data_8Z7V
# 
_entry.id   8Z7V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Z7V         pdb_00008z7v 10.2210/pdb8z7v/pdb 
WWPDB D_1300047112 ?            ?                   
EMDB  EMD-39829    ?            ?                   
# 
_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       2025-01-08 
# 
_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                        8Z7V 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Slc19A3-Amprolium outward structure' 
_pdbx_database_related.db_id          EMD-39829 
_pdbx_database_related.content_type   'associated EM volume' 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
4 qqh@fudan.edu.cn Qianhui Qu  ? 'principal investigator/group leader' 0000-0002-5753-2599 
5 gaopu@ibp.ac.cn  Pu      Gao ? 'principal investigator/group leader' 0000-0002-5328-9755 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, P.P.'  1 ? 
'Zhu, Z.N.' 2 ? 
'Wang, Y.'  3 ? 
'Gao, P.'   4 ? 
'Qu, Q.H.'  5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                10924 
_citation.page_last                 10924 
_citation.title                     'Substrate transport and drug interaction of human thiamine transporters SLC19A2/A3.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-024-55359-8 
_citation.pdbx_database_id_PubMed   39738067 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, P.'    1  ?                   
primary 'Zhu, Z.'   2  ?                   
primary 'Wang, Y.'  3  ?                   
primary 'Zhang, X.' 4  0000-0002-6305-1556 
primary 'Yang, C.'  5  ?                   
primary 'Zhu, Y.'   6  ?                   
primary 'Zhou, Z.'  7  ?                   
primary 'Chao, Y.'  8  ?                   
primary 'Long, Y.'  9  ?                   
primary 'Gao, Y.'   10 ?                   
primary 'Liu, S.'   11 ?                   
primary 'Zhang, L.' 12 0000-0002-9795-0314 
primary 'Gao, P.'   13 0000-0002-5328-9755 
primary 'Qu, Q.'    14 0000-0002-5753-2599 
# 
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 'Thiamine transporter 2' 55699.316 1 ? ? ? ? 
2 non-polymer syn Amprolium                243.327   1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ThTr-2,ThTr2,Solute carrier family 19 member 3' 
# 
_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       
;MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWTYSYLVLLLPVFVLTDYVRYK
PVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAEVAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQL
LVSLANMSYFYLNVISLASVSVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILST
SGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQILWDYKAPSQDSSIYNGAVE
AIATFGGAVAAFAVGYVKVNWDLLGELALVVFSVVNAGSLFLMHYTANIWACYAGYLIFKSSYMLLITIAVFQIAVNLNV
ERYALVFGINTFIALVIQTIMTVIVVDQRGLNLPVSIQFLVYGSYFAVIAGIFLMRSMYITYSTKSQKDVQSPAPSENPD
VSHPEEESNIIMSTKL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWTYSYLVLLLPVFVLTDYVRYK
PVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAEVAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQL
LVSLANMSYFYLNVISLASVSVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILST
SGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQILWDYKAPSQDSSIYNGAVE
AIATFGGAVAAFAVGYVKVNWDLLGELALVVFSVVNAGSLFLMHYTANIWACYAGYLIFKSSYMLLITIAVFQIAVNLNV
ERYALVFGINTFIALVIQTIMTVIVVDQRGLNLPVSIQFLVYGSYFAVIAGIFLMRSMYITYSTKSQKDVQSPAPSENPD
VSHPEEESNIIMSTKL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        Amprolium 
_pdbx_entity_nonpoly.comp_id     A1H5C 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   CYS n 
1 4   TYR n 
1 5   ARG n 
1 6   THR n 
1 7   SER n 
1 8   LEU n 
1 9   SER n 
1 10  SER n 
1 11  SER n 
1 12  TRP n 
1 13  ILE n 
1 14  TYR n 
1 15  PRO n 
1 16  THR n 
1 17  VAL n 
1 18  ILE n 
1 19  LEU n 
1 20  CYS n 
1 21  LEU n 
1 22  PHE n 
1 23  GLY n 
1 24  PHE n 
1 25  PHE n 
1 26  SER n 
1 27  MET n 
1 28  MET n 
1 29  ARG n 
1 30  PRO n 
1 31  SER n 
1 32  GLU n 
1 33  PRO n 
1 34  PHE n 
1 35  LEU n 
1 36  ILE n 
1 37  PRO n 
1 38  TYR n 
1 39  LEU n 
1 40  SER n 
1 41  GLY n 
1 42  PRO n 
1 43  ASP n 
1 44  LYS n 
1 45  ASN n 
1 46  LEU n 
1 47  THR n 
1 48  SER n 
1 49  ALA n 
1 50  GLU n 
1 51  ILE n 
1 52  THR n 
1 53  ASN n 
1 54  GLU n 
1 55  ILE n 
1 56  PHE n 
1 57  PRO n 
1 58  VAL n 
1 59  TRP n 
1 60  THR n 
1 61  TYR n 
1 62  SER n 
1 63  TYR n 
1 64  LEU n 
1 65  VAL n 
1 66  LEU n 
1 67  LEU n 
1 68  LEU n 
1 69  PRO n 
1 70  VAL n 
1 71  PHE n 
1 72  VAL n 
1 73  LEU n 
1 74  THR n 
1 75  ASP n 
1 76  TYR n 
1 77  VAL n 
1 78  ARG n 
1 79  TYR n 
1 80  LYS n 
1 81  PRO n 
1 82  VAL n 
1 83  ILE n 
1 84  ILE n 
1 85  LEU n 
1 86  GLN n 
1 87  GLY n 
1 88  ILE n 
1 89  SER n 
1 90  PHE n 
1 91  ILE n 
1 92  ILE n 
1 93  THR n 
1 94  TRP n 
1 95  LEU n 
1 96  LEU n 
1 97  LEU n 
1 98  LEU n 
1 99  PHE n 
1 100 GLY n 
1 101 GLN n 
1 102 GLY n 
1 103 VAL n 
1 104 LYS n 
1 105 THR n 
1 106 MET n 
1 107 GLN n 
1 108 VAL n 
1 109 VAL n 
1 110 GLU n 
1 111 PHE n 
1 112 PHE n 
1 113 TYR n 
1 114 GLY n 
1 115 MET n 
1 116 VAL n 
1 117 THR n 
1 118 ALA n 
1 119 ALA n 
1 120 GLU n 
1 121 VAL n 
1 122 ALA n 
1 123 TYR n 
1 124 TYR n 
1 125 ALA n 
1 126 TYR n 
1 127 ILE n 
1 128 TYR n 
1 129 SER n 
1 130 VAL n 
1 131 VAL n 
1 132 SER n 
1 133 PRO n 
1 134 GLU n 
1 135 HIS n 
1 136 TYR n 
1 137 GLN n 
1 138 ARG n 
1 139 VAL n 
1 140 SER n 
1 141 GLY n 
1 142 TYR n 
1 143 CYS n 
1 144 ARG n 
1 145 SER n 
1 146 VAL n 
1 147 THR n 
1 148 LEU n 
1 149 ALA n 
1 150 ALA n 
1 151 TYR n 
1 152 THR n 
1 153 ALA n 
1 154 GLY n 
1 155 SER n 
1 156 VAL n 
1 157 LEU n 
1 158 ALA n 
1 159 GLN n 
1 160 LEU n 
1 161 LEU n 
1 162 VAL n 
1 163 SER n 
1 164 LEU n 
1 165 ALA n 
1 166 ASN n 
1 167 MET n 
1 168 SER n 
1 169 TYR n 
1 170 PHE n 
1 171 TYR n 
1 172 LEU n 
1 173 ASN n 
1 174 VAL n 
1 175 ILE n 
1 176 SER n 
1 177 LEU n 
1 178 ALA n 
1 179 SER n 
1 180 VAL n 
1 181 SER n 
1 182 VAL n 
1 183 ALA n 
1 184 PHE n 
1 185 LEU n 
1 186 PHE n 
1 187 SER n 
1 188 LEU n 
1 189 PHE n 
1 190 LEU n 
1 191 PRO n 
1 192 MET n 
1 193 PRO n 
1 194 LYS n 
1 195 LYS n 
1 196 SER n 
1 197 MET n 
1 198 PHE n 
1 199 PHE n 
1 200 HIS n 
1 201 ALA n 
1 202 LYS n 
1 203 PRO n 
1 204 SER n 
1 205 ARG n 
1 206 GLU n 
1 207 ILE n 
1 208 LYS n 
1 209 LYS n 
1 210 SER n 
1 211 SER n 
1 212 SER n 
1 213 VAL n 
1 214 ASN n 
1 215 PRO n 
1 216 VAL n 
1 217 LEU n 
1 218 GLU n 
1 219 GLU n 
1 220 THR n 
1 221 HIS n 
1 222 GLU n 
1 223 GLY n 
1 224 GLU n 
1 225 ALA n 
1 226 PRO n 
1 227 GLY n 
1 228 CYS n 
1 229 GLU n 
1 230 GLU n 
1 231 GLN n 
1 232 LYS n 
1 233 PRO n 
1 234 THR n 
1 235 SER n 
1 236 GLU n 
1 237 ILE n 
1 238 LEU n 
1 239 SER n 
1 240 THR n 
1 241 SER n 
1 242 GLY n 
1 243 LYS n 
1 244 LEU n 
1 245 ASN n 
1 246 LYS n 
1 247 GLY n 
1 248 GLN n 
1 249 LEU n 
1 250 ASN n 
1 251 SER n 
1 252 LEU n 
1 253 LYS n 
1 254 PRO n 
1 255 SER n 
1 256 ASN n 
1 257 VAL n 
1 258 THR n 
1 259 VAL n 
1 260 ASP n 
1 261 VAL n 
1 262 PHE n 
1 263 VAL n 
1 264 GLN n 
1 265 TRP n 
1 266 PHE n 
1 267 GLN n 
1 268 ASP n 
1 269 LEU n 
1 270 LYS n 
1 271 GLU n 
1 272 CYS n 
1 273 TYR n 
1 274 SER n 
1 275 SER n 
1 276 LYS n 
1 277 ARG n 
1 278 LEU n 
1 279 PHE n 
1 280 TYR n 
1 281 TRP n 
1 282 SER n 
1 283 LEU n 
1 284 TRP n 
1 285 TRP n 
1 286 ALA n 
1 287 PHE n 
1 288 ALA n 
1 289 THR n 
1 290 ALA n 
1 291 GLY n 
1 292 PHE n 
1 293 ASN n 
1 294 GLN n 
1 295 VAL n 
1 296 LEU n 
1 297 ASN n 
1 298 TYR n 
1 299 VAL n 
1 300 GLN n 
1 301 ILE n 
1 302 LEU n 
1 303 TRP n 
1 304 ASP n 
1 305 TYR n 
1 306 LYS n 
1 307 ALA n 
1 308 PRO n 
1 309 SER n 
1 310 GLN n 
1 311 ASP n 
1 312 SER n 
1 313 SER n 
1 314 ILE n 
1 315 TYR n 
1 316 ASN n 
1 317 GLY n 
1 318 ALA n 
1 319 VAL n 
1 320 GLU n 
1 321 ALA n 
1 322 ILE n 
1 323 ALA n 
1 324 THR n 
1 325 PHE n 
1 326 GLY n 
1 327 GLY n 
1 328 ALA n 
1 329 VAL n 
1 330 ALA n 
1 331 ALA n 
1 332 PHE n 
1 333 ALA n 
1 334 VAL n 
1 335 GLY n 
1 336 TYR n 
1 337 VAL n 
1 338 LYS n 
1 339 VAL n 
1 340 ASN n 
1 341 TRP n 
1 342 ASP n 
1 343 LEU n 
1 344 LEU n 
1 345 GLY n 
1 346 GLU n 
1 347 LEU n 
1 348 ALA n 
1 349 LEU n 
1 350 VAL n 
1 351 VAL n 
1 352 PHE n 
1 353 SER n 
1 354 VAL n 
1 355 VAL n 
1 356 ASN n 
1 357 ALA n 
1 358 GLY n 
1 359 SER n 
1 360 LEU n 
1 361 PHE n 
1 362 LEU n 
1 363 MET n 
1 364 HIS n 
1 365 TYR n 
1 366 THR n 
1 367 ALA n 
1 368 ASN n 
1 369 ILE n 
1 370 TRP n 
1 371 ALA n 
1 372 CYS n 
1 373 TYR n 
1 374 ALA n 
1 375 GLY n 
1 376 TYR n 
1 377 LEU n 
1 378 ILE n 
1 379 PHE n 
1 380 LYS n 
1 381 SER n 
1 382 SER n 
1 383 TYR n 
1 384 MET n 
1 385 LEU n 
1 386 LEU n 
1 387 ILE n 
1 388 THR n 
1 389 ILE n 
1 390 ALA n 
1 391 VAL n 
1 392 PHE n 
1 393 GLN n 
1 394 ILE n 
1 395 ALA n 
1 396 VAL n 
1 397 ASN n 
1 398 LEU n 
1 399 ASN n 
1 400 VAL n 
1 401 GLU n 
1 402 ARG n 
1 403 TYR n 
1 404 ALA n 
1 405 LEU n 
1 406 VAL n 
1 407 PHE n 
1 408 GLY n 
1 409 ILE n 
1 410 ASN n 
1 411 THR n 
1 412 PHE n 
1 413 ILE n 
1 414 ALA n 
1 415 LEU n 
1 416 VAL n 
1 417 ILE n 
1 418 GLN n 
1 419 THR n 
1 420 ILE n 
1 421 MET n 
1 422 THR n 
1 423 VAL n 
1 424 ILE n 
1 425 VAL n 
1 426 VAL n 
1 427 ASP n 
1 428 GLN n 
1 429 ARG n 
1 430 GLY n 
1 431 LEU n 
1 432 ASN n 
1 433 LEU n 
1 434 PRO n 
1 435 VAL n 
1 436 SER n 
1 437 ILE n 
1 438 GLN n 
1 439 PHE n 
1 440 LEU n 
1 441 VAL n 
1 442 TYR n 
1 443 GLY n 
1 444 SER n 
1 445 TYR n 
1 446 PHE n 
1 447 ALA n 
1 448 VAL n 
1 449 ILE n 
1 450 ALA n 
1 451 GLY n 
1 452 ILE n 
1 453 PHE n 
1 454 LEU n 
1 455 MET n 
1 456 ARG n 
1 457 SER n 
1 458 MET n 
1 459 TYR n 
1 460 ILE n 
1 461 THR n 
1 462 TYR n 
1 463 SER n 
1 464 THR n 
1 465 LYS n 
1 466 SER n 
1 467 GLN n 
1 468 LYS n 
1 469 ASP n 
1 470 VAL n 
1 471 GLN n 
1 472 SER n 
1 473 PRO n 
1 474 ALA n 
1 475 PRO n 
1 476 SER n 
1 477 GLU n 
1 478 ASN n 
1 479 PRO n 
1 480 ASP n 
1 481 VAL n 
1 482 SER n 
1 483 HIS n 
1 484 PRO n 
1 485 GLU n 
1 486 GLU n 
1 487 GLU n 
1 488 SER n 
1 489 ASN n 
1 490 ILE n 
1 491 ILE n 
1 492 MET n 
1 493 SER n 
1 494 THR n 
1 495 LYS n 
1 496 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   496 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SLC19A3 
_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      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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 
A1H5C non-polymer         . Amprolium       '5-[(2-methylpyridin-1-ium-1-yl)methyl]-2-propyl-pyrimidin-4-amine' 'C14 H19 N4 1'   
243.327 
ALA   'L-peptide linking' y ALANINE         ?                                                                   'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE        ?                                                                   'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE      ?                                                                   'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                                                                   'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE        ?                                                                   'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE       ?                                                                   'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                                                                   'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE         ?                                                                   'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE       ?                                                                   'C6 H10 N3 O2 1' 
156.162 
ILE   'L-peptide linking' y ISOLEUCINE      ?                                                                   'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE         ?                                                                   'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE          ?                                                                   'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE      ?                                                                   'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE   ?                                                                   'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE         ?                                                                   'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE          ?                                                                   'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE       ?                                                                   'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN      ?                                                                   'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE        ?                                                                   'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE          ?                                                                   'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   CYS 3   3   ?   ?   ?   A . n 
A 1 4   TYR 4   4   ?   ?   ?   A . n 
A 1 5   ARG 5   5   ?   ?   ?   A . n 
A 1 6   THR 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   SER 9   9   ?   ?   ?   A . n 
A 1 10  SER 10  10  ?   ?   ?   A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  TRP 12  12  12  TRP TRP A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  THR 16  16  16  THR THR A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  CYS 20  20  20  CYS CYS A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  MET 27  27  27  MET MET A . n 
A 1 28  MET 28  28  28  MET MET A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  PRO 57  57  57  PRO PRO A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  TRP 59  59  59  TRP TRP A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ARG 78  78  78  ARG ARG A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  PRO 81  81  81  PRO PRO A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  SER 89  89  89  SER SER A . n 
A 1 90  PHE 90  90  90  PHE PHE A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 PHE 111 111 111 PHE PHE A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 TYR 128 128 128 TYR TYR A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 GLU 134 134 134 GLU GLU A . n 
A 1 135 HIS 135 135 135 HIS HIS A . n 
A 1 136 TYR 136 136 136 TYR TYR A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 ARG 138 138 138 ARG ARG A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 TYR 142 142 142 TYR TYR A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 MET 167 167 167 MET MET A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 PRO 193 193 193 PRO PRO A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 MET 197 197 ?   ?   ?   A . n 
A 1 198 PHE 198 198 ?   ?   ?   A . n 
A 1 199 PHE 199 199 ?   ?   ?   A . n 
A 1 200 HIS 200 200 ?   ?   ?   A . n 
A 1 201 ALA 201 201 ?   ?   ?   A . n 
A 1 202 LYS 202 202 ?   ?   ?   A . n 
A 1 203 PRO 203 203 ?   ?   ?   A . n 
A 1 204 SER 204 204 ?   ?   ?   A . n 
A 1 205 ARG 205 205 ?   ?   ?   A . n 
A 1 206 GLU 206 206 ?   ?   ?   A . n 
A 1 207 ILE 207 207 ?   ?   ?   A . n 
A 1 208 LYS 208 208 ?   ?   ?   A . n 
A 1 209 LYS 209 209 ?   ?   ?   A . n 
A 1 210 SER 210 210 ?   ?   ?   A . n 
A 1 211 SER 211 211 ?   ?   ?   A . n 
A 1 212 SER 212 212 ?   ?   ?   A . n 
A 1 213 VAL 213 213 ?   ?   ?   A . n 
A 1 214 ASN 214 214 ?   ?   ?   A . n 
A 1 215 PRO 215 215 ?   ?   ?   A . n 
A 1 216 VAL 216 216 ?   ?   ?   A . n 
A 1 217 LEU 217 217 ?   ?   ?   A . n 
A 1 218 GLU 218 218 ?   ?   ?   A . n 
A 1 219 GLU 219 219 ?   ?   ?   A . n 
A 1 220 THR 220 220 ?   ?   ?   A . n 
A 1 221 HIS 221 221 ?   ?   ?   A . n 
A 1 222 GLU 222 222 ?   ?   ?   A . n 
A 1 223 GLY 223 223 ?   ?   ?   A . n 
A 1 224 GLU 224 224 ?   ?   ?   A . n 
A 1 225 ALA 225 225 ?   ?   ?   A . n 
A 1 226 PRO 226 226 ?   ?   ?   A . n 
A 1 227 GLY 227 227 ?   ?   ?   A . n 
A 1 228 CYS 228 228 ?   ?   ?   A . n 
A 1 229 GLU 229 229 ?   ?   ?   A . n 
A 1 230 GLU 230 230 ?   ?   ?   A . n 
A 1 231 GLN 231 231 ?   ?   ?   A . n 
A 1 232 LYS 232 232 ?   ?   ?   A . n 
A 1 233 PRO 233 233 ?   ?   ?   A . n 
A 1 234 THR 234 234 ?   ?   ?   A . n 
A 1 235 SER 235 235 ?   ?   ?   A . n 
A 1 236 GLU 236 236 ?   ?   ?   A . n 
A 1 237 ILE 237 237 ?   ?   ?   A . n 
A 1 238 LEU 238 238 ?   ?   ?   A . n 
A 1 239 SER 239 239 ?   ?   ?   A . n 
A 1 240 THR 240 240 ?   ?   ?   A . n 
A 1 241 SER 241 241 ?   ?   ?   A . n 
A 1 242 GLY 242 242 ?   ?   ?   A . n 
A 1 243 LYS 243 243 ?   ?   ?   A . n 
A 1 244 LEU 244 244 ?   ?   ?   A . n 
A 1 245 ASN 245 245 ?   ?   ?   A . n 
A 1 246 LYS 246 246 ?   ?   ?   A . n 
A 1 247 GLY 247 247 ?   ?   ?   A . n 
A 1 248 GLN 248 248 ?   ?   ?   A . n 
A 1 249 LEU 249 249 ?   ?   ?   A . n 
A 1 250 ASN 250 250 ?   ?   ?   A . n 
A 1 251 SER 251 251 ?   ?   ?   A . n 
A 1 252 LEU 252 252 ?   ?   ?   A . n 
A 1 253 LYS 253 253 ?   ?   ?   A . n 
A 1 254 PRO 254 254 ?   ?   ?   A . n 
A 1 255 SER 255 255 ?   ?   ?   A . n 
A 1 256 ASN 256 256 ?   ?   ?   A . n 
A 1 257 VAL 257 257 ?   ?   ?   A . n 
A 1 258 THR 258 258 ?   ?   ?   A . n 
A 1 259 VAL 259 259 ?   ?   ?   A . n 
A 1 260 ASP 260 260 ?   ?   ?   A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 GLN 264 264 264 GLN GLN A . n 
A 1 265 TRP 265 265 265 TRP TRP A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 GLN 267 267 267 GLN GLN A . n 
A 1 268 ASP 268 268 268 ASP ASP A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 CYS 272 272 272 CYS CYS A . n 
A 1 273 TYR 273 273 273 TYR TYR A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 ARG 277 277 277 ARG ARG A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 TYR 280 280 280 TYR TYR A . n 
A 1 281 TRP 281 281 281 TRP TRP A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 TRP 284 284 284 TRP TRP A . n 
A 1 285 TRP 285 285 285 TRP TRP A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 PHE 287 287 287 PHE PHE A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 THR 289 289 289 THR THR A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 GLY 291 291 291 GLY GLY A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ASN 297 297 297 ASN ASN A . n 
A 1 298 TYR 298 298 298 TYR TYR A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 GLN 300 300 300 GLN GLN A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 LEU 302 302 302 LEU LEU A . n 
A 1 303 TRP 303 303 303 TRP TRP A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 SER 312 312 312 SER SER A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 ILE 314 314 314 ILE ILE A . n 
A 1 315 TYR 315 315 315 TYR TYR A . n 
A 1 316 ASN 316 316 316 ASN ASN A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 THR 324 324 324 THR THR A . n 
A 1 325 PHE 325 325 325 PHE PHE A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 ALA 328 328 328 ALA ALA A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 ALA 330 330 330 ALA ALA A . n 
A 1 331 ALA 331 331 331 ALA ALA A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 ALA 333 333 333 ALA ALA A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 TYR 336 336 336 TYR TYR A . n 
A 1 337 VAL 337 337 337 VAL VAL A . n 
A 1 338 LYS 338 338 338 LYS LYS A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 ASN 340 340 340 ASN ASN A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 LEU 343 343 343 LEU LEU A . n 
A 1 344 LEU 344 344 344 LEU LEU A . n 
A 1 345 GLY 345 345 345 GLY GLY A . n 
A 1 346 GLU 346 346 346 GLU GLU A . n 
A 1 347 LEU 347 347 347 LEU LEU A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 LEU 349 349 349 LEU LEU A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 PHE 352 352 352 PHE PHE A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 VAL 355 355 355 VAL VAL A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 PHE 361 361 361 PHE PHE A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 MET 363 363 363 MET MET A . n 
A 1 364 HIS 364 364 364 HIS HIS A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 ALA 367 367 367 ALA ALA A . n 
A 1 368 ASN 368 368 368 ASN ASN A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 TRP 370 370 370 TRP TRP A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 CYS 372 372 372 CYS CYS A . n 
A 1 373 TYR 373 373 373 TYR TYR A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 GLY 375 375 375 GLY GLY A . n 
A 1 376 TYR 376 376 376 TYR TYR A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 PHE 379 379 379 PHE PHE A . n 
A 1 380 LYS 380 380 380 LYS LYS A . n 
A 1 381 SER 381 381 381 SER SER A . n 
A 1 382 SER 382 382 382 SER SER A . n 
A 1 383 TYR 383 383 383 TYR TYR A . n 
A 1 384 MET 384 384 384 MET MET A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 THR 388 388 388 THR THR A . n 
A 1 389 ILE 389 389 389 ILE ILE A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 VAL 391 391 391 VAL VAL A . n 
A 1 392 PHE 392 392 392 PHE PHE A . n 
A 1 393 GLN 393 393 393 GLN GLN A . n 
A 1 394 ILE 394 394 394 ILE ILE A . n 
A 1 395 ALA 395 395 395 ALA ALA A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 ASN 397 397 397 ASN ASN A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 ASN 399 399 399 ASN ASN A . n 
A 1 400 VAL 400 400 400 VAL VAL A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 ARG 402 402 402 ARG ARG A . n 
A 1 403 TYR 403 403 403 TYR TYR A . n 
A 1 404 ALA 404 404 404 ALA ALA A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 VAL 406 406 406 VAL VAL A . n 
A 1 407 PHE 407 407 407 PHE PHE A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 ILE 409 409 409 ILE ILE A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 THR 411 411 411 THR THR A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 ILE 413 413 413 ILE ILE A . n 
A 1 414 ALA 414 414 414 ALA ALA A . n 
A 1 415 LEU 415 415 415 LEU LEU A . n 
A 1 416 VAL 416 416 416 VAL VAL A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLN 418 418 418 GLN GLN A . n 
A 1 419 THR 419 419 419 THR THR A . n 
A 1 420 ILE 420 420 420 ILE ILE A . n 
A 1 421 MET 421 421 421 MET MET A . n 
A 1 422 THR 422 422 422 THR THR A . n 
A 1 423 VAL 423 423 423 VAL VAL A . n 
A 1 424 ILE 424 424 424 ILE ILE A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 ASP 427 427 427 ASP ASP A . n 
A 1 428 GLN 428 428 428 GLN GLN A . n 
A 1 429 ARG 429 429 429 ARG ARG A . n 
A 1 430 GLY 430 430 430 GLY GLY A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ASN 432 432 432 ASN ASN A . n 
A 1 433 LEU 433 433 433 LEU LEU A . n 
A 1 434 PRO 434 434 434 PRO PRO A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 SER 436 436 436 SER SER A . n 
A 1 437 ILE 437 437 437 ILE ILE A . n 
A 1 438 GLN 438 438 438 GLN GLN A . n 
A 1 439 PHE 439 439 439 PHE PHE A . n 
A 1 440 LEU 440 440 440 LEU LEU A . n 
A 1 441 VAL 441 441 441 VAL VAL A . n 
A 1 442 TYR 442 442 442 TYR TYR A . n 
A 1 443 GLY 443 443 443 GLY GLY A . n 
A 1 444 SER 444 444 444 SER SER A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 PHE 446 446 446 PHE PHE A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 VAL 448 448 448 VAL VAL A . n 
A 1 449 ILE 449 449 449 ILE ILE A . n 
A 1 450 ALA 450 450 450 ALA ALA A . n 
A 1 451 GLY 451 451 451 GLY GLY A . n 
A 1 452 ILE 452 452 452 ILE ILE A . n 
A 1 453 PHE 453 453 453 PHE PHE A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 MET 455 455 455 MET MET A . n 
A 1 456 ARG 456 456 456 ARG ARG A . n 
A 1 457 SER 457 457 457 SER SER A . n 
A 1 458 MET 458 458 458 MET MET A . n 
A 1 459 TYR 459 459 459 TYR TYR A . n 
A 1 460 ILE 460 460 460 ILE ILE A . n 
A 1 461 THR 461 461 461 THR THR A . n 
A 1 462 TYR 462 462 ?   ?   ?   A . n 
A 1 463 SER 463 463 ?   ?   ?   A . n 
A 1 464 THR 464 464 ?   ?   ?   A . n 
A 1 465 LYS 465 465 ?   ?   ?   A . n 
A 1 466 SER 466 466 ?   ?   ?   A . n 
A 1 467 GLN 467 467 ?   ?   ?   A . n 
A 1 468 LYS 468 468 ?   ?   ?   A . n 
A 1 469 ASP 469 469 ?   ?   ?   A . n 
A 1 470 VAL 470 470 ?   ?   ?   A . n 
A 1 471 GLN 471 471 ?   ?   ?   A . n 
A 1 472 SER 472 472 ?   ?   ?   A . n 
A 1 473 PRO 473 473 ?   ?   ?   A . n 
A 1 474 ALA 474 474 ?   ?   ?   A . n 
A 1 475 PRO 475 475 ?   ?   ?   A . n 
A 1 476 SER 476 476 ?   ?   ?   A . n 
A 1 477 GLU 477 477 ?   ?   ?   A . n 
A 1 478 ASN 478 478 ?   ?   ?   A . n 
A 1 479 PRO 479 479 ?   ?   ?   A . n 
A 1 480 ASP 480 480 ?   ?   ?   A . n 
A 1 481 VAL 481 481 ?   ?   ?   A . n 
A 1 482 SER 482 482 ?   ?   ?   A . n 
A 1 483 HIS 483 483 ?   ?   ?   A . n 
A 1 484 PRO 484 484 ?   ?   ?   A . n 
A 1 485 GLU 485 485 ?   ?   ?   A . n 
A 1 486 GLU 486 486 ?   ?   ?   A . n 
A 1 487 GLU 487 487 ?   ?   ?   A . n 
A 1 488 SER 488 488 ?   ?   ?   A . n 
A 1 489 ASN 489 489 ?   ?   ?   A . n 
A 1 490 ILE 490 490 ?   ?   ?   A . n 
A 1 491 ILE 491 491 ?   ?   ?   A . n 
A 1 492 MET 492 492 ?   ?   ?   A . n 
A 1 493 SER 493 493 ?   ?   ?   A . n 
A 1 494 THR 494 494 ?   ?   ?   A . n 
A 1 495 LYS 495 495 ?   ?   ?   A . n 
A 1 496 LEU 496 496 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H5C 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H5C 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_nonpoly_scheme.asym_id         B 
_pdbx_nonpoly_scheme.entity_id       2 
_pdbx_nonpoly_scheme.mon_id          A1H5C 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     501 
_pdbx_nonpoly_scheme.auth_seq_num    501 
_pdbx_nonpoly_scheme.pdb_mon_id      A1H5C 
_pdbx_nonpoly_scheme.auth_mon_id     APL 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z7V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z7V 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z7V 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8Z7V 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.003 ? 3210 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.587 ? 4387 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.677 ? 427  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.040 ? 505  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.006 ? 525  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8Z7V 
_struct.title                        'Slc19A3-Amprolium outward structure' 
_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        8Z7V 
_struct_keywords.text            'Thiamine transporter, MFS, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    S19A3_HUMAN 
_struct_ref.pdbx_db_accession          Q9BZV2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDCYRTSLSSSWIYPTVILCLFGFFSMMRPSEPFLIPYLSGPDKNLTSAEITNEIFPVWTYSYLVLLLPVFVLTDYVRYK
PVIILQGISFIITWLLLLFGQGVKTMQVVEFFYGMVTAAEVAYYAYIYSVVSPEHYQRVSGYCRSVTLAAYTAGSVLAQL
LVSLANMSYFYLNVISLASVSVAFLFSLFLPMPKKSMFFHAKPSREIKKSSSVNPVLEETHEGEAPGCEEQKPTSEILST
SGKLNKGQLNSLKPSNVTVDVFVQWFQDLKECYSSKRLFYWSLWWAFATAGFNQVLNYVQILWDYKAPSQDSSIYNGAVE
AIATFGGAVAAFAVGYVKVNWDLLGELALVVFSVVNAGSLFLMHYTANIWACYAGYLIFKSSYMLLITIAVFQIAVNLNV
ERYALVFGINTFIALVIQTIMTVIVVDQRGLNLPVSIQFLVYGSYFAVIAGIFLMRSMYITYSTKSQKDVQSPAPSENPD
VSHPEEESNIIMSTKL
;
_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              8Z7V 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 496 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9BZV2 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  496 
_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       496 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 TRP A 12  ? MET A 28  ? TRP A 12  MET A 28  1 ? 17 
HELX_P HELX_P2  AA2 PHE A 34  ? GLY A 41  ? PHE A 34  GLY A 41  1 ? 8  
HELX_P HELX_P3  AA3 THR A 47  ? THR A 52  ? THR A 47  THR A 52  1 ? 6  
HELX_P HELX_P4  AA4 ILE A 55  ? LEU A 68  ? ILE A 55  LEU A 68  1 ? 14 
HELX_P HELX_P5  AA5 PRO A 69  ? THR A 74  ? PRO A 69  THR A 74  1 ? 6  
HELX_P HELX_P6  AA6 TYR A 79  ? GLY A 100 ? TYR A 79  GLY A 100 1 ? 22 
HELX_P HELX_P7  AA7 GLN A 101 ? SER A 129 ? GLN A 101 SER A 129 1 ? 29 
HELX_P HELX_P8  AA8 SER A 132 ? GLU A 134 ? SER A 132 GLU A 134 5 ? 3  
HELX_P HELX_P9  AA9 HIS A 135 ? LEU A 164 ? HIS A 135 LEU A 164 1 ? 30 
HELX_P HELX_P10 AB1 SER A 168 ? PHE A 189 ? SER A 168 PHE A 189 1 ? 22 
HELX_P HELX_P11 AB2 PHE A 262 ? SER A 274 ? PHE A 262 SER A 274 1 ? 13 
HELX_P HELX_P12 AB3 LEU A 278 ? ALA A 307 ? LEU A 278 ALA A 307 1 ? 30 
HELX_P HELX_P13 AB4 ASP A 311 ? VAL A 337 ? ASP A 311 VAL A 337 1 ? 27 
HELX_P HELX_P14 AB5 ASN A 340 ? THR A 366 ? ASN A 340 THR A 366 1 ? 27 
HELX_P HELX_P15 AB6 ASN A 368 ? LEU A 398 ? ASN A 368 LEU A 398 1 ? 31 
HELX_P HELX_P16 AB7 ARG A 402 ? VAL A 426 ? ARG A 402 VAL A 426 1 ? 25 
HELX_P HELX_P17 AB8 PRO A 434 ? THR A 461 ? PRO A 434 THR A 461 1 ? 28 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   8Z7V 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    356 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    382 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 TYR A 79  ? ? 68.29  -9.49 
2 1 ASN A 166 ? ? 39.47  42.44 
3 1 LYS A 338 ? ? -92.05 53.71 
4 1 ASN A 399 ? ? 52.67  17.17 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8Z7V 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    8Z7V 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.1 
_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               183814 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.5 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 slc19a3 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8Z7V 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TALOS ARCTICA' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1200 
_em_imaging.nominal_defocus_max             1500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              8Z7V 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8Z7V 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ASP 2   ? A ASP 2   
3   1 Y 1 A CYS 3   ? A CYS 3   
4   1 Y 1 A TYR 4   ? A TYR 4   
5   1 Y 1 A ARG 5   ? A ARG 5   
6   1 Y 1 A THR 6   ? A THR 6   
7   1 Y 1 A SER 7   ? A SER 7   
8   1 Y 1 A LEU 8   ? A LEU 8   
9   1 Y 1 A SER 9   ? A SER 9   
10  1 Y 1 A SER 10  ? A SER 10  
11  1 Y 1 A MET 197 ? A MET 197 
12  1 Y 1 A PHE 198 ? A PHE 198 
13  1 Y 1 A PHE 199 ? A PHE 199 
14  1 Y 1 A HIS 200 ? A HIS 200 
15  1 Y 1 A ALA 201 ? A ALA 201 
16  1 Y 1 A LYS 202 ? A LYS 202 
17  1 Y 1 A PRO 203 ? A PRO 203 
18  1 Y 1 A SER 204 ? A SER 204 
19  1 Y 1 A ARG 205 ? A ARG 205 
20  1 Y 1 A GLU 206 ? A GLU 206 
21  1 Y 1 A ILE 207 ? A ILE 207 
22  1 Y 1 A LYS 208 ? A LYS 208 
23  1 Y 1 A LYS 209 ? A LYS 209 
24  1 Y 1 A SER 210 ? A SER 210 
25  1 Y 1 A SER 211 ? A SER 211 
26  1 Y 1 A SER 212 ? A SER 212 
27  1 Y 1 A VAL 213 ? A VAL 213 
28  1 Y 1 A ASN 214 ? A ASN 214 
29  1 Y 1 A PRO 215 ? A PRO 215 
30  1 Y 1 A VAL 216 ? A VAL 216 
31  1 Y 1 A LEU 217 ? A LEU 217 
32  1 Y 1 A GLU 218 ? A GLU 218 
33  1 Y 1 A GLU 219 ? A GLU 219 
34  1 Y 1 A THR 220 ? A THR 220 
35  1 Y 1 A HIS 221 ? A HIS 221 
36  1 Y 1 A GLU 222 ? A GLU 222 
37  1 Y 1 A GLY 223 ? A GLY 223 
38  1 Y 1 A GLU 224 ? A GLU 224 
39  1 Y 1 A ALA 225 ? A ALA 225 
40  1 Y 1 A PRO 226 ? A PRO 226 
41  1 Y 1 A GLY 227 ? A GLY 227 
42  1 Y 1 A CYS 228 ? A CYS 228 
43  1 Y 1 A GLU 229 ? A GLU 229 
44  1 Y 1 A GLU 230 ? A GLU 230 
45  1 Y 1 A GLN 231 ? A GLN 231 
46  1 Y 1 A LYS 232 ? A LYS 232 
47  1 Y 1 A PRO 233 ? A PRO 233 
48  1 Y 1 A THR 234 ? A THR 234 
49  1 Y 1 A SER 235 ? A SER 235 
50  1 Y 1 A GLU 236 ? A GLU 236 
51  1 Y 1 A ILE 237 ? A ILE 237 
52  1 Y 1 A LEU 238 ? A LEU 238 
53  1 Y 1 A SER 239 ? A SER 239 
54  1 Y 1 A THR 240 ? A THR 240 
55  1 Y 1 A SER 241 ? A SER 241 
56  1 Y 1 A GLY 242 ? A GLY 242 
57  1 Y 1 A LYS 243 ? A LYS 243 
58  1 Y 1 A LEU 244 ? A LEU 244 
59  1 Y 1 A ASN 245 ? A ASN 245 
60  1 Y 1 A LYS 246 ? A LYS 246 
61  1 Y 1 A GLY 247 ? A GLY 247 
62  1 Y 1 A GLN 248 ? A GLN 248 
63  1 Y 1 A LEU 249 ? A LEU 249 
64  1 Y 1 A ASN 250 ? A ASN 250 
65  1 Y 1 A SER 251 ? A SER 251 
66  1 Y 1 A LEU 252 ? A LEU 252 
67  1 Y 1 A LYS 253 ? A LYS 253 
68  1 Y 1 A PRO 254 ? A PRO 254 
69  1 Y 1 A SER 255 ? A SER 255 
70  1 Y 1 A ASN 256 ? A ASN 256 
71  1 Y 1 A VAL 257 ? A VAL 257 
72  1 Y 1 A THR 258 ? A THR 258 
73  1 Y 1 A VAL 259 ? A VAL 259 
74  1 Y 1 A ASP 260 ? A ASP 260 
75  1 Y 1 A TYR 462 ? A TYR 462 
76  1 Y 1 A SER 463 ? A SER 463 
77  1 Y 1 A THR 464 ? A THR 464 
78  1 Y 1 A LYS 465 ? A LYS 465 
79  1 Y 1 A SER 466 ? A SER 466 
80  1 Y 1 A GLN 467 ? A GLN 467 
81  1 Y 1 A LYS 468 ? A LYS 468 
82  1 Y 1 A ASP 469 ? A ASP 469 
83  1 Y 1 A VAL 470 ? A VAL 470 
84  1 Y 1 A GLN 471 ? A GLN 471 
85  1 Y 1 A SER 472 ? A SER 472 
86  1 Y 1 A PRO 473 ? A PRO 473 
87  1 Y 1 A ALA 474 ? A ALA 474 
88  1 Y 1 A PRO 475 ? A PRO 475 
89  1 Y 1 A SER 476 ? A SER 476 
90  1 Y 1 A GLU 477 ? A GLU 477 
91  1 Y 1 A ASN 478 ? A ASN 478 
92  1 Y 1 A PRO 479 ? A PRO 479 
93  1 Y 1 A ASP 480 ? A ASP 480 
94  1 Y 1 A VAL 481 ? A VAL 481 
95  1 Y 1 A SER 482 ? A SER 482 
96  1 Y 1 A HIS 483 ? A HIS 483 
97  1 Y 1 A PRO 484 ? A PRO 484 
98  1 Y 1 A GLU 485 ? A GLU 485 
99  1 Y 1 A GLU 486 ? A GLU 486 
100 1 Y 1 A GLU 487 ? A GLU 487 
101 1 Y 1 A SER 488 ? A SER 488 
102 1 Y 1 A ASN 489 ? A ASN 489 
103 1 Y 1 A ILE 490 ? A ILE 490 
104 1 Y 1 A ILE 491 ? A ILE 491 
105 1 Y 1 A MET 492 ? A MET 492 
106 1 Y 1 A SER 493 ? A SER 493 
107 1 Y 1 A THR 494 ? A THR 494 
108 1 Y 1 A LYS 495 ? A LYS 495 
109 1 Y 1 A LEU 496 ? A LEU 496 
# 
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 
A1H5C C10  C Y N 1   
A1H5C N12  N Y N 2   
A1H5C C13  C Y N 3   
A1H5C C15  C N N 4   
A1H5C C03  C Y N 5   
A1H5C C04  C Y N 6   
A1H5C C05  C Y N 7   
A1H5C C06  C Y N 8   
A1H5C C07  C Y N 9   
A1H5C C08  C N N 10  
A1H5C C09  C N N 11  
A1H5C C11  C Y N 12  
A1H5C C14  C N N 13  
A1H5C C16  C N N 14  
A1H5C C18  C Y N 15  
A1H5C N02  N Y N 16  
A1H5C N17  N Y N 17  
A1H5C N19  N N N 18  
A1H5C H152 H N N 19  
A1H5C H151 H N N 20  
A1H5C H031 H N N 21  
A1H5C H041 H N N 22  
A1H5C H051 H N N 23  
A1H5C H061 H N N 24  
A1H5C H083 H N N 25  
A1H5C H082 H N N 26  
A1H5C H081 H N N 27  
A1H5C H092 H N N 28  
A1H5C H091 H N N 29  
A1H5C H111 H N N 30  
A1H5C H142 H N N 31  
A1H5C H141 H N N 32  
A1H5C H163 H N N 33  
A1H5C H162 H N N 34  
A1H5C H161 H N N 35  
A1H5C H192 H N N 36  
A1H5C H191 H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
GLN   N    N N N 125 
GLN   CA   C N S 126 
GLN   C    C N N 127 
GLN   O    O N N 128 
GLN   CB   C N N 129 
GLN   CG   C N N 130 
GLN   CD   C N N 131 
GLN   OE1  O N N 132 
GLN   NE2  N N N 133 
GLN   OXT  O N N 134 
GLN   H    H N N 135 
GLN   H2   H N N 136 
GLN   HA   H N N 137 
GLN   HB2  H N N 138 
GLN   HB3  H N N 139 
GLN   HG2  H N N 140 
GLN   HG3  H N N 141 
GLN   HE21 H N N 142 
GLN   HE22 H N N 143 
GLN   HXT  H N N 144 
GLU   N    N N N 145 
GLU   CA   C N S 146 
GLU   C    C N N 147 
GLU   O    O N N 148 
GLU   CB   C N N 149 
GLU   CG   C N N 150 
GLU   CD   C N N 151 
GLU   OE1  O N N 152 
GLU   OE2  O N N 153 
GLU   OXT  O N N 154 
GLU   H    H N N 155 
GLU   H2   H N N 156 
GLU   HA   H N N 157 
GLU   HB2  H N N 158 
GLU   HB3  H N N 159 
GLU   HG2  H N N 160 
GLU   HG3  H N N 161 
GLU   HE2  H N N 162 
GLU   HXT  H N N 163 
GLY   N    N N N 164 
GLY   CA   C N N 165 
GLY   C    C N N 166 
GLY   O    O N N 167 
GLY   OXT  O N N 168 
GLY   H    H N N 169 
GLY   H2   H N N 170 
GLY   HA2  H N N 171 
GLY   HA3  H N N 172 
GLY   HXT  H N N 173 
HIS   N    N N N 174 
HIS   CA   C N S 175 
HIS   C    C N N 176 
HIS   O    O N N 177 
HIS   CB   C N N 178 
HIS   CG   C Y N 179 
HIS   ND1  N Y N 180 
HIS   CD2  C Y N 181 
HIS   CE1  C Y N 182 
HIS   NE2  N Y N 183 
HIS   OXT  O N N 184 
HIS   H    H N N 185 
HIS   H2   H N N 186 
HIS   HA   H N N 187 
HIS   HB2  H N N 188 
HIS   HB3  H N N 189 
HIS   HD1  H N N 190 
HIS   HD2  H N N 191 
HIS   HE1  H N N 192 
HIS   HE2  H N N 193 
HIS   HXT  H N N 194 
ILE   N    N N N 195 
ILE   CA   C N S 196 
ILE   C    C N N 197 
ILE   O    O N N 198 
ILE   CB   C N S 199 
ILE   CG1  C N N 200 
ILE   CG2  C N N 201 
ILE   CD1  C N N 202 
ILE   OXT  O N N 203 
ILE   H    H N N 204 
ILE   H2   H N N 205 
ILE   HA   H N N 206 
ILE   HB   H N N 207 
ILE   HG12 H N N 208 
ILE   HG13 H N N 209 
ILE   HG21 H N N 210 
ILE   HG22 H N N 211 
ILE   HG23 H N N 212 
ILE   HD11 H N N 213 
ILE   HD12 H N N 214 
ILE   HD13 H N N 215 
ILE   HXT  H N N 216 
LEU   N    N N N 217 
LEU   CA   C N S 218 
LEU   C    C N N 219 
LEU   O    O N N 220 
LEU   CB   C N N 221 
LEU   CG   C N N 222 
LEU   CD1  C N N 223 
LEU   CD2  C N N 224 
LEU   OXT  O N N 225 
LEU   H    H N N 226 
LEU   H2   H N N 227 
LEU   HA   H N N 228 
LEU   HB2  H N N 229 
LEU   HB3  H N N 230 
LEU   HG   H N N 231 
LEU   HD11 H N N 232 
LEU   HD12 H N N 233 
LEU   HD13 H N N 234 
LEU   HD21 H N N 235 
LEU   HD22 H N N 236 
LEU   HD23 H N N 237 
LEU   HXT  H N N 238 
LYS   N    N N N 239 
LYS   CA   C N S 240 
LYS   C    C N N 241 
LYS   O    O N N 242 
LYS   CB   C N N 243 
LYS   CG   C N N 244 
LYS   CD   C N N 245 
LYS   CE   C N N 246 
LYS   NZ   N N N 247 
LYS   OXT  O N N 248 
LYS   H    H N N 249 
LYS   H2   H N N 250 
LYS   HA   H N N 251 
LYS   HB2  H N N 252 
LYS   HB3  H N N 253 
LYS   HG2  H N N 254 
LYS   HG3  H N N 255 
LYS   HD2  H N N 256 
LYS   HD3  H N N 257 
LYS   HE2  H N N 258 
LYS   HE3  H N N 259 
LYS   HZ1  H N N 260 
LYS   HZ2  H N N 261 
LYS   HZ3  H N N 262 
LYS   HXT  H N N 263 
MET   N    N N N 264 
MET   CA   C N S 265 
MET   C    C N N 266 
MET   O    O N N 267 
MET   CB   C N N 268 
MET   CG   C N N 269 
MET   SD   S N N 270 
MET   CE   C N N 271 
MET   OXT  O N N 272 
MET   H    H N N 273 
MET   H2   H N N 274 
MET   HA   H N N 275 
MET   HB2  H N N 276 
MET   HB3  H N N 277 
MET   HG2  H N N 278 
MET   HG3  H N N 279 
MET   HE1  H N N 280 
MET   HE2  H N N 281 
MET   HE3  H N N 282 
MET   HXT  H N N 283 
PHE   N    N N N 284 
PHE   CA   C N S 285 
PHE   C    C N N 286 
PHE   O    O N N 287 
PHE   CB   C N N 288 
PHE   CG   C Y N 289 
PHE   CD1  C Y N 290 
PHE   CD2  C Y N 291 
PHE   CE1  C Y N 292 
PHE   CE2  C Y N 293 
PHE   CZ   C Y N 294 
PHE   OXT  O N N 295 
PHE   H    H N N 296 
PHE   H2   H N N 297 
PHE   HA   H N N 298 
PHE   HB2  H N N 299 
PHE   HB3  H N N 300 
PHE   HD1  H N N 301 
PHE   HD2  H N N 302 
PHE   HE1  H N N 303 
PHE   HE2  H N N 304 
PHE   HZ   H N N 305 
PHE   HXT  H N N 306 
PRO   N    N N N 307 
PRO   CA   C N S 308 
PRO   C    C N N 309 
PRO   O    O N N 310 
PRO   CB   C N N 311 
PRO   CG   C N N 312 
PRO   CD   C N N 313 
PRO   OXT  O N N 314 
PRO   H    H N N 315 
PRO   HA   H N N 316 
PRO   HB2  H N N 317 
PRO   HB3  H N N 318 
PRO   HG2  H N N 319 
PRO   HG3  H N N 320 
PRO   HD2  H N N 321 
PRO   HD3  H N N 322 
PRO   HXT  H N N 323 
SER   N    N N N 324 
SER   CA   C N S 325 
SER   C    C N N 326 
SER   O    O N N 327 
SER   CB   C N N 328 
SER   OG   O N N 329 
SER   OXT  O N N 330 
SER   H    H N N 331 
SER   H2   H N N 332 
SER   HA   H N N 333 
SER   HB2  H N N 334 
SER   HB3  H N N 335 
SER   HG   H N N 336 
SER   HXT  H N N 337 
THR   N    N N N 338 
THR   CA   C N S 339 
THR   C    C N N 340 
THR   O    O N N 341 
THR   CB   C N R 342 
THR   OG1  O N N 343 
THR   CG2  C N N 344 
THR   OXT  O N N 345 
THR   H    H N N 346 
THR   H2   H N N 347 
THR   HA   H N N 348 
THR   HB   H N N 349 
THR   HG1  H N N 350 
THR   HG21 H N N 351 
THR   HG22 H N N 352 
THR   HG23 H N N 353 
THR   HXT  H N N 354 
TRP   N    N N N 355 
TRP   CA   C N S 356 
TRP   C    C N N 357 
TRP   O    O N N 358 
TRP   CB   C N N 359 
TRP   CG   C Y N 360 
TRP   CD1  C Y N 361 
TRP   CD2  C Y N 362 
TRP   NE1  N Y N 363 
TRP   CE2  C Y N 364 
TRP   CE3  C Y N 365 
TRP   CZ2  C Y N 366 
TRP   CZ3  C Y N 367 
TRP   CH2  C Y N 368 
TRP   OXT  O N N 369 
TRP   H    H N N 370 
TRP   H2   H N N 371 
TRP   HA   H N N 372 
TRP   HB2  H N N 373 
TRP   HB3  H N N 374 
TRP   HD1  H N N 375 
TRP   HE1  H N N 376 
TRP   HE3  H N N 377 
TRP   HZ2  H N N 378 
TRP   HZ3  H N N 379 
TRP   HH2  H N N 380 
TRP   HXT  H N N 381 
TYR   N    N N N 382 
TYR   CA   C N S 383 
TYR   C    C N N 384 
TYR   O    O N N 385 
TYR   CB   C N N 386 
TYR   CG   C Y N 387 
TYR   CD1  C Y N 388 
TYR   CD2  C Y N 389 
TYR   CE1  C Y N 390 
TYR   CE2  C Y N 391 
TYR   CZ   C Y N 392 
TYR   OH   O N N 393 
TYR   OXT  O N N 394 
TYR   H    H N N 395 
TYR   H2   H N N 396 
TYR   HA   H N N 397 
TYR   HB2  H N N 398 
TYR   HB3  H N N 399 
TYR   HD1  H N N 400 
TYR   HD2  H N N 401 
TYR   HE1  H N N 402 
TYR   HE2  H N N 403 
TYR   HH   H N N 404 
TYR   HXT  H N N 405 
VAL   N    N N N 406 
VAL   CA   C N S 407 
VAL   C    C N N 408 
VAL   O    O N N 409 
VAL   CB   C N N 410 
VAL   CG1  C N N 411 
VAL   CG2  C N N 412 
VAL   OXT  O N N 413 
VAL   H    H N N 414 
VAL   H2   H N N 415 
VAL   HA   H N N 416 
VAL   HB   H N N 417 
VAL   HG11 H N N 418 
VAL   HG12 H N N 419 
VAL   HG13 H N N 420 
VAL   HG21 H N N 421 
VAL   HG22 H N N 422 
VAL   HG23 H N N 423 
VAL   HXT  H N N 424 
# 
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 
A1H5C C05 C06  doub Y N 1   
A1H5C C05 C04  sing Y N 2   
A1H5C C06 C07  sing Y N 3   
A1H5C C04 C03  doub Y N 4   
A1H5C C03 N02  sing Y N 5   
A1H5C C07 N02  doub Y N 6   
A1H5C C07 C08  sing N N 7   
A1H5C N02 C09  sing N N 8   
A1H5C C09 C10  sing N N 9   
A1H5C N19 C18  sing N N 10  
A1H5C C10 C18  doub Y N 11  
A1H5C C10 C11  sing Y N 12  
A1H5C C18 N17  sing Y N 13  
A1H5C C11 N12  doub Y N 14  
A1H5C N17 C13  doub Y N 15  
A1H5C N12 C13  sing Y N 16  
A1H5C C13 C14  sing N N 17  
A1H5C C14 C15  sing N N 18  
A1H5C C16 C15  sing N N 19  
A1H5C C15 H152 sing N N 20  
A1H5C C15 H151 sing N N 21  
A1H5C C03 H031 sing N N 22  
A1H5C C04 H041 sing N N 23  
A1H5C C05 H051 sing N N 24  
A1H5C C06 H061 sing N N 25  
A1H5C C08 H083 sing N N 26  
A1H5C C08 H082 sing N N 27  
A1H5C C08 H081 sing N N 28  
A1H5C C09 H092 sing N N 29  
A1H5C C09 H091 sing N N 30  
A1H5C C11 H111 sing N N 31  
A1H5C C14 H142 sing N N 32  
A1H5C C14 H141 sing N N 33  
A1H5C C16 H163 sing N N 34  
A1H5C C16 H162 sing N N 35  
A1H5C C16 H161 sing N N 36  
A1H5C N19 H192 sing N N 37  
A1H5C N19 H191 sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
HIS   N   CA   sing N N 167 
HIS   N   H    sing N N 168 
HIS   N   H2   sing N N 169 
HIS   CA  C    sing N N 170 
HIS   CA  CB   sing N N 171 
HIS   CA  HA   sing N N 172 
HIS   C   O    doub N N 173 
HIS   C   OXT  sing N N 174 
HIS   CB  CG   sing N N 175 
HIS   CB  HB2  sing N N 176 
HIS   CB  HB3  sing N N 177 
HIS   CG  ND1  sing Y N 178 
HIS   CG  CD2  doub Y N 179 
HIS   ND1 CE1  doub Y N 180 
HIS   ND1 HD1  sing N N 181 
HIS   CD2 NE2  sing Y N 182 
HIS   CD2 HD2  sing N N 183 
HIS   CE1 NE2  sing Y N 184 
HIS   CE1 HE1  sing N N 185 
HIS   NE2 HE2  sing N N 186 
HIS   OXT HXT  sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TRP   N   CA   sing N N 342 
TRP   N   H    sing N N 343 
TRP   N   H2   sing N N 344 
TRP   CA  C    sing N N 345 
TRP   CA  CB   sing N N 346 
TRP   CA  HA   sing N N 347 
TRP   C   O    doub N N 348 
TRP   C   OXT  sing N N 349 
TRP   CB  CG   sing N N 350 
TRP   CB  HB2  sing N N 351 
TRP   CB  HB3  sing N N 352 
TRP   CG  CD1  doub Y N 353 
TRP   CG  CD2  sing Y N 354 
TRP   CD1 NE1  sing Y N 355 
TRP   CD1 HD1  sing N N 356 
TRP   CD2 CE2  doub Y N 357 
TRP   CD2 CE3  sing Y N 358 
TRP   NE1 CE2  sing Y N 359 
TRP   NE1 HE1  sing N N 360 
TRP   CE2 CZ2  sing Y N 361 
TRP   CE3 CZ3  doub Y N 362 
TRP   CE3 HE3  sing N N 363 
TRP   CZ2 CH2  doub Y N 364 
TRP   CZ2 HZ2  sing N N 365 
TRP   CZ3 CH2  sing Y N 366 
TRP   CZ3 HZ3  sing N N 367 
TRP   CH2 HH2  sing N N 368 
TRP   OXT HXT  sing N N 369 
TYR   N   CA   sing N N 370 
TYR   N   H    sing N N 371 
TYR   N   H2   sing N N 372 
TYR   CA  C    sing N N 373 
TYR   CA  CB   sing N N 374 
TYR   CA  HA   sing N N 375 
TYR   C   O    doub N N 376 
TYR   C   OXT  sing N N 377 
TYR   CB  CG   sing N N 378 
TYR   CB  HB2  sing N N 379 
TYR   CB  HB3  sing N N 380 
TYR   CG  CD1  doub Y N 381 
TYR   CG  CD2  sing Y N 382 
TYR   CD1 CE1  sing Y N 383 
TYR   CD1 HD1  sing N N 384 
TYR   CD2 CE2  doub Y N 385 
TYR   CD2 HD2  sing N N 386 
TYR   CE1 CZ   doub Y N 387 
TYR   CE1 HE1  sing N N 388 
TYR   CE2 CZ   sing Y N 389 
TYR   CE2 HE2  sing N N 390 
TYR   CZ  OH   sing N N 391 
TYR   OH  HH   sing N N 392 
TYR   OXT HXT  sing N N 393 
VAL   N   CA   sing N N 394 
VAL   N   H    sing N N 395 
VAL   N   H2   sing N N 396 
VAL   CA  C    sing N N 397 
VAL   CA  CB   sing N N 398 
VAL   CA  HA   sing N N 399 
VAL   C   O    doub N N 400 
VAL   C   OXT  sing N N 401 
VAL   CB  CG1  sing N N 402 
VAL   CB  CG2  sing N N 403 
VAL   CB  HB   sing N N 404 
VAL   CG1 HG11 sing N N 405 
VAL   CG1 HG12 sing N N 406 
VAL   CG1 HG13 sing N N 407 
VAL   CG2 HG21 sing N N 408 
VAL   CG2 HG22 sing N N 409 
VAL   CG2 HG23 sing N N 410 
VAL   OXT HXT  sing N N 411 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-21 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           8Z7V 
_em_admin.last_update        2025-01-08 
_em_admin.map_release_date   2025-01-08 
_em_admin.title              'Slc19A3-Amprolium outward structure' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          7108 
_em_entity_assembly_recombinant.organism             'Spodoptera frugiperda' 
_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         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K2 QUANTUM (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 ? ? 
MASKING                    ? 3  ? ? ? ? ? 
'CTF CORRECTION'           ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ? ? 
'MODEL FITTING'            ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ? ? 
OTHER                      ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ? ? 
CLASSIFICATION             ? 12 1 ? ? ? ? 
