data_9F0A
# 
_entry.id   9F0A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F0A         pdb_00009f0a 10.2210/pdb9f0a/pdb 
WWPDB D_1292137942 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F0A 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.mattevi@unipv.it 
_pdbx_contact_author.name_first         Andrea 
_pdbx_contact_author.name_last          Mattevi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9523-7128 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Barone, M.'  1 0000-0001-7184-2940 
'Mattevi, A.' 2 0000-0002-9523-7128 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'N5 Adduct of LSD1-CoREST in complex with MC4455' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Barone, M.'  1 0000-0001-7184-2940 
primary 'Mattevi, A.' 2 0000-0002-9523-7128 
# 
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 'Lysine-specific histone demethylase 1A' 81279.438 1 1.-.-.- ? ? ? 
2 polymer     man 'REST corepressor 1' 20244.824 1 ?       ? ? ? 
3 non-polymer syn 
;[[(2~{S},3~{R},4~{S},5~{S})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{S},3~{S},4~{R})-5-[5-[3-[4-[[4-[[(2~{S})-3-(3,4-dihydro-1~{H}-isoquinolin-2-yl)-2-oxidanyl-propyl]carbamoyl]pyridin-2-yl]amino]phenyl]propanoyl]-7,8-dimethyl-2,4-bis(oxidanylidene)-4~{a}~{H}-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate
;
1244.102  1 ?       ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'BRAF35-HDAC complex protein BHC110,Flavin-containing amine oxidase domain-containing protein 2' 
2 'Protein CoREST'                                                                                 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISG
PQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVI
IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPL
YEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELK
ELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLS
SRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEV
IAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVG
STTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYS
YVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATP
GVPAQQSPSM
;
;MDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISG
PQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVI
IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPL
YEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELK
ELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLS
SRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEV
IAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVG
STTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYS
YVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATP
GVPAQQSPSM
;
A ? 
2 'polypeptide(L)' no no 
;RAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWT
TEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKM
PEEEDEAPVLDVRYASAS
;
;RAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWT
TEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKM
PEEEDEAPVLDVRYASAS
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        
;[[(2~{S},3~{R},4~{S},5~{S})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{S},3~{S},4~{R})-5-[5-[3-[4-[[4-[[(2~{S})-3-(3,4-dihydro-1~{H}-isoquinolin-2-yl)-2-oxidanyl-propyl]carbamoyl]pyridin-2-yl]amino]phenyl]propanoyl]-7,8-dimethyl-2,4-bis(oxidanylidene)-4~{a}~{H}-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate
;
_pdbx_entity_nonpoly.comp_id     A1H8N 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLU n 
1 4   SER n 
1 5   LEU n 
1 6   ALA n 
1 7   ASN n 
1 8   LEU n 
1 9   SER n 
1 10  GLU n 
1 11  ASP n 
1 12  GLU n 
1 13  TYR n 
1 14  TYR n 
1 15  SER n 
1 16  GLU n 
1 17  GLU n 
1 18  GLU n 
1 19  ARG n 
1 20  ASN n 
1 21  ALA n 
1 22  LYS n 
1 23  ALA n 
1 24  GLU n 
1 25  LYS n 
1 26  GLU n 
1 27  LYS n 
1 28  LYS n 
1 29  LEU n 
1 30  PRO n 
1 31  PRO n 
1 32  PRO n 
1 33  PRO n 
1 34  PRO n 
1 35  GLN n 
1 36  ALA n 
1 37  PRO n 
1 38  PRO n 
1 39  GLU n 
1 40  GLU n 
1 41  GLU n 
1 42  ASN n 
1 43  GLU n 
1 44  SER n 
1 45  GLU n 
1 46  PRO n 
1 47  GLU n 
1 48  GLU n 
1 49  PRO n 
1 50  SER n 
1 51  GLY n 
1 52  VAL n 
1 53  GLU n 
1 54  GLY n 
1 55  ALA n 
1 56  ALA n 
1 57  PHE n 
1 58  GLN n 
1 59  SER n 
1 60  ARG n 
1 61  LEU n 
1 62  PRO n 
1 63  HIS n 
1 64  ASP n 
1 65  ARG n 
1 66  MET n 
1 67  THR n 
1 68  SER n 
1 69  GLN n 
1 70  GLU n 
1 71  ALA n 
1 72  ALA n 
1 73  CYS n 
1 74  PHE n 
1 75  PRO n 
1 76  ASP n 
1 77  ILE n 
1 78  ILE n 
1 79  SER n 
1 80  GLY n 
1 81  PRO n 
1 82  GLN n 
1 83  GLN n 
1 84  THR n 
1 85  GLN n 
1 86  LYS n 
1 87  VAL n 
1 88  PHE n 
1 89  LEU n 
1 90  PHE n 
1 91  ILE n 
1 92  ARG n 
1 93  ASN n 
1 94  ARG n 
1 95  THR n 
1 96  LEU n 
1 97  GLN n 
1 98  LEU n 
1 99  TRP n 
1 100 LEU n 
1 101 ASP n 
1 102 ASN n 
1 103 PRO n 
1 104 LYS n 
1 105 ILE n 
1 106 GLN n 
1 107 LEU n 
1 108 THR n 
1 109 PHE n 
1 110 GLU n 
1 111 ALA n 
1 112 THR n 
1 113 LEU n 
1 114 GLN n 
1 115 GLN n 
1 116 LEU n 
1 117 GLU n 
1 118 ALA n 
1 119 PRO n 
1 120 TYR n 
1 121 ASN n 
1 122 SER n 
1 123 ASP n 
1 124 THR n 
1 125 VAL n 
1 126 LEU n 
1 127 VAL n 
1 128 HIS n 
1 129 ARG n 
1 130 VAL n 
1 131 HIS n 
1 132 SER n 
1 133 TYR n 
1 134 LEU n 
1 135 GLU n 
1 136 ARG n 
1 137 HIS n 
1 138 GLY n 
1 139 LEU n 
1 140 ILE n 
1 141 ASN n 
1 142 PHE n 
1 143 GLY n 
1 144 ILE n 
1 145 TYR n 
1 146 LYS n 
1 147 ARG n 
1 148 ILE n 
1 149 LYS n 
1 150 PRO n 
1 151 LEU n 
1 152 PRO n 
1 153 THR n 
1 154 LYS n 
1 155 LYS n 
1 156 THR n 
1 157 GLY n 
1 158 LYS n 
1 159 VAL n 
1 160 ILE n 
1 161 ILE n 
1 162 ILE n 
1 163 GLY n 
1 164 SER n 
1 165 GLY n 
1 166 VAL n 
1 167 SER n 
1 168 GLY n 
1 169 LEU n 
1 170 ALA n 
1 171 ALA n 
1 172 ALA n 
1 173 ARG n 
1 174 GLN n 
1 175 LEU n 
1 176 GLN n 
1 177 SER n 
1 178 PHE n 
1 179 GLY n 
1 180 MET n 
1 181 ASP n 
1 182 VAL n 
1 183 THR n 
1 184 LEU n 
1 185 LEU n 
1 186 GLU n 
1 187 ALA n 
1 188 ARG n 
1 189 ASP n 
1 190 ARG n 
1 191 VAL n 
1 192 GLY n 
1 193 GLY n 
1 194 ARG n 
1 195 VAL n 
1 196 ALA n 
1 197 THR n 
1 198 PHE n 
1 199 ARG n 
1 200 LYS n 
1 201 GLY n 
1 202 ASN n 
1 203 TYR n 
1 204 VAL n 
1 205 ALA n 
1 206 ASP n 
1 207 LEU n 
1 208 GLY n 
1 209 ALA n 
1 210 MET n 
1 211 VAL n 
1 212 VAL n 
1 213 THR n 
1 214 GLY n 
1 215 LEU n 
1 216 GLY n 
1 217 GLY n 
1 218 ASN n 
1 219 PRO n 
1 220 MET n 
1 221 ALA n 
1 222 VAL n 
1 223 VAL n 
1 224 SER n 
1 225 LYS n 
1 226 GLN n 
1 227 VAL n 
1 228 ASN n 
1 229 MET n 
1 230 GLU n 
1 231 LEU n 
1 232 ALA n 
1 233 LYS n 
1 234 ILE n 
1 235 LYS n 
1 236 GLN n 
1 237 LYS n 
1 238 CYS n 
1 239 PRO n 
1 240 LEU n 
1 241 TYR n 
1 242 GLU n 
1 243 ALA n 
1 244 ASN n 
1 245 GLY n 
1 246 GLN n 
1 247 ALA n 
1 248 VAL n 
1 249 PRO n 
1 250 LYS n 
1 251 GLU n 
1 252 LYS n 
1 253 ASP n 
1 254 GLU n 
1 255 MET n 
1 256 VAL n 
1 257 GLU n 
1 258 GLN n 
1 259 GLU n 
1 260 PHE n 
1 261 ASN n 
1 262 ARG n 
1 263 LEU n 
1 264 LEU n 
1 265 GLU n 
1 266 ALA n 
1 267 THR n 
1 268 SER n 
1 269 TYR n 
1 270 LEU n 
1 271 SER n 
1 272 HIS n 
1 273 GLN n 
1 274 LEU n 
1 275 ASP n 
1 276 PHE n 
1 277 ASN n 
1 278 VAL n 
1 279 LEU n 
1 280 ASN n 
1 281 ASN n 
1 282 LYS n 
1 283 PRO n 
1 284 VAL n 
1 285 SER n 
1 286 LEU n 
1 287 GLY n 
1 288 GLN n 
1 289 ALA n 
1 290 LEU n 
1 291 GLU n 
1 292 VAL n 
1 293 VAL n 
1 294 ILE n 
1 295 GLN n 
1 296 LEU n 
1 297 GLN n 
1 298 GLU n 
1 299 LYS n 
1 300 HIS n 
1 301 VAL n 
1 302 LYS n 
1 303 ASP n 
1 304 GLU n 
1 305 GLN n 
1 306 ILE n 
1 307 GLU n 
1 308 HIS n 
1 309 TRP n 
1 310 LYS n 
1 311 LYS n 
1 312 ILE n 
1 313 VAL n 
1 314 LYS n 
1 315 THR n 
1 316 GLN n 
1 317 GLU n 
1 318 GLU n 
1 319 LEU n 
1 320 LYS n 
1 321 GLU n 
1 322 LEU n 
1 323 LEU n 
1 324 ASN n 
1 325 LYS n 
1 326 MET n 
1 327 VAL n 
1 328 ASN n 
1 329 LEU n 
1 330 LYS n 
1 331 GLU n 
1 332 LYS n 
1 333 ILE n 
1 334 LYS n 
1 335 GLU n 
1 336 LEU n 
1 337 HIS n 
1 338 GLN n 
1 339 GLN n 
1 340 TYR n 
1 341 LYS n 
1 342 GLU n 
1 343 ALA n 
1 344 SER n 
1 345 GLU n 
1 346 VAL n 
1 347 LYS n 
1 348 PRO n 
1 349 PRO n 
1 350 ARG n 
1 351 ASP n 
1 352 ILE n 
1 353 THR n 
1 354 ALA n 
1 355 GLU n 
1 356 PHE n 
1 357 LEU n 
1 358 VAL n 
1 359 LYS n 
1 360 SER n 
1 361 LYS n 
1 362 HIS n 
1 363 ARG n 
1 364 ASP n 
1 365 LEU n 
1 366 THR n 
1 367 ALA n 
1 368 LEU n 
1 369 CYS n 
1 370 LYS n 
1 371 GLU n 
1 372 TYR n 
1 373 ASP n 
1 374 GLU n 
1 375 LEU n 
1 376 ALA n 
1 377 GLU n 
1 378 THR n 
1 379 GLN n 
1 380 GLY n 
1 381 LYS n 
1 382 LEU n 
1 383 GLU n 
1 384 GLU n 
1 385 LYS n 
1 386 LEU n 
1 387 GLN n 
1 388 GLU n 
1 389 LEU n 
1 390 GLU n 
1 391 ALA n 
1 392 ASN n 
1 393 PRO n 
1 394 PRO n 
1 395 SER n 
1 396 ASP n 
1 397 VAL n 
1 398 TYR n 
1 399 LEU n 
1 400 SER n 
1 401 SER n 
1 402 ARG n 
1 403 ASP n 
1 404 ARG n 
1 405 GLN n 
1 406 ILE n 
1 407 LEU n 
1 408 ASP n 
1 409 TRP n 
1 410 HIS n 
1 411 PHE n 
1 412 ALA n 
1 413 ASN n 
1 414 LEU n 
1 415 GLU n 
1 416 PHE n 
1 417 ALA n 
1 418 ASN n 
1 419 ALA n 
1 420 THR n 
1 421 PRO n 
1 422 LEU n 
1 423 SER n 
1 424 THR n 
1 425 LEU n 
1 426 SER n 
1 427 LEU n 
1 428 LYS n 
1 429 HIS n 
1 430 TRP n 
1 431 ASP n 
1 432 GLN n 
1 433 ASP n 
1 434 ASP n 
1 435 ASP n 
1 436 PHE n 
1 437 GLU n 
1 438 PHE n 
1 439 THR n 
1 440 GLY n 
1 441 SER n 
1 442 HIS n 
1 443 LEU n 
1 444 THR n 
1 445 VAL n 
1 446 ARG n 
1 447 ASN n 
1 448 GLY n 
1 449 TYR n 
1 450 SER n 
1 451 CYS n 
1 452 VAL n 
1 453 PRO n 
1 454 VAL n 
1 455 ALA n 
1 456 LEU n 
1 457 ALA n 
1 458 GLU n 
1 459 GLY n 
1 460 LEU n 
1 461 ASP n 
1 462 ILE n 
1 463 LYS n 
1 464 LEU n 
1 465 ASN n 
1 466 THR n 
1 467 ALA n 
1 468 VAL n 
1 469 ARG n 
1 470 GLN n 
1 471 VAL n 
1 472 ARG n 
1 473 TYR n 
1 474 THR n 
1 475 ALA n 
1 476 SER n 
1 477 GLY n 
1 478 CYS n 
1 479 GLU n 
1 480 VAL n 
1 481 ILE n 
1 482 ALA n 
1 483 VAL n 
1 484 ASN n 
1 485 THR n 
1 486 ARG n 
1 487 SER n 
1 488 THR n 
1 489 SER n 
1 490 GLN n 
1 491 THR n 
1 492 PHE n 
1 493 ILE n 
1 494 TYR n 
1 495 LYS n 
1 496 CYS n 
1 497 ASP n 
1 498 ALA n 
1 499 VAL n 
1 500 LEU n 
1 501 CYS n 
1 502 THR n 
1 503 LEU n 
1 504 PRO n 
1 505 LEU n 
1 506 GLY n 
1 507 VAL n 
1 508 LEU n 
1 509 LYS n 
1 510 GLN n 
1 511 GLN n 
1 512 PRO n 
1 513 PRO n 
1 514 ALA n 
1 515 VAL n 
1 516 GLN n 
1 517 PHE n 
1 518 VAL n 
1 519 PRO n 
1 520 PRO n 
1 521 LEU n 
1 522 PRO n 
1 523 GLU n 
1 524 TRP n 
1 525 LYS n 
1 526 THR n 
1 527 SER n 
1 528 ALA n 
1 529 VAL n 
1 530 GLN n 
1 531 ARG n 
1 532 MET n 
1 533 GLY n 
1 534 PHE n 
1 535 GLY n 
1 536 ASN n 
1 537 LEU n 
1 538 ASN n 
1 539 LYS n 
1 540 VAL n 
1 541 VAL n 
1 542 LEU n 
1 543 CYS n 
1 544 PHE n 
1 545 ASP n 
1 546 ARG n 
1 547 VAL n 
1 548 PHE n 
1 549 TRP n 
1 550 ASP n 
1 551 PRO n 
1 552 SER n 
1 553 VAL n 
1 554 ASN n 
1 555 LEU n 
1 556 PHE n 
1 557 GLY n 
1 558 HIS n 
1 559 VAL n 
1 560 GLY n 
1 561 SER n 
1 562 THR n 
1 563 THR n 
1 564 ALA n 
1 565 SER n 
1 566 ARG n 
1 567 GLY n 
1 568 GLU n 
1 569 LEU n 
1 570 PHE n 
1 571 LEU n 
1 572 PHE n 
1 573 TRP n 
1 574 ASN n 
1 575 LEU n 
1 576 TYR n 
1 577 LYS n 
1 578 ALA n 
1 579 PRO n 
1 580 ILE n 
1 581 LEU n 
1 582 LEU n 
1 583 ALA n 
1 584 LEU n 
1 585 VAL n 
1 586 ALA n 
1 587 GLY n 
1 588 GLU n 
1 589 ALA n 
1 590 ALA n 
1 591 GLY n 
1 592 ILE n 
1 593 MET n 
1 594 GLU n 
1 595 ASN n 
1 596 ILE n 
1 597 SER n 
1 598 ASP n 
1 599 ASP n 
1 600 VAL n 
1 601 ILE n 
1 602 VAL n 
1 603 GLY n 
1 604 ARG n 
1 605 CYS n 
1 606 LEU n 
1 607 ALA n 
1 608 ILE n 
1 609 LEU n 
1 610 LYS n 
1 611 GLY n 
1 612 ILE n 
1 613 PHE n 
1 614 GLY n 
1 615 SER n 
1 616 SER n 
1 617 ALA n 
1 618 VAL n 
1 619 PRO n 
1 620 GLN n 
1 621 PRO n 
1 622 LYS n 
1 623 GLU n 
1 624 THR n 
1 625 VAL n 
1 626 VAL n 
1 627 SER n 
1 628 ARG n 
1 629 TRP n 
1 630 ARG n 
1 631 ALA n 
1 632 ASP n 
1 633 PRO n 
1 634 TRP n 
1 635 ALA n 
1 636 ARG n 
1 637 GLY n 
1 638 SER n 
1 639 TYR n 
1 640 SER n 
1 641 TYR n 
1 642 VAL n 
1 643 ALA n 
1 644 ALA n 
1 645 GLY n 
1 646 SER n 
1 647 SER n 
1 648 GLY n 
1 649 ASN n 
1 650 ASP n 
1 651 TYR n 
1 652 ASP n 
1 653 LEU n 
1 654 MET n 
1 655 ALA n 
1 656 GLN n 
1 657 PRO n 
1 658 ILE n 
1 659 THR n 
1 660 PRO n 
1 661 GLY n 
1 662 PRO n 
1 663 SER n 
1 664 ILE n 
1 665 PRO n 
1 666 GLY n 
1 667 ALA n 
1 668 PRO n 
1 669 GLN n 
1 670 PRO n 
1 671 ILE n 
1 672 PRO n 
1 673 ARG n 
1 674 LEU n 
1 675 PHE n 
1 676 PHE n 
1 677 ALA n 
1 678 GLY n 
1 679 GLU n 
1 680 HIS n 
1 681 THR n 
1 682 ILE n 
1 683 ARG n 
1 684 ASN n 
1 685 TYR n 
1 686 PRO n 
1 687 ALA n 
1 688 THR n 
1 689 VAL n 
1 690 HIS n 
1 691 GLY n 
1 692 ALA n 
1 693 LEU n 
1 694 LEU n 
1 695 SER n 
1 696 GLY n 
1 697 LEU n 
1 698 ARG n 
1 699 GLU n 
1 700 ALA n 
1 701 GLY n 
1 702 ARG n 
1 703 ILE n 
1 704 ALA n 
1 705 ASP n 
1 706 GLN n 
1 707 PHE n 
1 708 LEU n 
1 709 GLY n 
1 710 ALA n 
1 711 MET n 
1 712 TYR n 
1 713 THR n 
1 714 LEU n 
1 715 PRO n 
1 716 ARG n 
1 717 GLN n 
1 718 ALA n 
1 719 THR n 
1 720 PRO n 
1 721 GLY n 
1 722 VAL n 
1 723 PRO n 
1 724 ALA n 
1 725 GLN n 
1 726 GLN n 
1 727 SER n 
1 728 PRO n 
1 729 SER n 
1 730 MET n 
2 1   ARG n 
2 2   ALA n 
2 3   LYS n 
2 4   ARG n 
2 5   LYS n 
2 6   PRO n 
2 7   PRO n 
2 8   LYS n 
2 9   GLY n 
2 10  MET n 
2 11  PHE n 
2 12  LEU n 
2 13  SER n 
2 14  GLN n 
2 15  GLU n 
2 16  ASP n 
2 17  VAL n 
2 18  GLU n 
2 19  ALA n 
2 20  VAL n 
2 21  SER n 
2 22  ALA n 
2 23  ASN n 
2 24  ALA n 
2 25  THR n 
2 26  ALA n 
2 27  ALA n 
2 28  THR n 
2 29  THR n 
2 30  VAL n 
2 31  LEU n 
2 32  ARG n 
2 33  GLN n 
2 34  LEU n 
2 35  ASP n 
2 36  MET n 
2 37  GLU n 
2 38  LEU n 
2 39  VAL n 
2 40  SER n 
2 41  VAL n 
2 42  LYS n 
2 43  ARG n 
2 44  GLN n 
2 45  ILE n 
2 46  GLN n 
2 47  ASN n 
2 48  ILE n 
2 49  LYS n 
2 50  GLN n 
2 51  THR n 
2 52  ASN n 
2 53  SER n 
2 54  ALA n 
2 55  LEU n 
2 56  LYS n 
2 57  GLU n 
2 58  LYS n 
2 59  LEU n 
2 60  ASP n 
2 61  GLY n 
2 62  GLY n 
2 63  ILE n 
2 64  GLU n 
2 65  PRO n 
2 66  TYR n 
2 67  ARG n 
2 68  LEU n 
2 69  PRO n 
2 70  GLU n 
2 71  VAL n 
2 72  ILE n 
2 73  GLN n 
2 74  LYS n 
2 75  CYS n 
2 76  ASN n 
2 77  ALA n 
2 78  ARG n 
2 79  TRP n 
2 80  THR n 
2 81  THR n 
2 82  GLU n 
2 83  GLU n 
2 84  GLN n 
2 85  LEU n 
2 86  LEU n 
2 87  ALA n 
2 88  VAL n 
2 89  GLN n 
2 90  ALA n 
2 91  ILE n 
2 92  ARG n 
2 93  LYS n 
2 94  TYR n 
2 95  GLY n 
2 96  ARG n 
2 97  ASP n 
2 98  PHE n 
2 99  GLN n 
2 100 ALA n 
2 101 ILE n 
2 102 SER n 
2 103 ASP n 
2 104 VAL n 
2 105 ILE n 
2 106 GLY n 
2 107 ASN n 
2 108 LYS n 
2 109 SER n 
2 110 VAL n 
2 111 VAL n 
2 112 GLN n 
2 113 VAL n 
2 114 LYS n 
2 115 ASN n 
2 116 PHE n 
2 117 PHE n 
2 118 VAL n 
2 119 ASN n 
2 120 TYR n 
2 121 ARG n 
2 122 ARG n 
2 123 ARG n 
2 124 PHE n 
2 125 ASN n 
2 126 ILE n 
2 127 ASP n 
2 128 GLU n 
2 129 VAL n 
2 130 LEU n 
2 131 GLN n 
2 132 GLU n 
2 133 TRP n 
2 134 GLU n 
2 135 ALA n 
2 136 GLU n 
2 137 HIS n 
2 138 GLY n 
2 139 LYS n 
2 140 GLU n 
2 141 GLU n 
2 142 THR n 
2 143 ASN n 
2 144 GLY n 
2 145 PRO n 
2 146 SER n 
2 147 ASN n 
2 148 GLN n 
2 149 LYS n 
2 150 PRO n 
2 151 VAL n 
2 152 LYS n 
2 153 SER n 
2 154 PRO n 
2 155 ASP n 
2 156 ASN n 
2 157 SER n 
2 158 ILE n 
2 159 LYS n 
2 160 MET n 
2 161 PRO n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 ASP n 
2 166 GLU n 
2 167 ALA n 
2 168 PRO n 
2 169 VAL n 
2 170 LEU n 
2 171 ASP n 
2 172 VAL n 
2 173 ARG n 
2 174 TYR n 
2 175 ALA n 
2 176 SER n 
2 177 ALA n 
2 178 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 730 human ? 'KDM1A, AOF2, KDM1, KIAA0601, LSD1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 178 human ? 'RCOR1, KIAA0071, RCOR'             ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1H8N non-polymer         . 
;[[(2~{S},3~{R},4~{S},5~{S})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{S},3~{S},4~{R})-5-[5-[3-[4-[[4-[[(2~{S})-3-(3,4-dihydro-1~{H}-isoquinolin-2-yl)-2-oxidanyl-propyl]carbamoyl]pyridin-2-yl]amino]phenyl]propanoyl]-7,8-dimethyl-2,4-bis(oxidanylidene)-4~{a}~{H}-benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate
;
? 'C54 H63 N13 O18 P2' 1244.102 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'         89.093   
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'     175.209  
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'        132.118  
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103  
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'       121.158  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'       146.144  
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129  
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'         75.067   
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'     156.162  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'        131.173  
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'        131.173  
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'     147.195  
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'      149.211  
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'        165.189  
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'         115.130  
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'         105.093  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'         119.119  
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'      204.225  
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'        181.189  
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'        117.146  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   123 ?   ?   ?   A . n 
A 1 2   ASP 2   124 ?   ?   ?   A . n 
A 1 3   GLU 3   125 ?   ?   ?   A . n 
A 1 4   SER 4   126 ?   ?   ?   A . n 
A 1 5   LEU 5   127 ?   ?   ?   A . n 
A 1 6   ALA 6   128 ?   ?   ?   A . n 
A 1 7   ASN 7   129 ?   ?   ?   A . n 
A 1 8   LEU 8   130 ?   ?   ?   A . n 
A 1 9   SER 9   131 ?   ?   ?   A . n 
A 1 10  GLU 10  132 ?   ?   ?   A . n 
A 1 11  ASP 11  133 ?   ?   ?   A . n 
A 1 12  GLU 12  134 ?   ?   ?   A . n 
A 1 13  TYR 13  135 ?   ?   ?   A . n 
A 1 14  TYR 14  136 ?   ?   ?   A . n 
A 1 15  SER 15  137 ?   ?   ?   A . n 
A 1 16  GLU 16  138 ?   ?   ?   A . n 
A 1 17  GLU 17  139 ?   ?   ?   A . n 
A 1 18  GLU 18  140 ?   ?   ?   A . n 
A 1 19  ARG 19  141 ?   ?   ?   A . n 
A 1 20  ASN 20  142 ?   ?   ?   A . n 
A 1 21  ALA 21  143 ?   ?   ?   A . n 
A 1 22  LYS 22  144 ?   ?   ?   A . n 
A 1 23  ALA 23  145 ?   ?   ?   A . n 
A 1 24  GLU 24  146 ?   ?   ?   A . n 
A 1 25  LYS 25  147 ?   ?   ?   A . n 
A 1 26  GLU 26  148 ?   ?   ?   A . n 
A 1 27  LYS 27  149 ?   ?   ?   A . n 
A 1 28  LYS 28  150 ?   ?   ?   A . n 
A 1 29  LEU 29  151 ?   ?   ?   A . n 
A 1 30  PRO 30  152 ?   ?   ?   A . n 
A 1 31  PRO 31  153 ?   ?   ?   A . n 
A 1 32  PRO 32  154 ?   ?   ?   A . n 
A 1 33  PRO 33  155 ?   ?   ?   A . n 
A 1 34  PRO 34  156 ?   ?   ?   A . n 
A 1 35  GLN 35  157 ?   ?   ?   A . n 
A 1 36  ALA 36  158 ?   ?   ?   A . n 
A 1 37  PRO 37  159 ?   ?   ?   A . n 
A 1 38  PRO 38  160 ?   ?   ?   A . n 
A 1 39  GLU 39  161 ?   ?   ?   A . n 
A 1 40  GLU 40  162 ?   ?   ?   A . n 
A 1 41  GLU 41  163 ?   ?   ?   A . n 
A 1 42  ASN 42  164 ?   ?   ?   A . n 
A 1 43  GLU 43  165 ?   ?   ?   A . n 
A 1 44  SER 44  166 ?   ?   ?   A . n 
A 1 45  GLU 45  167 ?   ?   ?   A . n 
A 1 46  PRO 46  168 ?   ?   ?   A . n 
A 1 47  GLU 47  169 ?   ?   ?   A . n 
A 1 48  GLU 48  170 ?   ?   ?   A . n 
A 1 49  PRO 49  171 171 PRO PRO A . n 
A 1 50  SER 50  172 172 SER SER A . n 
A 1 51  GLY 51  173 173 GLY GLY A . n 
A 1 52  VAL 52  174 174 VAL VAL A . n 
A 1 53  GLU 53  175 175 GLU GLU A . n 
A 1 54  GLY 54  176 176 GLY GLY A . n 
A 1 55  ALA 55  177 177 ALA ALA A . n 
A 1 56  ALA 56  178 178 ALA ALA A . n 
A 1 57  PHE 57  179 179 PHE PHE A . n 
A 1 58  GLN 58  180 180 GLN GLN A . n 
A 1 59  SER 59  181 181 SER SER A . n 
A 1 60  ARG 60  182 182 ARG ARG A . n 
A 1 61  LEU 61  183 183 LEU LEU A . n 
A 1 62  PRO 62  184 184 PRO PRO A . n 
A 1 63  HIS 63  185 185 HIS HIS A . n 
A 1 64  ASP 64  186 186 ASP ASP A . n 
A 1 65  ARG 65  187 187 ARG ARG A . n 
A 1 66  MET 66  188 188 MET MET A . n 
A 1 67  THR 67  189 189 THR THR A . n 
A 1 68  SER 68  190 190 SER SER A . n 
A 1 69  GLN 69  191 191 GLN GLN A . n 
A 1 70  GLU 70  192 192 GLU GLU A . n 
A 1 71  ALA 71  193 193 ALA ALA A . n 
A 1 72  ALA 72  194 194 ALA ALA A . n 
A 1 73  CYS 73  195 195 CYS CYS A . n 
A 1 74  PHE 74  196 196 PHE PHE A . n 
A 1 75  PRO 75  197 197 PRO PRO A . n 
A 1 76  ASP 76  198 198 ASP ASP A . n 
A 1 77  ILE 77  199 199 ILE ILE A . n 
A 1 78  ILE 78  200 200 ILE ILE A . n 
A 1 79  SER 79  201 201 SER SER A . n 
A 1 80  GLY 80  202 202 GLY GLY A . n 
A 1 81  PRO 81  203 203 PRO PRO A . n 
A 1 82  GLN 82  204 204 GLN GLN A . n 
A 1 83  GLN 83  205 205 GLN GLN A . n 
A 1 84  THR 84  206 206 THR THR A . n 
A 1 85  GLN 85  207 207 GLN GLN A . n 
A 1 86  LYS 86  208 208 LYS LYS A . n 
A 1 87  VAL 87  209 209 VAL VAL A . n 
A 1 88  PHE 88  210 210 PHE PHE A . n 
A 1 89  LEU 89  211 211 LEU LEU A . n 
A 1 90  PHE 90  212 212 PHE PHE A . n 
A 1 91  ILE 91  213 213 ILE ILE A . n 
A 1 92  ARG 92  214 214 ARG ARG A . n 
A 1 93  ASN 93  215 215 ASN ASN A . n 
A 1 94  ARG 94  216 216 ARG ARG A . n 
A 1 95  THR 95  217 217 THR THR A . n 
A 1 96  LEU 96  218 218 LEU LEU A . n 
A 1 97  GLN 97  219 219 GLN GLN A . n 
A 1 98  LEU 98  220 220 LEU LEU A . n 
A 1 99  TRP 99  221 221 TRP TRP A . n 
A 1 100 LEU 100 222 222 LEU LEU A . n 
A 1 101 ASP 101 223 223 ASP ASP A . n 
A 1 102 ASN 102 224 224 ASN ASN A . n 
A 1 103 PRO 103 225 225 PRO PRO A . n 
A 1 104 LYS 104 226 226 LYS LYS A . n 
A 1 105 ILE 105 227 227 ILE ILE A . n 
A 1 106 GLN 106 228 228 GLN GLN A . n 
A 1 107 LEU 107 229 229 LEU LEU A . n 
A 1 108 THR 108 230 230 THR THR A . n 
A 1 109 PHE 109 231 231 PHE PHE A . n 
A 1 110 GLU 110 232 232 GLU GLU A . n 
A 1 111 ALA 111 233 233 ALA ALA A . n 
A 1 112 THR 112 234 234 THR THR A . n 
A 1 113 LEU 113 235 235 LEU LEU A . n 
A 1 114 GLN 114 236 236 GLN GLN A . n 
A 1 115 GLN 115 237 237 GLN GLN A . n 
A 1 116 LEU 116 238 238 LEU LEU A . n 
A 1 117 GLU 117 239 239 GLU GLU A . n 
A 1 118 ALA 118 240 240 ALA ALA A . n 
A 1 119 PRO 119 241 241 PRO PRO A . n 
A 1 120 TYR 120 242 242 TYR TYR A . n 
A 1 121 ASN 121 243 243 ASN ASN A . n 
A 1 122 SER 122 244 244 SER SER A . n 
A 1 123 ASP 123 245 245 ASP ASP A . n 
A 1 124 THR 124 246 246 THR THR A . n 
A 1 125 VAL 125 247 247 VAL VAL A . n 
A 1 126 LEU 126 248 248 LEU LEU A . n 
A 1 127 VAL 127 249 249 VAL VAL A . n 
A 1 128 HIS 128 250 250 HIS HIS A . n 
A 1 129 ARG 129 251 251 ARG ARG A . n 
A 1 130 VAL 130 252 252 VAL VAL A . n 
A 1 131 HIS 131 253 253 HIS HIS A . n 
A 1 132 SER 132 254 254 SER SER A . n 
A 1 133 TYR 133 255 255 TYR TYR A . n 
A 1 134 LEU 134 256 256 LEU LEU A . n 
A 1 135 GLU 135 257 257 GLU GLU A . n 
A 1 136 ARG 136 258 258 ARG ARG A . n 
A 1 137 HIS 137 259 259 HIS HIS A . n 
A 1 138 GLY 138 260 260 GLY GLY A . n 
A 1 139 LEU 139 261 261 LEU LEU A . n 
A 1 140 ILE 140 262 262 ILE ILE A . n 
A 1 141 ASN 141 263 263 ASN ASN A . n 
A 1 142 PHE 142 264 264 PHE PHE A . n 
A 1 143 GLY 143 265 265 GLY GLY A . n 
A 1 144 ILE 144 266 266 ILE ILE A . n 
A 1 145 TYR 145 267 267 TYR TYR A . n 
A 1 146 LYS 146 268 268 LYS LYS A . n 
A 1 147 ARG 147 269 269 ARG ARG A . n 
A 1 148 ILE 148 270 270 ILE ILE A . n 
A 1 149 LYS 149 271 271 LYS LYS A . n 
A 1 150 PRO 150 272 272 PRO PRO A . n 
A 1 151 LEU 151 273 273 LEU LEU A . n 
A 1 152 PRO 152 274 274 PRO PRO A . n 
A 1 153 THR 153 275 275 THR THR A . n 
A 1 154 LYS 154 276 276 LYS LYS A . n 
A 1 155 LYS 155 277 277 LYS LYS A . n 
A 1 156 THR 156 278 278 THR THR A . n 
A 1 157 GLY 157 279 279 GLY GLY A . n 
A 1 158 LYS 158 280 280 LYS LYS A . n 
A 1 159 VAL 159 281 281 VAL VAL A . n 
A 1 160 ILE 160 282 282 ILE ILE A . n 
A 1 161 ILE 161 283 283 ILE ILE A . n 
A 1 162 ILE 162 284 284 ILE ILE A . n 
A 1 163 GLY 163 285 285 GLY GLY A . n 
A 1 164 SER 164 286 286 SER SER A . n 
A 1 165 GLY 165 287 287 GLY GLY A . n 
A 1 166 VAL 166 288 288 VAL VAL A . n 
A 1 167 SER 167 289 289 SER SER A . n 
A 1 168 GLY 168 290 290 GLY GLY A . n 
A 1 169 LEU 169 291 291 LEU LEU A . n 
A 1 170 ALA 170 292 292 ALA ALA A . n 
A 1 171 ALA 171 293 293 ALA ALA A . n 
A 1 172 ALA 172 294 294 ALA ALA A . n 
A 1 173 ARG 173 295 295 ARG ARG A . n 
A 1 174 GLN 174 296 296 GLN GLN A . n 
A 1 175 LEU 175 297 297 LEU LEU A . n 
A 1 176 GLN 176 298 298 GLN GLN A . n 
A 1 177 SER 177 299 299 SER SER A . n 
A 1 178 PHE 178 300 300 PHE PHE A . n 
A 1 179 GLY 179 301 301 GLY GLY A . n 
A 1 180 MET 180 302 302 MET MET A . n 
A 1 181 ASP 181 303 303 ASP ASP A . n 
A 1 182 VAL 182 304 304 VAL VAL A . n 
A 1 183 THR 183 305 305 THR THR A . n 
A 1 184 LEU 184 306 306 LEU LEU A . n 
A 1 185 LEU 185 307 307 LEU LEU A . n 
A 1 186 GLU 186 308 308 GLU GLU A . n 
A 1 187 ALA 187 309 309 ALA ALA A . n 
A 1 188 ARG 188 310 310 ARG ARG A . n 
A 1 189 ASP 189 311 311 ASP ASP A . n 
A 1 190 ARG 190 312 312 ARG ARG A . n 
A 1 191 VAL 191 313 313 VAL VAL A . n 
A 1 192 GLY 192 314 314 GLY GLY A . n 
A 1 193 GLY 193 315 315 GLY GLY A . n 
A 1 194 ARG 194 316 316 ARG ARG A . n 
A 1 195 VAL 195 317 317 VAL VAL A . n 
A 1 196 ALA 196 318 318 ALA ALA A . n 
A 1 197 THR 197 319 319 THR THR A . n 
A 1 198 PHE 198 320 320 PHE PHE A . n 
A 1 199 ARG 199 321 321 ARG ARG A . n 
A 1 200 LYS 200 322 322 LYS LYS A . n 
A 1 201 GLY 201 323 323 GLY GLY A . n 
A 1 202 ASN 202 324 324 ASN ASN A . n 
A 1 203 TYR 203 325 325 TYR TYR A . n 
A 1 204 VAL 204 326 326 VAL VAL A . n 
A 1 205 ALA 205 327 327 ALA ALA A . n 
A 1 206 ASP 206 328 328 ASP ASP A . n 
A 1 207 LEU 207 329 329 LEU LEU A . n 
A 1 208 GLY 208 330 330 GLY GLY A . n 
A 1 209 ALA 209 331 331 ALA ALA A . n 
A 1 210 MET 210 332 332 MET MET A . n 
A 1 211 VAL 211 333 333 VAL VAL A . n 
A 1 212 VAL 212 334 334 VAL VAL A . n 
A 1 213 THR 213 335 335 THR THR A . n 
A 1 214 GLY 214 336 336 GLY GLY A . n 
A 1 215 LEU 215 337 337 LEU LEU A . n 
A 1 216 GLY 216 338 338 GLY GLY A . n 
A 1 217 GLY 217 339 339 GLY GLY A . n 
A 1 218 ASN 218 340 340 ASN ASN A . n 
A 1 219 PRO 219 341 341 PRO PRO A . n 
A 1 220 MET 220 342 342 MET MET A . n 
A 1 221 ALA 221 343 343 ALA ALA A . n 
A 1 222 VAL 222 344 344 VAL VAL A . n 
A 1 223 VAL 223 345 345 VAL VAL A . n 
A 1 224 SER 224 346 346 SER SER A . n 
A 1 225 LYS 225 347 347 LYS LYS A . n 
A 1 226 GLN 226 348 348 GLN GLN A . n 
A 1 227 VAL 227 349 349 VAL VAL A . n 
A 1 228 ASN 228 350 350 ASN ASN A . n 
A 1 229 MET 229 351 351 MET MET A . n 
A 1 230 GLU 230 352 352 GLU GLU A . n 
A 1 231 LEU 231 353 353 LEU LEU A . n 
A 1 232 ALA 232 354 354 ALA ALA A . n 
A 1 233 LYS 233 355 355 LYS LYS A . n 
A 1 234 ILE 234 356 356 ILE ILE A . n 
A 1 235 LYS 235 357 357 LYS LYS A . n 
A 1 236 GLN 236 358 358 GLN GLN A . n 
A 1 237 LYS 237 359 359 LYS LYS A . n 
A 1 238 CYS 238 360 360 CYS CYS A . n 
A 1 239 PRO 239 361 361 PRO PRO A . n 
A 1 240 LEU 240 362 362 LEU LEU A . n 
A 1 241 TYR 241 363 363 TYR TYR A . n 
A 1 242 GLU 242 364 364 GLU GLU A . n 
A 1 243 ALA 243 365 365 ALA ALA A . n 
A 1 244 ASN 244 366 366 ASN ASN A . n 
A 1 245 GLY 245 367 367 GLY GLY A . n 
A 1 246 GLN 246 368 368 GLN GLN A . n 
A 1 247 ALA 247 369 369 ALA ALA A . n 
A 1 248 VAL 248 370 370 VAL VAL A . n 
A 1 249 PRO 249 371 371 PRO PRO A . n 
A 1 250 LYS 250 372 372 LYS LYS A . n 
A 1 251 GLU 251 373 373 GLU GLU A . n 
A 1 252 LYS 252 374 374 LYS LYS A . n 
A 1 253 ASP 253 375 375 ASP ASP A . n 
A 1 254 GLU 254 376 376 GLU GLU A . n 
A 1 255 MET 255 377 377 MET MET A . n 
A 1 256 VAL 256 378 378 VAL VAL A . n 
A 1 257 GLU 257 379 379 GLU GLU A . n 
A 1 258 GLN 258 380 380 GLN GLN A . n 
A 1 259 GLU 259 381 381 GLU GLU A . n 
A 1 260 PHE 260 382 382 PHE PHE A . n 
A 1 261 ASN 261 383 383 ASN ASN A . n 
A 1 262 ARG 262 384 384 ARG ARG A . n 
A 1 263 LEU 263 385 385 LEU LEU A . n 
A 1 264 LEU 264 386 386 LEU LEU A . n 
A 1 265 GLU 265 387 387 GLU GLU A . n 
A 1 266 ALA 266 388 388 ALA ALA A . n 
A 1 267 THR 267 389 389 THR THR A . n 
A 1 268 SER 268 390 390 SER SER A . n 
A 1 269 TYR 269 391 391 TYR TYR A . n 
A 1 270 LEU 270 392 392 LEU LEU A . n 
A 1 271 SER 271 393 393 SER SER A . n 
A 1 272 HIS 272 394 394 HIS HIS A . n 
A 1 273 GLN 273 395 395 GLN GLN A . n 
A 1 274 LEU 274 396 396 LEU LEU A . n 
A 1 275 ASP 275 397 397 ASP ASP A . n 
A 1 276 PHE 276 398 398 PHE PHE A . n 
A 1 277 ASN 277 399 399 ASN ASN A . n 
A 1 278 VAL 278 400 400 VAL VAL A . n 
A 1 279 LEU 279 401 401 LEU LEU A . n 
A 1 280 ASN 280 402 402 ASN ASN A . n 
A 1 281 ASN 281 403 403 ASN ASN A . n 
A 1 282 LYS 282 404 404 LYS LYS A . n 
A 1 283 PRO 283 405 405 PRO PRO A . n 
A 1 284 VAL 284 406 406 VAL VAL A . n 
A 1 285 SER 285 407 407 SER SER A . n 
A 1 286 LEU 286 408 408 LEU LEU A . n 
A 1 287 GLY 287 409 409 GLY GLY A . n 
A 1 288 GLN 288 410 410 GLN GLN A . n 
A 1 289 ALA 289 411 411 ALA ALA A . n 
A 1 290 LEU 290 412 412 LEU LEU A . n 
A 1 291 GLU 291 413 413 GLU GLU A . n 
A 1 292 VAL 292 414 414 VAL VAL A . n 
A 1 293 VAL 293 415 415 VAL VAL A . n 
A 1 294 ILE 294 416 416 ILE ILE A . n 
A 1 295 GLN 295 417 417 GLN GLN A . n 
A 1 296 LEU 296 418 418 LEU LEU A . n 
A 1 297 GLN 297 419 419 GLN GLN A . n 
A 1 298 GLU 298 420 420 GLU GLU A . n 
A 1 299 LYS 299 421 421 LYS LYS A . n 
A 1 300 HIS 300 422 422 HIS HIS A . n 
A 1 301 VAL 301 423 423 VAL VAL A . n 
A 1 302 LYS 302 424 424 LYS LYS A . n 
A 1 303 ASP 303 425 425 ASP ASP A . n 
A 1 304 GLU 304 426 426 GLU GLU A . n 
A 1 305 GLN 305 427 427 GLN GLN A . n 
A 1 306 ILE 306 428 428 ILE ILE A . n 
A 1 307 GLU 307 429 429 GLU GLU A . n 
A 1 308 HIS 308 430 430 HIS HIS A . n 
A 1 309 TRP 309 431 431 TRP TRP A . n 
A 1 310 LYS 310 432 432 LYS LYS A . n 
A 1 311 LYS 311 433 433 LYS LYS A . n 
A 1 312 ILE 312 434 434 ILE ILE A . n 
A 1 313 VAL 313 435 435 VAL VAL A . n 
A 1 314 LYS 314 436 436 LYS LYS A . n 
A 1 315 THR 315 437 437 THR THR A . n 
A 1 316 GLN 316 438 438 GLN GLN A . n 
A 1 317 GLU 317 439 439 GLU GLU A . n 
A 1 318 GLU 318 440 440 GLU GLU A . n 
A 1 319 LEU 319 441 441 LEU LEU A . n 
A 1 320 LYS 320 442 442 LYS LYS A . n 
A 1 321 GLU 321 443 443 GLU GLU A . n 
A 1 322 LEU 322 444 444 LEU LEU A . n 
A 1 323 LEU 323 445 445 LEU LEU A . n 
A 1 324 ASN 324 446 446 ASN ASN A . n 
A 1 325 LYS 325 447 447 LYS LYS A . n 
A 1 326 MET 326 448 448 MET MET A . n 
A 1 327 VAL 327 449 449 VAL VAL A . n 
A 1 328 ASN 328 450 450 ASN ASN A . n 
A 1 329 LEU 329 451 451 LEU LEU A . n 
A 1 330 LYS 330 452 452 LYS LYS A . n 
A 1 331 GLU 331 453 453 GLU GLU A . n 
A 1 332 LYS 332 454 454 LYS LYS A . n 
A 1 333 ILE 333 455 455 ILE ILE A . n 
A 1 334 LYS 334 456 456 LYS LYS A . n 
A 1 335 GLU 335 457 457 GLU GLU A . n 
A 1 336 LEU 336 458 458 LEU LEU A . n 
A 1 337 HIS 337 459 459 HIS HIS A . n 
A 1 338 GLN 338 460 460 GLN GLN A . n 
A 1 339 GLN 339 461 461 GLN GLN A . n 
A 1 340 TYR 340 462 462 TYR TYR A . n 
A 1 341 LYS 341 463 463 LYS LYS A . n 
A 1 342 GLU 342 464 464 GLU GLU A . n 
A 1 343 ALA 343 465 465 ALA ALA A . n 
A 1 344 SER 344 466 466 SER SER A . n 
A 1 345 GLU 345 467 467 GLU GLU A . n 
A 1 346 VAL 346 468 468 VAL VAL A . n 
A 1 347 LYS 347 469 469 LYS LYS A . n 
A 1 348 PRO 348 470 470 PRO PRO A . n 
A 1 349 PRO 349 471 471 PRO PRO A . n 
A 1 350 ARG 350 472 472 ARG ARG A . n 
A 1 351 ASP 351 473 473 ASP ASP A . n 
A 1 352 ILE 352 474 474 ILE ILE A . n 
A 1 353 THR 353 475 475 THR THR A . n 
A 1 354 ALA 354 476 476 ALA ALA A . n 
A 1 355 GLU 355 477 477 GLU GLU A . n 
A 1 356 PHE 356 478 478 PHE PHE A . n 
A 1 357 LEU 357 479 479 LEU LEU A . n 
A 1 358 VAL 358 480 480 VAL VAL A . n 
A 1 359 LYS 359 481 481 LYS LYS A . n 
A 1 360 SER 360 482 482 SER SER A . n 
A 1 361 LYS 361 483 483 LYS LYS A . n 
A 1 362 HIS 362 484 484 HIS HIS A . n 
A 1 363 ARG 363 485 485 ARG ARG A . n 
A 1 364 ASP 364 486 486 ASP ASP A . n 
A 1 365 LEU 365 487 487 LEU LEU A . n 
A 1 366 THR 366 488 488 THR THR A . n 
A 1 367 ALA 367 489 489 ALA ALA A . n 
A 1 368 LEU 368 490 490 LEU LEU A . n 
A 1 369 CYS 369 491 491 CYS CYS A . n 
A 1 370 LYS 370 492 492 LYS LYS A . n 
A 1 371 GLU 371 493 493 GLU GLU A . n 
A 1 372 TYR 372 494 494 TYR TYR A . n 
A 1 373 ASP 373 495 495 ASP ASP A . n 
A 1 374 GLU 374 496 496 GLU GLU A . n 
A 1 375 LEU 375 497 497 LEU LEU A . n 
A 1 376 ALA 376 498 498 ALA ALA A . n 
A 1 377 GLU 377 499 499 GLU GLU A . n 
A 1 378 THR 378 500 500 THR THR A . n 
A 1 379 GLN 379 501 501 GLN GLN A . n 
A 1 380 GLY 380 502 502 GLY GLY A . n 
A 1 381 LYS 381 503 503 LYS LYS A . n 
A 1 382 LEU 382 504 504 LEU LEU A . n 
A 1 383 GLU 383 505 505 GLU GLU A . n 
A 1 384 GLU 384 506 506 GLU GLU A . n 
A 1 385 LYS 385 507 507 LYS LYS A . n 
A 1 386 LEU 386 508 508 LEU LEU A . n 
A 1 387 GLN 387 509 509 GLN GLN A . n 
A 1 388 GLU 388 510 510 GLU GLU A . n 
A 1 389 LEU 389 511 511 LEU LEU A . n 
A 1 390 GLU 390 512 512 GLU GLU A . n 
A 1 391 ALA 391 513 513 ALA ALA A . n 
A 1 392 ASN 392 514 514 ASN ASN A . n 
A 1 393 PRO 393 515 515 PRO PRO A . n 
A 1 394 PRO 394 516 516 PRO PRO A . n 
A 1 395 SER 395 517 517 SER SER A . n 
A 1 396 ASP 396 518 518 ASP ASP A . n 
A 1 397 VAL 397 519 519 VAL VAL A . n 
A 1 398 TYR 398 520 520 TYR TYR A . n 
A 1 399 LEU 399 521 521 LEU LEU A . n 
A 1 400 SER 400 522 522 SER SER A . n 
A 1 401 SER 401 523 523 SER SER A . n 
A 1 402 ARG 402 524 524 ARG ARG A . n 
A 1 403 ASP 403 525 525 ASP ASP A . n 
A 1 404 ARG 404 526 526 ARG ARG A . n 
A 1 405 GLN 405 527 527 GLN GLN A . n 
A 1 406 ILE 406 528 528 ILE ILE A . n 
A 1 407 LEU 407 529 529 LEU LEU A . n 
A 1 408 ASP 408 530 530 ASP ASP A . n 
A 1 409 TRP 409 531 531 TRP TRP A . n 
A 1 410 HIS 410 532 532 HIS HIS A . n 
A 1 411 PHE 411 533 533 PHE PHE A . n 
A 1 412 ALA 412 534 534 ALA ALA A . n 
A 1 413 ASN 413 535 535 ASN ASN A . n 
A 1 414 LEU 414 536 536 LEU LEU A . n 
A 1 415 GLU 415 537 537 GLU GLU A . n 
A 1 416 PHE 416 538 538 PHE PHE A . n 
A 1 417 ALA 417 539 539 ALA ALA A . n 
A 1 418 ASN 418 540 540 ASN ASN A . n 
A 1 419 ALA 419 541 541 ALA ALA A . n 
A 1 420 THR 420 542 542 THR THR A . n 
A 1 421 PRO 421 543 543 PRO PRO A . n 
A 1 422 LEU 422 544 544 LEU LEU A . n 
A 1 423 SER 423 545 545 SER SER A . n 
A 1 424 THR 424 546 546 THR THR A . n 
A 1 425 LEU 425 547 547 LEU LEU A . n 
A 1 426 SER 426 548 548 SER SER A . n 
A 1 427 LEU 427 549 549 LEU LEU A . n 
A 1 428 LYS 428 550 550 LYS LYS A . n 
A 1 429 HIS 429 551 551 HIS HIS A . n 
A 1 430 TRP 430 552 552 TRP TRP A . n 
A 1 431 ASP 431 553 553 ASP ASP A . n 
A 1 432 GLN 432 554 554 GLN GLN A . n 
A 1 433 ASP 433 555 555 ASP ASP A . n 
A 1 434 ASP 434 556 556 ASP ASP A . n 
A 1 435 ASP 435 557 557 ASP ASP A . n 
A 1 436 PHE 436 558 558 PHE PHE A . n 
A 1 437 GLU 437 559 559 GLU GLU A . n 
A 1 438 PHE 438 560 560 PHE PHE A . n 
A 1 439 THR 439 561 561 THR THR A . n 
A 1 440 GLY 440 562 562 GLY GLY A . n 
A 1 441 SER 441 563 563 SER SER A . n 
A 1 442 HIS 442 564 564 HIS HIS A . n 
A 1 443 LEU 443 565 565 LEU LEU A . n 
A 1 444 THR 444 566 566 THR THR A . n 
A 1 445 VAL 445 567 567 VAL VAL A . n 
A 1 446 ARG 446 568 568 ARG ARG A . n 
A 1 447 ASN 447 569 569 ASN ASN A . n 
A 1 448 GLY 448 570 570 GLY GLY A . n 
A 1 449 TYR 449 571 571 TYR TYR A . n 
A 1 450 SER 450 572 572 SER SER A . n 
A 1 451 CYS 451 573 573 CYS CYS A . n 
A 1 452 VAL 452 574 574 VAL VAL A . n 
A 1 453 PRO 453 575 575 PRO PRO A . n 
A 1 454 VAL 454 576 576 VAL VAL A . n 
A 1 455 ALA 455 577 577 ALA ALA A . n 
A 1 456 LEU 456 578 578 LEU LEU A . n 
A 1 457 ALA 457 579 579 ALA ALA A . n 
A 1 458 GLU 458 580 580 GLU GLU A . n 
A 1 459 GLY 459 581 581 GLY GLY A . n 
A 1 460 LEU 460 582 582 LEU LEU A . n 
A 1 461 ASP 461 583 583 ASP ASP A . n 
A 1 462 ILE 462 584 584 ILE ILE A . n 
A 1 463 LYS 463 585 585 LYS LYS A . n 
A 1 464 LEU 464 586 586 LEU LEU A . n 
A 1 465 ASN 465 587 587 ASN ASN A . n 
A 1 466 THR 466 588 588 THR THR A . n 
A 1 467 ALA 467 589 589 ALA ALA A . n 
A 1 468 VAL 468 590 590 VAL VAL A . n 
A 1 469 ARG 469 591 591 ARG ARG A . n 
A 1 470 GLN 470 592 592 GLN GLN A . n 
A 1 471 VAL 471 593 593 VAL VAL A . n 
A 1 472 ARG 472 594 594 ARG ARG A . n 
A 1 473 TYR 473 595 595 TYR TYR A . n 
A 1 474 THR 474 596 596 THR THR A . n 
A 1 475 ALA 475 597 597 ALA ALA A . n 
A 1 476 SER 476 598 598 SER SER A . n 
A 1 477 GLY 477 599 599 GLY GLY A . n 
A 1 478 CYS 478 600 600 CYS CYS A . n 
A 1 479 GLU 479 601 601 GLU GLU A . n 
A 1 480 VAL 480 602 602 VAL VAL A . n 
A 1 481 ILE 481 603 603 ILE ILE A . n 
A 1 482 ALA 482 604 604 ALA ALA A . n 
A 1 483 VAL 483 605 605 VAL VAL A . n 
A 1 484 ASN 484 606 606 ASN ASN A . n 
A 1 485 THR 485 607 607 THR THR A . n 
A 1 486 ARG 486 608 608 ARG ARG A . n 
A 1 487 SER 487 609 609 SER SER A . n 
A 1 488 THR 488 610 610 THR THR A . n 
A 1 489 SER 489 611 611 SER SER A . n 
A 1 490 GLN 490 612 612 GLN GLN A . n 
A 1 491 THR 491 613 613 THR THR A . n 
A 1 492 PHE 492 614 614 PHE PHE A . n 
A 1 493 ILE 493 615 615 ILE ILE A . n 
A 1 494 TYR 494 616 616 TYR TYR A . n 
A 1 495 LYS 495 617 617 LYS LYS A . n 
A 1 496 CYS 496 618 618 CYS CYS A . n 
A 1 497 ASP 497 619 619 ASP ASP A . n 
A 1 498 ALA 498 620 620 ALA ALA A . n 
A 1 499 VAL 499 621 621 VAL VAL A . n 
A 1 500 LEU 500 622 622 LEU LEU A . n 
A 1 501 CYS 501 623 623 CYS CYS A . n 
A 1 502 THR 502 624 624 THR THR A . n 
A 1 503 LEU 503 625 625 LEU LEU A . n 
A 1 504 PRO 504 626 626 PRO PRO A . n 
A 1 505 LEU 505 627 627 LEU LEU A . n 
A 1 506 GLY 506 628 628 GLY GLY A . n 
A 1 507 VAL 507 629 629 VAL VAL A . n 
A 1 508 LEU 508 630 630 LEU LEU A . n 
A 1 509 LYS 509 631 631 LYS LYS A . n 
A 1 510 GLN 510 632 632 GLN GLN A . n 
A 1 511 GLN 511 633 633 GLN GLN A . n 
A 1 512 PRO 512 634 634 PRO PRO A . n 
A 1 513 PRO 513 635 635 PRO PRO A . n 
A 1 514 ALA 514 636 636 ALA ALA A . n 
A 1 515 VAL 515 637 637 VAL VAL A . n 
A 1 516 GLN 516 638 638 GLN GLN A . n 
A 1 517 PHE 517 639 639 PHE PHE A . n 
A 1 518 VAL 518 640 640 VAL VAL A . n 
A 1 519 PRO 519 641 641 PRO PRO A . n 
A 1 520 PRO 520 642 642 PRO PRO A . n 
A 1 521 LEU 521 643 643 LEU LEU A . n 
A 1 522 PRO 522 644 644 PRO PRO A . n 
A 1 523 GLU 523 645 645 GLU GLU A . n 
A 1 524 TRP 524 646 646 TRP TRP A . n 
A 1 525 LYS 525 647 647 LYS LYS A . n 
A 1 526 THR 526 648 648 THR THR A . n 
A 1 527 SER 527 649 649 SER SER A . n 
A 1 528 ALA 528 650 650 ALA ALA A . n 
A 1 529 VAL 529 651 651 VAL VAL A . n 
A 1 530 GLN 530 652 652 GLN GLN A . n 
A 1 531 ARG 531 653 653 ARG ARG A . n 
A 1 532 MET 532 654 654 MET MET A . n 
A 1 533 GLY 533 655 655 GLY GLY A . n 
A 1 534 PHE 534 656 656 PHE PHE A . n 
A 1 535 GLY 535 657 657 GLY GLY A . n 
A 1 536 ASN 536 658 658 ASN ASN A . n 
A 1 537 LEU 537 659 659 LEU LEU A . n 
A 1 538 ASN 538 660 660 ASN ASN A . n 
A 1 539 LYS 539 661 661 LYS LYS A . n 
A 1 540 VAL 540 662 662 VAL VAL A . n 
A 1 541 VAL 541 663 663 VAL VAL A . n 
A 1 542 LEU 542 664 664 LEU LEU A . n 
A 1 543 CYS 543 665 665 CYS CYS A . n 
A 1 544 PHE 544 666 666 PHE PHE A . n 
A 1 545 ASP 545 667 667 ASP ASP A . n 
A 1 546 ARG 546 668 668 ARG ARG A . n 
A 1 547 VAL 547 669 669 VAL VAL A . n 
A 1 548 PHE 548 670 670 PHE PHE A . n 
A 1 549 TRP 549 671 671 TRP TRP A . n 
A 1 550 ASP 550 672 672 ASP ASP A . n 
A 1 551 PRO 551 673 673 PRO PRO A . n 
A 1 552 SER 552 674 674 SER SER A . n 
A 1 553 VAL 553 675 675 VAL VAL A . n 
A 1 554 ASN 554 676 676 ASN ASN A . n 
A 1 555 LEU 555 677 677 LEU LEU A . n 
A 1 556 PHE 556 678 678 PHE PHE A . n 
A 1 557 GLY 557 679 679 GLY GLY A . n 
A 1 558 HIS 558 680 680 HIS HIS A . n 
A 1 559 VAL 559 681 681 VAL VAL A . n 
A 1 560 GLY 560 682 682 GLY GLY A . n 
A 1 561 SER 561 683 683 SER SER A . n 
A 1 562 THR 562 684 684 THR THR A . n 
A 1 563 THR 563 685 685 THR THR A . n 
A 1 564 ALA 564 686 686 ALA ALA A . n 
A 1 565 SER 565 687 687 SER SER A . n 
A 1 566 ARG 566 688 688 ARG ARG A . n 
A 1 567 GLY 567 689 689 GLY GLY A . n 
A 1 568 GLU 568 690 690 GLU GLU A . n 
A 1 569 LEU 569 691 691 LEU LEU A . n 
A 1 570 PHE 570 692 692 PHE PHE A . n 
A 1 571 LEU 571 693 693 LEU LEU A . n 
A 1 572 PHE 572 694 694 PHE PHE A . n 
A 1 573 TRP 573 695 695 TRP TRP A . n 
A 1 574 ASN 574 696 696 ASN ASN A . n 
A 1 575 LEU 575 697 697 LEU LEU A . n 
A 1 576 TYR 576 698 698 TYR TYR A . n 
A 1 577 LYS 577 699 699 LYS LYS A . n 
A 1 578 ALA 578 700 700 ALA ALA A . n 
A 1 579 PRO 579 701 701 PRO PRO A . n 
A 1 580 ILE 580 702 702 ILE ILE A . n 
A 1 581 LEU 581 703 703 LEU LEU A . n 
A 1 582 LEU 582 704 704 LEU LEU A . n 
A 1 583 ALA 583 705 705 ALA ALA A . n 
A 1 584 LEU 584 706 706 LEU LEU A . n 
A 1 585 VAL 585 707 707 VAL VAL A . n 
A 1 586 ALA 586 708 708 ALA ALA A . n 
A 1 587 GLY 587 709 709 GLY GLY A . n 
A 1 588 GLU 588 710 710 GLU GLU A . n 
A 1 589 ALA 589 711 711 ALA ALA A . n 
A 1 590 ALA 590 712 712 ALA ALA A . n 
A 1 591 GLY 591 713 713 GLY GLY A . n 
A 1 592 ILE 592 714 714 ILE ILE A . n 
A 1 593 MET 593 715 715 MET MET A . n 
A 1 594 GLU 594 716 716 GLU GLU A . n 
A 1 595 ASN 595 717 717 ASN ASN A . n 
A 1 596 ILE 596 718 718 ILE ILE A . n 
A 1 597 SER 597 719 719 SER SER A . n 
A 1 598 ASP 598 720 720 ASP ASP A . n 
A 1 599 ASP 599 721 721 ASP ASP A . n 
A 1 600 VAL 600 722 722 VAL VAL A . n 
A 1 601 ILE 601 723 723 ILE ILE A . n 
A 1 602 VAL 602 724 724 VAL VAL A . n 
A 1 603 GLY 603 725 725 GLY GLY A . n 
A 1 604 ARG 604 726 726 ARG ARG A . n 
A 1 605 CYS 605 727 727 CYS CYS A . n 
A 1 606 LEU 606 728 728 LEU LEU A . n 
A 1 607 ALA 607 729 729 ALA ALA A . n 
A 1 608 ILE 608 730 730 ILE ILE A . n 
A 1 609 LEU 609 731 731 LEU LEU A . n 
A 1 610 LYS 610 732 732 LYS LYS A . n 
A 1 611 GLY 611 733 733 GLY GLY A . n 
A 1 612 ILE 612 734 734 ILE ILE A . n 
A 1 613 PHE 613 735 735 PHE PHE A . n 
A 1 614 GLY 614 736 736 GLY GLY A . n 
A 1 615 SER 615 737 737 SER SER A . n 
A 1 616 SER 616 738 738 SER SER A . n 
A 1 617 ALA 617 739 739 ALA ALA A . n 
A 1 618 VAL 618 740 740 VAL VAL A . n 
A 1 619 PRO 619 741 741 PRO PRO A . n 
A 1 620 GLN 620 742 742 GLN GLN A . n 
A 1 621 PRO 621 743 743 PRO PRO A . n 
A 1 622 LYS 622 744 744 LYS LYS A . n 
A 1 623 GLU 623 745 745 GLU GLU A . n 
A 1 624 THR 624 746 746 THR THR A . n 
A 1 625 VAL 625 747 747 VAL VAL A . n 
A 1 626 VAL 626 748 748 VAL VAL A . n 
A 1 627 SER 627 749 749 SER SER A . n 
A 1 628 ARG 628 750 750 ARG ARG A . n 
A 1 629 TRP 629 751 751 TRP TRP A . n 
A 1 630 ARG 630 752 752 ARG ARG A . n 
A 1 631 ALA 631 753 753 ALA ALA A . n 
A 1 632 ASP 632 754 754 ASP ASP A . n 
A 1 633 PRO 633 755 755 PRO PRO A . n 
A 1 634 TRP 634 756 756 TRP TRP A . n 
A 1 635 ALA 635 757 757 ALA ALA A . n 
A 1 636 ARG 636 758 758 ARG ARG A . n 
A 1 637 GLY 637 759 759 GLY GLY A . n 
A 1 638 SER 638 760 760 SER SER A . n 
A 1 639 TYR 639 761 761 TYR TYR A . n 
A 1 640 SER 640 762 762 SER SER A . n 
A 1 641 TYR 641 763 763 TYR TYR A . n 
A 1 642 VAL 642 764 764 VAL VAL A . n 
A 1 643 ALA 643 765 765 ALA ALA A . n 
A 1 644 ALA 644 766 766 ALA ALA A . n 
A 1 645 GLY 645 767 767 GLY GLY A . n 
A 1 646 SER 646 768 768 SER SER A . n 
A 1 647 SER 647 769 769 SER SER A . n 
A 1 648 GLY 648 770 770 GLY GLY A . n 
A 1 649 ASN 649 771 771 ASN ASN A . n 
A 1 650 ASP 650 772 772 ASP ASP A . n 
A 1 651 TYR 651 773 773 TYR TYR A . n 
A 1 652 ASP 652 774 774 ASP ASP A . n 
A 1 653 LEU 653 775 775 LEU LEU A . n 
A 1 654 MET 654 776 776 MET MET A . n 
A 1 655 ALA 655 777 777 ALA ALA A . n 
A 1 656 GLN 656 778 778 GLN GLN A . n 
A 1 657 PRO 657 779 779 PRO PRO A . n 
A 1 658 ILE 658 780 780 ILE ILE A . n 
A 1 659 THR 659 781 781 THR THR A . n 
A 1 660 PRO 660 782 782 PRO PRO A . n 
A 1 661 GLY 661 783 783 GLY GLY A . n 
A 1 662 PRO 662 784 784 PRO PRO A . n 
A 1 663 SER 663 785 785 SER SER A . n 
A 1 664 ILE 664 786 786 ILE ILE A . n 
A 1 665 PRO 665 787 787 PRO PRO A . n 
A 1 666 GLY 666 788 788 GLY GLY A . n 
A 1 667 ALA 667 789 789 ALA ALA A . n 
A 1 668 PRO 668 790 790 PRO PRO A . n 
A 1 669 GLN 669 791 791 GLN GLN A . n 
A 1 670 PRO 670 792 792 PRO PRO A . n 
A 1 671 ILE 671 793 793 ILE ILE A . n 
A 1 672 PRO 672 794 794 PRO PRO A . n 
A 1 673 ARG 673 795 795 ARG ARG A . n 
A 1 674 LEU 674 796 796 LEU LEU A . n 
A 1 675 PHE 675 797 797 PHE PHE A . n 
A 1 676 PHE 676 798 798 PHE PHE A . n 
A 1 677 ALA 677 799 799 ALA ALA A . n 
A 1 678 GLY 678 800 800 GLY GLY A . n 
A 1 679 GLU 679 801 801 GLU GLU A . n 
A 1 680 HIS 680 802 802 HIS HIS A . n 
A 1 681 THR 681 803 803 THR THR A . n 
A 1 682 ILE 682 804 804 ILE ILE A . n 
A 1 683 ARG 683 805 805 ARG ARG A . n 
A 1 684 ASN 684 806 806 ASN ASN A . n 
A 1 685 TYR 685 807 807 TYR TYR A . n 
A 1 686 PRO 686 808 808 PRO PRO A . n 
A 1 687 ALA 687 809 809 ALA ALA A . n 
A 1 688 THR 688 810 810 THR THR A . n 
A 1 689 VAL 689 811 811 VAL VAL A . n 
A 1 690 HIS 690 812 812 HIS HIS A . n 
A 1 691 GLY 691 813 813 GLY GLY A . n 
A 1 692 ALA 692 814 814 ALA ALA A . n 
A 1 693 LEU 693 815 815 LEU LEU A . n 
A 1 694 LEU 694 816 816 LEU LEU A . n 
A 1 695 SER 695 817 817 SER SER A . n 
A 1 696 GLY 696 818 818 GLY GLY A . n 
A 1 697 LEU 697 819 819 LEU LEU A . n 
A 1 698 ARG 698 820 820 ARG ARG A . n 
A 1 699 GLU 699 821 821 GLU GLU A . n 
A 1 700 ALA 700 822 822 ALA ALA A . n 
A 1 701 GLY 701 823 823 GLY GLY A . n 
A 1 702 ARG 702 824 824 ARG ARG A . n 
A 1 703 ILE 703 825 825 ILE ILE A . n 
A 1 704 ALA 704 826 826 ALA ALA A . n 
A 1 705 ASP 705 827 827 ASP ASP A . n 
A 1 706 GLN 706 828 828 GLN GLN A . n 
A 1 707 PHE 707 829 829 PHE PHE A . n 
A 1 708 LEU 708 830 830 LEU LEU A . n 
A 1 709 GLY 709 831 831 GLY GLY A . n 
A 1 710 ALA 710 832 832 ALA ALA A . n 
A 1 711 MET 711 833 833 MET MET A . n 
A 1 712 TYR 712 834 834 TYR TYR A . n 
A 1 713 THR 713 835 835 THR THR A . n 
A 1 714 LEU 714 836 836 LEU LEU A . n 
A 1 715 PRO 715 837 ?   ?   ?   A . n 
A 1 716 ARG 716 838 ?   ?   ?   A . n 
A 1 717 GLN 717 839 ?   ?   ?   A . n 
A 1 718 ALA 718 840 ?   ?   ?   A . n 
A 1 719 THR 719 841 ?   ?   ?   A . n 
A 1 720 PRO 720 842 ?   ?   ?   A . n 
A 1 721 GLY 721 843 ?   ?   ?   A . n 
A 1 722 VAL 722 844 ?   ?   ?   A . n 
A 1 723 PRO 723 845 ?   ?   ?   A . n 
A 1 724 ALA 724 846 ?   ?   ?   A . n 
A 1 725 GLN 725 847 ?   ?   ?   A . n 
A 1 726 GLN 726 848 ?   ?   ?   A . n 
A 1 727 SER 727 849 ?   ?   ?   A . n 
A 1 728 PRO 728 850 ?   ?   ?   A . n 
A 1 729 SER 729 851 ?   ?   ?   A . n 
A 1 730 MET 730 852 ?   ?   ?   A . n 
B 2 1   ARG 1   305 ?   ?   ?   B . n 
B 2 2   ALA 2   306 ?   ?   ?   B . n 
B 2 3   LYS 3   307 ?   ?   ?   B . n 
B 2 4   ARG 4   308 308 ARG ARG B . n 
B 2 5   LYS 5   309 309 LYS LYS B . n 
B 2 6   PRO 6   310 310 PRO PRO B . n 
B 2 7   PRO 7   311 311 PRO PRO B . n 
B 2 8   LYS 8   312 312 LYS LYS B . n 
B 2 9   GLY 9   313 313 GLY GLY B . n 
B 2 10  MET 10  314 314 MET MET B . n 
B 2 11  PHE 11  315 315 PHE PHE B . n 
B 2 12  LEU 12  316 316 LEU LEU B . n 
B 2 13  SER 13  317 317 SER SER B . n 
B 2 14  GLN 14  318 318 GLN GLN B . n 
B 2 15  GLU 15  319 319 GLU GLU B . n 
B 2 16  ASP 16  320 320 ASP ASP B . n 
B 2 17  VAL 17  321 321 VAL VAL B . n 
B 2 18  GLU 18  322 322 GLU GLU B . n 
B 2 19  ALA 19  323 323 ALA ALA B . n 
B 2 20  VAL 20  324 324 VAL VAL B . n 
B 2 21  SER 21  325 325 SER SER B . n 
B 2 22  ALA 22  326 326 ALA ALA B . n 
B 2 23  ASN 23  327 327 ASN ASN B . n 
B 2 24  ALA 24  328 328 ALA ALA B . n 
B 2 25  THR 25  329 329 THR THR B . n 
B 2 26  ALA 26  330 330 ALA ALA B . n 
B 2 27  ALA 27  331 331 ALA ALA B . n 
B 2 28  THR 28  332 332 THR THR B . n 
B 2 29  THR 29  333 333 THR THR B . n 
B 2 30  VAL 30  334 334 VAL VAL B . n 
B 2 31  LEU 31  335 335 LEU LEU B . n 
B 2 32  ARG 32  336 336 ARG ARG B . n 
B 2 33  GLN 33  337 337 GLN GLN B . n 
B 2 34  LEU 34  338 338 LEU LEU B . n 
B 2 35  ASP 35  339 339 ASP ASP B . n 
B 2 36  MET 36  340 340 MET MET B . n 
B 2 37  GLU 37  341 341 GLU GLU B . n 
B 2 38  LEU 38  342 342 LEU LEU B . n 
B 2 39  VAL 39  343 343 VAL VAL B . n 
B 2 40  SER 40  344 344 SER SER B . n 
B 2 41  VAL 41  345 345 VAL VAL B . n 
B 2 42  LYS 42  346 346 LYS LYS B . n 
B 2 43  ARG 43  347 347 ARG ARG B . n 
B 2 44  GLN 44  348 348 GLN GLN B . n 
B 2 45  ILE 45  349 349 ILE ILE B . n 
B 2 46  GLN 46  350 350 GLN GLN B . n 
B 2 47  ASN 47  351 351 ASN ASN B . n 
B 2 48  ILE 48  352 352 ILE ILE B . n 
B 2 49  LYS 49  353 353 LYS LYS B . n 
B 2 50  GLN 50  354 354 GLN GLN B . n 
B 2 51  THR 51  355 355 THR THR B . n 
B 2 52  ASN 52  356 356 ASN ASN B . n 
B 2 53  SER 53  357 357 SER SER B . n 
B 2 54  ALA 54  358 358 ALA ALA B . n 
B 2 55  LEU 55  359 359 LEU LEU B . n 
B 2 56  LYS 56  360 360 LYS LYS B . n 
B 2 57  GLU 57  361 361 GLU GLU B . n 
B 2 58  LYS 58  362 362 LYS LYS B . n 
B 2 59  LEU 59  363 363 LEU LEU B . n 
B 2 60  ASP 60  364 364 ASP ASP B . n 
B 2 61  GLY 61  365 365 GLY GLY B . n 
B 2 62  GLY 62  366 366 GLY GLY B . n 
B 2 63  ILE 63  367 367 ILE ILE B . n 
B 2 64  GLU 64  368 368 GLU GLU B . n 
B 2 65  PRO 65  369 369 PRO PRO B . n 
B 2 66  TYR 66  370 370 TYR TYR B . n 
B 2 67  ARG 67  371 371 ARG ARG B . n 
B 2 68  LEU 68  372 372 LEU LEU B . n 
B 2 69  PRO 69  373 373 PRO PRO B . n 
B 2 70  GLU 70  374 374 GLU GLU B . n 
B 2 71  VAL 71  375 375 VAL VAL B . n 
B 2 72  ILE 72  376 376 ILE ILE B . n 
B 2 73  GLN 73  377 377 GLN GLN B . n 
B 2 74  LYS 74  378 378 LYS LYS B . n 
B 2 75  CYS 75  379 379 CYS CYS B . n 
B 2 76  ASN 76  380 380 ASN ASN B . n 
B 2 77  ALA 77  381 381 ALA ALA B . n 
B 2 78  ARG 78  382 382 ARG ARG B . n 
B 2 79  TRP 79  383 383 TRP TRP B . n 
B 2 80  THR 80  384 384 THR THR B . n 
B 2 81  THR 81  385 385 THR THR B . n 
B 2 82  GLU 82  386 386 GLU GLU B . n 
B 2 83  GLU 83  387 387 GLU GLU B . n 
B 2 84  GLN 84  388 388 GLN GLN B . n 
B 2 85  LEU 85  389 389 LEU LEU B . n 
B 2 86  LEU 86  390 390 LEU LEU B . n 
B 2 87  ALA 87  391 391 ALA ALA B . n 
B 2 88  VAL 88  392 392 VAL VAL B . n 
B 2 89  GLN 89  393 393 GLN GLN B . n 
B 2 90  ALA 90  394 394 ALA ALA B . n 
B 2 91  ILE 91  395 395 ILE ILE B . n 
B 2 92  ARG 92  396 396 ARG ARG B . n 
B 2 93  LYS 93  397 397 LYS LYS B . n 
B 2 94  TYR 94  398 398 TYR TYR B . n 
B 2 95  GLY 95  399 399 GLY GLY B . n 
B 2 96  ARG 96  400 400 ARG ARG B . n 
B 2 97  ASP 97  401 401 ASP ASP B . n 
B 2 98  PHE 98  402 402 PHE PHE B . n 
B 2 99  GLN 99  403 403 GLN GLN B . n 
B 2 100 ALA 100 404 404 ALA ALA B . n 
B 2 101 ILE 101 405 405 ILE ILE B . n 
B 2 102 SER 102 406 406 SER SER B . n 
B 2 103 ASP 103 407 407 ASP ASP B . n 
B 2 104 VAL 104 408 408 VAL VAL B . n 
B 2 105 ILE 105 409 409 ILE ILE B . n 
B 2 106 GLY 106 410 410 GLY GLY B . n 
B 2 107 ASN 107 411 411 ASN ASN B . n 
B 2 108 LYS 108 412 412 LYS LYS B . n 
B 2 109 SER 109 413 413 SER SER B . n 
B 2 110 VAL 110 414 414 VAL VAL B . n 
B 2 111 VAL 111 415 415 VAL VAL B . n 
B 2 112 GLN 112 416 416 GLN GLN B . n 
B 2 113 VAL 113 417 417 VAL VAL B . n 
B 2 114 LYS 114 418 418 LYS LYS B . n 
B 2 115 ASN 115 419 419 ASN ASN B . n 
B 2 116 PHE 116 420 420 PHE PHE B . n 
B 2 117 PHE 117 421 421 PHE PHE B . n 
B 2 118 VAL 118 422 422 VAL VAL B . n 
B 2 119 ASN 119 423 423 ASN ASN B . n 
B 2 120 TYR 120 424 424 TYR TYR B . n 
B 2 121 ARG 121 425 425 ARG ARG B . n 
B 2 122 ARG 122 426 426 ARG ARG B . n 
B 2 123 ARG 123 427 427 ARG ARG B . n 
B 2 124 PHE 124 428 428 PHE PHE B . n 
B 2 125 ASN 125 429 429 ASN ASN B . n 
B 2 126 ILE 126 430 430 ILE ILE B . n 
B 2 127 ASP 127 431 431 ASP ASP B . n 
B 2 128 GLU 128 432 432 GLU GLU B . n 
B 2 129 VAL 129 433 433 VAL VAL B . n 
B 2 130 LEU 130 434 434 LEU LEU B . n 
B 2 131 GLN 131 435 435 GLN GLN B . n 
B 2 132 GLU 132 436 436 GLU GLU B . n 
B 2 133 TRP 133 437 437 TRP TRP B . n 
B 2 134 GLU 134 438 438 GLU GLU B . n 
B 2 135 ALA 135 439 439 ALA ALA B . n 
B 2 136 GLU 136 440 440 GLU GLU B . n 
B 2 137 HIS 137 441 ?   ?   ?   B . n 
B 2 138 GLY 138 442 ?   ?   ?   B . n 
B 2 139 LYS 139 443 ?   ?   ?   B . n 
B 2 140 GLU 140 444 ?   ?   ?   B . n 
B 2 141 GLU 141 445 ?   ?   ?   B . n 
B 2 142 THR 142 446 ?   ?   ?   B . n 
B 2 143 ASN 143 447 ?   ?   ?   B . n 
B 2 144 GLY 144 448 ?   ?   ?   B . n 
B 2 145 PRO 145 449 ?   ?   ?   B . n 
B 2 146 SER 146 450 ?   ?   ?   B . n 
B 2 147 ASN 147 451 ?   ?   ?   B . n 
B 2 148 GLN 148 452 ?   ?   ?   B . n 
B 2 149 LYS 149 453 ?   ?   ?   B . n 
B 2 150 PRO 150 454 ?   ?   ?   B . n 
B 2 151 VAL 151 455 ?   ?   ?   B . n 
B 2 152 LYS 152 456 ?   ?   ?   B . n 
B 2 153 SER 153 457 ?   ?   ?   B . n 
B 2 154 PRO 154 458 ?   ?   ?   B . n 
B 2 155 ASP 155 459 ?   ?   ?   B . n 
B 2 156 ASN 156 460 ?   ?   ?   B . n 
B 2 157 SER 157 461 ?   ?   ?   B . n 
B 2 158 ILE 158 462 ?   ?   ?   B . n 
B 2 159 LYS 159 463 ?   ?   ?   B . n 
B 2 160 MET 160 464 ?   ?   ?   B . n 
B 2 161 PRO 161 465 ?   ?   ?   B . n 
B 2 162 GLU 162 466 ?   ?   ?   B . n 
B 2 163 GLU 163 467 ?   ?   ?   B . n 
B 2 164 GLU 164 468 ?   ?   ?   B . n 
B 2 165 ASP 165 469 ?   ?   ?   B . n 
B 2 166 GLU 166 470 ?   ?   ?   B . n 
B 2 167 ALA 167 471 ?   ?   ?   B . n 
B 2 168 PRO 168 472 ?   ?   ?   B . n 
B 2 169 VAL 169 473 ?   ?   ?   B . n 
B 2 170 LEU 170 474 ?   ?   ?   B . n 
B 2 171 ASP 171 475 ?   ?   ?   B . n 
B 2 172 VAL 172 476 ?   ?   ?   B . n 
B 2 173 ARG 173 477 ?   ?   ?   B . n 
B 2 174 TYR 174 478 ?   ?   ?   B . n 
B 2 175 ALA 175 479 ?   ?   ?   B . n 
B 2 176 SER 176 480 ?   ?   ?   B . n 
B 2 177 ALA 177 481 ?   ?   ?   B . n 
B 2 178 SER 178 482 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H8N 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H8N 
_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         C 
_pdbx_nonpoly_scheme.entity_id       3 
_pdbx_nonpoly_scheme.mon_id          A1H8N 
_pdbx_nonpoly_scheme.ndb_seq_num     1 
_pdbx_nonpoly_scheme.pdb_seq_num     901 
_pdbx_nonpoly_scheme.auth_seq_num    1 
_pdbx_nonpoly_scheme.pdb_mon_id      A1H8N 
_pdbx_nonpoly_scheme.auth_mon_id     DRG 
_pdbx_nonpoly_scheme.pdb_strand_id   A 
_pdbx_nonpoly_scheme.pdb_ins_code    . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.19.2_4158: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    4 
# 
_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                     9F0A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     118.438 
_cell.length_a_esd                 ? 
_cell.length_b                     179.767 
_cell.length_b_esd                 ? 
_cell.length_c                     234.461 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9F0A 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   9F0A 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             6.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          79.99 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.2 M Sodium Tartrate, 0.1 M ADA, pH 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-02-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.17 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.17 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-3 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9F0A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.34 
_reflns.d_resolution_low                               117.23 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     36015 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          0.995 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.34 
_reflns_shell.d_res_low                                     3.49 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3939 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               12.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.357 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          89.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9F0A 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.36 
_refine.ls_d_res_low                             71.67 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     35683 
_refine.ls_number_reflns_R_free                  1979 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.77 
_refine.ls_percent_reflns_R_free                 5.55 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2010 
_refine.ls_R_factor_R_free                       0.2344 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1990 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.85 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.49 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6293 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         87 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6380 
_refine_hist.d_res_high                       3.36 
_refine_hist.d_res_low                        71.67 
# 
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 
'X-RAY DIFFRACTION' ? 0.011 ? 6518 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.430 ? 8845 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.054 ? 895  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.067 ? 988  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011 ? 1142 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.36 3.44  . . 126 2190 91.00  . . . . 0.3580 . . . . . . . . . . . 0.3883 
'X-RAY DIFFRACTION' 3.44 3.53  . . 140 2403 100.00 . . . . 0.3270 . . . . . . . . . . . 0.3826 
'X-RAY DIFFRACTION' 3.53 3.64  . . 141 2380 100.00 . . . . 0.3169 . . . . . . . . . . . 0.3602 
'X-RAY DIFFRACTION' 3.64 3.76  . . 140 2390 100.00 . . . . 0.2822 . . . . . . . . . . . 0.3034 
'X-RAY DIFFRACTION' 3.76 3.89  . . 142 2409 99.00  . . . . 0.2463 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 3.89 4.05  . . 140 2391 99.00  . . . . 0.2283 . . . . . . . . . . . 0.2805 
'X-RAY DIFFRACTION' 4.05 4.23  . . 141 2402 99.00  . . . . 0.2124 . . . . . . . . . . . 0.2435 
'X-RAY DIFFRACTION' 4.23 4.45  . . 137 2326 96.00  . . . . 0.1884 . . . . . . . . . . . 0.2329 
'X-RAY DIFFRACTION' 4.45 4.73  . . 143 2431 100.00 . . . . 0.1799 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 4.73 5.10  . . 142 2423 100.00 . . . . 0.1652 . . . . . . . . . . . 0.2232 
'X-RAY DIFFRACTION' 5.10 5.61  . . 144 2441 100.00 . . . . 0.1763 . . . . . . . . . . . 0.2496 
'X-RAY DIFFRACTION' 5.61 6.42  . . 145 2462 100.00 . . . . 0.1885 . . . . . . . . . . . 0.2088 
'X-RAY DIFFRACTION' 6.42 8.09  . . 145 2473 100.00 . . . . 0.1752 . . . . . . . . . . . 0.2143 
'X-RAY DIFFRACTION' 8.09 71.67 . . 153 2583 100.00 . . . . 0.1604 . . . . . . . . . . . 0.1695 
# 
_struct.entry_id                     9F0A 
_struct.title                        'N5 Adduct of LSD1-CoREST in complex with MC4455' 
_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        9F0A 
_struct_keywords.text            'Protein complex, Epigenetics, Inhibitor, Flavoprotein, Transcription, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP KDM1A_HUMAN O60341 ? 1 
;MDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISG
PQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVI
IIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPL
YEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELK
ELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLS
SRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEV
IAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVG
STTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYS
YVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATP
GVPAQQSPSM
;
123 
2 UNP RCOR1_HUMAN Q9UKL0 ? 2 
;RAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWT
TEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKM
PEEEDEAPVLDVRYASAS
;
305 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9F0A A 1 ? 730 ? O60341 123 ? 852 ? 123 852 
2 2 9F0A B 1 ? 178 ? Q9UKL0 305 ? 482 ? 305 482 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5450  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  37130 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 51  ? SER A 59  ? GLY A 173 SER A 181 1 ? 9  
HELX_P HELX_P2  AA2 THR A 67  ? PHE A 74  ? THR A 189 PHE A 196 1 ? 8  
HELX_P HELX_P3  AA3 PRO A 81  ? ASN A 102 ? PRO A 203 ASN A 224 1 ? 22 
HELX_P HELX_P4  AA4 THR A 108 ? LEU A 116 ? THR A 230 LEU A 238 1 ? 9  
HELX_P HELX_P5  AA5 VAL A 125 ? HIS A 137 ? VAL A 247 HIS A 259 1 ? 13 
HELX_P HELX_P6  AA6 GLY A 165 ? PHE A 178 ? GLY A 287 PHE A 300 1 ? 14 
HELX_P HELX_P7  AA7 ASN A 218 ? VAL A 227 ? ASN A 340 VAL A 349 1 ? 10 
HELX_P HELX_P8  AA8 PRO A 249 ? GLN A 273 ? PRO A 371 GLN A 395 1 ? 25 
HELX_P HELX_P9  AA9 SER A 285 ? VAL A 346 ? SER A 407 VAL A 468 1 ? 62 
HELX_P HELX_P10 AB1 ASP A 351 ? LEU A 389 ? ASP A 473 LEU A 511 1 ? 39 
HELX_P HELX_P11 AB2 ARG A 402 ? ALA A 419 ? ARG A 524 ALA A 541 1 ? 18 
HELX_P HELX_P12 AB3 ASP A 431 ? GLU A 437 ? ASP A 553 GLU A 559 5 ? 7  
HELX_P HELX_P13 AB4 SER A 450 ? GLU A 458 ? SER A 572 GLU A 580 1 ? 9  
HELX_P HELX_P14 AB5 PRO A 504 ? GLN A 510 ? PRO A 626 GLN A 632 1 ? 7  
HELX_P HELX_P15 AB6 PRO A 522 ? MET A 532 ? PRO A 644 MET A 654 1 ? 11 
HELX_P HELX_P16 AB7 ALA A 586 ? GLY A 591 ? ALA A 708 GLY A 713 1 ? 6  
HELX_P HELX_P17 AB8 ILE A 592 ? ILE A 596 ? ILE A 714 ILE A 718 5 ? 5  
HELX_P HELX_P18 AB9 SER A 597 ? GLY A 614 ? SER A 719 GLY A 736 1 ? 18 
HELX_P HELX_P19 AC1 ASN A 649 ? GLN A 656 ? ASN A 771 GLN A 778 1 ? 8  
HELX_P HELX_P20 AC2 GLY A 678 ? ILE A 682 ? GLY A 800 ILE A 804 5 ? 5  
HELX_P HELX_P21 AC3 THR A 688 ? LEU A 708 ? THR A 810 LEU A 830 1 ? 21 
HELX_P HELX_P22 AC4 SER B 13  ? SER B 21  ? SER B 317 SER B 325 1 ? 9  
HELX_P HELX_P23 AC5 THR B 25  ? LEU B 34  ? THR B 329 LEU B 338 1 ? 10 
HELX_P HELX_P24 AC6 LEU B 34  ? LEU B 59  ? LEU B 338 LEU B 363 1 ? 26 
HELX_P HELX_P25 AC7 THR B 80  ? GLY B 95  ? THR B 384 GLY B 399 1 ? 16 
HELX_P HELX_P26 AC8 ASP B 97  ? GLY B 106 ? ASP B 401 GLY B 410 1 ? 10 
HELX_P HELX_P27 AC9 SER B 109 ? TYR B 120 ? SER B 413 TYR B 424 1 ? 12 
HELX_P HELX_P28 AD1 ARG B 121 ? PHE B 124 ? ARG B 425 PHE B 428 5 ? 4  
HELX_P HELX_P29 AD2 ASN B 125 ? ALA B 135 ? ASN B 429 ALA B 439 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 118 A . ? ALA 240 A PRO 119 A ? PRO 241 A 1 2.80 
2 PRO 348 A . ? PRO 470 A PRO 349 A ? PRO 471 A 1 6.93 
3 GLN 511 A . ? GLN 633 A PRO 512 A ? PRO 634 A 1 4.49 
4 VAL 518 A . ? VAL 640 A PRO 519 A ? PRO 641 A 1 2.95 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? 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 ASP A 461 ? LYS A 463 ? ASP A 583 LYS A 585 
AA1 2 ASP A 181 ? LEU A 185 ? ASP A 303 LEU A 307 
AA1 3 LYS A 158 ? ILE A 162 ? LYS A 280 ILE A 284 
AA1 4 ALA A 498 ? CYS A 501 ? ALA A 620 CYS A 623 
AA1 5 LEU A 674 ? PHE A 676 ? LEU A 796 PHE A 798 
AA2 1 THR A 197 ? LYS A 200 ? THR A 319 LYS A 322 
AA2 2 TYR A 203 ? ASP A 206 ? TYR A 325 ASP A 328 
AA3 1 VAL A 211 ? VAL A 212 ? VAL A 333 VAL A 334 
AA3 2 LEU A 443 ? VAL A 445 ? LEU A 565 VAL A 567 
AA3 3 LEU A 231 ? LYS A 233 ? LEU A 353 LYS A 355 
AA4 1 THR A 491 ? CYS A 496 ? THR A 613 CYS A 618 
AA4 2 GLY A 477 ? ASN A 484 ? GLY A 599 ASN A 606 
AA4 3 THR A 466 ? THR A 474 ? THR A 588 THR A 596 
AA4 4 GLN A 516 ? VAL A 518 ? GLN A 638 VAL A 640 
AA5 1 GLY A 533 ? GLY A 535 ? GLY A 655 GLY A 657 
AA5 2 TYR A 639 ? TYR A 641 ? TYR A 761 TYR A 763 
AA6 1 LEU A 555 ? GLY A 557 ? LEU A 677 GLY A 679 
AA6 2 LEU A 571 ? ASN A 574 ? LEU A 693 ASN A 696 
AA6 3 ILE A 580 ? VAL A 585 ? ILE A 702 VAL A 707 
AA6 4 ASN A 538 ? CYS A 543 ? ASN A 660 CYS A 665 
AA6 5 GLU A 623 ? VAL A 626 ? GLU A 745 VAL A 748 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LYS A 463 ? O LYS A 585 N LEU A 184 ? N LEU A 306 
AA1 2 3 O LEU A 185 ? O LEU A 307 N ILE A 161 ? N ILE A 283 
AA1 3 4 N ILE A 162 ? N ILE A 284 O LEU A 500 ? O LEU A 622 
AA1 4 5 N CYS A 501 ? N CYS A 623 O PHE A 675 ? O PHE A 797 
AA2 1 2 N LYS A 200 ? N LYS A 322 O TYR A 203 ? O TYR A 325 
AA3 1 2 N VAL A 212 ? N VAL A 334 O LEU A 443 ? O LEU A 565 
AA3 2 3 O THR A 444 ? O THR A 566 N ALA A 232 ? N ALA A 354 
AA4 1 2 O PHE A 492 ? O PHE A 614 N ALA A 482 ? N ALA A 604 
AA4 2 3 O ILE A 481 ? O ILE A 603 N ARG A 469 ? N ARG A 591 
AA4 3 4 N VAL A 471 ? N VAL A 593 O VAL A 518 ? O VAL A 640 
AA5 1 2 N GLY A 535 ? N GLY A 657 O TYR A 639 ? O TYR A 761 
AA6 1 2 N PHE A 556 ? N PHE A 678 O PHE A 572 ? O PHE A 694 
AA6 2 3 N TRP A 573 ? N TRP A 695 O LEU A 582 ? O LEU A 704 
AA6 3 4 O ALA A 583 ? O ALA A 705 N VAL A 540 ? N VAL A 662 
AA6 4 5 N VAL A 541 ? N VAL A 663 O VAL A 625 ? O VAL A 747 
# 
_pdbx_entry_details.entry_id                   9F0A 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A LEU 386 ? ? OG1 A THR 389 ? ? 2.07 
2 1 OD1 A ASP 486 ? ? OH  B TYR 398 ? ? 2.15 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A PRO 794 ? ? N A PRO 794 ? ? 1.726 1.474 0.252 0.014 N 
2 1 CD B PRO 369 ? ? N B PRO 369 ? ? 1.606 1.474 0.132 0.014 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 N  A GLY 338 ? ? CA A GLY 338 ? ? C  A GLY 338 ? ? 93.95  113.10 -19.15 2.50 N 
2  1 CB A ASN 403 ? ? CA A ASN 403 ? ? C  A ASN 403 ? ? 84.39  110.40 -26.01 2.00 N 
3  1 CB A LYS 507 ? ? CA A LYS 507 ? ? C  A LYS 507 ? ? 123.32 110.40 12.92  2.00 N 
4  1 CB A ALA 579 ? ? CA A ALA 579 ? ? C  A ALA 579 ? ? 121.75 110.10 11.65  1.50 N 
5  1 CA A LEU 691 ? ? CB A LEU 691 ? ? CG A LEU 691 ? ? 97.82  115.30 -17.48 2.30 N 
6  1 CB A SER 737 ? ? CA A SER 737 ? ? C  A SER 737 ? ? 122.80 110.10 12.70  1.90 N 
7  1 N  A ALA 777 ? ? CA A ALA 777 ? ? C  A ALA 777 ? ? 129.08 111.00 18.08  2.70 N 
8  1 CB A ILE 793 ? ? CA A ILE 793 ? ? C  A ILE 793 ? ? 89.55  111.60 -22.05 2.00 N 
9  1 C  A ILE 793 ? ? N  A PRO 794 ? ? CA A PRO 794 ? ? 132.61 119.30 13.31  1.50 Y 
10 1 CA A PRO 794 ? ? N  A PRO 794 ? ? CD A PRO 794 ? ? 96.73  111.70 -14.97 1.40 N 
11 1 N  A PRO 794 ? ? CA A PRO 794 ? ? CB A PRO 794 ? ? 115.24 103.30 11.94  1.20 N 
12 1 N  A PRO 794 ? ? CA A PRO 794 ? ? C  A PRO 794 ? ? 92.43  112.10 -19.67 2.60 N 
13 1 N  A GLY 831 ? ? CA A GLY 831 ? ? C  A GLY 831 ? ? 147.90 113.10 34.80  2.50 N 
14 1 N  A ALA 832 ? ? CA A ALA 832 ? ? CB A ALA 832 ? ? 119.68 110.10 9.58   1.40 N 
15 1 CB B GLU 368 ? ? CA B GLU 368 ? ? C  B GLU 368 ? ? 89.75  110.40 -20.65 2.00 N 
16 1 C  B GLU 368 ? ? N  B PRO 369 ? ? CD B PRO 369 ? ? 99.93  128.40 -28.47 2.10 Y 
17 1 N  B PRO 369 ? ? CA B PRO 369 ? ? C  B PRO 369 ? ? 88.95  112.10 -23.15 2.60 N 
18 1 CD B LYS 418 ? ? CE B LYS 418 ? ? NZ B LYS 418 ? ? 97.68  111.70 -14.02 2.30 N 
19 1 N  B ALA 439 ? ? CA B ALA 439 ? ? C  B ALA 439 ? ? 88.09  111.00 -22.91 2.70 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 ARG A 182 ? ? 72.01   30.85   
2  1 HIS A 185 ? ? -59.63  -5.64   
3  1 ASN A 224 ? ? -151.08 89.79   
4  1 SER A 244 ? ? -123.46 -64.97  
5  1 HIS A 259 ? ? -93.40  33.76   
6  1 PRO A 274 ? ? -47.59  153.37  
7  1 ARG A 316 ? ? -48.66  -19.65  
8  1 MET A 332 ? ? -134.61 -58.94  
9  1 GLU A 373 ? ? -28.43  -54.70  
10 1 ASN A 403 ? ? 36.71   51.19   
11 1 ASN A 514 ? ? -113.11 58.39   
12 1 PRO A 516 ? ? -58.51  175.74  
13 1 PRO A 626 ? ? -36.91  131.39  
14 1 LEU A 693 ? ? -174.25 139.26  
15 1 ALA A 708 ? ? -106.09 -166.05 
16 1 PRO A 741 ? ? -76.79  -165.33 
17 1 ASP A 754 ? ? -35.54  114.54  
18 1 ALA A 757 ? ? -166.18 -43.68  
19 1 SER A 785 ? ? -61.47  -84.57  
20 1 TYR A 807 ? ? -145.18 42.57   
21 1 TYR A 834 ? ? -85.28  32.38   
22 1 ASN B 327 ? ? -158.27 -159.74 
23 1 PRO B 373 ? ? -57.33  175.49  
24 1 ALA B 381 ? ? -132.17 -45.57  
25 1 ARG B 425 ? ? 1.47    -102.77 
26 1 ARG B 426 ? ? -31.47  -37.92  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 ASN A 403 ? ? LYS A 404 ? ? 138.76  
2 1 THR A 684 ? ? THR A 685 ? ? 149.62  
3 1 PRO A 792 ? ? ILE A 793 ? ? 146.66  
4 1 ILE A 793 ? ? PRO A 794 ? ? -141.71 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 758 ? ? 0.295 'SIDE CHAIN' 
2 1 ARG B 425 ? ? 0.157 'SIDE CHAIN' 
3 1 ARG B 426 ? ? 0.292 'SIDE CHAIN' 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ILE 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              793 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -14.39 
# 
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 123 ? A MET 1   
2   1 Y 1 A ASP 124 ? A ASP 2   
3   1 Y 1 A GLU 125 ? A GLU 3   
4   1 Y 1 A SER 126 ? A SER 4   
5   1 Y 1 A LEU 127 ? A LEU 5   
6   1 Y 1 A ALA 128 ? A ALA 6   
7   1 Y 1 A ASN 129 ? A ASN 7   
8   1 Y 1 A LEU 130 ? A LEU 8   
9   1 Y 1 A SER 131 ? A SER 9   
10  1 Y 1 A GLU 132 ? A GLU 10  
11  1 Y 1 A ASP 133 ? A ASP 11  
12  1 Y 1 A GLU 134 ? A GLU 12  
13  1 Y 1 A TYR 135 ? A TYR 13  
14  1 Y 1 A TYR 136 ? A TYR 14  
15  1 Y 1 A SER 137 ? A SER 15  
16  1 Y 1 A GLU 138 ? A GLU 16  
17  1 Y 1 A GLU 139 ? A GLU 17  
18  1 Y 1 A GLU 140 ? A GLU 18  
19  1 Y 1 A ARG 141 ? A ARG 19  
20  1 Y 1 A ASN 142 ? A ASN 20  
21  1 Y 1 A ALA 143 ? A ALA 21  
22  1 Y 1 A LYS 144 ? A LYS 22  
23  1 Y 1 A ALA 145 ? A ALA 23  
24  1 Y 1 A GLU 146 ? A GLU 24  
25  1 Y 1 A LYS 147 ? A LYS 25  
26  1 Y 1 A GLU 148 ? A GLU 26  
27  1 Y 1 A LYS 149 ? A LYS 27  
28  1 Y 1 A LYS 150 ? A LYS 28  
29  1 Y 1 A LEU 151 ? A LEU 29  
30  1 Y 1 A PRO 152 ? A PRO 30  
31  1 Y 1 A PRO 153 ? A PRO 31  
32  1 Y 1 A PRO 154 ? A PRO 32  
33  1 Y 1 A PRO 155 ? A PRO 33  
34  1 Y 1 A PRO 156 ? A PRO 34  
35  1 Y 1 A GLN 157 ? A GLN 35  
36  1 Y 1 A ALA 158 ? A ALA 36  
37  1 Y 1 A PRO 159 ? A PRO 37  
38  1 Y 1 A PRO 160 ? A PRO 38  
39  1 Y 1 A GLU 161 ? A GLU 39  
40  1 Y 1 A GLU 162 ? A GLU 40  
41  1 Y 1 A GLU 163 ? A GLU 41  
42  1 Y 1 A ASN 164 ? A ASN 42  
43  1 Y 1 A GLU 165 ? A GLU 43  
44  1 Y 1 A SER 166 ? A SER 44  
45  1 Y 1 A GLU 167 ? A GLU 45  
46  1 Y 1 A PRO 168 ? A PRO 46  
47  1 Y 1 A GLU 169 ? A GLU 47  
48  1 Y 1 A GLU 170 ? A GLU 48  
49  1 Y 1 A PRO 837 ? A PRO 715 
50  1 Y 1 A ARG 838 ? A ARG 716 
51  1 Y 1 A GLN 839 ? A GLN 717 
52  1 Y 1 A ALA 840 ? A ALA 718 
53  1 Y 1 A THR 841 ? A THR 719 
54  1 Y 1 A PRO 842 ? A PRO 720 
55  1 Y 1 A GLY 843 ? A GLY 721 
56  1 Y 1 A VAL 844 ? A VAL 722 
57  1 Y 1 A PRO 845 ? A PRO 723 
58  1 Y 1 A ALA 846 ? A ALA 724 
59  1 Y 1 A GLN 847 ? A GLN 725 
60  1 Y 1 A GLN 848 ? A GLN 726 
61  1 Y 1 A SER 849 ? A SER 727 
62  1 Y 1 A PRO 850 ? A PRO 728 
63  1 Y 1 A SER 851 ? A SER 729 
64  1 Y 1 A MET 852 ? A MET 730 
65  1 Y 1 B ARG 305 ? B ARG 1   
66  1 Y 1 B ALA 306 ? B ALA 2   
67  1 Y 1 B LYS 307 ? B LYS 3   
68  1 Y 1 B HIS 441 ? B HIS 137 
69  1 Y 1 B GLY 442 ? B GLY 138 
70  1 Y 1 B LYS 443 ? B LYS 139 
71  1 Y 1 B GLU 444 ? B GLU 140 
72  1 Y 1 B GLU 445 ? B GLU 141 
73  1 Y 1 B THR 446 ? B THR 142 
74  1 Y 1 B ASN 447 ? B ASN 143 
75  1 Y 1 B GLY 448 ? B GLY 144 
76  1 Y 1 B PRO 449 ? B PRO 145 
77  1 Y 1 B SER 450 ? B SER 146 
78  1 Y 1 B ASN 451 ? B ASN 147 
79  1 Y 1 B GLN 452 ? B GLN 148 
80  1 Y 1 B LYS 453 ? B LYS 149 
81  1 Y 1 B PRO 454 ? B PRO 150 
82  1 Y 1 B VAL 455 ? B VAL 151 
83  1 Y 1 B LYS 456 ? B LYS 152 
84  1 Y 1 B SER 457 ? B SER 153 
85  1 Y 1 B PRO 458 ? B PRO 154 
86  1 Y 1 B ASP 459 ? B ASP 155 
87  1 Y 1 B ASN 460 ? B ASN 156 
88  1 Y 1 B SER 461 ? B SER 157 
89  1 Y 1 B ILE 462 ? B ILE 158 
90  1 Y 1 B LYS 463 ? B LYS 159 
91  1 Y 1 B MET 464 ? B MET 160 
92  1 Y 1 B PRO 465 ? B PRO 161 
93  1 Y 1 B GLU 466 ? B GLU 162 
94  1 Y 1 B GLU 467 ? B GLU 163 
95  1 Y 1 B GLU 468 ? B GLU 164 
96  1 Y 1 B ASP 469 ? B ASP 165 
97  1 Y 1 B GLU 470 ? B GLU 166 
98  1 Y 1 B ALA 471 ? B ALA 167 
99  1 Y 1 B PRO 472 ? B PRO 168 
100 1 Y 1 B VAL 473 ? B VAL 169 
101 1 Y 1 B LEU 474 ? B LEU 170 
102 1 Y 1 B ASP 475 ? B ASP 171 
103 1 Y 1 B VAL 476 ? B VAL 172 
104 1 Y 1 B ARG 477 ? B ARG 173 
105 1 Y 1 B TYR 478 ? B TYR 174 
106 1 Y 1 B ALA 479 ? B ALA 175 
107 1 Y 1 B SER 480 ? B SER 176 
108 1 Y 1 B ALA 481 ? B ALA 177 
109 1 Y 1 B SER 482 ? B SER 178 
# 
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 
A1H8N C4   C Y N 1   
A1H8N C14  C Y N 2   
A1H8N C5   C Y N 3   
A1H8N C6   C Y N 4   
A1H8N C11  C N N 5   
A1H8N C7   C Y N 6   
A1H8N C8   C N N 7   
A1H8N C9   C N N 8   
A1H8N C10  C N N 9   
A1H8N C12  C Y N 10  
A1H8N C13  C Y N 11  
A1H8N N1   N N N 12  
A1H8N N2   N N N 13  
A1H8N C3   C Y N 14  
A1H8N N3   N N N 15  
A1H8N C1   C N N 16  
A1H8N C15  C Y N 17  
A1H8N C16  C Y N 18  
A1H8N C17  C Y N 19  
A1H8N C18  C Y N 20  
A1H8N C19  C N N 21  
A1H8N C2   C Y N 22  
A1H8N C20  C N N 23  
A1H8N C21  C N S 24  
A1H8N C22  C N N 25  
A1H8N C23  C N N 26  
A1H8N C24  C N N 27  
A1H8N C25  C Y N 28  
A1H8N C26  C Y N 29  
A1H8N C27  C Y N 30  
A1H8N C28  C Y N 31  
A1H8N C29  C Y N 32  
A1H8N C30  C Y N 33  
A1H8N C31  C N N 34  
A1H8N C32  C Y N 35  
A1H8N C33  C Y N 36  
A1H8N C34  C Y N 37  
A1H8N C35  C Y N 38  
A1H8N C36  C N N 39  
A1H8N C37  C N N 40  
A1H8N C38  C N N 41  
A1H8N C39  C N N 42  
A1H8N C40  C N N 43  
A1H8N C41  C N R 44  
A1H8N C42  C N S 45  
A1H8N C43  C N S 46  
A1H8N C44  C N N 47  
A1H8N C45  C N N 48  
A1H8N C46  C N S 49  
A1H8N C47  C N S 50  
A1H8N C48  C Y N 51  
A1H8N C49  C Y N 52  
A1H8N C50  C Y N 53  
A1H8N C51  C Y N 54  
A1H8N C52  C Y N 55  
A1H8N C53  C N S 56  
A1H8N C54  C N R 57  
A1H8N N10  N Y N 58  
A1H8N N11  N N N 59  
A1H8N N12  N Y N 60  
A1H8N N13  N Y N 61  
A1H8N N4   N N N 62  
A1H8N N5   N Y N 63  
A1H8N N6   N N N 64  
A1H8N N7   N N N 65  
A1H8N N8   N N N 66  
A1H8N N9   N Y N 67  
A1H8N O1   O N N 68  
A1H8N O10  O N N 69  
A1H8N O11  O N N 70  
A1H8N O12  O N N 71  
A1H8N O13  O N N 72  
A1H8N O14  O N N 73  
A1H8N O15  O N N 74  
A1H8N O16  O N N 75  
A1H8N O17  O N N 76  
A1H8N O18  O N N 77  
A1H8N O2   O N N 78  
A1H8N O3   O N N 79  
A1H8N O4   O N N 80  
A1H8N O5   O N N 81  
A1H8N O6   O N N 82  
A1H8N O7   O N N 83  
A1H8N O8   O N N 84  
A1H8N O9   O N N 85  
A1H8N P1   P N N 86  
A1H8N P2   P N N 87  
A1H8N H1   H N N 88  
A1H8N H2   H N N 89  
A1H8N H3   H N N 90  
A1H8N H4   H N N 91  
A1H8N H5   H N N 92  
A1H8N H6   H N N 93  
A1H8N H7   H N N 94  
A1H8N H8   H N N 95  
A1H8N H9   H N N 96  
A1H8N H10  H N N 97  
A1H8N H11  H N N 98  
A1H8N H12  H N N 99  
A1H8N H13  H N N 100 
A1H8N H14  H N N 101 
A1H8N H15  H N N 102 
A1H8N H16  H N N 103 
A1H8N H17  H N N 104 
A1H8N H18  H N N 105 
A1H8N H19  H N N 106 
A1H8N H20  H N N 107 
A1H8N H21  H N N 108 
A1H8N H22  H N N 109 
A1H8N H23  H N N 110 
A1H8N H24  H N N 111 
A1H8N H25  H N N 112 
A1H8N H26  H N N 113 
A1H8N H27  H N N 114 
A1H8N H28  H N N 115 
A1H8N H29  H N N 116 
A1H8N H30  H N N 117 
A1H8N H31  H N N 118 
A1H8N H32  H N N 119 
A1H8N H33  H N N 120 
A1H8N H34  H N N 121 
A1H8N H35  H N N 122 
A1H8N H36  H N N 123 
A1H8N H38  H N N 124 
A1H8N H39  H N N 125 
A1H8N H40  H N N 126 
A1H8N H41  H N N 127 
A1H8N H42  H N N 128 
A1H8N H43  H N N 129 
A1H8N H44  H N N 130 
A1H8N H45  H N N 131 
A1H8N H46  H N N 132 
A1H8N H47  H N N 133 
A1H8N H48  H N N 134 
A1H8N H49  H N N 135 
A1H8N H50  H N N 136 
A1H8N H51  H N N 137 
A1H8N H52  H N N 138 
A1H8N H53  H N N 139 
A1H8N H54  H N N 140 
A1H8N H56  H N N 141 
A1H8N H57  H N N 142 
A1H8N H58  H N N 143 
A1H8N H59  H N N 144 
A1H8N H60  H N N 145 
A1H8N H61  H N N 146 
A1H8N H62  H N N 147 
A1H8N H63  H N N 148 
A1H8N H64  H N N 149 
A1H8N H37  H N N 150 
ALA   N    N N N 151 
ALA   CA   C N S 152 
ALA   C    C N N 153 
ALA   O    O N N 154 
ALA   CB   C N N 155 
ALA   OXT  O N N 156 
ALA   H    H N N 157 
ALA   H2   H N N 158 
ALA   HA   H N N 159 
ALA   HB1  H N N 160 
ALA   HB2  H N N 161 
ALA   HB3  H N N 162 
ALA   HXT  H N N 163 
ARG   N    N N N 164 
ARG   CA   C N S 165 
ARG   C    C N N 166 
ARG   O    O N N 167 
ARG   CB   C N N 168 
ARG   CG   C N N 169 
ARG   CD   C N N 170 
ARG   NE   N N N 171 
ARG   CZ   C N N 172 
ARG   NH1  N N N 173 
ARG   NH2  N N N 174 
ARG   OXT  O N N 175 
ARG   H    H N N 176 
ARG   H2   H N N 177 
ARG   HA   H N N 178 
ARG   HB2  H N N 179 
ARG   HB3  H N N 180 
ARG   HG2  H N N 181 
ARG   HG3  H N N 182 
ARG   HD2  H N N 183 
ARG   HD3  H N N 184 
ARG   HE   H N N 185 
ARG   HH11 H N N 186 
ARG   HH12 H N N 187 
ARG   HH21 H N N 188 
ARG   HH22 H N N 189 
ARG   HXT  H N N 190 
ASN   N    N N N 191 
ASN   CA   C N S 192 
ASN   C    C N N 193 
ASN   O    O N N 194 
ASN   CB   C N N 195 
ASN   CG   C N N 196 
ASN   OD1  O N N 197 
ASN   ND2  N N N 198 
ASN   OXT  O N N 199 
ASN   H    H N N 200 
ASN   H2   H N N 201 
ASN   HA   H N N 202 
ASN   HB2  H N N 203 
ASN   HB3  H N N 204 
ASN   HD21 H N N 205 
ASN   HD22 H N N 206 
ASN   HXT  H N N 207 
ASP   N    N N N 208 
ASP   CA   C N S 209 
ASP   C    C N N 210 
ASP   O    O N N 211 
ASP   CB   C N N 212 
ASP   CG   C N N 213 
ASP   OD1  O N N 214 
ASP   OD2  O N N 215 
ASP   OXT  O N N 216 
ASP   H    H N N 217 
ASP   H2   H N N 218 
ASP   HA   H N N 219 
ASP   HB2  H N N 220 
ASP   HB3  H N N 221 
ASP   HD2  H N N 222 
ASP   HXT  H N N 223 
CYS   N    N N N 224 
CYS   CA   C N R 225 
CYS   C    C N N 226 
CYS   O    O N N 227 
CYS   CB   C N N 228 
CYS   SG   S N N 229 
CYS   OXT  O N N 230 
CYS   H    H N N 231 
CYS   H2   H N N 232 
CYS   HA   H N N 233 
CYS   HB2  H N N 234 
CYS   HB3  H N N 235 
CYS   HG   H N N 236 
CYS   HXT  H N N 237 
GLN   N    N N N 238 
GLN   CA   C N S 239 
GLN   C    C N N 240 
GLN   O    O N N 241 
GLN   CB   C N N 242 
GLN   CG   C N N 243 
GLN   CD   C N N 244 
GLN   OE1  O N N 245 
GLN   NE2  N N N 246 
GLN   OXT  O N N 247 
GLN   H    H N N 248 
GLN   H2   H N N 249 
GLN   HA   H N N 250 
GLN   HB2  H N N 251 
GLN   HB3  H N N 252 
GLN   HG2  H N N 253 
GLN   HG3  H N N 254 
GLN   HE21 H N N 255 
GLN   HE22 H N N 256 
GLN   HXT  H N N 257 
GLU   N    N N N 258 
GLU   CA   C N S 259 
GLU   C    C N N 260 
GLU   O    O N N 261 
GLU   CB   C N N 262 
GLU   CG   C N N 263 
GLU   CD   C N N 264 
GLU   OE1  O N N 265 
GLU   OE2  O N N 266 
GLU   OXT  O N N 267 
GLU   H    H N N 268 
GLU   H2   H N N 269 
GLU   HA   H N N 270 
GLU   HB2  H N N 271 
GLU   HB3  H N N 272 
GLU   HG2  H N N 273 
GLU   HG3  H N N 274 
GLU   HE2  H N N 275 
GLU   HXT  H N N 276 
GLY   N    N N N 277 
GLY   CA   C N N 278 
GLY   C    C N N 279 
GLY   O    O N N 280 
GLY   OXT  O N N 281 
GLY   H    H N N 282 
GLY   H2   H N N 283 
GLY   HA2  H N N 284 
GLY   HA3  H N N 285 
GLY   HXT  H N N 286 
HIS   N    N N N 287 
HIS   CA   C N S 288 
HIS   C    C N N 289 
HIS   O    O N N 290 
HIS   CB   C N N 291 
HIS   CG   C Y N 292 
HIS   ND1  N Y N 293 
HIS   CD2  C Y N 294 
HIS   CE1  C Y N 295 
HIS   NE2  N Y N 296 
HIS   OXT  O N N 297 
HIS   H    H N N 298 
HIS   H2   H N N 299 
HIS   HA   H N N 300 
HIS   HB2  H N N 301 
HIS   HB3  H N N 302 
HIS   HD1  H N N 303 
HIS   HD2  H N N 304 
HIS   HE1  H N N 305 
HIS   HE2  H N N 306 
HIS   HXT  H N N 307 
ILE   N    N N N 308 
ILE   CA   C N S 309 
ILE   C    C N N 310 
ILE   O    O N N 311 
ILE   CB   C N S 312 
ILE   CG1  C N N 313 
ILE   CG2  C N N 314 
ILE   CD1  C N N 315 
ILE   OXT  O N N 316 
ILE   H    H N N 317 
ILE   H2   H N N 318 
ILE   HA   H N N 319 
ILE   HB   H N N 320 
ILE   HG12 H N N 321 
ILE   HG13 H N N 322 
ILE   HG21 H N N 323 
ILE   HG22 H N N 324 
ILE   HG23 H N N 325 
ILE   HD11 H N N 326 
ILE   HD12 H N N 327 
ILE   HD13 H N N 328 
ILE   HXT  H N N 329 
LEU   N    N N N 330 
LEU   CA   C N S 331 
LEU   C    C N N 332 
LEU   O    O N N 333 
LEU   CB   C N N 334 
LEU   CG   C N N 335 
LEU   CD1  C N N 336 
LEU   CD2  C N N 337 
LEU   OXT  O N N 338 
LEU   H    H N N 339 
LEU   H2   H N N 340 
LEU   HA   H N N 341 
LEU   HB2  H N N 342 
LEU   HB3  H N N 343 
LEU   HG   H N N 344 
LEU   HD11 H N N 345 
LEU   HD12 H N N 346 
LEU   HD13 H N N 347 
LEU   HD21 H N N 348 
LEU   HD22 H N N 349 
LEU   HD23 H N N 350 
LEU   HXT  H N N 351 
LYS   N    N N N 352 
LYS   CA   C N S 353 
LYS   C    C N N 354 
LYS   O    O N N 355 
LYS   CB   C N N 356 
LYS   CG   C N N 357 
LYS   CD   C N N 358 
LYS   CE   C N N 359 
LYS   NZ   N N N 360 
LYS   OXT  O N N 361 
LYS   H    H N N 362 
LYS   H2   H N N 363 
LYS   HA   H N N 364 
LYS   HB2  H N N 365 
LYS   HB3  H N N 366 
LYS   HG2  H N N 367 
LYS   HG3  H N N 368 
LYS   HD2  H N N 369 
LYS   HD3  H N N 370 
LYS   HE2  H N N 371 
LYS   HE3  H N N 372 
LYS   HZ1  H N N 373 
LYS   HZ2  H N N 374 
LYS   HZ3  H N N 375 
LYS   HXT  H N N 376 
MET   N    N N N 377 
MET   CA   C N S 378 
MET   C    C N N 379 
MET   O    O N N 380 
MET   CB   C N N 381 
MET   CG   C N N 382 
MET   SD   S N N 383 
MET   CE   C N N 384 
MET   OXT  O N N 385 
MET   H    H N N 386 
MET   H2   H N N 387 
MET   HA   H N N 388 
MET   HB2  H N N 389 
MET   HB3  H N N 390 
MET   HG2  H N N 391 
MET   HG3  H N N 392 
MET   HE1  H N N 393 
MET   HE2  H N N 394 
MET   HE3  H N N 395 
MET   HXT  H N N 396 
PHE   N    N N N 397 
PHE   CA   C N S 398 
PHE   C    C N N 399 
PHE   O    O N N 400 
PHE   CB   C N N 401 
PHE   CG   C Y N 402 
PHE   CD1  C Y N 403 
PHE   CD2  C Y N 404 
PHE   CE1  C Y N 405 
PHE   CE2  C Y N 406 
PHE   CZ   C Y N 407 
PHE   OXT  O N N 408 
PHE   H    H N N 409 
PHE   H2   H N N 410 
PHE   HA   H N N 411 
PHE   HB2  H N N 412 
PHE   HB3  H N N 413 
PHE   HD1  H N N 414 
PHE   HD2  H N N 415 
PHE   HE1  H N N 416 
PHE   HE2  H N N 417 
PHE   HZ   H N N 418 
PHE   HXT  H N N 419 
PRO   N    N N N 420 
PRO   CA   C N S 421 
PRO   C    C N N 422 
PRO   O    O N N 423 
PRO   CB   C N N 424 
PRO   CG   C N N 425 
PRO   CD   C N N 426 
PRO   OXT  O N N 427 
PRO   H    H N N 428 
PRO   HA   H N N 429 
PRO   HB2  H N N 430 
PRO   HB3  H N N 431 
PRO   HG2  H N N 432 
PRO   HG3  H N N 433 
PRO   HD2  H N N 434 
PRO   HD3  H N N 435 
PRO   HXT  H N N 436 
SER   N    N N N 437 
SER   CA   C N S 438 
SER   C    C N N 439 
SER   O    O N N 440 
SER   CB   C N N 441 
SER   OG   O N N 442 
SER   OXT  O N N 443 
SER   H    H N N 444 
SER   H2   H N N 445 
SER   HA   H N N 446 
SER   HB2  H N N 447 
SER   HB3  H N N 448 
SER   HG   H N N 449 
SER   HXT  H N N 450 
THR   N    N N N 451 
THR   CA   C N S 452 
THR   C    C N N 453 
THR   O    O N N 454 
THR   CB   C N R 455 
THR   OG1  O N N 456 
THR   CG2  C N N 457 
THR   OXT  O N N 458 
THR   H    H N N 459 
THR   H2   H N N 460 
THR   HA   H N N 461 
THR   HB   H N N 462 
THR   HG1  H N N 463 
THR   HG21 H N N 464 
THR   HG22 H N N 465 
THR   HG23 H N N 466 
THR   HXT  H N N 467 
TRP   N    N N N 468 
TRP   CA   C N S 469 
TRP   C    C N N 470 
TRP   O    O N N 471 
TRP   CB   C N N 472 
TRP   CG   C Y N 473 
TRP   CD1  C Y N 474 
TRP   CD2  C Y N 475 
TRP   NE1  N Y N 476 
TRP   CE2  C Y N 477 
TRP   CE3  C Y N 478 
TRP   CZ2  C Y N 479 
TRP   CZ3  C Y N 480 
TRP   CH2  C Y N 481 
TRP   OXT  O N N 482 
TRP   H    H N N 483 
TRP   H2   H N N 484 
TRP   HA   H N N 485 
TRP   HB2  H N N 486 
TRP   HB3  H N N 487 
TRP   HD1  H N N 488 
TRP   HE1  H N N 489 
TRP   HE3  H N N 490 
TRP   HZ2  H N N 491 
TRP   HZ3  H N N 492 
TRP   HH2  H N N 493 
TRP   HXT  H N N 494 
TYR   N    N N N 495 
TYR   CA   C N S 496 
TYR   C    C N N 497 
TYR   O    O N N 498 
TYR   CB   C N N 499 
TYR   CG   C Y N 500 
TYR   CD1  C Y N 501 
TYR   CD2  C Y N 502 
TYR   CE1  C Y N 503 
TYR   CE2  C Y N 504 
TYR   CZ   C Y N 505 
TYR   OH   O N N 506 
TYR   OXT  O N N 507 
TYR   H    H N N 508 
TYR   H2   H N N 509 
TYR   HA   H N N 510 
TYR   HB2  H N N 511 
TYR   HB3  H N N 512 
TYR   HD1  H N N 513 
TYR   HD2  H N N 514 
TYR   HE1  H N N 515 
TYR   HE2  H N N 516 
TYR   HH   H N N 517 
TYR   HXT  H N N 518 
VAL   N    N N N 519 
VAL   CA   C N S 520 
VAL   C    C N N 521 
VAL   O    O N N 522 
VAL   CB   C N N 523 
VAL   CG1  C N N 524 
VAL   CG2  C N N 525 
VAL   OXT  O N N 526 
VAL   H    H N N 527 
VAL   H2   H N N 528 
VAL   HA   H N N 529 
VAL   HB   H N N 530 
VAL   HG11 H N N 531 
VAL   HG12 H N N 532 
VAL   HG13 H N N 533 
VAL   HG21 H N N 534 
VAL   HG22 H N N 535 
VAL   HG23 H N N 536 
VAL   HXT  H N N 537 
# 
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 
A1H8N C8  C7   sing N N 1   
A1H8N O1  C9   doub N N 2   
A1H8N C7  C6   doub Y N 3   
A1H8N C7  C2   sing Y N 4   
A1H8N C6  C5   sing Y N 5   
A1H8N C9  C10  sing N N 6   
A1H8N C9  N1   sing N N 7   
A1H8N C1  C2   sing N N 8   
A1H8N C2  C3   doub Y N 9   
A1H8N C10 C11  sing N N 10  
A1H8N C11 C12  sing N N 11  
A1H8N C5  N1   sing N N 12  
A1H8N C5  C4   doub Y N 13  
A1H8N N1  C36  sing N N 14  
A1H8N C31 C30  sing N N 15  
A1H8N C31 N4   sing N N 16  
A1H8N C29 C30  doub Y N 17  
A1H8N C29 C28  sing Y N 18  
A1H8N C12 C13  doub Y N 19  
A1H8N C12 C35  sing Y N 20  
A1H8N C22 C21  sing N N 21  
A1H8N C22 N4   sing N N 22  
A1H8N C3  C4   sing Y N 23  
A1H8N O5  C39  doub N N 24  
A1H8N C13 C14  sing Y N 25  
A1H8N C30 C25  sing Y N 26  
A1H8N C28 C27  doub Y N 27  
A1H8N C21 O3   sing N N 28  
A1H8N C21 C20  sing N N 29  
A1H8N C4  N8   sing N N 30  
A1H8N N4  C23  sing N N 31  
A1H8N C35 C34  doub Y N 32  
A1H8N C36 C39  sing N N 33  
A1H8N C36 C37  doub N N 34  
A1H8N C39 N7   sing N N 35  
A1H8N C14 C15  doub Y N 36  
A1H8N C20 N3   sing N N 37  
A1H8N C34 C15  sing Y N 38  
A1H8N C27 C26  sing Y N 39  
A1H8N C25 C26  doub Y N 40  
A1H8N C25 C24  sing N N 41  
A1H8N N8  C37  sing N N 42  
A1H8N N8  C40  sing N N 43  
A1H8N C15 N2   sing N N 44  
A1H8N C23 C24  sing N N 45  
A1H8N C37 N6   sing N N 46  
A1H8N N7  C38  sing N N 47  
A1H8N N2  C16  sing N N 48  
A1H8N N3  C19  sing N N 49  
A1H8N C40 C41  sing N N 50  
A1H8N C16 C17  doub Y N 51  
A1H8N C16 N5   sing Y N 52  
A1H8N O6  C41  sing N N 53  
A1H8N C17 C18  sing Y N 54  
A1H8N N6  C38  sing N N 55  
A1H8N N5  C33  doub Y N 56  
A1H8N C41 C42  sing N N 57  
A1H8N C38 O4   doub N N 58  
A1H8N C18 C19  sing N N 59  
A1H8N C18 C32  doub Y N 60  
A1H8N C19 O2   doub N N 61  
A1H8N C33 C32  sing Y N 62  
A1H8N O17 C53  sing N N 63  
A1H8N C42 C43  sing N N 64  
A1H8N C42 O7   sing N N 65  
A1H8N O13 P2   doub N N 66  
A1H8N C43 O8   sing N N 67  
A1H8N C43 C44  sing N N 68  
A1H8N C48 N10  doub Y N 69  
A1H8N C48 N9   sing Y N 70  
A1H8N N10 C49  sing Y N 71  
A1H8N C53 C47  sing N N 72  
A1H8N C53 C54  sing N N 73  
A1H8N O18 C54  sing N N 74  
A1H8N O14 P2   sing N N 75  
A1H8N C47 N9   sing N N 76  
A1H8N C47 O16  sing N N 77  
A1H8N N9  C52  sing Y N 78  
A1H8N P2  O15  sing N N 79  
A1H8N P2  O12  sing N N 80  
A1H8N C49 C52  doub Y N 81  
A1H8N C49 C50  sing Y N 82  
A1H8N C54 C46  sing N N 83  
A1H8N C46 O16  sing N N 84  
A1H8N C46 C45  sing N N 85  
A1H8N C52 N13  sing Y N 86  
A1H8N C44 O9   sing N N 87  
A1H8N N11 C50  sing N N 88  
A1H8N C50 N12  doub Y N 89  
A1H8N O15 C45  sing N N 90  
A1H8N O12 P1   sing N N 91  
A1H8N O9  P1   sing N N 92  
A1H8N N13 C51  doub Y N 93  
A1H8N N12 C51  sing Y N 94  
A1H8N P1  O10  doub N N 95  
A1H8N P1  O11  sing N N 96  
A1H8N C14 H1   sing N N 97  
A1H8N C6  H2   sing N N 98  
A1H8N C11 H3   sing N N 99  
A1H8N C11 H4   sing N N 100 
A1H8N C8  H5   sing N N 101 
A1H8N C8  H6   sing N N 102 
A1H8N C8  H7   sing N N 103 
A1H8N C10 H8   sing N N 104 
A1H8N C10 H9   sing N N 105 
A1H8N C13 H10  sing N N 106 
A1H8N N2  H11  sing N N 107 
A1H8N C3  H12  sing N N 108 
A1H8N N3  H13  sing N N 109 
A1H8N C1  H14  sing N N 110 
A1H8N C1  H15  sing N N 111 
A1H8N C1  H16  sing N N 112 
A1H8N C17 H17  sing N N 113 
A1H8N C20 H18  sing N N 114 
A1H8N C20 H19  sing N N 115 
A1H8N C21 H20  sing N N 116 
A1H8N C22 H21  sing N N 117 
A1H8N C22 H22  sing N N 118 
A1H8N C23 H23  sing N N 119 
A1H8N C23 H24  sing N N 120 
A1H8N C24 H25  sing N N 121 
A1H8N C24 H26  sing N N 122 
A1H8N C26 H27  sing N N 123 
A1H8N C27 H28  sing N N 124 
A1H8N C28 H29  sing N N 125 
A1H8N C29 H30  sing N N 126 
A1H8N C31 H31  sing N N 127 
A1H8N C31 H32  sing N N 128 
A1H8N C32 H33  sing N N 129 
A1H8N C33 H34  sing N N 130 
A1H8N C34 H35  sing N N 131 
A1H8N C35 H36  sing N N 132 
A1H8N C40 H38  sing N N 133 
A1H8N C40 H39  sing N N 134 
A1H8N C41 H40  sing N N 135 
A1H8N C42 H41  sing N N 136 
A1H8N C43 H42  sing N N 137 
A1H8N C44 H43  sing N N 138 
A1H8N C44 H44  sing N N 139 
A1H8N C45 H45  sing N N 140 
A1H8N C45 H46  sing N N 141 
A1H8N C46 H47  sing N N 142 
A1H8N C47 H48  sing N N 143 
A1H8N C48 H49  sing N N 144 
A1H8N C51 H50  sing N N 145 
A1H8N C53 H51  sing N N 146 
A1H8N C54 H52  sing N N 147 
A1H8N N11 H53  sing N N 148 
A1H8N N11 H54  sing N N 149 
A1H8N N7  H56  sing N N 150 
A1H8N O11 H57  sing N N 151 
A1H8N O14 H58  sing N N 152 
A1H8N O17 H59  sing N N 153 
A1H8N O18 H60  sing N N 154 
A1H8N O3  H61  sing N N 155 
A1H8N O6  H62  sing N N 156 
A1H8N O7  H63  sing N N 157 
A1H8N O8  H64  sing N N 158 
A1H8N N6  H37  sing N N 159 
ALA   N   CA   sing N N 160 
