data_9BIM
# 
_entry.id   9BIM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9BIM         pdb_00009bim 10.2210/pdb9bim/pdb 
WWPDB D_1000283357 ?            ?                   
EMDB  EMD-44593    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2025-01-15 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 2 'Structure model' em_admin        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
12 2 'Structure model' '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BIM 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of human CHT1 in the HC-3 bound outward-facing state' 
_pdbx_database_related.db_id          EMD-44593 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              youxing.jiang@utsouthwestern.edu 
_pdbx_contact_author.name_first         Youxing 
_pdbx_contact_author.name_last          Jiang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1874-0504 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xue, J.'   1 0000-0002-7331-1382 
'Jiang, Y.' 2 0000-0002-1874-0504 
# 
_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            'Cell Discov' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2056-5968 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                116 
_citation.page_last                 116 
_citation.title                     'Structural mechanisms of human sodium-coupled high-affinity choline transporter CHT1.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41421-024-00731-7 
_citation.pdbx_database_id_PubMed   39587078 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xue, J.'   1 0000-0002-7331-1382 
primary 'Chen, H.'  2 ?                   
primary 'Wang, Y.'  3 0000-0001-9156-0377 
primary 'Jiang, Y.' 4 0000-0002-1874-0504 
# 
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 'High affinity choline transporter 1'                                        66526.625 1 ? ? ? ? 
2 non-polymer syn "(2S,2'S)-2,2'-biphenyl-4,4'-diylbis(2-hydroxy-4,4-dimethylmorpholin-4-ium)" 414.538   1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'hCHT1,Hemicholinium-3-sensitive choline transporter,CHT,Solute carrier family 5 member 7' 
# 
_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       
;MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGY
GLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVD
MHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSW
LDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMIL
PIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTK
TVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFK
TLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNK
EAFLDVDSSPEGSGTEDNLQAAAGGSWSHPQFEKGGGSGGGSGGSAWSHPQFEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGY
GLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVD
MHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSW
LDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMIL
PIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTK
TVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFK
TLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNK
EAFLDVDSSPEGSGTEDNLQAAAGGSWSHPQFEKGGGSGGGSGGSAWSHPQFEK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        "(2S,2'S)-2,2'-biphenyl-4,4'-diylbis(2-hydroxy-4,4-dimethylmorpholin-4-ium)" 
_pdbx_entity_nonpoly.comp_id     HC6 
# 
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   ALA n 
1 3   PHE n 
1 4   HIS n 
1 5   VAL n 
1 6   GLU n 
1 7   GLY n 
1 8   LEU n 
1 9   ILE n 
1 10  ALA n 
1 11  ILE n 
1 12  ILE n 
1 13  VAL n 
1 14  PHE n 
1 15  TYR n 
1 16  LEU n 
1 17  LEU n 
1 18  ILE n 
1 19  LEU n 
1 20  LEU n 
1 21  VAL n 
1 22  GLY n 
1 23  ILE n 
1 24  TRP n 
1 25  ALA n 
1 26  ALA n 
1 27  TRP n 
1 28  ARG n 
1 29  THR n 
1 30  LYS n 
1 31  ASN n 
1 32  SER n 
1 33  GLY n 
1 34  SER n 
1 35  ALA n 
1 36  GLU n 
1 37  GLU n 
1 38  ARG n 
1 39  SER n 
1 40  GLU n 
1 41  ALA n 
1 42  ILE n 
1 43  ILE n 
1 44  VAL n 
1 45  GLY n 
1 46  GLY n 
1 47  ARG n 
1 48  ASP n 
1 49  ILE n 
1 50  GLY n 
1 51  LEU n 
1 52  LEU n 
1 53  VAL n 
1 54  GLY n 
1 55  GLY n 
1 56  PHE n 
1 57  THR n 
1 58  MET n 
1 59  THR n 
1 60  ALA n 
1 61  THR n 
1 62  TRP n 
1 63  VAL n 
1 64  GLY n 
1 65  GLY n 
1 66  GLY n 
1 67  TYR n 
1 68  ILE n 
1 69  ASN n 
1 70  GLY n 
1 71  THR n 
1 72  ALA n 
1 73  GLU n 
1 74  ALA n 
1 75  VAL n 
1 76  TYR n 
1 77  VAL n 
1 78  PRO n 
1 79  GLY n 
1 80  TYR n 
1 81  GLY n 
1 82  LEU n 
1 83  ALA n 
1 84  TRP n 
1 85  ALA n 
1 86  GLN n 
1 87  ALA n 
1 88  PRO n 
1 89  ILE n 
1 90  GLY n 
1 91  TYR n 
1 92  SER n 
1 93  LEU n 
1 94  SER n 
1 95  LEU n 
1 96  ILE n 
1 97  LEU n 
1 98  GLY n 
1 99  GLY n 
1 100 LEU n 
1 101 PHE n 
1 102 PHE n 
1 103 ALA n 
1 104 LYS n 
1 105 PRO n 
1 106 MET n 
1 107 ARG n 
1 108 SER n 
1 109 LYS n 
1 110 GLY n 
1 111 TYR n 
1 112 VAL n 
1 113 THR n 
1 114 MET n 
1 115 LEU n 
1 116 ASP n 
1 117 PRO n 
1 118 PHE n 
1 119 GLN n 
1 120 GLN n 
1 121 ILE n 
1 122 TYR n 
1 123 GLY n 
1 124 LYS n 
1 125 ARG n 
1 126 MET n 
1 127 GLY n 
1 128 GLY n 
1 129 LEU n 
1 130 LEU n 
1 131 PHE n 
1 132 ILE n 
1 133 PRO n 
1 134 ALA n 
1 135 LEU n 
1 136 MET n 
1 137 GLY n 
1 138 GLU n 
1 139 MET n 
1 140 PHE n 
1 141 TRP n 
1 142 ALA n 
1 143 ALA n 
1 144 ALA n 
1 145 ILE n 
1 146 PHE n 
1 147 SER n 
1 148 ALA n 
1 149 LEU n 
1 150 GLY n 
1 151 ALA n 
1 152 THR n 
1 153 ILE n 
1 154 SER n 
1 155 VAL n 
1 156 ILE n 
1 157 ILE n 
1 158 ASP n 
1 159 VAL n 
1 160 ASP n 
1 161 MET n 
1 162 HIS n 
1 163 ILE n 
1 164 SER n 
1 165 VAL n 
1 166 ILE n 
1 167 ILE n 
1 168 SER n 
1 169 ALA n 
1 170 LEU n 
1 171 ILE n 
1 172 ALA n 
1 173 THR n 
1 174 LEU n 
1 175 TYR n 
1 176 THR n 
1 177 LEU n 
1 178 VAL n 
1 179 GLY n 
1 180 GLY n 
1 181 LEU n 
1 182 TYR n 
1 183 SER n 
1 184 VAL n 
1 185 ALA n 
1 186 TYR n 
1 187 THR n 
1 188 ASP n 
1 189 VAL n 
1 190 VAL n 
1 191 GLN n 
1 192 LEU n 
1 193 PHE n 
1 194 CYS n 
1 195 ILE n 
1 196 PHE n 
1 197 VAL n 
1 198 GLY n 
1 199 LEU n 
1 200 TRP n 
1 201 ILE n 
1 202 SER n 
1 203 VAL n 
1 204 PRO n 
1 205 PHE n 
1 206 ALA n 
1 207 LEU n 
1 208 SER n 
1 209 HIS n 
1 210 PRO n 
1 211 ALA n 
1 212 VAL n 
1 213 ALA n 
1 214 ASP n 
1 215 ILE n 
1 216 GLY n 
1 217 PHE n 
1 218 THR n 
1 219 ALA n 
1 220 VAL n 
1 221 HIS n 
1 222 ALA n 
1 223 LYS n 
1 224 TYR n 
1 225 GLN n 
1 226 LYS n 
1 227 PRO n 
1 228 TRP n 
1 229 LEU n 
1 230 GLY n 
1 231 THR n 
1 232 VAL n 
1 233 ASP n 
1 234 SER n 
1 235 SER n 
1 236 GLU n 
1 237 VAL n 
1 238 TYR n 
1 239 SER n 
1 240 TRP n 
1 241 LEU n 
1 242 ASP n 
1 243 SER n 
1 244 PHE n 
1 245 LEU n 
1 246 LEU n 
1 247 LEU n 
1 248 MET n 
1 249 LEU n 
1 250 GLY n 
1 251 GLY n 
1 252 ILE n 
1 253 PRO n 
1 254 TRP n 
1 255 GLN n 
1 256 ALA n 
1 257 TYR n 
1 258 PHE n 
1 259 GLN n 
1 260 ARG n 
1 261 VAL n 
1 262 LEU n 
1 263 SER n 
1 264 SER n 
1 265 SER n 
1 266 SER n 
1 267 ALA n 
1 268 THR n 
1 269 TYR n 
1 270 ALA n 
1 271 GLN n 
1 272 VAL n 
1 273 LEU n 
1 274 SER n 
1 275 PHE n 
1 276 LEU n 
1 277 ALA n 
1 278 ALA n 
1 279 PHE n 
1 280 GLY n 
1 281 CYS n 
1 282 LEU n 
1 283 VAL n 
1 284 MET n 
1 285 ALA n 
1 286 ILE n 
1 287 PRO n 
1 288 ALA n 
1 289 ILE n 
1 290 LEU n 
1 291 ILE n 
1 292 GLY n 
1 293 ALA n 
1 294 ILE n 
1 295 GLY n 
1 296 ALA n 
1 297 SER n 
1 298 THR n 
1 299 ASP n 
1 300 TRP n 
1 301 ASN n 
1 302 GLN n 
1 303 THR n 
1 304 ALA n 
1 305 TYR n 
1 306 GLY n 
1 307 LEU n 
1 308 PRO n 
1 309 ASP n 
1 310 PRO n 
1 311 LYS n 
1 312 THR n 
1 313 THR n 
1 314 GLU n 
1 315 GLU n 
1 316 ALA n 
1 317 ASP n 
1 318 MET n 
1 319 ILE n 
1 320 LEU n 
1 321 PRO n 
1 322 ILE n 
1 323 VAL n 
1 324 LEU n 
1 325 GLN n 
1 326 TYR n 
1 327 LEU n 
1 328 CYS n 
1 329 PRO n 
1 330 VAL n 
1 331 TYR n 
1 332 ILE n 
1 333 SER n 
1 334 PHE n 
1 335 PHE n 
1 336 GLY n 
1 337 LEU n 
1 338 GLY n 
1 339 ALA n 
1 340 VAL n 
1 341 SER n 
1 342 ALA n 
1 343 ALA n 
1 344 VAL n 
1 345 MET n 
1 346 SER n 
1 347 SER n 
1 348 ALA n 
1 349 ASP n 
1 350 SER n 
1 351 SER n 
1 352 ILE n 
1 353 LEU n 
1 354 SER n 
1 355 ALA n 
1 356 SER n 
1 357 SER n 
1 358 MET n 
1 359 PHE n 
1 360 ALA n 
1 361 ARG n 
1 362 ASN n 
1 363 ILE n 
1 364 TYR n 
1 365 GLN n 
1 366 LEU n 
1 367 SER n 
1 368 PHE n 
1 369 ARG n 
1 370 GLN n 
1 371 ASN n 
1 372 ALA n 
1 373 SER n 
1 374 ASP n 
1 375 LYS n 
1 376 GLU n 
1 377 ILE n 
1 378 VAL n 
1 379 TRP n 
1 380 VAL n 
1 381 MET n 
1 382 ARG n 
1 383 ILE n 
1 384 THR n 
1 385 VAL n 
1 386 PHE n 
1 387 VAL n 
1 388 PHE n 
1 389 GLY n 
1 390 ALA n 
1 391 SER n 
1 392 ALA n 
1 393 THR n 
1 394 ALA n 
1 395 MET n 
1 396 ALA n 
1 397 LEU n 
1 398 LEU n 
1 399 THR n 
1 400 LYS n 
1 401 THR n 
1 402 VAL n 
1 403 TYR n 
1 404 GLY n 
1 405 LEU n 
1 406 TRP n 
1 407 TYR n 
1 408 LEU n 
1 409 SER n 
1 410 SER n 
1 411 ASP n 
1 412 LEU n 
1 413 VAL n 
1 414 TYR n 
1 415 ILE n 
1 416 VAL n 
1 417 ILE n 
1 418 PHE n 
1 419 PRO n 
1 420 GLN n 
1 421 LEU n 
1 422 LEU n 
1 423 CYS n 
1 424 VAL n 
1 425 LEU n 
1 426 PHE n 
1 427 VAL n 
1 428 LYS n 
1 429 GLY n 
1 430 THR n 
1 431 ASN n 
1 432 THR n 
1 433 TYR n 
1 434 GLY n 
1 435 ALA n 
1 436 VAL n 
1 437 ALA n 
1 438 GLY n 
1 439 TYR n 
1 440 VAL n 
1 441 SER n 
1 442 GLY n 
1 443 LEU n 
1 444 PHE n 
1 445 LEU n 
1 446 ARG n 
1 447 ILE n 
1 448 THR n 
1 449 GLY n 
1 450 GLY n 
1 451 GLU n 
1 452 PRO n 
1 453 TYR n 
1 454 LEU n 
1 455 TYR n 
1 456 LEU n 
1 457 GLN n 
1 458 PRO n 
1 459 LEU n 
1 460 ILE n 
1 461 PHE n 
1 462 TYR n 
1 463 PRO n 
1 464 GLY n 
1 465 TYR n 
1 466 TYR n 
1 467 PRO n 
1 468 ASP n 
1 469 ASP n 
1 470 ASN n 
1 471 GLY n 
1 472 ILE n 
1 473 TYR n 
1 474 ASN n 
1 475 GLN n 
1 476 LYS n 
1 477 PHE n 
1 478 PRO n 
1 479 PHE n 
1 480 LYS n 
1 481 THR n 
1 482 LEU n 
1 483 ALA n 
1 484 MET n 
1 485 VAL n 
1 486 THR n 
1 487 SER n 
1 488 PHE n 
1 489 LEU n 
1 490 THR n 
1 491 ASN n 
1 492 ILE n 
1 493 CYS n 
1 494 ILE n 
1 495 SER n 
1 496 TYR n 
1 497 LEU n 
1 498 ALA n 
1 499 LYS n 
1 500 TYR n 
1 501 LEU n 
1 502 PHE n 
1 503 GLU n 
1 504 SER n 
1 505 GLY n 
1 506 THR n 
1 507 LEU n 
1 508 PRO n 
1 509 PRO n 
1 510 LYS n 
1 511 LEU n 
1 512 ASP n 
1 513 VAL n 
1 514 PHE n 
1 515 ASP n 
1 516 ALA n 
1 517 VAL n 
1 518 VAL n 
1 519 ALA n 
1 520 ARG n 
1 521 HIS n 
1 522 SER n 
1 523 GLU n 
1 524 GLU n 
1 525 ASN n 
1 526 MET n 
1 527 ASP n 
1 528 LYS n 
1 529 THR n 
1 530 ILE n 
1 531 LEU n 
1 532 VAL n 
1 533 LYS n 
1 534 ASN n 
1 535 GLU n 
1 536 ASN n 
1 537 ILE n 
1 538 LYS n 
1 539 LEU n 
1 540 ASP n 
1 541 GLU n 
1 542 LEU n 
1 543 ALA n 
1 544 LEU n 
1 545 VAL n 
1 546 LYS n 
1 547 PRO n 
1 548 ARG n 
1 549 GLN n 
1 550 SER n 
1 551 MET n 
1 552 THR n 
1 553 LEU n 
1 554 SER n 
1 555 SER n 
1 556 THR n 
1 557 PHE n 
1 558 THR n 
1 559 ASN n 
1 560 LYS n 
1 561 GLU n 
1 562 ALA n 
1 563 PHE n 
1 564 LEU n 
1 565 ASP n 
1 566 VAL n 
1 567 ASP n 
1 568 SER n 
1 569 SER n 
1 570 PRO n 
1 571 GLU n 
1 572 GLY n 
1 573 SER n 
1 574 GLY n 
1 575 THR n 
1 576 GLU n 
1 577 ASP n 
1 578 ASN n 
1 579 LEU n 
1 580 GLN n 
1 581 ALA n 
1 582 ALA n 
1 583 ALA n 
1 584 GLY n 
1 585 GLY n 
1 586 SER n 
1 587 TRP n 
1 588 SER n 
1 589 HIS n 
1 590 PRO n 
1 591 GLN n 
1 592 PHE n 
1 593 GLU n 
1 594 LYS n 
1 595 GLY n 
1 596 GLY n 
1 597 GLY n 
1 598 SER n 
1 599 GLY n 
1 600 GLY n 
1 601 GLY n 
1 602 SER n 
1 603 GLY n 
1 604 GLY n 
1 605 SER n 
1 606 ALA n 
1 607 TRP n 
1 608 SER n 
1 609 HIS n 
1 610 PRO n 
1 611 GLN n 
1 612 PHE n 
1 613 GLU n 
1 614 LYS 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                   614 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SLC5A7, CHT1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'      75.067  
HC6 non-polymer         . "(2S,2'S)-2,2'-biphenyl-4,4'-diylbis(2-hydroxy-4,4-dimethylmorpholin-4-ium)" ? 'C24 H34 N2 O4 2' 414.538 
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   ALA 2   2   2   ALA ALA A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   ILE 9   9   9   ILE ILE A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  PHE 14  14  14  PHE PHE A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  LEU 17  17  17  LEU LEU 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  LEU 20  20  20  LEU LEU A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  TRP 24  24  24  TRP TRP A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  TRP 27  27  27  TRP TRP A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  ASN 31  31  ?   ?   ?   A . n 
A 1 32  SER 32  32  ?   ?   ?   A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  SER 39  39  39  SER SER A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  VAL 44  44  44  VAL VAL A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  MET 58  58  58  MET MET A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  TRP 62  62  62  TRP TRP A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  VAL 75  75  75  VAL VAL 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  PRO 78  78  78  PRO PRO A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  TYR 80  80  80  TYR TYR A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  TRP 84  84  84  TRP TRP A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  GLN 86  86  86  GLN GLN A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 MET 106 106 106 MET MET A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 MET 114 114 114 MET MET A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ASP 116 116 116 ASP ASP A . n 
A 1 117 PRO 117 117 117 PRO PRO A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 GLN 119 119 119 GLN GLN A . n 
A 1 120 GLN 120 120 120 GLN GLN A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ARG 125 125 125 ARG ARG A . n 
A 1 126 MET 126 126 126 MET MET A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 MET 139 139 139 MET MET A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 TRP 141 141 141 TRP TRP A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 ILE 153 153 153 ILE ILE A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 ASP 160 160 160 ASP ASP A . n 
A 1 161 MET 161 161 161 MET MET A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 THR 173 173 173 THR THR A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 TYR 175 175 175 TYR TYR A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 GLN 191 191 191 GLN GLN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 CYS 194 194 194 CYS CYS A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 PHE 196 196 196 PHE PHE A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 TRP 200 200 200 TRP TRP A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 ASP 214 214 214 ASP ASP A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 TYR 224 224 224 TYR TYR A . n 
A 1 225 GLN 225 225 225 GLN GLN A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 TRP 228 228 228 TRP TRP A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 GLU 236 236 236 GLU GLU A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 TRP 240 240 240 TRP TRP A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 PHE 244 244 244 PHE PHE A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 MET 248 248 248 MET MET A . n 
A 1 249 LEU 249 249 249 LEU LEU A . n 
A 1 250 GLY 250 250 250 GLY GLY A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PRO 253 253 253 PRO PRO A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 GLN 255 255 255 GLN GLN A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 SER 263 263 263 SER SER A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 GLN 271 271 271 GLN GLN A . n 
A 1 272 VAL 272 272 272 VAL VAL A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 PHE 275 275 275 PHE PHE A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 PHE 279 279 279 PHE PHE A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 CYS 281 281 281 CYS CYS A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 MET 284 284 284 MET MET A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 ILE 286 286 286 ILE ILE A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 ALA 288 288 288 ALA ALA A . n 
A 1 289 ILE 289 289 289 ILE ILE A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 ALA 293 293 293 ALA ALA A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 ALA 296 296 296 ALA ALA A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 THR 298 298 298 THR THR A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 TRP 300 300 300 TRP TRP A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 GLN 302 302 302 GLN GLN A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 PRO 308 308 308 PRO PRO A . n 
A 1 309 ASP 309 309 309 ASP ASP A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 THR 312 312 312 THR THR A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 GLU 315 315 315 GLU GLU A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 ASP 317 317 317 ASP ASP A . n 
A 1 318 MET 318 318 318 MET MET A . n 
A 1 319 ILE 319 319 319 ILE ILE A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 PRO 321 321 321 PRO PRO A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 GLN 325 325 325 GLN GLN A . n 
A 1 326 TYR 326 326 326 TYR TYR A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 CYS 328 328 328 CYS CYS A . n 
A 1 329 PRO 329 329 329 PRO PRO A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 TYR 331 331 331 TYR TYR A . n 
A 1 332 ILE 332 332 332 ILE ILE A . n 
A 1 333 SER 333 333 333 SER SER A . n 
A 1 334 PHE 334 334 334 PHE PHE A . n 
A 1 335 PHE 335 335 335 PHE PHE A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 ALA 339 339 339 ALA ALA A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 MET 345 345 345 MET MET A . n 
A 1 346 SER 346 346 346 SER SER A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 SER 350 350 350 SER SER A . n 
A 1 351 SER 351 351 351 SER SER A . n 
A 1 352 ILE 352 352 352 ILE ILE A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 SER 354 354 354 SER SER A . n 
A 1 355 ALA 355 355 355 ALA ALA A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 MET 358 358 358 MET MET A . n 
A 1 359 PHE 359 359 359 PHE PHE A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 ARG 361 361 361 ARG ARG A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 TYR 364 364 364 TYR TYR A . n 
A 1 365 GLN 365 365 365 GLN GLN A . n 
A 1 366 LEU 366 366 366 LEU LEU A . n 
A 1 367 SER 367 367 367 SER SER A . n 
A 1 368 PHE 368 368 368 PHE PHE A . n 
A 1 369 ARG 369 369 369 ARG ARG A . n 
A 1 370 GLN 370 370 370 GLN GLN A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 ILE 377 377 377 ILE ILE A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 TRP 379 379 379 TRP TRP A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 MET 381 381 381 MET MET A . n 
A 1 382 ARG 382 382 382 ARG ARG A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 PHE 386 386 386 PHE PHE A . n 
A 1 387 VAL 387 387 387 VAL VAL A . n 
A 1 388 PHE 388 388 388 PHE PHE A . n 
A 1 389 GLY 389 389 389 GLY GLY A . n 
A 1 390 ALA 390 390 390 ALA ALA A . n 
A 1 391 SER 391 391 391 SER SER A . n 
A 1 392 ALA 392 392 392 ALA ALA A . n 
A 1 393 THR 393 393 393 THR THR A . n 
A 1 394 ALA 394 394 394 ALA ALA A . n 
A 1 395 MET 395 395 395 MET MET A . n 
A 1 396 ALA 396 396 396 ALA ALA A . n 
A 1 397 LEU 397 397 397 LEU LEU A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 LYS 400 400 400 LYS LYS A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 TYR 403 403 403 TYR TYR A . n 
A 1 404 GLY 404 404 404 GLY GLY A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 TRP 406 406 406 TRP TRP A . n 
A 1 407 TYR 407 407 407 TYR TYR A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 SER 409 409 409 SER SER A . n 
A 1 410 SER 410 410 410 SER SER A . n 
A 1 411 ASP 411 411 411 ASP ASP A . n 
A 1 412 LEU 412 412 412 LEU LEU A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 TYR 414 414 414 TYR TYR A . n 
A 1 415 ILE 415 415 415 ILE ILE 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 PHE 418 418 418 PHE PHE A . n 
A 1 419 PRO 419 419 419 PRO PRO A . n 
A 1 420 GLN 420 420 420 GLN GLN A . n 
A 1 421 LEU 421 421 421 LEU LEU A . n 
A 1 422 LEU 422 422 422 LEU LEU A . n 
A 1 423 CYS 423 423 423 CYS CYS A . n 
A 1 424 VAL 424 424 424 VAL VAL A . n 
A 1 425 LEU 425 425 425 LEU LEU A . n 
A 1 426 PHE 426 426 426 PHE PHE A . n 
A 1 427 VAL 427 427 427 VAL VAL A . n 
A 1 428 LYS 428 428 428 LYS LYS A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 THR 430 430 430 THR THR A . n 
A 1 431 ASN 431 431 431 ASN ASN A . n 
A 1 432 THR 432 432 432 THR THR A . n 
A 1 433 TYR 433 433 433 TYR TYR A . n 
A 1 434 GLY 434 434 434 GLY GLY A . n 
A 1 435 ALA 435 435 435 ALA ALA A . n 
A 1 436 VAL 436 436 436 VAL VAL A . n 
A 1 437 ALA 437 437 437 ALA ALA A . n 
A 1 438 GLY 438 438 438 GLY GLY A . n 
A 1 439 TYR 439 439 439 TYR TYR A . n 
A 1 440 VAL 440 440 440 VAL VAL A . n 
A 1 441 SER 441 441 441 SER SER A . n 
A 1 442 GLY 442 442 442 GLY GLY A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 LEU 445 445 445 LEU LEU A . n 
A 1 446 ARG 446 446 446 ARG ARG A . n 
A 1 447 ILE 447 447 447 ILE ILE A . n 
A 1 448 THR 448 448 448 THR THR A . n 
A 1 449 GLY 449 449 449 GLY GLY A . n 
A 1 450 GLY 450 450 450 GLY GLY A . n 
A 1 451 GLU 451 451 451 GLU GLU A . n 
A 1 452 PRO 452 452 452 PRO PRO A . n 
A 1 453 TYR 453 453 453 TYR TYR A . n 
A 1 454 LEU 454 454 454 LEU LEU A . n 
A 1 455 TYR 455 455 455 TYR TYR A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 GLN 457 457 457 GLN GLN A . n 
A 1 458 PRO 458 458 458 PRO PRO A . n 
A 1 459 LEU 459 459 459 LEU LEU A . n 
A 1 460 ILE 460 460 460 ILE ILE A . n 
A 1 461 PHE 461 461 461 PHE PHE A . n 
A 1 462 TYR 462 462 462 TYR TYR A . n 
A 1 463 PRO 463 463 463 PRO PRO A . n 
A 1 464 GLY 464 464 464 GLY GLY A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 TYR 466 466 466 TYR TYR A . n 
A 1 467 PRO 467 467 467 PRO PRO A . n 
A 1 468 ASP 468 468 468 ASP ASP A . n 
A 1 469 ASP 469 469 469 ASP ASP A . n 
A 1 470 ASN 470 470 470 ASN ASN A . n 
A 1 471 GLY 471 471 471 GLY GLY A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 TYR 473 473 473 TYR TYR A . n 
A 1 474 ASN 474 474 474 ASN ASN A . n 
A 1 475 GLN 475 475 475 GLN GLN A . n 
A 1 476 LYS 476 476 476 LYS LYS A . n 
A 1 477 PHE 477 477 477 PHE PHE A . n 
A 1 478 PRO 478 478 478 PRO PRO A . n 
A 1 479 PHE 479 479 479 PHE PHE A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 ALA 483 483 483 ALA ALA A . n 
A 1 484 MET 484 484 484 MET MET A . n 
A 1 485 VAL 485 485 485 VAL VAL A . n 
A 1 486 THR 486 486 486 THR THR A . n 
A 1 487 SER 487 487 487 SER SER A . n 
A 1 488 PHE 488 488 488 PHE PHE A . n 
A 1 489 LEU 489 489 489 LEU LEU A . n 
A 1 490 THR 490 490 490 THR THR A . n 
A 1 491 ASN 491 491 491 ASN ASN A . n 
A 1 492 ILE 492 492 492 ILE ILE A . n 
A 1 493 CYS 493 493 493 CYS CYS A . n 
A 1 494 ILE 494 494 494 ILE ILE A . n 
A 1 495 SER 495 495 495 SER SER A . n 
A 1 496 TYR 496 496 496 TYR TYR A . n 
A 1 497 LEU 497 497 497 LEU LEU A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 LYS 499 499 499 LYS LYS A . n 
A 1 500 TYR 500 500 500 TYR TYR A . n 
A 1 501 LEU 501 501 501 LEU LEU A . n 
A 1 502 PHE 502 502 502 PHE PHE A . n 
A 1 503 GLU 503 503 503 GLU GLU A . n 
A 1 504 SER 504 504 504 SER SER A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 THR 506 506 506 THR THR A . n 
A 1 507 LEU 507 507 507 LEU LEU A . n 
A 1 508 PRO 508 508 508 PRO PRO A . n 
A 1 509 PRO 509 509 509 PRO PRO A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 LEU 511 511 511 LEU LEU A . n 
A 1 512 ASP 512 512 512 ASP ASP A . n 
A 1 513 VAL 513 513 513 VAL VAL A . n 
A 1 514 PHE 514 514 514 PHE PHE A . n 
A 1 515 ASP 515 515 515 ASP ASP A . n 
A 1 516 ALA 516 516 516 ALA ALA A . n 
A 1 517 VAL 517 517 517 VAL VAL A . n 
A 1 518 VAL 518 518 518 VAL VAL A . n 
A 1 519 ALA 519 519 519 ALA ALA A . n 
A 1 520 ARG 520 520 ?   ?   ?   A . n 
A 1 521 HIS 521 521 ?   ?   ?   A . n 
A 1 522 SER 522 522 ?   ?   ?   A . n 
A 1 523 GLU 523 523 ?   ?   ?   A . n 
A 1 524 GLU 524 524 ?   ?   ?   A . n 
A 1 525 ASN 525 525 ?   ?   ?   A . n 
A 1 526 MET 526 526 ?   ?   ?   A . n 
A 1 527 ASP 527 527 ?   ?   ?   A . n 
A 1 528 LYS 528 528 ?   ?   ?   A . n 
A 1 529 THR 529 529 ?   ?   ?   A . n 
A 1 530 ILE 530 530 ?   ?   ?   A . n 
A 1 531 LEU 531 531 ?   ?   ?   A . n 
A 1 532 VAL 532 532 ?   ?   ?   A . n 
A 1 533 LYS 533 533 ?   ?   ?   A . n 
A 1 534 ASN 534 534 ?   ?   ?   A . n 
A 1 535 GLU 535 535 ?   ?   ?   A . n 
A 1 536 ASN 536 536 ?   ?   ?   A . n 
A 1 537 ILE 537 537 ?   ?   ?   A . n 
A 1 538 LYS 538 538 ?   ?   ?   A . n 
A 1 539 LEU 539 539 ?   ?   ?   A . n 
A 1 540 ASP 540 540 ?   ?   ?   A . n 
A 1 541 GLU 541 541 ?   ?   ?   A . n 
A 1 542 LEU 542 542 ?   ?   ?   A . n 
A 1 543 ALA 543 543 ?   ?   ?   A . n 
A 1 544 LEU 544 544 ?   ?   ?   A . n 
A 1 545 VAL 545 545 ?   ?   ?   A . n 
A 1 546 LYS 546 546 ?   ?   ?   A . n 
A 1 547 PRO 547 547 ?   ?   ?   A . n 
A 1 548 ARG 548 548 ?   ?   ?   A . n 
A 1 549 GLN 549 549 ?   ?   ?   A . n 
A 1 550 SER 550 550 ?   ?   ?   A . n 
A 1 551 MET 551 551 ?   ?   ?   A . n 
A 1 552 THR 552 552 ?   ?   ?   A . n 
A 1 553 LEU 553 553 ?   ?   ?   A . n 
A 1 554 SER 554 554 ?   ?   ?   A . n 
A 1 555 SER 555 555 ?   ?   ?   A . n 
A 1 556 THR 556 556 ?   ?   ?   A . n 
A 1 557 PHE 557 557 ?   ?   ?   A . n 
A 1 558 THR 558 558 ?   ?   ?   A . n 
A 1 559 ASN 559 559 ?   ?   ?   A . n 
A 1 560 LYS 560 560 ?   ?   ?   A . n 
A 1 561 GLU 561 561 ?   ?   ?   A . n 
A 1 562 ALA 562 562 ?   ?   ?   A . n 
A 1 563 PHE 563 563 ?   ?   ?   A . n 
A 1 564 LEU 564 564 ?   ?   ?   A . n 
A 1 565 ASP 565 565 ?   ?   ?   A . n 
A 1 566 VAL 566 566 ?   ?   ?   A . n 
A 1 567 ASP 567 567 ?   ?   ?   A . n 
A 1 568 SER 568 568 ?   ?   ?   A . n 
A 1 569 SER 569 569 ?   ?   ?   A . n 
A 1 570 PRO 570 570 ?   ?   ?   A . n 
A 1 571 GLU 571 571 ?   ?   ?   A . n 
A 1 572 GLY 572 572 ?   ?   ?   A . n 
A 1 573 SER 573 573 ?   ?   ?   A . n 
A 1 574 GLY 574 574 ?   ?   ?   A . n 
A 1 575 THR 575 575 ?   ?   ?   A . n 
A 1 576 GLU 576 576 ?   ?   ?   A . n 
A 1 577 ASP 577 577 ?   ?   ?   A . n 
A 1 578 ASN 578 578 ?   ?   ?   A . n 
A 1 579 LEU 579 579 ?   ?   ?   A . n 
A 1 580 GLN 580 580 ?   ?   ?   A . n 
A 1 581 ALA 581 581 ?   ?   ?   A . n 
A 1 582 ALA 582 582 ?   ?   ?   A . n 
A 1 583 ALA 583 583 ?   ?   ?   A . n 
A 1 584 GLY 584 584 ?   ?   ?   A . n 
A 1 585 GLY 585 585 ?   ?   ?   A . n 
A 1 586 SER 586 586 ?   ?   ?   A . n 
A 1 587 TRP 587 587 ?   ?   ?   A . n 
A 1 588 SER 588 588 ?   ?   ?   A . n 
A 1 589 HIS 589 589 ?   ?   ?   A . n 
A 1 590 PRO 590 590 ?   ?   ?   A . n 
A 1 591 GLN 591 591 ?   ?   ?   A . n 
A 1 592 PHE 592 592 ?   ?   ?   A . n 
A 1 593 GLU 593 593 ?   ?   ?   A . n 
A 1 594 LYS 594 594 ?   ?   ?   A . n 
A 1 595 GLY 595 595 ?   ?   ?   A . n 
A 1 596 GLY 596 596 ?   ?   ?   A . n 
A 1 597 GLY 597 597 ?   ?   ?   A . n 
A 1 598 SER 598 598 ?   ?   ?   A . n 
A 1 599 GLY 599 599 ?   ?   ?   A . n 
A 1 600 GLY 600 600 ?   ?   ?   A . n 
A 1 601 GLY 601 601 ?   ?   ?   A . n 
A 1 602 SER 602 602 ?   ?   ?   A . n 
A 1 603 GLY 603 603 ?   ?   ?   A . n 
A 1 604 GLY 604 604 ?   ?   ?   A . n 
A 1 605 SER 605 605 ?   ?   ?   A . n 
A 1 606 ALA 606 606 ?   ?   ?   A . n 
A 1 607 TRP 607 607 ?   ?   ?   A . n 
A 1 608 SER 608 608 ?   ?   ?   A . n 
A 1 609 HIS 609 609 ?   ?   ?   A . n 
A 1 610 PRO 610 610 ?   ?   ?   A . n 
A 1 611 GLN 611 611 ?   ?   ?   A . n 
A 1 612 PHE 612 612 ?   ?   ?   A . n 
A 1 613 GLU 613 613 ?   ?   ?   A . n 
A 1 614 LYS 614 614 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HC6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HC6 
_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          HC6 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     701 
_pdbx_nonpoly_scheme.auth_seq_num    601 
_pdbx_nonpoly_scheme.pdb_mon_id      HC6 
_pdbx_nonpoly_scheme.auth_mon_id     HC6 
_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                     9BIM 
_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                         9BIM 
_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                   9BIM 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9BIM 
_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 ? 4106 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.730 ? 5614 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.582 ? 564  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.045 ? 647  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.005 ? 680  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BIM 
_struct.title                        'Cryo-EM structure of human CHT1 in the HC-3 bound outward-facing state' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BIM 
_struct_keywords.text            'Choline transporter, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SC5A7_HUMAN 
_struct_ref.pdbx_db_accession          Q9GZV3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGY
GLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVD
MHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSW
LDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMIL
PIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTK
TVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFK
TLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNK
EAFLDVDSSPEGSGTEDNLQ
;
_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              9BIM 
_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                 580 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9GZV3 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  580 
_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       580 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BIM ALA A 581 ? UNP Q9GZV3 ? ? 'expression tag' 581 1  
1 9BIM ALA A 582 ? UNP Q9GZV3 ? ? 'expression tag' 582 2  
1 9BIM ALA A 583 ? UNP Q9GZV3 ? ? 'expression tag' 583 3  
1 9BIM GLY A 584 ? UNP Q9GZV3 ? ? 'expression tag' 584 4  
1 9BIM GLY A 585 ? UNP Q9GZV3 ? ? 'expression tag' 585 5  
1 9BIM SER A 586 ? UNP Q9GZV3 ? ? 'expression tag' 586 6  
1 9BIM TRP A 587 ? UNP Q9GZV3 ? ? 'expression tag' 587 7  
1 9BIM SER A 588 ? UNP Q9GZV3 ? ? 'expression tag' 588 8  
1 9BIM HIS A 589 ? UNP Q9GZV3 ? ? 'expression tag' 589 9  
1 9BIM PRO A 590 ? UNP Q9GZV3 ? ? 'expression tag' 590 10 
1 9BIM GLN A 591 ? UNP Q9GZV3 ? ? 'expression tag' 591 11 
1 9BIM PHE A 592 ? UNP Q9GZV3 ? ? 'expression tag' 592 12 
1 9BIM GLU A 593 ? UNP Q9GZV3 ? ? 'expression tag' 593 13 
1 9BIM LYS A 594 ? UNP Q9GZV3 ? ? 'expression tag' 594 14 
1 9BIM GLY A 595 ? UNP Q9GZV3 ? ? 'expression tag' 595 15 
1 9BIM GLY A 596 ? UNP Q9GZV3 ? ? 'expression tag' 596 16 
1 9BIM GLY A 597 ? UNP Q9GZV3 ? ? 'expression tag' 597 17 
1 9BIM SER A 598 ? UNP Q9GZV3 ? ? 'expression tag' 598 18 
1 9BIM GLY A 599 ? UNP Q9GZV3 ? ? 'expression tag' 599 19 
1 9BIM GLY A 600 ? UNP Q9GZV3 ? ? 'expression tag' 600 20 
1 9BIM GLY A 601 ? UNP Q9GZV3 ? ? 'expression tag' 601 21 
1 9BIM SER A 602 ? UNP Q9GZV3 ? ? 'expression tag' 602 22 
1 9BIM GLY A 603 ? UNP Q9GZV3 ? ? 'expression tag' 603 23 
1 9BIM GLY A 604 ? UNP Q9GZV3 ? ? 'expression tag' 604 24 
1 9BIM SER A 605 ? UNP Q9GZV3 ? ? 'expression tag' 605 25 
1 9BIM ALA A 606 ? UNP Q9GZV3 ? ? 'expression tag' 606 26 
1 9BIM TRP A 607 ? UNP Q9GZV3 ? ? 'expression tag' 607 27 
1 9BIM SER A 608 ? UNP Q9GZV3 ? ? 'expression tag' 608 28 
1 9BIM HIS A 609 ? UNP Q9GZV3 ? ? 'expression tag' 609 29 
1 9BIM PRO A 610 ? UNP Q9GZV3 ? ? 'expression tag' 610 30 
1 9BIM GLN A 611 ? UNP Q9GZV3 ? ? 'expression tag' 611 31 
1 9BIM PHE A 612 ? UNP Q9GZV3 ? ? 'expression tag' 612 32 
1 9BIM GLU A 613 ? UNP Q9GZV3 ? ? 'expression tag' 613 33 
1 9BIM LYS A 614 ? UNP Q9GZV3 ? ? 'expression tag' 614 34 
# 
_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 HIS A 4   ? THR A 29  ? HIS A 4   THR A 29  1 ? 26 
HELX_P HELX_P2  AA2 SER A 39  ? VAL A 44  ? SER A 39  VAL A 44  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 51  ? VAL A 63  ? LEU A 51  VAL A 63  1 ? 13 
HELX_P HELX_P4  AA4 GLY A 64  ? VAL A 77  ? GLY A 64  VAL A 77  1 ? 14 
HELX_P HELX_P5  AA5 GLY A 81  ? ALA A 85  ? GLY A 81  ALA A 85  5 ? 5  
HELX_P HELX_P6  AA6 GLN A 86  ? PHE A 102 ? GLN A 86  PHE A 102 1 ? 17 
HELX_P HELX_P7  AA7 PHE A 102 ? LYS A 109 ? PHE A 102 LYS A 109 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 115 ? ILE A 157 ? LEU A 115 ILE A 157 1 ? 43 
HELX_P HELX_P9  AA9 ASP A 160 ? GLY A 179 ? ASP A 160 GLY A 179 1 ? 20 
HELX_P HELX_P10 AB1 THR A 187 ? SER A 208 ? THR A 187 SER A 208 1 ? 22 
HELX_P HELX_P11 AB2 ASP A 214 ? HIS A 221 ? ASP A 214 HIS A 221 1 ? 8  
HELX_P HELX_P12 AB3 GLU A 236 ? GLY A 250 ? GLU A 236 GLY A 250 1 ? 15 
HELX_P HELX_P13 AB4 TRP A 254 ? SER A 263 ? TRP A 254 SER A 263 1 ? 10 
HELX_P HELX_P14 AB5 ALA A 267 ? THR A 298 ? ALA A 267 THR A 298 1 ? 32 
HELX_P HELX_P15 AB6 ILE A 319 ? LEU A 327 ? ILE A 319 LEU A 327 1 ? 9  
HELX_P HELX_P16 AB7 PRO A 329 ? ALA A 360 ? PRO A 329 ALA A 360 1 ? 32 
HELX_P HELX_P17 AB8 SER A 373 ? THR A 399 ? SER A 373 THR A 399 1 ? 27 
HELX_P HELX_P18 AB9 THR A 401 ? PHE A 426 ? THR A 401 PHE A 426 1 ? 26 
HELX_P HELX_P19 AC1 ASN A 431 ? GLY A 450 ? ASN A 431 GLY A 450 1 ? 20 
HELX_P HELX_P20 AC2 PRO A 478 ? GLY A 505 ? PRO A 478 GLY A 505 1 ? 28 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           307 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            307 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    308 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     308 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       5.03 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 466 ? PRO A 467 ? TYR A 466 PRO A 467 
AA1 2 TYR A 473 ? ASN A 474 ? TYR A 473 ASN A 474 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   TYR 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    466 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    TYR 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     466 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   ASN 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    474 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    ASN 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     474 
# 
_pdbx_entry_details.entry_id                   9BIM 
_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 
# 
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 LEU A 181 ? ? 59.23  -2.19  
2 1 VAL A 416 ? ? -92.81 -60.73 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BIM 
_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                    9BIM 
_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                  3.67 
_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               191427 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 'ORGANELLE OR CELLULAR COMPONENT' 
_em_entity_assembly.name                 'human CHT1 in the HC-3 bound state' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9BIM 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             800 
_em_imaging.nominal_defocus_max             1800 
_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              9BIM 
_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            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9BIM 
_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 ASN 31  ? A ASN 31  
3  1 Y 1 A SER 32  ? A SER 32  
4  1 Y 1 A ARG 520 ? A ARG 520 
5  1 Y 1 A HIS 521 ? A HIS 521 
6  1 Y 1 A SER 522 ? A SER 522 
7  1 Y 1 A GLU 523 ? A GLU 523 
8  1 Y 1 A GLU 524 ? A GLU 524 
9  1 Y 1 A ASN 525 ? A ASN 525 
10 1 Y 1 A MET 526 ? A MET 526 
11 1 Y 1 A ASP 527 ? A ASP 527 
12 1 Y 1 A LYS 528 ? A LYS 528 
13 1 Y 1 A THR 529 ? A THR 529 
14 1 Y 1 A ILE 530 ? A ILE 530 
15 1 Y 1 A LEU 531 ? A LEU 531 
16 1 Y 1 A VAL 532 ? A VAL 532 
17 1 Y 1 A LYS 533 ? A LYS 533 
18 1 Y 1 A ASN 534 ? A ASN 534 
19 1 Y 1 A GLU 535 ? A GLU 535 
20 1 Y 1 A ASN 536 ? A ASN 536 
21 1 Y 1 A ILE 537 ? A ILE 537 
22 1 Y 1 A LYS 538 ? A LYS 538 
23 1 Y 1 A LEU 539 ? A LEU 539 
24 1 Y 1 A ASP 540 ? A ASP 540 
25 1 Y 1 A GLU 541 ? A GLU 541 
26 1 Y 1 A LEU 542 ? A LEU 542 
27 1 Y 1 A ALA 543 ? A ALA 543 
28 1 Y 1 A LEU 544 ? A LEU 544 
29 1 Y 1 A VAL 545 ? A VAL 545 
30 1 Y 1 A LYS 546 ? A LYS 546 
31 1 Y 1 A PRO 547 ? A PRO 547 
32 1 Y 1 A ARG 548 ? A ARG 548 
33 1 Y 1 A GLN 549 ? A GLN 549 
34 1 Y 1 A SER 550 ? A SER 550 
35 1 Y 1 A MET 551 ? A MET 551 
36 1 Y 1 A THR 552 ? A THR 552 
37 1 Y 1 A LEU 553 ? A LEU 553 
38 1 Y 1 A SER 554 ? A SER 554 
39 1 Y 1 A SER 555 ? A SER 555 
40 1 Y 1 A THR 556 ? A THR 556 
41 1 Y 1 A PHE 557 ? A PHE 557 
42 1 Y 1 A THR 558 ? A THR 558 
43 1 Y 1 A ASN 559 ? A ASN 559 
44 1 Y 1 A LYS 560 ? A LYS 560 
45 1 Y 1 A GLU 561 ? A GLU 561 
46 1 Y 1 A ALA 562 ? A ALA 562 
47 1 Y 1 A PHE 563 ? A PHE 563 
48 1 Y 1 A LEU 564 ? A LEU 564 
49 1 Y 1 A ASP 565 ? A ASP 565 
50 1 Y 1 A VAL 566 ? A VAL 566 
51 1 Y 1 A ASP 567 ? A ASP 567 
52 1 Y 1 A SER 568 ? A SER 568 
53 1 Y 1 A SER 569 ? A SER 569 
54 1 Y 1 A PRO 570 ? A PRO 570 
55 1 Y 1 A GLU 571 ? A GLU 571 
56 1 Y 1 A GLY 572 ? A GLY 572 
57 1 Y 1 A SER 573 ? A SER 573 
58 1 Y 1 A GLY 574 ? A GLY 574 
59 1 Y 1 A THR 575 ? A THR 575 
60 1 Y 1 A GLU 576 ? A GLU 576 
61 1 Y 1 A ASP 577 ? A ASP 577 
62 1 Y 1 A ASN 578 ? A ASN 578 
63 1 Y 1 A LEU 579 ? A LEU 579 
64 1 Y 1 A GLN 580 ? A GLN 580 
65 1 Y 1 A ALA 581 ? A ALA 581 
66 1 Y 1 A ALA 582 ? A ALA 582 
67 1 Y 1 A ALA 583 ? A ALA 583 
68 1 Y 1 A GLY 584 ? A GLY 584 
69 1 Y 1 A GLY 585 ? A GLY 585 
70 1 Y 1 A SER 586 ? A SER 586 
71 1 Y 1 A TRP 587 ? A TRP 587 
72 1 Y 1 A SER 588 ? A SER 588 
73 1 Y 1 A HIS 589 ? A HIS 589 
74 1 Y 1 A PRO 590 ? A PRO 590 
75 1 Y 1 A GLN 591 ? A GLN 591 
76 1 Y 1 A PHE 592 ? A PHE 592 
77 1 Y 1 A GLU 593 ? A GLU 593 
78 1 Y 1 A LYS 594 ? A LYS 594 
79 1 Y 1 A GLY 595 ? A GLY 595 
80 1 Y 1 A GLY 596 ? A GLY 596 
81 1 Y 1 A GLY 597 ? A GLY 597 
82 1 Y 1 A SER 598 ? A SER 598 
83 1 Y 1 A GLY 599 ? A GLY 599 
84 1 Y 1 A GLY 600 ? A GLY 600 
85 1 Y 1 A GLY 601 ? A GLY 601 
86 1 Y 1 A SER 602 ? A SER 602 
87 1 Y 1 A GLY 603 ? A GLY 603 
88 1 Y 1 A GLY 604 ? A GLY 604 
89 1 Y 1 A SER 605 ? A SER 605 
90 1 Y 1 A ALA 606 ? A ALA 606 
91 1 Y 1 A TRP 607 ? A TRP 607 
92 1 Y 1 A SER 608 ? A SER 608 
93 1 Y 1 A HIS 609 ? A HIS 609 
94 1 Y 1 A PRO 610 ? A PRO 610 
95 1 Y 1 A GLN 611 ? A GLN 611 
96 1 Y 1 A PHE 612 ? A PHE 612 
97 1 Y 1 A GLU 613 ? A GLU 613 
98 1 Y 1 A LYS 614 ? A LYS 614 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HC6 CAC  C N N 137 
HC6 NAA  N N N 138 
HC6 CBA  C N N 139 
HC6 CBB  C N N 140 
HC6 CAB  C N N 141 
HC6 CAF  C N N 142 
HC6 OAE  O N N 143 
HC6 CAD  C N S 144 
HC6 OBC  O N N 145 
HC6 CAG  C Y N 146 
HC6 CAL  C Y N 147 
HC6 CAK  C Y N 148 
HC6 CAH  C Y N 149 
HC6 CAI  C Y N 150 
HC6 CAJ  C Y N 151 
HC6 CAM  C Y N 152 
HC6 CAR  C Y N 153 
HC6 CAQ  C Y N 154 
HC6 CAN  C Y N 155 
HC6 CAO  C Y N 156 
HC6 CAP  C Y N 157 
HC6 CAS  C N S 158 
HC6 OBD  O N N 159 
HC6 CAX  C N N 160 
HC6 OAT  O N N 161 
HC6 CAU  C N N 162 
HC6 CAV  C N N 163 
HC6 NAW  N N N 164 
HC6 CAZ  C N N 165 
HC6 CAY  C N N 166 
HC6 HAC  H N N 167 
HC6 HACA H N N 168 
HC6 HBA  H N N 169 
HC6 HBAA H N N 170 
HC6 HBAB H N N 171 
HC6 HBB  H N N 172 
HC6 HBBA H N N 173 
HC6 HBBB H N N 174 
HC6 HAB  H N N 175 
HC6 HABA H N N 176 
HC6 HAF  H N N 177 
HC6 HAFA H N N 178 
HC6 HAL  H N N 179 
HC6 HAK  H N N 180 
HC6 HAH  H N N 181 
HC6 HAI  H N N 182 
HC6 HAR  H N N 183 
HC6 HAQ  H N N 184 
HC6 HAN  H N N 185 
HC6 HAO  H N N 186 
HC6 HAX  H N N 187 
HC6 HAXA H N N 188 
HC6 HAU  H N N 189 
HC6 HAUA H N N 190 
HC6 HAV  H N N 191 
HC6 HAVA H N N 192 
HC6 HAZ  H N N 193 
HC6 HAZA H N N 194 
HC6 HAZB H N N 195 
HC6 HAY  H N N 196 
HC6 HAYA H N N 197 
HC6 HAYB H N N 198 
HC6 H33  H N N 199 
HC6 H34  H N N 200 
HIS N    N N N 201 
HIS CA   C N S 202 
HIS C    C N N 203 
HIS O    O N N 204 
HIS CB   C N N 205 
HIS CG   C Y N 206 
HIS ND1  N Y N 207 
HIS CD2  C Y N 208 
HIS CE1  C Y N 209 
HIS NE2  N Y N 210 
HIS OXT  O N N 211 
HIS H    H N N 212 
HIS H2   H N N 213 
HIS HA   H N N 214 
HIS HB2  H N N 215 
HIS HB3  H N N 216 
HIS HD1  H N N 217 
HIS HD2  H N N 218 
HIS HE1  H N N 219 
HIS HE2  H N N 220 
HIS HXT  H N N 221 
ILE N    N N N 222 
ILE CA   C N S 223 
ILE C    C N N 224 
ILE O    O N N 225 
ILE CB   C N S 226 
ILE CG1  C N N 227 
ILE CG2  C N N 228 
ILE CD1  C N N 229 
ILE OXT  O N N 230 
ILE H    H N N 231 
ILE H2   H N N 232 
ILE HA   H N N 233 
ILE HB   H N N 234 
ILE HG12 H N N 235 
ILE HG13 H N N 236 
ILE HG21 H N N 237 
ILE HG22 H N N 238 
ILE HG23 H N N 239 
ILE HD11 H N N 240 
ILE HD12 H N N 241 
ILE HD13 H N N 242 
ILE HXT  H N N 243 
LEU N    N N N 244 
LEU CA   C N S 245 
LEU C    C N N 246 
LEU O    O N N 247 
LEU CB   C N N 248 
LEU CG   C N N 249 
LEU CD1  C N N 250 
LEU CD2  C N N 251 
LEU OXT  O N N 252 
LEU H    H N N 253 
LEU H2   H N N 254 
LEU HA   H N N 255 
LEU HB2  H N N 256 
LEU HB3  H N N 257 
LEU HG   H N N 258 
LEU HD11 H N N 259 
LEU HD12 H N N 260 
LEU HD13 H N N 261 
LEU HD21 H N N 262 
LEU HD22 H N N 263 
LEU HD23 H N N 264 
LEU HXT  H N N 265 
LYS N    N N N 266 
LYS CA   C N S 267 
LYS C    C N N 268 
LYS O    O N N 269 
LYS CB   C N N 270 
LYS CG   C N N 271 
LYS CD   C N N 272 
LYS CE   C N N 273 
LYS NZ   N N N 274 
LYS OXT  O N N 275 
LYS H    H N N 276 
LYS H2   H N N 277 
LYS HA   H N N 278 
LYS HB2  H N N 279 
LYS HB3  H N N 280 
LYS HG2  H N N 281 
LYS HG3  H N N 282 
LYS HD2  H N N 283 
LYS HD3  H N N 284 
LYS HE2  H N N 285 
LYS HE3  H N N 286 
LYS HZ1  H N N 287 
LYS HZ2  H N N 288 
LYS HZ3  H N N 289 
LYS HXT  H N N 290 
MET N    N N N 291 
MET CA   C N S 292 
MET C    C N N 293 
MET O    O N N 294 
MET CB   C N N 295 
MET CG   C N N 296 
MET SD   S N N 297 
MET CE   C N N 298 
MET OXT  O N N 299 
MET H    H N N 300 
MET H2   H N N 301 
MET HA   H N N 302 
MET HB2  H N N 303 
MET HB3  H N N 304 
MET HG2  H N N 305 
MET HG3  H N N 306 
MET HE1  H N N 307 
MET HE2  H N N 308 
MET HE3  H N N 309 
MET HXT  H N N 310 
PHE N    N N N 311 
PHE CA   C N S 312 
PHE C    C N N 313 
PHE O    O N N 314 
PHE CB   C N N 315 
PHE CG   C Y N 316 
PHE CD1  C Y N 317 
PHE CD2  C Y N 318 
PHE CE1  C Y N 319 
PHE CE2  C Y N 320 
PHE CZ   C Y N 321 
PHE OXT  O N N 322 
PHE H    H N N 323 
PHE H2   H N N 324 
PHE HA   H N N 325 
PHE HB2  H N N 326 
PHE HB3  H N N 327 
PHE HD1  H N N 328 
PHE HD2  H N N 329 
PHE HE1  H N N 330 
PHE HE2  H N N 331 
PHE HZ   H N N 332 
PHE HXT  H N N 333 
PRO N    N N N 334 
PRO CA   C N S 335 
PRO C    C N N 336 
PRO O    O N N 337 
PRO CB   C N N 338 
PRO CG   C N N 339 
PRO CD   C N N 340 
PRO OXT  O N N 341 
PRO H    H N N 342 
PRO HA   H N N 343 
PRO HB2  H N N 344 
PRO HB3  H N N 345 
PRO HG2  H N N 346 
PRO HG3  H N N 347 
PRO HD2  H N N 348 
PRO HD3  H N N 349 
PRO HXT  H N N 350 
SER N    N N N 351 
SER CA   C N S 352 
SER C    C N N 353 
SER O    O N N 354 
SER CB   C N N 355 
SER OG   O N N 356 
SER OXT  O N N 357 
SER H    H N N 358 
SER H2   H N N 359 
SER HA   H N N 360 
SER HB2  H N N 361 
SER HB3  H N N 362 
SER HG   H N N 363 
SER HXT  H N N 364 
THR N    N N N 365 
THR CA   C N S 366 
THR C    C N N 367 
THR O    O N N 368 
THR CB   C N R 369 
THR OG1  O N N 370 
THR CG2  C N N 371 
THR OXT  O N N 372 
THR H    H N N 373 
THR H2   H N N 374 
THR HA   H N N 375 
THR HB   H N N 376 
THR HG1  H N N 377 
THR HG21 H N N 378 
THR HG22 H N N 379 
THR HG23 H N N 380 
THR HXT  H N N 381 
TRP N    N N N 382 
TRP CA   C N S 383 
TRP C    C N N 384 
TRP O    O N N 385 
TRP CB   C N N 386 
TRP CG   C Y N 387 
TRP CD1  C Y N 388 
TRP CD2  C Y N 389 
TRP NE1  N Y N 390 
TRP CE2  C Y N 391 
TRP CE3  C Y N 392 
TRP CZ2  C Y N 393 
TRP CZ3  C Y N 394 
TRP CH2  C Y N 395 
TRP OXT  O N N 396 
TRP H    H N N 397 
TRP H2   H N N 398 
TRP HA   H N N 399 
TRP HB2  H N N 400 
TRP HB3  H N N 401 
TRP HD1  H N N 402 
TRP HE1  H N N 403 
TRP HE3  H N N 404 
TRP HZ2  H N N 405 
TRP HZ3  H N N 406 
TRP HH2  H N N 407 
TRP HXT  H N N 408 
TYR N    N N N 409 
TYR CA   C N S 410 
TYR C    C N N 411 
TYR O    O N N 412 
TYR CB   C N N 413 
TYR CG   C Y N 414 
TYR CD1  C Y N 415 
TYR CD2  C Y N 416 
TYR CE1  C Y N 417 
TYR CE2  C Y N 418 
TYR CZ   C Y N 419 
TYR OH   O N N 420 
TYR OXT  O N N 421 
TYR H    H N N 422 
TYR H2   H N N 423 
TYR HA   H N N 424 
TYR HB2  H N N 425 
TYR HB3  H N N 426 
TYR HD1  H N N 427 
TYR HD2  H N N 428 
TYR HE1  H N N 429 
TYR HE2  H N N 430 
TYR HH   H N N 431 
TYR HXT  H N N 432 
VAL N    N N N 433 
VAL CA   C N S 434 
VAL C    C N N 435 
VAL O    O N N 436 
VAL CB   C N N 437 
VAL CG1  C N N 438 
VAL CG2  C N N 439 
VAL OXT  O N N 440 
VAL H    H N N 441 
VAL H2   H N N 442 
VAL HA   H N N 443 
VAL HB   H N N 444 
VAL HG11 H N N 445 
VAL HG12 H N N 446 
VAL HG13 H N N 447 
VAL HG21 H N N 448 
VAL HG22 H N N 449 
VAL HG23 H N N 450 
VAL HXT  H N N 451 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HC6 CAC NAA  sing N N 129 
HC6 CAC CAD  sing N N 130 
HC6 CAC HAC  sing N N 131 
HC6 CAC HACA sing N N 132 
HC6 NAA CBA  sing N N 133 
HC6 NAA CBB  sing N N 134 
HC6 NAA CAB  sing N N 135 
HC6 CBA HBA  sing N N 136 
HC6 CBA HBAA sing N N 137 
HC6 CBA HBAB sing N N 138 
HC6 CBB HBB  sing N N 139 
HC6 CBB HBBA sing N N 140 
HC6 CBB HBBB sing N N 141 
HC6 CAB CAF  sing N N 142 
HC6 CAB HAB  sing N N 143 
HC6 CAB HABA sing N N 144 
HC6 CAF OAE  sing N N 145 
HC6 CAF HAF  sing N N 146 
HC6 CAF HAFA sing N N 147 
HC6 OAE CAD  sing N N 148 
HC6 CAD OBC  sing N N 149 
HC6 CAD CAG  sing N N 150 
HC6 CAG CAL  doub Y N 151 
HC6 CAG CAH  sing Y N 152 
HC6 CAL CAK  sing Y N 153 
HC6 CAL HAL  sing N N 154 
HC6 CAK CAJ  doub Y N 155 
HC6 CAK HAK  sing N N 156 
HC6 CAH CAI  doub Y N 157 
HC6 CAH HAH  sing N N 158 
HC6 CAI CAJ  sing Y N 159 
HC6 CAI HAI  sing N N 160 
HC6 CAJ CAM  sing Y N 161 
HC6 CAM CAR  doub Y N 162 
HC6 CAM CAN  sing Y N 163 
HC6 CAR CAQ  sing Y N 164 
HC6 CAR HAR  sing N N 165 
HC6 CAQ CAP  doub Y N 166 
HC6 CAQ HAQ  sing N N 167 
HC6 CAN CAO  doub Y N 168 
HC6 CAN HAN  sing N N 169 
HC6 CAO CAP  sing Y N 170 
HC6 CAO HAO  sing N N 171 
HC6 CAP CAS  sing N N 172 
HC6 OBD CAS  sing N N 173 
HC6 CAS CAX  sing N N 174 
HC6 CAS OAT  sing N N 175 
HC6 CAX NAW  sing N N 176 
HC6 CAX HAX  sing N N 177 
HC6 CAX HAXA sing N N 178 
HC6 OAT CAU  sing N N 179 
HC6 CAU CAV  sing N N 180 
HC6 CAU HAU  sing N N 181 
HC6 CAU HAUA sing N N 182 
HC6 CAV NAW  sing N N 183 
HC6 CAV HAV  sing N N 184 
HC6 CAV HAVA sing N N 185 
HC6 NAW CAZ  sing N N 186 
HC6 NAW CAY  sing N N 187 
HC6 CAZ HAZ  sing N N 188 
HC6 CAZ HAZA sing N N 189 
HC6 CAZ HAZB sing N N 190 
HC6 CAY HAY  sing N N 191 
HC6 CAY HAYA sing N N 192 
HC6 CAY HAYB sing N N 193 
HC6 OBC H33  sing N N 194 
HC6 OBD H34  sing N N 195 
HIS N   CA   sing N N 196 
HIS N   H    sing N N 197 
HIS N   H2   sing N N 198 
HIS CA  C    sing N N 199 
HIS CA  CB   sing N N 200 
HIS CA  HA   sing N N 201 
HIS C   O    doub N N 202 
HIS C   OXT  sing N N 203 
HIS CB  CG   sing N N 204 
HIS CB  HB2  sing N N 205 
HIS CB  HB3  sing N N 206 
HIS CG  ND1  sing Y N 207 
HIS CG  CD2  doub Y N 208 
HIS ND1 CE1  doub Y N 209 
HIS ND1 HD1  sing N N 210 
HIS CD2 NE2  sing Y N 211 
HIS CD2 HD2  sing N N 212 
HIS CE1 NE2  sing Y N 213 
HIS CE1 HE1  sing N N 214 
HIS NE2 HE2  sing N N 215 
HIS OXT HXT  sing N N 216 
ILE N   CA   sing N N 217 
ILE N   H    sing N N 218 
ILE N   H2   sing N N 219 
ILE CA  C    sing N N 220 
ILE CA  CB   sing N N 221 
ILE CA  HA   sing N N 222 
ILE C   O    doub N N 223 
ILE C   OXT  sing N N 224 
ILE CB  CG1  sing N N 225 
ILE CB  CG2  sing N N 226 
ILE CB  HB   sing N N 227 
ILE CG1 CD1  sing N N 228 
ILE CG1 HG12 sing N N 229 
ILE CG1 HG13 sing N N 230 
ILE CG2 HG21 sing N N 231 
ILE CG2 HG22 sing N N 232 
ILE CG2 HG23 sing N N 233 
ILE CD1 HD11 sing N N 234 
ILE CD1 HD12 sing N N 235 
ILE CD1 HD13 sing N N 236 
ILE OXT HXT  sing N N 237 
LEU N   CA   sing N N 238 
LEU N   H    sing N N 239 
LEU N   H2   sing N N 240 
LEU CA  C    sing N N 241 
LEU CA  CB   sing N N 242 
LEU CA  HA   sing N N 243 
LEU C   O    doub N N 244 
LEU C   OXT  sing N N 245 
LEU CB  CG   sing N N 246 
LEU CB  HB2  sing N N 247 
LEU CB  HB3  sing N N 248 
LEU CG  CD1  sing N N 249 
LEU CG  CD2  sing N N 250 
LEU CG  HG   sing N N 251 
LEU CD1 HD11 sing N N 252 
LEU CD1 HD12 sing N N 253 
LEU CD1 HD13 sing N N 254 
LEU CD2 HD21 sing N N 255 
LEU CD2 HD22 sing N N 256 
LEU CD2 HD23 sing N N 257 
LEU OXT HXT  sing N N 258 
LYS N   CA   sing N N 259 
LYS N   H    sing N N 260 
LYS N   H2   sing N N 261 
LYS CA  C    sing N N 262 
LYS CA  CB   sing N N 263 
LYS CA  HA   sing N N 264 
LYS C   O    doub N N 265 
LYS C   OXT  sing N N 266 
LYS CB  CG   sing N N 267 
LYS CB  HB2  sing N N 268 
LYS CB  HB3  sing N N 269 
LYS CG  CD   sing N N 270 
LYS CG  HG2  sing N N 271 
LYS CG  HG3  sing N N 272 
LYS CD  CE   sing N N 273 
LYS CD  HD2  sing N N 274 
LYS CD  HD3  sing N N 275 
LYS CE  NZ   sing N N 276 
LYS CE  HE2  sing N N 277 
LYS CE  HE3  sing N N 278 
LYS NZ  HZ1  sing N N 279 
LYS NZ  HZ2  sing N N 280 
LYS NZ  HZ3  sing N N 281 
LYS OXT HXT  sing N N 282 
MET N   CA   sing N N 283 
MET N   H    sing N N 284 
MET N   H2   sing N N 285 
MET CA  C    sing N N 286 
MET CA  CB   sing N N 287 
MET CA  HA   sing N N 288 
MET C   O    doub N N 289 
MET C   OXT  sing N N 290 
MET CB  CG   sing N N 291 
MET CB  HB2  sing N N 292 
MET CB  HB3  sing N N 293 
MET CG  SD   sing N N 294 
MET CG  HG2  sing N N 295 
MET CG  HG3  sing N N 296 
MET SD  CE   sing N N 297 
MET CE  HE1  sing N N 298 
MET CE  HE2  sing N N 299 
MET CE  HE3  sing N N 300 
MET OXT HXT  sing N N 301 
PHE N   CA   sing N N 302 
PHE N   H    sing N N 303 
PHE N   H2   sing N N 304 
PHE CA  C    sing N N 305 
PHE CA  CB   sing N N 306 
PHE CA  HA   sing N N 307 
PHE C   O    doub N N 308 
PHE C   OXT  sing N N 309 
PHE CB  CG   sing N N 310 
PHE CB  HB2  sing N N 311 
PHE CB  HB3  sing N N 312 
PHE CG  CD1  doub Y N 313 
PHE CG  CD2  sing Y N 314 
PHE CD1 CE1  sing Y N 315 
PHE CD1 HD1  sing N N 316 
PHE CD2 CE2  doub Y N 317 
PHE CD2 HD2  sing N N 318 
PHE CE1 CZ   doub Y N 319 
PHE CE1 HE1  sing N N 320 
PHE CE2 CZ   sing Y N 321 
PHE CE2 HE2  sing N N 322 
PHE CZ  HZ   sing N N 323 
PHE OXT HXT  sing N N 324 
PRO N   CA   sing N N 325 
PRO N   CD   sing N N 326 
PRO N   H    sing N N 327 
PRO CA  C    sing N N 328 
PRO CA  CB   sing N N 329 
PRO CA  HA   sing N N 330 
PRO C   O    doub N N 331 
PRO C   OXT  sing N N 332 
PRO CB  CG   sing N N 333 
PRO CB  HB2  sing N N 334 
PRO CB  HB3  sing N N 335 
PRO CG  CD   sing N N 336 
PRO CG  HG2  sing N N 337 
PRO CG  HG3  sing N N 338 
PRO CD  HD2  sing N N 339 
PRO CD  HD3  sing N N 340 
PRO OXT HXT  sing N N 341 
SER N   CA   sing N N 342 
SER N   H    sing N N 343 
SER N   H2   sing N N 344 
SER CA  C    sing N N 345 
SER CA  CB   sing N N 346 
SER CA  HA   sing N N 347 
SER C   O    doub N N 348 
SER C   OXT  sing N N 349 
SER CB  OG   sing N N 350 
SER CB  HB2  sing N N 351 
SER CB  HB3  sing N N 352 
SER OG  HG   sing N N 353 
SER OXT HXT  sing N N 354 
THR N   CA   sing N N 355 
THR N   H    sing N N 356 
THR N   H2   sing N N 357 
THR CA  C    sing N N 358 
THR CA  CB   sing N N 359 
THR CA  HA   sing N N 360 
THR C   O    doub N N 361 
THR C   OXT  sing N N 362 
THR CB  OG1  sing N N 363 
THR CB  CG2  sing N N 364 
THR CB  HB   sing N N 365 
THR OG1 HG1  sing N N 366 
THR CG2 HG21 sing N N 367 
THR CG2 HG22 sing N N 368 
THR CG2 HG23 sing N N 369 
THR OXT HXT  sing N N 370 