RECONSTRUCTION             ? 13 1 ? ? ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8Z7V 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
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   . SER   A 1 11  ? 137.197 138.069 121.634 1.00 34.71 ? 11  SER   A N   1 
ATOM   2    C CA  . SER   A 1 11  ? 135.799 137.759 121.362 1.00 37.75 ? 11  SER   A CA  1 
ATOM   3    C C   . SER   A 1 11  ? 135.089 137.291 122.627 1.00 30.55 ? 11  SER   A C   1 
ATOM   4    O O   . SER   A 1 11  ? 134.153 137.933 123.102 1.00 33.57 ? 11  SER   A O   1 
ATOM   5    C CB  . SER   A 1 11  ? 135.688 136.692 120.271 1.00 32.01 ? 11  SER   A CB  1 
ATOM   6    O OG  . SER   A 1 11  ? 136.670 136.885 119.268 1.00 31.47 ? 11  SER   A OG  1 
ATOM   7    N N   . TRP   A 1 12  ? 135.546 136.163 123.169 1.00 22.60 ? 12  TRP   A N   1 
ATOM   8    C CA  . TRP   A 1 12  ? 134.982 135.595 124.384 1.00 24.19 ? 12  TRP   A CA  1 
ATOM   9    C C   . TRP   A 1 12  ? 135.523 136.237 125.651 1.00 24.71 ? 12  TRP   A C   1 
ATOM   10   O O   . TRP   A 1 12  ? 135.003 135.960 126.737 1.00 26.13 ? 12  TRP   A O   1 
ATOM   11   C CB  . TRP   A 1 12  ? 135.252 134.086 124.438 1.00 24.93 ? 12  TRP   A CB  1 
ATOM   12   C CG  . TRP   A 1 12  ? 136.696 133.760 124.675 1.00 27.59 ? 12  TRP   A CG  1 
ATOM   13   C CD1 . TRP   A 1 12  ? 137.691 133.720 123.743 1.00 22.78 ? 12  TRP   A CD1 1 
ATOM   14   C CD2 . TRP   A 1 12  ? 137.310 133.436 125.929 1.00 29.52 ? 12  TRP   A CD2 1 
ATOM   15   N NE1 . TRP   A 1 12  ? 138.884 133.389 124.336 1.00 21.01 ? 12  TRP   A NE1 1 
ATOM   16   C CE2 . TRP   A 1 12  ? 138.677 133.210 125.679 1.00 27.44 ? 12  TRP   A CE2 1 
ATOM   17   C CE3 . TRP   A 1 12  ? 136.836 133.316 127.237 1.00 24.91 ? 12  TRP   A CE3 1 
ATOM   18   C CZ2 . TRP   A 1 12  ? 139.574 132.869 126.688 1.00 26.33 ? 12  TRP   A CZ2 1 
ATOM   19   C CZ3 . TRP   A 1 12  ? 137.727 132.976 128.238 1.00 22.14 ? 12  TRP   A CZ3 1 
ATOM   20   C CH2 . TRP   A 1 12  ? 139.080 132.758 127.958 1.00 22.72 ? 12  TRP   A CH2 1 
ATOM   21   N N   . ILE   A 1 13  ? 136.551 137.084 125.548 1.00 16.88 ? 13  ILE   A N   1 
ATOM   22   C CA  . ILE   A 1 13  ? 137.224 137.604 126.736 1.00 18.56 ? 13  ILE   A CA  1 
ATOM   23   C C   . ILE   A 1 13  ? 136.372 138.571 127.540 1.00 12.01 ? 13  ILE   A C   1 
ATOM   24   O O   . ILE   A 1 13  ? 136.345 138.470 128.770 1.00 15.80 ? 13  ILE   A O   1 
ATOM   25   C CB  . ILE   A 1 13  ? 138.546 138.294 126.353 1.00 17.64 ? 13  ILE   A CB  1 
ATOM   26   C CG1 . ILE   A 1 13  ? 139.415 137.350 125.521 1.00 17.82 ? 13  ILE   A CG1 1 
ATOM   27   C CG2 . ILE   A 1 13  ? 139.299 138.736 127.597 1.00 9.73  ? 13  ILE   A CG2 1 
ATOM   28   C CD1 . ILE   A 1 13  ? 140.377 138.062 124.598 1.00 9.27  ? 13  ILE   A CD1 1 
ATOM   29   N N   . TYR   A 1 14  ? 135.677 139.507 126.892 1.00 20.08 ? 14  TYR   A N   1 
ATOM   30   C CA  . TYR   A 1 14  ? 134.894 140.491 127.634 1.00 27.16 ? 14  TYR   A CA  1 
ATOM   31   C C   . TYR   A 1 14  ? 133.729 139.861 128.396 1.00 19.36 ? 14  TYR   A C   1 
ATOM   32   O O   . TYR   A 1 14  ? 133.574 140.135 129.595 1.00 22.59 ? 14  TYR   A O   1 
ATOM   33   C CB  . TYR   A 1 14  ? 134.381 141.593 126.702 1.00 27.96 ? 14  TYR   A CB  1 
ATOM   34   C CG  . TYR   A 1 14  ? 133.424 142.552 127.375 1.00 23.71 ? 14  TYR   A CG  1 
ATOM   35   C CD1 . TYR   A 1 14  ? 133.893 143.599 128.156 1.00 25.30 ? 14  TYR   A CD1 1 
ATOM   36   C CD2 . TYR   A 1 14  ? 132.049 142.411 127.227 1.00 21.54 ? 14  TYR   A CD2 1 
ATOM   37   C CE1 . TYR   A 1 14  ? 133.023 144.476 128.773 1.00 25.25 ? 14  TYR   A CE1 1 
ATOM   38   C CE2 . TYR   A 1 14  ? 131.172 143.283 127.840 1.00 26.73 ? 14  TYR   A CE2 1 
ATOM   39   C CZ  . TYR   A 1 14  ? 131.664 144.313 128.612 1.00 18.56 ? 14  TYR   A CZ  1 
ATOM   40   O OH  . TYR   A 1 14  ? 130.792 145.185 129.223 1.00 25.88 ? 14  TYR   A OH  1 
ATOM   41   N N   . PRO   A 1 15  ? 132.871 139.048 127.760 1.00 18.18 ? 15  PRO   A N   1 
ATOM   42   C CA  . PRO   A 1 15  ? 131.780 138.429 128.535 1.00 15.78 ? 15  PRO   A CA  1 
ATOM   43   C C   . PRO   A 1 15  ? 132.281 137.527 129.647 1.00 11.10 ? 15  PRO   A C   1 
ATOM   44   O O   . PRO   A 1 15  ? 131.731 137.543 130.757 1.00 16.19 ? 15  PRO   A O   1 
ATOM   45   C CB  . PRO   A 1 15  ? 131.002 137.657 127.458 1.00 9.33  ? 15  PRO   A CB  1 
ATOM   46   C CG  . PRO   A 1 15  ? 132.047 137.343 126.442 1.00 12.78 ? 15  PRO   A CG  1 
ATOM   47   C CD  . PRO   A 1 15  ? 132.772 138.649 126.344 1.00 17.38 ? 15  PRO   A CD  1 
ATOM   48   N N   . THR   A 1 16  ? 133.333 136.748 129.381 1.00 10.03 ? 16  THR   A N   1 
ATOM   49   C CA  . THR   A 1 16  ? 133.883 135.871 130.406 1.00 9.97  ? 16  THR   A CA  1 
ATOM   50   C C   . THR   A 1 16  ? 134.450 136.666 131.569 1.00 8.40  ? 16  THR   A C   1 
ATOM   51   O O   . THR   A 1 16  ? 134.202 136.326 132.727 1.00 7.29  ? 16  THR   A O   1 
ATOM   52   C CB  . THR   A 1 16  ? 134.960 134.967 129.804 1.00 13.88 ? 16  THR   A CB  1 
ATOM   53   O OG1 . THR   A 1 16  ? 134.334 133.864 129.142 1.00 9.21  ? 16  THR   A OG1 1 
ATOM   54   C CG2 . THR   A 1 16  ? 135.887 134.434 130.887 1.00 9.75  ? 16  THR   A CG2 1 
ATOM   55   N N   . VAL   A 1 17  ? 135.188 137.735 131.285 1.00 10.85 ? 17  VAL   A N   1 
ATOM   56   C CA  . VAL   A 1 17  ? 135.760 138.571 132.333 1.00 6.47  ? 17  VAL   A CA  1 
ATOM   57   C C   . VAL   A 1 17  ? 134.673 139.249 133.155 1.00 11.68 ? 17  VAL   A C   1 
ATOM   58   O O   . VAL   A 1 17  ? 134.743 139.267 134.387 1.00 7.40  ? 17  VAL   A O   1 
ATOM   59   C CB  . VAL   A 1 17  ? 136.726 139.600 131.711 1.00 11.83 ? 17  VAL   A CB  1 
ATOM   60   C CG1 . VAL   A 1 17  ? 136.837 140.838 132.591 1.00 12.93 ? 17  VAL   A CG1 1 
ATOM   61   C CG2 . VAL   A 1 17  ? 138.095 138.975 131.492 1.00 6.96  ? 17  VAL   A CG2 1 
ATOM   62   N N   . ILE   A 1 18  ? 133.650 139.804 132.500 1.00 8.02  ? 18  ILE   A N   1 
ATOM   63   C CA  . ILE   A 1 18  ? 132.579 140.462 133.240 1.00 10.83 ? 18  ILE   A CA  1 
ATOM   64   C C   . ILE   A 1 18  ? 131.788 139.478 134.095 1.00 8.02  ? 18  ILE   A C   1 
ATOM   65   O O   . ILE   A 1 18  ? 131.530 139.762 135.273 1.00 4.38  ? 18  ILE   A O   1 
ATOM   66   C CB  . ILE   A 1 18  ? 131.644 141.220 132.284 1.00 9.24  ? 18  ILE   A CB  1 
ATOM   67   C CG1 . ILE   A 1 18  ? 132.360 142.439 131.703 1.00 10.52 ? 18  ILE   A CG1 1 
ATOM   68   C CG2 . ILE   A 1 18  ? 130.399 141.685 133.013 1.00 9.03  ? 18  ILE   A CG2 1 
ATOM   69   C CD1 . ILE   A 1 18  ? 132.934 143.365 132.753 1.00 13.33 ? 18  ILE   A CD1 1 
ATOM   70   N N   . LEU   A 1 19  ? 131.416 138.317 133.551 1.00 10.46 ? 19  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 19  ? 130.713 137.317 134.341 1.00 13.63 ? 19  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 19  ? 131.572 136.734 135.453 1.00 5.97  ? 19  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 19  ? 131.047 136.445 136.533 1.00 5.99  ? 19  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 19  ? 130.208 136.181 133.447 1.00 12.67 ? 19  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 19  ? 129.375 135.139 134.195 1.00 8.57  ? 19  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 19  ? 127.950 135.633 134.375 1.00 6.25  ? 19  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 19  ? 129.399 133.800 133.494 1.00 13.87 ? 19  LEU   A CD2 1 
ATOM   78   N N   . CYS   A 1 20  ? 132.871 136.553 135.220 1.00 5.15  ? 20  CYS   A N   1 
ATOM   79   C CA  . CYS   A 1 20  ? 133.786 136.116 136.260 1.00 9.18  ? 20  CYS   A CA  1 
ATOM   80   C C   . CYS   A 1 20  ? 133.910 137.133 137.379 1.00 8.93  ? 20  CYS   A C   1 
ATOM   81   O O   . CYS   A 1 20  ? 133.936 136.748 138.550 1.00 10.50 ? 20  CYS   A O   1 
ATOM   82   C CB  . CYS   A 1 20  ? 135.168 135.838 135.663 1.00 7.91  ? 20  CYS   A CB  1 
ATOM   83   S SG  . CYS   A 1 20  ? 135.356 134.188 134.949 1.00 9.18  ? 20  CYS   A SG  1 
ATOM   84   N N   . LEU   A 1 21  ? 133.979 138.424 137.047 1.00 3.46  ? 21  LEU   A N   1 
ATOM   85   C CA  . LEU   A 1 21  ? 133.971 139.454 138.080 1.00 2.67  ? 21  LEU   A CA  1 
ATOM   86   C C   . LEU   A 1 21  ? 132.661 139.439 138.856 1.00 8.93  ? 21  LEU   A C   1 
ATOM   87   O O   . LEU   A 1 21  ? 132.656 139.582 140.085 1.00 4.25  ? 21  LEU   A O   1 
ATOM   88   C CB  . LEU   A 1 21  ? 134.212 140.827 137.455 1.00 9.62  ? 21  LEU   A CB  1 
ATOM   89   C CG  . LEU   A 1 21  ? 135.665 141.169 137.122 1.00 6.61  ? 21  LEU   A CG  1 
ATOM   90   C CD1 . LEU   A 1 21  ? 135.730 142.272 136.079 1.00 6.19  ? 21  LEU   A CD1 1 
ATOM   91   C CD2 . LEU   A 1 21  ? 136.422 141.569 138.378 1.00 1.12  ? 21  LEU   A CD2 1 
ATOM   92   N N   . PHE   A 1 22  ? 131.538 139.266 138.154 1.00 9.17  ? 22  PHE   A N   1 
ATOM   93   C CA  . PHE   A 1 22  ? 130.247 139.182 138.831 1.00 4.18  ? 22  PHE   A CA  1 
ATOM   94   C C   . PHE   A 1 22  ? 130.217 138.015 139.808 1.00 5.46  ? 22  PHE   A C   1 
ATOM   95   O O   . PHE   A 1 22  ? 129.903 138.188 140.990 1.00 3.76  ? 22  PHE   A O   1 
ATOM   96   C CB  . PHE   A 1 22  ? 129.121 139.051 137.804 1.00 2.05  ? 22  PHE   A CB  1 
ATOM   97   C CG  . PHE   A 1 22  ? 127.879 138.398 138.346 1.00 8.71  ? 22  PHE   A CG  1 
ATOM   98   C CD1 . PHE   A 1 22  ? 127.039 139.084 139.205 1.00 5.42  ? 22  PHE   A CD1 1 
ATOM   99   C CD2 . PHE   A 1 22  ? 127.552 137.100 137.994 1.00 -0.00 ? 22  PHE   A CD2 1 
ATOM   100  C CE1 . PHE   A 1 22  ? 125.898 138.489 139.705 1.00 5.85  ? 22  PHE   A CE1 1 
ATOM   101  C CE2 . PHE   A 1 22  ? 126.411 136.500 138.492 1.00 2.95  ? 22  PHE   A CE2 1 
ATOM   102  C CZ  . PHE   A 1 22  ? 125.584 137.195 139.348 1.00 4.95  ? 22  PHE   A CZ  1 
ATOM   103  N N   . GLY   A 1 23  ? 130.565 136.817 139.334 1.00 8.49  ? 23  GLY   A N   1 
ATOM   104  C CA  . GLY   A 1 23  ? 130.574 135.641 140.186 1.00 3.20  ? 23  GLY   A CA  1 
ATOM   105  C C   . GLY   A 1 23  ? 131.590 135.704 141.303 1.00 8.71  ? 23  GLY   A C   1 
ATOM   106  O O   . GLY   A 1 23  ? 131.366 135.111 142.363 1.00 5.86  ? 23  GLY   A O   1 
ATOM   107  N N   . PHE   A 1 24  ? 132.703 136.406 141.090 1.00 4.67  ? 24  PHE   A N   1 
ATOM   108  C CA  . PHE   A 1 24  ? 133.655 136.633 142.166 1.00 13.81 ? 24  PHE   A CA  1 
ATOM   109  C C   . PHE   A 1 24  ? 133.054 137.523 143.242 1.00 11.42 ? 24  PHE   A C   1 
ATOM   110  O O   . PHE   A 1 24  ? 133.075 137.172 144.424 1.00 14.49 ? 24  PHE   A O   1 
ATOM   111  C CB  . PHE   A 1 24  ? 134.937 137.255 141.612 1.00 6.24  ? 24  PHE   A CB  1 
ATOM   112  C CG  . PHE   A 1 24  ? 135.957 137.585 142.665 1.00 5.89  ? 24  PHE   A CG  1 
ATOM   113  C CD1 . PHE   A 1 24  ? 136.793 136.603 143.168 1.00 13.84 ? 24  PHE   A CD1 1 
ATOM   114  C CD2 . PHE   A 1 24  ? 136.088 138.877 143.144 1.00 11.48 ? 24  PHE   A CD2 1 
ATOM   115  C CE1 . PHE   A 1 24  ? 137.733 136.900 144.134 1.00 5.17  ? 24  PHE   A CE1 1 
ATOM   116  C CE2 . PHE   A 1 24  ? 137.027 139.181 144.111 1.00 12.07 ? 24  PHE   A CE2 1 
ATOM   117  C CZ  . PHE   A 1 24  ? 137.851 138.191 144.606 1.00 12.05 ? 24  PHE   A CZ  1 
ATOM   118  N N   . PHE   A 1 25  ? 132.485 138.658 142.850 1.00 13.48 ? 25  PHE   A N   1 
ATOM   119  C CA  . PHE   A 1 25  ? 131.880 139.563 143.813 1.00 11.36 ? 25  PHE   A CA  1 
ATOM   120  C C   . PHE   A 1 25  ? 130.510 139.096 144.288 1.00 5.49  ? 25  PHE   A C   1 
ATOM   121  O O   . PHE   A 1 25  ? 130.021 139.602 145.303 1.00 4.45  ? 25  PHE   A O   1 
ATOM   122  C CB  . PHE   A 1 25  ? 131.781 140.970 143.217 1.00 4.51  ? 25  PHE   A CB  1 
ATOM   123  C CG  . PHE   A 1 25  ? 133.107 141.664 143.096 1.00 4.53  ? 25  PHE   A CG  1 
ATOM   124  C CD1 . PHE   A 1 25  ? 133.814 142.032 144.228 1.00 6.71  ? 25  PHE   A CD1 1 
ATOM   125  C CD2 . PHE   A 1 25  ? 133.653 141.937 141.854 1.00 12.85 ? 25  PHE   A CD2 1 
ATOM   126  C CE1 . PHE   A 1 25  ? 135.036 142.666 144.123 1.00 9.64  ? 25  PHE   A CE1 1 
ATOM   127  C CE2 . PHE   A 1 25  ? 134.875 142.571 141.742 1.00 9.78  ? 25  PHE   A CE2 1 
ATOM   128  C CZ  . PHE   A 1 25  ? 135.567 142.936 142.879 1.00 12.67 ? 25  PHE   A CZ  1 
ATOM   129  N N   . SER   A 1 26  ? 129.885 138.146 143.593 1.00 4.99  ? 26  SER   A N   1 
ATOM   130  C CA  . SER   A 1 26  ? 128.640 137.557 144.067 1.00 6.55  ? 26  SER   A CA  1 
ATOM   131  C C   . SER   A 1 26  ? 128.864 136.384 145.008 1.00 9.61  ? 26  SER   A C   1 
ATOM   132  O O   . SER   A 1 26  ? 127.896 135.894 145.599 1.00 13.45 ? 26  SER   A O   1 
ATOM   133  C CB  . SER   A 1 26  ? 127.774 137.097 142.889 1.00 9.36  ? 26  SER   A CB  1 
ATOM   134  O OG  . SER   A 1 26  ? 127.902 135.702 142.676 1.00 3.94  ? 26  SER   A OG  1 
ATOM   135  N N   . MET   A 1 27  ? 130.103 135.911 145.148 1.00 11.41 ? 27  MET   A N   1 
ATOM   136  C CA  . MET   A 1 27  ? 130.431 134.890 146.131 1.00 5.73  ? 27  MET   A CA  1 
ATOM   137  C C   . MET   A 1 27  ? 131.637 135.245 146.989 1.00 11.47 ? 27  MET   A C   1 
ATOM   138  O O   . MET   A 1 27  ? 132.019 134.442 147.849 1.00 7.28  ? 27  MET   A O   1 
ATOM   139  C CB  . MET   A 1 27  ? 130.660 133.531 145.453 1.00 12.04 ? 27  MET   A CB  1 
ATOM   140  C CG  . MET   A 1 27  ? 129.572 133.133 144.470 1.00 10.87 ? 27  MET   A CG  1 
ATOM   141  S SD  . MET   A 1 27  ? 128.312 132.089 145.233 1.00 8.97  ? 27  MET   A SD  1 
ATOM   142  C CE  . MET   A 1 27  ? 129.086 130.478 145.158 1.00 4.77  ? 27  MET   A CE  1 
ATOM   143  N N   . MET   A 1 28  ? 132.248 136.415 146.791 1.00 8.64  ? 28  MET   A N   1 
ATOM   144  C CA  . MET   A 1 28  ? 133.223 136.937 147.749 1.00 9.25  ? 28  MET   A CA  1 
ATOM   145  C C   . MET   A 1 28  ? 132.420 137.494 148.919 1.00 8.48  ? 28  MET   A C   1 
ATOM   146  O O   . MET   A 1 28  ? 132.234 138.702 149.083 1.00 9.11  ? 28  MET   A O   1 
ATOM   147  C CB  . MET   A 1 28  ? 134.123 137.993 147.117 1.00 10.30 ? 28  MET   A CB  1 
ATOM   148  C CG  . MET   A 1 28  ? 135.330 138.386 147.959 1.00 15.17 ? 28  MET   A CG  1 
ATOM   149  S SD  . MET   A 1 28  ? 135.071 139.848 148.983 1.00 13.64 ? 28  MET   A SD  1 
ATOM   150  C CE  . MET   A 1 28  ? 135.940 141.088 148.027 1.00 8.16  ? 28  MET   A CE  1 
ATOM   151  N N   . ARG   A 1 29  ? 131.913 136.577 149.735 1.00 5.71  ? 29  ARG   A N   1 
ATOM   152  C CA  . ARG   A 1 29  ? 131.012 136.915 150.834 1.00 14.66 ? 29  ARG   A CA  1 
ATOM   153  C C   . ARG   A 1 29  ? 131.683 136.559 152.150 1.00 10.67 ? 29  ARG   A C   1 
ATOM   154  O O   . ARG   A 1 29  ? 131.656 135.387 152.567 1.00 7.02  ? 29  ARG   A O   1 
ATOM   155  C CB  . ARG   A 1 29  ? 129.682 136.180 150.686 1.00 7.51  ? 29  ARG   A CB  1 
ATOM   156  C CG  . ARG   A 1 29  ? 128.679 136.893 149.795 1.00 12.43 ? 29  ARG   A CG  1 
ATOM   157  C CD  . ARG   A 1 29  ? 128.118 135.985 148.721 1.00 6.95  ? 29  ARG   A CD  1 
ATOM   158  N NE  . ARG   A 1 29  ? 127.674 134.702 149.250 1.00 10.81 ? 29  ARG   A NE  1 
ATOM   159  C CZ  . ARG   A 1 29  ? 127.174 133.722 148.511 1.00 14.69 ? 29  ARG   A CZ  1 
ATOM   160  N NH1 . ARG   A 1 29  ? 127.032 133.848 147.202 1.00 13.46 ? 29  ARG   A NH1 1 
ATOM   161  N NH2 . ARG   A 1 29  ? 126.807 132.588 149.099 1.00 7.39  ? 29  ARG   A NH2 1 
ATOM   162  N N   . PRO   A 1 30  ? 132.307 137.522 152.832 1.00 11.95 ? 30  PRO   A N   1 
ATOM   163  C CA  . PRO   A 1 30  ? 132.897 137.224 154.146 1.00 13.21 ? 30  PRO   A CA  1 
ATOM   164  C C   . PRO   A 1 30  ? 131.878 136.768 155.170 1.00 15.30 ? 30  PRO   A C   1 
ATOM   165  O O   . PRO   A 1 30  ? 132.257 136.134 156.162 1.00 8.58  ? 30  PRO   A O   1 
ATOM   166  C CB  . PRO   A 1 30  ? 133.538 138.559 154.549 1.00 7.20  ? 30  PRO   A CB  1 
ATOM   167  C CG  . PRO   A 1 30  ? 133.809 139.245 153.251 1.00 7.71  ? 30  PRO   A CG  1 
ATOM   168  C CD  . PRO   A 1 30  ? 132.655 138.874 152.365 1.00 11.88 ? 30  PRO   A CD  1 
ATOM   169  N N   . SER   A 1 31  ? 130.596 137.077 154.967 1.00 22.59 ? 31  SER   A N   1 
ATOM   170  C CA  . SER   A 1 31  ? 129.572 136.636 155.905 1.00 22.21 ? 31  SER   A CA  1 
ATOM   171  C C   . SER   A 1 31  ? 129.323 135.137 155.812 1.00 19.70 ? 31  SER   A C   1 
ATOM   172  O O   . SER   A 1 31  ? 128.865 134.530 156.785 1.00 26.41 ? 31  SER   A O   1 
ATOM   173  C CB  . SER   A 1 31  ? 128.272 137.399 155.656 1.00 22.32 ? 31  SER   A CB  1 
ATOM   174  O OG  . SER   A 1 31  ? 127.173 136.741 156.261 1.00 20.32 ? 31  SER   A OG  1 
ATOM   175  N N   . GLU   A 1 32  ? 129.608 134.525 154.661 1.00 23.17 ? 32  GLU   A N   1 
ATOM   176  C CA  . GLU   A 1 32  ? 129.298 133.107 154.481 1.00 25.12 ? 32  GLU   A CA  1 
ATOM   177  C C   . GLU   A 1 32  ? 130.030 132.201 155.466 1.00 24.36 ? 32  GLU   A C   1 
ATOM   178  O O   . GLU   A 1 32  ? 129.366 131.367 156.105 1.00 20.31 ? 32  GLU   A O   1 
ATOM   179  C CB  . GLU   A 1 32  ? 129.578 132.700 153.030 1.00 18.33 ? 32  GLU   A CB  1 
ATOM   180  C CG  . GLU   A 1 32  ? 128.496 133.108 152.046 1.00 21.37 ? 32  GLU   A CG  1 
ATOM   181  C CD  . GLU   A 1 32  ? 127.172 132.419 152.305 1.00 23.96 ? 32  GLU   A CD  1 
ATOM   182  O OE1 . GLU   A 1 32  ? 126.355 132.964 153.077 1.00 19.77 ? 32  GLU   A OE1 1 
ATOM   183  O OE2 . GLU   A 1 32  ? 126.947 131.335 151.730 1.00 25.19 ? 32  GLU   A OE2 1 
ATOM   184  N N   . PRO   A 1 33  ? 131.357 132.286 155.640 1.00 11.95 ? 33  PRO   A N   1 
ATOM   185  C CA  . PRO   A 1 33  ? 131.996 131.418 156.647 1.00 13.89 ? 33  PRO   A CA  1 
ATOM   186  C C   . PRO   A 1 33  ? 131.512 131.681 158.061 1.00 19.33 ? 33  PRO   A C   1 
ATOM   187  O O   . PRO   A 1 33  ? 131.418 130.745 158.865 1.00 13.22 ? 33  PRO   A O   1 
ATOM   188  C CB  . PRO   A 1 33  ? 133.490 131.732 156.484 1.00 17.68 ? 33  PRO   A CB  1 
ATOM   189  C CG  . PRO   A 1 33  ? 133.532 133.077 155.866 1.00 16.53 ? 33  PRO   A CG  1 
ATOM   190  C CD  . PRO   A 1 33  ? 132.348 133.138 154.957 1.00 20.53 ? 33  PRO   A CD  1 
ATOM   191  N N   . PHE   A 1 34  ? 131.199 132.932 158.389 1.00 11.34 ? 34  PHE   A N   1 
ATOM   192  C CA  . PHE   A 1 34  ? 130.711 133.310 159.714 1.00 9.37  ? 34  PHE   A CA  1 
ATOM   193  C C   . PHE   A 1 34  ? 129.222 133.627 159.699 1.00 16.06 ? 34  PHE   A C   1 
ATOM   194  O O   . PHE   A 1 34  ? 128.767 134.544 160.388 1.00 16.43 ? 34  PHE   A O   1 
ATOM   195  C CB  . PHE   A 1 34  ? 131.503 134.494 160.268 1.00 17.78 ? 34  PHE   A CB  1 
ATOM   196  C CG  . PHE   A 1 34  ? 132.990 134.261 160.347 1.00 18.03 ? 34  PHE   A CG  1 
ATOM   197  C CD1 . PHE   A 1 34  ? 133.773 134.228 159.204 1.00 11.05 ? 34  PHE   A CD1 1 
ATOM   198  C CD2 . PHE   A 1 34  ? 133.609 134.113 161.576 1.00 8.85  ? 34  PHE   A CD2 1 
ATOM   199  C CE1 . PHE   A 1 34  ? 135.136 134.021 159.287 1.00 18.20 ? 34  PHE   A CE1 1 
ATOM   200  C CE2 . PHE   A 1 34  ? 134.971 133.907 161.664 1.00 14.87 ? 34  PHE   A CE2 1 
ATOM   201  C CZ  . PHE   A 1 34  ? 135.736 133.863 160.519 1.00 18.21 ? 34  PHE   A CZ  1 
ATOM   202  N N   . LEU   A 1 35  ? 128.440 132.886 158.914 1.00 16.39 ? 35  LEU   A N   1 
ATOM   203  C CA  . LEU   A 1 35  ? 127.005 133.125 158.831 1.00 19.98 ? 35  LEU   A CA  1 
ATOM   204  C C   . LEU   A 1 35  ? 126.322 132.733 160.132 1.00 17.24 ? 35  LEU   A C   1 
ATOM   205  O O   . LEU   A 1 35  ? 125.665 133.566 160.764 1.00 14.72 ? 35  LEU   A O   1 
ATOM   206  C CB  . LEU   A 1 35  ? 126.398 132.360 157.650 1.00 15.68 ? 35  LEU   A CB  1 
ATOM   207  C CG  . LEU   A 1 35  ? 124.969 132.716 157.218 1.00 16.87 ? 35  LEU   A CG  1 
ATOM   208  C CD1 . LEU   A 1 35  ? 123.922 131.897 157.966 1.00 16.32 ? 35  LEU   A CD1 1 
ATOM   209  C CD2 . LEU   A 1 35  ? 124.707 134.207 157.387 1.00 20.09 ? 35  LEU   A CD2 1 
ATOM   210  N N   . ILE   A 1 36  ? 126.476 131.470 160.541 1.00 14.09 ? 36  ILE   A N   1 
ATOM   211  C CA  . ILE   A 1 36  ? 125.787 130.989 161.740 1.00 8.85  ? 36  ILE   A CA  1 
ATOM   212  C C   . ILE   A 1 36  ? 126.161 131.795 162.980 1.00 14.54 ? 36  ILE   A C   1 
ATOM   213  O O   . ILE   A 1 36  ? 125.257 132.158 163.748 1.00 6.65  ? 36  ILE   A O   1 
ATOM   214  C CB  . ILE   A 1 36  ? 126.011 129.477 161.910 1.00 6.17  ? 36  ILE   A CB  1 
ATOM   215  C CG1 . ILE   A 1 36  ? 125.036 128.697 161.025 1.00 6.26  ? 36  ILE   A CG1 1 
ATOM   216  C CG2 . ILE   A 1 36  ? 125.852 129.066 163.366 1.00 9.96  ? 36  ILE   A CG2 1 
ATOM   217  C CD1 . ILE   A 1 36  ? 125.050 127.203 161.263 1.00 5.12  ? 36  ILE   A CD1 1 
ATOM   218  N N   . PRO   A 1 37  ? 127.438 132.112 163.238 1.00 17.30 ? 37  PRO   A N   1 
ATOM   219  C CA  . PRO   A 1 37  ? 127.732 133.020 164.360 1.00 16.10 ? 37  PRO   A CA  1 
ATOM   220  C C   . PRO   A 1 37  ? 127.071 134.382 164.231 1.00 7.98  ? 37  PRO   A C   1 
ATOM   221  O O   . PRO   A 1 37  ? 126.762 135.006 165.254 1.00 9.59  ? 37  PRO   A O   1 
ATOM   222  C CB  . PRO   A 1 37  ? 129.265 133.143 164.333 1.00 11.15 ? 37  PRO   A CB  1 
ATOM   223  C CG  . PRO   A 1 37  ? 129.722 132.430 163.103 1.00 9.13  ? 37  PRO   A CG  1 
ATOM   224  C CD  . PRO   A 1 37  ? 128.661 131.456 162.748 1.00 15.92 ? 37  PRO   A CD  1 
ATOM   225  N N   . TYR   A 1 38  ? 126.852 134.869 163.007 1.00 10.44 ? 38  TYR   A N   1 
ATOM   226  C CA  . TYR   A 1 38  ? 126.321 136.218 162.832 1.00 16.40 ? 38  TYR   A CA  1 
ATOM   227  C C   . TYR   A 1 38  ? 124.889 136.326 163.344 1.00 12.82 ? 38  TYR   A C   1 
ATOM   228  O O   . TYR   A 1 38  ? 124.568 137.232 164.121 1.00 15.79 ? 38  TYR   A O   1 
ATOM   229  C CB  . TYR   A 1 38  ? 126.398 136.631 161.362 1.00 15.44 ? 38  TYR   A CB  1 
ATOM   230  C CG  . TYR   A 1 38  ? 125.571 137.853 161.028 1.00 16.05 ? 38  TYR   A CG  1 
ATOM   231  C CD1 . TYR   A 1 38  ? 125.769 139.055 161.696 1.00 11.60 ? 38  TYR   A CD1 1 
ATOM   232  C CD2 . TYR   A 1 38  ? 124.593 137.807 160.045 1.00 12.46 ? 38  TYR   A CD2 1 
ATOM   233  C CE1 . TYR   A 1 38  ? 125.018 140.173 161.394 1.00 14.98 ? 38  TYR   A CE1 1 
ATOM   234  C CE2 . TYR   A 1 38  ? 123.838 138.921 159.739 1.00 9.85  ? 38  TYR   A CE2 1 
ATOM   235  C CZ  . TYR   A 1 38  ? 124.054 140.100 160.415 1.00 11.90 ? 38  TYR   A CZ  1 
ATOM   236  O OH  . TYR   A 1 38  ? 123.302 141.211 160.111 1.00 12.99 ? 38  TYR   A OH  1 
ATOM   237  N N   . LEU   A 1 39  ? 124.011 135.413 162.925 1.00 15.97 ? 39  LEU   A N   1 
ATOM   238  C CA  . LEU   A 1 39  ? 122.613 135.474 163.328 1.00 21.75 ? 39  LEU   A CA  1 
ATOM   239  C C   . LEU   A 1 39  ? 122.348 134.742 164.638 1.00 20.15 ? 39  LEU   A C   1 
ATOM   240  O O   . LEU   A 1 39  ? 121.216 134.768 165.133 1.00 23.89 ? 39  LEU   A O   1 
ATOM   241  C CB  . LEU   A 1 39  ? 121.699 134.920 162.229 1.00 18.97 ? 39  LEU   A CB  1 
ATOM   242  C CG  . LEU   A 1 39  ? 121.533 133.405 162.082 1.00 24.75 ? 39  LEU   A CG  1 
ATOM   243  C CD1 . LEU   A 1 39  ? 120.349 133.076 161.198 1.00 21.60 ? 39  LEU   A CD1 1 
ATOM   244  C CD2 . LEU   A 1 39  ? 122.770 132.772 161.510 1.00 17.66 ? 39  LEU   A CD2 1 
ATOM   245  N N   . SER   A 1 40  ? 123.363 134.099 165.215 1.00 24.26 ? 40  SER   A N   1 
ATOM   246  C CA  . SER   A 1 40  ? 123.229 133.479 166.525 1.00 22.50 ? 40  SER   A CA  1 
ATOM   247  C C   . SER   A 1 40  ? 123.955 134.232 167.627 1.00 16.92 ? 40  SER   A C   1 
ATOM   248  O O   . SER   A 1 40  ? 123.780 133.885 168.800 1.00 20.58 ? 40  SER   A O   1 
ATOM   249  C CB  . SER   A 1 40  ? 123.738 132.029 166.495 1.00 23.17 ? 40  SER   A CB  1 
ATOM   250  O OG  . SER   A 1 40  ? 123.295 131.309 167.633 1.00 25.57 ? 40  SER   A OG  1 
ATOM   251  N N   . GLY   A 1 41  ? 124.754 135.243 167.296 1.00 26.04 ? 41  GLY   A N   1 
ATOM   252  C CA  . GLY   A 1 41  ? 125.438 136.034 168.288 1.00 35.81 ? 41  GLY   A CA  1 
ATOM   253  C C   . GLY   A 1 41  ? 124.627 137.243 168.703 1.00 29.81 ? 41  GLY   A C   1 
ATOM   254  O O   . GLY   A 1 41  ? 123.404 137.287 168.538 1.00 35.78 ? 41  GLY   A O   1 
ATOM   255  N N   . PRO   A 1 42  ? 125.299 138.255 169.255 1.00 37.15 ? 42  PRO   A N   1 
ATOM   256  C CA  . PRO   A 1 42  ? 124.579 139.465 169.686 1.00 39.39 ? 42  PRO   A CA  1 
ATOM   257  C C   . PRO   A 1 42  ? 123.952 140.244 168.543 1.00 36.85 ? 42  PRO   A C   1 
ATOM   258  O O   . PRO   A 1 42  ? 123.076 141.081 168.795 1.00 37.39 ? 42  PRO   A O   1 
ATOM   259  C CB  . PRO   A 1 42  ? 125.664 140.288 170.394 1.00 33.96 ? 42  PRO   A CB  1 
ATOM   260  C CG  . PRO   A 1 42  ? 126.953 139.793 169.829 1.00 36.97 ? 42  PRO   A CG  1 
ATOM   261  C CD  . PRO   A 1 42  ? 126.748 138.344 169.501 1.00 38.60 ? 42  PRO   A CD  1 
ATOM   262  N N   . ASP   A 1 43  ? 124.377 140.007 167.300 1.00 31.49 ? 43  ASP   A N   1 
ATOM   263  C CA  . ASP   A 1 43  ? 123.862 140.784 166.175 1.00 30.46 ? 43  ASP   A CA  1 
ATOM   264  C C   . ASP   A 1 43  ? 122.371 140.544 165.969 1.00 29.89 ? 43  ASP   A C   1 
ATOM   265  O O   . ASP   A 1 43  ? 121.601 141.490 165.765 1.00 31.55 ? 43  ASP   A O   1 
ATOM   266  C CB  . ASP   A 1 43  ? 124.645 140.444 164.907 1.00 26.13 ? 43  ASP   A CB  1 
ATOM   267  C CG  . ASP   A 1 43  ? 125.881 141.305 164.739 1.00 29.61 ? 43  ASP   A CG  1 
ATOM   268  O OD1 . ASP   A 1 43  ? 125.753 142.546 164.790 1.00 27.41 ? 43  ASP   A OD1 1 
ATOM   269  O OD2 . ASP   A 1 43  ? 126.980 140.740 164.557 1.00 26.73 ? 43  ASP   A OD2 1 
ATOM   270  N N   . LYS   A 1 44  ? 121.941 139.281 166.018 1.00 16.20 ? 44  LYS   A N   1 
ATOM   271  C CA  . LYS   A 1 44  ? 120.538 138.939 165.832 1.00 16.11 ? 44  LYS   A CA  1 
ATOM   272  C C   . LYS   A 1 44  ? 119.901 138.278 167.045 1.00 15.27 ? 44  LYS   A C   1 
ATOM   273  O O   . LYS   A 1 44  ? 118.678 138.364 167.198 1.00 18.31 ? 44  LYS   A O   1 
ATOM   274  C CB  . LYS   A 1 44  ? 120.369 138.014 164.619 1.00 16.39 ? 44  LYS   A CB  1 
ATOM   275  C CG  . LYS   A 1 44  ? 120.848 138.616 163.310 1.00 21.83 ? 44  LYS   A CG  1 
ATOM   276  C CD  . LYS   A 1 44  ? 119.794 138.484 162.225 1.00 18.87 ? 44  LYS   A CD  1 
ATOM   277  C CE  . LYS   A 1 44  ? 120.008 139.509 161.128 1.00 14.08 ? 44  LYS   A CE  1 
ATOM   278  N NZ  . LYS   A 1 44  ? 120.083 140.894 161.667 1.00 16.36 ? 44  LYS   A NZ  1 
ATOM   279  N N   . ASN   A 1 45  ? 120.691 137.621 167.896 1.00 20.62 ? 45  ASN   A N   1 
ATOM   280  C CA  . ASN   A 1 45  ? 120.203 137.000 169.129 1.00 25.16 ? 45  ASN   A CA  1 
ATOM   281  C C   . ASN   A 1 45  ? 119.129 135.948 168.848 1.00 25.98 ? 45  ASN   A C   1 
ATOM   282  O O   . ASN   A 1 45  ? 118.171 135.786 169.606 1.00 26.22 ? 45  ASN   A O   1 
ATOM   283  C CB  . ASN   A 1 45  ? 119.691 138.059 170.110 1.00 23.81 ? 45  ASN   A CB  1 
ATOM   284  C CG  . ASN   A 1 45  ? 120.801 138.659 170.951 1.00 19.89 ? 45  ASN   A CG  1 
ATOM   285  O OD1 . ASN   A 1 45  ? 121.770 137.982 171.295 1.00 19.71 ? 45  ASN   A OD1 1 
ATOM   286  N ND2 . ASN   A 1 45  ? 120.664 139.936 171.287 1.00 25.73 ? 45  ASN   A ND2 1 
ATOM   287  N N   . LEU   A 1 46  ? 119.294 135.229 167.742 1.00 33.29 ? 46  LEU   A N   1 
ATOM   288  C CA  . LEU   A 1 46  ? 118.421 134.108 167.431 1.00 36.03 ? 46  LEU   A CA  1 
ATOM   289  C C   . LEU   A 1 46  ? 118.983 132.818 168.024 1.00 33.74 ? 46  LEU   A C   1 
ATOM   290  O O   . LEU   A 1 46  ? 120.193 132.581 168.037 1.00 35.34 ? 46  LEU   A O   1 
ATOM   291  C CB  . LEU   A 1 46  ? 118.239 133.964 165.920 1.00 33.20 ? 46  LEU   A CB  1 
ATOM   292  C CG  . LEU   A 1 46  ? 117.952 135.232 165.115 1.00 35.72 ? 46  LEU   A CG  1 
ATOM   293  C CD1 . LEU   A 1 46  ? 117.897 134.917 163.628 1.00 33.70 ? 46  LEU   A CD1 1 
ATOM   294  C CD2 . LEU   A 1 46  ? 116.658 135.883 165.575 1.00 32.67 ? 46  LEU   A CD2 1 
ATOM   295  N N   . THR   A 1 47  ? 118.083 131.973 168.520 1.00 39.36 ? 47  THR   A N   1 
ATOM   296  C CA  . THR   A 1 47  ? 118.496 130.707 169.101 1.00 36.61 ? 47  THR   A CA  1 
ATOM   297  C C   . THR   A 1 47  ? 118.845 129.704 168.003 1.00 39.71 ? 47  THR   A C   1 
ATOM   298  O O   . THR   A 1 47  ? 118.324 129.755 166.886 1.00 36.73 ? 47  THR   A O   1 
ATOM   299  C CB  . THR   A 1 47  ? 117.403 130.146 170.017 1.00 45.76 ? 47  THR   A CB  1 
ATOM   300  O OG1 . THR   A 1 47  ? 117.971 129.174 170.904 1.00 37.75 ? 47  THR   A OG1 1 
ATOM   301  C CG2 . THR   A 1 47  ? 116.285 129.502 169.209 1.00 44.05 ? 47  THR   A CG2 1 
ATOM   302  N N   . SER   A 1 48  ? 119.752 128.789 168.335 1.00 38.53 ? 48  SER   A N   1 
ATOM   303  C CA  . SER   A 1 48  ? 120.272 127.823 167.376 1.00 36.66 ? 48  SER   A CA  1 
ATOM   304  C C   . SER   A 1 48  ? 119.254 126.762 166.977 1.00 35.48 ? 48  SER   A C   1 
ATOM   305  O O   . SER   A 1 48  ? 119.474 126.058 165.986 1.00 31.39 ? 48  SER   A O   1 
ATOM   306  C CB  . SER   A 1 48  ? 121.525 127.145 167.940 1.00 34.45 ? 48  SER   A CB  1 
ATOM   307  O OG  . SER   A 1 48  ? 122.110 126.279 166.983 1.00 33.23 ? 48  SER   A OG  1 
ATOM   308  N N   . ALA   A 1 49  ? 118.152 126.630 167.715 1.00 41.83 ? 49  ALA   A N   1 
ATOM   309  C CA  . ALA   A 1 49  ? 117.109 125.660 167.409 1.00 45.50 ? 49  ALA   A CA  1 
ATOM   310  C C   . ALA   A 1 49  ? 116.046 126.248 166.486 1.00 42.70 ? 49  ALA   A C   1 
ATOM   311  O O   . ALA   A 1 49  ? 115.049 125.592 166.174 1.00 48.74 ? 49  ALA   A O   1 
ATOM   312  C CB  . ALA   A 1 49  ? 116.470 125.136 168.694 1.00 48.67 ? 49  ALA   A CB  1 
ATOM   313  N N   . GLU   A 1 50  ? 116.253 127.486 166.043 1.00 30.97 ? 50  GLU   A N   1 
ATOM   314  C CA  . GLU   A 1 50  ? 115.312 128.173 165.168 1.00 29.51 ? 50  GLU   A CA  1 
ATOM   315  C C   . GLU   A 1 50  ? 116.060 128.646 163.925 1.00 30.33 ? 50  GLU   A C   1 
ATOM   316  O O   . GLU   A 1 50  ? 115.460 129.136 162.962 1.00 33.39 ? 50  GLU   A O   1 
ATOM   317  C CB  . GLU   A 1 50  ? 114.639 129.316 165.948 1.00 35.68 ? 50  GLU   A CB  1 
ATOM   318  C CG  . GLU   A 1 50  ? 114.318 130.596 165.192 1.00 30.48 ? 50  GLU   A CG  1 
ATOM   319  C CD  . GLU   A 1 50  ? 114.029 131.759 166.121 1.00 30.88 ? 50  GLU   A CD  1 
ATOM   320  O OE1 . GLU   A 1 50  ? 112.839 132.035 166.379 1.00 36.91 ? 50  GLU   A OE1 1 
ATOM   321  O OE2 . GLU   A 1 50  ? 114.993 132.396 166.597 1.00 32.56 ? 50  GLU   A OE2 1 
ATOM   322  N N   . ILE   A 1 51  ? 117.371 128.412 163.908 1.00 27.86 ? 51  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 51  ? 118.234 128.825 162.808 1.00 24.03 ? 51  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 51  ? 118.435 127.639 161.873 1.00 22.71 ? 51  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 51  ? 118.624 127.807 160.663 1.00 26.85 ? 51  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 51  ? 119.579 129.355 163.342 1.00 26.46 ? 51  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 51  ? 119.371 130.664 164.101 1.00 23.22 ? 51  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 51  ? 120.577 129.569 162.214 1.00 27.91 ? 51  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 51  ? 120.631 131.201 164.734 1.00 27.13 ? 51  ILE   A CD1 1 
ATOM   330  N N   . THR   A 1 52  ? 118.364 126.428 162.423 1.00 26.24 ? 52  THR   A N   1 
ATOM   331  C CA  . THR   A 1 52  ? 118.572 125.215 161.643 1.00 21.14 ? 52  THR   A CA  1 
ATOM   332  C C   . THR   A 1 52  ? 117.320 124.375 161.449 1.00 27.21 ? 52  THR   A C   1 
ATOM   333  O O   . THR   A 1 52  ? 117.251 123.637 160.459 1.00 21.92 ? 52  THR   A O   1 
ATOM   334  C CB  . THR   A 1 52  ? 119.650 124.335 162.294 1.00 24.89 ? 52  THR   A CB  1 
ATOM   335  O OG1 . THR   A 1 52  ? 119.253 124.000 163.630 1.00 27.55 ? 52  THR   A OG1 1 
ATOM   336  C CG2 . THR   A 1 52  ? 120.980 125.071 162.338 1.00 19.92 ? 52  THR   A CG2 1 
ATOM   337  N N   . ASN   A 1 53  ? 116.337 124.452 162.345 1.00 27.03 ? 53  ASN   A N   1 
ATOM   338  C CA  . ASN   A 1 53  ? 115.101 123.698 162.207 1.00 32.52 ? 53  ASN   A CA  1 
ATOM   339  C C   . ASN   A 1 53  ? 113.964 124.510 161.606 1.00 32.24 ? 53  ASN   A C   1 
ATOM   340  O O   . ASN   A 1 53  ? 112.933 123.931 161.249 1.00 29.18 ? 53  ASN   A O   1 
ATOM   341  C CB  . ASN   A 1 53  ? 114.658 123.147 163.571 1.00 32.46 ? 53  ASN   A CB  1 
ATOM   342  C CG  . ASN   A 1 53  ? 115.544 122.020 164.059 1.00 33.29 ? 53  ASN   A CG  1 
ATOM   343  O OD1 . ASN   A 1 53  ? 116.242 121.380 163.274 1.00 32.06 ? 53  ASN   A OD1 1 
ATOM   344  N ND2 . ASN   A 1 53  ? 115.523 121.772 165.364 1.00 32.33 ? 53  ASN   A ND2 1 
ATOM   345  N N   . GLU   A 1 54  ? 114.121 125.826 161.485 1.00 34.41 ? 54  GLU   A N   1 
ATOM   346  C CA  . GLU   A 1 54  ? 113.073 126.687 160.955 1.00 39.93 ? 54  GLU   A CA  1 
ATOM   347  C C   . GLU   A 1 54  ? 113.562 127.671 159.900 1.00 40.45 ? 54  GLU   A C   1 
ATOM   348  O O   . GLU   A 1 54  ? 112.761 128.079 159.049 1.00 39.52 ? 54  GLU   A O   1 
ATOM   349  C CB  . GLU   A 1 54  ? 112.390 127.445 162.109 1.00 41.41 ? 54  GLU   A CB  1 
ATOM   350  C CG  . GLU   A 1 54  ? 111.793 128.804 161.784 1.00 33.76 ? 54  GLU   A CG  1 
ATOM   351  C CD  . GLU   A 1 54  ? 111.056 129.402 162.967 1.00 41.12 ? 54  GLU   A CD  1 
ATOM   352  O OE1 . GLU   A 1 54  ? 110.687 130.594 162.901 1.00 40.74 ? 54  GLU   A OE1 1 
ATOM   353  O OE2 . GLU   A 1 54  ? 110.845 128.678 163.962 1.00 36.02 ? 54  GLU   A OE2 1 
ATOM   354  N N   . ILE   A 1 55  ? 114.843 128.023 159.889 1.00 17.19 ? 55  ILE   A N   1 
ATOM   355  C CA  . ILE   A 1 55  ? 115.386 129.014 158.963 1.00 20.94 ? 55  ILE   A CA  1 
ATOM   356  C C   . ILE   A 1 55  ? 116.012 128.358 157.735 1.00 18.07 ? 55  ILE   A C   1 
ATOM   357  O O   . ILE   A 1 55  ? 115.713 128.737 156.602 1.00 22.59 ? 55  ILE   A O   1 
ATOM   358  C CB  . ILE   A 1 55  ? 116.394 129.922 159.703 1.00 19.08 ? 55  ILE   A CB  1 
ATOM   359  C CG1 . ILE   A 1 55  ? 115.661 131.080 160.375 1.00 22.45 ? 55  ILE   A CG1 1 
ATOM   360  C CG2 . ILE   A 1 55  ? 117.461 130.447 158.767 1.00 24.53 ? 55  ILE   A CG2 1 
ATOM   361  C CD1 . ILE   A 1 55  ? 114.970 131.991 159.396 1.00 17.62 ? 55  ILE   A CD1 1 
ATOM   362  N N   . PHE   A 1 56  ? 116.881 127.369 157.937 1.00 16.84 ? 56  PHE   A N   1 
ATOM   363  C CA  . PHE   A 1 56  ? 117.523 126.707 156.802 1.00 24.42 ? 56  PHE   A CA  1 
ATOM   364  C C   . PHE   A 1 56  ? 116.578 125.829 155.982 1.00 20.82 ? 56  PHE   A C   1 
ATOM   365  O O   . PHE   A 1 56  ? 116.748 125.777 154.749 1.00 25.15 ? 56  PHE   A O   1 
ATOM   366  C CB  . PHE   A 1 56  ? 118.731 125.897 157.293 1.00 21.77 ? 56  PHE   A CB  1 
ATOM   367  C CG  . PHE   A 1 56  ? 119.906 126.743 157.711 1.00 25.34 ? 56  PHE   A CG  1 
ATOM   368  C CD1 . PHE   A 1 56  ? 119.856 128.125 157.615 1.00 20.87 ? 56  PHE   A CD1 1 
ATOM   369  C CD2 . PHE   A 1 56  ? 121.059 126.154 158.200 1.00 20.67 ? 56  PHE   A CD2 1 
ATOM   370  C CE1 . PHE   A 1 56  ? 120.933 128.901 157.999 1.00 16.76 ? 56  PHE   A CE1 1 
ATOM   371  C CE2 . PHE   A 1 56  ? 122.140 126.926 158.586 1.00 18.96 ? 56  PHE   A CE2 1 
ATOM   372  C CZ  . PHE   A 1 56  ? 122.076 128.301 158.484 1.00 15.67 ? 56  PHE   A CZ  1 
ATOM   373  N N   . PRO   A 1 57  ? 115.617 125.102 156.565 1.00 11.93 ? 57  PRO   A N   1 
ATOM   374  C CA  . PRO   A 1 57  ? 114.621 124.429 155.715 1.00 17.78 ? 57  PRO   A CA  1 
ATOM   375  C C   . PRO   A 1 57  ? 113.839 125.394 154.847 1.00 10.63 ? 57  PRO   A C   1 
ATOM   376  O O   . PRO   A 1 57  ? 113.438 125.029 153.734 1.00 13.99 ? 57  PRO   A O   1 
ATOM   377  C CB  . PRO   A 1 57  ? 113.715 123.711 156.728 1.00 18.95 ? 57  PRO   A CB  1 
ATOM   378  C CG  . PRO   A 1 57  ? 114.013 124.347 158.046 1.00 17.25 ? 57  PRO   A CG  1 
ATOM   379  C CD  . PRO   A 1 57  ? 115.454 124.718 157.977 1.00 17.23 ? 57  PRO   A CD  1 
ATOM   380  N N   . VAL   A 1 58  ? 113.614 126.620 155.322 1.00 8.13  ? 58  VAL   A N   1 
ATOM   381  C CA  . VAL   A 1 58  ? 112.971 127.632 154.489 1.00 10.66 ? 58  VAL   A CA  1 
ATOM   382  C C   . VAL   A 1 58  ? 113.840 127.948 153.280 1.00 12.06 ? 58  VAL   A C   1 
ATOM   383  O O   . VAL   A 1 58  ? 113.340 128.070 152.154 1.00 16.14 ? 58  VAL   A O   1 
ATOM   384  C CB  . VAL   A 1 58  ? 112.662 128.891 155.321 1.00 8.28  ? 58  VAL   A CB  1 
ATOM   385  C CG1 . VAL   A 1 58  ? 112.649 130.131 154.440 1.00 8.72  ? 58  VAL   A CG1 1 
ATOM   386  C CG2 . VAL   A 1 58  ? 111.333 128.728 156.038 1.00 8.86  ? 58  VAL   A CG2 1 
ATOM   387  N N   . TRP   A 1 59  ? 115.154 128.074 153.487 1.00 13.17 ? 59  TRP   A N   1 
ATOM   388  C CA  . TRP   A 1 59  ? 116.054 128.286 152.359 1.00 10.24 ? 59  TRP   A CA  1 
ATOM   389  C C   . TRP   A 1 59  ? 116.001 127.122 151.384 1.00 6.24  ? 59  TRP   A C   1 
ATOM   390  O O   . TRP   A 1 59  ? 115.995 127.326 150.168 1.00 10.75 ? 59  TRP   A O   1 
ATOM   391  C CB  . TRP   A 1 59  ? 117.493 128.481 152.830 1.00 7.79  ? 59  TRP   A CB  1 
ATOM   392  C CG  . TRP   A 1 59  ? 118.459 128.367 151.687 1.00 13.66 ? 59  TRP   A CG  1 
ATOM   393  C CD1 . TRP   A 1 59  ? 118.578 129.221 150.631 1.00 8.64  ? 59  TRP   A CD1 1 
ATOM   394  C CD2 . TRP   A 1 59  ? 119.404 127.314 151.459 1.00 5.95  ? 59  TRP   A CD2 1 
ATOM   395  N NE1 . TRP   A 1 59  ? 119.553 128.778 149.770 1.00 11.60 ? 59  TRP   A NE1 1 
ATOM   396  C CE2 . TRP   A 1 59  ? 120.076 127.610 150.257 1.00 14.11 ? 59  TRP   A CE2 1 
ATOM   397  C CE3 . TRP   A 1 59  ? 119.755 126.157 152.160 1.00 9.48  ? 59  TRP   A CE3 1 
ATOM   398  C CZ2 . TRP   A 1 59  ? 121.078 126.792 149.740 1.00 13.17 ? 59  TRP   A CZ2 1 
ATOM   399  C CZ3 . TRP   A 1 59  ? 120.751 125.346 151.646 1.00 10.78 ? 59  TRP   A CZ3 1 
ATOM   400  C CH2 . TRP   A 1 59  ? 121.401 125.667 150.448 1.00 11.08 ? 59  TRP   A CH2 1 
ATOM   401  N N   . THR   A 1 60  ? 115.989 125.891 151.898 1.00 11.77 ? 60  THR   A N   1 
ATOM   402  C CA  . THR   A 1 60  ? 115.955 124.728 151.012 1.00 10.21 ? 60  THR   A CA  1 
ATOM   403  C C   . THR   A 1 60  ? 114.670 124.695 150.189 1.00 2.50  ? 60  THR   A C   1 
ATOM   404  O O   . THR   A 1 60  ? 114.701 124.453 148.973 1.00 9.27  ? 60  THR   A O   1 
ATOM   405  C CB  . THR   A 1 60  ? 116.102 123.442 151.825 1.00 6.82  ? 60  THR   A CB  1 
ATOM   406  O OG1 . THR   A 1 60  ? 117.283 123.518 152.634 1.00 11.65 ? 60  THR   A OG1 1 
ATOM   407  C CG2 . THR   A 1 60  ? 116.205 122.239 150.902 1.00 4.39  ? 60  THR   A CG2 1 
ATOM   408  N N   . TYR   A 1 61  ? 113.530 124.945 150.834 1.00 6.48  ? 61  TYR   A N   1 
ATOM   409  C CA  . TYR   A 1 61  ? 112.255 124.931 150.124 1.00 4.63  ? 61  TYR   A CA  1 
ATOM   410  C C   . TYR   A 1 61  ? 112.185 126.053 149.096 1.00 8.10  ? 61  TYR   A C   1 
ATOM   411  O O   . TYR   A 1 61  ? 111.700 125.850 147.976 1.00 4.90  ? 61  TYR   A O   1 
ATOM   412  C CB  . TYR   A 1 61  ? 111.096 125.032 151.118 1.00 10.15 ? 61  TYR   A CB  1 
ATOM   413  C CG  . TYR   A 1 61  ? 110.924 123.823 152.020 1.00 11.84 ? 61  TYR   A CG  1 
ATOM   414  C CD1 . TYR   A 1 61  ? 111.836 122.774 152.005 1.00 11.47 ? 61  TYR   A CD1 1 
ATOM   415  C CD2 . TYR   A 1 61  ? 109.832 123.724 152.873 1.00 10.78 ? 61  TYR   A CD2 1 
ATOM   416  C CE1 . TYR   A 1 61  ? 111.676 121.673 152.823 1.00 12.27 ? 61  TYR   A CE1 1 
ATOM   417  C CE2 . TYR   A 1 61  ? 109.664 122.627 153.696 1.00 7.24  ? 61  TYR   A CE2 1 
ATOM   418  C CZ  . TYR   A 1 61  ? 110.587 121.604 153.666 1.00 8.10  ? 61  TYR   A CZ  1 
ATOM   419  O OH  . TYR   A 1 61  ? 110.422 120.508 154.482 1.00 12.05 ? 61  TYR   A OH  1 
ATOM   420  N N   . SER   A 1 62  ? 112.663 127.248 149.457 1.00 10.67 ? 62  SER   A N   1 
ATOM   421  C CA  . SER   A 1 62  ? 112.694 128.345 148.499 1.00 5.84  ? 62  SER   A CA  1 
ATOM   422  C C   . SER   A 1 62  ? 113.645 128.051 147.351 1.00 5.19  ? 62  SER   A C   1 
ATOM   423  O O   . SER   A 1 62  ? 113.367 128.425 146.210 1.00 4.59  ? 62  SER   A O   1 
ATOM   424  C CB  . SER   A 1 62  ? 113.089 129.643 149.199 1.00 5.07  ? 62  SER   A CB  1 
ATOM   425  O OG  . SER   A 1 62  ? 112.104 130.030 150.141 1.00 8.99  ? 62  SER   A OG  1 
ATOM   426  N N   . TYR   A 1 63  ? 114.758 127.372 147.630 1.00 3.87  ? 63  TYR   A N   1 
ATOM   427  C CA  . TYR   A 1 63  ? 115.669 126.945 146.576 1.00 3.02  ? 63  TYR   A CA  1 
ATOM   428  C C   . TYR   A 1 63  ? 114.966 126.015 145.598 1.00 10.29 ? 63  TYR   A C   1 
ATOM   429  O O   . TYR   A 1 63  ? 115.096 126.172 144.381 1.00 6.69  ? 63  TYR   A O   1 
ATOM   430  C CB  . TYR   A 1 63  ? 116.885 126.266 147.211 1.00 10.21 ? 63  TYR   A CB  1 
ATOM   431  C CG  . TYR   A 1 63  ? 118.104 126.109 146.325 1.00 7.26  ? 63  TYR   A CG  1 
ATOM   432  C CD1 . TYR   A 1 63  ? 118.120 126.589 145.024 1.00 7.24  ? 63  TYR   A CD1 1 
ATOM   433  C CD2 . TYR   A 1 63  ? 119.247 125.481 146.803 1.00 7.52  ? 63  TYR   A CD2 1 
ATOM   434  C CE1 . TYR   A 1 63  ? 119.236 126.439 144.224 1.00 7.48  ? 63  TYR   A CE1 1 
ATOM   435  C CE2 . TYR   A 1 63  ? 120.366 125.329 146.010 1.00 10.77 ? 63  TYR   A CE2 1 
ATOM   436  C CZ  . TYR   A 1 63  ? 120.355 125.811 144.721 1.00 6.76  ? 63  TYR   A CZ  1 
ATOM   437  O OH  . TYR   A 1 63  ? 121.468 125.664 143.926 1.00 11.78 ? 63  TYR   A OH  1 
ATOM   438  N N   . LEU   A 1 64  ? 114.190 125.058 146.113 1.00 0.34  ? 64  LEU   A N   1 
ATOM   439  C CA  . LEU   A 1 64  ? 113.448 124.158 145.231 1.00 1.50  ? 64  LEU   A CA  1 
ATOM   440  C C   . LEU   A 1 64  ? 112.422 124.917 144.390 1.00 1.23  ? 64  LEU   A C   1 
ATOM   441  O O   . LEU   A 1 64  ? 112.408 124.814 143.154 1.00 6.16  ? 64  LEU   A O   1 
ATOM   442  C CB  . LEU   A 1 64  ? 112.756 123.070 146.055 1.00 0.07  ? 64  LEU   A CB  1 