ALA   N   H    sing N N 161 
ALA   N   H2   sing N N 162 
ALA   CA  C    sing N N 163 
ALA   CA  CB   sing N N 164 
ALA   CA  HA   sing N N 165 
ALA   C   O    doub N N 166 
ALA   C   OXT  sing N N 167 
ALA   CB  HB1  sing N N 168 
ALA   CB  HB2  sing N N 169 
ALA   CB  HB3  sing N N 170 
ALA   OXT HXT  sing N N 171 
ARG   N   CA   sing N N 172 
ARG   N   H    sing N N 173 
ARG   N   H2   sing N N 174 
ARG   CA  C    sing N N 175 
ARG   CA  CB   sing N N 176 
ARG   CA  HA   sing N N 177 
ARG   C   O    doub N N 178 
ARG   C   OXT  sing N N 179 
ARG   CB  CG   sing N N 180 
ARG   CB  HB2  sing N N 181 
ARG   CB  HB3  sing N N 182 
ARG   CG  CD   sing N N 183 
ARG   CG  HG2  sing N N 184 
ARG   CG  HG3  sing N N 185 
ARG   CD  NE   sing N N 186 
ARG   CD  HD2  sing N N 187 
ARG   CD  HD3  sing N N 188 
ARG   NE  CZ   sing N N 189 
ARG   NE  HE   sing N N 190 
ARG   CZ  NH1  sing N N 191 
ARG   CZ  NH2  doub N N 192 
ARG   NH1 HH11 sing N N 193 
ARG   NH1 HH12 sing N N 194 
ARG   NH2 HH21 sing N N 195 
ARG   NH2 HH22 sing N N 196 
ARG   OXT HXT  sing N N 197 
ASN   N   CA   sing N N 198 
ASN   N   H    sing N N 199 
ASN   N   H2   sing N N 200 
ASN   CA  C    sing N N 201 
ASN   CA  CB   sing N N 202 
ASN   CA  HA   sing N N 203 
ASN   C   O    doub N N 204 
ASN   C   OXT  sing N N 205 
ASN   CB  CG   sing N N 206 
ASN   CB  HB2  sing N N 207 
ASN   CB  HB3  sing N N 208 
ASN   CG  OD1  doub N N 209 
ASN   CG  ND2  sing N N 210 
ASN   ND2 HD21 sing N N 211 
ASN   ND2 HD22 sing N N 212 
ASN   OXT HXT  sing N N 213 
ASP   N   CA   sing N N 214 
ASP   N   H    sing N N 215 
ASP   N   H2   sing N N 216 
ASP   CA  C    sing N N 217 
ASP   CA  CB   sing N N 218 
ASP   CA  HA   sing N N 219 
ASP   C   O    doub N N 220 
ASP   C   OXT  sing N N 221 
ASP   CB  CG   sing N N 222 
ASP   CB  HB2  sing N N 223 
ASP   CB  HB3  sing N N 224 
ASP   CG  OD1  doub N N 225 
ASP   CG  OD2  sing N N 226 
ASP   OD2 HD2  sing N N 227 
ASP   OXT HXT  sing N N 228 
CYS   N   CA   sing N N 229 
CYS   N   H    sing N N 230 
CYS   N   H2   sing N N 231 
CYS   CA  C    sing N N 232 
CYS   CA  CB   sing N N 233 
CYS   CA  HA   sing N N 234 
CYS   C   O    doub N N 235 
CYS   C   OXT  sing N N 236 
CYS   CB  SG   sing N N 237 
CYS   CB  HB2  sing N N 238 
CYS   CB  HB3  sing N N 239 
CYS   SG  HG   sing N N 240 
CYS   OXT HXT  sing N N 241 
GLN   N   CA   sing N N 242 
GLN   N   H    sing N N 243 
GLN   N   H2   sing N N 244 
GLN   CA  C    sing N N 245 
GLN   CA  CB   sing N N 246 
GLN   CA  HA   sing N N 247 
GLN   C   O    doub N N 248 
GLN   C   OXT  sing N N 249 
GLN   CB  CG   sing N N 250 
GLN   CB  HB2  sing N N 251 
GLN   CB  HB3  sing N N 252 
GLN   CG  CD   sing N N 253 
GLN   CG  HG2  sing N N 254 
GLN   CG  HG3  sing N N 255 
GLN   CD  OE1  doub N N 256 
GLN   CD  NE2  sing N N 257 
GLN   NE2 HE21 sing N N 258 
GLN   NE2 HE22 sing N N 259 
GLN   OXT HXT  sing N N 260 
GLU   N   CA   sing N N 261 
GLU   N   H    sing N N 262 
GLU   N   H2   sing N N 263 
GLU   CA  C    sing N N 264 
GLU   CA  CB   sing N N 265 
GLU   CA  HA   sing N N 266 
GLU   C   O    doub N N 267 
GLU   C   OXT  sing N N 268 
GLU   CB  CG   sing N N 269 
GLU   CB  HB2  sing N N 270 
GLU   CB  HB3  sing N N 271 
GLU   CG  CD   sing N N 272 
GLU   CG  HG2  sing N N 273 
GLU   CG  HG3  sing N N 274 
GLU   CD  OE1  doub N N 275 
GLU   CD  OE2  sing N N 276 
GLU   OE2 HE2  sing N N 277 
GLU   OXT HXT  sing N N 278 
GLY   N   CA   sing N N 279 
GLY   N   H    sing N N 280 
GLY   N   H2   sing N N 281 
GLY   CA  C    sing N N 282 
GLY   CA  HA2  sing N N 283 
GLY   CA  HA3  sing N N 284 
GLY   C   O    doub N N 285 
GLY   C   OXT  sing N N 286 
GLY   OXT HXT  sing N N 287 
HIS   N   CA   sing N N 288 
HIS   N   H    sing N N 289 
HIS   N   H2   sing N N 290 
HIS   CA  C    sing N N 291 
HIS   CA  CB   sing N N 292 
HIS   CA  HA   sing N N 293 
HIS   C   O    doub N N 294 
HIS   C   OXT  sing N N 295 
HIS   CB  CG   sing N N 296 
HIS   CB  HB2  sing N N 297 
HIS   CB  HB3  sing N N 298 
HIS   CG  ND1  sing Y N 299 
HIS   CG  CD2  doub Y N 300 
HIS   ND1 CE1  doub Y N 301 
HIS   ND1 HD1  sing N N 302 
HIS   CD2 NE2  sing Y N 303 
HIS   CD2 HD2  sing N N 304 
HIS   CE1 NE2  sing Y N 305 
HIS   CE1 HE1  sing N N 306 
HIS   NE2 HE2  sing N N 307 
HIS   OXT HXT  sing N N 308 
ILE   N   CA   sing N N 309 
ILE   N   H    sing N N 310 
ILE   N   H2   sing N N 311 
ILE   CA  C    sing N N 312 
ILE   CA  CB   sing N N 313 
ILE   CA  HA   sing N N 314 
ILE   C   O    doub N N 315 
ILE   C   OXT  sing N N 316 
ILE   CB  CG1  sing N N 317 
ILE   CB  CG2  sing N N 318 
ILE   CB  HB   sing N N 319 
ILE   CG1 CD1  sing N N 320 
ILE   CG1 HG12 sing N N 321 
ILE   CG1 HG13 sing N N 322 
ILE   CG2 HG21 sing N N 323 
ILE   CG2 HG22 sing N N 324 
ILE   CG2 HG23 sing N N 325 
ILE   CD1 HD11 sing N N 326 
ILE   CD1 HD12 sing N N 327 
ILE   CD1 HD13 sing N N 328 
ILE   OXT HXT  sing N N 329 
LEU   N   CA   sing N N 330 
LEU   N   H    sing N N 331 
LEU   N   H2   sing N N 332 
LEU   CA  C    sing N N 333 
LEU   CA  CB   sing N N 334 
LEU   CA  HA   sing N N 335 
LEU   C   O    doub N N 336 
LEU   C   OXT  sing N N 337 
LEU   CB  CG   sing N N 338 
LEU   CB  HB2  sing N N 339 
LEU   CB  HB3  sing N N 340 
LEU   CG  CD1  sing N N 341 
LEU   CG  CD2  sing N N 342 
LEU   CG  HG   sing N N 343 
LEU   CD1 HD11 sing N N 344 
LEU   CD1 HD12 sing N N 345 
LEU   CD1 HD13 sing N N 346 
LEU   CD2 HD21 sing N N 347 
LEU   CD2 HD22 sing N N 348 
LEU   CD2 HD23 sing N N 349 
LEU   OXT HXT  sing N N 350 
LYS   N   CA   sing N N 351 
LYS   N   H    sing N N 352 
LYS   N   H2   sing N N 353 
LYS   CA  C    sing N N 354 
LYS   CA  CB   sing N N 355 
LYS   CA  HA   sing N N 356 
LYS   C   O    doub N N 357 
LYS   C   OXT  sing N N 358 
LYS   CB  CG   sing N N 359 
LYS   CB  HB2  sing N N 360 
LYS   CB  HB3  sing N N 361 
LYS   CG  CD   sing N N 362 
LYS   CG  HG2  sing N N 363 
LYS   CG  HG3  sing N N 364 
LYS   CD  CE   sing N N 365 
LYS   CD  HD2  sing N N 366 
LYS   CD  HD3  sing N N 367 
LYS   CE  NZ   sing N N 368 
LYS   CE  HE2  sing N N 369 
LYS   CE  HE3  sing N N 370 
LYS   NZ  HZ1  sing N N 371 
LYS   NZ  HZ2  sing N N 372 
LYS   NZ  HZ3  sing N N 373 
LYS   OXT HXT  sing N N 374 
MET   N   CA   sing N N 375 
MET   N   H    sing N N 376 
MET   N   H2   sing N N 377 
MET   CA  C    sing N N 378 
MET   CA  CB   sing N N 379 
MET   CA  HA   sing N N 380 
MET   C   O    doub N N 381 
MET   C   OXT  sing N N 382 
MET   CB  CG   sing N N 383 
MET   CB  HB2  sing N N 384 
MET   CB  HB3  sing N N 385 
MET   CG  SD   sing N N 386 
MET   CG  HG2  sing N N 387 
MET   CG  HG3  sing N N 388 
MET   SD  CE   sing N N 389 
MET   CE  HE1  sing N N 390 
MET   CE  HE2  sing N N 391 
MET   CE  HE3  sing N N 392 
MET   OXT HXT  sing N N 393 
PHE   N   CA   sing N N 394 
PHE   N   H    sing N N 395 
PHE   N   H2   sing N N 396 
PHE   CA  C    sing N N 397 
PHE   CA  CB   sing N N 398 
PHE   CA  HA   sing N N 399 
PHE   C   O    doub N N 400 
PHE   C   OXT  sing N N 401 
PHE   CB  CG   sing N N 402 
PHE   CB  HB2  sing N N 403 
PHE   CB  HB3  sing N N 404 
PHE   CG  CD1  doub Y N 405 
PHE   CG  CD2  sing Y N 406 
PHE   CD1 CE1  sing Y N 407 
PHE   CD1 HD1  sing N N 408 
PHE   CD2 CE2  doub Y N 409 
PHE   CD2 HD2  sing N N 410 
PHE   CE1 CZ   doub Y N 411 
PHE   CE1 HE1  sing N N 412 
PHE   CE2 CZ   sing Y N 413 
PHE   CE2 HE2  sing N N 414 
PHE   CZ  HZ   sing N N 415 
PHE   OXT HXT  sing N N 416 
PRO   N   CA   sing N N 417 
PRO   N   CD   sing N N 418 
PRO   N   H    sing N N 419 
PRO   CA  C    sing N N 420 
PRO   CA  CB   sing N N 421 
PRO   CA  HA   sing N N 422 
PRO   C   O    doub N N 423 
PRO   C   OXT  sing N N 424 
PRO   CB  CG   sing N N 425 
PRO   CB  HB2  sing N N 426 
PRO   CB  HB3  sing N N 427 
PRO   CG  CD   sing N N 428 
PRO   CG  HG2  sing N N 429 
PRO   CG  HG3  sing N N 430 
PRO   CD  HD2  sing N N 431 
PRO   CD  HD3  sing N N 432 
PRO   OXT HXT  sing N N 433 
SER   N   CA   sing N N 434 
SER   N   H    sing N N 435 
SER   N   H2   sing N N 436 
SER   CA  C    sing N N 437 
SER   CA  CB   sing N N 438 
SER   CA  HA   sing N N 439 
SER   C   O    doub N N 440 
SER   C   OXT  sing N N 441 
SER   CB  OG   sing N N 442 
SER   CB  HB2  sing N N 443 
SER   CB  HB3  sing N N 444 
SER   OG  HG   sing N N 445 
SER   OXT HXT  sing N N 446 
THR   N   CA   sing N N 447 
THR   N   H    sing N N 448 
THR   N   H2   sing N N 449 
THR   CA  C    sing N N 450 
THR   CA  CB   sing N N 451 
THR   CA  HA   sing N N 452 
THR   C   O    doub N N 453 
THR   C   OXT  sing N N 454 
THR   CB  OG1  sing N N 455 
THR   CB  CG2  sing N N 456 
THR   CB  HB   sing N N 457 
THR   OG1 HG1  sing N N 458 
THR   CG2 HG21 sing N N 459 
THR   CG2 HG22 sing N N 460 
THR   CG2 HG23 sing N N 461 
THR   OXT HXT  sing N N 462 
TRP   N   CA   sing N N 463 
TRP   N   H    sing N N 464 
TRP   N   H2   sing N N 465 
TRP   CA  C    sing N N 466 
TRP   CA  CB   sing N N 467 
TRP   CA  HA   sing N N 468 
TRP   C   O    doub N N 469 
TRP   C   OXT  sing N N 470 
TRP   CB  CG   sing N N 471 
TRP   CB  HB2  sing N N 472 
TRP   CB  HB3  sing N N 473 
TRP   CG  CD1  doub Y N 474 
TRP   CG  CD2  sing Y N 475 
TRP   CD1 NE1  sing Y N 476 
TRP   CD1 HD1  sing N N 477 
TRP   CD2 CE2  doub Y N 478 
TRP   CD2 CE3  sing Y N 479 
TRP   NE1 CE2  sing Y N 480 
TRP   NE1 HE1  sing N N 481 
TRP   CE2 CZ2  sing Y N 482 
TRP   CE3 CZ3  doub Y N 483 
TRP   CE3 HE3  sing N N 484 
TRP   CZ2 CH2  doub Y N 485 
TRP   CZ2 HZ2  sing N N 486 
TRP   CZ3 CH2  sing Y N 487 
TRP   CZ3 HZ3  sing N N 488 
TRP   CH2 HH2  sing N N 489 
TRP   OXT HXT  sing N N 490 
TYR   N   CA   sing N N 491 
TYR   N   H    sing N N 492 
TYR   N   H2   sing N N 493 
TYR   CA  C    sing N N 494 
TYR   CA  CB   sing N N 495 
TYR   CA  HA   sing N N 496 
TYR   C   O    doub N N 497 
TYR   C   OXT  sing N N 498 
TYR   CB  CG   sing N N 499 
TYR   CB  HB2  sing N N 500 
TYR   CB  HB3  sing N N 501 
TYR   CG  CD1  doub Y N 502 
TYR   CG  CD2  sing Y N 503 
TYR   CD1 CE1  sing Y N 504 
TYR   CD1 HD1  sing N N 505 
TYR   CD2 CE2  doub Y N 506 
TYR   CD2 HD2  sing N N 507 
TYR   CE1 CZ   doub Y N 508 
TYR   CE1 HE1  sing N N 509 
TYR   CE2 CZ   sing Y N 510 
TYR   CE2 HE2  sing N N 511 
TYR   CZ  OH   sing N N 512 
TYR   OH  HH   sing N N 513 
TYR   OXT HXT  sing N N 514 
VAL   N   CA   sing N N 515 
VAL   N   H    sing N N 516 
VAL   N   H2   sing N N 517 
VAL   CA  C    sing N N 518 
VAL   CA  CB   sing N N 519 
VAL   CA  HA   sing N N 520 
VAL   C   O    doub N N 521 
VAL   C   OXT  sing N N 522 
VAL   CB  CG1  sing N N 523 
VAL   CB  CG2  sing N N 524 
VAL   CB  HB   sing N N 525 
VAL   CG1 HG11 sing N N 526 
VAL   CG1 HG12 sing N N 527 
VAL   CG1 HG13 sing N N 528 
VAL   CG2 HG21 sing N N 529 
VAL   CG2 HG22 sing N N 530 
VAL   CG2 HG23 sing N N 531 
VAL   OXT HXT  sing N N 532 
# 
_pdbx_audit_support.funding_organization   'Italian Ministry of Education' 
_pdbx_audit_support.country                Italy 
_pdbx_audit_support.grant_number           'MUR project 404 FISR2019_00374 MeDyCa' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2V1D 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F0A 
_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]   0.008443 
_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]   0.005563 
_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]   0.004265 
_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 
P 
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   . PRO   A 1 49  ? -15.946 39.391  98.148  1.00 157.50 ?  171 PRO   A N   1 
ATOM   2    C CA  . PRO   A 1 49  ? -16.334 38.955  99.502  1.00 166.16 ?  171 PRO   A CA  1 
ATOM   3    C C   . PRO   A 1 49  ? -17.719 39.488  99.979  1.00 167.28 ?  171 PRO   A C   1 
ATOM   4    O O   . PRO   A 1 49  ? -18.378 40.250  99.235  1.00 160.76 ?  171 PRO   A O   1 
ATOM   5    C CB  . PRO   A 1 49  ? -15.177 39.483  100.379 1.00 148.09 ?  171 PRO   A CB  1 
ATOM   6    C CG  . PRO   A 1 49  ? -13.990 39.522  99.441  1.00 141.44 ?  171 PRO   A CG  1 
ATOM   7    C CD  . PRO   A 1 49  ? -14.572 39.929  98.103  1.00 143.04 ?  171 PRO   A CD  1 
ATOM   8    N N   . SER   A 1 50  ? -18.143 39.070  101.185 1.00 164.86 ?  172 SER   A N   1 
ATOM   9    C CA  . SER   A 1 50  ? -19.479 39.347  101.721 1.00 160.67 ?  172 SER   A CA  1 
ATOM   10   C C   . SER   A 1 50  ? -19.480 39.306  103.253 1.00 154.32 ?  172 SER   A C   1 
ATOM   11   O O   . SER   A 1 50  ? -18.717 38.555  103.879 1.00 149.67 ?  172 SER   A O   1 
ATOM   12   C CB  . SER   A 1 50  ? -20.515 38.354  101.167 1.00 161.96 ?  172 SER   A CB  1 
ATOM   13   O OG  . SER   A 1 50  ? -20.546 37.146  101.919 1.00 156.88 ?  172 SER   A OG  1 
ATOM   14   N N   . GLY   A 1 51  ? -20.361 40.114  103.842 1.00 147.01 ?  173 GLY   A N   1 
ATOM   15   C CA  . GLY   A 1 51  ? -20.554 40.176  105.279 1.00 143.75 ?  173 GLY   A CA  1 
ATOM   16   C C   . GLY   A 1 51  ? -20.050 41.474  105.883 1.00 137.49 ?  173 GLY   A C   1 
ATOM   17   O O   . GLY   A 1 51  ? -19.900 42.500  105.209 1.00 128.61 ?  173 GLY   A O   1 
ATOM   18   N N   . VAL   A 1 52  ? -19.802 41.426  107.197 1.00 138.61 ?  174 VAL   A N   1 
ATOM   19   C CA  . VAL   A 1 52  ? -18.986 42.467  107.814 1.00 128.70 ?  174 VAL   A CA  1 
ATOM   20   C C   . VAL   A 1 52  ? -17.657 42.566  107.089 1.00 130.21 ?  174 VAL   A C   1 
ATOM   21   O O   . VAL   A 1 52  ? -17.151 43.663  106.841 1.00 134.36 ?  174 VAL   A O   1 
ATOM   22   C CB  . VAL   A 1 52  ? -18.785 42.208  109.321 1.00 128.07 ?  174 VAL   A CB  1 
ATOM   23   C CG1 . VAL   A 1 52  ? -20.100 42.342  110.066 1.00 131.36 ?  174 VAL   A CG1 1 
ATOM   24   C CG2 . VAL   A 1 52  ? -18.169 40.836  109.562 1.00 131.10 ?  174 VAL   A CG2 1 
ATOM   25   N N   . GLU   A 1 53  ? -17.087 41.419  106.711 1.00 135.73 ?  175 GLU   A N   1 
ATOM   26   C CA  . GLU   A 1 53  ? -15.845 41.382  105.944 1.00 133.41 ?  175 GLU   A CA  1 
ATOM   27   C C   . GLU   A 1 53  ? -15.999 41.998  104.554 1.00 125.03 ?  175 GLU   A C   1 
ATOM   28   O O   . GLU   A 1 53  ? -15.007 42.454  103.974 1.00 114.80 ?  175 GLU   A O   1 
ATOM   29   C CB  . GLU   A 1 53  ? -15.384 39.935  105.809 1.00 136.01 ?  175 GLU   A CB  1 
ATOM   30   C CG  . GLU   A 1 53  ? -15.102 39.243  107.118 1.00 131.39 ?  175 GLU   A CG  1 
ATOM   31   C CD  . GLU   A 1 53  ? -15.224 37.745  106.974 1.00 143.68 ?  175 GLU   A CD  1 
ATOM   32   O OE1 . GLU   A 1 53  ? -15.481 37.278  105.838 1.00 148.12 ?  175 GLU   A OE1 1 
ATOM   33   O OE2 . GLU   A 1 53  ? -15.082 37.038  107.993 1.00 149.85 ?  175 GLU   A OE2 1 
ATOM   34   N N   . GLY   A 1 54  ? -17.214 42.001  104.006 1.00 126.44 ?  176 GLY   A N   1 
ATOM   35   C CA  . GLY   A 1 54  ? -17.413 42.558  102.683 1.00 126.24 ?  176 GLY   A CA  1 
ATOM   36   C C   . GLY   A 1 54  ? -17.175 44.049  102.663 1.00 118.82 ?  176 GLY   A C   1 
ATOM   37   O O   . GLY   A 1 54  ? -16.557 44.575  101.734 1.00 119.30 ?  176 GLY   A O   1 
ATOM   38   N N   . ALA   A 1 55  ? -17.654 44.746  103.694 1.00 120.06 ?  177 ALA   A N   1 
ATOM   39   C CA  . ALA   A 1 55  ? -17.362 46.168  103.841 1.00 115.69 ?  177 ALA   A CA  1 
ATOM   40   C C   . ALA   A 1 55  ? -15.865 46.419  103.934 1.00 111.18 ?  177 ALA   A C   1 
ATOM   41   O O   . ALA   A 1 55  ? -15.319 47.242  103.195 1.00 110.35 ?  177 ALA   A O   1 
ATOM   42   C CB  . ALA   A 1 55  ? -18.053 46.717  105.078 1.00 116.43 ?  177 ALA   A CB  1 
ATOM   43   N N   . ALA   A 1 56  ? -15.189 45.723  104.853 1.00 112.41 ?  178 ALA   A N   1 
ATOM   44   C CA  . ALA   A 1 56  ? -13.748 45.898  105.031 1.00 114.89 ?  178 ALA   A CA  1 
ATOM   45   C C   . ALA   A 1 56  ? -13.000 45.818  103.705 1.00 112.10 ?  178 ALA   A C   1 
ATOM   46   O O   . ALA   A 1 56  ? -12.085 46.610  103.444 1.00 104.72 ?  178 ALA   A O   1 
ATOM   47   C CB  . ALA   A 1 56  ? -13.203 44.852  106.007 1.00 111.71 ?  178 ALA   A CB  1 
ATOM   48   N N   . PHE   A 1 57  ? -13.377 44.879  102.846 1.00 115.20 ?  179 PHE   A N   1 
ATOM   49   C CA  . PHE   A 1 57  ? -12.679 44.810  101.575 1.00 114.74 ?  179 PHE   A CA  1 
ATOM   50   C C   . PHE   A 1 57  ? -13.166 45.910  100.620 1.00 115.18 ?  179 PHE   A C   1 
ATOM   51   O O   . PHE   A 1 57  ? -12.350 46.564  99.953  1.00 114.98 ?  179 PHE   A O   1 
ATOM   52   C CB  . PHE   A 1 57  ? -12.814 43.401  100.975 1.00 114.86 ?  179 PHE   A CB  1 
ATOM   53   C CG  . PHE   A 1 57  ? -12.613 43.369  99.506  1.00 116.08 ?  179 PHE   A CG  1 
ATOM   54   C CD1 . PHE   A 1 57  ? -13.681 43.548  98.634  1.00 118.71 ?  179 PHE   A CD1 1 
ATOM   55   C CD2 . PHE   A 1 57  ? -11.338 43.272  98.991  1.00 117.13 ?  179 PHE   A CD2 1 
ATOM   56   C CE1 . PHE   A 1 57  ? -13.487 43.580  97.263  1.00 115.67 ?  179 PHE   A CE1 1 
ATOM   57   C CE2 . PHE   A 1 57  ? -11.137 43.299  97.625  1.00 126.78 ?  179 PHE   A CE2 1 
ATOM   58   C CZ  . PHE   A 1 57  ? -12.216 43.454  96.757  1.00 117.82 ?  179 PHE   A CZ  1 
ATOM   59   N N   . GLN   A 1 58  ? -14.480 46.156  100.552 1.00 107.75 ?  180 GLN   A N   1 
ATOM   60   C CA  . GLN   A 1 58  ? -14.957 47.232  99.693  1.00 104.29 ?  180 GLN   A CA  1 
ATOM   61   C C   . GLN   A 1 58  ? -14.468 48.599  100.171 1.00 109.84 ?  180 GLN   A C   1 
ATOM   62   O O   . GLN   A 1 58  ? -14.513 49.576  99.409  1.00 112.38 ?  180 GLN   A O   1 
ATOM   63   C CB  . GLN   A 1 58  ? -16.488 47.165  99.595  1.00 104.63 ?  180 GLN   A CB  1 
ATOM   64   C CG  . GLN   A 1 58  ? -17.186 48.403  99.017  1.00 112.22 ?  180 GLN   A CG  1 
ATOM   65   C CD  . GLN   A 1 58  ? -16.733 48.759  97.588  1.00 114.90 ?  180 GLN   A CD  1 
ATOM   66   O OE1 . GLN   A 1 58  ? -16.572 47.874  96.735  1.00 113.74 ?  180 GLN   A OE1 1 
ATOM   67   N NE2 . GLN   A 1 58  ? -16.524 50.067  97.329  1.00 107.96 ?  180 GLN   A NE2 1 
ATOM   68   N N   . SER   A 1 59  ? -13.953 48.686  101.394 1.00 111.33 ?  181 SER   A N   1 
ATOM   69   C CA  . SER   A 1 59  ? -13.370 49.915  101.910 1.00 105.83 ?  181 SER   A CA  1 
ATOM   70   C C   . SER   A 1 59  ? -11.844 49.900  101.862 1.00 101.43 ?  181 SER   A C   1 
ATOM   71   O O   . SER   A 1 59  ? -11.211 50.821  102.379 1.00 106.46 ?  181 SER   A O   1 
ATOM   72   C CB  . SER   A 1 59  ? -13.857 50.168  103.343 1.00 103.75 ?  181 SER   A CB  1 
ATOM   73   O OG  . SER   A 1 59  ? -15.216 50.551  103.389 1.00 102.82 ?  181 SER   A OG  1 
ATOM   74   N N   . ARG   A 1 60  ? -11.246 48.863  101.279 1.00 98.20  ?  182 ARG   A N   1 
ATOM   75   C CA  . ARG   A 1 60  ? -9.802  48.754  101.098 1.00 91.93  ?  182 ARG   A CA  1 
ATOM   76   C C   . ARG   A 1 60  ? -9.057  48.486  102.412 1.00 94.35  ?  182 ARG   A C   1 
ATOM   77   O O   . ARG   A 1 60  ? -7.896  48.864  102.552 1.00 92.25  ?  182 ARG   A O   1 
ATOM   78   C CB  . ARG   A 1 60  ? -9.241  49.998  100.399 1.00 84.04  ?  182 ARG   A CB  1 
ATOM   79   C CG  . ARG   A 1 60  ? -9.920  50.326  99.086  1.00 87.57  ?  182 ARG   A CG  1 
ATOM   80   C CD  . ARG   A 1 60  ? -9.673  51.755  98.659  1.00 88.66  ?  182 ARG   A CD  1 
ATOM   81   N NE  . ARG   A 1 60  ? -10.305 52.724  99.547  1.00 93.16  ?  182 ARG   A NE  1 
ATOM   82   C CZ  . ARG   A 1 60  ? -11.610 52.971  99.601  1.00 97.99  ?  182 ARG   A CZ  1 
ATOM   83   N NH1 . ARG   A 1 60  ? -12.470 52.351  98.805  1.00 94.90  ?  182 ARG   A NH1 1 
ATOM   84   N NH2 . ARG   A 1 60  ? -12.066 53.866  100.478 1.00 100.70 ?  182 ARG   A NH2 1 
ATOM   85   N N   . LEU   A 1 61  ? -9.675  47.788  103.375 1.00 99.38  ?  183 LEU   A N   1 
ATOM   86   C CA  . LEU   A 1 61  ? -8.992  47.460  104.629 1.00 98.81  ?  183 LEU   A CA  1 
ATOM   87   C C   . LEU   A 1 61  ? -9.071  45.970  104.946 1.00 95.15  ?  183 LEU   A C   1 
ATOM   88   O O   . LEU   A 1 61  ? -10.125 45.352  104.774 1.00 96.60  ?  183 LEU   A O   1 
ATOM   89   C CB  . LEU   A 1 61  ? -9.583  48.237  105.820 1.00 102.64 ?  183 LEU   A CB  1 
ATOM   90   C CG  . LEU   A 1 61  ? -9.847  49.747  105.796 1.00 100.70 ?  183 LEU   A CG  1 
ATOM   91   C CD1 . LEU   A 1 61  ? -11.278 49.948  105.379 1.00 95.68  ?  183 LEU   A CD1 1 
ATOM   92   C CD2 . LEU   A 1 61  ? -9.538  50.441  107.145 1.00 110.59 ?  183 LEU   A CD2 1 
ATOM   93   N N   . PRO   A 1 62  ? -7.992  45.375  105.458 1.00 92.25  ?  184 PRO   A N   1 
ATOM   94   C CA  . PRO   A 1 62  ? -7.999  43.933  105.766 1.00 104.61 ?  184 PRO   A CA  1 
ATOM   95   C C   . PRO   A 1 62  ? -8.841  43.639  106.999 1.00 111.66 ?  184 PRO   A C   1 
ATOM   96   O O   . PRO   A 1 62  ? -8.467  44.026  108.107 1.00 114.31 ?  184 PRO   A O   1 
ATOM   97   C CB  . PRO   A 1 62  ? -6.519  43.620  106.020 1.00 104.66 ?  184 PRO   A CB  1 
ATOM   98   C CG  . PRO   A 1 62  ? -5.937  44.900  106.457 1.00 97.50  ?  184 PRO   A CG  1 
ATOM   99   C CD  . PRO   A 1 62  ? -6.707  46.003  105.780 1.00 95.05  ?  184 PRO   A CD  1 
ATOM   100  N N   . HIS   A 1 63  ? -9.946  42.893  106.819 1.00 116.03 ?  185 HIS   A N   1 
ATOM   101  C CA  . HIS   A 1 63  ? -10.968 42.677  107.854 1.00 113.13 ?  185 HIS   A CA  1 
ATOM   102  C C   . HIS   A 1 63  ? -10.486 42.015  109.146 1.00 111.84 ?  185 HIS   A C   1 
ATOM   103  O O   . HIS   A 1 63  ? -11.270 41.886  110.090 1.00 111.80 ?  185 HIS   A O   1 
ATOM   104  C CB  . HIS   A 1 63  ? -12.120 41.825  107.303 1.00 118.98 ?  185 HIS   A CB  1 
ATOM   105  C CG  . HIS   A 1 63  ? -11.731 40.409  106.982 1.00 125.41 ?  185 HIS   A CG  1 
ATOM   106  N ND1 . HIS   A 1 63  ? -11.393 39.489  107.952 1.00 121.18 ?  185 HIS   A ND1 1 
ATOM   107  C CD2 . HIS   A 1 63  ? -11.628 39.757  105.800 1.00 127.19 ?  185 HIS   A CD2 1 
ATOM   108  C CE1 . HIS   A 1 63  ? -11.096 38.335  107.384 1.00 119.44 ?  185 HIS   A CE1 1 
ATOM   109  N NE2 . HIS   A 1 63  ? -11.233 38.470  106.079 1.00 126.07 ?  185 HIS   A NE2 1 
ATOM   110  N N   . ASP   A 1 64  ? -9.225  41.578  109.210 1.00 110.28 ?  186 ASP   A N   1 
ATOM   111  C CA  . ASP   A 1 64  ? -8.756  40.806  110.356 1.00 109.27 ?  186 ASP   A CA  1 
ATOM   112  C C   . ASP   A 1 64  ? -7.376  41.237  110.839 1.00 110.40 ?  186 ASP   A C   1 
ATOM   113  O O   . ASP   A 1 64  ? -6.685  40.452  111.493 1.00 108.51 ?  186 ASP   A O   1 
ATOM   114  C CB  . ASP   A 1 64  ? -8.744  39.336  109.993 1.00 117.82 ?  186 ASP   A CB  1 
ATOM   115  C CG  . ASP   A 1 64  ? -7.942  39.069  108.737 1.00 123.14 ?  186 ASP   A CG  1 
ATOM   116  O OD1 . ASP   A 1 64  ? -7.553  40.059  108.082 1.00 123.26 ?  186 ASP   A OD1 1 
ATOM   117  O OD2 . ASP   A 1 64  ? -7.718  37.887  108.391 1.00 126.73 ?  186 ASP   A OD2 1 
ATOM   118  N N   . ARG   A 1 65  ? -6.960  42.454  110.514 1.00 115.56 ?  187 ARG   A N   1 
ATOM   119  C CA  . ARG   A 1 65  ? -5.728  43.069  110.988 1.00 118.47 ?  187 ARG   A CA  1 
ATOM   120  C C   . ARG   A 1 65  ? -6.023  44.541  111.259 1.00 115.83 ?  187 ARG   A C   1 
ATOM   121  O O   . ARG   A 1 65  ? -6.847  45.160  110.574 1.00 110.09 ?  187 ARG   A O   1 
ATOM   122  C CB  . ARG   A 1 65  ? -4.591  42.918  109.946 1.00 120.35 ?  187 ARG   A CB  1 
ATOM   123  C CG  . ARG   A 1 65  ? -3.156  42.871  110.497 1.00 126.79 ?  187 ARG   A CG  1 
ATOM   124  C CD  . ARG   A 1 65  ? -2.121  42.480  109.402 1.00 134.08 ?  187 ARG   A CD  1 
ATOM   125  N NE  . ARG   A 1 65  ? -1.927  43.482  108.350 1.00 139.97 ?  187 ARG   A NE  1 
ATOM   126  C CZ  . ARG   A 1 65  ? -2.496  43.453  107.146 1.00 132.92 ?  187 ARG   A CZ  1 
ATOM   127  N NH1 . ARG   A 1 65  ? -3.368  42.511  106.812 1.00 124.89 ?  187 ARG   A NH1 1 
ATOM   128  N NH2 . ARG   A 1 65  ? -2.183  44.396  106.255 1.00 123.60 ?  187 ARG   A NH2 1 
ATOM   129  N N   . MET   A 1 66  ? -5.376  45.108  112.269 1.00 111.25 ?  188 MET   A N   1 
ATOM   130  C CA  . MET   A 1 66  ? -5.448  46.554  112.414 1.00 106.94 ?  188 MET   A CA  1 
ATOM   131  C C   . MET   A 1 66  ? -4.431  47.164  111.449 1.00 106.40 ?  188 MET   A C   1 
ATOM   132  O O   . MET   A 1 66  ? -3.289  46.675  111.376 1.00 101.91 ?  188 MET   A O   1 
ATOM   133  C CB  . MET   A 1 66  ? -5.176  46.966  113.864 1.00 105.11 ?  188 MET   A CB  1 
ATOM   134  C CG  . MET   A 1 66  ? -6.315  46.704  114.850 1.00 102.61 ?  188 MET   A CG  1 
ATOM   135  S SD  . MET   A 1 66  ? -5.971  47.205  116.574 1.00 107.83 ?  188 MET   A SD  1 
ATOM   136  C CE  . MET   A 1 66  ? -6.548  48.887  116.609 1.00 105.42 ?  188 MET   A CE  1 
ATOM   137  N N   . THR   A 1 67  ? -4.856  48.199  110.679 1.00 101.74 ?  189 THR   A N   1 
ATOM   138  C CA  . THR   A 1 67  ? -3.975  48.858  109.702 1.00 100.84 ?  189 THR   A CA  1 
ATOM   139  C C   . THR   A 1 67  ? -3.006  49.787  110.419 1.00 95.73  ?  189 THR   A C   1 
ATOM   140  O O   . THR   A 1 67  ? -3.253  50.231  111.537 1.00 96.19  ?  189 THR   A O   1 
ATOM   141  C CB  . THR   A 1 67  ? -4.733  49.670  108.612 1.00 98.76  ?  189 THR   A CB  1 
ATOM   142  O OG1 . THR   A 1 67  ? -5.328  50.862  109.140 1.00 104.27 ?  189 THR   A OG1 1 
ATOM   143  C CG2 . THR   A 1 67  ? -5.818  48.871  107.948 1.00 95.92  ?  189 THR   A CG2 1 
ATOM   144  N N   . SER   A 1 68  ? -1.888  50.086  109.758 1.00 97.87  ?  190 SER   A N   1 
ATOM   145  C CA  . SER   A 1 68  ? -0.893  50.971  110.367 1.00 104.97 ?  190 SER   A CA  1 
ATOM   146  C C   . SER   A 1 68  ? -1.492  52.308  110.817 1.00 99.79  ?  190 SER   A C   1 
ATOM   147  O O   . SER   A 1 68  ? -1.073  52.864  111.843 1.00 93.18  ?  190 SER   A O   1 
ATOM   148  C CB  . SER   A 1 68  ? 0.266   51.192  109.383 1.00 115.04 ?  190 SER   A CB  1 
ATOM   149  O OG  . SER   A 1 68  ? 1.275   52.039  109.917 1.00 108.79 ?  190 SER   A OG  1 
ATOM   150  N N   . GLN   A 1 69  ? -2.474  52.830  110.068 1.00 98.31  ?  191 GLN   A N   1 
ATOM   151  C CA  . GLN   A 1 69  ? -3.191  54.034  110.483 1.00 101.72 ?  191 GLN   A CA  1 
ATOM   152  C C   . GLN   A 1 69  ? -3.992  53.812  111.767 1.00 98.72  ?  191 GLN   A C   1 
ATOM   153  O O   . GLN   A 1 69  ? -3.892  54.591  112.723 1.00 93.22  ?  191 GLN   A O   1 
ATOM   154  C CB  . GLN   A 1 69  ? -4.108  54.495  109.354 1.00 104.72 ?  191 GLN   A CB  1 
ATOM   155  C CG  . GLN   A 1 69  ? -5.013  55.658  109.755 1.00 109.40 ?  191 GLN   A CG  1 
ATOM   156  C CD  . GLN   A 1 69  ? -5.565  56.451  108.566 1.00 115.89 ?  191 GLN   A CD  1 
ATOM   157  O OE1 . GLN   A 1 69  ? -5.515  56.011  107.413 1.00 132.66 ?  191 GLN   A OE1 1 
ATOM   158  N NE2 . GLN   A 1 69  ? -6.135  57.606  108.855 1.00 112.86 ?  191 GLN   A NE2 1 
ATOM   159  N N   . GLU   A 1 70  ? -4.813  52.768  111.797 1.00 99.94  ?  192 GLU   A N   1 
ATOM   160  C CA  . GLU   A 1 70  ? -5.592  52.472  112.991 1.00 95.20  ?  192 GLU   A CA  1 
ATOM   161  C C   . GLU   A 1 70  ? -4.709  52.198  114.196 1.00 92.37  ?  192 GLU   A C   1 
ATOM   162  O O   . GLU   A 1 70  ? -5.125  52.433  115.331 1.00 94.86  ?  192 GLU   A O   1 
ATOM   163  C CB  . GLU   A 1 70  ? -6.487  51.270  112.743 1.00 98.79  ?  192 GLU   A CB  1 
ATOM   164  C CG  . GLU   A 1 70  ? -7.687  51.560  111.903 1.00 99.85  ?  192 GLU   A CG  1 
ATOM   165  C CD  . GLU   A 1 70  ? -8.202  50.344  111.173 1.00 100.29 ?  192 GLU   A CD  1 
ATOM   166  O OE1 . GLU   A 1 70  ? -7.524  49.281  111.200 1.00 100.17 ?  192 GLU   A OE1 1 
ATOM   167  O OE2 . GLU   A 1 70  ? -9.305  50.463  110.594 1.00 98.35  ?  192 GLU   A OE2 1 
ATOM   168  N N   . ALA   A 1 71  ? -3.514  51.657  113.988 1.00 92.91  ?  193 ALA   A N   1 
ATOM   169  C CA  . ALA   A 1 71  ? -2.597  51.504  115.109 1.00 96.26  ?  193 ALA   A CA  1 
ATOM   170  C C   . ALA   A 1 71  ? -2.258  52.858  115.703 1.00 99.78  ?  193 ALA   A C   1 
ATOM   171  O O   . ALA   A 1 71  ? -2.160  53.010  116.926 1.00 101.52 ?  193 ALA   A O   1 
ATOM   172  C CB  . ALA   A 1 71  ? -1.316  50.794  114.672 1.00 97.28  ?  193 ALA   A CB  1 
ATOM   173  N N   . ALA   A 1 72  ? -2.082  53.859  114.851 1.00 98.18  ?  194 ALA   A N   1 
ATOM   174  C CA  . ALA   A 1 72  ? -1.650  55.142  115.363 1.00 98.16  ?  194 ALA   A CA  1 
ATOM   175  C C   . ALA   A 1 72  ? -2.763  55.874  116.092 1.00 97.08  ?  194 ALA   A C   1 
ATOM   176  O O   . ALA   A 1 72  ? -2.475  56.681  116.974 1.00 100.30 ?  194 ALA   A O   1 
ATOM   177  C CB  . ALA   A 1 72  ? -1.117  55.990  114.225 1.00 104.48 ?  194 ALA   A CB  1 
ATOM   178  N N   . CYS   A 1 73  ? -4.021  55.624  115.740 1.00 94.87  ?  195 CYS   A N   1 
ATOM   179  C CA  . CYS   A 1 73  ? -5.123  56.199  116.496 1.00 96.94  ?  195 CYS   A CA  1 
ATOM   180  C C   . CYS   A 1 73  ? -5.562  55.342  117.670 1.00 99.58  ?  195 CYS   A C   1 
ATOM   181  O O   . CYS   A 1 73  ? -6.029  55.882  118.676 1.00 110.10 ?  195 CYS   A O   1 
ATOM   182  C CB  . CYS   A 1 73  ? -6.332  56.421  115.603 1.00 100.72 ?  195 CYS   A CB  1 
ATOM   183  S SG  . CYS   A 1 73  ? -5.956  57.287  114.158 1.00 110.93 ?  195 CYS   A SG  1 
ATOM   184  N N   . PHE   A 1 74  ? -5.431  54.038  117.584 1.00 95.36  ?  196 PHE   A N   1 
ATOM   185  C CA  . PHE   A 1 74  ? -5.927  53.210  118.669 1.00 95.46  ?  196 PHE   A CA  1 
ATOM   186  C C   . PHE   A 1 74  ? -4.772  52.427  119.287 1.00 97.90  ?  196 PHE   A C   1 
ATOM   187  O O   . PHE   A 1 74  ? -4.889  51.217  119.502 1.00 95.44  ?  196 PHE   A O   1 
ATOM   188  C CB  . PHE   A 1 74  ? -7.021  52.284  118.143 1.00 94.17  ?  196 PHE   A CB  1 
ATOM   189  C CG  . PHE   A 1 74  ? -8.241  53.006  117.614 1.00 95.62  ?  196 PHE   A CG  1 
ATOM   190  C CD1 . PHE   A 1 74  ? -8.185  53.743  116.449 1.00 98.65  ?  196 PHE   A CD1 1 
ATOM   191  C CD2 . PHE   A 1 74  ? -9.464  52.860  118.222 1.00 100.13 ?  196 PHE   A CD2 1 
ATOM   192  C CE1 . PHE   A 1 74  ? -9.309  54.387  115.946 1.00 99.25  ?  196 PHE   A CE1 1 
ATOM   193  C CE2 . PHE   A 1 74  ? -10.597 53.493  117.715 1.00 101.67 ?  196 PHE   A CE2 1 
ATOM   194  C CZ  . PHE   A 1 74  ? -10.515 54.252  116.580 1.00 99.08  ?  196 PHE   A CZ  1 
ATOM   195  N N   . PRO   A 1 75  ? -3.649  53.076  119.615 1.00 99.05  ?  197 PRO   A N   1 
ATOM   196  C CA  . PRO   A 1 75  ? -2.474  52.323  120.063 1.00 101.61 ?  197 PRO   A CA  1 
ATOM   197  C C   . PRO   A 1 75  ? -2.616  51.765  121.446 1.00 101.10 ?  197 PRO   A C   1 
ATOM   198  O O   . PRO   A 1 75  ? -1.641  51.224  121.972 1.00 104.54 ?  197 PRO   A O   1 
ATOM   199  C CB  . PRO   A 1 75  ? -1.360  53.368  120.040 1.00 100.99 ?  197 PRO   A CB  1 
ATOM   200  C CG  . PRO   A 1 75  ? -2.036  54.587  120.310 1.00 94.91  ?  197 PRO   A CG  1 
ATOM   201  C CD  . PRO   A 1 75  ? -3.418  54.517  119.766 1.00 93.14  ?  197 PRO   A CD  1 
ATOM   202  N N   . ASP   A 1 76  ? -3.770  51.944  122.075 1.00 99.33  ?  198 ASP   A N   1 
ATOM   203  C CA  . ASP   A 1 76  ? -4.087  51.142  123.245 1.00 106.64 ?  198 ASP   A CA  1 
ATOM   204  C C   . ASP   A 1 76  ? -4.540  49.754  122.811 1.00 110.26 ?  198 ASP   A C   1 
ATOM   205  O O   . ASP   A 1 76  ? -4.099  48.744  123.374 1.00 117.80 ?  198 ASP   A O   1 
ATOM   206  C CB  . ASP   A 1 76  ? -5.174  51.825  124.067 1.00 102.16 ?  198 ASP   A CB  1 
ATOM   207  C CG  . ASP   A 1 76  ? -6.359  52.218  123.215 1.00 107.52 ?  198 ASP   A CG  1 
ATOM   208  O OD1 . ASP   A 1 76  ? -6.202  53.085  122.339 1.00 108.36 ?  198 ASP   A OD1 1 
ATOM   209  O OD2 . ASP   A 1 76  ? -7.450  51.650  123.400 1.00 114.60 ?  198 ASP   A OD2 1 
ATOM   210  N N   . ILE   A 1 77  ? -5.384  49.694  121.779 1.00 100.56 ?  199 ILE   A N   1 
ATOM   211  C CA  . ILE   A 1 77  ? -5.996  48.436  121.376 1.00 102.84 ?  199 ILE   A CA  1 
ATOM   212  C C   . ILE   A 1 77  ? -4.960  47.490  120.772 1.00 108.54 ?  199 ILE   A C   1 
ATOM   213  O O   . ILE   A 1 77  ? -4.780  46.355  121.239 1.00 113.94 ?  199 ILE   A O   1 
ATOM   214  C CB  . ILE   A 1 77  ? -7.152  48.734  120.415 1.00 95.63  ?  199 ILE   A CB  1 
ATOM   215  C CG1 . ILE   A 1 77  ? -8.193  49.526  121.182 1.00 87.53  ?  199 ILE   A CG1 1 
ATOM   216  C CG2 . ILE   A 1 77  ? -7.674  47.470  119.761 1.00 100.41 ?  199 ILE   A CG2 1 
ATOM   217  C CD1 . ILE   A 1 77  ? -9.512  49.393  120.635 1.00 92.80  ?  199 ILE   A CD1 1 
ATOM   218  N N   . ILE   A 1 78  ? -4.241  47.957  119.749 1.00 105.62 ?  200 ILE   A N   1 
ATOM   219  C CA  . ILE   A 1 78  ? -3.289  47.127  119.033 1.00 99.85  ?  200 ILE   A CA  1 
ATOM   220  C C   . ILE   A 1 78  ? -2.129  46.655  119.894 1.00 102.86 ?  200 ILE   A C   1 
ATOM   221  O O   . ILE   A 1 78  ? -1.435  45.718  119.507 1.00 109.52 ?  200 ILE   A O   1 
ATOM   222  C CB  . ILE   A 1 78  ? -2.744  47.881  117.813 1.00 99.22  ?  200 ILE   A CB  1 
ATOM   223  C CG1 . ILE   A 1 78  ? -2.433  46.900  116.714 1.00 96.30  ?  200 ILE   A CG1 1 
ATOM   224  C CG2 . ILE   A 1 78  ? -1.484  48.661  118.157 1.00 103.64 ?  200 ILE   A CG2 1 
ATOM   225  C CD1 . ILE   A 1 78  ? -1.899  47.525  115.517 1.00 98.24  ?  200 ILE   A CD1 1 
ATOM   226  N N   . SER   A 1 79  ? -1.861  47.276  121.034 1.00 104.08 ?  201 SER   A N   1 
ATOM   227  C CA  . SER   A 1 79  ? -0.774  46.788  121.874 1.00 109.89 ?  201 SER   A CA  1 
ATOM   228  C C   . SER   A 1 79  ? -1.265  45.823  122.933 1.00 118.85 ?  201 SER   A C   1 
ATOM   229  O O   . SER   A 1 79  ? -0.445  45.204  123.632 1.00 118.23 ?  201 SER   A O   1 
ATOM   230  C CB  . SER   A 1 79  ? -0.056  47.950  122.560 1.00 108.44 ?  201 SER   A CB  1 
ATOM   231  O OG  . SER   A 1 79  ? -0.825  48.453  123.644 1.00 109.14 ?  201 SER   A OG  1 
ATOM   232  N N   . GLY   A 1 80  ? -2.581  45.693  123.052 1.00 117.48 ?  202 GLY   A N   1 
ATOM   233  C CA  . GLY   A 1 80  ? -3.183  45.023  124.161 1.00 122.57 ?  202 GLY   A CA  1 
ATOM   234  C C   . GLY   A 1 80  ? -3.541  43.606  123.815 1.00 128.80 ?  202 GLY   A C   1 
ATOM   235  O O   . GLY   A 1 80  ? -2.736  42.841  123.271 1.00 130.19 ?  202 GLY   A O   1 
ATOM   236  N N   . PRO   A 1 81  ? -4.762  43.237  124.129 1.00 131.98 ?  203 PRO   A N   1 
ATOM   237  C CA  . PRO   A 1 81  ? -5.136  41.823  124.107 1.00 132.97 ?  203 PRO   A CA  1 
ATOM   238  C C   . PRO   A 1 81  ? -5.814  41.455  122.803 1.00 132.76 ?  203 PRO   A C   1 
ATOM   239  O O   . PRO   A 1 81  ? -6.610  42.243  122.273 1.00 128.32 ?  203 PRO   A O   1 
ATOM   240  C CB  . PRO   A 1 81  ? -6.101  41.712  125.286 1.00 129.81 ?  203 PRO   A CB  1 
ATOM   241  C CG  . PRO   A 1 81  ? -6.751  43.046  125.305 1.00 130.12 ?  203 PRO   A CG  1 
ATOM   242  C CD  . PRO   A 1 81  ? -5.714  44.046  124.903 1.00 132.56 ?  203 PRO   A CD  1 
ATOM   243  N N   . GLN   A 1 82  ? -5.509  40.253  122.293 1.00 134.34 ?  204 GLN   A N   1 
ATOM   244  C CA  . GLN   A 1 82  ? -6.061  39.810  121.015 1.00 134.32 ?  204 GLN   A CA  1 
ATOM   245  C C   . GLN   A 1 82  ? -7.577  39.912  121.004 1.00 131.58 ?  204 GLN   A C   1 
ATOM   246  O O   . GLN   A 1 82  ? -8.190  40.090  119.943 1.00 126.69 ?  204 GLN   A O   1 
ATOM   247  C CB  . GLN   A 1 82  ? -5.629  38.369  120.730 1.00 139.38 ?  204 GLN   A CB  1 
ATOM   248  C CG  . GLN   A 1 82  ? -4.245  38.239  120.113 1.00 137.87 ?  204 GLN   A CG  1 
ATOM   249  C CD  . GLN   A 1 82  ? -4.050  39.126  118.895 1.00 139.64 ?  204 GLN   A CD  1 
ATOM   250  O OE1 . GLN   A 1 82  ? -4.906  39.185  117.993 1.00 137.85 ?  204 GLN   A OE1 1 
ATOM   251  N NE2 . GLN   A 1 82  ? -2.915  39.827  118.860 1.00 136.39 ?  204 GLN   A NE2 1 
ATOM   252  N N   . GLN   A 1 83  ? -8.191  39.806  122.182 1.00 133.81 ?  205 GLN   A N   1 
ATOM   253  C CA  . GLN   A 1 83  ? -9.635  39.929  122.292 1.00 134.74 ?  205 GLN   A CA  1 
ATOM   254  C C   . GLN   A 1 83  ? -10.096 41.309  121.844 1.00 127.56 ?  205 GLN   A C   1 
ATOM   255  O O   . GLN   A 1 83  ? -10.923 41.435  120.931 1.00 121.32 ?  205 GLN   A O   1 
ATOM   256  C CB  . GLN   A 1 83  ? -10.066 39.634  123.733 1.00 136.39 ?  205 GLN   A CB  1 
ATOM   257  C CG  . GLN   A 1 83  ? -11.568 39.444  123.919 1.00 140.25 ?  205 GLN   A CG  1 
ATOM   258  C CD  . GLN   A 1 83  ? -12.268 38.954  122.657 1.00 147.69 ?  205 GLN   A CD  1 
ATOM   259  O OE1 . GLN   A 1 83  ? -11.997 37.852  122.165 1.00 155.01 ?  205 GLN   A OE1 1 
ATOM   260  N NE2 . GLN   A 1 83  ? -13.136 39.793  122.099 1.00 140.11 ?  205 GLN   A NE2 1 
ATOM   261  N N   . THR   A 1 84  ? -9.536  42.359  122.459 1.00 127.91 ?  206 THR   A N   1 
ATOM   262  C CA  . THR   A 1 84  ? -10.000 43.717  122.186 1.00 127.97 ?  206 THR   A CA  1 
ATOM   263  C C   . THR   A 1 84  ? -9.774  44.111  120.735 1.00 123.50 ?  206 THR   A C   1 
ATOM   264  O O   . THR   A 1 84  ? -10.611 44.805  120.148 1.00 118.51 ?  206 THR   A O   1 
ATOM   265  C CB  . THR   A 1 84  ? -9.321  44.722  123.107 1.00 126.46 ?  206 THR   A CB  1 
ATOM   266  O OG1 . THR   A 1 84  ? -9.404  44.253  124.453 1.00 132.58 ?  206 THR   A OG1 1 
ATOM   267  C CG2 . THR   A 1 84  ? -10.039 46.049  123.020 1.00 121.36 ?  206 THR   A CG2 1 
ATOM   268  N N   . GLN   A 1 85  ? -8.647  43.686  120.142 1.00 124.62 ?  207 GLN   A N   1 
ATOM   269  C CA  . GLN   A 1 85  ? -8.436  43.914  118.712 1.00 119.44 ?  207 GLN   A CA  1 
ATOM   270  C C   . GLN   A 1 85  ? -9.586  43.349  117.896 1.00 117.34 ?  207 GLN   A C   1 
ATOM   271  O O   . GLN   A 1 85  ? -10.036 43.967  116.926 1.00 115.51 ?  207 GLN   A O   1 
ATOM   272  C CB  . GLN   A 1 85  ? -7.125  43.290  118.235 1.00 111.52 ?  207 GLN   A CB  1 
ATOM   273  C CG  . GLN   A 1 85  ? -5.933  43.509  119.135 1.00 118.19 ?  207 GLN   A CG  1 
ATOM   274  C CD  . GLN   A 1 85  ? -4.640  43.236  118.410 1.00 113.40 ?  207 GLN   A CD  1 
ATOM   275  O OE1 . GLN   A 1 85  ? -4.658  42.920  117.226 1.00 113.22 ?  207 GLN   A OE1 1 
ATOM   276  N NE2 . GLN   A 1 85  ? -3.516  43.281  119.127 1.00 111.95 ?  207 GLN   A NE2 1 
ATOM   277  N N   . LYS   A 1 86  ? -10.086 42.178  118.279 1.00 121.19 ?  208 LYS   A N   1 
ATOM   278  C CA  . LYS   A 1 86  ? -11.148 41.569  117.492 1.00 124.82 ?  208 LYS   A CA  1 
ATOM   279  C C   . LYS   A 1 86  ? -12.477 42.283  117.724 1.00 120.45 ?  208 LYS   A C   1 
ATOM   280  O O   . LYS   A 1 86  ? -13.264 42.474  116.781 1.00 112.21 ?  208 LYS   A O   1 
ATOM   281  C CB  . LYS   A 1 86  ? -11.220 40.073  117.810 1.00 131.28 ?  208 LYS   A CB  1 
ATOM   282  C CG  . LYS   A 1 86  ? -10.007 39.307  117.251 1.00 132.36 ?  208 LYS   A CG  1 
ATOM   283  C CD  . LYS   A 1 86  ? -10.162 37.795  117.315 1.00 135.98 ?  208 LYS   A CD  1 
ATOM   284  C CE  . LYS   A 1 86  ? -8.803  37.113  117.172 1.00 136.08 ?  208 LYS   A CE  1 
ATOM   285  N NZ  . LYS   A 1 86  ? -8.891  35.646  117.426 1.00 137.87 ?  208 LYS   A NZ  1 
ATOM   286  N N   . VAL   A 1 87  ? -12.732 42.697  118.969 1.00 121.10 ?  209 VAL   A N   1 
ATOM   287  C CA  . VAL   A 1 87  ? -13.862 43.563  119.286 1.00 123.24 ?  209 VAL   A CA  1 
ATOM   288  C C   . VAL   A 1 87  ? -13.836 44.729  118.310 1.00 124.58 ?  209 VAL   A C   1 
ATOM   289  O O   . VAL   A 1 87  ? -14.709 44.869  117.444 1.00 123.55 ?  209 VAL   A O   1 
ATOM   290  C CB  . VAL   A 1 87  ? -13.792 44.093  120.731 1.00 119.77 ?  209 VAL   A CB  1 
ATOM   291  C CG1 . VAL   A 1 87  ? -15.107 44.752  121.097 1.00 117.98 ?  209 VAL   A CG1 1 
ATOM   292  C CG2 . VAL   A 1 87  ? -13.427 43.001  121.699 1.00 121.87 ?  209 VAL   A CG2 1 
ATOM   293  N N   . PHE   A 1 88  ? -12.807 45.562  118.460 1.00 122.73 ?  210 PHE   A N   1 
ATOM   294  C CA  . PHE   A 1 88  ? -12.592 46.727  117.615 1.00 115.33 ?  210 PHE   A CA  1 
ATOM   295  C C   . PHE   A 1 88  ? -12.803 46.411  116.144 1.00 112.48 ?  210 PHE   A C   1 
ATOM   296  O O   . PHE   A 1 88  ? -13.606 47.054  115.457 1.00 108.98 ?  210 PHE   A O   1 
ATOM   297  C CB  . PHE   A 1 88  ? -11.168 47.230  117.860 1.00 111.01 ?  210 PHE   A CB  1 
ATOM   298  C CG  . PHE   A 1 88  ? -10.618 48.020  116.741 1.00 110.10 ?  210 PHE   A CG  1 
ATOM   299  C CD1 . PHE   A 1 88  ? -11.026 49.324  116.548 1.00 111.46 ?  210 PHE   A CD1 1 
ATOM   300  C CD2 . PHE   A 1 88  ? -9.714  47.461  115.863 1.00 110.88 ?  210 PHE   A CD2 1 
ATOM   301  C CE1 . PHE   A 1 88  ? -10.536 50.057  115.520 1.00 105.87 ?  210 PHE   A CE1 1 
ATOM   302  C CE2 . PHE   A 1 88  ? -9.233  48.188  114.814 1.00 108.60 ?  210 PHE   A CE2 1 
ATOM   303  C CZ  . PHE   A 1 88  ? -9.635  49.487  114.646 1.00 109.10 ?  210 PHE   A CZ  1 
ATOM   304  N N   . LEU   A 1 89  ? -12.088 45.393  115.662 1.00 113.14 ?  211 LEU   A N   1 
ATOM   305  C CA  . LEU   A 1 89  ? -12.093 45.063  114.246 1.00 109.79 ?  211 LEU   A CA  1 
ATOM   306  C C   . LEU   A 1 89  ? -13.494 44.774  113.737 1.00 115.21 ?  211 LEU   A C   1 
ATOM   307  O O   . LEU   A 1 89  ? -13.797 45.088  112.581 1.00 112.56 ?  211 LEU   A O   1 
ATOM   308  C CB  . LEU   A 1 89  ? -11.141 43.894  114.001 1.00 106.13 ?  211 LEU   A CB  1 
ATOM   309  C CG  . LEU   A 1 89  ? -9.720  44.378  113.738 1.00 104.82 ?  211 LEU   A CG  1 
ATOM   310  C CD1 . LEU   A 1 89  ? -8.635  43.366  113.989 1.00 105.78 ?  211 LEU   A CD1 1 
ATOM   311  C CD2 . LEU   A 1 89  ? -9.712  44.729  112.282 1.00 109.87 ?  211 LEU   A CD2 1 
ATOM   312  N N   . PHE   A 1 90  ? -14.370 44.201  114.577 1.00 119.53 ?  212 PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 90  ? -15.776 44.070  114.189 1.00 122.11 ?  212 PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 90  ? -16.448 45.441  114.117 1.00 115.93 ?  212 PHE   A C   1 
ATOM   315  O O   . PHE   A 1 90  ? -17.161 45.757  113.154 1.00 112.80 ?  212 PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 90  ? -16.530 43.145  115.164 1.00 122.33 ?  212 PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 90  ? -18.020 42.966  114.835 1.00 127.44 ?  212 PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 90  ? -18.952 43.967  115.121 1.00 127.65 ?  212 PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 90  ? -18.489 41.789  114.273 1.00 131.00 ?  212 PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 90  ? -20.309 43.811  114.826 1.00 127.65 ?  212 PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 90  ? -19.849 41.630  113.979 1.00 134.04 ?  212 PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 90  ? -20.755 42.647  114.257 1.00 129.59 ?  212 PHE   A CZ  1 
ATOM   323  N N   . ILE   A 1 91  ? -16.243 46.265  115.138 1.00 113.35 ?  213 ILE   A N   1 
ATOM   324  C CA  . ILE   A 1 91  ? -16.969 47.522  115.196 1.00 115.22 ?  213 ILE   A CA  1 
ATOM   325  C C   . ILE   A 1 91  ? -16.628 48.366  113.977 1.00 112.41 ?  213 ILE   A C   1 
ATOM   326  O O   . ILE   A 1 91  ? -17.506 48.979  113.358 1.00 107.81 ?  213 ILE   A O   1 
ATOM   327  C CB  . ILE   A 1 91  ? -16.654 48.236  116.523 1.00 115.24 ?  213 ILE   A CB  1 
ATOM   328  C CG1 . ILE   A 1 91  ? -16.861 47.266  117.687 1.00 112.00 ?  213 ILE   A CG1 1 
ATOM   329  C CG2 . ILE   A 1 91  ? -17.597 49.396  116.724 1.00 111.03 ?  213 ILE   A CG2 1 
ATOM   330  C CD1 . ILE   A 1 91  ? -16.117 47.632  118.915 1.00 110.23 ?  213 ILE   A CD1 1 
ATOM   331  N N   . ARG   A 1 92  ? -15.349 48.353  113.583 1.00 113.88 ?  214 ARG   A N   1 
ATOM   332  C CA  . ARG   A 1 92  ? -14.899 49.016  112.361 1.00 111.69 ?  214 ARG   A CA  1 
ATOM   333  C C   . ARG   A 1 92  ? -15.618 48.466  111.137 1.00 113.57 ?  214 ARG   A C   1 
ATOM   334  O O   . ARG   A 1 92  ? -16.258 49.213  110.381 1.00 109.22 ?  214 ARG   A O   1 
ATOM   335  C CB  . ARG   A 1 92  ? -13.385 48.834  112.199 1.00 105.42 ?  214 ARG   A CB  1 
ATOM   336  C CG  . ARG   A 1 92  ? -12.792 49.615  111.030 1.00 101.34 ?  214 ARG   A CG  1 
ATOM   337  C CD  . ARG   A 1 92  ? -12.187 48.724  109.973 1.00 100.87 ?  214 ARG   A CD  1 
ATOM   338  N NE  . ARG   A 1 92  ? -10.795 48.389  110.236 1.00 104.76 ?  214 ARG   A NE  1 
ATOM   339  C CZ  . ARG   A 1 92  ? -10.216 47.281  109.798 1.00 101.93 ?  214 ARG   A CZ  1 
ATOM   340  N NH1 . ARG   A 1 92  ? -10.878 46.419  109.052 1.00 104.31 ?  214 ARG   A NH1 1 
ATOM   341  N NH2 . ARG   A 1 92  ? -8.945  47.032  110.118 1.00 96.04  ?  214 ARG   A NH2 1 
ATOM   342  N N   . ASN   A 1 93  ? -15.475 47.151  110.906 1.00 114.82 ?  215 ASN   A N   1 
ATOM   343  C CA  . ASN   A 1 93  ? -16.110 46.500  109.766 1.00 110.27 ?  215 ASN   A CA  1 
ATOM   344  C C   . ASN   A 1 93  ? -17.601 46.755  109.773 1.00 115.61 ?  215 ASN   A C   1 
ATOM   345  O O   . ASN   A 1 93  ? -18.192 47.122  108.749 1.00 116.25 ?  215 ASN   A O   1 
ATOM   346  C CB  . ASN   A 1 93  ? -15.843 44.998  109.794 1.00 111.98 ?  215 ASN   A CB  1 
ATOM   347  C CG  . ASN   A 1 93  ? -14.380 44.674  109.721 1.00 116.05 ?  215 ASN   A CG  1 
ATOM   348  O OD1 . ASN   A 1 93  ? -13.563 45.552  109.438 1.00 113.20 ?  215 ASN   A OD1 1 
ATOM   349  N ND2 . ASN   A 1 93  ? -14.034 43.400  109.939 1.00 116.26 ?  215 ASN   A ND2 1 
ATOM   350  N N   . ARG   A 1 94  ? -18.220 46.589  110.941 1.00 115.88 ?  216 ARG   A N   1 
ATOM   351  C CA  . ARG   A 1 94  ? -19.665 46.712  111.038 1.00 116.89 ?  216 ARG   A CA  1 
ATOM   352  C C   . ARG   A 1 94  ? -20.129 48.097  110.599 1.00 115.97 ?  216 ARG   A C   1 
ATOM   353  O O   . ARG   A 1 94  ? -21.100 48.222  109.840 1.00 114.31 ?  216 ARG   A O   1 
ATOM   354  C CB  . ARG   A 1 94  ? -20.091 46.384  112.470 1.00 118.11 ?  216 ARG   A CB  1 
ATOM   355  C CG  . ARG   A 1 94  ? -21.577 46.291  112.677 1.00 120.53 ?  216 ARG   A CG  1 
ATOM   356  C CD  . ARG   A 1 94  ? -22.270 45.387  111.683 1.00 119.63 ?  216 ARG   A CD  1 
ATOM   357  N NE  . ARG   A 1 94  ? -23.708 45.468  111.901 1.00 121.10 ?  216 ARG   A NE  1 
ATOM   358  C CZ  . ARG   A 1 94  ? -24.566 45.996  111.038 1.00 121.22 ?  216 ARG   A CZ  1 
ATOM   359  N NH1 . ARG   A 1 94  ? -24.176 46.429  109.855 1.00 121.69 ?  216 ARG   A NH1 1 
ATOM   360  N NH2 . ARG   A 1 94  ? -25.847 46.104  111.378 1.00 125.66 ?  216 ARG   A NH2 1 
ATOM   361  N N   . THR   A 1 95  ? -19.414 49.148  111.021 1.00 117.37 ?  217 THR   A N   1 
ATOM   362  C CA  . THR   A 1 95  ? -19.834 50.512  110.701 1.00 115.99 ?  217 THR   A CA  1 
ATOM   363  C C   . THR   A 1 95  ? -19.589 50.822  109.232 1.00 117.69 ?  217 THR   A C   1 
ATOM   364  O O   . THR   A 1 95  ? -20.432 51.439  108.560 1.00 117.48 ?  217 THR   A O   1 
ATOM   365  C CB  . THR   A 1 95  ? -19.084 51.519  111.566 1.00 109.62 ?  217 THR   A CB  1 
ATOM   366  O OG1 . THR   A 1 95  ? -19.000 51.037  112.909 1.00 108.27 ?  217 THR   A OG1 1 
ATOM   367  C CG2 . THR   A 1 95  ? -19.836 52.831  111.562 1.00 107.98 ?  217 THR   A CG2 1 
ATOM   368  N N   . LEU   A 1 96  ? -18.408 50.434  108.732 1.00 111.76 ?  218 LEU   A N   1 
ATOM   369  C CA  . LEU   A 1 96  ? -18.157 50.483  107.304 1.00 108.82 ?  218 LEU   A CA  1 
ATOM   370  C C   . LEU   A 1 96  ? -19.320 49.863  106.550 1.00 117.36 ?  218 LEU   A C   1 
ATOM   371  O O   . LEU   A 1 96  ? -19.817 50.439  105.572 1.00 116.55 ?  218 LEU   A O   1 
ATOM   372  C CB  . LEU   A 1 96  ? -16.847 49.767  106.989 1.00 104.17 ?  218 LEU   A CB  1 
ATOM   373  C CG  . LEU   A 1 96  ? -15.589 50.528  107.394 1.00 102.21 ?  218 LEU   A CG  1 
ATOM   374  C CD1 . LEU   A 1 96  ? -14.404 49.630  107.597 1.00 99.83  ?  218 LEU   A CD1 1 
ATOM   375  C CD2 . LEU   A 1 96  ? -15.271 51.560  106.333 1.00 107.93 ?  218 LEU   A CD2 1 
ATOM   376  N N   . GLN   A 1 97  ? -19.810 48.717  107.046 1.00 117.70 ?  219 GLN   A N   1 
ATOM   377  C CA  . GLN   A 1 97  ? -20.900 48.005  106.387 1.00 117.24 ?  219 GLN   A CA  1 
ATOM   378  C C   . GLN   A 1 97  ? -22.157 48.855  106.343 1.00 120.66 ?  219 GLN   A C   1 
ATOM   379  O O   . GLN   A 1 97  ? -22.821 48.931  105.304 1.00 124.32 ?  219 GLN   A O   1 
ATOM   380  C CB  . GLN   A 1 97  ? -21.141 46.662  107.092 1.00 120.55 ?  219 GLN   A CB  1 
ATOM   381  C CG  . GLN   A 1 97  ? -22.338 45.800  106.593 1.00 129.29 ?  219 GLN   A CG  1 
ATOM   382  C CD  . GLN   A 1 97  ? -22.291 44.311  107.083 1.00 135.54 ?  219 GLN   A CD  1 
ATOM   383  O OE1 . GLN   A 1 97  ? -22.085 44.021  108.272 1.00 127.00 ?  219 GLN   A OE1 1 
ATOM   384  N NE2 . GLN   A 1 97  ? -22.487 43.377  106.145 1.00 136.69 ?  219 GLN   A NE2 1 
ATOM   385  N N   . LEU   A 1 98  ? -22.468 49.553  107.434 1.00 116.11 ?  220 LEU   A N   1 
ATOM   386  C CA  . LEU   A 1 98  ? -23.665 50.382  107.433 1.00 116.78 ?  220 LEU   A CA  1 
ATOM   387  C C   . LEU   A 1 98  ? -23.545 51.516  106.431 1.00 120.59 ?  220 LEU   A C   1 
ATOM   388  O O   . LEU   A 1 98  ? -24.441 51.718  105.598 1.00 120.06 ?  220 LEU   A O   1 
ATOM   389  C CB  . LEU   A 1 98  ? -23.926 50.925  108.823 1.00 115.58 ?  220 LEU   A CB  1 
ATOM   390  C CG  . LEU   A 1 98  ? -24.432 49.795  109.698 1.00 117.35 ?  220 LEU   A CG  1 
ATOM   391  C CD1 . LEU   A 1 98  ? -23.694 49.812  111.012 1.00 114.62 ?  220 LEU   A CD1 1 
ATOM   392  C CD2 . LEU   A 1 98  ? -25.939 49.899  109.878 1.00 122.79 ?  220 LEU   A CD2 1 
ATOM   393  N N   . TRP   A 1 99  ? -22.441 52.269  106.493 1.00 116.27 ?  221 TRP   A N   1 
ATOM   394  C CA  . TRP   A 1 99  ? -22.292 53.392  105.577 1.00 119.28 ?  221 TRP   A CA  1 
ATOM   395  C C   . TRP   A 1 99  ? -22.386 52.920  104.143 1.00 120.01 ?  221 TRP   A C   1 
ATOM   396  O O   . TRP   A 1 99  ? -23.075 53.534  103.317 1.00 120.89 ?  221 TRP   A O   1 
ATOM   397  C CB  . TRP   A 1 99  ? -20.966 54.125  105.804 1.00 119.84 ?  221 TRP   A CB  1 
ATOM   398  C CG  . TRP   A 1 99  ? -20.526 54.982  104.608 1.00 117.05 ?  221 TRP   A CG  1 
ATOM   399  C CD1 . TRP   A 1 99  ? -19.403 54.826  103.858 1.00 114.73 ?  221 TRP   A CD1 1 
ATOM   400  C CD2 . TRP   A 1 99  ? -21.246 56.069  104.016 1.00 114.12 ?  221 TRP   A CD2 1 
ATOM   401  N NE1 . TRP   A 1 99  ? -19.363 55.760  102.859 1.00 110.61 ?  221 TRP   A NE1 1 
ATOM   402  C CE2 . TRP   A 1 99  ? -20.490 56.528  102.928 1.00 110.78 ?  221 TRP   A CE2 1 
ATOM   403  C CE3 . TRP   A 1 99  ? -22.454 56.697  104.305 1.00 118.53 ?  221 TRP   A CE3 1 
ATOM   404  C CZ2 . TRP   A 1 99  ? -20.893 57.584  102.138 1.00 114.29 ?  221 TRP   A CZ2 1 
ATOM   405  C CZ3 . TRP   A 1 99  ? -22.852 57.743  103.520 1.00 121.39 ?  221 TRP   A CZ3 1 
ATOM   406  C CH2 . TRP   A 1 99  ? -22.073 58.182  102.451 1.00 119.02 ?  221 TRP   A CH2 1 
ATOM   407  N N   . LEU   A 1 100 ? -21.724 51.806  103.844 1.00 119.32 ?  222 LEU   A N   1 
ATOM   408  C CA  . LEU   A 1 100 ? -21.689 51.311  102.479 1.00 118.59 ?  222 LEU   A CA  1 
ATOM   409  C C   . LEU   A 1 100 ? -23.076 50.905  102.011 1.00 123.46 ?  222 LEU   A C   1 
ATOM   410  O O   . LEU   A 1 100 ? -23.473 51.215  100.878 1.00 120.83 ?  222 LEU   A O   1 
ATOM   411  C CB  . LEU   A 1 100 ? -20.700 50.157  102.403 1.00 114.95 ?  222 LEU   A CB  1 
ATOM   412  C CG  . LEU   A 1 100 ? -19.281 50.711  102.354 1.00 111.73 ?  222 LEU   A CG  1 
ATOM   413  C CD1 . LEU   A 1 100 ? -18.256 49.622  102.570 1.00 110.41 ?  222 LEU   A CD1 1 
ATOM   414  C CD2 . LEU   A 1 100 ? -19.085 51.385  101.005 1.00 100.55 ?  222 LEU   A CD2 1 
ATOM   415  N N   . ASP   A 1 101 ? -23.847 50.256  102.893 1.00 126.00 ?  223 ASP   A N   1 
ATOM   416  C CA  . ASP   A 1 101 ? -25.151 49.703  102.530 1.00 132.62 ?  223 ASP   A CA  1 
ATOM   417  C C   . ASP   A 1 101 ? -26.207 50.778  102.331 1.00 130.30 ?  223 ASP   A C   1 
ATOM   418  O O   . ASP   A 1 101 ? -27.278 50.491  101.782 1.00 131.54 ?  223 ASP   A O   1 
ATOM   419  C CB  . ASP   A 1 101 ? -25.603 48.692  103.591 1.00 134.81 ?  223 ASP   A CB  1 
ATOM   420  C CG  . ASP   A 1 101 ? -24.895 47.325  103.448 1.00 146.75 ?  223 ASP   A CG  1 
ATOM   421  O OD1 . ASP   A 1 101 ? -24.396 47.016  102.328 1.00 144.56 ?  223 ASP   A OD1 1 
ATOM   422  O OD2 . ASP   A 1 101 ? -24.823 46.572  104.459 1.00 142.76 ?  223 ASP   A OD2 1 
ATOM   423  N N   . ASN   A 1 102 ? -25.924 52.006  102.754 1.00 127.78 ?  224 ASN   A N   1 
ATOM   424  C CA  . ASN   A 1 102 ? -26.767 53.148  102.420 1.00 129.07 ?  224 ASN   A CA  1 
ATOM   425  C C   . ASN   A 1 102 ? -25.878 54.378  102.393 1.00 127.74 ?  224 ASN   A C   1 
ATOM   426  O O   . ASN   A 1 102 ? -25.673 55.045  103.415 1.00 129.66 ?  224 ASN   A O   1 
ATOM   427  C CB  . ASN   A 1 102 ? -27.920 53.308  103.406 1.00 129.78 ?  224 ASN   A CB  1 
ATOM   428  C CG  . ASN   A 1 102 ? -28.871 54.407  103.005 1.00 135.29 ?  224 ASN   A CG  1 
ATOM   429  O OD1 . ASN   A 1 102 ? -28.829 54.913  101.870 1.00 134.44 ?  224 ASN   A OD1 1 
ATOM   430  N ND2 . ASN   A 1 102 ? -29.744 54.790  103.935 1.00 132.69 ?  224 ASN   A ND2 1 
ATOM   431  N N   . PRO   A 1 103 ? -25.304 54.694  101.240 1.00 121.68 ?  225 PRO   A N   1 
ATOM   432  C CA  . PRO   A 1 103 ? -24.405 55.844  101.144 1.00 118.37 ?  225 PRO   A CA  1 
ATOM   433  C C   . PRO   A 1 103 ? -25.085 57.135  100.730 1.00 122.82 ?  225 PRO   A C   1 
ATOM   434  O O   . PRO   A 1 103 ? -24.383 58.078  100.360 1.00 123.96 ?  225 PRO   A O   1 
ATOM   435  C CB  . PRO   A 1 103 ? -23.412 55.399  100.061 1.00 118.59 ?  225 PRO   A CB  1 
ATOM   436  C CG  . PRO   A 1 103 ? -24.019 54.141  99.420  1.00 118.90 ?  225 PRO   A CG  1 
ATOM   437  C CD  . PRO   A 1 103 ? -25.398 53.983  99.962  1.00 121.19 ?  225 PRO   A CD  1 
ATOM   438  N N   . LYS   A 1 104 ? -26.409 57.221  100.749 1.00 121.11 ?  226 LYS   A N   1 
ATOM   439  C CA  . LYS   A 1 104 ? -27.012 58.492  100.385 1.00 126.98 ?  226 LYS   A CA  1 
ATOM   440  C C   . LYS   A 1 104 ? -27.425 59.338  101.590 1.00 129.97 ?  226 LYS   A C   1 
ATOM   441  O O   . LYS   A 1 104 ? -27.855 60.486  101.401 1.00 123.24 ?  226 LYS   A O   1 
ATOM   442  C CB  . LYS   A 1 104 ? -28.205 58.278  99.441  1.00 130.23 ?  226 LYS   A CB  1 
ATOM   443  C CG  . LYS   A 1 104 ? -27.797 58.262  97.960  1.00 127.93 ?  226 LYS   A CG  1 
ATOM   444  C CD  . LYS   A 1 104 ? -28.967 58.504  96.983  1.00 130.14 ?  226 LYS   A CD  1 
ATOM   445  C CE  . LYS   A 1 104 ? -30.082 57.468  97.082  1.00 133.07 ?  226 LYS   A CE  1 
ATOM   446  N NZ  . LYS   A 1 104 ? -29.583 56.080  97.297  1.00 140.56 ?  226 LYS   A NZ  1 
ATOM   447  N N   . ILE   A 1 105 ? -27.282 58.821  102.818 1.00 129.42 ?  227 ILE   A N   1 
ATOM   448  C CA  . ILE   A 1 105 ? -27.525 59.602  104.027 1.00 129.70 ?  227 ILE   A CA  1 
ATOM   449  C C   . ILE   A 1 105 ? -26.365 59.410  104.994 1.00 127.77 ?  227 ILE   A C   1 
ATOM   450  O O   . ILE   A 1 105 ? -25.764 58.333  105.071 1.00 125.56 ?  227 ILE   A O   1 
ATOM   451  C CB  . ILE   A 1 105 ? -28.847 59.228  104.726 1.00 126.30 ?  227 ILE   A CB  1 
ATOM   452  C CG1 . ILE   A 1 105 ? -28.775 57.802  105.267 1.00 129.94 ?  227 ILE   A CG1 1 
ATOM   453  C CG2 . ILE   A 1 105 ? -30.013 59.375  103.768 1.00 126.20 ?  227 ILE   A CG2 1 
ATOM   454  C CD1 . ILE   A 1 105 ? -29.480 57.618  106.589 1.00 131.86 ?  227 ILE   A CD1 1 
ATOM   455  N N   . GLN   A 1 106 ? -26.069 60.466  105.749 1.00 122.82 ?  228 GLN   A N   1 
ATOM   456  C CA  . GLN   A 1 106 ? -25.009 60.409  106.744 1.00 120.00 ?  228 GLN   A CA  1 
ATOM   457  C C   . GLN   A 1 106 ? -25.267 59.308  107.775 1.00 114.27 ?  228 GLN   A C   1 
ATOM   458  O O   . GLN   A 1 106 ? -26.407 58.975  108.094 1.00 114.34 ?  228 GLN   A O   1 
ATOM   459  C CB  . GLN   A 1 106 ? -24.888 61.769  107.418 1.00 124.32 ?  228 GLN   A CB  1 
ATOM   460  C CG  . GLN   A 1 106 ? -24.369 61.734  108.835 1.00 126.60 ?  228 GLN   A CG  1 
ATOM   461  C CD  . GLN   A 1 106 ? -24.098 63.114  109.367 1.00 127.85 ?  228 GLN   A CD  1 
ATOM   462  O OE1 . GLN   A 1 106 ? -24.999 63.949  109.448 1.00 132.27 ?  228 GLN   A OE1 1 
ATOM   463  N NE2 . GLN   A 1 106 ? -22.847 63.370  109.723 1.00 127.44 ?  228 GLN   A NE2 1 
ATOM   464  N N   . LEU   A 1 107 ? -24.187 58.719  108.276 1.00 111.50 ?  229 LEU   A N   1 
ATOM   465  C CA  . LEU   A 1 107 ? -24.256 57.718  109.337 1.00 113.66 ?  229 LEU   A CA  1 
ATOM   466  C C   . LEU   A 1 107 ? -23.804 58.350  110.644 1.00 118.98 ?  229 LEU   A C   1 
ATOM   467  O O   . LEU   A 1 107 ? -22.628 58.300  111.000 1.00 115.86 ?  229 LEU   A O   1 
ATOM   468  C CB  . LEU   A 1 107 ? -23.394 56.511  109.022 1.00 113.75 ?  229 LEU   A CB  1 
ATOM   469  C CG  . LEU   A 1 107 ? -23.670 55.411  110.042 1.00 111.35 ?  229 LEU   A CG  1 
ATOM   470  C CD1 . LEU   A 1 107 ? -25.109 54.956  109.887 1.00 111.43 ?  229 LEU   A CD1 1 
ATOM   471  C CD2 . LEU   A 1 107 ? -22.695 54.245  109.922 1.00 109.48 ?  229 LEU   A CD2 1 
ATOM   472  N N   . THR   A 1 108 ? -24.759 58.927  111.371 1.00 128.10 ?  230 THR   A N   1 
ATOM   473  C CA  . THR   A 1 108 ? -24.494 59.490  112.689 1.00 125.16 ?  230 THR   A CA  1 
ATOM   474  C C   . THR   A 1 108 ? -24.014 58.416  113.647 1.00 122.09 ?  230 THR   A C   1 
ATOM   475  O O   . THR   A 1 108 ? -24.268 57.227  113.469 1.00 124.02 ?  230 THR   A O   1 
ATOM   476  C CB  . THR   A 1 108 ? -25.751 60.120  113.282 1.00 129.85 ?  230 THR   A CB  1 
ATOM   477  O OG1 . THR   A 1 108 ? -26.798 59.133  113.345 1.00 125.65 ?  230 THR   A OG1 1 
ATOM   478  C CG2 . THR   A 1 108 ? -26.191 61.325  112.455 1.00 133.92 ?  230 THR   A CG2 1 
ATOM   479  N N   . PHE   A 1 109 ? -23.328 58.860  114.695 1.00 122.33 ?  231 PHE   A N   1 
ATOM   480  C CA  . PHE   A 1 109 ? -22.867 57.933  115.724 1.00 123.63 ?  231 PHE   A CA  1 
ATOM   481  C C   . PHE   A 1 109 ? -24.046 57.242  116.394 1.00 128.75 ?  231 PHE   A C   1 
ATOM   482  O O   . PHE   A 1 109 ? -24.015 56.030  116.641 1.00 124.56 ?  231 PHE   A O   1 
ATOM   483  C CB  . PHE   A 1 109 ? -22.005 58.703  116.733 1.00 126.31 ?  231 PHE   A CB  1 
ATOM   484  C CG  . PHE   A 1 109 ? -21.659 57.946  117.998 1.00 122.99 ?  231 PHE   A CG  1 
ATOM   485  C CD1 . PHE   A 1 109 ? -21.468 56.573  118.003 1.00 122.03 ?  231 PHE   A CD1 1 
ATOM   486  C CD2 . PHE   A 1 109 ? -21.410 58.637  119.165 1.00 121.87 ?  231 PHE   A CD2 1 
ATOM   487  C CE1 . PHE   A 1 109 ? -21.124 55.904  119.164 1.00 119.33 ?  231 PHE   A CE1 1 
ATOM   488  C CE2 . PHE   A 1 109 ? -21.051 57.966  120.322 1.00 119.92 ?  231 PHE   A CE2 1 
ATOM   489  C CZ  . PHE   A 1 109 ? -20.911 56.600  120.317 1.00 117.68 ?  231 PHE   A CZ  1 
ATOM   490  N N   . GLU   A 1 110 ? -25.105 58.001  116.670 1.00 136.59 ?  232 GLU   A N   1 
ATOM   491  C CA  . GLU   A 1 110 ? -26.308 57.436  117.265 1.00 135.27 ?  232 GLU   A CA  1 
ATOM   492  C C   . GLU   A 1 110 ? -26.828 56.284  116.415 1.00 138.59 ?  232 GLU   A C   1 
ATOM   493  O O   . GLU   A 1 110 ? -27.062 55.176  116.917 1.00 139.06 ?  232 GLU   A O   1 
ATOM   494  C CB  . GLU   A 1 110 ? -27.369 58.532  117.403 1.00 136.47 ?  232 GLU   A CB  1 
ATOM   495  C CG  . GLU   A 1 110 ? -26.997 59.681  118.373 1.00 150.27 ?  232 GLU   A CG  1 
ATOM   496  C CD  . GLU   A 1 110 ? -25.915 60.659  117.829 1.00 151.55 ?  232 GLU   A CD  1 
ATOM   497  O OE1 . GLU   A 1 110 ? -25.924 60.995  116.616 1.00 148.66 ?  232 GLU   A OE1 1 
ATOM   498  O OE2 . GLU   A 1 110 ? -25.052 61.100  118.625 1.00 147.07 ?  232 GLU   A OE2 1 
ATOM   499  N N   . ALA   A 1 111 ? -26.970 56.527  115.104 1.00 137.04 ?  233 ALA   A N   1 
ATOM   500  C CA  . ALA   A 1 111 ? -27.474 55.508  114.189 1.00 136.06 ?  233 ALA   A CA  1 
ATOM   501  C C   . ALA   A 1 111 ? -26.651 54.230  114.255 1.00 129.41 ?  233 ALA   A C   1 
ATOM   502  O O   . ALA   A 1 111 ? -27.193 53.130  114.097 1.00 132.30 ?  233 ALA   A O   1 
ATOM   503  C CB  . ALA   A 1 111 ? -27.499 56.066  112.759 1.00 132.26 ?  233 ALA   A CB  1 
ATOM   504  N N   . THR   A 1 112 ? -25.351 54.352  114.510 1.00 124.46 ?  234 THR   A N   1 
ATOM   505  C CA  . THR   A 1 112 ? -24.475 53.190  114.497 1.00 127.72 ?  234 THR   A CA  1 
ATOM   506  C C   . THR   A 1 112 ? -24.614 52.367  115.772 1.00 133.49 ?  234 THR   A C   1 
ATOM   507  O O   . THR   A 1 112 ? -24.803 51.144  115.722 1.00 133.18 ?  234 THR   A O   1 
ATOM   508  C CB  . THR   A 1 112 ? -23.025 53.634  114.298 1.00 121.46 ?  234 THR   A CB  1 
ATOM   509  O OG1 . THR   A 1 112 ? -22.883 54.286  113.031 1.00 117.45 ?  234 THR   A OG1 1 
ATOM   510  C CG2 . THR   A 1 112 ? -22.095 52.448  114.352 1.00 121.63 ?  234 THR   A CG2 1 
ATOM   511  N N   . LEU   A 1 113 ? -24.517 53.022  116.926 1.00 135.68 ?  235 LEU   A N   1 
ATOM   512  C CA  . LEU   A 1 113 ? -24.644 52.300  118.184 1.00 136.28 ?  235 LEU   A CA  1 
ATOM   513  C C   . LEU   A 1 113 ? -26.005 51.635  118.292 1.00 136.79 ?  235 LEU   A C   1 
ATOM   514  O O   . LEU   A 1 113 ? -26.128 50.560  118.891 1.00 138.87 ?  235 LEU   A O   1 
ATOM   515  C CB  . LEU   A 1 113 ? -24.396 53.255  119.349 1.00 131.16 ?  235 LEU   A CB  1 
ATOM   516  C CG  . LEU   A 1 113 ? -24.167 52.608  120.707 1.00 130.98 ?  235 LEU   A CG  1 
ATOM   517  C CD1 . LEU   A 1 113 ? -23.125 51.526  120.593 1.00 136.29 ?  235 LEU   A CD1 1 
ATOM   518  C CD2 . LEU   A 1 113 ? -23.667 53.665  121.633 1.00 123.74 ?  235 LEU   A CD2 1 
ATOM   519  N N   . GLN   A 1 114 ? -27.028 52.256  117.706 1.00 138.14 ?  236 GLN   A N   1 
ATOM   520  C CA  . GLN   A 1 114 ? -28.339 51.648  117.531 1.00 145.56 ?  236 GLN   A CA  1 
ATOM   521  C C   . GLN   A 1 114 ? -28.366 50.251  116.913 1.00 146.41 ?  236 GLN   A C   1 
ATOM   522  O O   . GLN   A 1 114 ? -28.961 49.323  117.482 1.00 146.32 ?  236 GLN   A O   1 
ATOM   523  C CB  . GLN   A 1 114 ? -29.197 52.529  116.612 1.00 149.17 ?  236 GLN   A CB  1 
ATOM   524  C CG  . GLN   A 1 114 ? -30.656 52.095  116.479 1.00 159.44 ?  236 GLN   A CG  1 
ATOM   525  C CD  . GLN   A 1 114 ? -31.331 51.917  117.828 1.00 167.32 ?  236 GLN   A CD  1 
ATOM   526  O OE1 . GLN   A 1 114 ? -31.252 52.799  118.689 1.00 165.44 ?  236 GLN   A OE1 1 
ATOM   527  N NE2 . GLN   A 1 114 ? -31.996 50.771  118.022 1.00 166.22 ?  236 GLN   A NE2 1 
ATOM   528  N N   . GLN   A 1 115 ? -27.708 50.091  115.759 1.00 141.43 ?  237 GLN   A N   1 
ATOM   529  C CA  . GLN   A 1 115 ? -27.752 48.843  115.007 1.00 139.22 ?  237 GLN   A CA  1 
ATOM   530  C C   . GLN   A 1 115 ? -26.627 47.935  115.468 1.00 137.25 ?  237 GLN   A C   1 
ATOM   531  O O   . GLN   A 1 115 ? -26.564 46.789  115.012 1.00 139.05 ?  237 GLN   A O   1 
ATOM   532  C CB  . GLN   A 1 115 ? -27.660 49.084  113.511 1.00 131.36 ?  237 GLN   A CB  1 
ATOM   533  C CG  . GLN   A 1 115 ? -29.010 49.274  112.899 1.00 138.06 ?  237 GLN   A CG  1 
ATOM   534  C CD  . GLN   A 1 115 ? -28.968 50.237  111.750 1.00 149.68 ?  237 GLN   A CD  1 
ATOM   535  O OE1 . GLN   A 1 115 ? -29.220 49.868  110.600 1.00 155.32 ?  237 GLN   A OE1 1 
ATOM   536  N NE2 . GLN   A 1 115 ? -28.683 51.500  112.055 1.00 146.67 ?  237 GLN   A NE2 1 
ATOM   537  N N   . LEU   A 1 116 ? -25.755 48.387  116.354 1.00 135.13 ?  238 LEU   A N   1 
ATOM   538  C CA  . LEU   A 1 116 ? -24.851 47.456  116.999 1.00 139.15 ?  238 LEU   A CA  1 
ATOM   539  C C   . LEU   A 1 116 ? -25.593 46.580  118.003 1.00 149.31 ?  238 LEU   A C   1 
ATOM   540  O O   . LEU   A 1 116 ? -26.592 46.987  118.611 1.00 149.10 ?  238 LEU   A O   1 
ATOM   541  C CB  . LEU   A 1 116 ? -23.721 48.188  117.706 1.00 141.56 ?  238 LEU   A CB  1 
ATOM   542  C CG  . LEU   A 1 116 ? -22.381 47.978  117.032 1.00 139.57 ?  238 LEU   A CG  1 
ATOM   543  C CD1 . LEU   A 1 116 ? -21.294 48.774  117.733 1.00 135.60 ?  238 LEU   A CD1 1 
ATOM   544  C CD2 . LEU   A 1 116 ? -22.085 46.499  117.030 1.00 138.99 ?  238 LEU   A CD2 1 
ATOM   545  N N   . GLU   A 1 117 ? -25.079 45.359  118.175 1.00 156.61 ?  239 GLU   A N   1 
ATOM   546  C CA  . GLU   A 1 117 ? -25.586 44.384  119.135 1.00 154.96 ?  239 GLU   A CA  1 
ATOM   547  C C   . GLU   A 1 117 ? -24.448 43.961  120.054 1.00 148.05 ?  239 GLU   A C   1 
ATOM   548  O O   . GLU   A 1 117 ? -23.300 43.844  119.611 1.00 147.77 ?  239 GLU   A O   1 
ATOM   549  C CB  . GLU   A 1 117 ? -26.164 43.139  118.437 1.00 160.06 ?  239 GLU   A CB  1 
ATOM   550  C CG  . GLU   A 1 117 ? -27.128 43.420  117.281 1.00 164.79 ?  239 GLU   A CG  1 
ATOM   551  C CD  . GLU   A 1 117 ? -28.583 43.194  117.659 1.00 171.68 ?  239 GLU   A CD  1 
ATOM   552  O OE1 . GLU   A 1 117 ? -28.862 43.011  118.867 1.00 170.85 ?  239 GLU   A OE1 1 
ATOM   553  O OE2 . GLU   A 1 117 ? -29.442 43.180  116.746 1.00 175.66 ?  239 GLU   A OE2 1 
ATOM   554  N N   . ALA   A 1 118 ? -24.774 43.715  121.331 1.00 144.38 ?  240 ALA   A N   1 
ATOM   555  C CA  . ALA   A 1 118 ? -23.758 43.412  122.332 1.00 141.12 ?  240 ALA   A CA  1 
ATOM   556  C C   . ALA   A 1 118 ? -23.035 42.111  121.980 1.00 139.54 ?  240 ALA   A C   1 
ATOM   557  O O   . ALA   A 1 118 ? -23.546 41.298  121.208 1.00 139.36 ?  240 ALA   A O   1 
ATOM   558  C CB  . ALA   A 1 118 ? -24.395 43.325  123.717 1.00 135.61 ?  240 ALA   A CB  1 
ATOM   559  N N   . PRO   A 1 119 ? -21.816 41.896  122.512 1.00 137.78 ?  241 PRO   A N   1 
ATOM   560  C CA  . PRO   A 1 119 ? -21.015 42.688  123.461 1.00 140.42 ?  241 PRO   A CA  1 
ATOM   561  C C   . PRO   A 1 119 ? -20.381 43.953  122.860 1.00 143.46 ?  241 PRO   A C   1 
ATOM   562  O O   . PRO   A 1 119 ? -19.596 44.631  123.534 1.00 142.34 ?  241 PRO   A O   1 
ATOM   563  C CB  . PRO   A 1 119 ? -19.921 41.707  123.897 1.00 138.61 ?  241 PRO   A CB  1 
ATOM   564  C CG  . PRO   A 1 119 ? -19.800 40.730  122.778 1.00 136.30 ?  241 PRO   A CG  1 
ATOM   565  C CD  . PRO   A 1 119 ? -21.096 40.702  122.029 1.00 132.45 ?  241 PRO   A CD  1 
ATOM   566  N N   . TYR   A 1 120 ? -20.722 44.259  121.603 1.00 147.97 ?  242 TYR   A N   1 
ATOM   567  C CA  . TYR   A 1 120 ? -20.073 45.327  120.845 1.00 144.29 ?  242 TYR   A CA  1 
ATOM   568  C C   . TYR   A 1 120 ? -20.711 46.686  121.085 1.00 139.86 ?  242 TYR   A C   1 
ATOM   569  O O   . TYR   A 1 120 ? -19.986 47.680  121.188 1.00 138.74 ?  242 TYR   A O   1 
ATOM   570  C CB  . TYR   A 1 120 ? -20.065 44.990  119.348 1.00 139.97 ?  242 TYR   A CB  1 
ATOM   571  C CG  . TYR   A 1 120 ? -19.413 43.656  119.039 1.00 134.92 ?  242 TYR   A CG  1 
ATOM   572  C CD1 . TYR   A 1 120 ? -18.131 43.366  119.512 1.00 130.57 ?  242 TYR   A CD1 1 
ATOM   573  C CD2 . TYR   A 1 120 ? -20.074 42.691  118.295 1.00 130.37 ?  242 TYR   A CD2 1 
ATOM   574  C CE1 . TYR   A 1 120 ? -17.523 42.159  119.249 1.00 130.54 ?  242 TYR   A CE1 1 
ATOM   575  C CE2 . TYR   A 1 120 ? -19.474 41.477  118.021 1.00 138.93 ?  242 TYR   A CE2 1 
ATOM   576  C CZ  . TYR   A 1 120 ? -18.197 41.209  118.502 1.00 141.60 ?  242 TYR   A CZ  1 
ATOM   577  O OH  . TYR   A 1 120 ? -17.600 39.987  118.227 1.00 145.16 ?  242 TYR   A OH  1 
ATOM   578  N N   . ASN   A 1 121 ? -22.046 46.756  121.191 1.00 143.15 ?  243 ASN   A N   1 
ATOM   579  C CA  . ASN   A 1 121 ? -22.715 47.974  121.640 1.00 144.80 ?  243 ASN   A CA  1 
ATOM   580  C C   . ASN   A 1 121 ? -22.728 47.768  123.149 1.00 139.02 ?  243 ASN   A C   1 
ATOM   581  O O   . ASN   A 1 121 ? -23.798 47.662  123.761 1.00 136.43 ?  243 ASN   A O   1 
ATOM   582  C CB  . ASN   A 1 121 ? -24.153 48.039  121.104 1.00 144.46 ?  243 ASN   A CB  1 
ATOM   583  C CG  . ASN   A 1 121 ? -25.137 47.168  121.877 1.00 145.47 ?  243 ASN   A CG  1 
ATOM   584  O OD1 . ASN   A 1 121 ? -24.753 46.368  122.734 1.00 143.21 ?  243 ASN   A OD1 1 
ATOM   585  N ND2 . ASN   A 1 121 ? -26.427 47.303  121.542 1.00 143.09 ?  243 ASN   A ND2 1 
ATOM   586  N N   . SER   A 1 122 ? -21.547 47.719  123.762 1.00 137.53 ?  244 SER   A N   1 
ATOM   587  C CA  . SER   A 1 122 ? -21.416 47.667  125.214 1.00 142.90 ?  244 SER   A CA  1 
ATOM   588  C C   . SER   A 1 122 ? -20.535 48.886  125.504 1.00 142.19 ?  244 SER   A C   1 
ATOM   589  O O   . SER   A 1 122 ? -20.974 49.833  126.168 1.00 140.33 ?  244 SER   A O   1 
ATOM   590  C CB  . SER   A 1 122 ? -20.780 46.392  125.779 1.00 142.59 ?  244 SER   A CB  1 
ATOM   591  O OG  . SER   A 1 122 ? -19.365 46.447  125.682 1.00 144.43 ?  244 SER   A OG  1 
ATOM   592  N N   . ASP   A 1 123 ? -19.286 48.870  125.029 1.00 140.02 ?  245 ASP   A N   1 
ATOM   593  C CA  . ASP   A 1 123 ? -18.327 49.941  125.313 1.00 133.25 ?  245 ASP   A CA  1 
ATOM   594  C C   . ASP   A 1 123 ? -18.643 51.106  124.384 1.00 126.40 ?  245 ASP   A C   1 
ATOM   595  O O   . ASP   A 1 123 ? -18.292 51.083  123.206 1.00 126.91 ?  245 ASP   A O   1 
ATOM   596  C CB  . ASP   A 1 123 ? -16.896 49.440  125.130 1.00 128.10 ?  245 ASP   A CB  1 
ATOM   597  C CG  . ASP   A 1 123 ? -15.846 50.461  125.560 1.00 123.68 ?  245 ASP   A CG  1 
ATOM   598  O OD1 . ASP   A 1 123 ? -16.154 51.673  125.618 1.00 119.59 ?  245 ASP   A OD1 1 
ATOM   599  O OD2 . ASP   A 1 123 ? -14.702 50.038  125.840 1.00 120.92 ?  245 ASP   A OD2 1 
ATOM   600  N N   . THR   A 1 124 ? -19.304 52.140  124.905 1.00 125.31 ?  246 THR   A N   1 
ATOM   601  C CA  . THR   A 1 124 ? -19.826 53.205  124.059 1.00 125.78 ?  246 THR   A CA  1 
ATOM   602  C C   . THR   A 1 124 ? -18.858 54.369  123.897 1.00 122.90 ?  246 THR   A C   1 
ATOM   603  O O   . THR   A 1 124 ? -19.298 55.494  123.635 1.00 125.15 ?  246 THR   A O   1 
ATOM   604  C CB  . THR   A 1 124 ? -21.166 53.715  124.594 1.00 128.31 ?  246 THR   A CB  1 
ATOM   605  O OG1 . THR   A 1 124 ? -21.010 54.184  125.942 1.00 128.83 ?  246 THR   A OG1 1 
ATOM   606  C CG2 . THR   A 1 124 ? -22.175 52.592  124.573 1.00 134.30 ?  246 THR   A CG2 1 
ATOM   607  N N   . VAL   A 1 125 ? -17.557 54.137  124.062 1.00 119.67 ?  247 VAL   A N   1 
ATOM   608  C CA  . VAL   A 1 125 ? -16.538 55.014  123.507 1.00 118.92 ?  247 VAL   A CA  1 
ATOM   609  C C   . VAL   A 1 125 ? -15.681 54.297  122.468 1.00 120.53 ?  247 VAL   A C   1 
ATOM   610  O O   . VAL   A 1 125 ? -15.316 54.885  121.439 1.00 115.04 ?  247 VAL   A O   1 
ATOM   611  C CB  . VAL   A 1 125 ? -15.662 55.651  124.610 1.00 109.33 ?  247 VAL   A CB  1 
ATOM   612  C CG1 . VAL   A 1 125 ? -16.380 56.852  125.184 1.00 103.28 ?  247 VAL   A CG1 1 
ATOM   613  C CG2 . VAL   A 1 125 ? -15.337 54.652  125.691 1.00 109.87 ?  247 VAL   A CG2 1 
ATOM   614  N N   . LEU   A 1 126 ? -15.380 53.013  122.687 1.00 125.19 ?  248 LEU   A N   1 
ATOM   615  C CA  . LEU   A 1 126 ? -14.832 52.212  121.600 1.00 120.40 ?  248 LEU   A CA  1 
ATOM   616  C C   . LEU   A 1 126 ? -15.706 52.309  120.360 1.00 117.36 ?  248 LEU   A C   1 
ATOM   617  O O   . LEU   A 1 126 ? -15.195 52.278  119.241 1.00 119.97 ?  248 LEU   A O   1 
ATOM   618  C CB  . LEU   A 1 126 ? -14.675 50.749  122.016 1.00 114.21 ?  248 LEU   A CB  1 
ATOM   619  C CG  . LEU   A 1 126 ? -13.568 50.052  121.236 1.00 106.85 ?  248 LEU   A CG  1 
ATOM   620  C CD1 . LEU   A 1 126 ? -12.478 51.044  121.016 1.00 109.76 ?  248 LEU   A CD1 1 
ATOM   621  C CD2 . LEU   A 1 126 ? -13.017 48.863  121.985 1.00 115.71 ?  248 LEU   A CD2 1 
ATOM   622  N N   . VAL   A 1 127 ? -17.018 52.451  120.531 1.00 115.55 ?  249 VAL   A N   1 
ATOM   623  C CA  . VAL   A 1 127 ? -17.849 52.717  119.371 1.00 110.63 ?  249 VAL   A CA  1 
ATOM   624  C C   . VAL   A 1 127 ? -17.686 54.153  118.929 1.00 109.76 ?  249 VAL   A C   1 
ATOM   625  O O   . VAL   A 1 127 ? -17.561 54.425  117.735 1.00 109.33 ?  249 VAL   A O   1 
ATOM   626  C CB  . VAL   A 1 127 ? -19.312 52.374  119.658 1.00 115.09 ?  249 VAL   A CB  1 
ATOM   627  C CG1 . VAL   A 1 127 ? -20.174 52.810  118.509 1.00 112.15 ?  249 VAL   A CG1 1 
ATOM   628  C CG2 . VAL   A 1 127 ? -19.433 50.897  119.838 1.00 122.56 ?  249 VAL   A CG2 1 
ATOM   629  N N   . HIS   A 1 128 ? -17.654 55.093  119.877 1.00 114.42 ?  250 HIS   A N   1 
ATOM   630  C CA  . HIS   A 1 128 ? -17.447 56.497  119.523 1.00 116.07 ?  250 HIS   A CA  1 
ATOM   631  C C   . HIS   A 1 128 ? -16.138 56.690  118.770 1.00 117.78 ?  250 HIS   A C   1 
ATOM   632  O O   . HIS   A 1 128 ? -16.131 57.159  117.625 1.00 119.48 ?  250 HIS   A O   1 
ATOM   633  C CB  . HIS   A 1 128 ? -17.435 57.383  120.765 1.00 120.03 ?  250 HIS   A CB  1 
ATOM   634  C CG  . HIS   A 1 128 ? -17.689 58.827  120.470 1.00 119.84 ?  250 HIS   A CG  1 
ATOM   635  N ND1 . HIS   A 1 128 ? -18.065 59.273  119.221 1.00 122.50 ?  250 HIS   A ND1 1 
ATOM   636  C CD2 . HIS   A 1 128 ? -17.524 59.935  121.229 1.00 120.74 ?  250 HIS   A CD2 1 
ATOM   637  C CE1 . HIS   A 1 128 ? -18.186 60.589  119.239 1.00 121.24 ?  250 HIS   A CE1 1 
ATOM   638  N NE2 . HIS   A 1 128 ? -17.852 61.016  120.443 1.00 127.43 ?  250 HIS   A NE2 1 
ATOM   639  N N   . ARG   A 1 129 ? -15.014 56.356  119.419 1.00 117.90 ?  251 ARG   A N   1 
ATOM   640  C CA  . ARG   A 1 129 ? -13.695 56.508  118.806 1.00 116.68 ?  251 ARG   A CA  1 
ATOM   641  C C   . ARG   A 1 129 ? -13.668 55.948  117.387 1.00 117.46 ?  251 ARG   A C   1 
ATOM   642  O O   . ARG   A 1 129 ? -13.256 56.634  116.441 1.00 120.05 ?  251 ARG   A O   1 
ATOM   643  C CB  . ARG   A 1 129 ? -12.647 55.802  119.656 1.00 109.84 ?  251 ARG   A CB  1 
ATOM   644  C CG  . ARG   A 1 129 ? -12.244 56.535  120.860 1.00 104.20 ?  251 ARG   A CG  1 
ATOM   645  C CD  . ARG   A 1 129 ? -11.387 55.626  121.650 1.00 105.35 ?  251 ARG   A CD  1 
ATOM   646  N NE  . ARG   A 1 129 ? -10.000 55.752  121.240 1.00 109.22 ?  251 ARG   A NE  1 
ATOM   647  C CZ  . ARG   A 1 129 ? -9.019  55.000  121.713 1.00 110.37 ?  251 ARG   A CZ  1 
ATOM   648  N NH1 . ARG   A 1 129 ? -9.256  53.991  122.539 1.00 102.08 ?  251 ARG   A NH1 1 
ATOM   649  N NH2 . ARG   A 1 129 ? -7.769  55.267  121.351 1.00 113.25 ?  251 ARG   A NH2 1 
ATOM   650  N N   . VAL   A 1 130 ? -14.111 54.694  117.228 1.00 111.59 ?  252 VAL   A N   1 
ATOM   651  C CA  . VAL   A 1 130 ? -14.164 54.061  115.915 1.00 107.38 ?  252 VAL   A CA  1 
ATOM   652  C C   . VAL   A 1 130 ? -14.955 54.916  114.932 1.00 108.68 ?  252 VAL   A C   1 
ATOM   653  O O   . VAL   A 1 130 ? -14.467 55.242  113.843 1.00 111.03 ?  252 VAL   A O   1 
ATOM   654  C CB  . VAL   A 1 130 ? -14.730 52.635  116.035 1.00 106.10 ?  252 VAL   A CB  1 
ATOM   655  C CG1 . VAL   A 1 130 ? -15.226 52.121  114.693 1.00 104.80 ?  252 VAL   A CG1 1 
ATOM   656  C CG2 . VAL   A 1 130 ? -13.644 51.709  116.556 1.00 102.91 ?  252 VAL   A CG2 1 
ATOM   657  N N   . HIS   A 1 131 ? -16.175 55.312  115.300 1.00 102.24 ?  253 HIS   A N   1 
ATOM   658  C CA  . HIS   A 1 131 ? -16.987 56.070  114.357 1.00 102.37 ?  253 HIS   A CA  1 
ATOM   659  C C   . HIS   A 1 131 ? -16.275 57.331  113.912 1.00 110.61 ?  253 HIS   A C   1 
ATOM   660  O O   . HIS   A 1 131 ? -16.161 57.602  112.712 1.00 115.66 ?  253 HIS   A O   1 
ATOM   661  C CB  . HIS   A 1 131 ? -18.330 56.440  114.958 1.00 103.80 ?  253 HIS   A CB  1 
ATOM   662  C CG  . HIS   A 1 131 ? -19.207 57.223  114.032 1.00 103.90 ?  253 HIS   A CG  1 
ATOM   663  N ND1 . HIS   A 1 131 ? -19.032 58.571  113.802 1.00 111.94 ?  253 HIS   A ND1 1 
ATOM   664  C CD2 . HIS   A 1 131 ? -20.280 56.853  113.294 1.00 108.48 ?  253 HIS   A CD2 1 
ATOM   665  C CE1 . HIS   A 1 131 ? -19.953 58.995  112.954 1.00 117.33 ?  253 HIS   A CE1 1 
ATOM   666  N NE2 . HIS   A 1 131 ? -20.724 57.971  112.631 1.00 115.80 ?  253 HIS   A NE2 1 
ATOM   667  N N   . SER   A 1 132 ? -15.784 58.118  114.865 1.00 109.65 ?  254 SER   A N   1 
ATOM   668  C CA  . SER   A 1 132 ? -15.212 59.407  114.508 1.00 111.50 ?  254 SER   A CA  1 
ATOM   669  C C   . SER   A 1 132 ? -13.989 59.247  113.608 1.00 114.62 ?  254 SER   A C   1 
ATOM   670  O O   . SER   A 1 132 ? -13.874 59.939  112.587 1.00 112.44 ?  254 SER   A O   1 
ATOM   671  C CB  . SER   A 1 132 ? -14.892 60.183  115.775 1.00 116.10 ?  254 SER   A CB  1 
ATOM   672  O OG  . SER   A 1 132 ? -16.115 60.559  116.385 1.00 115.25 ?  254 SER   A OG  1 
ATOM   673  N N   . TYR   A 1 133 ? -13.086 58.318  113.951 1.00 115.36 ?  255 TYR   A N   1 
ATOM   674  C CA  . TYR   A 1 133 ? -11.968 57.977  113.067 1.00 113.14 ?  255 TYR   A CA  1 
ATOM   675  C C   . TYR   A 1 133 ? -12.455 57.684  111.649 1.00 105.22 ?  255 TYR   A C   1 
ATOM   676  O O   . TYR   A 1 133 ? -11.954 58.248  110.666 1.00 101.91 ?  255 TYR   A O   1 
ATOM   677  C CB  . TYR   A 1 133 ? -11.202 56.781  113.647 1.00 108.13 ?  255 TYR   A CB  1 
ATOM   678  C CG  . TYR   A 1 133 ? -10.419 55.982  112.641 1.00 105.23 ?  255 TYR   A CG  1 
ATOM   679  C CD1 . TYR   A 1 133 ? -11.023 54.937  111.956 1.00 107.34 ?  255 TYR   A CD1 1 
ATOM   680  C CD2 . TYR   A 1 133 ? -9.070  56.243  112.395 1.00 105.61 ?  255 TYR   A CD2 1 
ATOM   681  C CE1 . TYR   A 1 133 ? -10.332 54.179  111.019 1.00 110.56 ?  255 TYR   A CE1 1 
ATOM   682  C CE2 . TYR   A 1 133 ? -8.348  55.483  111.460 1.00 109.54 ?  255 TYR   A CE2 1 
ATOM   683  C CZ  . TYR   A 1 133 ? -8.996  54.442  110.770 1.00 116.56 ?  255 TYR   A CZ  1 
ATOM   684  O OH  . TYR   A 1 133 ? -8.350  53.646  109.822 1.00 117.34 ?  255 TYR   A OH  1 
ATOM   685  N N   . LEU   A 1 134 ? -13.451 56.812  111.532 1.00 104.71 ?  256 LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 134 ? -14.029 56.512  110.230 1.00 106.64 ?  256 LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 134 ? -14.497 57.778  109.534 1.00 102.59 ?  256 LEU   A C   1 
ATOM   688  O O   . LEU   A 1 134 ? -14.125 58.041  108.389 1.00 103.76 ?  256 LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 134 ? -15.182 55.524  110.400 1.00 109.24 ?  256 LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 134 ? -14.774 54.121  110.875 1.00 107.68 ?  256 LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 134 ? -15.878 53.150  110.576 1.00 112.87 ?  256 LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 134 ? -13.501 53.644  110.205 1.00 98.62  ?  256 LEU   A CD2 1 
ATOM   693  N N   . GLU   A 1 135 ? -15.288 58.594  110.230 1.00 106.25 ?  257 GLU   A N   1 
ATOM   694  C CA  . GLU   A 1 135 ? -15.878 59.782  109.613 1.00 111.84 ?  257 GLU   A CA  1 
ATOM   695  C C   . GLU   A 1 135 ? -14.822 60.818  109.261 1.00 106.00 ?  257 GLU   A C   1 
ATOM   696  O O   . GLU   A 1 135 ? -14.982 61.576  108.288 1.00 99.81  ?  257 GLU   A O   1 
ATOM   697  C CB  . GLU   A 1 135 ? -16.925 60.382  110.552 1.00 111.57 ?  257 GLU   A CB  1 
ATOM   698  C CG  . GLU   A 1 135 ? -17.819 61.439  109.923 1.00 116.06 ?  257 GLU   A CG  1 
ATOM   699  C CD  . GLU   A 1 135 ? -18.716 62.085  110.950 1.00 118.66 ?  257 GLU   A CD  1 
ATOM   700  O OE1 . GLU   A 1 135 ? -18.252 62.286  112.094 1.00 120.55 ?  257 GLU   A OE1 1 
ATOM   701  O OE2 . GLU   A 1 135 ? -19.897 62.340  110.626 1.00 119.93 ?  257 GLU   A OE2 1 
ATOM   702  N N   . ARG   A 1 136 ? -13.741 60.841  110.038 1.00 103.15 ?  258 ARG   A N   1 
ATOM   703  C CA  . ARG   A 1 136 ? -12.689 61.827  109.855 1.00 103.36 ?  258 ARG   A CA  1 
ATOM   704  C C   . ARG   A 1 136 ? -11.918 61.552  108.577 1.00 101.75 ?  258 ARG   A C   1 
ATOM   705  O O   . ARG   A 1 136 ? -11.755 62.439  107.727 1.00 101.09 ?  258 ARG   A O   1 
ATOM   706  C CB  . ARG   A 1 136 ? -11.775 61.811  111.085 1.00 102.95 ?  258 ARG   A CB  1 
ATOM   707  C CG  . ARG   A 1 136 ? -10.534 62.658  111.023 1.00 99.77  ?  258 ARG   A CG  1 
ATOM   708  C CD  . ARG   A 1 136 ? -10.827 64.113  110.683 1.00 102.06 ?  258 ARG   A CD  1 
ATOM   709  N NE  . ARG   A 1 136 ? -11.885 64.724  111.477 1.00 99.10  ?  258 ARG   A NE  1 
ATOM   710  C CZ  . ARG   A 1 136 ? -11.661 65.506  112.521 1.00 97.93  ?  258 ARG   A CZ  1 
ATOM   711  N NH1 . ARG   A 1 136 ? -10.441 65.656  113.024 1.00 93.41  ?  258 ARG   A NH1 1 
ATOM   712  N NH2 . ARG   A 1 136 ? -12.686 66.136  113.087 1.00 97.16  ?  258 ARG   A NH2 1 
ATOM   713  N N   . HIS   A 1 137 ? -11.470 60.317  108.398 1.00 97.61  ?  259 HIS   A N   1 
ATOM   714  C CA  . HIS   A 1 137 ? -10.667 60.017  107.229 1.00 97.42  ?  259 HIS   A CA  1 
ATOM   715  C C   . HIS   A 1 137 ? -11.489 59.503  106.073 1.00 94.70  ?  259 HIS   A C   1 
ATOM   716  O O   . HIS   A 1 137 ? -10.996 58.680  105.299 1.00 92.98  ?  259 HIS   A O   1 
ATOM   717  C CB  . HIS   A 1 137 ? -9.558  59.046  107.598 1.00 98.38  ?  259 HIS   A CB  1 
ATOM   718  C CG  . HIS   A 1 137 ? -8.755  59.508  108.767 1.00 106.52 ?  259 HIS   A CG  1 
ATOM   719  N ND1 . HIS   A 1 137 ? -7.571  60.204  108.630 1.00 111.48 ?  259 HIS   A ND1 1 
ATOM   720  C CD2 . HIS   A 1 137 ? -8.960  59.371  110.098 1.00 110.63 ?  259 HIS   A CD2 1 
ATOM   721  C CE1 . HIS   A 1 137 ? -7.085  60.482  109.827 1.00 111.55 ?  259 HIS   A CE1 1 
ATOM   722  N NE2 . HIS   A 1 137 ? -7.906  59.983  110.735 1.00 114.10 ?  259 HIS   A NE2 1 
ATOM   723  N N   . GLY   A 1 138 ? -12.719 59.987  105.930 1.00 98.64  ?  260 GLY   A N   1 
ATOM   724  C CA  . GLY   A 1 138 ? -13.559 59.676  104.781 1.00 100.97 ?  260 GLY   A CA  1 
ATOM   725  C C   . GLY   A 1 138 ? -13.720 58.204  104.462 1.00 99.78  ?  260 GLY   A C   1 
ATOM   726  O O   . GLY   A 1 138 ? -13.692 57.811  103.285 1.00 99.64  ?  260 GLY   A O   1 
ATOM   727  N N   . LEU   A 1 139 ? -13.852 57.370  105.479 1.00 95.44  ?  261 LEU   A N   1 
ATOM   728  C CA  . LEU   A 1 139 ? -14.232 55.998  105.219 1.00 102.14 ?  261 LEU   A CA  1 
ATOM   729  C C   . LEU   A 1 139 ? -15.736 55.834  105.336 1.00 106.92 ?  261 LEU   A C   1 
ATOM   730  O O   . LEU   A 1 139 ? -16.265 54.793  104.936 1.00 109.69 ?  261 LEU   A O   1 
ATOM   731  C CB  . LEU   A 1 139 ? -13.478 55.046  106.166 1.00 94.88  ?  261 LEU   A CB  1 
ATOM   732  C CG  . LEU   A 1 139 ? -12.016 54.909  105.682 1.00 86.41  ?  261 LEU   A CG  1 
ATOM   733  C CD1 . LEU   A 1 139 ? -11.153 53.960  106.509 1.00 80.79  ?  261 LEU   A CD1 1 
ATOM   734  C CD2 . LEU   A 1 139 ? -11.943 54.561  104.188 1.00 95.15  ?  261 LEU   A CD2 1 
ATOM   735  N N   . ILE   A 1 140 ? -16.419 56.871  105.839 1.00 105.66 ?  262 ILE   A N   1 
ATOM   736  C CA  . ILE   A 1 140 ? -17.872 56.945  105.948 1.00 107.70 ?  262 ILE   A CA  1 
ATOM   737  C C   . ILE   A 1 140 ? -18.222 58.418  105.840 1.00 109.78 ?  262 ILE   A C   1 
ATOM   738  O O   . ILE   A 1 140 ? -17.402 59.288  106.141 1.00 110.37 ?  262 ILE   A O   1 
ATOM   739  C CB  . ILE   A 1 140 ? -18.421 56.378  107.283 1.00 111.32 ?  262 ILE   A CB  1 
ATOM   740  C CG1 . ILE   A 1 140 ? -17.781 57.078  108.463 1.00 106.36 ?  262 ILE   A CG1 1 
ATOM   741  C CG2 . ILE   A 1 140 ? -18.094 54.913  107.471 1.00 114.00 ?  262 ILE   A CG2 1 
ATOM   742  C CD1 . ILE   A 1 140 ? -18.692 57.177  109.606 1.00 108.64 ?  262 ILE   A CD1 1 
ATOM   743  N N   . ASN   A 1 141 ? -19.455 58.702  105.430 1.00 113.16 ?  263 ASN   A N   1 
ATOM   744  C CA  . ASN   A 1 141 ? -19.928 60.076  105.216 1.00 113.73 ?  263 ASN   A CA  1 
ATOM   745  C C   . ASN   A 1 141 ? -18.882 60.900  104.473 1.00 112.40 ?  263 ASN   A C   1 
ATOM   746  O O   . ASN   A 1 141 ? -18.361 61.910  104.967 1.00 110.47 ?  263 ASN   A O   1 
ATOM   747  C CB  . ASN   A 1 141 ? -20.300 60.758  106.527 1.00 116.27 ?  263 ASN   A CB  1 
ATOM   748  C CG  . ASN   A 1 141 ? -21.093 59.861  107.445 1.00 118.94 ?  263 ASN   A CG  1 
ATOM   749  O OD1 . ASN   A 1 141 ? -22.070 59.244  107.029 1.00 124.82 ?  263 ASN   A OD1 1 
ATOM   750  N ND2 . ASN   A 1 141 ? -20.679 59.782  108.706 1.00 116.64 ?  263 ASN   A ND2 1 
ATOM   751  N N   . PHE   A 1 142 ? -18.547 60.403  103.282 1.00 109.23 ?  264 PHE   A N   1 
ATOM   752  C CA  . PHE   A 1 142 ? -17.826 61.149  102.263 1.00 108.45 ?  264 PHE   A CA  1 
ATOM   753  C C   . PHE   A 1 142 ? -18.638 61.132  100.979 1.00 105.25 ?  264 PHE   A C   1 
ATOM   754  O O   . PHE   A 1 142 ? -19.469 60.246  100.751 1.00 103.92 ?  264 PHE   A O   1 
ATOM   755  C CB  . PHE   A 1 142 ? -16.425 60.580  101.989 1.00 101.18 ?  264 PHE   A CB  1 
ATOM   756  C CG  . PHE   A 1 142 ? -16.428 59.231  101.311 1.00 104.99 ?  264 PHE   A CG  1 
ATOM   757  C CD1 . PHE   A 1 142 ? -16.566 59.119  99.928  1.00 100.46 ?  264 PHE   A CD1 1 
ATOM   758  C CD2 . PHE   A 1 142 ? -16.264 58.070  102.055 1.00 106.48 ?  264 PHE   A CD2 1 
ATOM   759  C CE1 . PHE   A 1 142 ? -16.563 57.870  99.310  1.00 98.31  ?  264 PHE   A CE1 1 
ATOM   760  C CE2 . PHE   A 1 142 ? -16.241 56.825  101.446 1.00 104.06 ?  264 PHE   A CE2 1 
ATOM   761  C CZ  . PHE   A 1 142 ? -16.397 56.725  100.071 1.00 100.08 ?  264 PHE   A CZ  1 
ATOM   762  N N   . GLY   A 1 143 ? -18.384 62.102  100.127 1.00 99.10  ?  265 GLY   A N   1 
ATOM   763  C CA  . GLY   A 1 143 ? -19.112 62.207  98.879  1.00 99.16  ?  265 GLY   A CA  1 
ATOM   764  C C   . GLY   A 1 143 ? -20.293 63.153  99.012  1.00 104.62 ?  265 GLY   A C   1 
ATOM   765  O O   . GLY   A 1 143 ? -20.126 64.313  99.390  1.00 111.50 ?  265 GLY   A O   1 
ATOM   766  N N   . ILE   A 1 144 ? -21.491 62.644  98.731  1.00 103.80 ?  266 ILE   A N   1 
ATOM   767  C CA  . ILE   A 1 144 ? -22.704 63.455  98.678  1.00 104.67 ?  266 ILE   A CA  1 
ATOM   768  C C   . ILE   A 1 144 ? -23.794 62.751  99.476  1.00 111.38 ?  266 ILE   A C   1 
ATOM   769  O O   . ILE   A 1 144 ? -24.462 61.850  98.959  1.00 114.50 ?  266 ILE   A O   1 
ATOM   770  C CB  . ILE   A 1 144 ? -23.148 63.705  97.244  1.00 92.20  ?  266 ILE   A CB  1 
ATOM   771  C CG1 . ILE   A 1 144 ? -22.052 64.472  96.528  1.00 91.35  ?  266 ILE   A CG1 1 
ATOM   772  C CG2 . ILE   A 1 144 ? -24.444 64.446  97.214  1.00 91.80  ?  266 ILE   A CG2 1 
ATOM   773  C CD1 . ILE   A 1 144 ? -22.406 64.842  95.146  1.00 93.48  ?  266 ILE   A CD1 1 
ATOM   774  N N   . TYR   A 1 145 ? -23.987 63.171  100.730 1.00 115.34 ?  267 TYR   A N   1 
ATOM   775  C CA  . TYR   A 1 145 ? -24.976 62.597  101.632 1.00 121.03 ?  267 TYR   A CA  1 
ATOM   776  C C   . TYR   A 1 145 ? -25.903 63.693  102.132 1.00 130.10 ?  267 TYR   A C   1 
ATOM   777  O O   . TYR   A 1 145 ? -25.489 64.853  102.253 1.00 135.09 ?  267 TYR   A O   1 
ATOM   778  C CB  . TYR   A 1 145 ? -24.309 61.895  102.838 1.00 120.40 ?  267 TYR   A CB  1 
ATOM   779  C CG  . TYR   A 1 145 ? -23.053 62.566  103.373 1.00 122.41 ?  267 TYR   A CG  1 
ATOM   780  C CD1 . TYR   A 1 145 ? -21.855 62.479  102.686 1.00 121.27 ?  267 TYR   A CD1 1 
ATOM   781  C CD2 . TYR   A 1 145 ? -23.050 63.240  104.583 1.00 125.63 ?  267 TYR   A CD2 1 
ATOM   782  C CE1 . TYR   A 1 145 ? -20.698 63.088  103.158 1.00 121.57 ?  267 TYR   A CE1 1 
ATOM   783  C CE2 . TYR   A 1 145 ? -21.881 63.844  105.073 1.00 126.89 ?  267 TYR   A CE2 1 
ATOM   784  C CZ  . TYR   A 1 145 ? -20.702 63.759  104.354 1.00 121.88 ?  267 TYR   A CZ  1 
ATOM   785  O OH  . TYR   A 1 145 ? -19.517 64.329  104.809 1.00 113.20 ?  267 TYR   A OH  1 
ATOM   786  N N   . LYS   A 1 146 ? -27.168 63.328  102.402 1.00 130.99 ?  268 LYS   A N   1 
ATOM   787  C CA  . LYS   A 1 146 ? -28.018 64.171  103.244 1.00 135.99 ?  268 LYS   A CA  1 
ATOM   788  C C   . LYS   A 1 146 ? -27.504 64.154  104.673 1.00 137.99 ?  268 LYS   A C   1 
ATOM   789  O O   . LYS   A 1 146 ? -27.378 63.087  105.292 1.00 132.22 ?  268 LYS   A O   1 
ATOM   790  C CB  . LYS   A 1 146 ? -29.491 63.760  103.227 1.00 133.47 ?  268 LYS   A CB  1 
ATOM   791  C CG  . LYS   A 1 146 ? -30.269 64.169  101.990 1.00 141.30 ?  268 LYS   A CG  1 
ATOM   792  C CD  . LYS   A 1 146 ? -31.701 64.579  102.396 1.00 137.90 ?  268 LYS   A CD  1 
ATOM   793  C CE  . LYS   A 1 146 ? -32.509 65.093  101.204 1.00 135.85 ?  268 LYS   A CE  1 
ATOM   794  N NZ  . LYS   A 1 146 ? -33.979 65.046  101.432 1.00 134.09 ?  268 LYS   A NZ  1 
ATOM   795  N N   . ARG   A 1 147 ? -27.217 65.346  105.188 1.00 139.07 ?  269 ARG   A N   1 
ATOM   796  C CA  . ARG   A 1 147 ? -26.629 65.494  106.507 1.00 139.94 ?  269 ARG   A CA  1 
ATOM   797  C C   . ARG   A 1 147 ? -27.768 65.442  107.511 1.00 140.82 ?  269 ARG   A C   1 
ATOM   798  O O   . ARG   A 1 147 ? -28.688 66.261  107.427 1.00 141.70 ?  269 ARG   A O   1 
ATOM   799  C CB  . ARG   A 1 147 ? -25.885 66.826  106.586 1.00 144.42 ?  269 ARG   A CB  1 
ATOM   800  C CG  . ARG   A 1 147 ? -24.724 66.900  107.575 1.00 146.80 ?  269 ARG   A CG  1 
ATOM   801  C CD  . ARG   A 1 147 ? -23.978 68.233  107.402 1.00 154.77 ?  269 ARG   A CD  1 
ATOM   802  N NE  . ARG   A 1 147 ? -23.980 68.726  106.020 1.00 164.67 ?  269 ARG   A NE  1 
ATOM   803  C CZ  . ARG   A 1 147 ? -23.066 68.453  105.092 1.00 162.52 ?  269 ARG   A CZ  1 
ATOM   804  N NH1 . ARG   A 1 147 ? -22.029 67.668  105.346 1.00 151.35 ?  269 ARG   A NH1 1 
ATOM   805  N NH2 . ARG   A 1 147 ? -23.191 68.994  103.880 1.00 154.64 ?  269 ARG   A NH2 1 
ATOM   806  N N   . ILE   A 1 148 ? -27.748 64.468  108.429 1.00 141.40 ?  270 ILE   A N   1 
