 219 'engineered mutation' 219 8  
1 9D6A TRP A 258 ? UNP P43005 CYS 256 'engineered mutation' 256 9  
1 9D6A CYS A 271 ? UNP P43005 LYS 269 'engineered mutation' 269 10 
1 9D6A 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,G 
# 
_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  ? ILE A 68  ? ALA A 53  ILE A 66  1 ? 14 
HELX_P HELX_P4  AA4 ILE A 68  ? LEU A 84  ? ILE A 66  LEU A 82  1 ? 17 
HELX_P HELX_P5  AA5 VAL A 88  ? LYS A 119 ? VAL A 86  LYS A 117 1 ? 32 
HELX_P HELX_P6  AA6 THR A 140 ? PHE A 152 ? THR A 138 PHE A 150 1 ? 13 
HELX_P HELX_P7  AA7 ASN A 155 ? ALA A 160 ? ASN A 153 ALA A 158 1 ? 6  
HELX_P HELX_P8  AA8 ASN A 213 ? MET A 231 ? ASN A 211 MET A 229 1 ? 19 
HELX_P HELX_P9  AA9 GLY A 235 ? VAL A 275 ? GLY A 233 VAL A 273 1 ? 41 
HELX_P HELX_P10 AB1 TRP A 278 ? LEU A 284 ? TRP A 276 LEU A 282 1 ? 7  
HELX_P HELX_P11 AB2 LEU A 284 ? VAL A 301 ? LEU A 282 VAL A 299 1 ? 18 
HELX_P HELX_P12 AB3 VAL A 301 ? VAL A 311 ? VAL A 299 VAL A 309 1 ? 11 
HELX_P HELX_P13 AB4 ASN A 314 ? MET A 322 ? ASN A 312 MET A 320 1 ? 9  
HELX_P HELX_P14 AB5 MET A 322 ? SER A 333 ? MET A 320 SER A 331 1 ? 12 
HELX_P HELX_P15 AB6 THR A 338 ? GLU A 348 ? THR A 336 GLU A 346 1 ? 11 
HELX_P HELX_P16 AB7 ASP A 353 ? ASN A 368 ? ASP A 351 ASN A 366 1 ? 16 
HELX_P HELX_P17 AB8 MET A 369 ? ASN A 387 ? MET A 367 ASN A 385 1 ? 19 
HELX_P HELX_P18 AB9 GLY A 392 ? ALA A 410 ? GLY A 390 ALA A 408 1 ? 19 
HELX_P HELX_P19 AC1 GLN A 415 ? THR A 420 ? GLN A 413 THR A 418 1 ? 6  
HELX_P HELX_P20 AC2 THR A 420 ? VAL A 428 ? THR A 418 VAL A 426 1 ? 9  
HELX_P HELX_P21 AC3 PRO A 431 ? ILE A 438 ? PRO A 429 ILE A 436 5 ? 8  
HELX_P HELX_P22 AC4 VAL A 441 ? SER A 468 ? VAL A 439 SER A 466 1 ? 28 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 271 SG  ? ? ? 1_555 A CYS 443 SG ? ? A CYS 269 A CYS 441 1_555 ? ? ? ? ? ? ? 2.900 ? ? 
metalc1  metalc ? ? A TYR 100 O   ? ? ? 1_555 E NA  .   NA ? ? A TYR 98  A NA  603 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc2  metalc ? ? A THR 103 OG1 ? ? ? 1_555 E NA  .   NA ? ? A THR 101 A NA  603 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc3  metalc ? ? A THR 104 OG1 ? ? ? 1_555 E NA  .   NA ? ? A THR 102 A NA  603 1_555 ? ? ? ? ? ? ? 2.151 ? ? 
metalc4  metalc ? ? A CYS 271 SG  ? ? ? 1_555 F HG  .   HG ? ? A CYS 269 A HG  604 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc5  metalc ? ? A GLY 364 O   ? ? ? 1_555 C NA  .   NA ? ? A GLY 362 A NA  601 1_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc6  metalc ? ? A THR 366 O   ? ? ? 1_555 D NA  .   NA ? ? A THR 364 A NA  602 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc7  metalc ? ? A ASN 368 O   ? ? ? 1_555 C NA  .   NA ? ? A ASN 366 A NA  601 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc8  metalc ? ? A ASN 368 OD1 ? ? ? 1_555 E NA  .   NA ? ? A ASN 366 A NA  603 1_555 ? ? ? ? ? ? ? 2.071 ? ? 
metalc9  metalc ? ? A ASP 370 OD1 ? ? ? 1_555 E NA  .   NA ? ? A ASP 368 A NA  603 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc10 metalc ? ? A SER 407 O   ? ? ? 1_555 D NA  .   NA ? ? A SER 405 A NA  602 1_555 ? ? ? ? ? ? ? 2.154 ? ? 
metalc11 metalc ? ? A ILE 408 O   ? ? ? 1_555 D NA  .   NA ? ? A ILE 406 A NA  602 1_555 ? ? ? ? ? ? ? 2.921 ? ? 
metalc12 metalc ? ? A ALA 410 O   ? ? ? 1_555 D NA  .   NA ? ? A ALA 408 A NA  602 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc13 metalc ? ? A CYS 443 SG  ? ? ? 1_555 F HG  .   HG ? ? A CYS 441 A HG  604 1_555 ? ? ? ? ? ? ? 2.721 ? ? 
metalc14 metalc ? ? A ASN 453 O   ? ? ? 1_555 C NA  .   NA ? ? A ASN 451 A NA  601 1_555 ? ? ? ? ? ? ? 2.619 ? ? 
metalc15 metalc ? ? A ASP 457 OD1 ? ? ? 1_555 C NA  .   NA ? ? A ASP 455 A NA  601 1_555 ? ? ? ? ? ? ? 2.774 ? ? 
metalc16 metalc ? ? A ASP 457 OD2 ? ? ? 1_555 C NA  .   NA ? ? A ASP 455 A NA  601 1_555 ? ? ? ? ? ? ? 2.247 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  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 88.6  ? 
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 77.3  ? 
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_555 141.9 ? 
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_555 115.6 ? 
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 99.8  ? 
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_555 118.2 ? 
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_555 161.4 ? 
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 94.0  ? 
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 89.5  ? 
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 82.2  ? 
11 SG  ? A CYS 271 ? A CYS 269 ? 1_555 HG ? F HG . ? A HG 604 ? 1_555 SG  ? A CYS 443 ? A CYS 441 ? 1_555 69.9  ? 
12 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 77.6  ? 
13 O   ? A GLY 364 ? A GLY 362 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 O   ? A ASN 453 ? A ASN 451 ? 1_555 142.9 ? 
14 O   ? A ASN 368 ? A ASN 366 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 O   ? A ASN 453 ? A ASN 451 ? 1_555 91.3  ? 
15 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 69.4  ? 
16 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 79.2  ? 
17 O   ? A ASN 453 ? A ASN 451 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OD1 ? A ASP 457 ? A ASP 455 ? 1_555 73.8  ? 
18 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 76.0  ? 
19 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_555 128.6 ? 
20 O   ? A ASN 453 ? A ASN 451 ? 1_555 NA ? C NA . ? A NA 601 ? 1_555 OD2 ? A ASP 457 ? A ASP 455 ? 1_555 84.4  ? 
21 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 50.5  ? 
22 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_555 117.8 ? 
23 O   ? A THR 366 ? A THR 364 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A ILE 408 ? A ILE 406 ? 1_555 79.9  ? 
24 O   ? A SER 407 ? A SER 405 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A ILE 408 ? A ILE 406 ? 1_555 83.1  ? 
25 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_555 117.0 ? 
26 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_555 121.7 ? 
27 O   ? A ILE 408 ? A ILE 406 ? 1_555 NA ? D NA . ? A NA 602 ? 1_555 O   ? A ALA 410 ? A ALA 408 ? 1_555 88.3  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       271 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      443 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        269 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       441 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
_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   GLN 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    163 
_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    GLN 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     161 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   SER 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    209 
_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    SER 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     207 
# 
_pdbx_entry_details.entry_id                   9D6A 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 274 ? ? -93.93 -60.36 
2 1 TRP A 276 ? ? 68.55  -3.98  
3 1 ASN A 312 ? ? -58.31 108.50 
4 1 GLN A 413 ? ? 76.24  -3.34  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9D6A 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   38.93 
_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                  8CTC 
_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                8CTC 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9D6A 
_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                  2.6 
_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               365660 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          5 
_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                        9D6A 
_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              9D6A 
_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            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9D6A 
_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              9D6A 
_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 GLU 471 ? A GLU 473 
68  1 Y 1 A GLN 472 ? A GLN 474 
69  1 Y 1 A MET 473 ? A MET 475 
70  1 Y 1 A ASP 474 ? A ASP 476 
71  1 Y 1 A VAL 475 ? A VAL 477 
72  1 Y 1 A SER 476 ? A SER 478 
73  1 Y 1 A SER 477 ? A SER 479 
74  1 Y 1 A GLU 478 ? A GLU 480 
75  1 Y 1 A VAL 479 ? A VAL 481 
76  1 Y 1 A ASN 480 ? A ASN 482 
77  1 Y 1 A ILE 481 ? A ILE 483 
78  1 Y 1 A VAL 482 ? A VAL 484 
79  1 Y 1 A ASN 483 ? A ASN 485 
80  1 Y 1 A PRO 484 ? A PRO 486 
81  1 Y 1 A PHE 485 ? A PHE 487 
82  1 Y 1 A ALA 486 ? A ALA 488 
83  1 Y 1 A LEU 487 ? A LEU 489 
84  1 Y 1 A GLU 488 ? A GLU 490 
85  1 Y 1 A SER 489 ? A SER 491 
86  1 Y 1 A THR 490 ? A THR 492 
87  1 Y 1 A ILE 491 ? A ILE 493 
88  1 Y 1 A LEU 492 ? A LEU 494 
89  1 Y 1 A ASP 493 ? A ASP 495 
90  1 Y 1 A ASN 494 ? A ASN 496 
91  1 Y 1 A GLU 495 ? A GLU 497 
92  1 Y 1 A ASP 496 ? A ASP 498 
93  1 Y 1 A SER 497 ? A SER 499 
94  1 Y 1 A ASP 498 ? A ASP 500 
95  1 Y 1 A THR 499 ? A THR 501 
96  1 Y 1 A LYS 500 ? A LYS 502 
97  1 Y 1 A LYS 501 ? A LYS 503 
98  1 Y 1 A SER 502 ? A SER 504 
99  1 Y 1 A TYR 503 ? A TYR 505 
100 1 Y 1 A VAL 504 ? A VAL 506 
101 1 Y 1 A ASN 505 ? A ASN 507 
102 1 Y 1 A GLY 506 ? A GLY 508 
103 1 Y 1 A GLY 507 ? A GLY 509 
104 1 Y 1 A PHE 508 ? A PHE 510 
105 1 Y 1 A ALA 509 ? A ALA 511 
106 1 Y 1 A VAL 510 ? A VAL 512 
107 1 Y 1 A ASP 511 ? A ASP 513 
108 1 Y 1 A LYS 512 ? A LYS 514 
109 1 Y 1 A SER 513 ? A SER 515 
110 1 Y 1 A ASP 514 ? A ASP 516 
111 1 Y 1 A THR 515 ? A THR 517 
112 1 Y 1 A ILE 516 ? A ILE 518 
113 1 Y 1 A SER 517 ? A SER 519 
114 1 Y 1 A PHE 518 ? A PHE 520 
115 1 Y 1 A THR 519 ? A THR 521 
116 1 Y 1 A GLN 520 ? A GLN 522 
117 1 Y 1 A THR 521 ? A THR 523 
118 1 Y 1 A SER 522 ? A SER 524 
119 1 Y 1 A GLN 523 ? A GLN 525 
120 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 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
NA  NA   NA N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SER N    N  N N 292 
SER CA   C  N S 293 
SER C    C  N N 294 
SER O    O  N N 295 
SER CB   C  N N 296 
SER OG   O  N N 297 
SER OXT  O  N N 298 
SER H    H  N N 299 
SER H2   H  N N 300 
SER HA   H  N N 301 
SER HB2  H  N N 302 
SER HB3  H  N N 303 
SER HG   H  N N 304 
SER HXT  H  N N 305 
THR N    N  N N 306 
THR CA   C  N S 307 
THR C    C  N N 308 
THR O    O  N N 309 
THR CB   C  N R 310 
THR OG1  O  N N 311 
THR CG2  C  N N 312 
THR OXT  O  N N 313 
THR H    H  N N 314 
THR H2   H  N N 315 
THR HA   H  N N 316 
THR HB   H  N N 317 
THR HG1  H  N N 318 
THR HG21 H  N N 319 
THR HG22 H  N N 320 
THR HG23 H  N N 321 
THR HXT  H  N N 322 
TRP N    N  N N 323 
TRP CA   C  N S 324 
TRP C    C  N N 325 
TRP O    O  N N 326 
TRP CB   C  N N 327 
TRP CG   C  Y N 328 
TRP CD1  C  Y N 329 
TRP CD2  C  Y N 330 
TRP NE1  N  Y N 331 
TRP CE2  C  Y N 332 
TRP CE3  C  Y N 333 
TRP CZ2  C  Y N 334 
TRP CZ3  C  Y N 335 
TRP CH2  C  Y N 336 
TRP OXT  O  N N 337 
TRP H    H  N N 338 
TRP H2   H  N N 339 
TRP HA   H  N N 340 
TRP HB2  H  N N 341 
TRP HB3  H  N N 342 
TRP HD1  H  N N 343 
TRP HE1  H  N N 344 
TRP HE3  H  N N 345 
TRP HZ2  H  N N 346 
TRP HZ3  H  N N 347 
TRP HH2  H  N N 348 
TRP HXT  H  N N 349 
TYR N    N  N N 350 
TYR CA   C  N S 351 
TYR C    C  N N 352 
TYR O    O  N N 353 
TYR CB   C  N N 354 
TYR CG   C  Y N 355 
TYR CD1  C  Y N 356 
TYR CD2  C  Y N 357 
TYR CE1  C  Y N 358 
TYR CE2  C  Y N 359 
TYR CZ   C  Y N 360 
TYR OH   O  N N 361 
TYR OXT  O  N N 362 
TYR H    H  N N 363 
TYR H2   H  N N 364 
TYR HA   H  N N 365 
TYR HB2  H  N N 366 
TYR HB3  H  N N 367 
TYR HD1  H  N N 368 
TYR HD2  H  N N 369 
TYR HE1  H  N N 370 
TYR HE2  H  N N 371 
TYR HH   H  N N 372 
TYR HXT  H  N N 373 
VAL N    N  N N 374 
VAL CA   C  N S 375 
VAL C    C  N N 376 
VAL O    O  N N 377 
VAL CB   C  N N 378 
VAL CG1  C  N N 379 
VAL CG2  C  N N 380 
VAL OXT  O  N N 381 
VAL H    H  N N 382 
VAL H2   H  N N 383 
VAL HA   H  N N 384 
VAL HB   H  N N 385 
VAL HG11 H  N N 386 
VAL HG12 H  N N 387 
VAL HG13 H  N N 388 
VAL HG21 H  N N 389 
VAL HG22 H  N N 390 
VAL HG23 H  N N 391 
VAL HXT  H  N N 392 
# 
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 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-14 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9D6A 
_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' 
# 
_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 ? ? ?         ? 
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           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'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   8CTC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9D6A 
_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  ? 146.942 98.463  137.832 1.00 51.61  ? 17  ASN A N   1 
ATOM   2    C  CA  . ASN A 1 19  ? 147.510 97.548  136.849 1.00 52.94  ? 17  ASN A CA  1 
ATOM   3    C  C   . ASN A 1 19  ? 148.016 98.317  135.632 1.00 54.06  ? 17  ASN A C   1 
ATOM   4    O  O   . ASN A 1 19  ? 147.713 99.498  135.464 1.00 53.15  ? 17  ASN A O   1 
ATOM   5    C  CB  . ASN A 1 19  ? 146.473 96.506  136.426 1.00 52.47  ? 17  ASN A CB  1 
ATOM   6    C  CG  . ASN A 1 19  ? 147.100 95.168  136.077 1.00 55.39  ? 17  ASN A CG  1 
ATOM   7    O  OD1 . ASN A 1 19  ? 147.829 94.583  136.878 1.00 54.67  ? 17  ASN A OD1 1 
ATOM   8    N  ND2 . ASN A 1 19  ? 146.813 94.676  134.877 1.00 51.69  ? 17  ASN A ND2 1 
ATOM   9    N  N   . ASN A 1 20  ? 148.787 97.636  134.787 1.00 52.23  ? 18  ASN A N   1 
ATOM   10   C  CA  . ASN A 1 20  ? 149.384 98.236  133.602 1.00 49.90  ? 18  ASN A CA  1 
ATOM   11   C  C   . ASN A 1 20  ? 148.632 97.890  132.323 1.00 51.24  ? 18  ASN A C   1 
ATOM   12   O  O   . ASN A 1 20  ? 149.158 98.112  131.229 1.00 49.25  ? 18  ASN A O   1 
ATOM   13   C  CB  . ASN A 1 20  ? 150.845 97.799  133.477 1.00 46.09  ? 18  ASN A CB  1 
ATOM   14   C  CG  . ASN A 1 20  ? 151.731 98.430  134.530 1.00 49.71  ? 18  ASN A CG  1 
ATOM   15   O  OD1 . ASN A 1 20  ? 152.144 99.582  134.399 1.00 52.66  ? 18  ASN A OD1 1 
ATOM   16   N  ND2 . ASN A 1 20  ? 152.025 97.680  135.584 1.00 45.93  ? 18  ASN A ND2 1 
ATOM   17   N  N   . TRP A 1 21  ? 147.416 97.349  132.433 1.00 51.19  ? 19  TRP A N   1 
ATOM   18   C  CA  . TRP A 1 21  ? 146.681 96.946  131.238 1.00 49.42  ? 19  TRP A CA  1 
ATOM   19   C  C   . TRP A 1 21  ? 146.525 98.101  130.259 1.00 44.62  ? 19  TRP A C   1 
ATOM   20   O  O   . TRP A 1 21  ? 146.505 97.883  129.043 1.00 41.95  ? 19  TRP A O   1 
ATOM   21   C  CB  . TRP A 1 21  ? 145.310 96.384  131.628 1.00 45.14  ? 19  TRP A CB  1 
ATOM   22   C  CG  . TRP A 1 21  ? 144.259 97.432  131.866 1.00 44.14  ? 19  TRP A CG  1 
ATOM   23   C  CD1 . TRP A 1 21  ? 143.861 97.933  133.071 1.00 45.62  ? 19  TRP A CD1 1 
ATOM   24   C  CD2 . TRP A 1 21  ? 143.469 98.101  130.873 1.00 51.00  ? 19  TRP A CD2 1 
ATOM   25   N  NE1 . TRP A 1 21  ? 142.877 98.876  132.891 1.00 52.77  ? 19  TRP A NE1 1 
ATOM   26   C  CE2 . TRP A 1 21  ? 142.619 98.998  131.551 1.00 54.10  ? 19  TRP A CE2 1 
ATOM   27   C  CE3 . TRP A 1 21  ? 143.402 98.034  129.478 1.00 47.10  ? 19  TRP A CE3 1 
ATOM   28   C  CZ2 . TRP A 1 21  ? 141.714 99.819  130.881 1.00 47.31  ? 19  TRP A CZ2 1 
ATOM   29   C  CZ3 . TRP A 1 21  ? 142.503 98.850  128.815 1.00 46.32  ? 19  TRP A CZ3 1 
ATOM   30   C  CH2 . TRP A 1 21  ? 141.671 99.730  129.517 1.00 46.68  ? 19  TRP A CH2 1 
ATOM   31   N  N   . VAL A 1 22  ? 146.417 99.332  130.762 1.00 39.69  ? 20  VAL A N   1 
ATOM   32   C  CA  . VAL A 1 22  ? 146.190 100.474 129.880 1.00 42.85  ? 20  VAL A CA  1 
ATOM   33   C  C   . VAL A 1 22  ? 147.349 100.634 128.906 1.00 44.65  ? 20  VAL A C   1 
ATOM   34   O  O   . VAL A 1 22  ? 147.146 100.853 127.707 1.00 47.04  ? 20  VAL A O   1 
ATOM   35   C  CB  . VAL A 1 22  ? 145.971 101.755 130.706 1.00 46.78  ? 20  VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 22  ? 145.682 102.934 129.787 1.00 45.57  ? 20  VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 22  ? 144.837 101.567 131.700 1.00 47.67  ? 20  VAL A CG2 1 
ATOM   38   N  N   . LEU A 1 23  ? 148.580 100.527 129.402 1.00 45.29  ? 21  LEU A N   1 
ATOM   39   C  CA  . LEU A 1 23  ? 149.757 100.742 128.571 1.00 38.02  ? 21  LEU A CA  1 
ATOM   40   C  C   . LEU A 1 23  ? 150.187 99.479  127.837 1.00 39.92  ? 21  LEU A C   1 
ATOM   41   O  O   . LEU A 1 23  ? 150.562 99.546  126.663 1.00 40.03  ? 21  LEU A O   1 
ATOM   42   C  CB  . LEU A 1 23  ? 150.912 101.264 129.431 1.00 39.53  ? 21  LEU A CB  1 
ATOM   43   C  CG  . LEU A 1 23  ? 152.110 101.878 128.704 1.00 43.99  ? 21  LEU A CG  1 
ATOM   44   C  CD1 . LEU A 1 23  ? 151.677 102.971 127.743 1.00 40.69  ? 21  LEU A CD1 1 
ATOM   45   C  CD2 . LEU A 1 23  ? 153.097 102.424 129.717 1.00 43.08  ? 21  LEU A CD2 1 
ATOM   46   N  N   . LEU A 1 24  ? 150.144 98.325  128.506 1.00 43.28  ? 22  LEU A N   1 
ATOM   47   C  CA  . LEU A 1 24  ? 150.533 97.080  127.851 1.00 43.31  ? 22  LEU A CA  1 
ATOM   48   C  C   . LEU A 1 24  ? 149.588 96.740  126.707 1.00 39.78  ? 22  LEU A C   1 
ATOM   49   O  O   . LEU A 1 24  ? 150.030 96.328  125.629 1.00 42.24  ? 22  LEU A O   1 
ATOM   50   C  CB  . LEU A 1 24  ? 150.566 95.943  128.871 1.00 47.44  ? 22  LEU A CB  1 
ATOM   51   C  CG  . LEU A 1 24  ? 151.862 95.773  129.663 1.00 46.23  ? 22  LEU A CG  1 
ATOM   52   C  CD1 . LEU A 1 24  ? 151.688 94.690  130.713 1.00 44.66  ? 22  LEU A CD1 1 
ATOM   53   C  CD2 . LEU A 1 24  ? 153.032 95.448  128.749 1.00 40.80  ? 22  LEU A CD2 1 
ATOM   54   N  N   . SER A 1 25  ? 148.281 96.903  126.922 1.00 40.70  ? 23  SER A N   1 
ATOM   55   C  CA  . SER A 1 25  ? 147.319 96.614  125.864 1.00 39.30  ? 23  SER A CA  1 
ATOM   56   C  C   . SER A 1 25  ? 147.490 97.567  124.689 1.00 38.21  ? 23  SER A C   1 
ATOM   57   O  O   . SER A 1 25  ? 147.369 97.162  123.528 1.00 40.52  ? 23  SER A O   1 
ATOM   58   C  CB  . SER A 1 25  ? 145.896 96.698  126.413 1.00 43.79  ? 23  SER A CB  1 
ATOM   59   O  OG  . SER A 1 25  ? 145.480 98.045  126.541 1.00 41.41  ? 23  SER A OG  1 
ATOM   60   N  N   . THR A 1 26  ? 147.759 98.841  124.971 1.00 43.60  ? 24  THR A N   1 
ATOM   61   C  CA  . THR A 1 26  ? 147.938 99.814  123.899 1.00 37.67  ? 24  THR A CA  1 
ATOM   62   C  C   . THR A 1 26  ? 149.196 99.520  123.090 1.00 36.93  ? 24  THR A C   1 
ATOM   63   O  O   . THR A 1 26  ? 149.202 99.678  121.864 1.00 44.25  ? 24  THR A O   1 
ATOM   64   C  CB  . THR A 1 26  ? 147.986 101.226 124.482 1.00 35.39  ? 24  THR A CB  1 
ATOM   65   O  OG1 . THR A 1 26  ? 146.737 101.523 125.115 1.00 41.33  ? 24  THR A OG1 1 
ATOM   66   C  CG2 . THR A 1 26  ? 148.231 102.246 123.394 1.00 39.18  ? 24  THR A CG2 1 
ATOM   67   N  N   . VAL A 1 27  ? 150.276 99.109  123.756 1.00 37.37  ? 25  VAL A N   1 
ATOM   68   C  CA  . VAL A 1 27  ? 151.483 98.718  123.035 1.00 38.42  ? 25  VAL A CA  1 
ATOM   69   C  C   . VAL A 1 27  ? 151.215 97.482  122.188 1.00 39.23  ? 25  VAL A C   1 
ATOM   70   O  O   . VAL A 1 27  ? 151.678 97.382  121.046 1.00 39.21  ? 25  VAL A O   1 
ATOM   71   C  CB  . VAL A 1 27  ? 152.643 98.487  124.020 1.00 38.64  ? 25  VAL A CB  1 
ATOM   72   C  CG1 . VAL A 1 27  ? 153.806 97.799  123.321 1.00 39.15  ? 25  VAL A CG1 1 
ATOM   73   C  CG2 . VAL A 1 27  ? 153.091 99.802  124.629 1.00 42.04  ? 25  VAL A CG2 1 
ATOM   74   N  N   . ALA A 1 28  ? 150.473 96.516  122.735 1.00 39.98  ? 26  ALA A N   1 
ATOM   75   C  CA  . ALA A 1 28  ? 150.124 95.327  121.967 1.00 32.54  ? 26  ALA A CA  1 
ATOM   76   C  C   . ALA A 1 28  ? 149.262 95.673  120.761 1.00 35.36  ? 26  ALA A C   1 
ATOM   77   O  O   . ALA A 1 28  ? 149.326 94.987  119.736 1.00 36.14  ? 26  ALA A O   1 
ATOM   78   C  CB  . ALA A 1 28  ? 149.403 94.320  122.861 1.00 34.30  ? 26  ALA A CB  1 
ATOM   79   N  N   . ALA A 1 29  ? 148.443 96.720  120.866 1.00 35.95  ? 27  ALA A N   1 
ATOM   80   C  CA  . ALA A 1 29  ? 147.632 97.138  119.728 1.00 33.64  ? 27  ALA A CA  1 
ATOM   81   C  C   . ALA A 1 29  ? 148.501 97.675  118.598 1.00 38.92  ? 27  ALA A C   1 
ATOM   82   O  O   . ALA A 1 29  ? 148.207 97.446  117.420 1.00 34.75  ? 27  ALA A O   1 
ATOM   83   C  CB  . ALA A 1 29  ? 146.619 98.191  120.168 1.00 34.83  ? 27  ALA A CB  1 
ATOM   84   N  N   . VAL A 1 30  ? 149.569 98.397  118.938 1.00 39.43  ? 28  VAL A N   1 
ATOM   85   C  CA  . VAL A 1 30  ? 150.436 98.971  117.914 1.00 36.34  ? 28  VAL A CA  1 
ATOM   86   C  C   . VAL A 1 30  ? 151.195 97.873  117.180 1.00 37.28  ? 28  VAL A C   1 
ATOM   87   O  O   . VAL A 1 30  ? 151.272 97.869  115.947 1.00 41.90  ? 28  VAL A O   1 
ATOM   88   C  CB  . VAL A 1 30  ? 151.396 99.999  118.539 1.00 42.58  ? 28  VAL A CB  1 
ATOM   89   C  CG1 . VAL A 1 30  ? 152.400 100.489 117.505 1.00 37.83  ? 28  VAL A CG1 1 
ATOM   90   C  CG2 . VAL A 1 30  ? 150.617 101.165 119.127 1.00 38.64  ? 28  VAL A CG2 1 
ATOM   91   N  N   . VAL A 1 31  ? 151.772 96.927  117.923 1.00 34.82  ? 29  VAL A N   1 
ATOM   92   C  CA  . VAL A 1 31  ? 152.535 95.863  117.280 1.00 40.93  ? 29  VAL A CA  1 
ATOM   93   C  C   . VAL A 1 31  ? 151.614 94.978  116.450 1.00 42.12  ? 29  VAL A C   1 
ATOM   94   O  O   . VAL A 1 31  ? 151.984 94.521  115.363 1.00 44.98  ? 29  VAL A O   1 
ATOM   95   C  CB  . VAL A 1 31  ? 153.319 95.047  118.326 1.00 42.38  ? 29  VAL A CB  1 
ATOM   96   C  CG1 . VAL A 1 31  ? 154.185 95.963  119.177 1.00 42.64  ? 29  VAL A CG1 1 
ATOM   97   C  CG2 . VAL A 1 31  ? 152.381 94.236  119.198 1.00 39.14  ? 29  VAL A CG2 1 
ATOM   98   N  N   . LEU A 1 32  ? 150.401 94.721  116.943 1.00 42.08  ? 30  LEU A N   1 
ATOM   99   C  CA  . LEU A 1 32  ? 149.450 93.925  116.175 1.00 39.80  ? 30  LEU A CA  1 
ATOM   100  C  C   . LEU A 1 32  ? 148.922 94.690  114.970 1.00 42.08  ? 30  LEU A C   1 
ATOM   101  O  O   . LEU A 1 32  ? 148.632 94.084  113.933 1.00 45.46  ? 30  LEU A O   1 
ATOM   102  C  CB  . LEU A 1 32  ? 148.294 93.481  117.071 1.00 37.83  ? 30  LEU A CB  1 
ATOM   103  C  CG  . LEU A 1 32  ? 148.638 92.441  118.141 1.00 45.56  ? 30  LEU A CG  1 
ATOM   104  C  CD1 . LEU A 1 32  ? 147.419 92.132  118.991 1.00 42.54  ? 30  LEU A CD1 1 
ATOM   105  C  CD2 . LEU A 1 32  ? 149.185 91.171  117.513 1.00 42.26  ? 30  LEU A CD2 1 
ATOM   106  N  N   . GLY A 1 33  ? 148.783 96.011  115.083 1.00 37.75  ? 31  GLY A N   1 
ATOM   107  C  CA  . GLY A 1 33  ? 148.373 96.799  113.934 1.00 34.90  ? 31  GLY A CA  1 
ATOM   108  C  C   . GLY A 1 33  ? 149.398 96.773  112.817 1.00 39.53  ? 31  GLY A C   1 
ATOM   109  O  O   . GLY A 1 33  ? 149.046 96.650  111.642 1.00 39.04  ? 31  GLY A O   1 
ATOM   110  N  N   . ILE A 1 34  ? 150.680 96.898  113.165 1.00 41.86  ? 32  ILE A N   1 
ATOM   111  C  CA  . ILE A 1 34  ? 151.733 96.813  112.158 1.00 38.96  ? 32  ILE A CA  1 
ATOM   112  C  C   . ILE A 1 34  ? 151.788 95.410  111.568 1.00 39.34  ? 32  ILE A C   1 
ATOM   113  O  O   . ILE A 1 34  ? 151.867 95.235  110.347 1.00 40.47  ? 32  ILE A O   1 
ATOM   114  C  CB  . ILE A 1 34  ? 153.089 97.223  112.762 1.00 42.18  ? 32  ILE A CB  1 
ATOM   115  C  CG1 . ILE A 1 34  ? 153.083 98.711  113.119 1.00 44.03  ? 32  ILE A CG1 1 
ATOM   116  C  CG2 . ILE A 1 34  ? 154.216 96.919  111.788 1.00 40.38  ? 32  ILE A CG2 1 
ATOM   117  C  CD1 . ILE A 1 34  ? 154.186 99.115  114.070 1.00 40.59  ? 32  ILE A CD1 1 
ATOM   118  N  N   . THR A 1 35  ? 151.749 94.388  112.425 1.00 40.28  ? 33  THR A N   1 
ATOM   119  C  CA  . THR A 1 35  ? 151.764 93.015  111.931 1.00 39.70  ? 33  THR A CA  1 
ATOM   120  C  C   . THR A 1 35  ? 150.528 92.723  111.091 1.00 41.57  ? 33  THR A C   1 
ATOM   121  O  O   . THR A 1 35  ? 150.622 92.090  110.033 1.00 48.80  ? 33  THR A O   1 
ATOM   122  C  CB  . THR A 1 35  ? 151.857 92.034  113.099 1.00 45.72  ? 33  THR A CB  1 
ATOM   123  O  OG1 . THR A 1 35  ? 152.699 92.577  114.122 1.00 48.60  ? 33  THR A OG1 1 
ATOM   124  C  CG2 . THR A 1 35  ? 152.423 90.702  112.636 1.00 45.27  ? 33  THR A CG2 1 
ATOM   125  N  N   . THR A 1 36  ? 149.358 93.173  111.548 1.00 43.67  ? 34  THR A N   1 
ATOM   126  C  CA  . THR A 1 36  ? 148.139 92.994  110.768 1.00 40.62  ? 34  THR A CA  1 
ATOM   127  C  C   . THR A 1 36  ? 148.209 93.770  109.460 1.00 40.16  ? 34  THR A C   1 
ATOM   128  O  O   . THR A 1 36  ? 147.859 93.250  108.395 1.00 40.09  ? 34  THR A O   1 
ATOM   129  C  CB  . THR A 1 36  ? 146.925 93.435  111.585 1.00 38.51  ? 34  THR A CB  1 
ATOM   130  O  OG1 . THR A 1 36  ? 146.870 92.689  112.806 1.00 44.66  ? 34  THR A OG1 1 
ATOM   131  C  CG2 . THR A 1 36  ? 145.640 93.219  110.802 1.00 38.43  ? 34  THR A CG2 1 
ATOM   132  N  N   . GLY A 1 37  ? 148.663 95.022  109.521 1.00 39.80  ? 35  GLY A N   1 
ATOM   133  C  CA  . GLY A 1 37  ? 148.689 95.846  108.326 1.00 42.12  ? 35  GLY A CA  1 
ATOM   134  C  C   . GLY A 1 37  ? 149.653 95.334  107.274 1.00 43.00  ? 35  GLY A C   1 
ATOM   135  O  O   . GLY A 1 37  ? 149.343 95.344  106.080 1.00 42.49  ? 35  GLY A O   1 
ATOM   136  N  N   . VAL A 1 38  ? 150.837 94.889  107.696 1.00 43.50  ? 36  VAL A N   1 
ATOM   137  C  CA  . VAL A 1 38  ? 151.837 94.428  106.738 1.00 41.66  ? 36  VAL A CA  1 
ATOM   138  C  C   . VAL A 1 38  ? 151.412 93.108  106.111 1.00 44.29  ? 36  VAL A C   1 
ATOM   139  O  O   . VAL A 1 38  ? 151.521 92.921  104.894 1.00 51.62  ? 36  VAL A O   1 
ATOM   140  C  CB  . VAL A 1 38  ? 153.212 94.312  107.419 1.00 43.90  ? 36  VAL A CB  1 
ATOM   141  C  CG1 . VAL A 1 38  ? 154.194 93.585  106.513 1.00 43.79  ? 36  VAL A CG1 1 
ATOM   142  C  CG2 . VAL A 1 38  ? 153.737 95.690  107.786 1.00 41.60  ? 36  VAL A CG2 1 
ATOM   143  N  N   . LEU A 1 39  ? 150.932 92.167  106.926 1.00 46.60  ? 37  LEU A N   1 
ATOM   144  C  CA  . LEU A 1 39  ? 150.503 90.880  106.388 1.00 46.65  ? 37  LEU A CA  1 
ATOM   145  C  C   . LEU A 1 39  ? 149.298 91.038  105.471 1.00 44.98  ? 37  LEU A C   1 
ATOM   146  O  O   . LEU A 1 39  ? 149.238 90.419  104.403 1.00 44.96  ? 37  LEU A O   1 
ATOM   147  C  CB  . LEU A 1 39  ? 150.186 89.914  107.529 1.00 45.32  ? 37  LEU A CB  1 
ATOM   148  C  CG  . LEU A 1 39  ? 151.376 89.460  108.377 1.00 48.62  ? 37  LEU A CG  1 
ATOM   149  C  CD1 . LEU A 1 39  ? 150.934 88.436  109.407 1.00 49.26  ? 37  LEU A CD1 1 
ATOM   150  C  CD2 . LEU A 1 39  ? 152.488 88.895  107.504 1.00 46.05  ? 37  LEU A CD2 1 
ATOM   151  N  N   . VAL A 1 40  ? 148.327 91.862  105.868 1.00 42.11  ? 38  VAL A N   1 
ATOM   152  C  CA  . VAL A 1 40  ? 147.168 92.103  105.016 1.00 43.62  ? 38  VAL A CA  1 
ATOM   153  C  C   . VAL A 1 40  ? 147.599 92.758  103.712 1.00 47.98  ? 38  VAL A C   1 
ATOM   154  O  O   . VAL A 1 40  ? 147.129 92.393  102.629 1.00 48.32  ? 38  VAL A O   1 
ATOM   155  C  CB  . VAL A 1 40  ? 146.126 92.957  105.761 1.00 42.75  ? 38  VAL A CB  1 
ATOM   156  C  CG1 . VAL A 1 40  ? 145.081 93.487  104.796 1.00 41.68  ? 38  VAL A CG1 1 
ATOM   157  C  CG2 . VAL A 1 40  ? 145.470 92.145  106.861 1.00 44.18  ? 38  VAL A CG2 1 
ATOM   158  N  N   . ARG A 1 41  ? 148.506 93.732  103.795 1.00 49.78  ? 39  ARG A N   1 
ATOM   159  C  CA  . ARG A 1 41  ? 148.952 94.435  102.598 1.00 49.09  ? 39  ARG A CA  1 
ATOM   160  C  C   . ARG A 1 41  ? 149.616 93.487  101.610 1.00 48.70  ? 39  ARG A C   1 
ATOM   161  O  O   . ARG A 1 41  ? 149.401 93.591  100.397 1.00 50.25  ? 39  ARG A O   1 
ATOM   162  C  CB  . ARG A 1 41  ? 149.911 95.558  102.988 1.00 48.75  ? 39  ARG A CB  1 
ATOM   163  C  CG  . ARG A 1 41  ? 150.047 96.649  101.949 1.00 51.22  ? 39  ARG A CG  1 
ATOM   164  C  CD  . ARG A 1 41  ? 151.237 97.542  102.238 1.00 48.00  ? 39  ARG A CD  1 
ATOM   165  N  NE  . ARG A 1 41  ? 151.764 98.154  101.026 1.00 51.31  ? 39  ARG A NE  1 
ATOM   166  C  CZ  . ARG A 1 41  ? 152.632 97.574  100.208 1.00 56.13  ? 39  ARG A CZ  1 
ATOM   167  N  NH1 . ARG A 1 41  ? 153.096 96.357  100.440 1.00 49.48  ? 39  ARG A NH1 1 
ATOM   168  N  NH2 . ARG A 1 41  ? 153.045 98.233  99.130  1.00 54.77  ? 39  ARG A NH2 1 
ATOM   169  N  N   . GLU A 1 42  ? 150.428 92.554  102.108 1.00 50.20  ? 40  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 42  ? 151.211 91.698  101.225 1.00 52.24  ? 40  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 42  ? 150.381 90.550  100.661 1.00 52.84  ? 40  GLU A C   1 
ATOM   172  O  O   . GLU A 1 42  ? 150.387 90.309  99.449  1.00 54.50  ? 40  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 42  ? 152.427 91.155  101.976 1.00 50.52  ? 40  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 42  ? 153.583 90.756  101.072 1.00 55.65  ? 40  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 42  ? 154.917 90.750  101.792 1.00 56.83  ? 40  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 42  ? 155.126 91.610  102.673 1.00 54.37  ? 40  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 42  ? 155.759 89.884  101.475 1.00 54.84  ? 40  GLU A OE2 1 
ATOM   178  N  N   . HIS A 1 43  ? 149.660 89.834  101.520 1.00 51.34  ? 41  HIS A N   1 
ATOM   179  C  CA  . HIS A 1 43  ? 148.994 88.596  101.138 1.00 50.40  ? 41  HIS A CA  1 
ATOM   180  C  C   . HIS A 1 43  ? 147.541 88.792  100.724 1.00 53.79  ? 41  HIS A C   1 
ATOM   181  O  O   . HIS A 1 43  ? 146.849 87.803  100.466 1.00 55.24  ? 41  HIS A O   1 
ATOM   182  C  CB  . HIS A 1 43  ? 149.067 87.590  102.288 1.00 50.91  ? 41  HIS A CB  1 
ATOM   183  C  CG  . HIS A 1 43  ? 150.422 87.490  102.913 1.00 55.40  ? 41  HIS A CG  1 
ATOM   184  N  ND1 . HIS A 1 43  ? 151.582 87.444  102.171 1.00 53.45  ? 41  HIS A ND1 1 
ATOM   185  C  CD2 . HIS A 1 43  ? 150.804 87.432  104.211 1.00 55.48  ? 41  HIS A CD2 1 
ATOM   186  C  CE1 . HIS A 1 43  ? 152.620 87.360  102.984 1.00 54.66  ? 41  HIS A CE1 1 
ATOM   187  N  NE2 . HIS A 1 43  ? 152.175 87.351  104.227 1.00 59.20  ? 41  HIS A NE2 1 
ATOM   188  N  N   . SER A 1 44  ? 147.061 90.030  100.652 1.00 50.11  ? 42  SER A N   1 
ATOM   189  C  CA  . SER A 1 44  ? 145.690 90.305  100.256 1.00 49.07  ? 42  SER A CA  1 
ATOM   190  C  C   . SER A 1 44  ? 145.676 91.385  99.186  1.00 54.49  ? 42  SER A C   1 
ATOM   191  O  O   . SER A 1 44  ? 146.644 92.128  99.008  1.00 59.54  ? 42  SER A O   1 
ATOM   192  C  CB  . SER A 1 44  ? 144.830 90.737  101.450 1.00 50.66  ? 42  SER A CB  1 
ATOM   193  O  OG  . SER A 1 44  ? 143.461 90.785  101.093 1.00 55.80  ? 42  SER A OG  1 
ATOM   194  N  N   . ASN A 1 45  ? 144.560 91.457  98.468  1.00 50.72  ? 43  ASN A N   1 
ATOM   195  C  CA  . ASN A 1 45  ? 144.365 92.397  97.369  1.00 51.96  ? 43  ASN A CA  1 
ATOM   196  C  C   . ASN A 1 45  ? 143.093 93.205  97.592  1.00 51.59  ? 43  ASN A C   1 
ATOM   197  O  O   . ASN A 1 45  ? 142.253 93.360  96.703  1.00 52.37  ? 43  ASN A O   1 
ATOM   198  C  CB  . ASN A 1 45  ? 144.323 91.652  96.036  1.00 50.88  ? 43  ASN A CB  1 
ATOM   199  C  CG  . ASN A 1 45  ? 145.195 92.298  94.980  1.00 53.15  ? 43  ASN A CG  1 
ATOM   200  O  OD1 . ASN A 1 45  ? 145.422 93.507  94.999  1.00 54.04  ? 43  ASN A OD1 1 
ATOM   201  N  ND2 . ASN A 1 45  ? 145.690 91.491  94.050  1.00 53.32  ? 43  ASN A ND2 1 
ATOM   202  N  N   . LEU A 1 46  ? 142.940 93.732  98.804  1.00 49.56  ? 44  LEU A N   1 
ATOM   203  C  CA  . LEU A 1 46  ? 141.743 94.486  99.146  1.00 47.31  ? 44  LEU A CA  1 
ATOM   204  C  C   . LEU A 1 46  ? 141.555 95.660  98.194  1.00 45.63  ? 44  LEU A C   1 
ATOM   205  O  O   . LEU A 1 46  ? 142.508 96.361  97.848  1.00 46.90  ? 44  LEU A O   1 
ATOM   206  C  CB  . LEU A 1 46  ? 141.830 94.996  100.586 1.00 46.38  ? 44  LEU A CB  1 
ATOM   207  C  CG  . LEU A 1 46  ? 141.954 93.960  101.703 1.00 45.99  ? 44  LEU A CG  1 
ATOM   208  C  CD1 . LEU A 1 46  ? 141.775 94.633  103.051 1.00 46.32  ? 44  LEU A CD1 1 
ATOM   209  C  CD2 . LEU A 1 46  ? 140.952 92.836  101.534 1.00 44.73  ? 44  LEU A CD2 1 
ATOM   210  N  N   . SER A 1 47  ? 140.312 95.868  97.769  1.00 45.00  ? 45  SER A N   1 
ATOM   211  C  CA  . SER A 1 47  ? 139.971 97.006  96.932  1.00 46.96  ? 45  SER A CA  1 
ATOM   212  C  C   . SER A 1 47  ? 139.837 98.259  97.793  1.00 44.31  ? 45  SER A C   1 
ATOM   213  O  O   . SER A 1 47  ? 140.014 98.230  99.013  1.00 44.69  ? 45  SER A O   1 
ATOM   214  C  CB  . SER A 1 47  ? 138.684 96.729  96.161  1.00 49.42  ? 45  SER A CB  1 
ATOM   215  O  OG  . SER A 1 47  ? 137.575 96.654  97.039  1.00 53.27  ? 45  SER A OG  1 
ATOM   216  N  N   . THR A 1 48  ? 139.516 99.383  97.151  1.00 43.17  ? 46  THR A N   1 
ATOM   217  C  CA  . THR A 1 48  ? 139.388 100.634 97.889  1.00 42.78  ? 46  THR A CA  1 
ATOM   218  C  C   . THR A 1 48  ? 138.281 100.546 98.931  1.00 46.25  ? 46  THR A C   1 
ATOM   219  O  O   . THR A 1 48  ? 138.438 101.032 100.057 1.00 48.63  ? 46  THR A O   1 
ATOM   220  C  CB  . THR A 1 48  ? 139.121 101.789 96.925  1.00 43.58  ? 46  THR A CB  1 
ATOM   221  O  OG1 . THR A 1 48  ? 140.066 101.744 95.850  1.00 49.21  ? 46  THR A OG1 1 
ATOM   222  C  CG2 . THR A 1 48  ? 139.241 103.123 97.644  1.00 41.00  ? 46  THR A CG2 1 
ATOM   223  N  N   . LEU A 1 49  ? 137.149 99.936  98.572  1.00 40.98  ? 47  LEU A N   1 
ATOM   224  C  CA  . LEU A 1 49  ? 136.046 99.815  99.519  1.00 40.56  ? 47  LEU A CA  1 
ATOM   225  C  C   . LEU A 1 49  ? 136.406 98.891  100.675 1.00 42.16  ? 47  LEU A C   1 
ATOM   226  O  O   . LEU A 1 49  ? 136.126 99.205  101.837 1.00 44.44  ? 47  LEU A O   1 
ATOM   227  C  CB  . LEU A 1 49  ? 134.796 99.310  98.802  1.00 41.10  ? 47  LEU A CB  1 
ATOM   228  C  CG  . LEU A 1 49  ? 133.769 100.383 98.445  1.00 44.07  ? 47  LEU A CG  1 
ATOM   229  C  CD1 . LEU A 1 49  ? 132.794 99.853  97.413  1.00 42.83  ? 47  LEU A CD1 1 
ATOM   230  C  CD2 . LEU A 1 49  ? 133.034 100.856 99.685  1.00 43.05  ? 47  LEU A CD2 1 
ATOM   231  N  N   . GLU A 1 50  ? 137.025 97.746  100.379 1.00 42.40  ? 48  GLU A N   1 
ATOM   232  C  CA  . GLU A 1 50  ? 137.391 96.814  101.440 1.00 41.37  ? 48  GLU A CA  1 
ATOM   233  C  C   . GLU A 1 50  ? 138.428 97.415  102.376 1.00 44.62  ? 48  GLU A C   1 
ATOM   234  O  O   . GLU A 1 50  ? 138.435 97.109  103.573 1.00 45.07  ? 48  GLU A O   1 
ATOM   235  C  CB  . GLU A 1 50  ? 137.911 95.511  100.836 1.00 43.78  ? 48  GLU A CB  1 
ATOM   236  C  CG  . GLU A 1 50  ? 136.950 94.867  99.852  1.00 44.57  ? 48  GLU A CG  1 
ATOM   237  C  CD  . GLU A 1 50  ? 137.274 93.413  99.581  1.00 50.21  ? 48  GLU A CD  1 
ATOM   238  O  OE1 . GLU A 1 50  ? 137.895 92.766  100.448 1.00 50.07  ? 48  GLU A OE1 1 
ATOM   239  O  OE2 . GLU A 1 50  ? 136.905 92.914  98.498  1.00 50.57  ? 48  GLU A OE2 1 
ATOM   240  N  N   . LYS A 1 51  ? 139.318 98.260  101.853 1.00 43.33  ? 49  LYS A N   1 
ATOM   241  C  CA  . LYS A 1 51  ? 140.258 98.963  102.718 1.00 36.71  ? 49  LYS A CA  1 
ATOM   242  C  C   . LYS A 1 51  ? 139.527 99.910  103.658 1.00 39.14  ? 49  LYS A C   1 
ATOM   243  O  O   . LYS A 1 51  ? 139.886 100.029 104.835 1.00 41.60  ? 49  LYS A O   1 
ATOM   244  C  CB  . LYS A 1 51  ? 141.274 99.729  101.874 1.00 44.86  ? 49  LYS A CB  1 
ATOM   245  C  CG  . LYS A 1 51  ? 142.261 98.845  101.142 1.00 47.20  ? 49  LYS A CG  1 
ATOM   246  C  CD  . LYS A 1 51  ? 143.160 99.660  100.232 1.00 44.26  ? 49  LYS A CD  1 
ATOM   247  C  CE  . LYS A 1 51  ? 144.198 98.788  99.555  1.00 43.93  ? 49  LYS A CE  1 
ATOM   248  N  NZ  . LYS A 1 51  ? 145.067 99.568  98.637  1.00 47.69  ? 49  LYS A NZ  1 
ATOM   249  N  N   . PHE A 1 52  ? 138.506 100.606 103.153 1.00 40.15  ? 50  PHE A N   1 
ATOM   250  C  CA  . PHE A 1 52  ? 137.739 101.512 104.000 1.00 35.86  ? 50  PHE A CA  1 
ATOM   251  C  C   . PHE A 1 52  ? 136.981 100.752 105.081 1.00 40.80  ? 50  PHE A C   1 
ATOM   252  O  O   . PHE A 1 52  ? 136.912 101.202 106.230 1.00 42.63  ? 50  PHE A O   1 
ATOM   253  C  CB  . PHE A 1 52  ? 136.774 102.334 103.148 1.00 36.27  ? 50  PHE A CB  1 
ATOM   254  C  CG  . PHE A 1 52  ? 135.952 103.308 103.940 1.00 40.72  ? 50  PHE A CG  1 
ATOM   255  C  CD1 . PHE A 1 52  ? 136.450 104.559 104.252 1.00 38.42  ? 50  PHE A CD1 1 
ATOM   256  C  CD2 . PHE A 1 52  ? 134.686 102.968 104.382 1.00 38.92  ? 50  PHE A CD2 1 
ATOM   257  C  CE1 . PHE A 1 52  ? 135.700 105.453 104.984 1.00 37.32  ? 50  PHE A CE1 1 
ATOM   258  C  CE2 . PHE A 1 52  ? 133.933 103.858 105.115 1.00 40.21  ? 50  PHE A CE2 1 
ATOM   259  C  CZ  . PHE A 1 52  ? 134.441 105.102 105.416 1.00 37.65  ? 50  PHE A CZ  1 
ATOM   260  N  N   . TYR A 1 53  ? 136.396 99.604  104.733 1.00 36.40  ? 51  TYR A N   1 
ATOM   261  C  CA  . TYR A 1 53  ? 135.675 98.816  105.726 1.00 30.56  ? 51  TYR A CA  1 
ATOM   262  C  C   . TYR A 1 53  ? 136.621 98.177  106.731 1.00 34.26  ? 51  TYR A C   1 
ATOM   263  O  O   . TYR A 1 53  ? 136.261 98.016  107.901 1.00 40.93  ? 51  TYR A O   1 
ATOM   264  C  CB  . TYR A 1 53  ? 134.835 97.740  105.037 1.00 35.61  ? 51  TYR A CB  1 