ATOM   443  C CG  . LEU   A 1 64  ? 113.614 121.940 146.622 1.00 5.36  ? 64  LEU   A CG  1 
ATOM   444  C CD1 . LEU   A 1 64  ? 112.895 121.234 147.760 1.00 0.00  ? 64  LEU   A CD1 1 
ATOM   445  C CD2 . LEU   A 1 64  ? 113.980 120.956 145.527 1.00 3.27  ? 64  LEU   A CD2 1 
ATOM   446  N N   . VAL   A 1 65  ? 111.563 125.702 145.047 1.00 9.03  ? 65  VAL   A N   1 
ATOM   447  C CA  . VAL   A 1 65  ? 110.464 126.367 144.352 1.00 7.93  ? 65  VAL   A CA  1 
ATOM   448  C C   . VAL   A 1 65  ? 110.928 127.568 143.541 1.00 9.12  ? 65  VAL   A C   1 
ATOM   449  O O   . VAL   A 1 65  ? 110.136 128.144 142.788 1.00 1.43  ? 65  VAL   A O   1 
ATOM   450  C CB  . VAL   A 1 65  ? 109.363 126.767 145.359 1.00 1.55  ? 65  VAL   A CB  1 
ATOM   451  C CG1 . VAL   A 1 65  ? 108.055 127.083 144.646 1.00 1.85  ? 65  VAL   A CG1 1 
ATOM   452  C CG2 . VAL   A 1 65  ? 109.127 125.645 146.350 1.00 6.20  ? 65  VAL   A CG2 1 
ATOM   453  N N   . LEU   A 1 66  ? 112.196 127.958 143.662 1.00 9.03  ? 66  LEU   A N   1 
ATOM   454  C CA  . LEU   A 1 66  ? 112.760 128.984 142.801 1.00 9.87  ? 66  LEU   A CA  1 
ATOM   455  C C   . LEU   A 1 66  ? 113.615 128.410 141.685 1.00 7.08  ? 66  LEU   A C   1 
ATOM   456  O O   . LEU   A 1 66  ? 113.763 129.061 140.647 1.00 7.29  ? 66  LEU   A O   1 
ATOM   457  C CB  . LEU   A 1 66  ? 113.593 129.973 143.623 1.00 9.06  ? 66  LEU   A CB  1 
ATOM   458  C CG  . LEU   A 1 66  ? 112.857 131.259 143.993 1.00 3.98  ? 66  LEU   A CG  1 
ATOM   459  C CD1 . LEU   A 1 66  ? 112.444 132.012 142.739 1.00 2.47  ? 66  LEU   A CD1 1 
ATOM   460  C CD2 . LEU   A 1 66  ? 111.647 130.954 144.855 1.00 1.71  ? 66  LEU   A CD2 1 
ATOM   461  N N   . LEU   A 1 67  ? 114.180 127.216 141.870 1.00 1.11  ? 67  LEU   A N   1 
ATOM   462  C CA  . LEU   A 1 67  ? 114.758 126.499 140.744 1.00 8.04  ? 67  LEU   A CA  1 
ATOM   463  C C   . LEU   A 1 67  ? 113.676 126.042 139.782 1.00 1.38  ? 67  LEU   A C   1 
ATOM   464  O O   . LEU   A 1 67  ? 113.911 125.993 138.570 1.00 2.55  ? 67  LEU   A O   1 
ATOM   465  C CB  . LEU   A 1 67  ? 115.565 125.298 141.234 1.00 8.10  ? 67  LEU   A CB  1 
ATOM   466  C CG  . LEU   A 1 67  ? 117.074 125.477 141.374 1.00 3.02  ? 67  LEU   A CG  1 
ATOM   467  C CD1 . LEU   A 1 67  ? 117.674 124.256 142.041 1.00 9.73  ? 67  LEU   A CD1 1 
ATOM   468  C CD2 . LEU   A 1 67  ? 117.715 125.723 140.019 1.00 2.58  ? 67  LEU   A CD2 1 
ATOM   469  N N   . LEU   A 1 68  ? 112.491 125.713 140.301 1.00 10.53 ? 68  LEU   A N   1 
ATOM   470  C CA  . LEU   A 1 68  ? 111.392 125.277 139.439 1.00 8.34  ? 68  LEU   A CA  1 
ATOM   471  C C   . LEU   A 1 68  ? 111.094 126.242 138.295 1.00 14.30 ? 68  LEU   A C   1 
ATOM   472  O O   . LEU   A 1 68  ? 110.922 125.774 137.159 1.00 8.86  ? 68  LEU   A O   1 
ATOM   473  C CB  . LEU   A 1 68  ? 110.142 125.020 140.293 1.00 9.53  ? 68  LEU   A CB  1 
ATOM   474  C CG  . LEU   A 1 68  ? 109.921 123.576 140.745 1.00 10.32 ? 68  LEU   A CG  1 
ATOM   475  C CD1 . LEU   A 1 68  ? 108.681 123.474 141.618 1.00 14.58 ? 68  LEU   A CD1 1 
ATOM   476  C CD2 . LEU   A 1 68  ? 109.813 122.652 139.543 1.00 5.50  ? 68  LEU   A CD2 1 
ATOM   477  N N   . PRO   A 1 69  ? 111.018 127.560 138.495 1.00 10.15 ? 69  PRO   A N   1 
ATOM   478  C CA  . PRO   A 1 69  ? 110.878 128.474 137.353 1.00 11.89 ? 69  PRO   A CA  1 
ATOM   479  C C   . PRO   A 1 69  ? 112.184 129.027 136.797 1.00 3.25  ? 69  PRO   A C   1 
ATOM   480  O O   . PRO   A 1 69  ? 112.130 129.923 135.950 1.00 8.20  ? 69  PRO   A O   1 
ATOM   481  C CB  . PRO   A 1 69  ? 110.035 129.608 137.949 1.00 6.24  ? 69  PRO   A CB  1 
ATOM   482  C CG  . PRO   A 1 69  ? 110.497 129.689 139.345 1.00 11.57 ? 69  PRO   A CG  1 
ATOM   483  C CD  . PRO   A 1 69  ? 110.841 128.280 139.769 1.00 8.56  ? 69  PRO   A CD  1 
ATOM   484  N N   . VAL   A 1 70  ? 113.344 128.539 137.236 1.00 11.62 ? 70  VAL   A N   1 
ATOM   485  C CA  . VAL   A 1 70  ? 114.604 129.010 136.666 1.00 9.25  ? 70  VAL   A CA  1 
ATOM   486  C C   . VAL   A 1 70  ? 114.907 128.284 135.362 1.00 11.00 ? 70  VAL   A C   1 
ATOM   487  O O   . VAL   A 1 70  ? 115.086 128.913 134.314 1.00 7.62  ? 70  VAL   A O   1 
ATOM   488  C CB  . VAL   A 1 70  ? 115.756 128.863 137.679 1.00 4.81  ? 70  VAL   A CB  1 
ATOM   489  C CG1 . VAL   A 1 70  ? 117.089 128.737 136.959 1.00 10.48 ? 70  VAL   A CG1 1 
ATOM   490  C CG2 . VAL   A 1 70  ? 115.799 130.071 138.593 1.00 7.83  ? 70  VAL   A CG2 1 
ATOM   491  N N   . PHE   A 1 71  ? 114.951 126.949 135.396 1.00 12.34 ? 71  PHE   A N   1 
ATOM   492  C CA  . PHE   A 1 71  ? 115.264 126.215 134.175 1.00 16.33 ? 71  PHE   A CA  1 
ATOM   493  C C   . PHE   A 1 71  ? 114.166 126.344 133.127 1.00 11.43 ? 71  PHE   A C   1 
ATOM   494  O O   . PHE   A 1 71  ? 114.443 126.171 131.935 1.00 9.64  ? 71  PHE   A O   1 
ATOM   495  C CB  . PHE   A 1 71  ? 115.548 124.740 134.485 1.00 10.88 ? 71  PHE   A CB  1 
ATOM   496  C CG  . PHE   A 1 71  ? 114.503 124.064 135.330 1.00 16.49 ? 71  PHE   A CG  1 
ATOM   497  C CD1 . PHE   A 1 71  ? 113.290 123.674 134.788 1.00 16.54 ? 71  PHE   A CD1 1 
ATOM   498  C CD2 . PHE   A 1 71  ? 114.754 123.780 136.661 1.00 15.61 ? 71  PHE   A CD2 1 
ATOM   499  C CE1 . PHE   A 1 71  ? 112.339 123.039 135.565 1.00 16.37 ? 71  PHE   A CE1 1 
ATOM   500  C CE2 . PHE   A 1 71  ? 113.807 123.145 137.443 1.00 9.45  ? 71  PHE   A CE2 1 
ATOM   501  C CZ  . PHE   A 1 71  ? 112.598 122.776 136.894 1.00 8.04  ? 71  PHE   A CZ  1 
ATOM   502  N N   . VAL   A 1 72  ? 112.934 126.644 133.539 1.00 12.57 ? 72  VAL   A N   1 
ATOM   503  C CA  . VAL   A 1 72  ? 111.866 126.881 132.573 1.00 13.44 ? 72  VAL   A CA  1 
ATOM   504  C C   . VAL   A 1 72  ? 112.064 128.216 131.863 1.00 12.05 ? 72  VAL   A C   1 
ATOM   505  O O   . VAL   A 1 72  ? 111.874 128.320 130.646 1.00 16.37 ? 72  VAL   A O   1 
ATOM   506  C CB  . VAL   A 1 72  ? 110.493 126.810 133.265 1.00 14.44 ? 72  VAL   A CB  1 
ATOM   507  C CG1 . VAL   A 1 72  ? 109.378 127.003 132.250 1.00 18.46 ? 72  VAL   A CG1 1 
ATOM   508  C CG2 . VAL   A 1 72  ? 110.332 125.485 133.986 1.00 12.15 ? 72  VAL   A CG2 1 
ATOM   509  N N   . LEU   A 1 73  ? 112.454 129.256 132.606 1.00 13.88 ? 73  LEU   A N   1 
ATOM   510  C CA  . LEU   A 1 73  ? 112.392 130.622 132.105 1.00 9.27  ? 73  LEU   A CA  1 
ATOM   511  C C   . LEU   A 1 73  ? 113.741 131.256 131.798 1.00 12.61 ? 73  LEU   A C   1 
ATOM   512  O O   . LEU   A 1 73  ? 113.781 132.222 131.031 1.00 10.35 ? 73  LEU   A O   1 
ATOM   513  C CB  . LEU   A 1 73  ? 111.654 131.519 133.109 1.00 7.43  ? 73  LEU   A CB  1 
ATOM   514  C CG  . LEU   A 1 73  ? 110.131 131.389 133.150 1.00 9.15  ? 73  LEU   A CG  1 
ATOM   515  C CD1 . LEU   A 1 73  ? 109.543 132.347 134.173 1.00 13.51 ? 73  LEU   A CD1 1 
ATOM   516  C CD2 . LEU   A 1 73  ? 109.537 131.638 131.774 1.00 11.84 ? 73  LEU   A CD2 1 
ATOM   517  N N   . THR   A 1 74  ? 114.838 130.756 132.374 1.00 12.48 ? 74  THR   A N   1 
ATOM   518  C CA  . THR   A 1 74  ? 116.131 131.406 132.171 1.00 9.03  ? 74  THR   A CA  1 
ATOM   519  C C   . THR   A 1 74  ? 116.548 131.367 130.706 1.00 12.99 ? 74  THR   A C   1 
ATOM   520  O O   . THR   A 1 74  ? 117.054 132.361 130.171 1.00 17.26 ? 74  THR   A O   1 
ATOM   521  C CB  . THR   A 1 74  ? 117.200 130.752 133.044 1.00 15.46 ? 74  THR   A CB  1 
ATOM   522  O OG1 . THR   A 1 74  ? 116.819 130.850 134.421 1.00 13.23 ? 74  THR   A OG1 1 
ATOM   523  C CG2 . THR   A 1 74  ? 118.532 131.446 132.849 1.00 17.05 ? 74  THR   A CG2 1 
ATOM   524  N N   . ASP   A 1 75  ? 116.346 130.229 130.041 1.00 29.46 ? 75  ASP   A N   1 
ATOM   525  C CA  . ASP   A 1 75  ? 116.675 130.136 128.623 1.00 26.40 ? 75  ASP   A CA  1 
ATOM   526  C C   . ASP   A 1 75  ? 115.811 131.077 127.794 1.00 20.77 ? 75  ASP   A C   1 
ATOM   527  O O   . ASP   A 1 75  ? 116.294 131.690 126.834 1.00 21.38 ? 75  ASP   A O   1 
ATOM   528  C CB  . ASP   A 1 75  ? 116.514 128.694 128.143 1.00 21.10 ? 75  ASP   A CB  1 
ATOM   529  C CG  . ASP   A 1 75  ? 117.174 127.695 129.069 1.00 24.96 ? 75  ASP   A CG  1 
ATOM   530  O OD1 . ASP   A 1 75  ? 118.420 127.618 129.073 1.00 24.20 ? 75  ASP   A OD1 1 
ATOM   531  O OD2 . ASP   A 1 75  ? 116.447 126.989 129.798 1.00 30.20 ? 75  ASP   A OD2 1 
ATOM   532  N N   . TYR   A 1 76  ? 114.529 131.200 128.147 1.00 25.25 ? 76  TYR   A N   1 
ATOM   533  C CA  . TYR   A 1 76  ? 113.634 132.083 127.405 1.00 33.30 ? 76  TYR   A CA  1 
ATOM   534  C C   . TYR   A 1 76  ? 114.048 133.543 127.548 1.00 31.25 ? 76  TYR   A C   1 
ATOM   535  O O   . TYR   A 1 76  ? 114.004 134.304 126.574 1.00 31.81 ? 76  TYR   A O   1 
ATOM   536  C CB  . TYR   A 1 76  ? 112.185 131.895 127.868 1.00 29.90 ? 76  TYR   A CB  1 
ATOM   537  C CG  . TYR   A 1 76  ? 111.610 130.491 127.741 1.00 30.26 ? 76  TYR   A CG  1 
ATOM   538  C CD1 . TYR   A 1 76  ? 112.390 129.416 127.325 1.00 28.34 ? 76  TYR   A CD1 1 
ATOM   539  C CD2 . TYR   A 1 76  ? 110.276 130.246 128.041 1.00 23.70 ? 76  TYR   A CD2 1 
ATOM   540  C CE1 . TYR   A 1 76  ? 111.860 128.147 127.214 1.00 27.10 ? 76  TYR   A CE1 1 
ATOM   541  C CE2 . TYR   A 1 76  ? 109.737 128.978 127.932 1.00 28.49 ? 76  TYR   A CE2 1 
ATOM   542  C CZ  . TYR   A 1 76  ? 110.534 127.932 127.519 1.00 30.87 ? 76  TYR   A CZ  1 
ATOM   543  O OH  . TYR   A 1 76  ? 110.003 126.668 127.408 1.00 28.26 ? 76  TYR   A OH  1 
ATOM   544  N N   . VAL   A 1 77  ? 114.456 133.955 128.754 1.00 13.93 ? 77  VAL   A N   1 
ATOM   545  C CA  . VAL   A 1 77  ? 114.824 135.346 128.998 1.00 10.73 ? 77  VAL   A CA  1 
ATOM   546  C C   . VAL   A 1 77  ? 116.278 135.639 128.656 1.00 9.47  ? 77  VAL   A C   1 
ATOM   547  O O   . VAL   A 1 77  ? 116.757 136.745 128.941 1.00 16.94 ? 77  VAL   A O   1 
ATOM   548  C CB  . VAL   A 1 77  ? 114.546 135.739 130.463 1.00 12.56 ? 77  VAL   A CB  1 
ATOM   549  C CG1 . VAL   A 1 77  ? 113.110 135.412 130.836 1.00 19.20 ? 77  VAL   A CG1 1 
ATOM   550  C CG2 . VAL   A 1 77  ? 115.512 135.030 131.389 1.00 11.56 ? 77  VAL   A CG2 1 
ATOM   551  N N   . ARG   A 1 78  ? 116.994 134.683 128.059 1.00 12.27 ? 78  ARG   A N   1 
ATOM   552  C CA  . ARG   A 1 78  ? 118.366 134.869 127.582 1.00 14.12 ? 78  ARG   A CA  1 
ATOM   553  C C   . ARG   A 1 78  ? 119.362 135.057 128.725 1.00 16.43 ? 78  ARG   A C   1 
ATOM   554  O O   . ARG   A 1 78  ? 120.367 135.754 128.574 1.00 13.52 ? 78  ARG   A O   1 
ATOM   555  C CB  . ARG   A 1 78  ? 118.456 136.032 126.588 1.00 10.13 ? 78  ARG   A CB  1 
ATOM   556  C CG  . ARG   A 1 78  ? 117.935 135.682 125.205 1.00 12.00 ? 78  ARG   A CG  1 
ATOM   557  C CD  . ARG   A 1 78  ? 117.998 136.868 124.265 1.00 13.92 ? 78  ARG   A CD  1 
ATOM   558  N NE  . ARG   A 1 78  ? 117.044 137.908 124.629 1.00 15.62 ? 78  ARG   A NE  1 
ATOM   559  C CZ  . ARG   A 1 78  ? 117.150 139.180 124.270 1.00 16.58 ? 78  ARG   A CZ  1 
ATOM   560  N NH1 . ARG   A 1 78  ? 118.165 139.609 123.538 1.00 10.18 ? 78  ARG   A NH1 1 
ATOM   561  N NH2 . ARG   A 1 78  ? 116.215 140.043 124.656 1.00 9.11  ? 78  ARG   A NH2 1 
ATOM   562  N N   . TYR   A 1 79  ? 119.069 134.457 129.879 1.00 14.20 ? 79  TYR   A N   1 
ATOM   563  C CA  . TYR   A 1 79  ? 120.029 134.200 130.952 1.00 17.11 ? 79  TYR   A CA  1 
ATOM   564  C C   . TYR   A 1 79  ? 120.542 135.446 131.667 1.00 9.13  ? 79  TYR   A C   1 
ATOM   565  O O   . TYR   A 1 79  ? 121.217 135.328 132.694 1.00 15.73 ? 79  TYR   A O   1 
ATOM   566  C CB  . TYR   A 1 79  ? 121.241 133.428 130.413 1.00 15.87 ? 79  TYR   A CB  1 
ATOM   567  C CG  . TYR   A 1 79  ? 120.934 132.158 129.649 1.00 13.50 ? 79  TYR   A CG  1 
ATOM   568  C CD1 . TYR   A 1 79  ? 120.654 132.188 128.289 1.00 18.15 ? 79  TYR   A CD1 1 
ATOM   569  C CD2 . TYR   A 1 79  ? 120.963 130.924 130.279 1.00 15.45 ? 79  TYR   A CD2 1 
ATOM   570  C CE1 . TYR   A 1 79  ? 120.382 131.032 127.588 1.00 9.06  ? 79  TYR   A CE1 1 
ATOM   571  C CE2 . TYR   A 1 79  ? 120.698 129.762 129.583 1.00 13.85 ? 79  TYR   A CE2 1 
ATOM   572  C CZ  . TYR   A 1 79  ? 120.408 129.822 128.239 1.00 17.60 ? 79  TYR   A CZ  1 
ATOM   573  O OH  . TYR   A 1 79  ? 120.142 128.664 127.545 1.00 17.31 ? 79  TYR   A OH  1 
ATOM   574  N N   . LYS   A 1 80  ? 120.245 136.636 131.155 1.00 10.69 ? 80  LYS   A N   1 
ATOM   575  C CA  . LYS   A 1 80  ? 120.712 137.832 131.850 1.00 10.93 ? 80  LYS   A CA  1 
ATOM   576  C C   . LYS   A 1 80  ? 119.766 138.273 132.966 1.00 9.98  ? 80  LYS   A C   1 
ATOM   577  O O   . LYS   A 1 80  ? 120.234 138.540 134.081 1.00 6.94  ? 80  LYS   A O   1 
ATOM   578  C CB  . LYS   A 1 80  ? 120.950 138.985 130.871 1.00 9.80  ? 80  LYS   A CB  1 
ATOM   579  C CG  . LYS   A 1 80  ? 121.746 140.127 131.484 1.00 10.91 ? 80  LYS   A CG  1 
ATOM   580  C CD  . LYS   A 1 80  ? 122.380 141.006 130.425 1.00 7.72  ? 80  LYS   A CD  1 
ATOM   581  C CE  . LYS   A 1 80  ? 121.685 142.352 130.338 1.00 12.75 ? 80  LYS   A CE  1 
ATOM   582  N NZ  . LYS   A 1 80  ? 122.660 143.465 130.172 1.00 6.14  ? 80  LYS   A NZ  1 
ATOM   583  N N   . PRO   A 1 81  ? 118.451 138.385 132.725 1.00 10.92 ? 81  PRO   A N   1 
ATOM   584  C CA  . PRO   A 1 81  ? 117.565 138.862 133.801 1.00 6.34  ? 81  PRO   A CA  1 
ATOM   585  C C   . PRO   A 1 81  ? 117.601 138.002 135.047 1.00 11.18 ? 81  PRO   A C   1 
ATOM   586  O O   . PRO   A 1 81  ? 117.505 138.543 136.155 1.00 7.72  ? 81  PRO   A O   1 
ATOM   587  C CB  . PRO   A 1 81  ? 116.178 138.845 133.145 1.00 11.52 ? 81  PRO   A CB  1 
ATOM   588  C CG  . PRO   A 1 81  ? 116.451 139.002 131.705 1.00 6.98  ? 81  PRO   A CG  1 
ATOM   589  C CD  . PRO   A 1 81  ? 117.705 138.223 131.464 1.00 5.58  ? 81  PRO   A CD  1 
ATOM   590  N N   . VAL   A 1 82  ? 117.742 136.683 134.907 1.00 12.59 ? 82  VAL   A N   1 
ATOM   591  C CA  . VAL   A 1 82  ? 117.839 135.826 136.084 1.00 8.00  ? 82  VAL   A CA  1 
ATOM   592  C C   . VAL   A 1 82  ? 119.117 136.129 136.855 1.00 12.24 ? 82  VAL   A C   1 
ATOM   593  O O   . VAL   A 1 82  ? 119.131 136.110 138.092 1.00 12.36 ? 82  VAL   A O   1 
ATOM   594  C CB  . VAL   A 1 82  ? 117.753 134.345 135.678 1.00 7.13  ? 82  VAL   A CB  1 
ATOM   595  C CG1 . VAL   A 1 82  ? 117.488 133.477 136.893 1.00 7.05  ? 82  VAL   A CG1 1 
ATOM   596  C CG2 . VAL   A 1 82  ? 116.664 134.149 134.645 1.00 6.90  ? 82  VAL   A CG2 1 
ATOM   597  N N   . ILE   A 1 83  ? 120.210 136.405 136.141 1.00 4.22  ? 83  ILE   A N   1 
ATOM   598  C CA  . ILE   A 1 83  ? 121.426 136.881 136.795 1.00 6.56  ? 83  ILE   A CA  1 
ATOM   599  C C   . ILE   A 1 83  ? 121.183 138.248 137.421 1.00 3.06  ? 83  ILE   A C   1 
ATOM   600  O O   . ILE   A 1 83  ? 121.583 138.512 138.561 1.00 3.90  ? 83  ILE   A O   1 
ATOM   601  C CB  . ILE   A 1 83  ? 122.593 136.920 135.793 1.00 9.54  ? 83  ILE   A CB  1 
ATOM   602  C CG1 . ILE   A 1 83  ? 123.150 135.518 135.564 1.00 10.79 ? 83  ILE   A CG1 1 
ATOM   603  C CG2 . ILE   A 1 83  ? 123.693 137.840 136.290 1.00 3.60  ? 83  ILE   A CG2 1 
ATOM   604  C CD1 . ILE   A 1 83  ? 124.330 135.495 134.632 1.00 5.11  ? 83  ILE   A CD1 1 
ATOM   605  N N   . ILE   A 1 84  ? 120.523 139.140 136.679 1.00 2.99  ? 84  ILE   A N   1 
ATOM   606  C CA  . ILE   A 1 84  ? 120.169 140.445 137.230 1.00 10.09 ? 84  ILE   A CA  1 
ATOM   607  C C   . ILE   A 1 84  ? 119.172 140.283 138.370 1.00 8.03  ? 84  ILE   A C   1 
ATOM   608  O O   . ILE   A 1 84  ? 119.236 140.999 139.376 1.00 6.46  ? 84  ILE   A O   1 
ATOM   609  C CB  . ILE   A 1 84  ? 119.631 141.366 136.120 1.00 3.96  ? 84  ILE   A CB  1 
ATOM   610  C CG1 . ILE   A 1 84  ? 120.712 141.599 135.062 1.00 9.27  ? 84  ILE   A CG1 1 
ATOM   611  C CG2 . ILE   A 1 84  ? 119.162 142.691 136.702 1.00 5.27  ? 84  ILE   A CG2 1 
ATOM   612  C CD1 . ILE   A 1 84  ? 120.416 142.743 134.119 1.00 10.15 ? 84  ILE   A CD1 1 
ATOM   613  N N   . LEU   A 1 85  ? 118.240 139.335 138.237 1.00 10.56 ? 85  LEU   A N   1 
ATOM   614  C CA  . LEU   A 1 85  ? 117.365 139.009 139.359 1.00 8.28  ? 85  LEU   A CA  1 
ATOM   615  C C   . LEU   A 1 85  ? 118.168 138.442 140.520 1.00 4.76  ? 85  LEU   A C   1 
ATOM   616  O O   . LEU   A 1 85  ? 117.865 138.716 141.686 1.00 13.26 ? 85  LEU   A O   1 
ATOM   617  C CB  . LEU   A 1 85  ? 116.281 138.023 138.920 1.00 5.10  ? 85  LEU   A CB  1 
ATOM   618  C CG  . LEU   A 1 85  ? 115.599 137.193 140.009 1.00 5.53  ? 85  LEU   A CG  1 
ATOM   619  C CD1 . LEU   A 1 85  ? 114.589 138.037 140.771 1.00 7.81  ? 85  LEU   A CD1 1 
ATOM   620  C CD2 . LEU   A 1 85  ? 114.931 135.970 139.404 1.00 7.54  ? 85  LEU   A CD2 1 
ATOM   621  N N   . GLN   A 1 86  ? 119.198 137.648 140.219 1.00 2.67  ? 86  GLN   A N   1 
ATOM   622  C CA  . GLN   A 1 86  ? 120.096 137.168 141.264 1.00 8.49  ? 86  GLN   A CA  1 
ATOM   623  C C   . GLN   A 1 86  ? 120.830 138.324 141.931 1.00 3.09  ? 86  GLN   A C   1 
ATOM   624  O O   . GLN   A 1 86  ? 120.967 138.357 143.159 1.00 7.64  ? 86  GLN   A O   1 
ATOM   625  C CB  . GLN   A 1 86  ? 121.088 136.167 140.675 1.00 8.74  ? 86  GLN   A CB  1 
ATOM   626  C CG  . GLN   A 1 86  ? 122.434 136.108 141.364 1.00 3.31  ? 86  GLN   A CG  1 
ATOM   627  C CD  . GLN   A 1 86  ? 123.238 134.890 140.955 1.00 7.21  ? 86  GLN   A CD  1 
ATOM   628  O OE1 . GLN   A 1 86  ? 123.657 134.098 141.798 1.00 8.69  ? 86  GLN   A OE1 1 
ATOM   629  N NE2 . GLN   A 1 86  ? 123.454 134.731 139.654 1.00 7.58  ? 86  GLN   A NE2 1 
ATOM   630  N N   . GLY   A 1 87  ? 121.306 139.285 141.136 1.00 7.83  ? 87  GLY   A N   1 
ATOM   631  C CA  . GLY   A 1 87  ? 122.009 140.423 141.707 1.00 4.82  ? 87  GLY   A CA  1 
ATOM   632  C C   . GLY   A 1 87  ? 121.122 141.266 142.602 1.00 9.18  ? 87  GLY   A C   1 
ATOM   633  O O   . GLY   A 1 87  ? 121.511 141.636 143.711 1.00 11.31 ? 87  GLY   A O   1 
ATOM   634  N N   . ILE   A 1 88  ? 119.911 141.577 142.131 1.00 8.68  ? 88  ILE   A N   1 
ATOM   635  C CA  . ILE   A 1 88  ? 118.974 142.355 142.938 1.00 12.25 ? 88  ILE   A CA  1 
ATOM   636  C C   . ILE   A 1 88  ? 118.582 141.584 144.190 1.00 4.99  ? 88  ILE   A C   1 
ATOM   637  O O   . ILE   A 1 88  ? 118.520 142.145 145.291 1.00 12.78 ? 88  ILE   A O   1 
ATOM   638  C CB  . ILE   A 1 88  ? 117.738 142.743 142.105 1.00 6.35  ? 88  ILE   A CB  1 
ATOM   639  C CG1 . ILE   A 1 88  ? 118.152 143.554 140.877 1.00 8.38  ? 88  ILE   A CG1 1 
ATOM   640  C CG2 . ILE   A 1 88  ? 116.748 143.527 142.951 1.00 7.43  ? 88  ILE   A CG2 1 
ATOM   641  C CD1 . ILE   A 1 88  ? 116.987 144.129 140.102 1.00 5.23  ? 88  ILE   A CD1 1 
ATOM   642  N N   . SER   A 1 89  ? 118.306 140.288 144.043 1.00 13.96 ? 89  SER   A N   1 
ATOM   643  C CA  . SER   A 1 89  ? 117.957 139.459 145.188 1.00 8.62  ? 89  SER   A CA  1 
ATOM   644  C C   . SER   A 1 89  ? 119.148 139.203 146.103 1.00 10.22 ? 89  SER   A C   1 
ATOM   645  O O   . SER   A 1 89  ? 118.946 138.883 147.278 1.00 9.86  ? 89  SER   A O   1 
ATOM   646  C CB  . SER   A 1 89  ? 117.342 138.146 144.702 1.00 6.24  ? 89  SER   A CB  1 
ATOM   647  O OG  . SER   A 1 89  ? 118.336 137.229 144.292 1.00 6.98  ? 89  SER   A OG  1 
ATOM   648  N N   . PHE   A 1 90  ? 120.379 139.332 145.599 1.00 5.96  ? 90  PHE   A N   1 
ATOM   649  C CA  . PHE   A 1 90  ? 121.528 139.422 146.497 1.00 10.27 ? 90  PHE   A CA  1 
ATOM   650  C C   . PHE   A 1 90  ? 121.465 140.688 147.338 1.00 7.81  ? 90  PHE   A C   1 
ATOM   651  O O   . PHE   A 1 90  ? 121.778 140.665 148.534 1.00 8.76  ? 90  PHE   A O   1 
ATOM   652  C CB  . PHE   A 1 90  ? 122.837 139.375 145.708 1.00 6.27  ? 90  PHE   A CB  1 
ATOM   653  C CG  . PHE   A 1 90  ? 123.462 138.011 145.646 1.00 13.07 ? 90  PHE   A CG  1 
ATOM   654  C CD1 . PHE   A 1 90  ? 123.828 137.356 146.810 1.00 6.26  ? 90  PHE   A CD1 1 
ATOM   655  C CD2 . PHE   A 1 90  ? 123.701 137.393 144.432 1.00 15.05 ? 90  PHE   A CD2 1 
ATOM   656  C CE1 . PHE   A 1 90  ? 124.410 136.105 146.765 1.00 6.97  ? 90  PHE   A CE1 1 
ATOM   657  C CE2 . PHE   A 1 90  ? 124.282 136.141 144.381 1.00 10.92 ? 90  PHE   A CE2 1 
ATOM   658  C CZ  . PHE   A 1 90  ? 124.637 135.496 145.549 1.00 5.64  ? 90  PHE   A CZ  1 
ATOM   659  N N   . ILE   A 1 91  ? 121.071 141.808 146.727 1.00 7.84  ? 91  ILE   A N   1 
ATOM   660  C CA  . ILE   A 1 91  ? 120.931 143.051 147.480 1.00 1.87  ? 91  ILE   A CA  1 
ATOM   661  C C   . ILE   A 1 91  ? 119.836 142.914 148.526 1.00 5.25  ? 91  ILE   A C   1 
ATOM   662  O O   . ILE   A 1 91  ? 120.002 143.336 149.675 1.00 7.37  ? 91  ILE   A O   1 
ATOM   663  C CB  . ILE   A 1 91  ? 120.658 144.233 146.531 1.00 1.47  ? 91  ILE   A CB  1 
ATOM   664  C CG1 . ILE   A 1 91  ? 121.656 144.239 145.376 1.00 5.48  ? 91  ILE   A CG1 1 
ATOM   665  C CG2 . ILE   A 1 91  ? 120.717 145.548 147.290 1.00 2.14  ? 91  ILE   A CG2 1 
ATOM   666  C CD1 . ILE   A 1 91  ? 123.091 144.173 145.820 1.00 7.56  ? 91  ILE   A CD1 1 
ATOM   667  N N   . ILE   A 1 92  ? 118.703 142.321 148.150 1.00 6.32  ? 92  ILE   A N   1 
ATOM   668  C CA  . ILE   A 1 92  ? 117.615 142.132 149.103 1.00 0.86  ? 92  ILE   A CA  1 
ATOM   669  C C   . ILE   A 1 92  ? 118.026 141.159 150.201 1.00 7.71  ? 92  ILE   A C   1 
ATOM   670  O O   . ILE   A 1 92  ? 117.759 141.393 151.388 1.00 0.17  ? 92  ILE   A O   1 
ATOM   671  C CB  . ILE   A 1 92  ? 116.343 141.661 148.376 1.00 7.70  ? 92  ILE   A CB  1 
ATOM   672  C CG1 . ILE   A 1 92  ? 115.917 142.688 147.327 1.00 4.68  ? 92  ILE   A CG1 1 
ATOM   673  C CG2 . ILE   A 1 92  ? 115.219 141.430 149.368 1.00 3.13  ? 92  ILE   A CG2 1 
ATOM   674  C CD1 . ILE   A 1 92  ? 115.312 142.073 146.085 1.00 6.68  ? 92  ILE   A CD1 1 
ATOM   675  N N   . THR   A 1 93  ? 118.691 140.061 149.826 1.00 9.37  ? 93  THR   A N   1 
ATOM   676  C CA  . THR   A 1 93  ? 119.068 139.045 150.805 1.00 12.08 ? 93  THR   A CA  1 
ATOM   677  C C   . THR   A 1 93  ? 119.932 139.638 151.907 1.00 4.98  ? 93  THR   A C   1 
ATOM   678  O O   . THR   A 1 93  ? 119.599 139.540 153.091 1.00 2.24  ? 93  THR   A O   1 
ATOM   679  C CB  . THR   A 1 93  ? 119.813 137.897 150.121 1.00 11.54 ? 93  THR   A CB  1 
ATOM   680  O OG1 . THR   A 1 93  ? 119.030 137.385 149.037 1.00 10.78 ? 93  THR   A OG1 1 
ATOM   681  C CG2 . THR   A 1 93  ? 120.089 136.777 151.113 1.00 9.49  ? 93  THR   A CG2 1 
ATOM   682  N N   . TRP   A 1 94  ? 121.025 140.302 151.534 1.00 7.19  ? 94  TRP   A N   1 
ATOM   683  C CA  . TRP   A 1 94  ? 121.926 140.838 152.544 1.00 9.09  ? 94  TRP   A CA  1 
ATOM   684  C C   . TRP   A 1 94  ? 121.441 142.156 153.131 1.00 9.82  ? 94  TRP   A C   1 
ATOM   685  O O   . TRP   A 1 94  ? 121.872 142.521 154.227 1.00 5.77  ? 94  TRP   A O   1 
ATOM   686  C CB  . TRP   A 1 94  ? 123.332 140.996 151.966 1.00 9.72  ? 94  TRP   A CB  1 
ATOM   687  C CG  . TRP   A 1 94  ? 124.229 139.869 152.369 1.00 9.52  ? 94  TRP   A CG  1 
ATOM   688  C CD1 . TRP   A 1 94  ? 125.075 139.837 153.437 1.00 8.15  ? 94  TRP   A CD1 1 
ATOM   689  C CD2 . TRP   A 1 94  ? 124.345 138.594 151.726 1.00 6.04  ? 94  TRP   A CD2 1 
ATOM   690  N NE1 . TRP   A 1 94  ? 125.722 138.626 153.492 1.00 8.99  ? 94  TRP   A NE1 1 
ATOM   691  C CE2 . TRP   A 1 94  ? 125.289 137.845 152.453 1.00 2.05  ? 94  TRP   A CE2 1 
ATOM   692  C CE3 . TRP   A 1 94  ? 123.746 138.016 150.603 1.00 9.77  ? 94  TRP   A CE3 1 
ATOM   693  C CZ2 . TRP   A 1 94  ? 125.652 136.549 152.093 1.00 10.98 ? 94  TRP   A CZ2 1 
ATOM   694  C CZ3 . TRP   A 1 94  ? 124.106 136.730 150.248 1.00 4.41  ? 94  TRP   A CZ3 1 
ATOM   695  C CH2 . TRP   A 1 94  ? 125.050 136.011 150.990 1.00 3.23  ? 94  TRP   A CH2 1 
ATOM   696  N N   . LEU   A 1 95  ? 120.540 142.864 152.448 1.00 2.17  ? 95  LEU   A N   1 
ATOM   697  C CA  . LEU   A 1 95  ? 119.930 144.044 153.049 1.00 2.99  ? 95  LEU   A CA  1 
ATOM   698  C C   . LEU   A 1 95  ? 119.020 143.656 154.205 1.00 8.80  ? 95  LEU   A C   1 
ATOM   699  O O   . LEU   A 1 95  ? 119.039 144.300 155.261 1.00 5.40  ? 95  LEU   A O   1 
ATOM   700  C CB  . LEU   A 1 95  ? 119.155 144.834 151.996 1.00 2.84  ? 95  LEU   A CB  1 
ATOM   701  C CG  . LEU   A 1 95  ? 119.864 146.048 151.394 1.00 1.35  ? 95  LEU   A CG  1 
ATOM   702  C CD1 . LEU   A 1 95  ? 118.956 146.756 150.403 1.00 2.87  ? 95  LEU   A CD1 1 
ATOM   703  C CD2 . LEU   A 1 95  ? 120.319 147.001 152.487 1.00 6.11  ? 95  LEU   A CD2 1 
ATOM   704  N N   . LEU   A 1 96  ? 118.215 142.607 154.027 1.00 4.64  ? 96  LEU   A N   1 
ATOM   705  C CA  . LEU   A 1 96  ? 117.401 142.113 155.130 1.00 5.97  ? 96  LEU   A CA  1 
ATOM   706  C C   . LEU   A 1 96  ? 118.230 141.309 156.125 1.00 5.84  ? 96  LEU   A C   1 
ATOM   707  O O   . LEU   A 1 96  ? 117.845 141.189 157.294 1.00 9.68  ? 96  LEU   A O   1 
ATOM   708  C CB  . LEU   A 1 96  ? 116.241 141.277 154.590 1.00 5.66  ? 96  LEU   A CB  1 
ATOM   709  C CG  . LEU   A 1 96  ? 115.186 142.035 153.785 1.00 4.86  ? 96  LEU   A CG  1 
ATOM   710  C CD1 . LEU   A 1 96  ? 114.370 141.073 152.943 1.00 8.15  ? 96  LEU   A CD1 1 
ATOM   711  C CD2 . LEU   A 1 96  ? 114.286 142.845 154.704 1.00 3.61  ? 96  LEU   A CD2 1 
ATOM   712  N N   . LEU   A 1 97  ? 119.357 140.749 155.681 1.00 4.64  ? 97  LEU   A N   1 
ATOM   713  C CA  . LEU   A 1 97  ? 120.292 140.103 156.595 1.00 3.12  ? 97  LEU   A CA  1 
ATOM   714  C C   . LEU   A 1 97  ? 120.994 141.129 157.475 1.00 6.24  ? 97  LEU   A C   1 
ATOM   715  O O   . LEU   A 1 97  ? 121.456 140.808 158.576 1.00 8.74  ? 97  LEU   A O   1 
ATOM   716  C CB  . LEU   A 1 97  ? 121.309 139.295 155.788 1.00 4.45  ? 97  LEU   A CB  1 
ATOM   717  C CG  . LEU   A 1 97  ? 122.307 138.368 156.480 1.00 7.82  ? 97  LEU   A CG  1 
ATOM   718  C CD1 . LEU   A 1 97  ? 121.610 137.495 157.490 1.00 4.54  ? 97  LEU   A CD1 1 
ATOM   719  C CD2 . LEU   A 1 97  ? 123.020 137.516 155.444 1.00 6.53  ? 97  LEU   A CD2 1 
ATOM   720  N N   . LEU   A 1 98  ? 121.088 142.371 156.999 1.00 3.58  ? 98  LEU   A N   1 
ATOM   721  C CA  . LEU   A 1 98  ? 121.780 143.413 157.747 1.00 6.59  ? 98  LEU   A CA  1 
ATOM   722  C C   . LEU   A 1 98  ? 120.848 144.096 158.739 1.00 11.36 ? 98  LEU   A C   1 
ATOM   723  O O   . LEU   A 1 98  ? 121.181 144.244 159.921 1.00 8.32  ? 98  LEU   A O   1 
ATOM   724  C CB  . LEU   A 1 98  ? 122.366 144.438 156.777 1.00 9.93  ? 98  LEU   A CB  1 
ATOM   725  C CG  . LEU   A 1 98  ? 123.782 144.198 156.263 1.00 7.31  ? 98  LEU   A CG  1 
ATOM   726  C CD1 . LEU   A 1 98  ? 124.266 145.412 155.498 1.00 7.25  ? 98  LEU   A CD1 1 
ATOM   727  C CD2 . LEU   A 1 98  ? 124.703 143.902 157.424 1.00 10.69 ? 98  LEU   A CD2 1 
ATOM   728  N N   . PHE   A 1 99  ? 119.670 144.517 158.277 1.00 5.19  ? 99  PHE   A N   1 
ATOM   729  C CA  . PHE   A 1 99  ? 118.791 145.379 159.057 1.00 10.25 ? 99  PHE   A CA  1 
ATOM   730  C C   . PHE   A 1 99  ? 117.459 144.702 159.353 1.00 13.94 ? 99  PHE   A C   1 
ATOM   731  O O   . PHE   A 1 99  ? 116.467 145.374 159.646 1.00 9.69  ? 99  PHE   A O   1 
ATOM   732  C CB  . PHE   A 1 99  ? 118.568 146.706 158.336 1.00 6.46  ? 99  PHE   A CB  1 
ATOM   733  C CG  . PHE   A 1 99  ? 119.827 147.315 157.792 1.00 12.99 ? 99  PHE   A CG  1 
ATOM   734  C CD1 . PHE   A 1 99  ? 120.738 147.925 158.636 1.00 7.03  ? 99  PHE   A CD1 1 
ATOM   735  C CD2 . PHE   A 1 99  ? 120.107 147.261 156.438 1.00 11.52 ? 99  PHE   A CD2 1 
ATOM   736  C CE1 . PHE   A 1 99  ? 121.900 148.481 158.138 1.00 9.92  ? 99  PHE   A CE1 1 
ATOM   737  C CE2 . PHE   A 1 99  ? 121.267 147.814 155.934 1.00 14.00 ? 99  PHE   A CE2 1 
ATOM   738  C CZ  . PHE   A 1 99  ? 122.164 148.425 156.785 1.00 10.76 ? 99  PHE   A CZ  1 
ATOM   739  N N   . GLY   A 1 100 ? 117.418 143.375 159.283 1.00 22.56 ? 100 GLY   A N   1 
ATOM   740  C CA  . GLY   A 1 100 ? 116.200 142.656 159.594 1.00 14.26 ? 100 GLY   A CA  1 
ATOM   741  C C   . GLY   A 1 100 ? 116.329 141.804 160.838 1.00 24.08 ? 100 GLY   A C   1 
ATOM   742  O O   . GLY   A 1 100 ? 117.026 140.785 160.833 1.00 14.96 ? 100 GLY   A O   1 
ATOM   743  N N   . GLN   A 1 101 ? 115.658 142.210 161.908 1.00 17.69 ? 101 GLN   A N   1 
ATOM   744  C CA  . GLN   A 1 101 ? 115.716 141.491 163.169 1.00 23.93 ? 101 GLN   A CA  1 
ATOM   745  C C   . GLN   A 1 101 ? 114.587 140.470 163.257 1.00 14.56 ? 101 GLN   A C   1 
ATOM   746  O O   . GLN   A 1 101 ? 113.583 140.549 162.545 1.00 22.70 ? 101 GLN   A O   1 
ATOM   747  C CB  . GLN   A 1 101 ? 115.641 142.466 164.347 1.00 23.09 ? 101 GLN   A CB  1 
ATOM   748  C CG  . GLN   A 1 101 ? 116.935 143.231 164.648 1.00 18.87 ? 101 GLN   A CG  1 
ATOM   749  C CD  . GLN   A 1 101 ? 118.072 142.358 165.170 1.00 17.03 ? 101 GLN   A CD  1 
ATOM   750  O OE1 . GLN   A 1 101 ? 118.079 141.139 165.001 1.00 22.50 ? 101 GLN   A OE1 1 
ATOM   751  N NE2 . GLN   A 1 101 ? 119.044 142.992 165.816 1.00 19.25 ? 101 GLN   A NE2 1 
ATOM   752  N N   . GLY   A 1 102 ? 114.770 139.497 164.146 1.00 33.94 ? 102 GLY   A N   1 
ATOM   753  C CA  . GLY   A 1 102 ? 113.785 138.455 164.343 1.00 41.87 ? 102 GLY   A CA  1 
ATOM   754  C C   . GLY   A 1 102 ? 113.846 137.390 163.267 1.00 41.55 ? 102 GLY   A C   1 
ATOM   755  O O   . GLY   A 1 102 ? 114.550 137.500 162.262 1.00 37.51 ? 102 GLY   A O   1 
ATOM   756  N N   . VAL   A 1 103 ? 113.074 136.324 163.493 1.00 29.83 ? 103 VAL   A N   1 
ATOM   757  C CA  . VAL   A 1 103 ? 113.001 135.213 162.554 1.00 25.45 ? 103 VAL   A CA  1 
ATOM   758  C C   . VAL   A 1 103 ? 111.990 135.458 161.443 1.00 28.10 ? 103 VAL   A C   1 
ATOM   759  O O   . VAL   A 1 103 ? 112.056 134.796 160.398 1.00 25.24 ? 103 VAL   A O   1 
ATOM   760  C CB  . VAL   A 1 103 ? 112.682 133.896 163.291 1.00 26.32 ? 103 VAL   A CB  1 
ATOM   761  C CG1 . VAL   A 1 103 ? 111.205 133.824 163.650 1.00 23.16 ? 103 VAL   A CG1 1 
ATOM   762  C CG2 . VAL   A 1 103 ? 113.104 132.698 162.456 1.00 30.91 ? 103 VAL   A CG2 1 
ATOM   763  N N   . LYS   A 1 104 ? 111.060 136.398 161.632 1.00 40.29 ? 104 LYS   A N   1 
ATOM   764  C CA  . LYS   A 1 104 ? 110.088 136.708 160.591 1.00 38.38 ? 104 LYS   A CA  1 
ATOM   765  C C   . LYS   A 1 104 ? 110.767 137.250 159.339 1.00 38.79 ? 104 LYS   A C   1 
ATOM   766  O O   . LYS   A 1 104 ? 110.439 136.835 158.222 1.00 37.49 ? 104 LYS   A O   1 
ATOM   767  C CB  . LYS   A 1 104 ? 109.060 137.712 161.116 1.00 44.51 ? 104 LYS   A CB  1 
ATOM   768  C CG  . LYS   A 1 104 ? 109.663 138.851 161.928 1.00 42.99 ? 104 LYS   A CG  1 
ATOM   769  C CD  . LYS   A 1 104 ? 108.638 139.490 162.851 1.00 45.29 ? 104 LYS   A CD  1 
ATOM   770  C CE  . LYS   A 1 104 ? 109.315 140.278 163.960 1.00 42.42 ? 104 LYS   A CE  1 
ATOM   771  N NZ  . LYS   A 1 104 ? 109.933 141.533 163.445 1.00 45.27 ? 104 LYS   A NZ  1 
ATOM   772  N N   . THR   A 1 105 ? 111.713 138.175 159.508 1.00 56.50 ? 105 THR   A N   1 
ATOM   773  C CA  . THR   A 1 105 ? 112.455 138.706 158.373 1.00 57.32 ? 105 THR   A CA  1 
ATOM   774  C C   . THR   A 1 105 ? 113.514 137.727 157.883 1.00 53.61 ? 105 THR   A C   1 
ATOM   775  O O   . THR   A 1 105 ? 113.794 137.672 156.681 1.00 56.02 ? 105 THR   A O   1 
ATOM   776  C CB  . THR   A 1 105 ? 113.097 140.045 158.750 1.00 51.34 ? 105 THR   A CB  1 
ATOM   777  O OG1 . THR   A 1 105 ? 112.071 140.996 159.063 1.00 52.76 ? 105 THR   A OG1 1 
ATOM   778  C CG2 . THR   A 1 105 ? 113.935 140.589 157.603 1.00 51.27 ? 105 THR   A CG2 1 
ATOM   779  N N   . MET   A 1 106 ? 114.098 136.938 158.787 1.00 34.83 ? 106 MET   A N   1 
ATOM   780  C CA  . MET   A 1 106 ? 115.158 136.017 158.389 1.00 33.16 ? 106 MET   A CA  1 
ATOM   781  C C   . MET   A 1 106 ? 114.635 134.891 157.505 1.00 34.82 ? 106 MET   A C   1 
ATOM   782  O O   . MET   A 1 106 ? 115.381 134.361 156.673 1.00 40.50 ? 106 MET   A O   1 
ATOM   783  C CB  . MET   A 1 106 ? 115.849 135.450 159.625 1.00 33.95 ? 106 MET   A CB  1 
ATOM   784  C CG  . MET   A 1 106 ? 116.845 136.403 160.250 1.00 40.57 ? 106 MET   A CG  1 
ATOM   785  S SD  . MET   A 1 106 ? 118.051 136.951 159.033 1.00 37.11 ? 106 MET   A SD  1 
ATOM   786  C CE  . MET   A 1 106 ? 119.179 135.568 159.065 1.00 34.50 ? 106 MET   A CE  1 
ATOM   787  N N   . GLN   A 1 107 ? 113.370 134.503 157.667 1.00 32.92 ? 107 GLN   A N   1 
ATOM   788  C CA  . GLN   A 1 107 ? 112.789 133.537 156.742 1.00 30.54 ? 107 GLN   A CA  1 
ATOM   789  C C   . GLN   A 1 107 ? 112.706 134.119 155.337 1.00 26.87 ? 107 GLN   A C   1 
ATOM   790  O O   . GLN   A 1 107 ? 112.960 133.421 154.348 1.00 32.27 ? 107 GLN   A O   1 
ATOM   791  C CB  . GLN   A 1 107 ? 111.414 133.095 157.239 1.00 28.68 ? 107 GLN   A CB  1 
ATOM   792  C CG  . GLN   A 1 107 ? 111.437 131.765 157.975 1.00 27.92 ? 107 GLN   A CG  1 
ATOM   793  C CD  . GLN   A 1 107 ? 110.243 131.576 158.887 1.00 27.65 ? 107 GLN   A CD  1 
ATOM   794  O OE1 . GLN   A 1 107 ? 109.543 132.533 159.219 1.00 31.32 ? 107 GLN   A OE1 1 
ATOM   795  N NE2 . GLN   A 1 107 ? 110.003 130.337 159.298 1.00 27.03 ? 107 GLN   A NE2 1 
ATOM   796  N N   . VAL   A 1 108 ? 112.352 135.406 155.260 1.00 12.46 ? 108 VAL   A N   1 
ATOM   797  C CA  . VAL   A 1 108 ? 112.239 136.121 153.953 1.00 7.33  ? 108 VAL   A CA  1 
ATOM   798  C C   . VAL   A 1 108 ? 113.635 136.204 153.326 1.00 9.82  ? 108 VAL   A C   1 
ATOM   799  O O   . VAL   A 1 108 ? 113.729 136.176 152.083 1.00 9.26  ? 108 VAL   A O   1 
ATOM   800  C CB  . VAL   A 1 108 ? 111.615 137.518 154.127 1.00 12.93 ? 108 VAL   A CB  1 
ATOM   801  C CG1 . VAL   A 1 108 ? 111.920 138.424 152.944 1.00 13.26 ? 108 VAL   A CG1 1 
ATOM   802  C CG2 . VAL   A 1 108 ? 110.115 137.440 154.370 1.00 6.22  ? 108 VAL   A CG2 1 
ATOM   803  N N   . VAL   A 1 109 ? 114.671 136.304 154.165 1.00 11.71 ? 109 VAL   A N   1 
ATOM   804  C CA  . VAL   A 1 109 ? 116.082 136.380 153.680 1.00 14.84 ? 109 VAL   A CA  1 
ATOM   805  C C   . VAL   A 1 109 ? 116.486 134.998 153.154 1.00 10.32 ? 109 VAL   A C   1 
ATOM   806  O O   . VAL   A 1 109 ? 117.184 134.937 152.122 1.00 15.08 ? 109 VAL   A O   1 
ATOM   807  C CB  . VAL   A 1 109 ? 117.035 136.859 154.791 1.00 8.65  ? 109 VAL   A CB  1 
ATOM   808  C CG1 . VAL   A 1 109 ? 118.413 136.228 154.663 1.00 11.95 ? 109 VAL   A CG1 1 
ATOM   809  C CG2 . VAL   A 1 109 ? 117.140 138.376 154.831 1.00 12.69 ? 109 VAL   A CG2 1 
ATOM   810  N N   . GLU   A 1 110 ? 116.086 133.944 153.875 1.00 14.43 ? 110 GLU   A N   1 
ATOM   811  C CA  . GLU   A 1 110 ? 116.374 132.547 153.456 1.00 12.29 ? 110 GLU   A CA  1 
ATOM   812  C C   . GLU   A 1 110 ? 115.688 132.331 152.105 1.00 16.32 ? 110 GLU   A C   1 
ATOM   813  O O   . GLU   A 1 110 ? 116.265 131.636 151.246 1.00 21.54 ? 110 GLU   A O   1 
ATOM   814  C CB  . GLU   A 1 110 ? 115.863 131.557 154.505 1.00 15.58 ? 110 GLU   A CB  1 
ATOM   815  C CG  . GLU   A 1 110 ? 116.825 131.354 155.662 1.00 19.95 ? 110 GLU   A CG  1 
ATOM   816  C CD  . GLU   A 1 110 ? 118.236 130.967 155.252 1.00 13.90 ? 110 GLU   A CD  1 
ATOM   817  O OE1 . GLU   A 1 110 ? 118.539 131.037 154.045 1.00 15.57 ? 110 GLU   A OE1 1 
ATOM   818  O OE2 . GLU   A 1 110 ? 119.028 130.597 156.142 1.00 13.60 ? 110 GLU   A OE2 1 
ATOM   819  N N   . PHE   A 1 111 ? 114.496 132.916 151.944 1.00 10.69 ? 111 PHE   A N   1 
ATOM   820  C CA  . PHE   A 1 111 ? 113.761 132.835 150.684 1.00 10.51 ? 111 PHE   A CA  1 
ATOM   821  C C   . PHE   A 1 111 ? 114.528 133.530 149.562 1.00 10.40 ? 111 PHE   A C   1 
ATOM   822  O O   . PHE   A 1 111 ? 114.677 132.989 148.458 1.00 6.05  ? 111 PHE   A O   1 
ATOM   823  C CB  . PHE   A 1 111 ? 112.371 133.448 150.864 1.00 10.44 ? 111 PHE   A CB  1 
ATOM   824  C CG  . PHE   A 1 111 ? 111.678 133.789 149.576 1.00 5.79  ? 111 PHE   A CG  1 
ATOM   825  C CD1 . PHE   A 1 111 ? 111.493 132.832 148.593 1.00 7.77  ? 111 PHE   A CD1 1 
ATOM   826  C CD2 . PHE   A 1 111 ? 111.203 135.070 149.353 1.00 7.24  ? 111 PHE   A CD2 1 
ATOM   827  C CE1 . PHE   A 1 111 ? 110.853 133.149 147.413 1.00 7.07  ? 111 PHE   A CE1 1 
ATOM   828  C CE2 . PHE   A 1 111 ? 110.563 135.392 148.174 1.00 4.10  ? 111 PHE   A CE2 1 
ATOM   829  C CZ  . PHE   A 1 111 ? 110.387 134.430 147.203 1.00 9.84  ? 111 PHE   A CZ  1 
ATOM   830  N N   . PHE   A 1 112 ? 115.050 134.724 149.837 1.00 11.45 ? 112 PHE   A N   1 
ATOM   831  C CA  . PHE   A 1 112 ? 115.809 135.437 148.815 1.00 10.51 ? 112 PHE   A CA  1 
ATOM   832  C C   . PHE   A 1 112 ? 117.165 134.788 148.561 1.00 10.86 ? 112 PHE   A C   1 
ATOM   833  O O   . PHE   A 1 112 ? 117.686 134.864 147.444 1.00 6.08  ? 112 PHE   A O   1 
ATOM   834  C CB  . PHE   A 1 112 ? 115.963 136.905 149.203 1.00 5.87  ? 112 PHE   A CB  1 
ATOM   835  C CG  . PHE   A 1 112 ? 114.784 137.752 148.821 1.00 9.52  ? 112 PHE   A CG  1 
ATOM   836  C CD1 . PHE   A 1 112 ? 114.679 138.277 147.545 1.00 13.13 ? 112 PHE   A CD1 1 
ATOM   837  C CD2 . PHE   A 1 112 ? 113.776 138.015 149.732 1.00 6.22  ? 112 PHE   A CD2 1 
ATOM   838  C CE1 . PHE   A 1 112 ? 113.595 139.052 147.186 1.00 9.01  ? 112 PHE   A CE1 1 
ATOM   839  C CE2 . PHE   A 1 112 ? 112.689 138.791 149.379 1.00 8.67  ? 112 PHE   A CE2 1 
ATOM   840  C CZ  . PHE   A 1 112 ? 112.598 139.309 148.105 1.00 9.35  ? 112 PHE   A CZ  1 
ATOM   841  N N   . TYR   A 1 113 ? 117.750 134.133 149.565 1.00 6.34  ? 113 TYR   A N   1 
ATOM   842  C CA  . TYR   A 1 113 ? 118.966 133.370 149.307 1.00 8.15  ? 113 TYR   A CA  1 
ATOM   843  C C   . TYR   A 1 113 ? 118.674 132.130 148.473 1.00 7.34  ? 113 TYR   A C   1 
ATOM   844  O O   . TYR   A 1 113 ? 119.510 131.716 147.664 1.00 13.17 ? 113 TYR   A O   1 
ATOM   845  C CB  . TYR   A 1 113 ? 119.654 132.985 150.615 1.00 12.73 ? 113 TYR   A CB  1 
ATOM   846  C CG  . TYR   A 1 113 ? 121.087 132.546 150.417 1.00 8.99  ? 113 TYR   A CG  1 
ATOM   847  C CD1 . TYR   A 1 113 ? 122.108 133.477 150.294 1.00 10.80 ? 113 TYR   A CD1 1 
ATOM   848  C CD2 . TYR   A 1 113 ? 121.416 131.201 150.341 1.00 6.18  ? 113 TYR   A CD2 1 
ATOM   849  C CE1 . TYR   A 1 113 ? 123.418 133.079 150.106 1.00 9.82  ? 113 TYR   A CE1 1 
ATOM   850  C CE2 . TYR   A 1 113 ? 122.720 130.793 150.153 1.00 7.69  ? 113 TYR   A CE2 1 
ATOM   851  C CZ  . TYR   A 1 113 ? 123.718 131.735 150.037 1.00 13.32 ? 113 TYR   A CZ  1 
ATOM   852  O OH  . TYR   A 1 113 ? 125.019 131.330 149.852 1.00 11.44 ? 113 TYR   A OH  1 
ATOM   853  N N   . GLY   A 1 114 ? 117.501 131.525 148.653 1.00 8.75  ? 114 GLY   A N   1 
ATOM   854  C CA  . GLY   A 1 114 ? 117.060 130.504 147.720 1.00 3.66  ? 114 GLY   A CA  1 
ATOM   855  C C   . GLY   A 1 114 ? 116.922 131.055 146.317 1.00 7.12  ? 114 GLY   A C   1 
ATOM   856  O O   . GLY   A 1 114 ? 117.257 130.384 145.339 1.00 12.28 ? 114 GLY   A O   1 
ATOM   857  N N   . MET   A 1 115 ? 116.433 132.292 146.203 1.00 13.72 ? 115 MET   A N   1 
ATOM   858  C CA  . MET   A 1 115 ? 116.399 132.963 144.906 1.00 10.69 ? 115 MET   A CA  1 
ATOM   859  C C   . MET   A 1 115 ? 117.797 133.068 144.301 1.00 5.75  ? 115 MET   A C   1 
ATOM   860  O O   . MET   A 1 115 ? 118.006 132.726 143.130 1.00 10.63 ? 115 MET   A O   1 
ATOM   861  C CB  . MET   A 1 115 ? 115.778 134.355 145.044 1.00 9.89  ? 115 MET   A CB  1 
ATOM   862  C CG  . MET   A 1 115 ? 114.271 134.409 144.882 1.00 8.92  ? 115 MET   A CG  1 
ATOM   863  S SD  . MET   A 1 115 ? 113.749 135.893 143.999 1.00 8.52  ? 115 MET   A SD  1 
ATOM   864  C CE  . MET   A 1 115 ? 112.022 135.984 144.461 1.00 10.23 ? 115 MET   A CE  1 
ATOM   865  N N   . VAL   A 1 116 ? 118.769 133.543 145.087 1.00 8.24  ? 116 VAL   A N   1 
ATOM   866  C CA  . VAL   A 1 116 ? 120.114 133.745 144.545 1.00 7.25  ? 116 VAL   A CA  1 
ATOM   867  C C   . VAL   A 1 116 ? 120.751 132.408 144.180 1.00 5.54  ? 116 VAL   A C   1 
ATOM   868  O O   . VAL   A 1 116 ? 121.445 132.299 143.164 1.00 8.99  ? 116 VAL   A O   1 
ATOM   869  C CB  . VAL   A 1 116 ? 121.009 134.561 145.507 1.00 0.39  ? 116 VAL   A CB  1 
ATOM   870  C CG1 . VAL   A 1 116 ? 120.268 135.743 146.088 1.00 9.66  ? 116 VAL   A CG1 1 
ATOM   871  C CG2 . VAL   A 1 116 ? 121.606 133.703 146.615 1.00 0.27  ? 116 VAL   A CG2 1 
ATOM   872  N N   . THR   A 1 117 ? 120.507 131.364 144.972 1.00 7.01  ? 117 THR   A N   1 
ATOM   873  C CA  . THR   A 1 117 ? 121.075 130.057 144.667 1.00 9.24  ? 117 THR   A CA  1 
ATOM   874  C C   . THR   A 1 117 ? 120.415 129.400 143.464 1.00 6.09  ? 117 THR   A C   1 
ATOM   875  O O   . THR   A 1 117 ? 121.094 128.703 142.701 1.00 11.25 ? 117 THR   A O   1 
ATOM   876  C CB  . THR   A 1 117 ? 120.968 129.130 145.881 1.00 5.49  ? 117 THR   A CB  1 
ATOM   877  O OG1 . THR   A 1 117 ? 119.743 129.387 146.576 1.00 7.86  ? 117 THR   A OG1 1 
ATOM   878  C CG2 . THR   A 1 117 ? 122.136 129.356 146.827 1.00 5.62  ? 117 THR   A CG2 1 
ATOM   879  N N   . ALA   A 1 118 ? 119.109 129.598 143.277 1.00 10.01 ? 118 ALA   A N   1 
ATOM   880  C CA  . ALA   A 1 118 ? 118.438 129.060 142.100 1.00 9.66  ? 118 ALA   A CA  1 
ATOM   881  C C   . ALA   A 1 118 ? 118.871 129.801 140.843 1.00 6.76  ? 118 ALA   A C   1 
ATOM   882  O O   . ALA   A 1 118 ? 118.996 129.202 139.769 1.00 4.86  ? 118 ALA   A O   1 
ATOM   883  C CB  . ALA   A 1 118 ? 116.924 129.138 142.280 1.00 10.45 ? 118 ALA   A CB  1 
ATOM   884  N N   . ALA   A 1 119 ? 119.104 131.106 140.958 1.00 7.26  ? 119 ALA   A N   1 
ATOM   885  C CA  . ALA   A 1 119 ? 119.575 131.902 139.836 1.00 11.81 ? 119 ALA   A CA  1 
ATOM   886  C C   . ALA   A 1 119 ? 121.074 131.758 139.600 1.00 8.73  ? 119 ALA   A C   1 
ATOM   887  O O   . ALA   A 1 119 ? 121.571 132.192 138.555 1.00 9.11  ? 119 ALA   A O   1 
ATOM   888  C CB  . ALA   A 1 119 ? 119.206 133.369 140.048 1.00 4.14  ? 119 ALA   A CB  1 