ATOM   807  C CA  . ILE   A 1 148 ? -28.788 64.435  109.460 1.00 144.65 ?  270 ILE   A CA  1 
ATOM   808  C C   . ILE   A 1 148 ? -28.607 65.592  110.440 1.00 153.62 ?  270 ILE   A C   1 
ATOM   809  O O   . ILE   A 1 148 ? -29.572 66.290  110.781 1.00 154.36 ?  270 ILE   A O   1 
ATOM   810  C CB  . ILE   A 1 148 ? -28.828 63.087  110.200 1.00 135.92 ?  270 ILE   A CB  1 
ATOM   811  C CG1 . ILE   A 1 148 ? -28.644 61.908  109.258 1.00 137.67 ?  270 ILE   A CG1 1 
ATOM   812  C CG2 . ILE   A 1 148 ? -30.158 62.934  110.898 1.00 134.85 ?  270 ILE   A CG2 1 
ATOM   813  C CD1 . ILE   A 1 148 ? -28.616 60.551  110.005 1.00 135.20 ?  270 ILE   A CD1 1 
ATOM   814  N N   . LYS   A 1 149 ? -27.364 65.806  110.922 1.00 153.78 ?  271 LYS   A N   1 
ATOM   815  C CA  . LYS   A 1 149 ? -27.009 66.960  111.752 1.00 154.44 ?  271 LYS   A CA  1 
ATOM   816  C C   . LYS   A 1 149 ? -26.558 68.114  110.861 1.00 157.37 ?  271 LYS   A C   1 
ATOM   817  O O   . LYS   A 1 149 ? -25.393 68.119  110.429 1.00 156.41 ?  271 LYS   A O   1 
ATOM   818  C CB  . LYS   A 1 149 ? -25.884 66.609  112.729 1.00 149.57 ?  271 LYS   A CB  1 
ATOM   819  C CG  . LYS   A 1 149 ? -26.151 65.417  113.618 1.00 144.30 ?  271 LYS   A CG  1 
ATOM   820  C CD  . LYS   A 1 149 ? -24.899 65.059  114.390 1.00 147.07 ?  271 LYS   A CD  1 
ATOM   821  C CE  . LYS   A 1 149 ? -25.124 63.864  115.305 1.00 147.77 ?  271 LYS   A CE  1 
ATOM   822  N NZ  . LYS   A 1 149 ? -25.496 64.280  116.683 1.00 155.29 ?  271 LYS   A NZ  1 
ATOM   823  N N   . PRO   A 1 150 ? -27.420 69.098  110.556 1.00 157.54 ?  272 PRO   A N   1 
ATOM   824  C CA  . PRO   A 1 150 ? -27.011 70.149  109.613 1.00 158.49 ?  272 PRO   A CA  1 
ATOM   825  C C   . PRO   A 1 150 ? -25.824 70.942  110.149 1.00 159.81 ?  272 PRO   A C   1 
ATOM   826  O O   . PRO   A 1 150 ? -25.491 70.905  111.340 1.00 151.48 ?  272 PRO   A O   1 
ATOM   827  C CB  . PRO   A 1 150 ? -28.266 71.021  109.437 1.00 144.48 ?  272 PRO   A CB  1 
ATOM   828  C CG  . PRO   A 1 150 ? -29.358 70.342  110.141 1.00 146.52 ?  272 PRO   A CG  1 
ATOM   829  C CD  . PRO   A 1 150 ? -28.799 69.283  111.044 1.00 149.31 ?  272 PRO   A CD  1 
ATOM   830  N N   . LEU   A 1 151 ? -25.179 71.652  109.225 1.00 159.89 ?  273 LEU   A N   1 
ATOM   831  C CA  . LEU   A 1 151 ? -23.798 72.074  109.392 1.00 157.08 ?  273 LEU   A CA  1 
ATOM   832  C C   . LEU   A 1 151 ? -23.610 72.856  110.692 1.00 160.88 ?  273 LEU   A C   1 
ATOM   833  O O   . LEU   A 1 151 ? -24.548 73.485  111.188 1.00 161.19 ?  273 LEU   A O   1 
ATOM   834  C CB  . LEU   A 1 151 ? -23.365 72.929  108.202 1.00 157.65 ?  273 LEU   A CB  1 
ATOM   835  C CG  . LEU   A 1 151 ? -22.750 72.147  107.036 1.00 160.36 ?  273 LEU   A CG  1 
ATOM   836  C CD1 . LEU   A 1 151 ? -22.555 73.026  105.774 1.00 153.67 ?  273 LEU   A CD1 1 
ATOM   837  C CD2 . LEU   A 1 151 ? -21.456 71.435  107.463 1.00 147.66 ?  273 LEU   A CD2 1 
ATOM   838  N N   . PRO   A 1 152 ? -22.413 72.795  111.282 1.00 164.79 ?  274 PRO   A N   1 
ATOM   839  C CA  . PRO   A 1 152 ? -22.101 73.626  112.454 1.00 160.98 ?  274 PRO   A CA  1 
ATOM   840  C C   . PRO   A 1 152 ? -22.489 75.095  112.296 1.00 157.82 ?  274 PRO   A C   1 
ATOM   841  O O   . PRO   A 1 152 ? -22.537 75.642  111.188 1.00 152.33 ?  274 PRO   A O   1 
ATOM   842  C CB  . PRO   A 1 152 ? -20.584 73.469  112.590 1.00 157.08 ?  274 PRO   A CB  1 
ATOM   843  C CG  . PRO   A 1 152 ? -20.331 72.039  112.117 1.00 157.43 ?  274 PRO   A CG  1 
ATOM   844  C CD  . PRO   A 1 152 ? -21.479 71.658  111.168 1.00 160.68 ?  274 PRO   A CD  1 
ATOM   845  N N   . THR   A 1 153 ? -22.747 75.728  113.449 1.00 161.93 ?  275 THR   A N   1 
ATOM   846  C CA  . THR   A 1 153 ? -23.211 77.113  113.484 1.00 159.12 ?  275 THR   A CA  1 
ATOM   847  C C   . THR   A 1 153 ? -22.131 78.073  112.993 1.00 153.19 ?  275 THR   A C   1 
ATOM   848  O O   . THR   A 1 153 ? -22.390 78.935  112.139 1.00 140.78 ?  275 THR   A O   1 
ATOM   849  C CB  . THR   A 1 153 ? -23.712 77.453  114.909 1.00 159.67 ?  275 THR   A CB  1 
ATOM   850  O OG1 . THR   A 1 153 ? -24.651 78.541  114.870 1.00 156.05 ?  275 THR   A OG1 1 
ATOM   851  C CG2 . THR   A 1 153 ? -22.578 77.697  115.948 1.00 151.48 ?  275 THR   A CG2 1 
ATOM   852  N N   . LYS   A 1 154 ? -20.899 77.895  113.474 1.00 151.44 ?  276 LYS   A N   1 
ATOM   853  C CA  . LYS   A 1 154 ? -19.807 78.804  113.179 1.00 144.85 ?  276 LYS   A CA  1 
ATOM   854  C C   . LYS   A 1 154 ? -18.588 78.016  112.740 1.00 135.27 ?  276 LYS   A C   1 
ATOM   855  O O   . LYS   A 1 154 ? -18.240 76.980  113.331 1.00 122.17 ?  276 LYS   A O   1 
ATOM   856  C CB  . LYS   A 1 154 ? -19.465 79.675  114.389 1.00 152.54 ?  276 LYS   A CB  1 
ATOM   857  C CG  . LYS   A 1 154 ? -20.219 81.010  114.445 1.00 154.87 ?  276 LYS   A CG  1 
ATOM   858  C CD  . LYS   A 1 154 ? -20.125 81.594  115.845 1.00 155.04 ?  276 LYS   A CD  1 
ATOM   859  C CE  . LYS   A 1 154 ? -21.163 80.905  116.742 1.00 158.02 ?  276 LYS   A CE  1 
ATOM   860  N NZ  . LYS   A 1 154 ? -20.697 80.616  118.136 1.00 156.58 ?  276 LYS   A NZ  1 
ATOM   861  N N   . LYS   A 1 155 ? -17.964 78.524  111.684 1.00 127.29 ?  277 LYS   A N   1 
ATOM   862  C CA  . LYS   A 1 155 ? -16.807 77.890  111.095 1.00 117.61 ?  277 LYS   A CA  1 
ATOM   863  C C   . LYS   A 1 155 ? -15.604 78.030  112.020 1.00 110.30 ?  277 LYS   A C   1 
ATOM   864  O O   . LYS   A 1 155 ? -15.551 78.895  112.890 1.00 118.40 ?  277 LYS   A O   1 
ATOM   865  C CB  . LYS   A 1 155 ? -16.530 78.495  109.713 1.00 121.64 ?  277 LYS   A CB  1 
ATOM   866  C CG  . LYS   A 1 155 ? -17.436 77.938  108.557 1.00 124.58 ?  277 LYS   A CG  1 
ATOM   867  C CD  . LYS   A 1 155 ? -17.563 78.903  107.335 1.00 122.44 ?  277 LYS   A CD  1 
ATOM   868  C CE  . LYS   A 1 155 ? -17.744 78.172  105.956 1.00 124.60 ?  277 LYS   A CE  1 
ATOM   869  N NZ  . LYS   A 1 155 ? -18.580 76.904  105.900 1.00 131.63 ?  277 LYS   A NZ  1 
ATOM   870  N N   . THR   A 1 156 ? -14.634 77.153  111.833 1.00 98.86  ?  278 THR   A N   1 
ATOM   871  C CA  . THR   A 1 156 ? -13.444 77.140  112.662 1.00 97.87  ?  278 THR   A CA  1 
ATOM   872  C C   . THR   A 1 156 ? -12.260 76.959  111.729 1.00 100.54 ?  278 THR   A C   1 
ATOM   873  O O   . THR   A 1 156 ? -12.230 75.989  110.974 1.00 103.34 ?  278 THR   A O   1 
ATOM   874  C CB  . THR   A 1 156 ? -13.535 76.000  113.661 1.00 96.64  ?  278 THR   A CB  1 
ATOM   875  O OG1 . THR   A 1 156 ? -14.896 75.898  114.078 1.00 101.35 ?  278 THR   A OG1 1 
ATOM   876  C CG2 . THR   A 1 156 ? -12.697 76.291  114.868 1.00 99.98  ?  278 THR   A CG2 1 
ATOM   877  N N   . GLY   A 1 157 ? -11.309 77.894  111.734 1.00 104.98 ?  279 GLY   A N   1 
ATOM   878  C CA  . GLY   A 1 157 ? -10.145 77.795  110.857 1.00 94.41  ?  279 GLY   A CA  1 
ATOM   879  C C   . GLY   A 1 157 ? -10.425 78.078  109.388 1.00 93.69  ?  279 GLY   A C   1 
ATOM   880  O O   . GLY   A 1 157 ? -11.545 77.858  108.910 1.00 95.40  ?  279 GLY   A O   1 
ATOM   881  N N   . LYS   A 1 158 ? -9.423  78.554  108.647 1.00 90.59  ?  280 LYS   A N   1 
ATOM   882  C CA  . LYS   A 1 158 ? -9.605  78.906  107.240 1.00 90.54  ?  280 LYS   A CA  1 
ATOM   883  C C   . LYS   A 1 158 ? -8.593  78.174  106.366 1.00 92.66  ?  280 LYS   A C   1 
ATOM   884  O O   . LYS   A 1 158 ? -7.378  78.274  106.599 1.00 88.97  ?  280 LYS   A O   1 
ATOM   885  C CB  . LYS   A 1 158 ? -9.473  80.412  107.029 1.00 93.01  ?  280 LYS   A CB  1 
ATOM   886  C CG  . LYS   A 1 158 ? -9.210  80.839  105.601 1.00 90.13  ?  280 LYS   A CG  1 
ATOM   887  C CD  . LYS   A 1 158 ? -10.496 80.813  104.776 1.00 100.49 ?  280 LYS   A CD  1 
ATOM   888  C CE  . LYS   A 1 158 ? -10.343 81.580  103.447 1.00 104.81 ?  280 LYS   A CE  1 
ATOM   889  N NZ  . LYS   A 1 158 ? -11.663 81.853  102.789 1.00 104.22 ?  280 LYS   A NZ  1 
ATOM   890  N N   . VAL   A 1 159 ? -9.110  77.459  105.357 1.00 90.63  ?  281 VAL   A N   1 
ATOM   891  C CA  . VAL   A 1 159 ? -8.345  76.648  104.410 1.00 82.13  ?  281 VAL   A CA  1 
ATOM   892  C C   . VAL   A 1 159 ? -8.632  77.134  103.006 1.00 83.47  ?  281 VAL   A C   1 
ATOM   893  O O   . VAL   A 1 159 ? -9.786  77.102  102.557 1.00 83.51  ?  281 VAL   A O   1 
ATOM   894  C CB  . VAL   A 1 159 ? -8.692  75.157  104.495 1.00 83.88  ?  281 VAL   A CB  1 
ATOM   895  C CG1 . VAL   A 1 159 ? -7.836  74.418  103.538 1.00 84.87  ?  281 VAL   A CG1 1 
ATOM   896  C CG2 . VAL   A 1 159 ? -8.448  74.614  105.879 1.00 81.71  ?  281 VAL   A CG2 1 
ATOM   897  N N   . ILE   A 1 160 ? -7.581  77.551  102.311 1.00 83.25  ?  282 ILE   A N   1 
ATOM   898  C CA  . ILE   A 1 160 ? -7.619  77.777  100.873 1.00 84.92  ?  282 ILE   A CA  1 
ATOM   899  C C   . ILE   A 1 160 ? -7.111  76.540  100.159 1.00 84.87  ?  282 ILE   A C   1 
ATOM   900  O O   . ILE   A 1 160 ? -6.065  75.988  100.524 1.00 79.18  ?  282 ILE   A O   1 
ATOM   901  C CB  . ILE   A 1 160 ? -6.817  79.030  100.482 1.00 82.16  ?  282 ILE   A CB  1 
ATOM   902  C CG1 . ILE   A 1 160 ? -7.630  80.257  100.872 1.00 88.47  ?  282 ILE   A CG1 1 
ATOM   903  C CG2 . ILE   A 1 160 ? -6.376  79.021  99.030  1.00 77.71  ?  282 ILE   A CG2 1 
ATOM   904  C CD1 . ILE   A 1 160 ? -8.946  80.366  100.073 1.00 86.13  ?  282 ILE   A CD1 1 
ATOM   905  N N   . ILE   A 1 161 ? -7.882  76.100  99.157  1.00 89.92  ?  283 ILE   A N   1 
ATOM   906  C CA  . ILE   A 1 161 ? -7.612  74.920  98.336  1.00 84.91  ?  283 ILE   A CA  1 
ATOM   907  C C   . ILE   A 1 161 ? -7.323  75.361  96.903  1.00 84.93  ?  283 ILE   A C   1 
ATOM   908  O O   . ILE   A 1 161 ? -8.174  75.981  96.253  1.00 85.05  ?  283 ILE   A O   1 
ATOM   909  C CB  . ILE   A 1 161 ? -8.787  73.943  98.370  1.00 82.23  ?  283 ILE   A CB  1 
ATOM   910  C CG1 . ILE   A 1 161 ? -8.739  73.134  99.655  1.00 85.68  ?  283 ILE   A CG1 1 
ATOM   911  C CG2 . ILE   A 1 161 ? -8.760  73.069  97.160  1.00 84.29  ?  283 ILE   A CG2 1 
ATOM   912  C CD1 . ILE   A 1 161 ? -9.799  72.062  99.701  1.00 89.03  ?  283 ILE   A CD1 1 
ATOM   913  N N   . ILE   A 1 162 ? -6.125  75.044  96.414  1.00 81.55  ?  284 ILE   A N   1 
ATOM   914  C CA  . ILE   A 1 162 ? -5.705  75.411  95.069  1.00 76.56  ?  284 ILE   A CA  1 
ATOM   915  C C   . ILE   A 1 162 ? -6.060  74.241  94.167  1.00 76.56  ?  284 ILE   A C   1 
ATOM   916  O O   . ILE   A 1 162 ? -5.453  73.171  94.262  1.00 72.13  ?  284 ILE   A O   1 
ATOM   917  C CB  . ILE   A 1 162 ? -4.209  75.723  95.004  1.00 72.52  ?  284 ILE   A CB  1 
ATOM   918  C CG1 . ILE   A 1 162 ? -3.857  76.833  95.966  1.00 69.79  ?  284 ILE   A CG1 1 
ATOM   919  C CG2 . ILE   A 1 162 ? -3.810  76.163  93.613  1.00 71.32  ?  284 ILE   A CG2 1 
ATOM   920  C CD1 . ILE   A 1 162 ? -2.423  77.191  95.912  1.00 67.71  ?  284 ILE   A CD1 1 
ATOM   921  N N   . GLY   A 1 163 ? -7.048  74.453  93.297  1.00 79.43  ?  285 GLY   A N   1 
ATOM   922  C CA  . GLY   A 1 163 ? -7.498  73.493  92.307  1.00 79.97  ?  285 GLY   A CA  1 
ATOM   923  C C   . GLY   A 1 163 ? -8.852  72.934  92.675  1.00 84.24  ?  285 GLY   A C   1 
ATOM   924  O O   . GLY   A 1 163 ? -9.007  72.426  93.785  1.00 88.50  ?  285 GLY   A O   1 
ATOM   925  N N   . SER   A 1 164 ? -9.852  73.040  91.795  1.00 84.03  ?  286 SER   A N   1 
ATOM   926  C CA  . SER   A 1 164 ? -11.115 72.338  91.999  1.00 84.68  ?  286 SER   A CA  1 
ATOM   927  C C   . SER   A 1 164 ? -11.174 71.050  91.182  1.00 92.40  ?  286 SER   A C   1 
ATOM   928  O O   . SER   A 1 164 ? -12.256 70.538  90.886  1.00 89.86  ?  286 SER   A O   1 
ATOM   929  C CB  . SER   A 1 164 ? -12.317 73.230  91.696  1.00 80.68  ?  286 SER   A CB  1 
ATOM   930  O OG  . SER   A 1 164 ? -12.415 73.518  90.317  1.00 85.67  ?  286 SER   A OG  1 
ATOM   931  N N   . GLY   A 1 165 ? -10.020 70.508  90.818  1.00 91.65  ?  287 GLY   A N   1 
ATOM   932  C CA  . GLY   A 1 165 ? -9.972  69.131  90.388  1.00 90.89  ?  287 GLY   A CA  1 
ATOM   933  C C   . GLY   A 1 165 ? -10.479 68.195  91.465  1.00 90.17  ?  287 GLY   A C   1 
ATOM   934  O O   . GLY   A 1 165 ? -10.793 68.572  92.591  1.00 86.94  ?  287 GLY   A O   1 
ATOM   935  N N   . VAL   A 1 166 ? -10.545 66.922  91.098  1.00 92.23  ?  288 VAL   A N   1 
ATOM   936  C CA  . VAL   A 1 166 ? -11.341 65.992  91.883  1.00 89.38  ?  288 VAL   A CA  1 
ATOM   937  C C   . VAL   A 1 166 ? -10.834 65.942  93.312  1.00 86.26  ?  288 VAL   A C   1 
ATOM   938  O O   . VAL   A 1 166 ? -11.617 65.988  94.265  1.00 84.80  ?  288 VAL   A O   1 
ATOM   939  C CB  . VAL   A 1 166 ? -11.317 64.607  91.235  1.00 86.52  ?  288 VAL   A CB  1 
ATOM   940  C CG1 . VAL   A 1 166 ? -12.123 63.599  92.104  1.00 72.01  ?  288 VAL   A CG1 1 
ATOM   941  C CG2 . VAL   A 1 166 ? -11.723 64.737  89.772  1.00 78.57  ?  288 VAL   A CG2 1 
ATOM   942  N N   . SER   A 1 167 ? -9.512  65.862  93.480  1.00 87.50  ?  289 SER   A N   1 
ATOM   943  C CA  . SER   A 1 167 ? -8.951  65.813  94.824  1.00 87.50  ?  289 SER   A CA  1 
ATOM   944  C C   . SER   A 1 167 ? -9.332  67.061  95.597  1.00 90.59  ?  289 SER   A C   1 
ATOM   945  O O   . SER   A 1 167 ? -9.749  66.984  96.763  1.00 84.01  ?  289 SER   A O   1 
ATOM   946  C CB  . SER   A 1 167 ? -7.434  65.654  94.764  1.00 83.75  ?  289 SER   A CB  1 
ATOM   947  O OG  . SER   A 1 167 ? -6.833  66.840  94.303  1.00 83.68  ?  289 SER   A OG  1 
ATOM   948  N N   . GLY   A 1 168 ? -9.218  68.227  94.945  1.00 92.86  ?  290 GLY   A N   1 
ATOM   949  C CA  . GLY   A 1 168 ? -9.645  69.474  95.552  1.00 88.51  ?  290 GLY   A CA  1 
ATOM   950  C C   . GLY   A 1 168 ? -11.043 69.355  96.121  1.00 86.76  ?  290 GLY   A C   1 
ATOM   951  O O   . GLY   A 1 168 ? -11.225 69.343  97.341  1.00 85.48  ?  290 GLY   A O   1 
ATOM   952  N N   . LEU   A 1 169 ? -12.022 69.217  95.218  1.00 88.98  ?  291 LEU   A N   1 
ATOM   953  C CA  . LEU   A 1 169 ? -13.430 69.082  95.584  1.00 87.56  ?  291 LEU   A CA  1 
ATOM   954  C C   . LEU   A 1 169 ? -13.634 68.073  96.707  1.00 85.44  ?  291 LEU   A C   1 
ATOM   955  O O   . LEU   A 1 169 ? -14.465 68.277  97.599  1.00 87.24  ?  291 LEU   A O   1 
ATOM   956  C CB  . LEU   A 1 169 ? -14.228 68.662  94.349  1.00 86.00  ?  291 LEU   A CB  1 
ATOM   957  C CG  . LEU   A 1 169 ? -13.940 69.497  93.109  1.00 89.48  ?  291 LEU   A CG  1 
ATOM   958  C CD1 . LEU   A 1 169 ? -14.407 68.803  91.855  1.00 88.25  ?  291 LEU   A CD1 1 
ATOM   959  C CD2 . LEU   A 1 169 ? -14.649 70.833  93.241  1.00 93.97  ?  291 LEU   A CD2 1 
ATOM   960  N N   . ALA   A 1 170 ? -12.887 66.979  96.680  1.00 78.74  ?  292 ALA   A N   1 
ATOM   961  C CA  . ALA   A 1 170 ? -13.157 65.915  97.627  1.00 79.81  ?  292 ALA   A CA  1 
ATOM   962  C C   . ALA   A 1 170 ? -12.717 66.312  99.018  1.00 84.22  ?  292 ALA   A C   1 
ATOM   963  O O   . ALA   A 1 170 ? -13.359 65.946  100.013 1.00 88.15  ?  292 ALA   A O   1 
ATOM   964  C CB  . ALA   A 1 170 ? -12.452 64.641  97.183  1.00 85.19  ?  292 ALA   A CB  1 
ATOM   965  N N   . ALA   A 1 171 ? -11.611 67.041  99.108  1.00 80.56  ?  293 ALA   A N   1 
ATOM   966  C CA  . ALA   A 1 171 ? -11.180 67.522  100.404 1.00 80.29  ?  293 ALA   A CA  1 
ATOM   967  C C   . ALA   A 1 171 ? -12.011 68.728  100.827 1.00 85.31  ?  293 ALA   A C   1 
ATOM   968  O O   . ALA   A 1 171 ? -12.421 68.826  101.989 1.00 87.23  ?  293 ALA   A O   1 
ATOM   969  C CB  . ALA   A 1 171 ? -9.689  67.841  100.361 1.00 77.98  ?  293 ALA   A CB  1 
ATOM   970  N N   . ALA   A 1 172 ? -12.301 69.638  99.892  1.00 87.40  ?  294 ALA   A N   1 
ATOM   971  C CA  . ALA   A 1 172 ? -13.153 70.778  100.212 1.00 89.10  ?  294 ALA   A CA  1 
ATOM   972  C C   . ALA   A 1 172 ? -14.465 70.312  100.836 1.00 89.85  ?  294 ALA   A C   1 
ATOM   973  O O   . ALA   A 1 172 ? -14.817 70.732  101.940 1.00 94.99  ?  294 ALA   A O   1 
ATOM   974  C CB  . ALA   A 1 172 ? -13.389 71.632  98.964  1.00 81.80  ?  294 ALA   A CB  1 
ATOM   975  N N   . ARG   A 1 173 ? -15.166 69.390  100.178 1.00 86.38  ?  295 ARG   A N   1 
ATOM   976  C CA  . ARG   A 1 173 ? -16.354 68.794  100.778 1.00 87.78  ?  295 ARG   A CA  1 
ATOM   977  C C   . ARG   A 1 173 ? -16.082 68.238  102.171 1.00 88.76  ?  295 ARG   A C   1 
ATOM   978  O O   . ARG   A 1 173 ? -16.848 68.490  103.098 1.00 93.33  ?  295 ARG   A O   1 
ATOM   979  C CB  . ARG   A 1 173 ? -16.899 67.696  99.879  1.00 88.38  ?  295 ARG   A CB  1 
ATOM   980  C CG  . ARG   A 1 173 ? -17.853 68.194  98.867  1.00 85.84  ?  295 ARG   A CG  1 
ATOM   981  C CD  . ARG   A 1 173 ? -18.935 67.200  98.766  1.00 88.04  ?  295 ARG   A CD  1 
ATOM   982  N NE  . ARG   A 1 173 ? -20.166 67.811  98.315  1.00 92.69  ?  295 ARG   A NE  1 
ATOM   983  C CZ  . ARG   A 1 173 ? -21.340 67.580  98.876  1.00 101.07 ?  295 ARG   A CZ  1 
ATOM   984  N NH1 . ARG   A 1 173 ? -21.456 66.758  99.915  1.00 99.48  ?  295 ARG   A NH1 1 
ATOM   985  N NH2 . ARG   A 1 173 ? -22.420 68.202  98.399  1.00 105.42 ?  295 ARG   A NH2 1 
ATOM   986  N N   . GLN   A 1 174 ? -15.007 67.463  102.338 1.00 89.90  ?  296 GLN   A N   1 
ATOM   987  C CA  . GLN   A 1 174 ? -14.726 66.857  103.645 1.00 96.27  ?  296 GLN   A CA  1 
ATOM   988  C C   . GLN   A 1 174 ? -14.379 67.912  104.703 1.00 96.20  ?  296 GLN   A C   1 
ATOM   989  O O   . GLN   A 1 174 ? -14.755 67.776  105.874 1.00 95.40  ?  296 GLN   A O   1 
ATOM   990  C CB  . GLN   A 1 174 ? -13.601 65.812  103.519 1.00 91.81  ?  296 GLN   A CB  1 
ATOM   991  C CG  . GLN   A 1 174 ? -14.008 64.363  103.232 1.00 85.47  ?  296 GLN   A CG  1 
ATOM   992  C CD  . GLN   A 1 174 ? -15.164 63.874  104.079 1.00 100.43 ?  296 GLN   A CD  1 
ATOM   993  O OE1 . GLN   A 1 174 ? -16.334 64.155  103.801 1.00 101.32 ?  296 GLN   A OE1 1 
ATOM   994  N NE2 . GLN   A 1 174 ? -14.839 63.096  105.109 1.00 104.73 ?  296 GLN   A NE2 1 
ATOM   995  N N   . LEU   A 1 175 ? -13.661 68.967  104.320 1.00 94.47  ?  297 LEU   A N   1 
ATOM   996  C CA  . LEU   A 1 175 ? -13.321 70.012  105.281 1.00 91.12  ?  297 LEU   A CA  1 
ATOM   997  C C   . LEU   A 1 175 ? -14.562 70.805  105.681 1.00 93.97  ?  297 LEU   A C   1 
ATOM   998  O O   . LEU   A 1 175 ? -14.916 70.867  106.862 1.00 96.08  ?  297 LEU   A O   1 
ATOM   999  C CB  . LEU   A 1 175 ? -12.229 70.906  104.699 1.00 81.01  ?  297 LEU   A CB  1 
ATOM   1000 C CG  . LEU   A 1 175 ? -10.866 70.224  104.646 1.00 78.18  ?  297 LEU   A CG  1 
ATOM   1001 C CD1 . LEU   A 1 175 ? -9.876  71.077  103.918 1.00 74.08  ?  297 LEU   A CD1 1 
ATOM   1002 C CD2 . LEU   A 1 175 ? -10.357 69.882  106.039 1.00 73.41  ?  297 LEU   A CD2 1 
ATOM   1003 N N   . GLN   A 1 176 ? -15.265 71.385  104.705 1.00 93.75  ?  298 GLN   A N   1 
ATOM   1004 C CA  . GLN   A 1 176 ? -16.566 71.980  104.996 1.00 93.55  ?  298 GLN   A CA  1 
ATOM   1005 C C   . GLN   A 1 176 ? -17.510 70.995  105.673 1.00 97.89  ?  298 GLN   A C   1 
ATOM   1006 O O   . GLN   A 1 176 ? -18.354 71.400  106.471 1.00 104.21 ?  298 GLN   A O   1 
ATOM   1007 C CB  . GLN   A 1 176 ? -17.219 72.495  103.725 1.00 94.06  ?  298 GLN   A CB  1 
ATOM   1008 C CG  . GLN   A 1 176 ? -18.503 73.197  104.030 1.00 112.13 ?  298 GLN   A CG  1 
ATOM   1009 C CD  . GLN   A 1 176 ? -19.321 73.509  102.809 1.00 121.23 ?  298 GLN   A CD  1 
ATOM   1010 O OE1 . GLN   A 1 176 ? -20.051 72.640  102.301 1.00 118.45 ?  298 GLN   A OE1 1 
ATOM   1011 N NE2 . GLN   A 1 176 ? -19.217 74.755  102.322 1.00 116.17 ?  298 GLN   A NE2 1 
ATOM   1012 N N   . SER   A 1 177 ? -17.398 69.699  105.362 1.00 102.22 ?  299 SER   A N   1 
ATOM   1013 C CA  . SER   A 1 177 ? -18.166 68.684  106.088 1.00 104.08 ?  299 SER   A CA  1 
ATOM   1014 C C   . SER   A 1 177 ? -17.856 68.714  107.568 1.00 99.14  ?  299 SER   A C   1 
ATOM   1015 O O   . SER   A 1 177 ? -18.701 68.349  108.386 1.00 100.74 ?  299 SER   A O   1 
ATOM   1016 C CB  . SER   A 1 177 ? -17.874 67.276  105.532 1.00 106.49 ?  299 SER   A CB  1 
ATOM   1017 O OG  . SER   A 1 177 ? -18.290 66.211  106.388 1.00 115.71 ?  299 SER   A OG  1 
ATOM   1018 N N   . PHE   A 1 178 ? -16.648 69.127  107.924 1.00 95.49  ?  300 PHE   A N   1 
ATOM   1019 C CA  . PHE   A 1 178 ? -16.171 69.119  109.296 1.00 100.14 ?  300 PHE   A CA  1 
ATOM   1020 C C   . PHE   A 1 178 ? -16.351 70.465  109.976 1.00 105.58 ?  300 PHE   A C   1 
ATOM   1021 O O   . PHE   A 1 178 ? -15.828 70.669  111.078 1.00 105.64 ?  300 PHE   A O   1 
ATOM   1022 C CB  . PHE   A 1 178 ? -14.699 68.730  109.315 1.00 105.43 ?  300 PHE   A CB  1 
ATOM   1023 C CG  . PHE   A 1 178 ? -14.435 67.338  108.816 1.00 107.05 ?  300 PHE   A CG  1 
ATOM   1024 C CD1 . PHE   A 1 178 ? -15.478 66.428  108.670 1.00 107.04 ?  300 PHE   A CD1 1 
ATOM   1025 C CD2 . PHE   A 1 178 ? -13.150 66.955  108.450 1.00 100.22 ?  300 PHE   A CD2 1 
ATOM   1026 C CE1 . PHE   A 1 178 ? -15.238 65.150  108.205 1.00 109.59 ?  300 PHE   A CE1 1 
ATOM   1027 C CE2 . PHE   A 1 178 ? -12.897 65.689  107.987 1.00 101.38 ?  300 PHE   A CE2 1 
ATOM   1028 C CZ  . PHE   A 1 178 ? -13.940 64.779  107.860 1.00 110.21 ?  300 PHE   A CZ  1 
ATOM   1029 N N   . GLY   A 1 179 ? -17.075 71.384  109.336 1.00 110.91 ?  301 GLY   A N   1 
ATOM   1030 C CA  . GLY   A 1 179 ? -17.166 72.768  109.758 1.00 106.41 ?  301 GLY   A CA  1 
ATOM   1031 C C   . GLY   A 1 179 ? -16.040 73.777  109.636 1.00 103.76 ?  301 GLY   A C   1 
ATOM   1032 O O   . GLY   A 1 179 ? -15.847 74.591  110.540 1.00 109.04 ?  301 GLY   A O   1 
ATOM   1033 N N   . MET   A 1 180 ? -15.264 73.721  108.558 1.00 95.40  ?  302 MET   A N   1 
ATOM   1034 C CA  . MET   A 1 180 ? -14.286 74.756  108.271 1.00 92.12  ?  302 MET   A CA  1 
ATOM   1035 C C   . MET   A 1 180 ? -14.608 75.725  107.153 1.00 97.79  ?  302 MET   A C   1 
ATOM   1036 O O   . MET   A 1 180 ? -15.495 75.482  106.332 1.00 100.92 ?  302 MET   A O   1 
ATOM   1037 C CB  . MET   A 1 180 ? -12.990 73.979  107.971 1.00 85.48  ?  302 MET   A CB  1 
ATOM   1038 C CG  . MET   A 1 180 ? -12.439 73.200  109.151 1.00 87.00  ?  302 MET   A CG  1 
ATOM   1039 S SD  . MET   A 1 180 ? -10.701 72.659  109.104 1.00 91.52  ?  302 MET   A SD  1 
ATOM   1040 C CE  . MET   A 1 180 ? -9.712  74.117  109.197 1.00 79.79  ?  302 MET   A CE  1 
ATOM   1041 N N   . ASP   A 1 181 ? -13.913 76.856  107.153 1.00 98.88  ?  303 ASP   A N   1 
ATOM   1042 C CA  . ASP   A 1 181 ? -14.099 77.830  106.087 1.00 102.22 ?  303 ASP   A CA  1 
ATOM   1043 C C   . ASP   A 1 181 ? -13.210 77.383  104.939 1.00 102.41 ?  303 ASP   A C   1 
ATOM   1044 O O   . ASP   A 1 181 ? -11.997 77.616  104.942 1.00 98.41  ?  303 ASP   A O   1 
ATOM   1045 C CB  . ASP   A 1 181 ? -13.762 79.243  106.548 1.00 102.95 ?  303 ASP   A CB  1 
ATOM   1046 C CG  . ASP   A 1 181 ? -14.127 80.319  105.495 1.00 116.65 ?  303 ASP   A CG  1 
ATOM   1047 O OD1 . ASP   A 1 181 ? -14.442 79.974  104.322 1.00 115.96 ?  303 ASP   A OD1 1 
ATOM   1048 O OD2 . ASP   A 1 181 ? -14.105 81.527  105.845 1.00 121.98 ?  303 ASP   A OD2 1 
ATOM   1049 N N   . VAL   A 1 182 ? -13.807 76.716  103.960 1.00 96.92  ?  304 VAL   A N   1 
ATOM   1050 C CA  . VAL   A 1 182 ? -13.072 76.246  102.805 1.00 91.14  ?  304 VAL   A CA  1 
ATOM   1051 C C   . VAL   A 1 182 ? -13.454 77.085  101.607 1.00 96.39  ?  304 VAL   A C   1 
ATOM   1052 O O   . VAL   A 1 182 ? -14.641 77.308  101.336 1.00 97.19  ?  304 VAL   A O   1 
ATOM   1053 C CB  . VAL   A 1 182 ? -13.325 74.762  102.542 1.00 90.65  ?  304 VAL   A CB  1 
ATOM   1054 C CG1 . VAL   A 1 182 ? -12.764 74.377  101.198 1.00 91.78  ?  304 VAL   A CG1 1 
ATOM   1055 C CG2 . VAL   A 1 182 ? -12.621 74.000  103.583 1.00 94.57  ?  304 VAL   A CG2 1 
ATOM   1056 N N   . THR   A 1 183 ? -12.438 77.544  100.894 1.00 95.17  ?  305 THR   A N   1 
ATOM   1057 C CA  . THR   A 1 183 ? -12.621 78.200  99.618  1.00 95.79  ?  305 THR   A CA  1 
ATOM   1058 C C   . THR   A 1 183 ? -11.572 77.695  98.639  1.00 98.38  ?  305 THR   A C   1 
ATOM   1059 O O   . THR   A 1 183 ? -10.387 77.600  98.987  1.00 92.52  ?  305 THR   A O   1 
ATOM   1060 C CB  . THR   A 1 183 ? -12.550 79.703  99.807  1.00 97.03  ?  305 THR   A CB  1 
ATOM   1061 O OG1 . THR   A 1 183 ? -13.673 80.082  100.616 1.00 105.72 ?  305 THR   A OG1 1 
ATOM   1062 C CG2 . THR   A 1 183 ? -12.562 80.435  98.462  1.00 90.27  ?  305 THR   A CG2 1 
ATOM   1063 N N   . LEU   A 1 184 ? -12.034 77.346  97.427  1.00 97.31  ?  306 LEU   A N   1 
ATOM   1064 C CA  . LEU   A 1 184 ? -11.227 76.757  96.369  1.00 88.37  ?  306 LEU   A CA  1 
ATOM   1065 C C   . LEU   A 1 184 ? -10.961 77.766  95.258  1.00 83.16  ?  306 LEU   A C   1 
ATOM   1066 O O   . LEU   A 1 184 ? -11.869 78.488  94.837  1.00 81.78  ?  306 LEU   A O   1 
ATOM   1067 C CB  . LEU   A 1 184 ? -11.908 75.523  95.758  1.00 91.92  ?  306 LEU   A CB  1 
ATOM   1068 C CG  . LEU   A 1 184 ? -12.471 74.315  96.512  1.00 89.55  ?  306 LEU   A CG  1 
ATOM   1069 C CD1 . LEU   A 1 184 ? -13.959 74.435  96.711  1.00 92.00  ?  306 LEU   A CD1 1 
ATOM   1070 C CD2 . LEU   A 1 184 ? -12.132 73.044  95.757  1.00 87.64  ?  306 LEU   A CD2 1 
ATOM   1071 N N   . LEU   A 1 185 ? -9.716  77.772  94.769  1.00 81.92  ?  307 LEU   A N   1 
ATOM   1072 C CA  . LEU   A 1 185 ? -9.230  78.684  93.738  1.00 85.59  ?  307 LEU   A CA  1 
ATOM   1073 C C   . LEU   A 1 185 ? -8.903  77.887  92.496  1.00 83.05  ?  307 LEU   A C   1 
ATOM   1074 O O   . LEU   A 1 185 ? -8.004  77.045  92.528  1.00 82.40  ?  307 LEU   A O   1 
ATOM   1075 C CB  . LEU   A 1 185 ? -7.971  79.429  94.177  1.00 85.73  ?  307 LEU   A CB  1 
ATOM   1076 C CG  . LEU   A 1 185 ? -8.026  80.177  95.493  1.00 83.23  ?  307 LEU   A CG  1 
ATOM   1077 C CD1 . LEU   A 1 185 ? -6.776  80.982  95.636  1.00 80.56  ?  307 LEU   A CD1 1 
ATOM   1078 C CD2 . LEU   A 1 185 ? -9.254  81.038  95.488  1.00 81.48  ?  307 LEU   A CD2 1 
ATOM   1079 N N   . GLU   A 1 186 ? -9.563  78.225  91.393  1.00 87.99  ?  308 GLU   A N   1 
ATOM   1080 C CA  . GLU   A 1 186 ? -9.520  77.470  90.145  1.00 91.11  ?  308 GLU   A CA  1 
ATOM   1081 C C   . GLU   A 1 186 ? -9.090  78.383  89.004  1.00 91.17  ?  308 GLU   A C   1 
ATOM   1082 O O   . GLU   A 1 186 ? -9.747  79.395  88.741  1.00 93.32  ?  308 GLU   A O   1 
ATOM   1083 C CB  . GLU   A 1 186 ? -10.904 76.873  89.865  1.00 92.24  ?  308 GLU   A CB  1 
ATOM   1084 C CG  . GLU   A 1 186 ? -11.033 76.120  88.574  1.00 93.92  ?  308 GLU   A CG  1 
ATOM   1085 C CD  . GLU   A 1 186 ? -10.002 75.043  88.434  1.00 94.91  ?  308 GLU   A CD  1 
ATOM   1086 O OE1 . GLU   A 1 186 ? -9.805  74.275  89.401  1.00 93.09  ?  308 GLU   A OE1 1 
ATOM   1087 O OE2 . GLU   A 1 186 ? -9.395  74.968  87.351  1.00 96.00  ?  308 GLU   A OE2 1 
ATOM   1088 N N   . ALA   A 1 187 ? -8.011  78.022  88.306  1.00 89.85  ?  309 ALA   A N   1 
ATOM   1089 C CA  . ALA   A 1 187 ? -7.600  78.828  87.155  1.00 91.81  ?  309 ALA   A CA  1 
ATOM   1090 C C   . ALA   A 1 187 ? -8.568  78.714  85.977  1.00 95.65  ?  309 ALA   A C   1 
ATOM   1091 O O   . ALA   A 1 187 ? -8.562  79.581  85.091  1.00 93.46  ?  309 ALA   A O   1 
ATOM   1092 C CB  . ALA   A 1 187 ? -6.192  78.437  86.698  1.00 86.48  ?  309 ALA   A CB  1 
ATOM   1093 N N   . ARG   A 1 188 ? -9.399  77.677  85.953  1.00 98.70  ?  310 ARG   A N   1 
ATOM   1094 C CA  . ARG   A 1 188 ? -10.248 77.359  84.814  1.00 101.13 ?  310 ARG   A CA  1 
ATOM   1095 C C   . ARG   A 1 188 ? -11.624 77.992  84.980  1.00 103.33 ?  310 ARG   A C   1 
ATOM   1096 O O   . ARG   A 1 188 ? -11.983 78.493  86.052  1.00 104.59 ?  310 ARG   A O   1 
ATOM   1097 C CB  . ARG   A 1 188 ? -10.396 75.848  84.676  1.00 100.65 ?  310 ARG   A CB  1 
ATOM   1098 C CG  . ARG   A 1 188 ? -9.167  75.110  84.176  1.00 99.53  ?  310 ARG   A CG  1 
ATOM   1099 C CD  . ARG   A 1 188 ? -9.455  73.608  84.182  1.00 100.74 ?  310 ARG   A CD  1 
ATOM   1100 N NE  . ARG   A 1 188 ? -8.243  72.822  84.009  1.00 98.75  ?  310 ARG   A NE  1 
ATOM   1101 C CZ  . ARG   A 1 188 ? -7.690  72.573  82.831  1.00 93.54  ?  310 ARG   A CZ  1 
ATOM   1102 N NH1 . ARG   A 1 188 ? -8.190  73.083  81.713  1.00 94.62  ?  310 ARG   A NH1 1 
ATOM   1103 N NH2 . ARG   A 1 188 ? -6.606  71.802  82.774  1.00 91.47  ?  310 ARG   A NH2 1 
ATOM   1104 N N   . ASP   A 1 189 ? -12.409 77.956  83.901  1.00 100.18 ?  311 ASP   A N   1 
ATOM   1105 C CA  . ASP   A 1 189 ? -13.807 78.353  83.958  1.00 98.18  ?  311 ASP   A CA  1 
ATOM   1106 C C   . ASP   A 1 189 ? -14.721 77.190  84.248  1.00 92.49  ?  311 ASP   A C   1 
ATOM   1107 O O   . ASP   A 1 189 ? -15.922 77.292  83.998  1.00 93.19  ?  311 ASP   A O   1 
ATOM   1108 C CB  . ASP   A 1 189 ? -14.231 79.027  82.659  1.00 101.57 ?  311 ASP   A CB  1 
ATOM   1109 C CG  . ASP   A 1 189 ? -13.616 78.372  81.460  1.00 110.23 ?  311 ASP   A CG  1 
ATOM   1110 O OD1 . ASP   A 1 189 ? -12.785 77.472  81.702  1.00 112.03 ?  311 ASP   A OD1 1 
ATOM   1111 O OD2 . ASP   A 1 189 ? -13.961 78.728  80.302  1.00 111.09 ?  311 ASP   A OD2 1 
ATOM   1112 N N   . ARG   A 1 190 ? -14.180 76.097  84.779  1.00 91.17  ?  312 ARG   A N   1 
ATOM   1113 C CA  . ARG   A 1 190 ? -14.943 74.895  85.091  1.00 94.51  ?  312 ARG   A CA  1 
ATOM   1114 C C   . ARG   A 1 190 ? -14.234 74.135  86.202  1.00 99.41  ?  312 ARG   A C   1 
ATOM   1115 O O   . ARG   A 1 190 ? -13.004 74.196  86.331  1.00 101.84 ?  312 ARG   A O   1 
ATOM   1116 C CB  . ARG   A 1 190 ? -15.089 73.999  83.851  1.00 101.58 ?  312 ARG   A CB  1 
ATOM   1117 C CG  . ARG   A 1 190 ? -13.729 73.676  83.217  1.00 103.82 ?  312 ARG   A CG  1 
ATOM   1118 C CD  . ARG   A 1 190 ? -13.761 73.020  81.826  1.00 103.26 ?  312 ARG   A CD  1 
ATOM   1119 N NE  . ARG   A 1 190 ? -12.492 72.340  81.582  1.00 107.52 ?  312 ARG   A NE  1 
ATOM   1120 C CZ  . ARG   A 1 190 ? -12.021 71.328  82.307  1.00 102.25 ?  312 ARG   A CZ  1 
ATOM   1121 N NH1 . ARG   A 1 190 ? -12.779 70.690  83.190  1.00 95.45  ?  312 ARG   A NH1 1 
ATOM   1122 N NH2 . ARG   A 1 190 ? -10.763 70.933  82.131  1.00 95.76  ?  312 ARG   A NH2 1 
ATOM   1123 N N   . VAL   A 1 191 ? -15.004 73.293  86.856  1.00 95.59  ?  313 VAL   A N   1 
ATOM   1124 C CA  . VAL   A 1 191 ? -14.412 72.424  87.887  1.00 97.33  ?  313 VAL   A CA  1 
ATOM   1125 C C   . VAL   A 1 191 ? -14.010 71.128  87.201  1.00 98.38  ?  313 VAL   A C   1 
ATOM   1126 O O   . VAL   A 1 191 ? -14.260 71.014  86.009  1.00 105.44 ?  313 VAL   A O   1 
ATOM   1127 C CB  . VAL   A 1 191 ? -15.477 72.155  88.947  1.00 94.09  ?  313 VAL   A CB  1 
ATOM   1128 C CG1 . VAL   A 1 191 ? -15.543 73.275  89.965  1.00 91.65  ?  313 VAL   A CG1 1 
ATOM   1129 C CG2 . VAL   A 1 191 ? -16.836 71.937  88.310  1.00 90.82  ?  313 VAL   A CG2 1 
ATOM   1130 N N   . GLY   A 1 192 ? -13.376 70.215  87.917  1.00 95.48  ?  314 GLY   A N   1 
ATOM   1131 C CA  . GLY   A 1 192 ? -13.064 68.898  87.402  1.00 94.34  ?  314 GLY   A CA  1 
ATOM   1132 C C   . GLY   A 1 192 ? -11.630 68.708  86.949  1.00 93.67  ?  314 GLY   A C   1 
ATOM   1133 O O   . GLY   A 1 192 ? -11.073 67.608  87.114  1.00 89.40  ?  314 GLY   A O   1 
ATOM   1134 N N   . GLY   A 1 193 ? -11.020 69.749  86.391  1.00 97.87  ?  315 GLY   A N   1 
ATOM   1135 C CA  . GLY   A 1 193 ? -9.654  69.609  85.908  1.00 99.36  ?  315 GLY   A CA  1 
ATOM   1136 C C   . GLY   A 1 193 ? -9.555  68.546  84.831  1.00 93.59  ?  315 GLY   A C   1 
ATOM   1137 O O   . GLY   A 1 193 ? -10.342 68.531  83.873  1.00 92.90  ?  315 GLY   A O   1 
ATOM   1138 N N   . ARG   A 1 194 ? -8.591  67.627  85.006  1.00 93.06  ?  316 ARG   A N   1 
ATOM   1139 C CA  . ARG   A 1 194 ? -8.374  66.494  84.101  1.00 90.58  ?  316 ARG   A CA  1 
ATOM   1140 C C   . ARG   A 1 194 ? -9.617  65.683  83.735  1.00 92.49  ?  316 ARG   A C   1 
ATOM   1141 O O   . ARG   A 1 194 ? -9.591  64.916  82.773  1.00 93.48  ?  316 ARG   A O   1 
ATOM   1142 C CB  . ARG   A 1 194 ? -7.112  65.717  84.484  1.00 83.32  ?  316 ARG   A CB  1 
ATOM   1143 C CG  . ARG   A 1 194 ? -5.799  66.365  84.147  1.00 79.80  ?  316 ARG   A CG  1 
ATOM   1144 C CD  . ARG   A 1 194 ? -4.670  65.615  84.850  1.00 80.46  ?  316 ARG   A CD  1 
ATOM   1145 N NE  . ARG   A 1 194 ? -4.472  66.060  86.223  1.00 78.22  ?  316 ARG   A NE  1 
ATOM   1146 C CZ  . ARG   A 1 194 ? -3.453  65.700  86.988  1.00 82.10  ?  316 ARG   A CZ  1 
ATOM   1147 N NH1 . ARG   A 1 194 ? -2.485  64.926  86.523  1.00 84.21  ?  316 ARG   A NH1 1 
ATOM   1148 N NH2 . ARG   A 1 194 ? -3.395  66.143  88.247  1.00 84.20  ?  316 ARG   A NH2 1 
ATOM   1149 N N   . VAL   A 1 195 ? -10.678 65.785  84.530  1.00 93.86  ?  317 VAL   A N   1 
ATOM   1150 C CA  . VAL   A 1 195 ? -11.997 65.286  84.178  1.00 85.65  ?  317 VAL   A CA  1 
ATOM   1151 C C   . VAL   A 1 195 ? -12.830 66.239  83.338  1.00 93.92  ?  317 VAL   A C   1 
ATOM   1152 O O   . VAL   A 1 195 ? -13.647 67.012  83.851  1.00 97.83  ?  317 VAL   A O   1 
ATOM   1153 C CB  . VAL   A 1 195 ? -12.670 64.900  85.506  1.00 82.65  ?  317 VAL   A CB  1 
ATOM   1154 C CG1 . VAL   A 1 195 ? -14.103 64.466  85.299  1.00 80.90  ?  317 VAL   A CG1 1 
ATOM   1155 C CG2 . VAL   A 1 195 ? -11.883 63.818  86.188  1.00 78.59  ?  317 VAL   A CG2 1 
ATOM   1156 N N   . ALA   A 1 196 ? -12.545 66.257  82.045  1.00 96.43  ?  318 ALA   A N   1 
ATOM   1157 C CA  . ALA   A 1 196 ? -13.161 67.180  81.107  1.00 96.00  ?  318 ALA   A CA  1 
ATOM   1158 C C   . ALA   A 1 196 ? -14.198 66.433  80.295  1.00 97.10  ?  318 ALA   A C   1 
ATOM   1159 O O   . ALA   A 1 196 ? -13.868 65.432  79.661  1.00 105.97 ?  318 ALA   A O   1 
ATOM   1160 C CB  . ALA   A 1 196 ? -12.104 67.768  80.175  1.00 92.36  ?  318 ALA   A CB  1 
ATOM   1161 N N   . THR   A 1 197 ? -15.439 66.900  80.308  1.00 98.03  ?  319 THR   A N   1 
ATOM   1162 C CA  . THR   A 1 197 ? -16.438 66.393  79.377  1.00 101.69 ?  319 THR   A CA  1 
ATOM   1163 C C   . THR   A 1 197 ? -16.757 67.433  78.317  1.00 111.26 ?  319 THR   A C   1 
ATOM   1164 O O   . THR   A 1 197 ? -16.961 68.611  78.635  1.00 118.03 ?  319 THR   A O   1 
ATOM   1165 C CB  . THR   A 1 197 ? -17.716 65.975  80.083  1.00 103.07 ?  319 THR   A CB  1 
ATOM   1166 O OG1 . THR   A 1 197 ? -17.491 64.760  80.805  1.00 99.96  ?  319 THR   A OG1 1 
ATOM   1167 C CG2 . THR   A 1 197 ? -18.826 65.794  79.085  1.00 107.86 ?  319 THR   A CG2 1 
ATOM   1168 N N   . PHE   A 1 198 ? -16.773 66.991  77.059  1.00 110.91 ?  320 PHE   A N   1 
ATOM   1169 C CA  . PHE   A 1 198 ? -17.219 67.800  75.936  1.00 115.43 ?  320 PHE   A CA  1 
ATOM   1170 C C   . PHE   A 1 198 ? -18.714 67.577  75.734  1.00 118.04 ?  320 PHE   A C   1 
ATOM   1171 O O   . PHE   A 1 198 ? -19.183 66.432  75.732  1.00 116.59 ?  320 PHE   A O   1 
ATOM   1172 C CB  . PHE   A 1 198 ? -16.428 67.441  74.672  1.00 113.78 ?  320 PHE   A CB  1 
ATOM   1173 C CG  . PHE   A 1 198 ? -17.017 67.995  73.398  1.00 114.68 ?  320 PHE   A CG  1 
ATOM   1174 C CD1 . PHE   A 1 198 ? -16.734 69.282  72.993  1.00 116.46 ?  320 PHE   A CD1 1 
ATOM   1175 C CD2 . PHE   A 1 198 ? -17.833 67.219  72.599  1.00 114.49 ?  320 PHE   A CD2 1 
ATOM   1176 C CE1 . PHE   A 1 198 ? -17.272 69.790  71.831  1.00 119.10 ?  320 PHE   A CE1 1 
ATOM   1177 C CE2 . PHE   A 1 198 ? -18.369 67.724  71.440  1.00 113.28 ?  320 PHE   A CE2 1 
ATOM   1178 C CZ  . PHE   A 1 198 ? -18.086 69.010  71.055  1.00 117.05 ?  320 PHE   A CZ  1 
ATOM   1179 N N   . ARG   A 1 199 ? -19.459 68.672  75.584  1.00 117.96 ?  321 ARG   A N   1 
ATOM   1180 C CA  . ARG   A 1 199 ? -20.898 68.603  75.371  1.00 116.12 ?  321 ARG   A CA  1 
ATOM   1181 C C   . ARG   A 1 199 ? -21.262 69.631  74.313  1.00 120.40 ?  321 ARG   A C   1 
ATOM   1182 O O   . ARG   A 1 199 ? -20.907 70.806  74.442  1.00 125.17 ?  321 ARG   A O   1 
ATOM   1183 C CB  . ARG   A 1 199 ? -21.663 68.844  76.678  1.00 115.00 ?  321 ARG   A CB  1 
ATOM   1184 C CG  . ARG   A 1 199 ? -21.710 67.621  77.608  1.00 112.38 ?  321 ARG   A CG  1 
ATOM   1185 C CD  . ARG   A 1 199 ? -22.384 67.930  78.949  1.00 112.70 ?  321 ARG   A CD  1 
ATOM   1186 N NE  . ARG   A 1 199 ? -21.777 67.243  80.091  1.00 116.90 ?  321 ARG   A NE  1 
ATOM   1187 C CZ  . ARG   A 1 199 ? -22.225 66.106  80.623  1.00 120.27 ?  321 ARG   A CZ  1 
ATOM   1188 N NH1 . ARG   A 1 199 ? -23.322 65.512  80.173  1.00 117.75 ?  321 ARG   A NH1 1 
ATOM   1189 N NH2 . ARG   A 1 199 ? -21.560 65.553  81.638  1.00 113.54 ?  321 ARG   A NH2 1 
ATOM   1190 N N   . LYS   A 1 200 ? -21.904 69.168  73.241  1.00 124.78 ?  322 LYS   A N   1 
ATOM   1191 C CA  . LYS   A 1 200 ? -22.500 70.009  72.206  1.00 127.78 ?  322 LYS   A CA  1 
ATOM   1192 C C   . LYS   A 1 200 ? -23.701 69.237  71.682  1.00 127.88 ?  322 LYS   A C   1 
ATOM   1193 O O   . LYS   A 1 200 ? -23.580 68.046  71.382  1.00 128.20 ?  322 LYS   A O   1 
ATOM   1194 C CB  . LYS   A 1 200 ? -21.510 70.337  71.076  1.00 121.14 ?  322 LYS   A CB  1 
ATOM   1195 C CG  . LYS   A 1 200 ? -21.478 71.802  70.658  1.00 123.60 ?  322 LYS   A CG  1 
ATOM   1196 C CD  . LYS   A 1 200 ? -20.886 71.976  69.257  1.00 136.12 ?  322 LYS   A CD  1 
ATOM   1197 C CE  . LYS   A 1 200 ? -20.674 73.459  68.888  1.00 141.14 ?  322 LYS   A CE  1 
ATOM   1198 N NZ  . LYS   A 1 200 ? -20.819 73.771  67.420  1.00 140.07 ?  322 LYS   A NZ  1 
ATOM   1199 N N   . GLY   A 1 201 ? -24.851 69.902  71.606  1.00 124.26 ?  323 GLY   A N   1 
ATOM   1200 C CA  . GLY   A 1 201 ? -26.105 69.211  71.378  1.00 126.36 ?  323 GLY   A CA  1 
ATOM   1201 C C   . GLY   A 1 201 ? -26.268 67.936  72.190  1.00 127.17 ?  323 GLY   A C   1 
ATOM   1202 O O   . GLY   A 1 201 ? -26.219 67.948  73.422  1.00 118.53 ?  323 GLY   A O   1 
ATOM   1203 N N   . ASN   A 1 202 ? -26.453 66.823  71.487  1.00 133.77 ?  324 ASN   A N   1 
ATOM   1204 C CA  . ASN   A 1 202 ? -26.611 65.497  72.070  1.00 132.34 ?  324 ASN   A CA  1 
ATOM   1205 C C   . ASN   A 1 202 ? -25.287 64.765  72.196  1.00 130.87 ?  324 ASN   A C   1 
ATOM   1206 O O   . ASN   A 1 202 ? -25.259 63.637  72.709  1.00 121.46 ?  324 ASN   A O   1 
ATOM   1207 C CB  . ASN   A 1 202 ? -27.551 64.664  71.204  1.00 137.53 ?  324 ASN   A CB  1 
ATOM   1208 C CG  . ASN   A 1 202 ? -28.910 65.302  71.053  1.00 146.55 ?  324 ASN   A CG  1 
ATOM   1209 O OD1 . ASN   A 1 202 ? -29.341 66.088  71.915  1.00 147.44 ?  324 ASN   A OD1 1 
ATOM   1210 N ND2 . ASN   A 1 202 ? -29.579 65.020  69.918  1.00 142.91 ?  324 ASN   A ND2 1 
ATOM   1211 N N   . TYR   A 1 203 ? -24.202 65.368  71.709  1.00 130.71 ?  325 TYR   A N   1 
ATOM   1212 C CA  . TYR   A 1 203 ? -22.892 64.744  71.774  1.00 132.02 ?  325 TYR   A CA  1 
ATOM   1213 C C   . TYR   A 1 203 ? -22.297 64.876  73.174  1.00 128.99 ?  325 TYR   A C   1 
ATOM   1214 O O   . TYR   A 1 203 ? -22.430 65.914  73.830  1.00 127.46 ?  325 TYR   A O   1 
ATOM   1215 C CB  . TYR   A 1 203 ? -21.941 65.360  70.746  1.00 129.75 ?  325 TYR   A CB  1 
ATOM   1216 C CG  . TYR   A 1 203 ? -22.340 65.177  69.295  1.00 136.00 ?  325 TYR   A CG  1 
ATOM   1217 C CD1 . TYR   A 1 203 ? -22.717 63.924  68.803  1.00 132.13 ?  325 TYR   A CD1 1 
ATOM   1218 C CD2 . TYR   A 1 203 ? -22.247 66.244  68.393  1.00 141.48 ?  325 TYR   A CD2 1 
ATOM   1219 C CE1 . TYR   A 1 203 ? -23.062 63.756  67.468  1.00 136.76 ?  325 TYR   A CE1 1 
ATOM   1220 C CE2 . TYR   A 1 203 ? -22.577 66.089  67.054  1.00 143.35 ?  325 TYR   A CE2 1 
ATOM   1221 C CZ  . TYR   A 1 203 ? -22.985 64.843  66.593  1.00 145.78 ?  325 TYR   A CZ  1 
ATOM   1222 O OH  . TYR   A 1 203 ? -23.312 64.698  65.256  1.00 146.54 ?  325 TYR   A OH  1 
ATOM   1223 N N   . VAL   A 1 204 ? -21.624 63.818  73.616  1.00 123.28 ?  326 VAL   A N   1 
ATOM   1224 C CA  . VAL   A 1 204 ? -21.013 63.748  74.935  1.00 110.56 ?  326 VAL   A CA  1 
ATOM   1225 C C   . VAL   A 1 204 ? -19.759 62.899  74.823  1.00 114.91 ?  326 VAL   A C   1 
ATOM   1226 O O   . VAL   A 1 204 ? -19.825 61.769  74.329  1.00 123.44 ?  326 VAL   A O   1 
ATOM   1227 C CB  . VAL   A 1 204 ? -22.003 63.136  75.938  1.00 115.71 ?  326 VAL   A CB  1 
ATOM   1228 C CG1 . VAL   A 1 204 ? -21.270 62.569  77.137  1.00 120.47 ?  326 VAL   A CG1 1 
ATOM   1229 C CG2 . VAL   A 1 204 ? -23.047 64.159  76.341  1.00 115.63 ?  326 VAL   A CG2 1 
ATOM   1230 N N   . ALA   A 1 205 ? -18.614 63.424  75.274  1.00 110.14 ?  327 ALA   A N   1 
ATOM   1231 C CA  . ALA   A 1 205 ? -17.349 62.684  75.154  1.00 115.18 ?  327 ALA   A CA  1 
ATOM   1232 C C   . ALA   A 1 205 ? -16.291 63.228  76.113  1.00 110.64 ?  327 ALA   A C   1 
ATOM   1233 O O   . ALA   A 1 205 ? -15.908 64.398  75.993  1.00 109.86 ?  327 ALA   A O   1 
ATOM   1234 C CB  . ALA   A 1 205 ? -16.839 62.754  73.702  1.00 113.83 ?  327 ALA   A CB  1 
ATOM   1235 N N   . ASP   A 1 206 ? -15.774 62.388  77.033  1.00 101.26 ?  328 ASP   A N   1 
ATOM   1236 C CA  . ASP   A 1 206 ? -14.693 62.840  77.919  1.00 100.90 ?  328 ASP   A CA  1 
ATOM   1237 C C   . ASP   A 1 206 ? -13.379 62.937  77.152  1.00 99.36  ?  328 ASP   A C   1 
ATOM   1238 O O   . ASP   A 1 206 ? -12.898 61.944  76.598  1.00 104.72 ?  328 ASP   A O   1 
ATOM   1239 C CB  . ASP   A 1 206 ? -14.472 61.917  79.125  1.00 103.55 ?  328 ASP   A CB  1 
ATOM   1240 C CG  . ASP   A 1 206 ? -15.727 61.635  79.920  1.00 110.44 ?  328 ASP   A CG  1 
ATOM   1241 O OD1 . ASP   A 1 206 ? -16.263 62.564  80.562  1.00 104.31 ?  328 ASP   A OD1 1 
ATOM   1242 O OD2 . ASP   A 1 206 ? -16.152 60.451  79.924  1.00 121.32 ?  328 ASP   A OD2 1 
ATOM   1243 N N   . LEU   A 1 207 ? -12.786 64.121  77.140  1.00 92.88  ?  329 LEU   A N   1 
ATOM   1244 C CA  . LEU   A 1 207 ? -11.372 64.291  76.847  1.00 87.35  ?  329 LEU   A CA  1 
ATOM   1245 C C   . LEU   A 1 207 ? -10.492 63.918  78.030  1.00 91.91  ?  329 LEU   A C   1 
ATOM   1246 O O   . LEU   A 1 207 ? -9.263  64.008  77.922  1.00 87.10  ?  329 LEU   A O   1 
ATOM   1247 C CB  . LEU   A 1 207 ? -11.143 65.739  76.474  1.00 88.12  ?  329 LEU   A CB  1 
ATOM   1248 C CG  . LEU   A 1 207 ? -12.223 66.117  75.477  1.00 95.35  ?  329 LEU   A CG  1 
ATOM   1249 C CD1 . LEU   A 1 207 ? -12.625 67.548  75.633  1.00 99.82  ?  329 LEU   A CD1 1 
ATOM   1250 C CD2 . LEU   A 1 207 ? -11.597 65.943  74.119  1.00 99.92  ?  329 LEU   A CD2 1 
ATOM   1251 N N   . GLY   A 1 208 ? -11.102 63.509  79.149  1.00 94.30  ?  330 GLY   A N   1 
ATOM   1252 C CA  . GLY   A 1 208 ? -10.428 63.390  80.424  1.00 90.77  ?  330 GLY   A CA  1 
ATOM   1253 C C   . GLY   A 1 208 ? -10.382 61.961  80.864  1.00 87.63  ?  330 GLY   A C   1 
ATOM   1254 O O   . GLY   A 1 208 ? -10.179 61.095  80.031  1.00 96.49  ?  330 GLY   A O   1 
ATOM   1255 N N   . ALA   A 1 209 ? -10.527 61.688  82.150  1.00 90.43  ?  331 ALA   A N   1 
ATOM   1256 C CA  . ALA   A 1 209 ? -10.773 60.320  82.574  1.00 97.81  ?  331 ALA   A CA  1 
ATOM   1257 C C   . ALA   A 1 209 ? -12.096 59.827  81.995  1.00 104.04 ?  331 ALA   A C   1 
ATOM   1258 O O   . ALA   A 1 209 ? -13.022 60.614  81.717  1.00 98.67  ?  331 ALA   A O   1 
ATOM   1259 C CB  . ALA   A 1 209 ? -10.783 60.205  84.092  1.00 94.31  ?  331 ALA   A CB  1 
ATOM   1260 N N   . MET   A 1 210 ? -12.103 58.529  81.672  1.00 100.83 ?  332 MET   A N   1 
ATOM   1261 C CA  . MET   A 1 210 ? -13.256 57.890  81.001  1.00 98.39  ?  332 MET   A CA  1 
ATOM   1262 C C   . MET   A 1 210 ? -13.550 56.569  81.697  1.00 100.21 ?  332 MET   A C   1 
ATOM   1263 O O   . MET   A 1 210 ? -14.671 56.378  82.141  1.00 98.34  ?  332 MET   A O   1 
ATOM   1264 C CB  . MET   A 1 210 ? -12.815 57.539  79.587  1.00 98.62  ?  332 MET   A CB  1 
ATOM   1265 C CG  . MET   A 1 210 ? -13.867 56.943  78.701  1.00 109.72 ?  332 MET   A CG  1 
ATOM   1266 S SD  . MET   A 1 210 ? -13.127 56.733  77.067  1.00 128.37 ?  332 MET   A SD  1 
ATOM   1267 C CE  . MET   A 1 210 ? -13.205 58.416  76.459  1.00 107.14 ?  332 MET   A CE  1 
ATOM   1268 N N   . VAL   A 1 211 ? -12.576 55.673  81.725  1.00 101.52 ?  333 VAL   A N   1 
ATOM   1269 C CA  . VAL   A 1 211 ? -12.749 54.370  82.372  1.00 100.25 ?  333 VAL   A CA  1 
ATOM   1270 C C   . VAL   A 1 211 ? -12.985 54.525  83.883  1.00 93.11  ?  333 VAL   A C   1 
ATOM   1271 O O   . VAL   A 1 211 ? -12.644 55.542  84.501  1.00 87.97  ?  333 VAL   A O   1 
ATOM   1272 C CB  . VAL   A 1 211 ? -11.493 53.516  82.073  1.00 107.77 ?  333 VAL   A CB  1 
ATOM   1273 C CG1 . VAL   A 1 211 ? -11.619 52.084  82.556  1.00 106.63 ?  333 VAL   A CG1 1 
ATOM   1274 C CG2 . VAL   A 1 211 ? -11.100 53.549  80.576  1.00 105.62 ?  333 VAL   A CG2 1 
ATOM   1275 N N   . VAL   A 1 212 ? -13.597 53.500  84.482  1.00 94.23  ?  334 VAL   A N   1 
ATOM   1276 C CA  . VAL   A 1 212 ? -13.702 53.338  85.942  1.00 97.75  ?  334 VAL   A CA  1 
ATOM   1277 C C   . VAL   A 1 212 ? -13.221 51.924  86.242  1.00 93.59  ?  334 VAL   A C   1 
ATOM   1278 O O   . VAL   A 1 212 ? -13.999 50.975  86.113  1.00 92.96  ?  334 VAL   A O   1 
ATOM   1279 C CB  . VAL   A 1 212 ? -15.136 53.541  86.478  1.00 89.50  ?  334 VAL   A CB  1 
ATOM   1280 C CG1 . VAL   A 1 212 ? -15.222 53.229  87.946  1.00 78.23  ?  334 VAL   A CG1 1 
ATOM   1281 C CG2 . VAL   A 1 212 ? -15.601 54.935  86.283  1.00 83.12  ?  334 VAL   A CG2 1 
ATOM   1282 N N   . THR   A 1 213 ? -11.955 51.767  86.655  1.00 91.11  ?  335 THR   A N   1 
ATOM   1283 C CA  . THR   A 1 213 ? -11.510 50.432  87.036  1.00 96.17  ?  335 THR   A CA  1 
ATOM   1284 C C   . THR   A 1 213 ? -12.493 49.875  88.059  1.00 97.74  ?  335 THR   A C   1 
ATOM   1285 O O   . THR   A 1 213 ? -13.118 50.626  88.809  1.00 101.40 ?  335 THR   A O   1 
ATOM   1286 C CB  . THR   A 1 213 ? -10.074 50.421  87.583  1.00 98.48  ?  335 THR   A CB  1 
ATOM   1287 O OG1 . THR   A 1 213 ? -10.050 50.876  88.933  1.00 96.86  ?  335 THR   A OG1 1 
ATOM   1288 C CG2 . THR   A 1 213 ? -9.161  51.302  86.729  1.00 95.73  ?  335 THR   A CG2 1 
ATOM   1289 N N   . GLY   A 1 214 ? -12.667 48.556  88.049  1.00 101.97 ?  336 GLY   A N   1 
ATOM   1290 C CA  . GLY   A 1 214 ? -13.932 47.956  88.470  1.00 103.69 ?  336 GLY   A CA  1 
ATOM   1291 C C   . GLY   A 1 214 ? -14.305 48.299  89.897  1.00 98.40  ?  336 GLY   A C   1 
ATOM   1292 O O   . GLY   A 1 214 ? -13.488 48.759  90.682  1.00 105.42 ?  336 GLY   A O   1 
ATOM   1293 N N   . LEU   A 1 215 ? -15.603 48.224  90.176  1.00 94.34  ?  337 LEU   A N   1 
ATOM   1294 C CA  . LEU   A 1 215 ? -16.132 48.685  91.477  1.00 97.33  ?  337 LEU   A CA  1 
ATOM   1295 C C   . LEU   A 1 215 ? -15.881 47.540  92.442  1.00 97.56  ?  337 LEU   A C   1 
ATOM   1296 O O   . LEU   A 1 215 ? -16.836 47.019  93.010  1.00 93.28  ?  337 LEU   A O   1 
ATOM   1297 C CB  . LEU   A 1 215 ? -17.642 48.841  91.327  1.00 86.56  ?  337 LEU   A CB  1 
ATOM   1298 C CG  . LEU   A 1 215 ? -18.120 49.345  89.972  1.00 88.18  ?  337 LEU   A CG  1 
ATOM   1299 C CD1 . LEU   A 1 215 ? -19.634 49.417  89.942  1.00 90.79  ?  337 LEU   A CD1 1 
ATOM   1300 C CD2 . LEU   A 1 215 ? -17.523 50.705  89.674  1.00 97.00  ?  337 LEU   A CD2 1 
ATOM   1301 N N   . GLY   A 1 216 ? -14.626 47.203  92.635  1.00 98.90  ?  338 GLY   A N   1 
ATOM   1302 C CA  . GLY   A 1 216 ? -14.326 46.072  93.514  1.00 104.61 ?  338 GLY   A CA  1 
ATOM   1303 C C   . GLY   A 1 216 ? -13.445 46.881  94.427  1.00 104.48 ?  338 GLY   A C   1 
ATOM   1304 O O   . GLY   A 1 216 ? -12.289 47.100  94.086  1.00 104.97 ?  338 GLY   A O   1 
ATOM   1305 N N   . GLY   A 1 217 ? -13.972 47.293  95.561  1.00 106.67 ?  339 GLY   A N   1 
ATOM   1306 C CA  . GLY   A 1 217 ? -13.165 48.160  96.425  1.00 106.87 ?  339 GLY   A CA  1 
ATOM   1307 C C   . GLY   A 1 217 ? -12.900 49.564  95.972  1.00 99.38  ?  339 GLY   A C   1 
ATOM   1308 O O   . GLY   A 1 217 ? -11.961 50.195  96.446  1.00 97.30  ?  339 GLY   A O   1 
ATOM   1309 N N   . ASN   A 1 218 ? -13.725 50.007  95.054  1.00 97.23  ?  340 ASN   A N   1 
ATOM   1310 C CA  . ASN   A 1 218 ? -13.521 51.329  94.498  1.00 98.59  ?  340 ASN   A CA  1 
ATOM   1311 C C   . ASN   A 1 218 ? -14.347 52.344  95.291  1.00 100.61 ?  340 ASN   A C   1 
ATOM   1312 O O   . ASN   A 1 218 ? -15.555 52.138  95.482  1.00 99.10  ?  340 ASN   A O   1 
ATOM   1313 C CB  . ASN   A 1 218 ? -13.902 51.339  93.019  1.00 92.58  ?  340 ASN   A CB  1 
ATOM   1314 C CG  . ASN   A 1 218 ? -13.430 52.577  92.303  1.00 93.46  ?  340 ASN   A CG  1 
ATOM   1315 O OD1 . ASN   A 1 218 ? -13.105 53.577  92.927  1.00 98.16  ?  340 ASN   A OD1 1 
ATOM   1316 N ND2 . ASN   A 1 218 ? -13.316 52.495  90.988  1.00 91.36  ?  340 ASN   A ND2 1 
ATOM   1317 N N   . PRO   A 1 219 ? -13.734 53.414  95.815  1.00 98.87  ?  341 PRO   A N   1 
ATOM   1318 C CA  . PRO   A 1 219 ? -14.540 54.481  96.404  1.00 96.14  ?  341 PRO   A CA  1 
ATOM   1319 C C   . PRO   A 1 219 ? -15.476 55.082  95.402  1.00 93.70  ?  341 PRO   A C   1 
ATOM   1320 O O   . PRO   A 1 219 ? -16.492 55.663  95.801  1.00 98.23  ?  341 PRO   A O   1 
ATOM   1321 C CB  . PRO   A 1 219 ? -13.494 55.502  96.878  1.00 92.68  ?  341 PRO   A CB  1 
ATOM   1322 C CG  . PRO   A 1 219 ? -12.279 55.195  96.099  1.00 90.91  ?  341 PRO   A CG  1 
ATOM   1323 C CD  . PRO   A 1 219 ? -12.298 53.708  95.955  1.00 99.20  ?  341 PRO   A CD  1 
ATOM   1324 N N   . MET   A 1 220 ? -15.167 54.964  94.108  1.00 89.31  ?  342 MET   A N   1 
ATOM   1325 C CA  . MET   A 1 220 ? -16.066 55.482  93.084  1.00 90.86  ?  342 MET   A CA  1 
ATOM   1326 C C   . MET   A 1 220 ? -17.382 54.726  93.056  1.00 95.40  ?  342 MET   A C   1 
ATOM   1327 O O   . MET   A 1 220 ? -18.406 55.281  92.637  1.00 93.00  ?  342 MET   A O   1 
ATOM   1328 C CB  . MET   A 1 220 ? -15.403 55.415  91.721  1.00 88.00  ?  342 MET   A CB  1 
ATOM   1329 C CG  . MET   A 1 220 ? -14.259 56.359  91.522  1.00 87.28  ?  342 MET   A CG  1 
ATOM   1330 S SD  . MET   A 1 220 ? -14.751 58.022  91.916  1.00 86.03  ?  342 MET   A SD  1 
ATOM   1331 C CE  . MET   A 1 220 ? -15.651 58.495  90.444  1.00 86.97  ?  342 MET   A CE  1 
ATOM   1332 N N   . ALA   A 1 221 ? -17.366 53.456  93.475  1.00 96.65  ?  343 ALA   A N   1 
ATOM   1333 C CA  . ALA   A 1 221 ? -18.602 52.703  93.652  1.00 96.95  ?  343 ALA   A CA  1 
ATOM   1334 C C   . ALA   A 1 221 ? -19.585 53.454  94.546  1.00 103.33 ?  343 ALA   A C   1 
ATOM   1335 O O   . ALA   A 1 221 ? -20.752 53.647  94.182  1.00 103.88 ?  343 ALA   A O   1 
ATOM   1336 C CB  . ALA   A 1 221 ? -18.283 51.335  94.241  1.00 100.99 ?  343 ALA   A CB  1 
ATOM   1337 N N   . VAL   A 1 222 ? -19.113 53.889  95.725  1.00 104.59 ?  344 VAL   A N   1 
ATOM   1338 C CA  . VAL   A 1 222 ? -19.917 54.697  96.647  1.00 102.35 ?  344 VAL   A CA  1 
ATOM   1339 C C   . VAL   A 1 222 ? -20.447 55.947  95.951  1.00 98.24  ?  344 VAL   A C   1 
ATOM   1340 O O   . VAL   A 1 222 ? -21.623 56.304  96.078  1.00 100.02 ?  344 VAL   A O   1 
ATOM   1341 C CB  . VAL   A 1 222 ? -19.072 55.060  97.882  1.00 93.54  ?  344 VAL   A CB  1 
ATOM   1342 C CG1 . VAL   A 1 222 ? -19.832 55.977  98.822  1.00 97.18  ?  344 VAL   A CG1 1 
ATOM   1343 C CG2 . VAL   A 1 222 ? -18.611 53.812  98.571  1.00 98.72  ?  344 VAL   A CG2 1 
ATOM   1344 N N   . VAL   A 1 223 ? -19.585 56.628  95.208  1.00 92.04  ?  345 VAL   A N   1 
ATOM   1345 C CA  . VAL   A 1 223 ? -19.975 57.870  94.564  1.00 97.36  ?  345 VAL   A CA  1 
ATOM   1346 C C   . VAL   A 1 223 ? -21.088 57.628  93.562  1.00 107.87 ?  345 VAL   A C   1 
ATOM   1347 O O   . VAL   A 1 223 ? -22.003 58.449  93.411  1.00 111.56 ?  345 VAL   A O   1 
ATOM   1348 C CB  . VAL   A 1 223 ? -18.748 58.494  93.889  1.00 96.72  ?  345 VAL   A CB  1 
ATOM   1349 C CG1 . VAL   A 1 223 ? -19.145 59.717  93.022  1.00 91.18  ?  345 VAL   A CG1 1 
ATOM   1350 C CG2 . VAL   A 1 223 ? -17.680 58.789  94.938  1.00 90.39  ?  345 VAL   A CG2 1 
ATOM   1351 N N   . SER   A 1 224 ? -21.013 56.503  92.843  1.00 110.00 ?  346 SER   A N   1 
ATOM   1352 C CA  . SER   A 1 224 ? -21.911 56.249  91.718  1.00 112.04 ?  346 SER   A CA  1 
ATOM   1353 C C   . SER   A 1 224 ? -23.321 55.942  92.189  1.00 112.26 ?  346 SER   A C   1 
ATOM   1354 O O   . SER   A 1 224 ? -24.288 56.134  91.443  1.00 116.21 ?  346 SER   A O   1 
ATOM   1355 C CB  . SER   A 1 224 ? -21.361 55.096  90.896  1.00 104.03 ?  346 SER   A CB  1 
ATOM   1356 O OG  . SER   A 1 224 ? -20.926 54.082  91.789  1.00 104.61 ?  346 SER   A OG  1 
ATOM   1357 N N   . LYS   A 1 225 ? -23.440 55.424  93.406  1.00 105.64 ?  347 LYS   A N   1 
ATOM   1358 C CA  . LYS   A 1 225 ? -24.732 55.323  94.054  1.00 109.00 ?  347 LYS   A CA  1 
ATOM   1359 C C   . LYS   A 1 225 ? -25.244 56.709  94.441  1.00 109.26 ?  347 LYS   A C   1 
ATOM   1360 O O   . LYS   A 1 225 ? -26.456 56.974  94.395  1.00 106.60 ?  347 LYS   A O   1 
ATOM   1361 C CB  . LYS   A 1 225 ? -24.571 54.428  95.281  1.00 113.73 ?  347 LYS   A CB  1 
ATOM   1362 C CG  . LYS   A 1 225 ? -24.432 52.923  95.026  1.00 105.61 ?  347 LYS   A CG  1 
ATOM   1363 C CD  . LYS   A 1 225 ? -23.721 52.340  96.238  1.00 108.19 ?  347 LYS   A CD  1 
ATOM   1364 C CE  . LYS   A 1 225 ? -23.865 50.859  96.438  1.00 112.32 ?  347 LYS   A CE  1 
ATOM   1365 N NZ  . LYS   A 1 225 ? -23.199 50.515  97.731  1.00 114.50 ?  347 LYS   A NZ  1 
ATOM   1366 N N   . GLN   A 1 226 ? -24.323 57.606  94.804  1.00 111.74 ?  348 GLN   A N   1 
ATOM   1367 C CA  . GLN   A 1 226 ? -24.666 58.952  95.253  1.00 115.35 ?  348 GLN   A CA  1 
ATOM   1368 C C   . GLN   A 1 226 ? -24.951 59.891  94.090  1.00 113.95 ?  348 GLN   A C   1 
ATOM   1369 O O   . GLN   A 1 226 ? -25.700 60.857  94.248  1.00 113.96 ?  348 GLN   A O   1 
ATOM   1370 C CB  . GLN   A 1 226 ? -23.525 59.526  96.094  1.00 109.11 ?  348 GLN   A CB  1 
ATOM   1371 C CG  . GLN   A 1 226 ? -23.468 58.996  97.503  1.00 110.47 ?  348 GLN   A CG  1 
ATOM   1372 C CD  . GLN   A 1 226 ? -22.221 59.452  98.223  1.00 111.55 ?  348 GLN   A CD  1 
ATOM   1373 O OE1 . GLN   A 1 226 ? -21.496 60.311  97.732  1.00 109.97 ?  348 GLN   A OE1 1 
ATOM   1374 N NE2 . GLN   A 1 226 ? -21.950 58.865  99.381  1.00 113.43 ?  348 GLN   A NE2 1 
ATOM   1375 N N   . VAL   A 1 227 ? -24.355 59.637  92.934  1.00 112.76 ?  349 VAL   A N   1 
ATOM   1376 C CA  . VAL   A 1 227 ? -24.538 60.462  91.754  1.00 113.25 ?  349 VAL   A CA  1 
ATOM   1377 C C   . VAL   A 1 227 ? -25.047 59.578  90.634  1.00 123.51 ?  349 VAL   A C   1 
ATOM   1378 O O   . VAL   A 1 227 ? -24.546 58.464  90.444  1.00 123.48 ?  349 VAL   A O   1 
ATOM   1379 C CB  . VAL   A 1 227 ? -23.222 61.138  91.358  1.00 112.72 ?  349 VAL   A CB  1 
ATOM   1380 C CG1 . VAL   A 1 227 ? -23.333 61.734  89.958  1.00 113.29 ?  349 VAL   A CG1 1 
ATOM   1381 C CG2 . VAL   A 1 227 ? -22.885 62.161  92.393  1.00 111.60 ?  349 VAL   A CG2 1 
ATOM   1382 N N   . ASN   A 1 228 ? -26.040 60.063  89.891  1.00 131.07 ?  350 ASN   A N   1 
ATOM   1383 C CA  . ASN   A 1 228 ? -26.615 59.229  88.837  1.00 142.92 ?  350 ASN   A CA  1 
ATOM   1384 C C   . ASN   A 1 228 ? -25.643 59.228  87.660  1.00 140.80 ?  350 ASN   A C   1 
ATOM   1385 O O   . ASN   A 1 228 ? -25.673 60.095  86.776  1.00 133.76 ?  350 ASN   A O   1 
ATOM   1386 C CB  . ASN   A 1 228 ? -28.000 59.713  88.421  1.00 153.64 ?  350 ASN   A CB  1 
ATOM   1387 C CG  . ASN   A 1 228 ? -28.673 58.760  87.427  1.00 157.80 ?  350 ASN   A CG  1 
ATOM   1388 O OD1 . ASN   A 1 228 ? -28.412 57.544  87.442  1.00 154.74 ?  350 ASN   A OD1 1 
ATOM   1389 N ND2 . ASN   A 1 228 ? -29.512 59.310  86.540  1.00 153.54 ?  350 ASN   A ND2 1 
ATOM   1390 N N   . MET   A 1 229 ? -24.752 58.245  87.665  1.00 134.44 ?  351 MET   A N   1 
ATOM   1391 C CA  . MET   A 1 229 ? -23.901 58.002  86.521  1.00 127.31 ?  351 MET   A CA  1 
ATOM   1392 C C   . MET   A 1 229 ? -24.431 56.800  85.770  1.00 133.51 ?  351 MET   A C   1 
ATOM   1393 O O   . MET   A 1 229 ? -25.064 55.906  86.344  1.00 135.21 ?  351 MET   A O   1 
ATOM   1394 C CB  . MET   A 1 229 ? -22.458 57.738  86.921  1.00 122.57 ?  351 MET   A CB  1 
ATOM   1395 C CG  . MET   A 1 229 ? -21.941 58.609  88.010  1.00 124.27 ?  351 MET   A CG  1 
ATOM   1396 S SD  . MET   A 1 229 ? -20.664 57.704  88.881  1.00 120.98 ?  351 MET   A SD  1 
ATOM   1397 C CE  . MET   A 1 229 ? -19.268 57.962  87.770  1.00 110.37 ?  351 MET   A CE  1 
ATOM   1398 N N   . GLU   A 1 230 ? -24.153 56.792  84.477  1.00 130.67 ?  352 GLU   A N   1 
ATOM   1399 C CA  . GLU   A 1 230 ? -24.537 55.714  83.584  1.00 125.19 ?  352 GLU   A CA  1 
ATOM   1400 C C   . GLU   A 1 230 ? -23.273 54.896  83.354  1.00 122.38 ?  352 GLU   A C   1 
ATOM   1401 O O   . GLU   A 1 230 ? -22.470 55.205  82.473  1.00 121.53 ?  352 GLU   A O   1 
ATOM   1402 C CB  . GLU   A 1 230 ? -25.111 56.290  82.299  1.00 127.80 ?  352 GLU   A CB  1 
ATOM   1403 C CG  . GLU   A 1 230 ? -26.330 55.568  81.783  1.00 141.50 ?  352 GLU   A CG  1 
ATOM   1404 C CD  . GLU   A 1 230 ? -26.940 56.260  80.569  1.00 154.92 ?  352 GLU   A CD  1 
ATOM   1405 O OE1 . GLU   A 1 230 ? -26.974 57.521  80.548  1.00 147.98 ?  352 GLU   A OE1 1 
ATOM   1406 O OE2 . GLU   A 1 230 ? -27.370 55.536  79.634  1.00 161.34 ?  352 GLU   A OE2 1 
ATOM   1407 N N   . LEU   A 1 231 ? -23.081 53.860  84.177  1.00 118.90 ?  353 LEU   A N   1 
ATOM   1408 C CA  . LEU   A 1 231 ? -21.917 52.978  84.075  1.00 117.34 ?  353 LEU   A CA  1 
ATOM   1409 C C   . LEU   A 1 231 ? -22.207 51.789  83.153  1.00 121.17 ?  353 LEU   A C   1 
ATOM   1410 O O   . LEU   A 1 231 ? -22.883 50.833  83.556  1.00 122.83 ?  353 LEU   A O   1 
ATOM   1411 C CB  . LEU   A 1 231 ? -21.484 52.475  85.449  1.00 110.58 ?  353 LEU   A CB  1 
ATOM   1412 C CG  . LEU   A 1 231 ? -20.870 53.438  86.440  1.00 105.00 ?  353 LEU   A CG  1 
ATOM   1413 C CD1 . LEU   A 1 231 ? -20.035 52.667  87.451  1.00 90.71  ?  353 LEU   A CD1 1 
ATOM   1414 C CD2 . LEU   A 1 231 ? -20.019 54.399  85.680  1.00 112.20 ?  353 LEU   A CD2 1 
ATOM   1415 N N   . ALA   A 1 232 ? -21.669 51.839  81.927  1.00 121.13 ?  354 ALA   A N   1 
ATOM   1416 C CA  . ALA   A 1 232 ? -21.678 50.737  80.969  1.00 115.00 ?  354 ALA   A CA  1 
ATOM   1417 C C   . ALA   A 1 232 ? -20.362 49.974  81.072  1.00 115.82 ?  354 ALA   A C   1 
ATOM   1418 O O   . ALA   A 1 232 ? -19.336 50.545  81.451  1.00 116.11 ?  354 ALA   A O   1 
ATOM   1419 C CB  . ALA   A 1 232 ? -21.871 51.254  79.537  1.00 113.02 ?  354 ALA   A CB  1 
ATOM   1420 N N   . LYS   A 1 233 ? -20.389 48.678  80.749  1.00 115.53 ?  355 LYS   A N   1 
ATOM   1421 C CA  . LYS   A 1 233 ? -19.135 47.940  80.799  1.00 111.85 ?  355 LYS   A CA  1 
ATOM   1422 C C   . LYS   A 1 233 ? -18.346 48.113  79.502  1.00 119.09 ?  355 LYS   A C   1 
ATOM   1423 O O   . LYS   A 1 233 ? -18.850 48.570  78.474  1.00 119.51 ?  355 LYS   A O   1 
ATOM   1424 C CB  . LYS   A 1 233 ? -19.367 46.466  81.081  1.00 105.39 ?  355 LYS   A CB  1 
ATOM   1425 C CG  . LYS   A 1 233 ? -20.272 46.214  82.270  1.00 117.53 ?  355 LYS   A CG  1 
ATOM   1426 C CD  . LYS   A 1 233 ? -20.626 44.722  82.408  1.00 133.62 ?  355 LYS   A CD  1 
ATOM   1427 C CE  . LYS   A 1 233 ? -20.639 44.246  83.865  1.00 128.74 ?  355 LYS   A CE  1 
ATOM   1428 N NZ  . LYS   A 1 233 ? -20.278 42.794  84.010  1.00 138.31 ?  355 LYS   A NZ  1 
ATOM   1429 N N   . ILE   A 1 234 ? -17.068 47.785  79.587  1.00 122.38 ?  356 ILE   A N   1 
ATOM   1430 C CA  . ILE   A 1 234 ? -16.162 47.810  78.451  1.00 125.29 ?  356 ILE   A CA  1 
ATOM   1431 C C   . ILE   A 1 234 ? -16.085 46.382  77.938  1.00 132.61 ?  356 ILE   A C   1 
ATOM   1432 O O   . ILE   A 1 234 ? -15.572 45.497  78.632  1.00 132.72 ?  356 ILE   A O   1 
ATOM   1433 C CB  . ILE   A 1 234 ? -14.778 48.346  78.844  1.00 123.94 ?  356 ILE   A CB  1 
ATOM   1434 C CG1 . ILE   A 1 234 ? -14.714 49.861  78.727  1.00 114.08 ?  356 ILE   A CG1 1 
ATOM   1435 C CG2 . ILE   A 1 234 ? -13.652 47.700  78.038  1.00 131.26 ?  356 ILE   A CG2 1 
ATOM   1436 C CD1 . ILE   A 1 234 ? -13.357 50.359  79.153  1.00 117.29 ?  356 ILE   A CD1 1 
ATOM   1437 N N   . LYS   A 1 235 ? -16.643 46.146  76.746  1.00 138.75 ?  357 LYS   A N   1 
ATOM   1438 C CA  . LYS   A 1 235 ? -16.567 44.839  76.096  1.00 132.94 ?  357 LYS   A CA  1 
ATOM   1439 C C   . LYS   A 1 235 ? -15.175 44.725  75.490  1.00 130.55 ?  357 LYS   A C   1 
ATOM   1440 O O   . LYS   A 1 235 ? -14.848 45.433  74.531  1.00 130.50 ?  357 LYS   A O   1 
ATOM   1441 C CB  . LYS   A 1 235 ? -17.668 44.669  75.043  1.00 139.21 ?  357 LYS   A CB  1 
ATOM   1442 C CG  . LYS   A 1 235 ? -19.135 44.888  75.534  1.00 141.29 ?  357 LYS   A CG  1 
ATOM   1443 C CD  . LYS   A 1 235 ? -20.204 44.657  74.422  1.00 144.90 ?  357 LYS   A CD  1 
ATOM   1444 C CE  . LYS   A 1 235 ? -21.416 45.615  74.530  1.00 135.94 ?  357 LYS   A CE  1 
ATOM   1445 N NZ  . LYS   A 1 235 ? -22.069 45.907  73.212  1.00 127.39 ?  357 LYS   A NZ  1 
ATOM   1446 N N   . GLN   A 1 236 ? -14.359 43.828  76.056  1.00 133.80 ?  358 GLN   A N   1 
ATOM   1447 C CA  . GLN   A 1 236 ? -12.906 43.863  75.908  1.00 136.46 ?  358 GLN   A CA  1 
ATOM   1448 C C   . GLN   A 1 236 ? -12.423 43.524  74.493  1.00 133.80 ?  358 GLN   A C   1 
ATOM   1449 O O   . GLN   A 1 236 ? -11.220 43.634  74.232  1.00 133.38 ?  358 GLN   A O   1 
ATOM   1450 C CB  . GLN   A 1 236 ? -12.253 42.898  76.926  1.00 138.28 ?  358 GLN   A CB  1 
ATOM   1451 C CG  . GLN   A 1 236 ? -12.420 43.229  78.454  1.00 146.65 ?  358 GLN   A CG  1 
ATOM   1452 C CD  . GLN   A 1 236 ? -11.703 44.514  78.958  1.00 149.67 ?  358 GLN   A CD  1 
ATOM   1453 O OE1 . GLN   A 1 236 ? -10.663 44.919  78.431  1.00 147.57 ?  358 GLN   A OE1 1 
ATOM   1454 N NE2 . GLN   A 1 236 ? -12.257 45.128  80.014  1.00 140.75 ?  358 GLN   A NE2 1 
ATOM   1455 N N   . LYS   A 1 237 ? -13.311 43.137  73.574  1.00 132.86 ?  359 LYS   A N   1 
ATOM   1456 C CA  . LYS   A 1 237 ? -12.871 42.590  72.293  1.00 132.74 ?  359 LYS   A CA  1 
ATOM   1457 C C   . LYS   A 1 237 ? -12.357 43.693  71.374  1.00 126.24 ?  359 LYS   A C   1 
ATOM   1458 O O   . LYS   A 1 237 ? -13.078 44.649  71.079  1.00 125.29 ?  359 LYS   A O   1 
ATOM   1459 C CB  . LYS   A 1 237 ? -14.011 41.838  71.600  1.00 133.87 ?  359 LYS   A CB  1 
ATOM   1460 C CG  . LYS   A 1 237 ? -13.503 40.768  70.626  1.00 140.45 ?  359 LYS   A CG  1 
ATOM   1461 C CD  . LYS   A 1 237 ? -14.596 40.203  69.730  1.00 143.51 ?  359 LYS   A CD  1 
ATOM   1462 C CE  . LYS   A 1 237 ? -14.586 40.937  68.382  1.00 144.75 ?  359 LYS   A CE  1 
ATOM   1463 N NZ  . LYS   A 1 237 ? -15.407 40.282  67.325  1.00 140.55 ?  359 LYS   A NZ  1 
ATOM   1464 N N   . CYS   A 1 238 ? -11.126 43.538  70.888  1.00 125.64 ?  360 CYS   A N   1 
ATOM   1465 C CA  . CYS   A 1 238 ? -10.468 44.568  70.082  1.00 123.55 ?  360 CYS   A CA  1 
ATOM   1466 C C   . CYS   A 1 238 ? -9.840  43.980  68.823  1.00 119.09 ?  360 CYS   A C   1 
ATOM   1467 O O   . CYS   A 1 238 ? -8.769  43.350  68.888  1.00 121.05 ?  360 CYS   A O   1 
ATOM   1468 C CB  . CYS   A 1 238 ? -9.419  45.310  70.903  1.00 122.05 ?  360 CYS   A CB  1 
ATOM   1469 S SG  . CYS   A 1 238 ? -9.005  46.941  70.222  1.00 119.80 ?  360 CYS   A SG  1 
ATOM   1470 N N   . PRO   A 1 239 ? -10.470 44.167  67.667  1.00 116.77 ?  361 PRO   A N   1 
ATOM   1471 C CA  . PRO   A 1 239 ? -9.864  43.745  66.395  1.00 120.61 ?  361 PRO   A CA  1 
ATOM   1472 C C   . PRO   A 1 239 ? -8.840  44.736  65.870  1.00 115.63 ?  361 PRO   A C   1 
ATOM   1473 O O   . PRO   A 1 239 ? -9.086  45.941  65.851  1.00 117.29 ?  361 PRO   A O   1 
ATOM   1474 C CB  . PRO   A 1 239 ? -11.064 43.686  65.444  1.00 124.04 ?  361 PRO   A CB  1 
ATOM   1475 C CG  . PRO   A 1 239 ? -12.085 44.590  66.054  1.00 118.10 ?  361 PRO   A CG  1 
ATOM   1476 C CD  . PRO   A 1 239 ? -11.897 44.496  67.532  1.00 117.24 ?  361 PRO   A CD  1 
ATOM   1477 N N   . LEU   A 1 240 ? -7.712  44.217  65.378  1.00 115.52 ?  362 LEU   A N   1 
ATOM   1478 C CA  . LEU   A 1 240 ? -6.629  45.055  64.866  1.00 117.39 ?  362 LEU   A CA  1 
ATOM   1479 C C   . LEU   A 1 240 ? -6.653  45.099  63.343  1.00 113.90 ?  362 LEU   A C   1 
ATOM   1480 O O   . LEU   A 1 240 ? -7.177  44.197  62.694  1.00 124.20 ?  362 LEU   A O   1 
ATOM   1481 C CB  . LEU   A 1 240 ? -5.265  44.552  65.333  1.00 116.70 ?  362 LEU   A CB  1 
ATOM   1482 C CG  . LEU   A 1 240 ? -5.195  44.103  66.785  1.00 109.87 ?  362 LEU   A CG  1 
ATOM   1483 C CD1 . LEU   A 1 240 ? -3.745  43.827  67.154  1.00 112.11 ?  362 LEU   A CD1 1 
ATOM   1484 C CD2 . LEU   A 1 240 ? -5.828  45.123  67.701  1.00 103.43 ?  362 LEU   A CD2 1 
ATOM   1485 N N   . TYR   A 1 241 ? -6.098  46.164  62.773  1.00 104.76 ?  363 TYR   A N   1 
ATOM   1486 C CA  . TYR   A 1 241 ? -6.288  46.449  61.354  1.00 110.90 ?  363 TYR   A CA  1 
ATOM   1487 C C   . TYR   A 1 241 ? -5.001  47.090  60.882  1.00 117.33 ?  363 TYR   A C   1 
ATOM   1488 O O   . TYR   A 1 241 ? -4.751  48.247  61.224  1.00 120.66 ?  363 TYR   A O   1 
ATOM   1489 C CB  . TYR   A 1 241 ? -7.455  47.408  61.138  1.00 113.59 ?  363 TYR   A CB  1 
ATOM   1490 C CG  . TYR   A 1 241 ? -8.830  46.831  61.364  1.00 118.98 ?  363 TYR   A CG  1 
ATOM   1491 C CD1 . TYR   A 1 241 ? -9.218  46.409  62.636  1.00 118.03 ?  363 TYR   A CD1 1 
ATOM   1492 C CD2 . TYR   A 1 241 ? -9.776  46.812  60.359  1.00 120.39 ?  363 TYR   A CD2 1 
ATOM   1493 C CE1 . TYR   A 1 241 ? -10.455 45.886  62.886  1.00 114.80 ?  363 TYR   A CE1 1 
ATOM   1494 C CE2 . TYR   A 1 241 ? -11.047 46.308  60.604  1.00 126.36 ?  363 TYR   A CE2 1 
ATOM   1495 C CZ  . TYR   A 1 241 ? -11.374 45.847  61.875  1.00 123.70 ?  363 TYR   A CZ  1 
ATOM   1496 O OH  . TYR   A 1 241 ? -12.617 45.336  62.155  1.00 126.19 ?  363 TYR   A OH  1 
ATOM   1497 N N   . GLU   A 1 242 ? -4.195  46.372  60.103  1.00 120.76 ?  364 GLU   A N   1 
ATOM   1498 C CA  . GLU   A 1 242 ? -2.936  46.944  59.624  1.00 120.74 ?  364 GLU   A CA  1 
ATOM   1499 C C   . GLU   A 1 242 ? -3.160  48.087  58.635  1.00 120.98 ?  364 GLU   A C   1 
ATOM   1500 O O   . GLU   A 1 242 ? -4.284  48.315  58.163  1.00 119.73 ?  364 GLU   A O   1 
ATOM   1501 C CB  . GLU   A 1 242 ? -2.124  45.887  58.874  1.00 125.84 ?  364 GLU   A CB  1 
ATOM   1502 C CG  . GLU   A 1 242 ? -1.759  44.670  59.724  1.00 131.21 ?  364 GLU   A CG  1 
ATOM   1503 C CD  . GLU   A 1 242 ? -1.674  43.399  58.894  1.00 140.32 ?  364 GLU   A CD  1 
ATOM   1504 O OE1 . GLU   A 1 242 ? -0.642  43.185  58.220  1.00 140.13 ?  364 GLU   A OE1 1 
ATOM   1505 O OE2 . GLU   A 1 242 ? -2.665  42.625  58.898  1.00 139.97 ?  364 GLU   A OE2 1 
ATOM   1506 N N   . ALA   A 1 243 ? -2.091  48.815  58.314  1.00 117.75 ?  365 ALA   A N   1 
ATOM   1507 C CA  . ALA   A 1 243 ? -2.228  49.980  57.448  1.00 121.31 ?  365 ALA   A CA  1 
ATOM   1508 C C   . ALA   A 1 243 ? -2.932  49.754  56.110  1.00 129.32 ?  365 ALA   A C   1 
ATOM   1509 O O   . ALA   A 1 243 ? -3.317  50.730  55.450  1.00 127.52 ?  365 ALA   A O   1 
ATOM   1510 C CB  . ALA   A 1 243 ? -0.843  50.600  57.238  1.00 122.98 ?  365 ALA   A CB  1 
ATOM   1511 N N   . ASN   A 1 244 ? -3.110  48.496  55.700  1.00 129.50 ?  366 ASN   A N   1 
ATOM   1512 C CA  . ASN   A 1 244 ? -3.887  48.185  54.505  1.00 124.86 ?  366 ASN   A CA  1 
ATOM   1513 C C   . ASN   A 1 244 ? -5.349  48.610  54.663  1.00 128.08 ?  366 ASN   A C   1 
ATOM   1514 O O   . ASN   A 1 244 ? -5.846  49.479  53.931  1.00 122.52 ?  366 ASN   A O   1 
ATOM   1515 C CB  . ASN   A 1 244 ? -3.752  46.682  54.196  1.00 124.90 ?  366 ASN   A CB  1 
ATOM   1516 C CG  . ASN   A 1 244 ? -4.410  45.768  55.260  1.00 130.55 ?  366 ASN   A CG  1 
ATOM   1517 O OD1 . ASN   A 1 244 ? -4.937  46.247  56.264  1.00 132.81 ?  366 ASN   A OD1 1 
ATOM   1518 N ND2 . ASN   A 1 244 ? -4.362  44.451  55.040  1.00 128.49 ?  366 ASN   A ND2 1 
ATOM   1519 N N   . GLY   A 1 245 ? -6.038  48.026  55.650  1.00 127.59 ?  367 GLY   A N   1 
ATOM   1520 C CA  . GLY   A 1 245 ? -7.459  48.190  55.866  1.00 127.79 ?  367 GLY   A CA  1 
ATOM   1521 C C   . GLY   A 1 245 ? -8.154  46.899  56.257  1.00 129.71 ?  367 GLY   A C   1 
ATOM   1522 O O   . GLY   A 1 245 ? -9.381  46.881  56.404  1.00 131.23 ?  367 GLY   A O   1 
ATOM   1523 N N   . GLN   A 1 246 ? -7.388  45.813  56.429  1.00 133.65 ?  368 GLN   A N   1 
ATOM   1524 C CA  . GLN   A 1 246 ? -7.934  44.484  56.693  1.00 129.54 ?  368 GLN   A CA  1 
ATOM   1525 C C   . GLN   A 1 246 ? -7.494  43.933  58.039  1.00 118.69 ?  368 GLN   A C   1 
ATOM   1526 O O   . GLN   A 1 246 ? -6.359  44.140  58.482  1.00 118.47 ?  368 GLN   A O   1 
ATOM   1527 C CB  . GLN   A 1 246 ? -7.531  43.447  55.637  1.00 139.56 ?  368 GLN   A CB  1 
ATOM   1528 C CG  . GLN   A 1 246 ? -8.123  43.616  54.237  1.00 149.16 ?  368 GLN   A CG  1 
ATOM   1529 C CD  . GLN   A 1 246 ? -7.724  42.459  53.317  1.00 158.87 ?  368 GLN   A CD  1 
ATOM   1530 O OE1 . GLN   A 1 246 ? -6.541  42.237  53.050  1.00 164.73 ?  368 GLN   A OE1 1 
ATOM   1531 N NE2 . GLN   A 1 246 ? -8.716  41.687  52.872  1.00 155.03 ?  368 GLN   A NE2 1 
ATOM   1532 N N   . ALA   A 1 247 ? -8.390  43.157  58.638  1.00 116.12 ?  369 ALA   A N   1 
ATOM   1533 C CA  . ALA   A 1 247 ? -8.180  42.639  59.982  1.00 122.01 ?  369 ALA   A CA  1 
ATOM   1534 C C   . ALA   A 1 247 ? -6.981  41.694  60.062  1.00 120.66 ?  369 ALA   A C   1 
ATOM   1535 O O   . ALA   A 1 247 ? -6.649  40.966  59.125  1.00 125.61 ?  369 ALA   A O   1 
ATOM   1536 C CB  . ALA   A 1 247 ? -9.436  41.920  60.479  1.00 119.25 ?  369 ALA   A CB  1 
ATOM   1537 N N   . VAL   A 1 248 ? -6.325  41.719  61.207  1.00 118.43 ?  370 VAL   A N   1 
ATOM   1538 C CA  . VAL   A 1 248 ? -5.294  40.741  61.502  1.00 128.00 ?  370 VAL   A CA  1 
ATOM   1539 C C   . VAL   A 1 248 ? -6.021  39.468  61.913  1.00 134.62 ?  370 VAL   A C   1 
ATOM   1540 O O   . VAL   A 1 248 ? -6.850  39.503  62.837  1.00 132.92 ?  370 VAL   A O   1 
ATOM   1541 C CB  . VAL   A 1 248 ? -4.338  41.265  62.582  1.00 129.54 ?  370 VAL   A CB  1 
ATOM   1542 C CG1 . VAL   A 1 248 ? -3.452  40.147  63.126  1.00 126.57 ?  370 VAL   A CG1 1 
ATOM   1543 C CG2 . VAL   A 1 248 ? -3.509  42.432  62.015  1.00 122.27 ?  370 VAL   A CG2 1 
ATOM   1544 N N   . PRO   A 1 249 ? -5.752  38.335  61.256  1.00 135.96 ?  371 PRO   A N   1 
ATOM   1545 C CA  . PRO   A 1 249 ? -6.552  37.124  61.500  1.00 130.61 ?  371 PRO   A CA  1 
ATOM   1546 C C   . PRO   A 1 249 ? -6.279  36.525  62.870  1.00 128.04 ?  371 PRO   A C   1 
ATOM   1547 O O   . PRO   A 1 249 ? -5.147  36.553  63.355  1.00 127.00 ?  371 PRO   A O   1 
ATOM   1548 C CB  . PRO   A 1 249 ? -6.109  36.173  60.381  1.00 140.15 ?  371 PRO   A CB  1 
ATOM   1549 C CG  . PRO   A 1 249 ? -4.928  36.856  59.668  1.00 136.47 ?  371 PRO   A CG  1 
ATOM   1550 C CD  . PRO   A 1 249 ? -4.575  38.090  60.401  1.00 130.04 ?  371 PRO   A CD  1 
ATOM   1551 N N   . LYS   A 1 250 ? -7.322  35.997  63.487  1.00 129.75 ?  372 LYS   A N   1 
ATOM   1552 C CA  . LYS   A 1 250 ? -7.129  35.450  64.844  1.00 139.15 ?  372 LYS   A CA  1 
ATOM   1553 C C   . LYS   A 1 250 ? -5.713  34.905  64.874  1.00 139.02 ?  372 LYS   A C   1 
ATOM   1554 O O   . LYS   A 1 250 ? -4.903  35.336  65.698  1.00 137.85 ?  372 LYS   A O   1 
ATOM   1555 C CB  . LYS   A 1 250 ? -8.133  34.334  65.114  1.00 135.90 ?  372 LYS   A CB  1 
ATOM   1556 C CG  . LYS   A 1 250 ? -9.521  34.566  64.536  1.00 140.82 ?  372 LYS   A CG  1 
ATOM   1557 C CD  . LYS   A 1 250 ? -10.566 34.882  65.584  1.00 142.24 ?  372 LYS   A CD  1 
ATOM   1558 C CE  . LYS   A 1 250 ? -11.888 35.314  64.986  1.00 138.88 ?  372 LYS   A CE  1 
ATOM   1559 N NZ  . LYS   A 1 250 ? -12.873 35.686  66.029  1.00 133.74 ?  372 LYS   A NZ  1 
ATOM   1560 N N   . GLU   A 1 251 ? -5.440  34.004  63.952  1.00 144.40 ?  373 GLU   A N   1 
ATOM   1561 C CA  . GLU   A 1 251 ? -4.109  33.410  63.961  1.00 147.47 ?  373 GLU   A CA  1 
ATOM   1562 C C   . GLU   A 1 251 ? -2.910  34.170  64.493  1.00 140.52 ?  373 GLU   A C   1 
ATOM   1563 O O   . GLU   A 1 251 ? -2.175  33.693  65.369  1.00 136.12 ?  373 GLU   A O   1 
ATOM   1564 C CB  . GLU   A 1 251 ? -3.634  33.150  62.524  1.00 152.15 ?  373 GLU   A CB  1 
ATOM   1565 C CG  . GLU   A 1 251 ? -3.831  31.751  62.007  1.00 152.20 ?  373 GLU   A CG  1 
ATOM   1566 C CD  . GLU   A 1 251 ? -2.739  30.822  62.508  1.00 154.05 ?  373 GLU   A CD  1 
ATOM   1567 O OE1 . GLU   A 1 251 ? -1.631  31.315  62.833  1.00 153.86 ?  373 GLU   A OE1 1 
ATOM   1568 O OE2 . GLU   A 1 251 ? -2.982  29.602  62.560  1.00 154.88 ?  373 GLU   A OE2 1 
ATOM   1569 N N   . LYS   A 1 252 ? -2.725  35.362  63.919  1.00 136.06 ?  374 LYS   A N   1 
ATOM   1570 C CA  . LYS   A 1 252 ? -1.688  36.286  64.346  1.00 132.14 ?  374 LYS   A CA  1 
ATOM   1571 C C   . LYS   A 1 252 ? -2.088  36.998  65.634  1.00 134.28 ?  374 LYS   A C   1 
ATOM   1572 O O   . LYS   A 1 252 ? -1.387  36.914  66.654  1.00 126.20 ?  374 LYS   A O   1 
ATOM   1573 C CB  . LYS   A 1 252 ? -1.458  37.288  63.222  1.00 127.06 ?  374 LYS   A CB  1 
ATOM   1574 C CG  . LYS   A 1 252 ? -1.043  36.672  61.939  1.00 125.87 ?  374 LYS   A CG  1 
ATOM   1575 C CD  . LYS   A 1 252 ? 0.221   35.896  62.083  1.00 125.21 ?  374 LYS   A CD  1 
ATOM   1576 C CE  . LYS   A 1 252 ? 1.345   36.859  62.303  1.00 129.81 ?  374 LYS   A CE  1 
ATOM   1577 N NZ  . LYS   A 1 252 ? 2.646   36.119  62.279  1.00 130.49 ?  374 LYS   A NZ  1 
ATOM   1578 N N   . ASP   A 1 253 ? -3.245  37.681  65.599  1.00 136.75 ?  375 ASP   A N   1 
ATOM   1579 C CA  . ASP   A 1 253 ? -3.801  38.481  66.689  1.00 132.98 ?  375 ASP   A CA  1 
ATOM   1580 C C   . ASP   A 1 253 ? -3.448  37.881  68.032  1.00 128.31 ?  375 ASP   A C   1 
ATOM   1581 O O   . ASP   A 1 253 ? -3.066  38.600  68.958  1.00 133.91 ?  375 ASP   A O   1 
ATOM   1582 C CB  . ASP   A 1 253 ? -5.324  38.598  66.572  1.00 131.14 ?  375 ASP   A CB  1 
ATOM   1583 C CG  . ASP   A 1 253 ? -5.861  39.886  67.184  1.00 132.19 ?  375 ASP   A CG  1 
ATOM   1584 O OD1 . ASP   A 1 253 ? -5.189  40.455  68.081  1.00 128.03 ?  375 ASP   A OD1 1 
ATOM   1585 O OD2 . ASP   A 1 253 ? -6.950  40.335  66.759  1.00 131.69 ?  375 ASP   A OD2 1 
ATOM   1586 N N   . GLU   A 1 254 ? -3.535  36.561  68.115  1.00 124.19 ?  376 GLU   A N   1 
ATOM   1587 C CA  . GLU   A 1 254 ? -3.341  35.851  69.363  1.00 125.59 ?  376 GLU   A CA  1 
ATOM   1588 C C   . GLU   A 1 254 ? -1.897  35.425  69.559  1.00 123.84 ?  376 GLU   A C   1 
ATOM   1589 O O   . GLU   A 1 254 ? -1.416  35.416  70.695  1.00 122.18 ?  376 GLU   A O   1 
ATOM   1590 C CB  . GLU   A 1 254 ? -4.272  34.637  69.398  1.00 135.24 ?  376 GLU   A CB  1 
ATOM   1591 C CG  . GLU   A 1 254 ? -5.761  35.040  69.387  1.00 145.55 ?  376 GLU   A CG  1 
ATOM   1592 C CD  . GLU   A 1 254 ? -6.732  33.854  69.335  1.00 146.35 ?  376 GLU   A CD  1 
ATOM   1593 O OE1 . GLU   A 1 254 ? -6.408  32.792  69.914  1.00 147.48 ?  376 GLU   A OE1 1 
ATOM   1594 O OE2 . GLU   A 1 254 ? -7.807  33.982  68.685  1.00 142.73 ?  376 GLU   A OE2 1 
ATOM   1595 N N   . MET   A 1 255 ? -1.178  35.087  68.487  1.00 130.06 ?  377 MET   A N   1 
ATOM   1596 C CA  . MET   A 1 255 ? 0.217   34.704  68.680  1.00 134.34 ?  377 MET   A CA  1 
ATOM   1597 C C   . MET   A 1 255 ? 1.141   35.897  68.820  1.00 129.08 ?  377 MET   A C   1 
ATOM   1598 O O   . MET   A 1 255 ? 2.207   35.757  69.430  1.00 127.86 ?  377 MET   A O   1 
ATOM   1599 C CB  . MET   A 1 255 ? 0.713   33.781  67.562  1.00 140.41 ?  377 MET   A CB  1 
ATOM   1600 C CG  . MET   A 1 255 ? 0.452   32.305  67.915  1.00 159.28 ?  377 MET   A CG  1 
ATOM   1601 S SD  . MET   A 1 255 ? 0.831   31.002  66.710  1.00 194.56 ?  377 MET   A SD  1 
ATOM   1602 C CE  . MET   A 1 255 ? 0.851   29.559  67.801  1.00 162.49 ?  377 MET   A CE  1 
ATOM   1603 N N   . VAL   A 1 256 ? 0.755   37.061  68.296  1.00 127.44 ?  378 VAL   A N   1 
ATOM   1604 C CA  . VAL   A 1 256 ? 1.470   38.295  68.603  1.00 120.12 ?  378 VAL   A CA  1 
ATOM   1605 C C   . VAL   A 1 256 ? 1.229   38.642  70.058  1.00 117.80 ?  378 VAL   A C   1 
ATOM   1606 O O   . VAL   A 1 256 ? 2.165   38.665  70.869  1.00 111.89 ?  378 VAL   A O   1 
ATOM   1607 C CB  . VAL   A 1 256 ? 1.029   39.464  67.714  1.00 117.38 ?  378 VAL   A CB  1 
ATOM   1608 C CG1 . VAL   A 1 256 ? 1.853   40.668  68.056  1.00 114.51 ?  378 VAL   A CG1 1 
ATOM   1609 C CG2 . VAL   A 1 256 ? 1.203   39.118  66.258  1.00 126.89 ?  378 VAL   A CG2 1 
ATOM   1610 N N   . GLU   A 1 257 ? -0.040  38.938  70.370  1.00 121.29 ?  379 GLU   A N   1 
ATOM   1611 C CA  . GLU   A 1 257 ? -0.477  39.237  71.730  1.00 116.94 ?  379 GLU   A CA  1 
ATOM   1612 C C   . GLU   A 1 257 ? 0.179   38.360  72.783  1.00 116.45 ?  379 GLU   A C   1 
ATOM   1613 O O   . GLU   A 1 257 ? 0.717   38.868  73.771  1.00 115.53 ?  379 GLU   A O   1 
ATOM   1614 C CB  . GLU   A 1 257 ? -1.992  39.097  71.834  1.00 114.42 ?  379 GLU   A CB  1 
ATOM   1615 C CG  . GLU   A 1 257 ? -2.480  39.106  73.268  1.00 114.89 ?  379 GLU   A CG  1 
ATOM   1616 C CD  . GLU   A 1 257 ? -3.809  39.794  73.430  1.00 123.05 ?  379 GLU   A CD  1 
ATOM   1617 O OE1 . GLU   A 1 257 ? -4.343  40.278  72.395  1.00 125.41 ?  379 GLU   A OE1 1 
ATOM   1618 O OE2 . GLU   A 1 257 ? -4.324  39.823  74.579  1.00 119.48 ?  379 GLU   A OE2 1 
ATOM   1619 N N   . GLN   A 1 258 ? 0.124   37.036  72.621  1.00 117.52 ?  380 GLN   A N   1 
ATOM   1620 C CA  . GLN   A 1 258 ? 0.708   36.212  73.668  1.00 119.42 ?  380 GLN   A CA  1 
ATOM   1621 C C   . GLN   A 1 258 ? 2.208   36.415  73.733  1.00 118.15 ?  380 GLN   A C   1 
ATOM   1622 O O   . GLN   A 1 258 ? 2.792   36.375  74.821  1.00 113.78 ?  380 GLN   A O   1 
ATOM   1623 C CB  . GLN   A 1 258 ? 0.424   34.733  73.475  1.00 129.27 ?  380 GLN   A CB  1 
ATOM   1624 C CG  . GLN   A 1 258 ? 0.610   33.990  74.806  1.00 137.26 ?  380 GLN   A CG  1 
ATOM   1625 C CD  . GLN   A 1 258 ? 1.075   32.545  74.643  1.00 148.25 ?  380 GLN   A CD  1 
ATOM   1626 O OE1 . GLN   A 1 258 ? 1.979   32.075  75.356  1.00 145.31 ?  380 GLN   A OE1 1 
ATOM   1627 N NE2 . GLN   A 1 258 ? 0.506   31.853  73.661  1.00 150.51 ?  380 GLN   A NE2 1 
ATOM   1628 N N   . GLU   A 1 259 ? 2.856   36.613  72.581  1.00 117.54 ?  381 GLU   A N   1 
ATOM   1629 C CA  . GLU   A 1 259 ? 4.286   36.888  72.622  1.00 116.21 ?  381 GLU   A CA  1 
ATOM   1630 C C   . GLU   A 1 259 ? 4.554   38.184  73.379  1.00 111.93 ?  381 GLU   A C   1 
ATOM   1631 O O   . GLU   A 1 259 ? 5.489   38.252  74.192  1.00 107.05 ?  381 GLU   A O   1 
ATOM   1632 C CB  . GLU   A 1 259 ? 4.878   36.908  71.205  1.00 109.35 ?  381 GLU   A CB  1 
ATOM   1633 C CG  . GLU   A 1 259 ? 6.426   36.794  71.151  1.00 104.74 ?  381 GLU   A CG  1 
ATOM   1634 C CD  . GLU   A 1 259 ? 7.006   35.554  71.891  1.00 117.47 ?  381 GLU   A CD  1 
ATOM   1635 O OE1 . GLU   A 1 259 ? 6.281   34.545  72.098  1.00 115.88 ?  381 GLU   A OE1 1 
ATOM   1636 O OE2 . GLU   A 1 259 ? 8.203   35.594  72.281  1.00 114.43 ?  381 GLU   A OE2 1 
ATOM   1637 N N   . PHE   A 1 260 ? 3.700   39.199  73.174  1.00 113.07 ?  382 PHE   A N   1 
ATOM   1638 C CA  . PHE   A 1 260 ? 3.746   40.446  73.941  1.00 112.28 ?  382 PHE   A CA  1 
ATOM   1639 C C   . PHE   A 1 260 ? 3.587   40.352  75.454  1.00 105.90 ?  382 PHE   A C   1 
ATOM   1640 O O   . PHE   A 1 260 ? 4.316   41.020  76.194  1.00 104.27 ?  382 PHE   A O   1 
ATOM   1641 C CB  . PHE   A 1 260 ? 2.589   41.383  73.540  1.00 113.17 ?  382 PHE   A CB  1 
ATOM   1642 C CG  . PHE   A 1 260 ? 2.272   42.461  74.564  1.00 110.54 ?  382 PHE   A CG  1 
ATOM   1643 C CD1 . PHE   A 1 260 ? 3.260   43.326  75.022  1.00 105.45 ?  382 PHE   A CD1 1 
ATOM   1644 C CD2 . PHE   A 1 260 ? 0.975   42.621  75.040  1.00 109.83 ?  382 PHE   A CD2 1 
ATOM   1645 C CE1 . PHE   A 1 260 ? 2.977   44.291  75.950  1.00 100.73 ?  382 PHE   A CE1 1 
ATOM   1646 C CE2 . PHE   A 1 260 ? 0.681   43.594  75.966  1.00 106.94 ?  382 PHE   A CE2 1 
ATOM   1647 C CZ  . PHE   A 1 260 ? 1.685   44.427  76.423  1.00 105.91 ?  382 PHE   A CZ  1 
ATOM   1648 N N   . ASN   A 1 261 ? 2.656   39.513  75.914  1.00 103.88 ?  383 ASN   A N   1 
ATOM   1649 C CA  . ASN   A 1 261 ? 2.473   39.286  77.344  1.00 103.53 ?  383 ASN   A CA  1 
ATOM   1650 C C   . ASN   A 1 261 ? 3.681   38.486  77.802  1.00 103.38 ?  383 ASN   A C   1 
ATOM   1651 O O   . ASN   A 1 261 ? 4.141   38.621  78.940  1.00 101.38 ?  383 ASN   A O   1 
ATOM   1652 C CB  . ASN   A 1 261 ? 1.205   38.469  77.545  1.00 104.17 ?  383 ASN   A CB  1 
ATOM   1653 C CG  . ASN   A 1 261 ? -0.032  39.311  77.470  1.00 109.95 ?  383 ASN   A CG  1 
ATOM   1654 O OD1 . ASN   A 1 261 ? -0.221  40.220  78.281  1.00 121.11 ?  383 ASN   A OD1 1 
ATOM   1655 N ND2 . ASN   A 1 261 ? -0.889  39.026  76.494  1.00 109.29 ?  383 ASN   A ND2 1 
ATOM   1656 N N   . ARG   A 1 262 ? 4.215   37.656  76.916  1.00 109.40 ?  384 ARG   A N   1 
ATOM   1657 C CA  . ARG   A 1 262 ? 5.355   36.822  77.261  1.00 113.71 ?  384 ARG   A CA  1 
ATOM   1658 C C   . ARG   A 1 262 ? 6.611   37.671  77.416  1.00 108.70 ?  384 ARG   A C   1 
ATOM   1659 O O   . ARG   A 1 262 ? 7.358   37.519  78.391  1.00 105.75 ?  384 ARG   A O   1 
ATOM   1660 C CB  . ARG   A 1 262 ? 5.503   35.745  76.181  1.00 118.66 ?  384 ARG   A CB  1 
ATOM   1661 C CG  . ARG   A 1 262 ? 4.650   34.478  76.447  1.00 125.55 ?  384 ARG   A CG  1 
ATOM   1662 C CD  . ARG   A 1 262 ? 4.586   33.491  75.253  1.00 128.81 ?  384 ARG   A CD  1 
ATOM   1663 N NE  . ARG   A 1 262 ? 5.886   33.124  74.711  1.00 129.67 ?  384 ARG   A NE  1 
ATOM   1664 C CZ  . ARG   A 1 262 ? 6.679   32.203  75.241  1.00 137.43 ?  384 ARG   A CZ  1 
ATOM   1665 N NH1 . ARG   A 1 262 ? 6.317   31.510  76.317  1.00 131.05 ?  384 ARG   A NH1 1 
ATOM   1666 N NH2 . ARG   A 1 262 ? 7.873   31.986  74.692  1.00 138.52 ?  384 ARG   A NH2 1 
ATOM   1667 N N   . LEU   A 1 263 ? 6.830   38.599  76.481  1.00 104.86 ?  385 LEU   A N   1 
ATOM   1668 C CA  . LEU   A 1 263 ? 7.940   39.533  76.604  1.00 102.74 ?  385 LEU   A CA  1 
ATOM   1669 C C   . LEU   A 1 263 ? 7.886   40.304  77.916  1.00 106.28 ?  385 LEU   A C   1 
ATOM   1670 O O   . LEU   A 1 263 ? 8.924   40.533  78.548  1.00 106.66 ?  385 LEU   A O   1 
ATOM   1671 C CB  . LEU   A 1 263 ? 7.926   40.510  75.441  1.00 97.66  ?  385 LEU   A CB  1 
ATOM   1672 C CG  . LEU   A 1 263 ? 8.249   39.891  74.104  1.00 98.22  ?  385 LEU   A CG  1 
ATOM   1673 C CD1 . LEU   A 1 263 ? 7.763   40.761  72.921  1.00 86.58  ?  385 LEU   A CD1 1 
ATOM   1674 C CD2 . LEU   A 1 263 ? 9.728   39.665  74.113  1.00 99.80  ?  385 LEU   A CD2 1 
ATOM   1675 N N   . LEU   A 1 264 ? 6.687   40.747  78.320  1.00 107.23 ?  386 LEU   A N   1 
ATOM   1676 C CA  . LEU   A 1 264 ? 6.544   41.532  79.543  1.00 98.08  ?  386 LEU   A CA  1 
ATOM   1677 C C   . LEU   A 1 264 ? 7.103   40.769  80.728  1.00 103.18 ?  386 LEU   A C   1 
ATOM   1678 O O   . LEU   A 1 264 ? 8.078   41.205  81.348  1.00 105.18 ?  386 LEU   A O   1 
ATOM   1679 C CB  . LEU   A 1 264 ? 5.079   41.897  79.783  1.00 95.41  ?  386 LEU   A CB  1 
ATOM   1680 C CG  . LEU   A 1 264 ? 4.666   43.225  79.151  1.00 98.15  ?  386 LEU   A CG  1 
ATOM   1681 C CD1 . LEU   A 1 264 ? 3.209   43.584  79.452  1.00 99.63  ?  386 LEU   A CD1 1 
ATOM   1682 C CD2 . LEU   A 1 264 ? 5.620   44.306  79.596  1.00 93.97  ?  386 LEU   A CD2 1 
ATOM   1683 N N   . GLU   A 1 265 ? 6.513   39.602  81.034  1.00 103.92 ?  387 GLU   A N   1 
ATOM   1684 C CA  . GLU   A 1 265 ? 7.007   38.767  82.128  1.00 105.43 ?  387 GLU   A CA  1 
ATOM   1685 C C   . GLU   A 1 265 ? 8.515   38.613  82.058  1.00 106.27 ?  387 GLU   A C   1 
ATOM   1686 O O   . GLU   A 1 265 ? 9.200   38.629  83.089  1.00 105.16 ?  387 GLU   A O   1 
ATOM   1687 C CB  . GLU   A 1 265 ? 6.400   37.366  82.076  1.00 114.21 ?  387 GLU   A CB  1 
ATOM   1688 C CG  . GLU   A 1 265 ? 4.988   37.229  81.565  1.00 121.09 ?  387 GLU   A CG  1 
ATOM   1689 C CD  . GLU   A 1 265 ? 4.356   35.893  81.966  1.00 128.43 ?  387 GLU   A CD  1 
ATOM   1690 O OE1 . GLU   A 1 265 ? 5.065   35.040  82.571  1.00 129.69 ?  387 GLU   A OE1 1 
ATOM   1691 O OE2 . GLU   A 1 265 ? 3.167   35.683  81.615  1.00 125.07 ?  387 GLU   A OE2 1 
ATOM   1692 N N   . ALA   A 1 266 ? 9.042   38.424  80.842  1.00 103.70 ?  388 ALA   A N   1 
ATOM   1693 C CA  . ALA   A 1 266 ? 10.477  38.251  80.665  1.00 103.23 ?  388 ALA   A CA  1 
ATOM   1694 C C   . ALA   A 1 266 ? 11.249  39.428  81.255  1.00 109.37 ?  388 ALA   A C   1 
ATOM   1695 O O   . ALA   A 1 266 ? 12.299  39.238  81.889  1.00 107.16 ?  388 ALA   A O   1 
ATOM   1696 C CB  . ALA   A 1 266 ? 10.793  38.069  79.182  1.00 104.24 ?  388 ALA   A CB  1 
ATOM   1697 N N   . THR   A 1 267 ? 10.732  40.652  81.066  1.00 109.60 ?  389 THR   A N   1 
ATOM   1698 C CA  . THR   A 1 267 ? 11.350  41.834  81.660  1.00 100.92 ?  389 THR   A CA  1 
ATOM   1699 C C   . THR   A 1 267 ? 11.266  41.766  83.172  1.00 102.38 ?  389 THR   A C   1 
ATOM   1700 O O   . THR   A 1 267 ? 12.259  41.990  83.871  1.00 102.76 ?  389 THR   A O   1 
ATOM   1701 C CB  . THR   A 1 267 ? 10.664  43.090  81.146  1.00 98.69  ?  389 THR   A CB  1 
ATOM   1702 O OG1 . THR   A 1 267 ? 9.247   42.904  81.191  1.00 99.11  ?  389 THR   A OG1 1 
ATOM   1703 C CG2 . THR   A 1 267 ? 11.049  43.320  79.703  1.00 99.44  ?  389 THR   A CG2 1 
ATOM   1704 N N   . SER   A 1 268 ? 10.087  41.413  83.689  1.00 104.00 ?  390 SER   A N   1 
ATOM   1705 C CA  . SER   A 1 268 ? 9.901   41.258  85.126  1.00 105.58 ?  390 SER   A CA  1 
ATOM   1706 C C   . SER   A 1 268 ? 10.872  40.237  85.700  1.00 102.49 ?  390 SER   A C   1 
ATOM   1707 O O   . SER   A 1 268 ? 11.364  40.397  86.825  1.00 97.00  ?  390 SER   A O   1 
ATOM   1708 C CB  . SER   A 1 268 ? 8.452   40.860  85.406  1.00 97.22  ?  390 SER   A CB  1 
ATOM   1709 O OG  . SER   A 1 268 ? 8.297   40.417  86.732  1.00 97.94  ?  390 SER   A OG  1 
ATOM   1710 N N   . TYR   A 1 269 ? 11.175  39.198  84.926  1.00 106.74 ?  391 TYR   A N   1 
ATOM   1711 C CA  . TYR   A 1 269 ? 12.203  38.250  85.323  1.00 110.26 ?  391 TYR   A CA  1 
ATOM   1712 C C   . TYR   A 1 269 ? 13.588  38.900  85.264  1.00 114.02 ?  391 TYR   A C   1 
ATOM   1713 O O   . TYR   A 1 269 ? 14.397  38.730  86.186  1.00 114.79 ?  391 TYR   A O   1 
ATOM   1714 C CB  . TYR   A 1 269 ? 12.112  37.004  84.433  1.00 111.86 ?  391 TYR   A CB  1 
ATOM   1715 C CG  . TYR   A 1 269 ? 13.207  35.976  84.659  1.00 121.47 ?  391 TYR   A CG  1 
ATOM   1716 C CD1 . TYR   A 1 269 ? 14.440  36.074  84.022  1.00 123.36 ?  391 TYR   A CD1 1 
ATOM   1717 C CD2 . TYR   A 1 269 ? 12.996  34.897  85.500  1.00 128.06 ?  391 TYR   A CD2 1 
ATOM   1718 C CE1 . TYR   A 1 269 ? 15.437  35.141  84.239  1.00 120.60 ?  391 TYR   A CE1 1 
ATOM   1719 C CE2 . TYR   A 1 269 ? 13.983  33.968  85.728  1.00 129.15 ?  391 TYR   A CE2 1 
ATOM   1720 C CZ  . TYR   A 1 269 ? 15.198  34.095  85.094  1.00 126.29 ?  391 TYR   A CZ  1 
ATOM   1721 O OH  . TYR   A 1 269 ? 16.177  33.164  85.316  1.00 130.53 ?  391 TYR   A OH  1 
ATOM   1722 N N   . LEU   A 1 270 ? 13.880  39.654  84.192  1.00 109.25 ?  392 LEU   A N   1 
ATOM   1723 C CA  . LEU   A 1 270 ? 15.103  40.456  84.165  1.00 107.05 ?  392 LEU   A CA  1 
ATOM   1724 C C   . LEU   A 1 270 ? 15.217  41.334  85.391  1.00 111.08 ?  392 LEU   A C   1 
ATOM   1725 O O   . LEU   A 1 270 ? 16.297  41.473  85.976  1.00 112.66 ?  392 LEU   A O   1 
ATOM   1726 C CB  . LEU   A 1 270 ? 15.142  41.346  82.936  1.00 101.00 ?  392 LEU   A CB  1 
ATOM   1727 C CG  . LEU   A 1 270 ? 16.138  40.944  81.885  1.00 103.91 ?  392 LEU   A CG  1 
ATOM   1728 C CD1 . LEU   A 1 270 ? 15.757  39.572  81.423  1.00 115.60 ?  392 LEU   A CD1 1 
ATOM   1729 C CD2 . LEU   A 1 270 ? 16.042  41.941  80.764  1.00 101.11 ?  392 LEU   A CD2 1 
ATOM   1730 N N   . SER   A 1 271 ? 14.111  41.960  85.776  1.00 109.05 ?  393 SER   A N   1 
ATOM   1731 C CA  . SER   A 1 271 ? 14.156  42.908  86.874  1.00 111.18 ?  393 SER   A CA  1 
ATOM   1732 C C   . SER   A 1 271 ? 14.366  42.184  88.192  1.00 116.42 ?  393 SER   A C   1 
ATOM   1733 O O   . SER   A 1 271 ? 15.366  42.414  88.882  1.00 119.09 ?  393 SER   A O   1 
ATOM   1734 C CB  . SER   A 1 271 ? 12.875  43.749  86.891  1.00 110.43 ?  393 SER   A CB  1 
ATOM   1735 O OG  . SER   A 1 271 ? 12.909  44.713  87.923  1.00 110.08 ?  393 SER   A OG  1 