TRP N   CA   sing N N 371 
TRP N   H    sing N N 372 
TRP N   H2   sing N N 373 
TRP CA  C    sing N N 374 
TRP CA  CB   sing N N 375 
TRP CA  HA   sing N N 376 
TRP C   O    doub N N 377 
TRP C   OXT  sing N N 378 
TRP CB  CG   sing N N 379 
TRP CB  HB2  sing N N 380 
TRP CB  HB3  sing N N 381 
TRP CG  CD1  doub Y N 382 
TRP CG  CD2  sing Y N 383 
TRP CD1 NE1  sing Y N 384 
TRP CD1 HD1  sing N N 385 
TRP CD2 CE2  doub Y N 386 
TRP CD2 CE3  sing Y N 387 
TRP NE1 CE2  sing Y N 388 
TRP NE1 HE1  sing N N 389 
TRP CE2 CZ2  sing Y N 390 
TRP CE3 CZ3  doub Y N 391 
TRP CE3 HE3  sing N N 392 
TRP CZ2 CH2  doub Y N 393 
TRP CZ2 HZ2  sing N N 394 
TRP CZ3 CH2  sing Y N 395 
TRP CZ3 HZ3  sing N N 396 
TRP CH2 HH2  sing N N 397 
TRP OXT HXT  sing N N 398 
TYR N   CA   sing N N 399 
TYR N   H    sing N N 400 
TYR N   H2   sing N N 401 
TYR CA  C    sing N N 402 
TYR CA  CB   sing N N 403 
TYR CA  HA   sing N N 404 
TYR C   O    doub N N 405 
TYR C   OXT  sing N N 406 
TYR CB  CG   sing N N 407 
TYR CB  HB2  sing N N 408 
TYR CB  HB3  sing N N 409 
TYR CG  CD1  doub Y N 410 
TYR CG  CD2  sing Y N 411 
TYR CD1 CE1  sing Y N 412 
TYR CD1 HD1  sing N N 413 
TYR CD2 CE2  doub Y N 414 
TYR CD2 HD2  sing N N 415 
TYR CE1 CZ   doub Y N 416 
TYR CE1 HE1  sing N N 417 
TYR CE2 CZ   sing Y N 418 
TYR CE2 HE2  sing N N 419 
TYR CZ  OH   sing N N 420 
TYR OH  HH   sing N N 421 
TYR OXT HXT  sing N N 422 
VAL N   CA   sing N N 423 
VAL N   H    sing N N 424 
VAL N   H2   sing N N 425 
VAL CA  C    sing N N 426 
VAL CA  CB   sing N N 427 
VAL CA  HA   sing N N 428 
VAL C   O    doub N N 429 
VAL C   OXT  sing N N 430 
VAL CB  CG1  sing N N 431 
VAL CB  CG2  sing N N 432 
VAL CB  HB   sing N N 433 
VAL CG1 HG11 sing N N 434 
VAL CG1 HG12 sing N N 435 
VAL CG1 HG13 sing N N 436 
VAL CG2 HG21 sing N N 437 
VAL CG2 HG22 sing N N 438 
VAL CG2 HG23 sing N N 439 
VAL OXT HXT  sing N N 440 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-23 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BIM 
_em_admin.last_update        2025-01-15 
_em_admin.map_release_date   2024-11-06 
_em_admin.title              'Cryo-EM structure of human CHT1 in the HC-3 bound outward-facing state' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R35GM140892 1 
'Welch Foundation'                                                                         'United States' I-1578      2 
'Howard Hughes Medical Institute (HHMI)'                                                   'United States' ?           3 
# 
_atom_sites.entry_id                    9BIM 
_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   . ALA A 1 2   ? 97.678  81.364  78.892  1.00 100.18 ? 2   ALA A N   1 
ATOM   2    C CA  . ALA A 1 2   ? 97.201  80.046  79.292  1.00 99.63  ? 2   ALA A CA  1 
ATOM   3    C C   . ALA A 1 2   ? 97.053  79.958  80.806  1.00 100.25 ? 2   ALA A C   1 
ATOM   4    O O   . ALA A 1 2   ? 97.439  80.875  81.530  1.00 100.96 ? 2   ALA A O   1 
ATOM   5    C CB  . ALA A 1 2   ? 98.143  78.965  78.787  1.00 98.15  ? 2   ALA A CB  1 
ATOM   6    N N   . PHE A 1 3   ? 96.491  78.848  81.279  1.00 101.23 ? 3   PHE A N   1 
ATOM   7    C CA  . PHE A 1 3   ? 96.288  78.610  82.704  1.00 101.76 ? 3   PHE A CA  1 
ATOM   8    C C   . PHE A 1 3   ? 97.368  77.651  83.193  1.00 102.47 ? 3   PHE A C   1 
ATOM   9    O O   . PHE A 1 3   ? 97.339  76.457  82.877  1.00 102.60 ? 3   PHE A O   1 
ATOM   10   C CB  . PHE A 1 3   ? 94.894  78.049  82.970  1.00 101.00 ? 3   PHE A CB  1 
ATOM   11   C CG  . PHE A 1 3   ? 94.523  78.013  84.425  1.00 99.56  ? 3   PHE A CG  1 
ATOM   12   C CD1 . PHE A 1 3   ? 95.012  78.966  85.302  1.00 98.29  ? 3   PHE A CD1 1 
ATOM   13   C CD2 . PHE A 1 3   ? 93.684  77.026  84.915  1.00 99.39  ? 3   PHE A CD2 1 
ATOM   14   C CE1 . PHE A 1 3   ? 94.673  78.936  86.640  1.00 97.50  ? 3   PHE A CE1 1 
ATOM   15   C CE2 . PHE A 1 3   ? 93.342  76.990  86.254  1.00 99.14  ? 3   PHE A CE2 1 
ATOM   16   C CZ  . PHE A 1 3   ? 93.837  77.947  87.116  1.00 98.36  ? 3   PHE A CZ  1 
ATOM   17   N N   . HIS A 1 4   ? 98.318  78.176  83.964  1.00 101.50 ? 4   HIS A N   1 
ATOM   18   C CA  . HIS A 1 4   ? 99.427  77.393  84.495  1.00 99.88  ? 4   HIS A CA  1 
ATOM   19   C C   . HIS A 1 4   ? 99.166  77.134  85.975  1.00 97.17  ? 4   HIS A C   1 
ATOM   20   O O   . HIS A 1 4   ? 99.170  78.068  86.784  1.00 96.47  ? 4   HIS A O   1 
ATOM   21   C CB  . HIS A 1 4   ? 100.751 78.125  84.283  1.00 100.98 ? 4   HIS A CB  1 
ATOM   22   C CG  . HIS A 1 4   ? 101.933 77.215  84.157  1.00 103.37 ? 4   HIS A CG  1 
ATOM   23   N ND1 . HIS A 1 4   ? 103.231 77.660  84.288  1.00 104.28 ? 4   HIS A ND1 1 
ATOM   24   C CD2 . HIS A 1 4   ? 102.014 75.887  83.908  1.00 104.76 ? 4   HIS A CD2 1 
ATOM   25   C CE1 . HIS A 1 4   ? 104.060 76.644  84.127  1.00 105.27 ? 4   HIS A CE1 1 
ATOM   26   N NE2 . HIS A 1 4   ? 103.347 75.557  83.895  1.00 105.78 ? 4   HIS A NE2 1 
ATOM   27   N N   . VAL A 1 5   ? 98.926  75.867  86.324  1.00 93.15  ? 5   VAL A N   1 
ATOM   28   C CA  . VAL A 1 5   ? 98.675  75.508  87.717  1.00 90.07  ? 5   VAL A CA  1 
ATOM   29   C C   . VAL A 1 5   ? 99.932  75.712  88.553  1.00 86.52  ? 5   VAL A C   1 
ATOM   30   O O   . VAL A 1 5   ? 99.886  76.288  89.650  1.00 83.63  ? 5   VAL A O   1 
ATOM   31   C CB  . VAL A 1 5   ? 98.161  74.061  87.812  1.00 90.54  ? 5   VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 5   ? 97.828  73.708  89.250  1.00 90.78  ? 5   VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 5   ? 96.947  73.871  86.916  1.00 90.73  ? 5   VAL A CG2 1 
ATOM   34   N N   . GLU A 1 6   ? 101.075 75.266  88.036  1.00 83.59  ? 6   GLU A N   1 
ATOM   35   C CA  . GLU A 1 6   ? 102.358 75.466  88.704  1.00 81.86  ? 6   GLU A CA  1 
ATOM   36   C C   . GLU A 1 6   ? 102.684 76.951  88.664  1.00 77.84  ? 6   GLU A C   1 
ATOM   37   O O   . GLU A 1 6   ? 103.113 77.485  87.640  1.00 79.74  ? 6   GLU A O   1 
ATOM   38   C CB  . GLU A 1 6   ? 103.449 74.637  88.036  1.00 83.84  ? 6   GLU A CB  1 
ATOM   39   C CG  . GLU A 1 6   ? 104.765 74.613  88.801  1.00 86.26  ? 6   GLU A CG  1 
ATOM   40   C CD  . GLU A 1 6   ? 104.630 74.011  90.188  1.00 88.40  ? 6   GLU A CD  1 
ATOM   41   O OE1 . GLU A 1 6   ? 103.858 73.041  90.348  1.00 90.21  ? 6   GLU A OE1 1 
ATOM   42   O OE2 . GLU A 1 6   ? 105.296 74.508  91.121  1.00 88.68  ? 6   GLU A OE2 1 
ATOM   43   N N   . GLY A 1 7   ? 102.481 77.617  89.793  1.00 71.86  ? 7   GLY A N   1 
ATOM   44   C CA  . GLY A 1 7   ? 102.585 79.056  89.896  1.00 69.17  ? 7   GLY A CA  1 
ATOM   45   C C   . GLY A 1 7   ? 101.357 79.608  90.586  1.00 66.61  ? 7   GLY A C   1 
ATOM   46   O O   . GLY A 1 7   ? 101.469 80.447  91.481  1.00 67.51  ? 7   GLY A O   1 
ATOM   47   N N   . LEU A 1 8   ? 100.179 79.084  90.236  1.00 63.51  ? 8   LEU A N   1 
ATOM   48   C CA  . LEU A 1 8   ? 99.018  79.285  91.094  1.00 61.85  ? 8   LEU A CA  1 
ATOM   49   C C   . LEU A 1 8   ? 99.225  78.590  92.432  1.00 60.81  ? 8   LEU A C   1 
ATOM   50   O O   . LEU A 1 8   ? 98.913  79.152  93.490  1.00 61.80  ? 8   LEU A O   1 
ATOM   51   C CB  . LEU A 1 8   ? 97.751  78.775  90.404  1.00 61.79  ? 8   LEU A CB  1 
ATOM   52   C CG  . LEU A 1 8   ? 96.416  78.963  91.131  1.00 61.97  ? 8   LEU A CG  1 
ATOM   53   C CD1 . LEU A 1 8   ? 95.346  79.385  90.148  1.00 62.65  ? 8   LEU A CD1 1 
ATOM   54   C CD2 . LEU A 1 8   ? 95.982  77.690  91.844  1.00 61.60  ? 8   LEU A CD2 1 
ATOM   55   N N   . ILE A 1 9   ? 99.769  77.370  92.396  1.00 57.83  ? 9   ILE A N   1 
ATOM   56   C CA  . ILE A 1 9   ? 100.148 76.678  93.625  1.00 54.77  ? 9   ILE A CA  1 
ATOM   57   C C   . ILE A 1 9   ? 101.209 77.475  94.375  1.00 52.66  ? 9   ILE A C   1 
ATOM   58   O O   . ILE A 1 9   ? 101.173 77.580  95.607  1.00 50.50  ? 9   ILE A O   1 
ATOM   59   C CB  . ILE A 1 9   ? 100.621 75.247  93.300  1.00 54.31  ? 9   ILE A CB  1 
ATOM   60   C CG1 . ILE A 1 9   ? 99.424  74.356  92.971  1.00 54.13  ? 9   ILE A CG1 1 
ATOM   61   C CG2 . ILE A 1 9   ? 101.410 74.646  94.452  1.00 54.80  ? 9   ILE A CG2 1 
ATOM   62   C CD1 . ILE A 1 9   ? 99.806  73.036  92.346  1.00 54.37  ? 9   ILE A CD1 1 
ATOM   63   N N   . ALA A 1 10  ? 102.152 78.076  93.641  1.00 51.19  ? 10  ALA A N   1 
ATOM   64   C CA  . ALA A 1 10  ? 103.203 78.870  94.273  1.00 49.82  ? 10  ALA A CA  1 
ATOM   65   C C   . ALA A 1 10  ? 102.637 80.101  94.972  1.00 48.64  ? 10  ALA A C   1 
ATOM   66   O O   . ALA A 1 10  ? 103.059 80.441  96.081  1.00 49.70  ? 10  ALA A O   1 
ATOM   67   C CB  . ALA A 1 10  ? 104.248 79.277  93.237  1.00 49.60  ? 10  ALA A CB  1 
ATOM   68   N N   . ILE A 1 11  ? 101.684 80.786  94.339  1.00 47.50  ? 11  ILE A N   1 
ATOM   69   C CA  . ILE A 1 11  ? 101.088 81.969  94.956  1.00 47.25  ? 11  ILE A CA  1 
ATOM   70   C C   . ILE A 1 11  ? 100.213 81.580  96.145  1.00 46.87  ? 11  ILE A C   1 
ATOM   71   O O   . ILE A 1 11  ? 100.168 82.294  97.154  1.00 46.59  ? 11  ILE A O   1 
ATOM   72   C CB  . ILE A 1 11  ? 100.327 82.790  93.899  1.00 47.25  ? 11  ILE A CB  1 
ATOM   73   C CG1 . ILE A 1 11  ? 101.335 83.490  92.991  1.00 48.12  ? 11  ILE A CG1 1 
ATOM   74   C CG2 . ILE A 1 11  ? 99.410  83.823  94.531  1.00 46.52  ? 11  ILE A CG2 1 
ATOM   75   C CD1 . ILE A 1 11  ? 100.726 84.139  91.796  1.00 48.28  ? 11  ILE A CD1 1 
ATOM   76   N N   . ILE A 1 12  ? 99.524  80.437  96.063  1.00 46.69  ? 12  ILE A N   1 
ATOM   77   C CA  . ILE A 1 12  ? 98.771  79.948  97.219  1.00 45.99  ? 12  ILE A CA  1 
ATOM   78   C C   . ILE A 1 12  ? 99.715  79.643  98.380  1.00 45.41  ? 12  ILE A C   1 
ATOM   79   O O   . ILE A 1 12  ? 99.426  79.968  99.541  1.00 45.28  ? 12  ILE A O   1 
ATOM   80   C CB  . ILE A 1 12  ? 97.925  78.723  96.825  1.00 45.79  ? 12  ILE A CB  1 
ATOM   81   C CG1 . ILE A 1 12  ? 96.746  79.153  95.951  1.00 45.59  ? 12  ILE A CG1 1 
ATOM   82   C CG2 . ILE A 1 12  ? 97.422  77.984  98.056  1.00 45.48  ? 12  ILE A CG2 1 
ATOM   83   C CD1 . ILE A 1 12  ? 95.775  78.036  95.635  1.00 45.40  ? 12  ILE A CD1 1 
ATOM   84   N N   . VAL A 1 13  ? 100.867 79.035  98.082  1.00 44.02  ? 13  VAL A N   1 
ATOM   85   C CA  . VAL A 1 13  ? 101.871 78.761  99.108  1.00 42.36  ? 13  VAL A CA  1 
ATOM   86   C C   . VAL A 1 13  ? 102.408 80.062  99.695  1.00 41.88  ? 13  VAL A C   1 
ATOM   87   O O   . VAL A 1 13  ? 102.625 80.169  100.907 1.00 42.04  ? 13  VAL A O   1 
ATOM   88   C CB  . VAL A 1 13  ? 102.995 77.883  98.522  1.00 41.11  ? 13  VAL A CB  1 
ATOM   89   C CG1 . VAL A 1 13  ? 104.254 77.949  99.372  1.00 40.61  ? 13  VAL A CG1 1 
ATOM   90   C CG2 . VAL A 1 13  ? 102.523 76.445  98.393  1.00 40.96  ? 13  VAL A CG2 1 
ATOM   91   N N   . PHE A 1 14  ? 102.625 81.071  98.849  1.00 41.40  ? 14  PHE A N   1 
ATOM   92   C CA  . PHE A 1 14  ? 103.088 82.369  99.332  1.00 41.24  ? 14  PHE A CA  1 
ATOM   93   C C   . PHE A 1 14  ? 102.063 83.012  100.260 1.00 41.67  ? 14  PHE A C   1 
ATOM   94   O O   . PHE A 1 14  ? 102.424 83.582  101.297 1.00 42.99  ? 14  PHE A O   1 
ATOM   95   C CB  . PHE A 1 14  ? 103.394 83.285  98.148  1.00 41.12  ? 14  PHE A CB  1 
ATOM   96   C CG  . PHE A 1 14  ? 103.724 84.696  98.538  1.00 41.32  ? 14  PHE A CG  1 
ATOM   97   C CD1 . PHE A 1 14  ? 104.765 84.964  99.409  1.00 41.27  ? 14  PHE A CD1 1 
ATOM   98   C CD2 . PHE A 1 14  ? 102.996 85.756  98.027  1.00 41.88  ? 14  PHE A CD2 1 
ATOM   99   C CE1 . PHE A 1 14  ? 105.070 86.264  99.767  1.00 41.29  ? 14  PHE A CE1 1 
ATOM   100  C CE2 . PHE A 1 14  ? 103.296 87.056  98.381  1.00 42.30  ? 14  PHE A CE2 1 
ATOM   101  C CZ  . PHE A 1 14  ? 104.334 87.310  99.252  1.00 41.88  ? 14  PHE A CZ  1 
ATOM   102  N N   . TYR A 1 15  ? 100.778 82.921  99.905  1.00 41.76  ? 15  TYR A N   1 
ATOM   103  C CA  . TYR A 1 15  ? 99.723  83.431  100.777 1.00 42.12  ? 15  TYR A CA  1 
ATOM   104  C C   . TYR A 1 15  ? 99.709  82.695  102.110 1.00 42.68  ? 15  TYR A C   1 
ATOM   105  O O   . TYR A 1 15  ? 99.547  83.313  103.170 1.00 43.22  ? 15  TYR A O   1 
ATOM   106  C CB  . TYR A 1 15  ? 98.361  83.295  100.100 1.00 42.23  ? 15  TYR A CB  1 
ATOM   107  C CG  . TYR A 1 15  ? 98.085  84.281  98.991  1.00 42.52  ? 15  TYR A CG  1 
ATOM   108  C CD1 . TYR A 1 15  ? 98.707  85.519  98.959  1.00 42.37  ? 15  TYR A CD1 1 
ATOM   109  C CD2 . TYR A 1 15  ? 97.177  83.979  97.985  1.00 43.04  ? 15  TYR A CD2 1 
ATOM   110  C CE1 . TYR A 1 15  ? 98.448  86.419  97.943  1.00 42.65  ? 15  TYR A CE1 1 
ATOM   111  C CE2 . TYR A 1 15  ? 96.910  84.873  96.970  1.00 42.99  ? 15  TYR A CE2 1 
ATOM   112  C CZ  . TYR A 1 15  ? 97.548  86.092  96.954  1.00 42.72  ? 15  TYR A CZ  1 
ATOM   113  O OH  . TYR A 1 15  ? 97.287  86.988  95.945  1.00 42.66  ? 15  TYR A OH  1 
ATOM   114  N N   . LEU A 1 16  ? 99.869  81.369  102.073 1.00 42.58  ? 16  LEU A N   1 
ATOM   115  C CA  . LEU A 1 16  ? 99.881  80.586  103.305 1.00 41.98  ? 16  LEU A CA  1 
ATOM   116  C C   . LEU A 1 16  ? 101.078 80.942  104.178 1.00 41.86  ? 16  LEU A C   1 
ATOM   117  O O   . LEU A 1 16  ? 100.954 81.006  105.404 1.00 42.34  ? 16  LEU A O   1 
ATOM   118  C CB  . LEU A 1 16  ? 99.873  79.093  102.982 1.00 41.83  ? 16  LEU A CB  1 
ATOM   119  C CG  . LEU A 1 16  ? 98.553  78.510  102.474 1.00 42.28  ? 16  LEU A CG  1 
ATOM   120  C CD1 . LEU A 1 16  ? 98.523  77.007  102.685 1.00 42.63  ? 16  LEU A CD1 1 
ATOM   121  C CD2 . LEU A 1 16  ? 97.362  79.169  103.154 1.00 42.34  ? 16  LEU A CD2 1 
ATOM   122  N N   . LEU A 1 17  ? 102.242 81.176  103.569 1.00 40.93  ? 17  LEU A N   1 
ATOM   123  C CA  . LEU A 1 17  ? 103.412 81.592  104.340 1.00 39.45  ? 17  LEU A CA  1 
ATOM   124  C C   . LEU A 1 17  ? 103.224 82.977  104.948 1.00 38.30  ? 17  LEU A C   1 
ATOM   125  O O   . LEU A 1 17  ? 103.640 83.213  106.087 1.00 38.15  ? 17  LEU A O   1 
ATOM   126  C CB  . LEU A 1 17  ? 104.674 81.551  103.477 1.00 39.04  ? 17  LEU A CB  1 
ATOM   127  C CG  . LEU A 1 17  ? 105.507 80.263  103.477 1.00 38.82  ? 17  LEU A CG  1 
ATOM   128  C CD1 . LEU A 1 17  ? 106.093 80.044  104.861 1.00 38.63  ? 17  LEU A CD1 1 
ATOM   129  C CD2 . LEU A 1 17  ? 104.721 79.039  103.048 1.00 38.83  ? 17  LEU A CD2 1 
ATOM   130  N N   . ILE A 1 18  ? 102.606 83.904  104.211 1.00 37.76  ? 18  ILE A N   1 
ATOM   131  C CA  . ILE A 1 18  ? 102.327 85.225  104.776 1.00 38.16  ? 18  ILE A CA  1 
ATOM   132  C C   . ILE A 1 18  ? 101.370 85.112  105.958 1.00 37.67  ? 18  ILE A C   1 
ATOM   133  O O   . ILE A 1 18  ? 101.583 85.729  107.011 1.00 37.95  ? 18  ILE A O   1 
ATOM   134  C CB  . ILE A 1 18  ? 101.781 86.174  103.692 1.00 39.12  ? 18  ILE A CB  1 
ATOM   135  C CG1 . ILE A 1 18  ? 102.861 86.472  102.653 1.00 40.19  ? 18  ILE A CG1 1 
ATOM   136  C CG2 . ILE A 1 18  ? 101.282 87.465  104.308 1.00 38.96  ? 18  ILE A CG2 1 
ATOM   137  C CD1 . ILE A 1 18  ? 104.113 87.077  103.237 1.00 40.53  ? 18  ILE A CD1 1 
ATOM   138  N N   . LEU A 1 19  ? 100.317 84.302  105.812 1.00 37.39  ? 19  LEU A N   1 
ATOM   139  C CA  . LEU A 1 19  ? 99.369  84.110  106.906 1.00 37.45  ? 19  LEU A CA  1 
ATOM   140  C C   . LEU A 1 19  ? 100.033 83.438  108.104 1.00 37.32  ? 19  LEU A C   1 
ATOM   141  O O   . LEU A 1 19  ? 99.749  83.787  109.256 1.00 37.60  ? 19  LEU A O   1 
ATOM   142  C CB  . LEU A 1 19  ? 98.172  83.293  106.423 1.00 37.33  ? 19  LEU A CB  1 
ATOM   143  C CG  . LEU A 1 19  ? 97.162  82.842  107.478 1.00 36.96  ? 19  LEU A CG  1 
ATOM   144  C CD1 . LEU A 1 19  ? 96.552  84.040  108.175 1.00 36.91  ? 19  LEU A CD1 1 
ATOM   145  C CD2 . LEU A 1 19  ? 96.082  81.982  106.849 1.00 36.89  ? 19  LEU A CD2 1 
ATOM   146  N N   . LEU A 1 20  ? 100.926 82.477  107.853 1.00 36.90  ? 20  LEU A N   1 
ATOM   147  C CA  . LEU A 1 20  ? 101.608 81.786  108.942 1.00 36.92  ? 20  LEU A CA  1 
ATOM   148  C C   . LEU A 1 20  ? 102.569 82.714  109.675 1.00 37.01  ? 20  LEU A C   1 
ATOM   149  O O   . LEU A 1 20  ? 102.671 82.659  110.906 1.00 36.95  ? 20  LEU A O   1 
ATOM   150  C CB  . LEU A 1 20  ? 102.345 80.564  108.399 1.00 36.88  ? 20  LEU A CB  1 
ATOM   151  C CG  . LEU A 1 20  ? 103.059 79.675  109.416 1.00 37.25  ? 20  LEU A CG  1 
ATOM   152  C CD1 . LEU A 1 20  ? 102.131 79.327  110.567 1.00 37.50  ? 20  LEU A CD1 1 
ATOM   153  C CD2 . LEU A 1 20  ? 103.580 78.415  108.747 1.00 37.36  ? 20  LEU A CD2 1 
ATOM   154  N N   . VAL A 1 21  ? 103.281 83.573  108.940 1.00 37.11  ? 21  VAL A N   1 
ATOM   155  C CA  . VAL A 1 21  ? 104.158 84.555  109.575 1.00 36.84  ? 21  VAL A CA  1 
ATOM   156  C C   . VAL A 1 21  ? 103.341 85.536  110.405 1.00 36.92  ? 21  VAL A C   1 
ATOM   157  O O   . VAL A 1 21  ? 103.726 85.896  111.526 1.00 37.18  ? 21  VAL A O   1 
ATOM   158  C CB  . VAL A 1 21  ? 105.016 85.272  108.515 1.00 36.49  ? 21  VAL A CB  1 
ATOM   159  C CG1 . VAL A 1 21  ? 105.694 86.497  109.101 1.00 36.26  ? 21  VAL A CG1 1 
ATOM   160  C CG2 . VAL A 1 21  ? 106.061 84.324  107.958 1.00 36.69  ? 21  VAL A CG2 1 
ATOM   161  N N   . GLY A 1 22  ? 102.191 85.965  109.882 1.00 37.51  ? 22  GLY A N   1 
ATOM   162  C CA  . GLY A 1 22  ? 101.326 86.844  110.652 1.00 38.40  ? 22  GLY A CA  1 
ATOM   163  C C   . GLY A 1 22  ? 100.793 86.195  111.916 1.00 39.42  ? 22  GLY A C   1 
ATOM   164  O O   . GLY A 1 22  ? 100.735 86.827  112.974 1.00 40.54  ? 22  GLY A O   1 
ATOM   165  N N   . ILE A 1 23  ? 100.409 84.919  111.828 1.00 39.87  ? 23  ILE A N   1 
ATOM   166  C CA  . ILE A 1 23  ? 99.907  84.201  112.997 1.00 40.19  ? 23  ILE A CA  1 
ATOM   167  C C   . ILE A 1 23  ? 101.016 84.005  114.027 1.00 40.85  ? 23  ILE A C   1 
ATOM   168  O O   . ILE A 1 23  ? 100.789 84.134  115.237 1.00 41.21  ? 23  ILE A O   1 
ATOM   169  C CB  . ILE A 1 23  ? 99.273  82.867  112.559 1.00 39.77  ? 23  ILE A CB  1 
ATOM   170  C CG1 . ILE A 1 23  ? 97.849  83.102  112.056 1.00 39.62  ? 23  ILE A CG1 1 
ATOM   171  C CG2 . ILE A 1 23  ? 99.263  81.850  113.690 1.00 39.69  ? 23  ILE A CG2 1 
ATOM   172  C CD1 . ILE A 1 23  ? 97.189  81.864  111.498 1.00 39.61  ? 23  ILE A CD1 1 
ATOM   173  N N   . TRP A 1 24  ? 102.236 83.707  113.567 1.00 41.29  ? 24  TRP A N   1 
ATOM   174  C CA  . TRP A 1 24  ? 103.366 83.583  114.483 1.00 41.87  ? 24  TRP A CA  1 
ATOM   175  C C   . TRP A 1 24  ? 103.666 84.907  115.176 1.00 42.13  ? 24  TRP A C   1 
ATOM   176  O O   . TRP A 1 24  ? 103.975 84.933  116.372 1.00 41.99  ? 24  TRP A O   1 
ATOM   177  C CB  . TRP A 1 24  ? 104.603 83.087  113.737 1.00 42.12  ? 24  TRP A CB  1 
ATOM   178  C CG  . TRP A 1 24  ? 105.882 83.406  114.450 1.00 42.50  ? 24  TRP A CG  1 
ATOM   179  C CD1 . TRP A 1 24  ? 106.414 82.739  115.514 1.00 42.50  ? 24  TRP A CD1 1 
ATOM   180  C CD2 . TRP A 1 24  ? 106.783 84.483  114.162 1.00 42.79  ? 24  TRP A CD2 1 
ATOM   181  N NE1 . TRP A 1 24  ? 107.592 83.328  115.902 1.00 42.44  ? 24  TRP A NE1 1 
ATOM   182  C CE2 . TRP A 1 24  ? 107.840 84.402  115.088 1.00 42.50  ? 24  TRP A CE2 1 
ATOM   183  C CE3 . TRP A 1 24  ? 106.798 85.506  113.209 1.00 43.29  ? 24  TRP A CE3 1 
ATOM   184  C CZ2 . TRP A 1 24  ? 108.902 85.303  115.089 1.00 42.51  ? 24  TRP A CZ2 1 
ATOM   185  C CZ3 . TRP A 1 24  ? 107.853 86.399  113.212 1.00 43.20  ? 24  TRP A CZ3 1 
ATOM   186  C CH2 . TRP A 1 24  ? 108.890 86.292  114.145 1.00 42.90  ? 24  TRP A CH2 1 
ATOM   187  N N   . ALA A 1 25  ? 103.594 86.017  114.435 1.00 42.68  ? 25  ALA A N   1 
ATOM   188  C CA  . ALA A 1 25  ? 103.809 87.326  115.042 1.00 43.25  ? 25  ALA A CA  1 
ATOM   189  C C   . ALA A 1 25  ? 102.709 87.660  116.041 1.00 43.97  ? 25  ALA A C   1 
ATOM   190  O O   . ALA A 1 25  ? 102.962 88.322  117.054 1.00 43.21  ? 25  ALA A O   1 
ATOM   191  C CB  . ALA A 1 25  ? 103.894 88.400  113.960 1.00 43.53  ? 25  ALA A CB  1 
ATOM   192  N N   . ALA A 1 26  ? 101.479 87.225  115.762 1.00 46.56  ? 26  ALA A N   1 
ATOM   193  C CA  . ALA A 1 26  ? 100.394 87.395  116.722 1.00 49.92  ? 26  ALA A CA  1 
ATOM   194  C C   . ALA A 1 26  ? 100.646 86.594  117.991 1.00 53.10  ? 26  ALA A C   1 
ATOM   195  O O   . ALA A 1 26  ? 100.405 87.081  119.102 1.00 54.01  ? 26  ALA A O   1 
ATOM   196  C CB  . ALA A 1 26  ? 99.069  86.977  116.090 1.00 49.81  ? 26  ALA A CB  1 
ATOM   197  N N   . TRP A 1 27  ? 101.123 85.357  117.844 1.00 56.76  ? 27  TRP A N   1 
ATOM   198  C CA  . TRP A 1 27  ? 101.302 84.484  119.000 1.00 59.18  ? 27  TRP A CA  1 
ATOM   199  C C   . TRP A 1 27  ? 102.490 84.912  119.853 1.00 59.48  ? 27  TRP A C   1 
ATOM   200  O O   . TRP A 1 27  ? 102.422 84.866  121.087 1.00 59.06  ? 27  TRP A O   1 
ATOM   201  C CB  . TRP A 1 27  ? 101.472 83.037  118.540 1.00 60.86  ? 27  TRP A CB  1 
ATOM   202  C CG  . TRP A 1 27  ? 101.994 82.133  119.609 1.00 62.42  ? 27  TRP A CG  1 
ATOM   203  C CD1 . TRP A 1 27  ? 101.372 81.799  120.776 1.00 63.06  ? 27  TRP A CD1 1 
ATOM   204  C CD2 . TRP A 1 27  ? 103.253 81.451  119.616 1.00 64.05  ? 27  TRP A CD2 1 
ATOM   205  N NE1 . TRP A 1 27  ? 102.164 80.948  121.508 1.00 63.81  ? 27  TRP A NE1 1 
ATOM   206  C CE2 . TRP A 1 27  ? 103.325 80.718  120.817 1.00 64.44  ? 27  TRP A CE2 1 
ATOM   207  C CE3 . TRP A 1 27  ? 104.326 81.386  118.722 1.00 64.57  ? 27  TRP A CE3 1 
ATOM   208  C CZ2 . TRP A 1 27  ? 104.426 79.932  121.147 1.00 64.79  ? 27  TRP A CZ2 1 
ATOM   209  C CZ3 . TRP A 1 27  ? 105.419 80.605  119.051 1.00 64.81  ? 27  TRP A CZ3 1 
ATOM   210  C CH2 . TRP A 1 27  ? 105.460 79.889  120.253 1.00 64.89  ? 27  TRP A CH2 1 
ATOM   211  N N   . ARG A 1 28  ? 103.590 85.320  119.216 1.00 60.25  ? 28  ARG A N   1 
ATOM   212  C CA  . ARG A 1 28  ? 104.805 85.639  119.961 1.00 61.29  ? 28  ARG A CA  1 
ATOM   213  C C   . ARG A 1 28  ? 104.643 86.911  120.785 1.00 61.34  ? 28  ARG A C   1 
ATOM   214  O O   . ARG A 1 28  ? 105.066 86.962  121.946 1.00 62.56  ? 28  ARG A O   1 
ATOM   215  C CB  . ARG A 1 28  ? 105.987 85.768  119.001 1.00 62.35  ? 28  ARG A CB  1 
ATOM   216  C CG  . ARG A 1 28  ? 107.269 86.255  119.653 1.00 63.71  ? 28  ARG A CG  1 
ATOM   217  C CD  . ARG A 1 28  ? 108.295 86.677  118.617 1.00 65.39  ? 28  ARG A CD  1 
ATOM   218  N NE  . ARG A 1 28  ? 109.248 87.638  119.160 1.00 67.73  ? 28  ARG A NE  1 
ATOM   219  C CZ  . ARG A 1 28  ? 110.096 88.347  118.428 1.00 69.37  ? 28  ARG A CZ  1 
ATOM   220  N NH1 . ARG A 1 28  ? 110.141 88.226  117.112 1.00 69.66  ? 28  ARG A NH1 1 
ATOM   221  N NH2 . ARG A 1 28  ? 110.920 89.198  119.033 1.00 69.91  ? 28  ARG A NH2 1 
ATOM   222  N N   . THR A 1 29  ? 104.026 87.944  120.211 1.00 60.63  ? 29  THR A N   1 
ATOM   223  C CA  . THR A 1 29  ? 103.896 89.238  120.867 1.00 60.19  ? 29  THR A CA  1 
ATOM   224  C C   . THR A 1 29  ? 102.545 89.418  121.550 1.00 59.76  ? 29  THR A C   1 
ATOM   225  O O   . THR A 1 29  ? 102.139 90.555  121.812 1.00 60.09  ? 29  THR A O   1 
ATOM   226  C CB  . THR A 1 29  ? 104.130 90.365  119.861 1.00 60.02  ? 29  THR A CB  1 
ATOM   227  O OG1 . THR A 1 29  ? 103.099 90.344  118.868 1.00 60.02  ? 29  THR A OG1 1 
ATOM   228  C CG2 . THR A 1 29  ? 105.481 90.197  119.184 1.00 59.46  ? 29  THR A CG2 1 
ATOM   229  N N   . LYS A 1 30  ? 101.842 88.329  121.840 1.00 59.14  ? 30  LYS A N   1 
ATOM   230  C CA  . LYS A 1 30  ? 100.554 88.415  122.518 1.00 59.20  ? 30  LYS A CA  1 
ATOM   231  C C   . LYS A 1 30  ? 100.735 88.762  123.992 1.00 57.87  ? 30  LYS A C   1 
ATOM   232  O O   . LYS A 1 30  ? 101.461 88.080  124.716 1.00 56.64  ? 30  LYS A O   1 
ATOM   233  C CB  . LYS A 1 30  ? 99.781  87.102  122.380 1.00 60.38  ? 30  LYS A CB  1 
ATOM   234  C CG  . LYS A 1 30  ? 98.622  86.964  123.353 1.00 61.28  ? 30  LYS A CG  1 
ATOM   235  C CD  . LYS A 1 30  ? 97.609  85.941  122.868 1.00 61.98  ? 30  LYS A CD  1 
ATOM   236  C CE  . LYS A 1 30  ? 96.432  85.834  123.825 1.00 62.29  ? 30  LYS A CE  1 
ATOM   237  N NZ  . LYS A 1 30  ? 95.350  84.966  123.284 1.00 62.77  ? 30  LYS A NZ  1 
ATOM   238  N N   . GLY A 1 33  ? 102.395 93.822  124.497 1.00 99.35  ? 33  GLY A N   1 
ATOM   239  C CA  . GLY A 1 33  ? 101.492 94.890  124.884 1.00 100.18 ? 33  GLY A CA  1 
ATOM   240  C C   . GLY A 1 33  ? 101.242 94.955  126.378 1.00 101.16 ? 33  GLY A C   1 
ATOM   241  O O   . GLY A 1 33  ? 101.863 94.226  127.152 1.00 98.75  ? 33  GLY A O   1 
ATOM   242  N N   . SER A 1 34  ? 100.333 95.836  126.784 1.00 103.94 ? 34  SER A N   1 
ATOM   243  C CA  . SER A 1 34  ? 99.994  95.971  128.193 1.00 105.24 ? 34  SER A CA  1 
ATOM   244  C C   . SER A 1 34  ? 99.205  94.758  128.675 1.00 107.43 ? 34  SER A C   1 
ATOM   245  O O   . SER A 1 34  ? 98.447  94.140  127.923 1.00 110.44 ? 34  SER A O   1 
ATOM   246  C CB  . SER A 1 34  ? 99.190  97.248  128.430 1.00 104.65 ? 34  SER A CB  1 
ATOM   247  O OG  . SER A 1 34  ? 99.090  97.534  129.814 1.00 103.01 ? 34  SER A OG  1 
ATOM   248  N N   . ALA A 1 35  ? 99.399  94.415  129.951 1.00 106.35 ? 35  ALA A N   1 
ATOM   249  C CA  . ALA A 1 35  ? 98.748  93.233  130.507 1.00 104.23 ? 35  ALA A CA  1 
ATOM   250  C C   . ALA A 1 35  ? 97.250  93.448  130.690 1.00 103.76 ? 35  ALA A C   1 
ATOM   251  O O   . ALA A 1 35  ? 96.450  92.547  130.412 1.00 104.49 ? 35  ALA A O   1 
ATOM   252  C CB  . ALA A 1 35  ? 99.400  92.853  131.836 1.00 102.59 ? 35  ALA A CB  1 
ATOM   253  N N   . GLU A 1 36  ? 96.851  94.630  131.156 1.00 100.97 ? 36  GLU A N   1 
ATOM   254  C CA  . GLU A 1 36  ? 95.455  94.901  131.479 1.00 97.16  ? 36  GLU A CA  1 
ATOM   255  C C   . GLU A 1 36  ? 94.714  95.658  130.388 1.00 93.93  ? 36  GLU A C   1 
ATOM   256  O O   . GLU A 1 36  ? 93.526  95.399  130.170 1.00 92.79  ? 36  GLU A O   1 
ATOM   257  C CB  . GLU A 1 36  ? 95.361  95.693  132.789 1.00 96.68  ? 36  GLU A CB  1 
ATOM   258  C CG  . GLU A 1 36  ? 93.973  95.719  133.407 1.00 96.68  ? 36  GLU A CG  1 
ATOM   259  C CD  . GLU A 1 36  ? 93.958  96.366  134.779 1.00 97.17  ? 36  GLU A CD  1 
ATOM   260  O OE1 . GLU A 1 36  ? 94.967  97.003  135.146 1.00 96.91  ? 36  GLU A OE1 1 
ATOM   261  O OE2 . GLU A 1 36  ? 92.938  96.239  135.488 1.00 98.78  ? 36  GLU A OE2 1 
ATOM   262  N N   . GLU A 1 37  ? 95.380  96.577  129.694 1.00 91.00  ? 37  GLU A N   1 
ATOM   263  C CA  . GLU A 1 37  ? 94.746  97.403  128.667 1.00 88.46  ? 37  GLU A CA  1 
ATOM   264  C C   . GLU A 1 37  ? 95.144  96.852  127.302 1.00 85.48  ? 37  GLU A C   1 
ATOM   265  O O   . GLU A 1 37  ? 96.175  97.218  126.738 1.00 85.12  ? 37  GLU A O   1 
ATOM   266  C CB  . GLU A 1 37  ? 95.148  98.865  128.826 1.00 89.38  ? 37  GLU A CB  1 
ATOM   267  C CG  . GLU A 1 37  ? 94.469  99.809  127.849 1.00 90.63  ? 37  GLU A CG  1 
ATOM   268  C CD  . GLU A 1 37  ? 94.854  101.258 128.075 1.00 91.58  ? 37  GLU A CD  1 
ATOM   269  O OE1 . GLU A 1 37  ? 95.669  101.525 128.984 1.00 91.98  ? 37  GLU A OE1 1 
ATOM   270  O OE2 . GLU A 1 37  ? 94.338  102.131 127.347 1.00 92.18  ? 37  GLU A OE2 1 
ATOM   271  N N   . ARG A 1 38  ? 94.314  95.957  126.770 1.00 82.65  ? 38  ARG A N   1 
ATOM   272  C CA  . ARG A 1 38  ? 94.534  95.384  125.450 1.00 81.34  ? 38  ARG A CA  1 
ATOM   273  C C   . ARG A 1 38  ? 93.760  96.108  124.357 1.00 78.64  ? 38  ARG A C   1 
ATOM   274  O O   . ARG A 1 38  ? 93.811  95.685  123.198 1.00 77.93  ? 38  ARG A O   1 
ATOM   275  C CB  . ARG A 1 38  ? 94.164  93.896  125.448 1.00 81.81  ? 38  ARG A CB  1 
ATOM   276  C CG  . ARG A 1 38  ? 95.066  93.031  126.324 1.00 81.32  ? 38  ARG A CG  1 
ATOM   277  C CD  . ARG A 1 38  ? 96.423  92.695  125.663 1.00 82.62  ? 38  ARG A CD  1 
ATOM   278  N NE  . ARG A 1 38  ? 96.436  92.386  124.231 1.00 85.41  ? 38  ARG A NE  1 
ATOM   279  C CZ  . ARG A 1 38  ? 95.656  91.517  123.593 1.00 87.85  ? 38  ARG A CZ  1 
ATOM   280  N NH1 . ARG A 1 38  ? 94.827  90.713  124.239 1.00 89.02  ? 38  ARG A NH1 1 
ATOM   281  N NH2 . ARG A 1 38  ? 95.741  91.424  122.270 1.00 88.53  ? 38  ARG A NH2 1 
ATOM   282  N N   . SER A 1 39  ? 93.035  97.176  124.698 1.00 75.82  ? 39  SER A N   1 
ATOM   283  C CA  . SER A 1 39  ? 92.369  97.977  123.675 1.00 74.52  ? 39  SER A CA  1 
ATOM   284  C C   . SER A 1 39  ? 93.381  98.668  122.772 1.00 70.10  ? 39  SER A C   1 
ATOM   285  O O   . SER A 1 39  ? 93.176  98.764  121.557 1.00 67.99  ? 39  SER A O   1 
ATOM   286  C CB  . SER A 1 39  ? 91.449  99.006  124.329 1.00 77.19  ? 39  SER A CB  1 
ATOM   287  O OG  . SER A 1 39  ? 90.819  99.817  123.353 1.00 80.25  ? 39  SER A OG  1 
ATOM   288  N N   . GLU A 1 40  ? 94.478  99.161  123.348 1.00 66.03  ? 40  GLU A N   1 
ATOM   289  C CA  . GLU A 1 40  ? 95.537  99.806  122.586 1.00 64.07  ? 40  GLU A CA  1 
ATOM   290  C C   . GLU A 1 40  ? 96.772  98.922  122.451 1.00 61.21  ? 40  GLU A C   1 
ATOM   291  O O   . GLU A 1 40  ? 97.855  99.417  122.133 1.00 60.72  ? 40  GLU A O   1 
ATOM   292  C CB  . GLU A 1 40  ? 95.905  101.153 123.211 1.00 65.06  ? 40  GLU A CB  1 
ATOM   293  C CG  . GLU A 1 40  ? 96.521  101.066 124.593 1.00 67.25  ? 40  GLU A CG  1 
ATOM   294  C CD  . GLU A 1 40  ? 96.800  102.434 125.180 1.00 69.25  ? 40  GLU A CD  1 
ATOM   295  O OE1 . GLU A 1 40  ? 96.488  103.441 124.511 1.00 71.85  ? 40  GLU A OE1 1 
ATOM   296  O OE2 . GLU A 1 40  ? 97.335  102.504 126.306 1.00 70.24  ? 40  GLU A OE2 1 
ATOM   297  N N   . ALA A 1 41  ? 96.635  97.621  122.687 1.00 58.77  ? 41  ALA A N   1 
ATOM   298  C CA  . ALA A 1 41  ? 97.671  96.672  122.309 1.00 57.71  ? 41  ALA A CA  1 
ATOM   299  C C   . ALA A 1 41  ? 97.519  96.224  120.865 1.00 56.81  ? 41  ALA A C   1 
ATOM   300  O O   . ALA A 1 41  ? 98.393  95.524  120.344 1.00 58.70  ? 41  ALA A O   1 
ATOM   301  C CB  . ALA A 1 41  ? 97.649  95.455  123.238 1.00 57.67  ? 41  ALA A CB  1 
ATOM   302  N N   . ILE A 1 42  ? 96.426  96.619  120.220 1.00 54.67  ? 42  ILE A N   1 
ATOM   303  C CA  . ILE A 1 42  ? 96.200  96.371  118.808 1.00 53.42  ? 42  ILE A CA  1 
ATOM   304  C C   . ILE A 1 42  ? 96.368  97.643  117.986 1.00 52.81  ? 42  ILE A C   1 
ATOM   305  O O   . ILE A 1 42  ? 96.918  97.608  116.883 1.00 51.67  ? 42  ILE A O   1 
ATOM   306  C CB  . ILE A 1 42  ? 94.798  95.754  118.601 1.00 52.81  ? 42  ILE A CB  1 
ATOM   307  C CG1 . ILE A 1 42  ? 94.703  94.396  119.297 1.00 52.15  ? 42  ILE A CG1 1 
ATOM   308  C CG2 . ILE A 1 42  ? 94.452  95.623  117.128 1.00 52.47  ? 42  ILE A CG2 1 
ATOM   309  C CD1 . ILE A 1 42  ? 93.299  93.849  119.363 1.00 52.15  ? 42  ILE A CD1 1 
ATOM   310  N N   . ILE A 1 43  ? 95.924  98.779  118.525 1.00 51.94  ? 43  ILE A N   1 
ATOM   311  C CA  . ILE A 1 43  ? 95.886  100.018 117.755 1.00 50.24  ? 43  ILE A CA  1 
ATOM   312  C C   . ILE A 1 43  ? 97.292  100.574 117.550 1.00 49.63  ? 43  ILE A C   1 
ATOM   313  O O   . ILE A 1 43  ? 97.694  100.885 116.422 1.00 48.06  ? 43  ILE A O   1 
ATOM   314  C CB  . ILE A 1 43  ? 94.980  101.043 118.455 1.00 49.33  ? 43  ILE A CB  1 
ATOM   315  C CG1 . ILE A 1 43  ? 93.517  100.785 118.125 1.00 48.57  ? 43  ILE A CG1 1 
ATOM   316  C CG2 . ILE A 1 43  ? 95.325  102.444 118.013 1.00 49.23  ? 43  ILE A CG2 1 
ATOM   317  C CD1 . ILE A 1 43  ? 92.591  101.497 119.060 1.00 48.39  ? 43  ILE A CD1 1 
ATOM   318  N N   . VAL A 1 44  ? 98.058  100.712 118.633 1.00 49.87  ? 44  VAL A N   1 
ATOM   319  C CA  . VAL A 1 44  ? 99.346  101.397 118.599 1.00 49.77  ? 44  VAL A CA  1 
ATOM   320  C C   . VAL A 1 44  ? 100.506 100.439 118.836 1.00 50.43  ? 44  VAL A C   1 
ATOM   321  O O   . VAL A 1 44  ? 101.661 100.792 118.560 1.00 50.42  ? 44  VAL A O   1 
ATOM   322  C CB  . VAL A 1 44  ? 99.373  102.566 119.610 1.00 49.29  ? 44  VAL A CB  1 
ATOM   323  C CG1 . VAL A 1 44  ? 99.252  102.068 121.041 1.00 48.79  ? 44  VAL A CG1 1 
ATOM   324  C CG2 . VAL A 1 44  ? 100.560 103.521 119.405 1.00 49.68  ? 44  VAL A CG2 1 
ATOM   325  N N   . GLY A 1 45  ? 100.233 99.211  119.272 1.00 50.88  ? 45  GLY A N   1 
ATOM   326  C CA  . GLY A 1 45  ? 101.240 98.172  119.275 1.00 51.07  ? 45  GLY A CA  1 
ATOM   327  C C   . GLY A 1 45  ? 102.084 98.068  120.525 1.00 52.20  ? 45  GLY A C   1 
ATOM   328  O O   . GLY A 1 45  ? 102.996 97.235  120.564 1.00 54.84  ? 45  GLY A O   1 
ATOM   329  N N   . GLY A 1 46  ? 101.833 98.889  121.537 1.00 52.29  ? 46  GLY A N   1 
ATOM   330  C CA  . GLY A 1 46  ? 102.620 98.831  122.749 1.00 52.35  ? 46  GLY A CA  1 
ATOM   331  C C   . GLY A 1 46  ? 103.865 99.685  122.747 1.00 52.78  ? 46  GLY A C   1 
ATOM   332  O O   . GLY A 1 46  ? 104.673 99.568  123.676 1.00 51.72  ? 46  GLY A O   1 
ATOM   333  N N   . ARG A 1 47  ? 104.055 100.518 121.720 1.00 53.86  ? 47  ARG A N   1 
ATOM   334  C CA  . ARG A 1 47  ? 105.120 101.517 121.642 1.00 53.98  ? 47  ARG A CA  1 
ATOM   335  C C   . ARG A 1 47  ? 106.511 100.894 121.656 1.00 54.69  ? 47  ARG A C   1 
ATOM   336  O O   . ARG A 1 47  ? 107.466 101.517 122.129 1.00 54.86  ? 47  ARG A O   1 
ATOM   337  C CB  . ARG A 1 47  ? 105.004 102.557 122.769 1.00 53.87  ? 47  ARG A CB  1 
ATOM   338  C CG  . ARG A 1 47  ? 103.955 103.652 122.562 1.00 54.23  ? 47  ARG A CG  1 
ATOM   339  C CD  . ARG A 1 47  ? 102.536 103.142 122.781 1.00 54.70  ? 47  ARG A CD  1 
ATOM   340  N NE  . ARG A 1 47  ? 101.538 104.195 122.645 1.00 55.50  ? 47  ARG A NE  1 
ATOM   341  C CZ  . ARG A 1 47  ? 101.140 104.976 123.639 1.00 55.32  ? 47  ARG A CZ  1 
ATOM   342  N NH1 . ARG A 1 47  ? 101.627 104.841 124.861 1.00 54.85  ? 47  ARG A NH1 1 
ATOM   343  N NH2 . ARG A 1 47  ? 100.226 105.912 123.402 1.00 55.53  ? 47  ARG A NH2 1 
ATOM   344  N N   . ASP A 1 48  ? 106.653 99.669  121.148 1.00 55.40  ? 48  ASP A N   1 
ATOM   345  C CA  . ASP A 1 48  ? 107.928 98.963  121.187 1.00 55.73  ? 48  ASP A CA  1 
ATOM   346  C C   . ASP A 1 48  ? 108.458 98.625  119.798 1.00 53.49  ? 48  ASP A C   1 
ATOM   347  O O   . ASP A 1 48  ? 109.427 97.866  119.684 1.00 54.43  ? 48  ASP A O   1 
ATOM   348  C CB  . ASP A 1 48  ? 107.798 97.687  122.024 1.00 58.40  ? 48  ASP A CB  1 
ATOM   349  C CG  . ASP A 1 48  ? 109.071 97.345  122.778 1.00 61.50  ? 48  ASP A CG  1 
ATOM   350  O OD1 . ASP A 1 48  ? 110.159 97.808  122.374 1.00 64.74  ? 48  ASP A OD1 1 
ATOM   351  O OD2 . ASP A 1 48  ? 108.983 96.610  123.784 1.00 63.78  ? 48  ASP A OD2 1 
ATOM   352  N N   . ILE A 1 49  ? 107.846 99.152  118.738 1.00 51.23  ? 49  ILE A N   1 
ATOM   353  C CA  . ILE A 1 49  ? 108.363 98.937  117.391 1.00 50.25  ? 49  ILE A CA  1 
ATOM   354  C C   . ILE A 1 49  ? 109.667 99.707  117.227 1.00 48.94  ? 49  ILE A C   1 
ATOM   355  O O   . ILE A 1 49  ? 109.747 100.900 117.546 1.00 48.45  ? 49  ILE A O   1 
ATOM   356  C CB  . ILE A 1 49  ? 107.324 99.356  116.340 1.00 50.34  ? 49  ILE A CB  1 
ATOM   357  C CG1 . ILE A 1 49  ? 106.094 98.448  116.414 1.00 50.43  ? 49  ILE A CG1 1 
ATOM   358  C CG2 . ILE A 1 49  ? 107.928 99.350  114.943 1.00 50.26  ? 49  ILE A CG2 1 
ATOM   359  C CD1 . ILE A 1 49  ? 106.249 97.133  115.678 1.00 50.46  ? 49  ILE A CD1 1 
ATOM   360  N N   . GLY A 1 50  ? 110.697 99.027  116.730 1.00 47.61  ? 50  GLY A N   1 
ATOM   361  C CA  . GLY A 1 50  ? 112.019 99.609  116.606 1.00 46.62  ? 50  GLY A CA  1 
ATOM   362  C C   . GLY A 1 50  ? 112.151 100.553 115.431 1.00 45.66  ? 50  GLY A C   1 
ATOM   363  O O   . GLY A 1 50  ? 111.178 101.166 114.977 1.00 45.31  ? 50  GLY A O   1 
ATOM   364  N N   . LEU A 1 51  ? 113.378 100.676 114.930 1.00 44.70  ? 51  LEU A N   1 
ATOM   365  C CA  . LEU A 1 51  ? 113.666 101.591 113.833 1.00 44.19  ? 51  LEU A CA  1 
ATOM   366  C C   . LEU A 1 51  ? 113.585 100.908 112.473 1.00 43.87  ? 51  LEU A C   1 
ATOM   367  O O   . LEU A 1 51  ? 112.817 101.337 111.606 1.00 43.89  ? 51  LEU A O   1 
ATOM   368  C CB  . LEU A 1 51  ? 115.050 102.216 114.022 1.00 44.11  ? 51  LEU A CB  1 
ATOM   369  C CG  . LEU A 1 51  ? 115.500 103.139 112.893 1.00 44.10  ? 51  LEU A CG  1 
ATOM   370  C CD1 . LEU A 1 51  ? 114.561 104.324 112.805 1.00 44.01  ? 51  LEU A CD1 1 
ATOM   371  C CD2 . LEU A 1 51  ? 116.933 103.596 113.105 1.00 44.09  ? 51  LEU A CD2 1 
ATOM   372  N N   . LEU A 1 52  ? 114.370 99.846  112.273 1.00 43.57  ? 52  LEU A N   1 
ATOM   373  C CA  . LEU A 1 52  ? 114.405 99.186  110.972 1.00 43.14  ? 52  LEU A CA  1 
ATOM   374  C C   . LEU A 1 52  ? 113.082 98.500  110.661 1.00 42.91  ? 52  LEU A C   1 
ATOM   375  O O   . LEU A 1 52  ? 112.604 98.557  109.521 1.00 42.72  ? 52  LEU A O   1 
ATOM   376  C CB  . LEU A 1 52  ? 115.554 98.179  110.920 1.00 42.91  ? 52  LEU A CB  1 
ATOM   377  C CG  . LEU A 1 52  ? 116.955 98.761  110.725 1.00 42.93  ? 52  LEU A CG  1 
ATOM   378  C CD1 . LEU A 1 52  ? 118.012 97.800  111.240 1.00 43.03  ? 52  LEU A CD1 1 
ATOM   379  C CD2 . LEU A 1 52  ? 117.198 99.095  109.263 1.00 42.77  ? 52  LEU A CD2 1 
ATOM   380  N N   . VAL A 1 53  ? 112.472 97.860  111.661 1.00 42.63  ? 53  VAL A N   1 
ATOM   381  C CA  . VAL A 1 53  ? 111.200 97.176  111.445 1.00 42.08  ? 53  VAL A CA  1 
ATOM   382  C C   . VAL A 1 53  ? 110.116 98.172  111.058 1.00 41.71  ? 53  VAL A C   1 
ATOM   383  O O   . VAL A 1 53  ? 109.362 97.949  110.104 1.00 41.15  ? 53  VAL A O   1 
ATOM   384  C CB  . VAL A 1 53  ? 110.807 96.372  112.697 1.00 42.25  ? 53  VAL A CB  1 
ATOM   385  C CG1 . VAL A 1 53  ? 109.478 95.672  112.480 1.00 42.24  ? 53  VAL A CG1 1 
ATOM   386  C CG2 . VAL A 1 53  ? 111.896 95.372  113.045 1.00 42.35  ? 53  VAL A CG2 1 
ATOM   387  N N   . GLY A 1 54  ? 110.041 99.299  111.768 1.00 41.50  ? 54  GLY A N   1 
ATOM   388  C CA  . GLY A 1 54  ? 109.041 100.304 111.443 1.00 41.39  ? 54  GLY A CA  1 
ATOM   389  C C   . GLY A 1 54  ? 109.284 100.973 110.103 1.00 41.39  ? 54  GLY A C   1 
ATOM   390  O O   . GLY A 1 54  ? 108.336 101.258 109.360 1.00 41.43  ? 54  GLY A O   1 
ATOM   391  N N   . GLY A 1 55  ? 110.553 101.233 109.773 1.00 41.52  ? 55  GLY A N   1 
ATOM   392  C CA  . GLY A 1 55  ? 110.862 101.815 108.477 1.00 41.41  ? 55  GLY A CA  1 
ATOM   393  C C   . GLY A 1 55  ? 110.482 100.899 107.331 1.00 41.20  ? 55  GLY A C   1 
ATOM   394  O O   . GLY A 1 55  ? 109.827 101.322 106.373 1.00 41.91  ? 55  GLY A O   1 
ATOM   395  N N   . PHE A 1 56  ? 110.851 99.617  107.438 1.00 40.95  ? 56  PHE A N   1 
ATOM   396  C CA  . PHE A 1 56  ? 110.452 98.632  106.438 1.00 41.03  ? 56  PHE A CA  1 
ATOM   397  C C   . PHE A 1 56  ? 108.936 98.528  106.350 1.00 40.95  ? 56  PHE A C   1 
ATOM   398  O O   . PHE A 1 56  ? 108.372 98.471  105.249 1.00 42.30  ? 56  PHE A O   1 
ATOM   399  C CB  . PHE A 1 56  ? 111.049 97.267  106.779 1.00 41.21  ? 56  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 56  ? 112.437 97.044  106.243 1.00 41.61  ? 56  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 56  ? 113.487 97.862  106.620 1.00 41.94  ? 56  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 56  ? 112.696 95.984  105.391 1.00 41.83  ? 56  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 56  ? 114.761 97.644  106.138 1.00 42.66  ? 56  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 56  ? 113.965 95.761  104.906 1.00 42.36  ? 56  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 56  ? 115.000 96.591  105.280 1.00 43.05  ? 56  PHE A CZ  1 
ATOM   406  N N   . THR A 1 57  ? 108.261 98.539  107.501 1.00 40.47  ? 57  THR A N   1 
ATOM   407  C CA  . THR A 1 57  ? 106.813 98.386  107.529 1.00 40.69  ? 57  THR A CA  1 
ATOM   408  C C   . THR A 1 57  ? 106.115 99.521  106.798 1.00 40.30  ? 57  THR A C   1 
ATOM   409  O O   . THR A 1 57  ? 105.292 99.288  105.908 1.00 40.68  ? 57  THR A O   1 
ATOM   410  C CB  . THR A 1 57  ? 106.328 98.312  108.975 1.00 41.46  ? 57  THR A CB  1 
ATOM   411  O OG1 . THR A 1 57  ? 106.945 97.201  109.638 1.00 41.61  ? 57  THR A OG1 1 
ATOM   412  C CG2 . THR A 1 57  ? 104.820 98.176  109.030 1.00 41.57  ? 57  THR A CG2 1 
ATOM   413  N N   . MET A 1 58  ? 106.444 100.762 107.143 1.00 39.61  ? 58  MET A N   1 
ATOM   414  C CA  . MET A 1 58  ? 105.694 101.870 106.563 1.00 39.37  ? 58  MET A CA  1 
ATOM   415  C C   . MET A 1 58  ? 106.142 102.147 105.125 1.00 39.34  ? 58  MET A C   1 
ATOM   416  O O   . MET A 1 58  ? 105.341 102.618 104.298 1.00 39.47  ? 58  MET A O   1 
ATOM   417  C CB  . MET A 1 58  ? 105.771 103.075 107.508 1.00 38.68  ? 58  MET A CB  1 
ATOM   418  C CG  . MET A 1 58  ? 104.979 104.297 107.095 1.00 38.03  ? 58  MET A CG  1 
ATOM   419  S SD  . MET A 1 58  ? 105.756 105.393 105.924 1.00 37.98  ? 58  MET A SD  1 
ATOM   420  C CE  . MET A 1 58  ? 106.963 106.100 107.033 1.00 38.43  ? 58  MET A CE  1 
ATOM   421  N N   . THR A 1 59  ? 107.396 101.802 104.785 1.00 39.89  ? 59  THR A N   1 
ATOM   422  C CA  . THR A 1 59  ? 107.807 101.793 103.384 1.00 40.73  ? 59  THR A CA  1 
ATOM   423  C C   . THR A 1 59  ? 106.959 100.826 102.570 1.00 40.13  ? 59  THR A C   1 
ATOM   424  O O   . THR A 1 59  ? 106.505 101.162 101.471 1.00 40.63  ? 59  THR A O   1 
ATOM   425  C CB  . THR A 1 59  ? 109.280 101.402 103.260 1.00 42.19  ? 59  THR A CB  1 
ATOM   426  O OG1 . THR A 1 59  ? 110.086 102.298 104.029 1.00 44.40  ? 59  THR A OG1 1 
ATOM   427  C CG2 . THR A 1 59  ? 109.729 101.458 101.806 1.00 42.19  ? 59  THR A CG2 1 
ATOM   428  N N   . ALA A 1 60  ? 106.723 99.621  103.094 1.00 39.45  ? 60  ALA A N   1 
ATOM   429  C CA  . ALA A 1 60  ? 105.851 98.690  102.387 1.00 39.09  ? 60  ALA A CA  1 
ATOM   430  C C   . ALA A 1 60  ? 104.396 99.126  102.433 1.00 39.11  ? 60  ALA A C   1 
ATOM   431  O O   . ALA A 1 60  ? 103.605 98.700  101.585 1.00 39.06  ? 60  ALA A O   1 
ATOM   432  C CB  . ALA A 1 60  ? 105.993 97.284  102.966 1.00 38.93  ? 60  ALA A CB  1 
ATOM   433  N N   . THR A 1 61  ? 104.030 99.955  103.412 1.00 39.60  ? 61  THR A N   1 
ATOM   434  C CA  . THR A 1 61  ? 102.679 100.501 103.462 1.00 39.69  ? 61  THR A CA  1 
ATOM   435  C C   . THR A 1 61  ? 102.421 101.438 102.289 1.00 39.99  ? 61  THR A C   1 
ATOM   436  O O   . THR A 1 61  ? 101.397 101.315 101.606 1.00 39.98  ? 61  THR A O   1 
ATOM   437  C CB  . THR A 1 61  ? 102.445 101.223 104.791 1.00 39.71  ? 61  THR A CB  1 
ATOM   438  O OG1 . THR A 1 61  ? 102.257 100.260 105.835 1.00 39.33  ? 61  THR A OG1 1 
ATOM   439  C CG2 . THR A 1 61  ? 101.227 102.125 104.709 1.00 39.85  ? 61  THR A CG2 1 
ATOM   440  N N   . TRP A 1 62  ? 103.337 102.376 102.025 1.00 40.64  ? 62  TRP A N   1 
ATOM   441  C CA  . TRP A 1 62  ? 103.074 103.289 100.909 1.00 41.10  ? 62  TRP A CA  1 
ATOM   442  C C   . TRP A 1 62  ? 103.217 102.616 99.548  1.00 40.62  ? 62  TRP A C   1 
ATOM   443  O O   . TRP A 1 62  ? 102.478 102.957 98.619  1.00 41.03  ? 62  TRP A O   1 
ATOM   444  C CB  . TRP A 1 62  ? 103.965 104.529 100.967 1.00 42.52  ? 62  TRP A CB  1 
ATOM   445  C CG  . TRP A 1 62  ? 103.607 105.525 102.035 1.00 44.00  ? 62  TRP A CG  1 
ATOM   446  C CD1 . TRP A 1 62  ? 104.473 106.137 102.883 1.00 45.24  ? 62  TRP A CD1 1 
ATOM   447  C CD2 . TRP A 1 62  ? 102.303 106.059 102.345 1.00 44.93  ? 62  TRP A CD2 1 
ATOM   448  N NE1 . TRP A 1 62  ? 103.801 106.991 103.717 1.00 46.19  ? 62  TRP A NE1 1 
ATOM   449  C CE2 . TRP A 1 62  ? 102.470 106.969 103.402 1.00 45.72  ? 62  TRP A CE2 1 
ATOM   450  C CE3 . TRP A 1 62  ? 101.016 105.851 101.837 1.00 45.48  ? 62  TRP A CE3 1 
ATOM   451  C CZ2 . TRP A 1 62  ? 101.405 107.666 103.963 1.00 45.94  ? 62  TRP A CZ2 1 
ATOM   452  C CZ3 . TRP A 1 62  ? 99.960  106.542 102.401 1.00 46.06  ? 62  TRP A CZ3 1 
ATOM   453  C CH2 . TRP A 1 62  ? 100.161 107.440 103.450 1.00 46.09  ? 62  TRP A CH2 1 
ATOM   454  N N   . VAL A 1 63  ? 104.137 101.666 99.401  1.00 40.01  ? 63  VAL A N   1 
ATOM   455  C CA  . VAL A 1 63  ? 104.350 101.036 98.102  1.00 39.91  ? 63  VAL A CA  1 
ATOM   456  C C   . VAL A 1 63  ? 103.297 99.961  97.866  1.00 40.06  ? 63  VAL A C   1 
ATOM   457  O O   . VAL A 1 63  ? 103.457 98.813  98.294  1.00 39.59  ? 63  VAL A O   1 
ATOM   458  C CB  . VAL A 1 63  ? 105.770 100.452 97.988  1.00 39.26  ? 63  VAL A CB  1 
ATOM   459  C CG1 . VAL A 1 63  ? 105.999 99.899  96.598  1.00 39.34  ? 63  VAL A CG1 1 
ATOM   460  C CG2 . VAL A 1 63  ? 106.798 101.519 98.286  1.00 38.78  ? 63  VAL A CG2 1 
ATOM   461  N N   . GLY A 1 64  ? 102.209 100.328 97.190  1.00 40.41  ? 64  GLY A N   1 
ATOM   462  C CA  . GLY A 1 64  ? 101.180 99.394  96.799  1.00 41.03  ? 64  GLY A CA  1 
ATOM   463  C C   . GLY A 1 64  ? 101.123 99.192  95.292  1.00 41.72  ? 64  GLY A C   1 
ATOM   464  O O   . GLY A 1 64  ? 101.794 99.862  94.512  1.00 42.24  ? 64  GLY A O   1 
ATOM   465  N N   . GLY A 1 65  ? 100.285 98.230  94.896  1.00 42.42  ? 65  GLY A N   1 
ATOM   466  C CA  . GLY A 1 65  ? 100.127 97.933  93.483  1.00 42.88  ? 65  GLY A CA  1 
ATOM   467  C C   . GLY A 1 65  ? 99.507  99.070  92.699  1.00 43.68  ? 65  GLY A C   1 
ATOM   468  O O   . GLY A 1 65  ? 99.845  99.278  91.531  1.00 43.80  ? 65  GLY A O   1 
ATOM   469  N N   . GLY A 1 66  ? 98.592  99.815  93.322  1.00 44.41  ? 66  GLY A N   1 
ATOM   470  C CA  . GLY A 1 66  ? 98.055  100.999 92.674  1.00 45.12  ? 66  GLY A CA  1 
ATOM   471  C C   . GLY A 1 66  ? 99.119  102.049 92.418  1.00 46.04  ? 66  GLY A C   1 
ATOM   472  O O   . GLY A 1 66  ? 99.141  102.675 91.359  1.00 46.49  ? 66  GLY A O   1 
ATOM   473  N N   . TYR A 1 67  ? 100.030 102.232 93.375  1.00 46.72  ? 67  TYR A N   1 
ATOM   474  C CA  . TYR A 1 67  ? 101.111 103.205 93.229  1.00 46.57  ? 67  TYR A CA  1 
ATOM   475  C C   . TYR A 1 67  ? 102.068 102.807 92.110  1.00 46.36  ? 67  TYR A C   1 
ATOM   476  O O   . TYR A 1 67  ? 102.429 103.635 91.261  1.00 46.32  ? 67  TYR A O   1 
ATOM   477  C CB  . TYR A 1 67  ? 101.831 103.338 94.575  1.00 46.63  ? 67  TYR A CB  1 
ATOM   478  C CG  . TYR A 1 67  ? 103.210 103.968 94.587  1.00 46.33  ? 67  TYR A CG  1 
ATOM   479  C CD1 . TYR A 1 67  ? 104.357 103.206 94.398  1.00 45.65  ? 67  TYR A CD1 1 
ATOM   480  C CD2 . TYR A 1 67  ? 103.363 105.319 94.844  1.00 47.05  ? 67  TYR A CD2 1 
ATOM   481  C CE1 . TYR A 1 67  ? 105.609 103.781 94.435  1.00 46.13  ? 67  TYR A CE1 1 
ATOM   482  C CE2 . TYR A 1 67  ? 104.609 105.901 94.886  1.00 47.21  ? 67  TYR A CE2 1 
ATOM   483  C CZ  . TYR A 1 67  ? 105.726 105.130 94.680  1.00 47.02  ? 67  TYR A CZ  1 
ATOM   484  O OH  . TYR A 1 67  ? 106.962 105.723 94.723  1.00 48.65  ? 67  TYR A OH  1 
ATOM   485  N N   . ILE A 1 68  ? 102.479 101.535 92.088  1.00 45.86  ? 68  ILE A N   1 
ATOM   486  C CA  . ILE A 1 68  ? 103.392 101.049 91.055  1.00 45.36  ? 68  ILE A CA  1 
ATOM   487  C C   . ILE A 1 68  ? 102.735 101.129 89.682  1.00 44.80  ? 68  ILE A C   1 
ATOM   488  O O   . ILE A 1 68  ? 103.349 101.574 88.703  1.00 44.44  ? 68  ILE A O   1 
ATOM   489  C CB  . ILE A 1 68  ? 103.851 99.615  91.375  1.00 45.68  ? 68  ILE A CB  1 
ATOM   490  C CG1 . ILE A 1 68  ? 104.517 99.548  92.748  1.00 46.21  ? 68  ILE A CG1 1 
ATOM   491  C CG2 . ILE A 1 68  ? 104.828 99.132  90.330  1.00 45.66  ? 68  ILE A CG2 1 
ATOM   492  C CD1 . ILE A 1 68  ? 105.809 100.319 92.833  1.00 46.39  ? 68  ILE A CD1 1 
ATOM   493  N N   . ASN A 1 69  ? 101.472 100.702 89.590  1.00 44.54  ? 69  ASN A N   1 
ATOM   494  C CA  . ASN A 1 69  ? 100.775 100.731 88.309  1.00 44.93  ? 69  ASN A CA  1 
ATOM   495  C C   . ASN A 1 69  ? 100.531 102.159 87.838  1.00 45.11  ? 69  ASN A C   1 
ATOM   496  O O   . ASN A 1 69  ? 100.606 102.436 86.639  1.00 45.83  ? 69  ASN A O   1 
ATOM   497  C CB  . ASN A 1 69  ? 99.460  99.961  88.402  1.00 44.66  ? 69  ASN A CB  1 
ATOM   498  C CG  . ASN A 1 69  ? 99.669  98.463  88.464  1.00 43.89  ? 69  ASN A CG  1 
ATOM   499  O OD1 . ASN A 1 69  ? 100.701 97.954  88.030  1.00 43.19  ? 69  ASN A OD1 1 
ATOM   500  N ND2 . ASN A 1 69  ? 98.688  97.748  88.998  1.00 43.45  ? 69  ASN A ND2 1 
ATOM   501  N N   . GLY A 1 70  ? 100.253 103.082 88.761  1.00 44.70  ? 70  GLY A N   1 
ATOM   502  C CA  . GLY A 1 70  ? 100.085 104.473 88.375  1.00 44.43  ? 70  GLY A CA  1 
ATOM   503  C C   . GLY A 1 70  ? 101.371 105.102 87.878  1.00 44.10  ? 70  GLY A C   1 
ATOM   504  O O   . GLY A 1 70  ? 101.364 105.851 86.897  1.00 43.58  ? 70  GLY A O   1 
ATOM   505  N N   . THR A 1 71  ? 102.493 104.807 88.544  1.00 43.62  ? 71  THR A N   1 
ATOM   506  C CA  . THR A 1 71  ? 103.780 105.313 88.074  1.00 42.99  ? 71  THR A CA  1 
ATOM   507  C C   . THR A 1 71  ? 104.131 104.739 86.704  1.00 43.05  ? 71  THR A C   1 
ATOM   508  O O   . THR A 1 71  ? 104.580 105.471 85.809  1.00 42.76  ? 71  THR A O   1 
ATOM   509  C CB  . THR A 1 71  ? 104.870 104.993 89.099  1.00 42.22  ? 71  THR A CB  1 
ATOM   510  O OG1 . THR A 1 71  ? 104.685 105.811 90.259  1.00 41.03  ? 71  THR A OG1 1 
ATOM   511  C CG2 . THR A 1 71  ? 106.250 105.261 88.528  1.00 42.84  ? 71  THR A CG2 1 
ATOM   512  N N   . ALA A 1 72  ? 103.903 103.436 86.511  1.00 43.15  ? 72  ALA A N   1 
ATOM   513  C CA  . ALA A 1 72  ? 104.186 102.812 85.221  1.00 43.16  ? 72  ALA A CA  1 
ATOM   514  C C   . ALA A 1 72  ? 103.270 103.348 84.125  1.00 44.01  ? 72  ALA A C   1 
ATOM   515  O O   . ALA A 1 72  ? 103.702 103.516 82.980  1.00 43.99  ? 72  ALA A O   1 
ATOM   516  C CB  . ALA A 1 72  ? 104.061 101.295 85.338  1.00 42.76  ? 72  ALA A CB  1 
ATOM   517  N N   . GLU A 1 73  ? 102.003 103.616 84.453  1.00 45.32  ? 73  GLU A N   1 
ATOM   518  C CA  . GLU A 1 73  ? 101.088 104.234 83.499  1.00 46.47  ? 73  GLU A CA  1 
ATOM   519  C C   . GLU A 1 73  ? 101.547 105.636 83.121  1.00 46.20  ? 73  GLU A C   1 
ATOM   520  O O   . GLU A 1 73  ? 101.538 106.005 81.941  1.00 46.02  ? 73  GLU A O   1 
ATOM   521  C CB  . GLU A 1 73  ? 99.678  104.283 84.086  1.00 47.81  ? 73  GLU A CB  1 
ATOM   522  C CG  . GLU A 1 73  ? 98.687  105.076 83.248  1.00 49.18  ? 73  GLU A CG  1 
ATOM   523  C CD  . GLU A 1 73  ? 97.326  105.192 83.905  1.00 50.16  ? 73  GLU A CD  1 
ATOM   524  O OE1 . GLU A 1 73  ? 97.149  104.643 85.012  1.00 50.03  ? 73  GLU A OE1 1 
ATOM   525  O OE2 . GLU A 1 73  ? 96.434  105.839 83.318  1.00 51.27  ? 73  GLU A OE2 1 
ATOM   526  N N   . ALA A 1 74  ? 101.948 106.433 84.115  1.00 45.59  ? 74  ALA A N   1 
ATOM   527  C CA  . ALA A 1 74  ? 102.366 107.806 83.847  1.00 45.09  ? 74  ALA A CA  1 
ATOM   528  C C   . ALA A 1 74  ? 103.624 107.844 82.991  1.00 44.94  ? 74  ALA A C   1 
ATOM   529  O O   . ALA A 1 74  ? 103.758 108.703 82.112  1.00 46.56  ? 74  ALA A O   1 
ATOM   530  C CB  . ALA A 1 74  ? 102.586 108.553 85.161  1.00 44.69  ? 74  ALA A CB  1 
ATOM   531  N N   . VAL A 1 75  ? 104.558 106.924 83.234  1.00 43.67  ? 75  VAL A N   1 
ATOM   532  C CA  . VAL A 1 75  ? 105.745 106.846 82.387  1.00 42.63  ? 75  VAL A CA  1 
ATOM   533  C C   . VAL A 1 75  ? 105.378 106.346 80.991  1.00 42.67  ? 75  VAL A C   1 
ATOM   534  O O   . VAL A 1 75  ? 105.909 106.829 79.984  1.00 42.60  ? 75  VAL A O   1 
ATOM   535  C CB  . VAL A 1 75  ? 106.814 105.961 83.055  1.00 41.88  ? 75  VAL A CB  1 
ATOM   536  C CG1 . VAL A 1 75  ? 107.989 105.730 82.123  1.00 41.60  ? 75  VAL A CG1 1 
ATOM   537  C CG2 . VAL A 1 75  ? 107.291 106.603 84.342  1.00 41.99  ? 75  VAL A CG2 1 
ATOM   538  N N   . TYR A 1 76  ? 104.443 105.395 80.907  1.00 43.26  ? 76  TYR A N   1 
ATOM   539  C CA  . TYR A 1 76  ? 104.177 104.707 79.646  1.00 44.18  ? 76  TYR A CA  1 
ATOM   540  C C   . TYR A 1 76  ? 103.495 105.612 78.624  1.00 45.59  ? 76  TYR A C   1 
ATOM   541  O O   . TYR A 1 76  ? 103.909 105.661 77.460  1.00 45.57  ? 76  TYR A O   1 
ATOM   542  C CB  . TYR A 1 76  ? 103.325 103.466 79.903  1.00 43.98  ? 76  TYR A CB  1 
ATOM   543  C CG  . TYR A 1 76  ? 102.778 102.837 78.645  1.00 43.64  ? 76  TYR A CG  1 
ATOM   544  C CD1 . TYR A 1 76  ? 103.627 102.330 77.674  1.00 43.63  ? 76  TYR A CD1 1 
ATOM   545  C CD2 . TYR A 1 76  ? 101.412 102.760 78.425  1.00 43.65  ? 76  TYR A CD2 1 