ATOM   889  N N   . GLU   A 1 120 ? 121.804 131.172 140.547 1.00 13.11 ? 120 GLU   A N   1 
ATOM   890  C CA  . GLU   A 1 120 ? 123.188 130.778 140.329 1.00 10.17 ? 120 GLU   A CA  1 
ATOM   891  C C   . GLU   A 1 120 ? 123.325 129.771 139.198 1.00 8.96  ? 120 GLU   A C   1 
ATOM   892  O O   . GLU   A 1 120 ? 124.400 129.670 138.600 1.00 11.00 ? 120 GLU   A O   1 
ATOM   893  C CB  . GLU   A 1 120 ? 123.784 130.199 141.616 1.00 10.49 ? 120 GLU   A CB  1 
ATOM   894  C CG  . GLU   A 1 120 ? 125.298 130.287 141.699 1.00 11.36 ? 120 GLU   A CG  1 
ATOM   895  C CD  . GLU   A 1 120 ? 125.771 131.583 142.329 1.00 16.46 ? 120 GLU   A CD  1 
ATOM   896  O OE1 . GLU   A 1 120 ? 125.139 132.035 143.306 1.00 10.31 ? 120 GLU   A OE1 1 
ATOM   897  O OE2 . GLU   A 1 120 ? 126.775 132.149 141.847 1.00 14.41 ? 120 GLU   A OE2 1 
ATOM   898  N N   . VAL   A 1 121 ? 122.260 129.022 138.895 1.00 9.19  ? 121 VAL   A N   1 
ATOM   899  C CA  . VAL   A 1 121 ? 122.210 128.221 137.678 1.00 12.55 ? 121 VAL   A CA  1 
ATOM   900  C C   . VAL   A 1 121 ? 122.316 129.086 136.433 1.00 7.21  ? 121 VAL   A C   1 
ATOM   901  O O   . VAL   A 1 121 ? 123.063 128.735 135.506 1.00 6.12  ? 121 VAL   A O   1 
ATOM   902  C CB  . VAL   A 1 121 ? 120.912 127.389 137.632 1.00 12.77 ? 121 VAL   A CB  1 
ATOM   903  C CG1 . VAL   A 1 121 ? 120.501 127.100 136.195 1.00 4.10  ? 121 VAL   A CG1 1 
ATOM   904  C CG2 . VAL   A 1 121 ? 121.083 126.101 138.416 1.00 13.17 ? 121 VAL   A CG2 1 
ATOM   905  N N   . ALA   A 1 122 ? 121.606 130.213 136.388 1.00 9.44  ? 122 ALA   A N   1 
ATOM   906  C CA  . ALA   A 1 122 ? 121.750 131.167 135.299 1.00 7.64  ? 122 ALA   A CA  1 
ATOM   907  C C   . ALA   A 1 122 ? 123.162 131.714 135.190 1.00 13.82 ? 122 ALA   A C   1 
ATOM   908  O O   . ALA   A 1 122 ? 123.632 131.962 134.077 1.00 4.46  ? 122 ALA   A O   1 
ATOM   909  C CB  . ALA   A 1 122 ? 120.769 132.328 135.476 1.00 9.04  ? 122 ALA   A CB  1 
ATOM   910  N N   . TYR   A 1 123 ? 123.854 131.893 136.317 1.00 7.97  ? 123 TYR   A N   1 
ATOM   911  C CA  . TYR   A 1 123 ? 125.223 132.397 136.276 1.00 13.37 ? 123 TYR   A CA  1 
ATOM   912  C C   . TYR   A 1 123 ? 126.130 131.460 135.489 1.00 9.46  ? 123 TYR   A C   1 
ATOM   913  O O   . TYR   A 1 123 ? 126.958 131.907 134.688 1.00 13.97 ? 123 TYR   A O   1 
ATOM   914  C CB  . TYR   A 1 123 ? 125.753 132.589 137.697 1.00 17.47 ? 123 TYR   A CB  1 
ATOM   915  C CG  . TYR   A 1 123 ? 127.261 132.601 137.785 1.00 16.41 ? 123 TYR   A CG  1 
ATOM   916  C CD1 . TYR   A 1 123 ? 127.993 133.699 137.356 1.00 12.18 ? 123 TYR   A CD1 1 
ATOM   917  C CD2 . TYR   A 1 123 ? 127.954 131.513 138.294 1.00 14.74 ? 123 TYR   A CD2 1 
ATOM   918  C CE1 . TYR   A 1 123 ? 129.371 133.714 137.433 1.00 15.43 ? 123 TYR   A CE1 1 
ATOM   919  C CE2 . TYR   A 1 123 ? 129.332 131.518 138.373 1.00 12.61 ? 123 TYR   A CE2 1 
ATOM   920  C CZ  . TYR   A 1 123 ? 130.035 132.621 137.942 1.00 12.95 ? 123 TYR   A CZ  1 
ATOM   921  O OH  . TYR   A 1 123 ? 131.409 132.631 138.021 1.00 9.17  ? 123 TYR   A OH  1 
ATOM   922  N N   . TYR   A 1 124 ? 125.989 130.152 135.705 1.00 12.99 ? 124 TYR   A N   1 
ATOM   923  C CA  . TYR   A 1 124 ? 126.840 129.195 135.008 1.00 10.72 ? 124 TYR   A CA  1 
ATOM   924  C C   . TYR   A 1 124 ? 126.421 129.036 133.551 1.00 16.57 ? 124 TYR   A C   1 
ATOM   925  O O   . TYR   A 1 124 ? 127.274 128.914 132.664 1.00 14.07 ? 124 TYR   A O   1 
ATOM   926  C CB  . TYR   A 1 124 ? 126.810 127.850 135.732 1.00 13.79 ? 124 TYR   A CB  1 
ATOM   927  C CG  . TYR   A 1 124 ? 127.523 127.868 137.065 1.00 18.16 ? 124 TYR   A CG  1 
ATOM   928  C CD1 . TYR   A 1 124 ? 128.893 128.079 137.140 1.00 14.58 ? 124 TYR   A CD1 1 
ATOM   929  C CD2 . TYR   A 1 124 ? 126.823 127.687 138.250 1.00 13.39 ? 124 TYR   A CD2 1 
ATOM   930  C CE1 . TYR   A 1 124 ? 129.547 128.101 138.358 1.00 11.99 ? 124 TYR   A CE1 1 
ATOM   931  C CE2 . TYR   A 1 124 ? 127.468 127.709 139.472 1.00 10.02 ? 124 TYR   A CE2 1 
ATOM   932  C CZ  . TYR   A 1 124 ? 128.829 127.916 139.520 1.00 13.48 ? 124 TYR   A CZ  1 
ATOM   933  O OH  . TYR   A 1 124 ? 129.475 127.937 140.735 1.00 9.56  ? 124 TYR   A OH  1 
ATOM   934  N N   . ALA   A 1 125 ? 125.115 129.042 133.282 1.00 13.63 ? 125 ALA   A N   1 
ATOM   935  C CA  . ALA   A 1 125 ? 124.603 128.768 131.945 1.00 15.75 ? 125 ALA   A CA  1 
ATOM   936  C C   . ALA   A 1 125 ? 124.624 129.974 131.018 1.00 20.37 ? 125 ALA   A C   1 
ATOM   937  O O   . ALA   A 1 125 ? 124.523 129.797 129.798 1.00 11.81 ? 125 ALA   A O   1 
ATOM   938  C CB  . ALA   A 1 125 ? 123.169 128.241 132.030 1.00 17.45 ? 125 ALA   A CB  1 
ATOM   939  N N   . TYR   A 1 126 ? 124.745 131.189 131.557 1.00 14.13 ? 126 TYR   A N   1 
ATOM   940  C CA  . TYR   A 1 126 ? 124.711 132.381 130.719 1.00 16.90 ? 126 TYR   A CA  1 
ATOM   941  C C   . TYR   A 1 126 ? 125.898 132.429 129.771 1.00 10.56 ? 126 TYR   A C   1 
ATOM   942  O O   . TYR   A 1 126 ? 125.748 132.762 128.589 1.00 9.96  ? 126 TYR   A O   1 
ATOM   943  C CB  . TYR   A 1 126 ? 124.675 133.625 131.607 1.00 13.12 ? 126 TYR   A CB  1 
ATOM   944  C CG  . TYR   A 1 126 ? 125.225 134.881 130.971 1.00 17.10 ? 126 TYR   A CG  1 
ATOM   945  C CD1 . TYR   A 1 126 ? 126.575 135.200 131.067 1.00 16.80 ? 126 TYR   A CD1 1 
ATOM   946  C CD2 . TYR   A 1 126 ? 124.394 135.760 130.294 1.00 11.04 ? 126 TYR   A CD2 1 
ATOM   947  C CE1 . TYR   A 1 126 ? 127.080 136.341 130.488 1.00 11.29 ? 126 TYR   A CE1 1 
ATOM   948  C CE2 . TYR   A 1 126 ? 124.891 136.910 129.719 1.00 12.03 ? 126 TYR   A CE2 1 
ATOM   949  C CZ  . TYR   A 1 126 ? 126.234 137.195 129.819 1.00 9.29  ? 126 TYR   A CZ  1 
ATOM   950  O OH  . TYR   A 1 126 ? 126.732 138.340 129.246 1.00 13.11 ? 126 TYR   A OH  1 
ATOM   951  N N   . ILE   A 1 127 ? 127.088 132.100 130.273 1.00 14.11 ? 127 ILE   A N   1 
ATOM   952  C CA  . ILE   A 1 127 ? 128.304 132.293 129.495 1.00 16.89 ? 127 ILE   A CA  1 
ATOM   953  C C   . ILE   A 1 127 ? 128.340 131.362 128.289 1.00 11.00 ? 127 ILE   A C   1 
ATOM   954  O O   . ILE   A 1 127 ? 128.894 131.717 127.242 1.00 11.82 ? 127 ILE   A O   1 
ATOM   955  C CB  . ILE   A 1 127 ? 129.532 132.116 130.405 1.00 10.46 ? 127 ILE   A CB  1 
ATOM   956  C CG1 . ILE   A 1 127 ? 130.791 132.649 129.717 1.00 11.43 ? 127 ILE   A CG1 1 
ATOM   957  C CG2 . ILE   A 1 127 ? 129.661 130.672 130.877 1.00 16.81 ? 127 ILE   A CG2 1 
ATOM   958  C CD1 . ILE   A 1 127 ? 130.786 134.144 129.524 1.00 14.32 ? 127 ILE   A CD1 1 
ATOM   959  N N   . TYR   A 1 128 ? 127.753 130.169 128.402 1.00 7.37  ? 128 TYR   A N   1 
ATOM   960  C CA  . TYR   A 1 128 ? 127.712 129.264 127.260 1.00 9.73  ? 128 TYR   A CA  1 
ATOM   961  C C   . TYR   A 1 128 ? 126.750 129.758 126.190 1.00 14.09 ? 128 TYR   A C   1 
ATOM   962  O O   . TYR   A 1 128 ? 126.878 129.383 125.020 1.00 12.50 ? 128 TYR   A O   1 
ATOM   963  C CB  . TYR   A 1 128 ? 127.336 127.859 127.723 1.00 11.15 ? 128 TYR   A CB  1 
ATOM   964  C CG  . TYR   A 1 128 ? 128.253 127.349 128.804 1.00 13.34 ? 128 TYR   A CG  1 
ATOM   965  C CD1 . TYR   A 1 128 ? 129.604 127.155 128.555 1.00 4.55  ? 128 TYR   A CD1 1 
ATOM   966  C CD2 . TYR   A 1 128 ? 127.776 127.085 130.077 1.00 4.86  ? 128 TYR   A CD2 1 
ATOM   967  C CE1 . TYR   A 1 128 ? 130.451 126.701 129.539 1.00 8.90  ? 128 TYR   A CE1 1 
ATOM   968  C CE2 . TYR   A 1 128 ? 128.617 126.631 131.068 1.00 7.65  ? 128 TYR   A CE2 1 
ATOM   969  C CZ  . TYR   A 1 128 ? 129.952 126.440 130.794 1.00 13.53 ? 128 TYR   A CZ  1 
ATOM   970  O OH  . TYR   A 1 128 ? 130.796 125.987 131.779 1.00 9.05  ? 128 TYR   A OH  1 
ATOM   971  N N   . SER   A 1 129 ? 125.789 130.599 126.567 1.00 9.25  ? 129 SER   A N   1 
ATOM   972  C CA  . SER   A 1 129 ? 124.885 131.205 125.602 1.00 12.80 ? 129 SER   A CA  1 
ATOM   973  C C   . SER   A 1 129 ? 125.449 132.473 124.979 1.00 8.32  ? 129 SER   A C   1 
ATOM   974  O O   . SER   A 1 129 ? 124.790 133.066 124.119 1.00 12.62 ? 129 SER   A O   1 
ATOM   975  C CB  . SER   A 1 129 ? 123.543 131.513 126.267 1.00 6.39  ? 129 SER   A CB  1 
ATOM   976  O OG  . SER   A 1 129 ? 123.584 132.758 126.941 1.00 6.59  ? 129 SER   A OG  1 
ATOM   977  N N   . VAL   A 1 130 ? 126.641 132.902 125.389 1.00 8.00  ? 130 VAL   A N   1 
ATOM   978  C CA  . VAL   A 1 130 ? 127.242 134.126 124.874 1.00 10.19 ? 130 VAL   A CA  1 
ATOM   979  C C   . VAL   A 1 130 ? 128.625 133.905 124.278 1.00 6.91  ? 130 VAL   A C   1 
ATOM   980  O O   . VAL   A 1 130 ? 129.132 134.800 123.583 1.00 11.43 ? 130 VAL   A O   1 
ATOM   981  C CB  . VAL   A 1 130 ? 127.301 135.222 125.962 1.00 6.14  ? 130 VAL   A CB  1 
ATOM   982  C CG1 . VAL   A 1 130 ? 128.513 135.028 126.853 1.00 5.65  ? 130 VAL   A CG1 1 
ATOM   983  C CG2 . VAL   A 1 130 ? 127.290 136.612 125.337 1.00 13.41 ? 130 VAL   A CG2 1 
ATOM   984  N N   . VAL   A 1 131 ? 129.254 132.752 124.505 1.00 6.02  ? 131 VAL   A N   1 
ATOM   985  C CA  . VAL   A 1 131 ? 130.545 132.440 123.908 1.00 7.51  ? 131 VAL   A CA  1 
ATOM   986  C C   . VAL   A 1 131 ? 130.388 131.225 123.004 1.00 9.37  ? 131 VAL   A C   1 
ATOM   987  O O   . VAL   A 1 131 ? 129.440 130.443 123.123 1.00 8.91  ? 131 VAL   A O   1 
ATOM   988  C CB  . VAL   A 1 131 ? 131.646 132.194 124.962 1.00 4.41  ? 131 VAL   A CB  1 
ATOM   989  C CG1 . VAL   A 1 131 ? 131.622 133.278 126.025 1.00 12.39 ? 131 VAL   A CG1 1 
ATOM   990  C CG2 . VAL   A 1 131 ? 131.495 130.816 125.587 1.00 13.16 ? 131 VAL   A CG2 1 
ATOM   991  N N   . SER   A 1 132 ? 131.334 131.080 122.080 1.00 12.41 ? 132 SER   A N   1 
ATOM   992  C CA  . SER   A 1 132 ? 131.306 129.966 121.149 1.00 7.12  ? 132 SER   A CA  1 
ATOM   993  C C   . SER   A 1 132 ? 131.644 128.660 121.869 1.00 9.56  ? 132 SER   A C   1 
ATOM   994  O O   . SER   A 1 132 ? 132.307 128.670 122.909 1.00 7.68  ? 132 SER   A O   1 
ATOM   995  C CB  . SER   A 1 132 ? 132.288 130.202 120.005 1.00 9.83  ? 132 SER   A CB  1 
ATOM   996  O OG  . SER   A 1 132 ? 133.477 130.816 120.470 1.00 14.03 ? 132 SER   A OG  1 
ATOM   997  N N   . PRO   A 1 133 ? 131.187 127.521 121.340 1.00 3.09  ? 133 PRO   A N   1 
ATOM   998  C CA  . PRO   A 1 133 ? 131.486 126.238 121.997 1.00 6.66  ? 133 PRO   A CA  1 
ATOM   999  C C   . PRO   A 1 133 ? 132.970 125.941 122.121 1.00 3.23  ? 133 PRO   A C   1 
ATOM   1000 O O   . PRO   A 1 133 ? 133.368 125.204 123.032 1.00 7.72  ? 133 PRO   A O   1 
ATOM   1001 C CB  . PRO   A 1 133 ? 130.780 125.215 121.097 1.00 3.23  ? 133 PRO   A CB  1 
ATOM   1002 C CG  . PRO   A 1 133 ? 129.679 125.984 120.455 1.00 0.84  ? 133 PRO   A CG  1 
ATOM   1003 C CD  . PRO   A 1 133 ? 130.231 127.361 120.230 1.00 7.49  ? 133 PRO   A CD  1 
ATOM   1004 N N   . GLU   A 1 134 ? 133.800 126.495 121.233 1.00 16.69 ? 134 GLU   A N   1 
ATOM   1005 C CA  . GLU   A 1 134 ? 135.233 126.213 121.269 1.00 13.76 ? 134 GLU   A CA  1 
ATOM   1006 C C   . GLU   A 1 134 ? 135.843 126.599 122.611 1.00 11.17 ? 134 GLU   A C   1 
ATOM   1007 O O   . GLU   A 1 134 ? 136.734 125.908 123.118 1.00 9.48  ? 134 GLU   A O   1 
ATOM   1008 C CB  . GLU   A 1 134 ? 135.932 126.948 120.124 1.00 12.28 ? 134 GLU   A CB  1 
ATOM   1009 C CG  . GLU   A 1 134 ? 137.290 127.535 120.478 1.00 9.43  ? 134 GLU   A CG  1 
ATOM   1010 C CD  . GLU   A 1 134 ? 138.014 128.096 119.271 1.00 16.00 ? 134 GLU   A CD  1 
ATOM   1011 O OE1 . GLU   A 1 134 ? 138.028 129.334 119.108 1.00 15.76 ? 134 GLU   A OE1 1 
ATOM   1012 O OE2 . GLU   A 1 134 ? 138.569 127.299 118.485 1.00 13.37 ? 134 GLU   A OE2 1 
ATOM   1013 N N   . HIS   A 1 135 ? 135.365 127.687 123.208 1.00 19.82 ? 135 HIS   A N   1 
ATOM   1014 C CA  . HIS   A 1 135 ? 135.871 128.156 124.490 1.00 17.50 ? 135 HIS   A CA  1 
ATOM   1015 C C   . HIS   A 1 135 ? 135.177 127.502 125.677 1.00 12.54 ? 135 HIS   A C   1 
ATOM   1016 O O   . HIS   A 1 135 ? 135.589 127.739 126.820 1.00 13.49 ? 135 HIS   A O   1 
ATOM   1017 C CB  . HIS   A 1 135 ? 135.724 129.677 124.583 1.00 14.08 ? 135 HIS   A CB  1 
ATOM   1018 C CG  . HIS   A 1 135 ? 136.256 130.405 123.390 1.00 15.50 ? 135 HIS   A CG  1 
ATOM   1019 N ND1 . HIS   A 1 135 ? 137.564 130.292 122.971 1.00 12.66 ? 135 HIS   A ND1 1 
ATOM   1020 C CD2 . HIS   A 1 135 ? 135.655 131.251 122.520 1.00 18.19 ? 135 HIS   A CD2 1 
ATOM   1021 C CE1 . HIS   A 1 135 ? 137.746 131.037 121.896 1.00 17.26 ? 135 HIS   A CE1 1 
ATOM   1022 N NE2 . HIS   A 1 135 ? 136.604 131.630 121.602 1.00 18.32 ? 135 HIS   A NE2 1 
ATOM   1023 N N   . TYR   A 1 136 ? 134.166 126.660 125.429 1.00 9.57  ? 136 TYR   A N   1 
ATOM   1024 C CA  . TYR   A 1 136 ? 133.358 126.110 126.515 1.00 13.72 ? 136 TYR   A CA  1 
ATOM   1025 C C   . TYR   A 1 136 ? 134.211 125.405 127.559 1.00 9.78  ? 136 TYR   A C   1 
ATOM   1026 O O   . TYR   A 1 136 ? 133.832 125.357 128.733 1.00 5.40  ? 136 TYR   A O   1 
ATOM   1027 C CB  . TYR   A 1 136 ? 132.313 125.141 125.966 1.00 13.97 ? 136 TYR   A CB  1 
ATOM   1028 C CG  . TYR   A 1 136 ? 131.066 125.800 125.426 1.00 11.80 ? 136 TYR   A CG  1 
ATOM   1029 C CD1 . TYR   A 1 136 ? 130.958 127.181 125.358 1.00 13.47 ? 136 TYR   A CD1 1 
ATOM   1030 C CD2 . TYR   A 1 136 ? 129.993 125.037 124.985 1.00 14.76 ? 136 TYR   A CD2 1 
ATOM   1031 C CE1 . TYR   A 1 136 ? 129.820 127.783 124.862 1.00 5.75  ? 136 TYR   A CE1 1 
ATOM   1032 C CE2 . TYR   A 1 136 ? 128.851 125.630 124.488 1.00 7.59  ? 136 TYR   A CE2 1 
ATOM   1033 C CZ  . TYR   A 1 136 ? 128.770 127.003 124.430 1.00 5.88  ? 136 TYR   A CZ  1 
ATOM   1034 O OH  . TYR   A 1 136 ? 127.633 127.598 123.935 1.00 9.46  ? 136 TYR   A OH  1 
ATOM   1035 N N   . GLN   A 1 137 ? 135.353 124.847 127.158 1.00 16.94 ? 137 GLN   A N   1 
ATOM   1036 C CA  . GLN   A 1 137 ? 136.281 124.302 128.142 1.00 9.12  ? 137 GLN   A CA  1 
ATOM   1037 C C   . GLN   A 1 137 ? 136.863 125.413 129.004 1.00 13.04 ? 137 GLN   A C   1 
ATOM   1038 O O   . GLN   A 1 137 ? 136.565 125.505 130.203 1.00 9.56  ? 137 GLN   A O   1 
ATOM   1039 C CB  . GLN   A 1 137 ? 137.395 123.525 127.436 1.00 16.03 ? 137 GLN   A CB  1 
ATOM   1040 C CG  . GLN   A 1 137 ? 138.633 123.294 128.293 1.00 16.72 ? 137 GLN   A CG  1 
ATOM   1041 C CD  . GLN   A 1 137 ? 139.451 122.106 127.839 1.00 8.74  ? 137 GLN   A CD  1 
ATOM   1042 O OE1 . GLN   A 1 137 ? 139.536 121.096 128.534 1.00 13.17 ? 137 GLN   A OE1 1 
ATOM   1043 N NE2 . GLN   A 1 137 ? 140.058 122.219 126.664 1.00 10.70 ? 137 GLN   A NE2 1 
ATOM   1044 N N   . ARG   A 1 138 ? 137.639 126.310 128.386 1.00 17.54 ? 138 ARG   A N   1 
ATOM   1045 C CA  . ARG   A 1 138 ? 138.361 127.332 129.136 1.00 17.45 ? 138 ARG   A CA  1 
ATOM   1046 C C   . ARG   A 1 138 ? 137.409 128.098 130.037 1.00 14.15 ? 138 ARG   A C   1 
ATOM   1047 O O   . ARG   A 1 138 ? 137.527 128.070 131.271 1.00 17.75 ? 138 ARG   A O   1 
ATOM   1048 C CB  . ARG   A 1 138 ? 139.066 128.288 128.171 1.00 11.46 ? 138 ARG   A CB  1 
ATOM   1049 C CG  . ARG   A 1 138 ? 140.400 127.793 127.647 1.00 16.99 ? 138 ARG   A CG  1 
ATOM   1050 C CD  . ARG   A 1 138 ? 141.001 128.791 126.672 1.00 12.36 ? 138 ARG   A CD  1 
ATOM   1051 N NE  . ARG   A 1 138 ? 140.279 128.814 125.406 1.00 10.37 ? 138 ARG   A NE  1 
ATOM   1052 C CZ  . ARG   A 1 138 ? 140.831 128.576 124.225 1.00 17.42 ? 138 ARG   A CZ  1 
ATOM   1053 N NH1 . ARG   A 1 138 ? 142.118 128.293 124.108 1.00 14.86 ? 138 ARG   A NH1 1 
ATOM   1054 N NH2 . ARG   A 1 138 ? 140.074 128.622 123.133 1.00 8.66  ? 138 ARG   A NH2 1 
ATOM   1055 N N   . VAL   A 1 139 ? 136.407 128.717 129.417 1.00 12.77 ? 139 VAL   A N   1 
ATOM   1056 C CA  . VAL   A 1 139 ? 135.364 129.478 130.085 1.00 11.08 ? 139 VAL   A CA  1 
ATOM   1057 C C   . VAL   A 1 139 ? 134.910 128.717 131.318 1.00 10.11 ? 139 VAL   A C   1 
ATOM   1058 O O   . VAL   A 1 139 ? 134.993 129.239 132.439 1.00 11.39 ? 139 VAL   A O   1 
ATOM   1059 C CB  . VAL   A 1 139 ? 134.186 129.725 129.127 1.00 6.60  ? 139 VAL   A CB  1 
ATOM   1060 C CG1 . VAL   A 1 139 ? 132.915 129.937 129.905 1.00 10.07 ? 139 VAL   A CG1 1 
ATOM   1061 C CG2 . VAL   A 1 139 ? 134.475 130.896 128.210 1.00 12.21 ? 139 VAL   A CG2 1 
ATOM   1062 N N   . SER   A 1 140 ? 134.507 127.455 131.120 1.00 9.33  ? 140 SER   A N   1 
ATOM   1063 C CA  . SER   A 1 140 ? 133.980 126.654 132.219 1.00 10.09 ? 140 SER   A CA  1 
ATOM   1064 C C   . SER   A 1 140 ? 134.882 126.768 133.432 1.00 17.21 ? 140 SER   A C   1 
ATOM   1065 O O   . SER   A 1 140 ? 134.490 127.327 134.467 1.00 14.97 ? 140 SER   A O   1 
ATOM   1066 C CB  . SER   A 1 140 ? 133.843 125.191 131.792 1.00 14.10 ? 140 SER   A CB  1 
ATOM   1067 O OG  . SER   A 1 140 ? 132.680 124.994 131.009 1.00 11.27 ? 140 SER   A OG  1 
ATOM   1068 N N   . GLY   A 1 141 ? 136.132 126.326 133.276 1.00 10.45 ? 141 GLY   A N   1 
ATOM   1069 C CA  . GLY   A 1 141 ? 137.091 126.360 134.354 1.00 16.22 ? 141 GLY   A CA  1 
ATOM   1070 C C   . GLY   A 1 141 ? 137.060 127.717 135.005 1.00 11.71 ? 141 GLY   A C   1 
ATOM   1071 O O   . GLY   A 1 141 ? 136.648 127.846 136.167 1.00 8.14  ? 141 GLY   A O   1 
ATOM   1072 N N   . TYR   A 1 142 ? 137.367 128.743 134.206 1.00 18.01 ? 142 TYR   A N   1 
ATOM   1073 C CA  . TYR   A 1 142 ? 137.496 130.086 134.748 1.00 11.07 ? 142 TYR   A CA  1 
ATOM   1074 C C   . TYR   A 1 142 ? 136.269 130.435 135.568 1.00 17.30 ? 142 TYR   A C   1 
ATOM   1075 O O   . TYR   A 1 142 ? 136.378 130.760 136.758 1.00 17.85 ? 142 TYR   A O   1 
ATOM   1076 C CB  . TYR   A 1 142 ? 137.704 131.095 133.617 1.00 13.90 ? 142 TYR   A CB  1 
ATOM   1077 C CG  . TYR   A 1 142 ? 138.955 130.857 132.801 1.00 15.02 ? 142 TYR   A CG  1 
ATOM   1078 C CD1 . TYR   A 1 142 ? 139.998 130.085 133.298 1.00 14.31 ? 142 TYR   A CD1 1 
ATOM   1079 C CD2 . TYR   A 1 142 ? 139.092 131.401 131.532 1.00 15.28 ? 142 TYR   A CD2 1 
ATOM   1080 C CE1 . TYR   A 1 142 ? 141.140 129.864 132.556 1.00 17.59 ? 142 TYR   A CE1 1 
ATOM   1081 C CE2 . TYR   A 1 142 ? 140.232 131.186 130.782 1.00 11.86 ? 142 TYR   A CE2 1 
ATOM   1082 C CZ  . TYR   A 1 142 ? 141.252 130.417 131.299 1.00 17.87 ? 142 TYR   A CZ  1 
ATOM   1083 O OH  . TYR   A 1 142 ? 142.389 130.200 130.555 1.00 14.71 ? 142 TYR   A OH  1 
ATOM   1084 N N   . CYS   A 1 143 ? 135.084 130.248 134.978 1.00 10.86 ? 143 CYS   A N   1 
ATOM   1085 C CA  . CYS   A 1 143 ? 133.854 130.578 135.683 1.00 11.98 ? 143 CYS   A CA  1 
ATOM   1086 C C   . CYS   A 1 143 ? 133.835 129.885 137.034 1.00 15.67 ? 143 CYS   A C   1 
ATOM   1087 O O   . CYS   A 1 143 ? 133.939 130.534 138.085 1.00 12.10 ? 143 CYS   A O   1 
ATOM   1088 C CB  . CYS   A 1 143 ? 132.640 130.177 134.843 1.00 11.02 ? 143 CYS   A CB  1 
ATOM   1089 S SG  . CYS   A 1 143 ? 132.151 131.404 133.611 1.00 11.32 ? 143 CYS   A SG  1 
ATOM   1090 N N   . ARG   A 1 144 ? 133.833 128.551 137.016 1.00 14.70 ? 144 ARG   A N   1 
ATOM   1091 C CA  . ARG   A 1 144 ? 133.803 127.818 138.271 1.00 12.27 ? 144 ARG   A CA  1 
ATOM   1092 C C   . ARG   A 1 144 ? 134.955 128.262 139.153 1.00 15.88 ? 144 ARG   A C   1 
ATOM   1093 O O   . ARG   A 1 144 ? 134.754 128.634 140.318 1.00 9.70  ? 144 ARG   A O   1 
ATOM   1094 C CB  . ARG   A 1 144 ? 133.858 126.314 138.005 1.00 12.20 ? 144 ARG   A CB  1 
ATOM   1095 C CG  . ARG   A 1 144 ? 133.741 125.465 139.255 1.00 12.24 ? 144 ARG   A CG  1 
ATOM   1096 C CD  . ARG   A 1 144 ? 132.338 125.527 139.833 1.00 12.41 ? 144 ARG   A CD  1 
ATOM   1097 N NE  . ARG   A 1 144 ? 131.327 125.109 138.869 1.00 6.84  ? 144 ARG   A NE  1 
ATOM   1098 C CZ  . ARG   A 1 144 ? 130.063 124.851 139.177 1.00 13.75 ? 144 ARG   A CZ  1 
ATOM   1099 N NH1 . ARG   A 1 144 ? 129.620 124.951 140.419 1.00 15.73 ? 144 ARG   A NH1 1 
ATOM   1100 N NH2 . ARG   A 1 144 ? 129.223 124.483 138.213 1.00 11.59 ? 144 ARG   A NH2 1 
ATOM   1101 N N   . SER   A 1 145 ? 136.153 128.352 138.566 1.00 9.16  ? 145 SER   A N   1 
ATOM   1102 C CA  . SER   A 1 145 ? 137.329 128.707 139.345 1.00 14.76 ? 145 SER   A CA  1 
ATOM   1103 C C   . SER   A 1 145 ? 137.095 130.012 140.082 1.00 7.31  ? 145 SER   A C   1 
ATOM   1104 O O   . SER   A 1 145 ? 137.211 130.070 141.314 1.00 10.52 ? 145 SER   A O   1 
ATOM   1105 C CB  . SER   A 1 145 ? 138.557 128.808 138.440 1.00 16.41 ? 145 SER   A CB  1 
ATOM   1106 O OG  . SER   A 1 145 ? 139.469 129.778 138.925 1.00 13.12 ? 145 SER   A OG  1 
ATOM   1107 N N   . VAL   A 1 146 ? 136.669 131.050 139.356 1.00 11.15 ? 146 VAL   A N   1 
ATOM   1108 C CA  . VAL   A 1 146 ? 136.574 132.352 140.001 1.00 8.64  ? 146 VAL   A CA  1 
ATOM   1109 C C   . VAL   A 1 146 ? 135.548 132.287 141.119 1.00 10.82 ? 146 VAL   A C   1 
ATOM   1110 O O   . VAL   A 1 146 ? 135.792 132.775 142.232 1.00 11.39 ? 146 VAL   A O   1 
ATOM   1111 C CB  . VAL   A 1 146 ? 136.275 133.468 138.977 1.00 5.81  ? 146 VAL   A CB  1 
ATOM   1112 C CG1 . VAL   A 1 146 ? 134.863 133.384 138.425 1.00 3.83  ? 146 VAL   A CG1 1 
ATOM   1113 C CG2 . VAL   A 1 146 ? 136.539 134.832 139.589 1.00 9.81  ? 146 VAL   A CG2 1 
ATOM   1114 N N   . THR   A 1 147 ? 134.435 131.583 140.879 1.00 8.73  ? 147 THR   A N   1 
ATOM   1115 C CA  . THR   A 1 147 ? 133.432 131.423 141.922 1.00 5.60  ? 147 THR   A CA  1 
ATOM   1116 C C   . THR   A 1 147 ? 134.066 130.831 143.168 1.00 10.23 ? 147 THR   A C   1 
ATOM   1117 O O   . THR   A 1 147 ? 133.998 131.419 144.256 1.00 4.69  ? 147 THR   A O   1 
ATOM   1118 C CB  . THR   A 1 147 ? 132.287 130.543 141.420 1.00 6.33  ? 147 THR   A CB  1 
ATOM   1119 O OG1 . THR   A 1 147 ? 131.396 131.330 140.621 1.00 12.21 ? 147 THR   A OG1 1 
ATOM   1120 C CG2 . THR   A 1 147 ? 131.518 129.945 142.584 1.00 4.45  ? 147 THR   A CG2 1 
ATOM   1121 N N   . LEU   A 1 148 ? 134.772 129.711 143.006 1.00 7.15  ? 148 LEU   A N   1 
ATOM   1122 C CA  . LEU   A 1 148 ? 135.449 129.109 144.145 1.00 4.33  ? 148 LEU   A CA  1 
ATOM   1123 C C   . LEU   A 1 148 ? 136.468 130.075 144.722 1.00 14.09 ? 148 LEU   A C   1 
ATOM   1124 O O   . LEU   A 1 148 ? 136.509 130.298 145.939 1.00 9.94  ? 148 LEU   A O   1 
ATOM   1125 C CB  . LEU   A 1 148 ? 136.103 127.797 143.727 1.00 7.05  ? 148 LEU   A CB  1 
ATOM   1126 C CG  . LEU   A 1 148 ? 135.087 126.779 143.220 1.00 13.40 ? 148 LEU   A CG  1 
ATOM   1127 C CD1 . LEU   A 1 148 ? 135.739 125.803 142.263 1.00 9.19  ? 148 LEU   A CD1 1 
ATOM   1128 C CD2 . LEU   A 1 148 ? 134.460 126.061 144.401 1.00 8.66  ? 148 LEU   A CD2 1 
ATOM   1129 N N   . ALA   A 1 149 ? 137.256 130.713 143.848 1.00 8.76  ? 149 ALA   A N   1 
ATOM   1130 C CA  . ALA   A 1 149 ? 138.189 131.726 144.318 1.00 5.53  ? 149 ALA   A CA  1 
ATOM   1131 C C   . ALA   A 1 149 ? 137.446 132.749 145.156 1.00 5.94  ? 149 ALA   A C   1 
ATOM   1132 O O   . ALA   A 1 149 ? 137.820 133.023 146.304 1.00 6.60  ? 149 ALA   A O   1 
ATOM   1133 C CB  . ALA   A 1 149 ? 138.892 132.391 143.134 1.00 5.33  ? 149 ALA   A CB  1 
ATOM   1134 N N   . ALA   A 1 150 ? 136.323 133.242 144.623 1.00 9.75  ? 150 ALA   A N   1 
ATOM   1135 C CA  . ALA   A 1 150 ? 135.457 134.147 145.359 1.00 10.86 ? 150 ALA   A CA  1 
ATOM   1136 C C   . ALA   A 1 150 ? 135.297 133.675 146.791 1.00 4.62  ? 150 ALA   A C   1 
ATOM   1137 O O   . ALA   A 1 150 ? 135.760 134.332 147.734 1.00 13.61 ? 150 ALA   A O   1 
ATOM   1138 C CB  . ALA   A 1 150 ? 134.096 134.233 144.668 1.00 11.43 ? 150 ALA   A CB  1 
ATOM   1139 N N   . TYR   A 1 151 ? 134.737 132.472 146.950 1.00 13.49 ? 151 TYR   A N   1 
ATOM   1140 C CA  . TYR   A 1 151 ? 134.454 131.973 148.287 1.00 12.95 ? 151 TYR   A CA  1 
ATOM   1141 C C   . TYR   A 1 151 ? 135.711 132.007 149.137 1.00 6.23  ? 151 TYR   A C   1 
ATOM   1142 O O   . TYR   A 1 151 ? 135.751 132.681 150.176 1.00 10.25 ? 151 TYR   A O   1 
ATOM   1143 C CB  . TYR   A 1 151 ? 133.883 130.557 148.214 1.00 9.89  ? 151 TYR   A CB  1 
ATOM   1144 C CG  . TYR   A 1 151 ? 133.474 129.995 149.557 1.00 12.16 ? 151 TYR   A CG  1 
ATOM   1145 C CD1 . TYR   A 1 151 ? 132.269 130.358 150.145 1.00 9.92  ? 151 TYR   A CD1 1 
ATOM   1146 C CD2 . TYR   A 1 151 ? 134.292 129.104 150.239 1.00 12.48 ? 151 TYR   A CD2 1 
ATOM   1147 C CE1 . TYR   A 1 151 ? 131.890 129.848 151.372 1.00 12.25 ? 151 TYR   A CE1 1 
ATOM   1148 C CE2 . TYR   A 1 151 ? 133.922 128.590 151.467 1.00 12.40 ? 151 TYR   A CE2 1 
ATOM   1149 C CZ  . TYR   A 1 151 ? 132.721 128.965 152.029 1.00 11.62 ? 151 TYR   A CZ  1 
ATOM   1150 O OH  . TYR   A 1 151 ? 132.348 128.455 153.251 1.00 6.94  ? 151 TYR   A OH  1 
ATOM   1151 N N   . THR   A 1 152 ? 136.792 131.389 148.648 1.00 9.61  ? 152 THR   A N   1 
ATOM   1152 C CA  . THR   A 1 152 ? 137.982 131.308 149.484 1.00 9.82  ? 152 THR   A CA  1 
ATOM   1153 C C   . THR   A 1 152 ? 138.506 132.704 149.773 1.00 11.05 ? 152 THR   A C   1 
ATOM   1154 O O   . THR   A 1 152 ? 138.827 133.021 150.926 1.00 4.34  ? 152 THR   A O   1 
ATOM   1155 C CB  . THR   A 1 152 ? 139.052 130.404 148.852 1.00 3.77  ? 152 THR   A CB  1 
ATOM   1156 O OG1 . THR   A 1 152 ? 140.108 130.183 149.795 1.00 5.92  ? 152 THR   A OG1 1 
ATOM   1157 C CG2 . THR   A 1 152 ? 139.644 130.990 147.584 1.00 5.21  ? 152 THR   A CG2 1 
ATOM   1158 N N   . ALA   A 1 153 ? 138.487 133.583 148.764 1.00 10.26 ? 153 ALA   A N   1 
ATOM   1159 C CA  . ALA   A 1 153 ? 138.848 134.974 148.995 1.00 8.24  ? 153 ALA   A CA  1 
ATOM   1160 C C   . ALA   A 1 153 ? 138.042 135.522 150.158 1.00 9.70  ? 153 ALA   A C   1 
ATOM   1161 O O   . ALA   A 1 153 ? 138.594 135.837 151.222 1.00 6.38  ? 153 ALA   A O   1 
ATOM   1162 C CB  . ALA   A 1 153 ? 138.618 135.800 147.728 1.00 3.10  ? 153 ALA   A CB  1 
ATOM   1163 N N   . GLY   A 1 154 ? 136.715 135.530 150.008 1.00 5.35  ? 154 GLY   A N   1 
ATOM   1164 C CA  . GLY   A 1 154 ? 135.877 135.993 151.096 1.00 7.93  ? 154 GLY   A CA  1 
ATOM   1165 C C   . GLY   A 1 154 ? 136.231 135.288 152.383 1.00 6.14  ? 154 GLY   A C   1 
ATOM   1166 O O   . GLY   A 1 154 ? 136.527 135.930 153.396 1.00 12.40 ? 154 GLY   A O   1 
ATOM   1167 N N   . SER   A 1 155 ? 136.330 133.957 152.319 1.00 10.43 ? 155 SER   A N   1 
ATOM   1168 C CA  . SER   A 1 155 ? 136.681 133.177 153.496 1.00 11.32 ? 155 SER   A CA  1 
ATOM   1169 C C   . SER   A 1 155 ? 137.931 133.744 154.147 1.00 9.35  ? 155 SER   A C   1 
ATOM   1170 O O   . SER   A 1 155 ? 137.883 134.243 155.279 1.00 5.32  ? 155 SER   A O   1 
ATOM   1171 C CB  . SER   A 1 155 ? 136.876 131.709 153.115 1.00 6.78  ? 155 SER   A CB  1 
ATOM   1172 O OG  . SER   A 1 155 ? 135.630 131.049 152.976 1.00 9.05  ? 155 SER   A OG  1 
ATOM   1173 N N   . VAL   A 1 156 ? 139.043 133.767 153.405 1.00 9.69  ? 156 VAL   A N   1 
ATOM   1174 C CA  . VAL   A 1 156 ? 140.282 134.223 154.022 1.00 7.95  ? 156 VAL   A CA  1 
ATOM   1175 C C   . VAL   A 1 156 ? 140.130 135.672 154.451 1.00 14.99 ? 156 VAL   A C   1 
ATOM   1176 O O   . VAL   A 1 156 ? 140.500 136.040 155.574 1.00 14.95 ? 156 VAL   A O   1 
ATOM   1177 C CB  . VAL   A 1 156 ? 141.494 134.000 153.092 1.00 11.00 ? 156 VAL   A CB  1 
ATOM   1178 C CG1 . VAL   A 1 156 ? 141.373 134.772 151.792 1.00 16.13 ? 156 VAL   A CG1 1 
ATOM   1179 C CG2 . VAL   A 1 156 ? 142.786 134.366 153.811 1.00 11.98 ? 156 VAL   A CG2 1 
ATOM   1180 N N   . LEU   A 1 157 ? 139.486 136.490 153.610 1.00 13.62 ? 157 LEU   A N   1 
ATOM   1181 C CA  . LEU   A 1 157 ? 139.241 137.875 153.988 1.00 11.54 ? 157 LEU   A CA  1 
ATOM   1182 C C   . LEU   A 1 157 ? 138.499 137.929 155.311 1.00 10.78 ? 157 LEU   A C   1 
ATOM   1183 O O   . LEU   A 1 157 ? 138.966 138.555 156.274 1.00 6.98  ? 157 LEU   A O   1 
ATOM   1184 C CB  . LEU   A 1 157 ? 138.452 138.590 152.890 1.00 10.27 ? 157 LEU   A CB  1 
ATOM   1185 C CG  . LEU   A 1 157 ? 137.985 140.013 153.199 1.00 13.92 ? 157 LEU   A CG  1 
ATOM   1186 C CD1 . LEU   A 1 157 ? 139.173 140.920 153.474 1.00 8.02  ? 157 LEU   A CD1 1 
ATOM   1187 C CD2 . LEU   A 1 157 ? 137.142 140.561 152.058 1.00 13.68 ? 157 LEU   A CD2 1 
ATOM   1188 N N   . ALA   A 1 158 ? 137.386 137.194 155.401 1.00 14.30 ? 158 ALA   A N   1 
ATOM   1189 C CA  . ALA   A 1 158 ? 136.621 137.159 156.638 1.00 8.51  ? 158 ALA   A CA  1 
ATOM   1190 C C   . ALA   A 1 158 ? 137.525 136.812 157.806 1.00 12.04 ? 158 ALA   A C   1 
ATOM   1191 O O   . ALA   A 1 158 ? 137.538 137.512 158.826 1.00 14.20 ? 158 ALA   A O   1 
ATOM   1192 C CB  . ALA   A 1 158 ? 135.476 136.153 156.520 1.00 5.97  ? 158 ALA   A CB  1 
ATOM   1193 N N   . GLN   A 1 159 ? 138.356 135.780 157.633 1.00 24.78 ? 159 GLN   A N   1 
ATOM   1194 C CA  . GLN   A 1 159 ? 139.212 135.342 158.726 1.00 17.90 ? 159 GLN   A CA  1 
ATOM   1195 C C   . GLN   A 1 159 ? 140.081 136.490 159.215 1.00 24.49 ? 159 GLN   A C   1 
ATOM   1196 O O   . GLN   A 1 159 ? 140.112 136.791 160.416 1.00 22.67 ? 159 GLN   A O   1 
ATOM   1197 C CB  . GLN   A 1 159 ? 140.069 134.157 158.283 1.00 19.44 ? 159 GLN   A CB  1 
ATOM   1198 C CG  . GLN   A 1 159 ? 140.332 133.159 159.392 1.00 17.51 ? 159 GLN   A CG  1 
ATOM   1199 C CD  . GLN   A 1 159 ? 139.061 132.765 160.118 1.00 22.35 ? 159 GLN   A CD  1 
ATOM   1200 O OE1 . GLN   A 1 159 ? 138.851 133.135 161.273 1.00 24.47 ? 159 GLN   A OE1 1 
ATOM   1201 N NE2 . GLN   A 1 159 ? 138.205 132.008 159.442 1.00 24.21 ? 159 GLN   A NE2 1 
ATOM   1202 N N   . LEU   A 1 160 ? 140.733 137.196 158.286 1.00 17.76 ? 160 LEU   A N   1 
ATOM   1203 C CA  . LEU   A 1 160 ? 141.585 138.304 158.698 1.00 21.04 ? 160 LEU   A CA  1 
ATOM   1204 C C   . LEU   A 1 160 ? 140.770 139.361 159.426 1.00 17.38 ? 160 LEU   A C   1 
ATOM   1205 O O   . LEU   A 1 160 ? 141.185 139.860 160.480 1.00 13.46 ? 160 LEU   A O   1 
ATOM   1206 C CB  . LEU   A 1 160 ? 142.302 138.908 157.490 1.00 15.77 ? 160 LEU   A CB  1 
ATOM   1207 C CG  . LEU   A 1 160 ? 142.812 137.934 156.427 1.00 14.85 ? 160 LEU   A CG  1 
ATOM   1208 C CD1 . LEU   A 1 160 ? 143.343 138.684 155.216 1.00 21.40 ? 160 LEU   A CD1 1 
ATOM   1209 C CD2 . LEU   A 1 160 ? 143.878 137.013 157.003 1.00 15.28 ? 160 LEU   A CD2 1 
ATOM   1210 N N   . LEU   A 1 161 ? 139.577 139.666 158.912 1.00 24.05 ? 161 LEU   A N   1 
ATOM   1211 C CA  . LEU   A 1 161 ? 138.754 140.693 159.532 1.00 19.32 ? 161 LEU   A CA  1 
ATOM   1212 C C   . LEU   A 1 161 ? 138.308 140.299 160.933 1.00 15.85 ? 161 LEU   A C   1 
ATOM   1213 O O   . LEU   A 1 161 ? 137.965 141.178 161.729 1.00 14.87 ? 161 LEU   A O   1 
ATOM   1214 C CB  . LEU   A 1 161 ? 137.550 140.998 158.642 1.00 17.83 ? 161 LEU   A CB  1 
ATOM   1215 C CG  . LEU   A 1 161 ? 137.947 141.563 157.275 1.00 15.36 ? 161 LEU   A CG  1 
ATOM   1216 C CD1 . LEU   A 1 161 ? 136.742 141.713 156.365 1.00 20.47 ? 161 LEU   A CD1 1 
ATOM   1217 C CD2 . LEU   A 1 161 ? 138.670 142.892 157.435 1.00 18.27 ? 161 LEU   A CD2 1 
ATOM   1218 N N   . VAL   A 1 162 ? 138.324 139.005 161.263 1.00 21.99 ? 162 VAL   A N   1 
ATOM   1219 C CA  . VAL   A 1 162 ? 138.028 138.578 162.627 1.00 21.38 ? 162 VAL   A CA  1 
ATOM   1220 C C   . VAL   A 1 162 ? 139.287 138.218 163.404 1.00 13.57 ? 162 VAL   A C   1 
ATOM   1221 O O   . VAL   A 1 162 ? 139.217 138.047 164.632 1.00 16.03 ? 162 VAL   A O   1 
ATOM   1222 C CB  . VAL   A 1 162 ? 137.031 137.397 162.640 1.00 16.70 ? 162 VAL   A CB  1 
ATOM   1223 C CG1 . VAL   A 1 162 ? 136.321 137.303 163.983 1.00 17.69 ? 162 VAL   A CG1 1 
ATOM   1224 C CG2 . VAL   A 1 162 ? 136.010 137.559 161.531 1.00 19.88 ? 162 VAL   A CG2 1 
ATOM   1225 N N   . SER   A 1 163 ? 140.441 138.123 162.740 1.00 25.64 ? 163 SER   A N   1 
ATOM   1226 C CA  . SER   A 1 163 ? 141.674 137.742 163.411 1.00 24.97 ? 163 SER   A CA  1 
ATOM   1227 C C   . SER   A 1 163 ? 142.698 138.865 163.492 1.00 23.39 ? 163 SER   A C   1 
ATOM   1228 O O   . SER   A 1 163 ? 143.678 138.730 164.232 1.00 29.87 ? 163 SER   A O   1 
ATOM   1229 C CB  . SER   A 1 163 ? 142.310 136.531 162.712 1.00 20.99 ? 163 SER   A CB  1 
ATOM   1230 O OG  . SER   A 1 163 ? 141.529 135.365 162.906 1.00 28.98 ? 163 SER   A OG  1 
ATOM   1231 N N   . LEU   A 1 164 ? 142.503 139.961 162.760 1.00 35.52 ? 164 LEU   A N   1 
ATOM   1232 C CA  . LEU   A 1 164 ? 143.449 141.070 162.772 1.00 40.49 ? 164 LEU   A CA  1 
ATOM   1233 C C   . LEU   A 1 164 ? 142.809 142.438 162.944 1.00 37.19 ? 164 LEU   A C   1 
ATOM   1234 O O   . LEU   A 1 164 ? 143.505 143.367 163.373 1.00 43.38 ? 164 LEU   A O   1 
ATOM   1235 C CB  . LEU   A 1 164 ? 144.283 141.076 161.482 1.00 34.86 ? 164 LEU   A CB  1 
ATOM   1236 C CG  . LEU   A 1 164 ? 145.269 139.918 161.318 1.00 35.51 ? 164 LEU   A CG  1 
ATOM   1237 C CD1 . LEU   A 1 164 ? 145.587 139.682 159.850 1.00 42.53 ? 164 LEU   A CD1 1 
ATOM   1238 C CD2 . LEU   A 1 164 ? 146.541 140.179 162.111 1.00 39.47 ? 164 LEU   A CD2 1 
ATOM   1239 N N   . ALA   A 1 165 ? 141.524 142.603 162.630 1.00 31.94 ? 165 ALA   A N   1 
ATOM   1240 C CA  . ALA   A 1 165 ? 140.851 143.889 162.758 1.00 28.86 ? 165 ALA   A CA  1 
ATOM   1241 C C   . ALA   A 1 165 ? 139.617 143.820 163.647 1.00 31.13 ? 165 ALA   A C   1 
ATOM   1242 O O   . ALA   A 1 165 ? 138.858 144.795 163.704 1.00 30.30 ? 165 ALA   A O   1 
ATOM   1243 C CB  . ALA   A 1 165 ? 140.469 144.430 161.377 1.00 30.88 ? 165 ALA   A CB  1 
ATOM   1244 N N   . ASN   A 1 166 ? 139.402 142.694 164.338 1.00 32.98 ? 166 ASN   A N   1 
ATOM   1245 C CA  . ASN   A 1 166 ? 138.253 142.437 165.207 1.00 32.74 ? 166 ASN   A CA  1 
ATOM   1246 C C   . ASN   A 1 166 ? 136.954 142.983 164.624 1.00 31.02 ? 166 ASN   A C   1 
ATOM   1247 O O   . ASN   A 1 166 ? 136.138 143.565 165.345 1.00 28.72 ? 166 ASN   A O   1 
ATOM   1248 C CB  . ASN   A 1 166 ? 138.484 143.001 166.618 1.00 32.28 ? 166 ASN   A CB  1 
ATOM   1249 C CG  . ASN   A 1 166 ? 138.914 144.457 166.616 1.00 28.97 ? 166 ASN   A CG  1 
ATOM   1250 O OD1 . ASN   A 1 166 ? 138.114 145.353 166.347 1.00 27.65 ? 166 ASN   A OD1 1 
ATOM   1251 N ND2 . ASN   A 1 166 ? 140.184 144.698 166.919 1.00 26.77 ? 166 ASN   A ND2 1 
ATOM   1252 N N   . MET   A 1 167 ? 136.756 142.794 163.322 1.00 28.31 ? 167 MET   A N   1 
ATOM   1253 C CA  . MET   A 1 167 ? 135.553 143.286 162.667 1.00 22.93 ? 167 MET   A CA  1 
ATOM   1254 C C   . MET   A 1 167 ? 134.351 142.447 163.080 1.00 23.99 ? 167 MET   A C   1 
ATOM   1255 O O   . MET   A 1 167 ? 134.402 141.213 163.053 1.00 21.60 ? 167 MET   A O   1 
ATOM   1256 C CB  . MET   A 1 167 ? 135.729 143.257 161.150 1.00 27.91 ? 167 MET   A CB  1 
ATOM   1257 C CG  . MET   A 1 167 ? 134.471 143.563 160.365 1.00 22.89 ? 167 MET   A CG  1 
ATOM   1258 S SD  . MET   A 1 167 ? 134.828 144.212 158.723 1.00 22.03 ? 167 MET   A SD  1 
ATOM   1259 C CE  . MET   A 1 167 ? 135.145 145.933 159.101 1.00 26.23 ? 167 MET   A CE  1 
ATOM   1260 N N   . SER   A 1 168 ? 133.270 143.118 163.464 1.00 8.42  ? 168 SER   A N   1 
ATOM   1261 C CA  . SER   A 1 168 ? 132.067 142.418 163.881 1.00 7.70  ? 168 SER   A CA  1 
ATOM   1262 C C   . SER   A 1 168 ? 131.412 141.725 162.691 1.00 14.89 ? 168 SER   A C   1 
ATOM   1263 O O   . SER   A 1 168 ? 131.646 142.066 161.528 1.00 13.96 ? 168 SER   A O   1 
ATOM   1264 C CB  . SER   A 1 168 ? 131.080 143.386 164.534 1.00 12.42 ? 168 SER   A CB  1 
ATOM   1265 O OG  . SER   A 1 168 ? 130.770 144.460 163.665 1.00 8.94  ? 168 SER   A OG  1 
ATOM   1266 N N   . TYR   A 1 169 ? 130.582 140.726 163.000 1.00 15.28 ? 169 TYR   A N   1 
ATOM   1267 C CA  . TYR   A 1 169 ? 129.895 139.983 161.949 1.00 15.43 ? 169 TYR   A CA  1 
ATOM   1268 C C   . TYR   A 1 169 ? 128.947 140.876 161.159 1.00 12.32 ? 169 TYR   A C   1 
ATOM   1269 O O   . TYR   A 1 169 ? 128.703 140.624 159.973 1.00 9.72  ? 169 TYR   A O   1 
ATOM   1270 C CB  . TYR   A 1 169 ? 129.138 138.805 162.559 1.00 17.85 ? 169 TYR   A CB  1 
ATOM   1271 C CG  . TYR   A 1 169 ? 130.015 137.874 163.363 1.00 13.65 ? 169 TYR   A CG  1 
ATOM   1272 C CD1 . TYR   A 1 169 ? 130.964 137.073 162.744 1.00 11.59 ? 169 TYR   A CD1 1 
ATOM   1273 C CD2 . TYR   A 1 169 ? 129.899 137.802 164.745 1.00 16.69 ? 169 TYR   A CD2 1 
ATOM   1274 C CE1 . TYR   A 1 169 ? 131.768 136.224 163.477 1.00 13.34 ? 169 TYR   A CE1 1 
ATOM   1275 C CE2 . TYR   A 1 169 ? 130.699 136.955 165.486 1.00 14.96 ? 169 TYR   A CE2 1 
ATOM   1276 C CZ  . TYR   A 1 169 ? 131.632 136.169 164.847 1.00 12.87 ? 169 TYR   A CZ  1 
ATOM   1277 O OH  . TYR   A 1 169 ? 132.432 135.323 165.580 1.00 10.31 ? 169 TYR   A OH  1 
ATOM   1278 N N   . PHE   A 1 170 ? 128.407 141.919 161.795 1.00 10.01 ? 170 PHE   A N   1 
ATOM   1279 C CA  . PHE   A 1 170 ? 127.556 142.864 161.079 1.00 8.36  ? 170 PHE   A CA  1 
ATOM   1280 C C   . PHE   A 1 170 ? 128.329 143.563 159.968 1.00 10.59 ? 170 PHE   A C   1 
ATOM   1281 O O   . PHE   A 1 170 ? 127.827 143.709 158.849 1.00 14.98 ? 170 PHE   A O   1 
ATOM   1282 C CB  . PHE   A 1 170 ? 126.974 143.888 162.053 1.00 13.72 ? 170 PHE   A CB  1 
ATOM   1283 C CG  . PHE   A 1 170 ? 126.153 144.957 161.390 1.00 14.29 ? 170 PHE   A CG  1 
ATOM   1284 C CD1 . PHE   A 1 170 ? 124.858 144.697 160.976 1.00 7.65  ? 170 PHE   A CD1 1 
ATOM   1285 C CD2 . PHE   A 1 170 ? 126.677 146.222 161.179 1.00 14.35 ? 170 PHE   A CD2 1 
ATOM   1286 C CE1 . PHE   A 1 170 ? 124.099 145.679 160.368 1.00 12.60 ? 170 PHE   A CE1 1 
ATOM   1287 C CE2 . PHE   A 1 170 ? 125.924 147.206 160.569 1.00 9.88  ? 170 PHE   A CE2 1 
ATOM   1288 C CZ  . PHE   A 1 170 ? 124.634 146.934 160.162 1.00 9.32  ? 170 PHE   A CZ  1 
ATOM   1289 N N   . TYR   A 1 171 ? 129.561 143.989 160.250 1.00 7.37  ? 171 TYR   A N   1 
ATOM   1290 C CA  . TYR   A 1 171 ? 130.358 144.622 159.206 1.00 13.96 ? 171 TYR   A CA  1 
ATOM   1291 C C   . TYR   A 1 171 ? 130.881 143.603 158.201 1.00 15.34 ? 171 TYR   A C   1 
ATOM   1292 O O   . TYR   A 1 171 ? 131.130 143.952 157.043 1.00 14.65 ? 171 TYR   A O   1 
ATOM   1293 C CB  . TYR   A 1 171 ? 131.504 145.420 159.824 1.00 8.99  ? 171 TYR   A CB  1 
ATOM   1294 C CG  . TYR   A 1 171 ? 131.059 146.741 160.408 1.00 13.32 ? 171 TYR   A CG  1 
ATOM   1295 C CD1 . TYR   A 1 171 ? 130.646 147.779 159.584 1.00 10.98 ? 171 TYR   A CD1 1 
ATOM   1296 C CD2 . TYR   A 1 171 ? 131.042 146.947 161.780 1.00 13.68 ? 171 TYR   A CD2 1 
ATOM   1297 C CE1 . TYR   A 1 171 ? 130.235 148.987 160.110 1.00 10.35 ? 171 TYR   A CE1 1 
ATOM   1298 C CE2 . TYR   A 1 171 ? 130.632 148.152 162.316 1.00 11.41 ? 171 TYR   A CE2 1 
ATOM   1299 C CZ  . TYR   A 1 171 ? 130.229 149.169 161.476 1.00 13.39 ? 171 TYR   A CZ  1 
ATOM   1300 O OH  . TYR   A 1 171 ? 129.820 150.372 162.004 1.00 6.52  ? 171 TYR   A OH  1 
ATOM   1301 N N   . LEU   A 1 172 ? 131.033 142.341 158.611 1.00 17.52 ? 172 LEU   A N   1 
ATOM   1302 C CA  . LEU   A 1 172 ? 131.308 141.290 157.636 1.00 15.81 ? 172 LEU   A CA  1 
ATOM   1303 C C   . LEU   A 1 172 ? 130.166 141.174 156.635 1.00 18.20 ? 172 LEU   A C   1 
ATOM   1304 O O   . LEU   A 1 172 ? 130.395 141.085 155.423 1.00 21.74 ? 172 LEU   A O   1 
ATOM   1305 C CB  . LEU   A 1 172 ? 131.532 139.955 158.346 1.00 16.08 ? 172 LEU   A CB  1 
ATOM   1306 C CG  . LEU   A 1 172 ? 132.910 139.699 158.954 1.00 16.08 ? 172 LEU   A CG  1 
ATOM   1307 C CD1 . LEU   A 1 172 ? 133.013 138.263 159.439 1.00 20.06 ? 172 LEU   A CD1 1 
ATOM   1308 C CD2 . LEU   A 1 172 ? 133.998 140.001 157.945 1.00 18.60 ? 172 LEU   A CD2 1 
ATOM   1309 N N   . ASN   A 1 173 ? 128.925 141.203 157.124 1.00 14.56 ? 173 ASN   A N   1 
ATOM   1310 C CA  . ASN   A 1 173 ? 127.777 141.179 156.226 1.00 17.51 ? 173 ASN   A CA  1 
ATOM   1311 C C   . ASN   A 1 173 ? 127.669 142.470 155.421 1.00 14.66 ? 173 ASN   A C   1 
ATOM   1312 O O   . ASN   A 1 173 ? 127.176 142.453 154.290 1.00 11.98 ? 173 ASN   A O   1 
ATOM   1313 C CB  . ASN   A 1 173 ? 126.498 140.933 157.022 1.00 15.13 ? 173 ASN   A CB  1 
ATOM   1314 C CG  . ASN   A 1 173 ? 126.382 139.505 157.512 1.00 13.96 ? 173 ASN   A CG  1 
ATOM   1315 O OD1 . ASN   A 1 173 ? 125.566 138.731 157.016 1.00 12.80 ? 173 ASN   A OD1 1 
ATOM   1316 N ND2 . ASN   A 1 173 ? 127.203 139.147 158.493 1.00 19.88 ? 173 ASN   A ND2 1 
ATOM   1317 N N   . VAL   A 1 174 ? 128.119 143.592 155.986 1.00 6.87  ? 174 VAL   A N   1 
ATOM   1318 C CA  . VAL   A 1 174 ? 128.146 144.851 155.241 1.00 5.96  ? 174 VAL   A CA  1 
ATOM   1319 C C   . VAL   A 1 174 ? 129.101 144.745 154.057 1.00 7.44  ? 174 VAL   A C   1 
ATOM   1320 O O   . VAL   A 1 174 ? 128.785 145.162 152.936 1.00 5.39  ? 174 VAL   A O   1 
ATOM   1321 C CB  . VAL   A 1 174 ? 128.534 146.015 156.172 1.00 6.98  ? 174 VAL   A CB  1 
ATOM   1322 C CG1 . VAL   A 1 174 ? 129.037 147.203 155.365 1.00 9.28  ? 174 VAL   A CG1 1 
ATOM   1323 C CG2 . VAL   A 1 174 ? 127.359 146.418 157.044 1.00 8.60  ? 174 VAL   A CG2 1 
ATOM   1324 N N   . ILE   A 1 175 ? 130.290 144.188 154.294 1.00 6.12  ? 175 ILE   A N   1 
ATOM   1325 C CA  . ILE   A 1 175 ? 131.253 143.985 153.217 1.00 7.07  ? 175 ILE   A CA  1 
ATOM   1326 C C   . ILE   A 1 175 ? 130.711 142.983 152.205 1.00 5.16  ? 175 ILE   A C   1 
ATOM   1327 O O   . ILE   A 1 175 ? 130.926 143.120 150.996 1.00 14.23 ? 175 ILE   A O   1 
ATOM   1328 C CB  . ILE   A 1 175 ? 132.610 143.543 153.797 1.00 6.80  ? 175 ILE   A CB  1 
ATOM   1329 C CG1 . ILE   A 1 175 ? 133.325 144.738 154.428 1.00 11.05 ? 175 ILE   A CG1 1 
ATOM   1330 C CG2 . ILE   A 1 175 ? 133.483 142.910 152.726 1.00 5.34  ? 175 ILE   A CG2 1 
ATOM   1331 C CD1 . ILE   A 1 175 ? 134.651 144.394 155.057 1.00 6.55  ? 175 ILE   A CD1 1 
ATOM   1332 N N   . SER   A 1 176 ? 129.986 141.969 152.682 1.00 10.19 ? 176 SER   A N   1 
ATOM   1333 C CA  . SER   A 1 176 ? 129.333 141.029 151.777 1.00 6.22  ? 176 SER   A CA  1 
ATOM   1334 C C   . SER   A 1 176 ? 128.320 141.730 150.879 1.00 9.05  ? 176 SER   A C   1 