ATOM   1736 N N   . HIS   A 1 272 ? 13.454  41.264  88.541  1.00 116.56 ?  394 HIS   A N   1 
ATOM   1737 C CA  . HIS   A 1 272 ? 13.429  40.762  89.911  1.00 119.89 ?  394 HIS   A CA  1 
ATOM   1738 C C   . HIS   A 1 272 ? 14.296  39.530  90.118  1.00 124.05 ?  394 HIS   A C   1 
ATOM   1739 O O   . HIS   A 1 272 ? 14.854  39.365  91.209  1.00 126.00 ?  394 HIS   A O   1 
ATOM   1740 C CB  . HIS   A 1 272 ? 11.984  40.493  90.361  1.00 113.00 ?  394 HIS   A CB  1 
ATOM   1741 C CG  . HIS   A 1 272 ? 11.112  41.716  90.322  1.00 126.69 ?  394 HIS   A CG  1 
ATOM   1742 N ND1 . HIS   A 1 272 ? 10.189  41.947  89.321  1.00 128.75 ?  394 HIS   A ND1 1 
ATOM   1743 C CD2 . HIS   A 1 272 ? 11.091  42.823  91.109  1.00 131.16 ?  394 HIS   A CD2 1 
ATOM   1744 C CE1 . HIS   A 1 272 ? 9.603   43.118  89.520  1.00 127.25 ?  394 HIS   A CE1 1 
ATOM   1745 N NE2 . HIS   A 1 272 ? 10.136  43.673  90.596  1.00 128.31 ?  394 HIS   A NE2 1 
ATOM   1746 N N   . GLN   A 1 273 ? 14.476  38.697  89.088  1.00 128.62 ?  395 GLN   A N   1 
ATOM   1747 C CA  . GLN   A 1 273 ? 15.149  37.407  89.246  1.00 128.48 ?  395 GLN   A CA  1 
ATOM   1748 C C   . GLN   A 1 273 ? 16.646  37.482  88.961  1.00 124.24 ?  395 GLN   A C   1 
ATOM   1749 O O   . GLN   A 1 273 ? 17.416  36.717  89.555  1.00 119.21 ?  395 GLN   A O   1 
ATOM   1750 C CB  . GLN   A 1 273 ? 14.517  36.375  88.309  1.00 129.02 ?  395 GLN   A CB  1 
ATOM   1751 C CG  . GLN   A 1 273 ? 13.047  36.007  88.597  1.00 131.86 ?  395 GLN   A CG  1 
ATOM   1752 C CD  . GLN   A 1 273 ? 12.789  35.572  90.011  1.00 143.06 ?  395 GLN   A CD  1 
ATOM   1753 O OE1 . GLN   A 1 273 ? 12.745  34.378  90.301  1.00 153.99 ?  395 GLN   A OE1 1 
ATOM   1754 N NE2 . GLN   A 1 273 ? 12.567  36.537  90.898  1.00 139.91 ?  395 GLN   A NE2 1 
ATOM   1755 N N   . LEU   A 1 274 ? 17.061  38.395  88.065  1.00 123.84 ?  396 LEU   A N   1 
ATOM   1756 C CA  . LEU   A 1 274 ? 18.446  38.590  87.640  1.00 124.63 ?  396 LEU   A CA  1 
ATOM   1757 C C   . LEU   A 1 274 ? 19.076  39.908  88.092  1.00 132.45 ?  396 LEU   A C   1 
ATOM   1758 O O   . LEU   A 1 274 ? 20.300  40.061  87.957  1.00 130.97 ?  396 LEU   A O   1 
ATOM   1759 C CB  . LEU   A 1 274 ? 18.529  38.537  86.112  1.00 119.94 ?  396 LEU   A CB  1 
ATOM   1760 C CG  . LEU   A 1 274 ? 18.095  37.264  85.414  1.00 122.81 ?  396 LEU   A CG  1 
ATOM   1761 C CD1 . LEU   A 1 274 ? 18.299  37.392  83.914  1.00 125.99 ?  396 LEU   A CD1 1 
ATOM   1762 C CD2 . LEU   A 1 274 ? 18.925  36.139  85.949  1.00 131.13 ?  396 LEU   A CD2 1 
ATOM   1763 N N   . ASP   A 1 275 ? 18.275  40.867  88.587  1.00 132.67 ?  397 ASP   A N   1 
ATOM   1764 C CA  . ASP   A 1 275 ? 18.715  42.225  88.967  1.00 133.00 ?  397 ASP   A CA  1 
ATOM   1765 C C   . ASP   A 1 275 ? 19.424  42.960  87.822  1.00 130.74 ?  397 ASP   A C   1 
ATOM   1766 O O   . ASP   A 1 275 ? 20.469  43.595  88.007  1.00 132.87 ?  397 ASP   A O   1 
ATOM   1767 C CB  . ASP   A 1 275 ? 19.577  42.215  90.240  1.00 133.77 ?  397 ASP   A CB  1 
ATOM   1768 C CG  . ASP   A 1 275 ? 19.401  43.494  91.082  1.00 139.87 ?  397 ASP   A CG  1 
ATOM   1769 O OD1 . ASP   A 1 275 ? 19.222  44.596  90.500  1.00 134.94 ?  397 ASP   A OD1 1 
ATOM   1770 O OD2 . ASP   A 1 275 ? 19.386  43.394  92.331  1.00 148.62 ?  397 ASP   A OD2 1 
ATOM   1771 N N   . PHE   A 1 276 ? 18.816  42.900  86.634  1.00 123.78 ?  398 PHE   A N   1 
ATOM   1772 C CA  . PHE   A 1 276 ? 19.145  43.795  85.519  1.00 120.26 ?  398 PHE   A CA  1 
ATOM   1773 C C   . PHE   A 1 276 ? 18.483  45.137  85.820  1.00 120.02 ?  398 PHE   A C   1 
ATOM   1774 O O   . PHE   A 1 276 ? 17.362  45.415  85.391  1.00 121.97 ?  398 PHE   A O   1 
ATOM   1775 C CB  . PHE   A 1 276 ? 18.663  43.206  84.192  1.00 113.57 ?  398 PHE   A CB  1 
ATOM   1776 C CG  . PHE   A 1 276 ? 19.098  43.980  82.963  1.00 110.54 ?  398 PHE   A CG  1 
ATOM   1777 C CD1 . PHE   A 1 276 ? 20.432  44.289  82.740  1.00 111.37 ?  398 PHE   A CD1 1 
ATOM   1778 C CD2 . PHE   A 1 276 ? 18.164  44.381  82.017  1.00 109.83 ?  398 PHE   A CD2 1 
ATOM   1779 C CE1 . PHE   A 1 276 ? 20.825  44.998  81.599  1.00 110.35 ?  398 PHE   A CE1 1 
ATOM   1780 C CE2 . PHE   A 1 276 ? 18.549  45.087  80.881  1.00 106.28 ?  398 PHE   A CE2 1 
ATOM   1781 C CZ  . PHE   A 1 276 ? 19.883  45.394  80.676  1.00 107.34 ?  398 PHE   A CZ  1 
ATOM   1782 N N   . ASN   A 1 277 ? 19.158  45.990  86.582  1.00 117.99 ?  399 ASN   A N   1 
ATOM   1783 C CA  . ASN   A 1 277 ? 18.488  47.215  86.976  1.00 114.47 ?  399 ASN   A CA  1 
ATOM   1784 C C   . ASN   A 1 277 ? 19.327  48.481  86.864  1.00 114.14 ?  399 ASN   A C   1 
ATOM   1785 O O   . ASN   A 1 277 ? 18.786  49.566  87.081  1.00 115.33 ?  399 ASN   A O   1 
ATOM   1786 C CB  . ASN   A 1 277 ? 17.944  47.043  88.393  1.00 119.16 ?  399 ASN   A CB  1 
ATOM   1787 C CG  . ASN   A 1 277 ? 16.660  46.234  88.412  1.00 115.19 ?  399 ASN   A CG  1 
ATOM   1788 O OD1 . ASN   A 1 277 ? 15.768  46.456  87.591  1.00 111.87 ?  399 ASN   A OD1 1 
ATOM   1789 N ND2 . ASN   A 1 277 ? 16.568  45.283  89.330  1.00 114.59 ?  399 ASN   A ND2 1 
ATOM   1790 N N   . VAL   A 1 278 ? 20.600  48.392  86.479  1.00 119.19 ?  400 VAL   A N   1 
ATOM   1791 C CA  . VAL   A 1 278 ? 21.435  49.555  86.171  1.00 122.02 ?  400 VAL   A CA  1 
ATOM   1792 C C   . VAL   A 1 278 ? 22.306  49.245  84.953  1.00 125.64 ?  400 VAL   A C   1 
ATOM   1793 O O   . VAL   A 1 278 ? 22.940  48.188  84.892  1.00 130.23 ?  400 VAL   A O   1 
ATOM   1794 C CB  . VAL   A 1 278 ? 22.326  49.949  87.363  1.00 123.35 ?  400 VAL   A CB  1 
ATOM   1795 C CG1 . VAL   A 1 278 ? 23.218  51.128  86.982  1.00 125.33 ?  400 VAL   A CG1 1 
ATOM   1796 C CG2 . VAL   A 1 278 ? 21.484  50.254  88.593  1.00 115.12 ?  400 VAL   A CG2 1 
ATOM   1797 N N   . LEU   A 1 279 ? 22.372  50.173  83.998  1.00 127.83 ?  401 LEU   A N   1 
ATOM   1798 C CA  . LEU   A 1 279 ? 23.100  49.962  82.741  1.00 132.52 ?  401 LEU   A CA  1 
ATOM   1799 C C   . LEU   A 1 279 ? 24.022  51.149  82.485  1.00 134.70 ?  401 LEU   A C   1 
ATOM   1800 O O   . LEU   A 1 279 ? 23.611  52.134  81.860  1.00 133.13 ?  401 LEU   A O   1 
ATOM   1801 C CB  . LEU   A 1 279 ? 22.135  49.756  81.575  1.00 130.21 ?  401 LEU   A CB  1 
ATOM   1802 C CG  . LEU   A 1 279 ? 22.755  49.074  80.358  1.00 133.26 ?  401 LEU   A CG  1 
ATOM   1803 C CD1 . LEU   A 1 279 ? 23.826  48.071  80.795  1.00 134.38 ?  401 LEU   A CD1 1 
ATOM   1804 C CD2 . LEU   A 1 279 ? 21.683  48.414  79.510  1.00 127.76 ?  401 LEU   A CD2 1 
ATOM   1805 N N   . ASN   A 1 280 ? 25.275  51.029  82.924  1.00 134.59 ?  402 ASN   A N   1 
ATOM   1806 C CA  . ASN   A 1 280 ? 26.237  52.128  82.865  1.00 139.14 ?  402 ASN   A CA  1 
ATOM   1807 C C   . ASN   A 1 280 ? 25.697  53.322  83.657  1.00 136.50 ?  402 ASN   A C   1 
ATOM   1808 O O   . ASN   A 1 280 ? 25.402  54.401  83.122  1.00 131.86 ?  402 ASN   A O   1 
ATOM   1809 C CB  . ASN   A 1 280 ? 26.589  52.523  81.416  1.00 148.48 ?  402 ASN   A CB  1 
ATOM   1810 C CG  . ASN   A 1 280 ? 26.806  51.310  80.486  1.00 158.06 ?  402 ASN   A CG  1 
ATOM   1811 O OD1 . ASN   A 1 280 ? 26.392  51.336  79.317  1.00 152.51 ?  402 ASN   A OD1 1 
ATOM   1812 N ND2 . ASN   A 1 280 ? 27.452  50.250  81.001  1.00 156.46 ?  402 ASN   A ND2 1 
ATOM   1813 N N   . ASN   A 1 281 ? 25.520  53.069  84.956  1.00 136.51 ?  403 ASN   A N   1 
ATOM   1814 C CA  . ASN   A 1 281 ? 25.184  54.056  85.980  1.00 131.59 ?  403 ASN   A CA  1 
ATOM   1815 C C   . ASN   A 1 281 ? 24.231  55.046  85.315  1.00 126.63 ?  403 ASN   A C   1 
ATOM   1816 O O   . ASN   A 1 281 ? 24.457  56.257  85.400  1.00 125.85 ?  403 ASN   A O   1 
ATOM   1817 C CB  . ASN   A 1 281 ? 26.177  55.225  85.953  1.00 136.24 ?  403 ASN   A CB  1 
ATOM   1818 C CG  . ASN   A 1 281 ? 27.568  54.827  86.447  1.00 142.58 ?  403 ASN   A CG  1 
ATOM   1819 O OD1 . ASN   A 1 281 ? 28.021  53.707  86.221  1.00 147.50 ?  403 ASN   A OD1 1 
ATOM   1820 N ND2 . ASN   A 1 281 ? 28.241  55.742  87.139  1.00 146.53 ?  403 ASN   A ND2 1 
ATOM   1821 N N   . LYS   A 1 282 ? 23.121  54.546  84.642  1.00 124.49 ?  404 LYS   A N   1 
ATOM   1822 C CA  . LYS   A 1 282 ? 21.731  54.991  84.581  1.00 118.66 ?  404 LYS   A CA  1 
ATOM   1823 C C   . LYS   A 1 282 ? 20.778  53.852  84.953  1.00 115.64 ?  404 LYS   A C   1 
ATOM   1824 O O   . LYS   A 1 282 ? 21.122  52.677  84.806  1.00 117.75 ?  404 LYS   A O   1 
ATOM   1825 C CB  . LYS   A 1 282 ? 21.402  55.505  83.182  1.00 112.17 ?  404 LYS   A CB  1 
ATOM   1826 C CG  . LYS   A 1 282 ? 22.528  56.305  82.529  1.00 113.10 ?  404 LYS   A CG  1 
ATOM   1827 C CD  . LYS   A 1 282 ? 21.955  57.289  81.508  1.00 121.08 ?  404 LYS   A CD  1 
ATOM   1828 C CE  . LYS   A 1 282 ? 22.437  57.005  80.082  1.00 122.11 ?  404 LYS   A CE  1 
ATOM   1829 N NZ  . LYS   A 1 282 ? 21.733  57.821  79.041  1.00 109.01 ?  404 LYS   A NZ  1 
ATOM   1830 N N   . PRO   A 1 283 ? 19.581  54.133  85.471  1.00 113.47 ?  405 PRO   A N   1 
ATOM   1831 C CA  . PRO   A 1 283 ? 18.619  53.055  85.718  1.00 108.39 ?  405 PRO   A CA  1 
ATOM   1832 C C   . PRO   A 1 283 ? 18.039  52.534  84.415  1.00 107.63 ?  405 PRO   A C   1 
ATOM   1833 O O   . PRO   A 1 283 ? 18.137  53.144  83.348  1.00 107.79 ?  405 PRO   A O   1 
ATOM   1834 C CB  . PRO   A 1 283 ? 17.540  53.712  86.585  1.00 102.95 ?  405 PRO   A CB  1 
ATOM   1835 C CG  . PRO   A 1 283 ? 17.642  55.138  86.278  1.00 103.78 ?  405 PRO   A CG  1 
ATOM   1836 C CD  . PRO   A 1 283 ? 19.114  55.396  86.059  1.00 114.06 ?  405 PRO   A CD  1 
ATOM   1837 N N   . VAL   A 1 284 ? 17.410  51.378  84.526  1.00 104.67 ?  406 VAL   A N   1 
ATOM   1838 C CA  . VAL   A 1 284 ? 16.934  50.632  83.377  1.00 99.92  ?  406 VAL   A CA  1 
ATOM   1839 C C   . VAL   A 1 284 ? 15.466  50.939  83.167  1.00 96.24  ?  406 VAL   A C   1 
ATOM   1840 O O   . VAL   A 1 284 ? 14.668  50.872  84.113  1.00 95.65  ?  406 VAL   A O   1 
ATOM   1841 C CB  . VAL   A 1 284 ? 17.154  49.132  83.586  1.00 102.76 ?  406 VAL   A CB  1 
ATOM   1842 C CG1 . VAL   A 1 284 ? 16.543  48.362  82.447  1.00 103.90 ?  406 VAL   A CG1 1 
ATOM   1843 C CG2 . VAL   A 1 284 ? 18.622  48.868  83.684  1.00 108.44 ?  406 VAL   A CG2 1 
ATOM   1844 N N   . SER   A 1 285 ? 15.104  51.263  81.933  1.00 89.61  ?  407 SER   A N   1 
ATOM   1845 C CA  . SER   A 1 285 ? 13.700  51.485  81.640  1.00 91.91  ?  407 SER   A CA  1 
ATOM   1846 C C   . SER   A 1 285 ? 13.023  50.174  81.246  1.00 90.28  ?  407 SER   A C   1 
ATOM   1847 O O   . SER   A 1 285 ? 13.663  49.142  81.068  1.00 91.68  ?  407 SER   A O   1 
ATOM   1848 C CB  . SER   A 1 285 ? 13.534  52.569  80.567  1.00 89.45  ?  407 SER   A CB  1 
ATOM   1849 O OG  . SER   A 1 285 ? 13.807  52.143  79.255  1.00 87.38  ?  407 SER   A OG  1 
ATOM   1850 N N   . LEU   A 1 286 ? 11.695  50.205  81.187  1.00 90.36  ?  408 LEU   A N   1 
ATOM   1851 C CA  . LEU   A 1 286 ? 10.965  49.053  80.679  1.00 89.68  ?  408 LEU   A CA  1 
ATOM   1852 C C   . LEU   A 1 286 ? 11.292  48.824  79.214  1.00 92.30  ?  408 LEU   A C   1 
ATOM   1853 O O   . LEU   A 1 286 ? 11.704  47.730  78.823  1.00 97.86  ?  408 LEU   A O   1 
ATOM   1854 C CB  . LEU   A 1 286 ? 9.468   49.250  80.869  1.00 88.87  ?  408 LEU   A CB  1 
ATOM   1855 C CG  . LEU   A 1 286 ? 8.640   48.081  80.381  1.00 88.22  ?  408 LEU   A CG  1 
ATOM   1856 C CD1 . LEU   A 1 286 ? 9.013   46.851  81.169  1.00 87.79  ?  408 LEU   A CD1 1 
ATOM   1857 C CD2 . LEU   A 1 286 ? 7.182   48.408  80.551  1.00 92.07  ?  408 LEU   A CD2 1 
ATOM   1858 N N   . GLY   A 1 287 ? 11.132  49.858  78.390  1.00 88.34  ?  409 GLY   A N   1 
ATOM   1859 C CA  . GLY   A 1 287 ? 11.501  49.753  76.989  1.00 90.48  ?  409 GLY   A CA  1 
ATOM   1860 C C   . GLY   A 1 287 ? 12.931  49.301  76.743  1.00 90.58  ?  409 GLY   A C   1 
ATOM   1861 O O   . GLY   A 1 287 ? 13.212  48.668  75.728  1.00 102.14 ?  409 GLY   A O   1 
ATOM   1862 N N   . GLN   A 1 288 ? 13.858  49.636  77.634  1.00 84.10  ?  410 GLN   A N   1 
ATOM   1863 C CA  . GLN   A 1 288 ? 15.205  49.089  77.516  1.00 85.51  ?  410 GLN   A CA  1 
ATOM   1864 C C   . GLN   A 1 288 ? 15.177  47.574  77.624  1.00 94.43  ?  410 GLN   A C   1 
ATOM   1865 O O   . GLN   A 1 288 ? 15.554  46.855  76.695  1.00 102.38 ?  410 GLN   A O   1 
ATOM   1866 C CB  . GLN   A 1 288 ? 16.083  49.656  78.616  1.00 92.51  ?  410 GLN   A CB  1 
ATOM   1867 C CG  . GLN   A 1 288 ? 17.060  50.708  78.236  1.00 98.61  ?  410 GLN   A CG  1 
ATOM   1868 C CD  . GLN   A 1 288 ? 17.713  51.296  79.484  1.00 109.09 ?  410 GLN   A CD  1 
ATOM   1869 O OE1 . GLN   A 1 288 ? 18.361  50.580  80.265  1.00 106.06 ?  410 GLN   A OE1 1 
ATOM   1870 N NE2 . GLN   A 1 288 ? 17.510  52.604  79.700  1.00 112.85 ?  410 GLN   A NE2 1 
ATOM   1871 N N   . ALA   A 1 289 ? 14.738  47.073  78.776  1.00 95.09  ?  411 ALA   A N   1 
ATOM   1872 C CA  . ALA   A 1 289 ? 14.666  45.639  79.000  1.00 94.33  ?  411 ALA   A CA  1 
ATOM   1873 C C   . ALA   A 1 289 ? 13.810  44.953  77.944  1.00 97.18  ?  411 ALA   A C   1 
ATOM   1874 O O   . ALA   A 1 289 ? 14.143  43.852  77.495  1.00 103.18 ?  411 ALA   A O   1 
ATOM   1875 C CB  . ALA   A 1 289 ? 14.125  45.360  80.402  1.00 96.76  ?  411 ALA   A CB  1 
ATOM   1876 N N   . LEU   A 1 290 ? 12.717  45.584  77.515  1.00 94.47  ?  412 LEU   A N   1 
ATOM   1877 C CA  . LEU   A 1 290 ? 11.922  44.978  76.455  1.00 94.69  ?  412 LEU   A CA  1 
ATOM   1878 C C   . LEU   A 1 290 ? 12.671  44.855  75.146  1.00 100.97 ?  412 LEU   A C   1 
ATOM   1879 O O   . LEU   A 1 290 ? 12.113  44.358  74.168  1.00 108.70 ?  412 LEU   A O   1 
ATOM   1880 C CB  . LEU   A 1 290 ? 10.635  45.735  76.158  1.00 88.21  ?  412 LEU   A CB  1 
ATOM   1881 C CG  . LEU   A 1 290 ? 9.446   45.406  77.018  1.00 88.29  ?  412 LEU   A CG  1 
ATOM   1882 C CD1 . LEU   A 1 290 ? 8.371   46.400  76.750  1.00 93.96  ?  412 LEU   A CD1 1 
ATOM   1883 C CD2 . LEU   A 1 290 ? 8.994   44.069  76.620  1.00 93.38  ?  412 LEU   A CD2 1 
ATOM   1884 N N   . GLU   A 1 291 ? 13.911  45.296  75.074  1.00 101.68 ?  413 GLU   A N   1 
ATOM   1885 C CA  . GLU   A 1 291 ? 14.622  45.028  73.842  1.00 103.24 ?  413 GLU   A CA  1 
ATOM   1886 C C   . GLU   A 1 291 ? 15.783  44.091  74.042  1.00 104.66 ?  413 GLU   A C   1 
ATOM   1887 O O   . GLU   A 1 291 ? 16.029  43.237  73.192  1.00 110.45 ?  413 GLU   A O   1 
ATOM   1888 C CB  . GLU   A 1 291 ? 15.103  46.319  73.217  1.00 107.76 ?  413 GLU   A CB  1 
ATOM   1889 C CG  . GLU   A 1 291 ? 14.017  46.835  72.330  1.00 116.99 ?  413 GLU   A CG  1 
ATOM   1890 C CD  . GLU   A 1 291 ? 14.490  47.912  71.440  1.00 127.87 ?  413 GLU   A CD  1 
ATOM   1891 O OE1 . GLU   A 1 291 ? 15.268  48.776  71.932  1.00 128.10 ?  413 GLU   A OE1 1 
ATOM   1892 O OE2 . GLU   A 1 291 ? 14.032  47.902  70.271  1.00 130.74 ?  413 GLU   A OE2 1 
ATOM   1893 N N   . VAL   A 1 292 ? 16.473  44.214  75.172  1.00 101.92 ?  414 VAL   A N   1 
ATOM   1894 C CA  . VAL   A 1 292 ? 17.391  43.169  75.581  1.00 104.84 ?  414 VAL   A CA  1 
ATOM   1895 C C   . VAL   A 1 292 ? 16.668  41.848  75.788  1.00 104.68 ?  414 VAL   A C   1 
ATOM   1896 O O   . VAL   A 1 292 ? 17.303  40.795  75.772  1.00 111.90 ?  414 VAL   A O   1 
ATOM   1897 C CB  . VAL   A 1 292 ? 18.152  43.635  76.830  1.00 106.36 ?  414 VAL   A CB  1 
ATOM   1898 C CG1 . VAL   A 1 292 ? 18.905  42.495  77.486  1.00 109.37 ?  414 VAL   A CG1 1 
ATOM   1899 C CG2 . VAL   A 1 292 ? 19.125  44.721  76.421  1.00 114.45 ?  414 VAL   A CG2 1 
ATOM   1900 N N   . VAL   A 1 293 ? 15.347  41.854  75.938  1.00 103.29 ?  415 VAL   A N   1 
ATOM   1901 C CA  . VAL   A 1 293 ? 14.631  40.585  75.861  1.00 103.47 ?  415 VAL   A CA  1 
ATOM   1902 C C   . VAL   A 1 293 ? 14.284  40.235  74.423  1.00 102.64 ?  415 VAL   A C   1 
ATOM   1903 O O   . VAL   A 1 293 ? 14.464  39.092  74.006  1.00 107.13 ?  415 VAL   A O   1 
ATOM   1904 C CB  . VAL   A 1 293 ? 13.389  40.587  76.764  1.00 101.51 ?  415 VAL   A CB  1 
ATOM   1905 C CG1 . VAL   A 1 293 ? 12.336  39.623  76.242  1.00 94.92  ?  415 VAL   A CG1 1 
ATOM   1906 C CG2 . VAL   A 1 293 ? 13.813  40.172  78.143  1.00 100.63 ?  415 VAL   A CG2 1 
ATOM   1907 N N   . ILE   A 1 294 ? 13.831  41.192  73.616  1.00 98.27  ?  416 ILE   A N   1 
ATOM   1908 C CA  . ILE   A 1 294 ? 13.605  40.862  72.215  1.00 99.70  ?  416 ILE   A CA  1 
ATOM   1909 C C   . ILE   A 1 294 ? 14.902  40.511  71.498  1.00 104.57 ?  416 ILE   A C   1 
ATOM   1910 O O   . ILE   A 1 294 ? 14.897  39.709  70.562  1.00 109.11 ?  416 ILE   A O   1 
ATOM   1911 C CB  . ILE   A 1 294 ? 12.840  41.989  71.503  1.00 95.86  ?  416 ILE   A CB  1 
ATOM   1912 C CG1 . ILE   A 1 294 ? 11.347  41.781  71.709  1.00 91.72  ?  416 ILE   A CG1 1 
ATOM   1913 C CG2 . ILE   A 1 294 ? 13.196  42.057  70.036  1.00 102.48 ?  416 ILE   A CG2 1 
ATOM   1914 C CD1 . ILE   A 1 294 ? 10.514  42.867  71.148  1.00 97.97  ?  416 ILE   A CD1 1 
ATOM   1915 N N   . GLN   A 1 295 ? 16.033  41.062  71.921  1.00 107.36 ?  417 GLN   A N   1 
ATOM   1916 C CA  . GLN   A 1 295 ? 17.272  40.706  71.237  1.00 106.49 ?  417 GLN   A CA  1 
ATOM   1917 C C   . GLN   A 1 295 ? 17.717  39.302  71.603  1.00 107.30 ?  417 GLN   A C   1 
ATOM   1918 O O   . GLN   A 1 295 ? 18.050  38.501  70.727  1.00 111.20 ?  417 GLN   A O   1 
ATOM   1919 C CB  . GLN   A 1 295 ? 18.370  41.709  71.545  1.00 107.78 ?  417 GLN   A CB  1 
ATOM   1920 C CG  . GLN   A 1 295 ? 18.354  42.852  70.576  1.00 109.85 ?  417 GLN   A CG  1 
ATOM   1921 C CD  . GLN   A 1 295 ? 18.679  44.155  71.236  1.00 118.06 ?  417 GLN   A CD  1 
ATOM   1922 O OE1 . GLN   A 1 295 ? 19.404  44.203  72.238  1.00 120.65 ?  417 GLN   A OE1 1 
ATOM   1923 N NE2 . GLN   A 1 295 ? 18.133  45.234  70.689  1.00 122.75 ?  417 GLN   A NE2 1 
ATOM   1924 N N   . LEU   A 1 296 ? 17.728  38.984  72.895  1.00 108.05 ?  418 LEU   A N   1 
ATOM   1925 C CA  . LEU   A 1 296 ? 18.039  37.631  73.334  1.00 108.50 ?  418 LEU   A CA  1 
ATOM   1926 C C   . LEU   A 1 296 ? 17.132  36.590  72.705  1.00 111.52 ?  418 LEU   A C   1 
ATOM   1927 O O   . LEU   A 1 296 ? 17.515  35.419  72.628  1.00 117.34 ?  418 LEU   A O   1 
ATOM   1928 C CB  . LEU   A 1 296 ? 17.961  37.552  74.853  1.00 105.51 ?  418 LEU   A CB  1 
ATOM   1929 C CG  . LEU   A 1 296 ? 19.334  37.648  75.503  1.00 113.21 ?  418 LEU   A CG  1 
ATOM   1930 C CD1 . LEU   A 1 296 ? 19.960  38.956  75.234  1.00 117.75 ?  418 LEU   A CD1 1 
ATOM   1931 C CD2 . LEU   A 1 296 ? 19.151  37.523  76.987  1.00 124.71 ?  418 LEU   A CD2 1 
ATOM   1932 N N   . GLN   A 1 297 ? 15.950  36.980  72.236  1.00 108.63 ?  419 GLN   A N   1 
ATOM   1933 C CA  . GLN   A 1 297 ? 15.125  36.026  71.508  1.00 112.06 ?  419 GLN   A CA  1 
ATOM   1934 C C   . GLN   A 1 297 ? 15.610  35.876  70.066  1.00 117.04 ?  419 GLN   A C   1 
ATOM   1935 O O   . GLN   A 1 297 ? 15.986  34.777  69.650  1.00 125.15 ?  419 GLN   A O   1 
ATOM   1936 C CB  . GLN   A 1 297 ? 13.651  36.429  71.573  1.00 107.98 ?  419 GLN   A CB  1 
ATOM   1937 C CG  . GLN   A 1 297 ? 13.095  36.369  72.979  1.00 109.31 ?  419 GLN   A CG  1 
ATOM   1938 C CD  . GLN   A 1 297 ? 13.494  35.108  73.710  1.00 117.18 ?  419 GLN   A CD  1 
ATOM   1939 O OE1 . GLN   A 1 297 ? 14.416  35.106  74.539  1.00 112.92 ?  419 GLN   A OE1 1 
ATOM   1940 N NE2 . GLN   A 1 297 ? 12.780  34.028  73.430  1.00 121.94 ?  419 GLN   A NE2 1 
ATOM   1941 N N   . GLU   A 1 298 ? 15.635  36.965  69.293  1.00 114.02 ?  420 GLU   A N   1 
ATOM   1942 C CA  . GLU   A 1 298 ? 16.284  36.943  67.982  1.00 115.92 ?  420 GLU   A CA  1 
ATOM   1943 C C   . GLU   A 1 298 ? 17.652  36.269  68.013  1.00 119.70 ?  420 GLU   A C   1 
ATOM   1944 O O   . GLU   A 1 298 ? 18.050  35.623  67.037  1.00 119.03 ?  420 GLU   A O   1 
ATOM   1945 C CB  . GLU   A 1 298 ? 16.467  38.354  67.433  1.00 116.23 ?  420 GLU   A CB  1 
ATOM   1946 C CG  . GLU   A 1 298 ? 15.479  38.745  66.390  1.00 121.44 ?  420 GLU   A CG  1 
ATOM   1947 C CD  . GLU   A 1 298 ? 15.350  40.237  66.321  1.00 126.20 ?  420 GLU   A CD  1 
ATOM   1948 O OE1 . GLU   A 1 298 ? 16.059  40.925  67.102  1.00 117.17 ?  420 GLU   A OE1 1 
ATOM   1949 O OE2 . GLU   A 1 298 ? 14.554  40.714  65.483  1.00 135.55 ?  420 GLU   A OE2 1 
ATOM   1950 N N   . LYS   A 1 299 ? 18.387  36.432  69.119  1.00 117.91 ?  421 LYS   A N   1 
ATOM   1951 C CA  . LYS   A 1 299 ? 19.695  35.798  69.225  1.00 114.01 ?  421 LYS   A CA  1 
ATOM   1952 C C   . LYS   A 1 299 ? 19.555  34.293  69.303  1.00 119.73 ?  421 LYS   A C   1 
ATOM   1953 O O   . LYS   A 1 299 ? 20.175  33.564  68.523  1.00 130.49 ?  421 LYS   A O   1 
ATOM   1954 C CB  . LYS   A 1 299 ? 20.461  36.312  70.438  1.00 112.74 ?  421 LYS   A CB  1 
ATOM   1955 C CG  . LYS   A 1 299 ? 21.816  35.678  70.593  1.00 106.10 ?  421 LYS   A CG  1 
ATOM   1956 C CD  . LYS   A 1 299 ? 21.894  34.954  71.891  1.00 112.13 ?  421 LYS   A CD  1 
ATOM   1957 C CE  . LYS   A 1 299 ? 23.307  34.978  72.385  1.00 115.60 ?  421 LYS   A CE  1 
ATOM   1958 N NZ  . LYS   A 1 299 ? 23.454  34.142  73.595  1.00 124.32 ?  421 LYS   A NZ  1 
ATOM   1959 N N   . HIS   A 1 300 ? 18.727  33.803  70.222  1.00 118.37 ?  422 HIS   A N   1 
ATOM   1960 C CA  . HIS   A 1 300 ? 18.601  32.358  70.368  1.00 123.16 ?  422 HIS   A CA  1 
ATOM   1961 C C   . HIS   A 1 300 ? 17.949  31.711  69.139  1.00 121.86 ?  422 HIS   A C   1 
ATOM   1962 O O   . HIS   A 1 300 ? 18.278  30.568  68.813  1.00 127.14 ?  422 HIS   A O   1 
ATOM   1963 C CB  . HIS   A 1 300 ? 17.870  32.053  71.678  1.00 126.63 ?  422 HIS   A CB  1 
ATOM   1964 C CG  . HIS   A 1 300 ? 17.060  30.792  71.675  1.00 126.12 ?  422 HIS   A CG  1 
ATOM   1965 N ND1 . HIS   A 1 300 ? 15.781  30.724  71.163  1.00 127.84 ?  422 HIS   A ND1 1 
ATOM   1966 C CD2 . HIS   A 1 300 ? 17.330  29.562  72.170  1.00 121.71 ?  422 HIS   A CD2 1 
ATOM   1967 C CE1 . HIS   A 1 300 ? 15.304  29.503  71.329  1.00 125.29 ?  422 HIS   A CE1 1 
ATOM   1968 N NE2 . HIS   A 1 300 ? 16.224  28.778  71.937  1.00 124.31 ?  422 HIS   A NE2 1 
ATOM   1969 N N   . VAL   A 1 301 ? 17.081  32.425  68.406  1.00 116.46 ?  423 VAL   A N   1 
ATOM   1970 C CA  . VAL   A 1 301 ? 16.635  31.925  67.099  1.00 120.99 ?  423 VAL   A CA  1 
ATOM   1971 C C   . VAL   A 1 301 ? 17.826  31.633  66.185  1.00 125.29 ?  423 VAL   A C   1 
ATOM   1972 O O   . VAL   A 1 301 ? 17.787  30.706  65.362  1.00 126.31 ?  423 VAL   A O   1 
ATOM   1973 C CB  . VAL   A 1 301 ? 15.655  32.920  66.436  1.00 120.85 ?  423 VAL   A CB  1 
ATOM   1974 C CG1 . VAL   A 1 301 ? 15.563  32.678  64.941  1.00 121.89 ?  423 VAL   A CG1 1 
ATOM   1975 C CG2 . VAL   A 1 301 ? 14.282  32.786  67.035  1.00 120.81 ?  423 VAL   A CG2 1 
ATOM   1976 N N   . LYS   A 1 302 ? 18.903  32.401  66.323  1.00 124.46 ?  424 LYS   A N   1 
ATOM   1977 C CA  . LYS   A 1 302 ? 20.094  32.170  65.521  1.00 117.73 ?  424 LYS   A CA  1 
ATOM   1978 C C   . LYS   A 1 302 ? 20.974  31.075  66.116  1.00 120.37 ?  424 LYS   A C   1 
ATOM   1979 O O   . LYS   A 1 302 ? 21.374  30.156  65.399  1.00 125.03 ?  424 LYS   A O   1 
ATOM   1980 C CB  . LYS   A 1 302 ? 20.846  33.480  65.355  1.00 112.08 ?  424 LYS   A CB  1 
ATOM   1981 C CG  . LYS   A 1 302 ? 19.991  34.459  64.605  1.00 116.17 ?  424 LYS   A CG  1 
ATOM   1982 C CD  . LYS   A 1 302 ? 20.613  35.817  64.486  1.00 117.20 ?  424 LYS   A CD  1 
ATOM   1983 C CE  . LYS   A 1 302 ? 19.534  36.823  64.128  1.00 119.55 ?  424 LYS   A CE  1 
ATOM   1984 N NZ  . LYS   A 1 302 ? 19.010  36.651  62.743  1.00 108.82 ?  424 LYS   A NZ  1 
ATOM   1985 N N   . ASP   A 1 303 ? 21.264  31.125  67.425  1.00 117.08 ?  425 ASP   A N   1 
ATOM   1986 C CA  . ASP   A 1 303 ? 21.988  30.012  68.045  1.00 123.87 ?  425 ASP   A CA  1 
ATOM   1987 C C   . ASP   A 1 303 ? 21.373  28.662  67.694  1.00 127.45 ?  425 ASP   A C   1 
ATOM   1988 O O   . ASP   A 1 303 ? 22.068  27.635  67.709  1.00 126.83 ?  425 ASP   A O   1 
ATOM   1989 C CB  . ASP   A 1 303 ? 22.031  30.113  69.582  1.00 128.08 ?  425 ASP   A CB  1 
ATOM   1990 C CG  . ASP   A 1 303 ? 22.741  31.350  70.104  1.00 127.04 ?  425 ASP   A CG  1 
ATOM   1991 O OD1 . ASP   A 1 303 ? 23.925  31.572  69.759  1.00 126.58 ?  425 ASP   A OD1 1 
ATOM   1992 O OD2 . ASP   A 1 303 ? 22.134  32.049  70.943  1.00 130.89 ?  425 ASP   A OD2 1 
ATOM   1993 N N   . GLU   A 1 304 ? 20.072  28.638  67.391  1.00 124.78 ?  426 GLU   A N   1 
ATOM   1994 C CA  . GLU   A 1 304 ? 19.400  27.368  67.175  1.00 125.06 ?  426 GLU   A CA  1 
ATOM   1995 C C   . GLU   A 1 304 ? 19.378  26.975  65.705  1.00 128.30 ?  426 GLU   A C   1 
ATOM   1996 O O   . GLU   A 1 304 ? 19.596  25.803  65.382  1.00 130.96 ?  426 GLU   A O   1 
ATOM   1997 C CB  . GLU   A 1 304 ? 17.982  27.403  67.740  1.00 121.92 ?  426 GLU   A CB  1 
ATOM   1998 C CG  . GLU   A 1 304 ? 17.362  26.027  67.782  1.00 126.26 ?  426 GLU   A CG  1 
ATOM   1999 C CD  . GLU   A 1 304 ? 16.570  25.774  69.049  1.00 130.36 ?  426 GLU   A CD  1 
ATOM   2000 O OE1 . GLU   A 1 304 ? 15.368  26.116  69.086  1.00 139.59 ?  426 GLU   A OE1 1 
ATOM   2001 O OE2 . GLU   A 1 304 ? 17.169  25.252  70.020  1.00 122.98 ?  426 GLU   A OE2 1 
ATOM   2002 N N   . GLN   A 1 305 ? 19.132  27.916  64.795  1.00 124.61 ?  427 GLN   A N   1 
ATOM   2003 C CA  . GLN   A 1 305 ? 19.458  27.634  63.406  1.00 124.19 ?  427 GLN   A CA  1 
ATOM   2004 C C   . GLN   A 1 305 ? 20.889  27.129  63.279  1.00 126.97 ?  427 GLN   A C   1 
ATOM   2005 O O   . GLN   A 1 305 ? 21.151  26.164  62.554  1.00 128.58 ?  427 GLN   A O   1 
ATOM   2006 C CB  . GLN   A 1 305 ? 19.277  28.871  62.543  1.00 125.62 ?  427 GLN   A CB  1 
ATOM   2007 C CG  . GLN   A 1 305 ? 18.102  28.847  61.631  1.00 126.30 ?  427 GLN   A CG  1 
ATOM   2008 C CD  . GLN   A 1 305 ? 17.759  30.244  61.173  1.00 136.85 ?  427 GLN   A CD  1 
ATOM   2009 O OE1 . GLN   A 1 305 ? 18.598  31.145  61.222  1.00 136.69 ?  427 GLN   A OE1 1 
ATOM   2010 N NE2 . GLN   A 1 305 ? 16.524  30.443  60.739  1.00 139.63 ?  427 GLN   A NE2 1 
ATOM   2011 N N   . ILE   A 1 306 ? 21.829  27.759  63.989  1.00 125.21 ?  428 ILE   A N   1 
ATOM   2012 C CA  . ILE   A 1 306 ? 23.235  27.389  63.847  1.00 122.29 ?  428 ILE   A CA  1 
ATOM   2013 C C   . ILE   A 1 306 ? 23.475  25.967  64.342  1.00 127.14 ?  428 ILE   A C   1 
ATOM   2014 O O   . ILE   A 1 306 ? 23.991  25.127  63.602  1.00 129.61 ?  428 ILE   A O   1 
ATOM   2015 C CB  . ILE   A 1 306 ? 24.146  28.407  64.548  1.00 121.06 ?  428 ILE   A CB  1 
ATOM   2016 C CG1 . ILE   A 1 306 ? 24.361  29.602  63.617  1.00 122.40 ?  428 ILE   A CG1 1 
ATOM   2017 C CG2 . ILE   A 1 306 ? 25.463  27.759  64.977  1.00 118.91 ?  428 ILE   A CG2 1 
ATOM   2018 C CD1 . ILE   A 1 306 ? 25.304  30.618  64.166  1.00 127.53 ?  428 ILE   A CD1 1 
ATOM   2019 N N   . GLU   A 1 307 ? 23.097  25.651  65.581  1.00 127.00 ?  429 GLU   A N   1 
ATOM   2020 C CA  . GLU   A 1 307 ? 23.413  24.288  66.009  1.00 128.25 ?  429 GLU   A CA  1 
ATOM   2021 C C   . GLU   A 1 307 ? 22.484  23.227  65.408  1.00 128.05 ?  429 GLU   A C   1 
ATOM   2022 O O   . GLU   A 1 307 ? 22.529  22.077  65.847  1.00 130.11 ?  429 GLU   A O   1 
ATOM   2023 C CB  . GLU   A 1 307 ? 23.423  24.146  67.534  1.00 127.96 ?  429 GLU   A CB  1 
ATOM   2024 C CG  . GLU   A 1 307 ? 22.069  23.930  68.172  1.00 131.72 ?  429 GLU   A CG  1 
ATOM   2025 C CD  . GLU   A 1 307 ? 22.188  23.219  69.513  1.00 137.46 ?  429 GLU   A CD  1 
ATOM   2026 O OE1 . GLU   A 1 307 ? 22.906  23.724  70.405  1.00 142.54 ?  429 GLU   A OE1 1 
ATOM   2027 O OE2 . GLU   A 1 307 ? 21.550  22.153  69.674  1.00 134.51 ?  429 GLU   A OE2 1 
ATOM   2028 N N   . HIS   A 1 308 ? 21.670  23.558  64.408  1.00 127.84 ?  430 HIS   A N   1 
ATOM   2029 C CA  . HIS   A 1 308 ? 20.960  22.541  63.639  1.00 128.54 ?  430 HIS   A CA  1 
ATOM   2030 C C   . HIS   A 1 308 ? 21.596  22.322  62.276  1.00 129.17 ?  430 HIS   A C   1 
ATOM   2031 O O   . HIS   A 1 308 ? 21.870  21.180  61.904  1.00 131.64 ?  430 HIS   A O   1 
ATOM   2032 C CB  . HIS   A 1 308 ? 19.491  22.916  63.455  1.00 133.31 ?  430 HIS   A CB  1 
ATOM   2033 C CG  . HIS   A 1 308 ? 18.831  22.237  62.292  1.00 133.00 ?  430 HIS   A CG  1 
ATOM   2034 N ND1 . HIS   A 1 308 ? 18.920  22.710  60.997  1.00 127.40 ?  430 HIS   A ND1 1 
ATOM   2035 C CD2 . HIS   A 1 308 ? 18.037  21.140  62.239  1.00 133.01 ?  430 HIS   A CD2 1 
ATOM   2036 C CE1 . HIS   A 1 308 ? 18.218  21.930  60.197  1.00 128.73 ?  430 HIS   A CE1 1 
ATOM   2037 N NE2 . HIS   A 1 308 ? 17.670  20.972  60.926  1.00 136.87 ?  430 HIS   A NE2 1 
ATOM   2038 N N   . TRP   A 1 309 ? 21.838  23.389  61.508  1.00 127.66 ?  431 TRP   A N   1 
ATOM   2039 C CA  . TRP   A 1 309 ? 22.694  23.196  60.350  1.00 124.54 ?  431 TRP   A CA  1 
ATOM   2040 C C   . TRP   A 1 309 ? 24.068  22.667  60.748  1.00 127.38 ?  431 TRP   A C   1 
ATOM   2041 O O   . TRP   A 1 309 ? 24.786  22.156  59.890  1.00 130.43 ?  431 TRP   A O   1 
ATOM   2042 C CB  . TRP   A 1 309 ? 22.885  24.472  59.547  1.00 118.02 ?  431 TRP   A CB  1 
ATOM   2043 C CG  . TRP   A 1 309 ? 21.674  25.045  58.945  1.00 123.86 ?  431 TRP   A CG  1 
ATOM   2044 C CD1 . TRP   A 1 309 ? 21.163  26.282  59.178  1.00 131.70 ?  431 TRP   A CD1 1 
ATOM   2045 C CD2 . TRP   A 1 309 ? 20.796  24.420  58.010  1.00 128.20 ?  431 TRP   A CD2 1 
ATOM   2046 N NE1 . TRP   A 1 309 ? 20.035  26.484  58.424  1.00 133.34 ?  431 TRP   A NE1 1 
ATOM   2047 C CE2 . TRP   A 1 309 ? 19.784  25.350  57.701  1.00 133.66 ?  431 TRP   A CE2 1 
ATOM   2048 C CE3 . TRP   A 1 309 ? 20.768  23.172  57.398  1.00 131.69 ?  431 TRP   A CE3 1 
ATOM   2049 C CZ2 . TRP   A 1 309 ? 18.748  25.064  56.813  1.00 135.81 ?  431 TRP   A CZ2 1 
ATOM   2050 C CZ3 . TRP   A 1 309 ? 19.734  22.890  56.510  1.00 141.16 ?  431 TRP   A CZ3 1 
ATOM   2051 C CH2 . TRP   A 1 309 ? 18.740  23.829  56.231  1.00 140.24 ?  431 TRP   A CH2 1 
ATOM   2052 N N   . LYS   A 1 310 ? 24.453  22.774  62.025  1.00 126.41 ?  432 LYS   A N   1 
ATOM   2053 C CA  . LYS   A 1 310 ? 25.694  22.168  62.489  1.00 124.27 ?  432 LYS   A CA  1 
ATOM   2054 C C   . LYS   A 1 310 ? 25.534  20.684  62.800  1.00 126.72 ?  432 LYS   A C   1 
ATOM   2055 O O   . LYS   A 1 310 ? 26.530  19.952  62.775  1.00 124.51 ?  432 LYS   A O   1 
ATOM   2056 C CB  . LYS   A 1 310 ? 26.217  22.900  63.724  1.00 124.08 ?  432 LYS   A CB  1 
ATOM   2057 C CG  . LYS   A 1 310 ? 27.536  23.622  63.526  1.00 122.50 ?  432 LYS   A CG  1 
ATOM   2058 C CD  . LYS   A 1 310 ? 28.021  24.161  64.872  1.00 136.36 ?  432 LYS   A CD  1 
ATOM   2059 C CE  . LYS   A 1 310 ? 29.250  25.057  64.759  1.00 143.09 ?  432 LYS   A CE  1 
ATOM   2060 N NZ  . LYS   A 1 310 ? 29.050  26.173  63.794  1.00 136.24 ?  432 LYS   A NZ  1 
ATOM   2061 N N   . LYS   A 1 311 ? 24.316  20.232  63.129  1.00 129.57 ?  433 LYS   A N   1 
ATOM   2062 C CA  . LYS   A 1 311 ? 24.025  18.799  63.101  1.00 127.35 ?  433 LYS   A CA  1 
ATOM   2063 C C   . LYS   A 1 311 ? 24.133  18.245  61.686  1.00 125.25 ?  433 LYS   A C   1 
ATOM   2064 O O   . LYS   A 1 311 ? 24.685  17.162  61.490  1.00 127.60 ?  433 LYS   A O   1 
ATOM   2065 C CB  . LYS   A 1 311 ? 22.628  18.490  63.656  1.00 131.99 ?  433 LYS   A CB  1 
ATOM   2066 C CG  . LYS   A 1 311 ? 22.263  18.968  65.069  1.00 136.16 ?  433 LYS   A CG  1 
ATOM   2067 C CD  . LYS   A 1 311 ? 21.145  18.078  65.666  1.00 134.72 ?  433 LYS   A CD  1 
ATOM   2068 C CE  . LYS   A 1 311 ? 19.782  18.503  65.037  1.00 140.51 ?  433 LYS   A CE  1 
ATOM   2069 N NZ  . LYS   A 1 311 ? 18.539  17.810  65.499  1.00 138.33 ?  433 LYS   A NZ  1 
ATOM   2070 N N   . ILE   A 1 312 ? 23.600  18.951  60.685  1.00 122.53 ?  434 ILE   A N   1 
ATOM   2071 C CA  . ILE   A 1 312 ? 23.697  18.432  59.324  1.00 121.15 ?  434 ILE   A CA  1 
ATOM   2072 C C   . ILE   A 1 312 ? 25.151  18.228  58.915  1.00 122.55 ?  434 ILE   A C   1 
ATOM   2073 O O   . ILE   A 1 312 ? 25.534  17.127  58.517  1.00 126.56 ?  434 ILE   A O   1 
ATOM   2074 C CB  . ILE   A 1 312 ? 22.924  19.305  58.320  1.00 119.23 ?  434 ILE   A CB  1 
ATOM   2075 C CG1 . ILE   A 1 312 ? 21.457  18.874  58.292  1.00 121.70 ?  434 ILE   A CG1 1 
ATOM   2076 C CG2 . ILE   A 1 312 ? 23.536  19.241  56.952  1.00 115.64 ?  434 ILE   A CG2 1 
ATOM   2077 C CD1 . ILE   A 1 312 ? 20.598  19.715  57.415  1.00 126.10 ?  434 ILE   A CD1 1 
ATOM   2078 N N   . VAL   A 1 313 ? 25.996  19.252  59.022  1.00 121.58 ?  435 VAL   A N   1 
ATOM   2079 C CA  . VAL   A 1 313 ? 27.380  19.054  58.588  1.00 120.08 ?  435 VAL   A CA  1 
ATOM   2080 C C   . VAL   A 1 313 ? 28.030  17.884  59.330  1.00 123.07 ?  435 VAL   A C   1 
ATOM   2081 O O   . VAL   A 1 313 ? 28.667  17.029  58.710  1.00 126.43 ?  435 VAL   A O   1 
ATOM   2082 C CB  . VAL   A 1 313 ? 28.212  20.340  58.731  1.00 119.55 ?  435 VAL   A CB  1 
ATOM   2083 C CG1 . VAL   A 1 313 ? 27.865  21.327  57.656  1.00 110.68 ?  435 VAL   A CG1 1 
ATOM   2084 C CG2 . VAL   A 1 313 ? 28.003  20.948  60.100  1.00 129.63 ?  435 VAL   A CG2 1 
ATOM   2085 N N   . LYS   A 1 314 ? 27.881  17.813  60.659  1.00 127.67 ?  436 LYS   A N   1 
ATOM   2086 C CA  . LYS   A 1 314 ? 28.623  16.781  61.393  1.00 133.98 ?  436 LYS   A CA  1 
ATOM   2087 C C   . LYS   A 1 314 ? 28.239  15.377  60.941  1.00 134.21 ?  436 LYS   A C   1 
ATOM   2088 O O   . LYS   A 1 314 ? 29.014  14.435  61.146  1.00 137.53 ?  436 LYS   A O   1 
ATOM   2089 C CB  . LYS   A 1 314 ? 28.434  16.905  62.921  1.00 142.58 ?  436 LYS   A CB  1 
ATOM   2090 C CG  . LYS   A 1 314 ? 29.406  16.010  63.770  1.00 148.76 ?  436 LYS   A CG  1 
ATOM   2091 C CD  . LYS   A 1 314 ? 28.781  15.432  65.071  1.00 156.88 ?  436 LYS   A CD  1 
ATOM   2092 C CE  . LYS   A 1 314 ? 29.261  13.984  65.373  1.00 159.41 ?  436 LYS   A CE  1 
ATOM   2093 N NZ  . LYS   A 1 314 ? 28.897  13.428  66.736  1.00 156.66 ?  436 LYS   A NZ  1 
ATOM   2094 N N   . THR   A 1 315 ? 27.076  15.217  60.311  1.00 131.07 ?  437 THR   A N   1 
ATOM   2095 C CA  . THR   A 1 315 ? 26.688  13.931  59.748  1.00 131.43 ?  437 THR   A CA  1 
ATOM   2096 C C   . THR   A 1 315 ? 26.957  13.866  58.243  1.00 125.22 ?  437 THR   A C   1 
ATOM   2097 O O   . THR   A 1 315 ? 27.598  12.921  57.786  1.00 132.57 ?  437 THR   A O   1 
ATOM   2098 C CB  . THR   A 1 315 ? 25.219  13.621  60.119  1.00 132.14 ?  437 THR   A CB  1 
ATOM   2099 O OG1 . THR   A 1 315 ? 24.798  12.367  59.576  1.00 133.65 ?  437 THR   A OG1 1 
ATOM   2100 C CG2 . THR   A 1 315 ? 24.293  14.669  59.627  1.00 133.34 ?  437 THR   A CG2 1 
ATOM   2101 N N   . GLN   A 1 316 ? 26.581  14.881  57.464  1.00 120.91 ?  438 GLN   A N   1 
ATOM   2102 C CA  . GLN   A 1 316 ? 27.014  14.923  56.067  1.00 118.60 ?  438 GLN   A CA  1 
ATOM   2103 C C   . GLN   A 1 316 ? 28.521  14.762  55.889  1.00 120.54 ?  438 GLN   A C   1 
ATOM   2104 O O   . GLN   A 1 316 ? 28.969  14.360  54.816  1.00 123.06 ?  438 GLN   A O   1 
ATOM   2105 C CB  . GLN   A 1 316 ? 26.579  16.224  55.416  1.00 113.96 ?  438 GLN   A CB  1 
ATOM   2106 C CG  . GLN   A 1 316 ? 26.738  16.233  53.939  1.00 113.21 ?  438 GLN   A CG  1 
ATOM   2107 C CD  . GLN   A 1 316 ? 25.430  15.987  53.270  1.00 124.36 ?  438 GLN   A CD  1 
ATOM   2108 O OE1 . GLN   A 1 316 ? 24.398  15.908  53.940  1.00 118.32 ?  438 GLN   A OE1 1 
ATOM   2109 N NE2 . GLN   A 1 316 ? 25.449  15.844  51.941  1.00 131.70 ?  438 GLN   A NE2 1 
ATOM   2110 N N   . GLU   A 1 317 ? 29.320  15.065  56.898  1.00 125.82 ?  439 GLU   A N   1 
ATOM   2111 C CA  . GLU   A 1 317 ? 30.746  14.809  56.790  1.00 126.08 ?  439 GLU   A CA  1 
ATOM   2112 C C   . GLU   A 1 317 ? 31.122  13.414  57.270  1.00 126.47 ?  439 GLU   A C   1 
ATOM   2113 O O   . GLU   A 1 317 ? 32.248  12.979  57.012  1.00 131.38 ?  439 GLU   A O   1 
ATOM   2114 C CB  . GLU   A 1 317 ? 31.544  15.869  57.564  1.00 134.56 ?  439 GLU   A CB  1 
ATOM   2115 C CG  . GLU   A 1 317 ? 32.962  16.134  57.027  1.00 141.02 ?  439 GLU   A CG  1 
ATOM   2116 C CD  . GLU   A 1 317 ? 33.561  17.463  57.517  1.00 149.58 ?  439 GLU   A CD  1 
ATOM   2117 O OE1 . GLU   A 1 317 ? 33.492  17.727  58.741  1.00 147.99 ?  439 GLU   A OE1 1 
ATOM   2118 O OE2 . GLU   A 1 317 ? 34.126  18.227  56.693  1.00 149.43 ?  439 GLU   A OE2 1 
ATOM   2119 N N   . GLU   A 1 318 ? 30.223  12.710  57.972  1.00 128.59 ?  440 GLU   A N   1 
ATOM   2120 C CA  . GLU   A 1 318 ? 30.393  11.267  58.156  1.00 129.95 ?  440 GLU   A CA  1 
ATOM   2121 C C   . GLU   A 1 318 ? 30.139  10.527  56.852  1.00 126.51 ?  440 GLU   A C   1 
ATOM   2122 O O   . GLU   A 1 318 ? 30.798  9.527   56.555  1.00 127.77 ?  440 GLU   A O   1 
ATOM   2123 C CB  . GLU   A 1 318 ? 29.440  10.726  59.219  1.00 129.77 ?  440 GLU   A CB  1 
ATOM   2124 C CG  . GLU   A 1 318 ? 29.966  10.681  60.631  1.00 140.02 ?  440 GLU   A CG  1 
ATOM   2125 C CD  . GLU   A 1 318 ? 28.893  10.211  61.619  1.00 154.01 ?  440 GLU   A CD  1 
ATOM   2126 O OE1 . GLU   A 1 318 ? 28.199  9.218   61.290  1.00 152.04 ?  440 GLU   A OE1 1 
ATOM   2127 O OE2 . GLU   A 1 318 ? 28.754  10.810  62.716  1.00 158.58 ?  440 GLU   A OE2 1 
ATOM   2128 N N   . LEU   A 1 319 ? 29.164  10.998  56.077  1.00 122.94 ?  441 LEU   A N   1 
ATOM   2129 C CA  . LEU   A 1 319 ? 28.916  10.442  54.758  1.00 120.37 ?  441 LEU   A CA  1 
ATOM   2130 C C   . LEU   A 1 319 ? 30.118  10.648  53.840  1.00 124.42 ?  441 LEU   A C   1 
ATOM   2131 O O   . LEU   A 1 319 ? 30.453  9.765   53.043  1.00 126.53 ?  441 LEU   A O   1 
ATOM   2132 C CB  . LEU   A 1 319 ? 27.671  11.090  54.165  1.00 117.84 ?  441 LEU   A CB  1 
ATOM   2133 C CG  . LEU   A 1 319 ? 26.880  10.337  53.110  1.00 117.71 ?  441 LEU   A CG  1 
ATOM   2134 C CD1 . LEU   A 1 319 ? 26.084  9.252   53.808  1.00 122.86 ?  441 LEU   A CD1 1 
ATOM   2135 C CD2 . LEU   A 1 319 ? 25.979  11.282  52.323  1.00 118.69 ?  441 LEU   A CD2 1 
ATOM   2136 N N   . LYS   A 1 320 ? 30.777  11.812  53.927  1.00 125.45 ?  442 LYS   A N   1 
ATOM   2137 C CA  . LYS   A 1 320 ? 31.985  12.032  53.131  1.00 122.96 ?  442 LYS   A CA  1 
ATOM   2138 C C   . LYS   A 1 320 ? 33.070  11.027  53.475  1.00 123.58 ?  442 LYS   A C   1 
ATOM   2139 O O   . LYS   A 1 320 ? 33.865  10.662  52.608  1.00 130.47 ?  442 LYS   A O   1 
ATOM   2140 C CB  . LYS   A 1 320 ? 32.538  13.453  53.314  1.00 121.96 ?  442 LYS   A CB  1 
ATOM   2141 C CG  . LYS   A 1 320 ? 33.709  13.810  52.379  1.00 112.21 ?  442 LYS   A CG  1 
ATOM   2142 C CD  . LYS   A 1 320 ? 34.598  14.882  53.010  1.00 120.43 ?  442 LYS   A CD  1 
ATOM   2143 C CE  . LYS   A 1 320 ? 35.567  15.511  52.019  1.00 129.27 ?  442 LYS   A CE  1 
ATOM   2144 N NZ  . LYS   A 1 320 ? 36.079  16.846  52.471  1.00 131.91 ?  442 LYS   A NZ  1 
ATOM   2145 N N   . GLU   A 1 321 ? 33.142  10.571  54.718  1.00 121.22 ?  443 GLU   A N   1 
ATOM   2146 C CA  . GLU   A 1 321 ? 34.175  9.595   55.015  1.00 128.28 ?  443 GLU   A CA  1 
ATOM   2147 C C   . GLU   A 1 321 ? 33.692  8.164   54.895  1.00 127.85 ?  443 GLU   A C   1 
ATOM   2148 O O   . GLU   A 1 321 ? 34.503  7.235   54.960  1.00 127.62 ?  443 GLU   A O   1 
ATOM   2149 C CB  . GLU   A 1 321 ? 34.768  9.833   56.395  1.00 131.76 ?  443 GLU   A CB  1 
ATOM   2150 C CG  . GLU   A 1 321 ? 35.981  10.722  56.288  1.00 137.45 ?  443 GLU   A CG  1 
ATOM   2151 C CD  . GLU   A 1 321 ? 36.830  10.683  57.524  1.00 149.52 ?  443 GLU   A CD  1 
ATOM   2152 O OE1 . GLU   A 1 321 ? 37.326  9.577   57.852  1.00 145.02 ?  443 GLU   A OE1 1 
ATOM   2153 O OE2 . GLU   A 1 321 ? 37.012  11.750  58.154  1.00 158.91 ?  443 GLU   A OE2 1 
ATOM   2154 N N   . LEU   A 1 322 ? 32.405  7.964   54.696  1.00 126.00 ?  444 LEU   A N   1 
ATOM   2155 C CA  . LEU   A 1 322 ? 31.958  6.632   54.355  1.00 121.72 ?  444 LEU   A CA  1 
ATOM   2156 C C   . LEU   A 1 322 ? 31.961  6.432   52.851  1.00 122.73 ?  444 LEU   A C   1 
ATOM   2157 O O   . LEU   A 1 322 ? 32.289  5.347   52.376  1.00 129.82 ?  444 LEU   A O   1 
ATOM   2158 C CB  . LEU   A 1 322 ? 30.569  6.394   54.916  1.00 122.18 ?  444 LEU   A CB  1 
ATOM   2159 C CG  . LEU   A 1 322 ? 30.178  4.940   54.924  1.00 120.36 ?  444 LEU   A CG  1 
ATOM   2160 C CD1 . LEU   A 1 322 ? 30.614  4.393   56.268  1.00 118.73 ?  444 LEU   A CD1 1 
ATOM   2161 C CD2 . LEU   A 1 322 ? 28.694  4.833   54.731  1.00 122.35 ?  444 LEU   A CD2 1 
ATOM   2162 N N   . LEU   A 1 323 ? 31.622  7.466   52.083  1.00 122.94 ?  445 LEU   A N   1 
ATOM   2163 C CA  . LEU   A 1 323 ? 31.720  7.337   50.636  1.00 122.62 ?  445 LEU   A CA  1 
ATOM   2164 C C   . LEU   A 1 323 ? 33.168  7.164   50.196  1.00 123.90 ?  445 LEU   A C   1 
ATOM   2165 O O   . LEU   A 1 323 ? 33.439  6.408   49.261  1.00 128.59 ?  445 LEU   A O   1 
ATOM   2166 C CB  . LEU   A 1 323 ? 31.075  8.532   49.938  1.00 122.90 ?  445 LEU   A CB  1 
ATOM   2167 C CG  . LEU   A 1 323 ? 29.553  8.593   50.078  1.00 122.43 ?  445 LEU   A CG  1 
ATOM   2168 C CD1 . LEU   A 1 323 ? 28.947  9.248   48.859  1.00 125.02 ?  445 LEU   A CD1 1 
ATOM   2169 C CD2 . LEU   A 1 323 ? 28.945  7.213   50.320  1.00 120.61 ?  445 LEU   A CD2 1 
ATOM   2170 N N   . ASN   A 1 324 ? 34.122  7.824   50.865  1.00 124.25 ?  446 ASN   A N   1 
ATOM   2171 C CA  . ASN   A 1 324 ? 35.523  7.596   50.508  1.00 125.05 ?  446 ASN   A CA  1 
ATOM   2172 C C   . ASN   A 1 324 ? 35.967  6.190   50.885  1.00 126.74 ?  446 ASN   A C   1 
ATOM   2173 O O   . ASN   A 1 324 ? 36.679  5.537   50.115  1.00 128.73 ?  446 ASN   A O   1 
ATOM   2174 C CB  . ASN   A 1 324 ? 36.455  8.632   51.144  1.00 124.53 ?  446 ASN   A CB  1 
ATOM   2175 C CG  . ASN   A 1 324 ? 36.742  9.807   50.212  1.00 132.66 ?  446 ASN   A CG  1 
ATOM   2176 O OD1 . ASN   A 1 324 ? 36.674  9.675   48.990  1.00 129.16 ?  446 ASN   A OD1 1 
ATOM   2177 N ND2 . ASN   A 1 324 ? 37.105  10.950  50.787  1.00 141.84 ?  446 ASN   A ND2 1 
ATOM   2178 N N   . LYS   A 1 325 ? 35.565  5.699   52.057  1.00 127.12 ?  447 LYS   A N   1 
ATOM   2179 C CA  . LYS   A 1 325 ? 35.900  4.319   52.396  1.00 127.95 ?  447 LYS   A CA  1 
ATOM   2180 C C   . LYS   A 1 325 ? 35.228  3.329   51.452  1.00 123.88 ?  447 LYS   A C   1 
ATOM   2181 O O   . LYS   A 1 325 ? 35.797  2.273   51.148  1.00 124.03 ?  447 LYS   A O   1 
ATOM   2182 C CB  . LYS   A 1 325 ? 35.540  4.023   53.855  1.00 130.49 ?  447 LYS   A CB  1 
ATOM   2183 C CG  . LYS   A 1 325 ? 35.773  2.572   54.239  1.00 137.66 ?  447 LYS   A CG  1 
ATOM   2184 C CD  . LYS   A 1 325 ? 37.106  2.242   54.885  1.00 143.32 ?  447 LYS   A CD  1 
ATOM   2185 C CE  . LYS   A 1 325 ? 37.257  0.704   54.916  1.00 151.75 ?  447 LYS   A CE  1 
ATOM   2186 N NZ  . LYS   A 1 325 ? 37.953  0.155   56.118  1.00 159.76 ?  447 LYS   A NZ  1 
ATOM   2187 N N   . MET   A 1 326 ? 34.040  3.659   50.954  1.00 121.32 ?  448 MET   A N   1 
ATOM   2188 C CA  . MET   A 1 326 ? 33.374  2.758   50.029  1.00 120.16 ?  448 MET   A CA  1 
ATOM   2189 C C   . MET   A 1 326 ? 34.045  2.758   48.665  1.00 120.32 ?  448 MET   A C   1 
ATOM   2190 O O   . MET   A 1 326 ? 34.255  1.691   48.083  1.00 126.00 ?  448 MET   A O   1 
ATOM   2191 C CB  . MET   A 1 326 ? 31.901  3.115   49.895  1.00 121.18 ?  448 MET   A CB  1 
ATOM   2192 C CG  . MET   A 1 326 ? 31.014  2.353   50.861  1.00 120.67 ?  448 MET   A CG  1 
ATOM   2193 S SD  . MET   A 1 326 ? 29.268  2.682   50.523  1.00 134.56 ?  448 MET   A SD  1 
ATOM   2194 C CE  . MET   A 1 326 ? 29.147  2.485   48.751  1.00 130.46 ?  448 MET   A CE  1 
ATOM   2195 N N   . VAL   A 1 327 ? 34.395  3.927   48.131  1.00 118.98 ?  449 VAL   A N   1 
ATOM   2196 C CA  . VAL   A 1 327 ? 34.961  3.919   46.786  1.00 118.54 ?  449 VAL   A CA  1 
ATOM   2197 C C   . VAL   A 1 327 ? 36.317  3.207   46.783  1.00 123.34 ?  449 VAL   A C   1 
ATOM   2198 O O   . VAL   A 1 327 ? 36.673  2.554   45.797  1.00 127.42 ?  449 VAL   A O   1 
ATOM   2199 C CB  . VAL   A 1 327 ? 35.056  5.347   46.210  1.00 110.94 ?  449 VAL   A CB  1 
ATOM   2200 C CG1 . VAL   A 1 327 ? 36.264  6.088   46.765  1.00 112.62 ?  449 VAL   A CG1 1 
ATOM   2201 C CG2 . VAL   A 1 327 ? 35.023  5.338   44.698  1.00 113.24 ?  449 VAL   A CG2 1 
ATOM   2202 N N   . ASN   A 1 328 ? 37.080  3.273   47.881  1.00 123.43 ?  450 ASN   A N   1 
ATOM   2203 C CA  . ASN   A 1 328 ? 38.358  2.564   47.912  1.00 122.72 ?  450 ASN   A CA  1 
ATOM   2204 C C   . ASN   A 1 328 ? 38.206  1.099   48.294  1.00 122.25 ?  450 ASN   A C   1 
ATOM   2205 O O   . ASN   A 1 328 ? 39.209  0.394   48.435  1.00 121.62 ?  450 ASN   A O   1 
ATOM   2206 C CB  . ASN   A 1 328 ? 39.356  3.255   48.854  1.00 122.88 ?  450 ASN   A CB  1 
ATOM   2207 C CG  . ASN   A 1 328 ? 39.961  4.527   48.247  1.00 127.68 ?  450 ASN   A CG  1 
ATOM   2208 O OD1 . ASN   A 1 328 ? 39.576  4.960   47.156  1.00 128.21 ?  450 ASN   A OD1 1 
ATOM   2209 N ND2 . ASN   A 1 328 ? 40.956  5.092   48.926  1.00 130.64 ?  450 ASN   A ND2 1 
ATOM   2210 N N   . LEU   A 1 329 ? 36.981  0.626   48.471  1.00 123.22 ?  451 LEU   A N   1 
ATOM   2211 C CA  . LEU   A 1 329 ? 36.724  -0.799  48.537  1.00 119.68 ?  451 LEU   A CA  1 
ATOM   2212 C C   . LEU   A 1 329 ? 36.252  -1.327  47.191  1.00 119.92 ?  451 LEU   A C   1 
ATOM   2213 O O   . LEU   A 1 329 ? 36.690  -2.396  46.753  1.00 122.06 ?  451 LEU   A O   1 
ATOM   2214 C CB  . LEU   A 1 329 ? 35.682  -1.093  49.615  1.00 114.69 ?  451 LEU   A CB  1 
ATOM   2215 C CG  . LEU   A 1 329 ? 36.034  -2.321  50.436  1.00 117.13 ?  451 LEU   A CG  1 
ATOM   2216 C CD1 . LEU   A 1 329 ? 37.440  -2.114  51.015  1.00 119.23 ?  451 LEU   A CD1 1 
ATOM   2217 C CD2 . LEU   A 1 329 ? 35.013  -2.540  51.528  1.00 116.40 ?  451 LEU   A CD2 1 
ATOM   2218 N N   . LYS   A 1 330 ? 35.383  -0.576  46.504  1.00 118.22 ?  452 LYS   A N   1 
ATOM   2219 C CA  . LYS   A 1 330 ? 35.116  -0.839  45.096  1.00 114.05 ?  452 LYS   A CA  1 
ATOM   2220 C C   . LYS   A 1 330 ? 36.385  -0.787  44.254  1.00 118.36 ?  452 LYS   A C   1 
ATOM   2221 O O   . LYS   A 1 330 ? 36.379  -1.269  43.123  1.00 118.69 ?  452 LYS   A O   1 
ATOM   2222 C CB  . LYS   A 1 330 ? 34.107  0.165   44.537  1.00 109.42 ?  452 LYS   A CB  1 
ATOM   2223 C CG  . LYS   A 1 330 ? 33.135  -0.389  43.520  1.00 104.19 ?  452 LYS   A CG  1 
ATOM   2224 C CD  . LYS   A 1 330 ? 32.945  0.595   42.367  1.00 115.00 ?  452 LYS   A CD  1 
ATOM   2225 C CE  . LYS   A 1 330 ? 31.985  0.052   41.322  1.00 123.71 ?  452 LYS   A CE  1 
ATOM   2226 N NZ  . LYS   A 1 330 ? 32.090  0.739   40.002  1.00 132.81 ?  452 LYS   A NZ  1 
ATOM   2227 N N   . GLU   A 1 331 ? 37.471  -0.195  44.750  1.00 119.59 ?  453 GLU   A N   1 
ATOM   2228 C CA  . GLU   A 1 331 ? 38.690  -0.307  43.961  1.00 118.03 ?  453 GLU   A CA  1 
ATOM   2229 C C   . GLU   A 1 331 ? 39.436  -1.587  44.265  1.00 119.77 ?  453 GLU   A C   1 
ATOM   2230 O O   . GLU   A 1 331 ? 39.908  -2.246  43.337  1.00 118.58 ?  453 GLU   A O   1 
ATOM   2231 C CB  . GLU   A 1 331 ? 39.610  0.893   44.171  1.00 115.63 ?  453 GLU   A CB  1 
ATOM   2232 C CG  . GLU   A 1 331 ? 39.260  2.059   43.263  1.00 127.22 ?  453 GLU   A CG  1 
ATOM   2233 C CD  . GLU   A 1 331 ? 38.855  1.624   41.843  1.00 136.47 ?  453 GLU   A CD  1 
ATOM   2234 O OE1 . GLU   A 1 331 ? 39.748  1.492   40.971  1.00 137.93 ?  453 GLU   A OE1 1 
ATOM   2235 O OE2 . GLU   A 1 331 ? 37.635  1.430   41.594  1.00 134.44 ?  453 GLU   A OE2 1 
ATOM   2236 N N   . LYS   A 1 332 ? 39.547  -1.952  45.547  1.00 122.34 ?  454 LYS   A N   1 
ATOM   2237 C CA  . LYS   A 1 332 ? 40.125  -3.245  45.902  1.00 118.21 ?  454 LYS   A CA  1 
ATOM   2238 C C   . LYS   A 1 332 ? 39.300  -4.384  45.316  1.00 117.39 ?  454 LYS   A C   1 
ATOM   2239 O O   . LYS   A 1 332 ? 39.851  -5.404  44.892  1.00 119.14 ?  454 LYS   A O   1 
ATOM   2240 C CB  . LYS   A 1 332 ? 40.209  -3.401  47.420  1.00 120.68 ?  454 LYS   A CB  1 
ATOM   2241 C CG  . LYS   A 1 332 ? 41.468  -2.878  48.114  1.00 128.10 ?  454 LYS   A CG  1 
ATOM   2242 C CD  . LYS   A 1 332 ? 41.190  -2.744  49.643  1.00 139.30 ?  454 LYS   A CD  1 
ATOM   2243 C CE  . LYS   A 1 332 ? 41.905  -1.566  50.333  1.00 135.48 ?  454 LYS   A CE  1 
ATOM   2244 N NZ  . LYS   A 1 332 ? 40.966  -0.811  51.225  1.00 129.70 ?  454 LYS   A NZ  1 
ATOM   2245 N N   . ILE   A 1 333 ? 37.978  -4.231  45.274  1.00 115.49 ?  455 ILE   A N   1 
ATOM   2246 C CA  . ILE   A 1 333 ? 37.154  -5.328  44.785  1.00 115.38 ?  455 ILE   A CA  1 
ATOM   2247 C C   . ILE   A 1 333 ? 37.222  -5.435  43.264  1.00 115.64 ?  455 ILE   A C   1 
ATOM   2248 O O   . ILE   A 1 333 ? 37.319  -6.537  42.715  1.00 113.60 ?  455 ILE   A O   1 
ATOM   2249 C CB  . ILE   A 1 333 ? 35.713  -5.180  45.302  1.00 117.79 ?  455 ILE   A CB  1 
ATOM   2250 C CG1 . ILE   A 1 333 ? 35.629  -5.752  46.726  1.00 115.09 ?  455 ILE   A CG1 1 
ATOM   2251 C CG2 . ILE   A 1 333 ? 34.737  -5.889  44.368  1.00 119.09 ?  455 ILE   A CG2 1 
ATOM   2252 C CD1 . ILE   A 1 333 ? 34.425  -5.332  47.505  1.00 114.75 ?  455 ILE   A CD1 1 
ATOM   2253 N N   . LYS   A 1 334 ? 37.206  -4.298  42.566  1.00 120.44 ?  456 LYS   A N   1 
ATOM   2254 C CA  . LYS   A 1 334 ? 37.381  -4.275  41.113  1.00 119.45 ?  456 LYS   A CA  1 
ATOM   2255 C C   . LYS   A 1 334 ? 38.624  -5.040  40.675  1.00 119.14 ?  456 LYS   A C   1 
ATOM   2256 O O   . LYS   A 1 334 ? 38.643  -5.647  39.602  1.00 116.91 ?  456 LYS   A O   1 
ATOM   2257 C CB  . LYS   A 1 334 ? 37.423  -2.810  40.663  1.00 120.66 ?  456 LYS   A CB  1 
ATOM   2258 C CG  . LYS   A 1 334 ? 37.029  -2.455  39.231  1.00 125.16 ?  456 LYS   A CG  1 
ATOM   2259 C CD  . LYS   A 1 334 ? 37.814  -1.211  38.793  1.00 139.78 ?  456 LYS   A CD  1 
ATOM   2260 C CE  . LYS   A 1 334 ? 37.479  -0.702  37.388  1.00 144.47 ?  456 LYS   A CE  1 
ATOM   2261 N NZ  . LYS   A 1 334 ? 38.489  0.322   36.942  1.00 149.28 ?  456 LYS   A NZ  1 
ATOM   2262 N N   . GLU   A 1 335 ? 39.638  -5.078  41.526  1.00 121.26 ?  457 GLU   A N   1 
ATOM   2263 C CA  . GLU   A 1 335 ? 40.954  -5.616  41.239  1.00 116.36 ?  457 GLU   A CA  1 
ATOM   2264 C C   . GLU   A 1 335 ? 41.130  -7.048  41.724  1.00 118.16 ?  457 GLU   A C   1 
ATOM   2265 O O   . GLU   A 1 335 ? 41.749  -7.853  41.025  1.00 122.21 ?  457 GLU   A O   1 
ATOM   2266 C CB  . GLU   A 1 335 ? 41.985  -4.705  41.890  1.00 117.58 ?  457 GLU   A CB  1 
ATOM   2267 C CG  . GLU   A 1 335 ? 43.406  -4.852  41.489  1.00 122.07 ?  457 GLU   A CG  1 
ATOM   2268 C CD  . GLU   A 1 335 ? 44.291  -4.643  42.704  1.00 128.73 ?  457 GLU   A CD  1 
ATOM   2269 O OE1 . GLU   A 1 335 ? 43.759  -4.178  43.733  1.00 126.82 ?  457 GLU   A OE1 1 
ATOM   2270 O OE2 . GLU   A 1 335 ? 45.507  -4.909  42.644  1.00 137.90 ?  457 GLU   A OE2 1 
ATOM   2271 N N   . LEU   A 1 336 ? 40.618  -7.393  42.910  1.00 113.68 ?  458 LEU   A N   1 
ATOM   2272 C CA  . LEU   A 1 336 ? 40.605  -8.796  43.301  1.00 108.52 ?  458 LEU   A CA  1 
ATOM   2273 C C   . LEU   A 1 336 ? 39.853  -9.637  42.293  1.00 114.24 ?  458 LEU   A C   1 
ATOM   2274 O O   . LEU   A 1 336 ? 40.298  -10.729 41.932  1.00 120.31 ?  458 LEU   A O   1 
ATOM   2275 C CB  . LEU   A 1 336 ? 39.963  -8.989  44.659  1.00 103.25 ?  458 LEU   A CB  1 
ATOM   2276 C CG  . LEU   A 1 336 ? 40.900  -9.254  45.807  1.00 106.90 ?  458 LEU   A CG  1 
ATOM   2277 C CD1 . LEU   A 1 336 ? 40.073  -9.892  46.896  1.00 106.84 ?  458 LEU   A CD1 1 
ATOM   2278 C CD2 . LEU   A 1 336 ? 42.045  -10.140 45.360  1.00 107.59 ?  458 LEU   A CD2 1 
ATOM   2279 N N   . HIS   A 1 337 ? 38.690  -9.163  41.857  1.00 114.75 ?  459 HIS   A N   1 
ATOM   2280 C CA  . HIS   A 1 337 ? 37.900  -9.918  40.895  1.00 112.34 ?  459 HIS   A CA  1 
ATOM   2281 C C   . HIS   A 1 337 ? 38.708  -10.226 39.644  1.00 114.52 ?  459 HIS   A C   1 
ATOM   2282 O O   . HIS   A 1 337 ? 38.704  -11.360 39.157  1.00 113.97 ?  459 HIS   A O   1 
ATOM   2283 C CB  . HIS   A 1 337 ? 36.650  -9.128  40.552  1.00 117.39 ?  459 HIS   A CB  1 
ATOM   2284 C CG  . HIS   A 1 337 ? 35.728  -9.836  39.625  1.00 115.76 ?  459 HIS   A CG  1 
ATOM   2285 N ND1 . HIS   A 1 337 ? 34.849  -10.806 40.055  1.00 116.81 ?  459 HIS   A ND1 1 
ATOM   2286 C CD2 . HIS   A 1 337 ? 35.535  -9.707  38.292  1.00 114.32 ?  459 HIS   A CD2 1 
ATOM   2287 C CE1 . HIS   A 1 337 ? 34.157  -11.252 39.022  1.00 120.55 ?  459 HIS   A CE1 1 
ATOM   2288 N NE2 . HIS   A 1 337 ? 34.552  -10.601 37.941  1.00 120.20 ?  459 HIS   A NE2 1 
ATOM   2289 N N   . GLN   A 1 338 ? 39.427  -9.229  39.126  1.00 118.05 ?  460 GLN   A N   1 
ATOM   2290 C CA  . GLN   A 1 338 ? 40.349  -9.456  38.014  1.00 117.42 ?  460 GLN   A CA  1 
ATOM   2291 C C   . GLN   A 1 338 ? 41.386  -10.521 38.358  1.00 115.75 ?  460 GLN   A C   1 
ATOM   2292 O O   . GLN   A 1 338 ? 41.630  -11.438 37.568  1.00 120.21 ?  460 GLN   A O   1 
ATOM   2293 C CB  . GLN   A 1 338 ? 41.021  -8.135  37.630  1.00 120.77 ?  460 GLN   A CB  1 
ATOM   2294 C CG  . GLN   A 1 338 ? 41.932  -8.155  36.396  1.00 122.46 ?  460 GLN   A CG  1 
ATOM   2295 C CD  . GLN   A 1 338 ? 41.429  -9.052  35.277  1.00 122.30 ?  460 GLN   A CD  1 
ATOM   2296 O OE1 . GLN   A 1 338 ? 40.344  -8.841  34.726  1.00 121.33 ?  460 GLN   A OE1 1 
ATOM   2297 N NE2 . GLN   A 1 338 ? 42.253  -10.024 34.891  1.00 119.33 ?  460 GLN   A NE2 1 
ATOM   2298 N N   . GLN   A 1 339 ? 42.009  -10.420 39.534  1.00 113.45 ?  461 GLN   A N   1 
ATOM   2299 C CA  . GLN   A 1 339 ? 42.959  -11.446 39.964  1.00 115.23 ?  461 GLN   A CA  1 
ATOM   2300 C C   . GLN   A 1 339 ? 42.310  -12.822 40.031  1.00 112.20 ?  461 GLN   A C   1 
ATOM   2301 O O   . GLN   A 1 339 ? 42.859  -13.807 39.527  1.00 109.24 ?  461 GLN   A O   1 
ATOM   2302 C CB  . GLN   A 1 339 ? 43.527  -11.095 41.330  1.00 118.32 ?  461 GLN   A CB  1 
ATOM   2303 C CG  . GLN   A 1 339 ? 44.749  -10.247 41.315  1.00 119.12 ?  461 GLN   A CG  1 
ATOM   2304 C CD  . GLN   A 1 339 ? 44.919  -9.526  42.623  1.00 122.35 ?  461 GLN   A CD  1 
ATOM   2305 O OE1 . GLN   A 1 339 ? 45.020  -10.143 43.693  1.00 121.72 ?  461 GLN   A OE1 1 
ATOM   2306 N NE2 . GLN   A 1 339 ? 44.948  -8.208  42.553  1.00 128.42 ?  461 GLN   A NE2 1 
ATOM   2307 N N   . TYR   A 1 340 ? 41.163  -12.916 40.702  1.00 109.93 ?  462 TYR   A N   1 
ATOM   2308 C CA  . TYR   A 1 340 ? 40.489  -14.196 40.831  1.00 106.48 ?  462 TYR   A CA  1 
ATOM   2309 C C   . TYR   A 1 340 ? 40.101  -14.753 39.472  1.00 109.67 ?  462 TYR   A C   1 
ATOM   2310 O O   . TYR   A 1 340 ? 40.182  -15.964 39.251  1.00 114.59 ?  462 TYR   A O   1 
ATOM   2311 C CB  . TYR   A 1 340 ? 39.262  -14.057 41.723  1.00 110.07 ?  462 TYR   A CB  1 
ATOM   2312 C CG  . TYR   A 1 340 ? 38.305  -15.230 41.633  1.00 113.64 ?  462 TYR   A CG  1 
ATOM   2313 C CD1 . TYR   A 1 340 ? 37.307  -15.272 40.649  1.00 111.96 ?  462 TYR   A CD1 1 
ATOM   2314 C CD2 . TYR   A 1 340 ? 38.389  -16.293 42.537  1.00 108.32 ?  462 TYR   A CD2 1 
ATOM   2315 C CE1 . TYR   A 1 340 ? 36.435  -16.335 40.564  1.00 109.82 ?  462 TYR   A CE1 1 
ATOM   2316 C CE2 . TYR   A 1 340 ? 37.515  -17.362 42.457  1.00 108.82 ?  462 TYR   A CE2 1 
ATOM   2317 C CZ  . TYR   A 1 340 ? 36.542  -17.377 41.468  1.00 110.15 ?  462 TYR   A CZ  1 
ATOM   2318 O OH  . TYR   A 1 340 ? 35.670  -18.433 41.381  1.00 104.68 ?  462 TYR   A OH  1 
ATOM   2319 N N   . LYS   A 1 341 ? 39.648  -13.903 38.553  1.00 110.61 ?  463 LYS   A N   1 
ATOM   2320 C CA  . LYS   A 1 341 ? 39.398  -14.390 37.199  1.00 115.93 ?  463 LYS   A CA  1 
ATOM   2321 C C   . LYS   A 1 341 ? 40.665  -15.002 36.599  1.00 116.56 ?  463 LYS   A C   1 
ATOM   2322 O O   . LYS   A 1 341 ? 40.658  -16.165 36.175  1.00 113.49 ?  463 LYS   A O   1 
ATOM   2323 C CB  . LYS   A 1 341 ? 38.846  -13.264 36.316  1.00 116.23 ?  463 LYS   A CB  1 
ATOM   2324 C CG  . LYS   A 1 341 ? 37.613  -13.674 35.491  1.00 118.90 ?  463 LYS   A CG  1 
ATOM   2325 C CD  . LYS   A 1 341 ? 36.439  -14.132 36.395  1.00 118.63 ?  463 LYS   A CD  1 
ATOM   2326 C CE  . LYS   A 1 341 ? 35.137  -14.320 35.600  1.00 119.81 ?  463 LYS   A CE  1 
ATOM   2327 N NZ  . LYS   A 1 341 ? 34.018  -14.871 36.416  1.00 113.41 ?  463 LYS   A NZ  1 
ATOM   2328 N N   . GLU   A 1 342 ? 41.777  -14.246 36.603  1.00 115.50 ?  464 GLU   A N   1 
ATOM   2329 C CA  . GLU   A 1 342 ? 43.063  -14.751 36.114  1.00 114.08 ?  464 GLU   A CA  1 
ATOM   2330 C C   . GLU   A 1 342 ? 43.467  -16.071 36.763  1.00 114.83 ?  464 GLU   A C   1 
ATOM   2331 O O   . GLU   A 1 342 ? 44.206  -16.854 36.161  1.00 115.67 ?  464 GLU   A O   1 
ATOM   2332 C CB  . GLU   A 1 342 ? 44.190  -13.753 36.387  1.00 113.74 ?  464 GLU   A CB  1 
ATOM   2333 C CG  . GLU   A 1 342 ? 44.654  -12.932 35.215  1.00 119.34 ?  464 GLU   A CG  1 
ATOM   2334 C CD  . GLU   A 1 342 ? 45.339  -11.653 35.678  1.00 122.24 ?  464 GLU   A CD  1 
ATOM   2335 O OE1 . GLU   A 1 342 ? 45.963  -11.721 36.770  1.00 120.61 ?  464 GLU   A OE1 1 
ATOM   2336 O OE2 . GLU   A 1 342 ? 45.231  -10.601 34.985  1.00 113.89 ?  464 GLU   A OE2 1 
ATOM   2337 N N   . ALA   A 1 343 ? 43.063  -16.307 38.009  1.00 112.46 ?  465 ALA   A N   1 
ATOM   2338 C CA  . ALA   A 1 343 ? 43.485  -17.519 38.692  1.00 106.53 ?  465 ALA   A CA  1 
ATOM   2339 C C   . ALA   A 1 343 ? 42.635  -18.712 38.320  1.00 104.62 ?  465 ALA   A C   1 
ATOM   2340 O O   . ALA   A 1 343 ? 43.043  -19.843 38.591  1.00 102.00 ?  465 ALA   A O   1 
ATOM   2341 C CB  . ALA   A 1 343 ? 43.442  -17.324 40.206  1.00 106.49 ?  465 ALA   A CB  1 
ATOM   2342 N N   . SER   A 1 344 ? 41.465  -18.477 37.728  1.00 108.13 ?  466 SER   A N   1 
ATOM   2343 C CA  . SER   A 1 344 ? 40.600  -19.540 37.235  1.00 112.59 ?  466 SER   A CA  1 
ATOM   2344 C C   . SER   A 1 344 ? 40.804  -19.826 35.758  1.00 119.01 ?  466 SER   A C   1 
ATOM   2345 O O   . SER   A 1 344 ? 40.371  -20.883 35.277  1.00 122.99 ?  466 SER   A O   1 
ATOM   2346 C CB  . SER   A 1 344 ? 39.133  -19.182 37.469  1.00 115.34 ?  466 SER   A CB  1 
ATOM   2347 O OG  . SER   A 1 344 ? 38.867  -19.092 38.853  1.00 117.60 ?  466 SER   A OG  1 
ATOM   2348 N N   . GLU   A 1 345 ? 41.438  -18.902 35.028  1.00 119.45 ?  467 GLU   A N   1 
ATOM   2349 C CA  . GLU   A 1 345 ? 41.824  -19.184 33.649  1.00 120.82 ?  467 GLU   A CA  1 
ATOM   2350 C C   . GLU   A 1 345 ? 42.820  -20.340 33.597  1.00 117.99 ?  467 GLU   A C   1 
ATOM   2351 O O   . GLU   A 1 345 ? 42.848  -21.081 32.605  1.00 127.22 ?  467 GLU   A O   1 
ATOM   2352 C CB  . GLU   A 1 345 ? 42.441  -17.938 32.976  1.00 128.05 ?  467 GLU   A CB  1 
ATOM   2353 C CG  . GLU   A 1 345 ? 41.770  -16.540 33.222  1.00 126.99 ?  467 GLU   A CG  1 
ATOM   2354 C CD  . GLU   A 1 345 ? 40.374  -16.348 32.612  1.00 128.43 ?  467 GLU   A CD  1 
ATOM   2355 O OE1 . GLU   A 1 345 ? 40.305  -16.033 31.404  1.00 134.37 ?  467 GLU   A OE1 1 
ATOM   2356 O OE2 . GLU   A 1 345 ? 39.355  -16.444 33.346  1.00 121.17 ?  467 GLU   A OE2 1 
ATOM   2357 N N   . VAL   A 1 346 ? 43.655  -20.498 34.637  1.00 103.58 ?  468 VAL   A N   1 
ATOM   2358 C CA  . VAL   A 1 346 ? 44.582  -21.620 34.708  1.00 98.91  ?  468 VAL   A CA  1 
ATOM   2359 C C   . VAL   A 1 346 ? 43.574  -22.731 34.512  1.00 109.30 ?  468 VAL   A C   1 
ATOM   2360 O O   . VAL   A 1 346 ? 42.561  -22.810 35.213  1.00 105.51 ?  468 VAL   A O   1 
ATOM   2361 C CB  . VAL   A 1 346 ? 45.473  -21.592 35.955  1.00 94.69  ?  468 VAL   A CB  1 
ATOM   2362 C CG1 . VAL   A 1 346 ? 46.483  -22.684 35.894  1.00 95.03  ?  468 VAL   A CG1 1 
ATOM   2363 C CG2 . VAL   A 1 346 ? 46.201  -20.329 35.990  1.00 110.33 ?  468 VAL   A CG2 1 
ATOM   2364 N N   . LYS   A 1 347 ? 43.844  -23.571 33.532  1.00 121.37 ?  469 LYS   A N   1 
ATOM   2365 C CA  . LYS   A 1 347 ? 43.019  -24.732 33.273  1.00 116.58 ?  469 LYS   A CA  1 
ATOM   2366 C C   . LYS   A 1 347 ? 43.523  -25.916 34.086  1.00 110.13 ?  469 LYS   A C   1 
ATOM   2367 O O   . LYS   A 1 347 ? 44.728  -26.214 34.068  1.00 108.88 ?  469 LYS   A O   1 
ATOM   2368 C CB  . LYS   A 1 347 ? 43.006  -25.048 31.779  1.00 123.53 ?  469 LYS   A CB  1 
ATOM   2369 C CG  . LYS   A 1 347 ? 42.056  -24.115 31.033  1.00 129.68 ?  469 LYS   A CG  1 
ATOM   2370 C CD  . LYS   A 1 347 ? 40.609  -24.555 31.288  1.00 136.29 ?  469 LYS   A CD  1 
ATOM   2371 C CE  . LYS   A 1 347 ? 39.644  -23.368 31.372  1.00 138.81 ?  469 LYS   A CE  1 
ATOM   2372 N NZ  . LYS   A 1 347 ? 39.520  -22.836 32.778  1.00 123.06 ?  469 LYS   A NZ  1 
ATOM   2373 N N   . PRO   A 1 348 ? 42.640  -26.589 34.810  1.00 105.33 ?  470 PRO   A N   1 
ATOM   2374 C CA  . PRO   A 1 348 ? 43.039  -27.691 35.648  1.00 102.70 ?  470 PRO   A CA  1 
ATOM   2375 C C   . PRO   A 1 348 ? 43.423  -28.871 34.780  1.00 108.96 ?  470 PRO   A C   1 
ATOM   2376 O O   . PRO   A 1 348 ? 43.075  -28.899 33.592  1.00 113.80 ?  470 PRO   A O   1 
ATOM   2377 C CB  . PRO   A 1 348 ? 41.765  -27.989 36.457  1.00 101.56 ?  470 PRO   A CB  1 
ATOM   2378 C CG  . PRO   A 1 348 ? 40.817  -26.904 36.140  1.00 103.12 ?  470 PRO   A CG  1 
ATOM   2379 C CD  . PRO   A 1 348 ? 41.183  -26.446 34.777  1.00 108.88 ?  470 PRO   A CD  1 
ATOM   2380 N N   . PRO   A 1 349 ? 44.096  -29.889 35.333  1.00 111.30 ?  471 PRO   A N   1 
ATOM   2381 C CA  . PRO   A 1 349 ? 44.370  -30.017 36.767  1.00 111.46 ?  471 PRO   A CA  1 
ATOM   2382 C C   . PRO   A 1 349 ? 45.583  -29.167 37.123  1.00 109.76 ?  471 PRO   A C   1 
ATOM   2383 O O   . PRO   A 1 349 ? 46.558  -29.123 36.352  1.00 111.03 ?  471 PRO   A O   1 
ATOM   2384 C CB  . PRO   A 1 349 ? 44.609  -31.524 36.945  1.00 109.96 ?  471 PRO   A CB  1 
ATOM   2385 C CG  . PRO   A 1 349 ? 45.078  -32.021 35.540  1.00 108.28 ?  471 PRO   A CG  1 
ATOM   2386 C CD  . PRO   A 1 349 ? 44.817  -30.902 34.534  1.00 106.37 ?  471 PRO   A CD  1 
ATOM   2387 N N   . ARG   A 1 350 ? 45.498  -28.436 38.228  1.00 103.47 ?  472 ARG   A N   1 
ATOM   2388 C CA  . ARG   A 1 350 ? 46.590  -27.572 38.641  1.00 103.69 ?  472 ARG   A CA  1 
ATOM   2389 C C   . ARG   A 1 350 ? 47.210  -28.145 39.897  1.00 102.02 ?  472 ARG   A C   1 
ATOM   2390 O O   . ARG   A 1 350 ? 46.636  -29.026 40.540  1.00 105.99 ?  472 ARG   A O   1 
ATOM   2391 C CB  . ARG   A 1 350 ? 46.115  -26.134 38.865  1.00 100.28 ?  472 ARG   A CB  1 
ATOM   2392 C CG  . ARG   A 1 350 ? 44.697  -26.046 39.371  1.00 102.20 ?  472 ARG   A CG  1 
ATOM   2393 C CD  . ARG   A 1 350 ? 43.959  -24.836 38.811  1.00 96.84  ?  472 ARG   A CD  1 
ATOM   2394 N NE  . ARG   A 1 350 ? 42.631  -24.734 39.404  1.00 98.02  ?  472 ARG   A NE  1 
ATOM   2395 C CZ  . ARG   A 1 350 ? 41.636  -24.012 38.909  1.00 102.10 ?  472 ARG   A CZ  1 
ATOM   2396 N NH1 . ARG   A 1 350 ? 41.791  -23.282 37.818  1.00 105.58 ?  472 ARG   A NH1 1 
ATOM   2397 N NH2 . ARG   A 1 350 ? 40.454  -24.025 39.523  1.00 100.87 ?  472 ARG   A NH2 1 
ATOM   2398 N N   . ASP   A 1 351 ? 48.414  -27.686 40.218  1.00 100.28 ?  473 ASP   A N   1 
ATOM   2399 C CA  . ASP   A 1 351 ? 48.988  -28.149 41.464  1.00 100.60 ?  473 ASP   A CA  1 
ATOM   2400 C C   . ASP   A 1 351 ? 48.290  -27.442 42.613  1.00 107.58 ?  473 ASP   A C   1 
ATOM   2401 O O   . ASP   A 1 351 ? 47.393  -26.619 42.411  1.00 111.19 ?  473 ASP   A O   1 
ATOM   2402 C CB  . ASP   A 1 351 ? 50.506  -27.966 41.495  1.00 99.48  ?  473 ASP   A CB  1 
ATOM   2403 C CG  . ASP   A 1 351 ? 50.945  -26.529 41.405  1.00 105.69 ?  473 ASP   A CG  1 
ATOM   2404 O OD1 . ASP   A 1 351 ? 50.106  -25.616 41.547  1.00 109.96 ?  473 ASP   A OD1 1 
ATOM   2405 O OD2 . ASP   A 1 351 ? 52.174  -26.316 41.270  1.00 109.15 ?  473 ASP   A OD2 1 
ATOM   2406 N N   . ILE   A 1 352 ? 48.699  -27.754 43.842  1.00 106.03 ?  474 ILE   A N   1 
ATOM   2407 C CA  . ILE   A 1 352 ? 47.905  -27.243 44.947  1.00 104.17 ?  474 ILE   A CA  1 
ATOM   2408 C C   . ILE   A 1 352 ? 48.126  -25.751 45.162  1.00 102.42 ?  474 ILE   A C   1 
ATOM   2409 O O   . ILE   A 1 352 ? 47.195  -25.047 45.563  1.00 102.28 ?  474 ILE   A O   1 
ATOM   2410 C CB  . ILE   A 1 352 ? 48.152  -28.041 46.230  1.00 101.58 ?  474 ILE   A CB  1 
ATOM   2411 C CG1 . ILE   A 1 352 ? 46.915  -27.894 47.109  1.00 105.09 ?  474 ILE   A CG1 1 
ATOM   2412 C CG2 . ILE   A 1 352 ? 49.422  -27.572 46.927  1.00 98.54  ?  474 ILE   A CG2 1 
ATOM   2413 C CD1 . ILE   A 1 352 ? 45.629  -28.204 46.349  1.00 107.93 ?  474 ILE   A CD1 1 
ATOM   2414 N N   . THR   A 1 353 ? 49.327  -25.229 44.893  1.00 102.20 ?  475 THR   A N   1 
ATOM   2415 C CA  . THR   A 1 353 ? 49.545  -23.803 45.132  1.00 103.65 ?  475 THR   A CA  1 
ATOM   2416 C C   . THR   A 1 353 ? 48.623  -22.961 44.256  1.00 104.92 ?  475 THR   A C   1 
ATOM   2417 O O   . THR   A 1 353 ? 47.984  -22.013 44.738  1.00 103.35 ?  475 THR   A O   1 
ATOM   2418 C CB  . THR   A 1 353 ? 51.015  -23.408 44.912  1.00 99.41  ?  475 THR   A CB  1 
ATOM   2419 O OG1 . THR   A 1 353 ? 51.363  -23.549 43.528  1.00 102.13 ?  475 THR   A OG1 1 
ATOM   2420 C CG2 . THR   A 1 353 ? 51.959  -24.208 45.792  1.00 93.51  ?  475 THR   A CG2 1 
ATOM   2421 N N   . ALA   A 1 354 ? 48.524  -23.306 42.967  1.00 99.76  ?  476 ALA   A N   1 
ATOM   2422 C CA  . ALA   A 1 354 ? 47.634  -22.573 42.076  1.00 103.41 ?  476 ALA   A CA  1 
ATOM   2423 C C   . ALA   A 1 354 ? 46.166  -22.931 42.285  1.00 103.30 ?  476 ALA   A C   1 
ATOM   2424 O O   . ALA   A 1 354 ? 45.290  -22.298 41.681  1.00 102.33 ?  476 ALA   A O   1 
ATOM   2425 C CB  . ALA   A 1 354 ? 48.039  -22.797 40.618  1.00 107.52 ?  476 ALA   A CB  1 
ATOM   2426 N N   . GLU   A 1 355 ? 45.873  -23.916 43.132  1.00 104.06 ?  477 GLU   A N   1 
ATOM   2427 C CA  . GLU   A 1 355 ? 44.501  -24.180 43.549  1.00 105.09 ?  477 GLU   A CA  1 
ATOM   2428 C C   . GLU   A 1 355 ? 44.168  -23.404 44.820  1.00 106.30 ?  477 GLU   A C   1 
ATOM   2429 O O   . GLU   A 1 355 ? 43.060  -22.871 44.964  1.00 102.49 ?  477 GLU   A O   1 
ATOM   2430 C CB  . GLU   A 1 355 ? 44.310  -25.689 43.747  1.00 98.92  ?  477 GLU   A CB  1 
ATOM   2431 C CG  . GLU   A 1 355 ? 42.923  -26.135 44.143  1.00 101.80 ?  477 GLU   A CG  1 
ATOM   2432 C CD  . GLU   A 1 355 ? 41.953  -26.118 42.965  1.00 107.52 ?  477 GLU   A CD  1 
ATOM   2433 O OE1 . GLU   A 1 355 ? 42.384  -26.321 41.811  1.00 102.55 ?  477 GLU   A OE1 1 
ATOM   2434 O OE2 . GLU   A 1 355 ? 40.742  -25.935 43.198  1.00 114.93 ?  477 GLU   A OE2 1 
ATOM   2435 N N   . PHE   A 1 356 ? 45.140  -23.321 45.736  1.00 108.22 ?  478 PHE   A N   1 
ATOM   2436 C CA  . PHE   A 1 356 ? 45.024  -22.454 46.898  1.00 103.85 ?  478 PHE   A CA  1 
ATOM   2437 C C   . PHE   A 1 356 ? 44.909  -21.008 46.482  1.00 103.95 ?  478 PHE   A C   1 
ATOM   2438 O O   . PHE   A 1 356 ? 44.413  -20.193 47.260  1.00 107.33 ?  478 PHE   A O   1 
ATOM   2439 C CB  . PHE   A 1 356 ? 46.228  -22.658 47.833  1.00 106.60 ?  478 PHE   A CB  1 
ATOM   2440 C CG  . PHE   A 1 356 ? 46.395  -21.582 48.881  1.00 109.31 ?  478 PHE   A CG  1 
ATOM   2441 C CD1 . PHE   A 1 356 ? 45.524  -21.496 49.953  1.00 115.16 ?  478 PHE   A CD1 1 
ATOM   2442 C CD2 . PHE   A 1 356 ? 47.448  -20.692 48.822  1.00 110.19 ?  478 PHE   A CD2 1 
ATOM   2443 C CE1 . PHE   A 1 356 ? 45.677  -20.518 50.920  1.00 116.39 ?  478 PHE   A CE1 1 
ATOM   2444 C CE2 . PHE   A 1 356 ? 47.611  -19.723 49.794  1.00 111.32 ?  478 PHE   A CE2 1 
ATOM   2445 C CZ  . PHE   A 1 356 ? 46.723  -19.635 50.839  1.00 113.77 ?  478 PHE   A CZ  1 
ATOM   2446 N N   . LEU   A 1 357 ? 45.339  -20.680 45.265  1.00 103.14 ?  479 LEU   A N   1 
ATOM   2447 C CA  . LEU   A 1 357 ? 45.204  -19.312 44.780  1.00 105.51 ?  479 LEU   A CA  1 
ATOM   2448 C C   . LEU   A 1 357 ? 43.752  -18.967 44.490  1.00 105.18 ?  479 LEU   A C   1 
ATOM   2449 O O   . LEU   A 1 357 ? 43.276  -17.889 44.859  1.00 107.11 ?  479 LEU   A O   1 
ATOM   2450 C CB  . LEU   A 1 357 ? 46.032  -19.102 43.525  1.00 98.51  ?  479 LEU   A CB  1 
ATOM   2451 C CG  . LEU   A 1 357 ? 46.273  -17.621 43.334  1.00 86.86  ?  479 LEU   A CG  1 
ATOM   2452 C CD1 . LEU   A 1 357 ? 47.283  -17.179 44.363  1.00 94.12  ?  479 LEU   A CD1 1 
ATOM   2453 C CD2 . LEU   A 1 357 ? 46.726  -17.325 41.950  1.00 89.38  ?  479 LEU   A CD2 1 
ATOM   2454 N N   . VAL   A 1 358 ? 43.042  -19.853 43.794  1.00 105.50 ?  480 VAL   A N   1 
ATOM   2455 C CA  . VAL   A 1 358 ? 41.621  -19.626 43.553  1.00 107.71 ?  480 VAL   A CA  1 
ATOM   2456 C C   . VAL   A 1 358 ? 40.872  -19.577 44.875  1.00 108.78 ?  480 VAL   A C   1 
ATOM   2457 O O   . VAL   A 1 358 ? 40.224  -18.579 45.212  1.00 111.79 ?  480 VAL   A O   1 
ATOM   2458 C CB  . VAL   A 1 358 ? 41.049  -20.708 42.621  1.00 104.63 ?  480 VAL   A CB  1 
ATOM   2459 C CG1 . VAL   A 1 358 ? 39.536  -20.577 42.517  1.00 102.66 ?  480 VAL   A CG1 1 
ATOM   2460 C CG2 . VAL   A 1 358 ? 41.664  -20.574 41.260  1.00 107.40 ?  480 VAL   A CG2 1 
ATOM   2461 N N   . LYS   A 1 359 ? 40.962  -20.657 45.650  1.00 111.18 ?  481 LYS   A N   1 
ATOM   2462 C CA  . LYS   A 1 359 ? 40.238  -20.717 46.914  1.00 117.82 ?  481 LYS   A CA  1 
ATOM   2463 C C   . LYS   A 1 359 ? 40.545  -19.493 47.783  1.00 114.94 ?  481 LYS   A C   1 
ATOM   2464 O O   . LYS   A 1 359 ? 39.638  -18.906 48.387  1.00 117.25 ?  481 LYS   A O   1 
ATOM   2465 C CB  . LYS   A 1 359 ? 40.568  -22.037 47.640  1.00 117.98 ?  481 LYS   A CB  1 
ATOM   2466 C CG  . LYS   A 1 359 ? 40.305  -23.334 46.835  1.00 106.36 ?  481 LYS   A CG  1 
ATOM   2467 C CD  . LYS   A 1 359 ? 38.823  -23.686 46.825  1.00 111.08 ?  481 LYS   A CD  1 
ATOM   2468 C CE  . LYS   A 1 359 ? 38.583  -25.167 46.605  1.00 118.03 ?  481 LYS   A CE  1 
ATOM   2469 N NZ  . LYS   A 1 359 ? 38.979  -25.990 47.785  1.00 113.96 ?  481 LYS   A NZ  1 
ATOM   2470 N N   . SER   A 1 360 ? 41.810  -19.065 47.815  1.00 111.16 ?  482 SER   A N   1 
ATOM   2471 C CA  . SER   A 1 360 ? 42.196  -17.864 48.542  1.00 110.71 ?  482 SER   A CA  1 
ATOM   2472 C C   . SER   A 1 360 ? 41.535  -16.613 47.960  1.00 113.86 ?  482 SER   A C   1 
ATOM   2473 O O   . SER   A 1 360 ? 40.701  -16.009 48.639  1.00 118.95 ?  482 SER   A O   1 
ATOM   2474 C CB  . SER   A 1 360 ? 43.715  -17.715 48.560  1.00 109.45 ?  482 SER   A CB  1 
ATOM   2475 O OG  . SER   A 1 360 ? 44.091  -16.397 48.901  1.00 120.28 ?  482 SER   A OG  1 
ATOM   2476 N N   . LYS   A 1 361 ? 41.869  -16.207 46.723  1.00 108.63 ?  483 LYS   A N   1 
ATOM   2477 C CA  . LYS   A 1 361 ? 41.235  -15.017 46.155  1.00 104.86 ?  483 LYS   A CA  1 
ATOM   2478 C C   . LYS   A 1 361 ? 39.711  -15.054 46.269  1.00 110.36 ?  483 LYS   A C   1 
ATOM   2479 O O   . LYS   A 1 361 ? 39.080  -13.995 46.263  1.00 113.56 ?  483 LYS   A O   1 
ATOM   2480 C CB  . LYS   A 1 361 ? 41.596  -14.801 44.673  1.00 100.20 ?  483 LYS   A CB  1 
ATOM   2481 C CG  . LYS   A 1 361 ? 43.048  -14.466 44.340  1.00 97.93  ?  483 LYS   A CG  1 
ATOM   2482 C CD  . LYS   A 1 361 ? 43.677  -13.440 45.262  1.00 113.80 ?  483 LYS   A CD  1 
ATOM   2483 C CE  . LYS   A 1 361 ? 45.164  -13.200 44.937  1.00 112.62 ?  483 LYS   A CE  1 
ATOM   2484 N NZ  . LYS   A 1 361 ? 45.920  -12.431 46.000  1.00 114.10 ?  483 LYS   A NZ  1 
ATOM   2485 N N   . HIS   A 1 362 ? 39.097  -16.236 46.383  1.00 112.47 ?  484 HIS   A N   1 
ATOM   2486 C CA  . HIS   A 1 362 ? 37.644  -16.297 46.537  1.00 113.49 ?  484 HIS   A CA  1 
ATOM   2487 C C   . HIS   A 1 362 ? 37.200  -15.856 47.924  1.00 118.33 ?  484 HIS   A C   1 
ATOM   2488 O O   . HIS   A 1 362 ? 36.229  -15.108 48.067  1.00 123.65 ?  484 HIS   A O   1 
ATOM   2489 C CB  . HIS   A 1 362 ? 37.132  -17.699 46.245  1.00 115.74 ?  484 HIS   A CB  1 
ATOM   2490 C CG  . HIS   A 1 362 ? 35.648  -17.838 46.394  1.00 121.51 ?  484 HIS   A CG  1 
ATOM   2491 N ND1 . HIS   A 1 362 ? 34.763  -17.519 45.384  1.00 119.77 ?  484 HIS   A ND1 1 
ATOM   2492 C CD2 . HIS   A 1 362 ? 34.896  -18.325 47.411  1.00 123.39 ?  484 HIS   A CD2 1 
ATOM   2493 C CE1 . HIS   A 1 362 ? 33.528  -17.761 45.786  1.00 122.29 ?  484 HIS   A CE1 1 
ATOM   2494 N NE2 . HIS   A 1 362 ? 33.582  -18.260 47.009  1.00 129.41 ?  484 HIS   A NE2 1 
ATOM   2495 N N   . ARG   A 1 363 ? 37.871  -16.329 48.965  1.00 119.35 ?  485 ARG   A N   1 
ATOM   2496 C CA  . ARG   A 1 363 ? 37.529  -15.860 50.302  1.00 118.91 ?  485 ARG   A CA  1 
ATOM   2497 C C   . ARG   A 1 363 ? 37.861  -14.387 50.471  1.00 117.24 ?  485 ARG   A C   1 
ATOM   2498 O O   . ARG   A 1 363 ? 37.085  -13.643 51.075  1.00 122.53 ?  485 ARG   A O   1 
ATOM   2499 C CB  . ARG   A 1 363 ? 38.262  -16.687 51.339  1.00 121.44 ?  485 ARG   A CB  1 
ATOM   2500 C CG  . ARG   A 1 363 ? 37.916  -16.348 52.737  1.00 123.47 ?  485 ARG   A CG  1 
ATOM   2501 C CD  . ARG   A 1 363 ? 39.223  -16.230 53.438  1.00 126.47 ?  485 ARG   A CD  1 
ATOM   2502 N NE  . ARG   A 1 363 ? 39.695  -14.856 53.479  1.00 124.78 ?  485 ARG   A NE  1 
ATOM   2503 C CZ  . ARG   A 1 363 ? 39.289  -13.983 54.387  1.00 127.88 ?  485 ARG   A CZ  1 
ATOM   2504 N NH1 . ARG   A 1 363 ? 38.454  -14.339 55.356  1.00 128.52 ?  485 ARG   A NH1 1 
ATOM   2505 N NH2 . ARG   A 1 363 ? 39.734  -12.729 54.330  1.00 123.78 ?  485 ARG   A NH2 1 
ATOM   2506 N N   . ASP   A 1 364 ? 39.012  -13.956 49.947  1.00 116.27 ?  486 ASP   A N   1 
ATOM   2507 C CA  . ASP   A 1 364 ? 39.390  -12.545 49.978  1.00 114.37 ?  486 ASP   A CA  1 
ATOM   2508 C C   . ASP   A 1 364 ? 38.348  -11.668 49.294  1.00 115.49 ?  486 ASP   A C   1 
ATOM   2509 O O   . ASP   A 1 364 ? 37.984  -10.614 49.818  1.00 120.68 ?  486 ASP   A O   1 
ATOM   2510 C CB  . ASP   A 1 364 ? 40.757  -12.362 49.319  1.00 113.85 ?  486 ASP   A CB  1 
ATOM   2511 C CG  . ASP   A 1 364 ? 41.865  -13.032 50.095  1.00 116.81 ?  486 ASP   A CG  1 
ATOM   2512 O OD1 . ASP   A 1 364 ? 41.520  -13.743 51.069  1.00 117.09 ?  486 ASP   A OD1 1 
ATOM   2513 O OD2 . ASP   A 1 364 ? 43.056  -12.892 49.708  1.00 112.55 ?  486 ASP   A OD2 1 
ATOM   2514 N N   . LEU   A 1 365 ? 37.865  -12.072 48.118  1.00 115.16 ?  487 LEU   A N   1 
ATOM   2515 C CA  . LEU   A 1 365 ? 36.818  -11.305 47.447  1.00 115.26 ?  487 LEU   A CA  1 
ATOM   2516 C C   . LEU   A 1 365 ? 35.443  -11.471 48.090  1.00 120.49 ?  487 LEU   A C   1 
ATOM   2517 O O   . LEU   A 1 365 ? 34.583  -10.606 47.899  1.00 121.74 ?  487 LEU   A O   1 
ATOM   2518 C CB  . LEU   A 1 365 ? 36.728  -11.677 45.964  1.00 112.11 ?  487 LEU   A CB  1 
ATOM   2519 C CG  . LEU   A 1 365 ? 35.867  -10.693 45.175  1.00 112.38 ?  487 LEU   A CG  1 
ATOM   2520 C CD1 . LEU   A 1 365 ? 36.625  -9.425  44.986  1.00 114.90 ?  487 LEU   A CD1 1 
ATOM   2521 C CD2 . LEU   A 1 365 ? 35.433  -11.237 43.839  1.00 117.11 ?  487 LEU   A CD2 1 
ATOM   2522 N N   . THR   A 1 366 ? 35.197  -12.553 48.837  1.00 122.44 ?  488 THR   A N   1 
ATOM   2523 C CA  . THR   A 1 366 ? 33.943  -12.623 49.580  1.00 120.86 ?  488 THR   A CA  1 
ATOM   2524 C C   . THR   A 1 366 ? 34.029  -11.807 50.861  1.00 126.52 ?  488 THR   A C   1 
ATOM   2525 O O   . THR   A 1 366 ? 33.020  -11.240 51.297  1.00 129.19 ?  488 THR   A O   1 
ATOM   2526 C CB  . THR   A 1 366 ? 33.576  -14.065 49.918  1.00 116.26 ?  488 THR   A CB  1 
ATOM   2527 O OG1 . THR   A 1 366 ? 33.830  -14.889 48.790  1.00 115.91 ?  488 THR   A OG1 1 
ATOM   2528 C CG2 . THR   A 1 366 ? 32.094  -14.156 50.189  1.00 125.85 ?  488 THR   A CG2 1 
ATOM   2529 N N   . ALA   A 1 367 ? 35.227  -11.733 51.458  1.00 125.02 ?  489 ALA   A N   1 
ATOM   2530 C CA  . ALA   A 1 367 ? 35.448  -10.910 52.645  1.00 122.47 ?  489 ALA   A CA  1 
ATOM   2531 C C   . ALA   A 1 367 ? 35.271  -9.425  52.332  1.00 125.68 ?  489 ALA   A C   1 
ATOM   2532 O O   . ALA   A 1 367 ? 34.562  -8.704  53.048  1.00 129.35 ?  489 ALA   A O   1 
ATOM   2533 C CB  . ALA   A 1 367 ? 36.844  -11.181 53.215  1.00 116.53 ?  489 ALA   A CB  1 
ATOM   2534 N N   . LEU   A 1 368 ? 35.919  -8.942  51.271  1.00 121.40 ?  490 LEU   A N   1 
ATOM   2535 C CA  . LEU   A 1 368 ? 35.730  -7.549  50.889  1.00 118.41 ?  490 LEU   A CA  1 
ATOM   2536 C C   . LEU   A 1 368 ? 34.304  -7.293  50.444  1.00 119.44 ?  490 LEU   A C   1 
ATOM   2537 O O   . LEU   A 1 368 ? 33.761  -6.221  50.699  1.00 127.16 ?  490 LEU   A O   1 
ATOM   2538 C CB  . LEU   A 1 368 ? 36.687  -7.146  49.777  1.00 116.36 ?  490 LEU   A CB  1 
ATOM   2539 C CG  . LEU   A 1 368 ? 38.172  -7.142  50.071  1.00 112.46 ?  490 LEU   A CG  1 
ATOM   2540 C CD1 . LEU   A 1 368 ? 38.742  -6.003  49.269  1.00 112.46 ?  490 LEU   A CD1 1 
ATOM   2541 C CD2 . LEU   A 1 368 ? 38.472  -7.028  51.565  1.00 110.70 ?  490 LEU   A CD2 1 
ATOM   2542 N N   . CYS   A 1 369 ? 33.683  -8.242  49.755  1.00 122.47 ?  491 CYS   A N   1 
ATOM   2543 C CA  . CYS   A 1 369 ? 32.291  -8.025  49.384  1.00 128.37 ?  491 CYS   A CA  1 
ATOM   2544 C C   . CYS   A 1 369 ? 31.400  -7.920  50.612  1.00 129.64 ?  491 CYS   A C   1 
ATOM   2545 O O   . CYS   A 1 369 ? 30.386  -7.214  50.578  1.00 130.75 ?  491 CYS   A O   1 
ATOM   2546 C CB  . CYS   A 1 369 ? 31.796  -9.128  48.451  1.00 130.18 ?  491 CYS   A CB  1 
ATOM   2547 S SG  . CYS   A 1 369 ? 32.161  -8.771  46.738  1.00 125.18 ?  491 CYS   A SG  1 
ATOM   2548 N N   . LYS   A 1 370 ? 31.759  -8.587  51.707  1.00 130.08 ?  492 LYS   A N   1 
ATOM   2549 C CA  . LYS   A 1 370 ? 30.972  -8.421  52.922  1.00 134.32 ?  492 LYS   A CA  1 
ATOM   2550 C C   . LYS   A 1 370 ? 31.188  -7.028  53.517  1.00 134.13 ?  492 LYS   A C   1 
ATOM   2551 O O   . LYS   A 1 370 ? 30.219  -6.309  53.786  1.00 134.62 ?  492 LYS   A O   1 
ATOM   2552 C CB  . LYS   A 1 370 ? 31.298  -9.527  53.931  1.00 131.96 ?  492 LYS   A CB  1 
ATOM   2553 C CG  . LYS   A 1 370 ? 30.312  -10.730 53.935  1.00 141.94 ?  492 LYS   A CG  1 
ATOM   2554 C CD  . LYS   A 1 370 ? 30.029  -11.366 52.534  1.00 144.72 ?  492 LYS   A CD  1 
ATOM   2555 C CE  . LYS   A 1 370 ? 29.360  -12.771 52.673  1.00 147.95 ?  492 LYS   A CE  1 
ATOM   2556 N NZ  . LYS   A 1 370 ? 29.160  -13.563 51.405  1.00 146.28 ?  492 LYS   A NZ  1 
ATOM   2557 N N   . GLU   A 1 371 ? 32.453  -6.619  53.702  1.00 129.60 ?  493 GLU   A N   1 
ATOM   2558 C CA  . GLU   A 1 371 ? 32.756  -5.264  54.162  1.00 122.83 ?  493 GLU   A CA  1 
ATOM   2559 C C   . GLU   A 1 371 ? 31.930  -4.224  53.415  1.00 124.21 ?  493 GLU   A C   1 
ATOM   2560 O O   . GLU   A 1 371 ? 31.179  -3.465  54.029  1.00 126.79 ?  493 GLU   A O   1 
ATOM   2561 C CB  . GLU   A 1 371 ? 34.234  -4.957  53.978  1.00 124.68 ?  493 GLU   A CB  1 
ATOM   2562 C CG  . GLU   A 1 371 ? 35.177  -5.580  54.962  1.00 131.21 ?  493 GLU   A CG  1 
ATOM   2563 C CD  . GLU   A 1 371 ? 36.500  -4.827  54.983  1.00 144.44 ?  493 GLU   A CD  1 
ATOM   2564 O OE1 . GLU   A 1 371 ? 36.495  -3.610  54.638  1.00 140.60 ?  493 GLU   A OE1 1 
ATOM   2565 O OE2 . GLU   A 1 371 ? 37.538  -5.462  55.302  1.00 144.78 ?  493 GLU   A OE2 1 
ATOM   2566 N N   . TYR   A 1 372 ? 32.045  -4.193  52.075  1.00 125.31 ?  494 TYR   A N   1 
ATOM   2567 C CA  . TYR   A 1 372 ? 31.356  -3.190  51.260  1.00 119.24 ?  494 TYR   A CA  1 
ATOM   2568 C C   . TYR   A 1 372 ? 29.840  -3.304  51.353  1.00 122.20 ?  494 TYR   A C   1 
ATOM   2569 O O   . TYR   A 1 372 ? 29.137  -2.345  51.037  1.00 127.93 ?  494 TYR   A O   1 
ATOM   2570 C CB  . TYR   A 1 372 ? 31.796  -3.266  49.785  1.00 111.94 ?  494 TYR   A CB  1 
ATOM   2571 C CG  . TYR   A 1 372 ? 31.058  -2.311  48.845  1.00 112.13 ?  494 TYR   A CG  1 
ATOM   2572 C CD1 . TYR   A 1 372 ? 29.744  -2.551  48.437  1.00 111.65 ?  494 TYR   A CD1 1 
ATOM   2573 C CD2 . TYR   A 1 372 ? 31.676  -1.166  48.363  1.00 112.16 ?  494 TYR   A CD2 1 
ATOM   2574 C CE1 . TYR   A 1 372 ? 29.066  -1.672  47.607  1.00 110.38 ?  494 TYR   A CE1 1 
ATOM   2575 C CE2 . TYR   A 1 372 ? 31.000  -0.288  47.505  1.00 108.97 ?  494 TYR   A CE2 1 
ATOM   2576 C CZ  . TYR   A 1 372 ? 29.697  -0.548  47.135  1.00 105.83 ?  494 TYR   A CZ  1 
ATOM   2577 O OH  . TYR   A 1 372 ? 29.017  0.313   46.295  1.00 107.73 ?  494 TYR   A OH  1 
ATOM   2578 N N   . ASP   A 1 373 ? 29.297  -4.424  51.791  1.00 126.30 ?  495 ASP   A N   1 
ATOM   2579 C CA  . ASP   A 1 373 ? 27.850  -4.427  51.972  1.00 129.31 ?  495 ASP   A CA  1 
ATOM   2580 C C   . ASP   A 1 373 ? 27.458  -3.747  53.284  1.00 132.98 ?  495 ASP   A C   1 
ATOM   2581 O O   . ASP   A 1 373 ? 26.575  -2.879  53.305  1.00 130.07 ?  495 ASP   A O   1 
ATOM   2582 C CB  . ASP   A 1 373 ? 27.335  -5.859  51.896  1.00 135.24 ?  495 ASP   A CB  1 
ATOM   2583 C CG  . ASP   A 1 373 ? 27.432  -6.426  50.493  1.00 137.46 ?  495 ASP   A CG  1 
ATOM   2584 O OD1 . ASP   A 1 373 ? 27.459  -5.620  49.531  1.00 135.77 ?  495 ASP   A OD1 1 
ATOM   2585 O OD2 . ASP   A 1 373 ? 27.506  -7.666  50.356  1.00 136.10 ?  495 ASP   A OD2 1 
ATOM   2586 N N   . GLU   A 1 374 ? 28.118  -4.137  54.383  1.00 134.78 ?  496 GLU   A N   1 
ATOM   2587 C CA  . GLU   A 1 374 ? 28.014  -3.436  55.662  1.00 131.52 ?  496 GLU   A CA  1 
ATOM   2588 C C   . GLU   A 1 374 ? 28.164  -1.930  55.501  1.00 132.39 ?  496 GLU   A C   1 
ATOM   2589 O O   . GLU   A 1 374 ? 27.383  -1.148  56.052  1.00 133.41 ?  496 GLU   A O   1 
ATOM   2590 C CB  . GLU   A 1 374 ? 29.096  -3.952  56.605  1.00 130.15 ?  496 GLU   A CB  1 
ATOM   2591 C CG  . GLU   A 1 374 ? 29.013  -5.428  56.898  1.00 135.76 ?  496 GLU   A CG  1 
ATOM   2592 C CD  . GLU   A 1 374 ? 29.537  -5.745  58.282  1.00 152.60 ?  496 GLU   A CD  1 
ATOM   2593 O OE1 . GLU   A 1 374 ? 29.690  -4.782  59.072  1.00 158.65 ?  496 GLU   A OE1 1 
ATOM   2594 O OE2 . GLU   A 1 374 ? 29.774  -6.941  58.589  1.00 151.27 ?  496 GLU   A OE2 1 
ATOM   2595 N N   . LEU   A 1 375 ? 29.184  -1.507  54.767  1.00 130.20 ?  497 LEU   A N   1 
ATOM   2596 C CA  . LEU   A 1 375 ? 29.524  -0.101  54.640  1.00 126.23 ?  497 LEU   A CA  1 
ATOM   2597 C C   . LEU   A 1 375 ? 28.685  0.617   53.601  1.00 127.95 ?  497 LEU   A C   1 
ATOM   2598 O O   . LEU   A 1 375 ? 29.074  1.708   53.199  1.00 133.14 ?  497 LEU   A O   1 
ATOM   2599 C CB  . LEU   A 1 375 ? 31.006  0.060   54.291  1.00 125.49 ?  497 LEU   A CB  1 
ATOM   2600 C CG  . LEU   A 1 375 ? 32.004  0.099   55.455  1.00 128.60 ?  497 LEU   A CG  1 
ATOM   2601 C CD1 . LEU   A 1 375 ? 31.848  -1.094  56.440  1.00 119.63 ?  497 LEU   A CD1 1 
ATOM   2602 C CD2 . LEU   A 1 375 ? 33.409  0.174   54.902  1.00 128.06 ?  497 LEU   A CD2 1 
ATOM   2603 N N   . ALA   A 1 376 ? 27.589  0.019   53.122  1.00 126.91 ?  498 ALA   A N   1 
ATOM   2604 C CA  . ALA   A 1 376 ? 26.527  0.749   52.435  1.00 130.76 ?  498 ALA   A CA  1 
ATOM   2605 C C   . ALA   A 1 376 ? 25.164  0.437   53.023  1.00 134.01 ?  498 ALA   A C   1 
ATOM   2606 O O   . ALA   A 1 376 ? 24.180  1.105   52.676  1.00 132.89 ?  498 ALA   A O   1 
ATOM   2607 C CB  . ALA   A 1 376 ? 26.522  0.451   50.931  1.00 120.07 ?  498 ALA   A CB  1 
ATOM   2608 N N   . GLU   A 1 377 ? 25.077  -0.593  53.863  1.00 138.22 ?  499 GLU   A N   1 
ATOM   2609 C CA  . GLU   A 1 377 ? 24.096  -0.629  54.941  1.00 148.48 ?  499 GLU   A CA  1 
ATOM   2610 C C   . GLU   A 1 377 ? 24.183  0.646   55.787  1.00 148.22 ?  499 GLU   A C   1 
ATOM   2611 O O   . GLU   A 1 377 ? 23.174  1.312   56.054  1.00 150.32 ?  499 GLU   A O   1 
ATOM   2612 C CB  . GLU   A 1 377 ? 24.350  -1.890  55.788  1.00 149.63 ?  499 GLU   A CB  1 
ATOM   2613 C CG  . GLU   A 1 377 ? 23.527  -2.063  57.063  1.00 157.69 ?  499 GLU   A CG  1 
ATOM   2614 C CD  . GLU   A 1 377 ? 22.050  -2.271  56.802  1.00 164.55 ?  499 GLU   A CD  1 
ATOM   2615 O OE1 . GLU   A 1 377 ? 21.709  -3.056  55.883  1.00 156.49 ?  499 GLU   A OE1 1 
ATOM   2616 O OE2 . GLU   A 1 377 ? 21.235  -1.649  57.527  1.00 170.57 ?  499 GLU   A OE2 1 
ATOM   2617 N N   . THR   A 1 378 ? 25.399  1.009   56.203  1.00 142.71 ?  500 THR   A N   1 
ATOM   2618 C CA  . THR   A 1 378 ? 25.594  2.236   56.963  1.00 135.59 ?  500 THR   A CA  1 
ATOM   2619 C C   . THR   A 1 378 ? 25.380  3.478   56.101  1.00 130.50 ?  500 THR   A C   1 
ATOM   2620 O O   . THR   A 1 378 ? 24.873  4.482   56.597  1.00 131.85 ?  500 THR   A O   1 
ATOM   2621 C CB  . THR   A 1 378 ? 26.986  2.212   57.593  1.00 133.26 ?  500 THR   A CB  1 
ATOM   2622 O OG1 . THR   A 1 378 ? 26.977  1.330   58.731  1.00 127.41 ?  500 THR   A OG1 1 
ATOM   2623 C CG2 . THR   A 1 378 ? 27.444  3.612   57.988  1.00 122.89 ?  500 THR   A CG2 1 
ATOM   2624 N N   . GLN   A 1 379 ? 25.723  3.430   54.811  1.00 130.08 ?  501 GLN   A N   1 
ATOM   2625 C CA  . GLN   A 1 379 ? 25.336  4.523   53.921  1.00 134.32 ?  501 GLN   A CA  1 
ATOM   2626 C C   . GLN   A 1 379 ? 23.824  4.666   53.840  1.00 141.68 ?  501 GLN   A C   1 
ATOM   2627 O O   . GLN   A 1 379 ? 23.313  5.749   53.523  1.00 142.04 ?  501 GLN   A O   1 
ATOM   2628 C CB  . GLN   A 1 379 ? 25.896  4.315   52.511  1.00 133.38 ?  501 GLN   A CB  1 
ATOM   2629 C CG  . GLN   A 1 379 ? 25.662  5.509   51.582  1.00 133.61 ?  501 GLN   A CG  1 
ATOM   2630 C CD  . GLN   A 1 379 ? 25.440  5.107   50.143  1.00 135.11 ?  501 GLN   A CD  1 
ATOM   2631 O OE1 . GLN   A 1 379 ? 25.628  3.947   49.780  1.00 137.23 ?  501 GLN   A OE1 1 
ATOM   2632 N NE2 . GLN   A 1 379 ? 25.029  6.067   49.310  1.00 131.79 ?  501 GLN   A NE2 1 
ATOM   2633 N N   . GLY   A 1 380 ? 23.090  3.585   54.100  1.00 143.28 ?  502 GLY   A N   1 
ATOM   2634 C CA  . GLY   A 1 380 ? 21.641  3.686   54.101  1.00 147.28 ?  502 GLY   A CA  1 
ATOM   2635 C C   . GLY   A 1 380 ? 21.128  4.550   55.236  1.00 144.94 ?  502 GLY   A C   1 
ATOM   2636 O O   . GLY   A 1 380 ? 20.374  5.505   55.016  1.00 144.25 ?  502 GLY   A O   1 
ATOM   2637 N N   . LYS   A 1 381 ? 21.563  4.244   56.464  1.00 143.05 ?  503 LYS   A N   1 
ATOM   2638 C CA  . LYS   A 1 381 ? 21.026  4.906   57.648  1.00 144.93 ?  503 LYS   A CA  1 
ATOM   2639 C C   . LYS   A 1 381 ? 21.378  6.395   57.674  1.00 145.30 ?  503 LYS   A C   1 
ATOM   2640 O O   . LYS   A 1 381 ? 20.525  7.233   57.997  1.00 146.84 ?  503 LYS   A O   1 
ATOM   2641 C CB  . LYS   A 1 381 ? 21.526  4.184   58.903  1.00 143.70 ?  503 LYS   A CB  1 
ATOM   2642 C CG  . LYS   A 1 381 ? 20.761  2.890   59.189  1.00 151.73 ?  503 LYS   A CG  1 
ATOM   2643 C CD  . LYS   A 1 381 ? 21.406  2.039   60.276  1.00 158.06 ?  503 LYS   A CD  1 
ATOM   2644 C CE  . LYS   A 1 381 ? 20.379  1.094   60.901  1.00 161.65 ?  503 LYS   A CE  1 
ATOM   2645 N NZ  . LYS   A 1 381 ? 20.853  -0.321  61.009  1.00 161.00 ?  503 LYS   A NZ  1 
ATOM   2646 N N   . LEU   A 1 382 ? 22.621  6.752   57.320  1.00 140.59 ?  504 LEU   A N   1 
ATOM   2647 C CA  . LEU   A 1 382 ? 22.983  8.166   57.313  1.00 131.73 ?  504 LEU   A CA  1 
ATOM   2648 C C   . LEU   A 1 382 ? 22.275  8.919   56.201  1.00 134.00 ?  504 LEU   A C   1 
ATOM   2649 O O   . LEU   A 1 382 ? 21.861  10.062  56.397  1.00 143.54 ?  504 LEU   A O   1 
ATOM   2650 C CB  . LEU   A 1 382 ? 24.494  8.375   57.194  1.00 123.74 ?  504 LEU   A CB  1 
ATOM   2651 C CG  . LEU   A 1 382 ? 25.490  7.716   58.154  1.00 131.26 ?  504 LEU   A CG  1 
ATOM   2652 C CD1 . LEU   A 1 382 ? 26.841  8.466   58.105  1.00 124.98 ?  504 LEU   A CD1 1 
ATOM   2653 C CD2 . LEU   A 1 382 ? 24.953  7.575   59.588  1.00 122.71 ?  504 LEU   A CD2 1 
ATOM   2654 N N   . GLU   A 1 383 ? 22.115  8.311   55.030  1.00 138.16 ?  505 GLU   A N   1 
ATOM   2655 C CA  . GLU   A 1 383 ? 21.564  9.078   53.915  1.00 146.18 ?  505 GLU   A CA  1 
ATOM   2656 C C   . GLU   A 1 383 ? 20.103  9.487   54.143  1.00 146.71 ?  505 GLU   A C   1 
ATOM   2657 O O   . GLU   A 1 383 ? 19.593  10.359  53.420  1.00 139.57 ?  505 GLU   A O   1 
ATOM   2658 C CB  . GLU   A 1 383 ? 21.742  8.280   52.611  1.00 146.58 ?  505 GLU   A CB  1 
ATOM   2659 C CG  . GLU   A 1 383 ? 21.641  9.105   51.326  1.00 146.70 ?  505 GLU   A CG  1 
ATOM   2660 C CD  . GLU   A 1 383 ? 22.233  8.403   50.111  1.00 144.78 ?  505 GLU   A CD  1 
ATOM   2661 O OE1 . GLU   A 1 383 ? 22.046  7.176   49.977  1.00 143.12 ?  505 GLU   A OE1 1 
ATOM   2662 O OE2 . GLU   A 1 383 ? 22.846  9.095   49.266  1.00 144.81 ?  505 GLU   A OE2 1 
ATOM   2663 N N   . GLU   A 1 384 ? 19.431  8.913   55.149  1.00 145.13 ?  506 GLU   A N   1 
ATOM   2664 C CA  . GLU   A 1 384 ? 18.079  9.331   55.505  1.00 149.45 ?  506 GLU   A CA  1 