ATOM   265  C  CG  . TYR A 1 53  ? 133.718 98.289  104.180 1.00 37.63  ? 51  TYR A CG  1 
ATOM   266  C  CD1 . TYR A 1 53  ? 132.983 99.392  104.586 1.00 34.59  ? 51  TYR A CD1 1 
ATOM   267  C  CD2 . TYR A 1 53  ? 133.403 97.705  102.964 1.00 41.49  ? 51  TYR A CD2 1 
ATOM   268  C  CE1 . TYR A 1 53  ? 131.969 99.896  103.808 1.00 36.99  ? 51  TYR A CE1 1 
ATOM   269  C  CE2 . TYR A 1 53  ? 132.389 98.203  102.178 1.00 38.96  ? 51  TYR A CE2 1 
ATOM   270  C  CZ  . TYR A 1 53  ? 131.674 99.299  102.605 1.00 41.44  ? 51  TYR A CZ  1 
ATOM   271  O  OH  . TYR A 1 53  ? 130.659 99.803  101.826 1.00 48.23  ? 51  TYR A OH  1 
ATOM   272  N  N   . PHE A 1 54  ? 137.826 97.804  106.298 1.00 38.71  ? 52  PHE A N   1 
ATOM   273  C  CA  . PHE A 1 54  ? 138.799 97.240  107.225 1.00 36.56  ? 52  PHE A CA  1 
ATOM   274  C  C   . PHE A 1 54  ? 139.178 98.238  108.310 1.00 35.16  ? 52  PHE A C   1 
ATOM   275  O  O   . PHE A 1 54  ? 139.425 97.847  109.455 1.00 37.47  ? 52  PHE A O   1 
ATOM   276  C  CB  . PHE A 1 54  ? 140.045 96.790  106.463 1.00 37.39  ? 52  PHE A CB  1 
ATOM   277  C  CG  . PHE A 1 54  ? 141.063 96.103  107.321 1.00 36.13  ? 52  PHE A CG  1 
ATOM   278  C  CD1 . PHE A 1 54  ? 142.006 96.835  108.021 1.00 40.16  ? 52  PHE A CD1 1 
ATOM   279  C  CD2 . PHE A 1 54  ? 141.078 94.726  107.430 1.00 37.94  ? 52  PHE A CD2 1 
ATOM   280  C  CE1 . PHE A 1 54  ? 142.940 96.206  108.813 1.00 41.11  ? 52  PHE A CE1 1 
ATOM   281  C  CE2 . PHE A 1 54  ? 142.011 94.092  108.219 1.00 38.40  ? 52  PHE A CE2 1 
ATOM   282  C  CZ  . PHE A 1 54  ? 142.943 94.832  108.911 1.00 38.34  ? 52  PHE A CZ  1 
ATOM   283  N  N   . ALA A 1 55  ? 139.226 99.522  107.973 1.00 36.93  ? 53  ALA A N   1 
ATOM   284  C  CA  . ALA A 1 55  ? 139.589 100.569 108.914 1.00 32.65  ? 53  ALA A CA  1 
ATOM   285  C  C   . ALA A 1 55  ? 138.398 101.090 109.704 1.00 35.24  ? 53  ALA A C   1 
ATOM   286  O  O   . ALA A 1 55  ? 138.549 102.053 110.460 1.00 36.34  ? 53  ALA A O   1 
ATOM   287  C  CB  . ALA A 1 55  ? 140.260 101.725 108.173 1.00 35.73  ? 53  ALA A CB  1 
ATOM   288  N  N   . PHE A 1 56  ? 137.223 100.483 109.543 1.00 32.81  ? 54  PHE A N   1 
ATOM   289  C  CA  . PHE A 1 56  ? 136.038 100.977 110.238 1.00 28.38  ? 54  PHE A CA  1 
ATOM   290  C  C   . PHE A 1 56  ? 136.181 100.952 111.753 1.00 30.16  ? 54  PHE A C   1 
ATOM   291  O  O   . PHE A 1 56  ? 135.788 101.941 112.395 1.00 33.86  ? 54  PHE A O   1 
ATOM   292  C  CB  . PHE A 1 56  ? 134.807 100.174 109.802 1.00 28.94  ? 54  PHE A CB  1 
ATOM   293  C  CG  . PHE A 1 56  ? 133.528 100.655 110.418 1.00 26.36  ? 54  PHE A CG  1 
ATOM   294  C  CD1 . PHE A 1 56  ? 132.957 101.848 110.013 1.00 30.20  ? 54  PHE A CD1 1 
ATOM   295  C  CD2 . PHE A 1 56  ? 132.900 99.921  111.407 1.00 26.34  ? 54  PHE A CD2 1 
ATOM   296  C  CE1 . PHE A 1 56  ? 131.785 102.296 110.578 1.00 25.05  ? 54  PHE A CE1 1 
ATOM   297  C  CE2 . PHE A 1 56  ? 131.728 100.367 111.975 1.00 25.82  ? 54  PHE A CE2 1 
ATOM   298  C  CZ  . PHE A 1 56  ? 131.171 101.556 111.559 1.00 23.02  ? 54  PHE A CZ  1 
ATOM   299  N  N   . PRO A 1 57  ? 136.697 99.895  112.386 1.00 29.54  ? 55  PRO A N   1 
ATOM   300  C  CA  . PRO A 1 57  ? 136.845 99.940  113.848 1.00 24.73  ? 55  PRO A CA  1 
ATOM   301  C  C   . PRO A 1 57  ? 137.709 101.091 114.323 1.00 28.42  ? 55  PRO A C   1 
ATOM   302  O  O   . PRO A 1 57  ? 137.465 101.633 115.407 1.00 34.75  ? 55  PRO A O   1 
ATOM   303  C  CB  . PRO A 1 57  ? 137.471 98.580  114.177 1.00 25.18  ? 55  PRO A CB  1 
ATOM   304  C  CG  . PRO A 1 57  ? 137.100 97.707  113.041 1.00 25.85  ? 55  PRO A CG  1 
ATOM   305  C  CD  . PRO A 1 57  ? 137.096 98.588  111.839 1.00 30.27  ? 55  PRO A CD  1 
ATOM   306  N  N   . GLY A 1 58  ? 138.722 101.479 113.546 1.00 31.33  ? 56  GLY A N   1 
ATOM   307  C  CA  . GLY A 1 58  ? 139.492 102.661 113.882 1.00 31.78  ? 56  GLY A CA  1 
ATOM   308  C  C   . GLY A 1 58  ? 138.776 103.949 113.549 1.00 28.85  ? 56  GLY A C   1 
ATOM   309  O  O   . GLY A 1 58  ? 139.033 104.981 114.174 1.00 28.06  ? 56  GLY A O   1 
ATOM   310  N  N   . GLU A 1 59  ? 137.881 103.914 112.560 1.00 31.42  ? 57  GLU A N   1 
ATOM   311  C  CA  . GLU A 1 59  ? 137.061 105.081 112.257 1.00 27.59  ? 57  GLU A CA  1 
ATOM   312  C  C   . GLU A 1 59  ? 136.124 105.407 113.412 1.00 26.40  ? 57  GLU A C   1 
ATOM   313  O  O   . GLU A 1 59  ? 135.915 106.580 113.737 1.00 32.22  ? 57  GLU A O   1 
ATOM   314  C  CB  . GLU A 1 59  ? 136.266 104.837 110.976 1.00 28.23  ? 57  GLU A CB  1 
ATOM   315  C  CG  . GLU A 1 59  ? 135.233 105.904 110.668 1.00 33.52  ? 57  GLU A CG  1 
ATOM   316  C  CD  . GLU A 1 59  ? 134.492 105.635 109.381 1.00 38.11  ? 57  GLU A CD  1 
ATOM   317  O  OE1 . GLU A 1 59  ? 134.791 104.616 108.726 1.00 33.49  ? 57  GLU A OE1 1 
ATOM   318  O  OE2 . GLU A 1 59  ? 133.610 106.443 109.023 1.00 38.39  ? 57  GLU A OE2 1 
ATOM   319  N  N   . ILE A 1 60  ? 135.544 104.382 114.037 1.00 30.67  ? 58  ILE A N   1 
ATOM   320  C  CA  . ILE A 1 60  ? 134.632 104.607 115.153 1.00 23.44  ? 58  ILE A CA  1 
ATOM   321  C  C   . ILE A 1 60  ? 135.374 105.219 116.332 1.00 25.65  ? 58  ILE A C   1 
ATOM   322  O  O   . ILE A 1 60  ? 134.819 106.038 117.073 1.00 30.47  ? 58  ILE A O   1 
ATOM   323  C  CB  . ILE A 1 60  ? 133.934 103.290 115.538 1.00 27.58  ? 58  ILE A CB  1 
ATOM   324  C  CG1 . ILE A 1 60  ? 132.971 102.857 114.430 1.00 31.44  ? 58  ILE A CG1 1 
ATOM   325  C  CG2 . ILE A 1 60  ? 133.204 103.436 116.860 1.00 24.56  ? 58  ILE A CG2 1 
ATOM   326  C  CD1 . ILE A 1 60  ? 131.917 103.888 114.071 1.00 28.58  ? 58  ILE A CD1 1 
ATOM   327  N  N   . LEU A 1 61  ? 136.633 104.826 116.534 1.00 27.34  ? 59  LEU A N   1 
ATOM   328  C  CA  . LEU A 1 61  ? 137.436 105.447 117.580 1.00 23.43  ? 59  LEU A CA  1 
ATOM   329  C  C   . LEU A 1 61  ? 137.631 106.932 117.305 1.00 21.31  ? 59  LEU A C   1 
ATOM   330  O  O   . LEU A 1 61  ? 137.609 107.750 118.230 1.00 33.65  ? 59  LEU A O   1 
ATOM   331  C  CB  . LEU A 1 61  ? 138.787 104.741 117.690 1.00 31.35  ? 59  LEU A CB  1 
ATOM   332  C  CG  . LEU A 1 61  ? 139.736 105.254 118.773 1.00 27.82  ? 59  LEU A CG  1 
ATOM   333  C  CD1 . LEU A 1 61  ? 139.262 104.806 120.143 1.00 26.85  ? 59  LEU A CD1 1 
ATOM   334  C  CD2 . LEU A 1 61  ? 141.144 104.775 118.513 1.00 28.60  ? 59  LEU A CD2 1 
ATOM   335  N  N   . MET A 1 62  ? 137.831 107.299 116.039 1.00 19.04  ? 60  MET A N   1 
ATOM   336  C  CA  . MET A 1 62  ? 137.979 108.708 115.695 1.00 19.94  ? 60  MET A CA  1 
ATOM   337  C  C   . MET A 1 62  ? 136.703 109.484 115.989 1.00 26.49  ? 60  MET A C   1 
ATOM   338  O  O   . MET A 1 62  ? 136.758 110.641 116.417 1.00 35.56  ? 60  MET A O   1 
ATOM   339  C  CB  . MET A 1 62  ? 138.361 108.847 114.220 1.00 30.05  ? 60  MET A CB  1 
ATOM   340  C  CG  . MET A 1 62  ? 139.772 108.378 113.872 1.00 31.47  ? 60  MET A CG  1 
ATOM   341  S  SD  . MET A 1 62  ? 141.106 108.905 114.971 1.00 45.99  ? 60  MET A SD  1 
ATOM   342  C  CE  . MET A 1 62  ? 140.652 110.602 115.343 1.00 33.83  ? 60  MET A CE  1 
ATOM   343  N  N   . ARG A 1 63  ? 135.543 108.869 115.749 1.00 32.33  ? 61  ARG A N   1 
ATOM   344  C  CA  . ARG A 1 63  ? 134.280 109.524 116.073 1.00 17.36  ? 61  ARG A CA  1 
ATOM   345  C  C   . ARG A 1 63  ? 134.129 109.699 117.579 1.00 20.46  ? 61  ARG A C   1 
ATOM   346  O  O   . ARG A 1 63  ? 133.655 110.742 118.043 1.00 23.54  ? 61  ARG A O   1 
ATOM   347  C  CB  . ARG A 1 63  ? 133.100 108.724 115.517 1.00 19.12  ? 61  ARG A CB  1 
ATOM   348  C  CG  . ARG A 1 63  ? 133.287 108.148 114.116 1.00 26.21  ? 61  ARG A CG  1 
ATOM   349  C  CD  . ARG A 1 63  ? 132.523 108.913 113.063 1.00 28.04  ? 61  ARG A CD  1 
ATOM   350  N  NE  . ARG A 1 63  ? 131.109 109.063 113.376 1.00 23.37  ? 61  ARG A NE  1 
ATOM   351  C  CZ  . ARG A 1 63  ? 130.261 109.771 112.646 1.00 22.65  ? 61  ARG A CZ  1 
ATOM   352  N  NH1 . ARG A 1 63  ? 130.648 110.391 111.545 1.00 22.87  ? 61  ARG A NH1 1 
ATOM   353  N  NH2 . ARG A 1 63  ? 128.994 109.867 113.033 1.00 27.89  ? 61  ARG A NH2 1 
ATOM   354  N  N   . MET A 1 64  ? 134.518 108.686 118.356 1.00 29.06  ? 62  MET A N   1 
ATOM   355  C  CA  . MET A 1 64  ? 134.454 108.799 119.809 1.00 22.32  ? 62  MET A CA  1 
ATOM   356  C  C   . MET A 1 64  ? 135.356 109.915 120.312 1.00 21.64  ? 62  MET A C   1 
ATOM   357  O  O   . MET A 1 64  ? 134.978 110.675 121.208 1.00 33.63  ? 62  MET A O   1 
ATOM   358  C  CB  . MET A 1 64  ? 134.859 107.480 120.465 1.00 20.83  ? 62  MET A CB  1 
ATOM   359  C  CG  . MET A 1 64  ? 133.810 106.395 120.433 1.00 18.64  ? 62  MET A CG  1 
ATOM   360  S  SD  . MET A 1 64  ? 134.565 104.761 120.463 1.00 23.01  ? 62  MET A SD  1 
ATOM   361  C  CE  . MET A 1 64  ? 133.118 103.713 120.458 1.00 26.49  ? 62  MET A CE  1 
ATOM   362  N  N   . LEU A 1 65  ? 136.565 110.014 119.759 1.00 22.06  ? 63  LEU A N   1 
ATOM   363  C  CA  . LEU A 1 65  ? 137.508 111.026 120.220 1.00 24.31  ? 63  LEU A CA  1 
ATOM   364  C  C   . LEU A 1 65  ? 137.080 112.421 119.789 1.00 25.46  ? 63  LEU A C   1 
ATOM   365  O  O   . LEU A 1 65  ? 137.196 113.377 120.562 1.00 27.84  ? 63  LEU A O   1 
ATOM   366  C  CB  . LEU A 1 65  ? 138.906 110.705 119.700 1.00 32.53  ? 63  LEU A CB  1 
ATOM   367  C  CG  . LEU A 1 65  ? 139.534 109.451 120.308 1.00 25.83  ? 63  LEU A CG  1 
ATOM   368  C  CD1 . LEU A 1 65  ? 140.728 108.999 119.491 1.00 30.53  ? 63  LEU A CD1 1 
ATOM   369  C  CD2 . LEU A 1 65  ? 139.930 109.699 121.752 1.00 25.47  ? 63  LEU A CD2 1 
ATOM   370  N  N   . LYS A 1 66  ? 136.590 112.563 118.557 1.00 29.18  ? 64  LYS A N   1 
ATOM   371  C  CA  . LYS A 1 66  ? 136.096 113.859 118.113 1.00 23.11  ? 64  LYS A CA  1 
ATOM   372  C  C   . LYS A 1 66  ? 134.826 114.255 118.853 1.00 21.81  ? 64  LYS A C   1 
ATOM   373  O  O   . LYS A 1 66  ? 134.518 115.446 118.960 1.00 33.03  ? 64  LYS A O   1 
ATOM   374  C  CB  . LYS A 1 66  ? 135.852 113.838 116.604 1.00 23.13  ? 64  LYS A CB  1 
ATOM   375  C  CG  . LYS A 1 66  ? 137.124 113.916 115.781 1.00 28.51  ? 64  LYS A CG  1 
ATOM   376  C  CD  . LYS A 1 66  ? 136.842 113.860 114.291 1.00 26.81  ? 64  LYS A CD  1 
ATOM   377  C  CE  . LYS A 1 66  ? 136.451 112.460 113.851 1.00 37.89  ? 64  LYS A CE  1 
ATOM   378  N  NZ  . LYS A 1 66  ? 136.485 112.298 112.374 1.00 32.94  ? 64  LYS A NZ  1 
ATOM   379  N  N   . LEU A 1 67  ? 134.083 113.277 119.371 1.00 24.93  ? 65  LEU A N   1 
ATOM   380  C  CA  . LEU A 1 67  ? 132.854 113.577 120.096 1.00 24.43  ? 65  LEU A CA  1 
ATOM   381  C  C   . LEU A 1 67  ? 133.138 114.343 121.382 1.00 23.57  ? 65  LEU A C   1 
ATOM   382  O  O   . LEU A 1 67  ? 132.381 115.247 121.751 1.00 28.74  ? 65  LEU A O   1 
ATOM   383  C  CB  . LEU A 1 67  ? 132.104 112.279 120.391 1.00 27.57  ? 65  LEU A CB  1 
ATOM   384  C  CG  . LEU A 1 67  ? 130.865 112.353 121.282 1.00 21.66  ? 65  LEU A CG  1 
ATOM   385  C  CD1 . LEU A 1 67  ? 129.810 113.252 120.671 1.00 22.67  ? 65  LEU A CD1 1 
ATOM   386  C  CD2 . LEU A 1 67  ? 130.313 110.962 121.501 1.00 25.66  ? 65  LEU A CD2 1 
ATOM   387  N  N   . ILE A 1 68  ? 134.219 113.996 122.077 1.00 27.90  ? 66  ILE A N   1 
ATOM   388  C  CA  . ILE A 1 68  ? 134.519 114.585 123.378 1.00 25.33  ? 66  ILE A CA  1 
ATOM   389  C  C   . ILE A 1 68  ? 135.435 115.793 123.227 1.00 26.87  ? 66  ILE A C   1 
ATOM   390  O  O   . ILE A 1 68  ? 135.867 116.378 124.225 1.00 32.94  ? 66  ILE A O   1 
ATOM   391  C  CB  . ILE A 1 68  ? 135.148 113.552 124.335 1.00 28.56  ? 66  ILE A CB  1 
ATOM   392  C  CG1 . ILE A 1 68  ? 136.407 112.916 123.732 1.00 31.34  ? 66  ILE A CG1 1 
ATOM   393  C  CG2 . ILE A 1 68  ? 134.140 112.479 124.688 1.00 32.87  ? 66  ILE A CG2 1 
ATOM   394  C  CD1 . ILE A 1 68  ? 137.697 113.563 124.179 1.00 35.72  ? 66  ILE A CD1 1 
ATOM   395  N  N   . ILE A 1 69  ? 135.737 116.184 121.987 1.00 32.79  ? 67  ILE A N   1 
ATOM   396  C  CA  . ILE A 1 69  ? 136.597 117.345 121.773 1.00 29.02  ? 67  ILE A CA  1 
ATOM   397  C  C   . ILE A 1 69  ? 135.941 118.598 122.337 1.00 23.59  ? 67  ILE A C   1 
ATOM   398  O  O   . ILE A 1 69  ? 136.552 119.353 123.100 1.00 31.45  ? 67  ILE A O   1 
ATOM   399  C  CB  . ILE A 1 69  ? 136.921 117.509 120.276 1.00 30.43  ? 67  ILE A CB  1 
ATOM   400  C  CG1 . ILE A 1 69  ? 138.070 116.585 119.874 1.00 32.56  ? 67  ILE A CG1 1 
ATOM   401  C  CG2 . ILE A 1 69  ? 137.273 118.961 119.953 1.00 32.78  ? 67  ILE A CG2 1 
ATOM   402  C  CD1 . ILE A 1 69  ? 138.368 116.592 118.392 1.00 33.27  ? 67  ILE A CD1 1 
ATOM   403  N  N   . LEU A 1 70  ? 134.681 118.840 121.964 1.00 22.08  ? 68  LEU A N   1 
ATOM   404  C  CA  . LEU A 1 70  ? 134.009 120.053 122.424 1.00 23.38  ? 68  LEU A CA  1 
ATOM   405  C  C   . LEU A 1 70  ? 133.776 120.029 123.928 1.00 27.22  ? 68  LEU A C   1 
ATOM   406  O  O   . LEU A 1 70  ? 134.158 120.999 124.606 1.00 27.06  ? 68  LEU A O   1 
ATOM   407  C  CB  . LEU A 1 70  ? 132.711 120.250 121.635 1.00 28.31  ? 68  LEU A CB  1 
ATOM   408  C  CG  . LEU A 1 70  ? 131.624 121.173 122.191 1.00 32.33  ? 68  LEU A CG  1 
ATOM   409  C  CD1 . LEU A 1 70  ? 131.890 122.604 121.777 1.00 31.66  ? 68  LEU A CD1 1 
ATOM   410  C  CD2 . LEU A 1 70  ? 130.259 120.719 121.709 1.00 26.49  ? 68  LEU A CD2 1 
ATOM   411  N  N   . PRO A 1 71  ? 133.171 118.991 124.515 1.00 30.51  ? 69  PRO A N   1 
ATOM   412  C  CA  . PRO A 1 71  ? 133.016 118.986 125.978 1.00 23.30  ? 69  PRO A CA  1 
ATOM   413  C  C   . PRO A 1 71  ? 134.330 119.110 126.723 1.00 26.50  ? 69  PRO A C   1 
ATOM   414  O  O   . PRO A 1 71  ? 134.394 119.788 127.754 1.00 31.04  ? 69  PRO A O   1 
ATOM   415  C  CB  . PRO A 1 71  ? 132.340 117.636 126.253 1.00 22.80  ? 69  PRO A CB  1 
ATOM   416  C  CG  . PRO A 1 71  ? 131.697 117.256 124.988 1.00 28.30  ? 69  PRO A CG  1 
ATOM   417  C  CD  . PRO A 1 71  ? 132.512 117.836 123.884 1.00 27.97  ? 69  PRO A CD  1 
ATOM   418  N  N   . LEU A 1 72  ? 135.388 118.467 126.230 1.00 24.90  ? 70  LEU A N   1 
ATOM   419  C  CA  . LEU A 1 72  ? 136.655 118.470 126.949 1.00 25.06  ? 70  LEU A CA  1 
ATOM   420  C  C   . LEU A 1 72  ? 137.330 119.832 126.872 1.00 29.47  ? 70  LEU A C   1 
ATOM   421  O  O   . LEU A 1 72  ? 137.801 120.361 127.884 1.00 38.25  ? 70  LEU A O   1 
ATOM   422  C  CB  . LEU A 1 72  ? 137.568 117.380 126.388 1.00 32.86  ? 70  LEU A CB  1 
ATOM   423  C  CG  . LEU A 1 72  ? 138.850 117.043 127.152 1.00 35.71  ? 70  LEU A CG  1 
ATOM   424  C  CD1 . LEU A 1 72  ? 138.668 117.148 128.658 1.00 36.58  ? 70  LEU A CD1 1 
ATOM   425  C  CD2 . LEU A 1 72  ? 139.308 115.650 126.775 1.00 31.67  ? 70  LEU A CD2 1 
ATOM   426  N  N   . ILE A 1 73  ? 137.382 120.419 125.677 1.00 29.63  ? 71  ILE A N   1 
ATOM   427  C  CA  . ILE A 1 73  ? 138.059 121.699 125.508 1.00 29.93  ? 71  ILE A CA  1 
ATOM   428  C  C   . ILE A 1 73  ? 137.342 122.793 126.288 1.00 25.06  ? 71  ILE A C   1 
ATOM   429  O  O   . ILE A 1 73  ? 137.977 123.605 126.967 1.00 35.96  ? 71  ILE A O   1 
ATOM   430  C  CB  . ILE A 1 73  ? 138.171 122.041 124.011 1.00 31.71  ? 71  ILE A CB  1 
ATOM   431  C  CG1 . ILE A 1 73  ? 139.314 121.248 123.378 1.00 30.50  ? 71  ILE A CG1 1 
ATOM   432  C  CG2 . ILE A 1 73  ? 138.387 123.533 123.809 1.00 31.74  ? 71  ILE A CG2 1 
ATOM   433  C  CD1 . ILE A 1 73  ? 139.323 121.285 121.871 1.00 32.87  ? 71  ILE A CD1 1 
ATOM   434  N  N   . ILE A 1 74  ? 136.013 122.835 126.211 1.00 20.86  ? 72  ILE A N   1 
ATOM   435  C  CA  . ILE A 1 74  ? 135.273 123.916 126.854 1.00 21.93  ? 72  ILE A CA  1 
ATOM   436  C  C   . ILE A 1 74  ? 135.406 123.829 128.369 1.00 25.75  ? 72  ILE A C   1 
ATOM   437  O  O   . ILE A 1 74  ? 135.711 124.822 129.038 1.00 35.06  ? 72  ILE A O   1 
ATOM   438  C  CB  . ILE A 1 74  ? 133.800 123.892 126.409 1.00 26.43  ? 72  ILE A CB  1 
ATOM   439  C  CG1 . ILE A 1 74  ? 133.656 124.605 125.063 1.00 26.25  ? 72  ILE A CG1 1 
ATOM   440  C  CG2 . ILE A 1 74  ? 132.905 124.543 127.460 1.00 28.38  ? 72  ILE A CG2 1 
ATOM   441  C  CD1 . ILE A 1 74  ? 132.312 124.412 124.406 1.00 33.40  ? 72  ILE A CD1 1 
ATOM   442  N  N   . SER A 1 75  ? 135.183 122.643 128.934 1.00 28.54  ? 73  SER A N   1 
ATOM   443  C  CA  . SER A 1 75  ? 135.205 122.509 130.386 1.00 28.55  ? 73  SER A CA  1 
ATOM   444  C  C   . SER A 1 75  ? 136.622 122.531 130.945 1.00 26.29  ? 73  SER A C   1 
ATOM   445  O  O   . SER A 1 75  ? 136.817 122.926 132.098 1.00 26.96  ? 73  SER A O   1 
ATOM   446  C  CB  . SER A 1 75  ? 134.487 121.227 130.809 1.00 22.55  ? 73  SER A CB  1 
ATOM   447  O  OG  . SER A 1 75  ? 134.884 120.125 130.017 1.00 26.30  ? 73  SER A OG  1 
ATOM   448  N  N   . SER A 1 76  ? 137.616 122.114 130.158 1.00 25.61  ? 74  SER A N   1 
ATOM   449  C  CA  . SER A 1 76  ? 139.000 122.188 130.617 1.00 26.59  ? 74  SER A CA  1 
ATOM   450  C  C   . SER A 1 76  ? 139.467 123.635 130.723 1.00 36.35  ? 74  SER A C   1 
ATOM   451  O  O   . SER A 1 76  ? 140.098 124.021 131.713 1.00 41.45  ? 74  SER A O   1 
ATOM   452  C  CB  . SER A 1 76  ? 139.913 121.408 129.674 1.00 33.49  ? 74  SER A CB  1 
ATOM   453  O  OG  . SER A 1 76  ? 139.948 120.034 130.014 1.00 43.80  ? 74  SER A OG  1 
ATOM   454  N  N   . MET A 1 77  ? 139.177 124.448 129.705 1.00 32.16  ? 75  MET A N   1 
ATOM   455  C  CA  . MET A 1 77  ? 139.596 125.845 129.740 1.00 24.55  ? 75  MET A CA  1 
ATOM   456  C  C   . MET A 1 77  ? 138.895 126.605 130.856 1.00 31.69  ? 75  MET A C   1 
ATOM   457  O  O   . MET A 1 77  ? 139.528 127.378 131.581 1.00 39.15  ? 75  MET A O   1 
ATOM   458  C  CB  . MET A 1 77  ? 139.324 126.516 128.394 1.00 30.88  ? 75  MET A CB  1 
ATOM   459  C  CG  . MET A 1 77  ? 139.952 125.825 127.200 1.00 32.13  ? 75  MET A CG  1 
ATOM   460  S  SD  . MET A 1 77  ? 141.722 126.100 127.066 1.00 46.66  ? 75  MET A SD  1 
ATOM   461  C  CE  . MET A 1 77  ? 142.289 124.407 127.039 1.00 34.71  ? 75  MET A CE  1 
ATOM   462  N  N   . ILE A 1 78  ? 137.585 126.410 131.006 1.00 27.36  ? 76  ILE A N   1 
ATOM   463  C  CA  . ILE A 1 78  ? 136.848 127.125 132.044 1.00 28.03  ? 76  ILE A CA  1 
ATOM   464  C  C   . ILE A 1 78  ? 137.311 126.674 133.422 1.00 30.03  ? 76  ILE A C   1 
ATOM   465  O  O   . ILE A 1 78  ? 137.548 127.492 134.318 1.00 30.01  ? 76  ILE A O   1 
ATOM   466  C  CB  . ILE A 1 78  ? 135.332 126.925 131.864 1.00 22.71  ? 76  ILE A CB  1 
ATOM   467  C  CG1 . ILE A 1 78  ? 134.876 127.507 130.527 1.00 27.52  ? 76  ILE A CG1 1 
ATOM   468  C  CG2 . ILE A 1 78  ? 134.572 127.579 133.003 1.00 24.68  ? 76  ILE A CG2 1 
ATOM   469  C  CD1 . ILE A 1 78  ? 133.509 127.050 130.093 1.00 26.90  ? 76  ILE A CD1 1 
ATOM   470  N  N   . THR A 1 79  ? 137.450 125.362 133.610 1.00 31.70  ? 77  THR A N   1 
ATOM   471  C  CA  . THR A 1 79  ? 137.832 124.834 134.915 1.00 29.41  ? 77  THR A CA  1 
ATOM   472  C  C   . THR A 1 79  ? 139.225 125.301 135.317 1.00 28.76  ? 77  THR A C   1 
ATOM   473  O  O   . THR A 1 79  ? 139.448 125.698 136.466 1.00 37.10  ? 77  THR A O   1 
ATOM   474  C  CB  . THR A 1 79  ? 137.766 123.309 134.897 1.00 28.12  ? 77  THR A CB  1 
ATOM   475  O  OG1 . THR A 1 79  ? 136.460 122.891 134.485 1.00 34.17  ? 77  THR A OG1 1 
ATOM   476  C  CG2 . THR A 1 79  ? 138.069 122.748 136.269 1.00 27.30  ? 77  THR A CG2 1 
ATOM   477  N  N   . GLY A 1 80  ? 140.180 125.251 134.388 1.00 32.46  ? 78  GLY A N   1 
ATOM   478  C  CA  . GLY A 1 80  ? 141.542 125.628 134.730 1.00 32.48  ? 78  GLY A CA  1 
ATOM   479  C  C   . GLY A 1 80  ? 141.661 127.085 135.128 1.00 34.45  ? 78  GLY A C   1 
ATOM   480  O  O   . GLY A 1 80  ? 142.263 127.416 136.151 1.00 39.29  ? 78  GLY A O   1 
ATOM   481  N  N   . VAL A 1 81  ? 141.078 127.977 134.328 1.00 36.86  ? 79  VAL A N   1 
ATOM   482  C  CA  . VAL A 1 81  ? 141.166 129.407 134.614 1.00 29.53  ? 79  VAL A CA  1 
ATOM   483  C  C   . VAL A 1 81  ? 140.322 129.758 135.833 1.00 29.86  ? 79  VAL A C   1 
ATOM   484  O  O   . VAL A 1 81  ? 140.741 130.536 136.698 1.00 38.65  ? 79  VAL A O   1 
ATOM   485  C  CB  . VAL A 1 81  ? 140.751 130.230 133.382 1.00 32.88  ? 79  VAL A CB  1 
ATOM   486  C  CG1 . VAL A 1 81  ? 141.113 131.679 133.581 1.00 37.26  ? 79  VAL A CG1 1 
ATOM   487  C  CG2 . VAL A 1 81  ? 141.439 129.717 132.131 1.00 32.30  ? 79  VAL A CG2 1 
ATOM   488  N  N   . ALA A 1 82  ? 139.115 129.199 135.914 1.00 32.14  ? 80  ALA A N   1 
ATOM   489  C  CA  . ALA A 1 82  ? 138.242 129.494 137.045 1.00 31.50  ? 80  ALA A CA  1 
ATOM   490  C  C   . ALA A 1 82  ? 138.867 129.041 138.357 1.00 36.00  ? 80  ALA A C   1 
ATOM   491  O  O   . ALA A 1 82  ? 138.670 129.676 139.399 1.00 37.02  ? 80  ALA A O   1 
ATOM   492  C  CB  . ALA A 1 82  ? 136.882 128.830 136.841 1.00 26.61  ? 80  ALA A CB  1 
ATOM   493  N  N   . ALA A 1 83  ? 139.616 127.936 138.330 1.00 36.71  ? 81  ALA A N   1 
ATOM   494  C  CA  . ALA A 1 83  ? 140.234 127.431 139.552 1.00 34.51  ? 81  ALA A CA  1 
ATOM   495  C  C   . ALA A 1 83  ? 141.286 128.395 140.082 1.00 39.08  ? 81  ALA A C   1 
ATOM   496  O  O   . ALA A 1 83  ? 141.430 128.561 141.299 1.00 39.86  ? 81  ALA A O   1 
ATOM   497  C  CB  . ALA A 1 83  ? 140.848 126.057 139.295 1.00 33.68  ? 81  ALA A CB  1 
ATOM   498  N  N   . LEU A 1 84  ? 142.038 129.033 139.187 1.00 43.28  ? 82  LEU A N   1 
ATOM   499  C  CA  . LEU A 1 84  ? 143.087 129.961 139.590 1.00 42.99  ? 82  LEU A CA  1 
ATOM   500  C  C   . LEU A 1 84  ? 142.525 131.074 140.463 1.00 44.17  ? 82  LEU A C   1 
ATOM   501  O  O   . LEU A 1 84  ? 141.734 131.899 139.995 1.00 43.52  ? 82  LEU A O   1 
ATOM   502  C  CB  . LEU A 1 84  ? 143.772 130.555 138.357 1.00 40.08  ? 82  LEU A CB  1 
ATOM   503  C  CG  . LEU A 1 84  ? 145.095 129.920 137.929 1.00 44.17  ? 82  LEU A CG  1 
ATOM   504  C  CD1 . LEU A 1 84  ? 145.010 128.405 137.932 1.00 45.15  ? 82  LEU A CD1 1 
ATOM   505  C  CD2 . LEU A 1 84  ? 145.488 130.430 136.555 1.00 42.36  ? 82  LEU A CD2 1 
ATOM   506  N  N   . ASP A 1 85  ? 142.933 131.109 141.728 1.00 44.86  ? 83  ASP A N   1 
ATOM   507  C  CA  . ASP A 1 85  ? 142.475 132.148 142.642 1.00 50.98  ? 83  ASP A CA  1 
ATOM   508  C  C   . ASP A 1 85  ? 142.824 133.524 142.097 1.00 49.19  ? 83  ASP A C   1 
ATOM   509  O  O   . ASP A 1 85  ? 143.968 133.782 141.712 1.00 47.41  ? 83  ASP A O   1 
ATOM   510  C  CB  . ASP A 1 85  ? 143.106 131.941 144.020 1.00 50.05  ? 83  ASP A CB  1 
ATOM   511  C  CG  . ASP A 1 85  ? 142.865 130.548 144.566 1.00 51.73  ? 83  ASP A CG  1 
ATOM   512  O  OD1 . ASP A 1 85  ? 142.187 129.752 143.884 1.00 51.83  ? 83  ASP A OD1 1 
ATOM   513  O  OD2 . ASP A 1 85  ? 143.353 130.248 145.675 1.00 51.03  ? 83  ASP A OD2 1 
ATOM   514  N  N   . SER A 1 86  ? 141.831 134.413 142.072 1.00 49.38  ? 84  SER A N   1 
ATOM   515  C  CA  . SER A 1 86  ? 142.030 135.727 141.468 1.00 51.81  ? 84  SER A CA  1 
ATOM   516  C  C   . SER A 1 86  ? 143.113 136.516 142.190 1.00 50.42  ? 84  SER A C   1 
ATOM   517  O  O   . SER A 1 86  ? 143.863 137.273 141.561 1.00 48.54  ? 84  SER A O   1 
ATOM   518  C  CB  . SER A 1 86  ? 140.716 136.506 141.476 1.00 47.99  ? 84  SER A CB  1 
ATOM   519  O  OG  . SER A 1 86  ? 139.675 135.746 140.893 1.00 45.98  ? 84  SER A OG  1 
ATOM   520  N  N   . ASN A 1 87  ? 143.209 136.354 143.510 1.00 51.73  ? 85  ASN A N   1 
ATOM   521  C  CA  . ASN A 1 87  ? 144.129 137.144 144.320 1.00 55.40  ? 85  ASN A CA  1 
ATOM   522  C  C   . ASN A 1 87  ? 145.533 137.167 143.731 1.00 54.56  ? 85  ASN A C   1 
ATOM   523  O  O   . ASN A 1 87  ? 146.042 138.235 143.377 1.00 52.05  ? 85  ASN A O   1 
ATOM   524  C  CB  . ASN A 1 87  ? 144.174 136.601 145.751 1.00 52.59  ? 85  ASN A CB  1 
ATOM   525  C  CG  . ASN A 1 87  ? 142.797 136.493 146.379 1.00 55.25  ? 85  ASN A CG  1 
ATOM   526  O  OD1 . ASN A 1 87  ? 141.794 136.865 145.768 1.00 53.78  ? 85  ASN A OD1 1 
ATOM   527  N  ND2 . ASN A 1 87  ? 142.741 135.983 147.603 1.00 49.72  ? 85  ASN A ND2 1 
ATOM   528  N  N   . VAL A 1 88  ? 146.170 136.001 143.617 1.00 53.99  ? 86  VAL A N   1 
ATOM   529  C  CA  . VAL A 1 88  ? 147.534 135.933 143.101 1.00 55.58  ? 86  VAL A CA  1 
ATOM   530  C  C   . VAL A 1 88  ? 147.759 134.792 142.124 1.00 51.41  ? 86  VAL A C   1 
ATOM   531  O  O   . VAL A 1 88  ? 148.749 134.821 141.372 1.00 50.20  ? 86  VAL A O   1 
ATOM   532  C  CB  . VAL A 1 88  ? 148.547 135.843 144.264 1.00 54.42  ? 86  VAL A CB  1 
ATOM   533  C  CG1 . VAL A 1 88  ? 148.478 137.097 145.121 1.00 49.91  ? 86  VAL A CG1 1 
ATOM   534  C  CG2 . VAL A 1 88  ? 148.292 134.600 145.102 1.00 48.61  ? 86  VAL A CG2 1 
ATOM   535  N  N   . SER A 1 89  ? 146.900 133.773 142.068 1.00 48.56  ? 87  SER A N   1 
ATOM   536  C  CA  . SER A 1 89  ? 147.142 132.666 141.153 1.00 47.00  ? 87  SER A CA  1 
ATOM   537  C  C   . SER A 1 89  ? 147.077 133.106 139.698 1.00 45.79  ? 87  SER A C   1 
ATOM   538  O  O   . SER A 1 89  ? 147.494 132.352 138.812 1.00 46.90  ? 87  SER A O   1 
ATOM   539  C  CB  . SER A 1 89  ? 146.140 131.541 141.406 1.00 47.98  ? 87  SER A CB  1 
ATOM   540  O  OG  . SER A 1 89  ? 146.148 131.149 142.767 1.00 49.46  ? 87  SER A OG  1 
ATOM   541  N  N   . GLY A 1 90  ? 146.560 134.306 139.429 1.00 44.68  ? 88  GLY A N   1 
ATOM   542  C  CA  . GLY A 1 90  ? 146.563 134.807 138.065 1.00 47.65  ? 88  GLY A CA  1 
ATOM   543  C  C   . GLY A 1 90  ? 147.960 134.882 137.479 1.00 50.00  ? 88  GLY A C   1 
ATOM   544  O  O   . GLY A 1 90  ? 148.159 134.625 136.290 1.00 51.60  ? 88  GLY A O   1 
ATOM   545  N  N   . LYS A 1 91  ? 148.948 135.240 138.305 1.00 50.88  ? 89  LYS A N   1 
ATOM   546  C  CA  . LYS A 1 91  ? 150.329 135.251 137.834 1.00 49.00  ? 89  LYS A CA  1 
ATOM   547  C  C   . LYS A 1 91  ? 150.766 133.856 137.406 1.00 47.10  ? 89  LYS A C   1 
ATOM   548  O  O   . LYS A 1 91  ? 151.489 133.700 136.415 1.00 48.04  ? 89  LYS A O   1 
ATOM   549  C  CB  . LYS A 1 91  ? 151.262 135.792 138.919 1.00 45.47  ? 89  LYS A CB  1 
ATOM   550  C  CG  . LYS A 1 91  ? 150.819 137.101 139.558 1.00 46.63  ? 89  LYS A CG  1 
ATOM   551  C  CD  . LYS A 1 91  ? 151.684 137.440 140.765 1.00 50.67  ? 89  LYS A CD  1 
ATOM   552  C  CE  . LYS A 1 91  ? 151.206 138.699 141.473 1.00 53.21  ? 89  LYS A CE  1 
ATOM   553  N  NZ  . LYS A 1 91  ? 149.786 138.607 141.909 1.00 54.13  ? 89  LYS A NZ  1 
ATOM   554  N  N   . ILE A 1 92  ? 150.336 132.830 138.142 1.00 44.26  ? 90  ILE A N   1 
ATOM   555  C  CA  . ILE A 1 92  ? 150.620 131.456 137.737 1.00 46.38  ? 90  ILE A CA  1 
ATOM   556  C  C   . ILE A 1 92  ? 150.031 131.184 136.360 1.00 49.84  ? 90  ILE A C   1 
ATOM   557  O  O   . ILE A 1 92  ? 150.630 130.480 135.538 1.00 50.78  ? 90  ILE A O   1 
ATOM   558  C  CB  . ILE A 1 92  ? 150.082 130.464 138.786 1.00 46.90  ? 90  ILE A CB  1 
ATOM   559  C  CG1 . ILE A 1 92  ? 150.628 130.804 140.175 1.00 47.01  ? 90  ILE A CG1 1 
ATOM   560  C  CG2 . ILE A 1 92  ? 150.446 129.033 138.405 1.00 46.16  ? 90  ILE A CG2 1 
ATOM   561  C  CD1 . ILE A 1 92  ? 150.154 129.874 141.267 1.00 47.67  ? 90  ILE A CD1 1 
ATOM   562  N  N   . GLY A 1 93  ? 148.841 131.723 136.093 1.00 44.36  ? 91  GLY A N   1 
ATOM   563  C  CA  . GLY A 1 93  ? 148.249 131.559 134.777 1.00 41.71  ? 91  GLY A CA  1 
ATOM   564  C  C   . GLY A 1 93  ? 149.030 132.280 133.696 1.00 42.82  ? 91  GLY A C   1 
ATOM   565  O  O   . GLY A 1 93  ? 149.260 131.738 132.612 1.00 47.64  ? 91  GLY A O   1 
ATOM   566  N  N   . LEU A 1 94  ? 149.445 133.518 133.974 1.00 45.37  ? 92  LEU A N   1 
ATOM   567  C  CA  . LEU A 1 94  ? 150.187 134.287 132.980 1.00 46.35  ? 92  LEU A CA  1 
ATOM   568  C  C   . LEU A 1 94  ? 151.531 133.641 132.675 1.00 42.52  ? 92  LEU A C   1 
ATOM   569  O  O   . LEU A 1 94  ? 151.985 133.646 131.526 1.00 41.89  ? 92  LEU A O   1 
ATOM   570  C  CB  . LEU A 1 94  ? 150.382 135.723 133.466 1.00 47.82  ? 92  LEU A CB  1 
ATOM   571  C  CG  . LEU A 1 94  ? 151.057 136.668 132.470 1.00 49.31  ? 92  LEU A CG  1 
ATOM   572  C  CD1 . LEU A 1 94  ? 150.134 136.971 131.299 1.00 46.69  ? 92  LEU A CD1 1 
ATOM   573  C  CD2 . LEU A 1 94  ? 151.487 137.949 133.163 1.00 42.24  ? 92  LEU A CD2 1 
ATOM   574  N  N   . ARG A 1 95  ? 152.192 133.094 133.695 1.00 43.76  ? 93  ARG A N   1 
ATOM   575  C  CA  . ARG A 1 95  ? 153.469 132.428 133.475 1.00 41.94  ? 93  ARG A CA  1 
ATOM   576  C  C   . ARG A 1 95  ? 153.317 131.243 132.533 1.00 45.61  ? 93  ARG A C   1 
ATOM   577  O  O   . ARG A 1 95  ? 154.250 130.896 131.801 1.00 44.91  ? 93  ARG A O   1 
ATOM   578  C  CB  . ARG A 1 95  ? 154.051 131.979 134.813 1.00 43.26  ? 93  ARG A CB  1 
ATOM   579  C  CG  . ARG A 1 95  ? 154.625 133.113 135.635 1.00 42.29  ? 93  ARG A CG  1 
ATOM   580  C  CD  . ARG A 1 95  ? 154.615 132.783 137.111 1.00 44.67  ? 93  ARG A CD  1 
ATOM   581  N  NE  . ARG A 1 95  ? 155.283 133.808 137.903 1.00 46.32  ? 93  ARG A NE  1 
ATOM   582  C  CZ  . ARG A 1 95  ? 155.111 133.982 139.206 1.00 48.59  ? 93  ARG A CZ  1 
ATOM   583  N  NH1 . ARG A 1 95  ? 154.278 133.224 139.900 1.00 45.17  ? 93  ARG A NH1 1 
ATOM   584  N  NH2 . ARG A 1 95  ? 155.789 134.941 139.828 1.00 51.02  ? 93  ARG A NH2 1 
ATOM   585  N  N   . ALA A 1 96  ? 152.148 130.601 132.546 1.00 42.46  ? 94  ALA A N   1 
ATOM   586  C  CA  . ALA A 1 96  ? 151.922 129.440 131.694 1.00 37.43  ? 94  ALA A CA  1 
ATOM   587  C  C   . ALA A 1 96  ? 151.763 129.845 130.234 1.00 42.24  ? 94  ALA A C   1 
ATOM   588  O  O   . ALA A 1 96  ? 152.344 129.223 129.339 1.00 51.39  ? 94  ALA A O   1 
ATOM   589  C  CB  . ALA A 1 96  ? 150.690 128.675 132.174 1.00 42.71  ? 94  ALA A CB  1 
ATOM   590  N  N   . VAL A 1 97  ? 150.970 130.887 129.971 1.00 42.12  ? 95  VAL A N   1 
ATOM   591  C  CA  . VAL A 1 97  ? 150.705 131.280 128.589 1.00 39.93  ? 95  VAL A CA  1 
ATOM   592  C  C   . VAL A 1 97  ? 151.971 131.787 127.920 1.00 38.34  ? 95  VAL A C   1 
ATOM   593  O  O   . VAL A 1 97  ? 152.162 131.601 126.712 1.00 41.69  ? 95  VAL A O   1 
ATOM   594  C  CB  . VAL A 1 97  ? 149.573 132.329 128.523 1.00 40.11  ? 95  VAL A CB  1 
ATOM   595  C  CG1 . VAL A 1 97  ? 148.440 131.951 129.455 1.00 45.19  ? 95  VAL A CG1 1 
ATOM   596  C  CG2 . VAL A 1 97  ? 150.094 133.717 128.840 1.00 40.09  ? 95  VAL A CG2 1 
ATOM   597  N  N   . VAL A 1 98  ? 152.846 132.450 128.675 1.00 36.49  ? 96  VAL A N   1 
ATOM   598  C  CA  . VAL A 1 98  ? 154.126 132.878 128.119 1.00 37.83  ? 96  VAL A CA  1 
ATOM   599  C  C   . VAL A 1 98  ? 154.956 131.663 127.723 1.00 40.31  ? 96  VAL A C   1 
ATOM   600  O  O   . VAL A 1 98  ? 155.568 131.630 126.649 1.00 42.86  ? 96  VAL A O   1 
ATOM   601  C  CB  . VAL A 1 98  ? 154.880 133.771 129.119 1.00 39.94  ? 96  VAL A CB  1 
ATOM   602  C  CG1 . VAL A 1 98  ? 156.275 134.087 128.599 1.00 36.09  ? 96  VAL A CG1 1 
ATOM   603  C  CG2 . VAL A 1 98  ? 154.106 135.050 129.372 1.00 41.50  ? 96  VAL A CG2 1 
ATOM   604  N  N   . TYR A 1 99  ? 154.991 130.648 128.589 1.00 37.50  ? 97  TYR A N   1 
ATOM   605  C  CA  . TYR A 1 99  ? 155.696 129.416 128.254 1.00 33.30  ? 97  TYR A CA  1 
ATOM   606  C  C   . TYR A 1 99  ? 155.060 128.724 127.055 1.00 35.46  ? 97  TYR A C   1 
ATOM   607  O  O   . TYR A 1 99  ? 155.764 128.235 126.166 1.00 39.51  ? 97  TYR A O   1 
ATOM   608  C  CB  . TYR A 1 99  ? 155.714 128.476 129.458 1.00 35.99  ? 97  TYR A CB  1 
ATOM   609  C  CG  . TYR A 1 99  ? 156.202 127.085 129.127 1.00 40.41  ? 97  TYR A CG  1 
ATOM   610  C  CD1 . TYR A 1 99  ? 157.551 126.770 129.189 1.00 35.27  ? 97  TYR A CD1 1 
ATOM   611  C  CD2 . TYR A 1 99  ? 155.314 126.087 128.747 1.00 42.61  ? 97  TYR A CD2 1 
ATOM   612  C  CE1 . TYR A 1 99  ? 158.000 125.504 128.885 1.00 36.33  ? 97  TYR A CE1 1 
ATOM   613  C  CE2 . TYR A 1 99  ? 155.756 124.822 128.439 1.00 36.82  ? 97  TYR A CE2 1 
ATOM   614  C  CZ  . TYR A 1 99  ? 157.099 124.534 128.512 1.00 36.10  ? 97  TYR A CZ  1 
ATOM   615  O  OH  . TYR A 1 99  ? 157.543 123.269 128.208 1.00 41.06  ? 97  TYR A OH  1 
ATOM   616  N  N   . TYR A 1 100 ? 153.726 128.668 127.015 1.00 31.47  ? 98  TYR A N   1 
ATOM   617  C  CA  . TYR A 1 100 ? 153.053 128.040 125.884 1.00 28.80  ? 98  TYR A CA  1 
ATOM   618  C  C   . TYR A 1 100 ? 153.413 128.733 124.579 1.00 35.30  ? 98  TYR A C   1 
ATOM   619  O  O   . TYR A 1 100 ? 153.686 128.075 123.570 1.00 40.94  ? 98  TYR A O   1 
ATOM   620  C  CB  . TYR A 1 100 ? 151.537 128.075 126.077 1.00 29.43  ? 98  TYR A CB  1 
ATOM   621  C  CG  . TYR A 1 100 ? 151.001 127.237 127.213 1.00 37.09  ? 98  TYR A CG  1 
ATOM   622  C  CD1 . TYR A 1 100 ? 151.747 126.210 127.772 1.00 40.90  ? 98  TYR A CD1 1 
ATOM   623  C  CD2 . TYR A 1 100 ? 149.734 127.476 127.722 1.00 37.08  ? 98  TYR A CD2 1 
ATOM   624  C  CE1 . TYR A 1 100 ? 151.244 125.447 128.804 1.00 39.72  ? 98  TYR A CE1 1 
ATOM   625  C  CE2 . TYR A 1 100 ? 149.226 126.723 128.752 1.00 33.90  ? 98  TYR A CE2 1 
ATOM   626  C  CZ  . TYR A 1 100 ? 149.983 125.712 129.291 1.00 38.84  ? 98  TYR A CZ  1 
ATOM   627  O  OH  . TYR A 1 100 ? 149.467 124.964 130.318 1.00 45.82  ? 98  TYR A OH  1 
ATOM   628  N  N   . PHE A 1 101 ? 153.405 130.065 124.579 1.00 41.94  ? 99  PHE A N   1 
ATOM   629  C  CA  . PHE A 1 101 ? 153.639 130.807 123.348 1.00 36.24  ? 99  PHE A CA  1 
ATOM   630  C  C   . PHE A 1 101 ? 155.105 130.753 122.941 1.00 39.23  ? 99  PHE A C   1 
ATOM   631  O  O   . PHE A 1 101 ? 155.420 130.602 121.755 1.00 39.83  ? 99  PHE A O   1 
ATOM   632  C  CB  . PHE A 1 101 ? 153.177 132.252 123.528 1.00 35.76  ? 99  PHE A CB  1 
ATOM   633  C  CG  . PHE A 1 101 ? 153.290 133.086 122.287 1.00 42.14  ? 99  PHE A CG  1 
ATOM   634  C  CD1 . PHE A 1 101 ? 152.448 132.864 121.211 1.00 39.77  ? 99  PHE A CD1 1 
ATOM   635  C  CD2 . PHE A 1 101 ? 154.236 134.091 122.196 1.00 41.07  ? 99  PHE A CD2 1 
ATOM   636  C  CE1 . PHE A 1 101 ? 152.547 133.629 120.069 1.00 41.54  ? 99  PHE A CE1 1 
ATOM   637  C  CE2 . PHE A 1 101 ? 154.340 134.858 121.057 1.00 41.98  ? 99  PHE A CE2 1 
ATOM   638  C  CZ  . PHE A 1 101 ? 153.494 134.628 119.992 1.00 44.50  ? 99  PHE A CZ  1 
ATOM   639  N  N   . ALA A 1 102 ? 156.015 130.873 123.909 1.00 34.50  ? 100 ALA A N   1 
ATOM   640  C  CA  . ALA A 1 102 ? 157.440 130.878 123.593 1.00 30.59  ? 100 ALA A CA  1 
ATOM   641  C  C   . ALA A 1 102 ? 157.875 129.553 122.983 1.00 36.97  ? 100 ALA A C   1 
ATOM   642  O  O   . ALA A 1 102 ? 158.596 129.525 121.980 1.00 36.30  ? 100 ALA A O   1 
ATOM   643  C  CB  . ALA A 1 102 ? 158.250 131.178 124.854 1.00 28.50  ? 100 ALA A CB  1 
ATOM   644  N  N   . THR A 1 103 ? 157.447 128.440 123.578 1.00 38.77  ? 101 THR A N   1 
ATOM   645  C  CA  . THR A 1 103 ? 157.873 127.133 123.089 1.00 34.43  ? 101 THR A CA  1 
ATOM   646  C  C   . THR A 1 103 ? 157.276 126.832 121.720 1.00 38.02  ? 101 THR A C   1 
ATOM   647  O  O   . THR A 1 103 ? 157.935 126.225 120.870 1.00 37.84  ? 101 THR A O   1 
ATOM   648  C  CB  . THR A 1 103 ? 157.489 126.048 124.092 1.00 36.17  ? 101 THR A CB  1 
ATOM   649  O  OG1 . THR A 1 103 ? 156.126 126.225 124.496 1.00 32.03  ? 101 THR A OG1 1 
ATOM   650  C  CG2 . THR A 1 103 ? 158.388 126.114 125.312 1.00 37.93  ? 101 THR A CG2 1 
ATOM   651  N  N   . THR A 1 104 ? 156.026 127.237 121.492 1.00 34.43  ? 102 THR A N   1 
ATOM   652  C  CA  . THR A 1 104 ? 155.411 127.029 120.185 1.00 33.64  ? 102 THR A CA  1 
ATOM   653  C  C   . THR A 1 104 ? 156.112 127.846 119.107 1.00 32.65  ? 102 THR A C   1 
ATOM   654  O  O   . THR A 1 104 ? 156.319 127.359 117.991 1.00 38.23  ? 102 THR A O   1 
ATOM   655  C  CB  . THR A 1 104 ? 153.926 127.380 120.244 1.00 40.01  ? 102 THR A CB  1 
ATOM   656  O  OG1 . THR A 1 104 ? 153.301 126.637 121.298 1.00 37.76  ? 102 THR A OG1 1 
ATOM   657  C  CG2 . THR A 1 104 ? 153.246 127.052 118.929 1.00 37.50  ? 102 THR A CG2 1 
ATOM   658  N  N   . LEU A 1 105 ? 156.476 129.091 119.415 1.00 34.67  ? 103 LEU A N   1 
ATOM   659  C  CA  . LEU A 1 105 ? 157.221 129.897 118.454 1.00 33.77  ? 103 LEU A CA  1 
ATOM   660  C  C   . LEU A 1 105 ? 158.580 129.281 118.160 1.00 36.43  ? 103 LEU A C   1 
ATOM   661  O  O   . LEU A 1 105 ? 159.017 129.249 117.005 1.00 46.54  ? 103 LEU A O   1 
ATOM   662  C  CB  . LEU A 1 105 ? 157.392 131.323 118.979 1.00 37.86  ? 103 LEU A CB  1 
ATOM   663  C  CG  . LEU A 1 105 ? 156.181 132.262 119.003 1.00 43.09  ? 103 LEU A CG  1 
ATOM   664  C  CD1 . LEU A 1 105 ? 156.647 133.696 118.800 1.00 40.48  ? 103 LEU A CD1 1 
ATOM   665  C  CD2 . LEU A 1 105 ? 155.133 131.893 117.963 1.00 42.04  ? 103 LEU A CD2 1 
ATOM   666  N  N   . ILE A 1 106 ? 159.265 128.789 119.193 1.00 32.12  ? 104 ILE A N   1 
ATOM   667  C  CA  . ILE A 1 106 ? 160.569 128.168 118.986 1.00 34.01  ? 104 ILE A CA  1 
ATOM   668  C  C   . ILE A 1 106 ? 160.433 126.937 118.101 1.00 37.39  ? 104 ILE A C   1 
ATOM   669  O  O   . ILE A 1 106 ? 161.244 126.712 117.195 1.00 39.36  ? 104 ILE A O   1 
ATOM   670  C  CB  . ILE A 1 106 ? 161.220 127.822 120.338 1.00 32.73  ? 104 ILE A CB  1 