ATOM   1335 O O   . SER   A 1 176 ? 128.258 141.466 149.671 1.00 10.55 ? 176 SER   A O   1 
ATOM   1336 C CB  . SER   A 1 176 ? 128.656 139.927 152.588 1.00 8.56  ? 176 SER   A CB  1 
ATOM   1337 O OG  . SER   A 1 176 ? 127.919 139.062 151.750 1.00 10.73 ? 176 SER   A OG  1 
ATOM   1338 N N   . LEU   A 1 177 ? 127.511 142.623 151.454 1.00 7.16  ? 177 LEU   A N   1 
ATOM   1339 C CA  . LEU   A 1 177 ? 126.536 143.372 150.668 1.00 5.70  ? 177 LEU   A CA  1 
ATOM   1340 C C   . LEU   A 1 177 ? 127.226 144.286 149.664 1.00 8.75  ? 177 LEU   A C   1 
ATOM   1341 O O   . LEU   A 1 177 ? 126.775 144.415 148.521 1.00 8.58  ? 177 LEU   A O   1 
ATOM   1342 C CB  . LEU   A 1 177 ? 125.625 144.180 151.590 1.00 8.66  ? 177 LEU   A CB  1 
ATOM   1343 C CG  . LEU   A 1 177 ? 124.754 145.237 150.908 1.00 7.41  ? 177 LEU   A CG  1 
ATOM   1344 C CD1 . LEU   A 1 177 ? 123.680 144.577 150.058 1.00 5.37  ? 177 LEU   A CD1 1 
ATOM   1345 C CD2 . LEU   A 1 177 ? 124.135 146.176 151.929 1.00 7.92  ? 177 LEU   A CD2 1 
ATOM   1346 N N   . ALA   A 1 178 ? 128.316 144.934 150.078 1.00 9.33  ? 178 ALA   A N   1 
ATOM   1347 C CA  . ALA   A 1 178 ? 129.075 145.769 149.154 1.00 5.94  ? 178 ALA   A CA  1 
ATOM   1348 C C   . ALA   A 1 178 ? 129.656 144.947 148.013 1.00 9.77  ? 178 ALA   A C   1 
ATOM   1349 O O   . ALA   A 1 178 ? 129.698 145.413 146.869 1.00 4.38  ? 178 ALA   A O   1 
ATOM   1350 C CB  . ALA   A 1 178 ? 130.186 146.506 149.900 1.00 7.37  ? 178 ALA   A CB  1 
ATOM   1351 N N   . SER   A 1 179 ? 130.110 143.727 148.304 1.00 5.20  ? 179 SER   A N   1 
ATOM   1352 C CA  . SER   A 1 179 ? 130.636 142.856 147.260 1.00 12.47 ? 179 SER   A CA  1 
ATOM   1353 C C   . SER   A 1 179 ? 129.542 142.445 146.284 1.00 10.01 ? 179 SER   A C   1 
ATOM   1354 O O   . SER   A 1 179 ? 129.711 142.559 145.064 1.00 4.88  ? 179 SER   A O   1 
ATOM   1355 C CB  . SER   A 1 179 ? 131.289 141.624 147.888 1.00 7.60  ? 179 SER   A CB  1 
ATOM   1356 O OG  . SER   A 1 179 ? 131.294 140.535 146.984 1.00 10.17 ? 179 SER   A OG  1 
ATOM   1357 N N   . VAL   A 1 180 ? 128.407 141.964 146.799 1.00 10.43 ? 180 VAL   A N   1 
ATOM   1358 C CA  . VAL   A 1 180 ? 127.319 141.564 145.913 1.00 3.29  ? 180 VAL   A CA  1 
ATOM   1359 C C   . VAL   A 1 180 ? 126.692 142.768 145.221 1.00 8.25  ? 180 VAL   A C   1 
ATOM   1360 O O   . VAL   A 1 180 ? 126.073 142.613 144.162 1.00 10.76 ? 180 VAL   A O   1 
ATOM   1361 C CB  . VAL   A 1 180 ? 126.255 140.749 146.673 1.00 9.25  ? 180 VAL   A CB  1 
ATOM   1362 C CG1 . VAL   A 1 180 ? 126.895 139.557 147.368 1.00 12.07 ? 180 VAL   A CG1 1 
ATOM   1363 C CG2 . VAL   A 1 180 ? 125.511 141.620 147.667 1.00 3.50  ? 180 VAL   A CG2 1 
ATOM   1364 N N   . SER   A 1 181 ? 126.831 143.968 145.792 1.00 2.47  ? 181 SER   A N   1 
ATOM   1365 C CA  . SER   A 1 181 ? 126.392 145.170 145.090 1.00 8.89  ? 181 SER   A CA  1 
ATOM   1366 C C   . SER   A 1 181 ? 127.283 145.456 143.890 1.00 7.35  ? 181 SER   A C   1 
ATOM   1367 O O   . SER   A 1 181 ? 126.793 145.832 142.819 1.00 5.70  ? 181 SER   A O   1 
ATOM   1368 C CB  . SER   A 1 181 ? 126.373 146.363 146.044 1.00 8.03  ? 181 SER   A CB  1 
ATOM   1369 O OG  . SER   A 1 181 ? 127.684 146.837 146.292 1.00 8.66  ? 181 SER   A OG  1 
ATOM   1370 N N   . VAL   A 1 182 ? 128.597 145.288 144.053 1.00 12.04 ? 182 VAL   A N   1 
ATOM   1371 C CA  . VAL   A 1 182 ? 129.508 145.390 142.917 1.00 12.30 ? 182 VAL   A CA  1 
ATOM   1372 C C   . VAL   A 1 182 ? 129.211 144.288 141.909 1.00 3.71  ? 182 VAL   A C   1 
ATOM   1373 O O   . VAL   A 1 182 ? 129.277 144.499 140.690 1.00 3.02  ? 182 VAL   A O   1 
ATOM   1374 C CB  . VAL   A 1 182 ? 130.968 145.346 143.408 1.00 3.05  ? 182 VAL   A CB  1 
ATOM   1375 C CG1 . VAL   A 1 182 ? 131.915 145.012 142.271 1.00 2.46  ? 182 VAL   A CG1 1 
ATOM   1376 C CG2 . VAL   A 1 182 ? 131.349 146.669 144.054 1.00 12.04 ? 182 VAL   A CG2 1 
ATOM   1377 N N   . ALA   A 1 183 ? 128.862 143.097 142.403 1.00 2.18  ? 183 ALA   A N   1 
ATOM   1378 C CA  . ALA   A 1 183 ? 128.457 142.013 141.515 1.00 9.65  ? 183 ALA   A CA  1 
ATOM   1379 C C   . ALA   A 1 183 ? 127.210 142.384 140.726 1.00 8.09  ? 183 ALA   A C   1 
ATOM   1380 O O   . ALA   A 1 183 ? 127.108 142.074 139.535 1.00 6.11  ? 183 ALA   A O   1 
ATOM   1381 C CB  . ALA   A 1 183 ? 128.217 140.737 142.317 1.00 4.70  ? 183 ALA   A CB  1 
ATOM   1382 N N   . PHE   A 1 184 ? 126.246 143.040 141.374 1.00 5.79  ? 184 PHE   A N   1 
ATOM   1383 C CA  . PHE   A 1 184 ? 125.050 143.480 140.663 1.00 4.79  ? 184 PHE   A CA  1 
ATOM   1384 C C   . PHE   A 1 184 ? 125.400 144.492 139.578 1.00 11.36 ? 184 PHE   A C   1 
ATOM   1385 O O   . PHE   A 1 184 ? 124.848 144.446 138.472 1.00 9.51  ? 184 PHE   A O   1 
ATOM   1386 C CB  . PHE   A 1 184 ? 124.041 144.067 141.650 1.00 2.51  ? 184 PHE   A CB  1 
ATOM   1387 C CG  . PHE   A 1 184 ? 122.891 144.777 140.994 1.00 6.87  ? 184 PHE   A CG  1 
ATOM   1388 C CD1 . PHE   A 1 184 ? 122.136 144.149 140.017 1.00 5.07  ? 184 PHE   A CD1 1 
ATOM   1389 C CD2 . PHE   A 1 184 ? 122.564 146.072 141.357 1.00 2.54  ? 184 PHE   A CD2 1 
ATOM   1390 C CE1 . PHE   A 1 184 ? 121.080 144.800 139.413 1.00 11.10 ? 184 PHE   A CE1 1 
ATOM   1391 C CE2 . PHE   A 1 184 ? 121.507 146.728 140.757 1.00 9.96  ? 184 PHE   A CE2 1 
ATOM   1392 C CZ  . PHE   A 1 184 ? 120.764 146.091 139.784 1.00 5.55  ? 184 PHE   A CZ  1 
ATOM   1393 N N   . LEU   A 1 185 ? 126.321 145.413 139.876 1.00 7.94  ? 185 LEU   A N   1 
ATOM   1394 C CA  . LEU   A 1 185 ? 126.748 146.383 138.874 1.00 3.22  ? 185 LEU   A CA  1 
ATOM   1395 C C   . LEU   A 1 185 ? 127.420 145.695 137.692 1.00 3.05  ? 185 LEU   A C   1 
ATOM   1396 O O   . LEU   A 1 185 ? 127.190 146.067 136.535 1.00 9.25  ? 185 LEU   A O   1 
ATOM   1397 C CB  . LEU   A 1 185 ? 127.688 147.411 139.503 1.00 9.74  ? 185 LEU   A CB  1 
ATOM   1398 C CG  . LEU   A 1 185 ? 127.123 148.272 140.634 1.00 5.21  ? 185 LEU   A CG  1 
ATOM   1399 C CD1 . LEU   A 1 185 ? 127.970 149.519 140.828 1.00 9.49  ? 185 LEU   A CD1 1 
ATOM   1400 C CD2 . LEU   A 1 185 ? 125.672 148.645 140.366 1.00 8.85  ? 185 LEU   A CD2 1 
ATOM   1401 N N   . PHE   A 1 186 ? 128.261 144.693 137.962 1.00 8.35  ? 186 PHE   A N   1 
ATOM   1402 C CA  . PHE   A 1 186 ? 128.887 143.945 136.875 1.00 6.90  ? 186 PHE   A CA  1 
ATOM   1403 C C   . PHE   A 1 186 ? 127.850 143.180 136.061 1.00 10.27 ? 186 PHE   A C   1 
ATOM   1404 O O   . PHE   A 1 186 ? 127.954 143.101 134.831 1.00 7.73  ? 186 PHE   A O   1 
ATOM   1405 C CB  . PHE   A 1 186 ? 129.944 142.991 137.429 1.00 9.22  ? 186 PHE   A CB  1 
ATOM   1406 C CG  . PHE   A 1 186 ? 131.287 143.629 137.629 1.00 13.08 ? 186 PHE   A CG  1 
ATOM   1407 C CD1 . PHE   A 1 186 ? 131.969 144.184 136.560 1.00 10.91 ? 186 PHE   A CD1 1 
ATOM   1408 C CD2 . PHE   A 1 186 ? 131.871 143.669 138.883 1.00 6.51  ? 186 PHE   A CD2 1 
ATOM   1409 C CE1 . PHE   A 1 186 ? 133.205 144.771 136.738 1.00 4.06  ? 186 PHE   A CE1 1 
ATOM   1410 C CE2 . PHE   A 1 186 ? 133.109 144.254 139.066 1.00 5.02  ? 186 PHE   A CE2 1 
ATOM   1411 C CZ  . PHE   A 1 186 ? 133.776 144.806 137.993 1.00 8.44  ? 186 PHE   A CZ  1 
ATOM   1412 N N   . SER   A 1 187 ? 126.849 142.606 136.730 1.00 5.01  ? 187 SER   A N   1 
ATOM   1413 C CA  . SER   A 1 187 ? 125.790 141.894 136.025 1.00 8.85  ? 187 SER   A CA  1 
ATOM   1414 C C   . SER   A 1 187 ? 124.974 142.832 135.148 1.00 10.17 ? 187 SER   A C   1 
ATOM   1415 O O   . SER   A 1 187 ? 124.494 142.424 134.085 1.00 2.62  ? 187 SER   A O   1 
ATOM   1416 C CB  . SER   A 1 187 ? 124.882 141.178 137.024 1.00 9.44  ? 187 SER   A CB  1 
ATOM   1417 O OG  . SER   A 1 187 ? 124.117 142.106 137.772 1.00 10.41 ? 187 SER   A OG  1 
ATOM   1418 N N   . LEU   A 1 188 ? 124.798 144.083 135.580 1.00 12.80 ? 188 LEU   A N   1 
ATOM   1419 C CA  . LEU   A 1 188 ? 124.129 145.066 134.735 1.00 3.58  ? 188 LEU   A CA  1 
ATOM   1420 C C   . LEU   A 1 188 ? 124.903 145.311 133.446 1.00 3.78  ? 188 LEU   A C   1 
ATOM   1421 O O   . LEU   A 1 188 ? 124.303 145.617 132.410 1.00 3.26  ? 188 LEU   A O   1 
ATOM   1422 C CB  . LEU   A 1 188 ? 123.943 146.376 135.499 1.00 6.33  ? 188 LEU   A CB  1 
ATOM   1423 C CG  . LEU   A 1 188 ? 122.827 146.398 136.544 1.00 3.76  ? 188 LEU   A CG  1 
ATOM   1424 C CD1 . LEU   A 1 188 ? 122.737 147.766 137.198 1.00 6.14  ? 188 LEU   A CD1 1 
ATOM   1425 C CD2 . LEU   A 1 188 ? 121.499 146.011 135.915 1.00 6.76  ? 188 LEU   A CD2 1 
ATOM   1426 N N   . PHE   A 1 189 ? 126.227 145.180 133.489 1.00 9.51  ? 189 PHE   A N   1 
ATOM   1427 C CA  . PHE   A 1 189 ? 127.075 145.380 132.323 1.00 4.74  ? 189 PHE   A CA  1 
ATOM   1428 C C   . PHE   A 1 189 ? 127.334 144.096 131.546 1.00 2.75  ? 189 PHE   A C   1 
ATOM   1429 O O   . PHE   A 1 189 ? 128.111 144.118 130.586 1.00 5.00  ? 189 PHE   A O   1 
ATOM   1430 C CB  . PHE   A 1 189 ? 128.410 146.003 132.743 1.00 6.40  ? 189 PHE   A CB  1 
ATOM   1431 C CG  . PHE   A 1 189 ? 128.272 147.353 133.386 1.00 1.08  ? 189 PHE   A CG  1 
ATOM   1432 C CD1 . PHE   A 1 189 ? 127.379 148.284 132.883 1.00 7.55  ? 189 PHE   A CD1 1 
ATOM   1433 C CD2 . PHE   A 1 189 ? 129.033 147.690 134.492 1.00 8.49  ? 189 PHE   A CD2 1 
ATOM   1434 C CE1 . PHE   A 1 189 ? 127.248 149.527 133.472 1.00 8.41  ? 189 PHE   A CE1 1 
ATOM   1435 C CE2 . PHE   A 1 189 ? 128.907 148.931 135.085 1.00 8.88  ? 189 PHE   A CE2 1 
ATOM   1436 C CZ  . PHE   A 1 189 ? 128.013 149.851 134.574 1.00 3.79  ? 189 PHE   A CZ  1 
ATOM   1437 N N   . LEU   A 1 190 ? 126.717 142.988 131.938 1.00 4.41  ? 190 LEU   A N   1 
ATOM   1438 C CA  . LEU   A 1 190 ? 126.887 141.742 131.206 1.00 0.99  ? 190 LEU   A CA  1 
ATOM   1439 C C   . LEU   A 1 190 ? 126.297 141.880 129.806 1.00 2.23  ? 190 LEU   A C   1 
ATOM   1440 O O   . LEU   A 1 190 ? 125.173 142.380 129.660 1.00 3.96  ? 190 LEU   A O   1 
ATOM   1441 C CB  . LEU   A 1 190 ? 126.213 140.587 131.946 1.00 2.82  ? 190 LEU   A CB  1 
ATOM   1442 C CG  . LEU   A 1 190 ? 127.046 139.845 132.991 1.00 3.32  ? 190 LEU   A CG  1 
ATOM   1443 C CD1 . LEU   A 1 190 ? 126.162 138.943 133.832 1.00 3.16  ? 190 LEU   A CD1 1 
ATOM   1444 C CD2 . LEU   A 1 190 ? 128.139 139.041 132.319 1.00 3.48  ? 190 LEU   A CD2 1 
ATOM   1445 N N   . PRO   A 1 191 ? 127.016 141.475 128.761 1.00 7.74  ? 191 PRO   A N   1 
ATOM   1446 C CA  . PRO   A 1 191 ? 126.440 141.521 127.410 1.00 14.97 ? 191 PRO   A CA  1 
ATOM   1447 C C   . PRO   A 1 191 ? 125.223 140.614 127.302 1.00 12.50 ? 191 PRO   A C   1 
ATOM   1448 O O   . PRO   A 1 191 ? 125.194 139.513 127.855 1.00 8.28  ? 191 PRO   A O   1 
ATOM   1449 C CB  . PRO   A 1 191 ? 127.589 141.042 126.514 1.00 9.63  ? 191 PRO   A CB  1 
ATOM   1450 C CG  . PRO   A 1 191 ? 128.533 140.334 127.430 1.00 7.77  ? 191 PRO   A CG  1 
ATOM   1451 C CD  . PRO   A 1 191 ? 128.414 141.015 128.754 1.00 10.62 ? 191 PRO   A CD  1 
ATOM   1452 N N   . MET   A 1 192 ? 124.215 141.087 126.583 1.00 11.14 ? 192 MET   A N   1 
ATOM   1453 C CA  . MET   A 1 192 ? 122.993 140.313 126.414 1.00 11.95 ? 192 MET   A CA  1 
ATOM   1454 C C   . MET   A 1 192 ? 123.211 139.222 125.371 1.00 12.27 ? 192 MET   A C   1 
ATOM   1455 O O   . MET   A 1 192 ? 123.616 139.524 124.243 1.00 17.21 ? 192 MET   A O   1 
ATOM   1456 C CB  . MET   A 1 192 ? 121.839 141.222 125.999 1.00 16.04 ? 192 MET   A CB  1 
ATOM   1457 C CG  . MET   A 1 192 ? 120.477 140.549 126.019 1.00 19.03 ? 192 MET   A CG  1 
ATOM   1458 S SD  . MET   A 1 192 ? 119.977 140.071 127.682 1.00 12.75 ? 192 MET   A SD  1 
ATOM   1459 C CE  . MET   A 1 192 ? 118.199 139.973 127.498 1.00 16.60 ? 192 MET   A CE  1 
ATOM   1460 N N   . PRO   A 1 193 ? 122.967 137.957 125.704 1.00 9.24  ? 193 PRO   A N   1 
ATOM   1461 C CA  . PRO   A 1 193 ? 123.111 136.893 124.706 1.00 14.06 ? 193 PRO   A CA  1 
ATOM   1462 C C   . PRO   A 1 193 ? 122.096 137.041 123.586 1.00 17.53 ? 193 PRO   A C   1 
ATOM   1463 O O   . PRO   A 1 193 ? 121.016 137.609 123.763 1.00 18.74 ? 193 PRO   A O   1 
ATOM   1464 C CB  . PRO   A 1 193 ? 122.863 135.611 125.510 1.00 9.00  ? 193 PRO   A CB  1 
ATOM   1465 C CG  . PRO   A 1 193 ? 123.080 135.996 126.931 1.00 11.43 ? 193 PRO   A CG  1 
ATOM   1466 C CD  . PRO   A 1 193 ? 122.646 137.424 127.036 1.00 11.14 ? 193 PRO   A CD  1 
ATOM   1467 N N   . LYS   A 1 194 ? 122.463 136.528 122.417 1.00 13.11 ? 194 LYS   A N   1 
ATOM   1468 C CA  . LYS   A 1 194 ? 121.577 136.593 121.265 1.00 12.74 ? 194 LYS   A CA  1 
ATOM   1469 C C   . LYS   A 1 194 ? 120.389 135.656 121.452 1.00 17.54 ? 194 LYS   A C   1 
ATOM   1470 O O   . LYS   A 1 194 ? 120.458 134.663 122.181 1.00 13.09 ? 194 LYS   A O   1 
ATOM   1471 C CB  . LYS   A 1 194 ? 122.338 136.241 119.989 1.00 15.42 ? 194 LYS   A CB  1 
ATOM   1472 C CG  . LYS   A 1 194 ? 123.644 137.004 119.830 1.00 19.03 ? 194 LYS   A CG  1 
ATOM   1473 C CD  . LYS   A 1 194 ? 123.417 138.505 119.899 1.00 15.58 ? 194 LYS   A CD  1 
ATOM   1474 C CE  . LYS   A 1 194 ? 124.724 139.254 120.098 1.00 15.33 ? 194 LYS   A CE  1 
ATOM   1475 N NZ  . LYS   A 1 194 ? 124.565 140.718 119.882 1.00 18.54 ? 194 LYS   A NZ  1 
ATOM   1476 N N   . LYS   A 1 195 ? 119.287 135.987 120.784 1.00 17.50 ? 195 LYS   A N   1 
ATOM   1477 C CA  . LYS   A 1 195 ? 118.053 135.231 120.944 1.00 20.71 ? 195 LYS   A CA  1 
ATOM   1478 C C   . LYS   A 1 195 ? 118.202 133.816 120.396 1.00 18.65 ? 195 LYS   A C   1 
ATOM   1479 O O   . LYS   A 1 195 ? 118.913 133.575 119.416 1.00 20.02 ? 195 LYS   A O   1 
ATOM   1480 C CB  . LYS   A 1 195 ? 116.898 135.944 120.241 1.00 17.22 ? 195 LYS   A CB  1 
ATOM   1481 C CG  . LYS   A 1 195 ? 116.375 137.158 120.990 1.00 16.56 ? 195 LYS   A CG  1 
ATOM   1482 C CD  . LYS   A 1 195 ? 115.344 137.914 120.170 1.00 15.02 ? 195 LYS   A CD  1 
ATOM   1483 C CE  . LYS   A 1 195 ? 114.095 138.203 120.985 1.00 23.06 ? 195 LYS   A CE  1 
ATOM   1484 N NZ  . LYS   A 1 195 ? 113.226 137.001 121.115 1.00 21.74 ? 195 LYS   A NZ  1 
ATOM   1485 N N   . SER   A 1 196 ? 117.519 132.878 121.050 1.00 27.20 ? 196 SER   A N   1 
ATOM   1486 C CA  . SER   A 1 196 ? 117.527 131.467 120.668 1.00 19.67 ? 196 SER   A CA  1 
ATOM   1487 C C   . SER   A 1 196 ? 118.944 130.903 120.605 1.00 27.15 ? 196 SER   A C   1 
ATOM   1488 O O   . SER   A 1 196 ? 119.488 130.686 119.523 1.00 27.18 ? 196 SER   A O   1 
ATOM   1489 C CB  . SER   A 1 196 ? 116.822 131.269 119.324 1.00 20.65 ? 196 SER   A CB  1 
ATOM   1490 O OG  . SER   A 1 196 ? 116.544 129.899 119.089 1.00 20.57 ? 196 SER   A OG  1 
ATOM   1491 N N   . VAL   A 1 261 ? 100.782 121.399 125.701 1.00 55.49 ? 261 VAL   A N   1 
ATOM   1492 C CA  . VAL   A 1 261 ? 101.949 122.272 125.702 1.00 51.83 ? 261 VAL   A CA  1 
ATOM   1493 C C   . VAL   A 1 261 ? 102.976 121.772 126.711 1.00 54.40 ? 261 VAL   A C   1 
ATOM   1494 O O   . VAL   A 1 261 ? 104.175 121.739 126.426 1.00 51.83 ? 261 VAL   A O   1 
ATOM   1495 C CB  . VAL   A 1 261 ? 101.552 123.730 125.997 1.00 59.45 ? 261 VAL   A CB  1 
ATOM   1496 C CG1 . VAL   A 1 261 ? 102.789 124.592 126.203 1.00 54.92 ? 261 VAL   A CG1 1 
ATOM   1497 C CG2 . VAL   A 1 261 ? 100.693 124.283 124.870 1.00 59.62 ? 261 VAL   A CG2 1 
ATOM   1498 N N   . PHE   A 1 262 ? 102.496 121.380 127.895 1.00 68.31 ? 262 PHE   A N   1 
ATOM   1499 C CA  . PHE   A 1 262 ? 103.395 120.881 128.932 1.00 66.70 ? 262 PHE   A CA  1 
ATOM   1500 C C   . PHE   A 1 262 ? 104.143 119.638 128.468 1.00 71.53 ? 262 PHE   A C   1 
ATOM   1501 O O   . PHE   A 1 262 ? 105.378 119.596 128.518 1.00 63.29 ? 262 PHE   A O   1 
ATOM   1502 C CB  . PHE   A 1 262 ? 102.607 120.583 130.207 1.00 68.18 ? 262 PHE   A CB  1 
ATOM   1503 C CG  . PHE   A 1 262 ? 102.671 121.679 131.233 1.00 68.48 ? 262 PHE   A CG  1 
ATOM   1504 C CD1 . PHE   A 1 262 ? 102.209 122.951 130.938 1.00 66.20 ? 262 PHE   A CD1 1 
ATOM   1505 C CD2 . PHE   A 1 262 ? 103.188 121.434 132.494 1.00 62.45 ? 262 PHE   A CD2 1 
ATOM   1506 C CE1 . PHE   A 1 262 ? 102.266 123.960 131.881 1.00 66.78 ? 262 PHE   A CE1 1 
ATOM   1507 C CE2 . PHE   A 1 262 ? 103.246 122.439 133.442 1.00 66.51 ? 262 PHE   A CE2 1 
ATOM   1508 C CZ  . PHE   A 1 262 ? 102.785 123.703 133.135 1.00 69.93 ? 262 PHE   A CZ  1 
ATOM   1509 N N   . VAL   A 1 263 ? 103.412 118.628 127.986 1.00 56.30 ? 263 VAL   A N   1 
ATOM   1510 C CA  . VAL   A 1 263 ? 104.040 117.381 127.547 1.00 57.65 ? 263 VAL   A CA  1 
ATOM   1511 C C   . VAL   A 1 263 ? 105.030 117.663 126.425 1.00 56.14 ? 263 VAL   A C   1 
ATOM   1512 O O   . VAL   A 1 263 ? 106.163 117.166 126.426 1.00 60.60 ? 263 VAL   A O   1 
ATOM   1513 C CB  . VAL   A 1 263 ? 102.971 116.363 127.112 1.00 63.63 ? 263 VAL   A CB  1 
ATOM   1514 C CG1 . VAL   A 1 263 ? 103.595 115.257 126.273 1.00 55.51 ? 263 VAL   A CG1 1 
ATOM   1515 C CG2 . VAL   A 1 263 ? 102.266 115.783 128.327 1.00 61.95 ? 263 VAL   A CG2 1 
ATOM   1516 N N   . GLN   A 1 264 ? 104.613 118.488 125.459 1.00 61.21 ? 264 GLN   A N   1 
ATOM   1517 C CA  . GLN   A 1 264 ? 105.526 118.932 124.412 1.00 59.48 ? 264 GLN   A CA  1 
ATOM   1518 C C   . GLN   A 1 264 ? 106.802 119.508 125.009 1.00 60.29 ? 264 GLN   A C   1 
ATOM   1519 O O   . GLN   A 1 264 ? 107.908 119.142 124.592 1.00 68.25 ? 264 GLN   A O   1 
ATOM   1520 C CB  . GLN   A 1 264 ? 104.839 119.966 123.520 1.00 67.79 ? 264 GLN   A CB  1 
ATOM   1521 C CG  . GLN   A 1 264 ? 105.764 120.626 122.511 1.00 61.79 ? 264 GLN   A CG  1 
ATOM   1522 C CD  . GLN   A 1 264 ? 105.774 122.137 122.634 1.00 68.38 ? 264 GLN   A CD  1 
ATOM   1523 O OE1 . GLN   A 1 264 ? 104.722 122.776 122.661 1.00 67.40 ? 264 GLN   A OE1 1 
ATOM   1524 N NE2 . GLN   A 1 264 ? 106.966 122.717 122.712 1.00 63.25 ? 264 GLN   A NE2 1 
ATOM   1525 N N   . TRP   A 1 265 ? 106.668 120.390 126.006 1.00 48.03 ? 265 TRP   A N   1 
ATOM   1526 C CA  . TRP   A 1 265 ? 107.844 120.907 126.695 1.00 49.65 ? 265 TRP   A CA  1 
ATOM   1527 C C   . TRP   A 1 265 ? 108.695 119.770 127.240 1.00 44.93 ? 265 TRP   A C   1 
ATOM   1528 O O   . TRP   A 1 265 ? 109.910 119.728 127.010 1.00 43.49 ? 265 TRP   A O   1 
ATOM   1529 C CB  . TRP   A 1 265 ? 107.421 121.849 127.822 1.00 46.00 ? 265 TRP   A CB  1 
ATOM   1530 C CG  . TRP   A 1 265 ? 108.569 122.540 128.489 1.00 43.50 ? 265 TRP   A CG  1 
ATOM   1531 C CD1 . TRP   A 1 265 ? 109.184 123.687 128.083 1.00 50.09 ? 265 TRP   A CD1 1 
ATOM   1532 C CD2 . TRP   A 1 265 ? 109.241 122.125 129.684 1.00 48.86 ? 265 TRP   A CD2 1 
ATOM   1533 N NE1 . TRP   A 1 265 ? 110.197 124.014 128.952 1.00 46.56 ? 265 TRP   A NE1 1 
ATOM   1534 C CE2 . TRP   A 1 265 ? 110.253 123.070 129.943 1.00 51.15 ? 265 TRP   A CE2 1 
ATOM   1535 C CE3 . TRP   A 1 265 ? 109.086 121.046 130.560 1.00 44.80 ? 265 TRP   A CE3 1 
ATOM   1536 C CZ2 . TRP   A 1 265 ? 111.104 122.970 131.041 1.00 45.80 ? 265 TRP   A CZ2 1 
ATOM   1537 C CZ3 . TRP   A 1 265 ? 109.933 120.948 131.649 1.00 46.27 ? 265 TRP   A CZ3 1 
ATOM   1538 C CH2 . TRP   A 1 265 ? 110.929 121.904 131.879 1.00 45.31 ? 265 TRP   A CH2 1 
ATOM   1539 N N   . PHE   A 1 266 ? 108.064 118.813 127.928 1.00 45.09 ? 266 PHE   A N   1 
ATOM   1540 C CA  . PHE   A 1 266 ? 108.792 117.638 128.388 1.00 52.91 ? 266 PHE   A CA  1 
ATOM   1541 C C   . PHE   A 1 266 ? 109.447 116.914 127.223 1.00 45.09 ? 266 PHE   A C   1 
ATOM   1542 O O   . PHE   A 1 266 ? 110.618 116.527 127.315 1.00 51.04 ? 266 PHE   A O   1 
ATOM   1543 C CB  . PHE   A 1 266 ? 107.854 116.698 129.144 1.00 45.41 ? 266 PHE   A CB  1 
ATOM   1544 C CG  . PHE   A 1 266 ? 107.887 116.879 130.635 1.00 44.31 ? 266 PHE   A CG  1 
ATOM   1545 C CD1 . PHE   A 1 266 ? 109.093 116.963 131.310 1.00 49.78 ? 266 PHE   A CD1 1 
ATOM   1546 C CD2 . PHE   A 1 266 ? 106.711 116.966 131.362 1.00 53.28 ? 266 PHE   A CD2 1 
ATOM   1547 C CE1 . PHE   A 1 266 ? 109.126 117.129 132.682 1.00 52.81 ? 266 PHE   A CE1 1 
ATOM   1548 C CE2 . PHE   A 1 266 ? 106.737 117.133 132.734 1.00 47.59 ? 266 PHE   A CE2 1 
ATOM   1549 C CZ  . PHE   A 1 266 ? 107.946 117.214 133.394 1.00 44.48 ? 266 PHE   A CZ  1 
ATOM   1550 N N   . GLN   A 1 267 ? 108.725 116.762 126.109 1.00 51.91 ? 267 GLN   A N   1 
ATOM   1551 C CA  . GLN   A 1 267 ? 109.320 116.191 124.911 1.00 51.96 ? 267 GLN   A CA  1 
ATOM   1552 C C   . GLN   A 1 267 ? 110.528 116.988 124.447 1.00 52.59 ? 267 GLN   A C   1 
ATOM   1553 O O   . GLN   A 1 267 ? 111.549 116.387 124.092 1.00 50.60 ? 267 GLN   A O   1 
ATOM   1554 C CB  . GLN   A 1 267 ? 108.283 116.114 123.788 1.00 51.98 ? 267 GLN   A CB  1 
ATOM   1555 C CG  . GLN   A 1 267 ? 108.860 115.746 122.431 1.00 52.88 ? 267 GLN   A CG  1 
ATOM   1556 C CD  . GLN   A 1 267 ? 107.995 116.224 121.281 1.00 48.44 ? 267 GLN   A CD  1 
ATOM   1557 O OE1 . GLN   A 1 267 ? 106.796 115.950 121.235 1.00 49.48 ? 267 GLN   A OE1 1 
ATOM   1558 N NE2 . GLN   A 1 267 ? 108.602 116.942 120.344 1.00 48.96 ? 267 GLN   A NE2 1 
ATOM   1559 N N   . ASP   A 1 268 ? 110.449 118.321 124.481 1.00 50.95 ? 268 ASP   A N   1 
ATOM   1560 C CA  . ASP   A 1 268 ? 111.623 119.130 124.188 1.00 50.86 ? 268 ASP   A CA  1 
ATOM   1561 C C   . ASP   A 1 268 ? 112.758 118.815 125.149 1.00 49.24 ? 268 ASP   A C   1 
ATOM   1562 O O   . ASP   A 1 268 ? 113.910 118.683 124.719 1.00 52.32 ? 268 ASP   A O   1 
ATOM   1563 C CB  . ASP   A 1 268 ? 111.272 120.617 124.248 1.00 49.09 ? 268 ASP   A CB  1 
ATOM   1564 C CG  . ASP   A 1 268 ? 110.568 121.101 122.996 1.00 52.28 ? 268 ASP   A CG  1 
ATOM   1565 O OD1 . ASP   A 1 268 ? 109.961 120.265 122.293 1.00 46.85 ? 268 ASP   A OD1 1 
ATOM   1566 O OD2 . ASP   A 1 268 ? 110.620 122.316 122.714 1.00 45.82 ? 268 ASP   A OD2 1 
ATOM   1567 N N   . LEU   A 1 269 ? 112.446 118.656 126.438 1.00 26.63 ? 269 LEU   A N   1 
ATOM   1568 C CA  . LEU   A 1 269 ? 113.458 118.227 127.395 1.00 24.35 ? 269 LEU   A CA  1 
ATOM   1569 C C   . LEU   A 1 269 ? 114.033 116.877 126.990 1.00 19.53 ? 269 LEU   A C   1 
ATOM   1570 O O   . LEU   A 1 269 ? 115.243 116.646 127.094 1.00 22.74 ? 269 LEU   A O   1 
ATOM   1571 C CB  . LEU   A 1 269 ? 112.856 118.168 128.800 1.00 26.48 ? 269 LEU   A CB  1 
ATOM   1572 C CG  . LEU   A 1 269 ? 113.636 117.404 129.870 1.00 17.74 ? 269 LEU   A CG  1 
ATOM   1573 C CD1 . LEU   A 1 269 ? 114.637 118.322 130.549 1.00 17.77 ? 269 LEU   A CD1 1 
ATOM   1574 C CD2 . LEU   A 1 269 ? 112.690 116.791 130.889 1.00 23.12 ? 269 LEU   A CD2 1 
ATOM   1575 N N   . LYS   A 1 270 ? 113.176 115.981 126.494 1.00 25.97 ? 270 LYS   A N   1 
ATOM   1576 C CA  . LYS   A 1 270 ? 113.653 114.704 125.977 1.00 31.38 ? 270 LYS   A CA  1 
ATOM   1577 C C   . LYS   A 1 270 ? 114.596 114.919 124.801 1.00 29.41 ? 270 LYS   A C   1 
ATOM   1578 O O   . LYS   A 1 270 ? 115.616 114.233 124.671 1.00 30.39 ? 270 LYS   A O   1 
ATOM   1579 C CB  . LYS   A 1 270 ? 112.467 113.826 125.571 1.00 24.81 ? 270 LYS   A CB  1 
ATOM   1580 C CG  . LYS   A 1 270 ? 112.835 112.380 125.283 1.00 24.57 ? 270 LYS   A CG  1 
ATOM   1581 C CD  . LYS   A 1 270 ? 111.833 111.423 125.909 1.00 29.98 ? 270 LYS   A CD  1 
ATOM   1582 C CE  . LYS   A 1 270 ? 112.414 110.025 126.042 1.00 27.82 ? 270 LYS   A CE  1 
ATOM   1583 N NZ  . LYS   A 1 270 ? 111.421 109.063 126.596 1.00 24.60 ? 270 LYS   A NZ  1 
ATOM   1584 N N   . GLU   A 1 271 ? 114.267 115.876 123.928 1.00 51.40 ? 271 GLU   A N   1 
ATOM   1585 C CA  . GLU   A 1 271 ? 115.189 116.228 122.856 1.00 54.41 ? 271 GLU   A CA  1 
ATOM   1586 C C   . GLU   A 1 271 ? 116.425 116.929 123.399 1.00 49.59 ? 271 GLU   A C   1 
ATOM   1587 O O   . GLU   A 1 271 ? 117.497 116.861 122.786 1.00 56.65 ? 271 GLU   A O   1 
ATOM   1588 C CB  . GLU   A 1 271 ? 114.491 117.110 121.821 1.00 57.19 ? 271 GLU   A CB  1 
ATOM   1589 C CG  . GLU   A 1 271 ? 113.181 116.545 121.299 1.00 57.31 ? 271 GLU   A CG  1 
ATOM   1590 C CD  . GLU   A 1 271 ? 112.499 117.474 120.315 1.00 54.99 ? 271 GLU   A CD  1 
ATOM   1591 O OE1 . GLU   A 1 271 ? 112.663 118.705 120.446 1.00 51.75 ? 271 GLU   A OE1 1 
ATOM   1592 O OE2 . GLU   A 1 271 ? 111.799 116.973 119.409 1.00 55.13 ? 271 GLU   A OE2 1 
ATOM   1593 N N   . CYS   A 1 272 ? 116.296 117.604 124.542 1.00 39.14 ? 272 CYS   A N   1 
ATOM   1594 C CA  . CYS   A 1 272 ? 117.423 118.308 125.134 1.00 39.41 ? 272 CYS   A CA  1 
ATOM   1595 C C   . CYS   A 1 272 ? 118.270 117.402 126.018 1.00 42.32 ? 272 CYS   A C   1 
ATOM   1596 O O   . CYS   A 1 272 ? 119.375 117.792 126.410 1.00 42.21 ? 272 CYS   A O   1 
ATOM   1597 C CB  . CYS   A 1 272 ? 116.911 119.511 125.933 1.00 45.05 ? 272 CYS   A CB  1 
ATOM   1598 S SG  . CYS   A 1 272 ? 118.178 120.645 126.532 1.00 38.81 ? 272 CYS   A SG  1 
ATOM   1599 N N   . TYR   A 1 273 ? 117.784 116.201 126.329 1.00 25.29 ? 273 TYR   A N   1 
ATOM   1600 C CA  . TYR   A 1 273 ? 118.496 115.248 127.169 1.00 27.03 ? 273 TYR   A CA  1 
ATOM   1601 C C   . TYR   A 1 273 ? 118.916 113.985 126.429 1.00 17.63 ? 273 TYR   A C   1 
ATOM   1602 O O   . TYR   A 1 273 ? 119.460 113.071 127.055 1.00 22.38 ? 273 TYR   A O   1 
ATOM   1603 C CB  . TYR   A 1 273 ? 117.640 114.871 128.379 1.00 24.19 ? 273 TYR   A CB  1 
ATOM   1604 C CG  . TYR   A 1 273 ? 118.116 115.490 129.668 1.00 26.06 ? 273 TYR   A CG  1 
ATOM   1605 C CD1 . TYR   A 1 273 ? 117.788 116.797 130.001 1.00 26.19 ? 273 TYR   A CD1 1 
ATOM   1606 C CD2 . TYR   A 1 273 ? 118.911 114.771 130.545 1.00 19.46 ? 273 TYR   A CD2 1 
ATOM   1607 C CE1 . TYR   A 1 273 ? 118.230 117.364 131.179 1.00 26.55 ? 273 TYR   A CE1 1 
ATOM   1608 C CE2 . TYR   A 1 273 ? 119.354 115.326 131.721 1.00 21.27 ? 273 TYR   A CE2 1 
ATOM   1609 C CZ  . TYR   A 1 273 ? 119.015 116.622 132.035 1.00 17.90 ? 273 TYR   A CZ  1 
ATOM   1610 O OH  . TYR   A 1 273 ? 119.466 117.171 133.213 1.00 18.48 ? 273 TYR   A OH  1 
ATOM   1611 N N   . SER   A 1 274 ? 118.677 113.907 125.122 1.00 38.36 ? 274 SER   A N   1 
ATOM   1612 C CA  . SER   A 1 274 ? 119.086 112.760 124.312 1.00 34.64 ? 274 SER   A CA  1 
ATOM   1613 C C   . SER   A 1 274 ? 120.450 112.985 123.676 1.00 32.72 ? 274 SER   A C   1 
ATOM   1614 O O   . SER   A 1 274 ? 120.749 112.448 122.606 1.00 30.23 ? 274 SER   A O   1 
ATOM   1615 C CB  . SER   A 1 274 ? 118.036 112.462 123.247 1.00 35.04 ? 274 SER   A CB  1 
ATOM   1616 O OG  . SER   A 1 274 ? 117.119 111.480 123.697 1.00 28.91 ? 274 SER   A OG  1 
ATOM   1617 N N   . SER   A 1 275 ? 121.295 113.780 124.325 1.00 26.09 ? 275 SER   A N   1 
ATOM   1618 C CA  . SER   A 1 275 ? 122.590 114.147 123.782 1.00 26.21 ? 275 SER   A CA  1 
ATOM   1619 C C   . SER   A 1 275 ? 123.616 113.039 124.019 1.00 29.05 ? 275 SER   A C   1 
ATOM   1620 O O   . SER   A 1 275 ? 123.371 112.062 124.732 1.00 29.48 ? 275 SER   A O   1 
ATOM   1621 C CB  . SER   A 1 275 ? 123.070 115.457 124.400 1.00 31.43 ? 275 SER   A CB  1 
ATOM   1622 O OG  . SER   A 1 275 ? 122.566 116.572 123.688 1.00 32.25 ? 275 SER   A OG  1 
ATOM   1623 N N   . LYS   A 1 276 ? 124.785 113.208 123.403 1.00 48.07 ? 276 LYS   A N   1 
ATOM   1624 C CA  . LYS   A 1 276 ? 125.868 112.240 123.522 1.00 47.25 ? 276 LYS   A CA  1 
ATOM   1625 C C   . LYS   A 1 276 ? 126.686 112.536 124.772 1.00 45.46 ? 276 LYS   A C   1 
ATOM   1626 O O   . LYS   A 1 276 ? 127.184 113.655 124.942 1.00 51.14 ? 276 LYS   A O   1 
ATOM   1627 C CB  . LYS   A 1 276 ? 126.754 112.281 122.278 1.00 43.01 ? 276 LYS   A CB  1 
ATOM   1628 C CG  . LYS   A 1 276 ? 128.013 111.429 122.377 1.00 50.42 ? 276 LYS   A CG  1 
ATOM   1629 C CD  . LYS   A 1 276 ? 129.254 112.287 122.588 1.00 44.58 ? 276 LYS   A CD  1 
ATOM   1630 C CE  . LYS   A 1 276 ? 129.543 113.158 121.376 1.00 46.95 ? 276 LYS   A CE  1 
ATOM   1631 N NZ  . LYS   A 1 276 ? 130.790 113.954 121.553 1.00 48.29 ? 276 LYS   A NZ  1 
ATOM   1632 N N   . ARG   A 1 277 ? 126.826 111.533 125.641 1.00 37.32 ? 277 ARG   A N   1 
ATOM   1633 C CA  . ARG   A 1 277 ? 127.628 111.638 126.861 1.00 36.63 ? 277 ARG   A CA  1 
ATOM   1634 C C   . ARG   A 1 277 ? 127.180 112.801 127.738 1.00 40.04 ? 277 ARG   A C   1 
ATOM   1635 O O   . ARG   A 1 277 ? 127.994 113.422 128.425 1.00 42.87 ? 277 ARG   A O   1 
ATOM   1636 C CB  . ARG   A 1 277 ? 129.120 111.766 126.541 1.00 41.88 ? 277 ARG   A CB  1 
ATOM   1637 C CG  . ARG   A 1 277 ? 129.910 110.476 126.678 1.00 36.14 ? 277 ARG   A CG  1 
ATOM   1638 C CD  . ARG   A 1 277 ? 131.412 110.738 126.681 1.00 43.96 ? 277 ARG   A CD  1 
ATOM   1639 N NE  . ARG   A 1 277 ? 131.875 111.357 125.444 1.00 39.75 ? 277 ARG   A NE  1 
ATOM   1640 C CZ  . ARG   A 1 277 ? 132.106 112.654 125.295 1.00 44.42 ? 277 ARG   A CZ  1 
ATOM   1641 N NH1 . ARG   A 1 277 ? 131.935 113.506 126.292 1.00 40.49 ? 277 ARG   A NH1 1 
ATOM   1642 N NH2 . ARG   A 1 277 ? 132.518 113.109 124.115 1.00 35.80 ? 277 ARG   A NH2 1 
ATOM   1643 N N   . LEU   A 1 278 ? 125.891 113.116 127.718 1.00 14.98 ? 278 LEU   A N   1 
ATOM   1644 C CA  . LEU   A 1 278 ? 125.359 114.211 128.515 1.00 21.49 ? 278 LEU   A CA  1 
ATOM   1645 C C   . LEU   A 1 278 ? 124.380 113.761 129.584 1.00 20.01 ? 278 LEU   A C   1 
ATOM   1646 O O   . LEU   A 1 278 ? 124.391 114.324 130.679 1.00 21.90 ? 278 LEU   A O   1 
ATOM   1647 C CB  . LEU   A 1 278 ? 124.682 115.251 127.605 1.00 16.24 ? 278 LEU   A CB  1 
ATOM   1648 C CG  . LEU   A 1 278 ? 123.765 116.322 128.200 1.00 18.23 ? 278 LEU   A CG  1 
ATOM   1649 C CD1 . LEU   A 1 278 ? 123.924 117.598 127.406 1.00 19.46 ? 278 LEU   A CD1 1 
ATOM   1650 C CD2 . LEU   A 1 278 ? 122.305 115.888 128.185 1.00 18.89 ? 278 LEU   A CD2 1 
ATOM   1651 N N   . PHE   A 1 279 ? 123.541 112.762 129.301 1.00 16.77 ? 279 PHE   A N   1 
ATOM   1652 C CA  . PHE   A 1 279 ? 122.620 112.261 130.315 1.00 18.72 ? 279 PHE   A CA  1 
ATOM   1653 C C   . PHE   A 1 279 ? 123.364 111.607 131.471 1.00 16.94 ? 279 PHE   A C   1 
ATOM   1654 O O   . PHE   A 1 279 ? 122.911 111.683 132.619 1.00 22.91 ? 279 PHE   A O   1 
ATOM   1655 C CB  . PHE   A 1 279 ? 121.638 111.274 129.684 1.00 24.32 ? 279 PHE   A CB  1 
ATOM   1656 C CG  . PHE   A 1 279 ? 120.676 110.666 130.661 1.00 15.12 ? 279 PHE   A CG  1 
ATOM   1657 C CD1 . PHE   A 1 279 ? 119.786 111.460 131.364 1.00 21.60 ? 279 PHE   A CD1 1 
ATOM   1658 C CD2 . PHE   A 1 279 ? 120.659 109.298 130.876 1.00 17.76 ? 279 PHE   A CD2 1 
ATOM   1659 C CE1 . PHE   A 1 279 ? 118.897 110.902 132.262 1.00 20.71 ? 279 PHE   A CE1 1 
ATOM   1660 C CE2 . PHE   A 1 279 ? 119.773 108.733 131.773 1.00 17.04 ? 279 PHE   A CE2 1 
ATOM   1661 C CZ  . PHE   A 1 279 ? 118.891 109.537 132.467 1.00 20.97 ? 279 PHE   A CZ  1 
ATOM   1662 N N   . TYR   A 1 280 ? 124.500 110.968 131.194 1.00 23.38 ? 280 TYR   A N   1 
ATOM   1663 C CA  . TYR   A 1 280 ? 125.316 110.370 132.242 1.00 22.61 ? 280 TYR   A CA  1 
ATOM   1664 C C   . TYR   A 1 280 ? 126.087 111.411 133.041 1.00 28.78 ? 280 TYR   A C   1 
ATOM   1665 O O   . TYR   A 1 280 ? 126.164 111.305 134.271 1.00 29.09 ? 280 TYR   A O   1 
ATOM   1666 C CB  . TYR   A 1 280 ? 126.285 109.354 131.633 1.00 25.80 ? 280 TYR   A CB  1 
ATOM   1667 C CG  . TYR   A 1 280 ? 125.598 108.106 131.128 1.00 21.81 ? 280 TYR   A CG  1 
ATOM   1668 C CD1 . TYR   A 1 280 ? 124.532 107.549 131.822 1.00 29.06 ? 280 TYR   A CD1 1 
ATOM   1669 C CD2 . TYR   A 1 280 ? 126.004 107.494 129.951 1.00 27.17 ? 280 TYR   A CD2 1 
ATOM   1670 C CE1 . TYR   A 1 280 ? 123.897 106.411 131.364 1.00 27.18 ? 280 TYR   A CE1 1 
ATOM   1671 C CE2 . TYR   A 1 280 ? 125.375 106.355 129.483 1.00 21.78 ? 280 TYR   A CE2 1 
ATOM   1672 C CZ  . TYR   A 1 280 ? 124.322 105.818 130.194 1.00 27.97 ? 280 TYR   A CZ  1 
ATOM   1673 O OH  . TYR   A 1 280 ? 123.693 104.685 129.732 1.00 22.07 ? 280 TYR   A OH  1 
ATOM   1674 N N   . TRP   A 1 281 ? 126.653 112.418 132.371 1.00 10.30 ? 281 TRP   A N   1 
ATOM   1675 C CA  . TRP   A 1 281 ? 127.196 113.566 133.089 1.00 11.09 ? 281 TRP   A CA  1 
ATOM   1676 C C   . TRP   A 1 281 ? 126.100 114.276 133.871 1.00 11.41 ? 281 TRP   A C   1 
ATOM   1677 O O   . TRP   A 1 281 ? 126.329 114.753 134.988 1.00 7.89  ? 281 TRP   A O   1 
ATOM   1678 C CB  . TRP   A 1 281 ? 127.868 114.530 132.112 1.00 11.58 ? 281 TRP   A CB  1 
ATOM   1679 C CG  . TRP   A 1 281 ? 129.312 114.233 131.839 1.00 13.01 ? 281 TRP   A CG  1 
ATOM   1680 C CD1 . TRP   A 1 281 ? 129.870 113.921 130.635 1.00 9.86  ? 281 TRP   A CD1 1 
ATOM   1681 C CD2 . TRP   A 1 281 ? 130.387 114.241 132.786 1.00 4.89  ? 281 TRP   A CD2 1 
ATOM   1682 N NE1 . TRP   A 1 281 ? 131.221 113.724 130.773 1.00 5.27  ? 281 TRP   A NE1 1 
ATOM   1683 C CE2 . TRP   A 1 281 ? 131.564 113.916 132.085 1.00 5.04  ? 281 TRP   A CE2 1 
ATOM   1684 C CE3 . TRP   A 1 281 ? 130.467 114.484 134.160 1.00 5.71  ? 281 TRP   A CE3 1 
ATOM   1685 C CZ2 . TRP   A 1 281 ? 132.804 113.831 132.709 1.00 5.25  ? 281 TRP   A CZ2 1 
ATOM   1686 C CZ3 . TRP   A 1 281 ? 131.700 114.404 134.777 1.00 11.77 ? 281 TRP   A CZ3 1 
ATOM   1687 C CH2 . TRP   A 1 281 ? 132.852 114.078 134.052 1.00 4.38  ? 281 TRP   A CH2 1 
ATOM   1688 N N   . SER   A 1 282 ? 124.899 114.354 133.294 1.00 5.79  ? 282 SER   A N   1 
ATOM   1689 C CA  . SER   A 1 282 ? 123.759 114.915 134.010 1.00 12.16 ? 282 SER   A CA  1 
ATOM   1690 C C   . SER   A 1 282 ? 123.402 114.071 135.226 1.00 13.11 ? 282 SER   A C   1 
ATOM   1691 O O   . SER   A 1 282 ? 123.099 114.609 136.297 1.00 9.43  ? 282 SER   A O   1 
ATOM   1692 C CB  . SER   A 1 282 ? 122.562 115.028 133.069 1.00 13.13 ? 282 SER   A CB  1 
ATOM   1693 O OG  . SER   A 1 282 ? 121.742 116.126 133.410 1.00 3.81  ? 282 SER   A OG  1 
ATOM   1694 N N   . LEU   A 1 283 ? 123.423 112.744 135.076 1.00 14.02 ? 283 LEU   A N   1 
ATOM   1695 C CA  . LEU   A 1 283 ? 123.122 111.867 136.203 1.00 7.65  ? 283 LEU   A CA  1 
ATOM   1696 C C   . LEU   A 1 283 ? 124.149 112.030 137.314 1.00 12.53 ? 283 LEU   A C   1 
ATOM   1697 O O   . LEU   A 1 283 ? 123.798 112.017 138.500 1.00 12.64 ? 283 LEU   A O   1 
ATOM   1698 C CB  . LEU   A 1 283 ? 123.058 110.412 135.738 1.00 13.14 ? 283 LEU   A CB  1 
ATOM   1699 C CG  . LEU   A 1 283 ? 121.723 109.953 135.147 1.00 9.12  ? 283 LEU   A CG  1 
ATOM   1700 C CD1 . LEU   A 1 283 ? 121.682 108.438 135.028 1.00 13.84 ? 283 LEU   A CD1 1 
ATOM   1701 C CD2 . LEU   A 1 283 ? 120.561 110.459 135.988 1.00 7.12  ? 283 LEU   A CD2 1 
ATOM   1702 N N   . TRP   A 1 284 ? 125.426 112.174 136.952 1.00 12.33 ? 284 TRP   A N   1 
ATOM   1703 C CA  . TRP   A 1 284 ? 126.444 112.474 137.953 1.00 9.17  ? 284 TRP   A CA  1 
ATOM   1704 C C   . TRP   A 1 284 ? 126.162 113.810 138.630 1.00 12.84 ? 284 TRP   A C   1 
ATOM   1705 O O   . TRP   A 1 284 ? 126.252 113.932 139.857 1.00 3.31  ? 284 TRP   A O   1 
ATOM   1706 C CB  . TRP   A 1 284 ? 127.831 112.478 137.310 1.00 10.23 ? 284 TRP   A CB  1 
ATOM   1707 C CG  . TRP   A 1 284 ? 128.924 112.802 138.275 1.00 8.64  ? 284 TRP   A CG  1 
ATOM   1708 C CD1 . TRP   A 1 284 ? 129.661 111.918 139.006 1.00 7.91  ? 284 TRP   A CD1 1 
ATOM   1709 C CD2 . TRP   A 1 284 ? 129.398 114.106 138.626 1.00 5.57  ? 284 TRP   A CD2 1 
ATOM   1710 N NE1 . TRP   A 1 284 ? 130.569 112.590 139.786 1.00 6.25  ? 284 TRP   A NE1 1 
ATOM   1711 C CE2 . TRP   A 1 284 ? 130.428 113.935 139.570 1.00 5.48  ? 284 TRP   A CE2 1 
ATOM   1712 C CE3 . TRP   A 1 284 ? 129.054 115.402 138.231 1.00 5.18  ? 284 TRP   A CE3 1 
ATOM   1713 C CZ2 . TRP   A 1 284 ? 131.110 115.010 140.130 1.00 10.98 ? 284 TRP   A CZ2 1 
ATOM   1714 C CZ3 . TRP   A 1 284 ? 129.736 116.466 138.784 1.00 8.01  ? 284 TRP   A CZ3 1 
ATOM   1715 C CH2 . TRP   A 1 284 ? 130.753 116.265 139.722 1.00 3.81  ? 284 TRP   A CH2 1 
ATOM   1716 N N   . TRP   A 1 285 ? 125.815 114.828 137.839 1.00 10.82 ? 285 TRP   A N   1 
ATOM   1717 C CA  . TRP   A 1 285 ? 125.461 116.126 138.406 1.00 8.39  ? 285 TRP   A CA  1 
ATOM   1718 C C   . TRP   A 1 285 ? 124.216 116.016 139.278 1.00 10.44 ? 285 TRP   A C   1 
ATOM   1719 O O   . TRP   A 1 285 ? 124.153 116.605 140.364 1.00 8.20  ? 285 TRP   A O   1 
ATOM   1720 C CB  . TRP   A 1 285 ? 125.262 117.138 137.274 1.00 7.05  ? 285 TRP   A CB  1 
ATOM   1721 C CG  . TRP   A 1 285 ? 125.129 118.580 137.695 1.00 12.91 ? 285 TRP   A CG  1 
ATOM   1722 C CD1 . TRP   A 1 285 ? 124.933 119.061 138.956 1.00 3.33  ? 285 TRP   A CD1 1 
ATOM   1723 C CD2 . TRP   A 1 285 ? 125.216 119.727 136.842 1.00 12.38 ? 285 TRP   A CD2 1 
ATOM   1724 N NE1 . TRP   A 1 285 ? 124.875 120.432 138.940 1.00 12.36 ? 285 TRP   A NE1 1 
ATOM   1725 C CE2 . TRP   A 1 285 ? 125.048 120.866 137.653 1.00 6.96  ? 285 TRP   A CE2 1 
ATOM   1726 C CE3 . TRP   A 1 285 ? 125.413 119.900 135.470 1.00 5.19  ? 285 TRP   A CE3 1 
ATOM   1727 C CZ2 . TRP   A 1 285 ? 125.071 122.158 137.137 1.00 9.24  ? 285 TRP   A CZ2 1 
ATOM   1728 C CZ3 . TRP   A 1 285 ? 125.436 121.181 134.961 1.00 4.83  ? 285 TRP   A CZ3 1 
ATOM   1729 C CH2 . TRP   A 1 285 ? 125.264 122.295 135.792 1.00 11.08 ? 285 TRP   A CH2 1 
ATOM   1730 N N   . ALA   A 1 286 ? 123.220 115.253 138.828 1.00 6.83  ? 286 ALA   A N   1 
ATOM   1731 C CA  . ALA   A 1 286 ? 122.002 115.083 139.610 1.00 7.20  ? 286 ALA   A CA  1 
ATOM   1732 C C   . ALA   A 1 286 ? 122.229 114.285 140.888 1.00 13.45 ? 286 ALA   A C   1 
ATOM   1733 O O   . ALA   A 1 286 ? 121.395 114.351 141.796 1.00 13.32 ? 286 ALA   A O   1 
ATOM   1734 C CB  . ALA   A 1 286 ? 120.925 114.406 138.762 1.00 9.65  ? 286 ALA   A CB  1 
ATOM   1735 N N   . PHE   A 1 287 ? 123.327 113.537 140.986 1.00 10.42 ? 287 PHE   A N   1 
ATOM   1736 C CA  . PHE   A 1 287 ? 123.551 112.664 142.132 1.00 5.32  ? 287 PHE   A CA  1 
ATOM   1737 C C   . PHE   A 1 287 ? 124.788 113.028 142.937 1.00 11.78 ? 287 PHE   A C   1 
ATOM   1738 O O   . PHE   A 1 287 ? 124.706 113.139 144.166 1.00 6.13  ? 287 PHE   A O   1 
ATOM   1739 C CB  . PHE   A 1 287 ? 123.644 111.201 141.670 1.00 4.74  ? 287 PHE   A CB  1 
ATOM   1740 C CG  . PHE   A 1 287 ? 122.309 110.535 141.504 1.00 2.21  ? 287 PHE   A CG  1 
ATOM   1741 C CD1 . PHE   A 1 287 ? 121.574 110.702 140.343 1.00 11.69 ? 287 PHE   A CD1 1 
ATOM   1742 C CD2 . PHE   A 1 287 ? 121.787 109.745 142.514 1.00 6.45  ? 287 PHE   A CD2 1 
ATOM   1743 C CE1 . PHE   A 1 287 ? 120.345 110.090 140.191 1.00 9.14  ? 287 PHE   A CE1 1 
ATOM   1744 C CE2 . PHE   A 1 287 ? 120.559 109.131 142.368 1.00 8.20  ? 287 PHE   A CE2 1 
ATOM   1745 C CZ  . PHE   A 1 287 ? 119.837 109.304 141.205 1.00 9.03  ? 287 PHE   A CZ  1 
ATOM   1746 N N   . ALA   A 1 288 ? 125.939 113.213 142.287 1.00 1.80  ? 288 ALA   A N   1 
ATOM   1747 C CA  . ALA   A 1 288 ? 127.168 113.443 143.039 1.00 10.49 ? 288 ALA   A CA  1 
ATOM   1748 C C   . ALA   A 1 288 ? 127.174 114.803 143.720 1.00 10.56 ? 288 ALA   A C   1 
ATOM   1749 O O   . ALA   A 1 288 ? 127.729 114.941 144.815 1.00 6.81  ? 288 ALA   A O   1 
ATOM   1750 C CB  . ALA   A 1 288 ? 128.383 113.304 142.127 1.00 10.93 ? 288 ALA   A CB  1 
ATOM   1751 N N   . THR   A 1 289 ? 126.570 115.815 143.101 1.00 8.13  ? 289 THR   A N   1 
ATOM   1752 C CA  . THR   A 1 289 ? 126.524 117.128 143.726 1.00 11.34 ? 289 THR   A CA  1 
ATOM   1753 C C   . THR   A 1 289 ? 125.573 117.177 144.913 1.00 9.28  ? 289 THR   A C   1 
ATOM   1754 O O   . THR   A 1 289 ? 125.765 118.008 145.804 1.00 11.60 ? 289 THR   A O   1 
ATOM   1755 C CB  . THR   A 1 289 ? 126.141 118.188 142.695 1.00 8.32  ? 289 THR   A CB  1 
ATOM   1756 O OG1 . THR   A 1 289 ? 124.727 118.164 142.481 1.00 13.51 ? 289 THR   A OG1 1 
ATOM   1757 C CG2 . THR   A 1 289 ? 126.856 117.914 141.386 1.00 6.01  ? 289 THR   A CG2 1 
ATOM   1758 N N   . ALA   A 1 290 ? 124.572 116.296 144.963 1.00 8.10  ? 290 ALA   A N   1 
ATOM   1759 C CA  . ALA   A 1 290 ? 123.762 116.171 146.171 1.00 8.17  ? 290 ALA   A CA  1 
ATOM   1760 C C   . ALA   A 1 290 ? 124.610 115.702 147.346 1.00 9.18  ? 290 ALA   A C   1 
ATOM   1761 O O   . ALA   A 1 290 ? 124.554 116.274 148.443 1.00 11.63 ? 290 ALA   A O   1 
ATOM   1762 C CB  . ALA   A 1 290 ? 122.602 115.207 145.925 1.00 17.23 ? 290 ALA   A CB  1 
ATOM   1763 N N   . GLY   A 1 291 ? 125.411 114.657 147.128 1.00 12.29 ? 291 GLY   A N   1 
ATOM   1764 C CA  . GLY   A 1 291 ? 126.332 114.218 148.162 1.00 17.66 ? 291 GLY   A CA  1 
ATOM   1765 C C   . GLY   A 1 291 ? 127.363 115.276 148.498 1.00 16.46 ? 291 GLY   A C   1 
ATOM   1766 O O   . GLY   A 1 291 ? 127.765 115.419 149.655 1.00 14.72 ? 291 GLY   A O   1 
ATOM   1767 N N   . PHE   A 1 292 ? 127.799 116.039 147.493 1.00 4.67  ? 292 PHE   A N   1 
ATOM   1768 C CA  . PHE   A 1 292 ? 128.740 117.124 147.749 1.00 4.89  ? 292 PHE   A CA  1 
ATOM   1769 C C   . PHE   A 1 292 ? 128.125 118.191 148.641 1.00 3.12  ? 292 PHE   A C   1 
ATOM   1770 O O   . PHE   A 1 292 ? 128.792 118.717 149.535 1.00 9.82  ? 292 PHE   A O   1 
ATOM   1771 C CB  . PHE   A 1 292 ? 129.206 117.752 146.441 1.00 9.22  ? 292 PHE   A CB  1 
ATOM   1772 C CG  . PHE   A 1 292 ? 129.846 119.098 146.620 1.00 7.12  ? 292 PHE   A CG  1 
ATOM   1773 C CD1 . PHE   A 1 292 ? 131.137 119.202 147.108 1.00 9.87  ? 292 PHE   A CD1 1 
ATOM   1774 C CD2 . PHE   A 1 292 ? 129.150 120.260 146.323 1.00 3.79  ? 292 PHE   A CD2 1 
ATOM   1775 C CE1 . PHE   A 1 292 ? 131.732 120.437 147.275 1.00 12.07 ? 292 PHE   A CE1 1 
ATOM   1776 C CE2 . PHE   A 1 292 ? 129.740 121.497 146.489 1.00 11.16 ? 292 PHE   A CE2 1 
ATOM   1777 C CZ  . PHE   A 1 292 ? 131.034 121.585 146.966 1.00 9.28  ? 292 PHE   A CZ  1 
ATOM   1778 N N   . ASN   A 1 293 ? 126.864 118.547 148.396 1.00 5.10  ? 293 ASN   A N   1 
ATOM   1779 C CA  . ASN   A 1 293 ? 126.208 119.550 149.228 1.00 5.48  ? 293 ASN   A CA  1 