ATOM   546  C CE1 . TYR A 1 76  ? 103.131 101.759 76.522  1.00 43.86  ? 76  TYR A CE1 1 
ATOM   547  C CE2 . TYR A 1 76  ? 100.907 102.192 77.277  1.00 43.81  ? 76  TYR A CE2 1 
ATOM   548  C CZ  . TYR A 1 76  ? 101.770 101.693 76.329  1.00 43.98  ? 76  TYR A CZ  1 
ATOM   549  O OH  . TYR A 1 76  ? 101.270 101.125 75.183  1.00 44.64  ? 76  TYR A OH  1 
ATOM   550  N N   . VAL A 1 77  ? 102.445 106.322 79.031  1.00 47.48  ? 77  VAL A N   1 
ATOM   551  C CA  . VAL A 1 77  ? 101.591 107.057 78.095  1.00 48.48  ? 77  VAL A CA  1 
ATOM   552  C C   . VAL A 1 77  ? 102.376 108.201 77.461  1.00 49.87  ? 77  VAL A C   1 
ATOM   553  O O   . VAL A 1 77  ? 103.270 108.769 78.104  1.00 50.61  ? 77  VAL A O   1 
ATOM   554  C CB  . VAL A 1 77  ? 100.314 107.568 78.783  1.00 48.02  ? 77  VAL A CB  1 
ATOM   555  C CG1 . VAL A 1 77  ? 99.427  106.405 79.184  1.00 47.66  ? 77  VAL A CG1 1 
ATOM   556  C CG2 . VAL A 1 77  ? 100.652 108.414 79.987  1.00 48.16  ? 77  VAL A CG2 1 
ATOM   557  N N   . PRO A 1 78  ? 102.100 108.553 76.202  1.00 50.98  ? 78  PRO A N   1 
ATOM   558  C CA  . PRO A 1 78  ? 102.917 109.586 75.546  1.00 52.04  ? 78  PRO A CA  1 
ATOM   559  C C   . PRO A 1 78  ? 102.638 110.993 76.042  1.00 53.25  ? 78  PRO A C   1 
ATOM   560  O O   . PRO A 1 78  ? 103.562 111.815 76.071  1.00 55.31  ? 78  PRO A O   1 
ATOM   561  C CB  . PRO A 1 78  ? 102.551 109.429 74.065  1.00 51.26  ? 78  PRO A CB  1 
ATOM   562  C CG  . PRO A 1 78  ? 101.176 108.866 74.080  1.00 50.84  ? 78  PRO A CG  1 
ATOM   563  C CD  . PRO A 1 78  ? 101.096 107.979 75.289  1.00 50.63  ? 78  PRO A CD  1 
ATOM   564  N N   . GLY A 1 79  ? 101.396 111.299 76.419  1.00 52.54  ? 79  GLY A N   1 
ATOM   565  C CA  . GLY A 1 79  ? 101.073 112.654 76.838  1.00 51.44  ? 79  GLY A CA  1 
ATOM   566  C C   . GLY A 1 79  ? 101.730 113.052 78.146  1.00 50.21  ? 79  GLY A C   1 
ATOM   567  O O   . GLY A 1 79  ? 102.219 114.176 78.287  1.00 49.47  ? 79  GLY A O   1 
ATOM   568  N N   . TYR A 1 80  ? 101.755 112.140 79.118  1.00 49.23  ? 80  TYR A N   1 
ATOM   569  C CA  . TYR A 1 80  ? 102.255 112.481 80.446  1.00 48.99  ? 80  TYR A CA  1 
ATOM   570  C C   . TYR A 1 80  ? 103.776 112.397 80.511  1.00 48.41  ? 80  TYR A C   1 
ATOM   571  O O   . TYR A 1 80  ? 104.453 113.398 80.766  1.00 48.92  ? 80  TYR A O   1 
ATOM   572  C CB  . TYR A 1 80  ? 101.618 111.569 81.500  1.00 49.44  ? 80  TYR A CB  1 
ATOM   573  C CG  . TYR A 1 80  ? 100.161 111.866 81.787  1.00 49.99  ? 80  TYR A CG  1 
ATOM   574  C CD1 . TYR A 1 80  ? 99.174  111.599 80.848  1.00 49.99  ? 80  TYR A CD1 1 
ATOM   575  C CD2 . TYR A 1 80  ? 99.775  112.415 83.002  1.00 50.58  ? 80  TYR A CD2 1 
ATOM   576  C CE1 . TYR A 1 80  ? 97.847  111.871 81.109  1.00 50.21  ? 80  TYR A CE1 1 
ATOM   577  C CE2 . TYR A 1 80  ? 98.449  112.691 83.271  1.00 50.57  ? 80  TYR A CE2 1 
ATOM   578  C CZ  . TYR A 1 80  ? 97.490  112.417 82.321  1.00 50.51  ? 80  TYR A CZ  1 
ATOM   579  O OH  . TYR A 1 80  ? 96.168  112.689 82.585  1.00 50.74  ? 80  TYR A OH  1 
ATOM   580  N N   . GLY A 1 81  ? 104.330 111.213 80.280  1.00 47.33  ? 81  GLY A N   1 
ATOM   581  C CA  . GLY A 1 81  ? 105.763 111.034 80.359  1.00 46.33  ? 81  GLY A CA  1 
ATOM   582  C C   . GLY A 1 81  ? 106.261 110.960 81.791  1.00 45.60  ? 81  GLY A C   1 
ATOM   583  O O   . GLY A 1 81  ? 105.492 110.921 82.755  1.00 45.66  ? 81  GLY A O   1 
ATOM   584  N N   . LEU A 1 82  ? 107.591 110.945 81.923  1.00 44.54  ? 82  LEU A N   1 
ATOM   585  C CA  . LEU A 1 82  ? 108.204 110.845 83.244  1.00 43.55  ? 82  LEU A CA  1 
ATOM   586  C C   . LEU A 1 82  ? 108.019 112.125 84.049  1.00 43.42  ? 82  LEU A C   1 
ATOM   587  O O   . LEU A 1 82  ? 107.919 112.070 85.280  1.00 43.27  ? 82  LEU A O   1 
ATOM   588  C CB  . LEU A 1 82  ? 109.692 110.509 83.113  1.00 43.08  ? 82  LEU A CB  1 
ATOM   589  C CG  . LEU A 1 82  ? 110.543 110.441 84.385  1.00 42.43  ? 82  LEU A CG  1 
ATOM   590  C CD1 . LEU A 1 82  ? 109.931 109.488 85.397  1.00 41.87  ? 82  LEU A CD1 1 
ATOM   591  C CD2 . LEU A 1 82  ? 111.967 110.030 84.065  1.00 42.51  ? 82  LEU A CD2 1 
ATOM   592  N N   . ALA A 1 83  ? 107.959 113.279 83.376  1.00 44.04  ? 83  ALA A N   1 
ATOM   593  C CA  . ALA A 1 83  ? 107.806 114.548 84.082  1.00 44.93  ? 83  ALA A CA  1 
ATOM   594  C C   . ALA A 1 83  ? 106.486 114.620 84.838  1.00 45.14  ? 83  ALA A C   1 
ATOM   595  O O   . ALA A 1 83  ? 106.392 115.314 85.856  1.00 44.54  ? 83  ALA A O   1 
ATOM   596  C CB  . ALA A 1 83  ? 107.917 115.713 83.099  1.00 44.96  ? 83  ALA A CB  1 
ATOM   597  N N   . TRP A 1 84  ? 105.464 113.916 84.361  1.00 45.36  ? 84  TRP A N   1 
ATOM   598  C CA  . TRP A 1 84  ? 104.190 113.827 85.057  1.00 44.90  ? 84  TRP A CA  1 
ATOM   599  C C   . TRP A 1 84  ? 104.101 112.616 85.977  1.00 45.05  ? 84  TRP A C   1 
ATOM   600  O O   . TRP A 1 84  ? 103.082 112.443 86.651  1.00 45.14  ? 84  TRP A O   1 
ATOM   601  C CB  . TRP A 1 84  ? 103.041 113.797 84.047  1.00 44.18  ? 84  TRP A CB  1 
ATOM   602  C CG  . TRP A 1 84  ? 102.670 115.151 83.534  1.00 43.41  ? 84  TRP A CG  1 
ATOM   603  C CD1 . TRP A 1 84  ? 103.280 115.841 82.530  1.00 42.98  ? 84  TRP A CD1 1 
ATOM   604  C CD2 . TRP A 1 84  ? 101.602 115.981 84.000  1.00 43.40  ? 84  TRP A CD2 1 
ATOM   605  N NE1 . TRP A 1 84  ? 102.659 117.050 82.341  1.00 43.09  ? 84  TRP A NE1 1 
ATOM   606  C CE2 . TRP A 1 84  ? 101.624 117.160 83.232  1.00 43.30  ? 84  TRP A CE2 1 
ATOM   607  C CE3 . TRP A 1 84  ? 100.628 115.841 84.992  1.00 43.89  ? 84  TRP A CE3 1 
ATOM   608  C CZ2 . TRP A 1 84  ? 100.712 118.192 83.424  1.00 43.68  ? 84  TRP A CZ2 1 
ATOM   609  C CZ3 . TRP A 1 84  ? 99.723  116.867 85.182  1.00 44.00  ? 84  TRP A CZ3 1 
ATOM   610  C CH2 . TRP A 1 84  ? 99.771  118.027 84.402  1.00 43.81  ? 84  TRP A CH2 1 
ATOM   611  N N   . ALA A 1 85  ? 105.136 111.773 86.017  1.00 45.54  ? 85  ALA A N   1 
ATOM   612  C CA  . ALA A 1 85  ? 105.202 110.664 86.969  1.00 46.00  ? 85  ALA A CA  1 
ATOM   613  C C   . ALA A 1 85  ? 105.748 111.193 88.295  1.00 45.50  ? 85  ALA A C   1 
ATOM   614  O O   . ALA A 1 85  ? 106.881 110.931 88.703  1.00 45.36  ? 85  ALA A O   1 
ATOM   615  C CB  . ALA A 1 85  ? 106.053 109.529 86.420  1.00 46.36  ? 85  ALA A CB  1 
ATOM   616  N N   . GLN A 1 86  ? 104.899 111.960 88.974  1.00 44.64  ? 86  GLN A N   1 
ATOM   617  C CA  . GLN A 1 86  ? 105.258 112.684 90.183  1.00 44.00  ? 86  GLN A CA  1 
ATOM   618  C C   . GLN A 1 86  ? 104.918 111.921 91.453  1.00 42.54  ? 86  GLN A C   1 
ATOM   619  O O   . GLN A 1 86  ? 105.015 112.485 92.547  1.00 42.39  ? 86  GLN A O   1 
ATOM   620  C CB  . GLN A 1 86  ? 104.564 114.044 90.183  1.00 44.73  ? 86  GLN A CB  1 
ATOM   621  C CG  . GLN A 1 86  ? 103.070 113.932 89.985  1.00 45.43  ? 86  GLN A CG  1 
ATOM   622  C CD  . GLN A 1 86  ? 102.439 115.237 89.569  1.00 46.55  ? 86  GLN A CD  1 
ATOM   623  O OE1 . GLN A 1 86  ? 101.307 115.269 89.090  1.00 48.61  ? 86  GLN A OE1 1 
ATOM   624  N NE2 . GLN A 1 86  ? 103.159 116.329 89.780  1.00 46.82  ? 86  GLN A NE2 1 
ATOM   625  N N   . ALA A 1 87  ? 104.502 110.662 91.333  1.00 40.96  ? 87  ALA A N   1 
ATOM   626  C CA  . ALA A 1 87  ? 104.266 109.844 92.521  1.00 40.05  ? 87  ALA A CA  1 
ATOM   627  C C   . ALA A 1 87  ? 105.528 109.581 93.341  1.00 39.08  ? 87  ALA A C   1 
ATOM   628  O O   . ALA A 1 87  ? 105.476 109.770 94.568  1.00 38.11  ? 87  ALA A O   1 
ATOM   629  C CB  . ALA A 1 87  ? 103.563 108.542 92.119  1.00 40.65  ? 87  ALA A CB  1 
ATOM   630  N N   . PRO A 1 88  ? 106.693 109.152 92.761  1.00 38.55  ? 88  PRO A N   1 
ATOM   631  C CA  . PRO A 1 88  ? 107.855 108.865 93.619  1.00 38.54  ? 88  PRO A CA  1 
ATOM   632  C C   . PRO A 1 88  ? 108.380 110.065 94.395  1.00 38.81  ? 88  PRO A C   1 
ATOM   633  O O   . PRO A 1 88  ? 108.487 110.010 95.627  1.00 39.34  ? 88  PRO A O   1 
ATOM   634  C CB  . PRO A 1 88  ? 108.908 108.364 92.624  1.00 38.29  ? 88  PRO A CB  1 
ATOM   635  C CG  . PRO A 1 88  ? 108.131 107.834 91.501  1.00 38.43  ? 88  PRO A CG  1 
ATOM   636  C CD  . PRO A 1 88  ? 106.979 108.767 91.365  1.00 38.38  ? 88  PRO A CD  1 
ATOM   637  N N   . ILE A 1 89  ? 108.711 111.149 93.690  1.00 38.44  ? 89  ILE A N   1 
ATOM   638  C CA  . ILE A 1 89  ? 109.254 112.320 94.371  1.00 37.85  ? 89  ILE A CA  1 
ATOM   639  C C   . ILE A 1 89  ? 108.188 112.984 95.234  1.00 37.59  ? 89  ILE A C   1 
ATOM   640  O O   . ILE A 1 89  ? 108.507 113.567 96.278  1.00 37.58  ? 89  ILE A O   1 
ATOM   641  C CB  . ILE A 1 89  ? 109.889 113.297 93.359  1.00 37.95  ? 89  ILE A CB  1 
ATOM   642  C CG1 . ILE A 1 89  ? 110.948 114.157 94.050  1.00 38.54  ? 89  ILE A CG1 1 
ATOM   643  C CG2 . ILE A 1 89  ? 108.850 114.176 92.673  1.00 37.54  ? 89  ILE A CG2 1 
ATOM   644  C CD1 . ILE A 1 89  ? 111.860 114.887 93.092  1.00 39.08  ? 89  ILE A CD1 1 
ATOM   645  N N   . GLY A 1 90  ? 106.913 112.873 94.850  1.00 37.74  ? 90  GLY A N   1 
ATOM   646  C CA  . GLY A 1 90  ? 105.851 113.406 95.687  1.00 37.65  ? 90  GLY A CA  1 
ATOM   647  C C   . GLY A 1 90  ? 105.752 112.689 97.018  1.00 37.56  ? 90  GLY A C   1 
ATOM   648  O O   . GLY A 1 90  ? 105.678 113.322 98.073  1.00 37.81  ? 90  GLY A O   1 
ATOM   649  N N   . TYR A 1 91  ? 105.781 111.353 96.987  1.00 37.25  ? 91  TYR A N   1 
ATOM   650  C CA  . TYR A 1 91  ? 105.740 110.576 98.223  1.00 36.56  ? 91  TYR A CA  1 
ATOM   651  C C   . TYR A 1 91  ? 106.986 110.818 99.065  1.00 36.74  ? 91  TYR A C   1 
ATOM   652  O O   . TYR A 1 91  ? 106.902 110.938 100.294 1.00 36.53  ? 91  TYR A O   1 
ATOM   653  C CB  . TYR A 1 91  ? 105.604 109.085 97.910  1.00 35.68  ? 91  TYR A CB  1 
ATOM   654  C CG  . TYR A 1 91  ? 104.210 108.602 97.557  1.00 34.94  ? 91  TYR A CG  1 
ATOM   655  C CD1 . TYR A 1 91  ? 103.376 109.343 96.734  1.00 34.86  ? 91  TYR A CD1 1 
ATOM   656  C CD2 . TYR A 1 91  ? 103.744 107.384 98.025  1.00 34.62  ? 91  TYR A CD2 1 
ATOM   657  C CE1 . TYR A 1 91  ? 102.120 108.894 96.399  1.00 34.71  ? 91  TYR A CE1 1 
ATOM   658  C CE2 . TYR A 1 91  ? 102.484 106.929 97.699  1.00 34.34  ? 91  TYR A CE2 1 
ATOM   659  C CZ  . TYR A 1 91  ? 101.679 107.688 96.883  1.00 34.22  ? 91  TYR A CZ  1 
ATOM   660  O OH  . TYR A 1 91  ? 100.424 107.244 96.548  1.00 33.71  ? 91  TYR A OH  1 
ATOM   661  N N   . SER A 1 92  ? 108.155 110.889 98.418  1.00 36.99  ? 92  SER A N   1 
ATOM   662  C CA  . SER A 1 92  ? 109.399 111.096 99.154  1.00 37.66  ? 92  SER A CA  1 
ATOM   663  C C   . SER A 1 92  ? 109.417 112.452 99.851  1.00 37.37  ? 92  SER A C   1 
ATOM   664  O O   . SER A 1 92  ? 109.795 112.547 101.026 1.00 37.27  ? 92  SER A O   1 
ATOM   665  C CB  . SER A 1 92  ? 110.592 110.961 98.211  1.00 38.35  ? 92  SER A CB  1 
ATOM   666  O OG  . SER A 1 92  ? 111.811 111.173 98.899  1.00 39.66  ? 92  SER A OG  1 
ATOM   667  N N   . LEU A 1 93  ? 109.001 113.512 99.150  1.00 37.21  ? 93  LEU A N   1 
ATOM   668  C CA  . LEU A 1 93  ? 108.942 114.823 99.784  1.00 37.32  ? 93  LEU A CA  1 
ATOM   669  C C   . LEU A 1 93  ? 107.849 114.889 100.840 1.00 37.99  ? 93  LEU A C   1 
ATOM   670  O O   . LEU A 1 93  ? 108.017 115.583 101.848 1.00 39.74  ? 93  LEU A O   1 
ATOM   671  C CB  . LEU A 1 93  ? 108.742 115.916 98.738  1.00 37.21  ? 93  LEU A CB  1 
ATOM   672  C CG  . LEU A 1 93  ? 109.987 116.227 97.912  1.00 37.42  ? 93  LEU A CG  1 
ATOM   673  C CD1 . LEU A 1 93  ? 109.680 117.259 96.846  1.00 37.91  ? 93  LEU A CD1 1 
ATOM   674  C CD2 . LEU A 1 93  ? 111.107 116.706 98.815  1.00 36.97  ? 93  LEU A CD2 1 
ATOM   675  N N   . SER A 1 94  ? 106.740 114.169 100.640 1.00 37.86  ? 94  SER A N   1 
ATOM   676  C CA  . SER A 1 94  ? 105.707 114.092 101.667 1.00 37.38  ? 94  SER A CA  1 
ATOM   677  C C   . SER A 1 94  ? 106.262 113.497 102.951 1.00 36.84  ? 94  SER A C   1 
ATOM   678  O O   . SER A 1 94  ? 106.031 114.022 104.046 1.00 36.35  ? 94  SER A O   1 
ATOM   679  C CB  . SER A 1 94  ? 104.531 113.258 101.163 1.00 37.58  ? 94  SER A CB  1 
ATOM   680  O OG  . SER A 1 94  ? 103.729 112.809 102.242 1.00 37.93  ? 94  SER A OG  1 
ATOM   681  N N   . LEU A 1 95  ? 107.027 112.412 102.830 1.00 36.32  ? 95  LEU A N   1 
ATOM   682  C CA  . LEU A 1 95  ? 107.556 111.753 104.019 1.00 35.68  ? 95  LEU A CA  1 
ATOM   683  C C   . LEU A 1 95  ? 108.657 112.580 104.672 1.00 35.62  ? 95  LEU A C   1 
ATOM   684  O O   . LEU A 1 95  ? 108.746 112.632 105.903 1.00 35.30  ? 95  LEU A O   1 
ATOM   685  C CB  . LEU A 1 95  ? 108.064 110.357 103.670 1.00 35.02  ? 95  LEU A CB  1 
ATOM   686  C CG  . LEU A 1 95  ? 107.085 109.208 103.899 1.00 34.41  ? 95  LEU A CG  1 
ATOM   687  C CD1 . LEU A 1 95  ? 105.830 109.415 103.086 1.00 34.22  ? 95  LEU A CD1 1 
ATOM   688  C CD2 . LEU A 1 95  ? 107.737 107.895 103.533 1.00 34.47  ? 95  LEU A CD2 1 
ATOM   689  N N   . ILE A 1 96  ? 109.498 113.240 103.869 1.00 35.48  ? 96  ILE A N   1 
ATOM   690  C CA  . ILE A 1 96  ? 110.534 114.110 104.428 1.00 35.19  ? 96  ILE A CA  1 
ATOM   691  C C   . ILE A 1 96  ? 109.901 115.270 105.190 1.00 35.29  ? 96  ILE A C   1 
ATOM   692  O O   . ILE A 1 96  ? 110.302 115.591 106.316 1.00 35.59  ? 96  ILE A O   1 
ATOM   693  C CB  . ILE A 1 96  ? 111.476 114.604 103.316 1.00 34.95  ? 96  ILE A CB  1 
ATOM   694  C CG1 . ILE A 1 96  ? 112.436 113.490 102.900 1.00 35.25  ? 96  ILE A CG1 1 
ATOM   695  C CG2 . ILE A 1 96  ? 112.256 115.825 103.761 1.00 34.67  ? 96  ILE A CG2 1 
ATOM   696  C CD1 . ILE A 1 96  ? 113.288 113.831 101.701 1.00 35.53  ? 96  ILE A CD1 1 
ATOM   697  N N   . LEU A 1 97  ? 108.881 115.896 104.594 1.00 35.81  ? 97  LEU A N   1 
ATOM   698  C CA  . LEU A 1 97  ? 108.187 117.007 105.238 1.00 36.20  ? 97  LEU A CA  1 
ATOM   699  C C   . LEU A 1 97  ? 107.495 116.555 106.520 1.00 36.75  ? 97  LEU A C   1 
ATOM   700  O O   . LEU A 1 97  ? 107.557 117.246 107.551 1.00 37.12  ? 97  LEU A O   1 
ATOM   701  C CB  . LEU A 1 97  ? 107.177 117.596 104.253 1.00 36.19  ? 97  LEU A CB  1 
ATOM   702  C CG  . LEU A 1 97  ? 106.381 118.851 104.590 1.00 36.32  ? 97  LEU A CG  1 
ATOM   703  C CD1 . LEU A 1 97  ? 107.313 119.945 105.030 1.00 36.37  ? 97  LEU A CD1 1 
ATOM   704  C CD2 . LEU A 1 97  ? 105.588 119.290 103.383 1.00 36.38  ? 97  LEU A CD2 1 
ATOM   705  N N   . GLY A 1 98  ? 106.845 115.388 106.476 1.00 37.45  ? 98  GLY A N   1 
ATOM   706  C CA  . GLY A 1 98  ? 106.192 114.865 107.663 1.00 38.35  ? 98  GLY A CA  1 
ATOM   707  C C   . GLY A 1 98  ? 107.171 114.572 108.781 1.00 38.61  ? 98  GLY A C   1 
ATOM   708  O O   . GLY A 1 98  ? 106.974 115.010 109.914 1.00 39.27  ? 98  GLY A O   1 
ATOM   709  N N   . GLY A 1 99  ? 108.269 113.885 108.460 1.00 38.24  ? 99  GLY A N   1 
ATOM   710  C CA  . GLY A 1 99  ? 109.270 113.585 109.467 1.00 37.69  ? 99  GLY A CA  1 
ATOM   711  C C   . GLY A 1 99  ? 109.934 114.819 110.041 1.00 36.96  ? 99  GLY A C   1 
ATOM   712  O O   . GLY A 1 99  ? 110.306 114.835 111.218 1.00 36.61  ? 99  GLY A O   1 
ATOM   713  N N   . LEU A 1 100 ? 110.102 115.864 109.228 1.00 36.77  ? 100 LEU A N   1 
ATOM   714  C CA  . LEU A 1 100 ? 110.687 117.095 109.747 1.00 37.08  ? 100 LEU A CA  1 
ATOM   715  C C   . LEU A 1 100 ? 109.739 117.805 110.708 1.00 37.73  ? 100 LEU A C   1 
ATOM   716  O O   . LEU A 1 100 ? 110.140 118.185 111.814 1.00 39.07  ? 100 LEU A O   1 
ATOM   717  C CB  . LEU A 1 100 ? 111.086 118.023 108.600 1.00 37.00  ? 100 LEU A CB  1 
ATOM   718  C CG  . LEU A 1 100 ? 112.371 117.692 107.845 1.00 37.09  ? 100 LEU A CG  1 
ATOM   719  C CD1 . LEU A 1 100 ? 112.348 118.326 106.469 1.00 37.18  ? 100 LEU A CD1 1 
ATOM   720  C CD2 . LEU A 1 100 ? 113.580 118.160 108.631 1.00 37.09  ? 100 LEU A CD2 1 
ATOM   721  N N   . PHE A 1 101 ? 108.476 117.992 110.319 1.00 38.18  ? 101 PHE A N   1 
ATOM   722  C CA  . PHE A 1 101 ? 107.599 118.864 111.097 1.00 38.97  ? 101 PHE A CA  1 
ATOM   723  C C   . PHE A 1 101 ? 106.497 118.148 111.865 1.00 40.16  ? 101 PHE A C   1 
ATOM   724  O O   . PHE A 1 101 ? 106.296 118.439 113.046 1.00 40.29  ? 101 PHE A O   1 
ATOM   725  C CB  . PHE A 1 101 ? 106.979 119.948 110.199 1.00 38.81  ? 101 PHE A CB  1 
ATOM   726  C CG  . PHE A 1 101 ? 107.991 120.797 109.483 1.00 38.62  ? 101 PHE A CG  1 
ATOM   727  C CD1 . PHE A 1 101 ? 108.520 120.407 108.268 1.00 38.49  ? 101 PHE A CD1 1 
ATOM   728  C CD2 . PHE A 1 101 ? 108.418 121.992 110.038 1.00 38.65  ? 101 PHE A CD2 1 
ATOM   729  C CE1 . PHE A 1 101 ? 109.452 121.192 107.618 1.00 38.42  ? 101 PHE A CE1 1 
ATOM   730  C CE2 . PHE A 1 101 ? 109.349 122.780 109.393 1.00 38.75  ? 101 PHE A CE2 1 
ATOM   731  C CZ  . PHE A 1 101 ? 109.866 122.379 108.180 1.00 38.62  ? 101 PHE A CZ  1 
ATOM   732  N N   . PHE A 1 102 ? 105.759 117.234 111.238 1.00 41.61  ? 102 PHE A N   1 
ATOM   733  C CA  . PHE A 1 102 ? 104.559 116.685 111.859 1.00 42.26  ? 102 PHE A CA  1 
ATOM   734  C C   . PHE A 1 102 ? 104.837 115.485 112.753 1.00 42.64  ? 102 PHE A C   1 
ATOM   735  O O   . PHE A 1 102 ? 104.059 115.220 113.676 1.00 42.88  ? 102 PHE A O   1 
ATOM   736  C CB  . PHE A 1 102 ? 103.552 116.280 110.780 1.00 42.13  ? 102 PHE A CB  1 
ATOM   737  C CG  . PHE A 1 102 ? 102.880 117.441 110.112 1.00 42.19  ? 102 PHE A CG  1 
ATOM   738  C CD1 . PHE A 1 102 ? 102.165 118.365 110.853 1.00 42.91  ? 102 PHE A CD1 1 
ATOM   739  C CD2 . PHE A 1 102 ? 102.970 117.614 108.743 1.00 42.11  ? 102 PHE A CD2 1 
ATOM   740  C CE1 . PHE A 1 102 ? 101.548 119.435 110.238 1.00 43.77  ? 102 PHE A CE1 1 
ATOM   741  C CE2 . PHE A 1 102 ? 102.355 118.681 108.122 1.00 42.97  ? 102 PHE A CE2 1 
ATOM   742  C CZ  . PHE A 1 102 ? 101.643 119.593 108.871 1.00 43.78  ? 102 PHE A CZ  1 
ATOM   743  N N   . ALA A 1 103 ? 105.919 114.747 112.495 1.00 42.16  ? 103 ALA A N   1 
ATOM   744  C CA  . ALA A 1 103 ? 106.160 113.502 113.219 1.00 41.71  ? 103 ALA A CA  1 
ATOM   745  C C   . ALA A 1 103 ? 106.572 113.756 114.663 1.00 41.70  ? 103 ALA A C   1 
ATOM   746  O O   . ALA A 1 103 ? 106.203 112.991 115.561 1.00 42.32  ? 103 ALA A O   1 
ATOM   747  C CB  . ALA A 1 103 ? 107.226 112.680 112.498 1.00 41.88  ? 103 ALA A CB  1 
ATOM   748  N N   . LYS A 1 104 ? 107.354 114.808 114.903 1.00 41.90  ? 104 LYS A N   1 
ATOM   749  C CA  . LYS A 1 104 ? 107.868 115.065 116.249 1.00 42.61  ? 104 LYS A CA  1 
ATOM   750  C C   . LYS A 1 104 ? 106.784 115.396 117.275 1.00 43.22  ? 104 LYS A C   1 
ATOM   751  O O   . LYS A 1 104 ? 106.817 114.807 118.369 1.00 43.22  ? 104 LYS A O   1 
ATOM   752  C CB  . LYS A 1 104 ? 108.943 116.157 116.183 1.00 43.11  ? 104 LYS A CB  1 
ATOM   753  C CG  . LYS A 1 104 ? 109.675 116.394 117.491 1.00 43.89  ? 104 LYS A CG  1 
ATOM   754  C CD  . LYS A 1 104 ? 110.611 115.242 117.813 1.00 44.33  ? 104 LYS A CD  1 
ATOM   755  C CE  . LYS A 1 104 ? 111.329 115.470 119.133 1.00 44.50  ? 104 LYS A CE  1 
ATOM   756  N NZ  . LYS A 1 104 ? 112.270 116.620 119.058 1.00 44.95  ? 104 LYS A NZ  1 
ATOM   757  N N   . PRO A 1 105 ? 105.820 116.299 117.026 1.00 44.01  ? 105 PRO A N   1 
ATOM   758  C CA  . PRO A 1 105 ? 104.820 116.562 118.074 1.00 43.95  ? 105 PRO A CA  1 
ATOM   759  C C   . PRO A 1 105 ? 103.807 115.445 118.244 1.00 43.83  ? 105 PRO A C   1 
ATOM   760  O O   . PRO A 1 105 ? 103.226 115.319 119.329 1.00 43.98  ? 105 PRO A O   1 
ATOM   761  C CB  . PRO A 1 105 ? 104.145 117.860 117.604 1.00 44.02  ? 105 PRO A CB  1 
ATOM   762  C CG  . PRO A 1 105 ? 105.069 118.436 116.596 1.00 44.36  ? 105 PRO A CG  1 
ATOM   763  C CD  . PRO A 1 105 ? 105.638 117.244 115.912 1.00 44.31  ? 105 PRO A CD  1 
ATOM   764  N N   . MET A 1 106 ? 103.559 114.643 117.205 1.00 43.65  ? 106 MET A N   1 
ATOM   765  C CA  . MET A 1 106 ? 102.614 113.538 117.336 1.00 43.93  ? 106 MET A CA  1 
ATOM   766  C C   . MET A 1 106 ? 103.128 112.468 118.290 1.00 42.96  ? 106 MET A C   1 
ATOM   767  O O   . MET A 1 106 ? 102.370 111.958 119.119 1.00 42.40  ? 106 MET A O   1 
ATOM   768  C CB  . MET A 1 106 ? 102.316 112.928 115.967 1.00 44.83  ? 106 MET A CB  1 
ATOM   769  C CG  . MET A 1 106 ? 101.325 113.714 115.132 1.00 45.62  ? 106 MET A CG  1 
ATOM   770  S SD  . MET A 1 106 ? 99.643  113.500 115.740 1.00 47.26  ? 106 MET A SD  1 
ATOM   771  C CE  . MET A 1 106 ? 98.851  114.963 115.083 1.00 47.01  ? 106 MET A CE  1 
ATOM   772  N N   . ARG A 1 107 ? 104.409 112.120 118.198 1.00 42.44  ? 107 ARG A N   1 
ATOM   773  C CA  . ARG A 1 107 ? 104.941 111.019 118.991 1.00 41.68  ? 107 ARG A CA  1 
ATOM   774  C C   . ARG A 1 107 ? 105.423 111.461 120.368 1.00 41.51  ? 107 ARG A C   1 
ATOM   775  O O   . ARG A 1 107 ? 105.356 110.671 121.318 1.00 41.19  ? 107 ARG A O   1 
ATOM   776  C CB  . ARG A 1 107 ? 106.078 110.331 118.224 1.00 41.49  ? 107 ARG A CB  1 
ATOM   777  C CG  . ARG A 1 107 ? 106.752 109.183 118.961 1.00 40.79  ? 107 ARG A CG  1 
ATOM   778  C CD  . ARG A 1 107 ? 105.738 108.121 119.361 1.00 40.16  ? 107 ARG A CD  1 
ATOM   779  N NE  . ARG A 1 107 ? 106.337 107.059 120.159 1.00 39.85  ? 107 ARG A NE  1 
ATOM   780  C CZ  . ARG A 1 107 ? 106.299 107.006 121.483 1.00 40.20  ? 107 ARG A CZ  1 
ATOM   781  N NH1 . ARG A 1 107 ? 105.701 107.946 122.195 1.00 40.63  ? 107 ARG A NH1 1 
ATOM   782  N NH2 . ARG A 1 107 ? 106.878 105.986 122.109 1.00 40.27  ? 107 ARG A NH2 1 
ATOM   783  N N   . SER A 1 108 ? 105.876 112.714 120.503 1.00 42.13  ? 108 SER A N   1 
ATOM   784  C CA  . SER A 1 108 ? 106.456 113.177 121.764 1.00 42.92  ? 108 SER A CA  1 
ATOM   785  C C   . SER A 1 108 ? 105.450 113.105 122.905 1.00 43.60  ? 108 SER A C   1 
ATOM   786  O O   . SER A 1 108 ? 105.804 112.748 124.034 1.00 43.90  ? 108 SER A O   1 
ATOM   787  C CB  . SER A 1 108 ? 106.983 114.602 121.606 1.00 43.01  ? 108 SER A CB  1 
ATOM   788  O OG  . SER A 1 108 ? 107.844 114.948 122.676 1.00 43.09  ? 108 SER A OG  1 
ATOM   789  N N   . LYS A 1 109 ? 104.195 113.439 122.631 1.00 44.39  ? 109 LYS A N   1 
ATOM   790  C CA  . LYS A 1 109 ? 103.099 113.230 123.564 1.00 45.33  ? 109 LYS A CA  1 
ATOM   791  C C   . LYS A 1 109 ? 102.213 112.103 123.048 1.00 45.73  ? 109 LYS A C   1 
ATOM   792  O O   . LYS A 1 109 ? 101.919 112.026 121.853 1.00 45.29  ? 109 LYS A O   1 
ATOM   793  C CB  . LYS A 1 109 ? 102.321 114.532 123.784 1.00 45.69  ? 109 LYS A CB  1 
ATOM   794  C CG  . LYS A 1 109 ? 101.642 115.109 122.559 1.00 45.97  ? 109 LYS A CG  1 
ATOM   795  C CD  . LYS A 1 109 ? 100.978 116.429 122.900 1.00 46.05  ? 109 LYS A CD  1 
ATOM   796  C CE  . LYS A 1 109 ? 100.285 117.028 121.694 1.00 46.05  ? 109 LYS A CE  1 
ATOM   797  N NZ  . LYS A 1 109 ? 101.255 117.445 120.645 1.00 46.37  ? 109 LYS A NZ  1 
ATOM   798  N N   . GLY A 1 110 ? 101.809 111.218 123.952 1.00 46.84  ? 110 GLY A N   1 
ATOM   799  C CA  . GLY A 1 110 ? 101.323 109.910 123.557 1.00 47.07  ? 110 GLY A CA  1 
ATOM   800  C C   . GLY A 1 110 ? 99.915  109.832 123.006 1.00 47.20  ? 110 GLY A C   1 
ATOM   801  O O   . GLY A 1 110 ? 99.006  109.353 123.691 1.00 47.73  ? 110 GLY A O   1 
ATOM   802  N N   . TYR A 1 111 ? 99.715  110.294 121.775 1.00 47.27  ? 111 TYR A N   1 
ATOM   803  C CA  . TYR A 1 111 ? 98.460  110.026 121.092 1.00 47.52  ? 111 TYR A CA  1 
ATOM   804  C C   . TYR A 1 111 ? 98.347  108.553 120.717 1.00 47.04  ? 111 TYR A C   1 
ATOM   805  O O   . TYR A 1 111 ? 99.338  107.822 120.630 1.00 48.18  ? 111 TYR A O   1 
ATOM   806  C CB  . TYR A 1 111 ? 98.309  110.889 119.841 1.00 47.89  ? 111 TYR A CB  1 
ATOM   807  C CG  . TYR A 1 111 ? 98.057  112.348 120.117 1.00 47.75  ? 111 TYR A CG  1 
ATOM   808  C CD1 . TYR A 1 111 ? 97.106  112.735 121.049 1.00 48.24  ? 111 TYR A CD1 1 
ATOM   809  C CD2 . TYR A 1 111 ? 98.736  113.337 119.423 1.00 47.29  ? 111 TYR A CD2 1 
ATOM   810  C CE1 . TYR A 1 111 ? 96.852  114.064 121.301 1.00 48.62  ? 111 TYR A CE1 1 
ATOM   811  C CE2 . TYR A 1 111 ? 98.489  114.673 119.668 1.00 48.02  ? 111 TYR A CE2 1 
ATOM   812  C CZ  . TYR A 1 111 ? 97.545  115.030 120.608 1.00 48.75  ? 111 TYR A CZ  1 
ATOM   813  O OH  . TYR A 1 111 ? 97.286  116.356 120.860 1.00 49.62  ? 111 TYR A OH  1 
ATOM   814  N N   . VAL A 1 112 ? 97.109  108.124 120.497 1.00 44.93  ? 112 VAL A N   1 
ATOM   815  C CA  . VAL A 1 112 ? 96.803  106.738 120.179 1.00 43.86  ? 112 VAL A CA  1 
ATOM   816  C C   . VAL A 1 112 ? 96.540  106.548 118.689 1.00 44.16  ? 112 VAL A C   1 
ATOM   817  O O   . VAL A 1 112 ? 97.021  105.585 118.091 1.00 44.59  ? 112 VAL A O   1 
ATOM   818  C CB  . VAL A 1 112 ? 95.605  106.266 121.031 1.00 42.83  ? 112 VAL A CB  1 
ATOM   819  C CG1 . VAL A 1 112 ? 95.191  104.865 120.657 1.00 42.38  ? 112 VAL A CG1 1 
ATOM   820  C CG2 . VAL A 1 112 ? 95.947  106.343 122.509 1.00 42.85  ? 112 VAL A CG2 1 
ATOM   821  N N   . THR A 1 113 ? 95.787  107.459 118.072 1.00 44.22  ? 113 THR A N   1 
ATOM   822  C CA  . THR A 1 113 ? 95.514  107.440 116.639 1.00 44.25  ? 113 THR A CA  1 
ATOM   823  C C   . THR A 1 113 ? 95.751  108.829 116.054 1.00 44.15  ? 113 THR A C   1 
ATOM   824  O O   . THR A 1 113 ? 96.205  109.751 116.737 1.00 43.96  ? 113 THR A O   1 
ATOM   825  C CB  . THR A 1 113 ? 94.078  106.988 116.335 1.00 44.51  ? 113 THR A CB  1 
ATOM   826  O OG1 . THR A 1 113 ? 93.149  107.906 116.924 1.00 45.42  ? 113 THR A OG1 1 
ATOM   827  C CG2 . THR A 1 113 ? 93.811  105.591 116.863 1.00 44.72  ? 113 THR A CG2 1 
ATOM   828  N N   . MET A 1 114 ? 95.443  108.962 114.760 1.00 44.39  ? 114 MET A N   1 
ATOM   829  C CA  . MET A 1 114 ? 95.456  110.267 114.103 1.00 44.56  ? 114 MET A CA  1 
ATOM   830  C C   . MET A 1 114 ? 94.452  111.224 114.721 1.00 44.87  ? 114 MET A C   1 
ATOM   831  O O   . MET A 1 114 ? 94.753  112.405 114.924 1.00 45.61  ? 114 MET A O   1 
ATOM   832  C CB  . MET A 1 114 ? 95.128  110.106 112.622 1.00 44.87  ? 114 MET A CB  1 
ATOM   833  C CG  . MET A 1 114 ? 95.554  111.222 111.715 1.00 45.28  ? 114 MET A CG  1 
ATOM   834  S SD  . MET A 1 114 ? 94.177  112.363 111.506 1.00 47.92  ? 114 MET A SD  1 
ATOM   835  C CE  . MET A 1 114 ? 93.374  111.719 110.046 1.00 47.13  ? 114 MET A CE  1 
ATOM   836  N N   . LEU A 1 115 ? 93.247  110.742 114.998 1.00 45.14  ? 115 LEU A N   1 
ATOM   837  C CA  . LEU A 1 115 ? 92.103  111.610 115.224 1.00 45.02  ? 115 LEU A CA  1 
ATOM   838  C C   . LEU A 1 115 ? 92.001  112.089 116.668 1.00 44.85  ? 115 LEU A C   1 
ATOM   839  O O   . LEU A 1 115 ? 91.195  112.982 116.955 1.00 44.46  ? 115 LEU A O   1 
ATOM   840  C CB  . LEU A 1 115 ? 90.830  110.866 114.789 1.00 44.99  ? 115 LEU A CB  1 
ATOM   841  C CG  . LEU A 1 115 ? 89.423  111.443 114.925 1.00 45.50  ? 115 LEU A CG  1 
ATOM   842  C CD1 . LEU A 1 115 ? 89.303  112.684 114.071 1.00 45.18  ? 115 LEU A CD1 1 
ATOM   843  C CD2 . LEU A 1 115 ? 88.399  110.420 114.511 1.00 46.10  ? 115 LEU A CD2 1 
ATOM   844  N N   . ASP A 1 116 ? 92.829  111.555 117.565 1.00 45.69  ? 116 ASP A N   1 
ATOM   845  C CA  . ASP A 1 116 ? 92.775  111.963 118.968 1.00 47.35  ? 116 ASP A CA  1 
ATOM   846  C C   . ASP A 1 116 ? 93.065  113.449 119.194 1.00 47.58  ? 116 ASP A C   1 
ATOM   847  O O   . ASP A 1 116 ? 92.364  114.055 120.023 1.00 48.94  ? 116 ASP A O   1 
ATOM   848  C CB  . ASP A 1 116 ? 93.713  111.073 119.797 1.00 48.80  ? 116 ASP A CB  1 
ATOM   849  C CG  . ASP A 1 116 ? 93.393  111.104 121.280 1.00 50.07  ? 116 ASP A CG  1 
ATOM   850  O OD1 . ASP A 1 116 ? 92.374  111.713 121.662 1.00 51.62  ? 116 ASP A OD1 1 
ATOM   851  O OD2 . ASP A 1 116 ? 94.163  110.516 122.068 1.00 50.22  ? 116 ASP A OD2 1 
ATOM   852  N N   . PRO A 1 117 ? 94.055  114.089 118.548 1.00 46.99  ? 117 PRO A N   1 
ATOM   853  C CA  . PRO A 1 117 ? 94.156  115.554 118.681 1.00 46.32  ? 117 PRO A CA  1 
ATOM   854  C C   . PRO A 1 117 ? 92.942  116.312 118.168 1.00 46.41  ? 117 PRO A C   1 
ATOM   855  O O   . PRO A 1 117 ? 92.615  117.367 118.723 1.00 45.97  ? 117 PRO A O   1 
ATOM   856  C CB  . PRO A 1 117 ? 95.415  115.900 117.870 1.00 45.99  ? 117 PRO A CB  1 
ATOM   857  C CG  . PRO A 1 117 ? 95.675  114.712 117.027 1.00 46.28  ? 117 PRO A CG  1 
ATOM   858  C CD  . PRO A 1 117 ? 95.248  113.560 117.866 1.00 46.81  ? 117 PRO A CD  1 
ATOM   859  N N   . PHE A 1 118 ? 92.274  115.821 117.119 1.00 46.31  ? 118 PHE A N   1 
ATOM   860  C CA  . PHE A 1 118 ? 91.087  116.512 116.619 1.00 45.92  ? 118 PHE A CA  1 
ATOM   861  C C   . PHE A 1 118 ? 89.955  116.481 117.635 1.00 47.34  ? 118 PHE A C   1 
ATOM   862  O O   . PHE A 1 118 ? 89.243  117.476 117.805 1.00 47.46  ? 118 PHE A O   1 
ATOM   863  C CB  . PHE A 1 118 ? 90.620  115.905 115.298 1.00 44.57  ? 118 PHE A CB  1 
ATOM   864  C CG  . PHE A 1 118 ? 91.562  116.133 114.160 1.00 43.71  ? 118 PHE A CG  1 
ATOM   865  C CD1 . PHE A 1 118 ? 92.221  117.338 114.025 1.00 43.42  ? 118 PHE A CD1 1 
ATOM   866  C CD2 . PHE A 1 118 ? 91.767  115.153 113.208 1.00 43.17  ? 118 PHE A CD2 1 
ATOM   867  C CE1 . PHE A 1 118 ? 93.085  117.551 112.976 1.00 43.30  ? 118 PHE A CE1 1 
ATOM   868  C CE2 . PHE A 1 118 ? 92.625  115.365 112.155 1.00 42.88  ? 118 PHE A CE2 1 
ATOM   869  C CZ  . PHE A 1 118 ? 93.285  116.563 112.039 1.00 42.78  ? 118 PHE A CZ  1 
ATOM   870  N N   . GLN A 1 119 ? 89.767  115.346 118.309 1.00 49.55  ? 119 GLN A N   1 
ATOM   871  C CA  . GLN A 1 119 ? 88.680  115.236 119.275 1.00 51.20  ? 119 GLN A CA  1 
ATOM   872  C C   . GLN A 1 119 ? 88.911  116.146 120.473 1.00 52.57  ? 119 GLN A C   1 
ATOM   873  O O   . GLN A 1 119 ? 88.035  116.941 120.828 1.00 54.92  ? 119 GLN A O   1 
ATOM   874  C CB  . GLN A 1 119 ? 88.514  113.786 119.721 1.00 51.43  ? 119 GLN A CB  1 
ATOM   875  C CG  . GLN A 1 119 ? 87.730  112.941 118.741 1.00 51.90  ? 119 GLN A CG  1 
ATOM   876  C CD  . GLN A 1 119 ? 87.342  111.602 119.318 1.00 52.78  ? 119 GLN A CD  1 
ATOM   877  O OE1 . GLN A 1 119 ? 87.940  111.135 120.286 1.00 54.34  ? 119 GLN A OE1 1 
ATOM   878  N NE2 . GLN A 1 119 ? 86.325  110.981 118.735 1.00 52.66  ? 119 GLN A NE2 1 
ATOM   879  N N   . GLN A 1 120 ? 90.110  116.093 121.060 1.00 53.22  ? 120 GLN A N   1 
ATOM   880  C CA  . GLN A 1 120 ? 90.394  116.816 122.298 1.00 54.54  ? 120 GLN A CA  1 
ATOM   881  C C   . GLN A 1 120 ? 90.292  118.329 122.143 1.00 55.38  ? 120 GLN A C   1 
ATOM   882  O O   . GLN A 1 120 ? 90.190  119.036 123.152 1.00 55.57  ? 120 GLN A O   1 
ATOM   883  C CB  . GLN A 1 120 ? 91.786  116.440 122.807 1.00 55.28  ? 120 GLN A CB  1 
ATOM   884  C CG  . GLN A 1 120 ? 91.926  114.977 123.192 1.00 56.26  ? 120 GLN A CG  1 
ATOM   885  C CD  . GLN A 1 120 ? 93.338  114.616 123.609 1.00 57.44  ? 120 GLN A CD  1 
ATOM   886  O OE1 . GLN A 1 120 ? 94.219  115.473 123.667 1.00 59.31  ? 120 GLN A OE1 1 
ATOM   887  N NE2 . GLN A 1 120 ? 93.561  113.340 123.898 1.00 57.48  ? 120 GLN A NE2 1 
ATOM   888  N N   . ILE A 1 121 ? 90.321  118.843 120.917 1.00 56.33  ? 121 ILE A N   1 
ATOM   889  C CA  . ILE A 1 121 ? 90.157  120.268 120.666 1.00 56.31  ? 121 ILE A CA  1 
ATOM   890  C C   . ILE A 1 121 ? 88.759  120.595 120.153 1.00 55.24  ? 121 ILE A C   1 
ATOM   891  O O   . ILE A 1 121 ? 88.146  121.565 120.600 1.00 55.63  ? 121 ILE A O   1 
ATOM   892  C CB  . ILE A 1 121 ? 91.238  120.769 119.684 1.00 57.14  ? 121 ILE A CB  1 
ATOM   893  C CG1 . ILE A 1 121 ? 92.626  120.304 120.126 1.00 58.02  ? 121 ILE A CG1 1 
ATOM   894  C CG2 . ILE A 1 121 ? 91.203  122.283 119.583 1.00 56.78  ? 121 ILE A CG2 1 
ATOM   895  C CD1 . ILE A 1 121 ? 93.015  120.766 121.512 1.00 58.17  ? 121 ILE A CD1 1 
ATOM   896  N N   . TYR A 1 122 ? 88.233  119.800 119.220 1.00 53.91  ? 122 TYR A N   1 
ATOM   897  C CA  . TYR A 1 122 ? 87.022  120.157 118.493 1.00 53.18  ? 122 TYR A CA  1 
ATOM   898  C C   . TYR A 1 122 ? 85.766  119.421 118.953 1.00 53.62  ? 122 TYR A C   1 
ATOM   899  O O   . TYR A 1 122 ? 84.710  119.612 118.342 1.00 54.22  ? 122 TYR A O   1 
ATOM   900  C CB  . TYR A 1 122 ? 87.215  119.906 116.993 1.00 52.19  ? 122 TYR A CB  1 
ATOM   901  C CG  . TYR A 1 122 ? 88.328  120.695 116.341 1.00 51.38  ? 122 TYR A CG  1 
ATOM   902  C CD1 . TYR A 1 122 ? 88.691  121.948 116.812 1.00 51.03  ? 122 TYR A CD1 1 
ATOM   903  C CD2 . TYR A 1 122 ? 88.999  120.192 115.235 1.00 51.07  ? 122 TYR A CD2 1 
ATOM   904  C CE1 . TYR A 1 122 ? 89.702  122.670 116.208 1.00 51.46  ? 122 TYR A CE1 1 
ATOM   905  C CE2 . TYR A 1 122 ? 90.007  120.906 114.626 1.00 51.20  ? 122 TYR A CE2 1 
ATOM   906  C CZ  . TYR A 1 122 ? 90.354  122.143 115.116 1.00 52.14  ? 122 TYR A CZ  1 
ATOM   907  O OH  . TYR A 1 122 ? 91.361  122.855 114.511 1.00 53.82  ? 122 TYR A OH  1 
ATOM   908  N N   . GLY A 1 123 ? 85.831  118.600 119.992 1.00 54.00  ? 123 GLY A N   1 
ATOM   909  C CA  . GLY A 1 123 ? 84.663  117.856 120.409 1.00 53.92  ? 123 GLY A CA  1 
ATOM   910  C C   . GLY A 1 123 ? 84.488  116.558 119.637 1.00 54.10  ? 123 GLY A C   1 
ATOM   911  O O   . GLY A 1 123 ? 85.012  116.366 118.539 1.00 54.85  ? 123 GLY A O   1 
ATOM   912  N N   . LYS A 1 124 ? 83.707  115.654 120.235 1.00 53.24  ? 124 LYS A N   1 
ATOM   913  C CA  . LYS A 1 124 ? 83.509  114.326 119.659 1.00 52.89  ? 124 LYS A CA  1 
ATOM   914  C C   . LYS A 1 124 ? 82.732  114.382 118.349 1.00 51.52  ? 124 LYS A C   1 
ATOM   915  O O   . LYS A 1 124 ? 82.983  113.572 117.445 1.00 51.98  ? 124 LYS A O   1 
ATOM   916  C CB  . LYS A 1 124 ? 82.782  113.428 120.660 1.00 54.37  ? 124 LYS A CB  1 
ATOM   917  C CG  . LYS A 1 124 ? 83.476  113.290 122.007 1.00 55.29  ? 124 LYS A CG  1 
ATOM   918  C CD  . LYS A 1 124 ? 84.833  112.623 121.879 1.00 55.76  ? 124 LYS A CD  1 
ATOM   919  C CE  . LYS A 1 124 ? 85.454  112.386 123.246 1.00 56.61  ? 124 LYS A CE  1 
ATOM   920  N NZ  . LYS A 1 124 ? 85.680  113.656 123.988 1.00 57.48  ? 124 LYS A NZ  1 
ATOM   921  N N   . ARG A 1 125 ? 81.782  115.313 118.233 1.00 50.09  ? 125 ARG A N   1 
ATOM   922  C CA  . ARG A 1 125 ? 80.998  115.433 117.007 1.00 49.58  ? 125 ARG A CA  1 
ATOM   923  C C   . ARG A 1 125 ? 81.883  115.806 115.825 1.00 48.22  ? 125 ARG A C   1 
ATOM   924  O O   . ARG A 1 125 ? 81.788  115.207 114.747 1.00 47.41  ? 125 ARG A O   1 
ATOM   925  C CB  . ARG A 1 125 ? 79.888  116.466 117.199 1.00 50.61  ? 125 ARG A CB  1 
ATOM   926  C CG  . ARG A 1 125 ? 78.915  116.128 118.314 1.00 51.69  ? 125 ARG A CG  1 
ATOM   927  C CD  . ARG A 1 125 ? 77.618  116.903 118.167 1.00 53.18  ? 125 ARG A CD  1 
ATOM   928  N NE  . ARG A 1 125 ? 77.062  117.280 119.460 1.00 55.54  ? 125 ARG A NE  1 
ATOM   929  C CZ  . ARG A 1 125 ? 77.405  118.370 120.133 1.00 58.02  ? 125 ARG A CZ  1 
ATOM   930  N NH1 . ARG A 1 125 ? 78.305  119.218 119.662 1.00 59.21  ? 125 ARG A NH1 1 
ATOM   931  N NH2 . ARG A 1 125 ? 76.832  118.616 121.307 1.00 58.46  ? 125 ARG A NH2 1 
ATOM   932  N N   . MET A 1 126 ? 82.776  116.779 116.015 1.00 47.22  ? 126 MET A N   1 
ATOM   933  C CA  . MET A 1 126 ? 83.684  117.137 114.932 1.00 46.43  ? 126 MET A CA  1 
ATOM   934  C C   . MET A 1 126 ? 84.757  116.072 114.739 1.00 45.75  ? 126 MET A C   1 
ATOM   935  O O   . MET A 1 126 ? 85.262  115.900 113.624 1.00 44.64  ? 126 MET A O   1 
ATOM   936  C CB  . MET A 1 126 ? 84.301  118.514 115.185 1.00 46.59  ? 126 MET A CB  1 
ATOM   937  C CG  . MET A 1 126 ? 85.229  118.969 114.075 1.00 47.20  ? 126 MET A CG  1 
ATOM   938  S SD  . MET A 1 126 ? 84.304  119.201 112.546 1.00 47.59  ? 126 MET A SD  1 
ATOM   939  C CE  . MET A 1 126 ? 85.380  120.308 111.653 1.00 47.01  ? 126 MET A CE  1 
ATOM   940  N N   . GLY A 1 127 ? 85.091  115.324 115.794 1.00 45.73  ? 127 GLY A N   1 
ATOM   941  C CA  . GLY A 1 127 ? 85.951  114.165 115.612 1.00 45.60  ? 127 GLY A CA  1 
ATOM   942  C C   . GLY A 1 127 ? 85.357  113.154 114.650 1.00 45.57  ? 127 GLY A C   1 
ATOM   943  O O   . GLY A 1 127 ? 86.033  112.666 113.744 1.00 46.21  ? 127 GLY A O   1 
ATOM   944  N N   . GLY A 1 128 ? 84.067  112.857 114.812 1.00 45.28  ? 128 GLY A N   1 
ATOM   945  C CA  . GLY A 1 128 ? 83.397  111.974 113.865 1.00 45.08  ? 128 GLY A CA  1 
ATOM   946  C C   . GLY A 1 128 ? 83.253  112.584 112.479 1.00 45.13  ? 128 GLY A C   1 
ATOM   947  O O   . GLY A 1 128 ? 83.392  111.889 111.461 1.00 45.83  ? 128 GLY A O   1 
ATOM   948  N N   . LEU A 1 129 ? 82.963  113.888 112.420 1.00 44.53  ? 129 LEU A N   1 
ATOM   949  C CA  . LEU A 1 129 ? 82.811  114.561 111.134 1.00 43.77  ? 129 LEU A CA  1 
ATOM   950  C C   . LEU A 1 129 ? 84.114  114.583 110.347 1.00 43.53  ? 129 LEU A C   1 
ATOM   951  O O   . LEU A 1 129 ? 84.089  114.602 109.114 1.00 43.17  ? 129 LEU A O   1 
ATOM   952  C CB  . LEU A 1 129 ? 82.297  115.986 111.339 1.00 43.51  ? 129 LEU A CB  1 
ATOM   953  C CG  . LEU A 1 129 ? 80.821  116.149 111.701 1.00 43.46  ? 129 LEU A CG  1 
ATOM   954  C CD1 . LEU A 1 129 ? 80.406  117.607 111.588 1.00 43.75  ? 129 LEU A CD1 1 
ATOM   955  C CD2 . LEU A 1 129 ? 79.949  115.272 110.819 1.00 43.42  ? 129 LEU A CD2 1 
ATOM   956  N N   . LEU A 1 130 ? 85.257  114.612 111.036 1.00 43.09  ? 130 LEU A N   1 
ATOM   957  C CA  . LEU A 1 130 ? 86.547  114.472 110.373 1.00 42.26  ? 130 LEU A CA  1 
ATOM   958  C C   . LEU A 1 130 ? 86.925  113.014 110.150 1.00 42.07  ? 130 LEU A C   1 
ATOM   959  O O   . LEU A 1 130 ? 87.746  112.725 109.274 1.00 42.43  ? 130 LEU A O   1 
ATOM   960  C CB  . LEU A 1 130 ? 87.642  115.165 111.186 1.00 41.60  ? 130 LEU A CB  1 
ATOM   961  C CG  . LEU A 1 130 ? 87.596  116.692 111.250 1.00 41.43  ? 130 LEU A CG  1 
ATOM   962  C CD1 . LEU A 1 130 ? 88.801  117.224 112.000 1.00 41.68  ? 130 LEU A CD1 1 
ATOM   963  C CD2 . LEU A 1 130 ? 87.525  117.291 109.861 1.00 41.53  ? 130 LEU A CD2 1 
ATOM   964  N N   . PHE A 1 131 ? 86.359  112.099 110.940 1.00 41.57  ? 131 PHE A N   1 
ATOM   965  C CA  . PHE A 1 131 ? 86.575  110.674 110.722 1.00 41.27  ? 131 PHE A CA  1 
ATOM   966  C C   . PHE A 1 131 ? 85.949  110.207 109.419 1.00 40.69  ? 131 PHE A C   1 
ATOM   967  O O   . PHE A 1 131 ? 86.494  109.315 108.759 1.00 41.12  ? 131 PHE A O   1 
ATOM   968  C CB  . PHE A 1 131 ? 86.005  109.883 111.902 1.00 41.80  ? 131 PHE A CB  1 
ATOM   969  C CG  . PHE A 1 131 ? 85.665  108.456 111.581 1.00 42.57  ? 131 PHE A CG  1 
ATOM   970  C CD1 . PHE A 1 131 ? 86.663  107.523 111.365 1.00 43.27  ? 131 PHE A CD1 1 
ATOM   971  C CD2 . PHE A 1 131 ? 84.346  108.046 111.511 1.00 42.69  ? 131 PHE A CD2 1 
ATOM   972  C CE1 . PHE A 1 131 ? 86.352  106.211 111.074 1.00 43.12  ? 131 PHE A CE1 1 
ATOM   973  C CE2 . PHE A 1 131 ? 84.029  106.736 111.221 1.00 42.97  ? 131 PHE A CE2 1 
ATOM   974  C CZ  . PHE A 1 131 ? 85.034  105.818 111.004 1.00 43.11  ? 131 PHE A CZ  1 
ATOM   975  N N   . ILE A 1 132 ? 84.801  110.785 109.048 1.00 40.35  ? 132 ILE A N   1 
ATOM   976  C CA  . ILE A 1 132 ? 84.099  110.336 107.838 1.00 40.26  ? 132 ILE A CA  1 
ATOM   977  C C   . ILE A 1 132 ? 84.948  110.460 106.571 1.00 39.94  ? 132 ILE A C   1 
ATOM   978  O O   . ILE A 1 132 ? 85.024  109.479 105.812 1.00 39.90  ? 132 ILE A O   1 
ATOM   979  C CB  . ILE A 1 132 ? 82.735  111.041 107.723 1.00 40.17  ? 132 ILE A CB  1 
ATOM   980  C CG1 . ILE A 1 132 ? 81.755  110.475 108.750 1.00 40.50  ? 132 ILE A CG1 1 
ATOM   981  C CG2 . ILE A 1 132 ? 82.170  110.896 106.322 1.00 39.78  ? 132 ILE A CG2 1 
ATOM   982  C CD1 . ILE A 1 132 ? 80.367  111.070 108.661 1.00 40.50  ? 132 ILE A CD1 1 
ATOM   983  N N   . PRO A 1 133 ? 85.609  111.597 106.278 1.00 39.84  ? 133 PRO A N   1 
ATOM   984  C CA  . PRO A 1 133 ? 86.512  111.606 105.112 1.00 39.61  ? 133 PRO A CA  1 
ATOM   985  C C   . PRO A 1 133 ? 87.687  110.654 105.236 1.00 40.44  ? 133 PRO A C   1 
ATOM   986  O O   . PRO A 1 133 ? 88.107  110.084 104.224 1.00 40.50  ? 133 PRO A O   1 
ATOM   987  C CB  . PRO A 1 133 ? 86.985  113.065 105.039 1.00 39.58  ? 133 PRO A CB  1 
ATOM   988  C CG  . PRO A 1 133 ? 85.948  113.831 105.726 1.00 40.27  ? 133 PRO A CG  1 
ATOM   989  C CD  . PRO A 1 133 ? 85.509  112.952 106.850 1.00 40.43  ? 133 PRO A CD  1 
ATOM   990  N N   . ALA A 1 134 ? 88.228  110.458 106.441 1.00 42.03  ? 134 ALA A N   1 
ATOM   991  C CA  . ALA A 1 134 ? 89.347  109.534 106.608 1.00 42.94  ? 134 ALA A CA  1 
ATOM   992  C C   . ALA A 1 134 ? 88.919  108.098 106.334 1.00 43.73  ? 134 ALA A C   1 
ATOM   993  O O   . ALA A 1 134 ? 89.614  107.357 105.628 1.00 44.50  ? 134 ALA A O   1 
ATOM   994  C CB  . ALA A 1 134 ? 89.935  109.665 108.012 1.00 42.57  ? 134 ALA A CB  1 
ATOM   995  N N   . LEU A 1 135 ? 87.768  107.693 106.881 1.00 43.96  ? 135 LEU A N   1 
ATOM   996  C CA  . LEU A 1 135 ? 87.229  106.367 106.597 1.00 43.57  ? 135 LEU A CA  1 
ATOM   997  C C   . LEU A 1 135 ? 86.944  106.197 105.113 1.00 43.61  ? 135 LEU A C   1 
ATOM   998  O O   . LEU A 1 135 ? 87.257  105.152 104.529 1.00 43.82  ? 135 LEU A O   1 
ATOM   999  C CB  . LEU A 1 135 ? 85.953  106.136 107.407 1.00 43.30  ? 135 LEU A CB  1 
ATOM   1000 C CG  . LEU A 1 135 ? 85.082  104.946 106.995 1.00 43.42  ? 135 LEU A CG  1 
ATOM   1001 C CD1 . LEU A 1 135 ? 85.845  103.641 107.119 1.00 43.92  ? 135 LEU A CD1 1 
ATOM   1002 C CD2 . LEU A 1 135 ? 83.789  104.899 107.792 1.00 43.41  ? 135 LEU A CD2 1 
ATOM   1003 N N   . MET A 1 136 ? 86.355  107.221 104.489 1.00 43.81  ? 136 MET A N   1 
ATOM   1004 C CA  . MET A 1 136 ? 86.050  107.160 103.065 1.00 43.90  ? 136 MET A CA  1 
ATOM   1005 C C   . MET A 1 136 ? 87.322  106.984 102.243 1.00 43.48  ? 136 MET A C   1 
ATOM   1006 O O   . MET A 1 136 ? 87.383  106.135 101.346 1.00 45.95  ? 136 MET A O   1 
ATOM   1007 C CB  . MET A 1 136 ? 85.303  108.429 102.652 1.00 44.77  ? 136 MET A CB  1 
ATOM   1008 C CG  . MET A 1 136 ? 84.269  108.236 101.567 1.00 45.48  ? 136 MET A CG  1 
ATOM   1009 S SD  . MET A 1 136 ? 83.133  109.632 101.456 1.00 47.14  ? 136 MET A SD  1 
ATOM   1010 C CE  . MET A 1 136 ? 84.021  110.709 100.337 1.00 46.90  ? 136 MET A CE  1 
ATOM   1011 N N   . GLY A 1 137 ? 88.364  107.750 102.572 1.00 42.13  ? 137 GLY A N   1 
ATOM   1012 C CA  . GLY A 1 137 ? 89.614  107.649 101.839 1.00 41.98  ? 137 GLY A CA  1 
ATOM   1013 C C   . GLY A 1 137 ? 90.284  106.299 102.000 1.00 41.95  ? 137 GLY A C   1 
ATOM   1014 O O   . GLY A 1 137 ? 90.739  105.703 101.021 1.00 41.00  ? 137 GLY A O   1 
ATOM   1015 N N   . GLU A 1 138 ? 90.350  105.797 103.238 1.00 42.49  ? 138 GLU A N   1 
ATOM   1016 C CA  . GLU A 1 138 ? 90.988  104.504 103.475 1.00 42.84  ? 138 GLU A CA  1 
ATOM   1017 C C   . GLU A 1 138 ? 90.240  103.381 102.766 1.00 43.35  ? 138 GLU A C   1 
ATOM   1018 O O   . GLU A 1 138 ? 90.853  102.528 102.110 1.00 43.90  ? 138 GLU A O   1 
ATOM   1019 C CB  . GLU A 1 138 ? 91.072  104.218 104.975 1.00 42.83  ? 138 GLU A CB  1 
ATOM   1020 C CG  . GLU A 1 138 ? 91.904  105.198 105.788 1.00 43.09  ? 138 GLU A CG  1 
ATOM   1021 C CD  . GLU A 1 138 ? 93.395  104.997 105.637 1.00 43.37  ? 138 GLU A CD  1 
ATOM   1022 O OE1 . GLU A 1 138 ? 93.813  104.053 104.935 1.00 43.91  ? 138 GLU A OE1 1 
ATOM   1023 O OE2 . GLU A 1 138 ? 94.156  105.777 106.246 1.00 44.09  ? 138 GLU A OE2 1 
ATOM   1024 N N   . MET A 1 139 ? 88.908  103.376 102.874 1.00 43.94  ? 139 MET A N   1 
ATOM   1025 C CA  . MET A 1 139 ? 88.116  102.320 102.255 1.00 44.40  ? 139 MET A CA  1 
ATOM   1026 C C   . MET A 1 139 ? 88.208  102.371 100.734 1.00 42.67  ? 139 MET A C   1 
ATOM   1027 O O   . MET A 1 139 ? 88.362  101.328 100.084 1.00 44.05  ? 139 MET A O   1 
ATOM   1028 C CB  . MET A 1 139 ? 86.668  102.427 102.729 1.00 47.48  ? 139 MET A CB  1 
ATOM   1029 C CG  . MET A 1 139 ? 85.863  101.151 102.609 1.00 50.28  ? 139 MET A CG  1 
ATOM   1030 S SD  . MET A 1 139 ? 84.325  101.242 103.548 1.00 55.48  ? 139 MET A SD  1 
ATOM   1031 C CE  . MET A 1 139 ? 83.588  102.731 102.879 1.00 53.43  ? 139 MET A CE  1 
ATOM   1032 N N   . PHE A 1 140 ? 88.153  103.570 100.144 1.00 40.84  ? 140 PHE A N   1 
ATOM   1033 C CA  . PHE A 1 140 ? 88.243  103.669 98.691  1.00 40.07  ? 140 PHE A CA  1 
ATOM   1034 C C   . PHE A 1 140 ? 89.637  103.315 98.188  1.00 38.88  ? 140 PHE A C   1 
ATOM   1035 O O   . PHE A 1 140 ? 89.774  102.701 97.125  1.00 39.41  ? 140 PHE A O   1 
ATOM   1036 C CB  . PHE A 1 140 ? 87.839  105.067 98.228  1.00 40.93  ? 140 PHE A CB  1 
ATOM   1037 C CG  . PHE A 1 140 ? 86.356  105.242 98.062  1.00 42.08  ? 140 PHE A CG  1 
ATOM   1038 C CD1 . PHE A 1 140 ? 85.646  104.430 97.198  1.00 42.69  ? 140 PHE A CD1 1 
ATOM   1039 C CD2 . PHE A 1 140 ? 85.675  106.227 98.754  1.00 42.38  ? 140 PHE A CD2 1 
ATOM   1040 C CE1 . PHE A 1 140 ? 84.285  104.589 97.039  1.00 43.23  ? 140 PHE A CE1 1 
ATOM   1041 C CE2 . PHE A 1 140 ? 84.314  106.389 98.596  1.00 42.53  ? 140 PHE A CE2 1 
ATOM   1042 C CZ  . PHE A 1 140 ? 83.619  105.570 97.738  1.00 42.95  ? 140 PHE A CZ  1 
ATOM   1043 N N   . TRP A 1 141 ? 90.685  103.687 98.932  1.00 37.36  ? 141 TRP A N   1 
ATOM   1044 C CA  . TRP A 1 141 ? 92.042  103.321 98.537  1.00 36.48  ? 141 TRP A CA  1 
ATOM   1045 C C   . TRP A 1 141 ? 92.240  101.811 98.583  1.00 35.39  ? 141 TRP A C   1 
ATOM   1046 O O   . TRP A 1 141 ? 92.825  101.222 97.659  1.00 35.40  ? 141 TRP A O   1 
ATOM   1047 C CB  . TRP A 1 141 ? 93.048  104.034 99.443  1.00 36.20  ? 141 TRP A CB  1 
ATOM   1048 C CG  . TRP A 1 141 ? 94.477  103.620 99.264  1.00 35.41  ? 141 TRP A CG  1 
ATOM   1049 C CD1 . TRP A 1 141 ? 95.106  103.315 98.093  1.00 34.73  ? 141 TRP A CD1 1 
ATOM   1050 C CD2 . TRP A 1 141 ? 95.460  103.481 100.295 1.00 34.90  ? 141 TRP A CD2 1 
ATOM   1051 N NE1 . TRP A 1 141 ? 96.418  102.988 98.333  1.00 34.34  ? 141 TRP A NE1 1 
ATOM   1052 C CE2 . TRP A 1 141 ? 96.660  103.084 99.678  1.00 34.53  ? 141 TRP A CE2 1 
ATOM   1053 C CE3 . TRP A 1 141 ? 95.441  103.652 101.683 1.00 35.00  ? 141 TRP A CE3 1 
ATOM   1054 C CZ2 . TRP A 1 141 ? 97.828  102.852 100.399 1.00 34.85  ? 141 TRP A CZ2 1 
ATOM   1055 C CZ3 . TRP A 1 141 ? 96.601  103.424 102.395 1.00 34.87  ? 141 TRP A CZ3 1 
ATOM   1056 C CH2 . TRP A 1 141 ? 97.778  103.029 101.753 1.00 35.06  ? 141 TRP A CH2 1 
ATOM   1057 N N   . ALA A 1 142 ? 91.745  101.166 99.645  1.00 34.52  ? 142 ALA A N   1 
ATOM   1058 C CA  . ALA A 1 142 ? 91.830  99.712  99.735  1.00 34.37  ? 142 ALA A CA  1 
ATOM   1059 C C   . ALA A 1 142 ? 91.061  99.045  98.603  1.00 34.29  ? 142 ALA A C   1 
ATOM   1060 O O   . ALA A 1 142 ? 91.551  98.086  97.994  1.00 34.58  ? 142 ALA A O   1 
ATOM   1061 C CB  . ALA A 1 142 ? 91.312  99.238  101.091 1.00 34.37  ? 142 ALA A CB  1 
ATOM   1062 N N   . ALA A 1 143 ? 89.865  99.552  98.289  1.00 34.77  ? 143 ALA A N   1 
ATOM   1063 C CA  . ALA A 1 143 ? 89.081  98.979  97.198  1.00 35.02  ? 143 ALA A CA  1 
ATOM   1064 C C   . ALA A 1 143 ? 89.779  99.155  95.853  1.00 35.06  ? 143 ALA A C   1 
ATOM   1065 O O   . ALA A 1 143 ? 89.775  98.240  95.022  1.00 36.04  ? 143 ALA A O   1 
ATOM   1066 C CB  . ALA A 1 143 ? 87.689  99.607  97.168  1.00 35.43  ? 143 ALA A CB  1 
ATOM   1067 N N   . ALA A 1 144 ? 90.389  100.319 95.622  1.00 34.96  ? 144 ALA A N   1 
ATOM   1068 C CA  . ALA A 1 144 ? 91.066  100.565 94.352  1.00 35.28  ? 144 ALA A CA  1 
ATOM   1069 C C   . ALA A 1 144 ? 92.265  99.643  94.170  1.00 35.21  ? 144 ALA A C   1 
ATOM   1070 O O   . ALA A 1 144 ? 92.456  99.060  93.094  1.00 35.44  ? 144 ALA A O   1 
ATOM   1071 C CB  . ALA A 1 144 ? 91.493  102.028 94.262  1.00 35.60  ? 144 ALA A CB  1 
ATOM   1072 N N   . ILE A 1 145 ? 93.081  99.480  95.214  1.00 34.92  ? 145 ILE A N   1 
ATOM   1073 C CA  . ILE A 1 145 ? 94.240  98.609  95.043  1.00 34.65  ? 145 ILE A CA  1 
ATOM   1074 C C   . ILE A 1 145 ? 93.825  97.139  95.001  1.00 35.18  ? 145 ILE A C   1 
ATOM   1075 O O   . ILE A 1 145 ? 94.485  96.324  94.342  1.00 35.90  ? 145 ILE A O   1 
ATOM   1076 C CB  . ILE A 1 145 ? 95.303  98.887  96.119  1.00 34.60  ? 145 ILE A CB  1 
ATOM   1077 C CG1 . ILE A 1 145 ? 94.744  98.664  97.518  1.00 35.30  ? 145 ILE A CG1 1 
ATOM   1078 C CG2 . ILE A 1 145 ? 95.842  100.301 95.968  1.00 34.66  ? 145 ILE A CG2 1 
ATOM   1079 C CD1 . ILE A 1 145 ? 95.650  99.171  98.594  1.00 35.62  ? 145 ILE A CD1 1 
ATOM   1080 N N   . PHE A 1 146 ? 92.722  96.769  95.664  1.00 35.55  ? 146 PHE A N   1 
ATOM   1081 C CA  . PHE A 1 146 ? 92.214  95.407  95.518  1.00 35.35  ? 146 PHE A CA  1 
ATOM   1082 C C   . PHE A 1 146 ? 91.718  95.150  94.100  1.00 35.71  ? 146 PHE A C   1 
ATOM   1083 O O   . PHE A 1 146 ? 91.916  94.057  93.559  1.00 36.51  ? 146 PHE A O   1 
ATOM   1084 C CB  . PHE A 1 146 ? 91.102  95.133  96.527  1.00 35.03  ? 146 PHE A CB  1 
ATOM   1085 C CG  . PHE A 1 146 ? 91.591  94.556  97.821  1.00 34.61  ? 146 PHE A CG  1 
ATOM   1086 C CD1 . PHE A 1 146 ? 92.383  93.424  97.830  1.00 34.30  ? 146 PHE A CD1 1 
ATOM   1087 C CD2 . PHE A 1 146 ? 91.229  95.123  99.029  1.00 34.86  ? 146 PHE A CD2 1 
ATOM   1088 C CE1 . PHE A 1 146 ? 92.828  92.884  99.019  1.00 34.34  ? 146 PHE A CE1 1 
ATOM   1089 C CE2 . PHE A 1 146 ? 91.665  94.584  100.220 1.00 34.83  ? 146 PHE A CE2 1 
ATOM   1090 C CZ  . PHE A 1 146 ? 92.467  93.465  100.215 1.00 34.36  ? 146 PHE A CZ  1 
ATOM   1091 N N   . SER A 1 147 ? 91.069  96.141  93.484  1.00 36.19  ? 147 SER A N   1 
ATOM   1092 C CA  . SER A 1 147 ? 90.672  96.000  92.086  1.00 36.77  ? 147 SER A CA  1 
ATOM   1093 C C   . SER A 1 147 ? 91.891  95.901  91.177  1.00 36.50  ? 147 SER A C   1 
ATOM   1094 O O   . SER A 1 147 ? 91.868  95.176  90.175  1.00 36.42  ? 147 SER A O   1 
ATOM   1095 C CB  . SER A 1 147 ? 89.785  97.170  91.668  1.00 37.82  ? 147 SER A CB  1 
ATOM   1096 O OG  . SER A 1 147 ? 89.268  96.973  90.365  1.00 39.02  ? 147 SER A OG  1 
ATOM   1097 N N   . ALA A 1 148 ? 92.963  96.625  91.512  1.00 36.28  ? 148 ALA A N   1 
ATOM   1098 C CA  . ALA A 1 148 ? 94.206  96.501  90.754  1.00 36.24  ? 148 ALA A CA  1 
ATOM   1099 C C   . ALA A 1 148 ? 94.780  95.091  90.852  1.00 36.14  ? 148 ALA A C   1 
ATOM   1100 O O   . ALA A 1 148 ? 95.209  94.519  89.842  1.00 35.52  ? 148 ALA A O   1 
ATOM   1101 C CB  . ALA A 1 148 ? 95.225  97.530  91.239  1.00 36.43  ? 148 ALA A CB  1 
ATOM   1102 N N   . LEU A 1 149 ? 94.789  94.513  92.060  1.00 36.63  ? 149 LEU A N   1 
ATOM   1103 C CA  . LEU A 1 149 ? 95.215  93.121  92.220  1.00 37.00  ? 149 LEU A CA  1 
ATOM   1104 C C   . LEU A 1 149 ? 94.334  92.170  91.421  1.00 37.46  ? 149 LEU A C   1 
ATOM   1105 O O   . LEU A 1 149 ? 94.838  91.236  90.785  1.00 38.58  ? 149 LEU A O   1 
ATOM   1106 C CB  . LEU A 1 149 ? 95.228  92.729  93.704  1.00 36.58  ? 149 LEU A CB  1 
ATOM   1107 C CG  . LEU A 1 149 ? 95.768  91.350  94.128  1.00 36.30  ? 149 LEU A CG  1 
ATOM   1108 C CD1 . LEU A 1 149 ? 96.345  91.365  95.516  1.00 36.17  ? 149 LEU A CD1 1 
ATOM   1109 C CD2 . LEU A 1 149 ? 94.644  90.325  94.144  1.00 36.18  ? 149 LEU A CD2 1 
ATOM   1110 N N   . GLY A 1 150 ? 93.017  92.375  91.469  1.00 37.61  ? 150 GLY A N   1 
ATOM   1111 C CA  . GLY A 1 150 ? 92.115  91.495  90.744  1.00 37.79  ? 150 GLY A CA  1 
ATOM   1112 C C   . GLY A 1 150 ? 92.359  91.529  89.249  1.00 38.34  ? 150 GLY A C   1 
ATOM   1113 O O   . GLY A 1 150 ? 92.452  90.485  88.597  1.00 38.65  ? 150 GLY A O   1 
ATOM   1114 N N   . ALA A 1 151 ? 92.502  92.735  88.693  1.00 39.42  ? 151 ALA A N   1 
ATOM   1115 C CA  . ALA A 1 151 ? 92.771  92.871  87.266  1.00 40.38  ? 151 ALA A CA  1 
ATOM   1116 C C   . ALA A 1 151 ? 94.127  92.281  86.892  1.00 40.91  ? 151 ALA A C   1 
ATOM   1117 O O   . ALA A 1 151 ? 94.252  91.605  85.864  1.00 41.34  ? 151 ALA A O   1 
ATOM   1118 C CB  . ALA A 1 151 ? 92.693  94.340  86.858  1.00 40.64  ? 151 ALA A CB  1 
ATOM   1119 N N   . THR A 1 152 ? 95.149  92.507  87.724  1.00 40.90  ? 152 THR A N   1 