ATOM   671  C  CG1 . ILE A 1 106 ? 161.550 129.095 121.118 1.00 37.59  ? 104 ILE A CG1 1 
ATOM   672  C  CG2 . ILE A 1 106 ? 162.479 127.011 120.122 1.00 35.26  ? 104 ILE A CG2 1 
ATOM   673  C  CD1 . ILE A 1 106 ? 161.689 128.878 122.605 1.00 35.08  ? 104 ILE A CD1 1 
ATOM   674  N  N   . ALA A 1 107 ? 159.411 126.117 118.353 1.00 38.11  ? 105 ALA A N   1 
ATOM   675  C  CA  . ALA A 1 107 ? 159.192 124.936 117.526 1.00 33.54  ? 105 ALA A CA  1 
ATOM   676  C  C   . ALA A 1 107 ? 158.891 125.321 116.084 1.00 34.75  ? 105 ALA A C   1 
ATOM   677  O  O   . ALA A 1 107 ? 159.396 124.693 115.147 1.00 40.34  ? 105 ALA A O   1 
ATOM   678  C  CB  . ALA A 1 107 ? 158.054 124.098 118.105 1.00 35.76  ? 105 ALA A CB  1 
ATOM   679  N  N   . VAL A 1 108 ? 158.061 126.346 115.885 1.00 36.72  ? 106 VAL A N   1 
ATOM   680  C  CA  . VAL A 1 108 ? 157.746 126.799 114.534 1.00 31.40  ? 106 VAL A CA  1 
ATOM   681  C  C   . VAL A 1 108 ? 158.990 127.348 113.851 1.00 34.82  ? 106 VAL A C   1 
ATOM   682  O  O   . VAL A 1 108 ? 159.258 127.050 112.682 1.00 41.10  ? 106 VAL A O   1 
ATOM   683  C  CB  . VAL A 1 108 ? 156.618 127.845 114.576 1.00 35.74  ? 106 VAL A CB  1 
ATOM   684  C  CG1 . VAL A 1 108 ? 156.516 128.571 113.253 1.00 36.54  ? 106 VAL A CG1 1 
ATOM   685  C  CG2 . VAL A 1 108 ? 155.306 127.185 114.920 1.00 36.95  ? 106 VAL A CG2 1 
ATOM   686  N  N   . ILE A 1 109 ? 159.764 128.169 114.563 1.00 34.58  ? 107 ILE A N   1 
ATOM   687  C  CA  . ILE A 1 109 ? 160.980 128.730 113.981 1.00 35.06  ? 107 ILE A CA  1 
ATOM   688  C  C   . ILE A 1 109 ? 161.979 127.623 113.675 1.00 38.24  ? 107 ILE A C   1 
ATOM   689  O  O   . ILE A 1 109 ? 162.611 127.614 112.613 1.00 42.74  ? 107 ILE A O   1 
ATOM   690  C  CB  . ILE A 1 109 ? 161.580 129.793 114.919 1.00 38.78  ? 107 ILE A CB  1 
ATOM   691  C  CG1 . ILE A 1 109 ? 160.677 131.027 114.964 1.00 38.12  ? 107 ILE A CG1 1 
ATOM   692  C  CG2 . ILE A 1 109 ? 162.979 130.175 114.466 1.00 33.96  ? 107 ILE A CG2 1 
ATOM   693  C  CD1 . ILE A 1 109 ? 160.875 131.884 116.192 1.00 32.70  ? 107 ILE A CD1 1 
ATOM   694  N  N   . LEU A 1 110 ? 162.135 126.670 114.596 1.00 30.50  ? 108 LEU A N   1 
ATOM   695  C  CA  . LEU A 1 110 ? 163.039 125.552 114.349 1.00 33.40  ? 108 LEU A CA  1 
ATOM   696  C  C   . LEU A 1 110 ? 162.595 124.746 113.137 1.00 39.59  ? 108 LEU A C   1 
ATOM   697  O  O   . LEU A 1 110 ? 163.426 124.329 112.322 1.00 39.90  ? 108 LEU A O   1 
ATOM   698  C  CB  . LEU A 1 110 ? 163.116 124.656 115.584 1.00 38.46  ? 108 LEU A CB  1 
ATOM   699  C  CG  . LEU A 1 110 ? 163.801 123.301 115.383 1.00 42.97  ? 108 LEU A CG  1 
ATOM   700  C  CD1 . LEU A 1 110 ? 165.260 123.492 115.001 1.00 35.82  ? 108 LEU A CD1 1 
ATOM   701  C  CD2 . LEU A 1 110 ? 163.678 122.456 116.630 1.00 40.35  ? 108 LEU A CD2 1 
ATOM   702  N  N   . GLY A 1 111 ? 161.291 124.508 113.005 1.00 41.97  ? 109 GLY A N   1 
ATOM   703  C  CA  . GLY A 1 111 ? 160.802 123.750 111.866 1.00 40.14  ? 109 GLY A CA  1 
ATOM   704  C  C   . GLY A 1 111 ? 161.072 124.442 110.545 1.00 38.64  ? 109 GLY A C   1 
ATOM   705  O  O   . GLY A 1 111 ? 161.458 123.801 109.566 1.00 41.81  ? 109 GLY A O   1 
ATOM   706  N  N   . ILE A 1 112 ? 160.875 125.760 110.498 1.00 41.63  ? 110 ILE A N   1 
ATOM   707  C  CA  . ILE A 1 112 ? 161.084 126.497 109.256 1.00 40.22  ? 110 ILE A CA  1 
ATOM   708  C  C   . ILE A 1 112 ? 162.558 126.497 108.874 1.00 39.02  ? 110 ILE A C   1 
ATOM   709  O  O   . ILE A 1 112 ? 162.905 126.427 107.690 1.00 42.77  ? 110 ILE A O   1 
ATOM   710  C  CB  . ILE A 1 112 ? 160.533 127.927 109.386 1.00 33.97  ? 110 ILE A CB  1 
ATOM   711  C  CG1 . ILE A 1 112 ? 159.006 127.900 109.387 1.00 37.42  ? 110 ILE A CG1 1 
ATOM   712  C  CG2 . ILE A 1 112 ? 161.050 128.798 108.252 1.00 41.54  ? 110 ILE A CG2 1 
ATOM   713  C  CD1 . ILE A 1 112 ? 158.375 129.178 109.870 1.00 41.72  ? 110 ILE A CD1 1 
ATOM   714  N  N   . VAL A 1 113 ? 163.447 126.598 109.861 1.00 34.47  ? 111 VAL A N   1 
ATOM   715  C  CA  . VAL A 1 113 ? 164.876 126.582 109.567 1.00 34.29  ? 111 VAL A CA  1 
ATOM   716  C  C   . VAL A 1 113 ? 165.284 125.234 108.989 1.00 35.41  ? 111 VAL A C   1 
ATOM   717  O  O   . VAL A 1 113 ? 166.040 125.162 108.014 1.00 42.36  ? 111 VAL A O   1 
ATOM   718  C  CB  . VAL A 1 113 ? 165.685 126.924 110.832 1.00 39.71  ? 111 VAL A CB  1 
ATOM   719  C  CG1 . VAL A 1 113 ? 167.172 126.730 110.581 1.00 37.03  ? 111 VAL A CG1 1 
ATOM   720  C  CG2 . VAL A 1 113 ? 165.401 128.348 111.275 1.00 42.18  ? 111 VAL A CG2 1 
ATOM   721  N  N   . LEU A 1 114 ? 164.797 124.144 109.585 1.00 40.14  ? 112 LEU A N   1 
ATOM   722  C  CA  . LEU A 1 114 ? 165.167 122.814 109.112 1.00 35.72  ? 112 LEU A CA  1 
ATOM   723  C  C   . LEU A 1 114 ? 164.604 122.539 107.724 1.00 40.02  ? 112 LEU A C   1 
ATOM   724  O  O   . LEU A 1 114 ? 165.311 122.016 106.855 1.00 43.09  ? 112 LEU A O   1 
ATOM   725  C  CB  . LEU A 1 114 ? 164.681 121.755 110.101 1.00 40.79  ? 112 LEU A CB  1 
ATOM   726  C  CG  . LEU A 1 114 ? 165.417 121.675 111.438 1.00 39.89  ? 112 LEU A CG  1 
ATOM   727  C  CD1 . LEU A 1 114 ? 164.739 120.668 112.346 1.00 41.41  ? 112 LEU A CD1 1 
ATOM   728  C  CD2 . LEU A 1 114 ? 166.877 121.310 111.236 1.00 39.19  ? 112 LEU A CD2 1 
ATOM   729  N  N   . VAL A 1 115 ? 163.333 122.872 107.495 1.00 40.35  ? 113 VAL A N   1 
ATOM   730  C  CA  . VAL A 1 115 ? 162.717 122.569 106.207 1.00 41.38  ? 113 VAL A CA  1 
ATOM   731  C  C   . VAL A 1 115 ? 163.324 123.432 105.108 1.00 41.64  ? 113 VAL A C   1 
ATOM   732  O  O   . VAL A 1 115 ? 163.514 122.973 103.975 1.00 44.82  ? 113 VAL A O   1 
ATOM   733  C  CB  . VAL A 1 115 ? 161.189 122.740 106.291 1.00 37.30  ? 113 VAL A CB  1 
ATOM   734  C  CG1 . VAL A 1 115 ? 160.817 124.202 106.418 1.00 37.68  ? 113 VAL A CG1 1 
ATOM   735  C  CG2 . VAL A 1 115 ? 160.521 122.117 105.079 1.00 34.97  ? 113 VAL A CG2 1 
ATOM   736  N  N   . VAL A 1 116 ? 163.628 124.693 105.415 1.00 36.05  ? 114 VAL A N   1 
ATOM   737  C  CA  . VAL A 1 116 ? 164.226 125.574 104.418 1.00 38.49  ? 114 VAL A CA  1 
ATOM   738  C  C   . VAL A 1 116 ? 165.661 125.157 104.122 1.00 42.42  ? 114 VAL A C   1 
ATOM   739  O  O   . VAL A 1 116 ? 166.116 125.229 102.976 1.00 45.68  ? 114 VAL A O   1 
ATOM   740  C  CB  . VAL A 1 116 ? 164.146 127.038 104.884 1.00 37.22  ? 114 VAL A CB  1 
ATOM   741  C  CG1 . VAL A 1 116 ? 165.077 127.908 104.059 1.00 39.60  ? 114 VAL A CG1 1 
ATOM   742  C  CG2 . VAL A 1 116 ? 162.718 127.543 104.788 1.00 40.44  ? 114 VAL A CG2 1 
ATOM   743  N  N   . SER A 1 117 ? 166.404 124.741 105.149 1.00 40.25  ? 115 SER A N   1 
ATOM   744  C  CA  . SER A 1 117 ? 167.796 124.352 104.944 1.00 37.92  ? 115 SER A CA  1 
ATOM   745  C  C   . SER A 1 117 ? 167.899 123.010 104.230 1.00 40.58  ? 115 SER A C   1 
ATOM   746  O  O   . SER A 1 117 ? 168.668 122.861 103.273 1.00 42.33  ? 115 SER A O   1 
ATOM   747  C  CB  . SER A 1 117 ? 168.528 124.301 106.285 1.00 40.35  ? 115 SER A CB  1 
ATOM   748  O  OG  . SER A 1 117 ? 168.209 125.423 107.087 1.00 43.67  ? 115 SER A OG  1 
ATOM   749  N  N   . ILE A 1 118 ? 167.138 122.014 104.688 1.00 44.79  ? 116 ILE A N   1 
ATOM   750  C  CA  . ILE A 1 118 ? 167.200 120.690 104.075 1.00 40.07  ? 116 ILE A CA  1 
ATOM   751  C  C   . ILE A 1 118 ? 166.548 120.705 102.698 1.00 45.94  ? 116 ILE A C   1 
ATOM   752  O  O   . ILE A 1 118 ? 167.027 120.053 101.763 1.00 49.29  ? 116 ILE A O   1 
ATOM   753  C  CB  . ILE A 1 118 ? 166.553 119.643 104.999 1.00 39.60  ? 116 ILE A CB  1 
ATOM   754  C  CG1 . ILE A 1 118 ? 167.353 119.521 106.299 1.00 42.05  ? 116 ILE A CG1 1 
ATOM   755  C  CG2 . ILE A 1 118 ? 166.470 118.297 104.296 1.00 41.11  ? 116 ILE A CG2 1 
ATOM   756  C  CD1 . ILE A 1 118 ? 166.649 118.739 107.386 1.00 42.12  ? 116 ILE A CD1 1 
ATOM   757  N  N   . LYS A 1 119 ? 165.447 121.437 102.552 1.00 40.31  ? 117 LYS A N   1 
ATOM   758  C  CA  . LYS A 1 119 ? 164.691 121.484 101.307 1.00 40.44  ? 117 LYS A CA  1 
ATOM   759  C  C   . LYS A 1 119 ? 164.237 120.084 100.918 1.00 41.32  ? 117 LYS A C   1 
ATOM   760  O  O   . LYS A 1 119 ? 164.711 119.535 99.916  1.00 43.61  ? 117 LYS A O   1 
ATOM   761  C  CB  . LYS A 1 119 ? 165.527 122.100 100.183 1.00 41.85  ? 117 LYS A CB  1 
ATOM   762  C  CG  . LYS A 1 119 ? 165.718 123.598 100.305 1.00 43.29  ? 117 LYS A CG  1 
ATOM   763  C  CD  . LYS A 1 119 ? 166.590 124.141 99.186  1.00 43.60  ? 117 LYS A CD  1 
ATOM   764  C  CE  . LYS A 1 119 ? 168.064 123.876 99.441  1.00 40.57  ? 117 LYS A CE  1 
ATOM   765  N  NZ  . LYS A 1 119 ? 168.549 124.541 100.680 1.00 44.26  ? 117 LYS A NZ  1 
ATOM   766  N  N   . PRO A 1 120 ? 163.329 119.472 101.680 1.00 41.15  ? 118 PRO A N   1 
ATOM   767  C  CA  . PRO A 1 120 ? 162.867 118.124 101.316 1.00 39.42  ? 118 PRO A CA  1 
ATOM   768  C  C   . PRO A 1 120 ? 162.223 118.054 99.943  1.00 40.96  ? 118 PRO A C   1 
ATOM   769  O  O   . PRO A 1 120 ? 162.355 117.030 99.261  1.00 45.43  ? 118 PRO A O   1 
ATOM   770  C  CB  . PRO A 1 120 ? 161.867 117.784 102.430 1.00 40.64  ? 118 PRO A CB  1 
ATOM   771  C  CG  . PRO A 1 120 ? 162.203 118.695 103.547 1.00 41.92  ? 118 PRO A CG  1 
ATOM   772  C  CD  . PRO A 1 120 ? 162.715 119.947 102.929 1.00 42.94  ? 118 PRO A CD  1 
ATOM   773  N  N   . GLY A 1 121 ? 161.530 119.104 99.516  1.00 43.88  ? 119 GLY A N   1 
ATOM   774  C  CA  . GLY A 1 121 ? 160.887 119.120 98.215  1.00 42.69  ? 119 GLY A CA  1 
ATOM   775  C  C   . GLY A 1 121 ? 161.618 119.984 97.206  1.00 44.99  ? 119 GLY A C   1 
ATOM   776  O  O   . GLY A 1 121 ? 162.244 119.478 96.275  1.00 44.05  ? 119 GLY A O   1 
ATOM   777  N  N   . SER A 1 139 ? 146.908 137.256 98.434  1.00 47.50  ? 137 SER A N   1 
ATOM   778  C  CA  . SER A 1 139 ? 145.662 136.954 99.127  1.00 49.84  ? 137 SER A CA  1 
ATOM   779  C  C   . SER A 1 139 ? 145.934 136.377 100.513 1.00 51.33  ? 137 SER A C   1 
ATOM   780  O  O   . SER A 1 139 ? 145.066 135.746 101.112 1.00 49.36  ? 137 SER A O   1 
ATOM   781  C  CB  . SER A 1 139 ? 144.818 135.977 98.307  1.00 49.21  ? 137 SER A CB  1 
ATOM   782  O  OG  . SER A 1 139 ? 145.446 134.710 98.215  1.00 50.61  ? 137 SER A OG  1 
ATOM   783  N  N   . THR A 1 140 ? 147.151 136.594 101.018 1.00 48.23  ? 138 THR A N   1 
ATOM   784  C  CA  . THR A 1 140 ? 147.491 136.129 102.356 1.00 47.00  ? 138 THR A CA  1 
ATOM   785  C  C   . THR A 1 140 ? 146.793 136.937 103.440 1.00 48.92  ? 138 THR A C   1 
ATOM   786  O  O   . THR A 1 140 ? 146.632 136.438 104.559 1.00 49.00  ? 138 THR A O   1 
ATOM   787  C  CB  . THR A 1 140 ? 149.005 136.190 102.571 1.00 45.61  ? 138 THR A CB  1 
ATOM   788  O  OG1 . THR A 1 140 ? 149.335 135.595 103.831 1.00 50.65  ? 138 THR A OG1 1 
ATOM   789  C  CG2 . THR A 1 140 ? 149.496 137.632 102.559 1.00 45.03  ? 138 THR A CG2 1 
ATOM   790  N  N   . VAL A 1 141 ? 146.380 138.169 103.136 1.00 47.48  ? 139 VAL A N   1 
ATOM   791  C  CA  . VAL A 1 141 ? 145.733 139.007 104.142 1.00 44.54  ? 139 VAL A CA  1 
ATOM   792  C  C   . VAL A 1 141 ? 144.410 138.392 104.577 1.00 42.29  ? 139 VAL A C   1 
ATOM   793  O  O   . VAL A 1 141 ? 144.066 138.402 105.765 1.00 43.71  ? 139 VAL A O   1 
ATOM   794  C  CB  . VAL A 1 141 ? 145.546 140.440 103.607 1.00 41.74  ? 139 VAL A CB  1 
ATOM   795  C  CG1 . VAL A 1 141 ? 144.722 140.444 102.326 1.00 44.77  ? 139 VAL A CG1 1 
ATOM   796  C  CG2 . VAL A 1 141 ? 144.901 141.322 104.663 1.00 42.17  ? 139 VAL A CG2 1 
ATOM   797  N  N   . ASP A 1 142 ? 143.648 137.845 103.629 1.00 41.14  ? 140 ASP A N   1 
ATOM   798  C  CA  . ASP A 1 142 ? 142.343 137.286 103.966 1.00 42.40  ? 140 ASP A CA  1 
ATOM   799  C  C   . ASP A 1 142 ? 142.474 136.126 104.944 1.00 44.51  ? 140 ASP A C   1 
ATOM   800  O  O   . ASP A 1 142 ? 141.673 135.998 105.876 1.00 46.49  ? 140 ASP A O   1 
ATOM   801  C  CB  . ASP A 1 142 ? 141.622 136.835 102.697 1.00 45.03  ? 140 ASP A CB  1 
ATOM   802  C  CG  . ASP A 1 142 ? 141.144 137.998 101.855 1.00 53.98  ? 140 ASP A CG  1 
ATOM   803  O  OD1 . ASP A 1 142 ? 140.410 138.856 102.389 1.00 49.35  ? 140 ASP A OD1 1 
ATOM   804  O  OD2 . ASP A 1 142 ? 141.503 138.057 100.660 1.00 55.62  ? 140 ASP A OD2 1 
ATOM   805  N  N   . ALA A 1 143 ? 143.470 135.263 104.742 1.00 45.94  ? 141 ALA A N   1 
ATOM   806  C  CA  . ALA A 1 143 ? 143.664 134.139 105.650 1.00 41.57  ? 141 ALA A CA  1 
ATOM   807  C  C   . ALA A 1 143 ? 144.074 134.611 107.039 1.00 43.55  ? 141 ALA A C   1 
ATOM   808  O  O   . ALA A 1 143 ? 143.608 134.068 108.047 1.00 40.36  ? 141 ALA A O   1 
ATOM   809  C  CB  . ALA A 1 143 ? 144.707 133.182 105.079 1.00 42.69  ? 141 ALA A CB  1 
ATOM   810  N  N   . MET A 1 144 ? 144.938 135.629 107.085 1.00 38.75  ? 142 MET A N   1 
ATOM   811  C  CA  . MET A 1 144 ? 145.387 136.187 108.387 1.00 37.13  ? 142 MET A CA  1 
ATOM   812  C  C   . MET A 1 144 ? 144.185 136.817 109.092 1.00 39.68  ? 142 MET A C   1 
ATOM   813  O  O   . MET A 1 144 ? 144.059 136.638 110.318 1.00 39.13  ? 142 MET A O   1 
ATOM   814  C  CB  . MET A 1 144 ? 146.463 137.257 108.183 1.00 43.73  ? 142 MET A CB  1 
ATOM   815  C  CG  . MET A 1 144 ? 147.720 136.735 107.515 1.00 46.35  ? 142 MET A CG  1 
ATOM   816  S  SD  . MET A 1 144 ? 148.262 135.150 108.200 1.00 59.98  ? 142 MET A SD  1 
ATOM   817  C  CE  . MET A 1 144 ? 147.547 134.021 107.006 1.00 46.38  ? 142 MET A CE  1 
ATOM   818  N  N   . LEU A 1 145 ? 143.340 137.526 108.338 1.00 46.04  ? 143 LEU A N   1 
ATOM   819  C  CA  . LEU A 1 145 ? 142.168 138.157 108.933 1.00 33.20  ? 143 LEU A CA  1 
ATOM   820  C  C   . LEU A 1 145 ? 141.132 137.124 109.353 1.00 30.54  ? 143 LEU A C   1 
ATOM   821  O  O   . LEU A 1 145 ? 140.331 137.386 110.255 1.00 41.63  ? 143 LEU A O   1 
ATOM   822  C  CB  . LEU A 1 145 ? 141.553 139.156 107.954 1.00 34.07  ? 143 LEU A CB  1 
ATOM   823  C  CG  . LEU A 1 145 ? 142.394 140.392 107.626 1.00 39.29  ? 143 LEU A CG  1 
ATOM   824  C  CD1 . LEU A 1 145 ? 141.665 141.266 106.624 1.00 37.00  ? 143 LEU A CD1 1 
ATOM   825  C  CD2 . LEU A 1 145 ? 142.731 141.183 108.878 1.00 35.64  ? 143 LEU A CD2 1 
ATOM   826  N  N   . ASP A 1 146 ? 141.131 135.951 108.715 1.00 29.20  ? 144 ASP A N   1 
ATOM   827  C  CA  . ASP A 1 146 ? 140.209 134.894 109.113 1.00 26.98  ? 144 ASP A CA  1 
ATOM   828  C  C   . ASP A 1 146 ? 140.596 134.284 110.452 1.00 28.69  ? 144 ASP A C   1 
ATOM   829  O  O   . ASP A 1 146 ? 139.741 133.725 111.145 1.00 36.90  ? 144 ASP A O   1 
ATOM   830  C  CB  . ASP A 1 146 ? 140.160 133.806 108.043 1.00 36.98  ? 144 ASP A CB  1 
ATOM   831  C  CG  . ASP A 1 146 ? 139.161 134.107 106.952 1.00 39.40  ? 144 ASP A CG  1 
ATOM   832  O  OD1 . ASP A 1 146 ? 138.476 135.145 107.037 1.00 35.64  ? 144 ASP A OD1 1 
ATOM   833  O  OD2 . ASP A 1 146 ? 139.057 133.304 106.004 1.00 39.27  ? 144 ASP A OD2 1 
ATOM   834  N  N   . LEU A 1 147 ? 141.874 134.356 110.822 1.00 34.87  ? 145 LEU A N   1 
ATOM   835  C  CA  . LEU A 1 147 ? 142.284 133.870 112.133 1.00 34.85  ? 145 LEU A CA  1 
ATOM   836  C  C   . LEU A 1 147 ? 141.727 134.753 113.240 1.00 31.50  ? 145 LEU A C   1 
ATOM   837  O  O   . LEU A 1 147 ? 141.321 134.256 114.295 1.00 31.54  ? 145 LEU A O   1 
ATOM   838  C  CB  . LEU A 1 147 ? 143.808 133.805 112.216 1.00 37.37  ? 145 LEU A CB  1 
ATOM   839  C  CG  . LEU A 1 147 ? 144.490 132.825 111.263 1.00 32.93  ? 145 LEU A CG  1 
ATOM   840  C  CD1 . LEU A 1 147 ? 145.992 133.035 111.284 1.00 39.34  ? 145 LEU A CD1 1 
ATOM   841  C  CD2 . LEU A 1 147 ? 144.143 131.394 111.622 1.00 35.41  ? 145 LEU A CD2 1 
ATOM   842  N  N   . ILE A 1 148 ? 141.708 136.068 113.017 1.00 33.31  ? 146 ILE A N   1 
ATOM   843  C  CA  . ILE A 1 148 ? 141.140 136.983 114.001 1.00 27.94  ? 146 ILE A CA  1 
ATOM   844  C  C   . ILE A 1 148 ? 139.627 136.828 114.059 1.00 29.62  ? 146 ILE A C   1 
ATOM   845  O  O   . ILE A 1 148 ? 139.024 136.899 115.136 1.00 33.27  ? 146 ILE A O   1 
ATOM   846  C  CB  . ILE A 1 148 ? 141.548 138.431 113.681 1.00 28.96  ? 146 ILE A CB  1 
ATOM   847  C  CG1 . ILE A 1 148 ? 143.072 138.557 113.606 1.00 33.67  ? 146 ILE A CG1 1 
ATOM   848  C  CG2 . ILE A 1 148 ? 140.995 139.380 114.732 1.00 29.60  ? 146 ILE A CG2 1 
ATOM   849  C  CD1 . ILE A 1 148 ? 143.545 139.795 112.886 1.00 36.45  ? 146 ILE A CD1 1 
ATOM   850  N  N   . ARG A 1 149 ? 138.987 136.628 112.905 1.00 30.56  ? 147 ARG A N   1 
ATOM   851  C  CA  . ARG A 1 149 ? 137.538 136.461 112.884 1.00 21.07  ? 147 ARG A CA  1 
ATOM   852  C  C   . ARG A 1 149 ? 137.118 135.199 113.623 1.00 25.69  ? 147 ARG A C   1 
ATOM   853  O  O   . ARG A 1 149 ? 136.096 135.190 114.319 1.00 42.63  ? 147 ARG A O   1 
ATOM   854  C  CB  . ARG A 1 149 ? 137.033 136.422 111.444 1.00 23.74  ? 147 ARG A CB  1 
ATOM   855  C  CG  . ARG A 1 149 ? 136.974 137.777 110.779 1.00 27.01  ? 147 ARG A CG  1 
ATOM   856  C  CD  . ARG A 1 149 ? 136.525 137.661 109.340 1.00 31.00  ? 147 ARG A CD  1 
ATOM   857  N  NE  . ARG A 1 149 ? 136.768 138.891 108.595 1.00 32.07  ? 147 ARG A NE  1 
ATOM   858  C  CZ  . ARG A 1 149 ? 137.557 138.999 107.534 1.00 36.23  ? 147 ARG A CZ  1 
ATOM   859  N  NH1 . ARG A 1 149 ? 138.216 137.961 107.045 1.00 41.66  ? 147 ARG A NH1 1 
ATOM   860  N  NH2 . ARG A 1 149 ? 137.689 140.183 106.945 1.00 34.68  ? 147 ARG A NH2 1 
ATOM   861  N  N   . ASN A 1 150 ? 137.885 134.120 113.475 1.00 25.12  ? 148 ASN A N   1 
ATOM   862  C  CA  . ASN A 1 150 ? 137.542 132.869 114.138 1.00 21.35  ? 148 ASN A CA  1 
ATOM   863  C  C   . ASN A 1 150 ? 137.827 132.910 115.632 1.00 20.10  ? 148 ASN A C   1 
ATOM   864  O  O   . ASN A 1 150 ? 137.258 132.110 116.379 1.00 31.00  ? 148 ASN A O   1 
ATOM   865  C  CB  . ASN A 1 150 ? 138.301 131.717 113.488 1.00 28.73  ? 148 ASN A CB  1 
ATOM   866  C  CG  . ASN A 1 150 ? 137.665 131.267 112.194 1.00 24.73  ? 148 ASN A CG  1 
ATOM   867  O  OD1 . ASN A 1 150 ? 136.661 130.562 112.199 1.00 30.92  ? 148 ASN A OD1 1 
ATOM   868  N  ND2 . ASN A 1 150 ? 138.239 131.685 111.077 1.00 23.40  ? 148 ASN A ND2 1 
ATOM   869  N  N   . MET A 1 151 ? 138.695 133.816 116.082 1.00 21.85  ? 149 MET A N   1 
ATOM   870  C  CA  . MET A 1 151 ? 138.876 134.028 117.511 1.00 19.14  ? 149 MET A CA  1 
ATOM   871  C  C   . MET A 1 151 ? 137.640 134.635 118.154 1.00 23.80  ? 149 MET A C   1 
ATOM   872  O  O   . MET A 1 151 ? 137.440 134.475 119.361 1.00 32.83  ? 149 MET A O   1 
ATOM   873  C  CB  . MET A 1 151 ? 140.076 134.941 117.760 1.00 25.01  ? 149 MET A CB  1 
ATOM   874  C  CG  . MET A 1 151 ? 141.377 134.211 118.010 1.00 29.90  ? 149 MET A CG  1 
ATOM   875  S  SD  . MET A 1 151 ? 142.643 135.297 118.687 1.00 52.91  ? 149 MET A SD  1 
ATOM   876  C  CE  . MET A 1 151 ? 143.123 136.210 117.225 1.00 36.84  ? 149 MET A CE  1 
ATOM   877  N  N   . PHE A 1 152 ? 136.814 135.329 117.376 1.00 30.95  ? 150 PHE A N   1 
ATOM   878  C  CA  . PHE A 1 152 ? 135.600 135.979 117.864 1.00 24.04  ? 150 PHE A CA  1 
ATOM   879  C  C   . PHE A 1 152 ? 134.451 135.537 116.971 1.00 24.25  ? 150 PHE A C   1 
ATOM   880  O  O   . PHE A 1 152 ? 134.006 136.288 116.094 1.00 32.42  ? 150 PHE A O   1 
ATOM   881  C  CB  . PHE A 1 152 ? 135.752 137.500 117.869 1.00 21.01  ? 150 PHE A CB  1 
ATOM   882  C  CG  . PHE A 1 152 ? 137.008 137.972 118.534 1.00 25.02  ? 150 PHE A CG  1 
ATOM   883  C  CD1 . PHE A 1 152 ? 137.117 137.975 119.914 1.00 25.96  ? 150 PHE A CD1 1 
ATOM   884  C  CD2 . PHE A 1 152 ? 138.087 138.398 117.781 1.00 26.15  ? 150 PHE A CD2 1 
ATOM   885  C  CE1 . PHE A 1 152 ? 138.273 138.401 120.526 1.00 29.95  ? 150 PHE A CE1 1 
ATOM   886  C  CE2 . PHE A 1 152 ? 139.245 138.823 118.391 1.00 25.98  ? 150 PHE A CE2 1 
ATOM   887  C  CZ  . PHE A 1 152 ? 139.339 138.825 119.764 1.00 22.38  ? 150 PHE A CZ  1 
ATOM   888  N  N   . PRO A 1 153 ? 133.955 134.314 117.155 1.00 23.93  ? 151 PRO A N   1 
ATOM   889  C  CA  . PRO A 1 153 ? 132.843 133.844 116.324 1.00 23.58  ? 151 PRO A CA  1 
ATOM   890  C  C   . PRO A 1 153 ? 131.581 134.658 116.561 1.00 22.49  ? 151 PRO A C   1 
ATOM   891  O  O   . PRO A 1 153 ? 131.349 135.187 117.649 1.00 30.30  ? 151 PRO A O   1 
ATOM   892  C  CB  . PRO A 1 153 ? 132.662 132.387 116.766 1.00 26.21  ? 151 PRO A CB  1 
ATOM   893  C  CG  . PRO A 1 153 ? 133.280 132.310 118.108 1.00 14.95  ? 151 PRO A CG  1 
ATOM   894  C  CD  . PRO A 1 153 ? 134.402 133.287 118.109 1.00 24.04  ? 151 PRO A CD  1 
ATOM   895  N  N   . GLU A 1 154 ? 130.760 134.759 115.515 1.00 15.57  ? 152 GLU A N   1 
ATOM   896  C  CA  . GLU A 1 154 ? 129.495 135.472 115.635 1.00 16.65  ? 152 GLU A CA  1 
ATOM   897  C  C   . GLU A 1 154 ? 128.468 134.693 116.445 1.00 19.59  ? 152 GLU A C   1 
ATOM   898  O  O   . GLU A 1 154 ? 127.542 135.300 116.991 1.00 28.36  ? 152 GLU A O   1 
ATOM   899  C  CB  . GLU A 1 154 ? 128.933 135.778 114.249 1.00 15.34  ? 152 GLU A CB  1 
ATOM   900  C  CG  . GLU A 1 154 ? 129.525 137.014 113.604 1.00 19.40  ? 152 GLU A CG  1 
ATOM   901  C  CD  . GLU A 1 154 ? 129.482 136.965 112.089 1.00 35.67  ? 152 GLU A CD  1 
ATOM   902  O  OE1 . GLU A 1 154 ? 129.525 135.854 111.522 1.00 37.04  ? 152 GLU A OE1 1 
ATOM   903  O  OE2 . GLU A 1 154 ? 129.404 138.041 111.462 1.00 39.02  ? 152 GLU A OE2 1 
ATOM   904  N  N   . ASN A 1 155 ? 128.606 133.373 116.534 1.00 21.57  ? 153 ASN A N   1 
ATOM   905  C  CA  . ASN A 1 155 ? 127.668 132.536 117.268 1.00 16.30  ? 153 ASN A CA  1 
ATOM   906  C  C   . ASN A 1 155 ? 128.445 131.452 117.995 1.00 12.77  ? 153 ASN A C   1 
ATOM   907  O  O   . ASN A 1 155 ? 129.346 130.840 117.416 1.00 20.59  ? 153 ASN A O   1 
ATOM   908  C  CB  . ASN A 1 155 ? 126.632 131.915 116.325 1.00 21.85  ? 153 ASN A CB  1 
ATOM   909  C  CG  . ASN A 1 155 ? 125.400 131.433 117.050 1.00 14.67  ? 153 ASN A CG  1 
ATOM   910  O  OD1 . ASN A 1 155 ? 125.371 130.324 117.574 1.00 23.30  ? 153 ASN A OD1 1 
ATOM   911  N  ND2 . ASN A 1 155 ? 124.374 132.267 117.089 1.00 21.64  ? 153 ASN A ND2 1 
ATOM   912  N  N   . LEU A 1 156 ? 128.104 131.226 119.265 1.00 18.22  ? 154 LEU A N   1 
ATOM   913  C  CA  . LEU A 1 156 ? 128.804 130.221 120.058 1.00 18.46  ? 154 LEU A CA  1 
ATOM   914  C  C   . LEU A 1 156 ? 128.389 128.807 119.676 1.00 15.51  ? 154 LEU A C   1 
ATOM   915  O  O   . LEU A 1 156 ? 129.230 127.904 119.625 1.00 23.79  ? 154 LEU A O   1 
ATOM   916  C  CB  . LEU A 1 156 ? 128.553 130.457 121.546 1.00 24.58  ? 154 LEU A CB  1 
ATOM   917  C  CG  . LEU A 1 156 ? 129.405 131.544 122.200 1.00 26.89  ? 154 LEU A CG  1 
ATOM   918  C  CD1 . LEU A 1 156 ? 128.916 131.818 123.610 1.00 22.00  ? 154 LEU A CD1 1 
ATOM   919  C  CD2 . LEU A 1 156 ? 130.871 131.153 122.202 1.00 27.06  ? 154 LEU A CD2 1 
ATOM   920  N  N   . VAL A 1 157 ? 127.098 128.589 119.427 1.00 17.67  ? 155 VAL A N   1 
ATOM   921  C  CA  . VAL A 1 157 ? 126.640 127.270 119.008 1.00 18.84  ? 155 VAL A CA  1 
ATOM   922  C  C   . VAL A 1 157 ? 127.218 126.918 117.644 1.00 17.90  ? 155 VAL A C   1 
ATOM   923  O  O   . VAL A 1 157 ? 127.663 125.788 117.416 1.00 28.13  ? 155 VAL A O   1 
ATOM   924  C  CB  . VAL A 1 157 ? 125.102 127.219 119.008 1.00 13.85  ? 155 VAL A CB  1 
ATOM   925  C  CG1 . VAL A 1 157 ? 124.610 125.862 118.548 1.00 18.31  ? 155 VAL A CG1 1 
ATOM   926  C  CG2 . VAL A 1 157 ? 124.570 127.535 120.390 1.00 17.61  ? 155 VAL A CG2 1 
ATOM   927  N  N   . GLN A 1 158 ? 127.225 127.876 116.718 1.00 9.74   ? 156 GLN A N   1 
ATOM   928  C  CA  . GLN A 1 158 ? 127.803 127.630 115.403 1.00 7.38   ? 156 GLN A CA  1 
ATOM   929  C  C   . GLN A 1 158 ? 129.299 127.364 115.500 1.00 18.72  ? 156 GLN A C   1 
ATOM   930  O  O   . GLN A 1 158 ? 129.838 126.534 114.761 1.00 27.21  ? 156 GLN A O   1 
ATOM   931  C  CB  . GLN A 1 158 ? 127.531 128.817 114.486 1.00 17.49  ? 156 GLN A CB  1 
ATOM   932  C  CG  . GLN A 1 158 ? 127.888 128.575 113.044 1.00 13.57  ? 156 GLN A CG  1 
ATOM   933  C  CD  . GLN A 1 158 ? 127.155 129.502 112.113 1.00 22.83  ? 156 GLN A CD  1 
ATOM   934  O  OE1 . GLN A 1 158 ? 126.993 130.684 112.401 1.00 32.00  ? 156 GLN A OE1 1 
ATOM   935  N  NE2 . GLN A 1 158 ? 126.711 128.975 110.983 1.00 25.81  ? 156 GLN A NE2 1 
ATOM   936  N  N   . ALA A 1 159 ? 129.989 128.064 116.401 1.00 21.08  ? 157 ALA A N   1 
ATOM   937  C  CA  . ALA A 1 159 ? 131.418 127.843 116.581 1.00 12.58  ? 157 ALA A CA  1 
ATOM   938  C  C   . ALA A 1 159 ? 131.724 126.429 117.050 1.00 16.80  ? 157 ALA A C   1 
ATOM   939  O  O   . ALA A 1 159 ? 132.864 125.974 116.910 1.00 22.62  ? 157 ALA A O   1 
ATOM   940  C  CB  . ALA A 1 159 ? 131.985 128.848 117.582 1.00 15.19  ? 157 ALA A CB  1 
ATOM   941  N  N   . ALA A 1 160 ? 130.737 125.725 117.604 1.00 28.08  ? 158 ALA A N   1 
ATOM   942  C  CA  . ALA A 1 160 ? 130.961 124.365 118.069 1.00 17.78  ? 158 ALA A CA  1 
ATOM   943  C  C   . ALA A 1 160 ? 131.191 123.389 116.925 1.00 19.35  ? 158 ALA A C   1 
ATOM   944  O  O   . ALA A 1 160 ? 131.801 122.339 117.144 1.00 35.84  ? 158 ALA A O   1 
ATOM   945  C  CB  . ALA A 1 160 ? 129.778 123.898 118.915 1.00 13.16  ? 158 ALA A CB  1 
ATOM   946  N  N   . PHE A 1 161 ? 130.707 123.694 115.719 1.00 17.42  ? 159 PHE A N   1 
ATOM   947  C  CA  . PHE A 1 161 ? 130.880 122.777 114.601 1.00 20.04  ? 159 PHE A CA  1 
ATOM   948  C  C   . PHE A 1 161 ? 131.149 123.466 113.267 1.00 21.87  ? 159 PHE A C   1 
ATOM   949  O  O   . PHE A 1 161 ? 131.175 122.782 112.238 1.00 29.25  ? 159 PHE A O   1 
ATOM   950  C  CB  . PHE A 1 161 ? 129.645 121.874 114.468 1.00 23.84  ? 159 PHE A CB  1 
ATOM   951  C  CG  . PHE A 1 161 ? 128.424 122.589 113.980 1.00 21.95  ? 159 PHE A CG  1 
ATOM   952  C  CD1 . PHE A 1 161 ? 127.724 123.436 114.817 1.00 15.44  ? 159 PHE A CD1 1 
ATOM   953  C  CD2 . PHE A 1 161 ? 127.976 122.415 112.685 1.00 21.55  ? 159 PHE A CD2 1 
ATOM   954  C  CE1 . PHE A 1 161 ? 126.606 124.097 114.371 1.00 18.06  ? 159 PHE A CE1 1 
ATOM   955  C  CE2 . PHE A 1 161 ? 126.859 123.074 112.235 1.00 21.65  ? 159 PHE A CE2 1 
ATOM   956  C  CZ  . PHE A 1 161 ? 126.174 123.918 113.079 1.00 21.87  ? 159 PHE A CZ  1 
ATOM   957  N  N   . GLN A 1 162 ? 131.345 124.782 113.233 1.00 19.49  ? 160 GLN A N   1 
ATOM   958  C  CA  . GLN A 1 162 ? 131.531 125.484 111.970 1.00 20.47  ? 160 GLN A CA  1 
ATOM   959  C  C   . GLN A 1 162 ? 132.585 126.571 112.122 1.00 22.76  ? 160 GLN A C   1 
ATOM   960  O  O   . GLN A 1 162 ? 132.825 127.088 113.214 1.00 29.57  ? 160 GLN A O   1 
ATOM   961  C  CB  . GLN A 1 162 ? 130.214 126.086 111.466 1.00 21.91  ? 160 GLN A CB  1 
ATOM   962  C  CG  . GLN A 1 162 ? 129.449 125.156 110.549 1.00 26.22  ? 160 GLN A CG  1 
ATOM   963  C  CD  . GLN A 1 162 ? 128.286 125.826 109.864 1.00 29.39  ? 160 GLN A CD  1 
ATOM   964  O  OE1 . GLN A 1 162 ? 127.766 126.832 110.338 1.00 38.31  ? 160 GLN A OE1 1 
ATOM   965  N  NE2 . GLN A 1 162 ? 127.875 125.275 108.732 1.00 31.39  ? 160 GLN A NE2 1 
ATOM   966  N  N   . GLN A 1 163 ? 133.206 126.915 110.996 1.00 21.81  ? 161 GLN A N   1 
ATOM   967  C  CA  . GLN A 1 163 ? 134.283 127.891 110.945 1.00 23.76  ? 161 GLN A CA  1 
ATOM   968  C  C   . GLN A 1 163 ? 133.992 128.918 109.860 1.00 26.48  ? 161 GLN A C   1 
ATOM   969  O  O   . GLN A 1 163 ? 133.253 128.657 108.910 1.00 37.34  ? 161 GLN A O   1 
ATOM   970  C  CB  . GLN A 1 163 ? 135.632 127.221 110.667 1.00 27.53  ? 161 GLN A CB  1 
ATOM   971  C  CG  . GLN A 1 163 ? 136.501 127.052 111.890 1.00 28.42  ? 161 GLN A CG  1 
ATOM   972  C  CD  . GLN A 1 163 ? 137.711 126.193 111.617 1.00 34.59  ? 161 GLN A CD  1 
ATOM   973  O  OE1 . GLN A 1 163 ? 137.756 125.463 110.629 1.00 38.97  ? 161 GLN A OE1 1 
ATOM   974  N  NE2 . GLN A 1 163 ? 138.703 126.274 112.492 1.00 36.69  ? 161 GLN A NE2 1 
ATOM   975  N  N   . TYR A 1 164 ? 134.602 130.089 110.005 1.00 31.25  ? 162 TYR A N   1 
ATOM   976  C  CA  . TYR A 1 164 ? 134.381 131.210 109.104 1.00 26.96  ? 162 TYR A CA  1 
ATOM   977  C  C   . TYR A 1 164 ? 135.526 131.313 108.105 1.00 38.79  ? 162 TYR A C   1 
ATOM   978  O  O   . TYR A 1 164 ? 136.698 131.235 108.485 1.00 41.39  ? 162 TYR A O   1 
ATOM   979  C  CB  . TYR A 1 164 ? 134.256 132.513 109.892 1.00 28.58  ? 162 TYR A CB  1 
ATOM   980  C  CG  . TYR A 1 164 ? 133.650 133.647 109.107 1.00 30.76  ? 162 TYR A CG  1 
ATOM   981  C  CD1 . TYR A 1 164 ? 132.308 133.643 108.771 1.00 35.36  ? 162 TYR A CD1 1 
ATOM   982  C  CD2 . TYR A 1 164 ? 134.422 134.724 108.705 1.00 32.19  ? 162 TYR A CD2 1 
ATOM   983  C  CE1 . TYR A 1 164 ? 131.751 134.678 108.057 1.00 36.96  ? 162 TYR A CE1 1 
ATOM   984  C  CE2 . TYR A 1 164 ? 133.875 135.762 107.992 1.00 30.88  ? 162 TYR A CE2 1 
ATOM   985  C  CZ  . TYR A 1 164 ? 132.540 135.735 107.669 1.00 37.14  ? 162 TYR A CZ  1 
ATOM   986  O  OH  . TYR A 1 164 ? 131.991 136.774 106.958 1.00 40.59  ? 162 TYR A OH  1 
ATOM   987  N  N   . LYS A 1 165 ? 135.180 131.489 106.832 1.00 37.04  ? 163 LYS A N   1 
ATOM   988  C  CA  . LYS A 1 165 ? 136.161 131.655 105.769 1.00 35.25  ? 163 LYS A CA  1 
ATOM   989  C  C   . LYS A 1 165 ? 135.705 132.774 104.849 1.00 34.57  ? 163 LYS A C   1 
ATOM   990  O  O   . LYS A 1 165 ? 134.533 132.825 104.469 1.00 42.21  ? 163 LYS A O   1 
ATOM   991  C  CB  . LYS A 1 165 ? 136.341 130.356 104.976 1.00 37.52  ? 163 LYS A CB  1 
ATOM   992  C  CG  . LYS A 1 165 ? 137.350 130.456 103.847 1.00 38.25  ? 163 LYS A CG  1 
ATOM   993  C  CD  . LYS A 1 165 ? 138.374 129.337 103.917 1.00 40.14  ? 163 LYS A CD  1 
ATOM   994  C  CE  . LYS A 1 165 ? 139.377 129.423 102.778 1.00 41.37  ? 163 LYS A CE  1 
ATOM   995  N  NZ  . LYS A 1 165 ? 138.718 129.477 101.445 1.00 44.80  ? 163 LYS A NZ  1 
ATOM   996  N  N   . THR A 1 166 ? 136.626 133.664 104.493 1.00 34.07  ? 164 THR A N   1 
ATOM   997  C  CA  . THR A 1 166 ? 136.346 134.760 103.577 1.00 39.03  ? 164 THR A CA  1 
ATOM   998  C  C   . THR A 1 166 ? 137.148 134.584 102.296 1.00 42.48  ? 164 THR A C   1 
ATOM   999  O  O   . THR A 1 166 ? 138.307 134.161 102.329 1.00 46.99  ? 164 THR A O   1 
ATOM   1000 C  CB  . THR A 1 166 ? 136.679 136.119 104.201 1.00 40.92  ? 164 THR A CB  1 
ATOM   1001 O  OG1 . THR A 1 166 ? 138.048 136.139 104.620 1.00 46.27  ? 164 THR A OG1 1 
ATOM   1002 C  CG2 . THR A 1 166 ? 135.781 136.398 105.393 1.00 42.49  ? 164 THR A CG2 1 
ATOM   1003 N  N   . LYS A 1 167 ? 136.520 134.906 101.170 1.00 43.62  ? 165 LYS A N   1 
ATOM   1004 C  CA  . LYS A 1 167 ? 137.177 134.911 99.874  1.00 46.07  ? 165 LYS A CA  1 
ATOM   1005 C  C   . LYS A 1 167 ? 136.798 136.183 99.135  1.00 46.18  ? 165 LYS A C   1 
ATOM   1006 O  O   . LYS A 1 167 ? 135.690 136.700 99.291  1.00 51.10  ? 165 LYS A O   1 
ATOM   1007 C  CB  . LYS A 1 167 ? 136.789 133.685 99.037  1.00 47.40  ? 165 LYS A CB  1 
ATOM   1008 C  CG  . LYS A 1 167 ? 135.295 133.536 98.813  1.00 48.62  ? 165 LYS A CG  1 
ATOM   1009 C  CD  . LYS A 1 167 ? 134.981 133.215 97.363  1.00 51.30  ? 165 LYS A CD  1 
ATOM   1010 C  CE  . LYS A 1 167 ? 133.569 132.679 97.208  1.00 49.39  ? 165 LYS A CE  1 
ATOM   1011 N  NZ  . LYS A 1 167 ? 133.259 132.329 95.796  1.00 53.38  ? 165 LYS A NZ  1 
ATOM   1012 N  N   . ARG A 1 168 ? 137.726 136.685 98.328  1.00 51.36  ? 166 ARG A N   1 
ATOM   1013 C  CA  . ARG A 1 168 ? 137.489 137.891 97.546  1.00 51.90  ? 166 ARG A CA  1 
ATOM   1014 C  C   . ARG A 1 168 ? 136.975 137.494 96.169  1.00 50.24  ? 166 ARG A C   1 
ATOM   1015 O  O   . ARG A 1 168 ? 137.634 136.737 95.449  1.00 52.31  ? 166 ARG A O   1 
ATOM   1016 C  CB  . ARG A 1 168 ? 138.758 138.733 97.430  1.00 48.46  ? 166 ARG A CB  1 
ATOM   1017 C  CG  . ARG A 1 168 ? 139.980 137.980 96.963  1.00 49.98  ? 166 ARG A CG  1 
ATOM   1018 C  CD  . ARG A 1 168 ? 141.152 138.921 96.767  1.00 53.23  ? 166 ARG A CD  1 
ATOM   1019 N  NE  . ARG A 1 168 ? 141.523 139.604 98.000  1.00 46.41  ? 166 ARG A NE  1 
ATOM   1020 C  CZ  . ARG A 1 168 ? 142.518 140.473 98.103  1.00 50.64  ? 166 ARG A CZ  1 
ATOM   1021 N  NH1 . ARG A 1 168 ? 143.263 140.797 97.060  1.00 52.71  ? 166 ARG A NH1 1 
ATOM   1022 N  NH2 . ARG A 1 168 ? 142.772 141.032 99.282  1.00 53.98  ? 166 ARG A NH2 1 
ATOM   1023 N  N   . GLU A 1 169 ? 135.797 137.996 95.813  1.00 54.52  ? 167 GLU A N   1 
ATOM   1024 C  CA  . GLU A 1 169 ? 135.192 137.716 94.521  1.00 55.64  ? 167 GLU A CA  1 
ATOM   1025 C  C   . GLU A 1 169 ? 134.594 138.999 93.968  1.00 53.90  ? 167 GLU A C   1 
ATOM   1026 O  O   . GLU A 1 169 ? 134.268 139.927 94.711  1.00 56.78  ? 167 GLU A O   1 
ATOM   1027 C  CB  . GLU A 1 169 ? 134.120 136.622 94.625  1.00 52.97  ? 167 GLU A CB  1 
ATOM   1028 C  CG  . GLU A 1 169 ? 132.779 137.100 95.160  1.00 54.34  ? 167 GLU A CG  1 
ATOM   1029 C  CD  . GLU A 1 169 ? 131.818 137.516 94.063  1.00 58.58  ? 167 GLU A CD  1 
ATOM   1030 O  OE1 . GLU A 1 169 ? 131.817 136.876 92.990  1.00 58.10  ? 167 GLU A OE1 1 
ATOM   1031 O  OE2 . GLU A 1 169 ? 131.061 138.487 94.273  1.00 59.21  ? 167 GLU A OE2 1 
ATOM   1032 N  N   . GLU A 1 170 ? 134.462 139.042 92.647  1.00 56.40  ? 168 GLU A N   1 
ATOM   1033 C  CA  . GLU A 1 170 ? 133.857 140.184 91.973  1.00 54.95  ? 168 GLU A CA  1 
ATOM   1034 C  C   . GLU A 1 170 ? 132.876 139.717 90.905  1.00 56.80  ? 168 GLU A C   1 
ATOM   1035 O  O   . GLU A 1 170 ? 131.797 140.287 90.750  1.00 60.52  ? 168 GLU A O   1 
ATOM   1036 C  CB  . GLU A 1 170 ? 134.933 141.073 91.349  1.00 54.02  ? 168 GLU A CB  1 
ATOM   1037 C  CG  . GLU A 1 170 ? 134.384 142.226 90.523  1.00 58.13  ? 168 GLU A CG  1 
ATOM   1038 C  CD  . GLU A 1 170 ? 133.251 142.958 91.216  1.00 61.92  ? 168 GLU A CD  1 
ATOM   1039 O  OE1 . GLU A 1 170 ? 133.482 143.520 92.306  1.00 61.03  ? 168 GLU A OE1 1 
ATOM   1040 O  OE2 . GLU A 1 170 ? 132.129 142.970 90.669  1.00 59.57  ? 168 GLU A OE2 1 
ATOM   1041 N  N   . TYR A 1 202 ? 136.984 143.761 93.546  1.00 53.91  ? 200 TYR A N   1 
ATOM   1042 C  CA  . TYR A 1 202 ? 136.894 142.624 94.454  1.00 60.56  ? 200 TYR A CA  1 
ATOM   1043 C  C   . TYR A 1 202 ? 136.182 143.014 95.744  1.00 57.60  ? 200 TYR A C   1 
ATOM   1044 O  O   . TYR A 1 202 ? 136.434 144.080 96.302  1.00 57.92  ? 200 TYR A O   1 
ATOM   1045 C  CB  . TYR A 1 202 ? 138.289 142.080 94.774  1.00 58.45  ? 200 TYR A CB  1 
ATOM   1046 C  CG  . TYR A 1 202 ? 138.987 141.442 93.596  1.00 57.45  ? 200 TYR A CG  1 
ATOM   1047 C  CD1 . TYR A 1 202 ? 138.409 140.383 92.911  1.00 57.98  ? 200 TYR A CD1 1 
ATOM   1048 C  CD2 . TYR A 1 202 ? 140.225 141.900 93.169  1.00 54.51  ? 200 TYR A CD2 1 
ATOM   1049 C  CE1 . TYR A 1 202 ? 139.043 139.799 91.833  1.00 56.71  ? 200 TYR A CE1 1 
ATOM   1050 C  CE2 . TYR A 1 202 ? 140.867 141.323 92.093  1.00 57.84  ? 200 TYR A CE2 1 
ATOM   1051 C  CZ  . TYR A 1 202 ? 140.272 140.272 91.429  1.00 61.21  ? 200 TYR A CZ  1 
ATOM   1052 O  OH  . TYR A 1 202 ? 140.909 139.693 90.355  1.00 59.54  ? 200 TYR A OH  1 
ATOM   1053 N  N   . LYS A 1 203 ? 135.288 142.146 96.210  1.00 50.29  ? 201 LYS A N   1 
ATOM   1054 C  CA  . LYS A 1 203 ? 134.617 142.321 97.488  1.00 51.74  ? 201 LYS A CA  1 
ATOM   1055 C  C   . LYS A 1 203 ? 134.755 141.044 98.301  1.00 52.77  ? 201 LYS A C   1 
ATOM   1056 O  O   . LYS A 1 203 ? 134.693 139.940 97.755  1.00 57.46  ? 201 LYS A O   1 
ATOM   1057 C  CB  . LYS A 1 203 ? 133.133 142.685 97.304  1.00 51.96  ? 201 LYS A CB  1 
ATOM   1058 C  CG  . LYS A 1 203 ? 132.254 141.585 96.720  1.00 50.75  ? 201 LYS A CG  1 
ATOM   1059 C  CD  . LYS A 1 203 ? 130.828 141.709 97.226  1.00 52.96  ? 201 LYS A CD  1 
ATOM   1060 C  CE  . LYS A 1 203 ? 129.842 141.014 96.304  1.00 56.55  ? 201 LYS A CE  1 
ATOM   1061 N  NZ  . LYS A 1 203 ? 130.021 139.537 96.301  1.00 52.76  ? 201 LYS A NZ  1 
ATOM   1062 N  N   . ILE A 1 204 ? 134.944 141.200 99.605  1.00 49.54  ? 202 ILE A N   1 
ATOM   1063 C  CA  . ILE A 1 204 ? 135.135 140.057 100.489 1.00 47.56  ? 202 ILE A CA  1 
ATOM   1064 C  C   . ILE A 1 204 ? 133.788 139.404 100.757 1.00 47.21  ? 202 ILE A C   1 
ATOM   1065 O  O   . ILE A 1 204 ? 132.820 140.076 101.133 1.00 46.94  ? 202 ILE A O   1 
ATOM   1066 C  CB  . ILE A 1 204 ? 135.813 140.491 101.797 1.00 49.05  ? 202 ILE A CB  1 
ATOM   1067 C  CG1 . ILE A 1 204 ? 137.109 141.252 101.506 1.00 50.49  ? 202 ILE A CG1 1 
ATOM   1068 C  CG2 . ILE A 1 204 ? 136.093 139.286 102.670 1.00 49.50  ? 202 ILE A CG2 1 
ATOM   1069 C  CD1 . ILE A 1 204 ? 138.100 140.492 100.656 1.00 46.11  ? 202 ILE A CD1 1 
ATOM   1070 N  N   . VAL A 1 205 ? 133.722 138.090 100.560 1.00 45.25  ? 203 VAL A N   1 
ATOM   1071 C  CA  . VAL A 1 205 ? 132.525 137.301 100.821 1.00 43.96  ? 203 VAL A CA  1 
ATOM   1072 C  C   . VAL A 1 205 ? 132.877 136.246 101.858 1.00 46.89  ? 203 VAL A C   1 
ATOM   1073 O  O   . VAL A 1 205 ? 133.834 135.487 101.676 1.00 53.81  ? 203 VAL A O   1 
ATOM   1074 C  CB  . VAL A 1 205 ? 131.984 136.643 99.540  1.00 49.18  ? 203 VAL A CB  1 
ATOM   1075 C  CG1 . VAL A 1 205 ? 130.566 136.145 99.761  1.00 45.46  ? 203 VAL A CG1 1 
ATOM   1076 C  CG2 . VAL A 1 205 ? 132.038 137.619 98.379  1.00 50.42  ? 203 VAL A CG2 1 