ATOM   1780 C C   . ASN   A 1 293 ? 125.965 119.021 150.636 1.00 6.13  ? 293 ASN   A C   1 
ATOM   1781 O O   . ASN   A 1 293 ? 126.065 119.773 151.613 1.00 10.67 ? 293 ASN   A O   1 
ATOM   1782 C CB  . ASN   A 1 293 ? 124.900 119.996 148.579 1.00 9.95  ? 293 ASN   A CB  1 
ATOM   1783 C CG  . ASN   A 1 293 ? 125.122 120.733 147.273 1.00 6.09  ? 293 ASN   A CG  1 
ATOM   1784 O OD1 . ASN   A 1 293 ? 125.961 121.631 147.189 1.00 6.86  ? 293 ASN   A OD1 1 
ATOM   1785 N ND2 . ASN   A 1 293 ? 124.371 120.357 146.245 1.00 10.07 ? 293 ASN   A ND2 1 
ATOM   1786 N N   . GLN   A 1 294 ? 125.653 117.730 150.762 1.00 10.41 ? 294 GLN   A N   1 
ATOM   1787 C CA  . GLN   A 1 294 ? 125.548 117.132 152.091 1.00 7.31  ? 294 GLN   A CA  1 
ATOM   1788 C C   . GLN   A 1 294 ? 126.880 117.204 152.829 1.00 8.40  ? 294 GLN   A C   1 
ATOM   1789 O O   . GLN   A 1 294 ? 126.928 117.535 154.023 1.00 4.43  ? 294 GLN   A O   1 
ATOM   1790 C CB  . GLN   A 1 294 ? 125.075 115.685 151.975 1.00 10.10 ? 294 GLN   A CB  1 
ATOM   1791 C CG  . GLN   A 1 294 ? 123.571 115.539 151.877 1.00 9.28  ? 294 GLN   A CG  1 
ATOM   1792 C CD  . GLN   A 1 294 ? 122.875 115.801 153.193 1.00 6.44  ? 294 GLN   A CD  1 
ATOM   1793 O OE1 . GLN   A 1 294 ? 122.394 116.906 153.445 1.00 9.59  ? 294 GLN   A OE1 1 
ATOM   1794 N NE2 . GLN   A 1 294 ? 122.810 114.782 154.041 1.00 9.41  ? 294 GLN   A NE2 1 
ATOM   1795 N N   . VAL   A 1 295 ? 127.975 116.901 152.128 1.00 8.06  ? 295 VAL   A N   1 
ATOM   1796 C CA  . VAL   A 1 295 ? 129.303 117.018 152.719 1.00 1.28  ? 295 VAL   A CA  1 
ATOM   1797 C C   . VAL   A 1 295 ? 129.589 118.464 153.098 1.00 5.33  ? 295 VAL   A C   1 
ATOM   1798 O O   . VAL   A 1 295 ? 130.150 118.740 154.159 1.00 8.98  ? 295 VAL   A O   1 
ATOM   1799 C CB  . VAL   A 1 295 ? 130.367 116.460 151.756 1.00 7.68  ? 295 VAL   A CB  1 
ATOM   1800 C CG1 . VAL   A 1 295 ? 131.762 116.852 152.217 1.00 4.18  ? 295 VAL   A CG1 1 
ATOM   1801 C CG2 . VAL   A 1 295 ? 130.243 114.951 151.649 1.00 9.75  ? 295 VAL   A CG2 1 
ATOM   1802 N N   . LEU   A 1 296 ? 129.202 119.407 152.240 1.00 4.63  ? 296 LEU   A N   1 
ATOM   1803 C CA  . LEU   A 1 296 ? 129.394 120.820 152.549 1.00 5.46  ? 296 LEU   A CA  1 
ATOM   1804 C C   . LEU   A 1 296 ? 128.668 121.201 153.830 1.00 11.66 ? 296 LEU   A C   1 
ATOM   1805 O O   . LEU   A 1 296 ? 129.206 121.937 154.666 1.00 10.21 ? 296 LEU   A O   1 
ATOM   1806 C CB  . LEU   A 1 296 ? 128.894 121.681 151.389 1.00 11.12 ? 296 LEU   A CB  1 
ATOM   1807 C CG  . LEU   A 1 296 ? 129.849 122.007 150.243 1.00 2.24  ? 296 LEU   A CG  1 
ATOM   1808 C CD1 . LEU   A 1 296 ? 129.435 123.312 149.579 1.00 5.92  ? 296 LEU   A CD1 1 
ATOM   1809 C CD2 . LEU   A 1 296 ? 131.283 122.078 150.728 1.00 4.48  ? 296 LEU   A CD2 1 
ATOM   1810 N N   . ASN   A 1 297 ? 127.440 120.711 153.996 1.00 7.43  ? 297 ASN   A N   1 
ATOM   1811 C CA  . ASN   A 1 297 ? 126.655 121.061 155.173 1.00 11.85 ? 297 ASN   A CA  1 
ATOM   1812 C C   . ASN   A 1 297 ? 127.232 120.443 156.442 1.00 11.71 ? 297 ASN   A C   1 
ATOM   1813 O O   . ASN   A 1 297 ? 127.289 121.104 157.485 1.00 9.08  ? 297 ASN   A O   1 
ATOM   1814 C CB  . ASN   A 1 297 ? 125.202 120.630 154.978 1.00 8.12  ? 297 ASN   A CB  1 
ATOM   1815 C CG  . ASN   A 1 297 ? 124.437 121.565 154.063 1.00 10.31 ? 297 ASN   A CG  1 
ATOM   1816 O OD1 . ASN   A 1 297 ? 124.931 121.962 153.008 1.00 9.80  ? 297 ASN   A OD1 1 
ATOM   1817 N ND2 . ASN   A 1 297 ? 123.222 121.921 154.463 1.00 9.97  ? 297 ASN   A ND2 1 
ATOM   1818 N N   . TYR   A 1 298 ? 127.669 119.183 156.381 1.00 13.09 ? 298 TYR   A N   1 
ATOM   1819 C CA  . TYR   A 1 298 ? 128.019 118.452 157.596 1.00 10.90 ? 298 TYR   A CA  1 
ATOM   1820 C C   . TYR   A 1 298 ? 129.518 118.223 157.774 1.00 14.66 ? 298 TYR   A C   1 
ATOM   1821 O O   . TYR   A 1 298 ? 129.917 117.489 158.686 1.00 9.45  ? 298 TYR   A O   1 
ATOM   1822 C CB  . TYR   A 1 298 ? 127.259 117.125 157.631 1.00 13.50 ? 298 TYR   A CB  1 
ATOM   1823 C CG  . TYR   A 1 298 ? 125.766 117.331 157.543 1.00 16.54 ? 298 TYR   A CG  1 
ATOM   1824 C CD1 . TYR   A 1 298 ? 125.070 117.928 158.586 1.00 14.17 ? 298 TYR   A CD1 1 
ATOM   1825 C CD2 . TYR   A 1 298 ? 125.055 116.957 156.412 1.00 6.97  ? 298 TYR   A CD2 1 
ATOM   1826 C CE1 . TYR   A 1 298 ? 123.708 118.132 158.511 1.00 12.38 ? 298 TYR   A CE1 1 
ATOM   1827 C CE2 . TYR   A 1 298 ? 123.691 117.158 156.328 1.00 8.03  ? 298 TYR   A CE2 1 
ATOM   1828 C CZ  . TYR   A 1 298 ? 123.023 117.746 157.381 1.00 13.21 ? 298 TYR   A CZ  1 
ATOM   1829 O OH  . TYR   A 1 298 ? 121.666 117.952 157.306 1.00 9.37  ? 298 TYR   A OH  1 
ATOM   1830 N N   . VAL   A 1 299 ? 130.361 118.863 156.963 1.00 16.58 ? 299 VAL   A N   1 
ATOM   1831 C CA  . VAL   A 1 299 ? 131.802 118.718 157.136 1.00 13.67 ? 299 VAL   A CA  1 
ATOM   1832 C C   . VAL   A 1 299 ? 132.262 119.420 158.407 1.00 9.76  ? 299 VAL   A C   1 
ATOM   1833 O O   . VAL   A 1 299 ? 133.146 118.927 159.119 1.00 15.14 ? 299 VAL   A O   1 
ATOM   1834 C CB  . VAL   A 1 299 ? 132.539 119.237 155.887 1.00 8.50  ? 299 VAL   A CB  1 
ATOM   1835 C CG1 . VAL   A 1 299 ? 132.187 120.694 155.605 1.00 12.99 ? 299 VAL   A CG1 1 
ATOM   1836 C CG2 . VAL   A 1 299 ? 134.031 119.068 156.046 1.00 8.39  ? 299 VAL   A CG2 1 
ATOM   1837 N N   . GLN   A 1 300 ? 131.675 120.578 158.715 1.00 28.59 ? 300 GLN   A N   1 
ATOM   1838 C CA  . GLN   A 1 300 ? 132.000 121.257 159.964 1.00 25.31 ? 300 GLN   A CA  1 
ATOM   1839 C C   . GLN   A 1 300 ? 131.596 120.409 161.162 1.00 29.28 ? 300 GLN   A C   1 
ATOM   1840 O O   . GLN   A 1 300 ? 132.322 120.343 162.160 1.00 29.94 ? 300 GLN   A O   1 
ATOM   1841 C CB  . GLN   A 1 300 ? 131.317 122.623 160.009 1.00 28.03 ? 300 GLN   A CB  1 
ATOM   1842 C CG  . GLN   A 1 300 ? 131.506 123.446 158.746 1.00 29.36 ? 300 GLN   A CG  1 
ATOM   1843 C CD  . GLN   A 1 300 ? 132.581 124.503 158.891 1.00 30.92 ? 300 GLN   A CD  1 
ATOM   1844 O OE1 . GLN   A 1 300 ? 133.063 124.767 159.993 1.00 30.86 ? 300 GLN   A OE1 1 
ATOM   1845 N NE2 . GLN   A 1 300 ? 132.966 125.113 157.777 1.00 28.98 ? 300 GLN   A NE2 1 
ATOM   1846 N N   . ILE   A 1 301 ? 130.443 119.743 161.076 1.00 13.97 ? 301 ILE   A N   1 
ATOM   1847 C CA  . ILE   A 1 301 ? 130.003 118.877 162.165 1.00 13.54 ? 301 ILE   A CA  1 
ATOM   1848 C C   . ILE   A 1 301 ? 130.939 117.682 162.306 1.00 18.21 ? 301 ILE   A C   1 
ATOM   1849 O O   . ILE   A 1 301 ? 131.260 117.255 163.423 1.00 16.49 ? 301 ILE   A O   1 
ATOM   1850 C CB  . ILE   A 1 301 ? 128.544 118.433 161.948 1.00 11.31 ? 301 ILE   A CB  1 
ATOM   1851 C CG1 . ILE   A 1 301 ? 127.710 119.535 161.285 1.00 15.12 ? 301 ILE   A CG1 1 
ATOM   1852 C CG2 . ILE   A 1 301 ? 127.912 118.053 163.274 1.00 18.55 ? 301 ILE   A CG2 1 
ATOM   1853 C CD1 . ILE   A 1 301 ? 127.721 120.873 162.016 1.00 10.97 ? 301 ILE   A CD1 1 
ATOM   1854 N N   . LEU   A 1 302 ? 131.391 117.122 161.180 1.00 17.08 ? 302 LEU   A N   1 
ATOM   1855 C CA  . LEU   A 1 302 ? 132.354 116.025 161.243 1.00 16.83 ? 302 LEU   A CA  1 
ATOM   1856 C C   . LEU   A 1 302 ? 133.662 116.478 161.878 1.00 13.62 ? 302 LEU   A C   1 
ATOM   1857 O O   . LEU   A 1 302 ? 134.268 115.739 162.661 1.00 9.00  ? 302 LEU   A O   1 
ATOM   1858 C CB  . LEU   A 1 302 ? 132.611 115.456 159.849 1.00 10.10 ? 302 LEU   A CB  1 
ATOM   1859 C CG  . LEU   A 1 302 ? 133.603 114.290 159.830 1.00 17.85 ? 302 LEU   A CG  1 
ATOM   1860 C CD1 . LEU   A 1 302 ? 132.940 113.015 160.326 1.00 9.07  ? 302 LEU   A CD1 1 
ATOM   1861 C CD2 . LEU   A 1 302 ? 134.199 114.086 158.451 1.00 12.35 ? 302 LEU   A CD2 1 
ATOM   1862 N N   . TRP   A 1 303 ? 134.119 117.685 161.541 1.00 18.07 ? 303 TRP   A N   1 
ATOM   1863 C CA  . TRP   A 1 303 ? 135.337 118.212 162.151 1.00 13.85 ? 303 TRP   A CA  1 
ATOM   1864 C C   . TRP   A 1 303 ? 135.162 118.423 163.649 1.00 21.69 ? 303 TRP   A C   1 
ATOM   1865 O O   . TRP   A 1 303 ? 136.074 118.137 164.433 1.00 13.44 ? 303 TRP   A O   1 
ATOM   1866 C CB  . TRP   A 1 303 ? 135.745 119.515 161.467 1.00 17.28 ? 303 TRP   A CB  1 
ATOM   1867 C CG  . TRP   A 1 303 ? 136.282 119.315 160.089 1.00 18.06 ? 303 TRP   A CG  1 
ATOM   1868 C CD1 . TRP   A 1 303 ? 136.835 118.176 159.586 1.00 14.19 ? 303 TRP   A CD1 1 
ATOM   1869 C CD2 . TRP   A 1 303 ? 136.330 120.283 159.037 1.00 16.54 ? 303 TRP   A CD2 1 
ATOM   1870 N NE1 . TRP   A 1 303 ? 137.222 118.372 158.283 1.00 16.79 ? 303 TRP   A NE1 1 
ATOM   1871 C CE2 . TRP   A 1 303 ? 136.922 119.659 157.922 1.00 19.55 ? 303 TRP   A CE2 1 
ATOM   1872 C CE3 . TRP   A 1 303 ? 135.928 121.617 158.927 1.00 18.22 ? 303 TRP   A CE3 1 
ATOM   1873 C CZ2 . TRP   A 1 303 ? 137.126 120.324 156.719 1.00 16.55 ? 303 TRP   A CZ2 1 
ATOM   1874 C CZ3 . TRP   A 1 303 ? 136.127 122.274 157.729 1.00 18.55 ? 303 TRP   A CZ3 1 
ATOM   1875 C CH2 . TRP   A 1 303 ? 136.720 121.627 156.640 1.00 16.41 ? 303 TRP   A CH2 1 
ATOM   1876 N N   . ASP   A 1 304 ? 134.001 118.933 164.066 1.00 21.75 ? 304 ASP   A N   1 
ATOM   1877 C CA  . ASP   A 1 304 ? 133.740 119.095 165.493 1.00 23.08 ? 304 ASP   A CA  1 
ATOM   1878 C C   . ASP   A 1 304 ? 133.734 117.749 166.206 1.00 18.31 ? 304 ASP   A C   1 
ATOM   1879 O O   . ASP   A 1 304 ? 134.238 117.630 167.329 1.00 24.38 ? 304 ASP   A O   1 
ATOM   1880 C CB  . ASP   A 1 304 ? 132.415 119.825 165.714 1.00 22.53 ? 304 ASP   A CB  1 
ATOM   1881 C CG  . ASP   A 1 304 ? 132.352 121.153 164.988 1.00 26.30 ? 304 ASP   A CG  1 
ATOM   1882 O OD1 . ASP   A 1 304 ? 133.421 121.672 164.602 1.00 18.72 ? 304 ASP   A OD1 1 
ATOM   1883 O OD2 . ASP   A 1 304 ? 131.234 121.678 164.801 1.00 21.16 ? 304 ASP   A OD2 1 
ATOM   1884 N N   . TYR   A 1 305 ? 133.157 116.725 165.573 1.00 31.37 ? 305 TYR   A N   1 
ATOM   1885 C CA  . TYR   A 1 305 ? 133.183 115.389 166.161 1.00 28.43 ? 305 TYR   A CA  1 
ATOM   1886 C C   . TYR   A 1 305 ? 134.607 114.854 166.260 1.00 29.67 ? 305 TYR   A C   1 
ATOM   1887 O O   . TYR   A 1 305 ? 134.988 114.267 167.280 1.00 26.55 ? 305 TYR   A O   1 
ATOM   1888 C CB  . TYR   A 1 305 ? 132.310 114.438 165.341 1.00 29.26 ? 305 TYR   A CB  1 
ATOM   1889 C CG  . TYR   A 1 305 ? 132.787 113.002 165.357 1.00 31.87 ? 305 TYR   A CG  1 
ATOM   1890 C CD1 . TYR   A 1 305 ? 132.622 112.206 166.483 1.00 24.41 ? 305 TYR   A CD1 1 
ATOM   1891 C CD2 . TYR   A 1 305 ? 133.407 112.445 164.247 1.00 30.49 ? 305 TYR   A CD2 1 
ATOM   1892 C CE1 . TYR   A 1 305 ? 133.060 110.895 166.502 1.00 32.11 ? 305 TYR   A CE1 1 
ATOM   1893 C CE2 . TYR   A 1 305 ? 133.848 111.135 164.257 1.00 22.56 ? 305 TYR   A CE2 1 
ATOM   1894 C CZ  . TYR   A 1 305 ? 133.672 110.366 165.387 1.00 24.56 ? 305 TYR   A CZ  1 
ATOM   1895 O OH  . TYR   A 1 305 ? 134.109 109.061 165.400 1.00 23.59 ? 305 TYR   A OH  1 
ATOM   1896 N N   . LYS   A 1 306 ? 135.407 115.043 165.208 1.00 26.64 ? 306 LYS   A N   1 
ATOM   1897 C CA  . LYS   A 1 306 ? 136.764 114.507 165.197 1.00 19.78 ? 306 LYS   A CA  1 
ATOM   1898 C C   . LYS   A 1 306 ? 137.659 115.230 166.196 1.00 28.95 ? 306 LYS   A C   1 
ATOM   1899 O O   . LYS   A 1 306 ? 138.365 114.589 166.983 1.00 22.86 ? 306 LYS   A O   1 
ATOM   1900 C CB  . LYS   A 1 306 ? 137.353 114.602 163.790 1.00 28.02 ? 306 LYS   A CB  1 
ATOM   1901 C CG  . LYS   A 1 306 ? 136.735 113.646 162.783 1.00 20.85 ? 306 LYS   A CG  1 
ATOM   1902 C CD  . LYS   A 1 306 ? 137.590 112.403 162.602 1.00 23.38 ? 306 LYS   A CD  1 
ATOM   1903 C CE  . LYS   A 1 306 ? 137.085 111.549 161.451 1.00 27.42 ? 306 LYS   A CE  1 
ATOM   1904 N NZ  . LYS   A 1 306 ? 135.622 111.292 161.540 1.00 24.92 ? 306 LYS   A NZ  1 
ATOM   1905 N N   . ALA   A 1 307 ? 137.645 116.562 166.180 1.00 21.18 ? 307 ALA   A N   1 
ATOM   1906 C CA  . ALA   A 1 307 ? 138.494 117.376 167.048 1.00 21.68 ? 307 ALA   A CA  1 
ATOM   1907 C C   . ALA   A 1 307 ? 137.633 118.411 167.758 1.00 22.30 ? 307 ALA   A C   1 
ATOM   1908 O O   . ALA   A 1 307 ? 137.478 119.542 167.277 1.00 20.96 ? 307 ALA   A O   1 
ATOM   1909 C CB  . ALA   A 1 307 ? 139.615 118.044 166.257 1.00 18.49 ? 307 ALA   A CB  1 
ATOM   1910 N N   . PRO   A 1 308 ? 137.055 118.061 168.907 1.00 23.65 ? 308 PRO   A N   1 
ATOM   1911 C CA  . PRO   A 1 308 ? 136.267 119.044 169.662 1.00 24.03 ? 308 PRO   A CA  1 
ATOM   1912 C C   . PRO   A 1 308 ? 137.146 120.106 170.304 1.00 23.04 ? 308 PRO   A C   1 
ATOM   1913 O O   . PRO   A 1 308 ? 137.313 120.132 171.527 1.00 28.10 ? 308 PRO   A O   1 
ATOM   1914 C CB  . PRO   A 1 308 ? 135.555 118.186 170.715 1.00 30.99 ? 308 PRO   A CB  1 
ATOM   1915 C CG  . PRO   A 1 308 ? 136.449 117.006 170.897 1.00 26.11 ? 308 PRO   A CG  1 
ATOM   1916 C CD  . PRO   A 1 308 ? 137.062 116.736 169.551 1.00 23.27 ? 308 PRO   A CD  1 
ATOM   1917 N N   . SER   A 1 309 ? 137.711 120.986 169.483 1.00 43.34 ? 309 SER   A N   1 
ATOM   1918 C CA  . SER   A 1 309 ? 138.602 122.038 169.947 1.00 45.10 ? 309 SER   A CA  1 
ATOM   1919 C C   . SER   A 1 309 ? 137.886 123.382 169.919 1.00 43.34 ? 309 SER   A C   1 
ATOM   1920 O O   . SER   A 1 309 ? 137.138 123.679 168.983 1.00 47.19 ? 309 SER   A O   1 
ATOM   1921 C CB  . SER   A 1 309 ? 139.866 122.101 169.087 1.00 48.50 ? 309 SER   A CB  1 
ATOM   1922 O OG  . SER   A 1 309 ? 140.519 123.351 169.230 1.00 47.78 ? 309 SER   A OG  1 
ATOM   1923 N N   . GLN   A 1 310 ? 138.115 124.187 170.959 1.00 64.57 ? 310 GLN   A N   1 
ATOM   1924 C CA  . GLN   A 1 310 ? 137.479 125.498 171.036 1.00 62.23 ? 310 GLN   A CA  1 
ATOM   1925 C C   . GLN   A 1 310 ? 137.930 126.402 169.895 1.00 64.35 ? 310 GLN   A C   1 
ATOM   1926 O O   . GLN   A 1 310 ? 137.113 127.108 169.292 1.00 57.66 ? 310 GLN   A O   1 
ATOM   1927 C CB  . GLN   A 1 310 ? 137.779 126.148 172.387 1.00 67.35 ? 310 GLN   A CB  1 
ATOM   1928 C CG  . GLN   A 1 310 ? 139.222 125.994 172.844 1.00 59.25 ? 310 GLN   A CG  1 
ATOM   1929 C CD  . GLN   A 1 310 ? 139.409 126.325 174.312 1.00 66.59 ? 310 GLN   A CD  1 
ATOM   1930 O OE1 . GLN   A 1 310 ? 138.484 126.791 174.978 1.00 65.60 ? 310 GLN   A OE1 1 
ATOM   1931 N NE2 . GLN   A 1 310 ? 140.610 126.084 174.824 1.00 65.53 ? 310 GLN   A NE2 1 
ATOM   1932 N N   . ASP   A 1 311 ? 139.227 126.395 169.583 1.00 74.32 ? 311 ASP   A N   1 
ATOM   1933 C CA  . ASP   A 1 311 ? 139.751 127.246 168.523 1.00 73.82 ? 311 ASP   A CA  1 
ATOM   1934 C C   . ASP   A 1 311 ? 139.500 126.683 167.131 1.00 75.91 ? 311 ASP   A C   1 
ATOM   1935 O O   . ASP   A 1 311 ? 139.562 127.441 166.156 1.00 80.12 ? 311 ASP   A O   1 
ATOM   1936 C CB  . ASP   A 1 311 ? 141.252 127.470 168.720 1.00 76.13 ? 311 ASP   A CB  1 
ATOM   1937 C CG  . ASP   A 1 311 ? 141.741 128.749 168.071 1.00 80.98 ? 311 ASP   A CG  1 
ATOM   1938 O OD1 . ASP   A 1 311 ? 141.098 129.802 168.267 1.00 75.15 ? 311 ASP   A OD1 1 
ATOM   1939 O OD2 . ASP   A 1 311 ? 142.769 128.703 167.363 1.00 77.82 ? 311 ASP   A OD2 1 
ATOM   1940 N N   . SER   A 1 312 ? 139.184 125.388 167.020 1.00 47.93 ? 312 SER   A N   1 
ATOM   1941 C CA  . SER   A 1 312 ? 139.057 124.737 165.718 1.00 44.55 ? 312 SER   A CA  1 
ATOM   1942 C C   . SER   A 1 312 ? 138.184 125.519 164.745 1.00 38.57 ? 312 SER   A C   1 
ATOM   1943 O O   . SER   A 1 312 ? 138.355 125.380 163.527 1.00 42.76 ? 312 SER   A O   1 
ATOM   1944 C CB  . SER   A 1 312 ? 138.492 123.325 165.893 1.00 41.47 ? 312 SER   A CB  1 
ATOM   1945 O OG  . SER   A 1 312 ? 137.153 123.367 166.356 1.00 43.44 ? 312 SER   A OG  1 
ATOM   1946 N N   . SER   A 1 313 ? 137.275 126.354 165.256 1.00 49.74 ? 313 SER   A N   1 
ATOM   1947 C CA  . SER   A 1 313 ? 136.409 127.148 164.392 1.00 48.12 ? 313 SER   A CA  1 
ATOM   1948 C C   . SER   A 1 313 ? 137.219 127.954 163.384 1.00 53.58 ? 313 SER   A C   1 
ATOM   1949 O O   . SER   A 1 313 ? 136.983 127.864 162.173 1.00 53.71 ? 313 SER   A O   1 
ATOM   1950 C CB  . SER   A 1 313 ? 135.531 128.071 165.239 1.00 55.57 ? 313 SER   A CB  1 
ATOM   1951 O OG  . SER   A 1 313 ? 136.316 129.026 165.933 1.00 48.22 ? 313 SER   A OG  1 
ATOM   1952 N N   . ILE   A 1 314 ? 138.209 128.720 163.860 1.00 38.15 ? 314 ILE   A N   1 
ATOM   1953 C CA  . ILE   A 1 314 ? 138.995 129.524 162.925 1.00 38.43 ? 314 ILE   A CA  1 
ATOM   1954 C C   . ILE   A 1 314 ? 139.729 128.614 161.954 1.00 36.63 ? 314 ILE   A C   1 
ATOM   1955 O O   . ILE   A 1 314 ? 139.911 128.959 160.780 1.00 32.21 ? 314 ILE   A O   1 
ATOM   1956 C CB  . ILE   A 1 314 ? 139.963 130.476 163.664 1.00 32.78 ? 314 ILE   A CB  1 
ATOM   1957 C CG1 . ILE   A 1 314 ? 140.946 131.118 162.682 1.00 34.35 ? 314 ILE   A CG1 1 
ATOM   1958 C CG2 . ILE   A 1 314 ? 140.756 129.747 164.718 1.00 35.58 ? 314 ILE   A CG2 1 
ATOM   1959 C CD1 . ILE   A 1 314 ? 141.993 131.989 163.343 1.00 34.94 ? 314 ILE   A CD1 1 
ATOM   1960 N N   . TYR   A 1 315 ? 140.139 127.430 162.413 1.00 51.93 ? 315 TYR   A N   1 
ATOM   1961 C CA  . TYR   A 1 315 ? 140.697 126.443 161.497 1.00 55.65 ? 315 TYR   A CA  1 
ATOM   1962 C C   . TYR   A 1 315 ? 139.646 125.974 160.499 1.00 55.96 ? 315 TYR   A C   1 
ATOM   1963 O O   . TYR   A 1 315 ? 139.877 125.993 159.283 1.00 55.42 ? 315 TYR   A O   1 
ATOM   1964 C CB  . TYR   A 1 315 ? 141.256 125.255 162.280 1.00 56.03 ? 315 TYR   A CB  1 
ATOM   1965 C CG  . TYR   A 1 315 ? 142.710 125.392 162.667 1.00 52.96 ? 315 TYR   A CG  1 
ATOM   1966 C CD1 . TYR   A 1 315 ? 143.689 125.596 161.703 1.00 56.89 ? 315 TYR   A CD1 1 
ATOM   1967 C CD2 . TYR   A 1 315 ? 143.106 125.311 163.995 1.00 53.32 ? 315 TYR   A CD2 1 
ATOM   1968 C CE1 . TYR   A 1 315 ? 145.021 125.719 162.053 1.00 53.29 ? 315 TYR   A CE1 1 
ATOM   1969 C CE2 . TYR   A 1 315 ? 144.434 125.433 164.355 1.00 50.45 ? 315 TYR   A CE2 1 
ATOM   1970 C CZ  . TYR   A 1 315 ? 145.387 125.637 163.380 1.00 54.07 ? 315 TYR   A CZ  1 
ATOM   1971 O OH  . TYR   A 1 315 ? 146.712 125.758 163.733 1.00 47.77 ? 315 TYR   A OH  1 
ATOM   1972 N N   . ASN   A 1 316 ? 138.461 125.605 160.999 1.00 31.40 ? 316 ASN   A N   1 
ATOM   1973 C CA  . ASN   A 1 316 ? 137.502 124.847 160.199 1.00 31.36 ? 316 ASN   A CA  1 
ATOM   1974 C C   . ASN   A 1 316 ? 137.177 125.567 158.898 1.00 36.60 ? 316 ASN   A C   1 
ATOM   1975 O O   . ASN   A 1 316 ? 137.529 125.100 157.808 1.00 31.81 ? 316 ASN   A O   1 
ATOM   1976 C CB  . ASN   A 1 316 ? 136.230 124.600 161.013 1.00 33.46 ? 316 ASN   A CB  1 
ATOM   1977 C CG  . ASN   A 1 316 ? 136.267 123.288 161.770 1.00 30.50 ? 316 ASN   A CG  1 
ATOM   1978 O OD1 . ASN   A 1 316 ? 137.254 122.554 161.716 1.00 32.39 ? 316 ASN   A OD1 1 
ATOM   1979 N ND2 . ASN   A 1 316 ? 135.188 122.985 162.482 1.00 39.70 ? 316 ASN   A ND2 1 
ATOM   1980 N N   . GLY   A 1 317 ? 136.554 126.742 159.002 1.00 30.06 ? 317 GLY   A N   1 
ATOM   1981 C CA  . GLY   A 1 317 ? 136.237 127.503 157.807 1.00 26.47 ? 317 GLY   A CA  1 
ATOM   1982 C C   . GLY   A 1 317 ? 137.463 127.783 156.966 1.00 30.19 ? 317 GLY   A C   1 
ATOM   1983 O O   . GLY   A 1 317 ? 137.416 127.700 155.735 1.00 34.40 ? 317 GLY   A O   1 
ATOM   1984 N N   . ALA   A 1 318 ? 138.592 128.073 157.623 1.00 29.50 ? 318 ALA   A N   1 
ATOM   1985 C CA  . ALA   A 1 318 ? 139.823 128.328 156.884 1.00 24.76 ? 318 ALA   A CA  1 
ATOM   1986 C C   . ALA   A 1 318 ? 140.164 127.153 155.984 1.00 23.68 ? 318 ALA   A C   1 
ATOM   1987 O O   . ALA   A 1 318 ? 140.477 127.340 154.801 1.00 28.46 ? 318 ALA   A O   1 
ATOM   1988 C CB  . ALA   A 1 318 ? 140.973 128.618 157.847 1.00 23.25 ? 318 ALA   A CB  1 
ATOM   1989 N N   . VAL   A 1 319 ? 140.060 125.929 156.509 1.00 19.81 ? 319 VAL   A N   1 
ATOM   1990 C CA  . VAL   A 1 319 ? 140.341 124.756 155.688 1.00 18.11 ? 319 VAL   A CA  1 
ATOM   1991 C C   . VAL   A 1 319 ? 139.403 124.723 154.493 1.00 25.91 ? 319 VAL   A C   1 
ATOM   1992 O O   . VAL   A 1 319 ? 139.828 124.477 153.355 1.00 21.75 ? 319 VAL   A O   1 
ATOM   1993 C CB  . VAL   A 1 319 ? 140.240 123.470 156.523 1.00 22.89 ? 319 VAL   A CB  1 
ATOM   1994 C CG1 . VAL   A 1 319 ? 140.263 122.257 155.607 1.00 24.64 ? 319 VAL   A CG1 1 
ATOM   1995 C CG2 . VAL   A 1 319 ? 141.378 123.412 157.527 1.00 25.24 ? 319 VAL   A CG2 1 
ATOM   1996 N N   . GLU   A 1 320 ? 138.119 125.014 154.728 1.00 27.33 ? 320 GLU   A N   1 
ATOM   1997 C CA  . GLU   A 1 320 ? 137.174 125.123 153.624 1.00 24.70 ? 320 GLU   A CA  1 
ATOM   1998 C C   . GLU   A 1 320 ? 137.724 126.056 152.559 1.00 31.14 ? 320 GLU   A C   1 
ATOM   1999 O O   . GLU   A 1 320 ? 137.798 125.695 151.377 1.00 23.17 ? 320 GLU   A O   1 
ATOM   2000 C CB  . GLU   A 1 320 ? 135.821 125.624 154.133 1.00 32.32 ? 320 GLU   A CB  1 
ATOM   2001 C CG  . GLU   A 1 320 ? 135.063 124.629 154.994 1.00 28.63 ? 320 GLU   A CG  1 
ATOM   2002 C CD  . GLU   A 1 320 ? 133.711 124.271 154.410 1.00 31.61 ? 320 GLU   A CD  1 
ATOM   2003 O OE1 . GLU   A 1 320 ? 133.555 124.358 153.174 1.00 28.94 ? 320 GLU   A OE1 1 
ATOM   2004 O OE2 . GLU   A 1 320 ? 132.804 123.905 155.186 1.00 25.37 ? 320 GLU   A OE2 1 
ATOM   2005 N N   . ALA   A 1 321 ? 138.177 127.240 152.982 1.00 11.52 ? 321 ALA   A N   1 
ATOM   2006 C CA  . ALA   A 1 321 ? 138.852 128.166 152.082 1.00 13.89 ? 321 ALA   A CA  1 
ATOM   2007 C C   . ALA   A 1 321 ? 139.884 127.437 151.235 1.00 18.18 ? 321 ALA   A C   1 
ATOM   2008 O O   . ALA   A 1 321 ? 139.760 127.366 150.006 1.00 10.41 ? 321 ALA   A O   1 
ATOM   2009 C CB  . ALA   A 1 321 ? 139.508 129.289 152.887 1.00 13.66 ? 321 ALA   A CB  1 
ATOM   2010 N N   . ILE   A 1 322 ? 140.877 126.825 151.891 1.00 11.75 ? 322 ILE   A N   1 
ATOM   2011 C CA  . ILE   A 1 322 ? 141.910 126.104 151.155 1.00 16.01 ? 322 ILE   A CA  1 
ATOM   2012 C C   . ILE   A 1 322 ? 141.271 125.062 150.252 1.00 16.35 ? 322 ILE   A C   1 
ATOM   2013 O O   . ILE   A 1 322 ? 141.549 125.008 149.047 1.00 12.56 ? 322 ILE   A O   1 
ATOM   2014 C CB  . ILE   A 1 322 ? 142.929 125.469 152.121 1.00 10.36 ? 322 ILE   A CB  1 
ATOM   2015 C CG1 . ILE   A 1 322 ? 143.918 126.517 152.640 1.00 8.99  ? 322 ILE   A CG1 1 
ATOM   2016 C CG2 . ILE   A 1 322 ? 143.675 124.332 151.438 1.00 10.30 ? 322 ILE   A CG2 1 
ATOM   2017 C CD1 . ILE   A 1 322 ? 143.461 127.259 153.870 1.00 11.04 ? 322 ILE   A CD1 1 
ATOM   2018 N N   . ALA   A 1 323 ? 140.350 124.269 150.806 1.00 1.02  ? 323 ALA   A N   1 
ATOM   2019 C CA  . ALA   A 1 323 ? 139.657 123.281 149.991 1.00 3.76  ? 323 ALA   A CA  1 
ATOM   2020 C C   . ALA   A 1 323 ? 138.979 123.956 148.811 1.00 1.25  ? 323 ALA   A C   1 
ATOM   2021 O O   . ALA   A 1 323 ? 139.208 123.586 147.652 1.00 4.61  ? 323 ALA   A O   1 
ATOM   2022 C CB  . ALA   A 1 323 ? 138.643 122.514 150.837 1.00 1.86  ? 323 ALA   A CB  1 
ATOM   2023 N N   . THR   A 1 324 ? 138.203 125.008 149.086 1.00 10.60 ? 324 THR   A N   1 
ATOM   2024 C CA  . THR   A 1 324 ? 137.585 125.755 148.001 1.00 13.00 ? 324 THR   A CA  1 
ATOM   2025 C C   . THR   A 1 324 ? 138.648 126.300 147.063 1.00 7.34  ? 324 THR   A C   1 
ATOM   2026 O O   . THR   A 1 324 ? 138.541 126.155 145.839 1.00 8.49  ? 324 THR   A O   1 
ATOM   2027 C CB  . THR   A 1 324 ? 136.722 126.885 148.559 1.00 9.97  ? 324 THR   A CB  1 
ATOM   2028 O OG1 . THR   A 1 324 ? 135.814 126.356 149.534 1.00 8.30  ? 324 THR   A OG1 1 
ATOM   2029 C CG2 . THR   A 1 324 ? 135.925 127.536 147.448 1.00 6.17  ? 324 THR   A CG2 1 
ATOM   2030 N N   . PHE   A 1 325 ? 139.721 126.866 147.626 1.00 9.02  ? 325 PHE   A N   1 
ATOM   2031 C CA  . PHE   A 1 325 ? 140.818 127.339 146.793 1.00 10.81 ? 325 PHE   A CA  1 
ATOM   2032 C C   . PHE   A 1 325 ? 141.373 126.199 145.957 1.00 15.65 ? 325 PHE   A C   1 
ATOM   2033 O O   . PHE   A 1 325 ? 141.579 126.345 144.746 1.00 14.37 ? 325 PHE   A O   1 
ATOM   2034 C CB  . PHE   A 1 325 ? 141.915 127.960 147.655 1.00 15.98 ? 325 PHE   A CB  1 
ATOM   2035 C CG  . PHE   A 1 325 ? 143.200 128.197 146.915 1.00 13.13 ? 325 PHE   A CG  1 
ATOM   2036 C CD1 . PHE   A 1 325 ? 143.223 128.982 145.774 1.00 10.28 ? 325 PHE   A CD1 1 
ATOM   2037 C CD2 . PHE   A 1 325 ? 144.383 127.628 147.355 1.00 14.24 ? 325 PHE   A CD2 1 
ATOM   2038 C CE1 . PHE   A 1 325 ? 144.402 129.199 145.089 1.00 11.00 ? 325 PHE   A CE1 1 
ATOM   2039 C CE2 . PHE   A 1 325 ? 145.566 127.842 146.674 1.00 8.26  ? 325 PHE   A CE2 1 
ATOM   2040 C CZ  . PHE   A 1 325 ? 145.575 128.629 145.539 1.00 17.00 ? 325 PHE   A CZ  1 
ATOM   2041 N N   . GLY   A 1 326 ? 141.573 125.034 146.581 1.00 7.15  ? 326 GLY   A N   1 
ATOM   2042 C CA  . GLY   A 1 326 ? 141.982 123.875 145.811 1.00 7.21  ? 326 GLY   A CA  1 
ATOM   2043 C C   . GLY   A 1 326 ? 141.003 123.592 144.693 1.00 10.36 ? 326 GLY   A C   1 
ATOM   2044 O O   . GLY   A 1 326 ? 141.385 123.500 143.522 1.00 12.43 ? 326 GLY   A O   1 
ATOM   2045 N N   . GLY   A 1 327 ? 139.711 123.553 145.029 1.00 6.19  ? 327 GLY   A N   1 
ATOM   2046 C CA  . GLY   A 1 327 ? 138.707 123.397 143.996 1.00 7.20  ? 327 GLY   A CA  1 
ATOM   2047 C C   . GLY   A 1 327 ? 138.840 124.464 142.933 1.00 8.69  ? 327 GLY   A C   1 
ATOM   2048 O O   . GLY   A 1 327 ? 138.812 124.166 141.735 1.00 7.95  ? 327 GLY   A O   1 
ATOM   2049 N N   . ALA   A 1 328 ? 139.048 125.712 143.361 1.00 7.56  ? 328 ALA   A N   1 
ATOM   2050 C CA  . ALA   A 1 328 ? 139.313 126.795 142.424 1.00 10.85 ? 328 ALA   A CA  1 
ATOM   2051 C C   . ALA   A 1 328 ? 140.387 126.385 141.429 1.00 11.15 ? 328 ALA   A C   1 
ATOM   2052 O O   . ALA   A 1 328 ? 140.136 126.310 140.220 1.00 8.57  ? 328 ALA   A O   1 
ATOM   2053 C CB  . ALA   A 1 328 ? 139.725 128.057 143.183 1.00 5.01  ? 328 ALA   A CB  1 
ATOM   2054 N N   . VAL   A 1 329 ? 141.576 126.040 141.933 1.00 5.32  ? 329 VAL   A N   1 
ATOM   2055 C CA  . VAL   A 1 329 ? 142.659 125.699 141.017 1.00 10.89 ? 329 VAL   A CA  1 
ATOM   2056 C C   . VAL   A 1 329 ? 142.284 124.456 140.224 1.00 5.83  ? 329 VAL   A C   1 
ATOM   2057 O O   . VAL   A 1 329 ? 142.555 124.369 139.019 1.00 8.85  ? 329 VAL   A O   1 
ATOM   2058 C CB  . VAL   A 1 329 ? 143.998 125.547 141.770 1.00 10.95 ? 329 VAL   A CB  1 
ATOM   2059 C CG1 . VAL   A 1 329 ? 144.163 124.167 142.389 1.00 5.74  ? 329 VAL   A CG1 1 
ATOM   2060 C CG2 . VAL   A 1 329 ? 145.163 125.858 140.841 1.00 5.20  ? 329 VAL   A CG2 1 
ATOM   2061 N N   . ALA   A 1 330 ? 141.580 123.515 140.862 1.00 5.15  ? 330 ALA   A N   1 
ATOM   2062 C CA  . ALA   A 1 330 ? 141.111 122.340 140.141 1.00 6.23  ? 330 ALA   A CA  1 
ATOM   2063 C C   . ALA   A 1 330 ? 140.189 122.754 139.007 1.00 13.27 ? 330 ALA   A C   1 
ATOM   2064 O O   . ALA   A 1 330 ? 140.363 122.326 137.859 1.00 5.80  ? 330 ALA   A O   1 
ATOM   2065 C CB  . ALA   A 1 330 ? 140.407 121.381 141.097 1.00 6.99  ? 330 ALA   A CB  1 
ATOM   2066 N N   . ALA   A 1 331 ? 139.231 123.637 139.300 1.00 5.89  ? 331 ALA   A N   1 
ATOM   2067 C CA  . ALA   A 1 331 ? 138.428 124.211 138.231 1.00 12.33 ? 331 ALA   A CA  1 
ATOM   2068 C C   . ALA   A 1 331 ? 139.317 124.979 137.267 1.00 7.88  ? 331 ALA   A C   1 
ATOM   2069 O O   . ALA   A 1 331 ? 139.221 124.812 136.045 1.00 9.70  ? 331 ALA   A O   1 
ATOM   2070 C CB  . ALA   A 1 331 ? 137.341 125.113 138.813 1.00 6.96  ? 331 ALA   A CB  1 
ATOM   2071 N N   . PHE   A 1 332 ? 140.240 125.780 137.807 1.00 14.15 ? 332 PHE   A N   1 
ATOM   2072 C CA  . PHE   A 1 332 ? 141.178 126.490 136.951 1.00 14.62 ? 332 PHE   A CA  1 
ATOM   2073 C C   . PHE   A 1 332 ? 142.058 125.524 136.178 1.00 15.11 ? 332 PHE   A C   1 
ATOM   2074 O O   . PHE   A 1 332 ? 142.598 125.896 135.132 1.00 14.61 ? 332 PHE   A O   1 
ATOM   2075 C CB  . PHE   A 1 332 ? 142.038 127.447 137.776 1.00 11.41 ? 332 PHE   A CB  1 
ATOM   2076 C CG  . PHE   A 1 332 ? 142.927 128.327 136.945 1.00 18.10 ? 332 PHE   A CG  1 
ATOM   2077 C CD1 . PHE   A 1 332 ? 142.389 129.341 136.170 1.00 11.75 ? 332 PHE   A CD1 1 
ATOM   2078 C CD2 . PHE   A 1 332 ? 144.299 128.138 136.934 1.00 14.62 ? 332 PHE   A CD2 1 
ATOM   2079 C CE1 . PHE   A 1 332 ? 143.202 130.152 135.403 1.00 13.10 ? 332 PHE   A CE1 1 
ATOM   2080 C CE2 . PHE   A 1 332 ? 145.118 128.946 136.168 1.00 13.39 ? 332 PHE   A CE2 1 
ATOM   2081 C CZ  . PHE   A 1 332 ? 144.568 129.955 135.402 1.00 17.10 ? 332 PHE   A CZ  1 
ATOM   2082 N N   . ALA   A 1 333 ? 142.211 124.291 136.667 1.00 14.86 ? 333 ALA   A N   1 
ATOM   2083 C CA  . ALA   A 1 333 ? 142.894 123.278 135.874 1.00 11.59 ? 333 ALA   A CA  1 
ATOM   2084 C C   . ALA   A 1 333 ? 142.084 122.928 134.635 1.00 14.38 ? 333 ALA   A C   1 
ATOM   2085 O O   . ALA   A 1 333 ? 142.608 122.961 133.515 1.00 13.08 ? 333 ALA   A O   1 
ATOM   2086 C CB  . ALA   A 1 333 ? 143.154 122.032 136.720 1.00 16.73 ? 333 ALA   A CB  1 
ATOM   2087 N N   . VAL   A 1 334 ? 140.789 122.648 134.811 1.00 9.43  ? 334 VAL   A N   1 
ATOM   2088 C CA  . VAL   A 1 334 ? 139.971 122.147 133.709 1.00 15.62 ? 334 VAL   A CA  1 
ATOM   2089 C C   . VAL   A 1 334 ? 139.932 123.158 132.571 1.00 12.43 ? 334 VAL   A C   1 
ATOM   2090 O O   . VAL   A 1 334 ? 140.050 122.801 131.393 1.00 12.17 ? 334 VAL   A O   1 
ATOM   2091 C CB  . VAL   A 1 334 ? 138.556 121.802 134.206 1.00 9.70  ? 334 VAL   A CB  1 
ATOM   2092 C CG1 . VAL   A 1 334 ? 137.652 121.444 133.036 1.00 9.03  ? 334 VAL   A CG1 1 
ATOM   2093 C CG2 . VAL   A 1 334 ? 138.612 120.664 135.207 1.00 11.88 ? 334 VAL   A CG2 1 
ATOM   2094 N N   . GLY   A 1 335 ? 139.767 124.437 132.907 1.00 18.65 ? 335 GLY   A N   1 
ATOM   2095 C CA  . GLY   A 1 335 ? 139.792 125.464 131.882 1.00 10.16 ? 335 GLY   A CA  1 
ATOM   2096 C C   . GLY   A 1 335 ? 141.154 125.619 131.233 1.00 11.67 ? 335 GLY   A C   1 
ATOM   2097 O O   . GLY   A 1 335 ? 141.250 125.885 130.032 1.00 16.84 ? 335 GLY   A O   1 
ATOM   2098 N N   . TYR   A 1 336 ? 142.226 125.446 132.009 1.00 45.13 ? 336 TYR   A N   1 
ATOM   2099 C CA  . TYR   A 1 336 ? 143.550 125.808 131.511 1.00 41.27 ? 336 TYR   A CA  1 
ATOM   2100 C C   . TYR   A 1 336 ? 144.157 124.695 130.665 1.00 41.63 ? 336 TYR   A C   1 
ATOM   2101 O O   . TYR   A 1 336 ? 144.767 124.962 129.623 1.00 42.68 ? 336 TYR   A O   1 
ATOM   2102 C CB  . TYR   A 1 336 ? 144.475 126.163 132.674 1.00 44.51 ? 336 TYR   A CB  1 
ATOM   2103 C CG  . TYR   A 1 336 ? 145.749 126.851 132.244 1.00 45.67 ? 336 TYR   A CG  1 
ATOM   2104 C CD1 . TYR   A 1 336 ? 145.760 128.208 131.946 1.00 47.05 ? 336 TYR   A CD1 1 
ATOM   2105 C CD2 . TYR   A 1 336 ? 146.940 126.147 132.132 1.00 45.29 ? 336 TYR   A CD2 1 
ATOM   2106 C CE1 . TYR   A 1 336 ? 146.920 128.844 131.551 1.00 40.85 ? 336 TYR   A CE1 1 
ATOM   2107 C CE2 . TYR   A 1 336 ? 148.107 126.774 131.738 1.00 47.74 ? 336 TYR   A CE2 1 
ATOM   2108 C CZ  . TYR   A 1 336 ? 148.091 128.123 131.449 1.00 46.29 ? 336 TYR   A CZ  1 
ATOM   2109 O OH  . TYR   A 1 336 ? 149.249 128.753 131.056 1.00 41.56 ? 336 TYR   A OH  1 
ATOM   2110 N N   . VAL   A 1 337 ? 144.012 123.441 131.098 1.00 18.67 ? 337 VAL   A N   1 
ATOM   2111 C CA  . VAL   A 1 337 ? 144.665 122.341 130.400 1.00 24.43 ? 337 VAL   A CA  1 
ATOM   2112 C C   . VAL   A 1 337 ? 144.047 122.168 129.019 1.00 16.88 ? 337 VAL   A C   1 
ATOM   2113 O O   . VAL   A 1 337 ? 142.818 122.153 128.859 1.00 21.96 ? 337 VAL   A O   1 
ATOM   2114 C CB  . VAL   A 1 337 ? 144.587 121.040 131.219 1.00 18.40 ? 337 VAL   A CB  1 
ATOM   2115 C CG1 . VAL   A 1 337 ? 145.406 121.167 132.496 1.00 23.89 ? 337 VAL   A CG1 1 
ATOM   2116 C CG2 . VAL   A 1 337 ? 143.144 120.666 131.530 1.00 19.27 ? 337 VAL   A CG2 1 
ATOM   2117 N N   . LYS   A 1 338 ? 144.905 122.062 128.005 1.00 33.56 ? 338 LYS   A N   1 
ATOM   2118 C CA  . LYS   A 1 338 ? 144.455 121.856 126.629 1.00 28.15 ? 338 LYS   A CA  1 
ATOM   2119 C C   . LYS   A 1 338 ? 144.404 120.357 126.335 1.00 31.04 ? 338 LYS   A C   1 
ATOM   2120 O O   . LYS   A 1 338 ? 144.982 119.847 125.374 1.00 34.26 ? 338 LYS   A O   1 
ATOM   2121 C CB  . LYS   A 1 338 ? 145.365 122.595 125.656 1.00 30.20 ? 338 LYS   A CB  1 
ATOM   2122 C CG  . LYS   A 1 338 ? 145.569 124.063 125.994 1.00 27.84 ? 338 LYS   A CG  1 
ATOM   2123 C CD  . LYS   A 1 338 ? 146.951 124.541 125.581 1.00 32.72 ? 338 LYS   A CD  1 
ATOM   2124 C CE  . LYS   A 1 338 ? 148.039 123.835 126.374 1.00 33.76 ? 338 LYS   A CE  1 
ATOM   2125 N NZ  . LYS   A 1 338 ? 147.773 123.878 127.839 1.00 29.03 ? 338 LYS   A NZ  1 
ATOM   2126 N N   . VAL   A 1 339 ? 143.685 119.649 127.202 1.00 26.62 ? 339 VAL   A N   1 
ATOM   2127 C CA  . VAL   A 1 339 ? 143.478 118.212 127.076 1.00 31.11 ? 339 VAL   A CA  1 
ATOM   2128 C C   . VAL   A 1 339 ? 142.050 117.978 126.605 1.00 30.83 ? 339 VAL   A C   1 
ATOM   2129 O O   . VAL   A 1 339 ? 141.142 118.755 126.927 1.00 29.18 ? 339 VAL   A O   1 
ATOM   2130 C CB  . VAL   A 1 339 ? 143.766 117.474 128.400 1.00 28.02 ? 339 VAL   A CB  1 
ATOM   2131 C CG1 . VAL   A 1 339 ? 142.649 117.700 129.410 1.00 30.28 ? 339 VAL   A CG1 1 
ATOM   2132 C CG2 . VAL   A 1 339 ? 143.982 115.988 128.148 1.00 31.18 ? 339 VAL   A CG2 1 
ATOM   2133 N N   . ASN   A 1 340 ? 141.858 116.922 125.821 1.00 44.79 ? 340 ASN   A N   1 
ATOM   2134 C CA  . ASN   A 1 340 ? 140.559 116.629 125.226 1.00 48.73 ? 340 ASN   A CA  1 
ATOM   2135 C C   . ASN   A 1 340 ? 139.735 115.799 126.202 1.00 50.38 ? 340 ASN   A C   1 
ATOM   2136 O O   . ASN   A 1 340 ? 140.125 114.684 126.563 1.00 52.10 ? 340 ASN   A O   1 
ATOM   2137 C CB  . ASN   A 1 340 ? 140.738 115.898 123.899 1.00 45.64 ? 340 ASN   A CB  1 
ATOM   2138 C CG  . ASN   A 1 340 ? 139.543 116.054 122.982 1.00 48.76 ? 340 ASN   A CG  1 
ATOM   2139 O OD1 . ASN   A 1 340 ? 138.858 117.076 123.003 1.00 47.56 ? 340 ASN   A OD1 1 
ATOM   2140 N ND2 . ASN   A 1 340 ? 139.287 115.037 122.167 1.00 49.00 ? 340 ASN   A ND2 1 
ATOM   2141 N N   . TRP   A 1 341 ? 138.599 116.342 126.634 1.00 29.60 ? 341 TRP   A N   1 
ATOM   2142 C CA  . TRP   A 1 341 ? 137.687 115.593 127.487 1.00 31.22 ? 341 TRP   A CA  1 
ATOM   2143 C C   . TRP   A 1 341 ? 136.722 114.732 126.685 1.00 29.58 ? 341 TRP   A C   1 
ATOM   2144 O O   . TRP   A 1 341 ? 135.892 114.037 127.281 1.00 30.82 ? 341 TRP   A O   1 
ATOM   2145 C CB  . TRP   A 1 341 ? 136.897 116.543 128.392 1.00 30.44 ? 341 TRP   A CB  1 
ATOM   2146 C CG  . TRP   A 1 341 ? 137.763 117.377 129.285 1.00 28.90 ? 341 TRP   A CG  1 
ATOM   2147 C CD1 . TRP   A 1 341 ? 138.001 118.712 129.167 1.00 24.67 ? 341 TRP   A CD1 1 
ATOM   2148 C CD2 . TRP   A 1 341 ? 138.549 116.928 130.396 1.00 26.57 ? 341 TRP   A CD2 1 
ATOM   2149 N NE1 . TRP   A 1 341 ? 138.861 119.132 130.151 1.00 27.82 ? 341 TRP   A NE1 1 
ATOM   2150 C CE2 . TRP   A 1 341 ? 139.216 118.054 130.917 1.00 26.09 ? 341 TRP   A CE2 1 
ATOM   2151 C CE3 . TRP   A 1 341 ? 138.745 115.686 131.007 1.00 30.61 ? 341 TRP   A CE3 1 
ATOM   2152 C CZ2 . TRP   A 1 341 ? 140.063 117.978 132.020 1.00 30.74 ? 341 TRP   A CZ2 1 
ATOM   2153 C CZ3 . TRP   A 1 341 ? 139.591 115.613 132.100 1.00 29.62 ? 341 TRP   A CZ3 1 
ATOM   2154 C CH2 . TRP   A 1 341 ? 140.238 116.750 132.595 1.00 27.83 ? 341 TRP   A CH2 1 
ATOM   2155 N N   . ASP   A 1 342 ? 136.801 114.775 125.352 1.00 49.06 ? 342 ASP   A N   1 
ATOM   2156 C CA  . ASP   A 1 342 ? 135.931 113.947 124.524 1.00 44.43 ? 342 ASP   A CA  1 
ATOM   2157 C C   . ASP   A 1 342 ? 136.179 112.466 124.779 1.00 42.59 ? 342 ASP   A C   1 
ATOM   2158 O O   . ASP   A 1 342 ? 135.232 111.677 124.881 1.00 49.88 ? 342 ASP   A O   1 
ATOM   2159 C CB  . ASP   A 1 342 ? 136.146 114.286 123.048 1.00 46.97 ? 342 ASP   A CB  1 
ATOM   2160 C CG  . ASP   A 1 342 ? 134.981 113.864 122.170 1.00 49.51 ? 342 ASP   A CG  1 
ATOM   2161 O OD1 . ASP   A 1 342 ? 134.219 112.960 122.570 1.00 44.38 ? 342 ASP   A OD1 1 
ATOM   2162 O OD2 . ASP   A 1 342 ? 134.828 114.441 121.073 1.00 43.16 ? 342 ASP   A OD2 1 
ATOM   2163 N N   . LEU   A 1 343 ? 137.446 112.070 124.888 1.00 30.86 ? 343 LEU   A N   1 
ATOM   2164 C CA  . LEU   A 1 343 ? 137.801 110.694 125.205 1.00 34.03 ? 343 LEU   A CA  1 
ATOM   2165 C C   . LEU   A 1 343 ? 138.135 110.488 126.674 1.00 28.10 ? 343 LEU   A C   1 
ATOM   2166 O O   . LEU   A 1 343 ? 137.993 109.369 127.178 1.00 29.03 ? 343 LEU   A O   1 
ATOM   2167 C CB  . LEU   A 1 343 ? 138.990 110.235 124.350 1.00 31.61 ? 343 LEU   A CB  1 
ATOM   2168 C CG  . LEU   A 1 343 ? 140.373 110.825 124.645 1.00 33.29 ? 343 LEU   A CG  1 
ATOM   2169 C CD1 . LEU   A 1 343 ? 141.462 109.885 124.153 1.00 34.58 ? 343 LEU   A CD1 1 
ATOM   2170 C CD2 . LEU   A 1 343 ? 140.537 112.200 124.013 1.00 28.17 ? 343 LEU   A CD2 1 
ATOM   2171 N N   . LEU   A 1 344 ? 138.571 111.534 127.372 1.00 28.42 ? 344 LEU   A N   1 
ATOM   2172 C CA  . LEU   A 1 344 ? 138.916 111.443 128.783 1.00 26.05 ? 344 LEU   A CA  1 
ATOM   2173 C C   . LEU   A 1 344 ? 137.770 111.827 129.708 1.00 28.88 ? 344 LEU   A C   1 
ATOM   2174 O O   . LEU   A 1 344 ? 137.944 111.781 130.930 1.00 24.21 ? 344 LEU   A O   1 
ATOM   2175 C CB  . LEU   A 1 344 ? 140.132 112.322 129.091 1.00 27.46 ? 344 LEU   A CB  1 
ATOM   2176 C CG  . LEU   A 1 344 ? 141.445 111.960 128.396 1.00 23.90 ? 344 LEU   A CG  1 
ATOM   2177 C CD1 . LEU   A 1 344 ? 142.607 112.686 129.053 1.00 22.37 ? 344 LEU   A CD1 1 
ATOM   2178 C CD2 . LEU   A 1 344 ? 141.670 110.457 128.418 1.00 27.05 ? 344 LEU   A CD2 1 
ATOM   2179 N N   . GLY   A 1 345 ? 136.614 112.212 129.165 1.00 24.61 ? 345 GLY   A N   1 
ATOM   2180 C CA  . GLY   A 1 345 ? 135.496 112.573 130.023 1.00 29.15 ? 345 GLY   A CA  1 
ATOM   2181 C C   . GLY   A 1 345 ? 135.045 111.418 130.894 1.00 28.14 ? 345 GLY   A C   1 
ATOM   2182 O O   . GLY   A 1 345 ? 134.872 111.567 132.106 1.00 30.52 ? 345 GLY   A O   1 
ATOM   2183 N N   . GLU   A 1 346 ? 134.867 110.242 130.291 1.00 42.94 ? 346 GLU   A N   1 
ATOM   2184 C CA  . GLU   A 1 346 ? 134.540 109.061 131.079 1.00 48.90 ? 346 GLU   A CA  1 
ATOM   2185 C C   . GLU   A 1 346 ? 135.673 108.719 132.035 1.00 44.16 ? 346 GLU   A C   1 
ATOM   2186 O O   . GLU   A 1 346 ? 135.432 108.365 133.195 1.00 43.80 ? 346 GLU   A O   1 
ATOM   2187 C CB  . GLU   A 1 346 ? 134.245 107.876 130.161 1.00 46.50 ? 346 GLU   A CB  1 
ATOM   2188 C CG  . GLU   A 1 346 ? 133.468 108.225 128.900 1.00 44.74 ? 346 GLU   A CG  1 
ATOM   2189 C CD  . GLU   A 1 346 ? 132.796 107.012 128.282 1.00 42.63 ? 346 GLU   A CD  1 
ATOM   2190 O OE1 . GLU   A 1 346 ? 133.249 105.883 128.560 1.00 43.90 ? 346 GLU   A OE1 1 
ATOM   2191 O OE2 . GLU   A 1 346 ? 131.821 107.183 127.519 1.00 40.90 ? 346 GLU   A OE2 1 
ATOM   2192 N N   . LEU   A 1 347 ? 136.918 108.814 131.564 1.00 16.31 ? 347 LEU   A N   1 
ATOM   2193 C CA  . LEU   A 1 347 ? 138.056 108.485 132.414 1.00 12.67 ? 347 LEU   A CA  1 
ATOM   2194 C C   . LEU   A 1 347 ? 138.155 109.444 133.592 1.00 16.99 ? 347 LEU   A C   1 
ATOM   2195 O O   . LEU   A 1 347 ? 138.375 109.016 134.732 1.00 15.11 ? 347 LEU   A O   1 
ATOM   2196 C CB  . LEU   A 1 347 ? 139.344 108.495 131.586 1.00 17.64 ? 347 LEU   A CB  1 
ATOM   2197 C CG  . LEU   A 1 347 ? 140.674 107.996 132.167 1.00 12.66 ? 347 LEU   A CG  1 
ATOM   2198 C CD1 . LEU   A 1 347 ? 141.641 107.702 131.036 1.00 17.92 ? 347 LEU   A CD1 1 
ATOM   2199 C CD2 . LEU   A 1 347 ? 141.314 108.994 133.119 1.00 15.30 ? 347 LEU   A CD2 1 
ATOM   2200 N N   . ALA   A 1 348 ? 138.013 110.747 133.333 1.00 14.40 ? 348 ALA   A N   1 
ATOM   2201 C CA  . ALA   A 1 348 ? 138.046 111.725 134.415 1.00 15.96 ? 348 ALA   A CA  1 
ATOM   2202 C C   . ALA   A 1 348 ? 136.903 111.490 135.389 1.00 13.03 ? 348 ALA   A C   1 
ATOM   2203 O O   . ALA   A 1 348 ? 137.098 111.527 136.610 1.00 15.26 ? 348 ALA   A O   1 
ATOM   2204 C CB  . ALA   A 1 348 ? 137.987 113.143 133.849 1.00 11.02 ? 348 ALA   A CB  1 
ATOM   2205 N N   . LEU   A 1 349 ? 135.706 111.220 134.866 1.00 15.11 ? 349 LEU   A N   1 
ATOM   2206 C CA  . LEU   A 1 349 ? 134.567 110.917 135.725 1.00 7.55  ? 349 LEU   A CA  1 
ATOM   2207 C C   . LEU   A 1 349 ? 134.879 109.748 136.651 1.00 14.53 ? 349 LEU   A C   1 
ATOM   2208 O O   . LEU   A 1 349 ? 134.737 109.857 137.873 1.00 7.29  ? 349 LEU   A O   1 
ATOM   2209 C CB  . LEU   A 1 349 ? 133.340 110.614 134.861 1.00 10.10 ? 349 LEU   A CB  1 
ATOM   2210 C CG  . LEU   A 1 349 ? 131.922 110.914 135.357 1.00 13.33 ? 349 LEU   A CG  1 
ATOM   2211 C CD1 . LEU   A 1 349 ? 130.901 110.440 134.329 1.00 12.29 ? 349 LEU   A CD1 1 
ATOM   2212 C CD2 . LEU   A 1 349 ? 131.631 110.291 136.709 1.00 12.18 ? 349 LEU   A CD2 1 
ATOM   2213 N N   . VAL   A 1 350 ? 135.347 108.632 136.087 1.00 14.49 ? 350 VAL   A N   1 
ATOM   2214 C CA  . VAL   A 1 350 ? 135.615 107.443 136.897 1.00 17.63 ? 350 VAL   A CA  1 
ATOM   2215 C C   . VAL   A 1 350 ? 136.694 107.725 137.940 1.00 19.28 ? 350 VAL   A C   1 
ATOM   2216 O O   . VAL   A 1 350 ? 136.510 107.466 139.137 1.00 14.50 ? 350 VAL   A O   1 
ATOM   2217 C CB  . VAL   A 1 350 ? 136.006 106.258 135.997 1.00 15.36 ? 350 VAL   A CB  1 
ATOM   2218 C CG1 . VAL   A 1 350 ? 136.303 105.054 136.845 1.00 10.74 ? 350 VAL   A CG1 1 
ATOM   2219 C CG2 . VAL   A 1 350 ? 134.891 105.935 135.030 1.00 13.99 ? 350 VAL   A CG2 1 
ATOM   2220 N N   . VAL   A 1 351 ? 137.826 108.283 137.506 1.00 13.19 ? 351 VAL   A N   1 
ATOM   2221 C CA  . VAL   A 1 351 ? 138.966 108.447 138.405 1.00 17.47 ? 351 VAL   A CA  1 
ATOM   2222 C C   . VAL   A 1 351 ? 138.623 109.406 139.535 1.00 9.62  ? 351 VAL   A C   1 
ATOM   2223 O O   . VAL   A 1 351 ? 138.860 109.115 140.711 1.00 15.83 ? 351 VAL   A O   1 
ATOM   2224 C CB  . VAL   A 1 351 ? 140.210 108.915 137.628 1.00 13.97 ? 351 VAL   A CB  1 
ATOM   2225 C CG1 . VAL   A 1 351 ? 141.353 109.186 138.591 1.00 14.58 ? 351 VAL   A CG1 1 