ATOM   1120 C CA  . THR A 1 152 ? 96.484  91.997  87.421  1.00 40.55  ? 152 THR A CA  1 
ATOM   1121 C C   . THR A 1 152 ? 96.511  90.471  87.415  1.00 39.88  ? 152 THR A C   1 
ATOM   1122 O O   . THR A 1 152 ? 97.063  89.852  86.496  1.00 39.50  ? 152 THR A O   1 
ATOM   1123 C CB  . THR A 1 152 ? 97.490  92.552  88.430  1.00 40.61  ? 152 THR A CB  1 
ATOM   1124 O OG1 . THR A 1 152 ? 97.608  93.969  88.255  1.00 41.31  ? 152 THR A OG1 1 
ATOM   1125 C CG2 . THR A 1 152 ? 98.851  91.917  88.239  1.00 40.63  ? 152 THR A CG2 1 
ATOM   1126 N N   . ILE A 1 153 ? 95.907  89.845  88.428  1.00 39.42  ? 153 ILE A N   1 
ATOM   1127 C CA  . ILE A 1 153 ? 95.905  88.386  88.487  1.00 39.06  ? 153 ILE A CA  1 
ATOM   1128 C C   . ILE A 1 153 ? 95.023  87.800  87.388  1.00 39.83  ? 153 ILE A C   1 
ATOM   1129 O O   . ILE A 1 153 ? 95.358  86.765  86.798  1.00 40.86  ? 153 ILE A O   1 
ATOM   1130 C CB  . ILE A 1 153 ? 95.505  87.906  89.896  1.00 38.19  ? 153 ILE A CB  1 
ATOM   1131 C CG1 . ILE A 1 153 ? 96.662  88.173  90.858  1.00 37.79  ? 153 ILE A CG1 1 
ATOM   1132 C CG2 . ILE A 1 153 ? 95.154  86.430  89.910  1.00 37.89  ? 153 ILE A CG2 1 
ATOM   1133 C CD1 . ILE A 1 153 ? 96.405  87.790  92.281  1.00 37.54  ? 153 ILE A CD1 1 
ATOM   1134 N N   . SER A 1 154 ? 93.907  88.462  87.063  1.00 40.97  ? 154 SER A N   1 
ATOM   1135 C CA  . SER A 1 154 ? 93.095  88.006  85.939  1.00 42.24  ? 154 SER A CA  1 
ATOM   1136 C C   . SER A 1 154 ? 93.841  88.133  84.616  1.00 42.33  ? 154 SER A C   1 
ATOM   1137 O O   . SER A 1 154 ? 93.556  87.389  83.671  1.00 42.22  ? 154 SER A O   1 
ATOM   1138 C CB  . SER A 1 154 ? 91.783  88.786  85.885  1.00 43.43  ? 154 SER A CB  1 
ATOM   1139 O OG  . SER A 1 154 ? 90.995  88.377  84.782  1.00 44.78  ? 154 SER A OG  1 
ATOM   1140 N N   . VAL A 1 155 ? 94.786  89.069  84.523  1.00 43.10  ? 155 VAL A N   1 
ATOM   1141 C CA  . VAL A 1 155 ? 95.588  89.188  83.309  1.00 44.35  ? 155 VAL A CA  1 
ATOM   1142 C C   . VAL A 1 155 ? 96.660  88.102  83.250  1.00 45.07  ? 155 VAL A C   1 
ATOM   1143 O O   . VAL A 1 155 ? 96.831  87.443  82.218  1.00 44.77  ? 155 VAL A O   1 
ATOM   1144 C CB  . VAL A 1 155 ? 96.199  90.599  83.215  1.00 44.61  ? 155 VAL A CB  1 
ATOM   1145 C CG1 . VAL A 1 155 ? 97.415  90.608  82.298  1.00 44.51  ? 155 VAL A CG1 1 
ATOM   1146 C CG2 . VAL A 1 155 ? 95.162  91.591  82.716  1.00 44.74  ? 155 VAL A CG2 1 
ATOM   1147 N N   . ILE A 1 156 ? 97.385  87.882  84.349  1.00 45.68  ? 156 ILE A N   1 
ATOM   1148 C CA  . ILE A 1 156 ? 98.565  87.019  84.295  1.00 45.40  ? 156 ILE A CA  1 
ATOM   1149 C C   . ILE A 1 156 ? 98.166  85.545  84.285  1.00 46.40  ? 156 ILE A C   1 
ATOM   1150 O O   . ILE A 1 156 ? 98.429  84.822  83.318  1.00 45.54  ? 156 ILE A O   1 
ATOM   1151 C CB  . ILE A 1 156 ? 99.525  87.336  85.454  1.00 44.55  ? 156 ILE A CB  1 
ATOM   1152 C CG1 . ILE A 1 156 ? 100.007 88.783  85.353  1.00 44.21  ? 156 ILE A CG1 1 
ATOM   1153 C CG2 . ILE A 1 156 ? 100.702 86.377  85.442  1.00 44.58  ? 156 ILE A CG2 1 
ATOM   1154 C CD1 . ILE A 1 156 ? 101.121 89.133  86.306  1.00 43.66  ? 156 ILE A CD1 1 
ATOM   1155 N N   . ILE A 1 157 ? 97.529  85.075  85.360  1.00 48.57  ? 157 ILE A N   1 
ATOM   1156 C CA  . ILE A 1 157 ? 97.257  83.644  85.478  1.00 50.29  ? 157 ILE A CA  1 
ATOM   1157 C C   . ILE A 1 157 ? 95.984  83.261  84.725  1.00 52.30  ? 157 ILE A C   1 
ATOM   1158 O O   . ILE A 1 157 ? 95.815  82.089  84.359  1.00 53.35  ? 157 ILE A O   1 
ATOM   1159 C CB  . ILE A 1 157 ? 97.165  83.248  86.963  1.00 50.25  ? 157 ILE A CB  1 
ATOM   1160 C CG1 . ILE A 1 157 ? 98.472  83.543  87.679  1.00 50.35  ? 157 ILE A CG1 1 
ATOM   1161 C CG2 . ILE A 1 157 ? 97.014  81.748  87.138  1.00 50.59  ? 157 ILE A CG2 1 
ATOM   1162 C CD1 . ILE A 1 157 ? 98.347  83.411  89.172  1.00 50.31  ? 157 ILE A CD1 1 
ATOM   1163 N N   . ASP A 1 158 ? 95.117  84.241  84.442  1.00 54.37  ? 158 ASP A N   1 
ATOM   1164 C CA  . ASP A 1 158 ? 93.782  84.035  83.867  1.00 56.13  ? 158 ASP A CA  1 
ATOM   1165 C C   . ASP A 1 158 ? 92.919  83.216  84.832  1.00 57.24  ? 158 ASP A C   1 
ATOM   1166 O O   . ASP A 1 158 ? 92.319  82.200  84.474  1.00 58.33  ? 158 ASP A O   1 
ATOM   1167 C CB  . ASP A 1 158 ? 93.855  83.399  82.468  1.00 56.87  ? 158 ASP A CB  1 
ATOM   1168 C CG  . ASP A 1 158 ? 92.515  83.389  81.737  1.00 58.08  ? 158 ASP A CG  1 
ATOM   1169 O OD1 . ASP A 1 158 ? 91.497  83.848  82.298  1.00 57.94  ? 158 ASP A OD1 1 
ATOM   1170 O OD2 . ASP A 1 158 ? 92.484  82.911  80.583  1.00 60.14  ? 158 ASP A OD2 1 
ATOM   1171 N N   . VAL A 1 159 ? 92.892  83.660  86.087  1.00 58.66  ? 159 VAL A N   1 
ATOM   1172 C CA  . VAL A 1 159 ? 91.939  83.204  87.091  1.00 60.13  ? 159 VAL A CA  1 
ATOM   1173 C C   . VAL A 1 159 ? 90.710  84.096  86.989  1.00 61.68  ? 159 VAL A C   1 
ATOM   1174 O O   . VAL A 1 159 ? 90.806  85.259  86.580  1.00 61.84  ? 159 VAL A O   1 
ATOM   1175 C CB  . VAL A 1 159 ? 92.575  83.242  88.501  1.00 60.56  ? 159 VAL A CB  1 
ATOM   1176 C CG1 . VAL A 1 159 ? 91.593  82.838  89.595  1.00 60.61  ? 159 VAL A CG1 1 
ATOM   1177 C CG2 . VAL A 1 159 ? 93.779  82.343  88.551  1.00 60.53  ? 159 VAL A CG2 1 
ATOM   1178 N N   . ASP A 1 160 ? 89.540  83.545  87.317  1.00 63.46  ? 160 ASP A N   1 
ATOM   1179 C CA  . ASP A 1 160 ? 88.330  84.350  87.411  1.00 64.82  ? 160 ASP A CA  1 
ATOM   1180 C C   . ASP A 1 160 ? 88.530  85.481  88.414  1.00 64.60  ? 160 ASP A C   1 
ATOM   1181 O O   . ASP A 1 160 ? 89.079  85.280  89.501  1.00 63.60  ? 160 ASP A O   1 
ATOM   1182 C CB  . ASP A 1 160 ? 87.146  83.475  87.821  1.00 65.58  ? 160 ASP A CB  1 
ATOM   1183 C CG  . ASP A 1 160 ? 85.819  84.033  87.352  1.00 66.31  ? 160 ASP A CG  1 
ATOM   1184 O OD1 . ASP A 1 160 ? 85.739  85.252  87.094  1.00 66.49  ? 160 ASP A OD1 1 
ATOM   1185 O OD2 . ASP A 1 160 ? 84.854  83.250  87.238  1.00 67.59  ? 160 ASP A OD2 1 
ATOM   1186 N N   . MET A 1 161 ? 88.091  86.682  88.030  1.00 64.24  ? 161 MET A N   1 
ATOM   1187 C CA  . MET A 1 161 ? 88.441  87.883  88.782  1.00 64.18  ? 161 MET A CA  1 
ATOM   1188 C C   . MET A 1 161 ? 87.757  87.929  90.143  1.00 62.80  ? 161 MET A C   1 
ATOM   1189 O O   . MET A 1 161 ? 88.324  88.474  91.097  1.00 62.90  ? 161 MET A O   1 
ATOM   1190 C CB  . MET A 1 161 ? 88.095  89.125  87.957  1.00 66.18  ? 161 MET A CB  1 
ATOM   1191 C CG  . MET A 1 161 ? 88.873  90.386  88.320  1.00 68.14  ? 161 MET A CG  1 
ATOM   1192 S SD  . MET A 1 161 ? 88.208  91.321  89.711  1.00 72.28  ? 161 MET A SD  1 
ATOM   1193 C CE  . MET A 1 161 ? 87.121  92.464  88.863  1.00 70.99  ? 161 MET A CE  1 
ATOM   1194 N N   . HIS A 1 162 ? 86.565  87.350  90.269  1.00 61.13  ? 162 HIS A N   1 
ATOM   1195 C CA  . HIS A 1 162 ? 85.817  87.470  91.515  1.00 60.27  ? 162 HIS A CA  1 
ATOM   1196 C C   . HIS A 1 162 ? 86.247  86.469  92.578  1.00 56.83  ? 162 HIS A C   1 
ATOM   1197 O O   . HIS A 1 162 ? 85.691  86.489  93.679  1.00 55.74  ? 162 HIS A O   1 
ATOM   1198 C CB  . HIS A 1 162 ? 84.311  87.339  91.253  1.00 62.64  ? 162 HIS A CB  1 
ATOM   1199 C CG  . HIS A 1 162 ? 83.925  86.120  90.475  1.00 65.47  ? 162 HIS A CG  1 
ATOM   1200 N ND1 . HIS A 1 162 ? 84.085  84.841  90.962  1.00 67.53  ? 162 HIS A ND1 1 
ATOM   1201 C CD2 . HIS A 1 162 ? 83.363  85.988  89.250  1.00 66.71  ? 162 HIS A CD2 1 
ATOM   1202 C CE1 . HIS A 1 162 ? 83.649  83.973  90.067  1.00 68.06  ? 162 HIS A CE1 1 
ATOM   1203 N NE2 . HIS A 1 162 ? 83.204  84.643  89.019  1.00 67.99  ? 162 HIS A NE2 1 
ATOM   1204 N N   . ILE A 1 163 ? 87.211  85.601  92.286  1.00 53.10  ? 163 ILE A N   1 
ATOM   1205 C CA  . ILE A 1 163 ? 87.713  84.641  93.258  1.00 50.33  ? 163 ILE A CA  1 
ATOM   1206 C C   . ILE A 1 163 ? 89.024  85.104  93.880  1.00 49.54  ? 163 ILE A C   1 
ATOM   1207 O O   . ILE A 1 163 ? 89.197  85.031  95.098  1.00 48.79  ? 163 ILE A O   1 
ATOM   1208 C CB  . ILE A 1 163 ? 87.864  83.254  92.593  1.00 48.55  ? 163 ILE A CB  1 
ATOM   1209 C CG1 . ILE A 1 163 ? 86.508  82.551  92.519  1.00 47.85  ? 163 ILE A CG1 1 
ATOM   1210 C CG2 . ILE A 1 163 ? 88.861  82.384  93.343  1.00 48.24  ? 163 ILE A CG2 1 
ATOM   1211 C CD1 . ILE A 1 163 ? 86.544  81.239  91.768  1.00 47.66  ? 163 ILE A CD1 1 
ATOM   1212 N N   . SER A 1 164 ? 89.947  85.603  93.053  1.00 49.17  ? 164 SER A N   1 
ATOM   1213 C CA  . SER A 1 164 ? 91.287  85.927  93.532  1.00 48.43  ? 164 SER A CA  1 
ATOM   1214 C C   . SER A 1 164 ? 91.280  87.122  94.477  1.00 46.17  ? 164 SER A C   1 
ATOM   1215 O O   . SER A 1 164 ? 91.965  87.105  95.508  1.00 45.92  ? 164 SER A O   1 
ATOM   1216 C CB  . SER A 1 164 ? 92.213  86.191  92.349  1.00 49.32  ? 164 SER A CB  1 
ATOM   1217 O OG  . SER A 1 164 ? 93.500  86.554  92.804  1.00 50.64  ? 164 SER A OG  1 
ATOM   1218 N N   . VAL A 1 165 ? 90.525  88.171  94.142  1.00 44.24  ? 165 VAL A N   1 
ATOM   1219 C CA  . VAL A 1 165 ? 90.459  89.329  95.027  1.00 43.50  ? 165 VAL A CA  1 
ATOM   1220 C C   . VAL A 1 165 ? 89.769  88.968  96.339  1.00 43.28  ? 165 VAL A C   1 
ATOM   1221 O O   . VAL A 1 165 ? 90.163  89.458  97.405  1.00 43.86  ? 165 VAL A O   1 
ATOM   1222 C CB  . VAL A 1 165 ? 89.795  90.527  94.311  1.00 42.90  ? 165 VAL A CB  1 
ATOM   1223 C CG1 . VAL A 1 165 ? 88.300  90.325  94.112  1.00 42.48  ? 165 VAL A CG1 1 
ATOM   1224 C CG2 . VAL A 1 165 ? 90.050  91.807  95.084  1.00 42.69  ? 165 VAL A CG2 1 
ATOM   1225 N N   . ILE A 1 166 ? 88.779  88.070  96.300  1.00 42.44  ? 166 ILE A N   1 
ATOM   1226 C CA  . ILE A 1 166 ? 88.115  87.640  97.526  1.00 41.76  ? 166 ILE A CA  1 
ATOM   1227 C C   . ILE A 1 166 ? 89.074  86.846  98.404  1.00 41.72  ? 166 ILE A C   1 
ATOM   1228 O O   . ILE A 1 166 ? 89.134  87.057  99.619  1.00 41.77  ? 166 ILE A O   1 
ATOM   1229 C CB  . ILE A 1 166 ? 86.838  86.843  97.196  1.00 41.29  ? 166 ILE A CB  1 
ATOM   1230 C CG1 . ILE A 1 166 ? 85.696  87.798  96.850  1.00 41.16  ? 166 ILE A CG1 1 
ATOM   1231 C CG2 . ILE A 1 166 ? 86.435  85.941  98.352  1.00 41.10  ? 166 ILE A CG2 1 
ATOM   1232 C CD1 . ILE A 1 166 ? 84.375  87.108  96.595  1.00 41.34  ? 166 ILE A CD1 1 
ATOM   1233 N N   . ILE A 1 167 ? 89.857  85.943  97.805  1.00 41.21  ? 167 ILE A N   1 
ATOM   1234 C CA  . ILE A 1 167 ? 90.814  85.155  98.584  1.00 40.21  ? 167 ILE A CA  1 
ATOM   1235 C C   . ILE A 1 167 ? 91.897  86.048  99.184  1.00 39.82  ? 167 ILE A C   1 
ATOM   1236 O O   . ILE A 1 167 ? 92.259  85.901  100.361 1.00 39.32  ? 167 ILE A O   1 
ATOM   1237 C CB  . ILE A 1 167 ? 91.415  84.034  97.716  1.00 39.76  ? 167 ILE A CB  1 
ATOM   1238 C CG1 . ILE A 1 167 ? 90.338  83.015  97.345  1.00 39.80  ? 167 ILE A CG1 1 
ATOM   1239 C CG2 . ILE A 1 167 ? 92.560  83.345  98.437  1.00 39.58  ? 167 ILE A CG2 1 
ATOM   1240 C CD1 . ILE A 1 167 ? 89.696  82.348  98.538  1.00 39.69  ? 167 ILE A CD1 1 
ATOM   1241 N N   . SER A 1 168 ? 92.424  86.990  98.396  1.00 39.70  ? 168 SER A N   1 
ATOM   1242 C CA  . SER A 1 168 ? 93.462  87.888  98.897  1.00 39.28  ? 168 SER A CA  1 
ATOM   1243 C C   . SER A 1 168 ? 92.938  88.761  100.033 1.00 38.41  ? 168 SER A C   1 
ATOM   1244 O O   . SER A 1 168 ? 93.601  88.918  101.068 1.00 39.46  ? 168 SER A O   1 
ATOM   1245 C CB  . SER A 1 168 ? 93.999  88.754  97.758  1.00 39.50  ? 168 SER A CB  1 
ATOM   1246 O OG  . SER A 1 168 ? 94.971  89.668  98.230  1.00 39.65  ? 168 SER A OG  1 
ATOM   1247 N N   . ALA A 1 169 ? 91.739  89.325  99.863  1.00 37.18  ? 169 ALA A N   1 
ATOM   1248 C CA  . ALA A 1 169 ? 91.154  90.147  100.914 1.00 37.58  ? 169 ALA A CA  1 
ATOM   1249 C C   . ALA A 1 169 ? 90.843  89.321  102.154 1.00 37.75  ? 169 ALA A C   1 
ATOM   1250 O O   . ALA A 1 169 ? 91.018  89.801  103.277 1.00 37.73  ? 169 ALA A O   1 
ATOM   1251 C CB  . ALA A 1 169 ? 89.894  90.837  100.401 1.00 38.34  ? 169 ALA A CB  1 
ATOM   1252 N N   . LEU A 1 170 ? 90.390  88.078  101.970 1.00 38.21  ? 170 LEU A N   1 
ATOM   1253 C CA  . LEU A 1 170 ? 90.100  87.210  103.105 1.00 38.81  ? 170 LEU A CA  1 
ATOM   1254 C C   . LEU A 1 170 ? 91.357  86.904  103.905 1.00 39.15  ? 170 LEU A C   1 
ATOM   1255 O O   . LEU A 1 170 ? 91.338  86.953  105.138 1.00 39.80  ? 170 LEU A O   1 
ATOM   1256 C CB  . LEU A 1 170 ? 89.448  85.917  102.620 1.00 38.82  ? 170 LEU A CB  1 
ATOM   1257 C CG  . LEU A 1 170 ? 89.213  84.835  103.672 1.00 38.66  ? 170 LEU A CG  1 
ATOM   1258 C CD1 . LEU A 1 170 ? 88.296  85.345  104.769 1.00 38.48  ? 170 LEU A CD1 1 
ATOM   1259 C CD2 . LEU A 1 170 ? 88.643  83.583  103.029 1.00 38.83  ? 170 LEU A CD2 1 
ATOM   1260 N N   . ILE A 1 171 ? 92.465  86.608  103.223 1.00 39.03  ? 171 ILE A N   1 
ATOM   1261 C CA  . ILE A 1 171 ? 93.704  86.294  103.932 1.00 38.78  ? 171 ILE A CA  1 
ATOM   1262 C C   . ILE A 1 171 ? 94.257  87.529  104.640 1.00 38.66  ? 171 ILE A C   1 
ATOM   1263 O O   . ILE A 1 171 ? 94.686  87.456  105.805 1.00 38.68  ? 171 ILE A O   1 
ATOM   1264 C CB  . ILE A 1 171 ? 94.721  85.673  102.959 1.00 38.82  ? 171 ILE A CB  1 
ATOM   1265 C CG1 . ILE A 1 171 ? 94.256  84.270  102.569 1.00 39.24  ? 171 ILE A CG1 1 
ATOM   1266 C CG2 . ILE A 1 171 ? 96.107  85.627  103.571 1.00 38.78  ? 171 ILE A CG2 1 
ATOM   1267 C CD1 . ILE A 1 171 ? 95.027  83.657  101.441 1.00 39.73  ? 171 ILE A CD1 1 
ATOM   1268 N N   . ALA A 1 172 ? 94.238  88.684  103.962 1.00 39.01  ? 172 ALA A N   1 
ATOM   1269 C CA  . ALA A 1 172 ? 94.709  89.918  104.584 1.00 39.12  ? 172 ALA A CA  1 
ATOM   1270 C C   . ALA A 1 172 ? 93.874  90.272  105.809 1.00 38.80  ? 172 ALA A C   1 
ATOM   1271 O O   . ALA A 1 172 ? 94.417  90.573  106.882 1.00 39.36  ? 172 ALA A O   1 
ATOM   1272 C CB  . ALA A 1 172 ? 94.686  91.060  103.569 1.00 39.58  ? 172 ALA A CB  1 
ATOM   1273 N N   . THR A 1 173 ? 92.546  90.207  105.671 1.00 38.10  ? 173 THR A N   1 
ATOM   1274 C CA  . THR A 1 173 ? 91.648  90.494  106.781 1.00 38.17  ? 173 THR A CA  1 
ATOM   1275 C C   . THR A 1 173 ? 91.847  89.503  107.917 1.00 38.32  ? 173 THR A C   1 
ATOM   1276 O O   . THR A 1 173 ? 91.835  89.889  109.088 1.00 39.51  ? 173 THR A O   1 
ATOM   1277 C CB  . THR A 1 173 ? 90.199  90.477  106.290 1.00 38.18  ? 173 THR A CB  1 
ATOM   1278 O OG1 . THR A 1 173 ? 89.993  91.557  105.372 1.00 38.89  ? 173 THR A OG1 1 
ATOM   1279 C CG2 . THR A 1 173 ? 89.223  90.620  107.446 1.00 37.89  ? 173 THR A CG2 1 
ATOM   1280 N N   . LEU A 1 174 ? 92.071  88.228  107.590 1.00 37.90  ? 174 LEU A N   1 
ATOM   1281 C CA  . LEU A 1 174 ? 92.250  87.210  108.619 1.00 37.26  ? 174 LEU A CA  1 
ATOM   1282 C C   . LEU A 1 174 ? 93.492  87.478  109.459 1.00 36.73  ? 174 LEU A C   1 
ATOM   1283 O O   . LEU A 1 174 ? 93.438  87.444  110.696 1.00 36.25  ? 174 LEU A O   1 
ATOM   1284 C CB  . LEU A 1 174 ? 92.325  85.828  107.972 1.00 37.22  ? 174 LEU A CB  1 
ATOM   1285 C CG  . LEU A 1 174 ? 92.355  84.638  108.928 1.00 37.37  ? 174 LEU A CG  1 
ATOM   1286 C CD1 . LEU A 1 174 ? 91.071  84.580  109.734 1.00 37.68  ? 174 LEU A CD1 1 
ATOM   1287 C CD2 . LEU A 1 174 ? 92.563  83.347  108.159 1.00 37.62  ? 174 LEU A CD2 1 
ATOM   1288 N N   . TYR A 1 175 ? 94.624  87.774  108.811 1.00 36.48  ? 175 TYR A N   1 
ATOM   1289 C CA  . TYR A 1 175 ? 95.823  87.945  109.629 1.00 35.65  ? 175 TYR A CA  1 
ATOM   1290 C C   . TYR A 1 175 ? 95.824  89.287  110.362 1.00 34.56  ? 175 TYR A C   1 
ATOM   1291 O O   . TYR A 1 175 ? 96.277  89.359  111.515 1.00 34.41  ? 175 TYR A O   1 
ATOM   1292 C CB  . TYR A 1 175 ? 97.100  87.714  108.801 1.00 35.72  ? 175 TYR A CB  1 
ATOM   1293 C CG  . TYR A 1 175 ? 97.633  88.826  107.916 1.00 35.79  ? 175 TYR A CG  1 
ATOM   1294 C CD1 . TYR A 1 175 ? 98.337  89.897  108.448 1.00 35.63  ? 175 TYR A CD1 1 
ATOM   1295 C CD2 . TYR A 1 175 ? 97.512  88.752  106.537 1.00 36.11  ? 175 TYR A CD2 1 
ATOM   1296 C CE1 . TYR A 1 175 ? 98.845  90.890  107.639 1.00 36.04  ? 175 TYR A CE1 1 
ATOM   1297 C CE2 . TYR A 1 175 ? 98.024  89.740  105.720 1.00 36.10  ? 175 TYR A CE2 1 
ATOM   1298 C CZ  . TYR A 1 175 ? 98.687  90.806  106.276 1.00 36.31  ? 175 TYR A CZ  1 
ATOM   1299 O OH  . TYR A 1 175 ? 99.197  91.794  105.467 1.00 36.59  ? 175 TYR A OH  1 
ATOM   1300 N N   . THR A 1 176 ? 95.288  90.355  109.751 1.00 33.93  ? 176 THR A N   1 
ATOM   1301 C CA  . THR A 1 176 ? 95.214  91.611  110.495 1.00 34.40  ? 176 THR A CA  1 
ATOM   1302 C C   . THR A 1 176 ? 94.169  91.548  111.603 1.00 35.04  ? 176 THR A C   1 
ATOM   1303 O O   . THR A 1 176 ? 94.263  92.295  112.583 1.00 35.17  ? 176 THR A O   1 
ATOM   1304 C CB  . THR A 1 176 ? 94.932  92.793  109.568 1.00 34.45  ? 176 THR A CB  1 
ATOM   1305 O OG1 . THR A 1 176 ? 95.088  94.013  110.300 1.00 35.19  ? 176 THR A OG1 1 
ATOM   1306 C CG2 . THR A 1 176 ? 93.528  92.750  109.017 1.00 34.45  ? 176 THR A CG2 1 
ATOM   1307 N N   . LEU A 1 177 ? 93.170  90.673  111.467 1.00 36.49  ? 177 LEU A N   1 
ATOM   1308 C CA  . LEU A 1 177 ? 92.205  90.461  112.535 1.00 37.67  ? 177 LEU A CA  1 
ATOM   1309 C C   . LEU A 1 177 ? 92.834  89.701  113.690 1.00 38.26  ? 177 LEU A C   1 
ATOM   1310 O O   . LEU A 1 177 ? 92.613  90.042  114.858 1.00 38.18  ? 177 LEU A O   1 
ATOM   1311 C CB  . LEU A 1 177 ? 90.986  89.716  111.977 1.00 38.29  ? 177 LEU A CB  1 
ATOM   1312 C CG  . LEU A 1 177 ? 89.796  89.278  112.834 1.00 38.64  ? 177 LEU A CG  1 
ATOM   1313 C CD1 . LEU A 1 177 ? 88.551  89.269  111.975 1.00 39.01  ? 177 LEU A CD1 1 
ATOM   1314 C CD2 . LEU A 1 177 ? 90.001  87.891  113.421 1.00 38.53  ? 177 LEU A CD2 1 
ATOM   1315 N N   . VAL A 1 178 ? 93.614  88.660  113.386 1.00 38.58  ? 178 VAL A N   1 
ATOM   1316 C CA  . VAL A 1 178 ? 94.159  87.841  114.462 1.00 38.11  ? 178 VAL A CA  1 
ATOM   1317 C C   . VAL A 1 178 ? 95.259  88.585  115.219 1.00 38.38  ? 178 VAL A C   1 
ATOM   1318 O O   . VAL A 1 178 ? 95.334  88.496  116.450 1.00 38.47  ? 178 VAL A O   1 
ATOM   1319 C CB  . VAL A 1 178 ? 94.617  86.463  113.934 1.00 37.65  ? 178 VAL A CB  1 
ATOM   1320 C CG1 . VAL A 1 178 ? 95.844  86.548  113.042 1.00 37.34  ? 178 VAL A CG1 1 
ATOM   1321 C CG2 . VAL A 1 178 ? 94.868  85.513  115.093 1.00 37.47  ? 178 VAL A CG2 1 
ATOM   1322 N N   . GLY A 1 179 ? 96.128  89.330  114.524 1.00 38.81  ? 179 GLY A N   1 
ATOM   1323 C CA  . GLY A 1 179 ? 97.206  89.934  115.293 1.00 38.80  ? 179 GLY A CA  1 
ATOM   1324 C C   . GLY A 1 179 ? 97.094  91.372  115.765 1.00 38.72  ? 179 GLY A C   1 
ATOM   1325 O O   . GLY A 1 179 ? 97.070  91.628  116.972 1.00 37.51  ? 179 GLY A O   1 
ATOM   1326 N N   . GLY A 1 180 ? 97.035  92.318  114.831 1.00 39.98  ? 180 GLY A N   1 
ATOM   1327 C CA  . GLY A 1 180 ? 96.861  93.725  115.149 1.00 41.49  ? 180 GLY A CA  1 
ATOM   1328 C C   . GLY A 1 180 ? 98.172  94.466  115.349 1.00 43.19  ? 180 GLY A C   1 
ATOM   1329 O O   . GLY A 1 180 ? 98.757  94.413  116.435 1.00 44.55  ? 180 GLY A O   1 
ATOM   1330 N N   . LEU A 1 181 ? 98.645  95.153  114.306 1.00 44.37  ? 181 LEU A N   1 
ATOM   1331 C CA  . LEU A 1 181 ? 99.842  96.003  114.282 1.00 44.97  ? 181 LEU A CA  1 
ATOM   1332 C C   . LEU A 1 181 ? 101.136 95.264  114.640 1.00 45.70  ? 181 LEU A C   1 
ATOM   1333 O O   . LEU A 1 181 ? 102.228 95.840  114.586 1.00 48.30  ? 181 LEU A O   1 
ATOM   1334 C CB  . LEU A 1 181 ? 99.663  97.238  115.167 1.00 44.75  ? 181 LEU A CB  1 
ATOM   1335 C CG  . LEU A 1 181 ? 100.520 98.395  114.628 1.00 44.09  ? 181 LEU A CG  1 
ATOM   1336 C CD1 . LEU A 1 181 ? 100.050 98.806  113.244 1.00 43.41  ? 181 LEU A CD1 1 
ATOM   1337 C CD2 . LEU A 1 181 ? 100.542 99.581  115.549 1.00 43.97  ? 181 LEU A CD2 1 
ATOM   1338 N N   . TYR A 1 182 ? 101.045 93.983  114.970 1.00 43.91  ? 182 TYR A N   1 
ATOM   1339 C CA  . TYR A 1 182 ? 102.207 93.114  115.005 1.00 43.27  ? 182 TYR A CA  1 
ATOM   1340 C C   . TYR A 1 182 ? 102.145 92.047  113.934 1.00 42.11  ? 182 TYR A C   1 
ATOM   1341 O O   . TYR A 1 182 ? 103.187 91.613  113.443 1.00 44.95  ? 182 TYR A O   1 
ATOM   1342 C CB  . TYR A 1 182 ? 102.344 92.444  116.375 1.00 44.19  ? 182 TYR A CB  1 
ATOM   1343 C CG  . TYR A 1 182 ? 103.127 93.262  117.370 1.00 45.40  ? 182 TYR A CG  1 
ATOM   1344 C CD1 . TYR A 1 182 ? 104.414 93.693  117.084 1.00 46.33  ? 182 TYR A CD1 1 
ATOM   1345 C CD2 . TYR A 1 182 ? 102.585 93.589  118.603 1.00 46.66  ? 182 TYR A CD2 1 
ATOM   1346 C CE1 . TYR A 1 182 ? 105.135 94.439  117.994 1.00 47.76  ? 182 TYR A CE1 1 
ATOM   1347 C CE2 . TYR A 1 182 ? 103.298 94.329  119.519 1.00 48.03  ? 182 TYR A CE2 1 
ATOM   1348 C CZ  . TYR A 1 182 ? 104.572 94.754  119.211 1.00 48.79  ? 182 TYR A CZ  1 
ATOM   1349 O OH  . TYR A 1 182 ? 105.285 95.494  120.124 1.00 51.19  ? 182 TYR A OH  1 
ATOM   1350 N N   . SER A 1 183 ? 100.938 91.628  113.568 1.00 39.45  ? 183 SER A N   1 
ATOM   1351 C CA  . SER A 1 183 ? 100.724 90.795  112.400 1.00 38.29  ? 183 SER A CA  1 
ATOM   1352 C C   . SER A 1 183 ? 100.816 91.574  111.100 1.00 37.66  ? 183 SER A C   1 
ATOM   1353 O O   . SER A 1 183 ? 100.878 90.950  110.039 1.00 37.59  ? 183 SER A O   1 
ATOM   1354 C CB  . SER A 1 183 ? 99.358  90.119  112.485 1.00 37.97  ? 183 SER A CB  1 
ATOM   1355 O OG  . SER A 1 183 ? 99.250  89.050  111.567 1.00 38.06  ? 183 SER A OG  1 
ATOM   1356 N N   . VAL A 1 184 ? 100.811 92.906  111.147 1.00 37.54  ? 184 VAL A N   1 
ATOM   1357 C CA  . VAL A 1 184 ? 100.929 93.712  109.937 1.00 38.11  ? 184 VAL A CA  1 
ATOM   1358 C C   . VAL A 1 184 ? 102.275 94.405  109.835 1.00 37.98  ? 184 VAL A C   1 
ATOM   1359 O O   . VAL A 1 184 ? 102.602 94.928  108.758 1.00 37.43  ? 184 VAL A O   1 
ATOM   1360 C CB  . VAL A 1 184 ? 99.805  94.764  109.836 1.00 38.92  ? 184 VAL A CB  1 
ATOM   1361 C CG1 . VAL A 1 184 ? 98.447  94.125  110.070 1.00 39.43  ? 184 VAL A CG1 1 
ATOM   1362 C CG2 . VAL A 1 184 ? 100.065 95.943  110.738 1.00 39.00  ? 184 VAL A CG2 1 
ATOM   1363 N N   . ALA A 1 185 ? 103.059 94.444  110.913 1.00 38.12  ? 185 ALA A N   1 
ATOM   1364 C CA  . ALA A 1 185 ? 104.375 95.060  110.895 1.00 37.97  ? 185 ALA A CA  1 
ATOM   1365 C C   . ALA A 1 185 ? 105.509 94.048  110.892 1.00 37.66  ? 185 ALA A C   1 
ATOM   1366 O O   . ALA A 1 185 ? 106.637 94.413  110.546 1.00 38.38  ? 185 ALA A O   1 
ATOM   1367 C CB  . ALA A 1 185 ? 104.542 96.003  112.094 1.00 37.94  ? 185 ALA A CB  1 
ATOM   1368 N N   . TYR A 1 186 ? 105.247 92.798  111.267 1.00 36.87  ? 186 TYR A N   1 
ATOM   1369 C CA  . TYR A 1 186 ? 106.221 91.730  111.110 1.00 36.11  ? 186 TYR A CA  1 
ATOM   1370 C C   . TYR A 1 186 ? 106.021 90.935  109.829 1.00 35.63  ? 186 TYR A C   1 
ATOM   1371 O O   . TYR A 1 186 ? 106.845 90.069  109.524 1.00 36.30  ? 186 TYR A O   1 
ATOM   1372 C CB  . TYR A 1 186 ? 106.185 90.778  112.312 1.00 36.11  ? 186 TYR A CB  1 
ATOM   1373 C CG  . TYR A 1 186 ? 106.769 91.358  113.583 1.00 36.45  ? 186 TYR A CG  1 
ATOM   1374 C CD1 . TYR A 1 186 ? 107.482 92.549  113.565 1.00 36.91  ? 186 TYR A CD1 1 
ATOM   1375 C CD2 . TYR A 1 186 ? 106.619 90.705  114.799 1.00 36.78  ? 186 TYR A CD2 1 
ATOM   1376 C CE1 . TYR A 1 186 ? 108.018 93.080  114.720 1.00 37.62  ? 186 TYR A CE1 1 
ATOM   1377 C CE2 . TYR A 1 186 ? 107.153 91.228  115.960 1.00 37.44  ? 186 TYR A CE2 1 
ATOM   1378 C CZ  . TYR A 1 186 ? 107.851 92.415  115.914 1.00 38.05  ? 186 TYR A CZ  1 
ATOM   1379 O OH  . TYR A 1 186 ? 108.385 92.942  117.066 1.00 39.49  ? 186 TYR A OH  1 
ATOM   1380 N N   . THR A 1 187 ? 104.949 91.198  109.081 1.00 35.77  ? 187 THR A N   1 
ATOM   1381 C CA  . THR A 1 187 ? 104.803 90.653  107.740 1.00 36.85  ? 187 THR A CA  1 
ATOM   1382 C C   . THR A 1 187 ? 105.129 91.675  106.662 1.00 37.41  ? 187 THR A C   1 
ATOM   1383 O O   . THR A 1 187 ? 105.297 91.293  105.500 1.00 36.93  ? 187 THR A O   1 
ATOM   1384 C CB  . THR A 1 187 ? 103.383 90.125  107.511 1.00 37.40  ? 187 THR A CB  1 
ATOM   1385 O OG1 . THR A 1 187 ? 103.364 89.334  106.319 1.00 37.43  ? 187 THR A OG1 1 
ATOM   1386 C CG2 . THR A 1 187 ? 102.423 91.274  107.313 1.00 37.79  ? 187 THR A CG2 1 
ATOM   1387 N N   . ASP A 1 188 ? 105.209 92.960  107.015 1.00 38.40  ? 188 ASP A N   1 
ATOM   1388 C CA  . ASP A 1 188 ? 105.630 93.968  106.053 1.00 38.80  ? 188 ASP A CA  1 
ATOM   1389 C C   . ASP A 1 188 ? 107.135 93.941  105.835 1.00 38.98  ? 188 ASP A C   1 
ATOM   1390 O O   . ASP A 1 188 ? 107.603 94.317  104.758 1.00 39.82  ? 188 ASP A O   1 
ATOM   1391 C CB  . ASP A 1 188 ? 105.184 95.355  106.509 1.00 38.80  ? 188 ASP A CB  1 
ATOM   1392 C CG  . ASP A 1 188 ? 103.786 95.698  106.045 1.00 38.72  ? 188 ASP A CG  1 
ATOM   1393 O OD1 . ASP A 1 188 ? 103.087 94.794  105.545 1.00 38.28  ? 188 ASP A OD1 1 
ATOM   1394 O OD2 . ASP A 1 188 ? 103.384 96.871  106.185 1.00 39.12  ? 188 ASP A OD2 1 
ATOM   1395 N N   . VAL A 1 189 ? 107.904 93.495  106.832 1.00 38.46  ? 189 VAL A N   1 
ATOM   1396 C CA  . VAL A 1 189 ? 109.333 93.295  106.625 1.00 38.09  ? 189 VAL A CA  1 
ATOM   1397 C C   . VAL A 1 189 ? 109.597 92.096  105.725 1.00 38.42  ? 189 VAL A C   1 
ATOM   1398 O O   . VAL A 1 189 ? 110.700 91.963  105.183 1.00 40.10  ? 189 VAL A O   1 
ATOM   1399 C CB  . VAL A 1 189 ? 110.063 93.143  107.972 1.00 37.65  ? 189 VAL A CB  1 
ATOM   1400 C CG1 . VAL A 1 189 ? 109.781 94.340  108.862 1.00 37.79  ? 189 VAL A CG1 1 
ATOM   1401 C CG2 . VAL A 1 189 ? 109.656 91.854  108.662 1.00 37.14  ? 189 VAL A CG2 1 
ATOM   1402 N N   . VAL A 1 190 ? 108.616 91.212  105.560 1.00 38.12  ? 190 VAL A N   1 
ATOM   1403 C CA  . VAL A 1 190 ? 108.705 90.128  104.588 1.00 38.17  ? 190 VAL A CA  1 
ATOM   1404 C C   . VAL A 1 190 ? 108.151 90.560  103.237 1.00 38.64  ? 190 VAL A C   1 
ATOM   1405 O O   . VAL A 1 190 ? 108.752 90.287  102.192 1.00 38.57  ? 190 VAL A O   1 
ATOM   1406 C CB  . VAL A 1 190 ? 107.970 88.885  105.131 1.00 37.83  ? 190 VAL A CB  1 
ATOM   1407 C CG1 . VAL A 1 190 ? 107.787 87.845  104.040 1.00 37.65  ? 190 VAL A CG1 1 
ATOM   1408 C CG2 . VAL A 1 190 ? 108.720 88.300  106.313 1.00 37.91  ? 190 VAL A CG2 1 
ATOM   1409 N N   . GLN A 1 191 ? 107.011 91.257  103.247 1.00 39.99  ? 191 GLN A N   1 
ATOM   1410 C CA  . GLN A 1 191 ? 106.384 91.684  102.001 1.00 41.42  ? 191 GLN A CA  1 
ATOM   1411 C C   . GLN A 1 191 ? 107.234 92.711  101.267 1.00 42.33  ? 191 GLN A C   1 
ATOM   1412 O O   . GLN A 1 191 ? 107.283 92.705  100.035 1.00 42.85  ? 191 GLN A O   1 
ATOM   1413 C CB  . GLN A 1 191 ? 104.989 92.244  102.273 1.00 41.72  ? 191 GLN A CB  1 
ATOM   1414 C CG  . GLN A 1 191 ? 103.895 91.197  102.257 1.00 42.26  ? 191 GLN A CG  1 
ATOM   1415 C CD  . GLN A 1 191 ? 102.683 91.614  103.057 1.00 42.63  ? 191 GLN A CD  1 
ATOM   1416 O OE1 . GLN A 1 191 ? 102.569 92.763  103.477 1.00 42.32  ? 191 GLN A OE1 1 
ATOM   1417 N NE2 . GLN A 1 191 ? 101.767 90.679  103.272 1.00 43.25  ? 191 GLN A NE2 1 
ATOM   1418 N N   . LEU A 1 192 ? 107.907 93.604  101.997 1.00 42.71  ? 192 LEU A N   1 
ATOM   1419 C CA  . LEU A 1 192 ? 108.756 94.599  101.349 1.00 42.25  ? 192 LEU A CA  1 
ATOM   1420 C C   . LEU A 1 192 ? 109.957 93.945  100.677 1.00 42.73  ? 192 LEU A C   1 
ATOM   1421 O O   . LEU A 1 192 ? 110.335 94.322  99.560  1.00 43.41  ? 192 LEU A O   1 
ATOM   1422 C CB  . LEU A 1 192 ? 109.219 95.639  102.367 1.00 41.71  ? 192 LEU A CB  1 
ATOM   1423 C CG  . LEU A 1 192 ? 110.101 96.750  101.802 1.00 41.27  ? 192 LEU A CG  1 
ATOM   1424 C CD1 . LEU A 1 192 ? 109.291 97.617  100.860 1.00 40.60  ? 192 LEU A CD1 1 
ATOM   1425 C CD2 . LEU A 1 192 ? 110.710 97.585  102.905 1.00 41.58  ? 192 LEU A CD2 1 
ATOM   1426 N N   . PHE A 1 193 ? 110.566 92.962  101.344 1.00 43.22  ? 193 PHE A N   1 
ATOM   1427 C CA  . PHE A 1 193 ? 111.659 92.210  100.736 1.00 44.66  ? 193 PHE A CA  1 
ATOM   1428 C C   . PHE A 1 193 ? 111.176 91.443  99.511  1.00 45.10  ? 193 PHE A C   1 
ATOM   1429 O O   . PHE A 1 193 ? 111.888 91.356  98.502  1.00 46.42  ? 193 PHE A O   1 
ATOM   1430 C CB  . PHE A 1 193 ? 112.274 91.269  101.773 1.00 45.51  ? 193 PHE A CB  1 
ATOM   1431 C CG  . PHE A 1 193 ? 113.097 90.159  101.185 1.00 47.07  ? 193 PHE A CG  1 
ATOM   1432 C CD1 . PHE A 1 193 ? 114.401 90.389  100.779 1.00 48.07  ? 193 PHE A CD1 1 
ATOM   1433 C CD2 . PHE A 1 193 ? 112.580 88.877  101.067 1.00 47.63  ? 193 PHE A CD2 1 
ATOM   1434 C CE1 . PHE A 1 193 ? 115.167 89.369  100.248 1.00 48.28  ? 193 PHE A CE1 1 
ATOM   1435 C CE2 . PHE A 1 193 ? 113.340 87.853  100.534 1.00 48.08  ? 193 PHE A CE2 1 
ATOM   1436 C CZ  . PHE A 1 193 ? 114.636 88.100  100.125 1.00 48.22  ? 193 PHE A CZ  1 
ATOM   1437 N N   . CYS A 1 194 ? 109.964 90.883  99.580  1.00 44.94  ? 194 CYS A N   1 
ATOM   1438 C CA  . CYS A 1 194 ? 109.397 90.201  98.421  1.00 44.96  ? 194 CYS A CA  1 
ATOM   1439 C C   . CYS A 1 194 ? 109.156 91.170  97.268  1.00 44.02  ? 194 CYS A C   1 
ATOM   1440 O O   . CYS A 1 194 ? 109.387 90.826  96.104  1.00 44.35  ? 194 CYS A O   1 
ATOM   1441 C CB  . CYS A 1 194 ? 108.099 89.497  98.810  1.00 45.88  ? 194 CYS A CB  1 
ATOM   1442 S SG  . CYS A 1 194 ? 107.570 88.238  97.631  1.00 48.35  ? 194 CYS A SG  1 
ATOM   1443 N N   . ILE A 1 195 ? 108.687 92.384  97.577  1.00 42.72  ? 195 ILE A N   1 
ATOM   1444 C CA  . ILE A 1 195 ? 108.505 93.415  96.556  1.00 41.62  ? 195 ILE A CA  1 
ATOM   1445 C C   . ILE A 1 195 ? 109.836 93.734  95.894  1.00 41.47  ? 195 ILE A C   1 
ATOM   1446 O O   . ILE A 1 195 ? 109.940 93.802  94.663  1.00 40.68  ? 195 ILE A O   1 
ATOM   1447 C CB  . ILE A 1 195 ? 107.886 94.683  97.174  1.00 41.07  ? 195 ILE A CB  1 
ATOM   1448 C CG1 . ILE A 1 195 ? 106.421 94.479  97.537  1.00 41.55  ? 195 ILE A CG1 1 
ATOM   1449 C CG2 . ILE A 1 195 ? 107.980 95.847  96.208  1.00 40.42  ? 195 ILE A CG2 1 
ATOM   1450 C CD1 . ILE A 1 195 ? 105.924 95.531  98.497  1.00 41.83  ? 195 ILE A CD1 1 
ATOM   1451 N N   . PHE A 1 196 ? 110.875 93.929  96.713  1.00 41.93  ? 196 PHE A N   1 
ATOM   1452 C CA  . PHE A 1 196 ? 112.203 94.249  96.198  1.00 42.22  ? 196 PHE A CA  1 
ATOM   1453 C C   . PHE A 1 196 ? 112.701 93.157  95.263  1.00 42.26  ? 196 PHE A C   1 
ATOM   1454 O O   . PHE A 1 196 ? 113.131 93.436  94.137  1.00 43.49  ? 196 PHE A O   1 
ATOM   1455 C CB  . PHE A 1 196 ? 113.173 94.434  97.366  1.00 42.73  ? 196 PHE A CB  1 
ATOM   1456 C CG  . PHE A 1 196 ? 114.570 94.797  96.954  1.00 43.99  ? 196 PHE A CG  1 
ATOM   1457 C CD1 . PHE A 1 196 ? 114.902 96.113  96.679  1.00 44.71  ? 196 PHE A CD1 1 
ATOM   1458 C CD2 . PHE A 1 196 ? 115.559 93.830  96.868  1.00 44.73  ? 196 PHE A CD2 1 
ATOM   1459 C CE1 . PHE A 1 196 ? 116.191 96.458  96.315  1.00 45.18  ? 196 PHE A CE1 1 
ATOM   1460 C CE2 . PHE A 1 196 ? 116.848 94.168  96.501  1.00 45.29  ? 196 PHE A CE2 1 
ATOM   1461 C CZ  . PHE A 1 196 ? 117.164 95.486  96.224  1.00 45.52  ? 196 PHE A CZ  1 
ATOM   1462 N N   . VAL A 1 197 ? 112.610 91.901  95.704  1.00 41.84  ? 197 VAL A N   1 
ATOM   1463 C CA  . VAL A 1 197 ? 113.106 90.779  94.910  1.00 41.89  ? 197 VAL A CA  1 
ATOM   1464 C C   . VAL A 1 197 ? 112.327 90.653  93.604  1.00 42.55  ? 197 VAL A C   1 
ATOM   1465 O O   . VAL A 1 197 ? 112.914 90.595  92.514  1.00 43.02  ? 197 VAL A O   1 
ATOM   1466 C CB  . VAL A 1 197 ? 113.046 89.485  95.738  1.00 41.58  ? 197 VAL A CB  1 
ATOM   1467 C CG1 . VAL A 1 197 ? 113.323 88.286  94.878  1.00 41.80  ? 197 VAL A CG1 1 
ATOM   1468 C CG2 . VAL A 1 197 ? 114.056 89.550  96.863  1.00 41.26  ? 197 VAL A CG2 1 
ATOM   1469 N N   . GLY A 1 198 ? 110.994 90.645  93.692  1.00 43.02  ? 198 GLY A N   1 
ATOM   1470 C CA  . GLY A 1 198 ? 110.182 90.426  92.507  1.00 43.50  ? 198 GLY A CA  1 
ATOM   1471 C C   . GLY A 1 198 ? 110.283 91.551  91.495  1.00 43.91  ? 198 GLY A C   1 
ATOM   1472 O O   . GLY A 1 198 ? 110.277 91.308  90.286  1.00 43.73  ? 198 GLY A O   1 
ATOM   1473 N N   . LEU A 1 199 ? 110.372 92.795  91.967  1.00 44.71  ? 199 LEU A N   1 
ATOM   1474 C CA  . LEU A 1 199 ? 110.484 93.912  91.040  1.00 45.31  ? 199 LEU A CA  1 
ATOM   1475 C C   . LEU A 1 199 ? 111.882 94.016  90.443  1.00 45.51  ? 199 LEU A C   1 
ATOM   1476 O O   . LEU A 1 199 ? 112.024 94.303  89.250  1.00 45.17  ? 199 LEU A O   1 
ATOM   1477 C CB  . LEU A 1 199 ? 110.100 95.216  91.737  1.00 45.59  ? 199 LEU A CB  1 
ATOM   1478 C CG  . LEU A 1 199 ? 108.603 95.520  91.801  1.00 45.50  ? 199 LEU A CG  1 
ATOM   1479 C CD1 . LEU A 1 199 ? 108.363 96.916  92.349  1.00 45.92  ? 199 LEU A CD1 1 
ATOM   1480 C CD2 . LEU A 1 199 ? 107.961 95.360  90.435  1.00 44.96  ? 199 LEU A CD2 1 
ATOM   1481 N N   . TRP A 1 200 ? 112.930 93.787  91.241  1.00 45.67  ? 200 TRP A N   1 
ATOM   1482 C CA  . TRP A 1 200 ? 114.278 94.016  90.746  1.00 45.74  ? 200 TRP A CA  1 
ATOM   1483 C C   . TRP A 1 200 ? 114.837 92.853  89.939  1.00 46.85  ? 200 TRP A C   1 
ATOM   1484 O O   . TRP A 1 200 ? 115.758 93.069  89.147  1.00 47.74  ? 200 TRP A O   1 
ATOM   1485 C CB  . TRP A 1 200 ? 115.219 94.334  91.906  1.00 45.18  ? 200 TRP A CB  1 
ATOM   1486 C CG  . TRP A 1 200 ? 115.399 95.803  92.138  1.00 44.74  ? 200 TRP A CG  1 
ATOM   1487 C CD1 . TRP A 1 200 ? 114.909 96.534  93.179  1.00 44.69  ? 200 TRP A CD1 1 
ATOM   1488 C CD2 . TRP A 1 200 ? 116.111 96.723  91.302  1.00 44.86  ? 200 TRP A CD2 1 
ATOM   1489 N NE1 . TRP A 1 200 ? 115.282 97.850  93.051  1.00 44.85  ? 200 TRP A NE1 1 
ATOM   1490 C CE2 . TRP A 1 200 ? 116.018 97.992  91.905  1.00 45.10  ? 200 TRP A CE2 1 
ATOM   1491 C CE3 . TRP A 1 200 ? 116.821 96.596  90.104  1.00 44.85  ? 200 TRP A CE3 1 
ATOM   1492 C CZ2 . TRP A 1 200 ? 116.606 99.126  91.351  1.00 45.23  ? 200 TRP A CZ2 1 
ATOM   1493 C CZ3 . TRP A 1 200 ? 117.405 97.723  89.556  1.00 44.84  ? 200 TRP A CZ3 1 
ATOM   1494 C CH2 . TRP A 1 200 ? 117.294 98.971  90.179  1.00 44.97  ? 200 TRP A CH2 1 
ATOM   1495 N N   . ILE A 1 201 ? 114.336 91.627  90.121  1.00 48.09  ? 201 ILE A N   1 
ATOM   1496 C CA  . ILE A 1 201 ? 114.797 90.553  89.243  1.00 49.69  ? 201 ILE A CA  1 
ATOM   1497 C C   . ILE A 1 201 ? 114.184 90.686  87.852  1.00 50.78  ? 201 ILE A C   1 
ATOM   1498 O O   . ILE A 1 201 ? 114.840 90.389  86.846  1.00 52.51  ? 201 ILE A O   1 
ATOM   1499 C CB  . ILE A 1 201 ? 114.523 89.173  89.873  1.00 50.06  ? 201 ILE A CB  1 
ATOM   1500 C CG1 . ILE A 1 201 ? 115.392 88.978  91.111  1.00 50.30  ? 201 ILE A CG1 1 
ATOM   1501 C CG2 . ILE A 1 201 ? 114.814 88.047  88.905  1.00 50.16  ? 201 ILE A CG2 1 
ATOM   1502 C CD1 . ILE A 1 201 ? 115.112 87.694  91.836  1.00 50.65  ? 201 ILE A CD1 1 
ATOM   1503 N N   . SER A 1 202 ? 112.940 91.159  87.761  1.00 50.20  ? 202 SER A N   1 
ATOM   1504 C CA  . SER A 1 202 ? 112.250 91.183  86.476  1.00 49.70  ? 202 SER A CA  1 
ATOM   1505 C C   . SER A 1 202 ? 112.799 92.228  85.511  1.00 48.90  ? 202 SER A C   1 
ATOM   1506 O O   . SER A 1 202 ? 112.638 92.065  84.296  1.00 48.87  ? 202 SER A O   1 
ATOM   1507 C CB  . SER A 1 202 ? 110.757 91.426  86.683  1.00 49.83  ? 202 SER A CB  1 
ATOM   1508 O OG  . SER A 1 202 ? 110.092 91.471  85.435  1.00 50.67  ? 202 SER A OG  1 
ATOM   1509 N N   . VAL A 1 203 ? 113.417 93.295  86.009  1.00 47.84  ? 203 VAL A N   1 
ATOM   1510 C CA  . VAL A 1 203 ? 113.900 94.382  85.155  1.00 47.09  ? 203 VAL A CA  1 
ATOM   1511 C C   . VAL A 1 203 ? 115.018 93.922  84.213  1.00 46.30  ? 203 VAL A C   1 
ATOM   1512 O O   . VAL A 1 203 ? 114.944 94.240  83.015  1.00 48.22  ? 203 VAL A O   1 
ATOM   1513 C CB  . VAL A 1 203 ? 114.318 95.601  86.000  1.00 47.28  ? 203 VAL A CB  1 
ATOM   1514 C CG1 . VAL A 1 203 ? 115.029 96.636  85.147  1.00 46.82  ? 203 VAL A CG1 1 
ATOM   1515 C CG2 . VAL A 1 203 ? 113.103 96.212  86.674  1.00 47.95  ? 203 VAL A CG2 1 
ATOM   1516 N N   . PRO A 1 204 ? 116.063 93.198  84.658  1.00 44.17  ? 204 PRO A N   1 
ATOM   1517 C CA  . PRO A 1 204 ? 117.034 92.683  83.674  1.00 43.63  ? 204 PRO A CA  1 
ATOM   1518 C C   . PRO A 1 204 ? 116.441 91.722  82.658  1.00 43.48  ? 204 PRO A C   1 
ATOM   1519 O O   . PRO A 1 204 ? 116.885 91.712  81.503  1.00 43.47  ? 204 PRO A O   1 
ATOM   1520 C CB  . PRO A 1 204 ? 118.086 91.989  84.549  1.00 43.54  ? 204 PRO A CB  1 
ATOM   1521 C CG  . PRO A 1 204 ? 118.011 92.686  85.830  1.00 43.78  ? 204 PRO A CG  1 
ATOM   1522 C CD  . PRO A 1 204 ? 116.559 92.966  86.029  1.00 43.74  ? 204 PRO A CD  1 
ATOM   1523 N N   . PHE A 1 205 ? 115.461 90.906  83.051  1.00 43.53  ? 205 PHE A N   1 
ATOM   1524 C CA  . PHE A 1 205 ? 114.830 90.004  82.092  1.00 44.08  ? 205 PHE A CA  1 
ATOM   1525 C C   . PHE A 1 205 ? 113.985 90.771  81.083  1.00 44.05  ? 205 PHE A C   1 
ATOM   1526 O O   . PHE A 1 205 ? 113.927 90.400  79.906  1.00 44.12  ? 205 PHE A O   1 
ATOM   1527 C CB  . PHE A 1 205 ? 113.988 88.962  82.825  1.00 44.77  ? 205 PHE A CB  1 
ATOM   1528 C CG  . PHE A 1 205 ? 114.798 87.868  83.454  1.00 45.46  ? 205 PHE A CG  1 
ATOM   1529 C CD1 . PHE A 1 205 ? 115.174 86.759  82.717  1.00 45.85  ? 205 PHE A CD1 1 
ATOM   1530 C CD2 . PHE A 1 205 ? 115.195 87.954  84.777  1.00 45.87  ? 205 PHE A CD2 1 
ATOM   1531 C CE1 . PHE A 1 205 ? 115.923 85.751  83.290  1.00 46.43  ? 205 PHE A CE1 1 
ATOM   1532 C CE2 . PHE A 1 205 ? 115.947 86.951  85.354  1.00 46.54  ? 205 PHE A CE2 1 
ATOM   1533 C CZ  . PHE A 1 205 ? 116.310 85.848  84.611  1.00 46.85  ? 205 PHE A CZ  1 
ATOM   1534 N N   . ALA A 1 206 ? 113.314 91.836  81.529  1.00 43.90  ? 206 ALA A N   1 
ATOM   1535 C CA  . ALA A 1 206 ? 112.544 92.665  80.607  1.00 43.56  ? 206 ALA A CA  1 
ATOM   1536 C C   . ALA A 1 206 ? 113.456 93.418  79.646  1.00 43.33  ? 206 ALA A C   1 
ATOM   1537 O O   . ALA A 1 206 ? 113.133 93.562  78.461  1.00 43.39  ? 206 ALA A O   1 
ATOM   1538 C CB  . ALA A 1 206 ? 111.662 93.638  81.387  1.00 43.37  ? 206 ALA A CB  1 
ATOM   1539 N N   . LEU A 1 207 ? 114.599 93.904  80.137  1.00 43.01  ? 207 LEU A N   1 
ATOM   1540 C CA  . LEU A 1 207 ? 115.504 94.672  79.287  1.00 43.09  ? 207 LEU A CA  1 
ATOM   1541 C C   . LEU A 1 207 ? 116.203 93.795  78.254  1.00 44.54  ? 207 LEU A C   1 
ATOM   1542 O O   . LEU A 1 207 ? 116.604 94.290  77.195  1.00 44.81  ? 207 LEU A O   1 
ATOM   1543 C CB  . LEU A 1 207 ? 116.539 95.401  80.143  1.00 42.33  ? 207 LEU A CB  1 
ATOM   1544 C CG  . LEU A 1 207 ? 116.078 96.690  80.823  1.00 41.60  ? 207 LEU A CG  1 
ATOM   1545 C CD1 . LEU A 1 207 ? 117.051 97.105  81.911  1.00 41.49  ? 207 LEU A CD1 1 
ATOM   1546 C CD2 . LEU A 1 207 ? 115.923 97.796  79.798  1.00 41.31  ? 207 LEU A CD2 1 
ATOM   1547 N N   . SER A 1 208 ? 116.361 92.503  78.538  1.00 46.73  ? 208 SER A N   1 
ATOM   1548 C CA  . SER A 1 208 ? 117.071 91.611  77.630  1.00 49.13  ? 208 SER A CA  1 
ATOM   1549 C C   . SER A 1 208 ? 116.213 91.123  76.470  1.00 49.86  ? 208 SER A C   1 
ATOM   1550 O O   . SER A 1 208 ? 116.738 90.440  75.585  1.00 50.17  ? 208 SER A O   1 
ATOM   1551 C CB  . SER A 1 208 ? 117.619 90.406  78.399  1.00 50.85  ? 208 SER A CB  1 
ATOM   1552 O OG  . SER A 1 208 ? 116.568 89.579  78.867  1.00 52.76  ? 208 SER A OG  1 
ATOM   1553 N N   . HIS A 1 209 ? 114.921 91.438  76.460  1.00 50.74  ? 209 HIS A N   1 
ATOM   1554 C CA  . HIS A 1 209 ? 114.053 90.996  75.378  1.00 51.32  ? 209 HIS A CA  1 
ATOM   1555 C C   . HIS A 1 209 ? 114.443 91.692  74.075  1.00 51.95  ? 209 HIS A C   1 
ATOM   1556 O O   . HIS A 1 209 ? 114.754 92.887  74.079  1.00 53.21  ? 209 HIS A O   1 
ATOM   1557 C CB  . HIS A 1 209 ? 112.591 91.288  75.716  1.00 51.49  ? 209 HIS A CB  1 
ATOM   1558 C CG  . HIS A 1 209 ? 111.613 90.447  74.956  1.00 52.67  ? 209 HIS A CG  1 
ATOM   1559 N ND1 . HIS A 1 209 ? 111.211 90.747  73.672  1.00 54.17  ? 209 HIS A ND1 1 
ATOM   1560 C CD2 . HIS A 1 209 ? 110.957 89.313  75.299  1.00 53.69  ? 209 HIS A CD2 1 
ATOM   1561 C CE1 . HIS A 1 209 ? 110.350 89.835  73.258  1.00 54.98  ? 209 HIS A CE1 1 
ATOM   1562 N NE2 . HIS A 1 209 ? 110.178 88.954  74.226  1.00 54.80  ? 209 HIS A NE2 1 
ATOM   1563 N N   . PRO A 1 210 ? 114.456 90.970  72.950  1.00 52.41  ? 210 PRO A N   1 
ATOM   1564 C CA  . PRO A 1 210 ? 114.845 91.599  71.676  1.00 53.10  ? 210 PRO A CA  1 
ATOM   1565 C C   . PRO A 1 210 ? 113.893 92.684  71.200  1.00 54.39  ? 210 PRO A C   1 
ATOM   1566 O O   . PRO A 1 210 ? 114.300 93.523  70.386  1.00 54.07  ? 210 PRO A O   1 
ATOM   1567 C CB  . PRO A 1 210 ? 114.877 90.416  70.698  1.00 52.55  ? 210 PRO A CB  1 
ATOM   1568 C CG  . PRO A 1 210 ? 113.987 89.390  71.316  1.00 52.32  ? 210 PRO A CG  1 
ATOM   1569 C CD  . PRO A 1 210 ? 114.194 89.530  72.794  1.00 52.12  ? 210 PRO A CD  1 
ATOM   1570 N N   . ALA A 1 211 ? 112.641 92.692  71.664  1.00 56.02  ? 211 ALA A N   1 
ATOM   1571 C CA  . ALA A 1 211 ? 111.715 93.751  71.272  1.00 56.57  ? 211 ALA A CA  1 
ATOM   1572 C C   . ALA A 1 211 ? 112.127 95.095  71.859  1.00 56.62  ? 211 ALA A C   1 
ATOM   1573 O O   . ALA A 1 211 ? 112.054 96.124  71.178  1.00 56.45  ? 211 ALA A O   1 
ATOM   1574 C CB  . ALA A 1 211 ? 110.294 93.392  71.698  1.00 56.95  ? 211 ALA A CB  1 
ATOM   1575 N N   . VAL A 1 212 ? 112.560 95.106  73.114  1.00 56.52  ? 212 VAL A N   1 
ATOM   1576 C CA  . VAL A 1 212 ? 112.979 96.339  73.772  1.00 57.27  ? 212 VAL A CA  1 
ATOM   1577 C C   . VAL A 1 212 ? 114.357 96.728  73.257  1.00 59.69  ? 212 VAL A C   1 
ATOM   1578 O O   . VAL A 1 212 ? 115.294 95.922  73.285  1.00 62.41  ? 212 VAL A O   1 
ATOM   1579 C CB  . VAL A 1 212 ? 112.986 96.162  75.297  1.00 56.28  ? 212 VAL A CB  1 
ATOM   1580 C CG1 . VAL A 1 212 ? 113.336 97.471  75.983  1.00 56.04  ? 212 VAL A CG1 1 
ATOM   1581 C CG2 . VAL A 1 212 ? 111.644 95.641  75.766  1.00 55.94  ? 212 VAL A CG2 1 
ATOM   1582 N N   . ALA A 1 213 ? 114.488 97.967  72.788  1.00 61.10  ? 213 ALA A N   1 
ATOM   1583 C CA  . ALA A 1 213 ? 115.735 98.430  72.189  1.00 62.60  ? 213 ALA A CA  1 
ATOM   1584 C C   . ALA A 1 213 ? 116.019 99.856  72.631  1.00 64.20  ? 213 ALA A C   1 
ATOM   1585 O O   . ALA A 1 213 ? 115.186 100.744 72.424  1.00 64.58  ? 213 ALA A O   1 
ATOM   1586 C CB  . ALA A 1 213 ? 115.673 98.348  70.661  1.00 62.19  ? 213 ALA A CB  1 
ATOM   1587 N N   . ASP A 1 214 ? 117.195 100.061 73.232  1.00 65.49  ? 214 ASP A N   1 
ATOM   1588 C CA  . ASP A 1 214 ? 117.763 101.382 73.509  1.00 65.65  ? 214 ASP A CA  1 
ATOM   1589 C C   . ASP A 1 214 ? 116.835 102.219 74.397  1.00 63.88  ? 214 ASP A C   1 
ATOM   1590 O O   . ASP A 1 214 ? 116.254 103.222 73.976  1.00 67.27  ? 214 ASP A O   1 
ATOM   1591 C CB  . ASP A 1 214 ? 118.090 102.113 72.202  1.00 67.95  ? 214 ASP A CB  1 
ATOM   1592 C CG  . ASP A 1 214 ? 119.208 101.447 71.427  1.00 69.62  ? 214 ASP A CG  1 
ATOM   1593 O OD1 . ASP A 1 214 ? 120.124 100.888 72.067  1.00 71.82  ? 214 ASP A OD1 1 
ATOM   1594 O OD2 . ASP A 1 214 ? 119.173 101.483 70.179  1.00 70.51  ? 214 ASP A OD2 1 
ATOM   1595 N N   . ILE A 1 215 ? 116.697 101.758 75.643  1.00 59.74  ? 215 ILE A N   1 
ATOM   1596 C CA  . ILE A 1 215 ? 115.893 102.483 76.625  1.00 57.20  ? 215 ILE A CA  1 
ATOM   1597 C C   . ILE A 1 215 ? 116.469 103.872 76.892  1.00 57.73  ? 215 ILE A C   1 
ATOM   1598 O O   . ILE A 1 215 ? 115.723 104.815 77.181  1.00 59.77  ? 215 ILE A O   1 
ATOM   1599 C CB  . ILE A 1 215 ? 115.753 101.650 77.919  1.00 54.58  ? 215 ILE A CB  1 
ATOM   1600 C CG1 . ILE A 1 215 ? 114.725 102.275 78.863  1.00 52.85  ? 215 ILE A CG1 1 
ATOM   1601 C CG2 . ILE A 1 215 ? 117.093 101.453 78.614  1.00 54.65  ? 215 ILE A CG2 1 
ATOM   1602 C CD1 . ILE A 1 215 ? 114.313 101.363 79.987  1.00 52.63  ? 215 ILE A CD1 1 
ATOM   1603 N N   . GLY A 1 216 ? 117.791 104.027 76.796  1.00 56.69  ? 216 GLY A N   1 
ATOM   1604 C CA  . GLY A 1 216 ? 118.383 105.347 76.941  1.00 55.65  ? 216 GLY A CA  1 
ATOM   1605 C C   . GLY A 1 216 ? 118.069 106.267 75.775  1.00 54.25  ? 216 GLY A C   1 
ATOM   1606 O O   . GLY A 1 216 ? 117.854 107.468 75.961  1.00 53.49  ? 216 GLY A O   1 
ATOM   1607 N N   . PHE A 1 217 ? 118.044 105.718 74.558  1.00 53.69  ? 217 PHE A N   1 
ATOM   1608 C CA  . PHE A 1 217 ? 117.834 106.534 73.367  1.00 53.51  ? 217 PHE A CA  1 
ATOM   1609 C C   . PHE A 1 217 ? 116.397 107.032 73.265  1.00 53.26  ? 217 PHE A C   1 
ATOM   1610 O O   . PHE A 1 217 ? 116.158 108.122 72.734  1.00 53.83  ? 217 PHE A O   1 
ATOM   1611 C CB  . PHE A 1 217 ? 118.223 105.732 72.123  1.00 53.85  ? 217 PHE A CB  1 
ATOM   1612 C CG  . PHE A 1 217 ? 117.756 106.333 70.828  1.00 53.66  ? 217 PHE A CG  1 
ATOM   1613 C CD1 . PHE A 1 217 ? 118.422 107.411 70.270  1.00 53.78  ? 217 PHE A CD1 1 
ATOM   1614 C CD2 . PHE A 1 217 ? 116.669 105.800 70.153  1.00 53.57  ? 217 PHE A CD2 1 
ATOM   1615 C CE1 . PHE A 1 217 ? 118.001 107.958 69.073  1.00 54.00  ? 217 PHE A CE1 1 
ATOM   1616 C CE2 . PHE A 1 217 ? 116.243 106.344 68.957  1.00 53.98  ? 217 PHE A CE2 1 
ATOM   1617 C CZ  . PHE A 1 217 ? 116.911 107.423 68.416  1.00 54.12  ? 217 PHE A CZ  1 
ATOM   1618 N N   . THR A 1 218 ? 115.433 106.259 73.767  1.00 53.42  ? 218 THR A N   1 
ATOM   1619 C CA  . THR A 1 218 ? 114.036 106.676 73.719  1.00 54.11  ? 218 THR A CA  1 
ATOM   1620 C C   . THR A 1 218 ? 113.746 107.812 74.698  1.00 55.24  ? 218 THR A C   1 
ATOM   1621 O O   . THR A 1 218 ? 112.735 108.507 74.546  1.00 56.86  ? 218 THR A O   1 
ATOM   1622 C CB  . THR A 1 218 ? 113.136 105.467 73.996  1.00 53.46  ? 218 THR A CB  1 
ATOM   1623 O OG1 . THR A 1 218 ? 113.603 104.349 73.233  1.00 52.42  ? 218 THR A OG1 1 
ATOM   1624 C CG2 . THR A 1 218 ? 111.695 105.737 73.582  1.00 53.44  ? 218 THR A CG2 1 
ATOM   1625 N N   . ALA A 1 219 ? 114.620 108.029 75.683  1.00 55.76  ? 219 ALA A N   1 
ATOM   1626 C CA  . ALA A 1 219 ? 114.411 109.112 76.641  1.00 56.07  ? 219 ALA A CA  1 
ATOM   1627 C C   . ALA A 1 219 ? 114.505 110.480 75.975  1.00 56.05  ? 219 ALA A C   1 
ATOM   1628 O O   . ALA A 1 219 ? 113.743 111.392 76.312  1.00 56.08  ? 219 ALA A O   1 
ATOM   1629 C CB  . ALA A 1 219 ? 115.419 109.002 77.783  1.00 56.28  ? 219 ALA A CB  1 
ATOM   1630 N N   . VAL A 1 220 ? 115.430 110.647 75.032  1.00 56.10  ? 220 VAL A N   1 
ATOM   1631 C CA  . VAL A 1 220 ? 115.650 111.939 74.389  1.00 56.41  ? 220 VAL A CA  1 
ATOM   1632 C C   . VAL A 1 220 ? 115.191 111.972 72.940  1.00 57.09  ? 220 VAL A C   1 
ATOM   1633 O O   . VAL A 1 220 ? 115.195 113.056 72.334  1.00 56.25  ? 220 VAL A O   1 
ATOM   1634 C CB  . VAL A 1 220 ? 117.129 112.370 74.481  1.00 56.62  ? 220 VAL A CB  1 
ATOM   1635 C CG1 . VAL A 1 220 ? 117.502 112.666 75.923  1.00 56.66  ? 220 VAL A CG1 1 
ATOM   1636 C CG2 . VAL A 1 220 ? 118.031 111.292 73.908  1.00 56.68  ? 220 VAL A CG2 1 
ATOM   1637 N N   . HIS A 1 221 ? 114.800 110.839 72.362  1.00 60.09  ? 221 HIS A N   1 
ATOM   1638 C CA  . HIS A 1 221 ? 114.343 110.789 70.982  1.00 63.27  ? 221 HIS A CA  1 
ATOM   1639 C C   . HIS A 1 221 ? 113.096 109.922 70.884  1.00 65.96  ? 221 HIS A C   1 
ATOM   1640 O O   . HIS A 1 221 ? 112.825 109.084 71.746  1.00 69.41  ? 221 HIS A O   1 
ATOM   1641 C CB  . HIS A 1 221 ? 115.432 110.252 70.046  1.00 63.71  ? 221 HIS A CB  1 
ATOM   1642 C CG  . HIS A 1 221 ? 116.569 111.202 69.835  1.00 64.12  ? 221 HIS A CG  1 
ATOM   1643 N ND1 . HIS A 1 221 ? 117.745 111.126 70.549  1.00 64.11  ? 221 HIS A ND1 1 
ATOM   1644 C CD2 . HIS A 1 221 ? 116.709 112.252 68.991  1.00 64.45  ? 221 HIS A CD2 1 
ATOM   1645 C CE1 . HIS A 1 221 ? 118.561 112.086 70.154  1.00 64.32  ? 221 HIS A CE1 1 
ATOM   1646 N NE2 . HIS A 1 221 ? 117.956 112.784 69.210  1.00 64.90  ? 221 HIS A NE2 1 
ATOM   1647 N N   . ALA A 1 222 ? 112.333 110.136 69.816  1.00 67.56  ? 222 ALA A N   1 
ATOM   1648 C CA  . ALA A 1 222 ? 111.066 109.451 69.599  1.00 68.67  ? 222 ALA A CA  1 
ATOM   1649 C C   . ALA A 1 222 ? 111.182 108.547 68.379  1.00 70.00  ? 222 ALA A C   1 
ATOM   1650 O O   . ALA A 1 222 ? 111.531 109.013 67.289  1.00 71.21  ? 222 ALA A O   1 
ATOM   1651 C CB  . ALA A 1 222 ? 109.933 110.459 69.412  1.00 68.83  ? 222 ALA A CB  1 
ATOM   1652 N N   . LYS A 1 223 ? 110.891 107.259 68.562  1.00 71.14  ? 223 LYS A N   1 
ATOM   1653 C CA  . LYS A 1 223 ? 110.842 106.315 67.452  1.00 72.73  ? 223 LYS A CA  1 
ATOM   1654 C C   . LYS A 1 223 ? 109.469 105.686 67.273  1.00 73.66  ? 223 LYS A C   1 
ATOM   1655 O O   . LYS A 1 223 ? 108.916 105.725 66.168  1.00 73.72  ? 223 LYS A O   1 
ATOM   1656 C CB  . LYS A 1 223 ? 111.911 105.223 67.630  1.00 73.00  ? 223 LYS A CB  1 
ATOM   1657 C CG  . LYS A 1 223 ? 112.067 104.695 69.048  1.00 73.42  ? 223 LYS A CG  1 
ATOM   1658 C CD  . LYS A 1 223 ? 113.359 103.906 69.201  1.00 73.95  ? 223 LYS A CD  1 
ATOM   1659 C CE  . LYS A 1 223 ? 113.525 102.887 68.084  1.00 73.28  ? 223 LYS A CE  1 
ATOM   1660 N NZ  . LYS A 1 223 ? 114.875 102.260 68.098  1.00 73.73  ? 223 LYS A NZ  1 
ATOM   1661 N N   . TYR A 1 224 ? 108.896 105.106 68.328  1.00 74.82  ? 224 TYR A N   1 
ATOM   1662 C CA  . TYR A 1 224 ? 107.570 104.500 68.267  1.00 75.06  ? 224 TYR A CA  1 
ATOM   1663 C C   . TYR A 1 224 ? 106.471 105.438 68.742  1.00 73.40  ? 224 TYR A C   1 
ATOM   1664 O O   . TYR A 1 224 ? 105.414 105.520 68.110  1.00 73.83  ? 224 TYR A O   1 
ATOM   1665 C CB  . TYR A 1 224 ? 107.530 103.218 69.104  1.00 76.28  ? 224 TYR A CB  1 
ATOM   1666 C CG  . TYR A 1 224 ? 108.516 102.159 68.668  1.00 77.08  ? 224 TYR A CG  1 
ATOM   1667 C CD1 . TYR A 1 224 ? 108.423 101.570 67.415  1.00 77.36  ? 224 TYR A CD1 1 
ATOM   1668 C CD2 . TYR A 1 224 ? 109.535 101.744 69.514  1.00 78.03  ? 224 TYR A CD2 1 
ATOM   1669 C CE1 . TYR A 1 224 ? 109.322 100.600 67.013  1.00 78.91  ? 224 TYR A CE1 1 
ATOM   1670 C CE2 . TYR A 1 224 ? 110.438 100.775 69.122  1.00 79.67  ? 224 TYR A CE2 1 
ATOM   1671 C CZ  . TYR A 1 224 ? 110.327 100.206 67.871  1.00 80.44  ? 224 TYR A CZ  1 
ATOM   1672 O OH  . TYR A 1 224 ? 111.225 99.241  67.478  1.00 83.32  ? 224 TYR A OH  1 
ATOM   1673 N N   . GLN A 1 225 ? 106.702 106.145 69.843  1.00 71.67  ? 225 GLN A N   1 
ATOM   1674 C CA  . GLN A 1 225 ? 105.745 107.091 70.397  1.00 70.85  ? 225 GLN A CA  1 
ATOM   1675 C C   . GLN A 1 225 ? 106.527 108.298 70.901  1.00 70.65  ? 225 GLN A C   1 
ATOM   1676 O O   . GLN A 1 225 ? 107.728 108.429 70.645  1.00 72.79  ? 225 GLN A O   1 
ATOM   1677 C CB  . GLN A 1 225 ? 104.906 106.423 71.494  1.00 70.58  ? 225 GLN A CB  1 
ATOM   1678 C CG  . GLN A 1 225 ? 105.694 106.064 72.745  1.00 71.28  ? 225 GLN A CG  1 
ATOM   1679 C CD  . GLN A 1 225 ? 104.817 105.946 73.972  1.00 72.59  ? 225 GLN A CD  1 
ATOM   1680 O OE1 . GLN A 1 225 ? 103.649 105.570 73.881  1.00 75.45  ? 225 GLN A OE1 1 
ATOM   1681 N NE2 . GLN A 1 225 ? 105.378 106.264 75.132  1.00 72.47  ? 225 GLN A NE2 1 
ATOM   1682 N N   . LYS A 1 226 ? 105.844 109.188 71.616  1.00 67.79  ? 226 LYS A N   1 
ATOM   1683 C CA  . LYS A 1 226 ? 106.523 110.313 72.238  1.00 64.02  ? 226 LYS A CA  1 
ATOM   1684 C C   . LYS A 1 226 ? 107.492 109.803 73.304  1.00 60.44  ? 226 LYS A C   1 
ATOM   1685 O O   . LYS A 1 226 ? 107.268 108.740 73.893  1.00 60.56  ? 226 LYS A O   1 
ATOM   1686 C CB  . LYS A 1 226 ? 105.508 111.273 72.857  1.00 64.14  ? 226 LYS A CB  1 
ATOM   1687 C CG  . LYS A 1 226 ? 104.668 112.028 71.842  1.00 64.93  ? 226 LYS A CG  1 
ATOM   1688 C CD  . LYS A 1 226 ? 103.814 113.088 72.515  1.00 65.85  ? 226 LYS A CD  1 
ATOM   1689 C CE  . LYS A 1 226 ? 102.952 113.827 71.505  1.00 67.54  ? 226 LYS A CE  1 
ATOM   1690 N NZ  . LYS A 1 226 ? 102.106 114.867 72.153  1.00 68.60  ? 226 LYS A NZ  1 
ATOM   1691 N N   . PRO A 1 227 ? 108.596 110.516 73.542  1.00 56.38  ? 227 PRO A N   1 
ATOM   1692 C CA  . PRO A 1 227 ? 109.580 110.047 74.526  1.00 54.26  ? 227 PRO A CA  1 
ATOM   1693 C C   . PRO A 1 227 ? 108.983 109.930 75.921  1.00 51.49  ? 227 PRO A C   1 
ATOM   1694 O O   . PRO A 1 227 ? 108.175 110.758 76.345  1.00 50.65  ? 227 PRO A O   1 