ATOM   1077 N  N   . GLY A 1 206 ? 132.105 136.197 102.935 1.00 39.83  ? 204 GLY A N   1 
ATOM   1078 C  CA  . GLY A 1 206 ? 132.348 135.278 104.035 1.00 35.02  ? 204 GLY A CA  1 
ATOM   1079 C  C   . GLY A 1 206 ? 131.305 134.175 104.061 1.00 38.44  ? 204 GLY A C   1 
ATOM   1080 O  O   . GLY A 1 206 ? 130.128 134.415 103.784 1.00 43.95  ? 204 GLY A O   1 
ATOM   1081 N  N   . MET A 1 207 ? 131.751 132.968 104.397 1.00 33.85  ? 205 MET A N   1 
ATOM   1082 C  CA  . MET A 1 207 ? 130.878 131.810 104.485 1.00 34.19  ? 205 MET A CA  1 
ATOM   1083 C  C   . MET A 1 207 ? 131.298 130.971 105.681 1.00 38.04  ? 205 MET A C   1 
ATOM   1084 O  O   . MET A 1 207 ? 132.467 130.967 106.074 1.00 37.85  ? 205 MET A O   1 
ATOM   1085 C  CB  . MET A 1 207 ? 130.934 130.972 103.200 1.00 37.54  ? 205 MET A CB  1 
ATOM   1086 C  CG  . MET A 1 207 ? 129.817 129.952 103.064 1.00 37.56  ? 205 MET A CG  1 
ATOM   1087 S  SD  . MET A 1 207 ? 130.323 128.496 102.132 1.00 53.48  ? 205 MET A SD  1 
ATOM   1088 C  CE  . MET A 1 207 ? 129.584 127.192 103.114 1.00 40.88  ? 205 MET A CE  1 
ATOM   1089 N  N   . TYR A 1 208 ? 130.333 130.264 106.262 1.00 32.12  ? 206 TYR A N   1 
ATOM   1090 C  CA  . TYR A 1 208 ? 130.576 129.383 107.398 1.00 21.49  ? 206 TYR A CA  1 
ATOM   1091 C  C   . TYR A 1 208 ? 130.624 127.947 106.893 1.00 31.96  ? 206 TYR A C   1 
ATOM   1092 O  O   . TYR A 1 208 ? 129.607 127.402 106.454 1.00 41.57  ? 206 TYR A O   1 
ATOM   1093 C  CB  . TYR A 1 208 ? 129.496 129.553 108.463 1.00 27.41  ? 206 TYR A CB  1 
ATOM   1094 C  CG  . TYR A 1 208 ? 129.822 130.608 109.490 1.00 32.89  ? 206 TYR A CG  1 
ATOM   1095 C  CD1 . TYR A 1 208 ? 130.733 130.358 110.505 1.00 22.26  ? 206 TYR A CD1 1 
ATOM   1096 C  CD2 . TYR A 1 208 ? 129.220 131.857 109.443 1.00 31.36  ? 206 TYR A CD2 1 
ATOM   1097 C  CE1 . TYR A 1 208 ? 131.034 131.319 111.441 1.00 23.93  ? 206 TYR A CE1 1 
ATOM   1098 C  CE2 . TYR A 1 208 ? 129.515 132.823 110.376 1.00 27.77  ? 206 TYR A CE2 1 
ATOM   1099 C  CZ  . TYR A 1 208 ? 130.422 132.551 111.372 1.00 30.88  ? 206 TYR A CZ  1 
ATOM   1100 O  OH  . TYR A 1 208 ? 130.717 133.517 112.303 1.00 37.25  ? 206 TYR A OH  1 
ATOM   1101 N  N   . SER A 1 209 ? 131.801 127.340 106.956 1.00 35.02  ? 207 SER A N   1 
ATOM   1102 C  CA  . SER A 1 209 ? 132.001 125.962 106.542 1.00 24.17  ? 207 SER A CA  1 
ATOM   1103 C  C   . SER A 1 209 ? 132.143 125.063 107.763 1.00 24.83  ? 207 SER A C   1 
ATOM   1104 O  O   . SER A 1 209 ? 132.404 125.522 108.876 1.00 30.14  ? 207 SER A O   1 
ATOM   1105 C  CB  . SER A 1 209 ? 133.239 125.842 105.649 1.00 33.65  ? 207 SER A CB  1 
ATOM   1106 O  OG  . SER A 1 209 ? 134.337 126.551 106.198 1.00 35.42  ? 207 SER A OG  1 
ATOM   1107 N  N   . ASP A 1 210 ? 131.971 123.765 107.539 1.00 32.82  ? 208 ASP A N   1 
ATOM   1108 C  CA  . ASP A 1 210 ? 132.000 122.813 108.638 1.00 32.06  ? 208 ASP A CA  1 
ATOM   1109 C  C   . ASP A 1 210 ? 133.406 122.702 109.220 1.00 31.44  ? 208 ASP A C   1 
ATOM   1110 O  O   . ASP A 1 210 ? 134.405 123.061 108.591 1.00 32.99  ? 208 ASP A O   1 
ATOM   1111 C  CB  . ASP A 1 210 ? 131.514 121.439 108.175 1.00 31.76  ? 208 ASP A CB  1 
ATOM   1112 C  CG  . ASP A 1 210 ? 130.125 121.098 108.696 1.00 37.13  ? 208 ASP A CG  1 
ATOM   1113 O  OD1 . ASP A 1 210 ? 129.489 121.959 109.338 1.00 34.69  ? 208 ASP A OD1 1 
ATOM   1114 O  OD2 . ASP A 1 210 ? 129.667 119.959 108.463 1.00 35.30  ? 208 ASP A OD2 1 
ATOM   1115 N  N   . GLY A 1 211 ? 133.468 122.191 110.446 1.00 31.53  ? 209 GLY A N   1 
ATOM   1116 C  CA  . GLY A 1 211 ? 134.711 122.101 111.182 1.00 26.87  ? 209 GLY A CA  1 
ATOM   1117 C  C   . GLY A 1 211 ? 134.659 122.911 112.457 1.00 26.23  ? 209 GLY A C   1 
ATOM   1118 O  O   . GLY A 1 211 ? 134.582 124.140 112.410 1.00 33.92  ? 209 GLY A O   1 
ATOM   1119 N  N   . ILE A 1 212 ? 134.702 122.232 113.605 1.00 25.73  ? 210 ILE A N   1 
ATOM   1120 C  CA  . ILE A 1 212 ? 134.587 122.919 114.885 1.00 18.02  ? 210 ILE A CA  1 
ATOM   1121 C  C   . ILE A 1 212 ? 135.610 124.038 114.952 1.00 25.19  ? 210 ILE A C   1 
ATOM   1122 O  O   . ILE A 1 212 ? 136.778 123.856 114.596 1.00 34.98  ? 210 ILE A O   1 
ATOM   1123 C  CB  . ILE A 1 212 ? 134.760 121.927 116.049 1.00 13.03  ? 210 ILE A CB  1 
ATOM   1124 C  CG1 . ILE A 1 212 ? 134.799 122.674 117.382 1.00 25.26  ? 210 ILE A CG1 1 
ATOM   1125 C  CG2 . ILE A 1 212 ? 136.030 121.111 115.883 1.00 29.31  ? 210 ILE A CG2 1 
ATOM   1126 C  CD1 . ILE A 1 212 ? 134.493 121.804 118.579 1.00 25.44  ? 210 ILE A CD1 1 
ATOM   1127 N  N   . ASN A 1 213 ? 135.167 125.211 115.403 1.00 27.82  ? 211 ASN A N   1 
ATOM   1128 C  CA  . ASN A 1 213 ? 136.047 126.366 115.561 1.00 20.42  ? 211 ASN A CA  1 
ATOM   1129 C  C   . ASN A 1 213 ? 136.647 126.313 116.961 1.00 23.26  ? 211 ASN A C   1 
ATOM   1130 O  O   . ASN A 1 213 ? 136.183 126.958 117.902 1.00 24.23  ? 211 ASN A O   1 
ATOM   1131 C  CB  . ASN A 1 213 ? 135.282 127.658 115.313 1.00 20.43  ? 211 ASN A CB  1 
ATOM   1132 C  CG  . ASN A 1 213 ? 136.125 128.887 115.547 1.00 21.03  ? 211 ASN A CG  1 
ATOM   1133 O  OD1 . ASN A 1 213 ? 137.347 128.844 115.435 1.00 27.96  ? 211 ASN A OD1 1 
ATOM   1134 N  ND2 . ASN A 1 213 ? 135.475 129.995 115.868 1.00 27.73  ? 211 ASN A ND2 1 
ATOM   1135 N  N   . VAL A 1 214 ? 137.707 125.515 117.091 1.00 25.65  ? 212 VAL A N   1 
ATOM   1136 C  CA  . VAL A 1 214 ? 138.352 125.336 118.387 1.00 23.95  ? 212 VAL A CA  1 
ATOM   1137 C  C   . VAL A 1 214 ? 138.968 126.641 118.867 1.00 25.28  ? 212 VAL A C   1 
ATOM   1138 O  O   . VAL A 1 214 ? 138.988 126.921 120.070 1.00 30.58  ? 212 VAL A O   1 
ATOM   1139 C  CB  . VAL A 1 214 ? 139.400 124.209 118.300 1.00 23.26  ? 212 VAL A CB  1 
ATOM   1140 C  CG1 . VAL A 1 214 ? 140.165 124.089 119.602 1.00 27.19  ? 212 VAL A CG1 1 
ATOM   1141 C  CG2 . VAL A 1 214 ? 138.728 122.894 117.955 1.00 26.03  ? 212 VAL A CG2 1 
ATOM   1142 N  N   . LEU A 1 215 ? 139.483 127.455 117.945 1.00 35.09  ? 213 LEU A N   1 
ATOM   1143 C  CA  . LEU A 1 215 ? 140.090 128.723 118.332 1.00 25.60  ? 213 LEU A CA  1 
ATOM   1144 C  C   . LEU A 1 215 ? 139.074 129.649 118.988 1.00 26.91  ? 213 LEU A C   1 
ATOM   1145 O  O   . LEU A 1 215 ? 139.364 130.273 120.015 1.00 28.22  ? 213 LEU A O   1 
ATOM   1146 C  CB  . LEU A 1 215 ? 140.708 129.390 117.105 1.00 26.33  ? 213 LEU A CB  1 
ATOM   1147 C  CG  . LEU A 1 215 ? 141.739 130.487 117.358 1.00 35.17  ? 213 LEU A CG  1 
ATOM   1148 C  CD1 . LEU A 1 215 ? 142.979 129.923 118.030 1.00 35.09  ? 213 LEU A CD1 1 
ATOM   1149 C  CD2 . LEU A 1 215 ? 142.097 131.168 116.050 1.00 35.17  ? 213 LEU A CD2 1 
ATOM   1150 N  N   . GLY A 1 216 ? 137.879 129.757 118.409 1.00 28.47  ? 214 GLY A N   1 
ATOM   1151 C  CA  . GLY A 1 216 ? 136.863 130.620 118.988 1.00 17.31  ? 214 GLY A CA  1 
ATOM   1152 C  C   . GLY A 1 216 ? 136.359 130.119 120.327 1.00 21.98  ? 214 GLY A C   1 
ATOM   1153 O  O   . GLY A 1 216 ? 136.084 130.911 121.232 1.00 27.44  ? 214 GLY A O   1 
ATOM   1154 N  N   . LEU A 1 217 ? 136.217 128.801 120.469 1.00 25.21  ? 215 LEU A N   1 
ATOM   1155 C  CA  . LEU A 1 217 ? 135.770 128.235 121.738 1.00 21.82  ? 215 LEU A CA  1 
ATOM   1156 C  C   . LEU A 1 217 ? 136.810 128.435 122.832 1.00 22.67  ? 215 LEU A C   1 
ATOM   1157 O  O   . LEU A 1 217 ? 136.459 128.702 123.986 1.00 26.30  ? 215 LEU A O   1 
ATOM   1158 C  CB  . LEU A 1 217 ? 135.459 126.751 121.567 1.00 26.83  ? 215 LEU A CB  1 
ATOM   1159 C  CG  . LEU A 1 217 ? 134.305 126.411 120.627 1.00 24.30  ? 215 LEU A CG  1 
ATOM   1160 C  CD1 . LEU A 1 217 ? 134.253 124.917 120.409 1.00 26.97  ? 215 LEU A CD1 1 
ATOM   1161 C  CD2 . LEU A 1 217 ? 132.988 126.925 121.179 1.00 19.52  ? 215 LEU A CD2 1 
ATOM   1162 N  N   . ILE A 1 218 ? 138.092 128.296 122.494 1.00 32.11  ? 216 ILE A N   1 
ATOM   1163 C  CA  . ILE A 1 218 ? 139.150 128.486 123.482 1.00 25.05  ? 216 ILE A CA  1 
ATOM   1164 C  C   . ILE A 1 218 ? 139.126 129.909 124.019 1.00 22.75  ? 216 ILE A C   1 
ATOM   1165 O  O   . ILE A 1 218 ? 139.253 130.134 125.227 1.00 26.90  ? 216 ILE A O   1 
ATOM   1166 C  CB  . ILE A 1 218 ? 140.519 128.139 122.869 1.00 28.90  ? 216 ILE A CB  1 
ATOM   1167 C  CG1 . ILE A 1 218 ? 140.720 126.626 122.835 1.00 30.33  ? 216 ILE A CG1 1 
ATOM   1168 C  CG2 . ILE A 1 218 ? 141.645 128.800 123.648 1.00 29.66  ? 216 ILE A CG2 1 
ATOM   1169 C  CD1 . ILE A 1 218 ? 141.698 126.180 121.780 1.00 34.54  ? 216 ILE A CD1 1 
ATOM   1170 N  N   . VAL A 1 219 ? 138.975 130.893 123.131 1.00 26.33  ? 217 VAL A N   1 
ATOM   1171 C  CA  . VAL A 1 219 ? 138.980 132.286 123.565 1.00 27.10  ? 217 VAL A CA  1 
ATOM   1172 C  C   . VAL A 1 219 ? 137.800 132.562 124.486 1.00 26.21  ? 217 VAL A C   1 
ATOM   1173 O  O   . VAL A 1 219 ? 137.947 133.210 125.528 1.00 28.68  ? 217 VAL A O   1 
ATOM   1174 C  CB  . VAL A 1 219 ? 138.980 133.226 122.346 1.00 28.33  ? 217 VAL A CB  1 
ATOM   1175 C  CG1 . VAL A 1 219 ? 138.834 134.671 122.788 1.00 22.39  ? 217 VAL A CG1 1 
ATOM   1176 C  CG2 . VAL A 1 219 ? 140.251 133.040 121.538 1.00 21.30  ? 217 VAL A CG2 1 
ATOM   1177 N  N   . PHE A 1 220 ? 136.611 132.082 124.120 1.00 26.59  ? 218 PHE A N   1 
ATOM   1178 C  CA  . PHE A 1 220 ? 135.447 132.302 124.971 1.00 26.50  ? 218 PHE A CA  1 
ATOM   1179 C  C   . PHE A 1 220 ? 135.556 131.518 126.271 1.00 26.32  ? 218 PHE A C   1 
ATOM   1180 O  O   . PHE A 1 220 ? 135.239 132.040 127.345 1.00 23.30  ? 218 PHE A O   1 
ATOM   1181 C  CB  . PHE A 1 220 ? 134.166 131.922 124.233 1.00 23.69  ? 218 PHE A CB  1 
ATOM   1182 C  CG  . PHE A 1 220 ? 132.932 132.053 125.075 1.00 27.73  ? 218 PHE A CG  1 
ATOM   1183 C  CD1 . PHE A 1 220 ? 132.320 133.281 125.242 1.00 27.35  ? 218 PHE A CD1 1 
ATOM   1184 C  CD2 . PHE A 1 220 ? 132.395 130.952 125.714 1.00 27.82  ? 218 PHE A CD2 1 
ATOM   1185 C  CE1 . PHE A 1 220 ? 131.194 133.406 126.022 1.00 27.60  ? 218 PHE A CE1 1 
ATOM   1186 C  CE2 . PHE A 1 220 ? 131.270 131.072 126.494 1.00 29.90  ? 218 PHE A CE2 1 
ATOM   1187 C  CZ  . PHE A 1 220 ? 130.668 132.300 126.648 1.00 30.86  ? 218 PHE A CZ  1 
ATOM   1188 N  N   . ALA A 1 221 ? 135.997 130.262 126.197 1.00 22.22  ? 219 ALA A N   1 
ATOM   1189 C  CA  . ALA A 1 221 ? 136.089 129.444 127.400 1.00 23.35  ? 219 ALA A CA  1 
ATOM   1190 C  C   . ALA A 1 221 ? 137.097 130.025 128.383 1.00 28.28  ? 219 ALA A C   1 
ATOM   1191 O  O   . ALA A 1 221 ? 136.872 130.005 129.598 1.00 28.12  ? 219 ALA A O   1 
ATOM   1192 C  CB  . ALA A 1 221 ? 136.457 128.010 127.027 1.00 21.73  ? 219 ALA A CB  1 
ATOM   1193 N  N   . LEU A 1 222 ? 138.221 130.537 127.880 1.00 30.92  ? 220 LEU A N   1 
ATOM   1194 C  CA  . LEU A 1 222 ? 139.185 131.193 128.756 1.00 27.03  ? 220 LEU A CA  1 
ATOM   1195 C  C   . LEU A 1 222 ? 138.629 132.501 129.307 1.00 26.83  ? 220 LEU A C   1 
ATOM   1196 O  O   . LEU A 1 222 ? 138.768 132.785 130.502 1.00 33.95  ? 220 LEU A O   1 
ATOM   1197 C  CB  . LEU A 1 222 ? 140.494 131.435 128.005 1.00 29.79  ? 220 LEU A CB  1 
ATOM   1198 C  CG  . LEU A 1 222 ? 141.264 130.181 127.581 1.00 33.42  ? 220 LEU A CG  1 
ATOM   1199 C  CD1 . LEU A 1 222 ? 142.415 130.544 126.658 1.00 31.75  ? 220 LEU A CD1 1 
ATOM   1200 C  CD2 . LEU A 1 222 ? 141.776 129.414 128.789 1.00 32.12  ? 220 LEU A CD2 1 
ATOM   1201 N  N   . VAL A 1 223 ? 138.001 133.312 128.456 1.00 25.99  ? 221 VAL A N   1 
ATOM   1202 C  CA  . VAL A 1 223 ? 137.401 134.556 128.928 1.00 25.79  ? 221 VAL A CA  1 
ATOM   1203 C  C   . VAL A 1 223 ? 136.251 134.264 129.881 1.00 24.64  ? 221 VAL A C   1 
ATOM   1204 O  O   . VAL A 1 223 ? 136.089 134.937 130.904 1.00 28.75  ? 221 VAL A O   1 
ATOM   1205 C  CB  . VAL A 1 223 ? 136.945 135.416 127.736 1.00 34.97  ? 221 VAL A CB  1 
ATOM   1206 C  CG1 . VAL A 1 223 ? 136.081 136.571 128.213 1.00 25.00  ? 221 VAL A CG1 1 
ATOM   1207 C  CG2 . VAL A 1 223 ? 138.146 135.934 126.968 1.00 33.24  ? 221 VAL A CG2 1 
ATOM   1208 N  N   . PHE A 1 224 ? 135.426 133.266 129.557 1.00 27.86  ? 222 PHE A N   1 
ATOM   1209 C  CA  . PHE A 1 224 ? 134.348 132.877 130.460 1.00 19.14  ? 222 PHE A CA  1 
ATOM   1210 C  C   . PHE A 1 224 ? 134.897 132.365 131.784 1.00 22.49  ? 222 PHE A C   1 
ATOM   1211 O  O   . PHE A 1 224 ? 134.379 132.705 132.853 1.00 30.59  ? 222 PHE A O   1 
ATOM   1212 C  CB  . PHE A 1 224 ? 133.471 131.816 129.799 1.00 23.33  ? 222 PHE A CB  1 
ATOM   1213 C  CG  . PHE A 1 224 ? 132.204 131.529 130.547 1.00 24.09  ? 222 PHE A CG  1 
ATOM   1214 C  CD1 . PHE A 1 224 ? 131.136 132.402 130.487 1.00 25.46  ? 222 PHE A CD1 1 
ATOM   1215 C  CD2 . PHE A 1 224 ? 132.083 130.385 131.316 1.00 30.80  ? 222 PHE A CD2 1 
ATOM   1216 C  CE1 . PHE A 1 224 ? 129.973 132.140 131.176 1.00 22.97  ? 222 PHE A CE1 1 
ATOM   1217 C  CE2 . PHE A 1 224 ? 130.921 130.119 132.007 1.00 26.21  ? 222 PHE A CE2 1 
ATOM   1218 C  CZ  . PHE A 1 224 ? 129.866 130.997 131.936 1.00 25.95  ? 222 PHE A CZ  1 
ATOM   1219 N  N   . GLY A 1 225 ? 135.946 131.543 131.736 1.00 24.16  ? 223 GLY A N   1 
ATOM   1220 C  CA  . GLY A 1 225 ? 136.542 131.053 132.966 1.00 20.61  ? 223 GLY A CA  1 
ATOM   1221 C  C   . GLY A 1 225 ? 137.113 132.168 133.819 1.00 27.04  ? 223 GLY A C   1 
ATOM   1222 O  O   . GLY A 1 225 ? 137.056 132.113 135.049 1.00 28.69  ? 223 GLY A O   1 
ATOM   1223 N  N   . LEU A 1 226 ? 137.682 133.191 133.178 1.00 24.77  ? 224 LEU A N   1 
ATOM   1224 C  CA  . LEU A 1 226 ? 138.192 134.336 133.923 1.00 24.53  ? 224 LEU A CA  1 
ATOM   1225 C  C   . LEU A 1 226 ? 137.070 135.064 134.648 1.00 27.07  ? 224 LEU A C   1 
ATOM   1226 O  O   . LEU A 1 226 ? 137.225 135.463 135.806 1.00 34.12  ? 224 LEU A O   1 
ATOM   1227 C  CB  . LEU A 1 226 ? 138.916 135.296 132.979 1.00 31.03  ? 224 LEU A CB  1 
ATOM   1228 C  CG  . LEU A 1 226 ? 140.343 134.927 132.577 1.00 30.53  ? 224 LEU A CG  1 
ATOM   1229 C  CD1 . LEU A 1 226 ? 140.822 135.818 131.445 1.00 27.03  ? 224 LEU A CD1 1 
ATOM   1230 C  CD2 . LEU A 1 226 ? 141.282 135.015 133.767 1.00 27.84  ? 224 LEU A CD2 1 
ATOM   1231 N  N   . VAL A 1 227 ? 135.932 135.249 133.979 1.00 30.37  ? 225 VAL A N   1 
ATOM   1232 C  CA  . VAL A 1 227 ? 134.844 136.026 134.562 1.00 23.52  ? 225 VAL A CA  1 
ATOM   1233 C  C   . VAL A 1 227 ? 134.233 135.293 135.751 1.00 26.27  ? 225 VAL A C   1 
ATOM   1234 O  O   . VAL A 1 227 ? 134.065 135.869 136.831 1.00 35.89  ? 225 VAL A O   1 
ATOM   1235 C  CB  . VAL A 1 227 ? 133.787 136.342 133.490 1.00 21.56  ? 225 VAL A CB  1 
ATOM   1236 C  CG1 . VAL A 1 227 ? 132.551 136.950 134.124 1.00 26.50  ? 225 VAL A CG1 1 
ATOM   1237 C  CG2 . VAL A 1 227 ? 134.365 137.274 132.444 1.00 24.32  ? 225 VAL A CG2 1 
ATOM   1238 N  N   . ILE A 1 228 ? 133.899 134.012 135.580 1.00 18.75  ? 226 ILE A N   1 
ATOM   1239 C  CA  . ILE A 1 228 ? 133.218 133.297 136.657 1.00 21.31  ? 226 ILE A CA  1 
ATOM   1240 C  C   . ILE A 1 228 ? 134.151 133.088 137.840 1.00 25.48  ? 226 ILE A C   1 
ATOM   1241 O  O   . ILE A 1 228 ? 133.703 133.054 138.992 1.00 32.74  ? 226 ILE A O   1 
ATOM   1242 C  CB  . ILE A 1 228 ? 132.633 131.965 136.149 1.00 23.99  ? 226 ILE A CB  1 
ATOM   1243 C  CG1 . ILE A 1 228 ? 133.738 130.992 135.735 1.00 30.41  ? 226 ILE A CG1 1 
ATOM   1244 C  CG2 . ILE A 1 228 ? 131.687 132.217 134.993 1.00 28.58  ? 226 ILE A CG2 1 
ATOM   1245 C  CD1 . ILE A 1 228 ? 133.228 129.617 135.373 1.00 19.39  ? 226 ILE A CD1 1 
ATOM   1246 N  N   . GLY A 1 229 ? 135.451 132.935 137.587 1.00 26.78  ? 227 GLY A N   1 
ATOM   1247 C  CA  . GLY A 1 229 ? 136.395 132.819 138.684 1.00 26.11  ? 227 GLY A CA  1 
ATOM   1248 C  C   . GLY A 1 229 ? 136.477 134.084 139.516 1.00 29.56  ? 227 GLY A C   1 
ATOM   1249 O  O   . GLY A 1 229 ? 136.662 134.026 140.734 1.00 31.37  ? 227 GLY A O   1 
ATOM   1250 N  N   . LYS A 1 230 ? 136.344 135.242 138.874 1.00 32.80  ? 228 LYS A N   1 
ATOM   1251 C  CA  . LYS A 1 230 ? 136.418 136.524 139.558 1.00 25.79  ? 228 LYS A CA  1 
ATOM   1252 C  C   . LYS A 1 230 ? 135.087 136.966 140.149 1.00 33.27  ? 228 LYS A C   1 
ATOM   1253 O  O   . LYS A 1 230 ? 135.047 137.989 140.840 1.00 36.37  ? 228 LYS A O   1 
ATOM   1254 C  CB  . LYS A 1 230 ? 136.922 137.604 138.597 1.00 31.01  ? 228 LYS A CB  1 
ATOM   1255 C  CG  . LYS A 1 230 ? 138.432 137.661 138.465 1.00 34.40  ? 228 LYS A CG  1 
ATOM   1256 C  CD  . LYS A 1 230 ? 138.858 138.698 137.433 1.00 35.51  ? 228 LYS A CD  1 
ATOM   1257 C  CE  . LYS A 1 230 ? 139.422 138.061 136.169 1.00 40.14  ? 228 LYS A CE  1 
ATOM   1258 N  NZ  . LYS A 1 230 ? 138.925 138.735 134.937 1.00 40.93  ? 228 LYS A NZ  1 
ATOM   1259 N  N   . MET A 1 231 ? 134.006 136.233 139.898 1.00 35.68  ? 229 MET A N   1 
ATOM   1260 C  CA  . MET A 1 231 ? 132.692 136.576 140.424 1.00 28.46  ? 229 MET A CA  1 
ATOM   1261 C  C   . MET A 1 231 ? 132.450 136.029 141.824 1.00 25.63  ? 229 MET A C   1 
ATOM   1262 O  O   . MET A 1 231 ? 131.383 136.277 142.392 1.00 30.59  ? 229 MET A O   1 
ATOM   1263 C  CB  . MET A 1 231 ? 131.601 136.073 139.475 1.00 27.93  ? 229 MET A CB  1 
ATOM   1264 C  CG  . MET A 1 231 ? 131.436 136.939 138.237 1.00 30.76  ? 229 MET A CG  1 
ATOM   1265 S  SD  . MET A 1 231 ? 130.349 136.289 136.951 1.00 37.33  ? 229 MET A SD  1 
ATOM   1266 C  CE  . MET A 1 231 ? 129.519 134.946 137.783 1.00 26.70  ? 229 MET A CE  1 
ATOM   1267 N  N   . GLY A 1 232 ? 133.405 135.300 142.390 1.00 31.44  ? 230 GLY A N   1 
ATOM   1268 C  CA  . GLY A 1 232 ? 133.283 134.879 143.778 1.00 32.44  ? 230 GLY A CA  1 
ATOM   1269 C  C   . GLY A 1 232 ? 132.120 133.930 143.986 1.00 32.56  ? 230 GLY A C   1 
ATOM   1270 O  O   . GLY A 1 232 ? 131.942 132.956 143.247 1.00 36.26  ? 230 GLY A O   1 
ATOM   1271 N  N   . GLU A 1 233 ? 131.320 134.207 145.018 1.00 34.65  ? 231 GLU A N   1 
ATOM   1272 C  CA  . GLU A 1 233 ? 130.216 133.317 145.359 1.00 28.35  ? 231 GLU A CA  1 
ATOM   1273 C  C   . GLU A 1 233 ? 129.095 133.385 144.332 1.00 30.14  ? 231 GLU A C   1 
ATOM   1274 O  O   . GLU A 1 233 ? 128.359 132.408 144.158 1.00 42.77  ? 231 GLU A O   1 
ATOM   1275 C  CB  . GLU A 1 233 ? 129.674 133.665 146.749 1.00 27.51  ? 231 GLU A CB  1 
ATOM   1276 C  CG  . GLU A 1 233 ? 129.165 132.488 147.591 1.00 33.44  ? 231 GLU A CG  1 
ATOM   1277 C  CD  . GLU A 1 233 ? 129.948 131.202 147.389 1.00 40.12  ? 231 GLU A CD  1 
ATOM   1278 O  OE1 . GLU A 1 233 ? 131.163 131.191 147.681 1.00 38.98  ? 231 GLU A OE1 1 
ATOM   1279 O  OE2 . GLU A 1 233 ? 129.348 130.204 146.936 1.00 37.79  ? 231 GLU A OE2 1 
ATOM   1280 N  N   . LYS A 1 234 ? 128.945 134.519 143.648 1.00 31.35  ? 232 LYS A N   1 
ATOM   1281 C  CA  . LYS A 1 234 ? 127.895 134.637 142.644 1.00 28.36  ? 232 LYS A CA  1 
ATOM   1282 C  C   . LYS A 1 234 ? 128.099 133.649 141.505 1.00 29.96  ? 232 LYS A C   1 
ATOM   1283 O  O   . LYS A 1 234 ? 127.124 133.135 140.949 1.00 43.23  ? 232 LYS A O   1 
ATOM   1284 C  CB  . LYS A 1 234 ? 127.846 136.066 142.103 1.00 30.03  ? 232 LYS A CB  1 
ATOM   1285 C  CG  . LYS A 1 234 ? 126.724 136.924 142.675 1.00 36.32  ? 232 LYS A CG  1 
ATOM   1286 C  CD  . LYS A 1 234 ? 126.724 136.943 144.201 1.00 38.06  ? 232 LYS A CD  1 
ATOM   1287 C  CE  . LYS A 1 234 ? 127.894 137.742 144.755 1.00 38.76  ? 232 LYS A CE  1 
ATOM   1288 N  NZ  . LYS A 1 234 ? 127.889 137.771 146.244 1.00 37.27  ? 232 LYS A NZ  1 
ATOM   1289 N  N   . GLY A 1 235 ? 129.348 133.375 141.144 1.00 29.34  ? 233 GLY A N   1 
ATOM   1290 C  CA  . GLY A 1 235 ? 129.673 132.466 140.069 1.00 28.16  ? 233 GLY A CA  1 
ATOM   1291 C  C   . GLY A 1 235 ? 130.132 131.092 140.499 1.00 26.67  ? 233 GLY A C   1 
ATOM   1292 O  O   . GLY A 1 235 ? 130.655 130.347 139.664 1.00 31.03  ? 233 GLY A O   1 
ATOM   1293 N  N   . GLN A 1 236 ? 129.956 130.728 141.770 1.00 28.18  ? 234 GLN A N   1 
ATOM   1294 C  CA  . GLN A 1 236 ? 130.423 129.427 142.237 1.00 23.14  ? 234 GLN A CA  1 
ATOM   1295 C  C   . GLN A 1 236 ? 129.646 128.285 141.598 1.00 25.64  ? 234 GLN A C   1 
ATOM   1296 O  O   . GLN A 1 236 ? 130.217 127.220 141.340 1.00 32.92  ? 234 GLN A O   1 
ATOM   1297 C  CB  . GLN A 1 236 ? 130.320 129.352 143.759 1.00 25.64  ? 234 GLN A CB  1 
ATOM   1298 C  CG  . GLN A 1 236 ? 131.023 128.156 144.375 1.00 23.54  ? 234 GLN A CG  1 
ATOM   1299 C  CD  . GLN A 1 236 ? 132.505 128.120 144.059 1.00 37.03  ? 234 GLN A CD  1 
ATOM   1300 O  OE1 . GLN A 1 236 ? 133.220 129.097 144.273 1.00 37.54  ? 234 GLN A OE1 1 
ATOM   1301 N  NE2 . GLN A 1 236 ? 132.974 126.987 143.550 1.00 29.53  ? 234 GLN A NE2 1 
ATOM   1302 N  N   . ILE A 1 237 ? 128.352 128.479 141.337 1.00 26.39  ? 235 ILE A N   1 
ATOM   1303 C  CA  . ILE A 1 237 ? 127.554 127.420 140.729 1.00 23.96  ? 235 ILE A CA  1 
ATOM   1304 C  C   . ILE A 1 237 ? 128.071 127.089 139.338 1.00 20.84  ? 235 ILE A C   1 
ATOM   1305 O  O   . ILE A 1 237 ? 128.021 125.931 138.908 1.00 25.14  ? 235 ILE A O   1 
ATOM   1306 C  CB  . ILE A 1 237 ? 126.066 127.820 140.696 1.00 30.20  ? 235 ILE A CB  1 
ATOM   1307 C  CG1 . ILE A 1 237 ? 125.220 126.655 140.187 1.00 19.67  ? 235 ILE A CG1 1 
ATOM   1308 C  CG2 . ILE A 1 237 ? 125.855 129.043 139.820 1.00 22.72  ? 235 ILE A CG2 1 
ATOM   1309 C  CD1 . ILE A 1 237 ? 123.796 126.689 140.660 1.00 21.33  ? 235 ILE A CD1 1 
ATOM   1310 N  N   . LEU A 1 238 ? 128.554 128.093 138.603 1.00 27.38  ? 236 LEU A N   1 
ATOM   1311 C  CA  . LEU A 1 238 ? 129.151 127.829 137.299 1.00 20.95  ? 236 LEU A CA  1 
ATOM   1312 C  C   . LEU A 1 238 ? 130.488 127.117 137.443 1.00 20.13  ? 236 LEU A C   1 
ATOM   1313 O  O   . LEU A 1 238 ? 130.811 126.226 136.651 1.00 31.17  ? 236 LEU A O   1 
ATOM   1314 C  CB  . LEU A 1 238 ? 129.323 129.133 136.524 1.00 24.45  ? 236 LEU A CB  1 
ATOM   1315 C  CG  . LEU A 1 238 ? 128.048 129.877 136.131 1.00 23.21  ? 236 LEU A CG  1 
ATOM   1316 C  CD1 . LEU A 1 238 ? 128.406 131.136 135.374 1.00 28.79  ? 236 LEU A CD1 1 
ATOM   1317 C  CD2 . LEU A 1 238 ? 127.132 128.998 135.301 1.00 21.34  ? 236 LEU A CD2 1 
ATOM   1318 N  N   . VAL A 1 239 ? 131.282 127.499 138.442 1.00 24.87  ? 237 VAL A N   1 
ATOM   1319 C  CA  . VAL A 1 239 ? 132.535 126.798 138.696 1.00 18.33  ? 237 VAL A CA  1 
ATOM   1320 C  C   . VAL A 1 239 ? 132.258 125.353 139.085 1.00 23.22  ? 237 VAL A C   1 
ATOM   1321 O  O   . VAL A 1 239 ? 132.921 124.428 138.605 1.00 38.37  ? 237 VAL A O   1 
ATOM   1322 C  CB  . VAL A 1 239 ? 133.348 127.534 139.778 1.00 19.62  ? 237 VAL A CB  1 
ATOM   1323 C  CG1 . VAL A 1 239 ? 134.624 126.778 140.094 1.00 25.14  ? 237 VAL A CG1 1 
ATOM   1324 C  CG2 . VAL A 1 239 ? 133.667 128.945 139.329 1.00 19.36  ? 237 VAL A CG2 1 
ATOM   1325 N  N   . ASP A 1 240 ? 131.268 125.134 139.953 1.00 21.61  ? 238 ASP A N   1 
ATOM   1326 C  CA  . ASP A 1 240 ? 130.884 123.773 140.311 1.00 16.81  ? 238 ASP A CA  1 
ATOM   1327 C  C   . ASP A 1 240 ? 130.362 123.011 139.101 1.00 12.81  ? 238 ASP A C   1 
ATOM   1328 O  O   . ASP A 1 240 ? 130.646 121.820 138.939 1.00 20.55  ? 238 ASP A O   1 
ATOM   1329 C  CB  . ASP A 1 240 ? 129.826 123.800 141.410 1.00 18.98  ? 238 ASP A CB  1 
ATOM   1330 C  CG  . ASP A 1 240 ? 130.305 124.496 142.660 1.00 29.57  ? 238 ASP A CG  1 
ATOM   1331 O  OD1 . ASP A 1 240 ? 131.532 124.660 142.814 1.00 32.49  ? 238 ASP A OD1 1 
ATOM   1332 O  OD2 . ASP A 1 240 ? 129.455 124.877 143.491 1.00 32.78  ? 238 ASP A OD2 1 
ATOM   1333 N  N   . PHE A 1 241 ? 129.588 123.678 138.245 1.00 17.93  ? 239 PHE A N   1 
ATOM   1334 C  CA  . PHE A 1 241 ? 129.016 123.008 137.084 1.00 17.37  ? 239 PHE A CA  1 
ATOM   1335 C  C   . PHE A 1 241 ? 130.104 122.515 136.139 1.00 18.35  ? 239 PHE A C   1 
ATOM   1336 O  O   . PHE A 1 241 ? 130.089 121.357 135.708 1.00 30.04  ? 239 PHE A O   1 
ATOM   1337 C  CB  . PHE A 1 241 ? 128.062 123.954 136.357 1.00 13.09  ? 239 PHE A CB  1 
ATOM   1338 C  CG  . PHE A 1 241 ? 127.381 123.335 135.175 1.00 19.93  ? 239 PHE A CG  1 
ATOM   1339 C  CD1 . PHE A 1 241 ? 126.225 122.593 135.336 1.00 24.71  ? 239 PHE A CD1 1 
ATOM   1340 C  CD2 . PHE A 1 241 ? 127.896 123.492 133.903 1.00 19.44  ? 239 PHE A CD2 1 
ATOM   1341 C  CE1 . PHE A 1 241 ? 125.598 122.022 134.251 1.00 18.64  ? 239 PHE A CE1 1 
ATOM   1342 C  CE2 . PHE A 1 241 ? 127.273 122.923 132.817 1.00 22.70  ? 239 PHE A CE2 1 
ATOM   1343 C  CZ  . PHE A 1 241 ? 126.121 122.186 132.991 1.00 12.09  ? 239 PHE A CZ  1 
ATOM   1344 N  N   . PHE A 1 242 ? 131.058 123.382 135.800 1.00 18.22  ? 240 PHE A N   1 
ATOM   1345 C  CA  . PHE A 1 242 ? 132.095 123.011 134.847 1.00 17.78  ? 240 PHE A CA  1 
ATOM   1346 C  C   . PHE A 1 242 ? 133.198 122.173 135.473 1.00 20.51  ? 240 PHE A C   1 
ATOM   1347 O  O   . PHE A 1 242 ? 133.905 121.468 134.749 1.00 26.26  ? 240 PHE A O   1 
ATOM   1348 C  CB  . PHE A 1 242 ? 132.686 124.266 134.208 1.00 19.76  ? 240 PHE A CB  1 
ATOM   1349 C  CG  . PHE A 1 242 ? 131.742 124.959 133.275 1.00 22.68  ? 240 PHE A CG  1 
ATOM   1350 C  CD1 . PHE A 1 242 ? 131.464 124.426 132.030 1.00 18.45  ? 240 PHE A CD1 1 
ATOM   1351 C  CD2 . PHE A 1 242 ? 131.118 126.135 133.648 1.00 22.31  ? 240 PHE A CD2 1 
ATOM   1352 C  CE1 . PHE A 1 242 ? 130.592 125.055 131.175 1.00 20.90  ? 240 PHE A CE1 1 
ATOM   1353 C  CE2 . PHE A 1 242 ? 130.244 126.766 132.794 1.00 21.32  ? 240 PHE A CE2 1 
ATOM   1354 C  CZ  . PHE A 1 242 ? 129.981 126.225 131.556 1.00 21.32  ? 240 PHE A CZ  1 
ATOM   1355 N  N   . ASN A 1 243 ? 133.367 122.235 136.794 1.00 19.50  ? 241 ASN A N   1 
ATOM   1356 C  CA  . ASN A 1 243 ? 134.238 121.278 137.466 1.00 12.94  ? 241 ASN A CA  1 
ATOM   1357 C  C   . ASN A 1 243 ? 133.699 119.864 137.311 1.00 23.31  ? 241 ASN A C   1 
ATOM   1358 O  O   . ASN A 1 243 ? 134.438 118.937 136.966 1.00 33.22  ? 241 ASN A O   1 
ATOM   1359 C  CB  . ASN A 1 243 ? 134.373 121.640 138.944 1.00 21.18  ? 241 ASN A CB  1 
ATOM   1360 C  CG  . ASN A 1 243 ? 135.720 121.267 139.513 1.00 33.40  ? 241 ASN A CG  1 
ATOM   1361 O  OD1 . ASN A 1 243 ? 135.817 120.452 140.429 1.00 38.88  ? 241 ASN A OD1 1 
ATOM   1362 N  ND2 . ASN A 1 243 ? 136.771 121.869 138.979 1.00 35.09  ? 241 ASN A ND2 1 
ATOM   1363 N  N   . ALA A 1 244 ? 132.400 119.684 137.559 1.00 21.88  ? 242 ALA A N   1 
ATOM   1364 C  CA  . ALA A 1 244 ? 131.787 118.373 137.391 1.00 16.72  ? 242 ALA A CA  1 
ATOM   1365 C  C   . ALA A 1 244 ? 131.774 117.953 135.929 1.00 20.50  ? 242 ALA A C   1 
ATOM   1366 O  O   . ALA A 1 244 ? 131.999 116.781 135.612 1.00 25.33  ? 242 ALA A O   1 
ATOM   1367 C  CB  . ALA A 1 244 ? 130.369 118.386 137.958 1.00 20.99  ? 242 ALA A CB  1 
ATOM   1368 N  N   . LEU A 1 245 ? 131.502 118.893 135.024 1.00 23.23  ? 243 LEU A N   1 
ATOM   1369 C  CA  . LEU A 1 245 ? 131.499 118.568 133.603 1.00 19.49  ? 243 LEU A CA  1 
ATOM   1370 C  C   . LEU A 1 245 ? 132.880 118.133 133.136 1.00 18.71  ? 243 LEU A C   1 
ATOM   1371 O  O   . LEU A 1 245 ? 133.009 117.197 132.340 1.00 26.45  ? 243 LEU A O   1 
ATOM   1372 C  CB  . LEU A 1 245 ? 131.010 119.768 132.794 1.00 23.04  ? 243 LEU A CB  1 
ATOM   1373 C  CG  . LEU A 1 245 ? 130.950 119.579 131.279 1.00 27.69  ? 243 LEU A CG  1 
ATOM   1374 C  CD1 . LEU A 1 245 ? 130.031 118.430 130.917 1.00 25.21  ? 243 LEU A CD1 1 
ATOM   1375 C  CD2 . LEU A 1 245 ? 130.500 120.858 130.603 1.00 27.42  ? 243 LEU A CD2 1 
ATOM   1376 N  N   . SER A 1 246 ? 133.928 118.809 133.610 1.00 28.68  ? 244 SER A N   1 
ATOM   1377 C  CA  . SER A 1 246 ? 135.284 118.408 133.255 1.00 25.72  ? 244 SER A CA  1 
ATOM   1378 C  C   . SER A 1 246 ? 135.605 117.024 133.803 1.00 26.93  ? 244 SER A C   1 
ATOM   1379 O  O   . SER A 1 246 ? 136.232 116.208 133.119 1.00 35.50  ? 244 SER A O   1 
ATOM   1380 C  CB  . SER A 1 246 ? 136.286 119.436 133.773 1.00 25.42  ? 244 SER A CB  1 
ATOM   1381 O  OG  . SER A 1 246 ? 137.439 119.475 132.954 1.00 38.21  ? 244 SER A OG  1 
ATOM   1382 N  N   . ASP A 1 247 ? 135.190 116.745 135.040 1.00 22.58  ? 245 ASP A N   1 
ATOM   1383 C  CA  . ASP A 1 247 ? 135.394 115.416 135.605 1.00 19.36  ? 245 ASP A CA  1 
ATOM   1384 C  C   . ASP A 1 247 ? 134.628 114.361 134.819 1.00 22.28  ? 245 ASP A C   1 
ATOM   1385 O  O   . ASP A 1 247 ? 135.142 113.265 134.574 1.00 34.04  ? 245 ASP A O   1 
ATOM   1386 C  CB  . ASP A 1 247 ? 134.968 115.401 137.071 1.00 24.16  ? 245 ASP A CB  1 
ATOM   1387 C  CG  . ASP A 1 247 ? 135.902 116.192 137.958 1.00 32.83  ? 245 ASP A CG  1 
ATOM   1388 O  OD1 . ASP A 1 247 ? 137.089 116.335 137.598 1.00 38.33  ? 245 ASP A OD1 1 
ATOM   1389 O  OD2 . ASP A 1 247 ? 135.451 116.672 139.019 1.00 33.59  ? 245 ASP A OD2 1 
ATOM   1390 N  N   . ALA A 1 248 ? 133.392 114.669 134.426 1.00 28.84  ? 246 ALA A N   1 
ATOM   1391 C  CA  . ALA A 1 248 ? 132.596 113.710 133.670 1.00 19.08  ? 246 ALA A CA  1 
ATOM   1392 C  C   . ALA A 1 248 ? 133.209 113.434 132.304 1.00 22.85  ? 246 ALA A C   1 
ATOM   1393 O  O   . ALA A 1 248 ? 133.197 112.293 131.833 1.00 33.12  ? 246 ALA A O   1 
ATOM   1394 C  CB  . ALA A 1 248 ? 131.166 114.222 133.523 1.00 17.62  ? 246 ALA A CB  1 
ATOM   1395 N  N   . THR A 1 249 ? 133.735 114.467 131.646 1.00 29.43  ? 247 THR A N   1 
ATOM   1396 C  CA  . THR A 1 249 ? 134.344 114.274 130.334 1.00 24.70  ? 247 THR A CA  1 
ATOM   1397 C  C   . THR A 1 249 ? 135.588 113.401 130.426 1.00 23.65  ? 247 THR A C   1 
ATOM   1398 O  O   . THR A 1 249 ? 135.837 112.572 129.545 1.00 27.82  ? 247 THR A O   1 
ATOM   1399 C  CB  . THR A 1 249 ? 134.684 115.625 129.708 1.00 22.47  ? 247 THR A CB  1 
ATOM   1400 O  OG1 . THR A 1 249 ? 133.583 116.523 129.878 1.00 25.65  ? 247 THR A OG1 1 
ATOM   1401 C  CG2 . THR A 1 249 ? 134.977 115.467 128.229 1.00 30.08  ? 247 THR A CG2 1 
ATOM   1402 N  N   . MET A 1 250 ? 136.391 113.584 131.474 1.00 25.00  ? 248 MET A N   1 
ATOM   1403 C  CA  . MET A 1 250 ? 137.566 112.740 131.653 1.00 23.42  ? 248 MET A CA  1 
ATOM   1404 C  C   . MET A 1 250 ? 137.168 111.301 131.949 1.00 26.93  ? 248 MET A C   1 
ATOM   1405 O  O   . MET A 1 250 ? 137.843 110.363 131.514 1.00 33.76  ? 248 MET A O   1 
ATOM   1406 C  CB  . MET A 1 250 ? 138.444 113.294 132.774 1.00 26.74  ? 248 MET A CB  1 
ATOM   1407 C  CG  . MET A 1 250 ? 139.120 114.620 132.453 1.00 30.12  ? 248 MET A CG  1 
ATOM   1408 S  SD  . MET A 1 250 ? 139.901 114.671 130.830 1.00 43.99  ? 248 MET A SD  1 
ATOM   1409 C  CE  . MET A 1 250 ? 141.394 113.736 131.143 1.00 29.19  ? 248 MET A CE  1 
ATOM   1410 N  N   . LYS A 1 251 ? 136.080 111.106 132.695 1.00 31.00  ? 249 LYS A N   1 
ATOM   1411 C  CA  . LYS A 1 251 ? 135.584 109.757 132.938 1.00 23.26  ? 249 LYS A CA  1 
ATOM   1412 C  C   . LYS A 1 251 ? 135.110 109.107 131.646 1.00 19.68  ? 249 LYS A C   1 
ATOM   1413 O  O   . LYS A 1 251 ? 135.300 107.903 131.442 1.00 30.12  ? 249 LYS A O   1 
ATOM   1414 C  CB  . LYS A 1 251 ? 134.457 109.795 133.966 1.00 22.61  ? 249 LYS A CB  1 
ATOM   1415 C  CG  . LYS A 1 251 ? 134.919 110.143 135.365 1.00 27.44  ? 249 LYS A CG  1 
ATOM   1416 C  CD  . LYS A 1 251 ? 134.585 109.042 136.354 1.00 32.83  ? 249 LYS A CD  1 
ATOM   1417 C  CE  . LYS A 1 251 ? 135.410 109.159 137.626 1.00 35.89  ? 249 LYS A CE  1 
ATOM   1418 N  NZ  . LYS A 1 251 ? 135.784 110.565 137.940 1.00 37.07  ? 249 LYS A NZ  1 
ATOM   1419 N  N   . ILE A 1 252 ? 134.475 109.882 130.766 1.00 19.68  ? 250 ILE A N   1 
ATOM   1420 C  CA  . ILE A 1 252 ? 134.059 109.348 129.475 1.00 20.37  ? 250 ILE A CA  1 
ATOM   1421 C  C   . ILE A 1 252 ? 135.275 109.010 128.622 1.00 21.28  ? 250 ILE A C   1 
ATOM   1422 O  O   . ILE A 1 252 ? 135.273 108.022 127.880 1.00 29.78  ? 250 ILE A O   1 
ATOM   1423 C  CB  . ILE A 1 252 ? 133.122 110.339 128.763 1.00 28.11  ? 250 ILE A CB  1 
ATOM   1424 C  CG1 . ILE A 1 252 ? 131.794 110.448 129.517 1.00 24.35  ? 250 ILE A CG1 1 
ATOM   1425 C  CG2 . ILE A 1 252 ? 132.877 109.903 127.328 1.00 25.66  ? 250 ILE A CG2 1 
ATOM   1426 C  CD1 . ILE A 1 252 ? 130.982 111.669 129.160 1.00 20.66  ? 250 ILE A CD1 1 
ATOM   1427 N  N   . VAL A 1 253 ? 136.327 109.826 128.704 1.00 27.13  ? 251 VAL A N   1 
ATOM   1428 C  CA  . VAL A 1 253 ? 137.553 109.532 127.969 1.00 25.36  ? 251 VAL A CA  1 
ATOM   1429 C  C   . VAL A 1 253 ? 138.154 108.219 128.449 1.00 25.41  ? 251 VAL A C   1 
ATOM   1430 O  O   . VAL A 1 253 ? 138.706 107.446 127.659 1.00 34.97  ? 251 VAL A O   1 
ATOM   1431 C  CB  . VAL A 1 253 ? 138.551 110.696 128.106 1.00 25.74  ? 251 VAL A CB  1 
ATOM   1432 C  CG1 . VAL A 1 253 ? 139.948 110.256 127.705 1.00 24.30  ? 251 VAL A CG1 1 
ATOM   1433 C  CG2 . VAL A 1 253 ? 138.105 111.875 127.265 1.00 28.59  ? 251 VAL A CG2 1 
ATOM   1434 N  N   . GLN A 1 254 ? 138.062 107.948 129.752 1.00 30.83  ? 252 GLN A N   1 
ATOM   1435 C  CA  . GLN A 1 254 ? 138.548 106.678 130.279 1.00 20.34  ? 252 GLN A CA  1 
ATOM   1436 C  C   . GLN A 1 254 ? 137.769 105.506 129.699 1.00 23.23  ? 252 GLN A C   1 
ATOM   1437 O  O   . GLN A 1 254 ? 138.342 104.448 129.421 1.00 38.38  ? 252 GLN A O   1 
ATOM   1438 C  CB  . GLN A 1 254 ? 138.455 106.674 131.802 1.00 28.27  ? 252 GLN A CB  1 
ATOM   1439 C  CG  . GLN A 1 254 ? 139.597 107.389 132.493 1.00 36.20  ? 252 GLN A CG  1 
ATOM   1440 C  CD  . GLN A 1 254 ? 139.317 107.639 133.961 1.00 42.17  ? 252 GLN A CD  1 
ATOM   1441 O  OE1 . GLN A 1 254 ? 139.563 108.730 134.475 1.00 40.27  ? 252 GLN A OE1 1 
ATOM   1442 N  NE2 . GLN A 1 254 ? 138.793 106.627 134.643 1.00 38.67  ? 252 GLN A NE2 1 
ATOM   1443 N  N   . ILE A 1 255 ? 136.456 105.668 129.526 1.00 26.12  ? 253 ILE A N   1 
ATOM   1444 C  CA  . ILE A 1 255 ? 135.653 104.613 128.914 1.00 26.63  ? 253 ILE A CA  1 
ATOM   1445 C  C   . ILE A 1 255 ? 136.122 104.355 127.490 1.00 23.66  ? 253 ILE A C   1 
ATOM   1446 O  O   . ILE A 1 255 ? 136.180 103.207 127.037 1.00 29.01  ? 253 ILE A O   1 
ATOM   1447 C  CB  . ILE A 1 255 ? 134.158 104.982 128.958 1.00 28.15  ? 253 ILE A CB  1 
ATOM   1448 C  CG1 . ILE A 1 255 ? 133.675 105.094 130.404 1.00 27.93  ? 253 ILE A CG1 1 
ATOM   1449 C  CG2 . ILE A 1 255 ? 133.334 103.949 128.208 1.00 26.52  ? 253 ILE A CG2 1 
ATOM   1450 C  CD1 . ILE A 1 255 ? 132.335 105.771 130.545 1.00 31.29  ? 253 ILE A CD1 1 
ATOM   1451 N  N   . ILE A 1 256 ? 136.447 105.420 126.756 1.00 28.11  ? 254 ILE A N   1 
ATOM   1452 C  CA  . ILE A 1 256 ? 136.929 105.259 125.390 1.00 25.81  ? 254 ILE A CA  1 
ATOM   1453 C  C   . ILE A 1 256 ? 138.271 104.541 125.371 1.00 29.53  ? 254 ILE A C   1 
ATOM   1454 O  O   . ILE A 1 256 ? 138.617 103.889 124.380 1.00 37.82  ? 254 ILE A O   1 
ATOM   1455 C  CB  . ILE A 1 256 ? 137.007 106.628 124.691 1.00 25.58  ? 254 ILE A CB  1 
ATOM   1456 C  CG1 . ILE A 1 256 ? 135.607 107.226 124.538 1.00 23.50  ? 254 ILE A CG1 1 
ATOM   1457 C  CG2 . ILE A 1 256 ? 137.673 106.497 123.333 1.00 32.24  ? 254 ILE A CG2 1 
ATOM   1458 C  CD1 . ILE A 1 256 ? 135.597 108.724 124.351 1.00 26.06  ? 254 ILE A CD1 1 
ATOM   1459 N  N   . MET A 1 257 ? 139.053 104.648 126.448 1.00 28.39  ? 255 MET A N   1 
ATOM   1460 C  CA  . MET A 1 257 ? 140.324 103.937 126.517 1.00 29.98  ? 255 MET A CA  1 
ATOM   1461 C  C   . MET A 1 257 ? 140.141 102.427 126.540 1.00 31.85  ? 255 MET A C   1 
ATOM   1462 O  O   . MET A 1 257 ? 141.086 101.699 126.222 1.00 38.57  ? 255 MET A O   1 
ATOM   1463 C  CB  . MET A 1 257 ? 141.112 104.367 127.755 1.00 33.11  ? 255 MET A CB  1 
ATOM   1464 C  CG  . MET A 1 257 ? 141.535 105.828 127.780 1.00 35.77  ? 255 MET A CG  1 
ATOM   1465 S  SD  . MET A 1 257 ? 142.216 106.421 126.224 1.00 50.24  ? 255 MET A SD  1 
ATOM   1466 C  CE  . MET A 1 257 ? 143.801 105.592 126.225 1.00 34.51  ? 255 MET A CE  1 
ATOM   1467 N  N   . TRP A 1 258 ? 138.961 101.938 126.925 1.00 30.20  ? 256 TRP A N   1 
ATOM   1468 C  CA  . TRP A 1 258 ? 138.699 100.505 126.856 1.00 24.02  ? 256 TRP A CA  1 
ATOM   1469 C  C   . TRP A 1 258 ? 138.605 100.035 125.412 1.00 28.12  ? 256 TRP A C   1 
ATOM   1470 O  O   . TRP A 1 258 ? 139.003 98.911  125.090 1.00 37.28  ? 256 TRP A O   1 
ATOM   1471 C  CB  . TRP A 1 258 ? 137.416 100.168 127.612 1.00 31.06  ? 256 TRP A CB  1 
ATOM   1472 C  CG  . TRP A 1 258 ? 137.557 100.247 129.095 1.00 36.55  ? 256 TRP A CG  1 
ATOM   1473 C  CD1 . TRP A 1 258 ? 137.105 101.241 129.907 1.00 35.75  ? 256 TRP A CD1 1 
ATOM   1474 C  CD2 . TRP A 1 258 ? 138.190 99.288  129.949 1.00 41.02  ? 256 TRP A CD2 1 
ATOM   1475 N  NE1 . TRP A 1 258 ? 137.418 100.966 131.213 1.00 34.95  ? 256 TRP A NE1 1 
ATOM   1476 C  CE2 . TRP A 1 258 ? 138.085 99.771  131.267 1.00 43.67  ? 256 TRP A CE2 1 
ATOM   1477 C  CE3 . TRP A 1 258 ? 138.835 98.068  129.727 1.00 39.69  ? 256 TRP A CE3 1 
ATOM   1478 C  CZ2 . TRP A 1 258 ? 138.602 99.079  132.359 1.00 44.99  ? 256 TRP A CZ2 1 
ATOM   1479 C  CZ3 . TRP A 1 258 ? 139.348 97.383  130.812 1.00 41.56  ? 256 TRP A CZ3 1 
ATOM   1480 C  CH2 . TRP A 1 258 ? 139.228 97.889  132.112 1.00 43.47  ? 256 TRP A CH2 1 
ATOM   1481 N  N   . TYR A 1 259 ? 138.073 100.879 124.532 1.00 30.55  ? 257 TYR A N   1 