ATOM   2665 C C   . GLU   A 1 384 ? 18.022  10.146  56.791  1.00 152.53 ?  506 GLU   A C   1 
ATOM   2666 O O   . GLU   A 1 384 ? 17.227  11.089  56.869  1.00 155.44 ?  506 GLU   A O   1 
ATOM   2667 C CB  . GLU   A 1 384 ? 17.146  8.115   55.620  1.00 154.80 ?  506 GLU   A CB  1 
ATOM   2668 C CG  . GLU   A 1 384 ? 17.556  7.052   56.633  1.00 162.36 ?  506 GLU   A CG  1 
ATOM   2669 C CD  . GLU   A 1 384 ? 16.389  6.132   57.018  1.00 173.25 ?  506 GLU   A CD  1 
ATOM   2670 O OE1 . GLU   A 1 384 ? 15.222  6.573   56.899  1.00 178.32 ?  506 GLU   A OE1 1 
ATOM   2671 O OE2 . GLU   A 1 384 ? 16.637  4.982   57.466  1.00 169.72 ?  506 GLU   A OE2 1 
ATOM   2672 N N   . LYS   A 1 385 ? 18.884  9.856   57.774  1.00 146.51 ?  507 LYS   A N   1 
ATOM   2673 C CA  . LYS   A 1 385 ? 19.122  10.761  58.897  1.00 139.56 ?  507 LYS   A CA  1 
ATOM   2674 C C   . LYS   A 1 385 ? 19.151  12.187  58.327  1.00 139.56 ?  507 LYS   A C   1 
ATOM   2675 O O   . LYS   A 1 385 ? 18.568  13.103  58.909  1.00 139.97 ?  507 LYS   A O   1 
ATOM   2676 C CB  . LYS   A 1 385 ? 20.218  10.195  59.798  1.00 125.99 ?  507 LYS   A CB  1 
ATOM   2677 C CG  . LYS   A 1 385 ? 20.347  10.917  61.097  1.00 129.51 ?  507 LYS   A CG  1 
ATOM   2678 C CD  . LYS   A 1 385 ? 21.635  10.595  61.793  1.00 134.81 ?  507 LYS   A CD  1 
ATOM   2679 C CE  . LYS   A 1 385 ? 21.810  11.510  62.999  1.00 141.92 ?  507 LYS   A CE  1 
ATOM   2680 N NZ  . LYS   A 1 385 ? 23.158  11.415  63.634  1.00 139.45 ?  507 LYS   A NZ  1 
ATOM   2681 N N   . LEU   A 1 386 ? 19.829  12.388  57.185  1.00 142.30 ?  508 LEU   A N   1 
ATOM   2682 C CA  . LEU   A 1 386 ? 19.939  13.673  56.496  1.00 145.22 ?  508 LEU   A CA  1 
ATOM   2683 C C   . LEU   A 1 386 ? 18.835  14.283  55.631  1.00 151.86 ?  508 LEU   A C   1 
ATOM   2684 O O   . LEU   A 1 386 ? 19.012  15.409  55.138  1.00 151.76 ?  508 LEU   A O   1 
ATOM   2685 C CB  . LEU   A 1 386 ? 21.227  13.552  55.659  1.00 142.24 ?  508 LEU   A CB  1 
ATOM   2686 C CG  . LEU   A 1 386 ? 22.553  13.688  56.401  1.00 132.52 ?  508 LEU   A CG  1 
ATOM   2687 C CD1 . LEU   A 1 386 ? 23.702  13.403  55.508  1.00 130.71 ?  508 LEU   A CD1 1 
ATOM   2688 C CD2 . LEU   A 1 386 ? 22.627  15.132  56.727  1.00 133.93 ?  508 LEU   A CD2 1 
ATOM   2689 N N   . GLN   A 1 387 ? 17.720  13.586  55.411  1.00 153.26 ?  509 GLN   A N   1 
ATOM   2690 C CA  . GLN   A 1 387 ? 16.486  14.303  55.107  1.00 157.62 ?  509 GLN   A CA  1 
ATOM   2691 C C   . GLN   A 1 387 ? 15.667  14.528  56.368  1.00 156.70 ?  509 GLN   A C   1 
ATOM   2692 O O   . GLN   A 1 387 ? 14.922  15.516  56.448  1.00 155.49 ?  509 GLN   A O   1 
ATOM   2693 C CB  . GLN   A 1 387 ? 15.658  13.566  54.050  1.00 159.46 ?  509 GLN   A CB  1 
ATOM   2694 C CG  . GLN   A 1 387 ? 16.228  13.693  52.646  1.00 167.78 ?  509 GLN   A CG  1 
ATOM   2695 C CD  . GLN   A 1 387 ? 15.764  12.580  51.713  1.00 180.22 ?  509 GLN   A CD  1 
ATOM   2696 O OE1 . GLN   A 1 387 ? 14.573  12.453  51.414  1.00 183.08 ?  509 GLN   A OE1 1 
ATOM   2697 N NE2 . GLN   A 1 387 ? 16.711  11.757  51.258  1.00 175.80 ?  509 GLN   A NE2 1 
ATOM   2698 N N   . GLU   A 1 388 ? 15.805  13.624  57.349  1.00 149.87 ?  510 GLU   A N   1 
ATOM   2699 C CA  . GLU   A 1 388 ? 15.481  13.894  58.746  1.00 147.06 ?  510 GLU   A CA  1 
ATOM   2700 C C   . GLU   A 1 388 ? 15.793  15.284  59.289  1.00 152.11 ?  510 GLU   A C   1 
ATOM   2701 O O   . GLU   A 1 388 ? 14.914  15.955  59.840  1.00 153.24 ?  510 GLU   A O   1 
ATOM   2702 C CB  . GLU   A 1 388 ? 16.258  12.934  59.656  1.00 147.26 ?  510 GLU   A CB  1 
ATOM   2703 C CG  . GLU   A 1 388 ? 16.285  13.308  61.148  1.00 155.30 ?  510 GLU   A CG  1 
ATOM   2704 C CD  . GLU   A 1 388 ? 14.976  13.092  61.887  1.00 164.30 ?  510 GLU   A CD  1 
ATOM   2705 O OE1 . GLU   A 1 388 ? 13.998  12.607  61.271  1.00 162.48 ?  510 GLU   A OE1 1 
ATOM   2706 O OE2 . GLU   A 1 388 ? 14.923  13.440  63.092  1.00 166.01 ?  510 GLU   A OE2 1 
ATOM   2707 N N   . LEU   A 1 389 ? 17.027  15.747  59.096  1.00 149.32 ?  511 LEU   A N   1 
ATOM   2708 C CA  . LEU   A 1 389 ? 17.450  16.981  59.734  1.00 140.00 ?  511 LEU   A CA  1 
ATOM   2709 C C   . LEU   A 1 389 ? 17.091  18.116  58.784  1.00 142.10 ?  511 LEU   A C   1 
ATOM   2710 O O   . LEU   A 1 389 ? 17.000  19.262  59.230  1.00 150.57 ?  511 LEU   A O   1 
ATOM   2711 C CB  . LEU   A 1 389 ? 18.935  16.978  60.084  1.00 133.85 ?  511 LEU   A CB  1 
ATOM   2712 C CG  . LEU   A 1 389 ? 19.249  15.893  61.123  1.00 137.30 ?  511 LEU   A CG  1 
ATOM   2713 C CD1 . LEU   A 1 389 ? 20.644  16.069  61.654  1.00 136.33 ?  511 LEU   A CD1 1 
ATOM   2714 C CD2 . LEU   A 1 389 ? 18.248  15.915  62.278  1.00 142.55 ?  511 LEU   A CD2 1 
ATOM   2715 N N   . GLU   A 1 390 ? 16.844  17.846  57.505  1.00 141.20 ?  512 GLU   A N   1 
ATOM   2716 C CA  . GLU   A 1 390 ? 16.350  18.900  56.624  1.00 148.19 ?  512 GLU   A CA  1 
ATOM   2717 C C   . GLU   A 1 390 ? 14.826  18.997  56.629  1.00 147.34 ?  512 GLU   A C   1 
ATOM   2718 O O   . GLU   A 1 390 ? 14.254  19.742  55.821  1.00 140.77 ?  512 GLU   A O   1 
ATOM   2719 C CB  . GLU   A 1 390 ? 16.886  18.695  55.206  1.00 149.57 ?  512 GLU   A CB  1 
ATOM   2720 C CG  . GLU   A 1 390 ? 17.939  19.731  54.818  1.00 151.16 ?  512 GLU   A CG  1 
ATOM   2721 C CD  . GLU   A 1 390 ? 18.900  19.227  53.751  1.00 158.43 ?  512 GLU   A CD  1 
ATOM   2722 O OE1 . GLU   A 1 390 ? 18.577  18.208  53.098  1.00 160.54 ?  512 GLU   A OE1 1 
ATOM   2723 O OE2 . GLU   A 1 390 ? 19.968  19.861  53.556  1.00 155.18 ?  512 GLU   A OE2 1 
ATOM   2724 N N   . ALA   A 1 391 ? 14.168  18.287  57.555  1.00 146.99 ?  513 ALA   A N   1 
ATOM   2725 C CA  . ALA   A 1 391 ? 12.715  18.254  57.668  1.00 148.01 ?  513 ALA   A CA  1 
ATOM   2726 C C   . ALA   A 1 391 ? 12.174  18.645  59.043  1.00 149.12 ?  513 ALA   A C   1 
ATOM   2727 O O   . ALA   A 1 391 ? 10.954  18.809  59.181  1.00 148.46 ?  513 ALA   A O   1 
ATOM   2728 C CB  . ALA   A 1 391 ? 12.187  16.858  57.306  1.00 143.48 ?  513 ALA   A CB  1 
ATOM   2729 N N   . ASN   A 1 392 ? 13.030  18.790  60.065  1.00 151.32 ?  514 ASN   A N   1 
ATOM   2730 C CA  . ASN   A 1 392 ? 12.662  19.585  61.236  1.00 149.57 ?  514 ASN   A CA  1 
ATOM   2731 C C   . ASN   A 1 392 ? 13.539  20.833  61.304  1.00 145.57 ?  514 ASN   A C   1 
ATOM   2732 O O   . ASN   A 1 392 ? 14.237  21.019  62.311  1.00 144.15 ?  514 ASN   A O   1 
ATOM   2733 C CB  . ASN   A 1 392 ? 12.797  18.821  62.574  1.00 154.65 ?  514 ASN   A CB  1 
ATOM   2734 C CG  . ASN   A 1 392 ? 14.135  18.042  62.729  1.00 158.66 ?  514 ASN   A CG  1 
ATOM   2735 O OD1 . ASN   A 1 392 ? 14.454  17.157  61.934  1.00 158.00 ?  514 ASN   A OD1 1 
ATOM   2736 N ND2 . ASN   A 1 392 ? 14.942  18.431  63.729  1.00 151.22 ?  514 ASN   A ND2 1 
ATOM   2737 N N   . PRO   A 1 393 ? 13.556  21.705  60.290  1.00 142.67 ?  515 PRO   A N   1 
ATOM   2738 C CA  . PRO   A 1 393 ? 14.442  22.864  60.356  1.00 143.54 ?  515 PRO   A CA  1 
ATOM   2739 C C   . PRO   A 1 393 ? 13.850  23.924  61.268  1.00 147.06 ?  515 PRO   A C   1 
ATOM   2740 O O   . PRO   A 1 393 ? 12.793  24.493  60.953  1.00 145.39 ?  515 PRO   A O   1 
ATOM   2741 C CB  . PRO   A 1 393 ? 14.512  23.342  58.897  1.00 136.86 ?  515 PRO   A CB  1 
ATOM   2742 C CG  . PRO   A 1 393 ? 13.227  22.957  58.335  1.00 137.35 ?  515 PRO   A CG  1 
ATOM   2743 C CD  . PRO   A 1 393 ? 12.798  21.697  59.024  1.00 140.63 ?  515 PRO   A CD  1 
ATOM   2744 N N   . PRO   A 1 394 ? 14.502  24.217  62.435  1.00 144.09 ?  516 PRO   A N   1 
ATOM   2745 C CA  . PRO   A 1 394 ? 13.909  25.162  63.385  1.00 140.96 ?  516 PRO   A CA  1 
ATOM   2746 C C   . PRO   A 1 394 ? 13.678  26.521  62.747  1.00 142.30 ?  516 PRO   A C   1 
ATOM   2747 O O   . PRO   A 1 394 ? 14.069  26.754  61.597  1.00 136.29 ?  516 PRO   A O   1 
ATOM   2748 C CB  . PRO   A 1 394 ? 14.939  25.219  64.521  1.00 140.30 ?  516 PRO   A CB  1 
ATOM   2749 C CG  . PRO   A 1 394 ? 16.212  24.882  63.901  1.00 134.28 ?  516 PRO   A CG  1 
ATOM   2750 C CD  . PRO   A 1 394 ? 15.898  23.908  62.791  1.00 143.76 ?  516 PRO   A CD  1 
ATOM   2751 N N   . SER   A 1 395 ? 13.061  27.424  63.504  1.00 143.86 ?  517 SER   A N   1 
ATOM   2752 C CA  . SER   A 1 395 ? 12.305  28.517  62.912  1.00 134.92 ?  517 SER   A CA  1 
ATOM   2753 C C   . SER   A 1 395 ? 13.196  29.490  62.157  1.00 125.42 ?  517 SER   A C   1 
ATOM   2754 O O   . SER   A 1 395 ? 14.353  29.728  62.512  1.00 124.04 ?  517 SER   A O   1 
ATOM   2755 C CB  . SER   A 1 395 ? 11.518  29.249  63.990  1.00 135.98 ?  517 SER   A CB  1 
ATOM   2756 O OG  . SER   A 1 395 ? 10.813  28.309  64.780  1.00 141.49 ?  517 SER   A OG  1 
ATOM   2757 N N   . ASP   A 1 396 ? 12.615  30.056  61.101  1.00 117.42 ?  518 ASP   A N   1 
ATOM   2758 C CA  . ASP   A 1 396 ? 13.336  30.947  60.205  1.00 125.08 ?  518 ASP   A CA  1 
ATOM   2759 C C   . ASP   A 1 396 ? 13.627  32.301  60.867  1.00 135.25 ?  518 ASP   A C   1 
ATOM   2760 O O   . ASP   A 1 396 ? 14.714  32.871  60.679  1.00 126.96 ?  518 ASP   A O   1 
ATOM   2761 C CB  . ASP   A 1 396 ? 12.507  31.095  58.923  1.00 130.66 ?  518 ASP   A CB  1 
ATOM   2762 C CG  . ASP   A 1 396 ? 13.164  31.982  57.868  1.00 141.67 ?  518 ASP   A CG  1 
ATOM   2763 O OD1 . ASP   A 1 396 ? 14.352  32.345  58.022  1.00 145.30 ?  518 ASP   A OD1 1 
ATOM   2764 O OD2 . ASP   A 1 396 ? 12.479  32.314  56.868  1.00 142.68 ?  518 ASP   A OD2 1 
ATOM   2765 N N   . VAL   A 1 397 ? 12.680  32.814  61.674  1.00 140.41 ?  519 VAL   A N   1 
ATOM   2766 C CA  . VAL   A 1 397 ? 12.704  34.176  62.214  1.00 126.94 ?  519 VAL   A CA  1 
ATOM   2767 C C   . VAL   A 1 397 ? 12.336  34.162  63.700  1.00 127.61 ?  519 VAL   A C   1 
ATOM   2768 O O   . VAL   A 1 397 ? 11.861  33.161  64.246  1.00 122.95 ?  519 VAL   A O   1 
ATOM   2769 C CB  . VAL   A 1 397 ? 11.739  35.111  61.443  1.00 118.22 ?  519 VAL   A CB  1 
ATOM   2770 C CG1 . VAL   A 1 397 ? 12.272  35.408  60.053  1.00 121.34 ?  519 VAL   A CG1 1 
ATOM   2771 C CG2 . VAL   A 1 397 ? 10.335  34.517  61.363  1.00 112.67 ?  519 VAL   A CG2 1 
ATOM   2772 N N   . TYR   A 1 398 ? 12.570  35.303  64.364  1.00 134.31 ?  520 TYR   A N   1 
ATOM   2773 C CA  . TYR   A 1 398 ? 11.881  35.587  65.625  1.00 130.00 ?  520 TYR   A CA  1 
ATOM   2774 C C   . TYR   A 1 398 ? 10.514  36.226  65.379  1.00 121.47 ?  520 TYR   A C   1 
ATOM   2775 O O   . TYR   A 1 398 ? 9.495   35.755  65.899  1.00 112.70 ?  520 TYR   A O   1 
ATOM   2776 C CB  . TYR   A 1 398 ? 12.689  36.520  66.536  1.00 125.21 ?  520 TYR   A CB  1 
ATOM   2777 C CG  . TYR   A 1 398 ? 11.912  36.755  67.812  1.00 120.29 ?  520 TYR   A CG  1 
ATOM   2778 C CD1 . TYR   A 1 398 ? 11.644  35.710  68.665  1.00 117.76 ?  520 TYR   A CD1 1 
ATOM   2779 C CD2 . TYR   A 1 398 ? 11.331  37.991  68.101  1.00 118.92 ?  520 TYR   A CD2 1 
ATOM   2780 C CE1 . TYR   A 1 398 ? 10.899  35.898  69.818  1.00 118.12 ?  520 TYR   A CE1 1 
ATOM   2781 C CE2 . TYR   A 1 398 ? 10.571  38.181  69.261  1.00 108.29 ?  520 TYR   A CE2 1 
ATOM   2782 C CZ  . TYR   A 1 398 ? 10.366  37.124  70.106  1.00 108.92 ?  520 TYR   A CZ  1 
ATOM   2783 O OH  . TYR   A 1 398 ? 9.627   37.250  71.247  1.00 105.44 ?  520 TYR   A OH  1 
ATOM   2784 N N   . LEU   A 1 399 ? 10.494  37.316  64.611  1.00 116.32 ?  521 LEU   A N   1 
ATOM   2785 C CA  . LEU   A 1 399 ? 9.257   37.938  64.177  1.00 116.70 ?  521 LEU   A CA  1 
ATOM   2786 C C   . LEU   A 1 399 ? 9.495   38.625  62.840  1.00 112.64 ?  521 LEU   A C   1 
ATOM   2787 O O   . LEU   A 1 399 ? 10.606  39.074  62.545  1.00 113.54 ?  521 LEU   A O   1 
ATOM   2788 C CB  . LEU   A 1 399 ? 8.733   38.953  65.202  1.00 120.74 ?  521 LEU   A CB  1 
ATOM   2789 C CG  . LEU   A 1 399 ? 8.264   38.497  66.587  1.00 117.39 ?  521 LEU   A CG  1 
ATOM   2790 C CD1 . LEU   A 1 399 ? 8.177   39.684  67.501  1.00 112.80 ?  521 LEU   A CD1 1 
ATOM   2791 C CD2 . LEU   A 1 399 ? 6.943   37.751  66.543  1.00 119.54 ?  521 LEU   A CD2 1 
ATOM   2792 N N   . SER   A 1 400 ? 8.429   38.719  62.049  1.00 107.16 ?  522 SER   A N   1 
ATOM   2793 C CA  . SER   A 1 400 ? 8.437   39.343  60.736  1.00 110.45 ?  522 SER   A CA  1 
ATOM   2794 C C   . SER   A 1 400 ? 8.140   40.836  60.833  1.00 116.20 ?  522 SER   A C   1 
ATOM   2795 O O   . SER   A 1 400 ? 7.841   41.357  61.905  1.00 124.69 ?  522 SER   A O   1 
ATOM   2796 C CB  . SER   A 1 400 ? 7.409   38.667  59.836  1.00 115.81 ?  522 SER   A CB  1 
ATOM   2797 O OG  . SER   A 1 400 ? 6.097   39.076  60.176  1.00 114.06 ?  522 SER   A OG  1 
ATOM   2798 N N   . SER   A 1 401 ? 8.195   41.537  59.693  1.00 112.66 ?  523 SER   A N   1 
ATOM   2799 C CA  . SER   A 1 401 ? 7.720   42.921  59.653  1.00 116.60 ?  523 SER   A CA  1 
ATOM   2800 C C   . SER   A 1 401 ? 6.266   43.020  60.085  1.00 115.88 ?  523 SER   A C   1 
ATOM   2801 O O   . SER   A 1 401 ? 5.910   43.856  60.915  1.00 118.39 ?  523 SER   A O   1 
ATOM   2802 C CB  . SER   A 1 401 ? 7.879   43.507  58.256  1.00 125.06 ?  523 SER   A CB  1 
ATOM   2803 O OG  . SER   A 1 401 ? 9.152   44.091  58.107  1.00 142.36 ?  523 SER   A OG  1 
ATOM   2804 N N   . ARG   A 1 402 ? 5.407   42.185  59.508  1.00 117.98 ?  524 ARG   A N   1 
ATOM   2805 C CA  . ARG   A 1 402 ? 4.012   42.131  59.928  1.00 119.56 ?  524 ARG   A CA  1 
ATOM   2806 C C   . ARG   A 1 402 ? 3.901   41.768  61.408  1.00 121.20 ?  524 ARG   A C   1 
ATOM   2807 O O   . ARG   A 1 402 ? 3.024   42.278  62.115  1.00 127.04 ?  524 ARG   A O   1 
ATOM   2808 C CB  . ARG   A 1 402 ? 3.256   41.126  59.048  1.00 126.64 ?  524 ARG   A CB  1 
ATOM   2809 C CG  . ARG   A 1 402 ? 1.802   41.452  58.719  1.00 127.73 ?  524 ARG   A CG  1 
ATOM   2810 C CD  . ARG   A 1 402 ? 1.176   40.353  57.858  1.00 128.70 ?  524 ARG   A CD  1 
ATOM   2811 N NE  . ARG   A 1 402 ? -0.280  40.450  57.802  1.00 138.05 ?  524 ARG   A NE  1 
ATOM   2812 C CZ  . ARG   A 1 402 ? -1.109  39.581  58.377  1.00 143.38 ?  524 ARG   A CZ  1 
ATOM   2813 N NH1 . ARG   A 1 402 ? -0.656  38.555  59.087  1.00 140.17 ?  524 ARG   A NH1 1 
ATOM   2814 N NH2 . ARG   A 1 402 ? -2.426  39.755  58.253  1.00 137.72 ?  524 ARG   A NH2 1 
ATOM   2815 N N   . ASP   A 1 403 ? 4.789   40.902  61.903  1.00 119.94 ?  525 ASP   A N   1 
ATOM   2816 C CA  . ASP   A 1 403 ? 4.789   40.537  63.318  1.00 119.17 ?  525 ASP   A CA  1 
ATOM   2817 C C   . ASP   A 1 403 ? 5.157   41.544  64.402  1.00 120.22 ?  525 ASP   A C   1 
ATOM   2818 O O   . ASP   A 1 403 ? 4.382   41.726  65.349  1.00 122.21 ?  525 ASP   A O   1 
ATOM   2819 C CB  . ASP   A 1 403 ? 5.786   39.414  63.606  1.00 124.53 ?  525 ASP   A CB  1 
ATOM   2820 C CG  . ASP   A 1 403 ? 5.486   38.119  62.841  1.00 127.55 ?  525 ASP   A CG  1 
ATOM   2821 O OD1 . ASP   A 1 403 ? 4.299   37.851  62.566  1.00 125.82 ?  525 ASP   A OD1 1 
ATOM   2822 O OD2 . ASP   A 1 403 ? 6.444   37.359  62.541  1.00 120.83 ?  525 ASP   A OD2 1 
ATOM   2823 N N   . ARG   A 1 404 ? 6.310   42.232  64.255  1.00 121.95 ?  526 ARG   A N   1 
ATOM   2824 C CA  . ARG   A 1 404 ? 6.859   43.099  65.308  1.00 119.85 ?  526 ARG   A CA  1 
ATOM   2825 C C   . ARG   A 1 404 ? 6.300   44.468  64.907  1.00 108.70 ?  526 ARG   A C   1 
ATOM   2826 O O   . ARG   A 1 404 ? 6.766   45.472  65.439  1.00 111.52 ?  526 ARG   A O   1 
ATOM   2827 C CB  . ARG   A 1 404 ? 8.423   43.209  65.292  1.00 115.41 ?  526 ARG   A CB  1 
ATOM   2828 C CG  . ARG   A 1 404 ? 9.125   44.109  66.408  1.00 112.53 ?  526 ARG   A CG  1 
ATOM   2829 C CD  . ARG   A 1 404 ? 10.691  44.209  66.418  1.00 126.22 ?  526 ARG   A CD  1 
ATOM   2830 N NE  . ARG   A 1 404 ? 11.240  45.067  67.490  1.00 137.97 ?  526 ARG   A NE  1 
ATOM   2831 C CZ  . ARG   A 1 404 ? 11.410  46.396  67.424  1.00 142.97 ?  526 ARG   A CZ  1 
ATOM   2832 N NH1 . ARG   A 1 404 ? 11.232  47.066  66.287  1.00 133.74 ?  526 ARG   A NH1 1 
ATOM   2833 N NH2 . ARG   A 1 404 ? 11.789  47.074  68.523  1.00 127.77 ?  526 ARG   A NH2 1 
ATOM   2834 N N   . GLN   A 1 405 ? 5.274   44.519  64.044  1.00 104.91 ?  527 GLN   A N   1 
ATOM   2835 C CA  . GLN   A 1 405 ? 4.526   45.745  63.763  1.00 112.27 ?  527 GLN   A CA  1 
ATOM   2836 C C   . GLN   A 1 405 ? 3.221   45.637  64.533  1.00 109.13 ?  527 GLN   A C   1 
ATOM   2837 O O   . GLN   A 1 405 ? 2.708   46.651  65.016  1.00 114.49 ?  527 GLN   A O   1 
ATOM   2838 C CB  . GLN   A 1 405 ? 4.184   45.912  62.293  1.00 121.81 ?  527 GLN   A CB  1 
ATOM   2839 C CG  . GLN   A 1 405 ? 5.082   46.809  61.489  1.00 125.04 ?  527 GLN   A CG  1 
ATOM   2840 C CD  . GLN   A 1 405 ? 4.510   47.032  60.097  1.00 127.37 ?  527 GLN   A CD  1 
ATOM   2841 O OE1 . GLN   A 1 405 ? 3.565   46.345  59.682  1.00 121.23 ?  527 GLN   A OE1 1 
ATOM   2842 N NE2 . GLN   A 1 405 ? 5.060   48.007  59.379  1.00 131.01 ?  527 GLN   A NE2 1 
ATOM   2843 N N   . ILE   A 1 406 ? 2.625   44.447  64.579  1.00 105.03 ?  528 ILE   A N   1 
ATOM   2844 C CA  . ILE   A 1 406 ? 1.467   44.225  65.442  1.00 111.19 ?  528 ILE   A CA  1 
ATOM   2845 C C   . ILE   A 1 406 ? 1.893   44.250  66.907  1.00 111.62 ?  528 ILE   A C   1 
ATOM   2846 O O   . ILE   A 1 406 ? 1.181   44.767  67.779  1.00 107.77 ?  528 ILE   A O   1 
ATOM   2847 C CB  . ILE   A 1 406 ? 0.786   42.890  65.084  1.00 115.14 ?  528 ILE   A CB  1 
ATOM   2848 C CG1 . ILE   A 1 406 ? 0.201   42.942  63.685  1.00 120.72 ?  528 ILE   A CG1 1 
ATOM   2849 C CG2 . ILE   A 1 406 ? -0.342  42.552  66.064  1.00 111.67 ?  528 ILE   A CG2 1 
ATOM   2850 C CD1 . ILE   A 1 406 ? -0.157  41.576  63.180  1.00 125.75 ?  528 ILE   A CD1 1 
ATOM   2851 N N   . LEU   A 1 407 ? 3.051   43.666  67.206  1.00 110.21 ?  529 LEU   A N   1 
ATOM   2852 C CA  . LEU   A 1 407 ? 3.621   43.816  68.530  1.00 101.12 ?  529 LEU   A CA  1 
ATOM   2853 C C   . LEU   A 1 407 ? 3.862   45.285  68.850  1.00 107.08 ?  529 LEU   A C   1 
ATOM   2854 O O   . LEU   A 1 407 ? 3.761   45.692  70.010  1.00 109.53 ?  529 LEU   A O   1 
ATOM   2855 C CB  . LEU   A 1 407 ? 4.918   43.028  68.614  1.00 94.69  ?  529 LEU   A CB  1 
ATOM   2856 C CG  . LEU   A 1 407 ? 5.647   43.118  69.939  1.00 97.78  ?  529 LEU   A CG  1 
ATOM   2857 C CD1 . LEU   A 1 407 ? 4.911   42.296  70.986  1.00 93.54  ?  529 LEU   A CD1 1 
ATOM   2858 C CD2 . LEU   A 1 407 ? 7.093   42.678  69.776  1.00 96.40  ?  529 LEU   A CD2 1 
ATOM   2859 N N   . ASP   A 1 408 ? 4.176   46.102  67.841  1.00 107.09 ?  530 ASP   A N   1 
ATOM   2860 C CA  . ASP   A 1 408 ? 4.342   47.525  68.102  1.00 101.45 ?  530 ASP   A CA  1 
ATOM   2861 C C   . ASP   A 1 408 ? 3.048   48.143  68.586  1.00 103.14 ?  530 ASP   A C   1 
ATOM   2862 O O   . ASP   A 1 408 ? 3.075   49.058  69.409  1.00 109.98 ?  530 ASP   A O   1 
ATOM   2863 C CB  . ASP   A 1 408 ? 4.841   48.250  66.862  1.00 105.01 ?  530 ASP   A CB  1 
ATOM   2864 C CG  . ASP   A 1 408 ? 6.334   48.442  66.886  1.00 111.64 ?  530 ASP   A CG  1 
ATOM   2865 O OD1 . ASP   A 1 408 ? 6.965   48.196  67.944  1.00 101.73 ?  530 ASP   A OD1 1 
ATOM   2866 O OD2 . ASP   A 1 408 ? 6.873   48.806  65.827  1.00 116.71 ?  530 ASP   A OD2 1 
ATOM   2867 N N   . TRP   A 1 409 ? 1.910   47.646  68.116  1.00 99.72  ?  531 TRP   A N   1 
ATOM   2868 C CA  . TRP   A 1 409 ? 0.635   48.129  68.633  1.00 96.73  ?  531 TRP   A CA  1 
ATOM   2869 C C   . TRP   A 1 409 ? 0.388   47.647  70.063  1.00 95.93  ?  531 TRP   A C   1 
ATOM   2870 O O   . TRP   A 1 409 ? -0.119  48.393  70.900  1.00 97.92  ?  531 TRP   A O   1 
ATOM   2871 C CB  . TRP   A 1 409 ? -0.472  47.683  67.698  1.00 98.46  ?  531 TRP   A CB  1 
ATOM   2872 C CG  . TRP   A 1 409 ? -1.852  48.057  68.066  1.00 93.69  ?  531 TRP   A CG  1 
ATOM   2873 C CD1 . TRP   A 1 409 ? -2.631  48.989  67.453  1.00 91.90  ?  531 TRP   A CD1 1 
ATOM   2874 C CD2 . TRP   A 1 409 ? -2.659  47.469  69.099  1.00 93.13  ?  531 TRP   A CD2 1 
ATOM   2875 N NE1 . TRP   A 1 409 ? -3.875  49.027  68.041  1.00 90.57  ?  531 TRP   A NE1 1 
ATOM   2876 C CE2 . TRP   A 1 409 ? -3.916  48.112  69.059  1.00 90.66  ?  531 TRP   A CE2 1 
ATOM   2877 C CE3 . TRP   A 1 409 ? -2.439  46.470  70.057  1.00 92.91  ?  531 TRP   A CE3 1 
ATOM   2878 C CZ2 . TRP   A 1 409 ? -4.946  47.796  69.943  1.00 88.24  ?  531 TRP   A CZ2 1 
ATOM   2879 C CZ3 . TRP   A 1 409 ? -3.456  46.157  70.930  1.00 94.18  ?  531 TRP   A CZ3 1 
ATOM   2880 C CH2 . TRP   A 1 409 ? -4.701  46.816  70.866  1.00 91.94  ?  531 TRP   A CH2 1 
ATOM   2881 N N   . HIS   A 1 410 ? 0.730   46.409  70.376  1.00 101.91 ?  532 HIS   A N   1 
ATOM   2882 C CA  . HIS   A 1 410 ? 0.622   45.998  71.776  1.00 107.25 ?  532 HIS   A CA  1 
ATOM   2883 C C   . HIS   A 1 410 ? 1.587   46.741  72.697  1.00 100.28 ?  532 HIS   A C   1 
ATOM   2884 O O   . HIS   A 1 410 ? 1.470   46.614  73.918  1.00 98.60  ?  532 HIS   A O   1 
ATOM   2885 C CB  . HIS   A 1 410 ? 0.854   44.490  71.900  1.00 108.85 ?  532 HIS   A CB  1 
ATOM   2886 C CG  . HIS   A 1 410 ? -0.312  43.677  71.454  1.00 107.14 ?  532 HIS   A CG  1 
ATOM   2887 N ND1 . HIS   A 1 410 ? -1.442  43.522  72.221  1.00 108.43 ?  532 HIS   A ND1 1 
ATOM   2888 C CD2 . HIS   A 1 410 ? -0.551  43.023  70.292  1.00 117.18 ?  532 HIS   A CD2 1 
ATOM   2889 C CE1 . HIS   A 1 410 ? -2.314  42.772  71.568  1.00 119.78 ?  532 HIS   A CE1 1 
ATOM   2890 N NE2 . HIS   A 1 410 ? -1.796  42.452  70.395  1.00 122.93 ?  532 HIS   A NE2 1 
ATOM   2891 N N   . PHE   A 1 411 ? 2.557   47.466  72.155  1.00 94.98  ?  533 PHE   A N   1 
ATOM   2892 C CA  . PHE   A 1 411 ? 3.367   48.338  72.981  1.00 94.12  ?  533 PHE   A CA  1 
ATOM   2893 C C   . PHE   A 1 411 ? 2.734   49.707  73.102  1.00 97.20  ?  533 PHE   A C   1 
ATOM   2894 O O   . PHE   A 1 411 ? 2.719   50.289  74.191  1.00 100.21 ?  533 PHE   A O   1 
ATOM   2895 C CB  . PHE   A 1 411 ? 4.773   48.453  72.412  1.00 95.09  ?  533 PHE   A CB  1 
ATOM   2896 C CG  . PHE   A 1 411 ? 5.598   47.230  72.619  1.00 99.74  ?  533 PHE   A CG  1 
ATOM   2897 C CD1 . PHE   A 1 411 ? 5.559   46.556  73.833  1.00 99.77  ?  533 PHE   A CD1 1 
ATOM   2898 C CD2 . PHE   A 1 411 ? 6.431   46.755  71.619  1.00 102.02 ?  533 PHE   A CD2 1 
ATOM   2899 C CE1 . PHE   A 1 411 ? 6.339   45.428  74.051  1.00 95.26  ?  533 PHE   A CE1 1 
ATOM   2900 C CE2 . PHE   A 1 411 ? 7.213   45.624  71.829  1.00 100.23 ?  533 PHE   A CE2 1 
ATOM   2901 C CZ  . PHE   A 1 411 ? 7.166   44.963  73.048  1.00 94.29  ?  533 PHE   A CZ  1 
ATOM   2902 N N   . ALA   A 1 412 ? 2.175   50.211  72.006  1.00 96.07  ?  534 ALA   A N   1 
ATOM   2903 C CA  . ALA   A 1 412 ? 1.400   51.436  72.075  1.00 93.74  ?  534 ALA   A CA  1 
ATOM   2904 C C   . ALA   A 1 412 ? 0.223   51.319  73.032  1.00 94.33  ?  534 ALA   A C   1 
ATOM   2905 O O   . ALA   A 1 412 ? -0.302  52.343  73.463  1.00 103.54 ?  534 ALA   A O   1 
ATOM   2906 C CB  . ALA   A 1 412 ? 0.910   51.835  70.690  1.00 91.68  ?  534 ALA   A CB  1 
ATOM   2907 N N   . ASN   A 1 413 ? -0.196  50.120  73.408  1.00 91.69  ?  535 ASN   A N   1 
ATOM   2908 C CA  . ASN   A 1 413 ? -1.202  50.093  74.458  1.00 94.48  ?  535 ASN   A CA  1 
ATOM   2909 C C   . ASN   A 1 413 ? -0.602  50.281  75.852  1.00 99.33  ?  535 ASN   A C   1 
ATOM   2910 O O   . ASN   A 1 413 ? -1.248  50.901  76.704  1.00 105.46 ?  535 ASN   A O   1 
ATOM   2911 C CB  . ASN   A 1 413 ? -2.032  48.814  74.431  1.00 101.64 ?  535 ASN   A CB  1 
ATOM   2912 C CG  . ASN   A 1 413 ? -3.498  49.107  74.656  1.00 100.07 ?  535 ASN   A CG  1 
ATOM   2913 O OD1 . ASN   A 1 413 ? -3.945  50.211  74.352  1.00 99.51  ?  535 ASN   A OD1 1 
ATOM   2914 N ND2 . ASN   A 1 413 ? -4.227  48.178  75.280  1.00 87.43  ?  535 ASN   A ND2 1 
ATOM   2915 N N   . LEU   A 1 414 ? 0.586   49.723  76.144  1.00 96.07  ?  536 LEU   A N   1 
ATOM   2916 C CA  . LEU   A 1 414 ? 1.301   50.173  77.341  1.00 93.23  ?  536 LEU   A CA  1 
ATOM   2917 C C   . LEU   A 1 414 ? 1.536   51.663  77.318  1.00 99.75  ?  536 LEU   A C   1 
ATOM   2918 O O   . LEU   A 1 414 ? 1.326   52.348  78.325  1.00 106.11 ?  536 LEU   A O   1 
ATOM   2919 C CB  . LEU   A 1 414 ? 2.624   49.458  77.528  1.00 84.45  ?  536 LEU   A CB  1 
ATOM   2920 C CG  . LEU   A 1 414 ? 2.497   48.564  78.734  1.00 88.72  ?  536 LEU   A CG  1 
ATOM   2921 C CD1 . LEU   A 1 414 ? 1.420   47.533  78.593  1.00 104.32 ?  536 LEU   A CD1 1 
ATOM   2922 C CD2 . LEU   A 1 414 ? 3.843   47.923  78.919  1.00 91.48  ?  536 LEU   A CD2 1 
ATOM   2923 N N   . GLU   A 1 415 ? 1.949   52.195  76.179  1.00 92.25  ?  537 GLU   A N   1 
ATOM   2924 C CA  . GLU   A 1 415 ? 2.167   53.621  76.142  1.00 91.86  ?  537 GLU   A CA  1 
ATOM   2925 C C   . GLU   A 1 415 ? 0.869   54.393  76.337  1.00 97.57  ?  537 GLU   A C   1 
ATOM   2926 O O   . GLU   A 1 415 ? 0.907   55.577  76.686  1.00 105.55 ?  537 GLU   A O   1 
ATOM   2927 C CB  . GLU   A 1 415 ? 2.886   53.958  74.849  1.00 91.21  ?  537 GLU   A CB  1 
ATOM   2928 C CG  . GLU   A 1 415 ? 4.049   53.023  74.707  1.00 92.75  ?  537 GLU   A CG  1 
ATOM   2929 C CD  . GLU   A 1 415 ? 5.131   53.488  73.764  1.00 97.23  ?  537 GLU   A CD  1 
ATOM   2930 O OE1 . GLU   A 1 415 ? 4.840   53.845  72.599  1.00 95.74  ?  537 GLU   A OE1 1 
ATOM   2931 O OE2 . GLU   A 1 415 ? 6.304   53.468  74.206  1.00 99.94  ?  537 GLU   A OE2 1 
ATOM   2932 N N   . PHE   A 1 416 ? -0.284  53.751  76.179  1.00 95.71  ?  538 PHE   A N   1 
ATOM   2933 C CA  . PHE   A 1 416 ? -1.516  54.430  76.567  1.00 95.89  ?  538 PHE   A CA  1 
ATOM   2934 C C   . PHE   A 1 416 ? -1.965  54.400  78.032  1.00 100.45 ?  538 PHE   A C   1 
ATOM   2935 O O   . PHE   A 1 416 ? -2.396  55.423  78.564  1.00 105.43 ?  538 PHE   A O   1 
ATOM   2936 C CB  . PHE   A 1 416 ? -2.699  53.861  75.778  1.00 97.45  ?  538 PHE   A CB  1 
ATOM   2937 C CG  . PHE   A 1 416 ? -4.011  54.044  76.439  1.00 103.30 ?  538 PHE   A CG  1 
ATOM   2938 C CD1 . PHE   A 1 416 ? -4.631  55.269  76.422  1.00 101.68 ?  538 PHE   A CD1 1 
ATOM   2939 C CD2 . PHE   A 1 416 ? -4.647  52.973  77.061  1.00 108.46 ?  538 PHE   A CD2 1 
ATOM   2940 C CE1 . PHE   A 1 416 ? -5.864  55.431  77.050  1.00 117.18 ?  538 PHE   A CE1 1 
ATOM   2941 C CE2 . PHE   A 1 416 ? -5.880  53.126  77.692  1.00 113.74 ?  538 PHE   A CE2 1 
ATOM   2942 C CZ  . PHE   A 1 416 ? -6.495  54.348  77.682  1.00 119.15 ?  538 PHE   A CZ  1 
ATOM   2943 N N   . ALA   A 1 417 ? -1.793  53.282  78.742  1.00 101.43 ?  539 ALA   A N   1 
ATOM   2944 C CA  . ALA   A 1 417 ? -2.402  53.185  80.074  1.00 107.13 ?  539 ALA   A CA  1 
ATOM   2945 C C   . ALA   A 1 417 ? -1.179  53.440  80.959  1.00 108.92 ?  539 ALA   A C   1 
ATOM   2946 O O   . ALA   A 1 417 ? -1.205  53.127  82.153  1.00 114.61 ?  539 ALA   A O   1 
ATOM   2947 C CB  . ALA   A 1 417 ? -2.966  51.823  80.488  1.00 113.11 ?  539 ALA   A CB  1 
ATOM   2948 N N   . ASN   A 1 418 ? -0.116  54.030  80.398  1.00 100.48 ?  540 ASN   A N   1 
ATOM   2949 C CA  . ASN   A 1 418 ? 0.971   54.601  81.188  1.00 98.79  ?  540 ASN   A CA  1 
ATOM   2950 C C   . ASN   A 1 418 ? 1.219   56.034  80.752  1.00 97.59  ?  540 ASN   A C   1 
ATOM   2951 O O   . ASN   A 1 418 ? 1.852   56.782  81.501  1.00 97.75  ?  540 ASN   A O   1 
ATOM   2952 C CB  . ASN   A 1 418 ? 2.294   53.840  81.074  1.00 92.60  ?  540 ASN   A CB  1 
ATOM   2953 C CG  . ASN   A 1 418 ? 2.290   52.588  81.866  1.00 95.33  ?  540 ASN   A CG  1 
ATOM   2954 O OD1 . ASN   A 1 418 ? 2.429   52.599  83.082  1.00 100.04 ?  540 ASN   A OD1 1 
ATOM   2955 N ND2 . ASN   A 1 418 ? 2.034   51.493  81.195  1.00 104.06 ?  540 ASN   A ND2 1 
ATOM   2956 N N   . ALA   A 1 419 ? 0.769   56.422  79.561  1.00 99.40  ?  541 ALA   A N   1 
ATOM   2957 C CA  . ALA   A 1 419 ? 0.890   57.796  79.056  1.00 99.05  ?  541 ALA   A CA  1 
ATOM   2958 C C   . ALA   A 1 419 ? 2.345   58.216  78.872  1.00 93.27  ?  541 ALA   A C   1 
ATOM   2959 O O   . ALA   A 1 419 ? 2.688   59.382  79.043  1.00 92.80  ?  541 ALA   A O   1 
ATOM   2960 C CB  . ALA   A 1 419 ? 0.149   58.796  79.957  1.00 93.19  ?  541 ALA   A CB  1 
ATOM   2961 N N   . THR   A 1 420 ? 3.221   57.287  78.509  1.00 91.20  ?  542 THR   A N   1 
ATOM   2962 C CA  . THR   A 1 420 ? 4.621   57.648  78.348  1.00 88.73  ?  542 THR   A CA  1 
ATOM   2963 C C   . THR   A 1 420 ? 5.317   56.632  77.455  1.00 85.16  ?  542 THR   A C   1 
ATOM   2964 O O   . THR   A 1 420 ? 4.867   55.487  77.351  1.00 82.85  ?  542 THR   A O   1 
ATOM   2965 C CB  . THR   A 1 420 ? 5.319   57.745  79.709  1.00 86.63  ?  542 THR   A CB  1 
ATOM   2966 O OG1 . THR   A 1 420 ? 6.652   58.246  79.544  1.00 84.63  ?  542 THR   A OG1 1 
ATOM   2967 C CG2 . THR   A 1 420 ? 5.349   56.398  80.392  1.00 88.60  ?  542 THR   A CG2 1 
ATOM   2968 N N   . PRO   A 1 421 ? 6.363   57.039  76.748  1.00 84.94  ?  543 PRO   A N   1 
ATOM   2969 C CA  . PRO   A 1 421 ? 7.187   56.072  76.016  1.00 88.67  ?  543 PRO   A CA  1 
ATOM   2970 C C   . PRO   A 1 421 ? 7.844   55.067  76.947  1.00 87.62  ?  543 PRO   A C   1 
ATOM   2971 O O   . PRO   A 1 421 ? 8.508   55.443  77.915  1.00 87.37  ?  543 PRO   A O   1 
ATOM   2972 C CB  . PRO   A 1 421 ? 8.227   56.957  75.321  1.00 90.98  ?  543 PRO   A CB  1 
ATOM   2973 C CG  . PRO   A 1 421 ? 7.695   58.349  75.385  1.00 85.44  ?  543 PRO   A CG  1 
ATOM   2974 C CD  . PRO   A 1 421 ? 6.426   58.376  76.146  1.00 86.20  ?  543 PRO   A CD  1 
ATOM   2975 N N   . LEU   A 1 422 ? 7.695   53.776  76.622  1.00 86.80  ?  544 LEU   A N   1 
ATOM   2976 C CA  . LEU   A 1 422 ? 8.159   52.736  77.535  1.00 89.59  ?  544 LEU   A CA  1 
ATOM   2977 C C   . LEU   A 1 422 ? 9.631   52.900  77.878  1.00 91.45  ?  544 LEU   A C   1 
ATOM   2978 O O   . LEU   A 1 422 ? 10.128  52.267  78.813  1.00 90.97  ?  544 LEU   A O   1 
ATOM   2979 C CB  . LEU   A 1 422 ? 7.894   51.339  76.974  1.00 87.14  ?  544 LEU   A CB  1 
ATOM   2980 C CG  . LEU   A 1 422 ? 6.469   51.169  76.468  1.00 89.10  ?  544 LEU   A CG  1 
ATOM   2981 C CD1 . LEU   A 1 422 ? 6.244   49.768  75.975  1.00 96.72  ?  544 LEU   A CD1 1 
ATOM   2982 C CD2 . LEU   A 1 422 ? 5.484   51.468  77.552  1.00 86.91  ?  544 LEU   A CD2 1 
ATOM   2983 N N   . SER   A 1 423 ? 10.320  53.777  77.156  1.00 89.66  ?  545 SER   A N   1 
ATOM   2984 C CA  . SER   A 1 423 ? 11.725  54.047  77.397  1.00 88.16  ?  545 SER   A CA  1 
ATOM   2985 C C   . SER   A 1 423 ? 11.966  54.918  78.610  1.00 87.19  ?  545 SER   A C   1 
ATOM   2986 O O   . SER   A 1 423 ? 13.134  55.113  78.968  1.00 83.90  ?  545 SER   A O   1 
ATOM   2987 C CB  . SER   A 1 423 ? 12.321  54.708  76.165  1.00 92.47  ?  545 SER   A CB  1 
ATOM   2988 O OG  . SER   A 1 423 ? 11.829  56.029  76.043  1.00 93.91  ?  545 SER   A OG  1 
ATOM   2989 N N   . THR   A 1 424 ? 10.894  55.452  79.220  1.00 91.52  ?  546 THR   A N   1 
ATOM   2990 C CA  . THR   A 1 424 ? 10.960  56.281  80.425  1.00 91.90  ?  546 THR   A CA  1 
ATOM   2991 C C   . THR   A 1 424 ? 10.392  55.614  81.674  1.00 94.12  ?  546 THR   A C   1 
ATOM   2992 O O   . THR   A 1 424 ? 10.830  55.967  82.776  1.00 93.33  ?  546 THR   A O   1 
ATOM   2993 C CB  . THR   A 1 424 ? 10.228  57.619  80.224  1.00 84.95  ?  546 THR   A CB  1 
ATOM   2994 O OG1 . THR   A 1 424 ? 8.814   57.407  80.188  1.00 81.40  ?  546 THR   A OG1 1 
ATOM   2995 C CG2 . THR   A 1 424 ? 10.654  58.252  78.925  1.00 87.09  ?  546 THR   A CG2 1 
ATOM   2996 N N   . LEU   A 1 425 ? 9.433   54.671  81.540  1.00 90.33  ?  547 LEU   A N   1 
ATOM   2997 C CA  . LEU   A 1 425 ? 8.942   53.916  82.695  1.00 85.50  ?  547 LEU   A CA  1 
ATOM   2998 C C   . LEU   A 1 425 ? 10.086  53.183  83.382  1.00 86.33  ?  547 LEU   A C   1 
ATOM   2999 O O   . LEU   A 1 425 ? 10.997  52.678  82.731  1.00 88.10  ?  547 LEU   A O   1 
ATOM   3000 C CB  . LEU   A 1 425 ? 7.868   52.910  82.291  1.00 78.97  ?  547 LEU   A CB  1 
ATOM   3001 C CG  . LEU   A 1 425 ? 6.494   53.453  81.944  1.00 77.13  ?  547 LEU   A CG  1 
ATOM   3002 C CD1 . LEU   A 1 425 ? 5.728   52.524  81.068  1.00 80.03  ?  547 LEU   A CD1 1 
ATOM   3003 C CD2 . LEU   A 1 425 ? 5.762   53.641  83.199  1.00 86.59  ?  547 LEU   A CD2 1 
ATOM   3004 N N   . SER   A 1 426 ? 10.056  53.137  84.707  1.00 87.72  ?  548 SER   A N   1 
ATOM   3005 C CA  . SER   A 1 426 ? 11.103  52.437  85.437  1.00 89.83  ?  548 SER   A CA  1 
ATOM   3006 C C   . SER   A 1 426 ? 10.895  50.942  85.309  1.00 95.72  ?  548 SER   A C   1 
ATOM   3007 O O   . SER   A 1 426 ? 9.766   50.451  85.404  1.00 97.38  ?  548 SER   A O   1 
ATOM   3008 C CB  . SER   A 1 426 ? 11.100  52.816  86.912  1.00 86.35  ?  548 SER   A CB  1 
ATOM   3009 O OG  . SER   A 1 426 ? 12.041  52.041  87.621  1.00 85.12  ?  548 SER   A OG  1 
ATOM   3010 N N   . LEU   A 1 427 ? 11.982  50.204  85.094  1.00 91.93  ?  549 LEU   A N   1 
ATOM   3011 C CA  . LEU   A 1 427 ? 11.807  48.764  84.993  1.00 93.72  ?  549 LEU   A CA  1 
ATOM   3012 C C   . LEU   A 1 427 ? 11.372  48.178  86.329  1.00 96.84  ?  549 LEU   A C   1 
ATOM   3013 O O   . LEU   A 1 427 ? 10.356  47.479  86.395  1.00 101.69 ?  549 LEU   A O   1 
ATOM   3014 C CB  . LEU   A 1 427 ? 13.076  48.089  84.491  1.00 100.76 ?  549 LEU   A CB  1 
ATOM   3015 C CG  . LEU   A 1 427 ? 13.013  46.566  84.580  1.00 94.09  ?  549 LEU   A CG  1 
ATOM   3016 C CD1 . LEU   A 1 427 ? 12.018  46.005  83.586  1.00 94.12  ?  549 LEU   A CD1 1 
ATOM   3017 C CD2 . LEU   A 1 427 ? 14.373  46.049  84.311  1.00 91.66  ?  549 LEU   A CD2 1 
ATOM   3018 N N   . LYS   A 1 428 ? 12.104  48.471  87.416  1.00 90.20  ?  550 LYS   A N   1 
ATOM   3019 C CA  . LYS   A 1 428 ? 11.752  47.824  88.675  1.00 95.81  ?  550 LYS   A CA  1 
ATOM   3020 C C   . LYS   A 1 428 ? 10.393  48.267  89.221  1.00 98.40  ?  550 LYS   A C   1 
ATOM   3021 O O   . LYS   A 1 428 ? 9.798   47.539  90.029  1.00 101.46 ?  550 LYS   A O   1 
ATOM   3022 C CB  . LYS   A 1 428 ? 12.848  48.016  89.737  1.00 95.98  ?  550 LYS   A CB  1 
ATOM   3023 C CG  . LYS   A 1 428 ? 12.784  46.878  90.811  1.00 110.19 ?  550 LYS   A CG  1 
ATOM   3024 C CD  . LYS   A 1 428 ? 13.749  46.929  92.032  1.00 120.00 ?  550 LYS   A CD  1 
ATOM   3025 C CE  . LYS   A 1 428 ? 15.247  46.923  91.680  1.00 126.01 ?  550 LYS   A CE  1 
ATOM   3026 N NZ  . LYS   A 1 428 ? 16.181  46.712  92.856  1.00 118.48 ?  550 LYS   A NZ  1 
ATOM   3027 N N   . HIS   A 1 429 ? 9.846   49.392  88.758  1.00 96.54  ?  551 HIS   A N   1 
ATOM   3028 C CA  . HIS   A 1 429 ? 8.733   50.015  89.472  1.00 99.05  ?  551 HIS   A CA  1 
ATOM   3029 C C   . HIS   A 1 429 ? 7.526   50.419  88.640  1.00 97.03  ?  551 HIS   A C   1 
ATOM   3030 O O   . HIS   A 1 429 ? 6.503   50.800  89.227  1.00 92.99  ?  551 HIS   A O   1 
ATOM   3031 C CB  . HIS   A 1 429 ? 9.242   51.245  90.220  1.00 90.14  ?  551 HIS   A CB  1 
ATOM   3032 C CG  . HIS   A 1 429 ? 10.045  50.897  91.420  1.00 88.01  ?  551 HIS   A CG  1 
ATOM   3033 N ND1 . HIS   A 1 429 ? 11.420  50.846  91.403  1.00 90.72  ?  551 HIS   A ND1 1 
ATOM   3034 C CD2 . HIS   A 1 429 ? 9.670   50.619  92.687  1.00 91.18  ?  551 HIS   A CD2 1 
ATOM   3035 C CE1 . HIS   A 1 429 ? 11.863  50.517  92.601  1.00 93.41  ?  551 HIS   A CE1 1 
ATOM   3036 N NE2 . HIS   A 1 429 ? 10.820  50.386  93.402  1.00 104.42 ?  551 HIS   A NE2 1 
ATOM   3037 N N   . TRP   A 1 430 ? 7.599   50.271  87.339  1.00 94.87  ?  552 TRP   A N   1 
ATOM   3038 C CA  . TRP   A 1 430 ? 6.516   50.741  86.458  1.00 94.32  ?  552 TRP   A CA  1 
ATOM   3039 C C   . TRP   A 1 430 ? 5.156   50.275  86.930  1.00 97.91  ?  552 TRP   A C   1 
ATOM   3040 O O   . TRP   A 1 430 ? 4.226   51.064  86.923  1.00 100.72 ?  552 TRP   A O   1 
ATOM   3041 C CB  . TRP   A 1 430 ? 6.811   50.209  85.061  1.00 97.70  ?  552 TRP   A CB  1 
ATOM   3042 C CG  . TRP   A 1 430 ? 6.287   48.853  84.720  1.00 100.42 ?  552 TRP   A CG  1 
ATOM   3043 C CD1 . TRP   A 1 430 ? 6.912   47.659  84.909  1.00 99.00  ?  552 TRP   A CD1 1 
ATOM   3044 C CD2 . TRP   A 1 430 ? 5.047   48.558  84.063  1.00 100.78 ?  552 TRP   A CD2 1 
ATOM   3045 N NE1 . TRP   A 1 430 ? 6.130   46.639  84.443  1.00 104.14 ?  552 TRP   A NE1 1 
ATOM   3046 C CE2 . TRP   A 1 430 ? 4.981   47.161  83.918  1.00 99.97  ?  552 TRP   A CE2 1 
ATOM   3047 C CE3 . TRP   A 1 430 ? 3.982   49.333  83.603  1.00 106.63 ?  552 TRP   A CE3 1 
ATOM   3048 C CZ2 . TRP   A 1 430 ? 3.892   46.525  83.334  1.00 110.70 ?  552 TRP   A CZ2 1 
ATOM   3049 C CZ3 . TRP   A 1 430 ? 2.905   48.704  83.024  1.00 109.44 ?  552 TRP   A CZ3 1 
ATOM   3050 C CH2 . TRP   A 1 430 ? 2.862   47.319  82.893  1.00 110.91 ?  552 TRP   A CH2 1 
ATOM   3051 N N   . ASP   A 1 431 ? 5.066   49.042  87.348  1.00 103.86 ?  553 ASP   A N   1 
ATOM   3052 C CA  . ASP   A 1 431 ? 3.781   48.426  87.652  1.00 106.42 ?  553 ASP   A CA  1 
ATOM   3053 C C   . ASP   A 1 431 ? 3.519   48.342  89.145  1.00 112.50 ?  553 ASP   A C   1 
ATOM   3054 O O   . ASP   A 1 431 ? 2.609   47.617  89.545  1.00 121.21 ?  553 ASP   A O   1 
ATOM   3055 C CB  . ASP   A 1 431 ? 3.676   47.004  87.065  1.00 116.52 ?  553 ASP   A CB  1 
ATOM   3056 C CG  . ASP   A 1 431 ? 4.798   46.039  87.560  1.00 122.52 ?  553 ASP   A CG  1 
ATOM   3057 O OD1 . ASP   A 1 431 ? 5.631   46.414  88.442  1.00 116.02 ?  553 ASP   A OD1 1 
ATOM   3058 O OD2 . ASP   A 1 431 ? 4.814   44.875  87.072  1.00 120.83 ?  553 ASP   A OD2 1 
ATOM   3059 N N   . GLN   A 1 432 ? 4.293   49.055  89.981  1.00 112.22 ?  554 GLN   A N   1 
ATOM   3060 C CA  . GLN   A 1 432 ? 4.249   48.830  91.432  1.00 110.81 ?  554 GLN   A CA  1 
ATOM   3061 C C   . GLN   A 1 432 ? 2.843   49.021  92.011  1.00 106.04 ?  554 GLN   A C   1 
ATOM   3062 O O   . GLN   A 1 432 ? 2.493   48.372  93.003  1.00 99.42  ?  554 GLN   A O   1 
ATOM   3063 C CB  . GLN   A 1 432 ? 5.256   49.749  92.131  1.00 108.00 ?  554 GLN   A CB  1 
ATOM   3064 C CG  . GLN   A 1 432 ? 4.970   51.221  91.914  1.00 106.78 ?  554 GLN   A CG  1 
ATOM   3065 C CD  . GLN   A 1 432 ? 4.265   51.877  93.091  1.00 105.16 ?  554 GLN   A CD  1 
ATOM   3066 O OE1 . GLN   A 1 432 ? 4.430   51.476  94.266  1.00 97.18  ?  554 GLN   A OE1 1 
ATOM   3067 N NE2 . GLN   A 1 432 ? 3.397   52.835  92.769  1.00 99.63  ?  554 GLN   A NE2 1 
ATOM   3068 N N   . ASP   A 1 433 ? 2.011   49.865  91.387  1.00 107.72 ?  555 ASP   A N   1 
ATOM   3069 C CA  . ASP   A 1 433 ? 0.620   50.023  91.803  1.00 106.50 ?  555 ASP   A CA  1 
ATOM   3070 C C   . ASP   A 1 433 ? -0.313  48.892  91.359  1.00 111.90 ?  555 ASP   A C   1 
ATOM   3071 O O   . ASP   A 1 433 ? -1.511  48.979  91.672  1.00 103.63 ?  555 ASP   A O   1 
ATOM   3072 C CB  . ASP   A 1 433 ? 0.054   51.386  91.336  1.00 110.50 ?  555 ASP   A CB  1 
ATOM   3073 C CG  . ASP   A 1 433 ? -0.015  51.552  89.811  1.00 114.45 ?  555 ASP   A CG  1 
ATOM   3074 O OD1 . ASP   A 1 433 ? 1.039   51.427  89.163  1.00 115.62 ?  555 ASP   A OD1 1 
ATOM   3075 O OD2 . ASP   A 1 433 ? -1.112  51.846  89.270  1.00 113.12 ?  555 ASP   A OD2 1 
ATOM   3076 N N   . ASP   A 1 434 ? 0.219   47.801  90.839  1.00 122.97 ?  556 ASP   A N   1 
ATOM   3077 C CA  . ASP   A 1 434 ? -0.695  46.761  90.308  1.00 123.92 ?  556 ASP   A CA  1 
ATOM   3078 C C   . ASP   A 1 434 ? -1.322  45.958  91.433  1.00 116.60 ?  556 ASP   A C   1 
ATOM   3079 O O   . ASP   A 1 434 ? -2.476  45.569  91.304  1.00 116.35 ?  556 ASP   A O   1 
ATOM   3080 C CB  . ASP   A 1 434 ? 0.060   45.801  89.391  1.00 123.01 ?  556 ASP   A CB  1 
ATOM   3081 C CG  . ASP   A 1 434 ? -0.825  44.949  88.504  1.00 134.53 ?  556 ASP   A CG  1 
ATOM   3082 O OD1 . ASP   A 1 434 ? -1.250  45.451  87.449  1.00 140.60 ?  556 ASP   A OD1 1 
ATOM   3083 O OD2 . ASP   A 1 434 ? -1.063  43.785  88.868  1.00 134.27 ?  556 ASP   A OD2 1 
ATOM   3084 N N   . ASP   A 1 435 ? -0.608  45.772  92.521  1.00 109.33 ?  557 ASP   A N   1 
ATOM   3085 C CA  . ASP   A 1 435 ? -1.090  44.850  93.527  1.00 111.97 ?  557 ASP   A CA  1 
ATOM   3086 C C   . ASP   A 1 435 ? -2.426  45.265  94.133  1.00 112.94 ?  557 ASP   A C   1 
ATOM   3087 O O   . ASP   A 1 435 ? -3.070  44.446  94.799  1.00 115.53 ?  557 ASP   A O   1 
ATOM   3088 C CB  . ASP   A 1 435 ? 0.001   44.728  94.572  1.00 113.02 ?  557 ASP   A CB  1 
ATOM   3089 C CG  . ASP   A 1 435 ? 1.106   43.808  94.121  1.00 131.17 ?  557 ASP   A CG  1 
ATOM   3090 O OD1 . ASP   A 1 435 ? 0.902   43.091  93.110  1.00 135.00 ?  557 ASP   A OD1 1 
ATOM   3091 O OD2 . ASP   A 1 435 ? 2.190   43.832  94.743  1.00 140.09 ?  557 ASP   A OD2 1 
ATOM   3092 N N   . PHE   A 1 436 ? -2.884  46.489  93.875  1.00 110.79 ?  558 PHE   A N   1 
ATOM   3093 C CA  . PHE   A 1 436 ? -4.006  47.068  94.592  1.00 104.66 ?  558 PHE   A CA  1 
ATOM   3094 C C   . PHE   A 1 436 ? -5.228  47.246  93.713  1.00 108.88 ?  558 PHE   A C   1 
ATOM   3095 O O   . PHE   A 1 436 ? -6.117  48.026  94.080  1.00 109.17 ?  558 PHE   A O   1 
ATOM   3096 C CB  . PHE   A 1 436 ? -3.604  48.420  95.180  1.00 98.79  ?  558 PHE   A CB  1 
ATOM   3097 C CG  . PHE   A 1 436 ? -2.354  48.376  96.030  1.00 101.22 ?  558 PHE   A CG  1 
ATOM   3098 C CD1 . PHE   A 1 436 ? -2.400  47.989  97.351  1.00 104.64 ?  558 PHE   A CD1 1 
ATOM   3099 C CD2 . PHE   A 1 436 ? -1.127  48.729  95.508  1.00 103.17 ?  558 PHE   A CD2 1 
ATOM   3100 C CE1 . PHE   A 1 436 ? -1.234  47.958  98.128  1.00 99.91  ?  558 PHE   A CE1 1 
ATOM   3101 C CE2 . PHE   A 1 436 ? 0.038   48.695  96.294  1.00 94.76  ?  558 PHE   A CE2 1 
ATOM   3102 C CZ  . PHE   A 1 436 ? -0.021  48.312  97.586  1.00 89.19  ?  558 PHE   A CZ  1 
ATOM   3103 N N   . GLU   A 1 437 ? -5.304  46.566  92.559  1.00 105.34 ?  559 GLU   A N   1 
ATOM   3104 C CA  . GLU   A 1 437 ? -6.302  47.014  91.600  1.00 108.20 ?  559 GLU   A CA  1 
ATOM   3105 C C   . GLU   A 1 437 ? -7.674  46.480  91.962  1.00 100.23 ?  559 GLU   A C   1 
ATOM   3106 O O   . GLU   A 1 437 ? -7.824  45.426  92.575  1.00 92.30  ?  559 GLU   A O   1 
ATOM   3107 C CB  . GLU   A 1 437 ? -6.000  46.643  90.146  1.00 105.98 ?  559 GLU   A CB  1 
ATOM   3108 C CG  . GLU   A 1 437 ? -6.649  47.746  89.263  1.00 119.02 ?  559 GLU   A CG  1 
ATOM   3109 C CD  . GLU   A 1 437 ? -6.584  47.562  87.762  1.00 127.02 ?  559 GLU   A CD  1 
ATOM   3110 O OE1 . GLU   A 1 437 ? -6.371  46.418  87.306  1.00 125.56 ?  559 GLU   A OE1 1 
ATOM   3111 O OE2 . GLU   A 1 437 ? -6.680  48.604  87.048  1.00 132.93 ?  559 GLU   A OE2 1 
ATOM   3112 N N   . PHE   A 1 438 ? -8.680  47.249  91.592  1.00 104.57 ?  560 PHE   A N   1 
ATOM   3113 C CA  . PHE   A 1 438 ? -10.043 46.920  91.954  1.00 103.89 ?  560 PHE   A CA  1 
ATOM   3114 C C   . PHE   A 1 438 ? -10.559 45.769  91.099  1.00 111.84 ?  560 PHE   A C   1 
ATOM   3115 O O   . PHE   A 1 438 ? -10.414 45.781  89.868  1.00 116.63 ?  560 PHE   A O   1 
ATOM   3116 C CB  . PHE   A 1 438 ? -10.931 48.138  91.766  1.00 105.38 ?  560 PHE   A CB  1 
ATOM   3117 C CG  . PHE   A 1 438 ? -10.532 49.333  92.580  1.00 105.28 ?  560 PHE   A CG  1 
ATOM   3118 C CD1 . PHE   A 1 438 ? -10.011 49.183  93.856  1.00 104.73 ?  560 PHE   A CD1 1 
ATOM   3119 C CD2 . PHE   A 1 438 ? -10.729 50.610  92.083  1.00 99.28  ?  560 PHE   A CD2 1 
ATOM   3120 C CE1 . PHE   A 1 438 ? -9.670  50.275  94.601  1.00 98.89  ?  560 PHE   A CE1 1 
ATOM   3121 C CE2 . PHE   A 1 438 ? -10.394 51.710  92.823  1.00 96.24  ?  560 PHE   A CE2 1 
ATOM   3122 C CZ  . PHE   A 1 438 ? -9.868  51.547  94.079  1.00 99.15  ?  560 PHE   A CZ  1 
ATOM   3123 N N   . THR   A 1 439 ? -11.198 44.798  91.759  1.00 110.83 ?  561 THR   A N   1 
ATOM   3124 C CA  . THR   A 1 439 ? -11.780 43.632  91.100  1.00 99.76  ?  561 THR   A CA  1 
ATOM   3125 C C   . THR   A 1 439 ? -13.103 44.007  90.429  1.00 101.06 ?  561 THR   A C   1 
ATOM   3126 O O   . THR   A 1 439 ? -14.075 44.378  91.094  1.00 97.91  ?  561 THR   A O   1 
ATOM   3127 C CB  . THR   A 1 439 ? -11.989 42.509  92.116  1.00 97.92  ?  561 THR   A CB  1 
ATOM   3128 O OG1 . THR   A 1 439 ? -13.200 42.718  92.856  1.00 96.45  ?  561 THR   A OG1 1 
ATOM   3129 C CG2 . THR   A 1 439 ? -10.821 42.455  93.094  1.00 100.39 ?  561 THR   A CG2 1 
ATOM   3130 N N   . GLY   A 1 440 ? -13.151 43.898  89.118  1.00 104.97 ?  562 GLY   A N   1 
ATOM   3131 C CA  . GLY   A 1 440 ? -14.366 44.211  88.401  1.00 104.07 ?  562 GLY   A CA  1 
ATOM   3132 C C   . GLY   A 1 440 ? -14.047 44.559  86.975  1.00 107.17 ?  562 GLY   A C   1 
ATOM   3133 O O   . GLY   A 1 440 ? -12.901 44.840  86.609  1.00 108.38 ?  562 GLY   A O   1 
ATOM   3134 N N   . SER   A 1 441 ? -15.078 44.520  86.145  1.00 109.05 ?  563 SER   A N   1 
ATOM   3135 C CA  . SER   A 1 441 ? -14.892 44.867  84.744  1.00 116.31 ?  563 SER   A CA  1 
ATOM   3136 C C   . SER   A 1 441 ? -14.790 46.384  84.668  1.00 106.96 ?  563 SER   A C   1 
ATOM   3137 O O   . SER   A 1 441 ? -15.603 47.092  85.262  1.00 108.57 ?  563 SER   A O   1 
ATOM   3138 C CB  . SER   A 1 441 ? -16.055 44.340  83.893  1.00 127.00 ?  563 SER   A CB  1 
ATOM   3139 O OG  . SER   A 1 441 ? -16.279 42.942  84.081  1.00 138.66 ?  563 SER   A OG  1 
ATOM   3140 N N   . HIS   A 1 442 ? -13.786 46.889  83.963  1.00 102.00 ?  564 HIS   A N   1 
ATOM   3141 C CA  . HIS   A 1 442 ? -13.708 48.332  83.804  1.00 102.88 ?  564 HIS   A CA  1 
ATOM   3142 C C   . HIS   A 1 442 ? -14.978 48.843  83.115  1.00 106.17 ?  564 HIS   A C   1 
ATOM   3143 O O   . HIS   A 1 442 ? -15.717 48.090  82.483  1.00 113.51 ?  564 HIS   A O   1 
ATOM   3144 C CB  . HIS   A 1 442 ? -12.426 48.705  83.057  1.00 104.36 ?  564 HIS   A CB  1 
ATOM   3145 C CG  . HIS   A 1 442 ? -11.183 48.336  83.808  1.00 104.19 ?  564 HIS   A CG  1 
ATOM   3146 N ND1 . HIS   A 1 442 ? -9.938  48.299  83.208  1.00 106.52 ?  564 HIS   A ND1 1 
ATOM   3147 C CD2 . HIS   A 1 442 ? -10.993 47.932  85.087  1.00 109.02 ?  564 HIS   A CD2 1 
ATOM   3148 C CE1 . HIS   A 1 442 ? -9.031  47.912  84.089  1.00 105.97 ?  564 HIS   A CE1 1 
ATOM   3149 N NE2 . HIS   A 1 442 ? -9.645  47.678  85.236  1.00 114.20 ?  564 HIS   A NE2 1 
ATOM   3150 N N   . LEU   A 1 443 ? -15.274 50.128  83.304  1.00 104.90 ?  565 LEU   A N   1 
ATOM   3151 C CA  . LEU   A 1 443 ? -16.538 50.697  82.857  1.00 103.01 ?  565 LEU   A CA  1 
ATOM   3152 C C   . LEU   A 1 443 ? -16.303 52.058  82.239  1.00 105.32 ?  565 LEU   A C   1 
ATOM   3153 O O   . LEU   A 1 443 ? -15.230 52.648  82.373  1.00 106.00 ?  565 LEU   A O   1 
ATOM   3154 C CB  . LEU   A 1 443 ? -17.496 50.863  84.027  1.00 99.31  ?  565 LEU   A CB  1 
ATOM   3155 C CG  . LEU   A 1 443 ? -18.012 49.578  84.630  1.00 100.73 ?  565 LEU   A CG  1 
ATOM   3156 C CD1 . LEU   A 1 443 ? -17.396 49.361  85.989  1.00 97.26  ?  565 LEU   A CD1 1 
ATOM   3157 C CD2 . LEU   A 1 443 ? -19.491 49.706  84.737  1.00 109.20 ?  565 LEU   A CD2 1 
ATOM   3158 N N   . THR   A 1 444 ? -17.330 52.567  81.568  1.00 108.82 ?  566 THR   A N   1 
ATOM   3159 C CA  . THR   A 1 444 ? -17.270 53.899  80.990  1.00 113.06 ?  566 THR   A CA  1 
ATOM   3160 C C   . THR   A 1 444 ? -18.491 54.679  81.444  1.00 114.15 ?  566 THR   A C   1 
ATOM   3161 O O   . THR   A 1 444 ? -19.566 54.112  81.662  1.00 113.35 ?  566 THR   A O   1 
ATOM   3162 C CB  . THR   A 1 444 ? -17.173 53.889  79.426  1.00 110.55 ?  566 THR   A CB  1 
ATOM   3163 O OG1 . THR   A 1 444 ? -18.239 53.127  78.836  1.00 109.79 ?  566 THR   A OG1 1 
ATOM   3164 C CG2 . THR   A 1 444 ? -15.835 53.305  79.008  1.00 106.91 ?  566 THR   A CG2 1 
ATOM   3165 N N   . VAL   A 1 445 ? -18.308 55.981  81.618  1.00 113.90 ?  567 VAL   A N   1 
ATOM   3166 C CA  . VAL   A 1 445 ? -19.404 56.853  82.004  1.00 115.26 ?  567 VAL   A CA  1 
ATOM   3167 C C   . VAL   A 1 445 ? -20.074 57.415  80.770  1.00 121.19 ?  567 VAL   A C   1 
ATOM   3168 O O   . VAL   A 1 445 ? -19.458 58.154  79.994  1.00 118.36 ?  567 VAL   A O   1 
ATOM   3169 C CB  . VAL   A 1 445 ? -18.934 57.961  82.935  1.00 112.56 ?  567 VAL   A CB  1 
ATOM   3170 C CG1 . VAL   A 1 445 ? -20.113 58.828  83.283  1.00 118.75 ?  567 VAL   A CG1 1 
ATOM   3171 C CG2 . VAL   A 1 445 ? -18.427 57.290  84.175  1.00 108.62 ?  567 VAL   A CG2 1 
ATOM   3172 N N   . ARG   A 1 446 ? -21.354 57.076  80.620  1.00 126.23 ?  568 ARG   A N   1 
ATOM   3173 C CA  . ARG   A 1 446 ? -22.088 57.308  79.392  1.00 130.75 ?  568 ARG   A CA  1 
ATOM   3174 C C   . ARG   A 1 446 ? -22.671 58.709  79.332  1.00 132.68 ?  568 ARG   A C   1 
ATOM   3175 O O   . ARG   A 1 446 ? -22.741 59.293  78.242  1.00 133.74 ?  568 ARG   A O   1 
ATOM   3176 C CB  . ARG   A 1 446 ? -23.178 56.237  79.238  1.00 133.34 ?  568 ARG   A CB  1 
ATOM   3177 C CG  . ARG   A 1 446 ? -22.831 55.230  78.140  1.00 143.37 ?  568 ARG   A CG  1 
ATOM   3178 C CD  . ARG   A 1 446 ? -24.018 54.752  77.314  1.00 148.28 ?  568 ARG   A CD  1 
ATOM   3179 N NE  . ARG   A 1 446 ? -23.573 53.779  76.323  1.00 152.12 ?  568 ARG   A NE  1 
ATOM   3180 C CZ  . ARG   A 1 446 ? -24.369 53.151  75.470  1.00 159.20 ?  568 ARG   A CZ  1 
ATOM   3181 N NH1 . ARG   A 1 446 ? -25.684 53.282  75.531  1.00 160.78 ?  568 ARG   A NH1 1 
ATOM   3182 N NH2 . ARG   A 1 446 ? -23.831 52.378  74.527  1.00 165.02 ?  568 ARG   A NH2 1 
ATOM   3183 N N   . ASN   A 1 447 ? -23.050 59.275  80.479  1.00 128.62 ?  569 ASN   A N   1 
ATOM   3184 C CA  . ASN   A 1 447 ? -23.529 60.649  80.554  1.00 127.60 ?  569 ASN   A CA  1 
ATOM   3185 C C   . ASN   A 1 447 ? -22.396 61.664  80.723  1.00 124.94 ?  569 ASN   A C   1 
ATOM   3186 O O   . ASN   A 1 447 ? -22.664 62.857  80.912  1.00 121.33 ?  569 ASN   A O   1 
ATOM   3187 C CB  . ASN   A 1 447 ? -24.549 60.785  81.690  1.00 127.91 ?  569 ASN   A CB  1 
ATOM   3188 C CG  . ASN   A 1 447 ? -24.143 60.008  82.927  1.00 129.69 ?  569 ASN   A CG  1 
ATOM   3189 O OD1 . ASN   A 1 447 ? -23.201 59.212  82.876  1.00 127.25 ?  569 ASN   A OD1 1 
ATOM   3190 N ND2 . ASN   A 1 447 ? -24.842 60.237  84.049  1.00 126.74 ?  569 ASN   A ND2 1 
ATOM   3191 N N   . GLY   A 1 448 ? -21.141 61.225  80.634  1.00 122.59 ?  570 GLY   A N   1 
ATOM   3192 C CA  . GLY   A 1 448 ? -20.011 62.123  80.786  1.00 116.08 ?  570 GLY   A CA  1 
ATOM   3193 C C   . GLY   A 1 448 ? -19.502 62.162  82.214  1.00 117.61 ?  570 GLY   A C   1 
ATOM   3194 O O   . GLY   A 1 448 ? -20.261 62.490  83.133  1.00 120.05 ?  570 GLY   A O   1 
ATOM   3195 N N   . TYR   A 1 449 ? -18.223 61.819  82.417  1.00 112.19 ?  571 TYR   A N   1 
ATOM   3196 C CA  . TYR   A 1 449 ? -17.638 61.791  83.760  1.00 106.70 ?  571 TYR   A CA  1 
ATOM   3197 C C   . TYR   A 1 449 ? -17.729 63.138  84.473  1.00 105.71 ?  571 TYR   A C   1 
ATOM   3198 O O   . TYR   A 1 449 ? -17.691 63.167  85.707  1.00 101.38 ?  571 TYR   A O   1 
ATOM   3199 C CB  . TYR   A 1 449 ? -16.173 61.325  83.677  1.00 103.21 ?  571 TYR   A CB  1 
ATOM   3200 C CG  . TYR   A 1 449 ? -15.648 60.480  84.836  1.00 93.45  ?  571 TYR   A CG  1 
ATOM   3201 C CD1 . TYR   A 1 449 ? -15.765 59.139  84.831  1.00 102.02 ?  571 TYR   A CD1 1 
ATOM   3202 C CD2 . TYR   A 1 449 ? -14.952 61.028  85.876  1.00 94.73  ?  571 TYR   A CD2 1 
ATOM   3203 C CE1 . TYR   A 1 449 ? -15.279 58.360  85.866  1.00 102.47 ?  571 TYR   A CE1 1 
ATOM   3204 C CE2 . TYR   A 1 449 ? -14.442 60.239  86.905  1.00 91.36  ?  571 TYR   A CE2 1 
ATOM   3205 C CZ  . TYR   A 1 449 ? -14.613 58.903  86.891  1.00 82.53  ?  571 TYR   A CZ  1 
ATOM   3206 O OH  . TYR   A 1 449 ? -14.122 58.075  87.878  1.00 72.43  ?  571 TYR   A OH  1 
ATOM   3207 N N   . SER   A 1 450 ? -17.857 64.251  83.734  1.00 104.79 ?  572 SER   A N   1 
ATOM   3208 C CA  . SER   A 1 450 ? -17.994 65.554  84.372  1.00 99.12  ?  572 SER   A CA  1 
ATOM   3209 C C   . SER   A 1 450 ? -19.204 65.616  85.284  1.00 101.54 ?  572 SER   A C   1 
ATOM   3210 O O   . SER   A 1 450 ? -19.282 66.502  86.138  1.00 100.82 ?  572 SER   A O   1 
ATOM   3211 C CB  . SER   A 1 450 ? -18.109 66.659  83.333  1.00 99.92  ?  572 SER   A CB  1 
ATOM   3212 O OG  . SER   A 1 450 ? -19.460 66.804  82.926  1.00 103.06 ?  572 SER   A OG  1 
ATOM   3213 N N   . CYS   A 1 451 ? -20.154 64.702  85.133  1.00 106.43 ?  573 CYS   A N   1 
ATOM   3214 C CA  . CYS   A 1 451 ? -21.269 64.679  86.069  1.00 108.73 ?  573 CYS   A CA  1 
ATOM   3215 C C   . CYS   A 1 451 ? -20.809 64.544  87.525  1.00 104.17 ?  573 CYS   A C   1 
ATOM   3216 O O   . CYS   A 1 451 ? -21.531 64.996  88.421  1.00 106.36 ?  573 CYS   A O   1 
ATOM   3217 C CB  . CYS   A 1 451 ? -22.258 63.570  85.654  1.00 112.61 ?  573 CYS   A CB  1 
ATOM   3218 S SG  . CYS   A 1 451 ? -21.960 61.877  86.248  1.00 125.61 ?  573 CYS   A SG  1 
ATOM   3219 N N   . VAL   A 1 452 ? -19.608 64.016  87.779  1.00 101.60 ?  574 VAL   A N   1 
ATOM   3220 C CA  . VAL   A 1 452 ? -19.135 63.694  89.134  1.00 97.17  ?  574 VAL   A CA  1 
ATOM   3221 C C   . VAL   A 1 452 ? -18.423 64.876  89.788  1.00 92.66  ?  574 VAL   A C   1 
ATOM   3222 O O   . VAL   A 1 452 ? -18.654 65.132  90.976  1.00 94.14  ?  574 VAL   A O   1 
ATOM   3223 C CB  . VAL   A 1 452 ? -18.224 62.449  89.137  1.00 97.42  ?  574 VAL   A CB  1 
ATOM   3224 C CG1 . VAL   A 1 452 ? -17.720 62.130  90.526  1.00 84.45  ?  574 VAL   A CG1 1 
ATOM   3225 C CG2 . VAL   A 1 452 ? -18.957 61.251  88.579  1.00 111.15 ?  574 VAL   A CG2 1 
ATOM   3226 N N   . PRO   A 1 453 ? -17.545 65.610  89.106  1.00 89.63  ?  575 PRO   A N   1 
ATOM   3227 C CA  . PRO   A 1 453 ? -17.027 66.824  89.743  1.00 89.89  ?  575 PRO   A CA  1 
ATOM   3228 C C   . PRO   A 1 453 ? -18.110 67.849  89.983  1.00 93.82  ?  575 PRO   A C   1 
ATOM   3229 O O   . PRO   A 1 453 ? -18.186 68.425  91.077  1.00 97.99  ?  575 PRO   A O   1 
ATOM   3230 C CB  . PRO   A 1 453 ? -15.965 67.338  88.762  1.00 90.79  ?  575 PRO   A CB  1 
ATOM   3231 C CG  . PRO   A 1 453 ? -16.054 66.505  87.581  1.00 96.15  ?  575 PRO   A CG  1 
ATOM   3232 C CD  . PRO   A 1 453 ? -16.760 65.248  87.922  1.00 96.91  ?  575 PRO   A CD  1 
ATOM   3233 N N   . VAL   A 1 454 ? -18.962 68.091  88.995  1.00 91.01  ?  576 VAL   A N   1 
ATOM   3234 C CA  . VAL   A 1 454 ? -20.032 69.050  89.201  1.00 91.44  ?  576 VAL   A CA  1 
ATOM   3235 C C   . VAL   A 1 454 ? -20.845 68.678  90.422  1.00 93.70  ?  576 VAL   A C   1 
ATOM   3236 O O   . VAL   A 1 454 ? -21.146 69.529  91.265  1.00 98.64  ?  576 VAL   A O   1 
ATOM   3237 C CB  . VAL   A 1 454 ? -20.910 69.139  87.957  1.00 90.25  ?  576 VAL   A CB  1 
ATOM   3238 C CG1 . VAL   A 1 454 ? -22.115 69.991  88.272  1.00 90.31  ?  576 VAL   A CG1 1 
ATOM   3239 C CG2 . VAL   A 1 454 ? -20.094 69.724  86.843  1.00 88.97  ?  576 VAL   A CG2 1 
ATOM   3240 N N   . ALA   A 1 455 ? -21.180 67.397  90.555  1.00 92.11  ?  577 ALA   A N   1 
ATOM   3241 C CA  . ALA   A 1 455 ? -21.919 66.942  91.727  1.00 96.63  ?  577 ALA   A CA  1 
ATOM   3242 C C   . ALA   A 1 455 ? -21.178 67.262  93.019  1.00 101.22 ?  577 ALA   A C   1 
ATOM   3243 O O   . ALA   A 1 455 ? -21.791 67.701  94.001  1.00 106.52 ?  577 ALA   A O   1 
ATOM   3244 C CB  . ALA   A 1 455 ? -22.182 65.444  91.634  1.00 98.00  ?  577 ALA   A CB  1 
ATOM   3245 N N   . LEU   A 1 456 ? -19.862 67.046  93.045  1.00 99.65  ?  578 LEU   A N   1 
ATOM   3246 C CA  . LEU   A 1 456 ? -19.100 67.326  94.260  1.00 100.75 ?  578 LEU   A CA  1 
ATOM   3247 C C   . LEU   A 1 456 ? -19.035 68.824  94.543  1.00 103.98 ?  578 LEU   A C   1 
ATOM   3248 O O   . LEU   A 1 456 ? -19.331 69.275  95.663  1.00 103.53 ?  578 LEU   A O   1 
ATOM   3249 C CB  . LEU   A 1 456 ? -17.700 66.728  94.147  1.00 90.63  ?  578 LEU   A CB  1 
ATOM   3250 C CG  . LEU   A 1 456 ? -17.683 65.205  94.268  1.00 86.68  ?  578 LEU   A CG  1 
ATOM   3251 C CD1 . LEU   A 1 456 ? -16.305 64.763  94.665  1.00 81.99  ?  578 LEU   A CD1 1 
ATOM   3252 C CD2 . LEU   A 1 456 ? -18.711 64.695  95.268  1.00 87.35  ?  578 LEU   A CD2 1 
ATOM   3253 N N   . ALA   A 1 457 ? -18.689 69.611  93.523  1.00 101.42 ?  579 ALA   A N   1 
ATOM   3254 C CA  . ALA   A 1 457 ? -18.502 71.048  93.646  1.00 103.51 ?  579 ALA   A CA  1 
ATOM   3255 C C   . ALA   A 1 457 ? -19.692 71.685  94.371  1.00 107.63 ?  579 ALA   A C   1 
ATOM   3256 O O   . ALA   A 1 457 ? -19.504 72.583  95.196  1.00 111.95 ?  579 ALA   A O   1 
ATOM   3257 C CB  . ALA   A 1 457 ? -17.987 71.592  92.314  1.00 99.13  ?  579 ALA   A CB  1 
ATOM   3258 N N   . GLU   A 1 458 ? -20.915 71.249  94.097  1.00 109.19 ?  580 GLU   A N   1 
ATOM   3259 C CA  . GLU   A 1 458 ? -22.064 71.827  94.777  1.00 117.15 ?  580 GLU   A CA  1 
ATOM   3260 C C   . GLU   A 1 458 ? -22.050 72.027  96.288  1.00 115.95 ?  580 GLU   A C   1 
ATOM   3261 O O   . GLU   A 1 458 ? -21.896 71.064  97.054  1.00 107.74 ?  580 GLU   A O   1 
ATOM   3262 C CB  . GLU   A 1 458 ? -23.326 71.072  94.385  1.00 122.50 ?  580 GLU   A CB  1 
ATOM   3263 C CG  . GLU   A 1 458 ? -24.563 71.719  94.990  1.00 136.95 ?  580 GLU   A CG  1 
ATOM   3264 C CD  . GLU   A 1 458 ? -25.696 70.742  95.217  1.00 152.29 ?  580 GLU   A CD  1 
ATOM   3265 O OE1 . GLU   A 1 458 ? -25.488 69.773  95.993  1.00 147.96 ?  580 GLU   A OE1 1 
ATOM   3266 O OE2 . GLU   A 1 458 ? -26.781 70.938  94.618  1.00 162.71 ?  580 GLU   A OE2 1 
ATOM   3267 N N   . GLY   A 1 459 ? -22.258 73.277  96.700  1.00 115.58 ?  581 GLY   A N   1 
ATOM   3268 C CA  . GLY   A 1 459 ? -22.229 73.664  98.088  1.00 110.58 ?  581 GLY   A CA  1 
ATOM   3269 C C   . GLY   A 1 459 ? -20.924 74.267  98.530  1.00 109.95 ?  581 GLY   A C   1 
ATOM   3270 O O   . GLY   A 1 459 ? -20.751 74.517  99.730  1.00 114.70 ?  581 GLY   A O   1 
ATOM   3271 N N   . LEU   A 1 460 ? -20.007 74.519  97.603  1.00 103.28 ?  582 LEU   A N   1 
ATOM   3272 C CA  . LEU   A 1 460 ? -18.632 74.863  97.923  1.00 100.78 ?  582 LEU   A CA  1 
ATOM   3273 C C   . LEU   A 1 460 ? -18.309 76.239  97.359  1.00 103.72 ?  582 LEU   A C   1 
ATOM   3274 O O   . LEU   A 1 460 ? -18.738 76.585  96.249  1.00 103.08 ?  582 LEU   A O   1 
ATOM   3275 C CB  . LEU   A 1 460 ? -17.665 73.818  97.341  1.00 99.33  ?  582 LEU   A CB  1 
ATOM   3276 C CG  . LEU   A 1 460 ? -17.770 72.364  97.828  1.00 101.39 ?  582 LEU   A CG  1 
ATOM   3277 C CD1 . LEU   A 1 460 ? -16.460 71.647  97.679  1.00 95.09  ?  582 LEU   A CD1 1 
ATOM   3278 C CD2 . LEU   A 1 460 ? -18.254 72.238  99.258  1.00 106.39 ?  582 LEU   A CD2 1 
ATOM   3279 N N   . ASP   A 1 461 ? -17.549 77.025  98.126  1.00 105.77 ?  583 ASP   A N   1 
ATOM   3280 C CA  . ASP   A 1 461 ? -17.121 78.360  97.687  1.00 107.73 ?  583 ASP   A CA  1 
ATOM   3281 C C   . ASP   A 1 461 ? -16.004 78.201  96.654  1.00 103.77 ?  583 ASP   A C   1 
ATOM   3282 O O   . ASP   A 1 461 ? -14.861 77.887  96.998  1.00 105.06 ?  583 ASP   A O   1 
ATOM   3283 C CB  . ASP   A 1 461 ? -16.672 79.192  98.891  1.00 107.04 ?  583 ASP   A CB  1 
ATOM   3284 C CG  . ASP   A 1 461 ? -16.438 80.673  98.550  1.00 110.19 ?  583 ASP   A CG  1 
ATOM   3285 O OD1 . ASP   A 1 461 ? -17.154 81.223  97.683  1.00 117.81 ?  583 ASP   A OD1 1 
ATOM   3286 O OD2 . ASP   A 1 461 ? -15.545 81.302  99.164  1.00 107.30 ?  583 ASP   A OD2 1 
ATOM   3287 N N   . ILE   A 1 462 ? -16.313 78.403  95.377  1.00 94.09  ?  584 ILE   A N   1 
ATOM   3288 C CA  . ILE   A 1 462 ? -15.355 78.125  94.315  1.00 94.16  ?  584 ILE   A CA  1 
ATOM   3289 C C   . ILE   A 1 462 ? -15.132 79.403  93.510  1.00 97.13  ?  584 ILE   A C   1 
ATOM   3290 O O   . ILE   A 1 462 ? -16.057 79.914  92.862  1.00 100.54 ?  584 ILE   A O   1 
ATOM   3291 C CB  . ILE   A 1 462 ? -15.830 76.972  93.417  1.00 95.28  ?  584 ILE   A CB  1 
ATOM   3292 C CG1 . ILE   A 1 462 ? -16.057 75.718  94.228  1.00 91.91  ?  584 ILE   A CG1 1 
ATOM   3293 C CG2 . ILE   A 1 462 ? -14.797 76.621  92.376  1.00 95.14  ?  584 ILE   A CG2 1 
ATOM   3294 C CD1 . ILE   A 1 462 ? -16.907 74.763  93.515  1.00 94.14  ?  584 ILE   A CD1 1 
ATOM   3295 N N   . LYS   A 1 463 ? -13.905 79.904  93.530  1.00 93.04  ?  585 LYS   A N   1 
ATOM   3296 C CA  . LYS   A 1 463 ? -13.547 81.120  92.806  1.00 93.22  ?  585 LYS   A CA  1 
ATOM   3297 C C   . LYS   A 1 463 ? -12.944 80.706  91.468  1.00 93.12  ?  585 LYS   A C   1 
ATOM   3298 O O   . LYS   A 1 463 ? -11.752 80.395  91.394  1.00 90.52  ?  585 LYS   A O   1 
ATOM   3299 C CB  . LYS   A 1 463 ? -12.568 81.971  93.616  1.00 95.45  ?  585 LYS   A CB  1 
ATOM   3300 C CG  . LYS   A 1 463 ? -13.086 82.486  94.989  1.00 99.72  ?  585 LYS   A CG  1 
ATOM   3301 C CD  . LYS   A 1 463 ? -14.406 83.254  94.928  1.00 99.07  ?  585 LYS   A CD  1 
ATOM   3302 C CE  . LYS   A 1 463 ? -14.924 83.551  96.316  1.00 98.12  ?  585 LYS   A CE  1 
ATOM   3303 N NZ  . LYS   A 1 463 ? -16.378 83.257  96.374  1.00 102.72 ?  585 LYS   A NZ  1 
ATOM   3304 N N   . LEU   A 1 464 ? -13.765 80.724  90.407  1.00 97.93  ?  586 LEU   A N   1 
ATOM   3305 C CA  . LEU   A 1 464 ? -13.352 80.321  89.062  1.00 96.10  ?  586 LEU   A CA  1 
ATOM   3306 C C   . LEU   A 1 464 ? -12.608 81.442  88.345  1.00 92.59  ?  586 LEU   A C   1 
ATOM   3307 O O   . LEU   A 1 464 ? -12.721 82.620  88.679  1.00 96.29  ?  586 LEU   A O   1 
ATOM   3308 C CB  . LEU   A 1 464 ? -14.555 79.894  88.220  1.00 92.57  ?  586 LEU   A CB  1 
ATOM   3309 C CG  . LEU   A 1 464 ? -15.291 78.686  88.817  1.00 96.57  ?  586 LEU   A CG  1 
ATOM   3310 C CD1 . LEU   A 1 464 ? -16.614 78.384  88.138  1.00 92.58  ?  586 LEU   A CD1 1 
ATOM   3311 C CD2 . LEU   A 1 464 ? -14.406 77.462  88.785  1.00 98.66  ?  586 LEU   A CD2 1 
ATOM   3312 N N   . ASN   A 1 465 ? -11.832 81.053  87.349  1.00 94.34  ?  587 ASN   A N   1 
ATOM   3313 C CA  . ASN   A 1 465 ? -11.019 81.996  86.578  1.00 101.48 ?  587 ASN   A CA  1 
ATOM   3314 C C   . ASN   A 1 465 ? -10.006 82.728  87.456  1.00 96.86  ?  587 ASN   A C   1 
ATOM   3315 O O   . ASN   A 1 465 ? -9.762  83.922  87.288  1.00 98.63  ?  587 ASN   A O   1 
ATOM   3316 C CB  . ASN   A 1 465 ? -11.896 82.998  85.834  1.00 107.04 ?  587 ASN   A CB  1 
ATOM   3317 C CG  . ASN   A 1 465 ? -12.762 82.341  84.811  1.00 111.03 ?  587 ASN   A CG  1 
ATOM   3318 O OD1 . ASN   A 1 465 ? -12.270 81.803  83.810  1.00 111.33 ?  587 ASN   A OD1 1 
ATOM   3319 N ND2 . ASN   A 1 465 ? -14.068 82.362  85.056  1.00 111.11 ?  587 ASN   A ND2 1 
ATOM   3320 N N   . THR   A 1 466 ? -9.369  81.996  88.363  1.00 92.97  ?  588 THR   A N   1 
ATOM   3321 C CA  . THR   A 1 466 ? -8.514  82.584  89.384  1.00 88.40  ?  588 THR   A CA  1 
ATOM   3322 C C   . THR   A 1 466 ? -7.171  81.860  89.381  1.00 84.77  ?  588 THR   A C   1 
ATOM   3323 O O   . THR   A 1 466 ? -7.014  80.813  90.013  1.00 83.97  ?  588 THR   A O   1 
ATOM   3324 C CB  . THR   A 1 466 ? -9.203  82.477  90.729  1.00 93.50  ?  588 THR   A CB  1 
ATOM   3325 O OG1 . THR   A 1 466 ? -10.581 82.833  90.562  1.00 92.69  ?  588 THR   A OG1 1 
ATOM   3326 C CG2 . THR   A 1 466 ? -8.566  83.425  91.712  1.00 95.00  ?  588 THR   A CG2 1 
ATOM   3327 N N   . ALA   A 1 467 ? -6.201  82.402  88.667  1.00 82.10  ?  589 ALA   A N   1 
ATOM   3328 C CA  . ALA   A 1 467 ? -4.917  81.728  88.551  1.00 82.04  ?  589 ALA   A CA  1 
ATOM   3329 C C   . ALA   A 1 467 ? -4.096  82.006  89.794  1.00 82.98  ?  589 ALA   A C   1 
ATOM   3330 O O   . ALA   A 1 467 ? -3.645  83.133  89.997  1.00 86.35  ?  589 ALA   A O   1 
ATOM   3331 C CB  . ALA   A 1 467 ? -4.167  82.193  87.310  1.00 81.12  ?  589 ALA   A CB  1 
ATOM   3332 N N   . VAL   A 1 468 ? -3.871  80.986  90.621  1.00 78.56  ?  590 VAL   A N   1 
ATOM   3333 C CA  . VAL   A 1 468 ? -2.939  81.170  91.723  1.00 79.82  ?  590 VAL   A CA  1 
ATOM   3334 C C   . VAL   A 1 468 ? -1.541  81.391  91.171  1.00 80.78  ?  590 VAL   A C   1 
ATOM   3335 O O   . VAL   A 1 468 ? -1.126  80.753  90.197  1.00 86.22  ?  590 VAL   A O   1 
ATOM   3336 C CB  . VAL   A 1 468 ? -2.995  79.986  92.695  1.00 79.87  ?  590 VAL   A CB  1 
ATOM   3337 C CG1 . VAL   A 1 468 ? -1.852  80.068  93.682  1.00 77.14  ?  590 VAL   A CG1 1 
ATOM   3338 C CG2 . VAL   A 1 468 ? -4.326  80.016  93.443  1.00 77.11  ?  590 VAL   A CG2 1 
ATOM   3339 N N   . ARG   A 1 469 ? -0.819  82.323  91.777  1.00 78.69  ?  591 ARG   A N   1 
ATOM   3340 C CA  . ARG   A 1 469 ? 0.417   82.851  91.225  1.00 82.94  ?  591 ARG   A CA  1 
ATOM   3341 C C   . ARG   A 1 469 ? 1.581   82.791  92.195  1.00 82.21  ?  591 ARG   A C   1 
ATOM   3342 O O   . ARG   A 1 469 ? 2.737   82.828  91.755  1.00 82.04  ?  591 ARG   A O   1 
ATOM   3343 C CB  . ARG   A 1 469 ? 0.192   84.307  90.797  1.00 88.33  ?  591 ARG   A CB  1 
ATOM   3344 C CG  . ARG   A 1 469 ? -0.294  84.458  89.392  1.00 96.80  ?  591 ARG   A CG  1 
ATOM   3345 C CD  . ARG   A 1 469 ? 0.694   85.210  88.551  1.00 107.18 ?  591 ARG   A CD  1 
ATOM   3346 N NE  . ARG   A 1 469 ? 0.166   85.472  87.218  1.00 114.84 ?  591 ARG   A NE  1 
ATOM   3347 C CZ  . ARG   A 1 469 ? 0.483   86.533  86.493  1.00 120.32 ?  591 ARG   A CZ  1 
ATOM   3348 N NH1 . ARG   A 1 469 ? 1.106   87.569  87.027  1.00 125.83 ?  591 ARG   A NH1 1 
ATOM   3349 N NH2 . ARG   A 1 469 ? 0.137   86.572  85.211  1.00 122.48 ?  591 ARG   A NH2 1 
ATOM   3350 N N   . GLN   A 1 470 ? 1.311   82.710  93.493  1.00 81.31  ?  592 GLN   A N   1 
ATOM   3351 C CA  . GLN   A 1 470 ? 2.324   82.692  94.531  1.00 80.41  ?  592 GLN   A CA  1 
ATOM   3352 C C   . GLN   A 1 470 ? 1.687   82.193  95.819  1.00 81.46  ?  592 GLN   A C   1 
ATOM   3353 O O   . GLN   A 1 470 ? 0.642   82.712  96.236  1.00 77.34  ?  592 GLN   A O   1 
ATOM   3354 C CB  . GLN   A 1 470 ? 2.909   84.076  94.750  1.00 82.69  ?  592 GLN   A CB  1 
ATOM   3355 C CG  . GLN   A 1 470 ? 4.252   84.025  95.436  1.00 88.15  ?  592 GLN   A CG  1 
ATOM   3356 C CD  . GLN   A 1 470 ? 4.819   85.395  95.736  1.00 89.69  ?  592 GLN   A CD  1 
ATOM   3357 O OE1 . GLN   A 1 470 ? 4.662   85.909  96.849  1.00 84.11  ?  592 GLN   A OE1 1 
ATOM   3358 N NE2 . GLN   A 1 470 ? 5.501   85.988  94.756  1.00 95.58  ?  592 GLN   A NE2 1 
ATOM   3359 N N   . VAL   A 1 471 ? 2.316   81.190  96.437  1.00 82.07  ?  593 VAL   A N   1 
ATOM   3360 C CA  . VAL   A 1 471 ? 1.907   80.679  97.743  1.00 82.47  ?  593 VAL   A CA  1 
ATOM   3361 C C   . VAL   A 1 471 ? 2.974   81.076  98.752  1.00 83.79  ?  593 VAL   A C   1 
ATOM   3362 O O   . VAL   A 1 471 ? 4.152   80.712  98.605  1.00 80.84  ?  593 VAL   A O   1 
ATOM   3363 C CB  . VAL   A 1 471 ? 1.683   79.159  97.751  1.00 78.10  ?  593 VAL   A CB  1 
ATOM   3364 C CG1 . VAL   A 1 471 ? 1.146   78.747  99.068  1.00 76.85  ?  593 VAL   A CG1 1 
ATOM   3365 C CG2 . VAL   A 1 471 ? 0.661   78.780  96.743  1.00 83.57  ?  593 VAL   A CG2 1 
ATOM   3366 N N   . ARG   A 1 472 ? 2.542   81.844  99.758  1.00 79.74  ?  594 ARG   A N   1 
ATOM   3367 C CA  . ARG   A 1 472 ? 3.351   82.341  100.854 1.00 73.11  ?  594 ARG   A CA  1 
ATOM   3368 C C   . ARG   A 1 472 ? 2.810   81.718  102.125 1.00 77.72  ?  594 ARG   A C   1 
ATOM   3369 O O   . ARG   A 1 472 ? 1.632   81.908  102.454 1.00 79.23  ?  594 ARG   A O   1 
ATOM   3370 C CB  . ARG   A 1 472 ? 3.245   83.858  100.978 1.00 90.18  ?  594 ARG   A CB  1 
ATOM   3371 C CG  . ARG   A 1 472 ? 3.651   84.690  99.784  1.00 91.61  ?  594 ARG   A CG  1 
ATOM   3372 C CD  . ARG   A 1 472 ? 3.721   86.173  100.151 1.00 88.21  ?  594 ARG   A CD  1 
ATOM   3373 N NE  . ARG   A 1 472 ? 4.921   86.756  99.569  1.00 90.19  ?  594 ARG   A NE  1 
ATOM   3374 C CZ  . ARG   A 1 472 ? 5.950   87.191  100.279 1.00 91.30  ?  594 ARG   A CZ  1 
ATOM   3375 N NH1 . ARG   A 1 472 ? 5.892   87.240  101.611 1.00 89.20  ?  594 ARG   A NH1 1 
ATOM   3376 N NH2 . ARG   A 1 472 ? 7.058   87.590  99.640  1.00 80.81  ?  594 ARG   A NH2 1 
ATOM   3377 N N   . TYR   A 1 473 ? 3.666   81.016  102.853 1.00 77.83  ?  595 TYR   A N   1 
ATOM   3378 C CA  . TYR   A 1 473 ? 3.249   80.307  104.054 1.00 78.25  ?  595 TYR   A CA  1 
ATOM   3379 C C   . TYR   A 1 473 ? 4.302   80.578  105.125 1.00 83.59  ?  595 TYR   A C   1 
ATOM   3380 O O   . TYR   A 1 473 ? 5.510   80.587  104.839 1.00 78.69  ?  595 TYR   A O   1 
ATOM   3381 C CB  . TYR   A 1 473 ? 3.068   78.788  103.760 1.00 75.44  ?  595 TYR   A CB  1 
ATOM   3382 C CG  . TYR   A 1 473 ? 4.339   78.135  103.237 1.00 75.83  ?  595 TYR   A CG  1 
ATOM   3383 C CD1 . TYR   A 1 473 ? 4.718   78.233  101.913 1.00 75.39  ?  595 TYR   A CD1 1 
ATOM   3384 C CD2 . TYR   A 1 473 ? 5.181   77.467  104.086 1.00 78.80  ?  595 TYR   A CD2 1 
ATOM   3385 C CE1 . TYR   A 1 473 ? 5.898   77.679  101.465 1.00 74.49  ?  595 TYR   A CE1 1 
ATOM   3386 C CE2 . TYR   A 1 473 ? 6.356   76.909  103.643 1.00 78.49  ?  595 TYR   A CE2 1 
ATOM   3387 C CZ  . TYR   A 1 473 ? 6.712   77.015  102.339 1.00 73.92  ?  595 TYR   A CZ  1 
ATOM   3388 O OH  . TYR   A 1 473 ? 7.903   76.442  101.942 1.00 77.27  ?  595 TYR   A OH  1 
ATOM   3389 N N   . THR   A 1 474 ? 3.839   80.849  106.350 1.00 85.95  ?  596 THR   A N   1 
ATOM   3390 C CA  . THR   A 1 474 ? 4.707   81.294  107.436 1.00 85.42  ?  596 THR   A CA  1 
ATOM   3391 C C   . THR   A 1 474 ? 4.282   80.649  108.740 1.00 88.94  ?  596 THR   A C   1 
ATOM   3392 O O   . THR   A 1 474 ? 3.229   80.008  108.833 1.00 90.01  ?  596 THR   A O   1 
ATOM   3393 C CB  . THR   A 1 474 ? 4.620   82.797  107.664 1.00 97.05  ?  596 THR   A CB  1 
ATOM   3394 O OG1 . THR   A 1 474 ? 3.363   83.083  108.304 1.00 96.94  ?  596 THR   A OG1 1 
ATOM   3395 C CG2 . THR   A 1 474 ? 4.737   83.580  106.331 1.00 96.01  ?  596 THR   A CG2 1 
ATOM   3396 N N   . ALA   A 1 475 ? 5.077   80.904  109.781 1.00 88.54  ?  597 ALA   A N   1 
ATOM   3397 C CA  . ALA   A 1 475 ? 4.779   80.349  111.096 1.00 92.62  ?  597 ALA   A CA  1 
ATOM   3398 C C   . ALA   A 1 475 ? 3.345   80.631  111.551 1.00 91.95  ?  597 ALA   A C   1 
ATOM   3399 O O   . ALA   A 1 475 ? 2.729   79.803  112.229 1.00 103.35 ?  597 ALA   A O   1 
ATOM   3400 C CB  . ALA   A 1 475 ? 5.783   80.890  112.106 1.00 93.78  ?  597 ALA   A CB  1 
ATOM   3401 N N   . SER   A 1 476 ? 2.783   81.757  111.158 1.00 91.54  ?  598 SER   A N   1 
ATOM   3402 C CA  . SER   A 1 476 ? 1.533   82.230  111.722 1.00 95.70  ?  598 SER   A CA  1 
ATOM   3403 C C   . SER   A 1 476 ? 0.373   82.190  110.741 1.00 95.18  ?  598 SER   A C   1 
ATOM   3404 O O   . SER   A 1 476 ? -0.747  82.578  111.106 1.00 99.55  ?  598 SER   A O   1 
ATOM   3405 C CB  . SER   A 1 476 ? 1.740   83.652  112.250 1.00 101.06 ?  598 SER   A CB  1 
ATOM   3406 O OG  . SER   A 1 476 ? 2.298   84.460  111.224 1.00 99.21  ?  598 SER   A OG  1 
ATOM   3407 N N   . GLY   A 1 477 ? 0.607   81.737  109.520 1.00 92.24  ?  599 GLY   A N   1 
ATOM   3408 C CA  . GLY   A 1 477 ? -0.450  81.638  108.533 1.00 91.52  ?  599 GLY   A CA  1 
ATOM   3409 C C   . GLY   A 1 477 ? 0.098   81.669  107.117 1.00 91.55  ?  599 GLY   A C   1 
ATOM   3410 O O   . GLY   A 1 477 ? 1.313   81.673  106.881 1.00 87.77  ?  599 GLY   A O   1 
ATOM   3411 N N   . CYS   A 1 478 ? -0.838  81.683  106.165 1.00 88.64  ?  600 CYS   A N   1 
ATOM   3412 C CA  . CYS   A 1 478 ? -0.488  81.755  104.758 1.00 84.20  ?  600 CYS   A CA  1 
ATOM   3413 C C   . CYS   A 1 478 ? -1.359  82.771  104.053 1.00 87.29  ?  600 CYS   A C   1 
ATOM   3414 O O   . CYS   A 1 478 ? -2.531  82.971  104.399 1.00 81.39  ?  600 CYS   A O   1 
ATOM   3415 C CB  . CYS   A 1 478 ? -0.701  80.451  104.018 1.00 85.33  ?  600 CYS   A CB  1 
ATOM   3416 S SG  . CYS   A 1 478 ? -0.277  79.034  104.896 1.00 91.06  ?  600 CYS   A SG  1 
ATOM   3417 N N   . GLU   A 1 479 ? -0.774  83.362  103.019 1.00 89.38  ?  601 GLU   A N   1 
ATOM   3418 C CA  . GLU   A 1 479 ? -1.511  84.126  102.029 1.00 95.13  ?  601 GLU   A CA  1 
ATOM   3419 C C   . GLU   A 1 479 ? -1.164  83.569  100.660 1.00 91.77  ?  601 GLU   A C   1 
ATOM   3420 O O   . GLU   A 1 479 ? -0.007  83.215  100.396 1.00 85.26  ?  601 GLU   A O   1 
ATOM   3421 C CB  . GLU   A 1 479 ? -1.233  85.661  102.119 1.00 100.31 ?  601 GLU   A CB  1 
ATOM   3422 C CG  . GLU   A 1 479 ? 0.232   86.076  102.288 1.00 104.43 ?  601 GLU   A CG  1 
ATOM   3423 C CD  . GLU   A 1 479 ? 0.390   87.530  102.737 1.00 114.38 ?  601 GLU   A CD  1 
ATOM   3424 O OE1 . GLU   A 1 479 ? -0.375  88.403  102.263 1.00 116.15 ?  601 GLU   A OE1 1 
ATOM   3425 O OE2 . GLU   A 1 479 ? 1.286   87.797  103.571 1.00 121.34 ?  601 GLU   A OE2 1 
ATOM   3426 N N   . VAL   A 1 480 ? -2.207  83.435  99.835  1.00 96.78  ?  602 VAL   A N   1 
ATOM   3427 C CA  . VAL   A 1 480 ? -2.146  82.914  98.472  1.00 92.27  ?  602 VAL   A CA  1 
ATOM   3428 C C   . VAL   A 1 480 ? -2.466  84.075  97.556  1.00 87.77  ?  602 VAL   A C   1 
ATOM   3429 O O   . VAL   A 1 480 ? -3.440  84.794  97.797  1.00 90.02  ?  602 VAL   A O   1 
ATOM   3430 C CB  . VAL   A 1 480 ? -3.169  81.781  98.247  1.00 93.53  ?  602 VAL   A CB  1 
ATOM   3431 C CG1 . VAL   A 1 480 ? -3.097  81.271  96.817  1.00 91.48  ?  602 VAL   A CG1 1 
ATOM   3432 C CG2 . VAL   A 1 480 ? -3.004  80.644  99.252  1.00 88.97  ?  602 VAL   A CG2 1 
ATOM   3433 N N   . ILE   A 1 481 ? -1.675  84.259  96.508  1.00 89.55  ?  603 ILE   A N   1 
ATOM   3434 C CA  . ILE   A 1 481 ? -1.861  85.397  95.610  1.00 94.56  ?  603 ILE   A CA  1 
ATOM   3435 C C   . ILE   A 1 481 ? -2.300  84.883  94.253  1.00 89.61  ?  603 ILE   A C   1 
ATOM   3436 O O   . ILE   A 1 481 ? -1.579  84.108  93.614  1.00 90.10  ?  603 ILE   A O   1 
ATOM   3437 C CB  . ILE   A 1 481 ? -0.589  86.240  95.478  1.00 91.15  ?  603 ILE   A CB  1 
ATOM   3438 C CG1 . ILE   A 1 481 ? 0.085   86.380  96.841  1.00 94.76  ?  603 ILE   A CG1 1 
ATOM   3439 C CG2 . ILE   A 1 481 ? -0.951  87.597  94.946  1.00 85.41  ?  603 ILE   A CG2 1 
ATOM   3440 C CD1 . ILE   A 1 481 ? 1.538   86.778  96.748  1.00 95.27  ?  603 ILE   A CD1 1 
ATOM   3441 N N   . ALA   A 1 482 ? -3.462  85.342  93.797  1.00 89.43  ?  604 ALA   A N   1 
ATOM   3442 C CA  . ALA   A 1 482 ? -4.017  84.938  92.512  1.00 93.82  ?  604 ALA   A CA  1 
ATOM   3443 C C   . ALA   A 1 482 ? -4.279  86.165  91.633  1.00 97.10  ?  604 ALA   A C   1 
ATOM   3444 O O   . ALA   A 1 482 ? -4.403  87.289  92.127  1.00 98.65  ?  604 ALA   A O   1 
ATOM   3445 C CB  . ALA   A 1 482 ? -5.310  84.129  92.715  1.00 87.42  ?  604 ALA   A CB  1 
ATOM   3446 N N   . VAL   A 1 483 ? -4.353  85.949  90.319  1.00 93.93  ?  605 VAL   A N   1 
ATOM   3447 C CA  . VAL   A 1 483 ? -4.815  86.967  89.382  1.00 90.88  ?  605 VAL   A CA  1 
ATOM   3448 C C   . VAL   A 1 483 ? -6.120  86.490  88.756  1.00 92.35  ?  605 VAL   A C   1 
ATOM   3449 O O   . VAL   A 1 483 ? -6.512  85.337  88.890  1.00 96.70  ?  605 VAL   A O   1 
ATOM   3450 C CB  . VAL   A 1 483 ? -3.763  87.287  88.302  1.00 98.06  ?  605 VAL   A CB  1 
ATOM   3451 C CG1 . VAL   A 1 483 ? -2.429  87.582  88.941  1.00 103.89 ?  605 VAL   A CG1 1 
ATOM   3452 C CG2 . VAL   A 1 483 ? -3.625  86.146  87.307  1.00 95.97  ?  605 VAL   A CG2 1 
ATOM   3453 N N   . ASN   A 1 484 ? -6.807  87.395  88.080  1.00 98.68  ?  606 ASN   A N   1 
ATOM   3454 C CA  . ASN   A 1 484 ? -7.948  87.014  87.262  1.00 104.84 ?  606 ASN   A CA  1 
ATOM   3455 C C   . ASN   A 1 484 ? -7.444  86.634  85.873  1.00 109.00 ?  606 ASN   A C   1 
ATOM   3456 O O   . ASN   A 1 484 ? -6.699  87.396  85.247  1.00 108.79 ?  606 ASN   A O   1 
ATOM   3457 C CB  . ASN   A 1 484 ? -8.971  88.143  87.163  1.00 110.35 ?  606 ASN   A CB  1 
ATOM   3458 C CG  . ASN   A 1 484 ? -10.228 87.719  86.437  1.00 112.38 ?  606 ASN   A CG  1 
ATOM   3459 O OD1 . ASN   A 1 484 ? -11.062 87.003  86.998  1.00 111.08 ?  606 ASN   A OD1 1 
ATOM   3460 N ND2 . ASN   A 1 484 ? -10.370 88.144  85.180  1.00 111.58 ?  606 ASN   A ND2 1 
ATOM   3461 N N   . THR   A 1 485 ? -7.857  85.452  85.400  1.00 109.44 ?  607 THR   A N   1 
ATOM   3462 C CA  . THR   A 1 485 ? -7.287  84.880  84.181  1.00 110.18 ?  607 THR   A CA  1 
ATOM   3463 C C   . THR   A 1 485 ? -7.600  85.715  82.956  1.00 115.75 ?  607 THR   A C   1 
ATOM   3464 O O   . THR   A 1 485 ? -6.816  85.732  82.000  1.00 117.26 ?  607 THR   A O   1 
ATOM   3465 C CB  . THR   A 1 485 ? -7.817  83.469  83.969  1.00 105.54 ?  607 THR   A CB  1 
ATOM   3466 O OG1 . THR   A 1 485 ? -9.220  83.448  84.265  1.00 104.53 ?  607 THR   A OG1 1 
ATOM   3467 C CG2 . THR   A 1 485 ? -7.093  82.498  84.864  1.00 98.60  ?  607 THR   A CG2 1 
ATOM   3468 N N   . ARG   A 1 486 ? -8.735  86.412  82.969  1.00 117.23 ?  608 ARG   A N   1 
ATOM   3469 C CA  . ARG   A 1 486 ? -9.221  87.096  81.778  1.00 118.81 ?  608 ARG   A CA  1 
ATOM   3470 C C   . ARG   A 1 486 ? -8.489  88.425  81.561  1.00 121.54 ?  608 ARG   A C   1 
ATOM   3471 O O   . ARG   A 1 486 ? -7.861  88.633  80.510  1.00 118.50 ?  608 ARG   A O   1 
ATOM   3472 C CB  . ARG   A 1 486 ? -10.737 87.255  81.901  1.00 118.81 ?  608 ARG   A CB  1 
ATOM   3473 C CG  . ARG   A 1 486 ? -11.438 85.873  81.938  1.00 119.09 ?  608 ARG   A CG  1 
ATOM   3474 C CD  . ARG   A 1 486 ? -12.838 85.915  82.536  1.00 119.54 ?  608 ARG   A CD  1 
ATOM   3475 N NE  . ARG   A 1 486 ? -12.837 86.120  83.979  1.00 124.20 ?  608 ARG   A NE  1 
ATOM   3476 C CZ  . ARG   A 1 486 ? -13.935 86.194  84.722  1.00 130.47 ?  608 ARG   A CZ  1 
ATOM   3477 N NH1 . ARG   A 1 486 ? -15.142 86.115  84.183  1.00 136.71 ?  608 ARG   A NH1 1 
ATOM   3478 N NH2 . ARG   A 1 486 ? -13.820 86.351  86.040  1.00 126.63 ?  608 ARG   A NH2 1 
ATOM   3479 N N   . SER   A 1 487 ? -8.538  89.331  82.560  1.00 126.10 ?  609 SER   A N   1 
ATOM   3480 C CA  . SER   A 1 487 ? -7.612  90.472  82.662  1.00 129.88 ?  609 SER   A CA  1 
ATOM   3481 C C   . SER   A 1 487 ? -6.613  90.140  83.775  1.00 122.80 ?  609 SER   A C   1 
ATOM   3482 O O   . SER   A 1 487 ? -6.943  90.193  84.965  1.00 112.96 ?  609 SER   A O   1 
ATOM   3483 C CB  . SER   A 1 487 ? -8.338  91.794  82.932  1.00 131.15 ?  609 SER   A CB  1 
ATOM   3484 O OG  . SER   A 1 487 ? -8.643  91.983  84.311  1.00 126.12 ?  609 SER   A OG  1 
ATOM   3485 N N   . THR   A 1 488 ? -5.385  89.785  83.372  1.00 125.47 ?  610 THR   A N   1 
ATOM   3486 C CA  . THR   A 1 488 ? -4.361  89.319  84.303  1.00 118.34 ?  610 THR   A CA  1 
ATOM   3487 C C   . THR   A 1 488 ? -3.854  90.428  85.212  1.00 122.82 ?  610 THR   A C   1 
ATOM   3488 O O   . THR   A 1 488 ? -3.108  90.138  86.154  1.00 123.25 ?  610 THR   A O   1 
ATOM   3489 C CB  . THR   A 1 488 ? -3.175  88.706  83.537  1.00 121.32 ?  610 THR   A CB  1 
ATOM   3490 O OG1 . THR   A 1 488 ? -2.233  89.725  83.160  1.00 125.38 ?  610 THR   A OG1 1 
ATOM   3491 C CG2 . THR   A 1 488 ? -3.675  88.025  82.264  1.00 127.08 ?  610 THR   A CG2 1 
ATOM   3492 N N   . SER   A 1 489 ? -4.232  91.683  84.945  1.00 127.18 ?  611 SER   A N   1 
ATOM   3493 C CA  . SER   A 1 489 ? -3.794  92.798  85.773  1.00 117.83 ?  611 SER   A CA  1 
ATOM   3494 C C   . SER   A 1 489 ? -4.402  92.744  87.164  1.00 115.97 ?  611 SER   A C   1 
ATOM   3495 O O   . SER   A 1 489 ? -3.797  93.238  88.121  1.00 120.12 ?  611 SER   A O   1 
ATOM   3496 C CB  . SER   A 1 489 ? -4.176  94.110  85.115  1.00 120.22 ?  611 SER   A CB  1 
ATOM   3497 O OG  . SER   A 1 489 ? -5.591  94.172  84.987  1.00 129.10 ?  611 SER   A OG  1 
ATOM   3498 N N   . GLN   A 1 490 ? -5.576  92.134  87.296  1.00 112.06 ?  612 GLN   A N   1 
ATOM   3499 C CA  . GLN   A 1 490 ? -6.444  92.339  88.448  1.00 110.98 ?  612 GLN   A CA  1 
ATOM   3500 C C   . GLN   A 1 490 ? -6.155  91.310  89.536  1.00 106.74 ?  612 GLN   A C   1 
ATOM   3501 O O   . GLN   A 1 490 ? -6.467  90.130  89.366  1.00 109.42 ?  612 GLN   A O   1 
ATOM   3502 C CB  . GLN   A 1 490 ? -7.893  92.253  88.006  1.00 114.90 ?  612 GLN   A CB  1 
ATOM   3503 C CG  . GLN   A 1 490 ? -8.798  92.873  89.010  1.00 128.51 ?  612 GLN   A CG  1 
ATOM   3504 C CD  . GLN   A 1 490 ? -10.076 92.114  89.173  1.00 130.57 ?  612 GLN   A CD  1 
ATOM   3505 O OE1 . GLN   A 1 490 ? -10.511 91.389  88.265  1.00 124.51 ?  612 GLN   A OE1 1 
ATOM   3506 N NE2 . GLN   A 1 490 ? -10.706 92.281  90.337  1.00 133.50 ?  612 GLN   A NE2 1 
ATOM   3507 N N   . THR   A 1 491 ? -5.638  91.767  90.685  1.00 107.58 ?  613 THR   A N   1 
ATOM   3508 C CA  . THR   A 1 491 ? -4.960  90.921  91.668  1.00 98.10  ?  613 THR   A CA  1 
ATOM   3509 C C   . THR   A 1 491 ? -5.820  90.609  92.899  1.00 93.58  ?  613 THR   A C   1 
ATOM   3510 O O   . THR   A 1 491 ? -6.652  91.418  93.320  1.00 97.72  ?  613 THR   A O   1 
ATOM   3511 C CB  . THR   A 1 491 ? -3.643  91.587  92.065  1.00 81.96  ?  613 THR   A CB  1 
ATOM   3512 O OG1 . THR   A 1 491 ? -2.736  91.490  90.959  1.00 84.76  ?  613 THR   A OG1 1 
ATOM   3513 C CG2 . THR   A 1 491 ? -3.040  90.973  93.272  1.00 72.39  ?  613 THR   A CG2 1 
ATOM   3514 N N   . PHE   A 1 492 ? -5.613  89.401  93.454  1.00 90.94  ?  614 PHE   A N   1 
ATOM   3515 C CA  . PHE   A 1 492 ? -6.373  88.823  94.570  1.00 94.16  ?  614 PHE   A CA  1 
ATOM   3516 C C   . PHE   A 1 492 ? -5.449  88.264  95.661  1.00 92.30  ?  614 PHE   A C   1 
ATOM   3517 O O   . PHE   A 1 492 ? -4.526  87.492  95.370  1.00 88.86  ?  614 PHE   A O   1 
ATOM   3518 C CB  . PHE   A 1 492 ? -7.277  87.708  94.058  1.00 89.49  ?  614 PHE   A CB  1 
ATOM   3519 C CG  . PHE   A 1 492 ? -8.483  88.194  93.347  1.00 94.14  ?  614 PHE   A CG  1 
ATOM   3520 C CD1 . PHE   A 1 492 ? -8.398  88.604  92.033  1.00 97.43  ?  614 PHE   A CD1 1 
ATOM   3521 C CD2 . PHE   A 1 492 ? -9.723  88.165  93.961  1.00 101.30 ?  614 PHE   A CD2 1 
ATOM   3522 C CE1 . PHE   A 1 492 ? -9.519  89.032  91.359  1.00 105.45 ?  614 PHE   A CE1 1 
ATOM   3523 C CE2 . PHE   A 1 492 ? -10.864 88.583  93.292  1.00 108.76 ?  614 PHE   A CE2 1 
ATOM   3524 C CZ  . PHE   A 1 492 ? -10.761 89.019  91.989  1.00 111.10 ?  614 PHE   A CZ  1 
ATOM   3525 N N   . ILE   A 1 493 ? -5.707  88.635  96.918  1.00 85.34  ?  615 ILE   A N   1 
ATOM   3526 C CA  . ILE   A 1 493 ? -4.942  88.147  98.060  1.00 83.54  ?  615 ILE   A CA  1 
ATOM   3527 C C   . ILE   A 1 493 ? -5.892  87.392  98.980  1.00 85.16  ?  615 ILE   A C   1 
ATOM   3528 O O   . ILE   A 1 493 ? -6.952  87.916  99.353  1.00 82.84  ?  615 ILE   A O   1 
ATOM   3529 C CB  . ILE   A 1 493 ? -4.243  89.287  98.828  1.00 89.06  ?  615 ILE   A CB  1 
ATOM   3530 C CG1 . ILE   A 1 493 ? -3.156  89.990  97.997  1.00 91.18  ?  615 ILE   A CG1 1 
ATOM   3531 C CG2 . ILE   A 1 493 ? -3.634  88.756  100.120 1.00 91.23  ?  615 ILE   A CG2 1 
ATOM   3532 C CD1 . ILE   A 1 493 ? -1.780  89.304  97.988  1.00 92.77  ?  615 ILE   A CD1 1 
ATOM   3533 N N   . TYR   A 1 494 ? -5.506  86.160  99.340  1.00 89.40  ?  616 TYR   A N   1 
ATOM   3534 C CA  . TYR   A 1 494 ? -6.288  85.257  100.186 1.00 88.20  ?  616 TYR   A CA  1 
ATOM   3535 C C   . TYR   A 1 494 ? -5.449  84.824  101.384 1.00 90.90  ?  616 TYR   A C   1 
ATOM   3536 O O   . TYR   A 1 494 ? -4.382  84.230  101.205 1.00 88.65  ?  616 TYR   A O   1 
ATOM   3537 C CB  . TYR   A 1 494 ? -6.749  84.029  99.399  1.00 78.49  ?  616 TYR   A CB  1 
ATOM   3538 C CG  . TYR   A 1 494 ? -7.815  84.291  98.348  1.00 80.99  ?  616 TYR   A CG  1 
ATOM   3539 C CD1 . TYR   A 1 494 ? -7.492  84.680  97.044  1.00 79.68  ?  616 TYR   A CD1 1 
ATOM   3540 C CD2 . TYR   A 1 494 ? -9.158  84.155  98.671  1.00 83.06  ?  616 TYR   A CD2 1 
ATOM   3541 C CE1 . TYR   A 1 494 ? -8.496  84.905  96.090  1.00 83.47  ?  616 TYR   A CE1 1 
ATOM   3542 C CE2 . TYR   A 1 494 ? -10.163 84.384  97.738  1.00 83.92  ?  616 TYR   A CE2 1 
ATOM   3543 C CZ  . TYR   A 1 494 ? -9.841  84.752  96.454  1.00 86.96  ?  616 TYR   A CZ  1 
ATOM   3544 O OH  . TYR   A 1 494 ? -10.895 84.966  95.571  1.00 92.38  ?  616 TYR   A OH  1 
ATOM   3545 N N   . LYS   A 1 495 ? -5.931  85.113  102.597 1.00 91.32  ?  617 LYS   A N   1 
ATOM   3546 C CA  . LYS   A 1 495 ? -5.264  84.727  103.836 1.00 92.22  ?  617 LYS   A CA  1 
ATOM   3547 C C   . LYS   A 1 495 ? -5.981  83.527  104.439 1.00 94.26  ?  617 LYS   A C   1 
ATOM   3548 O O   . LYS   A 1 495 ? -7.210  83.434  104.360 1.00 98.15  ?  617 LYS   A O   1 
ATOM   3549 C CB  . LYS   A 1 495 ? -5.271  85.869  104.862 1.00 99.40  ?  617 LYS   A CB  1 
ATOM   3550 C CG  . LYS   A 1 495 ? -4.867  87.294  104.405 1.00 106.04 ?  617 LYS   A CG  1 
ATOM   3551 C CD  . LYS   A 1 495 ? -3.379  87.673  104.631 1.00 108.01 ?  617 LYS   A CD  1 
ATOM   3552 C CE  . LYS   A 1 495 ? -2.988  88.992  103.895 1.00 110.69 ?  617 LYS   A CE  1 
ATOM   3553 N NZ  . LYS   A 1 495 ? -3.679  90.275  104.344 1.00 96.49  ?  617 LYS   A NZ  1 
ATOM   3554 N N   . CYS   A 1 496 ? -5.217  82.618  105.064 1.00 89.72  ?  618 CYS   A N   1 
ATOM   3555 C CA  . CYS   A 1 496 ? -5.800  81.371  105.567 1.00 85.68  ?  618 CYS   A CA  1 
ATOM   3556 C C   . CYS   A 1 496 ? -4.847  80.666  106.526 1.00 84.90  ?  618 CYS   A C   1 
ATOM   3557 O O   . CYS   A 1 496 ? -3.630  80.884  106.499 1.00 81.06  ?  618 CYS   A O   1 
ATOM   3558 C CB  . CYS   A 1 496 ? -6.129  80.426  104.420 1.00 89.88  ?  618 CYS   A CB  1 
ATOM   3559 S SG  . CYS   A 1 496 ? -4.635  79.908  103.511 1.00 102.46 ?  618 CYS   A SG  1 
ATOM   3560 N N   . ASP   A 1 497 ? -5.419  79.763  107.336 1.00 83.31  ?  619 ASP   A N   1 
ATOM   3561 C CA  . ASP   A 1 497 ? -4.602  78.969  108.258 1.00 94.69  ?  619 ASP   A CA  1 
ATOM   3562 C C   . ASP   A 1 497 ? -3.733  77.925  107.543 1.00 97.24  ?  619 ASP   A C   1 
ATOM   3563 O O   . ASP   A 1 497 ? -2.598  77.662  107.978 1.00 91.48  ?  619 ASP   A O   1 
ATOM   3564 C CB  . ASP   A 1 497 ? -5.484  78.270  109.288 1.00 92.61  ?  619 ASP   A CB  1 
ATOM   3565 C CG  . ASP   A 1 497 ? -6.165  79.232  110.216 1.00 96.09  ?  619 ASP   A CG  1 
ATOM   3566 O OD1 . ASP   A 1 497 ? -5.454  79.817  111.078 1.00 99.11  ?  619 ASP   A OD1 1 
ATOM   3567 O OD2 . ASP   A 1 497 ? -7.406  79.359  110.098 1.00 88.44  ?  619 ASP   A OD2 1 
ATOM   3568 N N   . ALA   A 1 498 ? -4.247  77.304  106.472 1.00 97.76  ?  620 ALA   A N   1 
ATOM   3569 C CA  . ALA   A 1 498 ? -3.523  76.283  105.721 1.00 86.26  ?  620 ALA   A CA  1 
ATOM   3570 C C   . ALA   A 1 498 ? -3.956  76.287  104.259 1.00 81.26  ?  620 ALA   A C   1 
ATOM   3571 O O   . ALA   A 1 498 ? -5.139  76.492  103.956 1.00 78.79  ?  620 ALA   A O   1 
ATOM   3572 C CB  . ALA   A 1 498 ? -3.755  74.896  106.327 1.00 88.03  ?  620 ALA   A CB  1 
ATOM   3573 N N   . VAL   A 1 499 ? -2.985  76.034  103.371 1.00 82.11  ?  621 VAL   A N   1 
ATOM   3574 C CA  . VAL   A 1 499 ? -3.187  75.882  101.924 1.00 78.15  ?  621 VAL   A CA  1 
ATOM   3575 C C   . VAL   A 1 499 ? -3.013  74.421  101.531 1.00 82.45  ?  621 VAL   A C   1 
ATOM   3576 O O   . VAL   A 1 499 ? -1.931  73.848  101.729 1.00 80.89  ?  621 VAL   A O   1 
ATOM   3577 C CB  . VAL   A 1 499 ? -2.200  76.727  101.116 1.00 74.27  ?  621 VAL   A CB  1 
ATOM   3578 C CG1 . VAL   A 1 499 ? -2.657  76.811  99.696  1.00 73.96  ?  621 VAL   A CG1 1 
ATOM   3579 C CG2 . VAL   A 1 499 ? -2.084  78.093  101.724 1.00 85.16  ?  621 VAL   A CG2 1 
ATOM   3580 N N   . LEU   A 1 500 ? -4.069  73.838  100.943 1.00 80.16  ?  622 LEU   A N   1 
ATOM   3581 C CA  . LEU   A 1 500 ? -4.028  72.516  100.339 1.00 74.38  ?  622 LEU   A CA  1 
ATOM   3582 C C   . LEU   A 1 500 ? -3.818  72.705  98.850  1.00 76.51  ?  622 LEU   A C   1 
ATOM   3583 O O   . LEU   A 1 500 ? -4.675  73.290  98.180  1.00 75.76  ?  622 LEU   A O   1 
ATOM   3584 C CB  . LEU   A 1 500 ? -5.321  71.748  100.585 1.00 79.22  ?  622 LEU   A CB  1 
ATOM   3585 C CG  . LEU   A 1 500 ? -5.413  70.369  99.915  1.00 79.69  ?  622 LEU   A CG  1 
ATOM   3586 C CD1 . LEU   A 1 500 ? -4.421  69.398  100.557 1.00 73.10  ?  622 LEU   A CD1 1 
ATOM   3587 C CD2 . LEU   A 1 500 ? -6.834  69.843  100.012 1.00 74.49  ?  622 LEU   A CD2 1 
ATOM   3588 N N   . CYS   A 1 501 ? -2.695  72.188  98.339  1.00 76.19  ?  623 CYS   A N   1 
ATOM   3589 C CA  . CYS   A 1 501 ? -2.268  72.390  96.960  1.00 74.95  ?  623 CYS   A CA  1 
ATOM   3590 C C   . CYS   A 1 501 ? -2.557  71.136  96.136  1.00 83.86  ?  623 CYS   A C   1 
ATOM   3591 O O   . CYS   A 1 501 ? -1.878  70.116  96.300  1.00 84.93  ?  623 CYS   A O   1 
ATOM   3592 C CB  . CYS   A 1 501 ? -0.781  72.706  96.938  1.00 72.23  ?  623 CYS   A CB  1 
ATOM   3593 S SG  . CYS   A 1 501 ? -0.044  72.687  95.291  1.00 80.35  ?  623 CYS   A SG  1 