ATOM   1695 C CB  . PRO A 1 227 ? 110.671 111.122 74.471  1.00 54.94  ? 227 PRO A CB  1 
ATOM   1696 C CG  . PRO A 1 227 ? 110.533 111.721 73.116  1.00 55.33  ? 227 PRO A CG  1 
ATOM   1697 C CD  . PRO A 1 227 ? 109.060 111.728 72.846  1.00 55.89  ? 227 PRO A CD  1 
ATOM   1698 N N   . TRP A 1 228 ? 109.394 108.879 76.634  1.00 49.11  ? 228 TRP A N   1 
ATOM   1699 C CA  . TRP A 1 228 ? 108.856 108.617 77.963  1.00 47.87  ? 228 TRP A CA  1 
ATOM   1700 C C   . TRP A 1 228 ? 109.343 109.622 78.996  1.00 48.63  ? 228 TRP A C   1 
ATOM   1701 O O   . TRP A 1 228 ? 108.760 109.701 80.082  1.00 49.89  ? 228 TRP A O   1 
ATOM   1702 C CB  . TRP A 1 228 ? 109.215 107.199 78.409  1.00 45.93  ? 228 TRP A CB  1 
ATOM   1703 C CG  . TRP A 1 228 ? 110.687 106.946 78.517  1.00 43.73  ? 228 TRP A CG  1 
ATOM   1704 C CD1 . TRP A 1 228 ? 111.548 106.676 77.496  1.00 42.59  ? 228 TRP A CD1 1 
ATOM   1705 C CD2 . TRP A 1 228 ? 111.471 106.931 79.717  1.00 42.18  ? 228 TRP A CD2 1 
ATOM   1706 N NE1 . TRP A 1 228 ? 112.819 106.496 77.984  1.00 41.68  ? 228 TRP A NE1 1 
ATOM   1707 C CE2 . TRP A 1 228 ? 112.798 106.648 79.345  1.00 41.38  ? 228 TRP A CE2 1 
ATOM   1708 C CE3 . TRP A 1 228 ? 111.179 107.130 81.069  1.00 41.88  ? 228 TRP A CE3 1 
ATOM   1709 C CZ2 . TRP A 1 228 ? 113.830 106.560 80.274  1.00 41.07  ? 228 TRP A CZ2 1 
ATOM   1710 C CZ3 . TRP A 1 228 ? 112.205 107.041 81.989  1.00 41.25  ? 228 TRP A CZ3 1 
ATOM   1711 C CH2 . TRP A 1 228 ? 113.514 106.759 81.588  1.00 41.18  ? 228 TRP A CH2 1 
ATOM   1712 N N   . LEU A 1 229 ? 110.401 110.376 78.691  1.00 49.14  ? 229 LEU A N   1 
ATOM   1713 C CA  . LEU A 1 229 ? 110.870 111.406 79.612  1.00 50.36  ? 229 LEU A CA  1 
ATOM   1714 C C   . LEU A 1 229 ? 109.830 112.507 79.779  1.00 53.14  ? 229 LEU A C   1 
ATOM   1715 O O   . LEU A 1 229 ? 109.612 112.999 80.891  1.00 54.15  ? 229 LEU A O   1 
ATOM   1716 C CB  . LEU A 1 229 ? 112.195 111.982 79.117  1.00 49.28  ? 229 LEU A CB  1 
ATOM   1717 C CG  . LEU A 1 229 ? 112.966 112.885 80.077  1.00 48.77  ? 229 LEU A CG  1 
ATOM   1718 C CD1 . LEU A 1 229 ? 113.342 112.125 81.332  1.00 48.18  ? 229 LEU A CD1 1 
ATOM   1719 C CD2 . LEU A 1 229 ? 114.205 113.436 79.396  1.00 48.97  ? 229 LEU A CD2 1 
ATOM   1720 N N   . GLY A 1 230 ? 109.181 112.904 78.688  1.00 55.57  ? 230 GLY A N   1 
ATOM   1721 C CA  . GLY A 1 230 ? 108.089 113.851 78.758  1.00 57.62  ? 230 GLY A CA  1 
ATOM   1722 C C   . GLY A 1 230 ? 108.554 115.279 78.957  1.00 59.68  ? 230 GLY A C   1 
ATOM   1723 O O   . GLY A 1 230 ? 109.744 115.590 79.011  1.00 60.17  ? 230 GLY A O   1 
ATOM   1724 N N   . THR A 1 231 ? 107.571 116.167 79.073  1.00 62.19  ? 231 THR A N   1 
ATOM   1725 C CA  . THR A 1 231 ? 107.837 117.584 79.271  1.00 63.84  ? 231 THR A CA  1 
ATOM   1726 C C   . THR A 1 231 ? 106.621 118.222 79.924  1.00 64.44  ? 231 THR A C   1 
ATOM   1727 O O   . THR A 1 231 ? 105.533 117.642 79.953  1.00 64.71  ? 231 THR A O   1 
ATOM   1728 C CB  . THR A 1 231 ? 108.168 118.290 77.951  1.00 64.25  ? 231 THR A CB  1 
ATOM   1729 O OG1 . THR A 1 231 ? 108.530 119.651 78.212  1.00 65.92  ? 231 THR A OG1 1 
ATOM   1730 C CG2 . THR A 1 231 ? 106.969 118.260 77.015  1.00 62.94  ? 231 THR A CG2 1 
ATOM   1731 N N   . VAL A 1 232 ? 106.826 119.424 80.454  1.00 65.72  ? 232 VAL A N   1 
ATOM   1732 C CA  . VAL A 1 232 ? 105.764 120.214 81.067  1.00 67.45  ? 232 VAL A CA  1 
ATOM   1733 C C   . VAL A 1 232 ? 105.597 121.482 80.243  1.00 69.00  ? 232 VAL A C   1 
ATOM   1734 O O   . VAL A 1 232 ? 106.541 122.271 80.112  1.00 70.16  ? 232 VAL A O   1 
ATOM   1735 C CB  . VAL A 1 232 ? 106.070 120.550 82.534  1.00 67.21  ? 232 VAL A CB  1 
ATOM   1736 C CG1 . VAL A 1 232 ? 104.868 121.208 83.187  1.00 66.20  ? 232 VAL A CG1 1 
ATOM   1737 C CG2 . VAL A 1 232 ? 106.474 119.298 83.292  1.00 67.54  ? 232 VAL A CG2 1 
ATOM   1738 N N   . ASP A 1 233 ? 104.402 121.676 79.692  1.00 70.24  ? 233 ASP A N   1 
ATOM   1739 C CA  . ASP A 1 233 ? 104.132 122.852 78.882  1.00 70.80  ? 233 ASP A CA  1 
ATOM   1740 C C   . ASP A 1 233 ? 104.051 124.099 79.759  1.00 70.94  ? 233 ASP A C   1 
ATOM   1741 O O   . ASP A 1 233 ? 103.907 124.024 80.982  1.00 70.17  ? 233 ASP A O   1 
ATOM   1742 C CB  . ASP A 1 233 ? 102.833 122.676 78.097  1.00 71.88  ? 233 ASP A CB  1 
ATOM   1743 C CG  . ASP A 1 233 ? 102.947 121.627 77.011  1.00 73.26  ? 233 ASP A CG  1 
ATOM   1744 O OD1 . ASP A 1 233 ? 104.082 121.348 76.571  1.00 74.89  ? 233 ASP A OD1 1 
ATOM   1745 O OD2 . ASP A 1 233 ? 101.903 121.081 76.598  1.00 74.06  ? 233 ASP A OD2 1 
ATOM   1746 N N   . SER A 1 234 ? 104.159 125.261 79.110  1.00 72.16  ? 234 SER A N   1 
ATOM   1747 C CA  . SER A 1 234 ? 104.087 126.526 79.835  1.00 73.64  ? 234 SER A CA  1 
ATOM   1748 C C   . SER A 1 234 ? 102.707 126.743 80.444  1.00 74.01  ? 234 SER A C   1 
ATOM   1749 O O   . SER A 1 234 ? 102.590 127.245 81.568  1.00 75.65  ? 234 SER A O   1 
ATOM   1750 C CB  . SER A 1 234 ? 104.451 127.684 78.907  1.00 73.97  ? 234 SER A CB  1 
ATOM   1751 O OG  . SER A 1 234 ? 105.763 127.532 78.394  1.00 75.52  ? 234 SER A OG  1 
ATOM   1752 N N   . SER A 1 235 ? 101.650 126.376 79.717  1.00 73.46  ? 235 SER A N   1 
ATOM   1753 C CA  . SER A 1 235 ? 100.298 126.571 80.231  1.00 73.11  ? 235 SER A CA  1 
ATOM   1754 C C   . SER A 1 235 ? 99.945  125.551 81.306  1.00 72.24  ? 235 SER A C   1 
ATOM   1755 O O   . SER A 1 235 ? 99.072  125.812 82.140  1.00 73.83  ? 235 SER A O   1 
ATOM   1756 C CB  . SER A 1 235 ? 99.287  126.505 79.087  1.00 73.25  ? 235 SER A CB  1 
ATOM   1757 O OG  . SER A 1 235 ? 99.274  125.220 78.492  1.00 73.38  ? 235 SER A OG  1 
ATOM   1758 N N   . GLU A 1 236 ? 100.604 124.392 81.306  1.00 69.22  ? 236 GLU A N   1 
ATOM   1759 C CA  . GLU A 1 236 ? 100.296 123.312 82.234  1.00 66.50  ? 236 GLU A CA  1 
ATOM   1760 C C   . GLU A 1 236 ? 101.206 123.307 83.457  1.00 62.91  ? 236 GLU A C   1 
ATOM   1761 O O   . GLU A 1 236 ? 101.284 122.291 84.156  1.00 61.81  ? 236 GLU A O   1 
ATOM   1762 C CB  . GLU A 1 236 ? 100.369 121.964 81.518  1.00 68.18  ? 236 GLU A CB  1 
ATOM   1763 C CG  . GLU A 1 236 ? 99.155  121.657 80.659  1.00 70.22  ? 236 GLU A CG  1 
ATOM   1764 C CD  . GLU A 1 236 ? 99.193  120.259 80.076  1.00 72.64  ? 236 GLU A CD  1 
ATOM   1765 O OE1 . GLU A 1 236 ? 100.278 119.641 80.081  1.00 73.63  ? 236 GLU A OE1 1 
ATOM   1766 O OE2 . GLU A 1 236 ? 98.138  119.779 79.612  1.00 75.35  ? 236 GLU A OE2 1 
ATOM   1767 N N   . VAL A 1 237 ? 101.907 124.411 83.720  1.00 59.08  ? 237 VAL A N   1 
ATOM   1768 C CA  . VAL A 1 237 ? 102.721 124.503 84.929  1.00 56.65  ? 237 VAL A CA  1 
ATOM   1769 C C   . VAL A 1 237 ? 101.837 124.490 86.170  1.00 56.12  ? 237 VAL A C   1 
ATOM   1770 O O   . VAL A 1 237 ? 102.135 123.803 87.155  1.00 56.52  ? 237 VAL A O   1 
ATOM   1771 C CB  . VAL A 1 237 ? 103.609 125.760 84.880  1.00 54.93  ? 237 VAL A CB  1 
ATOM   1772 C CG1 . VAL A 1 237 ? 104.318 125.970 86.207  1.00 54.40  ? 237 VAL A CG1 1 
ATOM   1773 C CG2 . VAL A 1 237 ? 104.618 125.651 83.754  1.00 54.86  ? 237 VAL A CG2 1 
ATOM   1774 N N   . TYR A 1 238 ? 100.730 125.236 86.137  1.00 56.02  ? 238 TYR A N   1 
ATOM   1775 C CA  . TYR A 1 238 ? 99.879  125.362 87.317  1.00 56.34  ? 238 TYR A CA  1 
ATOM   1776 C C   . TYR A 1 238 ? 99.169  124.053 87.643  1.00 55.80  ? 238 TYR A C   1 
ATOM   1777 O O   . TYR A 1 238 ? 99.030  123.700 88.819  1.00 56.81  ? 238 TYR A O   1 
ATOM   1778 C CB  . TYR A 1 238 ? 98.869  126.490 87.115  1.00 56.68  ? 238 TYR A CB  1 
ATOM   1779 C CG  . TYR A 1 238 ? 99.497  127.864 87.149  1.00 57.12  ? 238 TYR A CG  1 
ATOM   1780 C CD1 . TYR A 1 238 ? 100.238 128.281 88.247  1.00 56.98  ? 238 TYR A CD1 1 
ATOM   1781 C CD2 . TYR A 1 238 ? 99.353  128.743 86.084  1.00 57.87  ? 238 TYR A CD2 1 
ATOM   1782 C CE1 . TYR A 1 238 ? 100.817 129.534 88.284  1.00 57.59  ? 238 TYR A CE1 1 
ATOM   1783 C CE2 . TYR A 1 238 ? 99.929  129.998 86.112  1.00 58.79  ? 238 TYR A CE2 1 
ATOM   1784 C CZ  . TYR A 1 238 ? 100.660 130.388 87.214  1.00 58.67  ? 238 TYR A CZ  1 
ATOM   1785 O OH  . TYR A 1 238 ? 101.234 131.637 87.246  1.00 59.61  ? 238 TYR A OH  1 
ATOM   1786 N N   . SER A 1 239 ? 98.713  123.320 86.624  1.00 54.54  ? 239 SER A N   1 
ATOM   1787 C CA  . SER A 1 239 ? 98.067  122.034 86.875  1.00 54.39  ? 239 SER A CA  1 
ATOM   1788 C C   . SER A 1 239 ? 99.049  121.022 87.457  1.00 53.92  ? 239 SER A C   1 
ATOM   1789 O O   . SER A 1 239 ? 98.704  120.267 88.379  1.00 55.56  ? 239 SER A O   1 
ATOM   1790 C CB  . SER A 1 239 ? 97.445  121.500 85.586  1.00 54.57  ? 239 SER A CB  1 
ATOM   1791 O OG  . SER A 1 239 ? 96.791  120.264 85.811  1.00 55.64  ? 239 SER A OG  1 
ATOM   1792 N N   . TRP A 1 240 ? 100.278 120.993 86.932  1.00 52.03  ? 240 TRP A N   1 
ATOM   1793 C CA  . TRP A 1 240 ? 101.292 120.098 87.478  1.00 50.49  ? 240 TRP A CA  1 
ATOM   1794 C C   . TRP A 1 240 ? 101.640 120.470 88.911  1.00 49.47  ? 240 TRP A C   1 
ATOM   1795 O O   . TRP A 1 240 ? 101.817 119.590 89.758  1.00 49.31  ? 240 TRP A O   1 
ATOM   1796 C CB  . TRP A 1 240 ? 102.550 120.114 86.611  1.00 49.57  ? 240 TRP A CB  1 
ATOM   1797 C CG  . TRP A 1 240 ? 103.597 119.173 87.117  1.00 48.45  ? 240 TRP A CG  1 
ATOM   1798 C CD1 . TRP A 1 240 ? 103.587 117.814 87.024  1.00 48.13  ? 240 TRP A CD1 1 
ATOM   1799 C CD2 . TRP A 1 240 ? 104.796 119.516 87.822  1.00 47.46  ? 240 TRP A CD2 1 
ATOM   1800 N NE1 . TRP A 1 240 ? 104.709 117.289 87.614  1.00 47.81  ? 240 TRP A NE1 1 
ATOM   1801 C CE2 . TRP A 1 240 ? 105.468 118.314 88.112  1.00 47.37  ? 240 TRP A CE2 1 
ATOM   1802 C CE3 . TRP A 1 240 ? 105.368 120.724 88.229  1.00 47.45  ? 240 TRP A CE3 1 
ATOM   1803 C CZ2 . TRP A 1 240 ? 106.683 118.283 88.791  1.00 47.58  ? 240 TRP A CZ2 1 
ATOM   1804 C CZ3 . TRP A 1 240 ? 106.575 120.692 88.903  1.00 47.65  ? 240 TRP A CZ3 1 
ATOM   1805 C CH2 . TRP A 1 240 ? 107.219 119.480 89.177  1.00 47.69  ? 240 TRP A CH2 1 
ATOM   1806 N N   . LEU A 1 241 ? 101.744 121.771 89.200  1.00 48.66  ? 241 LEU A N   1 
ATOM   1807 C CA  . LEU A 1 241 ? 102.016 122.202 90.568  1.00 48.53  ? 241 LEU A CA  1 
ATOM   1808 C C   . LEU A 1 241 ? 100.868 121.839 91.499  1.00 48.80  ? 241 LEU A C   1 
ATOM   1809 O O   . LEU A 1 241 ? 101.096 121.459 92.652  1.00 48.28  ? 241 LEU A O   1 
ATOM   1810 C CB  . LEU A 1 241 ? 102.282 123.706 90.607  1.00 48.76  ? 241 LEU A CB  1 
ATOM   1811 C CG  . LEU A 1 241 ? 103.747 124.114 90.457  1.00 49.44  ? 241 LEU A CG  1 
ATOM   1812 C CD1 . LEU A 1 241 ? 103.896 125.623 90.534  1.00 49.76  ? 241 LEU A CD1 1 
ATOM   1813 C CD2 . LEU A 1 241 ? 104.593 123.433 91.518  1.00 49.62  ? 241 LEU A CD2 1 
ATOM   1814 N N   . ASP A 1 242 ? 99.628  121.939 91.012  1.00 50.49  ? 242 ASP A N   1 
ATOM   1815 C CA  . ASP A 1 242 ? 98.471  121.556 91.815  1.00 51.92  ? 242 ASP A CA  1 
ATOM   1816 C C   . ASP A 1 242 ? 98.505  120.075 92.163  1.00 51.53  ? 242 ASP A C   1 
ATOM   1817 O O   . ASP A 1 242 ? 98.326  119.694 93.326  1.00 53.55  ? 242 ASP A O   1 
ATOM   1818 C CB  . ASP A 1 242 ? 97.185  121.894 91.065  1.00 53.06  ? 242 ASP A CB  1 
ATOM   1819 C CG  . ASP A 1 242 ? 95.943  121.620 91.884  1.00 54.54  ? 242 ASP A CG  1 
ATOM   1820 O OD1 . ASP A 1 242 ? 96.040  121.586 93.129  1.00 55.91  ? 242 ASP A OD1 1 
ATOM   1821 O OD2 . ASP A 1 242 ? 94.866  121.434 91.280  1.00 56.05  ? 242 ASP A OD2 1 
ATOM   1822 N N   . SER A 1 243 ? 98.742  119.221 91.166  1.00 49.66  ? 243 SER A N   1 
ATOM   1823 C CA  . SER A 1 243 ? 98.778  117.785 91.435  1.00 48.49  ? 243 SER A CA  1 
ATOM   1824 C C   . SER A 1 243 ? 99.986  117.396 92.284  1.00 46.86  ? 243 SER A C   1 
ATOM   1825 O O   . SER A 1 243 ? 99.891  116.492 93.125  1.00 47.45  ? 243 SER A O   1 
ATOM   1826 C CB  . SER A 1 243 ? 98.770  117.006 90.123  1.00 49.43  ? 243 SER A CB  1 
ATOM   1827 O OG  . SER A 1 243 ? 98.856  115.614 90.362  1.00 51.17  ? 243 SER A OG  1 
ATOM   1828 N N   . PHE A 1 244 ? 101.117 118.077 92.100  1.00 44.97  ? 244 PHE A N   1 
ATOM   1829 C CA  . PHE A 1 244 ? 102.303 117.773 92.891  1.00 43.45  ? 244 PHE A CA  1 
ATOM   1830 C C   . PHE A 1 244 ? 102.129 118.210 94.340  1.00 41.54  ? 244 PHE A C   1 
ATOM   1831 O O   . PHE A 1 244 ? 102.571 117.513 95.259  1.00 40.96  ? 244 PHE A O   1 
ATOM   1832 C CB  . PHE A 1 244 ? 103.521 118.433 92.250  1.00 43.92  ? 244 PHE A CB  1 
ATOM   1833 C CG  . PHE A 1 244 ? 104.796 118.226 93.001  1.00 43.56  ? 244 PHE A CG  1 
ATOM   1834 C CD1 . PHE A 1 244 ? 105.273 116.950 93.238  1.00 43.40  ? 244 PHE A CD1 1 
ATOM   1835 C CD2 . PHE A 1 244 ? 105.546 119.307 93.422  1.00 43.24  ? 244 PHE A CD2 1 
ATOM   1836 C CE1 . PHE A 1 244 ? 106.456 116.757 93.916  1.00 43.41  ? 244 PHE A CE1 1 
ATOM   1837 C CE2 . PHE A 1 244 ? 106.732 119.122 94.092  1.00 43.04  ? 244 PHE A CE2 1 
ATOM   1838 C CZ  . PHE A 1 244 ? 107.187 117.845 94.343  1.00 43.33  ? 244 PHE A CZ  1 
ATOM   1839 N N   . LEU A 1 245 ? 101.471 119.350 94.569  1.00 40.32  ? 245 LEU A N   1 
ATOM   1840 C CA  . LEU A 1 245 ? 101.126 119.742 95.930  1.00 39.83  ? 245 LEU A CA  1 
ATOM   1841 C C   . LEU A 1 245 ? 100.101 118.797 96.536  1.00 38.89  ? 245 LEU A C   1 
ATOM   1842 O O   . LEU A 1 245 ? 100.146 118.533 97.742  1.00 38.11  ? 245 LEU A O   1 
ATOM   1843 C CB  . LEU A 1 245 ? 100.604 121.177 95.952  1.00 39.99  ? 245 LEU A CB  1 
ATOM   1844 C CG  . LEU A 1 245 ? 101.659 122.282 95.927  1.00 40.42  ? 245 LEU A CG  1 
ATOM   1845 C CD1 . LEU A 1 245 ? 101.007 123.642 96.092  1.00 40.51  ? 245 LEU A CD1 1 
ATOM   1846 C CD2 . LEU A 1 245 ? 102.697 122.052 97.007  1.00 40.69  ? 245 LEU A CD2 1 
ATOM   1847 N N   . LEU A 1 246 ? 99.176  118.283 95.720  1.00 39.02  ? 246 LEU A N   1 
ATOM   1848 C CA  . LEU A 1 246 ? 98.248  117.259 96.189  1.00 39.51  ? 246 LEU A CA  1 
ATOM   1849 C C   . LEU A 1 246 ? 98.992  116.027 96.684  1.00 39.49  ? 246 LEU A C   1 
ATOM   1850 O O   . LEU A 1 246 ? 98.688  115.502 97.760  1.00 38.98  ? 246 LEU A O   1 
ATOM   1851 C CB  . LEU A 1 246 ? 97.278  116.882 95.069  1.00 40.24  ? 246 LEU A CB  1 
ATOM   1852 C CG  . LEU A 1 246 ? 96.395  115.648 95.263  1.00 40.47  ? 246 LEU A CG  1 
ATOM   1853 C CD1 . LEU A 1 246 ? 95.460  115.819 96.434  1.00 40.62  ? 246 LEU A CD1 1 
ATOM   1854 C CD2 . LEU A 1 246 ? 95.611  115.348 93.996  1.00 40.29  ? 246 LEU A CD2 1 
ATOM   1855 N N   . LEU A 1 247 ? 99.988  115.567 95.927  1.00 39.86  ? 247 LEU A N   1 
ATOM   1856 C CA  . LEU A 1 247 ? 100.736 114.388 96.357  1.00 39.34  ? 247 LEU A CA  1 
ATOM   1857 C C   . LEU A 1 247 ? 101.659 114.689 97.535  1.00 39.20  ? 247 LEU A C   1 
ATOM   1858 O O   . LEU A 1 247 ? 101.911 113.803 98.359  1.00 37.83  ? 247 LEU A O   1 
ATOM   1859 C CB  . LEU A 1 247 ? 101.533 113.808 95.191  1.00 39.14  ? 247 LEU A CB  1 
ATOM   1860 C CG  . LEU A 1 247 ? 100.697 113.023 94.182  1.00 39.00  ? 247 LEU A CG  1 
ATOM   1861 C CD1 . LEU A 1 247 ? 101.569 112.489 93.064  1.00 39.48  ? 247 LEU A CD1 1 
ATOM   1862 C CD2 . LEU A 1 247 ? 99.964  111.894 94.877  1.00 38.73  ? 247 LEU A CD2 1 
ATOM   1863 N N   . MET A 1 248 ? 102.179 115.916 97.634  1.00 39.97  ? 248 MET A N   1 
ATOM   1864 C CA  . MET A 1 248 ? 103.071 116.253 98.741  1.00 40.64  ? 248 MET A CA  1 
ATOM   1865 C C   . MET A 1 248 ? 102.312 116.398 100.055 1.00 40.28  ? 248 MET A C   1 
ATOM   1866 O O   . MET A 1 248 ? 102.748 115.889 101.093 1.00 40.56  ? 248 MET A O   1 
ATOM   1867 C CB  . MET A 1 248 ? 103.835 117.543 98.444  1.00 41.76  ? 248 MET A CB  1 
ATOM   1868 C CG  . MET A 1 248 ? 104.803 117.926 99.556  1.00 42.54  ? 248 MET A CG  1 
ATOM   1869 S SD  . MET A 1 248 ? 105.833 119.367 99.223  1.00 43.92  ? 248 MET A SD  1 
ATOM   1870 C CE  . MET A 1 248 ? 105.795 119.418 97.441  1.00 43.48  ? 248 MET A CE  1 
ATOM   1871 N N   . LEU A 1 249 ? 101.182 117.101 100.039 1.00 39.31  ? 249 LEU A N   1 
ATOM   1872 C CA  . LEU A 1 249 ? 100.508 117.460 101.277 1.00 38.39  ? 249 LEU A CA  1 
ATOM   1873 C C   . LEU A 1 249 ? 99.315  116.575 101.602 1.00 38.40  ? 249 LEU A C   1 
ATOM   1874 O O   . LEU A 1 249 ? 98.891  116.542 102.761 1.00 37.62  ? 249 LEU A O   1 
ATOM   1875 C CB  . LEU A 1 249 ? 100.063 118.926 101.220 1.00 37.65  ? 249 LEU A CB  1 
ATOM   1876 C CG  . LEU A 1 249 ? 101.205 119.869 100.837 1.00 37.13  ? 249 LEU A CG  1 
ATOM   1877 C CD1 . LEU A 1 249 ? 100.720 121.284 100.607 1.00 37.01  ? 249 LEU A CD1 1 
ATOM   1878 C CD2 . LEU A 1 249 ? 102.271 119.848 101.909 1.00 37.34  ? 249 LEU A CD2 1 
ATOM   1879 N N   . GLY A 1 250 ? 98.765  115.859 100.623 1.00 38.82  ? 250 GLY A N   1 
ATOM   1880 C CA  . GLY A 1 250 ? 97.712  114.911 100.907 1.00 38.92  ? 250 GLY A CA  1 
ATOM   1881 C C   . GLY A 1 250 ? 98.189  113.566 101.394 1.00 39.40  ? 250 GLY A C   1 
ATOM   1882 O O   . GLY A 1 250 ? 97.374  112.778 101.876 1.00 39.76  ? 250 GLY A O   1 
ATOM   1883 N N   . GLY A 1 251 ? 99.486  113.282 101.271 1.00 40.16  ? 251 GLY A N   1 
ATOM   1884 C CA  . GLY A 1 251 ? 100.052 112.039 101.762 1.00 40.46  ? 251 GLY A CA  1 
ATOM   1885 C C   . GLY A 1 251 ? 100.387 112.020 103.236 1.00 40.23  ? 251 GLY A C   1 
ATOM   1886 O O   . GLY A 1 251 ? 100.650 110.946 103.785 1.00 40.14  ? 251 GLY A O   1 
ATOM   1887 N N   . ILE A 1 252 ? 100.393 113.180 103.883 1.00 39.84  ? 252 ILE A N   1 
ATOM   1888 C CA  . ILE A 1 252 ? 100.692 113.296 105.310 1.00 39.97  ? 252 ILE A CA  1 
ATOM   1889 C C   . ILE A 1 252 ? 99.523  112.880 106.206 1.00 40.76  ? 252 ILE A C   1 
ATOM   1890 O O   . ILE A 1 252 ? 99.716  112.000 107.056 1.00 41.79  ? 252 ILE A O   1 
ATOM   1891 C CB  . ILE A 1 252 ? 101.158 114.719 105.658 1.00 39.90  ? 252 ILE A CB  1 
ATOM   1892 C CG1 . ILE A 1 252 ? 102.433 115.068 104.894 1.00 40.16  ? 252 ILE A CG1 1 
ATOM   1893 C CG2 . ILE A 1 252 ? 101.382 114.849 107.150 1.00 39.91  ? 252 ILE A CG2 1 
ATOM   1894 C CD1 . ILE A 1 252 ? 102.978 116.438 105.223 1.00 40.20  ? 252 ILE A CD1 1 
ATOM   1895 N N   . PRO A 1 253 ? 98.313  113.439 106.085 1.00 40.97  ? 253 PRO A N   1 
ATOM   1896 C CA  . PRO A 1 253 ? 97.314  113.257 107.146 1.00 40.73  ? 253 PRO A CA  1 
ATOM   1897 C C   . PRO A 1 253 ? 96.632  111.898 107.174 1.00 40.72  ? 253 PRO A C   1 
ATOM   1898 O O   . PRO A 1 253 ? 95.583  111.778 107.810 1.00 41.91  ? 253 PRO A O   1 
ATOM   1899 C CB  . PRO A 1 253 ? 96.281  114.359 106.841 1.00 40.52  ? 253 PRO A CB  1 
ATOM   1900 C CG  . PRO A 1 253 ? 96.861  115.176 105.744 1.00 40.82  ? 253 PRO A CG  1 
ATOM   1901 C CD  . PRO A 1 253 ? 97.725  114.242 105.000 1.00 40.86  ? 253 PRO A CD  1 
ATOM   1902 N N   . TRP A 1 254 ? 97.156  110.875 106.511 1.00 39.82  ? 254 TRP A N   1 
ATOM   1903 C CA  . TRP A 1 254 ? 96.467  109.595 106.473 1.00 39.45  ? 254 TRP A CA  1 
ATOM   1904 C C   . TRP A 1 254 ? 96.647  108.846 107.790 1.00 39.59  ? 254 TRP A C   1 
ATOM   1905 O O   . TRP A 1 254 ? 97.654  109.004 108.485 1.00 38.96  ? 254 TRP A O   1 
ATOM   1906 C CB  . TRP A 1 254 ? 96.983  108.758 105.306 1.00 38.84  ? 254 TRP A CB  1 
ATOM   1907 C CG  . TRP A 1 254 ? 96.368  109.165 104.012 1.00 38.69  ? 254 TRP A CG  1 
ATOM   1908 C CD1 . TRP A 1 254 ? 96.735  110.218 103.241 1.00 39.21  ? 254 TRP A CD1 1 
ATOM   1909 C CD2 . TRP A 1 254 ? 95.277  108.534 103.335 1.00 38.67  ? 254 TRP A CD2 1 
ATOM   1910 N NE1 . TRP A 1 254 ? 95.943  110.292 102.124 1.00 39.47  ? 254 TRP A NE1 1 
ATOM   1911 C CE2 . TRP A 1 254 ? 95.038  109.266 102.158 1.00 39.25  ? 254 TRP A CE2 1 
ATOM   1912 C CE3 . TRP A 1 254 ? 94.481  107.422 103.608 1.00 38.73  ? 254 TRP A CE3 1 
ATOM   1913 C CZ2 . TRP A 1 254 ? 94.040  108.920 101.255 1.00 39.60  ? 254 TRP A CZ2 1 
ATOM   1914 C CZ3 . TRP A 1 254 ? 93.490  107.081 102.712 1.00 39.19  ? 254 TRP A CZ3 1 
ATOM   1915 C CH2 . TRP A 1 254 ? 93.277  107.827 101.549 1.00 39.46  ? 254 TRP A CH2 1 
ATOM   1916 N N   . GLN A 1 255 ? 95.643  108.033 108.135 1.00 40.55  ? 255 GLN A N   1 
ATOM   1917 C CA  . GLN A 1 255 ? 95.736  107.198 109.331 1.00 41.27  ? 255 GLN A CA  1 
ATOM   1918 C C   . GLN A 1 255 ? 96.857  106.174 109.211 1.00 42.52  ? 255 GLN A C   1 
ATOM   1919 O O   . GLN A 1 255 ? 97.549  105.887 110.194 1.00 42.87  ? 255 GLN A O   1 
ATOM   1920 C CB  . GLN A 1 255 ? 94.406  106.489 109.589 1.00 41.22  ? 255 GLN A CB  1 
ATOM   1921 C CG  . GLN A 1 255 ? 94.414  105.573 110.809 1.00 41.85  ? 255 GLN A CG  1 
ATOM   1922 C CD  . GLN A 1 255 ? 94.545  106.296 112.118 1.00 42.48  ? 255 GLN A CD  1 
ATOM   1923 O OE1 . GLN A 1 255 ? 93.900  107.311 112.335 1.00 43.25  ? 255 GLN A OE1 1 
ATOM   1924 N NE2 . GLN A 1 255 ? 95.390  105.781 113.002 1.00 42.47  ? 255 GLN A NE2 1 
ATOM   1925 N N   . ALA A 1 256 ? 97.052  105.618 108.011 1.00 43.95  ? 256 ALA A N   1 
ATOM   1926 C CA  . ALA A 1 256 ? 98.072  104.596 107.802 1.00 44.50  ? 256 ALA A CA  1 
ATOM   1927 C C   . ALA A 1 256 ? 99.481  105.117 108.043 1.00 46.10  ? 256 ALA A C   1 
ATOM   1928 O O   . ALA A 1 256 ? 100.391 104.318 108.287 1.00 47.63  ? 256 ALA A O   1 
ATOM   1929 C CB  . ALA A 1 256 ? 97.963  104.032 106.386 1.00 44.01  ? 256 ALA A CB  1 
ATOM   1930 N N   . TYR A 1 257 ? 99.686  106.431 107.979 1.00 46.81  ? 257 TYR A N   1 
ATOM   1931 C CA  . TYR A 1 257 ? 100.991 107.006 108.275 1.00 46.85  ? 257 TYR A CA  1 
ATOM   1932 C C   . TYR A 1 257 ? 101.175 107.326 109.754 1.00 48.01  ? 257 TYR A C   1 
ATOM   1933 O O   . TYR A 1 257 ? 102.216 106.989 110.325 1.00 48.51  ? 257 TYR A O   1 
ATOM   1934 C CB  . TYR A 1 257 ? 101.218 108.264 107.435 1.00 45.70  ? 257 TYR A CB  1 
ATOM   1935 C CG  . TYR A 1 257 ? 102.564 108.909 107.665 1.00 44.70  ? 257 TYR A CG  1 
ATOM   1936 C CD1 . TYR A 1 257 ? 103.722 108.361 107.143 1.00 44.28  ? 257 TYR A CD1 1 
ATOM   1937 C CD2 . TYR A 1 257 ? 102.668 110.084 108.388 1.00 44.61  ? 257 TYR A CD2 1 
ATOM   1938 C CE1 . TYR A 1 257 ? 104.948 108.960 107.358 1.00 44.09  ? 257 TYR A CE1 1 
ATOM   1939 C CE2 . TYR A 1 257 ? 103.883 110.686 108.608 1.00 44.33  ? 257 TYR A CE2 1 
ATOM   1940 C CZ  . TYR A 1 257 ? 105.020 110.122 108.092 1.00 43.92  ? 257 TYR A CZ  1 
ATOM   1941 O OH  . TYR A 1 257 ? 106.232 110.731 108.313 1.00 43.49  ? 257 TYR A OH  1 
ATOM   1942 N N   . PHE A 1 258 ? 100.194 107.963 110.400 1.00 48.83  ? 258 PHE A N   1 
ATOM   1943 C CA  . PHE A 1 258 ? 100.376 108.288 111.812 1.00 49.60  ? 258 PHE A CA  1 
ATOM   1944 C C   . PHE A 1 258 ? 100.264 107.078 112.728 1.00 48.75  ? 258 PHE A C   1 
ATOM   1945 O O   . PHE A 1 258 ? 100.715 107.147 113.874 1.00 48.76  ? 258 PHE A O   1 
ATOM   1946 C CB  . PHE A 1 258 ? 99.431  109.397 112.277 1.00 51.88  ? 258 PHE A CB  1 
ATOM   1947 C CG  . PHE A 1 258 ? 99.775  110.755 111.737 1.00 54.01  ? 258 PHE A CG  1 
ATOM   1948 C CD1 . PHE A 1 258 ? 101.005 110.994 111.159 1.00 53.92  ? 258 PHE A CD1 1 
ATOM   1949 C CD2 . PHE A 1 258 ? 98.901  111.809 111.876 1.00 56.13  ? 258 PHE A CD2 1 
ATOM   1950 C CE1 . PHE A 1 258 ? 101.332 112.248 110.683 1.00 55.14  ? 258 PHE A CE1 1 
ATOM   1951 C CE2 . PHE A 1 258 ? 99.220  113.060 111.404 1.00 57.61  ? 258 PHE A CE2 1 
ATOM   1952 C CZ  . PHE A 1 258 ? 100.438 113.281 110.806 1.00 57.26  ? 258 PHE A CZ  1 
ATOM   1953 N N   . GLN A 1 259 ? 99.678  105.973 112.272 1.00 47.69  ? 259 GLN A N   1 
ATOM   1954 C CA  . GLN A 1 259 ? 99.673  104.796 113.133 1.00 47.04  ? 259 GLN A CA  1 
ATOM   1955 C C   . GLN A 1 259 ? 101.074 104.215 113.302 1.00 46.54  ? 259 GLN A C   1 
ATOM   1956 O O   . GLN A 1 259 ? 101.365 103.617 114.344 1.00 47.55  ? 259 GLN A O   1 
ATOM   1957 C CB  . GLN A 1 259 ? 98.710  103.740 112.585 1.00 46.39  ? 259 GLN A CB  1 
ATOM   1958 C CG  . GLN A 1 259 ? 98.515  102.536 113.492 1.00 46.00  ? 259 GLN A CG  1 
ATOM   1959 C CD  . GLN A 1 259 ? 97.432  101.602 112.997 1.00 45.95  ? 259 GLN A CD  1 
ATOM   1960 O OE1 . GLN A 1 259 ? 96.753  101.888 112.013 1.00 46.77  ? 259 GLN A OE1 1 
ATOM   1961 N NE2 . GLN A 1 259 ? 97.239  100.496 113.701 1.00 45.43  ? 259 GLN A NE2 1 
ATOM   1962 N N   . ARG A 1 260 ? 101.954 104.402 112.314 1.00 44.82  ? 260 ARG A N   1 
ATOM   1963 C CA  . ARG A 1 260 ? 103.327 103.920 112.434 1.00 43.63  ? 260 ARG A CA  1 
ATOM   1964 C C   . ARG A 1 260 ? 104.203 104.876 113.238 1.00 43.91  ? 260 ARG A C   1 
ATOM   1965 O O   . ARG A 1 260 ? 105.053 104.430 114.017 1.00 44.73  ? 260 ARG A O   1 
ATOM   1966 C CB  . ARG A 1 260 ? 103.923 103.681 111.050 1.00 42.61  ? 260 ARG A CB  1 
ATOM   1967 C CG  . ARG A 1 260 ? 102.999 102.920 110.130 1.00 41.99  ? 260 ARG A CG  1 
ATOM   1968 C CD  . ARG A 1 260 ? 103.188 101.428 110.323 1.00 41.78  ? 260 ARG A CD  1 
ATOM   1969 N NE  . ARG A 1 260 ? 102.589 100.644 109.252 1.00 41.81  ? 260 ARG A NE  1 
ATOM   1970 C CZ  . ARG A 1 260 ? 101.299 100.357 109.160 1.00 42.17  ? 260 ARG A CZ  1 
ATOM   1971 N NH1 . ARG A 1 260 ? 100.427 100.789 110.056 1.00 42.57  ? 260 ARG A NH1 1 
ATOM   1972 N NH2 . ARG A 1 260 ? 100.873 99.610  108.148 1.00 42.23  ? 260 ARG A NH2 1 
ATOM   1973 N N   . VAL A 1 261 ? 104.034 106.189 113.050 1.00 43.71  ? 261 VAL A N   1 
ATOM   1974 C CA  . VAL A 1 261 ? 104.901 107.139 113.745 1.00 43.43  ? 261 VAL A CA  1 
ATOM   1975 C C   . VAL A 1 261 ? 104.587 107.154 115.240 1.00 42.56  ? 261 VAL A C   1 
ATOM   1976 O O   . VAL A 1 261 ? 105.477 107.395 116.065 1.00 42.26  ? 261 VAL A O   1 
ATOM   1977 C CB  . VAL A 1 261 ? 104.791 108.544 113.114 1.00 43.95  ? 261 VAL A CB  1 
ATOM   1978 C CG1 . VAL A 1 261 ? 103.425 109.123 113.295 1.00 44.19  ? 261 VAL A CG1 1 
ATOM   1979 C CG2 . VAL A 1 261 ? 105.815 109.486 113.682 1.00 44.46  ? 261 VAL A CG2 1 
ATOM   1980 N N   . LEU A 1 262 ? 103.334 106.881 115.619 1.00 41.87  ? 262 LEU A N   1 
ATOM   1981 C CA  . LEU A 1 262 ? 102.996 106.767 117.034 1.00 42.09  ? 262 LEU A CA  1 
ATOM   1982 C C   . LEU A 1 262 ? 103.542 105.482 117.642 1.00 42.55  ? 262 LEU A C   1 
ATOM   1983 O O   . LEU A 1 262 ? 103.772 105.421 118.854 1.00 42.43  ? 262 LEU A O   1 
ATOM   1984 C CB  . LEU A 1 262 ? 101.481 106.836 117.229 1.00 41.68  ? 262 LEU A CB  1 
ATOM   1985 C CG  . LEU A 1 262 ? 100.790 108.151 116.873 1.00 41.41  ? 262 LEU A CG  1 
ATOM   1986 C CD1 . LEU A 1 262 ? 99.285  108.012 116.974 1.00 41.41  ? 262 LEU A CD1 1 
ATOM   1987 C CD2 . LEU A 1 262 ? 101.277 109.260 117.766 1.00 41.32  ? 262 LEU A CD2 1 
ATOM   1988 N N   . SER A 1 263 ? 103.751 104.450 116.826 1.00 43.69  ? 263 SER A N   1 
ATOM   1989 C CA  . SER A 1 263 ? 104.208 103.162 117.330 1.00 45.44  ? 263 SER A CA  1 
ATOM   1990 C C   . SER A 1 263 ? 105.719 103.079 117.501 1.00 46.16  ? 263 SER A C   1 
ATOM   1991 O O   . SER A 1 263 ? 106.205 102.071 118.023 1.00 46.08  ? 263 SER A O   1 
ATOM   1992 C CB  . SER A 1 263 ? 103.740 102.042 116.399 1.00 46.40  ? 263 SER A CB  1 
ATOM   1993 O OG  . SER A 1 263 ? 104.624 101.885 115.305 1.00 47.28  ? 263 SER A OG  1 
ATOM   1994 N N   . SER A 1 264 ? 106.469 104.095 117.074 1.00 46.62  ? 264 SER A N   1 
ATOM   1995 C CA  . SER A 1 264 ? 107.919 104.071 117.215 1.00 46.34  ? 264 SER A CA  1 
ATOM   1996 C C   . SER A 1 264 ? 108.322 104.125 118.684 1.00 47.17  ? 264 SER A C   1 
ATOM   1997 O O   . SER A 1 264 ? 107.618 104.689 119.525 1.00 47.61  ? 264 SER A O   1 
ATOM   1998 C CB  . SER A 1 264 ? 108.551 105.234 116.454 1.00 45.90  ? 264 SER A CB  1 
ATOM   1999 O OG  . SER A 1 264 ? 108.321 105.112 115.063 1.00 45.80  ? 264 SER A OG  1 
ATOM   2000 N N   . SER A 1 265 ? 109.472 103.514 118.986 1.00 48.66  ? 265 SER A N   1 
ATOM   2001 C CA  . SER A 1 265 ? 109.905 103.373 120.374 1.00 50.42  ? 265 SER A CA  1 
ATOM   2002 C C   . SER A 1 265 ? 110.205 104.723 121.013 1.00 52.26  ? 265 SER A C   1 
ATOM   2003 O O   . SER A 1 265 ? 109.839 104.965 122.169 1.00 54.08  ? 265 SER A O   1 
ATOM   2004 C CB  . SER A 1 265 ? 111.131 102.465 120.450 1.00 50.49  ? 265 SER A CB  1 
ATOM   2005 O OG  . SER A 1 265 ? 112.245 103.064 119.814 1.00 50.71  ? 265 SER A OG  1 
ATOM   2006 N N   . SER A 1 266 ? 110.869 105.614 120.283 1.00 53.89  ? 266 SER A N   1 
ATOM   2007 C CA  . SER A 1 266 ? 111.224 106.928 120.794 1.00 54.23  ? 266 SER A CA  1 
ATOM   2008 C C   . SER A 1 266 ? 110.829 107.991 119.779 1.00 53.35  ? 266 SER A C   1 
ATOM   2009 O O   . SER A 1 266 ? 110.425 107.690 118.653 1.00 52.07  ? 266 SER A O   1 
ATOM   2010 C CB  . SER A 1 266 ? 112.723 107.020 121.111 1.00 55.39  ? 266 SER A CB  1 
ATOM   2011 O OG  . SER A 1 266 ? 113.060 108.307 121.596 1.00 56.94  ? 266 SER A OG  1 
ATOM   2012 N N   . ALA A 1 267 ? 110.938 109.254 120.199 1.00 52.74  ? 267 ALA A N   1 
ATOM   2013 C CA  . ALA A 1 267 ? 110.600 110.362 119.311 1.00 52.96  ? 267 ALA A CA  1 
ATOM   2014 C C   . ALA A 1 267 ? 111.570 110.458 118.139 1.00 52.87  ? 267 ALA A C   1 
ATOM   2015 O O   . ALA A 1 267 ? 111.155 110.716 117.004 1.00 54.04  ? 267 ALA A O   1 
ATOM   2016 C CB  . ALA A 1 267 ? 110.574 111.673 120.095 1.00 52.78  ? 267 ALA A CB  1 
ATOM   2017 N N   . THR A 1 268 ? 112.866 110.253 118.392 1.00 51.50  ? 268 THR A N   1 
ATOM   2018 C CA  . THR A 1 268 ? 113.864 110.387 117.335 1.00 50.28  ? 268 THR A CA  1 
ATOM   2019 C C   . THR A 1 268 ? 113.775 109.245 116.328 1.00 49.52  ? 268 THR A C   1 
ATOM   2020 O O   . THR A 1 268 ? 113.986 109.458 115.125 1.00 50.96  ? 268 THR A O   1 
ATOM   2021 C CB  . THR A 1 268 ? 115.263 110.455 117.952 1.00 50.05  ? 268 THR A CB  1 
ATOM   2022 O OG1 . THR A 1 268 ? 115.312 111.533 118.895 1.00 50.69  ? 268 THR A OG1 1 
ATOM   2023 C CG2 . THR A 1 268 ? 116.321 110.693 116.887 1.00 49.80  ? 268 THR A CG2 1 
ATOM   2024 N N   . TYR A 1 269 ? 113.427 108.042 116.789 1.00 47.85  ? 269 TYR A N   1 
ATOM   2025 C CA  . TYR A 1 269 ? 113.258 106.886 115.917 1.00 47.47  ? 269 TYR A CA  1 
ATOM   2026 C C   . TYR A 1 269 ? 111.966 106.939 115.118 1.00 46.84  ? 269 TYR A C   1 
ATOM   2027 O O   . TYR A 1 269 ? 111.661 105.986 114.397 1.00 46.44  ? 269 TYR A O   1 
ATOM   2028 C CB  . TYR A 1 269 ? 113.299 105.591 116.730 1.00 48.02  ? 269 TYR A CB  1 
ATOM   2029 C CG  . TYR A 1 269 ? 114.664 105.238 117.263 1.00 48.38  ? 269 TYR A CG  1 
ATOM   2030 C CD1 . TYR A 1 269 ? 115.813 105.718 116.653 1.00 48.63  ? 269 TYR A CD1 1 
ATOM   2031 C CD2 . TYR A 1 269 ? 114.805 104.412 118.369 1.00 48.56  ? 269 TYR A CD2 1 
ATOM   2032 C CE1 . TYR A 1 269 ? 117.065 105.395 117.135 1.00 49.76  ? 269 TYR A CE1 1 
ATOM   2033 C CE2 . TYR A 1 269 ? 116.052 104.082 118.858 1.00 49.08  ? 269 TYR A CE2 1 
ATOM   2034 C CZ  . TYR A 1 269 ? 117.179 104.576 118.237 1.00 50.28  ? 269 TYR A CZ  1 
ATOM   2035 O OH  . TYR A 1 269 ? 118.426 104.252 118.718 1.00 52.51  ? 269 TYR A OH  1 
ATOM   2036 N N   . ALA A 1 270 ? 111.196 108.015 115.256 1.00 45.83  ? 270 ALA A N   1 
ATOM   2037 C CA  . ALA A 1 270 ? 110.045 108.291 114.410 1.00 44.77  ? 270 ALA A CA  1 
ATOM   2038 C C   . ALA A 1 270 ? 110.435 109.170 113.226 1.00 43.91  ? 270 ALA A C   1 
ATOM   2039 O O   . ALA A 1 270 ? 110.117 108.855 112.074 1.00 43.66  ? 270 ALA A O   1 
ATOM   2040 C CB  . ALA A 1 270 ? 108.952 108.958 115.243 1.00 44.17  ? 270 ALA A CB  1 
ATOM   2041 N N   . GLN A 1 271 ? 111.141 110.267 113.504 1.00 42.66  ? 271 GLN A N   1 
ATOM   2042 C CA  . GLN A 1 271 ? 111.655 111.127 112.444 1.00 41.99  ? 271 GLN A CA  1 
ATOM   2043 C C   . GLN A 1 271 ? 112.669 110.390 111.574 1.00 41.09  ? 271 GLN A C   1 
ATOM   2044 O O   . GLN A 1 271 ? 112.648 110.508 110.338 1.00 41.65  ? 271 GLN A O   1 
ATOM   2045 C CB  . GLN A 1 271 ? 112.275 112.375 113.071 1.00 42.88  ? 271 GLN A CB  1 
ATOM   2046 C CG  . GLN A 1 271 ? 113.112 113.220 112.143 1.00 44.33  ? 271 GLN A CG  1 
ATOM   2047 C CD  . GLN A 1 271 ? 113.583 114.495 112.810 1.00 45.50  ? 271 GLN A CD  1 
ATOM   2048 O OE1 . GLN A 1 271 ? 112.867 115.084 113.620 1.00 45.85  ? 271 GLN A OE1 1 
ATOM   2049 N NE2 . GLN A 1 271 ? 114.794 114.927 112.477 1.00 45.99  ? 271 GLN A NE2 1 
ATOM   2050 N N   . VAL A 1 272 ? 113.559 109.612 112.198 1.00 40.22  ? 272 VAL A N   1 
ATOM   2051 C CA  . VAL A 1 272 ? 114.541 108.857 111.429 1.00 40.42  ? 272 VAL A CA  1 
ATOM   2052 C C   . VAL A 1 272 ? 113.850 107.778 110.604 1.00 41.37  ? 272 VAL A C   1 
ATOM   2053 O O   . VAL A 1 272 ? 114.237 107.508 109.461 1.00 42.49  ? 272 VAL A O   1 
ATOM   2054 C CB  . VAL A 1 272 ? 115.611 108.276 112.372 1.00 40.24  ? 272 VAL A CB  1 
ATOM   2055 C CG1 . VAL A 1 272 ? 116.464 107.236 111.667 1.00 40.61  ? 272 VAL A CG1 1 
ATOM   2056 C CG2 . VAL A 1 272 ? 116.477 109.388 112.924 1.00 40.21  ? 272 VAL A CG2 1 
ATOM   2057 N N   . LEU A 1 273 ? 112.795 107.171 111.156 1.00 41.62  ? 273 LEU A N   1 
ATOM   2058 C CA  . LEU A 1 273 ? 112.004 106.202 110.401 1.00 41.29  ? 273 LEU A CA  1 
ATOM   2059 C C   . LEU A 1 273 ? 111.357 106.852 109.184 1.00 41.21  ? 273 LEU A C   1 
ATOM   2060 O O   . LEU A 1 273 ? 111.335 106.263 108.095 1.00 41.08  ? 273 LEU A O   1 
ATOM   2061 C CB  . LEU A 1 273 ? 110.949 105.578 111.320 1.00 41.00  ? 273 LEU A CB  1 
ATOM   2062 C CG  . LEU A 1 273 ? 109.933 104.492 110.938 1.00 41.12  ? 273 LEU A CG  1 
ATOM   2063 C CD1 . LEU A 1 273 ? 109.407 103.870 112.213 1.00 41.31  ? 273 LEU A CD1 1 
ATOM   2064 C CD2 . LEU A 1 273 ? 108.753 105.017 110.136 1.00 41.00  ? 273 LEU A CD2 1 
ATOM   2065 N N   . SER A 1 274 ? 110.817 108.062 109.354 1.00 40.59  ? 274 SER A N   1 
ATOM   2066 C CA  . SER A 1 274 ? 110.188 108.759 108.237 1.00 39.74  ? 274 SER A CA  1 
ATOM   2067 C C   . SER A 1 274 ? 111.198 109.075 107.138 1.00 39.79  ? 274 SER A C   1 
ATOM   2068 O O   . SER A 1 274 ? 110.906 108.892 105.952 1.00 40.39  ? 274 SER A O   1 
ATOM   2069 C CB  . SER A 1 274 ? 109.505 110.034 108.728 1.00 39.07  ? 274 SER A CB  1 
ATOM   2070 O OG  . SER A 1 274 ? 108.272 109.735 109.358 1.00 38.85  ? 274 SER A OG  1 
ATOM   2071 N N   . PHE A 1 275 ? 112.399 109.529 107.511 1.00 39.20  ? 275 PHE A N   1 
ATOM   2072 C CA  . PHE A 1 275 ? 113.418 109.808 106.492 1.00 38.67  ? 275 PHE A CA  1 
ATOM   2073 C C   . PHE A 1 275 ? 113.885 108.528 105.799 1.00 39.78  ? 275 PHE A C   1 
ATOM   2074 O O   . PHE A 1 275 ? 114.068 108.500 104.570 1.00 40.58  ? 275 PHE A O   1 
ATOM   2075 C CB  . PHE A 1 275 ? 114.617 110.543 107.098 1.00 37.97  ? 275 PHE A CB  1 
ATOM   2076 C CG  . PHE A 1 275 ? 114.295 111.897 107.698 1.00 37.60  ? 275 PHE A CG  1 
ATOM   2077 C CD1 . PHE A 1 275 ? 113.055 112.495 107.533 1.00 37.11  ? 275 PHE A CD1 1 
ATOM   2078 C CD2 . PHE A 1 275 ? 115.257 112.575 108.425 1.00 37.67  ? 275 PHE A CD2 1 
ATOM   2079 C CE1 . PHE A 1 275 ? 112.782 113.729 108.084 1.00 37.08  ? 275 PHE A CE1 1 
ATOM   2080 C CE2 . PHE A 1 275 ? 114.988 113.811 108.978 1.00 37.35  ? 275 PHE A CE2 1 
ATOM   2081 C CZ  . PHE A 1 275 ? 113.749 114.388 108.806 1.00 37.16  ? 275 PHE A CZ  1 
ATOM   2082 N N   . LEU A 1 276 ? 114.070 107.454 106.570 1.00 41.18  ? 276 LEU A N   1 
ATOM   2083 C CA  . LEU A 1 276 ? 114.498 106.185 105.992 1.00 42.33  ? 276 LEU A CA  1 
ATOM   2084 C C   . LEU A 1 276 ? 113.462 105.651 105.012 1.00 41.46  ? 276 LEU A C   1 
ATOM   2085 O O   . LEU A 1 276 ? 113.811 105.118 103.953 1.00 40.90  ? 276 LEU A O   1 
ATOM   2086 C CB  . LEU A 1 276 ? 114.763 105.181 107.111 1.00 44.04  ? 276 LEU A CB  1 
ATOM   2087 C CG  . LEU A 1 276 ? 115.279 103.800 106.721 1.00 45.95  ? 276 LEU A CG  1 
ATOM   2088 C CD1 . LEU A 1 276 ? 116.632 103.904 106.042 1.00 46.84  ? 276 LEU A CD1 1 
ATOM   2089 C CD2 . LEU A 1 276 ? 115.357 102.919 107.958 1.00 46.28  ? 276 LEU A CD2 1 
ATOM   2090 N N   . ALA A 1 277 ? 112.179 105.805 105.338 1.00 40.76  ? 277 ALA A N   1 
ATOM   2091 C CA  . ALA A 1 277 ? 111.135 105.397 104.408 1.00 40.58  ? 277 ALA A CA  1 
ATOM   2092 C C   . ALA A 1 277 ? 111.040 106.333 103.210 1.00 40.22  ? 277 ALA A C   1 
ATOM   2093 O O   . ALA A 1 277 ? 110.671 105.896 102.116 1.00 39.99  ? 277 ALA A O   1 
ATOM   2094 C CB  . ALA A 1 277 ? 109.803 105.314 105.127 1.00 40.70  ? 277 ALA A CB  1 
ATOM   2095 N N   . ALA A 1 278 ? 111.348 107.618 103.391 1.00 40.20  ? 278 ALA A N   1 
ATOM   2096 C CA  . ALA A 1 278 ? 111.381 108.530 102.253 1.00 39.89  ? 278 ALA A CA  1 
ATOM   2097 C C   . ALA A 1 278 ? 112.497 108.186 101.281 1.00 39.77  ? 278 ALA A C   1 
ATOM   2098 O O   . ALA A 1 278 ? 112.414 108.546 100.103 1.00 39.63  ? 278 ALA A O   1 
ATOM   2099 C CB  . ALA A 1 278 ? 111.546 109.966 102.735 1.00 39.53  ? 278 ALA A CB  1 
ATOM   2100 N N   . PHE A 1 279 ? 113.540 107.512 101.756 1.00 39.88  ? 279 PHE A N   1 
ATOM   2101 C CA  . PHE A 1 279 ? 114.554 106.973 100.854 1.00 40.12  ? 279 PHE A CA  1 
ATOM   2102 C C   . PHE A 1 279 ? 114.114 105.645 100.243 1.00 40.21  ? 279 PHE A C   1 
ATOM   2103 O O   . PHE A 1 279 ? 114.322 105.398 99.041  1.00 41.47  ? 279 PHE A O   1 
ATOM   2104 C CB  . PHE A 1 279 ? 115.870 106.796 101.612 1.00 40.37  ? 279 PHE A CB  1 
ATOM   2105 C CG  . PHE A 1 279 ? 116.926 106.054 100.847 1.00 40.87  ? 279 PHE A CG  1 
ATOM   2106 C CD1 . PHE A 1 279 ? 117.500 106.604 99.713  1.00 41.01  ? 279 PHE A CD1 1 
ATOM   2107 C CD2 . PHE A 1 279 ? 117.363 104.814 101.278 1.00 41.21  ? 279 PHE A CD2 1 
ATOM   2108 C CE1 . PHE A 1 279 ? 118.484 105.924 99.017  1.00 41.10  ? 279 PHE A CE1 1 
ATOM   2109 C CE2 . PHE A 1 279 ? 118.344 104.131 100.587 1.00 41.26  ? 279 PHE A CE2 1 
ATOM   2110 C CZ  . PHE A 1 279 ? 118.906 104.686 99.457  1.00 41.33  ? 279 PHE A CZ  1 
ATOM   2111 N N   . GLY A 1 280 ? 113.484 104.799 101.060 1.00 39.53  ? 280 GLY A N   1 
ATOM   2112 C CA  . GLY A 1 280 ? 112.990 103.523 100.575 1.00 39.03  ? 280 GLY A CA  1 
ATOM   2113 C C   . GLY A 1 280 ? 111.935 103.648 99.494  1.00 38.54  ? 280 GLY A C   1 
ATOM   2114 O O   . GLY A 1 280 ? 111.835 102.784 98.624  1.00 38.23  ? 280 GLY A O   1 
ATOM   2115 N N   . CYS A 1 281 ? 111.129 104.712 99.535  1.00 38.16  ? 281 CYS A N   1 
ATOM   2116 C CA  . CYS A 1 281 ? 110.108 104.903 98.506  1.00 37.79  ? 281 CYS A CA  1 
ATOM   2117 C C   . CYS A 1 281 ? 110.732 105.127 97.132  1.00 37.55  ? 281 CYS A C   1 
ATOM   2118 O O   . CYS A 1 281 ? 110.277 104.549 96.139  1.00 37.73  ? 281 CYS A O   1 
ATOM   2119 C CB  . CYS A 1 281 ? 109.189 106.067 98.875  1.00 37.75  ? 281 CYS A CB  1 
ATOM   2120 S SG  . CYS A 1 281 ? 107.839 105.620 99.988  1.00 38.47  ? 281 CYS A SG  1 
ATOM   2121 N N   . LEU A 1 282 ? 111.777 105.955 97.053  1.00 37.55  ? 282 LEU A N   1 
ATOM   2122 C CA  . LEU A 1 282 ? 112.463 106.157 95.779  1.00 37.95  ? 282 LEU A CA  1 
ATOM   2123 C C   . LEU A 1 282 ? 113.176 104.888 95.327  1.00 38.85  ? 282 LEU A C   1 
ATOM   2124 O O   . LEU A 1 282 ? 113.160 104.549 94.130  1.00 39.78  ? 282 LEU A O   1 
ATOM   2125 C CB  . LEU A 1 282 ? 113.450 107.317 95.891  1.00 37.76  ? 282 LEU A CB  1 
ATOM   2126 C CG  . LEU A 1 282 ? 112.853 108.686 96.210  1.00 38.31  ? 282 LEU A CG  1 
ATOM   2127 C CD1 . LEU A 1 282 ? 113.913 109.765 96.096  1.00 38.27  ? 282 LEU A CD1 1 
ATOM   2128 C CD2 . LEU A 1 282 ? 111.692 108.980 95.279  1.00 39.01  ? 282 LEU A CD2 1 
ATOM   2129 N N   . VAL A 1 283 ? 113.798 104.171 96.272  1.00 40.11  ? 283 VAL A N   1 
ATOM   2130 C CA  . VAL A 1 283 ? 114.432 102.895 95.933  1.00 40.97  ? 283 VAL A CA  1 
ATOM   2131 C C   . VAL A 1 283 ? 113.403 101.917 95.373  1.00 42.52  ? 283 VAL A C   1 
ATOM   2132 O O   . VAL A 1 283 ? 113.682 101.173 94.425  1.00 41.75  ? 283 VAL A O   1 
ATOM   2133 C CB  . VAL A 1 283 ? 115.163 102.319 97.161  1.00 40.36  ? 283 VAL A CB  1 
ATOM   2134 C CG1 . VAL A 1 283 ? 115.732 100.943 96.860  1.00 40.28  ? 283 VAL A CG1 1 
ATOM   2135 C CG2 . VAL A 1 283 ? 116.275 103.247 97.581  1.00 39.94  ? 283 VAL A CG2 1 
ATOM   2136 N N   . MET A 1 284 ? 112.192 101.920 95.931  1.00 44.29  ? 284 MET A N   1 
ATOM   2137 C CA  . MET A 1 284 ? 111.145 101.014 95.481  1.00 44.86  ? 284 MET A CA  1 
ATOM   2138 C C   . MET A 1 284 ? 110.511 101.459 94.173  1.00 43.90  ? 284 MET A C   1 
ATOM   2139 O O   . MET A 1 284 ? 110.001 100.617 93.427  1.00 42.61  ? 284 MET A O   1 
ATOM   2140 C CB  . MET A 1 284 ? 110.053 100.913 96.545  1.00 46.69  ? 284 MET A CB  1 
ATOM   2141 C CG  . MET A 1 284 ? 110.318 99.845  97.566  1.00 48.32  ? 284 MET A CG  1 
ATOM   2142 S SD  . MET A 1 284 ? 110.605 98.236  96.838  1.00 50.59  ? 284 MET A SD  1 
ATOM   2143 C CE  . MET A 1 284 ? 111.687 97.568  98.088  1.00 50.89  ? 284 MET A CE  1 
ATOM   2144 N N   . ALA A 1 285 ? 110.530 102.760 93.887  1.00 43.54  ? 285 ALA A N   1 
ATOM   2145 C CA  . ALA A 1 285 ? 109.893 103.308 92.701  1.00 42.94  ? 285 ALA A CA  1 
ATOM   2146 C C   . ALA A 1 285 ? 110.786 103.300 91.472  1.00 42.59  ? 285 ALA A C   1 
ATOM   2147 O O   . ALA A 1 285 ? 110.268 103.436 90.358  1.00 42.50  ? 285 ALA A O   1 
ATOM   2148 C CB  . ALA A 1 285 ? 109.433 104.740 92.969  1.00 42.67  ? 285 ALA A CB  1 
ATOM   2149 N N   . ILE A 1 286 ? 112.107 103.182 91.647  1.00 42.59  ? 286 ILE A N   1 
ATOM   2150 C CA  . ILE A 1 286 ? 113.000 103.061 90.485  1.00 42.75  ? 286 ILE A CA  1 
ATOM   2151 C C   . ILE A 1 286 ? 112.634 101.888 89.571  1.00 43.58  ? 286 ILE A C   1 
ATOM   2152 O O   . ILE A 1 286 ? 112.583 102.088 88.344  1.00 44.37  ? 286 ILE A O   1 
ATOM   2153 C CB  . ILE A 1 286 ? 114.467 103.033 90.948  1.00 42.35  ? 286 ILE A CB  1 
ATOM   2154 C CG1 . ILE A 1 286 ? 114.936 104.445 91.300  1.00 42.88  ? 286 ILE A CG1 1 
ATOM   2155 C CG2 . ILE A 1 286 ? 115.371 102.427 89.882  1.00 41.98  ? 286 ILE A CG2 1 
ATOM   2156 C CD1 . ILE A 1 286 ? 116.376 104.518 91.754  1.00 43.14  ? 286 ILE A CD1 1 
ATOM   2157 N N   . PRO A 1 287 ? 112.367 100.666 90.072  1.00 44.28  ? 287 PRO A N   1 
ATOM   2158 C CA  . PRO A 1 287 ? 111.929 99.599  89.150  1.00 43.95  ? 287 PRO A CA  1 
ATOM   2159 C C   . PRO A 1 287 ? 110.632 99.896  88.423  1.00 43.54  ? 287 PRO A C   1 
ATOM   2160 O O   . PRO A 1 287 ? 110.481 99.481  87.268  1.00 43.69  ? 287 PRO A O   1 
ATOM   2161 C CB  . PRO A 1 287 ? 111.772 98.380  90.067  1.00 44.80  ? 287 PRO A CB  1 
ATOM   2162 C CG  . PRO A 1 287 ? 112.656 98.638  91.185  1.00 45.53  ? 287 PRO A CG  1 
ATOM   2163 C CD  . PRO A 1 287 ? 112.604 100.111 91.420  1.00 45.11  ? 287 PRO A CD  1 
ATOM   2164 N N   . ALA A 1 288 ? 109.683 100.585 89.063  1.00 43.24  ? 288 ALA A N   1 
ATOM   2165 C CA  . ALA A 1 288 ? 108.431 100.917 88.390  1.00 42.77  ? 288 ALA A CA  1 
ATOM   2166 C C   . ALA A 1 288 ? 108.670 101.851 87.212  1.00 41.69  ? 288 ALA A C   1 
ATOM   2167 O O   . ALA A 1 288 ? 108.106 101.655 86.129  1.00 42.01  ? 288 ALA A O   1 
ATOM   2168 C CB  . ALA A 1 288 ? 107.454 101.546 89.381  1.00 43.03  ? 288 ALA A CB  1 
ATOM   2169 N N   . ILE A 1 289 ? 109.520 102.863 87.405  1.00 40.32  ? 289 ILE A N   1 
ATOM   2170 C CA  . ILE A 1 289 ? 109.867 103.780 86.324  1.00 39.62  ? 289 ILE A CA  1 
ATOM   2171 C C   . ILE A 1 289 ? 110.582 103.035 85.206  1.00 39.28  ? 289 ILE A C   1 
ATOM   2172 O O   . ILE A 1 289 ? 110.305 103.252 84.018  1.00 39.00  ? 289 ILE A O   1 
ATOM   2173 C CB  . ILE A 1 289 ? 110.714 104.945 86.871  1.00 39.43  ? 289 ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 289 ? 109.832 105.929 87.638  1.00 39.35  ? 289 ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 289 ? 111.449 105.664 85.754  1.00 39.37  ? 289 ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 289 ? 110.595 107.079 88.251  1.00 39.54  ? 289 ILE A CD1 1 
ATOM   2177 N N   . LEU A 1 290 ? 111.501 102.132 85.565  1.00 39.61  ? 290 LEU A N   1 
ATOM   2178 C CA  . LEU A 1 290 ? 112.223 101.377 84.543  1.00 40.20  ? 290 LEU A CA  1 
ATOM   2179 C C   . LEU A 1 290 ? 111.289 100.482 83.733  1.00 41.17  ? 290 LEU A C   1 
ATOM   2180 O O   . LEU A 1 290 ? 111.408 100.408 82.505  1.00 42.26  ? 290 LEU A O   1 
ATOM   2181 C CB  . LEU A 1 290 ? 113.338 100.553 85.182  1.00 40.07  ? 290 LEU A CB  1 
ATOM   2182 C CG  . LEU A 1 290 ? 114.690 101.262 85.256  1.00 40.19  ? 290 LEU A CG  1 
ATOM   2183 C CD1 . LEU A 1 290 ? 115.748 100.343 85.839  1.00 40.86  ? 290 LEU A CD1 1 
ATOM   2184 C CD2 . LEU A 1 290 ? 115.102 101.755 83.880  1.00 39.99  ? 290 LEU A CD2 1 
ATOM   2185 N N   . ILE A 1 291 ? 110.347 99.804  84.394  1.00 41.18  ? 291 ILE A N   1 
ATOM   2186 C CA  . ILE A 1 291 ? 109.424 98.926  83.675  1.00 40.12  ? 291 ILE A CA  1 
ATOM   2187 C C   . ILE A 1 291 ? 108.466 99.743  82.812  1.00 39.82  ? 291 ILE A C   1 
ATOM   2188 O O   . ILE A 1 291 ? 108.113 99.335  81.698  1.00 39.50  ? 291 ILE A O   1 
ATOM   2189 C CB  . ILE A 1 291 ? 108.677 98.005  84.658  1.00 39.74  ? 291 ILE A CB  1 
ATOM   2190 C CG1 . ILE A 1 291 ? 109.658 97.040  85.323  1.00 39.93  ? 291 ILE A CG1 1 
ATOM   2191 C CG2 . ILE A 1 291 ? 107.614 97.198  83.940  1.00 39.59  ? 291 ILE A CG2 1 
ATOM   2192 C CD1 . ILE A 1 291 ? 109.005 96.030  86.240  1.00 40.09  ? 291 ILE A CD1 1 
ATOM   2193 N N   . GLY A 1 292 ? 108.035 100.909 83.301  1.00 39.64  ? 292 GLY A N   1 
ATOM   2194 C CA  . GLY A 1 292 ? 107.226 101.788 82.471  1.00 39.36  ? 292 GLY A CA  1 
ATOM   2195 C C   . GLY A 1 292 ? 107.961 102.257 81.230  1.00 39.25  ? 292 GLY A C   1 
ATOM   2196 O O   . GLY A 1 292 ? 107.388 102.309 80.139  1.00 38.86  ? 292 GLY A O   1 
ATOM   2197 N N   . ALA A 1 293 ? 109.246 102.589 81.375  1.00 39.85  ? 293 ALA A N   1 
ATOM   2198 C CA  . ALA A 1 293 ? 110.045 102.982 80.218  1.00 41.08  ? 293 ALA A CA  1 
ATOM   2199 C C   . ALA A 1 293 ? 110.241 101.817 79.255  1.00 42.03  ? 293 ALA A C   1 
ATOM   2200 O O   . ALA A 1 293 ? 110.251 102.010 78.033  1.00 42.90  ? 293 ALA A O   1 
ATOM   2201 C CB  . ALA A 1 293 ? 111.393 103.533 80.675  1.00 41.57  ? 293 ALA A CB  1 
ATOM   2202 N N   . ILE A 1 294 ? 110.411 100.604 79.790  1.00 42.87  ? 294 ILE A N   1 
ATOM   2203 C CA  . ILE A 1 294 ? 110.515 99.411  78.951  1.00 43.67  ? 294 ILE A CA  1 
ATOM   2204 C C   . ILE A 1 294 ? 109.237 99.212  78.146  1.00 45.34  ? 294 ILE A C   1 
ATOM   2205 O O   . ILE A 1 294 ? 109.281 98.938  76.940  1.00 45.48  ? 294 ILE A O   1 
ATOM   2206 C CB  . ILE A 1 294 ? 110.831 98.178  79.818  1.00 43.27  ? 294 ILE A CB  1 
ATOM   2207 C CG1 . ILE A 1 294 ? 112.261 98.239  80.346  1.00 44.12  ? 294 ILE A CG1 1 
ATOM   2208 C CG2 . ILE A 1 294 ? 110.615 96.897  79.042  1.00 42.62  ? 294 ILE A CG2 1 
ATOM   2209 C CD1 . ILE A 1 294 ? 112.495 97.341  81.537  1.00 44.38  ? 294 ILE A CD1 1 
ATOM   2210 N N   . GLY A 1 295 ? 108.083 99.357  78.798  1.00 47.53  ? 295 GLY A N   1 
ATOM   2211 C CA  . GLY A 1 295 ? 106.820 99.230  78.089  1.00 48.65  ? 295 GLY A CA  1 
ATOM   2212 C C   . GLY A 1 295 ? 106.616 100.320 77.054  1.00 49.50  ? 295 GLY A C   1 
ATOM   2213 O O   . GLY A 1 295 ? 106.028 100.081 75.996  1.00 49.77  ? 295 GLY A O   1 
ATOM   2214 N N   . ALA A 1 296 ? 107.091 101.534 77.348  1.00 50.26  ? 296 ALA A N   1 
ATOM   2215 C CA  . ALA A 1 296 ? 106.994 102.621 76.379  1.00 50.49  ? 296 ALA A CA  1 
ATOM   2216 C C   . ALA A 1 296 ? 107.879 102.368 75.165  1.00 50.79  ? 296 ALA A C   1 
ATOM   2217 O O   . ALA A 1 296 ? 107.494 102.683 74.033  1.00 51.00  ? 296 ALA A O   1 
ATOM   2218 C CB  . ALA A 1 296 ? 107.361 103.949 77.039  1.00 50.21  ? 296 ALA A CB  1 
ATOM   2219 N N   . SER A 1 297 ? 109.070 101.808 75.377  1.00 51.30  ? 297 SER A N   1 
ATOM   2220 C CA  . SER A 1 297 ? 110.010 101.580 74.287  1.00 52.58  ? 297 SER A CA  1 
ATOM   2221 C C   . SER A 1 297 ? 109.754 100.286 73.525  1.00 54.06  ? 297 SER A C   1 
ATOM   2222 O O   . SER A 1 297 ? 110.343 100.094 72.457  1.00 55.53  ? 297 SER A O   1 
ATOM   2223 C CB  . SER A 1 297 ? 111.441 101.571 74.825  1.00 52.26  ? 297 SER A CB  1 
ATOM   2224 O OG  . SER A 1 297 ? 111.777 102.824 75.388  1.00 52.68  ? 297 SER A OG  1 
ATOM   2225 N N   . THR A 1 298 ? 108.902 99.402  74.039  1.00 55.33  ? 298 THR A N   1 
ATOM   2226 C CA  . THR A 1 298 ? 108.725 98.090  73.429  1.00 57.06  ? 298 THR A CA  1 
ATOM   2227 C C   . THR A 1 298 ? 107.935 98.197  72.131  1.00 57.73  ? 298 THR A C   1 
ATOM   2228 O O   . THR A 1 298 ? 106.911 98.884  72.069  1.00 58.29  ? 298 THR A O   1 
ATOM   2229 C CB  . THR A 1 298 ? 108.012 97.147  74.397  1.00 57.72  ? 298 THR A CB  1 
ATOM   2230 O OG1 . THR A 1 298 ? 108.671 97.174  75.668  1.00 59.89  ? 298 THR A OG1 1 
ATOM   2231 C CG2 . THR A 1 298 ? 108.030 95.722  73.866  1.00 57.46  ? 298 THR A CG2 1 
ATOM   2232 N N   . ASP A 1 299 ? 108.414 97.517  71.092  1.00 58.84  ? 299 ASP A N   1 
ATOM   2233 C CA  . ASP A 1 299 ? 107.672 97.366  69.842  1.00 59.90  ? 299 ASP A CA  1 
ATOM   2234 C C   . ASP A 1 299 ? 106.738 96.178  70.023  1.00 59.12  ? 299 ASP A C   1 
ATOM   2235 O O   . ASP A 1 299 ? 107.169 95.023  69.990  1.00 60.78  ? 299 ASP A O   1 
ATOM   2236 C CB  . ASP A 1 299 ? 108.622 97.166  68.667  1.00 61.78  ? 299 ASP A CB  1 
ATOM   2237 C CG  . ASP A 1 299 ? 107.929 97.294  67.323  1.00 63.41  ? 299 ASP A CG  1 
ATOM   2238 O OD1 . ASP A 1 299 ? 106.708 97.556  67.297  1.00 64.73  ? 299 ASP A OD1 1 
ATOM   2239 O OD2 . ASP A 1 299 ? 108.607 97.130  66.288  1.00 64.76  ? 299 ASP A OD2 1 
ATOM   2240 N N   . TRP A 1 300 ? 105.447 96.459  70.210  1.00 56.22  ? 300 TRP A N   1 
ATOM   2241 C CA  . TRP A 1 300 ? 104.500 95.420  70.594  1.00 54.43  ? 300 TRP A CA  1 
ATOM   2242 C C   . TRP A 1 300 ? 104.174 94.454  69.464  1.00 56.23  ? 300 TRP A C   1 
ATOM   2243 O O   . TRP A 1 300 ? 103.577 93.405  69.728  1.00 57.48  ? 300 TRP A O   1 
ATOM   2244 C CB  . TRP A 1 300 ? 103.214 96.056  71.120  1.00 51.67  ? 300 TRP A CB  1 
ATOM   2245 C CG  . TRP A 1 300 ? 103.409 96.774  72.414  1.00 49.38  ? 300 TRP A CG  1 
ATOM   2246 C CD1 . TRP A 1 300 ? 103.496 98.122  72.597  1.00 48.60  ? 300 TRP A CD1 1 
ATOM   2247 C CD2 . TRP A 1 300 ? 103.568 96.183  73.708  1.00 48.09  ? 300 TRP A CD2 1 
ATOM   2248 N NE1 . TRP A 1 300 ? 103.685 98.408  73.926  1.00 48.31  ? 300 TRP A NE1 1 
ATOM   2249 C CE2 . TRP A 1 300 ? 103.735 97.234  74.629  1.00 47.98  ? 300 TRP A CE2 1 
ATOM   2250 C CE3 . TRP A 1 300 ? 103.581 94.868  74.178  1.00 47.95  ? 300 TRP A CE3 1 
ATOM   2251 C CZ2 . TRP A 1 300 ? 103.911 97.010  75.991  1.00 47.75  ? 300 TRP A CZ2 1 
ATOM   2252 C CZ3 . TRP A 1 300 ? 103.756 94.649  75.529  1.00 47.93  ? 300 TRP A CZ3 1 
ATOM   2253 C CH2 . TRP A 1 300 ? 103.919 95.714  76.420  1.00 47.62  ? 300 TRP A CH2 1 
ATOM   2254 N N   . ASN A 1 301 ? 104.540 94.775  68.222  1.00 57.97  ? 301 ASN A N   1 
ATOM   2255 C CA  . ASN A 1 301 ? 104.320 93.836  67.127  1.00 59.91  ? 301 ASN A CA  1 
ATOM   2256 C C   . ASN A 1 301 ? 105.227 92.618  67.250  1.00 63.45  ? 301 ASN A C   1 
ATOM   2257 O O   . ASN A 1 301 ? 104.823 91.506  66.891  1.00 65.06  ? 301 ASN A O   1 
ATOM   2258 C CB  . ASN A 1 301 ? 104.542 94.537  65.786  1.00 59.05  ? 301 ASN A CB  1 
ATOM   2259 C CG  . ASN A 1 301 ? 103.966 93.762  64.615  1.00 58.80  ? 301 ASN A CG  1 
ATOM   2260 O OD1 . ASN A 1 301 ? 103.347 92.713  64.790  1.00 58.25  ? 301 ASN A OD1 1 
ATOM   2261 N ND2 . ASN A 1 301 ? 104.168 94.280  63.409  1.00 58.91  ? 301 ASN A ND2 1 
ATOM   2262 N N   . GLN A 1 302 ? 106.449 92.804  67.757  1.00 66.53  ? 302 GLN A N   1 
ATOM   2263 C CA  . GLN A 1 302 ? 107.383 91.689  67.884  1.00 68.02  ? 302 GLN A CA  1 
ATOM   2264 C C   . GLN A 1 302 ? 106.952 90.720  68.979  1.00 68.01  ? 302 GLN A C   1 
ATOM   2265 O O   . GLN A 1 302 ? 107.155 89.507  68.855  1.00 68.00  ? 302 GLN A O   1 
ATOM   2266 C CB  . GLN A 1 302 ? 108.792 92.215  68.162  1.00 68.75  ? 302 GLN A CB  1 
ATOM   2267 C CG  . GLN A 1 302 ? 109.341 93.181  67.114  1.00 70.30  ? 302 GLN A CG  1 
ATOM   2268 C CD  . GLN A 1 302 ? 109.488 92.565  65.731  1.00 72.52  ? 302 GLN A CD  1 