ATOM   1482 C  CA  . TYR A 1 259 ? 137.976 100.561 123.115 1.00 27.86  ? 257 TYR A CA  1 
ATOM   1483 C  C   . TYR A 1 259 ? 139.201 100.995 122.323 1.00 30.54  ? 257 TYR A C   1 
ATOM   1484 O  O   . TYR A 1 259 ? 139.383 100.536 121.191 1.00 38.01  ? 257 TYR A O   1 
ATOM   1485 C  CB  . TYR A 1 259 ? 136.727 101.222 122.525 1.00 26.83  ? 257 TYR A CB  1 
ATOM   1486 C  CG  . TYR A 1 259 ? 136.559 101.015 121.042 1.00 30.05  ? 257 TYR A CG  1 
ATOM   1487 C  CD1 . TYR A 1 259 ? 136.127 99.800  120.536 1.00 30.21  ? 257 TYR A CD1 1 
ATOM   1488 C  CD2 . TYR A 1 259 ? 136.832 102.036 120.146 1.00 28.94  ? 257 TYR A CD2 1 
ATOM   1489 C  CE1 . TYR A 1 259 ? 135.975 99.608  119.182 1.00 30.05  ? 257 TYR A CE1 1 
ATOM   1490 C  CE2 . TYR A 1 259 ? 136.681 101.852 118.793 1.00 26.64  ? 257 TYR A CE2 1 
ATOM   1491 C  CZ  . TYR A 1 259 ? 136.252 100.638 118.316 1.00 29.37  ? 257 TYR A CZ  1 
ATOM   1492 O  OH  . TYR A 1 259 ? 136.104 100.455 116.964 1.00 37.99  ? 257 TYR A OH  1 
ATOM   1493 N  N   . MET A 1 260 ? 140.049 101.850 122.890 1.00 27.65  ? 258 MET A N   1 
ATOM   1494 C  CA  . MET A 1 260 ? 141.182 102.373 122.133 1.00 25.30  ? 258 MET A CA  1 
ATOM   1495 C  C   . MET A 1 260 ? 142.112 101.287 121.612 1.00 31.11  ? 258 MET A C   1 
ATOM   1496 O  O   . MET A 1 260 ? 142.535 101.388 120.448 1.00 30.29  ? 258 MET A O   1 
ATOM   1497 C  CB  . MET A 1 260 ? 141.959 103.375 122.996 1.00 28.62  ? 258 MET A CB  1 
ATOM   1498 C  CG  . MET A 1 260 ? 142.752 104.391 122.196 1.00 29.72  ? 258 MET A CG  1 
ATOM   1499 S  SD  . MET A 1 260 ? 142.718 106.038 122.914 1.00 51.50  ? 258 MET A SD  1 
ATOM   1500 C  CE  . MET A 1 260 ? 142.968 107.037 121.454 1.00 40.69  ? 258 MET A CE  1 
ATOM   1501 N  N   . PRO A 1 261 ? 142.482 100.261 122.385 1.00 36.36  ? 259 PRO A N   1 
ATOM   1502 C  CA  . PRO A 1 261 ? 143.380 99.235  121.827 1.00 33.54  ? 259 PRO A CA  1 
ATOM   1503 C  C   . PRO A 1 261 ? 142.849 98.600  120.556 1.00 35.05  ? 259 PRO A C   1 
ATOM   1504 O  O   . PRO A 1 261 ? 143.625 98.341  119.629 1.00 37.35  ? 259 PRO A O   1 
ATOM   1505 C  CB  . PRO A 1 261 ? 143.496 98.218  122.969 1.00 34.95  ? 259 PRO A CB  1 
ATOM   1506 C  CG  . PRO A 1 261 ? 143.189 98.984  124.196 1.00 35.10  ? 259 PRO A CG  1 
ATOM   1507 C  CD  . PRO A 1 261 ? 142.185 100.018 123.805 1.00 36.22  ? 259 PRO A CD  1 
ATOM   1508 N  N   . LEU A 1 262 ? 141.543 98.340  120.483 1.00 40.71  ? 260 LEU A N   1 
ATOM   1509 C  CA  . LEU A 1 262 ? 140.970 97.799  119.255 1.00 33.41  ? 260 LEU A CA  1 
ATOM   1510 C  C   . LEU A 1 262 ? 140.930 98.853  118.157 1.00 34.77  ? 260 LEU A C   1 
ATOM   1511 O  O   . LEU A 1 262 ? 141.238 98.560  116.997 1.00 35.24  ? 260 LEU A O   1 
ATOM   1512 C  CB  . LEU A 1 262 ? 139.569 97.256  119.522 1.00 31.94  ? 260 LEU A CB  1 
ATOM   1513 C  CG  . LEU A 1 262 ? 138.998 96.391  118.398 1.00 40.01  ? 260 LEU A CG  1 
ATOM   1514 C  CD1 . LEU A 1 262 ? 139.557 94.981  118.475 1.00 38.22  ? 260 LEU A CD1 1 
ATOM   1515 C  CD2 . LEU A 1 262 ? 137.481 96.378  118.448 1.00 40.53  ? 260 LEU A CD2 1 
ATOM   1516 N  N   . GLY A 1 263 ? 140.545 100.082 118.501 1.00 30.12  ? 261 GLY A N   1 
ATOM   1517 C  CA  . GLY A 1 263 ? 140.525 101.139 117.506 1.00 28.66  ? 261 GLY A CA  1 
ATOM   1518 C  C   . GLY A 1 263 ? 141.907 101.475 116.985 1.00 29.02  ? 261 GLY A C   1 
ATOM   1519 O  O   . GLY A 1 263 ? 142.085 101.732 115.794 1.00 37.44  ? 261 GLY A O   1 
ATOM   1520 N  N   . ILE A 1 264 ? 142.905 101.476 117.871 1.00 36.61  ? 262 ILE A N   1 
ATOM   1521 C  CA  . ILE A 1 264 ? 144.271 101.783 117.459 1.00 31.05  ? 262 ILE A CA  1 
ATOM   1522 C  C   . ILE A 1 264 ? 144.812 100.695 116.541 1.00 31.30  ? 262 ILE A C   1 
ATOM   1523 O  O   . ILE A 1 264 ? 145.579 100.975 115.613 1.00 42.94  ? 262 ILE A O   1 
ATOM   1524 C  CB  . ILE A 1 264 ? 145.166 101.976 118.697 1.00 32.34  ? 262 ILE A CB  1 
ATOM   1525 C  CG1 . ILE A 1 264 ? 144.819 103.283 119.415 1.00 35.96  ? 262 ILE A CG1 1 
ATOM   1526 C  CG2 . ILE A 1 264 ? 146.633 101.954 118.308 1.00 34.33  ? 262 ILE A CG2 1 
ATOM   1527 C  CD1 . ILE A 1 264 ? 145.198 104.540 118.660 1.00 40.26  ? 262 ILE A CD1 1 
ATOM   1528 N  N   . LEU A 1 265 ? 144.433 99.440  116.785 1.00 30.79  ? 263 LEU A N   1 
ATOM   1529 C  CA  . LEU A 1 265 ? 144.924 98.343  115.957 1.00 30.23  ? 263 LEU A CA  1 
ATOM   1530 C  C   . LEU A 1 265 ? 144.546 98.547  114.496 1.00 32.14  ? 263 LEU A C   1 
ATOM   1531 O  O   . LEU A 1 265 ? 145.384 98.399  113.600 1.00 33.76  ? 263 LEU A O   1 
ATOM   1532 C  CB  . LEU A 1 265 ? 144.371 97.015  116.472 1.00 29.85  ? 263 LEU A CB  1 
ATOM   1533 C  CG  . LEU A 1 265 ? 145.016 95.745  115.914 1.00 34.87  ? 263 LEU A CG  1 
ATOM   1534 C  CD1 . LEU A 1 265 ? 144.921 94.624  116.927 1.00 39.21  ? 263 LEU A CD1 1 
ATOM   1535 C  CD2 . LEU A 1 265 ? 144.376 95.329  114.600 1.00 34.89  ? 263 LEU A CD2 1 
ATOM   1536 N  N   . PHE A 1 266 ? 143.284 98.884  114.235 1.00 38.06  ? 264 PHE A N   1 
ATOM   1537 C  CA  . PHE A 1 266 ? 142.828 99.078  112.867 1.00 30.97  ? 264 PHE A CA  1 
ATOM   1538 C  C   . PHE A 1 266 ? 143.186 100.451 112.322 1.00 32.02  ? 264 PHE A C   1 
ATOM   1539 O  O   . PHE A 1 266 ? 143.158 100.645 111.102 1.00 38.79  ? 264 PHE A O   1 
ATOM   1540 C  CB  . PHE A 1 266 ? 141.317 98.865  112.789 1.00 29.40  ? 264 PHE A CB  1 
ATOM   1541 C  CG  . PHE A 1 266 ? 140.902 97.447  113.029 1.00 29.55  ? 264 PHE A CG  1 
ATOM   1542 C  CD1 . PHE A 1 266 ? 140.808 96.553  111.981 1.00 26.21  ? 264 PHE A CD1 1 
ATOM   1543 C  CD2 . PHE A 1 266 ? 140.617 97.003  114.306 1.00 34.65  ? 264 PHE A CD2 1 
ATOM   1544 C  CE1 . PHE A 1 266 ? 140.432 95.250  112.200 1.00 27.04  ? 264 PHE A CE1 1 
ATOM   1545 C  CE2 . PHE A 1 266 ? 140.240 95.700  114.530 1.00 32.71  ? 264 PHE A CE2 1 
ATOM   1546 C  CZ  . PHE A 1 266 ? 140.148 94.823  113.476 1.00 31.75  ? 264 PHE A CZ  1 
ATOM   1547 N  N   . LEU A 1 267 ? 143.515 101.404 113.193 1.00 32.58  ? 265 LEU A N   1 
ATOM   1548 C  CA  . LEU A 1 267 ? 144.012 102.693 112.727 1.00 35.58  ? 265 LEU A CA  1 
ATOM   1549 C  C   . LEU A 1 267 ? 145.420 102.555 112.161 1.00 38.47  ? 265 LEU A C   1 
ATOM   1550 O  O   . LEU A 1 267 ? 145.719 103.071 111.079 1.00 42.63  ? 265 LEU A O   1 
ATOM   1551 C  CB  . LEU A 1 267 ? 143.983 103.704 113.873 1.00 35.41  ? 265 LEU A CB  1 
ATOM   1552 C  CG  . LEU A 1 267 ? 143.468 105.119 113.597 1.00 37.01  ? 265 LEU A CG  1 
ATOM   1553 C  CD1 . LEU A 1 267 ? 142.122 105.117 112.902 1.00 36.04  ? 265 LEU A CD1 1 
ATOM   1554 C  CD2 . LEU A 1 267 ? 143.379 105.886 114.903 1.00 37.84  ? 265 LEU A CD2 1 
ATOM   1555 N  N   . ILE A 1 268 ? 146.298 101.857 112.883 1.00 40.39  ? 266 ILE A N   1 
ATOM   1556 C  CA  . ILE A 1 268 ? 147.649 101.620 112.386 1.00 36.97  ? 266 ILE A CA  1 
ATOM   1557 C  C   . ILE A 1 268 ? 147.624 100.647 111.216 1.00 39.94  ? 266 ILE A C   1 
ATOM   1558 O  O   . ILE A 1 268 ? 148.302 100.854 110.204 1.00 45.17  ? 266 ILE A O   1 
ATOM   1559 C  CB  . ILE A 1 268 ? 148.553 101.110 113.522 1.00 34.56  ? 266 ILE A CB  1 
ATOM   1560 C  CG1 . ILE A 1 268 ? 148.758 102.204 114.567 1.00 38.15  ? 266 ILE A CG1 1 
ATOM   1561 C  CG2 . ILE A 1 268 ? 149.891 100.650 112.972 1.00 39.03  ? 266 ILE A CG2 1 
ATOM   1562 C  CD1 . ILE A 1 268 ? 148.950 101.675 115.961 1.00 42.12  ? 266 ILE A CD1 1 
ATOM   1563 N  N   . ALA A 1 269 ? 146.852 99.566  111.337 1.00 38.56  ? 267 ALA A N   1 
ATOM   1564 C  CA  . ALA A 1 269 ? 146.777 98.590  110.256 1.00 39.02  ? 267 ALA A CA  1 
ATOM   1565 C  C   . ALA A 1 269 ? 146.188 99.208  108.997 1.00 39.80  ? 267 ALA A C   1 
ATOM   1566 O  O   . ALA A 1 269 ? 146.663 98.947  107.887 1.00 42.33  ? 267 ALA A O   1 
ATOM   1567 C  CB  . ALA A 1 269 ? 145.950 97.383  110.696 1.00 36.95  ? 267 ALA A CB  1 
ATOM   1568 N  N   . GLY A 1 270 ? 145.150 100.031 109.149 1.00 40.81  ? 268 GLY A N   1 
ATOM   1569 C  CA  . GLY A 1 270 ? 144.529 100.644 107.988 1.00 40.95  ? 268 GLY A CA  1 
ATOM   1570 C  C   . GLY A 1 270 ? 145.459 101.590 107.256 1.00 41.20  ? 268 GLY A C   1 
ATOM   1571 O  O   . GLY A 1 270 ? 145.451 101.655 106.025 1.00 45.26  ? 268 GLY A O   1 
ATOM   1572 N  N   . CYS A 1 271 ? 146.269 102.344 108.003 1.00 47.22  ? 269 CYS A N   1 
ATOM   1573 C  CA  . CYS A 1 271 ? 147.202 103.271 107.370 1.00 44.43  ? 269 CYS A CA  1 
ATOM   1574 C  C   . CYS A 1 271 ? 148.232 102.531 106.526 1.00 43.51  ? 269 CYS A C   1 
ATOM   1575 O  O   . CYS A 1 271 ? 148.551 102.957 105.411 1.00 48.22  ? 269 CYS A O   1 
ATOM   1576 C  CB  . CYS A 1 271 ? 147.897 104.120 108.432 1.00 46.03  ? 269 CYS A CB  1 
ATOM   1577 S  SG  . CYS A 1 271 ? 149.028 105.351 107.750 1.00 66.55  ? 269 CYS A SG  1 
ATOM   1578 N  N   . ILE A 1 272 ? 148.767 101.425 107.042 1.00 41.13  ? 270 ILE A N   1 
ATOM   1579 C  CA  . ILE A 1 272 ? 149.760 100.664 106.290 1.00 43.23  ? 270 ILE A CA  1 
ATOM   1580 C  C   . ILE A 1 272 ? 149.134 100.058 105.042 1.00 43.11  ? 270 ILE A C   1 
ATOM   1581 O  O   . ILE A 1 272 ? 149.753 100.023 103.974 1.00 48.44  ? 270 ILE A O   1 
ATOM   1582 C  CB  . ILE A 1 272 ? 150.395 99.584  107.184 1.00 43.07  ? 270 ILE A CB  1 
ATOM   1583 C  CG1 . ILE A 1 272 ? 151.137 100.225 108.355 1.00 43.42  ? 270 ILE A CG1 1 
ATOM   1584 C  CG2 . ILE A 1 272 ? 151.345 98.722  106.379 1.00 44.79  ? 270 ILE A CG2 1 
ATOM   1585 C  CD1 . ILE A 1 272 ? 151.217 99.344  109.569 1.00 41.10  ? 270 ILE A CD1 1 
ATOM   1586 N  N   . ILE A 1 273 ? 147.899 99.568  105.156 1.00 41.18  ? 271 ILE A N   1 
ATOM   1587 C  CA  . ILE A 1 273 ? 147.242 98.938  104.017 1.00 46.82  ? 271 ILE A CA  1 
ATOM   1588 C  C   . ILE A 1 273 ? 147.001 99.948  102.903 1.00 44.03  ? 271 ILE A C   1 
ATOM   1589 O  O   . ILE A 1 273 ? 147.046 99.597  101.718 1.00 42.62  ? 271 ILE A O   1 
ATOM   1590 C  CB  . ILE A 1 273 ? 145.932 98.269  104.470 1.00 42.91  ? 271 ILE A CB  1 
ATOM   1591 C  CG1 . ILE A 1 273 ? 146.237 97.024  105.302 1.00 40.87  ? 271 ILE A CG1 1 
ATOM   1592 C  CG2 . ILE A 1 273 ? 145.080 97.899  103.275 1.00 43.85  ? 271 ILE A CG2 1 
ATOM   1593 C  CD1 . ILE A 1 273 ? 145.125 96.628  106.237 1.00 41.46  ? 271 ILE A CD1 1 
ATOM   1594 N  N   . GLU A 1 274 ? 146.734 101.207 103.253 1.00 46.26  ? 272 GLU A N   1 
ATOM   1595 C  CA  . GLU A 1 274 ? 146.471 102.219 102.236 1.00 43.49  ? 272 GLU A CA  1 
ATOM   1596 C  C   . GLU A 1 274 ? 147.688 102.466 101.353 1.00 45.61  ? 272 GLU A C   1 
ATOM   1597 O  O   . GLU A 1 274 ? 147.538 102.836 100.183 1.00 47.07  ? 272 GLU A O   1 
ATOM   1598 C  CB  . GLU A 1 274 ? 146.030 103.520 102.901 1.00 41.65  ? 272 GLU A CB  1 
ATOM   1599 C  CG  . GLU A 1 274 ? 144.535 103.617 103.132 1.00 44.31  ? 272 GLU A CG  1 
ATOM   1600 C  CD  . GLU A 1 274 ? 144.112 104.981 103.638 1.00 51.11  ? 272 GLU A CD  1 
ATOM   1601 O  OE1 . GLU A 1 274 ? 144.381 105.287 104.819 1.00 48.35  ? 272 GLU A OE1 1 
ATOM   1602 O  OE2 . GLU A 1 274 ? 143.511 105.747 102.856 1.00 50.63  ? 272 GLU A OE2 1 
ATOM   1603 N  N   . VAL A 1 275 ? 148.896 102.275 101.888 1.00 52.35  ? 273 VAL A N   1 
ATOM   1604 C  CA  . VAL A 1 275 ? 150.098 102.471 101.088 1.00 53.17  ? 273 VAL A CA  1 
ATOM   1605 C  C   . VAL A 1 275 ? 150.093 101.496 99.920  1.00 53.01  ? 273 VAL A C   1 
ATOM   1606 O  O   . VAL A 1 275 ? 149.737 100.319 100.065 1.00 50.85  ? 273 VAL A O   1 
ATOM   1607 C  CB  . VAL A 1 275 ? 151.358 102.296 101.951 1.00 51.37  ? 273 VAL A CB  1 
ATOM   1608 C  CG1 . VAL A 1 275 ? 152.604 102.539 101.118 1.00 51.66  ? 273 VAL A CG1 1 
ATOM   1609 C  CG2 . VAL A 1 275 ? 151.323 103.238 103.145 1.00 50.97  ? 273 VAL A CG2 1 
ATOM   1610 N  N   . GLU A 1 276 ? 150.497 101.985 98.747  1.00 53.35  ? 274 GLU A N   1 
ATOM   1611 C  CA  . GLU A 1 276 ? 150.374 101.211 97.516  1.00 52.25  ? 274 GLU A CA  1 
ATOM   1612 C  C   . GLU A 1 276 ? 151.645 100.430 97.188  1.00 55.90  ? 274 GLU A C   1 
ATOM   1613 O  O   . GLU A 1 276 ? 151.616 99.198  97.111  1.00 56.23  ? 274 GLU A O   1 
ATOM   1614 C  CB  . GLU A 1 276 ? 150.007 102.142 96.355  1.00 51.97  ? 274 GLU A CB  1 
ATOM   1615 C  CG  . GLU A 1 276 ? 148.628 102.774 96.476  1.00 53.36  ? 274 GLU A CG  1 
ATOM   1616 C  CD  . GLU A 1 276 ? 147.519 101.746 96.604  1.00 59.32  ? 274 GLU A CD  1 
ATOM   1617 O  OE1 . GLU A 1 276 ? 147.381 100.900 95.696  1.00 54.55  ? 274 GLU A OE1 1 
ATOM   1618 O  OE2 . GLU A 1 276 ? 146.785 101.784 97.614  1.00 56.76  ? 274 GLU A OE2 1 
ATOM   1619 N  N   . ASP A 1 277 ? 152.769 101.129 96.998  1.00 56.24  ? 275 ASP A N   1 
ATOM   1620 C  CA  . ASP A 1 277 ? 153.976 100.500 96.474  1.00 57.02  ? 275 ASP A CA  1 
ATOM   1621 C  C   . ASP A 1 277 ? 155.227 100.793 97.295  1.00 58.08  ? 275 ASP A C   1 
ATOM   1622 O  O   . ASP A 1 277 ? 156.323 100.398 96.882  1.00 59.94  ? 275 ASP A O   1 
ATOM   1623 C  CB  . ASP A 1 277 ? 154.215 100.938 95.025  1.00 54.19  ? 275 ASP A CB  1 
ATOM   1624 C  CG  . ASP A 1 277 ? 154.348 102.440 94.888  1.00 58.24  ? 275 ASP A CG  1 
ATOM   1625 O  OD1 . ASP A 1 277 ? 154.083 103.152 95.879  1.00 58.32  ? 275 ASP A OD1 1 
ATOM   1626 O  OD2 . ASP A 1 277 ? 154.723 102.908 93.793  1.00 58.11  ? 275 ASP A OD2 1 
ATOM   1627 N  N   . TRP A 1 278 ? 155.105 101.484 98.426  1.00 51.18  ? 276 TRP A N   1 
ATOM   1628 C  CA  . TRP A 1 278 ? 156.207 101.850 99.312  1.00 52.37  ? 276 TRP A CA  1 
ATOM   1629 C  C   . TRP A 1 278 ? 157.142 102.877 98.686  1.00 53.48  ? 276 TRP A C   1 
ATOM   1630 O  O   . TRP A 1 278 ? 158.075 103.329 99.358  1.00 56.02  ? 276 TRP A O   1 
ATOM   1631 C  CB  . TRP A 1 278 ? 157.054 100.642 99.743  1.00 51.65  ? 276 TRP A CB  1 
ATOM   1632 C  CG  . TRP A 1 278 ? 156.387 99.715  100.719 1.00 53.30  ? 276 TRP A CG  1 
ATOM   1633 C  CD1 . TRP A 1 278 ? 156.250 98.364  100.595 1.00 53.08  ? 276 TRP A CD1 1 
ATOM   1634 C  CD2 . TRP A 1 278 ? 155.775 100.066 101.967 1.00 50.41  ? 276 TRP A CD2 1 
ATOM   1635 N  NE1 . TRP A 1 278 ? 155.592 97.851  101.684 1.00 53.53  ? 276 TRP A NE1 1 
ATOM   1636 C  CE2 . TRP A 1 278 ? 155.288 98.875  102.542 1.00 53.85  ? 276 TRP A CE2 1 
ATOM   1637 C  CE3 . TRP A 1 278 ? 155.591 101.270 102.654 1.00 53.31  ? 276 TRP A CE3 1 
ATOM   1638 C  CZ2 . TRP A 1 278 ? 154.629 98.854  103.769 1.00 54.42  ? 276 TRP A CZ2 1 
ATOM   1639 C  CZ3 . TRP A 1 278 ? 154.936 101.246 103.872 1.00 53.58  ? 276 TRP A CZ3 1 
ATOM   1640 C  CH2 . TRP A 1 278 ? 154.463 100.046 104.416 1.00 53.37  ? 276 TRP A CH2 1 
ATOM   1641 N  N   . GLU A 1 279 ? 156.931 103.264 97.427  1.00 53.72  ? 277 GLU A N   1 
ATOM   1642 C  CA  . GLU A 1 279 ? 157.796 104.265 96.816  1.00 53.63  ? 277 GLU A CA  1 
ATOM   1643 C  C   . GLU A 1 279 ? 157.507 105.655 97.362  1.00 53.17  ? 277 GLU A C   1 
ATOM   1644 O  O   . GLU A 1 279 ? 158.389 106.520 97.352  1.00 54.13  ? 277 GLU A O   1 
ATOM   1645 C  CB  . GLU A 1 279 ? 157.630 104.250 95.296  1.00 54.69  ? 277 GLU A CB  1 
ATOM   1646 C  CG  . GLU A 1 279 ? 158.772 103.575 94.547  1.00 56.14  ? 277 GLU A CG  1 
ATOM   1647 C  CD  . GLU A 1 279 ? 158.570 102.079 94.377  1.00 58.24  ? 277 GLU A CD  1 
ATOM   1648 O  OE1 . GLU A 1 279 ? 157.486 101.572 94.733  1.00 57.91  ? 277 GLU A OE1 1 
ATOM   1649 O  OE2 . GLU A 1 279 ? 159.499 101.408 93.881  1.00 56.20  ? 277 GLU A OE2 1 
ATOM   1650 N  N   . ILE A 1 280 ? 156.282 105.891 97.834  1.00 50.11  ? 278 ILE A N   1 
ATOM   1651 C  CA  . ILE A 1 280 ? 155.952 107.191 98.407  1.00 53.17  ? 278 ILE A CA  1 
ATOM   1652 C  C   . ILE A 1 280 ? 156.734 107.417 99.693  1.00 53.29  ? 278 ILE A C   1 
ATOM   1653 O  O   . ILE A 1 280 ? 157.144 108.543 99.996  1.00 54.74  ? 278 ILE A O   1 
ATOM   1654 C  CB  . ILE A 1 280 ? 154.434 107.306 98.632  1.00 52.92  ? 278 ILE A CB  1 
ATOM   1655 C  CG1 . ILE A 1 280 ? 153.955 106.273 99.654  1.00 50.35  ? 278 ILE A CG1 1 
ATOM   1656 C  CG2 . ILE A 1 280 ? 153.698 107.127 97.314  1.00 52.79  ? 278 ILE A CG2 1 
ATOM   1657 C  CD1 . ILE A 1 280 ? 152.461 106.300 99.888  1.00 52.32  ? 278 ILE A CD1 1 
ATOM   1658 N  N   . PHE A 1 281 ? 156.957 106.355 100.470 1.00 48.26  ? 279 PHE A N   1 
ATOM   1659 C  CA  . PHE A 1 281 ? 157.781 106.484 101.667 1.00 48.83  ? 279 PHE A CA  1 
ATOM   1660 C  C   . PHE A 1 281 ? 159.190 106.934 101.308 1.00 51.31  ? 279 PHE A C   1 
ATOM   1661 O  O   . PHE A 1 281 ? 159.800 107.729 102.030 1.00 51.72  ? 279 PHE A O   1 
ATOM   1662 C  CB  . PHE A 1 281 ? 157.816 105.159 102.425 1.00 50.97  ? 279 PHE A CB  1 
ATOM   1663 C  CG  . PHE A 1 281 ? 156.675 104.980 103.381 1.00 52.86  ? 279 PHE A CG  1 
ATOM   1664 C  CD1 . PHE A 1 281 ? 155.368 104.987 102.925 1.00 53.23  ? 279 PHE A CD1 1 
ATOM   1665 C  CD2 . PHE A 1 281 ? 156.907 104.807 104.733 1.00 52.54  ? 279 PHE A CD2 1 
ATOM   1666 C  CE1 . PHE A 1 281 ? 154.315 104.824 103.801 1.00 52.19  ? 279 PHE A CE1 1 
ATOM   1667 C  CE2 . PHE A 1 281 ? 155.856 104.643 105.614 1.00 52.07  ? 279 PHE A CE2 1 
ATOM   1668 C  CZ  . PHE A 1 281 ? 154.559 104.652 105.147 1.00 51.15  ? 279 PHE A CZ  1 
ATOM   1669 N  N   . ARG A 1 282 ? 159.727 106.426 100.198 1.00 50.90  ? 280 ARG A N   1 
ATOM   1670 C  CA  . ARG A 1 282 ? 160.999 106.931 99.697  1.00 46.98  ? 280 ARG A CA  1 
ATOM   1671 C  C   . ARG A 1 282 ? 160.875 108.388 99.267  1.00 50.58  ? 280 ARG A C   1 
ATOM   1672 O  O   . ARG A 1 282 ? 161.775 109.196 99.522  1.00 54.19  ? 280 ARG A O   1 
ATOM   1673 C  CB  . ARG A 1 282 ? 161.480 106.061 98.536  1.00 47.37  ? 280 ARG A CB  1 
ATOM   1674 C  CG  . ARG A 1 282 ? 162.643 106.650 97.748  1.00 53.78  ? 280 ARG A CG  1 
ATOM   1675 C  CD  . ARG A 1 282 ? 163.314 105.621 96.840  1.00 51.54  ? 280 ARG A CD  1 
ATOM   1676 N  NE  . ARG A 1 282 ? 163.562 104.348 97.511  1.00 54.69  ? 280 ARG A NE  1 
ATOM   1677 C  CZ  . ARG A 1 282 ? 162.835 103.248 97.353  1.00 56.75  ? 280 ARG A CZ  1 
ATOM   1678 N  NH1 . ARG A 1 282 ? 161.785 103.216 96.548  1.00 54.98  ? 280 ARG A NH1 1 
ATOM   1679 N  NH2 . ARG A 1 282 ? 163.170 102.150 98.024  1.00 55.80  ? 280 ARG A NH2 1 
ATOM   1680 N  N   . LYS A 1 283 ? 159.766 108.739 98.612  1.00 47.37  ? 281 LYS A N   1 
ATOM   1681 C  CA  . LYS A 1 283 ? 159.540 110.125 98.219  1.00 48.21  ? 281 LYS A CA  1 
ATOM   1682 C  C   . LYS A 1 283 ? 159.396 111.022 99.442  1.00 46.71  ? 281 LYS A C   1 
ATOM   1683 O  O   . LYS A 1 283 ? 159.898 112.152 99.456  1.00 52.34  ? 281 LYS A O   1 
ATOM   1684 C  CB  . LYS A 1 283 ? 158.297 110.208 97.328  1.00 50.03  ? 281 LYS A CB  1 
ATOM   1685 C  CG  . LYS A 1 283 ? 157.712 111.605 97.118  1.00 49.69  ? 281 LYS A CG  1 
ATOM   1686 C  CD  . LYS A 1 283 ? 156.221 111.623 97.412  1.00 48.88  ? 281 LYS A CD  1 
ATOM   1687 C  CE  . LYS A 1 283 ? 155.660 113.035 97.384  1.00 48.37  ? 281 LYS A CE  1 
ATOM   1688 N  NZ  . LYS A 1 283 ? 154.392 113.145 98.160  1.00 49.39  ? 281 LYS A NZ  1 
ATOM   1689 N  N   . LEU A 1 284 ? 158.711 110.540 100.474 1.00 42.57  ? 282 LEU A N   1 
ATOM   1690 C  CA  . LEU A 1 284 ? 158.491 111.296 101.697 1.00 39.57  ? 282 LEU A CA  1 
ATOM   1691 C  C   . LEU A 1 284 ? 159.560 111.037 102.749 1.00 40.24  ? 282 LEU A C   1 
ATOM   1692 O  O   . LEU A 1 284 ? 159.422 111.507 103.881 1.00 44.72  ? 282 LEU A O   1 
ATOM   1693 C  CB  . LEU A 1 284 ? 157.113 110.967 102.275 1.00 41.64  ? 282 LEU A CB  1 
ATOM   1694 C  CG  . LEU A 1 284 ? 155.911 111.500 101.495 1.00 42.35  ? 282 LEU A CG  1 
ATOM   1695 C  CD1 . LEU A 1 284 ? 154.619 110.998 102.113 1.00 43.06  ? 282 LEU A CD1 1 
ATOM   1696 C  CD2 . LEU A 1 284 ? 155.924 113.016 101.446 1.00 42.22  ? 282 LEU A CD2 1 
ATOM   1697 N  N   . GLY A 1 285 ? 160.614 110.297 102.406 1.00 41.93  ? 283 GLY A N   1 
ATOM   1698 C  CA  . GLY A 1 285 ? 161.634 109.982 103.393 1.00 40.25  ? 283 GLY A CA  1 
ATOM   1699 C  C   . GLY A 1 285 ? 162.318 111.217 103.945 1.00 43.66  ? 283 GLY A C   1 
ATOM   1700 O  O   . GLY A 1 285 ? 162.524 111.336 105.155 1.00 47.51  ? 283 GLY A O   1 
ATOM   1701 N  N   . LEU A 1 286 ? 162.680 112.155 103.068 1.00 45.43  ? 284 LEU A N   1 
ATOM   1702 C  CA  . LEU A 1 286 ? 163.363 113.359 103.526 1.00 38.29  ? 284 LEU A CA  1 
ATOM   1703 C  C   . LEU A 1 286 ? 162.415 114.296 104.261 1.00 39.58  ? 284 LEU A C   1 
ATOM   1704 O  O   . LEU A 1 286 ? 162.841 115.015 105.171 1.00 44.61  ? 284 LEU A O   1 
ATOM   1705 C  CB  . LEU A 1 286 ? 164.014 114.074 102.342 1.00 41.31  ? 284 LEU A CB  1 
ATOM   1706 C  CG  . LEU A 1 286 ? 165.392 114.689 102.601 1.00 42.00  ? 284 LEU A CG  1 
ATOM   1707 C  CD1 . LEU A 1 286 ? 166.402 113.629 103.001 1.00 38.65  ? 284 LEU A CD1 1 
ATOM   1708 C  CD2 . LEU A 1 286 ? 165.877 115.436 101.372 1.00 45.73  ? 284 LEU A CD2 1 
ATOM   1709 N  N   . TYR A 1 287 ? 161.136 114.310 103.884 1.00 37.21  ? 285 TYR A N   1 
ATOM   1710 C  CA  . TYR A 1 287 ? 160.160 115.096 104.630 1.00 35.33  ? 285 TYR A CA  1 
ATOM   1711 C  C   . TYR A 1 287 ? 160.000 114.564 106.049 1.00 39.48  ? 285 TYR A C   1 
ATOM   1712 O  O   . TYR A 1 287 ? 159.920 115.343 107.005 1.00 41.87  ? 285 TYR A O   1 
ATOM   1713 C  CB  . TYR A 1 287 ? 158.818 115.093 103.900 1.00 39.83  ? 285 TYR A CB  1 
ATOM   1714 C  CG  . TYR A 1 287 ? 157.638 115.403 104.790 1.00 42.76  ? 285 TYR A CG  1 
ATOM   1715 C  CD1 . TYR A 1 287 ? 157.491 116.654 105.368 1.00 38.75  ? 285 TYR A CD1 1 
ATOM   1716 C  CD2 . TYR A 1 287 ? 156.673 114.443 105.055 1.00 42.52  ? 285 TYR A CD2 1 
ATOM   1717 C  CE1 . TYR A 1 287 ? 156.418 116.942 106.181 1.00 40.37  ? 285 TYR A CE1 1 
ATOM   1718 C  CE2 . TYR A 1 287 ? 155.597 114.721 105.868 1.00 40.13  ? 285 TYR A CE2 1 
ATOM   1719 C  CZ  . TYR A 1 287 ? 155.475 115.972 106.430 1.00 39.91  ? 285 TYR A CZ  1 
ATOM   1720 O  OH  . TYR A 1 287 ? 154.405 116.259 107.243 1.00 42.46  ? 285 TYR A OH  1 
ATOM   1721 N  N   . MET A 1 288 ? 159.949 113.239 106.206 1.00 42.45  ? 286 MET A N   1 
ATOM   1722 C  CA  . MET A 1 288 ? 159.855 112.657 107.540 1.00 39.93  ? 286 MET A CA  1 
ATOM   1723 C  C   . MET A 1 288 ? 161.103 112.958 108.358 1.00 41.08  ? 286 MET A C   1 
ATOM   1724 O  O   . MET A 1 288 ? 161.017 113.219 109.563 1.00 43.94  ? 286 MET A O   1 
ATOM   1725 C  CB  . MET A 1 288 ? 159.639 111.149 107.444 1.00 39.13  ? 286 MET A CB  1 
ATOM   1726 C  CG  . MET A 1 288 ? 158.296 110.744 106.875 1.00 42.07  ? 286 MET A CG  1 
ATOM   1727 S  SD  . MET A 1 288 ? 158.049 108.961 106.912 1.00 58.75  ? 286 MET A SD  1 
ATOM   1728 C  CE  . MET A 1 288 ? 159.252 108.423 105.704 1.00 42.35  ? 286 MET A CE  1 
ATOM   1729 N  N   . ALA A 1 289 ? 162.274 112.916 107.722 1.00 37.91  ? 287 ALA A N   1 
ATOM   1730 C  CA  . ALA A 1 289 ? 163.508 113.233 108.430 1.00 39.20  ? 287 ALA A CA  1 
ATOM   1731 C  C   . ALA A 1 289 ? 163.485 114.661 108.958 1.00 40.86  ? 287 ALA A C   1 
ATOM   1732 O  O   . ALA A 1 289 ? 163.929 114.924 110.080 1.00 44.47  ? 287 ALA A O   1 
ATOM   1733 C  CB  . ALA A 1 289 ? 164.709 113.020 107.509 1.00 39.40  ? 287 ALA A CB  1 
ATOM   1734 N  N   . THR A 1 290 ? 162.974 115.600 108.159 1.00 38.88  ? 288 THR A N   1 
ATOM   1735 C  CA  . THR A 1 290 ? 162.901 116.988 108.604 1.00 37.71  ? 288 THR A CA  1 
ATOM   1736 C  C   . THR A 1 290 ? 161.984 117.137 109.811 1.00 34.67  ? 288 THR A C   1 
ATOM   1737 O  O   . THR A 1 290 ? 162.315 117.849 110.765 1.00 39.29  ? 288 THR A O   1 
ATOM   1738 C  CB  . THR A 1 290 ? 162.423 117.879 107.459 1.00 38.67  ? 288 THR A CB  1 
ATOM   1739 O  OG1 . THR A 1 290 ? 163.240 117.653 106.305 1.00 45.13  ? 288 THR A OG1 1 
ATOM   1740 C  CG2 . THR A 1 290 ? 162.503 119.344 107.849 1.00 40.40  ? 288 THR A CG2 1 
ATOM   1741 N  N   . VAL A 1 291 ? 160.821 116.485 109.786 1.00 32.84  ? 289 VAL A N   1 
ATOM   1742 C  CA  . VAL A 1 291 ? 159.913 116.565 110.925 1.00 34.53  ? 289 VAL A CA  1 
ATOM   1743 C  C   . VAL A 1 291 ? 160.480 115.801 112.113 1.00 38.45  ? 289 VAL A C   1 
ATOM   1744 O  O   . VAL A 1 291 ? 160.447 116.283 113.250 1.00 41.74  ? 289 VAL A O   1 
ATOM   1745 C  CB  . VAL A 1 291 ? 158.516 116.049 110.537 1.00 37.44  ? 289 VAL A CB  1 
ATOM   1746 C  CG1 . VAL A 1 291 ? 157.573 116.141 111.723 1.00 36.24  ? 289 VAL A CG1 1 
ATOM   1747 C  CG2 . VAL A 1 291 ? 157.967 116.833 109.365 1.00 42.22  ? 289 VAL A CG2 1 
ATOM   1748 N  N   . LEU A 1 292 ? 161.004 114.599 111.875 1.00 41.37  ? 290 LEU A N   1 
ATOM   1749 C  CA  . LEU A 1 292 ? 161.563 113.808 112.966 1.00 33.28  ? 290 LEU A CA  1 
ATOM   1750 C  C   . LEU A 1 292 ? 162.814 114.461 113.538 1.00 34.61  ? 290 LEU A C   1 
ATOM   1751 O  O   . LEU A 1 292 ? 163.046 114.407 114.750 1.00 39.99  ? 290 LEU A O   1 
ATOM   1752 C  CB  . LEU A 1 292 ? 161.868 112.392 112.481 1.00 41.28  ? 290 LEU A CB  1 
ATOM   1753 C  CG  . LEU A 1 292 ? 160.653 111.475 112.342 1.00 41.06  ? 290 LEU A CG  1 
ATOM   1754 C  CD1 . LEU A 1 292 ? 161.035 110.192 111.632 1.00 38.33  ? 290 LEU A CD1 1 
ATOM   1755 C  CD2 . LEU A 1 292 ? 160.050 111.173 113.700 1.00 38.16  ? 290 LEU A CD2 1 
ATOM   1756 N  N   . THR A 1 293 ? 163.639 115.069 112.683 1.00 37.89  ? 291 THR A N   1 
ATOM   1757 C  CA  . THR A 1 293 ? 164.793 115.812 113.178 1.00 37.61  ? 291 THR A CA  1 
ATOM   1758 C  C   . THR A 1 293 ? 164.356 116.988 114.041 1.00 39.71  ? 291 THR A C   1 
ATOM   1759 O  O   . THR A 1 293 ? 164.924 117.227 115.112 1.00 44.07  ? 291 THR A O   1 
ATOM   1760 C  CB  . THR A 1 293 ? 165.648 116.304 112.010 1.00 37.16  ? 291 THR A CB  1 
ATOM   1761 O  OG1 . THR A 1 293 ? 166.143 115.183 111.268 1.00 44.31  ? 291 THR A OG1 1 
ATOM   1762 C  CG2 . THR A 1 293 ? 166.819 117.129 112.512 1.00 35.05  ? 291 THR A CG2 1 
ATOM   1763 N  N   . GLY A 1 294 ? 163.349 117.736 113.590 1.00 34.67  ? 292 GLY A N   1 
ATOM   1764 C  CA  . GLY A 1 294 ? 162.877 118.867 114.369 1.00 34.79  ? 292 GLY A CA  1 
ATOM   1765 C  C   . GLY A 1 294 ? 162.239 118.448 115.678 1.00 34.73  ? 292 GLY A C   1 
ATOM   1766 O  O   . GLY A 1 294 ? 162.469 119.071 116.717 1.00 39.08  ? 292 GLY A O   1 
ATOM   1767 N  N   . LEU A 1 295 ? 161.428 117.389 115.649 1.00 30.87  ? 293 LEU A N   1 
ATOM   1768 C  CA  . LEU A 1 295 ? 160.822 116.894 116.881 1.00 35.19  ? 293 LEU A CA  1 
ATOM   1769 C  C   . LEU A 1 295 ? 161.885 116.408 117.856 1.00 32.41  ? 293 LEU A C   1 
ATOM   1770 O  O   . LEU A 1 295 ? 161.769 116.620 119.068 1.00 31.71  ? 293 LEU A O   1 
ATOM   1771 C  CB  . LEU A 1 295 ? 159.829 115.776 116.567 1.00 36.75  ? 293 LEU A CB  1 
ATOM   1772 C  CG  . LEU A 1 295 ? 158.571 116.177 115.792 1.00 34.73  ? 293 LEU A CG  1 
ATOM   1773 C  CD1 . LEU A 1 295 ? 157.736 114.951 115.478 1.00 37.75  ? 293 LEU A CD1 1 
ATOM   1774 C  CD2 . LEU A 1 295 ? 157.750 117.197 116.560 1.00 32.30  ? 293 LEU A CD2 1 
ATOM   1775 N  N   . ALA A 1 296 ? 162.925 115.744 117.348 1.00 37.06  ? 294 ALA A N   1 
ATOM   1776 C  CA  . ALA A 1 296 ? 164.008 115.291 118.213 1.00 36.58  ? 294 ALA A CA  1 
ATOM   1777 C  C   . ALA A 1 296 ? 164.766 116.464 118.820 1.00 38.00  ? 294 ALA A C   1 
ATOM   1778 O  O   . ALA A 1 296 ? 165.091 116.448 120.012 1.00 40.55  ? 294 ALA A O   1 
ATOM   1779 C  CB  . ALA A 1 296 ? 164.960 114.389 117.430 1.00 35.31  ? 294 ALA A CB  1 
ATOM   1780 N  N   . ILE A 1 297 ? 165.059 117.491 118.020 1.00 34.17  ? 295 ILE A N   1 
ATOM   1781 C  CA  . ILE A 1 297 ? 165.818 118.633 118.526 1.00 38.74  ? 295 ILE A CA  1 
ATOM   1782 C  C   . ILE A 1 297 ? 165.022 119.365 119.599 1.00 37.55  ? 295 ILE A C   1 
ATOM   1783 O  O   . ILE A 1 297 ? 165.546 119.699 120.668 1.00 42.25  ? 295 ILE A O   1 
ATOM   1784 C  CB  . ILE A 1 297 ? 166.205 119.575 117.371 1.00 43.73  ? 295 ILE A CB  1 
ATOM   1785 C  CG1 . ILE A 1 297 ? 167.357 118.977 116.563 1.00 38.95  ? 295 ILE A CG1 1 
ATOM   1786 C  CG2 . ILE A 1 297 ? 166.597 120.944 117.907 1.00 36.29  ? 295 ILE A CG2 1 
ATOM   1787 C  CD1 . ILE A 1 297 ? 167.545 119.615 115.207 1.00 34.57  ? 295 ILE A CD1 1 
ATOM   1788 N  N   . HIS A 1 298 ? 163.742 119.625 119.331 1.00 32.88  ? 296 HIS A N   1 
ATOM   1789 C  CA  . HIS A 1 298 ? 162.921 120.337 120.303 1.00 27.26  ? 296 HIS A CA  1 
ATOM   1790 C  C   . HIS A 1 298 ? 162.767 119.538 121.590 1.00 31.92  ? 296 HIS A C   1 
ATOM   1791 O  O   . HIS A 1 298 ? 162.816 120.100 122.689 1.00 36.46  ? 296 HIS A O   1 
ATOM   1792 C  CB  . HIS A 1 298 ? 161.551 120.649 119.705 1.00 35.04  ? 296 HIS A CB  1 
ATOM   1793 C  CG  . HIS A 1 298 ? 160.828 121.754 120.409 1.00 41.61  ? 296 HIS A CG  1 
ATOM   1794 N  ND1 . HIS A 1 298 ? 159.720 121.535 121.197 1.00 33.69  ? 296 HIS A ND1 1 
ATOM   1795 C  CD2 . HIS A 1 298 ? 161.062 123.086 120.451 1.00 36.73  ? 296 HIS A CD2 1 
ATOM   1796 C  CE1 . HIS A 1 298 ? 159.301 122.685 121.692 1.00 36.94  ? 296 HIS A CE1 1 
ATOM   1797 N  NE2 . HIS A 1 298 ? 160.097 123.642 121.254 1.00 33.76  ? 296 HIS A NE2 1 
ATOM   1798 N  N   . SER A 1 299 ? 162.577 118.226 121.473 1.00 37.18  ? 297 SER A N   1 
ATOM   1799 C  CA  . SER A 1 299 ? 162.316 117.402 122.646 1.00 35.79  ? 297 SER A CA  1 
ATOM   1800 C  C   . SER A 1 299 ? 163.578 117.140 123.457 1.00 35.98  ? 297 SER A C   1 
ATOM   1801 O  O   . SER A 1 299 ? 163.525 117.094 124.690 1.00 38.98  ? 297 SER A O   1 
ATOM   1802 C  CB  . SER A 1 299 ? 161.689 116.079 122.216 1.00 37.02  ? 297 SER A CB  1 
ATOM   1803 O  OG  . SER A 1 299 ? 160.537 116.304 121.428 1.00 44.55  ? 297 SER A OG  1 
ATOM   1804 N  N   . ILE A 1 300 ? 164.717 116.964 122.791 1.00 32.99  ? 298 ILE A N   1 
ATOM   1805 C  CA  . ILE A 1 300 ? 165.926 116.493 123.457 1.00 36.77  ? 298 ILE A CA  1 
ATOM   1806 C  C   . ILE A 1 300 ? 166.853 117.654 123.791 1.00 42.47  ? 298 ILE A C   1 
ATOM   1807 O  O   . ILE A 1 300 ? 167.663 117.559 124.718 1.00 48.02  ? 298 ILE A O   1 
ATOM   1808 C  CB  . ILE A 1 300 ? 166.656 115.448 122.593 1.00 40.24  ? 298 ILE A CB  1 
ATOM   1809 C  CG1 . ILE A 1 300 ? 165.749 114.243 122.336 1.00 40.25  ? 298 ILE A CG1 1 
ATOM   1810 C  CG2 . ILE A 1 300 ? 167.945 115.007 123.270 1.00 36.27  ? 298 ILE A CG2 1 
ATOM   1811 C  CD1 . ILE A 1 300 ? 166.246 113.323 121.246 1.00 40.10  ? 298 ILE A CD1 1 
ATOM   1812 N  N   . VAL A 1 301 ? 166.752 118.754 123.048 1.00 37.54  ? 299 VAL A N   1 
ATOM   1813 C  CA  . VAL A 1 301 ? 167.653 119.894 123.205 1.00 39.93  ? 299 VAL A CA  1 
ATOM   1814 C  C   . VAL A 1 301 ? 166.922 121.111 123.767 1.00 37.41  ? 299 VAL A C   1 
ATOM   1815 O  O   . VAL A 1 301 ? 167.237 121.582 124.859 1.00 40.20  ? 299 VAL A O   1 
ATOM   1816 C  CB  . VAL A 1 301 ? 168.361 120.233 121.874 1.00 40.84  ? 299 VAL A CB  1 
ATOM   1817 C  CG1 . VAL A 1 301 ? 169.376 121.339 122.084 1.00 34.11  ? 299 VAL A CG1 1 
ATOM   1818 C  CG2 . VAL A 1 301 ? 169.030 118.997 121.295 1.00 36.66  ? 299 VAL A CG2 1 
ATOM   1819 N  N   . ILE A 1 302 ? 165.933 121.625 123.038 1.00 37.71  ? 300 ILE A N   1 
ATOM   1820 C  CA  . ILE A 1 302 ? 165.354 122.922 123.382 1.00 35.94  ? 300 ILE A CA  1 
ATOM   1821 C  C   . ILE A 1 302 ? 164.568 122.834 124.685 1.00 38.64  ? 300 ILE A C   1 
ATOM   1822 O  O   . ILE A 1 302 ? 164.847 123.559 125.647 1.00 41.63  ? 300 ILE A O   1 
ATOM   1823 C  CB  . ILE A 1 302 ? 164.478 123.441 122.231 1.00 37.39  ? 300 ILE A CB  1 
ATOM   1824 C  CG1 . ILE A 1 302 ? 165.355 123.787 121.027 1.00 34.02  ? 300 ILE A CG1 1 
ATOM   1825 C  CG2 . ILE A 1 302 ? 163.676 124.654 122.678 1.00 38.45  ? 300 ILE A CG2 1 
ATOM   1826 C  CD1 . ILE A 1 302 ? 164.592 123.958 119.746 1.00 40.16  ? 300 ILE A CD1 1 
ATOM   1827 N  N   . LEU A 1 303 ? 163.569 121.955 124.734 1.00 34.49  ? 301 LEU A N   1 
ATOM   1828 C  CA  . LEU A 1 303 ? 162.726 121.876 125.925 1.00 31.92  ? 301 LEU A CA  1 
ATOM   1829 C  C   . LEU A 1 303 ? 163.524 121.531 127.174 1.00 34.11  ? 301 LEU A C   1 
ATOM   1830 O  O   . LEU A 1 303 ? 163.306 122.173 128.216 1.00 34.47  ? 301 LEU A O   1 
ATOM   1831 C  CB  . LEU A 1 303 ? 161.593 120.873 125.686 1.00 33.70  ? 301 LEU A CB  1 
ATOM   1832 C  CG  . LEU A 1 303 ? 160.412 121.379 124.856 1.00 34.51  ? 301 LEU A CG  1 
ATOM   1833 C  CD1 . LEU A 1 303 ? 159.440 120.247 124.575 1.00 36.05  ? 301 LEU A CD1 1 
ATOM   1834 C  CD2 . LEU A 1 303 ? 159.703 122.528 125.550 1.00 37.54  ? 301 LEU A CD2 1 
ATOM   1835 N  N   . PRO A 1 304 ? 164.430 120.550 127.161 1.00 35.98  ? 302 PRO A N   1 
ATOM   1836 C  CA  . PRO A 1 304 ? 165.296 120.357 128.335 1.00 33.85  ? 302 PRO A CA  1 
ATOM   1837 C  C   . PRO A 1 304 ? 166.124 121.580 128.690 1.00 41.03  ? 302 PRO A C   1 
ATOM   1838 O  O   . PRO A 1 304 ? 166.330 121.856 129.878 1.00 46.42  ? 302 PRO A O   1 
ATOM   1839 C  CB  . PRO A 1 304 ? 166.175 119.174 127.913 1.00 36.99  ? 302 PRO A CB  1 
ATOM   1840 C  CG  . PRO A 1 304 ? 165.334 118.412 126.970 1.00 36.88  ? 302 PRO A CG  1 
ATOM   1841 C  CD  . PRO A 1 304 ? 164.548 119.436 126.208 1.00 42.29  ? 302 PRO A CD  1 
ATOM   1842 N  N   . LEU A 1 305 ? 166.603 122.314 127.685 1.00 40.08  ? 303 LEU A N   1 
ATOM   1843 C  CA  . LEU A 1 305 ? 167.432 123.525 127.909 1.00 36.38  ? 303 LEU A CA  1 
ATOM   1844 C  C   . LEU A 1 305 ? 166.591 124.590 128.620 1.00 42.41  ? 303 LEU A C   1 
ATOM   1845 O  O   . LEU A 1 305 ? 167.132 125.228 129.533 1.00 48.08  ? 303 LEU A O   1 
ATOM   1846 C  CB  . LEU A 1 305 ? 167.960 124.036 126.567 1.00 40.61  ? 303 LEU A CB  1 
ATOM   1847 C  CG  . LEU A 1 305 ? 168.725 125.356 126.626 1.00 42.20  ? 303 LEU A CG  1 
ATOM   1848 C  CD1 . LEU A 1 305 ? 169.840 125.293 127.657 1.00 41.10  ? 303 LEU A CD1 1 
ATOM   1849 C  CD2 . LEU A 1 305 ? 169.283 125.715 125.260 1.00 41.14  ? 303 LEU A CD2 1 
ATOM   1850 N  N   . ILE A 1 306 ? 165.328 124.785 128.226 1.00 38.82  ? 304 ILE A N   1 
ATOM   1851 C  CA  . ILE A 1 306 ? 164.455 125.757 128.877 1.00 34.55  ? 304 ILE A CA  1 
ATOM   1852 C  C   . ILE A 1 306 ? 164.176 125.333 130.312 1.00 40.87  ? 304 ILE A C   1 
ATOM   1853 O  O   . ILE A 1 306 ? 164.192 126.158 131.233 1.00 43.93  ? 304 ILE A O   1 
ATOM   1854 C  CB  . ILE A 1 306 ? 163.153 125.932 128.074 1.00 39.70  ? 304 ILE A CB  1 
ATOM   1855 C  CG1 . ILE A 1 306 ? 163.446 126.551 126.707 1.00 39.76  ? 304 ILE A CG1 1 
ATOM   1856 C  CG2 . ILE A 1 306 ? 162.171 126.801 128.838 1.00 39.82  ? 304 ILE A CG2 1 
ATOM   1857 C  CD1 . ILE A 1 306 ? 162.394 126.253 125.666 1.00 37.48  ? 304 ILE A CD1 1 
ATOM   1858 N  N   . TYR A 1 307 ? 163.911 124.043 130.525 1.00 39.91  ? 305 TYR A N   1 
ATOM   1859 C  CA  . TYR A 1 307 ? 163.663 123.556 131.877 1.00 38.46  ? 305 TYR A CA  1 
ATOM   1860 C  C   . TYR A 1 307 ? 164.889 123.742 132.762 1.00 40.34  ? 305 TYR A C   1 
ATOM   1861 O  O   . TYR A 1 307 ? 164.770 124.159 133.919 1.00 46.80  ? 305 TYR A O   1 
ATOM   1862 C  CB  . TYR A 1 307 ? 163.249 122.084 131.833 1.00 37.91  ? 305 TYR A CB  1 
ATOM   1863 C  CG  . TYR A 1 307 ? 163.072 121.445 133.193 1.00 40.90  ? 305 TYR A CG  1 
ATOM   1864 C  CD1 . TYR A 1 307 ? 164.153 120.904 133.875 1.00 40.83  ? 305 TYR A CD1 1 
ATOM   1865 C  CD2 . TYR A 1 307 ? 161.823 121.384 133.795 1.00 44.87  ? 305 TYR A CD2 1 
ATOM   1866 C  CE1 . TYR A 1 307 ? 163.996 120.323 135.115 1.00 41.57  ? 305 TYR A CE1 1 
ATOM   1867 C  CE2 . TYR A 1 307 ? 161.657 120.805 135.035 1.00 42.46  ? 305 TYR A CE2 1 
ATOM   1868 C  CZ  . TYR A 1 307 ? 162.747 120.275 135.690 1.00 41.97  ? 305 TYR A CZ  1 
ATOM   1869 O  OH  . TYR A 1 307 ? 162.588 119.694 136.926 1.00 45.43  ? 305 TYR A OH  1 
ATOM   1870 N  N   . PHE A 1 308 ? 166.077 123.435 132.238 1.00 39.38  ? 306 PHE A N   1 
ATOM   1871 C  CA  . PHE A 1 308 ? 167.286 123.565 133.043 1.00 37.77  ? 306 PHE A CA  1 
ATOM   1872 C  C   . PHE A 1 308 ? 167.523 125.013 133.450 1.00 43.93  ? 306 PHE A C   1 
ATOM   1873 O  O   . PHE A 1 308 ? 167.882 125.293 134.599 1.00 47.58  ? 306 PHE A O   1 
ATOM   1874 C  CB  . PHE A 1 308 ? 168.492 123.030 132.274 1.00 40.69  ? 306 PHE A CB  1 
ATOM   1875 C  CG  . PHE A 1 308 ? 169.788 123.180 133.011 1.00 47.08  ? 306 PHE A CG  1 
ATOM   1876 C  CD1 . PHE A 1 308 ? 170.023 122.465 134.171 1.00 46.61  ? 306 PHE A CD1 1 
ATOM   1877 C  CD2 . PHE A 1 308 ? 170.766 124.042 132.553 1.00 44.97  ? 306 PHE A CD2 1 
ATOM   1878 C  CE1 . PHE A 1 308 ? 171.211 122.602 134.855 1.00 47.14  ? 306 PHE A CE1 1 
ATOM   1879 C  CE2 . PHE A 1 308 ? 171.957 124.183 133.234 1.00 43.70  ? 306 PHE A CE2 1 
ATOM   1880 C  CZ  . PHE A 1 308 ? 172.179 123.463 134.386 1.00 44.42  ? 306 PHE A CZ  1 
ATOM   1881 N  N   . ILE A 1 309 ? 167.331 125.947 132.518 1.00 46.36  ? 307 ILE A N   1 
ATOM   1882 C  CA  . ILE A 1 309 ? 167.584 127.356 132.808 1.00 44.12  ? 307 ILE A CA  1 
ATOM   1883 C  C   . ILE A 1 309 ? 166.636 127.853 133.893 1.00 45.52  ? 307 ILE A C   1 
ATOM   1884 O  O   . ILE A 1 309 ? 167.061 128.456 134.885 1.00 46.54  ? 307 ILE A O   1 
ATOM   1885 C  CB  . ILE A 1 309 ? 167.461 128.190 131.520 1.00 44.05  ? 307 ILE A CB  1 
ATOM   1886 C  CG1 . ILE A 1 309 ? 168.637 127.877 130.590 1.00 40.07  ? 307 ILE A CG1 1 
ATOM   1887 C  CG2 . ILE A 1 309 ? 167.389 129.683 131.846 1.00 47.13  ? 307 ILE A CG2 1 