ATOM   3594 N N   . THR   A 1 502 ? -3.550  71.198  95.238  1.00 82.01  ?  624 THR   A N   1 
ATOM   3595 C CA  . THR   A 1 502 ? -3.818  70.067  94.357  1.00 79.94  ?  624 THR   A CA  1 
ATOM   3596 C C   . THR   A 1 502 ? -3.357  70.387  92.936  1.00 79.42  ?  624 THR   A C   1 
ATOM   3597 O O   . THR   A 1 502 ? -3.889  69.869  91.952  1.00 82.56  ?  624 THR   A O   1 
ATOM   3598 C CB  . THR   A 1 502 ? -5.295  69.610  94.451  1.00 78.97  ?  624 THR   A CB  1 
ATOM   3599 O OG1 . THR   A 1 502 ? -6.226  70.383  93.669  1.00 70.67  ?  624 THR   A OG1 1 
ATOM   3600 C CG2 . THR   A 1 502 ? -5.734  69.646  95.891  1.00 76.21  ?  624 THR   A CG2 1 
ATOM   3601 N N   . LEU   A 1 503 ? -2.331  71.217  92.829  1.00 77.65  ?  625 LEU   A N   1 
ATOM   3602 C CA  . LEU   A 1 503 ? -1.779  71.578  91.534  1.00 77.70  ?  625 LEU   A CA  1 
ATOM   3603 C C   . LEU   A 1 503 ? -1.196  70.341  90.892  1.00 79.67  ?  625 LEU   A C   1 
ATOM   3604 O O   . LEU   A 1 503 ? -0.271  69.748  91.461  1.00 79.79  ?  625 LEU   A O   1 
ATOM   3605 C CB  . LEU   A 1 503 ? -0.674  72.623  91.638  1.00 79.56  ?  625 LEU   A CB  1 
ATOM   3606 C CG  . LEU   A 1 503 ? -0.972  74.089  91.899  1.00 78.08  ?  625 LEU   A CG  1 
ATOM   3607 C CD1 . LEU   A 1 503 ? 0.318   74.775  92.309  1.00 72.88  ?  625 LEU   A CD1 1 
ATOM   3608 C CD2 . LEU   A 1 503 ? -1.549  74.686  90.668  1.00 74.09  ?  625 LEU   A CD2 1 
ATOM   3609 N N   . PRO   A 1 504 ? -1.712  69.920  89.738  1.00 80.30  ?  626 PRO   A N   1 
ATOM   3610 C CA  . PRO   A 1 504 ? -1.095  68.876  88.904  1.00 80.74  ?  626 PRO   A CA  1 
ATOM   3611 C C   . PRO   A 1 504 ? 0.414   68.799  88.790  1.00 79.67  ?  626 PRO   A C   1 
ATOM   3612 O O   . PRO   A 1 504 ? 1.050   69.820  88.510  1.00 78.42  ?  626 PRO   A O   1 
ATOM   3613 C CB  . PRO   A 1 504 ? -1.618  69.249  87.517  1.00 79.94  ?  626 PRO   A CB  1 
ATOM   3614 C CG  . PRO   A 1 504 ? -2.988  69.722  87.822  1.00 80.86  ?  626 PRO   A CG  1 
ATOM   3615 C CD  . PRO   A 1 504 ? -2.810  70.585  89.033  1.00 81.24  ?  626 PRO   A CD  1 
ATOM   3616 N N   . LEU   A 1 505 ? 0.994   67.598  88.968  1.00 77.42  ?  627 LEU   A N   1 
ATOM   3617 C CA  . LEU   A 1 505 ? 2.453   67.487  88.931  1.00 79.00  ?  627 LEU   A CA  1 
ATOM   3618 C C   . LEU   A 1 505 ? 3.121   68.171  87.737  1.00 81.25  ?  627 LEU   A C   1 
ATOM   3619 O O   . LEU   A 1 505 ? 4.247   68.663  87.861  1.00 80.96  ?  627 LEU   A O   1 
ATOM   3620 C CB  . LEU   A 1 505 ? 2.895   66.022  89.017  1.00 78.57  ?  627 LEU   A CB  1 
ATOM   3621 C CG  . LEU   A 1 505 ? 4.395   65.766  88.734  1.00 78.80  ?  627 LEU   A CG  1 
ATOM   3622 C CD1 . LEU   A 1 505 ? 5.356   66.429  89.703  1.00 77.06  ?  627 LEU   A CD1 1 
ATOM   3623 C CD2 . LEU   A 1 505 ? 4.722   64.308  88.634  1.00 84.65  ?  627 LEU   A CD2 1 
ATOM   3624 N N   . GLY   A 1 506 ? 2.452   68.228  86.579  1.00 81.44  ?  628 GLY   A N   1 
ATOM   3625 C CA  . GLY   A 1 506 ? 3.012   68.962  85.451  1.00 77.93  ?  628 GLY   A CA  1 
ATOM   3626 C C   . GLY   A 1 506 ? 3.194   70.437  85.755  1.00 80.39  ?  628 GLY   A C   1 
ATOM   3627 O O   . GLY   A 1 506 ? 4.220   71.033  85.406  1.00 77.35  ?  628 GLY   A O   1 
ATOM   3628 N N   . VAL   A 1 507 ? 2.200   71.039  86.419  1.00 84.65  ?  629 VAL   A N   1 
ATOM   3629 C CA  . VAL   A 1 507 ? 2.280   72.441  86.817  1.00 81.03  ?  629 VAL   A CA  1 
ATOM   3630 C C   . VAL   A 1 507 ? 3.440   72.635  87.775  1.00 77.10  ?  629 VAL   A C   1 
ATOM   3631 O O   . VAL   A 1 507 ? 4.313   73.494  87.574  1.00 79.93  ?  629 VAL   A O   1 
ATOM   3632 C CB  . VAL   A 1 507 ? 0.954   72.887  87.456  1.00 75.45  ?  629 VAL   A CB  1 
ATOM   3633 C CG1 . VAL   A 1 507 ? 1.046   74.360  87.908  1.00 77.27  ?  629 VAL   A CG1 1 
ATOM   3634 C CG2 . VAL   A 1 507 ? -0.233  72.596  86.519  1.00 74.43  ?  629 VAL   A CG2 1 
ATOM   3635 N N   . LEU   A 1 508 ? 3.472   71.817  88.827  1.00 71.15  ?  630 LEU   A N   1 
ATOM   3636 C CA  . LEU   A 1 508 ? 4.544   71.884  89.808  1.00 74.80  ?  630 LEU   A CA  1 
ATOM   3637 C C   . LEU   A 1 508 ? 5.910   71.724  89.185  1.00 79.03  ?  630 LEU   A C   1 
ATOM   3638 O O   . LEU   A 1 508 ? 6.910   72.045  89.839  1.00 77.85  ?  630 LEU   A O   1 
ATOM   3639 C CB  . LEU   A 1 508 ? 4.390   70.799  90.857  1.00 74.35  ?  630 LEU   A CB  1 
ATOM   3640 C CG  . LEU   A 1 508 ? 3.345   70.923  91.926  1.00 69.15  ?  630 LEU   A CG  1 
ATOM   3641 C CD1 . LEU   A 1 508 ? 3.515   69.672  92.733  1.00 66.96  ?  630 LEU   A CD1 1 
ATOM   3642 C CD2 . LEU   A 1 508 ? 3.630   72.155  92.737  1.00 61.43  ?  630 LEU   A CD2 1 
ATOM   3643 N N   . LYS   A 1 509 ? 5.975   71.188  87.964  1.00 79.52  ?  631 LYS   A N   1 
ATOM   3644 C CA  . LYS   A 1 509 ? 7.250   70.897  87.333  1.00 79.47  ?  631 LYS   A CA  1 
ATOM   3645 C C   . LYS   A 1 509 ? 7.762   72.049  86.508  1.00 84.27  ?  631 LYS   A C   1 
ATOM   3646 O O   . LYS   A 1 509 ? 8.956   72.044  86.182  1.00 83.90  ?  631 LYS   A O   1 
ATOM   3647 C CB  . LYS   A 1 509 ? 7.155   69.654  86.440  1.00 79.06  ?  631 LYS   A CB  1 
ATOM   3648 C CG  . LYS   A 1 509 ? 7.638   68.354  87.087  1.00 79.28  ?  631 LYS   A CG  1 
ATOM   3649 C CD  . LYS   A 1 509 ? 7.050   67.111  86.437  1.00 71.59  ?  631 LYS   A CD  1 
ATOM   3650 C CE  . LYS   A 1 509 ? 7.906   65.921  86.730  1.00 77.29  ?  631 LYS   A CE  1 
ATOM   3651 N NZ  . LYS   A 1 509 ? 9.311   66.152  86.285  1.00 76.65  ?  631 LYS   A NZ  1 
ATOM   3652 N N   . GLN   A 1 510 ? 6.888   73.027  86.188  1.00 92.29  ?  632 GLN   A N   1 
ATOM   3653 C CA  . GLN   A 1 510 ? 7.215   74.111  85.257  1.00 93.36  ?  632 GLN   A CA  1 
ATOM   3654 C C   . GLN   A 1 510 ? 8.501   74.814  85.641  1.00 94.01  ?  632 GLN   A C   1 
ATOM   3655 O O   . GLN   A 1 510 ? 8.703   75.173  86.803  1.00 89.93  ?  632 GLN   A O   1 
ATOM   3656 C CB  . GLN   A 1 510 ? 6.106   75.159  85.189  1.00 88.72  ?  632 GLN   A CB  1 
ATOM   3657 C CG  . GLN   A 1 510 ? 4.862   74.846  84.380  1.00 95.71  ?  632 GLN   A CG  1 
ATOM   3658 C CD  . GLN   A 1 510 ? 4.159   76.159  83.911  1.00 102.07 ?  632 GLN   A CD  1 
ATOM   3659 O OE1 . GLN   A 1 510 ? 2.912   76.254  83.836  1.00 96.36  ?  632 GLN   A OE1 1 
ATOM   3660 N NE2 . GLN   A 1 510 ? 4.978   77.180  83.601  1.00 95.04  ?  632 GLN   A NE2 1 
ATOM   3661 N N   . GLN   A 1 511 ? 9.371   74.986  84.652  1.00 99.63  ?  633 GLN   A N   1 
ATOM   3662 C CA  . GLN   A 1 511 ? 10.526  75.880  84.736  1.00 101.29 ?  633 GLN   A CA  1 
ATOM   3663 C C   . GLN   A 1 511 ? 10.443  76.840  83.559  1.00 110.69 ?  633 GLN   A C   1 
ATOM   3664 O O   . GLN   A 1 511 ? 10.575  76.413  82.391  1.00 113.90 ?  633 GLN   A O   1 
ATOM   3665 C CB  . GLN   A 1 511 ? 11.864  75.138  84.722  1.00 100.38 ?  633 GLN   A CB  1 
ATOM   3666 C CG  . GLN   A 1 511 ? 12.284  74.651  86.092  1.00 105.01 ?  633 GLN   A CG  1 
ATOM   3667 C CD  . GLN   A 1 511 ? 11.715  75.504  87.237  1.00 106.50 ?  633 GLN   A CD  1 
ATOM   3668 O OE1 . GLN   A 1 511 ? 12.043  76.693  87.392  1.00 105.83 ?  633 GLN   A OE1 1 
ATOM   3669 N NE2 . GLN   A 1 511 ? 10.837  74.890  88.038  1.00 103.72 ?  633 GLN   A NE2 1 
ATOM   3670 N N   . PRO   A 1 512 ? 10.228  78.132  83.813  1.00 104.81 ?  634 PRO   A N   1 
ATOM   3671 C CA  . PRO   A 1 512 ? 10.168  78.657  85.178  1.00 96.57  ?  634 PRO   A CA  1 
ATOM   3672 C C   . PRO   A 1 512 ? 8.728   78.772  85.735  1.00 90.34  ?  634 PRO   A C   1 
ATOM   3673 O O   . PRO   A 1 512 ? 7.758   78.805  84.965  1.00 89.71  ?  634 PRO   A O   1 
ATOM   3674 C CB  . PRO   A 1 512 ? 10.856  80.012  85.029  1.00 102.78 ?  634 PRO   A CB  1 
ATOM   3675 C CG  . PRO   A 1 512 ? 10.575  80.416  83.599  1.00 111.62 ?  634 PRO   A CG  1 
ATOM   3676 C CD  . PRO   A 1 512 ? 10.150  79.201  82.814  1.00 103.81 ?  634 PRO   A CD  1 
ATOM   3677 N N   . PRO   A 1 513 ? 8.624   78.858  87.062  1.00 78.80  ?  635 PRO   A N   1 
ATOM   3678 C CA  . PRO   A 1 513 ? 7.431   78.382  87.792  1.00 83.75  ?  635 PRO   A CA  1 
ATOM   3679 C C   . PRO   A 1 513 ? 6.135   79.149  87.555  1.00 76.68  ?  635 PRO   A C   1 
ATOM   3680 O O   . PRO   A 1 513 ? 5.998   80.290  87.971  1.00 80.78  ?  635 PRO   A O   1 
ATOM   3681 C CB  . PRO   A 1 513 ? 7.865   78.497  89.256  1.00 85.10  ?  635 PRO   A CB  1 
ATOM   3682 C CG  . PRO   A 1 513 ? 9.330   78.323  89.205  1.00 85.81  ?  635 PRO   A CG  1 
ATOM   3683 C CD  . PRO   A 1 513 ? 9.794   78.949  87.943  1.00 79.34  ?  635 PRO   A CD  1 
ATOM   3684 N N   . ALA   A 1 514 ? 5.142   78.462  86.995  1.00 77.21  ?  636 ALA   A N   1 
ATOM   3685 C CA  . ALA   A 1 514 ? 3.772   78.960  86.990  1.00 74.93  ?  636 ALA   A CA  1 
ATOM   3686 C C   . ALA   A 1 514 ? 3.342   79.463  88.356  1.00 81.46  ?  636 ALA   A C   1 
ATOM   3687 O O   . ALA   A 1 514 ? 2.575   80.431  88.446  1.00 85.39  ?  636 ALA   A O   1 
ATOM   3688 C CB  . ALA   A 1 514 ? 2.803   77.857  86.548  1.00 88.22  ?  636 ALA   A CB  1 
ATOM   3689 N N   . VAL   A 1 515 ? 3.774   78.788  89.430  1.00 80.45  ?  637 VAL   A N   1 
ATOM   3690 C CA  . VAL   A 1 515 ? 3.448   79.187  90.799  1.00 76.04  ?  637 VAL   A CA  1 
ATOM   3691 C C   . VAL   A 1 515 ? 4.731   79.241  91.614  1.00 78.67  ?  637 VAL   A C   1 
ATOM   3692 O O   . VAL   A 1 515 ? 5.509   78.279  91.638  1.00 78.69  ?  637 VAL   A O   1 
ATOM   3693 C CB  . VAL   A 1 515 ? 2.413   78.266  91.461  1.00 69.08  ?  637 VAL   A CB  1 
ATOM   3694 C CG1 . VAL   A 1 515 ? 2.393   78.489  92.911  1.00 73.21  ?  637 VAL   A CG1 1 
ATOM   3695 C CG2 . VAL   A 1 515 ? 1.059   78.600  90.970  1.00 70.75  ?  637 VAL   A CG2 1 
ATOM   3696 N N   . GLN   A 1 516 ? 4.942   80.375  92.267  1.00 81.67  ?  638 GLN   A N   1 
ATOM   3697 C CA  . GLN   A 1 516 ? 6.089   80.666  93.114  1.00 84.37  ?  638 GLN   A CA  1 
ATOM   3698 C C   . GLN   A 1 516 ? 5.772   80.313  94.558  1.00 85.74  ?  638 GLN   A C   1 
ATOM   3699 O O   . GLN   A 1 516 ? 4.725   80.710  95.086  1.00 82.39  ?  638 GLN   A O   1 
ATOM   3700 C CB  . GLN   A 1 516 ? 6.406   82.158  93.006  1.00 92.19  ?  638 GLN   A CB  1 
ATOM   3701 C CG  . GLN   A 1 516 ? 7.389   82.732  94.010  1.00 93.57  ?  638 GLN   A CG  1 
ATOM   3702 C CD  . GLN   A 1 516 ? 8.166   83.904  93.442  1.00 107.53 ?  638 GLN   A CD  1 
ATOM   3703 O OE1 . GLN   A 1 516 ? 7.587   84.872  92.902  1.00 110.87 ?  638 GLN   A OE1 1 
ATOM   3704 N NE2 . GLN   A 1 516 ? 9.480   83.853  93.600  1.00 116.78 ?  638 GLN   A NE2 1 
ATOM   3705 N N   . PHE   A 1 517 ? 6.687   79.611  95.213  1.00 86.68  ?  639 PHE   A N   1 
ATOM   3706 C CA  . PHE   A 1 517 ? 6.495   79.255  96.614  1.00 85.67  ?  639 PHE   A CA  1 
ATOM   3707 C C   . PHE   A 1 517 ? 7.389   80.110  97.515  1.00 83.52  ?  639 PHE   A C   1 
ATOM   3708 O O   . PHE   A 1 517 ? 8.613   80.196  97.320  1.00 78.40  ?  639 PHE   A O   1 
ATOM   3709 C CB  . PHE   A 1 517 ? 6.726   77.753  96.831  1.00 85.09  ?  639 PHE   A CB  1 
ATOM   3710 C CG  . PHE   A 1 517 ? 5.524   76.907  96.459  1.00 85.08  ?  639 PHE   A CG  1 
ATOM   3711 C CD1 . PHE   A 1 517 ? 4.510   76.670  97.386  1.00 82.08  ?  639 PHE   A CD1 1 
ATOM   3712 C CD2 . PHE   A 1 517 ? 5.391   76.387  95.179  1.00 82.24  ?  639 PHE   A CD2 1 
ATOM   3713 C CE1 . PHE   A 1 517 ? 3.405   75.921  97.057  1.00 76.07  ?  639 PHE   A CE1 1 
ATOM   3714 C CE2 . PHE   A 1 517 ? 4.287   75.635  94.841  1.00 77.29  ?  639 PHE   A CE2 1 
ATOM   3715 C CZ  . PHE   A 1 517 ? 3.297   75.400  95.779  1.00 80.50  ?  639 PHE   A CZ  1 
ATOM   3716 N N   . VAL   A 1 518 ? 6.761   80.761  98.489  1.00 81.93  ?  640 VAL   A N   1 
ATOM   3717 C CA  . VAL   A 1 518 ? 7.480   81.617  99.425  1.00 78.90  ?  640 VAL   A CA  1 
ATOM   3718 C C   . VAL   A 1 518 ? 7.172   81.188  100.857 1.00 82.17  ?  640 VAL   A C   1 
ATOM   3719 O O   . VAL   A 1 518 ? 6.052   81.415  101.367 1.00 73.90  ?  640 VAL   A O   1 
ATOM   3720 C CB  . VAL   A 1 518 ? 7.150   83.090  99.183  1.00 79.64  ?  640 VAL   A CB  1 
ATOM   3721 C CG1 . VAL   A 1 518 ? 7.546   83.903  100.371 1.00 81.22  ?  640 VAL   A CG1 1 
ATOM   3722 C CG2 . VAL   A 1 518 ? 7.899   83.561  97.970  1.00 86.10  ?  640 VAL   A CG2 1 
ATOM   3723 N N   . PRO   A 1 519 ? 8.157   80.564  101.552 1.00 82.46  ?  641 PRO   A N   1 
ATOM   3724 C CA  . PRO   A 1 519 ? 9.525   80.332  101.029 1.00 76.54  ?  641 PRO   A CA  1 
ATOM   3725 C C   . PRO   A 1 519 ? 9.591   79.205  99.977  1.00 81.58  ?  641 PRO   A C   1 
ATOM   3726 O O   . PRO   A 1 519 ? 8.564   78.587  99.704  1.00 82.75  ?  641 PRO   A O   1 
ATOM   3727 C CB  . PRO   A 1 519 ? 10.312  79.967  102.284 1.00 65.66  ?  641 PRO   A CB  1 
ATOM   3728 C CG  . PRO   A 1 519 ? 9.308   79.431  103.207 1.00 71.02  ?  641 PRO   A CG  1 
ATOM   3729 C CD  . PRO   A 1 519 ? 8.005   80.087  102.939 1.00 73.13  ?  641 PRO   A CD  1 
ATOM   3730 N N   . PRO   A 1 520 ? 10.754  78.933  99.383  1.00 79.81  ?  642 PRO   A N   1 
ATOM   3731 C CA  . PRO   A 1 520 ? 10.806  77.883  98.370  1.00 81.13  ?  642 PRO   A CA  1 
ATOM   3732 C C   . PRO   A 1 520 ? 10.422  76.530  98.959  1.00 84.69  ?  642 PRO   A C   1 
ATOM   3733 O O   . PRO   A 1 520 ? 10.539  76.281  100.166 1.00 83.50  ?  642 PRO   A O   1 
ATOM   3734 C CB  . PRO   A 1 520 ? 12.278  77.890  97.938  1.00 77.47  ?  642 PRO   A CB  1 
ATOM   3735 C CG  . PRO   A 1 520 ? 12.746  79.166  98.275  1.00 73.34  ?  642 PRO   A CG  1 
ATOM   3736 C CD  . PRO   A 1 520 ? 12.105  79.459  99.594  1.00 80.51  ?  642 PRO   A CD  1 
ATOM   3737 N N   . LEU   A 1 521 ? 9.967   75.640  98.082  1.00 85.87  ?  643 LEU   A N   1 
ATOM   3738 C CA  . LEU   A 1 521 ? 9.769   74.259  98.491  1.00 79.72  ?  643 LEU   A CA  1 
ATOM   3739 C C   . LEU   A 1 521 ? 11.130  73.623  98.758  1.00 78.67  ?  643 LEU   A C   1 
ATOM   3740 O O   . LEU   A 1 521 ? 12.057  73.784  97.944  1.00 78.14  ?  643 LEU   A O   1 
ATOM   3741 C CB  . LEU   A 1 521 ? 8.985   73.505  97.419  1.00 78.82  ?  643 LEU   A CB  1 
ATOM   3742 C CG  . LEU   A 1 521 ? 7.546   74.024  97.465  1.00 77.45  ?  643 LEU   A CG  1 
ATOM   3743 C CD1 . LEU   A 1 521 ? 6.692   73.469  96.363  1.00 67.35  ?  643 LEU   A CD1 1 
ATOM   3744 C CD2 . LEU   A 1 521 ? 6.942   73.724  98.841  1.00 77.05  ?  643 LEU   A CD2 1 
ATOM   3745 N N   . PRO   A 1 522 ? 11.293  72.922  99.886  1.00 79.57  ?  644 PRO   A N   1 
ATOM   3746 C CA  . PRO   A 1 522 ? 12.601  72.338  100.255 1.00 79.77  ?  644 PRO   A CA  1 
ATOM   3747 C C   . PRO   A 1 522 ? 13.095  71.331  99.232  1.00 84.20  ?  644 PRO   A C   1 
ATOM   3748 O O   . PRO   A 1 522 ? 12.312  70.724  98.494  1.00 84.60  ?  644 PRO   A O   1 
ATOM   3749 C CB  . PRO   A 1 522 ? 12.315  71.639  101.579 1.00 73.17  ?  644 PRO   A CB  1 
ATOM   3750 C CG  . PRO   A 1 522 ? 10.813  71.438  101.562 1.00 72.61  ?  644 PRO   A CG  1 
ATOM   3751 C CD  . PRO   A 1 522 ? 10.222  72.580  100.832 1.00 70.98  ?  644 PRO   A CD  1 
ATOM   3752 N N   . GLU   A 1 523 ? 14.416  71.125  99.211  1.00 84.80  ?  645 GLU   A N   1 
ATOM   3753 C CA  . GLU   A 1 523 ? 14.982  70.230  98.199  1.00 94.22  ?  645 GLU   A CA  1 
ATOM   3754 C C   . GLU   A 1 523 ? 14.320  68.849  98.179  1.00 92.24  ?  645 GLU   A C   1 
ATOM   3755 O O   . GLU   A 1 523 ? 13.984  68.319  97.110  1.00 90.49  ?  645 GLU   A O   1 
ATOM   3756 C CB  . GLU   A 1 523 ? 16.477  70.056  98.390  1.00 103.38 ?  645 GLU   A CB  1 
ATOM   3757 C CG  . GLU   A 1 523 ? 16.864  68.673  97.902  1.00 110.01 ?  645 GLU   A CG  1 
ATOM   3758 C CD  . GLU   A 1 523 ? 18.251  68.602  97.395  1.00 133.57 ?  645 GLU   A CD  1 
ATOM   3759 O OE1 . GLU   A 1 523 ? 18.892  69.688  97.337  1.00 141.64 ?  645 GLU   A OE1 1 
ATOM   3760 O OE2 . GLU   A 1 523 ? 18.694  67.460  97.090  1.00 138.96 ?  645 GLU   A OE2 1 
ATOM   3761 N N   . TRP   A 1 524 ? 14.149  68.234  99.348  1.00 85.07  ?  646 TRP   A N   1 
ATOM   3762 C CA  . TRP   A 1 524 ? 13.529  66.924  99.352  1.00 79.03  ?  646 TRP   A CA  1 
ATOM   3763 C C   . TRP   A 1 524 ? 12.215  66.897  98.573  1.00 82.20  ?  646 TRP   A C   1 
ATOM   3764 O O   . TRP   A 1 524 ? 11.862  65.863  98.002  1.00 85.97  ?  646 TRP   A O   1 
ATOM   3765 C CB  . TRP   A 1 524 ? 13.305  66.452  100.772 1.00 68.93  ?  646 TRP   A CB  1 
ATOM   3766 C CG  . TRP   A 1 524 ? 12.365  67.199  101.608 1.00 70.07  ?  646 TRP   A CG  1 
ATOM   3767 C CD1 . TRP   A 1 524 ? 12.676  68.112  102.551 1.00 75.84  ?  646 TRP   A CD1 1 
ATOM   3768 C CD2 . TRP   A 1 524 ? 10.943  67.041  101.653 1.00 75.35  ?  646 TRP   A CD2 1 
ATOM   3769 N NE1 . TRP   A 1 524 ? 11.539  68.558  103.175 1.00 75.75  ?  646 TRP   A NE1 1 
ATOM   3770 C CE2 . TRP   A 1 524 ? 10.457  67.914  102.641 1.00 73.06  ?  646 TRP   A CE2 1 
ATOM   3771 C CE3 . TRP   A 1 524 ? 10.030  66.260  100.938 1.00 79.71  ?  646 TRP   A CE3 1 
ATOM   3772 C CZ2 . TRP   A 1 524 ? 9.095   68.037  102.938 1.00 74.79  ?  646 TRP   A CZ2 1 
ATOM   3773 C CZ3 . TRP   A 1 524 ? 8.667   66.379  101.243 1.00 83.54  ?  646 TRP   A CZ3 1 
ATOM   3774 C CH2 . TRP   A 1 524 ? 8.219   67.263  102.238 1.00 79.28  ?  646 TRP   A CH2 1 
ATOM   3775 N N   . LYS   A 1 525 ? 11.493  68.014  98.508  1.00 79.39  ?  647 LYS   A N   1 
ATOM   3776 C CA  . LYS   A 1 525 ? 10.250  68.024  97.759  1.00 74.55  ?  647 LYS   A CA  1 
ATOM   3777 C C   . LYS   A 1 525 ? 10.446  68.437  96.317  1.00 78.02  ?  647 LYS   A C   1 
ATOM   3778 O O   . LYS   A 1 525 ? 9.741   67.924  95.441  1.00 77.57  ?  647 LYS   A O   1 
ATOM   3779 C CB  . LYS   A 1 525 ? 9.231   68.933  98.434  1.00 71.30  ?  647 LYS   A CB  1 
ATOM   3780 C CG  . LYS   A 1 525 ? 8.049   69.287  97.582  1.00 70.20  ?  647 LYS   A CG  1 
ATOM   3781 C CD  . LYS   A 1 525 ? 6.920   68.300  97.708  1.00 75.04  ?  647 LYS   A CD  1 
ATOM   3782 C CE  . LYS   A 1 525 ? 6.259   68.327  99.077  1.00 79.21  ?  647 LYS   A CE  1 
ATOM   3783 N NZ  . LYS   A 1 525 ? 5.334   67.153  99.403  1.00 77.56  ?  647 LYS   A NZ  1 
ATOM   3784 N N   . THR   A 1 526 ? 11.395  69.332  96.033  1.00 83.21  ?  648 THR   A N   1 
ATOM   3785 C CA  . THR   A 1 526 ? 11.582  69.737  94.641  1.00 84.23  ?  648 THR   A CA  1 
ATOM   3786 C C   . THR   A 1 526 ? 12.193  68.598  93.849  1.00 81.39  ?  648 THR   A C   1 
ATOM   3787 O O   . THR   A 1 526 ? 11.838  68.391  92.684  1.00 82.67  ?  648 THR   A O   1 
ATOM   3788 C CB  . THR   A 1 526 ? 12.456  70.997  94.513  1.00 84.76  ?  648 THR   A CB  1 
ATOM   3789 O OG1 . THR   A 1 526 ? 13.755  70.765  95.067  1.00 92.46  ?  648 THR   A OG1 1 
ATOM   3790 C CG2 . THR   A 1 526 ? 11.838  72.168  95.266  1.00 80.93  ?  648 THR   A CG2 1 
ATOM   3791 N N   . SER   A 1 527 ? 13.090  67.829  94.481  1.00 83.78  ?  649 SER   A N   1 
ATOM   3792 C CA  . SER   A 1 527 ? 13.724  66.707  93.796  1.00 85.12  ?  649 SER   A CA  1 
ATOM   3793 C C   . SER   A 1 527 ? 12.739  65.577  93.582  1.00 80.56  ?  649 SER   A C   1 
ATOM   3794 O O   . SER   A 1 527 ? 12.771  64.907  92.545  1.00 79.77  ?  649 SER   A O   1 
ATOM   3795 C CB  . SER   A 1 527 ? 14.942  66.225  94.571  1.00 87.24  ?  649 SER   A CB  1 
ATOM   3796 O OG  . SER   A 1 527 ? 15.863  67.285  94.721  1.00 100.17 ?  649 SER   A OG  1 
ATOM   3797 N N   . ALA   A 1 528 ? 11.841  65.364  94.536  1.00 79.32  ?  650 ALA   A N   1 
ATOM   3798 C CA  . ALA   A 1 528 ? 10.752  64.437  94.293  1.00 76.52  ?  650 ALA   A CA  1 
ATOM   3799 C C   . ALA   A 1 528 ? 9.865   64.909  93.169  1.00 77.64  ?  650 ALA   A C   1 
ATOM   3800 O O   . ALA   A 1 528 ? 9.141   64.101  92.596  1.00 84.70  ?  650 ALA   A O   1 
ATOM   3801 C CB  . ALA   A 1 528 ? 9.909   64.243  95.546  1.00 80.33  ?  650 ALA   A CB  1 
ATOM   3802 N N   . VAL   A 1 529 ? 9.885   66.195  92.844  1.00 79.94  ?  651 VAL   A N   1 
ATOM   3803 C CA  . VAL   A 1 529 ? 9.073   66.644  91.722  1.00 82.27  ?  651 VAL   A CA  1 
ATOM   3804 C C   . VAL   A 1 529 ? 9.795   66.403  90.406  1.00 83.26  ?  651 VAL   A C   1 
ATOM   3805 O O   . VAL   A 1 529 ? 9.190   65.921  89.443  1.00 83.13  ?  651 VAL   A O   1 
ATOM   3806 C CB  . VAL   A 1 529 ? 8.663   68.114  91.906  1.00 82.39  ?  651 VAL   A CB  1 
ATOM   3807 C CG1 . VAL   A 1 529 ? 7.940   68.619  90.678  1.00 79.06  ?  651 VAL   A CG1 1 
ATOM   3808 C CG2 . VAL   A 1 529 ? 7.750   68.238  93.115  1.00 75.88  ?  651 VAL   A CG2 1 
ATOM   3809 N N   . GLN   A 1 530 ? 11.100  66.684  90.349  1.00 84.01  ?  652 GLN   A N   1 
ATOM   3810 C CA  . GLN   A 1 530 ? 11.837  66.418  89.118  1.00 90.46  ?  652 GLN   A CA  1 
ATOM   3811 C C   . GLN   A 1 530 ? 11.888  64.929  88.788  1.00 86.96  ?  652 GLN   A C   1 
ATOM   3812 O O   . GLN   A 1 530 ? 11.774  64.543  87.610  1.00 89.47  ?  652 GLN   A O   1 
ATOM   3813 C CB  . GLN   A 1 530 ? 13.248  67.000  89.187  1.00 93.58  ?  652 GLN   A CB  1 
ATOM   3814 C CG  . GLN   A 1 530 ? 13.307  68.400  88.604  1.00 113.06 ?  652 GLN   A CG  1 
ATOM   3815 C CD  . GLN   A 1 530 ? 14.700  68.992  88.619  1.00 133.20 ?  652 GLN   A CD  1 
ATOM   3816 O OE1 . GLN   A 1 530 ? 15.690  68.259  88.728  1.00 138.14 ?  652 GLN   A OE1 1 
ATOM   3817 N NE2 . GLN   A 1 530 ? 14.792  70.321  88.464  1.00 132.43 ?  652 GLN   A NE2 1 
ATOM   3818 N N   . ARG   A 1 531 ? 12.064  64.080  89.807  1.00 79.78  ?  653 ARG   A N   1 
ATOM   3819 C CA  . ARG   A 1 531 ? 12.264  62.659  89.547  1.00 79.23  ?  653 ARG   A CA  1 
ATOM   3820 C C   . ARG   A 1 531 ? 11.022  62.025  88.959  1.00 81.81  ?  653 ARG   A C   1 
ATOM   3821 O O   . ARG   A 1 531 ? 11.115  61.202  88.038  1.00 83.63  ?  653 ARG   A O   1 
ATOM   3822 C CB  . ARG   A 1 531 ? 12.652  61.924  90.819  1.00 82.96  ?  653 ARG   A CB  1 
ATOM   3823 C CG  . ARG   A 1 531 ? 14.130  61.955  91.160  1.00 85.89  ?  653 ARG   A CG  1 
ATOM   3824 C CD  . ARG   A 1 531 ? 14.450  61.004  92.309  1.00 80.34  ?  653 ARG   A CD  1 
ATOM   3825 N NE  . ARG   A 1 531 ? 13.630  61.250  93.491  1.00 75.79  ?  653 ARG   A NE  1 
ATOM   3826 C CZ  . ARG   A 1 531 ? 13.948  62.126  94.431  1.00 84.85  ?  653 ARG   A CZ  1 
ATOM   3827 N NH1 . ARG   A 1 531 ? 15.044  62.868  94.329  1.00 92.59  ?  653 ARG   A NH1 1 
ATOM   3828 N NH2 . ARG   A 1 531 ? 13.145  62.272  95.492  1.00 80.72  ?  653 ARG   A NH2 1 
ATOM   3829 N N   . MET   A 1 532 ? 9.855   62.396  89.470  1.00 79.76  ?  654 MET   A N   1 
ATOM   3830 C CA  . MET   A 1 532 ? 8.634   61.710  89.085  1.00 84.91  ?  654 MET   A CA  1 
ATOM   3831 C C   . MET   A 1 532 ? 8.314   61.941  87.619  1.00 83.92  ?  654 MET   A C   1 
ATOM   3832 O O   . MET   A 1 532 ? 8.833   62.844  86.959  1.00 83.07  ?  654 MET   A O   1 
ATOM   3833 C CB  . MET   A 1 532 ? 7.471   62.188  89.917  1.00 85.75  ?  654 MET   A CB  1 
ATOM   3834 C CG  . MET   A 1 532 ? 7.408   61.552  91.277  1.00 94.46  ?  654 MET   A CG  1 
ATOM   3835 S SD  . MET   A 1 532 ? 5.774   61.852  91.964  1.00 111.73 ?  654 MET   A SD  1 
ATOM   3836 C CE  . MET   A 1 532 ? 4.869   61.074  90.599  1.00 100.50 ?  654 MET   A CE  1 
ATOM   3837 N N   . GLY   A 1 533 ? 7.440   61.096  87.104  1.00 86.48  ?  655 GLY   A N   1 
ATOM   3838 C CA  . GLY   A 1 533 ? 7.101   61.123  85.704  1.00 85.00  ?  655 GLY   A CA  1 
ATOM   3839 C C   . GLY   A 1 533 ? 5.795   61.879  85.505  1.00 83.31  ?  655 GLY   A C   1 
ATOM   3840 O O   . GLY   A 1 533 ? 4.838   61.681  86.242  1.00 86.72  ?  655 GLY   A O   1 
ATOM   3841 N N   . PHE   A 1 534 ? 5.786   62.757  84.529  1.00 81.60  ?  656 PHE   A N   1 
ATOM   3842 C CA  . PHE   A 1 534 ? 4.515   63.282  84.087  1.00 83.96  ?  656 PHE   A CA  1 
ATOM   3843 C C   . PHE   A 1 534 ? 4.462   63.066  82.589  1.00 85.53  ?  656 PHE   A C   1 
ATOM   3844 O O   . PHE   A 1 534 ? 5.417   63.381  81.873  1.00 86.52  ?  656 PHE   A O   1 
ATOM   3845 C CB  . PHE   A 1 534 ? 4.314   64.751  84.500  1.00 81.17  ?  656 PHE   A CB  1 
ATOM   3846 C CG  . PHE   A 1 534 ? 2.867   65.115  84.710  1.00 79.48  ?  656 PHE   A CG  1 
ATOM   3847 C CD1 . PHE   A 1 534 ? 2.159   64.586  85.763  1.00 85.06  ?  656 PHE   A CD1 1 
ATOM   3848 C CD2 . PHE   A 1 534 ? 2.205   65.956  83.843  1.00 81.03  ?  656 PHE   A CD2 1 
ATOM   3849 C CE1 . PHE   A 1 534 ? 0.809   64.899  85.948  1.00 87.25  ?  656 PHE   A CE1 1 
ATOM   3850 C CE2 . PHE   A 1 534 ? 0.872   66.275  84.032  1.00 79.61  ?  656 PHE   A CE2 1 
ATOM   3851 C CZ  . PHE   A 1 534 ? 0.173   65.744  85.071  1.00 81.30  ?  656 PHE   A CZ  1 
ATOM   3852 N N   . GLY   A 1 535 ? 3.379   62.450  82.142  1.00 83.62  ?  657 GLY   A N   1 
ATOM   3853 C CA  . GLY   A 1 535 ? 3.267   62.010  80.779  1.00 88.70  ?  657 GLY   A CA  1 
ATOM   3854 C C   . GLY   A 1 535 ? 2.062   62.604  80.100  1.00 89.79  ?  657 GLY   A C   1 
ATOM   3855 O O   . GLY   A 1 535 ? 1.400   63.476  80.656  1.00 88.90  ?  657 GLY   A O   1 
ATOM   3856 N N   . ASN   A 1 536 ? 1.748   62.092  78.913  1.00 95.48  ?  658 ASN   A N   1 
ATOM   3857 C CA  . ASN   A 1 536 ? 0.876   62.738  77.944  1.00 89.93  ?  658 ASN   A CA  1 
ATOM   3858 C C   . ASN   A 1 536 ? 0.108   61.649  77.200  1.00 90.91  ?  658 ASN   A C   1 
ATOM   3859 O O   . ASN   A 1 536 ? 0.655   60.575  76.913  1.00 94.61  ?  658 ASN   A O   1 
ATOM   3860 C CB  . ASN   A 1 536 ? 1.730   63.598  76.989  1.00 90.86  ?  658 ASN   A CB  1 
ATOM   3861 C CG  . ASN   A 1 536 ? 0.918   64.567  76.135  1.00 93.15  ?  658 ASN   A CG  1 
ATOM   3862 O OD1 . ASN   A 1 536 ? -0.297  64.724  76.295  1.00 91.87  ?  658 ASN   A OD1 1 
ATOM   3863 N ND2 . ASN   A 1 536 ? 1.607   65.224  75.203  1.00 91.17  ?  658 ASN   A ND2 1 
ATOM   3864 N N   . LEU   A 1 537 ? -1.173  61.905  76.948  1.00 85.91  ?  659 LEU   A N   1 
ATOM   3865 C CA  . LEU   A 1 537 ? -1.900  61.160  75.933  1.00 91.51  ?  659 LEU   A CA  1 
ATOM   3866 C C   . LEU   A 1 537 ? -3.147  61.960  75.629  1.00 91.39  ?  659 LEU   A C   1 
ATOM   3867 O O   . LEU   A 1 537 ? -3.761  62.483  76.548  1.00 94.09  ?  659 LEU   A O   1 
ATOM   3868 C CB  . LEU   A 1 537 ? -2.280  59.749  76.394  1.00 94.12  ?  659 LEU   A CB  1 
ATOM   3869 C CG  . LEU   A 1 537 ? -3.377  59.522  77.423  1.00 93.04  ?  659 LEU   A CG  1 
ATOM   3870 C CD1 . LEU   A 1 537 ? -4.780  59.500  76.776  1.00 87.37  ?  659 LEU   A CD1 1 
ATOM   3871 C CD2 . LEU   A 1 537 ? -3.081  58.275  78.170  1.00 107.31 ?  659 LEU   A CD2 1 
ATOM   3872 N N   . ASN   A 1 538 ? -3.533  62.022  74.357  1.00 95.03  ?  660 ASN   A N   1 
ATOM   3873 C CA  . ASN   A 1 538 ? -4.573  62.920  73.868  1.00 91.98  ?  660 ASN   A CA  1 
ATOM   3874 C C   . ASN   A 1 538 ? -5.680  62.136  73.165  1.00 94.90  ?  660 ASN   A C   1 
ATOM   3875 O O   . ASN   A 1 538 ? -5.472  61.010  72.708  1.00 102.12 ?  660 ASN   A O   1 
ATOM   3876 C CB  . ASN   A 1 538 ? -3.959  63.952  72.920  1.00 94.04  ?  660 ASN   A CB  1 
ATOM   3877 C CG  . ASN   A 1 538 ? -3.193  65.017  73.658  1.00 95.55  ?  660 ASN   A CG  1 
ATOM   3878 O OD1 . ASN   A 1 538 ? -3.780  65.777  74.416  1.00 95.67  ?  660 ASN   A OD1 1 
ATOM   3879 N ND2 . ASN   A 1 538 ? -1.871  65.057  73.473  1.00 95.66  ?  660 ASN   A ND2 1 
ATOM   3880 N N   . LYS   A 1 539 ? -6.866  62.733  73.064  1.00 90.30  ?  661 LYS   A N   1 
ATOM   3881 C CA  . LYS   A 1 539 ? -8.019  62.071  72.462  1.00 90.13  ?  661 LYS   A CA  1 
ATOM   3882 C C   . LYS   A 1 539 ? -8.576  62.934  71.339  1.00 100.28 ?  661 LYS   A C   1 
ATOM   3883 O O   . LYS   A 1 539 ? -8.638  64.158  71.489  1.00 109.85 ?  661 LYS   A O   1 
ATOM   3884 C CB  . LYS   A 1 539 ? -9.101  61.857  73.488  1.00 84.70  ?  661 LYS   A CB  1 
ATOM   3885 C CG  . LYS   A 1 539 ? -8.808  60.824  74.495  1.00 82.90  ?  661 LYS   A CG  1 
ATOM   3886 C CD  . LYS   A 1 539 ? -9.921  60.842  75.483  1.00 86.66  ?  661 LYS   A CD  1 
ATOM   3887 C CE  . LYS   A 1 539 ? -9.570  60.078  76.708  1.00 91.49  ?  661 LYS   A CE  1 
ATOM   3888 N NZ  . LYS   A 1 539 ? -10.732 59.255  77.094  1.00 102.85 ?  661 LYS   A NZ  1 
ATOM   3889 N N   . VAL   A 1 540 ? -8.994  62.324  70.218  1.00 101.81 ?  662 VAL   A N   1 
ATOM   3890 C CA  . VAL   A 1 540 ? -9.692  63.049  69.153  1.00 101.79 ?  662 VAL   A CA  1 
ATOM   3891 C C   . VAL   A 1 540 ? -11.149 62.610  69.155  1.00 104.08 ?  662 VAL   A C   1 
ATOM   3892 O O   . VAL   A 1 540 ? -11.442 61.409  69.209  1.00 104.66 ?  662 VAL   A O   1 
ATOM   3893 C CB  . VAL   A 1 540 ? -9.062  62.833  67.767  1.00 97.34  ?  662 VAL   A CB  1 
ATOM   3894 C CG1 . VAL   A 1 540 ? -9.697  63.787  66.784  1.00 98.77  ?  662 VAL   A CG1 1 
ATOM   3895 C CG2 . VAL   A 1 540 ? -7.572  63.052  67.793  1.00 96.98  ?  662 VAL   A CG2 1 
ATOM   3896 N N   . VAL   A 1 541 ? -12.061 63.579  69.117  1.00 103.74 ?  663 VAL   A N   1 
ATOM   3897 C CA  . VAL   A 1 541 ? -13.488 63.292  69.195  1.00 111.52 ?  663 VAL   A CA  1 
ATOM   3898 C C   . VAL   A 1 541 ? -14.070 63.407  67.794  1.00 122.93 ?  663 VAL   A C   1 
ATOM   3899 O O   . VAL   A 1 541 ? -14.006 64.476  67.169  1.00 120.78 ?  663 VAL   A O   1 
ATOM   3900 C CB  . VAL   A 1 541 ? -14.208 64.239  70.162  1.00 107.50 ?  663 VAL   A CB  1 
ATOM   3901 C CG1 . VAL   A 1 541 ? -15.688 63.864  70.280  1.00 106.52 ?  663 VAL   A CG1 1 
ATOM   3902 C CG2 . VAL   A 1 541 ? -13.545 64.201  71.490  1.00 113.02 ?  663 VAL   A CG2 1 
ATOM   3903 N N   . LEU   A 1 542 ? -14.630 62.298  67.298  1.00 128.94 ?  664 LEU   A N   1 
ATOM   3904 C CA  . LEU   A 1 542 ? -15.217 62.227  65.965  1.00 124.81 ?  664 LEU   A CA  1 
ATOM   3905 C C   . LEU   A 1 542 ? -16.723 62.070  66.133  1.00 128.27 ?  664 LEU   A C   1 
ATOM   3906 O O   . LEU   A 1 542 ? -17.203 61.052  66.659  1.00 124.58 ?  664 LEU   A O   1 
ATOM   3907 C CB  . LEU   A 1 542 ? -14.587 61.093  65.159  1.00 121.91 ?  664 LEU   A CB  1 
ATOM   3908 C CG  . LEU   A 1 542 ? -13.099 61.397  64.930  1.00 117.39 ?  664 LEU   A CG  1 
ATOM   3909 C CD1 . LEU   A 1 542 ? -12.350 60.198  64.396  1.00 121.14 ?  664 LEU   A CD1 1 
ATOM   3910 C CD2 . LEU   A 1 542 ? -12.882 62.622  64.032  1.00 112.81 ?  664 LEU   A CD2 1 
ATOM   3911 N N   . CYS   A 1 543 ? -17.453 63.112  65.725  1.00 129.66 ?  665 CYS   A N   1 
ATOM   3912 C CA  . CYS   A 1 543 ? -18.909 63.170  65.802  1.00 137.09 ?  665 CYS   A CA  1 
ATOM   3913 C C   . CYS   A 1 543 ? -19.503 63.004  64.411  1.00 144.83 ?  665 CYS   A C   1 
ATOM   3914 O O   . CYS   A 1 543 ? -19.322 63.865  63.540  1.00 145.33 ?  665 CYS   A O   1 
ATOM   3915 C CB  . CYS   A 1 543 ? -19.368 64.483  66.421  1.00 134.90 ?  665 CYS   A CB  1 
ATOM   3916 S SG  . CYS   A 1 543 ? -18.895 64.616  68.098  1.00 127.58 ?  665 CYS   A SG  1 
ATOM   3917 N N   . PHE   A 1 544 ? -20.229 61.913  64.209  1.00 143.35 ?  666 PHE   A N   1 
ATOM   3918 C CA  . PHE   A 1 544 ? -20.876 61.677  62.936  1.00 144.07 ?  666 PHE   A CA  1 
ATOM   3919 C C   . PHE   A 1 544 ? -22.386 61.713  63.126  1.00 145.85 ?  666 PHE   A C   1 
ATOM   3920 O O   . PHE   A 1 544 ? -22.887 62.031  64.212  1.00 142.57 ?  666 PHE   A O   1 
ATOM   3921 C CB  . PHE   A 1 544 ? -20.388 60.355  62.340  1.00 142.21 ?  666 PHE   A CB  1 
ATOM   3922 C CG  . PHE   A 1 544 ? -18.894 60.284  62.151  1.00 137.86 ?  666 PHE   A CG  1 
ATOM   3923 C CD1 . PHE   A 1 544 ? -18.249 61.167  61.278  1.00 134.73 ?  666 PHE   A CD1 1 
ATOM   3924 C CD2 . PHE   A 1 544 ? -18.140 59.323  62.821  1.00 129.08 ?  666 PHE   A CD2 1 
ATOM   3925 C CE1 . PHE   A 1 544 ? -16.887 61.107  61.085  1.00 127.58 ?  666 PHE   A CE1 1 
ATOM   3926 C CE2 . PHE   A 1 544 ? -16.778 59.256  62.636  1.00 129.18 ?  666 PHE   A CE2 1 
ATOM   3927 C CZ  . PHE   A 1 544 ? -16.148 60.153  61.762  1.00 130.00 ?  666 PHE   A CZ  1 
ATOM   3928 N N   . ASP   A 1 545 ? -23.112 61.395  62.051  1.00 148.76 ?  667 ASP   A N   1 
ATOM   3929 C CA  . ASP   A 1 545 ? -24.568 61.321  62.051  1.00 146.64 ?  667 ASP   A CA  1 
ATOM   3930 C C   . ASP   A 1 545 ? -25.117 59.898  61.946  1.00 142.98 ?  667 ASP   A C   1 
ATOM   3931 O O   . ASP   A 1 545 ? -26.334 59.708  62.087  1.00 140.97 ?  667 ASP   A O   1 
ATOM   3932 C CB  . ASP   A 1 545 ? -25.108 62.199  60.915  1.00 142.76 ?  667 ASP   A CB  1 
ATOM   3933 C CG  . ASP   A 1 545 ? -24.428 61.901  59.607  1.00 148.73 ?  667 ASP   A CG  1 
ATOM   3934 O OD1 . ASP   A 1 545 ? -23.191 62.100  59.540  1.00 147.79 ?  667 ASP   A OD1 1 
ATOM   3935 O OD2 . ASP   A 1 545 ? -25.110 61.468  58.658  1.00 152.62 ?  667 ASP   A OD2 1 
ATOM   3936 N N   . ARG   A 1 546 ? -24.257 58.893  61.755  1.00 141.45 ?  668 ARG   A N   1 
ATOM   3937 C CA  . ARG   A 1 546 ? -24.682 57.500  61.762  1.00 136.44 ?  668 ARG   A CA  1 
ATOM   3938 C C   . ARG   A 1 546 ? -23.519 56.583  62.109  1.00 130.46 ?  668 ARG   A C   1 
ATOM   3939 O O   . ARG   A 1 546 ? -22.393 56.783  61.642  1.00 129.92 ?  668 ARG   A O   1 
ATOM   3940 C CB  . ARG   A 1 546 ? -25.251 57.109  60.409  1.00 145.81 ?  668 ARG   A CB  1 
ATOM   3941 C CG  . ARG   A 1 546 ? -24.235 57.270  59.296  1.00 147.87 ?  668 ARG   A CG  1 
ATOM   3942 C CD  . ARG   A 1 546 ? -24.811 58.176  58.239  1.00 153.12 ?  668 ARG   A CD  1 
ATOM   3943 N NE  . ARG   A 1 546 ? -23.925 58.378  57.103  1.00 156.59 ?  668 ARG   A NE  1 
ATOM   3944 C CZ  . ARG   A 1 546 ? -24.239 59.131  56.059  1.00 152.98 ?  668 ARG   A CZ  1 
ATOM   3945 N NH1 . ARG   A 1 546 ? -25.392 59.782  56.002  1.00 144.66 ?  668 ARG   A NH1 1 
ATOM   3946 N NH2 . ARG   A 1 546 ? -23.390 59.206  55.037  1.00 151.98 ?  668 ARG   A NH2 1 
ATOM   3947 N N   . VAL   A 1 547 ? -23.815 55.566  62.915  1.00 127.51 ?  669 VAL   A N   1 
ATOM   3948 C CA  . VAL   A 1 547 ? -22.847 54.507  63.198  1.00 139.77 ?  669 VAL   A CA  1 
ATOM   3949 C C   . VAL   A 1 547 ? -22.537 53.735  61.917  1.00 140.62 ?  669 VAL   A C   1 
ATOM   3950 O O   . VAL   A 1 547 ? -23.408 53.063  61.348  1.00 143.59 ?  669 VAL   A O   1 
ATOM   3951 C CB  . VAL   A 1 547 ? -23.368 53.573  64.315  1.00 142.22 ?  669 VAL   A CB  1 
ATOM   3952 C CG1 . VAL   A 1 547 ? -22.528 52.278  64.407  1.00 137.59 ?  669 VAL   A CG1 1 
ATOM   3953 C CG2 . VAL   A 1 547 ? -23.354 54.281  65.688  1.00 137.57 ?  669 VAL   A CG2 1 
ATOM   3954 N N   . PHE   A 1 548 ? -21.283 53.815  61.463  1.00 134.28 ?  670 PHE   A N   1 
ATOM   3955 C CA  . PHE   A 1 548 ? -20.789 52.992  60.370  1.00 129.89 ?  670 PHE   A CA  1 
ATOM   3956 C C   . PHE   A 1 548 ? -19.737 51.992  60.826  1.00 125.88 ?  670 PHE   A C   1 
ATOM   3957 O O   . PHE   A 1 548 ? -19.032 51.420  59.993  1.00 128.47 ?  670 PHE   A O   1 
ATOM   3958 C CB  . PHE   A 1 548 ? -20.252 53.887  59.256  1.00 131.80 ?  670 PHE   A CB  1 
ATOM   3959 C CG  . PHE   A 1 548 ? -19.077 54.712  59.653  1.00 131.25 ?  670 PHE   A CG  1 
ATOM   3960 C CD1 . PHE   A 1 548 ? -17.834 54.139  59.860  1.00 131.43 ?  670 PHE   A CD1 1 
ATOM   3961 C CD2 . PHE   A 1 548 ? -19.221 56.070  59.830  1.00 133.11 ?  670 PHE   A CD2 1 
ATOM   3962 C CE1 . PHE   A 1 548 ? -16.757 54.906  60.221  1.00 134.61 ?  670 PHE   A CE1 1 
ATOM   3963 C CE2 . PHE   A 1 548 ? -18.144 56.846  60.192  1.00 135.29 ?  670 PHE   A CE2 1 
ATOM   3964 C CZ  . PHE   A 1 548 ? -16.910 56.265  60.388  1.00 134.14 ?  670 PHE   A CZ  1 
ATOM   3965 N N   . TRP   A 1 549 ? -19.600 51.792  62.123  1.00 127.70 ?  671 TRP   A N   1 
ATOM   3966 C CA  . TRP   A 1 549 ? -18.672 50.841  62.708  1.00 131.42 ?  671 TRP   A CA  1 
ATOM   3967 C C   . TRP   A 1 549 ? -19.468 49.679  63.263  1.00 125.24 ?  671 TRP   A C   1 
ATOM   3968 O O   . TRP   A 1 549 ? -20.698 49.721  63.320  1.00 120.33 ?  671 TRP   A O   1 
ATOM   3969 C CB  . TRP   A 1 549 ? -17.813 51.502  63.809  1.00 138.26 ?  671 TRP   A CB  1 
ATOM   3970 C CG  . TRP   A 1 549 ? -18.583 52.461  64.748  1.00 136.78 ?  671 TRP   A CG  1 
ATOM   3971 C CD1 . TRP   A 1 549 ? -19.208 52.142  65.932  1.00 133.49 ?  671 TRP   A CD1 1 
ATOM   3972 C CD2 . TRP   A 1 549 ? -18.821 53.870  64.541  1.00 134.04 ?  671 TRP   A CD2 1 
ATOM   3973 N NE1 . TRP   A 1 549 ? -19.807 53.261  66.465  1.00 133.61 ?  671 TRP   A NE1 1 
ATOM   3974 C CE2 . TRP   A 1 549 ? -19.587 54.330  65.633  1.00 132.71 ?  671 TRP   A CE2 1 
ATOM   3975 C CE3 . TRP   A 1 549 ? -18.473 54.781  63.527  1.00 132.32 ?  671 TRP   A CE3 1 
ATOM   3976 C CZ2 . TRP   A 1 549 ? -20.004 55.655  65.742  1.00 133.98 ?  671 TRP   A CZ2 1 
ATOM   3977 C CZ3 . TRP   A 1 549 ? -18.882 56.101  63.642  1.00 127.10 ?  671 TRP   A CZ3 1 
ATOM   3978 C CH2 . TRP   A 1 549 ? -19.640 56.523  64.736  1.00 133.18 ?  671 TRP   A CH2 1 
ATOM   3979 N N   . ASP   A 1 550 ? -18.756 48.645  63.667  1.00 124.63 ?  672 ASP   A N   1 
ATOM   3980 C CA  . ASP   A 1 550 ? -19.446 47.526  64.284  1.00 134.10 ?  672 ASP   A CA  1 
ATOM   3981 C C   . ASP   A 1 550 ? -20.030 47.952  65.624  1.00 137.48 ?  672 ASP   A C   1 
ATOM   3982 O O   . ASP   A 1 550 ? -19.270 48.138  66.585  1.00 139.71 ?  672 ASP   A O   1 
ATOM   3983 C CB  . ASP   A 1 550 ? -18.499 46.346  64.459  1.00 140.71 ?  672 ASP   A CB  1 
ATOM   3984 C CG  . ASP   A 1 550 ? -19.235 45.060  64.822  1.00 143.65 ?  672 ASP   A CG  1 
ATOM   3985 O OD1 . ASP   A 1 550 ? -20.386 45.150  65.314  1.00 139.02 ?  672 ASP   A OD1 1 
ATOM   3986 O OD2 . ASP   A 1 550 ? -18.667 43.962  64.605  1.00 143.36 ?  672 ASP   A OD2 1 
ATOM   3987 N N   . PRO   A 1 551 ? -21.354 48.084  65.749  1.00 133.92 ?  673 PRO   A N   1 
ATOM   3988 C CA  . PRO   A 1 551 ? -21.919 48.722  66.946  1.00 136.10 ?  673 PRO   A CA  1 
ATOM   3989 C C   . PRO   A 1 551 ? -21.803 47.880  68.195  1.00 136.77 ?  673 PRO   A C   1 
ATOM   3990 O O   . PRO   A 1 551 ? -21.824 48.435  69.301  1.00 140.93 ?  673 PRO   A O   1 
ATOM   3991 C CB  . PRO   A 1 551 ? -23.388 48.938  66.562  1.00 131.86 ?  673 PRO   A CB  1 
ATOM   3992 C CG  . PRO   A 1 551 ? -23.397 48.863  65.075  1.00 133.38 ?  673 PRO   A CG  1 
ATOM   3993 C CD  . PRO   A 1 551 ? -22.391 47.813  64.752  1.00 131.83 ?  673 PRO   A CD  1 
ATOM   3994 N N   . SER   A 1 552 ? -21.712 46.559  68.065  1.00 137.81 ?  674 SER   A N   1 
ATOM   3995 C CA  . SER   A 1 552 ? -21.487 45.716  69.233  1.00 146.26 ?  674 SER   A CA  1 
ATOM   3996 C C   . SER   A 1 552 ? -20.040 45.750  69.683  1.00 143.97 ?  674 SER   A C   1 
ATOM   3997 O O   . SER   A 1 552 ? -19.727 45.246  70.770  1.00 142.70 ?  674 SER   A O   1 
ATOM   3998 C CB  . SER   A 1 552 ? -21.877 44.263  68.945  1.00 149.37 ?  674 SER   A CB  1 
ATOM   3999 O OG  . SER   A 1 552 ? -21.114 43.746  67.865  1.00 146.52 ?  674 SER   A OG  1 
ATOM   4000 N N   . VAL   A 1 553 ? -19.166 46.311  68.858  1.00 139.80 ?  675 VAL   A N   1 
ATOM   4001 C CA  . VAL   A 1 553 ? -17.757 46.476  69.181  1.00 141.91 ?  675 VAL   A CA  1 
ATOM   4002 C C   . VAL   A 1 553 ? -17.558 47.841  69.842  1.00 144.58 ?  675 VAL   A C   1 
ATOM   4003 O O   . VAL   A 1 553 ? -17.883 48.885  69.257  1.00 142.64 ?  675 VAL   A O   1 
ATOM   4004 C CB  . VAL   A 1 553 ? -16.898 46.303  67.918  1.00 136.60 ?  675 VAL   A CB  1 
ATOM   4005 C CG1 . VAL   A 1 553 ? -15.582 47.010  68.037  1.00 131.97 ?  675 VAL   A CG1 1 
ATOM   4006 C CG2 . VAL   A 1 553 ? -16.644 44.828  67.710  1.00 136.19 ?  675 VAL   A CG2 1 
ATOM   4007 N N   . ASN   A 1 554 ? -17.052 47.832  71.086  1.00 135.01 ?  676 ASN   A N   1 
ATOM   4008 C CA  . ASN   A 1 554 ? -16.804 49.093  71.766  1.00 130.51 ?  676 ASN   A CA  1 
ATOM   4009 C C   . ASN   A 1 554 ? -15.553 49.784  71.249  1.00 130.53 ?  676 ASN   A C   1 
ATOM   4010 O O   . ASN   A 1 554 ? -15.473 51.019  71.293  1.00 128.82 ?  676 ASN   A O   1 
ATOM   4011 C CB  . ASN   A 1 554 ? -16.696 48.883  73.269  1.00 133.15 ?  676 ASN   A CB  1 
ATOM   4012 C CG  . ASN   A 1 554 ? -18.045 48.708  73.925  1.00 139.41 ?  676 ASN   A CG  1 
ATOM   4013 O OD1 . ASN   A 1 554 ? -18.231 47.817  74.744  1.00 137.12 ?  676 ASN   A OD1 1 
ATOM   4014 N ND2 . ASN   A 1 554 ? -19.007 49.558  73.554  1.00 141.23 ?  676 ASN   A ND2 1 
ATOM   4015 N N   . LEU   A 1 555 ? -14.589 49.022  70.730  1.00 128.30 ?  677 LEU   A N   1 
ATOM   4016 C CA  . LEU   A 1 555 ? -13.279 49.572  70.393  1.00 122.23 ?  677 LEU   A CA  1 
ATOM   4017 C C   . LEU   A 1 555 ? -12.569 48.702  69.357  1.00 117.92 ?  677 LEU   A C   1 
ATOM   4018 O O   . LEU   A 1 555 ? -12.766 47.491  69.305  1.00 123.66 ?  677 LEU   A O   1 
ATOM   4019 C CB  . LEU   A 1 555 ? -12.416 49.716  71.650  1.00 118.57 ?  677 LEU   A CB  1 
ATOM   4020 C CG  . LEU   A 1 555 ? -12.032 48.444  72.406  1.00 119.73 ?  677 LEU   A CG  1 
ATOM   4021 C CD1 . LEU   A 1 555 ? -11.004 48.826  73.433  1.00 114.46 ?  677 LEU   A CD1 1 
ATOM   4022 C CD2 . LEU   A 1 555 ? -13.226 47.757  73.080  1.00 124.34 ?  677 LEU   A CD2 1 
ATOM   4023 N N   . PHE   A 1 556 ? -11.720 49.330  68.550  1.00 112.33 ?  678 PHE   A N   1 
ATOM   4024 C CA  . PHE   A 1 556 ? -10.996 48.614  67.513  1.00 106.95 ?  678 PHE   A CA  1 
ATOM   4025 C C   . PHE   A 1 556 ? -9.689  49.325  67.203  1.00 107.74 ?  678 PHE   A C   1 
ATOM   4026 O O   . PHE   A 1 556 ? -9.652  50.552  67.151  1.00 113.38 ?  678 PHE   A O   1 
ATOM   4027 C CB  . PHE   A 1 556 ? -11.853 48.491  66.265  1.00 106.39 ?  678 PHE   A CB  1 
ATOM   4028 C CG  . PHE   A 1 556 ? -12.214 49.800  65.620  1.00 103.28 ?  678 PHE   A CG  1 
ATOM   4029 C CD1 . PHE   A 1 556 ? -11.324 50.460  64.777  1.00 101.54 ?  678 PHE   A CD1 1 
ATOM   4030 C CD2 . PHE   A 1 556 ? -13.485 50.330  65.786  1.00 110.61 ?  678 PHE   A CD2 1 
ATOM   4031 C CE1 . PHE   A 1 556 ? -11.674 51.661  64.152  1.00 105.85 ?  678 PHE   A CE1 1 
ATOM   4032 C CE2 . PHE   A 1 556 ? -13.845 51.528  65.160  1.00 116.69 ?  678 PHE   A CE2 1 
ATOM   4033 C CZ  . PHE   A 1 556 ? -12.932 52.197  64.343  1.00 110.32 ?  678 PHE   A CZ  1 
ATOM   4034 N N   . GLY   A 1 557 ? -8.618  48.556  66.995  1.00 105.59 ?  679 GLY   A N   1 
ATOM   4035 C CA  . GLY   A 1 557 ? -7.287  49.116  66.856  1.00 101.55 ?  679 GLY   A CA  1 
ATOM   4036 C C   . GLY   A 1 557 ? -6.944  49.498  65.424  1.00 101.68 ?  679 GLY   A C   1 
ATOM   4037 O O   . GLY   A 1 557 ? -7.718  49.283  64.499  1.00 106.18 ?  679 GLY   A O   1 
ATOM   4038 N N   . HIS   A 1 558 ? -5.770  50.118  65.264  1.00 98.74  ?  680 HIS   A N   1 
ATOM   4039 C CA  . HIS   A 1 558 ? -5.150  50.360  63.966  1.00 98.44  ?  680 HIS   A CA  1 
ATOM   4040 C C   . HIS   A 1 558 ? -3.657  50.196  64.157  1.00 102.08 ?  680 HIS   A C   1 
ATOM   4041 O O   . HIS   A 1 558 ? -3.095  50.771  65.091  1.00 101.40 ?  680 HIS   A O   1 
ATOM   4042 C CB  . HIS   A 1 558 ? -5.467  51.751  63.419  1.00 94.12  ?  680 HIS   A CB  1 
ATOM   4043 C CG  . HIS   A 1 558 ? -4.438  52.284  62.467  1.00 102.79 ?  680 HIS   A CG  1 
ATOM   4044 N ND1 . HIS   A 1 558 ? -3.349  53.025  62.878  1.00 107.09 ?  680 HIS   A ND1 1 
ATOM   4045 C CD2 . HIS   A 1 558 ? -4.352  52.219  61.120  1.00 106.78 ?  680 HIS   A CD2 1 
ATOM   4046 C CE1 . HIS   A 1 558 ? -2.631  53.386  61.830  1.00 102.37 ?  680 HIS   A CE1 1 
ATOM   4047 N NE2 . HIS   A 1 558 ? -3.217  52.906  60.751  1.00 110.28 ?  680 HIS   A NE2 1 
ATOM   4048 N N   . VAL   A 1 559 ? -3.025  49.392  63.317  1.00 105.44 ?  681 VAL   A N   1 
ATOM   4049 C CA  . VAL   A 1 559 ? -1.611  49.085  63.488  1.00 105.95 ?  681 VAL   A CA  1 
ATOM   4050 C C   . VAL   A 1 559 ? -0.797  50.098  62.704  1.00 106.20 ?  681 VAL   A C   1 
ATOM   4051 O O   . VAL   A 1 559 ? -1.277  50.718  61.753  1.00 105.29 ?  681 VAL   A O   1 
ATOM   4052 C CB  . VAL   A 1 559 ? -1.304  47.631  63.083  1.00 108.48 ?  681 VAL   A CB  1 
ATOM   4053 C CG1 . VAL   A 1 559 ? 0.112   47.247  63.484  1.00 110.24 ?  681 VAL   A CG1 1 
ATOM   4054 C CG2 . VAL   A 1 559 ? -2.302  46.694  63.761  1.00 105.33 ?  681 VAL   A CG2 1 
ATOM   4055 N N   . GLY   A 1 560 ? 0.431   50.314  63.138  1.00 110.83 ?  682 GLY   A N   1 
ATOM   4056 C CA  . GLY   A 1 560 ? 1.184   51.476  62.722  1.00 121.53 ?  682 GLY   A CA  1 
ATOM   4057 C C   . GLY   A 1 560 ? 2.210   51.140  61.664  1.00 125.33 ?  682 GLY   A C   1 
ATOM   4058 O O   . GLY   A 1 560 ? 2.764   50.044  61.649  1.00 130.09 ?  682 GLY   A O   1 
ATOM   4059 N N   . SER   A 1 561 ? 2.454   52.114  60.783  1.00 122.53 ?  683 SER   A N   1 
ATOM   4060 C CA  . SER   A 1 561 ? 3.464   51.953  59.743  1.00 127.38 ?  683 SER   A CA  1 
ATOM   4061 C C   . SER   A 1 561 ? 4.822   51.612  60.336  1.00 127.26 ?  683 SER   A C   1 
ATOM   4062 O O   . SER   A 1 561 ? 5.576   50.804  59.776  1.00 120.37 ?  683 SER   A O   1 
ATOM   4063 C CB  . SER   A 1 561 ? 3.576   53.236  58.917  1.00 133.47 ?  683 SER   A CB  1 
ATOM   4064 O OG  . SER   A 1 561 ? 2.359   53.546  58.270  1.00 140.38 ?  683 SER   A OG  1 
ATOM   4065 N N   . THR   A 1 562 ? 5.153   52.210  61.466  1.00 125.55 ?  684 THR   A N   1 
ATOM   4066 C CA  . THR   A 1 562 ? 6.537   52.203  61.880  1.00 126.98 ?  684 THR   A CA  1 
ATOM   4067 C C   . THR   A 1 562 ? 6.626   51.484  63.230  1.00 133.99 ?  684 THR   A C   1 
ATOM   4068 O O   . THR   A 1 562 ? 5.643   50.899  63.712  1.00 131.32 ?  684 THR   A O   1 
ATOM   4069 C CB  . THR   A 1 562 ? 7.032   53.641  61.955  1.00 123.32 ?  684 THR   A CB  1 
ATOM   4070 O OG1 . THR   A 1 562 ? 6.618   54.310  60.762  1.00 125.53 ?  684 THR   A OG1 1 
ATOM   4071 C CG2 . THR   A 1 562 ? 8.559   53.648  61.935  1.00 121.73 ?  684 THR   A CG2 1 
ATOM   4072 N N   . THR   A 1 563 ? 7.830   51.486  63.818  1.00 136.44 ?  685 THR   A N   1 
ATOM   4073 C CA  . THR   A 1 563 ? 7.934   51.462  65.272  1.00 122.34 ?  685 THR   A CA  1 
ATOM   4074 C C   . THR   A 1 563 ? 7.629   52.852  65.809  1.00 113.94 ?  685 THR   A C   1 
ATOM   4075 O O   . THR   A 1 563 ? 6.808   53.012  66.717  1.00 107.58 ?  685 THR   A O   1 
ATOM   4076 C CB  . THR   A 1 563 ? 9.328   50.962  65.714  1.00 122.66 ?  685 THR   A CB  1 
ATOM   4077 O OG1 . THR   A 1 563 ? 9.507   49.572  65.373  1.00 126.93 ?  685 THR   A OG1 1 
ATOM   4078 C CG2 . THR   A 1 563 ? 9.506   51.101  67.198  1.00 119.25 ?  685 THR   A CG2 1 
ATOM   4079 N N   . ALA   A 1 564 ? 8.188   53.868  65.155  1.00 118.89 ?  686 ALA   A N   1 
ATOM   4080 C CA  . ALA   A 1 564 ? 8.195   55.241  65.630  1.00 114.20 ?  686 ALA   A CA  1 
ATOM   4081 C C   . ALA   A 1 564 ? 6.850   55.926  65.560  1.00 109.32 ?  686 ALA   A C   1 
ATOM   4082 O O   . ALA   A 1 564 ? 6.762   57.084  65.967  1.00 110.97 ?  686 ALA   A O   1 
ATOM   4083 C CB  . ALA   A 1 564 ? 9.184   56.071  64.821  1.00 115.27 ?  686 ALA   A CB  1 
ATOM   4084 N N   . SER   A 1 565 ? 5.820   55.294  65.025  1.00 111.83 ?  687 SER   A N   1 
ATOM   4085 C CA  . SER   A 1 565 ? 4.500   55.906  65.109  1.00 113.55 ?  687 SER   A CA  1 
ATOM   4086 C C   . SER   A 1 565 ? 3.472   54.886  65.576  1.00 108.80 ?  687 SER   A C   1 
ATOM   4087 O O   . SER   A 1 565 ? 2.290   54.959  65.210  1.00 101.92 ?  687 SER   A O   1 
ATOM   4088 C CB  . SER   A 1 565 ? 4.093   56.552  63.784  1.00 116.02 ?  687 SER   A CB  1 
ATOM   4089 O OG  . SER   A 1 565 ? 3.824   55.573  62.794  1.00 131.09 ?  687 SER   A OG  1 
ATOM   4090 N N   . ARG   A 1 566 ? 3.914   53.939  66.413  1.00 104.64 ?  688 ARG   A N   1 
ATOM   4091 C CA  . ARG   A 1 566 ? 2.983   52.994  67.010  1.00 101.61 ?  688 ARG   A CA  1 
ATOM   4092 C C   . ARG   A 1 566 ? 1.863   53.702  67.759  1.00 102.78 ?  688 ARG   A C   1 
ATOM   4093 O O   . ARG   A 1 566 ? 0.785   53.124  67.928  1.00 105.79 ?  688 ARG   A O   1 
ATOM   4094 C CB  . ARG   A 1 566 ? 3.733   51.972  67.903  1.00 97.17  ?  688 ARG   A CB  1 
ATOM   4095 C CG  . ARG   A 1 566 ? 4.517   52.438  69.146  1.00 96.12  ?  688 ARG   A CG  1 
ATOM   4096 C CD  . ARG   A 1 566 ? 5.286   51.241  69.766  1.00 94.26  ?  688 ARG   A CD  1 
ATOM   4097 N NE  . ARG   A 1 566 ? 6.101   51.498  70.953  1.00 91.01  ?  688 ARG   A NE  1 
ATOM   4098 C CZ  . ARG   A 1 566 ? 7.128   50.738  71.335  1.00 100.52 ?  688 ARG   A CZ  1 
ATOM   4099 N NH1 . ARG   A 1 566 ? 7.516   49.686  70.633  1.00 110.34 ?  688 ARG   A NH1 1 
ATOM   4100 N NH2 . ARG   A 1 566 ? 7.782   51.031  72.455  1.00 102.36 ?  688 ARG   A NH2 1 
ATOM   4101 N N   . GLY   A 1 567 ? 2.055   54.961  68.138  1.00 103.42 ?  689 GLY   A N   1 
ATOM   4102 C CA  . GLY   A 1 567 ? 1.041   55.650  68.910  1.00 102.80 ?  689 GLY   A CA  1 
ATOM   4103 C C   . GLY   A 1 567 ? -0.004  56.384  68.098  1.00 102.13 ?  689 GLY   A C   1 
ATOM   4104 O O   . GLY   A 1 567 ? -1.152  56.524  68.527  1.00 98.08  ?  689 GLY   A O   1 
ATOM   4105 N N   . GLU   A 1 568 ? 0.384   56.849  66.916  1.00 107.25 ?  690 GLU   A N   1 
ATOM   4106 C CA  . GLU   A 1 568 ? -0.414  57.812  66.172  1.00 104.95 ?  690 GLU   A CA  1 
ATOM   4107 C C   . GLU   A 1 568 ? -1.745  57.200  65.764  1.00 98.75  ?  690 GLU   A C   1 
ATOM   4108 O O   . GLU   A 1 568 ? -1.781  56.256  64.976  1.00 106.08 ?  690 GLU   A O   1 
ATOM   4109 C CB  . GLU   A 1 568 ? 0.382   58.289  64.964  1.00 107.25 ?  690 GLU   A CB  1 
ATOM   4110 C CG  . GLU   A 1 568 ? -0.272  59.326  64.117  1.00 107.32 ?  690 GLU   A CG  1 
ATOM   4111 C CD  . GLU   A 1 568 ? 0.757   59.979  63.218  1.00 120.66 ?  690 GLU   A CD  1 
ATOM   4112 O OE1 . GLU   A 1 568 ? 1.916   60.194  63.693  1.00 119.26 ?  690 GLU   A OE1 1 
ATOM   4113 O OE2 . GLU   A 1 568 ? 0.415   60.227  62.030  1.00 117.20 ?  690 GLU   A OE2 1 
ATOM   4114 N N   . LEU   A 1 569 ? -2.829  57.701  66.341  1.00 93.64  ?  691 LEU   A N   1 
ATOM   4115 C CA  . LEU   A 1 569 ? -4.191  57.248  66.063  1.00 95.01  ?  691 LEU   A CA  1 
ATOM   4116 C C   . LEU   A 1 569 ? -4.336  55.730  66.124  1.00 94.89  ?  691 LEU   A C   1 
ATOM   4117 O O   . LEU   A 1 569 ? -4.924  55.099  65.248  1.00 96.75  ?  691 LEU   A O   1 
ATOM   4118 C CB  . LEU   A 1 569 ? -4.656  57.798  64.730  1.00 93.35  ?  691 LEU   A CB  1 
ATOM   4119 C CG  . LEU   A 1 569 ? -4.705  59.259  65.116  1.00 92.20  ?  691 LEU   A CG  1 
ATOM   4120 C CD1 . LEU   A 1 569 ? -4.410  60.179  63.963  1.00 101.00 ?  691 LEU   A CD1 1 
ATOM   4121 C CD2 . LEU   A 1 569 ? -6.055  59.522  65.771  1.00 94.32  ?  691 LEU   A CD2 1 
ATOM   4122 N N   . PHE   A 1 570 ? -3.855  55.152  67.215  1.00 94.36  ?  692 PHE   A N   1 
ATOM   4123 C CA  . PHE   A 1 570 ? -3.691  53.716  67.321  1.00 95.20  ?  692 PHE   A CA  1 
ATOM   4124 C C   . PHE   A 1 570 ? -4.927  52.984  67.878  1.00 99.28  ?  692 PHE   A C   1 
ATOM   4125 O O   . PHE   A 1 570 ? -4.851  51.775  68.089  1.00 104.82 ?  692 PHE   A O   1 
ATOM   4126 C CB  . PHE   A 1 570 ? -2.452  53.414  68.184  1.00 94.24  ?  692 PHE   A CB  1 
ATOM   4127 C CG  . PHE   A 1 570 ? -2.720  53.438  69.667  1.00 101.25 ?  692 PHE   A CG  1 
ATOM   4128 C CD1 . PHE   A 1 570 ? -2.995  54.617  70.329  1.00 111.35 ?  692 PHE   A CD1 1 
ATOM   4129 C CD2 . PHE   A 1 570 ? -2.694  52.258  70.406  1.00 95.39  ?  692 PHE   A CD2 1 
ATOM   4130 C CE1 . PHE   A 1 570 ? -3.256  54.607  71.697  1.00 115.01 ?  692 PHE   A CE1 1 
ATOM   4131 C CE2 . PHE   A 1 570 ? -2.952  52.234  71.781  1.00 96.46  ?  692 PHE   A CE2 1 
ATOM   4132 C CZ  . PHE   A 1 570 ? -3.236  53.397  72.420  1.00 116.07 ?  692 PHE   A CZ  1 
ATOM   4133 N N   . LEU   A 1 571 ? -6.067  53.651  68.093  1.00 98.48  ?  693 LEU   A N   1 
ATOM   4134 C CA  . LEU   A 1 571 ? -7.195  52.990  68.763  1.00 97.29  ?  693 LEU   A CA  1 
ATOM   4135 C C   . LEU   A 1 571 ? -8.463  53.850  68.802  1.00 104.62 ?  693 LEU   A C   1 
ATOM   4136 O O   . LEU   A 1 571 ? -8.389  55.058  69.058  1.00 108.67 ?  693 LEU   A O   1 
ATOM   4137 C CB  . LEU   A 1 571 ? -6.777  52.596  70.183  1.00 90.34  ?  693 LEU   A CB  1 
ATOM   4138 C CG  . LEU   A 1 571 ? -7.776  52.086  71.224  1.00 98.32  ?  693 LEU   A CG  1 
ATOM   4139 C CD1 . LEU   A 1 571 ? -8.827  51.133  70.682  1.00 102.87 ?  693 LEU   A CD1 1 
ATOM   4140 C CD2 . LEU   A 1 571 ? -7.017  51.441  72.364  1.00 96.58  ?  693 LEU   A CD2 1 
ATOM   4141 N N   . PHE   A 1 572 ? -9.639  53.246  68.578  1.00 101.09 ?  694 PHE   A N   1 
ATOM   4142 C CA  . PHE   A 1 572 ? -10.899 53.980  68.447  1.00 107.45 ?  694 PHE   A CA  1 
ATOM   4143 C C   . PHE   A 1 572 ? -11.935 53.432  69.434  1.00 113.69 ?  694 PHE   A C   1 
ATOM   4144 O O   . PHE   A 1 572 ? -11.989 52.218  69.644  1.00 110.94 ?  694 PHE   A O   1 
ATOM   4145 C CB  . PHE   A 1 572 ? -11.420 53.887  66.982  1.00 106.87 ?  694 PHE   A CB  1 
ATOM   4146 C CG  . PHE   A 1 572 ? -10.564 54.638  65.966  1.00 105.15 ?  694 PHE   A CG  1 
ATOM   4147 C CD1 . PHE   A 1 572 ? -9.226  54.312  65.775  1.00 100.97 ?  694 PHE   A CD1 1 
ATOM   4148 C CD2 . PHE   A 1 572 ? -11.114 55.643  65.175  1.00 110.41 ?  694 PHE   A CD2 1 
ATOM   4149 C CE1 . PHE   A 1 572 ? -8.440  55.006  64.857  1.00 106.91 ?  694 PHE   A CE1 1 
ATOM   4150 C CE2 . PHE   A 1 572 ? -10.328 56.348  64.245  1.00 111.54 ?  694 PHE   A CE2 1 
ATOM   4151 C CZ  . PHE   A 1 572 ? -8.994  56.029  64.085  1.00 110.27 ?  694 PHE   A CZ  1 
ATOM   4152 N N   . TRP   A 1 573 ? -12.742 54.312  70.070  1.00 118.06 ?  695 TRP   A N   1 
ATOM   4153 C CA  . TRP   A 1 573 ? -13.852 53.869  70.930  1.00 118.61 ?  695 TRP   A CA  1 
ATOM   4154 C C   . TRP   A 1 573 ? -15.187 54.364  70.382  1.00 122.23 ?  695 TRP   A C   1 
ATOM   4155 O O   . TRP   A 1 573 ? -15.368 55.564  70.142  1.00 116.95 ?  695 TRP   A O   1 
ATOM   4156 C CB  . TRP   A 1 573 ? -13.754 54.318  72.406  1.00 116.92 ?  695 TRP   A CB  1 
ATOM   4157 C CG  . TRP   A 1 573 ? -12.446 54.166  73.219  1.00 116.78 ?  695 TRP   A CG  1 
ATOM   4158 C CD1 . TRP   A 1 573 ? -11.259 54.801  72.989  1.00 118.08 ?  695 TRP   A CD1 1 
ATOM   4159 C CD2 . TRP   A 1 573 ? -12.242 53.382  74.419  1.00 112.53 ?  695 TRP   A CD2 1 
ATOM   4160 N NE1 . TRP   A 1 573 ? -10.329 54.448  73.945  1.00 116.44 ?  695 TRP   A NE1 1 
ATOM   4161 C CE2 . TRP   A 1 573 ? -10.904 53.576  74.828  1.00 113.73 ?  695 TRP   A CE2 1 
ATOM   4162 C CE3 . TRP   A 1 573 ? -13.047 52.522  75.162  1.00 114.28 ?  695 TRP   A CE3 1 
ATOM   4163 C CZ2 . TRP   A 1 573 ? -10.358 52.947  75.947  1.00 113.74 ?  695 TRP   A CZ2 1 
ATOM   4164 C CZ3 . TRP   A 1 573 ? -12.504 51.900  76.278  1.00 116.99 ?  695 TRP   A CZ3 1 
ATOM   4165 C CH2 . TRP   A 1 573 ? -11.170 52.110  76.656  1.00 116.08 ?  695 TRP   A CH2 1 
ATOM   4166 N N   . ASN   A 1 574 ? -16.108 53.427  70.178  1.00 126.48 ?  696 ASN   A N   1 
ATOM   4167 C CA  . ASN   A 1 574 ? -17.544 53.678  70.197  1.00 134.23 ?  696 ASN   A CA  1 
ATOM   4168 C C   . ASN   A 1 574 ? -17.968 53.285  71.592  1.00 140.80 ?  696 ASN   A C   1 
ATOM   4169 O O   . ASN   A 1 574 ? -18.181 52.100  71.869  1.00 143.10 ?  696 ASN   A O   1 
ATOM   4170 C CB  . ASN   A 1 574 ? -18.317 52.826  69.199  1.00 140.54 ?  696 ASN   A CB  1 
ATOM   4171 C CG  . ASN   A 1 574 ? -19.832 52.791  69.506  1.00 146.69 ?  696 ASN   A CG  1 
ATOM   4172 O OD1 . ASN   A 1 574 ? -20.394 53.750  70.065  1.00 152.32 ?  696 ASN   A OD1 1 
ATOM   4173 N ND2 . ASN   A 1 574 ? -20.471 51.654  69.217  1.00 134.38 ?  696 ASN   A ND2 1 
ATOM   4174 N N   . LEU   A 1 575 ? -18.086 54.267  72.474  1.00 141.59 ?  697 LEU   A N   1 
ATOM   4175 C CA  . LEU   A 1 575 ? -18.547 53.983  73.822  1.00 141.80 ?  697 LEU   A CA  1 
ATOM   4176 C C   . LEU   A 1 575 ? -19.935 54.518  74.070  1.00 141.59 ?  697 LEU   A C   1 
ATOM   4177 O O   . LEU   A 1 575 ? -20.600 54.070  75.010  1.00 139.75 ?  697 LEU   A O   1 
ATOM   4178 C CB  . LEU   A 1 575 ? -17.591 54.598  74.846  1.00 135.87 ?  697 LEU   A CB  1 
ATOM   4179 C CG  . LEU   A 1 575 ? -16.308 53.814  75.103  1.00 131.54 ?  697 LEU   A CG  1 
ATOM   4180 C CD1 . LEU   A 1 575 ? -15.404 54.693  75.957  1.00 127.30 ?  697 LEU   A CD1 1 
ATOM   4181 C CD2 . LEU   A 1 575 ? -16.582 52.444  75.742  1.00 128.48 ?  697 LEU   A CD2 1 
ATOM   4182 N N   . TYR   A 1 576 ? -20.385 55.433  73.227  1.00 143.86 ?  698 TYR   A N   1 
ATOM   4183 C CA  . TYR   A 1 576 ? -21.520 56.277  73.524  1.00 149.89 ?  698 TYR   A CA  1 
ATOM   4184 C C   . TYR   A 1 576 ? -22.713 55.851  72.685  1.00 154.96 ?  698 TYR   A C   1 
ATOM   4185 O O   . TYR   A 1 576 ? -22.565 55.203  71.640  1.00 153.80 ?  698 TYR   A O   1 
ATOM   4186 C CB  . TYR   A 1 576 ? -21.157 57.747  73.273  1.00 148.67 ?  698 TYR   A CB  1 
ATOM   4187 C CG  . TYR   A 1 576 ? -20.030 58.210  74.183  1.00 145.46 ?  698 TYR   A CG  1 
ATOM   4188 C CD1 . TYR   A 1 576 ? -20.243 58.392  75.558  1.00 136.36 ?  698 TYR   A CD1 1 
ATOM   4189 C CD2 . TYR   A 1 576 ? -18.739 58.419  73.680  1.00 139.11 ?  698 TYR   A CD2 1 
ATOM   4190 C CE1 . TYR   A 1 576 ? -19.207 58.797  76.409  1.00 129.61 ?  698 TYR   A CE1 1 
ATOM   4191 C CE2 . TYR   A 1 576 ? -17.690 58.823  74.523  1.00 133.10 ?  698 TYR   A CE2 1 
ATOM   4192 C CZ  . TYR   A 1 576 ? -17.929 59.011  75.890  1.00 130.35 ?  698 TYR   A CZ  1 
ATOM   4193 O OH  . TYR   A 1 576 ? -16.899 59.401  76.736  1.00 119.61 ?  698 TYR   A OH  1 
ATOM   4194 N N   . LYS   A 1 577 ? -23.900 56.193  73.194  1.00 155.76 ?  699 LYS   A N   1 
ATOM   4195 C CA  . LYS   A 1 577 ? -25.139 55.979  72.454  1.00 159.76 ?  699 LYS   A CA  1 
ATOM   4196 C C   . LYS   A 1 577 ? -25.071 56.659  71.092  1.00 157.57 ?  699 LYS   A C   1 
ATOM   4197 O O   . LYS   A 1 577 ? -25.391 56.062  70.054  1.00 157.65 ?  699 LYS   A O   1 
ATOM   4198 C CB  . LYS   A 1 577 ? -26.319 56.531  73.260  1.00 158.74 ?  699 LYS   A CB  1 
ATOM   4199 C CG  . LYS   A 1 577 ? -26.269 56.249  74.760  1.00 155.36 ?  699 LYS   A CG  1 
ATOM   4200 C CD  . LYS   A 1 577 ? -27.009 57.341  75.525  1.00 156.80 ?  699 LYS   A CD  1 
ATOM   4201 C CE  . LYS   A 1 577 ? -26.830 57.234  77.035  1.00 151.34 ?  699 LYS   A CE  1 
ATOM   4202 N NZ  . LYS   A 1 577 ? -27.054 58.554  77.733  1.00 145.41 ?  699 LYS   A NZ  1 
ATOM   4203 N N   . ALA   A 1 578 ? -24.635 57.915  71.085  1.00 150.36 ?  700 ALA   A N   1 
ATOM   4204 C CA  . ALA   A 1 578 ? -24.572 58.707  69.885  1.00 144.01 ?  700 ALA   A CA  1 
ATOM   4205 C C   . ALA   A 1 578 ? -23.497 58.180  68.933  1.00 137.65 ?  700 ALA   A C   1 
ATOM   4206 O O   . ALA   A 1 578 ? -22.669 57.334  69.292  1.00 138.45 ?  700 ALA   A O   1 
ATOM   4207 C CB  . ALA   A 1 578 ? -24.315 60.172  70.251  1.00 139.47 ?  700 ALA   A CB  1 
ATOM   4208 N N   . PRO   A 1 579 ? -23.492 58.708  67.698  1.00 133.17 ?  701 PRO   A N   1 
ATOM   4209 C CA  . PRO   A 1 579 ? -22.460 58.386  66.749  1.00 135.54 ?  701 PRO   A CA  1 
ATOM   4210 C C   . PRO   A 1 579 ? -21.137 59.082  67.044  1.00 135.46 ?  701 PRO   A C   1 
ATOM   4211 O O   . PRO   A 1 579 ? -20.766 59.963  66.302  1.00 129.49 ?  701 PRO   A O   1 
ATOM   4212 C CB  . PRO   A 1 579 ? -22.905 59.193  65.539  1.00 136.63 ?  701 PRO   A CB  1 
ATOM   4213 C CG  . PRO   A 1 579 ? -23.712 60.311  66.107  1.00 135.04 ?  701 PRO   A CG  1 
ATOM   4214 C CD  . PRO   A 1 579 ? -24.524 59.581  67.138  1.00 136.39 ?  701 PRO   A CD  1 
ATOM   4215 N N   . ILE   A 1 580 ? -20.461 58.666  68.103  1.00 136.13 ?  702 ILE   A N   1 
ATOM   4216 C CA  . ILE   A 1 580 ? -19.200 59.355  68.467  1.00 130.12 ?  702 ILE   A CA  1 
ATOM   4217 C C   . ILE   A 1 580 ? -18.106 58.309  68.552  1.00 130.28 ?  702 ILE   A C   1 
ATOM   4218 O O   . ILE   A 1 580 ? -18.213 57.397  69.378  1.00 123.91 ?  702 ILE   A O   1 
ATOM   4219 C CB  . ILE   A 1 580 ? -19.337 60.112  69.791  1.00 132.90 ?  702 ILE   A CB  1 
ATOM   4220 C CG1 . ILE   A 1 580 ? -19.851 61.535  69.572  1.00 130.42 ?  702 ILE   A CG1 1 
ATOM   4221 C CG2 . ILE   A 1 580 ? -18.023 60.104  70.548  1.00 130.08 ?  702 ILE   A CG2 1 
ATOM   4222 C CD1 . ILE   A 1 580 ? -20.714 62.040  70.699  1.00 130.41 ?  702 ILE   A CD1 1 
ATOM   4223 N N   . LEU   A 1 581 ? -17.126 58.434  67.676  1.00 130.44 ?  703 LEU   A N   1 
ATOM   4224 C CA  . LEU   A 1 581 ? -15.969 57.525  67.740  1.00 128.39 ?  703 LEU   A CA  1 
ATOM   4225 C C   . LEU   A 1 581 ? -14.903 58.361  68.408  1.00 126.78 ?  703 LEU   A C   1 
ATOM   4226 O O   . LEU   A 1 581 ? -14.902 59.574  68.175  1.00 121.64 ?  703 LEU   A O   1 
ATOM   4227 C CB  . LEU   A 1 581 ? -15.554 57.112  66.334  1.00 129.92 ?  703 LEU   A CB  1 
ATOM   4228 C CG  . LEU   A 1 581 ? -15.957 55.700  65.926  1.00 130.99 ?  703 LEU   A CG  1 
ATOM   4229 C CD1 . LEU   A 1 581 ? -15.003 55.154  64.880  1.00 129.60 ?  703 LEU   A CD1 1 
ATOM   4230 C CD2 . LEU   A 1 581 ? -15.993 54.789  67.139  1.00 124.37 ?  703 LEU   A CD2 1 
ATOM   4231 N N   . LEU   A 1 582 ? -14.015 57.729  69.145  1.00 119.88 ?  704 LEU   A N   1 
ATOM   4232 C CA  . LEU   A 1 582 ? -13.086 58.479  69.964  1.00 113.11 ?  704 LEU   A CA  1 
ATOM   4233 C C   . LEU   A 1 582 ? -11.722 57.854  69.740  1.00 104.54 ?  704 LEU   A C   1 
ATOM   4234 O O   . LEU   A 1 582 ? -11.592 56.633  69.814  1.00 101.38 ?  704 LEU   A O   1 
ATOM   4235 C CB  . LEU   A 1 582 ? -13.556 58.412  71.416  1.00 116.70 ?  704 LEU   A CB  1 
ATOM   4236 C CG  . LEU   A 1 582 ? -13.183 59.351  72.552  1.00 113.36 ?  704 LEU   A CG  1 
ATOM   4237 C CD1 . LEU   A 1 582 ? -14.201 59.133  73.673  1.00 116.86 ?  704 LEU   A CD1 1 
ATOM   4238 C CD2 . LEU   A 1 582 ? -11.794 59.038  73.053  1.00 107.74 ?  704 LEU   A CD2 1 
ATOM   4239 N N   . ALA   A 1 583 ? -10.724 58.679  69.427  1.00 102.46 ?  705 ALA   A N   1 
ATOM   4240 C CA  . ALA   A 1 583 ? -9.465  58.236  68.826  1.00 99.56  ?  705 ALA   A CA  1 
ATOM   4241 C C   . ALA   A 1 583 ? -8.278  58.586  69.718  1.00 101.82 ?  705 ALA   A C   1 
ATOM   4242 O O   . ALA   A 1 583 ? -7.895  59.758  69.798  1.00 105.84 ?  705 ALA   A O   1 
ATOM   4243 C CB  . ALA   A 1 583 ? -9.285  58.885  67.453  1.00 103.50 ?  705 ALA   A CB  1 
ATOM   4244 N N   . LEU   A 1 584 ? -7.650  57.573  70.322  1.00 93.95  ?  706 LEU   A N   1 
ATOM   4245 C CA  . LEU   A 1 584 ? -6.506  57.762  71.217  1.00 92.60  ?  706 LEU   A CA  1 
ATOM   4246 C C   . LEU   A 1 584 ? -5.230  58.118  70.436  1.00 95.98  ?  706 LEU   A C   1 
ATOM   4247 O O   . LEU   A 1 584 ? -5.100  57.814  69.254  1.00 100.47 ?  706 LEU   A O   1 
ATOM   4248 C CB  . LEU   A 1 584 ? -6.287  56.490  72.032  1.00 97.21  ?  706 LEU   A CB  1 
ATOM   4249 C CG  . LEU   A 1 584 ? -6.850  56.397  73.459  1.00 106.60 ?  706 LEU   A CG  1 
ATOM   4250 C CD1 . LEU   A 1 584 ? -8.292  56.867  73.504  1.00 108.46 ?  706 LEU   A CD1 1 
ATOM   4251 C CD2 . LEU   A 1 584 ? -6.801  54.953  73.962  1.00 106.52 ?  706 LEU   A CD2 1 
ATOM   4252 N N   . VAL   A 1 585 ? -4.283  58.790  71.107  1.00 94.79  ?  707 VAL   A N   1 
ATOM   4253 C CA  . VAL   A 1 585 ? -2.984  59.164  70.528  1.00 91.52  ?  707 VAL   A CA  1 
ATOM   4254 C C   . VAL   A 1 585 ? -1.923  59.070  71.605  1.00 93.76  ?  707 VAL   A C   1 
ATOM   4255 O O   . VAL   A 1 585 ? -1.640  60.070  72.259  1.00 97.62  ?  707 VAL   A O   1 
ATOM   4256 C CB  . VAL   A 1 585 ? -2.962  60.605  69.982  1.00 87.52  ?  707 VAL   A CB  1 
ATOM   4257 C CG1 . VAL   A 1 585 ? -1.571  60.955  69.401  1.00 85.62  ?  707 VAL   A CG1 1 
ATOM   4258 C CG2 . VAL   A 1 585 ? -4.068  60.837  68.998  1.00 91.82  ?  707 VAL   A CG2 1 
ATOM   4259 N N   . ALA   A 1 586 ? -1.321  57.911  71.819  1.00 98.12  ?  708 ALA   A N   1 
ATOM   4260 C CA  . ALA   A 1 586 ? -0.427  57.793  72.969  1.00 97.37  ?  708 ALA   A CA  1 
ATOM   4261 C C   . ALA   A 1 586 ? 1.029   57.776  72.529  1.00 92.20  ?  708 ALA   A C   1 
ATOM   4262 O O   . ALA   A 1 586 ? 1.370   58.124  71.394  1.00 93.43  ?  708 ALA   A O   1 
ATOM   4263 C CB  . ALA   A 1 586 ? -0.759  56.548  73.794  1.00 99.01  ?  708 ALA   A CB  1 
ATOM   4264 N N   . GLY   A 1 587 ? 1.890   57.388  73.449  1.00 87.53  ?  709 GLY   A N   1 
ATOM   4265 C CA  . GLY   A 1 587 ? 3.260   57.109  73.096  1.00 91.65  ?  709 GLY   A CA  1 
ATOM   4266 C C   . GLY   A 1 587 ? 4.066   58.355  72.786  1.00 93.83  ?  709 GLY   A C   1 
ATOM   4267 O O   . GLY   A 1 587 ? 3.728   59.472  73.177  1.00 98.09  ?  709 GLY   A O   1 
ATOM   4268 N N   . GLU   A 1 588 ? 5.169   58.134  72.069  1.00 94.60  ?  710 GLU   A N   1 
ATOM   4269 C CA  . GLU   A 1 588 ? 5.950   59.247  71.542  1.00 94.35  ?  710 GLU   A CA  1 
ATOM   4270 C C   . GLU   A 1 588 ? 5.108   60.153  70.656  1.00 91.18  ?  710 GLU   A C   1 
ATOM   4271 O O   . GLU   A 1 588 ? 5.392   61.347  70.546  1.00 91.82  ?  710 GLU   A O   1 
ATOM   4272 C CB  . GLU   A 1 588 ? 7.144   58.703  70.762  1.00 93.74  ?  710 GLU   A CB  1 
ATOM   4273 C CG  . GLU   A 1 588 ? 8.199   58.050  71.627  1.00 91.64  ?  710 GLU   A CG  1 
ATOM   4274 C CD  . GLU   A 1 588 ? 9.046   59.070  72.333  1.00 95.62  ?  710 GLU   A CD  1 
ATOM   4275 O OE1 . GLU   A 1 588 ? 8.689   60.259  72.248  1.00 102.18 ?  710 GLU   A OE1 1 
ATOM   4276 O OE2 . GLU   A 1 588 ? 10.061  58.704  72.970  1.00 96.75  ?  710 GLU   A OE2 1 
ATOM   4277 N N   . ALA   A 1 589 ? 4.050   59.602  70.057  1.00 92.10  ?  711 ALA   A N   1 
ATOM   4278 C CA  . ALA   A 1 589 ? 3.242   60.310  69.070  1.00 94.90  ?  711 ALA   A CA  1 
ATOM   4279 C C   . ALA   A 1 589 ? 2.446   61.449  69.689  1.00 100.57 ?  711 ALA   A C   1 
ATOM   4280 O O   . ALA   A 1 589 ? 2.303   62.519  69.078  1.00 102.46 ?  711 ALA   A O   1 
ATOM   4281 C CB  . ALA   A 1 589 ? 2.289   59.328  68.391  1.00 98.98  ?  711 ALA   A CB  1 
ATOM   4282 N N   . ALA   A 1 590 ? 1.888   61.215  70.881  1.00 102.11 ?  712 ALA   A N   1 
ATOM   4283 C CA  . ALA   A 1 590 ? 1.067   62.213  71.568  1.00 102.92 ?  712 ALA   A CA  1 
ATOM   4284 C C   . ALA   A 1 590 ? 1.741   63.569  71.600  1.00 99.50  ?  712 ALA   A C   1 
ATOM   4285 O O   . ALA   A 1 590 ? 1.127   64.595  71.279  1.00 96.17  ?  712 ALA   A O   1 
ATOM   4286 C CB  . ALA   A 1 590 ? 0.795   61.760  73.000  1.00 100.79 ?  712 ALA   A CB  1 
ATOM   4287 N N   . GLY   A 1 591 ? 3.013   63.577  72.008  1.00 99.18  ?  713 GLY   A N   1 
ATOM   4288 C CA  . GLY   A 1 591 ? 3.762   64.802  72.176  1.00 102.05 ?  713 GLY   A CA  1 
ATOM   4289 C C   . GLY   A 1 591 ? 3.976   65.589  70.904  1.00 99.38  ?  713 GLY   A C   1 
ATOM   4290 O O   . GLY   A 1 591 ? 4.241   66.790  70.988  1.00 94.30  ?  713 GLY   A O   1 
ATOM   4291 N N   . ILE   A 1 592 ? 3.858   64.947  69.729  1.00 103.38 ?  714 ILE   A N   1 
ATOM   4292 C CA  . ILE   A 1 592 ? 4.152   65.615  68.464  1.00 99.56  ?  714 ILE   A CA  1 
ATOM   4293 C C   . ILE   A 1 592 ? 2.881   65.926  67.700  1.00 98.39  ?  714 ILE   A C   1 
ATOM   4294 O O   . ILE   A 1 592 ? 2.851   66.877  66.918  1.00 103.27 ?  714 ILE   A O   1 
ATOM   4295 C CB  . ILE   A 1 592 ? 5.089   64.800  67.569  1.00 94.34  ?  714 ILE   A CB  1 
ATOM   4296 C CG1 . ILE   A 1 592 ? 6.110   64.045  68.408  1.00 96.92  ?  714 ILE   A CG1 1 
ATOM   4297 C CG2 . ILE   A 1 592 ? 5.839   65.776  66.660  1.00 103.57 ?  714 ILE   A CG2 1 
ATOM   4298 C CD1 . ILE   A 1 592 ? 7.143   63.292  67.598  1.00 92.73  ?  714 ILE   A CD1 1 
ATOM   4299 N N   . MET   A 1 593 ? 1.831   65.138  67.908  1.00 96.45  ?  715 MET   A N   1 
ATOM   4300 C CA  . MET   A 1 593 ? 0.532   65.496  67.343  1.00 104.22 ?  715 MET   A CA  1 
ATOM   4301 C C   . MET   A 1 593 ? -0.066  66.776  67.944  1.00 110.27 ?  715 MET   A C   1 
ATOM   4302 O O   . MET   A 1 593 ? -1.155  67.197  67.531  1.00 110.74 ?  715 MET   A O   1 
ATOM   4303 C CB  . MET   A 1 593 ? -0.443  64.333  67.523  1.00 112.36 ?  715 MET   A CB  1 
ATOM   4304 C CG  . MET   A 1 593 ? -0.080  63.069  66.743  1.00 120.51 ?  715 MET   A CG  1 
ATOM   4305 S SD  . MET   A 1 593 ? -0.397  63.215  64.961  1.00 134.04 ?  715 MET   A SD  1 
ATOM   4306 C CE  . MET   A 1 593 ? -2.129  62.753  64.950  1.00 118.81 ?  715 MET   A CE  1 
ATOM   4307 N N   . GLU   A 1 594 ? 0.597   67.389  68.920  1.00 109.28 ?  716 GLU   A N   1 
ATOM   4308 C CA  . GLU   A 1 594 ? 0.212   68.683  69.456  1.00 104.80 ?  716 GLU   A CA  1 
ATOM   4309 C C   . GLU   A 1 594 ? 0.844   69.834  68.677  1.00 105.59 ?  716 GLU   A C   1 
ATOM   4310 O O   . GLU   A 1 594 ? 0.607   71.000  68.998  1.00 108.10 ?  716 GLU   A O   1 
ATOM   4311 C CB  . GLU   A 1 594 ? 0.591   68.729  70.940  1.00 99.54  ?  716 GLU   A CB  1 
ATOM   4312 C CG  . GLU   A 1 594 ? -0.332  67.912  71.835  1.00 99.23  ?  716 GLU   A CG  1 
ATOM   4313 C CD  . GLU   A 1 594 ? -0.274  68.350  73.300  1.00 98.77  ?  716 GLU   A CD  1 
ATOM   4314 O OE1 . GLU   A 1 594 ? 0.365   69.379  73.594  1.00 97.50  ?  716 GLU   A OE1 1 
ATOM   4315 O OE2 . GLU   A 1 594 ? -0.864  67.669  74.167  1.00 97.33  ?  716 GLU   A OE2 1 
ATOM   4316 N N   . ASN   A 1 595 ? 1.643   69.519  67.664  1.00 106.50 ?  717 ASN   A N   1 
ATOM   4317 C CA  . ASN   A 1 595 ? 2.285   70.469  66.769  1.00 108.63 ?  717 ASN   A CA  1 
ATOM   4318 C C   . ASN   A 1 595 ? 1.669   70.442  65.384  1.00 116.56 ?  717 ASN   A C   1 
ATOM   4319 O O   . ASN   A 1 595 ? 2.276   70.918  64.420  1.00 119.08 ?  717 ASN   A O   1 
ATOM   4320 C CB  . ASN   A 1 595 ? 3.765   70.148  66.670  1.00 114.97 ?  717 ASN   A CB  1 
ATOM   4321 C CG  . ASN   A 1 595 ? 4.573   71.056  67.484  1.00 120.89 ?  717 ASN   A CG  1 
ATOM   4322 O OD1 . ASN   A 1 595 ? 4.027   71.928  68.155  1.00 118.11 ?  717 ASN   A OD1 1 
ATOM   4323 N ND2 . ASN   A 1 595 ? 5.890   70.857  67.473  1.00 135.97 ?  717 ASN   A ND2 1 
ATOM   4324 N N   . ILE   A 1 596 ? 0.486   69.860  65.273  1.00 114.91 ?  718 ILE   A N   1 
ATOM   4325 C CA  . ILE   A 1 596 ? -0.177  69.602  64.009  1.00 114.70 ?  718 ILE   A CA  1 
ATOM   4326 C C   . ILE   A 1 596 ? -1.611  70.069  64.162  1.00 117.78 ?  718 ILE   A C   1 
ATOM   4327 O O   . ILE   A 1 596 ? -2.269  69.722  65.147  1.00 121.78 ?  718 ILE   A O   1 
ATOM   4328 C CB  . ILE   A 1 596 ? -0.118  68.107  63.654  1.00 110.65 ?  718 ILE   A CB  1 
ATOM   4329 C CG1 . ILE   A 1 596 ? 1.224   67.769  63.026  1.00 108.60 ?  718 ILE   A CG1 1 
ATOM   4330 C CG2 . ILE   A 1 596 ? -1.284  67.689  62.795  1.00 110.21 ?  718 ILE   A CG2 1 
ATOM   4331 C CD1 . ILE   A 1 596 ? 1.425   66.290  62.891  1.00 119.05 ?  718 ILE   A CD1 1 
ATOM   4332 N N   . SER   A 1 597 ? -2.086  70.868  63.209  1.00 115.18 ?  719 SER   A N   1 
ATOM   4333 C CA  . SER   A 1 597 ? -3.425  71.444  63.285  1.00 118.29 ?  719 SER   A CA  1 
ATOM   4334 C C   . SER   A 1 597 ? -4.518  70.398  63.492  1.00 118.05 ?  719 SER   A C   1 
ATOM   4335 O O   . SER   A 1 597 ? -4.296  69.202  63.276  1.00 118.85 ?  719 SER   A O   1 
ATOM   4336 C CB  . SER   A 1 597 ? -3.708  72.261  62.024  1.00 125.76 ?  719 SER   A CB  1 
ATOM   4337 O OG  . SER   A 1 597 ? -4.168  71.432  60.968  1.00 128.63 ?  719 SER   A OG  1 
ATOM   4338 N N   . ASP   A 1 598 ? -5.701  70.847  63.932  1.00 120.83 ?  720 ASP   A N   1 
ATOM   4339 C CA  . ASP   A 1 598 ? -6.830  69.939  64.138  1.00 125.44 ?  720 ASP   A CA  1 
ATOM   4340 C C   . ASP   A 1 598 ? -7.275  69.284  62.837  1.00 123.69 ?  720 ASP   A C   1 
ATOM   4341 O O   . ASP   A 1 598 ? -7.762  68.146  62.844  1.00 118.50 ?  720 ASP   A O   1 
ATOM   4342 C CB  . ASP   A 1 598 ? -8.022  70.691  64.741  1.00 130.19 ?  720 ASP   A CB  1 
ATOM   4343 C CG  . ASP   A 1 598 ? -7.696  71.364  66.052  1.00 130.10 ?  720 ASP   A CG  1 
ATOM   4344 O OD1 . ASP   A 1 598 ? -6.991  70.747  66.895  1.00 122.96 ?  720 ASP   A OD1 1 
ATOM   4345 O OD2 . ASP   A 1 598 ? -8.141  72.529  66.215  1.00 134.98 ?  720 ASP   A OD2 1 
ATOM   4346 N N   . ASP   A 1 599 ? -7.158  70.008  61.724  1.00 125.64 ?  721 ASP   A N   1 
ATOM   4347 C CA  . ASP   A 1 599 ? -7.576  69.480  60.432  1.00 125.20 ?  721 ASP   A CA  1 
ATOM   4348 C C   . ASP   A 1 599 ? -6.729  68.278  60.051  1.00 121.33 ?  721 ASP   A C   1 
ATOM   4349 O O   . ASP   A 1 599 ? -7.228  67.149  59.964  1.00 120.76 ?  721 ASP   A O   1 
ATOM   4350 C CB  . ASP   A 1 599 ? -7.485  70.584  59.379  1.00 124.13 ?  721 ASP   A CB  1 
ATOM   4351 C CG  . ASP   A 1 599 ? -8.097  71.893  59.862  1.00 133.66 ?  721 ASP   A CG  1 
ATOM   4352 O OD1 . ASP   A 1 599 ? -9.216  71.850  60.441  1.00 132.98 ?  721 ASP   A OD1 1 
ATOM   4353 O OD2 . ASP   A 1 599 ? -7.449  72.956  59.690  1.00 135.44 ?  721 ASP   A OD2 1 
ATOM   4354 N N   . VAL   A 1 600 ? -5.432  68.501  59.867  1.00 111.59 ?  722 VAL   A N   1 
ATOM   4355 C CA  . VAL   A 1 600 ? -4.482  67.454  59.537  1.00 112.07 ?  722 VAL   A CA  1 
ATOM   4356 C C   . VAL   A 1 600 ? -4.779  66.186  60.345  1.00 114.16 ?  722 VAL   A C   1 
ATOM   4357 O O   . VAL   A 1 600 ? -4.733  65.070  59.805  1.00 109.97 ?  722 VAL   A O   1 
ATOM   4358 C CB  . VAL   A 1 600 ? -3.053  67.973  59.776  1.00 110.77 ?  722 VAL   A CB  1 
ATOM   4359 C CG1 . VAL   A 1 600 ? -2.030  67.002  59.236  1.00 120.29 ?  722 VAL   A CG1 1 
ATOM   4360 C CG2 . VAL   A 1 600 ? -2.871  69.331  59.165  1.00 106.38 ?  722 VAL   A CG2 1 
ATOM   4361 N N   . ILE   A 1 601 ? -5.148  66.362  61.626  1.00 115.10 ?  723 ILE   A N   1 
ATOM   4362 C CA  . ILE   A 1 601 ? -5.344  65.234  62.541  1.00 117.73 ?  723 ILE   A CA  1 
ATOM   4363 C C   . ILE   A 1 601 ? -6.662  64.520  62.262  1.00 120.91 ?  723 ILE   A C   1 
ATOM   4364 O O   . ILE   A 1 601 ? -6.724  63.280  62.282  1.00 119.54 ?  723 ILE   A O   1 
ATOM   4365 C CB  . ILE   A 1 601 ? -5.258  65.689  64.014  1.00 113.19 ?  723 ILE   A CB  1 
ATOM   4366 C CG1 . ILE   A 1 601 ? -3.808  65.757  64.478  1.00 110.78 ?  723 ILE   A CG1 1 
ATOM   4367 C CG2 . ILE   A 1 601 ? -6.017  64.723  64.948  1.00 101.80 ?  723 ILE   A CG2 1 
ATOM   4368 C CD1 . ILE   A 1 601 ? -3.617  66.618  65.702  1.00 115.96 ?  723 ILE   A CD1 1 
ATOM   4369 N N   . VAL   A 1 602 ? -7.742  65.271  62.020  1.00 122.49 ?  724 VAL   A N   1 
ATOM   4370 C CA  . VAL   A 1 602 ? -8.990  64.601  61.660  1.00 125.82 ?  724 VAL   A CA  1 
ATOM   4371 C C   . VAL   A 1 602 ? -8.815  63.899  60.311  1.00 126.28 ?  724 VAL   A C   1 
ATOM   4372 O O   . VAL   A 1 602 ? -9.360  62.808  60.084  1.00 122.72 ?  724 VAL   A O   1 
ATOM   4373 C CB  . VAL   A 1 602 ? -10.180 65.592  61.655  1.00 123.29 ?  724 VAL   A CB  1 
ATOM   4374 C CG1 . VAL   A 1 602 ? -11.484 64.835  61.498  1.00 125.64 ?  724 VAL   A CG1 1 
ATOM   4375 C CG2 . VAL   A 1 602 ? -10.228 66.440  62.922  1.00 113.71 ?  724 VAL   A CG2 1 
ATOM   4376 N N   . GLY   A 1 603 ? -8.011  64.484  59.419  1.00 126.15 ?  725 GLY   A N   1 
ATOM   4377 C CA  . GLY   A 1 603 ? -7.683  63.872  58.146  1.00 121.27 ?  725 GLY   A CA  1 
ATOM   4378 C C   . GLY   A 1 603 ? -7.036  62.523  58.340  1.00 116.01 ?  725 GLY   A C   1 
ATOM   4379 O O   . GLY   A 1 603 ? -7.564  61.511  57.871  1.00 114.95 ?  725 GLY   A O   1 
ATOM   4380 N N   . ARG   A 1 604 ? -5.903  62.504  59.054  1.00 112.66 ?  726 ARG   A N   1 
ATOM   4381 C CA  . ARG   A 1 604 ? -5.240  61.243  59.356  1.00 112.36 ?  726 ARG   A CA  1 
ATOM   4382 C C   . ARG   A 1 604 ? -6.206  60.230  59.962  1.00 113.92 ?  726 ARG   A C   1 
ATOM   4383 O O   . ARG   A 1 604 ? -6.058  59.025  59.721  1.00 112.37 ?  726 ARG   A O   1 
ATOM   4384 C CB  . ARG   A 1 604 ? -4.035  61.475  60.280  1.00 108.74 ?  726 ARG   A CB  1 
ATOM   4385 C CG  . ARG   A 1 604 ? -2.961  62.420  59.732  1.00 106.18 ?  726 ARG   A CG  1 
ATOM   4386 C CD  . ARG   A 1 604 ? -1.671  62.348  60.548  1.00 104.07 ?  726 ARG   A CD  1 
ATOM   4387 N NE  . ARG   A 1 604 ? -0.672  63.314  60.093  1.00 111.12 ?  726 ARG   A NE  1 
ATOM   4388 C CZ  . ARG   A 1 604 ? 0.586   63.363  60.519  1.00 114.88 ?  726 ARG   A CZ  1 
ATOM   4389 N NH1 . ARG   A 1 604 ? 1.046   62.514  61.418  1.00 122.69 ?  726 ARG   A NH1 1 
ATOM   4390 N NH2 . ARG   A 1 604 ? 1.407   64.285  60.027  1.00 108.20 ?  726 ARG   A NH2 1 
ATOM   4391 N N   . CYS   A 1 605 ? -7.215  60.700  60.721  1.00 116.11 ?  727 CYS   A N   1 
ATOM   4392 C CA  . CYS   A 1 605 ? -8.229  59.802  61.295  1.00 124.45 ?  727 CYS   A CA  1 
ATOM   4393 C C   . CYS   A 1 605 ? -9.145  59.223  60.235  1.00 123.71 ?  727 CYS   A C   1 
ATOM   4394 O O   . CYS   A 1 605 ? -9.377  58.009  60.190  1.00 124.84 ?  727 CYS   A O   1 
ATOM   4395 C CB  . CYS   A 1 605 ? -9.111  60.511  62.329  1.00 123.62 ?  727 CYS   A CB  1 
ATOM   4396 S SG  . CYS   A 1 605 ? -8.435  60.813  63.934  1.00 122.24 ?  727 CYS   A SG  1 
ATOM   4397 N N   . LEU   A 1 606 ? -9.755  60.091  59.438  1.00 124.31 ?  728 LEU   A N   1 
ATOM   4398 C CA  . LEU   A 1 606 ? -10.723 59.625  58.459  1.00 127.33 ?  728 LEU   A CA  1 
ATOM   4399 C C   . LEU   A 1 606 ? -10.066 58.675  57.463  1.00 127.21 ?  728 LEU   A C   1 
ATOM   4400 O O   . LEU   A 1 606 ? -10.597 57.593  57.173  1.00 124.12 ?  728 LEU   A O   1 
ATOM   4401 C CB  . LEU   A 1 606 ? -11.363 60.834  57.778  1.00 126.85 ?  728 LEU   A CB  1 
ATOM   4402 C CG  . LEU   A 1 606 ? -12.090 61.718  58.806  1.00 125.55 ?  728 LEU   A CG  1 
ATOM   4403 C CD1 . LEU   A 1 606 ? -12.473 63.074  58.233  1.00 124.05 ?  728 LEU   A CD1 1 
ATOM   4404 C CD2 . LEU   A 1 606 ? -13.326 61.004  59.387  1.00 119.00 ?  728 LEU   A CD2 1 
ATOM   4405 N N   . ALA   A 1 607 ? -8.885  59.049  56.966  1.00 123.89 ?  729 ALA   A N   1 
ATOM   4406 C CA  . ALA   A 1 607 ? -8.109  58.143  56.131  1.00 122.03 ?  729 ALA   A CA  1 
ATOM   4407 C C   . ALA   A 1 607 ? -7.984  56.769  56.783  1.00 124.39 ?  729 ALA   A C   1 
ATOM   4408 O O   . ALA   A 1 607 ? -8.325  55.750  56.173  1.00 131.48 ?  729 ALA   A O   1 
ATOM   4409 C CB  . ALA   A 1 607 ? -6.735  58.746  55.846  1.00 115.87 ?  729 ALA   A CB  1 
ATOM   4410 N N   . ILE   A 1 608 ? -7.533  56.721  58.039  1.00 120.34 ?  730 ILE   A N   1 
ATOM   4411 C CA  . ILE   A 1 608 ? -7.389  55.426  58.708  1.00 124.98 ?  730 ILE   A CA  1 
ATOM   4412 C C   . ILE   A 1 608 ? -8.745  54.726  58.863  1.00 127.03 ?  730 ILE   A C   1 
ATOM   4413 O O   . ILE   A 1 608 ? -8.817  53.486  58.878  1.00 125.79 ?  730 ILE   A O   1 
ATOM   4414 C CB  . ILE   A 1 608 ? -6.629  55.602  60.050  1.00 120.23 ?  730 ILE   A CB  1 
ATOM   4415 C CG1 . ILE   A 1 608 ? -5.108  55.628  59.792  1.00 120.09 ?  730 ILE   A CG1 1 
ATOM   4416 C CG2 . ILE   A 1 608 ? -6.981  54.512  61.052  1.00 112.45 ?  730 ILE   A CG2 1 
ATOM   4417 C CD1 . ILE   A 1 608 ? -4.259  56.356  60.817  1.00 110.02 ?  730 ILE   A CD1 1 
ATOM   4418 N N   . LEU   A 1 609 ? -9.841  55.493  58.899  1.00 125.36 ?  731 LEU   A N   1 
ATOM   4419 C CA  . LEU   A 1 609 ? -11.179 54.898  58.961  1.00 129.93 ?  731 LEU   A CA  1 
ATOM   4420 C C   . LEU   A 1 609 ? -11.678 54.435  57.590  1.00 134.28 ?  731 LEU   A C   1 
ATOM   4421 O O   . LEU   A 1 609 ? -12.375 53.410  57.498  1.00 129.84 ?  731 LEU   A O   1 
ATOM   4422 C CB  . LEU   A 1 609 ? -12.170 55.900  59.550  1.00 130.00 ?  731 LEU   A CB  1 
ATOM   4423 C CG  . LEU   A 1 609 ? -12.073 56.275  61.019  1.00 125.17 ?  731 LEU   A CG  1 
ATOM   4424 C CD1 . LEU   A 1 609 ? -12.965 57.468  61.267  1.00 125.61 ?  731 LEU   A CD1 1 
ATOM   4425 C CD2 . LEU   A 1 609 ? -12.511 55.098  61.862  1.00 123.13 ?  731 LEU   A CD2 1 
ATOM   4426 N N   . LYS   A 1 610 ? -11.367 55.207  56.534  1.00 131.43 ?  732 LYS   A N   1 
ATOM   4427 C CA  . LYS   A 1 610 ? -11.706 54.831  55.159  1.00 131.12 ?  732 LYS   A CA  1 
ATOM   4428 C C   . LYS   A 1 610 ? -11.134 53.461  54.803  1.00 129.91 ?  732 LYS   A C   1 
ATOM   4429 O O   . LYS   A 1 610 ? -11.856 52.566  54.345  1.00 124.26 ?  732 LYS   A O   1 
ATOM   4430 C CB  . LYS   A 1 610 ? -11.172 55.884  54.180  1.00 131.40 ?  732 LYS   A CB  1 
ATOM   4431 C CG  . LYS   A 1 610 ? -11.856 57.253  54.199  1.00 131.26 ?  732 LYS   A CG  1 
ATOM   4432 C CD  . LYS   A 1 610 ? -11.116 58.205  53.231  1.00 134.49 ?  732 LYS   A CD  1 
ATOM   4433 C CE  . LYS   A 1 610 ? -11.662 59.640  53.227  1.00 132.23 ?  732 LYS   A CE  1 
ATOM   4434 N NZ  . LYS   A 1 610 ? -13.137 59.688  53.448  1.00 137.56 ?  732 LYS   A NZ  1 
ATOM   4435 N N   . GLY   A 1 611 ? -9.821  53.295  54.993  1.00 127.94 ?  733 GLY   A N   1 
ATOM   4436 C CA  . GLY   A 1 611 ? -9.202  52.000  54.777  1.00 127.33 ?  733 GLY   A CA  1 
ATOM   4437 C C   . GLY   A 1 611 ? -9.906  50.870  55.505  1.00 129.64 ?  733 GLY   A C   1 
ATOM   4438 O O   . GLY   A 1 611 ? -10.021 49.761  54.979  1.00 134.86 ?  733 GLY   A O   1 
ATOM   4439 N N   . ILE   A 1 612 ? -10.412 51.137  56.713  1.00 127.38 ?  734 ILE   A N   1 
ATOM   4440 C CA  . ILE   A 1 612 ? -10.959 50.059  57.539  1.00 134.11 ?  734 ILE   A CA  1 
ATOM   4441 C C   . ILE   A 1 612 ? -12.459 49.844  57.340  1.00 134.73 ?  734 ILE   A C   1 
ATOM   4442 O O   . ILE   A 1 612 ? -12.952 48.729  57.578  1.00 134.11 ?  734 ILE   A O   1 
ATOM   4443 C CB  . ILE   A 1 612 ? -10.616 50.313  59.023  1.00 134.30 ?  734 ILE   A CB  1 
ATOM   4444 C CG1 . ILE   A 1 612 ? -9.158  49.924  59.268  1.00 134.45 ?  734 ILE   A CG1 1 
ATOM   4445 C CG2 . ILE   A 1 612 ? -11.525 49.528  59.985  1.00 120.09 ?  734 ILE   A CG2 1 
ATOM   4446 C CD1 . ILE   A 1 612 ? -8.570  50.523  60.496  1.00 127.29 ?  734 ILE   A CD1 1 
ATOM   4447 N N   . PHE   A 1 613 ? -13.197 50.858  56.880  1.00 132.34 ?  735 PHE   A N   1 
ATOM   4448 C CA  . PHE   A 1 613 ? -14.629 50.701  56.657  1.00 135.52 ?  735 PHE   A CA  1 
ATOM   4449 C C   . PHE   A 1 613 ? -15.096 50.990  55.238  1.00 136.17 ?  735 PHE   A C   1 
ATOM   4450 O O   . PHE   A 1 613 ? -16.277 50.763  54.938  1.00 134.49 ?  735 PHE   A O   1 
ATOM   4451 C CB  . PHE   A 1 613 ? -15.427 51.571  57.644  1.00 136.60 ?  735 PHE   A CB  1 
ATOM   4452 C CG  . PHE   A 1 613 ? -15.416 51.039  59.038  1.00 135.93 ?  735 PHE   A CG  1 
ATOM   4453 C CD1 . PHE   A 1 613 ? -16.298 50.029  59.406  1.00 141.22 ?  735 PHE   A CD1 1 
ATOM   4454 C CD2 . PHE   A 1 613 ? -14.508 51.496  59.966  1.00 134.81 ?  735 PHE   A CD2 1 
ATOM   4455 C CE1 . PHE   A 1 613 ? -16.293 49.492  60.695  1.00 139.75 ?  735 PHE   A CE1 1 
ATOM   4456 C CE2 . PHE   A 1 613 ? -14.497 50.961  61.257  1.00 138.54 ?  735 PHE   A CE2 1 
ATOM   4457 C CZ  . PHE   A 1 613 ? -15.396 49.955  61.621  1.00 134.27 ?  735 PHE   A CZ  1 
ATOM   4458 N N   . GLY   A 1 614 ? -14.219 51.458  54.356  1.00 130.62 ?  736 GLY   A N   1 
ATOM   4459 C CA  . GLY   A 1 614 ? -14.616 51.696  52.985  1.00 129.62 ?  736 GLY   A CA  1 
ATOM   4460 C C   . GLY   A 1 614 ? -14.587 53.162  52.636  1.00 128.53 ?  736 GLY   A C   1 
ATOM   4461 O O   . GLY   A 1 614 ? -15.311 53.949  53.245  1.00 129.46 ?  736 GLY   A O   1 
ATOM   4462 N N   . SER   A 1 615 ? -13.773 53.538  51.637  1.00 131.59 ?  737 SER   A N   1 
ATOM   4463 C CA  . SER   A 1 615 ? -13.480 54.920  51.250  1.00 134.82 ?  737 SER   A CA  1 
ATOM   4464 C C   . SER   A 1 615 ? -14.825 55.813  51.222  1.00 137.61 ?  737 SER   A C   1 
ATOM   4465 O O   . SER   A 1 615 ? -14.813 57.024  51.548  1.00 136.23 ?  737 SER   A O   1 
ATOM   4466 C CB  . SER   A 1 615 ? -12.469 54.903  50.095  1.00 131.37 ?  737 SER   A CB  1 
ATOM   4467 O OG  . SER   A 1 615 ? -12.432 56.137  49.398  1.00 138.96 ?  737 SER   A OG  1 
ATOM   4468 N N   . SER   A 1 616 ? -15.964 55.210  50.872  1.00 136.44 ?  738 SER   A N   1 
ATOM   4469 C CA  . SER   A 1 616 ? -17.267 55.866  50.856  1.00 135.54 ?  738 SER   A CA  1 
ATOM   4470 C C   . SER   A 1 616 ? -18.155 55.895  52.088  1.00 135.20 ?  738 SER   A C   1 
ATOM   4471 O O   . SER   A 1 616 ? -18.785 56.922  52.355  1.00 133.65 ?  738 SER   A O   1 
ATOM   4472 C CB  . SER   A 1 616 ? -18.033 55.175  49.724  1.00 141.43 ?  738 SER   A CB  1 
ATOM   4473 O OG  . SER   A 1 616 ? -18.194 53.793  50.002  1.00 142.13 ?  738 SER   A OG  1 
ATOM   4474 N N   . ALA   A 1 617 ? -18.227 54.774  52.848  1.00 135.36 ?  739 ALA   A N   1 
ATOM   4475 C CA  . ALA   A 1 617 ? -18.996 54.538  54.087  1.00 140.64 ?  739 ALA   A CA  1 
ATOM   4476 C C   . ALA   A 1 617 ? -18.585 55.503  55.336  1.00 147.47 ?  739 ALA   A C   1 
ATOM   4477 O O   . ALA   A 1 617 ? -19.259 55.376  56.386  1.00 141.65 ?  739 ALA   A O   1 
ATOM   4478 C CB  . ALA   A 1 617 ? -18.907 53.061  54.468  1.00 131.62 ?  739 ALA   A CB  1 
ATOM   4479 N N   . VAL   A 1 618 ? -17.589 56.379  55.204  1.00 150.49 ?  740 VAL   A N   1 
ATOM   4480 C CA  . VAL   A 1 618 ? -17.079 57.218  56.283  1.00 138.28 ?  740 VAL   A CA  1 
ATOM   4481 C C   . VAL   A 1 618 ? -17.290 58.689  55.931  1.00 135.45 ?  740 VAL   A C   1 
ATOM   4482 O O   . VAL   A 1 618 ? -16.515 59.278  55.178  1.00 130.40 ?  740 VAL   A O   1 
ATOM   4483 C CB  . VAL   A 1 618 ? -15.581 56.919  56.508  1.00 137.45 ?  740 VAL   A CB  1 
ATOM   4484 C CG1 . VAL   A 1 618 ? -14.950 57.936  57.437  1.00 135.25 ?  740 VAL   A CG1 1 
ATOM   4485 C CG2 . VAL   A 1 618 ? -15.387 55.518  57.069  1.00 136.71 ?  740 VAL   A CG2 1 
ATOM   4486 N N   . PRO   A 1 619 ? -18.352 59.324  56.481  1.00 138.26 ?  741 PRO   A N   1 
ATOM   4487 C CA  . PRO   A 1 619 ? -18.709 60.691  56.053  1.00 139.79 ?  741 PRO   A CA  1 
ATOM   4488 C C   . PRO   A 1 619 ? -17.806 61.763  56.637  1.00 138.66 ?  741 PRO   A C   1 
ATOM   4489 O O   . PRO   A 1 619 ? -16.730 61.459  57.151  1.00 144.64 ?  741 PRO   A O   1 
ATOM   4490 C CB  . PRO   A 1 619 ? -20.155 60.852  56.554  1.00 136.66 ?  741 PRO   A CB  1 
ATOM   4491 C CG  . PRO   A 1 619 ? -20.297 59.904  57.690  1.00 136.55 ?  741 PRO   A CG  1 
ATOM   4492 C CD  . PRO   A 1 619 ? -19.249 58.812  57.532  1.00 137.90 ?  741 PRO   A CD  1 
ATOM   4493 N N   . GLN   A 1 620 ? -18.219 63.016  56.556  1.00 137.83 ?  742 GLN   A N   1 
ATOM   4494 C CA  . GLN   A 1 620 ? -17.511 64.005  57.351  1.00 140.42 ?  742 GLN   A CA  1 
ATOM   4495 C C   . GLN   A 1 620 ? -18.011 64.016  58.796  1.00 146.94 ?  742 GLN   A C   1 
ATOM   4496 O O   . GLN   A 1 620 ? -19.168 63.674  59.078  1.00 146.29 ?  742 GLN   A O   1 
ATOM   4497 C CB  . GLN   A 1 620 ? -17.644 65.400  56.744  1.00 136.76 ?  742 GLN   A CB  1 
ATOM   4498 C CG  . GLN   A 1 620 ? -16.721 65.640  55.572  1.00 137.61 ?  742 GLN   A CG  1 
ATOM   4499 C CD  . GLN   A 1 620 ? -15.311 65.146  55.851  1.00 136.65 ?  742 GLN   A CD  1 
ATOM   4500 O OE1 . GLN   A 1 620 ? -14.545 65.809  56.542  1.00 135.73 ?  742 GLN   A OE1 1 
ATOM   4501 N NE2 . GLN   A 1 620 ? -14.966 63.974  55.321  1.00 135.19 ?  742 GLN   A NE2 1 
ATOM   4502 N N   . PRO   A 1 621 ? -17.141 64.382  59.729  1.00 146.69 ?  743 PRO   A N   1 
ATOM   4503 C CA  . PRO   A 1 621 ? -17.594 64.622  61.097  1.00 141.93 ?  743 PRO   A CA  1 
ATOM   4504 C C   . PRO   A 1 621 ? -18.320 65.954  61.197  1.00 143.68 ?  743 PRO   A C   1 
ATOM   4505 O O   . PRO   A 1 621 ? -17.917 66.963  60.604  1.00 138.73 ?  743 PRO   A O   1 
ATOM   4506 C CB  . PRO   A 1 621 ? -16.291 64.634  61.899  1.00 141.19 ?  743 PRO   A CB  1 
ATOM   4507 C CG  . PRO   A 1 621 ? -15.265 65.113  60.911  1.00 141.21 ?  743 PRO   A CG  1 
ATOM   4508 C CD  . PRO   A 1 621 ? -15.695 64.621  59.563  1.00 141.83 ?  743 PRO   A CD  1 
ATOM   4509 N N   . LYS   A 1 622 ? -19.414 65.939  61.957  1.00 146.17 ?  744 LYS   A N   1 
ATOM   4510 C CA  . LYS   A 1 622 ? -20.144 67.171  62.230  1.00 147.24 ?  744 LYS   A CA  1 
ATOM   4511 C C   . LYS   A 1 622 ? -19.376 68.062  63.208  1.00 145.64 ?  744 LYS   A C   1 
ATOM   4512 O O   . LYS   A 1 622 ? -19.329 69.289  63.037  1.00 140.97 ?  744 LYS   A O   1 
ATOM   4513 C CB  . LYS   A 1 622 ? -21.529 66.823  62.776  1.00 148.28 ?  744 LYS   A CB  1 
ATOM   4514 C CG  . LYS   A 1 622 ? -22.392 66.039  61.799  1.00 150.50 ?  744 LYS   A CG  1 
ATOM   4515 C CD  . LYS   A 1 622 ? -22.871 66.939  60.659  1.00 158.22 ?  744 LYS   A CD  1 
ATOM   4516 C CE  . LYS   A 1 622 ? -22.683 66.278  59.292  1.00 155.40 ?  744 LYS   A CE  1 
ATOM   4517 N NZ  . LYS   A 1 622 ? -23.543 65.062  59.131  1.00 148.53 ?  744 LYS   A NZ  1 
ATOM   4518 N N   . GLU   A 1 623 ? -18.747 67.452  64.225  1.00 144.78 ?  745 GLU   A N   1 
ATOM   4519 C CA  . GLU   A 1 623 ? -18.019 68.151  65.279  1.00 136.67 ?  745 GLU   A CA  1 
ATOM   4520 C C   . GLU   A 1 623 ? -16.713 67.426  65.608  1.00 125.87 ?  745 GLU   A C   1 
ATOM   4521 O O   . GLU   A 1 623 ? -16.709 66.200  65.779  1.00 113.92 ?  745 GLU   A O   1 
ATOM   4522 C CB  . GLU   A 1 623 ? -18.903 68.284  66.528  1.00 138.02 ?  745 GLU   A CB  1 