ATOM   2269 O OE1 . GLN A 1 302 ? 109.543 91.345  65.576  1.00 73.12  ? 302 GLN A OE1 1 
ATOM   2270 N NE2 . GLN A 1 302 ? 109.553 93.417  64.715  1.00 74.26  ? 302 GLN A NE2 1 
ATOM   2271 N N   . THR A 1 303 ? 106.362 91.232  70.055  1.00 68.19  ? 303 THR A N   1 
ATOM   2272 C CA  . THR A 1 303 ? 105.978 90.396  71.181  1.00 69.09  ? 303 THR A CA  1 
ATOM   2273 C C   . THR A 1 303 ? 104.724 89.589  70.854  1.00 69.74  ? 303 THR A C   1 
ATOM   2274 O O   . THR A 1 303 ? 104.085 89.764  69.813  1.00 68.68  ? 303 THR A O   1 
ATOM   2275 C CB  . THR A 1 303 ? 105.743 91.246  72.428  1.00 68.77  ? 303 THR A CB  1 
ATOM   2276 O OG1 . THR A 1 303 ? 104.497 91.941  72.304  1.00 70.29  ? 303 THR A OG1 1 
ATOM   2277 C CG2 . THR A 1 303 ? 106.857 92.257  72.593  1.00 68.38  ? 303 THR A CG2 1 
ATOM   2278 N N   . ALA A 1 304 ? 104.372 88.687  71.772  1.00 71.00  ? 304 ALA A N   1 
ATOM   2279 C CA  . ALA A 1 304 ? 103.173 87.873  71.615  1.00 70.90  ? 304 ALA A CA  1 
ATOM   2280 C C   . ALA A 1 304 ? 101.891 88.666  71.827  1.00 71.04  ? 304 ALA A C   1 
ATOM   2281 O O   . ALA A 1 304 ? 100.815 88.173  71.470  1.00 72.63  ? 304 ALA A O   1 
ATOM   2282 C CB  . ALA A 1 304 ? 103.213 86.688  72.581  1.00 70.91  ? 304 ALA A CB  1 
ATOM   2283 N N   . TYR A 1 305 ? 101.977 89.865  72.409  1.00 70.01  ? 305 TYR A N   1 
ATOM   2284 C CA  . TYR A 1 305 ? 100.795 90.708  72.562  1.00 69.38  ? 305 TYR A CA  1 
ATOM   2285 C C   . TYR A 1 305 ? 100.249 91.137  71.207  1.00 72.04  ? 305 TYR A C   1 
ATOM   2286 O O   . TYR A 1 305 ? 99.031  91.158  70.997  1.00 72.85  ? 305 TYR A O   1 
ATOM   2287 C CB  . TYR A 1 305 ? 101.138 91.928  73.419  1.00 67.75  ? 305 TYR A CB  1 
ATOM   2288 C CG  . TYR A 1 305 ? 99.946  92.714  73.920  1.00 67.20  ? 305 TYR A CG  1 
ATOM   2289 C CD1 . TYR A 1 305 ? 99.309  93.647  73.114  1.00 66.93  ? 305 TYR A CD1 1 
ATOM   2290 C CD2 . TYR A 1 305 ? 99.461  92.523  75.205  1.00 67.39  ? 305 TYR A CD2 1 
ATOM   2291 C CE1 . TYR A 1 305 ? 98.223  94.363  73.572  1.00 67.45  ? 305 TYR A CE1 1 
ATOM   2292 C CE2 . TYR A 1 305 ? 98.375  93.235  75.673  1.00 67.13  ? 305 TYR A CE2 1 
ATOM   2293 C CZ  . TYR A 1 305 ? 97.761  94.153  74.852  1.00 67.39  ? 305 TYR A CZ  1 
ATOM   2294 O OH  . TYR A 1 305 ? 96.679  94.864  75.314  1.00 67.53  ? 305 TYR A OH  1 
ATOM   2295 N N   . GLY A 1 306 ? 101.133 91.486  70.278  1.00 75.20  ? 306 GLY A N   1 
ATOM   2296 C CA  . GLY A 1 306 ? 100.715 91.906  68.959  1.00 76.06  ? 306 GLY A CA  1 
ATOM   2297 C C   . GLY A 1 306 ? 100.226 93.340  68.937  1.00 77.08  ? 306 GLY A C   1 
ATOM   2298 O O   . GLY A 1 306 ? 100.161 94.037  69.950  1.00 77.65  ? 306 GLY A O   1 
ATOM   2299 N N   . LEU A 1 307 ? 99.869  93.781  67.737  1.00 77.03  ? 307 LEU A N   1 
ATOM   2300 C CA  . LEU A 1 307 ? 99.335  95.097  67.427  1.00 76.52  ? 307 LEU A CA  1 
ATOM   2301 C C   . LEU A 1 307 ? 97.813  95.037  67.398  1.00 75.41  ? 307 LEU A C   1 
ATOM   2302 O O   . LEU A 1 307 ? 97.244  94.059  66.900  1.00 75.01  ? 307 LEU A O   1 
ATOM   2303 C CB  . LEU A 1 307 ? 99.871  95.576  66.074  1.00 76.88  ? 307 LEU A CB  1 
ATOM   2304 C CG  . LEU A 1 307 ? 99.757  97.038  65.631  1.00 77.75  ? 307 LEU A CG  1 
ATOM   2305 C CD1 . LEU A 1 307 ? 100.976 97.432  64.814  1.00 78.12  ? 307 LEU A CD1 1 
ATOM   2306 C CD2 . LEU A 1 307 ? 98.488  97.275  64.826  1.00 77.87  ? 307 LEU A CD2 1 
ATOM   2307 N N   . PRO A 1 308 ? 97.088  96.045  67.912  1.00 73.99  ? 308 PRO A N   1 
ATOM   2308 C CA  . PRO A 1 308 ? 97.518  97.339  68.460  1.00 73.07  ? 308 PRO A CA  1 
ATOM   2309 C C   . PRO A 1 308 ? 98.176  97.299  69.840  1.00 71.65  ? 308 PRO A C   1 
ATOM   2310 O O   . PRO A 1 308 ? 97.996  96.356  70.608  1.00 70.61  ? 308 PRO A O   1 
ATOM   2311 C CB  . PRO A 1 308 ? 96.208  98.127  68.530  1.00 73.29  ? 308 PRO A CB  1 
ATOM   2312 C CG  . PRO A 1 308 ? 95.176  97.088  68.731  1.00 73.58  ? 308 PRO A CG  1 
ATOM   2313 C CD  . PRO A 1 308 ? 95.619  95.933  67.889  1.00 73.46  ? 308 PRO A CD  1 
ATOM   2314 N N   . ASP A 1 309 ? 98.939  98.352  70.127  1.00 70.18  ? 309 ASP A N   1 
ATOM   2315 C CA  . ASP A 1 309 ? 99.594  98.524  71.410  1.00 69.31  ? 309 ASP A CA  1 
ATOM   2316 C C   . ASP A 1 309 ? 98.561  98.782  72.513  1.00 65.54  ? 309 ASP A C   1 
ATOM   2317 O O   . ASP A 1 309 ? 97.426  99.168  72.225  1.00 64.94  ? 309 ASP A O   1 
ATOM   2318 C CB  . ASP A 1 309 ? 100.614 99.661  71.306  1.00 72.46  ? 309 ASP A CB  1 
ATOM   2319 C CG  . ASP A 1 309 ? 100.008 100.955 70.794  1.00 76.12  ? 309 ASP A CG  1 
ATOM   2320 O OD1 . ASP A 1 309 ? 98.810  100.970 70.450  1.00 79.82  ? 309 ASP A OD1 1 
ATOM   2321 O OD2 . ASP A 1 309 ? 100.743 101.961 70.723  1.00 79.23  ? 309 ASP A OD2 1 
ATOM   2322 N N   . PRO A 1 310 ? 98.922  98.537  73.783  1.00 63.08  ? 310 PRO A N   1 
ATOM   2323 C CA  . PRO A 1 310 ? 97.923  98.647  74.863  1.00 63.52  ? 310 PRO A CA  1 
ATOM   2324 C C   . PRO A 1 310 ? 97.286  100.019 75.017  1.00 65.13  ? 310 PRO A C   1 
ATOM   2325 O O   . PRO A 1 310 ? 96.124  100.097 75.437  1.00 68.49  ? 310 PRO A O   1 
ATOM   2326 C CB  . PRO A 1 310 ? 98.725  98.267  76.114  1.00 62.10  ? 310 PRO A CB  1 
ATOM   2327 C CG  . PRO A 1 310 ? 99.780  97.377  75.609  1.00 62.17  ? 310 PRO A CG  1 
ATOM   2328 C CD  . PRO A 1 310 ? 100.179 97.953  74.286  1.00 62.76  ? 310 PRO A CD  1 
ATOM   2329 N N   . LYS A 1 311 ? 97.997  101.105 74.703  1.00 64.15  ? 311 LYS A N   1 
ATOM   2330 C CA  . LYS A 1 311 ? 97.394  102.426 74.847  1.00 63.03  ? 311 LYS A CA  1 
ATOM   2331 C C   . LYS A 1 311 ? 96.294  102.678 73.823  1.00 63.76  ? 311 LYS A C   1 
ATOM   2332 O O   . LYS A 1 311 ? 95.442  103.543 74.051  1.00 64.52  ? 311 LYS A O   1 
ATOM   2333 C CB  . LYS A 1 311 ? 98.463  103.517 74.760  1.00 62.23  ? 311 LYS A CB  1 
ATOM   2334 C CG  . LYS A 1 311 ? 99.162  103.632 73.420  1.00 61.91  ? 311 LYS A CG  1 
ATOM   2335 C CD  . LYS A 1 311 ? 100.171 104.768 73.446  1.00 62.12  ? 311 LYS A CD  1 
ATOM   2336 C CE  . LYS A 1 311 ? 100.833 104.961 72.096  1.00 62.43  ? 311 LYS A CE  1 
ATOM   2337 N NZ  . LYS A 1 311 ? 101.741 103.831 71.764  1.00 63.14  ? 311 LYS A NZ  1 
ATOM   2338 N N   . THR A 1 312 ? 96.290  101.948 72.705  1.00 64.32  ? 312 THR A N   1 
ATOM   2339 C CA  . THR A 1 312 ? 95.189  102.063 71.754  1.00 64.65  ? 312 THR A CA  1 
ATOM   2340 C C   . THR A 1 312 ? 93.932  101.382 72.285  1.00 65.79  ? 312 THR A C   1 
ATOM   2341 O O   . THR A 1 312 ? 92.830  101.938 72.191  1.00 66.13  ? 312 THR A O   1 
ATOM   2342 C CB  . THR A 1 312 ? 95.599  101.472 70.403  1.00 64.22  ? 312 THR A CB  1 
ATOM   2343 O OG1 . THR A 1 312 ? 96.581  102.317 69.791  1.00 65.79  ? 312 THR A OG1 1 
ATOM   2344 C CG2 . THR A 1 312 ? 94.402  101.351 69.471  1.00 63.18  ? 312 THR A CG2 1 
ATOM   2345 N N   . THR A 1 313 ? 94.078  100.194 72.875  1.00 67.89  ? 313 THR A N   1 
ATOM   2346 C CA  . THR A 1 313 ? 92.952  99.430  73.400  1.00 69.28  ? 313 THR A CA  1 
ATOM   2347 C C   . THR A 1 313 ? 92.511  99.887  74.787  1.00 70.72  ? 313 THR A C   1 
ATOM   2348 O O   . THR A 1 313 ? 91.807  99.130  75.468  1.00 71.35  ? 313 THR A O   1 
ATOM   2349 C CB  . THR A 1 313 ? 93.292  97.938  73.439  1.00 68.86  ? 313 THR A CB  1 
ATOM   2350 O OG1 . THR A 1 313 ? 94.410  97.722  74.308  1.00 70.35  ? 313 THR A OG1 1 
ATOM   2351 C CG2 . THR A 1 313 ? 93.633  97.432  72.051  1.00 67.64  ? 313 THR A CG2 1 
ATOM   2352 N N   . GLU A 1 314 ? 92.924  101.087 75.209  1.00 71.87  ? 314 GLU A N   1 
ATOM   2353 C CA  . GLU A 1 314 ? 92.536  101.685 76.489  1.00 72.67  ? 314 GLU A CA  1 
ATOM   2354 C C   . GLU A 1 314 ? 92.948  100.819 77.678  1.00 71.30  ? 314 GLU A C   1 
ATOM   2355 O O   . GLU A 1 314 ? 92.287  100.820 78.719  1.00 71.09  ? 314 GLU A O   1 
ATOM   2356 C CB  . GLU A 1 314 ? 91.033  101.983 76.534  1.00 75.03  ? 314 GLU A CB  1 
ATOM   2357 C CG  . GLU A 1 314 ? 90.591  103.058 75.554  1.00 77.13  ? 314 GLU A CG  1 
ATOM   2358 C CD  . GLU A 1 314 ? 89.096  103.308 75.596  1.00 80.41  ? 314 GLU A CD  1 
ATOM   2359 O OE1 . GLU A 1 314 ? 88.387  102.563 76.303  1.00 84.63  ? 314 GLU A OE1 1 
ATOM   2360 O OE2 . GLU A 1 314 ? 88.631  104.250 74.920  1.00 82.70  ? 314 GLU A OE2 1 
ATOM   2361 N N   . GLU A 1 315 ? 94.045  100.076 77.532  1.00 68.99  ? 315 GLU A N   1 
ATOM   2362 C CA  . GLU A 1 315 ? 94.626  99.304  78.622  1.00 67.63  ? 315 GLU A CA  1 
ATOM   2363 C C   . GLU A 1 315 ? 95.895  99.951  79.162  1.00 65.46  ? 315 GLU A C   1 
ATOM   2364 O O   . GLU A 1 315 ? 96.717  99.272  79.784  1.00 64.76  ? 315 GLU A O   1 
ATOM   2365 C CB  . GLU A 1 315 ? 94.914  97.870  78.176  1.00 68.82  ? 315 GLU A CB  1 
ATOM   2366 C CG  . GLU A 1 315 ? 93.675  97.048  77.876  1.00 70.88  ? 315 GLU A CG  1 
ATOM   2367 C CD  . GLU A 1 315 ? 94.009  95.642  77.421  1.00 74.35  ? 315 GLU A CD  1 
ATOM   2368 O OE1 . GLU A 1 315 ? 95.206  95.348  77.221  1.00 76.35  ? 315 GLU A OE1 1 
ATOM   2369 O OE2 . GLU A 1 315 ? 93.074  94.828  77.264  1.00 78.47  ? 315 GLU A OE2 1 
ATOM   2370 N N   . ALA A 1 316 ? 96.071  101.254 78.931  1.00 63.51  ? 316 ALA A N   1 
ATOM   2371 C CA  . ALA A 1 316 ? 97.266  101.946 79.392  1.00 62.61  ? 316 ALA A CA  1 
ATOM   2372 C C   . ALA A 1 316 ? 97.323  102.068 80.908  1.00 61.87  ? 316 ALA A C   1 
ATOM   2373 O O   . ALA A 1 316 ? 98.401  102.326 81.453  1.00 61.69  ? 316 ALA A O   1 
ATOM   2374 C CB  . ALA A 1 316 ? 97.348  103.334 78.757  1.00 62.71  ? 316 ALA A CB  1 
ATOM   2375 N N   . ASP A 1 317 ? 96.193  101.895 81.600  1.00 61.68  ? 317 ASP A N   1 
ATOM   2376 C CA  . ASP A 1 317 ? 96.203  101.946 83.057  1.00 62.16  ? 317 ASP A CA  1 
ATOM   2377 C C   . ASP A 1 317 ? 96.923  100.753 83.670  1.00 61.46  ? 317 ASP A C   1 
ATOM   2378 O O   . ASP A 1 317 ? 97.315  100.816 84.839  1.00 62.72  ? 317 ASP A O   1 
ATOM   2379 C CB  . ASP A 1 317 ? 94.775  102.033 83.601  1.00 63.43  ? 317 ASP A CB  1 
ATOM   2380 C CG  . ASP A 1 317 ? 93.893  100.902 83.116  1.00 65.06  ? 317 ASP A CG  1 
ATOM   2381 O OD1 . ASP A 1 317 ? 93.382  100.989 81.980  1.00 66.75  ? 317 ASP A OD1 1 
ATOM   2382 O OD2 . ASP A 1 317 ? 93.704  99.928  83.874  1.00 66.72  ? 317 ASP A OD2 1 
ATOM   2383 N N   . MET A 1 318 ? 97.103  99.672  82.914  1.00 60.09  ? 318 MET A N   1 
ATOM   2384 C CA  . MET A 1 318 ? 97.899  98.527  83.351  1.00 59.84  ? 318 MET A CA  1 
ATOM   2385 C C   . MET A 1 318 ? 98.950  98.224  82.279  1.00 57.29  ? 318 MET A C   1 
ATOM   2386 O O   . MET A 1 318 ? 98.664  97.644  81.228  1.00 58.68  ? 318 MET A O   1 
ATOM   2387 C CB  . MET A 1 318 ? 96.999  97.327  83.697  1.00 62.52  ? 318 MET A CB  1 
ATOM   2388 C CG  . MET A 1 318 ? 96.173  96.696  82.576  1.00 65.55  ? 318 MET A CG  1 
ATOM   2389 S SD  . MET A 1 318 ? 95.098  95.378  83.161  1.00 70.65  ? 318 MET A SD  1 
ATOM   2390 C CE  . MET A 1 318 ? 93.851  96.341  84.009  1.00 70.93  ? 318 MET A CE  1 
ATOM   2391 N N   . ILE A 1 319 ? 100.174 98.681  82.526  1.00 53.10  ? 319 ILE A N   1 
ATOM   2392 C CA  . ILE A 1 319 ? 101.311 98.350  81.674  1.00 49.59  ? 319 ILE A CA  1 
ATOM   2393 C C   . ILE A 1 319 ? 102.367 97.558  82.426  1.00 47.69  ? 319 ILE A C   1 
ATOM   2394 O O   . ILE A 1 319 ? 103.241 96.949  81.787  1.00 47.65  ? 319 ILE A O   1 
ATOM   2395 C CB  . ILE A 1 319 ? 101.928 99.616  81.041  1.00 49.05  ? 319 ILE A CB  1 
ATOM   2396 C CG1 . ILE A 1 319 ? 102.718 99.278  79.775  1.00 48.45  ? 319 ILE A CG1 1 
ATOM   2397 C CG2 . ILE A 1 319 ? 102.811 100.336 82.035  1.00 49.43  ? 319 ILE A CG2 1 
ATOM   2398 C CD1 . ILE A 1 319 ? 101.928 98.495  78.758  1.00 47.95  ? 319 ILE A CD1 1 
ATOM   2399 N N   . LEU A 1 320 ? 102.303 97.526  83.759  1.00 45.62  ? 320 LEU A N   1 
ATOM   2400 C CA  . LEU A 1 320 ? 103.193 96.650  84.518  1.00 43.78  ? 320 LEU A CA  1 
ATOM   2401 C C   . LEU A 1 320 ? 102.853 95.171  84.342  1.00 43.05  ? 320 LEU A C   1 
ATOM   2402 O O   . LEU A 1 320 ? 103.780 94.382  84.087  1.00 43.41  ? 320 LEU A O   1 
ATOM   2403 C CB  . LEU A 1 320 ? 103.196 97.067  85.992  1.00 42.64  ? 320 LEU A CB  1 
ATOM   2404 C CG  . LEU A 1 320 ? 104.225 96.429  86.918  1.00 41.79  ? 320 LEU A CG  1 
ATOM   2405 C CD1 . LEU A 1 320 ? 105.528 97.196  86.895  1.00 41.43  ? 320 LEU A CD1 1 
ATOM   2406 C CD2 . LEU A 1 320 ? 103.674 96.356  88.316  1.00 41.63  ? 320 LEU A CD2 1 
ATOM   2407 N N   . PRO A 1 321 ? 101.594 94.713  84.475  1.00 42.07  ? 321 PRO A N   1 
ATOM   2408 C CA  . PRO A 1 321 ? 101.342 93.274  84.288  1.00 41.90  ? 321 PRO A CA  1 
ATOM   2409 C C   . PRO A 1 321 ? 101.589 92.780  82.874  1.00 42.26  ? 321 PRO A C   1 
ATOM   2410 O O   . PRO A 1 321 ? 101.976 91.618  82.704  1.00 44.38  ? 321 PRO A O   1 
ATOM   2411 C CB  . PRO A 1 321 ? 99.866  93.121  84.676  1.00 41.36  ? 321 PRO A CB  1 
ATOM   2412 C CG  . PRO A 1 321 ? 99.591  94.269  85.549  1.00 41.68  ? 321 PRO A CG  1 
ATOM   2413 C CD  . PRO A 1 321 ? 100.363 95.384  84.937  1.00 42.12  ? 321 PRO A CD  1 
ATOM   2414 N N   . ILE A 1 322 ? 101.369 93.614  81.856  1.00 41.60  ? 322 ILE A N   1 
ATOM   2415 C CA  . ILE A 1 322 ? 101.582 93.177  80.479  1.00 41.99  ? 322 ILE A CA  1 
ATOM   2416 C C   . ILE A 1 322 ? 103.064 92.931  80.218  1.00 42.29  ? 322 ILE A C   1 
ATOM   2417 O O   . ILE A 1 322 ? 103.441 91.935  79.587  1.00 42.21  ? 322 ILE A O   1 
ATOM   2418 C CB  . ILE A 1 322 ? 100.991 94.204  79.498  1.00 42.04  ? 322 ILE A CB  1 
ATOM   2419 C CG1 . ILE A 1 322 ? 99.475  94.284  79.665  1.00 42.55  ? 322 ILE A CG1 1 
ATOM   2420 C CG2 . ILE A 1 322 ? 101.325 93.833  78.070  1.00 41.95  ? 322 ILE A CG2 1 
ATOM   2421 C CD1 . ILE A 1 322 ? 98.832  95.371  78.839  1.00 42.86  ? 322 ILE A CD1 1 
ATOM   2422 N N   . VAL A 1 323 ? 103.925 93.829  80.706  1.00 42.46  ? 323 VAL A N   1 
ATOM   2423 C CA  . VAL A 1 323 ? 105.368 93.657  80.555  1.00 41.88  ? 323 VAL A CA  1 
ATOM   2424 C C   . VAL A 1 323 ? 105.837 92.409  81.294  1.00 42.03  ? 323 VAL A C   1 
ATOM   2425 O O   . VAL A 1 323 ? 106.667 91.644  80.787  1.00 42.59  ? 323 VAL A O   1 
ATOM   2426 C CB  . VAL A 1 323 ? 106.103 94.922  81.037  1.00 41.71  ? 323 VAL A CB  1 
ATOM   2427 C CG1 . VAL A 1 323 ? 107.584 94.652  81.231  1.00 41.82  ? 323 VAL A CG1 1 
ATOM   2428 C CG2 . VAL A 1 323 ? 105.898 96.055  80.051  1.00 41.60  ? 323 VAL A CG2 1 
ATOM   2429 N N   . LEU A 1 324 ? 105.303 92.179  82.497  1.00 41.91  ? 324 LEU A N   1 
ATOM   2430 C CA  . LEU A 1 324 ? 105.660 90.983  83.256  1.00 41.92  ? 324 LEU A CA  1 
ATOM   2431 C C   . LEU A 1 324 ? 105.230 89.713  82.531  1.00 42.85  ? 324 LEU A C   1 
ATOM   2432 O O   . LEU A 1 324 ? 105.989 88.740  82.466  1.00 43.79  ? 324 LEU A O   1 
ATOM   2433 C CB  . LEU A 1 324 ? 105.027 91.035  84.647  1.00 41.07  ? 324 LEU A CB  1 
ATOM   2434 C CG  . LEU A 1 324 ? 105.554 92.062  85.647  1.00 40.71  ? 324 LEU A CG  1 
ATOM   2435 C CD1 . LEU A 1 324 ? 104.629 92.155  86.847  1.00 41.02  ? 324 LEU A CD1 1 
ATOM   2436 C CD2 . LEU A 1 324 ? 106.951 91.704  86.090  1.00 40.54  ? 324 LEU A CD2 1 
ATOM   2437 N N   . GLN A 1 325 ? 104.017 89.703  81.975  1.00 43.88  ? 325 GLN A N   1 
ATOM   2438 C CA  . GLN A 1 325 ? 103.490 88.478  81.382  1.00 45.71  ? 325 GLN A CA  1 
ATOM   2439 C C   . GLN A 1 325 ? 104.141 88.169  80.038  1.00 46.89  ? 325 GLN A C   1 
ATOM   2440 O O   . GLN A 1 325 ? 104.500 87.016  79.772  1.00 47.07  ? 325 GLN A O   1 
ATOM   2441 C CB  . GLN A 1 325 ? 101.971 88.581  81.231  1.00 46.33  ? 325 GLN A CB  1 
ATOM   2442 C CG  . GLN A 1 325 ? 101.347 87.546  80.297  1.00 47.05  ? 325 GLN A CG  1 
ATOM   2443 C CD  . GLN A 1 325 ? 101.513 86.111  80.774  1.00 47.55  ? 325 GLN A CD  1 
ATOM   2444 O OE1 . GLN A 1 325 ? 101.778 85.853  81.948  1.00 47.85  ? 325 GLN A OE1 1 
ATOM   2445 N NE2 . GLN A 1 325 ? 101.360 85.166  79.854  1.00 47.71  ? 325 GLN A NE2 1 
ATOM   2446 N N   . TYR A 1 326 ? 104.314 89.177  79.183  1.00 48.72  ? 326 TYR A N   1 
ATOM   2447 C CA  . TYR A 1 326 ? 104.733 88.940  77.806  1.00 50.63  ? 326 TYR A CA  1 
ATOM   2448 C C   . TYR A 1 326 ? 106.240 89.056  77.603  1.00 51.99  ? 326 TYR A C   1 
ATOM   2449 O O   . TYR A 1 326 ? 106.849 88.170  76.998  1.00 53.25  ? 326 TYR A O   1 
ATOM   2450 C CB  . TYR A 1 326 ? 103.999 89.900  76.862  1.00 50.79  ? 326 TYR A CB  1 
ATOM   2451 C CG  . TYR A 1 326 ? 102.519 89.612  76.746  1.00 51.23  ? 326 TYR A CG  1 
ATOM   2452 C CD1 . TYR A 1 326 ? 101.614 90.136  77.660  1.00 51.38  ? 326 TYR A CD1 1 
ATOM   2453 C CD2 . TYR A 1 326 ? 102.028 88.805  75.729  1.00 51.41  ? 326 TYR A CD2 1 
ATOM   2454 C CE1 . TYR A 1 326 ? 100.262 89.870  77.560  1.00 51.63  ? 326 TYR A CE1 1 
ATOM   2455 C CE2 . TYR A 1 326 ? 100.677 88.534  75.621  1.00 51.68  ? 326 TYR A CE2 1 
ATOM   2456 C CZ  . TYR A 1 326 ? 99.800  89.069  76.540  1.00 51.84  ? 326 TYR A CZ  1 
ATOM   2457 O OH  . TYR A 1 326 ? 98.454  88.803  76.438  1.00 51.90  ? 326 TYR A OH  1 
ATOM   2458 N N   . LEU A 1 327 ? 106.856 90.136  78.089  1.00 52.68  ? 327 LEU A N   1 
ATOM   2459 C CA  . LEU A 1 327 ? 108.290 90.316  77.881  1.00 52.13  ? 327 LEU A CA  1 
ATOM   2460 C C   . LEU A 1 327 ? 109.107 89.361  78.743  1.00 52.93  ? 327 LEU A C   1 
ATOM   2461 O O   . LEU A 1 327 ? 110.066 88.747  78.260  1.00 53.16  ? 327 LEU A O   1 
ATOM   2462 C CB  . LEU A 1 327 ? 108.680 91.767  78.163  1.00 51.62  ? 327 LEU A CB  1 
ATOM   2463 C CG  . LEU A 1 327 ? 108.129 92.793  77.173  1.00 51.21  ? 327 LEU A CG  1 
ATOM   2464 C CD1 . LEU A 1 327 ? 108.461 94.204  77.615  1.00 50.84  ? 327 LEU A CD1 1 
ATOM   2465 C CD2 . LEU A 1 327 ? 108.684 92.527  75.790  1.00 50.99  ? 327 LEU A CD2 1 
ATOM   2466 N N   . CYS A 1 328 ? 108.748 89.221  80.013  1.00 53.39  ? 328 CYS A N   1 
ATOM   2467 C CA  . CYS A 1 328 ? 109.468 88.347  80.922  1.00 53.37  ? 328 CYS A CA  1 
ATOM   2468 C C   . CYS A 1 328 ? 109.015 86.899  80.753  1.00 53.84  ? 328 CYS A C   1 
ATOM   2469 O O   . CYS A 1 328 ? 107.896 86.637  80.305  1.00 54.31  ? 328 CYS A O   1 
ATOM   2470 C CB  . CYS A 1 328 ? 109.250 88.805  82.361  1.00 52.70  ? 328 CYS A CB  1 
ATOM   2471 S SG  . CYS A 1 328 ? 109.585 90.557  82.642  1.00 52.68  ? 328 CYS A SG  1 
ATOM   2472 N N   . PRO A 1 329 ? 109.875 85.925  81.102  1.00 53.80  ? 329 PRO A N   1 
ATOM   2473 C CA  . PRO A 1 329 ? 109.450 84.518  81.048  1.00 53.31  ? 329 PRO A CA  1 
ATOM   2474 C C   . PRO A 1 329 ? 108.437 84.166  82.128  1.00 53.02  ? 329 PRO A C   1 
ATOM   2475 O O   . PRO A 1 329 ? 108.028 85.030  82.908  1.00 52.90  ? 329 PRO A O   1 
ATOM   2476 C CB  . PRO A 1 329 ? 110.763 83.745  81.227  1.00 53.17  ? 329 PRO A CB  1 
ATOM   2477 C CG  . PRO A 1 329 ? 111.674 84.693  81.908  1.00 53.28  ? 329 PRO A CG  1 
ATOM   2478 C CD  . PRO A 1 329 ? 111.313 86.052  81.396  1.00 53.65  ? 329 PRO A CD  1 
ATOM   2479 N N   . VAL A 1 330 ? 108.032 82.894  82.179  1.00 52.43  ? 330 VAL A N   1 
ATOM   2480 C CA  . VAL A 1 330 ? 106.889 82.495  82.999  1.00 52.31  ? 330 VAL A CA  1 
ATOM   2481 C C   . VAL A 1 330 ? 107.203 82.637  84.486  1.00 51.72  ? 330 VAL A C   1 
ATOM   2482 O O   . VAL A 1 330 ? 106.423 83.224  85.247  1.00 52.29  ? 330 VAL A O   1 
ATOM   2483 C CB  . VAL A 1 330 ? 106.460 81.060  82.648  1.00 52.63  ? 330 VAL A CB  1 
ATOM   2484 C CG1 . VAL A 1 330 ? 105.359 80.590  83.583  1.00 52.66  ? 330 VAL A CG1 1 
ATOM   2485 C CG2 . VAL A 1 330 ? 106.003 80.986  81.201  1.00 52.36  ? 330 VAL A CG2 1 
ATOM   2486 N N   . TYR A 1 331 ? 108.347 82.109  84.927  1.00 50.76  ? 331 TYR A N   1 
ATOM   2487 C CA  . TYR A 1 331 ? 108.658 82.158  86.352  1.00 50.37  ? 331 TYR A CA  1 
ATOM   2488 C C   . TYR A 1 331 ? 109.025 83.567  86.803  1.00 48.88  ? 331 TYR A C   1 
ATOM   2489 O O   . TYR A 1 331 ? 108.707 83.956  87.932  1.00 47.92  ? 331 TYR A O   1 
ATOM   2490 C CB  . TYR A 1 331 ? 109.754 81.142  86.689  1.00 51.63  ? 331 TYR A CB  1 
ATOM   2491 C CG  . TYR A 1 331 ? 111.120 81.400  86.092  1.00 53.15  ? 331 TYR A CG  1 
ATOM   2492 C CD1 . TYR A 1 331 ? 112.057 82.190  86.746  1.00 53.88  ? 331 TYR A CD1 1 
ATOM   2493 C CD2 . TYR A 1 331 ? 111.481 80.831  84.877  1.00 53.95  ? 331 TYR A CD2 1 
ATOM   2494 C CE1 . TYR A 1 331 ? 113.308 82.412  86.203  1.00 54.36  ? 331 TYR A CE1 1 
ATOM   2495 C CE2 . TYR A 1 331 ? 112.728 81.051  84.325  1.00 54.28  ? 331 TYR A CE2 1 
ATOM   2496 C CZ  . TYR A 1 331 ? 113.636 81.843  84.992  1.00 54.36  ? 331 TYR A CZ  1 
ATOM   2497 O OH  . TYR A 1 331 ? 114.879 82.064  84.446  1.00 54.05  ? 331 TYR A OH  1 
ATOM   2498 N N   . ILE A 1 332 ? 109.658 84.357  85.934  1.00 48.30  ? 332 ILE A N   1 
ATOM   2499 C CA  . ILE A 1 332 ? 109.872 85.766  86.250  1.00 48.03  ? 332 ILE A CA  1 
ATOM   2500 C C   . ILE A 1 332 ? 108.542 86.509  86.299  1.00 48.38  ? 332 ILE A C   1 
ATOM   2501 O O   . ILE A 1 332 ? 108.358 87.419  87.120  1.00 49.49  ? 332 ILE A O   1 
ATOM   2502 C CB  . ILE A 1 332 ? 110.850 86.389  85.238  1.00 47.27  ? 332 ILE A CB  1 
ATOM   2503 C CG1 . ILE A 1 332 ? 112.218 85.727  85.371  1.00 47.52  ? 332 ILE A CG1 1 
ATOM   2504 C CG2 . ILE A 1 332 ? 110.998 87.878  85.465  1.00 46.67  ? 332 ILE A CG2 1 
ATOM   2505 C CD1 . ILE A 1 332 ? 112.826 85.895  86.735  1.00 47.56  ? 332 ILE A CD1 1 
ATOM   2506 N N   . SER A 1 333 ? 107.590 86.128  85.442  1.00 47.95  ? 333 SER A N   1 
ATOM   2507 C CA  . SER A 1 333 ? 106.250 86.701  85.515  1.00 47.07  ? 333 SER A CA  1 
ATOM   2508 C C   . SER A 1 333 ? 105.591 86.389  86.851  1.00 45.72  ? 333 SER A C   1 
ATOM   2509 O O   . SER A 1 333 ? 104.940 87.255  87.446  1.00 45.60  ? 333 SER A O   1 
ATOM   2510 C CB  . SER A 1 333 ? 105.387 86.182  84.367  1.00 47.55  ? 333 SER A CB  1 
ATOM   2511 O OG  . SER A 1 333 ? 104.075 86.707  84.442  1.00 48.06  ? 333 SER A OG  1 
ATOM   2512 N N   . PHE A 1 334 ? 105.752 85.158  87.341  1.00 44.70  ? 334 PHE A N   1 
ATOM   2513 C CA  . PHE A 1 334 ? 105.198 84.818  88.649  1.00 44.33  ? 334 PHE A CA  1 
ATOM   2514 C C   . PHE A 1 334 ? 105.908 85.557  89.776  1.00 44.08  ? 334 PHE A C   1 
ATOM   2515 O O   . PHE A 1 334 ? 105.268 85.924  90.765  1.00 44.67  ? 334 PHE A O   1 
ATOM   2516 C CB  . PHE A 1 334 ? 105.256 83.309  88.877  1.00 44.58  ? 334 PHE A CB  1 
ATOM   2517 C CG  . PHE A 1 334 ? 104.126 82.563  88.234  1.00 44.40  ? 334 PHE A CG  1 
ATOM   2518 C CD1 . PHE A 1 334 ? 102.831 82.723  88.691  1.00 44.53  ? 334 PHE A CD1 1 
ATOM   2519 C CD2 . PHE A 1 334 ? 104.357 81.705  87.174  1.00 44.30  ? 334 PHE A CD2 1 
ATOM   2520 C CE1 . PHE A 1 334 ? 101.786 82.043  88.101  1.00 44.79  ? 334 PHE A CE1 1 
ATOM   2521 C CE2 . PHE A 1 334 ? 103.317 81.020  86.580  1.00 44.52  ? 334 PHE A CE2 1 
ATOM   2522 C CZ  . PHE A 1 334 ? 102.030 81.190  87.045  1.00 44.68  ? 334 PHE A CZ  1 
ATOM   2523 N N   . PHE A 1 335 ? 107.219 85.784  89.650  1.00 43.93  ? 335 PHE A N   1 
ATOM   2524 C CA  . PHE A 1 335 ? 107.935 86.593  90.637  1.00 44.02  ? 335 PHE A CA  1 
ATOM   2525 C C   . PHE A 1 335 ? 107.391 88.017  90.679  1.00 43.66  ? 335 PHE A C   1 
ATOM   2526 O O   . PHE A 1 335 ? 107.147 88.576  91.758  1.00 43.93  ? 335 PHE A O   1 
ATOM   2527 C CB  . PHE A 1 335 ? 109.431 86.606  90.317  1.00 44.65  ? 335 PHE A CB  1 
ATOM   2528 C CG  . PHE A 1 335 ? 110.219 85.549  91.033  1.00 45.36  ? 335 PHE A CG  1 
ATOM   2529 C CD1 . PHE A 1 335 ? 110.004 84.207  90.773  1.00 45.77  ? 335 PHE A CD1 1 
ATOM   2530 C CD2 . PHE A 1 335 ? 111.189 85.899  91.954  1.00 45.63  ? 335 PHE A CD2 1 
ATOM   2531 C CE1 . PHE A 1 335 ? 110.733 83.235  91.426  1.00 45.94  ? 335 PHE A CE1 1 
ATOM   2532 C CE2 . PHE A 1 335 ? 111.922 84.932  92.610  1.00 45.79  ? 335 PHE A CE2 1 
ATOM   2533 C CZ  . PHE A 1 335 ? 111.694 83.597  92.345  1.00 45.92  ? 335 PHE A CZ  1 
ATOM   2534 N N   . GLY A 1 336 ? 107.185 88.617  89.506  1.00 43.32  ? 336 GLY A N   1 
ATOM   2535 C CA  . GLY A 1 336 ? 106.633 89.961  89.457  1.00 42.69  ? 336 GLY A CA  1 
ATOM   2536 C C   . GLY A 1 336 ? 105.211 90.027  89.982  1.00 41.82  ? 336 GLY A C   1 
ATOM   2537 O O   . GLY A 1 336 ? 104.832 90.987  90.660  1.00 40.74  ? 336 GLY A O   1 
ATOM   2538 N N   . LEU A 1 337 ? 104.408 89.003  89.685  1.00 42.12  ? 337 LEU A N   1 
ATOM   2539 C CA  . LEU A 1 337 ? 103.043 88.958  90.196  1.00 42.47  ? 337 LEU A CA  1 
ATOM   2540 C C   . LEU A 1 337 ? 103.027 88.789  91.709  1.00 42.40  ? 337 LEU A C   1 
ATOM   2541 O O   . LEU A 1 337 ? 102.179 89.371  92.393  1.00 43.05  ? 337 LEU A O   1 
ATOM   2542 C CB  . LEU A 1 337 ? 102.270 87.832  89.516  1.00 42.85  ? 337 LEU A CB  1 
ATOM   2543 C CG  . LEU A 1 337 ? 100.839 87.606  89.992  1.00 42.88  ? 337 LEU A CG  1 
ATOM   2544 C CD1 . LEU A 1 337 ? 100.070 88.900  89.904  1.00 43.54  ? 337 LEU A CD1 1 
ATOM   2545 C CD2 . LEU A 1 337 ? 100.184 86.561  89.129  1.00 42.81  ? 337 LEU A CD2 1 
ATOM   2546 N N   . GLY A 1 338 ? 103.952 87.994  92.248  1.00 42.48  ? 338 GLY A N   1 
ATOM   2547 C CA  . GLY A 1 338 ? 104.079 87.897  93.691  1.00 41.98  ? 338 GLY A CA  1 
ATOM   2548 C C   . GLY A 1 338 ? 104.466 89.218  94.323  1.00 41.40  ? 338 GLY A C   1 
ATOM   2549 O O   . GLY A 1 338 ? 103.959 89.578  95.386  1.00 40.40  ? 338 GLY A O   1 
ATOM   2550 N N   . ALA A 1 339 ? 105.358 89.966  93.667  1.00 42.21  ? 339 ALA A N   1 
ATOM   2551 C CA  . ALA A 1 339 ? 105.721 91.291  94.167  1.00 43.56  ? 339 ALA A CA  1 
ATOM   2552 C C   . ALA A 1 339 ? 104.526 92.240  94.164  1.00 44.64  ? 339 ALA A C   1 
ATOM   2553 O O   . ALA A 1 339 ? 104.297 92.966  95.141  1.00 46.21  ? 339 ALA A O   1 
ATOM   2554 C CB  . ALA A 1 339 ? 106.864 91.870  93.335  1.00 43.77  ? 339 ALA A CB  1 
ATOM   2555 N N   . VAL A 1 340 ? 103.748 92.242  93.078  1.00 44.40  ? 340 VAL A N   1 
ATOM   2556 C CA  . VAL A 1 340 ? 102.579 93.118  92.992  1.00 43.29  ? 340 VAL A CA  1 
ATOM   2557 C C   . VAL A 1 340 ? 101.531 92.731  94.032  1.00 42.61  ? 340 VAL A C   1 
ATOM   2558 O O   . VAL A 1 340 ? 100.935 93.597  94.687  1.00 42.29  ? 340 VAL A O   1 
ATOM   2559 C CB  . VAL A 1 340 ? 101.998 93.092  91.567  1.00 43.31  ? 340 VAL A CB  1 
ATOM   2560 C CG1 . VAL A 1 340 ? 100.706 93.889  91.496  1.00 43.47  ? 340 VAL A CG1 1 
ATOM   2561 C CG2 . VAL A 1 340 ? 103.003 93.641  90.587  1.00 43.01  ? 340 VAL A CG2 1 
ATOM   2562 N N   . SER A 1 341 ? 101.289 91.427  94.198  1.00 41.91  ? 341 SER A N   1 
ATOM   2563 C CA  . SER A 1 341 ? 100.324 90.964  95.189  1.00 41.37  ? 341 SER A CA  1 
ATOM   2564 C C   . SER A 1 341 ? 100.779 91.299  96.603  1.00 40.58  ? 341 SER A C   1 
ATOM   2565 O O   . SER A 1 341 ? 99.959  91.672  97.447  1.00 41.36  ? 341 SER A O   1 
ATOM   2566 C CB  . SER A 1 341 ? 100.098 89.462  95.038  1.00 41.58  ? 341 SER A CB  1 
ATOM   2567 O OG  . SER A 1 341 ? 99.201  88.981  96.022  1.00 42.18  ? 341 SER A OG  1 
ATOM   2568 N N   . ALA A 1 342 ? 102.081 91.175  96.880  1.00 39.73  ? 342 ALA A N   1 
ATOM   2569 C CA  . ALA A 1 342 ? 102.600 91.561  98.187  1.00 39.61  ? 342 ALA A CA  1 
ATOM   2570 C C   . ALA A 1 342 ? 102.419 93.052  98.432  1.00 39.42  ? 342 ALA A C   1 
ATOM   2571 O O   . ALA A 1 342 ? 102.055 93.463  99.539  1.00 40.26  ? 342 ALA A O   1 
ATOM   2572 C CB  . ALA A 1 342 ? 104.072 91.171  98.306  1.00 40.06  ? 342 ALA A CB  1 
ATOM   2573 N N   . ALA A 1 343 ? 102.656 93.875  97.407  1.00 38.91  ? 343 ALA A N   1 
ATOM   2574 C CA  . ALA A 1 343 ? 102.453 95.314  97.555  1.00 38.54  ? 343 ALA A CA  1 
ATOM   2575 C C   . ALA A 1 343 ? 100.993 95.647  97.837  1.00 38.09  ? 343 ALA A C   1 
ATOM   2576 O O   . ALA A 1 343 ? 100.691 96.467  98.718  1.00 36.94  ? 343 ALA A O   1 
ATOM   2577 C CB  . ALA A 1 343 ? 102.935 96.042  96.301  1.00 38.81  ? 343 ALA A CB  1 
ATOM   2578 N N   . VAL A 1 344 ? 100.072 95.013  97.105  1.00 38.17  ? 344 VAL A N   1 
ATOM   2579 C CA  . VAL A 1 344 ? 98.656  95.309  97.296  1.00 37.79  ? 344 VAL A CA  1 
ATOM   2580 C C   . VAL A 1 344 ? 98.194  94.837  98.668  1.00 37.69  ? 344 VAL A C   1 
ATOM   2581 O O   . VAL A 1 344 ? 97.460  95.548  99.360  1.00 37.58  ? 344 VAL A O   1 
ATOM   2582 C CB  . VAL A 1 344 ? 97.802  94.689  96.176  1.00 37.44  ? 344 VAL A CB  1 
ATOM   2583 C CG1 . VAL A 1 344 ? 96.330  94.763  96.544  1.00 37.53  ? 344 VAL A CG1 1 
ATOM   2584 C CG2 . VAL A 1 344 ? 98.049  95.387  94.865  1.00 37.27  ? 344 VAL A CG2 1 
ATOM   2585 N N   . MET A 1 345 ? 98.615  93.637  99.089  1.00 38.60  ? 345 MET A N   1 
ATOM   2586 C CA  . MET A 1 345 ? 98.241  93.166  100.419 1.00 40.03  ? 345 MET A CA  1 
ATOM   2587 C C   . MET A 1 345 ? 98.811  94.062  101.505 1.00 40.56  ? 345 MET A C   1 
ATOM   2588 O O   . MET A 1 345 ? 98.124  94.352  102.484 1.00 42.54  ? 345 MET A O   1 
ATOM   2589 C CB  . MET A 1 345 ? 98.686  91.723  100.654 1.00 41.30  ? 345 MET A CB  1 
ATOM   2590 C CG  . MET A 1 345 ? 97.997  90.684  99.807  1.00 42.88  ? 345 MET A CG  1 
ATOM   2591 S SD  . MET A 1 345 ? 98.580  89.043  100.259 1.00 46.47  ? 345 MET A SD  1 
ATOM   2592 C CE  . MET A 1 345 ? 100.213 89.055  99.530  1.00 46.52  ? 345 MET A CE  1 
ATOM   2593 N N   . SER A 1 346 ? 100.051 94.534  101.343 1.00 40.87  ? 346 SER A N   1 
ATOM   2594 C CA  . SER A 1 346 ? 100.639 95.418  102.345 1.00 41.24  ? 346 SER A CA  1 
ATOM   2595 C C   . SER A 1 346 ? 99.850  96.716  102.470 1.00 40.45  ? 346 SER A C   1 
ATOM   2596 O O   . SER A 1 346 ? 99.444  97.106  103.573 1.00 39.09  ? 346 SER A O   1 
ATOM   2597 C CB  . SER A 1 346 ? 102.097 95.708  101.994 1.00 42.81  ? 346 SER A CB  1 
ATOM   2598 O OG  . SER A 1 346 ? 102.194 96.767  101.060 1.00 44.67  ? 346 SER A OG  1 
ATOM   2599 N N   . SER A 1 347 ? 99.587  97.382  101.341 1.00 40.23  ? 347 SER A N   1 
ATOM   2600 C CA  . SER A 1 347 ? 98.896  98.669  101.402 1.00 39.77  ? 347 SER A CA  1 
ATOM   2601 C C   . SER A 1 347 ? 97.439  98.516  101.831 1.00 39.18  ? 347 SER A C   1 
ATOM   2602 O O   . SER A 1 347 ? 96.943  99.303  102.645 1.00 38.74  ? 347 SER A O   1 
ATOM   2603 C CB  . SER A 1 347 ? 98.993  99.384  100.058 1.00 39.99  ? 347 SER A CB  1 
ATOM   2604 O OG  . SER A 1 347 ? 100.318 99.823  99.830  1.00 40.29  ? 347 SER A OG  1 
ATOM   2605 N N   . ALA A 1 348 ? 96.737  97.506  101.311 1.00 38.79  ? 348 ALA A N   1 
ATOM   2606 C CA  . ALA A 1 348 ? 95.342  97.303  101.683 1.00 38.02  ? 348 ALA A CA  1 
ATOM   2607 C C   . ALA A 1 348 ? 95.206  96.824  103.118 1.00 37.65  ? 348 ALA A C   1 
ATOM   2608 O O   . ALA A 1 348 ? 94.233  97.168  103.791 1.00 37.82  ? 348 ALA A O   1 
ATOM   2609 C CB  . ALA A 1 348 ? 94.686  96.307  100.732 1.00 37.72  ? 348 ALA A CB  1 
ATOM   2610 N N   . ASP A 1 349 ? 96.163  96.034  103.598 1.00 38.51  ? 349 ASP A N   1 
ATOM   2611 C CA  . ASP A 1 349 ? 96.194  95.624  104.992 1.00 39.60  ? 349 ASP A CA  1 
ATOM   2612 C C   . ASP A 1 349 ? 96.406  96.821  105.908 1.00 39.19  ? 349 ASP A C   1 
ATOM   2613 O O   . ASP A 1 349 ? 95.730  96.948  106.938 1.00 40.01  ? 349 ASP A O   1 
ATOM   2614 C CB  . ASP A 1 349 ? 97.303  94.586  105.154 1.00 41.58  ? 349 ASP A CB  1 
ATOM   2615 C CG  . ASP A 1 349 ? 97.589  94.247  106.581 1.00 43.12  ? 349 ASP A CG  1 
ATOM   2616 O OD1 . ASP A 1 349 ? 96.658  94.282  107.403 1.00 44.52  ? 349 ASP A OD1 1 
ATOM   2617 O OD2 . ASP A 1 349 ? 98.760  93.937  106.872 1.00 44.62  ? 349 ASP A OD2 1 
ATOM   2618 N N   . SER A 1 350 ? 97.328  97.714  105.538 1.00 38.77  ? 350 SER A N   1 
ATOM   2619 C CA  . SER A 1 350 ? 97.516  98.940  106.304 1.00 38.32  ? 350 SER A CA  1 
ATOM   2620 C C   . SER A 1 350 ? 96.249  99.783  106.311 1.00 37.02  ? 350 SER A C   1 
ATOM   2621 O O   . SER A 1 350 ? 95.844  100.292 107.359 1.00 35.45  ? 350 SER A O   1 
ATOM   2622 C CB  . SER A 1 350 ? 98.682  99.740  105.732 1.00 39.11  ? 350 SER A CB  1 
ATOM   2623 O OG  . SER A 1 350 ? 99.913  99.069  105.936 1.00 39.84  ? 350 SER A OG  1 
ATOM   2624 N N   . SER A 1 351 ? 95.594  99.915  105.154 1.00 36.74  ? 351 SER A N   1 
ATOM   2625 C CA  . SER A 1 351 ? 94.370  100.709 105.071 1.00 36.62  ? 351 SER A CA  1 
ATOM   2626 C C   . SER A 1 351 ? 93.238  100.093 105.887 1.00 36.56  ? 351 SER A C   1 
ATOM   2627 O O   . SER A 1 351 ? 92.480  100.814 106.545 1.00 36.87  ? 351 SER A O   1 
ATOM   2628 C CB  . SER A 1 351 ? 93.948  100.866 103.612 1.00 36.57  ? 351 SER A CB  1 
ATOM   2629 O OG  . SER A 1 351 ? 92.742  101.598 103.512 1.00 36.93  ? 351 SER A OG  1 
ATOM   2630 N N   . ILE A 1 352 ? 93.103  98.766  105.854 1.00 36.76  ? 352 ILE A N   1 
ATOM   2631 C CA  . ILE A 1 352 ? 92.020  98.098  106.568 1.00 37.07  ? 352 ILE A CA  1 
ATOM   2632 C C   . ILE A 1 352 ? 92.230  98.189  108.073 1.00 37.64  ? 352 ILE A C   1 
ATOM   2633 O O   . ILE A 1 352 ? 91.293  98.488  108.823 1.00 37.56  ? 352 ILE A O   1 
ATOM   2634 C CB  . ILE A 1 352 ? 91.894  96.639  106.089 1.00 37.09  ? 352 ILE A CB  1 
ATOM   2635 C CG1 . ILE A 1 352 ? 91.060  96.574  104.809 1.00 37.51  ? 352 ILE A CG1 1 
ATOM   2636 C CG2 . ILE A 1 352 ? 91.278  95.755  107.162 1.00 36.64  ? 352 ILE A CG2 1 
ATOM   2637 C CD1 . ILE A 1 352 ? 90.998  95.198  104.190 1.00 38.02  ? 352 ILE A CD1 1 
ATOM   2638 N N   . LEU A 1 353 ? 93.457  97.945  108.543 1.00 38.98  ? 353 LEU A N   1 
ATOM   2639 C CA  . LEU A 1 353 ? 93.722  98.081  109.972 1.00 40.08  ? 353 LEU A CA  1 
ATOM   2640 C C   . LEU A 1 353 ? 93.622  99.534  110.419 1.00 41.10  ? 353 LEU A C   1 
ATOM   2641 O O   . LEU A 1 353 ? 93.179  99.814  111.537 1.00 41.33  ? 353 LEU A O   1 
ATOM   2642 C CB  . LEU A 1 353 ? 95.094  97.509  110.320 1.00 40.57  ? 353 LEU A CB  1 
ATOM   2643 C CG  . LEU A 1 353 ? 95.412  97.497  111.816 1.00 40.85  ? 353 LEU A CG  1 
ATOM   2644 C CD1 . LEU A 1 353 ? 94.368  96.707  112.582 1.00 40.70  ? 353 LEU A CD1 1 
ATOM   2645 C CD2 . LEU A 1 353 ? 96.792  96.932  112.062 1.00 41.02  ? 353 LEU A CD2 1 
ATOM   2646 N N   . SER A 1 354 ? 94.010  100.472 109.554 1.00 42.96  ? 354 SER A N   1 
ATOM   2647 C CA  . SER A 1 354 ? 94.000  101.880 109.923 1.00 44.55  ? 354 SER A CA  1 
ATOM   2648 C C   . SER A 1 354 ? 92.581  102.431 110.000 1.00 44.57  ? 354 SER A C   1 
ATOM   2649 O O   . SER A 1 354 ? 92.249  103.172 110.931 1.00 44.72  ? 354 SER A O   1 
ATOM   2650 C CB  . SER A 1 354 ? 94.836  102.664 108.917 1.00 45.93  ? 354 SER A CB  1 
ATOM   2651 O OG  . SER A 1 354 ? 94.066  102.985 107.777 1.00 47.34  ? 354 SER A OG  1 
ATOM   2652 N N   . ALA A 1 355 ? 91.729  102.080 109.033 1.00 44.26  ? 355 ALA A N   1 
ATOM   2653 C CA  . ALA A 1 355 ? 90.344  102.538 109.065 1.00 43.79  ? 355 ALA A CA  1 
ATOM   2654 C C   . ALA A 1 355 ? 89.574  101.909 110.216 1.00 43.84  ? 355 ALA A C   1 
ATOM   2655 O O   . ALA A 1 355 ? 88.671  102.541 110.775 1.00 43.94  ? 355 ALA A O   1 
ATOM   2656 C CB  . ALA A 1 355 ? 89.653  102.232 107.739 1.00 43.42  ? 355 ALA A CB  1 
ATOM   2657 N N   . SER A 1 356 ? 89.908  100.672 110.578 1.00 43.76  ? 356 SER A N   1 
ATOM   2658 C CA  . SER A 1 356 ? 89.285  100.019 111.718 1.00 44.00  ? 356 SER A CA  1 
ATOM   2659 C C   . SER A 1 356 ? 89.908  100.424 113.046 1.00 43.93  ? 356 SER A C   1 
ATOM   2660 O O   . SER A 1 356 ? 89.321  100.147 114.096 1.00 43.04  ? 356 SER A O   1 
ATOM   2661 C CB  . SER A 1 356 ? 89.363  98.502  111.555 1.00 44.23  ? 356 SER A CB  1 
ATOM   2662 O OG  . SER A 1 356 ? 88.489  97.850  112.457 1.00 44.94  ? 356 SER A OG  1 
ATOM   2663 N N   . SER A 1 357 ? 91.078  101.063 113.028 1.00 45.36  ? 357 SER A N   1 
ATOM   2664 C CA  . SER A 1 357 ? 91.677  101.583 114.250 1.00 47.18  ? 357 SER A CA  1 
ATOM   2665 C C   . SER A 1 357 ? 91.110  102.934 114.652 1.00 48.48  ? 357 SER A C   1 
ATOM   2666 O O   . SER A 1 357 ? 91.437  103.424 115.737 1.00 49.23  ? 357 SER A O   1 
ATOM   2667 C CB  . SER A 1 357 ? 93.192  101.702 114.097 1.00 47.94  ? 357 SER A CB  1 
ATOM   2668 O OG  . SER A 1 357 ? 93.743  102.451 115.163 1.00 48.04  ? 357 SER A OG  1 
ATOM   2669 N N   . MET A 1 358 ? 90.296  103.554 113.801 1.00 50.50  ? 358 MET A N   1 
ATOM   2670 C CA  . MET A 1 358 ? 89.567  104.759 114.170 1.00 52.90  ? 358 MET A CA  1 
ATOM   2671 C C   . MET A 1 358 ? 88.141  104.474 114.604 1.00 54.75  ? 358 MET A C   1 
ATOM   2672 O O   . MET A 1 358 ? 87.594  105.224 115.418 1.00 56.34  ? 358 MET A O   1 
ATOM   2673 C CB  . MET A 1 358 ? 89.535  105.754 113.005 1.00 53.24  ? 358 MET A CB  1 
ATOM   2674 C CG  . MET A 1 358 ? 90.740  106.668 112.920 1.00 53.57  ? 358 MET A CG  1 
ATOM   2675 S SD  . MET A 1 358 ? 90.847  107.504 111.328 1.00 55.47  ? 358 MET A SD  1 
ATOM   2676 C CE  . MET A 1 358 ? 90.699  106.114 110.214 1.00 55.34  ? 358 MET A CE  1 
ATOM   2677 N N   . PHE A 1 359 ? 87.521  103.416 114.077 1.00 55.62  ? 359 PHE A N   1 
ATOM   2678 C CA  . PHE A 1 359 ? 86.141  103.125 114.445 1.00 56.39  ? 359 PHE A CA  1 
ATOM   2679 C C   . PHE A 1 359 ? 86.047  102.621 115.879 1.00 56.22  ? 359 PHE A C   1 
ATOM   2680 O O   . PHE A 1 359 ? 85.231  103.109 116.665 1.00 58.01  ? 359 PHE A O   1 
ATOM   2681 C CB  . PHE A 1 359 ? 85.526  102.113 113.479 1.00 57.05  ? 359 PHE A CB  1 
ATOM   2682 C CG  . PHE A 1 359 ? 84.046  101.928 113.666 1.00 58.72  ? 359 PHE A CG  1 
ATOM   2683 C CD1 . PHE A 1 359 ? 83.150  102.804 113.080 1.00 60.17  ? 359 PHE A CD1 1 
ATOM   2684 C CD2 . PHE A 1 359 ? 83.550  100.892 114.440 1.00 59.34  ? 359 PHE A CD2 1 
ATOM   2685 C CE1 . PHE A 1 359 ? 81.789  102.644 113.252 1.00 61.04  ? 359 PHE A CE1 1 
ATOM   2686 C CE2 . PHE A 1 359 ? 82.191  100.727 114.614 1.00 60.24  ? 359 PHE A CE2 1 
ATOM   2687 C CZ  . PHE A 1 359 ? 81.310  101.605 114.020 1.00 61.14  ? 359 PHE A CZ  1 
ATOM   2688 N N   . ALA A 1 360 ? 86.886  101.655 116.245 1.00 54.47  ? 360 ALA A N   1 
ATOM   2689 C CA  . ALA A 1 360 ? 86.777  101.051 117.566 1.00 53.04  ? 360 ALA A CA  1 
ATOM   2690 C C   . ALA A 1 360 ? 87.449  101.873 118.654 1.00 51.83  ? 360 ALA A C   1 
ATOM   2691 O O   . ALA A 1 360 ? 87.271  101.568 119.837 1.00 51.82  ? 360 ALA A O   1 
ATOM   2692 C CB  . ALA A 1 360 ? 87.369  99.642  117.551 1.00 53.25  ? 360 ALA A CB  1 
ATOM   2693 N N   . ARG A 1 361 ? 88.216  102.899 118.291 1.00 51.01  ? 361 ARG A N   1 
ATOM   2694 C CA  . ARG A 1 361 ? 88.969  103.655 119.284 1.00 51.67  ? 361 ARG A CA  1 
ATOM   2695 C C   . ARG A 1 361 ? 88.168  104.814 119.865 1.00 52.85  ? 361 ARG A C   1 
ATOM   2696 O O   . ARG A 1 361 ? 88.055  104.937 121.088 1.00 55.78  ? 361 ARG A O   1 
ATOM   2697 C CB  . ARG A 1 361 ? 90.267  104.184 118.669 1.00 51.33  ? 361 ARG A CB  1 
ATOM   2698 C CG  . ARG A 1 361 ? 90.954  105.279 119.475 1.00 51.42  ? 361 ARG A CG  1 
ATOM   2699 C CD  . ARG A 1 361 ? 91.418  104.770 120.835 1.00 51.47  ? 361 ARG A CD  1 
ATOM   2700 N NE  . ARG A 1 361 ? 91.680  105.865 121.761 1.00 52.10  ? 361 ARG A NE  1 
ATOM   2701 C CZ  . ARG A 1 361 ? 92.316  105.732 122.916 1.00 53.25  ? 361 ARG A CZ  1 
ATOM   2702 N NH1 . ARG A 1 361 ? 92.761  104.557 123.329 1.00 54.39  ? 361 ARG A NH1 1 
ATOM   2703 N NH2 . ARG A 1 361 ? 92.507  106.805 123.678 1.00 53.09  ? 361 ARG A NH2 1 
ATOM   2704 N N   . ASN A 1 362 ? 87.632  105.682 119.017 1.00 52.22  ? 362 ASN A N   1 
ATOM   2705 C CA  . ASN A 1 362 ? 87.090  106.947 119.498 1.00 51.92  ? 362 ASN A CA  1 
ATOM   2706 C C   . ASN A 1 362 ? 85.632  107.194 119.141 1.00 51.03  ? 362 ASN A C   1 
ATOM   2707 O O   . ASN A 1 362 ? 84.887  107.711 119.976 1.00 50.77  ? 362 ASN A O   1 
ATOM   2708 C CB  . ASN A 1 362 ? 87.980  108.099 119.002 1.00 52.11  ? 362 ASN A CB  1 
ATOM   2709 C CG  . ASN A 1 362 ? 88.146  108.119 117.494 1.00 52.62  ? 362 ASN A CG  1 
ATOM   2710 O OD1 . ASN A 1 362 ? 87.258  107.724 116.740 1.00 55.37  ? 362 ASN A OD1 1 
ATOM   2711 N ND2 . ASN A 1 362 ? 89.317  108.553 117.050 1.00 52.07  ? 362 ASN A ND2 1 
ATOM   2712 N N   . ILE A 1 363 ? 85.191  106.856 117.927 1.00 49.96  ? 363 ILE A N   1 
ATOM   2713 C CA  . ILE A 1 363 ? 83.782  107.072 117.610 1.00 48.92  ? 363 ILE A CA  1 
ATOM   2714 C C   . ILE A 1 363 ? 82.912  106.026 118.308 1.00 49.12  ? 363 ILE A C   1 
ATOM   2715 O O   . ILE A 1 363 ? 81.742  106.284 118.614 1.00 47.93  ? 363 ILE A O   1 
ATOM   2716 C CB  . ILE A 1 363 ? 83.570  107.103 116.081 1.00 48.25  ? 363 ILE A CB  1 
ATOM   2717 C CG1 . ILE A 1 363 ? 82.109  107.381 115.721 1.00 49.13  ? 363 ILE A CG1 1 
ATOM   2718 C CG2 . ILE A 1 363 ? 83.989  105.812 115.454 1.00 47.37  ? 363 ILE A CG2 1 
ATOM   2719 C CD1 . ILE A 1 363 ? 81.873  107.574 114.240 1.00 49.62  ? 363 ILE A CD1 1 
ATOM   2720 N N   . TYR A 1 364 ? 83.467  104.851 118.609 1.00 50.85  ? 364 TYR A N   1 
ATOM   2721 C CA  . TYR A 1 364 ? 82.734  103.845 119.373 1.00 51.91  ? 364 TYR A CA  1 
ATOM   2722 C C   . TYR A 1 364 ? 83.044  103.939 120.866 1.00 52.18  ? 364 TYR A C   1 
ATOM   2723 O O   . TYR A 1 364 ? 82.138  104.126 121.683 1.00 52.33  ? 364 TYR A O   1 
ATOM   2724 C CB  . TYR A 1 364 ? 83.050  102.441 118.840 1.00 52.34  ? 364 TYR A CB  1 
ATOM   2725 C CG  . TYR A 1 364 ? 82.256  101.318 119.474 1.00 52.91  ? 364 TYR A CG  1 
ATOM   2726 C CD1 . TYR A 1 364 ? 82.698  100.689 120.632 1.00 53.08  ? 364 TYR A CD1 1 
ATOM   2727 C CD2 . TYR A 1 364 ? 81.066  100.883 118.910 1.00 53.25  ? 364 TYR A CD2 1 
ATOM   2728 C CE1 . TYR A 1 364 ? 81.975  99.665  121.210 1.00 52.81  ? 364 TYR A CE1 1 
ATOM   2729 C CE2 . TYR A 1 364 ? 80.336  99.859  119.481 1.00 53.46  ? 364 TYR A CE2 1 
ATOM   2730 C CZ  . TYR A 1 364 ? 80.796  99.255  120.630 1.00 52.90  ? 364 TYR A CZ  1 
ATOM   2731 O OH  . TYR A 1 364 ? 80.074  98.235  121.203 1.00 52.83  ? 364 TYR A OH  1 
ATOM   2732 N N   . GLN A 1 365 ? 84.320  103.802 121.234 1.00 53.08  ? 365 GLN A N   1 
ATOM   2733 C CA  . GLN A 1 365 ? 84.673  103.734 122.649 1.00 54.59  ? 365 GLN A CA  1 
ATOM   2734 C C   . GLN A 1 365 ? 84.594  105.102 123.319 1.00 55.23  ? 365 GLN A C   1 
ATOM   2735 O O   . GLN A 1 365 ? 84.135  105.208 124.461 1.00 56.15  ? 365 GLN A O   1 
ATOM   2736 C CB  . GLN A 1 365 ? 86.068  103.133 122.817 1.00 55.92  ? 365 GLN A CB  1 
ATOM   2737 C CG  . GLN A 1 365 ? 86.564  103.099 124.255 1.00 56.94  ? 365 GLN A CG  1 
ATOM   2738 C CD  . GLN A 1 365 ? 88.015  102.677 124.368 1.00 58.56  ? 365 GLN A CD  1 
ATOM   2739 O OE1 . GLN A 1 365 ? 88.606  102.182 123.409 1.00 60.52  ? 365 GLN A OE1 1 
ATOM   2740 N NE2 . GLN A 1 365 ? 88.597  102.872 125.544 1.00 58.84  ? 365 GLN A NE2 1 
ATOM   2741 N N   . LEU A 1 366 ? 85.039  106.158 122.643 1.00 55.71  ? 366 LEU A N   1 
ATOM   2742 C CA  . LEU A 1 366 ? 85.054  107.476 123.264 1.00 56.56  ? 366 LEU A CA  1 
ATOM   2743 C C   . LEU A 1 366 ? 83.817  108.313 122.960 1.00 58.57  ? 366 LEU A C   1 
ATOM   2744 O O   . LEU A 1 366 ? 83.626  109.353 123.600 1.00 58.24  ? 366 LEU A O   1 
ATOM   2745 C CB  . LEU A 1 366 ? 86.304  108.254 122.839 1.00 55.60  ? 366 LEU A CB  1 
ATOM   2746 C CG  . LEU A 1 366 ? 87.645  107.748 123.371 1.00 54.57  ? 366 LEU A CG  1 
ATOM   2747 C CD1 . LEU A 1 366 ? 88.787  108.588 122.826 1.00 54.17  ? 366 LEU A CD1 1 
ATOM   2748 C CD2 . LEU A 1 366 ? 87.652  107.752 124.890 1.00 54.21  ? 366 LEU A CD2 1 
ATOM   2749 N N   . SER A 1 367 ? 82.976  107.902 122.011 1.00 61.52  ? 367 SER A N   1 
ATOM   2750 C CA  . SER A 1 367 ? 81.792  108.680 121.657 1.00 63.79  ? 367 SER A CA  1 
ATOM   2751 C C   . SER A 1 367 ? 80.494  107.941 121.956 1.00 66.39  ? 367 SER A C   1 
ATOM   2752 O O   . SER A 1 367 ? 79.642  108.478 122.670 1.00 66.19  ? 367 SER A O   1 
ATOM   2753 C CB  . SER A 1 367 ? 81.853  109.087 120.180 1.00 63.77  ? 367 SER A CB  1 
ATOM   2754 O OG  . SER A 1 367 ? 83.027  109.830 119.904 1.00 63.48  ? 367 SER A OG  1 
ATOM   2755 N N   . PHE A 1 368 ? 80.310  106.726 121.435 1.00 69.70  ? 368 PHE A N   1 
ATOM   2756 C CA  . PHE A 1 368 ? 79.038  106.031 121.613 1.00 71.97  ? 368 PHE A CA  1 
ATOM   2757 C C   . PHE A 1 368 ? 78.921  105.421 123.007 1.00 74.87  ? 368 PHE A C   1 
ATOM   2758 O O   . PHE A 1 368 ? 78.043  105.799 123.789 1.00 75.86  ? 368 PHE A O   1 
ATOM   2759 C CB  . PHE A 1 368 ? 78.866  104.950 120.541 1.00 72.11  ? 368 PHE A CB  1 
ATOM   2760 C CG  . PHE A 1 368 ? 78.427  105.483 119.207 1.00 72.99  ? 368 PHE A CG  1 
ATOM   2761 C CD1 . PHE A 1 368 ? 77.481  106.491 119.126 1.00 72.40  ? 368 PHE A CD1 1 
ATOM   2762 C CD2 . PHE A 1 368 ? 78.946  104.962 118.033 1.00 74.27  ? 368 PHE A CD2 1 
ATOM   2763 C CE1 . PHE A 1 368 ? 77.072  106.981 117.898 1.00 72.62  ? 368 PHE A CE1 1 
ATOM   2764 C CE2 . PHE A 1 368 ? 78.542  105.447 116.803 1.00 73.82  ? 368 PHE A CE2 1 
ATOM   2765 C CZ  . PHE A 1 368 ? 77.603  106.457 116.736 1.00 73.33  ? 368 PHE A CZ  1 
ATOM   2766 N N   . ARG A 1 369 ? 79.799  104.477 123.334 1.00 78.03  ? 369 ARG A N   1 
ATOM   2767 C CA  . ARG A 1 369 ? 79.774  103.772 124.615 1.00 79.88  ? 369 ARG A CA  1 
ATOM   2768 C C   . ARG A 1 369 ? 81.024  104.172 125.391 1.00 82.48  ? 369 ARG A C   1 
ATOM   2769 O O   . ARG A 1 369 ? 82.056  103.503 125.307 1.00 82.44  ? 369 ARG A O   1 
ATOM   2770 C CB  . ARG A 1 369 ? 79.700  102.261 124.409 1.00 79.40  ? 369 ARG A CB  1 
ATOM   2771 C CG  . ARG A 1 369 ? 78.286  101.713 124.337 1.00 79.44  ? 369 ARG A CG  1 
ATOM   2772 C CD  . ARG A 1 369 ? 78.291  100.198 124.146 1.00 80.04  ? 369 ARG A CD  1 
ATOM   2773 N NE  . ARG A 1 369 ? 78.556  99.457  125.375 1.00 81.54  ? 369 ARG A NE  1 
ATOM   2774 C CZ  . ARG A 1 369 ? 77.759  99.417  126.437 1.00 82.51  ? 369 ARG A CZ  1 
ATOM   2775 N NH1 . ARG A 1 369 ? 76.578  100.016 126.445 1.00 83.07  ? 369 ARG A NH1 1 
ATOM   2776 N NH2 . ARG A 1 369 ? 78.149  98.740  127.513 1.00 82.78  ? 369 ARG A NH2 1 
ATOM   2777 N N   . GLN A 1 370 ? 80.918  105.268 126.149 1.00 86.14  ? 370 GLN A N   1 
ATOM   2778 C CA  . GLN A 1 370 ? 82.075  105.803 126.861 1.00 89.37  ? 370 GLN A CA  1 
ATOM   2779 C C   . GLN A 1 370 ? 82.567  104.846 127.941 1.00 91.99  ? 370 GLN A C   1 
ATOM   2780 O O   . GLN A 1 370 ? 83.777  104.648 128.096 1.00 92.43  ? 370 GLN A O   1 
ATOM   2781 C CB  . GLN A 1 370 ? 81.734  107.166 127.461 1.00 89.67  ? 370 GLN A CB  1 
ATOM   2782 C CG  . GLN A 1 370 ? 81.148  108.146 126.459 1.00 90.05  ? 370 GLN A CG  1 
ATOM   2783 C CD  . GLN A 1 370 ? 81.271  109.586 126.910 1.00 92.45  ? 370 GLN A CD  1 
ATOM   2784 O OE1 . GLN A 1 370 ? 82.272  109.977 127.509 1.00 94.38  ? 370 GLN A OE1 1 
ATOM   2785 N NE2 . GLN A 1 370 ? 80.251  110.386 126.622 1.00 94.32  ? 370 GLN A NE2 1 
ATOM   2786 N N   . ASN A 1 371 ? 81.650  104.242 128.693 1.00 93.85  ? 371 ASN A N   1 
ATOM   2787 C CA  . ASN A 1 371 ? 82.004  103.307 129.760 1.00 94.52  ? 371 ASN A CA  1 
ATOM   2788 C C   . ASN A 1 371 ? 81.746  101.895 129.244 1.00 93.19  ? 371 ASN A C   1 
ATOM   2789 O O   . ASN A 1 371 ? 80.638  101.367 129.346 1.00 92.27  ? 371 ASN A O   1 
ATOM   2790 C CB  . ASN A 1 371 ? 81.210  103.604 131.027 1.00 96.77  ? 371 ASN A CB  1 
ATOM   2791 C CG  . ASN A 1 371 ? 81.812  102.953 132.257 1.00 99.11  ? 371 ASN A CG  1 
ATOM   2792 O OD1 . ASN A 1 371 ? 82.861  102.314 132.184 1.00 100.05 ? 371 ASN A OD1 1 
ATOM   2793 N ND2 . ASN A 1 371 ? 81.149  103.116 133.396 1.00 100.95 ? 371 ASN A ND2 1 
ATOM   2794 N N   . ALA A 1 372 ? 82.788  101.279 128.688 1.00 92.13  ? 372 ALA A N   1 
ATOM   2795 C CA  . ALA A 1 372 ? 82.689  99.940  128.129 1.00 91.54  ? 372 ALA A CA  1 
ATOM   2796 C C   . ALA A 1 372 ? 83.908  99.128  128.537 1.00 91.77  ? 372 ALA A C   1 
ATOM   2797 O O   . ALA A 1 372 ? 85.009  99.664  128.687 1.00 95.16  ? 372 ALA A O   1 
ATOM   2798 C CB  . ALA A 1 372 ? 82.570  99.973  126.600 1.00 90.56  ? 372 ALA A CB  1 
ATOM   2799 N N   . SER A 1 373 ? 83.696  97.827  128.717 1.00 90.16  ? 373 SER A N   1 
ATOM   2800 C CA  . SER A 1 373 ? 84.782  96.929  129.081 1.00 87.18  ? 373 SER A CA  1 
ATOM   2801 C C   . SER A 1 373 ? 85.768  96.783  127.928 1.00 84.29  ? 373 SER A C   1 
ATOM   2802 O O   . SER A 1 373 ? 85.420  96.952  126.757 1.00 82.05  ? 373 SER A O   1 
ATOM   2803 C CB  . SER A 1 373 ? 84.232  95.560  129.480 1.00 87.44  ? 373 SER A CB  1 
ATOM   2804 O OG  . SER A 1 373 ? 83.497  94.976  128.420 1.00 88.79  ? 373 SER A OG  1 
ATOM   2805 N N   . ASP A 1 374 ? 87.018  96.469  128.276 1.00 82.17  ? 374 ASP A N   1 
ATOM   2806 C CA  . ASP A 1 374 ? 88.072  96.377  127.271 1.00 81.92  ? 374 ASP A CA  1 
ATOM   2807 C C   . ASP A 1 374 ? 87.876  95.181  126.347 1.00 79.03  ? 374 ASP A C   1 
ATOM   2808 O O   . ASP A 1 374 ? 88.235  95.250  125.165 1.00 78.63  ? 374 ASP A O   1 
ATOM   2809 C CB  . ASP A 1 374 ? 89.436  96.304  127.951 1.00 84.68  ? 374 ASP A CB  1 
ATOM   2810 C CG  . ASP A 1 374 ? 90.542  96.874  127.093 1.00 87.90  ? 374 ASP A CG  1 
ATOM   2811 O OD1 . ASP A 1 374 ? 90.934  96.213  126.110 1.00 90.52  ? 374 ASP A OD1 1 
ATOM   2812 O OD2 . ASP A 1 374 ? 91.019  97.986  127.403 1.00 90.09  ? 374 ASP A OD2 1 
ATOM   2813 N N   . LYS A 1 375 ? 87.322  94.082  126.866 1.00 76.46  ? 375 LYS A N   1 
ATOM   2814 C CA  . LYS A 1 375 ? 87.064  92.913  126.030 1.00 75.07  ? 375 LYS A CA  1 
ATOM   2815 C C   . LYS A 1 375 ? 86.038  93.226  124.949 1.00 73.94  ? 375 LYS A C   1 
ATOM   2816 O O   . LYS A 1 375 ? 86.162  92.761  123.809 1.00 73.45  ? 375 LYS A O   1 
ATOM   2817 C CB  . LYS A 1 375 ? 86.594  91.744  126.896 1.00 74.63  ? 375 LYS A CB  1 
ATOM   2818 C CG  . LYS A 1 375 ? 87.642  91.229  127.866 1.00 74.51  ? 375 LYS A CG  1 
ATOM   2819 C CD  . LYS A 1 375 ? 87.083  90.119  128.742 1.00 74.70  ? 375 LYS A CD  1 
ATOM   2820 C CE  . LYS A 1 375 ? 88.137  89.587  129.699 1.00 74.89  ? 375 LYS A CE  1 
ATOM   2821 N NZ  . LYS A 1 375 ? 88.670  90.657  130.586 1.00 75.43  ? 375 LYS A NZ  1 
ATOM   2822 N N   . GLU A 1 376 ? 85.016  94.015  125.291 1.00 71.97  ? 376 GLU A N   1 
ATOM   2823 C CA  . GLU A 1 376 ? 84.032  94.433  124.298 1.00 69.50  ? 376 GLU A CA  1 
ATOM   2824 C C   . GLU A 1 376 ? 84.677  95.289  123.215 1.00 67.11  ? 376 GLU A C   1 
ATOM   2825 O O   . GLU A 1 376 ? 84.344  95.159  122.032 1.00 65.62  ? 376 GLU A O   1 
ATOM   2826 C CB  . GLU A 1 376 ? 82.889  95.186  124.981 1.00 69.99  ? 376 GLU A CB  1 
ATOM   2827 C CG  . GLU A 1 376 ? 81.932  95.884  124.027 1.00 71.09  ? 376 GLU A CG  1 
ATOM   2828 C CD  . GLU A 1 376 ? 81.121  96.969  124.705 1.00 72.35  ? 376 GLU A CD  1 
ATOM   2829 O OE1 . GLU A 1 376 ? 80.714  96.771  125.869 1.00 73.98  ? 376 GLU A OE1 1 
ATOM   2830 O OE2 . GLU A 1 376 ? 80.888  98.021  124.073 1.00 73.07  ? 376 GLU A OE2 1 
ATOM   2831 N N   . ILE A 1 377 ? 85.617  96.158  123.597 1.00 65.01  ? 377 ILE A N   1 
ATOM   2832 C CA  . ILE A 1 377 ? 86.304  96.991  122.614 1.00 62.54  ? 377 ILE A CA  1 
ATOM   2833 C C   . ILE A 1 377 ? 87.186  96.140  121.707 1.00 60.17  ? 377 ILE A C   1 
ATOM   2834 O O   . ILE A 1 377 ? 87.261  96.379  120.499 1.00 59.72  ? 377 ILE A O   1 
ATOM   2835 C CB  . ILE A 1 377 ? 87.108  98.101  123.314 1.00 61.97  ? 377 ILE A CB  1 
ATOM   2836 C CG1 . ILE A 1 377 ? 86.194  98.927  124.219 1.00 61.81  ? 377 ILE A CG1 1 
ATOM   2837 C CG2 . ILE A 1 377 ? 87.770  99.007  122.293 1.00 61.07  ? 377 ILE A CG2 1 
ATOM   2838 C CD1 . ILE A 1 377 ? 85.046  99.580  123.487 1.00 61.76  ? 377 ILE A CD1 1 
ATOM   2839 N N   . VAL A 1 378 ? 87.854  95.127  122.265 1.00 57.79  ? 378 VAL A N   1 
ATOM   2840 C CA  . VAL A 1 378 ? 88.664  94.231  121.438 1.00 57.03  ? 378 VAL A CA  1 
ATOM   2841 C C   . VAL A 1 378 ? 87.784  93.458  120.458 1.00 57.59  ? 378 VAL A C   1 
ATOM   2842 O O   . VAL A 1 378 ? 88.121  93.311  119.273 1.00 58.85  ? 378 VAL A O   1 
ATOM   2843 C CB  . VAL A 1 378 ? 89.493  93.287  122.327 1.00 56.25  ? 378 VAL A CB  1 