ATOM   2226 C CG2 . VAL   A 1 351 ? 140.622 107.866 136.616 1.00 8.81  ? 351 VAL   A CG2 1 
ATOM   2227 N N   . PHE   A 1 352 ? 138.049 110.561 139.203 1.00 8.27  ? 352 PHE   A N   1 
ATOM   2228 C CA  . PHE   A 1 352 ? 137.802 111.555 140.236 1.00 9.64  ? 352 PHE   A CA  1 
ATOM   2229 C C   . PHE   A 1 352 ? 136.566 111.251 141.074 1.00 6.85  ? 352 PHE   A C   1 
ATOM   2230 O O   . PHE   A 1 352 ? 136.508 111.686 142.226 1.00 13.50 ? 352 PHE   A O   1 
ATOM   2231 C CB  . PHE   A 1 352 ? 137.723 112.942 139.603 1.00 15.51 ? 352 PHE   A CB  1 
ATOM   2232 C CG  . PHE   A 1 352 ? 139.051 113.450 139.118 1.00 12.27 ? 352 PHE   A CG  1 
ATOM   2233 C CD1 . PHE   A 1 352 ? 139.974 113.969 140.009 1.00 12.24 ? 352 PHE   A CD1 1 
ATOM   2234 C CD2 . PHE   A 1 352 ? 139.394 113.372 137.778 1.00 12.96 ? 352 PHE   A CD2 1 
ATOM   2235 C CE1 . PHE   A 1 352 ? 141.202 114.429 139.568 1.00 9.83  ? 352 PHE   A CE1 1 
ATOM   2236 C CE2 . PHE   A 1 352 ? 140.622 113.829 137.331 1.00 10.47 ? 352 PHE   A CE2 1 
ATOM   2237 C CZ  . PHE   A 1 352 ? 141.526 114.358 138.226 1.00 12.55 ? 352 PHE   A CZ  1 
ATOM   2238 N N   . SER   A 1 353 ? 135.607 110.466 140.569 1.00 13.48 ? 353 SER   A N   1 
ATOM   2239 C CA  . SER   A 1 353 ? 134.542 109.982 141.442 1.00 7.40  ? 353 SER   A CA  1 
ATOM   2240 C C   . SER   A 1 353 ? 135.078 108.963 142.439 1.00 8.66  ? 353 SER   A C   1 
ATOM   2241 O O   . SER   A 1 353 ? 134.697 108.974 143.617 1.00 12.81 ? 353 SER   A O   1 
ATOM   2242 C CB  . SER   A 1 353 ? 133.412 109.381 140.609 1.00 8.79  ? 353 SER   A CB  1 
ATOM   2243 O OG  . SER   A 1 353 ? 132.536 110.389 140.138 1.00 5.86  ? 353 SER   A OG  1 
ATOM   2244 N N   . VAL   A 1 354 ? 135.972 108.078 141.988 1.00 4.89  ? 354 VAL   A N   1 
ATOM   2245 C CA  . VAL   A 1 354 ? 136.620 107.161 142.918 1.00 5.26  ? 354 VAL   A CA  1 
ATOM   2246 C C   . VAL   A 1 354 ? 137.461 107.936 143.924 1.00 8.27  ? 354 VAL   A C   1 
ATOM   2247 O O   . VAL   A 1 354 ? 137.528 107.570 145.104 1.00 9.67  ? 354 VAL   A O   1 
ATOM   2248 C CB  . VAL   A 1 354 ? 137.453 106.125 142.140 1.00 12.12 ? 354 VAL   A CB  1 
ATOM   2249 C CG1 . VAL   A 1 354 ? 138.625 105.623 142.974 1.00 12.35 ? 354 VAL   A CG1 1 
ATOM   2250 C CG2 . VAL   A 1 354 ? 136.572 104.968 141.694 1.00 6.39  ? 354 VAL   A CG2 1 
ATOM   2251 N N   . VAL   A 1 355 ? 138.099 109.022 143.484 1.00 8.85  ? 355 VAL   A N   1 
ATOM   2252 C CA  . VAL   A 1 355 ? 138.867 109.865 144.393 1.00 4.14  ? 355 VAL   A CA  1 
ATOM   2253 C C   . VAL   A 1 355 ? 137.954 110.512 145.429 1.00 5.00  ? 355 VAL   A C   1 
ATOM   2254 O O   . VAL   A 1 355 ? 138.294 110.578 146.615 1.00 4.24  ? 355 VAL   A O   1 
ATOM   2255 C CB  . VAL   A 1 355 ? 139.666 110.913 143.596 1.00 5.45  ? 355 VAL   A CB  1 
ATOM   2256 C CG1 . VAL   A 1 355 ? 139.987 112.118 144.461 1.00 3.46  ? 355 VAL   A CG1 1 
ATOM   2257 C CG2 . VAL   A 1 355 ? 140.942 110.297 143.043 1.00 4.51  ? 355 VAL   A CG2 1 
ATOM   2258 N N   . ASN   A 1 356 ? 136.785 111.001 145.003 1.00 1.19  ? 356 ASN   A N   1 
ATOM   2259 C CA  . ASN   A 1 356 ? 135.826 111.566 145.950 1.00 9.60  ? 356 ASN   A CA  1 
ATOM   2260 C C   . ASN   A 1 356 ? 135.386 110.530 146.976 1.00 5.01  ? 356 ASN   A C   1 
ATOM   2261 O O   . ASN   A 1 356 ? 135.331 110.817 148.178 1.00 9.20  ? 356 ASN   A O   1 
ATOM   2262 C CB  . ASN   A 1 356 ? 134.607 112.117 145.210 1.00 7.43  ? 356 ASN   A CB  1 
ATOM   2263 C CG  . ASN   A 1 356 ? 134.943 113.298 144.331 1.00 4.55  ? 356 ASN   A CG  1 
ATOM   2264 O OD1 . ASN   A 1 356 ? 136.103 113.679 144.207 1.00 7.52  ? 356 ASN   A OD1 1 
ATOM   2265 N ND2 . ASN   A 1 356 ? 133.926 113.887 143.714 1.00 6.25  ? 356 ASN   A ND2 1 
ATOM   2266 N N   . ALA   A 1 357 ? 135.067 109.318 146.517 1.00 5.10  ? 357 ALA   A N   1 
ATOM   2267 C CA  . ALA   A 1 357 ? 134.647 108.269 147.442 1.00 7.28  ? 357 ALA   A CA  1 
ATOM   2268 C C   . ALA   A 1 357 ? 135.759 107.917 148.423 1.00 9.19  ? 357 ALA   A C   1 
ATOM   2269 O O   . ALA   A 1 357 ? 135.516 107.783 149.630 1.00 5.12  ? 357 ALA   A O   1 
ATOM   2270 C CB  . ALA   A 1 357 ? 134.207 107.031 146.664 1.00 2.19  ? 357 ALA   A CB  1 
ATOM   2271 N N   . GLY   A 1 358 ? 136.987 107.767 147.924 1.00 3.67  ? 358 GLY   A N   1 
ATOM   2272 C CA  . GLY   A 1 358 ? 138.102 107.444 148.794 1.00 8.95  ? 358 GLY   A CA  1 
ATOM   2273 C C   . GLY   A 1 358 ? 138.420 108.540 149.786 1.00 10.28 ? 358 GLY   A C   1 
ATOM   2274 O O   . GLY   A 1 358 ? 138.797 108.257 150.925 1.00 7.24  ? 358 GLY   A O   1 
ATOM   2275 N N   . SER   A 1 359 ? 138.284 109.801 149.373 1.00 2.00  ? 359 SER   A N   1 
ATOM   2276 C CA  . SER   A 1 359 ? 138.492 110.912 150.293 1.00 8.24  ? 359 SER   A CA  1 
ATOM   2277 C C   . SER   A 1 359 ? 137.409 110.955 151.362 1.00 5.94  ? 359 SER   A C   1 
ATOM   2278 O O   . SER   A 1 359 ? 137.699 111.220 152.534 1.00 8.21  ? 359 SER   A O   1 
ATOM   2279 C CB  . SER   A 1 359 ? 138.537 112.227 149.519 1.00 9.25  ? 359 SER   A CB  1 
ATOM   2280 O OG  . SER   A 1 359 ? 137.384 112.369 148.711 1.00 10.14 ? 359 SER   A OG  1 
ATOM   2281 N N   . LEU   A 1 360 ? 136.154 110.705 150.978 1.00 4.23  ? 360 LEU   A N   1 
ATOM   2282 C CA  . LEU   A 1 360 ? 135.076 110.695 151.962 1.00 6.23  ? 360 LEU   A CA  1 
ATOM   2283 C C   . LEU   A 1 360 ? 135.255 109.567 152.969 1.00 5.11  ? 360 LEU   A C   1 
ATOM   2284 O O   . LEU   A 1 360 ? 135.026 109.759 154.169 1.00 4.96  ? 360 LEU   A O   1 
ATOM   2285 C CB  . LEU   A 1 360 ? 133.722 110.585 151.266 1.00 6.27  ? 360 LEU   A CB  1 
ATOM   2286 C CG  . LEU   A 1 360 ? 133.176 111.870 150.643 1.00 6.92  ? 360 LEU   A CG  1 
ATOM   2287 C CD1 . LEU   A 1 360 ? 131.676 111.760 150.468 1.00 6.71  ? 360 LEU   A CD1 1 
ATOM   2288 C CD2 . LEU   A 1 360 ? 133.528 113.078 151.493 1.00 1.64  ? 360 LEU   A CD2 1 
ATOM   2289 N N   . PHE   A 1 361 ? 135.656 108.380 152.504 1.00 8.45  ? 361 PHE   A N   1 
ATOM   2290 C CA  . PHE   A 1 361 ? 135.976 107.306 153.440 1.00 15.91 ? 361 PHE   A CA  1 
ATOM   2291 C C   . PHE   A 1 361 ? 137.163 107.682 154.318 1.00 13.00 ? 361 PHE   A C   1 
ATOM   2292 O O   . PHE   A 1 361 ? 137.152 107.437 155.530 1.00 13.03 ? 361 PHE   A O   1 
ATOM   2293 C CB  . PHE   A 1 361 ? 136.253 106.006 152.686 1.00 15.86 ? 361 PHE   A CB  1 
ATOM   2294 C CG  . PHE   A 1 361 ? 135.012 105.279 152.253 1.00 7.93  ? 361 PHE   A CG  1 
ATOM   2295 C CD1 . PHE   A 1 361 ? 134.170 104.705 153.191 1.00 7.96  ? 361 PHE   A CD1 1 
ATOM   2296 C CD2 . PHE   A 1 361 ? 134.684 105.173 150.913 1.00 16.39 ? 361 PHE   A CD2 1 
ATOM   2297 C CE1 . PHE   A 1 361 ? 133.027 104.036 152.799 1.00 13.49 ? 361 PHE   A CE1 1 
ATOM   2298 C CE2 . PHE   A 1 361 ? 133.543 104.505 150.515 1.00 14.54 ? 361 PHE   A CE2 1 
ATOM   2299 C CZ  . PHE   A 1 361 ? 132.713 103.936 151.459 1.00 14.03 ? 361 PHE   A CZ  1 
ATOM   2300 N N   . LEU   A 1 362 ? 138.196 108.282 153.722 1.00 8.53  ? 362 LEU   A N   1 
ATOM   2301 C CA  . LEU   A 1 362 ? 139.325 108.787 154.494 1.00 7.55  ? 362 LEU   A CA  1 
ATOM   2302 C C   . LEU   A 1 362 ? 138.890 109.883 155.456 1.00 9.89  ? 362 LEU   A C   1 
ATOM   2303 O O   . LEU   A 1 362 ? 139.428 109.987 156.565 1.00 13.65 ? 362 LEU   A O   1 
ATOM   2304 C CB  . LEU   A 1 362 ? 140.408 109.301 153.542 1.00 10.45 ? 362 LEU   A CB  1 
ATOM   2305 C CG  . LEU   A 1 362 ? 141.392 110.376 154.011 1.00 11.43 ? 362 LEU   A CG  1 
ATOM   2306 C CD1 . LEU   A 1 362 ? 142.335 109.835 155.072 1.00 9.21  ? 362 LEU   A CD1 1 
ATOM   2307 C CD2 . LEU   A 1 362 ? 142.173 110.933 152.831 1.00 14.52 ? 362 LEU   A CD2 1 
ATOM   2308 N N   . MET   A 1 363 ? 137.918 110.704 155.052 1.00 7.40  ? 363 MET   A N   1 
ATOM   2309 C CA  . MET   A 1 363 ? 137.416 111.753 155.931 1.00 3.52  ? 363 MET   A CA  1 
ATOM   2310 C C   . MET   A 1 363 ? 136.731 111.169 157.159 1.00 6.51  ? 363 MET   A C   1 
ATOM   2311 O O   . MET   A 1 363 ? 136.680 111.819 158.209 1.00 5.40  ? 363 MET   A O   1 
ATOM   2312 C CB  . MET   A 1 363 ? 136.443 112.650 155.170 1.00 8.81  ? 363 MET   A CB  1 
ATOM   2313 C CG  . MET   A 1 363 ? 137.056 113.934 154.654 1.00 2.72  ? 363 MET   A CG  1 
ATOM   2314 S SD  . MET   A 1 363 ? 135.823 115.008 153.907 1.00 1.05  ? 363 MET   A SD  1 
ATOM   2315 C CE  . MET   A 1 363 ? 135.071 115.694 155.374 1.00 1.88  ? 363 MET   A CE  1 
ATOM   2316 N N   . HIS   A 1 364 ? 136.199 109.952 157.046 1.00 17.99 ? 364 HIS   A N   1 
ATOM   2317 C CA  . HIS   A 1 364 ? 135.485 109.289 158.129 1.00 22.66 ? 364 HIS   A CA  1 
ATOM   2318 C C   . HIS   A 1 364 ? 136.323 108.232 158.837 1.00 16.83 ? 364 HIS   A C   1 
ATOM   2319 O O   . HIS   A 1 364 ? 136.431 108.250 160.066 1.00 20.38 ? 364 HIS   A O   1 
ATOM   2320 C CB  . HIS   A 1 364 ? 134.203 108.641 157.595 1.00 20.35 ? 364 HIS   A CB  1 
ATOM   2321 C CG  . HIS   A 1 364 ? 133.690 107.534 158.461 1.00 18.20 ? 364 HIS   A CG  1 
ATOM   2322 N ND1 . HIS   A 1 364 ? 133.662 106.219 158.049 1.00 14.62 ? 364 HIS   A ND1 1 
ATOM   2323 C CD2 . HIS   A 1 364 ? 133.197 107.545 159.721 1.00 21.57 ? 364 HIS   A CD2 1 
ATOM   2324 C CE1 . HIS   A 1 364 ? 133.171 105.468 159.019 1.00 17.08 ? 364 HIS   A CE1 1 
ATOM   2325 N NE2 . HIS   A 1 364 ? 132.877 106.249 160.043 1.00 18.10 ? 364 HIS   A NE2 1 
ATOM   2326 N N   . TYR   A 1 365 ? 136.911 107.301 158.079 1.00 35.09 ? 365 TYR   A N   1 
ATOM   2327 C CA  . TYR   A 1 365 ? 137.570 106.149 158.688 1.00 37.95 ? 365 TYR   A CA  1 
ATOM   2328 C C   . TYR   A 1 365 ? 138.751 106.571 159.555 1.00 32.18 ? 365 TYR   A C   1 
ATOM   2329 O O   . TYR   A 1 365 ? 138.934 106.050 160.661 1.00 36.82 ? 365 TYR   A O   1 
ATOM   2330 C CB  . TYR   A 1 365 ? 138.025 105.174 157.603 1.00 31.47 ? 365 TYR   A CB  1 
ATOM   2331 C CG  . TYR   A 1 365 ? 136.995 104.125 157.253 1.00 41.15 ? 365 TYR   A CG  1 
ATOM   2332 C CD1 . TYR   A 1 365 ? 136.020 103.749 158.167 1.00 37.30 ? 365 TYR   A CD1 1 
ATOM   2333 C CD2 . TYR   A 1 365 ? 136.995 103.513 156.006 1.00 35.16 ? 365 TYR   A CD2 1 
ATOM   2334 C CE1 . TYR   A 1 365 ? 135.075 102.792 157.851 1.00 32.78 ? 365 TYR   A CE1 1 
ATOM   2335 C CE2 . TYR   A 1 365 ? 136.055 102.555 155.681 1.00 38.29 ? 365 TYR   A CE2 1 
ATOM   2336 C CZ  . TYR   A 1 365 ? 135.097 102.198 156.607 1.00 40.37 ? 365 TYR   A CZ  1 
ATOM   2337 O OH  . TYR   A 1 365 ? 134.158 101.244 156.288 1.00 34.50 ? 365 TYR   A OH  1 
ATOM   2338 N N   . THR   A 1 366 ? 139.558 107.511 159.074 1.00 42.24 ? 366 THR   A N   1 
ATOM   2339 C CA  . THR   A 1 366 ? 140.732 107.968 159.806 1.00 37.45 ? 366 THR   A CA  1 
ATOM   2340 C C   . THR   A 1 366 ? 140.317 109.043 160.803 1.00 44.14 ? 366 THR   A C   1 
ATOM   2341 O O   . THR   A 1 366 ? 139.837 110.111 160.408 1.00 41.59 ? 366 THR   A O   1 
ATOM   2342 C CB  . THR   A 1 366 ? 141.794 108.505 158.849 1.00 40.82 ? 366 THR   A CB  1 
ATOM   2343 O OG1 . THR   A 1 366 ? 141.304 109.685 158.201 1.00 43.88 ? 366 THR   A OG1 1 
ATOM   2344 C CG2 . THR   A 1 366 ? 142.140 107.457 157.801 1.00 37.26 ? 366 THR   A CG2 1 
ATOM   2345 N N   . ALA   A 1 367 ? 140.504 108.760 162.091 1.00 57.26 ? 367 ALA   A N   1 
ATOM   2346 C CA  . ALA   A 1 367 ? 140.147 109.703 163.150 1.00 54.81 ? 367 ALA   A CA  1 
ATOM   2347 C C   . ALA   A 1 367 ? 141.320 110.636 163.454 1.00 55.74 ? 367 ALA   A C   1 
ATOM   2348 O O   . ALA   A 1 367 ? 141.742 110.819 164.595 1.00 53.74 ? 367 ALA   A O   1 
ATOM   2349 C CB  . ALA   A 1 367 ? 139.697 108.950 164.397 1.00 56.37 ? 367 ALA   A CB  1 
ATOM   2350 N N   . ASN   A 1 368 ? 141.846 111.235 162.388 1.00 57.18 ? 368 ASN   A N   1 
ATOM   2351 C CA  . ASN   A 1 368 ? 142.899 112.236 162.479 1.00 51.66 ? 368 ASN   A CA  1 
ATOM   2352 C C   . ASN   A 1 368 ? 142.378 113.523 161.861 1.00 56.32 ? 368 ASN   A C   1 
ATOM   2353 O O   . ASN   A 1 368 ? 141.895 113.516 160.724 1.00 52.99 ? 368 ASN   A O   1 
ATOM   2354 C CB  . ASN   A 1 368 ? 144.176 111.773 161.769 1.00 59.36 ? 368 ASN   A CB  1 
ATOM   2355 C CG  . ASN   A 1 368 ? 145.266 112.829 161.775 1.00 52.18 ? 368 ASN   A CG  1 
ATOM   2356 O OD1 . ASN   A 1 368 ? 145.258 113.745 162.598 1.00 53.06 ? 368 ASN   A OD1 1 
ATOM   2357 N ND2 . ASN   A 1 368 ? 146.213 112.706 160.852 1.00 50.67 ? 368 ASN   A ND2 1 
ATOM   2358 N N   . ILE   A 1 369 ? 142.473 114.622 162.610 1.00 45.01 ? 369 ILE   A N   1 
ATOM   2359 C CA  . ILE   A 1 369 ? 141.876 115.872 162.154 1.00 46.11 ? 369 ILE   A CA  1 
ATOM   2360 C C   . ILE   A 1 369 ? 142.632 116.426 160.950 1.00 46.27 ? 369 ILE   A C   1 
ATOM   2361 O O   . ILE   A 1 369 ? 142.023 116.957 160.014 1.00 49.59 ? 369 ILE   A O   1 
ATOM   2362 C CB  . ILE   A 1 369 ? 141.796 116.883 163.314 1.00 44.01 ? 369 ILE   A CB  1 
ATOM   2363 C CG1 . ILE   A 1 369 ? 141.021 118.127 162.882 1.00 45.01 ? 369 ILE   A CG1 1 
ATOM   2364 C CG2 . ILE   A 1 369 ? 143.184 117.245 163.834 1.00 49.05 ? 369 ILE   A CG2 1 
ATOM   2365 C CD1 . ILE   A 1 369 ? 139.559 117.866 162.589 1.00 46.30 ? 369 ILE   A CD1 1 
ATOM   2366 N N   . TRP   A 1 370 ? 143.962 116.302 160.941 1.00 59.47 ? 370 TRP   A N   1 
ATOM   2367 C CA  . TRP   A 1 370 ? 144.733 116.746 159.782 1.00 55.72 ? 370 TRP   A CA  1 
ATOM   2368 C C   . TRP   A 1 370 ? 144.476 115.855 158.573 1.00 57.81 ? 370 TRP   A C   1 
ATOM   2369 O O   . TRP   A 1 370 ? 144.351 116.347 157.444 1.00 59.14 ? 370 TRP   A O   1 
ATOM   2370 C CB  . TRP   A 1 370 ? 146.222 116.781 160.121 1.00 54.27 ? 370 TRP   A CB  1 
ATOM   2371 C CG  . TRP   A 1 370 ? 146.638 118.014 160.863 1.00 53.26 ? 370 TRP   A CG  1 
ATOM   2372 C CD1 . TRP   A 1 370 ? 147.155 118.077 162.123 1.00 54.07 ? 370 TRP   A CD1 1 
ATOM   2373 C CD2 . TRP   A 1 370 ? 146.579 119.364 160.385 1.00 57.71 ? 370 TRP   A CD2 1 
ATOM   2374 N NE1 . TRP   A 1 370 ? 147.418 119.383 162.462 1.00 53.17 ? 370 TRP   A NE1 1 
ATOM   2375 C CE2 . TRP   A 1 370 ? 147.073 120.192 161.411 1.00 59.19 ? 370 TRP   A CE2 1 
ATOM   2376 C CE3 . TRP   A 1 370 ? 146.155 119.952 159.189 1.00 53.91 ? 370 TRP   A CE3 1 
ATOM   2377 C CZ2 . TRP   A 1 370 ? 147.155 121.577 161.279 1.00 55.44 ? 370 TRP   A CZ2 1 
ATOM   2378 C CZ3 . TRP   A 1 370 ? 146.237 121.326 159.060 1.00 57.20 ? 370 TRP   A CZ3 1 
ATOM   2379 C CH2 . TRP   A 1 370 ? 146.733 122.123 160.099 1.00 54.09 ? 370 TRP   A CH2 1 
ATOM   2380 N N   . ALA   A 1 371 ? 144.397 114.540 158.789 1.00 28.63 ? 371 ALA   A N   1 
ATOM   2381 C CA  . ALA   A 1 371 ? 144.051 113.636 157.699 1.00 26.14 ? 371 ALA   A CA  1 
ATOM   2382 C C   . ALA   A 1 371 ? 142.647 113.920 157.183 1.00 35.78 ? 371 ALA   A C   1 
ATOM   2383 O O   . ALA   A 1 371 ? 142.397 113.852 155.975 1.00 32.04 ? 371 ALA   A O   1 
ATOM   2384 C CB  . ALA   A 1 371 ? 144.172 112.183 158.157 1.00 29.71 ? 371 ALA   A CB  1 
ATOM   2385 N N   . CYS   A 1 372 ? 141.718 114.245 158.085 1.00 26.42 ? 372 CYS   A N   1 
ATOM   2386 C CA  . CYS   A 1 372 ? 140.370 114.602 157.659 1.00 30.05 ? 372 CYS   A CA  1 
ATOM   2387 C C   . CYS   A 1 372 ? 140.370 115.895 156.851 1.00 30.68 ? 372 CYS   A C   1 
ATOM   2388 O O   . CYS   A 1 372 ? 139.640 116.012 155.861 1.00 35.46 ? 372 CYS   A O   1 
ATOM   2389 C CB  . CYS   A 1 372 ? 139.448 114.723 158.871 1.00 28.94 ? 372 CYS   A CB  1 
ATOM   2390 S SG  . CYS   A 1 372 ? 137.741 115.142 158.460 1.00 32.30 ? 372 CYS   A SG  1 
ATOM   2391 N N   . TYR   A 1 373 ? 141.179 116.880 157.257 1.00 31.83 ? 373 TYR   A N   1 
ATOM   2392 C CA  . TYR   A 1 373 ? 141.274 118.115 156.483 1.00 27.04 ? 373 TYR   A CA  1 
ATOM   2393 C C   . TYR   A 1 373 ? 141.834 117.847 155.093 1.00 30.24 ? 373 TYR   A C   1 
ATOM   2394 O O   . TYR   A 1 373 ? 141.343 118.396 154.099 1.00 33.05 ? 373 TYR   A O   1 
ATOM   2395 C CB  . TYR   A 1 373 ? 142.147 119.145 157.201 1.00 26.15 ? 373 TYR   A CB  1 
ATOM   2396 C CG  . TYR   A 1 373 ? 141.506 119.822 158.392 1.00 31.24 ? 373 TYR   A CG  1 
ATOM   2397 C CD1 . TYR   A 1 373 ? 140.200 120.279 158.339 1.00 25.25 ? 373 TYR   A CD1 1 
ATOM   2398 C CD2 . TYR   A 1 373 ? 142.199 119.960 159.588 1.00 25.44 ? 373 TYR   A CD2 1 
ATOM   2399 C CE1 . TYR   A 1 373 ? 139.612 120.894 159.427 1.00 30.00 ? 373 TYR   A CE1 1 
ATOM   2400 C CE2 . TYR   A 1 373 ? 141.621 120.578 160.677 1.00 25.78 ? 373 TYR   A CE2 1 
ATOM   2401 C CZ  . TYR   A 1 373 ? 140.325 121.035 160.596 1.00 34.44 ? 373 TYR   A CZ  1 
ATOM   2402 O OH  . TYR   A 1 373 ? 139.741 121.643 161.683 1.00 29.24 ? 373 TYR   A OH  1 
ATOM   2403 N N   . ALA   A 1 374 ? 142.874 117.014 155.007 1.00 18.37 ? 374 ALA   A N   1 
ATOM   2404 C CA  . ALA   A 1 374 ? 143.448 116.680 153.707 1.00 26.23 ? 374 ALA   A CA  1 
ATOM   2405 C C   . ALA   A 1 374 ? 142.444 115.934 152.839 1.00 22.81 ? 374 ALA   A C   1 
ATOM   2406 O O   . ALA   A 1 374 ? 142.342 116.187 151.631 1.00 20.80 ? 374 ALA   A O   1 
ATOM   2407 C CB  . ALA   A 1 374 ? 144.721 115.854 153.890 1.00 27.25 ? 374 ALA   A CB  1 
ATOM   2408 N N   . GLY   A 1 375 ? 141.693 115.007 153.437 1.00 14.57 ? 375 GLY   A N   1 
ATOM   2409 C CA  . GLY   A 1 375 ? 140.666 114.304 152.689 1.00 7.79  ? 375 GLY   A CA  1 
ATOM   2410 C C   . GLY   A 1 375 ? 139.574 115.229 152.191 1.00 7.20  ? 375 GLY   A C   1 
ATOM   2411 O O   . GLY   A 1 375 ? 139.085 115.078 151.072 1.00 11.08 ? 375 GLY   A O   1 
ATOM   2412 N N   . TYR   A 1 376 ? 139.177 116.201 153.016 1.00 11.14 ? 376 TYR   A N   1 
ATOM   2413 C CA  . TYR   A 1 376 ? 138.174 117.166 152.580 1.00 6.09  ? 376 TYR   A CA  1 
ATOM   2414 C C   . TYR   A 1 376 ? 138.702 118.040 151.453 1.00 8.58  ? 376 TYR   A C   1 
ATOM   2415 O O   . TYR   A 1 376 ? 137.968 118.353 150.511 1.00 4.34  ? 376 TYR   A O   1 
ATOM   2416 C CB  . TYR   A 1 376 ? 137.719 118.035 153.749 1.00 4.66  ? 376 TYR   A CB  1 
ATOM   2417 C CG  . TYR   A 1 376 ? 136.746 119.114 153.333 1.00 10.33 ? 376 TYR   A CG  1 
ATOM   2418 C CD1 . TYR   A 1 376 ? 135.498 118.790 152.819 1.00 4.22  ? 376 TYR   A CD1 1 
ATOM   2419 C CD2 . TYR   A 1 376 ? 137.084 120.455 153.433 1.00 5.38  ? 376 TYR   A CD2 1 
ATOM   2420 C CE1 . TYR   A 1 376 ? 134.608 119.773 152.434 1.00 9.61  ? 376 TYR   A CE1 1 
ATOM   2421 C CE2 . TYR   A 1 376 ? 136.200 121.443 153.055 1.00 2.87  ? 376 TYR   A CE2 1 
ATOM   2422 C CZ  . TYR   A 1 376 ? 134.967 121.098 152.553 1.00 3.04  ? 376 TYR   A CZ  1 
ATOM   2423 O OH  . TYR   A 1 376 ? 134.093 122.087 152.173 1.00 5.59  ? 376 TYR   A OH  1 
ATOM   2424 N N   . LEU   A 1 377 ? 139.966 118.458 151.541 1.00 7.66  ? 377 LEU   A N   1 
ATOM   2425 C CA  . LEU   A 1 377 ? 140.557 119.231 150.455 1.00 7.92  ? 377 LEU   A CA  1 
ATOM   2426 C C   . LEU   A 1 377 ? 140.576 118.425 149.163 1.00 12.37 ? 377 LEU   A C   1 
ATOM   2427 O O   . LEU   A 1 377 ? 140.215 118.938 148.097 1.00 4.66  ? 377 LEU   A O   1 
ATOM   2428 C CB  . LEU   A 1 377 ? 141.971 119.675 150.833 1.00 7.88  ? 377 LEU   A CB  1 
ATOM   2429 C CG  . LEU   A 1 377 ? 142.948 119.919 149.679 1.00 10.68 ? 377 LEU   A CG  1 
ATOM   2430 C CD1 . LEU   A 1 377 ? 142.635 121.226 148.966 1.00 5.73  ? 377 LEU   A CD1 1 
ATOM   2431 C CD2 . LEU   A 1 377 ? 144.384 119.905 150.178 1.00 12.87 ? 377 LEU   A CD2 1 
ATOM   2432 N N   . ILE   A 1 378 ? 140.973 117.153 149.247 1.00 6.43  ? 378 ILE   A N   1 
ATOM   2433 C CA  . ILE   A 1 378 ? 141.007 116.298 148.063 1.00 1.12  ? 378 ILE   A CA  1 
ATOM   2434 C C   . ILE   A 1 378 ? 139.607 116.131 147.488 1.00 2.05  ? 378 ILE   A C   1 
ATOM   2435 O O   . ILE   A 1 378 ? 139.396 116.254 146.276 1.00 7.43  ? 378 ILE   A O   1 
ATOM   2436 C CB  . ILE   A 1 378 ? 141.644 114.938 148.405 1.00 4.01  ? 378 ILE   A CB  1 
ATOM   2437 C CG1 . ILE   A 1 378 ? 143.166 115.067 148.492 1.00 4.82  ? 378 ILE   A CG1 1 
ATOM   2438 C CG2 . ILE   A 1 378 ? 141.251 113.886 147.381 1.00 1.39  ? 378 ILE   A CG2 1 
ATOM   2439 C CD1 . ILE   A 1 378 ? 143.876 113.754 148.734 1.00 1.35  ? 378 ILE   A CD1 1 
ATOM   2440 N N   . PHE   A 1 379 ? 138.625 115.865 148.354 1.00 19.62 ? 379 PHE   A N   1 
ATOM   2441 C CA  . PHE   A 1 379 ? 137.253 115.680 147.897 1.00 10.41 ? 379 PHE   A CA  1 
ATOM   2442 C C   . PHE   A 1 379 ? 136.729 116.934 147.215 1.00 10.97 ? 379 PHE   A C   1 
ATOM   2443 O O   . PHE   A 1 379 ? 136.179 116.868 146.111 1.00 12.21 ? 379 PHE   A O   1 
ATOM   2444 C CB  . PHE   A 1 379 ? 136.352 115.300 149.074 1.00 18.04 ? 379 PHE   A CB  1 
ATOM   2445 C CG  . PHE   A 1 379 ? 134.884 115.432 148.781 1.00 14.54 ? 379 PHE   A CG  1 
ATOM   2446 C CD1 . PHE   A 1 379 ? 134.208 114.431 148.104 1.00 16.51 ? 379 PHE   A CD1 1 
ATOM   2447 C CD2 . PHE   A 1 379 ? 134.178 116.554 149.184 1.00 11.72 ? 379 PHE   A CD2 1 
ATOM   2448 C CE1 . PHE   A 1 379 ? 132.859 114.548 147.832 1.00 11.65 ? 379 PHE   A CE1 1 
ATOM   2449 C CE2 . PHE   A 1 379 ? 132.829 116.676 148.911 1.00 15.19 ? 379 PHE   A CE2 1 
ATOM   2450 C CZ  . PHE   A 1 379 ? 132.169 115.671 148.237 1.00 17.38 ? 379 PHE   A CZ  1 
ATOM   2451 N N   . LYS   A 1 380 ? 136.887 118.090 147.863 1.00 8.19  ? 380 LYS   A N   1 
ATOM   2452 C CA  . LYS   A 1 380 ? 136.357 119.329 147.309 1.00 12.26 ? 380 LYS   A CA  1 
ATOM   2453 C C   . LYS   A 1 380 ? 137.037 119.677 145.993 1.00 10.17 ? 380 LYS   A C   1 
ATOM   2454 O O   . LYS   A 1 380 ? 136.370 120.041 145.020 1.00 6.06  ? 380 LYS   A O   1 
ATOM   2455 C CB  . LYS   A 1 380 ? 136.514 120.466 148.319 1.00 5.91  ? 380 LYS   A CB  1 
ATOM   2456 C CG  . LYS   A 1 380 ? 135.961 121.797 147.838 1.00 7.31  ? 380 LYS   A CG  1 
ATOM   2457 C CD  . LYS   A 1 380 ? 135.102 122.456 148.905 1.00 11.13 ? 380 LYS   A CD  1 
ATOM   2458 C CE  . LYS   A 1 380 ? 134.171 123.494 148.301 1.00 12.94 ? 380 LYS   A CE  1 
ATOM   2459 N NZ  . LYS   A 1 380 ? 133.558 124.364 149.342 1.00 12.18 ? 380 LYS   A NZ  1 
ATOM   2460 N N   . SER   A 1 381 ? 138.366 119.554 145.932 1.00 6.61  ? 381 SER   A N   1 
ATOM   2461 C CA  . SER   A 1 381 ? 139.079 119.893 144.705 1.00 8.12  ? 381 SER   A CA  1 
ATOM   2462 C C   . SER   A 1 381 ? 138.696 118.955 143.567 1.00 10.11 ? 381 SER   A C   1 
ATOM   2463 O O   . SER   A 1 381 ? 138.403 119.402 142.450 1.00 9.46  ? 381 SER   A O   1 
ATOM   2464 C CB  . SER   A 1 381 ? 140.588 119.860 144.950 1.00 7.89  ? 381 SER   A CB  1 
ATOM   2465 O OG  . SER   A 1 381 ? 141.138 118.607 144.584 1.00 5.01  ? 381 SER   A OG  1 
ATOM   2466 N N   . SER   A 1 382 ? 138.684 117.646 143.832 1.00 9.54  ? 382 SER   A N   1 
ATOM   2467 C CA  . SER   A 1 382 ? 138.347 116.690 142.786 1.00 3.30  ? 382 SER   A CA  1 
ATOM   2468 C C   . SER   A 1 382 ? 136.905 116.856 142.328 1.00 11.08 ? 382 SER   A C   1 
ATOM   2469 O O   . SER   A 1 382 ? 136.620 116.759 141.130 1.00 11.05 ? 382 SER   A O   1 
ATOM   2470 C CB  . SER   A 1 382 ? 138.604 115.267 143.277 1.00 9.50  ? 382 SER   A CB  1 
ATOM   2471 O OG  . SER   A 1 382 ? 137.842 114.988 144.437 1.00 7.28  ? 382 SER   A OG  1 
ATOM   2472 N N   . TYR   A 1 383 ? 135.981 117.122 143.254 1.00 9.16  ? 383 TYR   A N   1 
ATOM   2473 C CA  . TYR   A 1 383 ? 134.597 117.323 142.846 1.00 6.12  ? 383 TYR   A CA  1 
ATOM   2474 C C   . TYR   A 1 383 ? 134.430 118.621 142.068 1.00 10.14 ? 383 TYR   A C   1 
ATOM   2475 O O   . TYR   A 1 383 ? 133.607 118.690 141.155 1.00 10.03 ? 383 TYR   A O   1 
ATOM   2476 C CB  . TYR   A 1 383 ? 133.657 117.312 144.051 1.00 3.72  ? 383 TYR   A CB  1 
ATOM   2477 C CG  . TYR   A 1 383 ? 132.341 117.992 143.741 1.00 5.35  ? 383 TYR   A CG  1 
ATOM   2478 C CD1 . TYR   A 1 383 ? 131.290 117.292 143.164 1.00 5.61  ? 383 TYR   A CD1 1 
ATOM   2479 C CD2 . TYR   A 1 383 ? 132.164 119.342 143.992 1.00 5.81  ? 383 TYR   A CD2 1 
ATOM   2480 C CE1 . TYR   A 1 383 ? 130.096 117.923 142.864 1.00 7.84  ? 383 TYR   A CE1 1 
ATOM   2481 C CE2 . TYR   A 1 383 ? 130.990 119.978 143.685 1.00 2.59  ? 383 TYR   A CE2 1 
ATOM   2482 C CZ  . TYR   A 1 383 ? 129.955 119.269 143.133 1.00 8.77  ? 383 TYR   A CZ  1 
ATOM   2483 O OH  . TYR   A 1 383 ? 128.783 119.927 142.848 1.00 4.19  ? 383 TYR   A OH  1 
ATOM   2484 N N   . MET   A 1 384 ? 135.153 119.680 142.445 1.00 10.19 ? 384 MET   A N   1 
ATOM   2485 C CA  . MET   A 1 384 ? 135.071 120.919 141.677 1.00 10.54 ? 384 MET   A CA  1 
ATOM   2486 C C   . MET   A 1 384 ? 135.581 120.706 140.261 1.00 9.51  ? 384 MET   A C   1 
ATOM   2487 O O   . MET   A 1 384 ? 134.971 121.173 139.292 1.00 9.86  ? 384 MET   A O   1 
ATOM   2488 C CB  . MET   A 1 384 ? 135.861 122.032 142.365 1.00 7.83  ? 384 MET   A CB  1 
ATOM   2489 C CG  . MET   A 1 384 ? 135.248 122.591 143.647 1.00 6.71  ? 384 MET   A CG  1 
ATOM   2490 S SD  . MET   A 1 384 ? 133.478 122.349 143.874 1.00 11.54 ? 384 MET   A SD  1 
ATOM   2491 C CE  . MET   A 1 384 ? 132.781 123.463 142.662 1.00 11.99 ? 384 MET   A CE  1 
ATOM   2492 N N   . LEU   A 1 385 ? 136.694 119.984 140.123 1.00 4.78  ? 385 LEU   A N   1 
ATOM   2493 C CA  . LEU   A 1 385 ? 137.185 119.625 138.798 1.00 5.64  ? 385 LEU   A CA  1 
ATOM   2494 C C   . LEU   A 1 385 ? 136.145 118.813 138.033 1.00 6.19  ? 385 LEU   A C   1 
ATOM   2495 O O   . LEU   A 1 385 ? 135.886 119.071 136.850 1.00 11.63 ? 385 LEU   A O   1 
ATOM   2496 C CB  . LEU   A 1 385 ? 138.504 118.860 138.943 1.00 4.86  ? 385 LEU   A CB  1 
ATOM   2497 C CG  . LEU   A 1 385 ? 139.197 118.154 137.777 1.00 8.85  ? 385 LEU   A CG  1 
ATOM   2498 C CD1 . LEU   A 1 385 ? 140.693 118.111 138.030 1.00 9.01  ? 385 LEU   A CD1 1 
ATOM   2499 C CD2 . LEU   A 1 385 ? 138.670 116.745 137.623 1.00 6.76  ? 385 LEU   A CD2 1 
ATOM   2500 N N   . LEU   A 1 386 ? 135.521 117.842 138.703 1.00 3.48  ? 386 LEU   A N   1 
ATOM   2501 C CA  . LEU   A 1 386 ? 134.548 116.980 138.041 1.00 9.56  ? 386 LEU   A CA  1 
ATOM   2502 C C   . LEU   A 1 386 ? 133.298 117.746 137.626 1.00 5.50  ? 386 LEU   A C   1 
ATOM   2503 O O   . LEU   A 1 386 ? 132.752 117.501 136.549 1.00 6.50  ? 386 LEU   A O   1 
ATOM   2504 C CB  . LEU   A 1 386 ? 134.177 115.814 138.950 1.00 4.88  ? 386 LEU   A CB  1 
ATOM   2505 C CG  . LEU   A 1 386 ? 134.782 114.469 138.559 1.00 6.44  ? 386 LEU   A CG  1 
ATOM   2506 C CD1 . LEU   A 1 386 ? 134.111 113.333 139.313 1.00 6.02  ? 386 LEU   A CD1 1 
ATOM   2507 C CD2 . LEU   A 1 386 ? 134.681 114.264 137.060 1.00 1.42  ? 386 LEU   A CD2 1 
ATOM   2508 N N   . ILE   A 1 387 ? 132.818 118.662 138.468 1.00 8.81  ? 387 ILE   A N   1 
ATOM   2509 C CA  . ILE   A 1 387 ? 131.628 119.429 138.113 1.00 10.07 ? 387 ILE   A CA  1 
ATOM   2510 C C   . ILE   A 1 387 ? 131.953 120.429 137.016 1.00 6.75  ? 387 ILE   A C   1 
ATOM   2511 O O   . ILE   A 1 387 ? 131.106 120.719 136.167 1.00 9.10  ? 387 ILE   A O   1 
ATOM   2512 C CB  . ILE   A 1 387 ? 131.008 120.111 139.349 1.00 7.75  ? 387 ILE   A CB  1 
ATOM   2513 C CG1 . ILE   A 1 387 ? 129.666 120.754 138.990 1.00 13.94 ? 387 ILE   A CG1 1 
ATOM   2514 C CG2 . ILE   A 1 387 ? 131.926 121.170 139.913 1.00 8.88  ? 387 ILE   A CG2 1 
ATOM   2515 C CD1 . ILE   A 1 387 ? 128.559 119.765 138.717 1.00 7.74  ? 387 ILE   A CD1 1 
ATOM   2516 N N   . THR   A 1 388 ? 133.177 120.965 136.995 1.00 5.69  ? 388 THR   A N   1 
ATOM   2517 C CA  . THR   A 1 388 ? 133.579 121.793 135.865 1.00 8.43  ? 388 THR   A CA  1 
ATOM   2518 C C   . THR   A 1 388 ? 133.567 120.988 134.572 1.00 2.26  ? 388 THR   A C   1 
ATOM   2519 O O   . THR   A 1 388 ? 133.054 121.454 133.546 1.00 3.41  ? 388 THR   A O   1 
ATOM   2520 C CB  . THR   A 1 388 ? 134.963 122.390 136.112 1.00 8.55  ? 388 THR   A CB  1 
ATOM   2521 O OG1 . THR   A 1 388 ? 134.997 123.004 137.405 1.00 9.13  ? 388 THR   A OG1 1 
ATOM   2522 C CG2 . THR   A 1 388 ? 135.273 123.431 135.059 1.00 7.78  ? 388 THR   A CG2 1 
ATOM   2523 N N   . ILE   A 1 389 ? 134.109 119.768 134.609 1.00 10.17 ? 389 ILE   A N   1 
ATOM   2524 C CA  . ILE   A 1 389 ? 134.077 118.911 133.426 1.00 3.06  ? 389 ILE   A CA  1 
ATOM   2525 C C   . ILE   A 1 389 ? 132.639 118.587 133.044 1.00 8.41  ? 389 ILE   A C   1 
ATOM   2526 O O   . ILE   A 1 389 ? 132.291 118.551 131.861 1.00 10.55 ? 389 ILE   A O   1 
ATOM   2527 C CB  . ILE   A 1 389 ? 134.900 117.630 133.657 1.00 2.88  ? 389 ILE   A CB  1 
ATOM   2528 C CG1 . ILE   A 1 389 ? 136.362 117.971 133.923 1.00 3.81  ? 389 ILE   A CG1 1 
ATOM   2529 C CG2 . ILE   A 1 389 ? 134.808 116.710 132.451 1.00 6.84  ? 389 ILE   A CG2 1 
ATOM   2530 C CD1 . ILE   A 1 389 ? 137.162 116.791 134.404 1.00 4.82  ? 389 ILE   A CD1 1 
ATOM   2531 N N   . ALA   A 1 390 ? 131.783 118.343 134.038 1.00 10.67 ? 390 ALA   A N   1 
ATOM   2532 C CA  . ALA   A 1 390 ? 130.386 118.020 133.767 1.00 4.34  ? 390 ALA   A CA  1 
ATOM   2533 C C   . ALA   A 1 390 ? 129.682 119.178 133.076 1.00 5.37  ? 390 ALA   A C   1 
ATOM   2534 O O   . ALA   A 1 390 ? 128.990 118.989 132.070 1.00 10.92 ? 390 ALA   A O   1 
ATOM   2535 C CB  . ALA   A 1 390 ? 129.671 117.662 135.070 1.00 13.47 ? 390 ALA   A CB  1 
ATOM   2536 N N   . VAL   A 1 391 ? 129.857 120.390 133.604 1.00 11.63 ? 391 VAL   A N   1 
ATOM   2537 C CA  . VAL   A 1 391 ? 129.219 121.565 133.022 1.00 11.35 ? 391 VAL   A CA  1 
ATOM   2538 C C   . VAL   A 1 391 ? 129.735 121.805 131.610 1.00 3.61  ? 391 VAL   A C   1 
ATOM   2539 O O   . VAL   A 1 391 ? 128.955 122.061 130.684 1.00 3.79  ? 391 VAL   A O   1 
ATOM   2540 C CB  . VAL   A 1 391 ? 129.438 122.789 133.931 1.00 3.06  ? 391 VAL   A CB  1 
ATOM   2541 C CG1 . VAL   A 1 391 ? 128.891 124.031 133.285 1.00 7.76  ? 391 VAL   A CG1 1 
ATOM   2542 C CG2 . VAL   A 1 391 ? 128.769 122.572 135.278 1.00 11.16 ? 391 VAL   A CG2 1 
ATOM   2543 N N   . PHE   A 1 392 ? 131.053 121.701 131.413 1.00 11.66 ? 392 PHE   A N   1 
ATOM   2544 C CA  . PHE   A 1 392 ? 131.624 121.907 130.085 1.00 14.16 ? 392 PHE   A CA  1 
ATOM   2545 C C   . PHE   A 1 392 ? 131.103 120.873 129.092 1.00 8.23  ? 392 PHE   A C   1 
ATOM   2546 O O   . PHE   A 1 392 ? 130.673 121.221 127.985 1.00 14.97 ? 392 PHE   A O   1 
ATOM   2547 C CB  . PHE   A 1 392 ? 133.151 121.858 130.167 1.00 8.22  ? 392 PHE   A CB  1 
ATOM   2548 C CG  . PHE   A 1 392 ? 133.813 121.325 128.927 1.00 6.89  ? 392 PHE   A CG  1 
ATOM   2549 C CD1 . PHE   A 1 392 ? 133.746 122.019 127.730 1.00 10.56 ? 392 PHE   A CD1 1 
ATOM   2550 C CD2 . PHE   A 1 392 ? 134.501 120.125 128.959 1.00 11.89 ? 392 PHE   A CD2 1 
ATOM   2551 C CE1 . PHE   A 1 392 ? 134.356 121.529 126.594 1.00 16.05 ? 392 PHE   A CE1 1 
ATOM   2552 C CE2 . PHE   A 1 392 ? 135.110 119.629 127.824 1.00 7.26  ? 392 PHE   A CE2 1 
ATOM   2553 C CZ  . PHE   A 1 392 ? 135.038 120.332 126.640 1.00 9.08  ? 392 PHE   A CZ  1 
ATOM   2554 N N   . GLN   A 1 393 ? 131.134 119.593 129.474 1.00 11.52 ? 393 GLN   A N   1 
ATOM   2555 C CA  . GLN   A 1 393 ? 130.720 118.527 128.571 1.00 14.37 ? 393 GLN   A CA  1 
ATOM   2556 C C   . GLN   A 1 393 ? 129.236 118.604 128.256 1.00 13.36 ? 393 GLN   A C   1 
ATOM   2557 O O   . GLN   A 1 393 ? 128.828 118.301 127.130 1.00 15.60 ? 393 GLN   A O   1 
ATOM   2558 C CB  . GLN   A 1 393 ? 131.067 117.166 129.173 1.00 13.95 ? 393 GLN   A CB  1 
ATOM   2559 C CG  . GLN   A 1 393 ? 132.554 116.860 129.186 1.00 19.75 ? 393 GLN   A CG  1 
ATOM   2560 C CD  . GLN   A 1 393 ? 133.017 116.174 127.919 1.00 18.37 ? 393 GLN   A CD  1 
ATOM   2561 O OE1 . GLN   A 1 393 ? 132.998 114.948 127.821 1.00 19.08 ? 393 GLN   A OE1 1 
ATOM   2562 N NE2 . GLN   A 1 393 ? 133.436 116.965 126.938 1.00 11.76 ? 393 GLN   A NE2 1 
ATOM   2563 N N   . ILE   A 1 394 ? 128.414 118.998 129.229 1.00 13.35 ? 394 ILE   A N   1 
ATOM   2564 C CA  . ILE   A 1 394 ? 127.002 119.212 128.949 1.00 9.75  ? 394 ILE   A CA  1 
ATOM   2565 C C   . ILE   A 1 394 ? 126.826 120.383 127.991 1.00 16.28 ? 394 ILE   A C   1 
ATOM   2566 O O   . ILE   A 1 394 ? 126.010 120.324 127.065 1.00 7.75  ? 394 ILE   A O   1 
ATOM   2567 C CB  . ILE   A 1 394 ? 126.226 119.420 130.261 1.00 8.66  ? 394 ILE   A CB  1 
ATOM   2568 C CG1 . ILE   A 1 394 ? 126.083 118.091 131.005 1.00 11.36 ? 394 ILE   A CG1 1 
ATOM   2569 C CG2 . ILE   A 1 394 ? 124.861 120.014 129.981 1.00 11.62 ? 394 ILE   A CG2 1 
ATOM   2570 C CD1 . ILE   A 1 394 ? 125.278 118.188 132.278 1.00 10.37 ? 394 ILE   A CD1 1 
ATOM   2571 N N   . ALA   A 1 395 ? 127.600 121.455 128.184 1.00 12.41 ? 395 ALA   A N   1 
ATOM   2572 C CA  . ALA   A 1 395 ? 127.465 122.628 127.327 1.00 12.64 ? 395 ALA   A CA  1 
ATOM   2573 C C   . ALA   A 1 395 ? 127.824 122.314 125.879 1.00 14.63 ? 395 ALA   A C   1 
ATOM   2574 O O   . ALA   A 1 395 ? 127.104 122.714 124.957 1.00 20.96 ? 395 ALA   A O   1 
ATOM   2575 C CB  . ALA   A 1 395 ? 128.332 123.766 127.862 1.00 13.53 ? 395 ALA   A CB  1 
ATOM   2576 N N   . VAL   A 1 396 ? 128.934 121.604 125.652 1.00 15.77 ? 396 VAL   A N   1 
ATOM   2577 C CA  . VAL   A 1 396 ? 129.333 121.312 124.276 1.00 10.88 ? 396 VAL   A CA  1 
ATOM   2578 C C   . VAL   A 1 396 ? 128.392 120.293 123.644 1.00 8.67  ? 396 VAL   A C   1 
ATOM   2579 O O   . VAL   A 1 396 ? 127.995 120.436 122.481 1.00 8.45  ? 396 VAL   A O   1 
ATOM   2580 C CB  . VAL   A 1 396 ? 130.798 120.842 124.207 1.00 9.82  ? 396 VAL   A CB  1 
ATOM   2581 C CG1 . VAL   A 1 396 ? 131.741 122.019 124.351 1.00 12.91 ? 396 VAL   A CG1 1 
ATOM   2582 C CG2 . VAL   A 1 396 ? 131.084 119.781 125.250 1.00 15.85 ? 396 VAL   A CG2 1 
ATOM   2583 N N   . ASN   A 1 397 ? 128.022 119.254 124.388 1.00 23.18 ? 397 ASN   A N   1 
ATOM   2584 C CA  . ASN   A 1 397 ? 127.207 118.178 123.840 1.00 19.42 ? 397 ASN   A CA  1 
ATOM   2585 C C   . ASN   A 1 397 ? 125.719 118.493 123.844 1.00 20.68 ? 397 ASN   A C   1 
ATOM   2586 O O   . ASN   A 1 397 ? 124.935 117.683 123.340 1.00 24.03 ? 397 ASN   A O   1 
ATOM   2587 C CB  . ASN   A 1 397 ? 127.454 116.883 124.618 1.00 24.28 ? 397 ASN   A CB  1 
ATOM   2588 C CG  . ASN   A 1 397 ? 128.917 116.492 124.651 1.00 19.09 ? 397 ASN   A CG  1 
ATOM   2589 O OD1 . ASN   A 1 397 ? 129.693 116.877 123.777 1.00 15.93 ? 397 ASN   A OD1 1 
ATOM   2590 N ND2 . ASN   A 1 397 ? 129.301 115.724 125.663 1.00 16.36 ? 397 ASN   A ND2 1 
ATOM   2591 N N   . LEU   A 1 398 ? 125.313 119.641 124.390 1.00 16.87 ? 398 LEU   A N   1 
ATOM   2592 C CA  . LEU   A 1 398 ? 123.890 119.940 124.512 1.00 12.22 ? 398 LEU   A CA  1 
ATOM   2593 C C   . LEU   A 1 398 ? 123.214 120.033 123.151 1.00 14.31 ? 398 LEU   A C   1 
ATOM   2594 O O   . LEU   A 1 398 ? 122.110 119.510 122.967 1.00 11.42 ? 398 LEU   A O   1 
ATOM   2595 C CB  . LEU   A 1 398 ? 123.695 121.241 125.289 1.00 17.97 ? 398 LEU   A CB  1 
ATOM   2596 C CG  . LEU   A 1 398 ? 122.310 121.492 125.878 1.00 14.53 ? 398 LEU   A CG  1 
ATOM   2597 C CD1 . LEU   A 1 398 ? 121.696 120.197 126.365 1.00 14.77 ? 398 LEU   A CD1 1 
ATOM   2598 C CD2 . LEU   A 1 398 ? 122.425 122.480 127.016 1.00 12.38 ? 398 LEU   A CD2 1 
ATOM   2599 N N   . ASN   A 1 399 ? 123.849 120.724 122.201 1.00 18.79 ? 399 ASN   A N   1 
ATOM   2600 C CA  . ASN   A 1 399 ? 123.344 120.956 120.847 1.00 13.69 ? 399 ASN   A CA  1 
ATOM   2601 C C   . ASN   A 1 399 ? 121.932 121.544 120.855 1.00 16.44 ? 399 ASN   A C   1 
ATOM   2602 O O   . ASN   A 1 399 ? 121.238 121.529 119.834 1.00 17.15 ? 399 ASN   A O   1 
ATOM   2603 C CB  . ASN   A 1 399 ? 123.471 119.673 119.993 1.00 16.51 ? 399 ASN   A CB  1 
ATOM   2604 C CG  . ASN   A 1 399 ? 122.411 118.605 120.286 1.00 14.53 ? 399 ASN   A CG  1 
ATOM   2605 O OD1 . ASN   A 1 399 ? 121.239 118.890 120.526 1.00 18.88 ? 399 ASN   A OD1 1 
ATOM   2606 N ND2 . ASN   A 1 399 ? 122.844 117.350 120.261 1.00 21.55 ? 399 ASN   A ND2 1 
ATOM   2607 N N   . VAL   A 1 400 ? 121.513 122.082 122.004 1.00 20.94 ? 400 VAL   A N   1 
ATOM   2608 C CA  . VAL   A 1 400 ? 120.270 122.828 122.144 1.00 16.48 ? 400 VAL   A CA  1 
ATOM   2609 C C   . VAL   A 1 400 ? 120.574 124.074 122.968 1.00 17.45 ? 400 VAL   A C   1 
ATOM   2610 O O   . VAL   A 1 400 ? 121.459 124.078 123.826 1.00 14.42 ? 400 VAL   A O   1 
ATOM   2611 C CB  . VAL   A 1 400 ? 119.138 122.006 122.808 1.00 13.00 ? 400 VAL   A CB  1 
ATOM   2612 C CG1 . VAL   A 1 400 ? 117.792 122.681 122.598 1.00 12.83 ? 400 VAL   A CG1 1 
ATOM   2613 C CG2 . VAL   A 1 400 ? 119.101 120.585 122.275 1.00 18.83 ? 400 VAL   A CG2 1 
ATOM   2614 N N   . GLU   A 1 401 ? 119.823 125.144 122.693 1.00 39.59 ? 401 GLU   A N   1 
ATOM   2615 C CA  . GLU   A 1 401 ? 120.067 126.420 123.358 1.00 34.04 ? 401 GLU   A CA  1 
ATOM   2616 C C   . GLU   A 1 401 ? 119.778 126.377 124.854 1.00 36.38 ? 401 GLU   A C   1 
ATOM   2617 O O   . GLU   A 1 401 ? 120.203 127.284 125.577 1.00 38.19 ? 401 GLU   A O   1 
ATOM   2618 C CB  . GLU   A 1 401 ? 119.225 127.521 122.711 1.00 33.50 ? 401 GLU   A CB  1 
ATOM   2619 C CG  . GLU   A 1 401 ? 117.730 127.379 122.951 1.00 40.10 ? 401 GLU   A CG  1 
ATOM   2620 C CD  . GLU   A 1 401 ? 117.173 128.477 123.840 1.00 38.45 ? 401 GLU   A CD  1 
ATOM   2621 O OE1 . GLU   A 1 401 ? 117.976 129.210 124.455 1.00 38.40 ? 401 GLU   A OE1 1 
ATOM   2622 O OE2 . GLU   A 1 401 ? 115.934 128.609 123.921 1.00 39.26 ? 401 GLU   A OE2 1 
ATOM   2623 N N   . ARG   A 1 402 ? 119.074 125.353 125.335 1.00 27.05 ? 402 ARG   A N   1 
ATOM   2624 C CA  . ARG   A 1 402 ? 118.665 125.299 126.734 1.00 22.80 ? 402 ARG   A CA  1 
ATOM   2625 C C   . ARG   A 1 402 ? 119.818 124.944 127.663 1.00 25.82 ? 402 ARG   A C   1 
ATOM   2626 O O   . ARG   A 1 402 ? 119.845 123.850 128.236 1.00 21.36 ? 402 ARG   A O   1 
ATOM   2627 C CB  . ARG   A 1 402 ? 117.529 124.291 126.919 1.00 23.72 ? 402 ARG   A CB  1 
ATOM   2628 C CG  . ARG   A 1 402 ? 116.670 124.054 125.693 1.00 26.43 ? 402 ARG   A CG  1 
ATOM   2629 C CD  . ARG   A 1 402 ? 115.836 125.287 125.380 1.00 23.82 ? 402 ARG   A CD  1 
ATOM   2630 N NE  . ARG   A 1 402 ? 115.140 125.779 126.564 1.00 20.21 ? 402 ARG   A NE  1 
ATOM   2631 C CZ  . ARG   A 1 402 ? 114.134 125.157 127.165 1.00 23.38 ? 402 ARG   A CZ  1 
ATOM   2632 N NH1 . ARG   A 1 402 ? 113.643 124.021 126.698 1.00 20.69 ? 402 ARG   A NH1 1 
ATOM   2633 N NH2 . ARG   A 1 402 ? 113.604 125.691 128.261 1.00 20.40 ? 402 ARG   A NH2 1 
ATOM   2634 N N   . TYR   A 1 403 ? 120.766 125.868 127.830 1.00 13.68 ? 403 TYR   A N   1 
ATOM   2635 C CA  . TYR   A 1 403 ? 121.860 125.640 128.769 1.00 9.18  ? 403 TYR   A CA  1 
ATOM   2636 C C   . TYR   A 1 403 ? 121.363 125.626 130.209 1.00 12.45 ? 403 TYR   A C   1 
ATOM   2637 O O   . TYR   A 1 403 ? 121.771 124.771 131.003 1.00 17.04 ? 403 TYR   A O   1 
ATOM   2638 C CB  . TYR   A 1 403 ? 122.940 126.704 128.581 1.00 11.42 ? 403 TYR   A CB  1 
ATOM   2639 C CG  . TYR   A 1 403 ? 123.669 126.590 127.265 1.00 9.47  ? 403 TYR   A CG  1 
ATOM   2640 C CD1 . TYR   A 1 403 ? 124.399 125.452 126.952 1.00 12.27 ? 403 TYR   A CD1 1 
ATOM   2641 C CD2 . TYR   A 1 403 ? 123.616 127.613 126.329 1.00 15.99 ? 403 TYR   A CD2 1 
ATOM   2642 C CE1 . TYR   A 1 403 ? 125.063 125.340 125.748 1.00 16.01 ? 403 TYR   A CE1 1 
ATOM   2643 C CE2 . TYR   A 1 403 ? 124.277 127.509 125.121 1.00 15.86 ? 403 TYR   A CE2 1 
ATOM   2644 C CZ  . TYR   A 1 403 ? 124.998 126.371 124.836 1.00 7.70  ? 403 TYR   A CZ  1 
ATOM   2645 O OH  . TYR   A 1 403 ? 125.659 126.264 123.634 1.00 10.25 ? 403 TYR   A OH  1 
ATOM   2646 N N   . ALA   A 1 404 ? 120.478 126.559 130.565 1.00 3.91  ? 404 ALA   A N   1 
ATOM   2647 C CA  . ALA   A 1 404 ? 119.989 126.633 131.935 1.00 1.17  ? 404 ALA   A CA  1 
ATOM   2648 C C   . ALA   A 1 404 ? 118.886 125.630 132.227 1.00 4.87  ? 404 ALA   A C   1 
ATOM   2649 O O   . ALA   A 1 404 ? 118.585 125.395 133.401 1.00 1.82  ? 404 ALA   A O   1 
ATOM   2650 C CB  . ALA   A 1 404 ? 119.483 128.040 132.248 1.00 1.19  ? 404 ALA   A CB  1 
ATOM   2651 N N   . LEU   A 1 405 ? 118.265 125.046 131.202 1.00 13.08 ? 405 LEU   A N   1 
ATOM   2652 C CA  . LEU   A 1 405 ? 117.295 123.990 131.460 1.00 11.34 ? 405 LEU   A CA  1 
ATOM   2653 C C   . LEU   A 1 405 ? 117.984 122.743 131.994 1.00 8.40  ? 405 LEU   A C   1 
ATOM   2654 O O   . LEU   A 1 405 ? 117.569 122.182 133.013 1.00 15.24 ? 405 LEU   A O   1 
ATOM   2655 C CB  . LEU   A 1 405 ? 116.501 123.666 130.196 1.00 8.27  ? 405 LEU   A CB  1 
ATOM   2656 C CG  . LEU   A 1 405 ? 115.824 122.295 130.217 1.00 12.84 ? 405 LEU   A CG  1 
ATOM   2657 C CD1 . LEU   A 1 405 ? 114.528 122.355 131.001 1.00 13.86 ? 405 LEU   A CD1 1 
ATOM   2658 C CD2 . LEU   A 1 405 ? 115.574 121.791 128.806 1.00 12.08 ? 405 LEU   A CD2 1 
ATOM   2659 N N   . VAL   A 1 406 ? 119.053 122.305 131.326 1.00 10.53 ? 406 VAL   A N   1 
ATOM   2660 C CA  . VAL   A 1 406 ? 119.780 121.131 131.795 1.00 5.43  ? 406 VAL   A CA  1 
ATOM   2661 C C   . VAL   A 1 406 ? 120.524 121.445 133.084 1.00 7.32  ? 406 VAL   A C   1 
ATOM   2662 O O   . VAL   A 1 406 ? 120.527 120.642 134.021 1.00 10.11 ? 406 VAL   A O   1 
ATOM   2663 C CB  . VAL   A 1 406 ? 120.728 120.610 130.703 1.00 8.19  ? 406 VAL   A CB  1 
ATOM   2664 C CG1 . VAL   A 1 406 ? 121.575 119.473 131.243 1.00 10.88 ? 406 VAL   A CG1 1 
ATOM   2665 C CG2 . VAL   A 1 406 ? 119.932 120.143 129.507 1.00 12.76 ? 406 VAL   A CG2 1 
ATOM   2666 N N   . PHE   A 1 407 ? 121.166 122.613 133.157 1.00 5.39  ? 407 PHE   A N   1 
ATOM   2667 C CA  . PHE   A 1 407 ? 121.805 123.013 134.407 1.00 12.52 ? 407 PHE   A CA  1 
ATOM   2668 C C   . PHE   A 1 407 ? 120.771 123.188 135.511 1.00 7.32  ? 407 PHE   A C   1 
ATOM   2669 O O   . PHE   A 1 407 ? 120.966 122.720 136.639 1.00 12.92 ? 407 PHE   A O   1 
ATOM   2670 C CB  . PHE   A 1 407 ? 122.596 124.312 134.223 1.00 9.66  ? 407 PHE   A CB  1 
ATOM   2671 C CG  . PHE   A 1 407 ? 123.764 124.206 133.274 1.00 11.39 ? 407 PHE   A CG  1 