ATOM   4523 C CG  . GLU   A 1 623 ? -20.041 69.314  66.413  1.00 140.56 ?  745 GLU   A CG  1 
ATOM   4524 C CD  . GLU   A 1 623 ? -19.521 70.739  66.188  1.00 143.05 ?  745 GLU   A CD  1 
ATOM   4525 O OE1 . GLU   A 1 623 ? -18.680 71.200  67.001  1.00 140.72 ?  745 GLU   A OE1 1 
ATOM   4526 O OE2 . GLU   A 1 623 ? -19.964 71.400  65.214  1.00 142.59 ?  745 GLU   A OE2 1 
ATOM   4527 N N   . THR   A 1 624 ? -15.614 68.199  65.705  1.00 123.10 ?  746 THR   A N   1 
ATOM   4528 C CA  . THR   A 1 624 ? -14.266 67.699  66.000  1.00 121.79 ?  746 THR   A CA  1 
ATOM   4529 C C   . THR   A 1 624 ? -13.590 68.463  67.144  1.00 124.66 ?  746 THR   A C   1 
ATOM   4530 O O   . THR   A 1 624 ? -13.585 69.702  67.150  1.00 124.09 ?  746 THR   A O   1 
ATOM   4531 C CB  . THR   A 1 624 ? -13.366 67.779  64.767  1.00 118.01 ?  746 THR   A CB  1 
ATOM   4532 O OG1 . THR   A 1 624 ? -13.447 69.098  64.211  1.00 120.82 ?  746 THR   A OG1 1 
ATOM   4533 C CG2 . THR   A 1 624 ? -13.743 66.733  63.750  1.00 119.07 ?  746 THR   A CG2 1 
ATOM   4534 N N   . VAL   A 1 625 ? -12.975 67.704  68.074  1.00 117.77 ?  747 VAL   A N   1 
ATOM   4535 C CA  . VAL   A 1 625 ? -12.318 68.169  69.306  1.00 105.55 ?  747 VAL   A CA  1 
ATOM   4536 C C   . VAL   A 1 625 ? -10.979 67.453  69.442  1.00 106.02 ?  747 VAL   A C   1 
ATOM   4537 O O   . VAL   A 1 625 ? -10.954 66.243  69.686  1.00 103.94 ?  747 VAL   A O   1 
ATOM   4538 C CB  . VAL   A 1 625 ? -13.154 67.882  70.560  1.00 101.35 ?  747 VAL   A CB  1 
ATOM   4539 C CG1 . VAL   A 1 625 ? -12.570 68.601  71.701  1.00 106.94 ?  747 VAL   A CG1 1 
ATOM   4540 C CG2 . VAL   A 1 625 ? -14.581 68.287  70.388  1.00 99.67  ?  747 VAL   A CG2 1 
ATOM   4541 N N   . VAL   A 1 626 ? -9.877  68.191  69.356  1.00 105.20 ?  748 VAL   A N   1 
ATOM   4542 C CA  . VAL   A 1 626 ? -8.533  67.623  69.492  1.00 103.75 ?  748 VAL   A CA  1 
ATOM   4543 C C   . VAL   A 1 626 ? -7.941  68.099  70.803  1.00 109.35 ?  748 VAL   A C   1 
ATOM   4544 O O   . VAL   A 1 626 ? -7.581  69.276  70.923  1.00 120.97 ?  748 VAL   A O   1 
ATOM   4545 C CB  . VAL   A 1 626 ? -7.610  68.034  68.340  1.00 108.32 ?  748 VAL   A CB  1 
ATOM   4546 C CG1 . VAL   A 1 626 ? -6.243  67.367  68.476  1.00 103.78 ?  748 VAL   A CG1 1 
ATOM   4547 C CG2 . VAL   A 1 626 ? -8.237  67.696  67.040  1.00 119.34 ?  748 VAL   A CG2 1 
ATOM   4548 N N   . SER   A 1 627 ? -7.756  67.190  71.756  1.00 100.43 ?  749 SER   A N   1 
ATOM   4549 C CA  . SER   A 1 627 ? -7.154  67.560  73.031  1.00 97.02  ?  749 SER   A CA  1 
ATOM   4550 C C   . SER   A 1 627 ? -5.653  67.870  72.908  1.00 96.83  ?  749 SER   A C   1 
ATOM   4551 O O   . SER   A 1 627 ? -4.937  67.340  72.049  1.00 96.95  ?  749 SER   A O   1 
ATOM   4552 C CB  . SER   A 1 627 ? -7.361  66.447  74.046  1.00 91.74  ?  749 SER   A CB  1 
ATOM   4553 O OG  . SER   A 1 627 ? -6.249  65.579  74.031  1.00 87.87  ?  749 SER   A OG  1 
ATOM   4554 N N   . ARG   A 1 628 ? -5.177  68.751  73.799  1.00 93.25  ?  750 ARG   A N   1 
ATOM   4555 C CA  . ARG   A 1 628 ? -3.754  69.126  73.893  1.00 100.11 ?  750 ARG   A CA  1 
ATOM   4556 C C   . ARG   A 1 628 ? -3.367  69.269  75.370  1.00 99.21  ?  750 ARG   A C   1 
ATOM   4557 O O   . ARG   A 1 628 ? -3.291  70.367  75.928  1.00 97.06  ?  750 ARG   A O   1 
ATOM   4558 C CB  . ARG   A 1 628 ? -3.449  70.408  73.133  1.00 109.47 ?  750 ARG   A CB  1 
ATOM   4559 C CG  . ARG   A 1 628 ? -2.994  70.209  71.731  1.00 110.32 ?  750 ARG   A CG  1 
ATOM   4560 C CD  . ARG   A 1 628 ? -2.697  71.551  71.058  1.00 112.77 ?  750 ARG   A CD  1 
ATOM   4561 N NE  . ARG   A 1 628 ? -2.349  71.304  69.667  1.00 122.38 ?  750 ARG   A NE  1 
ATOM   4562 C CZ  . ARG   A 1 628 ? -3.175  70.775  68.770  1.00 128.63 ?  750 ARG   A CZ  1 
ATOM   4563 N NH1 . ARG   A 1 628 ? -4.461  70.563  69.043  1.00 124.91 ?  750 ARG   A NH1 1 
ATOM   4564 N NH2 . ARG   A 1 628 ? -2.697  70.436  67.573  1.00 125.15 ?  750 ARG   A NH2 1 
ATOM   4565 N N   . TRP   A 1 629 ? -3.078  68.135  76.000  1.00 99.76  ?  751 TRP   A N   1 
ATOM   4566 C CA  . TRP   A 1 629 ? -2.894  68.123  77.438  1.00 88.85  ?  751 TRP   A CA  1 
ATOM   4567 C C   . TRP   A 1 629 ? -1.508  68.579  77.828  1.00 85.65  ?  751 TRP   A C   1 
ATOM   4568 O O   . TRP   A 1 629 ? -1.356  69.249  78.841  1.00 90.38  ?  751 TRP   A O   1 
ATOM   4569 C CB  . TRP   A 1 629 ? -3.161  66.736  77.994  1.00 88.53  ?  751 TRP   A CB  1 
ATOM   4570 C CG  . TRP   A 1 629 ? -4.597  66.385  78.099  1.00 88.53  ?  751 TRP   A CG  1 
ATOM   4571 C CD1 . TRP   A 1 629 ? -5.277  65.484  77.345  1.00 89.88  ?  751 TRP   A CD1 1 
ATOM   4572 C CD2 . TRP   A 1 629 ? -5.533  66.914  79.028  1.00 91.53  ?  751 TRP   A CD2 1 
ATOM   4573 N NE1 . TRP   A 1 629 ? -6.582  65.404  77.753  1.00 86.33  ?  751 TRP   A NE1 1 
ATOM   4574 C CE2 . TRP   A 1 629 ? -6.767  66.281  78.785  1.00 94.28  ?  751 TRP   A CE2 1 
ATOM   4575 C CE3 . TRP   A 1 629 ? -5.450  67.851  80.055  1.00 92.26  ?  751 TRP   A CE3 1 
ATOM   4576 C CZ2 . TRP   A 1 629 ? -7.917  66.570  79.526  1.00 98.22  ?  751 TRP   A CZ2 1 
ATOM   4577 C CZ3 . TRP   A 1 629 ? -6.589  68.131  80.793  1.00 95.50  ?  751 TRP   A CZ3 1 
ATOM   4578 C CH2 . TRP   A 1 629 ? -7.809  67.496  80.523  1.00 92.82  ?  751 TRP   A CH2 1 
ATOM   4579 N N   . ARG   A 1 630 ? -0.478  68.211  77.082  1.00 85.01  ?  752 ARG   A N   1 
ATOM   4580 C CA  . ARG   A 1 630 ? 0.826   68.763  77.415  1.00 85.14  ?  752 ARG   A CA  1 
ATOM   4581 C C   . ARG   A 1 630 ? 0.851   70.259  77.104  1.00 90.76  ?  752 ARG   A C   1 
ATOM   4582 O O   . ARG   A 1 630 ? 1.564   71.039  77.758  1.00 86.68  ?  752 ARG   A O   1 
ATOM   4583 C CB  . ARG   A 1 630 ? 1.909   67.994  76.664  1.00 85.38  ?  752 ARG   A CB  1 
ATOM   4584 C CG  . ARG   A 1 630 ? 3.361   68.234  77.080  1.00 86.96  ?  752 ARG   A CG  1 
ATOM   4585 C CD  . ARG   A 1 630 ? 3.767   67.619  78.386  1.00 80.74  ?  752 ARG   A CD  1 
ATOM   4586 N NE  . ARG   A 1 630 ? 4.291   66.283  78.160  1.00 88.13  ?  752 ARG   A NE  1 
ATOM   4587 C CZ  . ARG   A 1 630 ? 4.270   65.315  79.068  1.00 95.38  ?  752 ARG   A CZ  1 
ATOM   4588 N NH1 . ARG   A 1 630 ? 3.905   65.547  80.322  1.00 86.91  ?  752 ARG   A NH1 1 
ATOM   4589 N NH2 . ARG   A 1 630 ? 4.614   64.079  78.710  1.00 98.51  ?  752 ARG   A NH2 1 
ATOM   4590 N N   . ALA   A 1 631 ? 0.031   70.683  76.147  1.00 92.16  ?  753 ALA   A N   1 
ATOM   4591 C CA  . ALA   A 1 631 ? -0.080  72.105  75.855  1.00 92.76  ?  753 ALA   A CA  1 
ATOM   4592 C C   . ALA   A 1 631 ? -0.682  72.856  77.033  1.00 88.75  ?  753 ALA   A C   1 
ATOM   4593 O O   . ALA   A 1 631 ? -0.036  73.732  77.612  1.00 87.30  ?  753 ALA   A O   1 
ATOM   4594 C CB  . ALA   A 1 631 ? -0.921  72.312  74.595  1.00 102.64 ?  753 ALA   A CB  1 
ATOM   4595 N N   . ASP   A 1 632 ? -1.936  72.515  77.396  1.00 91.19  ?  754 ASP   A N   1 
ATOM   4596 C CA  . ASP   A 1 632 ? -2.783  73.046  78.467  1.00 88.08  ?  754 ASP   A CA  1 
ATOM   4597 C C   . ASP   A 1 632 ? -2.008  73.431  79.719  1.00 90.31  ?  754 ASP   A C   1 
ATOM   4598 O O   . ASP   A 1 632 ? -1.507  72.568  80.453  1.00 89.49  ?  754 ASP   A O   1 
ATOM   4599 C CB  . ASP   A 1 632 ? -3.856  72.024  78.842  1.00 91.63  ?  754 ASP   A CB  1 
ATOM   4600 C CG  . ASP   A 1 632 ? -4.817  72.520  79.929  1.00 91.99  ?  754 ASP   A CG  1 
ATOM   4601 O OD1 . ASP   A 1 632 ? -4.611  73.597  80.531  1.00 91.80  ?  754 ASP   A OD1 1 
ATOM   4602 O OD2 . ASP   A 1 632 ? -5.812  71.808  80.183  1.00 95.67  ?  754 ASP   A OD2 1 
ATOM   4603 N N   . PRO   A 1 633 ? -1.990  74.724  80.039  1.00 90.92  ?  755 PRO   A N   1 
ATOM   4604 C CA  . PRO   A 1 633 ? -1.128  75.230  81.114  1.00 87.54  ?  755 PRO   A CA  1 
ATOM   4605 C C   . PRO   A 1 633 ? -1.594  74.903  82.520  1.00 90.24  ?  755 PRO   A C   1 
ATOM   4606 O O   . PRO   A 1 633 ? -0.820  75.127  83.459  1.00 94.71  ?  755 PRO   A O   1 
ATOM   4607 C CB  . PRO   A 1 633 ? -1.178  76.721  80.885  1.00 87.99  ?  755 PRO   A CB  1 
ATOM   4608 C CG  . PRO   A 1 633 ? -2.583  76.903  80.354  1.00 87.18  ?  755 PRO   A CG  1 
ATOM   4609 C CD  . PRO   A 1 633 ? -2.743  75.802  79.389  1.00 86.88  ?  755 PRO   A CD  1 
ATOM   4610 N N   . TRP   A 1 634 ? -2.829  74.433  82.705  1.00 86.72  ?  756 TRP   A N   1 
ATOM   4611 C CA  . TRP   A 1 634 ? -3.347  74.010  84.001  1.00 83.71  ?  756 TRP   A CA  1 
ATOM   4612 C C   . TRP   A 1 634 ? -3.222  72.507  84.212  1.00 91.50  ?  756 TRP   A C   1 
ATOM   4613 O O   . TRP   A 1 634 ? -4.034  71.885  84.917  1.00 91.41  ?  756 TRP   A O   1 
ATOM   4614 C CB  . TRP   A 1 634 ? -4.793  74.451  84.125  1.00 84.65  ?  756 TRP   A CB  1 
ATOM   4615 C CG  . TRP   A 1 634 ? -4.981  75.865  83.671  1.00 91.54  ?  756 TRP   A CG  1 
ATOM   4616 C CD1 . TRP   A 1 634 ? -5.869  76.315  82.758  1.00 92.67  ?  756 TRP   A CD1 1 
ATOM   4617 C CD2 . TRP   A 1 634 ? -4.240  77.022  84.114  1.00 93.76  ?  756 TRP   A CD2 1 
ATOM   4618 N NE1 . TRP   A 1 634 ? -5.755  77.681  82.618  1.00 87.75  ?  756 TRP   A NE1 1 
ATOM   4619 C CE2 . TRP   A 1 634 ? -4.762  78.135  83.437  1.00 83.45  ?  756 TRP   A CE2 1 
ATOM   4620 C CE3 . TRP   A 1 634 ? -3.204  77.220  85.041  1.00 94.95  ?  756 TRP   A CE3 1 
ATOM   4621 C CZ2 . TRP   A 1 634 ? -4.288  79.409  83.632  1.00 84.98  ?  756 TRP   A CZ2 1 
ATOM   4622 C CZ3 . TRP   A 1 634 ? -2.735  78.480  85.229  1.00 94.92  ?  756 TRP   A CZ3 1 
ATOM   4623 C CH2 . TRP   A 1 634 ? -3.274  79.568  84.522  1.00 91.28  ?  756 TRP   A CH2 1 
ATOM   4624 N N   . ALA   A 1 635 ? -2.210  71.950  83.544  1.00 92.21  ?  757 ALA   A N   1 
ATOM   4625 C CA  . ALA   A 1 635 ? -1.980  70.497  83.614  1.00 83.73  ?  757 ALA   A CA  1 
ATOM   4626 C C   . ALA   A 1 635 ? -0.605  70.119  83.071  1.00 84.01  ?  757 ALA   A C   1 
ATOM   4627 O O   . ALA   A 1 635 ? 0.033   69.258  83.652  1.00 88.01  ?  757 ALA   A O   1 
ATOM   4628 C CB  . ALA   A 1 635 ? -3.032  69.850  82.811  1.00 80.37  ?  757 ALA   A CB  1 
ATOM   4629 N N   . ARG   A 1 636 ? -0.197  70.684  81.960  1.00 79.33  ?  758 ARG   A N   1 
ATOM   4630 C CA  . ARG   A 1 636 ? 1.173   70.388  81.511  1.00 82.47  ?  758 ARG   A CA  1 
ATOM   4631 C C   . ARG   A 1 636 ? 1.349   68.883  81.416  1.00 82.91  ?  758 ARG   A C   1 
ATOM   4632 O O   . ARG   A 1 636 ? 2.448   68.411  81.654  1.00 79.67  ?  758 ARG   A O   1 
ATOM   4633 C CB  . ARG   A 1 636 ? 2.118   70.991  82.530  1.00 87.25  ?  758 ARG   A CB  1 
ATOM   4634 C CG  . ARG   A 1 636 ? 2.225   72.503  82.437  1.00 86.92  ?  758 ARG   A CG  1 
ATOM   4635 C CD  . ARG   A 1 636 ? 2.952   72.897  81.171  1.00 94.62  ?  758 ARG   A CD  1 
ATOM   4636 N NE  . ARG   A 1 636 ? 3.384   74.282  81.205  1.00 108.39 ?  758 ARG   A NE  1 
ATOM   4637 C CZ  . ARG   A 1 636 ? 2.658   75.298  80.763  1.00 107.05 ?  758 ARG   A CZ  1 
ATOM   4638 N NH1 . ARG   A 1 636 ? 2.756   75.682  79.505  1.00 103.99 ?  758 ARG   A NH1 1 
ATOM   4639 N NH2 . ARG   A 1 636 ? 1.831   75.921  81.582  1.00 108.29 ?  758 ARG   A NH2 1 
ATOM   4640 N N   . GLY   A 1 637 ? 0.305   68.174  81.039  1.00 81.49  ?  759 GLY   A N   1 
ATOM   4641 C CA  . GLY   A 1 637 ? 0.334   66.742  80.836  1.00 85.01  ?  759 GLY   A CA  1 
ATOM   4642 C C   . GLY   A 1 637 ? -0.994  66.107  81.231  1.00 90.10  ?  759 GLY   A C   1 
ATOM   4643 O O   . GLY   A 1 637 ? -2.005  66.790  81.390  1.00 90.99  ?  759 GLY   A O   1 
ATOM   4644 N N   . SER   A 1 638 ? -0.955  64.780  81.401  1.00 87.06  ?  760 SER   A N   1 
ATOM   4645 C CA  . SER   A 1 638 ? -2.130  63.929  81.539  1.00 81.05  ?  760 SER   A CA  1 
ATOM   4646 C C   . SER   A 1 638 ? -2.177  63.195  82.868  1.00 87.69  ?  760 SER   A C   1 
ATOM   4647 O O   . SER   A 1 638 ? -3.214  63.199  83.530  1.00 92.76  ?  760 SER   A O   1 
ATOM   4648 C CB  . SER   A 1 638 ? -2.134  62.922  80.407  1.00 86.06  ?  760 SER   A CB  1 
ATOM   4649 O OG  . SER   A 1 638 ? -0.940  62.154  80.493  1.00 91.38  ?  760 SER   A OG  1 
ATOM   4650 N N   . TYR   A 1 639 ? -1.101  62.529  83.267  1.00 88.38  ?  761 TYR   A N   1 
ATOM   4651 C CA  . TYR   A 1 639 ? -1.004  61.969  84.611  1.00 84.13  ?  761 TYR   A CA  1 
ATOM   4652 C C   . TYR   A 1 639 ? 0.430   61.542  84.881  1.00 84.34  ?  761 TYR   A C   1 
ATOM   4653 O O   . TYR   A 1 639 ? 1.332   61.757  84.069  1.00 87.48  ?  761 TYR   A O   1 
ATOM   4654 C CB  . TYR   A 1 639 ? -1.982  60.821  84.841  1.00 85.55  ?  761 TYR   A CB  1 
ATOM   4655 C CG  . TYR   A 1 639 ? -2.263  59.799  83.754  1.00 88.17  ?  761 TYR   A CG  1 
ATOM   4656 C CD1 . TYR   A 1 639 ? -1.443  58.694  83.556  1.00 94.20  ?  761 TYR   A CD1 1 
ATOM   4657 C CD2 . TYR   A 1 639 ? -3.431  59.892  82.984  1.00 92.93  ?  761 TYR   A CD2 1 
ATOM   4658 C CE1 . TYR   A 1 639 ? -1.768  57.714  82.579  1.00 105.57 ?  761 TYR   A CE1 1 
ATOM   4659 C CE2 . TYR   A 1 639 ? -3.759  58.932  82.011  1.00 97.29  ?  761 TYR   A CE2 1 
ATOM   4660 C CZ  . TYR   A 1 639 ? -2.928  57.854  81.815  1.00 101.65 ?  761 TYR   A CZ  1 
ATOM   4661 O OH  . TYR   A 1 639 ? -3.274  56.915  80.883  1.00 97.85  ?  761 TYR   A OH  1 
ATOM   4662 N N   . SER   A 1 640 ? 0.649   60.966  86.044  1.00 81.54  ?  762 SER   A N   1 
ATOM   4663 C CA  . SER   A 1 640 ? 2.005   60.618  86.405  1.00 83.04  ?  762 SER   A CA  1 
ATOM   4664 C C   . SER   A 1 640 ? 2.313   59.194  85.997  1.00 87.85  ?  762 SER   A C   1 
ATOM   4665 O O   . SER   A 1 640 ? 1.436   58.328  85.928  1.00 91.61  ?  762 SER   A O   1 
ATOM   4666 C CB  . SER   A 1 640 ? 2.245   60.717  87.897  1.00 89.12  ?  762 SER   A CB  1 
ATOM   4667 O OG  . SER   A 1 640 ? 1.557   59.647  88.512  1.00 92.62  ?  762 SER   A OG  1 
ATOM   4668 N N   . TYR   A 1 641 ? 3.581   58.963  85.739  1.00 86.26  ?  763 TYR   A N   1 
ATOM   4669 C CA  . TYR   A 1 641 ? 4.108   57.637  85.593  1.00 82.23  ?  763 TYR   A CA  1 
ATOM   4670 C C   . TYR   A 1 641 ? 5.245   57.497  86.579  1.00 89.11  ?  763 TYR   A C   1 
ATOM   4671 O O   . TYR   A 1 641 ? 5.667   58.466  87.221  1.00 91.49  ?  763 TYR   A O   1 
ATOM   4672 C CB  . TYR   A 1 641 ? 4.573   57.383  84.170  1.00 81.40  ?  763 TYR   A CB  1 
ATOM   4673 C CG  . TYR   A 1 641 ? 5.709   58.226  83.610  1.00 82.45  ?  763 TYR   A CG  1 
ATOM   4674 C CD1 . TYR   A 1 641 ? 7.035   57.897  83.858  1.00 84.17  ?  763 TYR   A CD1 1 
ATOM   4675 C CD2 . TYR   A 1 641 ? 5.459   59.253  82.708  1.00 85.98  ?  763 TYR   A CD2 1 
ATOM   4676 C CE1 . TYR   A 1 641 ? 8.082   58.607  83.274  1.00 84.73  ?  763 TYR   A CE1 1 
ATOM   4677 C CE2 . TYR   A 1 641 ? 6.500   59.978  82.120  1.00 88.16  ?  763 TYR   A CE2 1 
ATOM   4678 C CZ  . TYR   A 1 641 ? 7.809   59.643  82.408  1.00 89.11  ?  763 TYR   A CZ  1 
ATOM   4679 O OH  . TYR   A 1 641 ? 8.841   60.361  81.841  1.00 91.57  ?  763 TYR   A OH  1 
ATOM   4680 N N   . VAL   A 1 642 ? 5.728   56.273  86.738  1.00 88.96  ?  764 VAL   A N   1 
ATOM   4681 C CA  . VAL   A 1 642 ? 6.887   56.063  87.584  1.00 84.58  ?  764 VAL   A CA  1 
ATOM   4682 C C   . VAL   A 1 642 ? 8.079   56.106  86.641  1.00 82.91  ?  764 VAL   A C   1 
ATOM   4683 O O   . VAL   A 1 642 ? 8.290   55.198  85.848  1.00 81.17  ?  764 VAL   A O   1 
ATOM   4684 C CB  . VAL   A 1 642 ? 6.795   54.758  88.356  1.00 79.34  ?  764 VAL   A CB  1 
ATOM   4685 C CG1 . VAL   A 1 642 ? 7.700   54.833  89.578  1.00 74.84  ?  764 VAL   A CG1 1 
ATOM   4686 C CG2 . VAL   A 1 642 ? 5.318   54.440  88.653  1.00 81.12  ?  764 VAL   A CG2 1 
ATOM   4687 N N   . ALA   A 1 643 ? 8.806   57.207  86.666  1.00 84.03  ?  765 ALA   A N   1 
ATOM   4688 C CA  . ALA   A 1 643 ? 9.936   57.326  85.769  1.00 85.78  ?  765 ALA   A CA  1 
ATOM   4689 C C   . ALA   A 1 643 ? 11.051  56.409  86.232  1.00 85.04  ?  765 ALA   A C   1 
ATOM   4690 O O   . ALA   A 1 643 ? 11.154  56.083  87.411  1.00 82.11  ?  765 ALA   A O   1 
ATOM   4691 C CB  . ALA   A 1 643 ? 10.428  58.771  85.713  1.00 87.27  ?  765 ALA   A CB  1 
ATOM   4692 N N   . ALA   A 1 644 ? 11.873  55.967  85.287  1.00 89.72  ?  766 ALA   A N   1 
ATOM   4693 C CA  . ALA   A 1 644 ? 13.148  55.374  85.651  1.00 89.58  ?  766 ALA   A CA  1 
ATOM   4694 C C   . ALA   A 1 644 ? 13.889  56.331  86.577  1.00 90.83  ?  766 ALA   A C   1 
ATOM   4695 O O   . ALA   A 1 644 ? 14.028  57.524  86.277  1.00 92.27  ?  766 ALA   A O   1 
ATOM   4696 C CB  . ALA   A 1 644 ? 13.966  55.078  84.393  1.00 88.59  ?  766 ALA   A CB  1 
ATOM   4697 N N   . GLY   A 1 645 ? 14.316  55.821  87.731  1.00 85.90  ?  767 GLY   A N   1 
ATOM   4698 C CA  . GLY   A 1 645 ? 14.931  56.637  88.750  1.00 85.92  ?  767 GLY   A CA  1 
ATOM   4699 C C   . GLY   A 1 645 ? 13.988  57.072  89.859  1.00 87.88  ?  767 GLY   A C   1 
ATOM   4700 O O   . GLY   A 1 645 ? 14.438  57.282  90.988  1.00 90.89  ?  767 GLY   A O   1 
ATOM   4701 N N   . SER   A 1 646 ? 12.701  57.242  89.556  1.00 88.17  ?  768 SER   A N   1 
ATOM   4702 C CA  . SER   A 1 646 ? 11.664  57.370  90.580  1.00 86.79  ?  768 SER   A CA  1 
ATOM   4703 C C   . SER   A 1 646 ? 11.382  55.996  91.190  1.00 88.31  ?  768 SER   A C   1 
ATOM   4704 O O   . SER   A 1 646 ? 11.570  54.955  90.556  1.00 89.79  ?  768 SER   A O   1 
ATOM   4705 C CB  . SER   A 1 646 ? 10.366  57.952  89.960  1.00 89.76  ?  768 SER   A CB  1 
ATOM   4706 O OG  . SER   A 1 646 ? 9.451   58.577  90.865  1.00 80.77  ?  768 SER   A OG  1 
ATOM   4707 N N   . SER   A 1 647 ? 10.933  55.984  92.426  1.00 87.60  ?  769 SER   A N   1 
ATOM   4708 C CA  . SER   A 1 647 ? 10.288  54.790  92.930  1.00 88.13  ?  769 SER   A CA  1 
ATOM   4709 C C   . SER   A 1 647 ? 8.840   55.118  93.240  1.00 87.78  ?  769 SER   A C   1 
ATOM   4710 O O   . SER   A 1 647 ? 8.361   56.228  93.014  1.00 87.10  ?  769 SER   A O   1 
ATOM   4711 C CB  . SER   A 1 647 ? 10.989  54.237  94.172  1.00 93.92  ?  769 SER   A CB  1 
ATOM   4712 O OG  . SER   A 1 647 ? 11.175  55.247  95.132  1.00 102.83 ?  769 SER   A OG  1 
ATOM   4713 N N   . GLY   A 1 648 ? 8.125   54.138  93.769  1.00 95.77  ?  770 GLY   A N   1 
ATOM   4714 C CA  . GLY   A 1 648 ? 6.822   54.528  94.248  1.00 95.70  ?  770 GLY   A CA  1 
ATOM   4715 C C   . GLY   A 1 648 ? 6.875   55.431  95.452  1.00 91.30  ?  770 GLY   A C   1 
ATOM   4716 O O   . GLY   A 1 648 ? 5.842   55.977  95.848  1.00 90.76  ?  770 GLY   A O   1 
ATOM   4717 N N   . ASN   A 1 649 ? 8.055   55.597  96.034  1.00 89.32  ?  771 ASN   A N   1 
ATOM   4718 C CA  . ASN   A 1 649 ? 8.199   56.291  97.299  1.00 94.09  ?  771 ASN   A CA  1 
ATOM   4719 C C   . ASN   A 1 649 ? 8.327   57.813  97.122  1.00 89.27  ?  771 ASN   A C   1 
ATOM   4720 O O   . ASN   A 1 649 ? 8.005   58.568  98.050  1.00 85.71  ?  771 ASN   A O   1 
ATOM   4721 C CB  . ASN   A 1 649 ? 9.375   55.635  98.053  1.00 97.17  ?  771 ASN   A CB  1 
ATOM   4722 C CG  . ASN   A 1 649 ? 9.969   56.518  99.115  1.00 111.98 ?  771 ASN   A CG  1 
ATOM   4723 O OD1 . ASN   A 1 649 ? 10.822  57.373  98.830  1.00 115.32 ?  771 ASN   A OD1 1 
ATOM   4724 N ND2 . ASN   A 1 649 ? 9.542   56.305  100.363 1.00 109.07 ?  771 ASN   A ND2 1 
ATOM   4725 N N   . ASP   A 1 650 ? 8.719   58.281  95.934  1.00 86.62  ?  772 ASP   A N   1 
ATOM   4726 C CA  . ASP   A 1 650 ? 8.542   59.687  95.593  1.00 81.15  ?  772 ASP   A CA  1 
ATOM   4727 C C   . ASP   A 1 650 ? 7.086   60.094  95.701  1.00 81.98  ?  772 ASP   A C   1 
ATOM   4728 O O   . ASP   A 1 650 ? 6.784   61.166  96.228  1.00 87.67  ?  772 ASP   A O   1 
ATOM   4729 C CB  . ASP   A 1 650 ? 9.060   59.956  94.191  1.00 79.11  ?  772 ASP   A CB  1 
ATOM   4730 C CG  . ASP   A 1 650 ? 10.555  60.089  94.159  1.00 81.90  ?  772 ASP   A CG  1 
ATOM   4731 O OD1 . ASP   A 1 650 ? 11.168  60.146  95.246  1.00 80.42  ?  772 ASP   A OD1 1 
ATOM   4732 O OD2 . ASP   A 1 650 ? 11.121  60.072  93.052  1.00 81.32  ?  772 ASP   A OD2 1 
ATOM   4733 N N   . TYR   A 1 651 ? 6.169   59.247  95.224  1.00 83.41  ?  773 TYR   A N   1 
ATOM   4734 C CA  . TYR   A 1 651 ? 4.732   59.459  95.413  1.00 83.88  ?  773 TYR   A CA  1 
ATOM   4735 C C   . TYR   A 1 651 ? 4.370   59.723  96.870  1.00 85.28  ?  773 TYR   A C   1 
ATOM   4736 O O   . TYR   A 1 651 ? 3.350   60.365  97.147  1.00 85.88  ?  773 TYR   A O   1 
ATOM   4737 C CB  . TYR   A 1 651 ? 3.938   58.233  94.923  1.00 84.87  ?  773 TYR   A CB  1 
ATOM   4738 C CG  . TYR   A 1 651 ? 3.847   58.133  93.433  1.00 84.05  ?  773 TYR   A CG  1 
ATOM   4739 C CD1 . TYR   A 1 651 ? 4.916   57.658  92.692  1.00 88.32  ?  773 TYR   A CD1 1 
ATOM   4740 C CD2 . TYR   A 1 651 ? 2.711   58.520  92.769  1.00 83.35  ?  773 TYR   A CD2 1 
ATOM   4741 C CE1 . TYR   A 1 651 ? 4.858   57.583  91.320  1.00 92.36  ?  773 TYR   A CE1 1 
ATOM   4742 C CE2 . TYR   A 1 651 ? 2.634   58.452  91.407  1.00 89.53  ?  773 TYR   A CE2 1 
ATOM   4743 C CZ  . TYR   A 1 651 ? 3.707   57.974  90.673  1.00 95.65  ?  773 TYR   A CZ  1 
ATOM   4744 O OH  . TYR   A 1 651 ? 3.637   57.904  89.287  1.00 96.00  ?  773 TYR   A OH  1 
ATOM   4745 N N   . ASP   A 1 652 ? 5.174   59.232  97.810  1.00 82.21  ?  774 ASP   A N   1 
ATOM   4746 C CA  . ASP   A 1 652 ? 4.903   59.467  99.218  1.00 81.60  ?  774 ASP   A CA  1 
ATOM   4747 C C   . ASP   A 1 652 ? 5.514   60.777  99.715  1.00 84.52  ?  774 ASP   A C   1 
ATOM   4748 O O   . ASP   A 1 652 ? 4.884   61.489  100.505 1.00 86.89  ?  774 ASP   A O   1 
ATOM   4749 C CB  . ASP   A 1 652 ? 5.384   58.269  100.044 1.00 81.88  ?  774 ASP   A CB  1 
ATOM   4750 C CG  . ASP   A 1 652 ? 4.282   57.200  100.238 1.00 93.11  ?  774 ASP   A CG  1 
ATOM   4751 O OD1 . ASP   A 1 652 ? 3.079   57.494  99.939  1.00 89.29  ?  774 ASP   A OD1 1 
ATOM   4752 O OD2 . ASP   A 1 652 ? 4.622   56.076  100.710 1.00 88.47  ?  774 ASP   A OD2 1 
ATOM   4753 N N   . LEU   A 1 653 ? 6.725   61.124  99.274  1.00 83.40  ?  775 LEU   A N   1 
ATOM   4754 C CA  . LEU   A 1 653 ? 7.186   62.490  99.459  1.00 79.04  ?  775 LEU   A CA  1 
ATOM   4755 C C   . LEU   A 1 653 ? 6.161   63.475  98.944  1.00 82.17  ?  775 LEU   A C   1 
ATOM   4756 O O   . LEU   A 1 653 ? 5.731   64.383  99.664  1.00 87.41  ?  775 LEU   A O   1 
ATOM   4757 C CB  . LEU   A 1 653 ? 8.502   62.721  98.750  1.00 75.21  ?  775 LEU   A CB  1 
ATOM   4758 C CG  . LEU   A 1 653 ? 9.572   61.756  99.143  1.00 70.48  ?  775 LEU   A CG  1 
ATOM   4759 C CD1 . LEU   A 1 653 ? 10.656  61.792  98.101  1.00 79.13  ?  775 LEU   A CD1 1 
ATOM   4760 C CD2 . LEU   A 1 653 ? 10.045  62.293  100.393 1.00 64.75  ?  775 LEU   A CD2 1 
ATOM   4761 N N   . MET   A 1 654 ? 5.737   63.301  97.705  1.00 77.82  ?  776 MET   A N   1 
ATOM   4762 C CA  . MET   A 1 654 ? 4.754   64.205  97.127  1.00 87.17  ?  776 MET   A CA  1 
ATOM   4763 C C   . MET   A 1 654 ? 3.719   64.633  98.157  1.00 87.89  ?  776 MET   A C   1 
ATOM   4764 O O   . MET   A 1 654 ? 3.403   65.820  98.222  1.00 90.15  ?  776 MET   A O   1 
ATOM   4765 C CB  . MET   A 1 654 ? 4.305   63.711  95.748  1.00 99.66  ?  776 MET   A CB  1 
ATOM   4766 C CG  . MET   A 1 654 ? 5.286   63.937  94.585  1.00 97.78  ?  776 MET   A CG  1 
ATOM   4767 S SD  . MET   A 1 654 ? 5.894   65.601  94.575  1.00 92.39  ?  776 MET   A SD  1 
ATOM   4768 C CE  . MET   A 1 654 ? 4.316   66.430  94.437  1.00 87.63  ?  776 MET   A CE  1 
ATOM   4769 N N   . ALA   A 1 655 ? 3.177   63.716  98.962  1.00 85.06  ?  777 ALA   A N   1 
ATOM   4770 C CA  . ALA   A 1 655 ? 2.349   64.157  100.074 1.00 86.97  ?  777 ALA   A CA  1 
ATOM   4771 C C   . ALA   A 1 655 ? 2.778   64.750  101.427 1.00 91.75  ?  777 ALA   A C   1 
ATOM   4772 O O   . ALA   A 1 655 ? 1.947   65.404  102.072 1.00 92.60  ?  777 ALA   A O   1 
ATOM   4773 C CB  . ALA   A 1 655 ? 1.429   62.946  100.281 1.00 72.58  ?  777 ALA   A CB  1 
ATOM   4774 N N   . GLN   A 1 656 ? 4.056   64.589  101.864 1.00 90.58  ?  778 GLN   A N   1 
ATOM   4775 C CA  . GLN   A 1 656 ? 4.498   65.095  103.174 1.00 88.96  ?  778 GLN   A CA  1 
ATOM   4776 C C   . GLN   A 1 656 ? 4.188   66.581  103.251 1.00 87.56  ?  778 GLN   A C   1 
ATOM   4777 O O   . GLN   A 1 656 ? 4.775   67.352  102.484 1.00 90.09  ?  778 GLN   A O   1 
ATOM   4778 C CB  . GLN   A 1 656 ? 6.010   64.915  103.410 1.00 88.89  ?  778 GLN   A CB  1 
ATOM   4779 C CG  . GLN   A 1 656 ? 6.548   63.529  103.840 1.00 106.00 ?  778 GLN   A CG  1 
ATOM   4780 C CD  . GLN   A 1 656 ? 5.763   62.826  104.958 1.00 124.18 ?  778 GLN   A CD  1 
ATOM   4781 O OE1 . GLN   A 1 656 ? 5.863   63.200  106.136 1.00 125.10 ?  778 GLN   A OE1 1 
ATOM   4782 N NE2 . GLN   A 1 656 ? 4.991   61.782  104.587 1.00 124.21 ?  778 GLN   A NE2 1 
ATOM   4783 N N   . PRO   A 1 657 ? 3.289   67.030  104.125 1.00 81.68  ?  779 PRO   A N   1 
ATOM   4784 C CA  . PRO   A 1 657 ? 3.012   68.462  104.206 1.00 85.83  ?  779 PRO   A CA  1 
ATOM   4785 C C   . PRO   A 1 657 ? 4.229   69.218  104.718 1.00 86.18  ?  779 PRO   A C   1 
ATOM   4786 O O   . PRO   A 1 657 ? 5.078   68.647  105.413 1.00 82.20  ?  779 PRO   A O   1 
ATOM   4787 C CB  . PRO   A 1 657 ? 1.830   68.538  105.182 1.00 81.27  ?  779 PRO   A CB  1 
ATOM   4788 C CG  . PRO   A 1 657 ? 1.882   67.312  105.908 1.00 78.12  ?  779 PRO   A CG  1 
ATOM   4789 C CD  . PRO   A 1 657 ? 2.346   66.286  104.958 1.00 84.95  ?  779 PRO   A CD  1 
ATOM   4790 N N   . ILE   A 1 658 ? 4.285   70.535  104.361 1.00 85.53  ?  780 ILE   A N   1 
ATOM   4791 C CA  . ILE   A 1 658 ? 5.439   71.419  104.606 1.00 85.22  ?  780 ILE   A CA  1 
ATOM   4792 C C   . ILE   A 1 658 ? 5.241   72.315  105.834 1.00 87.77  ?  780 ILE   A C   1 
ATOM   4793 O O   . ILE   A 1 658 ? 4.234   73.029  105.956 1.00 81.63  ?  780 ILE   A O   1 
ATOM   4794 C CB  . ILE   A 1 658 ? 5.731   72.290  103.389 1.00 74.29  ?  780 ILE   A CB  1 
ATOM   4795 C CG1 . ILE   A 1 658 ? 5.850   71.391  102.192 1.00 79.85  ?  780 ILE   A CG1 1 
ATOM   4796 C CG2 . ILE   A 1 658 ? 7.024   73.039  103.627 1.00 76.41  ?  780 ILE   A CG2 1 
ATOM   4797 C CD1 . ILE   A 1 658 ? 7.242   71.017  101.914 1.00 82.88  ?  780 ILE   A CD1 1 
ATOM   4798 N N   . THR   A 1 659 ? 6.233   72.311  106.723 1.00 86.58  ?  781 THR   A N   1 
ATOM   4799 C CA  . THR   A 1 659 ? 6.195   73.096  107.938 1.00 85.51  ?  781 THR   A CA  1 
ATOM   4800 C C   . THR   A 1 659 ? 7.203   74.222  107.835 1.00 94.22  ?  781 THR   A C   1 
ATOM   4801 O O   . THR   A 1 659 ? 8.402   73.962  107.632 1.00 97.32  ?  781 THR   A O   1 
ATOM   4802 C CB  . THR   A 1 659 ? 6.490   72.232  109.149 1.00 91.18  ?  781 THR   A CB  1 
ATOM   4803 O OG1 . THR   A 1 659 ? 5.325   71.477  109.491 1.00 90.55  ?  781 THR   A OG1 1 
ATOM   4804 C CG2 . THR   A 1 659 ? 6.946   73.079  110.324 1.00 97.86  ?  781 THR   A CG2 1 
ATOM   4805 N N   . PRO   A 1 660 ? 6.747   75.467  107.975 1.00 93.05  ?  782 PRO   A N   1 
ATOM   4806 C CA  . PRO   A 1 660 ? 7.621   76.625  107.795 1.00 84.43  ?  782 PRO   A CA  1 
ATOM   4807 C C   . PRO   A 1 660 ? 8.474   76.852  109.028 1.00 94.54  ?  782 PRO   A C   1 
ATOM   4808 O O   . PRO   A 1 660 ? 8.119   76.441  110.133 1.00 100.91 ?  782 PRO   A O   1 
ATOM   4809 C CB  . PRO   A 1 660 ? 6.625   77.768  107.633 1.00 86.71  ?  782 PRO   A CB  1 
ATOM   4810 C CG  . PRO   A 1 660 ? 5.424   77.311  108.439 1.00 81.30  ?  782 PRO   A CG  1 
ATOM   4811 C CD  . PRO   A 1 660 ? 5.357   75.851  108.292 1.00 89.25  ?  782 PRO   A CD  1 
ATOM   4812 N N   . GLY   A 1 661 ? 9.587   77.564  108.839 1.00 98.25  ?  783 GLY   A N   1 
ATOM   4813 C CA  . GLY   A 1 661 ? 10.429  77.965  109.957 1.00 110.81 ?  783 GLY   A CA  1 
ATOM   4814 C C   . GLY   A 1 661 ? 9.742   78.854  110.996 1.00 114.10 ?  783 GLY   A C   1 
ATOM   4815 O O   . GLY   A 1 661 ? 8.683   79.449  110.747 1.00 116.38 ?  783 GLY   A O   1 
ATOM   4816 N N   . PRO   A 1 662 ? 10.338  78.990  112.177 1.00 108.94 ?  784 PRO   A N   1 
ATOM   4817 C CA  . PRO   A 1 662 ? 9.687   79.796  113.205 1.00 111.15 ?  784 PRO   A CA  1 
ATOM   4818 C C   . PRO   A 1 662 ? 9.826   81.265  112.829 1.00 125.21 ?  784 PRO   A C   1 
ATOM   4819 O O   . PRO   A 1 662 ? 10.832  81.680  112.242 1.00 124.44 ?  784 PRO   A O   1 
ATOM   4820 C CB  . PRO   A 1 662 ? 10.468  79.455  114.479 1.00 111.53 ?  784 PRO   A CB  1 
ATOM   4821 C CG  . PRO   A 1 662 ? 11.846  79.094  113.982 1.00 115.26 ?  784 PRO   A CG  1 
ATOM   4822 C CD  . PRO   A 1 662 ? 11.763  78.784  112.481 1.00 112.07 ?  784 PRO   A CD  1 
ATOM   4823 N N   . SER   A 1 663 ? 8.785   82.048  113.125 1.00 128.53 ?  785 SER   A N   1 
ATOM   4824 C CA  . SER   A 1 663 ? 8.898   83.495  112.973 1.00 121.59 ?  785 SER   A CA  1 
ATOM   4825 C C   . SER   A 1 663 ? 9.995   84.003  113.899 1.00 125.75 ?  785 SER   A C   1 
ATOM   4826 O O   . SER   A 1 663 ? 11.158  84.134  113.491 1.00 122.67 ?  785 SER   A O   1 
ATOM   4827 C CB  . SER   A 1 663 ? 7.566   84.204  113.273 1.00 121.39 ?  785 SER   A CB  1 
ATOM   4828 O OG  . SER   A 1 663 ? 6.645   84.129  112.190 1.00 115.16 ?  785 SER   A OG  1 
ATOM   4829 N N   . ILE   A 1 664 ? 9.629   84.245  115.156 1.00 128.38 ?  786 ILE   A N   1 
ATOM   4830 C CA  . ILE   A 1 664 ? 10.501  84.852  116.159 1.00 127.52 ?  786 ILE   A CA  1 
ATOM   4831 C C   . ILE   A 1 664 ? 11.550  83.783  116.449 1.00 131.34 ?  786 ILE   A C   1 
ATOM   4832 O O   . ILE   A 1 664 ? 11.170  82.743  117.005 1.00 136.87 ?  786 ILE   A O   1 
ATOM   4833 C CB  . ILE   A 1 664 ? 9.720   85.183  117.442 1.00 128.68 ?  786 ILE   A CB  1 
ATOM   4834 C CG1 . ILE   A 1 664 ? 8.380   85.865  117.130 1.00 122.26 ?  786 ILE   A CG1 1 
ATOM   4835 C CG2 . ILE   A 1 664 ? 10.553  86.125  118.304 1.00 125.55 ?  786 ILE   A CG2 1 
ATOM   4836 C CD1 . ILE   A 1 664 ? 7.167   84.900  117.301 1.00 109.44 ?  786 ILE   A CD1 1 
ATOM   4837 N N   . PRO   A 1 665 ? 12.841  83.956  116.128 1.00 130.11 ?  787 PRO   A N   1 
ATOM   4838 C CA  . PRO   A 1 665 ? 13.752  82.794  116.137 1.00 132.93 ?  787 PRO   A CA  1 
ATOM   4839 C C   . PRO   A 1 665 ? 13.841  82.155  117.524 1.00 135.08 ?  787 PRO   A C   1 
ATOM   4840 O O   . PRO   A 1 665 ? 13.930  82.849  118.542 1.00 128.80 ?  787 PRO   A O   1 
ATOM   4841 C CB  . PRO   A 1 665 ? 15.096  83.384  115.687 1.00 121.84 ?  787 PRO   A CB  1 
ATOM   4842 C CG  . PRO   A 1 665 ? 15.039  84.781  116.103 1.00 128.72 ?  787 PRO   A CG  1 
ATOM   4843 C CD  . PRO   A 1 665 ? 13.581  85.223  116.054 1.00 130.28 ?  787 PRO   A CD  1 
ATOM   4844 N N   . GLY   A 1 666 ? 13.789  80.820  117.552 1.00 130.83 ?  788 GLY   A N   1 
ATOM   4845 C CA  . GLY   A 1 666 ? 13.622  80.084  118.797 1.00 120.97 ?  788 GLY   A CA  1 
ATOM   4846 C C   . GLY   A 1 666 ? 12.211  80.149  119.346 1.00 118.85 ?  788 GLY   A C   1 
ATOM   4847 O O   . GLY   A 1 666 ? 12.020  80.361  120.551 1.00 113.71 ?  788 GLY   A O   1 
ATOM   4848 N N   . ALA   A 1 667 ? 11.223  80.018  118.487 1.00 118.71 ?  789 ALA   A N   1 
ATOM   4849 C CA  . ALA   A 1 667 ? 9.831   79.882  118.864 1.00 115.36 ?  789 ALA   A CA  1 
ATOM   4850 C C   . ALA   A 1 667 ? 9.469   78.411  118.883 1.00 118.49 ?  789 ALA   A C   1 
ATOM   4851 O O   . ALA   A 1 667 ? 10.229  77.570  118.395 1.00 121.93 ?  789 ALA   A O   1 
ATOM   4852 C CB  . ALA   A 1 667 ? 8.946   80.644  117.873 1.00 117.00 ?  789 ALA   A CB  1 
ATOM   4853 N N   . PRO   A 1 668 ? 8.320   78.046  119.451 1.00 115.84 ?  790 PRO   A N   1 
ATOM   4854 C CA  . PRO   A 1 668 ? 7.852   76.666  119.289 1.00 111.11 ?  790 PRO   A CA  1 
ATOM   4855 C C   . PRO   A 1 668 ? 7.687   76.315  117.810 1.00 117.30 ?  790 PRO   A C   1 
ATOM   4856 O O   . PRO   A 1 668 ? 7.115   77.087  117.029 1.00 118.22 ?  790 PRO   A O   1 
ATOM   4857 C CB  . PRO   A 1 668 ? 6.513   76.664  120.037 1.00 107.62 ?  790 PRO   A CB  1 
ATOM   4858 C CG  . PRO   A 1 668 ? 6.055   78.089  119.991 1.00 114.70 ?  790 PRO   A CG  1 
ATOM   4859 C CD  . PRO   A 1 668 ? 7.344   78.844  120.216 1.00 116.49 ?  790 PRO   A CD  1 
ATOM   4860 N N   . GLN   A 1 669 ? 8.255   75.149  117.422 1.00 117.66 ?  791 GLN   A N   1 
ATOM   4861 C CA  . GLN   A 1 669 ? 8.079   74.492  116.124 1.00 118.57 ?  791 GLN   A CA  1 
ATOM   4862 C C   . GLN   A 1 669 ? 6.634   74.578  115.659 1.00 116.93 ?  791 GLN   A C   1 
ATOM   4863 O O   . GLN   A 1 669 ? 5.726   74.053  116.327 1.00 112.14 ?  791 GLN   A O   1 
ATOM   4864 C CB  . GLN   A 1 669 ? 8.485   73.017  116.187 1.00 115.80 ?  791 GLN   A CB  1 
ATOM   4865 C CG  . GLN   A 1 669 ? 8.096   72.245  114.934 1.00 118.52 ?  791 GLN   A CG  1 
ATOM   4866 C CD  . GLN   A 1 669 ? 9.283   71.877  114.077 1.00 129.33 ?  791 GLN   A CD  1 
ATOM   4867 O OE1 . GLN   A 1 669 ? 10.236  72.651  113.978 1.00 132.31 ?  791 GLN   A OE1 1 
ATOM   4868 N NE2 . GLN   A 1 669 ? 9.228   70.698  113.431 1.00 128.52 ?  791 GLN   A NE2 1 
ATOM   4869 N N   . PRO   A 1 670 ? 6.376   75.214  114.523 1.00 113.66 ?  792 PRO   A N   1 
ATOM   4870 C CA  . PRO   A 1 670 ? 4.989   75.500  114.160 1.00 114.24 ?  792 PRO   A CA  1 
ATOM   4871 C C   . PRO   A 1 670 ? 4.301   74.278  113.571 1.00 110.78 ?  792 PRO   A C   1 
ATOM   4872 O O   . PRO   A 1 670 ? 4.928   73.388  112.991 1.00 105.17 ?  792 PRO   A O   1 
ATOM   4873 C CB  . PRO   A 1 670 ? 5.105   76.636  113.127 1.00 99.15  ?  792 PRO   A CB  1 
ATOM   4874 C CG  . PRO   A 1 670 ? 6.601   76.949  113.024 1.00 102.05 ?  792 PRO   A CG  1 
ATOM   4875 C CD  . PRO   A 1 670 ? 7.328   75.746  113.538 1.00 106.40 ?  792 PRO   A CD  1 
ATOM   4876 N N   . ILE   A 1 671 ? 3.000   74.220  113.821 1.00 108.02 ?  793 ILE   A N   1 
ATOM   4877 C CA  . ILE   A 1 671 ? 1.984   73.664  112.934 1.00 103.82 ?  793 ILE   A CA  1 
ATOM   4878 C C   . ILE   A 1 671 ? 2.003   73.892  111.415 1.00 102.46 ?  793 ILE   A C   1 
ATOM   4879 O O   . ILE   A 1 671 ? 1.695   74.999  110.950 1.00 102.66 ?  793 ILE   A O   1 
ATOM   4880 C CB  . ILE   A 1 671 ? 0.706   74.532  113.036 1.00 108.62 ?  793 ILE   A CB  1 
ATOM   4881 C CG1 . ILE   A 1 671 ? 0.249   74.737  114.506 1.00 114.47 ?  793 ILE   A CG1 1 
ATOM   4882 C CG2 . ILE   A 1 671 ? -0.435  74.006  112.152 1.00 101.82 ?  793 ILE   A CG2 1 
ATOM   4883 C CD1 . ILE   A 1 671 ? 0.784   76.023  115.220 1.00 119.32 ?  793 ILE   A CD1 1 
ATOM   4884 N N   . PRO   A 1 672 ? 1.833   72.882  110.574 1.00 102.99 ?  794 PRO   A N   1 
ATOM   4885 C CA  . PRO   A 1 672 ? 2.444   72.552  109.280 1.00 97.87  ?  794 PRO   A CA  1 
ATOM   4886 C C   . PRO   A 1 672 ? 1.364   73.300  108.506 1.00 95.11  ?  794 PRO   A C   1 
ATOM   4887 O O   . PRO   A 1 672 ? 0.164   73.123  108.749 1.00 94.87  ?  794 PRO   A O   1 
ATOM   4888 C CB  . PRO   A 1 672 ? 2.440   71.059  108.915 1.00 90.45  ?  794 PRO   A CB  1 
ATOM   4889 C CG  . PRO   A 1 672 ? 2.286   70.326  110.232 1.00 87.63  ?  794 PRO   A CG  1 
ATOM   4890 C CD  . PRO   A 1 672 ? 1.539   71.258  111.079 1.00 96.12  ?  794 PRO   A CD  1 
ATOM   4891 N N   . ARG   A 1 673 ? 1.790   74.114  107.535 1.00 85.54  ?  795 ARG   A N   1 
ATOM   4892 C CA  . ARG   A 1 673 ? 0.862   75.038  106.885 1.00 86.09  ?  795 ARG   A CA  1 
ATOM   4893 C C   . ARG   A 1 673 ? 0.492   74.686  105.442 1.00 81.63  ?  795 ARG   A C   1 
ATOM   4894 O O   . ARG   A 1 673 ? -0.595  75.062  104.998 1.00 78.29  ?  795 ARG   A O   1 
ATOM   4895 C CB  . ARG   A 1 673 ? 1.425   76.474  106.920 1.00 87.74  ?  795 ARG   A CB  1 
ATOM   4896 C CG  . ARG   A 1 673 ? 1.668   77.067  108.324 1.00 88.19  ?  795 ARG   A CG  1 
ATOM   4897 C CD  . ARG   A 1 673 ? 0.362   77.512  108.942 1.00 87.96  ?  795 ARG   A CD  1 
ATOM   4898 N NE  . ARG   A 1 673 ? 0.522   78.097  110.265 1.00 88.76  ?  795 ARG   A NE  1 
ATOM   4899 C CZ  . ARG   A 1 673 ? -0.487  78.425  111.061 1.00 94.84  ?  795 ARG   A CZ  1 
ATOM   4900 N NH1 . ARG   A 1 673 ? -1.749  78.151  110.744 1.00 88.70  ?  795 ARG   A NH1 1 
ATOM   4901 N NH2 . ARG   A 1 673 ? -0.228  79.058  112.198 1.00 106.49 ?  795 ARG   A NH2 1 
ATOM   4902 N N   . LEU   A 1 674 ? 1.352   73.980  104.701 1.00 82.88  ?  796 LEU   A N   1 
ATOM   4903 C CA  . LEU   A 1 674 ? 1.179   73.690  103.273 1.00 79.83  ?  796 LEU   A CA  1 
ATOM   4904 C C   . LEU   A 1 674 ? 0.986   72.192  103.071 1.00 81.88  ?  796 LEU   A C   1 
ATOM   4905 O O   . LEU   A 1 674 ? 1.848   71.403  103.472 1.00 80.25  ?  796 LEU   A O   1 
ATOM   4906 C CB  . LEU   A 1 674 ? 2.402   74.141  102.474 1.00 80.10  ?  796 LEU   A CB  1 
ATOM   4907 C CG  . LEU   A 1 674 ? 2.342   74.151  100.952 1.00 75.31  ?  796 LEU   A CG  1 
ATOM   4908 C CD1 . LEU   A 1 674 ? 1.062   74.837  100.492 1.00 75.48  ?  796 LEU   A CD1 1 
ATOM   4909 C CD2 . LEU   A 1 674 ? 3.602   74.767  100.364 1.00 67.78  ?  796 LEU   A CD2 1 
ATOM   4910 N N   . PHE   A 1 675 ? -0.106  71.814  102.396 1.00 82.08  ?  797 PHE   A N   1 
ATOM   4911 C CA  . PHE   A 1 675 ? -0.534  70.428  102.223 1.00 80.00  ?  797 PHE   A CA  1 
ATOM   4912 C C   . PHE   A 1 675 ? -0.657  70.048  100.744 1.00 83.36  ?  797 PHE   A C   1 
ATOM   4913 O O   . PHE   A 1 675 ? -0.862  70.899  99.869  1.00 85.17  ?  797 PHE   A O   1 
ATOM   4914 C CB  . PHE   A 1 675 ? -1.870  70.203  102.921 1.00 78.76  ?  797 PHE   A CB  1 
ATOM   4915 C CG  . PHE   A 1 675 ? -1.812  70.396  104.412 1.00 83.42  ?  797 PHE   A CG  1 
ATOM   4916 C CD1 . PHE   A 1 675 ? -1.793  71.650  104.964 1.00 86.29  ?  797 PHE   A CD1 1 
ATOM   4917 C CD2 . PHE   A 1 675 ? -1.764  69.318  105.261 1.00 82.75  ?  797 PHE   A CD2 1 
ATOM   4918 C CE1 . PHE   A 1 675 ? -1.739  71.817  106.336 1.00 87.21  ?  797 PHE   A CE1 1 
ATOM   4919 C CE2 . PHE   A 1 675 ? -1.718  69.491  106.606 1.00 81.50  ?  797 PHE   A CE2 1 
ATOM   4920 C CZ  . PHE   A 1 675 ? -1.699  70.738  107.146 1.00 85.09  ?  797 PHE   A CZ  1 
ATOM   4921 N N   . PHE   A 1 676 ? -0.545  68.748  100.455 1.00 80.86  ?  798 PHE   A N   1 
ATOM   4922 C CA  . PHE   A 1 676 ? -0.573  68.278  99.071  1.00 78.02  ?  798 PHE   A CA  1 
ATOM   4923 C C   . PHE   A 1 676 ? -1.528  67.122  98.851  1.00 78.29  ?  798 PHE   A C   1 
ATOM   4924 O O   . PHE   A 1 676 ? -1.495  66.136  99.584  1.00 84.12  ?  798 PHE   A O   1 
ATOM   4925 C CB  . PHE   A 1 676 ? 0.802   67.856  98.602  1.00 74.44  ?  798 PHE   A CB  1 
ATOM   4926 C CG  . PHE   A 1 676 ? 1.778   68.944  98.644  1.00 77.23  ?  798 PHE   A CG  1 
ATOM   4927 C CD1 . PHE   A 1 676 ? 1.701   69.965  97.719  1.00 75.95  ?  798 PHE   A CD1 1 
ATOM   4928 C CD2 . PHE   A 1 676 ? 2.780   68.962  99.576  1.00 80.45  ?  798 PHE   A CD2 1 
ATOM   4929 C CE1 . PHE   A 1 676 ? 2.599   70.985  97.736  1.00 75.59  ?  798 PHE   A CE1 1 
ATOM   4930 C CE2 . PHE   A 1 676 ? 3.677   70.009  99.600  1.00 78.96  ?  798 PHE   A CE2 1 
ATOM   4931 C CZ  . PHE   A 1 676 ? 3.599   71.001  98.675  1.00 74.66  ?  798 PHE   A CZ  1 
ATOM   4932 N N   . ALA   A 1 677 ? -2.351  67.237  97.819  1.00 80.91  ?  799 ALA   A N   1 
ATOM   4933 C CA  . ALA   A 1 677 ? -3.150  66.123  97.334  1.00 81.89  ?  799 ALA   A CA  1 
ATOM   4934 C C   . ALA   A 1 677 ? -3.270  66.254  95.823  1.00 84.62  ?  799 ALA   A C   1 
ATOM   4935 O O   . ALA   A 1 677 ? -2.726  67.180  95.212  1.00 87.19  ?  799 ALA   A O   1 
ATOM   4936 C CB  . ALA   A 1 677 ? -4.524  66.060  98.006  1.00 81.90  ?  799 ALA   A CB  1 
ATOM   4937 N N   . GLY   A 1 678 ? -3.988  65.309  95.219  1.00 86.78  ?  800 GLY   A N   1 
ATOM   4938 C CA  . GLY   A 1 678 ? -3.927  65.114  93.780  1.00 87.64  ?  800 GLY   A CA  1 
ATOM   4939 C C   . GLY   A 1 678 ? -3.427  63.734  93.368  1.00 89.41  ?  800 GLY   A C   1 
ATOM   4940 O O   . GLY   A 1 678 ? -2.717  63.056  94.123  1.00 88.79  ?  800 GLY   A O   1 
ATOM   4941 N N   . GLU   A 1 679 ? -3.843  63.299  92.177  1.00 88.59  ?  801 GLU   A N   1 
ATOM   4942 C CA  . GLU   A 1 679 ? -3.359  62.118  91.465  1.00 79.10  ?  801 GLU   A CA  1 
ATOM   4943 C C   . GLU   A 1 679 ? -1.894  61.768  91.741  1.00 76.22  ?  801 GLU   A C   1 
ATOM   4944 O O   . GLU   A 1 679 ? -1.584  60.651  92.136  1.00 76.25  ?  801 GLU   A O   1 
ATOM   4945 C CB  . GLU   A 1 679 ? -3.613  62.365  89.973  1.00 81.26  ?  801 GLU   A CB  1 
ATOM   4946 C CG  . GLU   A 1 679 ? -3.014  61.426  89.063  1.00 85.41  ?  801 GLU   A CG  1 
ATOM   4947 C CD  . GLU   A 1 679 ? -1.686  61.907  88.551  1.00 83.75  ?  801 GLU   A CD  1 
ATOM   4948 O OE1 . GLU   A 1 679 ? -1.549  63.102  88.231  1.00 81.70  ?  801 GLU   A OE1 1 
ATOM   4949 O OE2 . GLU   A 1 679 ? -0.756  61.085  88.530  1.00 94.68  ?  801 GLU   A OE2 1 
ATOM   4950 N N   . HIS   A 1 680 ? -0.999  62.681  91.558  1.00 80.17  ?  802 HIS   A N   1 
ATOM   4951 C CA  . HIS   A 1 680 ? 0.415   62.415  91.811  1.00 83.55  ?  802 HIS   A CA  1 
ATOM   4952 C C   . HIS   A 1 680 ? 0.644   62.020  93.291  1.00 85.17  ?  802 HIS   A C   1 
ATOM   4953 O O   . HIS   A 1 680 ? 1.661   61.337  93.495  1.00 86.13  ?  802 HIS   A O   1 
ATOM   4954 C CB  . HIS   A 1 680 ? 1.271   63.572  91.283  1.00 87.80  ?  802 HIS   A CB  1 
ATOM   4955 C CG  . HIS   A 1 680 ? 0.808   64.908  91.767  1.00 88.65  ?  802 HIS   A CG  1 
ATOM   4956 N ND1 . HIS   A 1 680 ? -0.368  65.492  91.329  1.00 91.08  ?  802 HIS   A ND1 1 
ATOM   4957 C CD2 . HIS   A 1 680 ? 1.321   65.740  92.705  1.00 82.59  ?  802 HIS   A CD2 1 
ATOM   4958 C CE1 . HIS   A 1 680 ? -0.552  66.631  91.971  1.00 92.00  ?  802 HIS   A CE1 1 
ATOM   4959 N NE2 . HIS   A 1 680 ? 0.461   66.808  92.807  1.00 90.86  ?  802 HIS   A NE2 1 
ATOM   4960 N N   . THR   A 1 681 ? -0.154  62.380  94.304  1.00 80.79  ?  803 THR   A N   1 
ATOM   4961 C CA  . THR   A 1 681 ? 0.208   62.136  95.701  1.00 83.28  ?  803 THR   A CA  1 
ATOM   4962 C C   . THR   A 1 681 ? -0.086  60.825  96.426  1.00 88.39  ?  803 THR   A C   1 
ATOM   4963 O O   . THR   A 1 681 ? 0.192   60.720  97.633  1.00 92.47  ?  803 THR   A O   1 
ATOM   4964 C CB  . THR   A 1 681 ? -0.506  63.269  96.456  1.00 82.41  ?  803 THR   A CB  1 
ATOM   4965 O OG1 . THR   A 1 681 ? -1.919  63.009  96.520  1.00 76.80  ?  803 THR   A OG1 1 
ATOM   4966 C CG2 . THR   A 1 681 ? -0.274  64.576  95.745  1.00 82.72  ?  803 THR   A CG2 1 
ATOM   4967 N N   . ILE   A 1 682 ? -0.623  59.824  95.741  1.00 79.36  ?  804 ILE   A N   1 
ATOM   4968 C CA  . ILE   A 1 682 ? -1.180  58.651  96.383  1.00 73.39  ?  804 ILE   A CA  1 
ATOM   4969 C C   . ILE   A 1 682 ? -0.462  57.437  95.786  1.00 84.23  ?  804 ILE   A C   1 
ATOM   4970 O O   . ILE   A 1 682 ? -0.823  56.948  94.707  1.00 86.86  ?  804 ILE   A O   1 
ATOM   4971 C CB  . ILE   A 1 682 ? -2.711  58.623  96.226  1.00 66.97  ?  804 ILE   A CB  1 
ATOM   4972 C CG1 . ILE   A 1 682 ? -3.356  57.480  96.955  1.00 74.88  ?  804 ILE   A CG1 1 
ATOM   4973 C CG2 . ILE   A 1 682 ? -3.186  58.731  94.822  1.00 68.66  ?  804 ILE   A CG2 1 
ATOM   4974 C CD1 . ILE   A 1 682 ? -4.768  57.793  97.295  1.00 73.32  ?  804 ILE   A CD1 1 
ATOM   4975 N N   . ARG   A 1 683 ? 0.607   56.983  96.470  1.00 88.12  ?  805 ARG   A N   1 
ATOM   4976 C CA  . ARG   A 1 683 ? 1.432   55.832  96.059  1.00 88.32  ?  805 ARG   A CA  1 
ATOM   4977 C C   . ARG   A 1 683 ? 0.666   54.674  95.433  1.00 90.39  ?  805 ARG   A C   1 
ATOM   4978 O O   . ARG   A 1 683 ? 1.056   54.135  94.392  1.00 90.50  ?  805 ARG   A O   1 
ATOM   4979 C CB  . ARG   A 1 683 ? 2.186   55.293  97.275  1.00 86.06  ?  805 ARG   A CB  1 
ATOM   4980 C CG  . ARG   A 1 683 ? 3.378   54.420  96.982  1.00 82.85  ?  805 ARG   A CG  1 
ATOM   4981 C CD  . ARG   A 1 683 ? 3.824   53.732  98.253  1.00 84.46  ?  805 ARG   A CD  1 
ATOM   4982 N NE  . ARG   A 1 683 ? 4.990   52.876  98.068  1.00 94.61  ?  805 ARG   A NE  1 
ATOM   4983 C CZ  . ARG   A 1 683 ? 6.214   53.176  98.497  1.00 97.28  ?  805 ARG   A CZ  1 
ATOM   4984 N NH1 . ARG   A 1 683 ? 6.472   54.318  99.109  1.00 91.14  ?  805 ARG   A NH1 1 
ATOM   4985 N NH2 . ARG   A 1 683 ? 7.206   52.304  98.310  1.00 102.92 ?  805 ARG   A NH2 1 
ATOM   4986 N N   . ASN   A 1 684 ? -0.405  54.251  96.080  1.00 90.42  ?  806 ASN   A N   1 
ATOM   4987 C CA  . ASN   A 1 684 ? -1.062  53.021  95.696  1.00 87.70  ?  806 ASN   A CA  1 
ATOM   4988 C C   . ASN   A 1 684 ? -2.193  53.215  94.714  1.00 84.77  ?  806 ASN   A C   1 
ATOM   4989 O O   . ASN   A 1 684 ? -2.857  52.231  94.383  1.00 89.81  ?  806 ASN   A O   1 
ATOM   4990 C CB  . ASN   A 1 684 ? -1.562  52.313  96.941  1.00 86.45  ?  806 ASN   A CB  1 
ATOM   4991 C CG  . ASN   A 1 684 ? -0.421  51.812  97.766  1.00 93.16  ?  806 ASN   A CG  1 
ATOM   4992 O OD1 . ASN   A 1 684 ? 0.752   52.057  97.428  1.00 91.54  ?  806 ASN   A OD1 1 
ATOM   4993 N ND2 . ASN   A 1 684 ? -0.731  51.119  98.855  1.00 99.48  ?  806 ASN   A ND2 1 
ATOM   4994 N N   . TYR   A 1 685 ? -2.470  54.445  94.279  1.00 80.05  ?  807 TYR   A N   1 
ATOM   4995 C CA  . TYR   A 1 685 ? -3.499  54.627  93.260  1.00 83.78  ?  807 TYR   A CA  1 
ATOM   4996 C C   . TYR   A 1 685 ? -3.190  55.758  92.289  1.00 80.63  ?  807 TYR   A C   1 
ATOM   4997 O O   . TYR   A 1 685 ? -4.116  56.482  91.909  1.00 78.19  ?  807 TYR   A O   1 
ATOM   4998 C CB  . TYR   A 1 685 ? -4.877  54.858  93.904  1.00 78.50  ?  807 TYR   A CB  1 
ATOM   4999 C CG  . TYR   A 1 685 ? -5.347  53.703  94.798  1.00 86.89  ?  807 TYR   A CG  1 
ATOM   5000 C CD1 . TYR   A 1 685 ? -4.776  53.478  96.061  1.00 86.94  ?  807 TYR   A CD1 1 
ATOM   5001 C CD2 . TYR   A 1 685 ? -6.361  52.853  94.399  1.00 91.11  ?  807 TYR   A CD2 1 
ATOM   5002 C CE1 . TYR   A 1 685 ? -5.157  52.430  96.871  1.00 85.68  ?  807 TYR   A CE1 1 
ATOM   5003 C CE2 . TYR   A 1 685 ? -6.770  51.795  95.232  1.00 97.57  ?  807 TYR   A CE2 1 
ATOM   5004 C CZ  . TYR   A 1 685 ? -6.167  51.604  96.473  1.00 93.05  ?  807 TYR   A CZ  1 
ATOM   5005 O OH  . TYR   A 1 685 ? -6.559  50.581  97.317  1.00 95.83  ?  807 TYR   A OH  1 
ATOM   5006 N N   . PRO   A 1 686 ? -1.948  55.908  91.807  1.00 81.73  ?  808 PRO   A N   1 
ATOM   5007 C CA  . PRO   A 1 686 ? -1.640  57.048  90.938  1.00 76.93  ?  808 PRO   A CA  1 
ATOM   5008 C C   . PRO   A 1 686 ? -2.485  57.085  89.682  1.00 75.41  ?  808 PRO   A C   1 
ATOM   5009 O O   . PRO   A 1 686 ? -3.165  56.130  89.315  1.00 82.55  ?  808 PRO   A O   1 
ATOM   5010 C CB  . PRO   A 1 686 ? -0.163  56.848  90.587  1.00 78.23  ?  808 PRO   A CB  1 
ATOM   5011 C CG  . PRO   A 1 686 ? 0.161   55.490  90.947  1.00 83.07  ?  808 PRO   A CG  1 
ATOM   5012 C CD  . PRO   A 1 686 ? -0.751  55.081  92.035  1.00 82.02  ?  808 PRO   A CD  1 
ATOM   5013 N N   . ALA   A 1 687 ? -2.442  58.235  89.039  1.00 72.35  ?  809 ALA   A N   1 
ATOM   5014 C CA  . ALA   A 1 687 ? -2.959  58.431  87.697  1.00 80.69  ?  809 ALA   A CA  1 
ATOM   5015 C C   . ALA   A 1 687 ? -4.403  57.970  87.529  1.00 82.35  ?  809 ALA   A C   1 
ATOM   5016 O O   . ALA   A 1 687 ? -4.786  57.513  86.463  1.00 94.90  ?  809 ALA   A O   1 
ATOM   5017 C CB  . ALA   A 1 687 ? -2.055  57.751  86.676  1.00 88.98  ?  809 ALA   A CB  1 
ATOM   5018 N N   . THR   A 1 688 ? -5.241  58.098  88.546  1.00 81.45  ?  810 THR   A N   1 
ATOM   5019 C CA  . THR   A 1 688 ? -6.634  57.689  88.414  1.00 85.03  ?  810 THR   A CA  1 
ATOM   5020 C C   . THR   A 1 688 ? -7.535  58.664  89.154  1.00 87.17  ?  810 THR   A C   1 
ATOM   5021 O O   . THR   A 1 688 ? -7.089  59.403  90.030  1.00 90.83  ?  810 THR   A O   1 
ATOM   5022 C CB  . THR   A 1 688 ? -6.877  56.298  88.992  1.00 85.03  ?  810 THR   A CB  1 
ATOM   5023 O OG1 . THR   A 1 688 ? -6.339  56.248  90.321  1.00 85.56  ?  810 THR   A OG1 1 
ATOM   5024 C CG2 . THR   A 1 688 ? -6.180  55.242  88.135  1.00 92.23  ?  810 THR   A CG2 1 
ATOM   5025 N N   . VAL   A 1 689 ? -8.823  58.649  88.820  1.00 87.46  ?  811 VAL   A N   1 
ATOM   5026 C CA  . VAL   A 1 689 ? -9.771  59.500  89.537  1.00 82.19  ?  811 VAL   A CA  1 
ATOM   5027 C C   . VAL   A 1 689 ? -9.988  59.003  90.962  1.00 78.56  ?  811 VAL   A C   1 
ATOM   5028 O O   . VAL   A 1 689 ? -9.802  59.751  91.923  1.00 83.38  ?  811 VAL   A O   1 
ATOM   5029 C CB  . VAL   A 1 689 ? -11.087 59.628  88.757  1.00 76.43  ?  811 VAL   A CB  1 
ATOM   5030 C CG1 . VAL   A 1 689 ? -12.217 59.904  89.685  1.00 69.52  ?  811 VAL   A CG1 1 
ATOM   5031 C CG2 . VAL   A 1 689 ? -10.945 60.766  87.797  1.00 74.28  ?  811 VAL   A CG2 1 
ATOM   5032 N N   . HIS   A 1 690 ? -10.374 57.748  91.133  1.00 75.06  ?  812 HIS   A N   1 
ATOM   5033 C CA  . HIS   A 1 690 ? -10.497 57.215  92.483  1.00 80.90  ?  812 HIS   A CA  1 
ATOM   5034 C C   . HIS   A 1 690 ? -9.258  57.516  93.321  1.00 82.61  ?  812 HIS   A C   1 
ATOM   5035 O O   . HIS   A 1 690 ? -9.358  57.694  94.539  1.00 81.33  ?  812 HIS   A O   1 
ATOM   5036 C CB  . HIS   A 1 690 ? -10.773 55.694  92.438  1.00 94.01  ?  812 HIS   A CB  1 
ATOM   5037 C CG  . HIS   A 1 690 ? -9.782  54.891  91.623  1.00 92.68  ?  812 HIS   A CG  1 
ATOM   5038 N ND1 . HIS   A 1 690 ? -8.584  54.424  92.138  1.00 87.65  ?  812 HIS   A ND1 1 
ATOM   5039 C CD2 . HIS   A 1 690 ? -9.828  54.469  90.335  1.00 83.13  ?  812 HIS   A CD2 1 
ATOM   5040 C CE1 . HIS   A 1 690 ? -7.932  53.764  91.200  1.00 86.60  ?  812 HIS   A CE1 1 
ATOM   5041 N NE2 . HIS   A 1 690 ? -8.664  53.781  90.098  1.00 90.54  ?  812 HIS   A NE2 1 
ATOM   5042 N N   . GLY   A 1 691 ? -8.091  57.611  92.692  1.00 82.82  ?  813 GLY   A N   1 
ATOM   5043 C CA  . GLY   A 1 691 ? -6.874  57.849  93.440  1.00 82.99  ?  813 GLY   A CA  1 
ATOM   5044 C C   . GLY   A 1 691 ? -6.743  59.276  93.936  1.00 79.31  ?  813 GLY   A C   1 
ATOM   5045 O O   . GLY   A 1 691 ? -6.336  59.500  95.078  1.00 75.04  ?  813 GLY   A O   1 
ATOM   5046 N N   . ALA   A 1 692 ? -7.042  60.244  93.060  1.00 82.60  ?  814 ALA   A N   1 
ATOM   5047 C CA  . ALA   A 1 692 ? -7.103  61.648  93.463  1.00 83.07  ?  814 ALA   A CA  1 
ATOM   5048 C C   . ALA   A 1 692 ? -8.118  61.839  94.584  1.00 82.28  ?  814 ALA   A C   1 
ATOM   5049 O O   . ALA   A 1 692 ? -7.766  62.237  95.704  1.00 79.13  ?  814 ALA   A O   1 
ATOM   5050 C CB  . ALA   A 1 692 ? -7.452  62.528  92.254  1.00 78.88  ?  814 ALA   A CB  1 
ATOM   5051 N N   . LEU   A 1 693 ? -9.392  61.557  94.286  1.00 81.04  ?  815 LEU   A N   1 
ATOM   5052 C CA  . LEU   A 1 693 ? -10.479 61.467  95.258  1.00 83.45  ?  815 LEU   A CA  1 
ATOM   5053 C C   . LEU   A 1 693 ? -10.008 60.919  96.599  1.00 79.24  ?  815 LEU   A C   1 
ATOM   5054 O O   . LEU   A 1 693 ? -10.345 61.458  97.655  1.00 81.15  ?  815 LEU   A O   1 
ATOM   5055 C CB  . LEU   A 1 693 ? -11.601 60.571  94.712  1.00 85.18  ?  815 LEU   A CB  1 
ATOM   5056 C CG  . LEU   A 1 693 ? -12.973 60.261  95.360  1.00 75.22  ?  815 LEU   A CG  1 
ATOM   5057 C CD1 . LEU   A 1 693 ? -12.953 59.426  96.626  1.00 71.20  ?  815 LEU   A CD1 1 
ATOM   5058 C CD2 . LEU   A 1 693 ? -13.671 61.556  95.585  1.00 77.62  ?  815 LEU   A CD2 1 
ATOM   5059 N N   . LEU   A 1 694 ? -9.243  59.839  96.585  1.00 75.81  ?  816 LEU   A N   1 
ATOM   5060 C CA  . LEU   A 1 694 ? -8.835  59.291  97.866  1.00 79.79  ?  816 LEU   A CA  1 
ATOM   5061 C C   . LEU   A 1 694 ? -7.841  60.218  98.566  1.00 78.29  ?  816 LEU   A C   1 
ATOM   5062 O O   . LEU   A 1 694 ? -7.898  60.372  99.792  1.00 76.91  ?  816 LEU   A O   1 
ATOM   5063 C CB  . LEU   A 1 694 ? -8.262  57.882  97.677  1.00 80.65  ?  816 LEU   A CB  1 
ATOM   5064 C CG  . LEU   A 1 694 ? -9.246  56.718  97.770  1.00 73.80  ?  816 LEU   A CG  1 
ATOM   5065 C CD1 . LEU   A 1 694 ? -8.586  55.512  97.227  1.00 80.03  ?  816 LEU   A CD1 1 
ATOM   5066 C CD2 . LEU   A 1 694 ? -9.652  56.480  99.184  1.00 86.41  ?  816 LEU   A CD2 1 
ATOM   5067 N N   . SER   A 1 695 ? -6.948  60.864  97.806  1.00 77.89  ?  817 SER   A N   1 
ATOM   5068 C CA  . SER   A 1 695 ? -5.973  61.766  98.414  1.00 77.80  ?  817 SER   A CA  1 
ATOM   5069 C C   . SER   A 1 695 ? -6.656  62.977  98.996  1.00 80.18  ?  817 SER   A C   1 
ATOM   5070 O O   . SER   A 1 695 ? -6.241  63.476  100.049 1.00 82.03  ?  817 SER   A O   1 
ATOM   5071 C CB  . SER   A 1 695 ? -4.913  62.212  97.401  1.00 76.64  ?  817 SER   A CB  1 
ATOM   5072 O OG  . SER   A 1 695 ? -5.485  63.004  96.388  1.00 75.88  ?  817 SER   A OG  1 
ATOM   5073 N N   . GLY   A 1 696 ? -7.698  63.459  98.317  1.00 80.63  ?  818 GLY   A N   1 
ATOM   5074 C CA  . GLY   A 1 696 ? -8.492  64.542  98.869  1.00 83.92  ?  818 GLY   A CA  1 
ATOM   5075 C C   . GLY   A 1 696 ? -9.120  64.178  100.200 1.00 78.72  ?  818 GLY   A C   1 
ATOM   5076 O O   . GLY   A 1 696 ? -8.969  64.900  101.185 1.00 79.46  ?  818 GLY   A O   1 
ATOM   5077 N N   . LEU   A 1 697 ? -9.836  63.054  100.244 1.00 74.17  ?  819 LEU   A N   1 
ATOM   5078 C CA  . LEU   A 1 697 ? -10.378 62.596  101.511 1.00 78.67  ?  819 LEU   A CA  1 
ATOM   5079 C C   . LEU   A 1 697 ? -9.294  62.561  102.572 1.00 82.04  ?  819 LEU   A C   1 
ATOM   5080 O O   . LEU   A 1 697 ? -9.554  62.881  103.743 1.00 85.48  ?  819 LEU   A O   1 
ATOM   5081 C CB  . LEU   A 1 697 ? -10.995 61.209  101.356 1.00 79.82  ?  819 LEU   A CB  1 
ATOM   5082 C CG  . LEU   A 1 697 ? -12.269 61.085  100.533 1.00 79.83  ?  819 LEU   A CG  1 
ATOM   5083 C CD1 . LEU   A 1 697 ? -13.031 59.860  100.993 1.00 82.45  ?  819 LEU   A CD1 1 
ATOM   5084 C CD2 . LEU   A 1 697 ? -13.112 62.333  100.599 1.00 83.89  ?  819 LEU   A CD2 1 
ATOM   5085 N N   . ARG   A 1 698 ? -8.067  62.214  102.157 1.00 80.01  ?  820 ARG   A N   1 
ATOM   5086 C CA  . ARG   A 1 698 ? -6.953  62.016  103.077 1.00 78.38  ?  820 ARG   A CA  1 
ATOM   5087 C C   . ARG   A 1 698 ? -6.506  63.322  103.687 1.00 80.74  ?  820 ARG   A C   1 
ATOM   5088 O O   . ARG   A 1 698 ? -6.506  63.473  104.909 1.00 86.59  ?  820 ARG   A O   1 
ATOM   5089 C CB  . ARG   A 1 698 ? -5.774  61.369  102.361 1.00 76.97  ?  820 ARG   A CB  1 
ATOM   5090 C CG  . ARG   A 1 698 ? -4.528  61.307  103.215 1.00 75.97  ?  820 ARG   A CG  1 
ATOM   5091 C CD  . ARG   A 1 698 ? -3.250  61.010  102.399 1.00 80.34  ?  820 ARG   A CD  1 
ATOM   5092 N NE  . ARG   A 1 698 ? -2.695  62.120  101.624 1.00 82.15  ?  820 ARG   A NE  1 
ATOM   5093 C CZ  . ARG   A 1 698 ? -2.422  62.071  100.323 1.00 81.81  ?  820 ARG   A CZ  1 
ATOM   5094 N NH1 . ARG   A 1 698 ? -2.782  61.041  99.579  1.00 76.80  ?  820 ARG   A NH1 1 
ATOM   5095 N NH2 . ARG   A 1 698 ? -1.736  63.061  99.761  1.00 79.98  ?  820 ARG   A NH2 1 
ATOM   5096 N N   . GLU   A 1 699 ? -6.064  64.265  102.851 1.00 81.17  ?  821 GLU   A N   1 
ATOM   5097 C CA  . GLU   A 1 699 ? -5.538  65.510  103.396 1.00 80.09  ?  821 GLU   A CA  1 
ATOM   5098 C C   . GLU   A 1 699 ? -6.580  66.178  104.280 1.00 80.81  ?  821 GLU   A C   1 
ATOM   5099 O O   . GLU   A 1 699 ? -6.266  66.566  105.406 1.00 85.13  ?  821 GLU   A O   1 
ATOM   5100 C CB  . GLU   A 1 699 ? -5.051  66.429  102.270 1.00 74.40  ?  821 GLU   A CB  1 
ATOM   5101 C CG  . GLU   A 1 699 ? -3.756  65.946  101.618 1.00 74.36  ?  821 GLU   A CG  1 
ATOM   5102 C CD  . GLU   A 1 699 ? -2.595  65.659  102.614 1.00 81.30  ?  821 GLU   A CD  1 
ATOM   5103 O OE1 . GLU   A 1 699 ? -2.584  64.580  103.210 1.00 84.68  ?  821 GLU   A OE1 1 
ATOM   5104 O OE2 . GLU   A 1 699 ? -1.622  66.446  102.743 1.00 82.45  ?  821 GLU   A OE2 1 
ATOM   5105 N N   . ALA   A 1 700 ? -7.839  66.234  103.830 1.00 76.98  ?  822 ALA   A N   1 
ATOM   5106 C CA  . ALA   A 1 700 ? -8.910  66.746  104.678 1.00 76.74  ?  822 ALA   A CA  1 
ATOM   5107 C C   . ALA   A 1 700 ? -8.851  66.114  106.057 1.00 83.68  ?  822 ALA   A C   1 
ATOM   5108 O O   . ALA   A 1 700 ? -8.724  66.808  107.068 1.00 87.02  ?  822 ALA   A O   1 
ATOM   5109 C CB  . ALA   A 1 700 ? -10.272 66.497  104.045 1.00 76.73  ?  822 ALA   A CB  1 
ATOM   5110 N N   . GLY   A 1 701 ? -8.900  64.793  106.118 1.00 84.43  ?  823 GLY   A N   1 
ATOM   5111 C CA  . GLY   A 1 701 ? -8.730  64.120  107.394 1.00 90.51  ?  823 GLY   A CA  1 
ATOM   5112 C C   . GLY   A 1 701 ? -7.504  64.522  108.207 1.00 91.03  ?  823 GLY   A C   1 
ATOM   5113 O O   . GLY   A 1 701 ? -7.503  64.387  109.432 1.00 95.36  ?  823 GLY   A O   1 
ATOM   5114 N N   . ARG   A 1 702 ? -6.444  65.003  107.561 1.00 86.41  ?  824 ARG   A N   1 
ATOM   5115 C CA  . ARG   A 1 702 ? -5.247  65.336  108.319 1.00 84.67  ?  824 ARG   A CA  1 
ATOM   5116 C C   . ARG   A 1 702 ? -5.254  66.788  108.763 1.00 89.45  ?  824 ARG   A C   1 
ATOM   5117 O O   . ARG   A 1 702 ? -4.782  67.120  109.862 1.00 89.33  ?  824 ARG   A O   1 
ATOM   5118 C CB  . ARG   A 1 702 ? -3.992  65.081  107.490 1.00 82.29  ?  824 ARG   A CB  1 
ATOM   5119 C CG  . ARG   A 1 702 ? -2.866  65.945  107.998 1.00 91.05  ?  824 ARG   A CG  1 
ATOM   5120 C CD  . ARG   A 1 702 ? -1.504  65.562  107.515 1.00 92.93  ?  824 ARG   A CD  1 
ATOM   5121 N NE  . ARG   A 1 702 ? -1.498  65.039  106.160 1.00 84.46  ?  824 ARG   A NE  1 
ATOM   5122 C CZ  . ARG   A 1 702 ? -0.584  64.178  105.748 1.00 91.98  ?  824 ARG   A CZ  1 
ATOM   5123 N NH1 . ARG   A 1 702 ? 0.375   63.762  106.564 1.00 87.42  ?  824 ARG   A NH1 1 
ATOM   5124 N NH2 . ARG   A 1 702 ? -0.631  63.723  104.494 1.00 95.60  ?  824 ARG   A NH2 1 
ATOM   5125 N N   . ILE   A 1 703 ? -5.757  67.659  107.885 1.00 92.24  ?  825 ILE   A N   1 
ATOM   5126 C CA  . ILE   A 1 703 ? -5.938  69.070  108.208 1.00 86.05  ?  825 ILE   A CA  1 
ATOM   5127 C C   . ILE   A 1 703 ? -6.905  69.205  109.371 1.00 86.90  ?  825 ILE   A C   1 
ATOM   5128 O O   . ILE   A 1 703 ? -6.611  69.866  110.368 1.00 91.18  ?  825 ILE   A O   1 
ATOM   5129 C CB  . ILE   A 1 703 ? -6.425  69.827  106.963 1.00 78.55  ?  825 ILE   A CB  1 
ATOM   5130 C CG1 . ILE   A 1 703 ? -5.271  70.030  105.991 1.00 69.53  ?  825 ILE   A CG1 1 
ATOM   5131 C CG2 . ILE   A 1 703 ? -7.058  71.120  107.357 1.00 83.03  ?  825 ILE   A CG2 1 
ATOM   5132 C CD1 . ILE   A 1 703 ? -5.760  70.406  104.650 1.00 72.10  ?  825 ILE   A CD1 1 
ATOM   5133 N N   . ALA   A 1 704 ? -8.054  68.535  109.280 1.00 87.13  ?  826 ALA   A N   1 
ATOM   5134 C CA  . ALA   A 1 704 ? -8.989  68.500  110.399 1.00 89.73  ?  826 ALA   A CA  1 
ATOM   5135 C C   . ALA   A 1 704 ? -8.306  68.061  111.684 1.00 88.48  ?  826 ALA   A C   1 
ATOM   5136 O O   . ALA   A 1 704 ? -8.518  68.646  112.749 1.00 90.85  ?  826 ALA   A O   1 
ATOM   5137 C CB  . ALA   A 1 704 ? -10.152 67.567  110.072 1.00 92.92  ?  826 ALA   A CB  1 
ATOM   5138 N N   . ASP   A 1 705 ? -7.472  67.037  111.603 1.00 90.25  ?  827 ASP   A N   1 
ATOM   5139 C CA  . ASP   A 1 705 ? -6.731  66.623  112.782 1.00 97.35  ?  827 ASP   A CA  1 
ATOM   5140 C C   . ASP   A 1 705 ? -5.802  67.729  113.273 1.00 94.52  ?  827 ASP   A C   1 
ATOM   5141 O O   . ASP   A 1 705 ? -5.557  67.843  114.480 1.00 103.16 ?  827 ASP   A O   1 
ATOM   5142 C CB  . ASP   A 1 705 ? -5.923  65.349  112.490 1.00 101.50 ?  827 ASP   A CB  1 
ATOM   5143 C CG  . ASP   A 1 705 ? -6.759  64.071  112.560 1.00 101.40 ?  827 ASP   A CG  1 
ATOM   5144 O OD1 . ASP   A 1 705 ? -7.998  64.151  112.797 1.00 99.36  ?  827 ASP   A OD1 1 
ATOM   5145 O OD2 . ASP   A 1 705 ? -6.138  62.982  112.444 1.00 98.72  ?  827 ASP   A OD2 1 
ATOM   5146 N N   . GLN   A 1 706 ? -5.281  68.556  112.366 1.00 90.11  ?  828 GLN   A N   1 
ATOM   5147 C CA  . GLN   A 1 706 ? -4.324  69.578  112.781 1.00 92.45  ?  828 GLN   A CA  1 
ATOM   5148 C C   . GLN   A 1 706 ? -5.002  70.760  113.461 1.00 93.97  ?  828 GLN   A C   1 
ATOM   5149 O O   . GLN   A 1 706 ? -4.484  71.301  114.442 1.00 95.87  ?  828 GLN   A O   1 
ATOM   5150 C CB  . GLN   A 1 706 ? -3.523  70.071  111.586 1.00 94.46  ?  828 GLN   A CB  1 
ATOM   5151 C CG  . GLN   A 1 706 ? -2.469  71.083  111.962 1.00 93.89  ?  828 GLN   A CG  1 
ATOM   5152 C CD  . GLN   A 1 706 ? -1.373  70.438  112.778 1.00 105.23 ?  828 GLN   A CD  1 
ATOM   5153 O OE1 . GLN   A 1 706 ? -0.566  69.661  112.262 1.00 110.15 ?  828 GLN   A OE1 1 
ATOM   5154 N NE2 . GLN   A 1 706 ? -1.353  70.732  114.074 1.00 107.16 ?  828 GLN   A NE2 1 
ATOM   5155 N N   . PHE   A 1 707 ? -6.151  71.183  112.955 1.00 97.07  ?  829 PHE   A N   1 
ATOM   5156 C CA  . PHE   A 1 707 ? -6.747  72.434  113.376 1.00 92.29  ?  829 PHE   A CA  1 
ATOM   5157 C C   . PHE   A 1 707 ? -8.014  72.253  114.180 1.00 93.37  ?  829 PHE   A C   1 
ATOM   5158 O O   . PHE   A 1 707 ? -8.326  73.105  115.009 1.00 100.38 ?  829 PHE   A O   1 
ATOM   5159 C CB  . PHE   A 1 707 ? -6.992  73.317  112.144 1.00 87.38  ?  829 PHE   A CB  1 
ATOM   5160 C CG  . PHE   A 1 707 ? -5.718  73.655  111.437 1.00 84.64  ?  829 PHE   A CG  1 
ATOM   5161 C CD1 . PHE   A 1 707 ? -4.905  74.660  111.898 1.00 95.15  ?  829 PHE   A CD1 1 
ATOM   5162 C CD2 . PHE   A 1 707 ? -5.315  72.967  110.338 1.00 90.16  ?  829 PHE   A CD2 1 
ATOM   5163 C CE1 . PHE   A 1 707 ? -3.707  74.969  111.279 1.00 93.00  ?  829 PHE   A CE1 1 
ATOM   5164 C CE2 . PHE   A 1 707 ? -4.110  73.285  109.713 1.00 95.74  ?  829 PHE   A CE2 1 
ATOM   5165 C CZ  . PHE   A 1 707 ? -3.314  74.286  110.193 1.00 89.52  ?  829 PHE   A CZ  1 
ATOM   5166 N N   . LEU   A 1 708 ? -8.714  71.151  114.006 1.00 94.00  ?  830 LEU   A N   1 
ATOM   5167 C CA  . LEU   A 1 708 ? -9.831  70.842  114.872 1.00 99.98  ?  830 LEU   A CA  1 
ATOM   5168 C C   . LEU   A 1 708 ? -9.458  69.874  115.977 1.00 104.38 ?  830 LEU   A C   1 
ATOM   5169 O O   . LEU   A 1 708 ? -10.337 69.495  116.756 1.00 113.32 ?  830 LEU   A O   1 
ATOM   5170 C CB  . LEU   A 1 708 ? -10.990 70.286  114.048 1.00 96.23  ?  830 LEU   A CB  1 
ATOM   5171 C CG  . LEU   A 1 708 ? -11.206 71.117  112.781 1.00 95.05  ?  830 LEU   A CG  1 
ATOM   5172 C CD1 . LEU   A 1 708 ? -12.402 70.609  111.967 1.00 97.73  ?  830 LEU   A CD1 1 
ATOM   5173 C CD2 . LEU   A 1 708 ? -11.374 72.585  113.145 1.00 93.79  ?  830 LEU   A CD2 1 
ATOM   5174 N N   . GLY   A 1 709 ? -8.180  69.480  116.072 1.00 99.62  ?  831 GLY   A N   1 
ATOM   5175 C CA  . GLY   A 1 709 ? -7.716  68.534  117.074 1.00 108.35 ?  831 GLY   A CA  1 
ATOM   5176 C C   . GLY   A 1 709 ? -7.548  67.083  117.495 1.00 119.22 ?  831 GLY   A C   1 
ATOM   5177 O O   . GLY   A 1 709 ? -6.851  66.776  118.473 1.00 120.64 ?  831 GLY   A O   1 
ATOM   5178 N N   . ALA   A 1 710 ? -8.170  66.162  116.764 1.00 117.22 ?  832 ALA   A N   1 
ATOM   5179 C CA  . ALA   A 1 710 ? -8.143  64.745  117.130 1.00 123.72 ?  832 ALA   A CA  1 
ATOM   5180 C C   . ALA   A 1 710 ? -8.563  64.239  118.510 1.00 138.87 ?  832 ALA   A C   1 
ATOM   5181 O O   . ALA   A 1 710 ? -7.732  63.737  119.277 1.00 139.19 ?  832 ALA   A O   1 
ATOM   5182 C CB  . ALA   A 1 710 ? -7.110  63.823  116.498 1.00 121.25 ?  832 ALA   A CB  1 
ATOM   5183 N N   . MET   A 1 711 ? -9.868  64.347  118.814 1.00 143.35 ?  833 MET   A N   1 
ATOM   5184 C CA  . MET   A 1 711 ? -10.399 63.920  120.110 1.00 143.52 ?  833 MET   A CA  1 
ATOM   5185 C C   . MET   A 1 711 ? -10.510 62.396  120.236 1.00 136.35 ?  833 MET   A C   1 
ATOM   5186 O O   . MET   A 1 711 ? -10.601 61.882  121.359 1.00 135.04 ?  833 MET   A O   1 
ATOM   5187 C CB  . MET   A 1 711 ? -11.777 64.561  120.357 1.00 144.74 ?  833 MET   A CB  1 
ATOM   5188 C CG  . MET   A 1 711 ? -11.943 66.080  120.020 1.00 150.29 ?  833 MET   A CG  1 
ATOM   5189 S SD  . MET   A 1 711 ? -11.097 67.362  121.010 1.00 160.11 ?  833 MET   A SD  1 
ATOM   5190 C CE  . MET   A 1 711 ? -11.919 68.859  120.429 1.00 118.33 ?  833 MET   A CE  1 
ATOM   5191 N N   . TYR   A 1 712 ? -10.464 61.668  119.113 1.00 135.42 ?  834 TYR   A N   1 
ATOM   5192 C CA  . TYR   A 1 712 ? -10.711 60.225  119.033 1.00 140.65 ?  834 TYR   A CA  1 
ATOM   5193 C C   . TYR   A 1 712 ? -9.467  59.354  119.329 1.00 134.61 ?  834 TYR   A C   1 
ATOM   5194 O O   . TYR   A 1 712 ? -9.341  58.246  118.781 1.00 122.22 ?  834 TYR   A O   1 
ATOM   5195 C CB  . TYR   A 1 712 ? -11.293 59.878  117.648 1.00 136.97 ?  834 TYR   A CB  1 
ATOM   5196 C CG  . TYR   A 1 712 ? -10.428 60.340  116.484 1.00 130.74 ?  834 TYR   A CG  1 
ATOM   5197 C CD1 . TYR   A 1 712 ? -9.369  59.553  116.022 1.00 124.22 ?  834 TYR   A CD1 1 
ATOM   5198 C CD2 . TYR   A 1 712 ? -10.645 61.583  115.878 1.00 125.00 ?  834 TYR   A CD2 1 
ATOM   5199 C CE1 . TYR   A 1 712 ? -8.554  59.983  114.987 1.00 123.52 ?  834 TYR   A CE1 1 
ATOM   5200 C CE2 . TYR   A 1 712 ? -9.837  62.022  114.834 1.00 122.22 ?  834 TYR   A CE2 1 
ATOM   5201 C CZ  . TYR   A 1 712 ? -8.792  61.216  114.392 1.00 121.82 ?  834 TYR   A CZ  1 
ATOM   5202 O OH  . TYR   A 1 712 ? -7.983  61.633  113.356 1.00 111.18 ?  834 TYR   A OH  1 
ATOM   5203 N N   . THR   A 1 713 ? -8.557  59.793  120.203 1.00 139.16 ?  835 THR   A N   1 
ATOM   5204 C CA  . THR   A 1 713 ? -7.331  59.035  120.428 1.00 134.33 ?  835 THR   A CA  1 
ATOM   5205 C C   . THR   A 1 713 ? -7.018  58.795  121.915 1.00 139.62 ?  835 THR   A C   1 
ATOM   5206 O O   . THR   A 1 713 ? -5.922  58.303  122.231 1.00 139.59 ?  835 THR   A O   1 
ATOM   5207 C CB  . THR   A 1 713 ? -6.156  59.730  119.703 1.00 130.37 ?  835 THR   A CB  1 
ATOM   5208 O OG1 . THR   A 1 713 ? -6.298  61.158  119.782 1.00 133.25 ?  835 THR   A OG1 1 
ATOM   5209 C CG2 . THR   A 1 713 ? -6.159  59.351  118.234 1.00 118.52 ?  835 THR   A CG2 1 
ATOM   5210 N N   . LEU   A 1 714 ? -7.959  59.080  122.831 1.00 137.66 ?  836 LEU   A N   1 
ATOM   5211 C CA  . LEU   A 1 714 ? -7.780  58.805  124.272 1.00 135.98 ?  836 LEU   A CA  1 
ATOM   5212 C C   . LEU   A 1 714 ? -8.149  57.347  124.620 1.00 117.25 ?  836 LEU   A C   1 
ATOM   5213 O O   . LEU   A 1 714 ? -7.571  56.724  125.514 1.00 98.13  ?  836 LEU   A O   1 
ATOM   5214 C CB  . LEU   A 1 714 ? -8.631  59.761  125.141 1.00 144.81 ?  836 LEU   A CB  1 
ATOM   5215 C CG  . LEU   A 1 714 ? -8.117  61.151  125.581 1.00 138.55 ?  836 LEU   A CG  1 
ATOM   5216 C CD1 . LEU   A 1 714 ? -7.722  62.020  124.341 1.00 125.21 ?  836 LEU   A CD1 1 
ATOM   5217 C CD2 . LEU   A 1 714 ? -9.048  61.884  126.612 1.00 118.25 ?  836 LEU   A CD2 1 
ATOM   5218 N N   . ARG   B 2 4   ? 10.556  32.530  89.321  1.00 140.76 ?  308 ARG   B N   1 
ATOM   5219 C CA  . ARG   B 2 4   ? 11.698  31.621  89.549  1.00 159.21 ?  308 ARG   B CA  1 
ATOM   5220 C C   . ARG   B 2 4   ? 12.465  31.247  88.270  1.00 156.29 ?  308 ARG   B C   1 
ATOM   5221 O O   . ARG   B 2 4   ? 13.688  31.034  88.297  1.00 151.89 ?  308 ARG   B O   1 
ATOM   5222 C CB  . ARG   B 2 4   ? 11.244  30.330  90.270  1.00 164.15 ?  308 ARG   B CB  1 
ATOM   5223 C CG  . ARG   B 2 4   ? 11.504  30.305  91.793  1.00 166.26 ?  308 ARG   B CG  1 
ATOM   5224 C CD  . ARG   B 2 4   ? 13.017  30.193  92.050  1.00 169.11 ?  308 ARG   B CD  1 
ATOM   5225 N NE  . ARG   B 2 4   ? 13.474  30.592  93.381  1.00 177.80 ?  308 ARG   B NE  1 
ATOM   5226 C CZ  . ARG   B 2 4   ? 14.028  31.765  93.674  1.00 177.76 ?  308 ARG   B CZ  1 
ATOM   5227 N NH1 . ARG   B 2 4   ? 14.145  32.724  92.767  1.00 172.03 ?  308 ARG   B NH1 1 
ATOM   5228 N NH2 . ARG   B 2 4   ? 14.491  31.978  94.905  1.00 177.70 ?  308 ARG   B NH2 1 
ATOM   5229 N N   . LYS   B 2 5   ? 11.750  31.164  87.154  1.00 154.07 ?  309 LYS   B N   1 
ATOM   5230 C CA  . LYS   B 2 5   ? 12.319  30.755  85.878  1.00 145.15 ?  309 LYS   B CA  1 
ATOM   5231 C C   . LYS   B 2 5   ? 11.658  31.590  84.789  1.00 138.66 ?  309 LYS   B C   1 
ATOM   5232 O O   . LYS   B 2 5   ? 10.517  32.038  84.962  1.00 139.01 ?  309 LYS   B O   1 
ATOM   5233 C CB  . LYS   B 2 5   ? 12.110  29.244  85.641  1.00 144.12 ?  309 LYS   B CB  1 
ATOM   5234 C CG  . LYS   B 2 5   ? 13.275  28.373  86.183  1.00 153.68 ?  309 LYS   B CG  1 
ATOM   5235 C CD  . LYS   B 2 5   ? 13.276  26.891  85.700  1.00 158.06 ?  309 LYS   B CD  1 
ATOM   5236 C CE  . LYS   B 2 5   ? 14.025  25.970  86.706  1.00 148.89 ?  309 LYS   B CE  1 
ATOM   5237 N NZ  . LYS   B 2 5   ? 14.104  24.515  86.356  1.00 119.51 ?  309 LYS   B NZ  1 
ATOM   5238 N N   . PRO   B 2 6   ? 12.357  31.862  83.689  1.00 132.08 ?  310 PRO   B N   1 
ATOM   5239 C CA  . PRO   B 2 6   ? 11.780  32.698  82.632  1.00 125.06 ?  310 PRO   B CA  1 
ATOM   5240 C C   . PRO   B 2 6   ? 10.547  32.033  82.064  1.00 123.91 ?  310 PRO   B C   1 
ATOM   5241 O O   . PRO   B 2 6   ? 10.409  30.810  82.162  1.00 126.57 ?  310 PRO   B O   1 
ATOM   5242 C CB  . PRO   B 2 6   ? 12.890  32.765  81.578  1.00 126.49 ?  310 PRO   B CB  1 
ATOM   5243 C CG  . PRO   B 2 6   ? 14.136  32.421  82.302  1.00 129.34 ?  310 PRO   B CG  1 
ATOM   5244 C CD  . PRO   B 2 6   ? 13.738  31.457  83.377  1.00 130.77 ?  310 PRO   B CD  1 
ATOM   5245 N N   . PRO   B 2 7   ? 9.638   32.788  81.460  1.00 125.35 ?  311 PRO   B N   1 
ATOM   5246 C CA  . PRO   B 2 7   ? 8.484   32.157  80.804  1.00 130.45 ?  311 PRO   B CA  1 
ATOM   5247 C C   . PRO   B 2 7   ? 8.981   31.217  79.723  1.00 137.22 ?  311 PRO   B C   1 
ATOM   5248 O O   . PRO   B 2 7   ? 9.710   31.631  78.818  1.00 140.61 ?  311 PRO   B O   1 
ATOM   5249 C CB  . PRO   B 2 7   ? 7.712   33.343  80.213  1.00 130.66 ?  311 PRO   B CB  1 
ATOM   5250 C CG  . PRO   B 2 7   ? 8.275   34.541  80.882  1.00 129.68 ?  311 PRO   B CG  1 
ATOM   5251 C CD  . PRO   B 2 7   ? 9.705   34.221  81.174  1.00 128.02 ?  311 PRO   B CD  1 
ATOM   5252 N N   . LYS   B 2 8   ? 8.594   29.941  79.833  1.00 140.41 ?  312 LYS   B N   1 
ATOM   5253 C CA  . LYS   B 2 8   ? 9.193   28.889  79.012  1.00 145.46 ?  312 LYS   B CA  1 
ATOM   5254 C C   . LYS   B 2 8   ? 9.055   29.223  77.526  1.00 144.15 ?  312 LYS   B C   1 
ATOM   5255 O O   . LYS   B 2 8   ? 7.983   29.625  77.057  1.00 136.52 ?  312 LYS   B O   1 
ATOM   5256 C CB  . LYS   B 2 8   ? 8.561   27.524  79.341  1.00 143.78 ?  312 LYS   B CB  1 
ATOM   5257 C CG  . LYS   B 2 8   ? 9.509   26.545  80.091  1.00 147.21 ?  312 LYS   B CG  1 
ATOM   5258 C CD  . LYS   B 2 8   ? 8.767   25.374  80.775  1.00 153.24 ?  312 LYS   B CD  1 
ATOM   5259 C CE  . LYS   B 2 8   ? 9.504   24.864  82.033  1.00 152.29 ?  312 LYS   B CE  1 
ATOM   5260 N NZ  . LYS   B 2 8   ? 8.686   23.917  82.869  1.00 145.10 ?  312 LYS   B NZ  1 
ATOM   5261 N N   . GLY   B 2 9   ? 10.174  29.099  76.801  1.00 142.86 ?  313 GLY   B N   1 
ATOM   5262 C CA  . GLY   B 2 9   ? 10.301  29.611  75.451  1.00 142.73 ?  313 GLY   B CA  1 
ATOM   5263 C C   . GLY   B 2 9   ? 11.096  30.900  75.335  1.00 140.07 ?  313 GLY   B C   1 
ATOM   5264 O O   . GLY   B 2 9   ? 11.456  31.296  74.216  1.00 137.24 ?  313 GLY   B O   1 
ATOM   5265 N N   . MET   B 2 10  ? 11.367  31.568  76.448  1.00 135.40 ?  314 MET   B N   1 
ATOM   5266 C CA  . MET   B 2 10  ? 12.182  32.768  76.455  1.00 131.51 ?  314 MET   B CA  1 
ATOM   5267 C C   . MET   B 2 10  ? 13.560  32.395  76.975  1.00 129.07 ?  314 MET   B C   1 
ATOM   5268 O O   . MET   B 2 10  ? 13.682  31.709  77.995  1.00 126.46 ?  314 MET   B O   1 
ATOM   5269 C CB  . MET   B 2 10  ? 11.549  33.852  77.325  1.00 131.90 ?  314 MET   B CB  1 
ATOM   5270 C CG  . MET   B 2 10  ? 11.534  35.225  76.675  1.00 132.14 ?  314 MET   B CG  1 
ATOM   5271 S SD  . MET   B 2 10  ? 10.016  35.390  75.724  1.00 135.26 ?  314 MET   B SD  1 
ATOM   5272 C CE  . MET   B 2 10  ? 8.852   35.011  77.046  1.00 122.75 ?  314 MET   B CE  1 
ATOM   5273 N N   . PHE   B 2 11  ? 14.587  32.822  76.277  1.00 127.70 ?  315 PHE   B N   1 
ATOM   5274 C CA  . PHE   B 2 11  ? 15.935  32.422  76.637  1.00 129.87 ?  315 PHE   B CA  1 
ATOM   5275 C C   . PHE   B 2 11  ? 16.621  33.639  77.221  1.00 128.21 ?  315 PHE   B C   1 
ATOM   5276 O O   . PHE   B 2 11  ? 16.980  34.571  76.497  1.00 127.17 ?  315 PHE   B O   1 
ATOM   5277 C CB  . PHE   B 2 11  ? 16.673  31.868  75.435  1.00 136.68 ?  315 PHE   B CB  1 
ATOM   5278 C CG  . PHE   B 2 11  ? 16.436  30.405  75.227  1.00 139.82 ?  315 PHE   B CG  1 
ATOM   5279 C CD1 . PHE   B 2 11  ? 15.155  29.941  74.932  1.00 132.23 ?  315 PHE   B CD1 1 
ATOM   5280 C CD2 . PHE   B 2 11  ? 17.480  29.490  75.363  1.00 142.06 ?  315 PHE   B CD2 1 
ATOM   5281 C CE1 . PHE   B 2 11  ? 14.922  28.606  74.747  1.00 132.46 ?  315 PHE   B CE1 1 
ATOM   5282 C CE2 . PHE   B 2 11  ? 17.259  28.136  75.178  1.00 141.89 ?  315 PHE   B CE2 1 
ATOM   5283 C CZ  . PHE   B 2 11  ? 15.978  27.692  74.872  1.00 141.41 ?  315 PHE   B CZ  1 
ATOM   5284 N N   . LEU   B 2 12  ? 16.768  33.630  78.539  1.00 126.95 ?  316 LEU   B N   1 
ATOM   5285 C CA  . LEU   B 2 12  ? 17.386  34.725  79.275  1.00 130.85 ?  316 LEU   B CA  1 
ATOM   5286 C C   . LEU   B 2 12  ? 18.379  34.072  80.221  1.00 135.45 ?  316 LEU   B C   1 
ATOM   5287 O O   . LEU   B 2 12  ? 18.005  33.621  81.309  1.00 137.31 ?  316 LEU   B O   1 
ATOM   5288 C CB  . LEU   B 2 12  ? 16.352  35.551  80.036  1.00 124.52 ?  316 LEU   B CB  1 
ATOM   5289 C CG  . LEU   B 2 12  ? 15.017  35.719  79.314  1.00 119.76 ?  316 LEU   B CG  1 
ATOM   5290 C CD1 . LEU   B 2 12  ? 13.928  36.095  80.280  1.00 115.12 ?  316 LEU   B CD1 1 
ATOM   5291 C CD2 . LEU   B 2 12  ? 15.127  36.739  78.195  1.00 121.25 ?  316 LEU   B CD2 1 
ATOM   5292 N N   . SER   B 2 13  ? 19.630  33.985  79.805  1.00 134.84 ?  317 SER   B N   1 
ATOM   5293 C CA  . SER   B 2 13  ? 20.656  33.510  80.713  1.00 144.47 ?  317 SER   B CA  1 
ATOM   5294 C C   . SER   B 2 13  ? 21.480  34.696  81.181  1.00 144.36 ?  317 SER   B C   1 
ATOM   5295 O O   . SER   B 2 13  ? 21.640  35.683  80.457  1.00 141.40 ?  317 SER   B O   1 
ATOM   5296 C CB  . SER   B 2 13  ? 21.553  32.452  80.060  1.00 152.92 ?  317 SER   B CB  1 
ATOM   5297 O OG  . SER   B 2 13  ? 22.728  33.017  79.503  1.00 154.02 ?  317 SER   B OG  1 
ATOM   5298 N N   . GLN   B 2 14  ? 21.967  34.598  82.421  1.00 144.35 ?  318 GLN   B N   1 
ATOM   5299 C CA  . GLN   B 2 14  ? 22.840  35.630  82.975  1.00 149.24 ?  318 GLN   B CA  1 
ATOM   5300 C C   . GLN   B 2 14  ? 23.931  36.013  81.980  1.00 146.42 ?  318 GLN   B C   1 
ATOM   5301 O O   . GLN   B 2 14  ? 24.095  37.188  81.623  1.00 140.44 ?  318 GLN   B O   1 
ATOM   5302 C CB  . GLN   B 2 14  ? 23.449  35.125  84.288  1.00 149.62 ?  318 GLN   B CB  1 
ATOM   5303 C CG  . GLN   B 2 14  ? 24.336  36.131  85.021  1.00 153.00 ?  318 GLN   B CG  1 
ATOM   5304 C CD  . GLN   B 2 14  ? 23.626  37.436  85.365  1.00 150.97 ?  318 GLN   B CD  1 
ATOM   5305 O OE1 . GLN   B 2 14  ? 24.081  38.517  84.983  1.00 151.93 ?  318 GLN   B OE1 1 
ATOM   5306 N NE2 . GLN   B 2 14  ? 22.531  37.343  86.123  1.00 143.67 ?  318 GLN   B NE2 1 
ATOM   5307 N N   . GLU   B 2 15  ? 24.657  35.005  81.498  1.00 146.48 ?  319 GLU   B N   1 
ATOM   5308 C CA  . GLU   B 2 15  ? 25.749  35.212  80.555  1.00 147.13 ?  319 GLU   B CA  1 
ATOM   5309 C C   . GLU   B 2 15  ? 25.253  35.884  79.271  1.00 144.63 ?  319 GLU   B C   1 
ATOM   5310 O O   . GLU   B 2 15  ? 25.848  36.862  78.796  1.00 137.04 ?  319 GLU   B O   1 
ATOM   5311 C CB  . GLU   B 2 15  ? 26.405  33.848  80.295  1.00 147.52 ?  319 GLU   B CB  1 
ATOM   5312 C CG  . GLU   B 2 15  ? 27.530  33.779  79.281  1.00 150.95 ?  319 GLU   B CG  1 
ATOM   5313 C CD  . GLU   B 2 15  ? 27.794  32.352  78.828  1.00 158.81 ?  319 GLU   B CD  1 
ATOM   5314 O OE1 . GLU   B 2 15  ? 26.813  31.595  78.630  1.00 162.39 ?  319 GLU   B OE1 1 
ATOM   5315 O OE2 . GLU   B 2 15  ? 28.984  31.979  78.703  1.00 162.04 ?  319 GLU   B OE2 1 
ATOM   5316 N N   . ASP   B 2 16  ? 24.143  35.378  78.710  1.00 147.31 ?  320 ASP   B N   1 
ATOM   5317 C CA  . ASP   B 2 16  ? 23.556  35.956  77.501  1.00 141.37 ?  320 ASP   B CA  1 
ATOM   5318 C C   . ASP   B 2 16  ? 23.400  37.461  77.628  1.00 139.24 ?  320 ASP   B C   1 
ATOM   5319 O O   . ASP   B 2 16  ? 23.718  38.212  76.696  1.00 135.96 ?  320 ASP   B O   1 
ATOM   5320 C CB  . ASP   B 2 16  ? 22.174  35.342  77.218  1.00 142.99 ?  320 ASP   B CB  1 
ATOM   5321 C CG  . ASP   B 2 16  ? 22.226  34.037  76.417  1.00 144.92 ?  320 ASP   B CG  1 
ATOM   5322 O OD1 . ASP   B 2 16  ? 23.334  33.565  76.065  1.00 145.46 ?  320 ASP   B OD1 1 
ATOM   5323 O OD2 . ASP   B 2 16  ? 21.126  33.504  76.111  1.00 143.15 ?  320 ASP   B OD2 1 
ATOM   5324 N N   . VAL   B 2 17  ? 22.913  37.915  78.787  1.00 142.16 ?  321 VAL   B N   1 
ATOM   5325 C CA  . VAL   B 2 17  ? 22.427  39.285  78.922  1.00 141.23 ?  321 VAL   B CA  1 
ATOM   5326 C C   . VAL   B 2 17  ? 23.583  40.277  78.864  1.00 143.82 ?  321 VAL   B C   1 
ATOM   5327 O O   . VAL   B 2 17  ? 23.505  41.309  78.181  1.00 141.00 ?  321 VAL   B O   1 
ATOM   5328 C CB  . VAL   B 2 17  ? 21.618  39.425  80.223  1.00 132.87 ?  321 VAL   B CB  1 
ATOM   5329 C CG1 . VAL   B 2 17  ? 21.182  40.859  80.412  1.00 123.59 ?  321 VAL   B CG1 1 
ATOM   5330 C CG2 . VAL   B 2 17  ? 20.410  38.497  80.203  1.00 132.17 ?  321 VAL   B CG2 1 
ATOM   5331 N N   . GLU   B 2 18  ? 24.681  39.970  79.558  1.00 141.63 ?  322 GLU   B N   1 
ATOM   5332 C CA  . GLU   B 2 18  ? 25.809  40.888  79.628  1.00 139.26 ?  322 GLU   B CA  1 
ATOM   5333 C C   . GLU   B 2 18  ? 26.473  41.090  78.275  1.00 141.03 ?  322 GLU   B C   1 
ATOM   5334 O O   . GLU   B 2 18  ? 27.174  42.089  78.083  1.00 142.87 ?  322 GLU   B O   1 
ATOM   5335 C CB  . GLU   B 2 18  ? 26.804  40.360  80.646  1.00 139.27 ?  322 GLU   B CB  1 
ATOM   5336 C CG  . GLU   B 2 18  ? 26.121  40.013  81.955  1.00 145.55 ?  322 GLU   B CG  1 
ATOM   5337 C CD  . GLU   B 2 18  ? 27.073  39.463  82.990  1.00 155.18 ?  322 GLU   B CD  1 
ATOM   5338 O OE1 . GLU   B 2 18  ? 27.920  40.237  83.484  1.00 160.72 ?  322 GLU   B OE1 1 
ATOM   5339 O OE2 . GLU   B 2 18  ? 26.976  38.256  83.307  1.00 153.23 ?  322 GLU   B OE2 1 
ATOM   5340 N N   . ALA   B 2 19  ? 26.252  40.173  77.334  1.00 141.94 ?  323 ALA   B N   1 
ATOM   5341 C CA  . ALA   B 2 19  ? 26.858  40.253  76.012  1.00 142.33 ?  323 ALA   B CA  1 
ATOM   5342 C C   . ALA   B 2 19  ? 26.096  41.162  75.067  1.00 140.81 ?  323 ALA   B C   1 
ATOM   5343 O O   . ALA   B 2 19  ? 26.693  41.717  74.137  1.00 143.77 ?  323 ALA   B O   1 
ATOM   5344 C CB  . ALA   B 2 19  ? 26.954  38.859  75.392  1.00 142.80 ?  323 ALA   B CB  1 
ATOM   5345 N N   . VAL   B 2 20  ? 24.789  41.314  75.277  1.00 140.51 ?  324 VAL   B N   1 
ATOM   5346 C CA  . VAL   B 2 20  ? 23.989  42.223  74.464  1.00 143.56 ?  324 VAL   B CA  1 
ATOM   5347 C C   . VAL   B 2 20  ? 23.965  43.635  75.044  1.00 145.06 ?  324 VAL   B C   1 
ATOM   5348 O O   . VAL   B 2 20  ? 23.532  44.579  74.355  1.00 138.08 ?  324 VAL   B O   1 
ATOM   5349 C CB  . VAL   B 2 20  ? 22.595  41.586  74.316  1.00 137.64 ?  324 VAL   B CB  1 
ATOM   5350 C CG1 . VAL   B 2 20  ? 21.723  42.371  73.350  1.00 134.00 ?  324 VAL   B CG1 1 
ATOM   5351 C CG2 . VAL   B 2 20  ? 22.771  40.158  73.851  1.00 132.61 ?  324 VAL   B CG2 1 
ATOM   5352 N N   . SER   B 2 21  ? 24.467  43.813  76.272  1.00 145.42 ?  325 SER   B N   1 
ATOM   5353 C CA  . SER   B 2 21  ? 24.502  45.099  76.959  1.00 146.98 ?  325 SER   B CA  1 
ATOM   5354 C C   . SER   B 2 21  ? 25.914  45.636  77.183  1.00 149.51 ?  325 SER   B C   1 
ATOM   5355 O O   . SER   B 2 21  ? 26.066  46.690  77.814  1.00 151.81 ?  325 SER   B O   1 
ATOM   5356 C CB  . SER   B 2 21  ? 23.795  44.985  78.315  1.00 141.29 ?  325 SER   B CB  1 
ATOM   5357 O OG  . SER   B 2 21  ? 24.332  43.915  79.069  1.00 139.51 ?  325 SER   B OG  1 
ATOM   5358 N N   . ALA   B 2 22  ? 26.948  44.948  76.691  1.00 149.69 ?  326 ALA   B N   1 
ATOM   5359 C CA  . ALA   B 2 22  ? 28.319  45.384  76.937  1.00 148.20 ?  326 ALA   B CA  1 
ATOM   5360 C C   . ALA   B 2 22  ? 28.638  46.733  76.288  1.00 146.32 ?  326 ALA   B C   1 
ATOM   5361 O O   . ALA   B 2 22  ? 29.561  47.417  76.743  1.00 147.48 ?  326 ALA   B O   1 
ATOM   5362 C CB  . ALA   B 2 22  ? 29.294  44.307  76.459  1.00 147.56 ?  326 ALA   B CB  1 
ATOM   5363 N N   . ASN   B 2 23  ? 27.912  47.129  75.245  1.00 141.11 ?  327 ASN   B N   1 
ATOM   5364 C CA  . ASN   B 2 23  ? 27.978  48.504  74.750  1.00 144.16 ?  327 ASN   B CA  1 
ATOM   5365 C C   . ASN   B 2 23  ? 26.700  48.793  73.958  1.00 146.58 ?  327 ASN   B C   1 
ATOM   5366 O O   . ASN   B 2 23  ? 25.686  48.104  74.133  1.00 145.11 ?  327 ASN   B O   1 
ATOM   5367 C CB  . ASN   B 2 23  ? 29.264  48.738  73.936  1.00 147.31 ?  327 ASN   B CB  1 
ATOM   5368 C CG  . ASN   B 2 23  ? 29.279  47.992  72.613  1.00 150.99 ?  327 ASN   B CG  1 
ATOM   5369 O OD1 . ASN   B 2 23  ? 28.781  48.490  71.590  1.00 144.88 ?  327 ASN   B OD1 1 
ATOM   5370 N ND2 . ASN   B 2 23  ? 29.866  46.799  72.619  1.00 151.42 ?  327 ASN   B ND2 1 
ATOM   5371 N N   . ALA   B 2 24  ? 26.747  49.817  73.091  1.00 144.26 ?  328 ALA   B N   1 
ATOM   5372 C CA  . ALA   B 2 24  ? 25.550  50.250  72.369  1.00 142.92 ?  328 ALA   B CA  1 
ATOM   5373 C C   . ALA   B 2 24  ? 25.208  49.298  71.229  1.00 149.46 ?  328 ALA   B C   1 
ATOM   5374 O O   . ALA   B 2 24  ? 24.045  48.903  71.070  1.00 151.84 ?  328 ALA   B O   1 
ATOM   5375 C CB  . ALA   B 2 24  ? 25.730  51.670  71.837  1.00 133.13 ?  328 ALA   B CB  1 
ATOM   5376 N N   . THR   B 2 25  ? 26.203  48.921  70.419  1.00 150.10 ?  329 THR   B N   1 
ATOM   5377 C CA  . THR   B 2 25  ? 25.995  47.997  69.305  1.00 150.14 ?  329 THR   B CA  1 
ATOM   5378 C C   . THR   B 2 25  ? 26.386  46.548  69.619  1.00 145.53 ?  329 THR   B C   1 
ATOM   5379 O O   . THR   B 2 25  ? 26.252  45.688  68.740  1.00 143.08 ?  329 THR   B O   1 
ATOM   5380 C CB  . THR   B 2 25  ? 26.743  48.490  68.047  1.00 145.39 ?  329 THR   B CB  1 
ATOM   5381 O OG1 . THR   B 2 25  ? 28.064  48.935  68.399  1.00 137.25 ?  329 THR   B OG1 1 
ATOM   5382 C CG2 . THR   B 2 25  ? 25.946  49.600  67.313  1.00 128.24 ?  329 THR   B CG2 1 
ATOM   5383 N N   . ALA   B 2 26  ? 26.830  46.245  70.851  1.00 143.21 ?  330 ALA   B N   1 
ATOM   5384 C CA  . ALA   B 2 26  ? 27.061  44.856  71.253  1.00 140.21 ?  330 ALA   B CA  1 
ATOM   5385 C C   . ALA   B 2 26  ? 25.831  43.986  71.041  1.00 138.55 ?  330 ALA   B C   1 
ATOM   5386 O O   . ALA   B 2 26  ? 25.954  42.760  70.948  1.00 136.81 ?  330 ALA   B O   1 
ATOM   5387 C CB  . ALA   B 2 26  ? 27.488  44.778  72.718  1.00 141.10 ?  330 ALA   B CB  1 
ATOM   5388 N N   . ALA   B 2 27  ? 24.651  44.590  70.980  1.00 141.44 ?  331 ALA   B N   1 
ATOM   5389 C CA  . ALA   B 2 27  ? 23.480  43.903  70.464  1.00 138.36 ?  331 ALA   B CA  1 
ATOM   5390 C C   . ALA   B 2 27  ? 23.690  43.562  68.992  1.00 135.11 ?  331 ALA   B C   1 
ATOM   5391 O O   . ALA   B 2 27  ? 23.783  42.386  68.625  1.00 132.63 ?  331 ALA   B O   1 
ATOM   5392 C CB  . ALA   B 2 27  ? 22.231  44.768  70.650  1.00 139.23 ?  331 ALA   B CB  1 
ATOM   5393 N N   . THR   B 2 28  ? 23.792  44.589  68.143  1.00 136.97 ?  332 THR   B N   1 
ATOM   5394 C CA  . THR   B 2 28  ? 23.902  44.370  66.703  1.00 139.14 ?  332 THR   B CA  1 
ATOM   5395 C C   . THR   B 2 28  ? 25.200  43.664  66.310  1.00 138.24 ?  332 THR   B C   1 
ATOM   5396 O O   . THR   B 2 28  ? 25.264  43.062  65.232  1.00 135.17 ?  332 THR   B O   1 
ATOM   5397 C CB  . THR   B 2 28  ? 23.755  45.709  65.976  1.00 138.66 ?  332 THR   B CB  1 
ATOM   5398 O OG1 . THR   B 2 28  ? 22.599  46.376  66.481  1.00 140.65 ?  332 THR   B OG1 1 
ATOM   5399 C CG2 . THR   B 2 28  ? 23.558  45.506  64.495  1.00 142.92 ?  332 THR   B CG2 1 
ATOM   5400 N N   . THR   B 2 29  ? 26.229  43.709  67.157  1.00 140.55 ?  333 THR   B N   1 
ATOM   5401 C CA  . THR   B 2 29  ? 27.402  42.867  66.940  1.00 138.09 ?  333 THR   B CA  1 
ATOM   5402 C C   . THR   B 2 29  ? 27.024  41.393  66.992  1.00 136.50 ?  333 THR   B C   1 
ATOM   5403 O O   . THR   B 2 29  ? 27.143  40.674  65.995  1.00 138.87 ?  333 THR   B O   1 
ATOM   5404 C CB  . THR   B 2 29  ? 28.487  43.181  67.977  1.00 139.21 ?  333 THR   B CB  1 
ATOM   5405 O OG1 . THR   B 2 29  ? 29.181  44.378  67.599  1.00 138.44 ?  333 THR   B OG1 1 
ATOM   5406 C CG2 . THR   B 2 29  ? 29.484  42.016  68.119  1.00 132.96 ?  333 THR   B CG2 1 
ATOM   5407 N N   . VAL   B 2 30  ? 26.528  40.937  68.146  1.00 135.94 ?  334 VAL   B N   1 
ATOM   5408 C CA  . VAL   B 2 30  ? 26.332  39.510  68.388  1.00 134.22 ?  334 VAL   B CA  1 
ATOM   5409 C C   . VAL   B 2 30  ? 25.420  38.876  67.340  1.00 130.60 ?  334 VAL   B C   1 
ATOM   5410 O O   . VAL   B 2 30  ? 25.571  37.693  67.010  1.00 127.52 ?  334 VAL   B O   1 
ATOM   5411 C CB  . VAL   B 2 30  ? 25.812  39.314  69.827  1.00 128.54 ?  334 VAL   B CB  1 
ATOM   5412 C CG1 . VAL   B 2 30  ? 25.265  37.915  70.044  1.00 125.83 ?  334 VAL   B CG1 1 
ATOM   5413 C CG2 . VAL   B 2 30  ? 26.929  39.601  70.803  1.00 129.11 ?  334 VAL   B CG2 1 
ATOM   5414 N N   . LEU   B 2 31  ? 24.504  39.648  66.761  1.00 130.18 ?  335 LEU   B N   1 
ATOM   5415 C CA  . LEU   B 2 31  ? 23.579  39.105  65.774  1.00 132.30 ?  335 LEU   B CA  1 
ATOM   5416 C C   . LEU   B 2 31  ? 24.091  39.220  64.332  1.00 135.06 ?  335 LEU   B C   1 
ATOM   5417 O O   . LEU   B 2 31  ? 23.320  38.984  63.393  1.00 131.87 ?  335 LEU   B O   1 
ATOM   5418 C CB  . LEU   B 2 31  ? 22.208  39.782  65.894  1.00 128.90 ?  335 LEU   B CB  1 
ATOM   5419 C CG  . LEU   B 2 31  ? 21.466  39.650  67.228  1.00 116.67 ?  335 LEU   B CG  1 
ATOM   5420 C CD1 . LEU   B 2 31  ? 19.944  39.790  67.047  1.00 110.79 ?  335 LEU   B CD1 1 
ATOM   5421 C CD2 . LEU   B 2 31  ? 21.843  38.383  67.965  1.00 120.81 ?  335 LEU   B CD2 1 
ATOM   5422 N N   . ARG   B 2 32  ? 25.354  39.600  64.135  1.00 137.75 ?  336 ARG   B N   1 
ATOM   5423 C CA  . ARG   B 2 32  ? 26.048  39.417  62.863  1.00 136.58 ?  336 ARG   B CA  1 
ATOM   5424 C C   . ARG   B 2 32  ? 27.063  38.291  62.918  1.00 140.32 ?  336 ARG   B C   1 
ATOM   5425 O O   . ARG   B 2 32  ? 27.165  37.522  61.965  1.00 145.07 ?  336 ARG   B O   1 
ATOM   5426 C CB  . ARG   B 2 32  ? 26.767  40.694  62.435  1.00 137.27 ?  336 ARG   B CB  1 
ATOM   5427 C CG  . ARG   B 2 32  ? 26.044  41.503  61.405  1.00 139.00 ?  336 ARG   B CG  1 
ATOM   5428 C CD  . ARG   B 2 32  ? 26.972  42.604  60.932  1.00 154.40 ?  336 ARG   B CD  1 
ATOM   5429 N NE  . ARG   B 2 32  ? 26.285  43.874  60.715  1.00 163.52 ?  336 ARG   B NE  1 
ATOM   5430 C CZ  . ARG   B 2 32  ? 26.545  44.993  61.386  1.00 162.84 ?  336 ARG   B CZ  1 
ATOM   5431 N NH1 . ARG   B 2 32  ? 27.472  45.039  62.333  1.00 153.74 ?  336 ARG   B NH1 1 
ATOM   5432 N NH2 . ARG   B 2 32  ? 25.859  46.097  61.098  1.00 163.09 ?  336 ARG   B NH2 1 
ATOM   5433 N N   . GLN   B 2 33  ? 27.816  38.169  64.020  1.00 138.02 ?  337 GLN   B N   1 
ATOM   5434 C CA  . GLN   B 2 33  ? 28.683  37.007  64.199  1.00 137.02 ?  337 GLN   B CA  1 
ATOM   5435 C C   . GLN   B 2 33  ? 27.891  35.728  64.339  1.00 137.87 ?  337 GLN   B C   1 
ATOM   5436 O O   . GLN   B 2 33  ? 28.478  34.648  64.277  1.00 137.49 ?  337 GLN   B O   1 
ATOM   5437 C CB  . GLN   B 2 33  ? 29.586  37.171  65.413  1.00 137.03 ?  337 GLN   B CB  1 
ATOM   5438 C CG  . GLN   B 2 33  ? 30.937  37.629  64.988  1.00 143.32 ?  337 GLN   B CG  1 
ATOM   5439 C CD  . GLN   B 2 33  ? 30.941  39.133  64.771  1.00 158.38 ?  337 GLN   B CD  1 
ATOM   5440 O OE1 . GLN   B 2 33  ? 30.705  39.905  65.705  1.00 161.85 ?  337 GLN   B OE1 1 
ATOM   5441 N NE2 . GLN   B 2 33  ? 31.147  39.557  63.519  1.00 158.55 ?  337 GLN   B NE2 1 
ATOM   5442 N N   . LEU   B 2 34  ? 26.582  35.826  64.564  1.00 138.75 ?  338 LEU   B N   1 
ATOM   5443 C CA  . LEU   B 2 34  ? 25.692  34.702  64.318  1.00 133.23 ?  338 LEU   B CA  1 
ATOM   5444 C C   . LEU   B 2 34  ? 25.238  34.693  62.859  1.00 131.13 ?  338 LEU   B C   1 
ATOM   5445 O O   . LEU   B 2 34  ? 25.498  33.723  62.146  1.00 138.22 ?  338 LEU   B O   1 
ATOM   5446 C CB  . LEU   B 2 34  ? 24.516  34.726  65.302  1.00 127.08 ?  338 LEU   B CB  1 
ATOM   5447 C CG  . LEU   B 2 34  ? 24.903  34.365  66.737  1.00 125.57 ?  338 LEU   B CG  1 
ATOM   5448 C CD1 . LEU   B 2 34  ? 23.726  33.749  67.427  1.00 125.87 ?  338 LEU   B CD1 1 
ATOM   5449 C CD2 . LEU   B 2 34  ? 26.059  33.382  66.763  1.00 122.32 ?  338 LEU   B CD2 1 
ATOM   5450 N N   . ASP   B 2 35  ? 24.606  35.774  62.387  1.00 127.29 ?  339 ASP   B N   1 
ATOM   5451 C CA  . ASP   B 2 35  ? 24.109  35.795  61.009  1.00 131.78 ?  339 ASP   B CA  1 