ATOM   2844 C CG1 . VAL A 1 378 ? 90.185  92.229  121.489 1.00 56.15  ? 378 VAL A CG1 1 
ATOM   2845 C CG2 . VAL A 1 378 ? 90.516  94.077  123.118 1.00 56.50  ? 378 VAL A CG2 1 
ATOM   2846 N N   . TRP A 1 379 ? 86.637  92.963  120.931 1.00 56.77  ? 379 TRP A N   1 
ATOM   2847 C CA  . TRP A 1 379 ? 85.752  92.199  120.058 1.00 55.17  ? 379 TRP A CA  1 
ATOM   2848 C C   . TRP A 1 379 ? 85.143  93.076  118.968 1.00 52.54  ? 379 TRP A C   1 
ATOM   2849 O O   . TRP A 1 379 ? 85.020  92.643  117.814 1.00 52.07  ? 379 TRP A O   1 
ATOM   2850 C CB  . TRP A 1 379 ? 84.660  91.519  120.881 1.00 56.57  ? 379 TRP A CB  1 
ATOM   2851 C CG  . TRP A 1 379 ? 85.105  90.229  121.505 1.00 58.44  ? 379 TRP A CG  1 
ATOM   2852 C CD1 . TRP A 1 379 ? 85.142  89.937  122.837 1.00 59.58  ? 379 TRP A CD1 1 
ATOM   2853 C CD2 . TRP A 1 379 ? 85.579  89.058  120.825 1.00 59.88  ? 379 TRP A CD2 1 
ATOM   2854 N NE1 . TRP A 1 379 ? 85.609  88.660  123.029 1.00 60.69  ? 379 TRP A NE1 1 
ATOM   2855 C CE2 . TRP A 1 379 ? 85.884  88.099  121.811 1.00 60.68  ? 379 TRP A CE2 1 
ATOM   2856 C CE3 . TRP A 1 379 ? 85.774  88.727  119.480 1.00 60.15  ? 379 TRP A CE3 1 
ATOM   2857 C CZ2 . TRP A 1 379 ? 86.374  86.833  121.494 1.00 60.72  ? 379 TRP A CZ2 1 
ATOM   2858 C CZ3 . TRP A 1 379 ? 86.261  87.471  119.169 1.00 60.37  ? 379 TRP A CZ3 1 
ATOM   2859 C CH2 . TRP A 1 379 ? 86.554  86.540  120.171 1.00 60.57  ? 379 TRP A CH2 1 
ATOM   2860 N N   . VAL A 1 380 ? 84.760  94.311  119.307 1.00 49.81  ? 380 VAL A N   1 
ATOM   2861 C CA  . VAL A 1 380 ? 84.220  95.195  118.281 1.00 48.35  ? 380 VAL A CA  1 
ATOM   2862 C C   . VAL A 1 380 ? 85.323  95.629  117.324 1.00 47.08  ? 380 VAL A C   1 
ATOM   2863 O O   . VAL A 1 380 ? 85.061  95.858  116.142 1.00 46.94  ? 380 VAL A O   1 
ATOM   2864 C CB  . VAL A 1 380 ? 83.474  96.395  118.905 1.00 48.26  ? 380 VAL A CB  1 
ATOM   2865 C CG1 . VAL A 1 380 ? 84.426  97.434  119.456 1.00 48.77  ? 380 VAL A CG1 1 
ATOM   2866 C CG2 . VAL A 1 380 ? 82.536  97.022  117.887 1.00 48.26  ? 380 VAL A CG2 1 
ATOM   2867 N N   . MET A 1 381 ? 86.573  95.693  117.793 1.00 46.63  ? 381 MET A N   1 
ATOM   2868 C CA  . MET A 1 381 ? 87.701  95.926  116.898 1.00 47.01  ? 381 MET A CA  1 
ATOM   2869 C C   . MET A 1 381 ? 87.834  94.801  115.883 1.00 45.33  ? 381 MET A C   1 
ATOM   2870 O O   . MET A 1 381 ? 88.020  95.045  114.686 1.00 45.36  ? 381 MET A O   1 
ATOM   2871 C CB  . MET A 1 381 ? 88.989  96.052  117.709 1.00 49.72  ? 381 MET A CB  1 
ATOM   2872 C CG  . MET A 1 381 ? 90.228  96.327  116.883 1.00 51.78  ? 381 MET A CG  1 
ATOM   2873 S SD  . MET A 1 381 ? 90.588  98.082  116.823 1.00 54.62  ? 381 MET A SD  1 
ATOM   2874 C CE  . MET A 1 381 ? 90.733  98.403  118.577 1.00 55.09  ? 381 MET A CE  1 
ATOM   2875 N N   . ARG A 1 382 ? 87.737  93.556  116.350 1.00 44.13  ? 382 ARG A N   1 
ATOM   2876 C CA  . ARG A 1 382 ? 87.897  92.418  115.448 1.00 43.74  ? 382 ARG A CA  1 
ATOM   2877 C C   . ARG A 1 382 ? 86.754  92.341  114.438 1.00 42.95  ? 382 ARG A C   1 
ATOM   2878 O O   . ARG A 1 382 ? 86.988  92.147  113.234 1.00 42.78  ? 382 ARG A O   1 
ATOM   2879 C CB  . ARG A 1 382 ? 87.998  91.128  116.259 1.00 44.63  ? 382 ARG A CB  1 
ATOM   2880 C CG  . ARG A 1 382 ? 89.266  91.040  117.092 1.00 45.47  ? 382 ARG A CG  1 
ATOM   2881 C CD  . ARG A 1 382 ? 89.386  89.708  117.807 1.00 46.02  ? 382 ARG A CD  1 
ATOM   2882 N NE  . ARG A 1 382 ? 90.533  89.685  118.706 1.00 46.17  ? 382 ARG A NE  1 
ATOM   2883 C CZ  . ARG A 1 382 ? 91.766  89.363  118.343 1.00 45.80  ? 382 ARG A CZ  1 
ATOM   2884 N NH1 . ARG A 1 382 ? 92.057  89.044  117.093 1.00 46.16  ? 382 ARG A NH1 1 
ATOM   2885 N NH2 . ARG A 1 382 ? 92.733  89.367  119.256 1.00 45.26  ? 382 ARG A NH2 1 
ATOM   2886 N N   . ILE A 1 383 ? 85.512  92.518  114.899 1.00 42.31  ? 383 ILE A N   1 
ATOM   2887 C CA  . ILE A 1 383 ? 84.394  92.460  113.961 1.00 41.00  ? 383 ILE A CA  1 
ATOM   2888 C C   . ILE A 1 383 ? 84.393  93.675  113.040 1.00 40.22  ? 383 ILE A C   1 
ATOM   2889 O O   . ILE A 1 383 ? 83.936  93.584  111.897 1.00 38.95  ? 383 ILE A O   1 
ATOM   2890 C CB  . ILE A 1 383 ? 83.045  92.295  114.692 1.00 40.69  ? 383 ILE A CB  1 
ATOM   2891 C CG1 . ILE A 1 383 ? 82.629  93.582  115.401 1.00 40.74  ? 383 ILE A CG1 1 
ATOM   2892 C CG2 . ILE A 1 383 ? 83.099  91.126  115.662 1.00 40.61  ? 383 ILE A CG2 1 
ATOM   2893 C CD1 . ILE A 1 383 ? 81.236  93.529  115.981 1.00 40.91  ? 383 ILE A CD1 1 
ATOM   2894 N N   . THR A 1 384 ? 84.934  94.815  113.486 1.00 40.57  ? 384 THR A N   1 
ATOM   2895 C CA  . THR A 1 384 ? 85.046  95.971  112.605 1.00 40.48  ? 384 THR A CA  1 
ATOM   2896 C C   . THR A 1 384 ? 86.109  95.747  111.540 1.00 39.89  ? 384 THR A C   1 
ATOM   2897 O O   . THR A 1 384 ? 85.932  96.160  110.391 1.00 39.79  ? 384 THR A O   1 
ATOM   2898 C CB  . THR A 1 384 ? 85.358  97.227  113.416 1.00 40.98  ? 384 THR A CB  1 
ATOM   2899 O OG1 . THR A 1 384 ? 84.416  97.350  114.487 1.00 41.45  ? 384 THR A OG1 1 
ATOM   2900 C CG2 . THR A 1 384 ? 85.271  98.459  112.537 1.00 41.08  ? 384 THR A CG2 1 
ATOM   2901 N N   . VAL A 1 385 ? 87.212  95.085  111.901 1.00 40.04  ? 385 VAL A N   1 
ATOM   2902 C CA  . VAL A 1 385 ? 88.217  94.710  110.908 1.00 40.56  ? 385 VAL A CA  1 
ATOM   2903 C C   . VAL A 1 385 ? 87.599  93.801  109.854 1.00 40.46  ? 385 VAL A C   1 
ATOM   2904 O O   . VAL A 1 385 ? 87.771  94.013  108.646 1.00 41.23  ? 385 VAL A O   1 
ATOM   2905 C CB  . VAL A 1 385 ? 89.424  94.040  111.588 1.00 41.02  ? 385 VAL A CB  1 
ATOM   2906 C CG1 . VAL A 1 385 ? 90.272  93.321  110.565 1.00 40.95  ? 385 VAL A CG1 1 
ATOM   2907 C CG2 . VAL A 1 385 ? 90.265  95.064  112.321 1.00 41.39  ? 385 VAL A CG2 1 
ATOM   2908 N N   . PHE A 1 386 ? 86.842  92.792  110.298 1.00 40.30  ? 386 PHE A N   1 
ATOM   2909 C CA  . PHE A 1 386 ? 86.224  91.871  109.346 1.00 40.59  ? 386 PHE A CA  1 
ATOM   2910 C C   . PHE A 1 386 ? 85.189  92.570  108.467 1.00 39.95  ? 386 PHE A C   1 
ATOM   2911 O O   . PHE A 1 386 ? 85.150  92.348  107.250 1.00 39.21  ? 386 PHE A O   1 
ATOM   2912 C CB  . PHE A 1 386 ? 85.589  90.694  110.083 1.00 41.48  ? 386 PHE A CB  1 
ATOM   2913 C CG  . PHE A 1 386 ? 84.835  89.758  109.185 1.00 41.99  ? 386 PHE A CG  1 
ATOM   2914 C CD1 . PHE A 1 386 ? 85.514  88.870  108.368 1.00 42.26  ? 386 PHE A CD1 1 
ATOM   2915 C CD2 . PHE A 1 386 ? 83.450  89.763  109.158 1.00 42.11  ? 386 PHE A CD2 1 
ATOM   2916 C CE1 . PHE A 1 386 ? 84.826  88.007  107.539 1.00 42.56  ? 386 PHE A CE1 1 
ATOM   2917 C CE2 . PHE A 1 386 ? 82.757  88.903  108.331 1.00 42.21  ? 386 PHE A CE2 1 
ATOM   2918 C CZ  . PHE A 1 386 ? 83.446  88.023  107.521 1.00 42.50  ? 386 PHE A CZ  1 
ATOM   2919 N N   . VAL A 1 387 ? 84.347  93.421  109.062 1.00 39.76  ? 387 VAL A N   1 
ATOM   2920 C CA  . VAL A 1 387 ? 83.308  94.112  108.305 1.00 39.48  ? 387 VAL A CA  1 
ATOM   2921 C C   . VAL A 1 387 ? 83.925  95.088  107.310 1.00 40.41  ? 387 VAL A C   1 
ATOM   2922 O O   . VAL A 1 387 ? 83.471  95.193  106.166 1.00 40.43  ? 387 VAL A O   1 
ATOM   2923 C CB  . VAL A 1 387 ? 82.328  94.808  109.269 1.00 38.51  ? 387 VAL A CB  1 
ATOM   2924 C CG1 . VAL A 1 387 ? 81.562  95.921  108.573 1.00 37.52  ? 387 VAL A CG1 1 
ATOM   2925 C CG2 . VAL A 1 387 ? 81.361  93.793  109.852 1.00 38.64  ? 387 VAL A CG2 1 
ATOM   2926 N N   . PHE A 1 388 ? 84.974  95.806  107.719 1.00 41.99  ? 388 PHE A N   1 
ATOM   2927 C CA  . PHE A 1 388 ? 85.633  96.744  106.817 1.00 42.28  ? 388 PHE A CA  1 
ATOM   2928 C C   . PHE A 1 388 ? 86.336  96.016  105.681 1.00 42.05  ? 388 PHE A C   1 
ATOM   2929 O O   . PHE A 1 388 ? 86.327  96.491  104.541 1.00 42.49  ? 388 PHE A O   1 
ATOM   2930 C CB  . PHE A 1 388 ? 86.617  97.614  107.595 1.00 42.81  ? 388 PHE A CB  1 
ATOM   2931 C CG  . PHE A 1 388 ? 85.988  98.819  108.236 1.00 43.55  ? 388 PHE A CG  1 
ATOM   2932 C CD1 . PHE A 1 388 ? 84.611  98.921  108.358 1.00 44.44  ? 388 PHE A CD1 1 
ATOM   2933 C CD2 . PHE A 1 388 ? 86.775  99.836  108.743 1.00 43.99  ? 388 PHE A CD2 1 
ATOM   2934 C CE1 . PHE A 1 388 ? 84.033  100.023 108.954 1.00 44.86  ? 388 PHE A CE1 1 
ATOM   2935 C CE2 . PHE A 1 388 ? 86.202  100.936 109.346 1.00 44.71  ? 388 PHE A CE2 1 
ATOM   2936 C CZ  . PHE A 1 388 ? 84.829  101.032 109.448 1.00 44.77  ? 388 PHE A CZ  1 
ATOM   2937 N N   . GLY A 1 389 ? 86.939  94.858  105.962 1.00 41.99  ? 389 GLY A N   1 
ATOM   2938 C CA  . GLY A 1 389 ? 87.528  94.070  104.890 1.00 42.36  ? 389 GLY A CA  1 
ATOM   2939 C C   . GLY A 1 389 ? 86.494  93.564  103.903 1.00 42.95  ? 389 GLY A C   1 
ATOM   2940 O O   . GLY A 1 389 ? 86.702  93.616  102.685 1.00 42.99  ? 389 GLY A O   1 
ATOM   2941 N N   . ALA A 1 390 ? 85.357  93.079  104.414 1.00 43.29  ? 390 ALA A N   1 
ATOM   2942 C CA  . ALA A 1 390 ? 84.286  92.617  103.537 1.00 43.37  ? 390 ALA A CA  1 
ATOM   2943 C C   . ALA A 1 390 ? 83.715  93.761  102.708 1.00 43.04  ? 390 ALA A C   1 
ATOM   2944 O O   . ALA A 1 390 ? 83.442  93.593  101.515 1.00 43.10  ? 390 ALA A O   1 
ATOM   2945 C CB  . ALA A 1 390 ? 83.186  91.946  104.357 1.00 43.60  ? 390 ALA A CB  1 
ATOM   2946 N N   . SER A 1 391 ? 83.533  94.933  103.320 1.00 42.63  ? 391 SER A N   1 
ATOM   2947 C CA  . SER A 1 391 ? 83.032  96.090  102.586 1.00 42.73  ? 391 SER A CA  1 
ATOM   2948 C C   . SER A 1 391 ? 84.023  96.545  101.523 1.00 42.36  ? 391 SER A C   1 
ATOM   2949 O O   . SER A 1 391 ? 83.623  96.889  100.406 1.00 42.61  ? 391 SER A O   1 
ATOM   2950 C CB  . SER A 1 391 ? 82.721  97.234  103.549 1.00 43.11  ? 391 SER A CB  1 
ATOM   2951 O OG  . SER A 1 391 ? 81.575  96.945  104.329 1.00 44.93  ? 391 SER A OG  1 
ATOM   2952 N N   . ALA A 1 392 ? 85.319  96.544  101.848 1.00 42.39  ? 392 ALA A N   1 
ATOM   2953 C CA  . ALA A 1 392 ? 86.331  96.947  100.879 1.00 41.69  ? 392 ALA A CA  1 
ATOM   2954 C C   . ALA A 1 392 ? 86.371  95.996  99.691  1.00 40.64  ? 392 ALA A C   1 
ATOM   2955 O O   . ALA A 1 392 ? 86.410  96.441  98.538  1.00 39.66  ? 392 ALA A O   1 
ATOM   2956 C CB  . ALA A 1 392 ? 87.701  97.025  101.549 1.00 41.95  ? 392 ALA A CB  1 
ATOM   2957 N N   . THR A 1 393 ? 86.333  94.683  99.942  1.00 40.23  ? 393 THR A N   1 
ATOM   2958 C CA  . THR A 1 393 ? 86.383  93.754  98.816  1.00 40.50  ? 393 THR A CA  1 
ATOM   2959 C C   . THR A 1 393 ? 85.076  93.747  98.025  1.00 40.49  ? 393 THR A C   1 
ATOM   2960 O O   . THR A 1 393 ? 85.106  93.599  96.798  1.00 40.28  ? 393 THR A O   1 
ATOM   2961 C CB  . THR A 1 393 ? 86.761  92.344  99.286  1.00 40.94  ? 393 THR A CB  1 
ATOM   2962 O OG1 . THR A 1 393 ? 86.993  91.507  98.146  1.00 41.27  ? 393 THR A OG1 1 
ATOM   2963 C CG2 . THR A 1 393 ? 85.688  91.716  100.159 1.00 40.96  ? 393 THR A CG2 1 
ATOM   2964 N N   . ALA A 1 394 ? 83.930  93.955  98.685  1.00 40.24  ? 394 ALA A N   1 
ATOM   2965 C CA  . ALA A 1 394 ? 82.665  94.021  97.961  1.00 39.91  ? 394 ALA A CA  1 
ATOM   2966 C C   . ALA A 1 394 ? 82.588  95.273  97.100  1.00 39.91  ? 394 ALA A C   1 
ATOM   2967 O O   . ALA A 1 394 ? 82.062  95.232  95.984  1.00 40.30  ? 394 ALA A O   1 
ATOM   2968 C CB  . ALA A 1 394 ? 81.494  93.970  98.941  1.00 39.56  ? 394 ALA A CB  1 
ATOM   2969 N N   . MET A 1 395 ? 83.105  96.394  97.603  1.00 40.43  ? 395 MET A N   1 
ATOM   2970 C CA  . MET A 1 395 ? 83.137  97.619  96.814  1.00 41.31  ? 395 MET A CA  1 
ATOM   2971 C C   . MET A 1 395 ? 84.139  97.517  95.672  1.00 41.28  ? 395 MET A C   1 
ATOM   2972 O O   . MET A 1 395 ? 83.918  98.079  94.594  1.00 41.28  ? 395 MET A O   1 
ATOM   2973 C CB  . MET A 1 395 ? 83.464  98.798  97.725  1.00 42.30  ? 395 MET A CB  1 
ATOM   2974 C CG  . MET A 1 395 ? 83.272  100.158 97.107  1.00 42.96  ? 395 MET A CG  1 
ATOM   2975 S SD  . MET A 1 395 ? 83.842  101.418 98.254  1.00 45.19  ? 395 MET A SD  1 
ATOM   2976 C CE  . MET A 1 395 ? 83.181  100.785 99.791  1.00 44.50  ? 395 MET A CE  1 
ATOM   2977 N N   . ALA A 1 396 ? 85.252  96.812  95.893  1.00 41.38  ? 396 ALA A N   1 
ATOM   2978 C CA  . ALA A 1 396 ? 86.220  96.603  94.823  1.00 41.33  ? 396 ALA A CA  1 
ATOM   2979 C C   . ALA A 1 396 ? 85.653  95.717  93.723  1.00 40.93  ? 396 ALA A C   1 
ATOM   2980 O O   . ALA A 1 396 ? 85.901  95.956  92.536  1.00 39.59  ? 396 ALA A O   1 
ATOM   2981 C CB  . ALA A 1 396 ? 87.498  95.990  95.389  1.00 41.79  ? 396 ALA A CB  1 
ATOM   2982 N N   . LEU A 1 397 ? 84.894  94.689  94.096  1.00 41.57  ? 397 LEU A N   1 
ATOM   2983 C CA  . LEU A 1 397 ? 84.438  93.695  93.135  1.00 42.67  ? 397 LEU A CA  1 
ATOM   2984 C C   . LEU A 1 397 ? 83.131  94.067  92.445  1.00 43.46  ? 397 LEU A C   1 
ATOM   2985 O O   . LEU A 1 397 ? 82.963  93.772  91.256  1.00 43.21  ? 397 LEU A O   1 
ATOM   2986 C CB  . LEU A 1 397 ? 84.285  92.344  93.837  1.00 42.90  ? 397 LEU A CB  1 
ATOM   2987 C CG  . LEU A 1 397 ? 83.875  91.174  92.956  1.00 43.51  ? 397 LEU A CG  1 
ATOM   2988 C CD1 . LEU A 1 397 ? 84.955  90.953  91.925  1.00 44.03  ? 397 LEU A CD1 1 
ATOM   2989 C CD2 . LEU A 1 397 ? 83.669  89.933  93.803  1.00 43.31  ? 397 LEU A CD2 1 
ATOM   2990 N N   . LEU A 1 398 ? 82.211  94.725  93.150  1.00 45.25  ? 398 LEU A N   1 
ATOM   2991 C CA  . LEU A 1 398 ? 80.870  94.969  92.638  1.00 46.57  ? 398 LEU A CA  1 
ATOM   2992 C C   . LEU A 1 398 ? 80.730  96.303  91.917  1.00 48.07  ? 398 LEU A C   1 
ATOM   2993 O O   . LEU A 1 398 ? 79.812  96.455  91.103  1.00 48.19  ? 398 LEU A O   1 
ATOM   2994 C CB  . LEU A 1 398 ? 79.862  94.886  93.798  1.00 46.29  ? 398 LEU A CB  1 
ATOM   2995 C CG  . LEU A 1 398 ? 78.342  94.893  93.604  1.00 46.01  ? 398 LEU A CG  1 
ATOM   2996 C CD1 . LEU A 1 398 ? 77.699  94.067  94.703  1.00 46.04  ? 398 LEU A CD1 1 
ATOM   2997 C CD2 . LEU A 1 398 ? 77.773  96.304  93.638  1.00 45.73  ? 398 LEU A CD2 1 
ATOM   2998 N N   . THR A 1 399 ? 81.622  97.256  92.168  1.00 49.93  ? 399 THR A N   1 
ATOM   2999 C CA  . THR A 1 399 ? 81.529  98.594  91.603  1.00 51.18  ? 399 THR A CA  1 
ATOM   3000 C C   . THR A 1 399 ? 82.611  98.781  90.546  1.00 52.96  ? 399 THR A C   1 
ATOM   3001 O O   . THR A 1 399 ? 83.759  98.370  90.740  1.00 53.60  ? 399 THR A O   1 
ATOM   3002 C CB  . THR A 1 399 ? 81.663  99.654  92.703  1.00 50.94  ? 399 THR A CB  1 
ATOM   3003 O OG1 . THR A 1 399 ? 80.613  99.478  93.661  1.00 51.36  ? 399 THR A OG1 1 
ATOM   3004 C CG2 . THR A 1 399 ? 81.563  101.058 92.129  1.00 50.52  ? 399 THR A CG2 1 
ATOM   3005 N N   . LYS A 1 400 ? 82.234  99.373  89.414  1.00 54.75  ? 400 LYS A N   1 
ATOM   3006 C CA  . LYS A 1 400 ? 83.161  99.656  88.326  1.00 55.96  ? 400 LYS A CA  1 
ATOM   3007 C C   . LYS A 1 400 ? 83.718  101.075 88.365  1.00 57.07  ? 400 LYS A C   1 
ATOM   3008 O O   . LYS A 1 400 ? 84.522  101.432 87.497  1.00 57.58  ? 400 LYS A O   1 
ATOM   3009 C CB  . LYS A 1 400 ? 82.477  99.416  86.976  1.00 55.76  ? 400 LYS A CB  1 
ATOM   3010 C CG  . LYS A 1 400 ? 81.203  100.220 86.777  1.00 55.81  ? 400 LYS A CG  1 
ATOM   3011 C CD  . LYS A 1 400 ? 80.274  99.546  85.783  1.00 56.12  ? 400 LYS A CD  1 
ATOM   3012 C CE  . LYS A 1 400 ? 79.636  98.303  86.379  1.00 56.27  ? 400 LYS A CE  1 
ATOM   3013 N NZ  . LYS A 1 400 ? 78.858  98.616  87.610  1.00 56.44  ? 400 LYS A NZ  1 
ATOM   3014 N N   . THR A 1 401 ? 83.317  101.887 89.342  1.00 57.45  ? 401 THR A N   1 
ATOM   3015 C CA  . THR A 1 401 ? 83.731  103.283 89.400  1.00 57.20  ? 401 THR A CA  1 
ATOM   3016 C C   . THR A 1 401 ? 84.557  103.487 90.668  1.00 56.37  ? 401 THR A C   1 
ATOM   3017 O O   . THR A 1 401 ? 84.322  104.418 91.447  1.00 56.11  ? 401 THR A O   1 
ATOM   3018 C CB  . THR A 1 401 ? 82.505  104.203 89.350  1.00 57.74  ? 401 THR A CB  1 
ATOM   3019 O OG1 . THR A 1 401 ? 81.639  103.763 88.300  1.00 59.58  ? 401 THR A OG1 1 
ATOM   3020 C CG2 . THR A 1 401 ? 82.911  105.636 89.005  1.00 57.47  ? 401 THR A CG2 1 
ATOM   3021 N N   . VAL A 1 402 ? 85.500  102.578 90.914  1.00 55.96  ? 402 VAL A N   1 
ATOM   3022 C CA  . VAL A 1 402 ? 86.279  102.634 92.146  1.00 55.81  ? 402 VAL A CA  1 
ATOM   3023 C C   . VAL A 1 402 ? 87.426  103.632 92.029  1.00 55.05  ? 402 VAL A C   1 
ATOM   3024 O O   . VAL A 1 402 ? 87.742  104.337 92.992  1.00 55.15  ? 402 VAL A O   1 
ATOM   3025 C CB  . VAL A 1 402 ? 86.782  101.228 92.512  1.00 55.81  ? 402 VAL A CB  1 
ATOM   3026 C CG1 . VAL A 1 402 ? 87.520  101.256 93.832  1.00 55.32  ? 402 VAL A CG1 1 
ATOM   3027 C CG2 . VAL A 1 402 ? 85.622  100.265 92.585  1.00 56.16  ? 402 VAL A CG2 1 
ATOM   3028 N N   . TYR A 1 403 ? 88.072  103.707 90.860  1.00 53.55  ? 403 TYR A N   1 
ATOM   3029 C CA  . TYR A 1 403 ? 89.234  104.581 90.702  1.00 52.37  ? 403 TYR A CA  1 
ATOM   3030 C C   . TYR A 1 403 ? 88.857  106.053 90.834  1.00 52.07  ? 403 TYR A C   1 
ATOM   3031 O O   . TYR A 1 403 ? 89.547  106.821 91.517  1.00 52.67  ? 403 TYR A O   1 
ATOM   3032 C CB  . TYR A 1 403 ? 89.905  104.325 89.353  1.00 51.75  ? 403 TYR A CB  1 
ATOM   3033 C CG  . TYR A 1 403 ? 90.611  102.993 89.249  1.00 51.43  ? 403 TYR A CG  1 
ATOM   3034 C CD1 . TYR A 1 403 ? 91.856  102.801 89.829  1.00 50.48  ? 403 TYR A CD1 1 
ATOM   3035 C CD2 . TYR A 1 403 ? 90.037  101.933 88.562  1.00 52.02  ? 403 TYR A CD2 1 
ATOM   3036 C CE1 . TYR A 1 403 ? 92.509  101.589 89.733  1.00 50.70  ? 403 TYR A CE1 1 
ATOM   3037 C CE2 . TYR A 1 403 ? 90.681  100.716 88.461  1.00 52.08  ? 403 TYR A CE2 1 
ATOM   3038 C CZ  . TYR A 1 403 ? 91.917  100.550 89.048  1.00 51.60  ? 403 TYR A CZ  1 
ATOM   3039 O OH  . TYR A 1 403 ? 92.563  99.340  88.951  1.00 51.55  ? 403 TYR A OH  1 
ATOM   3040 N N   . GLY A 1 404 ? 87.769  106.466 90.180  1.00 51.46  ? 404 GLY A N   1 
ATOM   3041 C CA  . GLY A 1 404 ? 87.356  107.858 90.261  1.00 50.49  ? 404 GLY A CA  1 
ATOM   3042 C C   . GLY A 1 404 ? 86.942  108.260 91.662  1.00 49.39  ? 404 GLY A C   1 
ATOM   3043 O O   . GLY A 1 404 ? 87.273  109.353 92.130  1.00 49.97  ? 404 GLY A O   1 
ATOM   3044 N N   . LEU A 1 405 ? 86.221  107.377 92.353  1.00 48.27  ? 405 LEU A N   1 
ATOM   3045 C CA  . LEU A 1 405 ? 85.862  107.637 93.741  1.00 47.95  ? 405 LEU A CA  1 
ATOM   3046 C C   . LEU A 1 405 ? 87.089  107.663 94.642  1.00 47.90  ? 405 LEU A C   1 
ATOM   3047 O O   . LEU A 1 405 ? 87.129  108.440 95.599  1.00 49.48  ? 405 LEU A O   1 
ATOM   3048 C CB  . LEU A 1 405 ? 84.858  106.593 94.223  1.00 48.04  ? 405 LEU A CB  1 
ATOM   3049 C CG  . LEU A 1 405 ? 83.392  106.911 93.928  1.00 48.67  ? 405 LEU A CG  1 
ATOM   3050 C CD1 . LEU A 1 405 ? 82.516  105.687 94.135  1.00 48.80  ? 405 LEU A CD1 1 
ATOM   3051 C CD2 . LEU A 1 405 ? 82.920  108.063 94.798  1.00 48.84  ? 405 LEU A CD2 1 
ATOM   3052 N N   . TRP A 1 406 ? 88.095  106.835 94.351  1.00 47.10  ? 406 TRP A N   1 
ATOM   3053 C CA  . TRP A 1 406 ? 89.342  106.870 95.111  1.00 46.13  ? 406 TRP A CA  1 
ATOM   3054 C C   . TRP A 1 406 ? 90.046  108.210 94.945  1.00 45.90  ? 406 TRP A C   1 
ATOM   3055 O O   . TRP A 1 406 ? 90.511  108.807 95.925  1.00 45.50  ? 406 TRP A O   1 
ATOM   3056 C CB  . TRP A 1 406 ? 90.251  105.722 94.664  1.00 45.55  ? 406 TRP A CB  1 
ATOM   3057 C CG  . TRP A 1 406 ? 91.655  105.781 95.205  1.00 45.02  ? 406 TRP A CG  1 
ATOM   3058 C CD1 . TRP A 1 406 ? 92.038  106.157 96.459  1.00 45.17  ? 406 TRP A CD1 1 
ATOM   3059 C CD2 . TRP A 1 406 ? 92.859  105.446 94.503  1.00 44.44  ? 406 TRP A CD2 1 
ATOM   3060 N NE1 . TRP A 1 406 ? 93.404  106.080 96.580  1.00 45.09  ? 406 TRP A NE1 1 
ATOM   3061 C CE2 . TRP A 1 406 ? 93.931  105.645 95.393  1.00 44.47  ? 406 TRP A CE2 1 
ATOM   3062 C CE3 . TRP A 1 406 ? 93.134  105.000 93.208  1.00 44.15  ? 406 TRP A CE3 1 
ATOM   3063 C CZ2 . TRP A 1 406 ? 95.254  105.412 95.031  1.00 44.06  ? 406 TRP A CZ2 1 
ATOM   3064 C CZ3 . TRP A 1 406 ? 94.447  104.768 92.852  1.00 44.03  ? 406 TRP A CZ3 1 
ATOM   3065 C CH2 . TRP A 1 406 ? 95.490  104.975 93.759  1.00 43.92  ? 406 TRP A CH2 1 
ATOM   3066 N N   . TYR A 1 407 ? 90.131  108.700 93.705  1.00 45.65  ? 407 TYR A N   1 
ATOM   3067 C CA  . TYR A 1 407 ? 90.773  109.990 93.463  1.00 45.43  ? 407 TYR A CA  1 
ATOM   3068 C C   . TYR A 1 407 ? 89.998  111.123 94.126  1.00 44.73  ? 407 TYR A C   1 
ATOM   3069 O O   . TYR A 1 407 ? 90.595  112.018 94.738  1.00 44.62  ? 407 TYR A O   1 
ATOM   3070 C CB  . TYR A 1 407 ? 90.913  110.246 91.962  1.00 45.92  ? 407 TYR A CB  1 
ATOM   3071 C CG  . TYR A 1 407 ? 91.900  109.334 91.271  1.00 47.12  ? 407 TYR A CG  1 
ATOM   3072 C CD1 . TYR A 1 407 ? 93.172  109.141 91.786  1.00 47.64  ? 407 TYR A CD1 1 
ATOM   3073 C CD2 . TYR A 1 407 ? 91.566  108.684 90.090  1.00 48.00  ? 407 TYR A CD2 1 
ATOM   3074 C CE1 . TYR A 1 407 ? 94.078  108.310 91.156  1.00 48.29  ? 407 TYR A CE1 1 
ATOM   3075 C CE2 . TYR A 1 407 ? 92.464  107.852 89.454  1.00 48.49  ? 407 TYR A CE2 1 
ATOM   3076 C CZ  . TYR A 1 407 ? 93.720  107.670 89.990  1.00 48.64  ? 407 TYR A CZ  1 
ATOM   3077 O OH  . TYR A 1 407 ? 94.621  106.845 89.359  1.00 48.83  ? 407 TYR A OH  1 
ATOM   3078 N N   . LEU A 1 408 ? 88.664  111.089 94.028  1.00 44.68  ? 408 LEU A N   1 
ATOM   3079 C CA  . LEU A 1 408 ? 87.843  112.116 94.662  1.00 45.36  ? 408 LEU A CA  1 
ATOM   3080 C C   . LEU A 1 408 ? 87.987  112.088 96.178  1.00 46.71  ? 408 LEU A C   1 
ATOM   3081 O O   . LEU A 1 408 ? 88.078  113.141 96.817  1.00 48.98  ? 408 LEU A O   1 
ATOM   3082 C CB  . LEU A 1 408 ? 86.378  111.941 94.256  1.00 44.81  ? 408 LEU A CB  1 
ATOM   3083 C CG  . LEU A 1 408 ? 85.370  112.987 94.739  1.00 44.70  ? 408 LEU A CG  1 
ATOM   3084 C CD1 . LEU A 1 408 ? 84.416  113.348 93.618  1.00 45.05  ? 408 LEU A CD1 1 
ATOM   3085 C CD2 . LEU A 1 408 ? 84.587  112.482 95.940  1.00 44.54  ? 408 LEU A CD2 1 
ATOM   3086 N N   . SER A 1 409 ? 88.020  110.892 96.772  1.00 46.86  ? 409 SER A N   1 
ATOM   3087 C CA  . SER A 1 409 ? 88.133  110.790 98.222  1.00 46.35  ? 409 SER A CA  1 
ATOM   3088 C C   . SER A 1 409 ? 89.505  111.239 98.707  1.00 46.32  ? 409 SER A C   1 
ATOM   3089 O O   . SER A 1 409 ? 89.612  111.894 99.748  1.00 46.28  ? 409 SER A O   1 
ATOM   3090 C CB  . SER A 1 409 ? 87.844  109.360 98.670  1.00 46.01  ? 409 SER A CB  1 
ATOM   3091 O OG  . SER A 1 409 ? 87.543  109.321 100.052 1.00 45.59  ? 409 SER A OG  1 
ATOM   3092 N N   . SER A 1 410 ? 90.567  110.902 97.968  1.00 46.50  ? 410 SER A N   1 
ATOM   3093 C CA  . SER A 1 410 ? 91.900  111.372 98.338  1.00 47.11  ? 410 SER A CA  1 
ATOM   3094 C C   . SER A 1 410 ? 92.006  112.889 98.222  1.00 47.45  ? 410 SER A C   1 
ATOM   3095 O O   . SER A 1 410 ? 92.595  113.545 99.093  1.00 48.61  ? 410 SER A O   1 
ATOM   3096 C CB  . SER A 1 410 ? 92.955  110.691 97.469  1.00 47.04  ? 410 SER A CB  1 
ATOM   3097 O OG  . SER A 1 410 ? 92.991  109.297 97.717  1.00 47.15  ? 410 SER A OG  1 
ATOM   3098 N N   . ASP A 1 411 ? 91.432  113.462 97.160  1.00 47.27  ? 411 ASP A N   1 
ATOM   3099 C CA  . ASP A 1 411 ? 91.421  114.914 97.014  1.00 47.47  ? 411 ASP A CA  1 
ATOM   3100 C C   . ASP A 1 411 ? 90.631  115.574 98.137  1.00 45.57  ? 411 ASP A C   1 
ATOM   3101 O O   . ASP A 1 411 ? 91.029  116.625 98.652  1.00 44.63  ? 411 ASP A O   1 
ATOM   3102 C CB  . ASP A 1 411 ? 90.840  115.294 95.654  1.00 50.37  ? 411 ASP A CB  1 
ATOM   3103 C CG  . ASP A 1 411 ? 91.025  116.760 95.330  1.00 53.52  ? 411 ASP A CG  1 
ATOM   3104 O OD1 . ASP A 1 411 ? 91.866  117.416 95.979  1.00 55.84  ? 411 ASP A OD1 1 
ATOM   3105 O OD2 . ASP A 1 411 ? 90.324  117.257 94.425  1.00 57.14  ? 411 ASP A OD2 1 
ATOM   3106 N N   . LEU A 1 412 ? 89.512  114.967 98.535  1.00 45.42  ? 412 LEU A N   1 
ATOM   3107 C CA  . LEU A 1 412 ? 88.706  115.530 99.612  1.00 46.32  ? 412 LEU A CA  1 
ATOM   3108 C C   . LEU A 1 412 ? 89.429  115.427 100.951 1.00 46.45  ? 412 LEU A C   1 
ATOM   3109 O O   . LEU A 1 412 ? 89.324  116.333 101.784 1.00 47.53  ? 412 LEU A O   1 
ATOM   3110 C CB  . LEU A 1 412 ? 87.344  114.832 99.655  1.00 46.37  ? 412 LEU A CB  1 
ATOM   3111 C CG  . LEU A 1 412 ? 86.203  115.416 100.491 1.00 46.65  ? 412 LEU A CG  1 
ATOM   3112 C CD1 . LEU A 1 412 ? 84.884  115.052 99.842  1.00 46.87  ? 412 LEU A CD1 1 
ATOM   3113 C CD2 . LEU A 1 412 ? 86.223  114.915 101.923 1.00 46.71  ? 412 LEU A CD2 1 
ATOM   3114 N N   . VAL A 1 413 ? 90.166  114.335 101.174 1.00 45.73  ? 413 VAL A N   1 
ATOM   3115 C CA  . VAL A 1 413 ? 90.979  114.211 102.383 1.00 45.02  ? 413 VAL A CA  1 
ATOM   3116 C C   . VAL A 1 413 ? 92.037  115.305 102.422 1.00 44.31  ? 413 VAL A C   1 
ATOM   3117 O O   . VAL A 1 413 ? 92.216  115.979 103.443 1.00 42.86  ? 413 VAL A O   1 
ATOM   3118 C CB  . VAL A 1 413 ? 91.613  112.810 102.467 1.00 44.87  ? 413 VAL A CB  1 
ATOM   3119 C CG1 . VAL A 1 413 ? 92.749  112.795 103.474 1.00 44.80  ? 413 VAL A CG1 1 
ATOM   3120 C CG2 . VAL A 1 413 ? 90.567  111.785 102.858 1.00 44.86  ? 413 VAL A CG2 1 
ATOM   3121 N N   . TYR A 1 414 ? 92.720  115.524 101.296 1.00 44.48  ? 414 TYR A N   1 
ATOM   3122 C CA  . TYR A 1 414 ? 93.720  116.587 101.217 1.00 44.69  ? 414 TYR A CA  1 
ATOM   3123 C C   . TYR A 1 414 ? 93.112  117.962 101.470 1.00 43.63  ? 414 TYR A C   1 
ATOM   3124 O O   . TYR A 1 414 ? 93.712  118.796 102.157 1.00 43.71  ? 414 TYR A O   1 
ATOM   3125 C CB  . TYR A 1 414 ? 94.400  116.551 99.852  1.00 46.09  ? 414 TYR A CB  1 
ATOM   3126 C CG  . TYR A 1 414 ? 95.052  117.849 99.436  1.00 47.55  ? 414 TYR A CG  1 
ATOM   3127 C CD1 . TYR A 1 414 ? 96.209  118.305 100.050 1.00 49.36  ? 414 TYR A CD1 1 
ATOM   3128 C CD2 . TYR A 1 414 ? 94.508  118.615 98.415  1.00 47.80  ? 414 TYR A CD2 1 
ATOM   3129 C CE1 . TYR A 1 414 ? 96.802  119.491 99.657  1.00 50.37  ? 414 TYR A CE1 1 
ATOM   3130 C CE2 . TYR A 1 414 ? 95.092  119.793 98.017  1.00 48.48  ? 414 TYR A CE2 1 
ATOM   3131 C CZ  . TYR A 1 414 ? 96.236  120.229 98.639  1.00 49.93  ? 414 TYR A CZ  1 
ATOM   3132 O OH  . TYR A 1 414 ? 96.809  121.408 98.231  1.00 51.24  ? 414 TYR A OH  1 
ATOM   3133 N N   . ILE A 1 415 ? 91.929  118.221 100.912 1.00 42.63  ? 415 ILE A N   1 
ATOM   3134 C CA  . ILE A 1 415 ? 91.308  119.534 101.062 1.00 41.64  ? 415 ILE A CA  1 
ATOM   3135 C C   . ILE A 1 415 ? 90.819  119.751 102.493 1.00 41.16  ? 415 ILE A C   1 
ATOM   3136 O O   . ILE A 1 415 ? 90.950  120.849 103.045 1.00 40.88  ? 415 ILE A O   1 
ATOM   3137 C CB  . ILE A 1 415 ? 90.179  119.701 100.027 1.00 41.35  ? 415 ILE A CB  1 
ATOM   3138 C CG1 . ILE A 1 415 ? 90.775  119.919 98.636  1.00 41.22  ? 415 ILE A CG1 1 
ATOM   3139 C CG2 . ILE A 1 415 ? 89.265  120.859 100.380 1.00 41.36  ? 415 ILE A CG2 1 
ATOM   3140 C CD1 . ILE A 1 415 ? 89.747  120.134 97.560  1.00 41.26  ? 415 ILE A CD1 1 
ATOM   3141 N N   . VAL A 1 416 ? 90.273  118.713 103.126 1.00 41.10  ? 416 VAL A N   1 
ATOM   3142 C CA  . VAL A 1 416 ? 89.612  118.879 104.416 1.00 41.50  ? 416 VAL A CA  1 
ATOM   3143 C C   . VAL A 1 416 ? 90.555  118.636 105.590 1.00 42.27  ? 416 VAL A C   1 
ATOM   3144 O O   . VAL A 1 416 ? 90.773  119.533 106.410 1.00 42.72  ? 416 VAL A O   1 
ATOM   3145 C CB  . VAL A 1 416 ? 88.387  117.955 104.516 1.00 41.55  ? 416 VAL A CB  1 
ATOM   3146 C CG1 . VAL A 1 416 ? 87.800  118.024 105.903 1.00 41.20  ? 416 VAL A CG1 1 
ATOM   3147 C CG2 . VAL A 1 416 ? 87.348  118.348 103.485 1.00 41.90  ? 416 VAL A CG2 1 
ATOM   3148 N N   . ILE A 1 417 ? 91.109  117.423 105.685 1.00 42.36  ? 417 ILE A N   1 
ATOM   3149 C CA  . ILE A 1 417 ? 91.795  117.004 106.905 1.00 41.86  ? 417 ILE A CA  1 
ATOM   3150 C C   . ILE A 1 417 ? 93.106  117.761 107.089 1.00 41.53  ? 417 ILE A C   1 
ATOM   3151 O O   . ILE A 1 417 ? 93.467  118.130 108.213 1.00 41.20  ? 417 ILE A O   1 
ATOM   3152 C CB  . ILE A 1 417 ? 92.019  115.481 106.884 1.00 41.98  ? 417 ILE A CB  1 
ATOM   3153 C CG1 . ILE A 1 417 ? 90.689  114.752 106.713 1.00 42.40  ? 417 ILE A CG1 1 
ATOM   3154 C CG2 . ILE A 1 417 ? 92.688  115.015 108.162 1.00 42.04  ? 417 ILE A CG2 1 
ATOM   3155 C CD1 . ILE A 1 417 ? 89.697  115.041 107.810 1.00 42.75  ? 417 ILE A CD1 1 
ATOM   3156 N N   . PHE A 1 418 ? 93.840  117.997 106.000 1.00 41.27  ? 418 PHE A N   1 
ATOM   3157 C CA  . PHE A 1 418 ? 95.162  118.609 106.123 1.00 40.88  ? 418 PHE A CA  1 
ATOM   3158 C C   . PHE A 1 418 ? 95.143  120.025 106.701 1.00 40.61  ? 418 PHE A C   1 
ATOM   3159 O O   . PHE A 1 418 ? 96.008  120.314 107.546 1.00 42.78  ? 418 PHE A O   1 
ATOM   3160 C CB  . PHE A 1 418 ? 95.893  118.562 104.772 1.00 40.81  ? 418 PHE A CB  1 
ATOM   3161 C CG  . PHE A 1 418 ? 97.230  119.244 104.785 1.00 40.83  ? 418 PHE A CG  1 
ATOM   3162 C CD1 . PHE A 1 418 ? 98.350  118.581 105.250 1.00 41.17  ? 418 PHE A CD1 1 
ATOM   3163 C CD2 . PHE A 1 418 ? 97.372  120.539 104.316 1.00 40.90  ? 418 PHE A CD2 1 
ATOM   3164 C CE1 . PHE A 1 418 ? 99.582  119.201 105.264 1.00 41.24  ? 418 PHE A CE1 1 
ATOM   3165 C CE2 . PHE A 1 418 ? 98.602  121.164 104.328 1.00 40.89  ? 418 PHE A CE2 1 
ATOM   3166 C CZ  . PHE A 1 418 ? 99.708  120.493 104.801 1.00 41.03  ? 418 PHE A CZ  1 
ATOM   3167 N N   . PRO A 1 419 ? 94.252  120.949 106.298 1.00 39.10  ? 419 PRO A N   1 
ATOM   3168 C CA  . PRO A 1 419 ? 94.159  122.206 107.063 1.00 38.81  ? 419 PRO A CA  1 
ATOM   3169 C C   . PRO A 1 419 ? 93.787  121.993 108.519 1.00 39.27  ? 419 PRO A C   1 
ATOM   3170 O O   . PRO A 1 419 ? 94.297  122.705 109.393 1.00 39.91  ? 419 PRO A O   1 
ATOM   3171 C CB  . PRO A 1 419 ? 93.083  123.003 106.317 1.00 38.55  ? 419 PRO A CB  1 
ATOM   3172 C CG  . PRO A 1 419 ? 93.050  122.454 104.971 1.00 38.45  ? 419 PRO A CG  1 
ATOM   3173 C CD  . PRO A 1 419 ? 93.489  121.029 105.039 1.00 38.71  ? 419 PRO A CD  1 
ATOM   3174 N N   . GLN A 1 420 ? 92.915  121.023 108.807 1.00 39.41  ? 420 GLN A N   1 
ATOM   3175 C CA  . GLN A 1 420 ? 92.591  120.711 110.195 1.00 39.92  ? 420 GLN A CA  1 
ATOM   3176 C C   . GLN A 1 420 ? 93.806  120.163 110.932 1.00 40.35  ? 420 GLN A C   1 
ATOM   3177 O O   . GLN A 1 420 ? 94.019  120.479 112.107 1.00 39.74  ? 420 GLN A O   1 
ATOM   3178 C CB  . GLN A 1 420 ? 91.436  119.714 110.260 1.00 40.32  ? 420 GLN A CB  1 
ATOM   3179 C CG  . GLN A 1 420 ? 90.185  120.160 109.534 1.00 40.81  ? 420 GLN A CG  1 
ATOM   3180 C CD  . GLN A 1 420 ? 89.746  121.542 109.947 1.00 41.25  ? 420 GLN A CD  1 
ATOM   3181 O OE1 . GLN A 1 420 ? 89.419  121.778 111.106 1.00 42.00  ? 420 GLN A OE1 1 
ATOM   3182 N NE2 . GLN A 1 420 ? 89.733  122.468 108.997 1.00 41.14  ? 420 GLN A NE2 1 
ATOM   3183 N N   . LEU A 1 421 ? 94.606  119.331 110.258 1.00 41.53  ? 421 LEU A N   1 
ATOM   3184 C CA  . LEU A 1 421 ? 95.825  118.807 110.867 1.00 41.84  ? 421 LEU A CA  1 
ATOM   3185 C C   . LEU A 1 421 ? 96.823  119.918 111.156 1.00 42.11  ? 421 LEU A C   1 
ATOM   3186 O O   . LEU A 1 421 ? 97.474  119.917 112.206 1.00 42.32  ? 421 LEU A O   1 
ATOM   3187 C CB  . LEU A 1 421 ? 96.462  117.762 109.956 1.00 42.16  ? 421 LEU A CB  1 
ATOM   3188 C CG  . LEU A 1 421 ? 97.664  117.023 110.545 1.00 42.39  ? 421 LEU A CG  1 
ATOM   3189 C CD1 . LEU A 1 421 ? 97.366  116.518 111.947 1.00 42.66  ? 421 LEU A CD1 1 
ATOM   3190 C CD2 . LEU A 1 421 ? 98.095  115.896 109.638 1.00 42.81  ? 421 LEU A CD2 1 
ATOM   3191 N N   . LEU A 1 422 ? 96.968  120.864 110.233 1.00 42.28  ? 422 LEU A N   1 
ATOM   3192 C CA  . LEU A 1 422 ? 97.945  121.925 110.425 1.00 41.89  ? 422 LEU A CA  1 
ATOM   3193 C C   . LEU A 1 422 ? 97.456  122.957 111.434 1.00 42.31  ? 422 LEU A C   1 
ATOM   3194 O O   . LEU A 1 422 ? 98.274  123.629 112.071 1.00 42.66  ? 422 LEU A O   1 
ATOM   3195 C CB  . LEU A 1 422 ? 98.270  122.569 109.074 1.00 41.20  ? 422 LEU A CB  1 
ATOM   3196 C CG  . LEU A 1 422 ? 99.470  123.503 108.904 1.00 41.10  ? 422 LEU A CG  1 
ATOM   3197 C CD1 . LEU A 1 422 ? 99.973  123.392 107.478 1.00 41.08  ? 422 LEU A CD1 1 
ATOM   3198 C CD2 . LEU A 1 422 ? 99.136  124.946 109.215 1.00 41.58  ? 422 LEU A CD2 1 
ATOM   3199 N N   . CYS A 1 423 ? 96.138  123.086 111.607 1.00 43.44  ? 423 CYS A N   1 
ATOM   3200 C CA  . CYS A 1 423 ? 95.607  124.067 112.548 1.00 45.52  ? 423 CYS A CA  1 
ATOM   3201 C C   . CYS A 1 423 ? 95.754  123.622 114.000 1.00 45.74  ? 423 CYS A C   1 
ATOM   3202 O O   . CYS A 1 423 ? 96.018  124.454 114.873 1.00 47.55  ? 423 CYS A O   1 
ATOM   3203 C CB  . CYS A 1 423 ? 94.137  124.357 112.241 1.00 47.31  ? 423 CYS A CB  1 
ATOM   3204 S SG  . CYS A 1 423 ? 93.859  125.500 110.874 1.00 51.45  ? 423 CYS A SG  1 
ATOM   3205 N N   . VAL A 1 424 ? 95.570  122.330 114.286 1.00 44.78  ? 424 VAL A N   1 
ATOM   3206 C CA  . VAL A 1 424 ? 95.556  121.882 115.678 1.00 43.74  ? 424 VAL A CA  1 
ATOM   3207 C C   . VAL A 1 424 ? 96.950  121.950 116.291 1.00 43.19  ? 424 VAL A C   1 
ATOM   3208 O O   . VAL A 1 424 ? 97.107  122.303 117.466 1.00 42.50  ? 424 VAL A O   1 
ATOM   3209 C CB  . VAL A 1 424 ? 94.949  120.470 115.796 1.00 44.12  ? 424 VAL A CB  1 
ATOM   3210 C CG1 . VAL A 1 424 ? 93.463  120.516 115.532 1.00 44.85  ? 424 VAL A CG1 1 
ATOM   3211 C CG2 . VAL A 1 424 ? 95.617  119.500 114.841 1.00 44.40  ? 424 VAL A CG2 1 
ATOM   3212 N N   . LEU A 1 425 ? 97.983  121.619 115.517 1.00 43.20  ? 425 LEU A N   1 
ATOM   3213 C CA  . LEU A 1 425 ? 99.339  121.547 116.051 1.00 42.86  ? 425 LEU A CA  1 
ATOM   3214 C C   . LEU A 1 425 ? 100.048 122.898 115.996 1.00 43.70  ? 425 LEU A C   1 
ATOM   3215 O O   . LEU A 1 425 ? 100.480 123.424 117.026 1.00 44.34  ? 425 LEU A O   1 
ATOM   3216 C CB  . LEU A 1 425 ? 100.147 120.493 115.286 1.00 42.18  ? 425 LEU A CB  1 
ATOM   3217 C CG  . LEU A 1 425 ? 99.471  119.146 115.044 1.00 42.00  ? 425 LEU A CG  1 
ATOM   3218 C CD1 . LEU A 1 425 ? 100.371 118.247 114.218 1.00 41.77  ? 425 LEU A CD1 1 
ATOM   3219 C CD2 . LEU A 1 425 ? 99.125  118.489 116.366 1.00 41.88  ? 425 LEU A CD2 1 
ATOM   3220 N N   . PHE A 1 426 ? 100.173 123.466 114.797 1.00 44.57  ? 426 PHE A N   1 
ATOM   3221 C CA  . PHE A 1 426 ? 101.022 124.639 114.618 1.00 45.55  ? 426 PHE A CA  1 
ATOM   3222 C C   . PHE A 1 426 ? 100.341 125.919 115.087 1.00 46.66  ? 426 PHE A C   1 
ATOM   3223 O O   . PHE A 1 426 ? 101.002 126.808 115.635 1.00 47.87  ? 426 PHE A O   1 
ATOM   3224 C CB  . PHE A 1 426 ? 101.440 124.757 113.152 1.00 45.78  ? 426 PHE A CB  1 
ATOM   3225 C CG  . PHE A 1 426 ? 102.334 123.641 112.680 1.00 46.85  ? 426 PHE A CG  1 
ATOM   3226 C CD1 . PHE A 1 426 ? 102.971 122.804 113.583 1.00 46.80  ? 426 PHE A CD1 1 
ATOM   3227 C CD2 . PHE A 1 426 ? 102.538 123.433 111.328 1.00 47.85  ? 426 PHE A CD2 1 
ATOM   3228 C CE1 . PHE A 1 426 ? 103.788 121.783 113.146 1.00 47.02  ? 426 PHE A CE1 1 
ATOM   3229 C CE2 . PHE A 1 426 ? 103.357 122.413 110.885 1.00 47.86  ? 426 PHE A CE2 1 
ATOM   3230 C CZ  . PHE A 1 426 ? 103.981 121.588 111.796 1.00 47.52  ? 426 PHE A CZ  1 
ATOM   3231 N N   . VAL A 1 427 ? 99.036  126.033 114.888 1.00 47.70  ? 427 VAL A N   1 
ATOM   3232 C CA  . VAL A 1 427 ? 98.300  127.247 115.223 1.00 48.76  ? 427 VAL A CA  1 
ATOM   3233 C C   . VAL A 1 427 ? 97.670  127.090 116.599 1.00 50.68  ? 427 VAL A C   1 
ATOM   3234 O O   . VAL A 1 427 ? 97.076  126.054 116.914 1.00 50.51  ? 427 VAL A O   1 
ATOM   3235 C CB  . VAL A 1 427 ? 97.237  127.552 114.152 1.00 48.19  ? 427 VAL A CB  1 
ATOM   3236 C CG1 . VAL A 1 427 ? 96.577  128.894 114.422 1.00 48.21  ? 427 VAL A CG1 1 
ATOM   3237 C CG2 . VAL A 1 427 ? 97.861  127.534 112.769 1.00 47.96  ? 427 VAL A CG2 1 
ATOM   3238 N N   . LYS A 1 428 ? 97.808  128.117 117.430 1.00 54.76  ? 428 LYS A N   1 
ATOM   3239 C CA  . LYS A 1 428 ? 97.204  128.131 118.753 1.00 58.69  ? 428 LYS A CA  1 
ATOM   3240 C C   . LYS A 1 428 ? 95.953  129.001 118.753 1.00 59.95  ? 428 LYS A C   1 
ATOM   3241 O O   . LYS A 1 428 ? 95.881  130.021 118.064 1.00 58.94  ? 428 LYS A O   1 
ATOM   3242 C CB  . LYS A 1 428 ? 98.193  128.641 119.803 1.00 60.72  ? 428 LYS A CB  1 
ATOM   3243 C CG  . LYS A 1 428 ? 99.409  127.751 119.992 1.00 62.41  ? 428 LYS A CG  1 
ATOM   3244 C CD  . LYS A 1 428 ? 100.273 128.234 121.144 1.00 64.33  ? 428 LYS A CD  1 
ATOM   3245 C CE  . LYS A 1 428 ? 101.485 127.337 121.341 1.00 66.46  ? 428 LYS A CE  1 
ATOM   3246 N NZ  . LYS A 1 428 ? 102.325 127.784 122.486 1.00 67.89  ? 428 LYS A NZ  1 
ATOM   3247 N N   . GLY A 1 429 ? 94.964  128.583 119.539 1.00 61.35  ? 429 GLY A N   1 
ATOM   3248 C CA  . GLY A 1 429 ? 93.722  129.322 119.637 1.00 62.26  ? 429 GLY A CA  1 
ATOM   3249 C C   . GLY A 1 429 ? 92.699  129.016 118.569 1.00 63.17  ? 429 GLY A C   1 
ATOM   3250 O O   . GLY A 1 429 ? 91.796  129.828 118.346 1.00 65.60  ? 429 GLY A O   1 
ATOM   3251 N N   . THR A 1 430 ? 92.807  127.871 117.899 1.00 62.55  ? 430 THR A N   1 
ATOM   3252 C CA  . THR A 1 430 ? 91.827  127.487 116.892 1.00 62.15  ? 430 THR A CA  1 
ATOM   3253 C C   . THR A 1 430 ? 90.628  126.826 117.562 1.00 63.67  ? 430 THR A C   1 
ATOM   3254 O O   . THR A 1 430 ? 90.781  125.859 118.314 1.00 66.52  ? 430 THR A O   1 
ATOM   3255 C CB  . THR A 1 430 ? 92.453  126.539 115.870 1.00 60.17  ? 430 THR A CB  1 
ATOM   3256 O OG1 . THR A 1 430 ? 93.525  127.207 115.194 1.00 59.92  ? 430 THR A OG1 1 
ATOM   3257 C CG2 . THR A 1 430 ? 91.420  126.107 114.848 1.00 59.36  ? 430 THR A CG2 1 
ATOM   3258 N N   . ASN A 1 431 ? 89.437  127.346 117.283 1.00 63.91  ? 431 ASN A N   1 
ATOM   3259 C CA  . ASN A 1 431 ? 88.216  126.904 117.935 1.00 64.26  ? 431 ASN A CA  1 
ATOM   3260 C C   . ASN A 1 431 ? 87.484  125.885 117.066 1.00 64.72  ? 431 ASN A C   1 
ATOM   3261 O O   . ASN A 1 431 ? 87.954  125.476 116.002 1.00 65.71  ? 431 ASN A O   1 
ATOM   3262 C CB  . ASN A 1 431 ? 87.319  128.103 118.245 1.00 65.28  ? 431 ASN A CB  1 
ATOM   3263 C CG  . ASN A 1 431 ? 88.080  129.254 118.866 1.00 67.35  ? 431 ASN A CG  1 
ATOM   3264 O OD1 . ASN A 1 431 ? 87.915  130.407 118.471 1.00 69.04  ? 431 ASN A OD1 1 
ATOM   3265 N ND2 . ASN A 1 431 ? 88.917  128.947 119.851 1.00 68.58  ? 431 ASN A ND2 1 
ATOM   3266 N N   . THR A 1 432 ? 86.310  125.465 117.541 1.00 64.94  ? 432 THR A N   1 
ATOM   3267 C CA  . THR A 1 432 ? 85.483  124.530 116.788 1.00 64.45  ? 432 THR A CA  1 
ATOM   3268 C C   . THR A 1 432 ? 84.764  125.213 115.629 1.00 62.32  ? 432 THR A C   1 
ATOM   3269 O O   . THR A 1 432 ? 84.576  124.596 114.574 1.00 59.26  ? 432 THR A O   1 
ATOM   3270 C CB  . THR A 1 432 ? 84.471  123.864 117.726 1.00 66.22  ? 432 THR A CB  1 
ATOM   3271 O OG1 . THR A 1 432 ? 85.162  123.284 118.838 1.00 67.00  ? 432 THR A OG1 1 
ATOM   3272 C CG2 . THR A 1 432 ? 83.700  122.764 117.008 1.00 67.15  ? 432 THR A CG2 1 
ATOM   3273 N N   . TYR A 1 433 ? 84.366  126.477 115.807 1.00 61.80  ? 433 TYR A N   1 
ATOM   3274 C CA  . TYR A 1 433 ? 83.619  127.186 114.770 1.00 60.89  ? 433 TYR A CA  1 
ATOM   3275 C C   . TYR A 1 433 ? 84.452  127.362 113.507 1.00 59.54  ? 433 TYR A C   1 
ATOM   3276 O O   . TYR A 1 433 ? 83.950  127.175 112.392 1.00 60.18  ? 433 TYR A O   1 
ATOM   3277 C CB  . TYR A 1 433 ? 83.158  128.549 115.287 1.00 61.08  ? 433 TYR A CB  1 
ATOM   3278 C CG  . TYR A 1 433 ? 82.641  128.536 116.706 1.00 61.95  ? 433 TYR A CG  1 
ATOM   3279 C CD1 . TYR A 1 433 ? 81.305  128.277 116.976 1.00 62.08  ? 433 TYR A CD1 1 
ATOM   3280 C CD2 . TYR A 1 433 ? 83.486  128.804 117.774 1.00 63.40  ? 433 TYR A CD2 1 
ATOM   3281 C CE1 . TYR A 1 433 ? 80.830  128.270 118.272 1.00 63.18  ? 433 TYR A CE1 1 
ATOM   3282 C CE2 . TYR A 1 433 ? 83.021  128.797 119.069 1.00 64.23  ? 433 TYR A CE2 1 
ATOM   3283 C CZ  . TYR A 1 433 ? 81.694  128.531 119.313 1.00 64.04  ? 433 TYR A CZ  1 
ATOM   3284 O OH  . TYR A 1 433 ? 81.233  128.526 120.607 1.00 64.22  ? 433 TYR A OH  1 
ATOM   3285 N N   . GLY A 1 434 ? 85.725  127.727 113.663 1.00 57.94  ? 434 GLY A N   1 
ATOM   3286 C CA  . GLY A 1 434 ? 86.597  127.841 112.507 1.00 56.87  ? 434 GLY A CA  1 
ATOM   3287 C C   . GLY A 1 434 ? 86.831  126.507 111.828 1.00 55.56  ? 434 GLY A C   1 
ATOM   3288 O O   . GLY A 1 434 ? 86.930  126.436 110.601 1.00 56.39  ? 434 GLY A O   1 
ATOM   3289 N N   . ALA A 1 435 ? 86.913  125.433 112.615 1.00 54.30  ? 435 ALA A N   1 
ATOM   3290 C CA  . ALA A 1 435 ? 87.049  124.099 112.042 1.00 54.27  ? 435 ALA A CA  1 
ATOM   3291 C C   . ALA A 1 435 ? 85.824  123.722 111.217 1.00 54.12  ? 435 ALA A C   1 
ATOM   3292 O O   . ALA A 1 435 ? 85.952  123.176 110.115 1.00 53.55  ? 435 ALA A O   1 
ATOM   3293 C CB  . ALA A 1 435 ? 87.284  123.080 113.155 1.00 54.50  ? 435 ALA A CB  1 
ATOM   3294 N N   . VAL A 1 436 ? 84.628  124.014 111.735 1.00 53.05  ? 436 VAL A N   1 
ATOM   3295 C CA  . VAL A 1 436 ? 83.396  123.713 111.009 1.00 50.83  ? 436 VAL A CA  1 
ATOM   3296 C C   . VAL A 1 436 ? 83.306  124.550 109.737 1.00 50.24  ? 436 VAL A C   1 
ATOM   3297 O O   . VAL A 1 436 ? 82.906  124.052 108.677 1.00 49.65  ? 436 VAL A O   1 
ATOM   3298 C CB  . VAL A 1 436 ? 82.177  123.928 111.925 1.00 49.41  ? 436 VAL A CB  1 
ATOM   3299 C CG1 . VAL A 1 436 ? 80.881  123.892 111.131 1.00 48.95  ? 436 VAL A CG1 1 
ATOM   3300 C CG2 . VAL A 1 436 ? 82.153  122.882 113.025 1.00 49.16  ? 436 VAL A CG2 1 
ATOM   3301 N N   . ALA A 1 437 ? 83.682  125.830 109.821 1.00 50.14  ? 437 ALA A N   1 
ATOM   3302 C CA  . ALA A 1 437 ? 83.670  126.689 108.642 1.00 49.99  ? 437 ALA A CA  1 
ATOM   3303 C C   . ALA A 1 437 ? 84.652  126.198 107.586 1.00 49.28  ? 437 ALA A C   1 
ATOM   3304 O O   . ALA A 1 437 ? 84.340  126.203 106.390 1.00 47.92  ? 437 ALA A O   1 
ATOM   3305 C CB  . ALA A 1 437 ? 83.986  128.129 109.039 1.00 50.17  ? 437 ALA A CB  1 
ATOM   3306 N N   . GLY A 1 438 ? 85.841  125.766 108.009 1.00 49.88  ? 438 GLY A N   1 
ATOM   3307 C CA  . GLY A 1 438 ? 86.797  125.212 107.065 1.00 51.15  ? 438 GLY A CA  1 
ATOM   3308 C C   . GLY A 1 438 ? 86.306  123.928 106.426 1.00 52.54  ? 438 GLY A C   1 
ATOM   3309 O O   . GLY A 1 438 ? 86.489  123.716 105.225 1.00 54.46  ? 438 GLY A O   1 
ATOM   3310 N N   . TYR A 1 439 ? 85.669  123.061 107.219 1.00 52.79  ? 439 TYR A N   1 
ATOM   3311 C CA  . TYR A 1 439 ? 85.077  121.838 106.684 1.00 52.66  ? 439 TYR A CA  1 
ATOM   3312 C C   . TYR A 1 439 ? 84.031  122.154 105.621 1.00 52.28  ? 439 TYR A C   1 
ATOM   3313 O O   . TYR A 1 439 ? 84.053  121.585 104.522 1.00 52.45  ? 439 TYR A O   1 
ATOM   3314 C CB  . TYR A 1 439 ? 84.456  121.025 107.824 1.00 52.40  ? 439 TYR A CB  1 
ATOM   3315 C CG  . TYR A 1 439 ? 84.032  119.618 107.454 1.00 52.38  ? 439 TYR A CG  1 
ATOM   3316 C CD1 . TYR A 1 439 ? 82.797  119.370 106.868 1.00 52.85  ? 439 TYR A CD1 1 
ATOM   3317 C CD2 . TYR A 1 439 ? 84.857  118.537 107.715 1.00 51.93  ? 439 TYR A CD2 1 
ATOM   3318 C CE1 . TYR A 1 439 ? 82.408  118.088 106.534 1.00 53.25  ? 439 TYR A CE1 1 
ATOM   3319 C CE2 . TYR A 1 439 ? 84.479  117.252 107.384 1.00 51.80  ? 439 TYR A CE2 1 
ATOM   3320 C CZ  . TYR A 1 439 ? 83.253  117.033 106.796 1.00 53.02  ? 439 TYR A CZ  1 
ATOM   3321 O OH  . TYR A 1 439 ? 82.870  115.754 106.468 1.00 55.13  ? 439 TYR A OH  1 
ATOM   3322 N N   . VAL A 1 440 ? 83.114  123.074 105.934 1.00 51.27  ? 440 VAL A N   1 
ATOM   3323 C CA  . VAL A 1 440 ? 82.034  123.410 105.010 1.00 50.38  ? 440 VAL A CA  1 
ATOM   3324 C C   . VAL A 1 440 ? 82.589  124.045 103.741 1.00 50.61  ? 440 VAL A C   1 
ATOM   3325 O O   . VAL A 1 440 ? 82.179  123.693 102.629 1.00 50.42  ? 440 VAL A O   1 
ATOM   3326 C CB  . VAL A 1 440 ? 81.003  124.322 105.702 1.00 49.45  ? 440 VAL A CB  1 
ATOM   3327 C CG1 . VAL A 1 440 ? 80.014  124.878 104.694 1.00 49.18  ? 440 VAL A CG1 1 
ATOM   3328 C CG2 . VAL A 1 440 ? 80.267  123.552 106.784 1.00 49.25  ? 440 VAL A CG2 1 
ATOM   3329 N N   . SER A 1 441 ? 83.541  124.973 103.882 1.00 50.63  ? 441 SER A N   1 
ATOM   3330 C CA  . SER A 1 441 ? 84.108  125.638 102.711 1.00 50.23  ? 441 SER A CA  1 
ATOM   3331 C C   . SER A 1 441 ? 84.875  124.662 101.826 1.00 48.61  ? 441 SER A C   1 
ATOM   3332 O O   . SER A 1 441 ? 84.716  124.679 100.598 1.00 47.80  ? 441 SER A O   1 
ATOM   3333 C CB  . SER A 1 441 ? 85.013  126.788 103.149 1.00 51.19  ? 441 SER A CB  1 
ATOM   3334 O OG  . SER A 1 441 ? 85.571  127.449 102.028 1.00 52.48  ? 441 SER A OG  1 
ATOM   3335 N N   . GLY A 1 442 ? 85.703  123.800 102.423 1.00 48.09  ? 442 GLY A N   1 
ATOM   3336 C CA  . GLY A 1 442 ? 86.439  122.832 101.629 1.00 49.26  ? 442 GLY A CA  1 
ATOM   3337 C C   . GLY A 1 442 ? 85.530  121.847 100.920 1.00 51.36  ? 442 GLY A C   1 
ATOM   3338 O O   . GLY A 1 442 ? 85.720  121.558 99.734  1.00 53.05  ? 442 GLY A O   1 
ATOM   3339 N N   . LEU A 1 443 ? 84.514  121.340 101.627 1.00 53.09  ? 443 LEU A N   1 
ATOM   3340 C CA  . LEU A 1 443 ? 83.567  120.420 101.009 1.00 53.44  ? 443 LEU A CA  1 
ATOM   3341 C C   . LEU A 1 443 ? 82.792  121.093 99.882  1.00 54.03  ? 443 LEU A C   1 
ATOM   3342 O O   . LEU A 1 443 ? 82.586  120.494 98.820  1.00 54.47  ? 443 LEU A O   1 
ATOM   3343 C CB  . LEU A 1 443 ? 82.611  119.871 102.067 1.00 53.30  ? 443 LEU A CB  1 
ATOM   3344 C CG  . LEU A 1 443 ? 81.680  118.744 101.625 1.00 53.43  ? 443 LEU A CG  1 
ATOM   3345 C CD1 . LEU A 1 443 ? 82.483  117.508 101.274 1.00 53.43  ? 443 LEU A CD1 1 
ATOM   3346 C CD2 . LEU A 1 443 ? 80.660  118.438 102.709 1.00 53.68  ? 443 LEU A CD2 1 
ATOM   3347 N N   . PHE A 1 444 ? 82.371  122.346 100.087 1.00 54.07  ? 444 PHE A N   1 
ATOM   3348 C CA  . PHE A 1 444 ? 81.601  123.050 99.068  1.00 54.24  ? 444 PHE A CA  1 
ATOM   3349 C C   . PHE A 1 444 ? 82.435  123.318 97.822  1.00 54.04  ? 444 PHE A C   1 
ATOM   3350 O O   . PHE A 1 444 ? 81.959  123.112 96.700  1.00 54.53  ? 444 PHE A O   1 
ATOM   3351 C CB  . PHE A 1 444 ? 81.047  124.354 99.644  1.00 54.55  ? 444 PHE A CB  1 
ATOM   3352 C CG  . PHE A 1 444 ? 80.346  125.221 98.634  1.00 55.12  ? 444 PHE A CG  1 
ATOM   3353 C CD1 . PHE A 1 444 ? 79.024  124.982 98.300  1.00 55.38  ? 444 PHE A CD1 1 
ATOM   3354 C CD2 . PHE A 1 444 ? 80.997  126.293 98.043  1.00 54.98  ? 444 PHE A CD2 1 
ATOM   3355 C CE1 . PHE A 1 444 ? 78.372  125.778 97.378  1.00 55.11  ? 444 PHE A CE1 1 
ATOM   3356 C CE2 . PHE A 1 444 ? 80.350  127.092 97.121  1.00 54.71  ? 444 PHE A CE2 1 
ATOM   3357 C CZ  . PHE A 1 444 ? 79.036  126.835 96.789  1.00 54.91  ? 444 PHE A CZ  1 
ATOM   3358 N N   . LEU A 1 445 ? 83.680  123.776 97.993  1.00 53.47  ? 445 LEU A N   1 
ATOM   3359 C CA  . LEU A 1 445 ? 84.525  124.023 96.827  1.00 52.76  ? 445 LEU A CA  1 
ATOM   3360 C C   . LEU A 1 445 ? 84.896  122.729 96.112  1.00 52.45  ? 445 LEU A C   1 
ATOM   3361 O O   . LEU A 1 445 ? 84.978  122.706 94.878  1.00 53.35  ? 445 LEU A O   1 
ATOM   3362 C CB  . LEU A 1 445 ? 85.778  124.809 97.218  1.00 52.46  ? 445 LEU A CB  1 
ATOM   3363 C CG  . LEU A 1 445 ? 85.674  126.341 97.201  1.00 52.36  ? 445 LEU A CG  1 
ATOM   3364 C CD1 . LEU A 1 445 ? 84.816  126.907 98.318  1.00 52.36  ? 445 LEU A CD1 1 
ATOM   3365 C CD2 . LEU A 1 445 ? 87.063  126.959 97.235  1.00 52.65  ? 445 LEU A CD2 1 
ATOM   3366 N N   . ARG A 1 446 ? 85.106  121.636 96.853  1.00 52.86  ? 446 ARG A N   1 
ATOM   3367 C CA  . ARG A 1 446 ? 85.426  120.378 96.184  1.00 54.32  ? 446 ARG A CA  1 
ATOM   3368 C C   . ARG A 1 446 ? 84.218  119.822 95.434  1.00 56.61  ? 446 ARG A C   1 
ATOM   3369 O O   . ARG A 1 446 ? 84.370  119.245 94.351  1.00 56.99  ? 446 ARG A O   1 
ATOM   3370 C CB  . ARG A 1 446 ? 85.950  119.353 97.189  1.00 53.80  ? 446 ARG A CB  1 
ATOM   3371 C CG  . ARG A 1 446 ? 86.513  118.094 96.538  1.00 52.88  ? 446 ARG A CG  1 
ATOM   3372 C CD  . ARG A 1 446 ? 87.380  118.443 95.334  1.00 52.89  ? 446 ARG A CD  1 
ATOM   3373 N NE  . ARG A 1 446 ? 87.834  117.267 94.602  1.00 53.58  ? 446 ARG A NE  1 
ATOM   3374 C CZ  . ARG A 1 446 ? 87.350  116.887 93.428  1.00 54.23  ? 446 ARG A CZ  1 
ATOM   3375 N NH1 . ARG A 1 446 ? 86.388  117.566 92.825  1.00 54.41  ? 446 ARG A NH1 1 
ATOM   3376 N NH2 . ARG A 1 446 ? 87.848  115.803 92.841  1.00 54.34  ? 446 ARG A NH2 1 
ATOM   3377 N N   . ILE A 1 447 ? 83.014  119.979 95.990  1.00 59.13  ? 447 ILE A N   1 
ATOM   3378 C CA  . ILE A 1 447 ? 81.818  119.503 95.301  1.00 60.23  ? 447 ILE A CA  1 
ATOM   3379 C C   . ILE A 1 447 ? 81.534  120.351 94.066  1.00 61.91  ? 447 ILE A C   1 
ATOM   3380 O O   . ILE A 1 447 ? 81.247  119.819 92.986  1.00 62.37  ? 447 ILE A O   1 
ATOM   3381 C CB  . ILE A 1 447 ? 80.619  119.475 96.268  1.00 60.23  ? 447 ILE A CB  1 
ATOM   3382 C CG1 . ILE A 1 447 ? 80.762  118.314 97.253  1.00 60.47  ? 447 ILE A CG1 1 
ATOM   3383 C CG2 . ILE A 1 447 ? 79.306  119.367 95.510  1.00 60.03  ? 447 ILE A CG2 1 
ATOM   3384 C CD1 . ILE A 1 447 ? 79.766  118.355 98.389  1.00 60.59  ? 447 ILE A CD1 1 
ATOM   3385 N N   . THR A 1 448 ? 81.628  121.677 94.191  1.00 64.52  ? 448 THR A N   1 
ATOM   3386 C CA  . THR A 1 448 ? 81.379  122.546 93.047  1.00 67.28  ? 448 THR A CA  1 
ATOM   3387 C C   . THR A 1 448 ? 82.483  122.465 92.001  1.00 70.12  ? 448 THR A C   1 
ATOM   3388 O O   . THR A 1 448 ? 82.255  122.851 90.851  1.00 69.28  ? 448 THR A O   1 
ATOM   3389 C CB  . THR A 1 448 ? 81.209  123.994 93.505  1.00 67.74  ? 448 THR A CB  1 
ATOM   3390 O OG1 . THR A 1 448 ? 82.275  124.344 94.395  1.00 69.69  ? 448 THR A OG1 1 
ATOM   3391 C CG2 . THR A 1 448 ? 79.881  124.172 94.221  1.00 67.69  ? 448 THR A CG2 1 
ATOM   3392 N N   . GLY A 1 449 ? 83.673  121.988 92.373  1.00 74.82  ? 449 GLY A N   1 
ATOM   3393 C CA  . GLY A 1 449 ? 84.712  121.777 91.379  1.00 77.62  ? 449 GLY A CA  1 
ATOM   3394 C C   . GLY A 1 449 ? 84.362  120.678 90.393  1.00 80.98  ? 449 GLY A C   1 
ATOM   3395 O O   . GLY A 1 449 ? 84.664  120.781 89.202  1.00 82.95  ? 449 GLY A O   1 
ATOM   3396 N N   . GLY A 1 450 ? 83.730  119.615 90.873  1.00 84.09  ? 450 GLY A N   1 
ATOM   3397 C CA  . GLY A 1 450 ? 83.308  118.526 90.021  1.00 85.80  ? 450 GLY A CA  1 
ATOM   3398 C C   . GLY A 1 450 ? 84.418  117.523 89.756  1.00 88.26  ? 450 GLY A C   1 
ATOM   3399 O O   . GLY A 1 450 ? 85.598  117.767 90.000  1.00 87.13  ? 450 GLY A O   1 
ATOM   3400 N N   . GLU A 1 451 ? 84.014  116.363 89.240  1.00 92.73  ? 451 GLU A N   1 
ATOM   3401 C CA  . GLU A 1 451 ? 84.942  115.295 88.901  1.00 97.27  ? 451 GLU A CA  1 
ATOM   3402 C C   . GLU A 1 451 ? 84.569  114.725 87.538  1.00 101.05 ? 451 GLU A C   1 
ATOM   3403 O O   . GLU A 1 451 ? 83.403  114.348 87.322  1.00 104.13 ? 451 GLU A O   1 
ATOM   3404 C CB  . GLU A 1 451 ? 84.928  114.190 89.967  1.00 97.93  ? 451 GLU A CB  1 
ATOM   3405 C CG  . GLU A 1 451 ? 85.920  113.064 89.713  1.00 100.05 ? 451 GLU A CG  1 
ATOM   3406 C CD  . GLU A 1 451 ? 87.362  113.478 89.942  1.00 101.55 ? 451 GLU A CD  1 
ATOM   3407 O OE1 . GLU A 1 451 ? 87.594  114.501 90.620  1.00 100.58 ? 451 GLU A OE1 1 
ATOM   3408 O OE2 . GLU A 1 451 ? 88.267  112.778 89.441  1.00 104.28 ? 451 GLU A OE2 1 
ATOM   3409 N N   . PRO A 1 452 ? 85.509  114.668 86.590  1.00 103.23 ? 452 PRO A N   1 
ATOM   3410 C CA  . PRO A 1 452 ? 85.202  114.056 85.286  1.00 105.09 ? 452 PRO A CA  1 
ATOM   3411 C C   . PRO A 1 452 ? 84.842  112.582 85.369  1.00 108.44 ? 452 PRO A C   1 
ATOM   3412 O O   . PRO A 1 452 ? 84.036  112.106 84.560  1.00 108.04 ? 452 PRO A O   1 
ATOM   3413 C CB  . PRO A 1 452 ? 86.495  114.273 84.487  1.00 103.41 ? 452 PRO A CB  1 
ATOM   3414 C CG  . PRO A 1 452 ? 87.180  115.415 85.166  1.00 102.25 ? 452 PRO A CG  1 
ATOM   3415 C CD  . PRO A 1 452 ? 86.853  115.266 86.619  1.00 102.39 ? 452 PRO A CD  1 
ATOM   3416 N N   . TYR A 1 453 ? 85.424  111.842 86.317  1.00 113.24 ? 453 TYR A N   1 
ATOM   3417 C CA  . TYR A 1 453 ? 85.158  110.409 86.410  1.00 116.29 ? 453 TYR A CA  1 
ATOM   3418 C C   . TYR A 1 453 ? 83.730  110.132 86.864  1.00 118.50 ? 453 TYR A C   1 