ATOM   1888 C  CD1 . ILE A 1 309 ? 168.668 128.695 129.318 1.00 44.92  ? 307 ILE A CD1 1 
ATOM   1889 N  N   . VAL A 1 310 ? 165.336 127.609 133.720 1.00 38.92  ? 308 VAL A N   1 
ATOM   1890 C  CA  . VAL A 1 310 ? 164.359 128.067 134.703 1.00 42.94  ? 308 VAL A CA  1 
ATOM   1891 C  C   . VAL A 1 310 ? 164.474 127.256 135.988 1.00 46.07  ? 308 VAL A C   1 
ATOM   1892 O  O   . VAL A 1 310 ? 164.472 127.808 137.093 1.00 50.44  ? 308 VAL A O   1 
ATOM   1893 C  CB  . VAL A 1 310 ? 162.937 127.993 134.121 1.00 43.01  ? 308 VAL A CB  1 
ATOM   1894 C  CG1 . VAL A 1 310 ? 161.919 128.388 135.176 1.00 43.87  ? 308 VAL A CG1 1 
ATOM   1895 C  CG2 . VAL A 1 310 ? 162.817 128.879 132.894 1.00 43.30  ? 308 VAL A CG2 1 
ATOM   1896 N  N   . VAL A 1 311 ? 164.573 125.937 135.861 1.00 44.15  ? 309 VAL A N   1 
ATOM   1897 C  CA  . VAL A 1 311 ? 164.676 125.027 136.994 1.00 40.95  ? 309 VAL A CA  1 
ATOM   1898 C  C   . VAL A 1 311 ? 166.048 124.378 136.914 1.00 44.94  ? 309 VAL A C   1 
ATOM   1899 O  O   . VAL A 1 311 ? 166.309 123.581 136.004 1.00 49.67  ? 309 VAL A O   1 
ATOM   1900 C  CB  . VAL A 1 311 ? 163.566 123.968 136.983 1.00 42.02  ? 309 VAL A CB  1 
ATOM   1901 C  CG1 . VAL A 1 311 ? 163.469 123.282 138.332 1.00 45.91  ? 309 VAL A CG1 1 
ATOM   1902 C  CG2 . VAL A 1 311 ? 162.237 124.591 136.592 1.00 41.84  ? 309 VAL A CG2 1 
ATOM   1903 N  N   . ARG A 1 312 ? 166.923 124.699 137.864 1.00 40.90  ? 310 ARG A N   1 
ATOM   1904 C  CA  . ARG A 1 312 ? 168.289 124.178 137.849 1.00 45.31  ? 310 ARG A CA  1 
ATOM   1905 C  C   . ARG A 1 312 ? 168.304 122.726 138.334 1.00 47.64  ? 310 ARG A C   1 
ATOM   1906 O  O   . ARG A 1 312 ? 168.931 122.367 139.329 1.00 47.43  ? 310 ARG A O   1 
ATOM   1907 C  CB  . ARG A 1 312 ? 169.201 125.058 138.696 1.00 47.58  ? 310 ARG A CB  1 
ATOM   1908 C  CG  . ARG A 1 312 ? 169.205 126.541 138.319 1.00 47.70  ? 310 ARG A CG  1 
ATOM   1909 C  CD  . ARG A 1 312 ? 169.155 126.781 136.814 1.00 50.16  ? 310 ARG A CD  1 
ATOM   1910 N  NE  . ARG A 1 312 ? 169.977 127.915 136.412 1.00 49.31  ? 310 ARG A NE  1 
ATOM   1911 C  CZ  . ARG A 1 312 ? 171.291 127.868 136.241 1.00 51.05  ? 310 ARG A CZ  1 
ATOM   1912 N  NH1 . ARG A 1 312 ? 171.974 126.749 136.422 1.00 50.69  ? 310 ARG A NH1 1 
ATOM   1913 N  NH2 . ARG A 1 312 ? 171.938 128.972 135.879 1.00 47.56  ? 310 ARG A NH2 1 
ATOM   1914 N  N   . LYS A 1 313 ? 167.591 121.885 137.588 1.00 42.52  ? 311 LYS A N   1 
ATOM   1915 C  CA  . LYS A 1 313 ? 167.484 120.465 137.875 1.00 46.05  ? 311 LYS A CA  1 
ATOM   1916 C  C   . LYS A 1 313 ? 167.676 119.682 136.585 1.00 48.40  ? 311 LYS A C   1 
ATOM   1917 O  O   . LYS A 1 313 ? 167.465 120.199 135.486 1.00 53.29  ? 311 LYS A O   1 
ATOM   1918 C  CB  . LYS A 1 313 ? 166.129 120.117 138.505 1.00 46.04  ? 311 LYS A CB  1 
ATOM   1919 C  CG  . LYS A 1 313 ? 166.004 120.518 139.964 1.00 44.28  ? 311 LYS A CG  1 
ATOM   1920 C  CD  . LYS A 1 313 ? 164.560 120.475 140.439 1.00 45.62  ? 311 LYS A CD  1 
ATOM   1921 C  CE  . LYS A 1 313 ? 163.940 119.102 140.242 1.00 46.28  ? 311 LYS A CE  1 
ATOM   1922 N  NZ  . LYS A 1 313 ? 162.637 118.976 140.948 1.00 50.19  ? 311 LYS A NZ  1 
ATOM   1923 N  N   . ASN A 1 314 ? 168.085 118.425 136.731 1.00 44.38  ? 312 ASN A N   1 
ATOM   1924 C  CA  . ASN A 1 314 ? 168.306 117.558 135.581 1.00 40.83  ? 312 ASN A CA  1 
ATOM   1925 C  C   . ASN A 1 314 ? 167.020 117.442 134.771 1.00 44.13  ? 312 ASN A C   1 
ATOM   1926 O  O   . ASN A 1 314 ? 166.062 116.804 135.225 1.00 44.60  ? 312 ASN A O   1 
ATOM   1927 C  CB  . ASN A 1 314 ? 168.780 116.177 136.035 1.00 44.47  ? 312 ASN A CB  1 
ATOM   1928 C  CG  . ASN A 1 314 ? 169.219 115.302 134.878 1.00 48.73  ? 312 ASN A CG  1 
ATOM   1929 O  OD1 . ASN A 1 314 ? 169.272 115.747 133.733 1.00 47.17  ? 312 ASN A OD1 1 
ATOM   1930 N  ND2 . ASN A 1 314 ? 169.538 114.049 135.173 1.00 48.27  ? 312 ASN A ND2 1 
ATOM   1931 N  N   . PRO A 1 315 ? 166.944 118.046 133.582 1.00 43.46  ? 313 PRO A N   1 
ATOM   1932 C  CA  . PRO A 1 315 ? 165.708 117.929 132.793 1.00 39.38  ? 313 PRO A CA  1 
ATOM   1933 C  C   . PRO A 1 315 ? 165.389 116.505 132.392 1.00 42.80  ? 313 PRO A C   1 
ATOM   1934 O  O   . PRO A 1 315 ? 164.211 116.158 132.244 1.00 44.29  ? 313 PRO A O   1 
ATOM   1935 C  CB  . PRO A 1 315 ? 165.983 118.808 131.565 1.00 42.34  ? 313 PRO A CB  1 
ATOM   1936 C  CG  . PRO A 1 315 ? 167.193 119.604 131.896 1.00 47.04  ? 313 PRO A CG  1 
ATOM   1937 C  CD  . PRO A 1 315 ? 167.981 118.798 132.858 1.00 44.44  ? 313 PRO A CD  1 
ATOM   1938 N  N   . PHE A 1 316 ? 166.409 115.669 132.196 1.00 46.01  ? 314 PHE A N   1 
ATOM   1939 C  CA  . PHE A 1 316 ? 166.182 114.302 131.751 1.00 43.58  ? 314 PHE A CA  1 
ATOM   1940 C  C   . PHE A 1 316 ? 165.670 113.414 132.875 1.00 46.00  ? 314 PHE A C   1 
ATOM   1941 O  O   . PHE A 1 316 ? 164.965 112.436 132.610 1.00 51.66  ? 314 PHE A O   1 
ATOM   1942 C  CB  . PHE A 1 316 ? 167.471 113.739 131.156 1.00 42.43  ? 314 PHE A CB  1 
ATOM   1943 C  CG  . PHE A 1 316 ? 168.031 114.580 130.046 1.00 41.03  ? 314 PHE A CG  1 
ATOM   1944 C  CD1 . PHE A 1 316 ? 167.378 114.662 128.829 1.00 39.88  ? 314 PHE A CD1 1 
ATOM   1945 C  CD2 . PHE A 1 316 ? 169.196 115.301 130.224 1.00 43.17  ? 314 PHE A CD2 1 
ATOM   1946 C  CE1 . PHE A 1 316 ? 167.883 115.440 127.808 1.00 43.59  ? 314 PHE A CE1 1 
ATOM   1947 C  CE2 . PHE A 1 316 ? 169.705 116.079 129.206 1.00 46.74  ? 314 PHE A CE2 1 
ATOM   1948 C  CZ  . PHE A 1 316 ? 169.047 116.148 127.997 1.00 44.26  ? 314 PHE A CZ  1 
ATOM   1949 N  N   . ARG A 1 317 ? 166.006 113.730 134.127 1.00 43.46  ? 315 ARG A N   1 
ATOM   1950 C  CA  . ARG A 1 317 ? 165.367 113.048 135.246 1.00 41.66  ? 315 ARG A CA  1 
ATOM   1951 C  C   . ARG A 1 317 ? 163.880 113.374 135.299 1.00 43.11  ? 315 ARG A C   1 
ATOM   1952 O  O   . ARG A 1 317 ? 163.056 112.501 135.587 1.00 47.43  ? 315 ARG A O   1 
ATOM   1953 C  CB  . ARG A 1 317 ? 166.047 113.433 136.558 1.00 44.05  ? 315 ARG A CB  1 
ATOM   1954 C  CG  . ARG A 1 317 ? 165.264 113.025 137.795 1.00 43.22  ? 315 ARG A CG  1 
ATOM   1955 C  CD  . ARG A 1 317 ? 166.141 112.982 139.035 1.00 45.92  ? 315 ARG A CD  1 
ATOM   1956 N  NE  . ARG A 1 317 ? 167.063 111.852 139.021 1.00 50.65  ? 315 ARG A NE  1 
ATOM   1957 C  CZ  . ARG A 1 317 ? 168.344 111.919 138.678 1.00 50.15  ? 315 ARG A CZ  1 
ATOM   1958 N  NH1 . ARG A 1 317 ? 168.905 113.057 138.302 1.00 43.23  ? 315 ARG A NH1 1 
ATOM   1959 N  NH2 . ARG A 1 317 ? 169.082 110.813 138.713 1.00 47.35  ? 315 ARG A NH2 1 
ATOM   1960 N  N   . PHE A 1 318 ? 163.521 114.631 135.028 1.00 39.43  ? 316 PHE A N   1 
ATOM   1961 C  CA  . PHE A 1 318 ? 162.113 115.002 134.966 1.00 41.21  ? 316 PHE A CA  1 
ATOM   1962 C  C   . PHE A 1 318 ? 161.405 114.276 133.830 1.00 42.69  ? 316 PHE A C   1 
ATOM   1963 O  O   . PHE A 1 318 ? 160.254 113.850 133.977 1.00 44.89  ? 316 PHE A O   1 
ATOM   1964 C  CB  . PHE A 1 318 ? 161.980 116.515 134.799 1.00 42.87  ? 316 PHE A CB  1 
ATOM   1965 C  CG  . PHE A 1 318 ? 160.569 117.015 134.899 1.00 40.45  ? 316 PHE A CG  1 
ATOM   1966 C  CD1 . PHE A 1 318 ? 160.028 117.360 136.124 1.00 41.47  ? 316 PHE A CD1 1 
ATOM   1967 C  CD2 . PHE A 1 318 ? 159.783 117.140 133.769 1.00 41.75  ? 316 PHE A CD2 1 
ATOM   1968 C  CE1 . PHE A 1 318 ? 158.732 117.820 136.217 1.00 40.90  ? 316 PHE A CE1 1 
ATOM   1969 C  CE2 . PHE A 1 318 ? 158.487 117.596 133.859 1.00 40.35  ? 316 PHE A CE2 1 
ATOM   1970 C  CZ  . PHE A 1 318 ? 157.962 117.938 135.083 1.00 38.56  ? 316 PHE A CZ  1 
ATOM   1971 N  N   . ALA A 1 319 ? 162.075 114.132 132.686 1.00 45.15  ? 317 ALA A N   1 
ATOM   1972 C  CA  . ALA A 1 319 ? 161.473 113.435 131.556 1.00 43.95  ? 317 ALA A CA  1 
ATOM   1973 C  C   . ALA A 1 319 ? 161.273 111.955 131.851 1.00 43.70  ? 317 ALA A C   1 
ATOM   1974 O  O   . ALA A 1 319 ? 160.297 111.359 131.384 1.00 43.52  ? 317 ALA A O   1 
ATOM   1975 C  CB  . ALA A 1 319 ? 162.337 113.615 130.310 1.00 42.43  ? 317 ALA A CB  1 
ATOM   1976 N  N   . MET A 1 320 ? 162.184 111.346 132.613 1.00 42.41  ? 318 MET A N   1 
ATOM   1977 C  CA  . MET A 1 320 ? 162.033 109.937 132.961 1.00 42.03  ? 318 MET A CA  1 
ATOM   1978 C  C   . MET A 1 320 ? 160.776 109.709 133.787 1.00 46.20  ? 318 MET A C   1 
ATOM   1979 O  O   . MET A 1 320 ? 160.104 108.682 133.640 1.00 46.54  ? 318 MET A O   1 
ATOM   1980 C  CB  . MET A 1 320 ? 163.268 109.450 133.718 1.00 45.37  ? 318 MET A CB  1 
ATOM   1981 C  CG  . MET A 1 320 ? 164.501 109.284 132.847 1.00 49.94  ? 318 MET A CG  1 
ATOM   1982 S  SD  . MET A 1 320 ? 165.978 108.870 133.794 1.00 66.65  ? 318 MET A SD  1 
ATOM   1983 C  CE  . MET A 1 320 ? 167.243 109.685 132.821 1.00 47.06  ? 318 MET A CE  1 
ATOM   1984 N  N   . GLY A 1 321 ? 160.444 110.654 134.669 1.00 44.32  ? 319 GLY A N   1 
ATOM   1985 C  CA  . GLY A 1 321 ? 159.218 110.550 135.438 1.00 42.89  ? 319 GLY A CA  1 
ATOM   1986 C  C   . GLY A 1 321 ? 157.967 110.609 134.589 1.00 42.71  ? 319 GLY A C   1 
ATOM   1987 O  O   . GLY A 1 321 ? 156.904 110.167 135.035 1.00 45.09  ? 319 GLY A O   1 
ATOM   1988 N  N   . MET A 1 322 ? 158.069 111.145 133.375 1.00 41.91  ? 320 MET A N   1 
ATOM   1989 C  CA  . MET A 1 322 ? 156.952 111.223 132.447 1.00 40.99  ? 320 MET A CA  1 
ATOM   1990 C  C   . MET A 1 322 ? 156.976 110.104 131.415 1.00 41.69  ? 320 MET A C   1 
ATOM   1991 O  O   . MET A 1 322 ? 156.214 110.154 130.445 1.00 42.42  ? 320 MET A O   1 
ATOM   1992 C  CB  . MET A 1 322 ? 156.955 112.577 131.735 1.00 39.53  ? 320 MET A CB  1 
ATOM   1993 C  CG  . MET A 1 322 ? 157.063 113.775 132.664 1.00 42.45  ? 320 MET A CG  1 
ATOM   1994 S  SD  . MET A 1 322 ? 155.730 113.883 133.870 1.00 52.58  ? 320 MET A SD  1 
ATOM   1995 C  CE  . MET A 1 322 ? 154.290 113.832 132.810 1.00 36.55  ? 320 MET A CE  1 
ATOM   1996 N  N   . ALA A 1 323 ? 157.824 109.092 131.607 1.00 45.75  ? 321 ALA A N   1 
ATOM   1997 C  CA  . ALA A 1 323 ? 157.990 108.060 130.589 1.00 40.21  ? 321 ALA A CA  1 
ATOM   1998 C  C   . ALA A 1 323 ? 156.669 107.371 130.275 1.00 42.20  ? 321 ALA A C   1 
ATOM   1999 O  O   . ALA A 1 323 ? 156.359 107.111 129.108 1.00 47.63  ? 321 ALA A O   1 
ATOM   2000 C  CB  . ALA A 1 323 ? 159.030 107.040 131.046 1.00 36.78  ? 321 ALA A CB  1 
ATOM   2001 N  N   . GLN A 1 324 ? 155.876 107.062 131.303 1.00 43.64  ? 322 GLN A N   1 
ATOM   2002 C  CA  . GLN A 1 324 ? 154.587 106.423 131.063 1.00 38.88  ? 322 GLN A CA  1 
ATOM   2003 C  C   . GLN A 1 324 ? 153.669 107.327 130.253 1.00 41.23  ? 322 GLN A C   1 
ATOM   2004 O  O   . GLN A 1 324 ? 152.959 106.859 129.356 1.00 43.34  ? 322 GLN A O   1 
ATOM   2005 C  CB  . GLN A 1 324 ? 153.933 106.042 132.390 1.00 42.64  ? 322 GLN A CB  1 
ATOM   2006 C  CG  . GLN A 1 324 ? 154.052 104.567 132.736 1.00 44.33  ? 322 GLN A CG  1 
ATOM   2007 C  CD  . GLN A 1 324 ? 154.241 104.328 134.219 1.00 49.26  ? 322 GLN A CD  1 
ATOM   2008 O  OE1 . GLN A 1 324 ? 153.637 105.005 135.051 1.00 48.49  ? 322 GLN A OE1 1 
ATOM   2009 N  NE2 . GLN A 1 324 ? 155.082 103.360 134.560 1.00 50.37  ? 322 GLN A NE2 1 
ATOM   2010 N  N   . ALA A 1 325 ? 153.660 108.626 130.559 1.00 40.18  ? 323 ALA A N   1 
ATOM   2011 C  CA  . ALA A 1 325 ? 152.851 109.559 129.783 1.00 34.58  ? 323 ALA A CA  1 
ATOM   2012 C  C   . ALA A 1 325 ? 153.403 109.726 128.374 1.00 36.45  ? 323 ALA A C   1 
ATOM   2013 O  O   . ALA A 1 325 ? 152.642 109.729 127.400 1.00 37.76  ? 323 ALA A O   1 
ATOM   2014 C  CB  . ALA A 1 325 ? 152.782 110.909 130.495 1.00 37.60  ? 323 ALA A CB  1 
ATOM   2015 N  N   . LEU A 1 326 ? 154.723 109.872 128.244 1.00 38.14  ? 324 LEU A N   1 
ATOM   2016 C  CA  . LEU A 1 326 ? 155.323 109.986 126.920 1.00 38.08  ? 324 LEU A CA  1 
ATOM   2017 C  C   . LEU A 1 326 ? 155.115 108.713 126.114 1.00 33.32  ? 324 LEU A C   1 
ATOM   2018 O  O   . LEU A 1 326 ? 154.806 108.769 124.919 1.00 38.57  ? 324 LEU A O   1 
ATOM   2019 C  CB  . LEU A 1 326 ? 156.815 110.301 127.042 1.00 40.34  ? 324 LEU A CB  1 
ATOM   2020 C  CG  . LEU A 1 326 ? 157.186 111.599 127.759 1.00 41.98  ? 324 LEU A CG  1 
ATOM   2021 C  CD1 . LEU A 1 326 ? 158.694 111.729 127.869 1.00 35.11  ? 324 LEU A CD1 1 
ATOM   2022 C  CD2 . LEU A 1 326 ? 156.593 112.797 127.041 1.00 41.33  ? 324 LEU A CD2 1 
ATOM   2023 N  N   . LEU A 1 327 ? 155.289 107.554 126.749 1.00 41.03  ? 325 LEU A N   1 
ATOM   2024 C  CA  . LEU A 1 327 ? 155.078 106.292 126.049 1.00 36.01  ? 325 LEU A CA  1 
ATOM   2025 C  C   . LEU A 1 327 ? 153.609 106.102 125.699 1.00 36.39  ? 325 LEU A C   1 
ATOM   2026 O  O   . LEU A 1 327 ? 153.282 105.600 124.618 1.00 41.10  ? 325 LEU A O   1 
ATOM   2027 C  CB  . LEU A 1 327 ? 155.590 105.133 126.904 1.00 39.53  ? 325 LEU A CB  1 
ATOM   2028 C  CG  . LEU A 1 327 ? 155.373 103.721 126.361 1.00 43.24  ? 325 LEU A CG  1 
ATOM   2029 C  CD1 . LEU A 1 327 ? 156.032 103.555 125.003 1.00 42.82  ? 325 LEU A CD1 1 
ATOM   2030 C  CD2 . LEU A 1 327 ? 155.916 102.696 127.342 1.00 41.97  ? 325 LEU A CD2 1 
ATOM   2031 N  N   . THR A 1 328 ? 152.709 106.497 126.600 1.00 37.37  ? 326 THR A N   1 
ATOM   2032 C  CA  . THR A 1 328 ? 151.283 106.438 126.300 1.00 32.50  ? 326 THR A CA  1 
ATOM   2033 C  C   . THR A 1 328 ? 150.934 107.328 125.115 1.00 37.87  ? 326 THR A C   1 
ATOM   2034 O  O   . THR A 1 328 ? 150.150 106.936 124.244 1.00 42.82  ? 326 THR A O   1 
ATOM   2035 C  CB  . THR A 1 328 ? 150.473 106.852 127.527 1.00 36.27  ? 326 THR A CB  1 
ATOM   2036 O  OG1 . THR A 1 328 ? 150.765 105.969 128.616 1.00 40.64  ? 326 THR A OG1 1 
ATOM   2037 C  CG2 . THR A 1 328 ? 148.983 106.817 127.227 1.00 37.00  ? 326 THR A CG2 1 
ATOM   2038 N  N   . ALA A 1 329 ? 151.499 108.536 125.071 1.00 41.91  ? 327 ALA A N   1 
ATOM   2039 C  CA  . ALA A 1 329 ? 151.211 109.451 123.973 1.00 34.13  ? 327 ALA A CA  1 
ATOM   2040 C  C   . ALA A 1 329 ? 151.767 108.941 122.650 1.00 36.16  ? 327 ALA A C   1 
ATOM   2041 O  O   . ALA A 1 329 ? 151.191 109.214 121.592 1.00 36.71  ? 327 ALA A O   1 
ATOM   2042 C  CB  . ALA A 1 329 ? 151.781 110.833 124.286 1.00 35.77  ? 327 ALA A CB  1 
ATOM   2043 N  N   . LEU A 1 330 ? 152.878 108.206 122.687 1.00 38.86  ? 328 LEU A N   1 
ATOM   2044 C  CA  . LEU A 1 330 ? 153.495 107.700 121.469 1.00 35.47  ? 328 LEU A CA  1 
ATOM   2045 C  C   . LEU A 1 330 ? 152.719 106.551 120.842 1.00 37.45  ? 328 LEU A C   1 
ATOM   2046 O  O   . LEU A 1 330 ? 153.066 106.129 119.737 1.00 45.80  ? 328 LEU A O   1 
ATOM   2047 C  CB  . LEU A 1 330 ? 154.927 107.252 121.761 1.00 36.24  ? 328 LEU A CB  1 
ATOM   2048 C  CG  . LEU A 1 330 ? 155.841 107.114 120.542 1.00 34.50  ? 328 LEU A CG  1 
ATOM   2049 C  CD1 . LEU A 1 330 ? 156.207 108.477 119.989 1.00 38.04  ? 328 LEU A CD1 1 
ATOM   2050 C  CD2 . LEU A 1 330 ? 157.088 106.332 120.907 1.00 37.21  ? 328 LEU A CD2 1 
ATOM   2051 N  N   . MET A 1 331 ? 151.702 106.024 121.517 1.00 35.70  ? 329 MET A N   1 
ATOM   2052 C  CA  . MET A 1 331 ? 150.867 104.958 120.979 1.00 35.20  ? 329 MET A CA  1 
ATOM   2053 C  C   . MET A 1 331 ? 149.466 105.426 120.618 1.00 34.46  ? 329 MET A C   1 
ATOM   2054 O  O   . MET A 1 331 ? 149.000 105.169 119.505 1.00 35.20  ? 329 MET A O   1 
ATOM   2055 C  CB  . MET A 1 331 ? 150.779 103.792 121.975 1.00 38.60  ? 329 MET A CB  1 
ATOM   2056 C  CG  . MET A 1 331 ? 152.072 103.444 122.696 1.00 40.03  ? 329 MET A CG  1 
ATOM   2057 S  SD  . MET A 1 331 ? 153.021 102.222 121.776 1.00 48.33  ? 329 MET A SD  1 
ATOM   2058 C  CE  . MET A 1 331 ? 154.597 103.050 121.622 1.00 37.82  ? 329 MET A CE  1 
ATOM   2059 N  N   . ILE A 1 332 ? 148.774 106.109 121.531 1.00 37.11  ? 330 ILE A N   1 
ATOM   2060 C  CA  . ILE A 1 332 ? 147.400 106.511 121.257 1.00 37.31  ? 330 ILE A CA  1 
ATOM   2061 C  C   . ILE A 1 332 ? 147.328 107.801 120.450 1.00 38.12  ? 330 ILE A C   1 
ATOM   2062 O  O   . ILE A 1 332 ? 146.289 108.081 119.843 1.00 42.78  ? 330 ILE A O   1 
ATOM   2063 C  CB  . ILE A 1 332 ? 146.606 106.647 122.567 1.00 32.52  ? 330 ILE A CB  1 
ATOM   2064 C  CG1 . ILE A 1 332 ? 147.019 107.902 123.335 1.00 35.53  ? 330 ILE A CG1 1 
ATOM   2065 C  CG2 . ILE A 1 332 ? 146.808 105.416 123.427 1.00 33.41  ? 330 ILE A CG2 1 
ATOM   2066 C  CD1 . ILE A 1 332 ? 146.437 107.978 124.725 1.00 36.17  ? 330 ILE A CD1 1 
ATOM   2067 N  N   . SER A 1 333 ? 148.405 108.588 120.419 1.00 32.67  ? 331 SER A N   1 
ATOM   2068 C  CA  . SER A 1 333 ? 148.481 109.797 119.597 1.00 27.41  ? 331 SER A CA  1 
ATOM   2069 C  C   . SER A 1 333 ? 147.405 110.811 119.980 1.00 31.39  ? 331 SER A C   1 
ATOM   2070 O  O   . SER A 1 333 ? 146.850 111.503 119.127 1.00 31.48  ? 331 SER A O   1 
ATOM   2071 C  CB  . SER A 1 333 ? 148.383 109.456 118.109 1.00 35.36  ? 331 SER A CB  1 
ATOM   2072 O  OG  . SER A 1 333 ? 149.566 108.834 117.651 1.00 42.79  ? 331 SER A OG  1 
ATOM   2073 N  N   . SER A 1 334 ? 147.114 110.913 121.273 1.00 29.84  ? 332 SER A N   1 
ATOM   2074 C  CA  . SER A 1 334 ? 146.120 111.858 121.766 1.00 30.79  ? 332 SER A CA  1 
ATOM   2075 C  C   . SER A 1 334 ? 146.634 112.479 123.055 1.00 32.27  ? 332 SER A C   1 
ATOM   2076 O  O   . SER A 1 334 ? 146.851 111.769 124.041 1.00 39.34  ? 332 SER A O   1 
ATOM   2077 C  CB  . SER A 1 334 ? 144.773 111.167 121.993 1.00 35.24  ? 332 SER A CB  1 
ATOM   2078 O  OG  . SER A 1 334 ? 143.896 111.981 122.746 1.00 42.15  ? 332 SER A OG  1 
ATOM   2079 N  N   . SER A 1 335 ? 146.838 113.799 123.043 1.00 24.77  ? 333 SER A N   1 
ATOM   2080 C  CA  . SER A 1 335 ? 147.275 114.489 124.253 1.00 31.53  ? 333 SER A CA  1 
ATOM   2081 C  C   . SER A 1 335 ? 146.172 114.516 125.301 1.00 35.17  ? 333 SER A C   1 
ATOM   2082 O  O   . SER A 1 335 ? 146.449 114.450 126.504 1.00 38.24  ? 333 SER A O   1 
ATOM   2083 C  CB  . SER A 1 335 ? 147.723 115.912 123.920 1.00 36.90  ? 333 SER A CB  1 
ATOM   2084 O  OG  . SER A 1 335 ? 148.626 115.929 122.832 1.00 40.62  ? 333 SER A OG  1 
ATOM   2085 N  N   . SER A 1 336 ? 144.916 114.629 124.865 1.00 36.51  ? 334 SER A N   1 
ATOM   2086 C  CA  . SER A 1 336 ? 143.804 114.642 125.808 1.00 30.98  ? 334 SER A CA  1 
ATOM   2087 C  C   . SER A 1 336 ? 143.554 113.256 126.390 1.00 34.43  ? 334 SER A C   1 
ATOM   2088 O  O   . SER A 1 336 ? 143.217 113.125 127.572 1.00 41.08  ? 334 SER A O   1 
ATOM   2089 C  CB  . SER A 1 336 ? 142.548 115.171 125.120 1.00 36.01  ? 334 SER A CB  1 
ATOM   2090 O  OG  . SER A 1 336 ? 142.733 116.508 124.690 1.00 37.98  ? 334 SER A OG  1 
ATOM   2091 N  N   . ALA A 1 337 ? 143.712 112.210 125.577 1.00 33.87  ? 335 ALA A N   1 
ATOM   2092 C  CA  . ALA A 1 337 ? 143.508 110.852 126.070 1.00 32.16  ? 335 ALA A CA  1 
ATOM   2093 C  C   . ALA A 1 337 ? 144.580 110.448 127.072 1.00 35.35  ? 335 ALA A C   1 
ATOM   2094 O  O   . ALA A 1 337 ? 144.291 109.711 128.021 1.00 37.11  ? 335 ALA A O   1 
ATOM   2095 C  CB  . ALA A 1 337 ? 143.484 109.868 124.904 1.00 32.74  ? 335 ALA A CB  1 
ATOM   2096 N  N   . THR A 1 338 ? 145.813 110.906 126.881 1.00 33.31  ? 336 THR A N   1 
ATOM   2097 C  CA  . THR A 1 338 ? 146.905 110.597 127.795 1.00 39.10  ? 336 THR A CA  1 
ATOM   2098 C  C   . THR A 1 338 ? 146.971 111.548 128.981 1.00 38.99  ? 336 THR A C   1 
ATOM   2099 O  O   . THR A 1 338 ? 147.859 111.397 129.824 1.00 38.14  ? 336 THR A O   1 
ATOM   2100 C  CB  . THR A 1 338 ? 148.248 110.622 127.054 1.00 37.31  ? 336 THR A CB  1 
ATOM   2101 O  OG1 . THR A 1 338 ? 149.294 110.219 127.945 1.00 41.64  ? 336 THR A OG1 1 
ATOM   2102 C  CG2 . THR A 1 338 ? 148.558 112.005 126.537 1.00 36.90  ? 336 THR A CG2 1 
ATOM   2103 N  N   . LEU A 1 339 ? 146.058 112.513 129.068 1.00 37.24  ? 337 LEU A N   1 
ATOM   2104 C  CA  . LEU A 1 339 ? 146.108 113.476 130.163 1.00 35.07  ? 337 LEU A CA  1 
ATOM   2105 C  C   . LEU A 1 339 ? 146.086 112.817 131.536 1.00 34.31  ? 337 LEU A C   1 
ATOM   2106 O  O   . LEU A 1 339 ? 146.856 113.254 132.408 1.00 39.84  ? 337 LEU A O   1 
ATOM   2107 C  CB  . LEU A 1 339 ? 144.952 114.473 130.019 1.00 34.82  ? 337 LEU A CB  1 
ATOM   2108 C  CG  . LEU A 1 339 ? 145.054 115.764 130.833 1.00 38.85  ? 337 LEU A CG  1 
ATOM   2109 C  CD1 . LEU A 1 339 ? 146.322 116.527 130.498 1.00 40.89  ? 337 LEU A CD1 1 
ATOM   2110 C  CD2 . LEU A 1 339 ? 143.833 116.630 130.593 1.00 35.36  ? 337 LEU A CD2 1 
ATOM   2111 N  N   . PRO A 1 340 ? 145.258 111.804 131.806 1.00 34.10  ? 338 PRO A N   1 
ATOM   2112 C  CA  . PRO A 1 340 ? 145.304 111.173 133.134 1.00 32.75  ? 338 PRO A CA  1 
ATOM   2113 C  C   . PRO A 1 340 ? 146.666 110.603 133.479 1.00 40.83  ? 338 PRO A C   1 
ATOM   2114 O  O   . PRO A 1 340 ? 147.063 110.634 134.649 1.00 40.35  ? 338 PRO A O   1 
ATOM   2115 C  CB  . PRO A 1 340 ? 144.239 110.073 133.036 1.00 33.32  ? 338 PRO A CB  1 
ATOM   2116 C  CG  . PRO A 1 340 ? 143.357 110.486 131.920 1.00 36.98  ? 338 PRO A CG  1 
ATOM   2117 C  CD  . PRO A 1 340 ? 144.228 111.198 130.948 1.00 38.29  ? 338 PRO A CD  1 
ATOM   2118 N  N   . VAL A 1 341 ? 147.393 110.072 132.494 1.00 43.61  ? 339 VAL A N   1 
ATOM   2119 C  CA  . VAL A 1 341 ? 148.732 109.558 132.756 1.00 38.88  ? 339 VAL A CA  1 
ATOM   2120 C  C   . VAL A 1 341 ? 149.694 110.703 133.038 1.00 42.73  ? 339 VAL A C   1 
ATOM   2121 O  O   . VAL A 1 341 ? 150.576 110.593 133.898 1.00 47.42  ? 339 VAL A O   1 
ATOM   2122 C  CB  . VAL A 1 341 ? 149.212 108.692 131.578 1.00 39.39  ? 339 VAL A CB  1 
ATOM   2123 C  CG1 . VAL A 1 341 ? 150.492 107.966 131.945 1.00 38.83  ? 339 VAL A CG1 1 
ATOM   2124 C  CG2 . VAL A 1 341 ? 148.134 107.701 131.175 1.00 41.83  ? 339 VAL A CG2 1 
ATOM   2125 N  N   . THR A 1 342 ? 149.549 111.817 132.317 1.00 39.21  ? 340 THR A N   1 
ATOM   2126 C  CA  . THR A 1 342 ? 150.399 112.975 132.570 1.00 35.51  ? 340 THR A CA  1 
ATOM   2127 C  C   . THR A 1 342 ? 150.205 113.494 133.988 1.00 39.63  ? 340 THR A C   1 
ATOM   2128 O  O   . THR A 1 342 ? 151.174 113.858 134.662 1.00 41.80  ? 340 THR A O   1 
ATOM   2129 C  CB  . THR A 1 342 ? 150.102 114.076 131.552 1.00 38.52  ? 340 THR A CB  1 
ATOM   2130 O  OG1 . THR A 1 342 ? 149.813 113.489 130.279 1.00 39.81  ? 340 THR A OG1 1 
ATOM   2131 C  CG2 . THR A 1 342 ? 151.291 115.012 131.412 1.00 41.51  ? 340 THR A CG2 1 
ATOM   2132 N  N   . PHE A 1 343 ? 148.957 113.539 134.457 1.00 42.40  ? 341 PHE A N   1 
ATOM   2133 C  CA  . PHE A 1 343 ? 148.694 113.947 135.833 1.00 38.39  ? 341 PHE A CA  1 
ATOM   2134 C  C   . PHE A 1 343 ? 149.405 113.030 136.816 1.00 41.98  ? 341 PHE A C   1 
ATOM   2135 O  O   . PHE A 1 343 ? 150.110 113.492 137.720 1.00 43.89  ? 341 PHE A O   1 
ATOM   2136 C  CB  . PHE A 1 343 ? 147.192 113.938 136.100 1.00 36.72  ? 341 PHE A CB  1 
ATOM   2137 C  CG  . PHE A 1 343 ? 146.512 115.228 135.777 1.00 36.85  ? 341 PHE A CG  1 
ATOM   2138 C  CD1 . PHE A 1 343 ? 146.701 116.340 136.573 1.00 40.91  ? 341 PHE A CD1 1 
ATOM   2139 C  CD2 . PHE A 1 343 ? 145.674 115.327 134.684 1.00 35.93  ? 341 PHE A CD2 1 
ATOM   2140 C  CE1 . PHE A 1 343 ? 146.073 117.525 136.281 1.00 41.22  ? 341 PHE A CE1 1 
ATOM   2141 C  CE2 . PHE A 1 343 ? 145.044 116.512 134.390 1.00 37.65  ? 341 PHE A CE2 1 
ATOM   2142 C  CZ  . PHE A 1 343 ? 145.242 117.611 135.191 1.00 42.53  ? 341 PHE A CZ  1 
ATOM   2143 N  N   . ARG A 1 344 ? 149.228 111.719 136.651 1.00 40.54  ? 342 ARG A N   1 
ATOM   2144 C  CA  . ARG A 1 344 ? 149.849 110.766 137.562 1.00 39.26  ? 342 ARG A CA  1 
ATOM   2145 C  C   . ARG A 1 344 ? 151.365 110.892 137.533 1.00 43.01  ? 342 ARG A C   1 
ATOM   2146 O  O   . ARG A 1 344 ? 152.018 110.878 138.582 1.00 47.79  ? 342 ARG A O   1 
ATOM   2147 C  CB  . ARG A 1 344 ? 149.415 109.348 137.187 1.00 45.55  ? 342 ARG A CB  1 
ATOM   2148 C  CG  . ARG A 1 344 ? 150.008 108.237 138.040 1.00 43.60  ? 342 ARG A CG  1 
ATOM   2149 C  CD  . ARG A 1 344 ? 150.425 107.058 137.177 1.00 47.61  ? 342 ARG A CD  1 
ATOM   2150 N  NE  . ARG A 1 344 ? 149.357 106.633 136.280 1.00 48.28  ? 342 ARG A NE  1 
ATOM   2151 C  CZ  . ARG A 1 344 ? 149.543 105.966 135.149 1.00 49.30  ? 342 ARG A CZ  1 
ATOM   2152 N  NH1 . ARG A 1 344 ? 150.752 105.613 134.744 1.00 45.84  ? 342 ARG A NH1 1 
ATOM   2153 N  NH2 . ARG A 1 344 ? 148.489 105.643 134.405 1.00 47.81  ? 342 ARG A NH2 1 
ATOM   2154 N  N   . CYS A 1 345 ? 151.944 111.020 136.340 1.00 43.52  ? 343 CYS A N   1 
ATOM   2155 C  CA  . CYS A 1 345 ? 153.393 111.129 136.230 1.00 41.84  ? 343 CYS A CA  1 
ATOM   2156 C  C   . CYS A 1 345 ? 153.894 112.436 136.831 1.00 41.90  ? 343 CYS A C   1 
ATOM   2157 O  O   . CYS A 1 345 ? 154.849 112.447 137.616 1.00 49.08  ? 343 CYS A O   1 
ATOM   2158 C  CB  . CYS A 1 345 ? 153.808 111.015 134.764 1.00 40.11  ? 343 CYS A CB  1 
ATOM   2159 S  SG  . CYS A 1 345 ? 153.592 109.371 134.056 1.00 56.29  ? 343 CYS A SG  1 
ATOM   2160 N  N   . ALA A 1 346 ? 153.260 113.554 136.474 1.00 38.08  ? 344 ALA A N   1 
ATOM   2161 C  CA  . ALA A 1 346 ? 153.730 114.849 136.950 1.00 41.11  ? 344 ALA A CA  1 
ATOM   2162 C  C   . ALA A 1 346 ? 153.545 114.993 138.456 1.00 46.16  ? 344 ALA A C   1 
ATOM   2163 O  O   . ALA A 1 346 ? 154.441 115.481 139.152 1.00 43.65  ? 344 ALA A O   1 
ATOM   2164 C  CB  . ALA A 1 346 ? 152.999 115.969 136.213 1.00 40.49  ? 344 ALA A CB  1 
ATOM   2165 N  N   . GLU A 1 347 ? 152.390 114.576 138.977 1.00 49.27  ? 345 GLU A N   1 
ATOM   2166 C  CA  . GLU A 1 347 ? 152.075 114.820 140.380 1.00 45.68  ? 345 GLU A CA  1 
ATOM   2167 C  C   . GLU A 1 347 ? 152.810 113.862 141.312 1.00 47.77  ? 345 GLU A C   1 
ATOM   2168 O  O   . GLU A 1 347 ? 153.214 114.258 142.411 1.00 47.05  ? 345 GLU A O   1 
ATOM   2169 C  CB  . GLU A 1 347 ? 150.567 114.717 140.598 1.00 45.05  ? 345 GLU A CB  1 
ATOM   2170 C  CG  . GLU A 1 347 ? 149.795 115.926 140.097 1.00 44.86  ? 345 GLU A CG  1 
ATOM   2171 C  CD  . GLU A 1 347 ? 148.303 115.676 140.008 1.00 50.20  ? 345 GLU A CD  1 
ATOM   2172 O  OE1 . GLU A 1 347 ? 147.871 114.529 140.249 1.00 53.44  ? 345 GLU A OE1 1 
ATOM   2173 O  OE2 . GLU A 1 347 ? 147.560 116.628 139.692 1.00 50.82  ? 345 GLU A OE2 1 
ATOM   2174 N  N   . GLU A 1 348 ? 152.990 112.605 140.906 1.00 45.78  ? 346 GLU A N   1 
ATOM   2175 C  CA  . GLU A 1 348 ? 153.581 111.592 141.775 1.00 46.93  ? 346 GLU A CA  1 
ATOM   2176 C  C   . GLU A 1 348 ? 155.063 111.374 141.484 1.00 49.17  ? 346 GLU A C   1 
ATOM   2177 O  O   . GLU A 1 348 ? 155.901 111.515 142.378 1.00 47.07  ? 346 GLU A O   1 
ATOM   2178 C  CB  . GLU A 1 348 ? 152.813 110.271 141.637 1.00 44.86  ? 346 GLU A CB  1 
ATOM   2179 C  CG  . GLU A 1 348 ? 151.593 110.170 142.539 1.00 51.49  ? 346 GLU A CG  1 
ATOM   2180 C  CD  . GLU A 1 348 ? 150.333 109.802 141.781 1.00 54.05  ? 346 GLU A CD  1 
ATOM   2181 O  OE1 . GLU A 1 348 ? 150.395 108.899 140.921 1.00 53.52  ? 346 GLU A OE1 1 
ATOM   2182 O  OE2 . GLU A 1 348 ? 149.279 110.418 142.045 1.00 53.62  ? 346 GLU A OE2 1 
ATOM   2183 N  N   . ASN A 1 349 ? 155.402 111.022 140.243 1.00 46.81  ? 347 ASN A N   1 
ATOM   2184 C  CA  . ASN A 1 349 ? 156.797 110.748 139.915 1.00 41.27  ? 347 ASN A CA  1 
ATOM   2185 C  C   . ASN A 1 349 ? 157.660 111.991 140.088 1.00 47.22  ? 347 ASN A C   1 
ATOM   2186 O  O   . ASN A 1 349 ? 158.772 111.914 140.622 1.00 49.96  ? 347 ASN A O   1 
ATOM   2187 C  CB  . ASN A 1 349 ? 156.903 110.216 138.487 1.00 42.00  ? 347 ASN A CB  1 
ATOM   2188 C  CG  . ASN A 1 349 ? 156.755 108.714 138.412 1.00 45.83  ? 347 ASN A CG  1 
ATOM   2189 O  OD1 . ASN A 1 349 ? 155.836 108.202 137.775 1.00 48.79  ? 347 ASN A OD1 1 
ATOM   2190 N  ND2 . ASN A 1 349 ? 157.664 107.996 139.058 1.00 46.33  ? 347 ASN A ND2 1 
ATOM   2191 N  N   . ASN A 1 350 ? 157.167 113.145 139.640 1.00 45.61  ? 348 ASN A N   1 
ATOM   2192 C  CA  . ASN A 1 350 ? 157.910 114.395 139.724 1.00 41.52  ? 348 ASN A CA  1 
ATOM   2193 C  C   . ASN A 1 350 ? 157.524 115.244 140.928 1.00 44.56  ? 348 ASN A C   1 
ATOM   2194 O  O   . ASN A 1 350 ? 158.209 116.231 141.212 1.00 46.05  ? 348 ASN A O   1 
ATOM   2195 C  CB  . ASN A 1 350 ? 157.706 115.209 138.442 1.00 46.23  ? 348 ASN A CB  1 
ATOM   2196 C  CG  . ASN A 1 350 ? 158.235 114.499 137.213 1.00 43.96  ? 348 ASN A CG  1 
ATOM   2197 O  OD1 . ASN A 1 350 ? 159.277 113.850 137.260 1.00 46.75  ? 348 ASN A OD1 1 
ATOM   2198 N  ND2 . ASN A 1 350 ? 157.517 114.620 136.105 1.00 39.31  ? 348 ASN A ND2 1 
ATOM   2199 N  N   . GLN A 1 351 ? 156.456 114.887 141.639 1.00 50.20  ? 349 GLN A N   1 
ATOM   2200 C  CA  . GLN A 1 351 ? 156.053 115.582 142.861 1.00 48.84  ? 349 GLN A CA  1 
ATOM   2201 C  C   . GLN A 1 351 ? 155.738 117.052 142.604 1.00 44.69  ? 349 GLN A C   1 
ATOM   2202 O  O   . GLN A 1 351 ? 155.942 117.901 143.474 1.00 46.72  ? 349 GLN A O   1 
ATOM   2203 C  CB  . GLN A 1 351 ? 157.126 115.453 143.944 1.00 43.69  ? 349 GLN A CB  1 
ATOM   2204 C  CG  . GLN A 1 351 ? 157.478 114.019 144.299 1.00 43.56  ? 349 GLN A CG  1 
ATOM   2205 C  CD  . GLN A 1 351 ? 158.971 113.797 144.395 1.00 53.08  ? 349 GLN A CD  1 
ATOM   2206 O  OE1 . GLN A 1 351 ? 159.641 113.561 143.390 1.00 52.54  ? 349 GLN A OE1 1 
ATOM   2207 N  NE2 . GLN A 1 351 ? 159.502 113.869 145.610 1.00 50.50  ? 349 GLN A NE2 1 
ATOM   2208 N  N   . VAL A 1 352 ? 155.230 117.367 141.418 1.00 44.19  ? 350 VAL A N   1 
ATOM   2209 C  CA  . VAL A 1 352 ? 154.847 118.736 141.095 1.00 44.53  ? 350 VAL A CA  1 
ATOM   2210 C  C   . VAL A 1 352 ? 153.559 119.077 141.829 1.00 43.00  ? 350 VAL A C   1 
ATOM   2211 O  O   . VAL A 1 352 ? 152.682 118.223 142.009 1.00 47.04  ? 350 VAL A O   1 
ATOM   2212 C  CB  . VAL A 1 352 ? 154.686 118.912 139.575 1.00 43.30  ? 350 VAL A CB  1 
ATOM   2213 C  CG1 . VAL A 1 352 ? 154.308 120.347 139.251 1.00 41.54  ? 350 VAL A CG1 1 
ATOM   2214 C  CG2 . VAL A 1 352 ? 155.963 118.516 138.853 1.00 51.34  ? 350 VAL A CG2 1 
ATOM   2215 N  N   . ASP A 1 353 ? 153.441 120.331 142.257 1.00 46.38  ? 351 ASP A N   1 
ATOM   2216 C  CA  . ASP A 1 353 ? 152.260 120.764 142.990 1.00 48.68  ? 351 ASP A CA  1 
ATOM   2217 C  C   . ASP A 1 353 ? 151.003 120.544 142.159 1.00 46.49  ? 351 ASP A C   1 
ATOM   2218 O  O   . ASP A 1 353 ? 150.965 120.868 140.969 1.00 46.62  ? 351 ASP A O   1 
ATOM   2219 C  CB  . ASP A 1 353 ? 152.389 122.240 143.367 1.00 46.81  ? 351 ASP A CB  1 
ATOM   2220 C  CG  . ASP A 1 353 ? 151.849 122.538 144.747 1.00 51.25  ? 351 ASP A CG  1 
ATOM   2221 O  OD1 . ASP A 1 353 ? 152.288 121.883 145.714 1.00 53.56  ? 351 ASP A OD1 1 
ATOM   2222 O  OD2 . ASP A 1 353 ? 150.982 123.427 144.864 1.00 49.63  ? 351 ASP A OD2 1 
ATOM   2223 N  N   . LYS A 1 354 ? 149.968 119.989 142.793 1.00 45.21  ? 352 LYS A N   1 
ATOM   2224 C  CA  . LYS A 1 354 ? 148.701 119.782 142.104 1.00 43.99  ? 352 LYS A CA  1 
ATOM   2225 C  C   . LYS A 1 354 ? 147.994 121.093 141.797 1.00 46.96  ? 352 LYS A C   1 
ATOM   2226 O  O   . LYS A 1 354 ? 147.146 121.129 140.899 1.00 45.56  ? 352 LYS A O   1 
ATOM   2227 C  CB  . LYS A 1 354 ? 147.780 118.895 142.941 1.00 47.20  ? 352 LYS A CB  1 
ATOM   2228 C  CG  . LYS A 1 354 ? 148.340 117.518 143.245 1.00 49.62  ? 352 LYS A CG  1 
ATOM   2229 C  CD  . LYS A 1 354 ? 147.870 117.023 144.605 1.00 47.59  ? 352 LYS A CD  1 
ATOM   2230 C  CE  . LYS A 1 354 ? 148.192 115.551 144.815 1.00 49.19  ? 352 LYS A CE  1 
ATOM   2231 N  NZ  . LYS A 1 354 ? 147.675 114.689 143.715 1.00 48.86  ? 352 LYS A NZ  1 
ATOM   2232 N  N   . ARG A 1 355 ? 148.316 122.165 142.524 1.00 50.44  ? 353 ARG A N   1 
ATOM   2233 C  CA  . ARG A 1 355 ? 147.659 123.444 142.282 1.00 45.32  ? 353 ARG A CA  1 
ATOM   2234 C  C   . ARG A 1 355 ? 147.962 123.962 140.884 1.00 44.67  ? 353 ARG A C   1 
ATOM   2235 O  O   . ARG A 1 355 ? 147.067 124.457 140.189 1.00 46.67  ? 353 ARG A O   1 
ATOM   2236 C  CB  . ARG A 1 355 ? 148.092 124.461 143.336 1.00 45.10  ? 353 ARG A CB  1 
ATOM   2237 C  CG  . ARG A 1 355 ? 147.129 124.575 144.506 1.00 45.45  ? 353 ARG A CG  1 
ATOM   2238 C  CD  . ARG A 1 355 ? 147.748 125.298 145.690 1.00 45.77  ? 353 ARG A CD  1 
ATOM   2239 N  NE  . ARG A 1 355 ? 148.967 124.653 146.164 1.00 48.16  ? 353 ARG A NE  1 
ATOM   2240 C  CZ  . ARG A 1 355 ? 149.905 125.257 146.881 1.00 48.06  ? 353 ARG A CZ  1 
ATOM   2241 N  NH1 . ARG A 1 355 ? 149.797 126.527 147.235 1.00 51.71  ? 353 ARG A NH1 1 
ATOM   2242 N  NH2 . ARG A 1 355 ? 150.979 124.568 147.256 1.00 42.97  ? 353 ARG A NH2 1 
ATOM   2243 N  N   . ILE A 1 356 ? 149.219 123.856 140.452 1.00 43.65  ? 354 ILE A N   1 
ATOM   2244 C  CA  . ILE A 1 356 ? 149.594 124.323 139.123 1.00 45.31  ? 354 ILE A CA  1 
ATOM   2245 C  C   . ILE A 1 356 ? 149.485 123.226 138.069 1.00 43.96  ? 354 ILE A C   1 
ATOM   2246 O  O   . ILE A 1 356 ? 149.325 123.538 136.881 1.00 45.36  ? 354 ILE A O   1 
ATOM   2247 C  CB  . ILE A 1 356 ? 151.019 124.907 139.138 1.00 44.40  ? 354 ILE A CB  1 
ATOM   2248 C  CG1 . ILE A 1 356 ? 152.061 123.795 139.212 1.00 44.78  ? 354 ILE A CG1 1 
ATOM   2249 C  CG2 . ILE A 1 356 ? 151.198 125.862 140.308 1.00 45.07  ? 354 ILE A CG2 1 
ATOM   2250 C  CD1 . ILE A 1 356 ? 152.691 123.477 137.883 1.00 47.34  ? 354 ILE A CD1 1 
ATOM   2251 N  N   . THR A 1 357 ? 149.562 121.955 138.465 1.00 44.23  ? 355 THR A N   1 
ATOM   2252 C  CA  . THR A 1 357 ? 149.400 120.872 137.502 1.00 37.71  ? 355 THR A CA  1 
ATOM   2253 C  C   . THR A 1 357 ? 147.977 120.826 136.962 1.00 38.88  ? 355 THR A C   1 
ATOM   2254 O  O   . THR A 1 357 ? 147.762 120.509 135.788 1.00 39.57  ? 355 THR A O   1 
ATOM   2255 C  CB  . THR A 1 357 ? 149.769 119.536 138.145 1.00 39.18  ? 355 THR A CB  1 
ATOM   2256 O  OG1 . THR A 1 357 ? 151.109 119.594 138.645 1.00 46.96  ? 355 THR A OG1 1 
ATOM   2257 C  CG2 . THR A 1 357 ? 149.678 118.418 137.132 1.00 42.96  ? 355 THR A CG2 1 
ATOM   2258 N  N   . ARG A 1 358 ? 146.992 121.136 137.806 1.00 48.80  ? 356 ARG A N   1 
ATOM   2259 C  CA  . ARG A 1 358 ? 145.596 121.096 137.390 1.00 41.32  ? 356 ARG A CA  1 
ATOM   2260 C  C   . ARG A 1 358 ? 145.240 122.211 136.420 1.00 41.17  ? 356 ARG A C   1 
ATOM   2261 O  O   . ARG A 1 358 ? 144.150 122.177 135.841 1.00 42.12  ? 356 ARG A O   1 
ATOM   2262 C  CB  . ARG A 1 358 ? 144.684 121.168 138.619 1.00 39.23  ? 356 ARG A CB  1 
ATOM   2263 C  CG  . ARG A 1 358 ? 144.302 119.819 139.239 1.00 46.08  ? 356 ARG A CG  1 
ATOM   2264 C  CD  . ARG A 1 358 ? 143.650 118.841 138.258 1.00 46.84  ? 356 ARG A CD  1 
ATOM   2265 N  NE  . ARG A 1 358 ? 143.844 117.453 138.662 1.00 47.88  ? 356 ARG A NE  1 
ATOM   2266 C  CZ  . ARG A 1 358 ? 143.240 116.416 138.099 1.00 45.40  ? 356 ARG A CZ  1 
ATOM   2267 N  NH1 . ARG A 1 358 ? 142.384 116.570 137.103 1.00 43.26  ? 356 ARG A NH1 1 
ATOM   2268 N  NH2 . ARG A 1 358 ? 143.504 115.191 138.545 1.00 44.84  ? 356 ARG A NH2 1 
ATOM   2269 N  N   . PHE A 1 359 ? 146.116 123.196 136.239 1.00 43.06  ? 357 PHE A N   1 
ATOM   2270 C  CA  . PHE A 1 359 ? 145.922 124.246 135.248 1.00 40.51  ? 357 PHE A CA  1 
ATOM   2271 C  C   . PHE A 1 359 ? 146.800 124.045 134.020 1.00 36.40  ? 357 PHE A C   1 
ATOM   2272 O  O   . PHE A 1 359 ? 146.306 124.080 132.890 1.00 33.07  ? 357 PHE A O   1 
ATOM   2273 C  CB  . PHE A 1 359 ? 146.209 125.619 135.868 1.00 42.82  ? 357 PHE A CB  1 
ATOM   2274 C  CG  . PHE A 1 359 ? 146.260 126.732 134.863 1.00 41.88  ? 357 PHE A CG  1 
ATOM   2275 C  CD1 . PHE A 1 359 ? 145.098 127.331 134.418 1.00 38.70  ? 357 PHE A CD1 1 
ATOM   2276 C  CD2 . PHE A 1 359 ? 147.469 127.170 134.355 1.00 40.09  ? 357 PHE A CD2 1 
ATOM   2277 C  CE1 . PHE A 1 359 ? 145.140 128.349 133.491 1.00 39.04  ? 357 PHE A CE1 1 
ATOM   2278 C  CE2 . PHE A 1 359 ? 147.515 128.185 133.428 1.00 39.20  ? 357 PHE A CE2 1 
ATOM   2279 C  CZ  . PHE A 1 359 ? 146.350 128.776 132.995 1.00 38.89  ? 357 PHE A CZ  1 
ATOM   2280 N  N   . VAL A 1 360 ? 148.099 123.823 134.223 1.00 34.76  ? 358 VAL A N   1 
ATOM   2281 C  CA  . VAL A 1 360 ? 149.033 123.763 133.102 1.00 37.88  ? 358 VAL A CA  1 
ATOM   2282 C  C   . VAL A 1 360 ? 148.698 122.589 132.189 1.00 36.17  ? 358 VAL A C   1 
ATOM   2283 O  O   . VAL A 1 360 ? 148.657 122.727 130.962 1.00 42.14  ? 358 VAL A O   1 
ATOM   2284 C  CB  . VAL A 1 360 ? 150.481 123.682 133.618 1.00 35.85  ? 358 VAL A CB  1 
ATOM   2285 C  CG1 . VAL A 1 360 ? 151.456 123.490 132.467 1.00 35.19  ? 358 VAL A CG1 1 
ATOM   2286 C  CG2 . VAL A 1 360 ? 150.830 124.930 134.408 1.00 37.44  ? 358 VAL A CG2 1 
ATOM   2287 N  N   . LEU A 1 361 ? 148.446 121.412 132.777 1.00 35.41  ? 359 LEU A N   1 
ATOM   2288 C  CA  . LEU A 1 361 ? 148.258 120.216 131.954 1.00 35.61  ? 359 LEU A CA  1 
ATOM   2289 C  C   . LEU A 1 361 ? 146.969 120.276 131.149 1.00 36.92  ? 359 LEU A C   1 
ATOM   2290 O  O   . LEU A 1 361 ? 147.029 120.220 129.908 1.00 39.27  ? 359 LEU A O   1 
ATOM   2291 C  CB  . LEU A 1 361 ? 148.323 118.964 132.831 1.00 36.22  ? 359 LEU A CB  1 
ATOM   2292 C  CG  . LEU A 1 361 ? 149.685 118.588 133.420 1.00 34.16  ? 359 LEU A CG  1 
ATOM   2293 C  CD1 . LEU A 1 361 ? 149.593 117.245 134.115 1.00 36.74  ? 359 LEU A CD1 1 