ATOM   2672 C CD1 . PHE   A 1 407 ? 124.033 123.038 132.582 1.00 8.63  ? 407 PHE   A CD1 1 
ATOM   2673 C CD2 . PHE   A 1 407 ? 124.600 125.291 133.082 1.00 8.80  ? 407 PHE   A CD2 1 
ATOM   2674 C CE1 . PHE   A 1 407 ? 125.104 122.959 131.718 1.00 6.76  ? 407 PHE   A CE1 1 
ATOM   2675 C CE2 . PHE   A 1 407 ? 125.671 125.217 132.217 1.00 4.78  ? 407 PHE   A CE2 1 
ATOM   2676 C CZ  . PHE   A 1 407 ? 125.922 124.049 131.534 1.00 7.32  ? 407 PHE   A CZ  1 
ATOM   2677 N N   . GLY   A 1 408 ? 119.657 123.851 135.197 1.00 11.18 ? 408 GLY   A N   1 
ATOM   2678 C CA  . GLY   A 1 408 ? 118.638 124.088 136.206 1.00 9.36  ? 408 GLY   A CA  1 
ATOM   2679 C C   . GLY   A 1 408 ? 117.963 122.814 136.672 1.00 11.78 ? 408 GLY   A C   1 
ATOM   2680 O O   . GLY   A 1 408 ? 117.766 122.610 137.871 1.00 10.84 ? 408 GLY   A O   1 
ATOM   2681 N N   . ILE   A 1 409 ? 117.597 121.936 135.734 1.00 14.25 ? 409 ILE   A N   1 
ATOM   2682 C CA  . ILE   A 1 409 ? 116.953 120.692 136.142 1.00 6.31  ? 409 ILE   A CA  1 
ATOM   2683 C C   . ILE   A 1 409 ? 117.958 119.778 136.831 1.00 7.33  ? 409 ILE   A C   1 
ATOM   2684 O O   . ILE   A 1 409 ? 117.593 119.018 137.732 1.00 12.53 ? 409 ILE   A O   1 
ATOM   2685 C CB  . ILE   A 1 409 ? 116.267 120.000 134.947 1.00 14.69 ? 409 ILE   A CB  1 
ATOM   2686 C CG1 . ILE   A 1 409 ? 115.212 119.011 135.445 1.00 8.01  ? 409 ILE   A CG1 1 
ATOM   2687 C CG2 . ILE   A 1 409 ? 117.271 119.272 134.075 1.00 5.71  ? 409 ILE   A CG2 1 
ATOM   2688 C CD1 . ILE   A 1 409 ? 114.101 118.754 134.451 1.00 15.10 ? 409 ILE   A CD1 1 
ATOM   2689 N N   . ASN   A 1 410 ? 119.234 119.850 136.444 1.00 6.79  ? 410 ASN   A N   1 
ATOM   2690 C CA  . ASN   A 1 410 ? 120.267 119.092 137.138 1.00 3.08  ? 410 ASN   A CA  1 
ATOM   2691 C C   . ASN   A 1 410 ? 120.382 119.539 138.585 1.00 4.70  ? 410 ASN   A C   1 
ATOM   2692 O O   . ASN   A 1 410 ? 120.403 118.713 139.503 1.00 5.96  ? 410 ASN   A O   1 
ATOM   2693 C CB  . ASN   A 1 410 ? 121.607 119.258 136.424 1.00 3.71  ? 410 ASN   A CB  1 
ATOM   2694 C CG  . ASN   A 1 410 ? 121.828 118.215 135.359 1.00 8.72  ? 410 ASN   A CG  1 
ATOM   2695 O OD1 . ASN   A 1 410 ? 121.245 117.133 135.405 1.00 7.23  ? 410 ASN   A OD1 1 
ATOM   2696 N ND2 . ASN   A 1 410 ? 122.669 118.534 134.384 1.00 9.51  ? 410 ASN   A ND2 1 
ATOM   2697 N N   . THR   A 1 411 ? 120.442 120.853 138.808 1.00 6.34  ? 411 THR   A N   1 
ATOM   2698 C CA  . THR   A 1 411 ? 120.527 121.366 140.168 1.00 12.20 ? 411 THR   A CA  1 
ATOM   2699 C C   . THR   A 1 411 ? 119.252 121.081 140.951 1.00 7.62  ? 411 THR   A C   1 
ATOM   2700 O O   . THR   A 1 411 ? 119.319 120.801 142.150 1.00 9.26  ? 411 THR   A O   1 
ATOM   2701 C CB  . THR   A 1 411 ? 120.823 122.865 140.148 1.00 10.20 ? 411 THR   A CB  1 
ATOM   2702 O OG1 . THR   A 1 411 ? 121.930 123.118 139.274 1.00 10.93 ? 411 THR   A OG1 1 
ATOM   2703 C CG2 . THR   A 1 411 ? 121.178 123.355 141.543 1.00 6.79  ? 411 THR   A CG2 1 
ATOM   2704 N N   . PHE   A 1 412 ? 118.091 121.121 140.294 1.00 4.84  ? 412 PHE   A N   1 
ATOM   2705 C CA  . PHE   A 1 412 ? 116.839 120.834 140.987 1.00 8.53  ? 412 PHE   A CA  1 
ATOM   2706 C C   . PHE   A 1 412 ? 116.758 119.371 141.407 1.00 7.54  ? 412 PHE   A C   1 
ATOM   2707 O O   . PHE   A 1 412 ? 116.369 119.069 142.540 1.00 9.77  ? 412 PHE   A O   1 
ATOM   2708 C CB  . PHE   A 1 412 ? 115.651 121.206 140.100 1.00 10.16 ? 412 PHE   A CB  1 
ATOM   2709 C CG  . PHE   A 1 412 ? 114.318 120.859 140.697 1.00 2.15  ? 412 PHE   A CG  1 
ATOM   2710 C CD1 . PHE   A 1 412 ? 113.738 121.680 141.649 1.00 2.64  ? 412 PHE   A CD1 1 
ATOM   2711 C CD2 . PHE   A 1 412 ? 113.642 119.716 140.305 1.00 7.52  ? 412 PHE   A CD2 1 
ATOM   2712 C CE1 . PHE   A 1 412 ? 112.511 121.366 142.201 1.00 7.84  ? 412 PHE   A CE1 1 
ATOM   2713 C CE2 . PHE   A 1 412 ? 112.416 119.397 140.853 1.00 6.39  ? 412 PHE   A CE2 1 
ATOM   2714 C CZ  . PHE   A 1 412 ? 111.849 120.223 141.802 1.00 9.13  ? 412 PHE   A CZ  1 
ATOM   2715 N N   . ILE   A 1 413 ? 117.121 118.449 140.514 1.00 5.25  ? 413 ILE   A N   1 
ATOM   2716 C CA  . ILE   A 1 413 ? 117.106 117.031 140.860 1.00 6.12  ? 413 ILE   A CA  1 
ATOM   2717 C C   . ILE   A 1 413 ? 118.166 116.730 141.912 1.00 7.67  ? 413 ILE   A C   1 
ATOM   2718 O O   . ILE   A 1 413 ? 117.945 115.924 142.825 1.00 5.88  ? 413 ILE   A O   1 
ATOM   2719 C CB  . ILE   A 1 413 ? 117.291 116.174 139.595 1.00 8.18  ? 413 ILE   A CB  1 
ATOM   2720 C CG1 . ILE   A 1 413 ? 116.103 116.358 138.649 1.00 9.55  ? 413 ILE   A CG1 1 
ATOM   2721 C CG2 . ILE   A 1 413 ? 117.452 114.707 139.954 1.00 4.93  ? 413 ILE   A CG2 1 
ATOM   2722 C CD1 . ILE   A 1 413 ? 114.836 115.671 139.111 1.00 7.58  ? 413 ILE   A CD1 1 
ATOM   2723 N N   . ALA   A 1 414 ? 119.328 117.380 141.811 1.00 13.68 ? 414 ALA   A N   1 
ATOM   2724 C CA  . ALA   A 1 414 ? 120.367 117.203 142.816 1.00 6.99  ? 414 ALA   A CA  1 
ATOM   2725 C C   . ALA   A 1 414 ? 119.907 117.703 144.176 1.00 4.11  ? 414 ALA   A C   1 
ATOM   2726 O O   . ALA   A 1 414 ? 120.164 117.062 145.197 1.00 11.93 ? 414 ALA   A O   1 
ATOM   2727 C CB  . ALA   A 1 414 ? 121.639 117.926 142.382 1.00 8.79  ? 414 ALA   A CB  1 
ATOM   2728 N N   . LEU   A 1 415 ? 119.218 118.843 144.211 1.00 3.30  ? 415 LEU   A N   1 
ATOM   2729 C CA  . LEU   A 1 415 ? 118.697 119.356 145.470 1.00 11.68 ? 415 LEU   A CA  1 
ATOM   2730 C C   . LEU   A 1 415 ? 117.581 118.474 146.011 1.00 6.82  ? 415 LEU   A C   1 
ATOM   2731 O O   . LEU   A 1 415 ? 117.460 118.314 147.228 1.00 12.07 ? 415 LEU   A O   1 
ATOM   2732 C CB  . LEU   A 1 415 ? 118.213 120.792 145.285 1.00 6.80  ? 415 LEU   A CB  1 
ATOM   2733 C CG  . LEU   A 1 415 ? 117.761 121.539 146.537 1.00 3.55  ? 415 LEU   A CG  1 
ATOM   2734 C CD1 . LEU   A 1 415 ? 118.946 121.847 147.435 1.00 5.23  ? 415 LEU   A CD1 1 
ATOM   2735 C CD2 . LEU   A 1 415 ? 117.052 122.815 146.138 1.00 6.28  ? 415 LEU   A CD2 1 
ATOM   2736 N N   . VAL   A 1 416 ? 116.767 117.889 145.130 1.00 8.87  ? 416 VAL   A N   1 
ATOM   2737 C CA  . VAL   A 1 416 ? 115.735 116.954 145.572 1.00 3.21  ? 416 VAL   A CA  1 
ATOM   2738 C C   . VAL   A 1 416 ? 116.374 115.738 146.232 1.00 5.67  ? 416 VAL   A C   1 
ATOM   2739 O O   . VAL   A 1 416 ? 115.962 115.306 147.316 1.00 10.09 ? 416 VAL   A O   1 
ATOM   2740 C CB  . VAL   A 1 416 ? 114.839 116.548 144.388 1.00 6.70  ? 416 VAL   A CB  1 
ATOM   2741 C CG1 . VAL   A 1 416 ? 114.172 115.207 144.654 1.00 2.39  ? 416 VAL   A CG1 1 
ATOM   2742 C CG2 . VAL   A 1 416 ? 113.798 117.619 144.116 1.00 1.60  ? 416 VAL   A CG2 1 
ATOM   2743 N N   . ILE   A 1 417 ? 117.401 115.176 145.592 1.00 7.03  ? 417 ILE   A N   1 
ATOM   2744 C CA  . ILE   A 1 417 ? 118.081 114.012 146.153 1.00 9.76  ? 417 ILE   A CA  1 
ATOM   2745 C C   . ILE   A 1 417 ? 118.799 114.381 147.445 1.00 7.82  ? 417 ILE   A C   1 
ATOM   2746 O O   . ILE   A 1 417 ? 118.808 113.607 148.409 1.00 7.62  ? 417 ILE   A O   1 
ATOM   2747 C CB  . ILE   A 1 417 ? 119.040 113.402 145.113 1.00 6.73  ? 417 ILE   A CB  1 
ATOM   2748 C CG1 . ILE   A 1 417 ? 118.253 112.590 144.084 1.00 7.93  ? 417 ILE   A CG1 1 
ATOM   2749 C CG2 . ILE   A 1 417 ? 120.086 112.526 145.782 1.00 0.37  ? 417 ILE   A CG2 1 
ATOM   2750 C CD1 . ILE   A 1 417 ? 118.786 112.699 142.679 1.00 2.62  ? 417 ILE   A CD1 1 
ATOM   2751 N N   . GLN   A 1 418 ? 119.404 115.570 147.491 1.00 10.06 ? 418 GLN   A N   1 
ATOM   2752 C CA  . GLN   A 1 418 ? 120.079 116.020 148.702 1.00 11.78 ? 418 GLN   A CA  1 
ATOM   2753 C C   . GLN   A 1 418 ? 119.096 116.191 149.851 1.00 9.86  ? 418 GLN   A C   1 
ATOM   2754 O O   . GLN   A 1 418 ? 119.386 115.800 150.984 1.00 4.87  ? 418 GLN   A O   1 
ATOM   2755 C CB  . GLN   A 1 418 ? 120.821 117.328 148.431 1.00 12.47 ? 418 GLN   A CB  1 
ATOM   2756 C CG  . GLN   A 1 418 ? 121.277 118.056 149.682 1.00 12.14 ? 418 GLN   A CG  1 
ATOM   2757 C CD  . GLN   A 1 418 ? 121.628 119.504 149.413 1.00 3.98  ? 418 GLN   A CD  1 
ATOM   2758 O OE1 . GLN   A 1 418 ? 121.624 119.952 148.267 1.00 5.04  ? 418 GLN   A OE1 1 
ATOM   2759 N NE2 . GLN   A 1 418 ? 121.935 120.245 150.471 1.00 5.86  ? 418 GLN   A NE2 1 
ATOM   2760 N N   . THR   A 1 419 ? 117.923 116.765 149.577 1.00 14.14 ? 419 THR   A N   1 
ATOM   2761 C CA  . THR   A 1 419 ? 116.905 116.911 150.610 1.00 15.35 ? 419 THR   A CA  1 
ATOM   2762 C C   . THR   A 1 419 ? 116.388 115.554 151.071 1.00 12.54 ? 419 THR   A C   1 
ATOM   2763 O O   . THR   A 1 419 ? 116.171 115.342 152.269 1.00 8.75  ? 419 THR   A O   1 
ATOM   2764 C CB  . THR   A 1 419 ? 115.756 117.778 150.095 1.00 10.90 ? 419 THR   A CB  1 
ATOM   2765 O OG1 . THR   A 1 419 ? 116.273 119.033 149.634 1.00 8.13  ? 419 THR   A OG1 1 
ATOM   2766 C CG2 . THR   A 1 419 ? 114.741 118.032 151.198 1.00 15.93 ? 419 THR   A CG2 1 
ATOM   2767 N N   . ILE   A 1 420 ? 116.189 114.623 150.137 1.00 16.79 ? 420 ILE   A N   1 
ATOM   2768 C CA  . ILE   A 1 420 ? 115.702 113.293 150.497 1.00 14.25 ? 420 ILE   A CA  1 
ATOM   2769 C C   . ILE   A 1 420 ? 116.716 112.578 151.387 1.00 13.68 ? 420 ILE   A C   1 
ATOM   2770 O O   . ILE   A 1 420 ? 116.367 112.007 152.430 1.00 10.12 ? 420 ILE   A O   1 
ATOM   2771 C CB  . ILE   A 1 420 ? 115.385 112.484 149.226 1.00 12.33 ? 420 ILE   A CB  1 
ATOM   2772 C CG1 . ILE   A 1 420 ? 113.971 112.799 148.734 1.00 10.35 ? 420 ILE   A CG1 1 
ATOM   2773 C CG2 . ILE   A 1 420 ? 115.536 110.995 149.473 1.00 16.97 ? 420 ILE   A CG2 1 
ATOM   2774 C CD1 . ILE   A 1 420 ? 113.773 112.550 147.256 1.00 14.59 ? 420 ILE   A CD1 1 
ATOM   2775 N N   . MET   A 1 421 ? 117.991 112.618 151.000 1.00 20.34 ? 421 MET   A N   1 
ATOM   2776 C CA  . MET   A 1 421 ? 119.029 111.967 151.786 1.00 20.31 ? 421 MET   A CA  1 
ATOM   2777 C C   . MET   A 1 421 ? 119.350 112.725 153.067 1.00 20.67 ? 421 MET   A C   1 
ATOM   2778 O O   . MET   A 1 421 ? 119.898 112.131 153.997 1.00 21.16 ? 421 MET   A O   1 
ATOM   2779 C CB  . MET   A 1 421 ? 120.290 111.782 150.938 1.00 21.95 ? 421 MET   A CB  1 
ATOM   2780 C CG  . MET   A 1 421 ? 121.288 112.919 151.017 1.00 21.04 ? 421 MET   A CG  1 
ATOM   2781 S SD  . MET   A 1 421 ? 122.793 112.554 150.095 1.00 24.86 ? 421 MET   A SD  1 
ATOM   2782 C CE  . MET   A 1 421 ? 123.232 110.959 150.781 1.00 18.42 ? 421 MET   A CE  1 
ATOM   2783 N N   . THR   A 1 422 ? 119.009 114.012 153.143 1.00 11.08 ? 422 THR   A N   1 
ATOM   2784 C CA  . THR   A 1 422 ? 119.070 114.724 154.413 1.00 15.26 ? 422 THR   A CA  1 
ATOM   2785 C C   . THR   A 1 422 ? 117.949 114.270 155.336 1.00 17.23 ? 422 THR   A C   1 
ATOM   2786 O O   . THR   A 1 422 ? 118.153 114.117 156.546 1.00 15.83 ? 422 THR   A O   1 
ATOM   2787 C CB  . THR   A 1 422 ? 118.983 116.232 154.171 1.00 10.21 ? 422 THR   A CB  1 
ATOM   2788 O OG1 . THR   A 1 422 ? 120.012 116.636 153.260 1.00 10.13 ? 422 THR   A OG1 1 
ATOM   2789 C CG2 . THR   A 1 422 ? 119.136 117.000 155.474 1.00 9.71  ? 422 THR   A CG2 1 
ATOM   2790 N N   . VAL   A 1 423 ? 116.760 114.047 154.776 1.00 22.27 ? 423 VAL   A N   1 
ATOM   2791 C CA  . VAL   A 1 423 ? 115.636 113.557 155.568 1.00 15.82 ? 423 VAL   A CA  1 
ATOM   2792 C C   . VAL   A 1 423 ? 115.952 112.179 156.134 1.00 21.03 ? 423 VAL   A C   1 
ATOM   2793 O O   . VAL   A 1 423 ? 115.711 111.902 157.315 1.00 16.06 ? 423 VAL   A O   1 
ATOM   2794 C CB  . VAL   A 1 423 ? 114.350 113.542 154.723 1.00 13.78 ? 423 VAL   A CB  1 
ATOM   2795 C CG1 . VAL   A 1 423 ? 113.273 112.712 155.402 1.00 20.78 ? 423 VAL   A CG1 1 
ATOM   2796 C CG2 . VAL   A 1 423 ? 113.858 114.961 154.486 1.00 20.71 ? 423 VAL   A CG2 1 
ATOM   2797 N N   . ILE   A 1 424 ? 116.510 111.297 155.306 1.00 12.55 ? 424 ILE   A N   1 
ATOM   2798 C CA  . ILE   A 1 424 ? 116.793 109.937 155.764 1.00 14.93 ? 424 ILE   A CA  1 
ATOM   2799 C C   . ILE   A 1 424 ? 118.028 109.902 156.659 1.00 21.14 ? 424 ILE   A C   1 
ATOM   2800 O O   . ILE   A 1 424 ? 117.977 109.415 157.794 1.00 13.29 ? 424 ILE   A O   1 
ATOM   2801 C CB  . ILE   A 1 424 ? 116.941 108.971 154.574 1.00 12.53 ? 424 ILE   A CB  1 
ATOM   2802 C CG1 . ILE   A 1 424 ? 115.815 109.168 153.562 1.00 17.61 ? 424 ILE   A CG1 1 
ATOM   2803 C CG2 . ILE   A 1 424 ? 116.976 107.530 155.059 1.00 20.97 ? 424 ILE   A CG2 1 
ATOM   2804 C CD1 . ILE   A 1 424 ? 116.199 108.772 152.160 1.00 13.00 ? 424 ILE   A CD1 1 
ATOM   2805 N N   . VAL   A 1 425 ? 119.155 110.415 156.162 1.00 17.79 ? 425 VAL   A N   1 
ATOM   2806 C CA  . VAL   A 1 425 ? 120.444 110.152 156.795 1.00 19.50 ? 425 VAL   A CA  1 
ATOM   2807 C C   . VAL   A 1 425 ? 120.551 110.859 158.143 1.00 14.37 ? 425 VAL   A C   1 
ATOM   2808 O O   . VAL   A 1 425 ? 120.888 110.239 159.158 1.00 12.77 ? 425 VAL   A O   1 
ATOM   2809 C CB  . VAL   A 1 425 ? 121.591 110.560 155.851 1.00 21.53 ? 425 VAL   A CB  1 
ATOM   2810 C CG1 . VAL   A 1 425 ? 122.851 110.890 156.640 1.00 13.01 ? 425 VAL   A CG1 1 
ATOM   2811 C CG2 . VAL   A 1 425 ? 121.860 109.460 154.837 1.00 15.23 ? 425 VAL   A CG2 1 
ATOM   2812 N N   . VAL   A 1 426 ? 120.257 112.157 158.183 1.00 16.42 ? 426 VAL   A N   1 
ATOM   2813 C CA  . VAL   A 1 426 ? 120.623 112.958 159.348 1.00 12.76 ? 426 VAL   A CA  1 
ATOM   2814 C C   . VAL   A 1 426 ? 119.394 113.487 160.078 1.00 10.00 ? 426 VAL   A C   1 
ATOM   2815 O O   . VAL   A 1 426 ? 119.416 113.656 161.303 1.00 15.66 ? 426 VAL   A O   1 
ATOM   2816 C CB  . VAL   A 1 426 ? 121.564 114.107 158.935 1.00 12.98 ? 426 VAL   A CB  1 
ATOM   2817 C CG1 . VAL   A 1 426 ? 120.941 114.929 157.829 1.00 11.42 ? 426 VAL   A CG1 1 
ATOM   2818 C CG2 . VAL   A 1 426 ? 121.909 114.988 160.128 1.00 19.61 ? 426 VAL   A CG2 1 
ATOM   2819 N N   . ASP   A 1 427 ? 118.309 113.729 159.349 1.00 24.27 ? 427 ASP   A N   1 
ATOM   2820 C CA  . ASP   A 1 427 ? 117.131 114.324 159.964 1.00 29.90 ? 427 ASP   A CA  1 
ATOM   2821 C C   . ASP   A 1 427 ? 116.511 113.373 160.982 1.00 31.53 ? 427 ASP   A C   1 
ATOM   2822 O O   . ASP   A 1 427 ? 116.581 112.149 160.850 1.00 31.21 ? 427 ASP   A O   1 
ATOM   2823 C CB  . ASP   A 1 427 ? 116.098 114.700 158.904 1.00 24.47 ? 427 ASP   A CB  1 
ATOM   2824 C CG  . ASP   A 1 427 ? 115.618 116.131 159.042 1.00 24.99 ? 427 ASP   A CG  1 
ATOM   2825 O OD1 . ASP   A 1 427 ? 115.969 116.783 160.048 1.00 22.81 ? 427 ASP   A OD1 1 
ATOM   2826 O OD2 . ASP   A 1 427 ? 114.892 116.606 158.144 1.00 31.94 ? 427 ASP   A OD2 1 
ATOM   2827 N N   . GLN   A 1 428 ? 115.905 113.961 162.016 1.00 44.29 ? 428 GLN   A N   1 
ATOM   2828 C CA  . GLN   A 1 428 ? 115.285 113.167 163.073 1.00 41.38 ? 428 GLN   A CA  1 
ATOM   2829 C C   . GLN   A 1 428 ? 114.149 112.313 162.524 1.00 36.52 ? 428 GLN   A C   1 
ATOM   2830 O O   . GLN   A 1 428 ? 113.883 111.213 163.023 1.00 37.16 ? 428 GLN   A O   1 
ATOM   2831 C CB  . GLN   A 1 428 ? 114.787 114.090 164.188 1.00 41.19 ? 428 GLN   A CB  1 
ATOM   2832 C CG  . GLN   A 1 428 ? 114.050 113.385 165.315 1.00 37.94 ? 428 GLN   A CG  1 
ATOM   2833 C CD  . GLN   A 1 428 ? 112.570 113.712 165.336 1.00 38.42 ? 428 GLN   A CD  1 
ATOM   2834 O OE1 . GLN   A 1 428 ? 112.087 114.507 164.530 1.00 37.13 ? 428 GLN   A OE1 1 
ATOM   2835 N NE2 . GLN   A 1 428 ? 111.842 113.099 166.262 1.00 37.32 ? 428 GLN   A NE2 1 
ATOM   2836 N N   . ARG   A 1 429 ? 113.467 112.805 161.486 1.00 48.55 ? 429 ARG   A N   1 
ATOM   2837 C CA  . ARG   A 1 429 ? 112.369 112.051 160.890 1.00 49.01 ? 429 ARG   A CA  1 
ATOM   2838 C C   . ARG   A 1 429 ? 112.846 110.738 160.286 1.00 49.03 ? 429 ARG   A C   1 
ATOM   2839 O O   . ARG   A 1 429 ? 112.119 109.738 160.319 1.00 53.89 ? 429 ARG   A O   1 
ATOM   2840 C CB  . ARG   A 1 429 ? 111.669 112.897 159.825 1.00 45.21 ? 429 ARG   A CB  1 
ATOM   2841 C CG  . ARG   A 1 429 ? 111.160 114.238 160.328 1.00 51.48 ? 429 ARG   A CG  1 
ATOM   2842 C CD  . ARG   A 1 429 ? 111.582 115.368 159.404 1.00 51.85 ? 429 ARG   A CD  1 
ATOM   2843 N NE  . ARG   A 1 429 ? 110.875 115.322 158.130 1.00 49.76 ? 429 ARG   A NE  1 
ATOM   2844 C CZ  . ARG   A 1 429 ? 111.061 116.182 157.138 1.00 48.54 ? 429 ARG   A CZ  1 
ATOM   2845 N NH1 . ARG   A 1 429 ? 111.929 117.175 157.238 1.00 52.85 ? 429 ARG   A NH1 1 
ATOM   2846 N NH2 . ARG   A 1 429 ? 110.357 116.044 156.018 1.00 52.20 ? 429 ARG   A NH2 1 
ATOM   2847 N N   . GLY   A 1 430 ? 114.054 110.717 159.734 1.00 41.51 ? 430 GLY   A N   1 
ATOM   2848 C CA  . GLY   A 1 430 ? 114.608 109.529 159.121 1.00 50.64 ? 430 GLY   A CA  1 
ATOM   2849 C C   . GLY   A 1 430 ? 115.432 108.704 160.087 1.00 41.08 ? 430 GLY   A C   1 
ATOM   2850 O O   . GLY   A 1 430 ? 115.086 108.534 161.259 1.00 46.74 ? 430 GLY   A O   1 
ATOM   2851 N N   . LEU   A 1 431 ? 116.544 108.180 159.576 1.00 24.05 ? 431 LEU   A N   1 
ATOM   2852 C CA  . LEU   A 1 431 ? 117.433 107.339 160.366 1.00 26.67 ? 431 LEU   A CA  1 
ATOM   2853 C C   . LEU   A 1 431 ? 118.104 108.090 161.508 1.00 22.18 ? 431 LEU   A C   1 
ATOM   2854 O O   . LEU   A 1 431 ? 118.367 107.480 162.551 1.00 19.24 ? 431 LEU   A O   1 
ATOM   2855 C CB  . LEU   A 1 431 ? 118.506 106.721 159.467 1.00 24.15 ? 431 LEU   A CB  1 
ATOM   2856 C CG  . LEU   A 1 431 ? 118.028 105.889 158.277 1.00 18.58 ? 431 LEU   A CG  1 
ATOM   2857 C CD1 . LEU   A 1 431 ? 119.209 105.457 157.423 1.00 21.95 ? 431 LEU   A CD1 1 
ATOM   2858 C CD2 . LEU   A 1 431 ? 117.236 104.682 158.747 1.00 28.18 ? 431 LEU   A CD2 1 
ATOM   2859 N N   . ASN   A 1 432 ? 118.380 109.382 161.285 1.00 21.46 ? 432 ASN   A N   1 
ATOM   2860 C CA  . ASN   A 1 432 ? 119.073 110.259 162.268 1.00 14.30 ? 432 ASN   A CA  1 
ATOM   2861 C C   . ASN   A 1 432 ? 120.436 109.637 162.599 1.00 20.76 ? 432 ASN   A C   1 
ATOM   2862 O O   . ASN   A 1 432 ? 120.681 109.341 163.785 1.00 20.89 ? 432 ASN   A O   1 
ATOM   2863 C CB  . ASN   A 1 432 ? 118.220 110.543 163.509 1.00 22.06 ? 432 ASN   A CB  1 
ATOM   2864 C CG  . ASN   A 1 432 ? 118.906 111.459 164.500 1.00 15.02 ? 432 ASN   A CG  1 
ATOM   2865 O OD1 . ASN   A 1 432 ? 118.355 111.764 165.555 1.00 17.77 ? 432 ASN   A OD1 1 
ATOM   2866 N ND2 . ASN   A 1 432 ? 120.108 111.902 164.170 1.00 21.05 ? 432 ASN   A ND2 1 
ATOM   2867 N N   . LEU   A 1 433 ? 121.283 109.463 161.578 1.00 14.91 ? 433 LEU   A N   1 
ATOM   2868 C CA  . LEU   A 1 433 ? 122.598 108.859 161.750 1.00 14.17 ? 433 LEU   A CA  1 
ATOM   2869 C C   . LEU   A 1 433 ? 123.546 109.858 162.399 1.00 14.75 ? 433 LEU   A C   1 
ATOM   2870 O O   . LEU   A 1 433 ? 123.593 111.019 161.976 1.00 10.62 ? 433 LEU   A O   1 
ATOM   2871 C CB  . LEU   A 1 433 ? 123.164 108.404 160.414 1.00 8.49  ? 433 LEU   A CB  1 
ATOM   2872 C CG  . LEU   A 1 433 ? 122.305 107.388 159.661 1.00 15.60 ? 433 LEU   A CG  1 
ATOM   2873 C CD1 . LEU   A 1 433 ? 122.992 106.948 158.384 1.00 11.50 ? 433 LEU   A CD1 1 
ATOM   2874 C CD2 . LEU   A 1 433 ? 122.000 106.191 160.548 1.00 12.00 ? 433 LEU   A CD2 1 
ATOM   2875 N N   . PRO   A 1 434 ? 124.300 109.459 163.426 1.00 19.14 ? 434 PRO   A N   1 
ATOM   2876 C CA  . PRO   A 1 434 ? 125.306 110.366 163.993 1.00 19.59 ? 434 PRO   A CA  1 
ATOM   2877 C C   . PRO   A 1 434 ? 126.346 110.764 162.960 1.00 15.05 ? 434 PRO   A C   1 
ATOM   2878 O O   . PRO   A 1 434 ? 126.471 110.118 161.915 1.00 21.28 ? 434 PRO   A O   1 
ATOM   2879 C CB  . PRO   A 1 434 ? 125.923 109.537 165.127 1.00 16.82 ? 434 PRO   A CB  1 
ATOM   2880 C CG  . PRO   A 1 434 ? 124.846 108.573 165.505 1.00 19.33 ? 434 PRO   A CG  1 
ATOM   2881 C CD  . PRO   A 1 434 ? 124.181 108.215 164.206 1.00 22.68 ? 434 PRO   A CD  1 
ATOM   2882 N N   . VAL   A 1 435 ? 127.101 111.825 163.237 1.00 20.07 ? 435 VAL   A N   1 
ATOM   2883 C CA  . VAL   A 1 435 ? 128.080 112.350 162.296 1.00 18.01 ? 435 VAL   A CA  1 
ATOM   2884 C C   . VAL   A 1 435 ? 129.258 111.408 162.099 1.00 20.61 ? 435 VAL   A C   1 
ATOM   2885 O O   . VAL   A 1 435 ? 130.017 111.575 161.139 1.00 19.44 ? 435 VAL   A O   1 
ATOM   2886 C CB  . VAL   A 1 435 ? 128.572 113.746 162.729 1.00 18.94 ? 435 VAL   A CB  1 
ATOM   2887 C CG1 . VAL   A 1 435 ? 129.146 114.504 161.544 1.00 21.74 ? 435 VAL   A CG1 1 
ATOM   2888 C CG2 . VAL   A 1 435 ? 127.438 114.524 163.375 1.00 23.66 ? 435 VAL   A CG2 1 
ATOM   2889 N N   . SER   A 1 436 ? 129.421 110.411 162.965 1.00 24.10 ? 436 SER   A N   1 
ATOM   2890 C CA  . SER   A 1 436 ? 130.478 109.418 162.839 1.00 20.19 ? 436 SER   A CA  1 
ATOM   2891 C C   . SER   A 1 436 ? 130.118 108.291 161.878 1.00 25.00 ? 436 SER   A C   1 
ATOM   2892 O O   . SER   A 1 436 ? 130.946 107.407 161.641 1.00 21.75 ? 436 SER   A O   1 
ATOM   2893 C CB  . SER   A 1 436 ? 130.818 108.838 164.214 1.00 19.70 ? 436 SER   A CB  1 
ATOM   2894 O OG  . SER   A 1 436 ? 129.665 108.764 165.034 1.00 27.19 ? 436 SER   A OG  1 
ATOM   2895 N N   . ILE   A 1 437 ? 128.901 108.293 161.336 1.00 10.92 ? 437 ILE   A N   1 
ATOM   2896 C CA  . ILE   A 1 437 ? 128.492 107.310 160.340 1.00 15.96 ? 437 ILE   A CA  1 
ATOM   2897 C C   . ILE   A 1 437 ? 127.866 108.079 159.182 1.00 13.07 ? 437 ILE   A C   1 
ATOM   2898 O O   . ILE   A 1 437 ? 127.661 107.539 158.088 1.00 11.37 ? 437 ILE   A O   1 
ATOM   2899 C CB  . ILE   A 1 437 ? 127.531 106.267 160.949 1.00 11.33 ? 437 ILE   A CB  1 
ATOM   2900 C CG1 . ILE   A 1 437 ? 126.984 105.307 159.888 1.00 8.61  ? 437 ILE   A CG1 1 
ATOM   2901 C CG2 . ILE   A 1 437 ? 126.388 106.952 161.669 1.00 13.53 ? 437 ILE   A CG2 1 
ATOM   2902 C CD1 . ILE   A 1 437 ? 126.268 104.105 160.464 1.00 16.42 ? 437 ILE   A CD1 1 
ATOM   2903 N N   . GLN   A 1 438 ? 127.581 109.363 159.414 1.00 14.40 ? 438 GLN   A N   1 
ATOM   2904 C CA  . GLN   A 1 438 ? 127.080 110.223 158.347 1.00 14.65 ? 438 GLN   A CA  1 
ATOM   2905 C C   . GLN   A 1 438 ? 128.039 110.239 157.166 1.00 18.86 ? 438 GLN   A C   1 
ATOM   2906 O O   . GLN   A 1 438 ? 127.640 110.021 156.017 1.00 20.17 ? 438 GLN   A O   1 
ATOM   2907 C CB  . GLN   A 1 438 ? 126.872 111.643 158.874 1.00 20.51 ? 438 GLN   A CB  1 
ATOM   2908 C CG  . GLN   A 1 438 ? 125.478 111.940 159.380 1.00 16.70 ? 438 GLN   A CG  1 
ATOM   2909 C CD  . GLN   A 1 438 ? 125.074 113.375 159.120 1.00 13.94 ? 438 GLN   A CD  1 
ATOM   2910 O OE1 . GLN   A 1 438 ? 124.799 113.759 157.983 1.00 17.71 ? 438 GLN   A OE1 1 
ATOM   2911 N NE2 . GLN   A 1 438 ? 125.059 114.184 160.173 1.00 15.83 ? 438 GLN   A NE2 1 
ATOM   2912 N N   . PHE   A 1 439 ? 129.321 110.477 157.431 1.00 1.22  ? 439 PHE   A N   1 
ATOM   2913 C CA  . PHE   A 1 439 ? 130.283 110.493 156.342 1.00 8.07  ? 439 PHE   A CA  1 
ATOM   2914 C C   . PHE   A 1 439 ? 130.631 109.097 155.853 1.00 10.73 ? 439 PHE   A C   1 
ATOM   2915 O O   . PHE   A 1 439 ? 131.060 108.952 154.707 1.00 5.12  ? 439 PHE   A O   1 
ATOM   2916 C CB  . PHE   A 1 439 ? 131.543 111.249 156.756 1.00 4.21  ? 439 PHE   A CB  1 
ATOM   2917 C CG  . PHE   A 1 439 ? 131.547 112.673 156.300 1.00 6.75  ? 439 PHE   A CG  1 
ATOM   2918 C CD1 . PHE   A 1 439 ? 132.065 113.012 155.064 1.00 9.73  ? 439 PHE   A CD1 1 
ATOM   2919 C CD2 . PHE   A 1 439 ? 131.001 113.669 157.090 1.00 9.16  ? 439 PHE   A CD2 1 
ATOM   2920 C CE1 . PHE   A 1 439 ? 132.055 114.317 154.633 1.00 8.06  ? 439 PHE   A CE1 1 
ATOM   2921 C CE2 . PHE   A 1 439 ? 130.992 114.980 156.665 1.00 5.53  ? 439 PHE   A CE2 1 
ATOM   2922 C CZ  . PHE   A 1 439 ? 131.521 115.304 155.435 1.00 8.12  ? 439 PHE   A CZ  1 
ATOM   2923 N N   . LEU   A 1 440 ? 130.419 108.066 156.672 1.00 9.41  ? 440 LEU   A N   1 
ATOM   2924 C CA  . LEU   A 1 440 ? 130.518 106.701 156.167 1.00 10.09 ? 440 LEU   A CA  1 
ATOM   2925 C C   . LEU   A 1 440 ? 129.494 106.457 155.067 1.00 15.02 ? 440 LEU   A C   1 
ATOM   2926 O O   . LEU   A 1 440 ? 129.823 105.938 153.995 1.00 16.55 ? 440 LEU   A O   1 
ATOM   2927 C CB  . LEU   A 1 440 ? 130.325 105.702 157.308 1.00 9.15  ? 440 LEU   A CB  1 
ATOM   2928 C CG  . LEU   A 1 440 ? 130.091 104.248 156.895 1.00 10.21 ? 440 LEU   A CG  1 
ATOM   2929 C CD1 . LEU   A 1 440 ? 131.320 103.683 156.199 1.00 7.31  ? 440 LEU   A CD1 1 
ATOM   2930 C CD2 . LEU   A 1 440 ? 129.715 103.400 158.100 1.00 11.56 ? 440 LEU   A CD2 1 
ATOM   2931 N N   . VAL   A 1 441 ? 128.241 106.848 155.310 1.00 8.14  ? 441 VAL   A N   1 
ATOM   2932 C CA  . VAL   A 1 441 ? 127.214 106.647 154.291 1.00 12.45 ? 441 VAL   A CA  1 
ATOM   2933 C C   . VAL   A 1 441 ? 127.396 107.623 153.134 1.00 13.13 ? 441 VAL   A C   1 
ATOM   2934 O O   . VAL   A 1 441 ? 127.034 107.310 151.997 1.00 7.22  ? 441 VAL   A O   1 
ATOM   2935 C CB  . VAL   A 1 441 ? 125.797 106.724 154.895 1.00 6.86  ? 441 VAL   A CB  1 
ATOM   2936 C CG1 . VAL   A 1 441 ? 125.739 105.977 156.216 1.00 15.10 ? 441 VAL   A CG1 1 
ATOM   2937 C CG2 . VAL   A 1 441 ? 125.340 108.164 155.061 1.00 9.93  ? 441 VAL   A CG2 1 
ATOM   2938 N N   . TYR   A 1 442 ? 127.970 108.805 153.382 1.00 8.59  ? 442 TYR   A N   1 
ATOM   2939 C CA  . TYR   A 1 442 ? 128.291 109.701 152.273 1.00 12.89 ? 442 TYR   A CA  1 
ATOM   2940 C C   . TYR   A 1 442 ? 129.360 109.097 151.368 1.00 10.84 ? 442 TYR   A C   1 
ATOM   2941 O O   . TYR   A 1 442 ? 129.254 109.158 150.135 1.00 6.51  ? 442 TYR   A O   1 
ATOM   2942 C CB  . TYR   A 1 442 ? 128.745 111.061 152.804 1.00 4.11  ? 442 TYR   A CB  1 
ATOM   2943 C CG  . TYR   A 1 442 ? 127.647 111.856 153.471 1.00 8.61  ? 442 TYR   A CG  1 
ATOM   2944 C CD1 . TYR   A 1 442 ? 126.325 111.719 153.071 1.00 6.61  ? 442 TYR   A CD1 1 
ATOM   2945 C CD2 . TYR   A 1 442 ? 127.933 112.747 154.496 1.00 3.47  ? 442 TYR   A CD2 1 
ATOM   2946 C CE1 . TYR   A 1 442 ? 125.318 112.443 153.677 1.00 10.96 ? 442 TYR   A CE1 1 
ATOM   2947 C CE2 . TYR   A 1 442 ? 126.932 113.475 155.108 1.00 7.10  ? 442 TYR   A CE2 1 
ATOM   2948 C CZ  . TYR   A 1 442 ? 125.627 113.320 154.694 1.00 8.97  ? 442 TYR   A CZ  1 
ATOM   2949 O OH  . TYR   A 1 442 ? 124.626 114.043 155.300 1.00 10.81 ? 442 TYR   A OH  1 
ATOM   2950 N N   . GLY   A 1 443 ? 130.398 108.508 151.963 1.00 15.89 ? 443 GLY   A N   1 
ATOM   2951 C CA  . GLY   A 1 443 ? 131.406 107.827 151.172 1.00 12.60 ? 443 GLY   A CA  1 
ATOM   2952 C C   . GLY   A 1 443 ? 130.851 106.618 150.450 1.00 9.63  ? 443 GLY   A C   1 
ATOM   2953 O O   . GLY   A 1 443 ? 131.240 106.332 149.317 1.00 7.58  ? 443 GLY   A O   1 
ATOM   2954 N N   . SER   A 1 444 ? 129.933 105.892 151.092 1.00 10.22 ? 444 SER   A N   1 
ATOM   2955 C CA  . SER   A 1 444 ? 129.277 104.772 150.423 1.00 12.68 ? 444 SER   A CA  1 
ATOM   2956 C C   . SER   A 1 444 ? 128.439 105.250 149.242 1.00 16.09 ? 444 SER   A C   1 
ATOM   2957 O O   . SER   A 1 444 ? 128.407 104.599 148.194 1.00 16.43 ? 444 SER   A O   1 
ATOM   2958 C CB  . SER   A 1 444 ? 128.413 103.999 151.418 1.00 11.56 ? 444 SER   A CB  1 
ATOM   2959 O OG  . SER   A 1 444 ? 127.524 103.123 150.749 1.00 10.31 ? 444 SER   A OG  1 
ATOM   2960 N N   . TYR   A 1 445 ? 127.751 106.381 149.400 1.00 5.50  ? 445 TYR   A N   1 
ATOM   2961 C CA  . TYR   A 1 445 ? 126.966 106.955 148.311 1.00 7.92  ? 445 TYR   A CA  1 
ATOM   2962 C C   . TYR   A 1 445 ? 127.857 107.363 147.144 1.00 9.99  ? 445 TYR   A C   1 
ATOM   2963 O O   . TYR   A 1 445 ? 127.551 107.069 145.980 1.00 7.74  ? 445 TYR   A O   1 
ATOM   2964 C CB  . TYR   A 1 445 ? 126.172 108.145 148.852 1.00 5.31  ? 445 TYR   A CB  1 
ATOM   2965 C CG  . TYR   A 1 445 ? 125.447 108.986 147.829 1.00 8.69  ? 445 TYR   A CG  1 
ATOM   2966 C CD1 . TYR   A 1 445 ? 124.261 108.549 147.257 1.00 5.09  ? 445 TYR   A CD1 1 
ATOM   2967 C CD2 . TYR   A 1 445 ? 125.925 110.239 147.471 1.00 8.97  ? 445 TYR   A CD2 1 
ATOM   2968 C CE1 . TYR   A 1 445 ? 123.588 109.323 146.334 1.00 10.86 ? 445 TYR   A CE1 1 
ATOM   2969 C CE2 . TYR   A 1 445 ? 125.258 111.021 146.552 1.00 8.83  ? 445 TYR   A CE2 1 
ATOM   2970 C CZ  . TYR   A 1 445 ? 124.091 110.557 145.986 1.00 8.10  ? 445 TYR   A CZ  1 
ATOM   2971 O OH  . TYR   A 1 445 ? 123.420 111.330 145.069 1.00 5.52  ? 445 TYR   A OH  1 
ATOM   2972 N N   . PHE   A 1 446 ? 128.982 108.018 147.437 1.00 11.43 ? 446 PHE   A N   1 
ATOM   2973 C CA  . PHE   A 1 446 ? 129.906 108.395 146.372 1.00 12.55 ? 446 PHE   A CA  1 
ATOM   2974 C C   . PHE   A 1 446 ? 130.561 107.176 145.733 1.00 10.44 ? 446 PHE   A C   1 
ATOM   2975 O O   . PHE   A 1 446 ? 130.821 107.178 144.525 1.00 8.40  ? 446 PHE   A O   1 
ATOM   2976 C CB  . PHE   A 1 446 ? 130.963 109.358 146.905 1.00 4.07  ? 446 PHE   A CB  1 
ATOM   2977 C CG  . PHE   A 1 446 ? 130.663 110.800 146.617 1.00 5.81  ? 446 PHE   A CG  1 
ATOM   2978 C CD1 . PHE   A 1 446 ? 131.102 111.389 145.444 1.00 6.33  ? 446 PHE   A CD1 1 
ATOM   2979 C CD2 . PHE   A 1 446 ? 129.928 111.561 147.508 1.00 5.58  ? 446 PHE   A CD2 1 
ATOM   2980 C CE1 . PHE   A 1 446 ? 130.825 112.713 145.172 1.00 7.12  ? 446 PHE   A CE1 1 
ATOM   2981 C CE2 . PHE   A 1 446 ? 129.649 112.885 147.242 1.00 8.77  ? 446 PHE   A CE2 1 
ATOM   2982 C CZ  . PHE   A 1 446 ? 130.098 113.462 146.073 1.00 4.79  ? 446 PHE   A CZ  1 
ATOM   2983 N N   . ALA   A 1 447 ? 130.824 106.127 146.514 1.00 11.46 ? 447 ALA   A N   1 
ATOM   2984 C CA  . ALA   A 1 447 ? 131.371 104.899 145.949 1.00 10.08 ? 447 ALA   A CA  1 
ATOM   2985 C C   . ALA   A 1 447 ? 130.354 104.203 145.057 1.00 12.03 ? 447 ALA   A C   1 
ATOM   2986 O O   . ALA   A 1 447 ? 130.717 103.630 144.027 1.00 13.93 ? 447 ALA   A O   1 
ATOM   2987 C CB  . ALA   A 1 447 ? 131.834 103.966 147.068 1.00 13.86 ? 447 ALA   A CB  1 
ATOM   2988 N N   . VAL   A 1 448 ? 129.077 104.238 145.441 1.00 16.76 ? 448 VAL   A N   1 
ATOM   2989 C CA  . VAL   A 1 448 ? 128.024 103.699 144.586 1.00 16.62 ? 448 VAL   A CA  1 
ATOM   2990 C C   . VAL   A 1 448 ? 127.958 104.478 143.281 1.00 11.17 ? 448 VAL   A C   1 
ATOM   2991 O O   . VAL   A 1 448 ? 127.818 103.896 142.198 1.00 16.53 ? 448 VAL   A O   1 
ATOM   2992 C CB  . VAL   A 1 448 ? 126.674 103.716 145.330 1.00 8.95  ? 448 VAL   A CB  1 
ATOM   2993 C CG1 . VAL   A 1 448 ? 125.514 103.678 144.346 1.00 12.22 ? 448 VAL   A CG1 1 
ATOM   2994 C CG2 . VAL   A 1 448 ? 126.591 102.549 146.300 1.00 11.34 ? 448 VAL   A CG2 1 
ATOM   2995 N N   . ILE   A 1 449 ? 128.064 105.806 143.362 1.00 15.56 ? 449 ILE   A N   1 
ATOM   2996 C CA  . ILE   A 1 449 ? 128.060 106.626 142.152 1.00 14.25 ? 449 ILE   A CA  1 
ATOM   2997 C C   . ILE   A 1 449 ? 129.245 106.269 141.261 1.00 8.03  ? 449 ILE   A C   1 
ATOM   2998 O O   . ILE   A 1 449 ? 129.099 106.086 140.047 1.00 10.28 ? 449 ILE   A O   1 
ATOM   2999 C CB  . ILE   A 1 449 ? 128.058 108.120 142.519 1.00 7.57  ? 449 ILE   A CB  1 
ATOM   3000 C CG1 . ILE   A 1 449 ? 126.725 108.500 143.159 1.00 11.18 ? 449 ILE   A CG1 1 
ATOM   3001 C CG2 . ILE   A 1 449 ? 128.323 108.976 141.291 1.00 13.82 ? 449 ILE   A CG2 1 
ATOM   3002 C CD1 . ILE   A 1 449 ? 126.629 109.951 143.529 1.00 6.25  ? 449 ILE   A CD1 1 
ATOM   3003 N N   . ALA   A 1 450 ? 130.436 106.155 141.854 1.00 12.65 ? 450 ALA   A N   1 
ATOM   3004 C CA  . ALA   A 1 450 ? 131.630 105.833 141.077 1.00 20.51 ? 450 ALA   A CA  1 
ATOM   3005 C C   . ALA   A 1 450 ? 131.523 104.451 140.441 1.00 20.34 ? 450 ALA   A C   1 
ATOM   3006 O O   . ALA   A 1 450 ? 131.886 104.262 139.275 1.00 16.30 ? 450 ALA   A O   1 
ATOM   3007 C CB  . ALA   A 1 450 ? 132.872 105.926 141.963 1.00 17.20 ? 450 ALA   A CB  1 
ATOM   3008 N N   . GLY   A 1 451 ? 131.031 103.468 141.200 1.00 20.36 ? 451 GLY   A N   1 
ATOM   3009 C CA  . GLY   A 1 451 ? 130.878 102.126 140.661 1.00 27.16 ? 451 GLY   A CA  1 
ATOM   3010 C C   . GLY   A 1 451 ? 129.841 102.054 139.559 1.00 24.34 ? 451 GLY   A C   1 
ATOM   3011 O O   . GLY   A 1 451 ? 129.984 101.282 138.607 1.00 24.31 ? 451 GLY   A O   1 
ATOM   3012 N N   . ILE   A 1 452 ? 128.775 102.847 139.681 1.00 16.99 ? 452 ILE   A N   1 
ATOM   3013 C CA  . ILE   A 1 452 ? 127.809 102.966 138.595 1.00 25.41 ? 452 ILE   A CA  1 
ATOM   3014 C C   . ILE   A 1 452 ? 128.507 103.444 137.330 1.00 24.66 ? 452 ILE   A C   1 
ATOM   3015 O O   . ILE   A 1 452 ? 128.245 102.947 136.229 1.00 23.73 ? 452 ILE   A O   1 
ATOM   3016 C CB  . ILE   A 1 452 ? 126.662 103.908 139.003 1.00 24.29 ? 452 ILE   A CB  1 
ATOM   3017 C CG1 . ILE   A 1 452 ? 125.628 103.154 139.838 1.00 18.45 ? 452 ILE   A CG1 1 
ATOM   3018 C CG2 . ILE   A 1 452 ? 126.010 104.532 137.779 1.00 24.07 ? 452 ILE   A CG2 1 
ATOM   3019 C CD1 . ILE   A 1 452 ? 124.676 104.059 140.572 1.00 17.85 ? 452 ILE   A CD1 1 
ATOM   3020 N N   . PHE   A 1 453 ? 129.415 104.407 137.470 1.00 24.26 ? 453 PHE   A N   1 
ATOM   3021 C CA  . PHE   A 1 453 ? 130.226 104.860 136.350 1.00 17.22 ? 453 PHE   A CA  1 
ATOM   3022 C C   . PHE   A 1 453 ? 131.440 103.972 136.101 1.00 24.96 ? 453 PHE   A C   1 
ATOM   3023 O O   . PHE   A 1 453 ? 132.095 104.128 135.064 1.00 22.11 ? 453 PHE   A O   1 
ATOM   3024 C CB  . PHE   A 1 453 ? 130.648 106.308 136.577 1.00 19.24 ? 453 PHE   A CB  1 
ATOM   3025 C CG  . PHE   A 1 453 ? 129.504 107.277 136.497 1.00 24.49 ? 453 PHE   A CG  1 
ATOM   3026 C CD1 . PHE   A 1 453 ? 128.869 107.518 135.294 1.00 20.35 ? 453 PHE   A CD1 1 
ATOM   3027 C CD2 . PHE   A 1 453 ? 129.056 107.939 137.630 1.00 26.03 ? 453 PHE   A CD2 1 
ATOM   3028 C CE1 . PHE   A 1 453 ? 127.805 108.404 135.221 1.00 19.00 ? 453 PHE   A CE1 1 
ATOM   3029 C CE2 . PHE   A 1 453 ? 128.001 108.822 137.561 1.00 26.58 ? 453 PHE   A CE2 1 
ATOM   3030 C CZ  . PHE   A 1 453 ? 127.375 109.056 136.359 1.00 26.90 ? 453 PHE   A CZ  1 
ATOM   3031 N N   . LEU   A 1 454 ? 131.761 103.067 137.028 1.00 26.39 ? 454 LEU   A N   1 
ATOM   3032 C CA  . LEU   A 1 454 ? 132.662 101.952 136.756 1.00 31.97 ? 454 LEU   A CA  1 
ATOM   3033 C C   . LEU   A 1 454 ? 131.990 100.899 135.886 1.00 31.77 ? 454 LEU   A C   1 
ATOM   3034 O O   . LEU   A 1 454 ? 132.529 100.501 134.848 1.00 27.60 ? 454 LEU   A O   1 
ATOM   3035 C CB  . LEU   A 1 454 ? 133.125 101.305 138.071 1.00 26.99 ? 454 LEU   A CB  1 
ATOM   3036 C CG  . LEU   A 1 454 ? 134.578 100.856 138.251 1.00 26.17 ? 454 LEU   A CG  1 
ATOM   3037 C CD1 . LEU   A 1 454 ? 135.522 101.822 137.575 1.00 33.28 ? 454 LEU   A CD1 1 
ATOM   3038 C CD2 . LEU   A 1 454 ? 134.903 100.756 139.729 1.00 25.91 ? 454 LEU   A CD2 1 
ATOM   3039 N N   . MET   A 1 455 ? 130.807 100.447 136.303 1.00 57.34 ? 455 MET   A N   1 
ATOM   3040 C CA  . MET   A 1 455 ? 130.078 99.430  135.564 1.00 52.41 ? 455 MET   A CA  1 
ATOM   3041 C C   . MET   A 1 455 ? 129.578 99.948  134.226 1.00 57.49 ? 455 MET   A C   1 
ATOM   3042 O O   . MET   A 1 455 ? 129.299 99.142  133.335 1.00 56.52 ? 455 MET   A O   1 
ATOM   3043 C CB  . MET   A 1 455 ? 128.922 98.912  136.417 1.00 49.69 ? 455 MET   A CB  1 
ATOM   3044 C CG  . MET   A 1 455 ? 127.677 99.791  136.407 1.00 53.87 ? 455 MET   A CG  1 
ATOM   3045 S SD  . MET   A 1 455 ? 126.288 99.089  137.319 1.00 54.87 ? 455 MET   A SD  1 
ATOM   3046 C CE  . MET   A 1 455 ? 127.009 98.885  138.946 1.00 52.19 ? 455 MET   A CE  1 
ATOM   3047 N N   . ARG   A 1 456 ? 129.450 101.268 134.066 1.00 58.79 ? 456 ARG   A N   1 
ATOM   3048 C CA  . ARG   A 1 456 ? 129.129 101.810 132.750 1.00 61.99 ? 456 ARG   A CA  1 
ATOM   3049 C C   . ARG   A 1 456 ? 130.305 101.651 131.795 1.00 67.13 ? 456 ARG   A C   1 
ATOM   3050 O O   . ARG   A 1 456 ? 130.113 101.362 130.608 1.00 59.37 ? 456 ARG   A O   1 
ATOM   3051 C CB  . ARG   A 1 456 ? 128.723 103.281 132.861 1.00 59.79 ? 456 ARG   A CB  1 
ATOM   3052 C CG  . ARG   A 1 456 ? 128.133 103.860 131.579 1.00 65.76 ? 456 ARG   A CG  1 
ATOM   3053 C CD  . ARG   A 1 456 ? 129.099 104.809 130.883 1.00 63.88 ? 456 ARG   A CD  1 
ATOM   3054 N NE  . ARG   A 1 456 ? 128.682 105.110 129.518 1.00 63.72 ? 456 ARG   A NE  1 
ATOM   3055 C CZ  . ARG   A 1 456 ? 128.961 106.240 128.882 1.00 62.47 ? 456 ARG   A CZ  1 
ATOM   3056 N NH1 . ARG   A 1 456 ? 129.669 107.199 129.456 1.00 64.77 ? 456 ARG   A NH1 1 
ATOM   3057 N NH2 . ARG   A 1 456 ? 128.529 106.408 127.635 1.00 67.25 ? 456 ARG   A NH2 1 
ATOM   3058 N N   . SER   A 1 457 ? 131.530 101.845 132.291 1.00 48.82 ? 457 SER   A N   1 
ATOM   3059 C CA  . SER   A 1 457 ? 132.711 101.632 131.459 1.00 54.50 ? 457 SER   A CA  1 
ATOM   3060 C C   . SER   A 1 457 ? 132.864 100.163 131.078 1.00 50.22 ? 457 SER   A C   1 
ATOM   3061 O O   . SER   A 1 457 ? 133.213 99.844  129.935 1.00 51.06 ? 457 SER   A O   1 
ATOM   3062 C CB  . SER   A 1 457 ? 133.960 102.133 132.184 1.00 53.35 ? 457 SER   A CB  1 
ATOM   3063 O OG  . SER   A 1 457 ? 134.050 103.546 132.127 1.00 48.64 ? 457 SER   A OG  1 
ATOM   3064 N N   . MET   A 1 458 ? 132.616 99.255  132.025 1.00 54.83 ? 458 MET   A N   1 
ATOM   3065 C CA  . MET   A 1 458 ? 132.634 97.830  131.710 1.00 52.64 ? 458 MET   A CA  1 
ATOM   3066 C C   . MET   A 1 458 ? 131.518 97.462  130.740 1.00 51.80 ? 458 MET   A C   1 
ATOM   3067 O O   . MET   A 1 458 ? 131.714 96.617  129.859 1.00 48.35 ? 458 MET   A O   1 
ATOM   3068 C CB  . MET   A 1 458 ? 132.529 97.008  132.997 1.00 52.57 ? 458 MET   A CB  1 
ATOM   3069 C CG  . MET   A 1 458 ? 131.939 95.617  132.815 1.00 48.19 ? 458 MET   A CG  1 
ATOM   3070 S SD  . MET   A 1 458 ? 133.074 94.471  132.008 1.00 53.78 ? 458 MET   A SD  1 
ATOM   3071 C CE  . MET   A 1 458 ? 132.080 92.982  131.972 1.00 45.73 ? 458 MET   A CE  1 
ATOM   3072 N N   . TYR   A 1 459 ? 130.348 98.088  130.885 1.00 61.93 ? 459 TYR   A N   1 
ATOM   3073 C CA  . TYR   A 1 459 ? 129.269 97.891  129.925 1.00 65.84 ? 459 TYR   A CA  1 
ATOM   3074 C C   . TYR   A 1 459 ? 129.697 98.326  128.530 1.00 67.39 ? 459 TYR   A C   1 
ATOM   3075 O O   . TYR   A 1 459 ? 129.396 97.649  127.540 1.00 65.19 ? 459 TYR   A O   1 
ATOM   3076 C CB  . TYR   A 1 459 ? 128.028 98.659  130.385 1.00 69.04 ? 459 TYR   A CB  1 
ATOM   3077 C CG  . TYR   A 1 459 ? 127.120 99.116  129.267 1.00 70.02 ? 459 TYR   A CG  1 
ATOM   3078 C CD1 . TYR   A 1 459 ? 126.345 98.208  128.557 1.00 64.91 ? 459 TYR   A CD1 1 
ATOM   3079 C CD2 . TYR   A 1 459 ? 127.035 100.459 128.925 1.00 67.95 ? 459 TYR   A CD2 1 
ATOM   3080 C CE1 . TYR   A 1 459 ? 125.513 98.627  127.535 1.00 65.21 ? 459 TYR   A CE1 1 
ATOM   3081 C CE2 . TYR   A 1 459 ? 126.208 100.886 127.906 1.00 66.92 ? 459 TYR   A CE2 1 
ATOM   3082 C CZ  . TYR   A 1 459 ? 125.449 99.967  127.215 1.00 62.51 ? 459 TYR   A CZ  1 
ATOM   3083 O OH  . TYR   A 1 459 ? 124.624 100.389 126.199 1.00 61.36 ? 459 TYR   A OH  1 
ATOM   3084 N N   . ILE   A 1 460 ? 130.403 99.456  128.433 1.00 56.91 ? 460 ILE   A N   1 
ATOM   3085 C CA  . ILE   A 1 460 ? 131.000 99.866  127.167 1.00 55.27 ? 460 ILE   A CA  1 
ATOM   3086 C C   . ILE   A 1 460 ? 132.065 98.892  126.689 1.00 49.97 ? 460 ILE   A C   1 
ATOM   3087 O O   . ILE   A 1 460 ? 132.097 98.562  125.497 1.00 52.97 ? 460 ILE   A O   1 
ATOM   3088 C CB  . ILE   A 1 460 ? 131.594 101.285 127.291 1.00 50.92 ? 460 ILE   A CB  1 
ATOM   3089 C CG1 . ILE   A 1 460 ? 130.474 102.323 127.371 1.00 48.88 ? 460 ILE   A CG1 1 
ATOM   3090 C CG2 . ILE   A 1 460 ? 132.521 101.590 126.124 1.00 51.30 ? 460 ILE   A CG2 1 
ATOM   3091 C CD1 . ILE   A 1 460 ? 130.967 103.750 127.392 1.00 50.09 ? 460 ILE   A CD1 1 
ATOM   3092 N N   . THR   A 1 461 ? 132.922 98.418  127.592 1.00 40.39 ? 461 THR   A N   1 
ATOM   3093 C CA  . THR   A 1 461 ? 133.965 97.441  127.280 1.00 44.10 ? 461 THR   A CA  1 
ATOM   3094 C C   . THR   A 1 461 ? 134.902 97.947  126.187 1.00 49.44 ? 461 THR   A C   1 
ATOM   3095 O O   . THR   A 1 461 ? 135.921 98.576  126.473 1.00 48.51 ? 461 THR   A O   1 
ATOM   3096 C CB  . THR   A 1 461 ? 133.363 96.084  126.850 1.00 45.97 ? 461 THR   A CB  1 
ATOM   3097 O OG1 . THR   A 1 461 ? 132.993 95.333  128.013 1.00 43.41 ? 461 THR   A OG1 1 
ATOM   3098 C CG2 . THR   A 1 461 ? 134.369 95.282  126.038 1.00 42.54 ? 461 THR   A CG2 1 
HETATM 3099 C C10 . A1H5C B 2 .   ? 123.382 129.889 153.750 1.00 36.68 ? 501 A1H5C A C10 1 
HETATM 3100 N N12 . A1H5C B 2 .   ? 123.155 132.228 153.974 1.00 33.65 ? 501 A1H5C A N12 1 
HETATM 3101 C C13 . A1H5C B 2 .   ? 121.853 131.988 154.037 1.00 30.94 ? 501 A1H5C A C13 1 
HETATM 3102 C C15 . A1H5C B 2 .   ? 121.884 134.357 154.402 1.00 31.34 ? 501 A1H5C A C15 1 
HETATM 3103 C C03 . A1H5C B 2 .   ? 123.542 127.110 154.990 1.00 32.93 ? 501 A1H5C A C03 1 
HETATM 3104 C C04 . A1H5C B 2 .   ? 123.138 125.813 155.175 1.00 36.33 ? 501 A1H5C A C04 1 
HETATM 3105 C C05 . A1H5C B 2 .   ? 123.270 124.943 154.117 1.00 31.52 ? 501 A1H5C A C05 1 
HETATM 3106 C C06 . A1H5C B 2 .   ? 123.794 125.364 152.908 1.00 34.86 ? 501 A1H5C A C06 1 
HETATM 3107 C C07 . A1H5C B 2 .   ? 124.153 126.674 152.780 1.00 29.47 ? 501 A1H5C A C07 1 
HETATM 3108 C C08 . A1H5C B 2 .   ? 124.709 127.213 151.513 1.00 33.67 ? 501 A1H5C A C08 1 
HETATM 3109 C C09 . A1H5C B 2 .   ? 124.426 128.838 153.575 1.00 33.64 ? 501 A1H5C A C09 1 
HETATM 3110 C C11 . A1H5C B 2 .   ? 123.894 131.134 153.824 1.00 33.44 ? 501 A1H5C A C11 1 
HETATM 3111 C C14 . A1H5C B 2 .   ? 120.986 133.155 154.215 1.00 32.50 ? 501 A1H5C A C14 1 
HETATM 3112 C C16 . A1H5C B 2 .   ? 122.223 135.041 153.107 1.00 38.25 ? 501 A1H5C A C16 1 
HETATM 3113 C C18 . A1H5C B 2 .   ? 122.028 129.784 153.819 1.00 30.40 ? 501 A1H5C A C18 1 
HETATM 3114 N N02 . A1H5C B 2 .   ? 124.004 127.480 153.802 1.00 29.75 ? 501 A1H5C A N02 1 
HETATM 3115 N N17 . A1H5C B 2 .   ? 121.242 130.826 153.966 1.00 36.18 ? 501 A1H5C A N17 1 
HETATM 3116 N N19 . A1H5C B 2 .   ? 121.327 128.581 153.762 1.00 35.06 ? 501 A1H5C A N19 1 
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