ATOM   3419 O O   . TYR A 1 453 ? 83.093  109.187 86.383  1.00 122.40 ? 453 TYR A O   1 
ATOM   3420 C CB  . TYR A 1 453 ? 86.158  109.752 87.360  1.00 116.70 ? 453 TYR A CB  1 
ATOM   3421 C CG  . TYR A 1 453 ? 87.468  109.372 86.709  1.00 118.69 ? 453 TYR A CG  1 
ATOM   3422 C CD1 . TYR A 1 453 ? 87.627  108.138 86.094  1.00 119.00 ? 453 TYR A CD1 1 
ATOM   3423 C CD2 . TYR A 1 453 ? 88.547  110.248 86.712  1.00 120.43 ? 453 TYR A CD2 1 
ATOM   3424 C CE1 . TYR A 1 453 ? 88.824  107.786 85.498  1.00 120.71 ? 453 TYR A CE1 1 
ATOM   3425 C CE2 . TYR A 1 453 ? 89.747  109.905 86.119  1.00 121.85 ? 453 TYR A CE2 1 
ATOM   3426 C CZ  . TYR A 1 453 ? 89.880  108.673 85.514  1.00 122.56 ? 453 TYR A CZ  1 
ATOM   3427 O OH  . TYR A 1 453 ? 91.073  108.327 84.922  1.00 124.15 ? 453 TYR A OH  1 
ATOM   3428 N N   . LEU A 1 454 ? 83.212  110.937 87.788  1.00 118.56 ? 454 LEU A N   1 
ATOM   3429 C CA  . LEU A 1 454 ? 81.863  110.758 88.307  1.00 117.57 ? 454 LEU A CA  1 
ATOM   3430 C C   . LEU A 1 454 ? 80.800  111.432 87.450  1.00 118.79 ? 454 LEU A C   1 
ATOM   3431 O O   . LEU A 1 454 ? 79.614  111.349 87.791  1.00 119.90 ? 454 LEU A O   1 
ATOM   3432 C CB  . LEU A 1 454 ? 81.773  111.286 89.742  1.00 115.59 ? 454 LEU A CB  1 
ATOM   3433 C CG  . LEU A 1 454 ? 82.483  110.475 90.828  1.00 113.80 ? 454 LEU A CG  1 
ATOM   3434 C CD1 . LEU A 1 454 ? 81.971  110.873 92.201  1.00 113.75 ? 454 LEU A CD1 1 
ATOM   3435 C CD2 . LEU A 1 454 ? 82.301  108.983 90.601  1.00 111.91 ? 454 LEU A CD2 1 
ATOM   3436 N N   . TYR A 1 455 ? 81.201  112.094 86.358  1.00 119.52 ? 455 TYR A N   1 
ATOM   3437 C CA  . TYR A 1 455 ? 80.289  112.790 85.444  1.00 120.63 ? 455 TYR A CA  1 
ATOM   3438 C C   . TYR A 1 455 ? 79.455  113.841 86.176  1.00 122.03 ? 455 TYR A C   1 
ATOM   3439 O O   . TYR A 1 455 ? 78.268  114.023 85.898  1.00 122.28 ? 455 TYR A O   1 
ATOM   3440 C CB  . TYR A 1 455 ? 79.386  111.806 84.693  1.00 120.47 ? 455 TYR A CB  1 
ATOM   3441 C CG  . TYR A 1 455 ? 80.133  110.742 83.919  1.00 120.43 ? 455 TYR A CG  1 
ATOM   3442 C CD1 . TYR A 1 455 ? 80.478  109.535 84.515  1.00 119.06 ? 455 TYR A CD1 1 
ATOM   3443 C CD2 . TYR A 1 455 ? 80.491  110.944 82.593  1.00 121.50 ? 455 TYR A CD2 1 
ATOM   3444 C CE1 . TYR A 1 455 ? 81.160  108.560 83.811  1.00 118.42 ? 455 TYR A CE1 1 
ATOM   3445 C CE2 . TYR A 1 455 ? 81.172  109.975 81.881  1.00 121.60 ? 455 TYR A CE2 1 
ATOM   3446 C CZ  . TYR A 1 455 ? 81.504  108.785 82.495  1.00 120.09 ? 455 TYR A CZ  1 
ATOM   3447 O OH  . TYR A 1 455 ? 82.183  107.818 81.789  1.00 120.18 ? 455 TYR A OH  1 
ATOM   3448 N N   . LEU A 1 456 ? 80.083  114.539 87.118  1.00 122.83 ? 456 LEU A N   1 
ATOM   3449 C CA  . LEU A 1 456 ? 79.423  115.574 87.902  1.00 122.18 ? 456 LEU A CA  1 
ATOM   3450 C C   . LEU A 1 456 ? 79.700  116.928 87.262  1.00 125.03 ? 456 LEU A C   1 
ATOM   3451 O O   . LEU A 1 456 ? 80.862  117.299 87.062  1.00 128.63 ? 456 LEU A O   1 
ATOM   3452 C CB  . LEU A 1 456 ? 79.907  115.548 89.353  1.00 118.13 ? 456 LEU A CB  1 
ATOM   3453 C CG  . LEU A 1 456 ? 79.610  116.760 90.240  1.00 115.02 ? 456 LEU A CG  1 
ATOM   3454 C CD1 . LEU A 1 456 ? 78.112  117.006 90.362  1.00 113.89 ? 456 LEU A CD1 1 
ATOM   3455 C CD2 . LEU A 1 456 ? 80.238  116.579 91.612  1.00 113.66 ? 456 LEU A CD2 1 
ATOM   3456 N N   . GLN A 1 457 ? 78.639  117.655 86.940  1.00 124.30 ? 457 GLN A N   1 
ATOM   3457 C CA  . GLN A 1 457 ? 78.792  118.968 86.328  1.00 122.71 ? 457 GLN A CA  1 
ATOM   3458 C C   . GLN A 1 457 ? 79.279  119.973 87.366  1.00 121.50 ? 457 GLN A C   1 
ATOM   3459 O O   . GLN A 1 457 ? 78.711  120.049 88.462  1.00 122.60 ? 457 GLN A O   1 
ATOM   3460 C CB  . GLN A 1 457 ? 77.469  119.432 85.724  1.00 122.20 ? 457 GLN A CB  1 
ATOM   3461 C CG  . GLN A 1 457 ? 77.581  120.681 84.867  1.00 122.05 ? 457 GLN A CG  1 
ATOM   3462 C CD  . GLN A 1 457 ? 76.229  121.229 84.458  1.00 122.71 ? 457 GLN A CD  1 
ATOM   3463 O OE1 . GLN A 1 457 ? 75.204  120.892 85.051  1.00 122.90 ? 457 GLN A OE1 1 
ATOM   3464 N NE2 . GLN A 1 457 ? 76.219  122.080 83.438  1.00 123.45 ? 457 GLN A NE2 1 
ATOM   3465 N N   . PRO A 1 458 ? 80.322  120.749 87.071  1.00 117.44 ? 458 PRO A N   1 
ATOM   3466 C CA  . PRO A 1 458 ? 80.786  121.754 88.037  1.00 115.07 ? 458 PRO A CA  1 
ATOM   3467 C C   . PRO A 1 458 ? 79.841  122.947 88.087  1.00 113.95 ? 458 PRO A C   1 
ATOM   3468 O O   . PRO A 1 458 ? 79.484  123.521 87.056  1.00 113.30 ? 458 PRO A O   1 
ATOM   3469 C CB  . PRO A 1 458 ? 82.168  122.147 87.503  1.00 114.42 ? 458 PRO A CB  1 
ATOM   3470 C CG  . PRO A 1 458 ? 82.101  121.865 86.042  1.00 114.58 ? 458 PRO A CG  1 
ATOM   3471 C CD  . PRO A 1 458 ? 81.165  120.699 85.865  1.00 115.94 ? 458 PRO A CD  1 
ATOM   3472 N N   . LEU A 1 459 ? 79.431  123.312 89.304  1.00 111.92 ? 459 LEU A N   1 
ATOM   3473 C CA  . LEU A 1 459 ? 78.529  124.447 89.472  1.00 109.93 ? 459 LEU A CA  1 
ATOM   3474 C C   . LEU A 1 459 ? 79.242  125.768 89.212  1.00 113.70 ? 459 LEU A C   1 
ATOM   3475 O O   . LEU A 1 459 ? 78.660  126.689 88.627  1.00 115.56 ? 459 LEU A O   1 
ATOM   3476 C CB  . LEU A 1 459 ? 77.920  124.431 90.874  1.00 105.25 ? 459 LEU A CB  1 
ATOM   3477 C CG  . LEU A 1 459 ? 77.071  123.212 91.244  1.00 102.06 ? 459 LEU A CG  1 
ATOM   3478 C CD1 . LEU A 1 459 ? 76.295  123.473 92.524  1.00 100.56 ? 459 LEU A CD1 1 
ATOM   3479 C CD2 . LEU A 1 459 ? 76.128  122.837 90.111  1.00 101.09 ? 459 LEU A CD2 1 
ATOM   3480 N N   . ILE A 1 460 ? 80.497  125.883 89.640  1.00 116.58 ? 460 ILE A N   1 
ATOM   3481 C CA  . ILE A 1 460 ? 81.298  127.087 89.449  1.00 117.00 ? 460 ILE A CA  1 
ATOM   3482 C C   . ILE A 1 460 ? 82.314  126.816 88.349  1.00 119.91 ? 460 ILE A C   1 
ATOM   3483 O O   . ILE A 1 460 ? 83.037  125.814 88.395  1.00 122.36 ? 460 ILE A O   1 
ATOM   3484 C CB  . ILE A 1 460 ? 82.000  127.514 90.750  1.00 113.70 ? 460 ILE A CB  1 
ATOM   3485 C CG1 . ILE A 1 460 ? 81.035  127.434 91.932  1.00 111.70 ? 460 ILE A CG1 1 
ATOM   3486 C CG2 . ILE A 1 460 ? 82.562  128.920 90.614  1.00 112.89 ? 460 ILE A CG2 1 
ATOM   3487 C CD1 . ILE A 1 460 ? 81.689  127.704 93.269  1.00 111.00 ? 460 ILE A CD1 1 
ATOM   3488 N N   . PHE A 1 461 ? 82.367  127.707 87.362  1.00 119.51 ? 461 PHE A N   1 
ATOM   3489 C CA  . PHE A 1 461 ? 83.274  127.572 86.228  1.00 117.69 ? 461 PHE A CA  1 
ATOM   3490 C C   . PHE A 1 461 ? 84.493  128.457 86.464  1.00 119.09 ? 461 PHE A C   1 
ATOM   3491 O O   . PHE A 1 461 ? 84.422  129.680 86.308  1.00 121.74 ? 461 PHE A O   1 
ATOM   3492 C CB  . PHE A 1 461 ? 82.571  127.942 84.924  1.00 115.06 ? 461 PHE A CB  1 
ATOM   3493 C CG  . PHE A 1 461 ? 81.502  126.970 84.516  1.00 113.98 ? 461 PHE A CG  1 
ATOM   3494 C CD1 . PHE A 1 461 ? 81.836  125.752 83.946  1.00 114.01 ? 461 PHE A CD1 1 
ATOM   3495 C CD2 . PHE A 1 461 ? 80.163  127.273 84.700  1.00 112.81 ? 461 PHE A CD2 1 
ATOM   3496 C CE1 . PHE A 1 461 ? 80.856  124.855 83.568  1.00 114.11 ? 461 PHE A CE1 1 
ATOM   3497 C CE2 . PHE A 1 461 ? 79.177  126.379 84.324  1.00 112.73 ? 461 PHE A CE2 1 
ATOM   3498 C CZ  . PHE A 1 461 ? 79.525  125.169 83.758  1.00 113.02 ? 461 PHE A CZ  1 
ATOM   3499 N N   . TYR A 1 462 ? 85.608  127.835 86.838  1.00 119.03 ? 462 TYR A N   1 
ATOM   3500 C CA  . TYR A 1 462 ? 86.853  128.565 86.996  1.00 118.41 ? 462 TYR A CA  1 
ATOM   3501 C C   . TYR A 1 462 ? 87.402  128.963 85.625  1.00 119.72 ? 462 TYR A C   1 
ATOM   3502 O O   . TYR A 1 462 ? 87.086  128.326 84.617  1.00 119.46 ? 462 TYR A O   1 
ATOM   3503 C CB  . TYR A 1 462 ? 87.875  127.716 87.749  1.00 117.10 ? 462 TYR A CB  1 
ATOM   3504 C CG  . TYR A 1 462 ? 87.532  127.487 89.203  1.00 115.57 ? 462 TYR A CG  1 
ATOM   3505 C CD1 . TYR A 1 462 ? 86.704  126.440 89.586  1.00 115.55 ? 462 TYR A CD1 1 
ATOM   3506 C CD2 . TYR A 1 462 ? 88.036  128.319 90.194  1.00 114.83 ? 462 TYR A CD2 1 
ATOM   3507 C CE1 . TYR A 1 462 ? 86.388  126.227 90.915  1.00 115.49 ? 462 TYR A CE1 1 
ATOM   3508 C CE2 . TYR A 1 462 ? 87.726  128.114 91.524  1.00 116.09 ? 462 TYR A CE2 1 
ATOM   3509 C CZ  . TYR A 1 462 ? 86.902  127.068 91.878  1.00 116.51 ? 462 TYR A CZ  1 
ATOM   3510 O OH  . TYR A 1 462 ? 86.591  126.861 93.201  1.00 118.46 ? 462 TYR A OH  1 
ATOM   3511 N N   . PRO A 1 463 ? 88.201  130.032 85.557  1.00 119.84 ? 463 PRO A N   1 
ATOM   3512 C CA  . PRO A 1 463 ? 88.790  130.429 84.271  1.00 119.71 ? 463 PRO A CA  1 
ATOM   3513 C C   . PRO A 1 463 ? 89.695  129.345 83.700  1.00 120.44 ? 463 PRO A C   1 
ATOM   3514 O O   . PRO A 1 463 ? 90.386  128.634 84.432  1.00 121.72 ? 463 PRO A O   1 
ATOM   3515 C CB  . PRO A 1 463 ? 89.582  131.694 84.621  1.00 118.38 ? 463 PRO A CB  1 
ATOM   3516 C CG  . PRO A 1 463 ? 88.912  132.231 85.835  1.00 117.50 ? 463 PRO A CG  1 
ATOM   3517 C CD  . PRO A 1 463 ? 88.457  131.032 86.609  1.00 118.16 ? 463 PRO A CD  1 
ATOM   3518 N N   . GLY A 1 464 ? 89.681  129.228 82.375  1.00 120.88 ? 464 GLY A N   1 
ATOM   3519 C CA  . GLY A 1 464 ? 90.453  128.217 81.686  1.00 123.19 ? 464 GLY A CA  1 
ATOM   3520 C C   . GLY A 1 464 ? 89.775  126.875 81.531  1.00 126.71 ? 464 GLY A C   1 
ATOM   3521 O O   . GLY A 1 464 ? 90.442  125.908 81.142  1.00 128.31 ? 464 GLY A O   1 
ATOM   3522 N N   . TYR A 1 465 ? 88.480  126.779 81.823  1.00 130.40 ? 465 TYR A N   1 
ATOM   3523 C CA  . TYR A 1 465 ? 87.777  125.508 81.714  1.00 132.38 ? 465 TYR A CA  1 
ATOM   3524 C C   . TYR A 1 465 ? 87.617  125.102 80.253  1.00 132.66 ? 465 TYR A C   1 
ATOM   3525 O O   . TYR A 1 465 ? 87.406  125.944 79.376  1.00 130.63 ? 465 TYR A O   1 
ATOM   3526 C CB  . TYR A 1 465 ? 86.407  125.596 82.392  1.00 132.50 ? 465 TYR A CB  1 
ATOM   3527 C CG  . TYR A 1 465 ? 85.413  126.507 81.702  1.00 131.79 ? 465 TYR A CG  1 
ATOM   3528 C CD1 . TYR A 1 465 ? 85.416  127.877 81.935  1.00 130.99 ? 465 TYR A CD1 1 
ATOM   3529 C CD2 . TYR A 1 465 ? 84.453  125.993 80.837  1.00 131.14 ? 465 TYR A CD2 1 
ATOM   3530 C CE1 . TYR A 1 465 ? 84.506  128.711 81.311  1.00 131.45 ? 465 TYR A CE1 1 
ATOM   3531 C CE2 . TYR A 1 465 ? 83.540  126.819 80.209  1.00 130.91 ? 465 TYR A CE2 1 
ATOM   3532 C CZ  . TYR A 1 465 ? 83.570  128.176 80.450  1.00 131.86 ? 465 TYR A CZ  1 
ATOM   3533 O OH  . TYR A 1 465 ? 82.661  129.001 79.829  1.00 132.79 ? 465 TYR A OH  1 
ATOM   3534 N N   . TYR A 1 466 ? 87.725  123.803 79.996  1.00 134.65 ? 466 TYR A N   1 
ATOM   3535 C CA  . TYR A 1 466 ? 87.557  123.249 78.662  1.00 136.45 ? 466 TYR A CA  1 
ATOM   3536 C C   . TYR A 1 466 ? 86.729  121.976 78.745  1.00 139.16 ? 466 TYR A C   1 
ATOM   3537 O O   . TYR A 1 466 ? 86.823  121.236 79.732  1.00 143.91 ? 466 TYR A O   1 
ATOM   3538 C CB  . TYR A 1 466 ? 88.913  122.953 77.997  1.00 135.50 ? 466 TYR A CB  1 
ATOM   3539 C CG  . TYR A 1 466 ? 89.761  121.923 78.716  1.00 135.73 ? 466 TYR A CG  1 
ATOM   3540 C CD1 . TYR A 1 466 ? 90.616  122.296 79.745  1.00 135.73 ? 466 TYR A CD1 1 
ATOM   3541 C CD2 . TYR A 1 466 ? 89.724  120.582 78.350  1.00 135.18 ? 466 TYR A CD2 1 
ATOM   3542 C CE1 . TYR A 1 466 ? 91.397  121.363 80.401  1.00 135.23 ? 466 TYR A CE1 1 
ATOM   3543 C CE2 . TYR A 1 466 ? 90.500  119.642 79.001  1.00 134.38 ? 466 TYR A CE2 1 
ATOM   3544 C CZ  . TYR A 1 466 ? 91.335  120.038 80.025  1.00 134.59 ? 466 TYR A CZ  1 
ATOM   3545 O OH  . TYR A 1 466 ? 92.111  119.106 80.674  1.00 133.61 ? 466 TYR A OH  1 
ATOM   3546 N N   . PRO A 1 467 ? 85.913  121.696 77.733  1.00 137.86 ? 467 PRO A N   1 
ATOM   3547 C CA  . PRO A 1 467 ? 85.156  120.441 77.720  1.00 135.92 ? 467 PRO A CA  1 
ATOM   3548 C C   . PRO A 1 467 ? 86.019  119.265 77.294  1.00 136.09 ? 467 PRO A C   1 
ATOM   3549 O O   . PRO A 1 467 ? 86.979  119.405 76.533  1.00 138.16 ? 467 PRO A O   1 
ATOM   3550 C CB  . PRO A 1 467 ? 84.048  120.713 76.697  1.00 133.49 ? 467 PRO A CB  1 
ATOM   3551 C CG  . PRO A 1 467 ? 84.664  121.684 75.751  1.00 133.41 ? 467 PRO A CG  1 
ATOM   3552 C CD  . PRO A 1 467 ? 85.582  122.551 76.578  1.00 135.23 ? 467 PRO A CD  1 
ATOM   3553 N N   . ASP A 1 468 ? 85.661  118.089 77.803  1.00 133.80 ? 468 ASP A N   1 
ATOM   3554 C CA  . ASP A 1 468 ? 86.391  116.869 77.497  1.00 132.89 ? 468 ASP A CA  1 
ATOM   3555 C C   . ASP A 1 468 ? 85.764  116.177 76.286  1.00 132.76 ? 468 ASP A C   1 
ATOM   3556 O O   . ASP A 1 468 ? 84.877  116.719 75.621  1.00 131.81 ? 468 ASP A O   1 
ATOM   3557 C CB  . ASP A 1 468 ? 86.447  115.963 78.729  1.00 133.55 ? 468 ASP A CB  1 
ATOM   3558 C CG  . ASP A 1 468 ? 85.107  115.311 79.058  1.00 135.10 ? 468 ASP A CG  1 
ATOM   3559 O OD1 . ASP A 1 468 ? 84.046  115.830 78.652  1.00 137.88 ? 468 ASP A OD1 1 
ATOM   3560 O OD2 . ASP A 1 468 ? 85.120  114.261 79.735  1.00 132.87 ? 468 ASP A OD2 1 
ATOM   3561 N N   . ASP A 1 469 ? 86.230  114.963 75.985  1.00 132.30 ? 469 ASP A N   1 
ATOM   3562 C CA  . ASP A 1 469 ? 85.642  114.194 74.893  1.00 132.13 ? 469 ASP A CA  1 
ATOM   3563 C C   . ASP A 1 469 ? 84.235  113.716 75.235  1.00 134.68 ? 469 ASP A C   1 
ATOM   3564 O O   . ASP A 1 469 ? 83.373  113.624 74.353  1.00 134.68 ? 469 ASP A O   1 
ATOM   3565 C CB  . ASP A 1 469 ? 86.560  113.023 74.525  1.00 128.70 ? 469 ASP A CB  1 
ATOM   3566 C CG  . ASP A 1 469 ? 86.768  112.036 75.672  1.00 126.69 ? 469 ASP A CG  1 
ATOM   3567 O OD1 . ASP A 1 469 ? 86.252  112.257 76.788  1.00 125.45 ? 469 ASP A OD1 1 
ATOM   3568 O OD2 . ASP A 1 469 ? 87.462  111.022 75.448  1.00 125.82 ? 469 ASP A OD2 1 
ATOM   3569 N N   . ASN A 1 470 ? 83.984  113.406 76.507  1.00 136.67 ? 470 ASN A N   1 
ATOM   3570 C CA  . ASN A 1 470 ? 82.680  112.918 76.937  1.00 133.45 ? 470 ASN A CA  1 
ATOM   3571 C C   . ASN A 1 470 ? 81.629  114.016 77.035  1.00 134.56 ? 470 ASN A C   1 
ATOM   3572 O O   . ASN A 1 470 ? 80.445  113.702 77.192  1.00 136.20 ? 470 ASN A O   1 
ATOM   3573 C CB  . ASN A 1 470 ? 82.806  112.206 78.286  1.00 129.66 ? 470 ASN A CB  1 
ATOM   3574 C CG  . ASN A 1 470 ? 83.143  110.736 78.138  1.00 128.49 ? 470 ASN A CG  1 
ATOM   3575 O OD1 . ASN A 1 470 ? 83.418  110.258 77.038  1.00 128.28 ? 470 ASN A OD1 1 
ATOM   3576 N ND2 . ASN A 1 470 ? 83.125  110.010 79.249  1.00 128.04 ? 470 ASN A ND2 1 
ATOM   3577 N N   . GLY A 1 471 ? 82.024  115.283 76.948  1.00 135.02 ? 471 GLY A N   1 
ATOM   3578 C CA  . GLY A 1 471 ? 81.083  116.382 76.980  1.00 134.62 ? 471 GLY A CA  1 
ATOM   3579 C C   . GLY A 1 471 ? 80.909  117.070 78.315  1.00 135.36 ? 471 GLY A C   1 
ATOM   3580 O O   . GLY A 1 471 ? 79.977  117.871 78.457  1.00 136.81 ? 471 GLY A O   1 
ATOM   3581 N N   . ILE A 1 472 ? 81.764  116.790 79.295  1.00 136.06 ? 472 ILE A N   1 
ATOM   3582 C CA  . ILE A 1 472 ? 81.686  117.425 80.604  1.00 135.31 ? 472 ILE A CA  1 
ATOM   3583 C C   . ILE A 1 472 ? 82.852  118.397 80.744  1.00 137.35 ? 472 ILE A C   1 
ATOM   3584 O O   . ILE A 1 472 ? 83.926  118.205 80.162  1.00 141.57 ? 472 ILE A O   1 
ATOM   3585 C CB  . ILE A 1 472 ? 81.664  116.378 81.744  1.00 132.43 ? 472 ILE A CB  1 
ATOM   3586 C CG1 . ILE A 1 472 ? 81.159  117.001 83.048  1.00 131.50 ? 472 ILE A CG1 1 
ATOM   3587 C CG2 . ILE A 1 472 ? 83.031  115.732 81.938  1.00 130.07 ? 472 ILE A CG2 1 
ATOM   3588 C CD1 . ILE A 1 472 ? 79.708  117.423 82.996  1.00 131.44 ? 472 ILE A CD1 1 
ATOM   3589 N N   . TYR A 1 473 ? 82.621  119.473 81.490  1.00 137.27 ? 473 TYR A N   1 
ATOM   3590 C CA  . TYR A 1 473 ? 83.623  120.516 81.641  1.00 137.38 ? 473 TYR A CA  1 
ATOM   3591 C C   . TYR A 1 473 ? 84.676  120.117 82.666  1.00 133.49 ? 473 TYR A C   1 
ATOM   3592 O O   . TYR A 1 473 ? 84.356  119.625 83.752  1.00 133.23 ? 473 TYR A O   1 
ATOM   3593 C CB  . TYR A 1 473 ? 82.963  121.832 82.051  1.00 141.23 ? 473 TYR A CB  1 
ATOM   3594 C CG  . TYR A 1 473 ? 81.971  122.353 81.036  1.00 144.56 ? 473 TYR A CG  1 
ATOM   3595 C CD1 . TYR A 1 473 ? 82.402  122.971 79.869  1.00 144.94 ? 473 TYR A CD1 1 
ATOM   3596 C CD2 . TYR A 1 473 ? 80.603  122.221 81.241  1.00 144.81 ? 473 TYR A CD2 1 
ATOM   3597 C CE1 . TYR A 1 473 ? 81.500  123.448 78.937  1.00 144.34 ? 473 TYR A CE1 1 
ATOM   3598 C CE2 . TYR A 1 473 ? 79.693  122.695 80.315  1.00 144.34 ? 473 TYR A CE2 1 
ATOM   3599 C CZ  . TYR A 1 473 ? 80.147  123.307 79.165  1.00 144.37 ? 473 TYR A CZ  1 
ATOM   3600 O OH  . TYR A 1 473 ? 79.245  123.780 78.240  1.00 143.71 ? 473 TYR A OH  1 
ATOM   3601 N N   . ASN A 1 474 ? 85.939  120.336 82.313  1.00 128.83 ? 474 ASN A N   1 
ATOM   3602 C CA  . ASN A 1 474 ? 87.070  120.076 83.189  1.00 123.76 ? 474 ASN A CA  1 
ATOM   3603 C C   . ASN A 1 474 ? 87.759  121.389 83.538  1.00 119.89 ? 474 ASN A C   1 
ATOM   3604 O O   . ASN A 1 474 ? 87.810  122.317 82.726  1.00 122.66 ? 474 ASN A O   1 
ATOM   3605 C CB  . ASN A 1 474 ? 88.071  119.119 82.536  1.00 122.76 ? 474 ASN A CB  1 
ATOM   3606 C CG  . ASN A 1 474 ? 87.491  117.739 82.304  1.00 122.08 ? 474 ASN A CG  1 
ATOM   3607 O OD1 . ASN A 1 474 ? 86.352  117.461 82.679  1.00 120.82 ? 474 ASN A OD1 1 
ATOM   3608 N ND2 . ASN A 1 474 ? 88.274  116.864 81.685  1.00 121.88 ? 474 ASN A ND2 1 
ATOM   3609 N N   . GLN A 1 475 ? 88.292  121.458 84.754  1.00 114.24 ? 475 GLN A N   1 
ATOM   3610 C CA  . GLN A 1 475 ? 88.891  122.679 85.277  1.00 110.42 ? 475 GLN A CA  1 
ATOM   3611 C C   . GLN A 1 475 ? 90.406  122.617 85.125  1.00 105.78 ? 475 GLN A C   1 
ATOM   3612 O O   . GLN A 1 475 ? 91.064  121.777 85.748  1.00 108.03 ? 475 GLN A O   1 
ATOM   3613 C CB  . GLN A 1 475 ? 88.509  122.884 86.743  1.00 111.43 ? 475 GLN A CB  1 
ATOM   3614 C CG  . GLN A 1 475 ? 87.022  122.760 87.024  1.00 112.55 ? 475 GLN A CG  1 
ATOM   3615 C CD  . GLN A 1 475 ? 86.236  123.970 86.562  1.00 115.04 ? 475 GLN A CD  1 
ATOM   3616 O OE1 . GLN A 1 475 ? 86.807  125.006 86.224  1.00 117.01 ? 475 GLN A OE1 1 
ATOM   3617 N NE2 . GLN A 1 475 ? 84.915  123.845 86.545  1.00 115.61 ? 475 GLN A NE2 1 
ATOM   3618 N N   . LYS A 1 476 ? 90.953  123.506 84.295  1.00 99.56  ? 476 LYS A N   1 
ATOM   3619 C CA  . LYS A 1 476 ? 92.399  123.655 84.192  1.00 95.45  ? 476 LYS A CA  1 
ATOM   3620 C C   . LYS A 1 476 ? 92.973  124.481 85.336  1.00 89.16  ? 476 LYS A C   1 
ATOM   3621 O O   . LYS A 1 476 ? 94.174  124.388 85.611  1.00 89.01  ? 476 LYS A O   1 
ATOM   3622 C CB  . LYS A 1 476 ? 92.763  124.294 82.849  1.00 96.91  ? 476 LYS A CB  1 
ATOM   3623 C CG  . LYS A 1 476 ? 94.201  124.071 82.405  1.00 96.49  ? 476 LYS A CG  1 
ATOM   3624 C CD  . LYS A 1 476 ? 94.361  124.345 80.919  1.00 96.40  ? 476 LYS A CD  1 
ATOM   3625 C CE  . LYS A 1 476 ? 95.672  123.788 80.392  1.00 96.76  ? 476 LYS A CE  1 
ATOM   3626 N NZ  . LYS A 1 476 ? 95.758  123.886 78.908  1.00 98.07  ? 476 LYS A NZ  1 
ATOM   3627 N N   . PHE A 1 477 ? 92.143  125.279 86.000  1.00 82.05  ? 477 PHE A N   1 
ATOM   3628 C CA  . PHE A 1 477 ? 92.602  126.081 87.123  1.00 78.50  ? 477 PHE A CA  1 
ATOM   3629 C C   . PHE A 1 477 ? 92.945  125.177 88.306  1.00 75.43  ? 477 PHE A C   1 
ATOM   3630 O O   . PHE A 1 477 ? 92.263  124.175 88.540  1.00 76.67  ? 477 PHE A O   1 
ATOM   3631 C CB  . PHE A 1 477 ? 91.520  127.084 87.524  1.00 78.97  ? 477 PHE A CB  1 
ATOM   3632 C CG  . PHE A 1 477 ? 92.048  128.322 88.191  1.00 79.29  ? 477 PHE A CG  1 
ATOM   3633 C CD1 . PHE A 1 477 ? 92.947  129.149 87.538  1.00 79.62  ? 477 PHE A CD1 1 
ATOM   3634 C CD2 . PHE A 1 477 ? 91.636  128.664 89.468  1.00 79.06  ? 477 PHE A CD2 1 
ATOM   3635 C CE1 . PHE A 1 477 ? 93.431  130.290 88.151  1.00 80.03  ? 477 PHE A CE1 1 
ATOM   3636 C CE2 . PHE A 1 477 ? 92.115  129.803 90.085  1.00 79.46  ? 477 PHE A CE2 1 
ATOM   3637 C CZ  . PHE A 1 477 ? 93.013  130.617 89.426  1.00 79.99  ? 477 PHE A CZ  1 
ATOM   3638 N N   . PRO A 1 478 ? 93.995  125.497 89.067  1.00 71.28  ? 478 PRO A N   1 
ATOM   3639 C CA  . PRO A 1 478 ? 94.318  124.690 90.250  1.00 68.99  ? 478 PRO A CA  1 
ATOM   3640 C C   . PRO A 1 478 ? 93.344  124.918 91.394  1.00 67.06  ? 478 PRO A C   1 
ATOM   3641 O O   . PRO A 1 478 ? 93.676  125.589 92.376  1.00 66.63  ? 478 PRO A O   1 
ATOM   3642 C CB  . PRO A 1 478 ? 95.732  125.158 90.609  1.00 68.72  ? 478 PRO A CB  1 
ATOM   3643 C CG  . PRO A 1 478 ? 95.786  126.561 90.124  1.00 69.12  ? 478 PRO A CG  1 
ATOM   3644 C CD  . PRO A 1 478 ? 94.977  126.575 88.854  1.00 70.09  ? 478 PRO A CD  1 
ATOM   3645 N N   . PHE A 1 479 ? 92.137  124.361 91.283  1.00 64.67  ? 479 PHE A N   1 
ATOM   3646 C CA  . PHE A 1 479 ? 91.120  124.592 92.300  1.00 62.55  ? 479 PHE A CA  1 
ATOM   3647 C C   . PHE A 1 479 ? 91.323  123.746 93.549  1.00 60.45  ? 479 PHE A C   1 
ATOM   3648 O O   . PHE A 1 479 ? 90.727  124.053 94.584  1.00 60.69  ? 479 PHE A O   1 
ATOM   3649 C CB  . PHE A 1 479 ? 89.721  124.351 91.718  1.00 62.82  ? 479 PHE A CB  1 
ATOM   3650 C CG  . PHE A 1 479 ? 89.434  122.915 91.376  1.00 63.99  ? 479 PHE A CG  1 
ATOM   3651 C CD1 . PHE A 1 479 ? 89.824  122.389 90.155  1.00 64.45  ? 479 PHE A CD1 1 
ATOM   3652 C CD2 . PHE A 1 479 ? 88.741  122.101 92.258  1.00 64.95  ? 479 PHE A CD2 1 
ATOM   3653 C CE1 . PHE A 1 479 ? 89.553  121.073 89.832  1.00 64.77  ? 479 PHE A CE1 1 
ATOM   3654 C CE2 . PHE A 1 479 ? 88.468  120.785 91.940  1.00 65.41  ? 479 PHE A CE2 1 
ATOM   3655 C CZ  . PHE A 1 479 ? 88.873  120.272 90.725  1.00 65.26  ? 479 PHE A CZ  1 
ATOM   3656 N N   . LYS A 1 480 ? 92.160  122.708 93.491  1.00 57.92  ? 480 LYS A N   1 
ATOM   3657 C CA  . LYS A 1 480 ? 92.374  121.866 94.665  1.00 55.79  ? 480 LYS A CA  1 
ATOM   3658 C C   . LYS A 1 480 ? 93.218  122.583 95.714  1.00 55.43  ? 480 LYS A C   1 
ATOM   3659 O O   . LYS A 1 480 ? 92.807  122.715 96.875  1.00 56.88  ? 480 LYS A O   1 
ATOM   3660 C CB  . LYS A 1 480 ? 93.029  120.548 94.252  1.00 54.57  ? 480 LYS A CB  1 
ATOM   3661 C CG  . LYS A 1 480 ? 92.221  119.745 93.249  1.00 53.93  ? 480 LYS A CG  1 
ATOM   3662 C CD  . LYS A 1 480 ? 92.971  118.504 92.799  1.00 54.11  ? 480 LYS A CD  1 
ATOM   3663 C CE  . LYS A 1 480 ? 92.170  117.718 91.773  1.00 54.15  ? 480 LYS A CE  1 
ATOM   3664 N NZ  . LYS A 1 480 ? 92.865  116.467 91.360  1.00 54.60  ? 480 LYS A NZ  1 
ATOM   3665 N N   . THR A 1 481 ? 94.404  123.058 95.323  1.00 53.78  ? 481 THR A N   1 
ATOM   3666 C CA  . THR A 1 481 ? 95.242  123.785 96.270  1.00 52.88  ? 481 THR A CA  1 
ATOM   3667 C C   . THR A 1 481 ? 94.634  125.134 96.635  1.00 51.49  ? 481 THR A C   1 
ATOM   3668 O O   . THR A 1 481 ? 94.807  125.601 97.768  1.00 50.57  ? 481 THR A O   1 
ATOM   3669 C CB  . THR A 1 481 ? 96.663  123.945 95.716  1.00 53.59  ? 481 THR A CB  1 
ATOM   3670 O OG1 . THR A 1 481 ? 97.501  124.549 96.709  1.00 55.18  ? 481 THR A OG1 1 
ATOM   3671 C CG2 . THR A 1 481 ? 96.685  124.786 94.447  1.00 53.72  ? 481 THR A CG2 1 
ATOM   3672 N N   . LEU A 1 482 ? 93.892  125.757 95.714  1.00 50.76  ? 482 LEU A N   1 
ATOM   3673 C CA  . LEU A 1 482 ? 93.178  126.983 96.053  1.00 50.95  ? 482 LEU A CA  1 
ATOM   3674 C C   . LEU A 1 482 ? 92.077  126.707 97.068  1.00 51.27  ? 482 LEU A C   1 
ATOM   3675 O O   . LEU A 1 482 ? 91.854  127.511 97.979  1.00 51.78  ? 482 LEU A O   1 
ATOM   3676 C CB  . LEU A 1 482 ? 92.610  127.632 94.790  1.00 50.53  ? 482 LEU A CB  1 
ATOM   3677 C CG  . LEU A 1 482 ? 91.996  129.029 94.920  1.00 49.84  ? 482 LEU A CG  1 
ATOM   3678 C CD1 . LEU A 1 482 ? 92.374  129.871 93.717  1.00 50.04  ? 482 LEU A CD1 1 
ATOM   3679 C CD2 . LEU A 1 482 ? 90.481  128.965 95.051  1.00 49.12  ? 482 LEU A CD2 1 
ATOM   3680 N N   . ALA A 1 483 ? 91.385  125.573 96.930  1.00 51.17  ? 483 ALA A N   1 
ATOM   3681 C CA  . ALA A 1 483 ? 90.373  125.195 97.909  1.00 51.04  ? 483 ALA A CA  1 
ATOM   3682 C C   . ALA A 1 483 ? 90.998  124.928 99.270  1.00 50.81  ? 483 ALA A C   1 
ATOM   3683 O O   . ALA A 1 483 ? 90.439  125.317 100.301 1.00 50.44  ? 483 ALA A O   1 
ATOM   3684 C CB  . ALA A 1 483 ? 89.602  123.969 97.422  1.00 51.04  ? 483 ALA A CB  1 
ATOM   3685 N N   . MET A 1 484 ? 92.159  124.266 99.294  1.00 50.91  ? 484 MET A N   1 
ATOM   3686 C CA  . MET A 1 484 ? 92.838  124.028 100.567 1.00 51.13  ? 484 MET A CA  1 
ATOM   3687 C C   . MET A 1 484 ? 93.260  125.337 101.224 1.00 50.29  ? 484 MET A C   1 
ATOM   3688 O O   . MET A 1 484 ? 93.085  125.518 102.436 1.00 50.24  ? 484 MET A O   1 
ATOM   3689 C CB  . MET A 1 484 ? 94.065  123.141 100.374 1.00 52.23  ? 484 MET A CB  1 
ATOM   3690 C CG  . MET A 1 484 ? 94.765  122.838 101.690 1.00 53.58  ? 484 MET A CG  1 
ATOM   3691 S SD  . MET A 1 484 ? 96.275  123.784 101.954 1.00 55.95  ? 484 MET A SD  1 
ATOM   3692 C CE  . MET A 1 484 ? 97.453  122.821 101.028 1.00 55.80  ? 484 MET A CE  1 
ATOM   3693 N N   . VAL A 1 485 ? 93.826  126.258 100.438 1.00 49.18  ? 485 VAL A N   1 
ATOM   3694 C CA  . VAL A 1 485 ? 94.268  127.541 100.979 1.00 48.13  ? 485 VAL A CA  1 
ATOM   3695 C C   . VAL A 1 485 ? 93.077  128.343 101.487 1.00 48.27  ? 485 VAL A C   1 
ATOM   3696 O O   . VAL A 1 485 ? 93.138  128.963 102.557 1.00 49.41  ? 485 VAL A O   1 
ATOM   3697 C CB  . VAL A 1 485 ? 95.075  128.312 99.917  1.00 47.28  ? 485 VAL A CB  1 
ATOM   3698 C CG1 . VAL A 1 485 ? 95.170  129.789 100.261 1.00 47.02  ? 485 VAL A CG1 1 
ATOM   3699 C CG2 . VAL A 1 485 ? 96.462  127.712 99.774  1.00 47.00  ? 485 VAL A CG2 1 
ATOM   3700 N N   . THR A 1 486 ? 91.968  128.327 100.740 1.00 47.37  ? 486 THR A N   1 
ATOM   3701 C CA  . THR A 1 486 ? 90.760  129.019 101.176 1.00 46.72  ? 486 THR A CA  1 
ATOM   3702 C C   . THR A 1 486 ? 90.209  128.417 102.462 1.00 46.55  ? 486 THR A C   1 
ATOM   3703 O O   . THR A 1 486 ? 89.790  129.150 103.363 1.00 46.52  ? 486 THR A O   1 
ATOM   3704 C CB  . THR A 1 486 ? 89.704  128.977 100.071 1.00 46.42  ? 486 THR A CB  1 
ATOM   3705 O OG1 . THR A 1 486 ? 90.260  129.502 98.860  1.00 46.97  ? 486 THR A OG1 1 
ATOM   3706 C CG2 . THR A 1 486 ? 88.489  129.804 100.459 1.00 46.46  ? 486 THR A CG2 1 
ATOM   3707 N N   . SER A 1 487 ? 90.212  127.084 102.571 1.00 46.53  ? 487 SER A N   1 
ATOM   3708 C CA  . SER A 1 487 ? 89.734  126.434 103.788 1.00 47.01  ? 487 SER A CA  1 
ATOM   3709 C C   . SER A 1 487 ? 90.603  126.789 104.987 1.00 46.86  ? 487 SER A C   1 
ATOM   3710 O O   . SER A 1 487 ? 90.086  127.087 106.068 1.00 47.35  ? 487 SER A O   1 
ATOM   3711 C CB  . SER A 1 487 ? 89.691  124.919 103.593 1.00 47.41  ? 487 SER A CB  1 
ATOM   3712 O OG  . SER A 1 487 ? 89.414  124.258 104.815 1.00 47.80  ? 487 SER A OG  1 
ATOM   3713 N N   . PHE A 1 488 ? 91.925  126.780 104.809 1.00 46.75  ? 488 PHE A N   1 
ATOM   3714 C CA  . PHE A 1 488 ? 92.832  127.125 105.901 1.00 46.98  ? 488 PHE A CA  1 
ATOM   3715 C C   . PHE A 1 488 ? 92.658  128.581 106.329 1.00 47.22  ? 488 PHE A C   1 
ATOM   3716 O O   . PHE A 1 488 ? 92.571  128.883 107.531 1.00 46.92  ? 488 PHE A O   1 
ATOM   3717 C CB  . PHE A 1 488 ? 94.270  126.844 105.460 1.00 47.32  ? 488 PHE A CB  1 
ATOM   3718 C CG  . PHE A 1 488 ? 95.312  127.196 106.478 1.00 47.51  ? 488 PHE A CG  1 
ATOM   3719 C CD1 . PHE A 1 488 ? 95.171  126.822 107.801 1.00 47.72  ? 488 PHE A CD1 1 
ATOM   3720 C CD2 . PHE A 1 488 ? 96.454  127.880 106.099 1.00 47.62  ? 488 PHE A CD2 1 
ATOM   3721 C CE1 . PHE A 1 488 ? 96.142  127.139 108.730 1.00 47.76  ? 488 PHE A CE1 1 
ATOM   3722 C CE2 . PHE A 1 488 ? 97.425  128.201 107.022 1.00 47.85  ? 488 PHE A CE2 1 
ATOM   3723 C CZ  . PHE A 1 488 ? 97.270  127.828 108.338 1.00 47.95  ? 488 PHE A CZ  1 
ATOM   3724 N N   . LEU A 1 489 ? 92.574  129.492 105.354 1.00 48.07  ? 489 LEU A N   1 
ATOM   3725 C CA  . LEU A 1 489 ? 92.419  130.908 105.663 1.00 48.81  ? 489 LEU A CA  1 
ATOM   3726 C C   . LEU A 1 489 ? 91.082  131.192 106.333 1.00 49.60  ? 489 LEU A C   1 
ATOM   3727 O O   . LEU A 1 489 ? 91.021  131.971 107.291 1.00 50.02  ? 489 LEU A O   1 
ATOM   3728 C CB  . LEU A 1 489 ? 92.573  131.741 104.392 1.00 49.02  ? 489 LEU A CB  1 
ATOM   3729 C CG  . LEU A 1 489 ? 94.010  131.978 103.922 1.00 49.34  ? 489 LEU A CG  1 
ATOM   3730 C CD1 . LEU A 1 489 ? 94.047  133.020 102.818 1.00 49.64  ? 489 LEU A CD1 1 
ATOM   3731 C CD2 . LEU A 1 489 ? 94.898  132.393 105.083 1.00 49.22  ? 489 LEU A CD2 1 
ATOM   3732 N N   . THR A 1 490 ? 89.999  130.566 105.862 1.00 50.62  ? 490 THR A N   1 
ATOM   3733 C CA  . THR A 1 490 ? 88.708  130.807 106.494 1.00 51.41  ? 490 THR A CA  1 
ATOM   3734 C C   . THR A 1 490 ? 88.621  130.124 107.852 1.00 51.25  ? 490 THR A C   1 
ATOM   3735 O O   . THR A 1 490 ? 87.908  130.610 108.731 1.00 49.07  ? 490 THR A O   1 
ATOM   3736 C CB  . THR A 1 490 ? 87.555  130.372 105.580 1.00 51.99  ? 490 THR A CB  1 
ATOM   3737 O OG1 . THR A 1 490 ? 86.329  130.933 106.065 1.00 53.49  ? 490 THR A OG1 1 
ATOM   3738 C CG2 . THR A 1 490 ? 87.405  128.859 105.529 1.00 51.49  ? 490 THR A CG2 1 
ATOM   3739 N N   . ASN A 1 491 ? 89.372  129.038 108.063 1.00 53.50  ? 491 ASN A N   1 
ATOM   3740 C CA  . ASN A 1 491 ? 89.440  128.432 109.387 1.00 55.67  ? 491 ASN A CA  1 
ATOM   3741 C C   . ASN A 1 491 ? 90.072  129.406 110.373 1.00 56.97  ? 491 ASN A C   1 
ATOM   3742 O O   . ASN A 1 491 ? 89.520  129.661 111.452 1.00 57.31  ? 491 ASN A O   1 
ATOM   3743 C CB  . ASN A 1 491 ? 90.236  127.123 109.306 1.00 56.16  ? 491 ASN A CB  1 
ATOM   3744 C CG  . ASN A 1 491 ? 90.222  126.316 110.604 1.00 56.37  ? 491 ASN A CG  1 
ATOM   3745 O OD1 . ASN A 1 491 ? 89.944  126.826 111.688 1.00 57.30  ? 491 ASN A OD1 1 
ATOM   3746 N ND2 . ASN A 1 491 ? 90.539  125.034 110.485 1.00 56.45  ? 491 ASN A ND2 1 
ATOM   3747 N N   . ILE A 1 492 ? 91.208  129.998 109.988 1.00 59.27  ? 492 ILE A N   1 
ATOM   3748 C CA  . ILE A 1 492 ? 91.865  130.981 110.851 1.00 61.57  ? 492 ILE A CA  1 
ATOM   3749 C C   . ILE A 1 492 ? 90.956  132.183 111.083 1.00 65.29  ? 492 ILE A C   1 
ATOM   3750 O O   . ILE A 1 492 ? 90.800  132.659 112.216 1.00 66.86  ? 492 ILE A O   1 
ATOM   3751 C CB  . ILE A 1 492 ? 93.215  131.414 110.252 1.00 60.86  ? 492 ILE A CB  1 
ATOM   3752 C CG1 . ILE A 1 492 ? 94.202  130.253 110.234 1.00 60.46  ? 492 ILE A CG1 1 
ATOM   3753 C CG2 . ILE A 1 492 ? 93.803  132.578 111.029 1.00 60.38  ? 492 ILE A CG2 1 
ATOM   3754 C CD1 . ILE A 1 492 ? 95.458  130.583 109.481 1.00 60.46  ? 492 ILE A CD1 1 
ATOM   3755 N N   . CYS A 1 493 ? 90.329  132.680 110.012 1.00 68.20  ? 493 CYS A N   1 
ATOM   3756 C CA  . CYS A 1 493 ? 89.525  133.894 110.108 1.00 69.66  ? 493 CYS A CA  1 
ATOM   3757 C C   . CYS A 1 493 ? 88.299  133.686 110.990 1.00 69.73  ? 493 CYS A C   1 
ATOM   3758 O O   . CYS A 1 493 ? 88.002  134.519 111.851 1.00 69.84  ? 493 CYS A O   1 
ATOM   3759 C CB  . CYS A 1 493 ? 89.113  134.358 108.711 1.00 71.20  ? 493 CYS A CB  1 
ATOM   3760 S SG  . CYS A 1 493 ? 88.221  135.929 108.681 1.00 75.89  ? 493 CYS A SG  1 
ATOM   3761 N N   . ILE A 1 494 ? 87.582  132.574 110.803 1.00 69.62  ? 494 ILE A N   1 
ATOM   3762 C CA  . ILE A 1 494 ? 86.390  132.317 111.603 1.00 69.24  ? 494 ILE A CA  1 
ATOM   3763 C C   . ILE A 1 494 ? 86.763  132.023 113.052 1.00 70.11  ? 494 ILE A C   1 
ATOM   3764 O O   . ILE A 1 494 ? 86.070  132.462 113.977 1.00 70.43  ? 494 ILE A O   1 
ATOM   3765 C CB  . ILE A 1 494 ? 85.555  131.186 110.974 1.00 68.34  ? 494 ILE A CB  1 
ATOM   3766 C CG1 . ILE A 1 494 ? 85.021  131.626 109.611 1.00 67.74  ? 494 ILE A CG1 1 
ATOM   3767 C CG2 . ILE A 1 494 ? 84.392  130.793 111.869 1.00 67.83  ? 494 ILE A CG2 1 
ATOM   3768 C CD1 . ILE A 1 494 ? 84.093  132.816 109.678 1.00 67.53  ? 494 ILE A CD1 1 
ATOM   3769 N N   . SER A 1 495 ? 87.871  131.304 113.281 1.00 71.49  ? 495 SER A N   1 
ATOM   3770 C CA  . SER A 1 495 ? 88.309  131.050 114.652 1.00 73.03  ? 495 SER A CA  1 
ATOM   3771 C C   . SER A 1 495 ? 88.621  132.353 115.379 1.00 75.41  ? 495 SER A C   1 
ATOM   3772 O O   . SER A 1 495 ? 88.142  132.586 116.498 1.00 76.07  ? 495 SER A O   1 
ATOM   3773 C CB  . SER A 1 495 ? 89.533  130.135 114.650 1.00 73.13  ? 495 SER A CB  1 
ATOM   3774 O OG  . SER A 1 495 ? 89.222  128.860 114.122 1.00 74.43  ? 495 SER A OG  1 
ATOM   3775 N N   . TYR A 1 496 ? 89.399  133.231 114.740 1.00 78.97  ? 496 TYR A N   1 
ATOM   3776 C CA  . TYR A 1 496 ? 89.773  134.486 115.384 1.00 82.52  ? 496 TYR A CA  1 
ATOM   3777 C C   . TYR A 1 496 ? 88.571  135.411 115.542 1.00 83.20  ? 496 TYR A C   1 
ATOM   3778 O O   . TYR A 1 496 ? 88.450  136.105 116.558 1.00 81.01  ? 496 TYR A O   1 
ATOM   3779 C CB  . TYR A 1 496 ? 90.887  135.170 114.592 1.00 86.31  ? 496 TYR A CB  1 
ATOM   3780 C CG  . TYR A 1 496 ? 92.258  134.567 114.816 1.00 90.42  ? 496 TYR A CG  1 
ATOM   3781 C CD1 . TYR A 1 496 ? 92.442  133.515 115.706 1.00 92.09  ? 496 TYR A CD1 1 
ATOM   3782 C CD2 . TYR A 1 496 ? 93.368  135.047 114.134 1.00 93.40  ? 496 TYR A CD2 1 
ATOM   3783 C CE1 . TYR A 1 496 ? 93.690  132.961 115.911 1.00 94.59  ? 496 TYR A CE1 1 
ATOM   3784 C CE2 . TYR A 1 496 ? 94.621  134.499 114.333 1.00 95.51  ? 496 TYR A CE2 1 
ATOM   3785 C CZ  . TYR A 1 496 ? 94.776  133.457 115.223 1.00 96.66  ? 496 TYR A CZ  1 
ATOM   3786 O OH  . TYR A 1 496 ? 96.021  132.908 115.425 1.00 100.50 ? 496 TYR A OH  1 
ATOM   3787 N N   . LEU A 1 497 ? 87.666  135.424 114.559 1.00 86.03  ? 497 LEU A N   1 
ATOM   3788 C CA  . LEU A 1 497 ? 86.469  136.252 114.657 1.00 87.15  ? 497 LEU A CA  1 
ATOM   3789 C C   . LEU A 1 497 ? 85.560  135.788 115.787 1.00 86.87  ? 497 LEU A C   1 
ATOM   3790 O O   . LEU A 1 497 ? 85.036  136.613 116.543 1.00 84.81  ? 497 LEU A O   1 
ATOM   3791 C CB  . LEU A 1 497 ? 85.716  136.243 113.327 1.00 87.59  ? 497 LEU A CB  1 
ATOM   3792 C CG  . LEU A 1 497 ? 84.419  137.051 113.270 1.00 87.19  ? 497 LEU A CG  1 
ATOM   3793 C CD1 . LEU A 1 497 ? 84.684  138.512 113.590 1.00 87.30  ? 497 LEU A CD1 1 
ATOM   3794 C CD2 . LEU A 1 497 ? 83.759  136.907 111.909 1.00 86.70  ? 497 LEU A CD2 1 
ATOM   3795 N N   . ALA A 1 498 ? 85.361  134.473 115.921 1.00 88.24  ? 498 ALA A N   1 
ATOM   3796 C CA  . ALA A 1 498 ? 84.539  133.954 117.008 1.00 89.37  ? 498 ALA A CA  1 
ATOM   3797 C C   . ALA A 1 498 ? 85.175  134.236 118.361 1.00 91.16  ? 498 ALA A C   1 
ATOM   3798 O O   . ALA A 1 498 ? 84.480  134.612 119.315 1.00 92.72  ? 498 ALA A O   1 
ATOM   3799 C CB  . ALA A 1 498 ? 84.308  132.455 116.824 1.00 89.72  ? 498 ALA A CB  1 
ATOM   3800 N N   . LYS A 1 499 ? 86.499  134.073 118.461 1.00 94.47  ? 499 LYS A N   1 
ATOM   3801 C CA  . LYS A 1 499 ? 87.185  134.373 119.714 1.00 98.82  ? 499 LYS A CA  1 
ATOM   3802 C C   . LYS A 1 499 ? 87.050  135.847 120.078 1.00 103.40 ? 499 LYS A C   1 
ATOM   3803 O O   . LYS A 1 499 ? 86.775  136.183 121.236 1.00 103.70 ? 499 LYS A O   1 
ATOM   3804 C CB  . LYS A 1 499 ? 88.657  133.973 119.611 1.00 98.96  ? 499 LYS A CB  1 
ATOM   3805 C CG  . LYS A 1 499 ? 89.491  134.338 120.826 1.00 99.64  ? 499 LYS A CG  1 
ATOM   3806 C CD  . LYS A 1 499 ? 90.929  133.874 120.663 1.00 100.19 ? 499 LYS A CD  1 
ATOM   3807 C CE  . LYS A 1 499 ? 91.790  134.327 121.831 1.00 101.13 ? 499 LYS A CE  1 
ATOM   3808 N NZ  . LYS A 1 499 ? 93.220  133.955 121.645 1.00 102.41 ? 499 LYS A NZ  1 
ATOM   3809 N N   . TYR A 1 500 ? 87.209  136.740 119.096 1.00 107.80 ? 500 TYR A N   1 
ATOM   3810 C CA  . TYR A 1 500 ? 87.082  138.170 119.357 1.00 110.08 ? 500 TYR A CA  1 
ATOM   3811 C C   . TYR A 1 500 ? 85.655  138.546 119.741 1.00 110.78 ? 500 TYR A C   1 
ATOM   3812 O O   . TYR A 1 500 ? 85.449  139.370 120.640 1.00 110.02 ? 500 TYR A O   1 
ATOM   3813 C CB  . TYR A 1 500 ? 87.539  138.968 118.136 1.00 111.30 ? 500 TYR A CB  1 
ATOM   3814 C CG  . TYR A 1 500 ? 87.041  140.396 118.110 1.00 110.84 ? 500 TYR A CG  1 
ATOM   3815 C CD1 . TYR A 1 500 ? 87.597  141.360 118.941 1.00 109.35 ? 500 TYR A CD1 1 
ATOM   3816 C CD2 . TYR A 1 500 ? 86.023  140.783 117.247 1.00 110.76 ? 500 TYR A CD2 1 
ATOM   3817 C CE1 . TYR A 1 500 ? 87.147  142.667 118.920 1.00 108.61 ? 500 TYR A CE1 1 
ATOM   3818 C CE2 . TYR A 1 500 ? 85.567  142.088 117.219 1.00 110.39 ? 500 TYR A CE2 1 
ATOM   3819 C CZ  . TYR A 1 500 ? 86.133  143.025 118.057 1.00 109.96 ? 500 TYR A CZ  1 
ATOM   3820 O OH  . TYR A 1 500 ? 85.683  144.325 118.032 1.00 112.13 ? 500 TYR A OH  1 
ATOM   3821 N N   . LEU A 1 501 ? 84.658  137.964 119.068 1.00 111.45 ? 501 LEU A N   1 
ATOM   3822 C CA  . LEU A 1 501 ? 83.267  138.269 119.391 1.00 111.04 ? 501 LEU A CA  1 
ATOM   3823 C C   . LEU A 1 501 ? 82.897  137.786 120.788 1.00 113.85 ? 501 LEU A C   1 
ATOM   3824 O O   . LEU A 1 501 ? 82.193  138.487 121.524 1.00 113.89 ? 501 LEU A O   1 
ATOM   3825 C CB  . LEU A 1 501 ? 82.331  137.657 118.350 1.00 108.78 ? 501 LEU A CB  1 
ATOM   3826 C CG  . LEU A 1 501 ? 82.305  138.316 116.969 1.00 107.71 ? 501 LEU A CG  1 
ATOM   3827 C CD1 . LEU A 1 501 ? 81.333  137.593 116.050 1.00 106.37 ? 501 LEU A CD1 1 
ATOM   3828 C CD2 . LEU A 1 501 ? 81.947  139.788 117.083 1.00 108.36 ? 501 LEU A CD2 1 
ATOM   3829 N N   . PHE A 1 502 ? 83.356  136.593 121.174 1.00 118.63 ? 502 PHE A N   1 
ATOM   3830 C CA  . PHE A 1 502 ? 83.016  136.092 122.500 1.00 121.50 ? 502 PHE A CA  1 
ATOM   3831 C C   . PHE A 1 502 ? 83.813  136.779 123.604 1.00 124.25 ? 502 PHE A C   1 
ATOM   3832 O O   . PHE A 1 502 ? 83.321  136.890 124.732 1.00 127.99 ? 502 PHE A O   1 
ATOM   3833 C CB  . PHE A 1 502 ? 83.213  134.577 122.562 1.00 122.20 ? 502 PHE A CB  1 
ATOM   3834 C CG  . PHE A 1 502 ? 82.202  133.804 121.762 1.00 123.61 ? 502 PHE A CG  1 
ATOM   3835 C CD1 . PHE A 1 502 ? 80.860  134.142 121.810 1.00 122.75 ? 502 PHE A CD1 1 
ATOM   3836 C CD2 . PHE A 1 502 ? 82.590  132.736 120.971 1.00 125.80 ? 502 PHE A CD2 1 
ATOM   3837 C CE1 . PHE A 1 502 ? 79.925  133.435 121.077 1.00 123.06 ? 502 PHE A CE1 1 
ATOM   3838 C CE2 . PHE A 1 502 ? 81.660  132.025 120.235 1.00 125.22 ? 502 PHE A CE2 1 
ATOM   3839 C CZ  . PHE A 1 502 ? 80.326  132.376 120.289 1.00 123.66 ? 502 PHE A CZ  1 
ATOM   3840 N N   . GLU A 1 503 ? 85.032  137.242 123.313 1.00 124.84 ? 503 GLU A N   1 
ATOM   3841 C CA  . GLU A 1 503 ? 85.796  137.965 124.324 1.00 125.74 ? 503 GLU A CA  1 
ATOM   3842 C C   . GLU A 1 503 ? 85.299  139.397 124.495 1.00 128.19 ? 503 GLU A C   1 
ATOM   3843 O O   . GLU A 1 503 ? 85.266  139.913 125.617 1.00 128.95 ? 503 GLU A O   1 
ATOM   3844 C CB  . GLU A 1 503 ? 87.283  137.956 123.966 1.00 125.34 ? 503 GLU A CB  1 
ATOM   3845 C CG  . GLU A 1 503 ? 87.980  136.637 124.257 1.00 125.97 ? 503 GLU A CG  1 
ATOM   3846 C CD  . GLU A 1 503 ? 89.476  136.704 124.023 1.00 127.96 ? 503 GLU A CD  1 
ATOM   3847 O OE1 . GLU A 1 503 ? 89.944  137.705 123.440 1.00 131.55 ? 503 GLU A OE1 1 
ATOM   3848 O OE2 . GLU A 1 503 ? 90.185  135.756 124.422 1.00 127.04 ? 503 GLU A OE2 1 
ATOM   3849 N N   . SER A 1 504 ? 84.915  140.053 123.396 1.00 129.81 ? 504 SER A N   1 
ATOM   3850 C CA  . SER A 1 504 ? 84.457  141.436 123.477 1.00 128.73 ? 504 SER A CA  1 
ATOM   3851 C C   . SER A 1 504 ? 83.088  141.544 124.134 1.00 128.23 ? 504 SER A C   1 
ATOM   3852 O O   . SER A 1 504 ? 82.803  142.539 124.810 1.00 128.22 ? 504 SER A O   1 
ATOM   3853 C CB  . SER A 1 504 ? 84.426  142.061 122.083 1.00 128.14 ? 504 SER A CB  1 
ATOM   3854 O OG  . SER A 1 504 ? 83.965  143.400 122.134 1.00 127.60 ? 504 SER A OG  1 
ATOM   3855 N N   . GLY A 1 505 ? 82.233  140.543 123.950 1.00 127.71 ? 505 GLY A N   1 
ATOM   3856 C CA  . GLY A 1 505 ? 80.905  140.558 124.520 1.00 127.61 ? 505 GLY A CA  1 
ATOM   3857 C C   . GLY A 1 505 ? 79.796  140.995 123.590 1.00 129.56 ? 505 GLY A C   1 
ATOM   3858 O O   . GLY A 1 505 ? 78.687  141.263 124.067 1.00 129.92 ? 505 GLY A O   1 
ATOM   3859 N N   . THR A 1 506 ? 80.062  141.095 122.284 1.00 132.05 ? 506 THR A N   1 
ATOM   3860 C CA  . THR A 1 506 ? 79.004  141.428 121.334 1.00 132.98 ? 506 THR A CA  1 
ATOM   3861 C C   . THR A 1 506 ? 77.932  140.345 121.305 1.00 135.38 ? 506 THR A C   1 
ATOM   3862 O O   . THR A 1 506 ? 76.732  140.645 121.320 1.00 136.94 ? 506 THR A O   1 
ATOM   3863 C CB  . THR A 1 506 ? 79.596  141.637 119.940 1.00 131.12 ? 506 THR A CB  1 
ATOM   3864 O OG1 . THR A 1 506 ? 80.592  142.666 119.992 1.00 132.00 ? 506 THR A OG1 1 
ATOM   3865 C CG2 . THR A 1 506 ? 78.512  142.041 118.951 1.00 129.40 ? 506 THR A CG2 1 
ATOM   3866 N N   . LEU A 1 507 ? 78.346  139.079 121.273 1.00 136.62 ? 507 LEU A N   1 
ATOM   3867 C CA  . LEU A 1 507 ? 77.416  137.967 121.374 1.00 136.17 ? 507 LEU A CA  1 
ATOM   3868 C C   . LEU A 1 507 ? 77.238  137.559 122.834 1.00 138.60 ? 507 LEU A C   1 
ATOM   3869 O O   . LEU A 1 507 ? 78.165  137.698 123.639 1.00 139.34 ? 507 LEU A O   1 
ATOM   3870 C CB  . LEU A 1 507 ? 77.920  136.775 120.565 1.00 133.14 ? 507 LEU A CB  1 
ATOM   3871 C CG  . LEU A 1 507 ? 77.679  136.833 119.056 1.00 130.18 ? 507 LEU A CG  1 
ATOM   3872 C CD1 . LEU A 1 507 ? 78.407  135.698 118.352 1.00 129.64 ? 507 LEU A CD1 1 
ATOM   3873 C CD2 . LEU A 1 507 ? 76.191  136.791 118.748 1.00 128.35 ? 507 LEU A CD2 1 
ATOM   3874 N N   . PRO A 1 508 ? 76.051  137.084 123.204 1.00 140.33 ? 508 PRO A N   1 
ATOM   3875 C CA  . PRO A 1 508 ? 75.831  136.606 124.576 1.00 141.11 ? 508 PRO A CA  1 
ATOM   3876 C C   . PRO A 1 508 ? 76.722  135.420 124.893 1.00 143.88 ? 508 PRO A C   1 
ATOM   3877 O O   . PRO A 1 508 ? 76.961  134.563 124.028 1.00 147.24 ? 508 PRO A O   1 
ATOM   3878 C CB  . PRO A 1 508 ? 74.347  136.206 124.578 1.00 138.64 ? 508 PRO A CB  1 
ATOM   3879 C CG  . PRO A 1 508 ? 73.741  136.998 123.471 1.00 138.00 ? 508 PRO A CG  1 
ATOM   3880 C CD  . PRO A 1 508 ? 74.804  137.102 122.419 1.00 138.49 ? 508 PRO A CD  1 
ATOM   3881 N N   . PRO A 1 509 ? 77.249  135.346 126.119 1.00 142.60 ? 509 PRO A N   1 
ATOM   3882 C CA  . PRO A 1 509 ? 78.098  134.199 126.487 1.00 141.98 ? 509 PRO A CA  1 
ATOM   3883 C C   . PRO A 1 509 ? 77.371  132.866 126.472 1.00 141.99 ? 509 PRO A C   1 
ATOM   3884 O O   . PRO A 1 509 ? 78.019  131.822 126.330 1.00 144.53 ? 509 PRO A O   1 
ATOM   3885 C CB  . PRO A 1 509 ? 78.576  134.561 127.900 1.00 139.90 ? 509 PRO A CB  1 
ATOM   3886 C CG  . PRO A 1 509 ? 78.467  136.050 127.967 1.00 138.97 ? 509 PRO A CG  1 
ATOM   3887 C CD  . PRO A 1 509 ? 77.252  136.391 127.156 1.00 139.58 ? 509 PRO A CD  1 
ATOM   3888 N N   . LYS A 1 510 ? 76.048  132.864 126.630 1.00 138.35 ? 510 LYS A N   1 
ATOM   3889 C CA  . LYS A 1 510 ? 75.271  131.632 126.650 1.00 135.52 ? 510 LYS A CA  1 
ATOM   3890 C C   . LYS A 1 510 ? 74.748  131.223 125.278 1.00 135.47 ? 510 LYS A C   1 
ATOM   3891 O O   . LYS A 1 510 ? 74.188  130.129 125.151 1.00 136.20 ? 510 LYS A O   1 
ATOM   3892 C CB  . LYS A 1 510 ? 74.091  131.772 127.619 1.00 133.28 ? 510 LYS A CB  1 
ATOM   3893 C CG  . LYS A 1 510 ? 74.500  131.934 129.074 1.00 131.59 ? 510 LYS A CG  1 
ATOM   3894 C CD  . LYS A 1 510 ? 73.434  132.670 129.869 1.00 130.89 ? 510 LYS A CD  1 
ATOM   3895 C CE  . LYS A 1 510 ? 73.315  134.119 129.423 1.00 130.46 ? 510 LYS A CE  1 
ATOM   3896 N NZ  . LYS A 1 510 ? 72.267  134.851 130.186 1.00 131.17 ? 510 LYS A NZ  1 
ATOM   3897 N N   . LEU A 1 511 ? 74.912  132.065 124.256 1.00 135.32 ? 511 LEU A N   1 
ATOM   3898 C CA  . LEU A 1 511 ? 74.346  131.766 122.945 1.00 133.55 ? 511 LEU A CA  1 
ATOM   3899 C C   . LEU A 1 511 ? 75.134  130.690 122.207 1.00 133.09 ? 511 LEU A C   1 
ATOM   3900 O O   . LEU A 1 511 ? 74.570  129.998 121.352 1.00 133.79 ? 511 LEU A O   1 
ATOM   3901 C CB  . LEU A 1 511 ? 74.266  133.050 122.110 1.00 132.72 ? 511 LEU A CB  1 
ATOM   3902 C CG  . LEU A 1 511 ? 73.366  133.102 120.868 1.00 131.33 ? 511 LEU A CG  1 
ATOM   3903 C CD1 . LEU A 1 511 ? 72.817  134.505 120.689 1.00 130.82 ? 511 LEU A CD1 1 
ATOM   3904 C CD2 . LEU A 1 511 ? 74.112  132.688 119.607 1.00 129.65 ? 511 LEU A CD2 1 
ATOM   3905 N N   . ASP A 1 512 ? 76.417  130.530 122.521 1.00 131.88 ? 512 ASP A N   1 
ATOM   3906 C CA  . ASP A 1 512 ? 77.253  129.568 121.814 1.00 130.06 ? 512 ASP A CA  1 
ATOM   3907 C C   . ASP A 1 512 ? 76.811  128.137 122.103 1.00 130.39 ? 512 ASP A C   1 
ATOM   3908 O O   . ASP A 1 512 ? 76.424  127.799 123.225 1.00 131.12 ? 512 ASP A O   1 
ATOM   3909 C CB  . ASP A 1 512 ? 78.721  129.765 122.194 1.00 127.81 ? 512 ASP A CB  1 
ATOM   3910 C CG  . ASP A 1 512 ? 78.986  129.530 123.668 1.00 126.19 ? 512 ASP A CG  1 
ATOM   3911 O OD1 . ASP A 1 512 ? 78.054  129.699 124.480 1.00 123.95 ? 512 ASP A OD1 1 
ATOM   3912 O OD2 . ASP A 1 512 ? 80.133  129.185 124.017 1.00 124.88 ? 512 ASP A OD2 1 
ATOM   3913 N N   . VAL A 1 513 ? 76.853  127.298 121.073 1.00 129.98 ? 513 VAL A N   1 
ATOM   3914 C CA  . VAL A 1 513 ? 76.399  125.918 121.176 1.00 128.85 ? 513 VAL A CA  1 
ATOM   3915 C C   . VAL A 1 513 ? 77.562  124.947 121.342 1.00 127.44 ? 513 VAL A C   1 
ATOM   3916 O O   . VAL A 1 513 ? 77.458  123.982 122.100 1.00 129.71 ? 513 VAL A O   1 
ATOM   3917 C CB  . VAL A 1 513 ? 75.525  125.548 119.956 1.00 127.71 ? 513 VAL A CB  1 
ATOM   3918 C CG1 . VAL A 1 513 ? 74.166  126.218 120.065 1.00 126.71 ? 513 VAL A CG1 1 
ATOM   3919 C CG2 . VAL A 1 513 ? 76.203  125.962 118.659 1.00 127.16 ? 513 VAL A CG2 1 
ATOM   3920 N N   . PHE A 1 514 ? 78.677  125.180 120.647 1.00 122.96 ? 514 PHE A N   1 
ATOM   3921 C CA  . PHE A 1 514 ? 79.832  124.299 120.768 1.00 118.21 ? 514 PHE A CA  1 
ATOM   3922 C C   . PHE A 1 514 ? 80.597  124.507 122.067 1.00 119.17 ? 514 PHE A C   1 
ATOM   3923 O O   . PHE A 1 514 ? 81.280  123.580 122.518 1.00 116.95 ? 514 PHE A O   1 
ATOM   3924 C CB  . PHE A 1 514 ? 80.770  124.491 119.574 1.00 112.60 ? 514 PHE A CB  1 
ATOM   3925 C CG  . PHE A 1 514 ? 80.142  124.155 118.251 1.00 108.72 ? 514 PHE A CG  1 
ATOM   3926 C CD1 . PHE A 1 514 ? 80.113  122.847 117.798 1.00 106.51 ? 514 PHE A CD1 1 
ATOM   3927 C CD2 . PHE A 1 514 ? 79.581  125.145 117.463 1.00 107.75 ? 514 PHE A CD2 1 
ATOM   3928 C CE1 . PHE A 1 514 ? 79.536  122.533 116.581 1.00 106.79 ? 514 PHE A CE1 1 
ATOM   3929 C CE2 . PHE A 1 514 ? 79.003  124.838 116.246 1.00 107.70 ? 514 PHE A CE2 1 
ATOM   3930 C CZ  . PHE A 1 514 ? 78.980  123.530 115.805 1.00 107.65 ? 514 PHE A CZ  1 
ATOM   3931 N N   . ASP A 1 515 ? 80.510  125.701 122.660 1.00 122.15 ? 515 ASP A N   1 
ATOM   3932 C CA  . ASP A 1 515 ? 81.079  126.030 123.969 1.00 125.75 ? 515 ASP A CA  1 
ATOM   3933 C C   . ASP A 1 515 ? 82.599  125.859 124.003 1.00 126.55 ? 515 ASP A C   1 
ATOM   3934 O O   . ASP A 1 515 ? 83.183  125.632 125.066 1.00 130.51 ? 515 ASP A O   1 
ATOM   3935 C CB  . ASP A 1 515 ? 80.407  125.204 125.078 1.00 127.57 ? 515 ASP A CB  1 
ATOM   3936 C CG  . ASP A 1 515 ? 80.527  125.844 126.451 1.00 130.34 ? 515 ASP A CG  1 
ATOM   3937 O OD1 . ASP A 1 515 ? 79.733  126.760 126.751 1.00 133.06 ? 515 ASP A OD1 1 
ATOM   3938 O OD2 . ASP A 1 515 ? 81.398  125.418 127.238 1.00 131.04 ? 515 ASP A OD2 1 
ATOM   3939 N N   . ALA A 1 516 ? 83.259  125.961 122.848 1.00 124.32 ? 516 ALA A N   1 
ATOM   3940 C CA  . ALA A 1 516 ? 84.710  125.807 122.808 1.00 121.84 ? 516 ALA A CA  1 
ATOM   3941 C C   . ALA A 1 516 ? 85.429  127.040 123.345 1.00 120.15 ? 516 ALA A C   1 
ATOM   3942 O O   . ALA A 1 516 ? 86.399  126.913 124.100 1.00 121.40 ? 516 ALA A O   1 
ATOM   3943 C CB  . ALA A 1 516 ? 85.165  125.505 121.380 1.00 120.12 ? 516 ALA A CB  1 
ATOM   3944 N N   . VAL A 1 517 ? 84.974  128.236 122.963 1.00 116.06 ? 517 VAL A N   1 
ATOM   3945 C CA  . VAL A 1 517 ? 85.676  129.458 123.345 1.00 114.38 ? 517 VAL A CA  1 
ATOM   3946 C C   . VAL A 1 517 ? 85.505  129.742 124.833 1.00 113.59 ? 517 VAL A C   1 
ATOM   3947 O O   . VAL A 1 517 ? 86.470  130.088 125.527 1.00 111.05 ? 517 VAL A O   1 
ATOM   3948 C CB  . VAL A 1 517 ? 85.191  130.638 122.483 1.00 114.73 ? 517 VAL A CB  1 
ATOM   3949 C CG1 . VAL A 1 517 ? 85.758  131.951 123.000 1.00 114.75 ? 517 VAL A CG1 1 
ATOM   3950 C CG2 . VAL A 1 517 ? 85.576  130.423 121.032 1.00 114.68 ? 517 VAL A CG2 1 
ATOM   3951 N N   . VAL A 1 518 ? 84.279  129.604 125.345 1.00 115.43 ? 518 VAL A N   1 
ATOM   3952 C CA  . VAL A 1 518 ? 84.002  129.939 126.740 1.00 115.82 ? 518 VAL A CA  1 
ATOM   3953 C C   . VAL A 1 518 ? 84.730  128.982 127.678 1.00 116.79 ? 518 VAL A C   1 
ATOM   3954 O O   . VAL A 1 518 ? 85.360  129.403 128.656 1.00 118.93 ? 518 VAL A O   1 
ATOM   3955 C CB  . VAL A 1 518 ? 82.483  129.940 126.994 1.00 114.89 ? 518 VAL A CB  1 
ATOM   3956 C CG1 . VAL A 1 518 ? 82.183  130.035 128.483 1.00 113.54 ? 518 VAL A CG1 1 
ATOM   3957 C CG2 . VAL A 1 518 ? 81.822  131.081 126.237 1.00 113.93 ? 518 VAL A CG2 1 
ATOM   3958 N N   . ALA A 1 519 ? 84.671  127.687 127.387 1.00 114.30 ? 519 ALA A N   1 
ATOM   3959 C CA  . ALA A 1 519 ? 85.362  126.693 128.199 1.00 110.54 ? 519 ALA A CA  1 
ATOM   3960 C C   . ALA A 1 519 ? 86.606  126.177 127.484 1.00 108.65 ? 519 ALA A C   1 
ATOM   3961 O O   . ALA A 1 519 ? 87.581  126.907 127.309 1.00 107.39 ? 519 ALA A O   1 
ATOM   3962 C CB  . ALA A 1 519 ? 84.429  125.542 128.540 1.00 108.87 ? 519 ALA A CB  1 
HETATM 3963 C CAC . HC6 B 2 .   ? 97.381  107.639 97.871  1.00 43.10  ? 701 HC6 A CAC 1 
HETATM 3964 N NAA . HC6 B 2 .   ? 98.072  107.304 99.121  1.00 43.35  ? 701 HC6 A NAA 1 
HETATM 3965 C CBA . HC6 B 2 .   ? 97.136  107.223 100.242 1.00 43.64  ? 701 HC6 A CBA 1 
HETATM 3966 C CBB . HC6 B 2 .   ? 98.679  105.988 98.944  1.00 43.94  ? 701 HC6 A CBB 1 
HETATM 3967 C CAB . HC6 B 2 .   ? 99.141  108.247 99.433  1.00 42.85  ? 701 HC6 A CAB 1 
HETATM 3968 C CAF . HC6 B 2 .   ? 98.543  109.630 99.499  1.00 42.82  ? 701 HC6 A CAF 1 
HETATM 3969 O OAE . HC6 B 2 .   ? 98.132  109.938 98.183  1.00 43.13  ? 701 HC6 A OAE 1 
HETATM 3970 C CAD . HC6 B 2 .   ? 97.072  109.123 97.695  1.00 43.03  ? 701 HC6 A CAD 1 
HETATM 3971 O OBC . HC6 B 2 .   ? 95.848  109.454 98.342  1.00 43.73  ? 701 HC6 A OBC 1 
HETATM 3972 C CAG . HC6 B 2 .   ? 96.936  109.476 96.251  1.00 42.45  ? 701 HC6 A CAG 1 
HETATM 3973 C CAL . HC6 B 2 .   ? 96.220  110.608 95.910  1.00 42.58  ? 701 HC6 A CAL 1 
HETATM 3974 C CAK . HC6 B 2 .   ? 96.079  110.964 94.580  1.00 42.73  ? 701 HC6 A CAK 1 
HETATM 3975 C CAH . HC6 B 2 .   ? 97.521  108.698 95.266  1.00 41.90  ? 701 HC6 A CAH 1 
HETATM 3976 C CAI . HC6 B 2 .   ? 97.382  109.053 93.941  1.00 42.19  ? 701 HC6 A CAI 1 
HETATM 3977 C CAJ . HC6 B 2 .   ? 96.668  110.184 93.605  1.00 43.13  ? 701 HC6 A CAJ 1 
HETATM 3978 C CAM . HC6 B 2 .   ? 96.531  110.535 92.180  1.00 44.57  ? 701 HC6 A CAM 1 
HETATM 3979 C CAR . HC6 B 2 .   ? 97.263  109.812 91.256  1.00 45.07  ? 701 HC6 A CAR 1 
HETATM 3980 C CAQ . HC6 B 2 .   ? 97.151  110.114 89.911  1.00 46.05  ? 701 HC6 A CAQ 1 
HETATM 3981 C CAN . HC6 B 2 .   ? 95.683  111.555 91.777  1.00 45.68  ? 701 HC6 A CAN 1 
HETATM 3982 C CAO . HC6 B 2 .   ? 95.571  111.855 90.426  1.00 46.60  ? 701 HC6 A CAO 1 
HETATM 3983 C CAP . HC6 B 2 .   ? 96.308  111.133 89.497  1.00 48.05  ? 701 HC6 A CAP 1 
HETATM 3984 C CAS . HC6 B 2 .   ? 96.206  111.427 88.037  1.00 51.04  ? 701 HC6 A CAS 1 
HETATM 3985 O OBD . HC6 B 2 .   ? 97.406  112.054 87.577  1.00 51.96  ? 701 HC6 A OBD 1 
HETATM 3986 C CAX . HC6 B 2 .   ? 96.011  110.049 87.394  1.00 51.50  ? 701 HC6 A CAX 1 
HETATM 3987 O OAT . HC6 B 2 .   ? 95.079  112.279 87.842  1.00 52.86  ? 701 HC6 A OAT 1 
HETATM 3988 C CAU . HC6 B 2 .   ? 94.620  112.331 86.497  1.00 52.51  ? 701 HC6 A CAU 1 
HETATM 3989 C CAV . HC6 B 2 .   ? 94.184  110.934 86.080  1.00 51.98  ? 701 HC6 A CAV 1 
HETATM 3990 N NAW . HC6 B 2 .   ? 95.338  110.029 86.089  1.00 51.52  ? 701 HC6 A NAW 1 
HETATM 3991 C CAZ . HC6 B 2 .   ? 96.282  110.383 85.024  1.00 51.37  ? 701 HC6 A CAZ 1 
HETATM 3992 C CAY . HC6 B 2 .   ? 94.867  108.663 85.840  1.00 50.55  ? 701 HC6 A CAY 1 
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