ATOM   5452 C C   . ASP   B 2 35  ? 25.129  35.328  59.968  1.00 134.97 ?  339 ASP   B C   1 
ATOM   5453 O O   . ASP   B 2 35  ? 24.770  34.659  58.988  1.00 131.78 ?  339 ASP   B O   1 
ATOM   5454 C CB  . ASP   B 2 35  ? 23.586  37.191  60.644  1.00 138.68 ?  339 ASP   B CB  1 
ATOM   5455 C CG  . ASP   B 2 35  ? 22.072  37.324  60.820  1.00 135.59 ?  339 ASP   B CG  1 
ATOM   5456 O OD1 . ASP   B 2 35  ? 21.508  36.637  61.696  1.00 130.34 ?  339 ASP   B OD1 1 
ATOM   5457 O OD2 . ASP   B 2 35  ? 21.442  38.095  60.057  1.00 128.96 ?  339 ASP   B OD2 1 
ATOM   5458 N N   . MET   B 2 36  ? 26.390  35.619  60.227  1.00 136.87 ?  340 MET   B N   1 
ATOM   5459 C CA  . MET   B 2 36  ? 27.398  35.215  59.230  1.00 133.61 ?  340 MET   B CA  1 
ATOM   5460 C C   . MET   B 2 36  ? 27.664  33.777  59.630  1.00 130.43 ?  340 MET   B C   1 
ATOM   5461 O O   . MET   B 2 36  ? 27.555  32.889  58.782  1.00 137.74 ?  340 MET   B O   1 
ATOM   5462 C CB  . MET   B 2 36  ? 28.698  35.997  59.388  1.00 137.42 ?  340 MET   B CB  1 
ATOM   5463 C CG  . MET   B 2 36  ? 28.543  37.462  59.043  1.00 140.48 ?  340 MET   B CG  1 
ATOM   5464 S SD  . MET   B 2 36  ? 30.049  38.419  59.307  1.00 153.89 ?  340 MET   B SD  1 
ATOM   5465 C CE  . MET   B 2 36  ? 29.477  40.059  58.865  1.00 147.83 ?  340 MET   B CE  1 
ATOM   5466 N N   . GLU   B 2 37  ? 27.936  33.577  60.907  1.00 128.13 ?  341 GLU   B N   1 
ATOM   5467 C CA  . GLU   B 2 37  ? 28.278  32.204  61.323  1.00 134.44 ?  341 GLU   B CA  1 
ATOM   5468 C C   . GLU   B 2 37  ? 27.425  31.330  60.409  1.00 131.13 ?  341 GLU   B C   1 
ATOM   5469 O O   . GLU   B 2 37  ? 27.955  30.581  59.597  1.00 127.68 ?  341 GLU   B O   1 
ATOM   5470 C CB  . GLU   B 2 37  ? 27.968  31.924  62.785  1.00 139.94 ?  341 GLU   B CB  1 
ATOM   5471 C CG  . GLU   B 2 37  ? 28.397  30.545  63.234  1.00 140.68 ?  341 GLU   B CG  1 
ATOM   5472 C CD  . GLU   B 2 37  ? 29.899  30.349  63.196  1.00 140.38 ?  341 GLU   B CD  1 
ATOM   5473 O OE1 . GLU   B 2 37  ? 30.616  31.354  63.058  1.00 136.64 ?  341 GLU   B OE1 1 
ATOM   5474 O OE2 . GLU   B 2 37  ? 30.345  29.194  63.304  1.00 144.58 ?  341 GLU   B OE2 1 
ATOM   5475 N N   . LEU   B 2 38  ? 26.124  31.506  60.512  1.00 131.44 ?  342 LEU   B N   1 
ATOM   5476 C CA  . LEU   B 2 38  ? 25.297  30.651  59.646  1.00 128.00 ?  342 LEU   B CA  1 
ATOM   5477 C C   . LEU   B 2 38  ? 25.730  30.648  58.197  1.00 133.05 ?  342 LEU   B C   1 
ATOM   5478 O O   . LEU   B 2 38  ? 26.099  29.586  57.686  1.00 141.15 ?  342 LEU   B O   1 
ATOM   5479 C CB  . LEU   B 2 38  ? 23.888  31.216  59.747  1.00 130.19 ?  342 LEU   B CB  1 
ATOM   5480 C CG  . LEU   B 2 38  ? 22.810  30.373  59.074  1.00 131.42 ?  342 LEU   B CG  1 
ATOM   5481 C CD1 . LEU   B 2 38  ? 21.498  30.482  59.829  1.00 123.16 ?  342 LEU   B CD1 1 
ATOM   5482 C CD2 . LEU   B 2 38  ? 22.628  30.793  57.626  1.00 135.10 ?  342 LEU   B CD2 1 
ATOM   5483 N N   . VAL   B 2 39  ? 25.722  31.813  57.574  1.00 130.55 ?  343 VAL   B N   1 
ATOM   5484 C CA  . VAL   B 2 39  ? 26.031  31.721  56.150  1.00 130.36 ?  343 VAL   B CA  1 
ATOM   5485 C C   . VAL   B 2 39  ? 27.277  30.877  55.942  1.00 129.21 ?  343 VAL   B C   1 
ATOM   5486 O O   . VAL   B 2 39  ? 27.409  30.201  54.918  1.00 133.55 ?  343 VAL   B O   1 
ATOM   5487 C CB  . VAL   B 2 39  ? 26.177  33.112  55.522  1.00 128.65 ?  343 VAL   B CB  1 
ATOM   5488 C CG1 . VAL   B 2 39  ? 26.855  33.016  54.159  1.00 126.53 ?  343 VAL   B CG1 1 
ATOM   5489 C CG2 . VAL   B 2 39  ? 24.812  33.747  55.408  1.00 131.66 ?  343 VAL   B CG2 1 
ATOM   5490 N N   . SER   B 2 40  ? 28.178  30.857  56.927  1.00 128.60 ?  344 SER   B N   1 
ATOM   5491 C CA  . SER   B 2 40  ? 29.412  30.077  56.835  1.00 132.52 ?  344 SER   B CA  1 
ATOM   5492 C C   . SER   B 2 40  ? 29.149  28.571  56.844  1.00 130.67 ?  344 SER   B C   1 
ATOM   5493 O O   . SER   B 2 40  ? 29.661  27.838  55.992  1.00 133.46 ?  344 SER   B O   1 
ATOM   5494 C CB  . SER   B 2 40  ? 30.346  30.453  57.987  1.00 141.42 ?  344 SER   B CB  1 
ATOM   5495 O OG  . SER   B 2 40  ? 31.357  29.471  58.174  1.00 148.74 ?  344 SER   B OG  1 
ATOM   5496 N N   . VAL   B 2 41  ? 28.414  28.076  57.840  1.00 128.11 ?  345 VAL   B N   1 
ATOM   5497 C CA  . VAL   B 2 41  ? 28.103  26.653  57.848  1.00 125.25 ?  345 VAL   B CA  1 
ATOM   5498 C C   . VAL   B 2 41  ? 27.229  26.297  56.664  1.00 125.82 ?  345 VAL   B C   1 
ATOM   5499 O O   . VAL   B 2 41  ? 27.355  25.210  56.092  1.00 131.30 ?  345 VAL   B O   1 
ATOM   5500 C CB  . VAL   B 2 41  ? 27.457  26.246  59.182  1.00 122.06 ?  345 VAL   B CB  1 
ATOM   5501 C CG1 . VAL   B 2 41  ? 26.671  24.954  59.046  1.00 116.92 ?  345 VAL   B CG1 1 
ATOM   5502 C CG2 . VAL   B 2 41  ? 28.535  26.052  60.214  1.00 129.47 ?  345 VAL   B CG2 1 
ATOM   5503 N N   . LYS   B 2 42  ? 26.357  27.202  56.247  1.00 122.27 ?  346 LYS   B N   1 
ATOM   5504 C CA  . LYS   B 2 42  ? 25.517  26.895  55.105  1.00 124.05 ?  346 LYS   B CA  1 
ATOM   5505 C C   . LYS   B 2 42  ? 26.373  26.618  53.871  1.00 128.35 ?  346 LYS   B C   1 
ATOM   5506 O O   . LYS   B 2 42  ? 26.162  25.621  53.174  1.00 128.62 ?  346 LYS   B O   1 
ATOM   5507 C CB  . LYS   B 2 42  ? 24.529  28.034  54.879  1.00 132.64 ?  346 LYS   B CB  1 
ATOM   5508 C CG  . LYS   B 2 42  ? 23.110  27.540  54.655  1.00 140.66 ?  346 LYS   B CG  1 
ATOM   5509 C CD  . LYS   B 2 42  ? 22.080  28.625  54.937  1.00 141.37 ?  346 LYS   B CD  1 
ATOM   5510 C CE  . LYS   B 2 42  ? 20.708  28.018  55.155  1.00 138.58 ?  346 LYS   B CE  1 
ATOM   5511 N NZ  . LYS   B 2 42  ? 19.929  28.837  56.105  1.00 144.37 ?  346 LYS   B NZ  1 
ATOM   5512 N N   . ARG   B 2 43  ? 27.377  27.468  53.615  1.00 132.94 ?  347 ARG   B N   1 
ATOM   5513 C CA  . ARG   B 2 43  ? 28.358  27.224  52.552  1.00 131.24 ?  347 ARG   B CA  1 
ATOM   5514 C C   . ARG   B 2 43  ? 28.951  25.823  52.649  1.00 128.48 ?  347 ARG   B C   1 
ATOM   5515 O O   . ARG   B 2 43  ? 28.782  24.993  51.750  1.00 131.34 ?  347 ARG   B O   1 
ATOM   5516 C CB  . ARG   B 2 43  ? 29.489  28.255  52.625  1.00 129.58 ?  347 ARG   B CB  1 
ATOM   5517 C CG  . ARG   B 2 43  ? 29.288  29.489  51.792  1.00 136.97 ?  347 ARG   B CG  1 
ATOM   5518 C CD  . ARG   B 2 43  ? 30.472  30.443  51.931  1.00 140.68 ?  347 ARG   B CD  1 
ATOM   5519 N NE  . ARG   B 2 43  ? 30.827  30.980  50.624  1.00 151.91 ?  347 ARG   B NE  1 
ATOM   5520 C CZ  . ARG   B 2 43  ? 30.226  32.016  50.053  1.00 157.24 ?  347 ARG   B CZ  1 
ATOM   5521 N NH1 . ARG   B 2 43  ? 29.259  32.681  50.672  1.00 154.39 ?  347 ARG   B NH1 1 
ATOM   5522 N NH2 . ARG   B 2 43  ? 30.594  32.385  48.826  1.00 155.28 ?  347 ARG   B NH2 1 
ATOM   5523 N N   . GLN   B 2 44  ? 29.669  25.562  53.742  1.00 127.00 ?  348 GLN   B N   1 
ATOM   5524 C CA  . GLN   B 2 44  ? 30.320  24.280  53.982  1.00 127.15 ?  348 GLN   B CA  1 
ATOM   5525 C C   . GLN   B 2 44  ? 29.380  23.090  53.816  1.00 126.02 ?  348 GLN   B C   1 
ATOM   5526 O O   . GLN   B 2 44  ? 29.859  21.972  53.595  1.00 124.73 ?  348 GLN   B O   1 
ATOM   5527 C CB  . GLN   B 2 44  ? 30.933  24.315  55.387  1.00 139.02 ?  348 GLN   B CB  1 
ATOM   5528 C CG  . GLN   B 2 44  ? 31.596  23.034  55.884  1.00 147.65 ?  348 GLN   B CG  1 
ATOM   5529 C CD  . GLN   B 2 44  ? 32.430  23.254  57.158  1.00 159.97 ?  348 GLN   B CD  1 
ATOM   5530 O OE1 . GLN   B 2 44  ? 32.201  24.207  57.932  1.00 152.32 ?  348 GLN   B OE1 1 
ATOM   5531 N NE2 . GLN   B 2 44  ? 33.370  22.340  57.403  1.00 159.45 ?  348 GLN   B NE2 1 
ATOM   5532 N N   . ILE   B 2 45  ? 28.061  23.292  53.904  1.00 125.62 ?  349 ILE   B N   1 
ATOM   5533 C CA  . ILE   B 2 45  ? 27.125  22.225  53.547  1.00 122.90 ?  349 ILE   B CA  1 
ATOM   5534 C C   . ILE   B 2 45  ? 27.147  21.976  52.047  1.00 126.21 ?  349 ILE   B C   1 
ATOM   5535 O O   . ILE   B 2 45  ? 27.482  20.876  51.605  1.00 133.77 ?  349 ILE   B O   1 
ATOM   5536 C CB  . ILE   B 2 45  ? 25.702  22.530  54.042  1.00 122.94 ?  349 ILE   B CB  1 
ATOM   5537 C CG1 . ILE   B 2 45  ? 25.546  22.090  55.490  1.00 118.18 ?  349 ILE   B CG1 1 
ATOM   5538 C CG2 . ILE   B 2 45  ? 24.656  21.833  53.175  1.00 121.36 ?  349 ILE   B CG2 1 
ATOM   5539 C CD1 . ILE   B 2 45  ? 24.237  22.465  56.093  1.00 124.95 ?  349 ILE   B CD1 1 
ATOM   5540 N N   . GLN   B 2 46  ? 26.803  22.985  51.237  1.00 125.73 ?  350 GLN   B N   1 
ATOM   5541 C CA  . GLN   B 2 46  ? 26.751  22.747  49.796  1.00 128.03 ?  350 GLN   B CA  1 
ATOM   5542 C C   . GLN   B 2 46  ? 28.083  22.273  49.222  1.00 132.36 ?  350 GLN   B C   1 
ATOM   5543 O O   . GLN   B 2 46  ? 28.092  21.590  48.191  1.00 134.40 ?  350 GLN   B O   1 
ATOM   5544 C CB  . GLN   B 2 46  ? 26.270  23.988  49.051  1.00 127.54 ?  350 GLN   B CB  1 
ATOM   5545 C CG  . GLN   B 2 46  ? 24.808  23.862  48.652  1.00 133.51 ?  350 GLN   B CG  1 
ATOM   5546 C CD  . GLN   B 2 46  ? 24.105  25.195  48.491  1.00 147.88 ?  350 GLN   B CD  1 
ATOM   5547 O OE1 . GLN   B 2 46  ? 24.649  26.247  48.834  1.00 154.15 ?  350 GLN   B OE1 1 
ATOM   5548 N NE2 . GLN   B 2 46  ? 22.884  25.157  47.960  1.00 142.75 ?  350 GLN   B NE2 1 
ATOM   5549 N N   . ASN   B 2 47  ? 29.199  22.585  49.873  1.00 131.30 ?  351 ASN   B N   1 
ATOM   5550 C CA  . ASN   B 2 47  ? 30.486  22.026  49.482  1.00 128.14 ?  351 ASN   B CA  1 
ATOM   5551 C C   . ASN   B 2 47  ? 30.491  20.506  49.647  1.00 129.03 ?  351 ASN   B C   1 
ATOM   5552 O O   . ASN   B 2 47  ? 30.522  19.770  48.660  1.00 132.38 ?  351 ASN   B O   1 
ATOM   5553 C CB  . ASN   B 2 47  ? 31.593  22.671  50.310  1.00 130.81 ?  351 ASN   B CB  1 
ATOM   5554 C CG  . ASN   B 2 47  ? 32.925  22.643  49.619  1.00 134.67 ?  351 ASN   B CG  1 
ATOM   5555 O OD1 . ASN   B 2 47  ? 33.739  21.733  49.829  1.00 135.01 ?  351 ASN   B OD1 1 
ATOM   5556 N ND2 . ASN   B 2 47  ? 33.165  23.648  48.782  1.00 132.30 ?  351 ASN   B ND2 1 
ATOM   5557 N N   . ILE   B 2 48  ? 30.446  20.026  50.891  1.00 125.82 ?  352 ILE   B N   1 
ATOM   5558 C CA  . ILE   B 2 48  ? 30.392  18.595  51.182  1.00 122.25 ?  352 ILE   B CA  1 
ATOM   5559 C C   . ILE   B 2 48  ? 29.171  17.893  50.589  1.00 125.33 ?  352 ILE   B C   1 
ATOM   5560 O O   . ILE   B 2 48  ? 29.218  16.688  50.328  1.00 125.09 ?  352 ILE   B O   1 
ATOM   5561 C CB  . ILE   B 2 48  ? 30.476  18.441  52.712  1.00 120.71 ?  352 ILE   B CB  1 
ATOM   5562 C CG1 . ILE   B 2 48  ? 31.846  18.921  53.169  1.00 128.34 ?  352 ILE   B CG1 1 
ATOM   5563 C CG2 . ILE   B 2 48  ? 30.121  17.037  53.199  1.00 120.63 ?  352 ILE   B CG2 1 
ATOM   5564 C CD1 . ILE   B 2 48  ? 32.293  18.295  54.416  1.00 126.41 ?  352 ILE   B CD1 1 
ATOM   5565 N N   . LYS   B 2 49  ? 28.072  18.613  50.362  1.00 130.50 ?  353 LYS   B N   1 
ATOM   5566 C CA  . LYS   B 2 49  ? 26.913  18.021  49.702  1.00 128.84 ?  353 LYS   B CA  1 
ATOM   5567 C C   . LYS   B 2 49  ? 27.219  17.734  48.240  1.00 129.18 ?  353 LYS   B C   1 
ATOM   5568 O O   . LYS   B 2 49  ? 26.493  16.968  47.595  1.00 131.90 ?  353 LYS   B O   1 
ATOM   5569 C CB  . LYS   B 2 49  ? 25.713  18.969  49.852  1.00 130.51 ?  353 LYS   B CB  1 
ATOM   5570 C CG  . LYS   B 2 49  ? 24.288  18.441  49.592  1.00 134.57 ?  353 LYS   B CG  1 
ATOM   5571 C CD  . LYS   B 2 49  ? 23.278  19.557  49.982  1.00 137.47 ?  353 LYS   B CD  1 
ATOM   5572 C CE  . LYS   B 2 49  ? 21.806  19.246  49.710  1.00 138.12 ?  353 LYS   B CE  1 
ATOM   5573 N NZ  . LYS   B 2 49  ? 20.954  19.545  50.898  1.00 135.01 ?  353 LYS   B NZ  1 
ATOM   5574 N N   . GLN   B 2 50  ? 28.301  18.316  47.728  1.00 127.26 ?  354 GLN   B N   1 
ATOM   5575 C CA  . GLN   B 2 50  ? 28.791  18.163  46.363  1.00 131.17 ?  354 GLN   B CA  1 
ATOM   5576 C C   . GLN   B 2 50  ? 29.926  17.153  46.258  1.00 127.82 ?  354 GLN   B C   1 
ATOM   5577 O O   . GLN   B 2 50  ? 29.898  16.268  45.401  1.00 125.96 ?  354 GLN   B O   1 
ATOM   5578 C CB  . GLN   B 2 50  ? 29.274  19.520  45.849  1.00 134.58 ?  354 GLN   B CB  1 
ATOM   5579 C CG  . GLN   B 2 50  ? 29.610  19.540  44.394  1.00 138.08 ?  354 GLN   B CG  1 
ATOM   5580 C CD  . GLN   B 2 50  ? 28.594  20.311  43.608  1.00 144.66 ?  354 GLN   B CD  1 
ATOM   5581 O OE1 . GLN   B 2 50  ? 28.354  21.500  43.877  1.00 139.99 ?  354 GLN   B OE1 1 
ATOM   5582 N NE2 . GLN   B 2 50  ? 27.978  19.646  42.627  1.00 146.40 ?  354 GLN   B NE2 1 
ATOM   5583 N N   . THR   B 2 51  ? 30.954  17.314  47.090  1.00 129.21 ?  355 THR   B N   1 
ATOM   5584 C CA  . THR   B 2 51  ? 31.997  16.315  47.290  1.00 128.93 ?  355 THR   B CA  1 
ATOM   5585 C C   . THR   B 2 51  ? 31.358  14.938  47.438  1.00 125.26 ?  355 THR   B C   1 
ATOM   5586 O O   . THR   B 2 51  ? 31.836  13.959  46.860  1.00 126.34 ?  355 THR   B O   1 
ATOM   5587 C CB  . THR   B 2 51  ? 32.853  16.671  48.525  1.00 129.76 ?  355 THR   B CB  1 
ATOM   5588 O OG1 . THR   B 2 51  ? 33.731  17.777  48.228  1.00 126.41 ?  355 THR   B OG1 1 
ATOM   5589 C CG2 . THR   B 2 51  ? 33.660  15.462  49.013  1.00 125.81 ?  355 THR   B CG2 1 
ATOM   5590 N N   . ASN   B 2 52  ? 30.253  14.862  48.185  1.00 126.24 ?  356 ASN   B N   1 
ATOM   5591 C CA  . ASN   B 2 52  ? 29.530  13.609  48.341  1.00 122.81 ?  356 ASN   B CA  1 
ATOM   5592 C C   . ASN   B 2 52  ? 28.644  13.279  47.157  1.00 123.71 ?  356 ASN   B C   1 
ATOM   5593 O O   . ASN   B 2 52  ? 28.223  12.130  47.030  1.00 126.16 ?  356 ASN   B O   1 
ATOM   5594 C CB  . ASN   B 2 52  ? 28.671  13.626  49.600  1.00 120.81 ?  356 ASN   B CB  1 
ATOM   5595 C CG  . ASN   B 2 52  ? 29.473  13.373  50.832  1.00 119.24 ?  356 ASN   B CG  1 
ATOM   5596 O OD1 . ASN   B 2 52  ? 30.690  13.548  50.841  1.00 117.34 ?  356 ASN   B OD1 1 
ATOM   5597 N ND2 . ASN   B 2 52  ? 28.811  12.911  51.871  1.00 119.14 ?  356 ASN   B ND2 1 
ATOM   5598 N N   . SER   B 2 53  ? 28.326  14.241  46.301  1.00 124.68 ?  357 SER   B N   1 
ATOM   5599 C CA  . SER   B 2 53  ? 27.557  13.872  45.122  1.00 126.77 ?  357 SER   B CA  1 
ATOM   5600 C C   . SER   B 2 53  ? 28.453  13.213  44.077  1.00 129.03 ?  357 SER   B C   1 
ATOM   5601 O O   . SER   B 2 53  ? 28.008  12.300  43.369  1.00 131.59 ?  357 SER   B O   1 
ATOM   5602 C CB  . SER   B 2 53  ? 26.838  15.103  44.557  1.00 129.41 ?  357 SER   B CB  1 
ATOM   5603 O OG  . SER   B 2 53  ? 25.849  14.737  43.609  1.00 127.01 ?  357 SER   B OG  1 
ATOM   5604 N N   . ALA   B 2 54  ? 29.723  13.630  43.994  1.00 127.42 ?  358 ALA   B N   1 
ATOM   5605 C CA  . ALA   B 2 54  ? 30.660  13.019  43.056  1.00 127.80 ?  358 ALA   B CA  1 
ATOM   5606 C C   . ALA   B 2 54  ? 31.124  11.652  43.537  1.00 127.51 ?  358 ALA   B C   1 
ATOM   5607 O O   . ALA   B 2 54  ? 31.221  10.717  42.735  1.00 127.48 ?  358 ALA   B O   1 
ATOM   5608 C CB  . ALA   B 2 54  ? 31.859  13.936  42.833  1.00 123.53 ?  358 ALA   B CB  1 
ATOM   5609 N N   . LEU   B 2 55  ? 31.428  11.527  44.834  1.00 123.80 ?  359 LEU   B N   1 
ATOM   5610 C CA  . LEU   B 2 55  ? 31.718  10.214  45.403  1.00 125.81 ?  359 LEU   B CA  1 
ATOM   5611 C C   . LEU   B 2 55  ? 30.540  9.263   45.255  1.00 132.65 ?  359 LEU   B C   1 
ATOM   5612 O O   . LEU   B 2 55  ? 30.736  8.048   45.135  1.00 136.38 ?  359 LEU   B O   1 
ATOM   5613 C CB  . LEU   B 2 55  ? 32.088  10.312  46.884  1.00 119.99 ?  359 LEU   B CB  1 
ATOM   5614 C CG  . LEU   B 2 55  ? 33.277  11.139  47.359  1.00 123.00 ?  359 LEU   B CG  1 
ATOM   5615 C CD1 . LEU   B 2 55  ? 33.787  10.521  48.640  1.00 115.15 ?  359 LEU   B CD1 1 
ATOM   5616 C CD2 . LEU   B 2 55  ? 34.383  11.281  46.309  1.00 123.20 ?  359 LEU   B CD2 1 
ATOM   5617 N N   . LYS   B 2 56  ? 29.311  9.780   45.286  1.00 136.77 ?  360 LYS   B N   1 
ATOM   5618 C CA  . LYS   B 2 56  ? 28.153  8.902   45.141  1.00 138.54 ?  360 LYS   B CA  1 
ATOM   5619 C C   . LYS   B 2 56  ? 28.097  8.307   43.741  1.00 140.77 ?  360 LYS   B C   1 
ATOM   5620 O O   . LYS   B 2 56  ? 27.632  7.172   43.568  1.00 142.64 ?  360 LYS   B O   1 
ATOM   5621 C CB  . LYS   B 2 56  ? 26.857  9.665   45.474  1.00 141.54 ?  360 LYS   B CB  1 
ATOM   5622 C CG  . LYS   B 2 56  ? 26.018  9.101   46.650  1.00 135.04 ?  360 LYS   B CG  1 
ATOM   5623 C CD  . LYS   B 2 56  ? 24.706  9.893   46.852  1.00 134.22 ?  360 LYS   B CD  1 
ATOM   5624 C CE  . LYS   B 2 56  ? 23.661  9.619   45.771  1.00 133.61 ?  360 LYS   B CE  1 
ATOM   5625 N NZ  . LYS   B 2 56  ? 22.481  10.529  45.887  1.00 131.43 ?  360 LYS   B NZ  1 
ATOM   5626 N N   . GLU   B 2 57  ? 28.607  9.031   42.739  1.00 139.02 ?  361 GLU   B N   1 
ATOM   5627 C CA  . GLU   B 2 57  ? 28.523  8.557   41.365  1.00 142.40 ?  361 GLU   B CA  1 
ATOM   5628 C C   . GLU   B 2 57  ? 29.663  7.632   40.966  1.00 141.58 ?  361 GLU   B C   1 
ATOM   5629 O O   . GLU   B 2 57  ? 29.484  6.811   40.060  1.00 139.47 ?  361 GLU   B O   1 
ATOM   5630 C CB  . GLU   B 2 57  ? 28.472  9.733   40.405  1.00 140.74 ?  361 GLU   B CB  1 
ATOM   5631 C CG  . GLU   B 2 57  ? 27.486  9.486   39.310  1.00 148.17 ?  361 GLU   B CG  1 
ATOM   5632 C CD  . GLU   B 2 57  ? 27.831  10.242  38.062  1.00 160.80 ?  361 GLU   B CD  1 
ATOM   5633 O OE1 . GLU   B 2 57  ? 28.328  11.386  38.188  1.00 165.36 ?  361 GLU   B OE1 1 
ATOM   5634 O OE2 . GLU   B 2 57  ? 27.593  9.701   36.960  1.00 161.72 ?  361 GLU   B OE2 1 
ATOM   5635 N N   . LYS   B 2 58  ? 30.831  7.743   41.611  1.00 141.83 ?  362 LYS   B N   1 
ATOM   5636 C CA  . LYS   B 2 58  ? 31.895  6.764   41.396  1.00 138.61 ?  362 LYS   B CA  1 
ATOM   5637 C C   . LYS   B 2 58  ? 31.486  5.369   41.871  1.00 141.06 ?  362 LYS   B C   1 
ATOM   5638 O O   . LYS   B 2 58  ? 31.911  4.363   41.286  1.00 142.37 ?  362 LYS   B O   1 
ATOM   5639 C CB  . LYS   B 2 58  ? 33.187  7.219   42.087  1.00 126.45 ?  362 LYS   B CB  1 
ATOM   5640 C CG  . LYS   B 2 58  ? 33.972  8.238   41.276  1.00 128.89 ?  362 LYS   B CG  1 
ATOM   5641 C CD  . LYS   B 2 58  ? 34.933  9.051   42.131  1.00 136.44 ?  362 LYS   B CD  1 
ATOM   5642 C CE  . LYS   B 2 58  ? 35.194  10.440  41.526  1.00 141.17 ?  362 LYS   B CE  1 
ATOM   5643 N NZ  . LYS   B 2 58  ? 36.515  11.009  41.948  1.00 142.10 ?  362 LYS   B NZ  1 
ATOM   5644 N N   . LEU   B 2 59  ? 30.550  5.323   42.799  1.00 134.37 ?  363 LEU   B N   1 
ATOM   5645 C CA  . LEU   B 2 59  ? 30.125  4.005   43.302  1.00 134.59 ?  363 LEU   B CA  1 
ATOM   5646 C C   . LEU   B 2 59  ? 28.999  3.492   42.412  1.00 142.41 ?  363 LEU   B C   1 
ATOM   5647 O O   . LEU   B 2 59  ? 28.308  2.550   42.813  1.00 144.49 ?  363 LEU   B O   1 
ATOM   5648 C CB  . LEU   B 2 59  ? 29.696  4.157   44.756  1.00 131.29 ?  363 LEU   B CB  1 
ATOM   5649 C CG  . LEU   B 2 59  ? 30.813  4.563   45.711  1.00 127.83 ?  363 LEU   B CG  1 
ATOM   5650 C CD1 . LEU   B 2 59  ? 30.239  5.155   46.983  1.00 135.17 ?  363 LEU   B CD1 1 
ATOM   5651 C CD2 . LEU   B 2 59  ? 31.699  3.376   46.036  1.00 121.13 ?  363 LEU   B CD2 1 
ATOM   5652 N N   . ASP   B 2 60  ? 28.817  4.095   41.246  1.00 144.21 ?  364 ASP   B N   1 
ATOM   5653 C CA  . ASP   B 2 60  ? 27.833  3.560   40.315  1.00 149.55 ?  364 ASP   B CA  1 
ATOM   5654 C C   . ASP   B 2 60  ? 28.116  2.109   39.952  1.00 152.11 ?  364 ASP   B C   1 
ATOM   5655 O O   . ASP   B 2 60  ? 29.267  1.709   39.740  1.00 154.08 ?  364 ASP   B O   1 
ATOM   5656 C CB  . ASP   B 2 60  ? 27.777  4.359   39.029  1.00 152.50 ?  364 ASP   B CB  1 
ATOM   5657 C CG  . ASP   B 2 60  ? 26.672  3.871   38.133  1.00 158.73 ?  364 ASP   B CG  1 
ATOM   5658 O OD1 . ASP   B 2 60  ? 25.495  3.898   38.573  1.00 159.32 ?  364 ASP   B OD1 1 
ATOM   5659 O OD2 . ASP   B 2 60  ? 26.998  3.386   37.025  1.00 156.71 ?  364 ASP   B OD2 1 
ATOM   5660 N N   . GLY   B 2 61  ? 27.040  1.338   39.817  1.00 150.59 ?  365 GLY   B N   1 
ATOM   5661 C CA  . GLY   B 2 61  ? 27.124  -0.086  39.629  1.00 152.13 ?  365 GLY   B CA  1 
ATOM   5662 C C   . GLY   B 2 61  ? 27.178  -0.874  40.915  1.00 143.30 ?  365 GLY   B C   1 
ATOM   5663 O O   . GLY   B 2 61  ? 26.784  -2.047  40.925  1.00 141.00 ?  365 GLY   B O   1 
ATOM   5664 N N   . GLY   B 2 62  ? 27.736  -0.275  41.951  1.00 141.86 ?  366 GLY   B N   1 
ATOM   5665 C CA  . GLY   B 2 62  ? 27.909  -1.061  43.176  1.00 139.37 ?  366 GLY   B CA  1 
ATOM   5666 C C   . GLY   B 2 62  ? 28.805  -2.244  42.898  1.00 134.88 ?  366 GLY   B C   1 
ATOM   5667 O O   . GLY   B 2 62  ? 29.320  -2.341  41.786  1.00 133.28 ?  366 GLY   B O   1 
ATOM   5668 N N   . ILE   B 2 63  ? 28.979  -3.106  43.885  1.00 125.43 ?  367 ILE   B N   1 
ATOM   5669 C CA  . ILE   B 2 63  ? 29.810  -4.310  43.694  1.00 125.42 ?  367 ILE   B CA  1 
ATOM   5670 C C   . ILE   B 2 63  ? 28.869  -5.421  43.262  1.00 132.27 ?  367 ILE   B C   1 
ATOM   5671 O O   . ILE   B 2 63  ? 28.531  -6.268  44.086  1.00 134.12 ?  367 ILE   B O   1 
ATOM   5672 C CB  . ILE   B 2 63  ? 30.542  -4.641  44.999  1.00 118.74 ?  367 ILE   B CB  1 
ATOM   5673 C CG1 . ILE   B 2 63  ? 29.578  -4.819  46.172  1.00 121.57 ?  367 ILE   B CG1 1 
ATOM   5674 C CG2 . ILE   B 2 63  ? 31.586  -3.581  45.296  1.00 114.83 ?  367 ILE   B CG2 1 
ATOM   5675 C CD1 . ILE   B 2 63  ? 29.996  -5.904  47.131  1.00 122.12 ?  367 ILE   B CD1 1 
ATOM   5676 N N   . GLU   B 2 64  ? 28.442  -5.395  42.011  1.00 135.25 ?  368 GLU   B N   1 
ATOM   5677 C CA  . GLU   B 2 64  ? 27.602  -6.514  41.532  1.00 138.51 ?  368 GLU   B CA  1 
ATOM   5678 C C   . GLU   B 2 64  ? 27.926  -7.030  40.142  1.00 131.51 ?  368 GLU   B C   1 
ATOM   5679 O O   . GLU   B 2 64  ? 27.060  -7.642  39.515  1.00 126.14 ?  368 GLU   B O   1 
ATOM   5680 C CB  . GLU   B 2 64  ? 26.259  -6.006  41.023  1.00 137.09 ?  368 GLU   B CB  1 
ATOM   5681 C CG  . GLU   B 2 64  ? 25.447  -5.284  42.076  1.00 140.55 ?  368 GLU   B CG  1 
ATOM   5682 C CD  . GLU   B 2 64  ? 25.411  -5.998  43.414  1.00 142.36 ?  368 GLU   B CD  1 
ATOM   5683 O OE1 . GLU   B 2 64  ? 24.869  -7.113  43.470  1.00 139.97 ?  368 GLU   B OE1 1 
ATOM   5684 O OE2 . GLU   B 2 64  ? 25.934  -5.437  44.391  1.00 137.95 ?  368 GLU   B OE2 1 
ATOM   5685 N N   . PRO   B 2 65  ? 29.140  -6.798  39.637  1.00 131.75 ?  369 PRO   B N   1 
ATOM   5686 C CA  . PRO   B 2 65  ? 29.514  -7.357  38.375  1.00 131.49 ?  369 PRO   B CA  1 
ATOM   5687 C C   . PRO   B 2 65  ? 30.797  -7.892  39.024  1.00 126.29 ?  369 PRO   B C   1 
ATOM   5688 O O   . PRO   B 2 65  ? 31.718  -8.179  38.331  1.00 128.41 ?  369 PRO   B O   1 
ATOM   5689 C CB  . PRO   B 2 65  ? 29.907  -6.230  37.429  1.00 130.41 ?  369 PRO   B CB  1 
ATOM   5690 C CG  . PRO   B 2 65  ? 29.057  -5.072  37.865  1.00 132.63 ?  369 PRO   B CG  1 
ATOM   5691 C CD  . PRO   B 2 65  ? 29.030  -5.219  39.366  1.00 135.35 ?  369 PRO   B CD  1 
ATOM   5692 N N   . TYR   B 2 66  ? 30.806  -7.977  40.344  1.00 123.66 ?  370 TYR   B N   1 
ATOM   5693 C CA  . TYR   B 2 66  ? 32.018  -8.367  41.045  1.00 119.61 ?  370 TYR   B CA  1 
ATOM   5694 C C   . TYR   B 2 66  ? 31.731  -9.408  42.114  1.00 119.87 ?  370 TYR   B C   1 
ATOM   5695 O O   . TYR   B 2 66  ? 32.647  -9.786  42.850  1.00 120.04 ?  370 TYR   B O   1 
ATOM   5696 C CB  . TYR   B 2 66  ? 32.740  -7.161  41.659  1.00 121.02 ?  370 TYR   B CB  1 
ATOM   5697 C CG  . TYR   B 2 66  ? 33.127  -6.076  40.653  1.00 126.17 ?  370 TYR   B CG  1 
ATOM   5698 C CD1 . TYR   B 2 66  ? 32.170  -5.269  40.038  1.00 128.95 ?  370 TYR   B CD1 1 
ATOM   5699 C CD2 . TYR   B 2 66  ? 34.451  -5.836  40.343  1.00 123.66 ?  370 TYR   B CD2 1 
ATOM   5700 C CE1 . TYR   B 2 66  ? 32.534  -4.288  39.123  1.00 127.71 ?  370 TYR   B CE1 1 
ATOM   5701 C CE2 . TYR   B 2 66  ? 34.807  -4.862  39.434  1.00 118.80 ?  370 TYR   B CE2 1 
ATOM   5702 C CZ  . TYR   B 2 66  ? 33.862  -4.087  38.838  1.00 122.47 ?  370 TYR   B CZ  1 
ATOM   5703 O OH  . TYR   B 2 66  ? 34.259  -3.117  37.945  1.00 126.60 ?  370 TYR   B OH  1 
ATOM   5704 N N   . ARG   B 2 67  ? 30.503  -9.894  42.217  1.00 118.03 ?  371 ARG   B N   1 
ATOM   5705 C CA  . ARG   B 2 67  ? 30.237  -10.937 43.187  1.00 123.67 ?  371 ARG   B CA  1 
ATOM   5706 C C   . ARG   B 2 67  ? 30.454  -12.321 42.609  1.00 130.49 ?  371 ARG   B C   1 
ATOM   5707 O O   . ARG   B 2 67  ? 30.305  -12.552 41.406  1.00 132.00 ?  371 ARG   B O   1 
ATOM   5708 C CB  . ARG   B 2 67  ? 28.820  -10.850 43.733  1.00 131.77 ?  371 ARG   B CB  1 
ATOM   5709 C CG  . ARG   B 2 67  ? 28.773  -10.243 45.113  1.00 137.23 ?  371 ARG   B CG  1 
ATOM   5710 C CD  . ARG   B 2 67  ? 27.426  -10.434 45.782  1.00 135.82 ?  371 ARG   B CD  1 
ATOM   5711 N NE  . ARG   B 2 67  ? 27.230  -9.425  46.815  1.00 143.19 ?  371 ARG   B NE  1 
ATOM   5712 C CZ  . ARG   B 2 67  ? 26.874  -8.167  46.569  1.00 146.16 ?  371 ARG   B CZ  1 
ATOM   5713 N NH1 . ARG   B 2 67  ? 26.659  -7.735  45.332  1.00 141.05 ?  371 ARG   B NH1 1 
ATOM   5714 N NH2 . ARG   B 2 67  ? 26.742  -7.316  47.586  1.00 137.83 ?  371 ARG   B NH2 1 
ATOM   5715 N N   . LEU   B 2 68  ? 30.798  -13.246 43.497  1.00 133.83 ?  372 LEU   B N   1 
ATOM   5716 C CA  . LEU   B 2 68  ? 30.868  -14.663 43.190  1.00 138.06 ?  372 LEU   B CA  1 
ATOM   5717 C C   . LEU   B 2 68  ? 29.808  -15.405 43.974  1.00 142.72 ?  372 LEU   B C   1 
ATOM   5718 O O   . LEU   B 2 68  ? 29.670  -15.176 45.184  1.00 146.38 ?  372 LEU   B O   1 
ATOM   5719 C CB  . LEU   B 2 68  ? 32.241  -15.238 43.529  1.00 136.30 ?  372 LEU   B CB  1 
ATOM   5720 C CG  . LEU   B 2 68  ? 33.417  -14.334 43.190  1.00 133.50 ?  372 LEU   B CG  1 
ATOM   5721 C CD1 . LEU   B 2 68  ? 34.642  -14.814 43.956  1.00 124.94 ?  372 LEU   B CD1 1 
ATOM   5722 C CD2 . LEU   B 2 68  ? 33.657  -14.290 41.666  1.00 120.88 ?  372 LEU   B CD2 1 
ATOM   5723 N N   . PRO   B 2 69  ? 29.052  -16.290 43.325  1.00 143.44 ?  373 PRO   B N   1 
ATOM   5724 C CA  . PRO   B 2 69  ? 27.991  -17.031 44.021  1.00 147.48 ?  373 PRO   B CA  1 
ATOM   5725 C C   . PRO   B 2 69  ? 28.467  -17.843 45.224  1.00 154.29 ?  373 PRO   B C   1 
ATOM   5726 O O   . PRO   B 2 69  ? 29.669  -17.929 45.507  1.00 150.90 ?  373 PRO   B O   1 
ATOM   5727 C CB  . PRO   B 2 69  ? 27.421  -17.935 42.918  1.00 143.88 ?  373 PRO   B CB  1 
ATOM   5728 C CG  . PRO   B 2 69  ? 28.244  -17.659 41.673  1.00 136.15 ?  373 PRO   B CG  1 
ATOM   5729 C CD  . PRO   B 2 69  ? 28.911  -16.360 41.864  1.00 137.03 ?  373 PRO   B CD  1 
ATOM   5730 N N   . GLU   B 2 70  ? 27.508  -18.450 45.929  1.00 159.42 ?  374 GLU   B N   1 
ATOM   5731 C CA  . GLU   B 2 70  ? 27.736  -19.057 47.236  1.00 165.95 ?  374 GLU   B CA  1 
ATOM   5732 C C   . GLU   B 2 70  ? 28.192  -20.510 47.087  1.00 170.67 ?  374 GLU   B C   1 
ATOM   5733 O O   . GLU   B 2 70  ? 27.553  -21.304 46.384  1.00 164.87 ?  374 GLU   B O   1 
ATOM   5734 C CB  . GLU   B 2 70  ? 26.451  -18.984 48.070  1.00 168.48 ?  374 GLU   B CB  1 
ATOM   5735 C CG  . GLU   B 2 70  ? 26.612  -18.865 49.599  1.00 173.34 ?  374 GLU   B CG  1 
ATOM   5736 C CD  . GLU   B 2 70  ? 27.486  -17.691 50.078  1.00 181.02 ?  374 GLU   B CD  1 
ATOM   5737 O OE1 . GLU   B 2 70  ? 27.872  -16.813 49.271  1.00 178.55 ?  374 GLU   B OE1 1 
ATOM   5738 O OE2 . GLU   B 2 70  ? 27.777  -17.640 51.293  1.00 183.40 ?  374 GLU   B OE2 1 
ATOM   5739 N N   . VAL   B 2 71  ? 29.296  -20.849 47.751  1.00 173.24 ?  375 VAL   B N   1 
ATOM   5740 C CA  . VAL   B 2 71  ? 29.808  -22.238 47.757  1.00 175.53 ?  375 VAL   B CA  1 
ATOM   5741 C C   . VAL   B 2 71  ? 29.170  -22.913 48.967  1.00 179.66 ?  375 VAL   B C   1 
ATOM   5742 O O   . VAL   B 2 71  ? 29.742  -23.002 50.061  1.00 180.42 ?  375 VAL   B O   1 
ATOM   5743 C CB  . VAL   B 2 71  ? 31.343  -22.295 47.792  1.00 174.84 ?  375 VAL   B CB  1 
ATOM   5744 C CG1 . VAL   B 2 71  ? 31.842  -23.736 47.623  1.00 171.73 ?  375 VAL   B CG1 1 
ATOM   5745 C CG2 . VAL   B 2 71  ? 31.957  -21.378 46.746  1.00 160.59 ?  375 VAL   B CG2 1 
ATOM   5746 N N   . ILE   B 2 72  ? 27.949  -23.411 48.768  1.00 177.80 ?  376 ILE   B N   1 
ATOM   5747 C CA  . ILE   B 2 72  ? 27.179  -23.955 49.882  1.00 177.87 ?  376 ILE   B CA  1 
ATOM   5748 C C   . ILE   B 2 72  ? 27.571  -25.415 50.052  1.00 174.67 ?  376 ILE   B C   1 
ATOM   5749 O O   . ILE   B 2 72  ? 26.735  -26.309 49.892  1.00 172.72 ?  376 ILE   B O   1 
ATOM   5750 C CB  . ILE   B 2 72  ? 25.662  -23.826 49.643  1.00 178.06 ?  376 ILE   B CB  1 
ATOM   5751 C CG1 . ILE   B 2 72  ? 25.304  -22.423 49.147  1.00 179.85 ?  376 ILE   B CG1 1 
ATOM   5752 C CG2 . ILE   B 2 72  ? 24.903  -24.079 50.945  1.00 172.93 ?  376 ILE   B CG2 1 
ATOM   5753 C CD1 . ILE   B 2 72  ? 24.968  -22.375 47.655  1.00 172.43 ?  376 ILE   B CD1 1 
ATOM   5754 N N   . GLN   B 2 73  ? 28.840  -25.679 50.351  1.00 176.19 ?  377 GLN   B N   1 
ATOM   5755 C CA  . GLN   B 2 73  ? 29.354  -27.044 50.316  1.00 173.82 ?  377 GLN   B CA  1 
ATOM   5756 C C   . GLN   B 2 73  ? 29.349  -27.642 51.715  1.00 169.87 ?  377 GLN   B C   1 
ATOM   5757 O O   . GLN   B 2 73  ? 29.775  -26.994 52.681  1.00 165.94 ?  377 GLN   B O   1 
ATOM   5758 C CB  . GLN   B 2 73  ? 30.750  -27.106 49.688  1.00 173.00 ?  377 GLN   B CB  1 
ATOM   5759 C CG  . GLN   B 2 73  ? 31.908  -26.531 50.488  1.00 168.25 ?  377 GLN   B CG  1 
ATOM   5760 C CD  . GLN   B 2 73  ? 33.232  -27.119 50.022  1.00 164.83 ?  377 GLN   B CD  1 
ATOM   5761 O OE1 . GLN   B 2 73  ? 33.391  -28.348 49.966  1.00 160.38 ?  377 GLN   B OE1 1 
ATOM   5762 N NE2 . GLN   B 2 73  ? 34.173  -26.251 49.643  1.00 157.90 ?  377 GLN   B NE2 1 
ATOM   5763 N N   . LYS   B 2 74  ? 28.863  -28.882 51.806  1.00 167.61 ?  378 LYS   B N   1 
ATOM   5764 C CA  . LYS   B 2 74  ? 28.495  -29.470 53.088  1.00 165.83 ?  378 LYS   B CA  1 
ATOM   5765 C C   . LYS   B 2 74  ? 29.740  -29.880 53.864  1.00 160.01 ?  378 LYS   B C   1 
ATOM   5766 O O   . LYS   B 2 74  ? 30.679  -30.456 53.305  1.00 159.19 ?  378 LYS   B O   1 
ATOM   5767 C CB  . LYS   B 2 74  ? 27.560  -30.665 52.877  1.00 160.46 ?  378 LYS   B CB  1 
ATOM   5768 C CG  . LYS   B 2 74  ? 26.135  -30.272 52.441  1.00 154.64 ?  378 LYS   B CG  1 
ATOM   5769 C CD  . LYS   B 2 74  ? 25.106  -31.320 52.858  1.00 154.72 ?  378 LYS   B CD  1 
ATOM   5770 C CE  . LYS   B 2 74  ? 23.704  -31.005 52.332  1.00 150.91 ?  378 LYS   B CE  1 
ATOM   5771 N NZ  . LYS   B 2 74  ? 22.723  -32.103 52.645  1.00 147.66 ?  378 LYS   B NZ  1 
ATOM   5772 N N   . CYS   B 2 75  ? 29.731  -29.580 55.159  1.00 156.83 ?  379 CYS   B N   1 
ATOM   5773 C CA  . CYS   B 2 75  ? 30.921  -29.664 55.996  1.00 154.31 ?  379 CYS   B CA  1 
ATOM   5774 C C   . CYS   B 2 75  ? 31.258  -31.125 56.299  1.00 155.13 ?  379 CYS   B C   1 
ATOM   5775 O O   . CYS   B 2 75  ? 30.441  -31.847 56.879  1.00 159.55 ?  379 CYS   B O   1 
ATOM   5776 C CB  . CYS   B 2 75  ? 30.673  -28.875 57.280  1.00 152.26 ?  379 CYS   B CB  1 
ATOM   5777 S SG  . CYS   B 2 75  ? 32.118  -28.138 58.042  1.00 153.98 ?  379 CYS   B SG  1 
ATOM   5778 N N   . ASN   B 2 76  ? 32.460  -31.563 55.919  1.00 155.85 ?  380 ASN   B N   1 
ATOM   5779 C CA  . ASN   B 2 76  ? 32.863  -32.962 56.014  1.00 152.64 ?  380 ASN   B CA  1 
ATOM   5780 C C   . ASN   B 2 76  ? 33.683  -33.208 57.286  1.00 149.90 ?  380 ASN   B C   1 
ATOM   5781 O O   . ASN   B 2 76  ? 33.685  -32.389 58.215  1.00 148.26 ?  380 ASN   B O   1 
ATOM   5782 C CB  . ASN   B 2 76  ? 33.638  -33.372 54.752  1.00 149.64 ?  380 ASN   B CB  1 
ATOM   5783 C CG  . ASN   B 2 76  ? 33.680  -34.880 54.559  1.00 150.65 ?  380 ASN   B CG  1 
ATOM   5784 O OD1 . ASN   B 2 76  ? 34.458  -35.577 55.219  1.00 147.61 ?  380 ASN   B OD1 1 
ATOM   5785 N ND2 . ASN   B 2 76  ? 32.848  -35.390 53.649  1.00 148.51 ?  380 ASN   B ND2 1 
ATOM   5786 N N   . ALA   B 2 77  ? 34.397  -34.336 57.324  1.00 145.91 ?  381 ALA   B N   1 
ATOM   5787 C CA  . ALA   B 2 77  ? 35.058  -34.815 58.527  1.00 142.90 ?  381 ALA   B CA  1 
ATOM   5788 C C   . ALA   B 2 77  ? 36.499  -35.215 58.250  1.00 144.39 ?  381 ALA   B C   1 
ATOM   5789 O O   . ALA   B 2 77  ? 37.401  -34.862 59.017  1.00 138.27 ?  381 ALA   B O   1 
ATOM   5790 C CB  . ALA   B 2 77  ? 34.285  -35.999 59.102  1.00 141.54 ?  381 ALA   B CB  1 
ATOM   5791 N N   . ARG   B 2 78  ? 36.715  -35.958 57.160  1.00 152.32 ?  382 ARG   B N   1 
ATOM   5792 C CA  . ARG   B 2 78  ? 38.043  -36.446 56.792  1.00 152.96 ?  382 ARG   B CA  1 
ATOM   5793 C C   . ARG   B 2 78  ? 38.925  -35.323 56.258  1.00 149.77 ?  382 ARG   B C   1 
ATOM   5794 O O   . ARG   B 2 78  ? 38.450  -34.381 55.615  1.00 149.12 ?  382 ARG   B O   1 
ATOM   5795 C CB  . ARG   B 2 78  ? 37.946  -37.536 55.722  1.00 150.67 ?  382 ARG   B CB  1 
ATOM   5796 C CG  . ARG   B 2 78  ? 37.680  -38.915 56.248  1.00 158.01 ?  382 ARG   B CG  1 
ATOM   5797 C CD  . ARG   B 2 78  ? 36.807  -39.690 55.279  1.00 168.19 ?  382 ARG   B CD  1 
ATOM   5798 N NE  . ARG   B 2 78  ? 36.322  -40.929 55.877  1.00 178.41 ?  382 ARG   B NE  1 
ATOM   5799 C CZ  . ARG   B 2 78  ? 36.733  -42.145 55.541  1.00 177.64 ?  382 ARG   B CZ  1 
ATOM   5800 N NH1 . ARG   B 2 78  ? 37.581  -42.339 54.540  1.00 173.80 ?  382 ARG   B NH1 1 
ATOM   5801 N NH2 . ARG   B 2 78  ? 36.270  -43.196 56.217  1.00 174.25 ?  382 ARG   B NH2 1 
ATOM   5802 N N   . TRP   B 2 79  ? 40.234  -35.462 56.490  1.00 146.75 ?  383 TRP   B N   1 
ATOM   5803 C CA  . TRP   B 2 79  ? 41.241  -34.517 55.996  1.00 141.56 ?  383 TRP   B CA  1 
ATOM   5804 C C   . TRP   B 2 79  ? 41.904  -35.063 54.732  1.00 140.86 ?  383 TRP   B C   1 
ATOM   5805 O O   . TRP   B 2 79  ? 42.977  -35.671 54.794  1.00 139.18 ?  383 TRP   B O   1 
ATOM   5806 C CB  . TRP   B 2 79  ? 42.292  -34.251 57.063  1.00 137.31 ?  383 TRP   B CB  1 
ATOM   5807 C CG  . TRP   B 2 79  ? 41.866  -33.270 58.043  1.00 140.80 ?  383 TRP   B CG  1 
ATOM   5808 C CD1 . TRP   B 2 79  ? 41.500  -33.508 59.327  1.00 147.14 ?  383 TRP   B CD1 1 
ATOM   5809 C CD2 . TRP   B 2 79  ? 41.707  -31.864 57.826  1.00 139.85 ?  383 TRP   B CD2 1 
ATOM   5810 N NE1 . TRP   B 2 79  ? 41.149  -32.324 59.939  1.00 152.35 ?  383 TRP   B NE1 1 
ATOM   5811 C CE2 . TRP   B 2 79  ? 41.267  -31.303 59.032  1.00 144.27 ?  383 TRP   B CE2 1 
ATOM   5812 C CE3 . TRP   B 2 79  ? 41.911  -31.024 56.732  1.00 136.48 ?  383 TRP   B CE3 1 
ATOM   5813 C CZ2 . TRP   B 2 79  ? 41.025  -29.940 59.173  1.00 141.45 ?  383 TRP   B CZ2 1 
ATOM   5814 C CZ3 . TRP   B 2 79  ? 41.674  -29.670 56.879  1.00 131.25 ?  383 TRP   B CZ3 1 
ATOM   5815 C CH2 . TRP   B 2 79  ? 41.235  -29.145 58.083  1.00 132.32 ?  383 TRP   B CH2 1 
ATOM   5816 N N   . THR   B 2 80  ? 41.282  -34.822 53.571  1.00 136.71 ?  384 THR   B N   1 
ATOM   5817 C CA  . THR   B 2 80  ? 41.862  -35.312 52.325  1.00 131.87 ?  384 THR   B CA  1 
ATOM   5818 C C   . THR   B 2 80  ? 43.254  -34.722 52.140  1.00 129.47 ?  384 THR   B C   1 
ATOM   5819 O O   . THR   B 2 80  ? 43.508  -33.564 52.497  1.00 128.51 ?  384 THR   B O   1 
ATOM   5820 C CB  . THR   B 2 80  ? 40.977  -34.972 51.118  1.00 126.04 ?  384 THR   B CB  1 
ATOM   5821 O OG1 . THR   B 2 80  ? 41.180  -33.609 50.744  1.00 129.48 ?  384 THR   B OG1 1 
ATOM   5822 C CG2 . THR   B 2 80  ? 39.514  -35.185 51.437  1.00 129.65 ?  384 THR   B CG2 1 
ATOM   5823 N N   . THR   B 2 81  ? 44.168  -35.542 51.607  1.00 125.68 ?  385 THR   B N   1 
ATOM   5824 C CA  . THR   B 2 81  ? 45.542  -35.092 51.418  1.00 121.94 ?  385 THR   B CA  1 
ATOM   5825 C C   . THR   B 2 81  ? 45.588  -33.769 50.674  1.00 120.98 ?  385 THR   B C   1 
ATOM   5826 O O   . THR   B 2 81  ? 46.510  -32.973 50.878  1.00 119.60 ?  385 THR   B O   1 
ATOM   5827 C CB  . THR   B 2 81  ? 46.359  -36.147 50.666  1.00 123.39 ?  385 THR   B CB  1 
ATOM   5828 O OG1 . THR   B 2 81  ? 46.014  -37.470 51.118  1.00 134.60 ?  385 THR   B OG1 1 
ATOM   5829 C CG2 . THR   B 2 81  ? 47.834  -35.908 50.870  1.00 111.84 ?  385 THR   B CG2 1 
ATOM   5830 N N   . GLU   B 2 82  ? 44.595  -33.511 49.820  1.00 121.79 ?  386 GLU   B N   1 
ATOM   5831 C CA  . GLU   B 2 82  ? 44.466  -32.192 49.215  1.00 120.42 ?  386 GLU   B CA  1 
ATOM   5832 C C   . GLU   B 2 82  ? 44.111  -31.140 50.263  1.00 118.10 ?  386 GLU   B C   1 
ATOM   5833 O O   . GLU   B 2 82  ? 44.806  -30.126 50.399  1.00 113.54 ?  386 GLU   B O   1 
ATOM   5834 C CB  . GLU   B 2 82  ? 43.408  -32.215 48.113  1.00 123.73 ?  386 GLU   B CB  1 
ATOM   5835 C CG  . GLU   B 2 82  ? 42.878  -30.802 47.828  1.00 129.50 ?  386 GLU   B CG  1 
ATOM   5836 C CD  . GLU   B 2 82  ? 41.898  -30.732 46.669  1.00 138.34 ?  386 GLU   B CD  1 
ATOM   5837 O OE1 . GLU   B 2 82  ? 41.207  -31.748 46.425  1.00 144.18 ?  386 GLU   B OE1 1 
ATOM   5838 O OE2 . GLU   B 2 82  ? 41.829  -29.665 46.003  1.00 135.18 ?  386 GLU   B OE2 1 
ATOM   5839 N N   . GLU   B 2 83  ? 43.017  -31.363 51.007  1.00 121.58 ?  387 GLU   B N   1 
ATOM   5840 C CA  . GLU   B 2 83  ? 42.542  -30.367 51.962  1.00 118.12 ?  387 GLU   B CA  1 
ATOM   5841 C C   . GLU   B 2 83  ? 43.607  -30.026 52.976  1.00 114.97 ?  387 GLU   B C   1 
ATOM   5842 O O   . GLU   B 2 83  ? 43.650  -28.898 53.471  1.00 111.70 ?  387 GLU   B O   1 
ATOM   5843 C CB  . GLU   B 2 83  ? 41.299  -30.855 52.694  1.00 120.18 ?  387 GLU   B CB  1 
ATOM   5844 C CG  . GLU   B 2 83  ? 40.046  -30.909 51.866  1.00 125.00 ?  387 GLU   B CG  1 
ATOM   5845 C CD  . GLU   B 2 83  ? 39.072  -31.921 52.417  1.00 131.95 ?  387 GLU   B CD  1 
ATOM   5846 O OE1 . GLU   B 2 83  ? 39.478  -32.683 53.318  1.00 130.85 ?  387 GLU   B OE1 1 
ATOM   5847 O OE2 . GLU   B 2 83  ? 37.914  -31.964 51.948  1.00 136.20 ?  387 GLU   B OE2 1 
ATOM   5848 N N   . GLN   B 2 84  ? 44.459  -30.993 53.308  1.00 115.27 ?  388 GLN   B N   1 
ATOM   5849 C CA  . GLN   B 2 84  ? 45.585  -30.716 54.190  1.00 117.80 ?  388 GLN   B CA  1 
ATOM   5850 C C   . GLN   B 2 84  ? 46.487  -29.633 53.597  1.00 118.29 ?  388 GLN   B C   1 
ATOM   5851 O O   . GLN   B 2 84  ? 46.939  -28.716 54.300  1.00 115.43 ?  388 GLN   B O   1 
ATOM   5852 C CB  . GLN   B 2 84  ? 46.381  -32.002 54.431  1.00 116.66 ?  388 GLN   B CB  1 
ATOM   5853 C CG  . GLN   B 2 84  ? 45.566  -33.206 54.846  1.00 119.93 ?  388 GLN   B CG  1 
ATOM   5854 C CD  . GLN   B 2 84  ? 46.420  -34.272 55.485  1.00 120.17 ?  388 GLN   B CD  1 
ATOM   5855 O OE1 . GLN   B 2 84  ? 47.631  -34.118 55.608  1.00 117.13 ?  388 GLN   B OE1 1 
ATOM   5856 N NE2 . GLN   B 2 84  ? 45.797  -35.370 55.883  1.00 125.73 ?  388 GLN   B NE2 1 
ATOM   5857 N N   . LEU   B 2 85  ? 46.754  -29.724 52.290  1.00 119.47 ?  389 LEU   B N   1 
ATOM   5858 C CA  . LEU   B 2 85  ? 47.748  -28.853 51.674  1.00 111.00 ?  389 LEU   B CA  1 
ATOM   5859 C C   . LEU   B 2 85  ? 47.210  -27.446 51.511  1.00 112.05 ?  389 LEU   B C   1 
ATOM   5860 O O   . LEU   B 2 85  ? 47.943  -26.472 51.708  1.00 112.89 ?  389 LEU   B O   1 
ATOM   5861 C CB  . LEU   B 2 85  ? 48.174  -29.428 50.333  1.00 101.91 ?  389 LEU   B CB  1 
ATOM   5862 C CG  . LEU   B 2 85  ? 49.108  -30.598 50.533  1.00 96.38  ?  389 LEU   B CG  1 
ATOM   5863 C CD1 . LEU   B 2 85  ? 49.075  -31.401 49.287  1.00 101.53 ?  389 LEU   B CD1 1 
ATOM   5864 C CD2 . LEU   B 2 85  ? 50.513  -30.123 50.871  1.00 91.42  ?  389 LEU   B CD2 1 
ATOM   5865 N N   . LEU   B 2 86  ? 45.932  -27.327 51.142  1.00 111.57 ?  390 LEU   B N   1 
ATOM   5866 C CA  . LEU   B 2 86  ? 45.267  -26.033 51.176  1.00 111.19 ?  390 LEU   B CA  1 
ATOM   5867 C C   . LEU   B 2 86  ? 45.335  -25.419 52.574  1.00 118.51 ?  390 LEU   B C   1 
ATOM   5868 O O   . LEU   B 2 86  ? 45.497  -24.199 52.717  1.00 118.97 ?  390 LEU   B O   1 
ATOM   5869 C CB  . LEU   B 2 86  ? 43.821  -26.200 50.732  1.00 107.10 ?  390 LEU   B CB  1 
ATOM   5870 C CG  . LEU   B 2 86  ? 43.595  -26.377 49.246  1.00 105.44 ?  390 LEU   B CG  1 
ATOM   5871 C CD1 . LEU   B 2 86  ? 42.515  -27.396 49.026  1.00 115.16 ?  390 LEU   B CD1 1 
ATOM   5872 C CD2 . LEU   B 2 86  ? 43.155  -25.077 48.688  1.00 109.13 ?  390 LEU   B CD2 1 
ATOM   5873 N N   . ALA   B 2 87  ? 45.226  -26.253 53.620  1.00 118.34 ?  391 ALA   B N   1 
ATOM   5874 C CA  . ALA   B 2 87  ? 45.298  -25.760 54.993  1.00 109.90 ?  391 ALA   B CA  1 
ATOM   5875 C C   . ALA   B 2 87  ? 46.669  -25.182 55.299  1.00 107.78 ?  391 ALA   B C   1 
ATOM   5876 O O   . ALA   B 2 87  ? 46.777  -24.041 55.756  1.00 109.48 ?  391 ALA   B O   1 
ATOM   5877 C CB  . ALA   B 2 87  ? 44.970  -26.879 55.979  1.00 114.00 ?  391 ALA   B CB  1 
ATOM   5878 N N   . VAL   B 2 88  ? 47.730  -25.953 55.051  1.00 104.14 ?  392 VAL   B N   1 
ATOM   5879 C CA  . VAL   B 2 88  ? 49.069  -25.497 55.413  1.00 102.75 ?  392 VAL   B CA  1 
ATOM   5880 C C   . VAL   B 2 88  ? 49.388  -24.174 54.739  1.00 110.73 ?  392 VAL   B C   1 
ATOM   5881 O O   . VAL   B 2 88  ? 50.051  -23.310 55.319  1.00 113.53 ?  392 VAL   B O   1 
ATOM   5882 C CB  . VAL   B 2 88  ? 50.120  -26.556 55.061  1.00 102.64 ?  392 VAL   B CB  1 
ATOM   5883 C CG1 . VAL   B 2 88  ? 51.519  -25.916 54.986  1.00 99.12  ?  392 VAL   B CG1 1 
ATOM   5884 C CG2 . VAL   B 2 88  ? 50.078  -27.655 56.070  1.00 112.81 ?  392 VAL   B CG2 1 
ATOM   5885 N N   . GLN   B 2 89  ? 48.933  -23.988 53.503  1.00 113.14 ?  393 GLN   B N   1 
ATOM   5886 C CA  . GLN   B 2 89  ? 49.135  -22.680 52.904  1.00 111.93 ?  393 GLN   B CA  1 
ATOM   5887 C C   . GLN   B 2 89  ? 48.182  -21.674 53.505  1.00 114.61 ?  393 GLN   B C   1 
ATOM   5888 O O   . GLN   B 2 89  ? 48.540  -20.502 53.650  1.00 121.80 ?  393 GLN   B O   1 
ATOM   5889 C CB  . GLN   B 2 89  ? 48.935  -22.708 51.399  1.00 114.21 ?  393 GLN   B CB  1 
ATOM   5890 C CG  . GLN   B 2 89  ? 49.547  -23.869 50.683  1.00 112.60 ?  393 GLN   B CG  1 
ATOM   5891 C CD  . GLN   B 2 89  ? 49.583  -23.614 49.206  1.00 106.38 ?  393 GLN   B CD  1 
ATOM   5892 O OE1 . GLN   B 2 89  ? 48.978  -24.336 48.419  1.00 102.91 ?  393 GLN   B OE1 1 
ATOM   5893 N NE2 . GLN   B 2 89  ? 50.365  -22.616 48.810  1.00 108.65 ?  393 GLN   B NE2 1 
ATOM   5894 N N   . ALA   B 2 90  ? 46.965  -22.108 53.845  1.00 113.97 ?  394 ALA   B N   1 
ATOM   5895 C CA  . ALA   B 2 90  ? 46.017  -21.203 54.484  1.00 117.41 ?  394 ALA   B CA  1 
ATOM   5896 C C   . ALA   B 2 90  ? 46.622  -20.596 55.738  1.00 119.69 ?  394 ALA   B C   1 
ATOM   5897 O O   . ALA   B 2 90  ? 46.411  -19.419 56.036  1.00 121.27 ?  394 ALA   B O   1 
ATOM   5898 C CB  . ALA   B 2 90  ? 44.718  -21.935 54.813  1.00 118.97 ?  394 ALA   B CB  1 
ATOM   5899 N N   . ILE   B 2 91  ? 47.412  -21.375 56.465  1.00 117.99 ?  395 ILE   B N   1 
ATOM   5900 C CA  . ILE   B 2 91  ? 48.071  -20.835 57.642  1.00 118.34 ?  395 ILE   B CA  1 
ATOM   5901 C C   . ILE   B 2 91  ? 49.174  -19.871 57.240  1.00 118.42 ?  395 ILE   B C   1 
ATOM   5902 O O   . ILE   B 2 91  ? 49.267  -18.769 57.783  1.00 129.00 ?  395 ILE   B O   1 
ATOM   5903 C CB  . ILE   B 2 91  ? 48.594  -21.984 58.512  1.00 117.82 ?  395 ILE   B CB  1 
ATOM   5904 C CG1 . ILE   B 2 91  ? 47.454  -22.515 59.375  1.00 117.07 ?  395 ILE   B CG1 1 
ATOM   5905 C CG2 . ILE   B 2 91  ? 49.770  -21.533 59.342  1.00 119.01 ?  395 ILE   B CG2 1 
ATOM   5906 C CD1 . ILE   B 2 91  ? 47.614  -23.955 59.751  1.00 115.82 ?  395 ILE   B CD1 1 
ATOM   5907 N N   . ARG   B 2 92  ? 50.011  -20.246 56.270  1.00 115.36 ?  396 ARG   B N   1 
ATOM   5908 C CA  . ARG   B 2 92  ? 51.100  -19.363 55.854  1.00 119.67 ?  396 ARG   B CA  1 
ATOM   5909 C C   . ARG   B 2 92  ? 50.585  -18.008 55.363  1.00 119.71 ?  396 ARG   B C   1 
ATOM   5910 O O   . ARG   B 2 92  ? 51.284  -16.997 55.494  1.00 117.47 ?  396 ARG   B O   1 
ATOM   5911 C CB  . ARG   B 2 92  ? 51.937  -20.051 54.774  1.00 122.03 ?  396 ARG   B CB  1 
ATOM   5912 C CG  . ARG   B 2 92  ? 53.144  -19.272 54.266  1.00 121.22 ?  396 ARG   B CG  1 
ATOM   5913 C CD  . ARG   B 2 92  ? 54.080  -18.901 55.398  1.00 126.46 ?  396 ARG   B CD  1 
ATOM   5914 N NE  . ARG   B 2 92  ? 55.121  -17.963 54.988  1.00 128.87 ?  396 ARG   B NE  1 
ATOM   5915 C CZ  . ARG   B 2 92  ? 54.917  -16.698 54.648  1.00 127.57 ?  396 ARG   B CZ  1 
ATOM   5916 N NH1 . ARG   B 2 92  ? 53.707  -16.162 54.663  1.00 126.27 ?  396 ARG   B NH1 1 
ATOM   5917 N NH2 . ARG   B 2 92  ? 55.955  -15.949 54.284  1.00 124.81 ?  396 ARG   B NH2 1 
ATOM   5918 N N   . LYS   B 2 93  ? 49.369  -17.961 54.815  1.00 118.02 ?  397 LYS   B N   1 
ATOM   5919 C CA  . LYS   B 2 93  ? 48.792  -16.721 54.311  1.00 119.45 ?  397 LYS   B CA  1 
ATOM   5920 C C   . LYS   B 2 93  ? 47.833  -16.068 55.287  1.00 120.39 ?  397 LYS   B C   1 
ATOM   5921 O O   . LYS   B 2 93  ? 47.488  -14.901 55.094  1.00 120.29 ?  397 LYS   B O   1 
ATOM   5922 C CB  . LYS   B 2 93  ? 48.035  -16.949 52.986  1.00 121.73 ?  397 LYS   B CB  1 
ATOM   5923 C CG  . LYS   B 2 93  ? 47.772  -15.662 52.147  1.00 119.77 ?  397 LYS   B CG  1 
ATOM   5924 C CD  . LYS   B 2 93  ? 46.432  -15.717 51.408  1.00 113.36 ?  397 LYS   B CD  1 
ATOM   5925 C CE  . LYS   B 2 93  ? 45.871  -14.325 51.047  1.00 115.60 ?  397 LYS   B CE  1 
ATOM   5926 N NZ  . LYS   B 2 93  ? 46.695  -13.516 50.096  1.00 115.73 ?  397 LYS   B NZ  1 
ATOM   5927 N N   . TYR   B 2 94  ? 47.379  -16.782 56.314  1.00 126.58 ?  398 TYR   B N   1 
ATOM   5928 C CA  . TYR   B 2 94  ? 46.324  -16.262 57.184  1.00 132.83 ?  398 TYR   B CA  1 
ATOM   5929 C C   . TYR   B 2 94  ? 46.624  -16.331 58.681  1.00 135.21 ?  398 TYR   B C   1 
ATOM   5930 O O   . TYR   B 2 94  ? 46.004  -15.577 59.447  1.00 132.48 ?  398 TYR   B O   1 
ATOM   5931 C CB  . TYR   B 2 94  ? 45.000  -16.988 56.892  1.00 126.81 ?  398 TYR   B CB  1 
ATOM   5932 C CG  . TYR   B 2 94  ? 44.376  -16.560 55.580  1.00 120.15 ?  398 TYR   B CG  1 
ATOM   5933 C CD1 . TYR   B 2 94  ? 44.003  -15.249 55.381  1.00 117.54 ?  398 TYR   B CD1 1 
ATOM   5934 C CD2 . TYR   B 2 94  ? 44.194  -17.451 54.540  1.00 120.27 ?  398 TYR   B CD2 1 
ATOM   5935 C CE1 . TYR   B 2 94  ? 43.440  -14.837 54.218  1.00 116.31 ?  398 TYR   B CE1 1 
ATOM   5936 C CE2 . TYR   B 2 94  ? 43.632  -17.038 53.357  1.00 121.96 ?  398 TYR   B CE2 1 
ATOM   5937 C CZ  . TYR   B 2 94  ? 43.257  -15.721 53.207  1.00 118.32 ?  398 TYR   B CZ  1 
ATOM   5938 O OH  . TYR   B 2 94  ? 42.685  -15.265 52.045  1.00 119.53 ?  398 TYR   B OH  1 
ATOM   5939 N N   . GLY   B 2 95  ? 47.545  -17.192 59.119  1.00 137.36 ?  399 GLY   B N   1 
ATOM   5940 C CA  . GLY   B 2 95  ? 48.036  -17.204 60.486  1.00 140.14 ?  399 GLY   B CA  1 
ATOM   5941 C C   . GLY   B 2 95  ? 47.129  -17.885 61.488  1.00 142.20 ?  399 GLY   B C   1 
ATOM   5942 O O   . GLY   B 2 95  ? 47.132  -19.115 61.619  1.00 138.31 ?  399 GLY   B O   1 
ATOM   5943 N N   . ARG   B 2 96  ? 46.352  -17.090 62.217  1.00 144.99 ?  400 ARG   B N   1 
ATOM   5944 C CA  . ARG   B 2 96  ? 45.388  -17.635 63.151  1.00 144.06 ?  400 ARG   B CA  1 
ATOM   5945 C C   . ARG   B 2 96  ? 43.945  -17.327 62.788  1.00 141.20 ?  400 ARG   B C   1 
ATOM   5946 O O   . ARG   B 2 96  ? 43.045  -17.919 63.390  1.00 139.86 ?  400 ARG   B O   1 
ATOM   5947 C CB  . ARG   B 2 96  ? 45.681  -17.137 64.576  1.00 141.83 ?  400 ARG   B CB  1 
ATOM   5948 C CG  . ARG   B 2 96  ? 46.770  -17.943 65.245  1.00 139.73 ?  400 ARG   B CG  1 
ATOM   5949 C CD  . ARG   B 2 96  ? 47.434  -17.200 66.372  1.00 140.34 ?  400 ARG   B CD  1 
ATOM   5950 N NE  . ARG   B 2 96  ? 48.691  -17.836 66.752  1.00 146.74 ?  400 ARG   B NE  1 
ATOM   5951 C CZ  . ARG   B 2 96  ? 49.895  -17.366 66.448  1.00 147.60 ?  400 ARG   B CZ  1 
ATOM   5952 N NH1 . ARG   B 2 96  ? 50.045  -16.214 65.804  1.00 145.53 ?  400 ARG   B NH1 1 
ATOM   5953 N NH2 . ARG   B 2 96  ? 50.975  -18.062 66.808  1.00 139.41 ?  400 ARG   B NH2 1 
ATOM   5954 N N   . ASP   B 2 97  ? 43.694  -16.440 61.823  1.00 139.15 ?  401 ASP   B N   1 
ATOM   5955 C CA  . ASP   B 2 97  ? 42.325  -16.142 61.417  1.00 136.93 ?  401 ASP   B CA  1 
ATOM   5956 C C   . ASP   B 2 97  ? 41.946  -17.591 61.138  1.00 133.57 ?  401 ASP   B C   1 
ATOM   5957 O O   . ASP   B 2 97  ? 42.530  -18.250 60.272  1.00 135.15 ?  401 ASP   B O   1 
ATOM   5958 C CB  . ASP   B 2 97  ? 42.319  -15.124 60.270  1.00 133.71 ?  401 ASP   B CB  1 
ATOM   5959 C CG  . ASP   B 2 97  ? 40.915  -14.767 59.798  1.00 133.71 ?  401 ASP   B CG  1 
ATOM   5960 O OD1 . ASP   B 2 97  ? 39.927  -15.343 60.319  1.00 135.58 ?  401 ASP   B OD1 1 
ATOM   5961 O OD2 . ASP   B 2 97  ? 40.801  -13.880 58.920  1.00 127.61 ?  401 ASP   B OD2 1 
ATOM   5962 N N   . PHE   B 2 98  ? 40.961  -18.092 61.883  1.00 134.74 ?  402 PHE   B N   1 
ATOM   5963 C CA  . PHE   B 2 98  ? 40.637  -19.511 61.842  1.00 137.22 ?  402 PHE   B CA  1 
ATOM   5964 C C   . PHE   B 2 98  ? 39.406  -19.508 60.949  1.00 137.38 ?  402 PHE   B C   1 
ATOM   5965 O O   . PHE   B 2 98  ? 39.038  -20.562 60.415  1.00 136.11 ?  402 PHE   B O   1 
ATOM   5966 C CB  . PHE   B 2 98  ? 40.296  -20.156 63.183  1.00 135.98 ?  402 PHE   B CB  1 
ATOM   5967 C CG  . PHE   B 2 98  ? 41.479  -20.314 64.113  1.00 145.45 ?  402 PHE   B CG  1 
ATOM   5968 C CD1 . PHE   B 2 98  ? 42.609  -21.019 63.733  1.00 148.45 ?  402 PHE   B CD1 1 
ATOM   5969 C CD2 . PHE   B 2 98  ? 41.443  -19.776 65.397  1.00 150.47 ?  402 PHE   B CD2 1 
ATOM   5970 C CE1 . PHE   B 2 98  ? 43.691  -21.166 64.619  1.00 147.13 ?  402 PHE   B CE1 1 
ATOM   5971 C CE2 . PHE   B 2 98  ? 42.518  -19.933 66.282  1.00 150.48 ?  402 PHE   B CE2 1 
ATOM   5972 C CZ  . PHE   B 2 98  ? 43.642  -20.623 65.887  1.00 144.98 ?  402 PHE   B CZ  1 
ATOM   5973 N N   . GLN   B 2 99  ? 38.767  -18.345 60.783  1.00 132.10 ?  403 GLN   B N   1 
ATOM   5974 C CA  . GLN   B 2 99  ? 37.592  -18.248 59.927  1.00 130.36 ?  403 GLN   B CA  1 
ATOM   5975 C C   . GLN   B 2 99  ? 37.981  -18.341 58.459  1.00 133.96 ?  403 GLN   B C   1 
ATOM   5976 O O   . GLN   B 2 99  ? 37.406  -19.133 57.699  1.00 134.45 ?  403 GLN   B O   1 
ATOM   5977 C CB  . GLN   B 2 99  ? 36.852  -16.942 60.217  1.00 129.36 ?  403 GLN   B CB  1 
ATOM   5978 C CG  . GLN   B 2 99  ? 35.525  -16.745 59.481  1.00 132.42 ?  403 GLN   B CG  1 
ATOM   5979 C CD  . GLN   B 2 99  ? 34.551  -17.914 59.574  1.00 133.65 ?  403 GLN   B CD  1 
ATOM   5980 O OE1 . GLN   B 2 99  ? 34.716  -18.833 60.380  1.00 133.08 ?  403 GLN   B OE1 1 
ATOM   5981 N NE2 . GLN   B 2 99  ? 33.522  -17.878 58.732  1.00 136.99 ?  403 GLN   B NE2 1 
ATOM   5982 N N   . ALA   B 2 100 ? 38.966  -17.540 58.047  1.00 134.09 ?  404 ALA   B N   1 
ATOM   5983 C CA  . ALA   B 2 100 ? 39.446  -17.579 56.672  1.00 129.13 ?  404 ALA   B CA  1 
ATOM   5984 C C   . ALA   B 2 100 ? 39.916  -18.977 56.294  1.00 128.85 ?  404 ALA   B C   1 
ATOM   5985 O O   . ALA   B 2 100 ? 39.529  -19.514 55.249  1.00 130.02 ?  404 ALA   B O   1 
ATOM   5986 C CB  . ALA   B 2 100 ? 40.570  -16.563 56.488  1.00 125.35 ?  404 ALA   B CB  1 
ATOM   5987 N N   . ILE   B 2 101 ? 40.749  -19.591 57.134  1.00 121.91 ?  405 ILE   B N   1 
ATOM   5988 C CA  . ILE   B 2 101 ? 41.196  -20.939 56.819  1.00 121.87 ?  405 ILE   B CA  1 
ATOM   5989 C C   . ILE   B 2 101 ? 40.009  -21.857 56.575  1.00 124.11 ?  405 ILE   B C   1 
ATOM   5990 O O   . ILE   B 2 101 ? 40.003  -22.652 55.630  1.00 125.44 ?  405 ILE   B O   1 
ATOM   5991 C CB  . ILE   B 2 101 ? 42.126  -21.464 57.922  1.00 118.92 ?  405 ILE   B CB  1 
ATOM   5992 C CG1 . ILE   B 2 101 ? 43.404  -20.633 57.922  1.00 114.76 ?  405 ILE   B CG1 1 
ATOM   5993 C CG2 . ILE   B 2 101 ? 42.392  -22.934 57.728  1.00 120.52 ?  405 ILE   B CG2 1 
ATOM   5994 C CD1 . ILE   B 2 101 ? 44.141  -20.655 59.196  1.00 124.23 ?  405 ILE   B CD1 1 
ATOM   5995 N N   . SER   B 2 102 ? 38.958  -21.717 57.369  1.00 126.87 ?  406 SER   B N   1 
ATOM   5996 C CA  . SER   B 2 102 ? 37.806  -22.582 57.178  1.00 130.77 ?  406 SER   B CA  1 
ATOM   5997 C C   . SER   B 2 102 ? 36.934  -22.169 55.998  1.00 130.57 ?  406 SER   B C   1 
ATOM   5998 O O   . SER   B 2 102 ? 36.097  -22.965 55.559  1.00 136.40 ?  406 SER   B O   1 
ATOM   5999 C CB  . SER   B 2 102 ? 36.955  -22.624 58.442  1.00 135.61 ?  406 SER   B CB  1 
ATOM   6000 O OG  . SER   B 2 102 ? 35.604  -22.884 58.105  1.00 142.23 ?  406 SER   B OG  1 
ATOM   6001 N N   . ASP   B 2 103 ? 37.078  -20.955 55.484  1.00 126.00 ?  407 ASP   B N   1 
ATOM   6002 C CA  . ASP   B 2 103 ? 36.374  -20.629 54.249  1.00 131.60 ?  407 ASP   B CA  1 
ATOM   6003 C C   . ASP   B 2 103 ? 37.190  -20.999 53.016  1.00 131.29 ?  407 ASP   B C   1 
ATOM   6004 O O   . ASP   B 2 103 ? 36.619  -21.225 51.937  1.00 132.28 ?  407 ASP   B O   1 
ATOM   6005 C CB  . ASP   B 2 103 ? 36.016  -19.136 54.186  1.00 134.92 ?  407 ASP   B CB  1 
ATOM   6006 C CG  . ASP   B 2 103 ? 35.254  -18.649 55.407  1.00 132.84 ?  407 ASP   B CG  1 
ATOM   6007 O OD1 . ASP   B 2 103 ? 34.380  -19.397 55.916  1.00 131.84 ?  407 ASP   B OD1 1 
ATOM   6008 O OD2 . ASP   B 2 103 ? 35.532  -17.498 55.827  1.00 127.17 ?  407 ASP   B OD2 1 
ATOM   6009 N N   . VAL   B 2 104 ? 38.517  -21.043 53.153  1.00 128.20 ?  408 VAL   B N   1 
ATOM   6010 C CA  . VAL   B 2 104 ? 39.359  -21.489 52.052  1.00 124.34 ?  408 VAL   B CA  1 
ATOM   6011 C C   . VAL   B 2 104 ? 39.146  -22.977 51.808  1.00 124.10 ?  408 VAL   B C   1 
ATOM   6012 O O   . VAL   B 2 104 ? 38.851  -23.404 50.685  1.00 123.51 ?  408 VAL   B O   1 
ATOM   6013 C CB  . VAL   B 2 104 ? 40.833  -21.146 52.338  1.00 120.49 ?  408 VAL   B CB  1 
ATOM   6014 C CG1 . VAL   B 2 104 ? 41.750  -21.947 51.465  1.00 117.83 ?  408 VAL   B CG1 1 
ATOM   6015 C CG2 . VAL   B 2 104 ? 41.077  -19.674 52.086  1.00 116.36 ?  408 VAL   B CG2 1 
ATOM   6016 N N   . ILE   B 2 105 ? 39.232  -23.782 52.867  1.00 119.79 ?  409 ILE   B N   1 
ATOM   6017 C CA  . ILE   B 2 105 ? 39.055  -25.216 52.701  1.00 116.70 ?  409 ILE   B CA  1 
ATOM   6018 C C   . ILE   B 2 105 ? 37.605  -25.550 52.375  1.00 123.49 ?  409 ILE   B C   1 
ATOM   6019 O O   . ILE   B 2 105 ? 37.326  -26.565 51.733  1.00 128.26 ?  409 ILE   B O   1 
ATOM   6020 C CB  . ILE   B 2 105 ? 39.550  -25.944 53.955  1.00 115.20 ?  409 ILE   B CB  1 
ATOM   6021 C CG1 . ILE   B 2 105 ? 40.968  -25.486 54.279  1.00 114.61 ?  409 ILE   B CG1 1 
ATOM   6022 C CG2 . ILE   B 2 105 ? 39.579  -27.418 53.702  1.00 119.33 ?  409 ILE   B CG2 1 
ATOM   6023 C CD1 . ILE   B 2 105 ? 41.605  -26.238 55.395  1.00 110.78 ?  409 ILE   B CD1 1 
ATOM   6024 N N   . GLY   B 2 106 ? 36.663  -24.716 52.796  1.00 130.55 ?  410 GLY   B N   1 
ATOM   6025 C CA  . GLY   B 2 106 ? 35.292  -24.825 52.323  1.00 137.83 ?  410 GLY   B CA  1 
ATOM   6026 C C   . GLY   B 2 106 ? 34.417  -25.862 52.999  1.00 140.85 ?  410 GLY   B C   1 
ATOM   6027 O O   . GLY   B 2 106 ? 33.241  -25.595 53.278  1.00 143.07 ?  410 GLY   B O   1 
ATOM   6028 N N   . ASN   B 2 107 ? 34.968  -27.050 53.252  1.00 138.44 ?  411 ASN   B N   1 
ATOM   6029 C CA  . ASN   B 2 107 ? 34.257  -28.127 53.931  1.00 142.99 ?  411 ASN   B CA  1 
ATOM   6030 C C   . ASN   B 2 107 ? 34.996  -28.554 55.199  1.00 137.51 ?  411 ASN   B C   1 
ATOM   6031 O O   . ASN   B 2 107 ? 35.114  -29.735 55.522  1.00 141.37 ?  411 ASN   B O   1 
ATOM   6032 C CB  . ASN   B 2 107 ? 34.007  -29.305 52.981  1.00 146.96 ?  411 ASN   B CB  1 
ATOM   6033 C CG  . ASN   B 2 107 ? 35.203  -30.245 52.848  1.00 143.43 ?  411 ASN   B CG  1 
ATOM   6034 O OD1 . ASN   B 2 107 ? 36.353  -29.852 53.056  1.00 140.32 ?  411 ASN   B OD1 1 
ATOM   6035 N ND2 . ASN   B 2 107 ? 34.927  -31.499 52.496  1.00 139.07 ?  411 ASN   B ND2 1 
ATOM   6036 N N   . LYS   B 2 108 ? 35.501  -27.590 55.950  1.00 135.43 ?  412 LYS   B N   1 
ATOM   6037 C CA  . LYS   B 2 108 ? 36.031  -27.876 57.277  1.00 139.07 ?  412 LYS   B CA  1 
ATOM   6038 C C   . LYS   B 2 108 ? 35.572  -26.778 58.222  1.00 148.14 ?  412 LYS   B C   1 
ATOM   6039 O O   . LYS   B 2 108 ? 35.928  -25.607 58.043  1.00 144.02 ?  412 LYS   B O   1 
ATOM   6040 C CB  . LYS   B 2 108 ? 37.548  -28.004 57.263  1.00 134.93 ?  412 LYS   B CB  1 
ATOM   6041 C CG  . LYS   B 2 108 ? 38.002  -29.222 56.522  1.00 132.24 ?  412 LYS   B CG  1 
ATOM   6042 C CD  . LYS   B 2 108 ? 37.948  -30.410 57.425  1.00 130.88 ?  412 LYS   B CD  1 
ATOM   6043 C CE  . LYS   B 2 108 ? 38.436  -31.616 56.716  1.00 130.92 ?  412 LYS   B CE  1 
ATOM   6044 N NZ  . LYS   B 2 108 ? 37.609  -31.818 55.503  1.00 136.08 ?  412 LYS   B NZ  1 
ATOM   6045 N N   . SER   B 2 109 ? 34.768  -27.172 59.210  1.00 153.80 ?  413 SER   B N   1 
ATOM   6046 C CA  . SER   B 2 109 ? 34.322  -26.274 60.266  1.00 149.42 ?  413 SER   B CA  1 
ATOM   6047 C C   . SER   B 2 109 ? 35.511  -25.675 61.001  1.00 144.77 ?  413 SER   B C   1 
ATOM   6048 O O   . SER   B 2 109 ? 36.593  -26.271 61.078  1.00 143.23 ?  413 SER   B O   1 
ATOM   6049 C CB  . SER   B 2 109 ? 33.439  -27.025 61.259  1.00 148.43 ?  413 SER   B CB  1 
ATOM   6050 O OG  . SER   B 2 109 ? 34.243  -27.823 62.112  1.00 144.23 ?  413 SER   B OG  1 
ATOM   6051 N N   . VAL   B 2 110 ? 35.286  -24.487 61.567  1.00 141.14 ?  414 VAL   B N   1 
ATOM   6052 C CA  . VAL   B 2 110 ? 36.367  -23.770 62.234  1.00 145.22 ?  414 VAL   B CA  1 
ATOM   6053 C C   . VAL   B 2 110 ? 36.989  -24.627 63.326  1.00 146.08 ?  414 VAL   B C   1 
ATOM   6054 O O   . VAL   B 2 110 ? 38.183  -24.507 63.612  1.00 141.64 ?  414 VAL   B O   1 
ATOM   6055 C CB  . VAL   B 2 110 ? 35.861  -22.427 62.799  1.00 138.09 ?  414 VAL   B CB  1 
ATOM   6056 C CG1 . VAL   B 2 110 ? 37.039  -21.517 63.125  1.00 128.35 ?  414 VAL   B CG1 1 
ATOM   6057 C CG2 . VAL   B 2 110 ? 34.882  -21.762 61.832  1.00 134.66 ?  414 VAL   B CG2 1 
ATOM   6058 N N   . VAL   B 2 111 ? 36.206  -25.523 63.926  1.00 147.92 ?  415 VAL   B N   1 
ATOM   6059 C CA  . VAL   B 2 111 ? 36.716  -26.342 65.019  1.00 149.04 ?  415 VAL   B CA  1 
ATOM   6060 C C   . VAL   B 2 111 ? 37.562  -27.508 64.507  1.00 150.83 ?  415 VAL   B C   1 
ATOM   6061 O O   . VAL   B 2 111 ? 38.546  -27.900 65.154  1.00 149.02 ?  415 VAL   B O   1 
ATOM   6062 C CB  . VAL   B 2 111 ? 35.551  -26.813 65.906  1.00 147.38 ?  415 VAL   B CB  1 
ATOM   6063 C CG1 . VAL   B 2 111 ? 34.544  -27.622 65.107  1.00 142.76 ?  415 VAL   B CG1 1 
ATOM   6064 C CG2 . VAL   B 2 111 ? 36.086  -27.641 67.071  1.00 151.63 ?  415 VAL   B CG2 1 
ATOM   6065 N N   . GLN   B 2 112 ? 37.210  -28.083 63.355  1.00 146.66 ?  416 GLN   B N   1 
ATOM   6066 C CA  . GLN   B 2 112 ? 38.110  -29.052 62.753  1.00 145.05 ?  416 GLN   B CA  1 
ATOM   6067 C C   . GLN   B 2 112 ? 39.455  -28.410 62.456  1.00 147.11 ?  416 GLN   B C   1 
ATOM   6068 O O   . GLN   B 2 112 ? 40.491  -29.090 62.491  1.00 144.04 ?  416 GLN   B O   1 
ATOM   6069 C CB  . GLN   B 2 112 ? 37.466  -29.634 61.502  1.00 143.44 ?  416 GLN   B CB  1 
ATOM   6070 C CG  . GLN   B 2 112 ? 36.377  -30.646 61.826  1.00 146.62 ?  416 GLN   B CG  1 
ATOM   6071 C CD  . GLN   B 2 112 ? 35.359  -30.819 60.701  1.00 151.85 ?  416 GLN   B CD  1 
ATOM   6072 O OE1 . GLN   B 2 112 ? 34.835  -29.838 60.160  1.00 147.78 ?  416 GLN   B OE1 1 
ATOM   6073 N NE2 . GLN   B 2 112 ? 35.073  -32.073 60.346  1.00 150.55 ?  416 GLN   B NE2 1 
ATOM   6074 N N   . VAL   B 2 113 ? 39.456  -27.089 62.224  1.00 147.53 ?  417 VAL   B N   1 
ATOM   6075 C CA  . VAL   B 2 113 ? 40.692  -26.336 62.016  1.00 145.58 ?  417 VAL   B CA  1 
ATOM   6076 C C   . VAL   B 2 113 ? 41.549  -26.325 63.283  1.00 148.54 ?  417 VAL   B C   1 
ATOM   6077 O O   . VAL   B 2 113 ? 42.782  -26.252 63.205  1.00 147.67 ?  417 VAL   B O   1 
ATOM   6078 C CB  . VAL   B 2 113 ? 40.366  -24.907 61.513  1.00 135.48 ?  417 VAL   B CB  1 
ATOM   6079 C CG1 . VAL   B 2 113 ? 41.614  -24.047 61.407  1.00 128.06 ?  417 VAL   B CG1 1 
ATOM   6080 C CG2 . VAL   B 2 113 ? 39.628  -24.952 60.174  1.00 132.38 ?  417 VAL   B CG2 1 
ATOM   6081 N N   . LYS   B 2 114 ? 40.937  -26.440 64.464  1.00 149.13 ?  418 LYS   B N   1 
ATOM   6082 C CA  . LYS   B 2 114 ? 41.757  -26.474 65.674  1.00 149.09 ?  418 LYS   B CA  1 
ATOM   6083 C C   . LYS   B 2 114 ? 42.483  -27.797 65.769  1.00 147.86 ?  418 LYS   B C   1 
ATOM   6084 O O   . LYS   B 2 114 ? 43.711  -27.841 65.906  1.00 143.26 ?  418 LYS   B O   1 
ATOM   6085 C CB  . LYS   B 2 114 ? 40.941  -26.298 66.963  1.00 156.73 ?  418 LYS   B CB  1 
ATOM   6086 C CG  . LYS   B 2 114 ? 39.585  -25.648 66.923  1.00 153.94 ?  418 LYS   B CG  1 
ATOM   6087 C CD  . LYS   B 2 114 ? 39.575  -24.475 66.033  1.00 147.99 ?  418 LYS   B CD  1 
ATOM   6088 C CE  . LYS   B 2 114 ? 40.447  -23.372 66.462  1.00 150.00 ?  418 LYS   B CE  1 
ATOM   6089 N NZ  . LYS   B 2 114 ? 40.156  -22.460 65.373  1.00 150.22 ?  418 LYS   B NZ  1 
ATOM   6090 N N   . ASN   B 2 115 ? 41.705  -28.884 65.742  1.00 152.09 ?  419 ASN   B N   1 
ATOM   6091 C CA  . ASN   B 2 115 ? 42.255  -30.234 65.806  1.00 160.24 ?  419 ASN   B CA  1 
ATOM   6092 C C   . ASN   B 2 115 ? 43.408  -30.381 64.831  1.00 155.05 ?  419 ASN   B C   1 
ATOM   6093 O O   . ASN   B 2 115 ? 44.442  -30.989 65.146  1.00 148.74 ?  419 ASN   B O   1 
ATOM   6094 C CB  . ASN   B 2 115 ? 41.155  -31.255 65.485  1.00 164.47 ?  419 ASN   B CB  1 
ATOM   6095 C CG  . ASN   B 2 115 ? 40.160  -31.421 66.622  1.00 170.26 ?  419 ASN   B CG  1 
ATOM   6096 O OD1 . ASN   B 2 115 ? 39.542  -30.440 67.064  1.00 164.66 ?  419 ASN   B OD1 1 
ATOM   6097 N ND2 . ASN   B 2 115 ? 40.002  -32.661 67.109  1.00 169.73 ?  419 ASN   B ND2 1 
ATOM   6098 N N   . PHE   B 2 116 ? 43.238  -29.804 63.641  1.00 152.30 ?  420 PHE   B N   1 
ATOM   6099 C CA  . PHE   B 2 116 ? 44.311  -29.755 62.663  1.00 150.17 ?  420 PHE   B CA  1 
ATOM   6100 C C   . PHE   B 2 116 ? 45.534  -29.049 63.231  1.00 146.14 ?  420 PHE   B C   1 
ATOM   6101 O O   . PHE   B 2 116 ? 46.651  -29.585 63.193  1.00 145.93 ?  420 PHE   B O   1 
ATOM   6102 C CB  . PHE   B 2 116 ? 43.807  -29.053 61.406  1.00 145.19 ?  420 PHE   B CB  1 
ATOM   6103 C CG  . PHE   B 2 116 ? 44.685  -29.249 60.212  1.00 142.71 ?  420 PHE   B CG  1 
ATOM   6104 C CD1 . PHE   B 2 116 ? 45.847  -28.496 60.055  1.00 141.71 ?  420 PHE   B CD1 1 
ATOM   6105 C CD2 . PHE   B 2 116 ? 44.355  -30.174 59.250  1.00 137.12 ?  420 PHE   B CD2 1 
ATOM   6106 C CE1 . PHE   B 2 116 ? 46.660  -28.658 58.968  1.00 132.76 ?  420 PHE   B CE1 1 
ATOM   6107 C CE2 . PHE   B 2 116 ? 45.158  -30.345 58.163  1.00 139.80 ?  420 PHE   B CE2 1 
ATOM   6108 C CZ  . PHE   B 2 116 ? 46.321  -29.582 58.019  1.00 139.83 ?  420 PHE   B CZ  1 
ATOM   6109 N N   . PHE   B 2 117 ? 45.335  -27.844 63.772  1.00 141.07 ?  421 PHE   B N   1 
ATOM   6110 C CA  . PHE   B 2 117 ? 46.443  -27.070 64.311  1.00 140.72 ?  421 PHE   B CA  1 
ATOM   6111 C C   . PHE   B 2 117 ? 47.268  -27.842 65.317  1.00 147.55 ?  421 PHE   B C   1 
ATOM   6112 O O   . PHE   B 2 117 ? 48.454  -27.537 65.499  1.00 144.37 ?  421 PHE   B O   1 
ATOM   6113 C CB  . PHE   B 2 117 ? 45.926  -25.809 64.978  1.00 137.52 ?  421 PHE   B CB  1 
ATOM   6114 C CG  . PHE   B 2 117 ? 46.018  -24.613 64.116  1.00 138.14 ?  421 PHE   B CG  1 
ATOM   6115 C CD1 . PHE   B 2 117 ? 47.181  -23.855 64.093  1.00 135.04 ?  421 PHE   B CD1 1 
ATOM   6116 C CD2 . PHE   B 2 117 ? 44.953  -24.236 63.320  1.00 139.78 ?  421 PHE   B CD2 1 
ATOM   6117 C CE1 . PHE   B 2 117 ? 47.279  -22.732 63.293  1.00 131.27 ?  421 PHE   B CE1 1 
ATOM   6118 C CE2 . PHE   B 2 117 ? 45.045  -23.125 62.506  1.00 138.40 ?  421 PHE   B CE2 1 
ATOM   6119 C CZ  . PHE   B 2 117 ? 46.209  -22.360 62.505  1.00 135.09 ?  421 PHE   B CZ  1 
ATOM   6120 N N   . VAL   B 2 118 ? 46.673  -28.830 65.977  1.00 149.82 ?  422 VAL   B N   1 
ATOM   6121 C CA  . VAL   B 2 118 ? 47.313  -29.533 67.077  1.00 146.96 ?  422 VAL   B CA  1 
ATOM   6122 C C   . VAL   B 2 118 ? 47.709  -30.951 66.669  1.00 147.59 ?  422 VAL   B C   1 
ATOM   6123 O O   . VAL   B 2 118 ? 48.877  -31.326 66.775  1.00 150.27 ?  422 VAL   B O   1 
ATOM   6124 C CB  . VAL   B 2 118 ? 46.415  -29.529 68.334  1.00 141.47 ?  422 VAL   B CB  1 
ATOM   6125 C CG1 . VAL   B 2 118 ? 47.181  -30.064 69.523  1.00 144.96 ?  422 VAL   B CG1 1 
ATOM   6126 C CG2 . VAL   B 2 118 ? 45.896  -28.126 68.607  1.00 132.20 ?  422 VAL   B CG2 1 
ATOM   6127 N N   . ASN   B 2 119 ? 46.751  -31.745 66.170  1.00 146.71 ?  423 ASN   B N   1 
ATOM   6128 C CA  . ASN   B 2 119 ? 47.049  -33.123 65.762  1.00 153.06 ?  423 ASN   B CA  1 
ATOM   6129 C C   . ASN   B 2 119 ? 48.234  -33.187 64.803  1.00 149.73 ?  423 ASN   B C   1 
ATOM   6130 O O   . ASN   B 2 119 ? 49.163  -33.994 64.974  1.00 143.32 ?  423 ASN   B O   1 
ATOM   6131 C CB  . ASN   B 2 119 ? 45.813  -33.761 65.121  1.00 151.23 ?  423 ASN   B CB  1 
ATOM   6132 C CG  . ASN   B 2 119 ? 44.684  -33.965 66.109  1.00 158.34 ?  423 ASN   B CG  1 
ATOM   6133 O OD1 . ASN   B 2 119 ? 43.536  -33.626 65.834  1.00 158.68 ?  423 ASN   B OD1 1 
ATOM   6134 N ND2 . ASN   B 2 119 ? 44.995  -34.582 67.246  1.00 164.04 ?  423 ASN   B ND2 1 
ATOM   6135 N N   . TYR   B 2 120 ? 48.224  -32.321 63.797  1.00 148.94 ?  424 TYR   B N   1 
ATOM   6136 C CA  . TYR   B 2 120 ? 49.256  -32.375 62.779  1.00 148.21 ?  424 TYR   B CA  1 
ATOM   6137 C C   . TYR   B 2 120 ? 50.468  -31.523 63.135  1.00 143.25 ?  424 TYR   B C   1 
ATOM   6138 O O   . TYR   B 2 120 ? 51.594  -31.951 62.880  1.00 142.32 ?  424 TYR   B O   1 
ATOM   6139 C CB  . TYR   B 2 120 ? 48.654  -31.978 61.430  1.00 138.52 ?  424 TYR   B CB  1 
ATOM   6140 C CG  . TYR   B 2 120 ? 47.759  -33.074 60.889  1.00 137.03 ?  424 TYR   B CG  1 
ATOM   6141 C CD1 . TYR   B 2 120 ? 48.259  -34.359 60.666  1.00 131.29 ?  424 TYR   B CD1 1 
ATOM   6142 C CD2 . TYR   B 2 120 ? 46.415  -32.840 60.623  1.00 138.63 ?  424 TYR   B CD2 1 
ATOM   6143 C CE1 . TYR   B 2 120 ? 47.448  -35.379 60.169  1.00 132.46 ?  424 TYR   B CE1 1 
ATOM   6144 C CE2 . TYR   B 2 120 ? 45.589  -33.860 60.126  1.00 141.49 ?  424 TYR   B CE2 1 
ATOM   6145 C CZ  . TYR   B 2 120 ? 46.113  -35.128 59.902  1.00 138.31 ?  424 TYR   B CZ  1 
ATOM   6146 O OH  . TYR   B 2 120 ? 45.306  -36.139 59.409  1.00 132.35 ?  424 TYR   B OH  1 
ATOM   6147 N N   . ARG   B 2 121 ? 50.236  -30.359 63.710  1.00 143.38 ?  425 ARG   B N   1 
ATOM   6148 C CA  . ARG   B 2 121 ? 51.353  -29.443 64.022  1.00 145.70 ?  425 ARG   B CA  1 
ATOM   6149 C C   . ARG   B 2 121 ? 52.695  -29.989 63.579  1.00 142.06 ?  425 ARG   B C   1 
ATOM   6150 O O   . ARG   B 2 121 ? 53.018  -29.925 62.389  1.00 141.12 ?  425 ARG   B O   1 
ATOM   6151 C CB  . ARG   B 2 121 ? 51.435  -29.209 65.527  1.00 147.07 ?  425 ARG   B CB  1 
ATOM   6152 C CG  . ARG   B 2 121 ? 52.457  -28.162 65.943  1.00 144.19 ?  425 ARG   B CG  1 
ATOM   6153 C CD  . ARG   B 2 121 ? 52.113  -27.542 67.283  1.00 153.10 ?  425 ARG   B CD  1 
ATOM   6154 N NE  . ARG   B 2 121 ? 52.708  -28.263 68.398  1.00 158.16 ?  425 ARG   B NE  1 
ATOM   6155 C CZ  . ARG   B 2 121 ? 53.730  -27.818 69.120  1.00 158.51 ?  425 ARG   B CZ  1 
ATOM   6156 N NH1 . ARG   B 2 121 ? 53.871  -26.524 69.339  1.00 159.41 ?  425 ARG   B NH1 1 
ATOM   6157 N NH2 . ARG   B 2 121 ? 54.607  -28.671 69.619  1.00 145.77 ?  425 ARG   B NH2 1 
ATOM   6158 N N   . ARG   B 2 122 ? 53.438  -30.486 64.540  1.00 142.36 ?  426 ARG   B N   1 
ATOM   6159 C CA  . ARG   B 2 122 ? 54.791  -30.992 64.246  1.00 138.62 ?  426 ARG   B CA  1 
ATOM   6160 C C   . ARG   B 2 122 ? 55.023  -31.599 62.866  1.00 142.65 ?  426 ARG   B C   1 
ATOM   6161 O O   . ARG   B 2 122 ? 56.077  -31.368 62.267  1.00 136.75 ?  426 ARG   B O   1 
ATOM   6162 C CB  . ARG   B 2 122 ? 55.027  -32.193 65.152  1.00 144.01 ?  426 ARG   B CB  1 
ATOM   6163 C CG  . ARG   B 2 122 ? 54.122  -33.380 64.849  1.00 145.33 ?  426 ARG   B CG  1 
ATOM   6164 C CD  . ARG   B 2 122 ? 54.288  -34.541 65.809  1.00 147.20 ?  426 ARG   B CD  1 
ATOM   6165 N NE  . ARG   B 2 122 ? 53.443  -35.677 65.467  1.00 147.54 ?  426 ARG   B NE  1 
ATOM   6166 C CZ  . ARG   B 2 122 ? 52.166  -35.794 65.809  1.00 152.44 ?  426 ARG   B CZ  1 
ATOM   6167 N NH1 . ARG   B 2 122 ? 51.839  -36.283 66.991  1.00 148.55 ?  426 ARG   B NH1 1 
ATOM   6168 N NH2 . ARG   B 2 122 ? 51.219  -35.422 64.968  1.00 154.39 ?  426 ARG   B NH2 1 
ATOM   6169 N N   . ARG   B 2 123 ? 54.031  -32.320 62.363  1.00 146.69 ?  427 ARG   B N   1 
ATOM   6170 C CA  . ARG   B 2 123 ? 54.311  -33.042 61.121  1.00 139.66 ?  427 ARG   B CA  1 
ATOM   6171 C C   . ARG   B 2 123 ? 54.285  -32.013 60.004  1.00 135.44 ?  427 ARG   B C   1 
ATOM   6172 O O   . ARG   B 2 123 ? 54.937  -32.204 58.970  1.00 135.04 ?  427 ARG   B O   1 
ATOM   6173 C CB  . ARG   B 2 123 ? 53.337  -34.157 60.753  1.00 136.53 ?  427 ARG   B CB  1 
ATOM   6174 C CG  . ARG   B 2 123 ? 53.159  -35.272 61.750  1.00 138.83 ?  427 ARG   B CG  1 
ATOM   6175 C CD  . ARG   B 2 123 ? 52.317  -36.337 61.098  1.00 134.65 ?  427 ARG   B CD  1 
ATOM   6176 N NE  . ARG   B 2 123 ? 50.920  -36.241 61.500  1.00 130.36 ?  427 ARG   B NE  1 
ATOM   6177 C CZ  . ARG   B 2 123 ? 50.142  -37.288 61.725  1.00 137.83 ?  427 ARG   B CZ  1 
ATOM   6178 N NH1 . ARG   B 2 123 ? 50.580  -38.526 61.545  1.00 134.32 ?  427 ARG   B NH1 1 
ATOM   6179 N NH2 . ARG   B 2 123 ? 48.890  -37.088 62.117  1.00 142.36 ?  427 ARG   B NH2 1 
ATOM   6180 N N   . PHE   B 2 124 ? 53.485  -30.961 60.168  1.00 131.41 ?  428 PHE   B N   1 
ATOM   6181 C CA  . PHE   B 2 124 ? 53.438  -29.852 59.233  1.00 129.65 ?  428 PHE   B CA  1 
ATOM   6182 C C   . PHE   B 2 124 ? 54.143  -28.613 59.769  1.00 127.85 ?  428 PHE   B C   1 
ATOM   6183 O O   . PHE   B 2 124 ? 53.892  -27.510 59.280  1.00 122.04 ?  428 PHE   B O   1 
ATOM   6184 C CB  . PHE   B 2 124 ? 51.989  -29.544 58.862  1.00 125.30 ?  428 PHE   B CB  1 
ATOM   6185 C CG  . PHE   B 2 124 ? 51.378  -30.570 57.954  1.00 123.19 ?  428 PHE   B CG  1 
ATOM   6186 C CD1 . PHE   B 2 124 ? 52.187  -31.503 57.303  1.00 119.22 ?  428 PHE   B CD1 1 
ATOM   6187 C CD2 . PHE   B 2 124 ? 50.008  -30.595 57.728  1.00 123.03 ?  428 PHE   B CD2 1 
ATOM   6188 C CE1 . PHE   B 2 124 ? 51.643  -32.446 56.449  1.00 117.67 ?  428 PHE   B CE1 1 
ATOM   6189 C CE2 . PHE   B 2 124 ? 49.446  -31.536 56.872  1.00 121.13 ?  428 PHE   B CE2 1 
ATOM   6190 C CZ  . PHE   B 2 124 ? 50.263  -32.465 56.233  1.00 119.65 ?  428 PHE   B CZ  1 
ATOM   6191 N N   . ASN   B 2 125 ? 55.030  -28.785 60.752  1.00 128.41 ?  429 ASN   B N   1 
ATOM   6192 C CA  . ASN   B 2 125 ? 55.846  -27.712 61.303  1.00 127.97 ?  429 ASN   B CA  1 
ATOM   6193 C C   . ASN   B 2 125 ? 55.032  -26.438 61.487  1.00 134.70 ?  429 ASN   B C   1 
ATOM   6194 O O   . ASN   B 2 125 ? 55.537  -25.336 61.241  1.00 137.19 ?  429 ASN   B O   1 
ATOM   6195 C CB  . ASN   B 2 125 ? 57.064  -27.471 60.407  1.00 122.49 ?  429 ASN   B CB  1 
ATOM   6196 C CG  . ASN   B 2 125 ? 57.993  -28.675 60.354  1.00 124.90 ?  429 ASN   B CG  1 
ATOM   6197 O OD1 . ASN   B 2 125 ? 57.549  -29.801 60.130  1.00 130.92 ?  429 ASN   B OD1 1 
ATOM   6198 N ND2 . ASN   B 2 125 ? 59.290  -28.441 60.539  1.00 119.56 ?  429 ASN   B ND2 1 
ATOM   6199 N N   . ILE   B 2 126 ? 53.771  -26.583 61.920  1.00 133.26 ?  430 ILE   B N   1 
ATOM   6200 C CA  . ILE   B 2 126 ? 52.822  -25.475 61.991  1.00 130.56 ?  430 ILE   B CA  1 
ATOM   6201 C C   . ILE   B 2 126 ? 53.393  -24.362 62.858  1.00 135.24 ?  430 ILE   B C   1 
ATOM   6202 O O   . ILE   B 2 126 ? 52.969  -23.206 62.758  1.00 136.56 ?  430 ILE   B O   1 
ATOM   6203 C CB  . ILE   B 2 126 ? 51.444  -25.939 62.498  1.00 124.72 ?  430 ILE   B CB  1 
ATOM   6204 C CG1 . ILE   B 2 126 ? 50.896  -27.044 61.613  1.00 129.07 ?  430 ILE   B CG1 1 
ATOM   6205 C CG2 . ILE   B 2 126 ? 50.432  -24.812 62.477  1.00 123.88 ?  430 ILE   B CG2 1 
ATOM   6206 C CD1 . ILE   B 2 126 ? 49.472  -27.420 61.959  1.00 137.25 ?  430 ILE   B CD1 1 
ATOM   6207 N N   . ASP   B 2 127 ? 54.380  -24.691 63.692  1.00 139.43 ?  431 ASP   B N   1 
ATOM   6208 C CA  . ASP   B 2 127 ? 55.115  -23.653 64.410  1.00 143.90 ?  431 ASP   B CA  1 
ATOM   6209 C C   . ASP   B 2 127 ? 55.915  -22.773 63.446  1.00 142.38 ?  431 ASP   B C   1 
ATOM   6210 O O   . ASP   B 2 127 ? 55.670  -21.559 63.344  1.00 135.32 ?  431 ASP   B O   1 
ATOM   6211 C CB  . ASP   B 2 127 ? 56.022  -24.289 65.476  1.00 151.12 ?  431 ASP   B CB  1 
ATOM   6212 C CG  . ASP   B 2 127 ? 55.239  -24.854 66.679  1.00 157.19 ?  431 ASP   B CG  1 
ATOM   6213 O OD1 . ASP   B 2 127 ? 53.991  -24.926 66.620  1.00 159.35 ?  431 ASP   B OD1 1 
ATOM   6214 O OD2 . ASP   B 2 127 ? 55.879  -25.217 67.697  1.00 155.80 ?  431 ASP   B OD2 1 
ATOM   6215 N N   . GLU   B 2 128 ? 56.882  -23.370 62.731  1.00 141.07 ?  432 GLU   B N   1 
ATOM   6216 C CA  . GLU   B 2 128 ? 57.686  -22.616 61.769  1.00 136.00 ?  432 GLU   B CA  1 
ATOM   6217 C C   . GLU   B 2 128 ? 56.802  -21.833 60.827  1.00 137.06 ?  432 GLU   B C   1 
ATOM   6218 O O   . GLU   B 2 128 ? 57.028  -20.643 60.578  1.00 139.95 ?  432 GLU   B O   1 
ATOM   6219 C CB  . GLU   B 2 128 ? 58.565  -23.550 60.951  1.00 127.20 ?  432 GLU   B CB  1 
ATOM   6220 C CG  . GLU   B 2 128 ? 59.771  -24.045 61.652  1.00 130.70 ?  432 GLU   B CG  1 
ATOM   6221 C CD  . GLU   B 2 128 ? 60.268  -25.336 61.038  1.00 135.41 ?  432 GLU   B CD  1 
ATOM   6222 O OE1 . GLU   B 2 128 ? 60.744  -25.297 59.877  1.00 129.99 ?  432 GLU   B OE1 1 
ATOM   6223 O OE2 . GLU   B 2 128 ? 60.164  -26.394 61.711  1.00 140.18 ?  432 GLU   B OE2 1 
ATOM   6224 N N   . VAL   B 2 129 ? 55.783  -22.501 60.289  1.00 131.20 ?  433 VAL   B N   1 
ATOM   6225 C CA  . VAL   B 2 129 ? 54.895  -21.852 59.336  1.00 135.64 ?  433 VAL   B CA  1 
ATOM   6226 C C   . VAL   B 2 129 ? 54.260  -20.622 59.960  1.00 139.37 ?  433 VAL   B C   1 
ATOM   6227 O O   . VAL   B 2 129 ? 54.216  -19.544 59.353  1.00 138.09 ?  433 VAL   B O   1 
ATOM   6228 C CB  . VAL   B 2 129 ? 53.832  -22.839 58.842  1.00 129.41 ?  433 VAL   B CB  1 
ATOM   6229 C CG1 . VAL   B 2 129 ? 52.823  -22.102 57.982  1.00 128.64 ?  433 VAL   B CG1 1 
ATOM   6230 C CG2 . VAL   B 2 129 ? 54.506  -23.974 58.070  1.00 131.08 ?  433 VAL   B CG2 1 
ATOM   6231 N N   . LEU   B 2 130 ? 53.788  -20.759 61.200  1.00 139.15 ?  434 LEU   B N   1 
ATOM   6232 C CA  . LEU   B 2 130 ? 53.092  -19.656 61.848  1.00 137.41 ?  434 LEU   B CA  1 
ATOM   6233 C C   . LEU   B 2 130 ? 54.029  -18.501 62.146  1.00 144.14 ?  434 LEU   B C   1 
ATOM   6234 O O   . LEU   B 2 130 ? 53.674  -17.337 61.908  1.00 146.52 ?  434 LEU   B O   1 
ATOM   6235 C CB  . LEU   B 2 130 ? 52.405  -20.140 63.117  1.00 131.96 ?  434 LEU   B CB  1 
ATOM   6236 C CG  . LEU   B 2 130 ? 50.976  -20.566 62.796  1.00 132.30 ?  434 LEU   B CG  1 
ATOM   6237 C CD1 . LEU   B 2 130 ? 50.399  -21.503 63.831  1.00 124.94 ?  434 LEU   B CD1 1 
ATOM   6238 C CD2 . LEU   B 2 130 ? 50.125  -19.311 62.655  1.00 132.42 ?  434 LEU   B CD2 1 
ATOM   6239 N N   . GLN   B 2 131 ? 55.232  -18.792 62.652  1.00 143.36 ?  435 GLN   B N   1 
ATOM   6240 C CA  . GLN   B 2 131 ? 56.139  -17.702 63.000  1.00 150.38 ?  435 GLN   B CA  1 
ATOM   6241 C C   . GLN   B 2 131 ? 56.508  -16.872 61.773  1.00 149.24 ?  435 GLN   B C   1 
ATOM   6242 O O   . GLN   B 2 131 ? 56.758  -15.665 61.890  1.00 147.67 ?  435 GLN   B O   1 
ATOM   6243 C CB  . GLN   B 2 131 ? 57.397  -18.242 63.680  1.00 147.29 ?  435 GLN   B CB  1 
ATOM   6244 C CG  . GLN   B 2 131 ? 58.549  -18.515 62.741  1.00 146.81 ?  435 GLN   B CG  1 
ATOM   6245 C CD  . GLN   B 2 131 ? 59.474  -19.567 63.287  1.00 151.18 ?  435 GLN   B CD  1 
ATOM   6246 O OE1 . GLN   B 2 131 ? 59.193  -20.177 64.320  1.00 147.28 ?  435 GLN   B OE1 1 
ATOM   6247 N NE2 . GLN   B 2 131 ? 60.588  -19.790 62.601  1.00 156.00 ?  435 GLN   B NE2 1 
ATOM   6248 N N   . GLU   B 2 132 ? 56.515  -17.487 60.588  1.00 146.40 ?  436 GLU   B N   1 
ATOM   6249 C CA  . GLU   B 2 132 ? 56.849  -16.723 59.398  1.00 144.60 ?  436 GLU   B CA  1 
ATOM   6250 C C   . GLU   B 2 132 ? 55.682  -15.893 58.902  1.00 145.21 ?  436 GLU   B C   1 
ATOM   6251 O O   . GLU   B 2 132 ? 55.900  -14.848 58.278  1.00 145.98 ?  436 GLU   B O   1 
ATOM   6252 C CB  . GLU   B 2 132 ? 57.337  -17.639 58.295  1.00 135.92 ?  436 GLU   B CB  1 
ATOM   6253 C CG  . GLU   B 2 132 ? 58.813  -17.764 58.361  1.00 141.65 ?  436 GLU   B CG  1 
ATOM   6254 C CD  . GLU   B 2 132 ? 59.372  -18.355 57.119  1.00 137.61 ?  436 GLU   B CD  1 
ATOM   6255 O OE1 . GLU   B 2 132 ? 58.646  -19.118 56.452  1.00 138.35 ?  436 GLU   B OE1 1 
ATOM   6256 O OE2 . GLU   B 2 132 ? 60.538  -18.050 56.811  1.00 134.09 ?  436 GLU   B OE2 1 
ATOM   6257 N N   . TRP   B 2 133 ? 54.447  -16.336 59.155  1.00 144.70 ?  437 TRP   B N   1 
ATOM   6258 C CA  . TRP   B 2 133 ? 53.314  -15.461 58.893  1.00 144.05 ?  437 TRP   B CA  1 
ATOM   6259 C C   . TRP   B 2 133 ? 53.429  -14.173 59.689  1.00 149.77 ?  437 TRP   B C   1 
ATOM   6260 O O   . TRP   B 2 133 ? 52.985  -13.112 59.223  1.00 150.84 ?  437 TRP   B O   1 
ATOM   6261 C CB  . TRP   B 2 133 ? 51.993  -16.149 59.222  1.00 140.83 ?  437 TRP   B CB  1 
ATOM   6262 C CG  . TRP   B 2 133 ? 50.847  -15.185 59.118  1.00 145.78 ?  437 TRP   B CG  1 
ATOM   6263 C CD1 . TRP   B 2 133 ? 50.324  -14.654 57.970  1.00 147.04 ?  437 TRP   B CD1 1 
ATOM   6264 C CD2 . TRP   B 2 133 ? 50.103  -14.603 60.199  1.00 148.70 ?  437 TRP   B CD2 1 
ATOM   6265 N NE1 . TRP   B 2 133 ? 49.293  -13.788 58.269  1.00 148.52 ?  437 TRP   B NE1 1 
ATOM   6266 C CE2 . TRP   B 2 133 ? 49.133  -13.745 59.629  1.00 146.17 ?  437 TRP   B CE2 1 
ATOM   6267 C CE3 . TRP   B 2 133 ? 50.152  -14.736 61.592  1.00 150.94 ?  437 TRP   B CE3 1 
ATOM   6268 C CZ2 . TRP   B 2 133 ? 48.222  -13.027 60.401  1.00 144.82 ?  437 TRP   B CZ2 1 
ATOM   6269 C CZ3 . TRP   B 2 133 ? 49.242  -14.020 62.360  1.00 150.58 ?  437 TRP   B CZ3 1 
ATOM   6270 C CH2 . TRP   B 2 133 ? 48.291  -13.177 61.760  1.00 147.10 ?  437 TRP   B CH2 1 
ATOM   6271 N N   . GLU   B 2 134 ? 54.032  -14.246 60.882  1.00 148.89 ?  438 GLU   B N   1 
ATOM   6272 C CA  . GLU   B 2 134 ? 54.238  -13.044 61.683  1.00 155.85 ?  438 GLU   B CA  1 
ATOM   6273 C C   . GLU   B 2 134 ? 55.326  -12.136 61.094  1.00 154.39 ?  438 GLU   B C   1 
ATOM   6274 O O   . GLU   B 2 134 ? 55.242  -10.904 61.227  1.00 150.30 ?  438 GLU   B O   1 
ATOM   6275 C CB  . GLU   B 2 134 ? 54.538  -13.428 63.140  1.00 155.36 ?  438 GLU   B CB  1 
ATOM   6276 C CG  . GLU   B 2 134 ? 53.272  -13.570 64.014  1.00 156.38 ?  438 GLU   B CG  1 
ATOM   6277 C CD  . GLU   B 2 134 ? 53.387  -14.613 65.122  1.00 160.05 ?  438 GLU   B CD  1 
ATOM   6278 O OE1 . GLU   B 2 134 ? 54.440  -15.290 65.219  1.00 158.87 ?  438 GLU   B OE1 1 
ATOM   6279 O OE2 . GLU   B 2 134 ? 52.412  -14.747 65.902  1.00 157.55 ?  438 GLU   B OE2 1 
ATOM   6280 N N   . ALA   B 2 135 ? 56.281  -12.720 60.391  1.00 147.05 ?  439 ALA   B N   1 
ATOM   6281 C CA  . ALA   B 2 135 ? 57.259  -11.837 59.732  1.00 144.58 ?  439 ALA   B CA  1 
ATOM   6282 C C   . ALA   B 2 135 ? 56.201  -11.539 58.675  1.00 149.76 ?  439 ALA   B C   1 
ATOM   6283 O O   . ALA   B 2 135 ? 55.934  -12.413 57.849  1.00 148.82 ?  439 ALA   B O   1 
ATOM   6284 C CB  . ALA   B 2 135 ? 58.388  -12.661 59.210  1.00 137.74 ?  439 ALA   B CB  1 
ATOM   6285 N N   . GLU   B 2 136 ? 55.627  -10.343 58.710  1.00 150.84 ?  440 GLU   B N   1 
ATOM   6286 C CA  . GLU   B 2 136 ? 54.524  -10.017 57.778  1.00 145.77 ?  440 GLU   B CA  1 
ATOM   6287 C C   . GLU   B 2 136 ? 53.198  -9.541  58.365  1.00 143.36 ?  440 GLU   B C   1 
ATOM   6288 O O   . GLU   B 2 136 ? 52.189  -10.205 58.073  1.00 142.20 ?  440 GLU   B O   1 
ATOM   6289 C CB  . GLU   B 2 136 ? 54.223  -11.055 56.705  1.00 148.45 ?  440 GLU   B CB  1 
ATOM   6290 C CG  . GLU   B 2 136 ? 54.818  -10.755 55.342  1.00 148.41 ?  440 GLU   B CG  1 
ATOM   6291 C CD  . GLU   B 2 136 ? 54.310  -11.669 54.239  1.00 140.28 ?  440 GLU   B CD  1 
ATOM   6292 O OE1 . GLU   B 2 136 ? 53.104  -11.614 53.938  1.00 140.62 ?  440 GLU   B OE1 1 
ATOM   6293 O OE2 . GLU   B 2 136 ? 55.117  -12.439 53.688  1.00 127.99 ?  440 GLU   B OE2 1 
HETATM 6294 C C4  . A1H8N C 3 .   ? -6.922  60.367  82.740  1.00 97.64  ?  901 A1H8N A C4  1 
HETATM 6295 C C14 . A1H8N C 3 .   ? -5.810  52.007  83.424  1.00 135.79 ?  901 A1H8N A C14 1 
HETATM 6296 C C5  . A1H8N C 3 .   ? -7.396  59.609  81.642  1.00 102.69 ?  901 A1H8N A C5  1 
HETATM 6297 C C6  . A1H8N C 3 .   ? -7.330  60.150  80.347  1.00 100.80 ?  901 A1H8N A C6  1 
HETATM 6298 C C11 . A1H8N C 3 .   ? -7.633  54.685  81.426  1.00 129.31 ?  901 A1H8N A C11 1 
HETATM 6299 C C7  . A1H8N C 3 .   ? -6.879  61.427  80.159  1.00 98.51  ?  901 A1H8N A C7  1 
HETATM 6300 C C8  . A1H8N C 3 .   ? -6.840  62.024  78.774  1.00 93.75  ?  901 A1H8N A C8  1 
HETATM 6301 C C9  . A1H8N C 3 .   ? -7.789  57.234  80.916  1.00 109.42 ?  901 A1H8N A C9  1 
HETATM 6302 C C10 . A1H8N C 3 .   ? -6.935  56.049  81.286  1.00 113.50 ?  901 A1H8N A C10 1 
HETATM 6303 C C12 . A1H8N C 3 .   ? -6.691  53.991  82.373  1.00 135.41 ?  901 A1H8N A C12 1 
HETATM 6304 C C13 . A1H8N C 3 .   ? -6.704  52.607  82.552  1.00 134.48 ?  901 A1H8N A C13 1 
HETATM 6305 N N1  . A1H8N C 3 .   ? -7.833  58.255  81.866  1.00 102.94 ?  901 A1H8N A N1  1 
HETATM 6306 N N2  . A1H8N C 3 .   ? -3.899  52.223  84.948  1.00 146.85 ?  901 A1H8N A N2  1 
HETATM 6307 C C3  . A1H8N C 3 .   ? -6.460  61.664  82.514  1.00 92.88  ?  901 A1H8N A C3  1 
HETATM 6308 N N3  . A1H8N C 3 .   ? 0.134   49.758  85.013  1.00 134.54 ?  901 A1H8N A N3  1 
HETATM 6309 C C1  . A1H8N C 3 .   ? -5.917  63.585  81.001  1.00 87.38  ?  901 A1H8N A C1  1 
HETATM 6310 C C15 . A1H8N C 3 .   ? -4.866  52.791  84.097  1.00 142.54 ?  901 A1H8N A C15 1 
HETATM 6311 C C16 . A1H8N C 3 .   ? -2.721  52.775  85.359  1.00 145.09 ?  901 A1H8N A C16 1 
HETATM 6312 C C17 . A1H8N C 3 .   ? -1.811  51.744  85.486  1.00 142.25 ?  901 A1H8N A C17 1 
HETATM 6313 C C18 . A1H8N C 3 .   ? -0.495  51.991  85.849  1.00 133.73 ?  901 A1H8N A C18 1 
HETATM 6314 C C19 . A1H8N C 3 .   ? 0.392   50.773  85.869  1.00 133.02 ?  901 A1H8N A C19 1 
HETATM 6315 C C2  . A1H8N C 3 .   ? -6.433  62.188  81.248  1.00 95.14  ?  901 A1H8N A C2  1 
HETATM 6316 C C20 . A1H8N C 3 .   ? -0.336  49.943  83.637  1.00 132.88 ?  901 A1H8N A C20 1 
HETATM 6317 C C21 . A1H8N C 3 .   ? -1.100  48.964  82.728  1.00 137.43 ?  901 A1H8N A C21 1 
HETATM 6318 C C22 . A1H8N C 3 .   ? -0.331  47.694  82.389  1.00 136.48 ?  901 A1H8N A C22 1 
HETATM 6319 C C23 . A1H8N C 3 .   ? -0.912  46.188  84.193  1.00 146.78 ?  901 A1H8N A C23 1 
HETATM 6320 C C24 . A1H8N C 3 .   ? 0.493   45.865  84.654  1.00 140.80 ?  901 A1H8N A C24 1 
HETATM 6321 C C25 . A1H8N C 3 .   ? 0.922   44.580  83.988  1.00 146.58 ?  901 A1H8N A C25 1 
HETATM 6322 C C26 . A1H8N C 3 .   ? 1.772   43.652  84.619  1.00 139.60 ?  901 A1H8N A C26 1 
HETATM 6323 C C27 . A1H8N C 3 .   ? 2.129   42.480  83.984  1.00 135.96 ?  901 A1H8N A C27 1 
HETATM 6324 C C28 . A1H8N C 3 .   ? 1.642   42.210  82.716  1.00 138.36 ?  901 A1H8N A C28 1 
HETATM 6325 C C29 . A1H8N C 3 .   ? 0.800   43.109  82.084  1.00 141.42 ?  901 A1H8N A C29 1 
HETATM 6326 C C30 . A1H8N C 3 .   ? 0.420   44.304  82.715  1.00 147.24 ?  901 A1H8N A C30 1 
HETATM 6327 C C31 . A1H8N C 3 .   ? -0.506  45.249  81.974  1.00 138.43 ?  901 A1H8N A C31 1 
HETATM 6328 C C32 . A1H8N C 3 .   ? -0.133  53.306  86.109  1.00 124.28 ?  901 A1H8N A C32 1 
HETATM 6329 C C33 . A1H8N C 3 .   ? -1.109  54.284  85.981  1.00 123.43 ?  901 A1H8N A C33 1 
HETATM 6330 C C34 . A1H8N C 3 .   ? -4.835  54.169  83.905  1.00 128.56 ?  901 A1H8N A C34 1 
HETATM 6331 C C35 . A1H8N C 3 .   ? -5.746  54.756  83.054  1.00 124.55 ?  901 A1H8N A C35 1 
HETATM 6332 C C36 . A1H8N C 3 .   ? -8.312  57.967  83.185  1.00 99.05  ?  901 A1H8N A C36 1 
HETATM 6333 C C37 . A1H8N C 3 .   ? -7.840  58.722  84.286  1.00 102.04 ?  901 A1H8N A C37 1 
HETATM 6334 C C38 . A1H8N C 3 .   ? -9.221  57.392  85.796  1.00 97.96  ?  901 A1H8N A C38 1 
HETATM 6335 C C39 . A1H8N C 3 .   ? -9.250  56.919  83.413  1.00 98.53  ?  901 A1H8N A C39 1 
HETATM 6336 C C40 . A1H8N C 3 .   ? -6.236  60.422  85.157  1.00 94.94  ?  901 A1H8N A C40 1 
HETATM 6337 C C41 . A1H8N C 3 .   ? -6.766  61.770  85.633  1.00 93.39  ?  901 A1H8N A C41 1 
HETATM 6338 C C42 . A1H8N C 3 .   ? -6.403  62.127  87.079  1.00 89.09  ?  901 A1H8N A C42 1 
HETATM 6339 C C43 . A1H8N C 3 .   ? -7.006  63.443  87.573  1.00 89.02  ?  901 A1H8N A C43 1 
HETATM 6340 C C44 . A1H8N C 3 .   ? -6.446  63.874  88.916  1.00 90.51  ?  901 A1H8N A C44 1 
HETATM 6341 C C45 . A1H8N C 3 .   ? -6.454  70.278  89.758  1.00 89.76  ?  901 A1H8N A C45 1 
HETATM 6342 C C46 . A1H8N C 3 .   ? -6.399  71.466  88.822  1.00 87.62  ?  901 A1H8N A C46 1 
HETATM 6343 C C47 . A1H8N C 3 .   ? -5.545  73.278  88.141  1.00 85.21  ?  901 A1H8N A C47 1 
HETATM 6344 C C48 . A1H8N C 3 .   ? -3.398  74.428  87.690  1.00 85.20  ?  901 A1H8N A C48 1 
HETATM 6345 C C49 . A1H8N C 3 .   ? -3.610  76.319  88.615  1.00 84.70  ?  901 A1H8N A C49 1 
HETATM 6346 C C50 . A1H8N C 3 .   ? -3.470  77.608  89.137  1.00 81.44  ?  901 A1H8N A C50 1 
HETATM 6347 C C51 . A1H8N C 3 .   ? -5.610  77.352  89.990  1.00 82.04  ?  901 A1H8N A C51 1 
HETATM 6348 C C52 . A1H8N C 3 .   ? -4.794  75.649  88.863  1.00 84.85  ?  901 A1H8N A C52 1 
HETATM 6349 C C53 . A1H8N C 3 .   ? -7.031  73.509  87.892  1.00 83.90  ?  901 A1H8N A C53 1 
HETATM 6350 C C54 . A1H8N C 3 .   ? -7.644  72.341  88.667  1.00 83.86  ?  901 A1H8N A C54 1 
HETATM 6351 N N10 . A1H8N C 3 .   ? -2.736  75.545  87.871  1.00 88.18  ?  901 A1H8N A N10 1 
HETATM 6352 N N11 . A1H8N C 3 .   ? -2.369  78.333  88.968  1.00 82.16  ?  901 A1H8N A N11 1 
HETATM 6353 N N12 . A1H8N C 3 .   ? -4.515  78.111  89.838  1.00 82.25  ?  901 A1H8N A N12 1 
HETATM 6354 N N13 . A1H8N C 3 .   ? -5.853  76.124  89.543  1.00 80.68  ?  901 A1H8N A N13 1 
HETATM 6355 N N4  . A1H8N C 3 .   ? -0.989  46.421  82.743  1.00 145.79 ?  901 A1H8N A N4  1 
HETATM 6356 N N5  . A1H8N C 3 .   ? -2.386  54.055  85.616  1.00 126.66 ?  901 A1H8N A N5  1 
HETATM 6357 N N6  . A1H8N C 3 .   ? -8.299  58.428  85.534  1.00 100.61 ?  901 A1H8N A N6  1 
HETATM 6358 N N7  . A1H8N C 3 .   ? -9.649  56.687  84.710  1.00 101.23 ?  901 A1H8N A N7  1 
HETATM 6359 N N8  . A1H8N C 3 .   ? -6.975  59.809  84.048  1.00 99.47  ?  901 A1H8N A N8  1 
HETATM 6360 N N9  . A1H8N C 3 .   ? -4.645  74.423  88.260  1.00 84.95  ?  901 A1H8N A N9  1 
HETATM 6361 O O1  . A1H8N C 3 .   ? -8.267  57.354  79.795  1.00 113.17 ?  901 A1H8N A O1  1 
HETATM 6362 O O10 . A1H8N C 3 .   ? -5.137  65.551  91.034  1.00 79.54  ?  901 A1H8N A O10 1 
HETATM 6363 O O11 . A1H8N C 3 .   ? -7.505  66.433  91.335  1.00 90.25  -1 901 A1H8N A O11 1 
HETATM 6364 O O12 . A1H8N C 3 .   ? -5.924  67.143  89.363  1.00 81.67  ?  901 A1H8N A O12 1 
HETATM 6365 O O13 . A1H8N C 3 .   ? -5.873  68.632  87.304  1.00 79.30  ?  901 A1H8N A O13 1 
HETATM 6366 O O14 . A1H8N C 3 .   ? -7.919  67.173  87.988  1.00 84.29  -1 901 A1H8N A O14 1 
HETATM 6367 O O15 . A1H8N C 3 .   ? -7.342  69.230  89.242  1.00 93.45  ?  901 A1H8N A O15 1 
HETATM 6368 O O16 . A1H8N C 3 .   ? -5.448  72.444  89.291  1.00 84.18  ?  901 A1H8N A O16 1 
HETATM 6369 O O17 . A1H8N C 3 .   ? -7.201  73.332  86.504  1.00 80.82  ?  901 A1H8N A O17 1 
HETATM 6370 O O18 . A1H8N C 3 .   ? -8.757  71.833  87.945  1.00 87.04  ?  901 A1H8N A O18 1 
HETATM 6371 O O2  . A1H8N C 3 .   ? 1.333   50.721  86.658  1.00 134.11 ?  901 A1H8N A O2  1 
HETATM 6372 O O3  . A1H8N C 3 .   ? -2.438  48.686  83.143  1.00 140.65 ?  901 A1H8N A O3  1 
HETATM 6373 O O4  . A1H8N C 3 .   ? -9.627  57.125  86.913  1.00 89.07  ?  901 A1H8N A O4  1 
HETATM 6374 O O5  . A1H8N C 3 .   ? -9.719  56.256  82.537  1.00 106.83 ?  901 A1H8N A O5  1 
HETATM 6375 O O6  . A1H8N C 3 .   ? -8.181  61.739  85.448  1.00 94.21  ?  901 A1H8N A O6  1 
HETATM 6376 O O7  . A1H8N C 3 .   ? -6.882  61.079  87.916  1.00 87.28  ?  901 A1H8N A O7  1 
HETATM 6377 O O8  . A1H8N C 3 .   ? -8.434  63.403  87.665  1.00 90.17  ?  901 A1H8N A O8  1 
HETATM 6378 O O9  . A1H8N C 3 .   ? -7.169  65.008  89.461  1.00 89.91  ?  901 A1H8N A O9  1 
HETATM 6379 P P1  . A1H8N C 3 .   ? -6.405  66.027  90.422  1.00 88.88  ?  901 A1H8N A P1  1 
HETATM 6380 P P2  . A1H8N C 3 .   ? -6.760  68.038  88.341  1.00 82.65  ?  901 A1H8N A P2  1 
# 