ATOM   2294 C  CD2 . LEU A 1 361 ? 150.768 118.562 132.358 1.00 38.77  ? 359 LEU A CD2 1 
ATOM   2295 N  N   . PRO A 1 362 ? 145.785 120.373 131.760 1.00 35.26  ? 360 PRO A N   1 
ATOM   2296 C  CA  . PRO A 1 362 ? 144.556 120.356 130.949 1.00 32.87  ? 360 PRO A CA  1 
ATOM   2297 C  C   . PRO A 1 362 ? 144.479 121.494 129.950 1.00 33.46  ? 360 PRO A C   1 
ATOM   2298 O  O   . PRO A 1 362 ? 143.952 121.309 128.847 1.00 38.25  ? 360 PRO A O   1 
ATOM   2299 C  CB  . PRO A 1 362 ? 143.443 120.438 132.001 1.00 37.08  ? 360 PRO A CB  1 
ATOM   2300 C  CG  . PRO A 1 362 ? 144.078 121.029 133.191 1.00 37.56  ? 360 PRO A CG  1 
ATOM   2301 C  CD  . PRO A 1 362 ? 145.500 120.582 133.187 1.00 34.95  ? 360 PRO A CD  1 
ATOM   2302 N  N   . VAL A 1 363 ? 144.988 122.675 130.305 1.00 35.10  ? 361 VAL A N   1 
ATOM   2303 C  CA  . VAL A 1 363 ? 144.996 123.785 129.360 1.00 35.69  ? 361 VAL A CA  1 
ATOM   2304 C  C   . VAL A 1 363 ? 145.997 123.521 128.243 1.00 35.85  ? 361 VAL A C   1 
ATOM   2305 O  O   . VAL A 1 363 ? 145.706 123.751 127.064 1.00 34.43  ? 361 VAL A O   1 
ATOM   2306 C  CB  . VAL A 1 363 ? 145.292 125.107 130.089 1.00 37.60  ? 361 VAL A CB  1 
ATOM   2307 C  CG1 . VAL A 1 363 ? 145.398 126.249 129.096 1.00 34.22  ? 361 VAL A CG1 1 
ATOM   2308 C  CG2 . VAL A 1 363 ? 144.212 125.399 131.117 1.00 35.49  ? 361 VAL A CG2 1 
ATOM   2309 N  N   . GLY A 1 364 ? 147.182 123.022 128.589 1.00 39.57  ? 362 GLY A N   1 
ATOM   2310 C  CA  . GLY A 1 364 ? 148.200 122.746 127.596 1.00 31.73  ? 362 GLY A CA  1 
ATOM   2311 C  C   . GLY A 1 364 ? 147.965 121.510 126.760 1.00 35.55  ? 362 GLY A C   1 
ATOM   2312 O  O   . GLY A 1 364 ? 148.659 121.321 125.758 1.00 36.79  ? 362 GLY A O   1 
ATOM   2313 N  N   . ALA A 1 365 ? 147.007 120.663 127.139 1.00 38.10  ? 363 ALA A N   1 
ATOM   2314 C  CA  . ALA A 1 365 ? 146.716 119.476 126.345 1.00 32.25  ? 363 ALA A CA  1 
ATOM   2315 C  C   . ALA A 1 365 ? 146.167 119.826 124.970 1.00 36.71  ? 363 ALA A C   1 
ATOM   2316 O  O   . ALA A 1 365 ? 146.188 118.976 124.075 1.00 41.81  ? 363 ALA A O   1 
ATOM   2317 C  CB  . ALA A 1 365 ? 145.728 118.577 127.085 1.00 32.24  ? 363 ALA A CB  1 
ATOM   2318 N  N   . THR A 1 366 ? 145.675 121.050 124.784 1.00 35.92  ? 364 THR A N   1 
ATOM   2319 C  CA  . THR A 1 366 ? 145.226 121.517 123.479 1.00 38.70  ? 364 THR A CA  1 
ATOM   2320 C  C   . THR A 1 366 ? 145.832 122.846 123.056 1.00 36.04  ? 364 THR A C   1 
ATOM   2321 O  O   . THR A 1 366 ? 145.966 123.079 121.850 1.00 31.72  ? 364 THR A O   1 
ATOM   2322 C  CB  . THR A 1 366 ? 143.694 121.643 123.449 1.00 39.48  ? 364 THR A CB  1 
ATOM   2323 O  OG1 . THR A 1 366 ? 143.273 122.156 122.179 1.00 39.92  ? 364 THR A OG1 1 
ATOM   2324 C  CG2 . THR A 1 366 ? 143.205 122.558 124.554 1.00 41.28  ? 364 THR A CG2 1 
ATOM   2325 N  N   . ILE A 1 367 ? 146.253 123.684 124.000 1.00 32.47  ? 365 ILE A N   1 
ATOM   2326 C  CA  . ILE A 1 367 ? 146.781 125.030 123.623 1.00 31.01  ? 365 ILE A CA  1 
ATOM   2327 C  C   . ILE A 1 367 ? 148.280 124.914 123.325 1.00 36.05  ? 365 ILE A C   1 
ATOM   2328 O  O   . ILE A 1 367 ? 148.741 125.588 122.388 1.00 39.67  ? 365 ILE A O   1 
ATOM   2329 C  CB  . ILE A 1 367 ? 146.486 126.060 124.731 1.00 35.07  ? 365 ILE A CB  1 
ATOM   2330 C  CG1 . ILE A 1 367 ? 144.986 126.338 124.852 1.00 39.21  ? 365 ILE A CG1 1 
ATOM   2331 C  CG2 . ILE A 1 367 ? 147.277 127.339 124.512 1.00 36.91  ? 365 ILE A CG2 1 
ATOM   2332 C  CD1 . ILE A 1 367 ? 144.649 127.472 125.790 1.00 37.32  ? 365 ILE A CD1 1 
ATOM   2333 N  N   . ASN A 1 368 ? 149.002 124.076 124.069 1.00 34.35  ? 366 ASN A N   1 
ATOM   2334 C  CA  . ASN A 1 368 ? 150.448 123.938 123.919 1.00 29.11  ? 366 ASN A CA  1 
ATOM   2335 C  C   . ASN A 1 368 ? 150.735 122.695 123.087 1.00 37.60  ? 366 ASN A C   1 
ATOM   2336 O  O   . ASN A 1 368 ? 150.758 121.577 123.605 1.00 43.79  ? 366 ASN A O   1 
ATOM   2337 C  CB  . ASN A 1 368 ? 151.109 123.859 125.289 1.00 33.06  ? 366 ASN A CB  1 
ATOM   2338 C  CG  . ASN A 1 368 ? 152.608 124.011 125.224 1.00 39.58  ? 366 ASN A CG  1 
ATOM   2339 O  OD1 . ASN A 1 368 ? 153.146 124.576 124.274 1.00 44.00  ? 366 ASN A OD1 1 
ATOM   2340 N  ND2 . ASN A 1 368 ? 153.296 123.504 126.238 1.00 40.38  ? 366 ASN A ND2 1 
ATOM   2341 N  N   . MET A 1 369 ? 150.959 122.890 121.785 1.00 37.80  ? 367 MET A N   1 
ATOM   2342 C  CA  . MET A 1 369 ? 151.270 121.803 120.855 1.00 29.26  ? 367 MET A CA  1 
ATOM   2343 C  C   . MET A 1 369 ? 152.515 122.205 120.069 1.00 31.54  ? 367 MET A C   1 
ATOM   2344 O  O   . MET A 1 369 ? 152.422 122.737 118.962 1.00 38.65  ? 367 MET A O   1 
ATOM   2345 C  CB  . MET A 1 369 ? 150.089 121.519 119.938 1.00 28.55  ? 367 MET A CB  1 
ATOM   2346 C  CG  . MET A 1 369 ? 148.924 120.838 120.625 1.00 32.92  ? 367 MET A CG  1 
ATOM   2347 S  SD  . MET A 1 369 ? 147.697 120.238 119.457 1.00 38.86  ? 367 MET A SD  1 
ATOM   2348 C  CE  . MET A 1 369 ? 146.850 119.028 120.460 1.00 33.01  ? 367 MET A CE  1 
ATOM   2349 N  N   . ASP A 1 370 ? 153.688 121.936 120.645 1.00 32.04  ? 368 ASP A N   1 
ATOM   2350 C  CA  . ASP A 1 370 ? 154.935 122.253 119.958 1.00 32.50  ? 368 ASP A CA  1 
ATOM   2351 C  C   . ASP A 1 370 ? 155.208 121.268 118.830 1.00 39.07  ? 368 ASP A C   1 
ATOM   2352 O  O   . ASP A 1 370 ? 155.712 121.655 117.770 1.00 39.80  ? 368 ASP A O   1 
ATOM   2353 C  CB  . ASP A 1 370 ? 156.097 122.253 120.948 1.00 36.65  ? 368 ASP A CB  1 
ATOM   2354 C  CG  . ASP A 1 370 ? 155.838 123.132 122.149 1.00 42.29  ? 368 ASP A CG  1 
ATOM   2355 O  OD1 . ASP A 1 370 ? 154.978 124.030 122.052 1.00 44.46  ? 368 ASP A OD1 1 
ATOM   2356 O  OD2 . ASP A 1 370 ? 156.492 122.925 123.192 1.00 39.66  ? 368 ASP A OD2 1 
ATOM   2357 N  N   . GLY A 1 371 ? 154.899 119.989 119.045 1.00 34.59  ? 369 GLY A N   1 
ATOM   2358 C  CA  . GLY A 1 371 ? 155.100 119.009 117.993 1.00 26.73  ? 369 GLY A CA  1 
ATOM   2359 C  C   . GLY A 1 371 ? 154.238 119.280 116.777 1.00 29.77  ? 369 GLY A C   1 
ATOM   2360 O  O   . GLY A 1 371 ? 154.703 119.181 115.640 1.00 32.06  ? 369 GLY A O   1 
ATOM   2361 N  N   . THR A 1 372 ? 152.966 119.616 116.999 1.00 33.49  ? 370 THR A N   1 
ATOM   2362 C  CA  . THR A 1 372 ? 152.091 119.958 115.884 1.00 32.68  ? 370 THR A CA  1 
ATOM   2363 C  C   . THR A 1 372 ? 152.557 121.232 115.192 1.00 38.80  ? 370 THR A C   1 
ATOM   2364 O  O   . THR A 1 372 ? 152.593 121.297 113.959 1.00 42.34  ? 370 THR A O   1 
ATOM   2365 C  CB  . THR A 1 372 ? 150.652 120.111 116.375 1.00 31.95  ? 370 THR A CB  1 
ATOM   2366 O  OG1 . THR A 1 372 ? 150.285 118.960 117.141 1.00 36.68  ? 370 THR A OG1 1 
ATOM   2367 C  CG2 . THR A 1 372 ? 149.695 120.260 115.206 1.00 38.72  ? 370 THR A CG2 1 
ATOM   2368 N  N   . ALA A 1 373 ? 152.933 122.250 115.966 1.00 38.20  ? 371 ALA A N   1 
ATOM   2369 C  CA  . ALA A 1 373 ? 153.361 123.509 115.369 1.00 28.96  ? 371 ALA A CA  1 
ATOM   2370 C  C   . ALA A 1 373 ? 154.592 123.314 114.494 1.00 35.34  ? 371 ALA A C   1 
ATOM   2371 O  O   . ALA A 1 373 ? 154.672 123.864 113.390 1.00 38.82  ? 371 ALA A O   1 
ATOM   2372 C  CB  . ALA A 1 373 ? 153.635 124.536 116.465 1.00 34.50  ? 371 ALA A CB  1 
ATOM   2373 N  N   . LEU A 1 374 ? 155.564 122.535 114.971 1.00 32.61  ? 372 LEU A N   1 
ATOM   2374 C  CA  . LEU A 1 374 ? 156.730 122.227 114.151 1.00 29.29  ? 372 LEU A CA  1 
ATOM   2375 C  C   . LEU A 1 374 ? 156.332 121.451 112.904 1.00 33.85  ? 372 LEU A C   1 
ATOM   2376 O  O   . LEU A 1 374 ? 156.822 121.731 111.804 1.00 39.67  ? 372 LEU A O   1 
ATOM   2377 C  CB  . LEU A 1 374 ? 157.747 121.433 114.970 1.00 37.25  ? 372 LEU A CB  1 
ATOM   2378 C  CG  . LEU A 1 374 ? 159.139 121.275 114.358 1.00 36.31  ? 372 LEU A CG  1 
ATOM   2379 C  CD1 . LEU A 1 374 ? 160.193 121.275 115.447 1.00 35.57  ? 372 LEU A CD1 1 
ATOM   2380 C  CD2 . LEU A 1 374 ? 159.226 120.007 113.528 1.00 32.82  ? 372 LEU A CD2 1 
ATOM   2381 N  N   . TYR A 1 375 ? 155.446 120.467 113.057 1.00 37.87  ? 373 TYR A N   1 
ATOM   2382 C  CA  . TYR A 1 375 ? 155.043 119.644 111.923 1.00 36.82  ? 373 TYR A CA  1 
ATOM   2383 C  C   . TYR A 1 375 ? 154.257 120.454 110.900 1.00 36.67  ? 373 TYR A C   1 
ATOM   2384 O  O   . TYR A 1 375 ? 154.426 120.265 109.691 1.00 42.46  ? 373 TYR A O   1 
ATOM   2385 C  CB  . TYR A 1 375 ? 154.231 118.450 112.427 1.00 36.13  ? 373 TYR A CB  1 
ATOM   2386 C  CG  . TYR A 1 375 ? 153.198 117.921 111.461 1.00 40.46  ? 373 TYR A CG  1 
ATOM   2387 C  CD1 . TYR A 1 375 ? 153.508 116.897 110.578 1.00 39.68  ? 373 TYR A CD1 1 
ATOM   2388 C  CD2 . TYR A 1 375 ? 151.903 118.423 111.454 1.00 39.72  ? 373 TYR A CD2 1 
ATOM   2389 C  CE1 . TYR A 1 375 ? 152.567 116.404 109.702 1.00 41.42  ? 373 TYR A CE1 1 
ATOM   2390 C  CE2 . TYR A 1 375 ? 150.956 117.937 110.583 1.00 40.11  ? 373 TYR A CE2 1 
ATOM   2391 C  CZ  . TYR A 1 375 ? 151.292 116.926 109.710 1.00 47.63  ? 373 TYR A CZ  1 
ATOM   2392 O  OH  . TYR A 1 375 ? 150.350 116.433 108.839 1.00 53.24  ? 373 TYR A OH  1 
ATOM   2393 N  N   . GLU A 1 376 ? 153.391 121.358 111.363 1.00 36.28  ? 374 GLU A N   1 
ATOM   2394 C  CA  . GLU A 1 376 ? 152.623 122.185 110.438 1.00 32.94  ? 374 GLU A CA  1 
ATOM   2395 C  C   . GLU A 1 376 ? 153.536 123.079 109.608 1.00 35.92  ? 374 GLU A C   1 
ATOM   2396 O  O   . GLU A 1 376 ? 153.346 123.218 108.395 1.00 40.58  ? 374 GLU A O   1 
ATOM   2397 C  CB  . GLU A 1 376 ? 151.611 123.031 111.210 1.00 34.18  ? 374 GLU A CB  1 
ATOM   2398 C  CG  . GLU A 1 376 ? 150.608 122.227 112.021 1.00 38.93  ? 374 GLU A CG  1 
ATOM   2399 C  CD  . GLU A 1 376 ? 149.372 121.865 111.236 1.00 38.85  ? 374 GLU A CD  1 
ATOM   2400 O  OE1 . GLU A 1 376 ? 149.356 122.092 110.011 1.00 48.07  ? 374 GLU A OE1 1 
ATOM   2401 O  OE2 . GLU A 1 376 ? 148.416 121.348 111.847 1.00 35.96  ? 374 GLU A OE2 1 
ATOM   2402 N  N   . ALA A 1 377 ? 154.531 123.697 110.246 1.00 35.96  ? 375 ALA A N   1 
ATOM   2403 C  CA  . ALA A 1 377 ? 155.452 124.561 109.517 1.00 34.20  ? 375 ALA A CA  1 
ATOM   2404 C  C   . ALA A 1 377 ? 156.284 123.770 108.515 1.00 38.79  ? 375 ALA A C   1 
ATOM   2405 O  O   . ALA A 1 377 ? 156.454 124.198 107.369 1.00 39.42  ? 375 ALA A O   1 
ATOM   2406 C  CB  . ALA A 1 377 ? 156.359 125.299 110.499 1.00 37.57  ? 375 ALA A CB  1 
ATOM   2407 N  N   . VAL A 1 378 ? 156.816 122.618 108.929 1.00 41.42  ? 376 VAL A N   1 
ATOM   2408 C  CA  . VAL A 1 378 ? 157.596 121.793 108.011 1.00 36.96  ? 376 VAL A CA  1 
ATOM   2409 C  C   . VAL A 1 378 ? 156.712 121.271 106.888 1.00 36.68  ? 376 VAL A C   1 
ATOM   2410 O  O   . VAL A 1 378 ? 157.103 121.275 105.715 1.00 39.35  ? 376 VAL A O   1 
ATOM   2411 C  CB  . VAL A 1 378 ? 158.280 120.642 108.772 1.00 39.49  ? 376 VAL A CB  1 
ATOM   2412 C  CG1 . VAL A 1 378 ? 158.910 119.660 107.798 1.00 37.35  ? 376 VAL A CG1 1 
ATOM   2413 C  CG2 . VAL A 1 378 ? 159.323 121.183 109.728 1.00 41.07  ? 376 VAL A CG2 1 
ATOM   2414 N  N   . ALA A 1 379 ? 155.509 120.807 107.230 1.00 41.26  ? 377 ALA A N   1 
ATOM   2415 C  CA  . ALA A 1 379 ? 154.610 120.258 106.221 1.00 36.87  ? 377 ALA A CA  1 
ATOM   2416 C  C   . ALA A 1 379 ? 154.192 121.317 105.210 1.00 41.44  ? 377 ALA A C   1 
ATOM   2417 O  O   . ALA A 1 379 ? 154.183 121.057 104.002 1.00 43.67  ? 377 ALA A O   1 
ATOM   2418 C  CB  . ALA A 1 379 ? 153.382 119.654 106.897 1.00 37.38  ? 377 ALA A CB  1 
ATOM   2419 N  N   . ALA A 1 380 ? 153.839 122.514 105.681 1.00 45.88  ? 378 ALA A N   1 
ATOM   2420 C  CA  . ALA A 1 380 ? 153.390 123.563 104.772 1.00 37.20  ? 378 ALA A CA  1 
ATOM   2421 C  C   . ALA A 1 380 ? 154.503 123.995 103.826 1.00 35.04  ? 378 ALA A C   1 
ATOM   2422 O  O   . ALA A 1 380 ? 154.275 124.156 102.623 1.00 42.04  ? 378 ALA A O   1 
ATOM   2423 C  CB  . ALA A 1 380 ? 152.874 124.758 105.570 1.00 39.97  ? 378 ALA A CB  1 
ATOM   2424 N  N   . VAL A 1 381 ? 155.711 124.197 104.350 1.00 39.95  ? 379 VAL A N   1 
ATOM   2425 C  CA  . VAL A 1 381 ? 156.822 124.609 103.496 1.00 39.71  ? 379 VAL A CA  1 
ATOM   2426 C  C   . VAL A 1 381 ? 157.225 123.477 102.561 1.00 40.61  ? 379 VAL A C   1 
ATOM   2427 O  O   . VAL A 1 381 ? 157.602 123.713 101.408 1.00 44.16  ? 379 VAL A O   1 
ATOM   2428 C  CB  . VAL A 1 381 ? 158.007 125.086 104.352 1.00 37.86  ? 379 VAL A CB  1 
ATOM   2429 C  CG1 . VAL A 1 381 ? 159.192 125.423 103.465 1.00 38.92  ? 379 VAL A CG1 1 
ATOM   2430 C  CG2 . VAL A 1 381 ? 157.607 126.287 105.189 1.00 38.87  ? 379 VAL A CG2 1 
ATOM   2431 N  N   . PHE A 1 382 ? 157.168 122.234 103.042 1.00 39.85  ? 380 PHE A N   1 
ATOM   2432 C  CA  . PHE A 1 382 ? 157.499 121.101 102.185 1.00 38.05  ? 380 PHE A CA  1 
ATOM   2433 C  C   . PHE A 1 382 ? 156.533 120.997 101.013 1.00 40.40  ? 380 PHE A C   1 
ATOM   2434 O  O   . PHE A 1 382 ? 156.950 120.752 99.875  1.00 36.27  ? 380 PHE A O   1 
ATOM   2435 C  CB  . PHE A 1 382 ? 157.485 119.808 102.997 1.00 43.88  ? 380 PHE A CB  1 
ATOM   2436 C  CG  . PHE A 1 382 ? 157.419 118.569 102.155 1.00 44.60  ? 380 PHE A CG  1 
ATOM   2437 C  CD1 . PHE A 1 382 ? 158.464 118.234 101.317 1.00 39.34  ? 380 PHE A CD1 1 
ATOM   2438 C  CD2 . PHE A 1 382 ? 156.311 117.744 102.193 1.00 40.88  ? 380 PHE A CD2 1 
ATOM   2439 C  CE1 . PHE A 1 382 ? 158.410 117.100 100.541 1.00 39.00  ? 380 PHE A CE1 1 
ATOM   2440 C  CE2 . PHE A 1 382 ? 156.254 116.610 101.416 1.00 39.91  ? 380 PHE A CE2 1 
ATOM   2441 C  CZ  . PHE A 1 382 ? 157.305 116.288 100.590 1.00 40.26  ? 380 PHE A CZ  1 
ATOM   2442 N  N   . ILE A 1 383 ? 155.237 121.174 101.271 1.00 41.85  ? 381 ILE A N   1 
ATOM   2443 C  CA  . ILE A 1 383 ? 154.254 121.124 100.195 1.00 41.05  ? 381 ILE A CA  1 
ATOM   2444 C  C   . ILE A 1 383 ? 154.471 122.277 99.226  1.00 42.95  ? 381 ILE A C   1 
ATOM   2445 O  O   . ILE A 1 383 ? 154.329 122.119 98.009  1.00 41.92  ? 381 ILE A O   1 
ATOM   2446 C  CB  . ILE A 1 383 ? 152.829 121.128 100.777 1.00 42.27  ? 381 ILE A CB  1 
ATOM   2447 C  CG1 . ILE A 1 383 ? 152.516 119.773 101.412 1.00 43.03  ? 381 ILE A CG1 1 
ATOM   2448 C  CG2 . ILE A 1 383 ? 151.812 121.447 99.696  1.00 44.36  ? 381 ILE A CG2 1 
ATOM   2449 C  CD1 . ILE A 1 383 ? 151.351 119.800 102.372 1.00 43.67  ? 381 ILE A CD1 1 
ATOM   2450 N  N   . ALA A 1 384 ? 154.815 123.456 99.749  1.00 42.91  ? 382 ALA A N   1 
ATOM   2451 C  CA  . ALA A 1 384 ? 155.123 124.585 98.880  1.00 38.72  ? 382 ALA A CA  1 
ATOM   2452 C  C   . ALA A 1 384 ? 156.311 124.274 97.980  1.00 42.87  ? 382 ALA A C   1 
ATOM   2453 O  O   . ALA A 1 384 ? 156.311 124.625 96.796  1.00 50.21  ? 382 ALA A O   1 
ATOM   2454 C  CB  . ALA A 1 384 ? 155.399 125.830 99.721  1.00 42.42  ? 382 ALA A CB  1 
ATOM   2455 N  N   . GLN A 1 385 ? 157.334 123.617 98.527  1.00 39.16  ? 383 GLN A N   1 
ATOM   2456 C  CA  . GLN A 1 385 ? 158.477 123.220 97.713  1.00 38.42  ? 383 GLN A CA  1 
ATOM   2457 C  C   . GLN A 1 385 ? 158.066 122.231 96.630  1.00 41.23  ? 383 GLN A C   1 
ATOM   2458 O  O   . GLN A 1 385 ? 158.537 122.316 95.491  1.00 43.78  ? 383 GLN A O   1 
ATOM   2459 C  CB  . GLN A 1 385 ? 159.565 122.620 98.601  1.00 41.11  ? 383 GLN A CB  1 
ATOM   2460 C  CG  . GLN A 1 385 ? 160.300 123.641 99.450  1.00 40.67  ? 383 GLN A CG  1 
ATOM   2461 C  CD  . GLN A 1 385 ? 161.036 123.011 100.611 1.00 38.03  ? 383 GLN A CD  1 
ATOM   2462 O  OE1 . GLN A 1 385 ? 160.908 121.816 100.865 1.00 44.15  ? 383 GLN A OE1 1 
ATOM   2463 N  NE2 . GLN A 1 385 ? 161.813 123.813 101.323 1.00 39.54  ? 383 GLN A NE2 1 
ATOM   2464 N  N   . LEU A 1 386 ? 157.189 121.282 96.966  1.00 45.88  ? 384 LEU A N   1 
ATOM   2465 C  CA  . LEU A 1 386 ? 156.716 120.326 95.970  1.00 43.73  ? 384 LEU A CA  1 
ATOM   2466 C  C   . LEU A 1 386 ? 155.983 121.032 94.838  1.00 45.70  ? 384 LEU A C   1 
ATOM   2467 O  O   . LEU A 1 386 ? 156.154 120.683 93.664  1.00 47.81  ? 384 LEU A O   1 
ATOM   2468 C  CB  . LEU A 1 386 ? 155.800 119.293 96.626  1.00 41.34  ? 384 LEU A CB  1 
ATOM   2469 C  CG  . LEU A 1 386 ? 156.445 118.111 97.350  1.00 41.06  ? 384 LEU A CG  1 
ATOM   2470 C  CD1 . LEU A 1 386 ? 155.365 117.189 97.879  1.00 43.55  ? 384 LEU A CD1 1 
ATOM   2471 C  CD2 . LEU A 1 386 ? 157.394 117.348 96.439  1.00 42.74  ? 384 LEU A CD2 1 
ATOM   2472 N  N   . ASN A 1 387 ? 155.161 122.022 95.170  1.00 46.48  ? 385 ASN A N   1 
ATOM   2473 C  CA  . ASN A 1 387 ? 154.386 122.765 94.187  1.00 43.85  ? 385 ASN A CA  1 
ATOM   2474 C  C   . ASN A 1 387 ? 155.219 123.792 93.430  1.00 45.83  ? 385 ASN A C   1 
ATOM   2475 O  O   . ASN A 1 387 ? 154.657 124.575 92.659  1.00 43.46  ? 385 ASN A O   1 
ATOM   2476 C  CB  . ASN A 1 387 ? 153.210 123.459 94.877  1.00 46.56  ? 385 ASN A CB  1 
ATOM   2477 C  CG  . ASN A 1 387 ? 151.967 122.596 94.912  1.00 50.49  ? 385 ASN A CG  1 
ATOM   2478 O  OD1 . ASN A 1 387 ? 151.866 121.666 95.711  1.00 46.34  ? 385 ASN A OD1 1 
ATOM   2479 N  ND2 . ASN A 1 387 ? 151.010 122.901 94.045  1.00 54.05  ? 385 ASN A ND2 1 
ATOM   2480 N  N   . ASP A 1 388 ? 156.537 123.806 93.630  1.00 48.32  ? 386 ASP A N   1 
ATOM   2481 C  CA  . ASP A 1 388 ? 157.425 124.736 92.935  1.00 47.90  ? 386 ASP A CA  1 
ATOM   2482 C  C   . ASP A 1 388 ? 157.009 126.181 93.189  1.00 50.92  ? 386 ASP A C   1 
ATOM   2483 O  O   . ASP A 1 388 ? 157.088 127.036 92.305  1.00 54.89  ? 386 ASP A O   1 
ATOM   2484 C  CB  . ASP A 1 388 ? 157.460 124.440 91.434  1.00 51.21  ? 386 ASP A CB  1 
ATOM   2485 C  CG  . ASP A 1 388 ? 157.888 123.019 91.130  1.00 53.72  ? 386 ASP A CG  1 
ATOM   2486 O  OD1 . ASP A 1 388 ? 158.406 122.343 92.042  1.00 54.53  ? 386 ASP A OD1 1 
ATOM   2487 O  OD2 . ASP A 1 388 ? 157.704 122.576 89.977  1.00 51.38  ? 386 ASP A OD2 1 
ATOM   2488 N  N   . LEU A 1 389 ? 156.567 126.459 94.412  1.00 49.32  ? 387 LEU A N   1 
ATOM   2489 C  CA  . LEU A 1 389 ? 156.090 127.780 94.798  1.00 51.01  ? 387 LEU A CA  1 
ATOM   2490 C  C   . LEU A 1 389 ? 157.190 128.492 95.575  1.00 49.13  ? 387 LEU A C   1 
ATOM   2491 O  O   . LEU A 1 389 ? 157.685 127.969 96.578  1.00 50.15  ? 387 LEU A O   1 
ATOM   2492 C  CB  . LEU A 1 389 ? 154.813 127.668 95.632  1.00 47.55  ? 387 LEU A CB  1 
ATOM   2493 C  CG  . LEU A 1 389 ? 154.521 128.762 96.661  1.00 47.75  ? 387 LEU A CG  1 
ATOM   2494 C  CD1 . LEU A 1 389 ? 154.275 130.095 95.976  1.00 47.27  ? 387 LEU A CD1 1 
ATOM   2495 C  CD2 . LEU A 1 389 ? 153.329 128.373 97.518  1.00 50.59  ? 387 LEU A CD2 1 
ATOM   2496 N  N   . ASP A 1 390 ? 157.568 129.679 95.109  1.00 47.65  ? 388 ASP A N   1 
ATOM   2497 C  CA  . ASP A 1 390 ? 158.584 130.464 95.793  1.00 49.49  ? 388 ASP A CA  1 
ATOM   2498 C  C   . ASP A 1 390 ? 158.072 130.929 97.151  1.00 51.37  ? 388 ASP A C   1 
ATOM   2499 O  O   . ASP A 1 390 ? 156.881 131.196 97.334  1.00 51.88  ? 388 ASP A O   1 
ATOM   2500 C  CB  . ASP A 1 390 ? 158.987 131.670 94.945  1.00 50.00  ? 388 ASP A CB  1 
ATOM   2501 C  CG  . ASP A 1 390 ? 160.118 132.467 95.565  1.00 54.68  ? 388 ASP A CG  1 
ATOM   2502 O  OD1 . ASP A 1 390 ? 160.745 131.967 96.523  1.00 54.19  ? 388 ASP A OD1 1 
ATOM   2503 O  OD2 . ASP A 1 390 ? 160.379 133.595 95.096  1.00 55.90  ? 388 ASP A OD2 1 
ATOM   2504 N  N   . LEU A 1 391 ? 158.989 131.024 98.111  1.00 46.69  ? 389 LEU A N   1 
ATOM   2505 C  CA  . LEU A 1 391 ? 158.664 131.433 99.477  1.00 48.20  ? 389 LEU A CA  1 
ATOM   2506 C  C   . LEU A 1 391 ? 159.550 132.617 99.846  1.00 50.59  ? 389 LEU A C   1 
ATOM   2507 O  O   . LEU A 1 391 ? 160.743 132.448 100.115 1.00 48.15  ? 389 LEU A O   1 
ATOM   2508 C  CB  . LEU A 1 391 ? 158.853 130.281 100.458 1.00 48.16  ? 389 LEU A CB  1 
ATOM   2509 C  CG  . LEU A 1 391 ? 157.768 129.206 100.440 1.00 50.45  ? 389 LEU A CG  1 
ATOM   2510 C  CD1 . LEU A 1 391 ? 158.388 127.847 100.690 1.00 49.48  ? 389 LEU A CD1 1 
ATOM   2511 C  CD2 . LEU A 1 391 ? 156.690 129.508 101.468 1.00 49.12  ? 389 LEU A CD2 1 
ATOM   2512 N  N   . GLY A 1 392 ? 158.967 133.812 99.856  1.00 49.30  ? 390 GLY A N   1 
ATOM   2513 C  CA  . GLY A 1 392 ? 159.666 134.989 100.313 1.00 48.84  ? 390 GLY A CA  1 
ATOM   2514 C  C   . GLY A 1 392 ? 159.603 135.128 101.820 1.00 48.14  ? 390 GLY A C   1 
ATOM   2515 O  O   . GLY A 1 392 ? 159.024 134.311 102.534 1.00 50.02  ? 390 GLY A O   1 
ATOM   2516 N  N   . ILE A 1 393 ? 160.217 136.204 102.312 1.00 46.13  ? 391 ILE A N   1 
ATOM   2517 C  CA  . ILE A 1 393 ? 160.212 136.454 103.748 1.00 44.43  ? 391 ILE A CA  1 
ATOM   2518 C  C   . ILE A 1 393 ? 158.785 136.635 104.247 1.00 47.84  ? 391 ILE A C   1 
ATOM   2519 O  O   . ILE A 1 393 ? 158.432 136.182 105.342 1.00 48.08  ? 391 ILE A O   1 
ATOM   2520 C  CB  . ILE A 1 393 ? 161.092 137.676 104.079 1.00 45.60  ? 391 ILE A CB  1 
ATOM   2521 C  CG1 . ILE A 1 393 ? 161.365 137.777 105.587 1.00 48.11  ? 391 ILE A CG1 1 
ATOM   2522 C  CG2 . ILE A 1 393 ? 160.444 138.952 103.568 1.00 47.23  ? 391 ILE A CG2 1 
ATOM   2523 C  CD1 . ILE A 1 393 ? 161.691 136.462 106.273 1.00 45.81  ? 391 ILE A CD1 1 
ATOM   2524 N  N   . GLY A 1 394 ? 157.942 137.297 103.454 1.00 45.96  ? 392 GLY A N   1 
ATOM   2525 C  CA  . GLY A 1 394 ? 156.561 137.492 103.862 1.00 45.33  ? 392 GLY A CA  1 
ATOM   2526 C  C   . GLY A 1 394 ? 155.787 136.191 103.936 1.00 45.83  ? 392 GLY A C   1 
ATOM   2527 O  O   . GLY A 1 394 ? 154.999 135.979 104.862 1.00 48.64  ? 392 GLY A O   1 
ATOM   2528 N  N   . GLN A 1 395 ? 155.994 135.304 102.960 1.00 46.89  ? 393 GLN A N   1 
ATOM   2529 C  CA  . GLN A 1 395 ? 155.306 134.017 102.970 1.00 44.26  ? 393 GLN A CA  1 
ATOM   2530 C  C   . GLN A 1 395 ? 155.764 133.154 104.140 1.00 46.18  ? 393 GLN A C   1 
ATOM   2531 O  O   . GLN A 1 395 ? 154.963 132.424 104.732 1.00 45.87  ? 393 GLN A O   1 
ATOM   2532 C  CB  . GLN A 1 395 ? 155.535 133.292 101.647 1.00 49.62  ? 393 GLN A CB  1 
ATOM   2533 C  CG  . GLN A 1 395 ? 155.291 134.155 100.419 1.00 48.80  ? 393 GLN A CG  1 
ATOM   2534 C  CD  . GLN A 1 395 ? 154.489 133.436 99.356  1.00 54.15  ? 393 GLN A CD  1 
ATOM   2535 O  OE1 . GLN A 1 395 ? 153.439 132.861 99.639  1.00 50.43  ? 393 GLN A OE1 1 
ATOM   2536 N  NE2 . GLN A 1 395 ? 154.984 133.460 98.125  1.00 52.51  ? 393 GLN A NE2 1 
ATOM   2537 N  N   . ILE A 1 396 ? 157.051 133.218 104.482 1.00 44.95  ? 394 ILE A N   1 
ATOM   2538 C  CA  . ILE A 1 396 ? 157.558 132.443 105.609 1.00 42.55  ? 394 ILE A CA  1 
ATOM   2539 C  C   . ILE A 1 396 ? 156.958 132.943 106.917 1.00 44.17  ? 394 ILE A C   1 
ATOM   2540 O  O   . ILE A 1 396 ? 156.696 132.157 107.835 1.00 48.82  ? 394 ILE A O   1 
ATOM   2541 C  CB  . ILE A 1 396 ? 159.097 132.496 105.639 1.00 42.47  ? 394 ILE A CB  1 
ATOM   2542 C  CG1 . ILE A 1 396 ? 159.687 131.796 104.409 1.00 43.10  ? 394 ILE A CG1 1 
ATOM   2543 C  CG2 . ILE A 1 396 ? 159.627 131.878 106.922 1.00 44.00  ? 394 ILE A CG2 1 
ATOM   2544 C  CD1 . ILE A 1 396 ? 159.481 130.295 104.382 1.00 46.99  ? 394 ILE A CD1 1 
ATOM   2545 N  N   . ILE A 1 397 ? 156.743 134.255 107.032 1.00 42.93  ? 395 ILE A N   1 
ATOM   2546 C  CA  . ILE A 1 397 ? 156.221 134.814 108.276 1.00 39.99  ? 395 ILE A CA  1 
ATOM   2547 C  C   . ILE A 1 397 ? 154.762 134.420 108.474 1.00 42.25  ? 395 ILE A C   1 
ATOM   2548 O  O   . ILE A 1 397 ? 154.342 134.098 109.591 1.00 47.01  ? 395 ILE A O   1 
ATOM   2549 C  CB  . ILE A 1 397 ? 156.404 136.341 108.292 1.00 44.27  ? 395 ILE A CB  1 
ATOM   2550 C  CG1 . ILE A 1 397 ? 157.882 136.692 108.472 1.00 40.72  ? 395 ILE A CG1 1 
ATOM   2551 C  CG2 . ILE A 1 397 ? 155.580 136.965 109.405 1.00 43.84  ? 395 ILE A CG2 1 
ATOM   2552 C  CD1 . ILE A 1 397 ? 158.240 138.082 108.012 1.00 41.56  ? 395 ILE A CD1 1 
ATOM   2553 N  N   . THR A 1 398 ? 153.962 134.449 107.406 1.00 38.58  ? 396 THR A N   1 
ATOM   2554 C  CA  . THR A 1 398 ? 152.563 134.050 107.536 1.00 43.27  ? 396 THR A CA  1 
ATOM   2555 C  C   . THR A 1 398 ? 152.441 132.564 107.849 1.00 45.61  ? 396 THR A C   1 
ATOM   2556 O  O   . THR A 1 398 ? 151.510 132.147 108.546 1.00 44.07  ? 396 THR A O   1 
ATOM   2557 C  CB  . THR A 1 398 ? 151.782 134.397 106.266 1.00 43.63  ? 396 THR A CB  1 
ATOM   2558 O  OG1 . THR A 1 398 ? 150.435 133.922 106.387 1.00 39.60  ? 396 THR A OG1 1 
ATOM   2559 C  CG2 . THR A 1 398 ? 152.418 133.771 105.043 1.00 44.71  ? 396 THR A CG2 1 
ATOM   2560 N  N   . ILE A 1 399 ? 153.365 131.748 107.338 1.00 44.51  ? 397 ILE A N   1 
ATOM   2561 C  CA  . ILE A 1 399 ? 153.381 130.333 107.698 1.00 41.64  ? 397 ILE A CA  1 
ATOM   2562 C  C   . ILE A 1 399 ? 153.642 130.177 109.191 1.00 42.54  ? 397 ILE A C   1 
ATOM   2563 O  O   . ILE A 1 399 ? 153.014 129.357 109.869 1.00 45.02  ? 397 ILE A O   1 
ATOM   2564 C  CB  . ILE A 1 399 ? 154.426 129.575 106.859 1.00 41.46  ? 397 ILE A CB  1 
ATOM   2565 C  CG1 . ILE A 1 399 ? 153.925 129.408 105.423 1.00 45.73  ? 397 ILE A CG1 1 
ATOM   2566 C  CG2 . ILE A 1 399 ? 154.734 128.220 107.494 1.00 40.96  ? 397 ILE A CG2 1 
ATOM   2567 C  CD1 . ILE A 1 399 ? 154.903 128.714 104.496 1.00 39.93  ? 397 ILE A CD1 1 
ATOM   2568 N  N   . SER A 1 400 ? 154.581 130.961 109.723 1.00 36.10  ? 398 SER A N   1 
ATOM   2569 C  CA  . SER A 1 400 ? 154.889 130.884 111.146 1.00 39.23  ? 398 SER A CA  1 
ATOM   2570 C  C   . SER A 1 400 ? 153.677 131.257 111.990 1.00 42.74  ? 398 SER A C   1 
ATOM   2571 O  O   . SER A 1 400 ? 153.380 130.602 112.995 1.00 44.03  ? 398 SER A O   1 
ATOM   2572 C  CB  . SER A 1 400 ? 156.073 131.792 111.475 1.00 41.09  ? 398 SER A CB  1 
ATOM   2573 O  OG  . SER A 1 400 ? 157.082 131.695 110.487 1.00 44.95  ? 398 SER A OG  1 
ATOM   2574 N  N   . ILE A 1 401 ? 152.970 132.320 111.601 1.00 45.15  ? 399 ILE A N   1 
ATOM   2575 C  CA  . ILE A 1 401 ? 151.772 132.726 112.332 1.00 39.15  ? 399 ILE A CA  1 
ATOM   2576 C  C   . ILE A 1 401 ? 150.676 131.682 112.171 1.00 40.24  ? 399 ILE A C   1 
ATOM   2577 O  O   . ILE A 1 401 ? 150.023 131.285 113.142 1.00 40.56  ? 399 ILE A O   1 
ATOM   2578 C  CB  . ILE A 1 401 ? 151.298 134.113 111.860 1.00 40.15  ? 399 ILE A CB  1 
ATOM   2579 C  CG1 . ILE A 1 401 ? 152.406 135.152 112.049 1.00 40.21  ? 399 ILE A CG1 1 
ATOM   2580 C  CG2 . ILE A 1 401 ? 150.036 134.526 112.609 1.00 39.53  ? 399 ILE A CG2 1 
ATOM   2581 C  CD1 . ILE A 1 401 ? 152.114 136.483 111.393 1.00 40.93  ? 399 ILE A CD1 1 
ATOM   2582 N  N   . THR A 1 402 ? 150.453 131.227 110.938 1.00 43.29  ? 400 THR A N   1 
ATOM   2583 C  CA  . THR A 1 402 ? 149.382 130.270 110.689 1.00 38.69  ? 400 THR A CA  1 
ATOM   2584 C  C   . THR A 1 402 ? 149.655 128.946 111.389 1.00 42.16  ? 400 THR A C   1 
ATOM   2585 O  O   . THR A 1 402 ? 148.739 128.326 111.941 1.00 40.77  ? 400 THR A O   1 
ATOM   2586 C  CB  . THR A 1 402 ? 149.211 130.054 109.188 1.00 38.96  ? 400 THR A CB  1 
ATOM   2587 O  OG1 . THR A 1 402 ? 150.436 129.570 108.627 1.00 39.77  ? 400 THR A OG1 1 
ATOM   2588 C  CG2 . THR A 1 402 ? 148.844 131.357 108.516 1.00 40.16  ? 400 THR A CG2 1 
ATOM   2589 N  N   . ALA A 1 403 ? 150.909 128.493 111.369 1.00 43.81  ? 401 ALA A N   1 
ATOM   2590 C  CA  . ALA A 1 403 ? 151.265 127.261 112.065 1.00 36.21  ? 401 ALA A CA  1 
ATOM   2591 C  C   . ALA A 1 403 ? 151.056 127.397 113.567 1.00 39.45  ? 401 ALA A C   1 
ATOM   2592 O  O   . ALA A 1 403 ? 150.590 126.458 114.221 1.00 41.98  ? 401 ALA A O   1 
ATOM   2593 C  CB  . ALA A 1 403 ? 152.714 126.889 111.756 1.00 37.76  ? 401 ALA A CB  1 
ATOM   2594 N  N   . THR A 1 404 ? 151.405 128.554 114.132 1.00 36.57  ? 402 THR A N   1 
ATOM   2595 C  CA  . THR A 1 404 ? 151.219 128.765 115.564 1.00 35.58  ? 402 THR A CA  1 
ATOM   2596 C  C   . THR A 1 404 ? 149.747 128.698 115.944 1.00 37.89  ? 402 THR A C   1 
ATOM   2597 O  O   . THR A 1 404 ? 149.388 128.096 116.963 1.00 38.04  ? 402 THR A O   1 
ATOM   2598 C  CB  . THR A 1 404 ? 151.815 130.112 115.973 1.00 41.10  ? 402 THR A CB  1 
ATOM   2599 O  OG1 . THR A 1 404 ? 153.165 130.203 115.502 1.00 37.87  ? 402 THR A OG1 1 
ATOM   2600 C  CG2 . THR A 1 404 ? 151.801 130.271 117.484 1.00 39.95  ? 402 THR A CG2 1 
ATOM   2601 N  N   . SER A 1 405 ? 148.879 129.316 115.143 1.00 39.18  ? 403 SER A N   1 
ATOM   2602 C  CA  . SER A 1 405 ? 147.447 129.256 115.412 1.00 37.25  ? 403 SER A CA  1 
ATOM   2603 C  C   . SER A 1 405 ? 146.878 127.879 115.092 1.00 36.57  ? 403 SER A C   1 
ATOM   2604 O  O   . SER A 1 405 ? 145.944 127.421 115.759 1.00 46.25  ? 403 SER A O   1 
ATOM   2605 C  CB  . SER A 1 405 ? 146.720 130.333 114.610 1.00 38.22  ? 403 SER A CB  1 
ATOM   2606 O  OG  . SER A 1 405 ? 146.859 130.108 113.220 1.00 40.05  ? 403 SER A OG  1 
ATOM   2607 N  N   . ALA A 1 406 ? 147.420 127.210 114.073 1.00 32.92  ? 404 ALA A N   1 
ATOM   2608 C  CA  . ALA A 1 406 ? 146.962 125.865 113.745 1.00 38.90  ? 404 ALA A CA  1 
ATOM   2609 C  C   . ALA A 1 406 ? 147.235 124.898 114.890 1.00 39.09  ? 404 ALA A C   1 
ATOM   2610 O  O   . ALA A 1 406 ? 146.417 124.019 115.179 1.00 43.72  ? 404 ALA A O   1 
ATOM   2611 C  CB  . ALA A 1 406 ? 147.633 125.382 112.461 1.00 38.31  ? 404 ALA A CB  1 
ATOM   2612 N  N   . SER A 1 407 ? 148.388 125.037 115.546 1.00 31.63  ? 405 SER A N   1 
ATOM   2613 C  CA  . SER A 1 407 ? 148.687 124.192 116.696 1.00 30.57  ? 405 SER A CA  1 
ATOM   2614 C  C   . SER A 1 407 ? 147.717 124.457 117.841 1.00 34.02  ? 405 SER A C   1 
ATOM   2615 O  O   . SER A 1 407 ? 147.283 123.522 118.522 1.00 41.29  ? 405 SER A O   1 
ATOM   2616 C  CB  . SER A 1 407 ? 150.126 124.421 117.151 1.00 34.91  ? 405 SER A CB  1 
ATOM   2617 O  OG  . SER A 1 407 ? 150.202 125.490 118.075 1.00 39.99  ? 405 SER A OG  1 
ATOM   2618 N  N   . ILE A 1 408 ? 147.376 125.725 118.077 1.00 33.12  ? 406 ILE A N   1 
ATOM   2619 C  CA  . ILE A 1 408 ? 146.419 126.053 119.130 1.00 32.45  ? 406 ILE A CA  1 
ATOM   2620 C  C   . ILE A 1 408 ? 145.049 125.478 118.798 1.00 34.28  ? 406 ILE A C   1 
ATOM   2621 O  O   . ILE A 1 408 ? 144.375 124.902 119.660 1.00 41.30  ? 406 ILE A O   1 
ATOM   2622 C  CB  . ILE A 1 408 ? 146.353 127.577 119.341 1.00 29.38  ? 406 ILE A CB  1 
ATOM   2623 C  CG1 . ILE A 1 408 ? 147.709 128.110 119.805 1.00 34.25  ? 406 ILE A CG1 1 
ATOM   2624 C  CG2 . ILE A 1 408 ? 145.271 127.924 120.351 1.00 30.26  ? 406 ILE A CG2 1 
ATOM   2625 C  CD1 . ILE A 1 408 ? 147.849 129.608 119.682 1.00 35.11  ? 406 ILE A CD1 1 
ATOM   2626 N  N   . GLY A 1 409 ? 144.614 125.628 117.547 1.00 36.55  ? 407 GLY A N   1 
ATOM   2627 C  CA  . GLY A 1 409 ? 143.306 125.141 117.150 1.00 36.21  ? 407 GLY A CA  1 
ATOM   2628 C  C   . GLY A 1 409 ? 143.214 123.635 117.039 1.00 37.72  ? 407 GLY A C   1 
ATOM   2629 O  O   . GLY A 1 409 ? 142.108 123.090 117.091 1.00 44.91  ? 407 GLY A O   1 
ATOM   2630 N  N   . ALA A 1 410 ? 144.343 122.953 116.880 1.00 38.09  ? 408 ALA A N   1 
ATOM   2631 C  CA  . ALA A 1 410 ? 144.329 121.500 116.804 1.00 33.34  ? 408 ALA A CA  1 
ATOM   2632 C  C   . ALA A 1 410 ? 143.920 120.904 118.145 1.00 30.47  ? 408 ALA A C   1 
ATOM   2633 O  O   . ALA A 1 410 ? 144.323 121.386 119.206 1.00 31.12  ? 408 ALA A O   1 
ATOM   2634 C  CB  . ALA A 1 410 ? 145.702 120.976 116.389 1.00 36.72  ? 408 ALA A CB  1 
ATOM   2635 N  N   . ALA A 1 411 ? 143.114 119.852 118.092 1.00 36.54  ? 409 ALA A N   1 
ATOM   2636 C  CA  . ALA A 1 411 ? 142.652 119.170 119.289 1.00 36.51  ? 409 ALA A CA  1 
ATOM   2637 C  C   . ALA A 1 411 ? 143.574 118.004 119.633 1.00 37.27  ? 409 ALA A C   1 
ATOM   2638 O  O   . ALA A 1 411 ? 144.285 117.467 118.782 1.00 32.69  ? 409 ALA A O   1 
ATOM   2639 C  CB  . ALA A 1 411 ? 141.221 118.669 119.103 1.00 30.75  ? 409 ALA A CB  1 
ATOM   2640 N  N   . GLY A 1 412 ? 143.553 117.616 120.903 1.00 38.55  ? 410 GLY A N   1 
ATOM   2641 C  CA  . GLY A 1 412 ? 144.375 116.516 121.366 1.00 31.95  ? 410 GLY A CA  1 
ATOM   2642 C  C   . GLY A 1 412 ? 143.852 115.167 120.922 1.00 33.19  ? 410 GLY A C   1 
ATOM   2643 O  O   . GLY A 1 412 ? 143.553 114.306 121.753 1.00 34.37  ? 410 GLY A O   1 
ATOM   2644 N  N   . VAL A 1 413 ? 143.734 114.973 119.612 1.00 34.53  ? 411 VAL A N   1 
ATOM   2645 C  CA  . VAL A 1 413 ? 143.236 113.719 119.051 1.00 30.22  ? 411 VAL A CA  1 
ATOM   2646 C  C   . VAL A 1 413 ? 144.141 113.325 117.893 1.00 34.59  ? 411 VAL A C   1 
ATOM   2647 O  O   . VAL A 1 413 ? 144.889 114.158 117.358 1.00 38.55  ? 411 VAL A O   1 
ATOM   2648 C  CB  . VAL A 1 413 ? 141.761 113.840 118.601 1.00 35.26  ? 411 VAL A CB  1 
ATOM   2649 C  CG1 . VAL A 1 413 ? 140.865 114.069 119.806 1.00 28.79  ? 411 VAL A CG1 1 
ATOM   2650 C  CG2 . VAL A 1 413 ? 141.595 114.956 117.585 1.00 36.44  ? 411 VAL A CG2 1 
ATOM   2651 N  N   . PRO A 1 414 ? 144.113 112.036 117.483 1.00 36.63  ? 412 PRO A N   1 
ATOM   2652 C  CA  . PRO A 1 414 ? 144.884 111.599 116.329 1.00 40.13  ? 412 PRO A CA  1 
ATOM   2653 C  C   . PRO A 1 414 ? 144.434 112.355 115.076 1.00 42.55  ? 412 PRO A C   1 
ATOM   2654 O  O   . PRO A 1 414 ? 143.247 112.552 114.927 1.00 46.86  ? 412 PRO A O   1 
ATOM   2655 C  CB  . PRO A 1 414 ? 144.532 110.110 116.204 1.00 32.25  ? 412 PRO A CB  1 
ATOM   2656 C  CG  . PRO A 1 414 ? 144.143 109.707 117.602 1.00 29.45  ? 412 PRO A CG  1 
ATOM   2657 C  CD  . PRO A 1 414 ? 143.411 110.919 118.132 1.00 36.48  ? 412 PRO A CD  1 
ATOM   2658 N  N   . GLN A 1 415 ? 145.384 112.799 114.251 1.00 34.40  ? 413 GLN A N   1 
ATOM   2659 C  CA  . GLN A 1 415 ? 145.049 113.452 112.956 1.00 38.44  ? 413 GLN A CA  1 
ATOM   2660 C  C   . GLN A 1 415 ? 144.559 114.896 113.143 1.00 41.96  ? 413 GLN A C   1 
ATOM   2661 O  O   . GLN A 1 415 ? 144.316 115.544 112.110 1.00 40.18  ? 413 GLN A O   1 
ATOM   2662 C  CB  . GLN A 1 415 ? 144.040 112.590 112.195 1.00 40.95  ? 413 GLN A CB  1 
ATOM   2663 C  CG  . GLN A 1 415 ? 144.515 111.165 111.958 1.00 38.10  ? 413 GLN A CG  1 
ATOM   2664 C  CD  . GLN A 1 415 ? 143.361 110.199 111.844 1.00 40.70  ? 413 GLN A CD  1 
ATOM   2665 O  OE1 . GLN A 1 415 ? 142.209 110.549 112.082 1.00 39.93  ? 413 GLN A OE1 1 
ATOM   2666 N  NE2 . GLN A 1 415 ? 143.668 108.964 111.483 1.00 40.43  ? 413 GLN A NE2 1 
ATOM   2667 N  N   . ALA A 1 416 ? 144.414 115.395 114.379 1.00 38.75  ? 414 ALA A N   1 
ATOM   2668 C  CA  . ALA A 1 416 ? 144.045 116.799 114.522 1.00 37.21  ? 414 ALA A CA  1 
ATOM   2669 C  C   . ALA A 1 416 ? 144.925 117.702 113.666 1.00 37.69  ? 414 ALA A C   1 
ATOM   2670 O  O   . ALA A 1 416 ? 144.445 118.695 113.110 1.00 35.97  ? 414 ALA A O   1 
ATOM   2671 C  CB  . ALA A 1 416 ? 144.128 117.208 115.988 1.00 35.39  ? 414 ALA A CB  1 
ATOM   2672 N  N   . GLY A 1 417 ? 146.213 117.382 113.553 1.00 41.41  ? 415 GLY A N   1 
ATOM   2673 C  CA  . GLY A 1 417 ? 147.120 118.253 112.826 1.00 36.29  ? 415 GLY A CA  1 
ATOM   2674 C  C   . GLY A 1 417 ? 146.774 118.396 111.358 1.00 40.17  ? 415 GLY A C   1 
ATOM   2675 O  O   . GLY A 1 417 ? 147.131 119.394 110.728 1.00 46.53  ? 415 GLY A O   1 
ATOM   2676 N  N   . LEU A 1 418 ? 146.086 117.405 110.789 1.00 42.22  ? 416 LEU A N   1 
ATOM   2677 C  CA  . LEU A 1 418 ? 145.750 117.458 109.371 1.00 40.07  ? 416 LEU A CA  1 
ATOM   2678 C  C   . LEU A 1 418 ? 144.596 118.413 109.092 1.00 41.59  ? 416 LEU A C   1 
ATOM   2679 O  O   . LEU A 1 418 ? 144.591 119.092 108.060 1.00 45.88  ? 416 LEU A O   1 
ATOM   2680 C  CB  . LEU A 1 418 ? 145.412 116.059 108.861 1.00 43.17  ? 416 LEU A CB  1 
ATOM   2681 C  CG  . LEU A 1 418 ? 146.550 115.040 108.913 1.00 43.46  ? 416 LEU A CG  1 
ATOM   2682 C  CD1 . LEU A 1 418 ? 145.993 113.630 108.967 1.00 43.34  ? 416 LEU A CD1 1 
ATOM   2683 C  CD2 . LEU A 1 418 ? 147.471 115.214 107.717 1.00 44.16  ? 416 LEU A CD2 1 
ATOM   2684 N  N   . VAL A 1 419 ? 143.606 118.477 109.984 1.00 42.28  ? 417 VAL A N   1 
ATOM   2685 C  CA  . VAL A 1 419 ? 142.452 119.335 109.729 1.00 40.81  ? 417 VAL A CA  1 
ATOM   2686 C  C   . VAL A 1 419 ? 142.856 120.801 109.803 1.00 40.26  ? 417 VAL A C   1 
ATOM   2687 O  O   . VAL A 1 419 ? 142.356 121.636 109.041 1.00 47.99  ? 417 VAL A O   1 
ATOM   2688 C  CB  . VAL A 1 419 ? 141.301 119.010 110.703 1.00 40.07  ? 417 VAL A CB  1 
ATOM   2689 C  CG1 . VAL A 1 419 ? 141.121 117.506 110.841 1.00 40.85  ? 417 VAL A CG1 1 
ATOM   2690 C  CG2 . VAL A 1 419 ? 141.524 119.658 112.058 1.00 39.17  ? 417 VAL A CG2 1 
ATOM   2691 N  N   . THR A 1 420 ? 143.764 121.141 110.718 1.00 38.41  ? 418 THR A N   1 
ATOM   2692 C  CA  . THR A 1 420 ? 144.220 122.516 110.862 1.00 37.00  ? 418 THR A CA  1 
ATOM   2693 C  C   . THR A 1 420 ? 145.303 122.889 109.859 1.00 38.04  ? 418 THR A C   1 
ATOM   2694 O  O   . THR A 1 420 ? 145.658 124.068 109.769 1.00 40.49  ? 418 THR A O   1 
ATOM   2695 C  CB  . THR A 1 420 ? 144.748 122.753 112.278 1.00 38.36  ? 418 THR A CB  1 
ATOM   2696 O  OG1 . THR A 1 420 ? 145.847 121.873 112.536 1.00 38.57  ? 418 THR A OG1 1 
ATOM   2697 C  CG2 . THR A 1 420 ? 143.660 122.501 113.300 1.00 40.61  ? 418 THR A CG2 1 
ATOM   2698 N  N   . MET A 1 421 ? 145.838 121.922 109.111 1.00 38.25  ? 419 MET A N   1 
ATOM   2699 C  CA  . MET A 1 421 ? 146.851 122.241 108.114 1.00 39.93  ? 419 MET A CA  1 
ATOM   2700 C  C   . MET A 1 421 ? 146.234 122.932 106.907 1.00 45.57  ? 419 MET A C   1 
ATOM   2701 O  O   . MET A 1 421 ? 146.924 123.675 106.200 1.00 48.80  ? 419 MET A O   1 
ATOM   2702 C  CB  . MET A 1 421 ? 147.582 120.965 107.693 1.00 35.50  ? 419 MET A CB  1 
ATOM   2703 C  CG  . MET A 1 421 ? 148.400 121.078 106.409 1.00 41.94  ? 419 MET A CG  1 
ATOM   2704 S  SD  . MET A 1 421 ? 150.066 120.408 106.564 1.00 66.49  ? 419 MET A SD  1 
ATOM   2705 C  CE  . MET A 1 421 ? 149.743 118.826 107.339 1.00 48.25  ? 419 MET A CE  1 
ATOM   2706 N  N   . VAL A 1 422 ? 144.942 122.714 106.662 1.00 43.71  ? 420 VAL A N   1 
ATOM   2707 C  CA  . VAL A 1 422 ? 144.276 123.387 105.552 1.00 42.25  ? 420 VAL A CA  1 
ATOM   2708 C  C   . VAL A 1 422 ? 144.367 124.897 105.723 1.00 41.92  ? 420 VAL A C   1 
ATOM   2709 O  O   . VAL A 1 422 ? 144.555 125.638 104.752 1.00 48.87  ? 420 VAL A O   1 
ATOM   2710 C  CB  . VAL A 1 422 ? 142.815 122.910 105.445 1.00 46.63  ? 420 VAL A CB  1 
ATOM   2711 C  CG1 . VAL A 1 422 ? 141.974 123.908 104.659 1.00 45.84  ? 420 VAL A CG1 1 
ATOM   2712 C  CG2 . VAL A 1 422 ? 142.758 121.532 104.808 1.00 42.89  ? 420 VAL A CG2 1 
ATOM   2713 N  N   . ILE A 1 423 ? 144.239 125.374 106.961 1.00 37.27  ? 421 ILE A N   1 
ATOM   2714 C  CA  . ILE A 1 423 ? 144.368 126.802 107.225 1.00 40.99  ? 421 ILE A CA  1 
ATOM   2715 C  C   . ILE A 1 423 ? 145.785 127.275 106.920 1.00 41.47  ? 421 ILE A C   1 
ATOM   2716 O  O   . ILE A 1 423 ? 145.987 128.386 106.417 1.00 41.88  ? 421 ILE A O   1 
ATOM   2717 C  CB  . ILE A 1 423 ? 143.952 127.106 108.679 1.00 43.36  ? 421 ILE A CB  1 
ATOM   2718 C  CG1 . ILE A 1 423 ? 142.507 127.608 108.727 1.00 43.55  ? 421 ILE A CG1 1 
ATOM   2719 C  CG2 . ILE A 1 423 ? 144.879 128.122 109.337 1.00 38.21  ? 421 ILE A CG2 1 
ATOM   2720 C  CD1 . ILE A 1 423 ? 141.512 126.697 108.043 1.00 42.01  ? 421 ILE A CD1 1 
ATOM   2721 N  N   . VAL A 1 424 ? 146.788 126.448 107.219 1.00 39.94  ? 422 VAL A N   1 
ATOM   2722 C  CA  . VAL A 1 424 ? 148.171 126.832 106.948 1.00 37.96  ? 422 VAL A CA  1 
ATOM   2723 C  C   . VAL A 1 424 ? 148.442 126.842 105.448 1.00 41.47  ? 422 VAL A C   1 
ATOM   2724 O  O   . VAL A 1 424 ? 149.109 127.744 104.931 1.00 47.93  ? 422 VAL A O   1 
ATOM   2725 C  CB  . VAL A 1 424 ? 149.140 125.894 107.690 1.00 37.82  ? 422 VAL A CB  1 
ATOM   2726 C  CG1 . VAL A 1 424 ? 150.566 126.401 107.569 1.00 39.68  ? 422 VAL A CG1 1 
ATOM   2727 C  CG2 . VAL A 1 424 ? 148.741 125.765 109.149 1.00 38.78  ? 422 VAL A CG2 1 
ATOM   2728 N  N   . LEU A 1 425 ? 147.947 125.833 104.728 1.00 42.62  ? 423 LEU A N   1 
ATOM   2729 C  CA  . LEU A 1 425 ? 148.172 125.777 103.288 1.00 41.69  ? 423 LEU A CA  1 
ATOM   2730 C  C   . LEU A 1 425 ? 147.489 126.935 102.573 1.00 45.95  ? 423 LEU A C   1 
ATOM   2731 O  O   . LEU A 1 425 ? 148.070 127.538 101.663 1.00 42.54  ? 423 LEU A O   1 
ATOM   2732 C  CB  . LEU A 1 425 ? 147.675 124.444 102.732 1.00 45.66  ? 423 LEU A CB  1 
ATOM   2733 C  CG  . LEU A 1 425 ? 148.467 123.198 103.126 1.00 45.19  ? 423 LEU A CG  1 
ATOM   2734 C  CD1 . LEU A 1 425 ? 147.798 121.962 102.561 1.00 45.10  ? 423 LEU A CD1 1 
ATOM   2735 C  CD2 . LEU A 1 425 ? 149.907 123.291 102.651 1.00 44.50  ? 423 LEU A CD2 1 
ATOM   2736 N  N   . SER A 1 426 ? 146.255 127.255 102.964 1.00 47.71  ? 424 SER A N   1 
ATOM   2737 C  CA  . SER A 1 426 ? 145.523 128.325 102.295 1.00 43.65  ? 424 SER A CA  1 
ATOM   2738 C  C   . SER A 1 426 ? 146.154 129.686 102.551 1.00 43.54  ? 424 SER A C   1 
ATOM   2739 O  O   . SER A 1 426 ? 146.025 130.591 101.719 1.00 44.31  ? 424 SER A O   1 
ATOM   2740 C  CB  . SER A 1 426 ? 144.065 128.324 102.750 1.00 44.02  ? 424 SER A CB  1 
ATOM   2741 O  OG  . SER A 1 426 ? 143.954 128.711 104.106 1.00 46.68  ? 424 SER A OG  1 
ATOM   2742 N  N   . ALA A 1 427 ? 146.838 129.852 103.685 1.00 40.92  ? 425 ALA A N   1 
ATOM   2743 C  CA  . ALA A 1 427 ? 147.437 131.143 104.003 1.00 41.89  ? 425 ALA A CA  1 
ATOM   2744 C  C   . ALA A 1 427 ? 148.494 131.541 102.984 1.00 47.93  ? 425 ALA A C   1 
ATOM   2745 O  O   . ALA A 1 427 ? 148.745 132.736 102.788 1.00 44.48  ? 425 ALA A O   1 
ATOM   2746 C  CB  . ALA A 1 427 ? 148.041 131.109 105.405 1.00 44.58  ? 425 ALA A CB  1 
ATOM   2747 N  N   . VAL A 1 428 ? 149.126 130.568 102.335 1.00 50.65  ? 426 VAL A N   1 
ATOM   2748 C  CA  . VAL A 1 428 ? 150.121 130.831 101.305 1.00 45.56  ? 426 VAL A CA  1 
ATOM   2749 C  C   . VAL A 1 428 ? 149.572 130.511 99.915  1.00 46.93  ? 426 VAL A C   1 
ATOM   2750 O  O   . VAL A 1 428 ? 150.334 130.405 98.957  1.00 49.90  ? 426 VAL A O   1 
ATOM   2751 C  CB  . VAL A 1 428 ? 151.424 130.063 101.578 1.00 48.01  ? 426 VAL A CB  1 
ATOM   2752 C  CG1 . VAL A 1 428 ? 152.145 130.663 102.770 1.00 48.48  ? 426 VAL A CG1 1 
ATOM   2753 C  CG2 . VAL A 1 428 ? 151.144 128.585 101.802 1.00 47.01  ? 426 VAL A CG2 1 
ATOM   2754 N  N   . GLY A 1 429 ? 148.258 130.355 99.795  1.00 43.53  ? 427 GLY A N   1 
ATOM   2755 C  CA  . GLY A 1 429 ? 147.641 130.121 98.506  1.00 46.81  ? 427 GLY A CA  1 
ATOM   2756 C  C   . GLY A 1 429 ? 147.918 128.743 97.948  1.00 48.39  ? 427 GLY A C   1 
ATOM   2757 O  O   . GLY A 1 429 ? 148.487 128.610 96.860  1.00 53.15  ? 427 GLY A O   1 
ATOM   2758 N  N   . LEU A 1 430 ? 147.525 127.709 98.683  1.00 48.12  ? 428 LEU A N   1 
ATOM   2759 C  CA  . LEU A 1 430 ? 147.659 126.334 98.237  1.00 44.30  ? 428 LEU A CA  1 
ATOM   2760 C  C   . LEU A 1 430 ? 146.340 125.606 98.437  1.00 48.65  ? 428 LEU A C   1 
ATOM   2761 O  O   . LEU A 1 430 ? 145.577 125.937 99.349  1.00 48.45  ? 428 LEU A O   1 
ATOM   2762 C  CB  . LEU A 1 430 ? 148.769 125.602 99.004  1.00 44.92  ? 428 LEU A CB  1 
ATOM   2763 C  CG  . LEU A 1 430 ? 150.202 125.932 98.582  1.00 51.56  ? 428 LEU A CG  1 
ATOM   2764 C  CD1 . LEU A 1 430 ? 151.188 125.449 99.630  1.00 48.85  ? 428 LEU A CD1 1 
ATOM   2765 C  CD2 . LEU A 1 430 ? 150.519 125.326 97.228  1.00 46.12  ? 428 LEU A CD2 1 
ATOM   2766 N  N   . PRO A 1 431 ? 146.044 124.608 97.604  1.00 48.67  ? 429 PRO A N   1 
ATOM   2767 C  CA  . PRO A 1 431 ? 144.772 123.894 97.749  1.00 45.44  ? 429 PRO A CA  1 
ATOM   2768 C  C   . PRO A 1 431 ? 144.700 123.140 99.067  1.00 48.61  ? 429 PRO A C   1 
ATOM   2769 O  O   . PRO A 1 431 ? 145.709 122.682 99.605  1.00 48.80  ? 429 PRO A O   1 
ATOM   2770 C  CB  . PRO A 1 431 ? 144.753 122.931 96.554  1.00 48.31  ? 429 PRO A CB  1 
ATOM   2771 C  CG  . PRO A 1 431 ? 145.919 123.281 95.704  1.00 50.47  ? 429 PRO A CG  1 
ATOM   2772 C  CD  . PRO A 1 431 ? 146.877 124.060 96.522  1.00 48.35  ? 429 PRO A CD  1 
ATOM   2773 N  N   . ALA A 1 432 ? 143.479 123.018 99.589  1.00 50.96  ? 430 ALA A N   1 
ATOM   2774 C  CA  . ALA A 1 432 ? 143.245 122.195 100.767 1.00 48.15  ? 430 ALA A CA  1 
ATOM   2775 C  C   . ALA A 1 432 ? 143.406 120.710 100.477 1.00 50.69  ? 430 ALA A C   1 
ATOM   2776 O  O   . ALA A 1 432 ? 143.475 119.915 101.421 1.00 48.89  ? 430 ALA A O   1 
ATOM   2777 C  CB  . ALA A 1 432 ? 141.847 122.463 101.323 1.00 50.81  ? 430 ALA A CB  1 
ATOM   2778 N  N   . GLU A 1 433 ? 143.467 120.320 99.206  1.00 48.76  ? 431 GLU A N   1 
ATOM   2779 C  CA  . GLU A 1 433 ? 143.651 118.930 98.819  1.00 47.02  ? 431 GLU A CA  1 
ATOM   2780 C  C   . GLU A 1 433 ? 145.116 118.528 98.753  1.00 49.96  ? 431 GLU A C   1 
ATOM   2781 O  O   . GLU A 1 433 ? 145.413 117.382 98.405  1.00 52.85  ? 431 GLU A O   1 
ATOM   2782 C  CB  . GLU A 1 433 ? 142.990 118.670 97.462  1.00 49.40  ? 431 GLU A CB  1 
ATOM   2783 C  CG  . GLU A 1 433 ? 141.598 118.068 97.559  1.00 53.23  ? 431 GLU A CG  1 
ATOM   2784 C  CD  . GLU A 1 433 ? 140.586 119.033 98.146  1.00 56.13  ? 431 GLU A CD  1 
ATOM   2785 O  OE1 . GLU A 1 433 ? 140.236 120.018 97.462  1.00 57.76  ? 431 GLU A OE1 1 
ATOM   2786 O  OE2 . GLU A 1 433 ? 140.138 118.805 99.289  1.00 51.27  ? 431 GLU A OE2 1 
ATOM   2787 N  N   . ASP A 1 434 ? 146.037 119.441 99.059  1.00 48.68  ? 432 ASP A N   1 
ATOM   2788 C  CA  . ASP A 1 434 ? 147.450 119.095 99.107  1.00 46.20  ? 432 ASP A CA  1 
ATOM   2789 C  C   . ASP A 1 434 ? 147.849 118.436 100.419 1.00 45.53  ? 432 ASP A C   1 
ATOM   2790 O  O   . ASP A 1 434 ? 148.989 117.978 100.540 1.00 48.07  ? 432 ASP A O   1 
ATOM   2791 C  CB  . ASP A 1 434 ? 148.310 120.339 98.876  1.00 45.35  ? 432 ASP A CB  1 
ATOM   2792 C  CG  . ASP A 1 434 ? 148.629 120.566 97.410  1.00 49.38  ? 432 ASP A CG  1 
ATOM   2793 O  OD1 . ASP A 1 434 ? 148.487 119.620 96.608  1.00 46.15  ? 432 ASP A OD1 1 
ATOM   2794 O  OD2 . ASP A 1 434 ? 149.040 121.690 97.059  1.00 51.36  ? 432 ASP A OD2 1 
ATOM   2795 N  N   . VAL A 1 435 ? 146.946 118.376 101.399 1.00 45.86  ? 433 VAL A N   1 
ATOM   2796 C  CA  . VAL A 1 435 ? 147.195 117.614 102.610 1.00 45.47  ? 433 VAL A CA  1 
ATOM   2797 C  C   . VAL A 1 435 ? 147.328 116.127 102.324 1.00 45.49  ? 433 VAL A C   1 
ATOM   2798 O  O   . VAL A 1 435 ? 147.787 115.375 103.187 1.00 49.25  ? 433 VAL A O   1 
ATOM   2799 C  CB  . VAL A 1 435 ? 146.070 117.865 103.639 1.00 45.39  ? 433 VAL A CB  1 
ATOM   2800 C  CG1 . VAL A 1 435 ? 146.359 117.141 104.942 1.00 44.97  ? 433 VAL A CG1 1 
ATOM   2801 C  CG2 . VAL A 1 435 ? 145.903 119.351 103.884 1.00 47.24  ? 433 VAL A CG2 1 
ATOM   2802 N  N   . THR A 1 436 ? 146.939 115.684 101.131 1.00 45.46  ? 434 THR A N   1 
ATOM   2803 C  CA  . THR A 1 436 ? 147.097 114.292 100.735 1.00 45.15  ? 434 THR A CA  1 
ATOM   2804 C  C   . THR A 1 436 ? 148.477 113.990 100.167 1.00 43.96  ? 434 THR A C   1 
ATOM   2805 O  O   . THR A 1 436 ? 148.762 112.825 99.871  1.00 46.80  ? 434 THR A O   1 
ATOM   2806 C  CB  . THR A 1 436 ? 146.031 113.903 99.706  1.00 47.73  ? 434 THR A CB  1 
ATOM   2807 O  OG1 . THR A 1 436 ? 146.505 114.198 98.386  1.00 47.69  ? 434 THR A OG1 1 
ATOM   2808 C  CG2 . THR A 1 436 ? 144.724 114.636 99.969  1.00 46.01  ? 434 THR A CG2 1 
ATOM   2809 N  N   . LEU A 1 437 ? 149.332 114.999 100.000 1.00 44.90  ? 435 LEU A N   1 
ATOM   2810 C  CA  . LEU A 1 437 ? 150.710 114.754 99.597  1.00 46.30  ? 435 LEU A CA  1 
ATOM   2811 C  C   . LEU A 1 437 ? 151.564 114.235 100.743 1.00 46.43  ? 435 LEU A C   1 
ATOM   2812 O  O   . LEU A 1 437 ? 152.649 113.698 100.495 1.00 47.66  ? 435 LEU A O   1 
ATOM   2813 C  CB  . LEU A 1 437 ? 151.336 116.037 99.046  1.00 44.49  ? 435 LEU A CB  1 
ATOM   2814 C  CG  . LEU A 1 437 ? 150.845 116.525 97.683  1.00 45.79  ? 435 LEU A CG  1 
ATOM   2815 C  CD1 . LEU A 1 437 ? 151.413 117.902 97.386  1.00 50.77  ? 435 LEU A CD1 1 
ATOM   2816 C  CD2 . LEU A 1 437 ? 151.221 115.545 96.588  1.00 44.72  ? 435 LEU A CD2 1 
ATOM   2817 N  N   . ILE A 1 438 ? 151.104 114.387 101.984 1.00 47.37  ? 436 ILE A N   1 
ATOM   2818 C  CA  . ILE A 1 438 ? 151.865 113.980 103.158 1.00 44.81  ? 436 ILE A CA  1 
ATOM   2819 C  C   . ILE A 1 438 ? 150.991 113.165 104.102 1.00 45.33  ? 436 ILE A C   1 
ATOM   2820 O  O   . ILE A 1 438 ? 151.342 112.969 105.270 1.00 48.82  ? 436 ILE A O   1 
ATOM   2821 C  CB  . ILE A 1 438 ? 152.442 115.209 103.878 1.00 43.12  ? 436 ILE A CB  1 
ATOM   2822 C  CG1 . ILE A 1 438 ? 151.335 116.227 104.143 1.00 41.25  ? 436 ILE A CG1 1 
ATOM   2823 C  CG2 . ILE A 1 438 ? 153.542 115.838 103.051 1.00 44.87  ? 436 ILE A CG2 1 
ATOM   2824 C  CD1 . ILE A 1 438 ? 151.666 117.188 105.234 1.00 45.56  ? 436 ILE A CD1 1 
ATOM   2825 N  N   . ILE A 1 439 ? 149.843 112.693 103.612 1.00 44.66  ? 437 ILE A N   1 
ATOM   2826 C  CA  . ILE A 1 439 ? 148.932 111.935 104.464 1.00 43.79  ? 437 ILE A CA  1 
ATOM   2827 C  C   . ILE A 1 439 ? 149.384 110.491 104.648 1.00 39.59  ? 437 ILE A C   1 
ATOM   2828 O  O   . ILE A 1 439 ? 148.985 109.845 105.624 1.00 41.06  ? 437 ILE A O   1 
ATOM   2829 C  CB  . ILE A 1 439 ? 147.506 111.988 103.886 1.00 42.34  ? 437 ILE A CB  1 
ATOM   2830 C  CG1 . ILE A 1 439 ? 146.490 111.394 104.864 1.00 44.57  ? 437 ILE A CG1 1 
ATOM   2831 C  CG2 . ILE A 1 439 ? 147.433 111.245 102.562 1.00 46.73  ? 437 ILE A CG2 1 
ATOM   2832 C  CD1 . ILE A 1 439 ? 146.257 112.242 106.088 1.00 42.00  ? 437 ILE A CD1 1 
ATOM   2833 N  N   . ALA A 1 440 ? 150.220 109.971 103.748 1.00 40.27  ? 438 ALA A N   1 
ATOM   2834 C  CA  . ALA A 1 440 ? 150.604 108.564 103.818 1.00 40.60  ? 438 ALA A CA  1 
ATOM   2835 C  C   . ALA A 1 440 ? 151.363 108.253 105.101 1.00 45.47  ? 438 ALA A C   1 
ATOM   2836 O  O   . ALA A 1 440 ? 151.143 107.207 105.722 1.00 48.37  ? 438 ALA A O   1 
ATOM   2837 C  CB  . ALA A 1 440 ? 151.444 108.193 102.598 1.00 40.97  ? 438 ALA A CB  1 
ATOM   2838 N  N   . VAL A 1 441 ? 152.264 109.145 105.513 1.00 47.02  ? 439 VAL A N   1 
ATOM   2839 C  CA  . VAL A 1 441 ? 153.124 108.905 106.667 1.00 41.13  ? 439 VAL A CA  1 
ATOM   2840 C  C   . VAL A 1 441 ? 152.656 109.671 107.898 1.00 40.23  ? 439 VAL A C   1 
ATOM   2841 O  O   . VAL A 1 441 ? 153.402 109.779 108.874 1.00 45.24  ? 439 VAL A O   1 
ATOM   2842 C  CB  . VAL A 1 441 ? 154.586 109.247 106.342 1.00 40.43  ? 439 VAL A CB  1 
ATOM   2843 C  CG1 . VAL A 1 441 ? 155.092 108.378 105.203 1.00 44.79  ? 439 VAL A CG1 1 
ATOM   2844 C  CG2 . VAL A 1 441 ? 154.731 110.724 105.999 1.00 44.84  ? 439 VAL A CG2 1 
ATOM   2845 N  N   . ASP A 1 442 ? 151.431 110.199 107.882 1.00 38.57  ? 440 ASP A N   1 
ATOM   2846 C  CA  . ASP A 1 442 ? 150.967 111.011 109.000 1.00 37.24  ? 440 ASP A CA  1 
ATOM   2847 C  C   . ASP A 1 442 ? 150.790 110.187 110.269 1.00 41.39  ? 440 ASP A C   1 
ATOM   2848 O  O   . ASP A 1 442 ? 150.975 110.711 111.372 1.00 44.03  ? 440 ASP A O   1 
ATOM   2849 C  CB  . ASP A 1 442 ? 149.655 111.702 108.640 1.00 37.42  ? 440 ASP A CB  1 
ATOM   2850 C  CG  . ASP A 1 442 ? 149.223 112.701 109.688 1.00 41.65  ? 440 ASP A CG  1 
ATOM   2851 O  OD1 . ASP A 1 442 ? 149.736 113.838 109.671 1.00 46.00  ? 440 ASP A OD1 1 
ATOM   2852 O  OD2 . ASP A 1 442 ? 148.376 112.350 110.534 1.00 40.95  ? 440 ASP A OD2 1 
ATOM   2853 N  N   . CYS A 1 443 ? 150.423 108.911 110.142 1.00 47.00  ? 441 CYS A N   1 
ATOM   2854 C  CA  . CYS A 1 443 ? 150.232 108.086 111.331 1.00 43.92  ? 441 CYS A CA  1 
ATOM   2855 C  C   . CYS A 1 443 ? 151.517 107.988 112.141 1.00 41.79  ? 441 CYS A C   1 
ATOM   2856 O  O   . CYS A 1 443 ? 151.490 108.075 113.374 1.00 45.82  ? 441 CYS A O   1 
ATOM   2857 C  CB  . CYS A 1 443 ? 149.747 106.694 110.934 1.00 46.39  ? 441 CYS A CB  1 
ATOM   2858 S  SG  . CYS A 1 443 ? 148.111 106.666 110.166 1.00 58.20  ? 441 CYS A SG  1 
ATOM   2859 N  N   . LEU A 1 444 ? 152.652 107.791 111.469 1.00 35.10  ? 442 LEU A N   1 
ATOM   2860 C  CA  . LEU A 1 444 ? 153.929 107.766 112.173 1.00 36.45  ? 442 LEU A CA  1 
ATOM   2861 C  C   . LEU A 1 444 ? 154.268 109.139 112.739 1.00 38.21  ? 442 LEU A C   1 
ATOM   2862 O  O   . LEU A 1 444 ? 154.578 109.272 113.928 1.00 41.96  ? 442 LEU A O   1 
ATOM   2863 C  CB  . LEU A 1 444 ? 155.031 107.281 111.231 1.00 37.40  ? 442 LEU A CB  1 
ATOM   2864 C  CG  . LEU A 1 444 ? 156.458 107.275 111.784 1.00 39.04  ? 442 LEU A CG  1 
ATOM   2865 C  CD1 . LEU A 1 444 ? 156.743 105.977 112.514 1.00 41.56  ? 442 LEU A CD1 1 
ATOM   2866 C  CD2 . LEU A 1 444 ? 157.458 107.492 110.663 1.00 41.66  ? 442 LEU A CD2 1 
ATOM   2867 N  N   . LEU A 1 445 ? 154.206 110.177 111.902 1.00 33.22  ? 443 LEU A N   1 
ATOM   2868 C  CA  . LEU A 1 445 ? 154.557 111.516 112.357 1.00 33.64  ? 443 LEU A CA  1 
ATOM   2869 C  C   . LEU A 1 445 ? 153.565 112.054 113.375 1.00 38.26  ? 443 LEU A C   1 
ATOM   2870 O  O   . LEU A 1 445 ? 153.930 112.917 114.179 1.00 46.41  ? 443 LEU A O   1 
ATOM   2871 C  CB  . LEU A 1 445 ? 154.649 112.468 111.165 1.00 37.41  ? 443 LEU A CB  1 
ATOM   2872 C  CG  . LEU A 1 445 ? 155.763 112.161 110.161 1.00 43.05  ? 443 LEU A CG  1 
ATOM   2873 C  CD1 . LEU A 1 445 ? 155.711 113.127 108.993 1.00 39.70  ? 443 LEU A CD1 1 
ATOM   2874 C  CD2 . LEU A 1 445 ? 157.129 112.201 110.832 1.00 41.38  ? 443 LEU A CD2 1 
ATOM   2875 N  N   . ASP A 1 446 ? 152.322 111.572 113.354 1.00 37.60  ? 444 ASP A N   1 
ATOM   2876 C  CA  . ASP A 1 446 ? 151.358 111.965 114.373 1.00 29.23  ? 444 ASP A CA  1 
ATOM   2877 C  C   . ASP A 1 446 ? 151.707 111.369 115.728 1.00 35.47  ? 444 ASP A C   1 
ATOM   2878 O  O   . ASP A 1 446 ? 151.478 112.004 116.762 1.00 36.73  ? 444 ASP A O   1 
ATOM   2879 C  CB  . ASP A 1 446 ? 149.957 111.534 113.950 1.00 37.52  ? 444 ASP A CB  1 
ATOM   2880 C  CG  . ASP A 1 446 ? 148.932 111.753 115.033 1.00 45.44  ? 444 ASP A CG  1 
ATOM   2881 O  OD1 . ASP A 1 446 ? 148.946 112.832 115.660 1.00 41.80  ? 444 ASP A OD1 1 
ATOM   2882 O  OD2 . ASP A 1 446 ? 148.102 110.849 115.255 1.00 44.59  ? 444 ASP A OD2 1 
ATOM   2883 N  N   . ARG A 1 447 ? 152.254 110.153 115.740 1.00 41.38  ? 445 ARG A N   1 
ATOM   2884 C  CA  . ARG A 1 447 ? 152.652 109.528 116.995 1.00 34.86  ? 445 ARG A CA  1 
ATOM   2885 C  C   . ARG A 1 447 ? 153.712 110.355 117.708 1.00 36.99  ? 445 ARG A C   1 
ATOM   2886 O  O   . ARG A 1 447 ? 153.639 110.560 118.924 1.00 37.01  ? 445 ARG A O   1 
ATOM   2887 C  CB  . ARG A 1 447 ? 153.173 108.116 116.725 1.00 38.51  ? 445 ARG A CB  1 
ATOM   2888 C  CG  . ARG A 1 447 ? 152.271 107.001 117.216 1.00 38.28  ? 445 ARG A CG  1 
ATOM   2889 C  CD  . ARG A 1 447 ? 151.239 106.605 116.184 1.00 38.93  ? 445 ARG A CD  1 
ATOM   2890 N  NE  . ARG A 1 447 ? 150.167 105.819 116.779 1.00 39.22  ? 445 ARG A NE  1 
ATOM   2891 C  CZ  . ARG A 1 447 ? 148.991 105.600 116.208 1.00 44.38  ? 445 ARG A CZ  1 
ATOM   2892 N  NH1 . ARG A 1 447 ? 148.700 106.088 115.014 1.00 43.62  ? 445 ARG A NH1 1 
ATOM   2893 N  NH2 . ARG A 1 447 ? 148.081 104.877 116.855 1.00 45.43  ? 445 ARG A NH2 1 
ATOM   2894 N  N   . PHE A 1 448 ? 154.713 110.829 116.965 1.00 39.35  ? 446 PHE A N   1 
ATOM   2895 C  CA  . PHE A 1 448 ? 155.788 111.611 117.561 1.00 31.36  ? 446 PHE A CA  1 
ATOM   2896 C  C   . PHE A 1 448 ? 155.365 113.045 117.842 1.00 32.85  ? 446 PHE A C   1 
ATOM   2897 O  O   . PHE A 1 448 ? 155.919 113.681 118.744 1.00 41.89  ? 446 PHE A O   1 
ATOM   2898 C  CB  . PHE A 1 448 ? 157.011 111.578 116.649 1.00 37.63  ? 446 PHE A CB  1 
ATOM   2899 C  CG  . PHE A 1 448 ? 157.651 110.226 116.560 1.00 38.65  ? 446 PHE A CG  1 
ATOM   2900 C  CD1 . PHE A 1 448 ? 158.539 109.803 117.530 1.00 41.86  ? 446 PHE A CD1 1 
ATOM   2901 C  CD2 . PHE A 1 448 ? 157.351 109.371 115.516 1.00 41.02  ? 446 PHE A CD2 1 
ATOM   2902 C  CE1 . PHE A 1 448 ? 159.122 108.557 117.456 1.00 38.34  ? 446 PHE A CE1 1 
ATOM   2903 C  CE2 . PHE A 1 448 ? 157.932 108.124 115.438 1.00 40.19  ? 446 PHE A CE2 1 
ATOM   2904 C  CZ  . PHE A 1 448 ? 158.817 107.717 116.408 1.00 38.91  ? 446 PHE A CZ  1 
ATOM   2905 N  N   . ARG A 1 449 ? 154.400 113.569 117.087 1.00 34.41  ? 447 ARG A N   1 
ATOM   2906 C  CA  . ARG A 1 449 ? 153.842 114.880 117.400 1.00 30.40  ? 447 ARG A CA  1 
ATOM   2907 C  C   . ARG A 1 449 ? 153.276 114.904 118.811 1.00 35.78  ? 447 ARG A C   1 
ATOM   2908 O  O   . ARG A 1 449 ? 153.567 115.810 119.599 1.00 40.71  ? 447 ARG A O   1 
ATOM   2909 C  CB  . ARG A 1 449 ? 152.742 115.229 116.401 1.00 32.53  ? 447 ARG A CB  1 
ATOM   2910 C  CG  . ARG A 1 449 ? 153.163 116.120 115.271 1.00 38.51  ? 447 ARG A CG  1 
ATOM   2911 C  CD  . ARG A 1 449 ? 151.952 116.534 114.463 1.00 37.29  ? 447 ARG A CD  1 
ATOM   2912 N  NE  . ARG A 1 449 ? 151.649 115.583 113.401 1.00 38.77  ? 447 ARG A NE  1 
ATOM   2913 C  CZ  . ARG A 1 449 ? 150.437 115.130 113.110 1.00 42.90  ? 447 ARG A CZ  1 
ATOM   2914 N  NH1 . ARG A 1 449 ? 149.371 115.497 113.802 1.00 37.12  ? 447 ARG A NH1 1 
ATOM   2915 N  NH2 . ARG A 1 449 ? 150.289 114.288 112.092 1.00 45.35  ? 447 ARG A NH2 1 
ATOM   2916 N  N   . THR A 1 450 ? 152.456 113.906 119.144 1.00 35.56  ? 448 THR A N   1 
ATOM   2917 C  CA  . THR A 1 450 ? 151.792 113.883 120.441 1.00 32.09  ? 448 THR A CA  1 
ATOM   2918 C  C   . THR A 1 450 ? 152.801 113.790 121.575 1.00 34.56  ? 448 THR A C   1 
ATOM   2919 O  O   . THR A 1 450 ? 152.630 114.422 122.622 1.00 33.27  ? 448 THR A O   1 
ATOM   2920 C  CB  . THR A 1 450 ? 150.817 112.710 120.502 1.00 32.48  ? 448 THR A CB  1 
ATOM   2921 O  OG1 . THR A 1 450 ? 150.101 112.624 119.266 1.00 36.82  ? 448 THR A OG1 1 
ATOM   2922 C  CG2 . THR A 1 450 ? 149.838 112.889 121.645 1.00 38.12  ? 448 THR A CG2 1 
ATOM   2923 N  N   . MET A 1 451 ? 153.856 112.997 121.388 1.00 33.42  ? 449 MET A N   1 
ATOM   2924 C  CA  . MET A 1 451 ? 154.871 112.869 122.425 1.00 32.87  ? 449 MET A CA  1 
ATOM   2925 C  C   . MET A 1 451 ? 155.493 114.221 122.748 1.00 38.85  ? 449 MET A C   1 
ATOM   2926 O  O   . MET A 1 451 ? 155.675 114.565 123.921 1.00 44.63  ? 449 MET A O   1 
ATOM   2927 C  CB  . MET A 1 451 ? 155.940 111.873 121.978 1.00 33.07  ? 449 MET A CB  1 
ATOM   2928 C  CG  . MET A 1 451 ? 156.831 111.374 123.092 1.00 37.76  ? 449 MET A CG  1 
ATOM   2929 S  SD  . MET A 1 451 ? 158.570 111.382 122.628 1.00 59.67  ? 449 MET A SD  1 
ATOM   2930 C  CE  . MET A 1 451 ? 158.989 113.095 122.934 1.00 43.27  ? 449 MET A CE  1 
ATOM   2931 N  N   . VAL A 1 452 ? 155.824 115.004 121.719 1.00 30.78  ? 450 VAL A N   1 
ATOM   2932 C  CA  . VAL A 1 452 ? 156.372 116.335 121.952 1.00 31.93  ? 450 VAL A CA  1 
ATOM   2933 C  C   . VAL A 1 452 ? 155.298 117.279 122.479 1.00 34.07  ? 450 VAL A C   1 
ATOM   2934 O  O   . VAL A 1 452 ? 155.593 118.179 123.274 1.00 41.84  ? 450 VAL A O   1 
ATOM   2935 C  CB  . VAL A 1 452 ? 157.020 116.880 120.666 1.00 35.74  ? 450 VAL A CB  1 
ATOM   2936 C  CG1 . VAL A 1 452 ? 157.740 118.187 120.946 1.00 32.90  ? 450 VAL A CG1 1 
ATOM   2937 C  CG2 . VAL A 1 452 ? 157.979 115.860 120.088 1.00 36.30  ? 450 VAL A CG2 1 
ATOM   2938 N  N   . ASN A 1 453 ? 154.048 117.108 122.044 1.00 31.34  ? 451 ASN A N   1 
ATOM   2939 C  CA  . ASN A 1 453 ? 152.973 117.961 122.542 1.00 25.48  ? 451 ASN A CA  1 
ATOM   2940 C  C   . ASN A 1 453 ? 152.780 117.789 124.042 1.00 33.62  ? 451 ASN A C   1 
ATOM   2941 O  O   . ASN A 1 453 ? 152.625 118.775 124.771 1.00 38.41  ? 451 ASN A O   1 
ATOM   2942 C  CB  . ASN A 1 453 ? 151.670 117.653 121.807 1.00 27.27  ? 451 ASN A CB  1 
ATOM   2943 C  CG  . ASN A 1 453 ? 151.671 118.156 120.385 1.00 28.39  ? 451 ASN A CG  1 
ATOM   2944 O  OD1 . ASN A 1 453 ? 152.507 118.969 120.006 1.00 38.15  ? 451 ASN A OD1 1 
ATOM   2945 N  ND2 . ASN A 1 453 ? 150.729 117.677 119.588 1.00 26.45  ? 451 ASN A ND2 1 
ATOM   2946 N  N   . VAL A 1 454 ? 152.781 116.545 124.523 1.00 31.21  ? 452 VAL A N   1 
ATOM   2947 C  CA  . VAL A 1 454 ? 152.590 116.313 125.950 1.00 29.78  ? 452 VAL A CA  1 
ATOM   2948 C  C   . VAL A 1 454 ? 153.879 116.564 126.720 1.00 35.87  ? 452 VAL A C   1 
ATOM   2949 O  O   . VAL A 1 454 ? 153.837 116.945 127.894 1.00 40.20  ? 452 VAL A O   1 
ATOM   2950 C  CB  . VAL A 1 454 ? 152.056 114.892 126.203 1.00 32.81  ? 452 VAL A CB  1 
ATOM   2951 C  CG1 . VAL A 1 454 ? 150.805 114.639 125.380 1.00 37.45  ? 452 VAL A CG1 1 
ATOM   2952 C  CG2 . VAL A 1 454 ? 153.118 113.851 125.901 1.00 33.92  ? 452 VAL A CG2 1 
ATOM   2953 N  N   . LEU A 1 455 ? 155.037 116.355 126.091 1.00 36.94  ? 453 LEU A N   1 
ATOM   2954 C  CA  . LEU A 1 455 ? 156.298 116.667 126.753 1.00 29.72  ? 453 LEU A CA  1 
ATOM   2955 C  C   . LEU A 1 455 ? 156.401 118.156 127.050 1.00 35.47  ? 453 LEU A C   1 
ATOM   2956 O  O   . LEU A 1 455 ? 156.912 118.553 128.103 1.00 38.94  ? 453 LEU A O   1 
ATOM   2957 C  CB  . LEU A 1 455 ? 157.474 116.210 125.892 1.00 35.42  ? 453 LEU A CB  1 
ATOM   2958 C  CG  . LEU A 1 455 ? 158.865 116.422 126.493 1.00 35.56  ? 453 LEU A CG  1 
ATOM   2959 C  CD1 . LEU A 1 455 ? 159.097 115.502 127.676 1.00 34.05  ? 453 LEU A CD1 1 
ATOM   2960 C  CD2 . LEU A 1 455 ? 159.932 116.211 125.439 1.00 35.69  ? 453 LEU A CD2 1 
ATOM   2961 N  N   . GLY A 1 456 ? 155.930 118.997 126.129 1.00 39.01  ? 454 GLY A N   1 
ATOM   2962 C  CA  . GLY A 1 456 ? 155.923 120.426 126.390 1.00 37.27  ? 454 GLY A CA  1 
ATOM   2963 C  C   . GLY A 1 456 ? 155.105 120.787 127.614 1.00 37.15  ? 454 GLY A C   1 
ATOM   2964 O  O   . GLY A 1 456 ? 155.538 121.586 128.446 1.00 40.33  ? 454 GLY A O   1 
ATOM   2965 N  N   . ASP A 1 457 ? 153.913 120.200 127.742 1.00 40.13  ? 455 ASP A N   1 
ATOM   2966 C  CA  . ASP A 1 457 ? 153.087 120.459 128.917 1.00 38.01  ? 455 ASP A CA  1 
ATOM   2967 C  C   . ASP A 1 457 ? 153.769 119.967 130.186 1.00 35.51  ? 455 ASP A C   1 
ATOM   2968 O  O   . ASP A 1 457 ? 153.758 120.654 131.213 1.00 32.81  ? 455 ASP A O   1 
ATOM   2969 C  CB  . ASP A 1 457 ? 151.721 119.790 128.764 1.00 38.05  ? 455 ASP A CB  1 
ATOM   2970 C  CG  . ASP A 1 457 ? 151.100 120.038 127.410 1.00 40.34  ? 455 ASP A CG  1 
ATOM   2971 O  OD1 . ASP A 1 457 ? 151.460 121.043 126.769 1.00 39.26  ? 455 ASP A OD1 1 
ATOM   2972 O  OD2 . ASP A 1 457 ? 150.250 119.227 126.986 1.00 44.18  ? 455 ASP A OD2 1 
ATOM   2973 N  N   . ALA A 1 458 ? 154.363 118.774 130.136 1.00 39.74  ? 456 ALA A N   1 
ATOM   2974 C  CA  . ALA A 1 458 ? 154.999 118.217 131.323 1.00 37.95  ? 456 ALA A CA  1 
ATOM   2975 C  C   . ALA A 1 458 ? 156.158 119.086 131.788 1.00 37.20  ? 456 ALA A C   1 
ATOM   2976 O  O   . ALA A 1 458 ? 156.301 119.352 132.986 1.00 37.92  ? 456 ALA A O   1 
ATOM   2977 C  CB  . ALA A 1 458 ? 155.475 116.794 131.039 1.00 37.40  ? 456 ALA A CB  1 
ATOM   2978 N  N   . PHE A 1 459 ? 157.003 119.533 130.856 1.00 44.55  ? 457 PHE A N   1 
ATOM   2979 C  CA  . PHE A 1 459 ? 158.099 120.421 131.227 1.00 39.12  ? 457 PHE A CA  1 
ATOM   2980 C  C   . PHE A 1 459 ? 157.573 121.762 131.719 1.00 37.93  ? 457 PHE A C   1 
ATOM   2981 O  O   . PHE A 1 459 ? 158.079 122.310 132.703 1.00 42.36  ? 457 PHE A O   1 
ATOM   2982 C  CB  . PHE A 1 459 ? 159.043 120.621 130.040 1.00 39.13  ? 457 PHE A CB  1 
ATOM   2983 C  CG  . PHE A 1 459 ? 160.182 119.639 129.988 1.00 31.41  ? 457 PHE A CG  1 
ATOM   2984 C  CD1 . PHE A 1 459 ? 160.951 119.379 131.108 1.00 34.14  ? 457 PHE A CD1 1 
ATOM   2985 C  CD2 . PHE A 1 459 ? 160.489 118.984 128.811 1.00 35.73  ? 457 PHE A CD2 1 
ATOM   2986 C  CE1 . PHE A 1 459 ? 161.993 118.481 131.055 1.00 36.13  ? 457 PHE A CE1 1 
ATOM   2987 C  CE2 . PHE A 1 459 ? 161.534 118.086 128.755 1.00 40.47  ? 457 PHE A CE2 1 
ATOM   2988 C  CZ  . PHE A 1 459 ? 162.285 117.836 129.880 1.00 36.17  ? 457 PHE A CZ  1 
ATOM   2989 N  N   . GLY A 1 460 ? 156.558 122.306 131.045 1.00 41.45  ? 458 GLY A N   1 
ATOM   2990 C  CA  . GLY A 1 460 ? 155.965 123.552 131.495 1.00 39.39  ? 458 GLY A CA  1 
ATOM   2991 C  C   . GLY A 1 460 ? 155.360 123.445 132.877 1.00 37.14  ? 458 GLY A C   1 
ATOM   2992 O  O   . GLY A 1 460 ? 155.339 124.421 133.628 1.00 41.79  ? 458 GLY A O   1 
ATOM   2993 N  N   . THR A 1 461 ? 154.858 122.262 133.230 1.00 44.74  ? 459 THR A N   1 
ATOM   2994 C  CA  . THR A 1 461 ? 154.332 122.056 134.573 1.00 41.04  ? 459 THR A CA  1 
ATOM   2995 C  C   . THR A 1 461 ? 155.416 122.280 135.619 1.00 38.86  ? 459 THR A C   1 
ATOM   2996 O  O   . THR A 1 461 ? 155.175 122.927 136.644 1.00 42.78  ? 459 THR A O   1 
ATOM   2997 C  CB  . THR A 1 461 ? 153.741 120.649 134.683 1.00 42.72  ? 459 THR A CB  1 
ATOM   2998 O  OG1 . THR A 1 461 ? 152.667 120.505 133.747 1.00 41.55  ? 459 THR A OG1 1 
ATOM   2999 C  CG2 . THR A 1 461 ? 153.222 120.378 136.077 1.00 39.19  ? 459 THR A CG2 1 
ATOM   3000 N  N   . GLY A 1 462 ? 156.622 121.766 135.374 1.00 42.03  ? 460 GLY A N   1 
ATOM   3001 C  CA  . GLY A 1 462 ? 157.715 121.993 136.300 1.00 40.30  ? 460 GLY A CA  1 
ATOM   3002 C  C   . GLY A 1 462 ? 158.318 123.375 136.195 1.00 45.98  ? 460 GLY A C   1 
ATOM   3003 O  O   . GLY A 1 462 ? 158.845 123.898 137.181 1.00 46.58  ? 460 GLY A O   1 
ATOM   3004 N  N   . ILE A 1 463 ? 158.263 123.982 135.008 1.00 49.53  ? 461 ILE A N   1 
ATOM   3005 C  CA  . ILE A 1 463 ? 158.798 125.328 134.835 1.00 42.95  ? 461 ILE A CA  1 
ATOM   3006 C  C   . ILE A 1 463 ? 157.917 126.347 135.545 1.00 40.83  ? 461 ILE A C   1 
ATOM   3007 O  O   . ILE A 1 463 ? 158.415 127.240 136.238 1.00 45.41  ? 461 ILE A O   1 
ATOM   3008 C  CB  . ILE A 1 463 ? 158.944 125.646 133.335 1.00 45.79  ? 461 ILE A CB  1 
ATOM   3009 C  CG1 . ILE A 1 463 ? 160.236 125.038 132.790 1.00 45.09  ? 461 ILE A CG1 1 
ATOM   3010 C  CG2 . ILE A 1 463 ? 158.933 127.148 133.091 1.00 40.67  ? 461 ILE A CG2 1 
ATOM   3011 C  CD1 . ILE A 1 463 ? 160.170 124.696 131.322 1.00 42.12  ? 461 ILE A CD1 1 
ATOM   3012 N  N   . VAL A 1 464 ? 156.598 126.232 135.388 1.00 45.53  ? 462 VAL A N   1 
ATOM   3013 C  CA  . VAL A 1 464 ? 155.692 127.179 136.029 1.00 40.38  ? 462 VAL A CA  1 
ATOM   3014 C  C   . VAL A 1 464 ? 155.740 127.023 137.543 1.00 41.95  ? 462 VAL A C   1 
ATOM   3015 O  O   . VAL A 1 464 ? 155.659 128.008 138.284 1.00 47.49  ? 462 VAL A O   1 
ATOM   3016 C  CB  . VAL A 1 464 ? 154.263 126.999 135.489 1.00 35.04  ? 462 VAL A CB  1 
ATOM   3017 C  CG1 . VAL A 1 464 ? 153.283 127.831 136.295 1.00 41.49  ? 462 VAL A CG1 1 
ATOM   3018 C  CG2 . VAL A 1 464 ? 154.203 127.374 134.020 1.00 40.59  ? 462 VAL A CG2 1 
ATOM   3019 N  N   . GLU A 1 465 ? 155.869 125.787 138.026 1.00 41.14  ? 463 GLU A N   1 
ATOM   3020 C  CA  . GLU A 1 465 ? 155.925 125.561 139.465 1.00 42.56  ? 463 GLU A CA  1 
ATOM   3021 C  C   . GLU A 1 465 ? 157.129 126.256 140.085 1.00 43.16  ? 463 GLU A C   1 
ATOM   3022 O  O   . GLU A 1 465 ? 157.031 126.830 141.176 1.00 46.38  ? 463 GLU A O   1 
ATOM   3023 C  CB  . GLU A 1 465 ? 155.966 124.062 139.756 1.00 43.92  ? 463 GLU A CB  1 
ATOM   3024 C  CG  . GLU A 1 465 ? 155.450 123.692 141.134 1.00 46.35  ? 463 GLU A CG  1 
ATOM   3025 C  CD  . GLU A 1 465 ? 156.233 122.566 141.773 1.00 48.24  ? 463 GLU A CD  1 
ATOM   3026 O  OE1 . GLU A 1 465 ? 156.965 121.858 141.051 1.00 48.70  ? 463 GLU A OE1 1 
ATOM   3027 O  OE2 . GLU A 1 465 ? 156.113 122.384 143.002 1.00 48.14  ? 463 GLU A OE2 1 
ATOM   3028 N  N   . LYS A 1 466 ? 158.279 126.205 139.412 1.00 43.76  ? 464 LYS A N   1 
ATOM   3029 C  CA  . LYS A 1 466 ? 159.464 126.885 139.921 1.00 45.69  ? 464 LYS A CA  1 
ATOM   3030 C  C   . LYS A 1 466 ? 159.245 128.390 139.992 1.00 44.19  ? 464 LYS A C   1 
ATOM   3031 O  O   . LYS A 1 466 ? 159.598 129.030 140.989 1.00 51.03  ? 464 LYS A O   1 
ATOM   3032 C  CB  . LYS A 1 466 ? 160.670 126.556 139.039 1.00 45.03  ? 464 LYS A CB  1 
ATOM   3033 C  CG  . LYS A 1 466 ? 161.925 127.369 139.330 1.00 41.66  ? 464 LYS A CG  1 
ATOM   3034 C  CD  . LYS A 1 466 ? 162.496 127.050 140.700 1.00 42.96  ? 464 LYS A CD  1 
ATOM   3035 C  CE  . LYS A 1 466 ? 163.997 127.298 140.762 1.00 44.57  ? 464 LYS A CE  1 
ATOM   3036 N  NZ  . LYS A 1 466 ? 164.744 126.087 141.198 1.00 47.65  ? 464 LYS A NZ  1 
ATOM   3037 N  N   . LEU A 1 467 ? 158.659 128.974 138.946 1.00 36.37  ? 465 LEU A N   1 
ATOM   3038 C  CA  . LEU A 1 467 ? 158.450 130.415 138.921 1.00 42.72  ? 465 LEU A CA  1 
ATOM   3039 C  C   . LEU A 1 467 ? 157.384 130.864 139.910 1.00 45.68  ? 465 LEU A C   1 
ATOM   3040 O  O   . LEU A 1 467 ? 157.363 132.041 140.285 1.00 48.97  ? 465 LEU A O   1 
ATOM   3041 C  CB  . LEU A 1 467 ? 158.065 130.864 137.512 1.00 48.98  ? 465 LEU A CB  1 
ATOM   3042 C  CG  . LEU A 1 467 ? 159.073 130.561 136.401 1.00 45.83  ? 465 LEU A CG  1 
ATOM   3043 C  CD1 . LEU A 1 467 ? 158.553 131.070 135.070 1.00 42.46  ? 465 LEU A CD1 1 
ATOM   3044 C  CD2 . LEU A 1 467 ? 160.430 131.166 136.714 1.00 42.43  ? 465 LEU A CD2 1 
ATOM   3045 N  N   . SER A 1 468 ? 156.504 129.960 140.340 1.00 47.29  ? 466 SER A N   1 
ATOM   3046 C  CA  . SER A 1 468 ? 155.397 130.291 141.227 1.00 45.52  ? 466 SER A CA  1 
ATOM   3047 C  C   . SER A 1 468 ? 155.668 129.886 142.672 1.00 46.03  ? 466 SER A C   1 
ATOM   3048 O  O   . SER A 1 468 ? 154.728 129.638 143.431 1.00 50.43  ? 466 SER A O   1 
ATOM   3049 C  CB  . SER A 1 468 ? 154.113 129.631 140.727 1.00 43.11  ? 466 SER A CB  1 
ATOM   3050 O  OG  . SER A 1 468 ? 153.874 129.947 139.369 1.00 42.99  ? 466 SER A OG  1 
ATOM   3051 N  N   . LYS A 1 469 ? 156.939 129.820 143.071 1.00 45.33  ? 467 LYS A N   1 
ATOM   3052 C  CA  . LYS A 1 469 ? 157.256 129.429 144.441 1.00 49.16  ? 467 LYS A CA  1 
ATOM   3053 C  C   . LYS A 1 469 ? 156.689 130.427 145.441 1.00 50.67  ? 467 LYS A C   1 
ATOM   3054 O  O   . LYS A 1 469 ? 156.210 130.039 146.513 1.00 47.95  ? 467 LYS A O   1 
ATOM   3055 C  CB  . LYS A 1 469 ? 158.769 129.300 144.613 1.00 47.71  ? 467 LYS A CB  1 
ATOM   3056 C  CG  . LYS A 1 469 ? 159.246 129.468 146.049 1.00 48.41  ? 467 LYS A CG  1 
ATOM   3057 C  CD  . LYS A 1 469 ? 160.622 128.850 146.255 1.00 50.44  ? 467 LYS A CD  1 
ATOM   3058 C  CE  . LYS A 1 469 ? 160.538 127.443 146.836 1.00 49.94  ? 467 LYS A CE  1 
ATOM   3059 N  NZ  . LYS A 1 469 ? 161.721 127.120 147.680 1.00 48.40  ? 467 LYS A NZ  1 
ATOM   3060 N  N   . LYS A 1 470 ? 156.737 131.718 145.111 1.00 51.90  ? 468 LYS A N   1 
ATOM   3061 C  CA  . LYS A 1 470 ? 156.256 132.737 146.037 1.00 52.39  ? 468 LYS A CA  1 
ATOM   3062 C  C   . LYS A 1 470 ? 154.768 132.573 146.321 1.00 49.73  ? 468 LYS A C   1 
ATOM   3063 O  O   . LYS A 1 470 ? 154.330 132.704 147.470 1.00 53.53  ? 468 LYS A O   1 
ATOM   3064 C  CB  . LYS A 1 470 ? 156.544 134.128 145.472 1.00 51.83  ? 468 LYS A CB  1 
ATOM   3065 C  CG  . LYS A 1 470 ? 156.471 135.248 146.510 1.00 52.12  ? 468 LYS A CG  1 
ATOM   3066 C  CD  . LYS A 1 470 ? 155.935 136.584 145.973 1.00 52.97  ? 468 LYS A CD  1 
ATOM   3067 C  CE  . LYS A 1 470 ? 154.562 136.493 145.305 1.00 54.53  ? 468 LYS A CE  1 
ATOM   3068 N  NZ  . LYS A 1 470 ? 154.246 137.735 144.547 1.00 51.75  ? 468 LYS A NZ  1 
ATOM   3069 N  N   . GLU A 1 471 ? 153.973 132.288 145.289 1.00 47.89  ? 469 GLU A N   1 
ATOM   3070 C  CA  . GLU A 1 471 ? 152.527 132.209 145.449 1.00 49.86  ? 469 GLU A CA  1 
ATOM   3071 C  C   . GLU A 1 471 ? 152.050 130.860 145.969 1.00 51.69  ? 469 GLU A C   1 
ATOM   3072 O  O   . GLU A 1 471 ? 150.905 130.759 146.420 1.00 51.86  ? 469 GLU A O   1 
ATOM   3073 C  CB  . GLU A 1 471 ? 151.847 132.506 144.116 1.00 48.34  ? 469 GLU A CB  1 
ATOM   3074 C  CG  . GLU A 1 471 ? 152.032 133.933 143.655 1.00 52.41  ? 469 GLU A CG  1 
ATOM   3075 C  CD  . GLU A 1 471 ? 152.072 134.050 142.153 1.00 54.75  ? 469 GLU A CD  1 
ATOM   3076 O  OE1 . GLU A 1 471 ? 151.033 133.796 141.512 1.00 51.91  ? 469 GLU A OE1 1 
ATOM   3077 O  OE2 . GLU A 1 471 ? 153.144 134.396 141.615 1.00 54.91  ? 469 GLU A OE2 1 
ATOM   3078 N  N   . LEU A 1 472 ? 152.889 129.832 145.924 1.00 48.91  ? 470 LEU A N   1 
ATOM   3079 C  CA  . LEU A 1 472 ? 152.496 128.514 146.405 1.00 47.45  ? 470 LEU A CA  1 
ATOM   3080 C  C   . LEU A 1 472 ? 152.908 128.339 147.862 1.00 50.66  ? 470 LEU A C   1 
ATOM   3081 O  O   . LEU A 1 472 ? 152.914 129.298 148.635 1.00 50.52  ? 470 LEU A O   1 
ATOM   3082 C  CB  . LEU A 1 472 ? 153.121 127.416 145.541 1.00 46.78  ? 470 LEU A CB  1 
ATOM   3083 C  CG  . LEU A 1 472 ? 152.673 127.367 144.078 1.00 46.49  ? 470 LEU A CG  1 
ATOM   3084 C  CD1 . LEU A 1 472 ? 153.497 126.348 143.314 1.00 47.11  ? 470 LEU A CD1 1 
ATOM   3085 C  CD2 . LEU A 1 472 ? 151.193 127.051 143.961 1.00 44.52  ? 470 LEU A CD2 1 
HETATM 3086 N  N   . CYS B 2 .   ? 147.669 114.302 117.544 1.00 33.83  ? 600 CYS A N   1 
HETATM 3087 C  CA  . CYS B 2 .   ? 148.213 115.472 118.220 1.00 34.20  ? 600 CYS A CA  1 
HETATM 3088 C  C   . CYS B 2 .   ? 147.872 115.445 119.702 1.00 34.10  ? 600 CYS A C   1 
HETATM 3089 O  O   . CYS B 2 .   ? 148.481 116.144 120.506 1.00 36.36  ? 600 CYS A O   1 
HETATM 3090 C  CB  . CYS B 2 .   ? 147.681 116.755 117.586 1.00 30.82  ? 600 CYS A CB  1 
HETATM 3091 S  SG  . CYS B 2 .   ? 148.110 116.957 115.850 1.00 45.21  ? 600 CYS A SG  1 
HETATM 3092 O  OXT . CYS B 2 .   ? 146.979 114.723 120.134 1.00 40.45  ? 600 CYS A OXT 1 
HETATM 3093 NA NA  . NA  C 3 .   ? 150.148 119.626 124.777 1.00 30.79  ? 601 NA  A NA  1 
HETATM 3094 NA NA  . NA  D 3 .   ? 145.984 122.475 119.884 1.00 37.30  ? 602 NA  A NA  1 
HETATM 3095 NA NA  . NA  E 3 .   ? 154.176 125.977 123.149 1.00 36.90  ? 603 NA  A NA  1 
HETATM 3096 HG HG  . HG  F 4 .   ? 150.098 104.858 109.733 1.00 178.71 ? 604 HG  A HG  1 
HETATM 3097 O  O   . HOH G 5 .   ? 149.335 117.487 128.073 1.00 37.69  ? 701 HOH A O   1 
HETATM 3098 O  O   . HOH G 5 .   ? 150.739 125.409 120.321 1.00 26.45  ? 702 HOH A O   1 
HETATM 3099 O  O   . HOH G 5 .   ? 141.076 118.115 130.769 1.00 36.77  ? 703 HOH A O   1 
HETATM 3100 O  O   . HOH G 5 .   ? 142.265 118.557 123.537 1.00 36.33  ? 704 HOH A O   1 
HETATM 3101 O  O   . HOH G 5 .   ? 142.488 119.047 127.873 1.00 35.13  ? 705 HOH A O   1 
HETATM 3102 O  O   . HOH G 5 .   ? 143.553 125.367 137.884 1.00 39.53  ? 706 HOH A O   1 
HETATM 3103 O  O   . HOH G 5 .   ? 154.005 121.275 123.584 1.00 37.87  ? 707 HOH A O   1 
HETATM 3104 O  O   . HOH G 5 .   ? 139.631 116.325 122.924 1.00 30.22  ? 708 HOH A O   1 
HETATM 3105 O  O   . HOH G 5 .   ? 140.528 121.101 133.835 1.00 32.48  ? 709 HOH A O   1 
# 
